data_8JE5
# 
_entry.id   8JE5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8JE5         pdb_00008je5 10.2210/pdb8je5/pdb 
WWPDB D_1300037706 ?            ?                   
# 
_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       2024-11-27 
# 
_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                        8JE5 
_pdbx_database_status.recvd_initial_deposition_date   2023-05-15 
_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                 3 
_pdbx_contact_author.email              amit.icgeb@gmail.com 
_pdbx_contact_author.name_first         Amit 
_pdbx_contact_author.name_last          Sharma 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3305-0034 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Goswami, R.'       1 ?                   
'Manickam, Y.'      2 0000-0002-2119-062X 
'Chhibber-Goel, J.' 3 0000-0003-4654-5463 
'Harlos, K.'        4 ?                   
'Sharma, A.'        5 0000-0002-3305-0034 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Targeting Prolyl-tRNA synthetase of Anopheles culicifacies for the development of new larvicide' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Goswami, R.'       1 ?                   
primary 'Chhibber-Goel, J.' 2 0000-0003-4654-5463 
primary 'Manickam, Y.'      3 0000-0002-2119-062X 
primary 'Gupta, S.'         4 ?                   
primary 'Harlos, K.'        5 ?                   
primary 'Laleu, B.'         6 ?                   
primary 'Sharma, A.'        7 0000-0002-3305-0034 
# 
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 'PROLYL-TRNA SYNTHETASE'                                                                   58101.004 2  ? ? ? ? 
2 non-polymer syn '7-bromo-6-chloro-3-{3-[(2R,3S)-3-hydroxypiperidin-2-yl]-2-oxopropyl}quinazolin-4(3H)-one' 414.681   2  ? ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                                 65.409    2  ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                                             35.453    3  ? ? ? ? 
5 non-polymer syn GLYCEROL                                                                                   92.094    3  ? ? ? ? 
6 water       nat water                                                                                      18.015    16 ? ? ? ? 
# 
_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       
;MTRLGLEATKEDNLPDWYSQVITKGEMIEYYDVSGCYILRHWSFAIWKAIRNWFDAEITRLGVKECYFPIFVSRAALERE
KTHIADFAPEVAWVTKSGDSELAEPIAVRPTSETVMYPAYAKWIQSYRDLPIRLNQWNNVVRWEFKHPQPFLRTREFLWQ
EGHTAFATQKEADEEVLTILDLYAKVYTDLLAIPVVKGRKTEKEKFAGGDYTTTVEAYISASGRAIQGATSHHLGQNFSR
MFDIVYEHPETKEKEYVFQNSWGITTRTIGVMIMVHADNQGLVLPPRVACIQVVIVPCGITATTTDDERRRLYESCRELE
QTFVKAGIRCEGDYRDNYSPGWKYNHWELKGVPVRIELGFKDLQNDQFVAVRRDNGAKQTIKRAQATVEMPKLLETIHTS
MYERAERDLQSHTKLTKQWAEFLQFLETKNIIMAPFCGEISCEDRIKAESARDDAEAEAGAPAMGAKSLCIPFEQPAKID
PKVDKCVHPACGRVAKFYTLFGRSY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTRLGLEATKEDNLPDWYSQVITKGEMIEYYDVSGCYILRHWSFAIWKAIRNWFDAEITRLGVKECYFPIFVSRAALERE
KTHIADFAPEVAWVTKSGDSELAEPIAVRPTSETVMYPAYAKWIQSYRDLPIRLNQWNNVVRWEFKHPQPFLRTREFLWQ
EGHTAFATQKEADEEVLTILDLYAKVYTDLLAIPVVKGRKTEKEKFAGGDYTTTVEAYISASGRAIQGATSHHLGQNFSR
MFDIVYEHPETKEKEYVFQNSWGITTRTIGVMIMVHADNQGLVLPPRVACIQVVIVPCGITATTTDDERRRLYESCRELE
QTFVKAGIRCEGDYRDNYSPGWKYNHWELKGVPVRIELGFKDLQNDQFVAVRRDNGAKQTIKRAQATVEMPKLLETIHTS
MYERAERDLQSHTKLTKQWAEFLQFLETKNIIMAPFCGEISCEDRIKAESARDDAEAEAGAPAMGAKSLCIPFEQPAKID
PKVDKCVHPACGRVAKFYTLFGRSY
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '7-bromo-6-chloro-3-{3-[(2R,3S)-3-hydroxypiperidin-2-yl]-2-oxopropyl}quinazolin-4(3H)-one' HFG 
3 'ZINC ION'                                                                                 ZN  
4 'CHLORIDE ION'                                                                             CL  
5 GLYCEROL                                                                                   GOL 
6 water                                                                                      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   THR n 
1 3   ARG n 
1 4   LEU n 
1 5   GLY n 
1 6   LEU n 
1 7   GLU n 
1 8   ALA n 
1 9   THR n 
1 10  LYS n 
1 11  GLU n 
1 12  ASP n 
1 13  ASN n 
1 14  LEU n 
1 15  PRO n 
1 16  ASP n 
1 17  TRP n 
1 18  TYR n 
1 19  SER n 
1 20  GLN n 
1 21  VAL n 
1 22  ILE n 
1 23  THR n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  MET n 
1 28  ILE n 
1 29  GLU n 
1 30  TYR n 
1 31  TYR n 
1 32  ASP n 
1 33  VAL n 
1 34  SER n 
1 35  GLY n 
1 36  CYS n 
1 37  TYR n 
1 38  ILE n 
1 39  LEU n 
1 40  ARG n 
1 41  HIS n 
1 42  TRP n 
1 43  SER n 
1 44  PHE n 
1 45  ALA n 
1 46  ILE n 
1 47  TRP n 
1 48  LYS n 
1 49  ALA n 
1 50  ILE n 
1 51  ARG n 
1 52  ASN n 
1 53  TRP n 
1 54  PHE n 
1 55  ASP n 
1 56  ALA n 
1 57  GLU n 
1 58  ILE n 
1 59  THR n 
1 60  ARG n 
1 61  LEU n 
1 62  GLY n 
1 63  VAL n 
1 64  LYS n 
1 65  GLU n 
1 66  CYS n 
1 67  TYR n 
1 68  PHE n 
1 69  PRO n 
1 70  ILE n 
1 71  PHE n 
1 72  VAL n 
1 73  SER n 
1 74  ARG n 
1 75  ALA n 
1 76  ALA n 
1 77  LEU n 
1 78  GLU n 
1 79  ARG n 
1 80  GLU n 
1 81  LYS n 
1 82  THR n 
1 83  HIS n 
1 84  ILE n 
1 85  ALA n 
1 86  ASP n 
1 87  PHE n 
1 88  ALA n 
1 89  PRO n 
1 90  GLU n 
1 91  VAL n 
1 92  ALA n 
1 93  TRP n 
1 94  VAL n 
1 95  THR n 
1 96  LYS n 
1 97  SER n 
1 98  GLY n 
1 99  ASP n 
1 100 SER n 
1 101 GLU n 
1 102 LEU n 
1 103 ALA n 
1 104 GLU n 
1 105 PRO n 
1 106 ILE n 
1 107 ALA n 
1 108 VAL n 
1 109 ARG n 
1 110 PRO n 
1 111 THR n 
1 112 SER n 
1 113 GLU n 
1 114 THR n 
1 115 VAL n 
1 116 MET n 
1 117 TYR n 
1 118 PRO n 
1 119 ALA n 
1 120 TYR n 
1 121 ALA n 
1 122 LYS n 
1 123 TRP n 
1 124 ILE n 
1 125 GLN n 
1 126 SER n 
1 127 TYR n 
1 128 ARG n 
1 129 ASP n 
1 130 LEU n 
1 131 PRO n 
1 132 ILE n 
1 133 ARG n 
1 134 LEU n 
1 135 ASN n 
1 136 GLN n 
1 137 TRP n 
1 138 ASN n 
1 139 ASN n 
1 140 VAL n 
1 141 VAL n 
1 142 ARG n 
1 143 TRP n 
1 144 GLU n 
1 145 PHE n 
1 146 LYS n 
1 147 HIS n 
1 148 PRO n 
1 149 GLN n 
1 150 PRO n 
1 151 PHE n 
1 152 LEU n 
1 153 ARG n 
1 154 THR n 
1 155 ARG n 
1 156 GLU n 
1 157 PHE n 
1 158 LEU n 
1 159 TRP n 
1 160 GLN n 
1 161 GLU n 
1 162 GLY n 
1 163 HIS n 
1 164 THR n 
1 165 ALA n 
1 166 PHE n 
1 167 ALA n 
1 168 THR n 
1 169 GLN n 
1 170 LYS n 
1 171 GLU n 
1 172 ALA n 
1 173 ASP n 
1 174 GLU n 
1 175 GLU n 
1 176 VAL n 
1 177 LEU n 
1 178 THR n 
1 179 ILE n 
1 180 LEU n 
1 181 ASP n 
1 182 LEU n 
1 183 TYR n 
1 184 ALA n 
1 185 LYS n 
1 186 VAL n 
1 187 TYR n 
1 188 THR n 
1 189 ASP n 
1 190 LEU n 
1 191 LEU n 
1 192 ALA n 
1 193 ILE n 
1 194 PRO n 
1 195 VAL n 
1 196 VAL n 
1 197 LYS n 
1 198 GLY n 
1 199 ARG n 
1 200 LYS n 
1 201 THR n 
1 202 GLU n 
1 203 LYS n 
1 204 GLU n 
1 205 LYS n 
1 206 PHE n 
1 207 ALA n 
1 208 GLY n 
1 209 GLY n 
1 210 ASP n 
1 211 TYR n 
1 212 THR n 
1 213 THR n 
1 214 THR n 
1 215 VAL n 
1 216 GLU n 
1 217 ALA n 
1 218 TYR n 
1 219 ILE n 
1 220 SER n 
1 221 ALA n 
1 222 SER n 
1 223 GLY n 
1 224 ARG n 
1 225 ALA n 
1 226 ILE n 
1 227 GLN n 
1 228 GLY n 
1 229 ALA n 
1 230 THR n 
1 231 SER n 
1 232 HIS n 
1 233 HIS n 
1 234 LEU n 
1 235 GLY n 
1 236 GLN n 
1 237 ASN n 
1 238 PHE n 
1 239 SER n 
1 240 ARG n 
1 241 MET n 
1 242 PHE n 
1 243 ASP n 
1 244 ILE n 
1 245 VAL n 
1 246 TYR n 
1 247 GLU n 
1 248 HIS n 
1 249 PRO n 
1 250 GLU n 
1 251 THR n 
1 252 LYS n 
1 253 GLU n 
1 254 LYS n 
1 255 GLU n 
1 256 TYR n 
1 257 VAL n 
1 258 PHE n 
1 259 GLN n 
1 260 ASN n 
1 261 SER n 
1 262 TRP n 
1 263 GLY n 
1 264 ILE n 
1 265 THR n 
1 266 THR n 
1 267 ARG n 
1 268 THR n 
1 269 ILE n 
1 270 GLY n 
1 271 VAL n 
1 272 MET n 
1 273 ILE n 
1 274 MET n 
1 275 VAL n 
1 276 HIS n 
1 277 ALA n 
1 278 ASP n 
1 279 ASN n 
1 280 GLN n 
1 281 GLY n 
1 282 LEU n 
1 283 VAL n 
1 284 LEU n 
1 285 PRO n 
1 286 PRO n 
1 287 ARG n 
1 288 VAL n 
1 289 ALA n 
1 290 CYS n 
1 291 ILE n 
1 292 GLN n 
1 293 VAL n 
1 294 VAL n 
1 295 ILE n 
1 296 VAL n 
1 297 PRO n 
1 298 CYS n 
1 299 GLY n 
1 300 ILE n 
1 301 THR n 
1 302 ALA n 
1 303 THR n 
1 304 THR n 
1 305 THR n 
1 306 ASP n 
1 307 ASP n 
1 308 GLU n 
1 309 ARG n 
1 310 ARG n 
1 311 ARG n 
1 312 LEU n 
1 313 TYR n 
1 314 GLU n 
1 315 SER n 
1 316 CYS n 
1 317 ARG n 
1 318 GLU n 
1 319 LEU n 
1 320 GLU n 
1 321 GLN n 
1 322 THR n 
1 323 PHE n 
1 324 VAL n 
1 325 LYS n 
1 326 ALA n 
1 327 GLY n 
1 328 ILE n 
1 329 ARG n 
1 330 CYS n 
1 331 GLU n 
1 332 GLY n 
1 333 ASP n 
1 334 TYR n 
1 335 ARG n 
1 336 ASP n 
1 337 ASN n 
1 338 TYR n 
1 339 SER n 
1 340 PRO n 
1 341 GLY n 
1 342 TRP n 
1 343 LYS n 
1 344 TYR n 
1 345 ASN n 
1 346 HIS n 
1 347 TRP n 
1 348 GLU n 
1 349 LEU n 
1 350 LYS n 
1 351 GLY n 
1 352 VAL n 
1 353 PRO n 
1 354 VAL n 
1 355 ARG n 
1 356 ILE n 
1 357 GLU n 
1 358 LEU n 
1 359 GLY n 
1 360 PHE n 
1 361 LYS n 
1 362 ASP n 
1 363 LEU n 
1 364 GLN n 
1 365 ASN n 
1 366 ASP n 
1 367 GLN n 
1 368 PHE n 
1 369 VAL n 
1 370 ALA n 
1 371 VAL n 
1 372 ARG n 
1 373 ARG n 
1 374 ASP n 
1 375 ASN n 
1 376 GLY n 
1 377 ALA n 
1 378 LYS n 
1 379 GLN n 
1 380 THR n 
1 381 ILE n 
1 382 LYS n 
1 383 ARG n 
1 384 ALA n 
1 385 GLN n 
1 386 ALA n 
1 387 THR n 
1 388 VAL n 
1 389 GLU n 
1 390 MET n 
1 391 PRO n 
1 392 LYS n 
1 393 LEU n 
1 394 LEU n 
1 395 GLU n 
1 396 THR n 
1 397 ILE n 
1 398 HIS n 
1 399 THR n 
1 400 SER n 
1 401 MET n 
1 402 TYR n 
1 403 GLU n 
1 404 ARG n 
1 405 ALA n 
1 406 GLU n 
1 407 ARG n 
1 408 ASP n 
1 409 LEU n 
1 410 GLN n 
1 411 SER n 
1 412 HIS n 
1 413 THR n 
1 414 LYS n 
1 415 LEU n 
1 416 THR n 
1 417 LYS n 
1 418 GLN n 
1 419 TRP n 
1 420 ALA n 
1 421 GLU n 
1 422 PHE n 
1 423 LEU n 
1 424 GLN n 
1 425 PHE n 
1 426 LEU n 
1 427 GLU n 
1 428 THR n 
1 429 LYS n 
1 430 ASN n 
1 431 ILE n 
1 432 ILE n 
1 433 MET n 
1 434 ALA n 
1 435 PRO n 
1 436 PHE n 
1 437 CYS n 
1 438 GLY n 
1 439 GLU n 
1 440 ILE n 
1 441 SER n 
1 442 CYS n 
1 443 GLU n 
1 444 ASP n 
1 445 ARG n 
1 446 ILE n 
1 447 LYS n 
1 448 ALA n 
1 449 GLU n 
1 450 SER n 
1 451 ALA n 
1 452 ARG n 
1 453 ASP n 
1 454 ASP n 
1 455 ALA n 
1 456 GLU n 
1 457 ALA n 
1 458 GLU n 
1 459 ALA n 
1 460 GLY n 
1 461 ALA n 
1 462 PRO n 
1 463 ALA n 
1 464 MET n 
1 465 GLY n 
1 466 ALA n 
1 467 LYS n 
1 468 SER n 
1 469 LEU n 
1 470 CYS n 
1 471 ILE n 
1 472 PRO n 
1 473 PHE n 
1 474 GLU n 
1 475 GLN n 
1 476 PRO n 
1 477 ALA n 
1 478 LYS n 
1 479 ILE n 
1 480 ASP n 
1 481 PRO n 
1 482 LYS n 
1 483 VAL n 
1 484 ASP n 
1 485 LYS n 
1 486 CYS n 
1 487 VAL n 
1 488 HIS n 
1 489 PRO n 
1 490 ALA n 
1 491 CYS n 
1 492 GLY n 
1 493 ARG n 
1 494 VAL n 
1 495 ALA n 
1 496 LYS n 
1 497 PHE n 
1 498 TYR n 
1 499 THR n 
1 500 LEU n 
1 501 PHE n 
1 502 GLY n 
1 503 ARG n 
1 504 SER n 
1 505 TYR 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                   505 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Anopheles culicifacies' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     139723 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     511693 
_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                       pETM11 
_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 
CL  non-polymer         . 'CHLORIDE ION'                                                                             ? 'Cl -1' 
35.453  
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  
GOL non-polymer         . GLYCEROL                                                                                   
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'            92.094  
HFG non-polymer         . '7-bromo-6-chloro-3-{3-[(2R,3S)-3-hydroxypiperidin-2-yl]-2-oxopropyl}quinazolin-4(3H)-one' Halofuginone 
'C16 H17 Br Cl N3 O3' 414.681 
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 
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 
ZN  non-polymer         . 'ZINC ION'                                                                                 ? 'Zn 2' 
65.409  
# 
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   1218 ?    ?   ?   A . n 
A 1 2   THR 2   1219 ?    ?   ?   A . n 
A 1 3   ARG 3   1220 1220 ARG ARG A . n 
A 1 4   LEU 4   1221 1221 LEU LEU A . n 
A 1 5   GLY 5   1222 1222 GLY GLY A . n 
A 1 6   LEU 6   1223 1223 LEU LEU A . n 
A 1 7   GLU 7   1224 1224 GLU GLU A . n 
A 1 8   ALA 8   1225 1225 ALA ALA A . n 
A 1 9   THR 9   1226 1226 THR THR A . n 
A 1 10  LYS 10  1227 1227 LYS LYS A . n 
A 1 11  GLU 11  1228 1228 GLU GLU A . n 
A 1 12  ASP 12  1229 1229 ASP ASP A . n 
A 1 13  ASN 13  1230 1230 ASN ASN A . n 
A 1 14  LEU 14  1231 1231 LEU LEU A . n 
A 1 15  PRO 15  1232 1232 PRO PRO A . n 
A 1 16  ASP 16  1233 1233 ASP ASP A . n 
A 1 17  TRP 17  1234 1234 TRP TRP A . n 
A 1 18  TYR 18  1235 1235 TYR TYR A . n 
A 1 19  SER 19  1236 1236 SER SER A . n 
A 1 20  GLN 20  1237 1237 GLN GLN A . n 
A 1 21  VAL 21  1238 1238 VAL VAL A . n 
A 1 22  ILE 22  1239 1239 ILE ILE A . n 
A 1 23  THR 23  1240 1240 THR THR A . n 
A 1 24  LYS 24  1241 1241 LYS LYS A . n 
A 1 25  GLY 25  1242 1242 GLY GLY A . n 
A 1 26  GLU 26  1243 1243 GLU GLU A . n 
A 1 27  MET 27  1244 1244 MET MET A . n 
A 1 28  ILE 28  1245 1245 ILE ILE A . n 
A 1 29  GLU 29  1246 1246 GLU GLU A . n 
A 1 30  TYR 30  1247 1247 TYR TYR A . n 
A 1 31  TYR 31  1248 1248 TYR TYR A . n 
A 1 32  ASP 32  1249 1249 ASP ASP A . n 
A 1 33  VAL 33  1250 1250 VAL VAL A . n 
A 1 34  SER 34  1251 1251 SER SER A . n 
A 1 35  GLY 35  1252 1252 GLY GLY A . n 
A 1 36  CYS 36  1253 1253 CYS CYS A . n 
A 1 37  TYR 37  1254 1254 TYR TYR A . n 
A 1 38  ILE 38  1255 1255 ILE ILE A . n 
A 1 39  LEU 39  1256 1256 LEU LEU A . n 
A 1 40  ARG 40  1257 1257 ARG ARG A . n 
A 1 41  HIS 41  1258 1258 HIS HIS A . n 
A 1 42  TRP 42  1259 1259 TRP TRP A . n 
A 1 43  SER 43  1260 1260 SER SER A . n 
A 1 44  PHE 44  1261 1261 PHE PHE A . n 
A 1 45  ALA 45  1262 1262 ALA ALA A . n 
A 1 46  ILE 46  1263 1263 ILE ILE A . n 
A 1 47  TRP 47  1264 1264 TRP TRP A . n 
A 1 48  LYS 48  1265 1265 LYS LYS A . n 
A 1 49  ALA 49  1266 1266 ALA ALA A . n 
A 1 50  ILE 50  1267 1267 ILE ILE A . n 
A 1 51  ARG 51  1268 1268 ARG ARG A . n 
A 1 52  ASN 52  1269 1269 ASN ASN A . n 
A 1 53  TRP 53  1270 1270 TRP TRP A . n 
A 1 54  PHE 54  1271 1271 PHE PHE A . n 
A 1 55  ASP 55  1272 1272 ASP ASP A . n 
A 1 56  ALA 56  1273 1273 ALA ALA A . n 
A 1 57  GLU 57  1274 1274 GLU GLU A . n 
A 1 58  ILE 58  1275 1275 ILE ILE A . n 
A 1 59  THR 59  1276 1276 THR THR A . n 
A 1 60  ARG 60  1277 1277 ARG ARG A . n 
A 1 61  LEU 61  1278 1278 LEU LEU A . n 
A 1 62  GLY 62  1279 1279 GLY GLY A . n 
A 1 63  VAL 63  1280 1280 VAL VAL A . n 
A 1 64  LYS 64  1281 1281 LYS LYS A . n 
A 1 65  GLU 65  1282 1282 GLU GLU A . n 
A 1 66  CYS 66  1283 1283 CYS CYS A . n 
A 1 67  TYR 67  1284 1284 TYR TYR A . n 
A 1 68  PHE 68  1285 1285 PHE PHE A . n 
A 1 69  PRO 69  1286 1286 PRO PRO A . n 
A 1 70  ILE 70  1287 1287 ILE ILE A . n 
A 1 71  PHE 71  1288 1288 PHE PHE A . n 
A 1 72  VAL 72  1289 1289 VAL VAL A . n 
A 1 73  SER 73  1290 1290 SER SER A . n 
A 1 74  ARG 74  1291 1291 ARG ARG A . n 
A 1 75  ALA 75  1292 1292 ALA ALA A . n 
A 1 76  ALA 76  1293 1293 ALA ALA A . n 
A 1 77  LEU 77  1294 1294 LEU LEU A . n 
A 1 78  GLU 78  1295 1295 GLU GLU A . n 
A 1 79  ARG 79  1296 1296 ARG ARG A . n 
A 1 80  GLU 80  1297 1297 GLU GLU A . n 
A 1 81  LYS 81  1298 1298 LYS LYS A . n 
A 1 82  THR 82  1299 1299 THR THR A . n 
A 1 83  HIS 83  1300 1300 HIS HIS A . n 
A 1 84  ILE 84  1301 1301 ILE ILE A . n 
A 1 85  ALA 85  1302 1302 ALA ALA A . n 
A 1 86  ASP 86  1303 1303 ASP ASP A . n 
A 1 87  PHE 87  1304 1304 PHE PHE A . n 
A 1 88  ALA 88  1305 1305 ALA ALA A . n 
A 1 89  PRO 89  1306 1306 PRO PRO A . n 
A 1 90  GLU 90  1307 1307 GLU GLU A . n 
A 1 91  VAL 91  1308 1308 VAL VAL A . n 
A 1 92  ALA 92  1309 1309 ALA ALA A . n 
A 1 93  TRP 93  1310 1310 TRP TRP A . n 
A 1 94  VAL 94  1311 1311 VAL VAL A . n 
A 1 95  THR 95  1312 1312 THR THR A . n 
A 1 96  LYS 96  1313 1313 LYS LYS A . n 
A 1 97  SER 97  1314 1314 SER SER A . n 
A 1 98  GLY 98  1315 1315 GLY GLY A . n 
A 1 99  ASP 99  1316 1316 ASP ASP A . n 
A 1 100 SER 100 1317 1317 SER SER A . n 
A 1 101 GLU 101 1318 1318 GLU GLU A . n 
A 1 102 LEU 102 1319 1319 LEU LEU A . n 
A 1 103 ALA 103 1320 1320 ALA ALA A . n 
A 1 104 GLU 104 1321 1321 GLU GLU A . n 
A 1 105 PRO 105 1322 1322 PRO PRO A . n 
A 1 106 ILE 106 1323 1323 ILE ILE A . n 
A 1 107 ALA 107 1324 1324 ALA ALA A . n 
A 1 108 VAL 108 1325 1325 VAL VAL A . n 
A 1 109 ARG 109 1326 1326 ARG ARG A . n 
A 1 110 PRO 110 1327 1327 PRO PRO A . n 
A 1 111 THR 111 1328 1328 THR THR A . n 
A 1 112 SER 112 1329 1329 SER SER A . n 
A 1 113 GLU 113 1330 1330 GLU GLU A . n 
A 1 114 THR 114 1331 1331 THR THR A . n 
A 1 115 VAL 115 1332 1332 VAL VAL A . n 
A 1 116 MET 116 1333 1333 MET MET A . n 
A 1 117 TYR 117 1334 1334 TYR TYR A . n 
A 1 118 PRO 118 1335 1335 PRO PRO A . n 
A 1 119 ALA 119 1336 1336 ALA ALA A . n 
A 1 120 TYR 120 1337 1337 TYR TYR A . n 
A 1 121 ALA 121 1338 1338 ALA ALA A . n 
A 1 122 LYS 122 1339 1339 LYS LYS A . n 
A 1 123 TRP 123 1340 1340 TRP TRP A . n 
A 1 124 ILE 124 1341 1341 ILE ILE A . n 
A 1 125 GLN 125 1342 1342 GLN GLN A . n 
A 1 126 SER 126 1343 1343 SER SER A . n 
A 1 127 TYR 127 1344 1344 TYR TYR A . n 
A 1 128 ARG 128 1345 1345 ARG ARG A . n 
A 1 129 ASP 129 1346 1346 ASP ASP A . n 
A 1 130 LEU 130 1347 1347 LEU LEU A . n 
A 1 131 PRO 131 1348 1348 PRO PRO A . n 
A 1 132 ILE 132 1349 1349 ILE ILE A . n 
A 1 133 ARG 133 1350 1350 ARG ARG A . n 
A 1 134 LEU 134 1351 1351 LEU LEU A . n 
A 1 135 ASN 135 1352 1352 ASN ASN A . n 
A 1 136 GLN 136 1353 1353 GLN GLN A . n 
A 1 137 TRP 137 1354 1354 TRP TRP A . n 
A 1 138 ASN 138 1355 1355 ASN ASN A . n 
A 1 139 ASN 139 1356 1356 ASN ASN A . n 
A 1 140 VAL 140 1357 1357 VAL VAL A . n 
A 1 141 VAL 141 1358 1358 VAL VAL A . n 
A 1 142 ARG 142 1359 1359 ARG ARG A . n 
A 1 143 TRP 143 1360 1360 TRP TRP A . n 
A 1 144 GLU 144 1361 1361 GLU GLU A . n 
A 1 145 PHE 145 1362 1362 PHE PHE A . n 
A 1 146 LYS 146 1363 1363 LYS LYS A . n 
A 1 147 HIS 147 1364 1364 HIS HIS A . n 
A 1 148 PRO 148 1365 1365 PRO PRO A . n 
A 1 149 GLN 149 1366 1366 GLN GLN A . n 
A 1 150 PRO 150 1367 1367 PRO PRO A . n 
A 1 151 PHE 151 1368 1368 PHE PHE A . n 
A 1 152 LEU 152 1369 1369 LEU LEU A . n 
A 1 153 ARG 153 1370 1370 ARG ARG A . n 
A 1 154 THR 154 1371 1371 THR THR A . n 
A 1 155 ARG 155 1372 1372 ARG ARG A . n 
A 1 156 GLU 156 1373 1373 GLU GLU A . n 
A 1 157 PHE 157 1374 1374 PHE PHE A . n 
A 1 158 LEU 158 1375 1375 LEU LEU A . n 
A 1 159 TRP 159 1376 1376 TRP TRP A . n 
A 1 160 GLN 160 1377 1377 GLN GLN A . n 
A 1 161 GLU 161 1378 1378 GLU GLU A . n 
A 1 162 GLY 162 1379 1379 GLY GLY A . n 
A 1 163 HIS 163 1380 1380 HIS HIS A . n 
A 1 164 THR 164 1381 1381 THR THR A . n 
A 1 165 ALA 165 1382 1382 ALA ALA A . n 
A 1 166 PHE 166 1383 1383 PHE PHE A . n 
A 1 167 ALA 167 1384 1384 ALA ALA A . n 
A 1 168 THR 168 1385 1385 THR THR A . n 
A 1 169 GLN 169 1386 1386 GLN GLN A . n 
A 1 170 LYS 170 1387 1387 LYS LYS A . n 
A 1 171 GLU 171 1388 1388 GLU GLU A . n 
A 1 172 ALA 172 1389 1389 ALA ALA A . n 
A 1 173 ASP 173 1390 1390 ASP ASP A . n 
A 1 174 GLU 174 1391 1391 GLU GLU A . n 
A 1 175 GLU 175 1392 1392 GLU GLU A . n 
A 1 176 VAL 176 1393 1393 VAL VAL A . n 
A 1 177 LEU 177 1394 1394 LEU LEU A . n 
A 1 178 THR 178 1395 1395 THR THR A . n 
A 1 179 ILE 179 1396 1396 ILE ILE A . n 
A 1 180 LEU 180 1397 1397 LEU LEU A . n 
A 1 181 ASP 181 1398 1398 ASP ASP A . n 
A 1 182 LEU 182 1399 1399 LEU LEU A . n 
A 1 183 TYR 183 1400 1400 TYR TYR A . n 
A 1 184 ALA 184 1401 1401 ALA ALA A . n 
A 1 185 LYS 185 1402 1402 LYS LYS A . n 
A 1 186 VAL 186 1403 1403 VAL VAL A . n 
A 1 187 TYR 187 1404 1404 TYR TYR A . n 
A 1 188 THR 188 1405 1405 THR THR A . n 
A 1 189 ASP 189 1406 1406 ASP ASP A . n 
A 1 190 LEU 190 1407 1407 LEU LEU A . n 
A 1 191 LEU 191 1408 1408 LEU LEU A . n 
A 1 192 ALA 192 1409 1409 ALA ALA A . n 
A 1 193 ILE 193 1410 1410 ILE ILE A . n 
A 1 194 PRO 194 1411 1411 PRO PRO A . n 
A 1 195 VAL 195 1412 1412 VAL VAL A . n 
A 1 196 VAL 196 1413 1413 VAL VAL A . n 
A 1 197 LYS 197 1414 1414 LYS LYS A . n 
A 1 198 GLY 198 1415 1415 GLY GLY A . n 
A 1 199 ARG 199 1416 1416 ARG ARG A . n 
A 1 200 LYS 200 1417 1417 LYS LYS A . n 
A 1 201 THR 201 1418 1418 THR THR A . n 
A 1 202 GLU 202 1419 1419 GLU GLU A . n 
A 1 203 LYS 203 1420 1420 LYS LYS A . n 
A 1 204 GLU 204 1421 1421 GLU GLU A . n 
A 1 205 LYS 205 1422 1422 LYS LYS A . n 
A 1 206 PHE 206 1423 1423 PHE PHE A . n 
A 1 207 ALA 207 1424 1424 ALA ALA A . n 
A 1 208 GLY 208 1425 1425 GLY GLY A . n 
A 1 209 GLY 209 1426 1426 GLY GLY A . n 
A 1 210 ASP 210 1427 1427 ASP ASP A . n 
A 1 211 TYR 211 1428 1428 TYR TYR A . n 
A 1 212 THR 212 1429 1429 THR THR A . n 
A 1 213 THR 213 1430 1430 THR THR A . n 
A 1 214 THR 214 1431 1431 THR THR A . n 
A 1 215 VAL 215 1432 1432 VAL VAL A . n 
A 1 216 GLU 216 1433 1433 GLU GLU A . n 
A 1 217 ALA 217 1434 1434 ALA ALA A . n 
A 1 218 TYR 218 1435 1435 TYR TYR A . n 
A 1 219 ILE 219 1436 1436 ILE ILE A . n 
A 1 220 SER 220 1437 1437 SER SER A . n 
A 1 221 ALA 221 1438 1438 ALA ALA A . n 
A 1 222 SER 222 1439 1439 SER SER A . n 
A 1 223 GLY 223 1440 1440 GLY GLY A . n 
A 1 224 ARG 224 1441 1441 ARG ARG A . n 
A 1 225 ALA 225 1442 1442 ALA ALA A . n 
A 1 226 ILE 226 1443 1443 ILE ILE A . n 
A 1 227 GLN 227 1444 1444 GLN GLN A . n 
A 1 228 GLY 228 1445 1445 GLY GLY A . n 
A 1 229 ALA 229 1446 1446 ALA ALA A . n 
A 1 230 THR 230 1447 1447 THR THR A . n 
A 1 231 SER 231 1448 1448 SER SER A . n 
A 1 232 HIS 232 1449 1449 HIS HIS A . n 
A 1 233 HIS 233 1450 1450 HIS HIS A . n 
A 1 234 LEU 234 1451 1451 LEU LEU A . n 
A 1 235 GLY 235 1452 1452 GLY GLY A . n 
A 1 236 GLN 236 1453 1453 GLN GLN A . n 
A 1 237 ASN 237 1454 1454 ASN ASN A . n 
A 1 238 PHE 238 1455 1455 PHE PHE A . n 
A 1 239 SER 239 1456 1456 SER SER A . n 
A 1 240 ARG 240 1457 1457 ARG ARG A . n 
A 1 241 MET 241 1458 1458 MET MET A . n 
A 1 242 PHE 242 1459 1459 PHE PHE A . n 
A 1 243 ASP 243 1460 1460 ASP ASP A . n 
A 1 244 ILE 244 1461 1461 ILE ILE A . n 
A 1 245 VAL 245 1462 1462 VAL VAL A . n 
A 1 246 TYR 246 1463 1463 TYR TYR A . n 
A 1 247 GLU 247 1464 1464 GLU GLU A . n 
A 1 248 HIS 248 1465 1465 HIS HIS A . n 
A 1 249 PRO 249 1466 1466 PRO PRO A . n 
A 1 250 GLU 250 1467 1467 GLU GLU A . n 
A 1 251 THR 251 1468 1468 THR THR A . n 
A 1 252 LYS 252 1469 1469 LYS LYS A . n 
A 1 253 GLU 253 1470 1470 GLU GLU A . n 
A 1 254 LYS 254 1471 1471 LYS LYS A . n 
A 1 255 GLU 255 1472 1472 GLU GLU A . n 
A 1 256 TYR 256 1473 1473 TYR TYR A . n 
A 1 257 VAL 257 1474 1474 VAL VAL A . n 
A 1 258 PHE 258 1475 1475 PHE PHE A . n 
A 1 259 GLN 259 1476 1476 GLN GLN A . n 
A 1 260 ASN 260 1477 1477 ASN ASN A . n 
A 1 261 SER 261 1478 1478 SER SER A . n 
A 1 262 TRP 262 1479 1479 TRP TRP A . n 
A 1 263 GLY 263 1480 1480 GLY GLY A . n 
A 1 264 ILE 264 1481 1481 ILE ILE A . n 
A 1 265 THR 265 1482 1482 THR THR A . n 
A 1 266 THR 266 1483 1483 THR THR A . n 
A 1 267 ARG 267 1484 1484 ARG ARG A . n 
A 1 268 THR 268 1485 1485 THR THR A . n 
A 1 269 ILE 269 1486 1486 ILE ILE A . n 
A 1 270 GLY 270 1487 1487 GLY GLY A . n 
A 1 271 VAL 271 1488 1488 VAL VAL A . n 
A 1 272 MET 272 1489 1489 MET MET A . n 
A 1 273 ILE 273 1490 1490 ILE ILE A . n 
A 1 274 MET 274 1491 1491 MET MET A . n 
A 1 275 VAL 275 1492 1492 VAL VAL A . n 
A 1 276 HIS 276 1493 1493 HIS HIS A . n 
A 1 277 ALA 277 1494 1494 ALA ALA A . n 
A 1 278 ASP 278 1495 1495 ASP ASP A . n 
A 1 279 ASN 279 1496 1496 ASN ASN A . n 
A 1 280 GLN 280 1497 1497 GLN GLN A . n 
A 1 281 GLY 281 1498 1498 GLY GLY A . n 
A 1 282 LEU 282 1499 1499 LEU LEU A . n 
A 1 283 VAL 283 1500 1500 VAL VAL A . n 
A 1 284 LEU 284 1501 1501 LEU LEU A . n 
A 1 285 PRO 285 1502 1502 PRO PRO A . n 
A 1 286 PRO 286 1503 1503 PRO PRO A . n 
A 1 287 ARG 287 1504 1504 ARG ARG A . n 
A 1 288 VAL 288 1505 1505 VAL VAL A . n 
A 1 289 ALA 289 1506 1506 ALA ALA A . n 
A 1 290 CYS 290 1507 1507 CYS CYS A . n 
A 1 291 ILE 291 1508 1508 ILE ILE A . n 
A 1 292 GLN 292 1509 1509 GLN GLN A . n 
A 1 293 VAL 293 1510 1510 VAL VAL A . n 
A 1 294 VAL 294 1511 1511 VAL VAL A . n 
A 1 295 ILE 295 1512 1512 ILE ILE A . n 
A 1 296 VAL 296 1513 1513 VAL VAL A . n 
A 1 297 PRO 297 1514 1514 PRO PRO A . n 
A 1 298 CYS 298 1515 1515 CYS CYS A . n 
A 1 299 GLY 299 1516 1516 GLY GLY A . n 
A 1 300 ILE 300 1517 1517 ILE ILE A . n 
A 1 301 THR 301 1518 1518 THR THR A . n 
A 1 302 ALA 302 1519 1519 ALA ALA A . n 
A 1 303 THR 303 1520 1520 THR THR A . n 
A 1 304 THR 304 1521 1521 THR THR A . n 
A 1 305 THR 305 1522 1522 THR THR A . n 
A 1 306 ASP 306 1523 1523 ASP ASP A . n 
A 1 307 ASP 307 1524 1524 ASP ASP A . n 
A 1 308 GLU 308 1525 1525 GLU GLU A . n 
A 1 309 ARG 309 1526 1526 ARG ARG A . n 
A 1 310 ARG 310 1527 1527 ARG ARG A . n 
A 1 311 ARG 311 1528 1528 ARG ARG A . n 
A 1 312 LEU 312 1529 1529 LEU LEU A . n 
A 1 313 TYR 313 1530 1530 TYR TYR A . n 
A 1 314 GLU 314 1531 1531 GLU GLU A . n 
A 1 315 SER 315 1532 1532 SER SER A . n 
A 1 316 CYS 316 1533 1533 CYS CYS A . n 
A 1 317 ARG 317 1534 1534 ARG ARG A . n 
A 1 318 GLU 318 1535 1535 GLU GLU A . n 
A 1 319 LEU 319 1536 1536 LEU LEU A . n 
A 1 320 GLU 320 1537 1537 GLU GLU A . n 
A 1 321 GLN 321 1538 1538 GLN GLN A . n 
A 1 322 THR 322 1539 1539 THR THR A . n 
A 1 323 PHE 323 1540 1540 PHE PHE A . n 
A 1 324 VAL 324 1541 1541 VAL VAL A . n 
A 1 325 LYS 325 1542 1542 LYS LYS A . n 
A 1 326 ALA 326 1543 1543 ALA ALA A . n 
A 1 327 GLY 327 1544 1544 GLY GLY A . n 
A 1 328 ILE 328 1545 1545 ILE ILE A . n 
A 1 329 ARG 329 1546 1546 ARG ARG A . n 
A 1 330 CYS 330 1547 1547 CYS CYS A . n 
A 1 331 GLU 331 1548 1548 GLU GLU A . n 
A 1 332 GLY 332 1549 1549 GLY GLY A . n 
A 1 333 ASP 333 1550 1550 ASP ASP A . n 
A 1 334 TYR 334 1551 1551 TYR TYR A . n 
A 1 335 ARG 335 1552 1552 ARG ARG A . n 
A 1 336 ASP 336 1553 1553 ASP ASP A . n 
A 1 337 ASN 337 1554 1554 ASN ASN A . n 
A 1 338 TYR 338 1555 1555 TYR TYR A . n 
A 1 339 SER 339 1556 1556 SER SER A . n 
A 1 340 PRO 340 1557 1557 PRO PRO A . n 
A 1 341 GLY 341 1558 1558 GLY GLY A . n 
A 1 342 TRP 342 1559 1559 TRP TRP A . n 
A 1 343 LYS 343 1560 1560 LYS LYS A . n 
A 1 344 TYR 344 1561 1561 TYR TYR A . n 
A 1 345 ASN 345 1562 1562 ASN ASN A . n 
A 1 346 HIS 346 1563 1563 HIS HIS A . n 
A 1 347 TRP 347 1564 1564 TRP TRP A . n 
A 1 348 GLU 348 1565 1565 GLU GLU A . n 
A 1 349 LEU 349 1566 1566 LEU LEU A . n 
A 1 350 LYS 350 1567 1567 LYS LYS A . n 
A 1 351 GLY 351 1568 1568 GLY GLY A . n 
A 1 352 VAL 352 1569 1569 VAL VAL A . n 
A 1 353 PRO 353 1570 1570 PRO PRO A . n 
A 1 354 VAL 354 1571 1571 VAL VAL A . n 
A 1 355 ARG 355 1572 1572 ARG ARG A . n 
A 1 356 ILE 356 1573 1573 ILE ILE A . n 
A 1 357 GLU 357 1574 1574 GLU GLU A . n 
A 1 358 LEU 358 1575 1575 LEU LEU A . n 
A 1 359 GLY 359 1576 1576 GLY GLY A . n 
A 1 360 PHE 360 1577 1577 PHE PHE A . n 
A 1 361 LYS 361 1578 1578 LYS LYS A . n 
A 1 362 ASP 362 1579 1579 ASP ASP A . n 
A 1 363 LEU 363 1580 1580 LEU LEU A . n 
A 1 364 GLN 364 1581 1581 GLN GLN A . n 
A 1 365 ASN 365 1582 1582 ASN ASN A . n 
A 1 366 ASP 366 1583 1583 ASP ASP A . n 
A 1 367 GLN 367 1584 1584 GLN GLN A . n 
A 1 368 PHE 368 1585 1585 PHE PHE A . n 
A 1 369 VAL 369 1586 1586 VAL VAL A . n 
A 1 370 ALA 370 1587 1587 ALA ALA A . n 
A 1 371 VAL 371 1588 1588 VAL VAL A . n 
A 1 372 ARG 372 1589 1589 ARG ARG A . n 
A 1 373 ARG 373 1590 1590 ARG ARG A . n 
A 1 374 ASP 374 1591 1591 ASP ASP A . n 
A 1 375 ASN 375 1592 1592 ASN ASN A . n 
A 1 376 GLY 376 1593 1593 GLY GLY A . n 
A 1 377 ALA 377 1594 1594 ALA ALA A . n 
A 1 378 LYS 378 1595 1595 LYS LYS A . n 
A 1 379 GLN 379 1596 1596 GLN GLN A . n 
A 1 380 THR 380 1597 1597 THR THR A . n 
A 1 381 ILE 381 1598 1598 ILE ILE A . n 
A 1 382 LYS 382 1599 1599 LYS LYS A . n 
A 1 383 ARG 383 1600 1600 ARG ARG A . n 
A 1 384 ALA 384 1601 1601 ALA ALA A . n 
A 1 385 GLN 385 1602 1602 GLN GLN A . n 
A 1 386 ALA 386 1603 1603 ALA ALA A . n 
A 1 387 THR 387 1604 1604 THR THR A . n 
A 1 388 VAL 388 1605 1605 VAL VAL A . n 
A 1 389 GLU 389 1606 1606 GLU GLU A . n 
A 1 390 MET 390 1607 1607 MET MET A . n 
A 1 391 PRO 391 1608 1608 PRO PRO A . n 
A 1 392 LYS 392 1609 1609 LYS LYS A . n 
A 1 393 LEU 393 1610 1610 LEU LEU A . n 
A 1 394 LEU 394 1611 1611 LEU LEU A . n 
A 1 395 GLU 395 1612 1612 GLU GLU A . n 
A 1 396 THR 396 1613 1613 THR THR A . n 
A 1 397 ILE 397 1614 1614 ILE ILE A . n 
A 1 398 HIS 398 1615 1615 HIS HIS A . n 
A 1 399 THR 399 1616 1616 THR THR A . n 
A 1 400 SER 400 1617 1617 SER SER A . n 
A 1 401 MET 401 1618 1618 MET MET A . n 
A 1 402 TYR 402 1619 1619 TYR TYR A . n 
A 1 403 GLU 403 1620 1620 GLU GLU A . n 
A 1 404 ARG 404 1621 1621 ARG ARG A . n 
A 1 405 ALA 405 1622 1622 ALA ALA A . n 
A 1 406 GLU 406 1623 1623 GLU GLU A . n 
A 1 407 ARG 407 1624 1624 ARG ARG A . n 
A 1 408 ASP 408 1625 1625 ASP ASP A . n 
A 1 409 LEU 409 1626 1626 LEU LEU A . n 
A 1 410 GLN 410 1627 1627 GLN GLN A . n 
A 1 411 SER 411 1628 1628 SER SER A . n 
A 1 412 HIS 412 1629 1629 HIS HIS A . n 
A 1 413 THR 413 1630 1630 THR THR A . n 
A 1 414 LYS 414 1631 1631 LYS LYS A . n 
A 1 415 LEU 415 1632 1632 LEU LEU A . n 
A 1 416 THR 416 1633 1633 THR THR A . n 
A 1 417 LYS 417 1634 1634 LYS LYS A . n 
A 1 418 GLN 418 1635 1635 GLN GLN A . n 
A 1 419 TRP 419 1636 1636 TRP TRP A . n 
A 1 420 ALA 420 1637 1637 ALA ALA A . n 
A 1 421 GLU 421 1638 1638 GLU GLU A . n 
A 1 422 PHE 422 1639 1639 PHE PHE A . n 
A 1 423 LEU 423 1640 1640 LEU LEU A . n 
A 1 424 GLN 424 1641 1641 GLN GLN A . n 
A 1 425 PHE 425 1642 1642 PHE PHE A . n 
A 1 426 LEU 426 1643 1643 LEU LEU A . n 
A 1 427 GLU 427 1644 1644 GLU GLU A . n 
A 1 428 THR 428 1645 1645 THR THR A . n 
A 1 429 LYS 429 1646 1646 LYS LYS A . n 
A 1 430 ASN 430 1647 1647 ASN ASN A . n 
A 1 431 ILE 431 1648 1648 ILE ILE A . n 
A 1 432 ILE 432 1649 1649 ILE ILE A . n 
A 1 433 MET 433 1650 1650 MET MET A . n 
A 1 434 ALA 434 1651 1651 ALA ALA A . n 
A 1 435 PRO 435 1652 1652 PRO PRO A . n 
A 1 436 PHE 436 1653 1653 PHE PHE A . n 
A 1 437 CYS 437 1654 1654 CYS CYS A . n 
A 1 438 GLY 438 1655 1655 GLY GLY A . n 
A 1 439 GLU 439 1656 1656 GLU GLU A . n 
A 1 440 ILE 440 1657 1657 ILE ILE A . n 
A 1 441 SER 441 1658 1658 SER SER A . n 
A 1 442 CYS 442 1659 1659 CYS CYS A . n 
A 1 443 GLU 443 1660 1660 GLU GLU A . n 
A 1 444 ASP 444 1661 1661 ASP ASP A . n 
A 1 445 ARG 445 1662 1662 ARG ARG A . n 
A 1 446 ILE 446 1663 1663 ILE ILE A . n 
A 1 447 LYS 447 1664 1664 LYS LYS A . n 
A 1 448 ALA 448 1665 1665 ALA ALA A . n 
A 1 449 GLU 449 1666 1666 GLU GLU A . n 
A 1 450 SER 450 1667 1667 SER SER A . n 
A 1 451 ALA 451 1668 1668 ALA ALA A . n 
A 1 452 ARG 452 1669 ?    ?   ?   A . n 
A 1 453 ASP 453 1670 ?    ?   ?   A . n 
A 1 454 ASP 454 1671 ?    ?   ?   A . n 
A 1 455 ALA 455 1672 ?    ?   ?   A . n 
A 1 456 GLU 456 1673 ?    ?   ?   A . n 
A 1 457 ALA 457 1674 ?    ?   ?   A . n 
A 1 458 GLU 458 1675 ?    ?   ?   A . n 
A 1 459 ALA 459 1676 ?    ?   ?   A . n 
A 1 460 GLY 460 1677 ?    ?   ?   A . n 
A 1 461 ALA 461 1678 ?    ?   ?   A . n 
A 1 462 PRO 462 1679 ?    ?   ?   A . n 
A 1 463 ALA 463 1680 ?    ?   ?   A . n 
A 1 464 MET 464 1681 ?    ?   ?   A . n 
A 1 465 GLY 465 1682 1682 GLY GLY A . n 
A 1 466 ALA 466 1683 1683 ALA ALA A . n 
A 1 467 LYS 467 1684 1684 LYS LYS A . n 
A 1 468 SER 468 1685 1685 SER SER A . n 
A 1 469 LEU 469 1686 1686 LEU LEU A . n 
A 1 470 CYS 470 1687 1687 CYS CYS A . n 
A 1 471 ILE 471 1688 1688 ILE ILE A . n 
A 1 472 PRO 472 1689 1689 PRO PRO A . n 
A 1 473 PHE 473 1690 1690 PHE PHE A . n 
A 1 474 GLU 474 1691 1691 GLU GLU A . n 
A 1 475 GLN 475 1692 1692 GLN GLN A . n 
A 1 476 PRO 476 1693 1693 PRO PRO A . n 
A 1 477 ALA 477 1694 1694 ALA ALA A . n 
A 1 478 LYS 478 1695 1695 LYS LYS A . n 
A 1 479 ILE 479 1696 1696 ILE ILE A . n 
A 1 480 ASP 480 1697 1697 ASP ASP A . n 
A 1 481 PRO 481 1698 1698 PRO PRO A . n 
A 1 482 LYS 482 1699 1699 LYS LYS A . n 
A 1 483 VAL 483 1700 1700 VAL VAL A . n 
A 1 484 ASP 484 1701 1701 ASP ASP A . n 
A 1 485 LYS 485 1702 1702 LYS LYS A . n 
A 1 486 CYS 486 1703 1703 CYS CYS A . n 
A 1 487 VAL 487 1704 1704 VAL VAL A . n 
A 1 488 HIS 488 1705 1705 HIS HIS A . n 
A 1 489 PRO 489 1706 1706 PRO PRO A . n 
A 1 490 ALA 490 1707 1707 ALA ALA A . n 
A 1 491 CYS 491 1708 1708 CYS CYS A . n 
A 1 492 GLY 492 1709 1709 GLY GLY A . n 
A 1 493 ARG 493 1710 1710 ARG ARG A . n 
A 1 494 VAL 494 1711 1711 VAL VAL A . n 
A 1 495 ALA 495 1712 1712 ALA ALA A . n 
A 1 496 LYS 496 1713 1713 LYS LYS A . n 
A 1 497 PHE 497 1714 1714 PHE PHE A . n 
A 1 498 TYR 498 1715 1715 TYR TYR A . n 
A 1 499 THR 499 1716 1716 THR THR A . n 
A 1 500 LEU 500 1717 1717 LEU LEU A . n 
A 1 501 PHE 501 1718 1718 PHE PHE A . n 
A 1 502 GLY 502 1719 1719 GLY GLY A . n 
A 1 503 ARG 503 1720 1720 ARG ARG A . n 
A 1 504 SER 504 1721 1721 SER SER A . n 
A 1 505 TYR 505 1722 1722 TYR TYR A . n 
B 1 1   MET 1   1218 ?    ?   ?   B . n 
B 1 2   THR 2   1219 ?    ?   ?   B . n 
B 1 3   ARG 3   1220 ?    ?   ?   B . n 
B 1 4   LEU 4   1221 ?    ?   ?   B . n 
B 1 5   GLY 5   1222 ?    ?   ?   B . n 
B 1 6   LEU 6   1223 1223 LEU LEU B . n 
B 1 7   GLU 7   1224 1224 GLU GLU B . n 
B 1 8   ALA 8   1225 1225 ALA ALA B . n 
B 1 9   THR 9   1226 1226 THR THR B . n 
B 1 10  LYS 10  1227 1227 LYS LYS B . n 
B 1 11  GLU 11  1228 1228 GLU GLU B . n 
B 1 12  ASP 12  1229 1229 ASP ASP B . n 
B 1 13  ASN 13  1230 1230 ASN ASN B . n 
B 1 14  LEU 14  1231 1231 LEU LEU B . n 
B 1 15  PRO 15  1232 1232 PRO PRO B . n 
B 1 16  ASP 16  1233 1233 ASP ASP B . n 
B 1 17  TRP 17  1234 1234 TRP TRP B . n 
B 1 18  TYR 18  1235 1235 TYR TYR B . n 
B 1 19  SER 19  1236 1236 SER SER B . n 
B 1 20  GLN 20  1237 1237 GLN GLN B . n 
B 1 21  VAL 21  1238 1238 VAL VAL B . n 
B 1 22  ILE 22  1239 1239 ILE ILE B . n 
B 1 23  THR 23  1240 1240 THR THR B . n 
B 1 24  LYS 24  1241 1241 LYS LYS B . n 
B 1 25  GLY 25  1242 1242 GLY GLY B . n 
B 1 26  GLU 26  1243 1243 GLU GLU B . n 
B 1 27  MET 27  1244 1244 MET MET B . n 
B 1 28  ILE 28  1245 1245 ILE ILE B . n 
B 1 29  GLU 29  1246 1246 GLU GLU B . n 
B 1 30  TYR 30  1247 1247 TYR TYR B . n 
B 1 31  TYR 31  1248 1248 TYR TYR B . n 
B 1 32  ASP 32  1249 1249 ASP ASP B . n 
B 1 33  VAL 33  1250 1250 VAL VAL B . n 
B 1 34  SER 34  1251 1251 SER SER B . n 
B 1 35  GLY 35  1252 1252 GLY GLY B . n 
B 1 36  CYS 36  1253 1253 CYS CYS B . n 
B 1 37  TYR 37  1254 1254 TYR TYR B . n 
B 1 38  ILE 38  1255 1255 ILE ILE B . n 
B 1 39  LEU 39  1256 1256 LEU LEU B . n 
B 1 40  ARG 40  1257 1257 ARG ARG B . n 
B 1 41  HIS 41  1258 1258 HIS HIS B . n 
B 1 42  TRP 42  1259 1259 TRP TRP B . n 
B 1 43  SER 43  1260 1260 SER SER B . n 
B 1 44  PHE 44  1261 1261 PHE PHE B . n 
B 1 45  ALA 45  1262 1262 ALA ALA B . n 
B 1 46  ILE 46  1263 1263 ILE ILE B . n 
B 1 47  TRP 47  1264 1264 TRP TRP B . n 
B 1 48  LYS 48  1265 1265 LYS LYS B . n 
B 1 49  ALA 49  1266 1266 ALA ALA B . n 
B 1 50  ILE 50  1267 1267 ILE ILE B . n 
B 1 51  ARG 51  1268 1268 ARG ARG B . n 
B 1 52  ASN 52  1269 1269 ASN ASN B . n 
B 1 53  TRP 53  1270 1270 TRP TRP B . n 
B 1 54  PHE 54  1271 1271 PHE PHE B . n 
B 1 55  ASP 55  1272 1272 ASP ASP B . n 
B 1 56  ALA 56  1273 1273 ALA ALA B . n 
B 1 57  GLU 57  1274 1274 GLU GLU B . n 
B 1 58  ILE 58  1275 1275 ILE ILE B . n 
B 1 59  THR 59  1276 1276 THR THR B . n 
B 1 60  ARG 60  1277 1277 ARG ARG B . n 
B 1 61  LEU 61  1278 1278 LEU LEU B . n 
B 1 62  GLY 62  1279 1279 GLY GLY B . n 
B 1 63  VAL 63  1280 1280 VAL VAL B . n 
B 1 64  LYS 64  1281 1281 LYS LYS B . n 
B 1 65  GLU 65  1282 1282 GLU GLU B . n 
B 1 66  CYS 66  1283 1283 CYS CYS B . n 
B 1 67  TYR 67  1284 1284 TYR TYR B . n 
B 1 68  PHE 68  1285 1285 PHE PHE B . n 
B 1 69  PRO 69  1286 1286 PRO PRO B . n 
B 1 70  ILE 70  1287 1287 ILE ILE B . n 
B 1 71  PHE 71  1288 1288 PHE PHE B . n 
B 1 72  VAL 72  1289 1289 VAL VAL B . n 
B 1 73  SER 73  1290 1290 SER SER B . n 
B 1 74  ARG 74  1291 1291 ARG ARG B . n 
B 1 75  ALA 75  1292 1292 ALA ALA B . n 
B 1 76  ALA 76  1293 1293 ALA ALA B . n 
B 1 77  LEU 77  1294 1294 LEU LEU B . n 
B 1 78  GLU 78  1295 1295 GLU GLU B . n 
B 1 79  ARG 79  1296 1296 ARG ARG B . n 
B 1 80  GLU 80  1297 ?    ?   ?   B . n 
B 1 81  LYS 81  1298 ?    ?   ?   B . n 
B 1 82  THR 82  1299 ?    ?   ?   B . n 
B 1 83  HIS 83  1300 ?    ?   ?   B . n 
B 1 84  ILE 84  1301 ?    ?   ?   B . n 
B 1 85  ALA 85  1302 ?    ?   ?   B . n 
B 1 86  ASP 86  1303 1303 ASP ASP B . n 
B 1 87  PHE 87  1304 1304 PHE PHE B . n 
B 1 88  ALA 88  1305 1305 ALA ALA B . n 
B 1 89  PRO 89  1306 1306 PRO PRO B . n 
B 1 90  GLU 90  1307 1307 GLU GLU B . n 
B 1 91  VAL 91  1308 1308 VAL VAL B . n 
B 1 92  ALA 92  1309 1309 ALA ALA B . n 
B 1 93  TRP 93  1310 1310 TRP TRP B . n 
B 1 94  VAL 94  1311 1311 VAL VAL B . n 
B 1 95  THR 95  1312 1312 THR THR B . n 
B 1 96  LYS 96  1313 1313 LYS LYS B . n 
B 1 97  SER 97  1314 1314 SER SER B . n 
B 1 98  GLY 98  1315 1315 GLY GLY B . n 
B 1 99  ASP 99  1316 1316 ASP ASP B . n 
B 1 100 SER 100 1317 1317 SER SER B . n 
B 1 101 GLU 101 1318 1318 GLU GLU B . n 
B 1 102 LEU 102 1319 1319 LEU LEU B . n 
B 1 103 ALA 103 1320 1320 ALA ALA B . n 
B 1 104 GLU 104 1321 1321 GLU GLU B . n 
B 1 105 PRO 105 1322 1322 PRO PRO B . n 
B 1 106 ILE 106 1323 1323 ILE ILE B . n 
B 1 107 ALA 107 1324 1324 ALA ALA B . n 
B 1 108 VAL 108 1325 1325 VAL VAL B . n 
B 1 109 ARG 109 1326 1326 ARG ARG B . n 
B 1 110 PRO 110 1327 1327 PRO PRO B . n 
B 1 111 THR 111 1328 1328 THR THR B . n 
B 1 112 SER 112 1329 1329 SER SER B . n 
B 1 113 GLU 113 1330 1330 GLU GLU B . n 
B 1 114 THR 114 1331 1331 THR THR B . n 
B 1 115 VAL 115 1332 1332 VAL VAL B . n 
B 1 116 MET 116 1333 1333 MET MET B . n 
B 1 117 TYR 117 1334 1334 TYR TYR B . n 
B 1 118 PRO 118 1335 1335 PRO PRO B . n 
B 1 119 ALA 119 1336 1336 ALA ALA B . n 
B 1 120 TYR 120 1337 1337 TYR TYR B . n 
B 1 121 ALA 121 1338 1338 ALA ALA B . n 
B 1 122 LYS 122 1339 1339 LYS LYS B . n 
B 1 123 TRP 123 1340 1340 TRP TRP B . n 
B 1 124 ILE 124 1341 1341 ILE ILE B . n 
B 1 125 GLN 125 1342 1342 GLN GLN B . n 
B 1 126 SER 126 1343 1343 SER SER B . n 
B 1 127 TYR 127 1344 1344 TYR TYR B . n 
B 1 128 ARG 128 1345 1345 ARG ARG B . n 
B 1 129 ASP 129 1346 1346 ASP ASP B . n 
B 1 130 LEU 130 1347 1347 LEU LEU B . n 
B 1 131 PRO 131 1348 1348 PRO PRO B . n 
B 1 132 ILE 132 1349 1349 ILE ILE B . n 
B 1 133 ARG 133 1350 1350 ARG ARG B . n 
B 1 134 LEU 134 1351 1351 LEU LEU B . n 
B 1 135 ASN 135 1352 1352 ASN ASN B . n 
B 1 136 GLN 136 1353 1353 GLN GLN B . n 
B 1 137 TRP 137 1354 1354 TRP TRP B . n 
B 1 138 ASN 138 1355 1355 ASN ASN B . n 
B 1 139 ASN 139 1356 1356 ASN ASN B . n 
B 1 140 VAL 140 1357 1357 VAL VAL B . n 
B 1 141 VAL 141 1358 1358 VAL VAL B . n 
B 1 142 ARG 142 1359 1359 ARG ARG B . n 
B 1 143 TRP 143 1360 1360 TRP TRP B . n 
B 1 144 GLU 144 1361 1361 GLU GLU B . n 
B 1 145 PHE 145 1362 ?    ?   ?   B . n 
B 1 146 LYS 146 1363 1363 LYS LYS B . n 
B 1 147 HIS 147 1364 1364 HIS HIS B . n 
B 1 148 PRO 148 1365 1365 PRO PRO B . n 
B 1 149 GLN 149 1366 1366 GLN GLN B . n 
B 1 150 PRO 150 1367 1367 PRO PRO B . n 
B 1 151 PHE 151 1368 1368 PHE PHE B . n 
B 1 152 LEU 152 1369 1369 LEU LEU B . n 
B 1 153 ARG 153 1370 1370 ARG ARG B . n 
B 1 154 THR 154 1371 1371 THR THR B . n 
B 1 155 ARG 155 1372 1372 ARG ARG B . n 
B 1 156 GLU 156 1373 1373 GLU GLU B . n 
B 1 157 PHE 157 1374 1374 PHE PHE B . n 
B 1 158 LEU 158 1375 1375 LEU LEU B . n 
B 1 159 TRP 159 1376 1376 TRP TRP B . n 
B 1 160 GLN 160 1377 1377 GLN GLN B . n 
B 1 161 GLU 161 1378 1378 GLU GLU B . n 
B 1 162 GLY 162 1379 1379 GLY GLY B . n 
B 1 163 HIS 163 1380 1380 HIS HIS B . n 
B 1 164 THR 164 1381 1381 THR THR B . n 
B 1 165 ALA 165 1382 1382 ALA ALA B . n 
B 1 166 PHE 166 1383 1383 PHE PHE B . n 
B 1 167 ALA 167 1384 1384 ALA ALA B . n 
B 1 168 THR 168 1385 1385 THR THR B . n 
B 1 169 GLN 169 1386 1386 GLN GLN B . n 
B 1 170 LYS 170 1387 1387 LYS LYS B . n 
B 1 171 GLU 171 1388 1388 GLU GLU B . n 
B 1 172 ALA 172 1389 1389 ALA ALA B . n 
B 1 173 ASP 173 1390 1390 ASP ASP B . n 
B 1 174 GLU 174 1391 1391 GLU GLU B . n 
B 1 175 GLU 175 1392 1392 GLU GLU B . n 
B 1 176 VAL 176 1393 1393 VAL VAL B . n 
B 1 177 LEU 177 1394 1394 LEU LEU B . n 
B 1 178 THR 178 1395 1395 THR THR B . n 
B 1 179 ILE 179 1396 1396 ILE ILE B . n 
B 1 180 LEU 180 1397 1397 LEU LEU B . n 
B 1 181 ASP 181 1398 1398 ASP ASP B . n 
B 1 182 LEU 182 1399 1399 LEU LEU B . n 
B 1 183 TYR 183 1400 1400 TYR TYR B . n 
B 1 184 ALA 184 1401 1401 ALA ALA B . n 
B 1 185 LYS 185 1402 1402 LYS LYS B . n 
B 1 186 VAL 186 1403 1403 VAL VAL B . n 
B 1 187 TYR 187 1404 1404 TYR TYR B . n 
B 1 188 THR 188 1405 1405 THR THR B . n 
B 1 189 ASP 189 1406 1406 ASP ASP B . n 
B 1 190 LEU 190 1407 1407 LEU LEU B . n 
B 1 191 LEU 191 1408 1408 LEU LEU B . n 
B 1 192 ALA 192 1409 1409 ALA ALA B . n 
B 1 193 ILE 193 1410 1410 ILE ILE B . n 
B 1 194 PRO 194 1411 1411 PRO PRO B . n 
B 1 195 VAL 195 1412 1412 VAL VAL B . n 
B 1 196 VAL 196 1413 1413 VAL VAL B . n 
B 1 197 LYS 197 1414 1414 LYS LYS B . n 
B 1 198 GLY 198 1415 1415 GLY GLY B . n 
B 1 199 ARG 199 1416 1416 ARG ARG B . n 
B 1 200 LYS 200 1417 1417 LYS LYS B . n 
B 1 201 THR 201 1418 1418 THR THR B . n 
B 1 202 GLU 202 1419 1419 GLU GLU B . n 
B 1 203 LYS 203 1420 1420 LYS LYS B . n 
B 1 204 GLU 204 1421 1421 GLU GLU B . n 
B 1 205 LYS 205 1422 1422 LYS LYS B . n 
B 1 206 PHE 206 1423 1423 PHE PHE B . n 
B 1 207 ALA 207 1424 1424 ALA ALA B . n 
B 1 208 GLY 208 1425 1425 GLY GLY B . n 
B 1 209 GLY 209 1426 1426 GLY GLY B . n 
B 1 210 ASP 210 1427 1427 ASP ASP B . n 
B 1 211 TYR 211 1428 1428 TYR TYR B . n 
B 1 212 THR 212 1429 1429 THR THR B . n 
B 1 213 THR 213 1430 1430 THR THR B . n 
B 1 214 THR 214 1431 1431 THR THR B . n 
B 1 215 VAL 215 1432 1432 VAL VAL B . n 
B 1 216 GLU 216 1433 1433 GLU GLU B . n 
B 1 217 ALA 217 1434 1434 ALA ALA B . n 
B 1 218 TYR 218 1435 1435 TYR TYR B . n 
B 1 219 ILE 219 1436 1436 ILE ILE B . n 
B 1 220 SER 220 1437 1437 SER SER B . n 
B 1 221 ALA 221 1438 1438 ALA ALA B . n 
B 1 222 SER 222 1439 1439 SER SER B . n 
B 1 223 GLY 223 1440 1440 GLY GLY B . n 
B 1 224 ARG 224 1441 1441 ARG ARG B . n 
B 1 225 ALA 225 1442 1442 ALA ALA B . n 
B 1 226 ILE 226 1443 1443 ILE ILE B . n 
B 1 227 GLN 227 1444 1444 GLN GLN B . n 
B 1 228 GLY 228 1445 1445 GLY GLY B . n 
B 1 229 ALA 229 1446 1446 ALA ALA B . n 
B 1 230 THR 230 1447 1447 THR THR B . n 
B 1 231 SER 231 1448 1448 SER SER B . n 
B 1 232 HIS 232 1449 1449 HIS HIS B . n 
B 1 233 HIS 233 1450 1450 HIS HIS B . n 
B 1 234 LEU 234 1451 1451 LEU LEU B . n 
B 1 235 GLY 235 1452 1452 GLY GLY B . n 
B 1 236 GLN 236 1453 1453 GLN GLN B . n 
B 1 237 ASN 237 1454 1454 ASN ASN B . n 
B 1 238 PHE 238 1455 1455 PHE PHE B . n 
B 1 239 SER 239 1456 1456 SER SER B . n 
B 1 240 ARG 240 1457 1457 ARG ARG B . n 
B 1 241 MET 241 1458 1458 MET MET B . n 
B 1 242 PHE 242 1459 1459 PHE PHE B . n 
B 1 243 ASP 243 1460 1460 ASP ASP B . n 
B 1 244 ILE 244 1461 1461 ILE ILE B . n 
B 1 245 VAL 245 1462 1462 VAL VAL B . n 
B 1 246 TYR 246 1463 1463 TYR TYR B . n 
B 1 247 GLU 247 1464 1464 GLU GLU B . n 
B 1 248 HIS 248 1465 1465 HIS HIS B . n 
B 1 249 PRO 249 1466 1466 PRO PRO B . n 
B 1 250 GLU 250 1467 1467 GLU GLU B . n 
B 1 251 THR 251 1468 1468 THR THR B . n 
B 1 252 LYS 252 1469 1469 LYS LYS B . n 
B 1 253 GLU 253 1470 1470 GLU GLU B . n 
B 1 254 LYS 254 1471 1471 LYS LYS B . n 
B 1 255 GLU 255 1472 1472 GLU GLU B . n 
B 1 256 TYR 256 1473 1473 TYR TYR B . n 
B 1 257 VAL 257 1474 1474 VAL VAL B . n 
B 1 258 PHE 258 1475 1475 PHE PHE B . n 
B 1 259 GLN 259 1476 1476 GLN GLN B . n 
B 1 260 ASN 260 1477 1477 ASN ASN B . n 
B 1 261 SER 261 1478 1478 SER SER B . n 
B 1 262 TRP 262 1479 1479 TRP TRP B . n 
B 1 263 GLY 263 1480 1480 GLY GLY B . n 
B 1 264 ILE 264 1481 1481 ILE ILE B . n 
B 1 265 THR 265 1482 1482 THR THR B . n 
B 1 266 THR 266 1483 1483 THR THR B . n 
B 1 267 ARG 267 1484 1484 ARG ARG B . n 
B 1 268 THR 268 1485 1485 THR THR B . n 
B 1 269 ILE 269 1486 1486 ILE ILE B . n 
B 1 270 GLY 270 1487 1487 GLY GLY B . n 
B 1 271 VAL 271 1488 1488 VAL VAL B . n 
B 1 272 MET 272 1489 1489 MET MET B . n 
B 1 273 ILE 273 1490 1490 ILE ILE B . n 
B 1 274 MET 274 1491 1491 MET MET B . n 
B 1 275 VAL 275 1492 1492 VAL VAL B . n 
B 1 276 HIS 276 1493 1493 HIS HIS B . n 
B 1 277 ALA 277 1494 1494 ALA ALA B . n 
B 1 278 ASP 278 1495 1495 ASP ASP B . n 
B 1 279 ASN 279 1496 1496 ASN ASN B . n 
B 1 280 GLN 280 1497 1497 GLN GLN B . n 
B 1 281 GLY 281 1498 1498 GLY GLY B . n 
B 1 282 LEU 282 1499 1499 LEU LEU B . n 
B 1 283 VAL 283 1500 1500 VAL VAL B . n 
B 1 284 LEU 284 1501 1501 LEU LEU B . n 
B 1 285 PRO 285 1502 1502 PRO PRO B . n 
B 1 286 PRO 286 1503 1503 PRO PRO B . n 
B 1 287 ARG 287 1504 1504 ARG ARG B . n 
B 1 288 VAL 288 1505 1505 VAL VAL B . n 
B 1 289 ALA 289 1506 1506 ALA ALA B . n 
B 1 290 CYS 290 1507 1507 CYS CYS B . n 
B 1 291 ILE 291 1508 1508 ILE ILE B . n 
B 1 292 GLN 292 1509 1509 GLN GLN B . n 
B 1 293 VAL 293 1510 1510 VAL VAL B . n 
B 1 294 VAL 294 1511 1511 VAL VAL B . n 
B 1 295 ILE 295 1512 1512 ILE ILE B . n 
B 1 296 VAL 296 1513 1513 VAL VAL B . n 
B 1 297 PRO 297 1514 1514 PRO PRO B . n 
B 1 298 CYS 298 1515 1515 CYS CYS B . n 
B 1 299 GLY 299 1516 1516 GLY GLY B . n 
B 1 300 ILE 300 1517 1517 ILE ILE B . n 
B 1 301 THR 301 1518 1518 THR THR B . n 
B 1 302 ALA 302 1519 1519 ALA ALA B . n 
B 1 303 THR 303 1520 1520 THR THR B . n 
B 1 304 THR 304 1521 1521 THR THR B . n 
B 1 305 THR 305 1522 1522 THR THR B . n 
B 1 306 ASP 306 1523 1523 ASP ASP B . n 
B 1 307 ASP 307 1524 1524 ASP ASP B . n 
B 1 308 GLU 308 1525 1525 GLU GLU B . n 
B 1 309 ARG 309 1526 1526 ARG ARG B . n 
B 1 310 ARG 310 1527 1527 ARG ARG B . n 
B 1 311 ARG 311 1528 1528 ARG ARG B . n 
B 1 312 LEU 312 1529 1529 LEU LEU B . n 
B 1 313 TYR 313 1530 1530 TYR TYR B . n 
B 1 314 GLU 314 1531 1531 GLU GLU B . n 
B 1 315 SER 315 1532 1532 SER SER B . n 
B 1 316 CYS 316 1533 1533 CYS CYS B . n 
B 1 317 ARG 317 1534 1534 ARG ARG B . n 
B 1 318 GLU 318 1535 1535 GLU GLU B . n 
B 1 319 LEU 319 1536 1536 LEU LEU B . n 
B 1 320 GLU 320 1537 1537 GLU GLU B . n 
B 1 321 GLN 321 1538 1538 GLN GLN B . n 
B 1 322 THR 322 1539 1539 THR THR B . n 
B 1 323 PHE 323 1540 1540 PHE PHE B . n 
B 1 324 VAL 324 1541 1541 VAL VAL B . n 
B 1 325 LYS 325 1542 1542 LYS LYS B . n 
B 1 326 ALA 326 1543 1543 ALA ALA B . n 
B 1 327 GLY 327 1544 1544 GLY GLY B . n 
B 1 328 ILE 328 1545 1545 ILE ILE B . n 
B 1 329 ARG 329 1546 1546 ARG ARG B . n 
B 1 330 CYS 330 1547 1547 CYS CYS B . n 
B 1 331 GLU 331 1548 1548 GLU GLU B . n 
B 1 332 GLY 332 1549 1549 GLY GLY B . n 
B 1 333 ASP 333 1550 1550 ASP ASP B . n 
B 1 334 TYR 334 1551 1551 TYR TYR B . n 
B 1 335 ARG 335 1552 1552 ARG ARG B . n 
B 1 336 ASP 336 1553 1553 ASP ASP B . n 
B 1 337 ASN 337 1554 1554 ASN ASN B . n 
B 1 338 TYR 338 1555 1555 TYR TYR B . n 
B 1 339 SER 339 1556 1556 SER SER B . n 
B 1 340 PRO 340 1557 1557 PRO PRO B . n 
B 1 341 GLY 341 1558 1558 GLY GLY B . n 
B 1 342 TRP 342 1559 1559 TRP TRP B . n 
B 1 343 LYS 343 1560 1560 LYS LYS B . n 
B 1 344 TYR 344 1561 1561 TYR TYR B . n 
B 1 345 ASN 345 1562 1562 ASN ASN B . n 
B 1 346 HIS 346 1563 1563 HIS HIS B . n 
B 1 347 TRP 347 1564 1564 TRP TRP B . n 
B 1 348 GLU 348 1565 1565 GLU GLU B . n 
B 1 349 LEU 349 1566 1566 LEU LEU B . n 
B 1 350 LYS 350 1567 1567 LYS LYS B . n 
B 1 351 GLY 351 1568 1568 GLY GLY B . n 
B 1 352 VAL 352 1569 1569 VAL VAL B . n 
B 1 353 PRO 353 1570 1570 PRO PRO B . n 
B 1 354 VAL 354 1571 1571 VAL VAL B . n 
B 1 355 ARG 355 1572 1572 ARG ARG B . n 
B 1 356 ILE 356 1573 1573 ILE ILE B . n 
B 1 357 GLU 357 1574 1574 GLU GLU B . n 
B 1 358 LEU 358 1575 1575 LEU LEU B . n 
B 1 359 GLY 359 1576 1576 GLY GLY B . n 
B 1 360 PHE 360 1577 1577 PHE PHE B . n 
B 1 361 LYS 361 1578 1578 LYS LYS B . n 
B 1 362 ASP 362 1579 1579 ASP ASP B . n 
B 1 363 LEU 363 1580 1580 LEU LEU B . n 
B 1 364 GLN 364 1581 1581 GLN GLN B . n 
B 1 365 ASN 365 1582 1582 ASN ASN B . n 
B 1 366 ASP 366 1583 1583 ASP ASP B . n 
B 1 367 GLN 367 1584 1584 GLN GLN B . n 
B 1 368 PHE 368 1585 1585 PHE PHE B . n 
B 1 369 VAL 369 1586 1586 VAL VAL B . n 
B 1 370 ALA 370 1587 1587 ALA ALA B . n 
B 1 371 VAL 371 1588 1588 VAL VAL B . n 
B 1 372 ARG 372 1589 1589 ARG ARG B . n 
B 1 373 ARG 373 1590 1590 ARG ARG B . n 
B 1 374 ASP 374 1591 1591 ASP ASP B . n 
B 1 375 ASN 375 1592 1592 ASN ASN B . n 
B 1 376 GLY 376 1593 1593 GLY GLY B . n 
B 1 377 ALA 377 1594 1594 ALA ALA B . n 
B 1 378 LYS 378 1595 1595 LYS LYS B . n 
B 1 379 GLN 379 1596 1596 GLN GLN B . n 
B 1 380 THR 380 1597 1597 THR THR B . n 
B 1 381 ILE 381 1598 1598 ILE ILE B . n 
B 1 382 LYS 382 1599 1599 LYS LYS B . n 
B 1 383 ARG 383 1600 1600 ARG ARG B . n 
B 1 384 ALA 384 1601 1601 ALA ALA B . n 
B 1 385 GLN 385 1602 1602 GLN GLN B . n 
B 1 386 ALA 386 1603 1603 ALA ALA B . n 
B 1 387 THR 387 1604 1604 THR THR B . n 
B 1 388 VAL 388 1605 1605 VAL VAL B . n 
B 1 389 GLU 389 1606 1606 GLU GLU B . n 
B 1 390 MET 390 1607 1607 MET MET B . n 
B 1 391 PRO 391 1608 1608 PRO PRO B . n 
B 1 392 LYS 392 1609 1609 LYS LYS B . n 
B 1 393 LEU 393 1610 1610 LEU LEU B . n 
B 1 394 LEU 394 1611 1611 LEU LEU B . n 
B 1 395 GLU 395 1612 1612 GLU GLU B . n 
B 1 396 THR 396 1613 1613 THR THR B . n 
B 1 397 ILE 397 1614 1614 ILE ILE B . n 
B 1 398 HIS 398 1615 1615 HIS HIS B . n 
B 1 399 THR 399 1616 1616 THR THR B . n 
B 1 400 SER 400 1617 1617 SER SER B . n 
B 1 401 MET 401 1618 1618 MET MET B . n 
B 1 402 TYR 402 1619 1619 TYR TYR B . n 
B 1 403 GLU 403 1620 1620 GLU GLU B . n 
B 1 404 ARG 404 1621 1621 ARG ARG B . n 
B 1 405 ALA 405 1622 1622 ALA ALA B . n 
B 1 406 GLU 406 1623 1623 GLU GLU B . n 
B 1 407 ARG 407 1624 1624 ARG ARG B . n 
B 1 408 ASP 408 1625 1625 ASP ASP B . n 
B 1 409 LEU 409 1626 1626 LEU LEU B . n 
B 1 410 GLN 410 1627 1627 GLN GLN B . n 
B 1 411 SER 411 1628 1628 SER SER B . n 
B 1 412 HIS 412 1629 1629 HIS HIS B . n 
B 1 413 THR 413 1630 1630 THR THR B . n 
B 1 414 LYS 414 1631 1631 LYS LYS B . n 
B 1 415 LEU 415 1632 1632 LEU LEU B . n 
B 1 416 THR 416 1633 1633 THR THR B . n 
B 1 417 LYS 417 1634 1634 LYS LYS B . n 
B 1 418 GLN 418 1635 1635 GLN GLN B . n 
B 1 419 TRP 419 1636 1636 TRP TRP B . n 
B 1 420 ALA 420 1637 1637 ALA ALA B . n 
B 1 421 GLU 421 1638 1638 GLU GLU B . n 
B 1 422 PHE 422 1639 1639 PHE PHE B . n 
B 1 423 LEU 423 1640 1640 LEU LEU B . n 
B 1 424 GLN 424 1641 1641 GLN GLN B . n 
B 1 425 PHE 425 1642 1642 PHE PHE B . n 
B 1 426 LEU 426 1643 1643 LEU LEU B . n 
B 1 427 GLU 427 1644 1644 GLU GLU B . n 
B 1 428 THR 428 1645 1645 THR THR B . n 
B 1 429 LYS 429 1646 1646 LYS LYS B . n 
B 1 430 ASN 430 1647 1647 ASN ASN B . n 
B 1 431 ILE 431 1648 1648 ILE ILE B . n 
B 1 432 ILE 432 1649 1649 ILE ILE B . n 
B 1 433 MET 433 1650 1650 MET MET B . n 
B 1 434 ALA 434 1651 1651 ALA ALA B . n 
B 1 435 PRO 435 1652 1652 PRO PRO B . n 
B 1 436 PHE 436 1653 1653 PHE PHE B . n 
B 1 437 CYS 437 1654 1654 CYS CYS B . n 
B 1 438 GLY 438 1655 1655 GLY GLY B . n 
B 1 439 GLU 439 1656 1656 GLU GLU B . n 
B 1 440 ILE 440 1657 1657 ILE ILE B . n 
B 1 441 SER 441 1658 1658 SER SER B . n 
B 1 442 CYS 442 1659 1659 CYS CYS B . n 
B 1 443 GLU 443 1660 1660 GLU GLU B . n 
B 1 444 ASP 444 1661 1661 ASP ASP B . n 
B 1 445 ARG 445 1662 1662 ARG ARG B . n 
B 1 446 ILE 446 1663 1663 ILE ILE B . n 
B 1 447 LYS 447 1664 1664 LYS LYS B . n 
B 1 448 ALA 448 1665 1665 ALA ALA B . n 
B 1 449 GLU 449 1666 1666 GLU GLU B . n 
B 1 450 SER 450 1667 1667 SER SER B . n 
B 1 451 ALA 451 1668 1668 ALA ALA B . n 
B 1 452 ARG 452 1669 ?    ?   ?   B . n 
B 1 453 ASP 453 1670 ?    ?   ?   B . n 
B 1 454 ASP 454 1671 ?    ?   ?   B . n 
B 1 455 ALA 455 1672 ?    ?   ?   B . n 
B 1 456 GLU 456 1673 ?    ?   ?   B . n 
B 1 457 ALA 457 1674 ?    ?   ?   B . n 
B 1 458 GLU 458 1675 ?    ?   ?   B . n 
B 1 459 ALA 459 1676 ?    ?   ?   B . n 
B 1 460 GLY 460 1677 ?    ?   ?   B . n 
B 1 461 ALA 461 1678 ?    ?   ?   B . n 
B 1 462 PRO 462 1679 ?    ?   ?   B . n 
B 1 463 ALA 463 1680 ?    ?   ?   B . n 
B 1 464 MET 464 1681 ?    ?   ?   B . n 
B 1 465 GLY 465 1682 1682 GLY GLY B . n 
B 1 466 ALA 466 1683 1683 ALA ALA B . n 
B 1 467 LYS 467 1684 1684 LYS LYS B . n 
B 1 468 SER 468 1685 1685 SER SER B . n 
B 1 469 LEU 469 1686 1686 LEU LEU B . n 
B 1 470 CYS 470 1687 1687 CYS CYS B . n 
B 1 471 ILE 471 1688 1688 ILE ILE B . n 
B 1 472 PRO 472 1689 1689 PRO PRO B . n 
B 1 473 PHE 473 1690 1690 PHE PHE B . n 
B 1 474 GLU 474 1691 1691 GLU GLU B . n 
B 1 475 GLN 475 1692 1692 GLN GLN B . n 
B 1 476 PRO 476 1693 1693 PRO PRO B . n 
B 1 477 ALA 477 1694 1694 ALA ALA B . n 
B 1 478 LYS 478 1695 1695 LYS LYS B . n 
B 1 479 ILE 479 1696 1696 ILE ILE B . n 
B 1 480 ASP 480 1697 1697 ASP ASP B . n 
B 1 481 PRO 481 1698 1698 PRO PRO B . n 
B 1 482 LYS 482 1699 1699 LYS LYS B . n 
B 1 483 VAL 483 1700 1700 VAL VAL B . n 
B 1 484 ASP 484 1701 1701 ASP ASP B . n 
B 1 485 LYS 485 1702 1702 LYS LYS B . n 
B 1 486 CYS 486 1703 1703 CYS CYS B . n 
B 1 487 VAL 487 1704 1704 VAL VAL B . n 
B 1 488 HIS 488 1705 1705 HIS HIS B . n 
B 1 489 PRO 489 1706 1706 PRO PRO B . n 
B 1 490 ALA 490 1707 1707 ALA ALA B . n 
B 1 491 CYS 491 1708 1708 CYS CYS B . n 
B 1 492 GLY 492 1709 1709 GLY GLY B . n 
B 1 493 ARG 493 1710 1710 ARG ARG B . n 
B 1 494 VAL 494 1711 1711 VAL VAL B . n 
B 1 495 ALA 495 1712 1712 ALA ALA B . n 
B 1 496 LYS 496 1713 1713 LYS LYS B . n 
B 1 497 PHE 497 1714 1714 PHE PHE B . n 
B 1 498 TYR 498 1715 1715 TYR TYR B . n 
B 1 499 THR 499 1716 1716 THR THR B . n 
B 1 500 LEU 500 1717 1717 LEU LEU B . n 
B 1 501 PHE 501 1718 1718 PHE PHE B . n 
B 1 502 GLY 502 1719 1719 GLY GLY B . n 
B 1 503 ARG 503 1720 1720 ARG ARG B . n 
B 1 504 SER 504 1721 1721 SER SER B . n 
B 1 505 TYR 505 1722 1722 TYR TYR B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HFG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HFG 
_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 
C 2 HFG 1 1801 1802 HFG HFG A . 
D 3 ZN  1 1802 1803 ZN  ZN  A . 
E 4 CL  1 1803 1805 CL  CL  A . 
F 4 CL  1 1804 1806 CL  CL  A . 
G 5 GOL 1 1805 1807 GOL GOL A . 
H 2 HFG 1 1801 1802 HFG HFG B . 
I 3 ZN  1 1802 1803 ZN  ZN  B . 
J 4 CL  1 1803 1805 CL  CL  B . 
K 5 GOL 1 1804 1806 GOL GOL B . 
L 5 GOL 1 1805 1807 GOL GOL B . 
M 6 HOH 1 1901 1    HOH HOH A . 
M 6 HOH 2 1902 5    HOH HOH A . 
M 6 HOH 3 1903 7    HOH HOH A . 
M 6 HOH 4 1904 6    HOH HOH A . 
M 6 HOH 5 1905 2    HOH HOH A . 
M 6 HOH 6 1906 12   HOH HOH A . 
M 6 HOH 7 1907 8    HOH HOH A . 
M 6 HOH 8 1908 13   HOH HOH A . 
M 6 HOH 9 1909 16   HOH HOH A . 
N 6 HOH 1 1901 4    HOH HOH B . 
N 6 HOH 2 1902 11   HOH HOH B . 
N 6 HOH 3 1903 3    HOH HOH B . 
N 6 HOH 4 1904 15   HOH HOH B . 
N 6 HOH 5 1905 9    HOH HOH B . 
N 6 HOH 6 1906 14   HOH HOH B . 
N 6 HOH 7 1907 10   HOH HOH B . 
# 
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 GLU 1224 ? CG  ? A GLU 7   CG  
2   1 Y 1 A GLU 1224 ? CD  ? A GLU 7   CD  
3   1 Y 1 A GLU 1224 ? OE1 ? A GLU 7   OE1 
4   1 Y 1 A GLU 1224 ? OE2 ? A GLU 7   OE2 
5   1 Y 1 A ARG 1291 ? CG  ? A ARG 74  CG  
6   1 Y 1 A ARG 1291 ? CD  ? A ARG 74  CD  
7   1 Y 1 A ARG 1291 ? NE  ? A ARG 74  NE  
8   1 Y 1 A ARG 1291 ? CZ  ? A ARG 74  CZ  
9   1 Y 1 A ARG 1291 ? NH1 ? A ARG 74  NH1 
10  1 Y 1 A ARG 1291 ? NH2 ? A ARG 74  NH2 
11  1 Y 1 A ARG 1296 ? CG  ? A ARG 79  CG  
12  1 Y 1 A ARG 1296 ? CD  ? A ARG 79  CD  
13  1 Y 1 A ARG 1296 ? NE  ? A ARG 79  NE  
14  1 Y 1 A ARG 1296 ? CZ  ? A ARG 79  CZ  
15  1 Y 1 A ARG 1296 ? NH1 ? A ARG 79  NH1 
16  1 Y 1 A ARG 1296 ? NH2 ? A ARG 79  NH2 
17  1 Y 1 A LYS 1298 ? CG  ? A LYS 81  CG  
18  1 Y 1 A LYS 1298 ? CD  ? A LYS 81  CD  
19  1 Y 1 A LYS 1298 ? CE  ? A LYS 81  CE  
20  1 Y 1 A LYS 1298 ? NZ  ? A LYS 81  NZ  
21  1 Y 1 A HIS 1300 ? CG  ? A HIS 83  CG  
22  1 Y 1 A HIS 1300 ? ND1 ? A HIS 83  ND1 
23  1 Y 1 A HIS 1300 ? CD2 ? A HIS 83  CD2 
24  1 Y 1 A HIS 1300 ? CE1 ? A HIS 83  CE1 
25  1 Y 1 A HIS 1300 ? NE2 ? A HIS 83  NE2 
26  1 Y 1 A ILE 1301 ? CG1 ? A ILE 84  CG1 
27  1 Y 1 A ILE 1301 ? CG2 ? A ILE 84  CG2 
28  1 Y 1 A ILE 1301 ? CD1 ? A ILE 84  CD1 
29  1 Y 1 A ASP 1303 ? CG  ? A ASP 86  CG  
30  1 Y 1 A ASP 1303 ? OD1 ? A ASP 86  OD1 
31  1 Y 1 A ASP 1303 ? OD2 ? A ASP 86  OD2 
32  1 Y 1 A GLU 1318 ? CG  ? A GLU 101 CG  
33  1 Y 1 A GLU 1318 ? CD  ? A GLU 101 CD  
34  1 Y 1 A GLU 1318 ? OE1 ? A GLU 101 OE1 
35  1 Y 1 A GLU 1318 ? OE2 ? A GLU 101 OE2 
36  1 Y 1 A GLU 1321 ? CG  ? A GLU 104 CG  
37  1 Y 1 A GLU 1321 ? CD  ? A GLU 104 CD  
38  1 Y 1 A GLU 1321 ? OE1 ? A GLU 104 OE1 
39  1 Y 1 A GLU 1321 ? OE2 ? A GLU 104 OE2 
40  1 Y 1 A GLN 1342 ? CG  ? A GLN 125 CG  
41  1 Y 1 A GLN 1342 ? CD  ? A GLN 125 CD  
42  1 Y 1 A GLN 1342 ? OE1 ? A GLN 125 OE1 
43  1 Y 1 A GLN 1342 ? NE2 ? A GLN 125 NE2 
44  1 Y 1 A TYR 1344 ? CG  ? A TYR 127 CG  
45  1 Y 1 A TYR 1344 ? CD1 ? A TYR 127 CD1 
46  1 Y 1 A TYR 1344 ? CD2 ? A TYR 127 CD2 
47  1 Y 1 A TYR 1344 ? CE1 ? A TYR 127 CE1 
48  1 Y 1 A TYR 1344 ? CE2 ? A TYR 127 CE2 
49  1 Y 1 A TYR 1344 ? CZ  ? A TYR 127 CZ  
50  1 Y 1 A TYR 1344 ? OH  ? A TYR 127 OH  
51  1 Y 1 A ARG 1345 ? CZ  ? A ARG 128 CZ  
52  1 Y 1 A ARG 1345 ? NH1 ? A ARG 128 NH1 
53  1 Y 1 A ARG 1345 ? NH2 ? A ARG 128 NH2 
54  1 Y 1 A PHE 1362 ? CG  ? A PHE 145 CG  
55  1 Y 1 A PHE 1362 ? CD1 ? A PHE 145 CD1 
56  1 Y 1 A PHE 1362 ? CD2 ? A PHE 145 CD2 
57  1 Y 1 A PHE 1362 ? CE1 ? A PHE 145 CE1 
58  1 Y 1 A PHE 1362 ? CE2 ? A PHE 145 CE2 
59  1 Y 1 A PHE 1362 ? CZ  ? A PHE 145 CZ  
60  1 Y 1 A LYS 1363 ? CG  ? A LYS 146 CG  
61  1 Y 1 A LYS 1363 ? CD  ? A LYS 146 CD  
62  1 Y 1 A LYS 1363 ? CE  ? A LYS 146 CE  
63  1 Y 1 A LYS 1363 ? NZ  ? A LYS 146 NZ  
64  1 Y 1 A ARG 1370 ? CD  ? A ARG 153 CD  
65  1 Y 1 A ARG 1370 ? NE  ? A ARG 153 NE  
66  1 Y 1 A ARG 1370 ? CZ  ? A ARG 153 CZ  
67  1 Y 1 A ARG 1370 ? NH1 ? A ARG 153 NH1 
68  1 Y 1 A ARG 1370 ? NH2 ? A ARG 153 NH2 
69  1 Y 1 A ILE 1436 ? CG1 ? A ILE 219 CG1 
70  1 Y 1 A ILE 1436 ? CG2 ? A ILE 219 CG2 
71  1 Y 1 A ILE 1436 ? CD1 ? A ILE 219 CD1 
72  1 Y 1 A HIS 1465 ? CG  ? A HIS 248 CG  
73  1 Y 1 A HIS 1465 ? ND1 ? A HIS 248 ND1 
74  1 Y 1 A HIS 1465 ? CD2 ? A HIS 248 CD2 
75  1 Y 1 A HIS 1465 ? CE1 ? A HIS 248 CE1 
76  1 Y 1 A HIS 1465 ? NE2 ? A HIS 248 NE2 
77  1 Y 1 A GLU 1467 ? CG  ? A GLU 250 CG  
78  1 Y 1 A GLU 1467 ? CD  ? A GLU 250 CD  
79  1 Y 1 A GLU 1467 ? OE1 ? A GLU 250 OE1 
80  1 Y 1 A GLU 1467 ? OE2 ? A GLU 250 OE2 
81  1 Y 1 A THR 1468 ? OG1 ? A THR 251 OG1 
82  1 Y 1 A THR 1468 ? CG2 ? A THR 251 CG2 
83  1 Y 1 A LYS 1469 ? CG  ? A LYS 252 CG  
84  1 Y 1 A LYS 1469 ? CD  ? A LYS 252 CD  
85  1 Y 1 A LYS 1469 ? CE  ? A LYS 252 CE  
86  1 Y 1 A LYS 1469 ? NZ  ? A LYS 252 NZ  
87  1 Y 1 A GLU 1470 ? CG  ? A GLU 253 CG  
88  1 Y 1 A GLU 1470 ? CD  ? A GLU 253 CD  
89  1 Y 1 A GLU 1470 ? OE1 ? A GLU 253 OE1 
90  1 Y 1 A GLU 1470 ? OE2 ? A GLU 253 OE2 
91  1 Y 1 A LYS 1471 ? CG  ? A LYS 254 CG  
92  1 Y 1 A LYS 1471 ? CD  ? A LYS 254 CD  
93  1 Y 1 A LYS 1471 ? CE  ? A LYS 254 CE  
94  1 Y 1 A LYS 1471 ? NZ  ? A LYS 254 NZ  
95  1 Y 1 A GLN 1497 ? CG  ? A GLN 280 CG  
96  1 Y 1 A GLN 1497 ? CD  ? A GLN 280 CD  
97  1 Y 1 A GLN 1497 ? OE1 ? A GLN 280 OE1 
98  1 Y 1 A GLN 1497 ? NE2 ? A GLN 280 NE2 
99  1 Y 1 A THR 1518 ? OG1 ? A THR 301 OG1 
100 1 Y 1 A THR 1518 ? CG2 ? A THR 301 CG2 
101 1 Y 1 A THR 1521 ? OG1 ? A THR 304 OG1 
102 1 Y 1 A THR 1521 ? CG2 ? A THR 304 CG2 
103 1 Y 1 A THR 1522 ? OG1 ? A THR 305 OG1 
104 1 Y 1 A THR 1522 ? CG2 ? A THR 305 CG2 
105 1 Y 1 A ARG 1527 ? CG  ? A ARG 310 CG  
106 1 Y 1 A ARG 1527 ? CD  ? A ARG 310 CD  
107 1 Y 1 A ARG 1527 ? NE  ? A ARG 310 NE  
108 1 Y 1 A ARG 1527 ? CZ  ? A ARG 310 CZ  
109 1 Y 1 A ARG 1527 ? NH1 ? A ARG 310 NH1 
110 1 Y 1 A ARG 1527 ? NH2 ? A ARG 310 NH2 
111 1 Y 1 A ARG 1528 ? CG  ? A ARG 311 CG  
112 1 Y 1 A ARG 1528 ? CD  ? A ARG 311 CD  
113 1 Y 1 A ARG 1528 ? NE  ? A ARG 311 NE  
114 1 Y 1 A ARG 1528 ? CZ  ? A ARG 311 CZ  
115 1 Y 1 A ARG 1528 ? NH1 ? A ARG 311 NH1 
116 1 Y 1 A ARG 1528 ? NH2 ? A ARG 311 NH2 
117 1 Y 1 A GLU 1531 ? CG  ? A GLU 314 CG  
118 1 Y 1 A GLU 1531 ? CD  ? A GLU 314 CD  
119 1 Y 1 A GLU 1531 ? OE1 ? A GLU 314 OE1 
120 1 Y 1 A GLU 1531 ? OE2 ? A GLU 314 OE2 
121 1 Y 1 A LYS 1542 ? CG  ? A LYS 325 CG  
122 1 Y 1 A LYS 1542 ? CD  ? A LYS 325 CD  
123 1 Y 1 A LYS 1542 ? CE  ? A LYS 325 CE  
124 1 Y 1 A LYS 1542 ? NZ  ? A LYS 325 NZ  
125 1 Y 1 A GLU 1548 ? CG  ? A GLU 331 CG  
126 1 Y 1 A GLU 1548 ? CD  ? A GLU 331 CD  
127 1 Y 1 A GLU 1548 ? OE1 ? A GLU 331 OE1 
128 1 Y 1 A GLU 1548 ? OE2 ? A GLU 331 OE2 
129 1 Y 1 A LYS 1578 ? CG  ? A LYS 361 CG  
130 1 Y 1 A LYS 1578 ? CD  ? A LYS 361 CD  
131 1 Y 1 A LYS 1578 ? CE  ? A LYS 361 CE  
132 1 Y 1 A LYS 1578 ? NZ  ? A LYS 361 NZ  
133 1 Y 1 A GLN 1581 ? CG  ? A GLN 364 CG  
134 1 Y 1 A GLN 1581 ? CD  ? A GLN 364 CD  
135 1 Y 1 A GLN 1581 ? OE1 ? A GLN 364 OE1 
136 1 Y 1 A GLN 1581 ? NE2 ? A GLN 364 NE2 
137 1 Y 1 A LYS 1599 ? CG  ? A LYS 382 CG  
138 1 Y 1 A LYS 1599 ? CD  ? A LYS 382 CD  
139 1 Y 1 A LYS 1599 ? CE  ? A LYS 382 CE  
140 1 Y 1 A LYS 1599 ? NZ  ? A LYS 382 NZ  
141 1 Y 1 A LYS 1609 ? CG  ? A LYS 392 CG  
142 1 Y 1 A LYS 1609 ? CD  ? A LYS 392 CD  
143 1 Y 1 A LYS 1609 ? CE  ? A LYS 392 CE  
144 1 Y 1 A LYS 1609 ? NZ  ? A LYS 392 NZ  
145 1 Y 1 A GLU 1612 ? OE1 ? A GLU 395 OE1 
146 1 Y 1 A GLU 1612 ? OE2 ? A GLU 395 OE2 
147 1 Y 1 A LYS 1631 ? CG  ? A LYS 414 CG  
148 1 Y 1 A LYS 1631 ? CD  ? A LYS 414 CD  
149 1 Y 1 A LYS 1631 ? CE  ? A LYS 414 CE  
150 1 Y 1 A LYS 1631 ? NZ  ? A LYS 414 NZ  
151 1 Y 1 A LEU 1632 ? CG  ? A LEU 415 CG  
152 1 Y 1 A LEU 1632 ? CD1 ? A LEU 415 CD1 
153 1 Y 1 A LEU 1632 ? CD2 ? A LEU 415 CD2 
154 1 Y 1 A THR 1633 ? OG1 ? A THR 416 OG1 
155 1 Y 1 A THR 1633 ? CG2 ? A THR 416 CG2 
156 1 Y 1 A GLN 1635 ? CG  ? A GLN 418 CG  
157 1 Y 1 A GLN 1635 ? CD  ? A GLN 418 CD  
158 1 Y 1 A GLN 1635 ? OE1 ? A GLN 418 OE1 
159 1 Y 1 A GLN 1635 ? NE2 ? A GLN 418 NE2 
160 1 Y 1 A GLN 1641 ? CG  ? A GLN 424 CG  
161 1 Y 1 A GLN 1641 ? CD  ? A GLN 424 CD  
162 1 Y 1 A GLN 1641 ? OE1 ? A GLN 424 OE1 
163 1 Y 1 A GLN 1641 ? NE2 ? A GLN 424 NE2 
164 1 Y 1 A GLU 1644 ? CG  ? A GLU 427 CG  
165 1 Y 1 A GLU 1644 ? CD  ? A GLU 427 CD  
166 1 Y 1 A GLU 1644 ? OE1 ? A GLU 427 OE1 
167 1 Y 1 A GLU 1644 ? OE2 ? A GLU 427 OE2 
168 1 Y 1 A LYS 1646 ? CG  ? A LYS 429 CG  
169 1 Y 1 A LYS 1646 ? CD  ? A LYS 429 CD  
170 1 Y 1 A LYS 1646 ? CE  ? A LYS 429 CE  
171 1 Y 1 A LYS 1646 ? NZ  ? A LYS 429 NZ  
172 1 Y 1 A ARG 1662 ? CG  ? A ARG 445 CG  
173 1 Y 1 A ARG 1662 ? CD  ? A ARG 445 CD  
174 1 Y 1 A ARG 1662 ? NE  ? A ARG 445 NE  
175 1 Y 1 A ARG 1662 ? CZ  ? A ARG 445 CZ  
176 1 Y 1 A ARG 1662 ? NH1 ? A ARG 445 NH1 
177 1 Y 1 A ARG 1662 ? NH2 ? A ARG 445 NH2 
178 1 Y 1 A LYS 1684 ? CG  ? A LYS 467 CG  
179 1 Y 1 A LYS 1684 ? CD  ? A LYS 467 CD  
180 1 Y 1 A LYS 1684 ? CE  ? A LYS 467 CE  
181 1 Y 1 A LYS 1684 ? NZ  ? A LYS 467 NZ  
182 1 Y 1 A GLU 1691 ? CG  ? A GLU 474 CG  
183 1 Y 1 A GLU 1691 ? CD  ? A GLU 474 CD  
184 1 Y 1 A GLU 1691 ? OE1 ? A GLU 474 OE1 
185 1 Y 1 A GLU 1691 ? OE2 ? A GLU 474 OE2 
186 1 Y 1 A LYS 1695 ? CG  ? A LYS 478 CG  
187 1 Y 1 A LYS 1695 ? CD  ? A LYS 478 CD  
188 1 Y 1 A LYS 1695 ? CE  ? A LYS 478 CE  
189 1 Y 1 A LYS 1695 ? NZ  ? A LYS 478 NZ  
190 1 Y 1 A ILE 1696 ? CG1 ? A ILE 479 CG1 
191 1 Y 1 A ILE 1696 ? CG2 ? A ILE 479 CG2 
192 1 Y 1 A ILE 1696 ? CD1 ? A ILE 479 CD1 
193 1 Y 1 A ASP 1697 ? CG  ? A ASP 480 CG  
194 1 Y 1 A ASP 1697 ? OD1 ? A ASP 480 OD1 
195 1 Y 1 A ASP 1697 ? OD2 ? A ASP 480 OD2 
196 1 Y 1 A LYS 1699 ? CG  ? A LYS 482 CG  
197 1 Y 1 A LYS 1699 ? CD  ? A LYS 482 CD  
198 1 Y 1 A LYS 1699 ? CE  ? A LYS 482 CE  
199 1 Y 1 A LYS 1699 ? NZ  ? A LYS 482 NZ  
200 1 Y 1 A LYS 1702 ? CG  ? A LYS 485 CG  
201 1 Y 1 A LYS 1702 ? CD  ? A LYS 485 CD  
202 1 Y 1 A LYS 1702 ? CE  ? A LYS 485 CE  
203 1 Y 1 A LYS 1702 ? NZ  ? A LYS 485 NZ  
204 1 Y 1 A ARG 1710 ? CG  ? A ARG 493 CG  
205 1 Y 1 A ARG 1710 ? CD  ? A ARG 493 CD  
206 1 Y 1 A ARG 1710 ? NE  ? A ARG 493 NE  
207 1 Y 1 A ARG 1710 ? CZ  ? A ARG 493 CZ  
208 1 Y 1 A ARG 1710 ? NH1 ? A ARG 493 NH1 
209 1 Y 1 A ARG 1710 ? NH2 ? A ARG 493 NH2 
210 1 Y 1 A VAL 1711 ? CG1 ? A VAL 494 CG1 
211 1 Y 1 A VAL 1711 ? CG2 ? A VAL 494 CG2 
212 1 Y 1 A LYS 1713 ? CG  ? A LYS 496 CG  
213 1 Y 1 A LYS 1713 ? CD  ? A LYS 496 CD  
214 1 Y 1 A LYS 1713 ? CE  ? A LYS 496 CE  
215 1 Y 1 A LYS 1713 ? NZ  ? A LYS 496 NZ  
216 1 Y 1 B GLU 1224 ? CG  ? B GLU 7   CG  
217 1 Y 1 B GLU 1224 ? CD  ? B GLU 7   CD  
218 1 Y 1 B GLU 1224 ? OE1 ? B GLU 7   OE1 
219 1 Y 1 B GLU 1224 ? OE2 ? B GLU 7   OE2 
220 1 Y 1 B ARG 1291 ? CG  ? B ARG 74  CG  
221 1 Y 1 B ARG 1291 ? CD  ? B ARG 74  CD  
222 1 Y 1 B ARG 1291 ? NE  ? B ARG 74  NE  
223 1 Y 1 B ARG 1291 ? CZ  ? B ARG 74  CZ  
224 1 Y 1 B ARG 1291 ? NH1 ? B ARG 74  NH1 
225 1 Y 1 B ARG 1291 ? NH2 ? B ARG 74  NH2 
226 1 Y 1 B ARG 1296 ? CG  ? B ARG 79  CG  
227 1 Y 1 B ARG 1296 ? CD  ? B ARG 79  CD  
228 1 Y 1 B ARG 1296 ? NE  ? B ARG 79  NE  
229 1 Y 1 B ARG 1296 ? CZ  ? B ARG 79  CZ  
230 1 Y 1 B ARG 1296 ? NH1 ? B ARG 79  NH1 
231 1 Y 1 B ARG 1296 ? NH2 ? B ARG 79  NH2 
232 1 Y 1 B ASP 1303 ? CG  ? B ASP 86  CG  
233 1 Y 1 B ASP 1303 ? OD1 ? B ASP 86  OD1 
234 1 Y 1 B ASP 1303 ? OD2 ? B ASP 86  OD2 
235 1 Y 1 B GLU 1307 ? CG  ? B GLU 90  CG  
236 1 Y 1 B GLU 1307 ? CD  ? B GLU 90  CD  
237 1 Y 1 B GLU 1307 ? OE1 ? B GLU 90  OE1 
238 1 Y 1 B GLU 1307 ? OE2 ? B GLU 90  OE2 
239 1 Y 1 B GLU 1321 ? CG  ? B GLU 104 CG  
240 1 Y 1 B GLU 1321 ? CD  ? B GLU 104 CD  
241 1 Y 1 B GLU 1321 ? OE1 ? B GLU 104 OE1 
242 1 Y 1 B GLU 1321 ? OE2 ? B GLU 104 OE2 
243 1 Y 1 B GLN 1342 ? CG  ? B GLN 125 CG  
244 1 Y 1 B GLN 1342 ? CD  ? B GLN 125 CD  
245 1 Y 1 B GLN 1342 ? OE1 ? B GLN 125 OE1 
246 1 Y 1 B GLN 1342 ? NE2 ? B GLN 125 NE2 
247 1 Y 1 B LYS 1363 ? CG  ? B LYS 146 CG  
248 1 Y 1 B LYS 1363 ? CD  ? B LYS 146 CD  
249 1 Y 1 B LYS 1363 ? CE  ? B LYS 146 CE  
250 1 Y 1 B LYS 1363 ? NZ  ? B LYS 146 NZ  
251 1 Y 1 B HIS 1364 ? CG  ? B HIS 147 CG  
252 1 Y 1 B HIS 1364 ? ND1 ? B HIS 147 ND1 
253 1 Y 1 B HIS 1364 ? CD2 ? B HIS 147 CD2 
254 1 Y 1 B HIS 1364 ? CE1 ? B HIS 147 CE1 
255 1 Y 1 B HIS 1364 ? NE2 ? B HIS 147 NE2 
256 1 Y 1 B ILE 1436 ? CG1 ? B ILE 219 CG1 
257 1 Y 1 B ILE 1436 ? CG2 ? B ILE 219 CG2 
258 1 Y 1 B ILE 1436 ? CD1 ? B ILE 219 CD1 
259 1 Y 1 B MET 1458 ? CG  ? B MET 241 CG  
260 1 Y 1 B MET 1458 ? SD  ? B MET 241 SD  
261 1 Y 1 B MET 1458 ? CE  ? B MET 241 CE  
262 1 Y 1 B VAL 1462 ? CG1 ? B VAL 245 CG1 
263 1 Y 1 B VAL 1462 ? CG2 ? B VAL 245 CG2 
264 1 Y 1 B GLU 1467 ? CG  ? B GLU 250 CG  
265 1 Y 1 B GLU 1467 ? CD  ? B GLU 250 CD  
266 1 Y 1 B GLU 1467 ? OE1 ? B GLU 250 OE1 
267 1 Y 1 B GLU 1467 ? OE2 ? B GLU 250 OE2 
268 1 Y 1 B THR 1468 ? OG1 ? B THR 251 OG1 
269 1 Y 1 B THR 1468 ? CG2 ? B THR 251 CG2 
270 1 Y 1 B LYS 1469 ? CG  ? B LYS 252 CG  
271 1 Y 1 B LYS 1469 ? CD  ? B LYS 252 CD  
272 1 Y 1 B LYS 1469 ? CE  ? B LYS 252 CE  
273 1 Y 1 B LYS 1469 ? NZ  ? B LYS 252 NZ  
274 1 Y 1 B GLU 1470 ? CG  ? B GLU 253 CG  
275 1 Y 1 B GLU 1470 ? CD  ? B GLU 253 CD  
276 1 Y 1 B GLU 1470 ? OE1 ? B GLU 253 OE1 
277 1 Y 1 B GLU 1470 ? OE2 ? B GLU 253 OE2 
278 1 Y 1 B LYS 1471 ? CG  ? B LYS 254 CG  
279 1 Y 1 B LYS 1471 ? CD  ? B LYS 254 CD  
280 1 Y 1 B LYS 1471 ? CE  ? B LYS 254 CE  
281 1 Y 1 B LYS 1471 ? NZ  ? B LYS 254 NZ  
282 1 Y 1 B ILE 1517 ? CG1 ? B ILE 300 CG1 
283 1 Y 1 B ILE 1517 ? CG2 ? B ILE 300 CG2 
284 1 Y 1 B ILE 1517 ? CD1 ? B ILE 300 CD1 
285 1 Y 1 B THR 1518 ? OG1 ? B THR 301 OG1 
286 1 Y 1 B THR 1518 ? CG2 ? B THR 301 CG2 
287 1 Y 1 B THR 1520 ? OG1 ? B THR 303 OG1 
288 1 Y 1 B THR 1520 ? CG2 ? B THR 303 CG2 
289 1 Y 1 B THR 1521 ? OG1 ? B THR 304 OG1 
290 1 Y 1 B THR 1521 ? CG2 ? B THR 304 CG2 
291 1 Y 1 B THR 1522 ? OG1 ? B THR 305 OG1 
292 1 Y 1 B THR 1522 ? CG2 ? B THR 305 CG2 
293 1 Y 1 B ASP 1524 ? CG  ? B ASP 307 CG  
294 1 Y 1 B ASP 1524 ? OD1 ? B ASP 307 OD1 
295 1 Y 1 B ASP 1524 ? OD2 ? B ASP 307 OD2 
296 1 Y 1 B ARG 1526 ? CG  ? B ARG 309 CG  
297 1 Y 1 B ARG 1526 ? CD  ? B ARG 309 CD  
298 1 Y 1 B ARG 1526 ? NE  ? B ARG 309 NE  
299 1 Y 1 B ARG 1526 ? CZ  ? B ARG 309 CZ  
300 1 Y 1 B ARG 1526 ? NH1 ? B ARG 309 NH1 
301 1 Y 1 B ARG 1526 ? NH2 ? B ARG 309 NH2 
302 1 Y 1 B ARG 1528 ? CG  ? B ARG 311 CG  
303 1 Y 1 B ARG 1528 ? CD  ? B ARG 311 CD  
304 1 Y 1 B ARG 1528 ? NE  ? B ARG 311 NE  
305 1 Y 1 B ARG 1528 ? CZ  ? B ARG 311 CZ  
306 1 Y 1 B ARG 1528 ? NH1 ? B ARG 311 NH1 
307 1 Y 1 B ARG 1528 ? NH2 ? B ARG 311 NH2 
308 1 Y 1 B ARG 1534 ? CG  ? B ARG 317 CG  
309 1 Y 1 B ARG 1534 ? CD  ? B ARG 317 CD  
310 1 Y 1 B ARG 1534 ? NE  ? B ARG 317 NE  
311 1 Y 1 B ARG 1534 ? CZ  ? B ARG 317 CZ  
312 1 Y 1 B ARG 1534 ? NH1 ? B ARG 317 NH1 
313 1 Y 1 B ARG 1534 ? NH2 ? B ARG 317 NH2 
314 1 Y 1 B GLU 1535 ? CG  ? B GLU 318 CG  
315 1 Y 1 B GLU 1535 ? CD  ? B GLU 318 CD  
316 1 Y 1 B GLU 1535 ? OE1 ? B GLU 318 OE1 
317 1 Y 1 B GLU 1535 ? OE2 ? B GLU 318 OE2 
318 1 Y 1 B GLU 1548 ? CG  ? B GLU 331 CG  
319 1 Y 1 B GLU 1548 ? CD  ? B GLU 331 CD  
320 1 Y 1 B GLU 1548 ? OE1 ? B GLU 331 OE1 
321 1 Y 1 B GLU 1548 ? OE2 ? B GLU 331 OE2 
322 1 Y 1 B LYS 1578 ? CG  ? B LYS 361 CG  
323 1 Y 1 B LYS 1578 ? CD  ? B LYS 361 CD  
324 1 Y 1 B LYS 1578 ? CE  ? B LYS 361 CE  
325 1 Y 1 B LYS 1578 ? NZ  ? B LYS 361 NZ  
326 1 Y 1 B LEU 1580 ? CG  ? B LEU 363 CG  
327 1 Y 1 B LEU 1580 ? CD1 ? B LEU 363 CD1 
328 1 Y 1 B LEU 1580 ? CD2 ? B LEU 363 CD2 
329 1 Y 1 B GLN 1602 ? CG  ? B GLN 385 CG  
330 1 Y 1 B GLN 1602 ? CD  ? B GLN 385 CD  
331 1 Y 1 B GLN 1602 ? OE1 ? B GLN 385 OE1 
332 1 Y 1 B GLN 1602 ? NE2 ? B GLN 385 NE2 
333 1 Y 1 B LYS 1609 ? CG  ? B LYS 392 CG  
334 1 Y 1 B LYS 1609 ? CD  ? B LYS 392 CD  
335 1 Y 1 B LYS 1609 ? CE  ? B LYS 392 CE  
336 1 Y 1 B LYS 1609 ? NZ  ? B LYS 392 NZ  
337 1 Y 1 B GLU 1612 ? OE1 ? B GLU 395 OE1 
338 1 Y 1 B GLU 1612 ? OE2 ? B GLU 395 OE2 
339 1 Y 1 B SER 1617 ? OG  ? B SER 400 OG  
340 1 Y 1 B LYS 1631 ? CG  ? B LYS 414 CG  
341 1 Y 1 B LYS 1631 ? CD  ? B LYS 414 CD  
342 1 Y 1 B LYS 1631 ? CE  ? B LYS 414 CE  
343 1 Y 1 B LYS 1631 ? NZ  ? B LYS 414 NZ  
344 1 Y 1 B GLN 1641 ? CG  ? B GLN 424 CG  
345 1 Y 1 B GLN 1641 ? CD  ? B GLN 424 CD  
346 1 Y 1 B GLN 1641 ? OE1 ? B GLN 424 OE1 
347 1 Y 1 B GLN 1641 ? NE2 ? B GLN 424 NE2 
348 1 Y 1 B GLU 1644 ? CG  ? B GLU 427 CG  
349 1 Y 1 B GLU 1644 ? CD  ? B GLU 427 CD  
350 1 Y 1 B GLU 1644 ? OE1 ? B GLU 427 OE1 
351 1 Y 1 B GLU 1644 ? OE2 ? B GLU 427 OE2 
352 1 Y 1 B LYS 1646 ? CG  ? B LYS 429 CG  
353 1 Y 1 B LYS 1646 ? CD  ? B LYS 429 CD  
354 1 Y 1 B LYS 1646 ? CE  ? B LYS 429 CE  
355 1 Y 1 B LYS 1646 ? NZ  ? B LYS 429 NZ  
356 1 Y 1 B MET 1650 ? CE  ? B MET 433 CE  
357 1 Y 1 B SER 1658 ? OG  ? B SER 441 OG  
358 1 Y 1 B ARG 1662 ? CG  ? B ARG 445 CG  
359 1 Y 1 B ARG 1662 ? CD  ? B ARG 445 CD  
360 1 Y 1 B ARG 1662 ? NE  ? B ARG 445 NE  
361 1 Y 1 B ARG 1662 ? CZ  ? B ARG 445 CZ  
362 1 Y 1 B ARG 1662 ? NH1 ? B ARG 445 NH1 
363 1 Y 1 B ARG 1662 ? NH2 ? B ARG 445 NH2 
364 1 Y 1 B LYS 1684 ? CG  ? B LYS 467 CG  
365 1 Y 1 B LYS 1684 ? CD  ? B LYS 467 CD  
366 1 Y 1 B LYS 1684 ? CE  ? B LYS 467 CE  
367 1 Y 1 B LYS 1684 ? NZ  ? B LYS 467 NZ  
368 1 Y 1 B LYS 1695 ? CG  ? B LYS 478 CG  
369 1 Y 1 B LYS 1695 ? CD  ? B LYS 478 CD  
370 1 Y 1 B LYS 1695 ? CE  ? B LYS 478 CE  
371 1 Y 1 B LYS 1695 ? NZ  ? B LYS 478 NZ  
372 1 Y 1 B ILE 1696 ? CG1 ? B ILE 479 CG1 
373 1 Y 1 B ILE 1696 ? CG2 ? B ILE 479 CG2 
374 1 Y 1 B ILE 1696 ? CD1 ? B ILE 479 CD1 
375 1 Y 1 B ASP 1697 ? CG  ? B ASP 480 CG  
376 1 Y 1 B ASP 1697 ? OD1 ? B ASP 480 OD1 
377 1 Y 1 B ASP 1697 ? OD2 ? B ASP 480 OD2 
378 1 Y 1 B LYS 1699 ? CG  ? B LYS 482 CG  
379 1 Y 1 B LYS 1699 ? CD  ? B LYS 482 CD  
380 1 Y 1 B LYS 1699 ? CE  ? B LYS 482 CE  
381 1 Y 1 B LYS 1699 ? NZ  ? B LYS 482 NZ  
382 1 Y 1 B VAL 1711 ? CG1 ? B VAL 494 CG1 
383 1 Y 1 B VAL 1711 ? CG2 ? B VAL 494 CG2 
384 1 Y 1 B LYS 1713 ? CG  ? B LYS 496 CG  
385 1 Y 1 B LYS 1713 ? CD  ? B LYS 496 CD  
386 1 Y 1 B LYS 1713 ? CE  ? B LYS 496 CE  
387 1 Y 1 B LYS 1713 ? NZ  ? B LYS 496 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.15rc1_3423: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                     2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                     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                     8JE5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     81.129 
_cell.length_a_esd                 ? 
_cell.length_b                     114.473 
_cell.length_b_esd                 ? 
_cell.length_c                     120.463 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8JE5 
_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                   8JE5 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.41 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.90 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M Sodium chloride, 0.1 M Sodium HEPES  and 25% w/v PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_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 EIGER2 XE 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-10-05 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9763 
_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                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9763 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8JE5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.57 
_reflns.d_resolution_low                               82.98 
_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                                     33971 
_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                           93.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.168 
_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                                   1 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.57 
_reflns_shell.d_res_low                                     2.62 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1806 
_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                               14.2 
_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                               5.641 
_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                                  0.4 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8JE5 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.570 
_refine.ls_d_res_low                             57.237 
_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                     33521 
_refine.ls_number_reflns_R_free                  1602 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.03 
_refine.ls_percent_reflns_R_free                 4.78 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2091 
_refine.ls_R_factor_R_free                       0.2802 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2056 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      7F9A 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 35.98 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.49 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        7503 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         71 
_refine_hist.number_atoms_solvent             16 
_refine_hist.number_atoms_total               7590 
_refine_hist.d_res_high                       2.570 
_refine_hist.d_res_low                        57.237 
# 
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' ? 0.009 ? 7777  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.165 ? 10597 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 4.692 ? 4584  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.063 ? 1161  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009 ? 1393  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.5704 2.6534 . . 152 2533 90.00  . . . . 0.3774 . . . . . . . . . . . 0.3887 
'X-RAY DIFFRACTION' 2.6534 2.7482 . . 97  2051 94.00  . . . . 0.3525 . . . . . . . . . . . 0.4387 
'X-RAY DIFFRACTION' 2.7482 2.8582 . . 159 3107 100.00 . . . . 0.3392 . . . . . . . . . . . 0.4177 
'X-RAY DIFFRACTION' 2.8582 2.9883 . . 165 3100 100.00 . . . . 0.3056 . . . . . . . . . . . 0.3938 
'X-RAY DIFFRACTION' 2.9883 3.1459 . . 171 3103 100.00 . . . . 0.2785 . . . . . . . . . . . 0.3864 
'X-RAY DIFFRACTION' 3.1459 3.3429 . . 146 3135 100.00 . . . . 0.2468 . . . . . . . . . . . 0.3617 
'X-RAY DIFFRACTION' 3.3429 3.6010 . . 131 2667 85.00  . . . . 0.2240 . . . . . . . . . . . 0.3419 
'X-RAY DIFFRACTION' 3.6010 3.9633 . . 118 2486 79.00  . . . . 0.1908 . . . . . . . . . . . 0.2741 
'X-RAY DIFFRACTION' 3.9633 4.5366 . . 169 3164 100.00 . . . . 0.1644 . . . . . . . . . . . 0.2394 
'X-RAY DIFFRACTION' 4.5366 5.7148 . . 151 3203 100.00 . . . . 0.1598 . . . . . . . . . . . 0.2153 
'X-RAY DIFFRACTION' 5.7148 57.237 . . 143 3370 100.00 . . . . 0.1842 . . . . . . . . . . . 0.2320 
# 
_struct.entry_id                     8JE5 
_struct.title                        
'Crystal Structure of Anopheles culicifacies Prolyl-tRNA Synthetase (AcPRS) in complex with Halofuginone' 
_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        8JE5 
_struct_keywords.text            
'Malaria, Vector, Anopheles, Mosquito, Larvicidal, Aminoacyl-tRNA synthetase, LIGASE, LIGASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   LIGASE/INHIBITOR 
# 
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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L N N 5 ? 
M N N 6 ? 
N N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A182M1F8_9DIPT 
_struct_ref.pdbx_db_accession          A0A182M1F8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TRLGLEATKEDNLPDWYSQVITKGEMIEYYDVSGCYILRHWSFAIWKAIRNWFDAEITRLGVKECYFPIFVSRAALEREK
THIADFAPEVAWVTKSGDSELAEPIAVRPTSETVMYPAYAKWIQSYRDLPIRLNQWNNVVRWEFKHPQPFLRTREFLWQE
GHTAFATQKEADEEVLTILDLYAKVYTDLLAIPVVKGRKTEKEKFAGGDYTTTVEAYISASGRAIQGATSHHLGQNFSRM
FDIVYEHPETKEKEYVFQNSWGITTRTIGVMIMVHADNQGLVLPPRVACIQVVIVPCGITATTTDDERRRLYESCRELEQ
TFVKAGIRCEGDYRDNYSPGWKYNHWELKGVPVRIELGFKDLQNDQFVAVRRDNGAKQTIKRAQATVEMPKLLETIHTSM
YERAERDLQSHTKLTKQWAEFLQFLETKNIIMAPFCGEISCEDRIKAESARDDAEAEAGAPAMGAKSLCIPFEQPAKIDP
KVDKCVHPACGRVAKFYTLFGRSY
;
_struct_ref.pdbx_align_begin           1219 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8JE5 A 2 ? 505 ? A0A182M1F8 1219 ? 1722 ? 1219 1722 
2 1 8JE5 B 2 ? 505 ? A0A182M1F8 1219 ? 1722 ? 1219 1722 
# 
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 8JE5 MET A 1 ? UNP A0A182M1F8 ? ? 'initiating methionine' 1218 1 
2 8JE5 MET B 1 ? UNP A0A182M1F8 ? ? 'initiating methionine' 1218 2 
# 
_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   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 5900  ? 
1 MORE         -57   ? 
1 'SSA (A^2)'  37710 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
_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 ASN A 13  ? GLY A 25  ? ASN A 1230 GLY A 1242 1 ? 13 
HELX_P HELX_P2  AA2 ARG A 40  ? GLY A 62  ? ARG A 1257 GLY A 1279 1 ? 23 
HELX_P HELX_P3  AA3 SER A 73  ? ARG A 79  ? SER A 1290 ARG A 1296 1 ? 7  
HELX_P HELX_P4  AA4 PHE A 87  ? GLU A 90  ? PHE A 1304 GLU A 1307 5 ? 4  
HELX_P HELX_P5  AA5 SER A 112 ? ILE A 124 ? SER A 1329 ILE A 1341 1 ? 13 
HELX_P HELX_P6  AA6 SER A 126 ? LEU A 130 ? SER A 1343 LEU A 1347 5 ? 5  
HELX_P HELX_P7  AA7 THR A 168 ? LEU A 190 ? THR A 1385 LEU A 1407 1 ? 23 
HELX_P HELX_P8  AA8 GLN A 236 ? ASP A 243 ? GLN A 1453 ASP A 1460 1 ? 8  
HELX_P HELX_P9  AA9 THR A 266 ? ALA A 277 ? THR A 1483 ALA A 1494 1 ? 12 
HELX_P HELX_P10 AB1 THR A 305 ? ALA A 326 ? THR A 1522 ALA A 1543 1 ? 22 
HELX_P HELX_P11 AB2 SER A 339 ? GLY A 351 ? SER A 1556 GLY A 1568 1 ? 13 
HELX_P HELX_P12 AB3 GLY A 359 ? ASN A 365 ? GLY A 1576 ASN A 1582 1 ? 7  
HELX_P HELX_P13 AB4 GLN A 385 ? HIS A 412 ? GLN A 1602 HIS A 1629 1 ? 28 
HELX_P HELX_P14 AB5 GLN A 418 ? THR A 428 ? GLN A 1635 THR A 1645 1 ? 11 
HELX_P HELX_P15 AB6 GLU A 439 ? GLU A 449 ? GLU A 1656 GLU A 1666 1 ? 11 
HELX_P HELX_P16 AB7 ASN B 13  ? GLY B 25  ? ASN B 1230 GLY B 1242 1 ? 13 
HELX_P HELX_P17 AB8 ARG B 40  ? GLY B 62  ? ARG B 1257 GLY B 1279 1 ? 23 
HELX_P HELX_P18 AB9 ARG B 74  ? GLU B 78  ? ARG B 1291 GLU B 1295 1 ? 5  
HELX_P HELX_P19 AC1 PHE B 87  ? GLU B 90  ? PHE B 1304 GLU B 1307 5 ? 4  
HELX_P HELX_P20 AC2 SER B 112 ? ILE B 124 ? SER B 1329 ILE B 1341 1 ? 13 
HELX_P HELX_P21 AC3 SER B 126 ? LEU B 130 ? SER B 1343 LEU B 1347 5 ? 5  
HELX_P HELX_P22 AC4 THR B 168 ? LEU B 190 ? THR B 1385 LEU B 1407 1 ? 23 
HELX_P HELX_P23 AC5 GLN B 236 ? ASP B 243 ? GLN B 1453 ASP B 1460 1 ? 8  
HELX_P HELX_P24 AC6 THR B 266 ? ALA B 277 ? THR B 1483 ALA B 1494 1 ? 12 
HELX_P HELX_P25 AC7 ASP B 306 ? ALA B 326 ? ASP B 1523 ALA B 1543 1 ? 21 
HELX_P HELX_P26 AC8 SER B 339 ? LYS B 350 ? SER B 1556 LYS B 1567 1 ? 12 
HELX_P HELX_P27 AC9 GLY B 359 ? ASN B 365 ? GLY B 1576 ASN B 1582 1 ? 7  
HELX_P HELX_P28 AD1 GLN B 385 ? HIS B 412 ? GLN B 1602 HIS B 1629 1 ? 28 
HELX_P HELX_P29 AD2 GLN B 418 ? THR B 428 ? GLN B 1635 THR B 1645 1 ? 11 
HELX_P HELX_P30 AD3 GLU B 439 ? GLU B 449 ? GLU B 1656 GLU B 1666 1 ? 11 
# 
_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 CYS 437 SG ? ? ? 1_555 D ZN . ZN ? ? A CYS 1654 A ZN 1802 1_555 ? ? ? ? ? ? ? 2.495 ? ? 
metalc2 metalc ? ? A CYS 442 SG ? ? ? 1_555 D ZN . ZN ? ? A CYS 1659 A ZN 1802 1_555 ? ? ? ? ? ? ? 2.216 ? ? 
metalc3 metalc ? ? A CYS 486 SG ? ? ? 1_555 D ZN . ZN ? ? A CYS 1703 A ZN 1802 1_555 ? ? ? ? ? ? ? 2.487 ? ? 
metalc4 metalc ? ? A CYS 491 SG ? ? ? 1_555 D ZN . ZN ? ? A CYS 1708 A ZN 1802 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
metalc5 metalc ? ? B CYS 437 SG ? ? ? 1_555 I ZN . ZN ? ? B CYS 1654 B ZN 1802 1_555 ? ? ? ? ? ? ? 2.412 ? ? 
metalc6 metalc ? ? B CYS 442 SG ? ? ? 1_555 I ZN . ZN ? ? B CYS 1659 B ZN 1802 1_555 ? ? ? ? ? ? ? 2.107 ? ? 
metalc7 metalc ? ? B CYS 486 SG ? ? ? 1_555 I ZN . ZN ? ? B CYS 1703 B ZN 1802 1_555 ? ? ? ? ? ? ? 2.346 ? ? 
metalc8 metalc ? ? B CYS 491 SG ? ? ? 1_555 I ZN . ZN ? ? B CYS 1708 B ZN 1802 1_555 ? ? ? ? ? ? ? 2.002 ? ? 
# 
_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  SG ? A CYS 437 ? A CYS 1654 ? 1_555 ZN ? D ZN . ? A ZN 1802 ? 1_555 SG ? A CYS 442 ? A CYS 1659 ? 1_555 113.4 ? 
2  SG ? A CYS 437 ? A CYS 1654 ? 1_555 ZN ? D ZN . ? A ZN 1802 ? 1_555 SG ? A CYS 486 ? A CYS 1703 ? 1_555 111.6 ? 
3  SG ? A CYS 442 ? A CYS 1659 ? 1_555 ZN ? D ZN . ? A ZN 1802 ? 1_555 SG ? A CYS 486 ? A CYS 1703 ? 1_555 96.8  ? 
4  SG ? A CYS 437 ? A CYS 1654 ? 1_555 ZN ? D ZN . ? A ZN 1802 ? 1_555 SG ? A CYS 491 ? A CYS 1708 ? 1_555 120.0 ? 
5  SG ? A CYS 442 ? A CYS 1659 ? 1_555 ZN ? D ZN . ? A ZN 1802 ? 1_555 SG ? A CYS 491 ? A CYS 1708 ? 1_555 116.0 ? 
6  SG ? A CYS 486 ? A CYS 1703 ? 1_555 ZN ? D ZN . ? A ZN 1802 ? 1_555 SG ? A CYS 491 ? A CYS 1708 ? 1_555 94.2  ? 
7  SG ? B CYS 437 ? B CYS 1654 ? 1_555 ZN ? I ZN . ? B ZN 1802 ? 1_555 SG ? B CYS 442 ? B CYS 1659 ? 1_555 114.5 ? 
8  SG ? B CYS 437 ? B CYS 1654 ? 1_555 ZN ? I ZN . ? B ZN 1802 ? 1_555 SG ? B CYS 486 ? B CYS 1703 ? 1_555 130.9 ? 
9  SG ? B CYS 442 ? B CYS 1659 ? 1_555 ZN ? I ZN . ? B ZN 1802 ? 1_555 SG ? B CYS 486 ? B CYS 1703 ? 1_555 96.0  ? 
10 SG ? B CYS 437 ? B CYS 1654 ? 1_555 ZN ? I ZN . ? B ZN 1802 ? 1_555 SG ? B CYS 491 ? B CYS 1708 ? 1_555 116.3 ? 
11 SG ? B CYS 442 ? B CYS 1659 ? 1_555 ZN ? I ZN . ? B ZN 1802 ? 1_555 SG ? B CYS 491 ? B CYS 1708 ? 1_555 99.1  ? 
12 SG ? B CYS 486 ? B CYS 1703 ? 1_555 ZN ? I ZN . ? B ZN 1802 ? 1_555 SG ? B CYS 491 ? B CYS 1708 ? 1_555 93.9  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LEU 130 A . ? LEU 1347 A PRO 131 A ? PRO 1348 A 1 5.25 
2 LEU 130 B . ? LEU 1347 B PRO 131 B ? PRO 1348 B 1 5.52 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 8  ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 5  ? 
AA6 ? 4  ? 
AA7 ? 2  ? 
AA8 ? 11 ? 
AA9 ? 2  ? 
AB1 ? 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  ? anti-parallel 
AA2 1  2  ? parallel      
AA2 2  3  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA2 4  5  ? anti-parallel 
AA2 5  6  ? anti-parallel 
AA2 6  7  ? anti-parallel 
AA2 7  8  ? anti-parallel 
AA3 1  2  ? anti-parallel 
AA3 2  3  ? anti-parallel 
AA3 3  4  ? anti-parallel 
AA3 4  5  ? anti-parallel 
AA3 5  6  ? anti-parallel 
AA4 1  2  ? anti-parallel 
AA5 1  2  ? parallel      
AA5 2  3  ? parallel      
AA5 3  4  ? anti-parallel 
AA5 4  5  ? anti-parallel 
AA6 1  2  ? parallel      
AA6 2  3  ? anti-parallel 
AA6 3  4  ? anti-parallel 
AA7 1  2  ? anti-parallel 
AA8 1  2  ? parallel      
AA8 2  3  ? anti-parallel 
AA8 3  4  ? anti-parallel 
AA8 4  5  ? anti-parallel 
AA8 5  6  ? anti-parallel 
AA8 6  7  ? anti-parallel 
AA8 7  8  ? anti-parallel 
AA8 8  9  ? anti-parallel 
AA8 9  10 ? anti-parallel 
AA8 10 11 ? parallel      
AA9 1  2  ? anti-parallel 
AB1 1  2  ? parallel      
AB1 2  3  ? parallel      
AB1 3  4  ? anti-parallel 
AB1 4  5  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ILE A 28  ? GLU A 29  ? ILE A 1245 GLU A 1246 
AA1 2  ILE A 38  ? LEU A 39  ? ILE A 1255 LEU A 1256 
AA2 1  LYS A 64  ? GLU A 65  ? LYS A 1281 GLU A 1282 
AA2 2  ILE A 132 ? VAL A 141 ? ILE A 1349 VAL A 1358 
AA2 3  GLU A 156 ? PHE A 166 ? GLU A 1373 PHE A 1383 
AA2 4  PHE A 258 ? THR A 265 ? PHE A 1475 THR A 1482 
AA2 5  ARG A 224 ? GLY A 235 ? ARG A 1441 GLY A 1452 
AA2 6  TYR A 211 ? ILE A 219 ? TYR A 1428 ILE A 1436 
AA2 7  VAL A 196 ? ARG A 199 ? VAL A 1413 ARG A 1416 
AA2 8  ILE A 471 ? PRO A 472 ? ILE A 1688 PRO A 1689 
AA3 1  PHE A 71  ? VAL A 72  ? PHE A 1288 VAL A 1289 
AA3 2  SER A 100 ? VAL A 108 ? SER A 1317 VAL A 1325 
AA3 3  ALA A 92  ? SER A 97  ? ALA A 1309 SER A 1314 
AA3 4  ALA B 92  ? SER B 97  ? ALA B 1309 SER B 1314 
AA3 5  SER B 100 ? VAL B 108 ? SER B 1317 VAL B 1325 
AA3 6  PHE B 71  ? SER B 73  ? PHE B 1288 SER B 1290 
AA4 1  VAL A 245 ? GLU A 247 ? VAL A 1462 GLU A 1464 
AA4 2  LYS A 254 ? TYR A 256 ? LYS A 1471 TYR A 1473 
AA5 1  CYS A 330 ? GLY A 332 ? CYS A 1547 GLY A 1549 
AA5 2  VAL A 293 ? PRO A 297 ? VAL A 1510 PRO A 1514 
AA5 3  VAL A 354 ? LEU A 358 ? VAL A 1571 LEU A 1575 
AA5 4  GLN A 367 ? ARG A 372 ? GLN A 1584 ARG A 1589 
AA5 5  LYS A 378 ? LYS A 382 ? LYS A 1595 LYS A 1599 
AA6 1  THR A 413 ? LEU A 415 ? THR A 1630 LEU A 1632 
AA6 2  ILE A 431 ? PHE A 436 ? ILE A 1648 PHE A 1653 
AA6 3  PHE A 497 ? GLY A 502 ? PHE A 1714 GLY A 1719 
AA6 4  LYS A 467 ? SER A 468 ? LYS A 1684 SER A 1685 
AA7 1  ILE B 28  ? GLU B 29  ? ILE B 1245 GLU B 1246 
AA7 2  ILE B 38  ? LEU B 39  ? ILE B 1255 LEU B 1256 
AA8 1  LYS B 64  ? GLU B 65  ? LYS B 1281 GLU B 1282 
AA8 2  ILE B 132 ? VAL B 141 ? ILE B 1349 VAL B 1358 
AA8 3  GLU B 156 ? PHE B 166 ? GLU B 1373 PHE B 1383 
AA8 4  PHE B 258 ? THR B 265 ? PHE B 1475 THR B 1482 
AA8 5  ARG B 224 ? GLY B 235 ? ARG B 1441 GLY B 1452 
AA8 6  TYR B 211 ? ILE B 219 ? TYR B 1428 ILE B 1436 
AA8 7  VAL B 196 ? ARG B 199 ? VAL B 1413 ARG B 1416 
AA8 8  LYS B 467 ? PRO B 472 ? LYS B 1684 PRO B 1689 
AA8 9  PHE B 497 ? GLY B 502 ? PHE B 1714 GLY B 1719 
AA8 10 ILE B 431 ? PHE B 436 ? ILE B 1648 PHE B 1653 
AA8 11 THR B 413 ? LEU B 415 ? THR B 1630 LEU B 1632 
AA9 1  VAL B 245 ? GLU B 247 ? VAL B 1462 GLU B 1464 
AA9 2  LYS B 254 ? TYR B 256 ? LYS B 1471 TYR B 1473 
AB1 1  CYS B 330 ? GLY B 332 ? CYS B 1547 GLY B 1549 
AB1 2  VAL B 293 ? PRO B 297 ? VAL B 1510 PRO B 1514 
AB1 3  VAL B 354 ? LEU B 358 ? VAL B 1571 LEU B 1575 
AB1 4  GLN B 367 ? ARG B 372 ? GLN B 1584 ARG B 1589 
AB1 5  LYS B 378 ? LYS B 382 ? LYS B 1595 LYS B 1599 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N GLU A 29  ? N GLU A 1246 O ILE A 38  ? O ILE A 1255 
AA2 1  2  N LYS A 64  ? N LYS A 1281 O ASN A 135 ? O ASN A 1352 
AA2 2  3  N LEU A 134 ? N LEU A 1351 O HIS A 163 ? O HIS A 1380 
AA2 3  4  N PHE A 166 ? N PHE A 1383 O PHE A 258 ? O PHE A 1475 
AA2 4  5  O SER A 261 ? O SER A 1478 N HIS A 232 ? N HIS A 1449 
AA2 5  6  O ARG A 224 ? O ARG A 1441 N ILE A 219 ? N ILE A 1436 
AA2 6  7  O THR A 214 ? O THR A 1431 N GLY A 198 ? N GLY A 1415 
AA2 7  8  N ARG A 199 ? N ARG A 1416 O ILE A 471 ? O ILE A 1688 
AA3 1  2  N VAL A 72  ? N VAL A 1289 O ALA A 107 ? O ALA A 1324 
AA3 2  3  O SER A 100 ? O SER A 1317 N SER A 97  ? N SER A 1314 
AA3 3  4  N TRP A 93  ? N TRP A 1310 O LYS B 96  ? O LYS B 1313 
AA3 4  5  N ALA B 92  ? N ALA B 1309 O VAL B 108 ? O VAL B 1325 
AA3 5  6  O ALA B 107 ? O ALA B 1324 N VAL B 72  ? N VAL B 1289 
AA4 1  2  N TYR A 246 ? N TYR A 1463 O GLU A 255 ? O GLU A 1472 
AA5 1  2  O GLU A 331 ? O GLU A 1548 N ILE A 295 ? N ILE A 1512 
AA5 2  3  N VAL A 294 ? N VAL A 1511 O ILE A 356 ? O ILE A 1573 
AA5 3  4  N GLU A 357 ? N GLU A 1574 O VAL A 369 ? O VAL A 1586 
AA5 4  5  N ALA A 370 ? N ALA A 1587 O GLN A 379 ? O GLN A 1596 
AA6 1  2  N LYS A 414 ? N LYS A 1631 O ILE A 431 ? O ILE A 1648 
AA6 2  3  N ILE A 432 ? N ILE A 1649 O PHE A 501 ? O PHE A 1718 
AA6 3  4  O GLY A 502 ? O GLY A 1719 N LYS A 467 ? N LYS A 1684 
AA7 1  2  N GLU B 29  ? N GLU B 1246 O ILE B 38  ? O ILE B 1255 
AA8 1  2  N LYS B 64  ? N LYS B 1281 O ASN B 135 ? O ASN B 1352 
AA8 2  3  N LEU B 134 ? N LEU B 1351 O HIS B 163 ? O HIS B 1380 
AA8 3  4  N GLY B 162 ? N GLY B 1379 O TRP B 262 ? O TRP B 1479 
AA8 4  5  O SER B 261 ? O SER B 1478 N HIS B 232 ? N HIS B 1449 
AA8 5  6  O HIS B 233 ? O HIS B 1450 N TYR B 211 ? N TYR B 1428 
AA8 6  7  O THR B 214 ? O THR B 1431 N GLY B 198 ? N GLY B 1415 
AA8 7  8  N ARG B 199 ? N ARG B 1416 O ILE B 471 ? O ILE B 1688 
AA8 8  9  N LEU B 469 ? N LEU B 1686 O LEU B 500 ? O LEU B 1717 
AA8 9  10 O PHE B 497 ? O PHE B 1714 N PHE B 436 ? N PHE B 1653 
AA8 10 11 O MET B 433 ? O MET B 1650 N LYS B 414 ? N LYS B 1631 
AA9 1  2  N TYR B 246 ? N TYR B 1463 O GLU B 255 ? O GLU B 1472 
AB1 1  2  O GLU B 331 ? O GLU B 1548 N VAL B 293 ? N VAL B 1510 
AB1 2  3  N VAL B 296 ? N VAL B 1513 O ILE B 356 ? O ILE B 1573 
AB1 3  4  N GLU B 357 ? N GLU B 1574 O VAL B 369 ? O VAL B 1586 
AB1 4  5  N ALA B 370 ? N ALA B 1587 O GLN B 379 ? O GLN B 1596 
# 
_pdbx_entry_details.entry_id                   8JE5 
_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_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 LEU 1499 ? ? CG A LEU 1499 ? ? CD1 A LEU 1499 ? ? 99.94  111.00 -11.06 1.70 N 
2 1 C  B VAL 1289 ? ? N  B SER 1290 ? ? CA  B SER 1290 ? ? 105.60 121.70 -16.10 2.50 Y 
3 1 CA B CYS 1515 ? ? CB B CYS 1515 ? ? SG  B CYS 1515 ? ? 121.03 114.20 6.83   1.10 N 
4 1 CA B LEU 1640 ? ? CB B LEU 1640 ? ? CG  B LEU 1640 ? ? 133.15 115.30 17.85  2.30 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 1302 ? ? 50.14   -126.49 
2  1 ASP A 1303 ? ? -146.56 34.30   
3  1 GLU A 1307 ? ? -92.07  33.23   
4  1 THR A 1328 ? ? 172.57  162.96  
5  1 GLU A 1467 ? ? -77.53  -72.14  
6  1 ASP A 1495 ? ? -105.55 -160.97 
7  1 LYS A 1646 ? ? 72.49   51.59   
8  1 LEU A 1686 ? ? -104.62 -65.79  
9  1 VAL A 1700 ? ? -132.38 -52.68  
10 1 PHE B 1304 ? ? 88.56   -25.99  
11 1 GLU B 1307 ? ? -94.84  39.29   
12 1 THR B 1328 ? ? 174.06  161.69  
13 1 GLU B 1467 ? ? -74.77  -73.86  
14 1 ASP B 1495 ? ? -105.46 -159.01 
15 1 THR B 1518 ? ? -95.35  43.90   
16 1 ALA B 1519 ? ? 42.74   77.00   
17 1 ASN B 1554 ? ? -96.41  32.34   
18 1 GLN B 1584 ? ? -163.74 -169.41 
19 1 LYS B 1646 ? ? 70.85   46.45   
20 1 LEU B 1686 ? ? -106.21 -62.64  
21 1 ALA B 1694 ? ? 72.38   157.86  
22 1 VAL B 1700 ? ? -136.71 -48.14  
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -19.7950 
_pdbx_refine_tls.origin_y         -8.7184 
_pdbx_refine_tls.origin_z         8.2967 
_pdbx_refine_tls.T[1][1]          0.4122 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0088 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0849 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.4669 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0352 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.5680 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.1182 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0688 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.3098 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.7606 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.2091 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.0276 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0839 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0460 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.1470 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.1137 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0538 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0764 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.1003 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0761 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0292 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
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 1218 ? A MET 1   
2  1 Y 1 A THR 1219 ? A THR 2   
3  1 Y 1 A ARG 1669 ? A ARG 452 
4  1 Y 1 A ASP 1670 ? A ASP 453 
5  1 Y 1 A ASP 1671 ? A ASP 454 
6  1 Y 1 A ALA 1672 ? A ALA 455 
7  1 Y 1 A GLU 1673 ? A GLU 456 
8  1 Y 1 A ALA 1674 ? A ALA 457 
9  1 Y 1 A GLU 1675 ? A GLU 458 
10 1 Y 1 A ALA 1676 ? A ALA 459 
11 1 Y 1 A GLY 1677 ? A GLY 460 
12 1 Y 1 A ALA 1678 ? A ALA 461 
13 1 Y 1 A PRO 1679 ? A PRO 462 
14 1 Y 1 A ALA 1680 ? A ALA 463 
15 1 Y 1 A MET 1681 ? A MET 464 
16 1 Y 1 B MET 1218 ? B MET 1   
17 1 Y 1 B THR 1219 ? B THR 2   
18 1 Y 1 B ARG 1220 ? B ARG 3   
19 1 Y 1 B LEU 1221 ? B LEU 4   
20 1 Y 1 B GLY 1222 ? B GLY 5   
21 1 Y 1 B GLU 1297 ? B GLU 80  
22 1 Y 1 B LYS 1298 ? B LYS 81  
23 1 Y 1 B THR 1299 ? B THR 82  
24 1 Y 1 B HIS 1300 ? B HIS 83  
25 1 Y 1 B ILE 1301 ? B ILE 84  
26 1 Y 1 B ALA 1302 ? B ALA 85  
27 1 Y 1 B PHE 1362 ? B PHE 145 
28 1 Y 1 B ARG 1669 ? B ARG 452 
29 1 Y 1 B ASP 1670 ? B ASP 453 
30 1 Y 1 B ASP 1671 ? B ASP 454 
31 1 Y 1 B ALA 1672 ? B ALA 455 
32 1 Y 1 B GLU 1673 ? B GLU 456 
33 1 Y 1 B ALA 1674 ? B ALA 457 
34 1 Y 1 B GLU 1675 ? B GLU 458 
35 1 Y 1 B ALA 1676 ? B ALA 459 
36 1 Y 1 B GLY 1677 ? B GLY 460 
37 1 Y 1 B ALA 1678 ? B ALA 461 
38 1 Y 1 B PRO 1679 ? B PRO 462 
39 1 Y 1 B ALA 1680 ? B ALA 463 
40 1 Y 1 B MET 1681 ? B MET 464 
# 
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  
CL  CL    CL N N 74  
CYS N     N  N N 75  
CYS CA    C  N R 76  
CYS C     C  N N 77  
CYS O     O  N N 78  
CYS CB    C  N N 79  
CYS SG    S  N N 80  
CYS OXT   O  N N 81  
CYS H     H  N N 82  
CYS H2    H  N N 83  
CYS HA    H  N N 84  
CYS HB2   H  N N 85  
CYS HB3   H  N N 86  
CYS HG    H  N N 87  
CYS HXT   H  N N 88  
GLN N     N  N N 89  
GLN CA    C  N S 90  
GLN C     C  N N 91  
GLN O     O  N N 92  
GLN CB    C  N N 93  
GLN CG    C  N N 94  
GLN CD    C  N N 95  
GLN OE1   O  N N 96  
GLN NE2   N  N N 97  
GLN OXT   O  N N 98  
GLN H     H  N N 99  
GLN H2    H  N N 100 
GLN HA    H  N N 101 
GLN HB2   H  N N 102 
GLN HB3   H  N N 103 
GLN HG2   H  N N 104 
GLN HG3   H  N N 105 
GLN HE21  H  N N 106 
GLN HE22  H  N N 107 
GLN HXT   H  N N 108 
GLU N     N  N N 109 
GLU CA    C  N S 110 
GLU C     C  N N 111 
GLU O     O  N N 112 
GLU CB    C  N N 113 
GLU CG    C  N N 114 
GLU CD    C  N N 115 
GLU OE1   O  N N 116 
GLU OE2   O  N N 117 
GLU OXT   O  N N 118 
GLU H     H  N N 119 
GLU H2    H  N N 120 
GLU HA    H  N N 121 
GLU HB2   H  N N 122 
GLU HB3   H  N N 123 
GLU HG2   H  N N 124 
GLU HG3   H  N N 125 
GLU HE2   H  N N 126 
GLU HXT   H  N N 127 
GLY N     N  N N 128 
GLY CA    C  N N 129 
GLY C     C  N N 130 
GLY O     O  N N 131 
GLY OXT   O  N N 132 
GLY H     H  N N 133 
GLY H2    H  N N 134 
GLY HA2   H  N N 135 
GLY HA3   H  N N 136 
GLY HXT   H  N N 137 
GOL C1    C  N N 138 
GOL O1    O  N N 139 
GOL C2    C  N N 140 
GOL O2    O  N N 141 
GOL C3    C  N N 142 
GOL O3    O  N N 143 
GOL H11   H  N N 144 
GOL H12   H  N N 145 
GOL HO1   H  N N 146 
GOL H2    H  N N 147 
GOL HO2   H  N N 148 
GOL H31   H  N N 149 
GOL H32   H  N N 150 
GOL HO3   H  N N 151 
HFG "O4'" O  N N 152 
HFG C21   C  N N 153 
HFG "C3'" C  N N 154 
HFG "C2'" C  N R 155 
HFG "N1'" N  N N 156 
HFG "C6'" C  N N 157 
HFG "C5'" C  N N 158 
HFG "C4'" C  N N 159 
HFG C39   C  N S 160 
HFG "O7'" O  N N 161 
HFG "C1'" C  N N 162 
HFG N3    N  N N 163 
HFG C4    C  N N 164 
HFG O11   O  N N 165 
HFG C10   C  Y N 166 
HFG C5    C  Y N 167 
HFG C2    C  N N 168 
HFG N1    N  N N 169 
HFG C9    C  Y N 170 
HFG C8    C  Y N 171 
HFG C7    C  Y N 172 
HFG BR1   BR N N 173 
HFG C6    C  Y N 174 
HFG CL1   CL N N 175 
HFG H1    H  N N 176 
HFG H2    H  N N 177 
HFG H3    H  N N 178 
HFG H4    H  N N 179 
HFG H6    H  N N 180 
HFG H7    H  N N 181 
HFG H8    H  N N 182 
HFG H9    H  N N 183 
HFG H10   H  N N 184 
HFG H11   H  N N 185 
HFG H12   H  N N 186 
HFG H13   H  N N 187 
HFG H14   H  N N 188 
HFG H15   H  N N 189 
HFG H16   H  N N 190 
HFG H17   H  N N 191 
HFG H18   H  N N 192 
HIS N     N  N N 193 
HIS CA    C  N S 194 
HIS C     C  N N 195 
HIS O     O  N N 196 
HIS CB    C  N N 197 
HIS CG    C  Y N 198 
HIS ND1   N  Y N 199 
HIS CD2   C  Y N 200 
HIS CE1   C  Y N 201 
HIS NE2   N  Y N 202 
HIS OXT   O  N N 203 
HIS H     H  N N 204 
HIS H2    H  N N 205 
HIS HA    H  N N 206 
HIS HB2   H  N N 207 
HIS HB3   H  N N 208 
HIS HD1   H  N N 209 
HIS HD2   H  N N 210 
HIS HE1   H  N N 211 
HIS HE2   H  N N 212 
HIS HXT   H  N N 213 
HOH O     O  N N 214 
HOH H1    H  N N 215 
HOH H2    H  N N 216 
ILE N     N  N N 217 
ILE CA    C  N S 218 
ILE C     C  N N 219 
ILE O     O  N N 220 
ILE CB    C  N S 221 
ILE CG1   C  N N 222 
ILE CG2   C  N N 223 
ILE CD1   C  N N 224 
ILE OXT   O  N N 225 
ILE H     H  N N 226 
ILE H2    H  N N 227 
ILE HA    H  N N 228 
ILE HB    H  N N 229 
ILE HG12  H  N N 230 
ILE HG13  H  N N 231 
ILE HG21  H  N N 232 
ILE HG22  H  N N 233 
ILE HG23  H  N N 234 
ILE HD11  H  N N 235 
ILE HD12  H  N N 236 
ILE HD13  H  N N 237 
ILE HXT   H  N N 238 
LEU N     N  N N 239 
LEU CA    C  N S 240 
LEU C     C  N N 241 
LEU O     O  N N 242 
LEU CB    C  N N 243 
LEU CG    C  N N 244 
LEU CD1   C  N N 245 
LEU CD2   C  N N 246 
LEU OXT   O  N N 247 
LEU H     H  N N 248 
LEU H2    H  N N 249 
LEU HA    H  N N 250 
LEU HB2   H  N N 251 
LEU HB3   H  N N 252 
LEU HG    H  N N 253 
LEU HD11  H  N N 254 
LEU HD12  H  N N 255 
LEU HD13  H  N N 256 
LEU HD21  H  N N 257 
LEU HD22  H  N N 258 
LEU HD23  H  N N 259 
LEU HXT   H  N N 260 
LYS N     N  N N 261 
LYS CA    C  N S 262 
LYS C     C  N N 263 
LYS O     O  N N 264 
LYS CB    C  N N 265 
LYS CG    C  N N 266 
LYS CD    C  N N 267 
LYS CE    C  N N 268 
LYS NZ    N  N N 269 
LYS OXT   O  N N 270 
LYS H     H  N N 271 
LYS H2    H  N N 272 
LYS HA    H  N N 273 
LYS HB2   H  N N 274 
LYS HB3   H  N N 275 
LYS HG2   H  N N 276 
LYS HG3   H  N N 277 
LYS HD2   H  N N 278 
LYS HD3   H  N N 279 
LYS HE2   H  N N 280 
LYS HE3   H  N N 281 
LYS HZ1   H  N N 282 
LYS HZ2   H  N N 283 
LYS HZ3   H  N N 284 
LYS HXT   H  N N 285 
MET N     N  N N 286 
MET CA    C  N S 287 
MET C     C  N N 288 
MET O     O  N N 289 
MET CB    C  N N 290 
MET CG    C  N N 291 
MET SD    S  N N 292 
MET CE    C  N N 293 
MET OXT   O  N N 294 
MET H     H  N N 295 
MET H2    H  N N 296 
MET HA    H  N N 297 
MET HB2   H  N N 298 
MET HB3   H  N N 299 
MET HG2   H  N N 300 
MET HG3   H  N N 301 
MET HE1   H  N N 302 
MET HE2   H  N N 303 
MET HE3   H  N N 304 
MET HXT   H  N N 305 
PHE N     N  N N 306 
PHE CA    C  N S 307 
PHE C     C  N N 308 
PHE O     O  N N 309 
PHE CB    C  N N 310 
PHE CG    C  Y N 311 
PHE CD1   C  Y N 312 
PHE CD2   C  Y N 313 
PHE CE1   C  Y N 314 
PHE CE2   C  Y N 315 
PHE CZ    C  Y N 316 
PHE OXT   O  N N 317 
PHE H     H  N N 318 
PHE H2    H  N N 319 
PHE HA    H  N N 320 
PHE HB2   H  N N 321 
PHE HB3   H  N N 322 
PHE HD1   H  N N 323 
PHE HD2   H  N N 324 
PHE HE1   H  N N 325 
PHE HE2   H  N N 326 
PHE HZ    H  N N 327 
PHE HXT   H  N N 328 
PRO N     N  N N 329 
PRO CA    C  N S 330 
PRO C     C  N N 331 
PRO O     O  N N 332 
PRO CB    C  N N 333 
PRO CG    C  N N 334 
PRO CD    C  N N 335 
PRO OXT   O  N N 336 
PRO H     H  N N 337 
PRO HA    H  N N 338 
PRO HB2   H  N N 339 
PRO HB3   H  N N 340 
PRO HG2   H  N N 341 
PRO HG3   H  N N 342 
PRO HD2   H  N N 343 
PRO HD3   H  N N 344 
PRO HXT   H  N N 345 
SER N     N  N N 346 
SER CA    C  N S 347 
SER C     C  N N 348 
SER O     O  N N 349 
SER CB    C  N N 350 
SER OG    O  N N 351 
SER OXT   O  N N 352 
SER H     H  N N 353 
SER H2    H  N N 354 
SER HA    H  N N 355 
SER HB2   H  N N 356 
SER HB3   H  N N 357 
SER HG    H  N N 358 
SER HXT   H  N N 359 
THR N     N  N N 360 
THR CA    C  N S 361 
THR C     C  N N 362 
THR O     O  N N 363 
THR CB    C  N R 364 
THR OG1   O  N N 365 
THR CG2   C  N N 366 
THR OXT   O  N N 367 
THR H     H  N N 368 
THR H2    H  N N 369 
THR HA    H  N N 370 
THR HB    H  N N 371 
THR HG1   H  N N 372 
THR HG21  H  N N 373 
THR HG22  H  N N 374 
THR HG23  H  N N 375 
THR HXT   H  N N 376 
TRP N     N  N N 377 
TRP CA    C  N S 378 
TRP C     C  N N 379 
TRP O     O  N N 380 
TRP CB    C  N N 381 
TRP CG    C  Y N 382 
TRP CD1   C  Y N 383 
TRP CD2   C  Y N 384 
TRP NE1   N  Y N 385 
TRP CE2   C  Y N 386 
TRP CE3   C  Y N 387 
TRP CZ2   C  Y N 388 
TRP CZ3   C  Y N 389 
TRP CH2   C  Y N 390 
TRP OXT   O  N N 391 
TRP H     H  N N 392 
TRP H2    H  N N 393 
TRP HA    H  N N 394 
TRP HB2   H  N N 395 
TRP HB3   H  N N 396 
TRP HD1   H  N N 397 
TRP HE1   H  N N 398 
TRP HE3   H  N N 399 
TRP HZ2   H  N N 400 
TRP HZ3   H  N N 401 
TRP HH2   H  N N 402 
TRP HXT   H  N N 403 
TYR N     N  N N 404 
TYR CA    C  N S 405 
TYR C     C  N N 406 
TYR O     O  N N 407 
TYR CB    C  N N 408 
TYR CG    C  Y N 409 
TYR CD1   C  Y N 410 
TYR CD2   C  Y N 411 
TYR CE1   C  Y N 412 
TYR CE2   C  Y N 413 
TYR CZ    C  Y N 414 
TYR OH    O  N N 415 
TYR OXT   O  N N 416 
TYR H     H  N N 417 
TYR H2    H  N N 418 
TYR HA    H  N N 419 
TYR HB2   H  N N 420 
TYR HB3   H  N N 421 
TYR HD1   H  N N 422 
TYR HD2   H  N N 423 
TYR HE1   H  N N 424 
TYR HE2   H  N N 425 
TYR HH    H  N N 426 
TYR HXT   H  N N 427 
VAL N     N  N N 428 
VAL CA    C  N S 429 
VAL C     C  N N 430 
VAL O     O  N N 431 
VAL CB    C  N N 432 
VAL CG1   C  N N 433 
VAL CG2   C  N N 434 
VAL OXT   O  N N 435 
VAL H     H  N N 436 
VAL H2    H  N N 437 
VAL HA    H  N N 438 
VAL HB    H  N N 439 
VAL HG11  H  N N 440 
VAL HG12  H  N N 441 
VAL HG13  H  N N 442 
VAL HG21  H  N N 443 
VAL HG22  H  N N 444 
VAL HG23  H  N N 445 
VAL HXT   H  N N 446 
ZN  ZN    ZN N N 447 
# 
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 
GOL C1    O1    sing N N 129 
GOL C1    C2    sing N N 130 
GOL C1    H11   sing N N 131 
GOL C1    H12   sing N N 132 
GOL O1    HO1   sing N N 133 
GOL C2    O2    sing N N 134 
GOL C2    C3    sing N N 135 
GOL C2    H2    sing N N 136 
GOL O2    HO2   sing N N 137 
GOL C3    O3    sing N N 138 
GOL C3    H31   sing N N 139 
GOL C3    H32   sing N N 140 
GOL O3    HO3   sing N N 141 
HFG CL1   C6    sing N N 142 
HFG C6    C5    doub Y N 143 
HFG C6    C7    sing Y N 144 
HFG BR1   C7    sing N N 145 
HFG C5    C10   sing Y N 146 
HFG C7    C8    doub Y N 147 
HFG O11   C4    doub N N 148 
HFG C10   C4    sing N N 149 
HFG C10   C9    doub Y N 150 
HFG C8    C9    sing Y N 151 
HFG C4    N3    sing N N 152 
HFG C9    N1    sing N N 153 
HFG "N1'" "C6'" sing N N 154 
HFG "N1'" "C2'" sing N N 155 
HFG "C6'" "C5'" sing N N 156 
HFG "O4'" C21   doub N N 157 
HFG N3    "C1'" sing N N 158 
HFG N3    C2    sing N N 159 
HFG N1    C2    doub N N 160 
HFG C21   "C3'" sing N N 161 
HFG C21   "C1'" sing N N 162 
HFG "C3'" "C2'" sing N N 163 
HFG "C2'" C39   sing N N 164 
HFG "C5'" "C4'" sing N N 165 
HFG C39   "C4'" sing N N 166 
HFG C39   "O7'" sing N N 167 
HFG "C3'" H1    sing N N 168 
HFG "C3'" H2    sing N N 169 
HFG "C2'" H3    sing N N 170 
HFG "N1'" H4    sing N N 171 
HFG "C6'" H6    sing N N 172 
HFG "C6'" H7    sing N N 173 
HFG "C5'" H8    sing N N 174 
HFG "C5'" H9    sing N N 175 
HFG "C4'" H10   sing N N 176 
HFG "C4'" H11   sing N N 177 
HFG C39   H12   sing N N 178 
HFG "O7'" H13   sing N N 179 
HFG "C1'" H14   sing N N 180 
HFG "C1'" H15   sing N N 181 
HFG C5    H16   sing N N 182 
HFG C2    H17   sing N N 183 
HFG C8    H18   sing N N 184 
HIS N     CA    sing N N 185 
HIS N     H     sing N N 186 
HIS N     H2    sing N N 187 
HIS CA    C     sing N N 188 
HIS CA    CB    sing N N 189 
HIS CA    HA    sing N N 190 
HIS C     O     doub N N 191 
HIS C     OXT   sing N N 192 
HIS CB    CG    sing N N 193 
HIS CB    HB2   sing N N 194 
HIS CB    HB3   sing N N 195 
HIS CG    ND1   sing Y N 196 
HIS CG    CD2   doub Y N 197 
HIS ND1   CE1   doub Y N 198 
HIS ND1   HD1   sing N N 199 
HIS CD2   NE2   sing Y N 200 
HIS CD2   HD2   sing N N 201 
HIS CE1   NE2   sing Y N 202 
HIS CE1   HE1   sing N N 203 
HIS NE2   HE2   sing N N 204 
HIS OXT   HXT   sing N N 205 
HOH O     H1    sing N N 206 
HOH O     H2    sing N N 207 
ILE N     CA    sing N N 208 
ILE N     H     sing N N 209 
ILE N     H2    sing N N 210 
ILE CA    C     sing N N 211 
ILE CA    CB    sing N N 212 
ILE CA    HA    sing N N 213 
ILE C     O     doub N N 214 
ILE C     OXT   sing N N 215 
ILE CB    CG1   sing N N 216 
ILE CB    CG2   sing N N 217 
ILE CB    HB    sing N N 218 
ILE CG1   CD1   sing N N 219 
ILE CG1   HG12  sing N N 220 
ILE CG1   HG13  sing N N 221 
ILE CG2   HG21  sing N N 222 
ILE CG2   HG22  sing N N 223 
ILE CG2   HG23  sing N N 224 
ILE CD1   HD11  sing N N 225 
ILE CD1   HD12  sing N N 226 
ILE CD1   HD13  sing N N 227 
ILE OXT   HXT   sing N N 228 
LEU N     CA    sing N N 229 
LEU N     H     sing N N 230 
LEU N     H2    sing N N 231 
LEU CA    C     sing N N 232 
LEU CA    CB    sing N N 233 
LEU CA    HA    sing N N 234 
LEU C     O     doub N N 235 
LEU C     OXT   sing N N 236 
LEU CB    CG    sing N N 237 
LEU CB    HB2   sing N N 238 
LEU CB    HB3   sing N N 239 
LEU CG    CD1   sing N N 240 
LEU CG    CD2   sing N N 241 
LEU CG    HG    sing N N 242 
LEU CD1   HD11  sing N N 243 
LEU CD1   HD12  sing N N 244 
LEU CD1   HD13  sing N N 245 
LEU CD2   HD21  sing N N 246 
LEU CD2   HD22  sing N N 247 
LEU CD2   HD23  sing N N 248 
LEU OXT   HXT   sing N N 249 
LYS N     CA    sing N N 250 
LYS N     H     sing N N 251 
LYS N     H2    sing N N 252 
LYS CA    C     sing N N 253 
LYS CA    CB    sing N N 254 
LYS CA    HA    sing N N 255 
LYS C     O     doub N N 256 
LYS C     OXT   sing N N 257 
LYS CB    CG    sing N N 258 
LYS CB    HB2   sing N N 259 
LYS CB    HB3   sing N N 260 
LYS CG    CD    sing N N 261 
LYS CG    HG2   sing N N 262 
LYS CG    HG3   sing N N 263 
LYS CD    CE    sing N N 264 
LYS CD    HD2   sing N N 265 
LYS CD    HD3   sing N N 266 
LYS CE    NZ    sing N N 267 
LYS CE    HE2   sing N N 268 
LYS CE    HE3   sing N N 269 
LYS NZ    HZ1   sing N N 270 
LYS NZ    HZ2   sing N N 271 
LYS NZ    HZ3   sing N N 272 
LYS OXT   HXT   sing N N 273 
MET N     CA    sing N N 274 
MET N     H     sing N N 275 
MET N     H2    sing N N 276 
MET CA    C     sing N N 277 
MET CA    CB    sing N N 278 
MET CA    HA    sing N N 279 
MET C     O     doub N N 280 
MET C     OXT   sing N N 281 
MET CB    CG    sing N N 282 
MET CB    HB2   sing N N 283 
MET CB    HB3   sing N N 284 
MET CG    SD    sing N N 285 
MET CG    HG2   sing N N 286 
MET CG    HG3   sing N N 287 
MET SD    CE    sing N N 288 
MET CE    HE1   sing N N 289 
MET CE    HE2   sing N N 290 
MET CE    HE3   sing N N 291 
MET OXT   HXT   sing N N 292 
PHE N     CA    sing N N 293 
PHE N     H     sing N N 294 
PHE N     H2    sing N N 295 
PHE CA    C     sing N N 296 
PHE CA    CB    sing N N 297 
PHE CA    HA    sing N N 298 
PHE C     O     doub N N 299 
PHE C     OXT   sing N N 300 
PHE CB    CG    sing N N 301 
PHE CB    HB2   sing N N 302 
PHE CB    HB3   sing N N 303 
PHE CG    CD1   doub Y N 304 
PHE CG    CD2   sing Y N 305 
PHE CD1   CE1   sing Y N 306 
PHE CD1   HD1   sing N N 307 
PHE CD2   CE2   doub Y N 308 
PHE CD2   HD2   sing N N 309 
PHE CE1   CZ    doub Y N 310 
PHE CE1   HE1   sing N N 311 
PHE CE2   CZ    sing Y N 312 
PHE CE2   HE2   sing N N 313 
PHE CZ    HZ    sing N N 314 
PHE OXT   HXT   sing N N 315 
PRO N     CA    sing N N 316 
PRO N     CD    sing N N 317 
PRO N     H     sing N N 318 
PRO CA    C     sing N N 319 
PRO CA    CB    sing N N 320 
PRO CA    HA    sing N N 321 
PRO C     O     doub N N 322 
PRO C     OXT   sing N N 323 
PRO CB    CG    sing N N 324 
PRO CB    HB2   sing N N 325 
PRO CB    HB3   sing N N 326 
PRO CG    CD    sing N N 327 
PRO CG    HG2   sing N N 328 
PRO CG    HG3   sing N N 329 
PRO CD    HD2   sing N N 330 
PRO CD    HD3   sing N N 331 
PRO OXT   HXT   sing N N 332 
SER N     CA    sing N N 333 
SER N     H     sing N N 334 
SER N     H2    sing N N 335 
SER CA    C     sing N N 336 
SER CA    CB    sing N N 337 
SER CA    HA    sing N N 338 
SER C     O     doub N N 339 
SER C     OXT   sing N N 340 
SER CB    OG    sing N N 341 
SER CB    HB2   sing N N 342 
SER CB    HB3   sing N N 343 
SER OG    HG    sing N N 344 
SER OXT   HXT   sing N N 345 
THR N     CA    sing N N 346 
THR N     H     sing N N 347 
THR N     H2    sing N N 348 
THR CA    C     sing N N 349 
THR CA    CB    sing N N 350 
THR CA    HA    sing N N 351 
THR C     O     doub N N 352 
THR C     OXT   sing N N 353 
THR CB    OG1   sing N N 354 
THR CB    CG2   sing N N 355 
THR CB    HB    sing N N 356 
THR OG1   HG1   sing N N 357 
THR CG2   HG21  sing N N 358 
THR CG2   HG22  sing N N 359 
THR CG2   HG23  sing N N 360 
THR OXT   HXT   sing N N 361 
TRP N     CA    sing N N 362 
TRP N     H     sing N N 363 
TRP N     H2    sing N N 364 
TRP CA    C     sing N N 365 
TRP CA    CB    sing N N 366 
TRP CA    HA    sing N N 367 
TRP C     O     doub N N 368 
TRP C     OXT   sing N N 369 
TRP CB    CG    sing N N 370 
TRP CB    HB2   sing N N 371 
TRP CB    HB3   sing N N 372 
TRP CG    CD1   doub Y N 373 
TRP CG    CD2   sing Y N 374 
TRP CD1   NE1   sing Y N 375 
TRP CD1   HD1   sing N N 376 
TRP CD2   CE2   doub Y N 377 
TRP CD2   CE3   sing Y N 378 
TRP NE1   CE2   sing Y N 379 
TRP NE1   HE1   sing N N 380 
TRP CE2   CZ2   sing Y N 381 
TRP CE3   CZ3   doub Y N 382 
TRP CE3   HE3   sing N N 383 
TRP CZ2   CH2   doub Y N 384 
TRP CZ2   HZ2   sing N N 385 
TRP CZ3   CH2   sing Y N 386 
TRP CZ3   HZ3   sing N N 387 
TRP CH2   HH2   sing N N 388 
TRP OXT   HXT   sing N N 389 
TYR N     CA    sing N N 390 
TYR N     H     sing N N 391 
TYR N     H2    sing N N 392 
TYR CA    C     sing N N 393 
TYR CA    CB    sing N N 394 
TYR CA    HA    sing N N 395 
TYR C     O     doub N N 396 
TYR C     OXT   sing N N 397 
TYR CB    CG    sing N N 398 
TYR CB    HB2   sing N N 399 
TYR CB    HB3   sing N N 400 
TYR CG    CD1   doub Y N 401 
TYR CG    CD2   sing Y N 402 
TYR CD1   CE1   sing Y N 403 
TYR CD1   HD1   sing N N 404 
TYR CD2   CE2   doub Y N 405 
TYR CD2   HD2   sing N N 406 
TYR CE1   CZ    doub Y N 407 
TYR CE1   HE1   sing N N 408 
TYR CE2   CZ    sing Y N 409 
TYR CE2   HE2   sing N N 410 
TYR CZ    OH    sing N N 411 
TYR OH    HH    sing N N 412 
TYR OXT   HXT   sing N N 413 
VAL N     CA    sing N N 414 
VAL N     H     sing N N 415 
VAL N     H2    sing N N 416 
VAL CA    C     sing N N 417 
VAL CA    CB    sing N N 418 
VAL CA    HA    sing N N 419 
VAL C     O     doub N N 420 
VAL C     OXT   sing N N 421 
VAL CB    CG1   sing N N 422 
VAL CB    CG2   sing N N 423 
VAL CB    HB    sing N N 424 
VAL CG1   HG11  sing N N 425 
VAL CG1   HG12  sing N N 426 
VAL CG1   HG13  sing N N 427 
VAL CG2   HG21  sing N N 428 
VAL CG2   HG22  sing N N 429 
VAL CG2   HG23  sing N N 430 
VAL OXT   HXT   sing N N 431 
# 
_pdbx_audit_support.funding_organization   'Department of Biotechnology (DBT, India)' 
_pdbx_audit_support.country                India 
_pdbx_audit_support.grant_number           PR32713 
_pdbx_audit_support.ordinal                1 
# 
_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   7F9A 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8JE5 
_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.fract_transf_matrix[1][1]   0.012326 
_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]   0.008736 
_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]   0.008301 
_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 
BR 
C  
CL 
N  
O  
S  
ZN 
# 
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     . ARG A 1 3   ? 4.448   -26.558 -9.910  1.00 66.85  ? 1220 ARG A N     1 
ATOM   2    C  CA    . ARG A 1 3   ? 5.504   -26.355 -8.915  1.00 74.15  ? 1220 ARG A CA    1 
ATOM   3    C  C     . ARG A 1 3   ? 5.034   -26.625 -7.486  1.00 72.78  ? 1220 ARG A C     1 
ATOM   4    O  O     . ARG A 1 3   ? 5.134   -27.747 -7.032  1.00 89.38  ? 1220 ARG A O     1 
ATOM   5    C  CB    . ARG A 1 3   ? 6.117   -24.940 -8.996  1.00 82.37  ? 1220 ARG A CB    1 
ATOM   6    C  CG    . ARG A 1 3   ? 7.616   -24.941 -8.554  1.00 88.51  ? 1220 ARG A CG    1 
ATOM   7    C  CD    . ARG A 1 3   ? 8.430   -23.711 -8.957  1.00 88.19  ? 1220 ARG A CD    1 
ATOM   8    N  NE    . ARG A 1 3   ? 8.171   -23.301 -10.330 1.00 90.11  ? 1220 ARG A NE    1 
ATOM   9    C  CZ    . ARG A 1 3   ? 7.256   -22.403 -10.668 1.00 99.20  ? 1220 ARG A CZ    1 
ATOM   10   N  NH1   . ARG A 1 3   ? 6.529   -21.820 -9.725  1.00 106.13 ? 1220 ARG A NH1   1 
ATOM   11   N  NH2   . ARG A 1 3   ? 7.069   -22.082 -11.939 1.00 100.97 ? 1220 ARG A NH2   1 
ATOM   12   N  N     . LEU A 1 4   ? 4.539   -25.607 -6.783  1.00 78.38  ? 1221 LEU A N     1 
ATOM   13   C  CA    . LEU A 1 4   ? 4.208   -25.727 -5.358  1.00 78.70  ? 1221 LEU A CA    1 
ATOM   14   C  C     . LEU A 1 4   ? 3.443   -27.007 -5.023  1.00 79.39  ? 1221 LEU A C     1 
ATOM   15   O  O     . LEU A 1 4   ? 2.513   -27.402 -5.729  1.00 82.98  ? 1221 LEU A O     1 
ATOM   16   C  CB    . LEU A 1 4   ? 3.377   -24.523 -4.921  1.00 79.86  ? 1221 LEU A CB    1 
ATOM   17   C  CG    . LEU A 1 4   ? 4.198   -23.324 -4.445  1.00 84.73  ? 1221 LEU A CG    1 
ATOM   18   C  CD1   . LEU A 1 4   ? 3.290   -22.343 -3.733  1.00 78.34  ? 1221 LEU A CD1   1 
ATOM   19   C  CD2   . LEU A 1 4   ? 5.385   -23.769 -3.560  1.00 80.59  ? 1221 LEU A CD2   1 
ATOM   20   N  N     . GLY A 1 5   ? 3.817   -27.639 -3.912  1.00 77.36  ? 1222 GLY A N     1 
ATOM   21   C  CA    . GLY A 1 5   ? 3.177   -28.877 -3.510  1.00 72.34  ? 1222 GLY A CA    1 
ATOM   22   C  C     . GLY A 1 5   ? 3.361   -29.181 -2.042  1.00 76.19  ? 1222 GLY A C     1 
ATOM   23   O  O     . GLY A 1 5   ? 4.266   -28.666 -1.386  1.00 75.80  ? 1222 GLY A O     1 
ATOM   24   N  N     . LEU A 1 6   ? 2.487   -30.041 -1.533  1.00 81.30  ? 1223 LEU A N     1 
ATOM   25   C  CA    . LEU A 1 6   ? 2.554   -30.440 -0.135  1.00 81.44  ? 1223 LEU A CA    1 
ATOM   26   C  C     . LEU A 1 6   ? 3.800   -31.281 0.109   1.00 95.18  ? 1223 LEU A C     1 
ATOM   27   O  O     . LEU A 1 6   ? 4.093   -32.215 -0.647  1.00 103.06 ? 1223 LEU A O     1 
ATOM   28   C  CB    . LEU A 1 6   ? 1.303   -31.233 0.239   1.00 77.62  ? 1223 LEU A CB    1 
ATOM   29   C  CG    . LEU A 1 6   ? 0.178   -30.567 1.025   1.00 79.89  ? 1223 LEU A CG    1 
ATOM   30   C  CD1   . LEU A 1 6   ? -0.188  -29.218 0.415   1.00 81.02  ? 1223 LEU A CD1   1 
ATOM   31   C  CD2   . LEU A 1 6   ? -1.043  -31.500 1.080   1.00 75.99  ? 1223 LEU A CD2   1 
ATOM   32   N  N     . GLU A 1 7   ? 4.542   -30.947 1.162   1.00 89.30  ? 1224 GLU A N     1 
ATOM   33   C  CA    . GLU A 1 7   ? 5.763   -31.680 1.472   1.00 75.61  ? 1224 GLU A CA    1 
ATOM   34   C  C     . GLU A 1 7   ? 5.561   -32.706 2.568   1.00 76.85  ? 1224 GLU A C     1 
ATOM   35   O  O     . GLU A 1 7   ? 6.397   -33.595 2.707   1.00 92.02  ? 1224 GLU A O     1 
ATOM   36   C  CB    . GLU A 1 7   ? 6.902   -30.734 1.879   1.00 60.12  ? 1224 GLU A CB    1 
ATOM   37   N  N     . ALA A 1 8   ? 4.498   -32.597 3.359   1.00 83.27  ? 1225 ALA A N     1 
ATOM   38   C  CA    . ALA A 1 8   ? 4.197   -33.559 4.414   1.00 81.99  ? 1225 ALA A CA    1 
ATOM   39   C  C     . ALA A 1 8   ? 2.922   -34.333 4.074   1.00 77.14  ? 1225 ALA A C     1 
ATOM   40   O  O     . ALA A 1 8   ? 2.266   -34.091 3.049   1.00 68.98  ? 1225 ALA A O     1 
ATOM   41   C  CB    . ALA A 1 8   ? 4.069   -32.858 5.770   1.00 83.86  ? 1225 ALA A CB    1 
ATOM   42   N  N     . THR A 1 9   ? 2.552   -35.252 4.979   1.00 85.35  ? 1226 THR A N     1 
ATOM   43   C  CA    . THR A 1 9   ? 1.407   -36.137 4.779   1.00 85.62  ? 1226 THR A CA    1 
ATOM   44   C  C     . THR A 1 9   ? 0.555   -36.199 6.034   1.00 81.47  ? 1226 THR A C     1 
ATOM   45   O  O     . THR A 1 9   ? 1.056   -36.164 7.161   1.00 82.70  ? 1226 THR A O     1 
ATOM   46   C  CB    . THR A 1 9   ? 1.804   -37.599 4.405   1.00 76.74  ? 1226 THR A CB    1 
ATOM   47   O  OG1   . THR A 1 9   ? 2.561   -38.192 5.470   1.00 77.43  ? 1226 THR A OG1   1 
ATOM   48   C  CG2   . THR A 1 9   ? 2.569   -37.654 3.089   1.00 56.16  ? 1226 THR A CG2   1 
ATOM   49   N  N     . LYS A 1 10  ? -0.743  -36.359 5.797   1.00 77.23  ? 1227 LYS A N     1 
ATOM   50   C  CA    . LYS A 1 10  ? -1.743  -36.252 6.849   1.00 71.79  ? 1227 LYS A CA    1 
ATOM   51   C  C     . LYS A 1 10  ? -1.471  -37.238 7.981   1.00 73.88  ? 1227 LYS A C     1 
ATOM   52   O  O     . LYS A 1 10  ? -1.669  -36.917 9.155   1.00 77.56  ? 1227 LYS A O     1 
ATOM   53   C  CB    . LYS A 1 10  ? -3.117  -36.486 6.214   1.00 74.04  ? 1227 LYS A CB    1 
ATOM   54   C  CG    . LYS A 1 10  ? -4.301  -35.753 6.797   1.00 74.75  ? 1227 LYS A CG    1 
ATOM   55   C  CD    . LYS A 1 10  ? -5.581  -36.350 6.208   1.00 81.11  ? 1227 LYS A CD    1 
ATOM   56   C  CE    . LYS A 1 10  ? -6.847  -35.747 6.796   1.00 74.84  ? 1227 LYS A CE    1 
ATOM   57   N  NZ    . LYS A 1 10  ? -7.881  -35.387 5.761   1.00 59.83  ? 1227 LYS A NZ    1 
ATOM   58   N  N     . GLU A 1 11  ? -1.007  -38.435 7.649   1.00 78.72  ? 1228 GLU A N     1 
ATOM   59   C  CA    . GLU A 1 11  ? -0.908  -39.522 8.618   1.00 81.35  ? 1228 GLU A CA    1 
ATOM   60   C  C     . GLU A 1 11  ? 0.358   -39.502 9.457   1.00 86.97  ? 1228 GLU A C     1 
ATOM   61   O  O     . GLU A 1 11  ? 0.339   -39.981 10.593  1.00 81.50  ? 1228 GLU A O     1 
ATOM   62   C  CB    . GLU A 1 11  ? -0.988  -40.868 7.919   1.00 79.80  ? 1228 GLU A CB    1 
ATOM   63   C  CG    . GLU A 1 11  ? -2.235  -41.034 7.071   1.00 94.88  ? 1228 GLU A CG    1 
ATOM   64   C  CD    . GLU A 1 11  ? -2.088  -40.382 5.714   1.00 107.81 ? 1228 GLU A CD    1 
ATOM   65   O  OE1   . GLU A 1 11  ? -3.111  -40.194 5.014   1.00 100.30 ? 1228 GLU A OE1   1 
ATOM   66   O  OE2   . GLU A 1 11  ? -0.932  -40.049 5.359   1.00 119.43 ? 1228 GLU A OE2   1 
ATOM   67   N  N     . ASP A 1 12  ? 1.447   -38.945 8.933   1.00 92.02  ? 1229 ASP A N     1 
ATOM   68   C  CA    . ASP A 1 12  ? 2.718   -39.033 9.645   1.00 108.86 ? 1229 ASP A CA    1 
ATOM   69   C  C     . ASP A 1 12  ? 3.054   -37.751 10.392  1.00 117.66 ? 1229 ASP A C     1 
ATOM   70   O  O     . ASP A 1 12  ? 3.502   -37.796 11.538  1.00 133.27 ? 1229 ASP A O     1 
ATOM   71   C  CB    . ASP A 1 12  ? 3.849   -39.337 8.659   1.00 118.62 ? 1229 ASP A CB    1 
ATOM   72   C  CG    . ASP A 1 12  ? 3.554   -40.522 7.778   1.00 122.45 ? 1229 ASP A CG    1 
ATOM   73   O  OD1   . ASP A 1 12  ? 3.446   -41.661 8.296   1.00 122.23 ? 1229 ASP A OD1   1 
ATOM   74   O  OD2   . ASP A 1 12  ? 3.433   -40.302 6.554   1.00 123.09 ? 1229 ASP A OD2   1 
ATOM   75   N  N     . ASN A 1 13  ? 2.847   -36.599 9.762   1.00 109.13 ? 1230 ASN A N     1 
ATOM   76   C  CA    . ASN A 1 13  ? 3.076   -35.316 10.421  1.00 107.88 ? 1230 ASN A CA    1 
ATOM   77   C  C     . ASN A 1 13  ? 1.848   -34.452 10.171  1.00 101.54 ? 1230 ASN A C     1 
ATOM   78   O  O     . ASN A 1 13  ? 1.824   -33.622 9.254   1.00 97.19  ? 1230 ASN A O     1 
ATOM   79   C  CB    . ASN A 1 13  ? 4.351   -34.650 9.906   1.00 114.23 ? 1230 ASN A CB    1 
ATOM   80   C  CG    . ASN A 1 13  ? 4.787   -33.476 10.763  1.00 109.30 ? 1230 ASN A CG    1 
ATOM   81   O  OD1   . ASN A 1 13  ? 4.147   -33.141 11.756  1.00 104.35 ? 1230 ASN A OD1   1 
ATOM   82   N  ND2   . ASN A 1 13  ? 5.898   -32.850 10.380  1.00 106.92 ? 1230 ASN A ND2   1 
ATOM   83   N  N     . LEU A 1 14  ? 0.839   -34.613 11.020  1.00 90.54  ? 1231 LEU A N     1 
ATOM   84   C  CA    . LEU A 1 14  ? -0.405  -33.881 10.803  1.00 79.93  ? 1231 LEU A CA    1 
ATOM   85   C  C     . LEU A 1 14  ? -0.222  -32.373 10.903  1.00 74.80  ? 1231 LEU A C     1 
ATOM   86   O  O     . LEU A 1 14  ? -0.774  -31.661 10.053  1.00 76.46  ? 1231 LEU A O     1 
ATOM   87   C  CB    . LEU A 1 14  ? -1.494  -34.382 11.761  1.00 74.51  ? 1231 LEU A CB    1 
ATOM   88   C  CG    . LEU A 1 14  ? -2.930  -33.902 11.438  1.00 73.55  ? 1231 LEU A CG    1 
ATOM   89   C  CD1   . LEU A 1 14  ? -3.489  -34.490 10.143  1.00 69.83  ? 1231 LEU A CD1   1 
ATOM   90   C  CD2   . LEU A 1 14  ? -3.880  -34.169 12.586  1.00 49.68  ? 1231 LEU A CD2   1 
ATOM   91   N  N     . PRO A 1 15  ? 0.477   -31.818 11.898  1.00 74.73  ? 1232 PRO A N     1 
ATOM   92   C  CA    . PRO A 1 15  ? 0.557   -30.350 11.987  1.00 67.81  ? 1232 PRO A CA    1 
ATOM   93   C  C     . PRO A 1 15  ? 1.278   -29.711 10.821  1.00 75.90  ? 1232 PRO A C     1 
ATOM   94   O  O     . PRO A 1 15  ? 0.813   -28.697 10.291  1.00 78.78  ? 1232 PRO A O     1 
ATOM   95   C  CB    . PRO A 1 15  ? 1.318   -30.121 13.296  1.00 68.95  ? 1232 PRO A CB    1 
ATOM   96   C  CG    . PRO A 1 15  ? 1.002   -31.325 14.112  1.00 85.66  ? 1232 PRO A CG    1 
ATOM   97   C  CD    . PRO A 1 15  ? 0.973   -32.457 13.128  1.00 87.14  ? 1232 PRO A CD    1 
ATOM   98   N  N     . ASP A 1 16  ? 2.400   -30.276 10.384  1.00 85.29  ? 1233 ASP A N     1 
ATOM   99   C  CA    . ASP A 1 16  ? 3.066   -29.657 9.252   1.00 86.85  ? 1233 ASP A CA    1 
ATOM   100  C  C     . ASP A 1 16  ? 2.283   -29.911 7.975   1.00 87.40  ? 1233 ASP A C     1 
ATOM   101  O  O     . ASP A 1 16  ? 2.214   -29.032 7.110   1.00 89.56  ? 1233 ASP A O     1 
ATOM   102  C  CB    . ASP A 1 16  ? 4.500   -30.175 9.137   1.00 83.40  ? 1233 ASP A CB    1 
ATOM   103  C  CG    . ASP A 1 16  ? 5.323   -29.856 10.372  1.00 92.89  ? 1233 ASP A CG    1 
ATOM   104  O  OD1   . ASP A 1 16  ? 4.819   -29.129 11.248  1.00 94.97  ? 1233 ASP A OD1   1 
ATOM   105  O  OD2   . ASP A 1 16  ? 6.465   -30.348 10.488  1.00 104.28 ? 1233 ASP A OD2   1 
ATOM   106  N  N     . TRP A 1 17  ? 1.571   -31.036 7.899   1.00 81.31  ? 1234 TRP A N     1 
ATOM   107  C  CA    . TRP A 1 17  ? 0.656   -31.220 6.784   1.00 77.28  ? 1234 TRP A CA    1 
ATOM   108  C  C     . TRP A 1 17  ? -0.408  -30.127 6.757   1.00 75.54  ? 1234 TRP A C     1 
ATOM   109  O  O     . TRP A 1 17  ? -0.665  -29.536 5.700   1.00 78.35  ? 1234 TRP A O     1 
ATOM   110  C  CB    . TRP A 1 17  ? 0.015   -32.611 6.855   1.00 73.09  ? 1234 TRP A CB    1 
ATOM   111  C  CG    . TRP A 1 17  ? -1.101  -32.759 5.877   1.00 74.74  ? 1234 TRP A CG    1 
ATOM   112  C  CD1   . TRP A 1 17  ? -1.003  -33.081 4.551   1.00 76.63  ? 1234 TRP A CD1   1 
ATOM   113  C  CD2   . TRP A 1 17  ? -2.491  -32.536 6.133   1.00 74.18  ? 1234 TRP A CD2   1 
ATOM   114  N  NE1   . TRP A 1 17  ? -2.253  -33.077 3.965   1.00 73.09  ? 1234 TRP A NE1   1 
ATOM   115  C  CE2   . TRP A 1 17  ? -3.182  -32.748 4.917   1.00 69.93  ? 1234 TRP A CE2   1 
ATOM   116  C  CE3   . TRP A 1 17  ? -3.221  -32.172 7.273   1.00 65.63  ? 1234 TRP A CE3   1 
ATOM   117  C  CZ2   . TRP A 1 17  ? -4.562  -32.627 4.817   1.00 63.15  ? 1234 TRP A CZ2   1 
ATOM   118  C  CZ3   . TRP A 1 17  ? -4.583  -32.046 7.166   1.00 52.67  ? 1234 TRP A CZ3   1 
ATOM   119  C  CH2   . TRP A 1 17  ? -5.243  -32.277 5.949   1.00 54.60  ? 1234 TRP A CH2   1 
ATOM   120  N  N     . TYR A 1 18  ? -0.995  -29.813 7.924   1.00 77.44  ? 1235 TYR A N     1 
ATOM   121  C  CA    . TYR A 1 18  ? -2.070  -28.813 8.045   1.00 76.61  ? 1235 TYR A CA    1 
ATOM   122  C  C     . TYR A 1 18  ? -1.573  -27.413 7.690   1.00 70.86  ? 1235 TYR A C     1 
ATOM   123  O  O     . TYR A 1 18  ? -2.274  -26.658 6.999   1.00 75.64  ? 1235 TYR A O     1 
ATOM   124  C  CB    . TYR A 1 18  ? -2.634  -28.864 9.474   1.00 72.96  ? 1235 TYR A CB    1 
ATOM   125  C  CG    . TYR A 1 18  ? -3.814  -27.970 9.798   1.00 77.28  ? 1235 TYR A CG    1 
ATOM   126  C  CD1   . TYR A 1 18  ? -5.096  -28.272 9.361   1.00 73.08  ? 1235 TYR A CD1   1 
ATOM   127  C  CD2   . TYR A 1 18  ? -3.650  -26.838 10.597  1.00 85.26  ? 1235 TYR A CD2   1 
ATOM   128  C  CE1   . TYR A 1 18  ? -6.186  -27.452 9.695   1.00 73.86  ? 1235 TYR A CE1   1 
ATOM   129  C  CE2   . TYR A 1 18  ? -4.725  -26.005 10.931  1.00 74.42  ? 1235 TYR A CE2   1 
ATOM   130  C  CZ    . TYR A 1 18  ? -5.989  -26.317 10.482  1.00 75.36  ? 1235 TYR A CZ    1 
ATOM   131  O  OH    . TYR A 1 18  ? -7.052  -25.495 10.823  1.00 71.34  ? 1235 TYR A OH    1 
ATOM   132  N  N     . SER A 1 19  ? -0.350  -27.077 8.136   1.00 66.62  ? 1236 SER A N     1 
ATOM   133  C  CA    . SER A 1 19  ? 0.240   -25.784 7.842   1.00 71.10  ? 1236 SER A CA    1 
ATOM   134  C  C     . SER A 1 19  ? 0.566   -25.657 6.354   1.00 69.39  ? 1236 SER A C     1 
ATOM   135  O  O     . SER A 1 19  ? 0.346   -24.606 5.743   1.00 71.89  ? 1236 SER A O     1 
ATOM   136  C  CB    . SER A 1 19  ? 1.517   -25.587 8.669   1.00 75.38  ? 1236 SER A CB    1 
ATOM   137  O  OG    . SER A 1 19  ? 2.385   -24.629 8.078   1.00 91.65  ? 1236 SER A OG    1 
ATOM   138  N  N     . GLN A 1 20  ? 1.004   -26.745 5.736   1.00 64.41  ? 1237 GLN A N     1 
ATOM   139  C  CA    . GLN A 1 20  ? 1.252   -26.754 4.303   1.00 69.46  ? 1237 GLN A CA    1 
ATOM   140  C  C     . GLN A 1 20  ? -0.035  -26.643 3.497   1.00 72.85  ? 1237 GLN A C     1 
ATOM   141  O  O     . GLN A 1 20  ? -0.049  -25.992 2.451   1.00 71.42  ? 1237 GLN A O     1 
ATOM   142  C  CB    . GLN A 1 20  ? 1.980   -28.063 3.921   1.00 87.77  ? 1237 GLN A CB    1 
ATOM   143  C  CG    . GLN A 1 20  ? 3.402   -28.177 4.461   1.00 99.36  ? 1237 GLN A CG    1 
ATOM   144  C  CD    . GLN A 1 20  ? 4.321   -27.184 3.822   1.00 107.96 ? 1237 GLN A CD    1 
ATOM   145  O  OE1   . GLN A 1 20  ? 4.670   -27.341 2.667   1.00 117.83 ? 1237 GLN A OE1   1 
ATOM   146  N  NE2   . GLN A 1 20  ? 4.694   -26.129 4.558   1.00 104.48 ? 1237 GLN A NE2   1 
ATOM   147  N  N     . VAL A 1 21  ? -1.135  -27.226 3.968   1.00 74.87  ? 1238 VAL A N     1 
ATOM   148  C  CA    . VAL A 1 21  ? -2.376  -27.145 3.191   1.00 82.21  ? 1238 VAL A CA    1 
ATOM   149  C  C     . VAL A 1 21  ? -3.055  -25.777 3.352   1.00 81.81  ? 1238 VAL A C     1 
ATOM   150  O  O     . VAL A 1 21  ? -3.644  -25.253 2.395   1.00 68.10  ? 1238 VAL A O     1 
ATOM   151  C  CB    . VAL A 1 21  ? -3.317  -28.330 3.511   1.00 81.19  ? 1238 VAL A CB    1 
ATOM   152  C  CG1   . VAL A 1 21  ? -3.456  -28.530 4.970   1.00 78.01  ? 1238 VAL A CG1   1 
ATOM   153  C  CG2   . VAL A 1 21  ? -4.697  -28.133 2.882   1.00 86.57  ? 1238 VAL A CG2   1 
ATOM   154  N  N     . ILE A 1 22  ? -2.985  -25.161 4.542   1.00 84.34  ? 1239 ILE A N     1 
ATOM   155  C  CA    . ILE A 1 22  ? -3.608  -23.839 4.669   1.00 79.84  ? 1239 ILE A CA    1 
ATOM   156  C  C     . ILE A 1 22  ? -2.735  -22.748 4.049   1.00 79.37  ? 1239 ILE A C     1 
ATOM   157  O  O     . ILE A 1 22  ? -3.260  -21.713 3.611   1.00 69.87  ? 1239 ILE A O     1 
ATOM   158  C  CB    . ILE A 1 22  ? -3.917  -23.479 6.127   1.00 66.67  ? 1239 ILE A CB    1 
ATOM   159  C  CG1   . ILE A 1 22  ? -2.627  -23.534 6.946   1.00 63.11  ? 1239 ILE A CG1   1 
ATOM   160  C  CG2   . ILE A 1 22  ? -5.023  -24.359 6.671   1.00 51.16  ? 1239 ILE A CG2   1 
ATOM   161  C  CD1   . ILE A 1 22  ? -2.864  -23.389 8.388   1.00 52.03  ? 1239 ILE A CD1   1 
ATOM   162  N  N     . THR A 1 23  ? -1.413  -22.943 3.983   1.00 78.78  ? 1240 THR A N     1 
ATOM   163  C  CA    . THR A 1 23  ? -0.613  -21.936 3.296   1.00 67.81  ? 1240 THR A CA    1 
ATOM   164  C  C     . THR A 1 23  ? -0.532  -22.193 1.791   1.00 67.71  ? 1240 THR A C     1 
ATOM   165  O  O     . THR A 1 23  ? -0.856  -21.328 0.986   1.00 62.11  ? 1240 THR A O     1 
ATOM   166  C  CB    . THR A 1 23  ? 0.786   -21.860 3.910   1.00 63.81  ? 1240 THR A CB    1 
ATOM   167  O  OG1   . THR A 1 23  ? 1.330   -23.173 4.015   1.00 71.68  ? 1240 THR A OG1   1 
ATOM   168  C  CG2   . THR A 1 23  ? 0.738   -21.200 5.294   1.00 59.00  ? 1240 THR A CG2   1 
ATOM   169  N  N     . LYS A 1 24  ? -0.186  -23.394 1.371   1.00 75.66  ? 1241 LYS A N     1 
ATOM   170  C  CA    . LYS A 1 24  ? -0.094  -23.575 -0.068  1.00 80.56  ? 1241 LYS A CA    1 
ATOM   171  C  C     . LYS A 1 24  ? -1.486  -23.606 -0.709  1.00 72.36  ? 1241 LYS A C     1 
ATOM   172  O  O     . LYS A 1 24  ? -1.611  -23.401 -1.931  1.00 71.20  ? 1241 LYS A O     1 
ATOM   173  C  CB    . LYS A 1 24  ? 0.691   -24.862 -0.303  1.00 76.23  ? 1241 LYS A CB    1 
ATOM   174  C  CG    . LYS A 1 24  ? 2.082   -24.902 0.390   1.00 88.81  ? 1241 LYS A CG    1 
ATOM   175  C  CD    . LYS A 1 24  ? 2.968   -25.832 -0.447  1.00 96.28  ? 1241 LYS A CD    1 
ATOM   176  C  CE    . LYS A 1 24  ? 4.364   -26.194 0.085   1.00 105.45 ? 1241 LYS A CE    1 
ATOM   177  N  NZ    . LYS A 1 24  ? 5.483   -25.972 -0.874  1.00 108.77 ? 1241 LYS A NZ    1 
ATOM   178  N  N     . GLY A 1 25  ? -2.556  -23.776 0.092   1.00 63.10  ? 1242 GLY A N     1 
ATOM   179  C  CA    . GLY A 1 25  ? -3.922  -23.582 -0.344  1.00 47.01  ? 1242 GLY A CA    1 
ATOM   180  C  C     . GLY A 1 25  ? -4.393  -22.146 -0.242  1.00 68.02  ? 1242 GLY A C     1 
ATOM   181  O  O     . GLY A 1 25  ? -5.561  -21.866 -0.532  1.00 66.38  ? 1242 GLY A O     1 
ATOM   182  N  N     . GLU A 1 26  ? -3.463  -21.272 0.014   1.00 75.78  ? 1243 GLU A N     1 
ATOM   183  C  CA    . GLU A 1 26  ? -3.657  -19.862 0.069   1.00 82.13  ? 1243 GLU A CA    1 
ATOM   184  C  C     . GLU A 1 26  ? -4.775  -19.491 0.929   1.00 82.39  ? 1243 GLU A C     1 
ATOM   185  O  O     . GLU A 1 26  ? -5.499  -18.602 0.652   1.00 72.33  ? 1243 GLU A O     1 
ATOM   186  C  CB    . GLU A 1 26  ? -3.814  -19.300 -1.321  1.00 82.26  ? 1243 GLU A CB    1 
ATOM   187  C  CG    . GLU A 1 26  ? -2.782  -19.794 -2.285  1.00 76.87  ? 1243 GLU A CG    1 
ATOM   188  C  CD    . GLU A 1 26  ? -2.767  -19.024 -3.561  1.00 85.51  ? 1243 GLU A CD    1 
ATOM   189  O  OE1   . GLU A 1 26  ? -1.999  -19.345 -4.440  1.00 80.17  ? 1243 GLU A OE1   1 
ATOM   190  O  OE2   . GLU A 1 26  ? -3.524  -18.083 -3.690  1.00 94.10  ? 1243 GLU A OE2   1 
ATOM   191  N  N     . MET A 1 27  ? -4.881  -20.165 2.028   1.00 84.16  ? 1244 MET A N     1 
ATOM   192  C  CA    . MET A 1 27  ? -5.953  -19.888 2.901   1.00 79.71  ? 1244 MET A CA    1 
ATOM   193  C  C     . MET A 1 27  ? -5.607  -19.130 4.138   1.00 79.60  ? 1244 MET A C     1 
ATOM   194  O  O     . MET A 1 27  ? -6.443  -18.646 4.782   1.00 74.39  ? 1244 MET A O     1 
ATOM   195  C  CB    . MET A 1 27  ? -6.499  -21.212 3.296   1.00 73.77  ? 1244 MET A CB    1 
ATOM   196  C  CG    . MET A 1 27  ? -7.931  -21.141 3.573   1.00 76.86  ? 1244 MET A CG    1 
ATOM   197  S  SD    . MET A 1 27  ? -8.728  -22.655 3.313   1.00 85.53  ? 1244 MET A SD    1 
ATOM   198  C  CE    . MET A 1 27  ? -8.765  -22.544 1.600   1.00 91.32  ? 1244 MET A CE    1 
ATOM   199  N  N     . ILE A 1 28  ? -4.347  -18.994 4.469   1.00 83.80  ? 1245 ILE A N     1 
ATOM   200  C  CA    . ILE A 1 28  ? -3.947  -18.387 5.710   1.00 72.27  ? 1245 ILE A CA    1 
ATOM   201  C  C     . ILE A 1 28  ? -2.578  -17.784 5.569   1.00 78.23  ? 1245 ILE A C     1 
ATOM   202  O  O     . ILE A 1 28  ? -1.832  -18.268 4.798   1.00 76.65  ? 1245 ILE A O     1 
ATOM   203  C  CB    . ILE A 1 28  ? -3.780  -19.554 6.694   1.00 73.37  ? 1245 ILE A CB    1 
ATOM   204  C  CG1   . ILE A 1 28  ? -5.048  -19.963 7.358   1.00 69.94  ? 1245 ILE A CG1   1 
ATOM   205  C  CG2   . ILE A 1 28  ? -2.898  -19.280 7.867   1.00 64.04  ? 1245 ILE A CG2   1 
ATOM   206  C  CD1   . ILE A 1 28  ? -5.567  -18.931 8.268   1.00 59.37  ? 1245 ILE A CD1   1 
ATOM   207  N  N     . GLU A 1 29  ? -2.319  -16.628 6.161   1.00 77.43  ? 1246 GLU A N     1 
ATOM   208  C  CA    . GLU A 1 29  ? -0.970  -16.098 6.307   1.00 75.68  ? 1246 GLU A CA    1 
ATOM   209  C  C     . GLU A 1 29  ? -0.698  -15.858 7.786   1.00 73.22  ? 1246 GLU A C     1 
ATOM   210  O  O     . GLU A 1 29  ? -1.579  -15.407 8.524   1.00 69.80  ? 1246 GLU A O     1 
ATOM   211  C  CB    . GLU A 1 29  ? -0.723  -14.810 5.514   1.00 77.72  ? 1246 GLU A CB    1 
ATOM   212  C  CG    . GLU A 1 29  ? 0.794   -14.490 5.367   1.00 74.55  ? 1246 GLU A CG    1 
ATOM   213  C  CD    . GLU A 1 29  ? 1.515   -15.567 4.556   1.00 80.47  ? 1246 GLU A CD    1 
ATOM   214  O  OE1   . GLU A 1 29  ? 1.205   -15.678 3.344   1.00 80.10  ? 1246 GLU A OE1   1 
ATOM   215  O  OE2   . GLU A 1 29  ? 2.348   -16.325 5.135   1.00 77.49  ? 1246 GLU A OE2   1 
ATOM   216  N  N     . TYR A 1 30  ? 0.511   -16.206 8.221   1.00 77.99  ? 1247 TYR A N     1 
ATOM   217  C  CA    . TYR A 1 30  ? 0.889   -16.125 9.622   1.00 78.24  ? 1247 TYR A CA    1 
ATOM   218  C  C     . TYR A 1 30  ? 1.136   -14.667 10.028  1.00 82.95  ? 1247 TYR A C     1 
ATOM   219  O  O     . TYR A 1 30  ? 1.166   -13.751 9.198   1.00 77.90  ? 1247 TYR A O     1 
ATOM   220  C  CB    . TYR A 1 30  ? 2.085   -17.026 9.894   1.00 78.37  ? 1247 TYR A CB    1 
ATOM   221  C  CG    . TYR A 1 30  ? 1.737   -18.507 9.786   1.00 72.92  ? 1247 TYR A CG    1 
ATOM   222  C  CD1   . TYR A 1 30  ? 1.201   -19.188 10.873  1.00 70.56  ? 1247 TYR A CD1   1 
ATOM   223  C  CD2   . TYR A 1 30  ? 1.948   -19.215 8.605   1.00 57.67  ? 1247 TYR A CD2   1 
ATOM   224  C  CE1   . TYR A 1 30  ? 0.883   -20.520 10.804  1.00 71.63  ? 1247 TYR A CE1   1 
ATOM   225  C  CE2   . TYR A 1 30  ? 1.647   -20.558 8.518   1.00 68.18  ? 1247 TYR A CE2   1 
ATOM   226  C  CZ    . TYR A 1 30  ? 1.096   -21.217 9.624   1.00 81.78  ? 1247 TYR A CZ    1 
ATOM   227  O  OH    . TYR A 1 30  ? 0.749   -22.574 9.567   1.00 75.50  ? 1247 TYR A OH    1 
ATOM   228  N  N     . TYR A 1 31  ? 1.245   -14.451 11.339  1.00 82.12  ? 1248 TYR A N     1 
ATOM   229  C  CA    . TYR A 1 31  ? 1.043   -13.122 11.898  1.00 75.33  ? 1248 TYR A CA    1 
ATOM   230  C  C     . TYR A 1 31  ? 1.927   -12.904 13.108  1.00 76.53  ? 1248 TYR A C     1 
ATOM   231  O  O     . TYR A 1 31  ? 2.134   -13.820 13.906  1.00 72.46  ? 1248 TYR A O     1 
ATOM   232  C  CB    . TYR A 1 31  ? -0.401  -12.943 12.337  1.00 71.96  ? 1248 TYR A CB    1 
ATOM   233  C  CG    . TYR A 1 31  ? -0.806  -11.511 12.495  1.00 74.38  ? 1248 TYR A CG    1 
ATOM   234  C  CD1   . TYR A 1 31  ? -0.872  -10.673 11.398  1.00 78.10  ? 1248 TYR A CD1   1 
ATOM   235  C  CD2   . TYR A 1 31  ? -1.131  -10.996 13.735  1.00 76.29  ? 1248 TYR A CD2   1 
ATOM   236  C  CE1   . TYR A 1 31  ? -1.239  -9.364  11.533  1.00 80.59  ? 1248 TYR A CE1   1 
ATOM   237  C  CE2   . TYR A 1 31  ? -1.513  -9.680  13.880  1.00 87.05  ? 1248 TYR A CE2   1 
ATOM   238  C  CZ    . TYR A 1 31  ? -1.562  -8.864  12.774  1.00 90.03  ? 1248 TYR A CZ    1 
ATOM   239  O  OH    . TYR A 1 31  ? -1.934  -7.542  12.909  1.00 95.99  ? 1248 TYR A OH    1 
ATOM   240  N  N     . ASP A 1 32  ? 2.390   -11.658 13.273  1.00 86.81  ? 1249 ASP A N     1 
ATOM   241  C  CA    . ASP A 1 32  ? 3.351   -11.342 14.324  1.00 84.38  ? 1249 ASP A CA    1 
ATOM   242  C  C     . ASP A 1 32  ? 2.687   -11.127 15.677  1.00 77.85  ? 1249 ASP A C     1 
ATOM   243  O  O     . ASP A 1 32  ? 3.347   -10.658 16.612  1.00 81.82  ? 1249 ASP A O     1 
ATOM   244  C  CB    . ASP A 1 32  ? 4.217   -10.126 13.935  1.00 85.99  ? 1249 ASP A CB    1 
ATOM   245  C  CG    . ASP A 1 32  ? 3.455   -8.795  13.930  1.00 84.67  ? 1249 ASP A CG    1 
ATOM   246  O  OD1   . ASP A 1 32  ? 2.274   -8.758  13.514  1.00 85.77  ? 1249 ASP A OD1   1 
ATOM   247  O  OD2   . ASP A 1 32  ? 4.070   -7.765  14.326  1.00 75.36  ? 1249 ASP A OD2   1 
ATOM   248  N  N     . VAL A 1 33  ? 1.407   -11.464 15.801  1.00 71.68  ? 1250 VAL A N     1 
ATOM   249  C  CA    . VAL A 1 33  ? 0.718   -11.552 17.086  1.00 72.40  ? 1250 VAL A CA    1 
ATOM   250  C  C     . VAL A 1 33  ? 0.289   -12.997 17.255  1.00 71.39  ? 1250 VAL A C     1 
ATOM   251  O  O     . VAL A 1 33  ? -0.468  -13.525 16.426  1.00 70.59  ? 1250 VAL A O     1 
ATOM   252  C  CB    . VAL A 1 33  ? -0.502  -10.617 17.175  1.00 70.32  ? 1250 VAL A CB    1 
ATOM   253  C  CG1   . VAL A 1 33  ? -1.179  -10.786 18.518  1.00 73.39  ? 1250 VAL A CG1   1 
ATOM   254  C  CG2   . VAL A 1 33  ? -0.113  -9.168  16.960  1.00 60.31  ? 1250 VAL A CG2   1 
ATOM   255  N  N     . SER A 1 34  ? 0.738   -13.629 18.333  1.00 79.19  ? 1251 SER A N     1 
ATOM   256  C  CA    . SER A 1 34  ? 0.514   -15.059 18.463  1.00 92.02  ? 1251 SER A CA    1 
ATOM   257  C  C     . SER A 1 34  ? -0.976  -15.343 18.716  1.00 90.82  ? 1251 SER A C     1 
ATOM   258  O  O     . SER A 1 34  ? -1.709  -14.532 19.291  1.00 80.79  ? 1251 SER A O     1 
ATOM   259  C  CB    . SER A 1 34  ? 1.422   -15.618 19.565  1.00 89.66  ? 1251 SER A CB    1 
ATOM   260  O  OG    . SER A 1 34  ? 0.914   -16.784 20.188  1.00 98.23  ? 1251 SER A OG    1 
ATOM   261  N  N     . GLY A 1 35  ? -1.430  -16.503 18.237  1.00 85.75  ? 1252 GLY A N     1 
ATOM   262  C  CA    . GLY A 1 35  ? -2.826  -16.875 18.325  1.00 84.86  ? 1252 GLY A CA    1 
ATOM   263  C  C     . GLY A 1 35  ? -3.743  -16.294 17.267  1.00 81.54  ? 1252 GLY A C     1 
ATOM   264  O  O     . GLY A 1 35  ? -4.908  -16.735 17.170  1.00 75.56  ? 1252 GLY A O     1 
ATOM   265  N  N     . CYS A 1 36  ? -3.247  -15.364 16.439  1.00 72.73  ? 1253 CYS A N     1 
ATOM   266  C  CA    . CYS A 1 36  ? -4.066  -14.616 15.486  1.00 64.03  ? 1253 CYS A CA    1 
ATOM   267  C  C     . CYS A 1 36  ? -3.524  -14.840 14.080  1.00 64.35  ? 1253 CYS A C     1 
ATOM   268  O  O     . CYS A 1 36  ? -2.313  -14.940 13.886  1.00 73.35  ? 1253 CYS A O     1 
ATOM   269  C  CB    . CYS A 1 36  ? -4.073  -13.126 15.834  1.00 57.06  ? 1253 CYS A CB    1 
ATOM   270  S  SG    . CYS A 1 36  ? -4.375  -12.783 17.620  1.00 81.21  ? 1253 CYS A SG    1 
ATOM   271  N  N     . TYR A 1 37  ? -4.425  -14.964 13.112  1.00 62.14  ? 1254 TYR A N     1 
ATOM   272  C  CA    . TYR A 1 37  ? -4.080  -15.419 11.772  1.00 61.19  ? 1254 TYR A CA    1 
ATOM   273  C  C     . TYR A 1 37  ? -4.870  -14.625 10.741  1.00 65.34  ? 1254 TYR A C     1 
ATOM   274  O  O     . TYR A 1 37  ? -6.024  -14.231 10.966  1.00 68.33  ? 1254 TYR A O     1 
ATOM   275  C  CB    . TYR A 1 37  ? -4.364  -16.938 11.565  1.00 52.58  ? 1254 TYR A CB    1 
ATOM   276  C  CG    . TYR A 1 37  ? -3.712  -17.827 12.604  1.00 65.87  ? 1254 TYR A CG    1 
ATOM   277  C  CD1   . TYR A 1 37  ? -2.417  -18.315 12.422  1.00 62.92  ? 1254 TYR A CD1   1 
ATOM   278  C  CD2   . TYR A 1 37  ? -4.385  -18.166 13.783  1.00 67.33  ? 1254 TYR A CD2   1 
ATOM   279  C  CE1   . TYR A 1 37  ? -1.807  -19.102 13.380  1.00 63.06  ? 1254 TYR A CE1   1 
ATOM   280  C  CE2   . TYR A 1 37  ? -3.781  -18.954 14.750  1.00 71.96  ? 1254 TYR A CE2   1 
ATOM   281  C  CZ    . TYR A 1 37  ? -2.486  -19.417 14.543  1.00 76.81  ? 1254 TYR A CZ    1 
ATOM   282  O  OH    . TYR A 1 37  ? -1.861  -20.211 15.487  1.00 94.61  ? 1254 TYR A OH    1 
ATOM   283  N  N     . ILE A 1 38  ? -4.227  -14.391 9.606   1.00 56.67  ? 1255 ILE A N     1 
ATOM   284  C  CA    . ILE A 1 38  ? -4.853  -13.669 8.508   1.00 61.75  ? 1255 ILE A CA    1 
ATOM   285  C  C     . ILE A 1 38  ? -5.691  -14.651 7.695   1.00 62.52  ? 1255 ILE A C     1 
ATOM   286  O  O     . ILE A 1 38  ? -5.161  -15.631 7.162   1.00 73.04  ? 1255 ILE A O     1 
ATOM   287  C  CB    . ILE A 1 38  ? -3.792  -12.978 7.633   1.00 53.05  ? 1255 ILE A CB    1 
ATOM   288  C  CG1   . ILE A 1 38  ? -3.171  -11.799 8.387   1.00 48.54  ? 1255 ILE A CG1   1 
ATOM   289  C  CG2   . ILE A 1 38  ? -4.397  -12.547 6.298   1.00 55.54  ? 1255 ILE A CG2   1 
ATOM   290  C  CD1   . ILE A 1 38  ? -1.792  -11.442 7.944   1.00 50.63  ? 1255 ILE A CD1   1 
ATOM   291  N  N     . LEU A 1 39  ? -6.997  -14.396 7.606   1.00 48.88  ? 1256 LEU A N     1 
ATOM   292  C  CA    . LEU A 1 39  ? -7.851  -15.155 6.694   1.00 58.27  ? 1256 LEU A CA    1 
ATOM   293  C  C     . LEU A 1 39  ? -7.771  -14.519 5.310   1.00 54.65  ? 1256 LEU A C     1 
ATOM   294  O  O     . LEU A 1 39  ? -8.347  -13.458 5.061   1.00 56.02  ? 1256 LEU A O     1 
ATOM   295  C  CB    . LEU A 1 39  ? -9.291  -15.206 7.197   1.00 65.52  ? 1256 LEU A CB    1 
ATOM   296  C  CG    . LEU A 1 39  ? -9.437  -15.434 8.700   1.00 67.27  ? 1256 LEU A CG    1 
ATOM   297  C  CD1   . LEU A 1 39  ? -10.893 -15.267 9.152   1.00 52.89  ? 1256 LEU A CD1   1 
ATOM   298  C  CD2   . LEU A 1 39  ? -8.867  -16.807 9.090   1.00 71.24  ? 1256 LEU A CD2   1 
ATOM   299  N  N     . ARG A 1 40  ? -7.008  -15.142 4.421   1.00 46.79  ? 1257 ARG A N     1 
ATOM   300  C  CA    . ARG A 1 40  ? -6.961  -14.642 3.061   1.00 54.09  ? 1257 ARG A CA    1 
ATOM   301  C  C     . ARG A 1 40  ? -8.292  -14.936 2.416   1.00 53.35  ? 1257 ARG A C     1 
ATOM   302  O  O     . ARG A 1 40  ? -9.123  -15.680 2.967   1.00 61.32  ? 1257 ARG A O     1 
ATOM   303  C  CB    . ARG A 1 40  ? -5.789  -15.262 2.289   1.00 67.55  ? 1257 ARG A CB    1 
ATOM   304  C  CG    . ARG A 1 40  ? -4.403  -15.077 2.957   1.00 66.58  ? 1257 ARG A CG    1 
ATOM   305  C  CD    . ARG A 1 40  ? -3.232  -15.749 2.203   1.00 68.02  ? 1257 ARG A CD    1 
ATOM   306  N  NE    . ARG A 1 40  ? -3.160  -15.416 0.777   1.00 65.63  ? 1257 ARG A NE    1 
ATOM   307  C  CZ    . ARG A 1 40  ? -2.310  -15.976 -0.088  1.00 68.16  ? 1257 ARG A CZ    1 
ATOM   308  N  NH1   . ARG A 1 40  ? -1.440  -16.910 0.318   1.00 73.25  ? 1257 ARG A NH1   1 
ATOM   309  N  NH2   . ARG A 1 40  ? -2.334  -15.601 -1.368  1.00 62.51  ? 1257 ARG A NH2   1 
ATOM   310  N  N     . HIS A 1 41  ? -8.501  -14.368 1.230   1.00 58.62  ? 1258 HIS A N     1 
ATOM   311  C  CA    . HIS A 1 41  ? -9.850  -14.404 0.666   1.00 60.91  ? 1258 HIS A CA    1 
ATOM   312  C  C     . HIS A 1 41  ? -10.338 -15.832 0.381   1.00 67.75  ? 1258 HIS A C     1 
ATOM   313  O  O     . HIS A 1 41  ? -11.548 -16.096 0.472   1.00 68.84  ? 1258 HIS A O     1 
ATOM   314  C  CB    . HIS A 1 41  ? -9.926  -13.502 -0.562  1.00 52.05  ? 1258 HIS A CB    1 
ATOM   315  C  CG    . HIS A 1 41  ? -9.301  -14.067 -1.788  1.00 65.54  ? 1258 HIS A CG    1 
ATOM   316  N  ND1   . HIS A 1 41  ? -7.970  -13.885 -2.092  1.00 76.70  ? 1258 HIS A ND1   1 
ATOM   317  C  CD2   . HIS A 1 41  ? -9.831  -14.776 -2.810  1.00 73.22  ? 1258 HIS A CD2   1 
ATOM   318  C  CE1   . HIS A 1 41  ? -7.702  -14.473 -3.244  1.00 80.38  ? 1258 HIS A CE1   1 
ATOM   319  N  NE2   . HIS A 1 41  ? -8.814  -15.024 -3.698  1.00 76.87  ? 1258 HIS A NE2   1 
ATOM   320  N  N     . TRP A 1 42  ? -9.430  -16.777 0.098   1.00 66.40  ? 1259 TRP A N     1 
ATOM   321  C  CA    . TRP A 1 42  ? -9.889  -18.112 -0.293  1.00 71.32  ? 1259 TRP A CA    1 
ATOM   322  C  C     . TRP A 1 42  ? -10.610 -18.853 0.841   1.00 62.45  ? 1259 TRP A C     1 
ATOM   323  O  O     . TRP A 1 42  ? -11.545 -19.611 0.569   1.00 62.01  ? 1259 TRP A O     1 
ATOM   324  C  CB    . TRP A 1 42  ? -8.730  -18.945 -0.816  1.00 71.85  ? 1259 TRP A CB    1 
ATOM   325  C  CG    . TRP A 1 42  ? -9.176  -20.227 -1.434  1.00 70.89  ? 1259 TRP A CG    1 
ATOM   326  C  CD1   . TRP A 1 42  ? -9.022  -21.477 -0.920  1.00 75.09  ? 1259 TRP A CD1   1 
ATOM   327  C  CD2   . TRP A 1 42  ? -9.850  -20.387 -2.684  1.00 70.54  ? 1259 TRP A CD2   1 
ATOM   328  N  NE1   . TRP A 1 42  ? -9.560  -22.412 -1.776  1.00 75.64  ? 1259 TRP A NE1   1 
ATOM   329  C  CE2   . TRP A 1 42  ? -10.078 -21.768 -2.865  1.00 65.99  ? 1259 TRP A CE2   1 
ATOM   330  C  CE3   . TRP A 1 42  ? -10.282 -19.500 -3.668  1.00 75.34  ? 1259 TRP A CE3   1 
ATOM   331  C  CZ2   . TRP A 1 42  ? -10.707 -22.283 -3.991  1.00 61.65  ? 1259 TRP A CZ2   1 
ATOM   332  C  CZ3   . TRP A 1 42  ? -10.917 -20.019 -4.792  1.00 77.91  ? 1259 TRP A CZ3   1 
ATOM   333  C  CH2   . TRP A 1 42  ? -11.121 -21.394 -4.941  1.00 70.07  ? 1259 TRP A CH2   1 
ATOM   334  N  N     . SER A 1 43  ? -10.232 -18.626 2.104   1.00 52.31  ? 1260 SER A N     1 
ATOM   335  C  CA    . SER A 1 43  ? -10.995 -19.221 3.197   1.00 57.02  ? 1260 SER A CA    1 
ATOM   336  C  C     . SER A 1 43  ? -12.111 -18.310 3.695   1.00 79.62  ? 1260 SER A C     1 
ATOM   337  O  O     . SER A 1 43  ? -13.183 -18.790 4.138   1.00 84.27  ? 1260 SER A O     1 
ATOM   338  C  CB    . SER A 1 43  ? -10.070 -19.532 4.378   1.00 51.96  ? 1260 SER A CB    1 
ATOM   339  O  OG    . SER A 1 43  ? -9.541  -18.330 4.939   1.00 52.15  ? 1260 SER A OG    1 
ATOM   340  N  N     . PHE A 1 44  ? -11.911 -16.993 3.597   1.00 77.86  ? 1261 PHE A N     1 
ATOM   341  C  CA    . PHE A 1 44  ? -12.968 -16.096 4.012   1.00 65.52  ? 1261 PHE A CA    1 
ATOM   342  C  C     . PHE A 1 44  ? -14.215 -16.295 3.177   1.00 56.76  ? 1261 PHE A C     1 
ATOM   343  O  O     . PHE A 1 44  ? -15.321 -16.075 3.676   1.00 61.26  ? 1261 PHE A O     1 
ATOM   344  C  CB    . PHE A 1 44  ? -12.520 -14.635 3.969   1.00 67.46  ? 1261 PHE A CB    1 
ATOM   345  C  CG    . PHE A 1 44  ? -13.549 -13.727 4.530   1.00 60.42  ? 1261 PHE A CG    1 
ATOM   346  C  CD1   . PHE A 1 44  ? -13.646 -13.527 5.904   1.00 58.04  ? 1261 PHE A CD1   1 
ATOM   347  C  CD2   . PHE A 1 44  ? -14.490 -13.145 3.704   1.00 50.76  ? 1261 PHE A CD2   1 
ATOM   348  C  CE1   . PHE A 1 44  ? -14.646 -12.716 6.437   1.00 46.67  ? 1261 PHE A CE1   1 
ATOM   349  C  CE2   . PHE A 1 44  ? -15.482 -12.356 4.233   1.00 56.03  ? 1261 PHE A CE2   1 
ATOM   350  C  CZ    . PHE A 1 44  ? -15.552 -12.136 5.603   1.00 49.54  ? 1261 PHE A CZ    1 
ATOM   351  N  N     . ALA A 1 45  ? -14.073 -16.719 1.912   1.00 56.83  ? 1262 ALA A N     1 
ATOM   352  C  CA    . ALA A 1 45  ? -15.270 -17.034 1.121   1.00 54.49  ? 1262 ALA A CA    1 
ATOM   353  C  C     . ALA A 1 45  ? -16.016 -18.231 1.703   1.00 57.28  ? 1262 ALA A C     1 
ATOM   354  O  O     . ALA A 1 45  ? -17.257 -18.266 1.660   1.00 55.03  ? 1262 ALA A O     1 
ATOM   355  C  CB    . ALA A 1 45  ? -14.899 -17.291 -0.341  1.00 38.38  ? 1262 ALA A CB    1 
ATOM   356  N  N     . ILE A 1 46  ? -15.280 -19.205 2.269   1.00 48.89  ? 1263 ILE A N     1 
ATOM   357  C  CA    . ILE A 1 46  ? -15.929 -20.335 2.946   1.00 70.00  ? 1263 ILE A CA    1 
ATOM   358  C  C     . ILE A 1 46  ? -16.799 -19.813 4.080   1.00 59.66  ? 1263 ILE A C     1 
ATOM   359  O  O     . ILE A 1 46  ? -18.003 -20.106 4.169   1.00 59.46  ? 1263 ILE A O     1 
ATOM   360  C  CB    . ILE A 1 46  ? -14.878 -21.336 3.500   1.00 69.71  ? 1263 ILE A CB    1 
ATOM   361  C  CG1   . ILE A 1 46  ? -13.815 -21.770 2.471   1.00 65.39  ? 1263 ILE A CG1   1 
ATOM   362  C  CG2   . ILE A 1 46  ? -15.554 -22.541 4.126   1.00 57.37  ? 1263 ILE A CG2   1 
ATOM   363  C  CD1   . ILE A 1 46  ? -14.354 -22.123 1.125   1.00 69.26  ? 1263 ILE A CD1   1 
ATOM   364  N  N     . TRP A 1 47  ? -16.195 -18.998 4.946   1.00 61.12  ? 1264 TRP A N     1 
ATOM   365  C  CA    . TRP A 1 47  ? -16.951 -18.394 6.048   1.00 65.08  ? 1264 TRP A CA    1 
ATOM   366  C  C     . TRP A 1 47  ? -18.099 -17.550 5.531   1.00 65.54  ? 1264 TRP A C     1 
ATOM   367  O  O     . TRP A 1 47  ? -19.148 -17.457 6.167   1.00 66.86  ? 1264 TRP A O     1 
ATOM   368  C  CB    . TRP A 1 47  ? -16.047 -17.537 6.912   1.00 63.20  ? 1264 TRP A CB    1 
ATOM   369  C  CG    . TRP A 1 47  ? -16.754 -16.868 8.044   1.00 62.38  ? 1264 TRP A CG    1 
ATOM   370  C  CD1   . TRP A 1 47  ? -16.895 -15.527 8.227   1.00 61.52  ? 1264 TRP A CD1   1 
ATOM   371  C  CD2   . TRP A 1 47  ? -17.386 -17.496 9.175   1.00 65.67  ? 1264 TRP A CD2   1 
ATOM   372  N  NE1   . TRP A 1 47  ? -17.579 -15.272 9.391   1.00 60.57  ? 1264 TRP A NE1   1 
ATOM   373  C  CE2   . TRP A 1 47  ? -17.885 -16.461 10.001  1.00 65.51  ? 1264 TRP A CE2   1 
ATOM   374  C  CE3   . TRP A 1 47  ? -17.573 -18.826 9.571   1.00 60.09  ? 1264 TRP A CE3   1 
ATOM   375  C  CZ2   . TRP A 1 47  ? -18.564 -16.714 11.204  1.00 56.74  ? 1264 TRP A CZ2   1 
ATOM   376  C  CZ3   . TRP A 1 47  ? -18.246 -19.078 10.761  1.00 56.21  ? 1264 TRP A CZ3   1 
ATOM   377  C  CH2   . TRP A 1 47  ? -18.734 -18.022 11.565  1.00 57.91  ? 1264 TRP A CH2   1 
ATOM   378  N  N     . LYS A 1 48  ? -17.897 -16.883 4.402   1.00 65.60  ? 1265 LYS A N     1 
ATOM   379  C  CA    . LYS A 1 48  ? -18.930 -15.999 3.902   1.00 62.69  ? 1265 LYS A CA    1 
ATOM   380  C  C     . LYS A 1 48  ? -20.150 -16.811 3.474   1.00 55.70  ? 1265 LYS A C     1 
ATOM   381  O  O     . LYS A 1 48  ? -21.293 -16.435 3.761   1.00 53.80  ? 1265 LYS A O     1 
ATOM   382  C  CB    . LYS A 1 48  ? -18.338 -15.165 2.758   1.00 58.27  ? 1265 LYS A CB    1 
ATOM   383  C  CG    . LYS A 1 48  ? -19.194 -14.013 2.283   1.00 58.94  ? 1265 LYS A CG    1 
ATOM   384  C  CD    . LYS A 1 48  ? -18.537 -13.298 1.126   1.00 55.71  ? 1265 LYS A CD    1 
ATOM   385  C  CE    . LYS A 1 48  ? -19.575 -12.809 0.130   1.00 62.32  ? 1265 LYS A CE    1 
ATOM   386  N  NZ    . LYS A 1 48  ? -19.040 -12.725 -1.263  1.00 71.22  ? 1265 LYS A NZ    1 
ATOM   387  N  N     . ALA A 1 49  ? -19.923 -17.972 2.856   1.00 49.89  ? 1266 ALA A N     1 
ATOM   388  C  CA    . ALA A 1 49  ? -21.050 -18.827 2.475   1.00 55.41  ? 1266 ALA A CA    1 
ATOM   389  C  C     . ALA A 1 49  ? -21.771 -19.359 3.709   1.00 59.12  ? 1266 ALA A C     1 
ATOM   390  O  O     . ALA A 1 49  ? -23.011 -19.338 3.783   1.00 56.66  ? 1266 ALA A O     1 
ATOM   391  C  CB    . ALA A 1 49  ? -20.584 -19.993 1.602   1.00 41.65  ? 1266 ALA A CB    1 
ATOM   392  N  N     . ILE A 1 50  ? -21.004 -19.835 4.693   1.00 52.92  ? 1267 ILE A N     1 
ATOM   393  C  CA    . ILE A 1 50  ? -21.623 -20.335 5.919   1.00 59.07  ? 1267 ILE A CA    1 
ATOM   394  C  C     . ILE A 1 50  ? -22.447 -19.239 6.573   1.00 59.45  ? 1267 ILE A C     1 
ATOM   395  O  O     . ILE A 1 50  ? -23.631 -19.430 6.896   1.00 66.72  ? 1267 ILE A O     1 
ATOM   396  C  CB    . ILE A 1 50  ? -20.551 -20.890 6.882   1.00 67.34  ? 1267 ILE A CB    1 
ATOM   397  C  CG1   . ILE A 1 50  ? -19.841 -22.123 6.288   1.00 65.10  ? 1267 ILE A CG1   1 
ATOM   398  C  CG2   . ILE A 1 50  ? -21.162 -21.240 8.223   1.00 63.68  ? 1267 ILE A CG2   1 
ATOM   399  C  CD1   . ILE A 1 50  ? -18.513 -22.504 6.997   1.00 64.97  ? 1267 ILE A CD1   1 
ATOM   400  N  N     . ARG A 1 51  ? -21.829 -18.066 6.756   1.00 63.68  ? 1268 ARG A N     1 
ATOM   401  C  CA    . ARG A 1 51  ? -22.484 -16.938 7.402   1.00 58.62  ? 1268 ARG A CA    1 
ATOM   402  C  C     . ARG A 1 51  ? -23.748 -16.553 6.657   1.00 60.49  ? 1268 ARG A C     1 
ATOM   403  O  O     . ARG A 1 51  ? -24.818 -16.415 7.266   1.00 56.08  ? 1268 ARG A O     1 
ATOM   404  C  CB    . ARG A 1 51  ? -21.515 -15.766 7.522   1.00 66.53  ? 1268 ARG A CB    1 
ATOM   405  C  CG    . ARG A 1 51  ? -22.175 -14.435 7.877   1.00 73.75  ? 1268 ARG A CG    1 
ATOM   406  C  CD    . ARG A 1 51  ? -21.287 -13.269 7.515   1.00 70.57  ? 1268 ARG A CD    1 
ATOM   407  N  NE    . ARG A 1 51  ? -21.457 -12.887 6.114   1.00 73.35  ? 1268 ARG A NE    1 
ATOM   408  C  CZ    . ARG A 1 51  ? -20.644 -12.062 5.462   1.00 73.17  ? 1268 ARG A CZ    1 
ATOM   409  N  NH1   . ARG A 1 51  ? -19.602 -11.526 6.084   1.00 72.21  ? 1268 ARG A NH1   1 
ATOM   410  N  NH2   . ARG A 1 51  ? -20.864 -11.778 4.184   1.00 77.54  ? 1268 ARG A NH2   1 
ATOM   411  N  N     . ASN A 1 52  ? -23.650 -16.395 5.330   1.00 58.72  ? 1269 ASN A N     1 
ATOM   412  C  CA    . ASN A 1 52  ? -24.802 -15.961 4.550   1.00 54.27  ? 1269 ASN A CA    1 
ATOM   413  C  C     . ASN A 1 52  ? -25.947 -16.969 4.642   1.00 64.20  ? 1269 ASN A C     1 
ATOM   414  O  O     . ASN A 1 52  ? -27.117 -16.585 4.816   1.00 70.64  ? 1269 ASN A O     1 
ATOM   415  C  CB    . ASN A 1 52  ? -24.385 -15.749 3.091   1.00 52.16  ? 1269 ASN A CB    1 
ATOM   416  C  CG    . ASN A 1 52  ? -23.597 -14.457 2.871   1.00 60.67  ? 1269 ASN A CG    1 
ATOM   417  O  OD1   . ASN A 1 52  ? -23.304 -13.715 3.813   1.00 63.77  ? 1269 ASN A OD1   1 
ATOM   418  N  ND2   . ASN A 1 52  ? -23.254 -14.185 1.613   1.00 66.92  ? 1269 ASN A ND2   1 
ATOM   419  N  N     . TRP A 1 53  ? -25.632 -18.265 4.537   1.00 66.95  ? 1270 TRP A N     1 
ATOM   420  C  CA    . TRP A 1 53  ? -26.675 -19.286 4.599   1.00 62.20  ? 1270 TRP A CA    1 
ATOM   421  C  C     . TRP A 1 53  ? -27.388 -19.245 5.946   1.00 62.09  ? 1270 TRP A C     1 
ATOM   422  O  O     . TRP A 1 53  ? -28.629 -19.146 6.027   1.00 58.57  ? 1270 TRP A O     1 
ATOM   423  C  CB    . TRP A 1 53  ? -26.058 -20.661 4.334   1.00 53.81  ? 1270 TRP A CB    1 
ATOM   424  C  CG    . TRP A 1 53  ? -27.067 -21.750 4.300   1.00 50.89  ? 1270 TRP A CG    1 
ATOM   425  C  CD1   . TRP A 1 53  ? -27.696 -22.250 3.196   1.00 43.58  ? 1270 TRP A CD1   1 
ATOM   426  C  CD2   . TRP A 1 53  ? -27.590 -22.470 5.428   1.00 50.46  ? 1270 TRP A CD2   1 
ATOM   427  N  NE1   . TRP A 1 53  ? -28.599 -23.221 3.572   1.00 57.26  ? 1270 TRP A NE1   1 
ATOM   428  C  CE2   . TRP A 1 53  ? -28.545 -23.381 4.934   1.00 54.85  ? 1270 TRP A CE2   1 
ATOM   429  C  CE3   . TRP A 1 53  ? -27.351 -22.421 6.806   1.00 53.43  ? 1270 TRP A CE3   1 
ATOM   430  C  CZ2   . TRP A 1 53  ? -29.250 -24.251 5.766   1.00 54.01  ? 1270 TRP A CZ2   1 
ATOM   431  C  CZ3   . TRP A 1 53  ? -28.039 -23.281 7.632   1.00 64.90  ? 1270 TRP A CZ3   1 
ATOM   432  C  CH2   . TRP A 1 53  ? -28.987 -24.187 7.110   1.00 63.04  ? 1270 TRP A CH2   1 
ATOM   433  N  N     . PHE A 1 54  ? -26.606 -19.256 7.021   1.00 60.14  ? 1271 PHE A N     1 
ATOM   434  C  CA    . PHE A 1 54  ? -27.208 -19.314 8.344   1.00 61.32  ? 1271 PHE A CA    1 
ATOM   435  C  C     . PHE A 1 54  ? -27.981 -18.026 8.654   1.00 61.79  ? 1271 PHE A C     1 
ATOM   436  O  O     . PHE A 1 54  ? -29.039 -18.059 9.301   1.00 52.76  ? 1271 PHE A O     1 
ATOM   437  C  CB    . PHE A 1 54  ? -26.113 -19.591 9.369   1.00 49.44  ? 1271 PHE A CB    1 
ATOM   438  C  CG    . PHE A 1 54  ? -26.616 -19.683 10.765  1.00 54.17  ? 1271 PHE A CG    1 
ATOM   439  C  CD1   . PHE A 1 54  ? -27.265 -20.812 11.193  1.00 53.75  ? 1271 PHE A CD1   1 
ATOM   440  C  CD2   . PHE A 1 54  ? -26.499 -18.600 11.631  1.00 54.54  ? 1271 PHE A CD2   1 
ATOM   441  C  CE1   . PHE A 1 54  ? -27.729 -20.903 12.494  1.00 57.56  ? 1271 PHE A CE1   1 
ATOM   442  C  CE2   . PHE A 1 54  ? -26.959 -18.653 12.939  1.00 52.43  ? 1271 PHE A CE2   1 
ATOM   443  C  CZ    . PHE A 1 54  ? -27.571 -19.809 13.378  1.00 57.80  ? 1271 PHE A CZ    1 
ATOM   444  N  N     . ASP A 1 55  ? -27.464 -16.878 8.220   1.00 66.13  ? 1272 ASP A N     1 
ATOM   445  C  CA    . ASP A 1 55  ? -28.181 -15.637 8.467   1.00 70.56  ? 1272 ASP A CA    1 
ATOM   446  C  C     . ASP A 1 55  ? -29.514 -15.622 7.743   1.00 70.73  ? 1272 ASP A C     1 
ATOM   447  O  O     . ASP A 1 55  ? -30.529 -15.189 8.306   1.00 84.44  ? 1272 ASP A O     1 
ATOM   448  C  CB    . ASP A 1 55  ? -27.357 -14.430 8.035   1.00 66.68  ? 1272 ASP A CB    1 
ATOM   449  C  CG    . ASP A 1 55  ? -28.016 -13.132 8.434   1.00 58.01  ? 1272 ASP A CG    1 
ATOM   450  O  OD1   . ASP A 1 55  ? -27.665 -12.612 9.528   1.00 47.87  ? 1272 ASP A OD1   1 
ATOM   451  O  OD2   . ASP A 1 55  ? -28.911 -12.664 7.670   1.00 60.74  ? 1272 ASP A OD2   1 
ATOM   452  N  N     . ALA A 1 56  ? -29.531 -16.059 6.484   1.00 62.97  ? 1273 ALA A N     1 
ATOM   453  C  CA    . ALA A 1 56  ? -30.796 -16.100 5.767   1.00 65.19  ? 1273 ALA A CA    1 
ATOM   454  C  C     . ALA A 1 56  ? -31.799 -16.959 6.525   1.00 75.03  ? 1273 ALA A C     1 
ATOM   455  O  O     . ALA A 1 56  ? -32.964 -16.570 6.699   1.00 77.20  ? 1273 ALA A O     1 
ATOM   456  C  CB    . ALA A 1 56  ? -30.576 -16.615 4.349   1.00 67.52  ? 1273 ALA A CB    1 
ATOM   457  N  N     . GLU A 1 57  ? -31.339 -18.111 7.026   1.00 67.39  ? 1274 GLU A N     1 
ATOM   458  C  CA    . GLU A 1 57  ? -32.200 -18.980 7.820   1.00 56.14  ? 1274 GLU A CA    1 
ATOM   459  C  C     . GLU A 1 57  ? -32.757 -18.267 9.059   1.00 51.38  ? 1274 GLU A C     1 
ATOM   460  O  O     . GLU A 1 57  ? -33.971 -18.308 9.322   1.00 59.70  ? 1274 GLU A O     1 
ATOM   461  C  CB    . GLU A 1 57  ? -31.433 -20.252 8.228   1.00 65.89  ? 1274 GLU A CB    1 
ATOM   462  C  CG    . GLU A 1 57  ? -31.168 -21.267 7.092   1.00 70.28  ? 1274 GLU A CG    1 
ATOM   463  C  CD    . GLU A 1 57  ? -32.403 -21.611 6.252   1.00 80.20  ? 1274 GLU A CD    1 
ATOM   464  O  OE1   . GLU A 1 57  ? -33.554 -21.570 6.774   1.00 85.78  ? 1274 GLU A OE1   1 
ATOM   465  O  OE2   . GLU A 1 57  ? -32.213 -21.932 5.057   1.00 80.68  ? 1274 GLU A OE2   1 
ATOM   466  N  N     . ILE A 1 58  ? -31.889 -17.666 9.882   1.00 56.90  ? 1275 ILE A N     1 
ATOM   467  C  CA    . ILE A 1 58  ? -32.415 -17.116 11.137  1.00 63.47  ? 1275 ILE A CA    1 
ATOM   468  C  C     . ILE A 1 58  ? -33.227 -15.833 10.925  1.00 73.68  ? 1275 ILE A C     1 
ATOM   469  O  O     . ILE A 1 58  ? -34.052 -15.465 11.779  1.00 62.72  ? 1275 ILE A O     1 
ATOM   470  C  CB    . ILE A 1 58  ? -31.317 -16.876 12.179  1.00 58.59  ? 1275 ILE A CB    1 
ATOM   471  C  CG1   . ILE A 1 58  ? -30.328 -15.801 11.736  1.00 57.35  ? 1275 ILE A CG1   1 
ATOM   472  C  CG2   . ILE A 1 58  ? -30.605 -18.169 12.517  1.00 52.52  ? 1275 ILE A CG2   1 
ATOM   473  C  CD1   . ILE A 1 58  ? -29.290 -15.509 12.816  1.00 41.25  ? 1275 ILE A CD1   1 
ATOM   474  N  N     . THR A 1 59  ? -33.022 -15.117 9.825   1.00 84.00  ? 1276 THR A N     1 
ATOM   475  C  CA    . THR A 1 59  ? -33.931 -14.000 9.607   1.00 95.81  ? 1276 THR A CA    1 
ATOM   476  C  C     . THR A 1 59  ? -35.265 -14.509 9.067   1.00 82.75  ? 1276 THR A C     1 
ATOM   477  O  O     . THR A 1 59  ? -36.319 -14.010 9.475   1.00 74.18  ? 1276 THR A O     1 
ATOM   478  C  CB    . THR A 1 59  ? -33.292 -12.920 8.718   1.00 90.76  ? 1276 THR A CB    1 
ATOM   479  O  OG1   . THR A 1 59  ? -33.013 -13.450 7.419   1.00 107.26 ? 1276 THR A OG1   1 
ATOM   480  C  CG2   . THR A 1 59  ? -31.980 -12.424 9.353   1.00 78.71  ? 1276 THR A CG2   1 
ATOM   481  N  N     . ARG A 1 60  ? -35.254 -15.541 8.215   1.00 60.95  ? 1277 ARG A N     1 
ATOM   482  C  CA    . ARG A 1 60  ? -36.525 -16.158 7.859   1.00 68.54  ? 1277 ARG A CA    1 
ATOM   483  C  C     . ARG A 1 60  ? -37.233 -16.628 9.117   1.00 65.37  ? 1277 ARG A C     1 
ATOM   484  O  O     . ARG A 1 60  ? -38.458 -16.758 9.136   1.00 58.57  ? 1277 ARG A O     1 
ATOM   485  C  CB    . ARG A 1 60  ? -36.323 -17.312 6.860   1.00 69.49  ? 1277 ARG A CB    1 
ATOM   486  C  CG    . ARG A 1 60  ? -37.577 -18.193 6.624   1.00 83.22  ? 1277 ARG A CG    1 
ATOM   487  C  CD    . ARG A 1 60  ? -37.558 -19.078 5.354   1.00 94.72  ? 1277 ARG A CD    1 
ATOM   488  N  NE    . ARG A 1 60  ? -36.647 -20.222 5.414   1.00 113.75 ? 1277 ARG A NE    1 
ATOM   489  C  CZ    . ARG A 1 60  ? -36.476 -21.098 4.419   1.00 125.18 ? 1277 ARG A CZ    1 
ATOM   490  N  NH1   . ARG A 1 60  ? -37.160 -20.970 3.283   1.00 129.60 ? 1277 ARG A NH1   1 
ATOM   491  N  NH2   . ARG A 1 60  ? -35.627 -22.114 4.554   1.00 122.18 ? 1277 ARG A NH2   1 
ATOM   492  N  N     . LEU A 1 61  ? -36.473 -16.917 10.169  1.00 65.63  ? 1278 LEU A N     1 
ATOM   493  C  CA    . LEU A 1 61  ? -37.098 -17.310 11.418  1.00 63.75  ? 1278 LEU A CA    1 
ATOM   494  C  C     . LEU A 1 61  ? -37.661 -16.139 12.203  1.00 69.74  ? 1278 LEU A C     1 
ATOM   495  O  O     . LEU A 1 61  ? -38.551 -16.343 13.044  1.00 61.07  ? 1278 LEU A O     1 
ATOM   496  C  CB    . LEU A 1 61  ? -36.091 -18.087 12.264  1.00 73.84  ? 1278 LEU A CB    1 
ATOM   497  C  CG    . LEU A 1 61  ? -36.217 -19.542 11.791  1.00 75.11  ? 1278 LEU A CG    1 
ATOM   498  C  CD1   . LEU A 1 61  ? -35.161 -20.447 12.343  1.00 51.67  ? 1278 LEU A CD1   1 
ATOM   499  C  CD2   . LEU A 1 61  ? -37.625 -20.048 12.132  1.00 81.24  ? 1278 LEU A CD2   1 
ATOM   500  N  N     . GLY A 1 62  ? -37.180 -14.918 11.959  1.00 68.33  ? 1279 GLY A N     1 
ATOM   501  C  CA    . GLY A 1 62  ? -37.625 -13.786 12.735  1.00 54.87  ? 1279 GLY A CA    1 
ATOM   502  C  C     . GLY A 1 62  ? -36.614 -13.260 13.727  1.00 61.02  ? 1279 GLY A C     1 
ATOM   503  O  O     . GLY A 1 62  ? -36.993 -12.483 14.608  1.00 67.42  ? 1279 GLY A O     1 
ATOM   504  N  N     . VAL A 1 63  ? -35.372 -13.735 13.675  1.00 59.89  ? 1280 VAL A N     1 
ATOM   505  C  CA    . VAL A 1 63  ? -34.289 -13.112 14.420  1.00 58.02  ? 1280 VAL A CA    1 
ATOM   506  C  C     . VAL A 1 63  ? -33.852 -11.854 13.671  1.00 56.94  ? 1280 VAL A C     1 
ATOM   507  O  O     . VAL A 1 63  ? -34.086 -11.713 12.465  1.00 59.19  ? 1280 VAL A O     1 
ATOM   508  C  CB    . VAL A 1 63  ? -33.120 -14.109 14.594  1.00 60.30  ? 1280 VAL A CB    1 
ATOM   509  C  CG1   . VAL A 1 63  ? -32.096 -13.631 15.620  1.00 60.25  ? 1280 VAL A CG1   1 
ATOM   510  C  CG2   . VAL A 1 63  ? -33.642 -15.441 15.016  1.00 57.03  ? 1280 VAL A CG2   1 
ATOM   511  N  N     . LYS A 1 64  ? -33.262 -10.905 14.399  1.00 53.06  ? 1281 LYS A N     1 
ATOM   512  C  CA    . LYS A 1 64  ? -32.821 -9.643  13.812  1.00 59.99  ? 1281 LYS A CA    1 
ATOM   513  C  C     . LYS A 1 64  ? -31.344 -9.354  14.121  1.00 62.07  ? 1281 LYS A C     1 
ATOM   514  O  O     . LYS A 1 64  ? -30.836 -9.686  15.203  1.00 60.25  ? 1281 LYS A O     1 
ATOM   515  C  CB    . LYS A 1 64  ? -33.710 -8.470  14.298  1.00 62.02  ? 1281 LYS A CB    1 
ATOM   516  C  CG    . LYS A 1 64  ? -34.985 -8.264  13.460  1.00 62.79  ? 1281 LYS A CG    1 
ATOM   517  C  CD    . LYS A 1 64  ? -36.086 -7.670  14.303  1.00 68.99  ? 1281 LYS A CD    1 
ATOM   518  C  CE    . LYS A 1 64  ? -37.448 -7.824  13.654  1.00 80.31  ? 1281 LYS A CE    1 
ATOM   519  N  NZ    . LYS A 1 64  ? -37.639 -6.938  12.487  1.00 87.90  ? 1281 LYS A NZ    1 
ATOM   520  N  N     . GLU A 1 65  ? -30.666 -8.695  13.162  1.00 47.45  ? 1282 GLU A N     1 
ATOM   521  C  CA    . GLU A 1 65  ? -29.228 -8.406  13.243  1.00 47.31  ? 1282 GLU A CA    1 
ATOM   522  C  C     . GLU A 1 65  ? -28.954 -7.066  13.931  1.00 56.10  ? 1282 GLU A C     1 
ATOM   523  O  O     . GLU A 1 65  ? -29.575 -6.049  13.595  1.00 58.70  ? 1282 GLU A O     1 
ATOM   524  C  CB    . GLU A 1 65  ? -28.574 -8.396  11.849  1.00 40.55  ? 1282 GLU A CB    1 
ATOM   525  C  CG    . GLU A 1 65  ? -27.007 -8.587  11.904  1.00 52.97  ? 1282 GLU A CG    1 
ATOM   526  C  CD    . GLU A 1 65  ? -26.365 -8.867  10.538  1.00 57.99  ? 1282 GLU A CD    1 
ATOM   527  O  OE1   . GLU A 1 65  ? -27.102 -9.043  9.541   1.00 61.26  ? 1282 GLU A OE1   1 
ATOM   528  O  OE2   . GLU A 1 65  ? -25.112 -8.909  10.468  1.00 65.22  ? 1282 GLU A OE2   1 
ATOM   529  N  N     . CYS A 1 66  ? -28.005 -7.064  14.873  1.00 51.57  ? 1283 CYS A N     1 
ATOM   530  C  CA    . CYS A 1 66  ? -27.611 -5.861  15.596  1.00 66.70  ? 1283 CYS A CA    1 
ATOM   531  C  C     . CYS A 1 66  ? -26.089 -5.877  15.805  1.00 67.28  ? 1283 CYS A C     1 
ATOM   532  O  O     . CYS A 1 66  ? -25.386 -6.757  15.292  1.00 58.11  ? 1283 CYS A O     1 
ATOM   533  C  CB    . CYS A 1 66  ? -28.394 -5.752  16.908  1.00 63.56  ? 1283 CYS A CB    1 
ATOM   534  S  SG    . CYS A 1 66  ? -27.799 -6.873  18.176  1.00 74.64  ? 1283 CYS A SG    1 
ATOM   535  N  N     . TYR A 1 67  ? -25.572 -4.872  16.527  1.00 54.07  ? 1284 TYR A N     1 
ATOM   536  C  CA    . TYR A 1 67  ? -24.143 -4.815  16.837  1.00 58.02  ? 1284 TYR A CA    1 
ATOM   537  C  C     . TYR A 1 67  ? -23.873 -4.048  18.126  1.00 61.37  ? 1284 TYR A C     1 
ATOM   538  O  O     . TYR A 1 67  ? -24.128 -2.844  18.198  1.00 75.18  ? 1284 TYR A O     1 
ATOM   539  C  CB    . TYR A 1 67  ? -23.342 -4.190  15.693  1.00 51.95  ? 1284 TYR A CB    1 
ATOM   540  C  CG    . TYR A 1 67  ? -21.858 -4.310  15.967  1.00 73.14  ? 1284 TYR A CG    1 
ATOM   541  C  CD1   . TYR A 1 67  ? -21.185 -5.525  15.792  1.00 73.78  ? 1284 TYR A CD1   1 
ATOM   542  C  CD2   . TYR A 1 67  ? -21.136 -3.236  16.463  1.00 72.52  ? 1284 TYR A CD2   1 
ATOM   543  C  CE1   . TYR A 1 67  ? -19.831 -5.639  16.060  1.00 69.88  ? 1284 TYR A CE1   1 
ATOM   544  C  CE2   . TYR A 1 67  ? -19.781 -3.346  16.733  1.00 64.16  ? 1284 TYR A CE2   1 
ATOM   545  C  CZ    . TYR A 1 67  ? -19.134 -4.540  16.529  1.00 75.35  ? 1284 TYR A CZ    1 
ATOM   546  O  OH    . TYR A 1 67  ? -17.785 -4.627  16.812  1.00 91.69  ? 1284 TYR A OH    1 
ATOM   547  N  N     . PHE A 1 68  ? -23.332 -4.736  19.128  1.00 54.61  ? 1285 PHE A N     1 
ATOM   548  C  CA    . PHE A 1 68  ? -22.876 -4.158  20.381  1.00 64.79  ? 1285 PHE A CA    1 
ATOM   549  C  C     . PHE A 1 68  ? -21.388 -3.865  20.316  1.00 71.33  ? 1285 PHE A C     1 
ATOM   550  O  O     . PHE A 1 68  ? -20.676 -4.419  19.478  1.00 71.42  ? 1285 PHE A O     1 
ATOM   551  C  CB    . PHE A 1 68  ? -23.159 -5.117  21.536  1.00 70.79  ? 1285 PHE A CB    1 
ATOM   552  C  CG    . PHE A 1 68  ? -24.586 -5.133  21.957  1.00 66.50  ? 1285 PHE A CG    1 
ATOM   553  C  CD1   . PHE A 1 68  ? -25.563 -5.585  21.085  1.00 55.46  ? 1285 PHE A CD1   1 
ATOM   554  C  CD2   . PHE A 1 68  ? -24.958 -4.686  23.226  1.00 67.40  ? 1285 PHE A CD2   1 
ATOM   555  C  CE1   . PHE A 1 68  ? -26.885 -5.604  21.465  1.00 60.49  ? 1285 PHE A CE1   1 
ATOM   556  C  CE2   . PHE A 1 68  ? -26.279 -4.703  23.620  1.00 58.63  ? 1285 PHE A CE2   1 
ATOM   557  C  CZ    . PHE A 1 68  ? -27.252 -5.150  22.741  1.00 55.34  ? 1285 PHE A CZ    1 
ATOM   558  N  N     . PRO A 1 69  ? -20.873 -2.990  21.178  1.00 78.59  ? 1286 PRO A N     1 
ATOM   559  C  CA    . PRO A 1 69  ? -19.480 -2.553  21.025  1.00 78.98  ? 1286 PRO A CA    1 
ATOM   560  C  C     . PRO A 1 69  ? -18.506 -3.677  21.338  1.00 77.91  ? 1286 PRO A C     1 
ATOM   561  O  O     . PRO A 1 69  ? -18.841 -4.645  22.023  1.00 71.65  ? 1286 PRO A O     1 
ATOM   562  C  CB    . PRO A 1 69  ? -19.354 -1.397  22.025  1.00 77.80  ? 1286 PRO A CB    1 
ATOM   563  C  CG    . PRO A 1 69  ? -20.765 -0.933  22.257  1.00 70.66  ? 1286 PRO A CG    1 
ATOM   564  C  CD    . PRO A 1 69  ? -21.578 -2.203  22.205  1.00 73.92  ? 1286 PRO A CD    1 
ATOM   565  N  N     . ILE A 1 70  ? -17.275 -3.527  20.825  1.00 79.38  ? 1287 ILE A N     1 
ATOM   566  C  CA    . ILE A 1 70  ? -16.206 -4.495  21.084  1.00 76.72  ? 1287 ILE A CA    1 
ATOM   567  C  C     . ILE A 1 70  ? -15.659 -4.397  22.501  1.00 76.46  ? 1287 ILE A C     1 
ATOM   568  O  O     . ILE A 1 70  ? -15.021 -5.344  22.977  1.00 85.76  ? 1287 ILE A O     1 
ATOM   569  C  CB    . ILE A 1 70  ? -15.050 -4.335  20.073  1.00 75.32  ? 1287 ILE A CB    1 
ATOM   570  C  CG1   . ILE A 1 70  ? -14.095 -5.536  20.127  1.00 71.87  ? 1287 ILE A CG1   1 
ATOM   571  C  CG2   . ILE A 1 70  ? -14.237 -3.095  20.381  1.00 73.80  ? 1287 ILE A CG2   1 
ATOM   572  C  CD1   . ILE A 1 70  ? -14.603 -6.766  19.414  1.00 74.34  ? 1287 ILE A CD1   1 
ATOM   573  N  N     . PHE A 1 71  ? -15.909 -3.299  23.201  1.00 71.80  ? 1288 PHE A N     1 
ATOM   574  C  CA    . PHE A 1 71  ? -15.366 -3.075  24.537  1.00 75.56  ? 1288 PHE A CA    1 
ATOM   575  C  C     . PHE A 1 71  ? -16.477 -3.298  25.539  1.00 68.70  ? 1288 PHE A C     1 
ATOM   576  O  O     . PHE A 1 71  ? -17.635 -2.986  25.258  1.00 70.04  ? 1288 PHE A O     1 
ATOM   577  C  CB    . PHE A 1 71  ? -14.803 -1.659  24.704  1.00 82.34  ? 1288 PHE A CB    1 
ATOM   578  C  CG    . PHE A 1 71  ? -13.588 -1.395  23.883  1.00 84.03  ? 1288 PHE A CG    1 
ATOM   579  C  CD1   . PHE A 1 71  ? -12.413 -2.086  24.124  1.00 88.53  ? 1288 PHE A CD1   1 
ATOM   580  C  CD2   . PHE A 1 71  ? -13.630 -0.485  22.837  1.00 81.11  ? 1288 PHE A CD2   1 
ATOM   581  C  CE1   . PHE A 1 71  ? -11.288 -1.852  23.352  1.00 88.71  ? 1288 PHE A CE1   1 
ATOM   582  C  CE2   . PHE A 1 71  ? -12.510 -0.253  22.056  1.00 81.67  ? 1288 PHE A CE2   1 
ATOM   583  C  CZ    . PHE A 1 71  ? -11.340 -0.932  22.312  1.00 80.86  ? 1288 PHE A CZ    1 
ATOM   584  N  N     . VAL A 1 72  ? -16.115 -3.843  26.700  1.00 69.07  ? 1289 VAL A N     1 
ATOM   585  C  CA    . VAL A 1 72  ? -17.043 -4.123  27.793  1.00 76.67  ? 1289 VAL A CA    1 
ATOM   586  C  C     . VAL A 1 72  ? -16.476 -3.550  29.088  1.00 79.59  ? 1289 VAL A C     1 
ATOM   587  O  O     . VAL A 1 72  ? -15.260 -3.593  29.310  1.00 67.55  ? 1289 VAL A O     1 
ATOM   588  C  CB    . VAL A 1 72  ? -17.325 -5.632  27.913  1.00 70.99  ? 1289 VAL A CB    1 
ATOM   589  C  CG1   . VAL A 1 72  ? -18.231 -5.930  29.117  1.00 67.71  ? 1289 VAL A CG1   1 
ATOM   590  C  CG2   . VAL A 1 72  ? -17.969 -6.135  26.657  1.00 67.00  ? 1289 VAL A CG2   1 
ATOM   591  N  N     . SER A 1 73  ? -17.344 -2.937  29.897  1.00 86.84  ? 1290 SER A N     1 
ATOM   592  C  CA    . SER A 1 73  ? -16.911 -2.386  31.172  1.00 81.06  ? 1290 SER A CA    1 
ATOM   593  C  C     . SER A 1 73  ? -16.438 -3.474  32.132  1.00 86.90  ? 1290 SER A C     1 
ATOM   594  O  O     . SER A 1 73  ? -16.864 -4.629  32.053  1.00 96.31  ? 1290 SER A O     1 
ATOM   595  C  CB    . SER A 1 73  ? -18.063 -1.616  31.809  1.00 81.07  ? 1290 SER A CB    1 
ATOM   596  O  OG    . SER A 1 73  ? -17.991 -1.746  33.207  1.00 91.77  ? 1290 SER A OG    1 
ATOM   597  N  N     . ARG A 1 74  ? -15.505 -3.103  33.015  1.00 87.37  ? 1291 ARG A N     1 
ATOM   598  C  CA    . ARG A 1 74  ? -15.157 -3.954  34.144  1.00 87.11  ? 1291 ARG A CA    1 
ATOM   599  C  C     . ARG A 1 74  ? -16.409 -4.334  34.925  1.00 95.77  ? 1291 ARG A C     1 
ATOM   600  O  O     . ARG A 1 74  ? -16.554 -5.478  35.381  1.00 104.66 ? 1291 ARG A O     1 
ATOM   601  C  CB    . ARG A 1 74  ? -14.152 -3.241  35.057  1.00 83.67  ? 1291 ARG A CB    1 
ATOM   602  N  N     . ALA A 1 75  ? -17.324 -3.376  35.094  1.00 92.21  ? 1292 ALA A N     1 
ATOM   603  C  CA    . ALA A 1 75  ? -18.542 -3.608  35.867  1.00 86.78  ? 1292 ALA A CA    1 
ATOM   604  C  C     . ALA A 1 75  ? -19.523 -4.495  35.107  1.00 90.30  ? 1292 ALA A C     1 
ATOM   605  O  O     . ALA A 1 75  ? -20.140 -5.394  35.689  1.00 91.09  ? 1292 ALA A O     1 
ATOM   606  C  CB    . ALA A 1 75  ? -19.193 -2.271  36.241  1.00 72.63  ? 1292 ALA A CB    1 
ATOM   607  N  N     . ALA A 1 76  ? -19.741 -4.214  33.821  1.00 89.26  ? 1293 ALA A N     1 
ATOM   608  C  CA    . ALA A 1 76  ? -20.583 -5.104  33.030  1.00 84.17  ? 1293 ALA A CA    1 
ATOM   609  C  C     . ALA A 1 76  ? -20.071 -6.533  33.143  1.00 87.04  ? 1293 ALA A C     1 
ATOM   610  O  O     . ALA A 1 76  ? -20.849 -7.469  33.347  1.00 87.64  ? 1293 ALA A O     1 
ATOM   611  C  CB    . ALA A 1 76  ? -20.624 -4.637  31.572  1.00 79.32  ? 1293 ALA A CB    1 
ATOM   612  N  N     . LEU A 1 77  ? -18.748 -6.692  33.120  1.00 88.31  ? 1294 LEU A N     1 
ATOM   613  C  CA    . LEU A 1 77  ? -18.117 -8.006  33.145  1.00 85.18  ? 1294 LEU A CA    1 
ATOM   614  C  C     . LEU A 1 77  ? -18.281 -8.663  34.513  1.00 96.21  ? 1294 LEU A C     1 
ATOM   615  O  O     . LEU A 1 77  ? -18.829 -9.766  34.632  1.00 100.84 ? 1294 LEU A O     1 
ATOM   616  C  CB    . LEU A 1 77  ? -16.640 -7.846  32.778  1.00 76.28  ? 1294 LEU A CB    1 
ATOM   617  C  CG    . LEU A 1 77  ? -15.794 -8.998  32.249  1.00 77.97  ? 1294 LEU A CG    1 
ATOM   618  C  CD1   . LEU A 1 77  ? -15.651 -10.078 33.320  1.00 92.10  ? 1294 LEU A CD1   1 
ATOM   619  C  CD2   . LEU A 1 77  ? -16.352 -9.554  30.923  1.00 60.17  ? 1294 LEU A CD2   1 
ATOM   620  N  N     . GLU A 1 78  ? -17.780 -8.010  35.558  1.00 99.24  ? 1295 GLU A N     1 
ATOM   621  C  CA    . GLU A 1 78  ? -17.713 -8.607  36.884  1.00 106.69 ? 1295 GLU A CA    1 
ATOM   622  C  C     . GLU A 1 78  ? -18.995 -8.470  37.707  1.00 116.27 ? 1295 GLU A C     1 
ATOM   623  O  O     . GLU A 1 78  ? -19.196 -9.265  38.632  1.00 123.83 ? 1295 GLU A O     1 
ATOM   624  C  CB    . GLU A 1 78  ? -16.523 -8.017  37.642  1.00 108.00 ? 1295 GLU A CB    1 
ATOM   625  C  CG    . GLU A 1 78  ? -15.220 -8.213  36.873  1.00 108.37 ? 1295 GLU A CG    1 
ATOM   626  C  CD    . GLU A 1 78  ? -14.004 -8.401  37.767  1.00 113.17 ? 1295 GLU A CD    1 
ATOM   627  O  OE1   . GLU A 1 78  ? -14.146 -8.943  38.888  1.00 111.27 ? 1295 GLU A OE1   1 
ATOM   628  O  OE2   . GLU A 1 78  ? -12.897 -8.013  37.330  1.00 116.57 ? 1295 GLU A OE2   1 
ATOM   629  N  N     . ARG A 1 79  ? -19.855 -7.557  37.368  1.00 125.01 ? 1296 ARG A N     1 
ATOM   630  C  CA    . ARG A 1 79  ? -21.057 -7.421  38.105  1.00 131.16 ? 1296 ARG A CA    1 
ATOM   631  C  C     . ARG A 1 79  ? -21.857 -8.643  37.868  1.00 136.30 ? 1296 ARG A C     1 
ATOM   632  O  O     . ARG A 1 79  ? -22.019 -8.987  36.738  1.00 140.15 ? 1296 ARG A O     1 
ATOM   633  C  CB    . ARG A 1 79  ? -21.828 -6.269  37.511  1.00 130.15 ? 1296 ARG A CB    1 
ATOM   634  N  N     . GLU A 1 80  ? -22.372 -9.269  38.919  1.00 136.66 ? 1297 GLU A N     1 
ATOM   635  C  CA    . GLU A 1 80  ? -23.214 -10.453 38.824  1.00 135.60 ? 1297 GLU A CA    1 
ATOM   636  C  C     . GLU A 1 80  ? -22.550 -11.459 37.976  1.00 127.25 ? 1297 GLU A C     1 
ATOM   637  O  O     . GLU A 1 80  ? -23.068 -11.825 36.981  1.00 125.88 ? 1297 GLU A O     1 
ATOM   638  C  CB    . GLU A 1 80  ? -24.604 -10.123 38.277  1.00 142.64 ? 1297 GLU A CB    1 
ATOM   639  C  CG    . GLU A 1 80  ? -25.152 -8.808  38.802  1.00 152.44 ? 1297 GLU A CG    1 
ATOM   640  C  CD    . GLU A 1 80  ? -26.634 -8.815  39.103  1.00 160.07 ? 1297 GLU A CD    1 
ATOM   641  O  OE1   . GLU A 1 80  ? -27.207 -9.882  39.361  1.00 162.04 ? 1297 GLU A OE1   1 
ATOM   642  O  OE2   . GLU A 1 80  ? -27.232 -7.732  39.104  1.00 161.61 ? 1297 GLU A OE2   1 
ATOM   643  N  N     . LYS A 1 81  ? -21.374 -11.878 38.357  1.00 124.67 ? 1298 LYS A N     1 
ATOM   644  C  CA    . LYS A 1 81  ? -20.608 -12.740 37.509  1.00 126.41 ? 1298 LYS A CA    1 
ATOM   645  C  C     . LYS A 1 81  ? -21.266 -14.007 37.033  1.00 137.98 ? 1298 LYS A C     1 
ATOM   646  O  O     . LYS A 1 81  ? -21.723 -14.842 37.796  1.00 137.86 ? 1298 LYS A O     1 
ATOM   647  C  CB    . LYS A 1 81  ? -19.349 -13.124 38.257  1.00 119.44 ? 1298 LYS A CB    1 
ATOM   648  N  N     . THR A 1 82  ? -21.224 -14.144 35.714  1.00 146.24 ? 1299 THR A N     1 
ATOM   649  C  CA    . THR A 1 82  ? -21.775 -15.266 34.982  1.00 148.63 ? 1299 THR A CA    1 
ATOM   650  C  C     . THR A 1 82  ? -21.030 -16.452 35.379  1.00 160.18 ? 1299 THR A C     1 
ATOM   651  O  O     . THR A 1 82  ? -21.581 -17.477 35.747  1.00 163.94 ? 1299 THR A O     1 
ATOM   652  C  CB    . THR A 1 82  ? -21.316 -15.123 33.541  1.00 134.28 ? 1299 THR A CB    1 
ATOM   653  O  OG1   . THR A 1 82  ? -21.671 -13.830 33.080  1.00 128.97 ? 1299 THR A OG1   1 
ATOM   654  C  CG2   . THR A 1 82  ? -21.899 -16.173 32.661  1.00 124.43 ? 1299 THR A CG2   1 
ATOM   655  N  N     . HIS A 1 83  ? -19.729 -16.275 35.308  1.00 158.73 ? 1300 HIS A N     1 
ATOM   656  C  CA    . HIS A 1 83  ? -18.821 -17.282 35.684  1.00 160.90 ? 1300 HIS A CA    1 
ATOM   657  C  C     . HIS A 1 83  ? -17.586 -16.599 36.162  1.00 163.01 ? 1300 HIS A C     1 
ATOM   658  O  O     . HIS A 1 83  ? -16.862 -16.036 35.378  1.00 167.65 ? 1300 HIS A O     1 
ATOM   659  C  CB    . HIS A 1 83  ? -18.470 -18.122 34.477  1.00 156.55 ? 1300 HIS A CB    1 
ATOM   660  N  N     . ILE A 1 84  ? -17.325 -16.613 37.465  1.00 158.54 ? 1301 ILE A N     1 
ATOM   661  C  CA    . ILE A 1 84  ? -16.028 -16.141 37.922  1.00 150.35 ? 1301 ILE A CA    1 
ATOM   662  C  C     . ILE A 1 84  ? -15.126 -17.238 37.373  1.00 145.97 ? 1301 ILE A C     1 
ATOM   663  O  O     . ILE A 1 84  ? -14.124 -16.963 36.760  1.00 137.64 ? 1301 ILE A O     1 
ATOM   664  C  CB    . ILE A 1 84  ? -15.963 -16.083 39.445  1.00 146.43 ? 1301 ILE A CB    1 
ATOM   665  N  N     . ALA A 1 85  ? -15.499 -18.487 37.657  1.00 151.15 ? 1302 ALA A N     1 
ATOM   666  C  CA    . ALA A 1 85  ? -14.973 -19.635 36.989  1.00 152.41 ? 1302 ALA A CA    1 
ATOM   667  C  C     . ALA A 1 85  ? -13.493 -19.696 36.913  1.00 152.18 ? 1302 ALA A C     1 
ATOM   668  O  O     . ALA A 1 85  ? -12.808 -19.574 37.886  1.00 153.64 ? 1302 ALA A O     1 
ATOM   669  C  CB    . ALA A 1 85  ? -15.628 -19.736 35.609  1.00 147.21 ? 1302 ALA A CB    1 
ATOM   670  N  N     . ASP A 1 86  ? -13.017 -19.859 35.712  1.00 150.52 ? 1303 ASP A N     1 
ATOM   671  C  CA    . ASP A 1 86  ? -11.639 -19.938 35.494  1.00 147.55 ? 1303 ASP A CA    1 
ATOM   672  C  C     . ASP A 1 86  ? -11.571 -19.294 34.175  1.00 136.90 ? 1303 ASP A C     1 
ATOM   673  O  O     . ASP A 1 86  ? -10.800 -19.678 33.336  1.00 142.91 ? 1303 ASP A O     1 
ATOM   674  C  CB    . ASP A 1 86  ? -11.203 -21.394 35.427  1.00 150.20 ? 1303 ASP A CB    1 
ATOM   675  N  N     . PHE A 1 87  ? -12.433 -18.328 33.973  1.00 118.49 ? 1304 PHE A N     1 
ATOM   676  C  CA    . PHE A 1 87  ? -12.395 -17.582 32.725  1.00 106.43 ? 1304 PHE A CA    1 
ATOM   677  C  C     . PHE A 1 87  ? -11.690 -16.240 32.866  1.00 103.65 ? 1304 PHE A C     1 
ATOM   678  O  O     . PHE A 1 87  ? -10.985 -15.827 31.942  1.00 99.98  ? 1304 PHE A O     1 
ATOM   679  C  CB    . PHE A 1 87  ? -13.820 -17.332 32.214  1.00 101.97 ? 1304 PHE A CB    1 
ATOM   680  C  CG    . PHE A 1 87  ? -14.404 -18.465 31.406  1.00 103.49 ? 1304 PHE A CG    1 
ATOM   681  C  CD1   . PHE A 1 87  ? -13.668 -19.087 30.407  1.00 101.19 ? 1304 PHE A CD1   1 
ATOM   682  C  CD2   . PHE A 1 87  ? -15.718 -18.886 31.626  1.00 103.90 ? 1304 PHE A CD2   1 
ATOM   683  C  CE1   . PHE A 1 87  ? -14.226 -20.133 29.653  1.00 98.18  ? 1304 PHE A CE1   1 
ATOM   684  C  CE2   . PHE A 1 87  ? -16.281 -19.931 30.872  1.00 97.91  ? 1304 PHE A CE2   1 
ATOM   685  C  CZ    . PHE A 1 87  ? -15.533 -20.553 29.887  1.00 91.40  ? 1304 PHE A CZ    1 
ATOM   686  N  N     . ALA A 1 88  ? -11.801 -15.601 34.033  1.00 106.07 ? 1305 ALA A N     1 
ATOM   687  C  CA    . ALA A 1 88  ? -11.260 -14.255 34.215  1.00 106.38 ? 1305 ALA A CA    1 
ATOM   688  C  C     . ALA A 1 88  ? -9.813  -14.135 33.755  1.00 115.74 ? 1305 ALA A C     1 
ATOM   689  O  O     . ALA A 1 88  ? -9.461  -13.093 33.175  1.00 115.73 ? 1305 ALA A O     1 
ATOM   690  C  CB    . ALA A 1 88  ? -11.417 -13.836 35.685  1.00 103.56 ? 1305 ALA A CB    1 
ATOM   691  N  N     . PRO A 1 89  ? -8.944  -15.130 33.951  1.00 115.34 ? 1306 PRO A N     1 
ATOM   692  C  CA    . PRO A 1 89  ? -7.600  -15.029 33.372  1.00 116.72 ? 1306 PRO A CA    1 
ATOM   693  C  C     . PRO A 1 89  ? -7.578  -14.848 31.859  1.00 107.28 ? 1306 PRO A C     1 
ATOM   694  O  O     . PRO A 1 89  ? -6.612  -14.295 31.322  1.00 108.60 ? 1306 PRO A O     1 
ATOM   695  C  CB    . PRO A 1 89  ? -6.950  -16.362 33.776  1.00 121.66 ? 1306 PRO A CB    1 
ATOM   696  C  CG    . PRO A 1 89  ? -8.075  -17.208 34.387  1.00 117.78 ? 1306 PRO A CG    1 
ATOM   697  C  CD    . PRO A 1 89  ? -9.006  -16.210 34.948  1.00 116.14 ? 1306 PRO A CD    1 
ATOM   698  N  N     . GLU A 1 90  ? -8.604  -15.300 31.141  1.00 100.50 ? 1307 GLU A N     1 
ATOM   699  C  CA    . GLU A 1 90  ? -8.559  -15.299 29.684  1.00 98.79  ? 1307 GLU A CA    1 
ATOM   700  C  C     . GLU A 1 90  ? -9.141  -14.035 29.070  1.00 95.32  ? 1307 GLU A C     1 
ATOM   701  O  O     . GLU A 1 90  ? -9.666  -14.098 27.952  1.00 102.36 ? 1307 GLU A O     1 
ATOM   702  C  CB    . GLU A 1 90  ? -9.309  -16.518 29.134  1.00 100.98 ? 1307 GLU A CB    1 
ATOM   703  C  CG    . GLU A 1 90  ? -9.081  -17.824 29.873  1.00 109.11 ? 1307 GLU A CG    1 
ATOM   704  C  CD    . GLU A 1 90  ? -9.240  -19.036 28.963  1.00 116.71 ? 1307 GLU A CD    1 
ATOM   705  O  OE1   . GLU A 1 90  ? -8.263  -19.814 28.867  1.00 119.30 ? 1307 GLU A OE1   1 
ATOM   706  O  OE2   . GLU A 1 90  ? -10.333 -19.213 28.357  1.00 116.08 ? 1307 GLU A OE2   1 
ATOM   707  N  N     . VAL A 1 91  ? -9.008  -12.878 29.711  1.00 92.18  ? 1308 VAL A N     1 
ATOM   708  C  CA    . VAL A 1 91  ? -9.711  -11.676 29.276  1.00 90.80  ? 1308 VAL A CA    1 
ATOM   709  C  C     . VAL A 1 91  ? -8.704  -10.605 28.874  1.00 87.80  ? 1308 VAL A C     1 
ATOM   710  O  O     . VAL A 1 91  ? -7.871  -10.184 29.684  1.00 92.07  ? 1308 VAL A O     1 
ATOM   711  C  CB    . VAL A 1 91  ? -10.645 -11.157 30.380  1.00 88.00  ? 1308 VAL A CB    1 
ATOM   712  C  CG1   . VAL A 1 91  ? -11.416 -9.905  29.913  1.00 76.96  ? 1308 VAL A CG1   1 
ATOM   713  C  CG2   . VAL A 1 91  ? -11.574 -12.289 30.846  1.00 85.57  ? 1308 VAL A CG2   1 
ATOM   714  N  N     . ALA A 1 92  ? -8.817  -10.135 27.638  1.00 82.27  ? 1309 ALA A N     1 
ATOM   715  C  CA    . ALA A 1 92  ? -7.915  -9.118  27.116  1.00 89.42  ? 1309 ALA A CA    1 
ATOM   716  C  C     . ALA A 1 92  ? -8.341  -7.757  27.650  1.00 87.98  ? 1309 ALA A C     1 
ATOM   717  O  O     . ALA A 1 92  ? -9.479  -7.323  27.431  1.00 86.27  ? 1309 ALA A O     1 
ATOM   718  C  CB    . ALA A 1 92  ? -7.930  -9.129  25.587  1.00 88.51  ? 1309 ALA A CB    1 
ATOM   719  N  N     . TRP A 1 93  ? -7.419  -7.069  28.313  1.00 83.88  ? 1310 TRP A N     1 
ATOM   720  C  CA    . TRP A 1 93  ? -7.721  -5.823  28.996  1.00 90.62  ? 1310 TRP A CA    1 
ATOM   721  C  C     . TRP A 1 93  ? -6.952  -4.684  28.352  1.00 88.33  ? 1310 TRP A C     1 
ATOM   722  O  O     . TRP A 1 93  ? -5.720  -4.642  28.399  1.00 83.76  ? 1310 TRP A O     1 
ATOM   723  C  CB    . TRP A 1 93  ? -7.386  -5.901  30.479  1.00 95.15  ? 1310 TRP A CB    1 
ATOM   724  C  CG    . TRP A 1 93  ? -8.373  -6.680  31.258  1.00 95.59  ? 1310 TRP A CG    1 
ATOM   725  C  CD1   . TRP A 1 93  ? -8.228  -7.952  31.709  1.00 99.68  ? 1310 TRP A CD1   1 
ATOM   726  C  CD2   . TRP A 1 93  ? -9.675  -6.251  31.671  1.00 101.78 ? 1310 TRP A CD2   1 
ATOM   727  N  NE1   . TRP A 1 93  ? -9.356  -8.346  32.385  1.00 103.29 ? 1310 TRP A NE1   1 
ATOM   728  C  CE2   . TRP A 1 93  ? -10.262 -7.320  32.374  1.00 99.70  ? 1310 TRP A CE2   1 
ATOM   729  C  CE3   . TRP A 1 93  ? -10.404 -5.067  31.511  1.00 105.26 ? 1310 TRP A CE3   1 
ATOM   730  C  CZ2   . TRP A 1 93  ? -11.541 -7.241  32.927  1.00 90.82  ? 1310 TRP A CZ2   1 
ATOM   731  C  CZ3   . TRP A 1 93  ? -11.684 -4.992  32.061  1.00 101.29 ? 1310 TRP A CZ3   1 
ATOM   732  C  CH2   . TRP A 1 93  ? -12.232 -6.072  32.763  1.00 94.72  ? 1310 TRP A CH2   1 
ATOM   733  N  N     . VAL A 1 94  ? -7.697  -3.757  27.766  1.00 80.92  ? 1311 VAL A N     1 
ATOM   734  C  CA    . VAL A 1 94  ? -7.163  -2.450  27.451  1.00 74.40  ? 1311 VAL A CA    1 
ATOM   735  C  C     . VAL A 1 94  ? -6.947  -1.696  28.751  1.00 80.22  ? 1311 VAL A C     1 
ATOM   736  O  O     . VAL A 1 94  ? -7.781  -1.746  29.664  1.00 80.52  ? 1311 VAL A O     1 
ATOM   737  C  CB    . VAL A 1 94  ? -8.118  -1.707  26.513  1.00 75.68  ? 1311 VAL A CB    1 
ATOM   738  C  CG1   . VAL A 1 94  ? -7.685  -0.265  26.351  1.00 81.38  ? 1311 VAL A CG1   1 
ATOM   739  C  CG2   . VAL A 1 94  ? -8.183  -2.450  25.173  1.00 73.26  ? 1311 VAL A CG2   1 
ATOM   740  N  N     . THR A 1 95  ? -5.795  -1.054  28.879  1.00 88.06  ? 1312 THR A N     1 
ATOM   741  C  CA    . THR A 1 95  ? -5.601  -0.232  30.059  1.00 93.44  ? 1312 THR A CA    1 
ATOM   742  C  C     . THR A 1 95  ? -4.830  1.040   29.779  1.00 93.96  ? 1312 THR A C     1 
ATOM   743  O  O     . THR A 1 95  ? -4.485  1.742   30.737  1.00 97.03  ? 1312 THR A O     1 
ATOM   744  C  CB    . THR A 1 95  ? -4.892  -1.021  31.159  1.00 100.06 ? 1312 THR A CB    1 
ATOM   745  O  OG1   . THR A 1 95  ? -4.453  -0.109  32.175  1.00 107.42 ? 1312 THR A OG1   1 
ATOM   746  C  CG2   . THR A 1 95  ? -3.707  -1.758  30.571  1.00 91.33  ? 1312 THR A CG2   1 
ATOM   747  N  N     . LYS A 1 96  ? -4.571  1.386   28.525  1.00 93.01  ? 1313 LYS A N     1 
ATOM   748  C  CA    . LYS A 1 96  ? -3.926  2.661   28.261  1.00 100.69 ? 1313 LYS A CA    1 
ATOM   749  C  C     . LYS A 1 96  ? -4.362  3.170   26.892  1.00 89.46  ? 1313 LYS A C     1 
ATOM   750  O  O     . LYS A 1 96  ? -4.504  2.401   25.937  1.00 81.80  ? 1313 LYS A O     1 
ATOM   751  C  CB    . LYS A 1 96  ? -2.391  2.549   28.401  1.00 113.01 ? 1313 LYS A CB    1 
ATOM   752  C  CG    . LYS A 1 96  ? -1.614  2.060   27.183  1.00 122.84 ? 1313 LYS A CG    1 
ATOM   753  C  CD    . LYS A 1 96  ? -0.141  2.514   27.234  1.00 131.42 ? 1313 LYS A CD    1 
ATOM   754  C  CE    . LYS A 1 96  ? 0.811   1.600   26.431  1.00 130.88 ? 1313 LYS A CE    1 
ATOM   755  N  NZ    . LYS A 1 96  ? 1.885   2.362   25.694  1.00 127.29 ? 1313 LYS A NZ    1 
ATOM   756  N  N     . SER A 1 97  ? -4.641  4.471   26.838  1.00 87.88  ? 1314 SER A N     1 
ATOM   757  C  CA    . SER A 1 97  ? -4.868  5.213   25.601  1.00 85.04  ? 1314 SER A CA    1 
ATOM   758  C  C     . SER A 1 97  ? -3.547  5.904   25.233  1.00 97.11  ? 1314 SER A C     1 
ATOM   759  O  O     . SER A 1 97  ? -3.141  6.870   25.887  1.00 91.71  ? 1314 SER A O     1 
ATOM   760  C  CB    . SER A 1 97  ? -5.994  6.223   25.797  1.00 89.04  ? 1314 SER A CB    1 
ATOM   761  O  OG    . SER A 1 97  ? -5.790  7.377   25.019  1.00 103.93 ? 1314 SER A OG    1 
ATOM   762  N  N     . GLY A 1 98  ? -2.873  5.407   24.197  1.00 94.93  ? 1315 GLY A N     1 
ATOM   763  C  CA    . GLY A 1 98  ? -1.600  5.996   23.842  1.00 86.25  ? 1315 GLY A CA    1 
ATOM   764  C  C     . GLY A 1 98  ? -0.595  5.786   24.955  1.00 99.47  ? 1315 GLY A C     1 
ATOM   765  O  O     . GLY A 1 98  ? -0.051  4.690   25.112  1.00 94.53  ? 1315 GLY A O     1 
ATOM   766  N  N     . ASP A 1 99  ? -0.309  6.843   25.716  1.00 108.63 ? 1316 ASP A N     1 
ATOM   767  C  CA    . ASP A 1 99  ? 0.484   6.736   26.931  1.00 116.64 ? 1316 ASP A CA    1 
ATOM   768  C  C     . ASP A 1 99  ? -0.315  7.062   28.179  1.00 115.08 ? 1316 ASP A C     1 
ATOM   769  O  O     . ASP A 1 99  ? 0.228   6.979   29.287  1.00 112.47 ? 1316 ASP A O     1 
ATOM   770  C  CB    . ASP A 1 99  ? 1.705   7.642   26.848  1.00 122.76 ? 1316 ASP A CB    1 
ATOM   771  C  CG    . ASP A 1 99  ? 2.906   6.912   26.349  1.00 129.20 ? 1316 ASP A CG    1 
ATOM   772  O  OD1   . ASP A 1 99  ? 2.900   5.669   26.472  1.00 124.15 ? 1316 ASP A OD1   1 
ATOM   773  O  OD2   . ASP A 1 99  ? 3.837   7.566   25.832  1.00 140.15 ? 1316 ASP A OD2   1 
ATOM   774  N  N     . SER A 1 100 ? -1.578  7.444   28.026  1.00 113.61 ? 1317 SER A N     1 
ATOM   775  C  CA    . SER A 1 100 ? -2.447  7.705   29.163  1.00 116.75 ? 1317 SER A CA    1 
ATOM   776  C  C     . SER A 1 100 ? -3.148  6.418   29.591  1.00 117.49 ? 1317 SER A C     1 
ATOM   777  O  O     . SER A 1 100 ? -3.908  5.827   28.814  1.00 114.15 ? 1317 SER A O     1 
ATOM   778  C  CB    . SER A 1 100 ? -3.468  8.782   28.802  1.00 118.91 ? 1317 SER A CB    1 
ATOM   779  O  OG    . SER A 1 100 ? -2.839  9.909   28.211  1.00 122.63 ? 1317 SER A OG    1 
ATOM   780  N  N     . GLU A 1 101 ? -2.891  5.982   30.821  1.00 116.46 ? 1318 GLU A N     1 
ATOM   781  C  CA    . GLU A 1 101 ? -3.602  4.842   31.380  1.00 97.80  ? 1318 GLU A CA    1 
ATOM   782  C  C     . GLU A 1 101 ? -4.995  5.307   31.785  1.00 106.03 ? 1318 GLU A C     1 
ATOM   783  O  O     . GLU A 1 101 ? -5.166  6.417   32.290  1.00 107.05 ? 1318 GLU A O     1 
ATOM   784  C  CB    . GLU A 1 101 ? -2.845  4.270   32.585  1.00 77.31  ? 1318 GLU A CB    1 
ATOM   785  N  N     . LEU A 1 102 ? -6.000  4.469   31.559  1.00 108.37 ? 1319 LEU A N     1 
ATOM   786  C  CA    . LEU A 1 102 ? -7.360  4.910   31.844  1.00 109.03 ? 1319 LEU A CA    1 
ATOM   787  C  C     . LEU A 1 102 ? -7.788  4.485   33.240  1.00 117.64 ? 1319 LEU A C     1 
ATOM   788  O  O     . LEU A 1 102 ? -7.287  3.503   33.799  1.00 121.71 ? 1319 LEU A O     1 
ATOM   789  C  CB    . LEU A 1 102 ? -8.353  4.363   30.826  1.00 97.81  ? 1319 LEU A CB    1 
ATOM   790  C  CG    . LEU A 1 102 ? -7.953  4.487   29.367  1.00 102.61 ? 1319 LEU A CG    1 
ATOM   791  C  CD1   . LEU A 1 102 ? -7.254  3.227   28.930  1.00 103.40 ? 1319 LEU A CD1   1 
ATOM   792  C  CD2   . LEU A 1 102 ? -9.171  4.737   28.507  1.00 103.25 ? 1319 LEU A CD2   1 
ATOM   793  N  N     . ALA A 1 103 ? -8.758  5.229   33.783  1.00 121.12 ? 1320 ALA A N     1 
ATOM   794  C  CA    . ALA A 1 103 ? -9.148  5.077   35.183  1.00 122.09 ? 1320 ALA A CA    1 
ATOM   795  C  C     . ALA A 1 103 ? -9.648  3.666   35.455  1.00 120.60 ? 1320 ALA A C     1 
ATOM   796  O  O     . ALA A 1 103 ? -9.104  2.948   36.302  1.00 127.33 ? 1320 ALA A O     1 
ATOM   797  C  CB    . ALA A 1 103 ? -10.218 6.104   35.542  1.00 122.68 ? 1320 ALA A CB    1 
ATOM   798  N  N     . GLU A 1 104 ? -10.694 3.267   34.770  1.00 111.89 ? 1321 GLU A N     1 
ATOM   799  C  CA    . GLU A 1 104 ? -11.085 1.882   34.837  1.00 106.38 ? 1321 GLU A CA    1 
ATOM   800  C  C     . GLU A 1 104 ? -10.716 1.229   33.515  1.00 109.10 ? 1321 GLU A C     1 
ATOM   801  O  O     . GLU A 1 104 ? -10.772 1.889   32.471  1.00 101.82 ? 1321 GLU A O     1 
ATOM   802  C  CB    . GLU A 1 104 ? -12.585 1.721   35.106  1.00 98.47  ? 1321 GLU A CB    1 
ATOM   803  N  N     . PRO A 1 105 ? -10.231 -0.011  33.538  1.00 114.66 ? 1322 PRO A N     1 
ATOM   804  C  CA    . PRO A 1 105 ? -9.859  -0.698  32.298  1.00 111.12 ? 1322 PRO A CA    1 
ATOM   805  C  C     . PRO A 1 105 ? -11.050 -1.382  31.645  1.00 99.59  ? 1322 PRO A C     1 
ATOM   806  O  O     . PRO A 1 105 ? -11.995 -1.817  32.303  1.00 101.41 ? 1322 PRO A O     1 
ATOM   807  C  CB    . PRO A 1 105 ? -8.811  -1.719  32.772  1.00 116.56 ? 1322 PRO A CB    1 
ATOM   808  C  CG    . PRO A 1 105 ? -9.026  -1.861  34.277  1.00 119.50 ? 1322 PRO A CG    1 
ATOM   809  C  CD    . PRO A 1 105 ? -10.107 -0.898  34.704  1.00 118.39 ? 1322 PRO A CD    1 
ATOM   810  N  N     . ILE A 1 106 ? -10.988 -1.477  30.317  1.00 89.98  ? 1323 ILE A N     1 
ATOM   811  C  CA    . ILE A 1 106 ? -12.071 -2.036  29.517  1.00 87.94  ? 1323 ILE A CA    1 
ATOM   812  C  C     . ILE A 1 106 ? -11.591 -3.304  28.824  1.00 81.40  ? 1323 ILE A C     1 
ATOM   813  O  O     . ILE A 1 106 ? -10.427 -3.406  28.421  1.00 81.55  ? 1323 ILE A O     1 
ATOM   814  C  CB    . ILE A 1 106 ? -12.582 -0.994  28.501  1.00 91.87  ? 1323 ILE A CB    1 
ATOM   815  C  CG1   . ILE A 1 106 ? -11.506 -0.658  27.473  1.00 91.50  ? 1323 ILE A CG1   1 
ATOM   816  C  CG2   . ILE A 1 106 ? -12.937 0.278   29.227  1.00 89.66  ? 1323 ILE A CG2   1 
ATOM   817  C  CD1   . ILE A 1 106 ? -11.914 0.431   26.500  1.00 88.60  ? 1323 ILE A CD1   1 
ATOM   818  N  N     . ALA A 1 107 ? -12.483 -4.281  28.709  1.00 76.74  ? 1324 ALA A N     1 
ATOM   819  C  CA    . ALA A 1 107 ? -12.143 -5.603  28.202  1.00 66.32  ? 1324 ALA A CA    1 
ATOM   820  C  C     . ALA A 1 107 ? -12.651 -5.790  26.780  1.00 64.94  ? 1324 ALA A C     1 
ATOM   821  O  O     . ALA A 1 107 ? -13.742 -5.339  26.433  1.00 67.16  ? 1324 ALA A O     1 
ATOM   822  C  CB    . ALA A 1 107 ? -12.737 -6.677  29.104  1.00 65.44  ? 1324 ALA A CB    1 
ATOM   823  N  N     . VAL A 1 108 ? -11.865 -6.461  25.961  1.00 59.66  ? 1325 VAL A N     1 
ATOM   824  C  CA    . VAL A 1 108 ? -12.341 -6.864  24.644  1.00 65.42  ? 1325 VAL A CA    1 
ATOM   825  C  C     . VAL A 1 108 ? -13.245 -8.092  24.793  1.00 72.24  ? 1325 VAL A C     1 
ATOM   826  O  O     . VAL A 1 108 ? -12.907 -9.049  25.499  1.00 70.30  ? 1325 VAL A O     1 
ATOM   827  C  CB    . VAL A 1 108 ? -11.155 -7.127  23.708  1.00 64.62  ? 1325 VAL A CB    1 
ATOM   828  C  CG1   . VAL A 1 108 ? -11.625 -7.761  22.380  1.00 50.94  ? 1325 VAL A CG1   1 
ATOM   829  C  CG2   . VAL A 1 108 ? -10.400 -5.832  23.491  1.00 49.30  ? 1325 VAL A CG2   1 
ATOM   830  N  N     . ARG A 1 109 ? -14.415 -8.050  24.157  1.00 76.69  ? 1326 ARG A N     1 
ATOM   831  C  CA    . ARG A 1 109 ? -15.479 -9.009  24.450  1.00 77.33  ? 1326 ARG A CA    1 
ATOM   832  C  C     . ARG A 1 109 ? -15.051 -10.447 24.189  1.00 73.35  ? 1326 ARG A C     1 
ATOM   833  O  O     . ARG A 1 109 ? -14.464 -10.741 23.132  1.00 55.06  ? 1326 ARG A O     1 
ATOM   834  C  CB    . ARG A 1 109 ? -16.717 -8.722  23.611  1.00 80.00  ? 1326 ARG A CB    1 
ATOM   835  C  CG    . ARG A 1 109 ? -16.408 -8.503  22.164  1.00 81.57  ? 1326 ARG A CG    1 
ATOM   836  C  CD    . ARG A 1 109 ? -17.537 -8.943  21.259  1.00 83.35  ? 1326 ARG A CD    1 
ATOM   837  N  NE    . ARG A 1 109 ? -17.306 -8.384  19.938  1.00 86.03  ? 1326 ARG A NE    1 
ATOM   838  C  CZ    . ARG A 1 109 ? -18.020 -7.404  19.400  1.00 81.11  ? 1326 ARG A CZ    1 
ATOM   839  N  NH1   . ARG A 1 109 ? -19.054 -6.886  20.058  1.00 80.63  ? 1326 ARG A NH1   1 
ATOM   840  N  NH2   . ARG A 1 109 ? -17.699 -6.956  18.194  1.00 73.62  ? 1326 ARG A NH2   1 
ATOM   841  N  N     . PRO A 1 110 ? -15.352 -11.370 25.099  1.00 85.33  ? 1327 PRO A N     1 
ATOM   842  C  CA    . PRO A 1 110 ? -15.158 -12.799 24.814  1.00 78.58  ? 1327 PRO A CA    1 
ATOM   843  C  C     . PRO A 1 110 ? -16.464 -13.458 24.403  1.00 79.94  ? 1327 PRO A C     1 
ATOM   844  O  O     . PRO A 1 110 ? -16.474 -14.596 23.925  1.00 84.57  ? 1327 PRO A O     1 
ATOM   845  C  CB    . PRO A 1 110 ? -14.658 -13.340 26.152  1.00 69.47  ? 1327 PRO A CB    1 
ATOM   846  C  CG    . PRO A 1 110 ? -15.355 -12.461 27.180  1.00 74.52  ? 1327 PRO A CG    1 
ATOM   847  C  CD    . PRO A 1 110 ? -15.668 -11.123 26.517  1.00 81.62  ? 1327 PRO A CD    1 
ATOM   848  N  N     . THR A 1 111 ? -17.560 -12.706 24.577  1.00 81.47  ? 1328 THR A N     1 
ATOM   849  C  CA    . THR A 1 111 ? -18.959 -13.064 24.347  1.00 79.38  ? 1328 THR A CA    1 
ATOM   850  C  C     . THR A 1 111 ? -19.771 -11.891 24.889  1.00 79.85  ? 1328 THR A C     1 
ATOM   851  O  O     . THR A 1 111 ? -19.241 -11.095 25.677  1.00 75.95  ? 1328 THR A O     1 
ATOM   852  C  CB    . THR A 1 111 ? -19.340 -14.391 25.022  1.00 71.79  ? 1328 THR A CB    1 
ATOM   853  O  OG1   . THR A 1 111 ? -20.738 -14.642 24.847  1.00 79.75  ? 1328 THR A OG1   1 
ATOM   854  C  CG2   . THR A 1 111 ? -19.016 -14.374 26.508  1.00 60.01  ? 1328 THR A CG2   1 
ATOM   855  N  N     . SER A 1 112 ? -21.051 -11.752 24.527  1.00 76.83  ? 1329 SER A N     1 
ATOM   856  C  CA    . SER A 1 112 ? -21.735 -10.494 24.831  1.00 75.73  ? 1329 SER A CA    1 
ATOM   857  C  C     . SER A 1 112 ? -22.885 -10.634 25.828  1.00 71.58  ? 1329 SER A C     1 
ATOM   858  O  O     . SER A 1 112 ? -23.806 -9.821  25.825  1.00 78.99  ? 1329 SER A O     1 
ATOM   859  C  CB    . SER A 1 112 ? -22.235 -9.840  23.540  1.00 70.76  ? 1329 SER A CB    1 
ATOM   860  O  OG    . SER A 1 112 ? -21.241 -9.910  22.524  1.00 73.20  ? 1329 SER A OG    1 
ATOM   861  N  N     . GLU A 1 113 ? -22.831 -11.611 26.730  1.00 68.62  ? 1330 GLU A N     1 
ATOM   862  C  CA    . GLU A 1 113 ? -23.928 -11.787 27.685  1.00 72.37  ? 1330 GLU A CA    1 
ATOM   863  C  C     . GLU A 1 113 ? -24.046 -10.578 28.608  1.00 78.80  ? 1330 GLU A C     1 
ATOM   864  O  O     . GLU A 1 113 ? -25.129 -10.003 28.774  1.00 77.13  ? 1330 GLU A O     1 
ATOM   865  C  CB    . GLU A 1 113 ? -23.729 -13.072 28.509  1.00 55.70  ? 1330 GLU A CB    1 
ATOM   866  C  CG    . GLU A 1 113 ? -24.270 -14.356 27.850  1.00 71.04  ? 1330 GLU A CG    1 
ATOM   867  C  CD    . GLU A 1 113 ? -23.232 -15.123 27.008  1.00 78.98  ? 1330 GLU A CD    1 
ATOM   868  O  OE1   . GLU A 1 113 ? -22.205 -14.544 26.601  1.00 77.84  ? 1330 GLU A OE1   1 
ATOM   869  O  OE2   . GLU A 1 113 ? -23.453 -16.317 26.731  1.00 85.70  ? 1330 GLU A OE2   1 
ATOM   870  N  N     . THR A 1 114 ? -22.934 -10.186 29.219  1.00 81.72  ? 1331 THR A N     1 
ATOM   871  C  CA    . THR A 1 114 ? -22.930 -9.155  30.237  1.00 84.96  ? 1331 THR A CA    1 
ATOM   872  C  C     . THR A 1 114 ? -23.277 -7.776  29.699  1.00 86.85  ? 1331 THR A C     1 
ATOM   873  O  O     . THR A 1 114 ? -23.459 -6.845  30.491  1.00 78.87  ? 1331 THR A O     1 
ATOM   874  C  CB    . THR A 1 114 ? -21.574 -9.132  30.914  1.00 81.31  ? 1331 THR A CB    1 
ATOM   875  O  OG1   . THR A 1 114 ? -20.711 -8.254  30.185  1.00 86.21  ? 1331 THR A OG1   1 
ATOM   876  C  CG2   . THR A 1 114 ? -20.987 -10.512 30.903  1.00 76.56  ? 1331 THR A CG2   1 
ATOM   877  N  N     . VAL A 1 115 ? -23.349 -7.612  28.383  1.00 88.40  ? 1332 VAL A N     1 
ATOM   878  C  CA    . VAL A 1 115 ? -23.743 -6.355  27.777  1.00 85.87  ? 1332 VAL A CA    1 
ATOM   879  C  C     . VAL A 1 115 ? -25.158 -6.433  27.226  1.00 83.84  ? 1332 VAL A C     1 
ATOM   880  O  O     . VAL A 1 115 ? -25.967 -5.521  27.437  1.00 87.01  ? 1332 VAL A O     1 
ATOM   881  C  CB    . VAL A 1 115 ? -22.737 -5.933  26.690  1.00 80.06  ? 1332 VAL A CB    1 
ATOM   882  C  CG1   . VAL A 1 115 ? -21.546 -5.364  27.358  1.00 80.98  ? 1332 VAL A CG1   1 
ATOM   883  C  CG2   . VAL A 1 115 ? -22.332 -7.122  25.904  1.00 82.99  ? 1332 VAL A CG2   1 
ATOM   884  N  N     . MET A 1 116 ? -25.492 -7.549  26.571  1.00 76.94  ? 1333 MET A N     1 
ATOM   885  C  CA    . MET A 1 116 ? -26.807 -7.675  25.962  1.00 73.68  ? 1333 MET A CA    1 
ATOM   886  C  C     . MET A 1 116 ? -27.886 -7.981  26.978  1.00 70.98  ? 1333 MET A C     1 
ATOM   887  O  O     . MET A 1 116 ? -29.052 -7.767  26.673  1.00 82.12  ? 1333 MET A O     1 
ATOM   888  C  CB    . MET A 1 116 ? -26.797 -8.753  24.886  1.00 77.15  ? 1333 MET A CB    1 
ATOM   889  C  CG    . MET A 1 116 ? -25.906 -8.443  23.697  1.00 82.09  ? 1333 MET A CG    1 
ATOM   890  S  SD    . MET A 1 116 ? -25.986 -9.741  22.450  1.00 88.78  ? 1333 MET A SD    1 
ATOM   891  C  CE    . MET A 1 116 ? -27.700 -9.621  21.971  1.00 75.44  ? 1333 MET A CE    1 
ATOM   892  N  N     . TYR A 1 117 ? -27.541 -8.442  28.177  1.00 65.35  ? 1334 TYR A N     1 
ATOM   893  C  CA    . TYR A 1 117 ? -28.646 -8.776  29.074  1.00 75.91  ? 1334 TYR A CA    1 
ATOM   894  C  C     . TYR A 1 117 ? -29.157 -7.545  29.823  1.00 86.91  ? 1334 TYR A C     1 
ATOM   895  O  O     . TYR A 1 117 ? -30.379 -7.406  29.995  1.00 97.35  ? 1334 TYR A O     1 
ATOM   896  C  CB    . TYR A 1 117 ? -28.244 -9.937  29.994  1.00 70.42  ? 1334 TYR A CB    1 
ATOM   897  C  CG    . TYR A 1 117 ? -28.165 -11.215 29.166  1.00 71.46  ? 1334 TYR A CG    1 
ATOM   898  C  CD1   . TYR A 1 117 ? -28.556 -11.201 27.826  1.00 69.44  ? 1334 TYR A CD1   1 
ATOM   899  C  CD2   . TYR A 1 117 ? -27.699 -12.408 29.688  1.00 70.24  ? 1334 TYR A CD2   1 
ATOM   900  C  CE1   . TYR A 1 117 ? -28.488 -12.312 27.026  1.00 70.98  ? 1334 TYR A CE1   1 
ATOM   901  C  CE2   . TYR A 1 117 ? -27.636 -13.560 28.885  1.00 76.88  ? 1334 TYR A CE2   1 
ATOM   902  C  CZ    . TYR A 1 117 ? -28.035 -13.499 27.547  1.00 80.58  ? 1334 TYR A CZ    1 
ATOM   903  O  OH    . TYR A 1 117 ? -27.985 -14.606 26.713  1.00 81.56  ? 1334 TYR A OH    1 
ATOM   904  N  N     . PRO A 1 118 ? -28.295 -6.614  30.254  1.00 84.91  ? 1335 PRO A N     1 
ATOM   905  C  CA    . PRO A 1 118 ? -28.829 -5.312  30.709  1.00 89.06  ? 1335 PRO A CA    1 
ATOM   906  C  C     . PRO A 1 118 ? -29.670 -4.605  29.648  1.00 75.84  ? 1335 PRO A C     1 
ATOM   907  O  O     . PRO A 1 118 ? -30.692 -3.972  29.969  1.00 72.98  ? 1335 PRO A O     1 
ATOM   908  C  CB    . PRO A 1 118 ? -27.566 -4.512  31.062  1.00 92.34  ? 1335 PRO A CB    1 
ATOM   909  C  CG    . PRO A 1 118 ? -26.518 -5.508  31.298  1.00 92.86  ? 1335 PRO A CG    1 
ATOM   910  C  CD    . PRO A 1 118 ? -26.843 -6.727  30.487  1.00 80.88  ? 1335 PRO A CD    1 
ATOM   911  N  N     . ALA A 1 119 ? -29.260 -4.697  28.379  1.00 68.72  ? 1336 ALA A N     1 
ATOM   912  C  CA    . ALA A 1 119 ? -30.051 -4.095  27.311  1.00 69.02  ? 1336 ALA A CA    1 
ATOM   913  C  C     . ALA A 1 119 ? -31.441 -4.705  27.255  1.00 72.39  ? 1336 ALA A C     1 
ATOM   914  O  O     . ALA A 1 119 ? -32.439 -3.986  27.114  1.00 70.55  ? 1336 ALA A O     1 
ATOM   915  C  CB    . ALA A 1 119 ? -29.334 -4.252  25.967  1.00 71.01  ? 1336 ALA A CB    1 
ATOM   916  N  N     . TYR A 1 120 ? -31.531 -6.027  27.393  1.00 76.30  ? 1337 TYR A N     1 
ATOM   917  C  CA    . TYR A 1 120 ? -32.839 -6.670  27.401  1.00 78.43  ? 1337 TYR A CA    1 
ATOM   918  C  C     . TYR A 1 120 ? -33.646 -6.233  28.618  1.00 81.76  ? 1337 TYR A C     1 
ATOM   919  O  O     . TYR A 1 120 ? -34.868 -6.059  28.530  1.00 80.46  ? 1337 TYR A O     1 
ATOM   920  C  CB    . TYR A 1 120 ? -32.690 -8.201  27.352  1.00 74.95  ? 1337 TYR A CB    1 
ATOM   921  C  CG    . TYR A 1 120 ? -32.185 -8.764  26.019  1.00 69.31  ? 1337 TYR A CG    1 
ATOM   922  C  CD1   . TYR A 1 120 ? -31.502 -7.960  25.116  1.00 75.31  ? 1337 TYR A CD1   1 
ATOM   923  C  CD2   . TYR A 1 120 ? -32.414 -10.087 25.659  1.00 56.96  ? 1337 TYR A CD2   1 
ATOM   924  C  CE1   . TYR A 1 120 ? -31.036 -8.454  23.919  1.00 76.21  ? 1337 TYR A CE1   1 
ATOM   925  C  CE2   . TYR A 1 120 ? -31.949 -10.594 24.447  1.00 63.10  ? 1337 TYR A CE2   1 
ATOM   926  C  CZ    . TYR A 1 120 ? -31.253 -9.762  23.582  1.00 69.35  ? 1337 TYR A CZ    1 
ATOM   927  O  OH    . TYR A 1 120 ? -30.757 -10.208 22.370  1.00 64.59  ? 1337 TYR A OH    1 
ATOM   928  N  N     . ALA A 1 121 ? -32.977 -6.022  29.763  1.00 79.49  ? 1338 ALA A N     1 
ATOM   929  C  CA    . ALA A 1 121 ? -33.711 -5.569  30.944  1.00 77.90  ? 1338 ALA A CA    1 
ATOM   930  C  C     . ALA A 1 121 ? -34.322 -4.194  30.696  1.00 88.67  ? 1338 ALA A C     1 
ATOM   931  O  O     . ALA A 1 121 ? -35.447 -3.921  31.125  1.00 99.26  ? 1338 ALA A O     1 
ATOM   932  C  CB    . ALA A 1 121 ? -32.815 -5.561  32.182  1.00 58.10  ? 1338 ALA A CB    1 
ATOM   933  N  N     . LYS A 1 122 ? -33.616 -3.328  29.966  1.00 89.15  ? 1339 LYS A N     1 
ATOM   934  C  CA    . LYS A 1 122 ? -34.228 -2.051  29.611  1.00 87.82  ? 1339 LYS A CA    1 
ATOM   935  C  C     . LYS A 1 122 ? -35.320 -2.205  28.577  1.00 79.95  ? 1339 LYS A C     1 
ATOM   936  O  O     . LYS A 1 122 ? -36.361 -1.525  28.644  1.00 64.96  ? 1339 LYS A O     1 
ATOM   937  C  CB    . LYS A 1 122 ? -33.222 -1.118  28.983  1.00 100.61 ? 1339 LYS A CB    1 
ATOM   938  C  CG    . LYS A 1 122 ? -32.993 0.108   29.709  1.00 109.85 ? 1339 LYS A CG    1 
ATOM   939  C  CD    . LYS A 1 122 ? -32.513 1.203   28.748  1.00 112.48 ? 1339 LYS A CD    1 
ATOM   940  C  CE    . LYS A 1 122 ? -31.514 1.947   29.598  1.00 119.96 ? 1339 LYS A CE    1 
ATOM   941  N  NZ    . LYS A 1 122 ? -30.959 3.244   29.127  1.00 114.53 ? 1339 LYS A NZ    1 
ATOM   942  N  N     . TRP A 1 123 ? -35.107 -3.101  27.627  1.00 79.54  ? 1340 TRP A N     1 
ATOM   943  C  CA    . TRP A 1 123 ? -35.959 -3.074  26.465  1.00 75.56  ? 1340 TRP A CA    1 
ATOM   944  C  C     . TRP A 1 123 ? -37.249 -3.792  26.704  1.00 68.14  ? 1340 TRP A C     1 
ATOM   945  O  O     . TRP A 1 123 ? -38.153 -3.682  25.883  1.00 65.14  ? 1340 TRP A O     1 
ATOM   946  C  CB    . TRP A 1 123 ? -35.209 -3.659  25.279  1.00 74.52  ? 1340 TRP A CB    1 
ATOM   947  C  CG    . TRP A 1 123 ? -34.091 -2.809  24.811  1.00 73.83  ? 1340 TRP A CG    1 
ATOM   948  C  CD1   . TRP A 1 123 ? -33.872 -1.497  25.103  1.00 77.53  ? 1340 TRP A CD1   1 
ATOM   949  C  CD2   . TRP A 1 123 ? -33.016 -3.215  23.957  1.00 74.92  ? 1340 TRP A CD2   1 
ATOM   950  N  NE1   . TRP A 1 123 ? -32.729 -1.051  24.479  1.00 81.25  ? 1340 TRP A NE1   1 
ATOM   951  C  CE2   . TRP A 1 123 ? -32.180 -2.086  23.770  1.00 80.70  ? 1340 TRP A CE2   1 
ATOM   952  C  CE3   . TRP A 1 123 ? -32.680 -4.418  23.333  1.00 55.73  ? 1340 TRP A CE3   1 
ATOM   953  C  CZ2   . TRP A 1 123 ? -31.026 -2.128  22.984  1.00 76.50  ? 1340 TRP A CZ2   1 
ATOM   954  C  CZ3   . TRP A 1 123 ? -31.551 -4.461  22.556  1.00 69.97  ? 1340 TRP A CZ3   1 
ATOM   955  C  CH2   . TRP A 1 123 ? -30.728 -3.323  22.385  1.00 76.59  ? 1340 TRP A CH2   1 
ATOM   956  N  N     . ILE A 1 124 ? -37.335 -4.557  27.778  1.00 74.81  ? 1341 ILE A N     1 
ATOM   957  C  CA    . ILE A 1 124 ? -38.581 -5.234  28.077  1.00 75.15  ? 1341 ILE A CA    1 
ATOM   958  C  C     . ILE A 1 124 ? -39.194 -4.596  29.301  1.00 79.54  ? 1341 ILE A C     1 
ATOM   959  O  O     . ILE A 1 124 ? -38.836 -4.931  30.437  1.00 81.14  ? 1341 ILE A O     1 
ATOM   960  C  CB    . ILE A 1 124 ? -38.381 -6.743  28.242  1.00 75.73  ? 1341 ILE A CB    1 
ATOM   961  C  CG1   . ILE A 1 124 ? -37.452 -7.244  27.138  1.00 82.02  ? 1341 ILE A CG1   1 
ATOM   962  C  CG2   . ILE A 1 124 ? -39.695 -7.444  28.119  1.00 80.49  ? 1341 ILE A CG2   1 
ATOM   963  C  CD1   . ILE A 1 124 ? -36.669 -8.496  27.512  1.00 83.70  ? 1341 ILE A CD1   1 
ATOM   964  N  N     . GLN A 1 125 ? -40.058 -3.615  29.062  1.00 91.18  ? 1342 GLN A N     1 
ATOM   965  C  CA    . GLN A 1 125 ? -40.823 -2.964  30.106  1.00 104.04 ? 1342 GLN A CA    1 
ATOM   966  C  C     . GLN A 1 125 ? -42.255 -3.486  30.202  1.00 111.82 ? 1342 GLN A C     1 
ATOM   967  O  O     . GLN A 1 125 ? -42.936 -3.183  31.187  1.00 128.20 ? 1342 GLN A O     1 
ATOM   968  C  CB    . GLN A 1 125 ? -40.820 -1.442  29.882  1.00 101.11 ? 1342 GLN A CB    1 
ATOM   969  N  N     . SER A 1 126 ? -42.705 -4.297  29.240  1.00 101.87 ? 1343 SER A N     1 
ATOM   970  C  CA    . SER A 1 126 ? -44.059 -4.841  29.238  1.00 99.04  ? 1343 SER A CA    1 
ATOM   971  C  C     . SER A 1 126 ? -44.077 -6.196  28.544  1.00 86.51  ? 1343 SER A C     1 
ATOM   972  O  O     . SER A 1 126 ? -43.141 -6.568  27.826  1.00 70.99  ? 1343 SER A O     1 
ATOM   973  C  CB    . SER A 1 126 ? -45.038 -3.912  28.519  1.00 108.84 ? 1343 SER A CB    1 
ATOM   974  O  OG    . SER A 1 126 ? -44.981 -4.131  27.117  1.00 109.25 ? 1343 SER A OG    1 
ATOM   975  N  N     . TYR A 1 127 ? -45.186 -6.925  28.743  1.00 89.54  ? 1344 TYR A N     1 
ATOM   976  C  CA    . TYR A 1 127 ? -45.385 -8.191  28.031  1.00 88.52  ? 1344 TYR A CA    1 
ATOM   977  C  C     . TYR A 1 127 ? -45.338 -8.003  26.518  1.00 88.62  ? 1344 TYR A C     1 
ATOM   978  O  O     . TYR A 1 127 ? -44.889 -8.894  25.792  1.00 75.76  ? 1344 TYR A O     1 
ATOM   979  C  CB    . TYR A 1 127 ? -46.723 -8.825  28.431  1.00 80.81  ? 1344 TYR A CB    1 
ATOM   980  N  N     . ARG A 1 128 ? -45.785 -6.845  26.031  1.00 91.00  ? 1345 ARG A N     1 
ATOM   981  C  CA    . ARG A 1 128 ? -45.861 -6.591  24.599  1.00 80.98  ? 1345 ARG A CA    1 
ATOM   982  C  C     . ARG A 1 128 ? -44.497 -6.649  23.914  1.00 75.13  ? 1345 ARG A C     1 
ATOM   983  O  O     . ARG A 1 128 ? -44.428 -6.891  22.705  1.00 78.04  ? 1345 ARG A O     1 
ATOM   984  C  CB    . ARG A 1 128 ? -46.530 -5.231  24.376  1.00 88.01  ? 1345 ARG A CB    1 
ATOM   985  C  CG    . ARG A 1 128 ? -47.654 -4.903  25.388  1.00 90.74  ? 1345 ARG A CG    1 
ATOM   986  C  CD    . ARG A 1 128 ? -48.093 -3.420  25.373  1.00 86.24  ? 1345 ARG A CD    1 
ATOM   987  N  NE    . ARG A 1 128 ? -49.134 -3.137  26.368  1.00 78.30  ? 1345 ARG A NE    1 
ATOM   988  N  N     . ASP A 1 129 ? -43.408 -6.428  24.650  1.00 62.37  ? 1346 ASP A N     1 
ATOM   989  C  CA    . ASP A 1 129 ? -42.097 -6.345  24.017  1.00 74.29  ? 1346 ASP A CA    1 
ATOM   990  C  C     . ASP A 1 129 ? -41.488 -7.710  23.726  1.00 82.50  ? 1346 ASP A C     1 
ATOM   991  O  O     . ASP A 1 129 ? -40.368 -7.766  23.202  1.00 74.68  ? 1346 ASP A O     1 
ATOM   992  C  CB    . ASP A 1 129 ? -41.138 -5.500  24.888  1.00 78.05  ? 1346 ASP A CB    1 
ATOM   993  C  CG    . ASP A 1 129 ? -41.680 -4.070  25.163  1.00 87.40  ? 1346 ASP A CG    1 
ATOM   994  O  OD1   . ASP A 1 129 ? -41.922 -3.314  24.186  1.00 77.49  ? 1346 ASP A OD1   1 
ATOM   995  O  OD2   . ASP A 1 129 ? -41.870 -3.703  26.354  1.00 92.80  ? 1346 ASP A OD2   1 
ATOM   996  N  N     . LEU A 1 130 ? -42.225 -8.815  23.962  1.00 83.79  ? 1347 LEU A N     1 
ATOM   997  C  CA    . LEU A 1 130 ? -41.553 -10.094 23.759  1.00 78.23  ? 1347 LEU A CA    1 
ATOM   998  C  C     . LEU A 1 130 ? -42.100 -10.818 22.534  1.00 72.19  ? 1347 LEU A C     1 
ATOM   999  O  O     . LEU A 1 130 ? -43.263 -10.635 22.164  1.00 71.41  ? 1347 LEU A O     1 
ATOM   1000 C  CB    . LEU A 1 130 ? -41.728 -10.998 24.982  1.00 77.68  ? 1347 LEU A CB    1 
ATOM   1001 C  CG    . LEU A 1 130 ? -40.770 -10.850 26.161  1.00 87.81  ? 1347 LEU A CG    1 
ATOM   1002 C  CD1   . LEU A 1 130 ? -41.265 -11.665 27.340  1.00 88.54  ? 1347 LEU A CD1   1 
ATOM   1003 C  CD2   . LEU A 1 130 ? -39.388 -11.297 25.737  1.00 95.63  ? 1347 LEU A CD2   1 
ATOM   1004 N  N     . PRO A 1 131 ? -41.293 -11.661 21.884  1.00 64.97  ? 1348 PRO A N     1 
ATOM   1005 C  CA    . PRO A 1 131 ? -39.938 -12.072 22.267  1.00 66.20  ? 1348 PRO A CA    1 
ATOM   1006 C  C     . PRO A 1 131 ? -38.891 -11.164 21.698  1.00 67.80  ? 1348 PRO A C     1 
ATOM   1007 O  O     . PRO A 1 131 ? -39.192 -10.439 20.761  1.00 76.31  ? 1348 PRO A O     1 
ATOM   1008 C  CB    . PRO A 1 131 ? -39.812 -13.454 21.641  1.00 71.41  ? 1348 PRO A CB    1 
ATOM   1009 C  CG    . PRO A 1 131 ? -40.625 -13.344 20.394  1.00 68.40  ? 1348 PRO A CG    1 
ATOM   1010 C  CD    . PRO A 1 131 ? -41.757 -12.372 20.682  1.00 56.71  ? 1348 PRO A CD    1 
ATOM   1011 N  N     . ILE A 1 132 ? -37.672 -11.222 22.225  1.00 66.49  ? 1349 ILE A N     1 
ATOM   1012 C  CA    . ILE A 1 132 ? -36.526 -10.539 21.628  1.00 76.58  ? 1349 ILE A CA    1 
ATOM   1013 C  C     . ILE A 1 132 ? -35.568 -11.583 21.060  1.00 75.35  ? 1349 ILE A C     1 
ATOM   1014 O  O     . ILE A 1 132 ? -35.042 -12.432 21.791  1.00 73.10  ? 1349 ILE A O     1 
ATOM   1015 C  CB    . ILE A 1 132 ? -35.826 -9.606  22.626  1.00 80.10  ? 1349 ILE A CB    1 
ATOM   1016 C  CG1   . ILE A 1 132 ? -36.802 -8.506  23.055  1.00 76.98  ? 1349 ILE A CG1   1 
ATOM   1017 C  CG2   . ILE A 1 132 ? -34.528 -9.036  22.016  1.00 78.19  ? 1349 ILE A CG2   1 
ATOM   1018 C  CD1   . ILE A 1 132 ? -36.168 -7.289  23.698  1.00 70.34  ? 1349 ILE A CD1   1 
ATOM   1019 N  N     . ARG A 1 133 ? -35.343 -11.510 19.753  1.00 69.97  ? 1350 ARG A N     1 
ATOM   1020 C  CA    . ARG A 1 133 ? -34.495 -12.442 19.026  1.00 62.50  ? 1350 ARG A CA    1 
ATOM   1021 C  C     . ARG A 1 133 ? -33.465 -11.622 18.264  1.00 66.24  ? 1350 ARG A C     1 
ATOM   1022 O  O     . ARG A 1 133 ? -33.738 -11.199 17.133  1.00 54.80  ? 1350 ARG A O     1 
ATOM   1023 C  CB    . ARG A 1 133 ? -35.311 -13.289 18.067  1.00 69.67  ? 1350 ARG A CB    1 
ATOM   1024 C  CG    . ARG A 1 133 ? -36.716 -13.578 18.549  1.00 78.73  ? 1350 ARG A CG    1 
ATOM   1025 C  CD    . ARG A 1 133 ? -36.847 -15.011 19.005  1.00 81.79  ? 1350 ARG A CD    1 
ATOM   1026 N  NE    . ARG A 1 133 ? -36.424 -15.975 17.986  1.00 85.28  ? 1350 ARG A NE    1 
ATOM   1027 C  CZ    . ARG A 1 133 ? -37.108 -16.266 16.878  1.00 88.36  ? 1350 ARG A CZ    1 
ATOM   1028 N  NH1   . ARG A 1 133 ? -38.272 -15.668 16.615  1.00 89.18  ? 1350 ARG A NH1   1 
ATOM   1029 N  NH2   . ARG A 1 133 ? -36.622 -17.164 16.025  1.00 83.70  ? 1350 ARG A NH2   1 
ATOM   1030 N  N     . LEU A 1 134 ? -32.266 -11.462 18.850  1.00 79.41  ? 1351 LEU A N     1 
ATOM   1031 C  CA    . LEU A 1 134 ? -31.225 -10.609 18.290  1.00 68.36  ? 1351 LEU A CA    1 
ATOM   1032 C  C     . LEU A 1 134 ? -29.967 -11.430 18.050  1.00 71.01  ? 1351 LEU A C     1 
ATOM   1033 O  O     . LEU A 1 134 ? -29.645 -12.335 18.825  1.00 74.85  ? 1351 LEU A O     1 
ATOM   1034 C  CB    . LEU A 1 134 ? -30.906 -9.454  19.223  1.00 58.20  ? 1351 LEU A CB    1 
ATOM   1035 C  CG    . LEU A 1 134 ? -31.989 -8.383  19.388  1.00 63.43  ? 1351 LEU A CG    1 
ATOM   1036 C  CD1   . LEU A 1 134 ? -31.639 -7.404  20.497  1.00 46.10  ? 1351 LEU A CD1   1 
ATOM   1037 C  CD2   . LEU A 1 134 ? -32.165 -7.654  18.076  1.00 62.77  ? 1351 LEU A CD2   1 
ATOM   1038 N  N     . ASN A 1 135 ? -29.281 -11.137 16.945  1.00 73.48  ? 1352 ASN A N     1 
ATOM   1039 C  CA    . ASN A 1 135 ? -28.075 -11.851 16.548  1.00 73.97  ? 1352 ASN A CA    1 
ATOM   1040 C  C     . ASN A 1 135 ? -26.957 -10.876 16.200  1.00 72.21  ? 1352 ASN A C     1 
ATOM   1041 O  O     . ASN A 1 135 ? -27.203 -9.857  15.553  1.00 74.19  ? 1352 ASN A O     1 
ATOM   1042 C  CB    . ASN A 1 135 ? -28.377 -12.745 15.326  1.00 72.56  ? 1352 ASN A CB    1 
ATOM   1043 C  CG    . ASN A 1 135 ? -27.117 -13.242 14.628  1.00 69.96  ? 1352 ASN A CG    1 
ATOM   1044 O  OD1   . ASN A 1 135 ? -26.259 -13.847 15.255  1.00 65.86  ? 1352 ASN A OD1   1 
ATOM   1045 N  ND2   . ASN A 1 135 ? -27.015 -12.997 13.322  1.00 76.21  ? 1352 ASN A ND2   1 
ATOM   1046 N  N     . GLN A 1 136 ? -25.717 -11.197 16.578  1.00 78.94  ? 1353 GLN A N     1 
ATOM   1047 C  CA    . GLN A 1 136 ? -24.586 -10.436 16.058  1.00 78.40  ? 1353 GLN A CA    1 
ATOM   1048 C  C     . GLN A 1 136 ? -23.571 -11.352 15.404  1.00 66.92  ? 1353 GLN A C     1 
ATOM   1049 O  O     . GLN A 1 136 ? -23.236 -12.425 15.912  1.00 71.42  ? 1353 GLN A O     1 
ATOM   1050 C  CB    . GLN A 1 136 ? -23.848 -9.552  17.081  1.00 78.57  ? 1353 GLN A CB    1 
ATOM   1051 C  CG    . GLN A 1 136 ? -23.922 -9.930  18.505  1.00 81.93  ? 1353 GLN A CG    1 
ATOM   1052 C  CD    . GLN A 1 136 ? -23.251 -8.894  19.359  1.00 79.26  ? 1353 GLN A CD    1 
ATOM   1053 O  OE1   . GLN A 1 136 ? -22.486 -8.085  18.855  1.00 89.95  ? 1353 GLN A OE1   1 
ATOM   1054 N  NE2   . GLN A 1 136 ? -23.507 -8.925  20.657  1.00 80.96  ? 1353 GLN A NE2   1 
ATOM   1055 N  N     . TRP A 1 137 ? -23.099 -10.888 14.270  1.00 57.97  ? 1354 TRP A N     1 
ATOM   1056 C  CA    . TRP A 1 137 ? -21.948 -11.424 13.589  1.00 49.14  ? 1354 TRP A CA    1 
ATOM   1057 C  C     . TRP A 1 137 ? -20.775 -10.562 14.034  1.00 62.04  ? 1354 TRP A C     1 
ATOM   1058 O  O     . TRP A 1 137 ? -20.658 -9.402  13.619  1.00 64.16  ? 1354 TRP A O     1 
ATOM   1059 C  CB    . TRP A 1 137 ? -22.150 -11.343 12.085  1.00 48.00  ? 1354 TRP A CB    1 
ATOM   1060 C  CG    . TRP A 1 137 ? -23.148 -12.282 11.551  1.00 60.20  ? 1354 TRP A CG    1 
ATOM   1061 C  CD1   . TRP A 1 137 ? -24.425 -11.984 11.151  1.00 74.84  ? 1354 TRP A CD1   1 
ATOM   1062 C  CD2   . TRP A 1 137 ? -22.972 -13.687 11.320  1.00 69.50  ? 1354 TRP A CD2   1 
ATOM   1063 N  NE1   . TRP A 1 137 ? -25.055 -13.119 10.695  1.00 82.19  ? 1354 TRP A NE1   1 
ATOM   1064 C  CE2   . TRP A 1 137 ? -24.189 -14.179 10.794  1.00 77.46  ? 1354 TRP A CE2   1 
ATOM   1065 C  CE3   . TRP A 1 137 ? -21.910 -14.576 11.513  1.00 72.35  ? 1354 TRP A CE3   1 
ATOM   1066 C  CZ2   . TRP A 1 137 ? -24.370 -15.521 10.454  1.00 81.56  ? 1354 TRP A CZ2   1 
ATOM   1067 C  CZ3   . TRP A 1 137 ? -22.089 -15.923 11.176  1.00 74.15  ? 1354 TRP A CZ3   1 
ATOM   1068 C  CH2   . TRP A 1 137 ? -23.310 -16.377 10.657  1.00 81.66  ? 1354 TRP A CH2   1 
ATOM   1069 N  N     . ASN A 1 138 ? -19.921 -11.102 14.903  1.00 58.57  ? 1355 ASN A N     1 
ATOM   1070 C  CA    . ASN A 1 138 ? -18.876 -10.265 15.447  1.00 52.39  ? 1355 ASN A CA    1 
ATOM   1071 C  C     . ASN A 1 138 ? -17.644 -11.099 15.732  1.00 71.13  ? 1355 ASN A C     1 
ATOM   1072 O  O     . ASN A 1 138 ? -17.627 -12.317 15.548  1.00 76.76  ? 1355 ASN A O     1 
ATOM   1073 C  CB    . ASN A 1 138 ? -19.358 -9.537  16.701  1.00 47.76  ? 1355 ASN A CB    1 
ATOM   1074 C  CG    . ASN A 1 138 ? -19.670 -10.471 17.839  1.00 56.46  ? 1355 ASN A CG    1 
ATOM   1075 O  OD1   . ASN A 1 138 ? -19.095 -11.541 17.941  1.00 71.56  ? 1355 ASN A OD1   1 
ATOM   1076 N  ND2   . ASN A 1 138 ? -20.568 -10.059 18.726  1.00 49.66  ? 1355 ASN A ND2   1 
ATOM   1077 N  N     . ASN A 1 139 ? -16.616 -10.408 16.206  1.00 75.83  ? 1356 ASN A N     1 
ATOM   1078 C  CA    . ASN A 1 139 ? -15.335 -10.983 16.566  1.00 65.67  ? 1356 ASN A CA    1 
ATOM   1079 C  C     . ASN A 1 139 ? -15.198 -10.964 18.075  1.00 65.37  ? 1356 ASN A C     1 
ATOM   1080 O  O     . ASN A 1 139 ? -15.641 -10.028 18.741  1.00 67.40  ? 1356 ASN A O     1 
ATOM   1081 C  CB    . ASN A 1 139 ? -14.185 -10.217 15.921  1.00 70.70  ? 1356 ASN A CB    1 
ATOM   1082 C  CG    . ASN A 1 139 ? -14.287 -8.707  16.139  1.00 71.61  ? 1356 ASN A CG    1 
ATOM   1083 O  OD1   . ASN A 1 139 ? -15.374 -8.108  16.098  1.00 78.36  ? 1356 ASN A OD1   1 
ATOM   1084 N  ND2   . ASN A 1 139 ? -13.146 -8.092  16.379  1.00 52.50  ? 1356 ASN A ND2   1 
ATOM   1085 N  N     . VAL A 1 140 ? -14.624 -12.020 18.624  1.00 76.60  ? 1357 VAL A N     1 
ATOM   1086 C  CA    . VAL A 1 140 ? -14.310 -12.013 20.040  1.00 78.77  ? 1357 VAL A CA    1 
ATOM   1087 C  C     . VAL A 1 140 ? -12.866 -12.467 20.224  1.00 72.61  ? 1357 VAL A C     1 
ATOM   1088 O  O     . VAL A 1 140 ? -12.217 -13.000 19.312  1.00 70.30  ? 1357 VAL A O     1 
ATOM   1089 C  CB    . VAL A 1 140 ? -15.294 -12.868 20.875  1.00 81.65  ? 1357 VAL A CB    1 
ATOM   1090 C  CG1   . VAL A 1 140 ? -16.758 -12.566 20.485  1.00 82.72  ? 1357 VAL A CG1   1 
ATOM   1091 C  CG2   . VAL A 1 140 ? -15.005 -14.322 20.729  1.00 69.99  ? 1357 VAL A CG2   1 
ATOM   1092 N  N     . VAL A 1 141 ? -12.359 -12.192 21.418  1.00 66.97  ? 1358 VAL A N     1 
ATOM   1093 C  CA    . VAL A 1 141 ? -11.007 -12.538 21.801  1.00 67.16  ? 1358 VAL A CA    1 
ATOM   1094 C  C     . VAL A 1 141 ? -11.063 -13.291 23.115  1.00 65.69  ? 1358 VAL A C     1 
ATOM   1095 O  O     . VAL A 1 141 ? -11.690 -12.834 24.075  1.00 67.99  ? 1358 VAL A O     1 
ATOM   1096 C  CB    . VAL A 1 141 ? -10.105 -11.288 21.931  1.00 70.20  ? 1358 VAL A CB    1 
ATOM   1097 C  CG1   . VAL A 1 141 ? -8.681  -11.690 22.394  1.00 66.08  ? 1358 VAL A CG1   1 
ATOM   1098 C  CG2   . VAL A 1 141 ? -10.075 -10.482 20.600  1.00 59.22  ? 1358 VAL A CG2   1 
ATOM   1099 N  N     . ARG A 1 142 ? -10.430 -14.459 23.144  1.00 68.04  ? 1359 ARG A N     1 
ATOM   1100 C  CA    . ARG A 1 142 ? -10.206 -15.210 24.370  1.00 74.44  ? 1359 ARG A CA    1 
ATOM   1101 C  C     . ARG A 1 142 ? -8.720  -15.544 24.444  1.00 73.91  ? 1359 ARG A C     1 
ATOM   1102 O  O     . ARG A 1 142 ? -8.183  -16.205 23.549  1.00 71.31  ? 1359 ARG A O     1 
ATOM   1103 C  CB    . ARG A 1 142 ? -11.083 -16.463 24.428  1.00 81.95  ? 1359 ARG A CB    1 
ATOM   1104 C  CG    . ARG A 1 142 ? -12.596 -16.150 24.431  1.00 88.19  ? 1359 ARG A CG    1 
ATOM   1105 C  CD    . ARG A 1 142 ? -13.429 -17.274 23.826  1.00 86.42  ? 1359 ARG A CD    1 
ATOM   1106 N  NE    . ARG A 1 142 ? -14.863 -17.111 24.035  1.00 83.81  ? 1359 ARG A NE    1 
ATOM   1107 C  CZ    . ARG A 1 142 ? -15.748 -18.087 23.856  1.00 87.51  ? 1359 ARG A CZ    1 
ATOM   1108 N  NH1   . ARG A 1 142 ? -15.337 -19.283 23.482  1.00 73.93  ? 1359 ARG A NH1   1 
ATOM   1109 N  NH2   . ARG A 1 142 ? -17.043 -17.870 24.040  1.00 99.39  ? 1359 ARG A NH2   1 
ATOM   1110 N  N     . TRP A 1 143 ? -8.043  -15.006 25.459  1.00 74.85  ? 1360 TRP A N     1 
ATOM   1111 C  CA    . TRP A 1 143 ? -6.600  -15.163 25.632  1.00 82.60  ? 1360 TRP A CA    1 
ATOM   1112 C  C     . TRP A 1 143 ? -6.327  -16.546 26.212  1.00 88.68  ? 1360 TRP A C     1 
ATOM   1113 O  O     . TRP A 1 143 ? -6.049  -16.715 27.401  1.00 88.56  ? 1360 TRP A O     1 
ATOM   1114 C  CB    . TRP A 1 143 ? -6.025  -14.058 26.503  1.00 94.20  ? 1360 TRP A CB    1 
ATOM   1115 C  CG    . TRP A 1 143 ? -4.674  -13.665 26.034  1.00 104.33 ? 1360 TRP A CG    1 
ATOM   1116 C  CD1   . TRP A 1 143 ? -3.493  -13.847 26.689  1.00 111.56 ? 1360 TRP A CD1   1 
ATOM   1117 C  CD2   . TRP A 1 143 ? -4.347  -13.072 24.776  1.00 98.84  ? 1360 TRP A CD2   1 
ATOM   1118 N  NE1   . TRP A 1 143 ? -2.451  -13.379 25.928  1.00 106.58 ? 1360 TRP A NE1   1 
ATOM   1119 C  CE2   . TRP A 1 143 ? -2.948  -12.901 24.747  1.00 97.16  ? 1360 TRP A CE2   1 
ATOM   1120 C  CE3   . TRP A 1 143 ? -5.100  -12.663 23.674  1.00 92.23  ? 1360 TRP A CE3   1 
ATOM   1121 C  CZ2   . TRP A 1 143 ? -2.290  -12.344 23.661  1.00 92.38  ? 1360 TRP A CZ2   1 
ATOM   1122 C  CZ3   . TRP A 1 143 ? -4.438  -12.105 22.593  1.00 91.66  ? 1360 TRP A CZ3   1 
ATOM   1123 C  CH2   . TRP A 1 143 ? -3.054  -11.949 22.596  1.00 93.21  ? 1360 TRP A CH2   1 
ATOM   1124 N  N     . GLU A 1 144 ? -6.466  -17.551 25.349  1.00 99.87  ? 1361 GLU A N     1 
ATOM   1125 C  CA    . GLU A 1 144 ? -6.458  -18.949 25.770  1.00 114.47 ? 1361 GLU A CA    1 
ATOM   1126 C  C     . GLU A 1 144 ? -5.033  -19.465 25.918  1.00 126.91 ? 1361 GLU A C     1 
ATOM   1127 O  O     . GLU A 1 144 ? -4.275  -19.507 24.943  1.00 131.11 ? 1361 GLU A O     1 
ATOM   1128 C  CB    . GLU A 1 144 ? -7.224  -19.804 24.762  1.00 110.63 ? 1361 GLU A CB    1 
ATOM   1129 C  CG    . GLU A 1 144 ? -8.730  -19.828 24.974  1.00 109.63 ? 1361 GLU A CG    1 
ATOM   1130 C  CD    . GLU A 1 144 ? -9.435  -20.714 23.969  1.00 117.42 ? 1361 GLU A CD    1 
ATOM   1131 O  OE1   . GLU A 1 144 ? -10.644 -20.483 23.714  1.00 114.78 ? 1361 GLU A OE1   1 
ATOM   1132 O  OE2   . GLU A 1 144 ? -8.771  -21.637 23.435  1.00 124.19 ? 1361 GLU A OE2   1 
ATOM   1133 N  N     . PHE A 1 145 ? -4.681  -19.877 27.139  1.00 133.36 ? 1362 PHE A N     1 
ATOM   1134 C  CA    . PHE A 1 145 ? -3.366  -20.447 27.436  1.00 136.43 ? 1362 PHE A CA    1 
ATOM   1135 C  C     . PHE A 1 145 ? -3.333  -21.914 26.993  1.00 136.02 ? 1362 PHE A C     1 
ATOM   1136 O  O     . PHE A 1 145 ? -3.342  -22.851 27.795  1.00 133.20 ? 1362 PHE A O     1 
ATOM   1137 C  CB    . PHE A 1 145 ? -3.048  -20.295 28.918  1.00 134.87 ? 1362 PHE A CB    1 
ATOM   1138 N  N     . LYS A 1 146 ? -3.321  -22.098 25.670  1.00 133.34 ? 1363 LYS A N     1 
ATOM   1139 C  CA    . LYS A 1 146 ? -3.044  -23.386 25.050  1.00 127.19 ? 1363 LYS A CA    1 
ATOM   1140 C  C     . LYS A 1 146 ? -2.140  -23.142 23.844  1.00 129.99 ? 1363 LYS A C     1 
ATOM   1141 O  O     . LYS A 1 146 ? -1.731  -22.010 23.571  1.00 131.48 ? 1363 LYS A O     1 
ATOM   1142 C  CB    . LYS A 1 146 ? -4.341  -24.105 24.661  1.00 116.96 ? 1363 LYS A CB    1 
ATOM   1143 N  N     . HIS A 1 147 ? -1.880  -24.197 23.073  1.00 128.18 ? 1364 HIS A N     1 
ATOM   1144 C  CA    . HIS A 1 147 ? -1.039  -24.076 21.886  1.00 125.39 ? 1364 HIS A CA    1 
ATOM   1145 C  C     . HIS A 1 147 ? -1.901  -23.784 20.668  1.00 114.85 ? 1364 HIS A C     1 
ATOM   1146 O  O     . HIS A 1 147 ? -2.747  -24.616 20.309  1.00 116.93 ? 1364 HIS A O     1 
ATOM   1147 C  CB    . HIS A 1 147 ? -0.211  -25.334 21.668  1.00 137.79 ? 1364 HIS A CB    1 
ATOM   1148 C  CG    . HIS A 1 147 ? 0.715   -25.251 20.493  1.00 143.93 ? 1364 HIS A CG    1 
ATOM   1149 N  ND1   . HIS A 1 147 ? 0.280   -25.409 19.195  1.00 144.30 ? 1364 HIS A ND1   1 
ATOM   1150 C  CD2   . HIS A 1 147 ? 2.049   -25.026 20.419  1.00 145.84 ? 1364 HIS A CD2   1 
ATOM   1151 C  CE1   . HIS A 1 147 ? 1.306   -25.289 18.372  1.00 144.65 ? 1364 HIS A CE1   1 
ATOM   1152 N  NE2   . HIS A 1 147 ? 2.391   -25.055 19.088  1.00 145.30 ? 1364 HIS A NE2   1 
ATOM   1153 N  N     . PRO A 1 148 ? -1.753  -22.626 20.036  1.00 100.68 ? 1365 PRO A N     1 
ATOM   1154 C  CA    . PRO A 1 148 ? -2.722  -22.174 19.032  1.00 96.65  ? 1365 PRO A CA    1 
ATOM   1155 C  C     . PRO A 1 148 ? -2.551  -22.820 17.663  1.00 96.02  ? 1365 PRO A C     1 
ATOM   1156 O  O     . PRO A 1 148 ? -1.488  -23.332 17.302  1.00 90.75  ? 1365 PRO A O     1 
ATOM   1157 C  CB    . PRO A 1 148 ? -2.444  -20.674 18.947  1.00 85.64  ? 1365 PRO A CB    1 
ATOM   1158 C  CG    . PRO A 1 148 ? -0.978  -20.585 19.198  1.00 87.80  ? 1365 PRO A CG    1 
ATOM   1159 C  CD    . PRO A 1 148 ? -0.642  -21.675 20.197  1.00 95.32  ? 1365 PRO A CD    1 
ATOM   1160 N  N     . GLN A 1 149 ? -3.655  -22.788 16.902  1.00 92.55  ? 1366 GLN A N     1 
ATOM   1161 C  CA    . GLN A 1 149 ? -3.716  -23.338 15.554  1.00 80.22  ? 1366 GLN A CA    1 
ATOM   1162 C  C     . GLN A 1 149 ? -4.773  -22.639 14.711  1.00 71.46  ? 1366 GLN A C     1 
ATOM   1163 O  O     . GLN A 1 149 ? -5.865  -22.355 15.210  1.00 63.72  ? 1366 GLN A O     1 
ATOM   1164 C  CB    . GLN A 1 149 ? -3.991  -24.841 15.592  1.00 77.91  ? 1366 GLN A CB    1 
ATOM   1165 C  CG    . GLN A 1 149 ? -3.495  -25.587 14.370  1.00 79.22  ? 1366 GLN A CG    1 
ATOM   1166 C  CD    . GLN A 1 149 ? -3.732  -27.073 14.480  1.00 93.39  ? 1366 GLN A CD    1 
ATOM   1167 O  OE1   . GLN A 1 149 ? -4.353  -27.536 15.437  1.00 99.70  ? 1366 GLN A OE1   1 
ATOM   1168 N  NE2   . GLN A 1 149 ? -3.221  -27.836 13.514  1.00 95.32  ? 1366 GLN A NE2   1 
ATOM   1169 N  N     . PRO A 1 150 ? -4.491  -22.435 13.404  1.00 73.60  ? 1367 PRO A N     1 
ATOM   1170 C  CA    . PRO A 1 150 ? -5.254  -21.508 12.563  1.00 74.67  ? 1367 PRO A CA    1 
ATOM   1171 C  C     . PRO A 1 150 ? -6.763  -21.444 12.626  1.00 94.34  ? 1367 PRO A C     1 
ATOM   1172 O  O     . PRO A 1 150 ? -7.294  -20.327 12.580  1.00 110.94 ? 1367 PRO A O     1 
ATOM   1173 C  CB    . PRO A 1 150 ? -4.801  -21.916 11.162  1.00 69.92  ? 1367 PRO A CB    1 
ATOM   1174 C  CG    . PRO A 1 150 ? -3.320  -22.267 11.403  1.00 67.58  ? 1367 PRO A CG    1 
ATOM   1175 C  CD    . PRO A 1 150 ? -3.130  -22.550 12.870  1.00 70.75  ? 1367 PRO A CD    1 
ATOM   1176 N  N     . PHE A 1 151 ? -7.498  -22.532 12.642  1.00 83.99  ? 1368 PHE A N     1 
ATOM   1177 C  CA    . PHE A 1 151 ? -8.934  -22.323 12.765  1.00 75.69  ? 1368 PHE A CA    1 
ATOM   1178 C  C     . PHE A 1 151 ? -9.494  -22.899 14.052  1.00 79.59  ? 1368 PHE A C     1 
ATOM   1179 O  O     . PHE A 1 151 ? -10.602 -22.520 14.444  1.00 77.06  ? 1368 PHE A O     1 
ATOM   1180 C  CB    . PHE A 1 151 ? -9.690  -22.916 11.557  1.00 67.05  ? 1368 PHE A CB    1 
ATOM   1181 C  CG    . PHE A 1 151 ? -9.427  -22.206 10.239  1.00 68.74  ? 1368 PHE A CG    1 
ATOM   1182 C  CD1   . PHE A 1 151 ? -10.104 -21.033 9.905   1.00 73.37  ? 1368 PHE A CD1   1 
ATOM   1183 C  CD2   . PHE A 1 151 ? -8.541  -22.734 9.313   1.00 78.10  ? 1368 PHE A CD2   1 
ATOM   1184 C  CE1   . PHE A 1 151 ? -9.886  -20.384 8.674   1.00 66.69  ? 1368 PHE A CE1   1 
ATOM   1185 C  CE2   . PHE A 1 151 ? -8.308  -22.088 8.089   1.00 78.63  ? 1368 PHE A CE2   1 
ATOM   1186 C  CZ    . PHE A 1 151 ? -8.980  -20.911 7.773   1.00 68.10  ? 1368 PHE A CZ    1 
ATOM   1187 N  N     . LEU A 1 152 ? -8.721  -23.717 14.768  1.00 77.74  ? 1369 LEU A N     1 
ATOM   1188 C  CA    . LEU A 1 152 ? -9.271  -24.554 15.823  1.00 73.17  ? 1369 LEU A CA    1 
ATOM   1189 C  C     . LEU A 1 152 ? -9.092  -23.985 17.224  1.00 72.87  ? 1369 LEU A C     1 
ATOM   1190 O  O     . LEU A 1 152 ? -10.017 -24.068 18.036  1.00 86.29  ? 1369 LEU A O     1 
ATOM   1191 C  CB    . LEU A 1 152 ? -8.653  -25.951 15.716  1.00 73.81  ? 1369 LEU A CB    1 
ATOM   1192 C  CG    . LEU A 1 152 ? -8.871  -26.510 14.297  1.00 63.13  ? 1369 LEU A CG    1 
ATOM   1193 C  CD1   . LEU A 1 152 ? -7.852  -27.583 13.940  1.00 44.69  ? 1369 LEU A CD1   1 
ATOM   1194 C  CD2   . LEU A 1 152 ? -10.251 -27.052 14.148  1.00 43.11  ? 1369 LEU A CD2   1 
ATOM   1195 N  N     . ARG A 1 153 ? -7.925  -23.433 17.540  1.00 71.94  ? 1370 ARG A N     1 
ATOM   1196 C  CA    . ARG A 1 153 ? -7.689  -22.695 18.785  1.00 72.78  ? 1370 ARG A CA    1 
ATOM   1197 C  C     . ARG A 1 153 ? -6.984  -21.398 18.378  1.00 81.84  ? 1370 ARG A C     1 
ATOM   1198 O  O     . ARG A 1 153 ? -5.753  -21.356 18.233  1.00 75.90  ? 1370 ARG A O     1 
ATOM   1199 C  CB    . ARG A 1 153 ? -6.870  -23.501 19.802  1.00 71.58  ? 1370 ARG A CB    1 
ATOM   1200 C  CG    . ARG A 1 153 ? -7.128  -23.121 21.270  1.00 67.85  ? 1370 ARG A CG    1 
ATOM   1201 N  N     . THR A 1 154 ? -7.782  -20.354 18.145  1.00 82.48  ? 1371 THR A N     1 
ATOM   1202 C  CA    . THR A 1 154 ? -7.299  -19.009 17.844  1.00 75.98  ? 1371 THR A CA    1 
ATOM   1203 C  C     . THR A 1 154 ? -7.749  -18.034 18.920  1.00 77.10  ? 1371 THR A C     1 
ATOM   1204 O  O     . THR A 1 154 ? -8.819  -18.203 19.510  1.00 87.82  ? 1371 THR A O     1 
ATOM   1205 C  CB    . THR A 1 154 ? -7.810  -18.518 16.512  1.00 66.89  ? 1371 THR A CB    1 
ATOM   1206 O  OG1   . THR A 1 154 ? -9.197  -18.185 16.643  1.00 65.73  ? 1371 THR A OG1   1 
ATOM   1207 C  CG2   . THR A 1 154 ? -7.640  -19.591 15.462  1.00 60.30  ? 1371 THR A CG2   1 
ATOM   1208 N  N     . ARG A 1 155 ? -6.931  -17.002 19.172  1.00 73.65  ? 1372 ARG A N     1 
ATOM   1209 C  CA    . ARG A 1 155 ? -7.267  -16.078 20.252  1.00 71.62  ? 1372 ARG A CA    1 
ATOM   1210 C  C     . ARG A 1 155 ? -8.303  -15.052 19.819  1.00 76.38  ? 1372 ARG A C     1 
ATOM   1211 O  O     . ARG A 1 155 ? -9.211  -14.735 20.589  1.00 84.28  ? 1372 ARG A O     1 
ATOM   1212 C  CB    . ARG A 1 155 ? -6.012  -15.418 20.801  1.00 74.25  ? 1372 ARG A CB    1 
ATOM   1213 C  CG    . ARG A 1 155 ? -5.169  -16.408 21.594  1.00 93.29  ? 1372 ARG A CG    1 
ATOM   1214 C  CD    . ARG A 1 155 ? -4.319  -15.735 22.649  1.00 110.19 ? 1372 ARG A CD    1 
ATOM   1215 N  NE    . ARG A 1 155 ? -2.943  -15.526 22.205  1.00 116.22 ? 1372 ARG A NE    1 
ATOM   1216 C  CZ    . ARG A 1 155 ? -1.924  -16.291 22.577  1.00 118.04 ? 1372 ARG A CZ    1 
ATOM   1217 N  NH1   . ARG A 1 155 ? -2.132  -17.314 23.398  1.00 117.63 ? 1372 ARG A NH1   1 
ATOM   1218 N  NH2   . ARG A 1 155 ? -0.703  -16.036 22.127  1.00 118.93 ? 1372 ARG A NH2   1 
ATOM   1219 N  N     . GLU A 1 156 ? -8.197  -14.513 18.613  1.00 69.60  ? 1373 GLU A N     1 
ATOM   1220 C  CA    . GLU A 1 156 ? -9.317  -13.786 18.041  1.00 77.67  ? 1373 GLU A CA    1 
ATOM   1221 C  C     . GLU A 1 156 ? -9.966  -14.651 16.973  1.00 82.56  ? 1373 GLU A C     1 
ATOM   1222 O  O     . GLU A 1 156 ? -9.270  -15.280 16.168  1.00 90.90  ? 1373 GLU A O     1 
ATOM   1223 C  CB    . GLU A 1 156 ? -8.912  -12.443 17.433  1.00 73.49  ? 1373 GLU A CB    1 
ATOM   1224 C  CG    . GLU A 1 156 ? -10.094 -11.733 16.716  1.00 69.28  ? 1373 GLU A CG    1 
ATOM   1225 C  CD    . GLU A 1 156 ? -9.632  -10.814 15.597  1.00 71.33  ? 1373 GLU A CD    1 
ATOM   1226 O  OE1   . GLU A 1 156 ? -8.414  -10.763 15.328  1.00 72.13  ? 1373 GLU A OE1   1 
ATOM   1227 O  OE2   . GLU A 1 156 ? -10.481 -10.136 14.985  1.00 69.97  ? 1373 GLU A OE2   1 
ATOM   1228 N  N     . PHE A 1 157 ? -11.297 -14.693 16.983  1.00 70.75  ? 1374 PHE A N     1 
ATOM   1229 C  CA    . PHE A 1 157 ? -12.023 -15.395 15.933  1.00 64.91  ? 1374 PHE A CA    1 
ATOM   1230 C  C     . PHE A 1 157 ? -13.366 -14.731 15.698  1.00 67.49  ? 1374 PHE A C     1 
ATOM   1231 O  O     . PHE A 1 157 ? -13.899 -14.018 16.556  1.00 68.36  ? 1374 PHE A O     1 
ATOM   1232 C  CB    . PHE A 1 157 ? -12.268 -16.870 16.268  1.00 62.73  ? 1374 PHE A CB    1 
ATOM   1233 C  CG    . PHE A 1 157 ? -13.148 -17.080 17.475  1.00 53.75  ? 1374 PHE A CG    1 
ATOM   1234 C  CD1   . PHE A 1 157 ? -14.521 -17.172 17.348  1.00 57.96  ? 1374 PHE A CD1   1 
ATOM   1235 C  CD2   . PHE A 1 157 ? -12.590 -17.181 18.746  1.00 59.17  ? 1374 PHE A CD2   1 
ATOM   1236 C  CE1   . PHE A 1 157 ? -15.330 -17.359 18.468  1.00 62.63  ? 1374 PHE A CE1   1 
ATOM   1237 C  CE2   . PHE A 1 157 ? -13.394 -17.376 19.872  1.00 60.53  ? 1374 PHE A CE2   1 
ATOM   1238 C  CZ    . PHE A 1 157 ? -14.764 -17.470 19.728  1.00 62.06  ? 1374 PHE A CZ    1 
ATOM   1239 N  N     . LEU A 1 158 ? -13.930 -15.037 14.532  1.00 66.36  ? 1375 LEU A N     1 
ATOM   1240 C  CA    . LEU A 1 158 ? -15.264 -14.603 14.151  1.00 63.92  ? 1375 LEU A CA    1 
ATOM   1241 C  C     . LEU A 1 158 ? -16.299 -15.651 14.541  1.00 72.37  ? 1375 LEU A C     1 
ATOM   1242 O  O     . LEU A 1 158 ? -16.032 -16.856 14.498  1.00 74.52  ? 1375 LEU A O     1 
ATOM   1243 C  CB    . LEU A 1 158 ? -15.345 -14.381 12.648  1.00 53.26  ? 1375 LEU A CB    1 
ATOM   1244 C  CG    . LEU A 1 158 ? -14.210 -13.629 11.999  1.00 57.91  ? 1375 LEU A CG    1 
ATOM   1245 C  CD1   . LEU A 1 158 ? -14.593 -13.490 10.546  1.00 51.17  ? 1375 LEU A CD1   1 
ATOM   1246 C  CD2   . LEU A 1 158 ? -13.977 -12.254 12.687  1.00 63.21  ? 1375 LEU A CD2   1 
ATOM   1247 N  N     . TRP A 1 159 ? -17.487 -15.188 14.915  1.00 70.56  ? 1376 TRP A N     1 
ATOM   1248 C  CA    . TRP A 1 159 ? -18.609 -16.088 15.095  1.00 58.22  ? 1376 TRP A CA    1 
ATOM   1249 C  C     . TRP A 1 159 ? -19.878 -15.295 14.904  1.00 58.73  ? 1376 TRP A C     1 
ATOM   1250 O  O     . TRP A 1 159 ? -19.853 -14.092 14.633  1.00 63.43  ? 1376 TRP A O     1 
ATOM   1251 C  CB    . TRP A 1 159 ? -18.604 -16.766 16.479  1.00 57.61  ? 1376 TRP A CB    1 
ATOM   1252 C  CG    . TRP A 1 159 ? -18.906 -15.868 17.657  1.00 54.81  ? 1376 TRP A CG    1 
ATOM   1253 C  CD1   . TRP A 1 159 ? -19.043 -14.512 17.639  1.00 59.12  ? 1376 TRP A CD1   1 
ATOM   1254 C  CD2   . TRP A 1 159 ? -19.074 -16.264 19.041  1.00 63.53  ? 1376 TRP A CD2   1 
ATOM   1255 N  NE1   . TRP A 1 159 ? -19.282 -14.032 18.914  1.00 62.50  ? 1376 TRP A NE1   1 
ATOM   1256 C  CE2   . TRP A 1 159 ? -19.303 -15.078 19.794  1.00 62.17  ? 1376 TRP A CE2   1 
ATOM   1257 C  CE3   . TRP A 1 159 ? -19.053 -17.495 19.713  1.00 58.09  ? 1376 TRP A CE3   1 
ATOM   1258 C  CZ2   . TRP A 1 159 ? -19.510 -15.087 21.182  1.00 60.06  ? 1376 TRP A CZ2   1 
ATOM   1259 C  CZ3   . TRP A 1 159 ? -19.261 -17.505 21.101  1.00 65.09  ? 1376 TRP A CZ3   1 
ATOM   1260 C  CH2   . TRP A 1 159 ? -19.488 -16.303 21.818  1.00 66.30  ? 1376 TRP A CH2   1 
ATOM   1261 N  N     . GLN A 1 160 ? -20.987 -15.902 15.234  1.00 65.14  ? 1377 GLN A N     1 
ATOM   1262 C  CA    . GLN A 1 160 ? -22.237 -15.247 15.420  1.00 61.60  ? 1377 GLN A CA    1 
ATOM   1263 C  C     . GLN A 1 160 ? -22.723 -15.733 16.755  1.00 71.81  ? 1377 GLN A C     1 
ATOM   1264 O  O     . GLN A 1 160 ? -22.565 -16.825 17.113  1.00 83.47  ? 1377 GLN A O     1 
ATOM   1265 C  CB    . GLN A 1 160 ? -23.262 -15.596 14.389  1.00 59.30  ? 1377 GLN A CB    1 
ATOM   1266 C  CG    . GLN A 1 160 ? -23.641 -17.041 14.300  1.00 69.75  ? 1377 GLN A CG    1 
ATOM   1267 C  CD    . GLN A 1 160 ? -24.522 -17.540 15.390  1.00 78.81  ? 1377 GLN A CD    1 
ATOM   1268 O  OE1   . GLN A 1 160 ? -24.611 -18.692 15.593  1.00 72.25  ? 1377 GLN A OE1   1 
ATOM   1269 N  NE2   . GLN A 1 160 ? -25.175 -16.698 16.047  1.00 97.50  ? 1377 GLN A NE2   1 
ATOM   1270 N  N     . GLU A 1 161 ? -23.209 -14.851 17.555  1.00 64.68  ? 1378 GLU A N     1 
ATOM   1271 C  CA    . GLU A 1 161 ? -23.872 -15.112 18.825  1.00 65.68  ? 1378 GLU A CA    1 
ATOM   1272 C  C     . GLU A 1 161 ? -25.308 -14.601 18.752  1.00 69.29  ? 1378 GLU A C     1 
ATOM   1273 O  O     . GLU A 1 161 ? -25.549 -13.433 18.422  1.00 66.91  ? 1378 GLU A O     1 
ATOM   1274 C  CB    . GLU A 1 161 ? -23.122 -14.492 20.002  1.00 62.10  ? 1378 GLU A CB    1 
ATOM   1275 C  CG    . GLU A 1 161 ? -22.704 -13.057 19.894  1.00 63.83  ? 1378 GLU A CG    1 
ATOM   1276 C  CD    . GLU A 1 161 ? -22.104 -12.547 21.218  1.00 70.50  ? 1378 GLU A CD    1 
ATOM   1277 O  OE1   . GLU A 1 161 ? -22.584 -12.952 22.305  1.00 69.84  ? 1378 GLU A OE1   1 
ATOM   1278 O  OE2   . GLU A 1 161 ? -21.132 -11.751 21.170  1.00 66.45  ? 1378 GLU A OE2   1 
ATOM   1279 N  N     . GLY A 1 162 ? -26.258 -15.496 18.997  1.00 67.47  ? 1379 GLY A N     1 
ATOM   1280 C  CA    . GLY A 1 162 ? -27.670 -15.163 19.025  1.00 65.27  ? 1379 GLY A CA    1 
ATOM   1281 C  C     . GLY A 1 162 ? -28.157 -15.251 20.460  1.00 71.85  ? 1379 GLY A C     1 
ATOM   1282 O  O     . GLY A 1 162 ? -27.792 -16.183 21.194  1.00 78.47  ? 1379 GLY A O     1 
ATOM   1283 N  N     . HIS A 1 163 ? -28.956 -14.258 20.855  1.00 66.85  ? 1380 HIS A N     1 
ATOM   1284 C  CA    . HIS A 1 163 ? -29.470 -14.143 22.211  1.00 65.95  ? 1380 HIS A CA    1 
ATOM   1285 C  C     . HIS A 1 163 ? -30.949 -13.838 22.127  1.00 70.85  ? 1380 HIS A C     1 
ATOM   1286 O  O     . HIS A 1 163 ? -31.370 -12.957 21.358  1.00 75.38  ? 1380 HIS A O     1 
ATOM   1287 C  CB    . HIS A 1 163 ? -28.733 -13.082 23.002  1.00 62.98  ? 1380 HIS A CB    1 
ATOM   1288 C  CG    . HIS A 1 163 ? -27.270 -13.350 23.116  1.00 64.80  ? 1380 HIS A CG    1 
ATOM   1289 N  ND1   . HIS A 1 163 ? -26.705 -13.930 24.232  1.00 69.92  ? 1380 HIS A ND1   1 
ATOM   1290 C  CD2   . HIS A 1 163 ? -26.255 -13.144 22.239  1.00 68.43  ? 1380 HIS A CD2   1 
ATOM   1291 C  CE1   . HIS A 1 163 ? -25.397 -14.042 24.049  1.00 71.86  ? 1380 HIS A CE1   1 
ATOM   1292 N  NE2   . HIS A 1 163 ? -25.099 -13.577 22.845  1.00 67.09  ? 1380 HIS A NE2   1 
ATOM   1293 N  N     . THR A 1 164 ? -31.735 -14.618 22.875  1.00 58.58  ? 1381 THR A N     1 
ATOM   1294 C  CA    . THR A 1 164 ? -33.172 -14.678 22.683  1.00 52.20  ? 1381 THR A CA    1 
ATOM   1295 C  C     . THR A 1 164 ? -33.862 -14.761 24.037  1.00 58.81  ? 1381 THR A C     1 
ATOM   1296 O  O     . THR A 1 164 ? -33.355 -15.384 24.978  1.00 58.20  ? 1381 THR A O     1 
ATOM   1297 C  CB    . THR A 1 164 ? -33.578 -15.886 21.812  1.00 56.69  ? 1381 THR A CB    1 
ATOM   1298 O  OG1   . THR A 1 164 ? -33.125 -17.095 22.421  1.00 66.28  ? 1381 THR A OG1   1 
ATOM   1299 C  CG2   . THR A 1 164 ? -32.971 -15.807 20.424  1.00 50.61  ? 1381 THR A CG2   1 
ATOM   1300 N  N     . ALA A 1 165 ? -35.036 -14.125 24.112  1.00 57.48  ? 1382 ALA A N     1 
ATOM   1301 C  CA    . ALA A 1 165 ? -35.836 -14.042 25.330  1.00 70.56  ? 1382 ALA A CA    1 
ATOM   1302 C  C     . ALA A 1 165 ? -37.311 -14.173 24.989  1.00 69.02  ? 1382 ALA A C     1 
ATOM   1303 O  O     . ALA A 1 165 ? -37.822 -13.426 24.146  1.00 71.36  ? 1382 ALA A O     1 
ATOM   1304 C  CB    . ALA A 1 165 ? -35.597 -12.721 26.073  1.00 74.89  ? 1382 ALA A CB    1 
ATOM   1305 N  N     . PHE A 1 166 ? -37.986 -15.104 25.666  1.00 61.92  ? 1383 PHE A N     1 
ATOM   1306 C  CA    . PHE A 1 166 ? -39.387 -15.405 25.437  1.00 65.41  ? 1383 PHE A CA    1 
ATOM   1307 C  C     . PHE A 1 166 ? -40.145 -15.398 26.752  1.00 75.27  ? 1383 PHE A C     1 
ATOM   1308 O  O     . PHE A 1 166 ? -39.563 -15.483 27.836  1.00 66.98  ? 1383 PHE A O     1 
ATOM   1309 C  CB    . PHE A 1 166 ? -39.587 -16.778 24.812  1.00 64.36  ? 1383 PHE A CB    1 
ATOM   1310 C  CG    . PHE A 1 166 ? -38.720 -17.058 23.639  1.00 67.01  ? 1383 PHE A CG    1 
ATOM   1311 C  CD1   . PHE A 1 166 ? -37.432 -17.545 23.806  1.00 61.86  ? 1383 PHE A CD1   1 
ATOM   1312 C  CD2   . PHE A 1 166 ? -39.214 -16.885 22.355  1.00 70.15  ? 1383 PHE A CD2   1 
ATOM   1313 C  CE1   . PHE A 1 166 ? -36.646 -17.830 22.708  1.00 60.31  ? 1383 PHE A CE1   1 
ATOM   1314 C  CE2   . PHE A 1 166 ? -38.443 -17.175 21.255  1.00 65.13  ? 1383 PHE A CE2   1 
ATOM   1315 C  CZ    . PHE A 1 166 ? -37.156 -17.647 21.422  1.00 56.39  ? 1383 PHE A CZ    1 
ATOM   1316 N  N     . ALA A 1 167 ? -41.475 -15.391 26.632  1.00 81.98  ? 1384 ALA A N     1 
ATOM   1317 C  CA    . ALA A 1 167 ? -42.330 -15.508 27.806  1.00 80.19  ? 1384 ALA A CA    1 
ATOM   1318 C  C     . ALA A 1 167 ? -42.456 -16.952 28.278  1.00 81.88  ? 1384 ALA A C     1 
ATOM   1319 O  O     . ALA A 1 167 ? -42.433 -17.205 29.484  1.00 94.09  ? 1384 ALA A O     1 
ATOM   1320 C  CB    . ALA A 1 167 ? -43.709 -14.933 27.517  1.00 70.85  ? 1384 ALA A CB    1 
ATOM   1321 N  N     . THR A 1 168 ? -42.594 -17.902 27.362  1.00 68.10  ? 1385 THR A N     1 
ATOM   1322 C  CA    . THR A 1 168 ? -42.797 -19.302 27.703  1.00 80.24  ? 1385 THR A CA    1 
ATOM   1323 C  C     . THR A 1 168 ? -41.506 -20.119 27.621  1.00 76.16  ? 1385 THR A C     1 
ATOM   1324 O  O     . THR A 1 168 ? -40.641 -19.872 26.781  1.00 70.00  ? 1385 THR A O     1 
ATOM   1325 C  CB    . THR A 1 168 ? -43.830 -19.929 26.755  1.00 83.61  ? 1385 THR A CB    1 
ATOM   1326 O  OG1   . THR A 1 168 ? -43.622 -19.415 25.436  1.00 101.91 ? 1385 THR A OG1   1 
ATOM   1327 C  CG2   . THR A 1 168 ? -45.194 -19.568 27.197  1.00 68.71  ? 1385 THR A CG2   1 
ATOM   1328 N  N     . GLN A 1 169 ? -41.422 -21.167 28.441  1.00 81.97  ? 1386 GLN A N     1 
ATOM   1329 C  CA    . GLN A 1 169 ? -40.331 -22.117 28.247  1.00 86.17  ? 1386 GLN A CA    1 
ATOM   1330 C  C     . GLN A 1 169 ? -40.501 -22.928 26.965  1.00 74.69  ? 1386 GLN A C     1 
ATOM   1331 O  O     . GLN A 1 169 ? -39.503 -23.355 26.374  1.00 66.95  ? 1386 GLN A O     1 
ATOM   1332 C  CB    . GLN A 1 169 ? -40.214 -23.064 29.440  1.00 95.94  ? 1386 GLN A CB    1 
ATOM   1333 C  CG    . GLN A 1 169 ? -38.780 -23.409 29.716  1.00 100.83 ? 1386 GLN A CG    1 
ATOM   1334 C  CD    . GLN A 1 169 ? -38.618 -24.083 31.040  1.00 102.11 ? 1386 GLN A CD    1 
ATOM   1335 O  OE1   . GLN A 1 169 ? -37.786 -23.691 31.856  1.00 99.36  ? 1386 GLN A OE1   1 
ATOM   1336 N  NE2   . GLN A 1 169 ? -39.420 -25.110 31.271  1.00 106.30 ? 1386 GLN A NE2   1 
ATOM   1337 N  N     . LYS A 1 170 ? -41.735 -23.100 26.488  1.00 71.33  ? 1387 LYS A N     1 
ATOM   1338 C  CA    . LYS A 1 170 ? -41.953 -23.879 25.275  1.00 68.12  ? 1387 LYS A CA    1 
ATOM   1339 C  C     . LYS A 1 170 ? -41.317 -23.197 24.062  1.00 72.96  ? 1387 LYS A C     1 
ATOM   1340 O  O     . LYS A 1 170 ? -40.592 -23.838 23.284  1.00 77.49  ? 1387 LYS A O     1 
ATOM   1341 C  CB    . LYS A 1 170 ? -43.454 -24.088 25.055  1.00 70.73  ? 1387 LYS A CB    1 
ATOM   1342 C  CG    . LYS A 1 170 ? -43.773 -24.732 23.717  1.00 74.71  ? 1387 LYS A CG    1 
ATOM   1343 C  CD    . LYS A 1 170 ? -45.227 -25.122 23.585  1.00 78.31  ? 1387 LYS A CD    1 
ATOM   1344 C  CE    . LYS A 1 170 ? -45.697 -24.872 22.149  1.00 85.23  ? 1387 LYS A CE    1 
ATOM   1345 N  NZ    . LYS A 1 170 ? -47.070 -25.438 21.945  1.00 93.94  ? 1387 LYS A NZ    1 
ATOM   1346 N  N     . GLU A 1 171 ? -41.584 -21.893 23.884  1.00 70.24  ? 1388 GLU A N     1 
ATOM   1347 C  CA    . GLU A 1 171 ? -40.904 -21.102 22.859  1.00 73.96  ? 1388 GLU A CA    1 
ATOM   1348 C  C     . GLU A 1 171 ? -39.389 -21.308 22.904  1.00 76.13  ? 1388 GLU A C     1 
ATOM   1349 O  O     . GLU A 1 171 ? -38.747 -21.569 21.875  1.00 82.83  ? 1388 GLU A O     1 
ATOM   1350 C  CB    . GLU A 1 171 ? -41.232 -19.617 23.038  1.00 80.92  ? 1388 GLU A CB    1 
ATOM   1351 C  CG    . GLU A 1 171 ? -42.642 -19.148 22.654  1.00 78.36  ? 1388 GLU A CG    1 
ATOM   1352 C  CD    . GLU A 1 171 ? -42.888 -17.689 23.076  1.00 75.90  ? 1388 GLU A CD    1 
ATOM   1353 O  OE1   . GLU A 1 171 ? -42.546 -16.741 22.298  1.00 71.79  ? 1388 GLU A OE1   1 
ATOM   1354 O  OE2   . GLU A 1 171 ? -43.415 -17.512 24.208  1.00 64.33  ? 1388 GLU A OE2   1 
ATOM   1355 N  N     . ALA A 1 172 ? -38.807 -21.208 24.100  1.00 72.42  ? 1389 ALA A N     1 
ATOM   1356 C  CA    . ALA A 1 172 ? -37.357 -21.308 24.239  1.00 75.18  ? 1389 ALA A CA    1 
ATOM   1357 C  C     . ALA A 1 172 ? -36.842 -22.704 23.849  1.00 75.96  ? 1389 ALA A C     1 
ATOM   1358 O  O     . ALA A 1 172 ? -35.885 -22.828 23.067  1.00 67.26  ? 1389 ALA A O     1 
ATOM   1359 C  CB    . ALA A 1 172 ? -36.960 -20.925 25.669  1.00 75.98  ? 1389 ALA A CB    1 
ATOM   1360 N  N     . ASP A 1 173 ? -37.480 -23.766 24.373  1.00 76.82  ? 1390 ASP A N     1 
ATOM   1361 C  CA    . ASP A 1 173 ? -37.095 -25.144 24.042  1.00 69.25  ? 1390 ASP A CA    1 
ATOM   1362 C  C     . ASP A 1 173 ? -37.094 -25.358 22.533  1.00 63.87  ? 1390 ASP A C     1 
ATOM   1363 O  O     . ASP A 1 173 ? -36.088 -25.811 21.942  1.00 66.61  ? 1390 ASP A O     1 
ATOM   1364 C  CB    . ASP A 1 173 ? -38.073 -26.133 24.689  1.00 53.33  ? 1390 ASP A CB    1 
ATOM   1365 C  CG    . ASP A 1 173 ? -37.888 -26.271 26.207  1.00 69.31  ? 1390 ASP A CG    1 
ATOM   1366 O  OD1   . ASP A 1 173 ? -36.731 -26.284 26.689  1.00 66.67  ? 1390 ASP A OD1   1 
ATOM   1367 O  OD2   . ASP A 1 173 ? -38.916 -26.365 26.928  1.00 63.44  ? 1390 ASP A OD2   1 
ATOM   1368 N  N     . GLU A 1 174 ? -38.211 -24.993 21.885  1.00 57.84  ? 1391 GLU A N     1 
ATOM   1369 C  CA    . GLU A 1 174 ? -38.333 -25.245 20.456  1.00 60.13  ? 1391 GLU A CA    1 
ATOM   1370 C  C     . GLU A 1 174 ? -37.287 -24.469 19.666  1.00 65.93  ? 1391 GLU A C     1 
ATOM   1371 O  O     . GLU A 1 174 ? -36.723 -24.991 18.688  1.00 59.28  ? 1391 GLU A O     1 
ATOM   1372 C  CB    . GLU A 1 174 ? -39.737 -24.904 19.978  1.00 60.16  ? 1391 GLU A CB    1 
ATOM   1373 C  CG    . GLU A 1 174 ? -40.837 -25.559 20.792  1.00 71.98  ? 1391 GLU A CG    1 
ATOM   1374 C  CD    . GLU A 1 174 ? -42.225 -25.376 20.181  1.00 80.90  ? 1391 GLU A CD    1 
ATOM   1375 O  OE1   . GLU A 1 174 ? -42.441 -24.338 19.511  1.00 81.19  ? 1391 GLU A OE1   1 
ATOM   1376 O  OE2   . GLU A 1 174 ? -43.090 -26.267 20.371  1.00 81.33  ? 1391 GLU A OE2   1 
ATOM   1377 N  N     . GLU A 1 175 ? -36.969 -23.242 20.095  1.00 68.68  ? 1392 GLU A N     1 
ATOM   1378 C  CA    . GLU A 1 175 ? -35.920 -22.511 19.388  1.00 71.60  ? 1392 GLU A CA    1 
ATOM   1379 C  C     . GLU A 1 175 ? -34.569 -23.199 19.518  1.00 79.42  ? 1392 GLU A C     1 
ATOM   1380 O  O     . GLU A 1 175 ? -33.788 -23.231 18.559  1.00 76.61  ? 1392 GLU A O     1 
ATOM   1381 C  CB    . GLU A 1 175 ? -35.800 -21.071 19.869  1.00 64.97  ? 1392 GLU A CB    1 
ATOM   1382 C  CG    . GLU A 1 175 ? -34.652 -20.357 19.119  1.00 70.28  ? 1392 GLU A CG    1 
ATOM   1383 C  CD    . GLU A 1 175 ? -34.438 -18.938 19.539  1.00 69.25  ? 1392 GLU A CD    1 
ATOM   1384 O  OE1   . GLU A 1 175 ? -34.889 -18.029 18.809  1.00 66.42  ? 1392 GLU A OE1   1 
ATOM   1385 O  OE2   . GLU A 1 175 ? -33.831 -18.737 20.606  1.00 77.45  ? 1392 GLU A OE2   1 
ATOM   1386 N  N     . VAL A 1 176 ? -34.230 -23.661 20.723  1.00 80.83  ? 1393 VAL A N     1 
ATOM   1387 C  CA    . VAL A 1 176 ? -32.953 -24.352 20.890  1.00 71.08  ? 1393 VAL A CA    1 
ATOM   1388 C  C     . VAL A 1 176 ? -32.823 -25.454 19.845  1.00 64.67  ? 1393 VAL A C     1 
ATOM   1389 O  O     . VAL A 1 176 ? -31.802 -25.582 19.152  1.00 60.75  ? 1393 VAL A O     1 
ATOM   1390 C  CB    . VAL A 1 176 ? -32.819 -24.914 22.315  1.00 62.99  ? 1393 VAL A CB    1 
ATOM   1391 C  CG1   . VAL A 1 176 ? -31.576 -25.717 22.406  1.00 65.92  ? 1393 VAL A CG1   1 
ATOM   1392 C  CG2   . VAL A 1 176 ? -32.768 -23.809 23.336  1.00 62.06  ? 1393 VAL A CG2   1 
ATOM   1393 N  N     . LEU A 1 177 ? -33.891 -26.228 19.672  1.00 63.86  ? 1394 LEU A N     1 
ATOM   1394 C  CA    . LEU A 1 177 ? -33.812 -27.333 18.714  1.00 66.70  ? 1394 LEU A CA    1 
ATOM   1395 C  C     . LEU A 1 177 ? -33.789 -26.847 17.254  1.00 70.61  ? 1394 LEU A C     1 
ATOM   1396 O  O     . LEU A 1 177 ? -33.137 -27.462 16.399  1.00 67.79  ? 1394 LEU A O     1 
ATOM   1397 C  CB    . LEU A 1 177 ? -34.945 -28.318 18.971  1.00 68.20  ? 1394 LEU A CB    1 
ATOM   1398 C  CG    . LEU A 1 177 ? -34.746 -29.109 20.275  1.00 72.66  ? 1394 LEU A CG    1 
ATOM   1399 C  CD1   . LEU A 1 177 ? -35.689 -30.304 20.374  1.00 62.90  ? 1394 LEU A CD1   1 
ATOM   1400 C  CD2   . LEU A 1 177 ? -33.294 -29.565 20.432  1.00 73.27  ? 1394 LEU A CD2   1 
ATOM   1401 N  N     . THR A 1 178 ? -34.510 -25.769 16.929  1.00 69.99  ? 1395 THR A N     1 
ATOM   1402 C  CA    . THR A 1 178 ? -34.463 -25.257 15.551  1.00 68.15  ? 1395 THR A CA    1 
ATOM   1403 C  C     . THR A 1 178 ? -33.073 -24.717 15.198  1.00 65.19  ? 1395 THR A C     1 
ATOM   1404 O  O     . THR A 1 178 ? -32.549 -24.953 14.092  1.00 66.62  ? 1395 THR A O     1 
ATOM   1405 C  CB    . THR A 1 178 ? -35.529 -24.182 15.372  1.00 69.02  ? 1395 THR A CB    1 
ATOM   1406 O  OG1   . THR A 1 178 ? -36.685 -24.568 16.111  1.00 58.72  ? 1395 THR A OG1   1 
ATOM   1407 C  CG2   . THR A 1 178 ? -35.879 -24.000 13.906  1.00 76.64  ? 1395 THR A CG2   1 
ATOM   1408 N  N     . ILE A 1 179 ? -32.436 -24.025 16.141  1.00 56.23  ? 1396 ILE A N     1 
ATOM   1409 C  CA    . ILE A 1 179 ? -31.082 -23.563 15.883  1.00 64.16  ? 1396 ILE A CA    1 
ATOM   1410 C  C     . ILE A 1 179 ? -30.131 -24.752 15.755  1.00 69.33  ? 1396 ILE A C     1 
ATOM   1411 O  O     . ILE A 1 179 ? -29.227 -24.751 14.903  1.00 73.49  ? 1396 ILE A O     1 
ATOM   1412 C  CB    . ILE A 1 179 ? -30.620 -22.580 16.973  1.00 63.28  ? 1396 ILE A CB    1 
ATOM   1413 C  CG1   . ILE A 1 179 ? -31.569 -21.374 17.060  1.00 61.46  ? 1396 ILE A CG1   1 
ATOM   1414 C  CG2   . ILE A 1 179 ? -29.209 -22.104 16.657  1.00 62.02  ? 1396 ILE A CG2   1 
ATOM   1415 C  CD1   . ILE A 1 179 ? -31.570 -20.538 15.824  1.00 57.18  ? 1396 ILE A CD1   1 
ATOM   1416 N  N     . LEU A 1 180 ? -30.318 -25.793 16.580  1.00 60.02  ? 1397 LEU A N     1 
ATOM   1417 C  CA    . LEU A 1 180 ? -29.414 -26.937 16.476  1.00 60.82  ? 1397 LEU A CA    1 
ATOM   1418 C  C     . LEU A 1 180 ? -29.594 -27.672 15.146  1.00 59.89  ? 1397 LEU A C     1 
ATOM   1419 O  O     . LEU A 1 180 ? -28.611 -28.142 14.560  1.00 59.14  ? 1397 LEU A O     1 
ATOM   1420 C  CB    . LEU A 1 180 ? -29.595 -27.878 17.669  1.00 64.11  ? 1397 LEU A CB    1 
ATOM   1421 C  CG    . LEU A 1 180 ? -28.451 -28.871 17.946  1.00 72.45  ? 1397 LEU A CG    1 
ATOM   1422 C  CD1   . LEU A 1 180 ? -27.162 -28.165 18.302  1.00 84.54  ? 1397 LEU A CD1   1 
ATOM   1423 C  CD2   . LEU A 1 180 ? -28.805 -29.809 19.065  1.00 75.56  ? 1397 LEU A CD2   1 
ATOM   1424 N  N     . ASP A 1 181 ? -30.837 -27.777 14.650  1.00 55.96  ? 1398 ASP A N     1 
ATOM   1425 C  CA    . ASP A 1 181 ? -31.048 -28.366 13.330  1.00 57.82  ? 1398 ASP A CA    1 
ATOM   1426 C  C     . ASP A 1 181 ? -30.347 -27.554 12.252  1.00 64.36  ? 1398 ASP A C     1 
ATOM   1427 O  O     . ASP A 1 181 ? -29.778 -28.118 11.305  1.00 65.46  ? 1398 ASP A O     1 
ATOM   1428 C  CB    . ASP A 1 181 ? -32.542 -28.513 13.017  1.00 58.79  ? 1398 ASP A CB    1 
ATOM   1429 C  CG    . ASP A 1 181 ? -32.797 -29.415 11.795  1.00 78.83  ? 1398 ASP A CG    1 
ATOM   1430 O  OD1   . ASP A 1 181 ? -33.093 -28.877 10.708  1.00 81.04  ? 1398 ASP A OD1   1 
ATOM   1431 O  OD2   . ASP A 1 181 ? -32.676 -30.662 11.913  1.00 85.32  ? 1398 ASP A OD2   1 
ATOM   1432 N  N     . LEU A 1 182 ? -30.342 -26.223 12.390  1.00 69.35  ? 1399 LEU A N     1 
ATOM   1433 C  CA    . LEU A 1 182 ? -29.626 -25.452 11.378  1.00 68.74  ? 1399 LEU A CA    1 
ATOM   1434 C  C     . LEU A 1 182 ? -28.117 -25.617 11.498  1.00 62.22  ? 1399 LEU A C     1 
ATOM   1435 O  O     . LEU A 1 182 ? -27.428 -25.688 10.474  1.00 53.26  ? 1399 LEU A O     1 
ATOM   1436 C  CB    . LEU A 1 182 ? -29.978 -23.969 11.450  1.00 61.88  ? 1399 LEU A CB    1 
ATOM   1437 C  CG    . LEU A 1 182 ? -31.408 -23.570 11.113  1.00 60.22  ? 1399 LEU A CG    1 
ATOM   1438 C  CD1   . LEU A 1 182 ? -31.624 -22.073 11.514  1.00 50.62  ? 1399 LEU A CD1   1 
ATOM   1439 C  CD2   . LEU A 1 182 ? -31.703 -23.841 9.642   1.00 45.71  ? 1399 LEU A CD2   1 
ATOM   1440 N  N     . TYR A 1 183 ? -27.589 -25.718 12.719  1.00 55.26  ? 1400 TYR A N     1 
ATOM   1441 C  CA    . TYR A 1 183 ? -26.153 -25.934 12.865  1.00 57.94  ? 1400 TYR A CA    1 
ATOM   1442 C  C     . TYR A 1 183 ? -25.767 -27.260 12.241  1.00 66.40  ? 1400 TYR A C     1 
ATOM   1443 O  O     . TYR A 1 183 ? -24.777 -27.360 11.491  1.00 69.99  ? 1400 TYR A O     1 
ATOM   1444 C  CB    . TYR A 1 183 ? -25.742 -25.916 14.343  1.00 61.74  ? 1400 TYR A CB    1 
ATOM   1445 C  CG    . TYR A 1 183 ? -25.684 -24.543 14.981  1.00 71.49  ? 1400 TYR A CG    1 
ATOM   1446 C  CD1   . TYR A 1 183 ? -25.355 -23.416 14.236  1.00 67.25  ? 1400 TYR A CD1   1 
ATOM   1447 C  CD2   . TYR A 1 183 ? -25.956 -24.381 16.337  1.00 71.68  ? 1400 TYR A CD2   1 
ATOM   1448 C  CE1   . TYR A 1 183 ? -25.303 -22.177 14.829  1.00 66.01  ? 1400 TYR A CE1   1 
ATOM   1449 C  CE2   . TYR A 1 183 ? -25.901 -23.157 16.932  1.00 68.35  ? 1400 TYR A CE2   1 
ATOM   1450 C  CZ    . TYR A 1 183 ? -25.575 -22.056 16.183  1.00 73.06  ? 1400 TYR A CZ    1 
ATOM   1451 O  OH    . TYR A 1 183 ? -25.538 -20.825 16.799  1.00 72.21  ? 1400 TYR A OH    1 
ATOM   1452 N  N     . ALA A 1 184 ? -26.562 -28.294 12.547  1.00 70.67  ? 1401 ALA A N     1 
ATOM   1453 C  CA    . ALA A 1 184 ? -26.371 -29.611 11.961  1.00 64.78  ? 1401 ALA A CA    1 
ATOM   1454 C  C     . ALA A 1 184 ? -26.385 -29.534 10.446  1.00 62.58  ? 1401 ALA A C     1 
ATOM   1455 O  O     . ALA A 1 184 ? -25.573 -30.188 9.773   1.00 59.23  ? 1401 ALA A O     1 
ATOM   1456 C  CB    . ALA A 1 184 ? -27.461 -30.556 12.465  1.00 59.89  ? 1401 ALA A CB    1 
ATOM   1457 N  N     . LYS A 1 185 ? -27.273 -28.709 9.893   1.00 60.02  ? 1402 LYS A N     1 
ATOM   1458 C  CA    . LYS A 1 185 ? -27.311 -28.550 8.445   1.00 61.49  ? 1402 LYS A CA    1 
ATOM   1459 C  C     . LYS A 1 185 ? -26.062 -27.839 7.926   1.00 65.95  ? 1402 LYS A C     1 
ATOM   1460 O  O     . LYS A 1 185 ? -25.542 -28.188 6.861   1.00 64.68  ? 1402 LYS A O     1 
ATOM   1461 C  CB    . LYS A 1 185 ? -28.588 -27.816 8.039   1.00 65.64  ? 1402 LYS A CB    1 
ATOM   1462 C  CG    . LYS A 1 185 ? -29.251 -28.453 6.840   1.00 72.31  ? 1402 LYS A CG    1 
ATOM   1463 C  CD    . LYS A 1 185 ? -30.741 -28.174 6.741   1.00 73.81  ? 1402 LYS A CD    1 
ATOM   1464 C  CE    . LYS A 1 185 ? -31.427 -28.425 8.050   1.00 73.96  ? 1402 LYS A CE    1 
ATOM   1465 N  NZ    . LYS A 1 185 ? -32.885 -28.196 7.907   1.00 75.89  ? 1402 LYS A NZ    1 
ATOM   1466 N  N     . VAL A 1 186 ? -25.551 -26.854 8.672   1.00 65.14  ? 1403 VAL A N     1 
ATOM   1467 C  CA    . VAL A 1 186 ? -24.276 -26.241 8.298   1.00 72.38  ? 1403 VAL A CA    1 
ATOM   1468 C  C     . VAL A 1 186 ? -23.225 -27.321 8.105   1.00 65.32  ? 1403 VAL A C     1 
ATOM   1469 O  O     . VAL A 1 186 ? -22.496 -27.352 7.104   1.00 64.59  ? 1403 VAL A O     1 
ATOM   1470 C  CB    . VAL A 1 186 ? -23.821 -25.214 9.350   1.00 70.89  ? 1403 VAL A CB    1 
ATOM   1471 C  CG1   . VAL A 1 186 ? -22.359 -24.835 9.086   1.00 62.31  ? 1403 VAL A CG1   1 
ATOM   1472 C  CG2   . VAL A 1 186 ? -24.704 -23.978 9.329   1.00 68.49  ? 1403 VAL A CG2   1 
ATOM   1473 N  N     . TYR A 1 187 ? -23.139 -28.227 9.067   1.00 63.40  ? 1404 TYR A N     1 
ATOM   1474 C  CA    . TYR A 1 187 ? -22.084 -29.238 8.984   1.00 63.78  ? 1404 TYR A CA    1 
ATOM   1475 C  C     . TYR A 1 187 ? -22.369 -30.302 7.914   1.00 56.30  ? 1404 TYR A C     1 
ATOM   1476 O  O     . TYR A 1 187 ? -21.500 -30.608 7.098   1.00 53.11  ? 1404 TYR A O     1 
ATOM   1477 C  CB    . TYR A 1 187 ? -21.860 -29.864 10.347  1.00 64.14  ? 1404 TYR A CB    1 
ATOM   1478 C  CG    . TYR A 1 187 ? -20.894 -29.042 11.167  1.00 66.24  ? 1404 TYR A CG    1 
ATOM   1479 C  CD1   . TYR A 1 187 ? -21.361 -28.095 12.079  1.00 65.43  ? 1404 TYR A CD1   1 
ATOM   1480 C  CD2   . TYR A 1 187 ? -19.511 -29.187 11.009  1.00 58.42  ? 1404 TYR A CD2   1 
ATOM   1481 C  CE1   . TYR A 1 187 ? -20.480 -27.334 12.830  1.00 59.58  ? 1404 TYR A CE1   1 
ATOM   1482 C  CE2   . TYR A 1 187 ? -18.628 -28.425 11.751  1.00 55.41  ? 1404 TYR A CE2   1 
ATOM   1483 C  CZ    . TYR A 1 187 ? -19.118 -27.506 12.661  1.00 57.46  ? 1404 TYR A CZ    1 
ATOM   1484 O  OH    . TYR A 1 187 ? -18.260 -26.750 13.412  1.00 57.61  ? 1404 TYR A OH    1 
ATOM   1485 N  N     . THR A 1 188 ? -23.586 -30.824 7.827   1.00 55.59  ? 1405 THR A N     1 
ATOM   1486 C  CA    . THR A 1 188 ? -23.750 -31.923 6.876   1.00 60.73  ? 1405 THR A CA    1 
ATOM   1487 C  C     . THR A 1 188 ? -23.983 -31.412 5.461   1.00 60.00  ? 1405 THR A C     1 
ATOM   1488 O  O     . THR A 1 188 ? -23.305 -31.848 4.530   1.00 63.02  ? 1405 THR A O     1 
ATOM   1489 C  CB    . THR A 1 188 ? -24.884 -32.888 7.302   1.00 59.87  ? 1405 THR A CB    1 
ATOM   1490 O  OG1   . THR A 1 188 ? -26.171 -32.264 7.184   1.00 61.35  ? 1405 THR A OG1   1 
ATOM   1491 C  CG2   . THR A 1 188 ? -24.690 -33.345 8.723   1.00 47.08  ? 1405 THR A CG2   1 
ATOM   1492 N  N     . ASP A 1 189 ? -24.913 -30.466 5.285   1.00 60.45  ? 1406 ASP A N     1 
ATOM   1493 C  CA    . ASP A 1 189 ? -25.384 -30.071 3.957   1.00 62.05  ? 1406 ASP A CA    1 
ATOM   1494 C  C     . ASP A 1 189 ? -24.436 -29.115 3.243   1.00 68.58  ? 1406 ASP A C     1 
ATOM   1495 O  O     . ASP A 1 189 ? -24.358 -29.143 2.009   1.00 76.03  ? 1406 ASP A O     1 
ATOM   1496 C  CB    . ASP A 1 189 ? -26.774 -29.429 4.068   1.00 70.97  ? 1406 ASP A CB    1 
ATOM   1497 C  CG    . ASP A 1 189 ? -27.888 -30.440 4.445   1.00 82.67  ? 1406 ASP A CG    1 
ATOM   1498 O  OD1   . ASP A 1 189 ? -27.598 -31.614 4.796   1.00 83.00  ? 1406 ASP A OD1   1 
ATOM   1499 O  OD2   . ASP A 1 189 ? -29.072 -30.049 4.368   1.00 81.82  ? 1406 ASP A OD2   1 
ATOM   1500 N  N     . LEU A 1 190 ? -23.720 -28.267 3.985   1.00 65.66  ? 1407 LEU A N     1 
ATOM   1501 C  CA    . LEU A 1 190 ? -22.786 -27.298 3.415   1.00 60.97  ? 1407 LEU A CA    1 
ATOM   1502 C  C     . LEU A 1 190 ? -21.347 -27.795 3.440   1.00 62.60  ? 1407 LEU A C     1 
ATOM   1503 O  O     . LEU A 1 190 ? -20.634 -27.679 2.438   1.00 54.63  ? 1407 LEU A O     1 
ATOM   1504 C  CB    . LEU A 1 190 ? -22.871 -25.961 4.174   1.00 53.67  ? 1407 LEU A CB    1 
ATOM   1505 C  CG    . LEU A 1 190 ? -24.213 -25.208 4.134   1.00 63.22  ? 1407 LEU A CG    1 
ATOM   1506 C  CD1   . LEU A 1 190 ? -24.185 -23.922 4.984   1.00 64.85  ? 1407 LEU A CD1   1 
ATOM   1507 C  CD2   . LEU A 1 190 ? -24.676 -24.924 2.690   1.00 57.26  ? 1407 LEU A CD2   1 
ATOM   1508 N  N     . LEU A 1 191 ? -20.915 -28.355 4.568   1.00 64.39  ? 1408 LEU A N     1 
ATOM   1509 C  CA    . LEU A 1 191 ? -19.540 -28.794 4.762   1.00 59.10  ? 1408 LEU A CA    1 
ATOM   1510 C  C     . LEU A 1 191 ? -19.345 -30.294 4.548   1.00 66.27  ? 1408 LEU A C     1 
ATOM   1511 O  O     . LEU A 1 191 ? -18.215 -30.768 4.687   1.00 71.97  ? 1408 LEU A O     1 
ATOM   1512 C  CB    . LEU A 1 191 ? -19.066 -28.394 6.165   1.00 52.13  ? 1408 LEU A CB    1 
ATOM   1513 C  CG    . LEU A 1 191 ? -19.017 -26.859 6.326   1.00 53.33  ? 1408 LEU A CG    1 
ATOM   1514 C  CD1   . LEU A 1 191 ? -18.627 -26.380 7.735   1.00 44.47  ? 1408 LEU A CD1   1 
ATOM   1515 C  CD2   . LEU A 1 191 ? -18.134 -26.187 5.233   1.00 47.72  ? 1408 LEU A CD2   1 
ATOM   1516 N  N     . ALA A 1 192 ? -20.414 -31.047 4.225   1.00 68.49  ? 1409 ALA A N     1 
ATOM   1517 C  CA    . ALA A 1 192 ? -20.344 -32.500 3.958   1.00 62.40  ? 1409 ALA A CA    1 
ATOM   1518 C  C     . ALA A 1 192 ? -19.598 -33.247 5.073   1.00 63.15  ? 1409 ALA A C     1 
ATOM   1519 O  O     . ALA A 1 192 ? -18.854 -34.196 4.821   1.00 60.32  ? 1409 ALA A O     1 
ATOM   1520 C  CB    . ALA A 1 192 ? -19.735 -32.804 2.590   1.00 58.38  ? 1409 ALA A CB    1 
ATOM   1521 N  N     . ILE A 1 193 ? -19.809 -32.800 6.303   1.00 67.78  ? 1410 ILE A N     1 
ATOM   1522 C  CA    . ILE A 1 193 ? -19.234 -33.375 7.518   1.00 62.90  ? 1410 ILE A CA    1 
ATOM   1523 C  C     . ILE A 1 193 ? -20.372 -33.966 8.352   1.00 74.02  ? 1410 ILE A C     1 
ATOM   1524 O  O     . ILE A 1 193 ? -21.353 -33.267 8.626   1.00 75.05  ? 1410 ILE A O     1 
ATOM   1525 C  CB    . ILE A 1 193 ? -18.472 -32.313 8.336   1.00 68.05  ? 1410 ILE A CB    1 
ATOM   1526 C  CG1   . ILE A 1 193 ? -17.232 -31.788 7.601   1.00 74.77  ? 1410 ILE A CG1   1 
ATOM   1527 C  CG2   . ILE A 1 193 ? -18.102 -32.805 9.739   1.00 62.49  ? 1410 ILE A CG2   1 
ATOM   1528 C  CD1   . ILE A 1 193 ? -16.617 -30.553 8.297   1.00 65.53  ? 1410 ILE A CD1   1 
ATOM   1529 N  N     . PRO A 1 194 ? -20.298 -35.231 8.762   1.00 75.90  ? 1411 PRO A N     1 
ATOM   1530 C  CA    . PRO A 1 194 ? -21.285 -35.781 9.700   1.00 74.12  ? 1411 PRO A CA    1 
ATOM   1531 C  C     . PRO A 1 194 ? -20.992 -35.385 11.141  1.00 71.35  ? 1411 PRO A C     1 
ATOM   1532 O  O     . PRO A 1 194 ? -19.849 -35.137 11.516  1.00 89.54  ? 1411 PRO A O     1 
ATOM   1533 C  CB    . PRO A 1 194 ? -21.127 -37.289 9.504   1.00 82.60  ? 1411 PRO A CB    1 
ATOM   1534 C  CG    . PRO A 1 194 ? -19.679 -37.452 9.201   1.00 85.06  ? 1411 PRO A CG    1 
ATOM   1535 C  CD    . PRO A 1 194 ? -19.236 -36.202 8.458   1.00 78.71  ? 1411 PRO A CD    1 
ATOM   1536 N  N     . VAL A 1 195 ? -22.040 -35.347 11.966  1.00 68.78  ? 1412 VAL A N     1 
ATOM   1537 C  CA    . VAL A 1 195 ? -21.945 -34.926 13.367  1.00 72.42  ? 1412 VAL A CA    1 
ATOM   1538 C  C     . VAL A 1 195 ? -22.954 -35.709 14.211  1.00 72.76  ? 1412 VAL A C     1 
ATOM   1539 O  O     . VAL A 1 195 ? -23.798 -36.448 13.696  1.00 61.21  ? 1412 VAL A O     1 
ATOM   1540 C  CB    . VAL A 1 195 ? -22.206 -33.408 13.537  1.00 64.61  ? 1412 VAL A CB    1 
ATOM   1541 C  CG1   . VAL A 1 195 ? -21.220 -32.579 12.751  1.00 57.87  ? 1412 VAL A CG1   1 
ATOM   1542 C  CG2   . VAL A 1 195 ? -23.650 -33.077 13.095  1.00 48.49  ? 1412 VAL A CG2   1 
ATOM   1543 N  N     . VAL A 1 196 ? -22.859 -35.555 15.531  1.00 71.08  ? 1413 VAL A N     1 
ATOM   1544 C  CA    . VAL A 1 196 ? -23.808 -36.150 16.465  1.00 74.47  ? 1413 VAL A CA    1 
ATOM   1545 C  C     . VAL A 1 196 ? -24.483 -35.029 17.245  1.00 74.61  ? 1413 VAL A C     1 
ATOM   1546 O  O     . VAL A 1 196 ? -23.789 -34.211 17.859  1.00 72.27  ? 1413 VAL A O     1 
ATOM   1547 C  CB    . VAL A 1 196 ? -23.110 -37.120 17.435  1.00 77.93  ? 1413 VAL A CB    1 
ATOM   1548 C  CG1   . VAL A 1 196 ? -24.085 -37.616 18.491  1.00 75.31  ? 1413 VAL A CG1   1 
ATOM   1549 C  CG2   . VAL A 1 196 ? -22.449 -38.268 16.678  1.00 71.31  ? 1413 VAL A CG2   1 
ATOM   1550 N  N     . LYS A 1 197 ? -25.831 -35.007 17.235  1.00 73.01  ? 1414 LYS A N     1 
ATOM   1551 C  CA    . LYS A 1 197 ? -26.620 -34.059 18.023  1.00 70.20  ? 1414 LYS A CA    1 
ATOM   1552 C  C     . LYS A 1 197 ? -26.831 -34.625 19.421  1.00 74.42  ? 1414 LYS A C     1 
ATOM   1553 O  O     . LYS A 1 197 ? -27.129 -35.814 19.579  1.00 78.81  ? 1414 LYS A O     1 
ATOM   1554 C  CB    . LYS A 1 197 ? -27.994 -33.768 17.401  1.00 64.01  ? 1414 LYS A CB    1 
ATOM   1555 C  CG    . LYS A 1 197 ? -28.037 -33.347 15.926  1.00 54.22  ? 1414 LYS A CG    1 
ATOM   1556 C  CD    . LYS A 1 197 ? -29.098 -32.300 15.685  1.00 57.29  ? 1414 LYS A CD    1 
ATOM   1557 C  CE    . LYS A 1 197 ? -30.238 -32.747 14.746  1.00 65.24  ? 1414 LYS A CE    1 
ATOM   1558 N  NZ    . LYS A 1 197 ? -31.069 -31.559 14.233  1.00 47.60  ? 1414 LYS A NZ    1 
ATOM   1559 N  N     . GLY A 1 198 ? -26.681 -33.776 20.433  1.00 66.45  ? 1415 GLY A N     1 
ATOM   1560 C  CA    . GLY A 1 198 ? -26.816 -34.293 21.781  1.00 68.47  ? 1415 GLY A CA    1 
ATOM   1561 C  C     . GLY A 1 198 ? -26.949 -33.192 22.806  1.00 72.79  ? 1415 GLY A C     1 
ATOM   1562 O  O     . GLY A 1 198 ? -27.047 -32.010 22.477  1.00 80.57  ? 1415 GLY A O     1 
ATOM   1563 N  N     . ARG A 1 199 ? -26.971 -33.607 24.068  1.00 73.55  ? 1416 ARG A N     1 
ATOM   1564 C  CA    . ARG A 1 199 ? -26.951 -32.700 25.206  1.00 73.20  ? 1416 ARG A CA    1 
ATOM   1565 C  C     . ARG A 1 199 ? -25.616 -32.851 25.916  1.00 75.05  ? 1416 ARG A C     1 
ATOM   1566 O  O     . ARG A 1 199 ? -25.170 -33.975 26.170  1.00 78.05  ? 1416 ARG A O     1 
ATOM   1567 C  CB    . ARG A 1 199 ? -28.087 -32.986 26.185  1.00 58.47  ? 1416 ARG A CB    1 
ATOM   1568 C  CG    . ARG A 1 199 ? -29.321 -32.265 25.828  1.00 71.29  ? 1416 ARG A CG    1 
ATOM   1569 C  CD    . ARG A 1 199 ? -30.228 -32.012 27.031  1.00 84.50  ? 1416 ARG A CD    1 
ATOM   1570 N  NE    . ARG A 1 199 ? -31.569 -31.600 26.605  1.00 83.48  ? 1416 ARG A NE    1 
ATOM   1571 C  CZ    . ARG A 1 199 ? -32.536 -31.216 27.430  1.00 78.84  ? 1416 ARG A CZ    1 
ATOM   1572 N  NH1   . ARG A 1 199 ? -32.327 -31.196 28.740  1.00 72.11  ? 1416 ARG A NH1   1 
ATOM   1573 N  NH2   . ARG A 1 199 ? -33.714 -30.858 26.942  1.00 82.10  ? 1416 ARG A NH2   1 
ATOM   1574 N  N     . LYS A 1 200 ? -24.966 -31.731 26.208  1.00 65.38  ? 1417 LYS A N     1 
ATOM   1575 C  CA    . LYS A 1 200 ? -23.772 -31.809 27.030  1.00 67.03  ? 1417 LYS A CA    1 
ATOM   1576 C  C     . LYS A 1 200 ? -24.133 -32.419 28.377  1.00 74.20  ? 1417 LYS A C     1 
ATOM   1577 O  O     . LYS A 1 200 ? -25.253 -32.281 28.857  1.00 82.35  ? 1417 LYS A O     1 
ATOM   1578 C  CB    . LYS A 1 200 ? -23.160 -30.419 27.212  1.00 62.38  ? 1417 LYS A CB    1 
ATOM   1579 C  CG    . LYS A 1 200 ? -22.564 -29.828 25.930  1.00 66.59  ? 1417 LYS A CG    1 
ATOM   1580 C  CD    . LYS A 1 200 ? -21.323 -30.621 25.517  1.00 81.05  ? 1417 LYS A CD    1 
ATOM   1581 C  CE    . LYS A 1 200 ? -20.431 -29.888 24.531  1.00 88.30  ? 1417 LYS A CE    1 
ATOM   1582 N  NZ    . LYS A 1 200 ? -19.101 -30.576 24.376  1.00 96.11  ? 1417 LYS A NZ    1 
ATOM   1583 N  N     . THR A 1 201 ? -23.197 -33.150 28.969  1.00 86.08  ? 1418 THR A N     1 
ATOM   1584 C  CA    . THR A 1 201 ? -23.413 -33.601 30.338  1.00 84.10  ? 1418 THR A CA    1 
ATOM   1585 C  C     . THR A 1 201 ? -23.368 -32.407 31.284  1.00 73.50  ? 1418 THR A C     1 
ATOM   1586 O  O     . THR A 1 201 ? -23.073 -31.276 30.886  1.00 70.51  ? 1418 THR A O     1 
ATOM   1587 C  CB    . THR A 1 201 ? -22.376 -34.640 30.752  1.00 94.22  ? 1418 THR A CB    1 
ATOM   1588 O  OG1   . THR A 1 201 ? -21.103 -34.007 30.909  1.00 98.39  ? 1418 THR A OG1   1 
ATOM   1589 C  CG2   . THR A 1 201 ? -22.280 -35.746 29.722  1.00 90.74  ? 1418 THR A CG2   1 
ATOM   1590 N  N     . GLU A 1 202 ? -23.694 -32.661 32.547  1.00 75.18  ? 1419 GLU A N     1 
ATOM   1591 C  CA    . GLU A 1 202 ? -23.708 -31.578 33.528  1.00 87.44  ? 1419 GLU A CA    1 
ATOM   1592 C  C     . GLU A 1 202 ? -22.345 -30.926 33.669  1.00 92.41  ? 1419 GLU A C     1 
ATOM   1593 O  O     . GLU A 1 202 ? -22.250 -29.725 33.927  1.00 100.96 ? 1419 GLU A O     1 
ATOM   1594 C  CB    . GLU A 1 202 ? -24.156 -32.107 34.890  1.00 93.33  ? 1419 GLU A CB    1 
ATOM   1595 C  CG    . GLU A 1 202 ? -25.624 -32.456 34.983  1.00 99.63  ? 1419 GLU A CG    1 
ATOM   1596 C  CD    . GLU A 1 202 ? -26.533 -31.295 34.642  1.00 100.29 ? 1419 GLU A CD    1 
ATOM   1597 O  OE1   . GLU A 1 202 ? -27.231 -31.388 33.612  1.00 99.78  ? 1419 GLU A OE1   1 
ATOM   1598 O  OE2   . GLU A 1 202 ? -26.558 -30.301 35.404  1.00 103.27 ? 1419 GLU A OE2   1 
ATOM   1599 N  N     . LYS A 1 203 ? -21.276 -31.701 33.486  1.00 90.09  ? 1420 LYS A N     1 
ATOM   1600 C  CA    . LYS A 1 203 ? -19.930 -31.146 33.566  1.00 85.80  ? 1420 LYS A CA    1 
ATOM   1601 C  C     . LYS A 1 203 ? -19.638 -30.258 32.365  1.00 78.48  ? 1420 LYS A C     1 
ATOM   1602 O  O     . LYS A 1 203 ? -19.137 -29.137 32.511  1.00 77.15  ? 1420 LYS A O     1 
ATOM   1603 C  CB    . LYS A 1 203 ? -18.911 -32.277 33.678  1.00 89.38  ? 1420 LYS A CB    1 
ATOM   1604 C  CG    . LYS A 1 203 ? -17.500 -31.836 33.957  1.00 86.85  ? 1420 LYS A CG    1 
ATOM   1605 C  CD    . LYS A 1 203 ? -16.537 -32.995 33.794  1.00 82.08  ? 1420 LYS A CD    1 
ATOM   1606 C  CE    . LYS A 1 203 ? -15.082 -32.554 33.974  1.00 84.94  ? 1420 LYS A CE    1 
ATOM   1607 N  NZ    . LYS A 1 203 ? -14.217 -33.638 34.527  1.00 80.44  ? 1420 LYS A NZ    1 
ATOM   1608 N  N     . GLU A 1 204 ? -19.960 -30.740 31.170  1.00 75.85  ? 1421 GLU A N     1 
ATOM   1609 C  CA    . GLU A 1 204 ? -19.558 -30.084 29.938  1.00 84.62  ? 1421 GLU A CA    1 
ATOM   1610 C  C     . GLU A 1 204 ? -20.572 -29.070 29.455  1.00 81.49  ? 1421 GLU A C     1 
ATOM   1611 O  O     . GLU A 1 204 ? -20.298 -28.355 28.484  1.00 86.01  ? 1421 GLU A O     1 
ATOM   1612 C  CB    . GLU A 1 204 ? -19.315 -31.124 28.856  1.00 93.39  ? 1421 GLU A CB    1 
ATOM   1613 C  CG    . GLU A 1 204 ? -18.281 -32.130 29.256  1.00 96.55  ? 1421 GLU A CG    1 
ATOM   1614 C  CD    . GLU A 1 204 ? -16.897 -31.614 29.015  1.00 93.87  ? 1421 GLU A CD    1 
ATOM   1615 O  OE1   . GLU A 1 204 ? -16.663 -31.141 27.876  1.00 88.75  ? 1421 GLU A OE1   1 
ATOM   1616 O  OE2   . GLU A 1 204 ? -16.064 -31.685 29.953  1.00 91.36  ? 1421 GLU A OE2   1 
ATOM   1617 N  N     . LYS A 1 205 ? -21.724 -28.990 30.101  1.00 80.91  ? 1422 LYS A N     1 
ATOM   1618 C  CA    . LYS A 1 205 ? -22.690 -27.956 29.796  1.00 79.68  ? 1422 LYS A CA    1 
ATOM   1619 C  C     . LYS A 1 205 ? -22.082 -26.585 30.078  1.00 85.55  ? 1422 LYS A C     1 
ATOM   1620 O  O     . LYS A 1 205 ? -21.206 -26.431 30.941  1.00 81.44  ? 1422 LYS A O     1 
ATOM   1621 C  CB    . LYS A 1 205 ? -23.956 -28.180 30.650  1.00 68.12  ? 1422 LYS A CB    1 
ATOM   1622 C  CG    . LYS A 1 205 ? -24.959 -27.073 30.653  1.00 76.39  ? 1422 LYS A CG    1 
ATOM   1623 C  CD    . LYS A 1 205 ? -25.635 -27.002 31.995  1.00 86.23  ? 1422 LYS A CD    1 
ATOM   1624 C  CE    . LYS A 1 205 ? -26.048 -28.370 32.476  1.00 101.55 ? 1422 LYS A CE    1 
ATOM   1625 N  NZ    . LYS A 1 205 ? -27.041 -28.291 33.598  1.00 98.31  ? 1422 LYS A NZ    1 
ATOM   1626 N  N     . PHE A 1 206 ? -22.557 -25.578 29.342  1.00 82.64  ? 1423 PHE A N     1 
ATOM   1627 C  CA    . PHE A 1 206 ? -22.271 -24.193 29.687  1.00 85.70  ? 1423 PHE A CA    1 
ATOM   1628 C  C     . PHE A 1 206 ? -22.683 -23.945 31.127  1.00 73.82  ? 1423 PHE A C     1 
ATOM   1629 O  O     . PHE A 1 206 ? -23.823 -24.215 31.520  1.00 58.81  ? 1423 PHE A O     1 
ATOM   1630 C  CB    . PHE A 1 206 ? -23.015 -23.236 28.746  1.00 93.91  ? 1423 PHE A CB    1 
ATOM   1631 C  CG    . PHE A 1 206 ? -22.803 -21.796 29.067  1.00 99.42  ? 1423 PHE A CG    1 
ATOM   1632 C  CD1   . PHE A 1 206 ? -21.617 -21.369 29.643  1.00 105.89 ? 1423 PHE A CD1   1 
ATOM   1633 C  CD2   . PHE A 1 206 ? -23.775 -20.859 28.780  1.00 101.57 ? 1423 PHE A CD2   1 
ATOM   1634 C  CE1   . PHE A 1 206 ? -21.413 -20.037 29.947  1.00 104.41 ? 1423 PHE A CE1   1 
ATOM   1635 C  CE2   . PHE A 1 206 ? -23.569 -19.509 29.076  1.00 103.34 ? 1423 PHE A CE2   1 
ATOM   1636 C  CZ    . PHE A 1 206 ? -22.387 -19.104 29.662  1.00 101.77 ? 1423 PHE A CZ    1 
ATOM   1637 N  N     . ALA A 1 207 ? -21.730 -23.449 31.918  1.00 69.02  ? 1424 ALA A N     1 
ATOM   1638 C  CA    . ALA A 1 207 ? -21.911 -23.407 33.366  1.00 71.55  ? 1424 ALA A CA    1 
ATOM   1639 C  C     . ALA A 1 207 ? -23.184 -22.661 33.751  1.00 84.82  ? 1424 ALA A C     1 
ATOM   1640 O  O     . ALA A 1 207 ? -23.939 -23.114 34.625  1.00 87.53  ? 1424 ALA A O     1 
ATOM   1641 C  CB    . ALA A 1 207 ? -20.677 -22.786 34.022  1.00 68.14  ? 1424 ALA A CB    1 
ATOM   1642 N  N     . GLY A 1 208 ? -23.455 -21.527 33.091  1.00 86.45  ? 1425 GLY A N     1 
ATOM   1643 C  CA    . GLY A 1 208 ? -24.622 -20.725 33.421  1.00 87.50  ? 1425 GLY A CA    1 
ATOM   1644 C  C     . GLY A 1 208 ? -25.958 -21.225 32.892  1.00 94.79  ? 1425 GLY A C     1 
ATOM   1645 O  O     . GLY A 1 208 ? -26.998 -20.690 33.289  1.00 97.29  ? 1425 GLY A O     1 
ATOM   1646 N  N     . GLY A 1 209 ? -25.974 -22.249 32.031  1.00 96.71  ? 1426 GLY A N     1 
ATOM   1647 C  CA    . GLY A 1 209 ? -27.207 -22.653 31.394  1.00 87.53  ? 1426 GLY A CA    1 
ATOM   1648 C  C     . GLY A 1 209 ? -28.026 -23.626 32.212  1.00 78.98  ? 1426 GLY A C     1 
ATOM   1649 O  O     . GLY A 1 209 ? -27.581 -24.210 33.190  1.00 75.01  ? 1426 GLY A O     1 
ATOM   1650 N  N     . ASP A 1 210 ? -29.290 -23.757 31.832  1.00 82.87  ? 1427 ASP A N     1 
ATOM   1651 C  CA    . ASP A 1 210 ? -30.069 -24.889 32.308  1.00 83.57  ? 1427 ASP A CA    1 
ATOM   1652 C  C     . ASP A 1 210 ? -29.569 -26.168 31.661  1.00 86.32  ? 1427 ASP A C     1 
ATOM   1653 O  O     . ASP A 1 210 ? -29.204 -27.129 32.344  1.00 102.35 ? 1427 ASP A O     1 
ATOM   1654 C  CB    . ASP A 1 210 ? -31.550 -24.673 32.024  1.00 92.98  ? 1427 ASP A CB    1 
ATOM   1655 C  CG    . ASP A 1 210 ? -32.424 -25.455 32.958  1.00 106.97 ? 1427 ASP A CG    1 
ATOM   1656 O  OD1   . ASP A 1 210 ? -32.308 -25.208 34.176  1.00 113.82 ? 1427 ASP A OD1   1 
ATOM   1657 O  OD2   . ASP A 1 210 ? -33.203 -26.320 32.486  1.00 110.22 ? 1427 ASP A OD2   1 
ATOM   1658 N  N     . TYR A 1 211 ? -29.537 -26.196 30.335  1.00 74.72  ? 1428 TYR A N     1 
ATOM   1659 C  CA    . TYR A 1 211 ? -28.959 -27.325 29.637  1.00 73.86  ? 1428 TYR A CA    1 
ATOM   1660 C  C     . TYR A 1 211 ? -28.363 -26.830 28.331  1.00 70.86  ? 1428 TYR A C     1 
ATOM   1661 O  O     . TYR A 1 211 ? -28.720 -25.766 27.835  1.00 70.24  ? 1428 TYR A O     1 
ATOM   1662 C  CB    . TYR A 1 211 ? -30.007 -28.421 29.403  1.00 85.94  ? 1428 TYR A CB    1 
ATOM   1663 C  CG    . TYR A 1 211 ? -31.161 -28.070 28.469  1.00 79.92  ? 1428 TYR A CG    1 
ATOM   1664 C  CD1   . TYR A 1 211 ? -31.016 -28.177 27.094  1.00 77.15  ? 1428 TYR A CD1   1 
ATOM   1665 C  CD2   . TYR A 1 211 ? -32.399 -27.693 28.963  1.00 71.15  ? 1428 TYR A CD2   1 
ATOM   1666 C  CE1   . TYR A 1 211 ? -32.041 -27.885 26.239  1.00 76.22  ? 1428 TYR A CE1   1 
ATOM   1667 C  CE2   . TYR A 1 211 ? -33.438 -27.400 28.108  1.00 79.59  ? 1428 TYR A CE2   1 
ATOM   1668 C  CZ    . TYR A 1 211 ? -33.250 -27.495 26.737  1.00 79.75  ? 1428 TYR A CZ    1 
ATOM   1669 O  OH    . TYR A 1 211 ? -34.269 -27.204 25.841  1.00 81.11  ? 1428 TYR A OH    1 
ATOM   1670 N  N     . THR A 1 212 ? -27.511 -27.649 27.728  1.00 75.88  ? 1429 THR A N     1 
ATOM   1671 C  CA    . THR A 1 212 ? -26.738 -27.207 26.573  1.00 67.37  ? 1429 THR A CA    1 
ATOM   1672 C  C     . THR A 1 212 ? -26.764 -28.304 25.524  1.00 72.81  ? 1429 THR A C     1 
ATOM   1673 O  O     . THR A 1 212 ? -26.355 -29.437 25.792  1.00 85.75  ? 1429 THR A O     1 
ATOM   1674 C  CB    . THR A 1 212 ? -25.305 -26.856 26.986  1.00 62.81  ? 1429 THR A CB    1 
ATOM   1675 O  OG1   . THR A 1 212 ? -25.321 -25.642 27.759  1.00 74.69  ? 1429 THR A OG1   1 
ATOM   1676 C  CG2   . THR A 1 212 ? -24.426 -26.681 25.767  1.00 58.17  ? 1429 THR A CG2   1 
ATOM   1677 N  N     . THR A 1 213 ? -27.314 -27.992 24.363  1.00 77.12  ? 1430 THR A N     1 
ATOM   1678 C  CA    . THR A 1 213 ? -27.295 -28.916 23.243  1.00 77.94  ? 1430 THR A CA    1 
ATOM   1679 C  C     . THR A 1 213 ? -26.093 -28.614 22.382  1.00 75.82  ? 1430 THR A C     1 
ATOM   1680 O  O     . THR A 1 213 ? -25.479 -27.555 22.491  1.00 75.94  ? 1430 THR A O     1 
ATOM   1681 C  CB    . THR A 1 213 ? -28.573 -28.839 22.389  1.00 78.66  ? 1430 THR A CB    1 
ATOM   1682 O  OG1   . THR A 1 213 ? -28.673 -27.558 21.752  1.00 79.11  ? 1430 THR A OG1   1 
ATOM   1683 C  CG2   . THR A 1 213 ? -29.820 -29.111 23.230  1.00 77.52  ? 1430 THR A CG2   1 
ATOM   1684 N  N     . THR A 1 214 ? -25.748 -29.575 21.533  1.00 68.00  ? 1431 THR A N     1 
ATOM   1685 C  CA    . THR A 1 214 ? -24.536 -29.418 20.746  1.00 61.70  ? 1431 THR A CA    1 
ATOM   1686 C  C     . THR A 1 214 ? -24.545 -30.340 19.538  1.00 60.12  ? 1431 THR A C     1 
ATOM   1687 O  O     . THR A 1 214 ? -25.271 -31.347 19.487  1.00 53.52  ? 1431 THR A O     1 
ATOM   1688 C  CB    . THR A 1 214 ? -23.306 -29.701 21.593  1.00 67.90  ? 1431 THR A CB    1 
ATOM   1689 O  OG1   . THR A 1 214 ? -22.150 -29.714 20.749  1.00 68.78  ? 1431 THR A OG1   1 
ATOM   1690 C  CG2   . THR A 1 214 ? -23.474 -31.049 22.270  1.00 75.59  ? 1431 THR A CG2   1 
ATOM   1691 N  N     . VAL A 1 215 ? -23.729 -29.960 18.554  1.00 55.69  ? 1432 VAL A N     1 
ATOM   1692 C  CA    . VAL A 1 215 ? -23.306 -30.846 17.479  1.00 60.82  ? 1432 VAL A CA    1 
ATOM   1693 C  C     . VAL A 1 215 ? -21.822 -31.125 17.707  1.00 66.42  ? 1432 VAL A C     1 
ATOM   1694 O  O     . VAL A 1 215 ? -21.042 -30.198 17.963  1.00 66.34  ? 1432 VAL A O     1 
ATOM   1695 C  CB    . VAL A 1 215 ? -23.582 -30.250 16.080  1.00 53.23  ? 1432 VAL A CB    1 
ATOM   1696 C  CG1   . VAL A 1 215 ? -25.059 -30.092 15.857  1.00 54.30  ? 1432 VAL A CG1   1 
ATOM   1697 C  CG2   . VAL A 1 215 ? -22.913 -28.915 15.896  1.00 59.16  ? 1432 VAL A CG2   1 
ATOM   1698 N  N     . GLU A 1 216 ? -21.444 -32.409 17.698  1.00 71.69  ? 1433 GLU A N     1 
ATOM   1699 C  CA    . GLU A 1 216 ? -20.052 -32.812 17.907  1.00 65.74  ? 1433 GLU A CA    1 
ATOM   1700 C  C     . GLU A 1 216 ? -19.543 -33.560 16.690  1.00 62.65  ? 1433 GLU A C     1 
ATOM   1701 O  O     . GLU A 1 216 ? -20.293 -34.323 16.064  1.00 59.26  ? 1433 GLU A O     1 
ATOM   1702 C  CB    . GLU A 1 216 ? -19.899 -33.687 19.140  1.00 64.28  ? 1433 GLU A CB    1 
ATOM   1703 C  CG    . GLU A 1 216 ? -20.722 -33.235 20.338  1.00 77.15  ? 1433 GLU A CG    1 
ATOM   1704 C  CD    . GLU A 1 216 ? -19.915 -32.421 21.330  1.00 92.08  ? 1433 GLU A CD    1 
ATOM   1705 O  OE1   . GLU A 1 216 ? -20.499 -31.525 21.975  1.00 100.82 ? 1433 GLU A OE1   1 
ATOM   1706 O  OE2   . GLU A 1 216 ? -18.697 -32.682 21.468  1.00 95.01  ? 1433 GLU A OE2   1 
ATOM   1707 N  N     . ALA A 1 217 ? -18.286 -33.304 16.322  1.00 64.20  ? 1434 ALA A N     1 
ATOM   1708 C  CA    . ALA A 1 217 ? -17.663 -34.006 15.202  1.00 67.16  ? 1434 ALA A CA    1 
ATOM   1709 C  C     . ALA A 1 217 ? -16.343 -34.614 15.655  1.00 70.26  ? 1434 ALA A C     1 
ATOM   1710 O  O     . ALA A 1 217 ? -15.830 -34.299 16.730  1.00 75.23  ? 1434 ALA A O     1 
ATOM   1711 C  CB    . ALA A 1 217 ? -17.428 -33.090 13.998  1.00 61.34  ? 1434 ALA A CB    1 
ATOM   1712 N  N     . TYR A 1 218 ? -15.811 -35.526 14.845  1.00 73.92  ? 1435 TYR A N     1 
ATOM   1713 C  CA    . TYR A 1 218 ? -14.567 -36.225 15.160  1.00 83.16  ? 1435 TYR A CA    1 
ATOM   1714 C  C     . TYR A 1 218 ? -13.580 -36.000 14.025  1.00 77.31  ? 1435 TYR A C     1 
ATOM   1715 O  O     . TYR A 1 218 ? -13.929 -36.189 12.852  1.00 75.38  ? 1435 TYR A O     1 
ATOM   1716 C  CB    . TYR A 1 218 ? -14.799 -37.733 15.378  1.00 96.82  ? 1435 TYR A CB    1 
ATOM   1717 C  CG    . TYR A 1 218 ? -13.577 -38.507 15.859  1.00 108.85 ? 1435 TYR A CG    1 
ATOM   1718 C  CD1   . TYR A 1 218 ? -13.087 -39.594 15.138  1.00 111.33 ? 1435 TYR A CD1   1 
ATOM   1719 C  CD2   . TYR A 1 218 ? -12.914 -38.147 17.037  1.00 115.61 ? 1435 TYR A CD2   1 
ATOM   1720 C  CE1   . TYR A 1 218 ? -11.968 -40.306 15.572  1.00 118.14 ? 1435 TYR A CE1   1 
ATOM   1721 C  CE2   . TYR A 1 218 ? -11.790 -38.854 17.476  1.00 123.63 ? 1435 TYR A CE2   1 
ATOM   1722 C  CZ    . TYR A 1 218 ? -11.329 -39.930 16.736  1.00 121.44 ? 1435 TYR A CZ    1 
ATOM   1723 O  OH    . TYR A 1 218 ? -10.233 -40.635 17.154  1.00 119.35 ? 1435 TYR A OH    1 
ATOM   1724 N  N     . ILE A 1 219 ? -12.363 -35.587 14.366  1.00 66.00  ? 1436 ILE A N     1 
ATOM   1725 C  CA    . ILE A 1 219 ? -11.266 -35.589 13.414  1.00 71.02  ? 1436 ILE A CA    1 
ATOM   1726 C  C     . ILE A 1 219 ? -10.470 -36.854 13.723  1.00 68.52  ? 1436 ILE A C     1 
ATOM   1727 O  O     . ILE A 1 219 ? -9.868  -36.977 14.799  1.00 73.23  ? 1436 ILE A O     1 
ATOM   1728 C  CB    . ILE A 1 219 ? -10.415 -34.313 13.524  1.00 63.12  ? 1436 ILE A CB    1 
ATOM   1729 N  N     . SER A 1 220 ? -10.518 -37.822 12.805  1.00 58.31  ? 1437 SER A N     1 
ATOM   1730 C  CA    . SER A 1 220 ? -9.859  -39.110 13.030  1.00 77.37  ? 1437 SER A CA    1 
ATOM   1731 C  C     . SER A 1 220 ? -8.359  -39.058 12.754  1.00 95.77  ? 1437 SER A C     1 
ATOM   1732 O  O     . SER A 1 220 ? -7.592  -39.782 13.397  1.00 106.51 ? 1437 SER A O     1 
ATOM   1733 C  CB    . SER A 1 220 ? -10.517 -40.214 12.186  1.00 73.61  ? 1437 SER A CB    1 
ATOM   1734 O  OG    . SER A 1 220 ? -10.359 -39.996 10.791  1.00 63.69  ? 1437 SER A OG    1 
ATOM   1735 N  N     . ALA A 1 221 ? -7.928  -38.261 11.769  1.00 99.57  ? 1438 ALA A N     1 
ATOM   1736 C  CA    . ALA A 1 221 ? -6.503  -38.174 11.441  1.00 95.63  ? 1438 ALA A CA    1 
ATOM   1737 C  C     . ALA A 1 221 ? -5.676  -37.873 12.686  1.00 95.69  ? 1438 ALA A C     1 
ATOM   1738 O  O     . ALA A 1 221 ? -4.630  -38.490 12.919  1.00 107.22 ? 1438 ALA A O     1 
ATOM   1739 C  CB    . ALA A 1 221 ? -6.276  -37.130 10.349  1.00 91.38  ? 1438 ALA A CB    1 
ATOM   1740 N  N     . SER A 1 222 ? -6.127  -36.883 13.476  1.00 84.68  ? 1439 SER A N     1 
ATOM   1741 C  CA    . SER A 1 222 ? -5.566  -36.543 14.787  1.00 89.10  ? 1439 SER A CA    1 
ATOM   1742 C  C     . SER A 1 222 ? -6.000  -37.507 15.882  1.00 96.06  ? 1439 SER A C     1 
ATOM   1743 O  O     . SER A 1 222 ? -5.306  -37.642 16.900  1.00 96.15  ? 1439 SER A O     1 
ATOM   1744 C  CB    . SER A 1 222 ? -5.980  -35.140 15.219  1.00 92.15  ? 1439 SER A CB    1 
ATOM   1745 O  OG    . SER A 1 222 ? -5.929  -35.009 16.632  1.00 97.07  ? 1439 SER A OG    1 
ATOM   1746 N  N     . GLY A 1 223 ? -7.169  -38.130 15.741  1.00 107.20 ? 1440 GLY A N     1 
ATOM   1747 C  CA    . GLY A 1 223 ? -7.765  -38.890 16.823  1.00 109.40 ? 1440 GLY A CA    1 
ATOM   1748 C  C     . GLY A 1 223 ? -8.498  -38.104 17.887  1.00 107.66 ? 1440 GLY A C     1 
ATOM   1749 O  O     . GLY A 1 223 ? -8.658  -38.618 18.993  1.00 111.11 ? 1440 GLY A O     1 
ATOM   1750 N  N     . ARG A 1 224 ? -8.948  -36.878 17.612  1.00 102.91 ? 1441 ARG A N     1 
ATOM   1751 C  CA    . ARG A 1 224 ? -9.565  -36.070 18.659  1.00 95.88  ? 1441 ARG A CA    1 
ATOM   1752 C  C     . ARG A 1 224 ? -10.921 -35.551 18.188  1.00 91.65  ? 1441 ARG A C     1 
ATOM   1753 O  O     . ARG A 1 224 ? -11.142 -35.337 16.990  1.00 84.28  ? 1441 ARG A O     1 
ATOM   1754 C  CB    . ARG A 1 224 ? -8.627  -34.920 19.115  1.00 95.46  ? 1441 ARG A CB    1 
ATOM   1755 C  CG    . ARG A 1 224 ? -7.416  -35.445 19.887  1.00 103.15 ? 1441 ARG A CG    1 
ATOM   1756 C  CD    . ARG A 1 224 ? -6.619  -34.355 20.571  1.00 112.57 ? 1441 ARG A CD    1 
ATOM   1757 N  NE    . ARG A 1 224 ? -6.213  -34.708 21.936  1.00 112.87 ? 1441 ARG A NE    1 
ATOM   1758 C  CZ    . ARG A 1 224 ? -5.216  -35.532 22.251  1.00 107.95 ? 1441 ARG A CZ    1 
ATOM   1759 N  NH1   . ARG A 1 224 ? -4.499  -36.113 21.297  1.00 103.86 ? 1441 ARG A NH1   1 
ATOM   1760 N  NH2   . ARG A 1 224 ? -4.931  -35.769 23.527  1.00 110.39 ? 1441 ARG A NH2   1 
ATOM   1761 N  N     . ALA A 1 225 ? -11.839 -35.361 19.142  1.00 86.80  ? 1442 ALA A N     1 
ATOM   1762 C  CA    . ALA A 1 225 ? -13.184 -34.872 18.851  1.00 74.26  ? 1442 ALA A CA    1 
ATOM   1763 C  C     . ALA A 1 225 ? -13.311 -33.393 19.198  1.00 66.30  ? 1442 ALA A C     1 
ATOM   1764 O  O     . ALA A 1 225 ? -12.668 -32.898 20.124  1.00 62.26  ? 1442 ALA A O     1 
ATOM   1765 C  CB    . ALA A 1 225 ? -14.229 -35.692 19.619  1.00 68.87  ? 1442 ALA A CB    1 
ATOM   1766 N  N     . ILE A 1 226 ? -14.245 -32.713 18.533  1.00 76.82  ? 1443 ILE A N     1 
ATOM   1767 C  CA    . ILE A 1 226 ? -14.368 -31.263 18.692  1.00 80.38  ? 1443 ILE A CA    1 
ATOM   1768 C  C     . ILE A 1 226 ? -15.828 -30.829 18.598  1.00 79.38  ? 1443 ILE A C     1 
ATOM   1769 O  O     . ILE A 1 226 ? -16.612 -31.327 17.774  1.00 73.94  ? 1443 ILE A O     1 
ATOM   1770 C  CB    . ILE A 1 226 ? -13.503 -30.527 17.645  1.00 71.01  ? 1443 ILE A CB    1 
ATOM   1771 C  CG1   . ILE A 1 226 ? -13.605 -29.015 17.829  1.00 83.07  ? 1443 ILE A CG1   1 
ATOM   1772 C  CG2   . ILE A 1 226 ? -13.894 -30.936 16.233  1.00 50.32  ? 1443 ILE A CG2   1 
ATOM   1773 C  CD1   . ILE A 1 226 ? -12.409 -28.263 17.257  1.00 93.85  ? 1443 ILE A CD1   1 
ATOM   1774 N  N     . GLN A 1 227 ? -16.232 -29.913 19.447  1.00 80.67  ? 1444 GLN A N     1 
ATOM   1775 C  CA    . GLN A 1 227 ? -17.541 -29.341 19.439  1.00 69.86  ? 1444 GLN A CA    1 
ATOM   1776 C  C     . GLN A 1 227 ? -17.615 -28.530 18.211  1.00 65.60  ? 1444 GLN A C     1 
ATOM   1777 O  O     . GLN A 1 227 ? -16.772 -27.793 17.976  1.00 90.38  ? 1444 GLN A O     1 
ATOM   1778 C  CB    . GLN A 1 227 ? -17.573 -28.406 20.591  1.00 69.23  ? 1444 GLN A CB    1 
ATOM   1779 C  CG    . GLN A 1 227 ? -18.897 -27.857 20.941  1.00 69.43  ? 1444 GLN A CG    1 
ATOM   1780 C  CD    . GLN A 1 227 ? -18.787 -26.916 22.063  1.00 73.50  ? 1444 GLN A CD    1 
ATOM   1781 O  OE1   . GLN A 1 227 ? -18.706 -27.308 23.173  1.00 78.21  ? 1444 GLN A OE1   1 
ATOM   1782 N  NE2   . GLN A 1 227 ? -18.767 -25.671 21.774  1.00 76.44  ? 1444 GLN A NE2   1 
ATOM   1783 N  N     . GLY A 1 228 ? -18.641 -28.643 17.426  1.00 57.91  ? 1445 GLY A N     1 
ATOM   1784 C  CA    . GLY A 1 228 ? -18.757 -27.896 16.191  1.00 57.12  ? 1445 GLY A CA    1 
ATOM   1785 C  C     . GLY A 1 228 ? -19.631 -26.656 16.285  1.00 66.72  ? 1445 GLY A C     1 
ATOM   1786 O  O     . GLY A 1 228 ? -19.384 -25.668 15.581  1.00 72.05  ? 1445 GLY A O     1 
ATOM   1787 N  N     . ALA A 1 229 ? -20.650 -26.706 17.150  1.00 57.35  ? 1446 ALA A N     1 
ATOM   1788 C  CA    . ALA A 1 229 ? -21.569 -25.609 17.447  1.00 60.10  ? 1446 ALA A CA    1 
ATOM   1789 C  C     . ALA A 1 229 ? -22.327 -25.989 18.703  1.00 62.07  ? 1446 ALA A C     1 
ATOM   1790 O  O     . ALA A 1 229 ? -22.376 -27.164 19.069  1.00 68.94  ? 1446 ALA A O     1 
ATOM   1791 C  CB    . ALA A 1 229 ? -22.539 -25.329 16.294  1.00 48.04  ? 1446 ALA A CB    1 
ATOM   1792 N  N     . THR A 1 230 ? -22.917 -24.991 19.369  1.00 54.89  ? 1447 THR A N     1 
ATOM   1793 C  CA    . THR A 1 230 ? -23.779 -25.262 20.523  1.00 58.25  ? 1447 THR A CA    1 
ATOM   1794 C  C     . THR A 1 230 ? -24.942 -24.286 20.558  1.00 69.68  ? 1447 THR A C     1 
ATOM   1795 O  O     . THR A 1 230 ? -24.914 -23.193 19.972  1.00 64.45  ? 1447 THR A O     1 
ATOM   1796 C  CB    . THR A 1 230 ? -23.071 -25.213 21.907  1.00 63.08  ? 1447 THR A CB    1 
ATOM   1797 O  OG1   . THR A 1 230 ? -22.698 -23.872 22.252  1.00 72.95  ? 1447 THR A OG1   1 
ATOM   1798 C  CG2   . THR A 1 230 ? -21.876 -26.105 21.955  1.00 64.26  ? 1447 THR A CG2   1 
ATOM   1799 N  N     . SER A 1 231 ? -25.969 -24.715 21.283  1.00 70.27  ? 1448 SER A N     1 
ATOM   1800 C  CA    . SER A 1 231 ? -27.220 -23.975 21.376  1.00 60.74  ? 1448 SER A CA    1 
ATOM   1801 C  C     . SER A 1 231 ? -27.741 -24.216 22.784  1.00 66.98  ? 1448 SER A C     1 
ATOM   1802 O  O     . SER A 1 231 ? -28.149 -25.333 23.111  1.00 74.81  ? 1448 SER A O     1 
ATOM   1803 C  CB    . SER A 1 231 ? -28.185 -24.470 20.305  1.00 50.26  ? 1448 SER A CB    1 
ATOM   1804 O  OG    . SER A 1 231 ? -29.533 -24.155 20.621  1.00 60.16  ? 1448 SER A OG    1 
ATOM   1805 N  N     . HIS A 1 232 ? -27.677 -23.189 23.629  1.00 60.83  ? 1449 HIS A N     1 
ATOM   1806 C  CA    . HIS A 1 232 ? -27.968 -23.330 25.048  1.00 59.72  ? 1449 HIS A CA    1 
ATOM   1807 C  C     . HIS A 1 232 ? -29.383 -22.871 25.364  1.00 68.39  ? 1449 HIS A C     1 
ATOM   1808 O  O     . HIS A 1 232 ? -29.937 -21.985 24.706  1.00 77.41  ? 1449 HIS A O     1 
ATOM   1809 C  CB    . HIS A 1 232 ? -27.000 -22.531 25.916  1.00 61.42  ? 1449 HIS A CB    1 
ATOM   1810 C  CG    . HIS A 1 232 ? -25.590 -22.556 25.432  1.00 74.31  ? 1449 HIS A CG    1 
ATOM   1811 N  ND1   . HIS A 1 232 ? -24.695 -23.544 25.783  1.00 78.09  ? 1449 HIS A ND1   1 
ATOM   1812 C  CD2   . HIS A 1 232 ? -24.925 -21.721 24.604  1.00 75.32  ? 1449 HIS A CD2   1 
ATOM   1813 C  CE1   . HIS A 1 232 ? -23.535 -23.310 25.195  1.00 76.34  ? 1449 HIS A CE1   1 
ATOM   1814 N  NE2   . HIS A 1 232 ? -23.646 -22.207 24.479  1.00 74.26  ? 1449 HIS A NE2   1 
ATOM   1815 N  N     . HIS A 1 233 ? -29.949 -23.470 26.397  1.00 66.55  ? 1450 HIS A N     1 
ATOM   1816 C  CA    . HIS A 1 233 ? -31.172 -22.980 27.016  1.00 72.86  ? 1450 HIS A CA    1 
ATOM   1817 C  C     . HIS A 1 233 ? -30.785 -22.451 28.391  1.00 77.80  ? 1450 HIS A C     1 
ATOM   1818 O  O     . HIS A 1 233 ? -30.550 -23.228 29.323  1.00 78.32  ? 1450 HIS A O     1 
ATOM   1819 C  CB    . HIS A 1 233 ? -32.247 -24.054 27.117  1.00 71.78  ? 1450 HIS A CB    1 
ATOM   1820 C  CG    . HIS A 1 233 ? -33.441 -23.612 27.909  1.00 86.02  ? 1450 HIS A CG    1 
ATOM   1821 N  ND1   . HIS A 1 233 ? -34.171 -22.485 27.587  1.00 87.68  ? 1450 HIS A ND1   1 
ATOM   1822 C  CD2   . HIS A 1 233 ? -34.009 -24.119 29.029  1.00 88.73  ? 1450 HIS A CD2   1 
ATOM   1823 C  CE1   . HIS A 1 233 ? -35.148 -22.332 28.463  1.00 90.42  ? 1450 HIS A CE1   1 
ATOM   1824 N  NE2   . HIS A 1 233 ? -35.075 -23.313 29.346  1.00 89.48  ? 1450 HIS A NE2   1 
ATOM   1825 N  N     . LEU A 1 234 ? -30.732 -21.125 28.520  1.00 72.58  ? 1451 LEU A N     1 
ATOM   1826 C  CA    . LEU A 1 234 ? -30.388 -20.545 29.805  1.00 72.00  ? 1451 LEU A CA    1 
ATOM   1827 C  C     . LEU A 1 234 ? -31.541 -20.624 30.775  1.00 81.91  ? 1451 LEU A C     1 
ATOM   1828 O  O     . LEU A 1 234 ? -31.325 -20.474 31.984  1.00 84.93  ? 1451 LEU A O     1 
ATOM   1829 C  CB    . LEU A 1 234 ? -29.955 -19.085 29.649  1.00 69.04  ? 1451 LEU A CB    1 
ATOM   1830 C  CG    . LEU A 1 234 ? -28.708 -18.870 28.807  1.00 74.63  ? 1451 LEU A CG    1 
ATOM   1831 C  CD1   . LEU A 1 234 ? -27.697 -19.998 29.033  1.00 73.50  ? 1451 LEU A CD1   1 
ATOM   1832 C  CD2   . LEU A 1 234 ? -29.066 -18.749 27.361  1.00 69.65  ? 1451 LEU A CD2   1 
ATOM   1833 N  N     . GLY A 1 235 ? -32.750 -20.864 30.269  1.00 88.22  ? 1452 GLY A N     1 
ATOM   1834 C  CA    . GLY A 1 235 ? -33.879 -20.950 31.179  1.00 87.21  ? 1452 GLY A CA    1 
ATOM   1835 C  C     . GLY A 1 235 ? -34.117 -19.605 31.825  1.00 90.51  ? 1452 GLY A C     1 
ATOM   1836 O  O     . GLY A 1 235 ? -34.244 -18.584 31.143  1.00 94.86  ? 1452 GLY A O     1 
ATOM   1837 N  N     . GLN A 1 236 ? -34.200 -19.591 33.152  1.00 88.67  ? 1453 GLN A N     1 
ATOM   1838 C  CA    . GLN A 1 236 ? -34.460 -18.364 33.890  1.00 82.17  ? 1453 GLN A CA    1 
ATOM   1839 C  C     . GLN A 1 236 ? -33.264 -17.863 34.686  1.00 88.78  ? 1453 GLN A C     1 
ATOM   1840 O  O     . GLN A 1 236 ? -33.430 -16.966 35.515  1.00 86.00  ? 1453 GLN A O     1 
ATOM   1841 C  CB    . GLN A 1 236 ? -35.665 -18.547 34.819  1.00 79.29  ? 1453 GLN A CB    1 
ATOM   1842 C  CG    . GLN A 1 236 ? -36.975 -18.084 34.185  1.00 84.96  ? 1453 GLN A CG    1 
ATOM   1843 C  CD    . GLN A 1 236 ? -38.196 -18.267 35.072  1.00 88.05  ? 1453 GLN A CD    1 
ATOM   1844 O  OE1   . GLN A 1 236 ? -38.093 -18.596 36.262  1.00 88.67  ? 1453 GLN A OE1   1 
ATOM   1845 N  NE2   . GLN A 1 236 ? -39.369 -18.067 34.483  1.00 89.49  ? 1453 GLN A NE2   1 
ATOM   1846 N  N     . ASN A 1 237 ? -32.069 -18.419 34.474  1.00 93.26  ? 1454 ASN A N     1 
ATOM   1847 C  CA    . ASN A 1 237 ? -30.927 -18.038 35.306  1.00 98.59  ? 1454 ASN A CA    1 
ATOM   1848 C  C     . ASN A 1 237 ? -30.524 -16.592 35.066  1.00 93.84  ? 1454 ASN A C     1 
ATOM   1849 O  O     . ASN A 1 237 ? -30.398 -15.803 36.011  1.00 106.03 ? 1454 ASN A O     1 
ATOM   1850 C  CB    . ASN A 1 237 ? -29.747 -18.962 35.033  1.00 104.12 ? 1454 ASN A CB    1 
ATOM   1851 C  CG    . ASN A 1 237 ? -30.090 -20.400 35.261  1.00 103.85 ? 1454 ASN A CG    1 
ATOM   1852 O  OD1   . ASN A 1 237 ? -30.766 -20.733 36.233  1.00 109.58 ? 1454 ASN A OD1   1 
ATOM   1853 N  ND2   . ASN A 1 237 ? -29.647 -21.269 34.359  1.00 97.52  ? 1454 ASN A ND2   1 
ATOM   1854 N  N     . PHE A 1 238 ? -30.338 -16.221 33.804  1.00 85.99  ? 1455 PHE A N     1 
ATOM   1855 C  CA    . PHE A 1 238 ? -29.868 -14.879 33.518  1.00 87.23  ? 1455 PHE A CA    1 
ATOM   1856 C  C     . PHE A 1 238 ? -30.973 -13.850 33.682  1.00 88.27  ? 1455 PHE A C     1 
ATOM   1857 O  O     . PHE A 1 238 ? -30.711 -12.725 34.096  1.00 92.19  ? 1455 PHE A O     1 
ATOM   1858 C  CB    . PHE A 1 238 ? -29.295 -14.809 32.112  1.00 84.21  ? 1455 PHE A CB    1 
ATOM   1859 C  CG    . PHE A 1 238 ? -27.963 -15.448 31.981  1.00 86.27  ? 1455 PHE A CG    1 
ATOM   1860 C  CD1   . PHE A 1 238 ? -27.852 -16.773 31.599  1.00 96.47  ? 1455 PHE A CD1   1 
ATOM   1861 C  CD2   . PHE A 1 238 ? -26.820 -14.737 32.249  1.00 85.30  ? 1455 PHE A CD2   1 
ATOM   1862 C  CE1   . PHE A 1 238 ? -26.616 -17.375 31.480  1.00 101.29 ? 1455 PHE A CE1   1 
ATOM   1863 C  CE2   . PHE A 1 238 ? -25.579 -15.331 32.134  1.00 98.45  ? 1455 PHE A CE2   1 
ATOM   1864 C  CZ    . PHE A 1 238 ? -25.473 -16.652 31.746  1.00 102.62 ? 1455 PHE A CZ    1 
ATOM   1865 N  N     . SER A 1 239 ? -32.210 -14.193 33.350  1.00 83.59  ? 1456 SER A N     1 
ATOM   1866 C  CA    . SER A 1 239 ? -33.306 -13.274 33.635  1.00 81.98  ? 1456 SER A CA    1 
ATOM   1867 C  C     . SER A 1 239 ? -33.309 -12.894 35.108  1.00 84.04  ? 1456 SER A C     1 
ATOM   1868 O  O     . SER A 1 239 ? -33.337 -11.704 35.450  1.00 82.92  ? 1456 SER A O     1 
ATOM   1869 C  CB    . SER A 1 239 ? -34.629 -13.894 33.209  1.00 77.80  ? 1456 SER A CB    1 
ATOM   1870 O  OG    . SER A 1 239 ? -34.708 -15.186 33.745  1.00 81.23  ? 1456 SER A OG    1 
ATOM   1871 N  N     . ARG A 1 240 ? -33.272 -13.896 35.999  1.00 86.42  ? 1457 ARG A N     1 
ATOM   1872 C  CA    . ARG A 1 240 ? -33.267 -13.604 37.430  1.00 90.41  ? 1457 ARG A CA    1 
ATOM   1873 C  C     . ARG A 1 240 ? -32.012 -12.852 37.838  1.00 90.17  ? 1457 ARG A C     1 
ATOM   1874 O  O     . ARG A 1 240 ? -32.044 -12.065 38.791  1.00 96.22  ? 1457 ARG A O     1 
ATOM   1875 C  CB    . ARG A 1 240 ? -33.411 -14.878 38.241  1.00 94.45  ? 1457 ARG A CB    1 
ATOM   1876 C  CG    . ARG A 1 240 ? -34.691 -15.626 37.929  1.00 99.16  ? 1457 ARG A CG    1 
ATOM   1877 C  CD    . ARG A 1 240 ? -34.884 -16.856 38.795  1.00 103.74 ? 1457 ARG A CD    1 
ATOM   1878 N  NE    . ARG A 1 240 ? -36.187 -17.475 38.563  1.00 110.76 ? 1457 ARG A NE    1 
ATOM   1879 C  CZ    . ARG A 1 240 ? -37.313 -17.111 39.175  1.00 113.21 ? 1457 ARG A CZ    1 
ATOM   1880 N  NH1   . ARG A 1 240 ? -37.302 -16.119 40.061  1.00 114.39 ? 1457 ARG A NH1   1 
ATOM   1881 N  NH2   . ARG A 1 240 ? -38.452 -17.738 38.898  1.00 107.67 ? 1457 ARG A NH2   1 
ATOM   1882 N  N     . MET A 1 241 ? -30.889 -13.114 37.168  1.00 86.91  ? 1458 MET A N     1 
ATOM   1883 C  CA    . MET A 1 241 ? -29.674 -12.361 37.466  1.00 94.84  ? 1458 MET A CA    1 
ATOM   1884 C  C     . MET A 1 241 ? -29.820 -10.887 37.105  1.00 97.28  ? 1458 MET A C     1 
ATOM   1885 O  O     . MET A 1 241 ? -29.523 -10.003 37.916  1.00 100.10 ? 1458 MET A O     1 
ATOM   1886 C  CB    . MET A 1 241 ? -28.499 -12.976 36.719  1.00 102.11 ? 1458 MET A CB    1 
ATOM   1887 C  CG    . MET A 1 241 ? -28.005 -14.236 37.373  1.00 114.35 ? 1458 MET A CG    1 
ATOM   1888 S  SD    . MET A 1 241 ? -26.242 -14.455 37.152  1.00 120.34 ? 1458 MET A SD    1 
ATOM   1889 C  CE    . MET A 1 241 ? -26.075 -14.081 35.416  1.00 115.69 ? 1458 MET A CE    1 
ATOM   1890 N  N     . PHE A 1 242 ? -30.340 -10.608 35.917  1.00 95.94  ? 1459 PHE A N     1 
ATOM   1891 C  CA    . PHE A 1 242 ? -30.328 -9.285  35.322  1.00 92.93  ? 1459 PHE A CA    1 
ATOM   1892 C  C     . PHE A 1 242 ? -31.678 -8.583  35.400  1.00 96.69  ? 1459 PHE A C     1 
ATOM   1893 O  O     . PHE A 1 242 ? -31.852 -7.531  34.778  1.00 93.55  ? 1459 PHE A O     1 
ATOM   1894 C  CB    . PHE A 1 242 ? -29.860 -9.390  33.866  1.00 83.25  ? 1459 PHE A CB    1 
ATOM   1895 C  CG    . PHE A 1 242 ? -28.378 -9.529  33.734  1.00 84.02  ? 1459 PHE A CG    1 
ATOM   1896 C  CD1   . PHE A 1 242 ? -27.575 -8.406  33.574  1.00 92.40  ? 1459 PHE A CD1   1 
ATOM   1897 C  CD2   . PHE A 1 242 ? -27.778 -10.767 33.808  1.00 83.11  ? 1459 PHE A CD2   1 
ATOM   1898 C  CE1   . PHE A 1 242 ? -26.195 -8.519  33.479  1.00 94.75  ? 1459 PHE A CE1   1 
ATOM   1899 C  CE2   . PHE A 1 242 ? -26.400 -10.894 33.708  1.00 87.36  ? 1459 PHE A CE2   1 
ATOM   1900 C  CZ    . PHE A 1 242 ? -25.606 -9.766  33.545  1.00 92.35  ? 1459 PHE A CZ    1 
ATOM   1901 N  N     . ASP A 1 243 ? -32.616 -9.113  36.180  1.00 103.19 ? 1460 ASP A N     1 
ATOM   1902 C  CA    . ASP A 1 243 ? -33.929 -8.500  36.368  1.00 113.86 ? 1460 ASP A CA    1 
ATOM   1903 C  C     . ASP A 1 243 ? -34.540 -8.143  35.024  1.00 110.54 ? 1460 ASP A C     1 
ATOM   1904 O  O     . ASP A 1 243 ? -34.885 -6.995  34.736  1.00 118.84 ? 1460 ASP A O     1 
ATOM   1905 C  CB    . ASP A 1 243 ? -33.856 -7.274  37.278  1.00 125.22 ? 1460 ASP A CB    1 
ATOM   1906 C  CG    . ASP A 1 243 ? -33.356 -7.616  38.653  1.00 135.83 ? 1460 ASP A CG    1 
ATOM   1907 O  OD1   . ASP A 1 243 ? -32.124 -7.566  38.865  1.00 141.75 ? 1460 ASP A OD1   1 
ATOM   1908 O  OD2   . ASP A 1 243 ? -34.195 -7.951  39.515  1.00 137.43 ? 1460 ASP A OD2   1 
ATOM   1909 N  N     . ILE A 1 244 ? -34.647 -9.167  34.189  1.00 101.42 ? 1461 ILE A N     1 
ATOM   1910 C  CA    . ILE A 1 244 ? -35.372 -9.061  32.936  1.00 91.06  ? 1461 ILE A CA    1 
ATOM   1911 C  C     . ILE A 1 244 ? -36.777 -9.576  33.221  1.00 98.75  ? 1461 ILE A C     1 
ATOM   1912 O  O     . ILE A 1 244 ? -37.039 -10.778 33.173  1.00 101.29 ? 1461 ILE A O     1 
ATOM   1913 C  CB    . ILE A 1 244 ? -34.678 -9.838  31.823  1.00 80.10  ? 1461 ILE A CB    1 
ATOM   1914 C  CG1   . ILE A 1 244 ? -33.162 -9.560  31.879  1.00 86.98  ? 1461 ILE A CG1   1 
ATOM   1915 C  CG2   . ILE A 1 244 ? -35.294 -9.452  30.497  1.00 58.92  ? 1461 ILE A CG2   1 
ATOM   1916 C  CD1   . ILE A 1 244 ? -32.315 -10.395 30.923  1.00 85.38  ? 1461 ILE A CD1   1 
ATOM   1917 N  N     . VAL A 1 245 ? -37.691 -8.649  33.508  1.00 101.81 ? 1462 VAL A N     1 
ATOM   1918 C  CA    . VAL A 1 245 ? -39.017 -8.988  34.002  1.00 96.26  ? 1462 VAL A CA    1 
ATOM   1919 C  C     . VAL A 1 245 ? -40.088 -8.158  33.305  1.00 92.05  ? 1462 VAL A C     1 
ATOM   1920 O  O     . VAL A 1 245 ? -39.829 -7.073  32.764  1.00 86.30  ? 1462 VAL A O     1 
ATOM   1921 C  CB    . VAL A 1 245 ? -39.089 -8.791  35.528  1.00 89.05  ? 1462 VAL A CB    1 
ATOM   1922 C  CG1   . VAL A 1 245 ? -38.244 -9.799  36.216  1.00 87.35  ? 1462 VAL A CG1   1 
ATOM   1923 C  CG2   . VAL A 1 245 ? -38.594 -7.399  35.894  1.00 81.34  ? 1462 VAL A CG2   1 
ATOM   1924 N  N     . TYR A 1 246 ? -41.296 -8.716  33.304  1.00 86.21  ? 1463 TYR A N     1 
ATOM   1925 C  CA    . TYR A 1 246 ? -42.495 -8.040  32.840  1.00 87.05  ? 1463 TYR A CA    1 
ATOM   1926 C  C     . TYR A 1 246 ? -43.627 -8.371  33.796  1.00 88.89  ? 1463 TYR A C     1 
ATOM   1927 O  O     . TYR A 1 246 ? -43.579 -9.360  34.532  1.00 82.46  ? 1463 TYR A O     1 
ATOM   1928 C  CB    . TYR A 1 246 ? -42.881 -8.442  31.406  1.00 89.63  ? 1463 TYR A CB    1 
ATOM   1929 C  CG    . TYR A 1 246 ? -43.110 -9.921  31.255  1.00 91.81  ? 1463 TYR A CG    1 
ATOM   1930 C  CD1   . TYR A 1 246 ? -44.392 -10.453 31.102  1.00 91.53  ? 1463 TYR A CD1   1 
ATOM   1931 C  CD2   . TYR A 1 246 ? -42.038 -10.800 31.286  1.00 91.24  ? 1463 TYR A CD2   1 
ATOM   1932 C  CE1   . TYR A 1 246 ? -44.589 -11.849 30.977  1.00 86.87  ? 1463 TYR A CE1   1 
ATOM   1933 C  CE2   . TYR A 1 246 ? -42.221 -12.169 31.176  1.00 92.25  ? 1463 TYR A CE2   1 
ATOM   1934 C  CZ    . TYR A 1 246 ? -43.484 -12.697 31.017  1.00 83.75  ? 1463 TYR A CZ    1 
ATOM   1935 O  OH    . TYR A 1 246 ? -43.588 -14.071 30.896  1.00 76.86  ? 1463 TYR A OH    1 
ATOM   1936 N  N     . GLU A 1 247 ? -44.642 -7.523  33.809  1.00 98.93  ? 1464 GLU A N     1 
ATOM   1937 C  CA    . GLU A 1 247 ? -45.831 -7.859  34.569  1.00 109.68 ? 1464 GLU A CA    1 
ATOM   1938 C  C     . GLU A 1 247 ? -46.652 -8.856  33.760  1.00 113.86 ? 1464 GLU A C     1 
ATOM   1939 O  O     . GLU A 1 247 ? -46.882 -8.655  32.560  1.00 108.61 ? 1464 GLU A O     1 
ATOM   1940 C  CB    . GLU A 1 247 ? -46.639 -6.613  34.908  1.00 111.14 ? 1464 GLU A CB    1 
ATOM   1941 C  CG    . GLU A 1 247 ? -47.170 -6.636  36.332  1.00 115.74 ? 1464 GLU A CG    1 
ATOM   1942 C  CD    . GLU A 1 247 ? -48.367 -5.728  36.519  1.00 120.90 ? 1464 GLU A CD    1 
ATOM   1943 O  OE1   . GLU A 1 247 ? -49.133 -5.941  37.485  1.00 123.61 ? 1464 GLU A OE1   1 
ATOM   1944 O  OE2   . GLU A 1 247 ? -48.544 -4.805  35.698  1.00 119.95 ? 1464 GLU A OE2   1 
ATOM   1945 N  N     . HIS A 1 248 ? -47.044 -9.955  34.397  1.00 119.21 ? 1465 HIS A N     1 
ATOM   1946 C  CA    . HIS A 1 248 ? -47.901 -10.911 33.719  1.00 127.05 ? 1465 HIS A CA    1 
ATOM   1947 C  C     . HIS A 1 248 ? -49.242 -10.248 33.431  1.00 124.18 ? 1465 HIS A C     1 
ATOM   1948 O  O     . HIS A 1 248 ? -49.746 -9.484  34.265  1.00 123.54 ? 1465 HIS A O     1 
ATOM   1949 C  CB    . HIS A 1 248 ? -48.103 -12.183 34.549  1.00 133.32 ? 1465 HIS A CB    1 
ATOM   1950 N  N     . PRO A 1 249 ? -49.793 -10.428 32.230  1.00 126.43 ? 1466 PRO A N     1 
ATOM   1951 C  CA    . PRO A 1 249 ? -51.074 -9.767  31.923  1.00 134.96 ? 1466 PRO A CA    1 
ATOM   1952 C  C     . PRO A 1 249 ? -52.160 -10.149 32.913  1.00 137.20 ? 1466 PRO A C     1 
ATOM   1953 O  O     . PRO A 1 249 ? -52.854 -9.273  33.450  1.00 144.02 ? 1466 PRO A O     1 
ATOM   1954 C  CB    . PRO A 1 249 ? -51.376 -10.256 30.500  1.00 134.50 ? 1466 PRO A CB    1 
ATOM   1955 C  CG    . PRO A 1 249 ? -50.032 -10.629 29.935  1.00 127.84 ? 1466 PRO A CG    1 
ATOM   1956 C  CD    . PRO A 1 249 ? -49.270 -11.193 31.088  1.00 125.09 ? 1466 PRO A CD    1 
ATOM   1957 N  N     . GLU A 1 250 ? -52.331 -11.446 33.168  1.00 124.35 ? 1467 GLU A N     1 
ATOM   1958 C  CA    . GLU A 1 250 ? -53.242 -11.872 34.223  1.00 112.34 ? 1467 GLU A CA    1 
ATOM   1959 C  C     . GLU A 1 250 ? -52.592 -11.689 35.597  1.00 113.48 ? 1467 GLU A C     1 
ATOM   1960 O  O     . GLU A 1 250 ? -52.922 -10.759 36.340  1.00 117.37 ? 1467 GLU A O     1 
ATOM   1961 C  CB    . GLU A 1 250 ? -53.668 -13.322 33.984  1.00 106.67 ? 1467 GLU A CB    1 
ATOM   1962 N  N     . THR A 1 251 ? -51.613 -12.539 35.915  1.00 109.69 ? 1468 THR A N     1 
ATOM   1963 C  CA    . THR A 1 251 ? -50.949 -12.510 37.214  1.00 116.44 ? 1468 THR A CA    1 
ATOM   1964 C  C     . THR A 1 251 ? -50.283 -11.169 37.484  1.00 134.18 ? 1468 THR A C     1 
ATOM   1965 O  O     . THR A 1 251 ? -49.542 -10.644 36.651  1.00 145.63 ? 1468 THR A O     1 
ATOM   1966 C  CB    . THR A 1 251 ? -49.896 -13.619 37.295  1.00 108.60 ? 1468 THR A CB    1 
ATOM   1967 N  N     . LYS A 1 252 ? -50.571 -10.590 38.646  1.00 137.74 ? 1469 LYS A N     1 
ATOM   1968 C  CA    . LYS A 1 252 ? -49.959 -9.307  38.964  1.00 138.41 ? 1469 LYS A CA    1 
ATOM   1969 C  C     . LYS A 1 252 ? -48.463 -9.447  39.241  1.00 136.50 ? 1469 LYS A C     1 
ATOM   1970 O  O     . LYS A 1 252 ? -47.728 -8.463  39.119  1.00 133.54 ? 1469 LYS A O     1 
ATOM   1971 C  CB    . LYS A 1 252 ? -50.658 -8.678  40.174  1.00 142.34 ? 1469 LYS A CB    1 
ATOM   1972 N  N     . GLU A 1 253 ? -47.997 -10.662 39.539  1.00 132.56 ? 1470 GLU A N     1 
ATOM   1973 C  CA    . GLU A 1 253 ? -46.630 -10.922 39.976  1.00 120.85 ? 1470 GLU A CA    1 
ATOM   1974 C  C     . GLU A 1 253 ? -45.617 -10.766 38.845  1.00 111.89 ? 1470 GLU A C     1 
ATOM   1975 O  O     . GLU A 1 253 ? -45.935 -10.946 37.667  1.00 111.15 ? 1470 GLU A O     1 
ATOM   1976 C  CB    . GLU A 1 253 ? -46.532 -12.325 40.573  1.00 120.11 ? 1470 GLU A CB    1 
ATOM   1977 N  N     . LYS A 1 254 ? -44.401 -10.350 39.224  1.00 108.30 ? 1471 LYS A N     1 
ATOM   1978 C  CA    . LYS A 1 254 ? -43.278 -10.215 38.294  1.00 96.59  ? 1471 LYS A CA    1 
ATOM   1979 C  C     . LYS A 1 254 ? -42.951 -11.543 37.636  1.00 107.64 ? 1471 LYS A C     1 
ATOM   1980 O  O     . LYS A 1 254 ? -42.868 -12.579 38.306  1.00 111.53 ? 1471 LYS A O     1 
ATOM   1981 C  CB    . LYS A 1 254 ? -42.029 -9.703  39.023  1.00 86.00  ? 1471 LYS A CB    1 
ATOM   1982 N  N     . GLU A 1 255 ? -42.786 -11.524 36.317  1.00 108.07 ? 1472 GLU A N     1 
ATOM   1983 C  CA    . GLU A 1 255 ? -42.434 -12.715 35.562  1.00 104.36 ? 1472 GLU A CA    1 
ATOM   1984 C  C     . GLU A 1 255 ? -41.090 -12.510 34.893  1.00 103.99 ? 1472 GLU A C     1 
ATOM   1985 O  O     . GLU A 1 255 ? -40.855 -11.463 34.275  1.00 110.15 ? 1472 GLU A O     1 
ATOM   1986 C  CB    . GLU A 1 255 ? -43.497 -13.046 34.516  1.00 101.91 ? 1472 GLU A CB    1 
ATOM   1987 C  CG    . GLU A 1 255 ? -44.842 -13.307 35.131  1.00 104.52 ? 1472 GLU A CG    1 
ATOM   1988 C  CD    . GLU A 1 255 ? -44.839 -14.565 35.977  1.00 115.81 ? 1472 GLU A CD    1 
ATOM   1989 O  OE1   . GLU A 1 255 ? -43.872 -15.361 35.873  1.00 119.31 ? 1472 GLU A OE1   1 
ATOM   1990 O  OE2   . GLU A 1 255 ? -45.803 -14.754 36.752  1.00 121.28 ? 1472 GLU A OE2   1 
ATOM   1991 N  N     . TYR A 1 256 ? -40.218 -13.508 35.026  1.00 101.25 ? 1473 TYR A N     1 
ATOM   1992 C  CA    . TYR A 1 256 ? -38.905 -13.514 34.396  1.00 94.40  ? 1473 TYR A CA    1 
ATOM   1993 C  C     . TYR A 1 256 ? -38.997 -14.199 33.046  1.00 94.11  ? 1473 TYR A C     1 
ATOM   1994 O  O     . TYR A 1 256 ? -39.745 -15.167 32.874  1.00 103.66 ? 1473 TYR A O     1 
ATOM   1995 C  CB    . TYR A 1 256 ? -37.874 -14.239 35.262  1.00 94.07  ? 1473 TYR A CB    1 
ATOM   1996 C  CG    . TYR A 1 256 ? -37.691 -13.579 36.590  1.00 100.16 ? 1473 TYR A CG    1 
ATOM   1997 C  CD1   . TYR A 1 256 ? -38.572 -13.840 37.630  1.00 103.65 ? 1473 TYR A CD1   1 
ATOM   1998 C  CD2   . TYR A 1 256 ? -36.652 -12.679 36.806  1.00 105.61 ? 1473 TYR A CD2   1 
ATOM   1999 C  CE1   . TYR A 1 256 ? -38.431 -13.231 38.847  1.00 109.26 ? 1473 TYR A CE1   1 
ATOM   2000 C  CE2   . TYR A 1 256 ? -36.499 -12.058 38.031  1.00 111.98 ? 1473 TYR A CE2   1 
ATOM   2001 C  CZ    . TYR A 1 256 ? -37.399 -12.340 39.046  1.00 116.06 ? 1473 TYR A CZ    1 
ATOM   2002 O  OH    . TYR A 1 256 ? -37.270 -11.745 40.273  1.00 124.83 ? 1473 TYR A OH    1 
ATOM   2003 N  N     . VAL A 1 257 ? -38.235 -13.693 32.087  1.00 81.20  ? 1474 VAL A N     1 
ATOM   2004 C  CA    . VAL A 1 257 ? -38.251 -14.265 30.749  1.00 82.68  ? 1474 VAL A CA    1 
ATOM   2005 C  C     . VAL A 1 257 ? -37.442 -15.567 30.719  1.00 85.90  ? 1474 VAL A C     1 
ATOM   2006 O  O     . VAL A 1 257 ? -36.750 -15.899 31.689  1.00 87.73  ? 1474 VAL A O     1 
ATOM   2007 C  CB    . VAL A 1 257 ? -37.719 -13.232 29.746  1.00 70.88  ? 1474 VAL A CB    1 
ATOM   2008 C  CG1   . VAL A 1 257 ? -38.595 -12.014 29.795  1.00 74.94  ? 1474 VAL A CG1   1 
ATOM   2009 C  CG2   . VAL A 1 257 ? -36.274 -12.873 30.082  1.00 59.47  ? 1474 VAL A CG2   1 
ATOM   2010 N  N     . PHE A 1 258 ? -37.581 -16.340 29.638  1.00 77.54  ? 1475 PHE A N     1 
ATOM   2011 C  CA    . PHE A 1 258 ? -36.813 -17.559 29.387  1.00 79.40  ? 1475 PHE A CA    1 
ATOM   2012 C  C     . PHE A 1 258 ? -35.860 -17.293 28.232  1.00 78.72  ? 1475 PHE A C     1 
ATOM   2013 O  O     . PHE A 1 258 ? -36.291 -16.881 27.153  1.00 75.16  ? 1475 PHE A O     1 
ATOM   2014 C  CB    . PHE A 1 258 ? -37.712 -18.745 29.031  1.00 80.02  ? 1475 PHE A CB    1 
ATOM   2015 C  CG    . PHE A 1 258 ? -38.544 -19.248 30.175  1.00 86.03  ? 1475 PHE A CG    1 
ATOM   2016 C  CD1   . PHE A 1 258 ? -38.028 -20.166 31.069  1.00 90.32  ? 1475 PHE A CD1   1 
ATOM   2017 C  CD2   . PHE A 1 258 ? -39.847 -18.818 30.345  1.00 80.97  ? 1475 PHE A CD2   1 
ATOM   2018 C  CE1   . PHE A 1 258 ? -38.789 -20.635 32.117  1.00 88.32  ? 1475 PHE A CE1   1 
ATOM   2019 C  CE2   . PHE A 1 258 ? -40.608 -19.278 31.388  1.00 84.66  ? 1475 PHE A CE2   1 
ATOM   2020 C  CZ    . PHE A 1 258 ? -40.078 -20.188 32.279  1.00 88.80  ? 1475 PHE A CZ    1 
ATOM   2021 N  N     . GLN A 1 259 ? -34.577 -17.539 28.445  1.00 83.88  ? 1476 GLN A N     1 
ATOM   2022 C  CA    . GLN A 1 259 ? -33.566 -17.149 27.479  1.00 81.73  ? 1476 GLN A CA    1 
ATOM   2023 C  C     . GLN A 1 259 ? -32.859 -18.363 26.887  1.00 68.32  ? 1476 GLN A C     1 
ATOM   2024 O  O     . GLN A 1 259 ? -32.767 -19.423 27.524  1.00 66.57  ? 1476 GLN A O     1 
ATOM   2025 C  CB    . GLN A 1 259 ? -32.546 -16.202 28.115  1.00 83.60  ? 1476 GLN A CB    1 
ATOM   2026 C  CG    . GLN A 1 259 ? -33.166 -14.945 28.702  1.00 81.70  ? 1476 GLN A CG    1 
ATOM   2027 C  CD    . GLN A 1 259 ? -32.146 -14.100 29.448  1.00 77.11  ? 1476 GLN A CD    1 
ATOM   2028 O  OE1   . GLN A 1 259 ? -32.093 -14.104 30.681  1.00 84.72  ? 1476 GLN A OE1   1 
ATOM   2029 N  NE2   . GLN A 1 259 ? -31.317 -13.385 28.699  1.00 63.40  ? 1476 GLN A NE2   1 
ATOM   2030 N  N     . ASN A 1 260 ? -32.438 -18.193 25.624  1.00 64.92  ? 1477 ASN A N     1 
ATOM   2031 C  CA    . ASN A 1 260 ? -31.495 -19.067 24.929  1.00 68.09  ? 1477 ASN A CA    1 
ATOM   2032 C  C     . ASN A 1 260 ? -30.342 -18.245 24.385  1.00 72.38  ? 1477 ASN A C     1 
ATOM   2033 O  O     . ASN A 1 260 ? -30.486 -17.045 24.127  1.00 85.36  ? 1477 ASN A O     1 
ATOM   2034 C  CB    . ASN A 1 260 ? -32.076 -19.791 23.736  1.00 63.16  ? 1477 ASN A CB    1 
ATOM   2035 C  CG    . ASN A 1 260 ? -33.314 -20.544 24.056  1.00 63.03  ? 1477 ASN A CG    1 
ATOM   2036 O  OD1   . ASN A 1 260 ? -33.539 -21.007 25.183  1.00 64.89  ? 1477 ASN A OD1   1 
ATOM   2037 N  ND2   . ASN A 1 260 ? -34.142 -20.695 23.048  1.00 65.69  ? 1477 ASN A ND2   1 
ATOM   2038 N  N     . SER A 1 261 ? -29.195 -18.905 24.203  1.00 70.72  ? 1478 SER A N     1 
ATOM   2039 C  CA    . SER A 1 261 ? -28.099 -18.343 23.423  1.00 74.03  ? 1478 SER A CA    1 
ATOM   2040 C  C     . SER A 1 261 ? -27.473 -19.445 22.582  1.00 68.28  ? 1478 SER A C     1 
ATOM   2041 O  O     . SER A 1 261 ? -27.522 -20.624 22.930  1.00 70.68  ? 1478 SER A O     1 
ATOM   2042 C  CB    . SER A 1 261 ? -27.029 -17.663 24.299  1.00 76.67  ? 1478 SER A CB    1 
ATOM   2043 O  OG    . SER A 1 261 ? -26.145 -18.598 24.890  1.00 82.80  ? 1478 SER A OG    1 
ATOM   2044 N  N     . TRP A 1 262 ? -26.932 -19.054 21.438  1.00 57.40  ? 1479 TRP A N     1 
ATOM   2045 C  CA    . TRP A 1 262 ? -26.391 -20.047 20.520  1.00 60.05  ? 1479 TRP A CA    1 
ATOM   2046 C  C     . TRP A 1 262 ? -25.319 -19.390 19.660  1.00 64.76  ? 1479 TRP A C     1 
ATOM   2047 O  O     . TRP A 1 262 ? -25.360 -18.178 19.412  1.00 62.03  ? 1479 TRP A O     1 
ATOM   2048 C  CB    . TRP A 1 262 ? -27.508 -20.682 19.659  1.00 51.02  ? 1479 TRP A CB    1 
ATOM   2049 C  CG    . TRP A 1 262 ? -28.723 -19.791 19.442  1.00 64.01  ? 1479 TRP A CG    1 
ATOM   2050 C  CD1   . TRP A 1 262 ? -29.808 -19.653 20.272  1.00 72.93  ? 1479 TRP A CD1   1 
ATOM   2051 C  CD2   . TRP A 1 262 ? -28.970 -18.921 18.325  1.00 54.42  ? 1479 TRP A CD2   1 
ATOM   2052 N  NE1   . TRP A 1 262 ? -30.701 -18.762 19.738  1.00 63.80  ? 1479 TRP A NE1   1 
ATOM   2053 C  CE2   . TRP A 1 262 ? -30.211 -18.302 18.543  1.00 61.38  ? 1479 TRP A CE2   1 
ATOM   2054 C  CE3   . TRP A 1 262 ? -28.267 -18.620 17.159  1.00 59.70  ? 1479 TRP A CE3   1 
ATOM   2055 C  CZ2   . TRP A 1 262 ? -30.763 -17.402 17.635  1.00 64.00  ? 1479 TRP A CZ2   1 
ATOM   2056 C  CZ3   . TRP A 1 262 ? -28.807 -17.711 16.267  1.00 69.95  ? 1479 TRP A CZ3   1 
ATOM   2057 C  CH2   . TRP A 1 262 ? -30.038 -17.116 16.506  1.00 66.55  ? 1479 TRP A CH2   1 
ATOM   2058 N  N     . GLY A 1 263 ? -24.364 -20.189 19.193  1.00 68.89  ? 1480 GLY A N     1 
ATOM   2059 C  CA    . GLY A 1 263 ? -23.215 -19.620 18.512  1.00 68.15  ? 1480 GLY A CA    1 
ATOM   2060 C  C     . GLY A 1 263 ? -22.531 -20.607 17.598  1.00 57.23  ? 1480 GLY A C     1 
ATOM   2061 O  O     . GLY A 1 263 ? -22.511 -21.816 17.858  1.00 63.55  ? 1480 GLY A O     1 
ATOM   2062 N  N     . ILE A 1 264 ? -21.919 -20.080 16.540  1.00 59.22  ? 1481 ILE A N     1 
ATOM   2063 C  CA    . ILE A 1 264 ? -21.052 -20.938 15.716  1.00 53.94  ? 1481 ILE A CA    1 
ATOM   2064 C  C     . ILE A 1 264 ? -19.928 -20.092 15.141  1.00 54.25  ? 1481 ILE A C     1 
ATOM   2065 O  O     . ILE A 1 264 ? -20.140 -18.934 14.755  1.00 61.24  ? 1481 ILE A O     1 
ATOM   2066 C  CB    . ILE A 1 264 ? -21.826 -21.702 14.615  1.00 53.75  ? 1481 ILE A CB    1 
ATOM   2067 C  CG1   . ILE A 1 264 ? -20.946 -22.773 13.977  1.00 58.07  ? 1481 ILE A CG1   1 
ATOM   2068 C  CG2   . ILE A 1 264 ? -22.355 -20.783 13.518  1.00 50.86  ? 1481 ILE A CG2   1 
ATOM   2069 C  CD1   . ILE A 1 264 ? -21.647 -23.520 12.828  1.00 56.67  ? 1481 ILE A CD1   1 
ATOM   2070 N  N     . THR A 1 265 ? -18.727 -20.691 15.090  1.00 55.97  ? 1482 THR A N     1 
ATOM   2071 C  CA    . THR A 1 265 ? -17.446 -20.008 14.899  1.00 53.75  ? 1482 THR A CA    1 
ATOM   2072 C  C     . THR A 1 265 ? -16.728 -20.511 13.650  1.00 57.37  ? 1482 THR A C     1 
ATOM   2073 O  O     . THR A 1 265 ? -17.180 -21.422 12.964  1.00 63.57  ? 1482 THR A O     1 
ATOM   2074 C  CB    . THR A 1 265 ? -16.538 -20.200 16.118  1.00 54.81  ? 1482 THR A CB    1 
ATOM   2075 O  OG1   . THR A 1 265 ? -15.756 -21.394 15.963  1.00 61.33  ? 1482 THR A OG1   1 
ATOM   2076 C  CG2   . THR A 1 265 ? -17.348 -20.288 17.408  1.00 47.99  ? 1482 THR A CG2   1 
ATOM   2077 N  N     . THR A 1 266 ? -15.585 -19.903 13.357  1.00 63.64  ? 1483 THR A N     1 
ATOM   2078 C  CA    . THR A 1 266 ? -14.811 -20.277 12.178  1.00 67.57  ? 1483 THR A CA    1 
ATOM   2079 C  C     . THR A 1 266 ? -14.015 -21.568 12.358  1.00 67.11  ? 1483 THR A C     1 
ATOM   2080 O  O     . THR A 1 266 ? -13.389 -22.044 11.397  1.00 61.39  ? 1483 THR A O     1 
ATOM   2081 C  CB    . THR A 1 266 ? -13.875 -19.127 11.805  1.00 56.46  ? 1483 THR A CB    1 
ATOM   2082 O  OG1   . THR A 1 266 ? -13.393 -18.481 12.995  1.00 66.43  ? 1483 THR A OG1   1 
ATOM   2083 C  CG2   . THR A 1 266 ? -14.591 -18.156 10.923  1.00 44.52  ? 1483 THR A CG2   1 
ATOM   2084 N  N     . ARG A 1 267 ? -14.218 -22.183 13.469  1.00 56.94  ? 1484 ARG A N     1 
ATOM   2085 C  CA    . ARG A 1 267 ? -13.654 -23.422 13.731  1.00 64.01  ? 1484 ARG A CA    1 
ATOM   2086 C  C     . ARG A 1 267 ? -14.192 -24.406 12.753  1.00 65.27  ? 1484 ARG A C     1 
ATOM   2087 O  O     . ARG A 1 267 ? -13.581 -25.374 12.524  1.00 63.71  ? 1484 ARG A O     1 
ATOM   2088 C  CB    . ARG A 1 267 ? -14.151 -23.809 15.043  1.00 73.53  ? 1484 ARG A CB    1 
ATOM   2089 C  CG    . ARG A 1 267 ? -13.779 -25.184 15.420  1.00 83.35  ? 1484 ARG A CG    1 
ATOM   2090 C  CD    . ARG A 1 267 ? -14.425 -25.516 16.721  1.00 93.16  ? 1484 ARG A CD    1 
ATOM   2091 N  NE    . ARG A 1 267 ? -14.546 -24.365 17.567  1.00 110.54 ? 1484 ARG A NE    1 
ATOM   2092 C  CZ    . ARG A 1 267 ? -14.095 -24.284 18.792  1.00 121.27 ? 1484 ARG A CZ    1 
ATOM   2093 N  NH1   . ARG A 1 267 ? -13.503 -25.310 19.348  1.00 122.08 ? 1484 ARG A NH1   1 
ATOM   2094 N  NH2   . ARG A 1 267 ? -14.273 -23.167 19.456  1.00 118.71 ? 1484 ARG A NH2   1 
ATOM   2095 N  N     . THR A 1 268 ? -15.413 -24.214 12.320  1.00 51.07  ? 1485 THR A N     1 
ATOM   2096 C  CA    . THR A 1 268 ? -16.026 -24.986 11.247  1.00 55.64  ? 1485 THR A CA    1 
ATOM   2097 C  C     . THR A 1 268 ? -15.034 -25.250 10.117  1.00 55.41  ? 1485 THR A C     1 
ATOM   2098 O  O     . THR A 1 268 ? -14.832 -26.402 9.709   1.00 63.05  ? 1485 THR A O     1 
ATOM   2099 C  CB    . THR A 1 268 ? -17.276 -24.258 10.710  1.00 59.99  ? 1485 THR A CB    1 
ATOM   2100 O  OG1   . THR A 1 268 ? -16.933 -22.944 10.254  1.00 62.68  ? 1485 THR A OG1   1 
ATOM   2101 C  CG2   . THR A 1 268 ? -18.331 -24.121 11.776  1.00 61.61  ? 1485 THR A CG2   1 
ATOM   2102 N  N     . ILE A 1 269 ? -14.368 -24.194 9.638   1.00 51.33  ? 1486 ILE A N     1 
ATOM   2103 C  CA    . ILE A 1 269 ? -13.460 -24.330 8.498   1.00 61.86  ? 1486 ILE A CA    1 
ATOM   2104 C  C     . ILE A 1 269 ? -12.301 -25.282 8.822   1.00 63.76  ? 1486 ILE A C     1 
ATOM   2105 O  O     . ILE A 1 269 ? -11.885 -26.103 7.985   1.00 50.18  ? 1486 ILE A O     1 
ATOM   2106 C  CB    . ILE A 1 269 ? -12.959 -22.945 8.053   1.00 66.65  ? 1486 ILE A CB    1 
ATOM   2107 C  CG1   . ILE A 1 269 ? -14.120 -22.105 7.539   1.00 74.54  ? 1486 ILE A CG1   1 
ATOM   2108 C  CG2   . ILE A 1 269 ? -11.957 -23.075 6.930   1.00 60.87  ? 1486 ILE A CG2   1 
ATOM   2109 C  CD1   . ILE A 1 269 ? -13.738 -20.640 7.303   1.00 74.84  ? 1486 ILE A CD1   1 
ATOM   2110 N  N     . GLY A 1 270 ? -11.747 -25.183 10.029  1.00 69.28  ? 1487 GLY A N     1 
ATOM   2111 C  CA    . GLY A 1 270 ? -10.702 -26.123 10.401  1.00 79.48  ? 1487 GLY A CA    1 
ATOM   2112 C  C     . GLY A 1 270 ? -11.176 -27.556 10.289  1.00 83.42  ? 1487 GLY A C     1 
ATOM   2113 O  O     . GLY A 1 270 ? -10.525 -28.399 9.654   1.00 79.30  ? 1487 GLY A O     1 
ATOM   2114 N  N     . VAL A 1 271 ? -12.362 -27.830 10.846  1.00 82.75  ? 1488 VAL A N     1 
ATOM   2115 C  CA    . VAL A 1 271 ? -12.936 -29.163 10.722  1.00 72.15  ? 1488 VAL A CA    1 
ATOM   2116 C  C     . VAL A 1 271 ? -13.004 -29.561 9.257   1.00 59.61  ? 1488 VAL A C     1 
ATOM   2117 O  O     . VAL A 1 271 ? -12.562 -30.652 8.878   1.00 55.45  ? 1488 VAL A O     1 
ATOM   2118 C  CB    . VAL A 1 271 ? -14.309 -29.235 11.406  1.00 72.53  ? 1488 VAL A CB    1 
ATOM   2119 C  CG1   . VAL A 1 271 ? -14.735 -30.694 11.544  1.00 65.42  ? 1488 VAL A CG1   1 
ATOM   2120 C  CG2   . VAL A 1 271 ? -14.255 -28.540 12.767  1.00 72.01  ? 1488 VAL A CG2   1 
ATOM   2121 N  N     . MET A 1 272 ? -13.448 -28.688 8.414   1.00 57.49  ? 1489 MET A N     1 
ATOM   2122 C  CA    . MET A 1 272 ? -13.535 -28.970 7.018   1.00 59.73  ? 1489 MET A CA    1 
ATOM   2123 C  C     . MET A 1 272 ? -12.225 -29.377 6.403   1.00 52.86  ? 1489 MET A C     1 
ATOM   2124 O  O     . MET A 1 272 ? -12.179 -30.213 5.616   1.00 64.60  ? 1489 MET A O     1 
ATOM   2125 C  CB    . MET A 1 272 ? -14.133 -27.786 6.330   1.00 55.87  ? 1489 MET A CB    1 
ATOM   2126 C  CG    . MET A 1 272 ? -14.159 -27.884 4.843   1.00 64.35  ? 1489 MET A CG    1 
ATOM   2127 S  SD    . MET A 1 272 ? -13.913 -26.296 4.144   1.00 69.35  ? 1489 MET A SD    1 
ATOM   2128 C  CE    . MET A 1 272 ? -13.859 -26.675 2.466   1.00 57.52  ? 1489 MET A CE    1 
ATOM   2129 N  N     . ILE A 1 273 ? -11.163 -28.731 6.748   1.00 48.39  ? 1490 ILE A N     1 
ATOM   2130 C  CA    . ILE A 1 273 ? -9.810  -29.134 6.353   1.00 57.46  ? 1490 ILE A CA    1 
ATOM   2131 C  C     . ILE A 1 273 ? -9.483  -30.527 6.892   1.00 66.75  ? 1490 ILE A C     1 
ATOM   2132 O  O     . ILE A 1 273 ? -9.204  -31.468 6.127   1.00 61.43  ? 1490 ILE A O     1 
ATOM   2133 C  CB    . ILE A 1 273 ? -8.781  -28.094 6.830   1.00 64.59  ? 1490 ILE A CB    1 
ATOM   2134 C  CG1   . ILE A 1 273 ? -9.036  -26.740 6.149   1.00 72.49  ? 1490 ILE A CG1   1 
ATOM   2135 C  CG2   . ILE A 1 273 ? -7.359  -28.569 6.567   1.00 59.73  ? 1490 ILE A CG2   1 
ATOM   2136 C  CD1   . ILE A 1 273 ? -8.497  -25.550 6.963   1.00 73.28  ? 1490 ILE A CD1   1 
ATOM   2137 N  N     . MET A 1 274 ? -9.567  -30.691 8.222   1.00 72.46  ? 1491 MET A N     1 
ATOM   2138 C  CA    . MET A 1 274 ? -9.108  -31.936 8.826   1.00 65.50  ? 1491 MET A CA    1 
ATOM   2139 C  C     . MET A 1 274 ? -9.857  -33.111 8.251   1.00 66.68  ? 1491 MET A C     1 
ATOM   2140 O  O     . MET A 1 274 ? -9.312  -34.222 8.172   1.00 59.10  ? 1491 MET A O     1 
ATOM   2141 C  CB    . MET A 1 274 ? -9.338  -31.935 10.336  1.00 59.54  ? 1491 MET A CB    1 
ATOM   2142 C  CG    . MET A 1 274 ? -8.460  -31.017 11.126  1.00 61.76  ? 1491 MET A CG    1 
ATOM   2143 S  SD    . MET A 1 274 ? -6.751  -31.338 10.771  1.00 60.27  ? 1491 MET A SD    1 
ATOM   2144 C  CE    . MET A 1 274 ? -6.014  -30.789 12.294  1.00 60.38  ? 1491 MET A CE    1 
ATOM   2145 N  N     . VAL A 1 275 ? -11.093 -32.878 7.813   1.00 60.90  ? 1492 VAL A N     1 
ATOM   2146 C  CA    . VAL A 1 275 ? -11.904 -33.987 7.349   1.00 52.98  ? 1492 VAL A CA    1 
ATOM   2147 C  C     . VAL A 1 275 ? -11.693 -34.218 5.867   1.00 66.91  ? 1492 VAL A C     1 
ATOM   2148 O  O     . VAL A 1 275 ? -11.590 -35.362 5.426   1.00 80.18  ? 1492 VAL A O     1 
ATOM   2149 C  CB    . VAL A 1 275 ? -13.389 -33.728 7.686   1.00 54.33  ? 1492 VAL A CB    1 
ATOM   2150 C  CG1   . VAL A 1 275 ? -14.347 -34.696 6.914   1.00 44.22  ? 1492 VAL A CG1   1 
ATOM   2151 C  CG2   . VAL A 1 275 ? -13.598 -33.797 9.179   1.00 50.43  ? 1492 VAL A CG2   1 
ATOM   2152 N  N     . HIS A 1 276 ? -11.554 -33.149 5.077   1.00 59.82  ? 1493 HIS A N     1 
ATOM   2153 C  CA    . HIS A 1 276 ? -11.734 -33.308 3.644   1.00 53.66  ? 1493 HIS A CA    1 
ATOM   2154 C  C     . HIS A 1 276 ? -10.469 -33.112 2.848   1.00 58.82  ? 1493 HIS A C     1 
ATOM   2155 O  O     . HIS A 1 276 ? -10.435 -33.488 1.675   1.00 71.16  ? 1493 HIS A O     1 
ATOM   2156 C  CB    . HIS A 1 276 ? -12.808 -32.350 3.130   1.00 68.02  ? 1493 HIS A CB    1 
ATOM   2157 C  CG    . HIS A 1 276 ? -14.197 -32.701 3.571   1.00 66.88  ? 1493 HIS A CG    1 
ATOM   2158 N  ND1   . HIS A 1 276 ? -14.819 -33.873 3.212   1.00 68.67  ? 1493 HIS A ND1   1 
ATOM   2159 C  CD2   . HIS A 1 276 ? -15.088 -32.019 4.329   1.00 70.17  ? 1493 HIS A CD2   1 
ATOM   2160 C  CE1   . HIS A 1 276 ? -16.030 -33.901 3.733   1.00 70.94  ? 1493 HIS A CE1   1 
ATOM   2161 N  NE2   . HIS A 1 276 ? -16.218 -32.787 4.418   1.00 65.95  ? 1493 HIS A NE2   1 
ATOM   2162 N  N     . ALA A 1 277 ? -9.464  -32.475 3.427   1.00 51.76  ? 1494 ALA A N     1 
ATOM   2163 C  CA    . ALA A 1 277 ? -8.241  -32.196 2.700   1.00 61.14  ? 1494 ALA A CA    1 
ATOM   2164 C  C     . ALA A 1 277 ? -7.389  -33.468 2.643   1.00 72.38  ? 1494 ALA A C     1 
ATOM   2165 O  O     . ALA A 1 277 ? -7.192  -34.150 3.658   1.00 72.55  ? 1494 ALA A O     1 
ATOM   2166 C  CB    . ALA A 1 277 ? -7.504  -31.024 3.361   1.00 44.55  ? 1494 ALA A CB    1 
ATOM   2167 N  N     . ASP A 1 278 ? -6.875  -33.787 1.461   1.00 73.55  ? 1495 ASP A N     1 
ATOM   2168 C  CA    . ASP A 1 278 ? -6.089  -34.994 1.340   1.00 62.60  ? 1495 ASP A CA    1 
ATOM   2169 C  C     . ASP A 1 278 ? -4.603  -34.638 1.227   1.00 66.45  ? 1495 ASP A C     1 
ATOM   2170 O  O     . ASP A 1 278 ? -4.182  -33.522 1.574   1.00 64.83  ? 1495 ASP A O     1 
ATOM   2171 C  CB    . ASP A 1 278 ? -6.622  -35.833 0.165   1.00 60.97  ? 1495 ASP A CB    1 
ATOM   2172 C  CG    . ASP A 1 278 ? -6.485  -35.141 -1.196  1.00 68.43  ? 1495 ASP A CG    1 
ATOM   2173 O  OD1   . ASP A 1 278 ? -5.676  -34.199 -1.329  1.00 68.20  ? 1495 ASP A OD1   1 
ATOM   2174 O  OD2   . ASP A 1 278 ? -7.184  -35.567 -2.150  1.00 68.40  ? 1495 ASP A OD2   1 
ATOM   2175 N  N     . ASN A 1 279 ? -3.811  -35.579 0.727   1.00 76.82  ? 1496 ASN A N     1 
ATOM   2176 C  CA    . ASN A 1 279 ? -2.373  -35.383 0.655   1.00 74.73  ? 1496 ASN A CA    1 
ATOM   2177 C  C     . ASN A 1 279 ? -1.958  -34.563 -0.565  1.00 71.33  ? 1496 ASN A C     1 
ATOM   2178 O  O     . ASN A 1 279 ? -0.773  -34.308 -0.768  1.00 55.28  ? 1496 ASN A O     1 
ATOM   2179 C  CB    . ASN A 1 279 ? -1.668  -36.742 0.698   1.00 62.36  ? 1496 ASN A CB    1 
ATOM   2180 C  CG    . ASN A 1 279 ? -1.488  -37.248 2.137   1.00 72.43  ? 1496 ASN A CG    1 
ATOM   2181 O  OD1   . ASN A 1 279 ? -1.589  -36.473 3.092   1.00 74.33  ? 1496 ASN A OD1   1 
ATOM   2182 N  ND2   . ASN A 1 279 ? -1.200  -38.539 2.293   1.00 75.89  ? 1496 ASN A ND2   1 
ATOM   2183 N  N     . GLN A 1 280 ? -2.880  -34.173 -1.389  1.00 71.34  ? 1497 GLN A N     1 
ATOM   2184 C  CA    . GLN A 1 280 ? -2.522  -33.318 -2.460  1.00 63.89  ? 1497 GLN A CA    1 
ATOM   2185 C  C     . GLN A 1 280 ? -2.989  -31.959 -2.169  1.00 76.28  ? 1497 GLN A C     1 
ATOM   2186 O  O     . GLN A 1 280 ? -2.879  -31.153 -3.002  1.00 88.96  ? 1497 GLN A O     1 
ATOM   2187 C  CB    . GLN A 1 280 ? -3.174  -33.703 -3.735  1.00 68.41  ? 1497 GLN A CB    1 
ATOM   2188 N  N     . GLY A 1 281 ? -3.559  -31.681 -1.018  1.00 78.61  ? 1498 GLY A N     1 
ATOM   2189 C  CA    . GLY A 1 281 ? -4.037  -30.358 -0.767  1.00 73.11  ? 1498 GLY A CA    1 
ATOM   2190 C  C     . GLY A 1 281 ? -5.466  -30.348 -0.339  1.00 77.33  ? 1498 GLY A C     1 
ATOM   2191 O  O     . GLY A 1 281 ? -6.019  -31.330 -0.016  1.00 79.36  ? 1498 GLY A O     1 
ATOM   2192 N  N     . LEU A 1 282 ? -6.079  -29.187 -0.378  1.00 79.65  ? 1499 LEU A N     1 
ATOM   2193 C  CA    . LEU A 1 282 ? -7.452  -29.012 0.015   1.00 73.58  ? 1499 LEU A CA    1 
ATOM   2194 C  C     . LEU A 1 282 ? -8.449  -29.598 -0.867  1.00 70.51  ? 1499 LEU A C     1 
ATOM   2195 O  O     . LEU A 1 282 ? -8.254  -29.728 -2.020  1.00 71.27  ? 1499 LEU A O     1 
ATOM   2196 C  CB    . LEU A 1 282 ? -7.810  -27.581 -0.090  1.00 67.35  ? 1499 LEU A CB    1 
ATOM   2197 C  CG    . LEU A 1 282 ? -7.248  -26.573 0.811   1.00 63.68  ? 1499 LEU A CG    1 
ATOM   2198 C  CD1   . LEU A 1 282 ? -7.448  -25.359 -0.008  1.00 68.37  ? 1499 LEU A CD1   1 
ATOM   2199 C  CD2   . LEU A 1 282 ? -8.072  -26.522 2.049   1.00 56.04  ? 1499 LEU A CD2   1 
ATOM   2200 N  N     . VAL A 1 283 ? -9.566  -29.954 -0.289  1.00 69.36  ? 1500 VAL A N     1 
ATOM   2201 C  CA    . VAL A 1 283 ? -10.682 -30.479 -1.028  1.00 64.23  ? 1500 VAL A CA    1 
ATOM   2202 C  C     . VAL A 1 283 ? -11.905 -29.770 -0.501  1.00 65.62  ? 1500 VAL A C     1 
ATOM   2203 O  O     . VAL A 1 283 ? -12.264 -30.016 0.589   1.00 62.30  ? 1500 VAL A O     1 
ATOM   2204 C  CB    . VAL A 1 283 ? -10.851 -31.928 -0.777  1.00 58.46  ? 1500 VAL A CB    1 
ATOM   2205 C  CG1   . VAL A 1 283 ? -12.048 -32.375 -1.509  1.00 67.37  ? 1500 VAL A CG1   1 
ATOM   2206 C  CG2   . VAL A 1 283 ? -9.687  -32.691 -1.296  1.00 47.02  ? 1500 VAL A CG2   1 
ATOM   2207 N  N     . LEU A 1 284 ? -12.550 -28.913 -1.295  1.00 66.13  ? 1501 LEU A N     1 
ATOM   2208 C  CA    . LEU A 1 284 ? -13.636 -28.055 -0.824  1.00 71.99  ? 1501 LEU A CA    1 
ATOM   2209 C  C     . LEU A 1 284 ? -14.997 -28.720 -1.039  1.00 65.46  ? 1501 LEU A C     1 
ATOM   2210 O  O     . LEU A 1 284 ? -15.278 -29.222 -2.144  1.00 54.08  ? 1501 LEU A O     1 
ATOM   2211 C  CB    . LEU A 1 284 ? -13.602 -26.712 -1.531  1.00 72.82  ? 1501 LEU A CB    1 
ATOM   2212 C  CG    . LEU A 1 284 ? -12.345 -25.962 -1.122  1.00 66.51  ? 1501 LEU A CG    1 
ATOM   2213 C  CD1   . LEU A 1 284 ? -12.218 -24.656 -1.884  1.00 59.22  ? 1501 LEU A CD1   1 
ATOM   2214 C  CD2   . LEU A 1 284 ? -12.389 -25.730 0.372   1.00 61.71  ? 1501 LEU A CD2   1 
ATOM   2215 N  N     . PRO A 1 285 ? -15.839 -28.735 -0.011  1.00 58.80  ? 1502 PRO A N     1 
ATOM   2216 C  CA    . PRO A 1 285 ? -17.232 -29.106 -0.198  1.00 57.28  ? 1502 PRO A CA    1 
ATOM   2217 C  C     . PRO A 1 285 ? -17.849 -28.203 -1.243  1.00 59.91  ? 1502 PRO A C     1 
ATOM   2218 O  O     . PRO A 1 285 ? -17.736 -26.979 -1.135  1.00 61.01  ? 1502 PRO A O     1 
ATOM   2219 C  CB    . PRO A 1 285 ? -17.858 -28.862 1.183   1.00 54.58  ? 1502 PRO A CB    1 
ATOM   2220 C  CG    . PRO A 1 285 ? -16.742 -28.846 2.134   1.00 56.23  ? 1502 PRO A CG    1 
ATOM   2221 C  CD    . PRO A 1 285 ? -15.525 -28.383 1.382   1.00 58.84  ? 1502 PRO A CD    1 
ATOM   2222 N  N     . PRO A 1 286 ? -18.492 -28.761 -2.256  1.00 59.14  ? 1503 PRO A N     1 
ATOM   2223 C  CA    . PRO A 1 286 ? -18.980 -27.923 -3.363  1.00 62.01  ? 1503 PRO A CA    1 
ATOM   2224 C  C     . PRO A 1 286 ? -19.790 -26.702 -2.928  1.00 67.71  ? 1503 PRO A C     1 
ATOM   2225 O  O     . PRO A 1 286 ? -19.691 -25.643 -3.565  1.00 82.57  ? 1503 PRO A O     1 
ATOM   2226 C  CB    . PRO A 1 286 ? -19.823 -28.904 -4.196  1.00 71.86  ? 1503 PRO A CB    1 
ATOM   2227 C  CG    . PRO A 1 286 ? -19.288 -30.284 -3.839  1.00 70.03  ? 1503 PRO A CG    1 
ATOM   2228 C  CD    . PRO A 1 286 ? -18.838 -30.187 -2.411  1.00 65.29  ? 1503 PRO A CD    1 
ATOM   2229 N  N     . ARG A 1 287 ? -20.575 -26.806 -1.858  1.00 59.11  ? 1504 ARG A N     1 
ATOM   2230 C  CA    . ARG A 1 287 ? -21.538 -25.757 -1.535  1.00 61.63  ? 1504 ARG A CA    1 
ATOM   2231 C  C     . ARG A 1 287 ? -20.943 -24.554 -0.813  1.00 64.83  ? 1504 ARG A C     1 
ATOM   2232 O  O     . ARG A 1 287 ? -21.639 -23.542 -0.673  1.00 78.14  ? 1504 ARG A O     1 
ATOM   2233 C  CB    . ARG A 1 287 ? -22.708 -26.351 -0.737  1.00 63.29  ? 1504 ARG A CB    1 
ATOM   2234 C  CG    . ARG A 1 287 ? -23.607 -27.195 -1.651  1.00 52.39  ? 1504 ARG A CG    1 
ATOM   2235 C  CD    . ARG A 1 287 ? -24.939 -27.507 -1.068  1.00 59.43  ? 1504 ARG A CD    1 
ATOM   2236 N  NE    . ARG A 1 287 ? -25.612 -26.320 -0.584  1.00 67.70  ? 1504 ARG A NE    1 
ATOM   2237 C  CZ    . ARG A 1 287 ? -26.789 -26.343 0.015   1.00 66.46  ? 1504 ARG A CZ    1 
ATOM   2238 N  NH1   . ARG A 1 287 ? -27.419 -27.491 0.195   1.00 68.17  ? 1504 ARG A NH1   1 
ATOM   2239 N  NH2   . ARG A 1 287 ? -27.321 -25.219 0.453   1.00 69.15  ? 1504 ARG A NH2   1 
ATOM   2240 N  N     . VAL A 1 288 ? -19.687 -24.615 -0.380  1.00 59.82  ? 1505 VAL A N     1 
ATOM   2241 C  CA    . VAL A 1 288 ? -19.015 -23.472 0.228   1.00 54.78  ? 1505 VAL A CA    1 
ATOM   2242 C  C     . VAL A 1 288 ? -17.850 -22.966 -0.608  1.00 59.50  ? 1505 VAL A C     1 
ATOM   2243 O  O     . VAL A 1 288 ? -17.302 -21.887 -0.294  1.00 66.84  ? 1505 VAL A O     1 
ATOM   2244 C  CB    . VAL A 1 288 ? -18.534 -23.788 1.663   1.00 54.55  ? 1505 VAL A CB    1 
ATOM   2245 C  CG1   . VAL A 1 288 ? -19.707 -24.123 2.557   1.00 46.59  ? 1505 VAL A CG1   1 
ATOM   2246 C  CG2   . VAL A 1 288 ? -17.561 -24.923 1.652   1.00 57.65  ? 1505 VAL A CG2   1 
ATOM   2247 N  N     . ALA A 1 289 ? -17.492 -23.668 -1.681  1.00 50.32  ? 1506 ALA A N     1 
ATOM   2248 C  CA    . ALA A 1 289 ? -16.343 -23.290 -2.493  1.00 59.70  ? 1506 ALA A CA    1 
ATOM   2249 C  C     . ALA A 1 289 ? -16.637 -22.020 -3.269  1.00 69.39  ? 1506 ALA A C     1 
ATOM   2250 O  O     . ALA A 1 289 ? -17.570 -21.988 -4.077  1.00 68.95  ? 1506 ALA A O     1 
ATOM   2251 C  CB    . ALA A 1 289 ? -15.983 -24.409 -3.462  1.00 56.37  ? 1506 ALA A CB    1 
ATOM   2252 N  N     . CYS A 1 290 ? -15.809 -20.994 -3.049  1.00 77.17  ? 1507 CYS A N     1 
ATOM   2253 C  CA    . CYS A 1 290 ? -15.927 -19.752 -3.807  1.00 79.55  ? 1507 CYS A CA    1 
ATOM   2254 C  C     . CYS A 1 290 ? -16.000 -20.044 -5.304  1.00 71.29  ? 1507 CYS A C     1 
ATOM   2255 O  O     . CYS A 1 290 ? -16.863 -19.520 -6.010  1.00 69.01  ? 1507 CYS A O     1 
ATOM   2256 C  CB    . CYS A 1 290 ? -14.732 -18.842 -3.487  1.00 94.89  ? 1507 CYS A CB    1 
ATOM   2257 S  SG    . CYS A 1 290 ? -14.695 -17.204 -4.292  1.00 98.59  ? 1507 CYS A SG    1 
ATOM   2258 N  N     . ILE A 1 291 ? -15.119 -20.910 -5.800  1.00 69.15  ? 1508 ILE A N     1 
ATOM   2259 C  CA    . ILE A 1 291 ? -15.191 -21.419 -7.166  1.00 74.65  ? 1508 ILE A CA    1 
ATOM   2260 C  C     . ILE A 1 291 ? -15.576 -22.897 -7.091  1.00 78.13  ? 1508 ILE A C     1 
ATOM   2261 O  O     . ILE A 1 291 ? -14.887 -23.701 -6.450  1.00 81.20  ? 1508 ILE A O     1 
ATOM   2262 C  CB    . ILE A 1 291 ? -13.866 -21.229 -7.924  1.00 65.71  ? 1508 ILE A CB    1 
ATOM   2263 C  CG1   . ILE A 1 291 ? -13.419 -19.779 -7.838  1.00 59.18  ? 1508 ILE A CG1   1 
ATOM   2264 C  CG2   . ILE A 1 291 ? -14.035 -21.583 -9.406  1.00 62.96  ? 1508 ILE A CG2   1 
ATOM   2265 C  CD1   . ILE A 1 291 ? -12.270 -19.456 -8.779  1.00 50.94  ? 1508 ILE A CD1   1 
ATOM   2266 N  N     . GLN A 1 292 ? -16.701 -23.257 -7.699  1.00 75.27  ? 1509 GLN A N     1 
ATOM   2267 C  CA    . GLN A 1 292 ? -17.020 -24.680 -7.755  1.00 69.20  ? 1509 GLN A CA    1 
ATOM   2268 C  C     . GLN A 1 292 ? -16.339 -25.341 -8.931  1.00 65.43  ? 1509 GLN A C     1 
ATOM   2269 O  O     . GLN A 1 292 ? -15.849 -26.472 -8.817  1.00 74.30  ? 1509 GLN A O     1 
ATOM   2270 C  CB    . GLN A 1 292 ? -18.525 -24.910 -7.857  1.00 52.37  ? 1509 GLN A CB    1 
ATOM   2271 C  CG    . GLN A 1 292 ? -19.281 -24.677 -6.566  1.00 57.66  ? 1509 GLN A CG    1 
ATOM   2272 C  CD    . GLN A 1 292 ? -20.758 -24.371 -6.820  1.00 72.03  ? 1509 GLN A CD    1 
ATOM   2273 O  OE1   . GLN A 1 292 ? -21.150 -24.050 -7.944  1.00 75.24  ? 1509 GLN A OE1   1 
ATOM   2274 N  NE2   . GLN A 1 292 ? -21.573 -24.451 -5.773  1.00 74.56  ? 1509 GLN A NE2   1 
ATOM   2275 N  N     . VAL A 1 293 ? -16.280 -24.635 -10.052 1.00 56.69  ? 1510 VAL A N     1 
ATOM   2276 C  CA    . VAL A 1 293 ? -15.769 -25.172 -11.300 1.00 73.58  ? 1510 VAL A CA    1 
ATOM   2277 C  C     . VAL A 1 293 ? -14.732 -24.205 -11.837 1.00 74.01  ? 1510 VAL A C     1 
ATOM   2278 O  O     . VAL A 1 293 ? -15.032 -23.031 -12.048 1.00 68.21  ? 1510 VAL A O     1 
ATOM   2279 C  CB    . VAL A 1 293 ? -16.902 -25.368 -12.321 1.00 76.24  ? 1510 VAL A CB    1 
ATOM   2280 C  CG1   . VAL A 1 293 ? -16.385 -26.068 -13.550 1.00 87.73  ? 1510 VAL A CG1   1 
ATOM   2281 C  CG2   . VAL A 1 293 ? -18.044 -26.150 -11.690 1.00 72.25  ? 1510 VAL A CG2   1 
ATOM   2282 N  N     . VAL A 1 294 ? -13.541 -24.702 -12.135 1.00 83.16  ? 1511 VAL A N     1 
ATOM   2283 C  CA    . VAL A 1 294 ? -12.516 -23.875 -12.750 1.00 84.01  ? 1511 VAL A CA    1 
ATOM   2284 C  C     . VAL A 1 294 ? -12.191 -24.441 -14.124 1.00 84.51  ? 1511 VAL A C     1 
ATOM   2285 O  O     . VAL A 1 294 ? -11.970 -25.646 -14.284 1.00 85.51  ? 1511 VAL A O     1 
ATOM   2286 C  CB    . VAL A 1 294 ? -11.254 -23.770 -11.863 1.00 80.75  ? 1511 VAL A CB    1 
ATOM   2287 C  CG1   . VAL A 1 294 ? -10.641 -25.131 -11.574 1.00 73.41  ? 1511 VAL A CG1   1 
ATOM   2288 C  CG2   . VAL A 1 294 ? -10.239 -22.862 -12.506 1.00 83.31  ? 1511 VAL A CG2   1 
ATOM   2289 N  N     . ILE A 1 295 ? -12.210 -23.573 -15.119 1.00 83.17  ? 1512 ILE A N     1 
ATOM   2290 C  CA    . ILE A 1 295 ? -11.917 -23.945 -16.492 1.00 85.06  ? 1512 ILE A CA    1 
ATOM   2291 C  C     . ILE A 1 295 ? -10.461 -23.590 -16.757 1.00 87.74  ? 1512 ILE A C     1 
ATOM   2292 O  O     . ILE A 1 295 ? -10.095 -22.407 -16.738 1.00 92.49  ? 1512 ILE A O     1 
ATOM   2293 C  CB    . ILE A 1 295 ? -12.845 -23.222 -17.478 1.00 82.95  ? 1512 ILE A CB    1 
ATOM   2294 C  CG1   . ILE A 1 295 ? -14.318 -23.499 -17.149 1.00 82.57  ? 1512 ILE A CG1   1 
ATOM   2295 C  CG2   . ILE A 1 295 ? -12.477 -23.577 -18.915 1.00 70.39  ? 1512 ILE A CG2   1 
ATOM   2296 C  CD1   . ILE A 1 295 ? -15.279 -22.821 -18.098 1.00 80.31  ? 1512 ILE A CD1   1 
ATOM   2297 N  N     . VAL A 1 296 ? -9.630  -24.596 -17.002 1.00 73.21  ? 1513 VAL A N     1 
ATOM   2298 C  CA    . VAL A 1 296 ? -8.246  -24.387 -17.419 1.00 63.34  ? 1513 VAL A CA    1 
ATOM   2299 C  C     . VAL A 1 296 ? -8.176  -24.633 -18.921 1.00 64.16  ? 1513 VAL A C     1 
ATOM   2300 O  O     . VAL A 1 296 ? -8.461  -25.750 -19.361 1.00 64.67  ? 1513 VAL A O     1 
ATOM   2301 C  CB    . VAL A 1 296 ? -7.266  -25.316 -16.680 1.00 63.86  ? 1513 VAL A CB    1 
ATOM   2302 C  CG1   . VAL A 1 296 ? -5.873  -25.143 -17.266 1.00 57.01  ? 1513 VAL A CG1   1 
ATOM   2303 C  CG2   . VAL A 1 296 ? -7.265  -25.074 -15.161 1.00 51.34  ? 1513 VAL A CG2   1 
ATOM   2304 N  N     . PRO A 1 297 ? -7.849  -23.636 -19.735 1.00 78.34  ? 1514 PRO A N     1 
ATOM   2305 C  CA    . PRO A 1 297 ? -7.638  -23.915 -21.160 1.00 85.01  ? 1514 PRO A CA    1 
ATOM   2306 C  C     . PRO A 1 297 ? -6.350  -24.697 -21.342 1.00 83.64  ? 1514 PRO A C     1 
ATOM   2307 O  O     . PRO A 1 297 ? -5.296  -24.316 -20.834 1.00 88.66  ? 1514 PRO A O     1 
ATOM   2308 C  CB    . PRO A 1 297 ? -7.560  -22.521 -21.798 1.00 87.33  ? 1514 PRO A CB    1 
ATOM   2309 C  CG    . PRO A 1 297 ? -7.290  -21.581 -20.662 1.00 84.50  ? 1514 PRO A CG    1 
ATOM   2310 C  CD    . PRO A 1 297 ? -7.893  -22.190 -19.443 1.00 78.98  ? 1514 PRO A CD    1 
ATOM   2311 N  N     . CYS A 1 298 ? -6.454  -25.817 -22.034 1.00 89.78  ? 1515 CYS A N     1 
ATOM   2312 C  CA    . CYS A 1 298 ? -5.361  -26.759 -22.208 1.00 91.21  ? 1515 CYS A CA    1 
ATOM   2313 C  C     . CYS A 1 298 ? -5.016  -26.881 -23.685 1.00 94.36  ? 1515 CYS A C     1 
ATOM   2314 O  O     . CYS A 1 298 ? -5.729  -26.387 -24.563 1.00 97.35  ? 1515 CYS A O     1 
ATOM   2315 C  CB    . CYS A 1 298 ? -5.696  -28.128 -21.605 1.00 90.62  ? 1515 CYS A CB    1 
ATOM   2316 S  SG    . CYS A 1 298 ? -6.932  -29.080 -22.481 1.00 99.63  ? 1515 CYS A SG    1 
ATOM   2317 N  N     . GLY A 1 299 ? -3.888  -27.528 -23.949 1.00 92.22  ? 1516 GLY A N     1 
ATOM   2318 C  CA    . GLY A 1 299 ? -3.445  -27.765 -25.303 1.00 88.92  ? 1516 GLY A CA    1 
ATOM   2319 C  C     . GLY A 1 299 ? -2.652  -26.613 -25.855 1.00 88.86  ? 1516 GLY A C     1 
ATOM   2320 O  O     . GLY A 1 299 ? -2.329  -26.610 -27.051 1.00 91.89  ? 1516 GLY A O     1 
ATOM   2321 N  N     . ILE A 1 300 ? -2.374  -25.618 -25.019 1.00 89.67  ? 1517 ILE A N     1 
ATOM   2322 C  CA    . ILE A 1 300 ? -1.527  -24.481 -25.357 1.00 93.86  ? 1517 ILE A CA    1 
ATOM   2323 C  C     . ILE A 1 300 ? -0.061  -24.880 -25.242 1.00 100.83 ? 1517 ILE A C     1 
ATOM   2324 O  O     . ILE A 1 300 ? 0.414   -25.206 -24.148 1.00 65.84  ? 1517 ILE A O     1 
ATOM   2325 C  CB    . ILE A 1 300 ? -1.842  -23.285 -24.449 1.00 90.74  ? 1517 ILE A CB    1 
ATOM   2326 C  CG1   . ILE A 1 300 ? -3.291  -22.848 -24.638 1.00 73.53  ? 1517 ILE A CG1   1 
ATOM   2327 C  CG2   . ILE A 1 300 ? -0.864  -22.154 -24.710 1.00 99.84  ? 1517 ILE A CG2   1 
ATOM   2328 C  CD1   . ILE A 1 300 ? -3.767  -21.934 -23.553 1.00 66.22  ? 1517 ILE A CD1   1 
ATOM   2329 N  N     . THR A 1 301 ? 0.652   -24.863 -26.365 1.00 106.26 ? 1518 THR A N     1 
ATOM   2330 C  CA    . THR A 1 301 ? 2.059   -25.237 -26.402 1.00 110.68 ? 1518 THR A CA    1 
ATOM   2331 C  C     . THR A 1 301 ? 2.887   -23.964 -26.266 1.00 112.39 ? 1518 THR A C     1 
ATOM   2332 O  O     . THR A 1 301 ? 2.356   -22.848 -26.241 1.00 109.46 ? 1518 THR A O     1 
ATOM   2333 C  CB    . THR A 1 301 ? 2.413   -25.969 -27.696 1.00 72.61  ? 1518 THR A CB    1 
ATOM   2334 N  N     . ALA A 1 302 ? 4.207   -24.130 -26.180 1.00 123.33 ? 1519 ALA A N     1 
ATOM   2335 C  CA    . ALA A 1 302 ? 5.062   -22.949 -26.153 1.00 130.62 ? 1519 ALA A CA    1 
ATOM   2336 C  C     . ALA A 1 302 ? 4.841   -22.080 -27.378 1.00 127.72 ? 1519 ALA A C     1 
ATOM   2337 O  O     . ALA A 1 302 ? 5.081   -20.870 -27.330 1.00 131.63 ? 1519 ALA A O     1 
ATOM   2338 C  CB    . ALA A 1 302 ? 6.530   -23.348 -26.043 1.00 139.48 ? 1519 ALA A CB    1 
ATOM   2339 N  N     . THR A 1 303 ? 4.359   -22.664 -28.473 1.00 114.39 ? 1520 THR A N     1 
ATOM   2340 C  CA    . THR A 1 303 ? 4.103   -21.910 -29.691 1.00 104.26 ? 1520 THR A CA    1 
ATOM   2341 C  C     . THR A 1 303 ? 2.652   -22.023 -30.152 1.00 103.85 ? 1520 THR A C     1 
ATOM   2342 O  O     . THR A 1 303 ? 2.376   -21.998 -31.351 1.00 101.75 ? 1520 THR A O     1 
ATOM   2343 C  CB    . THR A 1 303 ? 5.055   -22.327 -30.803 1.00 108.71 ? 1520 THR A CB    1 
ATOM   2344 O  OG1   . THR A 1 303 ? 4.566   -21.809 -32.046 1.00 123.91 ? 1520 THR A OG1   1 
ATOM   2345 C  CG2   . THR A 1 303 ? 5.176   -23.835 -30.870 1.00 100.43 ? 1520 THR A CG2   1 
ATOM   2346 N  N     . THR A 1 304 ? 1.714   -22.203 -29.219 1.00 104.78 ? 1521 THR A N     1 
ATOM   2347 C  CA    . THR A 1 304 ? 0.326   -21.878 -29.522 1.00 98.50  ? 1521 THR A CA    1 
ATOM   2348 C  C     . THR A 1 304 ? 0.240   -20.381 -29.830 1.00 106.49 ? 1521 THR A C     1 
ATOM   2349 O  O     . THR A 1 304 ? 0.801   -19.558 -29.099 1.00 105.36 ? 1521 THR A O     1 
ATOM   2350 C  CB    . THR A 1 304 ? -0.580  -22.260 -28.346 1.00 81.07  ? 1521 THR A CB    1 
ATOM   2351 N  N     . THR A 1 305 ? -0.431  -20.032 -30.935 1.00 110.55 ? 1522 THR A N     1 
ATOM   2352 C  CA    . THR A 1 305 ? -0.514  -18.649 -31.417 1.00 106.02 ? 1522 THR A CA    1 
ATOM   2353 C  C     . THR A 1 305 ? -1.589  -17.833 -30.705 1.00 111.32 ? 1522 THR A C     1 
ATOM   2354 O  O     . THR A 1 305 ? -2.598  -18.364 -30.229 1.00 106.60 ? 1522 THR A O     1 
ATOM   2355 C  CB    . THR A 1 305 ? -0.786  -18.597 -32.924 1.00 94.12  ? 1522 THR A CB    1 
ATOM   2356 N  N     . ASP A 1 306 ? -1.357  -16.514 -30.654 1.00 118.17 ? 1523 ASP A N     1 
ATOM   2357 C  CA    . ASP A 1 306 ? -2.274  -15.603 -29.976 1.00 114.20 ? 1523 ASP A CA    1 
ATOM   2358 C  C     . ASP A 1 306 ? -3.678  -15.687 -30.554 1.00 114.84 ? 1523 ASP A C     1 
ATOM   2359 O  O     . ASP A 1 306 ? -4.657  -15.496 -29.829 1.00 113.65 ? 1523 ASP A O     1 
ATOM   2360 C  CB    . ASP A 1 306 ? -1.747  -14.177 -30.052 1.00 119.02 ? 1523 ASP A CB    1 
ATOM   2361 C  CG    . ASP A 1 306 ? -0.471  -14.001 -29.269 1.00 126.26 ? 1523 ASP A CG    1 
ATOM   2362 O  OD1   . ASP A 1 306 ? -0.122  -14.930 -28.507 1.00 128.69 ? 1523 ASP A OD1   1 
ATOM   2363 O  OD2   . ASP A 1 306 ? 0.183   -12.945 -29.423 1.00 126.17 ? 1523 ASP A OD2   1 
ATOM   2364 N  N     . ASP A 1 307 ? -3.806  -15.921 -31.863 1.00 119.03 ? 1524 ASP A N     1 
ATOM   2365 C  CA    . ASP A 1 307 ? -5.150  -16.063 -32.420 1.00 118.77 ? 1524 ASP A CA    1 
ATOM   2366 C  C     . ASP A 1 307 ? -5.779  -17.391 -32.009 1.00 113.95 ? 1524 ASP A C     1 
ATOM   2367 O  O     . ASP A 1 307 ? -6.955  -17.427 -31.629 1.00 109.12 ? 1524 ASP A O     1 
ATOM   2368 C  CB    . ASP A 1 307 ? -5.136  -15.910 -33.942 1.00 123.52 ? 1524 ASP A CB    1 
ATOM   2369 C  CG    . ASP A 1 307 ? -6.390  -15.220 -34.452 1.00 118.75 ? 1524 ASP A CG    1 
ATOM   2370 O  OD1   . ASP A 1 307 ? -7.042  -14.526 -33.638 1.00 109.46 ? 1524 ASP A OD1   1 
ATOM   2371 O  OD2   . ASP A 1 307 ? -6.739  -15.396 -35.641 1.00 119.33 ? 1524 ASP A OD2   1 
ATOM   2372 N  N     . GLU A 1 308 ? -5.018  -18.499 -32.093 1.00 110.74 ? 1525 GLU A N     1 
ATOM   2373 C  CA    . GLU A 1 308 ? -5.486  -19.764 -31.522 1.00 106.82 ? 1525 GLU A CA    1 
ATOM   2374 C  C     . GLU A 1 308 ? -5.745  -19.640 -30.022 1.00 99.56  ? 1525 GLU A C     1 
ATOM   2375 O  O     . GLU A 1 308 ? -6.781  -20.108 -29.518 1.00 102.90 ? 1525 GLU A O     1 
ATOM   2376 C  CB    . GLU A 1 308 ? -4.480  -20.887 -31.768 1.00 109.06 ? 1525 GLU A CB    1 
ATOM   2377 C  CG    . GLU A 1 308 ? -3.684  -20.754 -33.032 1.00 121.75 ? 1525 GLU A CG    1 
ATOM   2378 C  CD    . GLU A 1 308 ? -2.564  -21.765 -33.094 1.00 133.19 ? 1525 GLU A CD    1 
ATOM   2379 O  OE1   . GLU A 1 308 ? -1.576  -21.611 -32.345 1.00 136.44 ? 1525 GLU A OE1   1 
ATOM   2380 O  OE2   . GLU A 1 308 ? -2.671  -22.719 -33.893 1.00 139.37 ? 1525 GLU A OE2   1 
ATOM   2381 N  N     . ARG A 1 309 ? -4.817  -19.015 -29.291 1.00 84.70  ? 1526 ARG A N     1 
ATOM   2382 C  CA    . ARG A 1 309 ? -5.008  -18.867 -27.858 1.00 76.18  ? 1526 ARG A CA    1 
ATOM   2383 C  C     . ARG A 1 309 ? -6.268  -18.078 -27.571 1.00 92.60  ? 1526 ARG A C     1 
ATOM   2384 O  O     . ARG A 1 309 ? -7.051  -18.444 -26.688 1.00 87.76  ? 1526 ARG A O     1 
ATOM   2385 C  CB    . ARG A 1 309 ? -3.807  -18.193 -27.202 1.00 66.88  ? 1526 ARG A CB    1 
ATOM   2386 C  CG    . ARG A 1 309 ? -3.965  -18.127 -25.685 1.00 74.59  ? 1526 ARG A CG    1 
ATOM   2387 C  CD    . ARG A 1 309 ? -2.662  -18.390 -24.972 1.00 86.03  ? 1526 ARG A CD    1 
ATOM   2388 N  NE    . ARG A 1 309 ? -1.697  -17.336 -25.261 1.00 101.04 ? 1526 ARG A NE    1 
ATOM   2389 C  CZ    . ARG A 1 309 ? -0.482  -17.259 -24.725 1.00 109.37 ? 1526 ARG A CZ    1 
ATOM   2390 N  NH1   . ARG A 1 309 ? -0.083  -18.185 -23.863 1.00 107.17 ? 1526 ARG A NH1   1 
ATOM   2391 N  NH2   . ARG A 1 309 ? 0.332   -16.254 -25.049 1.00 113.35 ? 1526 ARG A NH2   1 
ATOM   2392 N  N     . ARG A 1 310 ? -6.483  -16.994 -28.322 1.00 102.64 ? 1527 ARG A N     1 
ATOM   2393 C  CA    . ARG A 1 310 ? -7.657  -16.160 -28.122 1.00 96.21  ? 1527 ARG A CA    1 
ATOM   2394 C  C     . ARG A 1 310 ? -8.931  -16.911 -28.480 1.00 96.01  ? 1527 ARG A C     1 
ATOM   2395 O  O     . ARG A 1 310 ? -9.921  -16.829 -27.750 1.00 90.04  ? 1527 ARG A O     1 
ATOM   2396 C  CB    . ARG A 1 310 ? -7.522  -14.887 -28.950 1.00 96.22  ? 1527 ARG A CB    1 
ATOM   2397 N  N     . ARG A 1 311 ? -8.913  -17.689 -29.568 1.00 97.52  ? 1528 ARG A N     1 
ATOM   2398 C  CA    . ARG A 1 311 ? -10.094 -18.459 -29.960 1.00 102.11 ? 1528 ARG A CA    1 
ATOM   2399 C  C     . ARG A 1 311 ? -10.499 -19.428 -28.846 1.00 104.62 ? 1528 ARG A C     1 
ATOM   2400 O  O     . ARG A 1 311 ? -11.683 -19.520 -28.459 1.00 101.33 ? 1528 ARG A O     1 
ATOM   2401 C  CB    . ARG A 1 311 ? -9.815  -19.199 -31.276 1.00 95.71  ? 1528 ARG A CB    1 
ATOM   2402 N  N     . LEU A 1 312 ? -9.512  -20.139 -28.295 1.00 103.18 ? 1529 LEU A N     1 
ATOM   2403 C  CA    . LEU A 1 312 ? -9.799  -21.055 -27.198 1.00 99.34  ? 1529 LEU A CA    1 
ATOM   2404 C  C     . LEU A 1 312 ? -10.248 -20.301 -25.949 1.00 87.54  ? 1529 LEU A C     1 
ATOM   2405 O  O     . LEU A 1 312 ? -11.258 -20.659 -25.333 1.00 83.30  ? 1529 LEU A O     1 
ATOM   2406 C  CB    . LEU A 1 312 ? -8.572  -21.924 -26.900 1.00 95.37  ? 1529 LEU A CB    1 
ATOM   2407 C  CG    . LEU A 1 312 ? -8.689  -22.807 -25.654 1.00 89.43  ? 1529 LEU A CG    1 
ATOM   2408 C  CD1   . LEU A 1 312 ? -9.695  -23.948 -25.856 1.00 62.66  ? 1529 LEU A CD1   1 
ATOM   2409 C  CD2   . LEU A 1 312 ? -7.330  -23.332 -25.271 1.00 90.30  ? 1529 LEU A CD2   1 
ATOM   2410 N  N     . TYR A 1 313 ? -9.513  -19.258 -25.561 1.00 84.48  ? 1530 TYR A N     1 
ATOM   2411 C  CA    . TYR A 1 313 ? -9.915  -18.436 -24.424 1.00 96.45  ? 1530 TYR A CA    1 
ATOM   2412 C  C     . TYR A 1 313 ? -11.356 -17.974 -24.559 1.00 103.07 ? 1530 TYR A C     1 
ATOM   2413 O  O     . TYR A 1 313 ? -12.093 -17.900 -23.569 1.00 94.16  ? 1530 TYR A O     1 
ATOM   2414 C  CB    . TYR A 1 313 ? -9.011  -17.205 -24.324 1.00 107.08 ? 1530 TYR A CB    1 
ATOM   2415 C  CG    . TYR A 1 313 ? -7.713  -17.383 -23.575 1.00 113.26 ? 1530 TYR A CG    1 
ATOM   2416 C  CD1   . TYR A 1 313 ? -7.034  -16.279 -23.060 1.00 111.39 ? 1530 TYR A CD1   1 
ATOM   2417 C  CD2   . TYR A 1 313 ? -7.155  -18.640 -23.389 1.00 111.03 ? 1530 TYR A CD2   1 
ATOM   2418 C  CE1   . TYR A 1 313 ? -5.840  -16.426 -22.382 1.00 106.15 ? 1530 TYR A CE1   1 
ATOM   2419 C  CE2   . TYR A 1 313 ? -5.958  -18.793 -22.710 1.00 105.74 ? 1530 TYR A CE2   1 
ATOM   2420 C  CZ    . TYR A 1 313 ? -5.306  -17.689 -22.207 1.00 102.11 ? 1530 TYR A CZ    1 
ATOM   2421 O  OH    . TYR A 1 313 ? -4.116  -17.848 -21.526 1.00 99.80  ? 1530 TYR A OH    1 
ATOM   2422 N  N     . GLU A 1 314 ? -11.777 -17.671 -25.789 1.00 110.82 ? 1531 GLU A N     1 
ATOM   2423 C  CA    . GLU A 1 314 ? -13.105 -17.112 -26.010 1.00 108.23 ? 1531 GLU A CA    1 
ATOM   2424 C  C     . GLU A 1 314 ? -14.172 -18.173 -25.828 1.00 105.63 ? 1531 GLU A C     1 
ATOM   2425 O  O     . GLU A 1 314 ? -15.195 -17.935 -25.164 1.00 108.33 ? 1531 GLU A O     1 
ATOM   2426 C  CB    . GLU A 1 314 ? -13.180 -16.500 -27.411 1.00 109.36 ? 1531 GLU A CB    1 
ATOM   2427 N  N     . SER A 1 315 ? -13.929 -19.371 -26.359 1.00 104.04 ? 1532 SER A N     1 
ATOM   2428 C  CA    . SER A 1 315 ? -14.906 -20.416 -26.102 1.00 109.37 ? 1532 SER A CA    1 
ATOM   2429 C  C     . SER A 1 315 ? -14.939 -20.768 -24.620 1.00 111.28 ? 1532 SER A C     1 
ATOM   2430 O  O     . SER A 1 315 ? -16.003 -21.102 -24.069 1.00 111.29 ? 1532 SER A O     1 
ATOM   2431 C  CB    . SER A 1 315 ? -14.602 -21.664 -26.928 1.00 106.73 ? 1532 SER A CB    1 
ATOM   2432 O  OG    . SER A 1 315 ? -15.759 -22.487 -27.011 1.00 105.78 ? 1532 SER A OG    1 
ATOM   2433 N  N     . CYS A 1 316 ? -13.795 -20.655 -23.945 1.00 104.03 ? 1533 CYS A N     1 
ATOM   2434 C  CA    . CYS A 1 316 ? -13.751 -20.924 -22.515 1.00 97.25  ? 1533 CYS A CA    1 
ATOM   2435 C  C     . CYS A 1 316 ? -14.556 -19.903 -21.745 1.00 86.84  ? 1533 CYS A C     1 
ATOM   2436 O  O     . CYS A 1 316 ? -15.235 -20.245 -20.772 1.00 82.64  ? 1533 CYS A O     1 
ATOM   2437 C  CB    . CYS A 1 316 ? -12.301 -20.943 -22.036 1.00 97.24  ? 1533 CYS A CB    1 
ATOM   2438 S  SG    . CYS A 1 316 ? -11.515 -22.491 -22.424 1.00 106.86 ? 1533 CYS A SG    1 
ATOM   2439 N  N     . ARG A 1 317 ? -14.508 -18.648 -22.175 1.00 86.69  ? 1534 ARG A N     1 
ATOM   2440 C  CA    . ARG A 1 317 ? -15.298 -17.637 -21.487 1.00 87.60  ? 1534 ARG A CA    1 
ATOM   2441 C  C     . ARG A 1 317 ? -16.774 -17.863 -21.742 1.00 82.11  ? 1534 ARG A C     1 
ATOM   2442 O  O     . ARG A 1 317 ? -17.595 -17.666 -20.844 1.00 76.07  ? 1534 ARG A O     1 
ATOM   2443 C  CB    . ARG A 1 317 ? -14.882 -16.235 -21.935 1.00 81.23  ? 1534 ARG A CB    1 
ATOM   2444 C  CG    . ARG A 1 317 ? -13.550 -15.809 -21.375 1.00 80.04  ? 1534 ARG A CG    1 
ATOM   2445 C  CD    . ARG A 1 317 ? -13.275 -14.363 -21.676 1.00 80.69  ? 1534 ARG A CD    1 
ATOM   2446 N  NE    . ARG A 1 317 ? -12.207 -13.835 -20.835 1.00 78.73  ? 1534 ARG A NE    1 
ATOM   2447 C  CZ    . ARG A 1 317 ? -10.938 -13.799 -21.207 1.00 87.16  ? 1534 ARG A CZ    1 
ATOM   2448 N  NH1   . ARG A 1 317 ? -10.594 -14.256 -22.406 1.00 94.97  ? 1534 ARG A NH1   1 
ATOM   2449 N  NH2   . ARG A 1 317 ? -10.019 -13.291 -20.393 1.00 90.21  ? 1534 ARG A NH2   1 
ATOM   2450 N  N     . GLU A 1 318 ? -17.113 -18.401 -22.913 1.00 79.41  ? 1535 GLU A N     1 
ATOM   2451 C  CA    . GLU A 1 318 ? -18.519 -18.656 -23.192 1.00 80.40  ? 1535 GLU A CA    1 
ATOM   2452 C  C     . GLU A 1 318 ? -19.053 -19.805 -22.351 1.00 91.07  ? 1535 GLU A C     1 
ATOM   2453 O  O     . GLU A 1 318 ? -20.188 -19.736 -21.846 1.00 90.43  ? 1535 GLU A O     1 
ATOM   2454 C  CB    . GLU A 1 318 ? -18.696 -18.980 -24.675 1.00 82.86  ? 1535 GLU A CB    1 
ATOM   2455 C  CG    . GLU A 1 318 ? -20.122 -19.186 -25.099 1.00 90.50  ? 1535 GLU A CG    1 
ATOM   2456 C  CD    . GLU A 1 318 ? -20.204 -19.892 -26.429 1.00 116.37 ? 1535 GLU A CD    1 
ATOM   2457 O  OE1   . GLU A 1 318 ? -21.302 -20.376 -26.780 1.00 126.43 ? 1535 GLU A OE1   1 
ATOM   2458 O  OE2   . GLU A 1 318 ? -19.160 -19.977 -27.119 1.00 124.50 ? 1535 GLU A OE2   1 
ATOM   2459 N  N     . LEU A 1 319 ? -18.226 -20.843 -22.135 1.00 95.95  ? 1536 LEU A N     1 
ATOM   2460 C  CA    . LEU A 1 319 ? -18.645 -21.922 -21.248 1.00 88.71  ? 1536 LEU A CA    1 
ATOM   2461 C  C     . LEU A 1 319 ? -18.753 -21.425 -19.815 1.00 83.23  ? 1536 LEU A C     1 
ATOM   2462 O  O     . LEU A 1 319 ? -19.729 -21.735 -19.112 1.00 79.49  ? 1536 LEU A O     1 
ATOM   2463 C  CB    . LEU A 1 319 ? -17.685 -23.105 -21.327 1.00 91.89  ? 1536 LEU A CB    1 
ATOM   2464 C  CG    . LEU A 1 319 ? -18.171 -24.324 -20.525 1.00 94.23  ? 1536 LEU A CG    1 
ATOM   2465 C  CD1   . LEU A 1 319 ? -19.569 -24.743 -20.959 1.00 99.38  ? 1536 LEU A CD1   1 
ATOM   2466 C  CD2   . LEU A 1 319 ? -17.218 -25.482 -20.668 1.00 95.92  ? 1536 LEU A CD2   1 
ATOM   2467 N  N     . GLU A 1 320 ? -17.774 -20.623 -19.381 1.00 77.09  ? 1537 GLU A N     1 
ATOM   2468 C  CA    . GLU A 1 320 ? -17.824 -20.042 -18.045 1.00 79.63  ? 1537 GLU A CA    1 
ATOM   2469 C  C     . GLU A 1 320 ? -19.079 -19.213 -17.856 1.00 87.38  ? 1537 GLU A C     1 
ATOM   2470 O  O     . GLU A 1 320 ? -19.744 -19.303 -16.816 1.00 80.48  ? 1537 GLU A O     1 
ATOM   2471 C  CB    . GLU A 1 320 ? -16.578 -19.186 -17.831 1.00 85.02  ? 1537 GLU A CB    1 
ATOM   2472 C  CG    . GLU A 1 320 ? -16.653 -18.112 -16.763 1.00 86.23  ? 1537 GLU A CG    1 
ATOM   2473 C  CD    . GLU A 1 320 ? -15.353 -17.331 -16.684 1.00 89.87  ? 1537 GLU A CD    1 
ATOM   2474 O  OE1   . GLU A 1 320 ? -15.047 -16.755 -15.616 1.00 90.29  ? 1537 GLU A OE1   1 
ATOM   2475 O  OE2   . GLU A 1 320 ? -14.627 -17.317 -17.700 1.00 89.77  ? 1537 GLU A OE2   1 
ATOM   2476 N  N     . GLN A 1 321 ? -19.469 -18.468 -18.892 1.00 97.95  ? 1538 GLN A N     1 
ATOM   2477 C  CA    . GLN A 1 321 ? -20.636 -17.602 -18.777 1.00 98.91  ? 1538 GLN A CA    1 
ATOM   2478 C  C     . GLN A 1 321 ? -21.919 -18.404 -18.702 1.00 88.75  ? 1538 GLN A C     1 
ATOM   2479 O  O     . GLN A 1 321 ? -22.781 -18.107 -17.868 1.00 87.79  ? 1538 GLN A O     1 
ATOM   2480 C  CB    . GLN A 1 321 ? -20.680 -16.618 -19.948 1.00 106.26 ? 1538 GLN A CB    1 
ATOM   2481 C  CG    . GLN A 1 321 ? -19.721 -15.454 -19.770 1.00 108.04 ? 1538 GLN A CG    1 
ATOM   2482 C  CD    . GLN A 1 321 ? -19.548 -15.112 -18.309 1.00 106.77 ? 1538 GLN A CD    1 
ATOM   2483 O  OE1   . GLN A 1 321 ? -20.520 -14.787 -17.612 1.00 104.63 ? 1538 GLN A OE1   1 
ATOM   2484 N  NE2   . GLN A 1 321 ? -18.312 -15.205 -17.824 1.00 104.64 ? 1538 GLN A NE2   1 
ATOM   2485 N  N     . THR A 1 322 ? -22.044 -19.461 -19.517 1.00 87.27  ? 1539 THR A N     1 
ATOM   2486 C  CA    . THR A 1 322 ? -23.272 -20.233 -19.421 1.00 89.13  ? 1539 THR A CA    1 
ATOM   2487 C  C     . THR A 1 322 ? -23.300 -21.066 -18.147 1.00 87.91  ? 1539 THR A C     1 
ATOM   2488 O  O     . THR A 1 322 ? -24.376 -21.475 -17.704 1.00 93.35  ? 1539 THR A O     1 
ATOM   2489 C  CB    . THR A 1 322 ? -23.498 -21.109 -20.651 1.00 87.63  ? 1539 THR A CB    1 
ATOM   2490 O  OG1   . THR A 1 322 ? -24.547 -22.039 -20.370 1.00 101.85 ? 1539 THR A OG1   1 
ATOM   2491 C  CG2   . THR A 1 322 ? -22.275 -21.869 -21.059 1.00 92.21  ? 1539 THR A CG2   1 
ATOM   2492 N  N     . PHE A 1 323 ? -22.155 -21.293 -17.511 1.00 87.96  ? 1540 PHE A N     1 
ATOM   2493 C  CA    . PHE A 1 323 ? -22.177 -21.860 -16.168 1.00 91.59  ? 1540 PHE A CA    1 
ATOM   2494 C  C     . PHE A 1 323 ? -22.639 -20.837 -15.132 1.00 91.89  ? 1540 PHE A C     1 
ATOM   2495 O  O     . PHE A 1 323 ? -23.413 -21.174 -14.231 1.00 90.73  ? 1540 PHE A O     1 
ATOM   2496 C  CB    . PHE A 1 323 ? -20.796 -22.408 -15.805 1.00 93.93  ? 1540 PHE A CB    1 
ATOM   2497 C  CG    . PHE A 1 323 ? -20.553 -23.789 -16.319 1.00 94.02  ? 1540 PHE A CG    1 
ATOM   2498 C  CD1   . PHE A 1 323 ? -21.588 -24.709 -16.373 1.00 97.08  ? 1540 PHE A CD1   1 
ATOM   2499 C  CD2   . PHE A 1 323 ? -19.302 -24.171 -16.761 1.00 95.19  ? 1540 PHE A CD2   1 
ATOM   2500 C  CE1   . PHE A 1 323 ? -21.371 -25.991 -16.848 1.00 100.47 ? 1540 PHE A CE1   1 
ATOM   2501 C  CE2   . PHE A 1 323 ? -19.083 -25.446 -17.243 1.00 97.55  ? 1540 PHE A CE2   1 
ATOM   2502 C  CZ    . PHE A 1 323 ? -20.113 -26.357 -17.282 1.00 99.39  ? 1540 PHE A CZ    1 
ATOM   2503 N  N     . VAL A 1 324 ? -22.147 -19.596 -15.205 1.00 92.33  ? 1541 VAL A N     1 
ATOM   2504 C  CA    . VAL A 1 324 ? -22.618 -18.572 -14.269 1.00 88.39  ? 1541 VAL A CA    1 
ATOM   2505 C  C     . VAL A 1 324 ? -24.124 -18.402 -14.396 1.00 86.97  ? 1541 VAL A C     1 
ATOM   2506 O  O     . VAL A 1 324 ? -24.852 -18.378 -13.393 1.00 80.83  ? 1541 VAL A O     1 
ATOM   2507 C  CB    . VAL A 1 324 ? -21.885 -17.228 -14.466 1.00 88.30  ? 1541 VAL A CB    1 
ATOM   2508 C  CG1   . VAL A 1 324 ? -22.035 -16.404 -13.205 1.00 84.06  ? 1541 VAL A CG1   1 
ATOM   2509 C  CG2   . VAL A 1 324 ? -20.433 -17.425 -14.736 1.00 85.13  ? 1541 VAL A CG2   1 
ATOM   2510 N  N     . LYS A 1 325 ? -24.605 -18.231 -15.635 1.00 91.91  ? 1542 LYS A N     1 
ATOM   2511 C  CA    . LYS A 1 325 ? -26.033 -18.030 -15.872 1.00 97.46  ? 1542 LYS A CA    1 
ATOM   2512 C  C     . LYS A 1 325 ? -26.855 -19.252 -15.478 1.00 106.48 ? 1542 LYS A C     1 
ATOM   2513 O  O     . LYS A 1 325 ? -28.048 -19.118 -15.185 1.00 113.47 ? 1542 LYS A O     1 
ATOM   2514 C  CB    . LYS A 1 325 ? -26.282 -17.669 -17.337 1.00 96.84  ? 1542 LYS A CB    1 
ATOM   2515 N  N     . ALA A 1 326 ? -26.243 -20.436 -15.435 1.00 104.09 ? 1543 ALA A N     1 
ATOM   2516 C  CA    . ALA A 1 326 ? -26.898 -21.601 -14.858 1.00 103.40 ? 1543 ALA A CA    1 
ATOM   2517 C  C     . ALA A 1 326 ? -26.869 -21.585 -13.339 1.00 99.18  ? 1543 ALA A C     1 
ATOM   2518 O  O     . ALA A 1 326 ? -27.377 -22.523 -12.718 1.00 98.34  ? 1543 ALA A O     1 
ATOM   2519 C  CB    . ALA A 1 326 ? -26.238 -22.885 -15.365 1.00 105.20 ? 1543 ALA A CB    1 
ATOM   2520 N  N     . GLY A 1 327 ? -26.305 -20.536 -12.742 1.00 92.47  ? 1544 GLY A N     1 
ATOM   2521 C  CA    . GLY A 1 327 ? -26.216 -20.358 -11.310 1.00 92.30  ? 1544 GLY A CA    1 
ATOM   2522 C  C     . GLY A 1 327 ? -25.056 -21.028 -10.606 1.00 89.83  ? 1544 GLY A C     1 
ATOM   2523 O  O     . GLY A 1 327 ? -24.927 -20.861 -9.385  1.00 94.56  ? 1544 GLY A O     1 
ATOM   2524 N  N     . ILE A 1 328 ? -24.184 -21.738 -11.317 1.00 83.02  ? 1545 ILE A N     1 
ATOM   2525 C  CA    . ILE A 1 328 ? -23.023 -22.375 -10.697 1.00 85.36  ? 1545 ILE A CA    1 
ATOM   2526 C  C     . ILE A 1 328 ? -21.804 -21.467 -10.836 1.00 76.70  ? 1545 ILE A C     1 
ATOM   2527 O  O     . ILE A 1 328 ? -21.574 -20.860 -11.893 1.00 77.31  ? 1545 ILE A O     1 
ATOM   2528 C  CB    . ILE A 1 328 ? -22.760 -23.793 -11.258 1.00 91.77  ? 1545 ILE A CB    1 
ATOM   2529 C  CG1   . ILE A 1 328 ? -22.637 -23.801 -12.775 1.00 94.56  ? 1545 ILE A CG1   1 
ATOM   2530 C  CG2   . ILE A 1 328 ? -23.871 -24.763 -10.840 1.00 90.12  ? 1545 ILE A CG2   1 
ATOM   2531 C  CD1   . ILE A 1 328 ? -22.815 -25.189 -13.358 1.00 91.04  ? 1545 ILE A CD1   1 
ATOM   2532 N  N     . ARG A 1 329 ? -21.024 -21.379 -9.758  1.00 61.52  ? 1546 ARG A N     1 
ATOM   2533 C  CA    . ARG A 1 329 ? -19.864 -20.499 -9.636  1.00 75.77  ? 1546 ARG A CA    1 
ATOM   2534 C  C     . ARG A 1 329 ? -18.660 -21.040 -10.405 1.00 89.74  ? 1546 ARG A C     1 
ATOM   2535 O  O     . ARG A 1 329 ? -17.859 -21.811 -9.872  1.00 97.21  ? 1546 ARG A O     1 
ATOM   2536 C  CB    . ARG A 1 329 ? -19.509 -20.344 -8.168  1.00 75.10  ? 1546 ARG A CB    1 
ATOM   2537 C  CG    . ARG A 1 329 ? -20.680 -20.027 -7.321  1.00 64.37  ? 1546 ARG A CG    1 
ATOM   2538 C  CD    . ARG A 1 329 ? -20.187 -19.566 -5.978  1.00 65.46  ? 1546 ARG A CD    1 
ATOM   2539 N  NE    . ARG A 1 329 ? -19.847 -20.654 -5.071  1.00 69.20  ? 1546 ARG A NE    1 
ATOM   2540 C  CZ    . ARG A 1 329 ? -20.717 -21.572 -4.668  1.00 70.03  ? 1546 ARG A CZ    1 
ATOM   2541 N  NH1   . ARG A 1 329 ? -21.970 -21.539 -5.100  1.00 65.16  ? 1546 ARG A NH1   1 
ATOM   2542 N  NH2   . ARG A 1 329 ? -20.339 -22.517 -3.829  1.00 73.42  ? 1546 ARG A NH2   1 
ATOM   2543 N  N     . CYS A 1 330 ? -18.466 -20.554 -11.627 1.00 84.54  ? 1547 CYS A N     1 
ATOM   2544 C  CA    . CYS A 1 330 ? -17.359 -20.979 -12.469 1.00 75.47  ? 1547 CYS A CA    1 
ATOM   2545 C  C     . CYS A 1 330 ? -16.510 -19.785 -12.854 1.00 83.66  ? 1547 CYS A C     1 
ATOM   2546 O  O     . CYS A 1 330 ? -17.044 -18.755 -13.272 1.00 100.98 ? 1547 CYS A O     1 
ATOM   2547 C  CB    . CYS A 1 330 ? -17.868 -21.642 -13.741 1.00 75.21  ? 1547 CYS A CB    1 
ATOM   2548 S  SG    . CYS A 1 330 ? -16.620 -21.761 -15.049 1.00 79.23  ? 1547 CYS A SG    1 
ATOM   2549 N  N     . GLU A 1 331 ? -15.192 -19.931 -12.735 1.00 76.13  ? 1548 GLU A N     1 
ATOM   2550 C  CA    . GLU A 1 331 ? -14.248 -18.953 -13.247 1.00 67.35  ? 1548 GLU A CA    1 
ATOM   2551 C  C     . GLU A 1 331 ? -13.290 -19.665 -14.188 1.00 72.76  ? 1548 GLU A C     1 
ATOM   2552 O  O     . GLU A 1 331 ? -13.089 -20.878 -14.088 1.00 81.70  ? 1548 GLU A O     1 
ATOM   2553 C  CB    . GLU A 1 331 ? -13.488 -18.226 -12.118 1.00 61.54  ? 1548 GLU A CB    1 
ATOM   2554 N  N     . GLY A 1 332 ? -12.745 -18.917 -15.138 1.00 77.58  ? 1549 GLY A N     1 
ATOM   2555 C  CA    . GLY A 1 332 ? -11.722 -19.416 -16.040 1.00 82.47  ? 1549 GLY A CA    1 
ATOM   2556 C  C     . GLY A 1 332 ? -10.379 -18.787 -15.710 1.00 80.66  ? 1549 GLY A C     1 
ATOM   2557 O  O     . GLY A 1 332 ? -10.305 -17.649 -15.240 1.00 94.15  ? 1549 GLY A O     1 
ATOM   2558 N  N     . ASP A 1 333 ? -9.320  -19.540 -15.925 1.00 74.54  ? 1550 ASP A N     1 
ATOM   2559 C  CA    . ASP A 1 333 ? -7.952  -19.112 -15.645 1.00 75.41  ? 1550 ASP A CA    1 
ATOM   2560 C  C     . ASP A 1 333 ? -7.305  -18.861 -17.002 1.00 82.42  ? 1550 ASP A C     1 
ATOM   2561 O  O     . ASP A 1 333 ? -7.006  -19.809 -17.739 1.00 82.79  ? 1550 ASP A O     1 
ATOM   2562 C  CB    . ASP A 1 333 ? -7.209  -20.168 -14.825 1.00 83.79  ? 1550 ASP A CB    1 
ATOM   2563 C  CG    . ASP A 1 333 ? -5.852  -19.696 -14.319 1.00 88.64  ? 1550 ASP A CG    1 
ATOM   2564 O  OD1   . ASP A 1 333 ? -5.259  -18.764 -14.915 1.00 87.60  ? 1550 ASP A OD1   1 
ATOM   2565 O  OD2   . ASP A 1 333 ? -5.365  -20.289 -13.330 1.00 87.40  ? 1550 ASP A OD2   1 
ATOM   2566 N  N     . TYR A 1 334 ? -7.160  -17.583 -17.361 1.00 83.56  ? 1551 TYR A N     1 
ATOM   2567 C  CA    . TYR A 1 334 ? -6.580  -17.178 -18.637 1.00 80.28  ? 1551 TYR A CA    1 
ATOM   2568 C  C     . TYR A 1 334 ? -5.207  -16.530 -18.477 1.00 81.58  ? 1551 TYR A C     1 
ATOM   2569 O  O     . TYR A 1 334 ? -4.758  -15.811 -19.375 1.00 93.15  ? 1551 TYR A O     1 
ATOM   2570 C  CB    . TYR A 1 334 ? -7.539  -16.240 -19.369 1.00 74.25  ? 1551 TYR A CB    1 
ATOM   2571 C  CG    . TYR A 1 334 ? -8.978  -16.716 -19.321 1.00 77.51  ? 1551 TYR A CG    1 
ATOM   2572 C  CD1   . TYR A 1 334 ? -9.442  -17.690 -20.210 1.00 83.21  ? 1551 TYR A CD1   1 
ATOM   2573 C  CD2   . TYR A 1 334 ? -9.870  -16.213 -18.368 1.00 64.11  ? 1551 TYR A CD2   1 
ATOM   2574 C  CE1   . TYR A 1 334 ? -10.758 -18.131 -20.164 1.00 81.80  ? 1551 TYR A CE1   1 
ATOM   2575 C  CE2   . TYR A 1 334 ? -11.186 -16.657 -18.312 1.00 62.24  ? 1551 TYR A CE2   1 
ATOM   2576 C  CZ    . TYR A 1 334 ? -11.623 -17.615 -19.212 1.00 73.33  ? 1551 TYR A CZ    1 
ATOM   2577 O  OH    . TYR A 1 334 ? -12.924 -18.067 -19.160 1.00 79.38  ? 1551 TYR A OH    1 
ATOM   2578 N  N     . ARG A 1 335 ? -4.512  -16.808 -17.377 1.00 74.73  ? 1552 ARG A N     1 
ATOM   2579 C  CA    . ARG A 1 335 ? -3.195  -16.229 -17.168 1.00 70.23  ? 1552 ARG A CA    1 
ATOM   2580 C  C     . ARG A 1 335 ? -2.220  -16.823 -18.173 1.00 76.62  ? 1552 ARG A C     1 
ATOM   2581 O  O     . ARG A 1 335 ? -2.248  -18.023 -18.456 1.00 80.14  ? 1552 ARG A O     1 
ATOM   2582 C  CB    . ARG A 1 335 ? -2.721  -16.500 -15.743 1.00 62.58  ? 1552 ARG A CB    1 
ATOM   2583 C  CG    . ARG A 1 335 ? -3.674  -15.934 -14.687 1.00 59.05  ? 1552 ARG A CG    1 
ATOM   2584 C  CD    . ARG A 1 335 ? -3.221  -16.288 -13.284 1.00 57.86  ? 1552 ARG A CD    1 
ATOM   2585 N  NE    . ARG A 1 335 ? -3.671  -17.612 -12.905 1.00 77.82  ? 1552 ARG A NE    1 
ATOM   2586 C  CZ    . ARG A 1 335 ? -3.490  -18.146 -11.702 1.00 84.05  ? 1552 ARG A CZ    1 
ATOM   2587 N  NH1   . ARG A 1 335 ? -2.857  -17.453 -10.764 1.00 79.76  ? 1552 ARG A NH1   1 
ATOM   2588 N  NH2   . ARG A 1 335 ? -3.937  -19.377 -11.445 1.00 76.42  ? 1552 ARG A NH2   1 
ATOM   2589 N  N     . ASP A 1 336 ? -1.410  -15.967 -18.772 1.00 75.41  ? 1553 ASP A N     1 
ATOM   2590 C  CA    . ASP A 1 336 ? -0.568  -16.394 -19.876 1.00 75.27  ? 1553 ASP A CA    1 
ATOM   2591 C  C     . ASP A 1 336 ? 0.793   -16.907 -19.433 1.00 73.61  ? 1553 ASP A C     1 
ATOM   2592 O  O     . ASP A 1 336 ? 1.491   -17.545 -20.236 1.00 64.69  ? 1553 ASP A O     1 
ATOM   2593 C  CB    . ASP A 1 336 ? -0.381  -15.245 -20.866 1.00 84.88  ? 1553 ASP A CB    1 
ATOM   2594 C  CG    . ASP A 1 336 ? -1.602  -15.010 -21.703 1.00 94.03  ? 1553 ASP A CG    1 
ATOM   2595 O  OD1   . ASP A 1 336 ? -1.988  -13.839 -21.889 1.00 97.41  ? 1553 ASP A OD1   1 
ATOM   2596 O  OD2   . ASP A 1 336 ? -2.185  -16.006 -22.160 1.00 99.61  ? 1553 ASP A OD2   1 
ATOM   2597 N  N     . ASN A 1 337 ? 1.224   -16.584 -18.212 1.00 79.75  ? 1554 ASN A N     1 
ATOM   2598 C  CA    . ASN A 1 337 ? 2.555   -16.956 -17.755 1.00 86.11  ? 1554 ASN A CA    1 
ATOM   2599 C  C     . ASN A 1 337 ? 2.529   -18.235 -16.937 1.00 91.41  ? 1554 ASN A C     1 
ATOM   2600 O  O     . ASN A 1 337 ? 3.430   -18.463 -16.119 1.00 98.30  ? 1554 ASN A O     1 
ATOM   2601 C  CB    . ASN A 1 337 ? 3.185   -15.830 -16.940 1.00 97.05  ? 1554 ASN A CB    1 
ATOM   2602 C  CG    . ASN A 1 337 ? 3.524   -14.630 -17.781 1.00 110.71 ? 1554 ASN A CG    1 
ATOM   2603 O  OD1   . ASN A 1 337 ? 2.845   -13.598 -17.717 1.00 114.26 ? 1554 ASN A OD1   1 
ATOM   2604 N  ND2   . ASN A 1 337 ? 4.588   -14.750 -18.582 1.00 113.20 ? 1554 ASN A ND2   1 
ATOM   2605 N  N     . TYR A 1 338 ? 1.533   -19.089 -17.185 1.00 84.80  ? 1555 TYR A N     1 
ATOM   2606 C  CA    . TYR A 1 338 ? 1.360   -20.344 -16.469 1.00 73.91  ? 1555 TYR A CA    1 
ATOM   2607 C  C     . TYR A 1 338 ? 0.869   -21.430 -17.425 1.00 75.74  ? 1555 TYR A C     1 
ATOM   2608 O  O     . TYR A 1 338 ? -0.080  -21.217 -18.186 1.00 81.55  ? 1555 TYR A O     1 
ATOM   2609 C  CB    . TYR A 1 338 ? 0.386   -20.149 -15.309 1.00 67.26  ? 1555 TYR A CB    1 
ATOM   2610 C  CG    . TYR A 1 338 ? 0.987   -19.408 -14.128 1.00 73.68  ? 1555 TYR A CG    1 
ATOM   2611 C  CD1   . TYR A 1 338 ? 2.250   -19.724 -13.665 1.00 84.98  ? 1555 TYR A CD1   1 
ATOM   2612 C  CD2   . TYR A 1 338 ? 0.289   -18.404 -13.476 1.00 78.49  ? 1555 TYR A CD2   1 
ATOM   2613 C  CE1   . TYR A 1 338 ? 2.807   -19.063 -12.595 1.00 98.98  ? 1555 TYR A CE1   1 
ATOM   2614 C  CE2   . TYR A 1 338 ? 0.836   -17.738 -12.392 1.00 88.99  ? 1555 TYR A CE2   1 
ATOM   2615 C  CZ    . TYR A 1 338 ? 2.099   -18.072 -11.958 1.00 103.80 ? 1555 TYR A CZ    1 
ATOM   2616 O  OH    . TYR A 1 338 ? 2.661   -17.411 -10.886 1.00 114.16 ? 1555 TYR A OH    1 
ATOM   2617 N  N     . SER A 1 339 ? 1.533   -22.584 -17.386 1.00 69.99  ? 1556 SER A N     1 
ATOM   2618 C  CA    . SER A 1 339 ? 1.159   -23.739 -18.194 1.00 70.24  ? 1556 SER A CA    1 
ATOM   2619 C  C     . SER A 1 339 ? -0.141  -24.392 -17.705 1.00 62.55  ? 1556 SER A C     1 
ATOM   2620 O  O     . SER A 1 339 ? -0.476  -24.336 -16.517 1.00 68.66  ? 1556 SER A O     1 
ATOM   2621 C  CB    . SER A 1 339 ? 2.287   -24.774 -18.209 1.00 77.48  ? 1556 SER A CB    1 
ATOM   2622 O  OG    . SER A 1 339 ? 2.512   -25.331 -16.921 1.00 75.45  ? 1556 SER A OG    1 
ATOM   2623 N  N     . PRO A 1 340 ? -0.886  -25.034 -18.612 1.00 61.19  ? 1557 PRO A N     1 
ATOM   2624 C  CA    . PRO A 1 340 ? -2.060  -25.831 -18.172 1.00 60.27  ? 1557 PRO A CA    1 
ATOM   2625 C  C     . PRO A 1 340 ? -1.785  -26.733 -16.967 1.00 63.01  ? 1557 PRO A C     1 
ATOM   2626 O  O     . PRO A 1 340 ? -2.535  -26.682 -15.985 1.00 62.03  ? 1557 PRO A O     1 
ATOM   2627 C  CB    . PRO A 1 340 ? -2.397  -26.666 -19.416 1.00 62.22  ? 1557 PRO A CB    1 
ATOM   2628 C  CG    . PRO A 1 340 ? -1.790  -25.902 -20.600 1.00 70.57  ? 1557 PRO A CG    1 
ATOM   2629 C  CD    . PRO A 1 340 ? -0.716  -24.978 -20.083 1.00 60.01  ? 1557 PRO A CD    1 
ATOM   2630 N  N     . GLY A 1 341 ? -0.691  -27.514 -16.987 1.00 68.80  ? 1558 GLY A N     1 
ATOM   2631 C  CA    . GLY A 1 341 ? -0.396  -28.385 -15.859 1.00 63.15  ? 1558 GLY A CA    1 
ATOM   2632 C  C     . GLY A 1 341 ? -0.129  -27.627 -14.572 1.00 72.65  ? 1558 GLY A C     1 
ATOM   2633 O  O     . GLY A 1 341 ? -0.582  -28.037 -13.493 1.00 73.55  ? 1558 GLY A O     1 
ATOM   2634 N  N     . TRP A 1 342 ? 0.612   -26.510 -14.664 1.00 68.51  ? 1559 TRP A N     1 
ATOM   2635 C  CA    . TRP A 1 342 ? 0.784   -25.620 -13.515 1.00 64.68  ? 1559 TRP A CA    1 
ATOM   2636 C  C     . TRP A 1 342 ? -0.560  -25.233 -12.922 1.00 66.64  ? 1559 TRP A C     1 
ATOM   2637 O  O     . TRP A 1 342 ? -0.728  -25.206 -11.696 1.00 76.82  ? 1559 TRP A O     1 
ATOM   2638 C  CB    . TRP A 1 342 ? 1.572   -24.361 -13.903 1.00 73.23  ? 1559 TRP A CB    1 
ATOM   2639 C  CG    . TRP A 1 342 ? 1.891   -23.473 -12.704 1.00 71.90  ? 1559 TRP A CG    1 
ATOM   2640 C  CD1   . TRP A 1 342 ? 3.081   -23.399 -12.024 1.00 66.74  ? 1559 TRP A CD1   1 
ATOM   2641 C  CD2   . TRP A 1 342 ? 0.998   -22.565 -12.041 1.00 65.18  ? 1559 TRP A CD2   1 
ATOM   2642 N  NE1   . TRP A 1 342 ? 2.976   -22.510 -10.983 1.00 67.71  ? 1559 TRP A NE1   1 
ATOM   2643 C  CE2   . TRP A 1 342 ? 1.710   -21.982 -10.974 1.00 66.87  ? 1559 TRP A CE2   1 
ATOM   2644 C  CE3   . TRP A 1 342 ? -0.332  -22.187 -12.248 1.00 76.09  ? 1559 TRP A CE3   1 
ATOM   2645 C  CZ2   . TRP A 1 342 ? 1.134   -21.034 -10.118 1.00 76.71  ? 1559 TRP A CZ2   1 
ATOM   2646 C  CZ3   . TRP A 1 342 ? -0.908  -21.252 -11.389 1.00 79.98  ? 1559 TRP A CZ3   1 
ATOM   2647 C  CH2   . TRP A 1 342 ? -0.173  -20.685 -10.340 1.00 75.68  ? 1559 TRP A CH2   1 
ATOM   2648 N  N     . LYS A 1 343 ? -1.533  -24.938 -13.782 1.00 57.72  ? 1560 LYS A N     1 
ATOM   2649 C  CA    . LYS A 1 343 ? -2.857  -24.551 -13.308 1.00 65.88  ? 1560 LYS A CA    1 
ATOM   2650 C  C     . LYS A 1 343 ? -3.601  -25.722 -12.661 1.00 65.87  ? 1560 LYS A C     1 
ATOM   2651 O  O     . LYS A 1 343 ? -4.271  -25.546 -11.628 1.00 55.78  ? 1560 LYS A O     1 
ATOM   2652 C  CB    . LYS A 1 343 ? -3.644  -23.955 -14.471 1.00 70.83  ? 1560 LYS A CB    1 
ATOM   2653 C  CG    . LYS A 1 343 ? -2.986  -22.703 -15.070 1.00 69.01  ? 1560 LYS A CG    1 
ATOM   2654 C  CD    . LYS A 1 343 ? -3.951  -21.935 -15.949 1.00 70.29  ? 1560 LYS A CD    1 
ATOM   2655 C  CE    . LYS A 1 343 ? -3.276  -20.777 -16.645 1.00 70.24  ? 1560 LYS A CE    1 
ATOM   2656 N  NZ    . LYS A 1 343 ? -3.536  -20.858 -18.098 1.00 71.90  ? 1560 LYS A NZ    1 
ATOM   2657 N  N     . TYR A 1 344 ? -3.515  -26.918 -13.263 1.00 72.68  ? 1561 TYR A N     1 
ATOM   2658 C  CA    . TYR A 1 344 ? -4.111  -28.109 -12.645 1.00 64.07  ? 1561 TYR A CA    1 
ATOM   2659 C  C     . TYR A 1 344 ? -3.627  -28.248 -11.214 1.00 64.47  ? 1561 TYR A C     1 
ATOM   2660 O  O     . TYR A 1 344 ? -4.430  -28.391 -10.278 1.00 55.43  ? 1561 TYR A O     1 
ATOM   2661 C  CB    . TYR A 1 344 ? -3.760  -29.382 -13.408 1.00 53.58  ? 1561 TYR A CB    1 
ATOM   2662 C  CG    . TYR A 1 344 ? -4.047  -29.394 -14.881 1.00 54.71  ? 1561 TYR A CG    1 
ATOM   2663 C  CD1   . TYR A 1 344 ? -4.866  -28.446 -15.477 1.00 57.60  ? 1561 TYR A CD1   1 
ATOM   2664 C  CD2   . TYR A 1 344 ? -3.493  -30.367 -15.683 1.00 56.33  ? 1561 TYR A CD2   1 
ATOM   2665 C  CE1   . TYR A 1 344 ? -5.102  -28.467 -16.848 1.00 62.79  ? 1561 TYR A CE1   1 
ATOM   2666 C  CE2   . TYR A 1 344 ? -3.727  -30.401 -17.047 1.00 67.29  ? 1561 TYR A CE2   1 
ATOM   2667 C  CZ    . TYR A 1 344 ? -4.533  -29.460 -17.627 1.00 67.80  ? 1561 TYR A CZ    1 
ATOM   2668 O  OH    . TYR A 1 344 ? -4.745  -29.529 -18.985 1.00 68.92  ? 1561 TYR A OH    1 
ATOM   2669 N  N     . ASN A 1 345 ? -2.305  -28.177 -11.027 1.00 52.00  ? 1562 ASN A N     1 
ATOM   2670 C  CA    . ASN A 1 345 ? -1.755  -28.349 -9.684  1.00 64.71  ? 1562 ASN A CA    1 
ATOM   2671 C  C     . ASN A 1 345 ? -2.152  -27.201 -8.767  1.00 66.34  ? 1562 ASN A C     1 
ATOM   2672 O  O     . ASN A 1 345 ? -2.394  -27.412 -7.566  1.00 66.03  ? 1562 ASN A O     1 
ATOM   2673 C  CB    . ASN A 1 345 ? -0.239  -28.488 -9.729  1.00 71.50  ? 1562 ASN A CB    1 
ATOM   2674 C  CG    . ASN A 1 345 ? 0.348   -28.677 -8.356  1.00 72.91  ? 1562 ASN A CG    1 
ATOM   2675 O  OD1   . ASN A 1 345 ? 0.257   -29.767 -7.775  1.00 76.62  ? 1562 ASN A OD1   1 
ATOM   2676 N  ND2   . ASN A 1 345 ? 0.925   -27.607 -7.804  1.00 65.44  ? 1562 ASN A ND2   1 
ATOM   2677 N  N     . HIS A 1 346 ? -2.215  -25.977 -9.311  1.00 69.35  ? 1563 HIS A N     1 
ATOM   2678 C  CA    . HIS A 1 346 ? -2.604  -24.823 -8.506  1.00 61.75  ? 1563 HIS A CA    1 
ATOM   2679 C  C     . HIS A 1 346 ? -4.005  -24.998 -7.943  1.00 69.11  ? 1563 HIS A C     1 
ATOM   2680 O  O     . HIS A 1 346 ? -4.216  -24.955 -6.719  1.00 75.76  ? 1563 HIS A O     1 
ATOM   2681 C  CB    . HIS A 1 346 ? -2.520  -23.544 -9.344  1.00 68.48  ? 1563 HIS A CB    1 
ATOM   2682 C  CG    . HIS A 1 346 ? -2.765  -22.299 -8.550  1.00 78.39  ? 1563 HIS A CG    1 
ATOM   2683 N  ND1   . HIS A 1 346 ? -3.904  -21.532 -8.693  1.00 77.77  ? 1563 HIS A ND1   1 
ATOM   2684 C  CD2   . HIS A 1 346 ? -2.043  -21.718 -7.562  1.00 78.22  ? 1563 HIS A CD2   1 
ATOM   2685 C  CE1   . HIS A 1 346 ? -3.867  -20.527 -7.837  1.00 75.35  ? 1563 HIS A CE1   1 
ATOM   2686 N  NE2   . HIS A 1 346 ? -2.748  -20.615 -7.140  1.00 73.82  ? 1563 HIS A NE2   1 
ATOM   2687 N  N     . TRP A 1 347 ? -4.976  -25.244 -8.824  1.00 67.14  ? 1564 TRP A N     1 
ATOM   2688 C  CA    . TRP A 1 347 ? -6.360  -25.328 -8.370  1.00 70.24  ? 1564 TRP A CA    1 
ATOM   2689 C  C     . TRP A 1 347 ? -6.634  -26.597 -7.586  1.00 74.80  ? 1564 TRP A C     1 
ATOM   2690 O  O     . TRP A 1 347 ? -7.562  -26.609 -6.759  1.00 69.16  ? 1564 TRP A O     1 
ATOM   2691 C  CB    . TRP A 1 347 ? -7.309  -25.226 -9.563  1.00 68.14  ? 1564 TRP A CB    1 
ATOM   2692 C  CG    . TRP A 1 347 ? -7.221  -23.885 -10.174 1.00 75.25  ? 1564 TRP A CG    1 
ATOM   2693 C  CD1   . TRP A 1 347 ? -6.705  -23.567 -11.400 1.00 72.65  ? 1564 TRP A CD1   1 
ATOM   2694 C  CD2   . TRP A 1 347 ? -7.603  -22.652 -9.565  1.00 74.86  ? 1564 TRP A CD2   1 
ATOM   2695 N  NE1   . TRP A 1 347 ? -6.762  -22.212 -11.598 1.00 62.59  ? 1564 TRP A NE1   1 
ATOM   2696 C  CE2   . TRP A 1 347 ? -7.310  -21.625 -10.486 1.00 67.03  ? 1564 TRP A CE2   1 
ATOM   2697 C  CE3   . TRP A 1 347 ? -8.180  -22.314 -8.331  1.00 74.53  ? 1564 TRP A CE3   1 
ATOM   2698 C  CZ2   . TRP A 1 347 ? -7.579  -20.288 -10.216 1.00 60.98  ? 1564 TRP A CZ2   1 
ATOM   2699 C  CZ3   . TRP A 1 347 ? -8.442  -20.991 -8.065  1.00 68.41  ? 1564 TRP A CZ3   1 
ATOM   2700 C  CH2   . TRP A 1 347 ? -8.141  -19.994 -9.002  1.00 65.38  ? 1564 TRP A CH2   1 
ATOM   2701 N  N     . GLU A 1 348 ? -5.809  -27.640 -7.778  1.00 64.93  ? 1565 GLU A N     1 
ATOM   2702 C  CA    . GLU A 1 348 ? -5.904  -28.803 -6.913  1.00 65.42  ? 1565 GLU A CA    1 
ATOM   2703 C  C     . GLU A 1 348 ? -5.511  -28.440 -5.492  1.00 62.31  ? 1565 GLU A C     1 
ATOM   2704 O  O     . GLU A 1 348 ? -6.262  -28.707 -4.548  1.00 62.46  ? 1565 GLU A O     1 
ATOM   2705 C  CB    . GLU A 1 348 ? -5.066  -29.945 -7.473  1.00 77.35  ? 1565 GLU A CB    1 
ATOM   2706 C  CG    . GLU A 1 348 ? -5.867  -30.837 -8.438  1.00 87.62  ? 1565 GLU A CG    1 
ATOM   2707 C  CD    . GLU A 1 348 ? -5.034  -31.885 -9.172  1.00 111.54 ? 1565 GLU A CD    1 
ATOM   2708 O  OE1   . GLU A 1 348 ? -3.995  -32.343 -8.624  1.00 117.69 ? 1565 GLU A OE1   1 
ATOM   2709 O  OE2   . GLU A 1 348 ? -5.431  -32.241 -10.311 1.00 121.35 ? 1565 GLU A OE2   1 
ATOM   2710 N  N     . LEU A 1 349 ? -4.362  -27.781 -5.322  1.00 64.06  ? 1566 LEU A N     1 
ATOM   2711 C  CA    . LEU A 1 349 ? -4.002  -27.286 -3.994  1.00 69.34  ? 1566 LEU A CA    1 
ATOM   2712 C  C     . LEU A 1 349 ? -5.132  -26.452 -3.396  1.00 67.61  ? 1566 LEU A C     1 
ATOM   2713 O  O     . LEU A 1 349 ? -5.470  -26.610 -2.216  1.00 70.25  ? 1566 LEU A O     1 
ATOM   2714 C  CB    . LEU A 1 349 ? -2.705  -26.464 -4.063  1.00 73.52  ? 1566 LEU A CB    1 
ATOM   2715 C  CG    . LEU A 1 349 ? -1.373  -27.230 -4.157  1.00 72.38  ? 1566 LEU A CG    1 
ATOM   2716 C  CD1   . LEU A 1 349 ? -0.239  -26.245 -4.373  1.00 65.49  ? 1566 LEU A CD1   1 
ATOM   2717 C  CD2   . LEU A 1 349 ? -1.114  -28.107 -2.924  1.00 48.49  ? 1566 LEU A CD2   1 
ATOM   2718 N  N     . LYS A 1 350 ? -5.762  -25.587 -4.208  1.00 61.27  ? 1567 LYS A N     1 
ATOM   2719 C  CA    . LYS A 1 350 ? -6.839  -24.746 -3.684  1.00 67.95  ? 1567 LYS A CA    1 
ATOM   2720 C  C     . LYS A 1 350 ? -8.153  -25.499 -3.488  1.00 76.11  ? 1567 LYS A C     1 
ATOM   2721 O  O     . LYS A 1 350 ? -9.052  -24.959 -2.835  1.00 87.64  ? 1567 LYS A O     1 
ATOM   2722 C  CB    . LYS A 1 350 ? -7.050  -23.534 -4.594  1.00 65.04  ? 1567 LYS A CB    1 
ATOM   2723 C  CG    . LYS A 1 350 ? -6.040  -22.405 -4.319  1.00 63.10  ? 1567 LYS A CG    1 
ATOM   2724 C  CD    . LYS A 1 350 ? -6.166  -21.283 -5.347  1.00 79.80  ? 1567 LYS A CD    1 
ATOM   2725 C  CE    . LYS A 1 350 ? -7.126  -20.151 -4.891  1.00 89.05  ? 1567 LYS A CE    1 
ATOM   2726 N  NZ    . LYS A 1 350 ? -6.471  -18.784 -4.728  1.00 89.86  ? 1567 LYS A NZ    1 
ATOM   2727 N  N     . GLY A 1 351 ? -8.294  -26.710 -4.038  1.00 66.20  ? 1568 GLY A N     1 
ATOM   2728 C  CA    . GLY A 1 351 ? -9.373  -27.597 -3.651  1.00 64.64  ? 1568 GLY A CA    1 
ATOM   2729 C  C     . GLY A 1 351 ? -10.704 -27.435 -4.353  1.00 74.36  ? 1568 GLY A C     1 
ATOM   2730 O  O     . GLY A 1 351 ? -11.741 -27.795 -3.777  1.00 73.22  ? 1568 GLY A O     1 
ATOM   2731 N  N     . VAL A 1 352 ? -10.711 -26.919 -5.580  1.00 74.81  ? 1569 VAL A N     1 
ATOM   2732 C  CA    . VAL A 1 352 ? -11.931 -26.623 -6.336  1.00 65.60  ? 1569 VAL A CA    1 
ATOM   2733 C  C     . VAL A 1 352 ? -12.615 -27.926 -6.750  1.00 66.08  ? 1569 VAL A C     1 
ATOM   2734 O  O     . VAL A 1 352 ? -12.004 -28.747 -7.441  1.00 63.26  ? 1569 VAL A O     1 
ATOM   2735 C  CB    . VAL A 1 352 ? -11.583 -25.749 -7.553  1.00 57.24  ? 1569 VAL A CB    1 
ATOM   2736 C  CG1   . VAL A 1 352 ? -12.797 -25.443 -8.414  1.00 57.50  ? 1569 VAL A CG1   1 
ATOM   2737 C  CG2   . VAL A 1 352 ? -10.893 -24.477 -7.092  1.00 52.96  ? 1569 VAL A CG2   1 
ATOM   2738 N  N     . PRO A 1 353 ? -13.876 -28.145 -6.388  1.00 63.69  ? 1570 PRO A N     1 
ATOM   2739 C  CA    . PRO A 1 353 ? -14.503 -29.452 -6.645  1.00 65.66  ? 1570 PRO A CA    1 
ATOM   2740 C  C     . PRO A 1 353 ? -14.333 -30.010 -8.058  1.00 64.62  ? 1570 PRO A C     1 
ATOM   2741 O  O     . PRO A 1 353 ? -14.205 -31.233 -8.207  1.00 71.66  ? 1570 PRO A O     1 
ATOM   2742 C  CB    . PRO A 1 353 ? -15.979 -29.178 -6.331  1.00 72.86  ? 1570 PRO A CB    1 
ATOM   2743 C  CG    . PRO A 1 353 ? -15.962 -28.097 -5.310  1.00 68.99  ? 1570 PRO A CG    1 
ATOM   2744 C  CD    . PRO A 1 353 ? -14.709 -27.288 -5.528  1.00 71.46  ? 1570 PRO A CD    1 
ATOM   2745 N  N     . VAL A 1 354 ? -14.363 -29.189 -9.098  1.00 56.78  ? 1571 VAL A N     1 
ATOM   2746 C  CA    . VAL A 1 354 ? -14.275 -29.689 -10.465 1.00 60.83  ? 1571 VAL A CA    1 
ATOM   2747 C  C     . VAL A 1 354 ? -13.330 -28.807 -11.258 1.00 72.04  ? 1571 VAL A C     1 
ATOM   2748 O  O     . VAL A 1 354 ? -13.440 -27.575 -11.225 1.00 76.80  ? 1571 VAL A O     1 
ATOM   2749 C  CB    . VAL A 1 354 ? -15.641 -29.718 -11.185 1.00 65.28  ? 1571 VAL A CB    1 
ATOM   2750 C  CG1   . VAL A 1 354 ? -15.473 -30.097 -12.695 1.00 49.55  ? 1571 VAL A CG1   1 
ATOM   2751 C  CG2   . VAL A 1 354 ? -16.583 -30.646 -10.493 1.00 70.26  ? 1571 VAL A CG2   1 
ATOM   2752 N  N     . ARG A 1 355 ? -12.453 -29.406 -12.051 1.00 63.74  ? 1572 ARG A N     1 
ATOM   2753 C  CA    . ARG A 1 355 ? -11.674 -28.711 -12.997 1.00 62.88  ? 1572 ARG A CA    1 
ATOM   2754 C  C     . ARG A 1 355 ? -12.149 -29.115 -14.374 1.00 69.24  ? 1572 ARG A C     1 
ATOM   2755 O  O     . ARG A 1 355 ? -12.427 -30.200 -14.593 1.00 72.32  ? 1572 ARG A O     1 
ATOM   2756 C  CB    . ARG A 1 355 ? -10.262 -29.154 -12.851 1.00 72.88  ? 1572 ARG A CB    1 
ATOM   2757 C  CG    . ARG A 1 355 ? -9.390  -28.870 -14.026 1.00 67.83  ? 1572 ARG A CG    1 
ATOM   2758 C  CD    . ARG A 1 355 ? -7.998  -29.188 -13.701 1.00 56.96  ? 1572 ARG A CD    1 
ATOM   2759 N  NE    . ARG A 1 355 ? -7.540  -30.381 -14.320 1.00 79.26  ? 1572 ARG A NE    1 
ATOM   2760 C  CZ    . ARG A 1 355 ? -6.944  -31.351 -13.680 1.00 92.43  ? 1572 ARG A CZ    1 
ATOM   2761 N  NH1   . ARG A 1 355 ? -6.757  -31.305 -12.401 1.00 55.07  ? 1572 ARG A NH1   1 
ATOM   2762 N  NH2   . ARG A 1 355 ? -6.552  -32.372 -14.351 1.00 116.49 ? 1572 ARG A NH2   1 
ATOM   2763 N  N     . ILE A 1 356 ? -12.283 -28.205 -15.293 1.00 70.22  ? 1573 ILE A N     1 
ATOM   2764 C  CA    . ILE A 1 356 ? -12.650 -28.487 -16.666 1.00 67.77  ? 1573 ILE A CA    1 
ATOM   2765 C  C     . ILE A 1 356 ? -11.428 -28.283 -17.530 1.00 71.35  ? 1573 ILE A C     1 
ATOM   2766 O  O     . ILE A 1 356 ? -10.865 -27.184 -17.583 1.00 76.22  ? 1573 ILE A O     1 
ATOM   2767 C  CB    . ILE A 1 356 ? -13.811 -27.603 -17.133 1.00 67.40  ? 1573 ILE A CB    1 
ATOM   2768 C  CG1   . ILE A 1 356 ? -15.092 -28.036 -16.430 1.00 69.82  ? 1573 ILE A CG1   1 
ATOM   2769 C  CG2   . ILE A 1 356 ? -13.928 -27.625 -18.673 1.00 60.10  ? 1573 ILE A CG2   1 
ATOM   2770 C  CD1   . ILE A 1 356 ? -16.271 -27.185 -16.809 1.00 79.07  ? 1573 ILE A CD1   1 
ATOM   2771 N  N     . GLU A 1 357 ? -10.997 -29.348 -18.171 1.00 79.37  ? 1574 GLU A N     1 
ATOM   2772 C  CA    . GLU A 1 357 ? -10.027 -29.252 -19.246 1.00 86.46  ? 1574 GLU A CA    1 
ATOM   2773 C  C     . GLU A 1 357 ? -10.761 -29.102 -20.571 1.00 93.70  ? 1574 GLU A C     1 
ATOM   2774 O  O     . GLU A 1 357 ? -11.524 -29.996 -20.977 1.00 102.25 ? 1574 GLU A O     1 
ATOM   2775 C  CB    . GLU A 1 357 ? -9.128  -30.479 -19.250 1.00 87.74  ? 1574 GLU A CB    1 
ATOM   2776 C  CG    . GLU A 1 357 ? -8.393  -30.658 -17.938 1.00 91.08  ? 1574 GLU A CG    1 
ATOM   2777 C  CD    . GLU A 1 357 ? -7.412  -31.807 -17.969 1.00 95.93  ? 1574 GLU A CD    1 
ATOM   2778 O  OE1   . GLU A 1 357 ? -7.185  -32.375 -19.068 1.00 104.60 ? 1574 GLU A OE1   1 
ATOM   2779 O  OE2   . GLU A 1 357 ? -6.871  -32.125 -16.888 1.00 92.87  ? 1574 GLU A OE2   1 
ATOM   2780 N  N     . LEU A 1 358 ? -10.554 -27.957 -21.222 1.00 93.10  ? 1575 LEU A N     1 
ATOM   2781 C  CA    . LEU A 1 358 ? -11.107 -27.675 -22.544 1.00 92.70  ? 1575 LEU A CA    1 
ATOM   2782 C  C     . LEU A 1 358 ? -9.957  -27.178 -23.406 1.00 93.65  ? 1575 LEU A C     1 
ATOM   2783 O  O     . LEU A 1 358 ? -9.458  -26.063 -23.199 1.00 92.56  ? 1575 LEU A O     1 
ATOM   2784 C  CB    . LEU A 1 358 ? -12.239 -26.645 -22.497 1.00 91.00  ? 1575 LEU A CB    1 
ATOM   2785 C  CG    . LEU A 1 358 ? -13.112 -26.652 -23.769 1.00 91.83  ? 1575 LEU A CG    1 
ATOM   2786 C  CD1   . LEU A 1 358 ? -14.467 -25.997 -23.490 1.00 89.35  ? 1575 LEU A CD1   1 
ATOM   2787 C  CD2   . LEU A 1 358 ? -12.453 -26.062 -25.043 1.00 87.23  ? 1575 LEU A CD2   1 
ATOM   2788 N  N     . GLY A 1 359 ? -9.541  -28.008 -24.365 1.00 89.51  ? 1576 GLY A N     1 
ATOM   2789 C  CA    . GLY A 1 359 ? -8.516  -27.658 -25.314 1.00 83.94  ? 1576 GLY A CA    1 
ATOM   2790 C  C     . GLY A 1 359 ? -9.073  -27.555 -26.717 1.00 86.93  ? 1576 GLY A C     1 
ATOM   2791 O  O     . GLY A 1 359 ? -10.284 -27.553 -26.932 1.00 94.24  ? 1576 GLY A O     1 
ATOM   2792 N  N     . PHE A 1 360 ? -8.160  -27.512 -27.687 1.00 83.25  ? 1577 PHE A N     1 
ATOM   2793 C  CA    . PHE A 1 360 ? -8.593  -27.360 -29.070 1.00 84.54  ? 1577 PHE A CA    1 
ATOM   2794 C  C     . PHE A 1 360 ? -9.292  -28.622 -29.562 1.00 98.10  ? 1577 PHE A C     1 
ATOM   2795 O  O     . PHE A 1 360 ? -10.359 -28.544 -30.190 1.00 103.67 ? 1577 PHE A O     1 
ATOM   2796 C  CB    . PHE A 1 360 ? -7.400  -27.023 -29.965 1.00 91.96  ? 1577 PHE A CB    1 
ATOM   2797 C  CG    . PHE A 1 360 ? -6.703  -25.725 -29.607 1.00 96.27  ? 1577 PHE A CG    1 
ATOM   2798 C  CD1   . PHE A 1 360 ? -7.342  -24.499 -29.798 1.00 95.66  ? 1577 PHE A CD1   1 
ATOM   2799 C  CD2   . PHE A 1 360 ? -5.410  -25.733 -29.087 1.00 94.26  ? 1577 PHE A CD2   1 
ATOM   2800 C  CE1   . PHE A 1 360 ? -6.713  -23.318 -29.478 1.00 99.03  ? 1577 PHE A CE1   1 
ATOM   2801 C  CE2   . PHE A 1 360 ? -4.772  -24.552 -28.764 1.00 99.73  ? 1577 PHE A CE2   1 
ATOM   2802 C  CZ    . PHE A 1 360 ? -5.423  -23.337 -28.958 1.00 101.98 ? 1577 PHE A CZ    1 
ATOM   2803 N  N     . LYS A 1 361 ? -8.720  -29.797 -29.274 1.00 104.74 ? 1578 LYS A N     1 
ATOM   2804 C  CA    . LYS A 1 361 ? -9.385  -31.041 -29.654 1.00 102.38 ? 1578 LYS A CA    1 
ATOM   2805 C  C     . LYS A 1 361 ? -10.754 -31.180 -28.986 1.00 101.16 ? 1578 LYS A C     1 
ATOM   2806 O  O     . LYS A 1 361 ? -11.671 -31.767 -29.576 1.00 99.14  ? 1578 LYS A O     1 
ATOM   2807 C  CB    . LYS A 1 361 ? -8.483  -32.240 -29.333 1.00 92.01  ? 1578 LYS A CB    1 
ATOM   2808 N  N     . ASP A 1 362 ? -10.931 -30.617 -27.784 1.00 99.53  ? 1579 ASP A N     1 
ATOM   2809 C  CA    . ASP A 1 362 ? -12.224 -30.721 -27.110 1.00 98.42  ? 1579 ASP A CA    1 
ATOM   2810 C  C     . ASP A 1 362 ? -13.273 -29.841 -27.781 1.00 98.23  ? 1579 ASP A C     1 
ATOM   2811 O  O     . ASP A 1 362 ? -14.401 -30.282 -28.031 1.00 89.68  ? 1579 ASP A O     1 
ATOM   2812 C  CB    . ASP A 1 362 ? -12.071 -30.368 -25.631 1.00 100.38 ? 1579 ASP A CB    1 
ATOM   2813 C  CG    . ASP A 1 362 ? -11.164 -31.334 -24.901 1.00 111.02 ? 1579 ASP A CG    1 
ATOM   2814 O  OD1   . ASP A 1 362 ? -11.194 -32.529 -25.258 1.00 120.25 ? 1579 ASP A OD1   1 
ATOM   2815 O  OD2   . ASP A 1 362 ? -10.416 -30.915 -23.992 1.00 111.86 ? 1579 ASP A OD2   1 
ATOM   2816 N  N     . LEU A 1 363 ? -12.919 -28.592 -28.086 1.00 108.57 ? 1580 LEU A N     1 
ATOM   2817 C  CA    . LEU A 1 363 ? -13.869 -27.700 -28.735 1.00 105.42 ? 1580 LEU A CA    1 
ATOM   2818 C  C     . LEU A 1 363 ? -14.149 -28.129 -30.169 1.00 106.45 ? 1580 LEU A C     1 
ATOM   2819 O  O     . LEU A 1 363 ? -15.231 -27.842 -30.690 1.00 116.32 ? 1580 LEU A O     1 
ATOM   2820 C  CB    . LEU A 1 363 ? -13.375 -26.248 -28.673 1.00 100.71 ? 1580 LEU A CB    1 
ATOM   2821 C  CG    . LEU A 1 363 ? -12.205 -25.719 -29.512 1.00 103.28 ? 1580 LEU A CG    1 
ATOM   2822 C  CD1   . LEU A 1 363 ? -12.597 -25.374 -30.966 1.00 107.45 ? 1580 LEU A CD1   1 
ATOM   2823 C  CD2   . LEU A 1 363 ? -11.595 -24.501 -28.810 1.00 97.94  ? 1580 LEU A CD2   1 
ATOM   2824 N  N     . GLN A 1 364 ? -13.217 -28.836 -30.807 1.00 100.13 ? 1581 GLN A N     1 
ATOM   2825 C  CA    . GLN A 1 364 ? -13.486 -29.301 -32.159 1.00 101.68 ? 1581 GLN A CA    1 
ATOM   2826 C  C     . GLN A 1 364 ? -14.490 -30.438 -32.156 1.00 109.00 ? 1581 GLN A C     1 
ATOM   2827 O  O     . GLN A 1 364 ? -15.107 -30.705 -33.192 1.00 113.43 ? 1581 GLN A O     1 
ATOM   2828 C  CB    . GLN A 1 364 ? -12.193 -29.738 -32.849 1.00 101.09 ? 1581 GLN A CB    1 
ATOM   2829 N  N     . ASN A 1 365 ? -14.623 -31.144 -31.033 1.00 115.63 ? 1582 ASN A N     1 
ATOM   2830 C  CA    . ASN A 1 365 ? -15.677 -32.130 -30.827 1.00 122.95 ? 1582 ASN A CA    1 
ATOM   2831 C  C     . ASN A 1 365 ? -16.815 -31.599 -29.967 1.00 121.46 ? 1582 ASN A C     1 
ATOM   2832 O  O     . ASN A 1 365 ? -17.642 -32.390 -29.497 1.00 118.47 ? 1582 ASN A O     1 
ATOM   2833 C  CB    . ASN A 1 365 ? -15.103 -33.405 -30.220 1.00 122.37 ? 1582 ASN A CB    1 
ATOM   2834 C  CG    . ASN A 1 365 ? -14.265 -34.166 -31.206 1.00 125.57 ? 1582 ASN A CG    1 
ATOM   2835 O  OD1   . ASN A 1 365 ? -13.279 -33.639 -31.718 1.00 122.02 ? 1582 ASN A OD1   1 
ATOM   2836 N  ND2   . ASN A 1 365 ? -14.657 -35.403 -31.499 1.00 131.82 ? 1582 ASN A ND2   1 
ATOM   2837 N  N     . ASP A 1 366 ? -16.845 -30.288 -29.766 1.00 123.57 ? 1583 ASP A N     1 
ATOM   2838 C  CA    . ASP A 1 366 ? -17.910 -29.615 -29.014 1.00 126.31 ? 1583 ASP A CA    1 
ATOM   2839 C  C     . ASP A 1 366 ? -18.179 -30.304 -27.690 1.00 117.50 ? 1583 ASP A C     1 
ATOM   2840 O  O     . ASP A 1 366 ? -19.242 -30.775 -27.439 1.00 120.82 ? 1583 ASP A O     1 
ATOM   2841 C  CB    . ASP A 1 366 ? -19.173 -29.601 -29.877 1.00 133.65 ? 1583 ASP A CB    1 
ATOM   2842 C  CG    . ASP A 1 366 ? -20.010 -28.406 -29.667 1.00 137.44 ? 1583 ASP A CG    1 
ATOM   2843 O  OD1   . ASP A 1 366 ? -21.146 -28.552 -29.218 1.00 138.34 ? 1583 ASP A OD1   1 
ATOM   2844 O  OD2   . ASP A 1 366 ? -19.554 -27.310 -29.971 1.00 140.08 ? 1583 ASP A OD2   1 
ATOM   2845 N  N     . GLN A 1 367 ? -17.191 -30.347 -26.846 1.00 103.63 ? 1584 GLN A N     1 
ATOM   2846 C  CA    . GLN A 1 367 ? -17.265 -31.077 -25.592 1.00 96.99  ? 1584 GLN A CA    1 
ATOM   2847 C  C     . GLN A 1 367 ? -16.174 -30.564 -24.666 1.00 90.01  ? 1584 GLN A C     1 
ATOM   2848 O  O     . GLN A 1 367 ? -15.422 -29.645 -25.004 1.00 85.85  ? 1584 GLN A O     1 
ATOM   2849 C  CB    . GLN A 1 367 ? -17.124 -32.574 -25.832 1.00 101.31 ? 1584 GLN A CB    1 
ATOM   2850 C  CG    . GLN A 1 367 ? -15.728 -32.950 -26.227 1.00 102.57 ? 1584 GLN A CG    1 
ATOM   2851 C  CD    . GLN A 1 367 ? -15.613 -34.400 -26.571 1.00 107.99 ? 1584 GLN A CD    1 
ATOM   2852 O  OE1   . GLN A 1 367 ? -16.549 -34.989 -27.096 1.00 113.69 ? 1584 GLN A OE1   1 
ATOM   2853 N  NE2   . GLN A 1 367 ? -14.460 -34.990 -26.286 1.00 108.44 ? 1584 GLN A NE2   1 
ATOM   2854 N  N     . PHE A 1 368 ? -16.062 -31.209 -23.508 1.00 86.71  ? 1585 PHE A N     1 
ATOM   2855 C  CA    . PHE A 1 368 ? -14.991 -30.894 -22.571 1.00 78.41  ? 1585 PHE A CA    1 
ATOM   2856 C  C     . PHE A 1 368 ? -14.845 -32.044 -21.581 1.00 74.77  ? 1585 PHE A C     1 
ATOM   2857 O  O     . PHE A 1 368 ? -15.668 -32.964 -21.545 1.00 80.51  ? 1585 PHE A O     1 
ATOM   2858 C  CB    . PHE A 1 368 ? -15.259 -29.569 -21.864 1.00 76.86  ? 1585 PHE A CB    1 
ATOM   2859 C  CG    . PHE A 1 368 ? -16.553 -29.533 -21.130 1.00 88.58  ? 1585 PHE A CG    1 
ATOM   2860 C  CD1   . PHE A 1 368 ? -17.752 -29.355 -21.811 1.00 94.40  ? 1585 PHE A CD1   1 
ATOM   2861 C  CD2   . PHE A 1 368 ? -16.580 -29.669 -19.752 1.00 90.76  ? 1585 PHE A CD2   1 
ATOM   2862 C  CE1   . PHE A 1 368 ? -18.947 -29.318 -21.133 1.00 94.50  ? 1585 PHE A CE1   1 
ATOM   2863 C  CE2   . PHE A 1 368 ? -17.780 -29.640 -19.065 1.00 93.69  ? 1585 PHE A CE2   1 
ATOM   2864 C  CZ    . PHE A 1 368 ? -18.962 -29.463 -19.755 1.00 92.08  ? 1585 PHE A CZ    1 
ATOM   2865 N  N     . VAL A 1 369 ? -13.775 -31.996 -20.785 1.00 62.30  ? 1586 VAL A N     1 
ATOM   2866 C  CA    . VAL A 1 369 ? -13.499 -33.011 -19.773 1.00 69.07  ? 1586 VAL A CA    1 
ATOM   2867 C  C     . VAL A 1 369 ? -13.664 -32.382 -18.403 1.00 62.77  ? 1586 VAL A C     1 
ATOM   2868 O  O     . VAL A 1 369 ? -13.141 -31.295 -18.158 1.00 65.55  ? 1586 VAL A O     1 
ATOM   2869 C  CB    . VAL A 1 369 ? -12.079 -33.599 -19.908 1.00 76.75  ? 1586 VAL A CB    1 
ATOM   2870 C  CG1   . VAL A 1 369 ? -11.955 -34.843 -19.064 1.00 75.01  ? 1586 VAL A CG1   1 
ATOM   2871 C  CG2   . VAL A 1 369 ? -11.717 -33.897 -21.366 1.00 76.02  ? 1586 VAL A CG2   1 
ATOM   2872 N  N     . ALA A 1 370 ? -14.404 -33.037 -17.515 1.00 58.72  ? 1587 ALA A N     1 
ATOM   2873 C  CA    . ALA A 1 370 ? -14.514 -32.590 -16.132 1.00 66.47  ? 1587 ALA A CA    1 
ATOM   2874 C  C     . ALA A 1 370 ? -13.821 -33.594 -15.217 1.00 62.42  ? 1587 ALA A C     1 
ATOM   2875 O  O     . ALA A 1 370 ? -13.985 -34.804 -15.371 1.00 66.53  ? 1587 ALA A O     1 
ATOM   2876 C  CB    . ALA A 1 370 ? -15.974 -32.387 -15.709 1.00 69.98  ? 1587 ALA A CB    1 
ATOM   2877 N  N     . VAL A 1 371 ? -13.068 -33.074 -14.250 1.00 55.42  ? 1588 VAL A N     1 
ATOM   2878 C  CA    . VAL A 1 371 ? -12.195 -33.844 -13.380 1.00 53.50  ? 1588 VAL A CA    1 
ATOM   2879 C  C     . VAL A 1 371 ? -12.485 -33.485 -11.928 1.00 63.60  ? 1588 VAL A C     1 
ATOM   2880 O  O     . VAL A 1 371 ? -12.390 -32.314 -11.544 1.00 72.84  ? 1588 VAL A O     1 
ATOM   2881 C  CB    . VAL A 1 371 ? -10.716 -33.544 -13.696 1.00 63.45  ? 1588 VAL A CB    1 
ATOM   2882 C  CG1   . VAL A 1 371 ? -9.813  -34.625 -13.092 1.00 65.92  ? 1588 VAL A CG1   1 
ATOM   2883 C  CG2   . VAL A 1 371 ? -10.478 -33.348 -15.237 1.00 54.79  ? 1588 VAL A CG2   1 
ATOM   2884 N  N     . ARG A 1 372 ? -12.748 -34.501 -11.110 1.00 59.10  ? 1589 ARG A N     1 
ATOM   2885 C  CA    . ARG A 1 372 ? -13.170 -34.292 -9.731  1.00 61.14  ? 1589 ARG A CA    1 
ATOM   2886 C  C     . ARG A 1 372 ? -11.969 -34.108 -8.821  1.00 64.26  ? 1589 ARG A C     1 
ATOM   2887 O  O     . ARG A 1 372 ? -11.057 -34.940 -8.812  1.00 67.02  ? 1589 ARG A O     1 
ATOM   2888 C  CB    . ARG A 1 372 ? -13.993 -35.480 -9.232  1.00 65.19  ? 1589 ARG A CB    1 
ATOM   2889 C  CG    . ARG A 1 372 ? -15.460 -35.498 -9.627  1.00 70.88  ? 1589 ARG A CG    1 
ATOM   2890 C  CD    . ARG A 1 372 ? -16.070 -36.811 -9.195  1.00 73.22  ? 1589 ARG A CD    1 
ATOM   2891 N  NE    . ARG A 1 372 ? -16.100 -36.937 -7.740  1.00 65.51  ? 1589 ARG A NE    1 
ATOM   2892 C  CZ    . ARG A 1 372 ? -16.948 -37.732 -7.096  1.00 61.98  ? 1589 ARG A CZ    1 
ATOM   2893 N  NH1   . ARG A 1 372 ? -17.826 -38.461 -7.780  1.00 51.62  ? 1589 ARG A NH1   1 
ATOM   2894 N  NH2   . ARG A 1 372 ? -16.935 -37.793 -5.776  1.00 59.40  ? 1589 ARG A NH2   1 
ATOM   2895 N  N     . ARG A 1 373 ? -12.021 -33.087 -7.966  1.00 64.20  ? 1590 ARG A N     1 
ATOM   2896 C  CA    . ARG A 1 373 ? -10.900 -32.861 -7.056  1.00 62.93  ? 1590 ARG A CA    1 
ATOM   2897 C  C     . ARG A 1 373 ? -10.761 -33.987 -6.042  1.00 66.63  ? 1590 ARG A C     1 
ATOM   2898 O  O     . ARG A 1 373 ? -9.644  -34.299 -5.620  1.00 61.72  ? 1590 ARG A O     1 
ATOM   2899 C  CB    . ARG A 1 373 ? -11.073 -31.537 -6.312  1.00 48.88  ? 1590 ARG A CB    1 
ATOM   2900 C  CG    . ARG A 1 373 ? -10.053 -31.299 -5.244  1.00 46.22  ? 1590 ARG A CG    1 
ATOM   2901 C  CD    . ARG A 1 373 ? -8.620  -31.330 -5.831  1.00 53.78  ? 1590 ARG A CD    1 
ATOM   2902 N  NE    . ARG A 1 373 ? -7.670  -31.018 -4.763  1.00 67.14  ? 1590 ARG A NE    1 
ATOM   2903 C  CZ    . ARG A 1 373 ? -7.175  -31.887 -3.875  1.00 63.47  ? 1590 ARG A CZ    1 
ATOM   2904 N  NH1   . ARG A 1 373 ? -7.501  -33.178 -3.908  1.00 59.63  ? 1590 ARG A NH1   1 
ATOM   2905 N  NH2   . ARG A 1 373 ? -6.339  -31.447 -2.939  1.00 53.71  ? 1590 ARG A NH2   1 
ATOM   2906 N  N     . ASP A 1 374 ? -11.876 -34.613 -5.656  1.00 75.43  ? 1591 ASP A N     1 
ATOM   2907 C  CA    . ASP A 1 374 ? -11.851 -35.630 -4.610  1.00 79.61  ? 1591 ASP A CA    1 
ATOM   2908 C  C     . ASP A 1 374 ? -11.315 -36.961 -5.128  1.00 77.90  ? 1591 ASP A C     1 
ATOM   2909 O  O     . ASP A 1 374 ? -10.460 -37.578 -4.489  1.00 73.67  ? 1591 ASP A O     1 
ATOM   2910 C  CB    . ASP A 1 374 ? -13.261 -35.786 -3.996  1.00 82.80  ? 1591 ASP A CB    1 
ATOM   2911 C  CG    . ASP A 1 374 ? -14.346 -36.290 -4.998  1.00 76.26  ? 1591 ASP A CG    1 
ATOM   2912 O  OD1   . ASP A 1 374 ? -14.078 -36.490 -6.206  1.00 68.60  ? 1591 ASP A OD1   1 
ATOM   2913 O  OD2   . ASP A 1 374 ? -15.507 -36.475 -4.557  1.00 68.32  ? 1591 ASP A OD2   1 
ATOM   2914 N  N     . ASN A 1 375 ? -11.812 -37.400 -6.289  1.00 87.74  ? 1592 ASN A N     1 
ATOM   2915 C  CA    . ASN A 1 375 ? -11.545 -38.697 -6.910  1.00 82.18  ? 1592 ASN A CA    1 
ATOM   2916 C  C     . ASN A 1 375 ? -10.398 -38.692 -7.910  1.00 75.58  ? 1592 ASN A C     1 
ATOM   2917 O  O     . ASN A 1 375 ? -9.710  -39.706 -8.057  1.00 86.77  ? 1592 ASN A O     1 
ATOM   2918 C  CB    . ASN A 1 375 ? -12.802 -39.197 -7.627  1.00 77.16  ? 1592 ASN A CB    1 
ATOM   2919 C  CG    . ASN A 1 375 ? -13.778 -39.825 -6.681  1.00 94.70  ? 1592 ASN A CG    1 
ATOM   2920 O  OD1   . ASN A 1 375 ? -13.547 -39.866 -5.469  1.00 105.91 ? 1592 ASN A OD1   1 
ATOM   2921 N  ND2   . ASN A 1 375 ? -14.873 -40.339 -7.219  1.00 100.74 ? 1592 ASN A ND2   1 
ATOM   2922 N  N     . GLY A 1 376 ? -10.202 -37.597 -8.633  1.00 66.91  ? 1593 GLY A N     1 
ATOM   2923 C  CA    . GLY A 1 376 ? -9.463  -37.638 -9.867  1.00 53.73  ? 1593 GLY A CA    1 
ATOM   2924 C  C     . GLY A 1 376 ? -10.248 -38.157 -11.035 1.00 74.34  ? 1593 GLY A C     1 
ATOM   2925 O  O     . GLY A 1 376 ? -9.723  -38.151 -12.157 1.00 74.27  ? 1593 GLY A O     1 
ATOM   2926 N  N     . ALA A 1 377 ? -11.499 -38.574 -10.810 1.00 74.99  ? 1594 ALA A N     1 
ATOM   2927 C  CA    . ALA A 1 377 ? -12.331 -39.152 -11.859 1.00 74.37  ? 1594 ALA A CA    1 
ATOM   2928 C  C     . ALA A 1 377 ? -12.632 -38.157 -12.973 1.00 70.47  ? 1594 ALA A C     1 
ATOM   2929 O  O     . ALA A 1 377 ? -13.120 -37.058 -12.719 1.00 78.79  ? 1594 ALA A O     1 
ATOM   2930 C  CB    . ALA A 1 377 ? -13.635 -39.659 -11.251 1.00 67.04  ? 1594 ALA A CB    1 
ATOM   2931 N  N     . LYS A 1 378 ? -12.409 -38.588 -14.212 1.00 67.53  ? 1595 LYS A N     1 
ATOM   2932 C  CA    . LYS A 1 378 ? -12.606 -37.790 -15.413 1.00 68.03  ? 1595 LYS A CA    1 
ATOM   2933 C  C     . LYS A 1 378 ? -13.844 -38.260 -16.168 1.00 74.53  ? 1595 LYS A C     1 
ATOM   2934 O  O     . LYS A 1 378 ? -14.035 -39.459 -16.379 1.00 76.51  ? 1595 LYS A O     1 
ATOM   2935 C  CB    . LYS A 1 378 ? -11.379 -37.860 -16.333 1.00 70.02  ? 1595 LYS A CB    1 
ATOM   2936 C  CG    . LYS A 1 378 ? -10.185 -37.054 -15.831 1.00 73.52  ? 1595 LYS A CG    1 
ATOM   2937 C  CD    . LYS A 1 378 ? -8.896  -37.410 -16.576 1.00 84.10  ? 1595 LYS A CD    1 
ATOM   2938 C  CE    . LYS A 1 378 ? -8.538  -36.419 -17.685 1.00 87.95  ? 1595 LYS A CE    1 
ATOM   2939 N  NZ    . LYS A 1 378 ? -7.552  -35.383 -17.211 1.00 87.38  ? 1595 LYS A NZ    1 
ATOM   2940 N  N     . GLN A 1 379 ? -14.650 -37.293 -16.618 1.00 80.02  ? 1596 GLN A N     1 
ATOM   2941 C  CA    . GLN A 1 379 ? -15.918 -37.523 -17.305 1.00 73.74  ? 1596 GLN A CA    1 
ATOM   2942 C  C     . GLN A 1 379 ? -16.025 -36.545 -18.459 1.00 67.84  ? 1596 GLN A C     1 
ATOM   2943 O  O     . GLN A 1 379 ? -15.889 -35.340 -18.255 1.00 79.27  ? 1596 GLN A O     1 
ATOM   2944 C  CB    . GLN A 1 379 ? -17.100 -37.327 -16.353 1.00 73.03  ? 1596 GLN A CB    1 
ATOM   2945 C  CG    . GLN A 1 379 ? -18.430 -37.222 -17.047 1.00 80.78  ? 1596 GLN A CG    1 
ATOM   2946 C  CD    . GLN A 1 379 ? -19.590 -37.263 -16.074 1.00 88.56  ? 1596 GLN A CD    1 
ATOM   2947 O  OE1   . GLN A 1 379 ? -19.395 -37.161 -14.865 1.00 84.35  ? 1596 GLN A OE1   1 
ATOM   2948 N  NE2   . GLN A 1 379 ? -20.807 -37.431 -16.595 1.00 94.02  ? 1596 GLN A NE2   1 
ATOM   2949 N  N     . THR A 1 380 ? -16.247 -37.052 -19.666 1.00 75.43  ? 1597 THR A N     1 
ATOM   2950 C  CA    . THR A 1 380 ? -16.353 -36.209 -20.852 1.00 84.12  ? 1597 THR A CA    1 
ATOM   2951 C  C     . THR A 1 380 ? -17.816 -35.852 -21.089 1.00 86.70  ? 1597 THR A C     1 
ATOM   2952 O  O     . THR A 1 380 ? -18.678 -36.737 -21.172 1.00 86.25  ? 1597 THR A O     1 
ATOM   2953 C  CB    . THR A 1 380 ? -15.750 -36.904 -22.076 1.00 79.03  ? 1597 THR A CB    1 
ATOM   2954 O  OG1   . THR A 1 380 ? -14.343 -37.063 -21.869 1.00 82.21  ? 1597 THR A OG1   1 
ATOM   2955 C  CG2   . THR A 1 380 ? -15.977 -36.087 -23.336 1.00 71.12  ? 1597 THR A CG2   1 
ATOM   2956 N  N     . ILE A 1 381 ? -18.090 -34.554 -21.177 1.00 76.94  ? 1598 ILE A N     1 
ATOM   2957 C  CA    . ILE A 1 381 ? -19.440 -34.034 -21.316 1.00 78.63  ? 1598 ILE A CA    1 
ATOM   2958 C  C     . ILE A 1 381 ? -19.558 -33.339 -22.663 1.00 83.13  ? 1598 ILE A C     1 
ATOM   2959 O  O     . ILE A 1 381 ? -18.717 -32.492 -23.012 1.00 81.24  ? 1598 ILE A O     1 
ATOM   2960 C  CB    . ILE A 1 381 ? -19.800 -33.056 -20.185 1.00 77.59  ? 1598 ILE A CB    1 
ATOM   2961 C  CG1   . ILE A 1 381 ? -19.667 -33.714 -18.810 1.00 70.12  ? 1598 ILE A CG1   1 
ATOM   2962 C  CG2   . ILE A 1 381 ? -21.183 -32.528 -20.409 1.00 83.45  ? 1598 ILE A CG2   1 
ATOM   2963 C  CD1   . ILE A 1 381 ? -20.652 -34.815 -18.565 1.00 92.34  ? 1598 ILE A CD1   1 
ATOM   2964 N  N     . LYS A 1 382 ? -20.623 -33.674 -23.394 1.00 86.85  ? 1599 LYS A N     1 
ATOM   2965 C  CA    . LYS A 1 382 ? -20.978 -32.945 -24.601 1.00 82.97  ? 1599 LYS A CA    1 
ATOM   2966 C  C     . LYS A 1 382 ? -21.367 -31.536 -24.181 1.00 86.76  ? 1599 LYS A C     1 
ATOM   2967 O  O     . LYS A 1 382 ? -22.057 -31.355 -23.171 1.00 83.94  ? 1599 LYS A O     1 
ATOM   2968 C  CB    . LYS A 1 382 ? -22.126 -33.654 -25.328 1.00 73.37  ? 1599 LYS A CB    1 
ATOM   2969 N  N     . ARG A 1 383 ? -20.856 -30.531 -24.901 1.00 90.60  ? 1600 ARG A N     1 
ATOM   2970 C  CA    . ARG A 1 383 ? -21.050 -29.143 -24.476 1.00 85.77  ? 1600 ARG A CA    1 
ATOM   2971 C  C     . ARG A 1 383 ? -22.532 -28.823 -24.251 1.00 97.56  ? 1600 ARG A C     1 
ATOM   2972 O  O     . ARG A 1 383 ? -22.882 -28.055 -23.342 1.00 87.61  ? 1600 ARG A O     1 
ATOM   2973 C  CB    . ARG A 1 383 ? -20.426 -28.191 -25.501 1.00 79.31  ? 1600 ARG A CB    1 
ATOM   2974 C  CG    . ARG A 1 383 ? -20.317 -26.775 -24.991 1.00 91.11  ? 1600 ARG A CG    1 
ATOM   2975 C  CD    . ARG A 1 383 ? -18.926 -26.172 -25.142 1.00 93.20  ? 1600 ARG A CD    1 
ATOM   2976 N  NE    . ARG A 1 383 ? -18.900 -24.815 -24.604 1.00 92.95  ? 1600 ARG A NE    1 
ATOM   2977 C  CZ    . ARG A 1 383 ? -18.058 -23.863 -24.996 1.00 103.35 ? 1600 ARG A CZ    1 
ATOM   2978 N  NH1   . ARG A 1 383 ? -17.156 -24.113 -25.934 1.00 103.71 ? 1600 ARG A NH1   1 
ATOM   2979 N  NH2   . ARG A 1 383 ? -18.123 -22.651 -24.455 1.00 110.27 ? 1600 ARG A NH2   1 
ATOM   2980 N  N     . ALA A 1 384 ? -23.415 -29.421 -25.065 1.00 102.25 ? 1601 ALA A N     1 
ATOM   2981 C  CA    . ALA A 1 384 ? -24.859 -29.207 -24.947 1.00 91.73  ? 1601 ALA A CA    1 
ATOM   2982 C  C     . ALA A 1 384 ? -25.381 -29.573 -23.563 1.00 96.45  ? 1601 ALA A C     1 
ATOM   2983 O  O     . ALA A 1 384 ? -26.068 -28.776 -22.909 1.00 91.58  ? 1601 ALA A O     1 
ATOM   2984 C  CB    . ALA A 1 384 ? -25.587 -30.021 -26.008 1.00 85.52  ? 1601 ALA A CB    1 
ATOM   2985 N  N     . GLN A 1 385 ? -25.047 -30.776 -23.089 1.00 100.58 ? 1602 GLN A N     1 
ATOM   2986 C  CA    . GLN A 1 385 ? -25.551 -31.273 -21.815 1.00 104.11 ? 1602 GLN A CA    1 
ATOM   2987 C  C     . GLN A 1 385 ? -24.890 -30.619 -20.609 1.00 91.89  ? 1602 GLN A C     1 
ATOM   2988 O  O     . GLN A 1 385 ? -25.227 -30.998 -19.472 1.00 83.10  ? 1602 GLN A O     1 
ATOM   2989 C  CB    . GLN A 1 385 ? -25.360 -32.784 -21.741 1.00 121.92 ? 1602 GLN A CB    1 
ATOM   2990 C  CG    . GLN A 1 385 ? -26.170 -33.576 -22.744 1.00 143.56 ? 1602 GLN A CG    1 
ATOM   2991 C  CD    . GLN A 1 385 ? -25.777 -35.047 -22.752 1.00 161.56 ? 1602 GLN A CD    1 
ATOM   2992 O  OE1   . GLN A 1 385 ? -24.701 -35.414 -22.273 1.00 168.03 ? 1602 GLN A OE1   1 
ATOM   2993 N  NE2   . GLN A 1 385 ? -26.650 -35.898 -23.293 1.00 166.36 ? 1602 GLN A NE2   1 
ATOM   2994 N  N     . ALA A 1 386 ? -23.994 -29.648 -20.837 1.00 86.67  ? 1603 ALA A N     1 
ATOM   2995 C  CA    . ALA A 1 386 ? -23.245 -29.022 -19.754 1.00 83.15  ? 1603 ALA A CA    1 
ATOM   2996 C  C     . ALA A 1 386 ? -24.180 -28.555 -18.650 1.00 93.48  ? 1603 ALA A C     1 
ATOM   2997 O  O     . ALA A 1 386 ? -24.084 -28.988 -17.493 1.00 92.50  ? 1603 ALA A O     1 
ATOM   2998 C  CB    . ALA A 1 386 ? -22.430 -27.834 -20.288 1.00 74.48  ? 1603 ALA A CB    1 
ATOM   2999 N  N     . THR A 1 387 ? -25.118 -27.681 -19.017 1.00 100.94 ? 1604 THR A N     1 
ATOM   3000 C  CA    . THR A 1 387 ? -26.002 -27.057 -18.045 1.00 101.32 ? 1604 THR A CA    1 
ATOM   3001 C  C     . THR A 1 387 ? -26.722 -28.071 -17.164 1.00 95.07  ? 1604 THR A C     1 
ATOM   3002 O  O     . THR A 1 387 ? -27.048 -27.759 -16.010 1.00 97.17  ? 1604 THR A O     1 
ATOM   3003 C  CB    . THR A 1 387 ? -27.024 -26.213 -18.794 1.00 108.97 ? 1604 THR A CB    1 
ATOM   3004 O  OG1   . THR A 1 387 ? -28.066 -25.841 -17.891 1.00 119.57 ? 1604 THR A OG1   1 
ATOM   3005 C  CG2   . THR A 1 387 ? -27.619 -27.024 -19.958 1.00 107.59 ? 1604 THR A CG2   1 
ATOM   3006 N  N     . VAL A 1 388 ? -26.926 -29.299 -17.657 1.00 86.55  ? 1605 VAL A N     1 
ATOM   3007 C  CA    . VAL A 1 388 ? -27.725 -30.259 -16.908 1.00 84.88  ? 1605 VAL A CA    1 
ATOM   3008 C  C     . VAL A 1 388 ? -26.824 -31.250 -16.195 1.00 91.53  ? 1605 VAL A C     1 
ATOM   3009 O  O     . VAL A 1 388 ? -27.181 -31.805 -15.144 1.00 89.17  ? 1605 VAL A O     1 
ATOM   3010 C  CB    . VAL A 1 388 ? -28.684 -31.043 -17.826 1.00 87.06  ? 1605 VAL A CB    1 
ATOM   3011 C  CG1   . VAL A 1 388 ? -29.600 -31.926 -16.991 1.00 92.56  ? 1605 VAL A CG1   1 
ATOM   3012 C  CG2   . VAL A 1 388 ? -29.492 -30.089 -18.691 1.00 86.39  ? 1605 VAL A CG2   1 
ATOM   3013 N  N     . GLU A 1 389 ? -25.630 -31.481 -16.755 1.00 98.17  ? 1606 GLU A N     1 
ATOM   3014 C  CA    . GLU A 1 389 ? -24.745 -32.482 -16.174 1.00 89.88  ? 1606 GLU A CA    1 
ATOM   3015 C  C     . GLU A 1 389 ? -23.988 -31.930 -14.973 1.00 85.21  ? 1606 GLU A C     1 
ATOM   3016 O  O     . GLU A 1 389 ? -23.820 -32.635 -13.969 1.00 91.90  ? 1606 GLU A O     1 
ATOM   3017 C  CB    . GLU A 1 389 ? -23.749 -32.956 -17.235 1.00 90.99  ? 1606 GLU A CB    1 
ATOM   3018 C  CG    . GLU A 1 389 ? -24.284 -33.966 -18.251 1.00 105.19 ? 1606 GLU A CG    1 
ATOM   3019 C  CD    . GLU A 1 389 ? -24.724 -35.289 -17.644 1.00 110.09 ? 1606 GLU A CD    1 
ATOM   3020 O  OE1   . GLU A 1 389 ? -24.134 -35.712 -16.620 1.00 114.62 ? 1606 GLU A OE1   1 
ATOM   3021 O  OE2   . GLU A 1 389 ? -25.660 -35.905 -18.210 1.00 105.14 ? 1606 GLU A OE2   1 
ATOM   3022 N  N     . MET A 1 390 ? -23.571 -30.662 -15.032 1.00 74.02  ? 1607 MET A N     1 
ATOM   3023 C  CA    . MET A 1 390 ? -22.691 -30.088 -14.018 1.00 73.25  ? 1607 MET A CA    1 
ATOM   3024 C  C     . MET A 1 390 ? -23.334 -29.974 -12.642 1.00 83.03  ? 1607 MET A C     1 
ATOM   3025 O  O     . MET A 1 390 ? -22.628 -30.161 -11.637 1.00 91.83  ? 1607 MET A O     1 
ATOM   3026 C  CB    . MET A 1 390 ? -22.155 -28.721 -14.471 1.00 74.23  ? 1607 MET A CB    1 
ATOM   3027 C  CG    . MET A 1 390 ? -20.980 -28.192 -13.607 1.00 77.10  ? 1607 MET A CG    1 
ATOM   3028 S  SD    . MET A 1 390 ? -19.574 -29.335 -13.494 1.00 81.42  ? 1607 MET A SD    1 
ATOM   3029 C  CE    . MET A 1 390 ? -19.119 -29.439 -15.225 1.00 78.24  ? 1607 MET A CE    1 
ATOM   3030 N  N     . PRO A 1 391 ? -24.629 -29.652 -12.518 1.00 84.58  ? 1608 PRO A N     1 
ATOM   3031 C  CA    . PRO A 1 391 ? -25.239 -29.704 -11.176 1.00 81.43  ? 1608 PRO A CA    1 
ATOM   3032 C  C     . PRO A 1 391 ? -25.273 -31.122 -10.617 1.00 75.72  ? 1608 PRO A C     1 
ATOM   3033 O  O     . PRO A 1 391 ? -24.853 -31.344 -9.471  1.00 74.04  ? 1608 PRO A O     1 
ATOM   3034 C  CB    . PRO A 1 391 ? -26.642 -29.122 -11.404 1.00 79.41  ? 1608 PRO A CB    1 
ATOM   3035 C  CG    . PRO A 1 391 ? -26.480 -28.222 -12.591 1.00 76.03  ? 1608 PRO A CG    1 
ATOM   3036 C  CD    . PRO A 1 391 ? -25.485 -28.916 -13.473 1.00 84.69  ? 1608 PRO A CD    1 
ATOM   3037 N  N     . LYS A 1 392 ? -25.759 -32.090 -11.401 1.00 78.80  ? 1609 LYS A N     1 
ATOM   3038 C  CA    . LYS A 1 392 ? -25.700 -33.486 -10.973 1.00 82.76  ? 1609 LYS A CA    1 
ATOM   3039 C  C     . LYS A 1 392 ? -24.328 -33.796 -10.389 1.00 87.04  ? 1609 LYS A C     1 
ATOM   3040 O  O     . LYS A 1 392 ? -24.212 -34.205 -9.225  1.00 87.41  ? 1609 LYS A O     1 
ATOM   3041 C  CB    . LYS A 1 392 ? -26.014 -34.428 -12.143 1.00 81.29  ? 1609 LYS A CB    1 
ATOM   3042 N  N     . LEU A 1 393 ? -23.274 -33.518 -11.171 1.00 84.47  ? 1610 LEU A N     1 
ATOM   3043 C  CA    . LEU A 1 393 ? -21.901 -33.787 -10.742 1.00 78.94  ? 1610 LEU A CA    1 
ATOM   3044 C  C     . LEU A 1 393 ? -21.619 -33.182 -9.378  1.00 82.97  ? 1610 LEU A C     1 
ATOM   3045 O  O     . LEU A 1 393 ? -21.169 -33.883 -8.458  1.00 69.37  ? 1610 LEU A O     1 
ATOM   3046 C  CB    . LEU A 1 393 ? -20.891 -33.260 -11.763 1.00 72.01  ? 1610 LEU A CB    1 
ATOM   3047 C  CG    . LEU A 1 393 ? -19.410 -33.603 -11.478 1.00 72.57  ? 1610 LEU A CG    1 
ATOM   3048 C  CD1   . LEU A 1 393 ? -19.160 -35.115 -11.379 1.00 57.25  ? 1610 LEU A CD1   1 
ATOM   3049 C  CD2   . LEU A 1 393 ? -18.445 -32.997 -12.502 1.00 77.00  ? 1610 LEU A CD2   1 
ATOM   3050 N  N     . LEU A 1 394 ? -21.911 -31.882 -9.218  1.00 80.12  ? 1611 LEU A N     1 
ATOM   3051 C  CA    . LEU A 1 394 ? -21.596 -31.226 -7.953  1.00 66.77  ? 1611 LEU A CA    1 
ATOM   3052 C  C     . LEU A 1 394 ? -22.420 -31.831 -6.832  1.00 60.82  ? 1611 LEU A C     1 
ATOM   3053 O  O     . LEU A 1 394 ? -21.888 -32.115 -5.747  1.00 69.68  ? 1611 LEU A O     1 
ATOM   3054 C  CB    . LEU A 1 394 ? -21.824 -29.722 -8.062  1.00 70.12  ? 1611 LEU A CB    1 
ATOM   3055 C  CG    . LEU A 1 394 ? -20.786 -29.002 -8.930  1.00 77.88  ? 1611 LEU A CG    1 
ATOM   3056 C  CD1   . LEU A 1 394 ? -21.386 -27.757 -9.546  1.00 77.23  ? 1611 LEU A CD1   1 
ATOM   3057 C  CD2   . LEU A 1 394 ? -19.488 -28.663 -8.153  1.00 73.60  ? 1611 LEU A CD2   1 
ATOM   3058 N  N     . GLU A 1 395 ? -23.692 -32.145 -7.119  1.00 66.96  ? 1612 GLU A N     1 
ATOM   3059 C  CA    . GLU A 1 395 ? -24.493 -32.966 -6.213  1.00 69.91  ? 1612 GLU A CA    1 
ATOM   3060 C  C     . GLU A 1 395 ? -23.738 -34.248 -5.842  1.00 65.05  ? 1612 GLU A C     1 
ATOM   3061 O  O     . GLU A 1 395 ? -23.423 -34.496 -4.663  1.00 63.18  ? 1612 GLU A O     1 
ATOM   3062 C  CB    . GLU A 1 395 ? -25.852 -33.275 -6.856  1.00 74.96  ? 1612 GLU A CB    1 
ATOM   3063 C  CG    . GLU A 1 395 ? -26.822 -32.072 -6.937  1.00 73.84  ? 1612 GLU A CG    1 
ATOM   3064 C  CD    . GLU A 1 395 ? -28.209 -32.441 -7.487  1.00 68.80  ? 1612 GLU A CD    1 
ATOM   3065 N  N     . THR A 1 396 ? -23.387 -35.043 -6.856  1.00 52.36  ? 1613 THR A N     1 
ATOM   3066 C  CA    . THR A 1 396 ? -22.682 -36.291 -6.596  1.00 72.98  ? 1613 THR A CA    1 
ATOM   3067 C  C     . THR A 1 396 ? -21.452 -36.051 -5.733  1.00 62.85  ? 1613 THR A C     1 
ATOM   3068 O  O     . THR A 1 396 ? -21.212 -36.779 -4.752  1.00 59.71  ? 1613 THR A O     1 
ATOM   3069 C  CB    . THR A 1 396 ? -22.311 -36.993 -7.906  1.00 84.25  ? 1613 THR A CB    1 
ATOM   3070 O  OG1   . THR A 1 396 ? -21.652 -36.062 -8.763  1.00 101.76 ? 1613 THR A OG1   1 
ATOM   3071 C  CG2   . THR A 1 396 ? -23.555 -37.522 -8.610  1.00 79.60  ? 1613 THR A CG2   1 
ATOM   3072 N  N     . ILE A 1 397 ? -20.683 -35.003 -6.048  1.00 56.34  ? 1614 ILE A N     1 
ATOM   3073 C  CA    . ILE A 1 397 ? -19.418 -34.856 -5.340  1.00 61.52  ? 1614 ILE A CA    1 
ATOM   3074 C  C     . ILE A 1 397 ? -19.699 -34.700 -3.857  1.00 69.30  ? 1614 ILE A C     1 
ATOM   3075 O  O     . ILE A 1 397 ? -19.109 -35.396 -3.015  1.00 77.16  ? 1614 ILE A O     1 
ATOM   3076 C  CB    . ILE A 1 397 ? -18.593 -33.692 -5.908  1.00 66.30  ? 1614 ILE A CB    1 
ATOM   3077 C  CG1   . ILE A 1 397 ? -17.867 -34.128 -7.177  1.00 67.44  ? 1614 ILE A CG1   1 
ATOM   3078 C  CG2   . ILE A 1 397 ? -17.550 -33.254 -4.912  1.00 72.05  ? 1614 ILE A CG2   1 
ATOM   3079 C  CD1   . ILE A 1 397 ? -17.429 -32.941 -8.006  1.00 74.05  ? 1614 ILE A CD1   1 
ATOM   3080 N  N     . HIS A 1 398 ? -20.675 -33.844 -3.525  1.00 68.60  ? 1615 HIS A N     1 
ATOM   3081 C  CA    . HIS A 1 398 ? -21.022 -33.650 -2.128  1.00 63.94  ? 1615 HIS A CA    1 
ATOM   3082 C  C     . HIS A 1 398 ? -21.331 -34.991 -1.483  1.00 67.34  ? 1615 HIS A C     1 
ATOM   3083 O  O     . HIS A 1 398 ? -20.728 -35.369 -0.465  1.00 65.62  ? 1615 HIS A O     1 
ATOM   3084 C  CB    . HIS A 1 398 ? -22.210 -32.708 -2.007  1.00 57.95  ? 1615 HIS A CB    1 
ATOM   3085 C  CG    . HIS A 1 398 ? -22.586 -32.404 -0.592  1.00 55.16  ? 1615 HIS A CG    1 
ATOM   3086 N  ND1   . HIS A 1 398 ? -23.596 -33.068 0.068   1.00 54.46  ? 1615 HIS A ND1   1 
ATOM   3087 C  CD2   . HIS A 1 398 ? -22.075 -31.519 0.296   1.00 55.38  ? 1615 HIS A CD2   1 
ATOM   3088 C  CE1   . HIS A 1 398 ? -23.696 -32.607 1.301   1.00 54.51  ? 1615 HIS A CE1   1 
ATOM   3089 N  NE2   . HIS A 1 398 ? -22.786 -31.662 1.463   1.00 61.18  ? 1615 HIS A NE2   1 
ATOM   3090 N  N     . THR A 1 399 ? -22.230 -35.755 -2.109  1.00 62.18  ? 1616 THR A N     1 
ATOM   3091 C  CA    . THR A 1 399 ? -22.615 -37.018 -1.503  1.00 69.72  ? 1616 THR A CA    1 
ATOM   3092 C  C     . THR A 1 399 ? -21.374 -37.860 -1.206  1.00 64.62  ? 1616 THR A C     1 
ATOM   3093 O  O     . THR A 1 399 ? -21.185 -38.304 -0.065  1.00 65.57  ? 1616 THR A O     1 
ATOM   3094 C  CB    . THR A 1 399 ? -23.634 -37.761 -2.381  1.00 70.25  ? 1616 THR A CB    1 
ATOM   3095 O  OG1   . THR A 1 399 ? -24.646 -36.849 -2.843  1.00 60.94  ? 1616 THR A OG1   1 
ATOM   3096 C  CG2   . THR A 1 399 ? -24.286 -38.874 -1.576  1.00 53.36  ? 1616 THR A CG2   1 
ATOM   3097 N  N     . SER A 1 400 ? -20.439 -37.953 -2.167  1.00 50.44  ? 1617 SER A N     1 
ATOM   3098 C  CA    . SER A 1 400 ? -19.295 -38.827 -1.930  1.00 67.87  ? 1617 SER A CA    1 
ATOM   3099 C  C     . SER A 1 400 ? -18.500 -38.338 -0.728  1.00 74.43  ? 1617 SER A C     1 
ATOM   3100 O  O     . SER A 1 400 ? -18.350 -39.069 0.265   1.00 74.69  ? 1617 SER A O     1 
ATOM   3101 C  CB    . SER A 1 400 ? -18.355 -38.861 -3.141  1.00 66.78  ? 1617 SER A CB    1 
ATOM   3102 O  OG    . SER A 1 400 ? -19.033 -39.151 -4.355  1.00 79.94  ? 1617 SER A OG    1 
ATOM   3103 N  N     . MET A 1 401 ? -18.199 -37.030 -0.714  1.00 69.57  ? 1618 MET A N     1 
ATOM   3104 C  CA    . MET A 1 401 ? -17.511 -36.412 0.407   1.00 45.96  ? 1618 MET A CA    1 
ATOM   3105 C  C     . MET A 1 401 ? -18.225 -36.719 1.709   1.00 67.01  ? 1618 MET A C     1 
ATOM   3106 O  O     . MET A 1 401 ? -17.578 -37.066 2.710   1.00 57.49  ? 1618 MET A O     1 
ATOM   3107 C  CB    . MET A 1 401 ? -17.430 -34.886 0.211   1.00 65.89  ? 1618 MET A CB    1 
ATOM   3108 C  CG    . MET A 1 401 ? -16.605 -34.380 -0.976  1.00 65.62  ? 1618 MET A CG    1 
ATOM   3109 S  SD    . MET A 1 401 ? -15.922 -32.744 -0.630  1.00 79.18  ? 1618 MET A SD    1 
ATOM   3110 C  CE    . MET A 1 401 ? -15.553 -32.226 -2.306  1.00 86.15  ? 1618 MET A CE    1 
ATOM   3111 N  N     . TYR A 1 402 ? -19.565 -36.579 1.720   1.00 59.86  ? 1619 TYR A N     1 
ATOM   3112 C  CA    . TYR A 1 402 ? -20.303 -36.808 2.956   1.00 59.26  ? 1619 TYR A CA    1 
ATOM   3113 C  C     . TYR A 1 402 ? -20.269 -38.277 3.359   1.00 61.61  ? 1619 TYR A C     1 
ATOM   3114 O  O     . TYR A 1 402 ? -19.912 -38.606 4.500   1.00 62.66  ? 1619 TYR A O     1 
ATOM   3115 C  CB    . TYR A 1 402 ? -21.750 -36.329 2.848   1.00 63.70  ? 1619 TYR A CB    1 
ATOM   3116 C  CG    . TYR A 1 402 ? -22.501 -36.548 4.153   1.00 68.92  ? 1619 TYR A CG    1 
ATOM   3117 C  CD1   . TYR A 1 402 ? -22.331 -35.682 5.231   1.00 61.61  ? 1619 TYR A CD1   1 
ATOM   3118 C  CD2   . TYR A 1 402 ? -23.352 -37.643 4.323   1.00 74.48  ? 1619 TYR A CD2   1 
ATOM   3119 C  CE1   . TYR A 1 402 ? -22.988 -35.888 6.431   1.00 66.73  ? 1619 TYR A CE1   1 
ATOM   3120 C  CE2   . TYR A 1 402 ? -24.024 -37.856 5.524   1.00 73.77  ? 1619 TYR A CE2   1 
ATOM   3121 C  CZ    . TYR A 1 402 ? -23.837 -36.979 6.572   1.00 74.62  ? 1619 TYR A CZ    1 
ATOM   3122 O  OH    . TYR A 1 402 ? -24.501 -37.193 7.756   1.00 72.03  ? 1619 TYR A OH    1 
ATOM   3123 N  N     . GLU A 1 403 ? -20.628 -39.184 2.445   1.00 56.41  ? 1620 GLU A N     1 
ATOM   3124 C  CA    . GLU A 1 403 ? -20.792 -40.565 2.905   1.00 79.55  ? 1620 GLU A CA    1 
ATOM   3125 C  C     . GLU A 1 403 ? -19.453 -41.160 3.313   1.00 79.94  ? 1620 GLU A C     1 
ATOM   3126 O  O     . GLU A 1 403 ? -19.346 -41.812 4.360   1.00 67.37  ? 1620 GLU A O     1 
ATOM   3127 C  CB    . GLU A 1 403 ? -21.481 -41.420 1.845   1.00 85.61  ? 1620 GLU A CB    1 
ATOM   3128 C  CG    . GLU A 1 403 ? -22.915 -40.991 1.558   1.00 87.64  ? 1620 GLU A CG    1 
ATOM   3129 C  CD    . GLU A 1 403 ? -23.521 -41.775 0.429   1.00 97.97  ? 1620 GLU A CD    1 
ATOM   3130 O  OE1   . GLU A 1 403 ? -24.764 -41.831 0.358   1.00 108.64 ? 1620 GLU A OE1   1 
ATOM   3131 O  OE2   . GLU A 1 403 ? -22.756 -42.339 -0.384  1.00 104.99 ? 1620 GLU A OE2   1 
ATOM   3132 N  N     . ARG A 1 404 ? -18.401 -40.751 2.643   1.00 81.47  ? 1621 ARG A N     1 
ATOM   3133 C  CA    . ARG A 1 404 ? -17.069 -41.129 2.996   1.00 72.01  ? 1621 ARG A CA    1 
ATOM   3134 C  C     . ARG A 1 404 ? -16.798 -40.690 4.342   1.00 72.55  ? 1621 ARG A C     1 
ATOM   3135 O  O     . ARG A 1 404 ? -16.422 -41.446 5.114   1.00 85.92  ? 1621 ARG A O     1 
ATOM   3136 C  CB    . ARG A 1 404 ? -16.087 -40.358 2.209   1.00 78.62  ? 1621 ARG A CB    1 
ATOM   3137 C  CG    . ARG A 1 404 ? -15.645 -41.004 0.951   1.00 94.91  ? 1621 ARG A CG    1 
ATOM   3138 C  CD    . ARG A 1 404 ? -14.373 -40.382 0.482   1.00 104.17 ? 1621 ARG A CD    1 
ATOM   3139 N  NE    . ARG A 1 404 ? -14.289 -40.495 -0.943  1.00 116.11 ? 1621 ARG A NE    1 
ATOM   3140 C  CZ    . ARG A 1 404 ? -14.440 -39.478 -1.766  1.00 123.74 ? 1621 ARG A CZ    1 
ATOM   3141 N  NH1   . ARG A 1 404 ? -14.636 -38.267 -1.316  1.00 126.52 ? 1621 ARG A NH1   1 
ATOM   3142 N  NH2   . ARG A 1 404 ? -14.357 -39.672 -3.045  1.00 121.11 ? 1621 ARG A NH2   1 
ATOM   3143 N  N     . ALA A 1 405 ? -17.049 -39.456 4.645   1.00 68.82  ? 1622 ALA A N     1 
ATOM   3144 C  CA    . ALA A 1 405 ? -16.796 -38.964 5.993   1.00 68.13  ? 1622 ALA A CA    1 
ATOM   3145 C  C     . ALA A 1 405 ? -17.618 -39.732 7.020   1.00 65.36  ? 1622 ALA A C     1 
ATOM   3146 O  O     . ALA A 1 405 ? -17.076 -40.209 8.023   1.00 67.61  ? 1622 ALA A O     1 
ATOM   3147 C  CB    . ALA A 1 405 ? -17.064 -37.451 6.075   1.00 65.99  ? 1622 ALA A CB    1 
ATOM   3148 N  N     . GLU A 1 406 ? -18.909 -39.947 6.745   1.00 71.32  ? 1623 GLU A N     1 
ATOM   3149 C  CA    . GLU A 1 406 ? -19.727 -40.664 7.718   1.00 82.79  ? 1623 GLU A CA    1 
ATOM   3150 C  C     . GLU A 1 406 ? -19.215 -42.092 7.899   1.00 85.05  ? 1623 GLU A C     1 
ATOM   3151 O  O     . GLU A 1 406 ? -19.129 -42.581 9.035   1.00 78.76  ? 1623 GLU A O     1 
ATOM   3152 C  CB    . GLU A 1 406 ? -21.209 -40.595 7.339   1.00 84.50  ? 1623 GLU A CB    1 
ATOM   3153 C  CG    . GLU A 1 406 ? -21.793 -41.746 6.585   1.00 92.58  ? 1623 GLU A CG    1 
ATOM   3154 C  CD    . GLU A 1 406 ? -23.296 -41.640 6.510   1.00 96.38  ? 1623 GLU A CD    1 
ATOM   3155 O  OE1   . GLU A 1 406 ? -23.922 -41.346 7.554   1.00 90.18  ? 1623 GLU A OE1   1 
ATOM   3156 O  OE2   . GLU A 1 406 ? -23.843 -41.820 5.401   1.00 99.77  ? 1623 GLU A OE2   1 
ATOM   3157 N  N     . ARG A 1 407 ? -18.824 -42.760 6.799   1.00 80.06  ? 1624 ARG A N     1 
ATOM   3158 C  CA    . ARG A 1 407 ? -18.212 -44.083 6.922   1.00 82.88  ? 1624 ARG A CA    1 
ATOM   3159 C  C     . ARG A 1 407 ? -17.065 -44.040 7.927   1.00 87.38  ? 1624 ARG A C     1 
ATOM   3160 O  O     . ARG A 1 407 ? -17.011 -44.848 8.863   1.00 98.27  ? 1624 ARG A O     1 
ATOM   3161 C  CB    . ARG A 1 407 ? -17.702 -44.582 5.564   1.00 75.75  ? 1624 ARG A CB    1 
ATOM   3162 C  CG    . ARG A 1 407 ? -18.764 -45.130 4.639   1.00 77.65  ? 1624 ARG A CG    1 
ATOM   3163 C  CD    . ARG A 1 407 ? -18.161 -45.711 3.354   1.00 74.58  ? 1624 ARG A CD    1 
ATOM   3164 N  NE    . ARG A 1 407 ? -18.538 -44.970 2.148   1.00 72.10  ? 1624 ARG A NE    1 
ATOM   3165 C  CZ    . ARG A 1 407 ? -19.788 -44.796 1.702   1.00 81.54  ? 1624 ARG A CZ    1 
ATOM   3166 N  NH1   . ARG A 1 407 ? -20.835 -45.305 2.358   1.00 76.67  ? 1624 ARG A NH1   1 
ATOM   3167 N  NH2   . ARG A 1 407 ? -19.999 -44.104 0.582   1.00 85.03  ? 1624 ARG A NH2   1 
ATOM   3168 N  N     . ASP A 1 408 ? -16.153 -43.072 7.767   1.00 80.18  ? 1625 ASP A N     1 
ATOM   3169 C  CA    . ASP A 1 408 ? -15.027 -42.990 8.686   1.00 80.81  ? 1625 ASP A CA    1 
ATOM   3170 C  C     . ASP A 1 408 ? -15.522 -42.819 10.116  1.00 73.81  ? 1625 ASP A C     1 
ATOM   3171 O  O     . ASP A 1 408 ? -15.031 -43.485 11.044  1.00 67.26  ? 1625 ASP A O     1 
ATOM   3172 C  CB    . ASP A 1 408 ? -14.080 -41.864 8.282   1.00 79.00  ? 1625 ASP A CB    1 
ATOM   3173 C  CG    . ASP A 1 408 ? -12.684 -42.013 8.914   1.00 73.84  ? 1625 ASP A CG    1 
ATOM   3174 O  OD1   . ASP A 1 408 ? -12.167 -43.163 9.056   1.00 69.84  ? 1625 ASP A OD1   1 
ATOM   3175 O  OD2   . ASP A 1 408 ? -12.124 -40.960 9.293   1.00 67.37  ? 1625 ASP A OD2   1 
ATOM   3176 N  N     . LEU A 1 409 ? -16.520 -41.951 10.305  1.00 66.37  ? 1626 LEU A N     1 
ATOM   3177 C  CA    . LEU A 1 409 ? -17.038 -41.724 11.648  1.00 61.86  ? 1626 LEU A CA    1 
ATOM   3178 C  C     . LEU A 1 409 ? -17.571 -43.019 12.237  1.00 72.92  ? 1626 LEU A C     1 
ATOM   3179 O  O     . LEU A 1 409 ? -17.345 -43.311 13.417  1.00 76.82  ? 1626 LEU A O     1 
ATOM   3180 C  CB    . LEU A 1 409 ? -18.136 -40.667 11.624  1.00 59.06  ? 1626 LEU A CB    1 
ATOM   3181 C  CG    . LEU A 1 409 ? -18.795 -40.480 12.988  1.00 55.76  ? 1626 LEU A CG    1 
ATOM   3182 C  CD1   . LEU A 1 409 ? -17.749 -40.135 14.042  1.00 49.01  ? 1626 LEU A CD1   1 
ATOM   3183 C  CD2   . LEU A 1 409 ? -19.831 -39.419 12.921  1.00 57.19  ? 1626 LEU A CD2   1 
ATOM   3184 N  N     . GLN A 1 410 ? -18.243 -43.834 11.418  1.00 77.29  ? 1627 GLN A N     1 
ATOM   3185 C  CA    . GLN A 1 410 ? -18.817 -45.040 11.983  1.00 80.14  ? 1627 GLN A CA    1 
ATOM   3186 C  C     . GLN A 1 410 ? -17.736 -46.072 12.223  1.00 82.77  ? 1627 GLN A C     1 
ATOM   3187 O  O     . GLN A 1 410 ? -17.813 -46.825 13.196  1.00 84.79  ? 1627 GLN A O     1 
ATOM   3188 C  CB    . GLN A 1 410 ? -19.901 -45.577 11.049  1.00 91.33  ? 1627 GLN A CB    1 
ATOM   3189 C  CG    . GLN A 1 410 ? -21.197 -44.734 11.061  1.00 102.76 ? 1627 GLN A CG    1 
ATOM   3190 C  CD    . GLN A 1 410 ? -21.900 -44.674 9.708   1.00 109.66 ? 1627 GLN A CD    1 
ATOM   3191 O  OE1   . GLN A 1 410 ? -21.359 -45.097 8.681   1.00 111.35 ? 1627 GLN A OE1   1 
ATOM   3192 N  NE2   . GLN A 1 410 ? -23.121 -44.158 9.711   1.00 111.55 ? 1627 GLN A NE2   1 
ATOM   3193 N  N     . SER A 1 411 ? -16.661 -46.015 11.433  1.00 89.63  ? 1628 SER A N     1 
ATOM   3194 C  CA    . SER A 1 411 ? -15.494 -46.844 11.671  1.00 87.79  ? 1628 SER A CA    1 
ATOM   3195 C  C     . SER A 1 411 ? -14.745 -46.443 12.927  1.00 96.24  ? 1628 SER A C     1 
ATOM   3196 O  O     . SER A 1 411 ? -13.901 -47.205 13.400  1.00 101.68 ? 1628 SER A O     1 
ATOM   3197 C  CB    . SER A 1 411 ? -14.556 -46.776 10.477  1.00 90.75  ? 1628 SER A CB    1 
ATOM   3198 O  OG    . SER A 1 411 ? -13.224 -46.986 10.908  1.00 105.97 ? 1628 SER A OG    1 
ATOM   3199 N  N     . HIS A 1 412 ? -15.039 -45.271 13.484  1.00 96.75  ? 1629 HIS A N     1 
ATOM   3200 C  CA    . HIS A 1 412 ? -14.337 -44.771 14.658  1.00 93.41  ? 1629 HIS A CA    1 
ATOM   3201 C  C     . HIS A 1 412 ? -15.302 -44.535 15.812  1.00 87.32  ? 1629 HIS A C     1 
ATOM   3202 O  O     . HIS A 1 412 ? -14.960 -43.819 16.761  1.00 81.12  ? 1629 HIS A O     1 
ATOM   3203 C  CB    . HIS A 1 412 ? -13.599 -43.469 14.334  1.00 96.93  ? 1629 HIS A CB    1 
ATOM   3204 C  CG    . HIS A 1 412 ? -12.326 -43.655 13.571  1.00 100.27 ? 1629 HIS A CG    1 
ATOM   3205 N  ND1   . HIS A 1 412 ? -11.086 -43.607 14.174  1.00 100.91 ? 1629 HIS A ND1   1 
ATOM   3206 C  CD2   . HIS A 1 412 ? -12.095 -43.869 12.254  1.00 98.36  ? 1629 HIS A CD2   1 
ATOM   3207 C  CE1   . HIS A 1 412 ? -10.147 -43.794 13.263  1.00 97.98  ? 1629 HIS A CE1   1 
ATOM   3208 N  NE2   . HIS A 1 412 ? -10.733 -43.959 12.090  1.00 99.70  ? 1629 HIS A NE2   1 
ATOM   3209 N  N     . THR A 1 413 ? -16.466 -45.191 15.789  1.00 73.03  ? 1630 THR A N     1 
ATOM   3210 C  CA    . THR A 1 413 ? -17.395 -45.179 16.915  1.00 80.35  ? 1630 THR A CA    1 
ATOM   3211 C  C     . THR A 1 413 ? -17.665 -46.608 17.378  1.00 83.49  ? 1630 THR A C     1 
ATOM   3212 O  O     . THR A 1 413 ? -18.403 -47.359 16.722  1.00 85.86  ? 1630 THR A O     1 
ATOM   3213 C  CB    . THR A 1 413 ? -18.700 -44.483 16.534  1.00 69.93  ? 1630 THR A CB    1 
ATOM   3214 O  OG1   . THR A 1 413 ? -18.399 -43.186 16.006  1.00 83.92  ? 1630 THR A OG1   1 
ATOM   3215 C  CG2   . THR A 1 413 ? -19.608 -44.341 17.753  1.00 56.32  ? 1630 THR A CG2   1 
ATOM   3216 N  N     . LYS A 1 414 ? -17.119 -46.945 18.541  1.00 73.47  ? 1631 LYS A N     1 
ATOM   3217 C  CA    . LYS A 1 414 ? -17.228 -48.264 19.129  1.00 77.03  ? 1631 LYS A CA    1 
ATOM   3218 C  C     . LYS A 1 414 ? -18.026 -48.140 20.423  1.00 93.01  ? 1631 LYS A C     1 
ATOM   3219 O  O     . LYS A 1 414 ? -17.832 -47.189 21.178  1.00 98.12  ? 1631 LYS A O     1 
ATOM   3220 C  CB    . LYS A 1 414 ? -15.820 -48.858 19.384  1.00 60.05  ? 1631 LYS A CB    1 
ATOM   3221 N  N     . LEU A 1 415 ? -18.930 -49.094 20.673  1.00 95.19  ? 1632 LEU A N     1 
ATOM   3222 C  CA    . LEU A 1 415 ? -19.726 -49.159 21.896  1.00 82.41  ? 1632 LEU A CA    1 
ATOM   3223 C  C     . LEU A 1 415 ? -19.250 -50.312 22.778  1.00 81.50  ? 1632 LEU A C     1 
ATOM   3224 O  O     . LEU A 1 415 ? -18.933 -51.394 22.278  1.00 85.48  ? 1632 LEU A O     1 
ATOM   3225 C  CB    . LEU A 1 415 ? -21.220 -49.329 21.580  1.00 79.43  ? 1632 LEU A CB    1 
ATOM   3226 N  N     . THR A 1 416 ? -19.211 -50.079 24.090  1.00 77.84  ? 1633 THR A N     1 
ATOM   3227 C  CA    . THR A 1 416 ? -18.911 -51.114 25.066  1.00 85.50  ? 1633 THR A CA    1 
ATOM   3228 C  C     . THR A 1 416 ? -19.735 -50.838 26.310  1.00 87.84  ? 1633 THR A C     1 
ATOM   3229 O  O     . THR A 1 416 ? -20.254 -49.738 26.500  1.00 83.78  ? 1633 THR A O     1 
ATOM   3230 C  CB    . THR A 1 416 ? -17.419 -51.156 25.441  1.00 91.01  ? 1633 THR A CB    1 
ATOM   3231 N  N     . LYS A 1 417 ? -19.873 -51.857 27.151  1.00 94.19  ? 1634 LYS A N     1 
ATOM   3232 C  CA    . LYS A 1 417 ? -20.348 -51.655 28.509  1.00 93.78  ? 1634 LYS A CA    1 
ATOM   3233 C  C     . LYS A 1 417 ? -19.258 -51.972 29.505  1.00 98.53  ? 1634 LYS A C     1 
ATOM   3234 O  O     . LYS A 1 417 ? -19.472 -51.838 30.716  1.00 104.31 ? 1634 LYS A O     1 
ATOM   3235 C  CB    . LYS A 1 417 ? -21.584 -52.513 28.804  1.00 93.89  ? 1634 LYS A CB    1 
ATOM   3236 C  CG    . LYS A 1 417 ? -22.698 -52.420 27.769  1.00 91.89  ? 1634 LYS A CG    1 
ATOM   3237 C  CD    . LYS A 1 417 ? -24.027 -52.890 28.339  1.00 91.80  ? 1634 LYS A CD    1 
ATOM   3238 C  CE    . LYS A 1 417 ? -25.026 -53.257 27.244  1.00 95.44  ? 1634 LYS A CE    1 
ATOM   3239 N  NZ    . LYS A 1 417 ? -26.192 -54.037 27.773  1.00 98.48  ? 1634 LYS A NZ    1 
ATOM   3240 N  N     . GLN A 1 418 ? -18.088 -52.367 29.014  1.00 93.75  ? 1635 GLN A N     1 
ATOM   3241 C  CA    . GLN A 1 418 ? -16.985 -52.813 29.845  1.00 88.21  ? 1635 GLN A CA    1 
ATOM   3242 C  C     . GLN A 1 418 ? -15.867 -51.790 29.746  1.00 84.35  ? 1635 GLN A C     1 
ATOM   3243 O  O     . GLN A 1 418 ? -15.573 -51.281 28.660  1.00 86.12  ? 1635 GLN A O     1 
ATOM   3244 C  CB    . GLN A 1 418 ? -16.499 -54.213 29.422  1.00 80.75  ? 1635 GLN A CB    1 
ATOM   3245 N  N     . TRP A 1 419 ? -15.292 -51.471 30.911  1.00 88.49  ? 1636 TRP A N     1 
ATOM   3246 C  CA    . TRP A 1 419 ? -14.300 -50.402 31.066  1.00 93.88  ? 1636 TRP A CA    1 
ATOM   3247 C  C     . TRP A 1 419 ? -12.983 -50.737 30.372  1.00 97.25  ? 1636 TRP A C     1 
ATOM   3248 O  O     . TRP A 1 419 ? -12.327 -49.857 29.795  1.00 93.78  ? 1636 TRP A O     1 
ATOM   3249 C  CB    . TRP A 1 419 ? -14.087 -50.187 32.566  1.00 93.21  ? 1636 TRP A CB    1 
ATOM   3250 C  CG    . TRP A 1 419 ? -13.075 -49.196 33.018  1.00 94.03  ? 1636 TRP A CG    1 
ATOM   3251 C  CD1   . TRP A 1 419 ? -12.115 -49.410 33.944  1.00 93.99  ? 1636 TRP A CD1   1 
ATOM   3252 C  CD2   . TRP A 1 419 ? -12.977 -47.807 32.653  1.00 99.51  ? 1636 TRP A CD2   1 
ATOM   3253 N  NE1   . TRP A 1 419 ? -11.390 -48.263 34.153  1.00 99.36  ? 1636 TRP A NE1   1 
ATOM   3254 C  CE2   . TRP A 1 419 ? -11.902 -47.262 33.375  1.00 98.83  ? 1636 TRP A CE2   1 
ATOM   3255 C  CE3   . TRP A 1 419 ? -13.685 -46.977 31.775  1.00 102.39 ? 1636 TRP A CE3   1 
ATOM   3256 C  CZ2   . TRP A 1 419 ? -11.512 -45.928 33.250  1.00 97.04  ? 1636 TRP A CZ2   1 
ATOM   3257 C  CZ3   . TRP A 1 419 ? -13.290 -45.641 31.650  1.00 93.71  ? 1636 TRP A CZ3   1 
ATOM   3258 C  CH2   . TRP A 1 419 ? -12.221 -45.137 32.383  1.00 91.87  ? 1636 TRP A CH2   1 
ATOM   3259 N  N     . ALA A 1 420 ? -12.581 -52.009 30.422  1.00 102.53 ? 1637 ALA A N     1 
ATOM   3260 C  CA    . ALA A 1 420 ? -11.358 -52.447 29.763  1.00 98.09  ? 1637 ALA A CA    1 
ATOM   3261 C  C     . ALA A 1 420 ? -11.492 -52.307 28.255  1.00 94.86  ? 1637 ALA A C     1 
ATOM   3262 O  O     . ALA A 1 420 ? -10.575 -51.827 27.576  1.00 95.19  ? 1637 ALA A O     1 
ATOM   3263 C  CB    . ALA A 1 420 ? -11.047 -53.891 30.149  1.00 102.47 ? 1637 ALA A CB    1 
ATOM   3264 N  N     . GLU A 1 421 ? -12.633 -52.736 27.711  1.00 98.36  ? 1638 GLU A N     1 
ATOM   3265 C  CA    . GLU A 1 421 ? -12.865 -52.564 26.289  1.00 92.30  ? 1638 GLU A CA    1 
ATOM   3266 C  C     . GLU A 1 421 ? -12.985 -51.091 25.942  1.00 99.72  ? 1638 GLU A C     1 
ATOM   3267 O  O     . GLU A 1 421 ? -12.592 -50.688 24.840  1.00 101.89 ? 1638 GLU A O     1 
ATOM   3268 C  CB    . GLU A 1 421 ? -14.116 -53.339 25.860  1.00 81.21  ? 1638 GLU A CB    1 
ATOM   3269 C  CG    . GLU A 1 421 ? -14.014 -53.922 24.462  1.00 78.56  ? 1638 GLU A CG    1 
ATOM   3270 C  CD    . GLU A 1 421 ? -15.266 -54.644 24.033  1.00 101.37 ? 1638 GLU A CD    1 
ATOM   3271 O  OE1   . GLU A 1 421 ? -15.186 -55.858 23.756  1.00 113.14 ? 1638 GLU A OE1   1 
ATOM   3272 O  OE2   . GLU A 1 421 ? -16.336 -54.001 23.971  1.00 109.85 ? 1638 GLU A OE2   1 
ATOM   3273 N  N     . PHE A 1 422 ? -13.467 -50.271 26.890  1.00 110.18 ? 1639 PHE A N     1 
ATOM   3274 C  CA    . PHE A 1 422 ? -13.483 -48.818 26.716  1.00 108.69 ? 1639 PHE A CA    1 
ATOM   3275 C  C     . PHE A 1 422 ? -12.071 -48.283 26.514  1.00 109.74 ? 1639 PHE A C     1 
ATOM   3276 O  O     . PHE A 1 422 ? -11.812 -47.504 25.587  1.00 105.77 ? 1639 PHE A O     1 
ATOM   3277 C  CB    . PHE A 1 422 ? -14.152 -48.156 27.933  1.00 107.10 ? 1639 PHE A CB    1 
ATOM   3278 C  CG    . PHE A 1 422 ? -14.207 -46.631 27.886  1.00 100.42 ? 1639 PHE A CG    1 
ATOM   3279 C  CD1   . PHE A 1 422 ? -15.359 -45.975 27.458  1.00 95.21  ? 1639 PHE A CD1   1 
ATOM   3280 C  CD2   . PHE A 1 422 ? -13.134 -45.863 28.321  1.00 101.04 ? 1639 PHE A CD2   1 
ATOM   3281 C  CE1   . PHE A 1 422 ? -15.429 -44.594 27.426  1.00 98.27  ? 1639 PHE A CE1   1 
ATOM   3282 C  CE2   . PHE A 1 422 ? -13.192 -44.488 28.295  1.00 104.77 ? 1639 PHE A CE2   1 
ATOM   3283 C  CZ    . PHE A 1 422 ? -14.347 -43.849 27.847  1.00 107.25 ? 1639 PHE A CZ    1 
ATOM   3284 N  N     . LEU A 1 423 ? -11.122 -48.752 27.329  1.00 103.77 ? 1640 LEU A N     1 
ATOM   3285 C  CA    . LEU A 1 423 ? -9.789  -48.166 27.291  1.00 93.08  ? 1640 LEU A CA    1 
ATOM   3286 C  C     . LEU A 1 423 ? -8.968  -48.744 26.156  1.00 95.13  ? 1640 LEU A C     1 
ATOM   3287 O  O     . LEU A 1 423 ? -8.136  -48.039 25.572  1.00 93.05  ? 1640 LEU A O     1 
ATOM   3288 C  CB    . LEU A 1 423 ? -9.081  -48.406 28.624  1.00 86.07  ? 1640 LEU A CB    1 
ATOM   3289 C  CG    . LEU A 1 423 ? -9.724  -47.706 29.819  1.00 89.02  ? 1640 LEU A CG    1 
ATOM   3290 C  CD1   . LEU A 1 423 ? -9.047  -48.115 31.126  1.00 89.48  ? 1640 LEU A CD1   1 
ATOM   3291 C  CD2   . LEU A 1 423 ? -9.706  -46.191 29.631  1.00 83.69  ? 1640 LEU A CD2   1 
ATOM   3292 N  N     . GLN A 1 424 ? -9.267  -49.983 25.764  1.00 102.09 ? 1641 GLN A N     1 
ATOM   3293 C  CA    . GLN A 1 424 ? -8.699  -50.527 24.538  1.00 103.01 ? 1641 GLN A CA    1 
ATOM   3294 C  C     . GLN A 1 424 ? -9.139  -49.687 23.341  1.00 96.91  ? 1641 GLN A C     1 
ATOM   3295 O  O     . GLN A 1 424 ? -8.305  -49.103 22.639  1.00 88.83  ? 1641 GLN A O     1 
ATOM   3296 C  CB    . GLN A 1 424 ? -9.106  -52.005 24.375  1.00 90.88  ? 1641 GLN A CB    1 
ATOM   3297 N  N     . PHE A 1 425 ? -10.458 -49.554 23.147  1.00 97.15  ? 1642 PHE A N     1 
ATOM   3298 C  CA    . PHE A 1 425 ? -11.001 -48.710 22.084  1.00 100.32 ? 1642 PHE A CA    1 
ATOM   3299 C  C     . PHE A 1 425 ? -10.413 -47.303 22.104  1.00 101.02 ? 1642 PHE A C     1 
ATOM   3300 O  O     . PHE A 1 425 ? -10.121 -46.731 21.050  1.00 99.76  ? 1642 PHE A O     1 
ATOM   3301 C  CB    . PHE A 1 425 ? -12.528 -48.646 22.193  1.00 106.22 ? 1642 PHE A CB    1 
ATOM   3302 C  CG    . PHE A 1 425 ? -13.219 -49.946 21.874  1.00 119.03 ? 1642 PHE A CG    1 
ATOM   3303 C  CD1   . PHE A 1 425 ? -12.536 -50.989 21.263  1.00 122.75 ? 1642 PHE A CD1   1 
ATOM   3304 C  CD2   . PHE A 1 425 ? -14.557 -50.124 22.192  1.00 124.49 ? 1642 PHE A CD2   1 
ATOM   3305 C  CE1   . PHE A 1 425 ? -13.179 -52.179 20.974  1.00 125.02 ? 1642 PHE A CE1   1 
ATOM   3306 C  CE2   . PHE A 1 425 ? -15.206 -51.313 21.901  1.00 126.37 ? 1642 PHE A CE2   1 
ATOM   3307 C  CZ    . PHE A 1 425 ? -14.515 -52.340 21.293  1.00 125.98 ? 1642 PHE A CZ    1 
ATOM   3308 N  N     . LEU A 1 426 ? -10.256 -46.711 23.288  1.00 98.95  ? 1643 LEU A N     1 
ATOM   3309 C  CA    . LEU A 1 426 ? -9.737  -45.354 23.316  1.00 97.44  ? 1643 LEU A CA    1 
ATOM   3310 C  C     . LEU A 1 426 ? -8.266  -45.307 22.920  1.00 106.81 ? 1643 LEU A C     1 
ATOM   3311 O  O     . LEU A 1 426 ? -7.839  -44.370 22.235  1.00 96.82  ? 1643 LEU A O     1 
ATOM   3312 C  CB    . LEU A 1 426 ? -9.925  -44.757 24.708  1.00 93.28  ? 1643 LEU A CB    1 
ATOM   3313 C  CG    . LEU A 1 426 ? -9.449  -43.313 24.908  1.00 87.09  ? 1643 LEU A CG    1 
ATOM   3314 C  CD1   . LEU A 1 426 ? -10.342 -42.715 25.914  1.00 91.83  ? 1643 LEU A CD1   1 
ATOM   3315 C  CD2   . LEU A 1 426 ? -8.031  -43.227 25.414  1.00 87.17  ? 1643 LEU A CD2   1 
ATOM   3316 N  N     . GLU A 1 427 ? -7.499  -46.336 23.294  1.00 112.60 ? 1644 GLU A N     1 
ATOM   3317 C  CA    . GLU A 1 427 ? -6.096  -46.403 22.913  1.00 102.96 ? 1644 GLU A CA    1 
ATOM   3318 C  C     . GLU A 1 427 ? -5.940  -46.567 21.408  1.00 105.02 ? 1644 GLU A C     1 
ATOM   3319 O  O     . GLU A 1 427 ? -5.001  -46.016 20.819  1.00 99.98  ? 1644 GLU A O     1 
ATOM   3320 C  CB    . GLU A 1 427 ? -5.411  -47.550 23.658  1.00 95.79  ? 1644 GLU A CB    1 
ATOM   3321 N  N     . THR A 1 428 ? -6.848  -47.320 20.768  1.00 103.65 ? 1645 THR A N     1 
ATOM   3322 C  CA    . THR A 1 428 ? -6.821  -47.519 19.320  1.00 101.94 ? 1645 THR A CA    1 
ATOM   3323 C  C     . THR A 1 428 ? -7.378  -46.332 18.528  1.00 110.23 ? 1645 THR A C     1 
ATOM   3324 O  O     . THR A 1 428 ? -7.727  -46.529 17.358  1.00 116.77 ? 1645 THR A O     1 
ATOM   3325 C  CB    . THR A 1 428 ? -7.583  -48.782 18.907  1.00 97.37  ? 1645 THR A CB    1 
ATOM   3326 O  OG1   . THR A 1 428 ? -8.967  -48.476 18.723  1.00 104.65 ? 1645 THR A OG1   1 
ATOM   3327 C  CG2   . THR A 1 428 ? -7.438  -49.871 19.938  1.00 94.26  ? 1645 THR A CG2   1 
ATOM   3328 N  N     . LYS A 1 429 ? -7.529  -45.147 19.136  1.00 101.93 ? 1646 LYS A N     1 
ATOM   3329 C  CA    . LYS A 1 429 ? -7.815  -43.893 18.416  1.00 93.86  ? 1646 LYS A CA    1 
ATOM   3330 C  C     . LYS A 1 429 ? -9.248  -43.804 17.867  1.00 91.49  ? 1646 LYS A C     1 
ATOM   3331 O  O     . LYS A 1 429 ? -9.456  -43.527 16.683  1.00 98.06  ? 1646 LYS A O     1 
ATOM   3332 C  CB    . LYS A 1 429 ? -6.798  -43.661 17.289  1.00 90.42  ? 1646 LYS A CB    1 
ATOM   3333 N  N     . ASN A 1 430 ? -10.243 -44.044 18.725  1.00 80.11  ? 1647 ASN A N     1 
ATOM   3334 C  CA    . ASN A 1 430 ? -11.629 -43.785 18.338  1.00 81.59  ? 1647 ASN A CA    1 
ATOM   3335 C  C     . ASN A 1 430 ? -12.447 -43.441 19.586  1.00 87.41  ? 1647 ASN A C     1 
ATOM   3336 O  O     . ASN A 1 430 ? -11.908 -43.309 20.689  1.00 88.71  ? 1647 ASN A O     1 
ATOM   3337 C  CB    . ASN A 1 430 ? -12.230 -44.935 17.503  1.00 83.19  ? 1647 ASN A CB    1 
ATOM   3338 C  CG    . ASN A 1 430 ? -12.101 -46.304 18.144  1.00 90.92  ? 1647 ASN A CG    1 
ATOM   3339 O  OD1   . ASN A 1 430 ? -11.025 -46.718 18.568  1.00 95.54  ? 1647 ASN A OD1   1 
ATOM   3340 N  ND2   . ASN A 1 430 ? -13.204 -47.044 18.158  1.00 94.30  ? 1647 ASN A ND2   1 
ATOM   3341 N  N     . ILE A 1 431 ? -13.751 -43.205 19.385  1.00 82.84  ? 1648 ILE A N     1 
ATOM   3342 C  CA    . ILE A 1 431 ? -14.643 -42.689 20.426  1.00 92.92  ? 1648 ILE A CA    1 
ATOM   3343 C  C     . ILE A 1 431 ? -15.675 -43.743 20.786  1.00 103.87 ? 1648 ILE A C     1 
ATOM   3344 O  O     . ILE A 1 431 ? -16.022 -44.616 19.979  1.00 107.85 ? 1648 ILE A O     1 
ATOM   3345 C  CB    . ILE A 1 431 ? -15.375 -41.400 20.013  1.00 89.19  ? 1648 ILE A CB    1 
ATOM   3346 C  CG1   . ILE A 1 431 ? -16.134 -41.656 18.720  1.00 81.11  ? 1648 ILE A CG1   1 
ATOM   3347 C  CG2   . ILE A 1 431 ? -14.409 -40.247 19.876  1.00 92.06  ? 1648 ILE A CG2   1 
ATOM   3348 C  CD1   . ILE A 1 431 ? -17.179 -40.651 18.426  1.00 77.29  ? 1648 ILE A CD1   1 
ATOM   3349 N  N     . ILE A 1 432 ? -16.182 -43.647 22.011  1.00 95.72  ? 1649 ILE A N     1 
ATOM   3350 C  CA    . ILE A 1 432 ? -16.872 -44.760 22.641  1.00 92.27  ? 1649 ILE A CA    1 
ATOM   3351 C  C     . ILE A 1 432 ? -18.220 -44.295 23.181  1.00 81.40  ? 1649 ILE A C     1 
ATOM   3352 O  O     . ILE A 1 432 ? -18.282 -43.378 24.007  1.00 75.96  ? 1649 ILE A O     1 
ATOM   3353 C  CB    . ILE A 1 432 ? -16.030 -45.387 23.765  1.00 96.08  ? 1649 ILE A CB    1 
ATOM   3354 C  CG1   . ILE A 1 432 ? -14.641 -45.776 23.245  1.00 91.32  ? 1649 ILE A CG1   1 
ATOM   3355 C  CG2   . ILE A 1 432 ? -16.741 -46.597 24.322  1.00 104.36 ? 1649 ILE A CG2   1 
ATOM   3356 C  CD1   . ILE A 1 432 ? -13.496 -45.063 23.927  1.00 88.78  ? 1649 ILE A CD1   1 
ATOM   3357 N  N     . MET A 1 433 ? -19.292 -44.945 22.747  1.00 67.01  ? 1650 MET A N     1 
ATOM   3358 C  CA    . MET A 1 433 ? -20.561 -44.816 23.439  1.00 77.60  ? 1650 MET A CA    1 
ATOM   3359 C  C     . MET A 1 433 ? -20.661 -45.886 24.524  1.00 85.62  ? 1650 MET A C     1 
ATOM   3360 O  O     . MET A 1 433 ? -20.490 -47.081 24.253  1.00 94.08  ? 1650 MET A O     1 
ATOM   3361 C  CB    . MET A 1 433 ? -21.728 -44.914 22.472  1.00 91.28  ? 1650 MET A CB    1 
ATOM   3362 C  CG    . MET A 1 433 ? -22.822 -43.988 22.923  1.00 102.28 ? 1650 MET A CG    1 
ATOM   3363 S  SD    . MET A 1 433 ? -24.085 -43.750 21.692  1.00 108.29 ? 1650 MET A SD    1 
ATOM   3364 C  CE    . MET A 1 433 ? -23.148 -43.857 20.178  1.00 103.55 ? 1650 MET A CE    1 
ATOM   3365 N  N     . ALA A 1 434 ? -20.882 -45.454 25.754  1.00 81.48  ? 1651 ALA A N     1 
ATOM   3366 C  CA    . ALA A 1 434 ? -20.939 -46.353 26.895  1.00 73.87  ? 1651 ALA A CA    1 
ATOM   3367 C  C     . ALA A 1 434 ? -22.002 -45.856 27.859  1.00 80.53  ? 1651 ALA A C     1 
ATOM   3368 O  O     . ALA A 1 434 ? -22.336 -44.667 27.866  1.00 81.14  ? 1651 ALA A O     1 
ATOM   3369 C  CB    . ALA A 1 434 ? -19.589 -46.456 27.611  1.00 69.11  ? 1651 ALA A CB    1 
ATOM   3370 N  N     . PRO A 1 435 ? -22.542 -46.736 28.696  1.00 83.85  ? 1652 PRO A N     1 
ATOM   3371 C  CA    . PRO A 1 435 ? -23.518 -46.287 29.693  1.00 88.63  ? 1652 PRO A CA    1 
ATOM   3372 C  C     . PRO A 1 435 ? -22.844 -45.524 30.826  1.00 92.28  ? 1652 PRO A C     1 
ATOM   3373 O  O     . PRO A 1 435 ? -21.907 -46.022 31.456  1.00 92.77  ? 1652 PRO A O     1 
ATOM   3374 C  CB    . PRO A 1 435 ? -24.135 -47.598 30.191  1.00 90.37  ? 1652 PRO A CB    1 
ATOM   3375 C  CG    . PRO A 1 435 ? -23.123 -48.613 29.937  1.00 85.60  ? 1652 PRO A CG    1 
ATOM   3376 C  CD    . PRO A 1 435 ? -22.413 -48.201 28.681  1.00 85.15  ? 1652 PRO A CD    1 
ATOM   3377 N  N     . PHE A 1 436 ? -23.388 -44.339 31.131  1.00 95.63  ? 1653 PHE A N     1 
ATOM   3378 C  CA    . PHE A 1 436 ? -22.771 -43.375 32.037  1.00 86.30  ? 1653 PHE A CA    1 
ATOM   3379 C  C     . PHE A 1 436 ? -23.797 -42.927 33.063  1.00 72.42  ? 1653 PHE A C     1 
ATOM   3380 O  O     . PHE A 1 436 ? -24.947 -42.663 32.721  1.00 71.99  ? 1653 PHE A O     1 
ATOM   3381 C  CB    . PHE A 1 436 ? -22.237 -42.160 31.270  1.00 84.48  ? 1653 PHE A CB    1 
ATOM   3382 C  CG    . PHE A 1 436 ? -21.641 -41.101 32.144  1.00 85.15  ? 1653 PHE A CG    1 
ATOM   3383 C  CD1   . PHE A 1 436 ? -20.909 -41.443 33.274  1.00 87.59  ? 1653 PHE A CD1   1 
ATOM   3384 C  CD2   . PHE A 1 436 ? -21.796 -39.756 31.826  1.00 85.26  ? 1653 PHE A CD2   1 
ATOM   3385 C  CE1   . PHE A 1 436 ? -20.358 -40.464 34.080  1.00 93.63  ? 1653 PHE A CE1   1 
ATOM   3386 C  CE2   . PHE A 1 436 ? -21.241 -38.765 32.619  1.00 84.42  ? 1653 PHE A CE2   1 
ATOM   3387 C  CZ    . PHE A 1 436 ? -20.516 -39.119 33.752  1.00 91.74  ? 1653 PHE A CZ    1 
ATOM   3388 N  N     . CYS A 1 437 ? -23.374 -42.870 34.330  1.00 72.72  ? 1654 CYS A N     1 
ATOM   3389 C  CA    . CYS A 1 437 ? -24.237 -42.452 35.435  1.00 86.57  ? 1654 CYS A CA    1 
ATOM   3390 C  C     . CYS A 1 437 ? -24.625 -40.982 35.340  1.00 88.61  ? 1654 CYS A C     1 
ATOM   3391 O  O     . CYS A 1 437 ? -25.586 -40.567 35.990  1.00 95.23  ? 1654 CYS A O     1 
ATOM   3392 C  CB    . CYS A 1 437 ? -23.586 -42.736 36.783  1.00 96.76  ? 1654 CYS A CB    1 
ATOM   3393 S  SG    . CYS A 1 437 ? -22.298 -41.574 37.237  1.00 105.69 ? 1654 CYS A SG    1 
ATOM   3394 N  N     . GLY A 1 438 ? -23.832 -40.172 34.650  1.00 87.19  ? 1655 GLY A N     1 
ATOM   3395 C  CA    . GLY A 1 438 ? -24.076 -38.761 34.490  1.00 78.89  ? 1655 GLY A CA    1 
ATOM   3396 C  C     . GLY A 1 438 ? -23.489 -37.868 35.566  1.00 91.62  ? 1655 GLY A C     1 
ATOM   3397 O  O     . GLY A 1 438 ? -23.279 -36.674 35.302  1.00 93.66  ? 1655 GLY A O     1 
ATOM   3398 N  N     . GLU A 1 439 ? -23.134 -38.415 36.733  1.00 93.94  ? 1656 GLU A N     1 
ATOM   3399 C  CA    . GLU A 1 439 ? -22.688 -37.550 37.814  1.00 92.75  ? 1656 GLU A CA    1 
ATOM   3400 C  C     . GLU A 1 439 ? -21.292 -37.039 37.514  1.00 93.40  ? 1656 GLU A C     1 
ATOM   3401 O  O     . GLU A 1 439 ? -20.529 -37.662 36.769  1.00 87.45  ? 1656 GLU A O     1 
ATOM   3402 C  CB    . GLU A 1 439 ? -22.745 -38.270 39.160  1.00 89.25  ? 1656 GLU A CB    1 
ATOM   3403 C  CG    . GLU A 1 439 ? -24.108 -38.907 39.431  1.00 102.51 ? 1656 GLU A CG    1 
ATOM   3404 C  CD    . GLU A 1 439 ? -25.114 -37.954 40.096  1.00 122.23 ? 1656 GLU A CD    1 
ATOM   3405 O  OE1   . GLU A 1 439 ? -26.114 -38.450 40.665  1.00 126.84 ? 1656 GLU A OE1   1 
ATOM   3406 O  OE2   . GLU A 1 439 ? -24.913 -36.714 40.042  1.00 131.54 ? 1656 GLU A OE2   1 
ATOM   3407 N  N     . ILE A 1 440 ? -20.971 -35.884 38.103  1.00 98.27  ? 1657 ILE A N     1 
ATOM   3408 C  CA    . ILE A 1 440 ? -19.769 -35.151 37.714  1.00 95.31  ? 1657 ILE A CA    1 
ATOM   3409 C  C     . ILE A 1 440 ? -18.515 -35.855 38.220  1.00 95.37  ? 1657 ILE A C     1 
ATOM   3410 O  O     . ILE A 1 440 ? -17.553 -36.038 37.463  1.00 94.15  ? 1657 ILE A O     1 
ATOM   3411 C  CB    . ILE A 1 440 ? -19.850 -33.693 38.200  1.00 97.46  ? 1657 ILE A CB    1 
ATOM   3412 C  CG1   . ILE A 1 440 ? -21.050 -32.987 37.558  1.00 106.35 ? 1657 ILE A CG1   1 
ATOM   3413 C  CG2   . ILE A 1 440 ? -18.553 -32.945 37.887  1.00 93.60  ? 1657 ILE A CG2   1 
ATOM   3414 C  CD1   . ILE A 1 440 ? -22.357 -33.139 38.351  1.00 115.70 ? 1657 ILE A CD1   1 
ATOM   3415 N  N     . SER A 1 441 ? -18.494 -36.228 39.511  1.00 92.96  ? 1658 SER A N     1 
ATOM   3416 C  CA    . SER A 1 441 ? -17.405 -37.039 40.054  1.00 86.65  ? 1658 SER A CA    1 
ATOM   3417 C  C     . SER A 1 441 ? -17.036 -38.192 39.126  1.00 88.87  ? 1658 SER A C     1 
ATOM   3418 O  O     . SER A 1 441 ? -15.847 -38.460 38.898  1.00 98.67  ? 1658 SER A O     1 
ATOM   3419 C  CB    . SER A 1 441 ? -17.732 -37.555 41.462  1.00 86.07  ? 1658 SER A CB    1 
ATOM   3420 O  OG    . SER A 1 441 ? -18.965 -38.243 41.538  1.00 92.66  ? 1658 SER A OG    1 
ATOM   3421 N  N     . CYS A 1 442 ? -18.025 -38.914 38.599  1.00 83.45  ? 1659 CYS A N     1 
ATOM   3422 C  CA    . CYS A 1 442 ? -17.656 -40.110 37.848  1.00 96.07  ? 1659 CYS A CA    1 
ATOM   3423 C  C     . CYS A 1 442 ? -17.082 -39.746 36.489  1.00 96.31  ? 1659 CYS A C     1 
ATOM   3424 O  O     . CYS A 1 442 ? -16.171 -40.419 36.001  1.00 89.50  ? 1659 CYS A O     1 
ATOM   3425 C  CB    . CYS A 1 442 ? -18.853 -41.044 37.683  1.00 103.85 ? 1659 CYS A CB    1 
ATOM   3426 S  SG    . CYS A 1 442 ? -18.512 -42.365 36.478  1.00 107.88 ? 1659 CYS A SG    1 
ATOM   3427 N  N     . GLU A 1 443 ? -17.570 -38.661 35.885  1.00 108.88 ? 1660 GLU A N     1 
ATOM   3428 C  CA    . GLU A 1 443 ? -16.933 -38.147 34.677  1.00 110.68 ? 1660 GLU A CA    1 
ATOM   3429 C  C     . GLU A 1 443 ? -15.482 -37.752 34.948  1.00 112.87 ? 1660 GLU A C     1 
ATOM   3430 O  O     . GLU A 1 443 ? -14.603 -37.933 34.093  1.00 108.55 ? 1660 GLU A O     1 
ATOM   3431 C  CB    . GLU A 1 443 ? -17.736 -36.967 34.139  1.00 107.44 ? 1660 GLU A CB    1 
ATOM   3432 C  CG    . GLU A 1 443 ? -17.367 -36.550 32.731  1.00 108.32 ? 1660 GLU A CG    1 
ATOM   3433 C  CD    . GLU A 1 443 ? -18.385 -35.615 32.091  1.00 95.24  ? 1660 GLU A CD    1 
ATOM   3434 O  OE1   . GLU A 1 443 ? -17.975 -34.818 31.210  1.00 84.16  ? 1660 GLU A OE1   1 
ATOM   3435 O  OE2   . GLU A 1 443 ? -19.584 -35.702 32.446  1.00 93.84  ? 1660 GLU A OE2   1 
ATOM   3436 N  N     . ASP A 1 444 ? -15.222 -37.187 36.133  1.00 118.31 ? 1661 ASP A N     1 
ATOM   3437 C  CA    . ASP A 1 444 ? -13.856 -36.852 36.536  1.00 117.19 ? 1661 ASP A CA    1 
ATOM   3438 C  C     . ASP A 1 444 ? -12.988 -38.102 36.647  1.00 113.90 ? 1661 ASP A C     1 
ATOM   3439 O  O     . ASP A 1 444 ? -11.857 -38.124 36.149  1.00 108.83 ? 1661 ASP A O     1 
ATOM   3440 C  CB    . ASP A 1 444 ? -13.859 -36.088 37.872  1.00 119.25 ? 1661 ASP A CB    1 
ATOM   3441 C  CG    . ASP A 1 444 ? -14.469 -34.686 37.765  1.00 121.90 ? 1661 ASP A CG    1 
ATOM   3442 O  OD1   . ASP A 1 444 ? -15.376 -34.369 38.561  1.00 127.04 ? 1661 ASP A OD1   1 
ATOM   3443 O  OD2   . ASP A 1 444 ? -14.047 -33.892 36.899  1.00 121.90 ? 1661 ASP A OD2   1 
ATOM   3444 N  N     . ARG A 1 445 ? -13.499 -39.148 37.321  1.00 113.55 ? 1662 ARG A N     1 
ATOM   3445 C  CA    . ARG A 1 445 ? -12.731 -40.390 37.481  1.00 108.76 ? 1662 ARG A CA    1 
ATOM   3446 C  C     . ARG A 1 445 ? -12.482 -41.054 36.135  1.00 110.39 ? 1662 ARG A C     1 
ATOM   3447 O  O     . ARG A 1 445 ? -11.403 -41.612 35.894  1.00 119.58 ? 1662 ARG A O     1 
ATOM   3448 C  CB    . ARG A 1 445 ? -13.444 -41.361 38.425  1.00 97.16  ? 1662 ARG A CB    1 
ATOM   3449 N  N     . ILE A 1 446 ? -13.468 -40.981 35.241  1.00 99.05  ? 1663 ILE A N     1 
ATOM   3450 C  CA    . ILE A 1 446 ? -13.325 -41.525 33.896  1.00 92.18  ? 1663 ILE A CA    1 
ATOM   3451 C  C     . ILE A 1 446 ? -12.204 -40.808 33.158  1.00 100.83 ? 1663 ILE A C     1 
ATOM   3452 O  O     . ILE A 1 446 ? -11.295 -41.440 32.602  1.00 103.64 ? 1663 ILE A O     1 
ATOM   3453 C  CB    . ILE A 1 446 ? -14.662 -41.393 33.141  1.00 87.97  ? 1663 ILE A CB    1 
ATOM   3454 C  CG1   . ILE A 1 446 ? -15.679 -42.421 33.646  1.00 97.06  ? 1663 ILE A CG1   1 
ATOM   3455 C  CG2   . ILE A 1 446 ? -14.467 -41.449 31.614  1.00 66.16  ? 1663 ILE A CG2   1 
ATOM   3456 C  CD1   . ILE A 1 446 ? -17.076 -42.151 33.136  1.00 97.22  ? 1663 ILE A CD1   1 
ATOM   3457 N  N     . LYS A 1 447 ? -12.240 -39.470 33.175  1.00 109.46 ? 1664 LYS A N     1 
ATOM   3458 C  CA    . LYS A 1 447 ? -11.237 -38.661 32.482  1.00 117.12 ? 1664 LYS A CA    1 
ATOM   3459 C  C     . LYS A 1 447 ? -9.835  -38.913 33.028  1.00 119.12 ? 1664 LYS A C     1 
ATOM   3460 O  O     . LYS A 1 447 ? -8.872  -39.074 32.264  1.00 122.73 ? 1664 LYS A O     1 
ATOM   3461 C  CB    . LYS A 1 447 ? -11.614 -37.183 32.608  1.00 113.00 ? 1664 LYS A CB    1 
ATOM   3462 C  CG    . LYS A 1 447 ? -10.783 -36.218 31.782  1.00 103.46 ? 1664 LYS A CG    1 
ATOM   3463 C  CD    . LYS A 1 447 ? -10.775 -34.856 32.458  1.00 99.40  ? 1664 LYS A CD    1 
ATOM   3464 C  CE    . LYS A 1 447 ? -10.448 -33.751 31.469  1.00 98.16  ? 1664 LYS A CE    1 
ATOM   3465 N  NZ    . LYS A 1 447 ? -11.059 -32.458 31.871  1.00 93.62  ? 1664 LYS A NZ    1 
ATOM   3466 N  N     . ALA A 1 448 ? -9.698  -38.914 34.356  1.00 116.48 ? 1665 ALA A N     1 
ATOM   3467 C  CA    . ALA A 1 448 ? -8.395  -39.135 34.967  1.00 107.43 ? 1665 ALA A CA    1 
ATOM   3468 C  C     . ALA A 1 448 ? -7.856  -40.507 34.610  1.00 110.90 ? 1665 ALA A C     1 
ATOM   3469 O  O     . ALA A 1 448 ? -6.674  -40.654 34.271  1.00 115.25 ? 1665 ALA A O     1 
ATOM   3470 C  CB    . ALA A 1 448 ? -8.494  -38.987 36.487  1.00 97.97  ? 1665 ALA A CB    1 
ATOM   3471 N  N     . GLU A 1 449 ? -8.717  -41.519 34.642  1.00 107.06 ? 1666 GLU A N     1 
ATOM   3472 C  CA    . GLU A 1 449 ? -8.262  -42.894 34.531  1.00 102.60 ? 1666 GLU A CA    1 
ATOM   3473 C  C     . GLU A 1 449 ? -8.160  -43.385 33.086  1.00 98.38  ? 1666 GLU A C     1 
ATOM   3474 O  O     . GLU A 1 449 ? -7.907  -44.572 32.876  1.00 96.55  ? 1666 GLU A O     1 
ATOM   3475 C  CB    . GLU A 1 449 ? -9.174  -43.792 35.376  1.00 94.74  ? 1666 GLU A CB    1 
ATOM   3476 C  CG    . GLU A 1 449 ? -9.110  -43.394 36.845  1.00 90.84  ? 1666 GLU A CG    1 
ATOM   3477 C  CD    . GLU A 1 449 ? -9.871  -44.316 37.759  1.00 97.47  ? 1666 GLU A CD    1 
ATOM   3478 O  OE1   . GLU A 1 449 ? -10.002 -45.497 37.403  1.00 101.73 ? 1666 GLU A OE1   1 
ATOM   3479 O  OE2   . GLU A 1 449 ? -10.285 -43.885 38.859  1.00 101.66 ? 1666 GLU A OE2   1 
ATOM   3480 N  N     . SER A 1 450 ? -8.305  -42.495 32.093  1.00 92.37  ? 1667 SER A N     1 
ATOM   3481 C  CA    . SER A 1 450 ? -7.990  -42.848 30.709  1.00 93.81  ? 1667 SER A CA    1 
ATOM   3482 C  C     . SER A 1 450 ? -6.681  -42.224 30.221  1.00 102.72 ? 1667 SER A C     1 
ATOM   3483 O  O     . SER A 1 450 ? -6.394  -42.246 29.017  1.00 65.32  ? 1667 SER A O     1 
ATOM   3484 C  CB    . SER A 1 450 ? -9.142  -42.484 29.772  1.00 97.13  ? 1667 SER A CB    1 
ATOM   3485 O  OG    . SER A 1 450 ? -9.796  -41.315 30.208  1.00 109.96 ? 1667 SER A OG    1 
ATOM   3486 N  N     . ALA A 1 451 ? -5.912  -41.628 31.136  1.00 106.24 ? 1668 ALA A N     1 
ATOM   3487 C  CA    . ALA A 1 451 ? -4.627  -40.995 30.830  1.00 109.42 ? 1668 ALA A CA    1 
ATOM   3488 C  C     . ALA A 1 451 ? -3.516  -42.042 30.702  1.00 110.91 ? 1668 ALA A C     1 
ATOM   3489 O  O     . ALA A 1 451 ? -2.492  -41.790 30.061  1.00 110.92 ? 1668 ALA A O     1 
ATOM   3490 C  CB    . ALA A 1 451 ? -4.281  -39.965 31.902  1.00 106.17 ? 1668 ALA A CB    1 
ATOM   3491 N  N     . GLY A 1 465 ? -6.491  -38.506 28.164  1.00 82.51  ? 1682 GLY A N     1 
ATOM   3492 C  CA    . GLY A 1 465 ? -7.711  -38.449 28.954  1.00 94.27  ? 1682 GLY A CA    1 
ATOM   3493 C  C     . GLY A 1 465 ? -8.973  -38.416 28.099  1.00 105.28 ? 1682 GLY A C     1 
ATOM   3494 O  O     . GLY A 1 465 ? -8.919  -38.031 26.931  1.00 116.08 ? 1682 GLY A O     1 
ATOM   3495 N  N     . ALA A 1 466 ? -10.113 -38.823 28.657  1.00 99.16  ? 1683 ALA A N     1 
ATOM   3496 C  CA    . ALA A 1 466 ? -11.351 -38.933 27.885  1.00 86.08  ? 1683 ALA A CA    1 
ATOM   3497 C  C     . ALA A 1 466 ? -12.455 -38.119 28.541  1.00 86.97  ? 1683 ALA A C     1 
ATOM   3498 O  O     . ALA A 1 466 ? -12.802 -38.364 29.700  1.00 85.25  ? 1683 ALA A O     1 
ATOM   3499 C  CB    . ALA A 1 466 ? -11.805 -40.385 27.754  1.00 78.72  ? 1683 ALA A CB    1 
ATOM   3500 N  N     . LYS A 1 467 ? -13.053 -37.210 27.781  1.00 87.43  ? 1684 LYS A N     1 
ATOM   3501 C  CA    . LYS A 1 467 ? -14.157 -36.390 28.252  1.00 80.72  ? 1684 LYS A CA    1 
ATOM   3502 C  C     . LYS A 1 467 ? -15.468 -36.870 27.650  1.00 84.07  ? 1684 LYS A C     1 
ATOM   3503 O  O     . LYS A 1 467 ? -15.487 -37.557 26.624  1.00 66.56  ? 1684 LYS A O     1 
ATOM   3504 C  CB    . LYS A 1 467 ? -13.931 -34.915 27.896  1.00 65.20  ? 1684 LYS A CB    1 
ATOM   3505 N  N     . SER A 1 468 ? -16.565 -36.502 28.288  1.00 102.52 ? 1685 SER A N     1 
ATOM   3506 C  CA    . SER A 1 468 ? -17.848 -36.557 27.624  1.00 103.92 ? 1685 SER A CA    1 
ATOM   3507 C  C     . SER A 1 468 ? -17.842 -35.696 26.372  1.00 97.53  ? 1685 SER A C     1 
ATOM   3508 O  O     . SER A 1 468 ? -17.186 -34.649 26.291  1.00 102.43 ? 1685 SER A O     1 
ATOM   3509 C  CB    . SER A 1 468 ? -18.973 -36.096 28.560  1.00 107.09 ? 1685 SER A CB    1 
ATOM   3510 O  OG    . SER A 1 468 ? -20.182 -36.123 27.863  1.00 121.60 ? 1685 SER A OG    1 
ATOM   3511 N  N     . LEU A 1 469 ? -18.555 -36.172 25.367  1.00 77.81  ? 1686 LEU A N     1 
ATOM   3512 C  CA    . LEU A 1 469 ? -18.854 -35.407 24.176  1.00 66.05  ? 1686 LEU A CA    1 
ATOM   3513 C  C     . LEU A 1 469 ? -20.301 -34.922 24.181  1.00 66.63  ? 1686 LEU A C     1 
ATOM   3514 O  O     . LEU A 1 469 ? -20.562 -33.721 24.316  1.00 66.96  ? 1686 LEU A O     1 
ATOM   3515 C  CB    . LEU A 1 469 ? -18.602 -36.238 22.902  1.00 63.33  ? 1686 LEU A CB    1 
ATOM   3516 C  CG    . LEU A 1 469 ? -17.143 -36.427 22.501  1.00 67.96  ? 1686 LEU A CG    1 
ATOM   3517 C  CD1   . LEU A 1 469 ? -16.366 -37.185 23.513  1.00 68.44  ? 1686 LEU A CD1   1 
ATOM   3518 C  CD2   . LEU A 1 469 ? -17.088 -37.121 21.183  1.00 68.05  ? 1686 LEU A CD2   1 
ATOM   3519 N  N     . CYS A 1 470 ? -21.249 -35.846 24.108  1.00 68.38  ? 1687 CYS A N     1 
ATOM   3520 C  CA    . CYS A 1 470 ? -22.652 -35.541 24.322  1.00 69.60  ? 1687 CYS A CA    1 
ATOM   3521 C  C     . CYS A 1 470 ? -23.375 -36.801 24.744  1.00 78.89  ? 1687 CYS A C     1 
ATOM   3522 O  O     . CYS A 1 470 ? -22.905 -37.925 24.535  1.00 80.97  ? 1687 CYS A O     1 
ATOM   3523 C  CB    . CYS A 1 470 ? -23.321 -34.989 23.067  1.00 66.50  ? 1687 CYS A CB    1 
ATOM   3524 S  SG    . CYS A 1 470 ? -23.185 -36.103 21.653  1.00 70.35  ? 1687 CYS A SG    1 
ATOM   3525 N  N     . ILE A 1 471 ? -24.551 -36.590 25.313  1.00 82.30  ? 1688 ILE A N     1 
ATOM   3526 C  CA    . ILE A 1 471 ? -25.527 -37.650 25.506  1.00 71.43  ? 1688 ILE A CA    1 
ATOM   3527 C  C     . ILE A 1 471 ? -26.340 -37.678 24.222  1.00 75.14  ? 1688 ILE A C     1 
ATOM   3528 O  O     . ILE A 1 471 ? -27.221 -36.830 24.036  1.00 83.48  ? 1688 ILE A O     1 
ATOM   3529 C  CB    . ILE A 1 471 ? -26.399 -37.374 26.733  1.00 69.27  ? 1688 ILE A CB    1 
ATOM   3530 C  CG1   . ILE A 1 471 ? -25.500 -36.953 27.903  1.00 66.61  ? 1688 ILE A CG1   1 
ATOM   3531 C  CG2   . ILE A 1 471 ? -27.277 -38.573 27.022  1.00 58.43  ? 1688 ILE A CG2   1 
ATOM   3532 C  CD1   . ILE A 1 471 ? -26.199 -36.145 28.940  1.00 56.22  ? 1688 ILE A CD1   1 
ATOM   3533 N  N     . PRO A 1 472 ? -26.062 -38.600 23.304  1.00 79.67  ? 1689 PRO A N     1 
ATOM   3534 C  CA    . PRO A 1 472 ? -26.639 -38.492 21.960  1.00 70.90  ? 1689 PRO A CA    1 
ATOM   3535 C  C     . PRO A 1 472 ? -28.154 -38.576 21.999  1.00 76.41  ? 1689 PRO A C     1 
ATOM   3536 O  O     . PRO A 1 472 ? -28.742 -39.289 22.814  1.00 74.76  ? 1689 PRO A O     1 
ATOM   3537 C  CB    . PRO A 1 472 ? -26.032 -39.679 21.206  1.00 62.10  ? 1689 PRO A CB    1 
ATOM   3538 C  CG    . PRO A 1 472 ? -24.904 -40.172 22.077  1.00 72.74  ? 1689 PRO A CG    1 
ATOM   3539 C  CD    . PRO A 1 472 ? -25.264 -39.827 23.471  1.00 82.41  ? 1689 PRO A CD    1 
ATOM   3540 N  N     . PHE A 1 473 ? -28.776 -37.797 21.120  1.00 79.34  ? 1690 PHE A N     1 
ATOM   3541 C  CA    . PHE A 1 473 ? -30.217 -37.854 20.955  1.00 74.08  ? 1690 PHE A CA    1 
ATOM   3542 C  C     . PHE A 1 473 ? -30.654 -39.213 20.433  1.00 77.06  ? 1690 PHE A C     1 
ATOM   3543 O  O     . PHE A 1 473 ? -31.577 -39.832 20.975  1.00 75.04  ? 1690 PHE A O     1 
ATOM   3544 C  CB    . PHE A 1 473 ? -30.653 -36.755 19.996  1.00 73.53  ? 1690 PHE A CB    1 
ATOM   3545 C  CG    . PHE A 1 473 ? -30.646 -35.413 20.598  1.00 72.02  ? 1690 PHE A CG    1 
ATOM   3546 C  CD1   . PHE A 1 473 ? -30.499 -35.262 21.962  1.00 77.55  ? 1690 PHE A CD1   1 
ATOM   3547 C  CD2   . PHE A 1 473 ? -30.803 -34.291 19.807  1.00 71.09  ? 1690 PHE A CD2   1 
ATOM   3548 C  CE1   . PHE A 1 473 ? -30.510 -33.999 22.530  1.00 80.47  ? 1690 PHE A CE1   1 
ATOM   3549 C  CE2   . PHE A 1 473 ? -30.806 -33.032 20.369  1.00 68.61  ? 1690 PHE A CE2   1 
ATOM   3550 C  CZ    . PHE A 1 473 ? -30.657 -32.885 21.729  1.00 66.78  ? 1690 PHE A CZ    1 
ATOM   3551 N  N     . GLU A 1 474 ? -30.016 -39.688 19.367  1.00 75.81  ? 1691 GLU A N     1 
ATOM   3552 C  CA    . GLU A 1 474 ? -30.259 -41.052 18.916  1.00 77.92  ? 1691 GLU A CA    1 
ATOM   3553 C  C     . GLU A 1 474 ? -29.464 -41.969 19.840  1.00 81.50  ? 1691 GLU A C     1 
ATOM   3554 O  O     . GLU A 1 474 ? -28.240 -42.076 19.734  1.00 84.32  ? 1691 GLU A O     1 
ATOM   3555 C  CB    . GLU A 1 474 ? -29.869 -41.221 17.451  1.00 74.90  ? 1691 GLU A CB    1 
ATOM   3556 N  N     . GLN A 1 475 ? -30.146 -42.598 20.771  1.00 80.94  ? 1692 GLN A N     1 
ATOM   3557 C  CA    . GLN A 1 475 ? -29.454 -43.491 21.678  1.00 79.17  ? 1692 GLN A CA    1 
ATOM   3558 C  C     . GLN A 1 475 ? -29.257 -44.832 20.981  1.00 87.98  ? 1692 GLN A C     1 
ATOM   3559 O  O     . GLN A 1 475 ? -30.089 -45.231 20.164  1.00 86.63  ? 1692 GLN A O     1 
ATOM   3560 C  CB    . GLN A 1 475 ? -30.248 -43.678 22.957  1.00 71.66  ? 1692 GLN A CB    1 
ATOM   3561 C  CG    . GLN A 1 475 ? -30.138 -42.503 23.909  1.00 74.66  ? 1692 GLN A CG    1 
ATOM   3562 C  CD    . GLN A 1 475 ? -29.048 -42.682 24.939  1.00 70.95  ? 1692 GLN A CD    1 
ATOM   3563 O  OE1   . GLN A 1 475 ? -29.004 -43.686 25.644  1.00 83.57  ? 1692 GLN A OE1   1 
ATOM   3564 N  NE2   . GLN A 1 475 ? -28.158 -41.713 25.027  1.00 75.09  ? 1692 GLN A NE2   1 
ATOM   3565 N  N     . PRO A 1 476 ? -28.152 -45.539 21.258  1.00 92.47  ? 1693 PRO A N     1 
ATOM   3566 C  CA    . PRO A 1 476 ? -27.946 -46.829 20.573  1.00 93.89  ? 1693 PRO A CA    1 
ATOM   3567 C  C     . PRO A 1 476 ? -28.875 -47.924 21.075  1.00 105.08 ? 1693 PRO A C     1 
ATOM   3568 O  O     . PRO A 1 476 ? -29.224 -48.831 20.308  1.00 111.24 ? 1693 PRO A O     1 
ATOM   3569 C  CB    . PRO A 1 476 ? -26.470 -47.145 20.852  1.00 85.57  ? 1693 PRO A CB    1 
ATOM   3570 C  CG    . PRO A 1 476 ? -26.119 -46.358 22.101  1.00 79.42  ? 1693 PRO A CG    1 
ATOM   3571 C  CD    . PRO A 1 476 ? -27.051 -45.190 22.183  1.00 83.94  ? 1693 PRO A CD    1 
ATOM   3572 N  N     . ALA A 1 477 ? -29.309 -47.843 22.328  1.00 103.00 ? 1694 ALA A N     1 
ATOM   3573 C  CA    . ALA A 1 477 ? -30.226 -48.795 22.938  1.00 102.98 ? 1694 ALA A CA    1 
ATOM   3574 C  C     . ALA A 1 477 ? -30.764 -48.137 24.198  1.00 108.94 ? 1694 ALA A C     1 
ATOM   3575 O  O     . ALA A 1 477 ? -30.195 -47.160 24.699  1.00 106.74 ? 1694 ALA A O     1 
ATOM   3576 C  CB    . ALA A 1 477 ? -29.557 -50.139 23.260  1.00 90.62  ? 1694 ALA A CB    1 
ATOM   3577 N  N     . LYS A 1 478 ? -31.865 -48.675 24.707  1.00 108.92 ? 1695 LYS A N     1 
ATOM   3578 C  CA    . LYS A 1 478 ? -32.460 -48.135 25.916  1.00 100.98 ? 1695 LYS A CA    1 
ATOM   3579 C  C     . LYS A 1 478 ? -31.879 -48.926 27.078  1.00 98.60  ? 1695 LYS A C     1 
ATOM   3580 O  O     . LYS A 1 478 ? -31.785 -50.156 27.011  1.00 95.20  ? 1695 LYS A O     1 
ATOM   3581 C  CB    . LYS A 1 478 ? -33.989 -48.232 25.883  1.00 93.41  ? 1695 LYS A CB    1 
ATOM   3582 N  N     . ILE A 1 479 ? -31.440 -48.216 28.115  1.00 100.83 ? 1696 ILE A N     1 
ATOM   3583 C  CA    . ILE A 1 479 ? -30.724 -48.868 29.202  1.00 102.70 ? 1696 ILE A CA    1 
ATOM   3584 C  C     . ILE A 1 479 ? -31.714 -49.734 29.974  1.00 112.59 ? 1696 ILE A C     1 
ATOM   3585 O  O     . ILE A 1 479 ? -32.721 -49.236 30.488  1.00 108.86 ? 1696 ILE A O     1 
ATOM   3586 C  CB    . ILE A 1 479 ? -30.040 -47.833 30.105  1.00 89.45  ? 1696 ILE A CB    1 
ATOM   3587 N  N     . ASP A 1 480 ? -31.412 -51.040 30.087  1.00 118.23 ? 1697 ASP A N     1 
ATOM   3588 C  CA    . ASP A 1 480 ? -32.299 -51.979 30.758  1.00 117.79 ? 1697 ASP A CA    1 
ATOM   3589 C  C     . ASP A 1 480 ? -31.824 -52.106 32.194  1.00 115.87 ? 1697 ASP A C     1 
ATOM   3590 O  O     . ASP A 1 480 ? -30.846 -52.817 32.461  1.00 128.13 ? 1697 ASP A O     1 
ATOM   3591 C  CB    . ASP A 1 480 ? -32.307 -53.346 30.067  1.00 117.75 ? 1697 ASP A CB    1 
ATOM   3592 N  N     . PRO A 1 481 ? -32.483 -51.446 33.147  1.00 105.51 ? 1698 PRO A N     1 
ATOM   3593 C  CA    . PRO A 1 481 ? -31.928 -51.317 34.504  1.00 99.07  ? 1698 PRO A CA    1 
ATOM   3594 C  C     . PRO A 1 481 ? -31.760 -52.619 35.251  1.00 112.47 ? 1698 PRO A C     1 
ATOM   3595 O  O     . PRO A 1 481 ? -31.077 -52.618 36.286  1.00 124.30 ? 1698 PRO A O     1 
ATOM   3596 C  CB    . PRO A 1 481 ? -32.950 -50.419 35.216  1.00 94.42  ? 1698 PRO A CB    1 
ATOM   3597 C  CG    . PRO A 1 481 ? -33.768 -49.801 34.128  1.00 95.08  ? 1698 PRO A CG    1 
ATOM   3598 C  CD    . PRO A 1 481 ? -33.791 -50.792 33.016  1.00 104.42 ? 1698 PRO A CD    1 
ATOM   3599 N  N     . LYS A 1 482 ? -32.363 -53.723 34.800  1.00 103.73 ? 1699 LYS A N     1 
ATOM   3600 C  CA    . LYS A 1 482 ? -32.120 -54.986 35.478  1.00 111.43 ? 1699 LYS A CA    1 
ATOM   3601 C  C     . LYS A 1 482 ? -30.644 -55.377 35.415  1.00 121.71 ? 1699 LYS A C     1 
ATOM   3602 O  O     . LYS A 1 482 ? -30.185 -56.187 36.230  1.00 126.84 ? 1699 LYS A O     1 
ATOM   3603 C  CB    . LYS A 1 482 ? -33.016 -56.079 34.882  1.00 109.44 ? 1699 LYS A CB    1 
ATOM   3604 N  N     . VAL A 1 483 ? -29.873 -54.768 34.508  1.00 118.26 ? 1700 VAL A N     1 
ATOM   3605 C  CA    . VAL A 1 483 ? -28.488 -55.164 34.246  1.00 113.26 ? 1700 VAL A CA    1 
ATOM   3606 C  C     . VAL A 1 483 ? -27.542 -53.959 34.214  1.00 109.36 ? 1700 VAL A C     1 
ATOM   3607 O  O     . VAL A 1 483 ? -26.561 -53.923 34.966  1.00 101.52 ? 1700 VAL A O     1 
ATOM   3608 C  CB    . VAL A 1 483 ? -28.418 -56.006 32.953  1.00 107.98 ? 1700 VAL A CB    1 
ATOM   3609 C  CG1   . VAL A 1 483 ? -29.113 -55.301 31.771  1.00 109.04 ? 1700 VAL A CG1   1 
ATOM   3610 C  CG2   . VAL A 1 483 ? -26.998 -56.332 32.594  1.00 104.56 ? 1700 VAL A CG2   1 
ATOM   3611 N  N     . ASP A 1 484 ? -27.866 -52.947 33.408  1.00 114.67 ? 1701 ASP A N     1 
ATOM   3612 C  CA    . ASP A 1 484 ? -26.906 -51.893 33.085  1.00 109.59 ? 1701 ASP A CA    1 
ATOM   3613 C  C     . ASP A 1 484 ? -26.450 -51.079 34.296  1.00 117.45 ? 1701 ASP A C     1 
ATOM   3614 O  O     . ASP A 1 484 ? -27.264 -50.626 35.104  1.00 130.84 ? 1701 ASP A O     1 
ATOM   3615 C  CB    . ASP A 1 484 ? -27.499 -50.965 32.037  1.00 93.32  ? 1701 ASP A CB    1 
ATOM   3616 C  CG    . ASP A 1 484 ? -27.702 -51.655 30.708  1.00 99.07  ? 1701 ASP A CG    1 
ATOM   3617 O  OD1   . ASP A 1 484 ? -27.128 -52.762 30.533  1.00 108.65 ? 1701 ASP A OD1   1 
ATOM   3618 O  OD2   . ASP A 1 484 ? -28.423 -51.101 29.852  1.00 91.06  ? 1701 ASP A OD2   1 
ATOM   3619 N  N     . LYS A 1 485 ? -25.132 -50.923 34.428  1.00 108.71 ? 1702 LYS A N     1 
ATOM   3620 C  CA    . LYS A 1 485 ? -24.527 -50.033 35.412  1.00 100.75 ? 1702 LYS A CA    1 
ATOM   3621 C  C     . LYS A 1 485 ? -23.561 -49.123 34.664  1.00 95.45  ? 1702 LYS A C     1 
ATOM   3622 O  O     . LYS A 1 485 ? -23.150 -49.428 33.543  1.00 91.46  ? 1702 LYS A O     1 
ATOM   3623 C  CB    . LYS A 1 485 ? -23.830 -50.805 36.543  1.00 94.46  ? 1702 LYS A CB    1 
ATOM   3624 N  N     . CYS A 1 486 ? -23.271 -47.961 35.244  1.00 98.62  ? 1703 CYS A N     1 
ATOM   3625 C  CA    . CYS A 1 486 ? -22.355 -47.014 34.612  1.00 95.00  ? 1703 CYS A CA    1 
ATOM   3626 C  C     . CYS A 1 486 ? -21.001 -47.664 34.361  1.00 93.51  ? 1703 CYS A C     1 
ATOM   3627 O  O     . CYS A 1 486 ? -20.520 -48.464 35.170  1.00 100.77 ? 1703 CYS A O     1 
ATOM   3628 C  CB    . CYS A 1 486 ? -22.179 -45.755 35.471  1.00 89.47  ? 1703 CYS A CB    1 
ATOM   3629 S  SG    . CYS A 1 486 ? -20.732 -44.697 35.053  1.00 85.82  ? 1703 CYS A SG    1 
ATOM   3630 N  N     . VAL A 1 487 ? -20.393 -47.325 33.219  1.00 84.38  ? 1704 VAL A N     1 
ATOM   3631 C  CA    . VAL A 1 487 ? -19.201 -48.023 32.756  1.00 87.29  ? 1704 VAL A CA    1 
ATOM   3632 C  C     . VAL A 1 487 ? -18.012 -47.834 33.690  1.00 87.84  ? 1704 VAL A C     1 
ATOM   3633 O  O     . VAL A 1 487 ? -17.079 -48.641 33.670  1.00 80.79  ? 1704 VAL A O     1 
ATOM   3634 C  CB    . VAL A 1 487 ? -18.846 -47.557 31.327  1.00 83.56  ? 1704 VAL A CB    1 
ATOM   3635 C  CG1   . VAL A 1 487 ? -18.324 -46.117 31.335  1.00 67.76  ? 1704 VAL A CG1   1 
ATOM   3636 C  CG2   . VAL A 1 487 ? -17.853 -48.533 30.670  1.00 81.53  ? 1704 VAL A CG2   1 
ATOM   3637 N  N     . HIS A 1 488 ? -18.016 -46.812 34.522  1.00 93.10  ? 1705 HIS A N     1 
ATOM   3638 C  CA    . HIS A 1 488 ? -16.885 -46.698 35.428  1.00 100.62 ? 1705 HIS A CA    1 
ATOM   3639 C  C     . HIS A 1 488 ? -17.091 -47.605 36.632  1.00 102.80 ? 1705 HIS A C     1 
ATOM   3640 O  O     . HIS A 1 488 ? -18.143 -47.539 37.278  1.00 99.63  ? 1705 HIS A O     1 
ATOM   3641 C  CB    . HIS A 1 488 ? -16.662 -45.280 35.907  1.00 105.40 ? 1705 HIS A CB    1 
ATOM   3642 C  CG    . HIS A 1 488 ? -15.443 -45.143 36.760  1.00 114.57 ? 1705 HIS A CG    1 
ATOM   3643 N  ND1   . HIS A 1 488 ? -14.251 -45.760 36.446  1.00 114.63 ? 1705 HIS A ND1   1 
ATOM   3644 C  CD2   . HIS A 1 488 ? -15.234 -44.492 37.928  1.00 117.43 ? 1705 HIS A CD2   1 
ATOM   3645 C  CE1   . HIS A 1 488 ? -13.357 -45.484 37.376  1.00 115.61 ? 1705 HIS A CE1   1 
ATOM   3646 N  NE2   . HIS A 1 488 ? -13.926 -44.715 38.287  1.00 117.12 ? 1705 HIS A NE2   1 
ATOM   3647 N  N     . PRO A 1 489 ? -16.114 -48.457 36.961  1.00 100.57 ? 1706 PRO A N     1 
ATOM   3648 C  CA    . PRO A 1 489 ? -16.294 -49.394 38.087  1.00 100.86 ? 1706 PRO A CA    1 
ATOM   3649 C  C     . PRO A 1 489 ? -16.343 -48.752 39.475  1.00 100.20 ? 1706 PRO A C     1 
ATOM   3650 O  O     . PRO A 1 489 ? -16.839 -49.403 40.407  1.00 101.54 ? 1706 PRO A O     1 
ATOM   3651 C  CB    . PRO A 1 489 ? -15.080 -50.324 37.963  1.00 97.16  ? 1706 PRO A CB    1 
ATOM   3652 C  CG    . PRO A 1 489 ? -14.681 -50.250 36.507  1.00 95.67  ? 1706 PRO A CG    1 
ATOM   3653 C  CD    . PRO A 1 489 ? -14.961 -48.820 36.111  1.00 95.63  ? 1706 PRO A CD    1 
ATOM   3654 N  N     . ALA A 1 490 ? -15.873 -47.516 39.669  1.00 102.89 ? 1707 ALA A N     1 
ATOM   3655 C  CA    . ALA A 1 490 ? -15.870 -46.973 41.032  1.00 112.45 ? 1707 ALA A CA    1 
ATOM   3656 C  C     . ALA A 1 490 ? -17.230 -46.431 41.457  1.00 120.22 ? 1707 ALA A C     1 
ATOM   3657 O  O     . ALA A 1 490 ? -17.608 -46.535 42.629  1.00 117.35 ? 1707 ALA A O     1 
ATOM   3658 C  CB    . ALA A 1 490 ? -14.823 -45.866 41.160  1.00 111.24 ? 1707 ALA A CB    1 
ATOM   3659 N  N     . CYS A 1 491 ? -17.995 -45.896 40.517  1.00 125.00 ? 1708 CYS A N     1 
ATOM   3660 C  CA    . CYS A 1 491 ? -19.361 -45.529 40.841  1.00 127.37 ? 1708 CYS A CA    1 
ATOM   3661 C  C     . CYS A 1 491 ? -20.230 -46.764 40.610  1.00 131.32 ? 1708 CYS A C     1 
ATOM   3662 O  O     . CYS A 1 491 ? -20.000 -47.541 39.680  1.00 120.74 ? 1708 CYS A O     1 
ATOM   3663 C  CB    . CYS A 1 491 ? -19.848 -44.336 39.999  1.00 119.13 ? 1708 CYS A CB    1 
ATOM   3664 S  SG    . CYS A 1 491 ? -20.377 -44.826 38.371  1.00 117.13 ? 1708 CYS A SG    1 
ATOM   3665 N  N     . GLY A 1 492 ? -21.155 -47.003 41.523  1.00 134.37 ? 1709 GLY A N     1 
ATOM   3666 C  CA    . GLY A 1 492 ? -22.052 -48.124 41.395  1.00 134.15 ? 1709 GLY A CA    1 
ATOM   3667 C  C     . GLY A 1 492 ? -23.423 -47.672 40.974  1.00 134.90 ? 1709 GLY A C     1 
ATOM   3668 O  O     . GLY A 1 492 ? -24.384 -48.441 41.107  1.00 137.65 ? 1709 GLY A O     1 
ATOM   3669 N  N     . ARG A 1 493 ? -23.537 -46.433 40.495  1.00 124.31 ? 1710 ARG A N     1 
ATOM   3670 C  CA    . ARG A 1 493 ? -24.792 -45.896 40.006  1.00 119.19 ? 1710 ARG A CA    1 
ATOM   3671 C  C     . ARG A 1 493 ? -25.234 -46.664 38.764  1.00 119.37 ? 1710 ARG A C     1 
ATOM   3672 O  O     . ARG A 1 493 ? -24.415 -47.015 37.906  1.00 120.57 ? 1710 ARG A O     1 
ATOM   3673 C  CB    . ARG A 1 493 ? -24.625 -44.412 39.692  1.00 109.56 ? 1710 ARG A CB    1 
ATOM   3674 N  N     . VAL A 1 494 ? -26.536 -46.969 38.701  1.00 115.19 ? 1711 VAL A N     1 
ATOM   3675 C  CA    . VAL A 1 494 ? -27.141 -47.484 37.476  1.00 103.55 ? 1711 VAL A CA    1 
ATOM   3676 C  C     . VAL A 1 494 ? -26.996 -46.448 36.359  1.00 94.43  ? 1711 VAL A C     1 
ATOM   3677 O  O     . VAL A 1 494 ? -26.986 -45.232 36.600  1.00 89.09  ? 1711 VAL A O     1 
ATOM   3678 C  CB    . VAL A 1 494 ? -28.617 -47.853 37.701  1.00 76.79  ? 1711 VAL A CB    1 
ATOM   3679 N  N     . ALA A 1 495 ? -26.862 -46.935 35.128  1.00 93.33  ? 1712 ALA A N     1 
ATOM   3680 C  CA    . ALA A 1 495 ? -26.645 -46.053 33.986  1.00 91.01  ? 1712 ALA A CA    1 
ATOM   3681 C  C     . ALA A 1 495 ? -27.873 -45.200 33.684  1.00 100.47 ? 1712 ALA A C     1 
ATOM   3682 O  O     . ALA A 1 495 ? -28.988 -45.717 33.546  1.00 98.93  ? 1712 ALA A O     1 
ATOM   3683 C  CB    . ALA A 1 495 ? -26.291 -46.873 32.751  1.00 75.15  ? 1712 ALA A CB    1 
ATOM   3684 N  N     . LYS A 1 496 ? -27.660 -43.890 33.535  1.00 101.45 ? 1713 LYS A N     1 
ATOM   3685 C  CA    . LYS A 1 496 ? -28.754 -43.018 33.132  1.00 93.25  ? 1713 LYS A CA    1 
ATOM   3686 C  C     . LYS A 1 496 ? -28.991 -43.069 31.632  1.00 88.60  ? 1713 LYS A C     1 
ATOM   3687 O  O     . LYS A 1 496 ? -30.124 -42.884 31.185  1.00 93.03  ? 1713 LYS A O     1 
ATOM   3688 C  CB    . LYS A 1 496 ? -28.484 -41.583 33.580  1.00 93.77  ? 1713 LYS A CB    1 
ATOM   3689 N  N     . PHE A 1 497 ? -27.950 -43.286 30.845  1.00 82.90  ? 1714 PHE A N     1 
ATOM   3690 C  CA    . PHE A 1 497 ? -28.068 -43.262 29.392  1.00 80.26  ? 1714 PHE A CA    1 
ATOM   3691 C  C     . PHE A 1 497 ? -26.741 -43.718 28.803  1.00 72.48  ? 1714 PHE A C     1 
ATOM   3692 O  O     . PHE A 1 497 ? -25.800 -44.058 29.525  1.00 80.67  ? 1714 PHE A O     1 
ATOM   3693 C  CB    . PHE A 1 497 ? -28.435 -41.870 28.879  1.00 79.18  ? 1714 PHE A CB    1 
ATOM   3694 C  CG    . PHE A 1 497 ? -27.913 -40.763 29.739  1.00 87.25  ? 1714 PHE A CG    1 
ATOM   3695 C  CD1   . PHE A 1 497 ? -26.548 -40.567 29.887  1.00 92.98  ? 1714 PHE A CD1   1 
ATOM   3696 C  CD2   . PHE A 1 497 ? -28.783 -39.927 30.422  1.00 85.42  ? 1714 PHE A CD2   1 
ATOM   3697 C  CE1   . PHE A 1 497 ? -26.061 -39.542 30.693  1.00 93.26  ? 1714 PHE A CE1   1 
ATOM   3698 C  CE2   . PHE A 1 497 ? -28.302 -38.902 31.225  1.00 81.85  ? 1714 PHE A CE2   1 
ATOM   3699 C  CZ    . PHE A 1 497 ? -26.943 -38.709 31.357  1.00 88.64  ? 1714 PHE A CZ    1 
ATOM   3700 N  N     . TYR A 1 498 ? -26.701 -43.781 27.480  1.00 65.50  ? 1715 TYR A N     1 
ATOM   3701 C  CA    . TYR A 1 498 ? -25.441 -43.879 26.761  1.00 76.52  ? 1715 TYR A CA    1 
ATOM   3702 C  C     . TYR A 1 498 ? -24.881 -42.472 26.562  1.00 81.96  ? 1715 TYR A C     1 
ATOM   3703 O  O     . TYR A 1 498 ? -25.614 -41.551 26.179  1.00 82.53  ? 1715 TYR A O     1 
ATOM   3704 C  CB    . TYR A 1 498 ? -25.642 -44.590 25.421  1.00 74.82  ? 1715 TYR A CB    1 
ATOM   3705 C  CG    . TYR A 1 498 ? -25.713 -46.078 25.609  1.00 84.96  ? 1715 TYR A CG    1 
ATOM   3706 C  CD1   . TYR A 1 498 ? -24.557 -46.820 25.861  1.00 83.62  ? 1715 TYR A CD1   1 
ATOM   3707 C  CD2   . TYR A 1 498 ? -26.931 -46.739 25.587  1.00 91.41  ? 1715 TYR A CD2   1 
ATOM   3708 C  CE1   . TYR A 1 498 ? -24.613 -48.183 26.058  1.00 77.27  ? 1715 TYR A CE1   1 
ATOM   3709 C  CE2   . TYR A 1 498 ? -27.002 -48.108 25.785  1.00 89.64  ? 1715 TYR A CE2   1 
ATOM   3710 C  CZ    . TYR A 1 498 ? -25.842 -48.819 26.017  1.00 83.03  ? 1715 TYR A CZ    1 
ATOM   3711 O  OH    . TYR A 1 498 ? -25.931 -50.167 26.212  1.00 88.40  ? 1715 TYR A OH    1 
ATOM   3712 N  N     . THR A 1 499 ? -23.590 -42.304 26.842  1.00 78.16  ? 1716 THR A N     1 
ATOM   3713 C  CA    . THR A 1 499 ? -22.872 -41.066 26.580  1.00 74.14  ? 1716 THR A CA    1 
ATOM   3714 C  C     . THR A 1 499 ? -21.707 -41.388 25.662  1.00 77.64  ? 1716 THR A C     1 
ATOM   3715 O  O     . THR A 1 499 ? -21.260 -42.542 25.578  1.00 78.27  ? 1716 THR A O     1 
ATOM   3716 C  CB    . THR A 1 499 ? -22.337 -40.435 27.883  1.00 74.57  ? 1716 THR A CB    1 
ATOM   3717 O  OG1   . THR A 1 499 ? -23.401 -40.273 28.823  1.00 84.07  ? 1716 THR A OG1   1 
ATOM   3718 C  CG2   . THR A 1 499 ? -21.712 -39.080 27.641  1.00 74.12  ? 1716 THR A CG2   1 
ATOM   3719 N  N     . LEU A 1 500 ? -21.216 -40.361 24.971  1.00 72.00  ? 1717 LEU A N     1 
ATOM   3720 C  CA    . LEU A 1 500 ? -20.096 -40.508 24.056  1.00 77.06  ? 1717 LEU A CA    1 
ATOM   3721 C  C     . LEU A 1 500 ? -18.858 -39.897 24.687  1.00 82.20  ? 1717 LEU A C     1 
ATOM   3722 O  O     . LEU A 1 500 ? -18.863 -38.712 25.042  1.00 79.68  ? 1717 LEU A O     1 
ATOM   3723 C  CB    . LEU A 1 500 ? -20.388 -39.832 22.720  1.00 76.30  ? 1717 LEU A CB    1 
ATOM   3724 C  CG    . LEU A 1 500 ? -19.753 -40.449 21.481  1.00 76.98  ? 1717 LEU A CG    1 
ATOM   3725 C  CD1   . LEU A 1 500 ? -20.293 -41.853 21.224  1.00 83.64  ? 1717 LEU A CD1   1 
ATOM   3726 C  CD2   . LEU A 1 500 ? -20.033 -39.556 20.293  1.00 76.26  ? 1717 LEU A CD2   1 
ATOM   3727 N  N     . PHE A 1 501 ? -17.795 -40.697 24.789  1.00 83.16  ? 1718 PHE A N     1 
ATOM   3728 C  CA    . PHE A 1 501 ? -16.530 -40.262 25.348  1.00 78.89  ? 1718 PHE A CA    1 
ATOM   3729 C  C     . PHE A 1 501 ? -15.453 -40.370 24.284  1.00 85.82  ? 1718 PHE A C     1 
ATOM   3730 O  O     . PHE A 1 501 ? -15.494 -41.250 23.410  1.00 84.24  ? 1718 PHE A O     1 
ATOM   3731 C  CB    . PHE A 1 501 ? -16.110 -41.092 26.552  1.00 68.04  ? 1718 PHE A CB    1 
ATOM   3732 C  CG    . PHE A 1 501 ? -17.115 -41.126 27.641  1.00 71.55  ? 1718 PHE A CG    1 
ATOM   3733 C  CD1   . PHE A 1 501 ? -18.218 -41.971 27.555  1.00 74.14  ? 1718 PHE A CD1   1 
ATOM   3734 C  CD2   . PHE A 1 501 ? -16.959 -40.331 28.766  1.00 69.33  ? 1718 PHE A CD2   1 
ATOM   3735 C  CE1   . PHE A 1 501 ? -19.158 -42.013 28.568  1.00 78.89  ? 1718 PHE A CE1   1 
ATOM   3736 C  CE2   . PHE A 1 501 ? -17.894 -40.366 29.788  1.00 71.98  ? 1718 PHE A CE2   1 
ATOM   3737 C  CZ    . PHE A 1 501 ? -18.994 -41.210 29.690  1.00 78.57  ? 1718 PHE A CZ    1 
ATOM   3738 N  N     . GLY A 1 502 ? -14.474 -39.479 24.394  1.00 81.82  ? 1719 GLY A N     1 
ATOM   3739 C  CA    . GLY A 1 502 ? -13.341 -39.489 23.487  1.00 80.50  ? 1719 GLY A CA    1 
ATOM   3740 C  C     . GLY A 1 502 ? -12.292 -38.529 23.992  1.00 77.61  ? 1719 GLY A C     1 
ATOM   3741 O  O     . GLY A 1 502 ? -12.515 -37.777 24.946  1.00 64.78  ? 1719 GLY A O     1 
ATOM   3742 N  N     . ARG A 1 503 ? -11.137 -38.565 23.332  1.00 90.05  ? 1720 ARG A N     1 
ATOM   3743 C  CA    . ARG A 1 503 ? -10.097 -37.585 23.591  1.00 89.65  ? 1720 ARG A CA    1 
ATOM   3744 C  C     . ARG A 1 503 ? -10.473 -36.280 22.886  1.00 99.08  ? 1720 ARG A C     1 
ATOM   3745 O  O     . ARG A 1 503 ? -10.911 -36.282 21.728  1.00 83.26  ? 1720 ARG A O     1 
ATOM   3746 C  CB    . ARG A 1 503 ? -8.742  -38.109 23.112  1.00 81.55  ? 1720 ARG A CB    1 
ATOM   3747 C  CG    . ARG A 1 503 ? -8.136  -39.223 23.986  1.00 82.25  ? 1720 ARG A CG    1 
ATOM   3748 C  CD    . ARG A 1 503 ? -6.730  -38.848 24.514  1.00 84.87  ? 1720 ARG A CD    1 
ATOM   3749 N  NE    . ARG A 1 503 ? -6.199  -39.850 25.431  1.00 87.08  ? 1720 ARG A NE    1 
ATOM   3750 C  CZ    . ARG A 1 503 ? -5.589  -40.961 25.032  1.00 95.67  ? 1720 ARG A CZ    1 
ATOM   3751 N  NH1   . ARG A 1 503 ? -5.429  -41.188 23.734  1.00 97.74  ? 1720 ARG A NH1   1 
ATOM   3752 N  NH2   . ARG A 1 503 ? -5.153  -41.847 25.925  1.00 99.53  ? 1720 ARG A NH2   1 
ATOM   3753 N  N     . SER A 1 504 ? -10.301 -35.161 23.591  1.00 110.91 ? 1721 SER A N     1 
ATOM   3754 C  CA    . SER A 1 504 ? -10.893 -33.889 23.202  1.00 115.71 ? 1721 SER A CA    1 
ATOM   3755 C  C     . SER A 1 504 ? -9.895  -32.944 22.539  1.00 119.84 ? 1721 SER A C     1 
ATOM   3756 O  O     . SER A 1 504 ? -8.676  -33.070 22.665  1.00 115.73 ? 1721 SER A O     1 
ATOM   3757 C  CB    . SER A 1 504 ? -11.496 -33.196 24.437  1.00 121.00 ? 1721 SER A CB    1 
ATOM   3758 O  OG    . SER A 1 504 ? -12.594 -32.358 24.114  1.00 121.07 ? 1721 SER A OG    1 
ATOM   3759 N  N     . TYR A 1 505 ? -10.443 -31.993 21.793  1.00 122.32 ? 1722 TYR A N     1 
ATOM   3760 C  CA    . TYR A 1 505 ? -9.658  -30.885 21.302  1.00 123.54 ? 1722 TYR A CA    1 
ATOM   3761 C  C     . TYR A 1 505 ? -9.731  -29.757 22.325  1.00 123.34 ? 1722 TYR A C     1 
ATOM   3762 O  O     . TYR A 1 505 ? -10.793 -29.545 22.921  1.00 117.60 ? 1722 TYR A O     1 
ATOM   3763 C  CB    . TYR A 1 505 ? -10.144 -30.418 19.942  1.00 122.89 ? 1722 TYR A CB    1 
ATOM   3764 C  CG    . TYR A 1 505 ? -9.016  -29.929 19.081  1.00 122.29 ? 1722 TYR A CG    1 
ATOM   3765 C  CD1   . TYR A 1 505 ? -8.286  -28.805 19.442  1.00 125.48 ? 1722 TYR A CD1   1 
ATOM   3766 C  CD2   . TYR A 1 505 ? -8.659  -30.605 17.924  1.00 120.89 ? 1722 TYR A CD2   1 
ATOM   3767 C  CE1   . TYR A 1 505 ? -7.245  -28.352 18.666  1.00 131.08 ? 1722 TYR A CE1   1 
ATOM   3768 C  CE2   . TYR A 1 505 ? -7.620  -30.163 17.135  1.00 125.87 ? 1722 TYR A CE2   1 
ATOM   3769 C  CZ    . TYR A 1 505 ? -6.912  -29.033 17.511  1.00 133.80 ? 1722 TYR A CZ    1 
ATOM   3770 O  OH    . TYR A 1 505 ? -5.866  -28.583 16.731  1.00 139.62 ? 1722 TYR A OH    1 
ATOM   3771 O  OXT   . TYR A 1 505 ? -8.747  -29.048 22.573  1.00 123.83 ? 1722 TYR A OXT   1 
ATOM   3772 N  N     . LEU B 1 6   ? -41.381 13.374  19.929  1.00 94.06  ? 1223 LEU B N     1 
ATOM   3773 C  CA    . LEU B 1 6   ? -40.181 14.215  19.847  1.00 92.53  ? 1223 LEU B CA    1 
ATOM   3774 C  C     . LEU B 1 6   ? -40.299 15.452  20.734  1.00 97.43  ? 1223 LEU B C     1 
ATOM   3775 O  O     . LEU B 1 6   ? -41.308 16.139  20.692  1.00 93.51  ? 1223 LEU B O     1 
ATOM   3776 C  CB    . LEU B 1 6   ? -39.923 14.630  18.404  1.00 89.74  ? 1223 LEU B CB    1 
ATOM   3777 C  CG    . LEU B 1 6   ? -38.462 14.469  17.993  1.00 94.13  ? 1223 LEU B CG    1 
ATOM   3778 C  CD1   . LEU B 1 6   ? -37.836 13.214  18.630  1.00 88.99  ? 1223 LEU B CD1   1 
ATOM   3779 C  CD2   . LEU B 1 6   ? -38.345 14.391  16.495  1.00 93.72  ? 1223 LEU B CD2   1 
ATOM   3780 N  N     . GLU B 1 7   ? -39.274 15.737  21.540  1.00 105.51 ? 1224 GLU B N     1 
ATOM   3781 C  CA    . GLU B 1 7   ? -39.340 16.858  22.477  1.00 105.62 ? 1224 GLU B CA    1 
ATOM   3782 C  C     . GLU B 1 7   ? -38.556 18.100  22.054  1.00 109.82 ? 1224 GLU B C     1 
ATOM   3783 O  O     . GLU B 1 7   ? -38.901 19.201  22.496  1.00 118.14 ? 1224 GLU B O     1 
ATOM   3784 C  CB    . GLU B 1 7   ? -38.856 16.416  23.867  1.00 105.25 ? 1224 GLU B CB    1 
ATOM   3785 N  N     . ALA B 1 8   ? -37.520 17.982  21.227  1.00 110.81 ? 1225 ALA B N     1 
ATOM   3786 C  CA    . ALA B 1 8   ? -36.759 19.147  20.762  1.00 103.89 ? 1225 ALA B CA    1 
ATOM   3787 C  C     . ALA B 1 8   ? -36.902 19.294  19.248  1.00 108.09 ? 1225 ALA B C     1 
ATOM   3788 O  O     . ALA B 1 8   ? -37.621 18.534  18.589  1.00 108.43 ? 1225 ALA B O     1 
ATOM   3789 C  CB    . ALA B 1 8   ? -35.285 19.061  21.170  1.00 96.94  ? 1225 ALA B CB    1 
ATOM   3790 N  N     . THR B 1 9   ? -36.224 20.304  18.696  1.00 106.01 ? 1226 THR B N     1 
ATOM   3791 C  CA    . THR B 1 9   ? -36.340 20.575  17.269  1.00 106.29 ? 1226 THR B CA    1 
ATOM   3792 C  C     . THR B 1 9   ? -35.006 20.948  16.628  1.00 102.23 ? 1226 THR B C     1 
ATOM   3793 O  O     . THR B 1 9   ? -34.113 21.535  17.252  1.00 100.16 ? 1226 THR B O     1 
ATOM   3794 C  CB    . THR B 1 9   ? -37.371 21.677  16.980  1.00 107.20 ? 1226 THR B CB    1 
ATOM   3795 O  OG1   . THR B 1 9   ? -37.559 21.786  15.564  1.00 113.23 ? 1226 THR B OG1   1 
ATOM   3796 C  CG2   . THR B 1 9   ? -36.906 22.998  17.519  1.00 102.73 ? 1226 THR B CG2   1 
ATOM   3797 N  N     . LYS B 1 10  ? -34.906 20.570  15.352  1.00 97.77  ? 1227 LYS B N     1 
ATOM   3798 C  CA    . LYS B 1 10  ? -33.702 20.755  14.552  1.00 95.73  ? 1227 LYS B CA    1 
ATOM   3799 C  C     . LYS B 1 10  ? -33.306 22.227  14.456  1.00 105.76 ? 1227 LYS B C     1 
ATOM   3800 O  O     . LYS B 1 10  ? -32.114 22.558  14.491  1.00 108.13 ? 1227 LYS B O     1 
ATOM   3801 C  CB    . LYS B 1 10  ? -33.959 20.165  13.162  1.00 84.59  ? 1227 LYS B CB    1 
ATOM   3802 C  CG    . LYS B 1 10  ? -32.767 19.597  12.393  1.00 73.24  ? 1227 LYS B CG    1 
ATOM   3803 C  CD    . LYS B 1 10  ? -33.228 19.297  10.955  1.00 71.74  ? 1227 LYS B CD    1 
ATOM   3804 C  CE    . LYS B 1 10  ? -32.102 18.904  10.021  1.00 65.11  ? 1227 LYS B CE    1 
ATOM   3805 N  NZ    . LYS B 1 10  ? -32.418 17.637  9.311   1.00 64.40  ? 1227 LYS B NZ    1 
ATOM   3806 N  N     . GLU B 1 11  ? -34.287 23.130  14.393  1.00 115.96 ? 1228 GLU B N     1 
ATOM   3807 C  CA    . GLU B 1 11  ? -33.982 24.520  14.066  1.00 114.48 ? 1228 GLU B CA    1 
ATOM   3808 C  C     . GLU B 1 11  ? -33.348 25.241  15.236  1.00 122.27 ? 1228 GLU B C     1 
ATOM   3809 O  O     . GLU B 1 11  ? -32.590 26.188  15.022  1.00 135.38 ? 1228 GLU B O     1 
ATOM   3810 C  CB    . GLU B 1 11  ? -35.253 25.275  13.673  1.00 113.69 ? 1228 GLU B CB    1 
ATOM   3811 C  CG    . GLU B 1 11  ? -35.746 24.987  12.292  1.00 127.97 ? 1228 GLU B CG    1 
ATOM   3812 C  CD    . GLU B 1 11  ? -36.784 23.886  12.297  1.00 140.49 ? 1228 GLU B CD    1 
ATOM   3813 O  OE1   . GLU B 1 11  ? -36.532 22.832  11.667  1.00 134.94 ? 1228 GLU B OE1   1 
ATOM   3814 O  OE2   . GLU B 1 11  ? -37.843 24.072  12.937  1.00 148.61 ? 1228 GLU B OE2   1 
ATOM   3815 N  N     . ASP B 1 12  ? -33.665 24.820  16.467  1.00 125.64 ? 1229 ASP B N     1 
ATOM   3816 C  CA    . ASP B 1 12  ? -33.255 25.571  17.639  1.00 131.54 ? 1229 ASP B CA    1 
ATOM   3817 C  C     . ASP B 1 12  ? -32.203 24.864  18.483  1.00 129.99 ? 1229 ASP B C     1 
ATOM   3818 O  O     . ASP B 1 12  ? -31.261 25.543  18.951  1.00 126.66 ? 1229 ASP B O     1 
ATOM   3819 C  CB    . ASP B 1 12  ? -34.510 25.848  18.486  1.00 144.32 ? 1229 ASP B CB    1 
ATOM   3820 C  CG    . ASP B 1 12  ? -34.293 26.817  19.626  1.00 166.66 ? 1229 ASP B CG    1 
ATOM   3821 O  OD1   . ASP B 1 12  ? -33.616 27.812  19.381  1.00 173.32 ? 1229 ASP B OD1   1 
ATOM   3822 O  OD2   . ASP B 1 12  ? -34.891 26.597  20.699  1.00 174.69 ? 1229 ASP B OD2   1 
ATOM   3823 N  N     . ASN B 1 13  ? -32.337 23.561  18.752  1.00 121.90 ? 1230 ASN B N     1 
ATOM   3824 C  CA    . ASN B 1 13  ? -31.362 22.794  19.543  1.00 122.05 ? 1230 ASN B CA    1 
ATOM   3825 C  C     . ASN B 1 13  ? -31.006 21.552  18.749  1.00 119.90 ? 1230 ASN B C     1 
ATOM   3826 O  O     . ASN B 1 13  ? -31.627 20.511  18.919  1.00 127.51 ? 1230 ASN B O     1 
ATOM   3827 C  CB    . ASN B 1 13  ? -31.878 22.470  20.921  1.00 122.55 ? 1230 ASN B CB    1 
ATOM   3828 C  CG    . ASN B 1 13  ? -30.851 21.762  21.793  1.00 128.01 ? 1230 ASN B CG    1 
ATOM   3829 O  OD1   . ASN B 1 13  ? -29.785 21.364  21.301  1.00 127.96 ? 1230 ASN B OD1   1 
ATOM   3830 N  ND2   . ASN B 1 13  ? -31.152 21.602  23.073  1.00 132.01 ? 1230 ASN B ND2   1 
ATOM   3831 N  N     . LEU B 1 14  ? -29.998 21.673  17.901  1.00 107.68 ? 1231 LEU B N     1 
ATOM   3832 C  CA    . LEU B 1 14  ? -29.639 20.545  17.051  1.00 95.02  ? 1231 LEU B CA    1 
ATOM   3833 C  C     . LEU B 1 14  ? -29.150 19.327  17.828  1.00 95.46  ? 1231 LEU B C     1 
ATOM   3834 O  O     . LEU B 1 14  ? -29.579 18.208  17.499  1.00 91.57  ? 1231 LEU B O     1 
ATOM   3835 C  CB    . LEU B 1 14  ? -28.600 20.998  16.036  1.00 88.68  ? 1231 LEU B CB    1 
ATOM   3836 C  CG    . LEU B 1 14  ? -28.410 19.953  14.946  1.00 85.95  ? 1231 LEU B CG    1 
ATOM   3837 C  CD1   . LEU B 1 14  ? -29.700 19.798  14.179  1.00 88.13  ? 1231 LEU B CD1   1 
ATOM   3838 C  CD2   . LEU B 1 14  ? -27.262 20.292  14.020  1.00 75.84  ? 1231 LEU B CD2   1 
ATOM   3839 N  N     . PRO B 1 15  ? -28.251 19.445  18.816  1.00 100.41 ? 1232 PRO B N     1 
ATOM   3840 C  CA    . PRO B 1 15  ? -27.696 18.219  19.411  1.00 95.53  ? 1232 PRO B CA    1 
ATOM   3841 C  C     . PRO B 1 15  ? -28.704 17.397  20.181  1.00 101.52 ? 1232 PRO B C     1 
ATOM   3842 O  O     . PRO B 1 15  ? -28.724 16.164  20.028  1.00 104.30 ? 1232 PRO B O     1 
ATOM   3843 C  CB    . PRO B 1 15  ? -26.573 18.741  20.319  1.00 94.42  ? 1232 PRO B CB    1 
ATOM   3844 C  CG    . PRO B 1 15  ? -26.214 20.053  19.751  1.00 97.07  ? 1232 PRO B CG    1 
ATOM   3845 C  CD    . PRO B 1 15  ? -27.520 20.636  19.285  1.00 103.39 ? 1232 PRO B CD    1 
ATOM   3846 N  N     . ASP B 1 16  ? -29.545 18.027  20.995  1.00 106.98 ? 1233 ASP B N     1 
ATOM   3847 C  CA    . ASP B 1 16  ? -30.517 17.235  21.733  1.00 116.82 ? 1233 ASP B CA    1 
ATOM   3848 C  C     . ASP B 1 16  ? -31.648 16.737  20.837  1.00 109.53 ? 1233 ASP B C     1 
ATOM   3849 O  O     . ASP B 1 16  ? -32.226 15.688  21.116  1.00 117.25 ? 1233 ASP B O     1 
ATOM   3850 C  CB    . ASP B 1 16  ? -31.063 18.033  22.915  1.00 129.05 ? 1233 ASP B CB    1 
ATOM   3851 C  CG    . ASP B 1 16  ? -29.962 18.558  23.819  1.00 137.64 ? 1233 ASP B CG    1 
ATOM   3852 O  OD1   . ASP B 1 16  ? -29.221 17.731  24.388  1.00 142.00 ? 1233 ASP B OD1   1 
ATOM   3853 O  OD2   . ASP B 1 16  ? -29.844 19.789  23.973  1.00 140.25 ? 1233 ASP B OD2   1 
ATOM   3854 N  N     . TRP B 1 17  ? -31.936 17.442  19.746  1.00 97.71  ? 1234 TRP B N     1 
ATOM   3855 C  CA    . TRP B 1 17  ? -32.799 16.882  18.712  1.00 88.17  ? 1234 TRP B CA    1 
ATOM   3856 C  C     . TRP B 1 17  ? -32.187 15.631  18.090  1.00 87.55  ? 1234 TRP B C     1 
ATOM   3857 O  O     . TRP B 1 17  ? -32.893 14.657  17.831  1.00 99.52  ? 1234 TRP B O     1 
ATOM   3858 C  CB    . TRP B 1 17  ? -33.054 17.926  17.643  1.00 77.42  ? 1234 TRP B CB    1 
ATOM   3859 C  CG    . TRP B 1 17  ? -33.584 17.372  16.359  1.00 77.76  ? 1234 TRP B CG    1 
ATOM   3860 C  CD1   . TRP B 1 17  ? -34.891 17.279  15.989  1.00 71.19  ? 1234 TRP B CD1   1 
ATOM   3861 C  CD2   . TRP B 1 17  ? -32.817 16.881  15.249  1.00 82.10  ? 1234 TRP B CD2   1 
ATOM   3862 N  NE1   . TRP B 1 17  ? -34.990 16.764  14.721  1.00 73.87  ? 1234 TRP B NE1   1 
ATOM   3863 C  CE2   . TRP B 1 17  ? -33.729 16.510  14.245  1.00 78.67  ? 1234 TRP B CE2   1 
ATOM   3864 C  CE3   . TRP B 1 17  ? -31.447 16.723  15.007  1.00 84.64  ? 1234 TRP B CE3   1 
ATOM   3865 C  CZ2   . TRP B 1 17  ? -33.317 15.987  13.021  1.00 68.02  ? 1234 TRP B CZ2   1 
ATOM   3866 C  CZ3   . TRP B 1 17  ? -31.042 16.199  13.799  1.00 76.91  ? 1234 TRP B CZ3   1 
ATOM   3867 C  CH2   . TRP B 1 17  ? -31.972 15.847  12.818  1.00 71.76  ? 1234 TRP B CH2   1 
ATOM   3868 N  N     . TYR B 1 18  ? -30.884 15.660  17.799  1.00 74.13  ? 1235 TYR B N     1 
ATOM   3869 C  CA    . TYR B 1 18  ? -30.226 14.491  17.238  1.00 82.14  ? 1235 TYR B CA    1 
ATOM   3870 C  C     . TYR B 1 18  ? -30.303 13.328  18.212  1.00 91.62  ? 1235 TYR B C     1 
ATOM   3871 O  O     . TYR B 1 18  ? -30.573 12.185  17.817  1.00 90.39  ? 1235 TYR B O     1 
ATOM   3872 C  CB    . TYR B 1 18  ? -28.771 14.831  16.927  1.00 81.81  ? 1235 TYR B CB    1 
ATOM   3873 C  CG    . TYR B 1 18  ? -27.971 13.789  16.170  1.00 75.74  ? 1235 TYR B CG    1 
ATOM   3874 C  CD1   . TYR B 1 18  ? -28.063 13.687  14.784  1.00 75.14  ? 1235 TYR B CD1   1 
ATOM   3875 C  CD2   . TYR B 1 18  ? -27.075 12.952  16.833  1.00 68.48  ? 1235 TYR B CD2   1 
ATOM   3876 C  CE1   . TYR B 1 18  ? -27.296 12.778  14.081  1.00 73.73  ? 1235 TYR B CE1   1 
ATOM   3877 C  CE2   . TYR B 1 18  ? -26.317 12.037  16.139  1.00 69.68  ? 1235 TYR B CE2   1 
ATOM   3878 C  CZ    . TYR B 1 18  ? -26.435 11.946  14.766  1.00 74.18  ? 1235 TYR B CZ    1 
ATOM   3879 O  OH    . TYR B 1 18  ? -25.684 11.019  14.088  1.00 74.18  ? 1235 TYR B OH    1 
ATOM   3880 N  N     . SER B 1 19  ? -30.118 13.614  19.503  1.00 91.79  ? 1236 SER B N     1 
ATOM   3881 C  CA    . SER B 1 19  ? -30.181 12.556  20.505  1.00 92.29  ? 1236 SER B CA    1 
ATOM   3882 C  C     . SER B 1 19  ? -31.586 11.987  20.623  1.00 91.30  ? 1236 SER B C     1 
ATOM   3883 O  O     . SER B 1 19  ? -31.764 10.759  20.667  1.00 93.98  ? 1236 SER B O     1 
ATOM   3884 C  CB    . SER B 1 19  ? -29.708 13.098  21.849  1.00 92.28  ? 1236 SER B CB    1 
ATOM   3885 O  OG    . SER B 1 19  ? -30.397 12.451  22.902  1.00 107.84 ? 1236 SER B OG    1 
ATOM   3886 N  N     . GLN B 1 20  ? -32.602 12.855  20.577  1.00 88.16  ? 1237 GLN B N     1 
ATOM   3887 C  CA    . GLN B 1 20  ? -33.972 12.358  20.611  1.00 81.33  ? 1237 GLN B CA    1 
ATOM   3888 C  C     . GLN B 1 20  ? -34.324 11.599  19.333  1.00 79.61  ? 1237 GLN B C     1 
ATOM   3889 O  O     . GLN B 1 20  ? -35.067 10.617  19.387  1.00 86.75  ? 1237 GLN B O     1 
ATOM   3890 C  CB    . GLN B 1 20  ? -34.942 13.506  20.851  1.00 84.83  ? 1237 GLN B CB    1 
ATOM   3891 C  CG    . GLN B 1 20  ? -35.176 13.814  22.322  1.00 102.84 ? 1237 GLN B CG    1 
ATOM   3892 C  CD    . GLN B 1 20  ? -36.559 13.389  22.791  1.00 120.20 ? 1237 GLN B CD    1 
ATOM   3893 O  OE1   . GLN B 1 20  ? -37.513 13.364  22.009  1.00 123.52 ? 1237 GLN B OE1   1 
ATOM   3894 N  NE2   . GLN B 1 20  ? -36.676 13.052  24.075  1.00 128.00 ? 1237 GLN B NE2   1 
ATOM   3895 N  N     . VAL B 1 21  ? -33.731 11.970  18.198  1.00 76.19  ? 1238 VAL B N     1 
ATOM   3896 C  CA    . VAL B 1 21  ? -34.039 11.285  16.949  1.00 78.31  ? 1238 VAL B CA    1 
ATOM   3897 C  C     . VAL B 1 21  ? -33.414 9.897   16.924  1.00 76.05  ? 1238 VAL B C     1 
ATOM   3898 O  O     . VAL B 1 21  ? -34.039 8.932   16.483  1.00 67.61  ? 1238 VAL B O     1 
ATOM   3899 C  CB    . VAL B 1 21  ? -33.561 12.133  15.754  1.00 83.76  ? 1238 VAL B CB    1 
ATOM   3900 C  CG1   . VAL B 1 21  ? -33.332 11.257  14.504  1.00 81.09  ? 1238 VAL B CG1   1 
ATOM   3901 C  CG2   . VAL B 1 21  ? -34.574 13.234  15.451  1.00 89.25  ? 1238 VAL B CG2   1 
ATOM   3902 N  N     . ILE B 1 22  ? -32.194 9.763   17.435  1.00 73.22  ? 1239 ILE B N     1 
ATOM   3903 C  CA    . ILE B 1 22  ? -31.576 8.446   17.434  1.00 69.07  ? 1239 ILE B CA    1 
ATOM   3904 C  C     . ILE B 1 22  ? -32.087 7.558   18.571  1.00 75.48  ? 1239 ILE B C     1 
ATOM   3905 O  O     . ILE B 1 22  ? -31.996 6.328   18.466  1.00 78.93  ? 1239 ILE B O     1 
ATOM   3906 C  CB    . ILE B 1 22  ? -30.048 8.577   17.484  1.00 69.01  ? 1239 ILE B CB    1 
ATOM   3907 C  CG1   . ILE B 1 22  ? -29.641 9.354   18.730  1.00 67.99  ? 1239 ILE B CG1   1 
ATOM   3908 C  CG2   . ILE B 1 22  ? -29.525 9.271   16.225  1.00 62.39  ? 1239 ILE B CG2   1 
ATOM   3909 C  CD1   . ILE B 1 22  ? -28.188 9.635   18.752  1.00 68.91  ? 1239 ILE B CD1   1 
ATOM   3910 N  N     . THR B 1 23  ? -32.610 8.133   19.665  1.00 72.27  ? 1240 THR B N     1 
ATOM   3911 C  CA    . THR B 1 23  ? -33.170 7.294   20.726  1.00 65.79  ? 1240 THR B CA    1 
ATOM   3912 C  C     . THR B 1 23  ? -34.633 6.932   20.471  1.00 72.83  ? 1240 THR B C     1 
ATOM   3913 O  O     . THR B 1 23  ? -35.027 5.775   20.633  1.00 79.05  ? 1240 THR B O     1 
ATOM   3914 C  CB    . THR B 1 23  ? -33.085 7.974   22.093  1.00 60.80  ? 1240 THR B CB    1 
ATOM   3915 O  OG1   . THR B 1 23  ? -33.866 9.174   22.059  1.00 69.65  ? 1240 THR B OG1   1 
ATOM   3916 C  CG2   . THR B 1 23  ? -31.652 8.268   22.468  1.00 56.52  ? 1240 THR B CG2   1 
ATOM   3917 N  N     . LYS B 1 24  ? -35.471 7.907   20.128  1.00 67.16  ? 1241 LYS B N     1 
ATOM   3918 C  CA    . LYS B 1 24  ? -36.861 7.556   19.888  1.00 72.93  ? 1241 LYS B CA    1 
ATOM   3919 C  C     . LYS B 1 24  ? -37.036 6.864   18.548  1.00 79.97  ? 1241 LYS B C     1 
ATOM   3920 O  O     . LYS B 1 24  ? -38.131 6.369   18.264  1.00 85.21  ? 1241 LYS B O     1 
ATOM   3921 C  CB    . LYS B 1 24  ? -37.758 8.799   19.987  1.00 62.84  ? 1241 LYS B CB    1 
ATOM   3922 C  CG    . LYS B 1 24  ? -37.473 9.597   21.233  1.00 63.98  ? 1241 LYS B CG    1 
ATOM   3923 C  CD    . LYS B 1 24  ? -38.651 10.446  21.674  1.00 76.18  ? 1241 LYS B CD    1 
ATOM   3924 C  CE    . LYS B 1 24  ? -38.690 10.542  23.204  1.00 85.16  ? 1241 LYS B CE    1 
ATOM   3925 N  NZ    . LYS B 1 24  ? -40.047 10.959  23.709  1.00 85.06  ? 1241 LYS B NZ    1 
ATOM   3926 N  N     . GLY B 1 25  ? -36.000 6.825   17.716  1.00 76.94  ? 1242 GLY B N     1 
ATOM   3927 C  CA    . GLY B 1 25  ? -36.002 5.997   16.528  1.00 84.31  ? 1242 GLY B CA    1 
ATOM   3928 C  C     . GLY B 1 25  ? -35.495 4.575   16.687  1.00 88.74  ? 1242 GLY B C     1 
ATOM   3929 O  O     . GLY B 1 25  ? -35.315 3.901   15.665  1.00 93.45  ? 1242 GLY B O     1 
ATOM   3930 N  N     . GLU B 1 26  ? -35.228 4.107   17.919  1.00 92.19  ? 1243 GLU B N     1 
ATOM   3931 C  CA    . GLU B 1 26  ? -34.826 2.720   18.173  1.00 92.01  ? 1243 GLU B CA    1 
ATOM   3932 C  C     . GLU B 1 26  ? -33.572 2.377   17.383  1.00 89.78  ? 1243 GLU B C     1 
ATOM   3933 O  O     . GLU B 1 26  ? -33.399 1.242   16.926  1.00 90.86  ? 1243 GLU B O     1 
ATOM   3934 C  CB    . GLU B 1 26  ? -35.954 1.726   17.856  1.00 86.32  ? 1243 GLU B CB    1 
ATOM   3935 C  CG    . GLU B 1 26  ? -37.034 1.641   18.948  1.00 95.31  ? 1243 GLU B CG    1 
ATOM   3936 C  CD    . GLU B 1 26  ? -38.112 0.545   18.727  1.00 91.45  ? 1243 GLU B CD    1 
ATOM   3937 O  OE1   . GLU B 1 26  ? -39.041 0.516   19.560  1.00 88.98  ? 1243 GLU B OE1   1 
ATOM   3938 O  OE2   . GLU B 1 26  ? -38.049 -0.275  17.764  1.00 75.46  ? 1243 GLU B OE2   1 
ATOM   3939 N  N     . MET B 1 27  ? -32.711 3.354   17.226  1.00 85.51  ? 1244 MET B N     1 
ATOM   3940 C  CA    . MET B 1 27  ? -31.499 3.158   16.489  1.00 77.42  ? 1244 MET B CA    1 
ATOM   3941 C  C     . MET B 1 27  ? -30.274 2.927   17.261  1.00 75.27  ? 1244 MET B C     1 
ATOM   3942 O  O     . MET B 1 27  ? -29.419 2.280   16.798  1.00 73.42  ? 1244 MET B O     1 
ATOM   3943 C  CB    . MET B 1 27  ? -31.171 4.392   15.725  1.00 60.33  ? 1244 MET B CB    1 
ATOM   3944 C  CG    . MET B 1 27  ? -32.149 4.708   14.694  1.00 63.76  ? 1244 MET B CG    1 
ATOM   3945 S  SD    . MET B 1 27  ? -31.399 5.042   13.151  1.00 85.99  ? 1244 MET B SD    1 
ATOM   3946 C  CE    . MET B 1 27  ? -30.398 6.396   13.532  1.00 86.22  ? 1244 MET B CE    1 
ATOM   3947 N  N     . ILE B 1 28  ? -30.245 3.412   18.465  1.00 71.77  ? 1245 ILE B N     1 
ATOM   3948 C  CA    . ILE B 1 28  ? -29.051 3.513   19.286  1.00 72.34  ? 1245 ILE B CA    1 
ATOM   3949 C  C     . ILE B 1 28  ? -29.466 3.209   20.712  1.00 72.95  ? 1245 ILE B C     1 
ATOM   3950 O  O     . ILE B 1 28  ? -30.528 3.651   21.162  1.00 80.27  ? 1245 ILE B O     1 
ATOM   3951 C  CB    . ILE B 1 28  ? -28.443 4.933   19.175  1.00 74.21  ? 1245 ILE B CB    1 
ATOM   3952 C  CG1   . ILE B 1 28  ? -27.753 5.121   17.824  1.00 74.63  ? 1245 ILE B CG1   1 
ATOM   3953 C  CG2   . ILE B 1 28  ? -27.548 5.287   20.381  1.00 66.48  ? 1245 ILE B CG2   1 
ATOM   3954 C  CD1   . ILE B 1 28  ? -26.821 4.013   17.483  1.00 69.86  ? 1245 ILE B CD1   1 
ATOM   3955 N  N     . GLU B 1 29  ? -28.629 2.476   21.432  1.00 66.15  ? 1246 GLU B N     1 
ATOM   3956 C  CA    . GLU B 1 29  ? -28.790 2.386   22.872  1.00 69.26  ? 1246 GLU B CA    1 
ATOM   3957 C  C     . GLU B 1 29  ? -27.492 2.783   23.543  1.00 75.09  ? 1246 GLU B C     1 
ATOM   3958 O  O     . GLU B 1 29  ? -26.417 2.349   23.123  1.00 78.09  ? 1246 GLU B O     1 
ATOM   3959 C  CB    . GLU B 1 29  ? -29.201 0.986   23.303  1.00 70.54  ? 1246 GLU B CB    1 
ATOM   3960 C  CG    . GLU B 1 29  ? -29.506 0.866   24.781  1.00 71.35  ? 1246 GLU B CG    1 
ATOM   3961 C  CD    . GLU B 1 29  ? -30.621 1.775   25.216  1.00 78.64  ? 1246 GLU B CD    1 
ATOM   3962 O  OE1   . GLU B 1 29  ? -30.467 2.408   26.284  1.00 84.23  ? 1246 GLU B OE1   1 
ATOM   3963 O  OE2   . GLU B 1 29  ? -31.646 1.853   24.490  1.00 76.94  ? 1246 GLU B OE2   1 
ATOM   3964 N  N     . TYR B 1 30  ? -27.603 3.591   24.599  1.00 82.60  ? 1247 TYR B N     1 
ATOM   3965 C  CA    . TYR B 1 30  ? -26.417 4.146   25.222  1.00 83.03  ? 1247 TYR B CA    1 
ATOM   3966 C  C     . TYR B 1 30  ? -25.687 3.055   26.003  1.00 85.63  ? 1247 TYR B C     1 
ATOM   3967 O  O     . TYR B 1 30  ? -26.245 1.996   26.319  1.00 89.07  ? 1247 TYR B O     1 
ATOM   3968 C  CB    . TYR B 1 30  ? -26.795 5.343   26.106  1.00 79.99  ? 1247 TYR B CB    1 
ATOM   3969 C  CG    . TYR B 1 30  ? -27.305 6.539   25.300  1.00 85.99  ? 1247 TYR B CG    1 
ATOM   3970 C  CD1   . TYR B 1 30  ? -26.457 7.248   24.449  1.00 79.38  ? 1247 TYR B CD1   1 
ATOM   3971 C  CD2   . TYR B 1 30  ? -28.633 6.940   25.374  1.00 94.74  ? 1247 TYR B CD2   1 
ATOM   3972 C  CE1   . TYR B 1 30  ? -26.914 8.319   23.700  1.00 81.82  ? 1247 TYR B CE1   1 
ATOM   3973 C  CE2   . TYR B 1 30  ? -29.099 8.018   24.632  1.00 98.67  ? 1247 TYR B CE2   1 
ATOM   3974 C  CZ    . TYR B 1 30  ? -28.235 8.704   23.791  1.00 97.48  ? 1247 TYR B CZ    1 
ATOM   3975 O  OH    . TYR B 1 30  ? -28.696 9.782   23.047  1.00 105.61 ? 1247 TYR B OH    1 
ATOM   3976 N  N     . TYR B 1 31  ? -24.410 3.318   26.285  1.00 78.91  ? 1248 TYR B N     1 
ATOM   3977 C  CA    . TYR B 1 31  ? -23.475 2.276   26.685  1.00 84.84  ? 1248 TYR B CA    1 
ATOM   3978 C  C     . TYR B 1 31  ? -22.445 2.860   27.641  1.00 81.79  ? 1248 TYR B C     1 
ATOM   3979 O  O     . TYR B 1 31  ? -22.006 4.000   27.479  1.00 90.76  ? 1248 TYR B O     1 
ATOM   3980 C  CB    . TYR B 1 31  ? -22.794 1.644   25.459  1.00 92.13  ? 1248 TYR B CB    1 
ATOM   3981 C  CG    . TYR B 1 31  ? -22.038 0.378   25.780  1.00 95.09  ? 1248 TYR B CG    1 
ATOM   3982 C  CD1   . TYR B 1 31  ? -22.672 -0.698  26.396  1.00 94.96  ? 1248 TYR B CD1   1 
ATOM   3983 C  CD2   . TYR B 1 31  ? -20.690 0.263   25.480  1.00 89.36  ? 1248 TYR B CD2   1 
ATOM   3984 C  CE1   . TYR B 1 31  ? -21.978 -1.851  26.704  1.00 96.41  ? 1248 TYR B CE1   1 
ATOM   3985 C  CE2   . TYR B 1 31  ? -20.000 -0.878  25.777  1.00 93.46  ? 1248 TYR B CE2   1 
ATOM   3986 C  CZ    . TYR B 1 31  ? -20.643 -1.930  26.389  1.00 97.33  ? 1248 TYR B CZ    1 
ATOM   3987 O  OH    . TYR B 1 31  ? -19.922 -3.054  26.679  1.00 100.44 ? 1248 TYR B OH    1 
ATOM   3988 N  N     . ASP B 1 32  ? -22.020 2.043   28.605  1.00 86.57  ? 1249 ASP B N     1 
ATOM   3989 C  CA    . ASP B 1 32  ? -21.188 2.501   29.713  1.00 87.22  ? 1249 ASP B CA    1 
ATOM   3990 C  C     . ASP B 1 32  ? -19.709 2.611   29.367  1.00 80.40  ? 1249 ASP B C     1 
ATOM   3991 O  O     . ASP B 1 32  ? -18.885 2.811   30.266  1.00 74.12  ? 1249 ASP B O     1 
ATOM   3992 C  CB    . ASP B 1 32  ? -21.379 1.593   30.934  1.00 96.95  ? 1249 ASP B CB    1 
ATOM   3993 C  CG    . ASP B 1 32  ? -21.009 0.157   30.673  1.00 110.40 ? 1249 ASP B CG    1 
ATOM   3994 O  OD1   . ASP B 1 32  ? -20.960 -0.271  29.498  1.00 118.94 ? 1249 ASP B OD1   1 
ATOM   3995 O  OD2   . ASP B 1 32  ? -20.796 -0.558  31.671  1.00 114.91 ? 1249 ASP B OD2   1 
ATOM   3996 N  N     . VAL B 1 33  ? -19.360 2.532   28.091  1.00 83.98  ? 1250 VAL B N     1 
ATOM   3997 C  CA    . VAL B 1 33  ? -18.027 2.866   27.613  1.00 86.30  ? 1250 VAL B CA    1 
ATOM   3998 C  C     . VAL B 1 33  ? -18.164 4.084   26.716  1.00 83.97  ? 1250 VAL B C     1 
ATOM   3999 O  O     . VAL B 1 33  ? -18.881 4.049   25.707  1.00 87.83  ? 1250 VAL B O     1 
ATOM   4000 C  CB    . VAL B 1 33  ? -17.376 1.704   26.847  1.00 89.42  ? 1250 VAL B CB    1 
ATOM   4001 C  CG1   . VAL B 1 33  ? -15.936 2.071   26.444  1.00 85.31  ? 1250 VAL B CG1   1 
ATOM   4002 C  CG2   . VAL B 1 33  ? -17.439 0.414   27.671  1.00 91.91  ? 1250 VAL B CG2   1 
ATOM   4003 N  N     . SER B 1 34  ? -17.465 5.150   27.056  1.00 79.53  ? 1251 SER B N     1 
ATOM   4004 C  CA    . SER B 1 34  ? -17.669 6.357   26.284  1.00 84.52  ? 1251 SER B CA    1 
ATOM   4005 C  C     . SER B 1 34  ? -17.121 6.178   24.871  1.00 78.46  ? 1251 SER B C     1 
ATOM   4006 O  O     . SER B 1 34  ? -16.157 5.439   24.632  1.00 89.31  ? 1251 SER B O     1 
ATOM   4007 C  CB    . SER B 1 34  ? -17.008 7.549   26.975  1.00 100.64 ? 1251 SER B CB    1 
ATOM   4008 O  OG    . SER B 1 34  ? -17.191 7.504   28.381  1.00 107.15 ? 1251 SER B OG    1 
ATOM   4009 N  N     . GLY B 1 35  ? -17.753 6.872   23.927  1.00 65.62  ? 1252 GLY B N     1 
ATOM   4010 C  CA    . GLY B 1 35  ? -17.422 6.743   22.534  1.00 59.60  ? 1252 GLY B CA    1 
ATOM   4011 C  C     . GLY B 1 35  ? -18.082 5.602   21.839  1.00 71.04  ? 1252 GLY B C     1 
ATOM   4012 O  O     . GLY B 1 35  ? -17.972 5.503   20.608  1.00 84.31  ? 1252 GLY B O     1 
ATOM   4013 N  N     . CYS B 1 36  ? -18.782 4.738   22.565  1.00 67.78  ? 1253 CYS B N     1 
ATOM   4014 C  CA    . CYS B 1 36  ? -19.299 3.519   21.974  1.00 69.51  ? 1253 CYS B CA    1 
ATOM   4015 C  C     . CYS B 1 36  ? -20.796 3.413   22.213  1.00 82.09  ? 1253 CYS B C     1 
ATOM   4016 O  O     . CYS B 1 36  ? -21.299 3.735   23.295  1.00 90.64  ? 1253 CYS B O     1 
ATOM   4017 C  CB    . CYS B 1 36  ? -18.573 2.312   22.548  1.00 72.76  ? 1253 CYS B CB    1 
ATOM   4018 S  SG    . CYS B 1 36  ? -16.765 2.530   22.549  1.00 77.73  ? 1253 CYS B SG    1 
ATOM   4019 N  N     . TYR B 1 37  ? -21.509 2.955   21.193  1.00 77.75  ? 1254 TYR B N     1 
ATOM   4020 C  CA    . TYR B 1 37  ? -22.953 2.957   21.213  1.00 72.29  ? 1254 TYR B CA    1 
ATOM   4021 C  C     . TYR B 1 37  ? -23.426 1.681   20.557  1.00 74.75  ? 1254 TYR B C     1 
ATOM   4022 O  O     . TYR B 1 37  ? -22.825 1.214   19.589  1.00 83.79  ? 1254 TYR B O     1 
ATOM   4023 C  CB    . TYR B 1 37  ? -23.546 4.170   20.480  1.00 73.17  ? 1254 TYR B CB    1 
ATOM   4024 C  CG    . TYR B 1 37  ? -23.012 5.497   20.951  1.00 75.28  ? 1254 TYR B CG    1 
ATOM   4025 C  CD1   . TYR B 1 37  ? -23.604 6.169   22.017  1.00 77.98  ? 1254 TYR B CD1   1 
ATOM   4026 C  CD2   . TYR B 1 37  ? -21.914 6.085   20.328  1.00 69.44  ? 1254 TYR B CD2   1 
ATOM   4027 C  CE1   . TYR B 1 37  ? -23.120 7.395   22.446  1.00 79.64  ? 1254 TYR B CE1   1 
ATOM   4028 C  CE2   . TYR B 1 37  ? -21.428 7.309   20.747  1.00 80.82  ? 1254 TYR B CE2   1 
ATOM   4029 C  CZ    . TYR B 1 37  ? -22.035 7.961   21.801  1.00 81.76  ? 1254 TYR B CZ    1 
ATOM   4030 O  OH    . TYR B 1 37  ? -21.530 9.168   22.213  1.00 81.39  ? 1254 TYR B OH    1 
ATOM   4031 N  N     . ILE B 1 38  ? -24.536 1.153   21.069  1.00 68.87  ? 1255 ILE B N     1 
ATOM   4032 C  CA    . ILE B 1 38  ? -25.123 -0.070  20.544  1.00 74.43  ? 1255 ILE B CA    1 
ATOM   4033 C  C     . ILE B 1 38  ? -25.908 0.269   19.287  1.00 72.31  ? 1255 ILE B C     1 
ATOM   4034 O  O     . ILE B 1 38  ? -26.852 1.065   19.333  1.00 68.91  ? 1255 ILE B O     1 
ATOM   4035 C  CB    . ILE B 1 38  ? -26.038 -0.738  21.575  1.00 68.27  ? 1255 ILE B CB    1 
ATOM   4036 C  CG1   . ILE B 1 38  ? -25.285 -1.042  22.857  1.00 66.37  ? 1255 ILE B CG1   1 
ATOM   4037 C  CG2   . ILE B 1 38  ? -26.625 -1.991  20.974  1.00 57.04  ? 1255 ILE B CG2   1 
ATOM   4038 C  CD1   . ILE B 1 38  ? -26.184 -1.327  24.003  1.00 61.69  ? 1255 ILE B CD1   1 
ATOM   4039 N  N     . LEU B 1 39  ? -25.545 -0.356  18.174  1.00 70.05  ? 1256 LEU B N     1 
ATOM   4040 C  CA    . LEU B 1 39  ? -26.360 -0.247  16.969  1.00 69.99  ? 1256 LEU B CA    1 
ATOM   4041 C  C     . LEU B 1 39  ? -27.487 -1.256  17.089  1.00 71.55  ? 1256 LEU B C     1 
ATOM   4042 O  O     . LEU B 1 39  ? -27.276 -2.460  16.925  1.00 73.02  ? 1256 LEU B O     1 
ATOM   4043 C  CB    . LEU B 1 39  ? -25.541 -0.499  15.710  1.00 53.65  ? 1256 LEU B CB    1 
ATOM   4044 C  CG    . LEU B 1 39  ? -24.188 0.194   15.641  1.00 59.34  ? 1256 LEU B CG    1 
ATOM   4045 C  CD1   . LEU B 1 39  ? -23.613 -0.092  14.281  1.00 48.33  ? 1256 LEU B CD1   1 
ATOM   4046 C  CD2   . LEU B 1 39  ? -24.334 1.695   15.878  1.00 45.26  ? 1256 LEU B CD2   1 
ATOM   4047 N  N     . ARG B 1 40  ? -28.686 -0.763  17.395  1.00 64.61  ? 1257 ARG B N     1 
ATOM   4048 C  CA    . ARG B 1 40  ? -29.861 -1.612  17.422  1.00 57.95  ? 1257 ARG B CA    1 
ATOM   4049 C  C     . ARG B 1 40  ? -30.218 -2.020  16.003  1.00 70.56  ? 1257 ARG B C     1 
ATOM   4050 O  O     . ARG B 1 40  ? -29.653 -1.510  15.025  1.00 74.57  ? 1257 ARG B O     1 
ATOM   4051 C  CB    . ARG B 1 40  ? -31.024 -0.894  18.086  1.00 56.98  ? 1257 ARG B CB    1 
ATOM   4052 C  CG    . ARG B 1 40  ? -30.602 -0.194  19.337  1.00 62.07  ? 1257 ARG B CG    1 
ATOM   4053 C  CD    . ARG B 1 40  ? -31.789 0.176   20.151  1.00 72.82  ? 1257 ARG B CD    1 
ATOM   4054 N  NE    . ARG B 1 40  ? -32.684 -0.958  20.262  1.00 75.85  ? 1257 ARG B NE    1 
ATOM   4055 C  CZ    . ARG B 1 40  ? -33.954 -0.861  20.615  1.00 81.13  ? 1257 ARG B CZ    1 
ATOM   4056 N  NH1   . ARG B 1 40  ? -34.476 0.326   20.888  1.00 73.30  ? 1257 ARG B NH1   1 
ATOM   4057 N  NH2   . ARG B 1 40  ? -34.694 -1.953  20.679  1.00 90.00  ? 1257 ARG B NH2   1 
ATOM   4058 N  N     . HIS B 1 41  ? -31.163 -2.959  15.882  1.00 64.00  ? 1258 HIS B N     1 
ATOM   4059 C  CA    . HIS B 1 41  ? -31.384 -3.528  14.560  1.00 64.64  ? 1258 HIS B CA    1 
ATOM   4060 C  C     . HIS B 1 41  ? -31.841 -2.471  13.571  1.00 63.48  ? 1258 HIS B C     1 
ATOM   4061 O  O     . HIS B 1 41  ? -31.429 -2.505  12.401  1.00 55.35  ? 1258 HIS B O     1 
ATOM   4062 C  CB    . HIS B 1 41  ? -32.380 -4.688  14.615  1.00 69.38  ? 1258 HIS B CB    1 
ATOM   4063 C  CG    . HIS B 1 41  ? -33.780 -4.282  14.933  1.00 82.27  ? 1258 HIS B CG    1 
ATOM   4064 N  ND1   . HIS B 1 41  ? -34.809 -4.397  14.022  1.00 83.62  ? 1258 HIS B ND1   1 
ATOM   4065 C  CD2   . HIS B 1 41  ? -34.334 -3.799  16.071  1.00 87.29  ? 1258 HIS B CD2   1 
ATOM   4066 C  CE1   . HIS B 1 41  ? -35.933 -3.987  14.578  1.00 83.15  ? 1258 HIS B CE1   1 
ATOM   4067 N  NE2   . HIS B 1 41  ? -35.673 -3.618  15.821  1.00 88.43  ? 1258 HIS B NE2   1 
ATOM   4068 N  N     . TRP B 1 42  ? -32.579 -1.456  14.041  1.00 79.32  ? 1259 TRP B N     1 
ATOM   4069 C  CA    . TRP B 1 42  ? -33.150 -0.500  13.099  1.00 73.25  ? 1259 TRP B CA    1 
ATOM   4070 C  C     . TRP B 1 42  ? -32.076 0.336   12.396  1.00 67.64  ? 1259 TRP B C     1 
ATOM   4071 O  O     . TRP B 1 42  ? -32.222 0.645   11.210  1.00 73.09  ? 1259 TRP B O     1 
ATOM   4072 C  CB    . TRP B 1 42  ? -34.182 0.382   13.791  1.00 70.96  ? 1259 TRP B CB    1 
ATOM   4073 C  CG    . TRP B 1 42  ? -35.069 1.110   12.784  1.00 73.79  ? 1259 TRP B CG    1 
ATOM   4074 C  CD1   . TRP B 1 42  ? -35.057 2.442   12.500  1.00 65.47  ? 1259 TRP B CD1   1 
ATOM   4075 C  CD2   . TRP B 1 42  ? -36.058 0.534   11.918  1.00 76.15  ? 1259 TRP B CD2   1 
ATOM   4076 N  NE1   . TRP B 1 42  ? -35.956 2.731   11.518  1.00 58.61  ? 1259 TRP B NE1   1 
ATOM   4077 C  CE2   . TRP B 1 42  ? -36.601 1.584   11.152  1.00 70.43  ? 1259 TRP B CE2   1 
ATOM   4078 C  CE3   . TRP B 1 42  ? -36.553 -0.760  11.728  1.00 71.63  ? 1259 TRP B CE3   1 
ATOM   4079 C  CZ2   . TRP B 1 42  ? -37.618 1.380   10.209  1.00 71.44  ? 1259 TRP B CZ2   1 
ATOM   4080 C  CZ3   . TRP B 1 42  ? -37.577 -0.957  10.787  1.00 64.03  ? 1259 TRP B CZ3   1 
ATOM   4081 C  CH2   . TRP B 1 42  ? -38.085 0.101   10.041  1.00 63.83  ? 1259 TRP B CH2   1 
ATOM   4082 N  N     . SER B 1 43  ? -30.963 0.639   13.054  1.00 60.96  ? 1260 SER B N     1 
ATOM   4083 C  CA    . SER B 1 43  ? -29.913 1.359   12.330  1.00 74.07  ? 1260 SER B CA    1 
ATOM   4084 C  C     . SER B 1 43  ? -28.910 0.425   11.674  1.00 72.82  ? 1260 SER B C     1 
ATOM   4085 O  O     . SER B 1 43  ? -28.375 0.731   10.583  1.00 73.50  ? 1260 SER B O     1 
ATOM   4086 C  CB    . SER B 1 43  ? -29.169 2.334   13.265  1.00 65.25  ? 1260 SER B CB    1 
ATOM   4087 O  OG    . SER B 1 43  ? -28.599 1.704   14.399  1.00 59.49  ? 1260 SER B OG    1 
ATOM   4088 N  N     . PHE B 1 44  ? -28.694 -0.737  12.284  1.00 70.58  ? 1261 PHE B N     1 
ATOM   4089 C  CA    . PHE B 1 44  ? -27.786 -1.689  11.672  1.00 66.93  ? 1261 PHE B CA    1 
ATOM   4090 C  C     . PHE B 1 44  ? -28.279 -2.109  10.297  1.00 62.31  ? 1261 PHE B C     1 
ATOM   4091 O  O     . PHE B 1 44  ? -27.467 -2.416  9.414   1.00 55.85  ? 1261 PHE B O     1 
ATOM   4092 C  CB    . PHE B 1 44  ? -27.583 -2.909  12.569  1.00 60.38  ? 1261 PHE B CB    1 
ATOM   4093 C  CG    . PHE B 1 44  ? -26.535 -3.827  12.047  1.00 65.46  ? 1261 PHE B CG    1 
ATOM   4094 C  CD1   . PHE B 1 44  ? -25.241 -3.748  12.520  1.00 64.11  ? 1261 PHE B CD1   1 
ATOM   4095 C  CD2   . PHE B 1 44  ? -26.838 -4.739  11.028  1.00 58.66  ? 1261 PHE B CD2   1 
ATOM   4096 C  CE1   . PHE B 1 44  ? -24.275 -4.563  12.010  1.00 58.54  ? 1261 PHE B CE1   1 
ATOM   4097 C  CE2   . PHE B 1 44  ? -25.894 -5.542  10.505  1.00 47.44  ? 1261 PHE B CE2   1 
ATOM   4098 C  CZ    . PHE B 1 44  ? -24.599 -5.466  10.997  1.00 54.77  ? 1261 PHE B CZ    1 
ATOM   4099 N  N     . ALA B 1 45  ? -29.593 -2.117  10.087  1.00 53.20  ? 1262 ALA B N     1 
ATOM   4100 C  CA    . ALA B 1 45  ? -30.086 -2.448  8.757   1.00 52.01  ? 1262 ALA B CA    1 
ATOM   4101 C  C     . ALA B 1 45  ? -29.711 -1.380  7.721   1.00 52.06  ? 1262 ALA B C     1 
ATOM   4102 O  O     . ALA B 1 45  ? -29.438 -1.707  6.561   1.00 65.09  ? 1262 ALA B O     1 
ATOM   4103 C  CB    . ALA B 1 45  ? -31.592 -2.682  8.810   1.00 55.39  ? 1262 ALA B CB    1 
ATOM   4104 N  N     . ILE B 1 46  ? -29.705 -0.101  8.090   1.00 53.22  ? 1263 ILE B N     1 
ATOM   4105 C  CA    . ILE B 1 46  ? -29.249 0.901   7.115   1.00 71.76  ? 1263 ILE B CA    1 
ATOM   4106 C  C     . ILE B 1 46  ? -27.803 0.612   6.734   1.00 68.09  ? 1263 ILE B C     1 
ATOM   4107 O  O     . ILE B 1 46  ? -27.416 0.654   5.549   1.00 69.05  ? 1263 ILE B O     1 
ATOM   4108 C  CB    . ILE B 1 46  ? -29.438 2.351   7.630   1.00 71.10  ? 1263 ILE B CB    1 
ATOM   4109 C  CG1   . ILE B 1 46  ? -30.825 2.549   8.222   1.00 45.41  ? 1263 ILE B CG1   1 
ATOM   4110 C  CG2   . ILE B 1 46  ? -29.325 3.352   6.469   1.00 62.48  ? 1263 ILE B CG2   1 
ATOM   4111 C  CD1   . ILE B 1 46  ? -31.022 3.869   8.962   1.00 58.89  ? 1263 ILE B CD1   1 
ATOM   4112 N  N     . TRP B 1 47  ? -26.979 0.312   7.740   1.00 62.95  ? 1264 TRP B N     1 
ATOM   4113 C  CA    . TRP B 1 47  ? -25.606 -0.071  7.427   1.00 54.39  ? 1264 TRP B CA    1 
ATOM   4114 C  C     . TRP B 1 47  ? -25.549 -1.307  6.540   1.00 63.46  ? 1264 TRP B C     1 
ATOM   4115 O  O     . TRP B 1 47  ? -24.674 -1.416  5.679   1.00 69.97  ? 1264 TRP B O     1 
ATOM   4116 C  CB    . TRP B 1 47  ? -24.814 -0.334  8.698   1.00 58.28  ? 1264 TRP B CB    1 
ATOM   4117 C  CG    . TRP B 1 47  ? -23.341 -0.630  8.417   1.00 69.35  ? 1264 TRP B CG    1 
ATOM   4118 C  CD1   . TRP B 1 47  ? -22.626 -1.721  8.827   1.00 69.88  ? 1264 TRP B CD1   1 
ATOM   4119 C  CD2   . TRP B 1 47  ? -22.419 0.200   7.684   1.00 74.60  ? 1264 TRP B CD2   1 
ATOM   4120 N  NE1   . TRP B 1 47  ? -21.314 -1.618  8.403   1.00 73.44  ? 1264 TRP B NE1   1 
ATOM   4121 C  CE2   . TRP B 1 47  ? -21.164 -0.452  7.699   1.00 76.94  ? 1264 TRP B CE2   1 
ATOM   4122 C  CE3   . TRP B 1 47  ? -22.531 1.431   7.023   1.00 64.32  ? 1264 TRP B CE3   1 
ATOM   4123 C  CZ2   . TRP B 1 47  ? -20.041 0.079   7.068   1.00 73.23  ? 1264 TRP B CZ2   1 
ATOM   4124 C  CZ3   . TRP B 1 47  ? -21.415 1.952   6.397   1.00 68.03  ? 1264 TRP B CZ3   1 
ATOM   4125 C  CH2   . TRP B 1 47  ? -20.183 1.278   6.427   1.00 71.33  ? 1264 TRP B CH2   1 
ATOM   4126 N  N     . LYS B 1 48  ? -26.433 -2.276  6.781   1.00 59.43  ? 1265 LYS B N     1 
ATOM   4127 C  CA    . LYS B 1 48  ? -26.356 -3.538  6.058   1.00 61.58  ? 1265 LYS B CA    1 
ATOM   4128 C  C     . LYS B 1 48  ? -26.713 -3.327  4.593   1.00 67.59  ? 1265 LYS B C     1 
ATOM   4129 O  O     . LYS B 1 48  ? -26.125 -3.957  3.700   1.00 54.72  ? 1265 LYS B O     1 
ATOM   4130 C  CB    . LYS B 1 48  ? -27.241 -4.573  6.764   1.00 59.52  ? 1265 LYS B CB    1 
ATOM   4131 C  CG    . LYS B 1 48  ? -27.608 -5.818  5.972   1.00 70.31  ? 1265 LYS B CG    1 
ATOM   4132 C  CD    . LYS B 1 48  ? -28.265 -6.866  6.886   1.00 86.64  ? 1265 LYS B CD    1 
ATOM   4133 C  CE    . LYS B 1 48  ? -29.278 -7.757  6.156   1.00 109.90 ? 1265 LYS B CE    1 
ATOM   4134 N  NZ    . LYS B 1 48  ? -30.626 -7.762  6.824   1.00 123.60 ? 1265 LYS B NZ    1 
ATOM   4135 N  N     . ALA B 1 49  ? -27.649 -2.411  4.334   1.00 65.17  ? 1266 ALA B N     1 
ATOM   4136 C  CA    . ALA B 1 49  ? -28.009 -2.059  2.962   1.00 60.42  ? 1266 ALA B CA    1 
ATOM   4137 C  C     . ALA B 1 49  ? -26.840 -1.384  2.244   1.00 67.61  ? 1266 ALA B C     1 
ATOM   4138 O  O     . ALA B 1 49  ? -26.523 -1.724  1.090   1.00 69.96  ? 1266 ALA B O     1 
ATOM   4139 C  CB    . ALA B 1 49  ? -29.256 -1.172  2.980   1.00 62.63  ? 1266 ALA B CB    1 
ATOM   4140 N  N     . ILE B 1 50  ? -26.177 -0.430  2.917   1.00 63.96  ? 1267 ILE B N     1 
ATOM   4141 C  CA    . ILE B 1 50  ? -24.972 0.176   2.337   1.00 61.80  ? 1267 ILE B CA    1 
ATOM   4142 C  C     . ILE B 1 50  ? -23.887 -0.888  2.103   1.00 62.35  ? 1267 ILE B C     1 
ATOM   4143 O  O     . ILE B 1 50  ? -23.304 -0.983  1.013   1.00 62.35  ? 1267 ILE B O     1 
ATOM   4144 C  CB    . ILE B 1 50  ? -24.479 1.333   3.223   1.00 53.22  ? 1267 ILE B CB    1 
ATOM   4145 C  CG1   . ILE B 1 50  ? -25.587 2.379   3.374   1.00 48.95  ? 1267 ILE B CG1   1 
ATOM   4146 C  CG2   . ILE B 1 50  ? -23.266 1.994   2.613   1.00 60.83  ? 1267 ILE B CG2   1 
ATOM   4147 C  CD1   . ILE B 1 50  ? -25.304 3.451   4.446   1.00 45.95  ? 1267 ILE B CD1   1 
ATOM   4148 N  N     . ARG B 1 51  ? -23.614 -1.712  3.124   1.00 59.02  ? 1268 ARG B N     1 
ATOM   4149 C  CA    . ARG B 1 51  ? -22.605 -2.767  3.044   1.00 72.07  ? 1268 ARG B CA    1 
ATOM   4150 C  C     . ARG B 1 51  ? -22.842 -3.681  1.847   1.00 77.50  ? 1268 ARG B C     1 
ATOM   4151 O  O     . ARG B 1 51  ? -21.921 -3.957  1.068   1.00 80.99  ? 1268 ARG B O     1 
ATOM   4152 C  CB    . ARG B 1 51  ? -22.623 -3.584  4.343   1.00 71.61  ? 1268 ARG B CB    1 
ATOM   4153 C  CG    . ARG B 1 51  ? -21.735 -4.840  4.348   1.00 60.53  ? 1268 ARG B CG    1 
ATOM   4154 C  CD    . ARG B 1 51  ? -22.038 -5.716  5.542   1.00 67.35  ? 1268 ARG B CD    1 
ATOM   4155 N  NE    . ARG B 1 51  ? -23.089 -6.673  5.209   1.00 87.63  ? 1268 ARG B NE    1 
ATOM   4156 C  CZ    . ARG B 1 51  ? -23.801 -7.366  6.090   1.00 89.45  ? 1268 ARG B CZ    1 
ATOM   4157 N  NH1   . ARG B 1 51  ? -23.594 -7.230  7.395   1.00 87.05  ? 1268 ARG B NH1   1 
ATOM   4158 N  NH2   . ARG B 1 51  ? -24.725 -8.201  5.647   1.00 99.25  ? 1268 ARG B NH2   1 
ATOM   4159 N  N     . ASN B 1 52  ? -24.068 -4.196  1.712   1.00 68.86  ? 1269 ASN B N     1 
ATOM   4160 C  CA    . ASN B 1 52  ? -24.348 -5.136  0.637   1.00 67.96  ? 1269 ASN B CA    1 
ATOM   4161 C  C     . ASN B 1 52  ? -24.280 -4.463  -0.723  1.00 60.09  ? 1269 ASN B C     1 
ATOM   4162 O  O     . ASN B 1 52  ? -23.689 -5.020  -1.660  1.00 48.09  ? 1269 ASN B O     1 
ATOM   4163 C  CB    . ASN B 1 52  ? -25.693 -5.818  0.874   1.00 66.28  ? 1269 ASN B CB    1 
ATOM   4164 C  CG    . ASN B 1 52  ? -25.658 -6.744  2.083   1.00 63.46  ? 1269 ASN B CG    1 
ATOM   4165 O  OD1   . ASN B 1 52  ? -24.623 -6.888  2.752   1.00 74.15  ? 1269 ASN B OD1   1 
ATOM   4166 N  ND2   . ASN B 1 52  ? -26.778 -7.366  2.371   1.00 58.28  ? 1269 ASN B ND2   1 
ATOM   4167 N  N     . TRP B 1 53  ? -24.843 -3.252  -0.852  1.00 60.12  ? 1270 TRP B N     1 
ATOM   4168 C  CA    . TRP B 1 53  ? -24.796 -2.580  -2.146  1.00 51.60  ? 1270 TRP B CA    1 
ATOM   4169 C  C     . TRP B 1 53  ? -23.356 -2.392  -2.606  1.00 64.87  ? 1270 TRP B C     1 
ATOM   4170 O  O     . TRP B 1 53  ? -22.992 -2.734  -3.748  1.00 70.33  ? 1270 TRP B O     1 
ATOM   4171 C  CB    . TRP B 1 53  ? -25.520 -1.244  -2.063  1.00 63.94  ? 1270 TRP B CB    1 
ATOM   4172 C  CG    . TRP B 1 53  ? -25.582 -0.616  -3.402  1.00 74.65  ? 1270 TRP B CG    1 
ATOM   4173 C  CD1   . TRP B 1 53  ? -26.556 -0.793  -4.340  1.00 69.48  ? 1270 TRP B CD1   1 
ATOM   4174 C  CD2   . TRP B 1 53  ? -24.599 0.241   -3.996  1.00 69.60  ? 1270 TRP B CD2   1 
ATOM   4175 N  NE1   . TRP B 1 53  ? -26.250 -0.087  -5.476  1.00 67.61  ? 1270 TRP B NE1   1 
ATOM   4176 C  CE2   . TRP B 1 53  ? -25.053 0.557   -5.293  1.00 66.27  ? 1270 TRP B CE2   1 
ATOM   4177 C  CE3   . TRP B 1 53  ? -23.383 0.773   -3.557  1.00 73.08  ? 1270 TRP B CE3   1 
ATOM   4178 C  CZ2   . TRP B 1 53  ? -24.339 1.390   -6.154  1.00 63.06  ? 1270 TRP B CZ2   1 
ATOM   4179 C  CZ3   . TRP B 1 53  ? -22.672 1.599   -4.414  1.00 77.81  ? 1270 TRP B CZ3   1 
ATOM   4180 C  CH2   . TRP B 1 53  ? -23.157 1.903   -5.699  1.00 73.36  ? 1270 TRP B CH2   1 
ATOM   4181 N  N     . PHE B 1 54  ? -22.508 -1.875  -1.702  1.00 62.37  ? 1271 PHE B N     1 
ATOM   4182 C  CA    . PHE B 1 54  ? -21.129 -1.570  -2.056  1.00 67.38  ? 1271 PHE B CA    1 
ATOM   4183 C  C     . PHE B 1 54  ? -20.320 -2.834  -2.280  1.00 73.60  ? 1271 PHE B C     1 
ATOM   4184 O  O     . PHE B 1 54  ? -19.489 -2.892  -3.199  1.00 72.92  ? 1271 PHE B O     1 
ATOM   4185 C  CB    . PHE B 1 54  ? -20.484 -0.725  -0.956  1.00 73.13  ? 1271 PHE B CB    1 
ATOM   4186 C  CG    . PHE B 1 54  ? -19.099 -0.216  -1.296  1.00 68.26  ? 1271 PHE B CG    1 
ATOM   4187 C  CD1   . PHE B 1 54  ? -18.935 0.772   -2.251  1.00 58.41  ? 1271 PHE B CD1   1 
ATOM   4188 C  CD2   . PHE B 1 54  ? -17.973 -0.725  -0.655  1.00 69.25  ? 1271 PHE B CD2   1 
ATOM   4189 C  CE1   . PHE B 1 54  ? -17.690 1.254   -2.568  1.00 63.15  ? 1271 PHE B CE1   1 
ATOM   4190 C  CE2   . PHE B 1 54  ? -16.717 -0.255  -0.971  1.00 69.74  ? 1271 PHE B CE2   1 
ATOM   4191 C  CZ    . PHE B 1 54  ? -16.572 0.743   -1.928  1.00 72.54  ? 1271 PHE B CZ    1 
ATOM   4192 N  N     . ASP B 1 55  ? -20.531 -3.849  -1.440  1.00 78.57  ? 1272 ASP B N     1 
ATOM   4193 C  CA    . ASP B 1 55  ? -19.756 -5.065  -1.581  1.00 69.16  ? 1272 ASP B CA    1 
ATOM   4194 C  C     . ASP B 1 55  ? -20.049 -5.706  -2.915  1.00 65.88  ? 1272 ASP B C     1 
ATOM   4195 O  O     . ASP B 1 55  ? -19.136 -6.153  -3.610  1.00 68.86  ? 1272 ASP B O     1 
ATOM   4196 C  CB    . ASP B 1 55  ? -20.058 -6.010  -0.425  1.00 64.63  ? 1272 ASP B CB    1 
ATOM   4197 C  CG    . ASP B 1 55  ? -18.979 -7.052  -0.224  1.00 64.26  ? 1272 ASP B CG    1 
ATOM   4198 O  OD1   . ASP B 1 55  ? -18.054 -6.804  0.575   1.00 53.06  ? 1272 ASP B OD1   1 
ATOM   4199 O  OD2   . ASP B 1 55  ? -19.072 -8.126  -0.862  1.00 70.63  ? 1272 ASP B OD2   1 
ATOM   4200 N  N     . ALA B 1 56  ? -21.318 -5.733  -3.306  1.00 63.14  ? 1273 ALA B N     1 
ATOM   4201 C  CA    . ALA B 1 56  ? -21.645 -6.282  -4.614  1.00 64.42  ? 1273 ALA B CA    1 
ATOM   4202 C  C     . ALA B 1 56  ? -20.945 -5.500  -5.712  1.00 67.97  ? 1273 ALA B C     1 
ATOM   4203 O  O     . ALA B 1 56  ? -20.396 -6.088  -6.653  1.00 69.91  ? 1273 ALA B O     1 
ATOM   4204 C  CB    . ALA B 1 56  ? -23.158 -6.288  -4.826  1.00 57.29  ? 1273 ALA B CB    1 
ATOM   4205 N  N     . GLU B 1 57  ? -20.947 -4.169  -5.605  1.00 67.47  ? 1274 GLU B N     1 
ATOM   4206 C  CA    . GLU B 1 57  ? -20.269 -3.356  -6.610  1.00 73.77  ? 1274 GLU B CA    1 
ATOM   4207 C  C     . GLU B 1 57  ? -18.781 -3.705  -6.726  1.00 69.70  ? 1274 GLU B C     1 
ATOM   4208 O  O     . GLU B 1 57  ? -18.289 -4.062  -7.806  1.00 80.45  ? 1274 GLU B O     1 
ATOM   4209 C  CB    . GLU B 1 57  ? -20.456 -1.876  -6.271  1.00 78.82  ? 1274 GLU B CB    1 
ATOM   4210 C  CG    . GLU B 1 57  ? -21.883 -1.411  -6.459  1.00 87.22  ? 1274 GLU B CG    1 
ATOM   4211 C  CD    . GLU B 1 57  ? -22.383 -1.628  -7.875  1.00 96.08  ? 1274 GLU B CD    1 
ATOM   4212 O  OE1   . GLU B 1 57  ? -21.579 -1.492  -8.826  1.00 97.35  ? 1274 GLU B OE1   1 
ATOM   4213 O  OE2   . GLU B 1 57  ? -23.583 -1.927  -8.036  1.00 99.54  ? 1274 GLU B OE2   1 
ATOM   4214 N  N     . ILE B 1 58  ? -18.048 -3.628  -5.613  1.00 60.15  ? 1275 ILE B N     1 
ATOM   4215 C  CA    . ILE B 1 58  ? -16.598 -3.791  -5.700  1.00 64.53  ? 1275 ILE B CA    1 
ATOM   4216 C  C     . ILE B 1 58  ? -16.240 -5.236  -5.980  1.00 69.87  ? 1275 ILE B C     1 
ATOM   4217 O  O     . ILE B 1 58  ? -15.133 -5.530  -6.448  1.00 69.67  ? 1275 ILE B O     1 
ATOM   4218 C  CB    . ILE B 1 58  ? -15.881 -3.312  -4.425  1.00 55.00  ? 1275 ILE B CB    1 
ATOM   4219 C  CG1   . ILE B 1 58  ? -16.326 -4.148  -3.214  1.00 52.98  ? 1275 ILE B CG1   1 
ATOM   4220 C  CG2   . ILE B 1 58  ? -16.159 -1.848  -4.214  1.00 53.00  ? 1275 ILE B CG2   1 
ATOM   4221 C  CD1   . ILE B 1 58  ? -15.516 -3.891  -1.951  1.00 52.98  ? 1275 ILE B CD1   1 
ATOM   4222 N  N     . THR B 1 59  ? -17.162 -6.144  -5.696  1.00 64.49  ? 1276 THR B N     1 
ATOM   4223 C  CA    . THR B 1 59  ? -16.954 -7.537  -6.017  1.00 63.86  ? 1276 THR B CA    1 
ATOM   4224 C  C     . THR B 1 59  ? -17.093 -7.750  -7.510  1.00 66.91  ? 1276 THR B C     1 
ATOM   4225 O  O     . THR B 1 59  ? -16.280 -8.438  -8.133  1.00 72.21  ? 1276 THR B O     1 
ATOM   4226 C  CB    . THR B 1 59  ? -17.984 -8.353  -5.246  1.00 54.78  ? 1276 THR B CB    1 
ATOM   4227 O  OG1   . THR B 1 59  ? -17.639 -8.327  -3.855  1.00 65.78  ? 1276 THR B OG1   1 
ATOM   4228 C  CG2   . THR B 1 59  ? -18.067 -9.794  -5.776  1.00 56.13  ? 1276 THR B CG2   1 
ATOM   4229 N  N     . ARG B 1 60  ? -18.071 -7.094  -8.107  1.00 66.38  ? 1277 ARG B N     1 
ATOM   4230 C  CA    . ARG B 1 60  ? -18.193 -7.110  -9.549  1.00 70.86  ? 1277 ARG B CA    1 
ATOM   4231 C  C     . ARG B 1 60  ? -16.961 -6.521  -10.197 1.00 74.00  ? 1277 ARG B C     1 
ATOM   4232 O  O     . ARG B 1 60  ? -16.570 -6.956  -11.283 1.00 73.77  ? 1277 ARG B O     1 
ATOM   4233 C  CB    . ARG B 1 60  ? -19.459 -6.344  -9.942  1.00 82.89  ? 1277 ARG B CB    1 
ATOM   4234 C  CG    . ARG B 1 60  ? -19.674 -6.143  -11.426 1.00 92.25  ? 1277 ARG B CG    1 
ATOM   4235 C  CD    . ARG B 1 60  ? -20.793 -5.143  -11.684 1.00 90.11  ? 1277 ARG B CD    1 
ATOM   4236 N  NE    . ARG B 1 60  ? -20.518 -3.841  -11.073 1.00 103.76 ? 1277 ARG B NE    1 
ATOM   4237 C  CZ    . ARG B 1 60  ? -19.875 -2.834  -11.667 1.00 104.23 ? 1277 ARG B CZ    1 
ATOM   4238 N  NH1   . ARG B 1 60  ? -19.422 -2.961  -12.909 1.00 100.80 ? 1277 ARG B NH1   1 
ATOM   4239 N  NH2   . ARG B 1 60  ? -19.684 -1.694  -11.010 1.00 96.20  ? 1277 ARG B NH2   1 
ATOM   4240 N  N     . LEU B 1 61  ? -16.304 -5.574  -9.510  1.00 80.58  ? 1278 LEU B N     1 
ATOM   4241 C  CA    . LEU B 1 61  ? -15.110 -4.899  -10.037 1.00 79.97  ? 1278 LEU B CA    1 
ATOM   4242 C  C     . LEU B 1 61  ? -13.854 -5.762  -10.020 1.00 76.82  ? 1278 LEU B C     1 
ATOM   4243 O  O     . LEU B 1 61  ? -12.901 -5.445  -10.737 1.00 74.26  ? 1278 LEU B O     1 
ATOM   4244 C  CB    . LEU B 1 61  ? -14.833 -3.618  -9.246  1.00 79.07  ? 1278 LEU B CB    1 
ATOM   4245 C  CG    . LEU B 1 61  ? -15.771 -2.448  -9.562  1.00 77.23  ? 1278 LEU B CG    1 
ATOM   4246 C  CD1   . LEU B 1 61  ? -15.716 -1.415  -8.464  1.00 81.41  ? 1278 LEU B CD1   1 
ATOM   4247 C  CD2   . LEU B 1 61  ? -15.438 -1.832  -10.900 1.00 69.59  ? 1278 LEU B CD2   1 
ATOM   4248 N  N     . GLY B 1 62  ? -13.824 -6.825  -9.220  1.00 71.28  ? 1279 GLY B N     1 
ATOM   4249 C  CA    . GLY B 1 62  ? -12.660 -7.661  -9.059  1.00 43.22  ? 1279 GLY B CA    1 
ATOM   4250 C  C     . GLY B 1 62  ? -11.955 -7.562  -7.714  1.00 71.05  ? 1279 GLY B C     1 
ATOM   4251 O  O     . GLY B 1 62  ? -10.927 -8.226  -7.522  1.00 81.49  ? 1279 GLY B O     1 
ATOM   4252 N  N     . VAL B 1 63  ? -12.489 -6.809  -6.770  1.00 66.67  ? 1280 VAL B N     1 
ATOM   4253 C  CA    . VAL B 1 63  ? -11.948 -6.777  -5.416  1.00 57.39  ? 1280 VAL B CA    1 
ATOM   4254 C  C     . VAL B 1 63  ? -12.446 -7.986  -4.644  1.00 53.70  ? 1280 VAL B C     1 
ATOM   4255 O  O     . VAL B 1 63  ? -13.553 -8.491  -4.875  1.00 67.53  ? 1280 VAL B O     1 
ATOM   4256 C  CB    . VAL B 1 63  ? -12.340 -5.459  -4.718  1.00 56.32  ? 1280 VAL B CB    1 
ATOM   4257 C  CG1   . VAL B 1 63  ? -11.664 -5.335  -3.333  1.00 51.12  ? 1280 VAL B CG1   1 
ATOM   4258 C  CG2   . VAL B 1 63  ? -12.037 -4.288  -5.633  1.00 45.95  ? 1280 VAL B CG2   1 
ATOM   4259 N  N     . LYS B 1 64  ? -11.654 -8.427  -3.685  1.00 58.80  ? 1281 LYS B N     1 
ATOM   4260 C  CA    . LYS B 1 64  ? -11.975 -9.636  -2.951  1.00 65.58  ? 1281 LYS B CA    1 
ATOM   4261 C  C     . LYS B 1 64  ? -11.919 -9.375  -1.459  1.00 57.13  ? 1281 LYS B C     1 
ATOM   4262 O  O     . LYS B 1 64  ? -11.134 -8.556  -0.982  1.00 70.28  ? 1281 LYS B O     1 
ATOM   4263 C  CB    . LYS B 1 64  ? -11.031 -10.780 -3.334  1.00 72.46  ? 1281 LYS B CB    1 
ATOM   4264 C  CG    . LYS B 1 64  ? -11.427 -11.484 -4.620  1.00 74.83  ? 1281 LYS B CG    1 
ATOM   4265 C  CD    . LYS B 1 64  ? -10.193 -11.917 -5.359  1.00 91.57  ? 1281 LYS B CD    1 
ATOM   4266 C  CE    . LYS B 1 64  ? -10.515 -12.509 -6.711  1.00 96.81  ? 1281 LYS B CE    1 
ATOM   4267 N  NZ    . LYS B 1 64  ? -9.250  -12.529 -7.519  1.00 103.88 ? 1281 LYS B NZ    1 
ATOM   4268 N  N     . GLU B 1 65  ? -12.769 -10.085 -0.737  1.00 49.44  ? 1282 GLU B N     1 
ATOM   4269 C  CA    . GLU B 1 65  ? -12.950 -9.886  0.688   1.00 53.09  ? 1282 GLU B CA    1 
ATOM   4270 C  C     . GLU B 1 65  ? -12.042 -10.805 1.505   1.00 62.20  ? 1282 GLU B C     1 
ATOM   4271 O  O     . GLU B 1 65  ? -11.901 -11.994 1.198   1.00 69.50  ? 1282 GLU B O     1 
ATOM   4272 C  CB    . GLU B 1 65  ? -14.415 -10.100 1.047   1.00 41.87  ? 1282 GLU B CB    1 
ATOM   4273 C  CG    . GLU B 1 65  ? -14.737 -9.688  2.442   1.00 49.46  ? 1282 GLU B CG    1 
ATOM   4274 C  CD    . GLU B 1 65  ? -16.215 -9.676  2.660   1.00 56.90  ? 1282 GLU B CD    1 
ATOM   4275 O  OE1   . GLU B 1 65  ? -16.980 -9.906  1.668   1.00 58.75  ? 1282 GLU B OE1   1 
ATOM   4276 O  OE2   . GLU B 1 65  ? -16.593 -9.440  3.826   1.00 53.75  ? 1282 GLU B OE2   1 
ATOM   4277 N  N     . CYS B 1 66  ? -11.408 -10.239 2.529   1.00 65.25  ? 1283 CYS B N     1 
ATOM   4278 C  CA    . CYS B 1 66  ? -10.522 -10.960 3.434   1.00 71.06  ? 1283 CYS B CA    1 
ATOM   4279 C  C     . CYS B 1 66  ? -10.733 -10.424 4.846   1.00 70.34  ? 1283 CYS B C     1 
ATOM   4280 O  O     . CYS B 1 66  ? -11.524 -9.509  5.064   1.00 64.54  ? 1283 CYS B O     1 
ATOM   4281 C  CB    . CYS B 1 66  ? -9.064  -10.787 3.006   1.00 70.42  ? 1283 CYS B CB    1 
ATOM   4282 S  SG    . CYS B 1 66  ? -8.513  -9.055  3.157   1.00 69.93  ? 1283 CYS B SG    1 
ATOM   4283 N  N     . TYR B 1 67  ? -9.979  -10.950 5.811   1.00 65.61  ? 1284 TYR B N     1 
ATOM   4284 C  CA    . TYR B 1 67  ? -10.080 -10.423 7.167   1.00 62.26  ? 1284 TYR B CA    1 
ATOM   4285 C  C     . TYR B 1 67  ? -8.759  -10.618 7.894   1.00 75.64  ? 1284 TYR B C     1 
ATOM   4286 O  O     . TYR B 1 67  ? -8.386  -11.759 8.188   1.00 89.48  ? 1284 TYR B O     1 
ATOM   4287 C  CB    . TYR B 1 67  ? -11.203 -11.099 7.935   1.00 56.81  ? 1284 TYR B CB    1 
ATOM   4288 C  CG    . TYR B 1 67  ? -11.368 -10.506 9.306   1.00 57.81  ? 1284 TYR B CG    1 
ATOM   4289 C  CD1   . TYR B 1 67  ? -11.960 -9.261  9.466   1.00 55.98  ? 1284 TYR B CD1   1 
ATOM   4290 C  CD2   . TYR B 1 67  ? -10.907 -11.166 10.440  1.00 51.23  ? 1284 TYR B CD2   1 
ATOM   4291 C  CE1   . TYR B 1 67  ? -12.104 -8.686  10.719  1.00 64.19  ? 1284 TYR B CE1   1 
ATOM   4292 C  CE2   . TYR B 1 67  ? -11.047 -10.607 11.704  1.00 59.05  ? 1284 TYR B CE2   1 
ATOM   4293 C  CZ    . TYR B 1 67  ? -11.650 -9.355  11.840  1.00 66.17  ? 1284 TYR B CZ    1 
ATOM   4294 O  OH    . TYR B 1 67  ? -11.809 -8.761  13.089  1.00 65.73  ? 1284 TYR B OH    1 
ATOM   4295 N  N     . PHE B 1 68  ? -8.068  -9.480  8.238   1.00 61.18  ? 1285 PHE B N     1 
ATOM   4296 C  CA    . PHE B 1 68  ? -6.851  -9.441  9.046   1.00 49.17  ? 1285 PHE B CA    1 
ATOM   4297 C  C     . PHE B 1 68  ? -7.207  -9.199  10.513  1.00 46.95  ? 1285 PHE B C     1 
ATOM   4298 O  O     . PHE B 1 68  ? -8.325  -8.786  10.831  1.00 54.52  ? 1285 PHE B O     1 
ATOM   4299 C  CB    . PHE B 1 68  ? -5.921  -8.337  8.553   1.00 66.15  ? 1285 PHE B CB    1 
ATOM   4300 C  CG    . PHE B 1 68  ? -5.259  -8.609  7.223   1.00 75.87  ? 1285 PHE B CG    1 
ATOM   4301 C  CD1   . PHE B 1 68  ? -6.011  -8.731  6.055   1.00 73.96  ? 1285 PHE B CD1   1 
ATOM   4302 C  CD2   . PHE B 1 68  ? -3.861  -8.673  7.131   1.00 81.95  ? 1285 PHE B CD2   1 
ATOM   4303 C  CE1   . PHE B 1 68  ? -5.381  -8.938  4.817   1.00 73.11  ? 1285 PHE B CE1   1 
ATOM   4304 C  CE2   . PHE B 1 68  ? -3.220  -8.892  5.899   1.00 73.26  ? 1285 PHE B CE2   1 
ATOM   4305 C  CZ    . PHE B 1 68  ? -3.979  -9.017  4.745   1.00 70.90  ? 1285 PHE B CZ    1 
ATOM   4306 N  N     . PRO B 1 69  ? -6.303  -9.466  11.447  1.00 57.19  ? 1286 PRO B N     1 
ATOM   4307 C  CA    . PRO B 1 69  ? -6.695  -9.436  12.863  1.00 69.78  ? 1286 PRO B CA    1 
ATOM   4308 C  C     . PRO B 1 69  ? -7.059  -8.044  13.373  1.00 67.24  ? 1286 PRO B C     1 
ATOM   4309 O  O     . PRO B 1 69  ? -6.724  -7.007  12.799  1.00 71.95  ? 1286 PRO B O     1 
ATOM   4310 C  CB    . PRO B 1 69  ? -5.456  -9.983  13.590  1.00 71.21  ? 1286 PRO B CB    1 
ATOM   4311 C  CG    . PRO B 1 69  ? -4.762  -10.794 12.565  1.00 73.77  ? 1286 PRO B CG    1 
ATOM   4312 C  CD    . PRO B 1 69  ? -4.963  -10.047 11.278  1.00 70.21  ? 1286 PRO B CD    1 
ATOM   4313 N  N     . ILE B 1 70  ? -7.795  -8.052  14.483  1.00 66.31  ? 1287 ILE B N     1 
ATOM   4314 C  CA    . ILE B 1 70  ? -8.127  -6.833  15.193  1.00 68.05  ? 1287 ILE B CA    1 
ATOM   4315 C  C     . ILE B 1 70  ? -6.912  -6.288  15.920  1.00 69.92  ? 1287 ILE B C     1 
ATOM   4316 O  O     . ILE B 1 70  ? -6.927  -5.112  16.314  1.00 76.99  ? 1287 ILE B O     1 
ATOM   4317 C  CB    . ILE B 1 70  ? -9.265  -7.112  16.197  1.00 74.19  ? 1287 ILE B CB    1 
ATOM   4318 C  CG1   . ILE B 1 70  ? -9.847  -5.828  16.809  1.00 73.25  ? 1287 ILE B CG1   1 
ATOM   4319 C  CG2   . ILE B 1 70  ? -8.762  -8.034  17.320  1.00 71.73  ? 1287 ILE B CG2   1 
ATOM   4320 C  CD1   . ILE B 1 70  ? -10.952 -5.180  15.985  1.00 76.87  ? 1287 ILE B CD1   1 
ATOM   4321 N  N     . PHE B 1 71  ? -5.866  -7.111  16.120  1.00 59.54  ? 1288 PHE B N     1 
ATOM   4322 C  CA    . PHE B 1 71  ? -4.697  -6.744  16.920  1.00 65.60  ? 1288 PHE B CA    1 
ATOM   4323 C  C     . PHE B 1 71  ? -3.465  -6.483  16.063  1.00 74.41  ? 1288 PHE B C     1 
ATOM   4324 O  O     . PHE B 1 71  ? -3.206  -7.195  15.089  1.00 79.07  ? 1288 PHE B O     1 
ATOM   4325 C  CB    . PHE B 1 71  ? -4.350  -7.830  17.921  1.00 72.75  ? 1288 PHE B CB    1 
ATOM   4326 C  CG    . PHE B 1 71  ? -5.264  -7.880  19.089  1.00 81.48  ? 1288 PHE B CG    1 
ATOM   4327 C  CD1   . PHE B 1 71  ? -5.531  -6.736  19.822  1.00 85.51  ? 1288 PHE B CD1   1 
ATOM   4328 C  CD2   . PHE B 1 71  ? -5.830  -9.082  19.484  1.00 73.75  ? 1288 PHE B CD2   1 
ATOM   4329 C  CE1   . PHE B 1 71  ? -6.364  -6.783  20.924  1.00 85.88  ? 1288 PHE B CE1   1 
ATOM   4330 C  CE2   . PHE B 1 71  ? -6.659  -9.144  20.583  1.00 71.85  ? 1288 PHE B CE2   1 
ATOM   4331 C  CZ    . PHE B 1 71  ? -6.929  -7.991  21.308  1.00 83.24  ? 1288 PHE B CZ    1 
ATOM   4332 N  N     . VAL B 1 72  ? -2.675  -5.496  16.473  1.00 77.87  ? 1289 VAL B N     1 
ATOM   4333 C  CA    . VAL B 1 72  ? -1.414  -5.145  15.826  1.00 81.33  ? 1289 VAL B CA    1 
ATOM   4334 C  C     . VAL B 1 72  ? -0.360  -5.098  16.938  1.00 87.78  ? 1289 VAL B C     1 
ATOM   4335 O  O     . VAL B 1 72  ? -0.549  -4.371  17.911  1.00 86.04  ? 1289 VAL B O     1 
ATOM   4336 C  CB    . VAL B 1 72  ? -1.571  -3.787  15.112  1.00 62.60  ? 1289 VAL B CB    1 
ATOM   4337 C  CG1   . VAL B 1 72  ? -0.275  -3.285  14.513  1.00 67.61  ? 1289 VAL B CG1   1 
ATOM   4338 C  CG2   . VAL B 1 72  ? -2.610  -3.916  14.031  1.00 67.11  ? 1289 VAL B CG2   1 
ATOM   4339 N  N     . SER B 1 73  ? 0.749   -5.843  16.837  1.00 81.30  ? 1290 SER B N     1 
ATOM   4340 C  CA    . SER B 1 73  ? 1.515   -5.572  18.048  1.00 98.97  ? 1290 SER B CA    1 
ATOM   4341 C  C     . SER B 1 73  ? 2.447   -4.406  17.763  1.00 103.22 ? 1290 SER B C     1 
ATOM   4342 O  O     . SER B 1 73  ? 2.636   -3.994  16.608  1.00 92.86  ? 1290 SER B O     1 
ATOM   4343 C  CB    . SER B 1 73  ? 2.338   -6.732  18.645  1.00 104.74 ? 1290 SER B CB    1 
ATOM   4344 O  OG    . SER B 1 73  ? 3.640   -6.757  18.163  1.00 90.74  ? 1290 SER B OG    1 
ATOM   4345 N  N     . ARG B 1 74  ? 3.044   -3.885  18.848  1.00 103.55 ? 1291 ARG B N     1 
ATOM   4346 C  CA    . ARG B 1 74  ? 3.737   -2.603  18.806  1.00 99.01  ? 1291 ARG B CA    1 
ATOM   4347 C  C     . ARG B 1 74  ? 4.688   -2.477  17.633  1.00 96.61  ? 1291 ARG B C     1 
ATOM   4348 O  O     . ARG B 1 74  ? 4.775   -1.412  17.005  1.00 98.56  ? 1291 ARG B O     1 
ATOM   4349 C  CB    . ARG B 1 74  ? 4.498   -2.385  20.118  1.00 94.23  ? 1291 ARG B CB    1 
ATOM   4350 N  N     . ALA B 1 75  ? 5.397   -3.554  17.309  1.00 93.40  ? 1292 ALA B N     1 
ATOM   4351 C  CA    . ALA B 1 75  ? 6.410   -3.496  16.257  1.00 84.10  ? 1292 ALA B CA    1 
ATOM   4352 C  C     . ALA B 1 75  ? 5.783   -3.306  14.878  1.00 94.07  ? 1292 ALA B C     1 
ATOM   4353 O  O     . ALA B 1 75  ? 6.229   -2.465  14.089  1.00 98.56  ? 1292 ALA B O     1 
ATOM   4354 C  CB    . ALA B 1 75  ? 7.243   -4.772  16.286  1.00 65.33  ? 1292 ALA B CB    1 
ATOM   4355 N  N     . ALA B 1 76  ? 4.749   -4.084  14.566  1.00 103.74 ? 1293 ALA B N     1 
ATOM   4356 C  CA    . ALA B 1 76  ? 4.059   -3.902  13.297  1.00 106.91 ? 1293 ALA B CA    1 
ATOM   4357 C  C     . ALA B 1 76  ? 3.660   -2.452  13.115  1.00 97.22  ? 1293 ALA B C     1 
ATOM   4358 O  O     . ALA B 1 76  ? 3.821   -1.887  12.026  1.00 94.67  ? 1293 ALA B O     1 
ATOM   4359 C  CB    . ALA B 1 76  ? 2.827   -4.810  13.234  1.00 107.42 ? 1293 ALA B CB    1 
ATOM   4360 N  N     . LEU B 1 77  ? 3.202   -1.821  14.201  1.00 91.13  ? 1294 LEU B N     1 
ATOM   4361 C  CA    . LEU B 1 77  ? 2.659   -0.471  14.126  1.00 90.15  ? 1294 LEU B CA    1 
ATOM   4362 C  C     . LEU B 1 77  ? 3.750   0.569   13.902  1.00 97.20  ? 1294 LEU B C     1 
ATOM   4363 O  O     . LEU B 1 77  ? 3.770   1.254   12.871  1.00 91.77  ? 1294 LEU B O     1 
ATOM   4364 C  CB    . LEU B 1 77  ? 1.865   -0.158  15.398  1.00 81.77  ? 1294 LEU B CB    1 
ATOM   4365 C  CG    . LEU B 1 77  ? 0.802   0.949   15.272  1.00 76.36  ? 1294 LEU B CG    1 
ATOM   4366 C  CD1   . LEU B 1 77  ? -0.080  0.783   14.016  1.00 60.01  ? 1294 LEU B CD1   1 
ATOM   4367 C  CD2   . LEU B 1 77  ? -0.058  1.053   16.527  1.00 78.62  ? 1294 LEU B CD2   1 
ATOM   4368 N  N     . GLU B 1 78  ? 4.698   0.676   14.836  1.00 99.16  ? 1295 GLU B N     1 
ATOM   4369 C  CA    . GLU B 1 78  ? 5.618   1.816   14.851  1.00 100.86 ? 1295 GLU B CA    1 
ATOM   4370 C  C     . GLU B 1 78  ? 6.722   1.601   13.815  1.00 105.70 ? 1295 GLU B C     1 
ATOM   4371 O  O     . GLU B 1 78  ? 7.888   1.353   14.125  1.00 109.16 ? 1295 GLU B O     1 
ATOM   4372 C  CB    . GLU B 1 78  ? 6.176   2.024   16.254  1.00 106.83 ? 1295 GLU B CB    1 
ATOM   4373 C  CG    . GLU B 1 78  ? 5.123   1.884   17.368  1.00 113.28 ? 1295 GLU B CG    1 
ATOM   4374 C  CD    . GLU B 1 78  ? 5.514   2.561   18.682  1.00 122.05 ? 1295 GLU B CD    1 
ATOM   4375 O  OE1   . GLU B 1 78  ? 5.752   3.790   18.674  1.00 129.17 ? 1295 GLU B OE1   1 
ATOM   4376 O  OE2   . GLU B 1 78  ? 5.561   1.869   19.726  1.00 124.14 ? 1295 GLU B OE2   1 
ATOM   4377 N  N     . ARG B 1 79  ? 6.326   1.717   12.549  1.00 111.33 ? 1296 ARG B N     1 
ATOM   4378 C  CA    . ARG B 1 79  ? 7.252   1.568   11.427  1.00 114.51 ? 1296 ARG B CA    1 
ATOM   4379 C  C     . ARG B 1 79  ? 6.790   2.399   10.228  1.00 113.80 ? 1296 ARG B C     1 
ATOM   4380 O  O     . ARG B 1 79  ? 6.992   3.615   10.193  1.00 118.46 ? 1296 ARG B O     1 
ATOM   4381 C  CB    . ARG B 1 79  ? 7.390   0.088   11.037  1.00 112.15 ? 1296 ARG B CB    1 
ATOM   4382 N  N     . ASP B 1 86  ? 1.387   12.552  16.310  1.00 100.00 ? 1303 ASP B N     1 
ATOM   4383 C  CA    . ASP B 1 86  ? 1.183   12.042  14.957  1.00 102.60 ? 1303 ASP B CA    1 
ATOM   4384 C  C     . ASP B 1 86  ? 0.221   10.838  14.953  1.00 116.75 ? 1303 ASP B C     1 
ATOM   4385 O  O     . ASP B 1 86  ? 0.527   9.797   14.347  1.00 113.80 ? 1303 ASP B O     1 
ATOM   4386 C  CB    . ASP B 1 86  ? 2.531   11.664  14.321  1.00 97.37  ? 1303 ASP B CB    1 
ATOM   4387 N  N     . PHE B 1 87  ? -0.926  11.018  15.639  1.00 121.32 ? 1304 PHE B N     1 
ATOM   4388 C  CA    . PHE B 1 87  ? -2.033  10.069  15.838  1.00 107.86 ? 1304 PHE B CA    1 
ATOM   4389 C  C     . PHE B 1 87  ? -1.780  9.213   17.078  1.00 112.80 ? 1304 PHE B C     1 
ATOM   4390 O  O     . PHE B 1 87  ? -2.727  8.738   17.708  1.00 97.84  ? 1304 PHE B O     1 
ATOM   4391 C  CB    . PHE B 1 87  ? -2.283  9.154   14.625  1.00 86.33  ? 1304 PHE B CB    1 
ATOM   4392 C  CG    . PHE B 1 87  ? -3.187  9.745   13.552  1.00 86.58  ? 1304 PHE B CG    1 
ATOM   4393 C  CD1   . PHE B 1 87  ? -2.825  9.662   12.206  1.00 84.58  ? 1304 PHE B CD1   1 
ATOM   4394 C  CD2   . PHE B 1 87  ? -4.397  10.357  13.873  1.00 93.99  ? 1304 PHE B CD2   1 
ATOM   4395 C  CE1   . PHE B 1 87  ? -3.640  10.194  11.201  1.00 83.58  ? 1304 PHE B CE1   1 
ATOM   4396 C  CE2   . PHE B 1 87  ? -5.215  10.893  12.870  1.00 94.72  ? 1304 PHE B CE2   1 
ATOM   4397 C  CZ    . PHE B 1 87  ? -4.830  10.808  11.535  1.00 88.41  ? 1304 PHE B CZ    1 
ATOM   4398 N  N     . ALA B 1 88  ? -0.509  9.034   17.445  1.00 135.31 ? 1305 ALA B N     1 
ATOM   4399 C  CA    . ALA B 1 88  ? -0.137  8.090   18.501  1.00 140.91 ? 1305 ALA B CA    1 
ATOM   4400 C  C     . ALA B 1 88  ? -0.944  8.201   19.797  1.00 147.06 ? 1305 ALA B C     1 
ATOM   4401 O  O     . ALA B 1 88  ? -1.268  7.146   20.370  1.00 147.95 ? 1305 ALA B O     1 
ATOM   4402 C  CB    . ALA B 1 88  ? 1.366   8.235   18.791  1.00 139.08 ? 1305 ALA B CB    1 
ATOM   4403 N  N     . PRO B 1 89  ? -1.326  9.388   20.295  1.00 144.14 ? 1306 PRO B N     1 
ATOM   4404 C  CA    . PRO B 1 89  ? -2.141  9.417   21.525  1.00 138.93 ? 1306 PRO B CA    1 
ATOM   4405 C  C     . PRO B 1 89  ? -3.455  8.647   21.437  1.00 127.23 ? 1306 PRO B C     1 
ATOM   4406 O  O     . PRO B 1 89  ? -3.951  8.175   22.469  1.00 133.87 ? 1306 PRO B O     1 
ATOM   4407 C  CB    . PRO B 1 89  ? -2.387  10.922  21.755  1.00 139.25 ? 1306 PRO B CB    1 
ATOM   4408 C  CG    . PRO B 1 89  ? -1.869  11.630  20.529  1.00 139.87 ? 1306 PRO B CG    1 
ATOM   4409 C  CD    . PRO B 1 89  ? -0.814  10.733  19.974  1.00 142.81 ? 1306 PRO B CD    1 
ATOM   4410 N  N     . GLU B 1 90  ? -4.028  8.492   20.247  1.00 112.03 ? 1307 GLU B N     1 
ATOM   4411 C  CA    . GLU B 1 90  ? -5.371  7.934   20.071  1.00 102.24 ? 1307 GLU B CA    1 
ATOM   4412 C  C     . GLU B 1 90  ? -5.401  6.423   19.782  1.00 95.69  ? 1307 GLU B C     1 
ATOM   4413 O  O     . GLU B 1 90  ? -6.171  6.000   18.922  1.00 102.64 ? 1307 GLU B O     1 
ATOM   4414 C  CB    . GLU B 1 90  ? -6.087  8.715   18.970  1.00 97.69  ? 1307 GLU B CB    1 
ATOM   4415 N  N     . VAL B 1 91  ? -4.566  5.587   20.406  1.00 87.22  ? 1308 VAL B N     1 
ATOM   4416 C  CA    . VAL B 1 91  ? -4.493  4.161   20.093  1.00 81.22  ? 1308 VAL B CA    1 
ATOM   4417 C  C     . VAL B 1 91  ? -4.752  3.331   21.351  1.00 84.54  ? 1308 VAL B C     1 
ATOM   4418 O  O     . VAL B 1 91  ? -4.080  3.507   22.375  1.00 89.27  ? 1308 VAL B O     1 
ATOM   4419 C  CB    . VAL B 1 91  ? -3.142  3.793   19.453  1.00 88.10  ? 1308 VAL B CB    1 
ATOM   4420 C  CG1   . VAL B 1 91  ? -2.994  2.286   19.357  1.00 93.16  ? 1308 VAL B CG1   1 
ATOM   4421 C  CG2   . VAL B 1 91  ? -3.033  4.419   18.071  1.00 73.74  ? 1308 VAL B CG2   1 
ATOM   4422 N  N     . ALA B 1 92  ? -5.713  2.416   21.268  1.00 78.87  ? 1309 ALA B N     1 
ATOM   4423 C  CA    . ALA B 1 92  ? -6.056  1.560   22.399  1.00 87.62  ? 1309 ALA B CA    1 
ATOM   4424 C  C     . ALA B 1 92  ? -5.059  0.409   22.545  1.00 90.49  ? 1309 ALA B C     1 
ATOM   4425 O  O     . ALA B 1 92  ? -4.728  -0.267  21.566  1.00 78.22  ? 1309 ALA B O     1 
ATOM   4426 C  CB    . ALA B 1 92  ? -7.474  1.015   22.244  1.00 86.07  ? 1309 ALA B CB    1 
ATOM   4427 N  N     . TRP B 1 93  ? -4.539  0.220   23.757  1.00 96.34  ? 1310 TRP B N     1 
ATOM   4428 C  CA    . TRP B 1 93  ? -3.504  -0.772  24.022  1.00 96.69  ? 1310 TRP B CA    1 
ATOM   4429 C  C     . TRP B 1 93  ? -3.999  -1.824  25.006  1.00 93.81  ? 1310 TRP B C     1 
ATOM   4430 O  O     . TRP B 1 93  ? -4.300  -1.502  26.162  1.00 92.20  ? 1310 TRP B O     1 
ATOM   4431 C  CB    . TRP B 1 93  ? -2.246  -0.103  24.571  1.00 98.53  ? 1310 TRP B CB    1 
ATOM   4432 C  CG    . TRP B 1 93  ? -1.492  0.646   23.546  1.00 101.21 ? 1310 TRP B CG    1 
ATOM   4433 C  CD1   . TRP B 1 93  ? -1.499  1.997   23.333  1.00 103.25 ? 1310 TRP B CD1   1 
ATOM   4434 C  CD2   . TRP B 1 93  ? -0.611  0.090   22.577  1.00 104.78 ? 1310 TRP B CD2   1 
ATOM   4435 N  NE1   . TRP B 1 93  ? -0.671  2.315   22.283  1.00 101.35 ? 1310 TRP B NE1   1 
ATOM   4436 C  CE2   . TRP B 1 93  ? -0.111  1.160   21.803  1.00 101.64 ? 1310 TRP B CE2   1 
ATOM   4437 C  CE3   . TRP B 1 93  ? -0.191  -1.212  22.287  1.00 109.12 ? 1310 TRP B CE3   1 
ATOM   4438 C  CZ2   . TRP B 1 93  ? 0.785   0.965   20.757  1.00 103.15 ? 1310 TRP B CZ2   1 
ATOM   4439 C  CZ3   . TRP B 1 93  ? 0.699   -1.407  21.246  1.00 109.50 ? 1310 TRP B CZ3   1 
ATOM   4440 C  CH2   . TRP B 1 93  ? 1.180   -0.323  20.494  1.00 110.74 ? 1310 TRP B CH2   1 
ATOM   4441 N  N     . VAL B 1 94  ? -4.097  -3.073  24.543  1.00 90.45  ? 1311 VAL B N     1 
ATOM   4442 C  CA    . VAL B 1 94  ? -4.166  -4.223  25.442  1.00 87.62  ? 1311 VAL B CA    1 
ATOM   4443 C  C     . VAL B 1 94  ? -2.779  -4.480  26.016  1.00 86.37  ? 1311 VAL B C     1 
ATOM   4444 O  O     . VAL B 1 94  ? -1.794  -4.579  25.273  1.00 88.88  ? 1311 VAL B O     1 
ATOM   4445 C  CB    . VAL B 1 94  ? -4.707  -5.462  24.709  1.00 88.31  ? 1311 VAL B CB    1 
ATOM   4446 C  CG1   . VAL B 1 94  ? -4.840  -6.645  25.689  1.00 89.06  ? 1311 VAL B CG1   1 
ATOM   4447 C  CG2   . VAL B 1 94  ? -6.037  -5.153  24.039  1.00 85.44  ? 1311 VAL B CG2   1 
ATOM   4448 N  N     . THR B 1 95  ? -2.694  -4.626  27.343  1.00 86.08  ? 1312 THR B N     1 
ATOM   4449 C  CA    . THR B 1 95  ? -1.409  -4.934  27.955  1.00 97.88  ? 1312 THR B CA    1 
ATOM   4450 C  C     . THR B 1 95  ? -1.508  -5.936  29.098  1.00 112.68 ? 1312 THR B C     1 
ATOM   4451 O  O     . THR B 1 95  ? -0.495  -6.198  29.755  1.00 127.92 ? 1312 THR B O     1 
ATOM   4452 C  CB    . THR B 1 95  ? -0.727  -3.660  28.499  1.00 99.22  ? 1312 THR B CB    1 
ATOM   4453 O  OG1   . THR B 1 95  ? -1.368  -3.269  29.724  1.00 98.26  ? 1312 THR B OG1   1 
ATOM   4454 C  CG2   . THR B 1 95  ? -0.786  -2.494  27.520  1.00 96.39  ? 1312 THR B CG2   1 
ATOM   4455 N  N     . LYS B 1 96  ? -2.671  -6.526  29.341  1.00 106.77 ? 1313 LYS B N     1 
ATOM   4456 C  CA    . LYS B 1 96  ? -2.751  -7.575  30.339  1.00 102.47 ? 1313 LYS B CA    1 
ATOM   4457 C  C     . LYS B 1 96  ? -3.875  -8.517  29.953  1.00 96.09  ? 1313 LYS B C     1 
ATOM   4458 O  O     . LYS B 1 96  ? -4.924  -8.087  29.468  1.00 90.25  ? 1313 LYS B O     1 
ATOM   4459 C  CB    . LYS B 1 96  ? -2.953  -7.015  31.762  1.00 108.57 ? 1313 LYS B CB    1 
ATOM   4460 C  CG    . LYS B 1 96  ? -4.334  -6.438  32.067  1.00 114.04 ? 1313 LYS B CG    1 
ATOM   4461 C  CD    . LYS B 1 96  ? -4.611  -6.332  33.576  1.00 117.69 ? 1313 LYS B CD    1 
ATOM   4462 C  CE    . LYS B 1 96  ? -5.752  -5.339  33.870  1.00 121.75 ? 1313 LYS B CE    1 
ATOM   4463 N  NZ    . LYS B 1 96  ? -6.687  -5.743  34.985  1.00 121.47 ? 1313 LYS B NZ    1 
ATOM   4464 N  N     . SER B 1 97  ? -3.599  -9.808  30.083  1.00 93.14  ? 1314 SER B N     1 
ATOM   4465 C  CA    . SER B 1 97  ? -4.602  -10.861 30.015  1.00 87.03  ? 1314 SER B CA    1 
ATOM   4466 C  C     . SER B 1 97  ? -4.949  -11.240 31.453  1.00 92.72  ? 1314 SER B C     1 
ATOM   4467 O  O     . SER B 1 97  ? -4.090  -11.740 32.197  1.00 85.68  ? 1314 SER B O     1 
ATOM   4468 C  CB    . SER B 1 97  ? -4.101  -12.051 29.213  1.00 73.50  ? 1314 SER B CB    1 
ATOM   4469 O  OG    . SER B 1 97  ? -2.983  -12.623 29.844  1.00 71.81  ? 1314 SER B OG    1 
ATOM   4470 N  N     . GLY B 1 98  ? -6.193  -10.953 31.846  1.00 90.54  ? 1315 GLY B N     1 
ATOM   4471 C  CA    . GLY B 1 98  ? -6.691  -11.140 33.193  1.00 94.86  ? 1315 GLY B CA    1 
ATOM   4472 C  C     . GLY B 1 98  ? -5.990  -10.203 34.159  1.00 104.95 ? 1315 GLY B C     1 
ATOM   4473 O  O     . GLY B 1 98  ? -6.183  -8.984  34.106  1.00 110.66 ? 1315 GLY B O     1 
ATOM   4474 N  N     . ASP B 1 99  ? -5.160  -10.755 35.035  1.00 110.95 ? 1316 ASP B N     1 
ATOM   4475 C  CA    . ASP B 1 99  ? -4.293  -9.973  35.900  1.00 112.02 ? 1316 ASP B CA    1 
ATOM   4476 C  C     . ASP B 1 99  ? -2.828  -10.247 35.608  1.00 112.23 ? 1316 ASP B C     1 
ATOM   4477 O  O     . ASP B 1 99  ? -1.956  -9.648  36.257  1.00 114.99 ? 1316 ASP B O     1 
ATOM   4478 C  CB    . ASP B 1 99  ? -4.605  -10.253 37.374  1.00 115.92 ? 1316 ASP B CB    1 
ATOM   4479 C  CG    . ASP B 1 99  ? -5.956  -9.715  37.791  1.00 122.34 ? 1316 ASP B CG    1 
ATOM   4480 O  OD1   . ASP B 1 99  ? -6.499  -8.821  37.095  1.00 123.47 ? 1316 ASP B OD1   1 
ATOM   4481 O  OD2   . ASP B 1 99  ? -6.476  -10.190 38.816  1.00 127.72 ? 1316 ASP B OD2   1 
ATOM   4482 N  N     . SER B 1 100 ? -2.551  -11.148 34.652  1.00 115.10 ? 1317 SER B N     1 
ATOM   4483 C  CA    . SER B 1 100 ? -1.210  -11.492 34.200  1.00 120.83 ? 1317 SER B CA    1 
ATOM   4484 C  C     . SER B 1 100 ? -0.791  -10.495 33.123  1.00 123.75 ? 1317 SER B C     1 
ATOM   4485 O  O     . SER B 1 100 ? -1.442  -10.399 32.078  1.00 130.56 ? 1317 SER B O     1 
ATOM   4486 C  CB    . SER B 1 100 ? -1.215  -12.927 33.665  1.00 124.83 ? 1317 SER B CB    1 
ATOM   4487 O  OG    . SER B 1 100 ? 0.037   -13.365 33.141  1.00 133.22 ? 1317 SER B OG    1 
ATOM   4488 N  N     . GLU B 1 101 ? 0.299   -9.763  33.372  1.00 119.14 ? 1318 GLU B N     1 
ATOM   4489 C  CA    . GLU B 1 101 ? 0.791   -8.768  32.419  1.00 113.90 ? 1318 GLU B CA    1 
ATOM   4490 C  C     . GLU B 1 101 ? 1.469   -9.442  31.235  1.00 115.64 ? 1318 GLU B C     1 
ATOM   4491 O  O     . GLU B 1 101 ? 2.134   -10.473 31.387  1.00 122.49 ? 1318 GLU B O     1 
ATOM   4492 C  CB    . GLU B 1 101 ? 1.771   -7.814  33.095  1.00 114.41 ? 1318 GLU B CB    1 
ATOM   4493 C  CG    . GLU B 1 101 ? 1.912   -6.460  32.417  1.00 123.76 ? 1318 GLU B CG    1 
ATOM   4494 C  CD    . GLU B 1 101 ? 0.936   -5.443  32.960  1.00 137.90 ? 1318 GLU B CD    1 
ATOM   4495 O  OE1   . GLU B 1 101 ? 0.577   -5.536  34.154  1.00 144.42 ? 1318 GLU B OE1   1 
ATOM   4496 O  OE2   . GLU B 1 101 ? 0.515   -4.559  32.185  1.00 142.52 ? 1318 GLU B OE2   1 
ATOM   4497 N  N     . LEU B 1 102 ? 1.265   -8.882  30.049  1.00 112.20 ? 1319 LEU B N     1 
ATOM   4498 C  CA    . LEU B 1 102 ? 1.799   -9.469  28.831  1.00 115.99 ? 1319 LEU B CA    1 
ATOM   4499 C  C     . LEU B 1 102 ? 3.101   -8.794  28.436  1.00 118.95 ? 1319 LEU B C     1 
ATOM   4500 O  O     . LEU B 1 102 ? 3.333   -7.621  28.745  1.00 119.42 ? 1319 LEU B O     1 
ATOM   4501 C  CB    . LEU B 1 102 ? 0.790   -9.375  27.689  1.00 110.87 ? 1319 LEU B CB    1 
ATOM   4502 C  CG    . LEU B 1 102 ? -0.153  -10.578 27.652  1.00 109.76 ? 1319 LEU B CG    1 
ATOM   4503 C  CD1   . LEU B 1 102 ? -0.705  -10.709 26.269  1.00 105.43 ? 1319 LEU B CD1   1 
ATOM   4504 C  CD2   . LEU B 1 102 ? 0.554   -11.876 28.088  1.00 114.13 ? 1319 LEU B CD2   1 
ATOM   4505 N  N     . ALA B 1 103 ? 3.937   -9.553  27.722  1.00 119.54 ? 1320 ALA B N     1 
ATOM   4506 C  CA    . ALA B 1 103 ? 5.302   -9.117  27.441  1.00 122.75 ? 1320 ALA B CA    1 
ATOM   4507 C  C     . ALA B 1 103 ? 5.323   -7.868  26.566  1.00 116.98 ? 1320 ALA B C     1 
ATOM   4508 O  O     . ALA B 1 103 ? 5.756   -6.795  26.997  1.00 117.72 ? 1320 ALA B O     1 
ATOM   4509 C  CB    . ALA B 1 103 ? 6.083   -10.254 26.779  1.00 124.36 ? 1320 ALA B CB    1 
ATOM   4510 N  N     . GLU B 1 104 ? 4.844   -7.986  25.343  1.00 108.55 ? 1321 GLU B N     1 
ATOM   4511 C  CA    . GLU B 1 104 ? 4.735   -6.790  24.541  1.00 102.05 ? 1321 GLU B CA    1 
ATOM   4512 C  C     . GLU B 1 104 ? 3.269   -6.405  24.389  1.00 97.30  ? 1321 GLU B C     1 
ATOM   4513 O  O     . GLU B 1 104 ? 2.420   -7.280  24.186  1.00 91.31  ? 1321 GLU B O     1 
ATOM   4514 C  CB    . GLU B 1 104 ? 5.362   -6.984  23.155  1.00 95.99  ? 1321 GLU B CB    1 
ATOM   4515 N  N     . PRO B 1 105 ? 2.949   -5.118  24.471  1.00 94.77  ? 1322 PRO B N     1 
ATOM   4516 C  CA    . PRO B 1 105 ? 1.555   -4.693  24.340  1.00 94.16  ? 1322 PRO B CA    1 
ATOM   4517 C  C     . PRO B 1 105 ? 1.132   -4.608  22.886  1.00 95.04  ? 1322 PRO B C     1 
ATOM   4518 O  O     . PRO B 1 105 ? 1.930   -4.326  21.988  1.00 100.27 ? 1322 PRO B O     1 
ATOM   4519 C  CB    . PRO B 1 105 ? 1.541   -3.300  24.983  1.00 95.59  ? 1322 PRO B CB    1 
ATOM   4520 C  CG    . PRO B 1 105 ? 2.945   -3.071  25.526  1.00 90.04  ? 1322 PRO B CG    1 
ATOM   4521 C  CD    . PRO B 1 105 ? 3.844   -3.998  24.793  1.00 88.17  ? 1322 PRO B CD    1 
ATOM   4522 N  N     . ILE B 1 106 ? -0.146  -4.888  22.666  1.00 90.00  ? 1323 ILE B N     1 
ATOM   4523 C  CA    . ILE B 1 106 ? -0.719  -4.905  21.330  1.00 87.81  ? 1323 ILE B CA    1 
ATOM   4524 C  C     . ILE B 1 106 ? -1.814  -3.854  21.253  1.00 90.17  ? 1323 ILE B C     1 
ATOM   4525 O  O     . ILE B 1 106 ? -2.541  -3.591  22.219  1.00 91.88  ? 1323 ILE B O     1 
ATOM   4526 C  CB    . ILE B 1 106 ? -1.264  -6.294  20.928  1.00 91.84  ? 1323 ILE B CB    1 
ATOM   4527 C  CG1   . ILE B 1 106 ? -2.347  -6.765  21.897  1.00 99.80  ? 1323 ILE B CG1   1 
ATOM   4528 C  CG2   . ILE B 1 106 ? -0.148  -7.321  20.892  1.00 97.35  ? 1323 ILE B CG2   1 
ATOM   4529 C  CD1   . ILE B 1 106 ? -2.761  -8.237  21.702  1.00 99.05  ? 1323 ILE B CD1   1 
ATOM   4530 N  N     . ALA B 1 107 ? -1.931  -3.266  20.072  1.00 83.82  ? 1324 ALA B N     1 
ATOM   4531 C  CA    . ALA B 1 107 ? -2.820  -2.156  19.799  1.00 82.48  ? 1324 ALA B CA    1 
ATOM   4532 C  C     . ALA B 1 107 ? -4.069  -2.667  19.099  1.00 90.00  ? 1324 ALA B C     1 
ATOM   4533 O  O     . ALA B 1 107 ? -3.990  -3.560  18.246  1.00 95.36  ? 1324 ALA B O     1 
ATOM   4534 C  CB    . ALA B 1 107 ? -2.127  -1.122  18.911  1.00 62.63  ? 1324 ALA B CB    1 
ATOM   4535 N  N     . VAL B 1 108 ? -5.220  -2.091  19.457  1.00 78.68  ? 1325 VAL B N     1 
ATOM   4536 C  CA    . VAL B 1 108 ? -6.442  -2.360  18.717  1.00 68.66  ? 1325 VAL B CA    1 
ATOM   4537 C  C     . VAL B 1 108 ? -6.422  -1.523  17.450  1.00 68.68  ? 1325 VAL B C     1 
ATOM   4538 O  O     . VAL B 1 108 ? -6.231  -0.305  17.499  1.00 72.26  ? 1325 VAL B O     1 
ATOM   4539 C  CB    . VAL B 1 108 ? -7.685  -2.072  19.570  1.00 73.24  ? 1325 VAL B CB    1 
ATOM   4540 C  CG1   . VAL B 1 108 ? -8.923  -2.615  18.864  1.00 72.10  ? 1325 VAL B CG1   1 
ATOM   4541 C  CG2   . VAL B 1 108 ? -7.556  -2.716  20.946  1.00 72.74  ? 1325 VAL B CG2   1 
ATOM   4542 N  N     . ARG B 1 109 ? -6.631  -2.176  16.318  1.00 70.95  ? 1326 ARG B N     1 
ATOM   4543 C  CA    . ARG B 1 109 ? -6.361  -1.557  15.032  1.00 73.26  ? 1326 ARG B CA    1 
ATOM   4544 C  C     . ARG B 1 109 ? -7.203  -0.300  14.841  1.00 77.19  ? 1326 ARG B C     1 
ATOM   4545 O  O     . ARG B 1 109 ? -8.407  -0.306  15.147  1.00 77.00  ? 1326 ARG B O     1 
ATOM   4546 C  CB    . ARG B 1 109 ? -6.629  -2.542  13.895  1.00 69.57  ? 1326 ARG B CB    1 
ATOM   4547 C  CG    . ARG B 1 109 ? -8.021  -3.119  13.900  1.00 62.49  ? 1326 ARG B CG    1 
ATOM   4548 C  CD    . ARG B 1 109 ? -8.529  -3.427  12.508  1.00 64.68  ? 1326 ARG B CD    1 
ATOM   4549 N  NE    . ARG B 1 109 ? -9.799  -4.121  12.657  1.00 78.10  ? 1326 ARG B NE    1 
ATOM   4550 C  CZ    . ARG B 1 109 ? -9.993  -5.421  12.448  1.00 79.21  ? 1326 ARG B CZ    1 
ATOM   4551 N  NH1   . ARG B 1 109 ? -8.996  -6.199  12.037  1.00 87.87  ? 1326 ARG B NH1   1 
ATOM   4552 N  NH2   . ARG B 1 109 ? -11.193 -5.934  12.647  1.00 65.35  ? 1326 ARG B NH2   1 
ATOM   4553 N  N     . PRO B 1 110 ? -6.605  0.795   14.378  1.00 73.52  ? 1327 PRO B N     1 
ATOM   4554 C  CA    . PRO B 1 110 ? -7.370  1.993   14.003  1.00 73.43  ? 1327 PRO B CA    1 
ATOM   4555 C  C     . PRO B 1 110 ? -7.546  2.134   12.500  1.00 75.60  ? 1327 PRO B C     1 
ATOM   4556 O  O     . PRO B 1 110 ? -8.238  3.039   12.023  1.00 73.63  ? 1327 PRO B O     1 
ATOM   4557 C  CB    . PRO B 1 110 ? -6.518  3.116   14.574  1.00 62.88  ? 1327 PRO B CB    1 
ATOM   4558 C  CG    . PRO B 1 110 ? -5.103  2.571   14.502  1.00 61.50  ? 1327 PRO B CG    1 
ATOM   4559 C  CD    . PRO B 1 110 ? -5.166  1.066   14.442  1.00 68.80  ? 1327 PRO B CD    1 
ATOM   4560 N  N     . THR B 1 111 ? -6.867  1.252   11.766  1.00 68.97  ? 1328 THR B N     1 
ATOM   4561 C  CA    . THR B 1 111 ? -6.815  1.177   10.309  1.00 72.01  ? 1328 THR B CA    1 
ATOM   4562 C  C     . THR B 1 111 ? -5.779  0.087   10.059  1.00 74.27  ? 1328 THR B C     1 
ATOM   4563 O  O     . THR B 1 111 ? -4.995  -0.205  10.971  1.00 66.87  ? 1328 THR B O     1 
ATOM   4564 C  CB    . THR B 1 111 ? -6.442  2.525   9.675   1.00 67.81  ? 1328 THR B CB    1 
ATOM   4565 O  OG1   . THR B 1 111 ? -6.160  2.376   8.276   1.00 74.55  ? 1328 THR B OG1   1 
ATOM   4566 C  CG2   . THR B 1 111 ? -5.229  3.125   10.377  1.00 54.69  ? 1328 THR B CG2   1 
ATOM   4567 N  N     . SER B 1 112 ? -5.730  -0.515  8.856   1.00 72.31  ? 1329 SER B N     1 
ATOM   4568 C  CA    . SER B 1 112 ? -4.976  -1.759  8.697   1.00 80.95  ? 1329 SER B CA    1 
ATOM   4569 C  C     . SER B 1 112 ? -3.769  -1.666  7.756   1.00 82.74  ? 1329 SER B C     1 
ATOM   4570 O  O     . SER B 1 112 ? -3.294  -2.690  7.260   1.00 92.07  ? 1329 SER B O     1 
ATOM   4571 C  CB    . SER B 1 112 ? -5.910  -2.882  8.211   1.00 77.59  ? 1329 SER B CB    1 
ATOM   4572 O  OG    . SER B 1 112 ? -6.967  -3.145  9.126   1.00 80.97  ? 1329 SER B OG    1 
ATOM   4573 N  N     . GLU B 1 113 ? -3.195  -0.482  7.559   1.00 79.13  ? 1330 GLU B N     1 
ATOM   4574 C  CA    . GLU B 1 113 ? -2.042  -0.381  6.655   1.00 81.75  ? 1330 GLU B CA    1 
ATOM   4575 C  C     . GLU B 1 113 ? -0.829  -1.143  7.198   1.00 83.41  ? 1330 GLU B C     1 
ATOM   4576 O  O     . GLU B 1 113 ? -0.213  -1.960  6.487   1.00 84.69  ? 1330 GLU B O     1 
ATOM   4577 C  CB    . GLU B 1 113 ? -1.709  1.084   6.385   1.00 67.18  ? 1330 GLU B CB    1 
ATOM   4578 C  CG    . GLU B 1 113 ? -2.447  1.641   5.155   1.00 71.29  ? 1330 GLU B CG    1 
ATOM   4579 C  CD    . GLU B 1 113 ? -3.674  2.496   5.481   1.00 75.78  ? 1330 GLU B CD    1 
ATOM   4580 O  OE1   . GLU B 1 113 ? -4.245  2.360   6.591   1.00 68.56  ? 1330 GLU B OE1   1 
ATOM   4581 O  OE2   . GLU B 1 113 ? -4.067  3.301   4.604   1.00 81.14  ? 1330 GLU B OE2   1 
ATOM   4582 N  N     . THR B 1 114 ? -0.498  -0.906  8.471   1.00 73.05  ? 1331 THR B N     1 
ATOM   4583 C  CA    . THR B 1 114 ? 0.672   -1.477  9.128   1.00 66.98  ? 1331 THR B CA    1 
ATOM   4584 C  C     . THR B 1 114 ? 0.618   -3.000  9.248   1.00 84.16  ? 1331 THR B C     1 
ATOM   4585 O  O     . THR B 1 114 ? 1.630   -3.617  9.599   1.00 107.52 ? 1331 THR B O     1 
ATOM   4586 C  CB    . THR B 1 114 ? 0.801   -0.850  10.523  1.00 65.68  ? 1331 THR B CB    1 
ATOM   4587 O  OG1   . THR B 1 114 ? -0.503  -0.657  11.078  1.00 70.89  ? 1331 THR B OG1   1 
ATOM   4588 C  CG2   . THR B 1 114 ? 1.428   0.502   10.425  1.00 52.63  ? 1331 THR B CG2   1 
ATOM   4589 N  N     . VAL B 1 115 ? -0.523  -3.625  8.982   1.00 80.71  ? 1332 VAL B N     1 
ATOM   4590 C  CA    . VAL B 1 115 ? -0.647  -5.068  9.024   1.00 85.08  ? 1332 VAL B CA    1 
ATOM   4591 C  C     . VAL B 1 115 ? -0.756  -5.667  7.629   1.00 87.65  ? 1332 VAL B C     1 
ATOM   4592 O  O     . VAL B 1 115 ? -0.079  -6.647  7.322   1.00 102.20 ? 1332 VAL B O     1 
ATOM   4593 C  CB    . VAL B 1 115 ? -1.849  -5.487  9.891   1.00 87.04  ? 1332 VAL B CB    1 
ATOM   4594 C  CG1   . VAL B 1 115 ? -3.124  -5.014  9.273   1.00 79.82  ? 1332 VAL B CG1   1 
ATOM   4595 C  CG2   . VAL B 1 115 ? -1.907  -6.969  9.987   1.00 96.37  ? 1332 VAL B CG2   1 
ATOM   4596 N  N     . MET B 1 116 ? -1.576  -5.090  6.764   1.00 78.87  ? 1333 MET B N     1 
ATOM   4597 C  CA    . MET B 1 116 ? -1.741  -5.715  5.464   1.00 79.10  ? 1333 MET B CA    1 
ATOM   4598 C  C     . MET B 1 116 ? -0.601  -5.391  4.518   1.00 79.89  ? 1333 MET B C     1 
ATOM   4599 O  O     . MET B 1 116 ? -0.429  -6.092  3.517   1.00 83.55  ? 1333 MET B O     1 
ATOM   4600 C  CB    . MET B 1 116 ? -3.052  -5.295  4.802   1.00 76.18  ? 1333 MET B CB    1 
ATOM   4601 C  CG    . MET B 1 116 ? -4.262  -5.353  5.695   1.00 70.70  ? 1333 MET B CG    1 
ATOM   4602 S  SD    . MET B 1 116 ? -5.631  -4.494  4.891   1.00 82.23  ? 1333 MET B SD    1 
ATOM   4603 C  CE    . MET B 1 116 ? -5.645  -5.286  3.277   1.00 78.81  ? 1333 MET B CE    1 
ATOM   4604 N  N     . TYR B 1 117 ? 0.195   -4.386  4.804   1.00 76.63  ? 1334 TYR B N     1 
ATOM   4605 C  CA    . TYR B 1 117 ? 1.194   -4.118  3.775   1.00 76.82  ? 1334 TYR B CA    1 
ATOM   4606 C  C     . TYR B 1 117 ? 2.407   -5.050  3.865   1.00 71.70  ? 1334 TYR B C     1 
ATOM   4607 O  O     . TYR B 1 117 ? 2.932   -5.452  2.814   1.00 65.99  ? 1334 TYR B O     1 
ATOM   4608 C  CB    . TYR B 1 117 ? 1.565   -2.633  3.808   1.00 71.56  ? 1334 TYR B CB    1 
ATOM   4609 C  CG    . TYR B 1 117 ? 0.426   -1.806  3.232   1.00 78.46  ? 1334 TYR B CG    1 
ATOM   4610 C  CD1   . TYR B 1 117 ? -0.681  -2.435  2.669   1.00 85.57  ? 1334 TYR B CD1   1 
ATOM   4611 C  CD2   . TYR B 1 117 ? 0.440   -0.423  3.248   1.00 72.27  ? 1334 TYR B CD2   1 
ATOM   4612 C  CE1   . TYR B 1 117 ? -1.730  -1.719  2.148   1.00 80.25  ? 1334 TYR B CE1   1 
ATOM   4613 C  CE2   . TYR B 1 117 ? -0.620  0.307   2.715   1.00 71.88  ? 1334 TYR B CE2   1 
ATOM   4614 C  CZ    . TYR B 1 117 ? -1.704  -0.353  2.166   1.00 76.14  ? 1334 TYR B CZ    1 
ATOM   4615 O  OH    . TYR B 1 117 ? -2.781  0.338   1.633   1.00 77.62  ? 1334 TYR B OH    1 
ATOM   4616 N  N     . PRO B 1 118 ? 2.873   -5.440  5.065   1.00 67.83  ? 1335 PRO B N     1 
ATOM   4617 C  CA    . PRO B 1 118 ? 3.864   -6.526  5.129   1.00 74.75  ? 1335 PRO B CA    1 
ATOM   4618 C  C     . PRO B 1 118 ? 3.407   -7.795  4.425   1.00 82.41  ? 1335 PRO B C     1 
ATOM   4619 O  O     . PRO B 1 118 ? 4.193   -8.464  3.732   1.00 85.97  ? 1335 PRO B O     1 
ATOM   4620 C  CB    . PRO B 1 118 ? 4.014   -6.764  6.636   1.00 72.90  ? 1335 PRO B CB    1 
ATOM   4621 C  CG    . PRO B 1 118 ? 3.510   -5.537  7.291   1.00 67.51  ? 1335 PRO B CG    1 
ATOM   4622 C  CD    . PRO B 1 118 ? 2.564   -4.895  6.402   1.00 63.76  ? 1335 PRO B CD    1 
ATOM   4623 N  N     . ALA B 1 119 ? 2.134   -8.141  4.588   1.00 76.39  ? 1336 ALA B N     1 
ATOM   4624 C  CA    . ALA B 1 119 ? 1.594   -9.278  3.862   1.00 75.11  ? 1336 ALA B CA    1 
ATOM   4625 C  C     . ALA B 1 119 ? 1.669   -9.052  2.357   1.00 77.96  ? 1336 ALA B C     1 
ATOM   4626 O  O     . ALA B 1 119 ? 1.967   -9.983  1.597   1.00 79.50  ? 1336 ALA B O     1 
ATOM   4627 C  CB    . ALA B 1 119 ? 0.158   -9.539  4.298   1.00 74.39  ? 1336 ALA B CB    1 
ATOM   4628 N  N     . TYR B 1 120 ? 1.391   -7.823  1.900   1.00 71.60  ? 1337 TYR B N     1 
ATOM   4629 C  CA    . TYR B 1 120 ? 1.472   -7.571  0.467   1.00 83.82  ? 1337 TYR B CA    1 
ATOM   4630 C  C     . TYR B 1 120 ? 2.900   -7.757  -0.043  1.00 90.61  ? 1337 TYR B C     1 
ATOM   4631 O  O     . TYR B 1 120 ? 3.109   -8.281  -1.144  1.00 92.15  ? 1337 TYR B O     1 
ATOM   4632 C  CB    . TYR B 1 120 ? 0.957   -6.168  0.143   1.00 93.83  ? 1337 TYR B CB    1 
ATOM   4633 C  CG    . TYR B 1 120 ? -0.566  -6.005  0.123   1.00 91.96  ? 1337 TYR B CG    1 
ATOM   4634 C  CD1   . TYR B 1 120 ? -1.401  -6.915  0.757   1.00 89.03  ? 1337 TYR B CD1   1 
ATOM   4635 C  CD2   . TYR B 1 120 ? -1.160  -4.922  -0.527  1.00 86.76  ? 1337 TYR B CD2   1 
ATOM   4636 C  CE1   . TYR B 1 120 ? -2.776  -6.756  0.742   1.00 85.65  ? 1337 TYR B CE1   1 
ATOM   4637 C  CE2   . TYR B 1 120 ? -2.528  -4.762  -0.553  1.00 75.66  ? 1337 TYR B CE2   1 
ATOM   4638 C  CZ    . TYR B 1 120 ? -3.328  -5.678  0.085   1.00 80.92  ? 1337 TYR B CZ    1 
ATOM   4639 O  OH    . TYR B 1 120 ? -4.690  -5.516  0.073   1.00 83.93  ? 1337 TYR B OH    1 
ATOM   4640 N  N     . ALA B 1 121 ? 3.898   -7.351  0.750   1.00 94.58  ? 1338 ALA B N     1 
ATOM   4641 C  CA    . ALA B 1 121 ? 5.288   -7.558  0.343   1.00 94.49  ? 1338 ALA B CA    1 
ATOM   4642 C  C     . ALA B 1 121 ? 5.630   -9.040  0.285   1.00 89.39  ? 1338 ALA B C     1 
ATOM   4643 O  O     . ALA B 1 121 ? 6.339   -9.489  -0.625  1.00 93.15  ? 1338 ALA B O     1 
ATOM   4644 C  CB    . ALA B 1 121 ? 6.233   -6.842  1.300   1.00 104.86 ? 1338 ALA B CB    1 
ATOM   4645 N  N     . LYS B 1 122 ? 5.108   -9.818  1.234   1.00 82.75  ? 1339 LYS B N     1 
ATOM   4646 C  CA    . LYS B 1 122 ? 5.391   -11.251 1.256   1.00 82.32  ? 1339 LYS B CA    1 
ATOM   4647 C  C     . LYS B 1 122 ? 4.710   -11.969 0.094   1.00 86.60  ? 1339 LYS B C     1 
ATOM   4648 O  O     . LYS B 1 122 ? 5.262   -12.925 -0.467  1.00 78.37  ? 1339 LYS B O     1 
ATOM   4649 C  CB    . LYS B 1 122 ? 4.941   -11.836 2.595   1.00 72.25  ? 1339 LYS B CB    1 
ATOM   4650 C  CG    . LYS B 1 122 ? 5.235   -13.294 2.798   1.00 84.86  ? 1339 LYS B CG    1 
ATOM   4651 C  CD    . LYS B 1 122 ? 4.827   -13.733 4.197   1.00 94.58  ? 1339 LYS B CD    1 
ATOM   4652 C  CE    . LYS B 1 122 ? 5.111   -12.647 5.231   1.00 94.42  ? 1339 LYS B CE    1 
ATOM   4653 N  NZ    . LYS B 1 122 ? 4.243   -12.800 6.445   1.00 93.09  ? 1339 LYS B NZ    1 
ATOM   4654 N  N     . TRP B 1 123 ? 3.512   -11.521 -0.287  1.00 91.79  ? 1340 TRP B N     1 
ATOM   4655 C  CA    . TRP B 1 123 ? 2.744   -12.196 -1.324  1.00 83.36  ? 1340 TRP B CA    1 
ATOM   4656 C  C     . TRP B 1 123 ? 3.093   -11.754 -2.738  1.00 80.97  ? 1340 TRP B C     1 
ATOM   4657 O  O     . TRP B 1 123 ? 2.659   -12.412 -3.686  1.00 75.91  ? 1340 TRP B O     1 
ATOM   4658 C  CB    . TRP B 1 123 ? 1.258   -11.987 -1.114  1.00 86.36  ? 1340 TRP B CB    1 
ATOM   4659 C  CG    . TRP B 1 123 ? 0.696   -12.623 0.112   1.00 87.32  ? 1340 TRP B CG    1 
ATOM   4660 C  CD1   . TRP B 1 123 ? 1.185   -13.703 0.803   1.00 85.97  ? 1340 TRP B CD1   1 
ATOM   4661 C  CD2   . TRP B 1 123 ? -0.474  -12.198 0.806   1.00 76.50  ? 1340 TRP B CD2   1 
ATOM   4662 N  NE1   . TRP B 1 123 ? 0.380   -13.963 1.890   1.00 80.56  ? 1340 TRP B NE1   1 
ATOM   4663 C  CE2   . TRP B 1 123 ? -0.640  -13.047 1.913   1.00 75.56  ? 1340 TRP B CE2   1 
ATOM   4664 C  CE3   . TRP B 1 123 ? -1.387  -11.156 0.611   1.00 74.71  ? 1340 TRP B CE3   1 
ATOM   4665 C  CZ2   . TRP B 1 123 ? -1.686  -12.887 2.814   1.00 82.12  ? 1340 TRP B CZ2   1 
ATOM   4666 C  CZ3   . TRP B 1 123 ? -2.421  -11.007 1.502   1.00 68.18  ? 1340 TRP B CZ3   1 
ATOM   4667 C  CH2   . TRP B 1 123 ? -2.567  -11.864 2.586   1.00 75.79  ? 1340 TRP B CH2   1 
ATOM   4668 N  N     . ILE B 1 124 ? 3.841   -10.673 -2.919  1.00 89.43  ? 1341 ILE B N     1 
ATOM   4669 C  CA    . ILE B 1 124 ? 4.207   -10.205 -4.255  1.00 94.60  ? 1341 ILE B CA    1 
ATOM   4670 C  C     . ILE B 1 124 ? 5.671   -10.577 -4.455  1.00 94.24  ? 1341 ILE B C     1 
ATOM   4671 O  O     . ILE B 1 124 ? 6.584   -9.786  -4.198  1.00 98.17  ? 1341 ILE B O     1 
ATOM   4672 C  CB    . ILE B 1 124 ? 3.947   -8.711  -4.415  1.00 101.01 ? 1341 ILE B CB    1 
ATOM   4673 C  CG1   . ILE B 1 124 ? 2.467   -8.443  -4.198  1.00 92.51  ? 1341 ILE B CG1   1 
ATOM   4674 C  CG2   . ILE B 1 124 ? 4.333   -8.224  -5.806  1.00 108.06 ? 1341 ILE B CG2   1 
ATOM   4675 C  CD1   . ILE B 1 124 ? 2.178   -7.057  -3.934  1.00 88.26  ? 1341 ILE B CD1   1 
ATOM   4676 N  N     . GLN B 1 125 ? 5.887   -11.800 -4.957  1.00 90.20  ? 1342 GLN B N     1 
ATOM   4677 C  CA    . GLN B 1 125 ? 7.209   -12.315 -5.253  1.00 85.09  ? 1342 GLN B CA    1 
ATOM   4678 C  C     . GLN B 1 125 ? 7.574   -12.174 -6.722  1.00 89.47  ? 1342 GLN B C     1 
ATOM   4679 O  O     . GLN B 1 125 ? 8.728   -12.432 -7.081  1.00 104.58 ? 1342 GLN B O     1 
ATOM   4680 C  CB    . GLN B 1 125 ? 7.331   -13.787 -4.821  1.00 75.69  ? 1342 GLN B CB    1 
ATOM   4681 N  N     . SER B 1 126 ? 6.628   -11.794 -7.577  1.00 67.98  ? 1343 SER B N     1 
ATOM   4682 C  CA    . SER B 1 126 ? 6.921   -11.574 -8.987  1.00 72.87  ? 1343 SER B CA    1 
ATOM   4683 C  C     . SER B 1 126 ? 5.898   -10.603 -9.541  1.00 81.73  ? 1343 SER B C     1 
ATOM   4684 O  O     . SER B 1 126 ? 4.880   -10.330 -8.909  1.00 81.91  ? 1343 SER B O     1 
ATOM   4685 C  CB    . SER B 1 126 ? 6.908   -12.872 -9.801  1.00 76.15  ? 1343 SER B CB    1 
ATOM   4686 O  OG    . SER B 1 126 ? 5.590   -13.332 -10.048 1.00 77.63  ? 1343 SER B OG    1 
ATOM   4687 N  N     . TYR B 1 127 ? 6.175   -10.087 -10.744 1.00 92.86  ? 1344 TYR B N     1 
ATOM   4688 C  CA    . TYR B 1 127 ? 5.178   -9.292  -11.459 1.00 90.52  ? 1344 TYR B CA    1 
ATOM   4689 C  C     . TYR B 1 127 ? 3.883   -10.070 -11.650 1.00 82.12  ? 1344 TYR B C     1 
ATOM   4690 O  O     . TYR B 1 127 ? 2.802   -9.470  -11.716 1.00 71.17  ? 1344 TYR B O     1 
ATOM   4691 C  CB    . TYR B 1 127 ? 5.717   -8.867  -12.824 1.00 95.31  ? 1344 TYR B CB    1 
ATOM   4692 C  CG    . TYR B 1 127 ? 5.733   -9.996  -13.840 1.00 103.53 ? 1344 TYR B CG    1 
ATOM   4693 C  CD1   . TYR B 1 127 ? 4.665   -10.199 -14.714 1.00 102.29 ? 1344 TYR B CD1   1 
ATOM   4694 C  CD2   . TYR B 1 127 ? 6.816   -10.870 -13.917 1.00 112.43 ? 1344 TYR B CD2   1 
ATOM   4695 C  CE1   . TYR B 1 127 ? 4.677   -11.232 -15.637 1.00 106.57 ? 1344 TYR B CE1   1 
ATOM   4696 C  CE2   . TYR B 1 127 ? 6.838   -11.905 -14.840 1.00 117.34 ? 1344 TYR B CE2   1 
ATOM   4697 C  CZ    . TYR B 1 127 ? 5.768   -12.078 -15.698 1.00 120.53 ? 1344 TYR B CZ    1 
ATOM   4698 O  OH    . TYR B 1 127 ? 5.793   -13.108 -16.610 1.00 131.61 ? 1344 TYR B OH    1 
ATOM   4699 N  N     . ARG B 1 128 ? 3.987   -11.408 -11.748 1.00 82.61  ? 1345 ARG B N     1 
ATOM   4700 C  CA    . ARG B 1 128 ? 2.841   -12.273 -12.013 1.00 75.80  ? 1345 ARG B CA    1 
ATOM   4701 C  C     . ARG B 1 128 ? 1.760   -12.114 -10.944 1.00 77.95  ? 1345 ARG B C     1 
ATOM   4702 O  O     . ARG B 1 128 ? 0.572   -12.336 -11.217 1.00 74.46  ? 1345 ARG B O     1 
ATOM   4703 C  CB    . ARG B 1 128 ? 3.312   -13.728 -12.105 1.00 65.13  ? 1345 ARG B CB    1 
ATOM   4704 C  CG    . ARG B 1 128 ? 4.419   -13.975 -13.144 1.00 72.31  ? 1345 ARG B CG    1 
ATOM   4705 C  CD    . ARG B 1 128 ? 4.679   -15.487 -13.423 1.00 80.63  ? 1345 ARG B CD    1 
ATOM   4706 N  NE    . ARG B 1 128 ? 5.729   -16.045 -12.568 1.00 95.38  ? 1345 ARG B NE    1 
ATOM   4707 C  CZ    . ARG B 1 128 ? 7.035   -15.798 -12.722 1.00 103.89 ? 1345 ARG B CZ    1 
ATOM   4708 N  NH1   . ARG B 1 128 ? 7.460   -15.004 -13.708 1.00 104.63 ? 1345 ARG B NH1   1 
ATOM   4709 N  NH2   . ARG B 1 128 ? 7.922   -16.343 -11.889 1.00 96.27  ? 1345 ARG B NH2   1 
ATOM   4710 N  N     . ASP B 1 129 ? 2.153   -11.690 -9.746  1.00 76.54  ? 1346 ASP B N     1 
ATOM   4711 C  CA    . ASP B 1 129 ? 1.298   -11.518 -8.583  1.00 70.89  ? 1346 ASP B CA    1 
ATOM   4712 C  C     . ASP B 1 129 ? 0.503   -10.202 -8.578  1.00 71.89  ? 1346 ASP B C     1 
ATOM   4713 O  O     . ASP B 1 129 ? -0.064  -9.868  -7.531  1.00 73.10  ? 1346 ASP B O     1 
ATOM   4714 C  CB    . ASP B 1 129 ? 2.129   -11.588 -7.293  1.00 72.47  ? 1346 ASP B CB    1 
ATOM   4715 C  CG    . ASP B 1 129 ? 2.846   -12.904 -7.120  1.00 83.56  ? 1346 ASP B CG    1 
ATOM   4716 O  OD1   . ASP B 1 129 ? 2.174   -13.955 -7.205  1.00 93.68  ? 1346 ASP B OD1   1 
ATOM   4717 O  OD2   . ASP B 1 129 ? 4.083   -12.884 -6.880  1.00 88.81  ? 1346 ASP B OD2   1 
ATOM   4718 N  N     . LEU B 1 130 ? 0.487   -9.393  -9.664  1.00 79.17  ? 1347 LEU B N     1 
ATOM   4719 C  CA    . LEU B 1 130 ? -0.323  -8.166  -9.526  1.00 74.70  ? 1347 LEU B CA    1 
ATOM   4720 C  C     . LEU B 1 130 ? -1.518  -8.152  -10.481 1.00 76.90  ? 1347 LEU B C     1 
ATOM   4721 O  O     . LEU B 1 130 ? -1.478  -8.753  -11.557 1.00 76.59  ? 1347 LEU B O     1 
ATOM   4722 C  CB    . LEU B 1 130 ? 0.515   -6.903  -9.758  1.00 64.83  ? 1347 LEU B CB    1 
ATOM   4723 C  CG    . LEU B 1 130 ? 1.612   -6.712  -8.738  1.00 63.26  ? 1347 LEU B CG    1 
ATOM   4724 C  CD1   . LEU B 1 130 ? 2.514   -5.641  -9.294  1.00 70.18  ? 1347 LEU B CD1   1 
ATOM   4725 C  CD2   . LEU B 1 130 ? 1.046   -6.325  -7.377  1.00 54.76  ? 1347 LEU B CD2   1 
ATOM   4726 N  N     . PRO B 1 131 ? -2.613  -7.473  -10.088 1.00 79.76  ? 1348 PRO B N     1 
ATOM   4727 C  CA    . PRO B 1 131 ? -2.791  -6.634  -8.892  1.00 73.18  ? 1348 PRO B CA    1 
ATOM   4728 C  C     . PRO B 1 131 ? -3.245  -7.380  -7.629  1.00 79.08  ? 1348 PRO B C     1 
ATOM   4729 O  O     . PRO B 1 131 ? -3.649  -8.550  -7.705  1.00 91.38  ? 1348 PRO B O     1 
ATOM   4730 C  CB    . PRO B 1 131 ? -3.879  -5.658  -9.333  1.00 68.92  ? 1348 PRO B CB    1 
ATOM   4731 C  CG    . PRO B 1 131 ? -4.721  -6.454  -10.242 1.00 66.47  ? 1348 PRO B CG    1 
ATOM   4732 C  CD    . PRO B 1 131 ? -3.818  -7.446  -10.939 1.00 75.77  ? 1348 PRO B CD    1 
ATOM   4733 N  N     . ILE B 1 132 ? -3.158  -6.716  -6.479  1.00 66.59  ? 1349 ILE B N     1 
ATOM   4734 C  CA    . ILE B 1 132 ? -3.797  -7.159  -5.254  1.00 62.00  ? 1349 ILE B CA    1 
ATOM   4735 C  C     . ILE B 1 132 ? -4.945  -6.210  -4.988  1.00 70.51  ? 1349 ILE B C     1 
ATOM   4736 O  O     . ILE B 1 132 ? -4.740  -5.011  -4.817  1.00 78.82  ? 1349 ILE B O     1 
ATOM   4737 C  CB    . ILE B 1 132 ? -2.872  -7.171  -4.048  1.00 63.70  ? 1349 ILE B CB    1 
ATOM   4738 C  CG1   . ILE B 1 132 ? -1.640  -8.024  -4.320  1.00 81.64  ? 1349 ILE B CG1   1 
ATOM   4739 C  CG2   . ILE B 1 132 ? -3.667  -7.646  -2.825  1.00 56.23  ? 1349 ILE B CG2   1 
ATOM   4740 C  CD1   . ILE B 1 132 ? -1.737  -9.420  -3.819  1.00 91.38  ? 1349 ILE B CD1   1 
ATOM   4741 N  N     . ARG B 1 133 ? -6.167  -6.740  -4.951  1.00 83.76  ? 1350 ARG B N     1 
ATOM   4742 C  CA    . ARG B 1 133 ? -7.363  -5.930  -4.753  1.00 79.02  ? 1350 ARG B CA    1 
ATOM   4743 C  C     . ARG B 1 133 ? -8.159  -6.554  -3.609  1.00 72.83  ? 1350 ARG B C     1 
ATOM   4744 O  O     . ARG B 1 133 ? -8.914  -7.514  -3.828  1.00 73.97  ? 1350 ARG B O     1 
ATOM   4745 C  CB    . ARG B 1 133 ? -8.133  -5.866  -6.072  1.00 74.66  ? 1350 ARG B CB    1 
ATOM   4746 C  CG    . ARG B 1 133 ? -7.162  -5.930  -7.262  1.00 80.75  ? 1350 ARG B CG    1 
ATOM   4747 C  CD    . ARG B 1 133 ? -7.696  -5.325  -8.533  1.00 83.40  ? 1350 ARG B CD    1 
ATOM   4748 N  NE    . ARG B 1 133 ? -8.321  -4.031  -8.297  1.00 87.67  ? 1350 ARG B NE    1 
ATOM   4749 C  CZ    . ARG B 1 133 ? -9.567  -3.747  -8.662  1.00 86.01  ? 1350 ARG B CZ    1 
ATOM   4750 N  NH1   . ARG B 1 133 ? -10.297 -4.672  -9.269  1.00 96.29  ? 1350 ARG B NH1   1 
ATOM   4751 N  NH2   . ARG B 1 133 ? -10.088 -2.554  -8.425  1.00 76.91  ? 1350 ARG B NH2   1 
ATOM   4752 N  N     . LEU B 1 134 ? -7.953  -6.063  -2.374  1.00 57.39  ? 1351 LEU B N     1 
ATOM   4753 C  CA    . LEU B 1 134 ? -8.559  -6.739  -1.237  1.00 67.16  ? 1351 LEU B CA    1 
ATOM   4754 C  C     . LEU B 1 134 ? -9.348  -5.761  -0.384  1.00 66.03  ? 1351 LEU B C     1 
ATOM   4755 O  O     . LEU B 1 134 ? -8.897  -4.646  -0.145  1.00 51.37  ? 1351 LEU B O     1 
ATOM   4756 C  CB    . LEU B 1 134 ? -7.507  -7.462  -0.374  1.00 68.95  ? 1351 LEU B CB    1 
ATOM   4757 C  CG    . LEU B 1 134 ? -6.672  -8.554  -1.064  1.00 72.41  ? 1351 LEU B CG    1 
ATOM   4758 C  CD1   . LEU B 1 134 ? -5.783  -9.244  -0.047  1.00 57.22  ? 1351 LEU B CD1   1 
ATOM   4759 C  CD2   . LEU B 1 134 ? -7.545  -9.559  -1.818  1.00 78.45  ? 1351 LEU B CD2   1 
ATOM   4760 N  N     . ASN B 1 135 ? -10.510 -6.195  0.121   1.00 62.89  ? 1352 ASN B N     1 
ATOM   4761 C  CA    . ASN B 1 135 ? -11.359 -5.340  0.933   1.00 60.13  ? 1352 ASN B CA    1 
ATOM   4762 C  C     . ASN B 1 135 ? -11.663 -6.031  2.258   1.00 68.53  ? 1352 ASN B C     1 
ATOM   4763 O  O     . ASN B 1 135 ? -11.711 -7.265  2.336   1.00 68.26  ? 1352 ASN B O     1 
ATOM   4764 C  CB    . ASN B 1 135 ? -12.648 -4.987  0.215   1.00 56.28  ? 1352 ASN B CB    1 
ATOM   4765 C  CG    . ASN B 1 135 ? -13.662 -4.373  1.148   1.00 65.61  ? 1352 ASN B CG    1 
ATOM   4766 O  OD1   . ASN B 1 135 ? -13.315 -3.524  1.950   1.00 66.88  ? 1352 ASN B OD1   1 
ATOM   4767 N  ND2   . ASN B 1 135 ? -14.908 -4.825  1.078   1.00 76.36  ? 1352 ASN B ND2   1 
ATOM   4768 N  N     . GLN B 1 136 ? -11.788 -5.225  3.317   1.00 68.52  ? 1353 GLN B N     1 
ATOM   4769 C  CA    . GLN B 1 136 ? -12.225 -5.690  4.626   1.00 58.12  ? 1353 GLN B CA    1 
ATOM   4770 C  C     . GLN B 1 136 ? -13.440 -4.908  5.089   1.00 62.70  ? 1353 GLN B C     1 
ATOM   4771 O  O     . GLN B 1 136 ? -13.496 -3.684  4.954   1.00 76.14  ? 1353 GLN B O     1 
ATOM   4772 C  CB    . GLN B 1 136 ? -11.158 -5.505  5.679   1.00 40.32  ? 1353 GLN B CB    1 
ATOM   4773 C  CG    . GLN B 1 136 ? -10.121 -6.562  5.763   1.00 48.20  ? 1353 GLN B CG    1 
ATOM   4774 C  CD    . GLN B 1 136 ? -9.265  -6.393  7.002   1.00 59.99  ? 1353 GLN B CD    1 
ATOM   4775 O  OE1   . GLN B 1 136 ? -9.573  -6.935  8.064   1.00 77.26  ? 1353 GLN B OE1   1 
ATOM   4776 N  NE2   . GLN B 1 136 ? -8.195  -5.618  6.878   1.00 60.46  ? 1353 GLN B NE2   1 
ATOM   4777 N  N     . TRP B 1 137 ? -14.406 -5.626  5.621   1.00 56.10  ? 1354 TRP B N     1 
ATOM   4778 C  CA    . TRP B 1 137 ? -15.503 -5.068  6.390   1.00 43.53  ? 1354 TRP B CA    1 
ATOM   4779 C  C     . TRP B 1 137 ? -15.168 -5.316  7.852   1.00 51.78  ? 1354 TRP B C     1 
ATOM   4780 O  O     . TRP B 1 137 ? -15.312 -6.430  8.346   1.00 64.79  ? 1354 TRP B O     1 
ATOM   4781 C  CB    . TRP B 1 137 ? -16.818 -5.723  5.993   1.00 47.46  ? 1354 TRP B CB    1 
ATOM   4782 C  CG    . TRP B 1 137 ? -17.245 -5.387  4.601   1.00 54.67  ? 1354 TRP B CG    1 
ATOM   4783 C  CD1   . TRP B 1 137 ? -17.068 -6.146  3.478   1.00 63.24  ? 1354 TRP B CD1   1 
ATOM   4784 C  CD2   . TRP B 1 137 ? -17.918 -4.204  4.185   1.00 42.69  ? 1354 TRP B CD2   1 
ATOM   4785 N  NE1   . TRP B 1 137 ? -17.586 -5.502  2.383   1.00 62.00  ? 1354 TRP B NE1   1 
ATOM   4786 C  CE2   . TRP B 1 137 ? -18.107 -4.301  2.785   1.00 60.29  ? 1354 TRP B CE2   1 
ATOM   4787 C  CE3   . TRP B 1 137 ? -18.369 -3.063  4.851   1.00 46.60  ? 1354 TRP B CE3   1 
ATOM   4788 C  CZ2   . TRP B 1 137 ? -18.746 -3.302  2.038   1.00 59.69  ? 1354 TRP B CZ2   1 
ATOM   4789 C  CZ3   . TRP B 1 137 ? -18.995 -2.048  4.097   1.00 48.07  ? 1354 TRP B CZ3   1 
ATOM   4790 C  CH2   . TRP B 1 137 ? -19.168 -2.184  2.705   1.00 49.44  ? 1354 TRP B CH2   1 
ATOM   4791 N  N     . ASN B 1 138 ? -14.721 -4.296  8.567   1.00 62.10  ? 1355 ASN B N     1 
ATOM   4792 C  CA    . ASN B 1 138 ? -14.312 -4.590  9.932   1.00 69.31  ? 1355 ASN B CA    1 
ATOM   4793 C  C     . ASN B 1 138 ? -14.558 -3.394  10.830  1.00 67.58  ? 1355 ASN B C     1 
ATOM   4794 O  O     . ASN B 1 138 ? -14.990 -2.318  10.390  1.00 58.63  ? 1355 ASN B O     1 
ATOM   4795 C  CB    . ASN B 1 138 ? -12.841 -5.021  10.016  1.00 69.36  ? 1355 ASN B CB    1 
ATOM   4796 C  CG    . ASN B 1 138 ? -11.884 -3.969  9.485   1.00 84.05  ? 1355 ASN B CG    1 
ATOM   4797 O  OD1   . ASN B 1 138 ? -12.032 -2.773  9.737   1.00 84.19  ? 1355 ASN B OD1   1 
ATOM   4798 N  ND2   . ASN B 1 138 ? -10.896 -4.417  8.732   1.00 100.26 ? 1355 ASN B ND2   1 
ATOM   4799 N  N     . ASN B 1 139 ? -14.233 -3.607  12.102  1.00 54.44  ? 1356 ASN B N     1 
ATOM   4800 C  CA    . ASN B 1 139 ? -14.375 -2.614  13.139  1.00 56.50  ? 1356 ASN B CA    1 
ATOM   4801 C  C     . ASN B 1 139 ? -12.998 -2.077  13.482  1.00 62.71  ? 1356 ASN B C     1 
ATOM   4802 O  O     . ASN B 1 139 ? -12.048 -2.842  13.644  1.00 70.58  ? 1356 ASN B O     1 
ATOM   4803 C  CB    . ASN B 1 139 ? -15.032 -3.221  14.384  1.00 51.65  ? 1356 ASN B CB    1 
ATOM   4804 C  CG    . ASN B 1 139 ? -14.269 -4.395  14.939  1.00 64.34  ? 1356 ASN B CG    1 
ATOM   4805 O  OD1   . ASN B 1 139 ? -13.604 -5.116  14.196  1.00 78.58  ? 1356 ASN B OD1   1 
ATOM   4806 N  ND2   . ASN B 1 139 ? -14.362 -4.604  16.255  1.00 63.49  ? 1356 ASN B ND2   1 
ATOM   4807 N  N     . VAL B 1 140 ? -12.889 -0.759  13.617  1.00 66.81  ? 1357 VAL B N     1 
ATOM   4808 C  CA    . VAL B 1 140 ? -11.646 -0.202  14.132  1.00 68.64  ? 1357 VAL B CA    1 
ATOM   4809 C  C     . VAL B 1 140 ? -11.996 0.741   15.267  1.00 63.54  ? 1357 VAL B C     1 
ATOM   4810 O  O     . VAL B 1 140 ? -13.135 1.212   15.388  1.00 61.17  ? 1357 VAL B O     1 
ATOM   4811 C  CB    . VAL B 1 140 ? -10.818 0.513   13.045  1.00 74.32  ? 1357 VAL B CB    1 
ATOM   4812 C  CG1   . VAL B 1 140 ? -10.512 -0.434  11.898  1.00 74.24  ? 1357 VAL B CG1   1 
ATOM   4813 C  CG2   . VAL B 1 140 ? -11.564 1.755   12.525  1.00 73.44  ? 1357 VAL B CG2   1 
ATOM   4814 N  N     . VAL B 1 141 ? -11.004 0.996   16.120  1.00 59.43  ? 1358 VAL B N     1 
ATOM   4815 C  CA    . VAL B 1 141 ? -11.174 1.952   17.205  1.00 71.38  ? 1358 VAL B CA    1 
ATOM   4816 C  C     . VAL B 1 141 ? -10.042 2.960   17.141  1.00 86.42  ? 1358 VAL B C     1 
ATOM   4817 O  O     . VAL B 1 141 ? -8.863  2.584   17.067  1.00 90.06  ? 1358 VAL B O     1 
ATOM   4818 C  CB    . VAL B 1 141 ? -11.256 1.291   18.598  1.00 70.97  ? 1358 VAL B CB    1 
ATOM   4819 C  CG1   . VAL B 1 141 ? -10.124 0.424   18.832  1.00 70.95  ? 1358 VAL B CG1   1 
ATOM   4820 C  CG2   . VAL B 1 141 ? -11.275 2.363   19.695  1.00 78.06  ? 1358 VAL B CG2   1 
ATOM   4821 N  N     . ARG B 1 142 ? -10.418 4.244   17.138  1.00 84.25  ? 1359 ARG B N     1 
ATOM   4822 C  CA    . ARG B 1 142 ? -9.498  5.365   17.258  1.00 71.02  ? 1359 ARG B CA    1 
ATOM   4823 C  C     . ARG B 1 142 ? -10.036 6.138   18.436  1.00 68.79  ? 1359 ARG B C     1 
ATOM   4824 O  O     . ARG B 1 142 ? -11.127 6.708   18.362  1.00 80.30  ? 1359 ARG B O     1 
ATOM   4825 C  CB    . ARG B 1 142 ? -9.472  6.215   15.999  1.00 68.09  ? 1359 ARG B CB    1 
ATOM   4826 C  CG    . ARG B 1 142 ? -9.267  5.437   14.710  1.00 71.68  ? 1359 ARG B CG    1 
ATOM   4827 C  CD    . ARG B 1 142 ? -9.752  6.232   13.514  1.00 80.17  ? 1359 ARG B CD    1 
ATOM   4828 N  NE    . ARG B 1 142 ? -9.272  5.651   12.269  1.00 83.99  ? 1359 ARG B NE    1 
ATOM   4829 C  CZ    . ARG B 1 142 ? -9.509  6.162   11.069  1.00 91.57  ? 1359 ARG B CZ    1 
ATOM   4830 N  NH1   . ARG B 1 142 ? -10.219 7.270   10.943  1.00 97.52  ? 1359 ARG B NH1   1 
ATOM   4831 N  NH2   . ARG B 1 142 ? -9.024  5.569   9.992   1.00 95.28  ? 1359 ARG B NH2   1 
ATOM   4832 N  N     . TRP B 1 143 ? -9.276  6.158   19.517  1.00 70.24  ? 1360 TRP B N     1 
ATOM   4833 C  CA    . TRP B 1 143 ? -9.746  6.736   20.764  1.00 88.79  ? 1360 TRP B CA    1 
ATOM   4834 C  C     . TRP B 1 143 ? -9.729  8.269   20.692  1.00 101.06 ? 1360 TRP B C     1 
ATOM   4835 O  O     . TRP B 1 143 ? -9.098  8.966   21.490  1.00 91.67  ? 1360 TRP B O     1 
ATOM   4836 C  CB    . TRP B 1 143 ? -8.865  6.210   21.885  1.00 90.14  ? 1360 TRP B CB    1 
ATOM   4837 C  CG    . TRP B 1 143 ? -9.490  6.244   23.190  1.00 85.38  ? 1360 TRP B CG    1 
ATOM   4838 C  CD1   . TRP B 1 143 ? -9.242  7.132   24.188  1.00 83.02  ? 1360 TRP B CD1   1 
ATOM   4839 C  CD2   . TRP B 1 143 ? -10.471 5.339   23.683  1.00 86.73  ? 1360 TRP B CD2   1 
ATOM   4840 N  NE1   . TRP B 1 143 ? -10.022 6.845   25.279  1.00 87.95  ? 1360 TRP B NE1   1 
ATOM   4841 C  CE2   . TRP B 1 143 ? -10.788 5.747   24.996  1.00 91.67  ? 1360 TRP B CE2   1 
ATOM   4842 C  CE3   . TRP B 1 143 ? -11.133 4.231   23.138  1.00 87.48  ? 1360 TRP B CE3   1 
ATOM   4843 C  CZ2   . TRP B 1 143 ? -11.730 5.086   25.778  1.00 97.88  ? 1360 TRP B CZ2   1 
ATOM   4844 C  CZ3   . TRP B 1 143 ? -12.070 3.570   23.917  1.00 91.16  ? 1360 TRP B CZ3   1 
ATOM   4845 C  CH2   . TRP B 1 143 ? -12.360 4.002   25.226  1.00 96.58  ? 1360 TRP B CH2   1 
ATOM   4846 N  N     . GLU B 1 144 ? -10.442 8.780   19.691  1.00 108.93 ? 1361 GLU B N     1 
ATOM   4847 C  CA    . GLU B 1 144 ? -10.486 10.195  19.365  1.00 105.81 ? 1361 GLU B CA    1 
ATOM   4848 C  C     . GLU B 1 144 ? -11.665 10.821  20.097  1.00 100.86 ? 1361 GLU B C     1 
ATOM   4849 O  O     . GLU B 1 144 ? -11.566 11.905  20.647  1.00 108.23 ? 1361 GLU B O     1 
ATOM   4850 C  CB    . GLU B 1 144 ? -10.575 10.392  17.841  1.00 107.88 ? 1361 GLU B CB    1 
ATOM   4851 C  CG    . GLU B 1 144 ? -9.240  10.139  17.109  1.00 114.59 ? 1361 GLU B CG    1 
ATOM   4852 C  CD    . GLU B 1 144 ? -9.351  10.302  15.601  1.00 121.88 ? 1361 GLU B CD    1 
ATOM   4853 O  OE1   . GLU B 1 144 ? -10.361 10.892  15.155  1.00 122.94 ? 1361 GLU B OE1   1 
ATOM   4854 O  OE2   . GLU B 1 144 ? -8.431  9.849   14.869  1.00 122.07 ? 1361 GLU B OE2   1 
ATOM   4855 N  N     . LYS B 1 146 ? -12.991 13.366  21.576  1.00 107.11 ? 1363 LYS B N     1 
ATOM   4856 C  CA    . LYS B 1 146 ? -13.542 14.704  21.788  1.00 101.02 ? 1363 LYS B CA    1 
ATOM   4857 C  C     . LYS B 1 146 ? -14.833 14.509  22.557  1.00 108.61 ? 1363 LYS B C     1 
ATOM   4858 O  O     . LYS B 1 146 ? -14.885 13.703  23.487  1.00 116.10 ? 1363 LYS B O     1 
ATOM   4859 C  CB    . LYS B 1 146 ? -13.773 15.442  20.463  1.00 91.33  ? 1363 LYS B CB    1 
ATOM   4860 N  N     . HIS B 1 147 ? -15.847 15.310  22.224  1.00 104.33 ? 1364 HIS B N     1 
ATOM   4861 C  CA    . HIS B 1 147 ? -17.195 15.065  22.722  1.00 99.24  ? 1364 HIS B CA    1 
ATOM   4862 C  C     . HIS B 1 147 ? -17.831 14.128  21.706  1.00 95.62  ? 1364 HIS B C     1 
ATOM   4863 O  O     . HIS B 1 147 ? -18.140 14.563  20.588  1.00 100.85 ? 1364 HIS B O     1 
ATOM   4864 C  CB    . HIS B 1 147 ? -17.990 16.356  22.834  1.00 95.96  ? 1364 HIS B CB    1 
ATOM   4865 N  N     . PRO B 1 148 ? -18.024 12.859  22.023  1.00 87.13  ? 1365 PRO B N     1 
ATOM   4866 C  CA    . PRO B 1 148 ? -18.400 11.895  20.989  1.00 80.97  ? 1365 PRO B CA    1 
ATOM   4867 C  C     . PRO B 1 148 ? -19.879 11.973  20.657  1.00 80.69  ? 1365 PRO B C     1 
ATOM   4868 O  O     . PRO B 1 148 ? -20.703 12.421  21.448  1.00 85.82  ? 1365 PRO B O     1 
ATOM   4869 C  CB    . PRO B 1 148 ? -18.035 10.540  21.606  1.00 81.59  ? 1365 PRO B CB    1 
ATOM   4870 C  CG    . PRO B 1 148 ? -18.174 10.771  23.077  1.00 85.07  ? 1365 PRO B CG    1 
ATOM   4871 C  CD    . PRO B 1 148 ? -17.848 12.219  23.339  1.00 85.20  ? 1365 PRO B CD    1 
ATOM   4872 N  N     . GLN B 1 149 ? -20.211 11.480  19.466  1.00 80.21  ? 1366 GLN B N     1 
ATOM   4873 C  CA    . GLN B 1 149 ? -21.583 11.485  18.991  1.00 75.16  ? 1366 GLN B CA    1 
ATOM   4874 C  C     . GLN B 1 149 ? -21.802 10.243  18.147  1.00 87.20  ? 1366 GLN B C     1 
ATOM   4875 O  O     . GLN B 1 149 ? -20.918 9.873   17.356  1.00 100.58 ? 1366 GLN B O     1 
ATOM   4876 C  CB    . GLN B 1 149 ? -21.866 12.713  18.158  1.00 78.63  ? 1366 GLN B CB    1 
ATOM   4877 C  CG    . GLN B 1 149 ? -23.227 13.309  18.377  1.00 88.05  ? 1366 GLN B CG    1 
ATOM   4878 C  CD    . GLN B 1 149 ? -23.485 14.470  17.445  1.00 97.62  ? 1366 GLN B CD    1 
ATOM   4879 O  OE1   . GLN B 1 149 ? -22.633 14.830  16.636  1.00 99.83  ? 1366 GLN B OE1   1 
ATOM   4880 N  NE2   . GLN B 1 149 ? -24.663 15.061  17.551  1.00 106.00 ? 1366 GLN B NE2   1 
ATOM   4881 N  N     . PRO B 1 150 ? -22.961 9.593   18.298  1.00 81.23  ? 1367 PRO B N     1 
ATOM   4882 C  CA    . PRO B 1 150 ? -23.142 8.210   17.819  1.00 90.00  ? 1367 PRO B CA    1 
ATOM   4883 C  C     . PRO B 1 150 ? -22.700 7.849   16.399  1.00 104.07 ? 1367 PRO B C     1 
ATOM   4884 O  O     . PRO B 1 150 ? -22.188 6.742   16.216  1.00 122.23 ? 1367 PRO B O     1 
ATOM   4885 C  CB    . PRO B 1 150 ? -24.642 7.999   18.040  1.00 85.82  ? 1367 PRO B CB    1 
ATOM   4886 C  CG    . PRO B 1 150 ? -24.913 8.762   19.275  1.00 81.57  ? 1367 PRO B CG    1 
ATOM   4887 C  CD    . PRO B 1 150 ? -23.807 9.783   19.473  1.00 84.07  ? 1367 PRO B CD    1 
ATOM   4888 N  N     . PHE B 1 151 ? -22.928 8.655   15.373  1.00 90.60  ? 1368 PHE B N     1 
ATOM   4889 C  CA    . PHE B 1 151 ? -22.445 8.190   14.079  1.00 73.60  ? 1368 PHE B CA    1 
ATOM   4890 C  C     . PHE B 1 151 ? -21.348 9.066   13.540  1.00 82.13  ? 1368 PHE B C     1 
ATOM   4891 O  O     . PHE B 1 151 ? -20.691 8.690   12.574  1.00 87.49  ? 1368 PHE B O     1 
ATOM   4892 C  CB    . PHE B 1 151 ? -23.599 8.105   13.091  1.00 77.55  ? 1368 PHE B CB    1 
ATOM   4893 C  CG    . PHE B 1 151 ? -24.672 7.141   13.515  1.00 82.46  ? 1368 PHE B CG    1 
ATOM   4894 C  CD1   . PHE B 1 151 ? -24.535 5.779   13.278  1.00 84.05  ? 1368 PHE B CD1   1 
ATOM   4895 C  CD2   . PHE B 1 151 ? -25.803 7.591   14.169  1.00 72.24  ? 1368 PHE B CD2   1 
ATOM   4896 C  CE1   . PHE B 1 151 ? -25.522 4.884   13.677  1.00 86.92  ? 1368 PHE B CE1   1 
ATOM   4897 C  CE2   . PHE B 1 151 ? -26.790 6.702   14.571  1.00 81.38  ? 1368 PHE B CE2   1 
ATOM   4898 C  CZ    . PHE B 1 151 ? -26.650 5.346   14.322  1.00 83.35  ? 1368 PHE B CZ    1 
ATOM   4899 N  N     . LEU B 1 152 ? -21.130 10.212  14.164  1.00 82.32  ? 1369 LEU B N     1 
ATOM   4900 C  CA    . LEU B 1 152 ? -20.216 11.217  13.682  1.00 77.71  ? 1369 LEU B CA    1 
ATOM   4901 C  C     . LEU B 1 152 ? -18.903 11.189  14.439  1.00 78.33  ? 1369 LEU B C     1 
ATOM   4902 O  O     . LEU B 1 152 ? -17.834 11.214  13.816  1.00 89.54  ? 1369 LEU B O     1 
ATOM   4903 C  CB    . LEU B 1 152 ? -20.889 12.586  13.788  1.00 80.30  ? 1369 LEU B CB    1 
ATOM   4904 C  CG    . LEU B 1 152 ? -22.338 12.446  13.305  1.00 73.23  ? 1369 LEU B CG    1 
ATOM   4905 C  CD1   . LEU B 1 152 ? -23.096 13.770  13.395  1.00 66.64  ? 1369 LEU B CD1   1 
ATOM   4906 C  CD2   . LEU B 1 152 ? -22.359 11.894  11.878  1.00 70.57  ? 1369 LEU B CD2   1 
ATOM   4907 N  N     . ARG B 1 153 ? -18.955 11.044  15.764  1.00 66.70  ? 1370 ARG B N     1 
ATOM   4908 C  CA    . ARG B 1 153 ? -17.744 10.933  16.573  1.00 74.70  ? 1370 ARG B CA    1 
ATOM   4909 C  C     . ARG B 1 153 ? -17.880 9.691   17.442  1.00 80.12  ? 1370 ARG B C     1 
ATOM   4910 O  O     . ARG B 1 153 ? -18.314 9.780   18.593  1.00 75.63  ? 1370 ARG B O     1 
ATOM   4911 C  CB    . ARG B 1 153 ? -17.523 12.185  17.414  1.00 82.50  ? 1370 ARG B CB    1 
ATOM   4912 C  CG    . ARG B 1 153 ? -17.802 13.494  16.671  1.00 93.57  ? 1370 ARG B CG    1 
ATOM   4913 C  CD    . ARG B 1 153 ? -17.385 14.721  17.485  1.00 101.35 ? 1370 ARG B CD    1 
ATOM   4914 N  NE    . ARG B 1 153 ? -18.428 15.170  18.409  1.00 108.66 ? 1370 ARG B NE    1 
ATOM   4915 C  CZ    . ARG B 1 153 ? -19.469 15.927  18.065  1.00 111.86 ? 1370 ARG B CZ    1 
ATOM   4916 N  NH1   . ARG B 1 153 ? -19.619 16.322  16.806  1.00 116.70 ? 1370 ARG B NH1   1 
ATOM   4917 N  NH2   . ARG B 1 153 ? -20.364 16.288  18.980  1.00 109.28 ? 1370 ARG B NH2   1 
ATOM   4918 N  N     . THR B 1 154 ? -17.446 8.543   16.910  1.00 85.52  ? 1371 THR B N     1 
ATOM   4919 C  CA    . THR B 1 154 ? -17.419 7.304   17.674  1.00 78.65  ? 1371 THR B CA    1 
ATOM   4920 C  C     . THR B 1 154 ? -16.000 6.817   17.841  1.00 73.58  ? 1371 THR B C     1 
ATOM   4921 O  O     . THR B 1 154 ? -15.187 6.923   16.919  1.00 76.64  ? 1371 THR B O     1 
ATOM   4922 C  CB    . THR B 1 154 ? -18.207 6.180   17.008  1.00 71.15  ? 1371 THR B CB    1 
ATOM   4923 O  OG1   . THR B 1 154 ? -18.070 6.265   15.585  1.00 86.67  ? 1371 THR B OG1   1 
ATOM   4924 C  CG2   . THR B 1 154 ? -19.632 6.275   17.396  1.00 63.53  ? 1371 THR B CG2   1 
ATOM   4925 N  N     . ARG B 1 155 ? -15.732 6.224   19.005  1.00 72.62  ? 1372 ARG B N     1 
ATOM   4926 C  CA    . ARG B 1 155 ? -14.405 5.677   19.252  1.00 76.19  ? 1372 ARG B CA    1 
ATOM   4927 C  C     . ARG B 1 155 ? -14.248 4.313   18.580  1.00 79.71  ? 1372 ARG B C     1 
ATOM   4928 O  O     . ARG B 1 155 ? -13.255 4.080   17.891  1.00 82.70  ? 1372 ARG B O     1 
ATOM   4929 C  CB    . ARG B 1 155 ? -14.142 5.592   20.755  1.00 80.43  ? 1372 ARG B CB    1 
ATOM   4930 C  CG    . ARG B 1 155 ? -14.037 6.973   21.395  1.00 91.39  ? 1372 ARG B CG    1 
ATOM   4931 C  CD    . ARG B 1 155 ? -13.140 6.972   22.611  1.00 96.39  ? 1372 ARG B CD    1 
ATOM   4932 N  NE    . ARG B 1 155 ? -13.675 7.714   23.750  1.00 92.50  ? 1372 ARG B NE    1 
ATOM   4933 C  CZ    . ARG B 1 155 ? -13.170 8.857   24.198  1.00 105.69 ? 1372 ARG B CZ    1 
ATOM   4934 N  NH1   . ARG B 1 155 ? -12.115 9.397   23.597  1.00 112.96 ? 1372 ARG B NH1   1 
ATOM   4935 N  NH2   . ARG B 1 155 ? -13.716 9.460   25.251  1.00 108.32 ? 1372 ARG B NH2   1 
ATOM   4936 N  N     . GLU B 1 156 ? -15.248 3.440   18.681  1.00 74.20  ? 1373 GLU B N     1 
ATOM   4937 C  CA    . GLU B 1 156 ? -15.300 2.238   17.859  1.00 69.32  ? 1373 GLU B CA    1 
ATOM   4938 C  C     . GLU B 1 156 ? -16.319 2.435   16.748  1.00 71.67  ? 1373 GLU B C     1 
ATOM   4939 O  O     . GLU B 1 156 ? -17.433 2.907   16.999  1.00 83.22  ? 1373 GLU B O     1 
ATOM   4940 C  CB    . GLU B 1 156 ? -15.672 0.997   18.672  1.00 56.42  ? 1373 GLU B CB    1 
ATOM   4941 C  CG    . GLU B 1 156 ? -15.554 -0.255  17.794  1.00 62.73  ? 1373 GLU B CG    1 
ATOM   4942 C  CD    . GLU B 1 156 ? -16.467 -1.392  18.191  1.00 74.30  ? 1373 GLU B CD    1 
ATOM   4943 O  OE1   . GLU B 1 156 ? -17.285 -1.233  19.121  1.00 83.76  ? 1373 GLU B OE1   1 
ATOM   4944 O  OE2   . GLU B 1 156 ? -16.375 -2.460  17.554  1.00 78.50  ? 1373 GLU B OE2   1 
ATOM   4945 N  N     . PHE B 1 157 ? -15.952 2.072   15.525  1.00 66.39  ? 1374 PHE B N     1 
ATOM   4946 C  CA    . PHE B 1 157 ? -16.940 2.163   14.468  1.00 61.29  ? 1374 PHE B CA    1 
ATOM   4947 C  C     . PHE B 1 157 ? -16.673 1.114   13.407  1.00 62.95  ? 1374 PHE B C     1 
ATOM   4948 O  O     . PHE B 1 157 ? -15.584 0.531   13.313  1.00 71.50  ? 1374 PHE B O     1 
ATOM   4949 C  CB    . PHE B 1 157 ? -17.007 3.567   13.842  1.00 62.84  ? 1374 PHE B CB    1 
ATOM   4950 C  CG    . PHE B 1 157 ? -15.738 4.023   13.182  1.00 73.51  ? 1374 PHE B CG    1 
ATOM   4951 C  CD1   . PHE B 1 157 ? -15.509 3.788   11.835  1.00 67.59  ? 1374 PHE B CD1   1 
ATOM   4952 C  CD2   . PHE B 1 157 ? -14.781 4.728   13.912  1.00 85.81  ? 1374 PHE B CD2   1 
ATOM   4953 C  CE1   . PHE B 1 157 ? -14.329 4.235   11.230  1.00 83.49  ? 1374 PHE B CE1   1 
ATOM   4954 C  CE2   . PHE B 1 157 ? -13.600 5.170   13.319  1.00 83.30  ? 1374 PHE B CE2   1 
ATOM   4955 C  CZ    . PHE B 1 157 ? -13.371 4.928   11.978  1.00 81.74  ? 1374 PHE B CZ    1 
ATOM   4956 N  N     . LEU B 1 158 ? -17.704 0.892   12.608  1.00 51.57  ? 1375 LEU B N     1 
ATOM   4957 C  CA    . LEU B 1 158 ? -17.662 -0.019  11.480  1.00 54.20  ? 1375 LEU B CA    1 
ATOM   4958 C  C     . LEU B 1 158 ? -17.282 0.715   10.214  1.00 67.27  ? 1375 LEU B C     1 
ATOM   4959 O  O     . LEU B 1 158 ? -17.664 1.872   10.011  1.00 89.07  ? 1375 LEU B O     1 
ATOM   4960 C  CB    . LEU B 1 158 ? -19.027 -0.688  11.268  1.00 48.28  ? 1375 LEU B CB    1 
ATOM   4961 C  CG    . LEU B 1 158 ? -19.764 -1.181  12.518  1.00 50.02  ? 1375 LEU B CG    1 
ATOM   4962 C  CD1   . LEU B 1 158 ? -21.110 -1.755  12.172  1.00 64.23  ? 1375 LEU B CD1   1 
ATOM   4963 C  CD2   . LEU B 1 158 ? -18.927 -2.223  13.271  1.00 59.09  ? 1375 LEU B CD2   1 
ATOM   4964 N  N     . TRP B 1 159 ? -16.539 0.038   9.356   1.00 59.12  ? 1376 TRP B N     1 
ATOM   4965 C  CA    . TRP B 1 159 ? -16.327 0.581   8.028   1.00 64.01  ? 1376 TRP B CA    1 
ATOM   4966 C  C     . TRP B 1 159 ? -15.980 -0.561  7.098   1.00 60.82  ? 1376 TRP B C     1 
ATOM   4967 O  O     . TRP B 1 159 ? -15.880 -1.720  7.509   1.00 64.13  ? 1376 TRP B O     1 
ATOM   4968 C  CB    . TRP B 1 159 ? -15.225 1.648   8.034   1.00 59.53  ? 1376 TRP B CB    1 
ATOM   4969 C  CG    . TRP B 1 159 ? -13.832 1.162   8.359   1.00 67.07  ? 1376 TRP B CG    1 
ATOM   4970 C  CD1   . TRP B 1 159 ? -13.481 -0.040  8.887   1.00 74.26  ? 1376 TRP B CD1   1 
ATOM   4971 C  CD2   . TRP B 1 159 ? -12.604 1.896   8.195   1.00 78.72  ? 1376 TRP B CD2   1 
ATOM   4972 N  NE1   . TRP B 1 159 ? -12.119 -0.114  9.056   1.00 77.83  ? 1376 TRP B NE1   1 
ATOM   4973 C  CE2   . TRP B 1 159 ? -11.555 1.062   8.641   1.00 80.15  ? 1376 TRP B CE2   1 
ATOM   4974 C  CE3   . TRP B 1 159 ? -12.291 3.177   7.718   1.00 71.71  ? 1376 TRP B CE3   1 
ATOM   4975 C  CZ2   . TRP B 1 159 ? -10.215 1.459   8.611   1.00 73.77  ? 1376 TRP B CZ2   1 
ATOM   4976 C  CZ3   . TRP B 1 159 ? -10.958 3.569   7.689   1.00 72.06  ? 1376 TRP B CZ3   1 
ATOM   4977 C  CH2   . TRP B 1 159 ? -9.938  2.713   8.133   1.00 74.13  ? 1376 TRP B CH2   1 
ATOM   4978 N  N     . GLN B 1 160 ? -15.518 -0.163  5.943   1.00 65.23  ? 1377 GLN B N     1 
ATOM   4979 C  CA    . GLN B 1 160 ? -14.862 -1.024  5.030   1.00 54.48  ? 1377 GLN B CA    1 
ATOM   4980 C  C     . GLN B 1 160 ? -13.648 -0.273  4.605   1.00 61.14  ? 1377 GLN B C     1 
ATOM   4981 O  O     . GLN B 1 160 ? -13.685 0.839   4.348   1.00 70.64  ? 1377 GLN B O     1 
ATOM   4982 C  CB    . GLN B 1 160 ? -15.654 -1.390  3.831   1.00 59.15  ? 1377 GLN B CB    1 
ATOM   4983 C  CG    . GLN B 1 160 ? -16.030 -0.261  2.953   1.00 77.45  ? 1377 GLN B CG    1 
ATOM   4984 C  CD    . GLN B 1 160 ? -14.944 0.154   2.069   1.00 89.17  ? 1377 GLN B CD    1 
ATOM   4985 O  OE1   . GLN B 1 160 ? -14.874 1.277   1.649   1.00 98.46  ? 1377 GLN B OE1   1 
ATOM   4986 N  NE2   . GLN B 1 160 ? -14.083 -0.739  1.795   1.00 88.11  ? 1377 GLN B NE2   1 
ATOM   4987 N  N     . GLU B 1 161 ? -12.525 -0.909  4.668   1.00 65.69  ? 1378 GLU B N     1 
ATOM   4988 C  CA    . GLU B 1 161 ? -11.247 -0.414  4.186   1.00 61.28  ? 1378 GLU B CA    1 
ATOM   4989 C  C     . GLU B 1 161 ? -10.762 -1.351  3.083   1.00 65.39  ? 1378 GLU B C     1 
ATOM   4990 O  O     . GLU B 1 161 ? -10.610 -2.557  3.307   1.00 69.70  ? 1378 GLU B O     1 
ATOM   4991 C  CB    . GLU B 1 161 ? -10.223 -0.310  5.325   1.00 62.89  ? 1378 GLU B CB    1 
ATOM   4992 C  CG    . GLU B 1 161 ? -10.196 -1.462  6.305   1.00 70.90  ? 1378 GLU B CG    1 
ATOM   4993 C  CD    . GLU B 1 161 ? -8.941  -1.450  7.193   1.00 75.58  ? 1378 GLU B CD    1 
ATOM   4994 O  OE1   . GLU B 1 161 ? -7.882  -0.935  6.755   1.00 74.58  ? 1378 GLU B OE1   1 
ATOM   4995 O  OE2   . GLU B 1 161 ? -9.011  -1.982  8.326   1.00 72.52  ? 1378 GLU B OE2   1 
ATOM   4996 N  N     . GLY B 1 162 ? -10.578 -0.806  1.884   1.00 64.50  ? 1379 GLY B N     1 
ATOM   4997 C  CA    . GLY B 1 162 ? -10.074 -1.549  0.736   1.00 65.97  ? 1379 GLY B CA    1 
ATOM   4998 C  C     . GLY B 1 162 ? -8.681  -1.064  0.377   1.00 68.17  ? 1379 GLY B C     1 
ATOM   4999 O  O     . GLY B 1 162 ? -8.435  0.143   0.346   1.00 75.96  ? 1379 GLY B O     1 
ATOM   5000 N  N     . HIS B 1 163 ? -7.784  -2.014  0.088   1.00 62.41  ? 1380 HIS B N     1 
ATOM   5001 C  CA    . HIS B 1 163 ? -6.362  -1.763  -0.155  1.00 61.10  ? 1380 HIS B CA    1 
ATOM   5002 C  C     . HIS B 1 163 ? -5.918  -2.524  -1.399  1.00 66.91  ? 1380 HIS B C     1 
ATOM   5003 O  O     . HIS B 1 163 ? -6.187  -3.727  -1.544  1.00 87.25  ? 1380 HIS B O     1 
ATOM   5004 C  CB    . HIS B 1 163 ? -5.510  -2.185  1.041   1.00 61.58  ? 1380 HIS B CB    1 
ATOM   5005 C  CG    . HIS B 1 163 ? -5.900  -1.548  2.352   1.00 74.86  ? 1380 HIS B CG    1 
ATOM   5006 N  ND1   . HIS B 1 163 ? -5.159  -0.543  2.947   1.00 78.83  ? 1380 HIS B ND1   1 
ATOM   5007 C  CD2   . HIS B 1 163 ? -6.923  -1.810  3.201   1.00 71.76  ? 1380 HIS B CD2   1 
ATOM   5008 C  CE1   . HIS B 1 163 ? -5.719  -0.209  4.098   1.00 79.00  ? 1380 HIS B CE1   1 
ATOM   5009 N  NE2   . HIS B 1 163 ? -6.790  -0.964  4.275   1.00 72.91  ? 1380 HIS B NE2   1 
ATOM   5010 N  N     . THR B 1 164 ? -5.279  -1.812  -2.314  1.00 61.43  ? 1381 THR B N     1 
ATOM   5011 C  CA    . THR B 1 164 ? -5.024  -2.322  -3.652  1.00 66.60  ? 1381 THR B CA    1 
ATOM   5012 C  C     . THR B 1 164 ? -3.634  -1.886  -4.114  1.00 81.24  ? 1381 THR B C     1 
ATOM   5013 O  O     . THR B 1 164 ? -3.174  -0.787  -3.790  1.00 82.82  ? 1381 THR B O     1 
ATOM   5014 C  CB    . THR B 1 164 ? -6.092  -1.828  -4.629  1.00 66.81  ? 1381 THR B CB    1 
ATOM   5015 O  OG1   . THR B 1 164 ? -5.874  -0.439  -4.919  1.00 68.05  ? 1381 THR B OG1   1 
ATOM   5016 C  CG2   . THR B 1 164 ? -7.491  -2.005  -4.053  1.00 58.84  ? 1381 THR B CG2   1 
ATOM   5017 N  N     . ALA B 1 165 ? -2.989  -2.758  -4.898  1.00 79.17  ? 1382 ALA B N     1 
ATOM   5018 C  CA    . ALA B 1 165 ? -1.634  -2.563  -5.417  1.00 72.24  ? 1382 ALA B CA    1 
ATOM   5019 C  C     . ALA B 1 165 ? -1.579  -3.023  -6.867  1.00 72.91  ? 1382 ALA B C     1 
ATOM   5020 O  O     . ALA B 1 165 ? -2.004  -4.133  -7.185  1.00 76.09  ? 1382 ALA B O     1 
ATOM   5021 C  CB    . ALA B 1 165 ? -0.592  -3.320  -4.590  1.00 57.58  ? 1382 ALA B CB    1 
ATOM   5022 N  N     . PHE B 1 166 ? -1.057  -2.166  -7.738  1.00 76.51  ? 1383 PHE B N     1 
ATOM   5023 C  CA    . PHE B 1 166 ? -0.996  -2.389  -9.174  1.00 83.35  ? 1383 PHE B CA    1 
ATOM   5024 C  C     . PHE B 1 166 ? 0.430   -2.169  -9.651  1.00 88.98  ? 1383 PHE B C     1 
ATOM   5025 O  O     . PHE B 1 166 ? 1.280   -1.628  -8.938  1.00 88.06  ? 1383 PHE B O     1 
ATOM   5026 C  CB    . PHE B 1 166 ? -1.904  -1.433  -9.964  1.00 83.93  ? 1383 PHE B CB    1 
ATOM   5027 C  CG    . PHE B 1 166 ? -3.310  -1.376  -9.491  1.00 80.57  ? 1383 PHE B CG    1 
ATOM   5028 C  CD1   . PHE B 1 166 ? -3.654  -0.637  -8.374  1.00 81.72  ? 1383 PHE B CD1   1 
ATOM   5029 C  CD2   . PHE B 1 166 ? -4.311  -2.029  -10.200 1.00 77.39  ? 1383 PHE B CD2   1 
ATOM   5030 C  CE1   . PHE B 1 166 ? -4.989  -0.582  -7.944  1.00 77.94  ? 1383 PHE B CE1   1 
ATOM   5031 C  CE2   . PHE B 1 166 ? -5.638  -1.971  -9.792  1.00 59.97  ? 1383 PHE B CE2   1 
ATOM   5032 C  CZ    . PHE B 1 166 ? -5.978  -1.256  -8.659  1.00 59.92  ? 1383 PHE B CZ    1 
ATOM   5033 N  N     . ALA B 1 167 ? 0.672   -2.559  -10.900 1.00 89.53  ? 1384 ALA B N     1 
ATOM   5034 C  CA    . ALA B 1 167 ? 1.978   -2.317  -11.490 1.00 82.61  ? 1384 ALA B CA    1 
ATOM   5035 C  C     . ALA B 1 167 ? 2.096   -0.881  -11.995 1.00 96.50  ? 1384 ALA B C     1 
ATOM   5036 O  O     . ALA B 1 167 ? 3.102   -0.209  -11.735 1.00 111.45 ? 1384 ALA B O     1 
ATOM   5037 C  CB    . ALA B 1 167 ? 2.240   -3.327  -12.609 1.00 67.99  ? 1384 ALA B CB    1 
ATOM   5038 N  N     . THR B 1 168 ? 1.091   -0.384  -12.712 1.00 94.66  ? 1385 THR B N     1 
ATOM   5039 C  CA    . THR B 1 168 ? 1.166   0.983   -13.207 1.00 94.27  ? 1385 THR B CA    1 
ATOM   5040 C  C     . THR B 1 168 ? 0.329   1.929   -12.357 1.00 92.61  ? 1385 THR B C     1 
ATOM   5041 O  O     . THR B 1 168 ? -0.665  1.548   -11.736 1.00 90.99  ? 1385 THR B O     1 
ATOM   5042 C  CB    . THR B 1 168 ? 0.746   1.114   -14.676 1.00 97.95  ? 1385 THR B CB    1 
ATOM   5043 O  OG1   . THR B 1 168 ? 0.671   2.509   -15.006 1.00 121.90 ? 1385 THR B OG1   1 
ATOM   5044 C  CG2   . THR B 1 168 ? -0.600  0.511   -14.935 1.00 87.23  ? 1385 THR B CG2   1 
ATOM   5045 N  N     . GLN B 1 169 ? 0.742   3.196   -12.373 1.00 94.68  ? 1386 GLN B N     1 
ATOM   5046 C  CA    . GLN B 1 169 ? -0.023  4.252   -11.735 1.00 95.95  ? 1386 GLN B CA    1 
ATOM   5047 C  C     . GLN B 1 169 ? -1.353  4.523   -12.436 1.00 94.02  ? 1386 GLN B C     1 
ATOM   5048 O  O     . GLN B 1 169 ? -2.268  5.078   -11.810 1.00 90.66  ? 1386 GLN B O     1 
ATOM   5049 C  CB    . GLN B 1 169 ? 0.815   5.526   -11.689 1.00 93.07  ? 1386 GLN B CB    1 
ATOM   5050 C  CG    . GLN B 1 169 ? 0.344   6.518   -10.655 1.00 92.29  ? 1386 GLN B CG    1 
ATOM   5051 C  CD    . GLN B 1 169 ? 1.237   7.722   -10.572 1.00 87.59  ? 1386 GLN B CD    1 
ATOM   5052 O  OE1   . GLN B 1 169 ? 1.359   8.488   -11.533 1.00 84.49  ? 1386 GLN B OE1   1 
ATOM   5053 N  NE2   . GLN B 1 169 ? 1.873   7.904   -9.420  1.00 82.18  ? 1386 GLN B NE2   1 
ATOM   5054 N  N     . LYS B 1 170 ? -1.480  4.168   -13.714 1.00 89.30  ? 1387 LYS B N     1 
ATOM   5055 C  CA    . LYS B 1 170 ? -2.728  4.449   -14.410 1.00 85.61  ? 1387 LYS B CA    1 
ATOM   5056 C  C     . LYS B 1 170 ? -3.870  3.608   -13.859 1.00 89.26  ? 1387 LYS B C     1 
ATOM   5057 O  O     . LYS B 1 170 ? -4.956  4.129   -13.572 1.00 85.34  ? 1387 LYS B O     1 
ATOM   5058 C  CB    . LYS B 1 170 ? -2.570  4.209   -15.903 1.00 80.61  ? 1387 LYS B CB    1 
ATOM   5059 C  CG    . LYS B 1 170 ? -3.767  4.680   -16.669 1.00 81.48  ? 1387 LYS B CG    1 
ATOM   5060 C  CD    . LYS B 1 170 ? -4.008  3.819   -17.861 1.00 89.08  ? 1387 LYS B CD    1 
ATOM   5061 C  CE    . LYS B 1 170 ? -3.147  4.290   -18.991 1.00 99.90  ? 1387 LYS B CE    1 
ATOM   5062 N  NZ    . LYS B 1 170 ? -3.863  5.362   -19.742 1.00 107.01 ? 1387 LYS B NZ    1 
ATOM   5063 N  N     . GLU B 1 171 ? -3.649  2.301   -13.728 1.00 86.84  ? 1388 GLU B N     1 
ATOM   5064 C  CA    . GLU B 1 171 ? -4.625  1.451   -13.064 1.00 77.46  ? 1388 GLU B CA    1 
ATOM   5065 C  C     . GLU B 1 171 ? -5.040  2.058   -11.735 1.00 78.56  ? 1388 GLU B C     1 
ATOM   5066 O  O     . GLU B 1 171 ? -6.235  2.215   -11.451 1.00 81.47  ? 1388 GLU B O     1 
ATOM   5067 C  CB    . GLU B 1 171 ? -4.043  0.051   -12.840 1.00 74.21  ? 1388 GLU B CB    1 
ATOM   5068 C  CG    . GLU B 1 171 ? -3.722  -0.725  -14.091 1.00 91.81  ? 1388 GLU B CG    1 
ATOM   5069 C  CD    . GLU B 1 171 ? -3.013  -2.062  -13.805 1.00 108.12 ? 1388 GLU B CD    1 
ATOM   5070 O  OE1   . GLU B 1 171 ? -3.585  -3.122  -14.142 1.00 112.32 ? 1388 GLU B OE1   1 
ATOM   5071 O  OE2   . GLU B 1 171 ? -1.887  -2.060  -13.255 1.00 109.41 ? 1388 GLU B OE2   1 
ATOM   5072 N  N     . ALA B 1 172 ? -4.052  2.439   -10.923 1.00 76.17  ? 1389 ALA B N     1 
ATOM   5073 C  CA    . ALA B 1 172 ? -4.341  2.896   -9.568  1.00 71.11  ? 1389 ALA B CA    1 
ATOM   5074 C  C     . ALA B 1 172 ? -5.184  4.170   -9.586  1.00 73.19  ? 1389 ALA B C     1 
ATOM   5075 O  O     . ALA B 1 172 ? -6.181  4.275   -8.860  1.00 81.47  ? 1389 ALA B O     1 
ATOM   5076 C  CB    . ALA B 1 172 ? -3.035  3.088   -8.786  1.00 52.51  ? 1389 ALA B CB    1 
ATOM   5077 N  N     . ASP B 1 173 ? -4.796  5.149   -10.412 1.00 70.02  ? 1390 ASP B N     1 
ATOM   5078 C  CA    . ASP B 1 173 ? -5.568  6.387   -10.539 1.00 75.09  ? 1390 ASP B CA    1 
ATOM   5079 C  C     . ASP B 1 173 ? -7.003  6.108   -10.963 1.00 79.94  ? 1390 ASP B C     1 
ATOM   5080 O  O     . ASP B 1 173 ? -7.965  6.599   -10.337 1.00 94.70  ? 1390 ASP B O     1 
ATOM   5081 C  CB    . ASP B 1 173 ? -4.896  7.317   -11.545 1.00 80.57  ? 1390 ASP B CB    1 
ATOM   5082 C  CG    . ASP B 1 173 ? -3.645  7.963   -10.991 1.00 91.66  ? 1390 ASP B CG    1 
ATOM   5083 O  OD1   . ASP B 1 173 ? -3.594  8.194   -9.760  1.00 86.68  ? 1390 ASP B OD1   1 
ATOM   5084 O  OD2   . ASP B 1 173 ? -2.719  8.241   -11.784 1.00 101.22 ? 1390 ASP B OD2   1 
ATOM   5085 N  N     . GLU B 1 174 ? -7.170  5.318   -12.032 1.00 77.91  ? 1391 GLU B N     1 
ATOM   5086 C  CA    . GLU B 1 174 ? -8.510  5.109   -12.560 1.00 75.73  ? 1391 GLU B CA    1 
ATOM   5087 C  C     . GLU B 1 174 ? -9.381  4.421   -11.527 1.00 74.30  ? 1391 GLU B C     1 
ATOM   5088 O  O     . GLU B 1 174 ? -10.546 4.800   -11.338 1.00 74.74  ? 1391 GLU B O     1 
ATOM   5089 C  CB    . GLU B 1 174 ? -8.442  4.322   -13.871 1.00 84.62  ? 1391 GLU B CB    1 
ATOM   5090 C  CG    . GLU B 1 174 ? -8.107  5.242   -15.039 1.00 107.24 ? 1391 GLU B CG    1 
ATOM   5091 C  CD    . GLU B 1 174 ? -7.888  4.541   -16.372 1.00 120.69 ? 1391 GLU B CD    1 
ATOM   5092 O  OE1   . GLU B 1 174 ? -7.531  3.345   -16.381 1.00 114.13 ? 1391 GLU B OE1   1 
ATOM   5093 O  OE2   . GLU B 1 174 ? -8.045  5.215   -17.420 1.00 130.86 ? 1391 GLU B OE2   1 
ATOM   5094 N  N     . GLU B 1 175 ? -8.796  3.489   -10.766 1.00 72.90  ? 1392 GLU B N     1 
ATOM   5095 C  CA    . GLU B 1 175 ? -9.544  2.865   -9.683  1.00 68.75  ? 1392 GLU B CA    1 
ATOM   5096 C  C     . GLU B 1 175 ? -9.968  3.895   -8.629  1.00 71.44  ? 1392 GLU B C     1 
ATOM   5097 O  O     . GLU B 1 175 ? -11.104 3.858   -8.140  1.00 67.99  ? 1392 GLU B O     1 
ATOM   5098 C  CB    . GLU B 1 175 ? -8.724  1.756   -9.025  1.00 55.86  ? 1392 GLU B CB    1 
ATOM   5099 C  CG    . GLU B 1 175 ? -9.469  1.131   -7.820  1.00 64.35  ? 1392 GLU B CG    1 
ATOM   5100 C  CD    . GLU B 1 175 ? -8.651  0.141   -7.016  1.00 78.13  ? 1392 GLU B CD    1 
ATOM   5101 O  OE1   . GLU B 1 175 ? -8.802  -1.067  -7.271  1.00 82.84  ? 1392 GLU B OE1   1 
ATOM   5102 O  OE2   . GLU B 1 175 ? -7.875  0.561   -6.122  1.00 79.45  ? 1392 GLU B OE2   1 
ATOM   5103 N  N     . VAL B 1 176 ? -9.052  4.787   -8.220  1.00 70.81  ? 1393 VAL B N     1 
ATOM   5104 C  CA    . VAL B 1 176 ? -9.418  5.796   -7.218  1.00 63.59  ? 1393 VAL B CA    1 
ATOM   5105 C  C     . VAL B 1 176 ? -10.701 6.497   -7.648  1.00 68.64  ? 1393 VAL B C     1 
ATOM   5106 O  O     . VAL B 1 176 ? -11.641 6.689   -6.855  1.00 67.17  ? 1393 VAL B O     1 
ATOM   5107 C  CB    . VAL B 1 176 ? -8.277  6.815   -7.003  1.00 55.92  ? 1393 VAL B CB    1 
ATOM   5108 C  CG1   . VAL B 1 176 ? -8.786  8.008   -6.198  1.00 65.76  ? 1393 VAL B CG1   1 
ATOM   5109 C  CG2   . VAL B 1 176 ? -7.077  6.200   -6.300  1.00 64.52  ? 1393 VAL B CG2   1 
ATOM   5110 N  N     . LEU B 1 177 ? -10.770 6.843   -8.932  1.00 66.16  ? 1394 LEU B N     1 
ATOM   5111 C  CA    . LEU B 1 177 ? -11.937 7.564   -9.431  1.00 59.23  ? 1394 LEU B CA    1 
ATOM   5112 C  C     . LEU B 1 177 ? -13.179 6.676   -9.474  1.00 70.40  ? 1394 LEU B C     1 
ATOM   5113 O  O     . LEU B 1 177 ? -14.285 7.128   -9.162  1.00 71.80  ? 1394 LEU B O     1 
ATOM   5114 C  CB    . LEU B 1 177 ? -11.627 8.118   -10.813 1.00 69.89  ? 1394 LEU B CB    1 
ATOM   5115 C  CG    . LEU B 1 177 ? -10.420 9.046   -10.768 1.00 71.30  ? 1394 LEU B CG    1 
ATOM   5116 C  CD1   . LEU B 1 177 ? -10.074 9.594   -12.160 1.00 74.06  ? 1394 LEU B CD1   1 
ATOM   5117 C  CD2   . LEU B 1 177 ? -10.747 10.149  -9.786  1.00 65.88  ? 1394 LEU B CD2   1 
ATOM   5118 N  N     . THR B 1 178 ? -13.014 5.404   -9.839  1.00 79.78  ? 1395 THR B N     1 
ATOM   5119 C  CA    . THR B 1 178 ? -14.163 4.500   -9.893  1.00 71.87  ? 1395 THR B CA    1 
ATOM   5120 C  C     . THR B 1 178 ? -14.782 4.297   -8.512  1.00 60.80  ? 1395 THR B C     1 
ATOM   5121 O  O     . THR B 1 178 ? -16.011 4.329   -8.354  1.00 63.67  ? 1395 THR B O     1 
ATOM   5122 C  CB    . THR B 1 178 ? -13.716 3.175   -10.503 1.00 67.75  ? 1395 THR B CB    1 
ATOM   5123 O  OG1   . THR B 1 178 ? -13.072 3.440   -11.763 1.00 61.86  ? 1395 THR B OG1   1 
ATOM   5124 C  CG2   . THR B 1 178 ? -14.907 2.200   -10.687 1.00 60.62  ? 1395 THR B CG2   1 
ATOM   5125 N  N     . ILE B 1 179 ? -13.939 4.147   -7.490  1.00 60.92  ? 1396 ILE B N     1 
ATOM   5126 C  CA    . ILE B 1 179 ? -14.428 3.999   -6.124  1.00 56.86  ? 1396 ILE B CA    1 
ATOM   5127 C  C     . ILE B 1 179 ? -15.062 5.295   -5.635  1.00 68.37  ? 1396 ILE B C     1 
ATOM   5128 O  O     . ILE B 1 179 ? -16.051 5.274   -4.890  1.00 69.01  ? 1396 ILE B O     1 
ATOM   5129 C  CB    . ILE B 1 179 ? -13.300 3.537   -5.189  1.00 63.52  ? 1396 ILE B CB    1 
ATOM   5130 C  CG1   . ILE B 1 179 ? -12.665 2.215   -5.685  1.00 58.38  ? 1396 ILE B CG1   1 
ATOM   5131 C  CG2   . ILE B 1 179 ? -13.829 3.444   -3.741  1.00 70.22  ? 1396 ILE B CG2   1 
ATOM   5132 C  CD1   . ILE B 1 179 ? -13.588 0.964   -5.579  1.00 44.36  ? 1396 ILE B CD1   1 
ATOM   5133 N  N     . LEU B 1 180 ? -14.497 6.449   -6.008  1.00 75.00  ? 1397 LEU B N     1 
ATOM   5134 C  CA    . LEU B 1 180 ? -15.145 7.685   -5.583  1.00 68.84  ? 1397 LEU B CA    1 
ATOM   5135 C  C     . LEU B 1 180 ? -16.516 7.833   -6.241  1.00 66.60  ? 1397 LEU B C     1 
ATOM   5136 O  O     . LEU B 1 180 ? -17.484 8.265   -5.603  1.00 63.33  ? 1397 LEU B O     1 
ATOM   5137 C  CB    . LEU B 1 180 ? -14.262 8.881   -5.904  1.00 73.31  ? 1397 LEU B CB    1 
ATOM   5138 C  CG    . LEU B 1 180 ? -14.732 10.162  -5.210  1.00 74.31  ? 1397 LEU B CG    1 
ATOM   5139 C  CD1   . LEU B 1 180 ? -14.325 10.146  -3.741  1.00 77.04  ? 1397 LEU B CD1   1 
ATOM   5140 C  CD2   . LEU B 1 180 ? -14.216 11.384  -5.933  1.00 61.34  ? 1397 LEU B CD2   1 
ATOM   5141 N  N     . ASP B 1 181 ? -16.622 7.446   -7.510  1.00 67.95  ? 1398 ASP B N     1 
ATOM   5142 C  CA    . ASP B 1 181 ? -17.915 7.442   -8.176  1.00 75.99  ? 1398 ASP B CA    1 
ATOM   5143 C  C     . ASP B 1 181 ? -18.893 6.546   -7.431  1.00 70.20  ? 1398 ASP B C     1 
ATOM   5144 O  O     . ASP B 1 181 ? -20.049 6.920   -7.214  1.00 71.89  ? 1398 ASP B O     1 
ATOM   5145 C  CB    . ASP B 1 181 ? -17.728 6.977   -9.624  1.00 92.23  ? 1398 ASP B CB    1 
ATOM   5146 C  CG    . ASP B 1 181 ? -18.869 7.378   -10.537 1.00 108.28 ? 1398 ASP B CG    1 
ATOM   5147 O  OD1   . ASP B 1 181 ? -19.868 6.630   -10.617 1.00 103.50 ? 1398 ASP B OD1   1 
ATOM   5148 O  OD2   . ASP B 1 181 ? -18.747 8.434   -11.198 1.00 121.79 ? 1398 ASP B OD2   1 
ATOM   5149 N  N     . LEU B 1 182 ? -18.412 5.406   -6.929  1.00 66.62  ? 1399 LEU B N     1 
ATOM   5150 C  CA    . LEU B 1 182 ? -19.301 4.509   -6.204  1.00 61.79  ? 1399 LEU B CA    1 
ATOM   5151 C  C     . LEU B 1 182 ? -19.750 5.105   -4.877  1.00 69.39  ? 1399 LEU B C     1 
ATOM   5152 O  O     . LEU B 1 182 ? -20.899 4.900   -4.464  1.00 61.43  ? 1399 LEU B O     1 
ATOM   5153 C  CB    . LEU B 1 182 ? -18.598 3.180   -5.931  1.00 59.00  ? 1399 LEU B CB    1 
ATOM   5154 C  CG    . LEU B 1 182 ? -18.428 2.196   -7.077  1.00 58.78  ? 1399 LEU B CG    1 
ATOM   5155 C  CD1   . LEU B 1 182 ? -17.778 0.909   -6.526  1.00 62.67  ? 1399 LEU B CD1   1 
ATOM   5156 C  CD2   . LEU B 1 182 ? -19.764 1.916   -7.721  1.00 45.88  ? 1399 LEU B CD2   1 
ATOM   5157 N  N     . TYR B 1 183 ? -18.860 5.831   -4.196  1.00 71.71  ? 1400 TYR B N     1 
ATOM   5158 C  CA    . TYR B 1 183 ? -19.233 6.469   -2.939  1.00 66.55  ? 1400 TYR B CA    1 
ATOM   5159 C  C     . TYR B 1 183 ? -20.276 7.544   -3.174  1.00 72.09  ? 1400 TYR B C     1 
ATOM   5160 O  O     . TYR B 1 183 ? -21.254 7.654   -2.427  1.00 77.65  ? 1400 TYR B O     1 
ATOM   5161 C  CB    . TYR B 1 183 ? -18.006 7.065   -2.263  1.00 61.63  ? 1400 TYR B CB    1 
ATOM   5162 C  CG    . TYR B 1 183 ? -17.080 6.057   -1.630  1.00 67.84  ? 1400 TYR B CG    1 
ATOM   5163 C  CD1   . TYR B 1 183 ? -17.569 4.896   -1.046  1.00 60.27  ? 1400 TYR B CD1   1 
ATOM   5164 C  CD2   . TYR B 1 183 ? -15.702 6.268   -1.618  1.00 63.85  ? 1400 TYR B CD2   1 
ATOM   5165 C  CE1   . TYR B 1 183 ? -16.717 3.997   -0.455  1.00 58.33  ? 1400 TYR B CE1   1 
ATOM   5166 C  CE2   . TYR B 1 183 ? -14.840 5.362   -1.038  1.00 56.87  ? 1400 TYR B CE2   1 
ATOM   5167 C  CZ    . TYR B 1 183 ? -15.339 4.230   -0.459  1.00 60.61  ? 1400 TYR B CZ    1 
ATOM   5168 O  OH    . TYR B 1 183 ? -14.455 3.340   0.131   1.00 54.48  ? 1400 TYR B OH    1 
ATOM   5169 N  N     . ALA B 1 184 ? -20.047 8.388   -4.177  1.00 78.41  ? 1401 ALA B N     1 
ATOM   5170 C  CA    . ALA B 1 184 ? -21.052 9.388   -4.535  1.00 81.13  ? 1401 ALA B CA    1 
ATOM   5171 C  C     . ALA B 1 184 ? -22.378 8.713   -4.859  1.00 76.95  ? 1401 ALA B C     1 
ATOM   5172 O  O     . ALA B 1 184 ? -23.445 9.239   -4.538  1.00 73.35  ? 1401 ALA B O     1 
ATOM   5173 C  CB    . ALA B 1 184 ? -20.562 10.253  -5.703  1.00 67.05  ? 1401 ALA B CB    1 
ATOM   5174 N  N     . LYS B 1 185 ? -22.329 7.545   -5.506  1.00 75.33  ? 1402 LYS B N     1 
ATOM   5175 C  CA    . LYS B 1 185 ? -23.562 6.826   -5.797  1.00 73.26  ? 1402 LYS B CA    1 
ATOM   5176 C  C     . LYS B 1 185 ? -24.197 6.293   -4.519  1.00 74.54  ? 1402 LYS B C     1 
ATOM   5177 O  O     . LYS B 1 185 ? -25.420 6.310   -4.377  1.00 89.94  ? 1402 LYS B O     1 
ATOM   5178 C  CB    . LYS B 1 185 ? -23.293 5.703   -6.795  1.00 73.41  ? 1402 LYS B CB    1 
ATOM   5179 C  CG    . LYS B 1 185 ? -23.111 6.216   -8.219  1.00 80.41  ? 1402 LYS B CG    1 
ATOM   5180 C  CD    . LYS B 1 185 ? -23.474 5.167   -9.258  1.00 90.28  ? 1402 LYS B CD    1 
ATOM   5181 C  CE    . LYS B 1 185 ? -22.894 5.532   -10.618 1.00 104.52 ? 1402 LYS B CE    1 
ATOM   5182 N  NZ    . LYS B 1 185 ? -22.471 4.306   -11.387 1.00 114.69 ? 1402 LYS B NZ    1 
ATOM   5183 N  N     . VAL B 1 186 ? -23.386 5.825   -3.573  1.00 69.56  ? 1403 VAL B N     1 
ATOM   5184 C  CA    . VAL B 1 186 ? -23.902 5.506   -2.243  1.00 61.34  ? 1403 VAL B CA    1 
ATOM   5185 C  C     . VAL B 1 186 ? -24.652 6.703   -1.671  1.00 68.30  ? 1403 VAL B C     1 
ATOM   5186 O  O     . VAL B 1 186 ? -25.799 6.589   -1.223  1.00 62.91  ? 1403 VAL B O     1 
ATOM   5187 C  CB    . VAL B 1 186 ? -22.759 5.080   -1.311  1.00 57.96  ? 1403 VAL B CB    1 
ATOM   5188 C  CG1   . VAL B 1 186 ? -23.178 5.267   0.131   1.00 53.67  ? 1403 VAL B CG1   1 
ATOM   5189 C  CG2   . VAL B 1 186 ? -22.376 3.649   -1.576  1.00 62.98  ? 1403 VAL B CG2   1 
ATOM   5190 N  N     . TYR B 1 187 ? -24.028 7.888   -1.733  1.00 75.39  ? 1404 TYR B N     1 
ATOM   5191 C  CA    . TYR B 1 187 ? -24.608 9.062   -1.080  1.00 68.37  ? 1404 TYR B CA    1 
ATOM   5192 C  C     . TYR B 1 187 ? -25.864 9.546   -1.804  1.00 64.61  ? 1404 TYR B C     1 
ATOM   5193 O  O     . TYR B 1 187 ? -26.876 9.836   -1.161  1.00 64.90  ? 1404 TYR B O     1 
ATOM   5194 C  CB    . TYR B 1 187 ? -23.555 10.168  -0.946  1.00 62.42  ? 1404 TYR B CB    1 
ATOM   5195 C  CG    . TYR B 1 187 ? -22.907 10.072  0.399   1.00 56.76  ? 1404 TYR B CG    1 
ATOM   5196 C  CD1   . TYR B 1 187 ? -21.693 9.421   0.556   1.00 58.59  ? 1404 TYR B CD1   1 
ATOM   5197 C  CD2   . TYR B 1 187 ? -23.557 10.527  1.532   1.00 59.12  ? 1404 TYR B CD2   1 
ATOM   5198 C  CE1   . TYR B 1 187 ? -21.109 9.265   1.805   1.00 53.76  ? 1404 TYR B CE1   1 
ATOM   5199 C  CE2   . TYR B 1 187 ? -22.986 10.395  2.780   1.00 57.87  ? 1404 TYR B CE2   1 
ATOM   5200 C  CZ    . TYR B 1 187 ? -21.759 9.756   2.912   1.00 59.53  ? 1404 TYR B CZ    1 
ATOM   5201 O  OH    . TYR B 1 187 ? -21.182 9.594   4.152   1.00 57.39  ? 1404 TYR B OH    1 
ATOM   5202 N  N     . THR B 1 188 ? -25.844 9.585   -3.133  1.00 63.81  ? 1405 THR B N     1 
ATOM   5203 C  CA    . THR B 1 188 ? -26.958 10.139  -3.891  1.00 76.19  ? 1405 THR B CA    1 
ATOM   5204 C  C     . THR B 1 188 ? -28.057 9.124   -4.189  1.00 84.67  ? 1405 THR B C     1 
ATOM   5205 O  O     . THR B 1 188 ? -29.241 9.407   -3.983  1.00 85.06  ? 1405 THR B O     1 
ATOM   5206 C  CB    . THR B 1 188 ? -26.450 10.739  -5.211  1.00 73.77  ? 1405 THR B CB    1 
ATOM   5207 O  OG1   . THR B 1 188 ? -25.810 9.716   -5.999  1.00 71.65  ? 1405 THR B OG1   1 
ATOM   5208 C  CG2   . THR B 1 188 ? -25.490 11.889  -4.941  1.00 61.85  ? 1405 THR B CG2   1 
ATOM   5209 N  N     . ASP B 1 189 ? -27.690 7.954   -4.708  1.00 85.90  ? 1406 ASP B N     1 
ATOM   5210 C  CA    . ASP B 1 189 ? -28.658 6.989   -5.214  1.00 79.72  ? 1406 ASP B CA    1 
ATOM   5211 C  C     . ASP B 1 189 ? -29.284 6.166   -4.098  1.00 78.02  ? 1406 ASP B C     1 
ATOM   5212 O  O     . ASP B 1 189 ? -30.445 5.747   -4.219  1.00 87.91  ? 1406 ASP B O     1 
ATOM   5213 C  CB    . ASP B 1 189 ? -27.985 6.090   -6.254  1.00 70.92  ? 1406 ASP B CB    1 
ATOM   5214 C  CG    . ASP B 1 189 ? -27.700 6.824   -7.578  1.00 80.51  ? 1406 ASP B CG    1 
ATOM   5215 O  OD1   . ASP B 1 189 ? -27.991 8.035   -7.690  1.00 89.06  ? 1406 ASP B OD1   1 
ATOM   5216 O  OD2   . ASP B 1 189 ? -27.173 6.187   -8.515  1.00 90.35  ? 1406 ASP B OD2   1 
ATOM   5217 N  N     . LEU B 1 190 ? -28.537 5.916   -3.023  1.00 64.88  ? 1407 LEU B N     1 
ATOM   5218 C  CA    . LEU B 1 190 ? -29.040 5.179   -1.867  1.00 74.08  ? 1407 LEU B CA    1 
ATOM   5219 C  C     . LEU B 1 190 ? -29.487 6.090   -0.734  1.00 77.84  ? 1407 LEU B C     1 
ATOM   5220 O  O     . LEU B 1 190 ? -30.547 5.870   -0.149  1.00 89.51  ? 1407 LEU B O     1 
ATOM   5221 C  CB    . LEU B 1 190 ? -27.974 4.239   -1.315  1.00 78.35  ? 1407 LEU B CB    1 
ATOM   5222 C  CG    . LEU B 1 190 ? -27.670 2.824   -1.791  1.00 70.21  ? 1407 LEU B CG    1 
ATOM   5223 C  CD1   . LEU B 1 190 ? -27.754 2.628   -3.301  1.00 63.18  ? 1407 LEU B CD1   1 
ATOM   5224 C  CD2   . LEU B 1 190 ? -26.277 2.571   -1.299  1.00 61.82  ? 1407 LEU B CD2   1 
ATOM   5225 N  N     . LEU B 1 191 ? -28.693 7.094   -0.397  1.00 70.34  ? 1408 LEU B N     1 
ATOM   5226 C  CA    . LEU B 1 191 ? -29.019 7.969   0.713   1.00 71.38  ? 1408 LEU B CA    1 
ATOM   5227 C  C     . LEU B 1 191 ? -29.670 9.258   0.256   1.00 69.31  ? 1408 LEU B C     1 
ATOM   5228 O  O     . LEU B 1 191 ? -30.078 10.061  1.099   1.00 76.61  ? 1408 LEU B O     1 
ATOM   5229 C  CB    . LEU B 1 191 ? -27.765 8.264   1.545   1.00 74.67  ? 1408 LEU B CB    1 
ATOM   5230 C  CG    . LEU B 1 191 ? -27.280 7.025   2.306   1.00 68.54  ? 1408 LEU B CG    1 
ATOM   5231 C  CD1   . LEU B 1 191 ? -26.223 7.392   3.335   1.00 74.13  ? 1408 LEU B CD1   1 
ATOM   5232 C  CD2   . LEU B 1 191 ? -28.472 6.307   2.958   1.00 62.87  ? 1408 LEU B CD2   1 
ATOM   5233 N  N     . ALA B 1 192 ? -29.824 9.444   -1.053  1.00 66.29  ? 1409 ALA B N     1 
ATOM   5234 C  CA    . ALA B 1 192 ? -30.526 10.597  -1.609  1.00 71.19  ? 1409 ALA B CA    1 
ATOM   5235 C  C     . ALA B 1 192 ? -29.945 11.918  -1.088  1.00 70.83  ? 1409 ALA B C     1 
ATOM   5236 O  O     . ALA B 1 192 ? -30.646 12.913  -0.914  1.00 69.20  ? 1409 ALA B O     1 
ATOM   5237 C  CB    . ALA B 1 192 ? -32.032 10.484  -1.326  1.00 68.98  ? 1409 ALA B CB    1 
ATOM   5238 N  N     . ILE B 1 193 ? -28.639 11.941  -0.889  1.00 72.30  ? 1410 ILE B N     1 
ATOM   5239 C  CA    . ILE B 1 193 ? -27.912 13.112  -0.405  1.00 68.02  ? 1410 ILE B CA    1 
ATOM   5240 C  C     . ILE B 1 193 ? -27.008 13.596  -1.529  1.00 56.64  ? 1410 ILE B C     1 
ATOM   5241 O  O     . ILE B 1 193 ? -26.208 12.809  -2.046  1.00 58.89  ? 1410 ILE B O     1 
ATOM   5242 C  CB    . ILE B 1 193 ? -27.079 12.784  0.846   1.00 66.91  ? 1410 ILE B CB    1 
ATOM   5243 C  CG1   . ILE B 1 193 ? -27.971 12.312  2.002   1.00 53.69  ? 1410 ILE B CG1   1 
ATOM   5244 C  CG2   . ILE B 1 193 ? -26.198 13.971  1.216   1.00 70.63  ? 1410 ILE B CG2   1 
ATOM   5245 C  CD1   . ILE B 1 193 ? -27.156 11.917  3.249   1.00 62.91  ? 1410 ILE B CD1   1 
ATOM   5246 N  N     . PRO B 1 194 ? -27.067 14.858  -1.906  1.00 55.90  ? 1411 PRO B N     1 
ATOM   5247 C  CA    . PRO B 1 194 ? -26.119 15.371  -2.892  1.00 67.43  ? 1411 PRO B CA    1 
ATOM   5248 C  C     . PRO B 1 194 ? -24.750 15.585  -2.266  1.00 69.08  ? 1411 PRO B C     1 
ATOM   5249 O  O     . PRO B 1 194 ? -24.621 15.789  -1.056  1.00 68.60  ? 1411 PRO B O     1 
ATOM   5250 C  CB    . PRO B 1 194 ? -26.757 16.698  -3.319  1.00 64.31  ? 1411 PRO B CB    1 
ATOM   5251 C  CG    . PRO B 1 194 ? -27.490 17.136  -2.125  1.00 59.03  ? 1411 PRO B CG    1 
ATOM   5252 C  CD    . PRO B 1 194 ? -27.979 15.901  -1.426  1.00 58.77  ? 1411 PRO B CD    1 
ATOM   5253 N  N     . VAL B 1 195 ? -23.713 15.481  -3.104  1.00 71.00  ? 1412 VAL B N     1 
ATOM   5254 C  CA    . VAL B 1 195 ? -22.326 15.654  -2.670  1.00 79.97  ? 1412 VAL B CA    1 
ATOM   5255 C  C     . VAL B 1 195 ? -21.514 16.252  -3.813  1.00 79.06  ? 1412 VAL B C     1 
ATOM   5256 O  O     . VAL B 1 195 ? -21.914 16.203  -4.978  1.00 84.12  ? 1412 VAL B O     1 
ATOM   5257 C  CB    . VAL B 1 195 ? -21.668 14.325  -2.213  1.00 79.67  ? 1412 VAL B CB    1 
ATOM   5258 C  CG1   . VAL B 1 195 ? -22.152 13.924  -0.826  1.00 70.10  ? 1412 VAL B CG1   1 
ATOM   5259 C  CG2   . VAL B 1 195 ? -21.911 13.207  -3.233  1.00 79.30  ? 1412 VAL B CG2   1 
ATOM   5260 N  N     . VAL B 1 196 ? -20.319 16.749  -3.480  1.00 70.08  ? 1413 VAL B N     1 
ATOM   5261 C  CA    . VAL B 1 196 ? -19.367 17.288  -4.451  1.00 68.90  ? 1413 VAL B CA    1 
ATOM   5262 C  C     . VAL B 1 196 ? -18.112 16.429  -4.415  1.00 72.22  ? 1413 VAL B C     1 
ATOM   5263 O  O     . VAL B 1 196 ? -17.553 16.175  -3.334  1.00 67.76  ? 1413 VAL B O     1 
ATOM   5264 C  CB    . VAL B 1 196 ? -19.003 18.750  -4.155  1.00 76.02  ? 1413 VAL B CB    1 
ATOM   5265 C  CG1   . VAL B 1 196 ? -20.063 19.694  -4.686  1.00 66.90  ? 1413 VAL B CG1   1 
ATOM   5266 C  CG2   . VAL B 1 196 ? -18.832 18.922  -2.670  1.00 84.49  ? 1413 VAL B CG2   1 
ATOM   5267 N  N     . LYS B 1 197 ? -17.687 15.967  -5.592  1.00 65.18  ? 1414 LYS B N     1 
ATOM   5268 C  CA    . LYS B 1 197 ? -16.465 15.193  -5.723  1.00 54.82  ? 1414 LYS B CA    1 
ATOM   5269 C  C     . LYS B 1 197 ? -15.260 16.135  -5.858  1.00 85.98  ? 1414 LYS B C     1 
ATOM   5270 O  O     . LYS B 1 197 ? -15.291 17.130  -6.599  1.00 69.72  ? 1414 LYS B O     1 
ATOM   5271 C  CB    . LYS B 1 197 ? -16.550 14.268  -6.936  1.00 54.42  ? 1414 LYS B CB    1 
ATOM   5272 C  CG    . LYS B 1 197 ? -17.805 13.352  -7.030  1.00 64.02  ? 1414 LYS B CG    1 
ATOM   5273 C  CD    . LYS B 1 197 ? -17.909 12.681  -8.426  1.00 61.80  ? 1414 LYS B CD    1 
ATOM   5274 C  CE    . LYS B 1 197 ? -18.368 11.204  -8.354  1.00 83.24  ? 1414 LYS B CE    1 
ATOM   5275 N  NZ    . LYS B 1 197 ? -17.732 10.323  -9.410  1.00 82.84  ? 1414 LYS B NZ    1 
ATOM   5276 N  N     . GLY B 1 198 ? -14.188 15.820  -5.145  1.00 81.34  ? 1415 GLY B N     1 
ATOM   5277 C  CA    . GLY B 1 198 ? -13.069 16.730  -5.233  1.00 73.44  ? 1415 GLY B CA    1 
ATOM   5278 C  C     . GLY B 1 198 ? -11.808 16.092  -4.710  1.00 86.13  ? 1415 GLY B C     1 
ATOM   5279 O  O     . GLY B 1 198 ? -11.790 14.932  -4.290  1.00 90.89  ? 1415 GLY B O     1 
ATOM   5280 N  N     . ARG B 1 199 ? -10.749 16.891  -4.744  1.00 86.04  ? 1416 ARG B N     1 
ATOM   5281 C  CA    . ARG B 1 199 ? -9.429  16.527  -4.260  1.00 84.49  ? 1416 ARG B CA    1 
ATOM   5282 C  C     . ARG B 1 199 ? -9.143  17.354  -3.018  1.00 80.64  ? 1416 ARG B C     1 
ATOM   5283 O  O     . ARG B 1 199 ? -9.365  18.568  -3.020  1.00 90.97  ? 1416 ARG B O     1 
ATOM   5284 C  CB    . ARG B 1 199 ? -8.385  16.791  -5.346  1.00 90.65  ? 1416 ARG B CB    1 
ATOM   5285 C  CG    . ARG B 1 199 ? -7.067  16.074  -5.169  1.00 101.67 ? 1416 ARG B CG    1 
ATOM   5286 C  CD    . ARG B 1 199 ? -6.232  16.166  -6.451  1.00 116.33 ? 1416 ARG B CD    1 
ATOM   5287 N  NE    . ARG B 1 199 ? -6.536  15.094  -7.407  1.00 120.67 ? 1416 ARG B NE    1 
ATOM   5288 C  CZ    . ARG B 1 199 ? -5.620  14.417  -8.103  1.00 120.29 ? 1416 ARG B CZ    1 
ATOM   5289 N  NH1   . ARG B 1 199 ? -4.332  14.707  -7.972  1.00 121.13 ? 1416 ARG B NH1   1 
ATOM   5290 N  NH2   . ARG B 1 199 ? -5.993  13.459  -8.943  1.00 116.67 ? 1416 ARG B NH2   1 
ATOM   5291 N  N     . LYS B 1 200 ? -8.727  16.693  -1.941  1.00 71.43  ? 1417 LYS B N     1 
ATOM   5292 C  CA    . LYS B 1 200 ? -8.295  17.427  -0.765  1.00 64.67  ? 1417 LYS B CA    1 
ATOM   5293 C  C     . LYS B 1 200 ? -7.072  18.260  -1.111  1.00 77.16  ? 1417 LYS B C     1 
ATOM   5294 O  O     . LYS B 1 200 ? -6.247  17.875  -1.945  1.00 91.64  ? 1417 LYS B O     1 
ATOM   5295 C  CB    . LYS B 1 200 ? -7.968  16.481  0.392   1.00 66.96  ? 1417 LYS B CB    1 
ATOM   5296 C  CG    . LYS B 1 200 ? -9.111  15.527  0.799   1.00 74.29  ? 1417 LYS B CG    1 
ATOM   5297 C  CD    . LYS B 1 200 ? -10.223 16.253  1.565   1.00 83.31  ? 1417 LYS B CD    1 
ATOM   5298 C  CE    . LYS B 1 200 ? -11.145 15.291  2.312   1.00 85.04  ? 1417 LYS B CE    1 
ATOM   5299 N  NZ    . LYS B 1 200 ? -12.140 15.997  3.179   1.00 88.09  ? 1417 LYS B NZ    1 
ATOM   5300 N  N     . THR B 1 201 ? -6.953  19.415  -0.466  1.00 77.93  ? 1418 THR B N     1 
ATOM   5301 C  CA    . THR B 1 201 ? -5.728  20.166  -0.592  1.00 76.66  ? 1418 THR B CA    1 
ATOM   5302 C  C     . THR B 1 201 ? -4.604  19.405  0.105   1.00 71.85  ? 1418 THR B C     1 
ATOM   5303 O  O     . THR B 1 201 ? -4.828  18.478  0.881   1.00 78.59  ? 1418 THR B O     1 
ATOM   5304 C  CB    . THR B 1 201 ? -5.871  21.554  0.029   1.00 81.89  ? 1418 THR B CB    1 
ATOM   5305 O  OG1   . THR B 1 201 ? -6.235  21.408  1.409   1.00 75.45  ? 1418 THR B OG1   1 
ATOM   5306 C  CG2   . THR B 1 201 ? -6.929  22.382  -0.701  1.00 82.01  ? 1418 THR B CG2   1 
ATOM   5307 N  N     . GLU B 1 202 ? -3.369  19.831  -0.163  1.00 71.41  ? 1419 GLU B N     1 
ATOM   5308 C  CA    . GLU B 1 202 ? -2.245  19.124  0.427   1.00 84.97  ? 1419 GLU B CA    1 
ATOM   5309 C  C     . GLU B 1 202 ? -2.309  19.150  1.948   1.00 83.84  ? 1419 GLU B C     1 
ATOM   5310 O  O     . GLU B 1 202 ? -1.784  18.261  2.616   1.00 89.38  ? 1419 GLU B O     1 
ATOM   5311 C  CB    . GLU B 1 202 ? -0.923  19.689  -0.090  1.00 85.71  ? 1419 GLU B CB    1 
ATOM   5312 C  CG    . GLU B 1 202 ? -0.793  19.475  -1.588  1.00 94.63  ? 1419 GLU B CG    1 
ATOM   5313 C  CD    . GLU B 1 202 ? -0.045  18.184  -1.942  1.00 98.21  ? 1419 GLU B CD    1 
ATOM   5314 O  OE1   . GLU B 1 202 ? 0.670   17.612  -1.081  1.00 100.99 ? 1419 GLU B OE1   1 
ATOM   5315 O  OE2   . GLU B 1 202 ? -0.171  17.740  -3.101  1.00 103.10 ? 1419 GLU B OE2   1 
ATOM   5316 N  N     . LYS B 1 203 ? -2.944  20.154  2.532   1.00 81.02  ? 1420 LYS B N     1 
ATOM   5317 C  CA    . LYS B 1 203 ? -3.072  20.177  3.981   1.00 78.09  ? 1420 LYS B CA    1 
ATOM   5318 C  C     . LYS B 1 203 ? -3.980  19.057  4.461   1.00 78.21  ? 1420 LYS B C     1 
ATOM   5319 O  O     . LYS B 1 203 ? -3.635  18.344  5.407   1.00 78.82  ? 1420 LYS B O     1 
ATOM   5320 C  CB    . LYS B 1 203 ? -3.610  21.543  4.450   1.00 76.40  ? 1420 LYS B CB    1 
ATOM   5321 C  CG    . LYS B 1 203 ? -3.971  21.488  5.916   1.00 74.39  ? 1420 LYS B CG    1 
ATOM   5322 C  CD    . LYS B 1 203 ? -4.627  22.733  6.449   1.00 79.34  ? 1420 LYS B CD    1 
ATOM   5323 C  CE    . LYS B 1 203 ? -5.094  22.509  7.877   1.00 76.46  ? 1420 LYS B CE    1 
ATOM   5324 N  NZ    . LYS B 1 203 ? -4.977  23.767  8.651   1.00 84.74  ? 1420 LYS B NZ    1 
ATOM   5325 N  N     . GLU B 1 204 ? -5.145  18.890  3.826   1.00 83.58  ? 1421 GLU B N     1 
ATOM   5326 C  CA    . GLU B 1 204 ? -6.211  18.011  4.310   1.00 86.07  ? 1421 GLU B CA    1 
ATOM   5327 C  C     . GLU B 1 204 ? -6.165  16.591  3.761   1.00 84.96  ? 1421 GLU B C     1 
ATOM   5328 O  O     . GLU B 1 204 ? -6.919  15.748  4.250   1.00 87.62  ? 1421 GLU B O     1 
ATOM   5329 C  CB    . GLU B 1 204 ? -7.589  18.611  3.969   1.00 86.73  ? 1421 GLU B CB    1 
ATOM   5330 C  CG    . GLU B 1 204 ? -7.931  19.828  4.795   1.00 88.94  ? 1421 GLU B CG    1 
ATOM   5331 C  CD    . GLU B 1 204 ? -8.375  19.454  6.190   1.00 89.61  ? 1421 GLU B CD    1 
ATOM   5332 O  OE1   . GLU B 1 204 ? -9.337  18.665  6.303   1.00 99.52  ? 1421 GLU B OE1   1 
ATOM   5333 O  OE2   . GLU B 1 204 ? -7.759  19.933  7.167   1.00 86.91  ? 1421 GLU B OE2   1 
ATOM   5334 N  N     . LYS B 1 205 ? -5.327  16.307  2.765   1.00 81.95  ? 1422 LYS B N     1 
ATOM   5335 C  CA    . LYS B 1 205 ? -5.150  14.958  2.226   1.00 68.14  ? 1422 LYS B CA    1 
ATOM   5336 C  C     . LYS B 1 205 ? -4.556  14.005  3.263   1.00 75.64  ? 1422 LYS B C     1 
ATOM   5337 O  O     . LYS B 1 205 ? -4.009  14.427  4.285   1.00 78.77  ? 1422 LYS B O     1 
ATOM   5338 C  CB    . LYS B 1 205 ? -4.265  14.975  0.989   1.00 59.24  ? 1422 LYS B CB    1 
ATOM   5339 C  CG    . LYS B 1 205 ? -2.801  15.019  1.310   1.00 60.41  ? 1422 LYS B CG    1 
ATOM   5340 C  CD    . LYS B 1 205 ? -2.048  14.610  0.086   1.00 70.48  ? 1422 LYS B CD    1 
ATOM   5341 C  CE    . LYS B 1 205 ? -0.566  14.688  0.282   1.00 64.80  ? 1422 LYS B CE    1 
ATOM   5342 N  NZ    . LYS B 1 205 ? 0.051   14.657  -1.066  1.00 73.83  ? 1422 LYS B NZ    1 
ATOM   5343 N  N     . PHE B 1 206 ? -4.756  12.694  3.018   1.00 78.42  ? 1423 PHE B N     1 
ATOM   5344 C  CA    . PHE B 1 206 ? -4.082  11.627  3.754   1.00 72.62  ? 1423 PHE B CA    1 
ATOM   5345 C  C     . PHE B 1 206 ? -2.586  11.796  3.696   1.00 79.45  ? 1423 PHE B C     1 
ATOM   5346 O  O     . PHE B 1 206 ? -2.008  11.809  2.602   1.00 77.04  ? 1423 PHE B O     1 
ATOM   5347 C  CB    . PHE B 1 206 ? -4.436  10.263  3.161   1.00 81.15  ? 1423 PHE B CB    1 
ATOM   5348 C  CG    . PHE B 1 206 ? -3.901  9.081   3.953   1.00 83.80  ? 1423 PHE B CG    1 
ATOM   5349 C  CD1   . PHE B 1 206 ? -4.040  9.026   5.331   1.00 83.56  ? 1423 PHE B CD1   1 
ATOM   5350 C  CD2   . PHE B 1 206 ? -3.282  8.016   3.313   1.00 89.40  ? 1423 PHE B CD2   1 
ATOM   5351 C  CE1   . PHE B 1 206 ? -3.571  7.937   6.058   1.00 79.70  ? 1423 PHE B CE1   1 
ATOM   5352 C  CE2   . PHE B 1 206 ? -2.813  6.919   4.036   1.00 89.88  ? 1423 PHE B CE2   1 
ATOM   5353 C  CZ    . PHE B 1 206 ? -2.960  6.885   5.410   1.00 84.85  ? 1423 PHE B CZ    1 
ATOM   5354 N  N     . ALA B 1 207 ? -1.968  11.854  4.881   1.00 87.82  ? 1424 ALA B N     1 
ATOM   5355 C  CA    . ALA B 1 207 ? -0.549  12.200  5.000   1.00 90.04  ? 1424 ALA B CA    1 
ATOM   5356 C  C     . ALA B 1 207 ? 0.339   11.245  4.207   1.00 95.91  ? 1424 ALA B C     1 
ATOM   5357 O  O     . ALA B 1 207 ? 1.246   11.671  3.485   1.00 100.52 ? 1424 ALA B O     1 
ATOM   5358 C  CB    . ALA B 1 207 ? -0.131  12.206  6.474   1.00 78.19  ? 1424 ALA B CB    1 
ATOM   5359 N  N     . GLY B 1 208 ? 0.084   9.949   4.310   1.00 97.40  ? 1425 GLY B N     1 
ATOM   5360 C  CA    . GLY B 1 208 ? 0.979   9.046   3.615   1.00 103.89 ? 1425 GLY B CA    1 
ATOM   5361 C  C     . GLY B 1 208 ? 0.773   8.939   2.120   1.00 106.55 ? 1425 GLY B C     1 
ATOM   5362 O  O     . GLY B 1 208 ? 1.606   8.332   1.440   1.00 121.21 ? 1425 GLY B O     1 
ATOM   5363 N  N     . GLY B 1 209 ? -0.307  9.510   1.591   1.00 93.82  ? 1426 GLY B N     1 
ATOM   5364 C  CA    . GLY B 1 209 ? -0.621  9.368   0.186   1.00 78.85  ? 1426 GLY B CA    1 
ATOM   5365 C  C     . GLY B 1 209 ? -0.003  10.439  -0.701  1.00 77.54  ? 1426 GLY B C     1 
ATOM   5366 O  O     . GLY B 1 209 ? 0.472   11.475  -0.241  1.00 74.12  ? 1426 GLY B O     1 
ATOM   5367 N  N     . ASP B 1 210 ? -0.027  10.152  -2.004  1.00 79.86  ? 1427 ASP B N     1 
ATOM   5368 C  CA    . ASP B 1 210 ? 0.182   11.174  -3.024  1.00 75.50  ? 1427 ASP B CA    1 
ATOM   5369 C  C     . ASP B 1 210 ? -0.970  12.179  -3.002  1.00 87.49  ? 1427 ASP B C     1 
ATOM   5370 O  O     . ASP B 1 210 ? -0.755  13.391  -2.850  1.00 88.75  ? 1427 ASP B O     1 
ATOM   5371 C  CB    . ASP B 1 210 ? 0.298   10.495  -4.397  1.00 72.64  ? 1427 ASP B CB    1 
ATOM   5372 C  CG    . ASP B 1 210 ? 0.740   11.442  -5.521  1.00 94.01  ? 1427 ASP B CG    1 
ATOM   5373 O  OD1   . ASP B 1 210 ? 0.917   10.944  -6.660  1.00 94.57  ? 1427 ASP B OD1   1 
ATOM   5374 O  OD2   . ASP B 1 210 ? 0.909   12.663  -5.288  1.00 105.36 ? 1427 ASP B OD2   1 
ATOM   5375 N  N     . TYR B 1 211 ? -2.206  11.687  -3.140  1.00 81.85  ? 1428 TYR B N     1 
ATOM   5376 C  CA    . TYR B 1 211 ? -3.379  12.540  -3.058  1.00 77.04  ? 1428 TYR B CA    1 
ATOM   5377 C  C     . TYR B 1 211 ? -4.546  11.735  -2.523  1.00 84.08  ? 1428 TYR B C     1 
ATOM   5378 O  O     . TYR B 1 211 ? -4.467  10.518  -2.364  1.00 91.57  ? 1428 TYR B O     1 
ATOM   5379 C  CB    . TYR B 1 211 ? -3.738  13.174  -4.408  1.00 72.46  ? 1428 TYR B CB    1 
ATOM   5380 C  CG    . TYR B 1 211 ? -4.072  12.194  -5.487  1.00 77.29  ? 1428 TYR B CG    1 
ATOM   5381 C  CD1   . TYR B 1 211 ? -5.345  11.656  -5.593  1.00 86.95  ? 1428 TYR B CD1   1 
ATOM   5382 C  CD2   . TYR B 1 211 ? -3.116  11.806  -6.413  1.00 77.05  ? 1428 TYR B CD2   1 
ATOM   5383 C  CE1   . TYR B 1 211 ? -5.656  10.742  -6.586  1.00 92.33  ? 1428 TYR B CE1   1 
ATOM   5384 C  CE2   . TYR B 1 211 ? -3.415  10.896  -7.410  1.00 85.63  ? 1428 TYR B CE2   1 
ATOM   5385 C  CZ    . TYR B 1 211 ? -4.689  10.364  -7.496  1.00 91.35  ? 1428 TYR B CZ    1 
ATOM   5386 O  OH    . TYR B 1 211 ? -4.993  9.451   -8.490  1.00 87.38  ? 1428 TYR B OH    1 
ATOM   5387 N  N     . THR B 1 212 ? -5.628  12.457  -2.236  1.00 85.83  ? 1429 THR B N     1 
ATOM   5388 C  CA    . THR B 1 212 ? -6.834  11.946  -1.592  1.00 78.59  ? 1429 THR B CA    1 
ATOM   5389 C  C     . THR B 1 212 ? -8.044  12.545  -2.308  1.00 83.18  ? 1429 THR B C     1 
ATOM   5390 O  O     . THR B 1 212 ? -8.186  13.774  -2.343  1.00 86.05  ? 1429 THR B O     1 
ATOM   5391 C  CB    . THR B 1 212 ? -6.861  12.347  -0.106  1.00 68.49  ? 1429 THR B CB    1 
ATOM   5392 O  OG1   . THR B 1 212 ? -5.846  11.655  0.634   1.00 64.00  ? 1429 THR B OG1   1 
ATOM   5393 C  CG2   . THR B 1 212 ? -8.225  12.080  0.504   1.00 66.30  ? 1429 THR B CG2   1 
ATOM   5394 N  N     . THR B 1 213 ? -8.889  11.711  -2.924  1.00 81.19  ? 1430 THR B N     1 
ATOM   5395 C  CA    . THR B 1 213 ? -10.157 12.232  -3.434  1.00 75.33  ? 1430 THR B CA    1 
ATOM   5396 C  C     . THR B 1 213 ? -11.236 12.017  -2.387  1.00 68.71  ? 1430 THR B C     1 
ATOM   5397 O  O     . THR B 1 213 ? -11.079 11.202  -1.470  1.00 69.45  ? 1430 THR B O     1 
ATOM   5398 C  CB    . THR B 1 213 ? -10.582 11.597  -4.754  1.00 72.66  ? 1430 THR B CB    1 
ATOM   5399 O  OG1   . THR B 1 213 ? -10.910 10.225  -4.550  1.00 66.66  ? 1430 THR B OG1   1 
ATOM   5400 C  CG2   . THR B 1 213 ? -9.485  11.709  -5.773  1.00 81.95  ? 1430 THR B CG2   1 
ATOM   5401 N  N     . THR B 1 214 ? -12.346 12.742  -2.543  1.00 62.64  ? 1431 THR B N     1 
ATOM   5402 C  CA    . THR B 1 214 ? -13.357 12.787  -1.493  1.00 67.49  ? 1431 THR B CA    1 
ATOM   5403 C  C     . THR B 1 214 ? -14.698 13.214  -2.073  1.00 70.91  ? 1431 THR B C     1 
ATOM   5404 O  O     . THR B 1 214 ? -14.770 13.815  -3.150  1.00 74.51  ? 1431 THR B O     1 
ATOM   5405 C  CB    . THR B 1 214 ? -12.910 13.745  -0.374  1.00 75.24  ? 1431 THR B CB    1 
ATOM   5406 O  OG1   . THR B 1 214 ? -13.840 13.727  0.714   1.00 83.78  ? 1431 THR B OG1   1 
ATOM   5407 C  CG2   . THR B 1 214 ? -12.783 15.183  -0.909  1.00 74.76  ? 1431 THR B CG2   1 
ATOM   5408 N  N     . VAL B 1 215 ? -15.765 12.852  -1.357  1.00 76.59  ? 1432 VAL B N     1 
ATOM   5409 C  CA    . VAL B 1 215 ? -17.098 13.429  -1.537  1.00 77.99  ? 1432 VAL B CA    1 
ATOM   5410 C  C     . VAL B 1 215 ? -17.461 14.230  -0.288  1.00 74.18  ? 1432 VAL B C     1 
ATOM   5411 O  O     . VAL B 1 215 ? -17.259 13.766  0.841   1.00 60.12  ? 1432 VAL B O     1 
ATOM   5412 C  CB    . VAL B 1 215 ? -18.165 12.358  -1.838  1.00 72.31  ? 1432 VAL B CB    1 
ATOM   5413 C  CG1   . VAL B 1 215 ? -17.975 11.826  -3.248  1.00 71.07  ? 1432 VAL B CG1   1 
ATOM   5414 C  CG2   . VAL B 1 215 ? -18.155 11.228  -0.787  1.00 66.29  ? 1432 VAL B CG2   1 
ATOM   5415 N  N     . GLU B 1 216 ? -17.962 15.447  -0.480  1.00 82.65  ? 1433 GLU B N     1 
ATOM   5416 C  CA    . GLU B 1 216 ? -18.386 16.258  0.654   1.00 74.87  ? 1433 GLU B CA    1 
ATOM   5417 C  C     . GLU B 1 216 ? -19.877 16.550  0.547   1.00 68.71  ? 1433 GLU B C     1 
ATOM   5418 O  O     . GLU B 1 216 ? -20.400 16.774  -0.556  1.00 63.83  ? 1433 GLU B O     1 
ATOM   5419 C  CB    . GLU B 1 216 ? -17.580 17.562  0.754   1.00 79.22  ? 1433 GLU B CB    1 
ATOM   5420 C  CG    . GLU B 1 216 ? -16.068 17.375  0.781   1.00 78.73  ? 1433 GLU B CG    1 
ATOM   5421 C  CD    . GLU B 1 216 ? -15.485 17.242  2.184   1.00 85.55  ? 1433 GLU B CD    1 
ATOM   5422 O  OE1   . GLU B 1 216 ? -14.529 16.452  2.343   1.00 93.94  ? 1433 GLU B OE1   1 
ATOM   5423 O  OE2   . GLU B 1 216 ? -15.949 17.929  3.121   1.00 81.46  ? 1433 GLU B OE2   1 
ATOM   5424 N  N     . ALA B 1 217 ? -20.548 16.533  1.707   1.00 64.97  ? 1434 ALA B N     1 
ATOM   5425 C  CA    . ALA B 1 217 ? -21.974 16.795  1.814   1.00 73.84  ? 1434 ALA B CA    1 
ATOM   5426 C  C     . ALA B 1 217 ? -22.212 17.911  2.822   1.00 80.39  ? 1434 ALA B C     1 
ATOM   5427 O  O     . ALA B 1 217 ? -21.344 18.218  3.645   1.00 78.90  ? 1434 ALA B O     1 
ATOM   5428 C  CB    . ALA B 1 217 ? -22.747 15.548  2.239   1.00 84.05  ? 1434 ALA B CB    1 
ATOM   5429 N  N     . TYR B 1 218 ? -23.423 18.494  2.771   1.00 80.38  ? 1435 TYR B N     1 
ATOM   5430 C  CA    . TYR B 1 218 ? -23.773 19.679  3.547   1.00 76.95  ? 1435 TYR B CA    1 
ATOM   5431 C  C     . TYR B 1 218 ? -24.958 19.389  4.452   1.00 75.51  ? 1435 TYR B C     1 
ATOM   5432 O  O     . TYR B 1 218 ? -26.001 18.910  3.984   1.00 82.17  ? 1435 TYR B O     1 
ATOM   5433 C  CB    . TYR B 1 218 ? -24.106 20.844  2.602   1.00 93.06  ? 1435 TYR B CB    1 
ATOM   5434 C  CG    . TYR B 1 218 ? -24.448 22.175  3.251   1.00 107.87 ? 1435 TYR B CG    1 
ATOM   5435 C  CD1   . TYR B 1 218 ? -25.612 22.861  2.904   1.00 113.80 ? 1435 TYR B CD1   1 
ATOM   5436 C  CD2   . TYR B 1 218 ? -23.601 22.759  4.188   1.00 111.50 ? 1435 TYR B CD2   1 
ATOM   5437 C  CE1   . TYR B 1 218 ? -25.930 24.086  3.487   1.00 119.65 ? 1435 TYR B CE1   1 
ATOM   5438 C  CE2   . TYR B 1 218 ? -23.909 23.977  4.777   1.00 113.49 ? 1435 TYR B CE2   1 
ATOM   5439 C  CZ    . TYR B 1 218 ? -25.071 24.635  4.425   1.00 116.67 ? 1435 TYR B CZ    1 
ATOM   5440 O  OH    . TYR B 1 218 ? -25.366 25.845  5.011   1.00 112.05 ? 1435 TYR B OH    1 
ATOM   5441 N  N     . ILE B 1 219 ? -24.799 19.695  5.741   1.00 64.58  ? 1436 ILE B N     1 
ATOM   5442 C  CA    . ILE B 1 219 ? -25.890 19.684  6.709   1.00 68.77  ? 1436 ILE B CA    1 
ATOM   5443 C  C     . ILE B 1 219 ? -26.293 21.138  6.965   1.00 77.30  ? 1436 ILE B C     1 
ATOM   5444 O  O     . ILE B 1 219 ? -25.506 21.924  7.512   1.00 73.11  ? 1436 ILE B O     1 
ATOM   5445 C  CB    . ILE B 1 219 ? -25.476 18.968  8.007   1.00 58.72  ? 1436 ILE B CB    1 
ATOM   5446 N  N     . SER B 1 220 ? -27.516 21.504  6.569   1.00 80.51  ? 1437 SER B N     1 
ATOM   5447 C  CA    . SER B 1 220 ? -27.960 22.895  6.647   1.00 73.13  ? 1437 SER B CA    1 
ATOM   5448 C  C     . SER B 1 220 ? -28.341 23.348  8.056   1.00 90.06  ? 1437 SER B C     1 
ATOM   5449 O  O     . SER B 1 220 ? -28.215 24.541  8.372   1.00 100.44 ? 1437 SER B O     1 
ATOM   5450 C  CB    . SER B 1 220 ? -29.141 23.117  5.727   1.00 69.81  ? 1437 SER B CB    1 
ATOM   5451 O  OG    . SER B 1 220 ? -30.291 22.405  6.157   1.00 83.98  ? 1437 SER B OG    1 
ATOM   5452 N  N     . ALA B 1 221 ? -28.886 22.449  8.876   1.00 100.18 ? 1438 ALA B N     1 
ATOM   5453 C  CA    . ALA B 1 221 ? -29.221 22.789  10.251  1.00 103.66 ? 1438 ALA B CA    1 
ATOM   5454 C  C     . ALA B 1 221 ? -28.022 23.424  10.952  1.00 114.33 ? 1438 ALA B C     1 
ATOM   5455 O  O     . ALA B 1 221 ? -28.129 24.492  11.564  1.00 124.17 ? 1438 ALA B O     1 
ATOM   5456 C  CB    . ALA B 1 221 ? -29.677 21.535  11.000  1.00 91.32  ? 1438 ALA B CB    1 
ATOM   5457 N  N     . SER B 1 222 ? -26.871 22.766  10.878  1.00 109.42 ? 1439 SER B N     1 
ATOM   5458 C  CA    . SER B 1 222 ? -25.606 23.305  11.363  1.00 98.54  ? 1439 SER B CA    1 
ATOM   5459 C  C     . SER B 1 222 ? -25.006 24.389  10.475  1.00 103.17 ? 1439 SER B C     1 
ATOM   5460 O  O     . SER B 1 222 ? -24.255 25.228  10.971  1.00 108.77 ? 1439 SER B O     1 
ATOM   5461 C  CB    . SER B 1 222 ? -24.598 22.143  11.491  1.00 96.52  ? 1439 SER B CB    1 
ATOM   5462 O  OG    . SER B 1 222 ? -24.209 21.625  10.212  1.00 94.29  ? 1439 SER B OG    1 
ATOM   5463 N  N     . GLY B 1 223 ? -25.314 24.377  9.185   1.00 104.51 ? 1440 GLY B N     1 
ATOM   5464 C  CA    . GLY B 1 223 ? -24.589 25.188  8.241   1.00 88.47  ? 1440 GLY B CA    1 
ATOM   5465 C  C     . GLY B 1 223 ? -23.225 24.618  7.903   1.00 90.59  ? 1440 GLY B C     1 
ATOM   5466 O  O     . GLY B 1 223 ? -22.404 25.296  7.272   1.00 87.59  ? 1440 GLY B O     1 
ATOM   5467 N  N     . ARG B 1 224 ? -22.981 23.349  8.220   1.00 99.50  ? 1441 ARG B N     1 
ATOM   5468 C  CA    . ARG B 1 224 ? -21.635 22.791  8.180   1.00 102.68 ? 1441 ARG B CA    1 
ATOM   5469 C  C     . ARG B 1 224 ? -21.538 21.625  7.208   1.00 110.02 ? 1441 ARG B C     1 
ATOM   5470 O  O     . ARG B 1 224 ? -22.495 20.867  6.993   1.00 115.68 ? 1441 ARG B O     1 
ATOM   5471 C  CB    . ARG B 1 224 ? -21.170 22.305  9.582   1.00 89.11  ? 1441 ARG B CB    1 
ATOM   5472 C  CG    . ARG B 1 224 ? -21.123 23.406  10.636  1.00 88.98  ? 1441 ARG B CG    1 
ATOM   5473 C  CD    . ARG B 1 224 ? -20.109 23.176  11.771  1.00 87.34  ? 1441 ARG B CD    1 
ATOM   5474 N  NE    . ARG B 1 224 ? -19.644 24.475  12.302  1.00 87.51  ? 1441 ARG B NE    1 
ATOM   5475 C  CZ    . ARG B 1 224 ? -19.247 24.680  13.555  1.00 86.99  ? 1441 ARG B CZ    1 
ATOM   5476 N  NH1   . ARG B 1 224 ? -19.263 23.678  14.418  1.00 99.09  ? 1441 ARG B NH1   1 
ATOM   5477 N  NH2   . ARG B 1 224 ? -18.853 25.875  13.952  1.00 88.44  ? 1441 ARG B NH2   1 
ATOM   5478 N  N     . ALA B 1 225 ? -20.336 21.472  6.670   1.00 102.79 ? 1442 ALA B N     1 
ATOM   5479 C  CA    . ALA B 1 225 ? -20.014 20.430  5.715   1.00 102.50 ? 1442 ALA B CA    1 
ATOM   5480 C  C     . ALA B 1 225 ? -19.320 19.251  6.402   1.00 92.23  ? 1442 ALA B C     1 
ATOM   5481 O  O     . ALA B 1 225 ? -18.757 19.367  7.493   1.00 111.99 ? 1442 ALA B O     1 
ATOM   5482 C  CB    . ALA B 1 225 ? -19.131 21.012  4.609   1.00 101.84 ? 1442 ALA B CB    1 
ATOM   5483 N  N     . ILE B 1 226 ? -19.393 18.093  5.763   1.00 81.21  ? 1443 ILE B N     1 
ATOM   5484 C  CA    . ILE B 1 226 ? -18.778 16.907  6.341   1.00 76.25  ? 1443 ILE B CA    1 
ATOM   5485 C  C     . ILE B 1 226 ? -18.329 16.009  5.203   1.00 70.39  ? 1443 ILE B C     1 
ATOM   5486 O  O     . ILE B 1 226 ? -18.942 15.983  4.126   1.00 70.82  ? 1443 ILE B O     1 
ATOM   5487 C  CB    . ILE B 1 226 ? -19.708 16.174  7.337   1.00 68.83  ? 1443 ILE B CB    1 
ATOM   5488 C  CG1   . ILE B 1 226 ? -18.917 15.106  8.119   1.00 80.32  ? 1443 ILE B CG1   1 
ATOM   5489 C  CG2   . ILE B 1 226 ? -20.872 15.559  6.618   1.00 56.98  ? 1443 ILE B CG2   1 
ATOM   5490 C  CD1   . ILE B 1 226 ? -19.749 14.236  9.062   1.00 81.63  ? 1443 ILE B CD1   1 
ATOM   5491 N  N     . GLN B 1 227 ? -17.184 15.354  5.439   1.00 60.90  ? 1444 GLN B N     1 
ATOM   5492 C  CA    . GLN B 1 227 ? -16.551 14.400  4.539   1.00 62.03  ? 1444 GLN B CA    1 
ATOM   5493 C  C     . GLN B 1 227 ? -17.270 13.051  4.603   1.00 75.82  ? 1444 GLN B C     1 
ATOM   5494 O  O     . GLN B 1 227 ? -17.273 12.395  5.652   1.00 73.90  ? 1444 GLN B O     1 
ATOM   5495 C  CB    . GLN B 1 227 ? -15.096 14.280  4.970   1.00 62.83  ? 1444 GLN B CB    1 
ATOM   5496 C  CG    . GLN B 1 227 ? -14.156 13.540  4.074   1.00 75.61  ? 1444 GLN B CG    1 
ATOM   5497 C  CD    . GLN B 1 227 ? -13.065 12.894  4.895   1.00 98.99  ? 1444 GLN B CD    1 
ATOM   5498 O  OE1   . GLN B 1 227 ? -13.136 12.860  6.120   1.00 113.39 ? 1444 GLN B OE1   1 
ATOM   5499 N  NE2   . GLN B 1 227 ? -12.055 12.389  4.237   1.00 100.51 ? 1444 GLN B NE2   1 
ATOM   5500 N  N     . GLY B 1 228 ? -17.811 12.600  3.472   1.00 84.39  ? 1445 GLY B N     1 
ATOM   5501 C  CA    . GLY B 1 228 ? -18.646 11.420  3.461   1.00 80.22  ? 1445 GLY B CA    1 
ATOM   5502 C  C     . GLY B 1 228 ? -17.921 10.117  3.210   1.00 77.70  ? 1445 GLY B C     1 
ATOM   5503 O  O     . GLY B 1 228 ? -18.364 9.075   3.702   1.00 84.90  ? 1445 GLY B O     1 
ATOM   5504 N  N     . ALA B 1 229 ? -16.824 10.156  2.455   1.00 70.16  ? 1446 ALA B N     1 
ATOM   5505 C  CA    . ALA B 1 229 ? -16.005 8.978   2.154   1.00 70.01  ? 1446 ALA B CA    1 
ATOM   5506 C  C     . ALA B 1 229 ? -14.685 9.454   1.558   1.00 73.18  ? 1446 ALA B C     1 
ATOM   5507 O  O     . ALA B 1 229 ? -14.532 10.626  1.199   1.00 74.82  ? 1446 ALA B O     1 
ATOM   5508 C  CB    . ALA B 1 229 ? -16.707 8.003   1.198   1.00 46.58  ? 1446 ALA B CB    1 
ATOM   5509 N  N     . THR B 1 230 ? -13.726 8.532   1.452   1.00 75.32  ? 1447 THR B N     1 
ATOM   5510 C  CA    . THR B 1 230 ? -12.467 8.863   0.791   1.00 70.77  ? 1447 THR B CA    1 
ATOM   5511 C  C     . THR B 1 230 ? -11.902 7.717   -0.010  1.00 62.01  ? 1447 THR B C     1 
ATOM   5512 O  O     . THR B 1 230 ? -12.081 6.550   0.317   1.00 74.02  ? 1447 THR B O     1 
ATOM   5513 C  CB    . THR B 1 230 ? -11.376 9.240   1.765   1.00 65.12  ? 1447 THR B CB    1 
ATOM   5514 O  OG1   . THR B 1 230 ? -11.510 8.431   2.944   1.00 68.92  ? 1447 THR B OG1   1 
ATOM   5515 C  CG2   . THR B 1 230 ? -11.456 10.707  2.042   1.00 62.27  ? 1447 THR B CG2   1 
ATOM   5516 N  N     . SER B 1 231 ? -11.077 8.098   -0.971  1.00 58.55  ? 1448 SER B N     1 
ATOM   5517 C  CA    . SER B 1 231 ? -10.430 7.176   -1.896  1.00 58.23  ? 1448 SER B CA    1 
ATOM   5518 C  C     . SER B 1 231 ? -9.065  7.781   -2.238  1.00 65.30  ? 1448 SER B C     1 
ATOM   5519 O  O     . SER B 1 231 ? -8.998  8.749   -3.008  1.00 67.58  ? 1448 SER B O     1 
ATOM   5520 C  CB    . SER B 1 231 ? -11.308 6.996   -3.135  1.00 58.28  ? 1448 SER B CB    1 
ATOM   5521 O  OG    . SER B 1 231 ? -10.586 6.469   -4.233  1.00 68.64  ? 1448 SER B OG    1 
ATOM   5522 N  N     . HIS B 1 232 ? -7.981  7.203   -1.687  1.00 61.11  ? 1449 HIS B N     1 
ATOM   5523 C  CA    . HIS B 1 232 ? -6.630  7.770   -1.741  1.00 61.76  ? 1449 HIS B CA    1 
ATOM   5524 C  C     . HIS B 1 232 ? -5.761  7.150   -2.831  1.00 63.45  ? 1449 HIS B C     1 
ATOM   5525 O  O     . HIS B 1 232 ? -5.894  5.972   -3.166  1.00 64.75  ? 1449 HIS B O     1 
ATOM   5526 C  CB    . HIS B 1 232 ? -5.886  7.586   -0.413  1.00 62.01  ? 1449 HIS B CB    1 
ATOM   5527 C  CG    . HIS B 1 232 ? -6.720  7.822   0.810   1.00 75.20  ? 1449 HIS B CG    1 
ATOM   5528 N  ND1   . HIS B 1 232 ? -6.941  9.081   1.334   1.00 75.80  ? 1449 HIS B ND1   1 
ATOM   5529 C  CD2   . HIS B 1 232 ? -7.339  6.953   1.647   1.00 74.21  ? 1449 HIS B CD2   1 
ATOM   5530 C  CE1   . HIS B 1 232 ? -7.684  8.979   2.423   1.00 76.77  ? 1449 HIS B CE1   1 
ATOM   5531 N  NE2   . HIS B 1 232 ? -7.938  7.699   2.635   1.00 79.19  ? 1449 HIS B NE2   1 
ATOM   5532 N  N     . HIS B 1 233 ? -4.813  7.931   -3.339  1.00 69.39  ? 1450 HIS B N     1 
ATOM   5533 C  CA    . HIS B 1 233 ? -3.722  7.364   -4.126  1.00 80.53  ? 1450 HIS B CA    1 
ATOM   5534 C  C     . HIS B 1 233 ? -2.439  7.457   -3.311  1.00 82.37  ? 1450 HIS B C     1 
ATOM   5535 O  O     . HIS B 1 233 ? -1.872  8.541   -3.156  1.00 95.57  ? 1450 HIS B O     1 
ATOM   5536 C  CB    . HIS B 1 233 ? -3.543  8.039   -5.479  1.00 88.35  ? 1450 HIS B CB    1 
ATOM   5537 C  CG    . HIS B 1 233 ? -2.411  7.457   -6.273  1.00 97.79  ? 1450 HIS B CG    1 
ATOM   5538 N  ND1   . HIS B 1 233 ? -2.348  6.120   -6.607  1.00 97.48  ? 1450 HIS B ND1   1 
ATOM   5539 C  CD2   . HIS B 1 233 ? -1.277  8.015   -6.759  1.00 101.23 ? 1450 HIS B CD2   1 
ATOM   5540 C  CE1   . HIS B 1 233 ? -1.240  5.886   -7.286  1.00 98.06  ? 1450 HIS B CE1   1 
ATOM   5541 N  NE2   . HIS B 1 233 ? -0.572  7.020   -7.391  1.00 101.14 ? 1450 HIS B NE2   1 
ATOM   5542 N  N     . LEU B 1 234 ? -1.998  6.321   -2.784  1.00 73.79  ? 1451 LEU B N     1 
ATOM   5543 C  CA    . LEU B 1 234 ? -0.762  6.248   -2.023  1.00 75.97  ? 1451 LEU B CA    1 
ATOM   5544 C  C     . LEU B 1 234 ? 0.470   6.249   -2.921  1.00 77.17  ? 1451 LEU B C     1 
ATOM   5545 O  O     . LEU B 1 234 ? 1.600   6.386   -2.417  1.00 58.90  ? 1451 LEU B O     1 
ATOM   5546 C  CB    . LEU B 1 234 ? -0.775  4.990   -1.160  1.00 78.54  ? 1451 LEU B CB    1 
ATOM   5547 C  CG    . LEU B 1 234 ? -2.095  4.655   -0.461  1.00 78.29  ? 1451 LEU B CG    1 
ATOM   5548 C  CD1   . LEU B 1 234 ? -2.001  3.278   0.182   1.00 67.51  ? 1451 LEU B CD1   1 
ATOM   5549 C  CD2   . LEU B 1 234 ? -2.445  5.735   0.573   1.00 76.17  ? 1451 LEU B CD2   1 
ATOM   5550 N  N     . GLY B 1 235 ? 0.278   6.000   -4.217  1.00 77.08  ? 1452 GLY B N     1 
ATOM   5551 C  CA    . GLY B 1 235 ? 1.406   6.024   -5.134  1.00 69.78  ? 1452 GLY B CA    1 
ATOM   5552 C  C     . GLY B 1 235 ? 2.413   4.951   -4.771  1.00 83.28  ? 1452 GLY B C     1 
ATOM   5553 O  O     . GLY B 1 235 ? 2.066   3.785   -4.534  1.00 77.09  ? 1452 GLY B O     1 
ATOM   5554 N  N     . GLN B 1 236 ? 3.681   5.353   -4.687  1.00 87.45  ? 1453 GLN B N     1 
ATOM   5555 C  CA    . GLN B 1 236 ? 4.766   4.440   -4.359  1.00 86.47  ? 1453 GLN B CA    1 
ATOM   5556 C  C     . GLN B 1 236 ? 5.290   4.659   -2.949  1.00 82.29  ? 1453 GLN B C     1 
ATOM   5557 O  O     . GLN B 1 236 ? 6.335   4.104   -2.592  1.00 80.41  ? 1453 GLN B O     1 
ATOM   5558 C  CB    . GLN B 1 236 ? 5.903   4.574   -5.369  1.00 91.70  ? 1453 GLN B CB    1 
ATOM   5559 C  CG    . GLN B 1 236 ? 5.926   3.501   -6.429  1.00 96.34  ? 1453 GLN B CG    1 
ATOM   5560 C  CD    . GLN B 1 236 ? 6.989   3.770   -7.465  1.00 108.37 ? 1453 GLN B CD    1 
ATOM   5561 O  OE1   . GLN B 1 236 ? 7.692   4.777   -7.396  1.00 111.47 ? 1453 GLN B OE1   1 
ATOM   5562 N  NE2   . GLN B 1 236 ? 7.107   2.879   -8.439  1.00 116.14 ? 1453 GLN B NE2   1 
ATOM   5563 N  N     . ASN B 1 237 ? 4.589   5.457   -2.142  1.00 77.83  ? 1454 ASN B N     1 
ATOM   5564 C  CA    . ASN B 1 237 ? 5.073   5.780   -0.806  1.00 83.99  ? 1454 ASN B CA    1 
ATOM   5565 C  C     . ASN B 1 237 ? 5.052   4.556   0.095   1.00 88.00  ? 1454 ASN B C     1 
ATOM   5566 O  O     . ASN B 1 237 ? 6.060   4.221   0.734   1.00 100.30 ? 1454 ASN B O     1 
ATOM   5567 C  CB    . ASN B 1 237 ? 4.243   6.918   -0.204  1.00 85.99  ? 1454 ASN B CB    1 
ATOM   5568 C  CG    . ASN B 1 237 ? 4.266   8.172   -1.065  1.00 83.43  ? 1454 ASN B CG    1 
ATOM   5569 O  OD1   . ASN B 1 237 ? 5.277   8.478   -1.699  1.00 88.32  ? 1454 ASN B OD1   1 
ATOM   5570 N  ND2   . ASN B 1 237 ? 3.146   8.893   -1.105  1.00 72.62  ? 1454 ASN B ND2   1 
ATOM   5571 N  N     . PHE B 1 238 ? 3.921   3.856   0.142   1.00 91.27  ? 1455 PHE B N     1 
ATOM   5572 C  CA    . PHE B 1 238 ? 3.816   2.728   1.062   1.00 91.86  ? 1455 PHE B CA    1 
ATOM   5573 C  C     . PHE B 1 238 ? 4.547   1.489   0.562   1.00 86.63  ? 1455 PHE B C     1 
ATOM   5574 O  O     . PHE B 1 238 ? 5.060   0.712   1.379   1.00 76.37  ? 1455 PHE B O     1 
ATOM   5575 C  CB    . PHE B 1 238 ? 2.357   2.415   1.321   1.00 86.69  ? 1455 PHE B CB    1 
ATOM   5576 C  CG    . PHE B 1 238 ? 1.769   3.240   2.398   1.00 82.64  ? 1455 PHE B CG    1 
ATOM   5577 C  CD1   . PHE B 1 238 ? 1.092   4.399   2.095   1.00 87.76  ? 1455 PHE B CD1   1 
ATOM   5578 C  CD2   . PHE B 1 238 ? 1.910   2.870   3.720   1.00 83.19  ? 1455 PHE B CD2   1 
ATOM   5579 C  CE1   . PHE B 1 238 ? 0.547   5.165   3.090   1.00 93.11  ? 1455 PHE B CE1   1 
ATOM   5580 C  CE2   . PHE B 1 238 ? 1.362   3.631   4.726   1.00 89.01  ? 1455 PHE B CE2   1 
ATOM   5581 C  CZ    . PHE B 1 238 ? 0.681   4.782   4.412   1.00 92.09  ? 1455 PHE B CZ    1 
ATOM   5582 N  N     . SER B 1 239 ? 4.564   1.268   -0.755  1.00 88.46  ? 1456 SER B N     1 
ATOM   5583 C  CA    . SER B 1 239 ? 5.404   0.213   -1.302  1.00 86.65  ? 1456 SER B CA    1 
ATOM   5584 C  C     . SER B 1 239 ? 6.855   0.396   -0.860  1.00 89.62  ? 1456 SER B C     1 
ATOM   5585 O  O     . SER B 1 239 ? 7.475   -0.535  -0.328  1.00 95.72  ? 1456 SER B O     1 
ATOM   5586 C  CB    . SER B 1 239 ? 5.278   0.178   -2.829  1.00 85.95  ? 1456 SER B CB    1 
ATOM   5587 O  OG    . SER B 1 239 ? 5.526   1.451   -3.402  1.00 88.35  ? 1456 SER B OG    1 
ATOM   5588 N  N     . ARG B 1 240 ? 7.404   1.605   -1.033  1.00 77.93  ? 1457 ARG B N     1 
ATOM   5589 C  CA    . ARG B 1 240 ? 8.785   1.843   -0.620  1.00 74.53  ? 1457 ARG B CA    1 
ATOM   5590 C  C     . ARG B 1 240 ? 8.949   1.688   0.884   1.00 80.36  ? 1457 ARG B C     1 
ATOM   5591 O  O     . ARG B 1 240 ? 9.955   1.145   1.346   1.00 93.37  ? 1457 ARG B O     1 
ATOM   5592 C  CB    . ARG B 1 240 ? 9.240   3.239   -1.051  1.00 74.56  ? 1457 ARG B CB    1 
ATOM   5593 C  CG    . ARG B 1 240 ? 9.240   3.441   -2.557  1.00 82.74  ? 1457 ARG B CG    1 
ATOM   5594 C  CD    . ARG B 1 240 ? 9.750   4.804   -2.966  1.00 91.10  ? 1457 ARG B CD    1 
ATOM   5595 N  NE    . ARG B 1 240 ? 10.289  4.772   -4.324  1.00 103.32 ? 1457 ARG B NE    1 
ATOM   5596 C  CZ    . ARG B 1 240 ? 9.777   5.436   -5.354  1.00 108.51 ? 1457 ARG B CZ    1 
ATOM   5597 N  NH1   . ARG B 1 240 ? 8.705   6.204   -5.186  1.00 116.82 ? 1457 ARG B NH1   1 
ATOM   5598 N  NH2   . ARG B 1 240 ? 10.342  5.335   -6.553  1.00 100.76 ? 1457 ARG B NH2   1 
ATOM   5599 N  N     . MET B 1 241 ? 7.951   2.100   1.666   1.00 93.41  ? 1458 MET B N     1 
ATOM   5600 C  CA    . MET B 1 241 ? 8.059   1.926   3.113   1.00 92.98  ? 1458 MET B CA    1 
ATOM   5601 C  C     . MET B 1 241 ? 8.146   0.448   3.489   1.00 90.75  ? 1458 MET B C     1 
ATOM   5602 O  O     . MET B 1 241 ? 8.976   0.057   4.315   1.00 91.70  ? 1458 MET B O     1 
ATOM   5603 C  CB    . MET B 1 241 ? 6.876   2.597   3.822   1.00 86.86  ? 1458 MET B CB    1 
ATOM   5604 N  N     . PHE B 1 242 ? 7.303   -0.390  2.897   1.00 82.36  ? 1459 PHE B N     1 
ATOM   5605 C  CA    . PHE B 1 242 ? 7.176   -1.777  3.316   1.00 83.08  ? 1459 PHE B CA    1 
ATOM   5606 C  C     . PHE B 1 242 ? 7.813   -2.742  2.325   1.00 92.59  ? 1459 PHE B C     1 
ATOM   5607 O  O     . PHE B 1 242 ? 7.602   -3.963  2.435   1.00 94.60  ? 1459 PHE B O     1 
ATOM   5608 C  CB    . PHE B 1 242 ? 5.699   -2.122  3.537   1.00 76.82  ? 1459 PHE B CB    1 
ATOM   5609 C  CG    . PHE B 1 242 ? 5.145   -1.580  4.816   1.00 80.16  ? 1459 PHE B CG    1 
ATOM   5610 C  CD1   . PHE B 1 242 ? 5.180   -2.333  5.978   1.00 70.79  ? 1459 PHE B CD1   1 
ATOM   5611 C  CD2   . PHE B 1 242 ? 4.619   -0.301  4.869   1.00 89.34  ? 1459 PHE B CD2   1 
ATOM   5612 C  CE1   . PHE B 1 242 ? 4.686   -1.842  7.175   1.00 66.86  ? 1459 PHE B CE1   1 
ATOM   5613 C  CE2   . PHE B 1 242 ? 4.116   0.199   6.063   1.00 91.25  ? 1459 PHE B CE2   1 
ATOM   5614 C  CZ    . PHE B 1 242 ? 4.149   -0.580  7.218   1.00 82.27  ? 1459 PHE B CZ    1 
ATOM   5615 N  N     . ASP B 1 243 ? 8.599   -2.225  1.376   1.00 83.75  ? 1460 ASP B N     1 
ATOM   5616 C  CA    . ASP B 1 243 ? 9.287   -3.031  0.367   1.00 84.46  ? 1460 ASP B CA    1 
ATOM   5617 C  C     . ASP B 1 243 ? 8.327   -3.982  -0.342  1.00 98.99  ? 1460 ASP B C     1 
ATOM   5618 O  O     . ASP B 1 243 ? 8.476   -5.213  -0.323  1.00 103.21 ? 1460 ASP B O     1 
ATOM   5619 C  CB    . ASP B 1 243 ? 10.466  -3.794  0.977   1.00 89.92  ? 1460 ASP B CB    1 
ATOM   5620 C  CG    . ASP B 1 243 ? 11.609  -3.994  -0.021  1.00 116.29 ? 1460 ASP B CG    1 
ATOM   5621 O  OD1   . ASP B 1 243 ? 11.961  -3.020  -0.733  1.00 125.09 ? 1460 ASP B OD1   1 
ATOM   5622 O  OD2   . ASP B 1 243 ? 12.167  -5.113  -0.089  1.00 123.61 ? 1460 ASP B OD2   1 
ATOM   5623 N  N     . ILE B 1 244 ? 7.297   -3.391  -0.936  1.00 97.52  ? 1461 ILE B N     1 
ATOM   5624 C  CA    . ILE B 1 244 ? 6.430   -4.128  -1.843  1.00 99.88  ? 1461 ILE B CA    1 
ATOM   5625 C  C     . ILE B 1 244 ? 6.977   -3.840  -3.233  1.00 94.67  ? 1461 ILE B C     1 
ATOM   5626 O  O     . ILE B 1 244 ? 6.718   -2.784  -3.809  1.00 97.64  ? 1461 ILE B O     1 
ATOM   5627 C  CB    . ILE B 1 244 ? 4.958   -3.737  -1.685  1.00 98.71  ? 1461 ILE B CB    1 
ATOM   5628 C  CG1   . ILE B 1 244 ? 4.596   -3.611  -0.206  1.00 93.45  ? 1461 ILE B CG1   1 
ATOM   5629 C  CG2   . ILE B 1 244 ? 4.066   -4.826  -2.242  1.00 92.26  ? 1461 ILE B CG2   1 
ATOM   5630 C  CD1   . ILE B 1 244 ? 3.520   -2.603  0.090   1.00 78.13  ? 1461 ILE B CD1   1 
ATOM   5631 N  N     . VAL B 1 245 ? 7.784   -4.772  -3.740  1.00 89.31  ? 1462 VAL B N     1 
ATOM   5632 C  CA    . VAL B 1 245 ? 8.513   -4.604  -4.990  1.00 90.97  ? 1462 VAL B CA    1 
ATOM   5633 C  C     . VAL B 1 245 ? 8.418   -5.894  -5.802  1.00 90.37  ? 1462 VAL B C     1 
ATOM   5634 O  O     . VAL B 1 245 ? 8.142   -6.979  -5.280  1.00 88.78  ? 1462 VAL B O     1 
ATOM   5635 C  CB    . VAL B 1 245 ? 9.998   -4.200  -4.754  1.00 79.58  ? 1462 VAL B CB    1 
ATOM   5636 N  N     . TYR B 1 246 ? 8.650   -5.749  -7.094  1.00 86.03  ? 1463 TYR B N     1 
ATOM   5637 C  CA    . TYR B 1 246 ? 8.737   -6.863  -8.014  1.00 87.18  ? 1463 TYR B CA    1 
ATOM   5638 C  C     . TYR B 1 246 ? 9.976   -6.676  -8.874  1.00 101.69 ? 1463 TYR B C     1 
ATOM   5639 O  O     . TYR B 1 246 ? 10.488  -5.564  -9.032  1.00 106.02 ? 1463 TYR B O     1 
ATOM   5640 C  CB    . TYR B 1 246 ? 7.485   -6.986  -8.900  1.00 86.54  ? 1463 TYR B CB    1 
ATOM   5641 C  CG    . TYR B 1 246 ? 7.055   -5.715  -9.640  1.00 96.65  ? 1463 TYR B CG    1 
ATOM   5642 C  CD1   . TYR B 1 246 ? 7.332   -5.537  -10.992 1.00 98.56  ? 1463 TYR B CD1   1 
ATOM   5643 C  CD2   . TYR B 1 246 ? 6.342   -4.716  -8.992  1.00 94.09  ? 1463 TYR B CD2   1 
ATOM   5644 C  CE1   . TYR B 1 246 ? 6.924   -4.397  -11.668 1.00 97.22  ? 1463 TYR B CE1   1 
ATOM   5645 C  CE2   . TYR B 1 246 ? 5.930   -3.578  -9.659  1.00 101.63 ? 1463 TYR B CE2   1 
ATOM   5646 C  CZ    . TYR B 1 246 ? 6.223   -3.417  -10.997 1.00 104.60 ? 1463 TYR B CZ    1 
ATOM   5647 O  OH    . TYR B 1 246 ? 5.818   -2.257  -11.649 1.00 107.36 ? 1463 TYR B OH    1 
ATOM   5648 N  N     . GLU B 1 247 ? 10.456  -7.785  -9.432  1.00 109.26 ? 1464 GLU B N     1 
ATOM   5649 C  CA    . GLU B 1 247 ? 11.603  -7.744  -10.328 1.00 109.01 ? 1464 GLU B CA    1 
ATOM   5650 C  C     . GLU B 1 247 ? 11.152  -7.182  -11.664 1.00 105.95 ? 1464 GLU B C     1 
ATOM   5651 O  O     . GLU B 1 247 ? 10.190  -7.677  -12.257 1.00 104.14 ? 1464 GLU B O     1 
ATOM   5652 C  CB    . GLU B 1 247 ? 12.178  -9.153  -10.516 1.00 119.20 ? 1464 GLU B CB    1 
ATOM   5653 C  CG    . GLU B 1 247 ? 13.697  -9.239  -10.672 1.00 132.90 ? 1464 GLU B CG    1 
ATOM   5654 C  CD    . GLU B 1 247 ? 14.215  -10.658 -10.947 1.00 139.65 ? 1464 GLU B CD    1 
ATOM   5655 O  OE1   . GLU B 1 247 ? 13.508  -11.649 -10.639 1.00 134.01 ? 1464 GLU B OE1   1 
ATOM   5656 O  OE2   . GLU B 1 247 ? 15.347  -10.772 -11.471 1.00 143.42 ? 1464 GLU B OE2   1 
ATOM   5657 N  N     . HIS B 1 248 ? 11.812  -6.135  -12.129 1.00 111.65 ? 1465 HIS B N     1 
ATOM   5658 C  CA    . HIS B 1 248 ? 11.481  -5.648  -13.456 1.00 121.29 ? 1465 HIS B CA    1 
ATOM   5659 C  C     . HIS B 1 248 ? 11.923  -6.715  -14.447 1.00 118.53 ? 1465 HIS B C     1 
ATOM   5660 O  O     . HIS B 1 248 ? 13.079  -7.152  -14.402 1.00 116.17 ? 1465 HIS B O     1 
ATOM   5661 C  CB    . HIS B 1 248 ? 12.148  -4.302  -13.752 1.00 130.66 ? 1465 HIS B CB    1 
ATOM   5662 C  CG    . HIS B 1 248 ? 11.471  -3.516  -14.835 1.00 137.11 ? 1465 HIS B CG    1 
ATOM   5663 N  ND1   . HIS B 1 248 ? 11.029  -4.092  -16.007 1.00 138.54 ? 1465 HIS B ND1   1 
ATOM   5664 C  CD2   . HIS B 1 248 ? 11.156  -2.201  -14.921 1.00 139.66 ? 1465 HIS B CD2   1 
ATOM   5665 C  CE1   . HIS B 1 248 ? 10.470  -3.168  -16.768 1.00 140.20 ? 1465 HIS B CE1   1 
ATOM   5666 N  NE2   . HIS B 1 248 ? 10.534  -2.012  -16.132 1.00 140.00 ? 1465 HIS B NE2   1 
ATOM   5667 N  N     . PRO B 1 249 ? 11.041  -7.169  -15.335 1.00 111.74 ? 1466 PRO B N     1 
ATOM   5668 C  CA    . PRO B 1 249 ? 11.434  -8.256  -16.246 1.00 104.47 ? 1466 PRO B CA    1 
ATOM   5669 C  C     . PRO B 1 249 ? 12.628  -7.927  -17.125 1.00 96.48  ? 1466 PRO B C     1 
ATOM   5670 O  O     . PRO B 1 249 ? 13.519  -8.769  -17.269 1.00 98.35  ? 1466 PRO B O     1 
ATOM   5671 C  CB    . PRO B 1 249 ? 10.147  -8.509  -17.046 1.00 99.28  ? 1466 PRO B CB    1 
ATOM   5672 C  CG    . PRO B 1 249 ? 9.062   -8.189  -16.051 1.00 98.75  ? 1466 PRO B CG    1 
ATOM   5673 C  CD    . PRO B 1 249 ? 9.586   -6.947  -15.350 1.00 106.79 ? 1466 PRO B CD    1 
ATOM   5674 N  N     . GLU B 1 250 ? 12.721  -6.717  -17.582 1.00 104.89 ? 1467 GLU B N     1 
ATOM   5675 C  CA    . GLU B 1 250 ? 13.804  -6.392  -18.449 1.00 112.05 ? 1467 GLU B CA    1 
ATOM   5676 C  C     . GLU B 1 250 ? 15.110  -6.259  -17.725 1.00 124.46 ? 1467 GLU B C     1 
ATOM   5677 O  O     . GLU B 1 250 ? 15.977  -7.093  -17.847 1.00 124.51 ? 1467 GLU B O     1 
ATOM   5678 C  CB    . GLU B 1 250 ? 13.484  -5.129  -19.203 1.00 108.65 ? 1467 GLU B CB    1 
ATOM   5679 N  N     . THR B 1 251 ? 15.281  -5.184  -16.998 1.00 133.34 ? 1468 THR B N     1 
ATOM   5680 C  CA    . THR B 1 251 ? 16.508  -4.991  -16.267 1.00 130.61 ? 1468 THR B CA    1 
ATOM   5681 C  C     . THR B 1 251 ? 16.005  -5.177  -14.940 1.00 122.55 ? 1468 THR B C     1 
ATOM   5682 O  O     . THR B 1 251 ? 15.240  -4.367  -14.503 1.00 125.73 ? 1468 THR B O     1 
ATOM   5683 C  CB    . THR B 1 251 ? 16.959  -3.543  -16.315 1.00 131.33 ? 1468 THR B CB    1 
ATOM   5684 N  N     . LYS B 1 252 ? 16.556  -6.049  -14.138 1.00 118.04 ? 1469 LYS B N     1 
ATOM   5685 C  CA    . LYS B 1 252 ? 15.896  -6.313  -12.881 1.00 117.28 ? 1469 LYS B CA    1 
ATOM   5686 C  C     . LYS B 1 252 ? 16.050  -5.354  -11.730 1.00 114.46 ? 1469 LYS B C     1 
ATOM   5687 O  O     . LYS B 1 252 ? 16.442  -5.705  -10.648 1.00 110.08 ? 1469 LYS B O     1 
ATOM   5688 C  CB    . LYS B 1 252 ? 16.246  -7.714  -12.438 1.00 118.10 ? 1469 LYS B CB    1 
ATOM   5689 N  N     . GLU B 1 253 ? 15.557  -4.166  -11.963 1.00 115.90 ? 1470 GLU B N     1 
ATOM   5690 C  CA    . GLU B 1 253 ? 15.558  -3.102  -11.057 1.00 110.59 ? 1470 GLU B CA    1 
ATOM   5691 C  C     . GLU B 1 253 ? 14.371  -3.349  -10.207 1.00 110.51 ? 1470 GLU B C     1 
ATOM   5692 O  O     . GLU B 1 253 ? 13.318  -3.674  -10.696 1.00 115.46 ? 1470 GLU B O     1 
ATOM   5693 C  CB    . GLU B 1 253 ? 15.360  -1.825  -11.854 1.00 104.12 ? 1470 GLU B CB    1 
ATOM   5694 N  N     . LYS B 1 254 ? 14.547  -3.242  -8.915  1.00 105.34 ? 1471 LYS B N     1 
ATOM   5695 C  CA    . LYS B 1 254 ? 13.403  -3.400  -8.030  1.00 95.77  ? 1471 LYS B CA    1 
ATOM   5696 C  C     . LYS B 1 254 ? 12.367  -2.341  -8.404  1.00 106.51 ? 1471 LYS B C     1 
ATOM   5697 O  O     . LYS B 1 254 ? 12.694  -1.157  -8.564  1.00 117.81 ? 1471 LYS B O     1 
ATOM   5698 C  CB    . LYS B 1 254 ? 13.833  -3.309  -6.555  1.00 68.70  ? 1471 LYS B CB    1 
ATOM   5699 N  N     . GLU B 1 255 ? 11.128  -2.775  -8.606  1.00 99.62  ? 1472 GLU B N     1 
ATOM   5700 C  CA    . GLU B 1 255 ? 10.053  -1.881  -8.997  1.00 93.50  ? 1472 GLU B CA    1 
ATOM   5701 C  C     . GLU B 1 255 ? 9.040   -1.851  -7.874  1.00 87.17  ? 1472 GLU B C     1 
ATOM   5702 O  O     . GLU B 1 255 ? 8.655   -2.896  -7.346  1.00 77.18  ? 1472 GLU B O     1 
ATOM   5703 C  CB    . GLU B 1 255 ? 9.400   -2.323  -10.308 1.00 89.58  ? 1472 GLU B CB    1 
ATOM   5704 C  CG    . GLU B 1 255 ? 9.978   -1.631  -11.537 1.00 101.11 ? 1472 GLU B CG    1 
ATOM   5705 C  CD    . GLU B 1 255 ? 9.386   -0.255  -11.781 1.00 111.04 ? 1472 GLU B CD    1 
ATOM   5706 O  OE1   . GLU B 1 255 ? 9.648   0.306   -12.866 1.00 109.27 ? 1472 GLU B OE1   1 
ATOM   5707 O  OE2   . GLU B 1 255 ? 8.657   0.264   -10.902 1.00 117.54 ? 1472 GLU B OE2   1 
ATOM   5708 N  N     . TYR B 1 256 ? 8.640   -0.656  -7.492  1.00 89.39  ? 1473 TYR B N     1 
ATOM   5709 C  CA    . TYR B 1 256 ? 7.672   -0.511  -6.432  1.00 90.41  ? 1473 TYR B CA    1 
ATOM   5710 C  C     . TYR B 1 256 ? 6.276   -0.446  -7.028  1.00 88.22  ? 1473 TYR B C     1 
ATOM   5711 O  O     . TYR B 1 256 ? 6.078   0.061   -8.140  1.00 85.54  ? 1473 TYR B O     1 
ATOM   5712 C  CB    . TYR B 1 256 ? 8.002   0.719   -5.595  1.00 94.57  ? 1473 TYR B CB    1 
ATOM   5713 C  CG    . TYR B 1 256 ? 9.276   0.511   -4.817  1.00 97.54  ? 1473 TYR B CG    1 
ATOM   5714 C  CD1   . TYR B 1 256 ? 9.277   -0.267  -3.665  1.00 93.19  ? 1473 TYR B CD1   1 
ATOM   5715 C  CD2   . TYR B 1 256 ? 10.492  1.063   -5.249  1.00 100.60 ? 1473 TYR B CD2   1 
ATOM   5716 C  CE1   . TYR B 1 256 ? 10.443  -0.480  -2.941  1.00 98.65  ? 1473 TYR B CE1   1 
ATOM   5717 C  CE2   . TYR B 1 256 ? 11.673  0.863   -4.524  1.00 92.76  ? 1473 TYR B CE2   1 
ATOM   5718 C  CZ    . TYR B 1 256 ? 11.640  0.084   -3.368  1.00 97.43  ? 1473 TYR B CZ    1 
ATOM   5719 O  OH    . TYR B 1 256 ? 12.788  -0.143  -2.629  1.00 98.16  ? 1473 TYR B OH    1 
ATOM   5720 N  N     . VAL B 1 257 ? 5.332   -1.051  -6.322  1.00 86.91  ? 1474 VAL B N     1 
ATOM   5721 C  CA    . VAL B 1 257 ? 3.966   -1.071  -6.802  1.00 93.13  ? 1474 VAL B CA    1 
ATOM   5722 C  C     . VAL B 1 257 ? 3.296   0.267   -6.505  1.00 90.49  ? 1474 VAL B C     1 
ATOM   5723 O  O     . VAL B 1 257 ? 3.769   1.072   -5.692  1.00 97.49  ? 1474 VAL B O     1 
ATOM   5724 C  CB    . VAL B 1 257 ? 3.193   -2.241  -6.179  1.00 89.98  ? 1474 VAL B CB    1 
ATOM   5725 C  CG1   . VAL B 1 257 ? 3.584   -3.524  -6.869  1.00 88.59  ? 1474 VAL B CG1   1 
ATOM   5726 C  CG2   . VAL B 1 257 ? 3.471   -2.323  -4.689  1.00 86.15  ? 1474 VAL B CG2   1 
ATOM   5727 N  N     . PHE B 1 258 ? 2.169   0.495   -7.159  1.00 64.78  ? 1475 PHE B N     1 
ATOM   5728 C  CA    . PHE B 1 258 ? 1.378   1.688   -6.935  1.00 75.15  ? 1475 PHE B CA    1 
ATOM   5729 C  C     . PHE B 1 258 ? 0.130   1.273   -6.161  1.00 74.65  ? 1475 PHE B C     1 
ATOM   5730 O  O     . PHE B 1 258 ? -0.580  0.349   -6.562  1.00 68.89  ? 1475 PHE B O     1 
ATOM   5731 C  CB    . PHE B 1 258 ? 1.050   2.367   -8.264  1.00 83.15  ? 1475 PHE B CB    1 
ATOM   5732 C  CG    . PHE B 1 258 ? 2.239   3.048   -8.900  1.00 93.13  ? 1475 PHE B CG    1 
ATOM   5733 C  CD1   . PHE B 1 258 ? 2.468   4.407   -8.709  1.00 95.86  ? 1475 PHE B CD1   1 
ATOM   5734 C  CD2   . PHE B 1 258 ? 3.145   2.325   -9.668  1.00 96.04  ? 1475 PHE B CD2   1 
ATOM   5735 C  CE1   . PHE B 1 258 ? 3.567   5.030   -9.290  1.00 90.37  ? 1475 PHE B CE1   1 
ATOM   5736 C  CE2   . PHE B 1 258 ? 4.248   2.946   -10.249 1.00 90.28  ? 1475 PHE B CE2   1 
ATOM   5737 C  CZ    . PHE B 1 258 ? 4.457   4.294   -10.062 1.00 87.39  ? 1475 PHE B CZ    1 
ATOM   5738 N  N     . GLN B 1 259 ? -0.095  1.913   -5.021  1.00 69.52  ? 1476 GLN B N     1 
ATOM   5739 C  CA    . GLN B 1 259 ? -1.139  1.521   -4.095  1.00 62.38  ? 1476 GLN B CA    1 
ATOM   5740 C  C     . GLN B 1 259 ? -2.189  2.615   -3.943  1.00 78.24  ? 1476 GLN B C     1 
ATOM   5741 O  O     . GLN B 1 259 ? -1.878  3.822   -3.972  1.00 87.34  ? 1476 GLN B O     1 
ATOM   5742 C  CB    . GLN B 1 259 ? -0.574  1.191   -2.713  1.00 56.15  ? 1476 GLN B CB    1 
ATOM   5743 C  CG    . GLN B 1 259 ? 0.419   0.060   -2.682  1.00 63.02  ? 1476 GLN B CG    1 
ATOM   5744 C  CD    . GLN B 1 259 ? 1.069   -0.083  -1.311  1.00 77.48  ? 1476 GLN B CD    1 
ATOM   5745 O  OE1   . GLN B 1 259 ? 2.135   0.486   -1.065  1.00 90.11  ? 1476 GLN B OE1   1 
ATOM   5746 N  NE2   . GLN B 1 259 ? 0.426   -0.835  -0.410  1.00 70.07  ? 1476 GLN B NE2   1 
ATOM   5747 N  N     . ASN B 1 260 ? -3.432  2.144   -3.748  1.00 83.33  ? 1477 ASN B N     1 
ATOM   5748 C  CA    . ASN B 1 260 ? -4.590  2.923   -3.320  1.00 76.65  ? 1477 ASN B CA    1 
ATOM   5749 C  C     . ASN B 1 260 ? -5.183  2.307   -2.060  1.00 71.36  ? 1477 ASN B C     1 
ATOM   5750 O  O     . ASN B 1 260 ? -5.076  1.096   -1.831  1.00 77.69  ? 1477 ASN B O     1 
ATOM   5751 C  CB    . ASN B 1 260 ? -5.733  2.932   -4.354  1.00 65.34  ? 1477 ASN B CB    1 
ATOM   5752 C  CG    . ASN B 1 260 ? -5.301  3.360   -5.742  1.00 70.64  ? 1477 ASN B CG    1 
ATOM   5753 O  OD1   . ASN B 1 260 ? -4.296  4.054   -5.924  1.00 77.44  ? 1477 ASN B OD1   1 
ATOM   5754 N  ND2   . ASN B 1 260 ? -6.083  2.941   -6.745  1.00 57.23  ? 1477 ASN B ND2   1 
ATOM   5755 N  N     . SER B 1 261 ? -5.833  3.146   -1.253  1.00 60.89  ? 1478 SER B N     1 
ATOM   5756 C  CA    . SER B 1 261 ? -6.741  2.654   -0.228  1.00 60.99  ? 1478 SER B CA    1 
ATOM   5757 C  C     . SER B 1 261 ? -7.961  3.562   -0.199  1.00 71.22  ? 1478 SER B C     1 
ATOM   5758 O  O     . SER B 1 261 ? -7.903  4.729   -0.587  1.00 83.34  ? 1478 SER B O     1 
ATOM   5759 C  CB    . SER B 1 261 ? -6.094  2.528   1.164   1.00 58.97  ? 1478 SER B CB    1 
ATOM   5760 O  OG    . SER B 1 261 ? -5.657  3.767   1.669   1.00 68.02  ? 1478 SER B OG    1 
ATOM   5761 N  N     . TRP B 1 262 ? -9.084  2.991   0.216   1.00 73.87  ? 1479 TRP B N     1 
ATOM   5762 C  CA    . TRP B 1 262 ? -10.360 3.687   0.205   1.00 71.43  ? 1479 TRP B CA    1 
ATOM   5763 C  C     . TRP B 1 262 ? -11.214 3.148   1.337   1.00 79.45  ? 1479 TRP B C     1 
ATOM   5764 O  O     . TRP B 1 262 ? -11.054 2.007   1.768   1.00 91.31  ? 1479 TRP B O     1 
ATOM   5765 C  CB    . TRP B 1 262 ? -11.091 3.536   -1.138  1.00 67.71  ? 1479 TRP B CB    1 
ATOM   5766 C  CG    . TRP B 1 262 ? -10.753 2.292   -1.932  1.00 76.34  ? 1479 TRP B CG    1 
ATOM   5767 C  CD1   . TRP B 1 262 ? -9.693  2.120   -2.780  1.00 64.88  ? 1479 TRP B CD1   1 
ATOM   5768 C  CD2   . TRP B 1 262 ? -11.492 1.056   -1.965  1.00 89.52  ? 1479 TRP B CD2   1 
ATOM   5769 N  NE1   . TRP B 1 262 ? -9.727  0.863   -3.332  1.00 71.30  ? 1479 TRP B NE1   1 
ATOM   5770 C  CE2   . TRP B 1 262 ? -10.815 0.187   -2.844  1.00 80.89  ? 1479 TRP B CE2   1 
ATOM   5771 C  CE3   . TRP B 1 262 ? -12.656 0.600   -1.331  1.00 89.95  ? 1479 TRP B CE3   1 
ATOM   5772 C  CZ2   . TRP B 1 262 ? -11.268 -1.104  -3.109  1.00 62.76  ? 1479 TRP B CZ2   1 
ATOM   5773 C  CZ3   . TRP B 1 262 ? -13.097 -0.669  -1.594  1.00 80.77  ? 1479 TRP B CZ3   1 
ATOM   5774 C  CH2   . TRP B 1 262 ? -12.409 -1.510  -2.473  1.00 67.08  ? 1479 TRP B CH2   1 
ATOM   5775 N  N     . GLY B 1 263 ? -12.138 3.974   1.811   1.00 75.45  ? 1480 GLY B N     1 
ATOM   5776 C  CA    . GLY B 1 263 ? -12.857 3.641   3.024   1.00 67.81  ? 1480 GLY B CA    1 
ATOM   5777 C  C     . GLY B 1 263 ? -14.205 4.310   3.057   1.00 71.14  ? 1480 GLY B C     1 
ATOM   5778 O  O     . GLY B 1 263 ? -14.419 5.349   2.422   1.00 81.25  ? 1480 GLY B O     1 
ATOM   5779 N  N     . ILE B 1 264 ? -15.138 3.680   3.762   1.00 62.45  ? 1481 ILE B N     1 
ATOM   5780 C  CA    . ILE B 1 264 ? -16.400 4.357   4.079   1.00 57.89  ? 1481 ILE B CA    1 
ATOM   5781 C  C     . ILE B 1 264 ? -16.943 3.768   5.368   1.00 64.56  ? 1481 ILE B C     1 
ATOM   5782 O  O     . ILE B 1 264 ? -16.837 2.557   5.610   1.00 73.90  ? 1481 ILE B O     1 
ATOM   5783 C  CB    . ILE B 1 264 ? -17.428 4.281   2.920   1.00 50.55  ? 1481 ILE B CB    1 
ATOM   5784 C  CG1   . ILE B 1 264 ? -18.460 5.417   3.027   1.00 52.89  ? 1481 ILE B CG1   1 
ATOM   5785 C  CG2   . ILE B 1 264 ? -18.151 2.918   2.896   1.00 54.16  ? 1481 ILE B CG2   1 
ATOM   5786 C  CD1   . ILE B 1 264 ? -19.462 5.528   1.857   1.00 44.52  ? 1481 ILE B CD1   1 
ATOM   5787 N  N     . THR B 1 265 ? -17.509 4.630   6.206   1.00 60.59  ? 1482 THR B N     1 
ATOM   5788 C  CA    . THR B 1 265 ? -17.827 4.278   7.585   1.00 66.15  ? 1482 THR B CA    1 
ATOM   5789 C  C     . THR B 1 265 ? -19.319 4.482   7.875   1.00 65.23  ? 1482 THR B C     1 
ATOM   5790 O  O     . THR B 1 265 ? -20.120 4.898   7.022   1.00 58.32  ? 1482 THR B O     1 
ATOM   5791 C  CB    . THR B 1 265 ? -16.958 5.070   8.574   1.00 70.23  ? 1482 THR B CB    1 
ATOM   5792 O  OG1   . THR B 1 265 ? -17.451 6.413   8.727   1.00 77.39  ? 1482 THR B OG1   1 
ATOM   5793 C  CG2   . THR B 1 265 ? -15.500 5.089   8.122   1.00 60.15  ? 1482 THR B CG2   1 
ATOM   5794 N  N     . THR B 1 266 ? -19.691 4.169   9.115   1.00 68.51  ? 1483 THR B N     1 
ATOM   5795 C  CA    . THR B 1 266 ? -21.088 4.325   9.496   1.00 75.22  ? 1483 THR B CA    1 
ATOM   5796 C  C     . THR B 1 266 ? -21.474 5.788   9.715   1.00 68.34  ? 1483 THR B C     1 
ATOM   5797 O  O     . THR B 1 266 ? -22.646 6.083   9.979   1.00 74.73  ? 1483 THR B O     1 
ATOM   5798 C  CB    . THR B 1 266 ? -21.361 3.490   10.752  1.00 70.88  ? 1483 THR B CB    1 
ATOM   5799 O  OG1   . THR B 1 266 ? -20.255 3.604   11.669  1.00 74.87  ? 1483 THR B OG1   1 
ATOM   5800 C  CG2   . THR B 1 266 ? -21.538 2.058   10.361  1.00 73.62  ? 1483 THR B CG2   1 
ATOM   5801 N  N     . ARG B 1 267 ? -20.521 6.703   9.568   1.00 66.54  ? 1484 ARG B N     1 
ATOM   5802 C  CA    . ARG B 1 267 ? -20.825 8.122   9.551   1.00 73.57  ? 1484 ARG B CA    1 
ATOM   5803 C  C     . ARG B 1 267 ? -21.932 8.462   8.553   1.00 72.59  ? 1484 ARG B C     1 
ATOM   5804 O  O     . ARG B 1 267 ? -22.724 9.381   8.805   1.00 77.24  ? 1484 ARG B O     1 
ATOM   5805 C  CB    . ARG B 1 267 ? -19.529 8.896   9.267   1.00 72.91  ? 1484 ARG B CB    1 
ATOM   5806 C  CG    . ARG B 1 267 ? -19.663 10.113  8.399   1.00 76.94  ? 1484 ARG B CG    1 
ATOM   5807 C  CD    . ARG B 1 267 ? -18.300 10.620  8.054   1.00 81.18  ? 1484 ARG B CD    1 
ATOM   5808 N  NE    . ARG B 1 267 ? -17.470 10.685  9.246   1.00 89.34  ? 1484 ARG B NE    1 
ATOM   5809 C  CZ    . ARG B 1 267 ? -16.437 11.503  9.383   1.00 96.65  ? 1484 ARG B CZ    1 
ATOM   5810 N  NH1   . ARG B 1 267 ? -16.102 12.315  8.392   1.00 94.88  ? 1484 ARG B NH1   1 
ATOM   5811 N  NH2   . ARG B 1 267 ? -15.738 11.506  10.507  1.00 104.29 ? 1484 ARG B NH2   1 
ATOM   5812 N  N     . THR B 1 268 ? -22.030 7.712   7.448   1.00 59.17  ? 1485 THR B N     1 
ATOM   5813 C  CA    . THR B 1 268 ? -23.138 7.868   6.506   1.00 66.59  ? 1485 THR B CA    1 
ATOM   5814 C  C     . THR B 1 268 ? -24.472 8.027   7.233   1.00 66.40  ? 1485 THR B C     1 
ATOM   5815 O  O     . THR B 1 268 ? -25.223 8.984   6.990   1.00 75.41  ? 1485 THR B O     1 
ATOM   5816 C  CB    . THR B 1 268 ? -23.203 6.665   5.544   1.00 72.39  ? 1485 THR B CB    1 
ATOM   5817 O  OG1   . THR B 1 268 ? -23.487 5.461   6.273   1.00 67.15  ? 1485 THR B OG1   1 
ATOM   5818 C  CG2   . THR B 1 268 ? -21.889 6.484   4.822   1.00 73.41  ? 1485 THR B CG2   1 
ATOM   5819 N  N     . ILE B 1 269 ? -24.755 7.123   8.175   1.00 60.91  ? 1486 ILE B N     1 
ATOM   5820 C  CA    . ILE B 1 269 ? -26.054 7.151   8.836   1.00 64.13  ? 1486 ILE B CA    1 
ATOM   5821 C  C     . ILE B 1 269 ? -26.245 8.480   9.549   1.00 64.35  ? 1486 ILE B C     1 
ATOM   5822 O  O     . ILE B 1 269 ? -27.271 9.143   9.382   1.00 63.30  ? 1486 ILE B O     1 
ATOM   5823 C  CB    . ILE B 1 269 ? -26.205 5.954   9.794   1.00 60.57  ? 1486 ILE B CB    1 
ATOM   5824 C  CG1   . ILE B 1 269 ? -26.236 4.652   8.989   1.00 63.80  ? 1486 ILE B CG1   1 
ATOM   5825 C  CG2   . ILE B 1 269 ? -27.504 6.056   10.596  1.00 56.93  ? 1486 ILE B CG2   1 
ATOM   5826 C  CD1   . ILE B 1 269 ? -25.844 3.437   9.784   1.00 53.22  ? 1486 ILE B CD1   1 
ATOM   5827 N  N     . GLY B 1 270 ? -25.218 8.931   10.274  1.00 61.13  ? 1487 GLY B N     1 
ATOM   5828 C  CA    . GLY B 1 270 ? -25.301 10.235  10.908  1.00 61.54  ? 1487 GLY B CA    1 
ATOM   5829 C  C     . GLY B 1 270 ? -25.574 11.335  9.899   1.00 65.39  ? 1487 GLY B C     1 
ATOM   5830 O  O     . GLY B 1 270 ? -26.507 12.127  10.067  1.00 57.80  ? 1487 GLY B O     1 
ATOM   5831 N  N     . VAL B 1 271 ? -24.807 11.349  8.800   1.00 50.13  ? 1488 VAL B N     1 
ATOM   5832 C  CA    . VAL B 1 271 ? -25.080 12.291  7.729   1.00 68.47  ? 1488 VAL B CA    1 
ATOM   5833 C  C     . VAL B 1 271 ? -26.530 12.166  7.293   1.00 79.62  ? 1488 VAL B C     1 
ATOM   5834 O  O     . VAL B 1 271 ? -27.288 13.153  7.297   1.00 80.48  ? 1488 VAL B O     1 
ATOM   5835 C  CB    . VAL B 1 271 ? -24.127 12.053  6.555   1.00 65.67  ? 1488 VAL B CB    1 
ATOM   5836 C  CG1   . VAL B 1 271 ? -24.373 13.102  5.462   1.00 59.97  ? 1488 VAL B CG1   1 
ATOM   5837 C  CG2   . VAL B 1 271 ? -22.709 12.073  7.063   1.00 64.12  ? 1488 VAL B CG2   1 
ATOM   5838 N  N     . MET B 1 272 ? -26.990 10.962  7.016   1.00 74.07  ? 1489 MET B N     1 
ATOM   5839 C  CA    . MET B 1 272 ? -28.357 10.833  6.592   1.00 63.17  ? 1489 MET B CA    1 
ATOM   5840 C  C     . MET B 1 272 ? -29.338 11.269  7.600   1.00 59.49  ? 1489 MET B C     1 
ATOM   5841 O  O     . MET B 1 272 ? -30.296 11.755  7.226   1.00 64.09  ? 1489 MET B O     1 
ATOM   5842 C  CB    . MET B 1 272 ? -28.708 9.492   5.972   1.00 75.69  ? 1489 MET B CB    1 
ATOM   5843 C  CG    . MET B 1 272 ? -29.190 8.449   6.931   1.00 72.11  ? 1489 MET B CG    1 
ATOM   5844 S  SD    . MET B 1 272 ? -30.621 7.508   6.586   1.00 66.26  ? 1489 MET B SD    1 
ATOM   5845 C  CE    . MET B 1 272 ? -31.030 7.324   8.246   1.00 61.72  ? 1489 MET B CE    1 
ATOM   5846 N  N     . ILE B 1 273 ? -29.113 11.043  8.868   1.00 61.82  ? 1490 ILE B N     1 
ATOM   5847 C  CA    . ILE B 1 273 ? -29.987 11.630  9.881   1.00 61.02  ? 1490 ILE B CA    1 
ATOM   5848 C  C     . ILE B 1 273 ? -30.010 13.133  9.708   1.00 65.72  ? 1490 ILE B C     1 
ATOM   5849 O  O     . ILE B 1 273 ? -31.034 13.727  9.353   1.00 67.43  ? 1490 ILE B O     1 
ATOM   5850 C  CB    . ILE B 1 273 ? -29.512 11.265  11.298  1.00 57.77  ? 1490 ILE B CB    1 
ATOM   5851 C  CG1   . ILE B 1 273 ? -29.688 9.781   11.597  1.00 55.58  ? 1490 ILE B CG1   1 
ATOM   5852 C  CG2   . ILE B 1 273 ? -30.233 12.129  12.366  1.00 55.75  ? 1490 ILE B CG2   1 
ATOM   5853 C  CD1   . ILE B 1 273 ? -28.835 9.396   12.762  1.00 66.27  ? 1490 ILE B CD1   1 
ATOM   5854 N  N     . MET B 1 274 ? -28.837 13.750  9.854   1.00 76.40  ? 1491 MET B N     1 
ATOM   5855 C  CA    . MET B 1 274 ? -28.791 15.195  9.888   1.00 78.45  ? 1491 MET B CA    1 
ATOM   5856 C  C     . MET B 1 274 ? -29.281 15.790  8.585   1.00 71.82  ? 1491 MET B C     1 
ATOM   5857 O  O     . MET B 1 274 ? -29.858 16.878  8.607   1.00 70.00  ? 1491 MET B O     1 
ATOM   5858 C  CB    . MET B 1 274 ? -27.393 15.684  10.289  1.00 76.68  ? 1491 MET B CB    1 
ATOM   5859 C  CG    . MET B 1 274 ? -27.419 16.164  11.752  1.00 88.62  ? 1491 MET B CG    1 
ATOM   5860 S  SD    . MET B 1 274 ? -25.836 16.455  12.520  1.00 109.09 ? 1491 MET B SD    1 
ATOM   5861 C  CE    . MET B 1 274 ? -26.281 16.622  14.252  1.00 105.30 ? 1491 MET B CE    1 
ATOM   5862 N  N     . VAL B 1 275 ? -29.199 15.060  7.473   1.00 67.75  ? 1492 VAL B N     1 
ATOM   5863 C  CA    . VAL B 1 275 ? -29.629 15.746  6.267   1.00 62.66  ? 1492 VAL B CA    1 
ATOM   5864 C  C     . VAL B 1 275 ? -31.134 15.703  6.149   1.00 72.52  ? 1492 VAL B C     1 
ATOM   5865 O  O     . VAL B 1 275 ? -31.778 16.706  5.820   1.00 76.30  ? 1492 VAL B O     1 
ATOM   5866 C  CB    . VAL B 1 275 ? -28.993 15.110  5.015   1.00 61.16  ? 1492 VAL B CB    1 
ATOM   5867 C  CG1   . VAL B 1 275 ? -29.820 15.472  3.751   1.00 55.30  ? 1492 VAL B CG1   1 
ATOM   5868 C  CG2   . VAL B 1 275 ? -27.542 15.540  4.860   1.00 54.48  ? 1492 VAL B CG2   1 
ATOM   5869 N  N     . HIS B 1 276 ? -31.727 14.563  6.507   1.00 77.82  ? 1493 HIS B N     1 
ATOM   5870 C  CA    . HIS B 1 276 ? -33.086 14.232  6.108   1.00 64.61  ? 1493 HIS B CA    1 
ATOM   5871 C  C     . HIS B 1 276 ? -34.080 14.172  7.255   1.00 65.58  ? 1493 HIS B C     1 
ATOM   5872 O  O     . HIS B 1 276 ? -35.278 14.318  7.012   1.00 72.63  ? 1493 HIS B O     1 
ATOM   5873 C  CB    . HIS B 1 276 ? -33.112 12.872  5.397   1.00 61.24  ? 1493 HIS B CB    1 
ATOM   5874 C  CG    . HIS B 1 276 ? -32.572 12.890  4.001   1.00 62.27  ? 1493 HIS B CG    1 
ATOM   5875 N  ND1   . HIS B 1 276 ? -32.985 13.797  3.052   1.00 68.61  ? 1493 HIS B ND1   1 
ATOM   5876 C  CD2   . HIS B 1 276 ? -31.722 12.044  3.367   1.00 70.39  ? 1493 HIS B CD2   1 
ATOM   5877 C  CE1   . HIS B 1 276 ? -32.384 13.534  1.904   1.00 71.84  ? 1493 HIS B CE1   1 
ATOM   5878 N  NE2   . HIS B 1 276 ? -31.613 12.475  2.068   1.00 64.80  ? 1493 HIS B NE2   1 
ATOM   5879 N  N     . ALA B 1 277 ? -33.627 13.979  8.487   1.00 73.18  ? 1494 ALA B N     1 
ATOM   5880 C  CA    . ALA B 1 277 ? -34.552 13.771  9.593   1.00 77.45  ? 1494 ALA B CA    1 
ATOM   5881 C  C     . ALA B 1 277 ? -35.229 15.089  9.946   1.00 79.66  ? 1494 ALA B C     1 
ATOM   5882 O  O     . ALA B 1 277 ? -34.582 16.140  9.998   1.00 72.67  ? 1494 ALA B O     1 
ATOM   5883 C  CB    . ALA B 1 277 ? -33.809 13.187  10.802  1.00 70.32  ? 1494 ALA B CB    1 
ATOM   5884 N  N     . ASP B 1 278 ? -36.548 15.042  10.153  1.00 83.74  ? 1495 ASP B N     1 
ATOM   5885 C  CA    . ASP B 1 278 ? -37.284 16.263  10.445  1.00 84.75  ? 1495 ASP B CA    1 
ATOM   5886 C  C     . ASP B 1 278 ? -37.660 16.319  11.930  1.00 84.12  ? 1495 ASP B C     1 
ATOM   5887 O  O     . ASP B 1 278 ? -36.995 15.715  12.779  1.00 77.37  ? 1495 ASP B O     1 
ATOM   5888 C  CB    . ASP B 1 278 ? -38.488 16.399  9.483   1.00 83.34  ? 1495 ASP B CB    1 
ATOM   5889 C  CG    . ASP B 1 278 ? -39.568 15.341  9.682   1.00 78.87  ? 1495 ASP B CG    1 
ATOM   5890 O  OD1   . ASP B 1 278 ? -39.799 14.873  10.817  1.00 76.10  ? 1495 ASP B OD1   1 
ATOM   5891 O  OD2   . ASP B 1 278 ? -40.216 14.997  8.668   1.00 76.43  ? 1495 ASP B OD2   1 
ATOM   5892 N  N     . ASN B 1 279 ? -38.667 17.118  12.253  1.00 95.51  ? 1496 ASN B N     1 
ATOM   5893 C  CA    . ASN B 1 279 ? -39.062 17.292  13.644  1.00 97.70  ? 1496 ASN B CA    1 
ATOM   5894 C  C     . ASN B 1 279 ? -40.016 16.207  14.128  1.00 87.86  ? 1496 ASN B C     1 
ATOM   5895 O  O     . ASN B 1 279 ? -40.466 16.252  15.277  1.00 84.36  ? 1496 ASN B O     1 
ATOM   5896 C  CB    . ASN B 1 279 ? -39.664 18.690  13.833  1.00 98.83  ? 1496 ASN B CB    1 
ATOM   5897 C  CG    . ASN B 1 279 ? -38.615 19.757  13.772  1.00 100.02 ? 1496 ASN B CG    1 
ATOM   5898 O  OD1   . ASN B 1 279 ? -37.490 19.545  14.230  1.00 100.17 ? 1496 ASN B OD1   1 
ATOM   5899 N  ND2   . ASN B 1 279 ? -38.954 20.911  13.193  1.00 103.60 ? 1496 ASN B ND2   1 
ATOM   5900 N  N     . GLN B 1 280 ? -40.316 15.221  13.302  1.00 88.15  ? 1497 GLN B N     1 
ATOM   5901 C  CA    . GLN B 1 280 ? -41.096 14.085  13.754  1.00 92.61  ? 1497 GLN B CA    1 
ATOM   5902 C  C     . GLN B 1 280 ? -40.257 12.822  13.880  1.00 81.35  ? 1497 GLN B C     1 
ATOM   5903 O  O     . GLN B 1 280 ? -40.776 11.788  14.305  1.00 89.13  ? 1497 GLN B O     1 
ATOM   5904 C  CB    . GLN B 1 280 ? -42.288 13.876  12.814  1.00 104.35 ? 1497 GLN B CB    1 
ATOM   5905 C  CG    . GLN B 1 280 ? -43.047 15.180  12.528  1.00 114.70 ? 1497 GLN B CG    1 
ATOM   5906 C  CD    . GLN B 1 280 ? -43.540 15.278  11.099  1.00 121.72 ? 1497 GLN B CD    1 
ATOM   5907 O  OE1   . GLN B 1 280 ? -44.590 14.741  10.754  1.00 122.66 ? 1497 GLN B OE1   1 
ATOM   5908 N  NE2   . GLN B 1 280 ? -42.780 15.971  10.257  1.00 126.53 ? 1497 GLN B NE2   1 
ATOM   5909 N  N     . GLY B 1 281 ? -38.974 12.892  13.555  1.00 68.45  ? 1498 GLY B N     1 
ATOM   5910 C  CA    . GLY B 1 281 ? -38.069 11.760  13.686  1.00 79.08  ? 1498 GLY B CA    1 
ATOM   5911 C  C     . GLY B 1 281 ? -37.290 11.478  12.409  1.00 79.47  ? 1498 GLY B C     1 
ATOM   5912 O  O     . GLY B 1 281 ? -37.000 12.390  11.628  1.00 82.65  ? 1498 GLY B O     1 
ATOM   5913 N  N     . LEU B 1 282 ? -36.929 10.202  12.213  1.00 69.02  ? 1499 LEU B N     1 
ATOM   5914 C  CA    . LEU B 1 282 ? -36.217 9.821   10.997  1.00 68.21  ? 1499 LEU B CA    1 
ATOM   5915 C  C     . LEU B 1 282 ? -37.140 9.851   9.792   1.00 75.33  ? 1499 LEU B C     1 
ATOM   5916 O  O     . LEU B 1 282 ? -38.363 9.763   9.918   1.00 89.80  ? 1499 LEU B O     1 
ATOM   5917 C  CB    . LEU B 1 282 ? -35.620 8.428   11.115  1.00 63.80  ? 1499 LEU B CB    1 
ATOM   5918 C  CG    . LEU B 1 282 ? -34.373 8.278   11.981  1.00 73.40  ? 1499 LEU B CG    1 
ATOM   5919 C  CD1   . LEU B 1 282 ? -34.365 6.898   12.581  1.00 72.44  ? 1499 LEU B CD1   1 
ATOM   5920 C  CD2   . LEU B 1 282 ? -33.057 8.541   11.216  1.00 75.71  ? 1499 LEU B CD2   1 
ATOM   5921 N  N     . VAL B 1 283 ? -36.551 10.054  8.617   1.00 75.54  ? 1500 VAL B N     1 
ATOM   5922 C  CA    . VAL B 1 283 ? -37.231 9.724   7.368   1.00 75.38  ? 1500 VAL B CA    1 
ATOM   5923 C  C     . VAL B 1 283 ? -36.164 9.098   6.492   1.00 77.64  ? 1500 VAL B C     1 
ATOM   5924 O  O     . VAL B 1 283 ? -35.265 9.791   6.009   1.00 79.84  ? 1500 VAL B O     1 
ATOM   5925 C  CB    . VAL B 1 283 ? -37.940 10.915  6.682   1.00 76.79  ? 1500 VAL B CB    1 
ATOM   5926 C  CG1   . VAL B 1 283 ? -37.099 12.120  6.623   1.00 78.52  ? 1500 VAL B CG1   1 
ATOM   5927 C  CG2   . VAL B 1 283 ? -38.405 10.544  5.254   1.00 76.27  ? 1500 VAL B CG2   1 
ATOM   5928 N  N     . LEU B 1 284 ? -36.289 7.791   6.269   1.00 78.57  ? 1501 LEU B N     1 
ATOM   5929 C  CA    . LEU B 1 284 ? -35.287 6.954   5.652   1.00 74.20  ? 1501 LEU B CA    1 
ATOM   5930 C  C     . LEU B 1 284 ? -35.413 7.005   4.136   1.00 71.08  ? 1501 LEU B C     1 
ATOM   5931 O  O     . LEU B 1 284 ? -36.518 6.844   3.610   1.00 73.40  ? 1501 LEU B O     1 
ATOM   5932 C  CB    . LEU B 1 284 ? -35.479 5.527   6.129   1.00 80.46  ? 1501 LEU B CB    1 
ATOM   5933 C  CG    . LEU B 1 284 ? -35.713 5.373   7.632   1.00 77.94  ? 1501 LEU B CG    1 
ATOM   5934 C  CD1   . LEU B 1 284 ? -35.871 3.881   8.017   1.00 59.61  ? 1501 LEU B CD1   1 
ATOM   5935 C  CD2   . LEU B 1 284 ? -34.581 6.051   8.411   1.00 87.51  ? 1501 LEU B CD2   1 
ATOM   5936 N  N     . PRO B 1 285 ? -34.314 7.187   3.413   1.00 68.13  ? 1502 PRO B N     1 
ATOM   5937 C  CA    . PRO B 1 285 ? -34.341 7.031   1.957   1.00 74.45  ? 1502 PRO B CA    1 
ATOM   5938 C  C     . PRO B 1 285 ? -34.868 5.660   1.581   1.00 78.55  ? 1502 PRO B C     1 
ATOM   5939 O  O     . PRO B 1 285 ? -34.442 4.647   2.164   1.00 71.59  ? 1502 PRO B O     1 
ATOM   5940 C  CB    . PRO B 1 285 ? -32.864 7.183   1.546   1.00 71.71  ? 1502 PRO B CB    1 
ATOM   5941 C  CG    . PRO B 1 285 ? -32.135 7.693   2.769   1.00 67.33  ? 1502 PRO B CG    1 
ATOM   5942 C  CD    . PRO B 1 285 ? -32.946 7.243   3.954   1.00 60.55  ? 1502 PRO B CD    1 
ATOM   5943 N  N     . PRO B 1 286 ? -35.812 5.591   0.634   1.00 79.30  ? 1503 PRO B N     1 
ATOM   5944 C  CA    . PRO B 1 286 ? -36.425 4.293   0.304   1.00 81.49  ? 1503 PRO B CA    1 
ATOM   5945 C  C     . PRO B 1 286 ? -35.418 3.172   0.071   1.00 69.25  ? 1503 PRO B C     1 
ATOM   5946 O  O     . PRO B 1 286 ? -35.678 2.032   0.482   1.00 82.61  ? 1503 PRO B O     1 
ATOM   5947 C  CB    . PRO B 1 286 ? -37.238 4.610   -0.963  1.00 82.57  ? 1503 PRO B CB    1 
ATOM   5948 C  CG    . PRO B 1 286 ? -37.583 6.040   -0.840  1.00 78.53  ? 1503 PRO B CG    1 
ATOM   5949 C  CD    . PRO B 1 286 ? -36.417 6.694   -0.132  1.00 79.19  ? 1503 PRO B CD    1 
ATOM   5950 N  N     . ARG B 1 287 ? -34.264 3.458   -0.531  1.00 60.17  ? 1504 ARG B N     1 
ATOM   5951 C  CA    . ARG B 1 287 ? -33.358 2.387   -0.945  1.00 59.95  ? 1504 ARG B CA    1 
ATOM   5952 C  C     . ARG B 1 287 ? -32.549 1.789   0.207   1.00 57.13  ? 1504 ARG B C     1 
ATOM   5953 O  O     . ARG B 1 287 ? -31.920 0.745   0.024   1.00 73.34  ? 1504 ARG B O     1 
ATOM   5954 C  CB    . ARG B 1 287 ? -32.415 2.885   -2.042  1.00 57.78  ? 1504 ARG B CB    1 
ATOM   5955 C  CG    . ARG B 1 287 ? -33.113 3.242   -3.345  1.00 63.90  ? 1504 ARG B CG    1 
ATOM   5956 C  CD    . ARG B 1 287 ? -32.904 2.169   -4.403  1.00 72.04  ? 1504 ARG B CD    1 
ATOM   5957 N  NE    . ARG B 1 287 ? -31.906 2.546   -5.402  1.00 85.74  ? 1504 ARG B NE    1 
ATOM   5958 C  CZ    . ARG B 1 287 ? -30.880 1.783   -5.771  1.00 99.51  ? 1504 ARG B CZ    1 
ATOM   5959 N  NH1   . ARG B 1 287 ? -30.699 0.584   -5.223  1.00 96.68  ? 1504 ARG B NH1   1 
ATOM   5960 N  NH2   . ARG B 1 287 ? -30.031 2.219   -6.697  1.00 104.28 ? 1504 ARG B NH2   1 
ATOM   5961 N  N     . VAL B 1 288 ? -32.571 2.387   1.392   1.00 54.03  ? 1505 VAL B N     1 
ATOM   5962 C  CA    . VAL B 1 288 ? -31.925 1.806   2.563   1.00 59.01  ? 1505 VAL B CA    1 
ATOM   5963 C  C     . VAL B 1 288 ? -32.908 1.453   3.671   1.00 65.66  ? 1505 VAL B C     1 
ATOM   5964 O  O     . VAL B 1 288 ? -32.492 0.867   4.684   1.00 63.93  ? 1505 VAL B O     1 
ATOM   5965 C  CB    . VAL B 1 288 ? -30.819 2.732   3.116   1.00 62.26  ? 1505 VAL B CB    1 
ATOM   5966 C  CG1   . VAL B 1 288 ? -29.846 3.072   2.023   1.00 58.71  ? 1505 VAL B CG1   1 
ATOM   5967 C  CG2   . VAL B 1 288 ? -31.429 3.995   3.686   1.00 75.35  ? 1505 VAL B CG2   1 
ATOM   5968 N  N     . ALA B 1 289 ? -34.185 1.795   3.544   1.00 69.49  ? 1506 ALA B N     1 
ATOM   5969 C  CA    . ALA B 1 289 ? -35.114 1.522   4.632   1.00 66.22  ? 1506 ALA B CA    1 
ATOM   5970 C  C     . ALA B 1 289 ? -35.390 0.017   4.729   1.00 70.98  ? 1506 ALA B C     1 
ATOM   5971 O  O     . ALA B 1 289 ? -35.781 -0.614  3.742   1.00 60.73  ? 1506 ALA B O     1 
ATOM   5972 C  CB    . ALA B 1 289 ? -36.394 2.324   4.421   1.00 54.67  ? 1506 ALA B CB    1 
ATOM   5973 N  N     . CYS B 1 290 ? -35.128 -0.565  5.909   1.00 79.51  ? 1507 CYS B N     1 
ATOM   5974 C  CA    . CYS B 1 290 ? -35.422 -1.982  6.150   1.00 71.62  ? 1507 CYS B CA    1 
ATOM   5975 C  C     . CYS B 1 290 ? -36.855 -2.312  5.752   1.00 78.12  ? 1507 CYS B C     1 
ATOM   5976 O  O     . CYS B 1 290 ? -37.101 -3.242  4.964   1.00 77.08  ? 1507 CYS B O     1 
ATOM   5977 C  CB    . CYS B 1 290 ? -35.154 -2.321  7.631   1.00 70.26  ? 1507 CYS B CB    1 
ATOM   5978 S  SG    . CYS B 1 290 ? -35.586 -4.001  8.241   1.00 90.84  ? 1507 CYS B SG    1 
ATOM   5979 N  N     . ILE B 1 291 ? -37.810 -1.510  6.232   1.00 78.87  ? 1508 ILE B N     1 
ATOM   5980 C  CA    . ILE B 1 291 ? -39.201 -1.604  5.818   1.00 71.42  ? 1508 ILE B CA    1 
ATOM   5981 C  C     . ILE B 1 291 ? -39.515 -0.365  4.999   1.00 72.97  ? 1508 ILE B C     1 
ATOM   5982 O  O     . ILE B 1 291 ? -39.438 0.755   5.514   1.00 75.51  ? 1508 ILE B O     1 
ATOM   5983 C  CB    . ILE B 1 291 ? -40.148 -1.732  7.018   1.00 70.59  ? 1508 ILE B CB    1 
ATOM   5984 C  CG1   . ILE B 1 291 ? -39.603 -2.754  8.008   1.00 65.40  ? 1508 ILE B CG1   1 
ATOM   5985 C  CG2   . ILE B 1 291 ? -41.528 -2.153  6.555   1.00 71.95  ? 1508 ILE B CG2   1 
ATOM   5986 C  CD1   . ILE B 1 291 ? -40.378 -2.822  9.282   1.00 58.85  ? 1508 ILE B CD1   1 
ATOM   5987 N  N     . GLN B 1 292 ? -39.892 -0.564  3.737   1.00 64.55  ? 1509 GLN B N     1 
ATOM   5988 C  CA    . GLN B 1 292 ? -40.250 0.581   2.917   1.00 67.96  ? 1509 GLN B CA    1 
ATOM   5989 C  C     . GLN B 1 292 ? -41.673 1.018   3.191   1.00 81.06  ? 1509 GLN B C     1 
ATOM   5990 O  O     . GLN B 1 292 ? -41.972 2.223   3.194   1.00 79.86  ? 1509 GLN B O     1 
ATOM   5991 C  CB    . GLN B 1 292 ? -40.061 0.249   1.441   1.00 62.74  ? 1509 GLN B CB    1 
ATOM   5992 C  CG    . GLN B 1 292 ? -38.607 0.291   1.027   1.00 72.17  ? 1509 GLN B CG    1 
ATOM   5993 C  CD    . GLN B 1 292 ? -38.351 -0.375  -0.314  1.00 79.53  ? 1509 GLN B CD    1 
ATOM   5994 O  OE1   . GLN B 1 292 ? -39.028 -1.334  -0.704  1.00 70.12  ? 1509 GLN B OE1   1 
ATOM   5995 N  NE2   . GLN B 1 292 ? -37.359 0.138   -1.031  1.00 88.25  ? 1509 GLN B NE2   1 
ATOM   5996 N  N     . VAL B 1 293 ? -42.554 0.044   3.418   1.00 79.80  ? 1510 VAL B N     1 
ATOM   5997 C  CA    . VAL B 1 293 ? -43.982 0.253   3.633   1.00 72.98  ? 1510 VAL B CA    1 
ATOM   5998 C  C     . VAL B 1 293 ? -44.392 -0.527  4.866   1.00 70.50  ? 1510 VAL B C     1 
ATOM   5999 O  O     . VAL B 1 293 ? -44.092 -1.724  4.950   1.00 65.08  ? 1510 VAL B O     1 
ATOM   6000 C  CB    . VAL B 1 293 ? -44.803 -0.227  2.430   1.00 67.12  ? 1510 VAL B CB    1 
ATOM   6001 C  CG1   . VAL B 1 293 ? -46.229 0.057   2.705   1.00 63.95  ? 1510 VAL B CG1   1 
ATOM   6002 C  CG2   . VAL B 1 293 ? -44.334 0.416   1.138   1.00 70.95  ? 1510 VAL B CG2   1 
ATOM   6003 N  N     . VAL B 1 294 ? -45.101 0.115   5.803   1.00 65.25  ? 1511 VAL B N     1 
ATOM   6004 C  CA    . VAL B 1 294 ? -45.686 -0.606  6.939   1.00 71.75  ? 1511 VAL B CA    1 
ATOM   6005 C  C     . VAL B 1 294 ? -47.207 -0.468  6.894   1.00 82.35  ? 1511 VAL B C     1 
ATOM   6006 O  O     . VAL B 1 294 ? -47.728 0.655   6.776   1.00 96.14  ? 1511 VAL B O     1 
ATOM   6007 C  CB    . VAL B 1 294 ? -45.114 -0.129  8.299   1.00 65.61  ? 1511 VAL B CB    1 
ATOM   6008 C  CG1   . VAL B 1 294 ? -45.382 1.353   8.543   1.00 78.07  ? 1511 VAL B CG1   1 
ATOM   6009 C  CG2   . VAL B 1 294 ? -45.730 -0.934  9.438   1.00 64.62  ? 1511 VAL B CG2   1 
ATOM   6010 N  N     . ILE B 1 295 ? -47.907 -1.607  7.028   1.00 73.30  ? 1512 ILE B N     1 
ATOM   6011 C  CA    . ILE B 1 295 ? -49.368 -1.680  6.945   1.00 77.64  ? 1512 ILE B CA    1 
ATOM   6012 C  C     . ILE B 1 295 ? -49.939 -1.583  8.356   1.00 84.63  ? 1512 ILE B C     1 
ATOM   6013 O  O     . ILE B 1 295 ? -49.782 -2.492  9.167   1.00 71.81  ? 1512 ILE B O     1 
ATOM   6014 C  CB    . ILE B 1 295 ? -49.851 -2.986  6.284   1.00 75.03  ? 1512 ILE B CB    1 
ATOM   6015 C  CG1   . ILE B 1 295 ? -49.154 -3.282  4.946   1.00 64.26  ? 1512 ILE B CG1   1 
ATOM   6016 C  CG2   . ILE B 1 295 ? -51.377 -2.951  6.116   1.00 87.60  ? 1512 ILE B CG2   1 
ATOM   6017 C  CD1   . ILE B 1 295 ? -49.807 -2.691  3.716   1.00 72.18  ? 1512 ILE B CD1   1 
ATOM   6018 N  N     . VAL B 1 296 ? -50.649 -0.512  8.673   1.00 93.81  ? 1513 VAL B N     1 
ATOM   6019 C  CA    . VAL B 1 296 ? -51.332 -0.432  9.959   1.00 98.85  ? 1513 VAL B CA    1 
ATOM   6020 C  C     . VAL B 1 296 ? -52.813 -0.698  9.709   1.00 98.27  ? 1513 VAL B C     1 
ATOM   6021 O  O     . VAL B 1 296 ? -53.462 0.093   9.008   1.00 89.11  ? 1513 VAL B O     1 
ATOM   6022 C  CB    . VAL B 1 296 ? -51.103 0.918   10.644  1.00 93.88  ? 1513 VAL B CB    1 
ATOM   6023 C  CG1   . VAL B 1 296 ? -51.623 0.867   12.089  1.00 96.91  ? 1513 VAL B CG1   1 
ATOM   6024 C  CG2   . VAL B 1 296 ? -49.634 1.279   10.610  1.00 81.58  ? 1513 VAL B CG2   1 
ATOM   6025 N  N     . PRO B 1 297 ? -53.372 -1.794  10.220  1.00 101.06 ? 1514 PRO B N     1 
ATOM   6026 C  CA    . PRO B 1 297 ? -54.817 -2.006  10.116  1.00 100.46 ? 1514 PRO B CA    1 
ATOM   6027 C  C     . PRO B 1 297 ? -55.529 -1.047  11.057  1.00 100.02 ? 1514 PRO B C     1 
ATOM   6028 O  O     . PRO B 1 297 ? -55.121 -0.887  12.208  1.00 95.98  ? 1514 PRO B O     1 
ATOM   6029 C  CB    . PRO B 1 297 ? -54.997 -3.460  10.553  1.00 101.67 ? 1514 PRO B CB    1 
ATOM   6030 C  CG    . PRO B 1 297 ? -53.826 -3.748  11.403  1.00 97.66  ? 1514 PRO B CG    1 
ATOM   6031 C  CD    . PRO B 1 297 ? -52.692 -2.908  10.897  1.00 98.12  ? 1514 PRO B CD    1 
ATOM   6032 N  N     . CYS B 1 298 ? -56.557 -0.369  10.552  1.00 106.24 ? 1515 CYS B N     1 
ATOM   6033 C  CA    . CYS B 1 298 ? -57.264 0.679   11.278  1.00 104.95 ? 1515 CYS B CA    1 
ATOM   6034 C  C     . CYS B 1 298 ? -58.680 0.226   11.615  1.00 100.66 ? 1515 CYS B C     1 
ATOM   6035 O  O     . CYS B 1 298 ? -59.262 -0.677  10.998  1.00 89.67  ? 1515 CYS B O     1 
ATOM   6036 C  CB    . CYS B 1 298 ? -57.398 2.001   10.494  1.00 108.24 ? 1515 CYS B CB    1 
ATOM   6037 S  SG    . CYS B 1 298 ? -56.136 2.516   9.326   1.00 121.26 ? 1515 CYS B SG    1 
ATOM   6038 N  N     . GLY B 1 299 ? -59.251 0.901   12.600  1.00 103.31 ? 1516 GLY B N     1 
ATOM   6039 C  CA    . GLY B 1 299 ? -60.644 0.669   12.863  1.00 116.79 ? 1516 GLY B CA    1 
ATOM   6040 C  C     . GLY B 1 299 ? -60.934 -0.522  13.734  1.00 109.46 ? 1516 GLY B C     1 
ATOM   6041 O  O     . GLY B 1 299 ? -62.102 -0.895  13.852  1.00 110.17 ? 1516 GLY B O     1 
ATOM   6042 N  N     . ILE B 1 300 ? -59.928 -1.151  14.339  1.00 106.56 ? 1517 ILE B N     1 
ATOM   6043 C  CA    . ILE B 1 300 ? -60.285 -2.224  15.256  1.00 107.60 ? 1517 ILE B CA    1 
ATOM   6044 C  C     . ILE B 1 300 ? -60.967 -1.520  16.420  1.00 120.34 ? 1517 ILE B C     1 
ATOM   6045 O  O     . ILE B 1 300 ? -60.333 -0.779  17.174  1.00 121.90 ? 1517 ILE B O     1 
ATOM   6046 C  CB    . ILE B 1 300 ? -59.068 -3.036  15.704  1.00 101.03 ? 1517 ILE B CB    1 
ATOM   6047 N  N     . THR B 1 301 ? -62.273 -1.737  16.552  1.00 132.44 ? 1518 THR B N     1 
ATOM   6048 C  CA    . THR B 1 301 ? -63.107 -0.928  17.433  1.00 139.67 ? 1518 THR B CA    1 
ATOM   6049 C  C     . THR B 1 301 ? -63.287 -1.564  18.797  1.00 144.23 ? 1518 THR B C     1 
ATOM   6050 O  O     . THR B 1 301 ? -64.393 -1.581  19.342  1.00 154.73 ? 1518 THR B O     1 
ATOM   6051 C  CB    . THR B 1 301 ? -64.459 -0.649  16.781  1.00 137.26 ? 1518 THR B CB    1 
ATOM   6052 N  N     . ALA B 1 302 ? -62.187 -2.079  19.354  1.00 137.77 ? 1519 ALA B N     1 
ATOM   6053 C  CA    . ALA B 1 302 ? -62.113 -2.564  20.725  1.00 141.02 ? 1519 ALA B CA    1 
ATOM   6054 C  C     . ALA B 1 302 ? -63.337 -3.382  21.120  1.00 144.46 ? 1519 ALA B C     1 
ATOM   6055 O  O     . ALA B 1 302 ? -64.220 -2.890  21.830  1.00 141.92 ? 1519 ALA B O     1 
ATOM   6056 C  CB    . ALA B 1 302 ? -61.926 -1.378  21.677  1.00 143.85 ? 1519 ALA B CB    1 
ATOM   6057 N  N     . THR B 1 303 ? -63.392 -4.629  20.660  1.00 147.70 ? 1520 THR B N     1 
ATOM   6058 C  CA    . THR B 1 303 ? -64.494 -5.549  20.930  1.00 151.91 ? 1520 THR B CA    1 
ATOM   6059 C  C     . THR B 1 303 ? -65.845 -5.011  20.464  1.00 155.65 ? 1520 THR B C     1 
ATOM   6060 O  O     . THR B 1 303 ? -66.885 -5.432  20.975  1.00 163.66 ? 1520 THR B O     1 
ATOM   6061 C  CB    . THR B 1 303 ? -64.569 -5.916  22.420  1.00 151.55 ? 1520 THR B CB    1 
ATOM   6062 N  N     . THR B 1 304 ? -65.867 -4.073  19.507  1.00 152.17 ? 1521 THR B N     1 
ATOM   6063 C  CA    . THR B 1 304 ? -67.089 -3.886  18.730  1.00 146.41 ? 1521 THR B CA    1 
ATOM   6064 C  C     . THR B 1 304 ? -67.363 -5.114  17.877  1.00 159.12 ? 1521 THR B C     1 
ATOM   6065 O  O     . THR B 1 304 ? -68.524 -5.419  17.580  1.00 167.99 ? 1521 THR B O     1 
ATOM   6066 C  CB    . THR B 1 304 ? -67.005 -2.650  17.841  1.00 130.78 ? 1521 THR B CB    1 
ATOM   6067 N  N     . THR B 1 305 ? -66.307 -5.824  17.484  1.00 153.64 ? 1522 THR B N     1 
ATOM   6068 C  CA    . THR B 1 305 ? -66.407 -7.020  16.664  1.00 146.88 ? 1522 THR B CA    1 
ATOM   6069 C  C     . THR B 1 305 ? -65.101 -7.793  16.817  1.00 133.95 ? 1522 THR B C     1 
ATOM   6070 O  O     . THR B 1 305 ? -64.044 -7.186  17.019  1.00 122.32 ? 1522 THR B O     1 
ATOM   6071 C  CB    . THR B 1 305 ? -66.683 -6.648  15.203  1.00 146.99 ? 1522 THR B CB    1 
ATOM   6072 N  N     . ASP B 1 306 ? -65.183 -9.139  16.724  1.00 134.96 ? 1523 ASP B N     1 
ATOM   6073 C  CA    . ASP B 1 306 ? -64.042 -10.040 16.930  1.00 140.10 ? 1523 ASP B CA    1 
ATOM   6074 C  C     . ASP B 1 306 ? -63.711 -10.912 15.729  1.00 146.96 ? 1523 ASP B C     1 
ATOM   6075 O  O     . ASP B 1 306 ? -62.527 -11.150 15.456  1.00 143.86 ? 1523 ASP B O     1 
ATOM   6076 C  CB    . ASP B 1 306 ? -64.287 -10.972 18.138  1.00 136.81 ? 1523 ASP B CB    1 
ATOM   6077 C  CG    . ASP B 1 306 ? -63.054 -11.832 18.505  1.00 130.07 ? 1523 ASP B CG    1 
ATOM   6078 O  OD1   . ASP B 1 306 ? -62.672 -11.816 19.691  1.00 130.59 ? 1523 ASP B OD1   1 
ATOM   6079 O  OD2   . ASP B 1 306 ? -62.468 -12.538 17.646  1.00 122.64 ? 1523 ASP B OD2   1 
ATOM   6080 N  N     . ASP B 1 307 ? -64.710 -11.394 14.990  1.00 151.40 ? 1524 ASP B N     1 
ATOM   6081 C  CA    . ASP B 1 307 ? -64.409 -12.257 13.860  1.00 149.83 ? 1524 ASP B CA    1 
ATOM   6082 C  C     . ASP B 1 307 ? -63.685 -11.472 12.781  1.00 131.40 ? 1524 ASP B C     1 
ATOM   6083 O  O     . ASP B 1 307 ? -62.678 -11.941 12.220  1.00 124.86 ? 1524 ASP B O     1 
ATOM   6084 C  CB    . ASP B 1 307 ? -65.694 -12.854 13.289  1.00 160.68 ? 1524 ASP B CB    1 
ATOM   6085 N  N     . GLU B 1 308 ? -64.151 -10.249 12.528  1.00 128.56 ? 1525 GLU B N     1 
ATOM   6086 C  CA    . GLU B 1 308 ? -63.488 -9.307  11.640  1.00 124.99 ? 1525 GLU B CA    1 
ATOM   6087 C  C     . GLU B 1 308 ? -62.020 -9.069  11.961  1.00 110.65 ? 1525 GLU B C     1 
ATOM   6088 O  O     . GLU B 1 308 ? -61.273 -8.738  11.037  1.00 112.66 ? 1525 GLU B O     1 
ATOM   6089 C  CB    . GLU B 1 308 ? -64.234 -7.970  11.675  1.00 123.74 ? 1525 GLU B CB    1 
ATOM   6090 C  CG    . GLU B 1 308 ? -65.717 -8.036  11.348  1.00 110.81 ? 1525 GLU B CG    1 
ATOM   6091 C  CD    . GLU B 1 308 ? -66.510 -8.597  12.517  1.00 125.29 ? 1525 GLU B CD    1 
ATOM   6092 O  OE1   . GLU B 1 308 ? -65.860 -9.111  13.456  1.00 122.69 ? 1525 GLU B OE1   1 
ATOM   6093 O  OE2   . GLU B 1 308 ? -67.760 -8.441  12.556  1.00 133.13 ? 1525 GLU B OE2   1 
ATOM   6094 N  N     . ARG B 1 309 ? -61.583 -9.243  13.218  1.00 106.78 ? 1526 ARG B N     1 
ATOM   6095 C  CA    . ARG B 1 309 ? -60.173 -8.997  13.541  1.00 117.89 ? 1526 ARG B CA    1 
ATOM   6096 C  C     . ARG B 1 309 ? -59.257 -9.825  12.653  1.00 117.87 ? 1526 ARG B C     1 
ATOM   6097 O  O     . ARG B 1 309 ? -58.315 -9.303  12.033  1.00 109.37 ? 1526 ARG B O     1 
ATOM   6098 C  CB    . ARG B 1 309 ? -59.906 -9.321  15.010  1.00 120.48 ? 1526 ARG B CB    1 
ATOM   6099 N  N     . ARG B 1 310 ? -59.571 -11.115 12.528  1.00 117.55 ? 1527 ARG B N     1 
ATOM   6100 C  CA    . ARG B 1 310 ? -58.787 -11.974 11.658  1.00 110.58 ? 1527 ARG B CA    1 
ATOM   6101 C  C     . ARG B 1 310 ? -58.997 -11.623 10.189  1.00 101.82 ? 1527 ARG B C     1 
ATOM   6102 O  O     . ARG B 1 310 ? -58.047 -11.665 9.406   1.00 101.23 ? 1527 ARG B O     1 
ATOM   6103 C  CB    . ARG B 1 310 ? -59.124 -13.442 11.916  1.00 111.98 ? 1527 ARG B CB    1 
ATOM   6104 C  CG    . ARG B 1 310 ? -58.385 -14.035 13.092  1.00 110.58 ? 1527 ARG B CG    1 
ATOM   6105 C  CD    . ARG B 1 310 ? -58.757 -15.484 13.270  1.00 112.18 ? 1527 ARG B CD    1 
ATOM   6106 N  NE    . ARG B 1 310 ? -59.866 -15.682 14.201  1.00 112.37 ? 1527 ARG B NE    1 
ATOM   6107 C  CZ    . ARG B 1 310 ? -59.701 -15.905 15.499  1.00 111.48 ? 1527 ARG B CZ    1 
ATOM   6108 N  NH1   . ARG B 1 310 ? -58.471 -15.940 16.005  1.00 114.89 ? 1527 ARG B NH1   1 
ATOM   6109 N  NH2   . ARG B 1 310 ? -60.753 -16.088 16.286  1.00 104.43 ? 1527 ARG B NH2   1 
ATOM   6110 N  N     . ARG B 1 311 ? -60.229 -11.271 9.799   1.00 99.93  ? 1528 ARG B N     1 
ATOM   6111 C  CA    . ARG B 1 311 ? -60.514 -10.941 8.402   1.00 92.08  ? 1528 ARG B CA    1 
ATOM   6112 C  C     . ARG B 1 311 ? -59.672 -9.763  7.920   1.00 102.21 ? 1528 ARG B C     1 
ATOM   6113 O  O     . ARG B 1 311 ? -59.041 -9.821  6.853   1.00 96.68  ? 1528 ARG B O     1 
ATOM   6114 C  CB    . ARG B 1 311 ? -62.002 -10.633 8.244   1.00 79.19  ? 1528 ARG B CB    1 
ATOM   6115 N  N     . LEU B 1 312 ? -59.640 -8.688  8.711   1.00 111.01 ? 1529 LEU B N     1 
ATOM   6116 C  CA    . LEU B 1 312 ? -58.855 -7.500  8.373   1.00 104.56 ? 1529 LEU B CA    1 
ATOM   6117 C  C     . LEU B 1 312 ? -57.361 -7.794  8.405   1.00 90.00  ? 1529 LEU B C     1 
ATOM   6118 O  O     . LEU B 1 312 ? -56.629 -7.440  7.470   1.00 86.47  ? 1529 LEU B O     1 
ATOM   6119 C  CB    . LEU B 1 312 ? -59.187 -6.361  9.333   1.00 107.31 ? 1529 LEU B CB    1 
ATOM   6120 C  CG    . LEU B 1 312 ? -58.286 -5.134  9.313   1.00 104.80 ? 1529 LEU B CG    1 
ATOM   6121 C  CD1   . LEU B 1 312 ? -58.337 -4.466  7.948   1.00 104.11 ? 1529 LEU B CD1   1 
ATOM   6122 C  CD2   . LEU B 1 312 ? -58.771 -4.168  10.380  1.00 108.18 ? 1529 LEU B CD2   1 
ATOM   6123 N  N     . TYR B 1 313 ? -56.889 -8.431  9.483   1.00 74.32  ? 1530 TYR B N     1 
ATOM   6124 C  CA    . TYR B 1 313 ? -55.494 -8.842  9.538   1.00 84.27  ? 1530 TYR B CA    1 
ATOM   6125 C  C     . TYR B 1 313 ? -55.108 -9.656  8.305   1.00 97.22  ? 1530 TYR B C     1 
ATOM   6126 O  O     . TYR B 1 313 ? -53.982 -9.548  7.798   1.00 107.21 ? 1530 TYR B O     1 
ATOM   6127 C  CB    . TYR B 1 313 ? -55.263 -9.631  10.830  1.00 96.52  ? 1530 TYR B CB    1 
ATOM   6128 C  CG    . TYR B 1 313 ? -55.044 -8.742  12.037  1.00 106.89 ? 1530 TYR B CG    1 
ATOM   6129 C  CD1   . TYR B 1 313 ? -55.316 -7.375  11.972  1.00 122.35 ? 1530 TYR B CD1   1 
ATOM   6130 C  CD2   . TYR B 1 313 ? -54.554 -9.258  13.231  1.00 100.14 ? 1530 TYR B CD2   1 
ATOM   6131 C  CE1   . TYR B 1 313 ? -55.102 -6.544  13.060  1.00 125.85 ? 1530 TYR B CE1   1 
ATOM   6132 C  CE2   . TYR B 1 313 ? -54.342 -8.435  14.330  1.00 107.87 ? 1530 TYR B CE2   1 
ATOM   6133 C  CZ    . TYR B 1 313 ? -54.614 -7.073  14.240  1.00 118.29 ? 1530 TYR B CZ    1 
ATOM   6134 O  OH    . TYR B 1 313 ? -54.402 -6.237  15.323  1.00 113.98 ? 1530 TYR B OH    1 
ATOM   6135 N  N     . GLU B 1 314 ? -56.047 -10.450 7.791   1.00 102.45 ? 1531 GLU B N     1 
ATOM   6136 C  CA    . GLU B 1 314 ? -55.779 -11.331 6.663   1.00 98.22  ? 1531 GLU B CA    1 
ATOM   6137 C  C     . GLU B 1 314 ? -55.694 -10.561 5.347   1.00 94.02  ? 1531 GLU B C     1 
ATOM   6138 O  O     . GLU B 1 314 ? -54.816 -10.838 4.510   1.00 90.13  ? 1531 GLU B O     1 
ATOM   6139 C  CB    . GLU B 1 314 ? -56.858 -12.419 6.613   1.00 93.20  ? 1531 GLU B CB    1 
ATOM   6140 C  CG    . GLU B 1 314 ? -56.708 -13.429 5.481   1.00 99.45  ? 1531 GLU B CG    1 
ATOM   6141 C  CD    . GLU B 1 314 ? -55.291 -13.996 5.328   1.00 107.70 ? 1531 GLU B CD    1 
ATOM   6142 O  OE1   . GLU B 1 314 ? -54.481 -13.987 6.295   1.00 105.80 ? 1531 GLU B OE1   1 
ATOM   6143 O  OE2   . GLU B 1 314 ? -54.982 -14.446 4.209   1.00 116.48 ? 1531 GLU B OE2   1 
ATOM   6144 N  N     . SER B 1 315 ? -56.596 -9.596  5.137   1.00 97.69  ? 1532 SER B N     1 
ATOM   6145 C  CA    . SER B 1 315 ? -56.475 -8.790  3.924   1.00 94.12  ? 1532 SER B CA    1 
ATOM   6146 C  C     . SER B 1 315 ? -55.195 -7.970  3.949   1.00 97.13  ? 1532 SER B C     1 
ATOM   6147 O  O     . SER B 1 315 ? -54.521 -7.811  2.916   1.00 101.08 ? 1532 SER B O     1 
ATOM   6148 C  CB    . SER B 1 315 ? -57.677 -7.875  3.768   1.00 88.85  ? 1532 SER B CB    1 
ATOM   6149 O  OG    . SER B 1 315 ? -57.657 -7.318  2.474   1.00 94.24  ? 1532 SER B OG    1 
ATOM   6150 N  N     . CYS B 1 316 ? -54.793 -7.530  5.143   1.00 94.48  ? 1533 CYS B N     1 
ATOM   6151 C  CA    . CYS B 1 316 ? -53.521 -6.835  5.271   1.00 91.74  ? 1533 CYS B CA    1 
ATOM   6152 C  C     . CYS B 1 316 ? -52.365 -7.772  4.939   1.00 96.33  ? 1533 CYS B C     1 
ATOM   6153 O  O     . CYS B 1 316 ? -51.368 -7.355  4.335   1.00 92.34  ? 1533 CYS B O     1 
ATOM   6154 C  CB    . CYS B 1 316 ? -53.377 -6.274  6.687   1.00 88.38  ? 1533 CYS B CB    1 
ATOM   6155 S  SG    . CYS B 1 316 ? -54.497 -4.907  7.135   1.00 95.76  ? 1533 CYS B SG    1 
ATOM   6156 N  N     . ARG B 1 317 ? -52.493 -9.056  5.314   1.00 97.99  ? 1534 ARG B N     1 
ATOM   6157 C  CA    . ARG B 1 317 ? -51.443 -10.024 5.018   1.00 89.72  ? 1534 ARG B CA    1 
ATOM   6158 C  C     . ARG B 1 317 ? -51.329 -10.325 3.533   1.00 92.96  ? 1534 ARG B C     1 
ATOM   6159 O  O     . ARG B 1 317 ? -50.205 -10.499 3.045   1.00 99.65  ? 1534 ARG B O     1 
ATOM   6160 C  CB    . ARG B 1 317 ? -51.668 -11.327 5.787   1.00 86.59  ? 1534 ARG B CB    1 
ATOM   6161 N  N     . GLU B 1 318 ? -52.444 -10.334 2.788   1.00 90.92  ? 1535 GLU B N     1 
ATOM   6162 C  CA    . GLU B 1 318 ? -52.261 -10.553 1.362   1.00 100.27 ? 1535 GLU B CA    1 
ATOM   6163 C  C     . GLU B 1 318 ? -51.709 -9.311  0.683   1.00 96.85  ? 1535 GLU B C     1 
ATOM   6164 O  O     . GLU B 1 318 ? -50.942 -9.433  -0.273  1.00 99.80  ? 1535 GLU B O     1 
ATOM   6165 C  CB    . GLU B 1 318 ? -53.543 -10.933 0.623   1.00 121.62 ? 1535 GLU B CB    1 
ATOM   6166 N  N     . LEU B 1 319 ? -52.053 -8.108  1.161   1.00 92.67  ? 1536 LEU B N     1 
ATOM   6167 C  CA    . LEU B 1 319 ? -51.414 -6.928  0.577   1.00 91.95  ? 1536 LEU B CA    1 
ATOM   6168 C  C     . LEU B 1 319 ? -49.911 -6.930  0.866   1.00 81.88  ? 1536 LEU B C     1 
ATOM   6169 O  O     . LEU B 1 319 ? -49.096 -6.697  -0.032  1.00 73.35  ? 1536 LEU B O     1 
ATOM   6170 C  CB    . LEU B 1 319 ? -52.057 -5.637  1.097   1.00 101.03 ? 1536 LEU B CB    1 
ATOM   6171 C  CG    . LEU B 1 319 ? -51.493 -4.327  0.540   1.00 100.17 ? 1536 LEU B CG    1 
ATOM   6172 C  CD1   . LEU B 1 319 ? -51.546 -4.321  -0.982  1.00 94.04  ? 1536 LEU B CD1   1 
ATOM   6173 C  CD2   . LEU B 1 319 ? -52.253 -3.116  1.080   1.00 107.26 ? 1536 LEU B CD2   1 
ATOM   6174 N  N     . GLU B 1 320 ? -49.519 -7.207  2.111   1.00 84.81  ? 1537 GLU B N     1 
ATOM   6175 C  CA    . GLU B 1 320 ? -48.094 -7.285  2.431   1.00 83.76  ? 1537 GLU B CA    1 
ATOM   6176 C  C     . GLU B 1 320 ? -47.406 -8.373  1.618   1.00 95.18  ? 1537 GLU B C     1 
ATOM   6177 O  O     . GLU B 1 320 ? -46.269 -8.194  1.163   1.00 88.54  ? 1537 GLU B O     1 
ATOM   6178 C  CB    . GLU B 1 320 ? -47.913 -7.524  3.932   1.00 81.40  ? 1537 GLU B CB    1 
ATOM   6179 C  CG    . GLU B 1 320 ? -46.604 -8.136  4.391   1.00 78.10  ? 1537 GLU B CG    1 
ATOM   6180 C  CD    . GLU B 1 320 ? -46.649 -8.528  5.871   1.00 76.66  ? 1537 GLU B CD    1 
ATOM   6181 O  OE1   . GLU B 1 320 ? -45.587 -8.650  6.519   1.00 71.38  ? 1537 GLU B OE1   1 
ATOM   6182 O  OE2   . GLU B 1 320 ? -47.764 -8.708  6.396   1.00 79.75  ? 1537 GLU B OE2   1 
ATOM   6183 N  N     . GLN B 1 321 ? -48.098 -9.496  1.387   1.00 106.47 ? 1538 GLN B N     1 
ATOM   6184 C  CA    . GLN B 1 321 ? -47.480 -10.596 0.650   1.00 111.02 ? 1538 GLN B CA    1 
ATOM   6185 C  C     . GLN B 1 321 ? -47.277 -10.225 -0.810  1.00 103.23 ? 1538 GLN B C     1 
ATOM   6186 O  O     . GLN B 1 321 ? -46.240 -10.553 -1.401  1.00 99.11  ? 1538 GLN B O     1 
ATOM   6187 C  CB    . GLN B 1 321 ? -48.315 -11.878 0.768   1.00 113.61 ? 1538 GLN B CB    1 
ATOM   6188 C  CG    . GLN B 1 321 ? -48.203 -12.575 2.109   1.00 114.90 ? 1538 GLN B CG    1 
ATOM   6189 C  CD    . GLN B 1 321 ? -46.834 -12.415 2.729   1.00 120.58 ? 1538 GLN B CD    1 
ATOM   6190 O  OE1   . GLN B 1 321 ? -45.833 -12.892 2.184   1.00 123.38 ? 1538 GLN B OE1   1 
ATOM   6191 N  NE2   . GLN B 1 321 ? -46.775 -11.722 3.868   1.00 119.59 ? 1538 GLN B NE2   1 
ATOM   6192 N  N     . THR B 1 322 ? -48.246 -9.528  -1.406  1.00 103.03 ? 1539 THR B N     1 
ATOM   6193 C  CA    . THR B 1 322 ? -48.055 -9.128  -2.791  1.00 102.26 ? 1539 THR B CA    1 
ATOM   6194 C  C     . THR B 1 322 ? -47.057 -7.982  -2.915  1.00 103.06 ? 1539 THR B C     1 
ATOM   6195 O  O     . THR B 1 322 ? -46.407 -7.859  -3.957  1.00 99.69  ? 1539 THR B O     1 
ATOM   6196 C  CB    . THR B 1 322 ? -49.396 -8.734  -3.429  1.00 100.03 ? 1539 THR B CB    1 
ATOM   6197 O  OG1   . THR B 1 322 ? -50.161 -7.953  -2.514  1.00 94.38  ? 1539 THR B OG1   1 
ATOM   6198 C  CG2   . THR B 1 322 ? -50.211 -9.981  -3.822  1.00 109.25 ? 1539 THR B CG2   1 
ATOM   6199 N  N     . PHE B 1 323 ? -46.846 -7.201  -1.848  1.00 95.38  ? 1540 PHE B N     1 
ATOM   6200 C  CA    . PHE B 1 323 ? -45.770 -6.217  -1.903  1.00 93.65  ? 1540 PHE B CA    1 
ATOM   6201 C  C     . PHE B 1 323 ? -44.419 -6.902  -1.811  1.00 100.40 ? 1540 PHE B C     1 
ATOM   6202 O  O     . PHE B 1 323 ? -43.492 -6.556  -2.553  1.00 105.57 ? 1540 PHE B O     1 
ATOM   6203 C  CB    . PHE B 1 323 ? -45.915 -5.157  -0.807  1.00 83.61  ? 1540 PHE B CB    1 
ATOM   6204 C  CG    . PHE B 1 323 ? -46.887 -4.056  -1.153  1.00 84.18  ? 1540 PHE B CG    1 
ATOM   6205 C  CD1   . PHE B 1 323 ? -47.187 -3.772  -2.479  1.00 79.60  ? 1540 PHE B CD1   1 
ATOM   6206 C  CD2   . PHE B 1 323 ? -47.500 -3.308  -0.159  1.00 83.24  ? 1540 PHE B CD2   1 
ATOM   6207 C  CE1   . PHE B 1 323 ? -48.085 -2.776  -2.814  1.00 78.19  ? 1540 PHE B CE1   1 
ATOM   6208 C  CE2   . PHE B 1 323 ? -48.408 -2.301  -0.489  1.00 86.19  ? 1540 PHE B CE2   1 
ATOM   6209 C  CZ    . PHE B 1 323 ? -48.698 -2.039  -1.819  1.00 84.58  ? 1540 PHE B CZ    1 
ATOM   6210 N  N     . VAL B 1 324 ? -44.280 -7.875  -0.910  1.00 92.14  ? 1541 VAL B N     1 
ATOM   6211 C  CA    . VAL B 1 324 ? -43.019 -8.603  -0.838  1.00 85.80  ? 1541 VAL B CA    1 
ATOM   6212 C  C     . VAL B 1 324 ? -42.722 -9.253  -2.183  1.00 101.04 ? 1541 VAL B C     1 
ATOM   6213 O  O     . VAL B 1 324 ? -41.649 -9.058  -2.765  1.00 106.13 ? 1541 VAL B O     1 
ATOM   6214 C  CB    . VAL B 1 324 ? -43.040 -9.641  0.299   1.00 76.53  ? 1541 VAL B CB    1 
ATOM   6215 C  CG1   . VAL B 1 324 ? -41.623 -10.236 0.493   1.00 65.00  ? 1541 VAL B CG1   1 
ATOM   6216 C  CG2   . VAL B 1 324 ? -43.546 -9.032  1.593   1.00 72.92  ? 1541 VAL B CG2   1 
ATOM   6217 N  N     . LYS B 1 325 ? -43.688 -10.008 -2.712  1.00 106.64 ? 1542 LYS B N     1 
ATOM   6218 C  CA    . LYS B 1 325 ? -43.499 -10.703 -3.981  1.00 108.01 ? 1542 LYS B CA    1 
ATOM   6219 C  C     . LYS B 1 325 ? -43.344 -9.740  -5.158  1.00 99.37  ? 1542 LYS B C     1 
ATOM   6220 O  O     . LYS B 1 325 ? -42.829 -10.139 -6.207  1.00 97.74  ? 1542 LYS B O     1 
ATOM   6221 C  CB    . LYS B 1 325 ? -44.650 -11.704 -4.184  1.00 115.57 ? 1542 LYS B CB    1 
ATOM   6222 C  CG    . LYS B 1 325 ? -44.597 -12.845 -3.134  1.00 118.31 ? 1542 LYS B CG    1 
ATOM   6223 C  CD    . LYS B 1 325 ? -45.691 -13.905 -3.257  1.00 117.03 ? 1542 LYS B CD    1 
ATOM   6224 C  CE    . LYS B 1 325 ? -45.696 -14.826 -2.023  1.00 111.07 ? 1542 LYS B CE    1 
ATOM   6225 N  NZ    . LYS B 1 325 ? -46.868 -15.764 -1.978  1.00 112.05 ? 1542 LYS B NZ    1 
ATOM   6226 N  N     . ALA B 1 326 ? -43.796 -8.495  -5.024  1.00 100.52 ? 1543 ALA B N     1 
ATOM   6227 C  CA    . ALA B 1 326 ? -43.486 -7.452  -5.997  1.00 96.88  ? 1543 ALA B CA    1 
ATOM   6228 C  C     . ALA B 1 326 ? -42.108 -6.839  -5.793  1.00 91.28  ? 1543 ALA B C     1 
ATOM   6229 O  O     . ALA B 1 326 ? -41.768 -5.874  -6.490  1.00 89.82  ? 1543 ALA B O     1 
ATOM   6230 C  CB    . ALA B 1 326 ? -44.538 -6.344  -5.946  1.00 98.72  ? 1543 ALA B CB    1 
ATOM   6231 N  N     . GLY B 1 327 ? -41.320 -7.341  -4.843  1.00 82.62  ? 1544 GLY B N     1 
ATOM   6232 C  CA    . GLY B 1 327 ? -40.027 -6.757  -4.580  1.00 70.79  ? 1544 GLY B CA    1 
ATOM   6233 C  C     . GLY B 1 327 ? -40.043 -5.545  -3.674  1.00 83.01  ? 1544 GLY B C     1 
ATOM   6234 O  O     . GLY B 1 327 ? -38.989 -4.912  -3.490  1.00 72.66  ? 1544 GLY B O     1 
ATOM   6235 N  N     . ILE B 1 328 ? -41.208 -5.173  -3.126  1.00 91.02  ? 1545 ILE B N     1 
ATOM   6236 C  CA    . ILE B 1 328 ? -41.307 -4.053  -2.195  1.00 90.33  ? 1545 ILE B CA    1 
ATOM   6237 C  C     . ILE B 1 328 ? -41.148 -4.599  -0.783  1.00 90.61  ? 1545 ILE B C     1 
ATOM   6238 O  O     . ILE B 1 328 ? -41.801 -5.584  -0.405  1.00 89.77  ? 1545 ILE B O     1 
ATOM   6239 C  CB    . ILE B 1 328 ? -42.652 -3.317  -2.346  1.00 84.13  ? 1545 ILE B CB    1 
ATOM   6240 C  CG1   . ILE B 1 328 ? -42.704 -2.510  -3.640  1.00 80.42  ? 1545 ILE B CG1   1 
ATOM   6241 C  CG2   . ILE B 1 328 ? -42.933 -2.432  -1.142  1.00 81.71  ? 1545 ILE B CG2   1 
ATOM   6242 C  CD1   . ILE B 1 328 ? -44.061 -2.565  -4.310  1.00 94.22  ? 1545 ILE B CD1   1 
ATOM   6243 N  N     . ARG B 1 329 ? -40.281 -3.961  0.002   1.00 80.14  ? 1546 ARG B N     1 
ATOM   6244 C  CA    . ARG B 1 329 ? -40.034 -4.412  1.372   1.00 68.92  ? 1546 ARG B CA    1 
ATOM   6245 C  C     . ARG B 1 329 ? -41.181 -3.900  2.246   1.00 74.66  ? 1546 ARG B C     1 
ATOM   6246 O  O     . ARG B 1 329 ? -41.144 -2.783  2.775   1.00 98.75  ? 1546 ARG B O     1 
ATOM   6247 C  CB    . ARG B 1 329 ? -38.666 -3.940  1.873   1.00 55.30  ? 1546 ARG B CB    1 
ATOM   6248 C  CG    . ARG B 1 329 ? -37.468 -4.530  1.156   1.00 55.67  ? 1546 ARG B CG    1 
ATOM   6249 C  CD    . ARG B 1 329 ? -36.155 -4.213  1.891   1.00 58.11  ? 1546 ARG B CD    1 
ATOM   6250 N  NE    . ARG B 1 329 ? -35.897 -2.783  2.011   1.00 67.97  ? 1546 ARG B NE    1 
ATOM   6251 C  CZ    . ARG B 1 329 ? -35.640 -1.975  0.983   1.00 74.52  ? 1546 ARG B CZ    1 
ATOM   6252 N  NH1   . ARG B 1 329 ? -35.592 -2.458  -0.253  1.00 64.59  ? 1546 ARG B NH1   1 
ATOM   6253 N  NH2   . ARG B 1 329 ? -35.435 -0.674  1.185   1.00 76.79  ? 1546 ARG B NH2   1 
ATOM   6254 N  N     . CYS B 1 330 ? -42.197 -4.742  2.439   1.00 72.10  ? 1547 CYS B N     1 
ATOM   6255 C  CA    . CYS B 1 330 ? -43.372 -4.375  3.228   1.00 75.41  ? 1547 CYS B CA    1 
ATOM   6256 C  C     . CYS B 1 330 ? -43.559 -5.322  4.396   1.00 78.39  ? 1547 CYS B C     1 
ATOM   6257 O  O     . CYS B 1 330 ? -43.550 -6.536  4.208   1.00 87.78  ? 1547 CYS B O     1 
ATOM   6258 C  CB    . CYS B 1 330 ? -44.634 -4.402  2.367   1.00 68.36  ? 1547 CYS B CB    1 
ATOM   6259 S  SG    . CYS B 1 330 ? -46.194 -4.341  3.309   1.00 80.29  ? 1547 CYS B SG    1 
ATOM   6260 N  N     . GLU B 1 331 ? -43.759 -4.761  5.590   1.00 76.49  ? 1548 GLU B N     1 
ATOM   6261 C  CA    . GLU B 1 331 ? -44.184 -5.514  6.760   1.00 77.79  ? 1548 GLU B CA    1 
ATOM   6262 C  C     . GLU B 1 331 ? -45.475 -4.863  7.269   1.00 82.62  ? 1548 GLU B C     1 
ATOM   6263 O  O     . GLU B 1 331 ? -45.661 -3.653  7.134   1.00 84.14  ? 1548 GLU B O     1 
ATOM   6264 C  CB    . GLU B 1 331 ? -43.075 -5.560  7.846   1.00 55.05  ? 1548 GLU B CB    1 
ATOM   6265 N  N     . GLY B 1 332 ? -46.373 -5.663  7.846   1.00 78.08  ? 1549 GLY B N     1 
ATOM   6266 C  CA    . GLY B 1 332 ? -47.622 -5.172  8.414   1.00 69.27  ? 1549 GLY B CA    1 
ATOM   6267 C  C     . GLY B 1 332 ? -47.567 -5.263  9.927   1.00 69.78  ? 1549 GLY B C     1 
ATOM   6268 O  O     . GLY B 1 332 ? -46.838 -6.085  10.473  1.00 75.87  ? 1549 GLY B O     1 
ATOM   6269 N  N     . ASP B 1 333 ? -48.278 -4.378  10.609  1.00 75.70  ? 1550 ASP B N     1 
ATOM   6270 C  CA    . ASP B 1 333 ? -48.281 -4.329  12.073  1.00 89.37  ? 1550 ASP B CA    1 
ATOM   6271 C  C     . ASP B 1 333 ? -49.620 -4.853  12.578  1.00 97.58  ? 1550 ASP B C     1 
ATOM   6272 O  O     . ASP B 1 333 ? -50.600 -4.106  12.664  1.00 102.48 ? 1550 ASP B O     1 
ATOM   6273 C  CB    . ASP B 1 333 ? -48.022 -2.905  12.572  1.00 101.48 ? 1550 ASP B CB    1 
ATOM   6274 C  CG    . ASP B 1 333 ? -47.713 -2.843  14.064  1.00 104.91 ? 1550 ASP B CG    1 
ATOM   6275 O  OD1   . ASP B 1 333 ? -48.081 -3.778  14.808  1.00 104.42 ? 1550 ASP B OD1   1 
ATOM   6276 O  OD2   . ASP B 1 333 ? -47.113 -1.834  14.493  1.00 104.37 ? 1550 ASP B OD2   1 
ATOM   6277 N  N     . TYR B 1 334 ? -49.638 -6.117  12.989  1.00 101.94 ? 1551 TYR B N     1 
ATOM   6278 C  CA    . TYR B 1 334 ? -50.855 -6.769  13.455  1.00 104.40 ? 1551 TYR B CA    1 
ATOM   6279 C  C     . TYR B 1 334 ? -50.855 -6.974  14.964  1.00 107.57 ? 1551 TYR B C     1 
ATOM   6280 O  O     . TYR B 1 334 ? -51.533 -7.875  15.463  1.00 124.43 ? 1551 TYR B O     1 
ATOM   6281 C  CB    . TYR B 1 334 ? -51.043 -8.109  12.739  1.00 97.37  ? 1551 TYR B CB    1 
ATOM   6282 C  CG    . TYR B 1 334 ? -50.704 -8.092  11.264  1.00 91.60  ? 1551 TYR B CG    1 
ATOM   6283 C  CD1   . TYR B 1 334 ? -51.524 -7.438  10.353  1.00 89.29  ? 1551 TYR B CD1   1 
ATOM   6284 C  CD2   . TYR B 1 334 ? -49.561 -8.738  10.781  1.00 93.42  ? 1551 TYR B CD2   1 
ATOM   6285 C  CE1   . TYR B 1 334 ? -51.225 -7.419  9.006   1.00 93.87  ? 1551 TYR B CE1   1 
ATOM   6286 C  CE2   . TYR B 1 334 ? -49.252 -8.725  9.421   1.00 91.97  ? 1551 TYR B CE2   1 
ATOM   6287 C  CZ    . TYR B 1 334 ? -50.094 -8.060  8.540   1.00 98.63  ? 1551 TYR B CZ    1 
ATOM   6288 O  OH    . TYR B 1 334 ? -49.813 -8.029  7.191   1.00 101.30 ? 1551 TYR B OH    1 
ATOM   6289 N  N     . ARG B 1 335 ? -50.089 -6.177  15.701  1.00 95.63  ? 1552 ARG B N     1 
ATOM   6290 C  CA    . ARG B 1 335 ? -50.053 -6.338  17.148  1.00 92.10  ? 1552 ARG B CA    1 
ATOM   6291 C  C     . ARG B 1 335 ? -51.330 -5.803  17.767  1.00 102.62 ? 1552 ARG B C     1 
ATOM   6292 O  O     . ARG B 1 335 ? -51.772 -4.693  17.456  1.00 108.43 ? 1552 ARG B O     1 
ATOM   6293 C  CB    . ARG B 1 335 ? -48.836 -5.632  17.731  1.00 93.33  ? 1552 ARG B CB    1 
ATOM   6294 C  CG    . ARG B 1 335 ? -47.526 -6.301  17.348  1.00 86.78  ? 1552 ARG B CG    1 
ATOM   6295 C  CD    . ARG B 1 335 ? -46.357 -5.489  17.797  1.00 82.44  ? 1552 ARG B CD    1 
ATOM   6296 N  NE    . ARG B 1 335 ? -46.165 -4.342  16.918  1.00 96.03  ? 1552 ARG B NE    1 
ATOM   6297 C  CZ    . ARG B 1 335 ? -45.426 -3.285  17.229  1.00 97.43  ? 1552 ARG B CZ    1 
ATOM   6298 N  NH1   . ARG B 1 335 ? -44.806 -3.248  18.396  1.00 97.19  ? 1552 ARG B NH1   1 
ATOM   6299 N  NH2   . ARG B 1 335 ? -45.300 -2.275  16.373  1.00 94.09  ? 1552 ARG B NH2   1 
ATOM   6300 N  N     . ASP B 1 336 ? -51.911 -6.582  18.670  1.00 110.69 ? 1553 ASP B N     1 
ATOM   6301 C  CA    . ASP B 1 336 ? -53.240 -6.265  19.167  1.00 120.50 ? 1553 ASP B CA    1 
ATOM   6302 C  C     . ASP B 1 336 ? -53.206 -5.318  20.356  1.00 117.12 ? 1553 ASP B C     1 
ATOM   6303 O  O     . ASP B 1 336 ? -54.209 -4.642  20.624  1.00 118.28 ? 1553 ASP B O     1 
ATOM   6304 C  CB    . ASP B 1 336 ? -53.976 -7.558  19.555  1.00 128.29 ? 1553 ASP B CB    1 
ATOM   6305 C  CG    . ASP B 1 336 ? -54.137 -8.526  18.383  1.00 128.93 ? 1553 ASP B CG    1 
ATOM   6306 O  OD1   . ASP B 1 336 ? -53.704 -9.692  18.505  1.00 128.03 ? 1553 ASP B OD1   1 
ATOM   6307 O  OD2   . ASP B 1 336 ? -54.697 -8.130  17.342  1.00 128.40 ? 1553 ASP B OD2   1 
ATOM   6308 N  N     . ASN B 1 337 ? -52.063 -5.223  21.036  1.00 112.18 ? 1554 ASN B N     1 
ATOM   6309 C  CA    . ASN B 1 337 ? -51.915 -4.484  22.284  1.00 110.39 ? 1554 ASN B CA    1 
ATOM   6310 C  C     . ASN B 1 337 ? -51.370 -3.075  22.072  1.00 107.52 ? 1554 ASN B C     1 
ATOM   6311 O  O     . ASN B 1 337 ? -50.623 -2.573  22.917  1.00 105.11 ? 1554 ASN B O     1 
ATOM   6312 C  CB    . ASN B 1 337 ? -51.021 -5.254  23.258  1.00 118.12 ? 1554 ASN B CB    1 
ATOM   6313 C  CG    . ASN B 1 337 ? -51.542 -6.662  23.560  1.00 122.27 ? 1554 ASN B CG    1 
ATOM   6314 O  OD1   . ASN B 1 337 ? -52.536 -7.115  22.978  1.00 117.45 ? 1554 ASN B OD1   1 
ATOM   6315 N  ND2   . ASN B 1 337 ? -50.858 -7.365  24.467  1.00 123.43 ? 1554 ASN B ND2   1 
ATOM   6316 N  N     . TYR B 1 338 ? -51.697 -2.443  20.943  1.00 111.24 ? 1555 TYR B N     1 
ATOM   6317 C  CA    . TYR B 1 338 ? -51.275 -1.081  20.642  1.00 105.98 ? 1555 TYR B CA    1 
ATOM   6318 C  C     . TYR B 1 338 ? -52.383 -0.334  19.918  1.00 104.06 ? 1555 TYR B C     1 
ATOM   6319 O  O     . TYR B 1 338 ? -53.013 -0.882  19.009  1.00 105.70 ? 1555 TYR B O     1 
ATOM   6320 C  CB    . TYR B 1 338 ? -50.017 -1.057  19.777  1.00 103.91 ? 1555 TYR B CB    1 
ATOM   6321 C  CG    . TYR B 1 338 ? -48.803 -1.601  20.470  1.00 99.98  ? 1555 TYR B CG    1 
ATOM   6322 C  CD1   . TYR B 1 338 ? -48.122 -2.692  19.943  1.00 98.20  ? 1555 TYR B CD1   1 
ATOM   6323 C  CD2   . TYR B 1 338 ? -48.334 -1.034  21.651  1.00 93.48  ? 1555 TYR B CD2   1 
ATOM   6324 C  CE1   . TYR B 1 338 ? -47.013 -3.207  20.566  1.00 95.30  ? 1555 TYR B CE1   1 
ATOM   6325 C  CE2   . TYR B 1 338 ? -47.219 -1.541  22.286  1.00 94.58  ? 1555 TYR B CE2   1 
ATOM   6326 C  CZ    . TYR B 1 338 ? -46.559 -2.635  21.735  1.00 96.58  ? 1555 TYR B CZ    1 
ATOM   6327 O  OH    . TYR B 1 338 ? -45.441 -3.176  22.339  1.00 93.74  ? 1555 TYR B OH    1 
ATOM   6328 N  N     . SER B 1 339 ? -52.603 0.920   20.304  1.00 104.39 ? 1556 SER B N     1 
ATOM   6329 C  CA    . SER B 1 339 ? -53.562 1.741   19.588  1.00 107.41 ? 1556 SER B CA    1 
ATOM   6330 C  C     . SER B 1 339 ? -53.080 1.978   18.152  1.00 121.93 ? 1556 SER B C     1 
ATOM   6331 O  O     . SER B 1 339 ? -51.873 1.999   17.891  1.00 126.75 ? 1556 SER B O     1 
ATOM   6332 C  CB    . SER B 1 339 ? -53.760 3.072   20.314  1.00 103.25 ? 1556 SER B CB    1 
ATOM   6333 O  OG    . SER B 1 339 ? -54.048 4.123   19.418  1.00 108.56 ? 1556 SER B OG    1 
ATOM   6334 N  N     . PRO B 1 340 ? -54.003 2.073   17.191  1.00 128.13 ? 1557 PRO B N     1 
ATOM   6335 C  CA    . PRO B 1 340 ? -53.602 2.461   15.829  1.00 127.12 ? 1557 PRO B CA    1 
ATOM   6336 C  C     . PRO B 1 340 ? -52.748 3.719   15.765  1.00 123.22 ? 1557 PRO B C     1 
ATOM   6337 O  O     . PRO B 1 340 ? -51.737 3.740   15.048  1.00 127.52 ? 1557 PRO B O     1 
ATOM   6338 C  CB    . PRO B 1 340 ? -54.953 2.639   15.116  1.00 129.88 ? 1557 PRO B CB    1 
ATOM   6339 C  CG    . PRO B 1 340 ? -55.849 1.676   15.819  1.00 136.05 ? 1557 PRO B CG    1 
ATOM   6340 C  CD    . PRO B 1 340 ? -55.392 1.594   17.249  1.00 135.32 ? 1557 PRO B CD    1 
ATOM   6341 N  N     . GLY B 1 341 ? -53.133 4.772   16.488  1.00 117.68 ? 1558 GLY B N     1 
ATOM   6342 C  CA    . GLY B 1 341 ? -52.351 5.999   16.470  1.00 110.21 ? 1558 GLY B CA    1 
ATOM   6343 C  C     . GLY B 1 341 ? -50.959 5.802   17.039  1.00 110.42 ? 1558 GLY B C     1 
ATOM   6344 O  O     . GLY B 1 341 ? -49.982 6.405   16.567  1.00 115.64 ? 1558 GLY B O     1 
ATOM   6345 N  N     . TRP B 1 342 ? -50.857 4.989   18.092  1.00 99.06  ? 1559 TRP B N     1 
ATOM   6346 C  CA    . TRP B 1 342 ? -49.552 4.573   18.593  1.00 93.54  ? 1559 TRP B CA    1 
ATOM   6347 C  C     . TRP B 1 342 ? -48.683 4.002   17.472  1.00 85.35  ? 1559 TRP B C     1 
ATOM   6348 O  O     . TRP B 1 342 ? -47.493 4.320   17.369  1.00 85.59  ? 1559 TRP B O     1 
ATOM   6349 C  CB    . TRP B 1 342 ? -49.752 3.557   19.715  1.00 100.14 ? 1559 TRP B CB    1 
ATOM   6350 C  CG    . TRP B 1 342 ? -48.504 3.188   20.422  1.00 104.95 ? 1559 TRP B CG    1 
ATOM   6351 C  CD1   . TRP B 1 342 ? -48.113 3.617   21.650  1.00 107.59 ? 1559 TRP B CD1   1 
ATOM   6352 C  CD2   . TRP B 1 342 ? -47.470 2.303   19.953  1.00 108.49 ? 1559 TRP B CD2   1 
ATOM   6353 N  NE1   . TRP B 1 342 ? -46.894 3.064   21.977  1.00 110.55 ? 1559 TRP B NE1   1 
ATOM   6354 C  CE2   . TRP B 1 342 ? -46.479 2.254   20.954  1.00 107.67 ? 1559 TRP B CE2   1 
ATOM   6355 C  CE3   . TRP B 1 342 ? -47.289 1.543   18.790  1.00 111.33 ? 1559 TRP B CE3   1 
ATOM   6356 C  CZ2   . TRP B 1 342 ? -45.321 1.478   20.827  1.00 104.63 ? 1559 TRP B CZ2   1 
ATOM   6357 C  CZ3   . TRP B 1 342 ? -46.128 0.772   18.664  1.00 107.18 ? 1559 TRP B CZ3   1 
ATOM   6358 C  CH2   . TRP B 1 342 ? -45.165 0.748   19.678  1.00 99.88  ? 1559 TRP B CH2   1 
ATOM   6359 N  N     . LYS B 1 343 ? -49.265 3.167   16.609  1.00 82.11  ? 1560 LYS B N     1 
ATOM   6360 C  CA    . LYS B 1 343 ? -48.495 2.599   15.507  1.00 90.18  ? 1560 LYS B CA    1 
ATOM   6361 C  C     . LYS B 1 343 ? -48.123 3.666   14.476  1.00 88.97  ? 1560 LYS B C     1 
ATOM   6362 O  O     . LYS B 1 343 ? -46.994 3.669   13.954  1.00 84.37  ? 1560 LYS B O     1 
ATOM   6363 C  CB    . LYS B 1 343 ? -49.276 1.455   14.858  1.00 93.03  ? 1560 LYS B CB    1 
ATOM   6364 C  CG    . LYS B 1 343 ? -49.470 0.242   15.759  1.00 94.88  ? 1560 LYS B CG    1 
ATOM   6365 C  CD    . LYS B 1 343 ? -50.228 -0.881  15.049  1.00 93.20  ? 1560 LYS B CD    1 
ATOM   6366 C  CE    . LYS B 1 343 ? -50.568 -2.007  16.014  1.00 88.58  ? 1560 LYS B CE    1 
ATOM   6367 N  NZ    . LYS B 1 343 ? -51.891 -2.595  15.731  1.00 94.48  ? 1560 LYS B NZ    1 
ATOM   6368 N  N     . TYR B 1 344 ? -49.061 4.568   14.156  1.00 83.99  ? 1561 TYR B N     1 
ATOM   6369 C  CA    . TYR B 1 344 ? -48.744 5.668   13.252  1.00 90.13  ? 1561 TYR B CA    1 
ATOM   6370 C  C     . TYR B 1 344 ? -47.501 6.415   13.730  1.00 93.83  ? 1561 TYR B C     1 
ATOM   6371 O  O     . TYR B 1 344 ? -46.530 6.600   12.977  1.00 89.80  ? 1561 TYR B O     1 
ATOM   6372 C  CB    . TYR B 1 344 ? -49.911 6.654   13.146  1.00 94.58  ? 1561 TYR B CB    1 
ATOM   6373 C  CG    . TYR B 1 344 ? -51.202 6.166   12.507  1.00 100.70 ? 1561 TYR B CG    1 
ATOM   6374 C  CD1   . TYR B 1 344 ? -51.359 4.854   12.065  1.00 96.30  ? 1561 TYR B CD1   1 
ATOM   6375 C  CD2   . TYR B 1 344 ? -52.274 7.041   12.346  1.00 102.93 ? 1561 TYR B CD2   1 
ATOM   6376 C  CE1   . TYR B 1 344 ? -52.549 4.435   11.489  1.00 96.27  ? 1561 TYR B CE1   1 
ATOM   6377 C  CE2   . TYR B 1 344 ? -53.464 6.631   11.779  1.00 103.08 ? 1561 TYR B CE2   1 
ATOM   6378 C  CZ    . TYR B 1 344 ? -53.599 5.336   11.352  1.00 106.65 ? 1561 TYR B CZ    1 
ATOM   6379 O  OH    . TYR B 1 344 ? -54.798 4.959   10.788  1.00 114.31 ? 1561 TYR B OH    1 
ATOM   6380 N  N     . ASN B 1 345 ? -47.508 6.823   15.002  1.00 86.99  ? 1562 ASN B N     1 
ATOM   6381 C  CA    . ASN B 1 345 ? -46.392 7.599   15.538  1.00 78.22  ? 1562 ASN B CA    1 
ATOM   6382 C  C     . ASN B 1 345 ? -45.110 6.786   15.581  1.00 81.25  ? 1562 ASN B C     1 
ATOM   6383 O  O     . ASN B 1 345 ? -44.024 7.309   15.312  1.00 96.51  ? 1562 ASN B O     1 
ATOM   6384 C  CB    . ASN B 1 345 ? -46.735 8.104   16.937  1.00 90.02  ? 1562 ASN B CB    1 
ATOM   6385 C  CG    . ASN B 1 345 ? -45.589 8.866   17.592  1.00 95.89  ? 1562 ASN B CG    1 
ATOM   6386 O  OD1   . ASN B 1 345 ? -44.975 8.383   18.546  1.00 98.90  ? 1562 ASN B OD1   1 
ATOM   6387 N  ND2   . ASN B 1 345 ? -45.301 10.060  17.085  1.00 94.56  ? 1562 ASN B ND2   1 
ATOM   6388 N  N     . HIS B 1 346 ? -45.211 5.506   15.928  1.00 75.47  ? 1563 HIS B N     1 
ATOM   6389 C  CA    . HIS B 1 346 ? -44.037 4.647   15.992  1.00 74.38  ? 1563 HIS B CA    1 
ATOM   6390 C  C     . HIS B 1 346 ? -43.324 4.603   14.646  1.00 72.82  ? 1563 HIS B C     1 
ATOM   6391 O  O     . HIS B 1 346 ? -42.124 4.893   14.550  1.00 71.47  ? 1563 HIS B O     1 
ATOM   6392 C  CB    . HIS B 1 346 ? -44.511 3.267   16.433  1.00 83.16  ? 1563 HIS B CB    1 
ATOM   6393 C  CG    . HIS B 1 346 ? -43.441 2.232   16.560  1.00 76.93  ? 1563 HIS B CG    1 
ATOM   6394 N  ND1   . HIS B 1 346 ? -42.623 2.144   17.665  1.00 75.17  ? 1563 HIS B ND1   1 
ATOM   6395 C  CD2   . HIS B 1 346 ? -43.125 1.177   15.768  1.00 73.07  ? 1563 HIS B CD2   1 
ATOM   6396 C  CE1   . HIS B 1 346 ? -41.821 1.102   17.529  1.00 74.89  ? 1563 HIS B CE1   1 
ATOM   6397 N  NE2   . HIS B 1 346 ? -42.108 0.498   16.389  1.00 74.77  ? 1563 HIS B NE2   1 
ATOM   6398 N  N     . TRP B 1 347 ? -44.060 4.264   13.587  1.00 72.04  ? 1564 TRP B N     1 
ATOM   6399 C  CA    . TRP B 1 347 ? -43.433 4.145   12.278  1.00 72.01  ? 1564 TRP B CA    1 
ATOM   6400 C  C     . TRP B 1 347 ? -43.110 5.500   11.667  1.00 82.54  ? 1564 TRP B C     1 
ATOM   6401 O  O     . TRP B 1 347 ? -42.318 5.556   10.724  1.00 95.31  ? 1564 TRP B O     1 
ATOM   6402 C  CB    . TRP B 1 347 ? -44.309 3.305   11.356  1.00 76.93  ? 1564 TRP B CB    1 
ATOM   6403 C  CG    . TRP B 1 347 ? -44.556 1.941   11.945  1.00 77.34  ? 1564 TRP B CG    1 
ATOM   6404 C  CD1   . TRP B 1 347 ? -45.734 1.449   12.390  1.00 69.28  ? 1564 TRP B CD1   1 
ATOM   6405 C  CD2   . TRP B 1 347 ? -43.574 0.920   12.195  1.00 79.70  ? 1564 TRP B CD2   1 
ATOM   6406 N  NE1   . TRP B 1 347 ? -45.564 0.175   12.878  1.00 76.38  ? 1564 TRP B NE1   1 
ATOM   6407 C  CE2   . TRP B 1 347 ? -44.247 -0.171  12.777  1.00 76.85  ? 1564 TRP B CE2   1 
ATOM   6408 C  CE3   . TRP B 1 347 ? -42.198 0.820   11.970  1.00 67.97  ? 1564 TRP B CE3   1 
ATOM   6409 C  CZ2   . TRP B 1 347 ? -43.595 -1.346  13.145  1.00 81.13  ? 1564 TRP B CZ2   1 
ATOM   6410 C  CZ3   . TRP B 1 347 ? -41.550 -0.356  12.327  1.00 73.06  ? 1564 TRP B CZ3   1 
ATOM   6411 C  CH2   . TRP B 1 347 ? -42.246 -1.418  12.911  1.00 78.53  ? 1564 TRP B CH2   1 
ATOM   6412 N  N     . GLU B 1 348 ? -43.725 6.584   12.154  1.00 83.79  ? 1565 GLU B N     1 
ATOM   6413 C  CA    . GLU B 1 348 ? -43.245 7.922   11.809  1.00 77.81  ? 1565 GLU B CA    1 
ATOM   6414 C  C     . GLU B 1 348 ? -41.865 8.182   12.407  1.00 77.08  ? 1565 GLU B C     1 
ATOM   6415 O  O     . GLU B 1 348 ? -40.938 8.599   11.699  1.00 69.29  ? 1565 GLU B O     1 
ATOM   6416 C  CB    . GLU B 1 348 ? -44.224 8.978   12.298  1.00 72.93  ? 1565 GLU B CB    1 
ATOM   6417 C  CG    . GLU B 1 348 ? -45.324 9.327   11.319  1.00 92.43  ? 1565 GLU B CG    1 
ATOM   6418 C  CD    . GLU B 1 348 ? -46.184 10.476  11.823  1.00 101.39 ? 1565 GLU B CD    1 
ATOM   6419 O  OE1   . GLU B 1 348 ? -45.655 11.289  12.611  1.00 93.29  ? 1565 GLU B OE1   1 
ATOM   6420 O  OE2   . GLU B 1 348 ? -47.378 10.554  11.448  1.00 111.71 ? 1565 GLU B OE2   1 
ATOM   6421 N  N     . LEU B 1 349 ? -41.721 7.951   13.720  1.00 71.51  ? 1566 LEU B N     1 
ATOM   6422 C  CA    . LEU B 1 349 ? -40.430 8.073   14.403  1.00 69.05  ? 1566 LEU B CA    1 
ATOM   6423 C  C     . LEU B 1 349 ? -39.331 7.225   13.760  1.00 64.86  ? 1566 LEU B C     1 
ATOM   6424 O  O     . LEU B 1 349 ? -38.185 7.671   13.637  1.00 67.17  ? 1566 LEU B O     1 
ATOM   6425 C  CB    . LEU B 1 349 ? -40.578 7.672   15.866  1.00 71.80  ? 1566 LEU B CB    1 
ATOM   6426 C  CG    . LEU B 1 349 ? -41.242 8.640   16.833  1.00 80.94  ? 1566 LEU B CG    1 
ATOM   6427 C  CD1   . LEU B 1 349 ? -41.522 7.905   18.129  1.00 83.73  ? 1566 LEU B CD1   1 
ATOM   6428 C  CD2   . LEU B 1 349 ? -40.378 9.871   17.076  1.00 73.24  ? 1566 LEU B CD2   1 
ATOM   6429 N  N     . LYS B 1 350 ? -39.647 5.976   13.395  1.00 71.81  ? 1567 LYS B N     1 
ATOM   6430 C  CA    . LYS B 1 350 ? -38.658 5.077   12.807  1.00 68.31  ? 1567 LYS B CA    1 
ATOM   6431 C  C     . LYS B 1 350 ? -38.370 5.388   11.342  1.00 65.34  ? 1567 LYS B C     1 
ATOM   6432 O  O     . LYS B 1 350 ? -37.410 4.849   10.782  1.00 67.73  ? 1567 LYS B O     1 
ATOM   6433 C  CB    . LYS B 1 350 ? -39.125 3.618   12.942  1.00 75.02  ? 1567 LYS B CB    1 
ATOM   6434 C  CG    . LYS B 1 350 ? -38.912 3.007   14.325  1.00 71.94  ? 1567 LYS B CG    1 
ATOM   6435 C  CD    . LYS B 1 350 ? -39.349 1.585   14.345  1.00 69.15  ? 1567 LYS B CD    1 
ATOM   6436 C  CE    . LYS B 1 350 ? -38.230 0.663   14.770  1.00 73.13  ? 1567 LYS B CE    1 
ATOM   6437 N  NZ    . LYS B 1 350 ? -38.550 -0.797  14.598  1.00 55.23  ? 1567 LYS B NZ    1 
ATOM   6438 N  N     . GLY B 1 351 ? -39.182 6.226   10.711  1.00 66.38  ? 1568 GLY B N     1 
ATOM   6439 C  CA    . GLY B 1 351 ? -38.878 6.740   9.392   1.00 71.86  ? 1568 GLY B CA    1 
ATOM   6440 C  C     . GLY B 1 351 ? -39.337 5.904   8.217   1.00 75.29  ? 1568 GLY B C     1 
ATOM   6441 O  O     . GLY B 1 351 ? -38.758 6.027   7.128   1.00 76.22  ? 1568 GLY B O     1 
ATOM   6442 N  N     . VAL B 1 352 ? -40.382 5.093   8.379   1.00 70.20  ? 1569 VAL B N     1 
ATOM   6443 C  CA    . VAL B 1 352 ? -40.815 4.208   7.302   1.00 68.97  ? 1569 VAL B CA    1 
ATOM   6444 C  C     . VAL B 1 352 ? -41.391 5.074   6.192   1.00 78.63  ? 1569 VAL B C     1 
ATOM   6445 O  O     . VAL B 1 352 ? -42.331 5.850   6.423   1.00 82.63  ? 1569 VAL B O     1 
ATOM   6446 C  CB    . VAL B 1 352 ? -41.841 3.170   7.797   1.00 69.47  ? 1569 VAL B CB    1 
ATOM   6447 C  CG1   . VAL B 1 352 ? -42.255 2.220   6.652   1.00 60.20  ? 1569 VAL B CG1   1 
ATOM   6448 C  CG2   . VAL B 1 352 ? -41.278 2.376   8.978   1.00 71.02  ? 1569 VAL B CG2   1 
ATOM   6449 N  N     . PRO B 1 353 ? -40.839 4.968   4.981   1.00 79.17  ? 1570 PRO B N     1 
ATOM   6450 C  CA    . PRO B 1 353 ? -41.247 5.864   3.877   1.00 69.87  ? 1570 PRO B CA    1 
ATOM   6451 C  C     . PRO B 1 353 ? -42.748 5.964   3.631   1.00 68.87  ? 1570 PRO B C     1 
ATOM   6452 O  O     . PRO B 1 353 ? -43.221 7.048   3.268   1.00 79.92  ? 1570 PRO B O     1 
ATOM   6453 C  CB    . PRO B 1 353 ? -40.501 5.278   2.672   1.00 76.36  ? 1570 PRO B CB    1 
ATOM   6454 C  CG    . PRO B 1 353 ? -39.261 4.635   3.259   1.00 69.57  ? 1570 PRO B CG    1 
ATOM   6455 C  CD    . PRO B 1 353 ? -39.649 4.158   4.647   1.00 67.56  ? 1570 PRO B CD    1 
ATOM   6456 N  N     . VAL B 1 354 ? -43.507 4.883   3.788   1.00 76.21  ? 1571 VAL B N     1 
ATOM   6457 C  CA    . VAL B 1 354 ? -44.938 4.884   3.507   1.00 76.85  ? 1571 VAL B CA    1 
ATOM   6458 C  C     . VAL B 1 354 ? -45.671 4.168   4.626   1.00 80.02  ? 1571 VAL B C     1 
ATOM   6459 O  O     . VAL B 1 354 ? -45.286 3.059   5.024   1.00 72.73  ? 1571 VAL B O     1 
ATOM   6460 C  CB    . VAL B 1 354 ? -45.259 4.209   2.159   1.00 73.73  ? 1571 VAL B CB    1 
ATOM   6461 C  CG1   . VAL B 1 354 ? -46.735 3.831   2.078   1.00 77.66  ? 1571 VAL B CG1   1 
ATOM   6462 C  CG2   . VAL B 1 354 ? -44.869 5.108   1.001   1.00 61.06  ? 1571 VAL B CG2   1 
ATOM   6463 N  N     . ARG B 1 355 ? -46.760 4.775   5.087   1.00 89.35  ? 1572 ARG B N     1 
ATOM   6464 C  CA    . ARG B 1 355 ? -47.698 4.113   5.977   1.00 89.36  ? 1572 ARG B CA    1 
ATOM   6465 C  C     . ARG B 1 355 ? -48.943 3.780   5.187   1.00 85.57  ? 1572 ARG B C     1 
ATOM   6466 O  O     . ARG B 1 355 ? -49.431 4.616   4.428   1.00 87.34  ? 1572 ARG B O     1 
ATOM   6467 C  CB    . ARG B 1 355 ? -48.072 5.006   7.147   1.00 101.32 ? 1572 ARG B CB    1 
ATOM   6468 C  CG    . ARG B 1 355 ? -46.957 5.313   8.109   1.00 110.01 ? 1572 ARG B CG    1 
ATOM   6469 C  CD    . ARG B 1 355 ? -47.540 5.434   9.502   1.00 115.35 ? 1572 ARG B CD    1 
ATOM   6470 N  NE    . ARG B 1 355 ? -48.315 6.664   9.698   1.00 115.32 ? 1572 ARG B NE    1 
ATOM   6471 C  CZ    . ARG B 1 355 ? -49.618 6.809   9.456   1.00 113.51 ? 1572 ARG B CZ    1 
ATOM   6472 N  NH1   . ARG B 1 355 ? -50.347 5.806   8.989   1.00 114.16 ? 1572 ARG B NH1   1 
ATOM   6473 N  NH2   . ARG B 1 355 ? -50.201 7.974   9.688   1.00 114.50 ? 1572 ARG B NH2   1 
ATOM   6474 N  N     . ILE B 1 356 ? -49.446 2.560   5.343   1.00 90.17  ? 1573 ILE B N     1 
ATOM   6475 C  CA    . ILE B 1 356 ? -50.723 2.174   4.750   1.00 83.88  ? 1573 ILE B CA    1 
ATOM   6476 C  C     . ILE B 1 356 ? -51.734 2.079   5.872   1.00 80.88  ? 1573 ILE B C     1 
ATOM   6477 O  O     . ILE B 1 356 ? -51.599 1.234   6.771   1.00 74.57  ? 1573 ILE B O     1 
ATOM   6478 C  CB    . ILE B 1 356 ? -50.663 0.853   3.986   1.00 81.29  ? 1573 ILE B CB    1 
ATOM   6479 C  CG1   . ILE B 1 356 ? -49.514 0.843   2.989   1.00 75.19  ? 1573 ILE B CG1   1 
ATOM   6480 C  CG2   . ILE B 1 356 ? -51.983 0.677   3.265   1.00 77.01  ? 1573 ILE B CG2   1 
ATOM   6481 C  CD1   . ILE B 1 356 ? -49.886 1.265   1.615   1.00 83.10  ? 1573 ILE B CD1   1 
ATOM   6482 N  N     . GLU B 1 357 ? -52.724 2.967   5.816   1.00 89.27  ? 1574 GLU B N     1 
ATOM   6483 C  CA    . GLU B 1 357 ? -53.929 2.891   6.629   1.00 84.79  ? 1574 GLU B CA    1 
ATOM   6484 C  C     . GLU B 1 357 ? -54.966 2.090   5.844   1.00 91.11  ? 1574 GLU B C     1 
ATOM   6485 O  O     . GLU B 1 357 ? -55.393 2.495   4.743   1.00 96.52  ? 1574 GLU B O     1 
ATOM   6486 C  CB    . GLU B 1 357 ? -54.416 4.298   6.991   1.00 81.37  ? 1574 GLU B CB    1 
ATOM   6487 C  CG    . GLU B 1 357 ? -53.372 5.096   7.800   1.00 91.20  ? 1574 GLU B CG    1 
ATOM   6488 C  CD    . GLU B 1 357 ? -53.759 6.550   8.130   1.00 104.23 ? 1574 GLU B CD    1 
ATOM   6489 O  OE1   . GLU B 1 357 ? -54.929 6.976   7.934   1.00 106.80 ? 1574 GLU B OE1   1 
ATOM   6490 O  OE2   . GLU B 1 357 ? -52.855 7.271   8.604   1.00 107.15 ? 1574 GLU B OE2   1 
ATOM   6491 N  N     . LEU B 1 358 ? -55.336 0.939   6.401   1.00 95.71  ? 1575 LEU B N     1 
ATOM   6492 C  CA    . LEU B 1 358 ? -56.277 0.004   5.792   1.00 100.46 ? 1575 LEU B CA    1 
ATOM   6493 C  C     . LEU B 1 358 ? -57.342 -0.349  6.822   1.00 101.29 ? 1575 LEU B C     1 
ATOM   6494 O  O     . LEU B 1 358 ? -57.049 -1.024  7.814   1.00 108.09 ? 1575 LEU B O     1 
ATOM   6495 C  CB    . LEU B 1 358 ? -55.542 -1.248  5.301   1.00 99.07  ? 1575 LEU B CB    1 
ATOM   6496 C  CG    . LEU B 1 358 ? -56.311 -2.263  4.461   1.00 109.39 ? 1575 LEU B CG    1 
ATOM   6497 C  CD1   . LEU B 1 358 ? -56.640 -1.684  3.113   1.00 114.80 ? 1575 LEU B CD1   1 
ATOM   6498 C  CD2   . LEU B 1 358 ? -55.490 -3.531  4.285   1.00 107.76 ? 1575 LEU B CD2   1 
ATOM   6499 N  N     . GLY B 1 359 ? -58.564 0.139   6.603   1.00 103.78 ? 1576 GLY B N     1 
ATOM   6500 C  CA    . GLY B 1 359 ? -59.692 -0.157  7.450   1.00 109.76 ? 1576 GLY B CA    1 
ATOM   6501 C  C     . GLY B 1 359 ? -60.756 -0.982  6.746   1.00 118.89 ? 1576 GLY B C     1 
ATOM   6502 O  O     . GLY B 1 359 ? -60.556 -1.538  5.665   1.00 117.91 ? 1576 GLY B O     1 
ATOM   6503 N  N     . PHE B 1 360 ? -61.923 -1.047  7.386   1.00 127.37 ? 1577 PHE B N     1 
ATOM   6504 C  CA    . PHE B 1 360 ? -62.997 -1.879  6.853   1.00 122.70 ? 1577 PHE B CA    1 
ATOM   6505 C  C     . PHE B 1 360 ? -63.610 -1.258  5.609   1.00 118.80 ? 1577 PHE B C     1 
ATOM   6506 O  O     . PHE B 1 360 ? -63.804 -1.943  4.599   1.00 122.96 ? 1577 PHE B O     1 
ATOM   6507 C  CB    . PHE B 1 360 ? -64.040 -2.137  7.933   1.00 117.74 ? 1577 PHE B CB    1 
ATOM   6508 C  CG    . PHE B 1 360 ? -63.556 -3.070  9.000   1.00 122.09 ? 1577 PHE B CG    1 
ATOM   6509 C  CD1   . PHE B 1 360 ? -63.048 -4.320  8.661   1.00 129.28 ? 1577 PHE B CD1   1 
ATOM   6510 C  CD2   . PHE B 1 360 ? -63.573 -2.699  10.332  1.00 129.94 ? 1577 PHE B CD2   1 
ATOM   6511 C  CE1   . PHE B 1 360 ? -62.575 -5.197  9.633   1.00 127.73 ? 1577 PHE B CE1   1 
ATOM   6512 C  CE2   . PHE B 1 360 ? -63.107 -3.565  11.311  1.00 135.22 ? 1577 PHE B CE2   1 
ATOM   6513 C  CZ    . PHE B 1 360 ? -62.604 -4.822  10.957  1.00 131.01 ? 1577 PHE B CZ    1 
ATOM   6514 N  N     . LYS B 1 361 ? -63.903 0.043   5.651   1.00 112.42 ? 1578 LYS B N     1 
ATOM   6515 C  CA    . LYS B 1 361 ? -64.365 0.714   4.440   1.00 114.52 ? 1578 LYS B CA    1 
ATOM   6516 C  C     . LYS B 1 361 ? -63.314 0.618   3.339   1.00 114.42 ? 1578 LYS B C     1 
ATOM   6517 O  O     . LYS B 1 361 ? -63.653 0.607   2.148   1.00 128.44 ? 1578 LYS B O     1 
ATOM   6518 C  CB    . LYS B 1 361 ? -64.724 2.176   4.738   1.00 104.82 ? 1578 LYS B CB    1 
ATOM   6519 N  N     . ASP B 1 362 ? -62.039 0.532   3.715   1.00 98.35  ? 1579 ASP B N     1 
ATOM   6520 C  CA    . ASP B 1 362 ? -61.007 0.400   2.699   1.00 103.71 ? 1579 ASP B CA    1 
ATOM   6521 C  C     . ASP B 1 362 ? -61.068 -0.987  2.061   1.00 113.54 ? 1579 ASP B C     1 
ATOM   6522 O  O     . ASP B 1 362 ? -61.061 -1.112  0.829   1.00 117.15 ? 1579 ASP B O     1 
ATOM   6523 C  CB    . ASP B 1 362 ? -59.620 0.688   3.303   1.00 97.82  ? 1579 ASP B CB    1 
ATOM   6524 C  CG    . ASP B 1 362 ? -59.463 2.140   3.813   1.00 107.62 ? 1579 ASP B CG    1 
ATOM   6525 O  OD1   . ASP B 1 362 ? -60.114 3.068   3.265   1.00 117.16 ? 1579 ASP B OD1   1 
ATOM   6526 O  OD2   . ASP B 1 362 ? -58.667 2.360   4.760   1.00 105.01 ? 1579 ASP B OD2   1 
ATOM   6527 N  N     . LEU B 1 363 ? -61.201 -2.037  2.880   1.00 112.38 ? 1580 LEU B N     1 
ATOM   6528 C  CA    . LEU B 1 363 ? -61.244 -3.394  2.340   1.00 106.12 ? 1580 LEU B CA    1 
ATOM   6529 C  C     . LEU B 1 363 ? -62.521 -3.647  1.551   1.00 103.82 ? 1580 LEU B C     1 
ATOM   6530 O  O     . LEU B 1 363 ? -62.532 -4.486  0.643   1.00 105.98 ? 1580 LEU B O     1 
ATOM   6531 C  CB    . LEU B 1 363 ? -61.115 -4.417  3.474   1.00 101.87 ? 1580 LEU B CB    1 
ATOM   6532 N  N     . GLN B 1 364 ? -63.599 -2.938  1.882   1.00 102.15 ? 1581 GLN B N     1 
ATOM   6533 C  CA    . GLN B 1 364 ? -64.866 -3.086  1.170   1.00 108.77 ? 1581 GLN B CA    1 
ATOM   6534 C  C     . GLN B 1 364 ? -64.891 -2.341  -0.165  1.00 117.54 ? 1581 GLN B C     1 
ATOM   6535 O  O     . GLN B 1 364 ? -65.602 -2.767  -1.085  1.00 128.44 ? 1581 GLN B O     1 
ATOM   6536 C  CB    . GLN B 1 364 ? -66.003 -2.626  2.086   1.00 114.92 ? 1581 GLN B CB    1 
ATOM   6537 C  CG    . GLN B 1 364 ? -67.161 -1.898  1.423   1.00 124.23 ? 1581 GLN B CG    1 
ATOM   6538 C  CD    . GLN B 1 364 ? -68.237 -1.512  2.423   1.00 122.00 ? 1581 GLN B CD    1 
ATOM   6539 O  OE1   . GLN B 1 364 ? -68.329 -2.106  3.497   1.00 123.70 ? 1581 GLN B OE1   1 
ATOM   6540 N  NE2   . GLN B 1 364 ? -69.070 -0.535  2.068   1.00 114.16 ? 1581 GLN B NE2   1 
ATOM   6541 N  N     . ASN B 1 365 ? -64.105 -1.269  -0.307  1.00 117.22 ? 1582 ASN B N     1 
ATOM   6542 C  CA    . ASN B 1 365 ? -63.940 -0.559  -1.572  1.00 120.17 ? 1582 ASN B CA    1 
ATOM   6543 C  C     . ASN B 1 365 ? -62.683 -0.980  -2.328  1.00 118.14 ? 1582 ASN B C     1 
ATOM   6544 O  O     . ASN B 1 365 ? -62.336 -0.344  -3.328  1.00 119.44 ? 1582 ASN B O     1 
ATOM   6545 C  CB    . ASN B 1 365 ? -63.900 0.953   -1.336  1.00 127.98 ? 1582 ASN B CB    1 
ATOM   6546 C  CG    . ASN B 1 365 ? -65.258 1.535   -1.009  1.00 137.27 ? 1582 ASN B CG    1 
ATOM   6547 O  OD1   . ASN B 1 365 ? -65.895 1.124   -0.041  1.00 145.67 ? 1582 ASN B OD1   1 
ATOM   6548 N  ND2   . ASN B 1 365 ? -65.704 2.510   -1.806  1.00 135.61 ? 1582 ASN B ND2   1 
ATOM   6549 N  N     . ASP B 1 366 ? -62.003 -2.033  -1.876  1.00 121.32 ? 1583 ASP B N     1 
ATOM   6550 C  CA    . ASP B 1 366 ? -60.848 -2.601  -2.569  1.00 132.78 ? 1583 ASP B CA    1 
ATOM   6551 C  C     . ASP B 1 366 ? -59.770 -1.543  -2.823  1.00 141.32 ? 1583 ASP B C     1 
ATOM   6552 O  O     . ASP B 1 366 ? -59.370 -1.272  -3.959  1.00 146.39 ? 1583 ASP B O     1 
ATOM   6553 C  CB    . ASP B 1 366 ? -61.263 -3.285  -3.871  1.00 140.17 ? 1583 ASP B CB    1 
ATOM   6554 C  CG    . ASP B 1 366 ? -60.230 -4.271  -4.339  1.00 143.98 ? 1583 ASP B CG    1 
ATOM   6555 O  OD1   . ASP B 1 366 ? -60.155 -5.365  -3.746  1.00 146.18 ? 1583 ASP B OD1   1 
ATOM   6556 O  OD2   . ASP B 1 366 ? -59.474 -3.942  -5.277  1.00 147.38 ? 1583 ASP B OD2   1 
ATOM   6557 N  N     . GLN B 1 367 ? -59.253 -1.001  -1.743  1.00 136.18 ? 1584 GLN B N     1 
ATOM   6558 C  CA    . GLN B 1 367 ? -58.227 0.009   -1.805  1.00 125.51 ? 1584 GLN B CA    1 
ATOM   6559 C  C     . GLN B 1 367 ? -57.549 0.156   -0.449  1.00 121.62 ? 1584 GLN B C     1 
ATOM   6560 O  O     . GLN B 1 367 ? -57.759 -0.634  0.459   1.00 114.70 ? 1584 GLN B O     1 
ATOM   6561 C  CB    . GLN B 1 367 ? -58.890 1.322   -2.117  1.00 118.93 ? 1584 GLN B CB    1 
ATOM   6562 C  CG    . GLN B 1 367 ? -59.890 1.716   -1.051  1.00 114.49 ? 1584 GLN B CG    1 
ATOM   6563 C  CD    . GLN B 1 367 ? -60.463 3.064   -1.302  1.00 118.20 ? 1584 GLN B CD    1 
ATOM   6564 O  OE1   . GLN B 1 367 ? -60.576 3.470   -2.444  1.00 118.08 ? 1584 GLN B OE1   1 
ATOM   6565 N  NE2   . GLN B 1 367 ? -60.824 3.772   -0.247  1.00 119.45 ? 1584 GLN B NE2   1 
ATOM   6566 N  N     . PHE B 1 368 ? -56.744 1.198   -0.322  1.00 117.63 ? 1585 PHE B N     1 
ATOM   6567 C  CA    . PHE B 1 368 ? -56.038 1.509   0.916   1.00 109.01 ? 1585 PHE B CA    1 
ATOM   6568 C  C     . PHE B 1 368 ? -55.552 2.934   0.766   1.00 97.10  ? 1585 PHE B C     1 
ATOM   6569 O  O     . PHE B 1 368 ? -55.501 3.459   -0.348  1.00 89.53  ? 1585 PHE B O     1 
ATOM   6570 C  CB    . PHE B 1 368 ? -54.858 0.557   1.170   1.00 110.66 ? 1585 PHE B CB    1 
ATOM   6571 C  CG    . PHE B 1 368 ? -53.902 0.454   0.019   1.00 107.64 ? 1585 PHE B CG    1 
ATOM   6572 C  CD1   . PHE B 1 368 ? -54.123 -0.457  -1.002  1.00 108.74 ? 1585 PHE B CD1   1 
ATOM   6573 C  CD2   . PHE B 1 368 ? -52.787 1.274   -0.050  1.00 104.79 ? 1585 PHE B CD2   1 
ATOM   6574 C  CE1   . PHE B 1 368 ? -53.249 -0.552  -2.070  1.00 108.07 ? 1585 PHE B CE1   1 
ATOM   6575 C  CE2   . PHE B 1 368 ? -51.906 1.183   -1.109  1.00 102.47 ? 1585 PHE B CE2   1 
ATOM   6576 C  CZ    . PHE B 1 368 ? -52.138 0.266   -2.120  1.00 106.21 ? 1585 PHE B CZ    1 
ATOM   6577 N  N     . VAL B 1 369 ? -55.161 3.566   1.868   1.00 97.86  ? 1586 VAL B N     1 
ATOM   6578 C  CA    . VAL B 1 369 ? -54.558 4.887   1.748   1.00 99.58  ? 1586 VAL B CA    1 
ATOM   6579 C  C     . VAL B 1 369 ? -53.107 4.750   2.162   1.00 86.31  ? 1586 VAL B C     1 
ATOM   6580 O  O     . VAL B 1 369 ? -52.801 4.178   3.218   1.00 74.61  ? 1586 VAL B O     1 
ATOM   6581 C  CB    . VAL B 1 369 ? -55.301 5.974   2.553   1.00 106.15 ? 1586 VAL B CB    1 
ATOM   6582 C  CG1   . VAL B 1 369 ? -55.614 5.518   3.955   1.00 115.97 ? 1586 VAL B CG1   1 
ATOM   6583 C  CG2   . VAL B 1 369 ? -54.502 7.289   2.573   1.00 97.66  ? 1586 VAL B CG2   1 
ATOM   6584 N  N     . ALA B 1 370 ? -52.212 5.222   1.301   1.00 86.71  ? 1587 ALA B N     1 
ATOM   6585 C  CA    . ALA B 1 370 ? -50.791 5.263   1.600   1.00 87.52  ? 1587 ALA B CA    1 
ATOM   6586 C  C     . ALA B 1 370 ? -50.402 6.720   1.778   1.00 89.55  ? 1587 ALA B C     1 
ATOM   6587 O  O     . ALA B 1 370 ? -50.794 7.583   0.980   1.00 93.18  ? 1587 ALA B O     1 
ATOM   6588 C  CB    . ALA B 1 370 ? -49.967 4.594   0.499   1.00 84.50  ? 1587 ALA B CB    1 
ATOM   6589 N  N     . VAL B 1 371 ? -49.644 6.986   2.833   1.00 81.23  ? 1588 VAL B N     1 
ATOM   6590 C  CA    . VAL B 1 371 ? -49.311 8.340   3.235   1.00 75.20  ? 1588 VAL B CA    1 
ATOM   6591 C  C     . VAL B 1 371 ? -47.794 8.426   3.380   1.00 83.65  ? 1588 VAL B C     1 
ATOM   6592 O  O     . VAL B 1 371 ? -47.162 7.547   4.006   1.00 67.35  ? 1588 VAL B O     1 
ATOM   6593 C  CB    . VAL B 1 371 ? -50.075 8.728   4.527   1.00 73.48  ? 1588 VAL B CB    1 
ATOM   6594 C  CG1   . VAL B 1 371 ? -51.512 8.262   4.447   1.00 75.50  ? 1588 VAL B CG1   1 
ATOM   6595 C  CG2   . VAL B 1 371 ? -49.473 8.134   5.767   1.00 78.99  ? 1588 VAL B CG2   1 
ATOM   6596 N  N     . ARG B 1 372 ? -47.214 9.471   2.767   1.00 89.76  ? 1589 ARG B N     1 
ATOM   6597 C  CA    . ARG B 1 372 ? -45.765 9.587   2.632   1.00 72.56  ? 1589 ARG B CA    1 
ATOM   6598 C  C     . ARG B 1 372 ? -45.168 10.105  3.930   1.00 74.34  ? 1589 ARG B C     1 
ATOM   6599 O  O     . ARG B 1 372 ? -45.701 11.028  4.541   1.00 73.64  ? 1589 ARG B O     1 
ATOM   6600 C  CB    . ARG B 1 372 ? -45.417 10.538  1.495   1.00 76.94  ? 1589 ARG B CB    1 
ATOM   6601 C  CG    . ARG B 1 372 ? -45.616 10.018  0.085   1.00 77.86  ? 1589 ARG B CG    1 
ATOM   6602 C  CD    . ARG B 1 372 ? -45.429 11.156  -0.930  1.00 90.67  ? 1589 ARG B CD    1 
ATOM   6603 N  NE    . ARG B 1 372 ? -44.095 11.772  -0.858  1.00 93.10  ? 1589 ARG B NE    1 
ATOM   6604 C  CZ    . ARG B 1 372 ? -43.450 12.331  -1.885  1.00 90.40  ? 1589 ARG B CZ    1 
ATOM   6605 N  NH1   . ARG B 1 372 ? -43.997 12.364  -3.093  1.00 87.21  ? 1589 ARG B NH1   1 
ATOM   6606 N  NH2   . ARG B 1 372 ? -42.249 12.862  -1.705  1.00 86.36  ? 1589 ARG B NH2   1 
ATOM   6607 N  N     . ARG B 1 373 ? -44.067 9.491   4.368   1.00 82.16  ? 1590 ARG B N     1 
ATOM   6608 C  CA    . ARG B 1 373 ? -43.434 9.970   5.592   1.00 77.67  ? 1590 ARG B CA    1 
ATOM   6609 C  C     . ARG B 1 373 ? -42.821 11.354  5.412   1.00 75.00  ? 1590 ARG B C     1 
ATOM   6610 O  O     . ARG B 1 373 ? -42.716 12.107  6.382   1.00 70.85  ? 1590 ARG B O     1 
ATOM   6611 C  CB    . ARG B 1 373 ? -42.385 8.979   6.057   1.00 65.55  ? 1590 ARG B CB    1 
ATOM   6612 C  CG    . ARG B 1 373 ? -41.601 9.415   7.288   1.00 57.99  ? 1590 ARG B CG    1 
ATOM   6613 C  CD    . ARG B 1 373 ? -42.503 9.712   8.465   1.00 59.21  ? 1590 ARG B CD    1 
ATOM   6614 N  NE    . ARG B 1 373 ? -41.743 10.265  9.584   1.00 80.16  ? 1590 ARG B NE    1 
ATOM   6615 C  CZ    . ARG B 1 373 ? -41.311 11.527  9.667   1.00 78.84  ? 1590 ARG B CZ    1 
ATOM   6616 N  NH1   . ARG B 1 373 ? -41.567 12.404  8.693   1.00 73.01  ? 1590 ARG B NH1   1 
ATOM   6617 N  NH2   . ARG B 1 373 ? -40.620 11.912  10.735  1.00 76.54  ? 1590 ARG B NH2   1 
ATOM   6618 N  N     . ASP B 1 374 ? -42.368 11.688  4.203   1.00 78.05  ? 1591 ASP B N     1 
ATOM   6619 C  CA    . ASP B 1 374 ? -41.760 12.999  4.009   1.00 85.46  ? 1591 ASP B CA    1 
ATOM   6620 C  C     . ASP B 1 374 ? -42.828 14.085  3.866   1.00 89.59  ? 1591 ASP B C     1 
ATOM   6621 O  O     . ASP B 1 374 ? -42.757 15.124  4.530   1.00 91.53  ? 1591 ASP B O     1 
ATOM   6622 C  CB    . ASP B 1 374 ? -40.786 12.970  2.817   1.00 83.09  ? 1591 ASP B CB    1 
ATOM   6623 C  CG    . ASP B 1 374 ? -41.473 12.735  1.468   1.00 87.25  ? 1591 ASP B CG    1 
ATOM   6624 O  OD1   . ASP B 1 374 ? -42.681 12.400  1.425   1.00 85.60  ? 1591 ASP B OD1   1 
ATOM   6625 O  OD2   . ASP B 1 374 ? -40.774 12.887  0.439   1.00 83.56  ? 1591 ASP B OD2   1 
ATOM   6626 N  N     . ASN B 1 375 ? -43.863 13.823  3.079   1.00 89.04  ? 1592 ASN B N     1 
ATOM   6627 C  CA    . ASN B 1 375 ? -44.863 14.824  2.740   1.00 85.15  ? 1592 ASN B CA    1 
ATOM   6628 C  C     . ASN B 1 375 ? -45.954 14.927  3.778   1.00 90.85  ? 1592 ASN B C     1 
ATOM   6629 O  O     . ASN B 1 375 ? -46.475 16.017  4.023   1.00 102.25 ? 1592 ASN B O     1 
ATOM   6630 C  CB    . ASN B 1 375 ? -45.556 14.452  1.436   1.00 87.77  ? 1592 ASN B CB    1 
ATOM   6631 C  CG    . ASN B 1 375 ? -44.832 14.929  0.241   1.00 98.03  ? 1592 ASN B CG    1 
ATOM   6632 O  OD1   . ASN B 1 375 ? -43.881 15.691  0.349   1.00 102.72 ? 1592 ASN B OD1   1 
ATOM   6633 N  ND2   . ASN B 1 375 ? -45.276 14.491  -0.929  1.00 105.27 ? 1592 ASN B ND2   1 
ATOM   6634 N  N     . GLY B 1 376 ? -46.340 13.810  4.376   1.00 82.83  ? 1593 GLY B N     1 
ATOM   6635 C  CA    . GLY B 1 376 ? -47.653 13.757  4.960   1.00 82.42  ? 1593 GLY B CA    1 
ATOM   6636 C  C     . GLY B 1 376 ? -48.745 13.618  3.923   1.00 90.14  ? 1593 GLY B C     1 
ATOM   6637 O  O     . GLY B 1 376 ? -49.910 13.422  4.295   1.00 97.37  ? 1593 GLY B O     1 
ATOM   6638 N  N     . ALA B 1 377 ? -48.396 13.689  2.633   1.00 84.39  ? 1594 ALA B N     1 
ATOM   6639 C  CA    . ALA B 1 377 ? -49.364 13.546  1.553   1.00 79.45  ? 1594 ALA B CA    1 
ATOM   6640 C  C     . ALA B 1 377 ? -50.001 12.155  1.557   1.00 89.03  ? 1594 ALA B C     1 
ATOM   6641 O  O     . ALA B 1 377 ? -49.316 11.129  1.698   1.00 92.20  ? 1594 ALA B O     1 
ATOM   6642 C  CB    . ALA B 1 377 ? -48.711 13.824  0.203   1.00 70.81  ? 1594 ALA B CB    1 
ATOM   6643 N  N     . LYS B 1 378 ? -51.326 12.146  1.413   1.00 93.84  ? 1595 LYS B N     1 
ATOM   6644 C  CA    . LYS B 1 378 ? -52.185 10.976  1.431   1.00 87.94  ? 1595 LYS B CA    1 
ATOM   6645 C  C     . LYS B 1 378 ? -52.626 10.686  0.011   1.00 90.89  ? 1595 LYS B C     1 
ATOM   6646 O  O     . LYS B 1 378 ? -52.978 11.603  -0.736  1.00 98.14  ? 1595 LYS B O     1 
ATOM   6647 C  CB    . LYS B 1 378 ? -53.434 11.216  2.283   1.00 86.58  ? 1595 LYS B CB    1 
ATOM   6648 C  CG    . LYS B 1 378 ? -53.217 11.277  3.768   1.00 92.04  ? 1595 LYS B CG    1 
ATOM   6649 C  CD    . LYS B 1 378 ? -54.514 10.977  4.496   1.00 105.53 ? 1595 LYS B CD    1 
ATOM   6650 C  CE    . LYS B 1 378 ? -54.266 10.689  5.964   1.00 113.00 ? 1595 LYS B CE    1 
ATOM   6651 N  NZ    . LYS B 1 378 ? -53.680 11.875  6.635   1.00 115.40 ? 1595 LYS B NZ    1 
ATOM   6652 N  N     . GLN B 1 379 ? -52.587 9.418   -0.366  1.00 92.26  ? 1596 GLN B N     1 
ATOM   6653 C  CA    . GLN B 1 379 ? -52.985 9.008   -1.698  1.00 93.51  ? 1596 GLN B CA    1 
ATOM   6654 C  C     . GLN B 1 379 ? -53.656 7.652   -1.567  1.00 105.25 ? 1596 GLN B C     1 
ATOM   6655 O  O     . GLN B 1 379 ? -53.081 6.738   -0.968  1.00 111.92 ? 1596 GLN B O     1 
ATOM   6656 C  CB    . GLN B 1 379 ? -51.765 8.970   -2.614  1.00 92.26  ? 1596 GLN B CB    1 
ATOM   6657 C  CG    . GLN B 1 379 ? -51.929 8.195   -3.869  1.00 99.55  ? 1596 GLN B CG    1 
ATOM   6658 C  CD    . GLN B 1 379 ? -50.615 8.046   -4.563  1.00 99.25  ? 1596 GLN B CD    1 
ATOM   6659 O  OE1   . GLN B 1 379 ? -49.577 8.417   -4.018  1.00 82.01  ? 1596 GLN B OE1   1 
ATOM   6660 N  NE2   . GLN B 1 379 ? -50.640 7.506   -5.773  1.00 111.82 ? 1596 GLN B NE2   1 
ATOM   6661 N  N     . THR B 1 380 ? -54.879 7.533   -2.084  1.00 109.74 ? 1597 THR B N     1 
ATOM   6662 C  CA    . THR B 1 380 ? -55.643 6.290   -1.996  1.00 107.06 ? 1597 THR B CA    1 
ATOM   6663 C  C     . THR B 1 380 ? -55.411 5.448   -3.244  1.00 96.40  ? 1597 THR B C     1 
ATOM   6664 O  O     . THR B 1 380 ? -55.593 5.926   -4.365  1.00 95.31  ? 1597 THR B O     1 
ATOM   6665 C  CB    . THR B 1 380 ? -57.132 6.588   -1.818  1.00 119.56 ? 1597 THR B CB    1 
ATOM   6666 O  OG1   . THR B 1 380 ? -57.690 6.993   -3.072  1.00 127.40 ? 1597 THR B OG1   1 
ATOM   6667 C  CG2   . THR B 1 380 ? -57.325 7.713   -0.810  1.00 121.19 ? 1597 THR B CG2   1 
ATOM   6668 N  N     . ILE B 1 381 ? -54.992 4.205   -3.051  1.00 101.00 ? 1598 ILE B N     1 
ATOM   6669 C  CA    . ILE B 1 381 ? -54.645 3.314   -4.153  1.00 109.33 ? 1598 ILE B CA    1 
ATOM   6670 C  C     . ILE B 1 381 ? -55.615 2.145   -4.170  1.00 114.09 ? 1598 ILE B C     1 
ATOM   6671 O  O     . ILE B 1 381 ? -55.854 1.514   -3.132  1.00 115.33 ? 1598 ILE B O     1 
ATOM   6672 C  CB    . ILE B 1 381 ? -53.197 2.803   -4.049  1.00 100.56 ? 1598 ILE B CB    1 
ATOM   6673 C  CG1   . ILE B 1 381 ? -52.211 3.980   -3.953  1.00 109.05 ? 1598 ILE B CG1   1 
ATOM   6674 C  CG2   . ILE B 1 381 ? -52.892 1.883   -5.223  1.00 80.44  ? 1598 ILE B CG2   1 
ATOM   6675 C  CD1   . ILE B 1 381 ? -51.723 4.291   -2.542  1.00 110.03 ? 1598 ILE B CD1   1 
ATOM   6676 N  N     . LYS B 1 382 ? -56.178 1.873   -5.348  1.00 116.18 ? 1599 LYS B N     1 
ATOM   6677 C  CA    . LYS B 1 382 ? -56.953 0.659   -5.569  1.00 124.65 ? 1599 LYS B CA    1 
ATOM   6678 C  C     . LYS B 1 382 ? -56.024 -0.554  -5.574  1.00 119.63 ? 1599 LYS B C     1 
ATOM   6679 O  O     . LYS B 1 382 ? -54.960 -0.522  -6.197  1.00 110.25 ? 1599 LYS B O     1 
ATOM   6680 C  CB    . LYS B 1 382 ? -57.730 0.762   -6.888  1.00 133.22 ? 1599 LYS B CB    1 
ATOM   6681 C  CG    . LYS B 1 382 ? -56.951 1.371   -8.065  1.00 134.82 ? 1599 LYS B CG    1 
ATOM   6682 C  CD    . LYS B 1 382 ? -57.773 1.341   -9.353  1.00 135.60 ? 1599 LYS B CD    1 
ATOM   6683 C  CE    . LYS B 1 382 ? -58.322 -0.061  -9.616  1.00 134.37 ? 1599 LYS B CE    1 
ATOM   6684 N  NZ    . LYS B 1 382 ? -58.324 -0.434  -11.058 1.00 130.70 ? 1599 LYS B NZ    1 
ATOM   6685 N  N     . ARG B 1 383 ? -56.427 -1.624  -4.869  1.00 123.43 ? 1600 ARG B N     1 
ATOM   6686 C  CA    . ARG B 1 383 ? -55.563 -2.799  -4.714  1.00 114.91 ? 1600 ARG B CA    1 
ATOM   6687 C  C     . ARG B 1 383 ? -55.070 -3.304  -6.063  1.00 118.50 ? 1600 ARG B C     1 
ATOM   6688 O  O     . ARG B 1 383 ? -53.925 -3.758  -6.186  1.00 116.54 ? 1600 ARG B O     1 
ATOM   6689 C  CB    . ARG B 1 383 ? -56.306 -3.925  -3.986  1.00 106.67 ? 1600 ARG B CB    1 
ATOM   6690 C  CG    . ARG B 1 383 ? -56.768 -3.605  -2.571  1.00 103.32 ? 1600 ARG B CG    1 
ATOM   6691 C  CD    . ARG B 1 383 ? -55.676 -3.854  -1.558  1.00 102.96 ? 1600 ARG B CD    1 
ATOM   6692 N  NE    . ARG B 1 383 ? -55.323 -5.264  -1.451  1.00 103.13 ? 1600 ARG B NE    1 
ATOM   6693 C  CZ    . ARG B 1 383 ? -55.408 -5.985  -0.334  1.00 110.11 ? 1600 ARG B CZ    1 
ATOM   6694 N  NH1   . ARG B 1 383 ? -55.835 -5.432  0.794   1.00 103.57 ? 1600 ARG B NH1   1 
ATOM   6695 N  NH2   . ARG B 1 383 ? -55.057 -7.268  -0.344  1.00 118.66 ? 1600 ARG B NH2   1 
ATOM   6696 N  N     . ALA B 1 384 ? -55.916 -3.199  -7.093  1.00 122.06 ? 1601 ALA B N     1 
ATOM   6697 C  CA    . ALA B 1 384 ? -55.555 -3.653  -8.431  1.00 116.98 ? 1601 ALA B CA    1 
ATOM   6698 C  C     . ALA B 1 384 ? -54.251 -3.015  -8.897  1.00 116.82 ? 1601 ALA B C     1 
ATOM   6699 O  O     . ALA B 1 384 ? -53.329 -3.711  -9.336  1.00 127.02 ? 1601 ALA B O     1 
ATOM   6700 C  CB    . ALA B 1 384 ? -56.699 -3.336  -9.399  1.00 115.31 ? 1601 ALA B CB    1 
ATOM   6701 N  N     . GLN B 1 385 ? -54.154 -1.689  -8.804  1.00 109.67 ? 1602 GLN B N     1 
ATOM   6702 C  CA    . GLN B 1 385 ? -52.958 -0.959  -9.214  1.00 110.56 ? 1602 GLN B CA    1 
ATOM   6703 C  C     . GLN B 1 385 ? -51.821 -0.995  -8.181  1.00 104.43 ? 1602 GLN B C     1 
ATOM   6704 O  O     . GLN B 1 385 ? -50.765 -0.396  -8.434  1.00 104.33 ? 1602 GLN B O     1 
ATOM   6705 C  CB    . GLN B 1 385 ? -53.331 0.497   -9.526  1.00 114.62 ? 1602 GLN B CB    1 
ATOM   6706 N  N     . ALA B 1 386 ? -51.984 -1.693  -7.053  1.00 96.65  ? 1603 ALA B N     1 
ATOM   6707 C  CA    . ALA B 1 386 ? -51.014 -1.590  -5.968  1.00 90.90  ? 1603 ALA B CA    1 
ATOM   6708 C  C     . ALA B 1 386 ? -49.583 -1.862  -6.438  1.00 106.42 ? 1603 ALA B C     1 
ATOM   6709 O  O     . ALA B 1 386 ? -48.723 -0.966  -6.419  1.00 98.20  ? 1603 ALA B O     1 
ATOM   6710 C  CB    . ALA B 1 386 ? -51.407 -2.538  -4.837  1.00 79.95  ? 1603 ALA B CB    1 
ATOM   6711 N  N     . THR B 1 387 ? -49.319 -3.084  -6.916  1.00 114.55 ? 1604 THR B N     1 
ATOM   6712 C  CA    . THR B 1 387 ? -47.954 -3.451  -7.299  1.00 109.76 ? 1604 THR B CA    1 
ATOM   6713 C  C     . THR B 1 387 ? -47.340 -2.470  -8.284  1.00 104.25 ? 1604 THR B C     1 
ATOM   6714 O  O     . THR B 1 387 ? -46.119 -2.456  -8.439  1.00 117.33 ? 1604 THR B O     1 
ATOM   6715 C  CB    . THR B 1 387 ? -47.865 -4.861  -7.908  1.00 111.96 ? 1604 THR B CB    1 
ATOM   6716 O  OG1   . THR B 1 387 ? -48.125 -4.796  -9.315  1.00 117.23 ? 1604 THR B OG1   1 
ATOM   6717 C  CG2   . THR B 1 387 ? -48.833 -5.824  -7.249  1.00 116.46 ? 1604 THR B CG2   1 
ATOM   6718 N  N     . VAL B 1 388 ? -48.144 -1.675  -8.979  1.00 100.77 ? 1605 VAL B N     1 
ATOM   6719 C  CA    . VAL B 1 388 ? -47.621 -0.799  -10.012 1.00 99.66  ? 1605 VAL B CA    1 
ATOM   6720 C  C     . VAL B 1 388 ? -47.445 0.628   -9.506  1.00 114.96 ? 1605 VAL B C     1 
ATOM   6721 O  O     . VAL B 1 388 ? -46.476 1.301   -9.862  1.00 120.62 ? 1605 VAL B O     1 
ATOM   6722 C  CB    . VAL B 1 388 ? -48.566 -0.845  -11.231 1.00 88.11  ? 1605 VAL B CB    1 
ATOM   6723 C  CG1   . VAL B 1 388 ? -48.156 0.183   -12.281 1.00 88.90  ? 1605 VAL B CG1   1 
ATOM   6724 C  CG2   . VAL B 1 388 ? -48.607 -2.237  -11.802 1.00 82.07  ? 1605 VAL B CG2   1 
ATOM   6725 N  N     . GLU B 1 389 ? -48.326 1.098   -8.619  1.00 116.99 ? 1606 GLU B N     1 
ATOM   6726 C  CA    . GLU B 1 389 ? -48.142 2.472   -8.181  1.00 108.37 ? 1606 GLU B CA    1 
ATOM   6727 C  C     . GLU B 1 389 ? -47.128 2.558   -7.056  1.00 101.47 ? 1606 GLU B C     1 
ATOM   6728 O  O     . GLU B 1 389 ? -46.395 3.543   -6.961  1.00 113.80 ? 1606 GLU B O     1 
ATOM   6729 C  CB    . GLU B 1 389 ? -49.470 3.100   -7.775  1.00 108.25 ? 1606 GLU B CB    1 
ATOM   6730 C  CG    . GLU B 1 389 ? -49.314 4.587   -7.584  1.00 126.15 ? 1606 GLU B CG    1 
ATOM   6731 C  CD    . GLU B 1 389 ? -50.341 5.382   -8.336  1.00 152.55 ? 1606 GLU B CD    1 
ATOM   6732 O  OE1   . GLU B 1 389 ? -50.541 5.091   -9.532  1.00 157.73 ? 1606 GLU B OE1   1 
ATOM   6733 O  OE2   . GLU B 1 389 ? -50.941 6.302   -7.740  1.00 159.05 ? 1606 GLU B OE2   1 
ATOM   6734 N  N     . MET B 1 390 ? -47.062 1.535   -6.221  1.00 82.37  ? 1607 MET B N     1 
ATOM   6735 C  CA    . MET B 1 390 ? -46.198 1.597   -5.056  1.00 71.67  ? 1607 MET B CA    1 
ATOM   6736 C  C     . MET B 1 390 ? -44.722 1.721   -5.414  1.00 84.85  ? 1607 MET B C     1 
ATOM   6737 O  O     . MET B 1 390 ? -44.002 2.425   -4.684  1.00 83.69  ? 1607 MET B O     1 
ATOM   6738 C  CB    . MET B 1 390 ? -46.442 0.366   -4.176  1.00 79.53  ? 1607 MET B CB    1 
ATOM   6739 C  CG    . MET B 1 390 ? -45.678 0.375   -2.864  1.00 85.58  ? 1607 MET B CG    1 
ATOM   6740 S  SD    . MET B 1 390 ? -46.093 1.808   -1.872  1.00 96.54  ? 1607 MET B SD    1 
ATOM   6741 C  CE    . MET B 1 390 ? -47.873 1.594   -1.745  1.00 76.50  ? 1607 MET B CE    1 
ATOM   6742 N  N     . PRO B 1 391 ? -44.198 1.091   -6.491  1.00 95.66  ? 1608 PRO B N     1 
ATOM   6743 C  CA    . PRO B 1 391 ? -42.793 1.325   -6.846  1.00 94.88  ? 1608 PRO B CA    1 
ATOM   6744 C  C     . PRO B 1 391 ? -42.586 2.758   -7.279  1.00 100.77 ? 1608 PRO B C     1 
ATOM   6745 O  O     . PRO B 1 391 ? -41.711 3.453   -6.748  1.00 115.57 ? 1608 PRO B O     1 
ATOM   6746 C  CB    . PRO B 1 391 ? -42.547 0.348   -8.000  1.00 93.67  ? 1608 PRO B CB    1 
ATOM   6747 C  CG    . PRO B 1 391 ? -43.608 -0.663  -7.872  1.00 97.93  ? 1608 PRO B CG    1 
ATOM   6748 C  CD    . PRO B 1 391 ? -44.797 0.102   -7.395  1.00 100.80 ? 1608 PRO B CD    1 
ATOM   6749 N  N     . LYS B 1 392 ? -43.414 3.208   -8.227  1.00 93.66  ? 1609 LYS B N     1 
ATOM   6750 C  CA    . LYS B 1 392 ? -43.409 4.611   -8.627  1.00 88.39  ? 1609 LYS B CA    1 
ATOM   6751 C  C     . LYS B 1 392 ? -43.345 5.504   -7.393  1.00 96.94  ? 1609 LYS B C     1 
ATOM   6752 O  O     . LYS B 1 392 ? -42.425 6.322   -7.249  1.00 102.29 ? 1609 LYS B O     1 
ATOM   6753 C  CB    . LYS B 1 392 ? -44.650 4.927   -9.479  1.00 67.31  ? 1609 LYS B CB    1 
ATOM   6754 N  N     . LEU B 1 393 ? -44.272 5.287   -6.450  1.00 95.75  ? 1610 LEU B N     1 
ATOM   6755 C  CA    . LEU B 1 393 ? -44.335 6.112   -5.246  1.00 92.38  ? 1610 LEU B CA    1 
ATOM   6756 C  C     . LEU B 1 393 ? -42.969 6.221   -4.583  1.00 85.39  ? 1610 LEU B C     1 
ATOM   6757 O  O     . LEU B 1 393 ? -42.474 7.332   -4.343  1.00 77.43  ? 1610 LEU B O     1 
ATOM   6758 C  CB    . LEU B 1 393 ? -45.368 5.542   -4.266  1.00 87.71  ? 1610 LEU B CB    1 
ATOM   6759 C  CG    . LEU B 1 393 ? -45.789 6.519   -3.162  1.00 83.40  ? 1610 LEU B CG    1 
ATOM   6760 C  CD1   . LEU B 1 393 ? -46.418 7.751   -3.761  1.00 76.33  ? 1610 LEU B CD1   1 
ATOM   6761 C  CD2   . LEU B 1 393 ? -46.736 5.884   -2.160  1.00 82.33  ? 1610 LEU B CD2   1 
ATOM   6762 N  N     . LEU B 1 394 ? -42.323 5.071   -4.336  1.00 84.24  ? 1611 LEU B N     1 
ATOM   6763 C  CA    . LEU B 1 394 ? -41.042 5.084   -3.640  1.00 85.45  ? 1611 LEU B CA    1 
ATOM   6764 C  C     . LEU B 1 394 ? -39.948 5.728   -4.488  1.00 87.23  ? 1611 LEU B C     1 
ATOM   6765 O  O     . LEU B 1 394 ? -39.148 6.526   -3.975  1.00 88.18  ? 1611 LEU B O     1 
ATOM   6766 C  CB    . LEU B 1 394 ? -40.644 3.671   -3.218  1.00 69.25  ? 1611 LEU B CB    1 
ATOM   6767 C  CG    . LEU B 1 394 ? -41.608 2.999   -2.231  1.00 78.23  ? 1611 LEU B CG    1 
ATOM   6768 C  CD1   . LEU B 1 394 ? -41.624 1.479   -2.450  1.00 94.59  ? 1611 LEU B CD1   1 
ATOM   6769 C  CD2   . LEU B 1 394 ? -41.275 3.323   -0.785  1.00 67.31  ? 1611 LEU B CD2   1 
ATOM   6770 N  N     . GLU B 1 395 ? -39.935 5.451   -5.796  1.00 78.15  ? 1612 GLU B N     1 
ATOM   6771 C  CA    . GLU B 1 395 ? -39.109 6.248   -6.695  1.00 77.71  ? 1612 GLU B CA    1 
ATOM   6772 C  C     . GLU B 1 395 ? -39.366 7.730   -6.439  1.00 87.42  ? 1612 GLU B C     1 
ATOM   6773 O  O     . GLU B 1 395 ? -38.455 8.487   -6.077  1.00 97.50  ? 1612 GLU B O     1 
ATOM   6774 C  CB    . GLU B 1 395 ? -39.408 5.887   -8.160  1.00 76.34  ? 1612 GLU B CB    1 
ATOM   6775 C  CG    . GLU B 1 395 ? -38.761 4.617   -8.687  1.00 73.17  ? 1612 GLU B CG    1 
ATOM   6776 C  CD    . GLU B 1 395 ? -38.892 4.500   -10.205 1.00 72.30  ? 1612 GLU B CD    1 
ATOM   6777 N  N     . THR B 1 396 ? -40.638 8.134   -6.568  1.00 88.68  ? 1613 THR B N     1 
ATOM   6778 C  CA    . THR B 1 396 ? -41.043 9.521   -6.354  1.00 83.55  ? 1613 THR B CA    1 
ATOM   6779 C  C     . THR B 1 396 ? -40.499 10.073  -5.040  1.00 76.89  ? 1613 THR B C     1 
ATOM   6780 O  O     . THR B 1 396 ? -40.096 11.241  -4.967  1.00 80.98  ? 1613 THR B O     1 
ATOM   6781 C  CB    . THR B 1 396 ? -42.563 9.619   -6.408  1.00 83.76  ? 1613 THR B CB    1 
ATOM   6782 O  OG1   . THR B 1 396 ? -42.994 9.354   -7.748  1.00 90.46  ? 1613 THR B OG1   1 
ATOM   6783 C  CG2   . THR B 1 396 ? -43.055 11.010  -5.989  1.00 79.20  ? 1613 THR B CG2   1 
ATOM   6784 N  N     . ILE B 1 397 ? -40.520 9.264   -3.975  1.00 76.79  ? 1614 ILE B N     1 
ATOM   6785 C  CA    . ILE B 1 397 ? -40.094 9.774   -2.676  1.00 76.96  ? 1614 ILE B CA    1 
ATOM   6786 C  C     . ILE B 1 397 ? -38.608 10.129  -2.725  1.00 94.03  ? 1614 ILE B C     1 
ATOM   6787 O  O     . ILE B 1 397 ? -38.205 11.254  -2.393  1.00 93.29  ? 1614 ILE B O     1 
ATOM   6788 C  CB    . ILE B 1 397 ? -40.415 8.748   -1.571  1.00 80.34  ? 1614 ILE B CB    1 
ATOM   6789 C  CG1   . ILE B 1 397 ? -41.937 8.618   -1.364  1.00 88.73  ? 1614 ILE B CG1   1 
ATOM   6790 C  CG2   . ILE B 1 397 ? -39.721 9.100   -0.253  1.00 72.24  ? 1614 ILE B CG2   1 
ATOM   6791 C  CD1   . ILE B 1 397 ? -42.388 7.212   -0.880  1.00 82.38  ? 1614 ILE B CD1   1 
ATOM   6792 N  N     . HIS B 1 398 ? -37.786 9.199   -3.240  1.00 95.54  ? 1615 HIS B N     1 
ATOM   6793 C  CA    . HIS B 1 398 ? -36.343 9.411   -3.293  1.00 75.28  ? 1615 HIS B CA    1 
ATOM   6794 C  C     . HIS B 1 398 ? -36.022 10.717  -3.992  1.00 74.94  ? 1615 HIS B C     1 
ATOM   6795 O  O     . HIS B 1 398 ? -35.363 11.595  -3.420  1.00 84.84  ? 1615 HIS B O     1 
ATOM   6796 C  CB    . HIS B 1 398 ? -35.652 8.237   -4.006  1.00 71.70  ? 1615 HIS B CB    1 
ATOM   6797 C  CG    . HIS B 1 398 ? -34.191 8.471   -4.264  1.00 70.44  ? 1615 HIS B CG    1 
ATOM   6798 N  ND1   . HIS B 1 398 ? -33.727 9.122   -5.390  1.00 70.22  ? 1615 HIS B ND1   1 
ATOM   6799 C  CD2   . HIS B 1 398 ? -33.094 8.154   -3.535  1.00 64.68  ? 1615 HIS B CD2   1 
ATOM   6800 C  CE1   . HIS B 1 398 ? -32.408 9.204   -5.338  1.00 74.92  ? 1615 HIS B CE1   1 
ATOM   6801 N  NE2   . HIS B 1 398 ? -32.000 8.614   -4.228  1.00 73.22  ? 1615 HIS B NE2   1 
ATOM   6802 N  N     . THR B 1 399 ? -36.528 10.881  -5.217  1.00 69.75  ? 1616 THR B N     1 
ATOM   6803 C  CA    . THR B 1 399 ? -36.280 12.102  -5.979  1.00 71.87  ? 1616 THR B CA    1 
ATOM   6804 C  C     . THR B 1 399 ? -36.618 13.342  -5.152  1.00 75.44  ? 1616 THR B C     1 
ATOM   6805 O  O     . THR B 1 399 ? -35.804 14.278  -5.052  1.00 70.31  ? 1616 THR B O     1 
ATOM   6806 C  CB    . THR B 1 399 ? -37.095 12.071  -7.278  1.00 73.05  ? 1616 THR B CB    1 
ATOM   6807 O  OG1   . THR B 1 399 ? -37.049 10.756  -7.838  1.00 76.73  ? 1616 THR B OG1   1 
ATOM   6808 C  CG2   . THR B 1 399 ? -36.517 13.039  -8.279  1.00 77.57  ? 1616 THR B CG2   1 
ATOM   6809 N  N     . SER B 1 400 ? -37.779 13.329  -4.474  1.00 73.24  ? 1617 SER B N     1 
ATOM   6810 C  CA    . SER B 1 400 ? -38.190 14.539  -3.769  1.00 87.34  ? 1617 SER B CA    1 
ATOM   6811 C  C     . SER B 1 400 ? -37.237 14.819  -2.621  1.00 83.69  ? 1617 SER B C     1 
ATOM   6812 O  O     . SER B 1 400 ? -36.869 15.969  -2.369  1.00 77.03  ? 1617 SER B O     1 
ATOM   6813 C  CB    . SER B 1 400 ? -39.638 14.420  -3.252  1.00 97.05  ? 1617 SER B CB    1 
ATOM   6814 N  N     . MET B 1 401 ? -36.795 13.768  -1.940  1.00 80.93  ? 1618 MET B N     1 
ATOM   6815 C  CA    . MET B 1 401 ? -35.767 13.924  -0.919  1.00 77.19  ? 1618 MET B CA    1 
ATOM   6816 C  C     . MET B 1 401 ? -34.468 14.473  -1.511  1.00 83.75  ? 1618 MET B C     1 
ATOM   6817 O  O     . MET B 1 401 ? -33.937 15.490  -1.038  1.00 88.55  ? 1618 MET B O     1 
ATOM   6818 C  CB    . MET B 1 401 ? -35.549 12.577  -0.223  1.00 76.05  ? 1618 MET B CB    1 
ATOM   6819 C  CG    . MET B 1 401 ? -36.834 11.943  0.316   1.00 72.56  ? 1618 MET B CG    1 
ATOM   6820 S  SD    . MET B 1 401 ? -36.531 10.503  1.337   1.00 77.48  ? 1618 MET B SD    1 
ATOM   6821 C  CE    . MET B 1 401 ? -35.451 11.141  2.616   1.00 64.19  ? 1618 MET B CE    1 
ATOM   6822 N  N     . TYR B 1 402 ? -33.987 13.871  -2.606  1.00 81.23  ? 1619 TYR B N     1 
ATOM   6823 C  CA    . TYR B 1 402 ? -32.675 14.261  -3.115  1.00 79.13  ? 1619 TYR B CA    1 
ATOM   6824 C  C     . TYR B 1 402 ? -32.702 15.706  -3.569  1.00 80.41  ? 1619 TYR B C     1 
ATOM   6825 O  O     . TYR B 1 402 ? -31.884 16.531  -3.129  1.00 87.32  ? 1619 TYR B O     1 
ATOM   6826 C  CB    . TYR B 1 402 ? -32.233 13.352  -4.263  1.00 79.89  ? 1619 TYR B CB    1 
ATOM   6827 C  CG    . TYR B 1 402 ? -30.888 13.772  -4.808  1.00 76.16  ? 1619 TYR B CG    1 
ATOM   6828 C  CD1   . TYR B 1 402 ? -29.709 13.414  -4.165  1.00 80.63  ? 1619 TYR B CD1   1 
ATOM   6829 C  CD2   . TYR B 1 402 ? -30.798 14.568  -5.945  1.00 74.98  ? 1619 TYR B CD2   1 
ATOM   6830 C  CE1   . TYR B 1 402 ? -28.484 13.825  -4.659  1.00 79.01  ? 1619 TYR B CE1   1 
ATOM   6831 C  CE2   . TYR B 1 402 ? -29.589 14.980  -6.434  1.00 60.89  ? 1619 TYR B CE2   1 
ATOM   6832 C  CZ    . TYR B 1 402 ? -28.442 14.613  -5.795  1.00 70.40  ? 1619 TYR B CZ    1 
ATOM   6833 O  OH    . TYR B 1 402 ? -27.256 15.035  -6.319  1.00 82.69  ? 1619 TYR B OH    1 
ATOM   6834 N  N     . GLU B 1 403 ? -33.689 16.038  -4.402  1.00 78.39  ? 1620 GLU B N     1 
ATOM   6835 C  CA    . GLU B 1 403 ? -33.813 17.392  -4.930  1.00 87.59  ? 1620 GLU B CA    1 
ATOM   6836 C  C     . GLU B 1 403 ? -34.007 18.392  -3.793  1.00 80.97  ? 1620 GLU B C     1 
ATOM   6837 O  O     . GLU B 1 403 ? -33.412 19.484  -3.811  1.00 69.76  ? 1620 GLU B O     1 
ATOM   6838 C  CB    . GLU B 1 403 ? -34.964 17.446  -5.944  1.00 82.22  ? 1620 GLU B CB    1 
ATOM   6839 C  CG    . GLU B 1 403 ? -34.699 16.567  -7.195  1.00 96.10  ? 1620 GLU B CG    1 
ATOM   6840 C  CD    . GLU B 1 403 ? -35.872 16.504  -8.170  1.00 99.45  ? 1620 GLU B CD    1 
ATOM   6841 O  OE1   . GLU B 1 403 ? -35.656 16.310  -9.393  1.00 88.40  ? 1620 GLU B OE1   1 
ATOM   6842 O  OE2   . GLU B 1 403 ? -37.019 16.642  -7.705  1.00 110.26 ? 1620 GLU B OE2   1 
ATOM   6843 N  N     . ARG B 1 404 ? -34.675 17.991  -2.752  1.00 85.72  ? 1621 ARG B N     1 
ATOM   6844 C  CA    . ARG B 1 404 ? -34.834 18.823  -1.606  1.00 86.67  ? 1621 ARG B CA    1 
ATOM   6845 C  C     . ARG B 1 404 ? -33.484 19.182  -1.029  1.00 89.52  ? 1621 ARG B C     1 
ATOM   6846 O  O     . ARG B 1 404 ? -33.158 20.309  -0.906  1.00 97.71  ? 1621 ARG B O     1 
ATOM   6847 C  CB    . ARG B 1 404 ? -35.662 18.099  -0.573  1.00 87.35  ? 1621 ARG B CB    1 
ATOM   6848 C  CG    . ARG B 1 404 ? -36.608 19.005  0.151   1.00 97.11  ? 1621 ARG B CG    1 
ATOM   6849 C  CD    . ARG B 1 404 ? -37.458 18.335  1.201   1.00 102.11 ? 1621 ARG B CD    1 
ATOM   6850 N  NE    . ARG B 1 404 ? -38.232 17.227  0.693   1.00 105.73 ? 1621 ARG B NE    1 
ATOM   6851 C  CZ    . ARG B 1 404 ? -39.318 17.338  -0.042  1.00 125.63 ? 1621 ARG B CZ    1 
ATOM   6852 N  NH1   . ARG B 1 404 ? -39.762 18.524  -0.394  1.00 125.12 ? 1621 ARG B NH1   1 
ATOM   6853 N  NH2   . ARG B 1 404 ? -39.939 16.251  -0.449  1.00 136.40 ? 1621 ARG B NH2   1 
ATOM   6854 N  N     . ALA B 1 405 ? -32.677 18.203  -0.731  1.00 81.16  ? 1622 ALA B N     1 
ATOM   6855 C  CA    . ALA B 1 405 ? -31.335 18.405  -0.227  1.00 82.33  ? 1622 ALA B CA    1 
ATOM   6856 C  C     . ALA B 1 405 ? -30.505 19.166  -1.242  1.00 79.50  ? 1622 ALA B C     1 
ATOM   6857 O  O     . ALA B 1 405 ? -29.775 20.097  -0.883  1.00 81.17  ? 1622 ALA B O     1 
ATOM   6858 C  CB    . ALA B 1 405 ? -30.718 17.049  0.103   1.00 86.20  ? 1622 ALA B CB    1 
ATOM   6859 N  N     . GLU B 1 406 ? -30.670 18.835  -2.526  1.00 69.52  ? 1623 GLU B N     1 
ATOM   6860 C  CA    . GLU B 1 406 ? -29.909 19.533  -3.548  1.00 77.31  ? 1623 GLU B CA    1 
ATOM   6861 C  C     . GLU B 1 406 ? -30.252 21.009  -3.543  1.00 98.77  ? 1623 GLU B C     1 
ATOM   6862 O  O     . GLU B 1 406 ? -29.364 21.869  -3.423  1.00 110.78 ? 1623 GLU B O     1 
ATOM   6863 C  CB    . GLU B 1 406 ? -30.221 18.932  -4.909  1.00 88.13  ? 1623 GLU B CB    1 
ATOM   6864 C  CG    . GLU B 1 406 ? -29.476 19.574  -6.041  1.00 103.16 ? 1623 GLU B CG    1 
ATOM   6865 C  CD    . GLU B 1 406 ? -29.463 18.694  -7.266  1.00 112.94 ? 1623 GLU B CD    1 
ATOM   6866 O  OE1   . GLU B 1 406 ? -28.361 18.223  -7.644  1.00 116.37 ? 1623 GLU B OE1   1 
ATOM   6867 O  OE2   . GLU B 1 406 ? -30.555 18.472  -7.840  1.00 110.84 ? 1623 GLU B OE2   1 
ATOM   6868 N  N     . ARG B 1 407 ? -31.555 21.312  -3.543  1.00 102.80 ? 1624 ARG B N     1 
ATOM   6869 C  CA    . ARG B 1 407 ? -32.000 22.696  -3.491  1.00 102.12 ? 1624 ARG B CA    1 
ATOM   6870 C  C     . ARG B 1 407 ? -31.306 23.403  -2.345  1.00 105.89 ? 1624 ARG B C     1 
ATOM   6871 O  O     . ARG B 1 407 ? -30.579 24.390  -2.543  1.00 107.45 ? 1624 ARG B O     1 
ATOM   6872 C  CB    . ARG B 1 407 ? -33.520 22.729  -3.321  1.00 92.86  ? 1624 ARG B CB    1 
ATOM   6873 C  CG    . ARG B 1 407 ? -34.155 24.084  -3.395  1.00 97.90  ? 1624 ARG B CG    1 
ATOM   6874 C  CD    . ARG B 1 407 ? -35.530 24.039  -2.753  1.00 105.02 ? 1624 ARG B CD    1 
ATOM   6875 N  NE    . ARG B 1 407 ? -35.448 23.431  -1.429  1.00 105.28 ? 1624 ARG B NE    1 
ATOM   6876 C  CZ    . ARG B 1 407 ? -36.463 22.850  -0.795  1.00 96.74  ? 1624 ARG B CZ    1 
ATOM   6877 N  NH1   . ARG B 1 407 ? -37.665 22.785  -1.352  1.00 82.98  ? 1624 ARG B NH1   1 
ATOM   6878 N  NH2   . ARG B 1 407 ? -36.260 22.333  0.413   1.00 101.17 ? 1624 ARG B NH2   1 
ATOM   6879 N  N     . ASP B 1 408 ? -31.376 22.788  -1.166  1.00 101.49 ? 1625 ASP B N     1 
ATOM   6880 C  CA    . ASP B 1 408 ? -30.830 23.417  0.018   1.00 98.36  ? 1625 ASP B CA    1 
ATOM   6881 C  C     . ASP B 1 408 ? -29.353 23.725  -0.182  1.00 91.86  ? 1625 ASP B C     1 
ATOM   6882 O  O     . ASP B 1 408 ? -28.938 24.890  -0.153  1.00 97.67  ? 1625 ASP B O     1 
ATOM   6883 C  CB    . ASP B 1 408 ? -31.067 22.467  1.183   1.00 99.36  ? 1625 ASP B CB    1 
ATOM   6884 C  CG    . ASP B 1 408 ? -31.215 23.157  2.488   1.00 110.91 ? 1625 ASP B CG    1 
ATOM   6885 O  OD1   . ASP B 1 408 ? -30.622 22.618  3.431   1.00 101.95 ? 1625 ASP B OD1   1 
ATOM   6886 O  OD2   . ASP B 1 408 ? -31.918 24.192  2.588   1.00 127.92 ? 1625 ASP B OD2   1 
ATOM   6887 N  N     . LEU B 1 409 ? -28.594 22.715  -0.590  1.00 83.76  ? 1626 LEU B N     1 
ATOM   6888 C  CA    . LEU B 1 409 ? -27.154 22.870  -0.729  1.00 78.78  ? 1626 LEU B CA    1 
ATOM   6889 C  C     . LEU B 1 409 ? -26.807 23.896  -1.780  1.00 90.67  ? 1626 LEU B C     1 
ATOM   6890 O  O     . LEU B 1 409 ? -25.862 24.667  -1.605  1.00 100.85 ? 1626 LEU B O     1 
ATOM   6891 C  CB    . LEU B 1 409 ? -26.513 21.528  -1.075  1.00 70.21  ? 1626 LEU B CB    1 
ATOM   6892 C  CG    . LEU B 1 409 ? -25.038 21.497  -1.408  1.00 79.67  ? 1626 LEU B CG    1 
ATOM   6893 C  CD1   . LEU B 1 409 ? -24.420 20.466  -0.528  1.00 92.24  ? 1626 LEU B CD1   1 
ATOM   6894 C  CD2   . LEU B 1 409 ? -24.923 21.104  -2.850  1.00 80.37  ? 1626 LEU B CD2   1 
ATOM   6895 N  N     . GLN B 1 410 ? -27.523 23.912  -2.897  1.00 93.63  ? 1627 GLN B N     1 
ATOM   6896 C  CA    . GLN B 1 410 ? -27.059 24.884  -3.876  1.00 101.46 ? 1627 GLN B CA    1 
ATOM   6897 C  C     . GLN B 1 410 ? -27.538 26.281  -3.548  1.00 107.84 ? 1627 GLN B C     1 
ATOM   6898 O  O     . GLN B 1 410 ? -26.928 27.248  -4.002  1.00 105.13 ? 1627 GLN B O     1 
ATOM   6899 C  CB    . GLN B 1 410 ? -27.407 24.445  -5.293  1.00 107.47 ? 1627 GLN B CB    1 
ATOM   6900 C  CG    . GLN B 1 410 ? -26.160 23.799  -5.888  1.00 125.06 ? 1627 GLN B CG    1 
ATOM   6901 C  CD    . GLN B 1 410 ? -26.450 22.664  -6.831  1.00 138.45 ? 1627 GLN B CD    1 
ATOM   6902 O  OE1   . GLN B 1 410 ? -27.475 22.658  -7.510  1.00 142.88 ? 1627 GLN B OE1   1 
ATOM   6903 N  NE2   . GLN B 1 410 ? -25.550 21.678  -6.868  1.00 140.54 ? 1627 GLN B NE2   1 
ATOM   6904 N  N     . SER B 1 411 ? -28.597 26.408  -2.751  1.00 116.68 ? 1628 SER B N     1 
ATOM   6905 C  CA    . SER B 1 411 ? -28.864 27.740  -2.251  1.00 119.42 ? 1628 SER B CA    1 
ATOM   6906 C  C     . SER B 1 411 ? -27.787 28.179  -1.251  1.00 118.55 ? 1628 SER B C     1 
ATOM   6907 O  O     . SER B 1 411 ? -27.788 29.374  -0.898  1.00 129.14 ? 1628 SER B O     1 
ATOM   6908 C  CB    . SER B 1 411 ? -30.313 27.842  -1.720  1.00 117.74 ? 1628 SER B CB    1 
ATOM   6909 O  OG    . SER B 1 411 ? -30.470 27.588  -0.342  1.00 120.99 ? 1628 SER B OG    1 
ATOM   6910 N  N     . HIS B 1 412 ? -26.860 27.310  -0.889  1.00 85.59  ? 1629 HIS B N     1 
ATOM   6911 C  CA    . HIS B 1 412 ? -25.865 27.703  0.074   1.00 87.76  ? 1629 HIS B CA    1 
ATOM   6912 C  C     . HIS B 1 412 ? -24.424 27.518  -0.258  1.00 81.84  ? 1629 HIS B C     1 
ATOM   6913 O  O     . HIS B 1 412 ? -23.592 27.374  0.587   1.00 74.36  ? 1629 HIS B O     1 
ATOM   6914 C  CB    . HIS B 1 412 ? -26.127 27.084  1.387   1.00 93.37  ? 1629 HIS B CB    1 
ATOM   6915 C  CG    . HIS B 1 412 ? -27.339 27.596  2.056   1.00 125.22 ? 1629 HIS B CG    1 
ATOM   6916 N  ND1   . HIS B 1 412 ? -28.564 26.999  1.930   1.00 129.86 ? 1629 HIS B ND1   1 
ATOM   6917 C  CD2   . HIS B 1 412 ? -27.518 28.652  2.870   1.00 128.91 ? 1629 HIS B CD2   1 
ATOM   6918 C  CE1   . HIS B 1 412 ? -29.439 27.643  2.676   1.00 127.59 ? 1629 HIS B CE1   1 
ATOM   6919 N  NE2   . HIS B 1 412 ? -28.836 28.667  3.232   1.00 133.02 ? 1629 HIS B NE2   1 
ATOM   6920 N  N     . THR B 1 413 ? -24.138 27.506  -1.517  1.00 84.75  ? 1630 THR B N     1 
ATOM   6921 C  CA    . THR B 1 413 ? -22.740 27.481  -1.955  1.00 87.96  ? 1630 THR B CA    1 
ATOM   6922 C  C     . THR B 1 413 ? -22.518 28.764  -2.753  1.00 95.90  ? 1630 THR B C     1 
ATOM   6923 O  O     . THR B 1 413 ? -23.122 28.968  -3.816  1.00 101.41 ? 1630 THR B O     1 
ATOM   6924 C  CB    . THR B 1 413 ? -22.373 26.209  -2.755  1.00 83.13  ? 1630 THR B CB    1 
ATOM   6925 O  OG1   . THR B 1 413 ? -22.739 26.326  -4.134  1.00 84.74  ? 1630 THR B OG1   1 
ATOM   6926 C  CG2   . THR B 1 413 ? -23.077 25.018  -2.204  1.00 85.68  ? 1630 THR B CG2   1 
ATOM   6927 N  N     . LYS B 1 414 ? -21.672 29.636  -2.219  1.00 93.50  ? 1631 LYS B N     1 
ATOM   6928 C  CA    . LYS B 1 414 ? -21.459 30.971  -2.758  1.00 95.09  ? 1631 LYS B CA    1 
ATOM   6929 C  C     . LYS B 1 414 ? -20.066 31.070  -3.360  1.00 97.98  ? 1631 LYS B C     1 
ATOM   6930 O  O     . LYS B 1 414 ? -19.118 30.455  -2.867  1.00 97.42  ? 1631 LYS B O     1 
ATOM   6931 C  CB    . LYS B 1 414 ? -21.649 32.035  -1.671  1.00 75.48  ? 1631 LYS B CB    1 
ATOM   6932 N  N     . LEU B 1 415 ? -19.961 31.814  -4.456  1.00 105.13 ? 1632 LEU B N     1 
ATOM   6933 C  CA    . LEU B 1 415 ? -18.704 32.034  -5.154  1.00 104.19 ? 1632 LEU B CA    1 
ATOM   6934 C  C     . LEU B 1 415 ? -18.221 33.445  -4.887  1.00 106.78 ? 1632 LEU B C     1 
ATOM   6935 O  O     . LEU B 1 415 ? -19.009 34.391  -4.898  1.00 128.64 ? 1632 LEU B O     1 
ATOM   6936 C  CB    . LEU B 1 415 ? -18.883 31.834  -6.661  1.00 106.44 ? 1632 LEU B CB    1 
ATOM   6937 C  CG    . LEU B 1 415 ? -17.673 31.880  -7.589  1.00 104.31 ? 1632 LEU B CG    1 
ATOM   6938 C  CD1   . LEU B 1 415 ? -16.733 30.714  -7.304  1.00 103.47 ? 1632 LEU B CD1   1 
ATOM   6939 C  CD2   . LEU B 1 415 ? -18.131 31.852  -9.036  1.00 100.31 ? 1632 LEU B CD2   1 
ATOM   6940 N  N     . THR B 1 416 ? -16.928 33.580  -4.630  1.00 106.01 ? 1633 THR B N     1 
ATOM   6941 C  CA    . THR B 1 416 ? -16.319 34.892  -4.497  1.00 106.18 ? 1633 THR B CA    1 
ATOM   6942 C  C     . THR B 1 416 ? -14.860 34.818  -4.915  1.00 103.12 ? 1633 THR B C     1 
ATOM   6943 O  O     . THR B 1 416 ? -14.267 33.743  -4.999  1.00 110.35 ? 1633 THR B O     1 
ATOM   6944 C  CB    . THR B 1 416 ? -16.408 35.419  -3.065  1.00 109.63 ? 1633 THR B CB    1 
ATOM   6945 O  OG1   . THR B 1 416 ? -15.730 36.678  -2.986  1.00 123.38 ? 1633 THR B OG1   1 
ATOM   6946 C  CG2   . THR B 1 416 ? -15.742 34.454  -2.111  1.00 101.79 ? 1633 THR B CG2   1 
ATOM   6947 N  N     . LYS B 1 417 ? -14.293 35.984  -5.180  1.00 100.47 ? 1634 LYS B N     1 
ATOM   6948 C  CA    . LYS B 1 417 ? -12.851 36.154  -5.213  1.00 95.15  ? 1634 LYS B CA    1 
ATOM   6949 C  C     . LYS B 1 417 ? -12.378 37.094  -4.113  1.00 92.02  ? 1634 LYS B C     1 
ATOM   6950 O  O     . LYS B 1 417 ? -11.166 37.290  -3.968  1.00 97.07  ? 1634 LYS B O     1 
ATOM   6951 C  CB    . LYS B 1 417 ? -12.405 36.681  -6.585  1.00 85.57  ? 1634 LYS B CB    1 
ATOM   6952 C  CG    . LYS B 1 417 ? -13.047 35.953  -7.750  1.00 85.62  ? 1634 LYS B CG    1 
ATOM   6953 C  CD    . LYS B 1 417 ? -12.192 36.071  -8.987  1.00 88.98  ? 1634 LYS B CD    1 
ATOM   6954 C  CE    . LYS B 1 417 ? -12.909 36.825  -10.086 1.00 98.77  ? 1634 LYS B CE    1 
ATOM   6955 N  NZ    . LYS B 1 417 ? -12.529 36.290  -11.419 1.00 105.58 ? 1634 LYS B NZ    1 
ATOM   6956 N  N     . GLN B 1 418 ? -13.297 37.654  -3.315  1.00 89.75  ? 1635 GLN B N     1 
ATOM   6957 C  CA    . GLN B 1 418 ? -12.981 38.660  -2.311  1.00 88.53  ? 1635 GLN B CA    1 
ATOM   6958 C  C     . GLN B 1 418 ? -13.212 38.164  -0.894  1.00 96.20  ? 1635 GLN B C     1 
ATOM   6959 O  O     . GLN B 1 418 ? -14.274 37.622  -0.572  1.00 115.09 ? 1635 GLN B O     1 
ATOM   6960 C  CB    . GLN B 1 418 ? -13.801 39.906  -2.539  1.00 89.96  ? 1635 GLN B CB    1 
ATOM   6961 C  CG    . GLN B 1 418 ? -13.208 41.088  -1.837  1.00 102.02 ? 1635 GLN B CG    1 
ATOM   6962 C  CD    . GLN B 1 418 ? -12.290 41.884  -2.745  1.00 110.40 ? 1635 GLN B CD    1 
ATOM   6963 O  OE1   . GLN B 1 418 ? -12.138 41.592  -3.932  1.00 109.62 ? 1635 GLN B OE1   1 
ATOM   6964 N  NE2   . GLN B 1 418 ? -11.650 42.864  -2.179  1.00 112.88 ? 1635 GLN B NE2   1 
ATOM   6965 N  N     . TRP B 1 419 ? -12.220 38.426  -0.045  1.00 90.85  ? 1636 TRP B N     1 
ATOM   6966 C  CA    . TRP B 1 419 ? -12.160 37.861  1.300   1.00 94.25  ? 1636 TRP B CA    1 
ATOM   6967 C  C     . TRP B 1 419 ? -13.279 38.399  2.189   1.00 89.36  ? 1636 TRP B C     1 
ATOM   6968 O  O     . TRP B 1 419 ? -13.785 37.681  3.059   1.00 95.16  ? 1636 TRP B O     1 
ATOM   6969 C  CB    . TRP B 1 419 ? -10.749 38.125  1.856   1.00 104.20 ? 1636 TRP B CB    1 
ATOM   6970 C  CG    . TRP B 1 419 ? -10.402 37.760  3.301   1.00 105.64 ? 1636 TRP B CG    1 
ATOM   6971 C  CD1   . TRP B 1 419 ? -10.054 38.633  4.293   1.00 109.26 ? 1636 TRP B CD1   1 
ATOM   6972 C  CD2   . TRP B 1 419 ? -10.294 36.452  3.875   1.00 93.97  ? 1636 TRP B CD2   1 
ATOM   6973 N  NE1   . TRP B 1 419 ? -9.770  37.957  5.453   1.00 102.16 ? 1636 TRP B NE1   1 
ATOM   6974 C  CE2   . TRP B 1 419 ? -9.913  36.616  5.224   1.00 93.10  ? 1636 TRP B CE2   1 
ATOM   6975 C  CE3   . TRP B 1 419 ? -10.496 35.164  3.387   1.00 95.31  ? 1636 TRP B CE3   1 
ATOM   6976 C  CZ2   . TRP B 1 419 ? -9.735  35.543  6.088   1.00 86.73  ? 1636 TRP B CZ2   1 
ATOM   6977 C  CZ3   . TRP B 1 419 ? -10.319 34.100  4.249   1.00 95.88  ? 1636 TRP B CZ3   1 
ATOM   6978 C  CH2   . TRP B 1 419 ? -9.939  34.299  5.585   1.00 89.84  ? 1636 TRP B CH2   1 
ATOM   6979 N  N     . ALA B 1 420 ? -13.709 39.637  1.961   1.00 96.10  ? 1637 ALA B N     1 
ATOM   6980 C  CA    . ALA B 1 420 ? -14.742 40.240  2.805   1.00 105.12 ? 1637 ALA B CA    1 
ATOM   6981 C  C     . ALA B 1 420 ? -16.079 39.528  2.657   1.00 102.45 ? 1637 ALA B C     1 
ATOM   6982 O  O     . ALA B 1 420 ? -16.731 39.201  3.655   1.00 98.98  ? 1637 ALA B O     1 
ATOM   6983 C  CB    . ALA B 1 420 ? -14.898 41.721  2.468   1.00 100.13 ? 1637 ALA B CB    1 
ATOM   6984 N  N     . GLU B 1 421 ? -16.528 39.311  1.422   1.00 104.55 ? 1638 GLU B N     1 
ATOM   6985 C  CA    . GLU B 1 421 ? -17.748 38.539  1.265   1.00 110.60 ? 1638 GLU B CA    1 
ATOM   6986 C  C     . GLU B 1 421 ? -17.518 37.074  1.582   1.00 108.44 ? 1638 GLU B C     1 
ATOM   6987 O  O     . GLU B 1 421 ? -18.460 36.407  2.004   1.00 109.48 ? 1638 GLU B O     1 
ATOM   6988 C  CB    . GLU B 1 421 ? -18.340 38.711  -0.125  1.00 119.31 ? 1638 GLU B CB    1 
ATOM   6989 C  CG    . GLU B 1 421 ? -17.358 38.611  -1.235  1.00 131.93 ? 1638 GLU B CG    1 
ATOM   6990 C  CD    . GLU B 1 421 ? -18.061 38.462  -2.554  1.00 143.52 ? 1638 GLU B CD    1 
ATOM   6991 O  OE1   . GLU B 1 421 ? -19.310 38.431  -2.548  1.00 141.31 ? 1638 GLU B OE1   1 
ATOM   6992 O  OE2   . GLU B 1 421 ? -17.372 38.383  -3.591  1.00 152.28 ? 1638 GLU B OE2   1 
ATOM   6993 N  N     . PHE B 1 422 ? -16.287 36.554  1.406   1.00 108.53 ? 1639 PHE B N     1 
ATOM   6994 C  CA    . PHE B 1 422 ? -15.993 35.187  1.861   1.00 111.60 ? 1639 PHE B CA    1 
ATOM   6995 C  C     . PHE B 1 422 ? -16.329 35.053  3.337   1.00 118.29 ? 1639 PHE B C     1 
ATOM   6996 O  O     . PHE B 1 422 ? -17.013 34.102  3.749   1.00 108.60 ? 1639 PHE B O     1 
ATOM   6997 C  CB    . PHE B 1 422 ? -14.507 34.844  1.605   1.00 102.53 ? 1639 PHE B CB    1 
ATOM   6998 C  CG    . PHE B 1 422 ? -14.032 33.489  2.200   1.00 85.22  ? 1639 PHE B CG    1 
ATOM   6999 C  CD1   . PHE B 1 422 ? -13.801 32.393  1.367   1.00 84.06  ? 1639 PHE B CD1   1 
ATOM   7000 C  CD2   . PHE B 1 422 ? -13.749 33.338  3.564   1.00 78.18  ? 1639 PHE B CD2   1 
ATOM   7001 C  CE1   . PHE B 1 422 ? -13.340 31.160  1.882   1.00 74.67  ? 1639 PHE B CE1   1 
ATOM   7002 C  CE2   . PHE B 1 422 ? -13.299 32.099  4.084   1.00 79.46  ? 1639 PHE B CE2   1 
ATOM   7003 C  CZ    . PHE B 1 422 ? -13.091 31.024  3.236   1.00 74.59  ? 1639 PHE B CZ    1 
ATOM   7004 N  N     . LEU B 1 423 ? -15.958 36.078  4.126   1.00 113.20 ? 1640 LEU B N     1 
ATOM   7005 C  CA    . LEU B 1 423 ? -16.073 36.041  5.579   1.00 114.02 ? 1640 LEU B CA    1 
ATOM   7006 C  C     . LEU B 1 423 ? -17.494 36.398  6.010   1.00 112.83 ? 1640 LEU B C     1 
ATOM   7007 O  O     . LEU B 1 423 ? -18.020 35.838  6.991   1.00 117.88 ? 1640 LEU B O     1 
ATOM   7008 C  CB    . LEU B 1 423 ? -15.032 36.999  6.134   1.00 115.32 ? 1640 LEU B CB    1 
ATOM   7009 C  CG    . LEU B 1 423 ? -14.117 36.956  7.364   1.00 119.20 ? 1640 LEU B CG    1 
ATOM   7010 C  CD1   . LEU B 1 423 ? -13.209 35.800  7.133   1.00 125.48 ? 1640 LEU B CD1   1 
ATOM   7011 C  CD2   . LEU B 1 423 ? -13.277 38.222  7.260   1.00 118.81 ? 1640 LEU B CD2   1 
ATOM   7012 N  N     . GLN B 1 424 ? -18.201 37.197  5.213   1.00 108.13 ? 1641 GLN B N     1 
ATOM   7013 C  CA    . GLN B 1 424 ? -19.631 37.422  5.401   1.00 98.35  ? 1641 GLN B CA    1 
ATOM   7014 C  C     . GLN B 1 424 ? -20.460 36.163  5.126   1.00 95.98  ? 1641 GLN B C     1 
ATOM   7015 O  O     . GLN B 1 424 ? -21.257 35.743  5.974   1.00 81.63  ? 1641 GLN B O     1 
ATOM   7016 C  CB    . GLN B 1 424 ? -20.064 38.597  4.512   1.00 93.09  ? 1641 GLN B CB    1 
ATOM   7017 N  N     . PHE B 1 425 ? -20.330 35.578  3.928   1.00 92.56  ? 1642 PHE B N     1 
ATOM   7018 C  CA    . PHE B 1 425 ? -20.950 34.279  3.656   1.00 93.01  ? 1642 PHE B CA    1 
ATOM   7019 C  C     . PHE B 1 425 ? -20.658 33.295  4.772   1.00 99.35  ? 1642 PHE B C     1 
ATOM   7020 O  O     . PHE B 1 425 ? -21.542 32.551  5.203   1.00 99.54  ? 1642 PHE B O     1 
ATOM   7021 C  CB    . PHE B 1 425 ? -20.412 33.646  2.366   1.00 91.67  ? 1642 PHE B CB    1 
ATOM   7022 C  CG    . PHE B 1 425 ? -20.668 34.432  1.124   1.00 99.33  ? 1642 PHE B CG    1 
ATOM   7023 C  CD1   . PHE B 1 425 ? -21.725 35.313  1.035   1.00 80.59  ? 1642 PHE B CD1   1 
ATOM   7024 C  CD2   . PHE B 1 425 ? -19.828 34.279  0.028   1.00 100.91 ? 1642 PHE B CD2   1 
ATOM   7025 C  CE1   . PHE B 1 425 ? -21.942 36.008  -0.126  1.00 81.89  ? 1642 PHE B CE1   1 
ATOM   7026 C  CE2   . PHE B 1 425 ? -20.033 34.995  -1.144  1.00 101.53 ? 1642 PHE B CE2   1 
ATOM   7027 C  CZ    . PHE B 1 425 ? -21.089 35.848  -1.224  1.00 81.69  ? 1642 PHE B CZ    1 
ATOM   7028 N  N     . LEU B 1 426 ? -19.419 33.291  5.272   1.00 109.99 ? 1643 LEU B N     1 
ATOM   7029 C  CA    . LEU B 1 426 ? -19.084 32.332  6.311   1.00 107.59 ? 1643 LEU B CA    1 
ATOM   7030 C  C     . LEU B 1 426 ? -19.879 32.612  7.576   1.00 98.18  ? 1643 LEU B C     1 
ATOM   7031 O  O     . LEU B 1 426 ? -20.183 31.684  8.322   1.00 81.00  ? 1643 LEU B O     1 
ATOM   7032 C  CB    . LEU B 1 426 ? -17.580 32.364  6.592   1.00 110.59 ? 1643 LEU B CB    1 
ATOM   7033 C  CG    . LEU B 1 426 ? -17.063 31.347  7.607   1.00 102.42 ? 1643 LEU B CG    1 
ATOM   7034 C  CD1   . LEU B 1 426 ? -16.920 29.988  6.949   1.00 92.86  ? 1643 LEU B CD1   1 
ATOM   7035 C  CD2   . LEU B 1 426 ? -15.746 31.812  8.221   1.00 100.07 ? 1643 LEU B CD2   1 
ATOM   7036 N  N     . GLU B 1 427 ? -20.213 33.882  7.840   1.00 113.43 ? 1644 GLU B N     1 
ATOM   7037 C  CA    . GLU B 1 427 ? -21.133 34.181  8.940   1.00 114.61 ? 1644 GLU B CA    1 
ATOM   7038 C  C     . GLU B 1 427 ? -22.570 33.713  8.647   1.00 117.32 ? 1644 GLU B C     1 
ATOM   7039 O  O     . GLU B 1 427 ? -23.269 33.254  9.557   1.00 115.86 ? 1644 GLU B O     1 
ATOM   7040 C  CB    . GLU B 1 427 ? -21.112 35.675  9.249   1.00 112.18 ? 1644 GLU B CB    1 
ATOM   7041 N  N     . THR B 1 428 ? -23.037 33.817  7.385   1.00 117.11 ? 1645 THR B N     1 
ATOM   7042 C  CA    . THR B 1 428 ? -24.414 33.446  7.004   1.00 107.50 ? 1645 THR B CA    1 
ATOM   7043 C  C     . THR B 1 428 ? -24.676 31.914  6.843   1.00 111.49 ? 1645 THR B C     1 
ATOM   7044 O  O     . THR B 1 428 ? -25.648 31.562  6.162   1.00 101.13 ? 1645 THR B O     1 
ATOM   7045 C  CB    . THR B 1 428 ? -24.842 34.141  5.704   1.00 98.63  ? 1645 THR B CB    1 
ATOM   7046 O  OG1   . THR B 1 428 ? -24.460 33.317  4.587   1.00 89.66  ? 1645 THR B OG1   1 
ATOM   7047 C  CG2   . THR B 1 428 ? -24.254 35.584  5.578   1.00 92.95  ? 1645 THR B CG2   1 
ATOM   7048 N  N     . LYS B 1 429 ? -23.812 31.021  7.348   1.00 119.90 ? 1646 LYS B N     1 
ATOM   7049 C  CA    . LYS B 1 429 ? -24.070 29.566  7.440   1.00 121.68 ? 1646 LYS B CA    1 
ATOM   7050 C  C     . LYS B 1 429 ? -24.062 28.854  6.070   1.00 123.04 ? 1646 LYS B C     1 
ATOM   7051 O  O     . LYS B 1 429 ? -24.859 27.948  5.807   1.00 119.72 ? 1646 LYS B O     1 
ATOM   7052 C  CB    . LYS B 1 429 ? -25.365 29.268  8.241   1.00 126.57 ? 1646 LYS B CB    1 
ATOM   7053 N  N     . ASN B 1 430 ? -23.054 29.146  5.245   1.00 124.94 ? 1647 ASN B N     1 
ATOM   7054 C  CA    . ASN B 1 430 ? -22.946 28.402  3.992   1.00 114.99 ? 1647 ASN B CA    1 
ATOM   7055 C  C     . ASN B 1 430 ? -21.492 28.271  3.545   1.00 103.72 ? 1647 ASN B C     1 
ATOM   7056 O  O     . ASN B 1 430 ? -20.575 28.776  4.190   1.00 82.93  ? 1647 ASN B O     1 
ATOM   7057 C  CB    . ASN B 1 430 ? -23.843 29.030  2.923   1.00 114.19 ? 1647 ASN B CB    1 
ATOM   7058 C  CG    . ASN B 1 430 ? -23.592 30.474  2.673   1.00 105.70 ? 1647 ASN B CG    1 
ATOM   7059 O  OD1   . ASN B 1 430 ? -23.094 31.184  3.526   1.00 114.28 ? 1647 ASN B OD1   1 
ATOM   7060 N  ND2   . ASN B 1 430 ? -24.005 30.939  1.495   1.00 89.25  ? 1647 ASN B ND2   1 
ATOM   7061 N  N     . ILE B 1 431 ? -21.280 27.552  2.433   1.00 104.60 ? 1648 ILE B N     1 
ATOM   7062 C  CA    . ILE B 1 431 ? -19.929 27.164  2.031   1.00 103.39 ? 1648 ILE B CA    1 
ATOM   7063 C  C     . ILE B 1 431 ? -19.552 27.874  0.736   1.00 113.00 ? 1648 ILE B C     1 
ATOM   7064 O  O     . ILE B 1 431 ? -20.402 28.137  -0.121  1.00 119.16 ? 1648 ILE B O     1 
ATOM   7065 C  CB    . ILE B 1 431 ? -19.801 25.624  1.945   1.00 99.70  ? 1648 ILE B CB    1 
ATOM   7066 C  CG1   . ILE B 1 431 ? -20.575 24.993  0.771   1.00 89.00  ? 1648 ILE B CG1   1 
ATOM   7067 C  CG2   . ILE B 1 431 ? -20.302 24.984  3.232   1.00 105.33 ? 1648 ILE B CG2   1 
ATOM   7068 C  CD1   . ILE B 1 431 ? -19.774 24.782  -0.514  1.00 107.98 ? 1648 ILE B CD1   1 
ATOM   7069 N  N     . ILE B 1 432 ? -18.249 28.151  0.587   1.00 104.98 ? 1649 ILE B N     1 
ATOM   7070 C  CA    . ILE B 1 432 ? -17.743 29.200  -0.303  1.00 89.67  ? 1649 ILE B CA    1 
ATOM   7071 C  C     . ILE B 1 432 ? -16.684 28.632  -1.238  1.00 89.92  ? 1649 ILE B C     1 
ATOM   7072 O  O     . ILE B 1 432 ? -15.663 28.110  -0.779  1.00 84.22  ? 1649 ILE B O     1 
ATOM   7073 C  CB    . ILE B 1 432 ? -17.146 30.376  0.484   1.00 85.84  ? 1649 ILE B CB    1 
ATOM   7074 C  CG1   . ILE B 1 432 ? -18.093 30.853  1.580   1.00 83.62  ? 1649 ILE B CG1   1 
ATOM   7075 C  CG2   . ILE B 1 432 ? -16.794 31.530  -0.458  1.00 91.07  ? 1649 ILE B CG2   1 
ATOM   7076 C  CD1   . ILE B 1 432 ? -17.650 30.460  2.968   1.00 81.92  ? 1649 ILE B CD1   1 
ATOM   7077 N  N     . MET B 1 433 ? -16.894 28.784  -2.541  1.00 92.91  ? 1650 MET B N     1 
ATOM   7078 C  CA    . MET B 1 433 ? -15.845 28.515  -3.514  1.00 91.63  ? 1650 MET B CA    1 
ATOM   7079 C  C     . MET B 1 433 ? -15.031 29.787  -3.744  1.00 81.26  ? 1650 MET B C     1 
ATOM   7080 O  O     . MET B 1 433 ? -15.564 30.789  -4.204  1.00 74.35  ? 1650 MET B O     1 
ATOM   7081 C  CB    . MET B 1 433 ? -16.445 28.011  -4.825  1.00 70.24  ? 1650 MET B CB    1 
ATOM   7082 C  CG    . MET B 1 433 ? -15.888 26.683  -5.248  1.00 100.11 ? 1650 MET B CG    1 
ATOM   7083 S  SD    . MET B 1 433 ? -17.121 25.571  -5.957  1.00 100.03 ? 1650 MET B SD    1 
ATOM   7084 N  N     . ALA B 1 434 ? -13.729 29.711  -3.506  1.00 83.05  ? 1651 ALA B N     1 
ATOM   7085 C  CA    . ALA B 1 434 ? -12.828 30.845  -3.567  1.00 74.92  ? 1651 ALA B CA    1 
ATOM   7086 C  C     . ALA B 1 434 ? -11.527 30.445  -4.247  1.00 77.02  ? 1651 ALA B C     1 
ATOM   7087 O  O     . ALA B 1 434 ? -11.161 29.264  -4.252  1.00 89.72  ? 1651 ALA B O     1 
ATOM   7088 C  CB    . ALA B 1 434 ? -12.535 31.377  -2.158  1.00 83.58  ? 1651 ALA B CB    1 
ATOM   7089 N  N     . PRO B 1 435 ? -10.830 31.399  -4.863  1.00 80.71  ? 1652 PRO B N     1 
ATOM   7090 C  CA    . PRO B 1 435 ? -9.531  31.098  -5.499  1.00 98.21  ? 1652 PRO B CA    1 
ATOM   7091 C  C     . PRO B 1 435 ? -8.416  30.947  -4.468  1.00 104.74 ? 1652 PRO B C     1 
ATOM   7092 O  O     . PRO B 1 435 ? -8.226  31.815  -3.616  1.00 105.30 ? 1652 PRO B O     1 
ATOM   7093 C  CB    . PRO B 1 435 ? -9.294  32.310  -6.410  1.00 103.28 ? 1652 PRO B CB    1 
ATOM   7094 C  CG    . PRO B 1 435 ? -10.114 33.413  -5.801  1.00 94.82  ? 1652 PRO B CG    1 
ATOM   7095 C  CD    . PRO B 1 435 ? -11.297 32.767  -5.148  1.00 81.53  ? 1652 PRO B CD    1 
ATOM   7096 N  N     . PHE B 1 436 ? -7.653  29.856  -4.573  1.00 103.73 ? 1653 PHE B N     1 
ATOM   7097 C  CA    . PHE B 1 436 ? -6.724  29.448  -3.529  1.00 102.37 ? 1653 PHE B CA    1 
ATOM   7098 C  C     . PHE B 1 436 ? -5.377  29.083  -4.129  1.00 102.23 ? 1653 PHE B C     1 
ATOM   7099 O  O     . PHE B 1 436 ? -5.300  28.464  -5.208  1.00 99.94  ? 1653 PHE B O     1 
ATOM   7100 C  CB    . PHE B 1 436 ? -7.274  28.264  -2.735  1.00 102.31 ? 1653 PHE B CB    1 
ATOM   7101 C  CG    . PHE B 1 436 ? -6.391  27.817  -1.603  1.00 105.47 ? 1653 PHE B CG    1 
ATOM   7102 C  CD1   . PHE B 1 436 ? -5.760  28.735  -0.781  1.00 104.89 ? 1653 PHE B CD1   1 
ATOM   7103 C  CD2   . PHE B 1 436 ? -6.213  26.457  -1.351  1.00 109.25 ? 1653 PHE B CD2   1 
ATOM   7104 C  CE1   . PHE B 1 436 ? -4.946  28.308  0.264   1.00 106.84 ? 1653 PHE B CE1   1 
ATOM   7105 C  CE2   . PHE B 1 436 ? -5.412  26.017  -0.302  1.00 108.61 ? 1653 PHE B CE2   1 
ATOM   7106 C  CZ    . PHE B 1 436 ? -4.770  26.944  0.500   1.00 111.09 ? 1653 PHE B CZ    1 
ATOM   7107 N  N     . CYS B 1 437 ? -4.329  29.523  -3.436  1.00 102.22 ? 1654 CYS B N     1 
ATOM   7108 C  CA    . CYS B 1 437 ? -2.972  29.183  -3.838  1.00 96.34  ? 1654 CYS B CA    1 
ATOM   7109 C  C     . CYS B 1 437 ? -2.642  27.702  -3.652  1.00 88.35  ? 1654 CYS B C     1 
ATOM   7110 O  O     . CYS B 1 437 ? -1.833  27.165  -4.405  1.00 94.39  ? 1654 CYS B O     1 
ATOM   7111 C  CB    . CYS B 1 437 ? -1.957  30.060  -3.101  1.00 101.65 ? 1654 CYS B CB    1 
ATOM   7112 S  SG    . CYS B 1 437 ? -1.611  29.670  -1.381  1.00 93.63  ? 1654 CYS B SG    1 
ATOM   7113 N  N     . GLY B 1 438 ? -3.274  27.016  -2.705  1.00 83.69  ? 1655 GLY B N     1 
ATOM   7114 C  CA    . GLY B 1 438 ? -2.918  25.638  -2.464  1.00 80.13  ? 1655 GLY B CA    1 
ATOM   7115 C  C     . GLY B 1 438 ? -1.864  25.413  -1.395  1.00 78.41  ? 1655 GLY B C     1 
ATOM   7116 O  O     . GLY B 1 438 ? -1.571  24.258  -1.036  1.00 81.94  ? 1655 GLY B O     1 
ATOM   7117 N  N     . GLU B 1 439 ? -1.230  26.463  -0.920  1.00 85.01  ? 1656 GLU B N     1 
ATOM   7118 C  CA    . GLU B 1 439 ? -0.184  26.283  0.061   1.00 87.96  ? 1656 GLU B CA    1 
ATOM   7119 C  C     . GLU B 1 439 ? -0.769  25.945  1.431   1.00 87.89  ? 1656 GLU B C     1 
ATOM   7120 O  O     . GLU B 1 439 ? -1.916  26.258  1.759   1.00 80.73  ? 1656 GLU B O     1 
ATOM   7121 C  CB    . GLU B 1 439 ? 0.663   27.545  0.168   1.00 87.19  ? 1656 GLU B CB    1 
ATOM   7122 C  CG    . GLU B 1 439 ? 1.372   27.854  -1.111  1.00 97.13  ? 1656 GLU B CG    1 
ATOM   7123 C  CD    . GLU B 1 439 ? 2.441   26.846  -1.419  1.00 106.14 ? 1656 GLU B CD    1 
ATOM   7124 O  OE1   . GLU B 1 439 ? 3.361   26.681  -0.590  1.00 112.44 ? 1656 GLU B OE1   1 
ATOM   7125 O  OE2   . GLU B 1 439 ? 2.348   26.216  -2.487  1.00 106.54 ? 1656 GLU B OE2   1 
ATOM   7126 N  N     . ILE B 1 440 ? 0.050   25.263  2.227   1.00 93.60  ? 1657 ILE B N     1 
ATOM   7127 C  CA    . ILE B 1 440 ? -0.373  24.872  3.562   1.00 95.50  ? 1657 ILE B CA    1 
ATOM   7128 C  C     . ILE B 1 440 ? -0.381  26.082  4.480   1.00 93.96  ? 1657 ILE B C     1 
ATOM   7129 O  O     . ILE B 1 440 ? -1.346  26.330  5.205   1.00 84.02  ? 1657 ILE B O     1 
ATOM   7130 C  CB    . ILE B 1 440 ? 0.523   23.740  4.099   1.00 93.58  ? 1657 ILE B CB    1 
ATOM   7131 C  CG1   . ILE B 1 440 ? 0.356   22.484  3.229   1.00 94.81  ? 1657 ILE B CG1   1 
ATOM   7132 C  CG2   . ILE B 1 440 ? 0.210   23.432  5.580   1.00 82.70  ? 1657 ILE B CG2   1 
ATOM   7133 C  CD1   . ILE B 1 440 ? 1.167   21.290  3.664   1.00 73.54  ? 1657 ILE B CD1   1 
ATOM   7134 N  N     . SER B 1 441 ? 0.707   26.845  4.469   1.00 105.14 ? 1658 SER B N     1 
ATOM   7135 C  CA    . SER B 1 441 ? 0.797   28.135  5.177   1.00 104.77 ? 1658 SER B CA    1 
ATOM   7136 C  C     . SER B 1 441 ? -0.484  28.955  5.041   1.00 103.16 ? 1658 SER B C     1 
ATOM   7137 O  O     . SER B 1 441 ? -1.101  29.344  6.052   1.00 101.35 ? 1658 SER B O     1 
ATOM   7138 C  CB    . SER B 1 441 ? 2.038   28.883  4.655   1.00 108.78 ? 1658 SER B CB    1 
ATOM   7139 N  N     . CYS B 1 442 ? -0.955  29.116  3.792   1.00 103.17 ? 1659 CYS B N     1 
ATOM   7140 C  CA    . CYS B 1 442 ? -2.060  30.018  3.528   1.00 100.94 ? 1659 CYS B CA    1 
ATOM   7141 C  C     . CYS B 1 442 ? -3.387  29.423  3.969   1.00 106.42 ? 1659 CYS B C     1 
ATOM   7142 O  O     . CYS B 1 442 ? -4.267  30.135  4.453   1.00 114.27 ? 1659 CYS B O     1 
ATOM   7143 C  CB    . CYS B 1 442 ? -2.122  30.324  2.042   1.00 93.67  ? 1659 CYS B CB    1 
ATOM   7144 S  SG    . CYS B 1 442 ? -3.414  31.382  1.499   1.00 84.10  ? 1659 CYS B SG    1 
ATOM   7145 N  N     . GLU B 1 443 ? -3.542  28.111  3.838   1.00 108.57 ? 1660 GLU B N     1 
ATOM   7146 C  CA    . GLU B 1 443 ? -4.727  27.435  4.352   1.00 98.44  ? 1660 GLU B CA    1 
ATOM   7147 C  C     . GLU B 1 443 ? -4.830  27.605  5.862   1.00 90.78  ? 1660 GLU B C     1 
ATOM   7148 O  O     . GLU B 1 443 ? -5.911  27.893  6.402   1.00 88.16  ? 1660 GLU B O     1 
ATOM   7149 C  CB    . GLU B 1 443 ? -4.643  25.955  3.945   1.00 89.67  ? 1660 GLU B CB    1 
ATOM   7150 C  CG    . GLU B 1 443 ? -5.902  25.158  4.166   1.00 92.14  ? 1660 GLU B CG    1 
ATOM   7151 C  CD    . GLU B 1 443 ? -5.879  23.813  3.443   1.00 96.38  ? 1660 GLU B CD    1 
ATOM   7152 O  OE1   . GLU B 1 443 ? -5.168  23.691  2.414   1.00 97.86  ? 1660 GLU B OE1   1 
ATOM   7153 O  OE2   . GLU B 1 443 ? -6.552  22.871  3.926   1.00 95.17  ? 1660 GLU B OE2   1 
ATOM   7154 N  N     . ASP B 1 444 ? -3.693  27.477  6.549   1.00 95.88  ? 1661 ASP B N     1 
ATOM   7155 C  CA    . ASP B 1 444 ? -3.658  27.669  7.992   1.00 97.47  ? 1661 ASP B CA    1 
ATOM   7156 C  C     . ASP B 1 444 ? -4.091  29.086  8.352   1.00 101.44 ? 1661 ASP B C     1 
ATOM   7157 O  O     . ASP B 1 444 ? -4.915  29.289  9.255   1.00 104.14 ? 1661 ASP B O     1 
ATOM   7158 C  CB    . ASP B 1 444 ? -2.254  27.356  8.525   1.00 100.92 ? 1661 ASP B CB    1 
ATOM   7159 C  CG    . ASP B 1 444 ? -1.842  25.874  8.318   1.00 106.65 ? 1661 ASP B CG    1 
ATOM   7160 O  OD1   . ASP B 1 444 ? -0.801  25.624  7.675   1.00 109.02 ? 1661 ASP B OD1   1 
ATOM   7161 O  OD2   . ASP B 1 444 ? -2.552  24.957  8.794   1.00 107.81 ? 1661 ASP B OD2   1 
ATOM   7162 N  N     . ARG B 1 445 ? -3.564  30.084  7.631   1.00 102.94 ? 1662 ARG B N     1 
ATOM   7163 C  CA    . ARG B 1 445 ? -3.969  31.468  7.899   1.00 100.22 ? 1662 ARG B CA    1 
ATOM   7164 C  C     . ARG B 1 445 ? -5.462  31.686  7.614   1.00 92.73  ? 1662 ARG B C     1 
ATOM   7165 O  O     . ARG B 1 445 ? -6.130  32.427  8.344   1.00 83.51  ? 1662 ARG B O     1 
ATOM   7166 C  CB    . ARG B 1 445 ? -3.108  32.458  7.096   1.00 95.50  ? 1662 ARG B CB    1 
ATOM   7167 N  N     . ILE B 1 446 ? -6.006  31.037  6.573   1.00 96.39  ? 1663 ILE B N     1 
ATOM   7168 C  CA    . ILE B 1 446 ? -7.430  31.165  6.250   1.00 93.88  ? 1663 ILE B CA    1 
ATOM   7169 C  C     . ILE B 1 446 ? -8.285  30.657  7.401   1.00 93.90  ? 1663 ILE B C     1 
ATOM   7170 O  O     . ILE B 1 446 ? -9.219  31.336  7.860   1.00 77.61  ? 1663 ILE B O     1 
ATOM   7171 C  CB    . ILE B 1 446 ? -7.758  30.420  4.939   1.00 87.98  ? 1663 ILE B CB    1 
ATOM   7172 C  CG1   . ILE B 1 446 ? -7.112  31.130  3.750   1.00 104.76 ? 1663 ILE B CG1   1 
ATOM   7173 C  CG2   . ILE B 1 446 ? -9.281  30.271  4.744   1.00 75.65  ? 1663 ILE B CG2   1 
ATOM   7174 C  CD1   . ILE B 1 446 ? -7.616  30.685  2.383   1.00 108.07 ? 1663 ILE B CD1   1 
ATOM   7175 N  N     . LYS B 1 447 ? -7.971  29.461  7.897   1.00 82.53  ? 1664 LYS B N     1 
ATOM   7176 C  CA    . LYS B 1 447 ? -8.747  28.966  9.022   1.00 100.95 ? 1664 LYS B CA    1 
ATOM   7177 C  C     . LYS B 1 447 ? -8.601  29.885  10.234  1.00 110.95 ? 1664 LYS B C     1 
ATOM   7178 O  O     . LYS B 1 447 ? -9.599  30.254  10.871  1.00 111.78 ? 1664 LYS B O     1 
ATOM   7179 C  CB    . LYS B 1 447 ? -8.362  27.537  9.385   1.00 108.00 ? 1664 LYS B CB    1 
ATOM   7180 C  CG    . LYS B 1 447 ? -9.422  26.900  10.282  1.00 105.71 ? 1664 LYS B CG    1 
ATOM   7181 C  CD    . LYS B 1 447 ? -8.860  26.671  11.661  1.00 110.18 ? 1664 LYS B CD    1 
ATOM   7182 C  CE    . LYS B 1 447 ? -9.816  25.907  12.540  1.00 113.24 ? 1664 LYS B CE    1 
ATOM   7183 N  NZ    . LYS B 1 447 ? -9.042  25.008  13.447  1.00 110.17 ? 1664 LYS B NZ    1 
ATOM   7184 N  N     . ALA B 1 448 ? -7.367  30.300  10.543  1.00 112.30 ? 1665 ALA B N     1 
ATOM   7185 C  CA    . ALA B 1 448 ? -7.136  31.104  11.744  1.00 114.68 ? 1665 ALA B CA    1 
ATOM   7186 C  C     . ALA B 1 448 ? -7.890  32.430  11.700  1.00 122.42 ? 1665 ALA B C     1 
ATOM   7187 O  O     . ALA B 1 448 ? -8.524  32.829  12.685  1.00 129.43 ? 1665 ALA B O     1 
ATOM   7188 C  CB    . ALA B 1 448 ? -5.645  31.368  11.922  1.00 106.96 ? 1665 ALA B CB    1 
ATOM   7189 N  N     . GLU B 1 449 ? -7.840  33.126  10.572  1.00 127.60 ? 1666 GLU B N     1 
ATOM   7190 C  CA    . GLU B 1 449 ? -8.458  34.427  10.452  1.00 129.58 ? 1666 GLU B CA    1 
ATOM   7191 C  C     . GLU B 1 449 ? -9.907  34.325  9.988   1.00 136.60 ? 1666 GLU B C     1 
ATOM   7192 O  O     . GLU B 1 449 ? -10.539 35.342  9.686   1.00 137.96 ? 1666 GLU B O     1 
ATOM   7193 C  CB    . GLU B 1 449 ? -7.607  35.312  9.524   1.00 126.01 ? 1666 GLU B CB    1 
ATOM   7194 C  CG    . GLU B 1 449 ? -6.178  35.597  10.099  1.00 121.65 ? 1666 GLU B CG    1 
ATOM   7195 C  CD    . GLU B 1 449 ? -5.175  36.156  9.091   1.00 121.14 ? 1666 GLU B CD    1 
ATOM   7196 O  OE1   . GLU B 1 449 ? -5.517  37.120  8.379   1.00 124.82 ? 1666 GLU B OE1   1 
ATOM   7197 O  OE2   . GLU B 1 449 ? -4.036  35.635  9.025   1.00 121.56 ? 1666 GLU B OE2   1 
ATOM   7198 N  N     . SER B 1 450 ? -10.482 33.126  9.933   1.00 145.07 ? 1667 SER B N     1 
ATOM   7199 C  CA    . SER B 1 450 ? -11.901 32.950  9.686   1.00 143.97 ? 1667 SER B CA    1 
ATOM   7200 C  C     . SER B 1 450 ? -12.690 32.520  10.915  1.00 140.99 ? 1667 SER B C     1 
ATOM   7201 O  O     . SER B 1 450 ? -13.880 32.169  10.782  1.00 147.12 ? 1667 SER B O     1 
ATOM   7202 C  CB    . SER B 1 450 ? -12.103 31.964  8.552   1.00 144.87 ? 1667 SER B CB    1 
ATOM   7203 O  OG    . SER B 1 450 ? -11.351 30.782  8.786   1.00 142.20 ? 1667 SER B OG    1 
ATOM   7204 N  N     . ALA B 1 451 ? -12.097 32.549  12.111  1.00 127.97 ? 1668 ALA B N     1 
ATOM   7205 C  CA    . ALA B 1 451 ? -12.767 32.040  13.291  1.00 114.07 ? 1668 ALA B CA    1 
ATOM   7206 C  C     . ALA B 1 451 ? -13.907 32.938  13.749  1.00 118.45 ? 1668 ALA B C     1 
ATOM   7207 O  O     . ALA B 1 451 ? -14.018 33.291  14.923  1.00 123.73 ? 1668 ALA B O     1 
ATOM   7208 C  CB    . ALA B 1 451 ? -11.791 31.861  14.420  1.00 105.45 ? 1668 ALA B CB    1 
ATOM   7209 N  N     . GLY B 1 465 ? -14.236 28.589  12.758  1.00 84.37  ? 1682 GLY B N     1 
ATOM   7210 C  CA    . GLY B 1 465 ? -13.096 28.666  11.847  1.00 89.58  ? 1682 GLY B CA    1 
ATOM   7211 C  C     . GLY B 1 465 ? -13.406 27.915  10.568  1.00 98.95  ? 1682 GLY B C     1 
ATOM   7212 O  O     . GLY B 1 465 ? -14.261 27.051  10.602  1.00 121.04 ? 1682 GLY B O     1 
ATOM   7213 N  N     . ALA B 1 466 ? -12.725 28.189  9.455   1.00 89.68  ? 1683 ALA B N     1 
ATOM   7214 C  CA    . ALA B 1 466 ? -13.082 27.601  8.162   1.00 83.99  ? 1683 ALA B CA    1 
ATOM   7215 C  C     . ALA B 1 466 ? -11.920 26.822  7.557   1.00 90.83  ? 1683 ALA B C     1 
ATOM   7216 O  O     . ALA B 1 466 ? -10.821 27.357  7.407   1.00 89.53  ? 1683 ALA B O     1 
ATOM   7217 C  CB    . ALA B 1 466 ? -13.523 28.677  7.172   1.00 79.51  ? 1683 ALA B CB    1 
ATOM   7218 N  N     . LYS B 1 467 ? -12.160 25.562  7.208   1.00 101.64 ? 1684 LYS B N     1 
ATOM   7219 C  CA    . LYS B 1 467 ? -11.172 24.733  6.537   1.00 94.43  ? 1684 LYS B CA    1 
ATOM   7220 C  C     . LYS B 1 467 ? -11.542 24.564  5.068   1.00 91.21  ? 1684 LYS B C     1 
ATOM   7221 O  O     . LYS B 1 467 ? -12.684 24.778  4.664   1.00 97.99  ? 1684 LYS B O     1 
ATOM   7222 C  CB    . LYS B 1 467 ? -11.059 23.357  7.204   1.00 84.06  ? 1684 LYS B CB    1 
ATOM   7223 N  N     . SER B 1 468 ? -10.542 24.214  4.261   1.00 88.05  ? 1685 SER B N     1 
ATOM   7224 C  CA    . SER B 1 468 ? -10.801 23.665  2.938   1.00 86.93  ? 1685 SER B CA    1 
ATOM   7225 C  C     . SER B 1 468 ? -11.636 22.404  3.076   1.00 87.53  ? 1685 SER B C     1 
ATOM   7226 O  O     . SER B 1 468 ? -11.498 21.657  4.046   1.00 84.95  ? 1685 SER B O     1 
ATOM   7227 C  CB    . SER B 1 468 ? -9.509  23.329  2.222   1.00 85.52  ? 1685 SER B CB    1 
ATOM   7228 O  OG    . SER B 1 468 ? -8.879  22.249  2.866   1.00 92.60  ? 1685 SER B OG    1 
ATOM   7229 N  N     . LEU B 1 469 ? -12.543 22.187  2.115   1.00 89.64  ? 1686 LEU B N     1 
ATOM   7230 C  CA    . LEU B 1 469 ? -13.307 20.937  2.014   1.00 79.87  ? 1686 LEU B CA    1 
ATOM   7231 C  C     . LEU B 1 469 ? -12.815 20.071  0.859   1.00 71.54  ? 1686 LEU B C     1 
ATOM   7232 O  O     . LEU B 1 469 ? -12.304 18.975  1.088   1.00 73.46  ? 1686 LEU B O     1 
ATOM   7233 C  CB    . LEU B 1 469 ? -14.804 21.241  1.867   1.00 80.61  ? 1686 LEU B CB    1 
ATOM   7234 C  CG    . LEU B 1 469 ? -15.355 22.257  2.867   1.00 79.39  ? 1686 LEU B CG    1 
ATOM   7235 C  CD1   . LEU B 1 469 ? -16.644 22.911  2.353   1.00 76.96  ? 1686 LEU B CD1   1 
ATOM   7236 C  CD2   . LEU B 1 469 ? -15.554 21.610  4.226   1.00 70.56  ? 1686 LEU B CD2   1 
ATOM   7237 N  N     . CYS B 1 470 ? -12.918 20.549  -0.383  1.00 73.49  ? 1687 CYS B N     1 
ATOM   7238 C  CA    . CYS B 1 470 ? -12.239 19.911  -1.504  1.00 82.23  ? 1687 CYS B CA    1 
ATOM   7239 C  C     . CYS B 1 470 ? -11.953 20.927  -2.603  1.00 96.00  ? 1687 CYS B C     1 
ATOM   7240 O  O     . CYS B 1 470 ? -12.553 22.012  -2.662  1.00 103.31 ? 1687 CYS B O     1 
ATOM   7241 C  CB    . CYS B 1 470 ? -13.071 18.789  -2.089  1.00 82.27  ? 1687 CYS B CB    1 
ATOM   7242 S  SG    . CYS B 1 470 ? -14.520 19.415  -2.922  1.00 77.44  ? 1687 CYS B SG    1 
ATOM   7243 N  N     . ILE B 1 471 ? -11.023 20.558  -3.480  1.00 97.76  ? 1688 ILE B N     1 
ATOM   7244 C  CA    . ILE B 1 471 ? -10.846 21.266  -4.746  1.00 92.61  ? 1688 ILE B CA    1 
ATOM   7245 C  C     . ILE B 1 471 ? -11.759 20.586  -5.758  1.00 92.65  ? 1688 ILE B C     1 
ATOM   7246 O  O     . ILE B 1 471 ? -11.401 19.521  -6.278  1.00 88.95  ? 1688 ILE B O     1 
ATOM   7247 C  CB    . ILE B 1 471 ? -9.387  21.255  -5.224  1.00 84.77  ? 1688 ILE B CB    1 
ATOM   7248 C  CG1   . ILE B 1 471 ? -8.414  21.511  -4.069  1.00 85.17  ? 1688 ILE B CG1   1 
ATOM   7249 C  CG2   . ILE B 1 471 ? -9.195  22.280  -6.317  1.00 79.04  ? 1688 ILE B CG2   1 
ATOM   7250 C  CD1   . ILE B 1 471 ? -7.056  20.834  -4.255  1.00 76.38  ? 1688 ILE B CD1   1 
ATOM   7251 N  N     . PRO B 1 472 ? -12.923 21.158  -6.077  1.00 89.52  ? 1689 PRO B N     1 
ATOM   7252 C  CA    . PRO B 1 472 ? -13.943 20.400  -6.817  1.00 78.62  ? 1689 PRO B CA    1 
ATOM   7253 C  C     . PRO B 1 472 ? -13.473 19.998  -8.211  1.00 82.62  ? 1689 PRO B C     1 
ATOM   7254 O  O     . PRO B 1 472 ? -12.797 20.765  -8.905  1.00 90.67  ? 1689 PRO B O     1 
ATOM   7255 C  CB    . PRO B 1 472 ? -15.124 21.376  -6.886  1.00 83.39  ? 1689 PRO B CB    1 
ATOM   7256 C  CG    . PRO B 1 472 ? -14.760 22.537  -5.994  1.00 86.45  ? 1689 PRO B CG    1 
ATOM   7257 C  CD    . PRO B 1 472 ? -13.278 22.582  -5.959  1.00 82.89  ? 1689 PRO B CD    1 
ATOM   7258 N  N     . PHE B 1 473 ? -13.860 18.786  -8.629  1.00 82.55  ? 1690 PHE B N     1 
ATOM   7259 C  CA    . PHE B 1 473 ? -13.571 18.356  -9.995  1.00 83.82  ? 1690 PHE B CA    1 
ATOM   7260 C  C     . PHE B 1 473 ? -14.279 19.259  -10.991 1.00 89.89  ? 1690 PHE B C     1 
ATOM   7261 O  O     . PHE B 1 473 ? -13.671 19.763  -11.941 1.00 82.89  ? 1690 PHE B O     1 
ATOM   7262 C  CB    . PHE B 1 473 ? -14.026 16.918  -10.225 1.00 86.69  ? 1690 PHE B CB    1 
ATOM   7263 C  CG    . PHE B 1 473 ? -13.282 15.895  -9.436  1.00 85.12  ? 1690 PHE B CG    1 
ATOM   7264 C  CD1   . PHE B 1 473 ? -13.676 14.565  -9.489  1.00 87.25  ? 1690 PHE B CD1   1 
ATOM   7265 C  CD2   . PHE B 1 473 ? -12.201 16.241  -8.652  1.00 84.21  ? 1690 PHE B CD2   1 
ATOM   7266 C  CE1   . PHE B 1 473 ? -13.017 13.606  -8.775  1.00 92.22  ? 1690 PHE B CE1   1 
ATOM   7267 C  CE2   . PHE B 1 473 ? -11.523 15.283  -7.930  1.00 89.41  ? 1690 PHE B CE2   1 
ATOM   7268 C  CZ    . PHE B 1 473 ? -11.932 13.960  -7.990  1.00 96.39  ? 1690 PHE B CZ    1 
ATOM   7269 N  N     . GLU B 1 474 ? -15.574 19.477  -10.777 1.00 97.75  ? 1691 GLU B N     1 
ATOM   7270 C  CA    . GLU B 1 474 ? -16.332 20.456  -11.542 1.00 104.04 ? 1691 GLU B CA    1 
ATOM   7271 C  C     . GLU B 1 474 ? -15.959 21.833  -10.994 1.00 96.92  ? 1691 GLU B C     1 
ATOM   7272 O  O     . GLU B 1 474 ? -16.420 22.231  -9.920  1.00 101.63 ? 1691 GLU B O     1 
ATOM   7273 C  CB    . GLU B 1 474 ? -17.825 20.162  -11.430 1.00 114.97 ? 1691 GLU B CB    1 
ATOM   7274 C  CG    . GLU B 1 474 ? -18.729 21.079  -12.259 1.00 132.68 ? 1691 GLU B CG    1 
ATOM   7275 C  CD    . GLU B 1 474 ? -18.259 21.239  -13.701 1.00 144.32 ? 1691 GLU B CD    1 
ATOM   7276 O  OE1   . GLU B 1 474 ? -17.784 20.239  -14.292 1.00 153.57 ? 1691 GLU B OE1   1 
ATOM   7277 O  OE2   . GLU B 1 474 ? -18.366 22.365  -14.241 1.00 139.12 ? 1691 GLU B OE2   1 
ATOM   7278 N  N     . GLN B 1 475 ? -15.090 22.565  -11.724 1.00 83.38  ? 1692 GLN B N     1 
ATOM   7279 C  CA    . GLN B 1 475 ? -14.689 23.857  -11.162 1.00 83.88  ? 1692 GLN B CA    1 
ATOM   7280 C  C     . GLN B 1 475 ? -15.702 24.958  -11.497 1.00 84.32  ? 1692 GLN B C     1 
ATOM   7281 O  O     . GLN B 1 475 ? -16.305 24.939  -12.571 1.00 89.14  ? 1692 GLN B O     1 
ATOM   7282 C  CB    . GLN B 1 475 ? -13.309 24.272  -11.689 1.00 89.11  ? 1692 GLN B CB    1 
ATOM   7283 C  CG    . GLN B 1 475 ? -12.095 23.650  -10.966 1.00 92.87  ? 1692 GLN B CG    1 
ATOM   7284 C  CD    . GLN B 1 475 ? -11.693 24.384  -9.689  1.00 91.79  ? 1692 GLN B CD    1 
ATOM   7285 O  OE1   . GLN B 1 475 ? -11.273 25.538  -9.719  1.00 83.61  ? 1692 GLN B OE1   1 
ATOM   7286 N  NE2   . GLN B 1 475 ? -11.830 23.704  -8.555  1.00 99.56  ? 1692 GLN B NE2   1 
ATOM   7287 N  N     . PRO B 1 476 ? -15.953 25.907  -10.576 1.00 88.82  ? 1693 PRO B N     1 
ATOM   7288 C  CA    . PRO B 1 476 ? -16.747 27.105  -10.924 1.00 94.89  ? 1693 PRO B CA    1 
ATOM   7289 C  C     . PRO B 1 476 ? -15.913 28.134  -11.671 1.00 112.73 ? 1693 PRO B C     1 
ATOM   7290 O  O     . PRO B 1 476 ? -15.245 28.935  -11.012 1.00 129.69 ? 1693 PRO B O     1 
ATOM   7291 C  CB    . PRO B 1 476 ? -17.167 27.657  -9.561  1.00 90.74  ? 1693 PRO B CB    1 
ATOM   7292 C  CG    . PRO B 1 476 ? -16.063 27.247  -8.649  1.00 89.82  ? 1693 PRO B CG    1 
ATOM   7293 C  CD    . PRO B 1 476 ? -15.605 25.873  -9.144  1.00 88.16  ? 1693 PRO B CD    1 
ATOM   7294 N  N     . ALA B 1 477 ? -15.936 28.137  -13.008 1.00 115.16 ? 1694 ALA B N     1 
ATOM   7295 C  CA    . ALA B 1 477 ? -15.119 29.013  -13.862 1.00 115.36 ? 1694 ALA B CA    1 
ATOM   7296 C  C     . ALA B 1 477 ? -13.640 28.599  -13.865 1.00 115.29 ? 1694 ALA B C     1 
ATOM   7297 O  O     . ALA B 1 477 ? -13.170 27.944  -12.926 1.00 113.58 ? 1694 ALA B O     1 
ATOM   7298 C  CB    . ALA B 1 477 ? -15.258 30.483  -13.447 1.00 104.87 ? 1694 ALA B CB    1 
ATOM   7299 N  N     . LYS B 1 478 ? -12.896 28.992  -14.905 1.00 114.04 ? 1695 LYS B N     1 
ATOM   7300 C  CA    . LYS B 1 478 ? -11.490 28.618  -15.075 1.00 104.19 ? 1695 LYS B CA    1 
ATOM   7301 C  C     . LYS B 1 478 ? -10.553 29.740  -14.631 1.00 108.39 ? 1695 LYS B C     1 
ATOM   7302 O  O     . LYS B 1 478 ? -10.762 30.913  -14.962 1.00 106.95 ? 1695 LYS B O     1 
ATOM   7303 C  CB    . LYS B 1 478 ? -11.182 28.240  -16.530 1.00 86.84  ? 1695 LYS B CB    1 
ATOM   7304 N  N     . ILE B 1 479 ? -9.519  29.361  -13.881 1.00 101.79 ? 1696 ILE B N     1 
ATOM   7305 C  CA    . ILE B 1 479 ? -8.611  30.324  -13.274 1.00 99.44  ? 1696 ILE B CA    1 
ATOM   7306 C  C     . ILE B 1 479 ? -7.710  30.953  -14.338 1.00 108.25 ? 1696 ILE B C     1 
ATOM   7307 O  O     . ILE B 1 479 ? -7.032  30.249  -15.096 1.00 116.82 ? 1696 ILE B O     1 
ATOM   7308 C  CB    . ILE B 1 479 ? -7.798  29.631  -12.168 1.00 85.88  ? 1696 ILE B CB    1 
ATOM   7309 N  N     . ASP B 1 480 ? -7.719  32.288  -14.422 1.00 105.62 ? 1697 ASP B N     1 
ATOM   7310 C  CA    . ASP B 1 480 ? -6.871  33.021  -15.358 1.00 115.28 ? 1697 ASP B CA    1 
ATOM   7311 C  C     . ASP B 1 480 ? -5.676  33.607  -14.610 1.00 114.35 ? 1697 ASP B C     1 
ATOM   7312 O  O     . ASP B 1 480 ? -5.812  34.655  -13.962 1.00 113.26 ? 1697 ASP B O     1 
ATOM   7313 C  CB    . ASP B 1 480 ? -7.658  34.131  -16.063 1.00 120.63 ? 1697 ASP B CB    1 
ATOM   7314 N  N     . PRO B 1 481 ? -4.489  32.994  -14.683 1.00 113.47 ? 1698 PRO B N     1 
ATOM   7315 C  CA    . PRO B 1 481 ? -3.382  33.404  -13.798 1.00 105.79 ? 1698 PRO B CA    1 
ATOM   7316 C  C     . PRO B 1 481 ? -2.923  34.832  -14.000 1.00 124.38 ? 1698 PRO B C     1 
ATOM   7317 O  O     . PRO B 1 481 ? -2.176  35.349  -13.156 1.00 132.02 ? 1698 PRO B O     1 
ATOM   7318 C  CB    . PRO B 1 481 ? -2.256  32.430  -14.159 1.00 89.37  ? 1698 PRO B CB    1 
ATOM   7319 C  CG    . PRO B 1 481 ? -2.916  31.316  -14.879 1.00 93.67  ? 1698 PRO B CG    1 
ATOM   7320 C  CD    . PRO B 1 481 ? -4.098  31.891  -15.573 1.00 107.61 ? 1698 PRO B CD    1 
ATOM   7321 N  N     . LYS B 1 482 ? -3.307  35.474  -15.101 1.00 119.58 ? 1699 LYS B N     1 
ATOM   7322 C  CA    . LYS B 1 482 ? -2.949  36.868  -15.287 1.00 120.26 ? 1699 LYS B CA    1 
ATOM   7323 C  C     . LYS B 1 482 ? -3.567  37.764  -14.220 1.00 132.74 ? 1699 LYS B C     1 
ATOM   7324 O  O     . LYS B 1 482 ? -3.130  38.913  -14.065 1.00 144.70 ? 1699 LYS B O     1 
ATOM   7325 C  CB    . LYS B 1 482 ? -3.360  37.328  -16.690 1.00 115.49 ? 1699 LYS B CB    1 
ATOM   7326 N  N     . VAL B 1 483 ? -4.596  37.294  -13.512 1.00 132.11 ? 1700 VAL B N     1 
ATOM   7327 C  CA    . VAL B 1 483 ? -5.283  38.160  -12.562 1.00 128.87 ? 1700 VAL B CA    1 
ATOM   7328 C  C     . VAL B 1 483 ? -5.574  37.433  -11.249 1.00 126.07 ? 1700 VAL B C     1 
ATOM   7329 O  O     . VAL B 1 483 ? -5.321  37.978  -10.169 1.00 131.21 ? 1700 VAL B O     1 
ATOM   7330 C  CB    . VAL B 1 483 ? -6.567  38.758  -13.173 1.00 125.63 ? 1700 VAL B CB    1 
ATOM   7331 C  CG1   . VAL B 1 483 ? -7.485  37.667  -13.729 1.00 125.50 ? 1700 VAL B CG1   1 
ATOM   7332 C  CG2   . VAL B 1 483 ? -7.272  39.614  -12.143 1.00 122.86 ? 1700 VAL B CG2   1 
ATOM   7333 N  N     . ASP B 1 484 ? -6.128  36.220  -11.316 1.00 114.56 ? 1701 ASP B N     1 
ATOM   7334 C  CA    . ASP B 1 484 ? -6.632  35.549  -10.115 1.00 110.72 ? 1701 ASP B CA    1 
ATOM   7335 C  C     . ASP B 1 484 ? -5.528  35.315  -9.089  1.00 105.12 ? 1701 ASP B C     1 
ATOM   7336 O  O     . ASP B 1 484 ? -4.532  34.646  -9.375  1.00 104.02 ? 1701 ASP B O     1 
ATOM   7337 C  CB    . ASP B 1 484 ? -7.249  34.205  -10.492 1.00 112.76 ? 1701 ASP B CB    1 
ATOM   7338 C  CG    . ASP B 1 484 ? -8.398  34.351  -11.428 1.00 112.95 ? 1701 ASP B CG    1 
ATOM   7339 O  OD1   . ASP B 1 484 ? -9.023  35.430  -11.406 1.00 114.72 ? 1701 ASP B OD1   1 
ATOM   7340 O  OD2   . ASP B 1 484 ? -8.664  33.400  -12.193 1.00 107.68 ? 1701 ASP B OD2   1 
ATOM   7341 N  N     . LYS B 1 485 ? -5.761  35.787  -7.864  1.00 100.90 ? 1702 LYS B N     1 
ATOM   7342 C  CA    . LYS B 1 485 ? -4.862  35.589  -6.737  1.00 95.84  ? 1702 LYS B CA    1 
ATOM   7343 C  C     . LYS B 1 485 ? -5.620  34.942  -5.593  1.00 98.09  ? 1702 LYS B C     1 
ATOM   7344 O  O     . LYS B 1 485 ? -6.822  35.172  -5.421  1.00 97.16  ? 1702 LYS B O     1 
ATOM   7345 C  CB    . LYS B 1 485 ? -4.279  36.915  -6.208  1.00 89.83  ? 1702 LYS B CB    1 
ATOM   7346 C  CG    . LYS B 1 485 ? -3.683  37.865  -7.239  1.00 92.25  ? 1702 LYS B CG    1 
ATOM   7347 C  CD    . LYS B 1 485 ? -2.181  37.689  -7.314  1.00 93.05  ? 1702 LYS B CD    1 
ATOM   7348 C  CE    . LYS B 1 485 ? -1.579  38.826  -8.048  1.00 95.83  ? 1702 LYS B CE    1 
ATOM   7349 N  NZ    . LYS B 1 485 ? -1.926  40.067  -7.327  1.00 104.62 ? 1702 LYS B NZ    1 
ATOM   7350 N  N     . CYS B 1 486 ? -4.897  34.184  -4.776  1.00 97.13  ? 1703 CYS B N     1 
ATOM   7351 C  CA    . CYS B 1 486 ? -5.529  33.507  -3.659  1.00 97.65  ? 1703 CYS B CA    1 
ATOM   7352 C  C     . CYS B 1 486 ? -6.233  34.513  -2.760  1.00 96.93  ? 1703 CYS B C     1 
ATOM   7353 O  O     . CYS B 1 486 ? -5.690  35.566  -2.429  1.00 98.19  ? 1703 CYS B O     1 
ATOM   7354 C  CB    . CYS B 1 486 ? -4.507  32.712  -2.857  1.00 100.28 ? 1703 CYS B CB    1 
ATOM   7355 S  SG    . CYS B 1 486 ? -5.103  32.221  -1.224  1.00 102.79 ? 1703 CYS B SG    1 
ATOM   7356 N  N     . VAL B 1 487 ? -7.439  34.144  -2.329  1.00 98.01  ? 1704 VAL B N     1 
ATOM   7357 C  CA    . VAL B 1 487 ? -8.358  35.058  -1.681  1.00 90.26  ? 1704 VAL B CA    1 
ATOM   7358 C  C     . VAL B 1 487 ? -7.816  35.572  -0.349  1.00 91.19  ? 1704 VAL B C     1 
ATOM   7359 O  O     . VAL B 1 487 ? -8.230  36.646  0.109   1.00 86.00  ? 1704 VAL B O     1 
ATOM   7360 C  CB    . VAL B 1 487 ? -9.730  34.342  -1.533  1.00 88.67  ? 1704 VAL B CB    1 
ATOM   7361 C  CG1   . VAL B 1 487 ? -9.565  32.950  -0.940  1.00 85.82  ? 1704 VAL B CG1   1 
ATOM   7362 C  CG2   . VAL B 1 487 ? -10.729 35.159  -0.725  1.00 91.24  ? 1704 VAL B CG2   1 
ATOM   7363 N  N     . HIS B 1 488 ? -6.838  34.890  0.252   1.00 97.06  ? 1705 HIS B N     1 
ATOM   7364 C  CA    . HIS B 1 488 ? -6.335  35.426  1.513   1.00 108.74 ? 1705 HIS B CA    1 
ATOM   7365 C  C     . HIS B 1 488 ? -5.389  36.588  1.240   1.00 114.73 ? 1705 HIS B C     1 
ATOM   7366 O  O     . HIS B 1 488 ? -4.436  36.444  0.460   1.00 108.31 ? 1705 HIS B O     1 
ATOM   7367 C  CB    . HIS B 1 488 ? -5.636  34.366  2.358   1.00 105.36 ? 1705 HIS B CB    1 
ATOM   7368 C  CG    . HIS B 1 488 ? -5.235  34.869  3.712   1.00 105.16 ? 1705 HIS B CG    1 
ATOM   7369 N  ND1   . HIS B 1 488 ? -6.060  35.658  4.486   1.00 103.72 ? 1705 HIS B ND1   1 
ATOM   7370 C  CD2   . HIS B 1 488 ? -4.085  34.731  4.413   1.00 107.55 ? 1705 HIS B CD2   1 
ATOM   7371 C  CE1   . HIS B 1 488 ? -5.444  35.965  5.613   1.00 104.96 ? 1705 HIS B CE1   1 
ATOM   7372 N  NE2   . HIS B 1 488 ? -4.243  35.417  5.594   1.00 107.21 ? 1705 HIS B NE2   1 
ATOM   7373 N  N     . PRO B 1 489 ? -5.626  37.745  1.856   1.00 116.69 ? 1706 PRO B N     1 
ATOM   7374 C  CA    . PRO B 1 489 ? -4.816  38.925  1.539   1.00 113.23 ? 1706 PRO B CA    1 
ATOM   7375 C  C     . PRO B 1 489 ? -3.350  38.822  1.954   1.00 118.89 ? 1706 PRO B C     1 
ATOM   7376 O  O     . PRO B 1 489 ? -2.548  39.631  1.480   1.00 134.44 ? 1706 PRO B O     1 
ATOM   7377 C  CB    . PRO B 1 489 ? -5.534  40.043  2.295   1.00 105.54 ? 1706 PRO B CB    1 
ATOM   7378 C  CG    . PRO B 1 489 ? -6.909  39.579  2.449   1.00 111.03 ? 1706 PRO B CG    1 
ATOM   7379 C  CD    . PRO B 1 489 ? -6.818  38.098  2.646   1.00 112.10 ? 1706 PRO B CD    1 
ATOM   7380 N  N     . ALA B 1 490 ? -2.977  37.893  2.832   1.00 114.79 ? 1707 ALA B N     1 
ATOM   7381 C  CA    . ALA B 1 490 ? -1.583  37.790  3.253   1.00 107.84 ? 1707 ALA B CA    1 
ATOM   7382 C  C     . ALA B 1 490 ? -0.734  36.988  2.273   1.00 118.00 ? 1707 ALA B C     1 
ATOM   7383 O  O     . ALA B 1 490 ? 0.493   37.182  2.223   1.00 146.40 ? 1707 ALA B O     1 
ATOM   7384 C  CB    . ALA B 1 490 ? -1.482  37.214  4.672   1.00 104.51 ? 1707 ALA B CB    1 
ATOM   7385 N  N     . CYS B 1 491 ? -1.298  35.984  1.587   1.00 131.99 ? 1708 CYS B N     1 
ATOM   7386 C  CA    . CYS B 1 491 ? -0.588  35.334  0.478   1.00 127.25 ? 1708 CYS B CA    1 
ATOM   7387 C  C     . CYS B 1 491 ? -1.017  36.017  -0.810  1.00 135.46 ? 1708 CYS B C     1 
ATOM   7388 O  O     . CYS B 1 491 ? -2.204  36.182  -1.068  1.00 138.62 ? 1708 CYS B O     1 
ATOM   7389 C  CB    . CYS B 1 491 ? -0.840  33.801  0.432   1.00 114.20 ? 1708 CYS B CB    1 
ATOM   7390 S  SG    . CYS B 1 491 ? -2.167  33.308  -0.627  1.00 111.01 ? 1708 CYS B SG    1 
ATOM   7391 N  N     . GLY B 1 492 ? -0.034  36.370  -1.622  1.00 91.36  ? 1709 GLY B N     1 
ATOM   7392 C  CA    . GLY B 1 492 ? -0.284  37.067  -2.871  1.00 92.49  ? 1709 GLY B CA    1 
ATOM   7393 C  C     . GLY B 1 492 ? -0.013  36.154  -4.038  1.00 100.31 ? 1709 GLY B C     1 
ATOM   7394 O  O     . GLY B 1 492 ? 0.173   36.581  -5.180  1.00 105.05 ? 1709 GLY B O     1 
ATOM   7395 N  N     . ARG B 1 493 ? 0.056   34.869  -3.720  1.00 100.50 ? 1710 ARG B N     1 
ATOM   7396 C  CA    . ARG B 1 493 ? 0.313   33.869  -4.740  1.00 103.63 ? 1710 ARG B CA    1 
ATOM   7397 C  C     . ARG B 1 493 ? -0.785  33.906  -5.797  1.00 103.11 ? 1710 ARG B C     1 
ATOM   7398 O  O     . ARG B 1 493 ? -1.950  34.173  -5.497  1.00 102.01 ? 1710 ARG B O     1 
ATOM   7399 C  CB    . ARG B 1 493 ? 0.389   32.496  -4.086  1.00 97.55  ? 1710 ARG B CB    1 
ATOM   7400 C  CG    . ARG B 1 493 ? 1.634   32.281  -3.257  1.00 104.34 ? 1710 ARG B CG    1 
ATOM   7401 C  CD    . ARG B 1 493 ? 1.283   31.856  -1.829  1.00 100.27 ? 1710 ARG B CD    1 
ATOM   7402 N  NE    . ARG B 1 493 ? 2.482   31.460  -1.092  1.00 104.13 ? 1710 ARG B NE    1 
ATOM   7403 C  CZ    . ARG B 1 493 ? 2.583   31.369  0.234   1.00 100.04 ? 1710 ARG B CZ    1 
ATOM   7404 N  NH1   . ARG B 1 493 ? 1.546   31.646  1.029   1.00 88.11  ? 1710 ARG B NH1   1 
ATOM   7405 N  NH2   . ARG B 1 493 ? 3.744   31.001  0.766   1.00 96.98  ? 1710 ARG B NH2   1 
ATOM   7406 N  N     . VAL B 1 494 ? -0.408  33.696  -7.058  1.00 101.00 ? 1711 VAL B N     1 
ATOM   7407 C  CA    . VAL B 1 494 ? -1.438  33.508  -8.065  1.00 103.18 ? 1711 VAL B CA    1 
ATOM   7408 C  C     . VAL B 1 494 ? -2.284  32.317  -7.642  1.00 109.00 ? 1711 VAL B C     1 
ATOM   7409 O  O     . VAL B 1 494 ? -1.772  31.327  -7.106  1.00 113.05 ? 1711 VAL B O     1 
ATOM   7410 C  CB    . VAL B 1 494 ? -0.823  33.296  -9.458  1.00 102.12 ? 1711 VAL B CB    1 
ATOM   7411 N  N     . ALA B 1 495 ? -3.591  32.408  -7.858  1.00 102.85 ? 1712 ALA B N     1 
ATOM   7412 C  CA    . ALA B 1 495 ? -4.461  31.338  -7.404  1.00 93.70  ? 1712 ALA B CA    1 
ATOM   7413 C  C     . ALA B 1 495 ? -4.170  30.092  -8.226  1.00 97.07  ? 1712 ALA B C     1 
ATOM   7414 O  O     . ALA B 1 495 ? -3.989  30.160  -9.446  1.00 80.14  ? 1712 ALA B O     1 
ATOM   7415 C  CB    . ALA B 1 495 ? -5.928  31.753  -7.511  1.00 90.26  ? 1712 ALA B CB    1 
ATOM   7416 N  N     . LYS B 1 496 ? -4.030  28.961  -7.548  1.00 100.29 ? 1713 LYS B N     1 
ATOM   7417 C  CA    . LYS B 1 496 ? -3.851  27.726  -8.288  1.00 96.38  ? 1713 LYS B CA    1 
ATOM   7418 C  C     . LYS B 1 496 ? -5.174  27.213  -8.808  1.00 99.43  ? 1713 LYS B C     1 
ATOM   7419 O  O     . LYS B 1 496 ? -5.217  26.623  -9.892  1.00 98.30  ? 1713 LYS B O     1 
ATOM   7420 C  CB    . LYS B 1 496 ? -3.178  26.668  -7.417  1.00 91.14  ? 1713 LYS B CB    1 
ATOM   7421 N  N     . PHE B 1 497 ? -6.259  27.449  -8.075  1.00 107.36 ? 1714 PHE B N     1 
ATOM   7422 C  CA    . PHE B 1 497 ? -7.533  26.877  -8.506  1.00 98.60  ? 1714 PHE B CA    1 
ATOM   7423 C  C     . PHE B 1 497 ? -8.635  27.422  -7.610  1.00 94.01  ? 1714 PHE B C     1 
ATOM   7424 O  O     . PHE B 1 497 ? -8.362  28.101  -6.622  1.00 101.18 ? 1714 PHE B O     1 
ATOM   7425 C  CB    . PHE B 1 497 ? -7.459  25.356  -8.434  1.00 91.68  ? 1714 PHE B CB    1 
ATOM   7426 C  CG    . PHE B 1 497 ? -6.719  24.868  -7.232  1.00 93.15  ? 1714 PHE B CG    1 
ATOM   7427 C  CD1   . PHE B 1 497 ? -7.106  25.291  -5.975  1.00 95.32  ? 1714 PHE B CD1   1 
ATOM   7428 C  CD2   . PHE B 1 497 ? -5.618  24.026  -7.357  1.00 85.23  ? 1714 PHE B CD2   1 
ATOM   7429 C  CE1   . PHE B 1 497 ? -6.425  24.890  -4.839  1.00 96.41  ? 1714 PHE B CE1   1 
ATOM   7430 C  CE2   . PHE B 1 497 ? -4.931  23.606  -6.243  1.00 80.87  ? 1714 PHE B CE2   1 
ATOM   7431 C  CZ    . PHE B 1 497 ? -5.352  24.046  -4.965  1.00 91.06  ? 1714 PHE B CZ    1 
ATOM   7432 N  N     . TYR B 1 498 ? -9.881  27.087  -7.926  1.00 74.25  ? 1715 TYR B N     1 
ATOM   7433 C  CA    . TYR B 1 498 ? -10.982 27.350  -7.003  1.00 73.64  ? 1715 TYR B CA    1 
ATOM   7434 C  C     . TYR B 1 498 ? -11.162 26.168  -6.068  1.00 75.01  ? 1715 TYR B C     1 
ATOM   7435 O  O     . TYR B 1 498 ? -11.160 25.025  -6.529  1.00 73.25  ? 1715 TYR B O     1 
ATOM   7436 C  CB    . TYR B 1 498 ? -12.284 27.585  -7.760  1.00 79.87  ? 1715 TYR B CB    1 
ATOM   7437 C  CG    . TYR B 1 498 ? -12.492 28.980  -8.248  1.00 74.82  ? 1715 TYR B CG    1 
ATOM   7438 C  CD1   . TYR B 1 498 ? -12.927 29.971  -7.382  1.00 85.83  ? 1715 TYR B CD1   1 
ATOM   7439 C  CD2   . TYR B 1 498 ? -12.269 29.313  -9.582  1.00 75.00  ? 1715 TYR B CD2   1 
ATOM   7440 C  CE1   . TYR B 1 498 ? -13.136 31.279  -7.823  1.00 90.27  ? 1715 TYR B CE1   1 
ATOM   7441 C  CE2   . TYR B 1 498 ? -12.462 30.626  -10.037 1.00 80.51  ? 1715 TYR B CE2   1 
ATOM   7442 C  CZ    . TYR B 1 498 ? -12.905 31.597  -9.147  1.00 89.51  ? 1715 TYR B CZ    1 
ATOM   7443 O  OH    . TYR B 1 498 ? -13.110 32.890  -9.575  1.00 102.64 ? 1715 TYR B OH    1 
ATOM   7444 N  N     . THR B 1 499 ? -11.289 26.429  -4.764  1.00 78.11  ? 1716 THR B N     1 
ATOM   7445 C  CA    . THR B 1 499 ? -11.685 25.375  -3.836  1.00 94.35  ? 1716 THR B CA    1 
ATOM   7446 C  C     . THR B 1 499 ? -12.847 25.818  -2.961  1.00 95.37  ? 1716 THR B C     1 
ATOM   7447 O  O     . THR B 1 499 ? -13.140 27.010  -2.798  1.00 98.54  ? 1716 THR B O     1 
ATOM   7448 C  CB    . THR B 1 499 ? -10.566 24.868  -2.912  1.00 102.54 ? 1716 THR B CB    1 
ATOM   7449 O  OG1   . THR B 1 499 ? -10.528 25.659  -1.720  1.00 112.09 ? 1716 THR B OG1   1 
ATOM   7450 C  CG2   . THR B 1 499 ? -9.278  24.911  -3.579  1.00 103.09 ? 1716 THR B CG2   1 
ATOM   7451 N  N     . LEU B 1 500 ? -13.439 24.806  -2.336  1.00 82.19  ? 1717 LEU B N     1 
ATOM   7452 C  CA    . LEU B 1 500 ? -14.595 24.939  -1.482  1.00 81.85  ? 1717 LEU B CA    1 
ATOM   7453 C  C     . LEU B 1 500 ? -14.154 24.928  -0.028  1.00 80.11  ? 1717 LEU B C     1 
ATOM   7454 O  O     . LEU B 1 500 ? -13.429 24.022  0.399   1.00 80.01  ? 1717 LEU B O     1 
ATOM   7455 C  CB    . LEU B 1 500 ? -15.529 23.770  -1.768  1.00 85.93  ? 1717 LEU B CB    1 
ATOM   7456 C  CG    . LEU B 1 500 ? -17.027 23.956  -1.639  1.00 81.53  ? 1717 LEU B CG    1 
ATOM   7457 C  CD1   . LEU B 1 500 ? -17.541 25.123  -2.498  1.00 78.50  ? 1717 LEU B CD1   1 
ATOM   7458 C  CD2   . LEU B 1 500 ? -17.587 22.658  -2.099  1.00 78.93  ? 1717 LEU B CD2   1 
ATOM   7459 N  N     . PHE B 1 501 ? -14.575 25.949  0.720   1.00 85.14  ? 1718 PHE B N     1 
ATOM   7460 C  CA    . PHE B 1 501 ? -14.299 26.061  2.145   1.00 90.40  ? 1718 PHE B CA    1 
ATOM   7461 C  C     . PHE B 1 501 ? -15.612 26.120  2.907   1.00 85.74  ? 1718 PHE B C     1 
ATOM   7462 O  O     . PHE B 1 501 ? -16.645 26.522  2.361   1.00 86.75  ? 1718 PHE B O     1 
ATOM   7463 C  CB    . PHE B 1 501 ? -13.474 27.311  2.519   1.00 92.30  ? 1718 PHE B CB    1 
ATOM   7464 C  CG    . PHE B 1 501 ? -12.234 27.490  1.725   1.00 90.72  ? 1718 PHE B CG    1 
ATOM   7465 C  CD1   . PHE B 1 501 ? -12.300 27.970  0.433   1.00 94.50  ? 1718 PHE B CD1   1 
ATOM   7466 C  CD2   . PHE B 1 501 ? -10.999 27.191  2.273   1.00 99.15  ? 1718 PHE B CD2   1 
ATOM   7467 C  CE1   . PHE B 1 501 ? -11.157 28.152  -0.308  1.00 104.05 ? 1718 PHE B CE1   1 
ATOM   7468 C  CE2   . PHE B 1 501 ? -9.850  27.357  1.540   1.00 103.28 ? 1718 PHE B CE2   1 
ATOM   7469 C  CZ    . PHE B 1 501 ? -9.923  27.842  0.245   1.00 109.26 ? 1718 PHE B CZ    1 
ATOM   7470 N  N     . GLY B 1 502 ? -15.558 25.699  4.165   1.00 81.62  ? 1719 GLY B N     1 
ATOM   7471 C  CA    . GLY B 1 502 ? -16.696 25.806  5.053   1.00 84.06  ? 1719 GLY B CA    1 
ATOM   7472 C  C     . GLY B 1 502 ? -16.285 25.470  6.468   1.00 92.72  ? 1719 GLY B C     1 
ATOM   7473 O  O     . GLY B 1 502 ? -15.143 25.083  6.731   1.00 88.25  ? 1719 GLY B O     1 
ATOM   7474 N  N     . ARG B 1 503 ? -17.225 25.682  7.391   1.00 107.70 ? 1720 ARG B N     1 
ATOM   7475 C  CA    . ARG B 1 503 ? -17.113 25.173  8.756   1.00 111.27 ? 1720 ARG B CA    1 
ATOM   7476 C  C     . ARG B 1 503 ? -17.577 23.714  8.776   1.00 123.17 ? 1720 ARG B C     1 
ATOM   7477 O  O     . ARG B 1 503 ? -18.520 23.348  8.072   1.00 132.02 ? 1720 ARG B O     1 
ATOM   7478 C  CB    . ARG B 1 503 ? -17.945 26.029  9.717   1.00 100.75 ? 1720 ARG B CB    1 
ATOM   7479 C  CG    . ARG B 1 503 ? -17.654 27.517  9.595   1.00 97.34  ? 1720 ARG B CG    1 
ATOM   7480 C  CD    . ARG B 1 503 ? -17.130 28.117  10.903  1.00 97.91  ? 1720 ARG B CD    1 
ATOM   7481 N  NE    . ARG B 1 503 ? -17.633 29.465  11.101  1.00 105.13 ? 1720 ARG B NE    1 
ATOM   7482 C  CZ    . ARG B 1 503 ? -17.903 29.989  12.287  1.00 107.40 ? 1720 ARG B CZ    1 
ATOM   7483 N  NH1   . ARG B 1 503 ? -17.708 29.276  13.396  1.00 110.00 ? 1720 ARG B NH1   1 
ATOM   7484 N  NH2   . ARG B 1 503 ? -18.383 31.223  12.352  1.00 100.47 ? 1720 ARG B NH2   1 
ATOM   7485 N  N     . SER B 1 504 ? -16.874 22.851  9.506   1.00 122.89 ? 1721 SER B N     1 
ATOM   7486 C  CA    . SER B 1 504 ? -17.160 21.435  9.329   1.00 124.56 ? 1721 SER B CA    1 
ATOM   7487 C  C     . SER B 1 504 ? -16.886 20.636  10.599  1.00 124.82 ? 1721 SER B C     1 
ATOM   7488 O  O     . SER B 1 504 ? -16.132 21.060  11.479  1.00 116.37 ? 1721 SER B O     1 
ATOM   7489 C  CB    . SER B 1 504 ? -16.360 20.864  8.162   1.00 130.03 ? 1721 SER B CB    1 
ATOM   7490 O  OG    . SER B 1 504 ? -14.970 20.934  8.447   1.00 132.14 ? 1721 SER B OG    1 
ATOM   7491 N  N     . TYR B 1 505 ? -17.453 19.415  10.622  1.00 121.57 ? 1722 TYR B N     1 
ATOM   7492 C  CA    . TYR B 1 505 ? -17.227 18.397  11.651  1.00 121.12 ? 1722 TYR B CA    1 
ATOM   7493 C  C     . TYR B 1 505 ? -15.927 17.664  11.362  1.00 126.71 ? 1722 TYR B C     1 
ATOM   7494 O  O     . TYR B 1 505 ? -15.634 17.329  10.209  1.00 128.28 ? 1722 TYR B O     1 
ATOM   7495 C  CB    . TYR B 1 505 ? -18.338 17.328  11.668  1.00 122.91 ? 1722 TYR B CB    1 
ATOM   7496 C  CG    . TYR B 1 505 ? -19.739 17.781  11.983  1.00 126.43 ? 1722 TYR B CG    1 
ATOM   7497 C  CD1   . TYR B 1 505 ? -20.381 17.354  13.144  1.00 128.61 ? 1722 TYR B CD1   1 
ATOM   7498 C  CD2   . TYR B 1 505 ? -20.441 18.600  11.107  1.00 125.58 ? 1722 TYR B CD2   1 
ATOM   7499 C  CE1   . TYR B 1 505 ? -21.679 17.761  13.438  1.00 126.77 ? 1722 TYR B CE1   1 
ATOM   7500 C  CE2   . TYR B 1 505 ? -21.733 19.013  11.389  1.00 123.94 ? 1722 TYR B CE2   1 
ATOM   7501 C  CZ    . TYR B 1 505 ? -22.346 18.594  12.554  1.00 122.86 ? 1722 TYR B CZ    1 
ATOM   7502 O  OH    . TYR B 1 505 ? -23.626 19.014  12.826  1.00 117.03 ? 1722 TYR B OH    1 
ATOM   7503 O  OXT   . TYR B 1 505 ? -15.162 17.338  12.270  1.00 132.37 ? 1722 TYR B OXT   1 
HETATM 7504 O  "O4'" . HFG C 2 .   ? -19.623 -17.875 25.085  1.00 78.92  ? 1801 HFG A "O4'" 1 
HETATM 7505 C  C21   . HFG C 2 .   ? -20.116 -18.699 25.826  1.00 83.56  ? 1801 HFG A C21   1 
HETATM 7506 C  "C3'" . HFG C 2 .   ? -21.606 -18.919 25.906  1.00 80.35  ? 1801 HFG A "C3'" 1 
HETATM 7507 C  "C2'" . HFG C 2 .   ? -22.384 -18.463 24.665  1.00 78.30  ? 1801 HFG A "C2'" 1 
HETATM 7508 N  "N1'" . HFG C 2 .   ? -22.292 -17.009 24.470  1.00 79.62  ? 1801 HFG A "N1'" 1 
HETATM 7509 C  "C6'" . HFG C 2 .   ? -23.211 -16.587 23.404  1.00 76.81  ? 1801 HFG A "C6'" 1 
HETATM 7510 C  "C5'" . HFG C 2 .   ? -22.898 -17.271 22.069  1.00 71.62  ? 1801 HFG A "C5'" 1 
HETATM 7511 C  "C4'" . HFG C 2 .   ? -22.882 -18.790 22.236  1.00 64.98  ? 1801 HFG A "C4'" 1 
HETATM 7512 C  C39   . HFG C 2 .   ? -21.954 -19.157 23.378  1.00 67.77  ? 1801 HFG A C39   1 
HETATM 7513 O  "O7'" . HFG C 2 .   ? -21.951 -20.565 23.577  1.00 75.62  ? 1801 HFG A "O7'" 1 
HETATM 7514 C  "C1'" . HFG C 2 .   ? -19.274 -19.579 26.747  1.00 87.44  ? 1801 HFG A "C1'" 1 
HETATM 7515 N  N3    . HFG C 2 .   ? -18.051 -18.922 27.161  1.00 82.88  ? 1801 HFG A N3    1 
HETATM 7516 C  C4    . HFG C 2 .   ? -18.139 -17.812 28.004  1.00 87.65  ? 1801 HFG A C4    1 
HETATM 7517 O  O11   . HFG C 2 .   ? -19.213 -17.456 28.459  1.00 86.78  ? 1801 HFG A O11   1 
HETATM 7518 C  C10   . HFG C 2 .   ? -16.864 -17.138 28.247  1.00 93.46  ? 1801 HFG A C10   1 
HETATM 7519 C  C5    . HFG C 2 .   ? -16.803 -16.025 29.088  1.00 94.54  ? 1801 HFG A C5    1 
HETATM 7520 C  C2    . HFG C 2 .   ? -16.845 -19.324 26.652  1.00 81.37  ? 1801 HFG A C2    1 
HETATM 7521 N  N1    . HFG C 2 .   ? -15.712 -18.760 26.828  1.00 82.84  ? 1801 HFG A N1    1 
HETATM 7522 C  C9    . HFG C 2 .   ? -15.701 -17.625 27.638  1.00 90.91  ? 1801 HFG A C9    1 
HETATM 7523 C  C8    . HFG C 2 .   ? -14.490 -16.978 27.844  1.00 100.59 ? 1801 HFG A C8    1 
HETATM 7524 C  C7    . HFG C 2 .   ? -14.441 -15.865 28.666  1.00 116.65 ? 1801 HFG A C7    1 
HETATM 7525 BR BR1   . HFG C 2 .   ? -12.790 -14.956 28.844  1.00 132.79 ? 1801 HFG A BR1   1 
HETATM 7526 C  C6    . HFG C 2 .   ? -15.587 -15.402 29.302  1.00 108.97 ? 1801 HFG A C6    1 
HETATM 7527 CL CL1   . HFG C 2 .   ? -15.505 -14.085 30.433  1.00 114.33 ? 1801 HFG A CL1   1 
HETATM 7528 ZN ZN    . ZN  D 3 .   ? -20.459 -43.251 37.058  1.00 111.60 ? 1802 ZN  A ZN    1 
HETATM 7529 CL CL    . CL  E 4 .   ? -18.676 -23.283 27.984  1.00 102.43 ? 1803 CL  A CL    1 
HETATM 7530 CL CL    . CL  F 4 .   ? -12.379 -20.817 18.546  0.94 110.14 ? 1804 CL  A CL    1 
HETATM 7531 C  C1    . GOL G 5 .   ? -23.875 -11.080 7.790   0.88 51.92  ? 1805 GOL A C1    1 
HETATM 7532 O  O1    . GOL G 5 .   ? -23.773 -9.943  8.602   0.88 51.80  ? 1805 GOL A O1    1 
HETATM 7533 C  C2    . GOL G 5 .   ? -25.227 -10.979 7.165   0.88 53.46  ? 1805 GOL A C2    1 
HETATM 7534 O  O2    . GOL G 5 .   ? -25.790 -9.686  7.440   0.88 57.68  ? 1805 GOL A O2    1 
HETATM 7535 C  C3    . GOL G 5 .   ? -25.041 -11.292 5.636   0.88 51.83  ? 1805 GOL A C3    1 
HETATM 7536 O  O3    . GOL G 5 .   ? -26.125 -10.599 4.935   0.88 71.82  ? 1805 GOL A O3    1 
HETATM 7537 O  "O4'" . HFG H 2 .   ? -7.264  5.450   8.157   0.94 71.80  ? 1801 HFG B "O4'" 1 
HETATM 7538 C  C21   . HFG H 2 .   ? -6.773  6.322   7.478   0.94 74.40  ? 1801 HFG B C21   1 
HETATM 7539 C  "C3'" . HFG H 2 .   ? -6.349  6.089   6.049   0.94 76.24  ? 1801 HFG B "C3'" 1 
HETATM 7540 C  "C2'" . HFG H 2 .   ? -7.108  4.997   5.282   0.94 70.39  ? 1801 HFG B "C2'" 1 
HETATM 7541 N  "N1'" . HFG H 2 .   ? -6.920  3.648   5.830   0.94 57.66  ? 1801 HFG B "N1'" 1 
HETATM 7542 C  "C6'" . HFG H 2 .   ? -7.480  2.647   4.916   0.94 53.20  ? 1801 HFG B "C6'" 1 
HETATM 7543 C  "C5'" . HFG H 2 .   ? -8.960  2.840   4.718   0.94 57.22  ? 1801 HFG B "C5'" 1 
HETATM 7544 C  "C4'" . HFG H 2 .   ? -9.259  4.257   4.240   0.94 66.12  ? 1801 HFG B "C4'" 1 
HETATM 7545 C  C39   . HFG H 2 .   ? -8.607  5.252   5.183   0.94 69.97  ? 1801 HFG B C39   1 
HETATM 7546 O  "O7'" . HFG H 2 .   ? -8.860  6.606   4.799   0.94 54.62  ? 1801 HFG B "O7'" 1 
HETATM 7547 C  "C1'" . HFG H 2 .   ? -6.456  7.692   8.039   0.94 79.67  ? 1801 HFG B "C1'" 1 
HETATM 7548 N  N3    . HFG H 2 .   ? -6.259  7.666   9.479   0.94 73.55  ? 1801 HFG B N3    1 
HETATM 7549 C  C4    . HFG H 2 .   ? -5.167  6.967   9.988   0.94 77.47  ? 1801 HFG B C4    1 
HETATM 7550 O  O11   . HFG H 2 .   ? -4.325  6.474   9.241   0.94 77.96  ? 1801 HFG B O11   1 
HETATM 7551 C  C10   . HFG H 2 .   ? -5.124  6.897   11.449  0.94 74.77  ? 1801 HFG B C10   1 
HETATM 7552 C  C5    . HFG H 2 .   ? -4.117  6.186   12.085  0.94 68.50  ? 1801 HFG B C5    1 
HETATM 7553 C  C2    . HFG H 2 .   ? -7.169  8.262   10.310  0.94 67.96  ? 1801 HFG B C2    1 
HETATM 7554 N  N1    . HFG H 2 .   ? -7.171  8.228   11.592  0.94 76.11  ? 1801 HFG B N1    1 
HETATM 7555 C  C9    . HFG H 2 .   ? -6.135  7.515   12.187  0.94 84.34  ? 1801 HFG B C9    1 
HETATM 7556 C  C8    . HFG H 2 .   ? -6.143  7.382   13.583  0.94 106.39 ? 1801 HFG B C8    1 
HETATM 7557 C  C7    . HFG H 2 .   ? -5.146  6.652   14.203  0.94 123.09 ? 1801 HFG B C7    1 
HETATM 7558 BR BR1   . HFG H 2 .   ? -5.226  6.424   16.084  0.94 210.79 ? 1801 HFG B BR1   1 
HETATM 7559 C  C6    . HFG H 2 .   ? -4.131  6.070   13.465  0.94 85.38  ? 1801 HFG B C6    1 
HETATM 7560 CL CL1   . HFG H 2 .   ? -2.864  5.178   14.237  0.94 94.02  ? 1801 HFG B CL1   1 
HETATM 7561 ZN ZN    . ZN  I 3 .   ? -2.979  31.479  -0.560  0.76 84.76  ? 1802 ZN  B ZN    1 
HETATM 7562 CL CL    . CL  J 4 .   ? -16.398 8.291   12.816  1.00 99.33  ? 1803 CL  B CL    1 
HETATM 7563 C  C1    . GOL K 5 .   ? -19.812 -8.052  4.479   0.96 61.26  ? 1804 GOL B C1    1 
HETATM 7564 O  O1    . GOL K 5 .   ? -18.746 -8.715  5.161   0.96 52.86  ? 1804 GOL B O1    1 
HETATM 7565 C  C2    . GOL K 5 .   ? -19.820 -8.561  3.008   0.96 67.27  ? 1804 GOL B C2    1 
HETATM 7566 O  O2    . GOL K 5 .   ? -19.905 -9.916  2.982   0.96 68.32  ? 1804 GOL B O2    1 
HETATM 7567 C  C3    . GOL K 5 .   ? -21.060 -7.931  2.330   0.96 75.93  ? 1804 GOL B C3    1 
HETATM 7568 O  O3    . GOL K 5 .   ? -22.048 -8.940  2.254   0.96 84.92  ? 1804 GOL B O3    1 
HETATM 7569 C  C1    . GOL L 5 .   ? -27.761 12.020  -10.038 1.00 119.64 ? 1805 GOL B C1    1 
HETATM 7570 O  O1    . GOL L 5 .   ? -27.984 13.151  -10.783 1.00 116.45 ? 1805 GOL B O1    1 
HETATM 7571 C  C2    . GOL L 5 .   ? -29.137 11.486  -9.640  1.00 122.32 ? 1805 GOL B C2    1 
HETATM 7572 O  O2    . GOL L 5 .   ? -29.220 10.131  -9.777  1.00 122.59 ? 1805 GOL B O2    1 
HETATM 7573 C  C3    . GOL L 5 .   ? -29.358 11.947  -8.174  1.00 117.85 ? 1805 GOL B C3    1 
HETATM 7574 O  O3    . GOL L 5 .   ? -30.171 10.968  -7.567  1.00 112.84 ? 1805 GOL B O3    1 
HETATM 7575 O  O     . HOH M 6 .   ? -32.348 -16.896 31.603  1.00 59.83  ? 1901 HOH A O     1 
HETATM 7576 O  O     . HOH M 6 .   ? -33.161 -23.622 3.228   1.00 65.09  ? 1902 HOH A O     1 
HETATM 7577 O  O     . HOH M 6 .   ? -31.161 -14.094 26.045  1.00 78.50  ? 1903 HOH A O     1 
HETATM 7578 O  O     . HOH M 6 .   ? -20.757 -29.048 0.044   1.00 68.00  ? 1904 HOH A O     1 
HETATM 7579 O  O     . HOH M 6 .   ? -6.196  -16.590 -1.119  1.00 53.37  ? 1905 HOH A O     1 
HETATM 7580 O  O     . HOH M 6 .   ? -5.701  -13.043 -0.430  1.00 41.79  ? 1906 HOH A O     1 
HETATM 7581 O  O     . HOH M 6 .   ? -18.215 -20.491 23.362  1.00 51.57  ? 1907 HOH A O     1 
HETATM 7582 O  O     . HOH M 6 .   ? -35.593 -30.791 29.337  1.00 123.65 ? 1908 HOH A O     1 
HETATM 7583 O  O     . HOH M 6 .   ? -16.857 -25.770 29.330  1.00 91.56  ? 1909 HOH A O     1 
HETATM 7584 O  O     . HOH N 6 .   ? -21.343 -8.452  -7.093  1.00 69.34  ? 1901 HOH B O     1 
HETATM 7585 O  O     . HOH N 6 .   ? -33.342 -3.501  19.075  1.00 57.54  ? 1902 HOH B O     1 
HETATM 7586 O  O     . HOH N 6 .   ? -3.112  22.018  -1.919  1.00 67.12  ? 1903 HOH B O     1 
HETATM 7587 O  O     . HOH N 6 .   ? -6.875  -9.577  -6.133  1.00 68.60  ? 1904 HOH B O     1 
HETATM 7588 O  O     . HOH N 6 .   ? -9.687  7.704   7.654   1.00 69.68  ? 1905 HOH B O     1 
HETATM 7589 O  O     . HOH N 6 .   ? -1.208  36.285  7.684   1.00 107.30 ? 1906 HOH B O     1 
HETATM 7590 O  O     . HOH N 6 .   ? -15.028 9.513   5.911   1.00 49.38  ? 1907 HOH B 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     . ARG A 3   ? 0.7332 0.8526 0.9542 0.1560  0.0947  0.0128  1220 ARG A N     
2    C  CA    . ARG A 3   ? 0.8018 0.9502 1.0653 0.1567  0.0918  0.0223  1220 ARG A CA    
3    C  C     . ARG A 3   ? 0.7789 0.9334 1.0532 0.1522  0.0720  0.0232  1220 ARG A C     
4    O  O     . ARG A 3   ? 0.9890 1.1387 1.2684 0.1599  0.0706  0.0228  1220 ARG A O     
5    C  CB    . ARG A 3   ? 0.8923 1.0625 1.1749 0.1489  0.0944  0.0293  1220 ARG A CB    
6    C  CG    . ARG A 3   ? 0.9453 1.1447 1.2729 0.1541  0.1011  0.0389  1220 ARG A CG    
7    C  CD    . ARG A 3   ? 0.9281 1.1469 1.2758 0.1485  0.1102  0.0456  1220 ARG A CD    
8    N  NE    . ARG A 3   ? 0.9678 1.1693 1.2868 0.1489  0.1255  0.0426  1220 ARG A NE    
9    C  CZ    . ARG A 3   ? 1.0956 1.2851 1.3885 0.1392  0.1199  0.0396  1220 ARG A CZ    
10   N  NH1   . ARG A 3   ? 1.1820 1.3751 1.4755 0.1286  0.1004  0.0387  1220 ARG A NH1   
11   N  NH2   . ARG A 3   ? 1.1324 1.3059 1.3980 0.1407  0.1338  0.0378  1220 ARG A NH2   
12   N  N     . LEU A 4   ? 0.8456 1.0096 1.1227 0.1401  0.0577  0.0246  1221 LEU A N     
13   C  CA    . LEU A 4   ? 0.8432 1.0153 1.1318 0.1353  0.0397  0.0265  1221 LEU A CA    
14   C  C     . LEU A 4   ? 0.8642 1.0163 1.1360 0.1403  0.0344  0.0213  1221 LEU A C     
15   O  O     . LEU A 4   ? 0.9276 1.0557 1.1693 0.1405  0.0368  0.0134  1221 LEU A O     
16   C  CB    . LEU A 4   ? 0.8601 1.0342 1.1401 0.1215  0.0269  0.0251  1221 LEU A CB    
17   C  CG    . LEU A 4   ? 0.9039 1.1038 1.2117 0.1143  0.0240  0.0320  1221 LEU A CG    
18   C  CD1   . LEU A 4   ? 0.8261 1.0254 1.1252 0.1015  0.0092  0.0298  1221 LEU A CD1   
19   C  CD2   . LEU A 4   ? 0.8318 1.0551 1.1753 0.1194  0.0213  0.0394  1221 LEU A CD2   
20   N  N     . GLY A 5   ? 0.8286 0.9906 1.1199 0.1439  0.0263  0.0262  1222 GLY A N     
21   C  CA    . GLY A 5   ? 0.7757 0.9191 1.0540 0.1489  0.0220  0.0228  1222 GLY A CA    
22   C  C     . GLY A 5   ? 0.8140 0.9700 1.1108 0.1486  0.0083  0.0292  1222 GLY A C     
23   O  O     . GLY A 5   ? 0.7917 0.9728 1.1157 0.1477  0.0038  0.0369  1222 GLY A O     
24   N  N     . LEU A 6   ? 0.8900 1.0279 1.1711 0.1491  0.0016  0.0261  1223 LEU A N     
25   C  CA    . LEU A 6   ? 0.8851 1.0310 1.1784 0.1494  -0.0110 0.0324  1223 LEU A CA    
26   C  C     . LEU A 6   ? 1.0464 1.2040 1.3659 0.1625  -0.0058 0.0406  1223 LEU A C     
27   O  O     . LEU A 6   ? 1.1512 1.2959 1.4686 0.1733  0.0071  0.0388  1223 LEU A O     
28   C  CB    . LEU A 6   ? 0.8527 0.9741 1.1225 0.1473  -0.0168 0.0273  1223 LEU A CB    
29   C  CG    . LEU A 6   ? 0.8868 1.0057 1.1429 0.1347  -0.0303 0.0248  1223 LEU A CG    
30   C  CD1   . LEU A 6   ? 0.9019 1.0260 1.1504 0.1248  -0.0303 0.0203  1223 LEU A CD1   
31   C  CD2   . LEU A 6   ? 0.8538 0.9461 1.0873 0.1339  -0.0317 0.0190  1223 LEU A CD2   
32   N  N     . GLU A 7   ? 0.9557 1.1376 1.2998 0.1618  -0.0160 0.0495  1224 GLU A N     
33   C  CA    . GLU A 7   ? 0.7679 0.9645 1.1406 0.1744  -0.0130 0.0586  1224 GLU A CA    
34   C  C     . GLU A 7   ? 0.7862 0.9756 1.1582 0.1798  -0.0225 0.0639  1224 GLU A C     
35   O  O     . GLU A 7   ? 0.9705 1.1646 1.3613 0.1927  -0.0183 0.0709  1224 GLU A O     
36   C  CB    . GLU A 7   ? 0.5494 0.7802 0.9545 0.1716  -0.0181 0.0664  1224 GLU A CB    
37   N  N     . ALA A 8   ? 0.8780 1.0564 1.2296 0.1709  -0.0346 0.0614  1225 ALA A N     
38   C  CA    . ALA A 8   ? 0.8664 1.0352 1.2136 0.1752  -0.0430 0.0667  1225 ALA A CA    
39   C  C     . ALA A 8   ? 0.8260 0.9616 1.1434 0.1740  -0.0384 0.0586  1225 ALA A C     
40   O  O     . ALA A 8   ? 0.7332 0.8544 1.0332 0.1695  -0.0304 0.0487  1225 ALA A O     
41   C  CB    . ALA A 8   ? 0.8844 1.0684 1.2334 0.1661  -0.0609 0.0717  1225 ALA A CB    
42   N  N     . THR A 9   ? 0.9360 1.0594 1.2474 0.1776  -0.0443 0.0633  1226 THR A N     
43   C  CA    . THR A 9   ? 0.9580 1.0500 1.2451 0.1769  -0.0403 0.0569  1226 THR A CA    
44   C  C     . THR A 9   ? 0.9117 0.9977 1.1863 0.1698  -0.0527 0.0601  1226 THR A C     
45   O  O     . THR A 9   ? 0.9188 1.0193 1.2041 0.1716  -0.0628 0.0700  1226 THR A O     
46   C  CB    . THR A 9   ? 0.8501 0.9243 1.1413 0.1914  -0.0292 0.0590  1226 THR A CB    
47   O  OG1   . THR A 9   ? 0.8496 0.9340 1.1584 0.2006  -0.0356 0.0720  1226 THR A OG1   
48   C  CG2   . THR A 9   ? 0.5860 0.6618 0.8862 0.1993  -0.0142 0.0547  1226 THR A CG2   
49   N  N     . LYS A 10  ? 0.8732 0.9367 1.1246 0.1621  -0.0513 0.0516  1227 LYS A N     
50   C  CA    . LYS A 10  ? 0.8112 0.8680 1.0484 0.1532  -0.0610 0.0528  1227 LYS A CA    
51   C  C     . LYS A 10  ? 0.8379 0.8902 1.0791 0.1609  -0.0655 0.0639  1227 LYS A C     
52   O  O     . LYS A 10  ? 0.8834 0.9428 1.1209 0.1562  -0.0761 0.0699  1227 LYS A O     
53   C  CB    . LYS A 10  ? 0.8551 0.8872 1.0708 0.1457  -0.0563 0.0418  1227 LYS A CB    
54   C  CG    . LYS A 10  ? 0.8695 0.8999 1.0708 0.1324  -0.0642 0.0383  1227 LYS A CG    
55   C  CD    . LYS A 10  ? 0.9643 0.9689 1.1487 0.1275  -0.0591 0.0292  1227 LYS A CD    
56   C  CE    . LYS A 10  ? 0.8898 0.8917 1.0621 0.1151  -0.0656 0.0261  1227 LYS A CE    
57   N  NZ    . LYS A 10  ? 0.7067 0.6987 0.8677 0.1070  -0.0628 0.0143  1227 LYS A NZ    
58   N  N     . GLU A 11  ? 0.9014 0.9408 1.1488 0.1731  -0.0572 0.0670  1228 GLU A N     
59   C  CA    . GLU A 11  ? 0.9379 0.9669 1.1861 0.1810  -0.0597 0.0775  1228 GLU A CA    
60   C  C     . GLU A 11  ? 0.9943 1.0469 1.2634 0.1901  -0.0674 0.0910  1228 GLU A C     
61   O  O     . GLU A 11  ? 0.9268 0.9768 1.1931 0.1929  -0.0750 0.1011  1228 GLU A O     
62   C  CB    . GLU A 11  ? 0.9278 0.9303 1.1739 0.1905  -0.0471 0.0750  1228 GLU A CB    
63   C  CG    . GLU A 11  ? 1.1339 1.1115 1.3596 0.1816  -0.0403 0.0614  1228 GLU A CG    
64   C  CD    . GLU A 11  ? 1.2960 1.2787 1.5215 0.1793  -0.0333 0.0502  1228 GLU A CD    
65   O  OE1   . GLU A 11  ? 1.2112 1.1797 1.4200 0.1701  -0.0309 0.0387  1228 GLU A OE1   
66   O  OE2   . GLU A 11  ? 1.4311 1.4328 1.6740 0.1869  -0.0305 0.0536  1228 GLU A OE2   
67   N  N     . ASP A 12  ? 1.0436 1.1193 1.3335 0.1946  -0.0661 0.0919  1229 ASP A N     
68   C  CA    . ASP A 12  ? 1.2410 1.3401 1.5549 0.2044  -0.0733 0.1050  1229 ASP A CA    
69   C  C     . ASP A 12  ? 1.3410 1.4686 1.6611 0.1952  -0.0878 0.1078  1229 ASP A C     
70   O  O     . ASP A 12  ? 1.5325 1.6727 1.8583 0.1976  -0.1002 0.1185  1229 ASP A O     
71   C  CB    . ASP A 12  ? 1.3535 1.4620 1.6916 0.2167  -0.0620 0.1058  1229 ASP A CB    
72   C  CG    . ASP A 12  ? 1.4143 1.4932 1.7450 0.2255  -0.0463 0.1008  1229 ASP A CG    
73   O  OD1   . ASP A 12  ? 1.4184 1.4796 1.7461 0.2339  -0.0454 0.1076  1229 ASP A OD1   
74   O  OD2   . ASP A 12  ? 1.4259 1.4984 1.7527 0.2238  -0.0347 0.0900  1229 ASP A OD2   
75   N  N     . ASN A 13  ? 1.2304 1.3676 1.5486 0.1845  -0.0867 0.0983  1230 ASN A N     
76   C  CA    . ASN A 13  ? 1.2050 1.3664 1.5274 0.1741  -0.0997 0.0992  1230 ASN A CA    
77   C  C     . ASN A 13  ? 1.1362 1.2866 1.4354 0.1594  -0.0993 0.0876  1230 ASN A C     
78   O  O     . ASN A 13  ? 1.0784 1.2345 1.3800 0.1536  -0.0938 0.0796  1230 ASN A O     
79   C  CB    . ASN A 13  ? 1.2662 1.4562 1.6179 0.1770  -0.0989 0.1012  1230 ASN A CB    
80   C  CG    . ASN A 13  ? 1.1922 1.4084 1.5523 0.1677  -0.1143 0.1040  1230 ASN A CG    
81   O  OD1   . ASN A 13  ? 1.1367 1.3491 1.4788 0.1594  -0.1255 0.1042  1230 ASN A OD1   
82   N  ND2   . ASN A 13  ? 1.1440 1.3865 1.5319 0.1688  -0.1143 0.1061  1230 ASN A ND2   
83   N  N     . LEU A 14  ? 1.0092 1.1445 1.2865 0.1534  -0.1051 0.0876  1231 LEU A N     
84   C  CA    . LEU A 14  ? 0.8855 1.0095 1.1420 0.1404  -0.1040 0.0771  1231 LEU A CA    
85   C  C     . LEU A 14  ? 0.8124 0.9568 1.0729 0.1297  -0.1111 0.0733  1231 LEU A C     
86   O  O     . LEU A 14  ? 0.8366 0.9774 1.0911 0.1225  -0.1055 0.0639  1231 LEU A O     
87   C  CB    . LEU A 14  ? 0.8307 0.9354 1.0651 0.1366  -0.1077 0.0788  1231 LEU A CB    
88   C  CG    . LEU A 14  ? 0.8304 0.9193 1.0447 0.1248  -0.1041 0.0680  1231 LEU A CG    
89   C  CD1   . LEU A 14  ? 0.7908 0.8611 1.0013 0.1266  -0.0918 0.0597  1231 LEU A CD1   
90   C  CD2   . LEU A 14  ? 0.5388 0.6145 0.7345 0.1200  -0.1088 0.0710  1231 LEU A CD2   
91   N  N     . PRO A 15  ? 0.8020 0.9664 1.0709 0.1278  -0.1235 0.0797  1232 PRO A N     
92   C  CA    . PRO A 15  ? 0.7083 0.8890 0.9794 0.1163  -0.1298 0.0747  1232 PRO A CA    
93   C  C     . PRO A 15  ? 0.7995 0.9944 1.0900 0.1164  -0.1228 0.0709  1232 PRO A C     
94   O  O     . PRO A 15  ? 0.8379 1.0327 1.1228 0.1070  -0.1202 0.0629  1232 PRO A O     
95   C  CB    . PRO A 15  ? 0.7144 0.9132 0.9922 0.1160  -0.1451 0.0832  1232 PRO A CB    
96   C  CG    . PRO A 15  ? 0.9352 1.1190 1.2006 0.1234  -0.1473 0.0908  1232 PRO A CG    
97   C  CD    . PRO A 15  ? 0.9569 1.1261 1.2278 0.1340  -0.1337 0.0911  1232 PRO A CD    
98   N  N     . ASP A 16  ? 0.9068 1.1134 1.2204 0.1271  -0.1186 0.0769  1233 ASP A N     
99   C  CA    . ASP A 16  ? 0.9164 1.1357 1.2477 0.1271  -0.1101 0.0735  1233 ASP A CA    
100  C  C     . ASP A 16  ? 0.9353 1.1334 1.2523 0.1278  -0.0954 0.0649  1233 ASP A C     
101  O  O     . ASP A 16  ? 0.9615 1.1628 1.2788 0.1219  -0.0896 0.0587  1233 ASP A O     
102  C  CB    . ASP A 16  ? 0.8560 1.0950 1.2180 0.1388  -0.1086 0.0825  1233 ASP A CB    
103  C  CG    . ASP A 16  ? 0.9629 1.2257 1.3408 0.1374  -0.1251 0.0910  1233 ASP A CG    
104  O  OD1   . ASP A 16  ? 0.9938 1.2574 1.3574 0.1266  -0.1368 0.0888  1233 ASP A OD1   
105  O  OD2   . ASP A 16  ? 1.0925 1.3729 1.4968 0.1474  -0.1266 0.0999  1233 ASP A OD2   
106  N  N     . TRP A 17  ? 0.8711 1.0459 1.1725 0.1334  -0.0905 0.0639  1234 TRP A N     
107  C  CA    . TRP A 17  ? 0.8330 0.9862 1.1170 0.1318  -0.0793 0.0544  1234 TRP A CA    
108  C  C     . TRP A 17  ? 0.8183 0.9670 1.0850 0.1182  -0.0830 0.0465  1234 TRP A C     
109  O  O     . TRP A 17  ? 0.8563 1.0022 1.1186 0.1145  -0.0760 0.0397  1234 TRP A O     
110  C  CB    . TRP A 17  ? 0.7927 0.9210 1.0633 0.1385  -0.0750 0.0545  1234 TRP A CB    
111  C  CG    . TRP A 17  ? 0.8280 0.9336 1.0783 0.1344  -0.0668 0.0439  1234 TRP A CG    
112  C  CD1   . TRP A 17  ? 0.8557 0.9516 1.1040 0.1392  -0.0546 0.0379  1234 TRP A CD1   
113  C  CD2   . TRP A 17  ? 0.8328 0.9236 1.0622 0.1244  -0.0707 0.0379  1234 TRP A CD2   
114  N  NE1   . TRP A 17  ? 0.8248 0.9008 1.0513 0.1323  -0.0522 0.0284  1234 TRP A NE1   
115  C  CE2   . TRP A 17  ? 0.7890 0.8625 1.0055 0.1233  -0.0618 0.0285  1234 TRP A CE2   
116  C  CE3   . TRP A 17  ? 0.7276 0.8183 0.9477 0.1163  -0.0805 0.0395  1234 TRP A CE3   
117  C  CZ2   . TRP A 17  ? 0.7146 0.7725 0.9125 0.1145  -0.0635 0.0212  1234 TRP A CZ2   
118  C  CZ3   . TRP A 17  ? 0.5749 0.6496 0.7768 0.1080  -0.0804 0.0324  1234 TRP A CZ3   
119  C  CH2   . TRP A 17  ? 0.6075 0.6669 0.8000 0.1071  -0.0724 0.0235  1234 TRP A CH2   
120  N  N     . TYR A 18  ? 0.8456 0.9940 1.1025 0.1111  -0.0938 0.0479  1235 TYR A N     
121  C  CA    . TYR A 18  ? 0.8422 0.9855 1.0831 0.0988  -0.0973 0.0410  1235 TYR A CA    
122  C  C     . TYR A 18  ? 0.7601 0.9211 1.0111 0.0919  -0.0987 0.0386  1235 TYR A C     
123  O  O     . TYR A 18  ? 0.8258 0.9807 1.0673 0.0852  -0.0950 0.0316  1235 TYR A O     
124  C  CB    . TYR A 18  ? 0.8010 0.9407 1.0304 0.0943  -0.1075 0.0441  1235 TYR A CB    
125  C  CG    . TYR A 18  ? 0.8636 0.9964 1.0763 0.0828  -0.1106 0.0377  1235 TYR A CG    
126  C  CD1   . TYR A 18  ? 0.8222 0.9352 1.0191 0.0799  -0.1051 0.0315  1235 TYR A CD1   
127  C  CD2   . TYR A 18  ? 0.9602 1.1060 1.1734 0.0747  -0.1193 0.0378  1235 TYR A CD2   
128  C  CE1   . TYR A 18  ? 0.8382 0.9460 1.0223 0.0700  -0.1076 0.0263  1235 TYR A CE1   
129  C  CE2   . TYR A 18  ? 0.8303 0.9689 1.0285 0.0649  -0.1212 0.0319  1235 TYR A CE2   
130  C  CZ    . TYR A 18  ? 0.8528 0.9730 1.0374 0.0630  -0.1151 0.0266  1235 TYR A CZ    
131  O  OH    . TYR A 18  ? 0.8080 0.9223 0.9803 0.0541  -0.1164 0.0214  1235 TYR A OH    
132  N  N     . SER A 19  ? 0.6923 0.8752 0.9637 0.0936  -0.1041 0.0449  1236 SER A N     
133  C  CA    . SER A 19  ? 0.7389 0.9394 1.0232 0.0868  -0.1052 0.0434  1236 SER A CA    
134  C  C     . SER A 19  ? 0.7150 0.9153 1.0062 0.0902  -0.0920 0.0404  1236 SER A C     
135  O  O     . SER A 19  ? 0.7470 0.9487 1.0358 0.0830  -0.0889 0.0358  1236 SER A O     
136  C  CB    . SER A 19  ? 0.7774 1.0023 1.0845 0.0880  -0.1146 0.0511  1236 SER A CB    
137  O  OG    . SER A 19  ? 0.9706 1.2139 1.2978 0.0845  -0.1120 0.0509  1236 SER A OG    
138  N  N     . GLN A 20  ? 0.6515 0.8471 0.9485 0.1014  -0.0833 0.0428  1237 GLN A N     
139  C  CA    . GLN A 20  ? 0.7161 0.9080 1.0151 0.1056  -0.0694 0.0396  1237 GLN A CA    
140  C  C     . GLN A 20  ? 0.7751 0.9447 1.0482 0.1013  -0.0642 0.0307  1237 GLN A C     
141  O  O     . GLN A 20  ? 0.7583 0.9271 1.0284 0.0990  -0.0566 0.0269  1237 GLN A O     
142  C  CB    . GLN A 20  ? 0.9453 1.1347 1.2548 0.1197  -0.0609 0.0437  1237 GLN A CB    
143  C  CG    . GLN A 20  ? 1.0735 1.2878 1.4137 0.1259  -0.0641 0.0532  1237 GLN A CG    
144  C  CD    . GLN A 20  ? 1.1690 1.4035 1.5295 0.1232  -0.0588 0.0543  1237 GLN A CD    
145  O  OE1   . GLN A 20  ? 1.2940 1.5255 1.6577 0.1288  -0.0446 0.0527  1237 GLN A OE1   
146  N  NE2   . GLN A 20  ? 1.1142 1.3683 1.4875 0.1139  -0.0696 0.0567  1237 GLN A NE2   
147  N  N     . VAL A 21  ? 0.8127 0.9647 1.0673 0.0996  -0.0685 0.0277  1238 VAL A N     
148  C  CA    . VAL A 21  ? 0.9196 1.0520 1.1519 0.0953  -0.0647 0.0194  1238 VAL A CA    
149  C  C     . VAL A 21  ? 0.9156 1.0517 1.1411 0.0837  -0.0704 0.0160  1238 VAL A C     
150  O  O     . VAL A 21  ? 0.7483 0.8766 0.9627 0.0803  -0.0658 0.0105  1238 VAL A O     
151  C  CB    . VAL A 21  ? 0.9186 1.0303 1.1359 0.0977  -0.0658 0.0172  1238 VAL A CB    
152  C  CG1   . VAL A 21  ? 0.8766 0.9918 1.0958 0.0957  -0.0757 0.0223  1238 VAL A CG1   
153  C  CG2   . VAL A 21  ? 0.9994 1.0938 1.1960 0.0913  -0.0648 0.0087  1238 VAL A CG2   
154  N  N     . ILE A 22  ? 0.9421 1.0892 1.1732 0.0777  -0.0803 0.0190  1239 ILE A N     
155  C  CA    . ILE A 22  ? 0.8865 1.0355 1.1114 0.0671  -0.0844 0.0153  1239 ILE A CA    
156  C  C     . ILE A 22  ? 0.8711 1.0350 1.1097 0.0645  -0.0809 0.0164  1239 ILE A C     
157  O  O     . ILE A 22  ? 0.7539 0.9151 0.9858 0.0577  -0.0799 0.0127  1239 ILE A O     
158  C  CB    . ILE A 22  ? 0.7192 0.8721 0.9420 0.0609  -0.0954 0.0168  1239 ILE A CB    
159  C  CG1   . ILE A 22  ? 0.6616 0.8333 0.9028 0.0633  -0.1013 0.0238  1239 ILE A CG1   
160  C  CG2   . ILE A 22  ? 0.5337 0.6697 0.7405 0.0616  -0.0973 0.0152  1239 ILE A CG2   
161  C  CD1   . ILE A 22  ? 0.5225 0.6962 0.7583 0.0586  -0.1122 0.0255  1239 ILE A CD1   
162  N  N     . THR A 23  ? 0.8516 1.0312 1.1104 0.0698  -0.0784 0.0219  1240 THR A N     
163  C  CA    . THR A 23  ? 0.7037 0.8965 0.9763 0.0670  -0.0732 0.0231  1240 THR A CA    
164  C  C     . THR A 23  ? 0.7068 0.8914 0.9744 0.0729  -0.0595 0.0212  1240 THR A C     
165  O  O     . THR A 23  ? 0.6397 0.8203 0.8998 0.0684  -0.0547 0.0185  1240 THR A O     
166  C  CB    . THR A 23  ? 0.6362 0.8523 0.9360 0.0686  -0.0770 0.0299  1240 THR A CB    
167  O  OG1   . THR A 23  ? 0.7329 0.9503 1.0405 0.0796  -0.0749 0.0342  1240 THR A OG1   
168  C  CG2   . THR A 23  ? 0.5713 0.7964 0.8740 0.0599  -0.0912 0.0306  1240 THR A CG2   
169  N  N     . LYS A 24  ? 0.8089 0.9884 1.0774 0.0832  -0.0529 0.0224  1241 LYS A N     
170  C  CA    . LYS A 24  ? 0.8765 1.0471 1.1373 0.0884  -0.0394 0.0199  1241 LYS A CA    
171  C  C     . LYS A 24  ? 0.7896 0.9379 1.0220 0.0855  -0.0389 0.0124  1241 LYS A C     
172  O  O     . LYS A 24  ? 0.7814 0.9214 1.0023 0.0869  -0.0299 0.0094  1241 LYS A O     
173  C  CB    . LYS A 24  ? 0.8186 0.9890 1.0887 0.1007  -0.0319 0.0227  1241 LYS A CB    
174  C  CG    . LYS A 24  ? 0.9593 1.1541 1.2610 0.1045  -0.0337 0.0311  1241 LYS A CG    
175  C  CD    . LYS A 24  ? 1.0507 1.2454 1.3622 0.1172  -0.0197 0.0334  1241 LYS A CD    
176  C  CE    . LYS A 24  ? 1.1481 1.3657 1.4929 0.1246  -0.0194 0.0422  1241 LYS A CE    
177  N  NZ    . LYS A 24  ? 1.1794 1.4099 1.5435 0.1301  -0.0047 0.0455  1241 LYS A NZ    
178  N  N     . GLY A 25  ? 0.6792 0.8183 0.9000 0.0808  -0.0488 0.0094  1242 GLY A N     
179  C  CA    . GLY A 25  ? 0.4885 0.6107 0.6870 0.0760  -0.0507 0.0030  1242 GLY A CA    
180  C  C     . GLY A 25  ? 0.7536 0.8806 0.9502 0.0665  -0.0552 0.0022  1242 GLY A C     
181  O  O     . GLY A 25  ? 0.7422 0.8572 0.9227 0.0623  -0.0579 -0.0024 1242 GLY A O     
182  N  N     . GLU A 26  ? 0.8404 0.9846 1.0543 0.0630  -0.0561 0.0068  1243 GLU A N     
183  C  CA    . GLU A 26  ? 0.9193 1.0678 1.1337 0.0543  -0.0584 0.0065  1243 GLU A CA    
184  C  C     . GLU A 26  ? 0.9278 1.0699 1.1328 0.0473  -0.0682 0.0032  1243 GLU A C     
185  O  O     . GLU A 26  ? 0.8048 0.9418 1.0018 0.0417  -0.0690 0.0010  1243 GLU A O     
186  C  CB    . GLU A 26  ? 0.9274 1.0679 1.1303 0.0550  -0.0496 0.0049  1243 GLU A CB    
187  C  CG    . GLU A 26  ? 0.8541 1.0009 1.0658 0.0618  -0.0378 0.0084  1243 GLU A CG    
188  C  CD    . GLU A 26  ? 0.9703 1.1096 1.1692 0.0618  -0.0288 0.0079  1243 GLU A CD    
189  O  OE1   . GLU A 26  ? 0.9025 1.0418 1.1019 0.0685  -0.0174 0.0095  1243 GLU A OE1   
190  O  OE2   . GLU A 26  ? 1.0851 1.2177 1.2726 0.0557  -0.0326 0.0062  1243 GLU A OE2   
191  N  N     . MET A 27  ? 0.9499 1.0920 1.1560 0.0480  -0.0749 0.0036  1244 MET A N     
192  C  CA    . MET A 27  ? 0.8988 1.0342 1.0956 0.0420  -0.0827 0.0007  1244 MET A CA    
193  C  C     . MET A 27  ? 0.8903 1.0374 1.0967 0.0354  -0.0899 0.0026  1244 MET A C     
194  O  O     . MET A 27  ? 0.8286 0.9706 1.0272 0.0292  -0.0945 -0.0003 1244 MET A O     
195  C  CB    . MET A 27  ? 0.8293 0.9549 1.0185 0.0462  -0.0851 0.0000  1244 MET A CB    
196  C  CG    . MET A 27  ? 0.8771 0.9884 1.0546 0.0513  -0.0793 -0.0035 1244 MET A CG    
197  S  SD    . MET A 27  ? 0.9971 1.0920 1.1606 0.0494  -0.0835 -0.0077 1244 MET A SD    
198  C  CE    . MET A 27  ? 1.0660 1.1681 1.2358 0.0470  -0.0907 -0.0033 1244 MET A CE    
199  N  N     . ILE A 28  ? 0.9326 1.0953 1.1560 0.0366  -0.0908 0.0071  1245 ILE A N     
200  C  CA    . ILE A 28  ? 0.7796 0.9542 1.0123 0.0310  -0.0996 0.0089  1245 ILE A CA    
201  C  C     . ILE A 28  ? 0.8422 1.0343 1.0958 0.0294  -0.0978 0.0124  1245 ILE A C     
202  O  O     . ILE A 28  ? 0.8172 1.0146 1.0808 0.0358  -0.0902 0.0154  1245 ILE A O     
203  C  CB    . ILE A 28  ? 0.7930 0.9692 1.0256 0.0357  -0.1059 0.0120  1245 ILE A CB    
204  C  CG1   . ILE A 28  ? 0.7615 0.9212 0.9746 0.0349  -0.1084 0.0089  1245 ILE A CG1   
205  C  CG2   . ILE A 28  ? 0.6642 0.8578 0.9112 0.0325  -0.1150 0.0159  1245 ILE A CG2   
206  C  CD1   . ILE A 28  ? 0.6323 0.7875 0.8359 0.0260  -0.1127 0.0048  1245 ILE A CD1   
207  N  N     . GLU A 29  ? 0.8274 1.0273 1.0874 0.0204  -0.1038 0.0114  1246 GLU A N     
208  C  CA    . GLU A 29  ? 0.7909 1.0103 1.0741 0.0174  -0.1058 0.0151  1246 GLU A CA    
209  C  C     . GLU A 29  ? 0.7562 0.9837 1.0422 0.0115  -0.1190 0.0148  1246 GLU A C     
210  O  O     . GLU A 29  ? 0.7219 0.9387 0.9916 0.0057  -0.1242 0.0102  1246 GLU A O     
211  C  CB    . GLU A 29  ? 0.8134 1.0353 1.1044 0.0109  -0.0995 0.0142  1246 GLU A CB    
212  C  CG    . GLU A 29  ? 0.7564 1.0000 1.0761 0.0095  -0.0984 0.0192  1246 GLU A CG    
213  C  CD    . GLU A 29  ? 0.8254 1.0760 1.1561 0.0206  -0.0898 0.0244  1246 GLU A CD    
214  O  OE1   . GLU A 29  ? 0.8268 1.0675 1.1492 0.0253  -0.0781 0.0242  1246 GLU A OE1   
215  O  OE2   . GLU A 29  ? 0.7779 1.0427 1.1239 0.0253  -0.0949 0.0286  1246 GLU A OE2   
216  N  N     . TYR A 30  ? 0.8036 1.0498 1.1097 0.0134  -0.1244 0.0199  1247 TYR A N     
217  C  CA    . TYR A 30  ? 0.8031 1.0585 1.1113 0.0088  -0.1385 0.0204  1247 TYR A CA    
218  C  C     . TYR A 30  ? 0.8591 1.1197 1.1729 -0.0040 -0.1439 0.0162  1247 TYR A C     
219  O  O     . TYR A 30  ? 0.7934 1.0529 1.1136 -0.0087 -0.1362 0.0143  1247 TYR A O     
220  C  CB    . TYR A 30  ? 0.7915 1.0657 1.1205 0.0161  -0.1431 0.0279  1247 TYR A CB    
221  C  CG    . TYR A 30  ? 0.7285 0.9938 1.0482 0.0283  -0.1395 0.0315  1247 TYR A CG    
222  C  CD1   . TYR A 30  ? 0.7070 0.9641 1.0097 0.0302  -0.1480 0.0322  1247 TYR A CD1   
223  C  CD2   . TYR A 30  ? 0.5336 0.7972 0.8605 0.0377  -0.1271 0.0341  1247 TYR A CD2   
224  C  CE1   . TYR A 30  ? 0.7263 0.9740 1.0212 0.0407  -0.1445 0.0357  1247 TYR A CE1   
225  C  CE2   . TYR A 30  ? 0.6727 0.9266 0.9913 0.0483  -0.1238 0.0367  1247 TYR A CE2   
226  C  CZ    . TYR A 30  ? 0.8529 1.0985 1.1560 0.0496  -0.1326 0.0376  1247 TYR A CZ    
227  O  OH    . TYR A 30  ? 0.7802 1.0139 1.0747 0.0597  -0.1289 0.0404  1247 TYR A OH    
228  N  N     . TYR A 31  ? 0.8490 1.1133 1.1578 -0.0098 -0.1572 0.0145  1248 TYR A N     
229  C  CA    . TYR A 31  ? 0.7661 1.0266 1.0695 -0.0224 -0.1624 0.0079  1248 TYR A CA    
230  C  C     . TYR A 31  ? 0.7734 1.0491 1.0853 -0.0286 -0.1781 0.0081  1248 TYR A C     
231  O  O     . TYR A 31  ? 0.7216 1.0023 1.0291 -0.0233 -0.1869 0.0120  1248 TYR A O     
232  C  CB    . TYR A 31  ? 0.7411 0.9785 1.0145 -0.0242 -0.1611 0.0017  1248 TYR A CB    
233  C  CG    . TYR A 31  ? 0.7767 1.0052 1.0441 -0.0354 -0.1609 -0.0055 1248 TYR A CG    
234  C  CD1   . TYR A 31  ? 0.8220 1.0474 1.0981 -0.0382 -0.1508 -0.0066 1248 TYR A CD1   
235  C  CD2   . TYR A 31  ? 0.8084 1.0302 1.0600 -0.0429 -0.1702 -0.0113 1248 TYR A CD2   
236  C  CE1   . TYR A 31  ? 0.8584 1.0742 1.1296 -0.0478 -0.1500 -0.0128 1248 TYR A CE1   
237  C  CE2   . TYR A 31  ? 0.9500 1.1617 1.1959 -0.0528 -0.1690 -0.0185 1248 TYR A CE2   
238  C  CZ    . TYR A 31  ? 0.9852 1.1939 1.2419 -0.0552 -0.1590 -0.0191 1248 TYR A CZ    
239  O  OH    . TYR A 31  ? 1.0661 1.2634 1.3178 -0.0646 -0.1573 -0.0258 1248 TYR A OH    
240  N  N     . ASP A 32  ? 0.8982 1.1796 1.2204 -0.0404 -0.1820 0.0038  1249 ASP A N     
241  C  CA    . ASP A 32  ? 0.8582 1.1562 1.1917 -0.0479 -0.1980 0.0034  1249 ASP A CA    
242  C  C     . ASP A 32  ? 0.7894 1.0742 1.0941 -0.0535 -0.2090 -0.0030 1249 ASP A C     
243  O  O     . ASP A 32  ? 0.8353 1.1299 1.1437 -0.0619 -0.2232 -0.0056 1249 ASP A O     
244  C  CB    . ASP A 32  ? 0.8660 1.1763 1.2250 -0.0591 -0.1979 0.0012  1249 ASP A CB    
245  C  CG    . ASP A 32  ? 0.8605 1.1517 1.2047 -0.0700 -0.1938 -0.0079 1249 ASP A CG    
246  O  OD1   . ASP A 32  ? 0.8887 1.1587 1.2115 -0.0664 -0.1835 -0.0106 1249 ASP A OD1   
247  O  OD2   . ASP A 32  ? 0.7364 1.0343 1.0925 -0.0824 -0.2009 -0.0124 1249 ASP A OD2   
248  N  N     . VAL A 33  ? 0.7281 0.9910 1.0044 -0.0491 -0.2029 -0.0056 1250 VAL A N     
249  C  CA    . VAL A 33  ? 0.7515 1.0011 0.9983 -0.0514 -0.2112 -0.0100 1250 VAL A CA    
250  C  C     . VAL A 33  ? 0.7440 0.9896 0.9788 -0.0391 -0.2098 -0.0033 1250 VAL A C     
251  O  O     . VAL A 33  ? 0.7387 0.9738 0.9695 -0.0316 -0.1973 -0.0016 1250 VAL A O     
252  C  CB    . VAL A 33  ? 0.7406 0.9667 0.9647 -0.0576 -0.2039 -0.0191 1250 VAL A CB    
253  C  CG1   . VAL A 33  ? 0.7942 1.0068 0.9875 -0.0591 -0.2111 -0.0231 1250 VAL A CG1   
254  C  CG2   . VAL A 33  ? 0.6094 0.8367 0.8453 -0.0696 -0.2041 -0.0256 1250 VAL A CG2   
255  N  N     . SER A 34  ? 0.8428 1.0954 1.0708 -0.0371 -0.2228 0.0004  1251 SER A N     
256  C  CA    . SER A 34  ? 1.0084 1.2588 1.2291 -0.0249 -0.2216 0.0083  1251 SER A CA    
257  C  C     . SER A 34  ? 1.0119 1.2368 1.2019 -0.0226 -0.2131 0.0049  1251 SER A C     
258  O  O     . SER A 34  ? 0.8962 1.1072 1.0660 -0.0303 -0.2131 -0.0029 1251 SER A O     
259  C  CB    . SER A 34  ? 0.9734 1.2382 1.1951 -0.0233 -0.2385 0.0142  1251 SER A CB    
260  O  OG    . SER A 34  ? 1.0921 1.3469 1.2935 -0.0143 -0.2395 0.0200  1251 SER A OG    
261  N  N     . GLY A 35  ? 0.9503 1.1692 1.1385 -0.0120 -0.2050 0.0107  1252 GLY A N     
262  C  CA    . GLY A 35  ? 0.9543 1.1512 1.1188 -0.0094 -0.1959 0.0084  1252 GLY A CA    
263  C  C     . GLY A 35  ? 0.9158 1.1013 1.0811 -0.0114 -0.1825 0.0026  1252 GLY A C     
264  O  O     . GLY A 35  ? 0.8505 1.0198 1.0008 -0.0082 -0.1742 0.0015  1252 GLY A O     
265  N  N     . CYS A 36  ? 0.7954 0.9893 0.9787 -0.0162 -0.1800 -0.0004 1253 CYS A N     
266  C  CA    . CYS A 36  ? 0.6888 0.8721 0.8720 -0.0188 -0.1688 -0.0058 1253 CYS A CA    
267  C  C     . CYS A 36  ? 0.6825 0.8751 0.8874 -0.0138 -0.1615 -0.0020 1253 CYS A C     
268  O  O     . CYS A 36  ? 0.7840 0.9940 1.0090 -0.0128 -0.1656 0.0023  1253 CYS A O     
269  C  CB    . CYS A 36  ? 0.6022 0.7831 0.7829 -0.0301 -0.1714 -0.0133 1253 CYS A CB    
270  S  SG    . CYS A 36  ? 0.9196 1.0917 1.0742 -0.0369 -0.1819 -0.0185 1253 CYS A SG    
271  N  N     . TYR A 37  ? 0.6598 0.8408 0.8605 -0.0103 -0.1506 -0.0033 1254 TYR A N     
272  C  CA    . TYR A 37  ? 0.6414 0.8273 0.8563 -0.0038 -0.1426 0.0003  1254 TYR A CA    
273  C  C     . TYR A 37  ? 0.6983 0.8739 0.9103 -0.0062 -0.1333 -0.0039 1254 TYR A C     
274  O  O     . TYR A 37  ? 0.7459 0.9075 0.9428 -0.0090 -0.1313 -0.0084 1254 TYR A O     
275  C  CB    . TYR A 37  ? 0.5355 0.7166 0.7458 0.0065  -0.1395 0.0047  1254 TYR A CB    
276  C  CG    . TYR A 37  ? 0.7011 0.8897 0.9120 0.0103  -0.1483 0.0100  1254 TYR A CG    
277  C  CD1   . TYR A 37  ? 0.6513 0.8570 0.8822 0.0154  -0.1513 0.0161  1254 TYR A CD1   
278  C  CD2   . TYR A 37  ? 0.7292 0.9081 0.9210 0.0093  -0.1535 0.0095  1254 TYR A CD2   
279  C  CE1   . TYR A 37  ? 0.6502 0.8635 0.8825 0.0195  -0.1603 0.0219  1254 TYR A CE1   
280  C  CE2   . TYR A 37  ? 0.7862 0.9713 0.9767 0.0131  -0.1621 0.0153  1254 TYR A CE2   
281  C  CZ    . TYR A 37  ? 0.8349 1.0375 1.0460 0.0183  -0.1662 0.0216  1254 TYR A CZ    
282  O  OH    . TYR A 37  ? 1.0580 1.2677 1.2691 0.0230  -0.1756 0.0284  1254 TYR A OH    
283  N  N     . ILE A 38  ? 0.5810 0.7641 0.8081 -0.0046 -0.1274 -0.0017 1255 ILE A N     
284  C  CA    . ILE A 38  ? 0.6492 0.8234 0.8737 -0.0058 -0.1187 -0.0041 1255 ILE A CA    
285  C  C     . ILE A 38  ? 0.6659 0.8294 0.8803 0.0023  -0.1123 -0.0035 1255 ILE A C     
286  O  O     . ILE A 38  ? 0.7955 0.9637 1.0158 0.0095  -0.1095 0.0002  1255 ILE A O     
287  C  CB    . ILE A 38  ? 0.5289 0.7146 0.7721 -0.0078 -0.1143 -0.0014 1255 ILE A CB    
288  C  CG1   . ILE A 38  ? 0.4661 0.6594 0.7186 -0.0180 -0.1205 -0.0035 1255 ILE A CG1   
289  C  CG2   . ILE A 38  ? 0.5654 0.7412 0.8038 -0.0061 -0.1042 -0.0019 1255 ILE A CG2   
290  C  CD1   . ILE A 38  ? 0.4788 0.6895 0.7554 -0.0202 -0.1193 0.0005  1255 ILE A CD1   
291  N  N     . LEU A 39  ? 0.5026 0.6518 0.7028 0.0010  -0.1102 -0.0074 1256 LEU A N     
292  C  CA    . LEU A 39  ? 0.6278 0.7668 0.8194 0.0071  -0.1047 -0.0077 1256 LEU A CA    
293  C  C     . LEU A 39  ? 0.5813 0.7193 0.7760 0.0077  -0.0977 -0.0072 1256 LEU A C     
294  O  O     . LEU A 39  ? 0.6016 0.7340 0.7931 0.0034  -0.0962 -0.0093 1256 LEU A O     
295  C  CB    . LEU A 39  ? 0.7287 0.8546 0.9062 0.0055  -0.1057 -0.0115 1256 LEU A CB    
296  C  CG    . LEU A 39  ? 0.7529 0.8783 0.9247 0.0028  -0.1117 -0.0123 1256 LEU A CG    
297  C  CD1   . LEU A 39  ? 0.5791 0.6918 0.7387 0.0006  -0.1106 -0.0161 1256 LEU A CD1   
298  C  CD2   . LEU A 39  ? 0.8014 0.9308 0.9744 0.0087  -0.1143 -0.0082 1256 LEU A CD2   
299  N  N     . ARG A 40  ? 0.4780 0.6211 0.6788 0.0135  -0.0930 -0.0040 1257 ARG A N     
300  C  CA    . ARG A 40  ? 0.5714 0.7119 0.7716 0.0149  -0.0856 -0.0032 1257 ARG A CA    
301  C  C     . ARG A 40  ? 0.5722 0.6983 0.7564 0.0175  -0.0842 -0.0062 1257 ARG A C     
302  O  O     . ARG A 40  ? 0.6779 0.7974 0.8544 0.0186  -0.0880 -0.0087 1257 ARG A O     
303  C  CB    . ARG A 40  ? 0.7359 0.8850 0.9457 0.0209  -0.0795 0.0008  1257 ARG A CB    
304  C  CG    . ARG A 40  ? 0.7110 0.8776 0.9411 0.0188  -0.0818 0.0045  1257 ARG A CG    
305  C  CD    . ARG A 40  ? 0.7219 0.8982 0.9645 0.0258  -0.0745 0.0090  1257 ARG A CD    
306  N  NE    . ARG A 40  ? 0.6944 0.8660 0.9330 0.0284  -0.0639 0.0100  1257 ARG A NE    
307  C  CZ    . ARG A 40  ? 0.7227 0.8991 0.9680 0.0352  -0.0548 0.0132  1257 ARG A CZ    
308  N  NH1   . ARG A 40  ? 0.7791 0.9661 1.0381 0.0407  -0.0551 0.0159  1257 ARG A NH1   
309  N  NH2   . ARG A 40  ? 0.6558 0.8259 0.8935 0.0371  -0.0449 0.0140  1257 ARG A NH2   
310  N  N     . HIS A 41  ? 0.6423 0.7635 0.8216 0.0183  -0.0789 -0.0056 1258 HIS A N     
311  C  CA    . HIS A 41  ? 0.6802 0.7889 0.8453 0.0194  -0.0796 -0.0085 1258 HIS A CA    
312  C  C     . HIS A 41  ? 0.7720 0.8740 0.9282 0.0250  -0.0803 -0.0108 1258 HIS A C     
313  O  O     . HIS A 41  ? 0.7912 0.8849 0.9393 0.0244  -0.0839 -0.0140 1258 HIS A O     
314  C  CB    . HIS A 41  ? 0.5709 0.6756 0.7312 0.0196  -0.0746 -0.0064 1258 HIS A CB    
315  C  CG    . HIS A 41  ? 0.7437 0.8476 0.8989 0.0256  -0.0679 -0.0045 1258 HIS A CG    
316  N  ND1   . HIS A 41  ? 0.8785 0.9916 1.0441 0.0265  -0.0613 -0.0005 1258 HIS A ND1   
317  C  CD2   . HIS A 41  ? 0.8490 0.9436 0.9895 0.0307  -0.0663 -0.0062 1258 HIS A CD2   
318  C  CE1   . HIS A 41  ? 0.9296 1.0384 1.0862 0.0327  -0.0547 0.0003  1258 HIS A CE1   
319  N  NE2   . HIS A 41  ? 0.8946 0.9915 1.0345 0.0352  -0.0580 -0.0036 1258 HIS A NE2   
320  N  N     . TRP A 42  ? 0.7527 0.8583 0.9118 0.0302  -0.0768 -0.0094 1259 TRP A N     
321  C  CA    . TRP A 42  ? 0.8213 0.9178 0.9708 0.0355  -0.0765 -0.0121 1259 TRP A CA    
322  C  C     . TRP A 42  ? 0.7102 0.8033 0.8594 0.0341  -0.0824 -0.0142 1259 TRP A C     
323  O  O     . TRP A 42  ? 0.7112 0.7939 0.8511 0.0353  -0.0839 -0.0177 1259 TRP A O     
324  C  CB    . TRP A 42  ? 0.8256 0.9255 0.9789 0.0421  -0.0701 -0.0101 1259 TRP A CB    
325  C  CG    . TRP A 42  ? 0.8215 0.9092 0.9628 0.0476  -0.0685 -0.0138 1259 TRP A CG    
326  C  CD1   . TRP A 42  ? 0.8749 0.9598 1.0183 0.0515  -0.0690 -0.0144 1259 TRP A CD1   
327  C  CD2   . TRP A 42  ? 0.8265 0.9023 0.9513 0.0494  -0.0663 -0.0176 1259 TRP A CD2   
328  N  NE1   . TRP A 42  ? 0.8911 0.9620 1.0208 0.0553  -0.0668 -0.0190 1259 TRP A NE1   
329  C  CE2   . TRP A 42  ? 0.7747 0.8402 0.8923 0.0539  -0.0657 -0.0214 1259 TRP A CE2   
330  C  CE3   . TRP A 42  ? 0.8920 0.9640 1.0066 0.0478  -0.0653 -0.0180 1259 TRP A CE3   
331  C  CZ2   . TRP A 42  ? 0.7302 0.7820 0.8304 0.0560  -0.0647 -0.0265 1259 TRP A CZ2   
332  C  CZ3   . TRP A 42  ? 0.9349 0.9941 1.0314 0.0506  -0.0648 -0.0223 1259 TRP A CZ3   
333  C  CH2   . TRP A 42  ? 0.8412 0.8905 0.9306 0.0543  -0.0647 -0.0270 1259 TRP A CH2   
334  N  N     . SER A 43  ? 0.5761 0.6770 0.7343 0.0310  -0.0860 -0.0122 1260 SER A N     
335  C  CA    . SER A 43  ? 0.6382 0.7345 0.7936 0.0293  -0.0908 -0.0136 1260 SER A CA    
336  C  C     . SER A 43  ? 0.9267 1.0196 1.0788 0.0232  -0.0939 -0.0160 1260 SER A C     
337  O  O     . SER A 43  ? 0.9898 1.0752 1.1369 0.0220  -0.0959 -0.0183 1260 SER A O     
338  C  CB    . SER A 43  ? 0.5685 0.6735 0.7322 0.0297  -0.0936 -0.0101 1260 SER A CB    
339  O  OG    . SER A 43  ? 0.5654 0.6801 0.7361 0.0244  -0.0960 -0.0089 1260 SER A OG    
340  N  N     . PHE A 44  ? 0.9018 0.9993 1.0574 0.0193  -0.0936 -0.0155 1261 PHE A N     
341  C  CA    . PHE A 44  ? 0.7478 0.8410 0.9009 0.0144  -0.0954 -0.0178 1261 PHE A CA    
342  C  C     . PHE A 44  ? 0.6419 0.7264 0.7884 0.0158  -0.0952 -0.0203 1261 PHE A C     
343  O  O     . PHE A 44  ? 0.7007 0.7809 0.8460 0.0131  -0.0970 -0.0223 1261 PHE A O     
344  C  CB    . PHE A 44  ? 0.7691 0.8669 0.9273 0.0102  -0.0945 -0.0169 1261 PHE A CB    
345  C  CG    . PHE A 44  ? 0.6823 0.7748 0.8386 0.0058  -0.0957 -0.0194 1261 PHE A CG    
346  C  CD1   . PHE A 44  ? 0.6520 0.7448 0.8083 0.0018  -0.0981 -0.0210 1261 PHE A CD1   
347  C  CD2   . PHE A 44  ? 0.5628 0.6494 0.7163 0.0063  -0.0943 -0.0200 1261 PHE A CD2   
348  C  CE1   . PHE A 44  ? 0.5109 0.5975 0.6648 -0.0016 -0.0977 -0.0238 1261 PHE A CE1   
349  C  CE2   . PHE A 44  ? 0.6312 0.7130 0.7847 0.0033  -0.0947 -0.0220 1261 PHE A CE2   
350  C  CZ    . PHE A 44  ? 0.5489 0.6305 0.7029 -0.0006 -0.0957 -0.0241 1261 PHE A CZ    
351  N  N     . ALA A 45  ? 0.6452 0.7270 0.7871 0.0199  -0.0932 -0.0202 1262 ALA A N     
352  C  CA    . ALA A 45  ? 0.6206 0.6943 0.7553 0.0209  -0.0949 -0.0230 1262 ALA A CA    
353  C  C     . ALA A 45  ? 0.6581 0.7267 0.7918 0.0209  -0.0972 -0.0256 1262 ALA A C     
354  O  O     . ALA A 45  ? 0.6312 0.6954 0.7643 0.0190  -0.0999 -0.0279 1262 ALA A O     
355  C  CB    . ALA A 45  ? 0.4203 0.4910 0.5471 0.0252  -0.0924 -0.0229 1262 ALA A CB    
356  N  N     . ILE A 46  ? 0.5510 0.6204 0.6861 0.0231  -0.0961 -0.0246 1263 ILE A N     
357  C  CA    . ILE A 46  ? 0.8206 0.8839 0.9550 0.0229  -0.0974 -0.0260 1263 ILE A CA    
358  C  C     . ILE A 46  ? 0.6883 0.7523 0.8261 0.0180  -0.0990 -0.0262 1263 ILE A C     
359  O  O     . ILE A 46  ? 0.6874 0.7462 0.8255 0.0159  -0.1001 -0.0284 1263 ILE A O     
360  C  CB    . ILE A 46  ? 0.8161 0.8805 0.9520 0.0266  -0.0958 -0.0234 1263 ILE A CB    
361  C  CG1   . ILE A 46  ? 0.7617 0.8267 0.8961 0.0323  -0.0923 -0.0228 1263 ILE A CG1   
362  C  CG2   . ILE A 46  ? 0.6632 0.7192 0.7975 0.0266  -0.0963 -0.0242 1263 ILE A CG2   
363  C  CD1   . ILE A 46  ? 0.8164 0.8728 0.9423 0.0341  -0.0914 -0.0269 1263 ILE A CD1   
364  N  N     . TRP A 47  ? 0.7037 0.7741 0.8444 0.0160  -0.0989 -0.0240 1264 TRP A N     
365  C  CA    . TRP A 47  ? 0.7538 0.8236 0.8955 0.0116  -0.0992 -0.0246 1264 TRP A CA    
366  C  C     . TRP A 47  ? 0.7596 0.8273 0.9033 0.0095  -0.0992 -0.0269 1264 TRP A C     
367  O  O     . TRP A 47  ? 0.7767 0.8415 0.9223 0.0070  -0.0985 -0.0282 1264 TRP A O     
368  C  CB    . TRP A 47  ? 0.7275 0.8035 0.8702 0.0093  -0.0997 -0.0230 1264 TRP A CB    
369  C  CG    . TRP A 47  ? 0.7186 0.7922 0.8595 0.0050  -0.0992 -0.0245 1264 TRP A CG    
370  C  CD1   . TRP A 47  ? 0.7070 0.7815 0.8492 0.0015  -0.0985 -0.0261 1264 TRP A CD1   
371  C  CD2   . TRP A 47  ? 0.7633 0.8320 0.8998 0.0038  -0.0983 -0.0244 1264 TRP A CD2   
372  N  NE1   . TRP A 47  ? 0.6976 0.7678 0.8359 -0.0015 -0.0970 -0.0277 1264 TRP A NE1   
373  C  CE2   . TRP A 47  ? 0.7626 0.8296 0.8970 -0.0002 -0.0967 -0.0265 1264 TRP A CE2   
374  C  CE3   . TRP A 47  ? 0.6950 0.7595 0.8287 0.0058  -0.0979 -0.0226 1264 TRP A CE3   
375  C  CZ2   . TRP A 47  ? 0.6553 0.7169 0.7839 -0.0021 -0.0941 -0.0268 1264 TRP A CZ2   
376  C  CZ3   . TRP A 47  ? 0.6493 0.7085 0.7779 0.0037  -0.0956 -0.0222 1264 TRP A CZ3   
377  C  CH2   . TRP A 47  ? 0.6722 0.7304 0.7978 -0.0002 -0.0936 -0.0244 1264 TRP A CH2   
378  N  N     . LYS A 48  ? 0.7597 0.8291 0.9035 0.0108  -0.0995 -0.0268 1265 LYS A N     
379  C  CA    . LYS A 48  ? 0.7226 0.7906 0.8689 0.0096  -0.1002 -0.0279 1265 LYS A CA    
380  C  C     . LYS A 48  ? 0.6351 0.6990 0.7824 0.0100  -0.1024 -0.0300 1265 LYS A C     
381  O  O     . LYS A 48  ? 0.6093 0.6726 0.7623 0.0081  -0.1028 -0.0310 1265 LYS A O     
382  C  CB    . LYS A 48  ? 0.6666 0.7364 0.8109 0.0113  -0.0999 -0.0261 1265 LYS A CB    
383  C  CG    . LYS A 48  ? 0.6747 0.7433 0.8216 0.0107  -0.1005 -0.0257 1265 LYS A CG    
384  C  CD    . LYS A 48  ? 0.6349 0.7039 0.7778 0.0127  -0.0995 -0.0229 1265 LYS A CD    
385  C  CE    . LYS A 48  ? 0.7202 0.7863 0.8616 0.0146  -0.1024 -0.0221 1265 LYS A CE    
386  N  NZ    . LYS A 48  ? 0.8366 0.9010 0.9686 0.0179  -0.1023 -0.0197 1265 LYS A NZ    
387  N  N     . ALA A 49  ? 0.5640 0.6248 0.7068 0.0123  -0.1037 -0.0311 1266 ALA A N     
388  C  CA    . ALA A 49  ? 0.6349 0.6912 0.7792 0.0116  -0.1066 -0.0339 1266 ALA A CA    
389  C  C     . ALA A 49  ? 0.6803 0.7351 0.8309 0.0085  -0.1048 -0.0342 1266 ALA A C     
390  O  O     . ALA A 49  ? 0.6467 0.7014 0.8048 0.0061  -0.1060 -0.0356 1266 ALA A O     
391  C  CB    . ALA A 49  ? 0.4650 0.5159 0.6016 0.0144  -0.1077 -0.0359 1266 ALA A CB    
392  N  N     . ILE A 50  ? 0.6030 0.6569 0.7509 0.0088  -0.1018 -0.0324 1267 ILE A N     
393  C  CA    . ILE A 50  ? 0.6807 0.7319 0.8317 0.0062  -0.0991 -0.0318 1267 ILE A CA    
394  C  C     . ILE A 50  ? 0.6827 0.7368 0.8393 0.0033  -0.0970 -0.0318 1267 ILE A C     
395  O  O     . ILE A 50  ? 0.7728 0.8255 0.9367 0.0010  -0.0954 -0.0327 1267 ILE A O     
396  C  CB    . ILE A 50  ? 0.7878 0.8379 0.9330 0.0076  -0.0970 -0.0288 1267 ILE A CB    
397  C  CG1   . ILE A 50  ? 0.7620 0.8079 0.9035 0.0113  -0.0978 -0.0285 1267 ILE A CG1   
398  C  CG2   . ILE A 50  ? 0.7426 0.7891 0.8879 0.0050  -0.0935 -0.0273 1267 ILE A CG2   
399  C  CD1   . ILE A 50  ? 0.7612 0.8088 0.8985 0.0144  -0.0970 -0.0245 1267 ILE A CD1   
400  N  N     . ARG A 51  ? 0.7357 0.7937 0.8901 0.0035  -0.0964 -0.0310 1268 ARG A N     
401  C  CA    . ARG A 51  ? 0.6699 0.7289 0.8284 0.0013  -0.0936 -0.0316 1268 ARG A CA    
402  C  C     . ARG A 51  ? 0.6899 0.7502 0.8583 0.0012  -0.0947 -0.0327 1268 ARG A C     
403  O  O     . ARG A 51  ? 0.6316 0.6915 0.8076 -0.0004 -0.0914 -0.0333 1268 ARG A O     
404  C  CB    . ARG A 51  ? 0.7706 0.8321 0.9251 0.0011  -0.0934 -0.0311 1268 ARG A CB    
405  C  CG    . ARG A 51  ? 0.8610 0.9218 1.0196 -0.0005 -0.0905 -0.0322 1268 ARG A CG    
406  C  CD    . ARG A 51  ? 0.8207 0.8831 0.9775 -0.0008 -0.0912 -0.0319 1268 ARG A CD    
407  N  NE    . ARG A 51  ? 0.8540 0.9181 1.0147 0.0018  -0.0937 -0.0306 1268 ARG A NE    
408  C  CZ    . ARG A 51  ? 0.8518 0.9171 1.0110 0.0022  -0.0942 -0.0291 1268 ARG A CZ    
409  N  NH1   . ARG A 51  ? 0.8404 0.9064 0.9967 -0.0003 -0.0929 -0.0292 1268 ARG A NH1   
410  N  NH2   . ARG A 51  ? 0.9067 0.9723 1.0670 0.0049  -0.0963 -0.0272 1268 ARG A NH2   
411  N  N     . ASN A 52  ? 0.6668 0.7289 0.8354 0.0034  -0.0994 -0.0328 1269 ASN A N     
412  C  CA    . ASN A 52  ? 0.6066 0.6711 0.7843 0.0038  -0.1023 -0.0333 1269 ASN A CA    
413  C  C     . ASN A 52  ? 0.7295 0.7937 0.9160 0.0019  -0.1035 -0.0348 1269 ASN A C     
414  O  O     . ASN A 52  ? 0.8057 0.8731 1.0049 0.0009  -0.1027 -0.0348 1269 ASN A O     
415  C  CB    . ASN A 52  ? 0.5815 0.6467 0.7536 0.0066  -0.1077 -0.0327 1269 ASN A CB    
416  C  CG    . ASN A 52  ? 0.6904 0.7563 0.8584 0.0081  -0.1060 -0.0304 1269 ASN A CG    
417  O  OD1   . ASN A 52  ? 0.7294 0.7951 0.8986 0.0066  -0.1015 -0.0299 1269 ASN A OD1   
418  N  ND2   . ASN A 52  ? 0.7716 0.8374 0.9337 0.0107  -0.1093 -0.0290 1269 ASN A ND2   
419  N  N     . TRP A 53  ? 0.7672 0.8276 0.9489 0.0012  -0.1048 -0.0360 1270 TRP A N     
420  C  CA    . TRP A 53  ? 0.7044 0.7636 0.8952 -0.0016 -0.1057 -0.0377 1270 TRP A CA    
421  C  C     . TRP A 53  ? 0.7000 0.7595 0.8995 -0.0042 -0.0986 -0.0365 1270 TRP A C     
422  O  O     . TRP A 53  ? 0.6492 0.7125 0.8636 -0.0062 -0.0980 -0.0368 1270 TRP A O     
423  C  CB    . TRP A 53  ? 0.6032 0.6557 0.7856 -0.0015 -0.1071 -0.0392 1270 TRP A CB    
424  C  CG    . TRP A 53  ? 0.5641 0.6137 0.7557 -0.0052 -0.1084 -0.0414 1270 TRP A CG    
425  C  CD1   . TRP A 53  ? 0.4705 0.5196 0.6658 -0.0067 -0.1155 -0.0449 1270 TRP A CD1   
426  C  CD2   . TRP A 53  ? 0.5575 0.6038 0.7559 -0.0085 -0.1024 -0.0401 1270 TRP A CD2   
427  N  NE1   . TRP A 53  ? 0.6409 0.6874 0.8473 -0.0113 -0.1146 -0.0464 1270 TRP A NE1   
428  C  CE2   . TRP A 53  ? 0.6102 0.6548 0.8189 -0.0123 -0.1059 -0.0430 1270 TRP A CE2   
429  C  CE3   . TRP A 53  ? 0.5966 0.6409 0.7924 -0.0088 -0.0945 -0.0368 1270 TRP A CE3   
430  C  CZ2   . TRP A 53  ? 0.5979 0.6386 0.8159 -0.0166 -0.1006 -0.0422 1270 TRP A CZ2   
431  C  CZ3   . TRP A 53  ? 0.7411 0.7811 0.9437 -0.0122 -0.0892 -0.0356 1270 TRP A CZ3   
432  C  CH2   . TRP A 53  ? 0.7141 0.7524 0.9287 -0.0162 -0.0917 -0.0380 1270 TRP A CH2   
433  N  N     . PHE A 54  ? 0.6796 0.7356 0.8699 -0.0040 -0.0931 -0.0348 1271 PHE A N     
434  C  CA    . PHE A 54  ? 0.6939 0.7480 0.8879 -0.0063 -0.0854 -0.0336 1271 PHE A CA    
435  C  C     . PHE A 54  ? 0.6955 0.7539 0.8984 -0.0063 -0.0817 -0.0337 1271 PHE A C     
436  O  O     . PHE A 54  ? 0.5772 0.6364 0.7909 -0.0081 -0.0759 -0.0334 1271 PHE A O     
437  C  CB    . PHE A 54  ? 0.5501 0.5991 0.7292 -0.0058 -0.0819 -0.0316 1271 PHE A CB    
438  C  CG    . PHE A 54  ? 0.6117 0.6569 0.7896 -0.0079 -0.0737 -0.0300 1271 PHE A CG    
439  C  CD1   . PHE A 54  ? 0.6064 0.6473 0.7887 -0.0100 -0.0699 -0.0286 1271 PHE A CD1   
440  C  CD2   . PHE A 54  ? 0.6184 0.6634 0.7906 -0.0079 -0.0691 -0.0303 1271 PHE A CD2   
441  C  CE1   . PHE A 54  ? 0.6571 0.6935 0.8365 -0.0117 -0.0610 -0.0264 1271 PHE A CE1   
442  C  CE2   . PHE A 54  ? 0.5947 0.6348 0.7625 -0.0095 -0.0607 -0.0291 1271 PHE A CE2   
443  C  CZ    . PHE A 54  ? 0.6630 0.6990 0.8341 -0.0113 -0.0563 -0.0268 1271 PHE A CZ    
444  N  N     . ASP A 55  ? 0.7510 0.8117 0.9501 -0.0040 -0.0840 -0.0340 1272 ASP A N     
445  C  CA    . ASP A 55  ? 0.8033 0.8665 1.0112 -0.0033 -0.0802 -0.0341 1272 ASP A CA    
446  C  C     . ASP A 55  ? 0.7970 0.8665 1.0238 -0.0030 -0.0828 -0.0340 1272 ASP A C     
447  O  O     . ASP A 55  ? 0.9656 1.0374 1.2053 -0.0031 -0.0769 -0.0336 1272 ASP A O     
448  C  CB    . ASP A 55  ? 0.7565 0.8196 0.9574 -0.0011 -0.0823 -0.0340 1272 ASP A CB    
449  C  CG    . ASP A 55  ? 0.6443 0.7072 0.8526 -0.0001 -0.0770 -0.0343 1272 ASP A CG    
450  O  OD1   . ASP A 55  ? 0.5203 0.5780 0.7206 -0.0013 -0.0706 -0.0356 1272 ASP A OD1   
451  O  OD2   . ASP A 55  ? 0.6727 0.7403 0.8949 0.0021  -0.0794 -0.0332 1272 ASP A OD2   
452  N  N     . ALA A 56  ? 0.6970 0.7696 0.9258 -0.0023 -0.0918 -0.0343 1273 ALA A N     
453  C  CA    . ALA A 56  ? 0.7166 0.7964 0.9638 -0.0024 -0.0964 -0.0342 1273 ALA A CA    
454  C  C     . ALA A 56  ? 0.8361 0.9174 1.0972 -0.0062 -0.0914 -0.0345 1273 ALA A C     
455  O  O     . ALA A 56  ? 0.8550 0.9429 1.1355 -0.0063 -0.0888 -0.0336 1273 ALA A O     
456  C  CB    . ALA A 56  ? 0.7473 0.8282 0.9899 -0.0019 -0.1075 -0.0353 1273 ALA A CB    
457  N  N     . GLU A 57  ? 0.7443 0.8193 0.9967 -0.0090 -0.0890 -0.0353 1274 GLU A N     
458  C  CA    . GLU A 57  ? 0.5982 0.6727 0.8623 -0.0130 -0.0828 -0.0348 1274 GLU A CA    
459  C  C     . GLU A 57  ? 0.5357 0.6107 0.8059 -0.0126 -0.0710 -0.0331 1274 GLU A C     
460  O  O     . GLU A 57  ? 0.6324 0.7130 0.9230 -0.0144 -0.0664 -0.0323 1274 GLU A O     
461  C  CB    . GLU A 57  ? 0.7294 0.7946 0.9795 -0.0150 -0.0813 -0.0349 1274 GLU A CB    
462  C  CG    . GLU A 57  ? 0.7866 0.8495 1.0341 -0.0162 -0.0908 -0.0374 1274 GLU A CG    
463  C  CD    . GLU A 57  ? 0.9034 0.9730 1.1709 -0.0196 -0.0973 -0.0395 1274 GLU A CD    
464  O  OE1   . GLU A 57  ? 0.9655 1.0409 1.2529 -0.0224 -0.0925 -0.0384 1274 GLU A OE1   
465  O  OE2   . GLU A 57  ? 0.9109 0.9803 1.1744 -0.0194 -0.1073 -0.0425 1274 GLU A OE2   
466  N  N     . ILE A 58  ? 0.6135 0.6821 0.8663 -0.0108 -0.0653 -0.0327 1275 ILE A N     
467  C  CA    . ILE A 58  ? 0.6967 0.7631 0.9517 -0.0108 -0.0531 -0.0319 1275 ILE A CA    
468  C  C     . ILE A 58  ? 0.8187 0.8915 1.0892 -0.0079 -0.0509 -0.0322 1275 ILE A C     
469  O  O     . ILE A 58  ? 0.6768 0.7497 0.9566 -0.0077 -0.0401 -0.0317 1275 ILE A O     
470  C  CB    . ILE A 58  ? 0.6462 0.7031 0.8769 -0.0104 -0.0481 -0.0320 1275 ILE A CB    
471  C  CG1   . ILE A 58  ? 0.6344 0.6908 0.8538 -0.0077 -0.0536 -0.0336 1275 ILE A CG1   
472  C  CG2   . ILE A 58  ? 0.5758 0.6266 0.7932 -0.0124 -0.0494 -0.0305 1275 ILE A CG2   
473  C  CD1   . ILE A 58  ? 0.4406 0.4888 0.6380 -0.0081 -0.0496 -0.0342 1275 ILE A CD1   
474  N  N     . THR A 59  ? 0.9471 1.0244 1.2201 -0.0050 -0.0598 -0.0325 1276 THR A N     
475  C  CA    . THR A 59  ? 1.0887 1.1722 1.3794 -0.0017 -0.0576 -0.0317 1276 THR A CA    
476  C  C     . THR A 59  ? 0.9105 1.0052 1.2283 -0.0027 -0.0607 -0.0303 1276 THR A C     
477  O  O     . THR A 59  ? 0.7936 0.8937 1.1311 -0.0012 -0.0534 -0.0291 1276 THR A O     
478  C  CB    . THR A 59  ? 1.0270 1.1103 1.3110 0.0022  -0.0647 -0.0315 1276 THR A CB    
479  O  OG1   . THR A 59  ? 1.2351 1.3225 1.5179 0.0021  -0.0774 -0.0310 1276 THR A OG1   
480  C  CG2   . THR A 59  ? 0.8860 0.9589 1.1458 0.0020  -0.0613 -0.0331 1276 THR A CG2   
481  N  N     . ARG A 60  ? 0.6325 0.7307 0.9525 -0.0056 -0.0709 -0.0308 1277 ARG A N     
482  C  CA    . ARG A 60  ? 0.7164 0.8250 1.0627 -0.0083 -0.0738 -0.0302 1277 ARG A CA    
483  C  C     . ARG A 60  ? 0.6730 0.7807 1.0302 -0.0113 -0.0600 -0.0293 1277 ARG A C     
484  O  O     . ARG A 60  ? 0.5744 0.6923 0.9588 -0.0127 -0.0576 -0.0279 1277 ARG A O     
485  C  CB    . ARG A 60  ? 0.7292 0.8384 1.0726 -0.0121 -0.0862 -0.0321 1277 ARG A CB    
486  C  CG    . ARG A 60  ? 0.8911 1.0097 1.2612 -0.0171 -0.0892 -0.0324 1277 ARG A CG    
487  C  CD    . ARG A 60  ? 1.0365 1.1567 1.4058 -0.0205 -0.1044 -0.0354 1277 ARG A CD    
488  N  NE    . ARG A 60  ? 1.2884 1.3963 1.6373 -0.0238 -0.1048 -0.0380 1277 ARG A NE    
489  C  CZ    . ARG A 60  ? 1.4359 1.5411 1.7793 -0.0268 -0.1160 -0.0416 1277 ARG A CZ    
490  N  NH1   . ARG A 60  ? 1.4847 1.5992 1.8402 -0.0274 -0.1288 -0.0433 1277 ARG A NH1   
491  N  NH2   . ARG A 60  ? 1.4080 1.5008 1.7334 -0.0289 -0.1145 -0.0437 1277 ARG A NH2   
492  N  N     . LEU A 61  ? 0.6870 0.7831 1.0233 -0.0125 -0.0509 -0.0296 1278 LEU A N     
493  C  CA    . LEU A 61  ? 0.6621 0.7555 1.0047 -0.0149 -0.0364 -0.0281 1278 LEU A CA    
494  C  C     . LEU A 61  ? 0.7353 0.8295 1.0849 -0.0110 -0.0242 -0.0275 1278 LEU A C     
495  O  O     . LEU A 61  ? 0.6204 0.7161 0.9838 -0.0124 -0.0116 -0.0259 1278 LEU A O     
496  C  CB    . LEU A 61  ? 0.8033 0.8833 1.1191 -0.0172 -0.0319 -0.0280 1278 LEU A CB    
497  C  CG    . LEU A 61  ? 0.8174 0.8975 1.1390 -0.0222 -0.0379 -0.0278 1278 LEU A CG    
498  C  CD1   . LEU A 61  ? 0.5330 0.6004 0.8299 -0.0236 -0.0365 -0.0270 1278 LEU A CD1   
499  C  CD2   . LEU A 61  ? 0.8833 0.9704 1.2331 -0.0262 -0.0301 -0.0259 1278 LEU A CD2   
500  N  N     . GLY A 62  ? 0.7209 0.8134 1.0618 -0.0062 -0.0264 -0.0286 1279 GLY A N     
501  C  CA    . GLY A 62  ? 0.5500 0.6402 0.8947 -0.0022 -0.0141 -0.0288 1279 GLY A CA    
502  C  C     . GLY A 62  ? 0.6429 0.7183 0.9574 -0.0015 -0.0067 -0.0313 1279 GLY A C     
503  O  O     . GLY A 62  ? 0.7259 0.7961 1.0398 0.0009  0.0061  -0.0324 1279 GLY A O     
504  N  N     . VAL A 63  ? 0.6392 0.7075 0.9290 -0.0037 -0.0139 -0.0324 1280 VAL A N     
505  C  CA    . VAL A 63  ? 0.6287 0.6849 0.8909 -0.0032 -0.0108 -0.0350 1280 VAL A CA    
506  C  C     . VAL A 63  ? 0.6150 0.6717 0.8767 0.0003  -0.0171 -0.0365 1280 VAL A C     
507  O  O     . VAL A 63  ? 0.6357 0.7012 0.9121 0.0021  -0.0266 -0.0349 1280 VAL A O     
508  C  CB    . VAL A 63  ? 0.6669 0.7175 0.9066 -0.0065 -0.0169 -0.0347 1280 VAL A CB    
509  C  CG1   . VAL A 63  ? 0.6795 0.7184 0.8913 -0.0070 -0.0130 -0.0370 1280 VAL A CG1   
510  C  CG2   . VAL A 63  ? 0.6237 0.6746 0.8684 -0.0098 -0.0126 -0.0320 1280 VAL A CG2   
511  N  N     . LYS A 64  ? 0.5751 0.6215 0.8194 0.0011  -0.0114 -0.0396 1281 LYS A N     
512  C  CA    . LYS A 64  ? 0.6640 0.7084 0.9071 0.0039  -0.0156 -0.0411 1281 LYS A CA    
513  C  C     . LYS A 64  ? 0.7021 0.7374 0.9187 0.0013  -0.0197 -0.0439 1281 LYS A C     
514  O  O     . LYS A 64  ? 0.6881 0.7156 0.8855 -0.0016 -0.0152 -0.0461 1281 LYS A O     
515  C  CB    . LYS A 64  ? 0.6875 0.7278 0.9412 0.0078  -0.0038 -0.0426 1281 LYS A CB    
516  C  CG    . LYS A 64  ? 0.6826 0.7350 0.9680 0.0123  -0.0045 -0.0389 1281 LYS A CG    
517  C  CD    . LYS A 64  ? 0.7576 0.8076 1.0562 0.0157  0.0111  -0.0398 1281 LYS A CD    
518  C  CE    . LYS A 64  ? 0.8842 0.9495 1.2178 0.0192  0.0108  -0.0353 1281 LYS A CE    
519  N  NZ    . LYS A 64  ? 0.9732 1.0446 1.3220 0.0244  0.0019  -0.0324 1281 LYS A NZ    
520  N  N     . GLU A 65  ? 0.5167 0.5533 0.7329 0.0025  -0.0284 -0.0436 1282 GLU A N     
521  C  CA    . GLU A 65  ? 0.5235 0.5544 0.7196 -0.0003 -0.0337 -0.0456 1282 GLU A CA    
522  C  C     . GLU A 65  ? 0.6417 0.6613 0.8285 -0.0007 -0.0272 -0.0501 1282 GLU A C     
523  O  O     . GLU A 65  ? 0.6713 0.6889 0.8701 0.0028  -0.0233 -0.0501 1282 GLU A O     
524  C  CB    . GLU A 65  ? 0.4344 0.4719 0.6343 0.0007  -0.0452 -0.0427 1282 GLU A CB    
525  C  CG    . GLU A 65  ? 0.5985 0.6339 0.7803 -0.0028 -0.0515 -0.0437 1282 GLU A CG    
526  C  CD    . GLU A 65  ? 0.6588 0.7011 0.8435 -0.0017 -0.0613 -0.0404 1282 GLU A CD    
527  O  OE1   . GLU A 65  ? 0.6939 0.7421 0.8917 0.0014  -0.0646 -0.0376 1282 GLU A OE1   
528  O  OE2   . GLU A 65  ? 0.7542 0.7961 0.9280 -0.0039 -0.0657 -0.0407 1282 GLU A OE2   
529  N  N     . CYS A 66  ? 0.5941 0.6059 0.7595 -0.0048 -0.0267 -0.0538 1283 CYS A N     
530  C  CA    . CYS A 66  ? 0.7939 0.7933 0.9470 -0.0067 -0.0216 -0.0593 1283 CYS A CA    
531  C  C     . CYS A 66  ? 0.8079 0.8054 0.9431 -0.0118 -0.0299 -0.0614 1283 CYS A C     
532  O  O     . CYS A 66  ? 0.6890 0.6953 0.8236 -0.0128 -0.0388 -0.0578 1283 CYS A O     
533  C  CB    . CYS A 66  ? 0.7600 0.7498 0.9052 -0.0065 -0.0088 -0.0632 1283 CYS A CB    
534  S  SG    . CYS A 66  ? 0.9098 0.8961 1.0299 -0.0110 -0.0088 -0.0644 1283 CYS A SG    
535  N  N     . TYR A 67  ? 0.6488 0.6349 0.7707 -0.0151 -0.0271 -0.0673 1284 TYR A N     
536  C  CA    . TYR A 67  ? 0.7043 0.6893 0.8107 -0.0208 -0.0353 -0.0698 1284 TYR A CA    
537  C  C     . TYR A 67  ? 0.7583 0.7287 0.8447 -0.0253 -0.0306 -0.0778 1284 TYR A C     
538  O  O     . TYR A 67  ? 0.9364 0.8960 1.0240 -0.0255 -0.0247 -0.0824 1284 TYR A O     
539  C  CB    . TYR A 67  ? 0.6226 0.6122 0.7390 -0.0217 -0.0426 -0.0678 1284 TYR A CB    
540  C  CG    . TYR A 67  ? 0.8941 0.8863 0.9988 -0.0276 -0.0516 -0.0693 1284 TYR A CG    
541  C  CD1   . TYR A 67  ? 0.8989 0.9025 1.0018 -0.0276 -0.0594 -0.0649 1284 TYR A CD1   
542  C  CD2   . TYR A 67  ? 0.8922 0.8752 0.9881 -0.0332 -0.0522 -0.0753 1284 TYR A CD2   
543  C  CE1   . TYR A 67  ? 0.8508 0.8585 0.9458 -0.0324 -0.0678 -0.0657 1284 TYR A CE1   
544  C  CE2   . TYR A 67  ? 0.7875 0.7748 0.8754 -0.0390 -0.0612 -0.0766 1284 TYR A CE2   
545  C  CZ    . TYR A 67  ? 0.9247 0.9252 1.0131 -0.0383 -0.0691 -0.0714 1284 TYR A CZ    
546  O  OH    . TYR A 67  ? 1.1315 1.1378 1.2145 -0.0436 -0.0782 -0.0722 1284 TYR A OH    
547  N  N     . PHE A 68  ? 0.6796 0.6487 0.7465 -0.0287 -0.0334 -0.0794 1285 PHE A N     
548  C  CA    . PHE A 68  ? 0.8208 0.7767 0.8641 -0.0339 -0.0319 -0.0872 1285 PHE A CA    
549  C  C     . PHE A 68  ? 0.9046 0.8638 0.9416 -0.0402 -0.0443 -0.0892 1285 PHE A C     
550  O  O     . PHE A 68  ? 0.8974 0.8704 0.9458 -0.0399 -0.0534 -0.0834 1285 PHE A O     
551  C  CB    . PHE A 68  ? 0.9044 0.8570 0.9284 -0.0337 -0.0285 -0.0869 1285 PHE A CB    
552  C  CG    . PHE A 68  ? 0.8519 0.7971 0.8777 -0.0292 -0.0136 -0.0873 1285 PHE A CG    
553  C  CD1   . PHE A 68  ? 0.7008 0.6554 0.7509 -0.0236 -0.0093 -0.0812 1285 PHE A CD1   
554  C  CD2   . PHE A 68  ? 0.8761 0.8052 0.8797 -0.0306 -0.0038 -0.0941 1285 PHE A CD2   
555  C  CE1   . PHE A 68  ? 0.7643 0.7142 0.8200 -0.0195 0.0045  -0.0811 1285 PHE A CE1   
556  C  CE2   . PHE A 68  ? 0.7659 0.6887 0.7729 -0.0260 0.0116  -0.0941 1285 PHE A CE2   
557  C  CZ    . PHE A 68  ? 0.7113 0.6453 0.7461 -0.0205 0.0159  -0.0874 1285 PHE A CZ    
558  N  N     . PRO A 69  ? 1.0064 0.9534 1.0262 -0.0461 -0.0448 -0.0975 1286 PRO A N     
559  C  CA    . PRO A 69  ? 1.0103 0.9614 1.0291 -0.0530 -0.0566 -0.0997 1286 PRO A CA    
560  C  C     . PRO A 69  ? 0.9951 0.9589 1.0062 -0.0548 -0.0684 -0.0954 1286 PRO A C     
561  O  O     . PRO A 69  ? 0.9199 0.8841 0.9183 -0.0522 -0.0672 -0.0929 1286 PRO A O     
562  C  CB    . PRO A 69  ? 1.0079 0.9405 1.0078 -0.0592 -0.0534 -0.1108 1286 PRO A CB    
563  C  CG    . PRO A 69  ? 0.9222 0.8410 0.9214 -0.0539 -0.0377 -0.1136 1286 PRO A CG    
564  C  CD    . PRO A 69  ? 0.9592 0.8872 0.9624 -0.0470 -0.0337 -0.1059 1286 PRO A CD    
565  N  N     . ILE A 70  ? 1.0073 0.9815 1.0274 -0.0592 -0.0794 -0.0941 1287 ILE A N     
566  C  CA    . ILE A 70  ? 0.9705 0.9580 0.9864 -0.0607 -0.0916 -0.0899 1287 ILE A CA    
567  C  C     . ILE A 70  ? 0.9782 0.9586 0.9681 -0.0668 -0.0977 -0.0961 1287 ILE A C     
568  O  O     . ILE A 70  ? 1.0958 1.0850 1.0775 -0.0666 -0.1066 -0.0920 1287 ILE A O     
569  C  CB    . ILE A 70  ? 0.9412 0.9433 0.9773 -0.0632 -0.1004 -0.0862 1287 ILE A CB    
570  C  CG1   . ILE A 70  ? 0.8917 0.9100 0.9292 -0.0620 -0.1112 -0.0796 1287 ILE A CG1   
571  C  CG2   . ILE A 70  ? 0.9245 0.9210 0.9585 -0.0724 -0.1050 -0.0939 1287 ILE A CG2   
572  C  CD1   . ILE A 70  ? 0.9170 0.9436 0.9640 -0.0535 -0.1082 -0.0710 1287 ILE A CD1   
573  N  N     . PHE A 71  ? 0.9297 0.8933 0.9052 -0.0719 -0.0932 -0.1059 1288 PHE A N     
574  C  CA    . PHE A 71  ? 0.9893 0.9442 0.9374 -0.0786 -0.0999 -0.1134 1288 PHE A CA    
575  C  C     . PHE A 71  ? 0.9160 0.8548 0.8395 -0.0751 -0.0887 -0.1164 1288 PHE A C     
576  O  O     . PHE A 71  ? 0.9340 0.8638 0.8634 -0.0703 -0.0745 -0.1172 1288 PHE A O     
577  C  CB    . PHE A 71  ? 1.0793 1.0240 1.0253 -0.0879 -0.1027 -0.1238 1288 PHE A CB    
578  C  CG    . PHE A 71  ? 1.0880 1.0482 1.0566 -0.0929 -0.1139 -0.1212 1288 PHE A CG    
579  C  CD1   . PHE A 71  ? 1.1394 1.1160 1.1083 -0.0960 -0.1290 -0.1174 1288 PHE A CD1   
580  C  CD2   . PHE A 71  ? 1.0441 1.0030 1.0349 -0.0939 -0.1088 -0.1216 1288 PHE A CD2   
581  C  CE1   . PHE A 71  ? 1.1287 1.1209 1.1211 -0.1004 -0.1381 -0.1146 1288 PHE A CE1   
582  C  CE2   . PHE A 71  ? 1.0393 1.0124 1.0515 -0.0986 -0.1175 -0.1185 1288 PHE A CE2   
583  C  CZ    . PHE A 71  ? 1.0227 1.0129 1.0366 -0.1020 -0.1318 -0.1152 1288 PHE A CZ    
584  N  N     . VAL A 72  ? 0.9307 0.8666 0.8272 -0.0772 -0.0950 -0.1176 1289 VAL A N     
585  C  CA    . VAL A 72  ? 1.0416 0.9616 0.9101 -0.0744 -0.0847 -0.1201 1289 VAL A CA    
586  C  C     . VAL A 72  ? 1.0944 1.0006 0.9291 -0.0823 -0.0913 -0.1303 1289 VAL A C     
587  O  O     . VAL A 72  ? 0.9401 0.8554 0.7710 -0.0883 -0.1080 -0.1309 1289 VAL A O     
588  C  CB    . VAL A 72  ? 0.9673 0.8966 0.8335 -0.0675 -0.0843 -0.1089 1289 VAL A CB    
589  C  CG1   . VAL A 72  ? 0.9417 0.8539 0.7771 -0.0651 -0.0729 -0.1109 1289 VAL A CG1   
590  C  CG2   . VAL A 72  ? 0.9025 0.8429 0.8001 -0.0606 -0.0775 -0.1007 1289 VAL A CG2   
591  N  N     . SER A 73  ? 1.2012 1.0854 1.0129 -0.0825 -0.0782 -0.1388 1290 SER A N     
592  C  CA    . SER A 73  ? 1.1457 1.0136 0.9206 -0.0899 -0.0833 -0.1497 1290 SER A CA    
593  C  C     . SER A 73  ? 1.2273 1.0992 0.9751 -0.0894 -0.0934 -0.1444 1290 SER A C     
594  O  O     . SER A 73  ? 1.3428 1.2227 1.0937 -0.0820 -0.0894 -0.1333 1290 SER A O     
595  C  CB    . SER A 73  ? 1.1610 1.0033 0.9162 -0.0884 -0.0642 -0.1592 1290 SER A CB    
596  O  OG    . SER A 73  ? 1.3159 1.1429 1.0281 -0.0913 -0.0653 -0.1650 1290 SER A OG    
597  N  N     . ARG A 74  ? 1.2436 1.1104 0.9655 -0.0978 -0.1076 -0.1520 1291 ARG A N     
598  C  CA    . ARG A 74  ? 1.2523 1.1175 0.9401 -0.0975 -0.1163 -0.1486 1291 ARG A CA    
599  C  C     . ARG A 74  ? 1.3773 1.2238 1.0377 -0.0911 -0.0973 -0.1480 1291 ARG A C     
600  O  O     . ARG A 74  ? 1.4933 1.3431 1.1400 -0.0857 -0.0973 -0.1380 1291 ARG A O     
601  C  CB    . ARG A 74  ? 1.2205 1.0782 0.8805 -0.1084 -0.1327 -0.1599 1291 ARG A CB    
602  N  N     . ALA A 75  ? 1.3415 1.1676 0.9944 -0.0914 -0.0801 -0.1582 1292 ALA A N     
603  C  CA    . ALA A 75  ? 1.2875 1.0947 0.9151 -0.0856 -0.0599 -0.1587 1292 ALA A CA    
604  C  C     . ALA A 75  ? 1.3189 1.1370 0.9751 -0.0758 -0.0459 -0.1461 1292 ALA A C     
605  O  O     . ALA A 75  ? 1.3357 1.1496 0.9755 -0.0704 -0.0368 -0.1390 1292 ALA A O     
606  C  CB    . ALA A 75  ? 1.1212 0.9035 0.7348 -0.0885 -0.0451 -0.1739 1292 ALA A CB    
607  N  N     . ALA A 76  ? 1.2876 1.1182 0.9858 -0.0736 -0.0432 -0.1435 1293 ALA A N     
608  C  CA    . ALA A 76  ? 1.2095 1.0524 0.9363 -0.0651 -0.0331 -0.1316 1293 ALA A CA    
609  C  C     . ALA A 76  ? 1.2420 1.0992 0.9657 -0.0625 -0.0438 -0.1191 1293 ALA A C     
610  O  O     . ALA A 76  ? 1.2507 1.1072 0.9720 -0.0565 -0.0332 -0.1108 1293 ALA A O     
611  C  CB    . ALA A 76  ? 1.1290 0.9855 0.8994 -0.0640 -0.0339 -0.1301 1293 ALA A CB    
612  N  N     . LEU A 77  ? 1.2550 1.1238 0.9767 -0.0671 -0.0646 -0.1179 1294 LEU A N     
613  C  CA    . LEU A 77  ? 1.2103 1.0938 0.9324 -0.0642 -0.0764 -0.1057 1294 LEU A CA    
614  C  C     . LEU A 77  ? 1.3684 1.2386 1.0486 -0.0628 -0.0741 -0.1031 1294 LEU A C     
615  O  O     . LEU A 77  ? 1.4270 1.2983 1.1061 -0.0566 -0.0667 -0.0925 1294 LEU A O     
616  C  CB    . LEU A 77  ? 1.0885 0.9882 0.8215 -0.0696 -0.0987 -0.1059 1294 LEU A CB    
617  C  CG    . LEU A 77  ? 1.0966 1.0180 0.8479 -0.0661 -0.1126 -0.0934 1294 LEU A CG    
618  C  CD1   . LEU A 77  ? 1.2870 1.2045 1.0077 -0.0629 -0.1168 -0.0855 1294 LEU A CD1   
619  C  CD2   . LEU A 77  ? 0.8543 0.7881 0.6439 -0.0596 -0.1043 -0.0853 1294 LEU A CD2   
620  N  N     . GLU A 78  ? 1.4231 1.2799 1.0677 -0.0690 -0.0810 -0.1125 1295 GLU A N     
621  C  CA    . GLU A 78  ? 1.5361 1.3808 1.1368 -0.0683 -0.0827 -0.1098 1295 GLU A CA    
622  C  C     . GLU A 78  ? 1.6747 1.4956 1.2476 -0.0653 -0.0595 -0.1135 1295 GLU A C     
623  O  O     . GLU A 78  ? 1.7837 1.5958 1.3255 -0.0622 -0.0561 -0.1070 1295 GLU A O     
624  C  CB    . GLU A 78  ? 1.5629 1.4047 1.1360 -0.0767 -0.1029 -0.1183 1295 GLU A CB    
625  C  CG    . GLU A 78  ? 1.5493 1.4165 1.1519 -0.0795 -0.1254 -0.1136 1295 GLU A CG    
626  C  CD    . GLU A 78  ? 1.6180 1.4890 1.1931 -0.0843 -0.1483 -0.1135 1295 GLU A CD    
627  O  OE1   . GLU A 78  ? 1.6113 1.4699 1.1463 -0.0823 -0.1482 -0.1103 1295 GLU A OE1   
628  O  OE2   . GLU A 78  ? 1.6492 1.5362 1.2436 -0.0901 -0.1665 -0.1160 1295 GLU A OE2   
629  N  N     . ARG A 79  ? 1.7858 1.5958 1.3684 -0.0658 -0.0431 -0.1231 1296 ARG A N     
630  C  CA    . ARG A 79  ? 1.8779 1.6672 1.4384 -0.0619 -0.0193 -0.1255 1296 ARG A CA    
631  C  C     . ARG A 79  ? 1.9333 1.7315 1.5140 -0.0539 -0.0072 -0.1110 1296 ARG A C     
632  O  O     . ARG A 79  ? 1.9618 1.7786 1.5849 -0.0513 -0.0094 -0.1044 1296 ARG A O     
633  C  CB    . ARG A 79  ? 1.8653 1.6425 1.4375 -0.0628 -0.0035 -0.1378 1296 ARG A CB    
634  N  N     . GLU A 80  ? 1.9530 1.7374 1.5022 -0.0506 0.0050  -0.1060 1297 GLU A N     
635  C  CA    . GLU A 80  ? 1.9319 1.7221 1.4983 -0.0438 0.0184  -0.0926 1297 GLU A CA    
636  C  C     . GLU A 80  ? 1.8111 1.6230 1.4009 -0.0422 0.0009  -0.0799 1297 GLU A C     
637  O  O     . GLU A 80  ? 1.7748 1.6021 1.4059 -0.0392 0.0031  -0.0740 1297 GLU A O     
638  C  CB    . GLU A 80  ? 2.0077 1.8004 1.6116 -0.0406 0.0377  -0.0948 1297 GLU A CB    
639  C  CG    . GLU A 80  ? 2.1460 1.9171 1.7288 -0.0390 0.0620  -0.1021 1297 GLU A CG    
640  C  CD    . GLU A 80  ? 2.2457 2.0125 1.8237 -0.0337 0.0802  -0.0911 1297 GLU A CD    
641  O  OE1   . GLU A 80  ? 2.2601 2.0413 1.8556 -0.0317 0.0731  -0.0784 1297 GLU A OE1   
642  O  OE2   . GLU A 80  ? 2.2782 2.0268 1.8354 -0.0318 0.1019  -0.0951 1297 GLU A OE2   
643  N  N     . LYS A 81  ? 1.7873 1.6000 1.3497 -0.0440 -0.0172 -0.0764 1298 LYS A N     
644  C  CA    . LYS A 81  ? 1.7954 1.6289 1.3787 -0.0428 -0.0367 -0.0662 1298 LYS A CA    
645  C  C     . LYS A 81  ? 1.9295 1.7722 1.5410 -0.0364 -0.0277 -0.0526 1298 LYS A C     
646  O  O     . LYS A 81  ? 1.9374 1.7715 1.5291 -0.0327 -0.0200 -0.0429 1298 LYS A O     
647  C  CB    . LYS A 81  ? 1.7210 1.5513 1.2659 -0.0442 -0.0544 -0.0624 1298 LYS A CB    
648  N  N     . THR A 82  ? 2.0138 1.8725 1.6703 -0.0355 -0.0282 -0.0522 1299 THR A N     
649  C  CA    . THR A 82  ? 2.0306 1.8997 1.7172 -0.0304 -0.0230 -0.0405 1299 THR A CA    
650  C  C     . THR A 82  ? 2.1799 2.0524 1.8536 -0.0272 -0.0339 -0.0278 1299 THR A C     
651  O  O     . THR A 82  ? 2.2326 2.0977 1.8987 -0.0234 -0.0229 -0.0181 1299 THR A O     
652  C  CB    . THR A 82  ? 1.8276 1.7154 1.5591 -0.0306 -0.0298 -0.0423 1299 THR A CB    
653  O  OG1   . THR A 82  ? 1.7573 1.6417 1.5012 -0.0330 -0.0202 -0.0533 1299 THR A OG1   
654  C  CG2   . THR A 82  ? 1.6896 1.5868 1.4511 -0.0259 -0.0245 -0.0316 1299 THR A CG2   
655  N  N     . HIS A 83  ? 2.1582 2.0418 1.8309 -0.0286 -0.0553 -0.0274 1300 HIS A N     
656  C  CA    . HIS A 83  ? 2.1875 2.0762 1.8497 -0.0251 -0.0687 -0.0154 1300 HIS A CA    
657  C  C     . HIS A 83  ? 2.2165 2.1122 1.8650 -0.0292 -0.0905 -0.0208 1300 HIS A C     
658  O  O     . HIS A 83  ? 2.2601 2.1738 1.9361 -0.0301 -0.1046 -0.0215 1300 HIS A O     
659  C  CB    . HIS A 83  ? 2.1149 2.0184 1.8149 -0.0203 -0.0710 -0.0058 1300 HIS A CB    
660  N  N     . ILE A 84  ? 2.1790 2.0602 1.7847 -0.0323 -0.0927 -0.0253 1301 ILE A N     
661  C  CA    . ILE A 84  ? 2.0799 1.9666 1.6663 -0.0361 -0.1152 -0.0282 1301 ILE A CA    
662  C  C     . ILE A 84  ? 2.0132 1.9167 1.6163 -0.0306 -0.1302 -0.0143 1301 ILE A C     
663  O  O     . ILE A 84  ? 1.8938 1.8160 1.5198 -0.0322 -0.1474 -0.0152 1301 ILE A O     
664  C  CB    . ILE A 84  ? 2.0553 1.9214 1.5871 -0.0383 -0.1148 -0.0313 1301 ILE A CB    
665  N  N     . ALA A 85  ? 2.0841 1.9807 1.6783 -0.0238 -0.1220 -0.0010 1302 ALA A N     
666  C  CA    . ALA A 85  ? 2.0878 1.9974 1.7056 -0.0169 -0.1288 0.0130  1302 ALA A CA    
667  C  C     . ALA A 85  ? 2.0760 2.0043 1.7017 -0.0169 -0.1540 0.0154  1302 ALA A C     
668  O  O     . ALA A 85  ? 2.1050 2.0314 1.7011 -0.0201 -0.1682 0.0129  1302 ALA A O     
669  C  CB    . ALA A 85  ? 2.0043 1.9223 1.6666 -0.0150 -0.1170 0.0130  1302 ALA A CB    
670  N  N     . ASP A 86  ? 2.0355 1.9822 1.7014 -0.0134 -0.1597 0.0203  1303 ASP A N     
671  C  CA    . ASP A 86  ? 1.9849 1.9527 1.6687 -0.0142 -0.1813 0.0205  1303 ASP A CA    
672  C  C     . ASP A 86  ? 1.8314 1.8136 1.5565 -0.0175 -0.1796 0.0121  1303 ASP A C     
673  O  O     . ASP A 86  ? 1.8910 1.8919 1.6471 -0.0145 -0.1891 0.0165  1303 ASP A O     
674  C  CB    . ASP A 86  ? 2.0128 1.9899 1.7043 -0.0053 -0.1914 0.0365  1303 ASP A CB    
675  N  N     . PHE A 87  ? 1.6012 1.5746 1.3263 -0.0234 -0.1674 -0.0001 1304 PHE A N     
676  C  CA    . PHE A 87  ? 1.4326 1.4178 1.1936 -0.0267 -0.1655 -0.0080 1304 PHE A CA    
677  C  C     . PHE A 87  ? 1.3965 1.3869 1.1550 -0.0356 -0.1769 -0.0201 1304 PHE A C     
678  O  O     . PHE A 87  ? 1.3342 1.3412 1.1231 -0.0377 -0.1844 -0.0228 1304 PHE A O     
679  C  CB    . PHE A 87  ? 1.3772 1.3507 1.1466 -0.0269 -0.1440 -0.0129 1304 PHE A CB    
680  C  CG    . PHE A 87  ? 1.3881 1.3638 1.1803 -0.0199 -0.1340 -0.0035 1304 PHE A CG    
681  C  CD1   . PHE A 87  ? 1.3434 1.3358 1.1657 -0.0158 -0.1419 0.0026  1304 PHE A CD1   
682  C  CD2   . PHE A 87  ? 1.4010 1.3616 1.1851 -0.0178 -0.1157 -0.0014 1304 PHE A CD2   
683  C  CE1   . PHE A 87  ? 1.2989 1.2911 1.1405 -0.0098 -0.1325 0.0100  1304 PHE A CE1   
684  C  CE2   . PHE A 87  ? 1.3174 1.2794 1.1234 -0.0125 -0.1069 0.0064  1304 PHE A CE2   
685  C  CZ    . PHE A 87  ? 1.2208 1.1978 1.0543 -0.0086 -0.1157 0.0117  1304 PHE A CZ    
686  N  N     . ALA A 88  ? 1.4441 1.4204 1.1659 -0.0408 -0.1788 -0.0271 1305 ALA A N     
687  C  CA    . ALA A 88  ? 1.4491 1.4265 1.1663 -0.0504 -0.1880 -0.0404 1305 ALA A CA    
688  C  C     . ALA A 88  ? 1.5518 1.5526 1.2931 -0.0529 -0.2087 -0.0389 1305 ALA A C     
689  O  O     . ALA A 88  ? 1.5432 1.5507 1.3034 -0.0599 -0.2118 -0.0485 1305 ALA A O     
690  C  CB    . ALA A 88  ? 1.4359 1.3943 1.1045 -0.0547 -0.1901 -0.0464 1305 ALA A CB    
691  N  N     . PRO A 89  ? 1.5414 1.5555 1.2854 -0.0476 -0.2225 -0.0271 1306 PRO A N     
692  C  CA    . PRO A 89  ? 1.5406 1.5795 1.3147 -0.0493 -0.2402 -0.0252 1306 PRO A CA    
693  C  C     . PRO A 89  ? 1.4019 1.4540 1.2203 -0.0483 -0.2329 -0.0259 1306 PRO A C     
694  O  O     . PRO A 89  ? 1.4045 1.4740 1.2477 -0.0529 -0.2439 -0.0289 1306 PRO A O     
695  C  CB    . PRO A 89  ? 1.6012 1.6496 1.3719 -0.0405 -0.2513 -0.0098 1306 PRO A CB    
696  C  CG    . PRO A 89  ? 1.5688 1.5959 1.3106 -0.0339 -0.2365 -0.0033 1306 PRO A CG    
697  C  CD    . PRO A 89  ? 1.5642 1.5704 1.2783 -0.0411 -0.2253 -0.0161 1306 PRO A CD    
698  N  N     . GLU A 90  ? 1.3150 1.3595 1.1441 -0.0427 -0.2149 -0.0231 1307 GLU A N     
699  C  CA    . GLU A 90  ? 1.2760 1.3328 1.1447 -0.0404 -0.2089 -0.0222 1307 GLU A CA    
700  C  C     . GLU A 90  ? 1.2310 1.2817 1.1092 -0.0472 -0.1990 -0.0342 1307 GLU A C     
701  O  O     . GLU A 90  ? 1.3115 1.3641 1.2134 -0.0442 -0.1878 -0.0336 1307 GLU A O     
702  C  CB    . GLU A 90  ? 1.3020 1.3551 1.1796 -0.0308 -0.1963 -0.0125 1307 GLU A CB    
703  C  CG    . GLU A 90  ? 1.4107 1.4623 1.2726 -0.0232 -0.2013 -0.0002 1307 GLU A CG    
704  C  CD    . GLU A 90  ? 1.4977 1.5541 1.3827 -0.0140 -0.1943 0.0099  1307 GLU A CD    
705  O  OE1   . GLU A 90  ? 1.5220 1.5918 1.4189 -0.0083 -0.2051 0.0190  1307 GLU A OE1   
706  O  OE2   . GLU A 90  ? 1.4907 1.5374 1.3825 -0.0123 -0.1785 0.0085  1307 GLU A OE2   
707  N  N     . VAL A 91  ? 1.1990 1.2426 1.0607 -0.0563 -0.2035 -0.0452 1308 VAL A N     
708  C  CA    . VAL A 91  ? 1.1835 1.2167 1.0498 -0.0620 -0.1922 -0.0565 1308 VAL A CA    
709  C  C     . VAL A 91  ? 1.1356 1.1803 1.0201 -0.0706 -0.2031 -0.0636 1308 VAL A C     
710  O  O     . VAL A 91  ? 1.1933 1.2407 1.0643 -0.0774 -0.2177 -0.0679 1308 VAL A O     
711  C  CB    . VAL A 91  ? 1.1683 1.1776 0.9975 -0.0652 -0.1837 -0.0645 1308 VAL A CB    
712  C  CG1   . VAL A 91  ? 1.0302 1.0279 0.8659 -0.0701 -0.1709 -0.0759 1308 VAL A CG1   
713  C  CG2   . VAL A 91  ? 1.1470 1.1458 0.9586 -0.0570 -0.1729 -0.0562 1308 VAL A CG2   
714  N  N     . ALA A 92  ? 1.0536 1.1043 0.9680 -0.0708 -0.1958 -0.0651 1309 ALA A N     
715  C  CA    . ALA A 92  ? 1.1336 1.1949 1.0690 -0.0789 -0.2036 -0.0709 1309 ALA A CA    
716  C  C     . ALA A 92  ? 1.1274 1.1704 1.0450 -0.0881 -0.1998 -0.0845 1309 ALA A C     
717  O  O     . ALA A 92  ? 1.1128 1.1398 1.0254 -0.0866 -0.1842 -0.0889 1309 ALA A O     
718  C  CB    . ALA A 92  ? 1.1067 1.1787 1.0775 -0.0752 -0.1957 -0.0668 1309 ALA A CB    
719  N  N     . TRP A 93  ? 1.0771 1.1229 0.9872 -0.0976 -0.2141 -0.0914 1310 TRP A N     
720  C  CA    . TRP A 93  ? 1.1760 1.2025 1.0647 -0.1071 -0.2122 -0.1053 1310 TRP A CA    
721  C  C     . TRP A 93  ? 1.1364 1.1699 1.0500 -0.1167 -0.2172 -0.1119 1310 TRP A C     
722  O  O     . TRP A 93  ? 1.0681 1.1191 0.9952 -0.1224 -0.2334 -0.1109 1310 TRP A O     
723  C  CB    . TRP A 93  ? 1.2482 1.2671 1.1000 -0.1116 -0.2247 -0.1098 1310 TRP A CB    
724  C  CG    . TRP A 93  ? 1.2695 1.2731 1.0894 -0.1040 -0.2156 -0.1063 1310 TRP A CG    
725  C  CD1   . TRP A 93  ? 1.3225 1.3332 1.1317 -0.0966 -0.2212 -0.0952 1310 TRP A CD1   
726  C  CD2   . TRP A 93  ? 1.3643 1.3427 1.1602 -0.1028 -0.1980 -0.1134 1310 TRP A CD2   
727  N  NE1   . TRP A 93  ? 1.3847 1.3758 1.1640 -0.0914 -0.2080 -0.0947 1310 TRP A NE1   
728  C  CE2   . TRP A 93  ? 1.3483 1.3200 1.1196 -0.0950 -0.1934 -0.1059 1310 TRP A CE2   
729  C  CE3   . TRP A 93  ? 1.4150 1.3755 1.2089 -0.1072 -0.1849 -0.1249 1310 TRP A CE3   
730  C  CZ2   . TRP A 93  ? 1.2520 1.2010 0.9976 -0.0919 -0.1758 -0.1096 1310 TRP A CZ2   
731  C  CZ3   . TRP A 93  ? 1.3806 1.3186 1.1494 -0.1033 -0.1677 -0.1287 1310 TRP A CZ3   
732  C  CH2   . TRP A 93  ? 1.3068 1.2399 1.0521 -0.0960 -0.1632 -0.1211 1310 TRP A CH2   
733  N  N     . VAL A 94  ? 1.0448 1.0644 0.9653 -0.1183 -0.2029 -0.1183 1311 VAL A N     
734  C  CA    . VAL A 94  ? 0.9584 0.9757 0.8927 -0.1291 -0.2055 -0.1274 1311 VAL A CA    
735  C  C     . VAL A 94  ? 1.0478 1.0495 0.9507 -0.1395 -0.2142 -0.1404 1311 VAL A C     
736  O  O     . VAL A 94  ? 1.0696 1.0515 0.9384 -0.1375 -0.2079 -0.1455 1311 VAL A O     
737  C  CB    . VAL A 94  ? 0.9745 0.9789 0.9220 -0.1266 -0.1871 -0.1297 1311 VAL A CB    
738  C  CG1   . VAL A 94  ? 1.0465 1.0428 1.0028 -0.1382 -0.1882 -0.1402 1311 VAL A CG1   
739  C  CG2   . VAL A 94  ? 0.9279 0.9494 0.9063 -0.1173 -0.1812 -0.1171 1311 VAL A CG2   
740  N  N     . THR A 95  ? 1.1406 1.1514 1.0538 -0.1509 -0.2291 -0.1458 1312 THR A N     
741  C  CA    . THR A 95  ? 1.2245 1.2184 1.1075 -0.1621 -0.2375 -0.1599 1312 THR A CA    
742  C  C     . THR A 95  ? 1.2251 1.2186 1.1263 -0.1759 -0.2436 -0.1696 1312 THR A C     
743  O  O     . THR A 95  ? 1.2756 1.2569 1.1541 -0.1870 -0.2536 -0.1822 1312 THR A O     
744  C  CB    . THR A 95  ? 1.3124 1.3163 1.1731 -0.1633 -0.2568 -0.1576 1312 THR A CB    
745  O  OG1   . THR A 95  ? 1.4182 1.4090 1.2543 -0.1766 -0.2685 -0.1722 1312 THR A OG1   
746  C  CG2   . THR A 95  ? 1.1794 1.2166 1.0743 -0.1619 -0.2712 -0.1457 1312 THR A CG2   
747  N  N     . LYS A 96  ? 1.1966 1.2012 1.1361 -0.1760 -0.2376 -0.1647 1313 LYS A N     
748  C  CA    . LYS A 96  ? 1.2895 1.2905 1.2458 -0.1895 -0.2410 -0.1740 1313 LYS A CA    
749  C  C     . LYS A 96  ? 1.1381 1.1369 1.1241 -0.1856 -0.2239 -0.1695 1313 LYS A C     
750  O  O     . LYS A 96  ? 1.0289 1.0432 1.0361 -0.1751 -0.2175 -0.1567 1313 LYS A O     
751  C  CB    . LYS A 96  ? 1.4300 1.4572 1.4066 -0.1991 -0.2631 -0.1723 1313 LYS A CB    
752  C  CG    . LYS A 96  ? 1.5297 1.5865 1.5511 -0.1953 -0.2643 -0.1588 1313 LYS A CG    
753  C  CD    . LYS A 96  ? 1.6230 1.7003 1.6701 -0.2090 -0.2825 -0.1612 1313 LYS A CD    
754  C  CE    . LYS A 96  ? 1.5918 1.7042 1.6769 -0.2033 -0.2889 -0.1461 1313 LYS A CE    
755  N  NZ    . LYS A 96  ? 1.5274 1.6560 1.6532 -0.2143 -0.2927 -0.1461 1313 LYS A NZ    
756  N  N     . SER A 97  ? 1.1260 1.1030 1.1101 -0.1937 -0.2161 -0.1805 1314 SER A N     
757  C  CA    . SER A 97  ? 1.0819 1.0550 1.0942 -0.1930 -0.2022 -0.1776 1314 SER A CA    
758  C  C     . SER A 97  ? 1.2207 1.2073 1.2619 -0.2066 -0.2132 -0.1794 1314 SER A C     
759  O  O     . SER A 97  ? 1.1595 1.1329 1.1920 -0.2202 -0.2199 -0.1923 1314 SER A O     
760  C  CB    . SER A 97  ? 1.1499 1.0898 1.1433 -0.1930 -0.1863 -0.1878 1314 SER A CB    
761  O  OG    . SER A 97  ? 1.3338 1.2654 1.3497 -0.1999 -0.1795 -0.1906 1314 SER A OG    
762  N  N     . GLY A 98  ? 1.1729 1.1855 1.2485 -0.2032 -0.2145 -0.1668 1315 GLY A N     
763  C  CA    . GLY A 98  ? 1.0479 1.0756 1.1536 -0.2159 -0.2241 -0.1674 1315 GLY A CA    
764  C  C     . GLY A 98  ? 1.2137 1.2542 1.3115 -0.2262 -0.2464 -0.1734 1315 GLY A C     
765  O  O     . GLY A 98  ? 1.1413 1.2061 1.2444 -0.2209 -0.2576 -0.1648 1315 GLY A O     
766  N  N     . ASP A 99  ? 1.3392 1.3633 1.4251 -0.2412 -0.2535 -0.1882 1316 ASP A N     
767  C  CA    . ASP A 99  ? 1.4435 1.4746 1.5139 -0.2517 -0.2756 -0.1964 1316 ASP A CA    
768  C  C     . ASP A 99  ? 1.4498 1.4507 1.4719 -0.2539 -0.2760 -0.2106 1316 ASP A C     
769  O  O     . ASP A 99  ? 1.4230 1.4259 1.4245 -0.2622 -0.2944 -0.2185 1316 ASP A O     
770  C  CB    . ASP A 99  ? 1.5084 1.5493 1.6068 -0.2697 -0.2877 -0.2025 1316 ASP A CB    
771  C  CG    . ASP A 99  ? 1.5641 1.6443 1.7006 -0.2696 -0.3000 -0.1900 1316 ASP A CG    
772  O  OD1   . ASP A 99  ? 1.4958 1.5939 1.6276 -0.2575 -0.3050 -0.1797 1316 ASP A OD1   
773  O  OD2   . ASP A 99  ? 1.6871 1.7796 1.8585 -0.2813 -0.3037 -0.1902 1316 ASP A OD2   
774  N  N     . SER A 100 ? 1.4467 1.4198 1.4502 -0.2466 -0.2561 -0.2140 1317 SER A N     
775  C  CA    . SER A 100 ? 1.5119 1.4552 1.4691 -0.2466 -0.2528 -0.2268 1317 SER A CA    
776  C  C     . SER A 100 ? 1.5278 1.4756 1.4607 -0.2316 -0.2507 -0.2184 1317 SER A C     
777  O  O     . SER A 100 ? 1.4810 1.4324 1.4238 -0.2177 -0.2359 -0.2072 1317 SER A O     
778  C  CB    . SER A 100 ? 1.5517 1.4629 1.5034 -0.2457 -0.2315 -0.2343 1317 SER A CB    
779  O  OG    . SER A 100 ? 1.5908 1.4986 1.5699 -0.2581 -0.2311 -0.2392 1317 SER A OG    
780  N  N     . GLU A 101 ? 1.5257 1.4728 1.4264 -0.2347 -0.2657 -0.2238 1318 GLU A N     
781  C  CA    . GLU A 101 ? 1.2989 1.2456 1.1714 -0.2216 -0.2629 -0.2171 1318 GLU A CA    
782  C  C     . GLU A 101 ? 1.4255 1.3377 1.2653 -0.2164 -0.2430 -0.2257 1318 GLU A C     
783  O  O     . GLU A 101 ? 1.4531 1.3397 1.2748 -0.2260 -0.2401 -0.2412 1318 GLU A O     
784  C  CB    . GLU A 101 ? 1.0448 1.0010 0.8917 -0.2266 -0.2858 -0.2195 1318 GLU A CB    
785  N  N     . LEU A 102 ? 1.4578 1.3687 1.2912 -0.2014 -0.2287 -0.2160 1319 LEU A N     
786  C  CA    . LEU A 102 ? 1.4845 1.3651 1.2929 -0.1956 -0.2081 -0.2230 1319 LEU A CA    
787  C  C     . LEU A 102 ? 1.6152 1.4800 1.3747 -0.1940 -0.2103 -0.2291 1319 LEU A C     
788  O  O     . LEU A 102 ? 1.6656 1.5460 1.4127 -0.1922 -0.2246 -0.2226 1319 LEU A O     
789  C  CB    . LEU A 102 ? 1.3341 1.2194 1.1628 -0.1808 -0.1893 -0.2103 1319 LEU A CB    
790  C  CG    . LEU A 102 ? 1.3731 1.2774 1.2483 -0.1795 -0.1871 -0.2008 1319 LEU A CG    
791  C  CD1   . LEU A 102 ? 1.3659 1.3020 1.2607 -0.1739 -0.1985 -0.1860 1319 LEU A CD1   
792  C  CD2   . LEU A 102 ? 1.3810 1.2738 1.2681 -0.1694 -0.1651 -0.1969 1319 LEU A CD2   
793  N  N     . ALA A 103 ? 1.6792 1.5121 1.4107 -0.1939 -0.1948 -0.2410 1320 ALA A N     
794  C  CA    . ALA A 103 ? 1.7153 1.5278 1.3959 -0.1944 -0.1954 -0.2498 1320 ALA A CA    
795  C  C     . ALA A 103 ? 1.6972 1.5204 1.3647 -0.1815 -0.1925 -0.2363 1320 ALA A C     
796  O  O     . ALA A 103 ? 1.7880 1.6188 1.4313 -0.1828 -0.2081 -0.2340 1320 ALA A O     
797  C  CB    . ALA A 103 ? 1.7423 1.5187 1.4003 -0.1943 -0.1748 -0.2636 1320 ALA A CB    
798  N  N     . GLU A 104 ? 1.5817 1.4050 1.2644 -0.1690 -0.1730 -0.2271 1321 GLU A N     
799  C  CA    . GLU A 104 ? 1.5090 1.3456 1.1876 -0.1573 -0.1708 -0.2128 1321 GLU A CA    
800  C  C     . GLU A 104 ? 1.5179 1.3841 1.2434 -0.1517 -0.1739 -0.1976 1321 GLU A C     
801  O  O     . GLU A 104 ? 1.4139 1.2828 1.1718 -0.1526 -0.1673 -0.1978 1321 GLU A O     
802  C  CB    . GLU A 104 ? 1.4216 1.2380 1.0817 -0.1469 -0.1467 -0.2126 1321 GLU A CB    
803  N  N     . PRO A 105 ? 1.5798 1.4676 1.3091 -0.1466 -0.1851 -0.1849 1322 PRO A N     
804  C  CA    . PRO A 105 ? 1.5118 1.4267 1.2836 -0.1408 -0.1876 -0.1709 1322 PRO A CA    
805  C  C     . PRO A 105 ? 1.3623 1.2765 1.1451 -0.1278 -0.1686 -0.1612 1322 PRO A C     
806  O  O     . PRO A 105 ? 1.3986 1.2988 1.1557 -0.1216 -0.1574 -0.1607 1322 PRO A O     
807  C  CB    . PRO A 105 ? 1.5753 1.5110 1.3423 -0.1410 -0.2082 -0.1626 1322 PRO A CB    
808  C  CG    . PRO A 105 ? 1.6353 1.5529 1.3524 -0.1428 -0.2120 -0.1690 1322 PRO A CG    
809  C  CD    . PRO A 105 ? 1.6397 1.5262 1.3325 -0.1445 -0.1939 -0.1821 1322 PRO A CD    
810  N  N     . ILE A 106 ? 1.2222 1.1522 1.0443 -0.1240 -0.1650 -0.1533 1323 ILE A N     
811  C  CA    . ILE A 106 ? 1.1907 1.1219 1.0285 -0.1127 -0.1486 -0.1446 1323 ILE A CA    
812  C  C     . ILE A 106 ? 1.0923 1.0484 0.9522 -0.1060 -0.1557 -0.1301 1323 ILE A C     
813  O  O     . ILE A 106 ? 1.0817 1.0565 0.9604 -0.1098 -0.1699 -0.1267 1323 ILE A O     
814  C  CB    . ILE A 106 ? 1.2347 1.1592 1.0968 -0.1131 -0.1362 -0.1484 1323 ILE A CB    
815  C  CG1   . ILE A 106 ? 1.2128 1.1556 1.1081 -0.1180 -0.1463 -0.1453 1323 ILE A CG1   
816  C  CG2   . ILE A 106 ? 1.2225 1.1213 1.0628 -0.1201 -0.1299 -0.1632 1323 ILE A CG2   
817  C  CD1   . ILE A 106 ? 1.1714 1.1063 1.0887 -0.1190 -0.1351 -0.1486 1323 ILE A CD1   
818  N  N     . ALA A 107 ? 1.0338 0.9899 0.8920 -0.0960 -0.1455 -0.1217 1324 ALA A N     
819  C  CA    . ALA A 107 ? 0.8901 0.8659 0.7639 -0.0889 -0.1509 -0.1084 1324 ALA A CA    
820  C  C     . ALA A 107 ? 0.8588 0.8431 0.7654 -0.0825 -0.1411 -0.1019 1324 ALA A C     
821  O  O     . ALA A 107 ? 0.8898 0.8624 0.7996 -0.0798 -0.1264 -0.1047 1324 ALA A O     
822  C  CB    . ALA A 107 ? 0.8899 0.8590 0.7375 -0.0827 -0.1473 -0.1030 1324 ALA A CB    
823  N  N     . VAL A 108 ? 0.7772 0.7818 0.7077 -0.0799 -0.1492 -0.0932 1325 VAL A N     
824  C  CA    . VAL A 108 ? 0.8385 0.8511 0.7959 -0.0729 -0.1407 -0.0862 1325 VAL A CA    
825  C  C     . VAL A 108 ? 0.9283 0.9384 0.8782 -0.0642 -0.1330 -0.0787 1325 VAL A C     
826  O  O     . VAL A 108 ? 0.9072 0.9208 0.8432 -0.0619 -0.1395 -0.0735 1325 VAL A O     
827  C  CB    . VAL A 108 ? 0.8124 0.8462 0.7968 -0.0732 -0.1509 -0.0801 1325 VAL A CB    
828  C  CG1   . VAL A 108 ? 0.6288 0.6704 0.6365 -0.0651 -0.1428 -0.0722 1325 VAL A CG1   
829  C  CG2   . VAL A 108 ? 0.6146 0.6495 0.6091 -0.0825 -0.1559 -0.0875 1325 VAL A CG2   
830  N  N     . ARG A 109 ? 0.9837 0.9874 0.9428 -0.0595 -0.1192 -0.0781 1326 ARG A N     
831  C  CA    . ARG A 109 ? 0.9968 0.9944 0.9471 -0.0529 -0.1097 -0.0732 1326 ARG A CA    
832  C  C     . ARG A 109 ? 0.9398 0.9501 0.8970 -0.0473 -0.1156 -0.0626 1326 ARG A C     
833  O  O     . ARG A 109 ? 0.6959 0.7202 0.6761 -0.0453 -0.1204 -0.0580 1326 ARG A O     
834  C  CB    . ARG A 109 ? 1.0269 1.0196 0.9930 -0.0491 -0.0958 -0.0736 1326 ARG A CB    
835  C  CG    . ARG A 109 ? 1.0333 1.0380 1.0281 -0.0478 -0.0980 -0.0709 1326 ARG A CG    
836  C  CD    . ARG A 109 ? 1.0501 1.0556 1.0611 -0.0415 -0.0881 -0.0666 1326 ARG A CD    
837  N  NE    . ARG A 109 ? 1.0740 1.0870 1.1077 -0.0412 -0.0893 -0.0659 1326 ARG A NE    
838  C  CZ    . ARG A 109 ? 1.0107 1.0175 1.0537 -0.0411 -0.0818 -0.0694 1326 ARG A CZ    
839  N  NH1   . ARG A 109 ? 1.0122 1.0057 1.0459 -0.0409 -0.0719 -0.0741 1326 ARG A NH1   
840  N  NH2   . ARG A 109 ? 0.9073 0.9210 0.9690 -0.0406 -0.0838 -0.0676 1326 ARG A NH2   
841  N  N     . PRO A 110 ? 1.1000 1.1046 1.0375 -0.0444 -0.1143 -0.0583 1327 PRO A N     
842  C  CA    . PRO A 110 ? 1.0091 1.0226 0.9538 -0.0381 -0.1171 -0.0479 1327 PRO A CA    
843  C  C     . PRO A 110 ? 1.0259 1.0336 0.9777 -0.0329 -0.1035 -0.0442 1327 PRO A C     
844  O  O     . PRO A 110 ? 1.0792 1.0928 1.0413 -0.0278 -0.1037 -0.0364 1327 PRO A O     
845  C  CB    . PRO A 110 ? 0.9043 0.9137 0.8213 -0.0385 -0.1244 -0.0451 1327 PRO A CB    
846  C  CG    . PRO A 110 ? 0.9829 0.9748 0.8738 -0.0430 -0.1171 -0.0536 1327 PRO A CG    
847  C  CD    . PRO A 110 ? 1.0690 1.0584 0.9740 -0.0472 -0.1118 -0.0629 1327 PRO A CD    
848  N  N     . THR A 111 ? 1.0506 1.0467 0.9983 -0.0344 -0.0916 -0.0503 1328 THR A N     
849  C  CA    . THR A 111 ? 1.0241 1.0137 0.9784 -0.0308 -0.0775 -0.0487 1328 THR A CA    
850  C  C     . THR A 111 ? 1.0377 1.0142 0.9818 -0.0338 -0.0673 -0.0573 1328 THR A C     
851  O  O     . THR A 111 ? 0.9970 0.9668 0.9220 -0.0384 -0.0712 -0.0636 1328 THR A O     
852  C  CB    . THR A 111 ? 0.9335 0.9186 0.8755 -0.0271 -0.0737 -0.0409 1328 THR A CB    
853  O  OG1   . THR A 111 ? 1.0336 1.0127 0.9838 -0.0248 -0.0593 -0.0400 1328 THR A OG1   
854  C  CG2   . THR A 111 ? 0.7989 0.7736 0.7074 -0.0293 -0.0756 -0.0418 1328 THR A CG2   
855  N  N     . SER A 112 ? 0.9970 0.9691 0.9530 -0.0313 -0.0542 -0.0580 1329 SER A N     
856  C  CA    . SER A 112 ? 0.9882 0.9493 0.9400 -0.0333 -0.0446 -0.0664 1329 SER A CA    
857  C  C     . SER A 112 ? 0.9453 0.8929 0.8816 -0.0318 -0.0295 -0.0673 1329 SER A C     
858  O  O     . SER A 112 ? 1.0398 0.9800 0.9814 -0.0311 -0.0178 -0.0723 1329 SER A O     
859  C  CB    . SER A 112 ? 0.9134 0.8808 0.8943 -0.0317 -0.0417 -0.0677 1329 SER A CB    
860  O  OG    . SER A 112 ? 0.9349 0.9152 0.9310 -0.0323 -0.0540 -0.0651 1329 SER A OG    
861  N  N     . GLU A 113 ? 0.9159 0.8592 0.8321 -0.0310 -0.0287 -0.0623 1330 GLU A N     
862  C  CA    . GLU A 113 ? 0.9730 0.9030 0.8738 -0.0295 -0.0126 -0.0623 1330 GLU A CA    
863  C  C     . GLU A 113 ? 1.0675 0.9819 0.9447 -0.0325 -0.0061 -0.0725 1330 GLU A C     
864  O  O     . GLU A 113 ? 1.0480 0.9538 0.9287 -0.0309 0.0093  -0.0765 1330 GLU A O     
865  C  CB    . GLU A 113 ? 0.7695 0.6965 0.6502 -0.0281 -0.0136 -0.0542 1330 GLU A CB    
866  C  CG    . GLU A 113 ? 0.9537 0.8892 0.8563 -0.0244 -0.0105 -0.0444 1330 GLU A CG    
867  C  CD    . GLU A 113 ? 1.0451 0.9944 0.9613 -0.0234 -0.0264 -0.0386 1330 GLU A CD    
868  O  OE1   . GLU A 113 ? 1.0276 0.9840 0.9462 -0.0253 -0.0391 -0.0422 1330 GLU A OE1   
869  O  OE2   . GLU A 113 ? 1.1260 1.0788 1.0515 -0.0207 -0.0254 -0.0305 1330 GLU A OE2   
870  N  N     . THR A 114 ? 1.1138 1.0242 0.9672 -0.0368 -0.0179 -0.0770 1331 THR A N     
871  C  CA    . THR A 114 ? 1.1700 1.0632 0.9948 -0.0405 -0.0133 -0.0872 1331 THR A CA    
872  C  C     . THR A 114 ? 1.1903 1.0792 1.0302 -0.0419 -0.0077 -0.0965 1331 THR A C     
873  O  O     . THR A 114 ? 1.1022 0.9743 0.9203 -0.0445 -0.0008 -0.1061 1331 THR A O     
874  C  CB    . THR A 114 ? 1.1328 1.0253 0.9315 -0.0456 -0.0303 -0.0895 1331 THR A CB    
875  O  OG1   . THR A 114 ? 1.1869 1.0873 1.0013 -0.0499 -0.0424 -0.0950 1331 THR A OG1   
876  C  CG2   . THR A 114 ? 1.0689 0.9729 0.8673 -0.0431 -0.0405 -0.0780 1331 THR A CG2   
877  N  N     . VAL A 115 ? 1.1939 1.0962 1.0687 -0.0402 -0.0106 -0.0940 1332 VAL A N     
878  C  CA    . VAL A 115 ? 1.1575 1.0560 1.0492 -0.0404 -0.0050 -0.1009 1332 VAL A CA    
879  C  C     . VAL A 115 ? 1.1230 1.0233 1.0391 -0.0342 0.0104  -0.0974 1332 VAL A C     
880  O  O     . VAL A 115 ? 1.1667 1.0556 1.0838 -0.0326 0.0236  -0.1035 1332 VAL A O     
881  C  CB    . VAL A 115 ? 1.0731 0.9841 0.9848 -0.0433 -0.0198 -0.1008 1332 VAL A CB    
882  C  CG1   . VAL A 115 ? 1.0942 0.9994 0.9832 -0.0504 -0.0313 -0.1078 1332 VAL A CG1   
883  C  CG2   . VAL A 115 ? 1.0984 1.0278 1.0272 -0.0408 -0.0293 -0.0905 1332 VAL A CG2   
884  N  N     . MET A 116 ? 1.0245 0.9388 0.9602 -0.0306 0.0091  -0.0878 1333 MET A N     
885  C  CA    . MET A 116 ? 0.9726 0.8916 0.9351 -0.0254 0.0213  -0.0841 1333 MET A CA    
886  C  C     . MET A 116 ? 0.9461 0.8544 0.8965 -0.0230 0.0388  -0.0838 1333 MET A C     
887  O  O     . MET A 116 ? 1.0797 0.9893 1.0511 -0.0190 0.0514  -0.0830 1333 MET A O     
888  C  CB    . MET A 116 ? 1.0025 0.9392 0.9899 -0.0232 0.0134  -0.0749 1333 MET A CB    
889  C  CG    . MET A 116 ? 1.0557 1.0039 1.0594 -0.0244 -0.0012 -0.0744 1333 MET A CG    
890  S  SD    . MET A 116 ? 1.1258 1.0920 1.1555 -0.0214 -0.0088 -0.0646 1333 MET A SD    
891  C  CE    . MET A 116 ? 0.9472 0.9157 1.0035 -0.0169 0.0051  -0.0630 1333 MET A CE    
892  N  N     . TYR A 117 ? 0.8892 0.7871 0.8067 -0.0251 0.0402  -0.0842 1334 TYR A N     
893  C  CA    . TYR A 117 ? 1.0296 0.9175 0.9372 -0.0224 0.0589  -0.0829 1334 TYR A CA    
894  C  C     . TYR A 117 ? 1.1800 1.0500 1.0721 -0.0221 0.0731  -0.0930 1334 TYR A C     
895  O  O     . TYR A 117 ? 1.3097 1.1759 1.2131 -0.0180 0.0913  -0.0927 1334 TYR A O     
896  C  CB    . TYR A 117 ? 0.9707 0.8545 0.8505 -0.0237 0.0568  -0.0770 1334 TYR A CB    
897  C  CG    . TYR A 117 ? 0.9706 0.8710 0.8735 -0.0224 0.0486  -0.0663 1334 TYR A CG    
898  C  CD1   . TYR A 117 ? 0.9272 0.8426 0.8687 -0.0204 0.0456  -0.0640 1334 TYR A CD1   
899  C  CD2   . TYR A 117 ? 0.9610 0.8611 0.8468 -0.0228 0.0438  -0.0587 1334 TYR A CD2   
900  C  CE1   . TYR A 117 ? 0.9356 0.8644 0.8970 -0.0195 0.0382  -0.0557 1334 TYR A CE1   
901  C  CE2   . TYR A 117 ? 1.0334 0.9468 0.9411 -0.0214 0.0370  -0.0497 1334 TYR A CE2   
902  C  CZ    . TYR A 117 ? 1.0630 0.9905 1.0083 -0.0201 0.0343  -0.0489 1334 TYR A CZ    
903  O  OH    . TYR A 117 ? 1.0646 1.0039 1.0304 -0.0190 0.0276  -0.0413 1334 TYR A OH    
904  N  N     . PRO A 118 ? 1.1664 1.0251 1.0348 -0.0263 0.0661  -0.1023 1335 PRO A N     
905  C  CA    . PRO A 118 ? 1.2274 1.0690 1.0876 -0.0255 0.0798  -0.1128 1335 PRO A CA    
906  C  C     . PRO A 118 ? 1.0445 0.8932 0.9440 -0.0209 0.0868  -0.1128 1335 PRO A C     
907  O  O     . PRO A 118 ? 1.0102 0.8488 0.9140 -0.0167 0.1050  -0.1168 1335 PRO A O     
908  C  CB    . PRO A 118 ? 1.2807 1.1127 1.1151 -0.0322 0.0659  -0.1222 1335 PRO A CB    
909  C  CG    . PRO A 118 ? 1.2900 1.1301 1.1081 -0.0358 0.0493  -0.1166 1335 PRO A CG    
910  C  CD    . PRO A 118 ? 1.1224 0.9819 0.9687 -0.0319 0.0469  -0.1039 1335 PRO A CD    
911  N  N     . ALA A 119 ? 0.9390 0.8050 0.8672 -0.0210 0.0729  -0.1081 1336 ALA A N     
912  C  CA    . ALA A 119 ? 0.9278 0.8017 0.8929 -0.0161 0.0778  -0.1066 1336 ALA A CA    
913  C  C     . ALA A 119 ? 0.9610 0.8417 0.9479 -0.0103 0.0928  -0.1001 1336 ALA A C     
914  O  O     . ALA A 119 ? 0.9326 0.8102 0.9378 -0.0053 0.1064  -0.1020 1336 ALA A O     
915  C  CB    . ALA A 119 ? 0.9394 0.8307 0.9279 -0.0173 0.0598  -0.1016 1336 ALA A CB    
916  N  N     . TYR A 120 ? 1.0076 0.8973 0.9940 -0.0108 0.0910  -0.0923 1337 TYR A N     
917  C  CA    . TYR A 120 ? 1.0253 0.9216 1.0330 -0.0064 0.1055  -0.0860 1337 TYR A CA    
918  C  C     . TYR A 120 ? 1.0792 0.9582 1.0691 -0.0041 0.1273  -0.0909 1337 TYR A C     
919  O  O     . TYR A 120 ? 1.0537 0.9357 1.0677 0.0009  0.1430  -0.0892 1337 TYR A O     
920  C  CB    . TYR A 120 ? 0.9775 0.8845 0.9859 -0.0083 0.0992  -0.0768 1337 TYR A CB    
921  C  CG    . TYR A 120 ? 0.8919 0.8173 0.9243 -0.0092 0.0810  -0.0711 1337 TYR A CG    
922  C  CD1   . TYR A 120 ? 0.9635 0.8933 1.0048 -0.0097 0.0683  -0.0744 1337 TYR A CD1   
923  C  CD2   . TYR A 120 ? 0.7271 0.6641 0.7729 -0.0095 0.0777  -0.0627 1337 TYR A CD2   
924  C  CE1   . TYR A 120 ? 0.9634 0.9085 1.0238 -0.0102 0.0531  -0.0695 1337 TYR A CE1   
925  C  CE2   . TYR A 120 ? 0.7934 0.7452 0.8588 -0.0101 0.0618  -0.0585 1337 TYR A CE2   
926  C  CZ    . TYR A 120 ? 0.8692 0.8251 0.9409 -0.0103 0.0498  -0.0620 1337 TYR A CZ    
927  O  OH    . TYR A 120 ? 0.7989 0.7682 0.8873 -0.0106 0.0350  -0.0581 1337 TYR A OH    
928  N  N     . ALA A 121 ? 1.0706 0.9313 1.0182 -0.0075 0.1288  -0.0973 1338 ALA A N     
929  C  CA    . ALA A 121 ? 1.0639 0.9058 0.9902 -0.0052 0.1505  -0.1028 1338 ALA A CA    
930  C  C     . ALA A 121 ? 1.1975 1.0321 1.1396 -0.0010 0.1613  -0.1104 1338 ALA A C     
931  O  O     . ALA A 121 ? 1.3309 1.1594 1.2811 0.0042  0.1825  -0.1112 1338 ALA A O     
932  C  CB    . ALA A 121 ? 0.8367 0.6594 0.7115 -0.0101 0.1479  -0.1089 1338 ALA A CB    
933  N  N     . LYS A 122 ? 1.2011 1.0365 1.1499 -0.0026 0.1478  -0.1151 1339 LYS A N     
934  C  CA    . LYS A 122 ? 1.1800 1.0089 1.1477 0.0022  0.1578  -0.1208 1339 LYS A CA    
935  C  C     . LYS A 122 ? 1.0578 0.9060 1.0740 0.0089  0.1625  -0.1124 1339 LYS A C     
936  O  O     . LYS A 122 ? 0.8634 0.7073 0.8973 0.0154  0.1796  -0.1141 1339 LYS A O     
937  C  CB    . LYS A 122 ? 1.3435 1.1693 1.3099 -0.0013 0.1421  -0.1266 1339 LYS A CB    
938  C  CG    . LYS A 122 ? 1.4771 1.2783 1.4183 -0.0026 0.1498  -0.1390 1339 LYS A CG    
939  C  CD    . LYS A 122 ? 1.5047 1.3057 1.4635 -0.0032 0.1399  -0.1424 1339 LYS A CD    
940  C  CE    . LYS A 122 ? 1.6200 1.3986 1.5392 -0.0105 0.1358  -0.1549 1339 LYS A CE    
941  N  NZ    . LYS A 122 ? 1.5536 1.3213 1.4768 -0.0130 0.1304  -0.1623 1339 LYS A NZ    
942  N  N     . TRP A 123 ? 1.0382 0.9077 1.0761 0.0075  0.1474  -0.1034 1340 TRP A N     
943  C  CA    . TRP A 123 ? 0.9666 0.8545 1.0497 0.0128  0.1468  -0.0966 1340 TRP A CA    
944  C  C     . TRP A 123 ? 0.8625 0.7594 0.9670 0.0169  0.1623  -0.0902 1340 TRP A C     
945  O  O     . TRP A 123 ? 0.8066 0.7182 0.9502 0.0220  0.1646  -0.0852 1340 TRP A O     
946  C  CB    . TRP A 123 ? 0.9430 0.8486 1.0400 0.0097  0.1244  -0.0905 1340 TRP A CB    
947  C  CG    . TRP A 123 ? 0.9397 0.8395 1.0261 0.0067  0.1105  -0.0955 1340 TRP A CG    
948  C  CD1   . TRP A 123 ? 0.9961 0.8788 1.0710 0.0072  0.1156  -0.1041 1340 TRP A CD1   
949  C  CD2   . TRP A 123 ? 0.9498 0.8603 1.0367 0.0024  0.0899  -0.0923 1340 TRP A CD2   
950  N  NE1   . TRP A 123 ? 1.0450 0.9277 1.1145 0.0029  0.0991  -0.1061 1340 TRP A NE1   
951  C  CE2   . TRP A 123 ? 1.0297 0.9299 1.1065 0.0001  0.0835  -0.0988 1340 TRP A CE2   
952  C  CE3   . TRP A 123 ? 0.6984 0.6254 0.7936 0.0002  0.0771  -0.0847 1340 TRP A CE3   
953  C  CZ2   . TRP A 123 ? 0.9744 0.8818 1.0504 -0.0041 0.0654  -0.0973 1340 TRP A CZ2   
954  C  CZ3   . TRP A 123 ? 0.8773 0.8106 0.9705 -0.0033 0.0595  -0.0837 1340 TRP A CZ3   
955  C  CH2   . TRP A 123 ? 0.9672 0.8914 1.0514 -0.0054 0.0539  -0.0897 1340 TRP A CH2   
956  N  N     . ILE A 124 ? 0.9575 0.8469 1.0381 0.0145  0.1720  -0.0897 1341 ILE A N     
957  C  CA    . ILE A 124 ? 0.9523 0.8494 1.0536 0.0178  0.1889  -0.0835 1341 ILE A CA    
958  C  C     . ILE A 124 ? 1.0209 0.8983 1.1031 0.0213  0.2132  -0.0899 1341 ILE A C     
959  O  O     . ILE A 124 ? 1.0594 0.9209 1.1026 0.0181  0.2202  -0.0927 1341 ILE A O     
960  C  CB    . ILE A 124 ? 0.9590 0.8645 1.0539 0.0129  0.1832  -0.0758 1341 ILE A CB    
961  C  CG1   . ILE A 124 ? 1.0314 0.9507 1.1342 0.0090  0.1579  -0.0722 1341 ILE A CG1   
962  C  CG2   . ILE A 124 ? 1.0030 0.9225 1.1327 0.0156  0.1964  -0.0680 1341 ILE A CG2   
963  C  CD1   . ILE A 124 ? 1.0608 0.9796 1.1397 0.0034  0.1487  -0.0678 1341 ILE A CD1   
964  N  N     . GLN A 125 ? 1.1599 1.0369 1.2674 0.0282  0.2257  -0.0923 1342 GLN A N     
965  C  CA    . GLN A 125 ? 1.3322 1.1919 1.4288 0.0332  0.2516  -0.0980 1342 GLN A CA    
966  C  C     . GLN A 125 ? 1.4146 1.2876 1.5463 0.0383  0.2708  -0.0904 1342 GLN A C     
967  O  O     . GLN A 125 ? 1.6301 1.4894 1.7514 0.0422  0.2951  -0.0938 1342 GLN A O     
968  C  CB    . GLN A 125 ? 1.2980 1.1454 1.3983 0.0382  0.2550  -0.1065 1342 GLN A CB    
969  N  N     . SER A 126 ? 1.2667 1.1656 1.4384 0.0378  0.2610  -0.0805 1343 SER A N     
970  C  CA    . SER A 126 ? 1.2126 1.1274 1.4230 0.0415  0.2771  -0.0727 1343 SER A CA    
971  C  C     . SER A 126 ? 1.0396 0.9762 1.2714 0.0360  0.2624  -0.0630 1343 SER A C     
972  O  O     . SER A 126 ? 0.8436 0.7858 1.0681 0.0311  0.2390  -0.0620 1343 SER A O     
973  C  CB    . SER A 126 ? 1.3175 1.2441 1.5738 0.0503  0.2834  -0.0718 1343 SER A CB    
974  O  OG    . SER A 126 ? 1.3036 1.2531 1.5943 0.0496  0.2611  -0.0658 1343 SER A OG    
975  N  N     . TYR A 127 ? 1.0642 1.0133 1.3246 0.0368  0.2772  -0.0558 1344 TYR A N     
976  C  CA    . TYR A 127 ? 1.0354 1.0057 1.3224 0.0314  0.2648  -0.0468 1344 TYR A CA    
977  C  C     . TYR A 127 ? 1.0180 1.0090 1.3403 0.0323  0.2421  -0.0445 1344 TYR A C     
978  O  O     . TYR A 127 ? 0.8497 0.8518 1.1769 0.0266  0.2231  -0.0404 1344 TYR A O     
979  C  CB    . TYR A 127 ? 0.9232 0.9048 1.2426 0.0324  0.2858  -0.0399 1344 TYR A CB    
980  N  N     . ARG A 128 ? 1.0392 1.0340 1.3844 0.0397  0.2440  -0.0470 1345 ARG A N     
981  C  CA    . ARG A 128 ? 0.8945 0.9087 1.2738 0.0416  0.2240  -0.0439 1345 ARG A CA    
982  C  C     . ARG A 128 ? 0.8304 0.8404 1.1838 0.0368  0.1990  -0.0464 1345 ARG A C     
983  O  O     . ARG A 128 ? 0.8541 0.8809 1.2303 0.0358  0.1798  -0.0424 1345 ARG A O     
984  C  CB    . ARG A 128 ? 0.9755 0.9901 1.3784 0.0514  0.2330  -0.0461 1345 ARG A CB    
985  C  CG    . ARG A 128 ? 1.0073 1.0174 1.4230 0.0574  0.2629  -0.0464 1345 ARG A CG    
986  C  CD    . ARG A 128 ? 0.9487 0.9514 1.3768 0.0680  0.2740  -0.0505 1345 ARG A CD    
987  N  NE    . ARG A 128 ? 0.8461 0.8436 1.2852 0.0741  0.3042  -0.0511 1345 ARG A NE    
988  N  N     . ASP A 129 ? 0.6917 0.6800 0.9981 0.0338  0.1986  -0.0528 1346 ASP A N     
989  C  CA    . ASP A 129 ? 0.8513 0.8360 1.1354 0.0299  0.1762  -0.0553 1346 ASP A CA    
990  C  C     . ASP A 129 ? 0.9554 0.9478 1.2313 0.0225  0.1614  -0.0508 1346 ASP A C     
991  O  O     . ASP A 129 ? 0.8628 0.8534 1.1211 0.0191  0.1432  -0.0523 1346 ASP A O     
992  C  CB    . ASP A 129 ? 0.9222 0.8817 1.1616 0.0292  0.1802  -0.0644 1346 ASP A CB    
993  C  CG    . ASP A 129 ? 1.0423 0.9907 1.2878 0.0367  0.1951  -0.0701 1346 ASP A CG    
994  O  OD1   . ASP A 129 ? 0.9050 0.8619 1.1776 0.0416  0.1881  -0.0689 1346 ASP A OD1   
995  O  OD2   . ASP A 129 ? 1.1246 1.0546 1.3468 0.0381  0.2143  -0.0757 1346 ASP A OD2   
996  N  N     . LEU A 130 ? 0.9634 0.9652 1.2552 0.0199  0.1687  -0.0449 1347 LEU A N     
997  C  CA    . LEU A 130 ? 0.8957 0.9010 1.1757 0.0130  0.1553  -0.0411 1347 LEU A CA    
998  C  C     . LEU A 130 ? 0.7986 0.8264 1.1180 0.0115  0.1426  -0.0352 1347 LEU A C     
999  O  O     . LEU A 130 ? 0.7711 0.8131 1.1290 0.0147  0.1489  -0.0322 1347 LEU A O     
1000 C  CB    . LEU A 130 ? 0.8987 0.8940 1.1588 0.0096  0.1707  -0.0387 1347 LEU A CB    
1001 C  CG    . LEU A 130 ? 1.0517 1.0240 1.2608 0.0080  0.1757  -0.0434 1347 LEU A CG    
1002 C  CD1   . LEU A 130 ? 1.0684 1.0320 1.2638 0.0061  0.1945  -0.0395 1347 LEU A CD1   
1003 C  CD2   . LEU A 130 ? 1.1592 1.1296 1.3447 0.0036  0.1537  -0.0438 1347 LEU A CD2   
1004 N  N     . PRO A 131 ? 0.7086 0.7402 1.0198 0.0066  0.1243  -0.0334 1348 PRO A N     
1005 C  CA    . PRO A 131 ? 0.7422 0.7603 1.0129 0.0027  0.1157  -0.0353 1348 PRO A CA    
1006 C  C     . PRO A 131 ? 0.7690 0.7830 1.0242 0.0042  0.1015  -0.0402 1348 PRO A C     
1007 O  O     . PRO A 131 ? 0.8661 0.8894 1.1440 0.0077  0.0951  -0.0406 1348 PRO A O     
1008 C  CB    . PRO A 131 ? 0.8016 0.8295 1.0822 -0.0025 0.1039  -0.0302 1348 PRO A CB    
1009 C  CG    . PRO A 131 ? 0.7434 0.7905 1.0652 -0.0010 0.0956  -0.0282 1348 PRO A CG    
1010 C  CD    . PRO A 131 ? 0.5861 0.6373 0.9313 0.0044  0.1109  -0.0288 1348 PRO A CD    
1011 N  N     . ILE A 132 ? 0.7692 0.7699 0.9872 0.0016  0.0962  -0.0431 1349 ILE A N     
1012 C  CA    . ILE A 132 ? 0.9026 0.9006 1.1065 0.0016  0.0810  -0.0469 1349 ILE A CA    
1013 C  C     . ILE A 132 ? 0.8882 0.8910 1.0836 -0.0025 0.0644  -0.0439 1349 ILE A C     
1014 O  O     . ILE A 132 ? 0.8696 0.8653 1.0426 -0.0057 0.0651  -0.0423 1349 ILE A O     
1015 C  CB    . ILE A 132 ? 0.9645 0.9442 1.1347 0.0017  0.0869  -0.0537 1349 ILE A CB    
1016 C  CG1   . ILE A 132 ? 0.9234 0.8975 1.1041 0.0066  0.1038  -0.0573 1349 ILE A CG1   
1017 C  CG2   . ILE A 132 ? 0.9455 0.9233 1.1019 0.0002  0.0702  -0.0571 1349 ILE A CG2   
1018 C  CD1   . ILE A 132 ? 0.8542 0.8106 1.0077 0.0072  0.1075  -0.0656 1349 ILE A CD1   
1019 N  N     . ARG A 133 ? 0.8106 0.8247 1.0232 -0.0019 0.0499  -0.0428 1350 ARG A N     
1020 C  CA    . ARG A 133 ? 0.7157 0.7352 0.9240 -0.0048 0.0344  -0.0403 1350 ARG A CA    
1021 C  C     . ARG A 133 ? 0.7656 0.7850 0.9661 -0.0039 0.0217  -0.0432 1350 ARG A C     
1022 O  O     . ARG A 133 ? 0.6109 0.6396 0.8316 -0.0016 0.0146  -0.0425 1350 ARG A O     
1023 C  CB    . ARG A 133 ? 0.7918 0.8255 1.0299 -0.0054 0.0295  -0.0360 1350 ARG A CB    
1024 C  CG    . ARG A 133 ? 0.8978 0.9357 1.1578 -0.0051 0.0438  -0.0335 1350 ARG A CG    
1025 C  CD    . ARG A 133 ? 0.9380 0.9745 1.1951 -0.0095 0.0470  -0.0295 1350 ARG A CD    
1026 N  NE    . ARG A 133 ? 0.9779 1.0212 1.2411 -0.0122 0.0318  -0.0275 1350 ARG A NE    
1027 C  CZ    . ARG A 133 ? 1.0028 1.0595 1.2950 -0.0129 0.0240  -0.0264 1350 ARG A CZ    
1028 N  NH1   . ARG A 133 ? 1.0002 1.0671 1.3210 -0.0107 0.0291  -0.0260 1350 ARG A NH1   
1029 N  NH2   . ARG A 133 ? 0.9427 1.0025 1.2350 -0.0155 0.0108  -0.0256 1350 ARG A NH2   
1030 N  N     . LEU A 134 ? 0.9453 0.9550 1.1170 -0.0059 0.0182  -0.0459 1351 LEU A N     
1031 C  CA    . LEU A 134 ? 0.8085 0.8170 0.9719 -0.0059 0.0080  -0.0489 1351 LEU A CA    
1032 C  C     . LEU A 134 ? 0.8463 0.8566 0.9953 -0.0086 -0.0044 -0.0472 1351 LEU A C     
1033 O  O     . LEU A 134 ? 0.9014 0.9076 1.0351 -0.0107 -0.0031 -0.0454 1351 LEU A O     
1034 C  CB    . LEU A 134 ? 0.6906 0.6858 0.8350 -0.0062 0.0151  -0.0548 1351 LEU A CB    
1035 C  CG    . LEU A 134 ? 0.7535 0.7450 0.9115 -0.0024 0.0275  -0.0575 1351 LEU A CG    
1036 C  CD1   . LEU A 134 ? 0.5476 0.5224 0.6815 -0.0034 0.0358  -0.0645 1351 LEU A CD1   
1037 C  CD2   . LEU A 134 ? 0.7349 0.7346 0.9155 0.0008  0.0204  -0.0563 1351 LEU A CD2   
1038 N  N     . ASN A 135 ? 0.8736 0.8901 1.0284 -0.0082 -0.0158 -0.0469 1352 ASN A N     
1039 C  CA    . ASN A 135 ? 0.8819 0.9016 1.0268 -0.0099 -0.0272 -0.0451 1352 ASN A CA    
1040 C  C     . ASN A 135 ? 0.8628 0.8813 0.9998 -0.0107 -0.0342 -0.0479 1352 ASN A C     
1041 O  O     . ASN A 135 ? 0.8840 0.9033 1.0315 -0.0091 -0.0342 -0.0493 1352 ASN A O     
1042 C  CB    . ASN A 135 ? 0.8547 0.8847 1.0174 -0.0086 -0.0342 -0.0412 1352 ASN A CB    
1043 C  CG    . ASN A 135 ? 0.8230 0.8566 0.9787 -0.0090 -0.0456 -0.0398 1352 ASN A CG    
1044 O  OD1   . ASN A 135 ? 0.7772 0.8078 0.9174 -0.0105 -0.0477 -0.0390 1352 ASN A OD1   
1045 N  ND2   . ASN A 135 ? 0.8961 0.9363 1.0632 -0.0073 -0.0527 -0.0391 1352 ASN A ND2   
1046 N  N     . GLN A 136 ? 0.9541 0.9712 1.0742 -0.0131 -0.0406 -0.0480 1353 GLN A N     
1047 C  CA    . GLN A 136 ? 0.9476 0.9664 1.0647 -0.0144 -0.0485 -0.0497 1353 GLN A CA    
1048 C  C     . GLN A 136 ? 0.7997 0.8265 0.9166 -0.0143 -0.0583 -0.0459 1353 GLN A C     
1049 O  O     . GLN A 136 ? 0.8592 0.8866 0.9677 -0.0146 -0.0601 -0.0434 1353 GLN A O     
1050 C  CB    . GLN A 136 ? 0.9587 0.9689 1.0576 -0.0182 -0.0477 -0.0548 1353 GLN A CB    
1051 C  CG    . GLN A 136 ? 1.0105 1.0125 1.0899 -0.0200 -0.0428 -0.0564 1353 GLN A CG    
1052 C  CD    . GLN A 136 ? 0.9855 0.9784 1.0474 -0.0241 -0.0431 -0.0627 1353 GLN A CD    
1053 O  OE1   . GLN A 136 ? 1.1193 1.1139 1.1846 -0.0262 -0.0489 -0.0649 1353 GLN A OE1   
1054 N  NE2   . GLN A 136 ? 1.0171 0.9996 1.0593 -0.0256 -0.0368 -0.0656 1353 GLN A NE2   
1055 N  N     . TRP A 137 ? 0.6813 0.7137 0.8075 -0.0135 -0.0638 -0.0453 1354 TRP A N     
1056 C  CA    . TRP A 137 ? 0.5673 0.6067 0.6932 -0.0133 -0.0722 -0.0426 1354 TRP A CA    
1057 C  C     . TRP A 137 ? 0.7340 0.7721 0.8510 -0.0169 -0.0755 -0.0452 1354 TRP A C     
1058 O  O     . TRP A 137 ? 0.7599 0.7963 0.8815 -0.0181 -0.0749 -0.0473 1354 TRP A O     
1059 C  CB    . TRP A 137 ? 0.5463 0.5914 0.6861 -0.0104 -0.0751 -0.0404 1354 TRP A CB    
1060 C  CG    . TRP A 137 ? 0.6970 0.7446 0.8458 -0.0077 -0.0744 -0.0383 1354 TRP A CG    
1061 C  CD1   . TRP A 137 ? 0.8784 0.9260 1.0391 -0.0060 -0.0710 -0.0384 1354 TRP A CD1   
1062 C  CD2   . TRP A 137 ? 0.8141 0.8644 0.9621 -0.0066 -0.0776 -0.0358 1354 TRP A CD2   
1063 N  NE1   . TRP A 137 ? 0.9681 1.0191 1.1359 -0.0048 -0.0727 -0.0365 1354 TRP A NE1   
1064 C  CE2   . TRP A 137 ? 0.9108 0.9622 1.0701 -0.0052 -0.0762 -0.0352 1354 TRP A CE2   
1065 C  CE3   . TRP A 137 ? 0.8524 0.9042 0.9923 -0.0065 -0.0816 -0.0339 1354 TRP A CE3   
1066 C  CZ2   . TRP A 137 ? 0.9617 1.0142 1.1232 -0.0045 -0.0785 -0.0335 1354 TRP A CZ2   
1067 C  CZ3   . TRP A 137 ? 0.8744 0.9266 1.0163 -0.0047 -0.0830 -0.0317 1354 TRP A CZ3   
1068 C  CH2   . TRP A 137 ? 0.9663 1.0181 1.1183 -0.0042 -0.0813 -0.0320 1354 TRP A CH2   
1069 N  N     . ASN A 138 ? 0.6940 0.7327 0.7988 -0.0189 -0.0793 -0.0449 1355 ASN A N     
1070 C  CA    . ASN A 138 ? 0.6185 0.6564 0.7155 -0.0234 -0.0832 -0.0481 1355 ASN A CA    
1071 C  C     . ASN A 138 ? 0.8552 0.9006 0.9469 -0.0238 -0.0913 -0.0450 1355 ASN A C     
1072 O  O     . ASN A 138 ? 0.9247 0.9741 1.0178 -0.0202 -0.0928 -0.0404 1355 ASN A O     
1073 C  CB    . ASN A 138 ? 0.5684 0.5949 0.6514 -0.0266 -0.0779 -0.0536 1355 ASN A CB    
1074 C  CG    . ASN A 138 ? 0.6849 0.7072 0.7531 -0.0261 -0.0759 -0.0525 1355 ASN A CG    
1075 O  OD1   . ASN A 138 ? 0.8753 0.9032 0.9404 -0.0247 -0.0812 -0.0480 1355 ASN A OD1   
1076 N  ND2   . ASN A 138 ? 0.6058 0.6172 0.6640 -0.0269 -0.0674 -0.0563 1355 ASN A ND2   
1077 N  N     . ASN A 139 ? 0.9159 0.9628 1.0025 -0.0285 -0.0966 -0.0476 1356 ASN A N     
1078 C  CA    . ASN A 139 ? 0.7853 0.8409 0.8688 -0.0294 -0.1055 -0.0449 1356 ASN A CA    
1079 C  C     . ASN A 139 ? 0.7903 0.8396 0.8540 -0.0329 -0.1079 -0.0477 1356 ASN A C     
1080 O  O     . ASN A 139 ? 0.8228 0.8619 0.8763 -0.0369 -0.1043 -0.0538 1356 ASN A O     
1081 C  CB    . ASN A 139 ? 0.8424 0.9066 0.9374 -0.0327 -0.1108 -0.0454 1356 ASN A CB    
1082 C  CG    . ASN A 139 ? 0.8570 0.9135 0.9504 -0.0388 -0.1085 -0.0520 1356 ASN A CG    
1083 O  OD1   . ASN A 139 ? 0.9466 0.9925 1.0381 -0.0383 -0.1008 -0.0552 1356 ASN A OD1   
1084 N  ND2   . ASN A 139 ? 0.6126 0.6742 0.7079 -0.0445 -0.1152 -0.0541 1356 ASN A ND2   
1085 N  N     . VAL A 140 ? 0.9332 0.9873 0.9899 -0.0309 -0.1137 -0.0431 1357 VAL A N     
1086 C  CA    . VAL A 140 ? 0.9693 1.0185 1.0052 -0.0341 -0.1182 -0.0449 1357 VAL A CA    
1087 C  C     . VAL A 140 ? 0.8861 0.9483 0.9245 -0.0345 -0.1306 -0.0409 1357 VAL A C     
1088 O  O     . VAL A 140 ? 0.8470 0.9211 0.9028 -0.0310 -0.1337 -0.0358 1357 VAL A O     
1089 C  CB    . VAL A 140 ? 1.0147 1.0535 1.0342 -0.0309 -0.1117 -0.0426 1357 VAL A CB    
1090 C  CG1   . VAL A 140 ? 1.0297 1.0593 1.0539 -0.0294 -0.0990 -0.0452 1357 VAL A CG1   
1091 C  CG2   . VAL A 140 ? 0.8639 0.9088 0.8865 -0.0252 -0.1148 -0.0341 1357 VAL A CG2   
1092 N  N     . VAL A 141 ? 0.8214 0.8812 0.8421 -0.0389 -0.1376 -0.0435 1358 VAL A N     
1093 C  CA    . VAL A 141 ? 0.8192 0.8917 0.8410 -0.0399 -0.1510 -0.0400 1358 VAL A CA    
1094 C  C     . VAL A 141 ? 0.8109 0.8772 0.8078 -0.0384 -0.1550 -0.0369 1358 VAL A C     
1095 O  O     . VAL A 141 ? 0.8524 0.9048 0.8263 -0.0418 -0.1516 -0.0422 1358 VAL A O     
1096 C  CB    . VAL A 141 ? 0.8545 0.9321 0.8805 -0.0485 -0.1590 -0.0466 1358 VAL A CB    
1097 C  CG1   . VAL A 141 ? 0.7961 0.8894 0.8253 -0.0497 -0.1743 -0.0424 1358 VAL A CG1   
1098 C  CG2   . VAL A 141 ? 0.7060 0.7880 0.7559 -0.0501 -0.1536 -0.0488 1358 VAL A CG2   
1099 N  N     . ARG A 142 ? 0.8362 0.9120 0.8371 -0.0326 -0.1613 -0.0280 1359 ARG A N     
1100 C  CA    . ARG A 142 ? 0.9258 0.9982 0.9043 -0.0307 -0.1679 -0.0232 1359 ARG A CA    
1101 C  C     . ARG A 142 ? 0.9096 1.0001 0.8988 -0.0298 -0.1833 -0.0178 1359 ARG A C     
1102 O  O     . ARG A 142 ? 0.8648 0.9677 0.8770 -0.0243 -0.1842 -0.0115 1359 ARG A O     
1103 C  CB    . ARG A 142 ? 1.0261 1.0895 0.9979 -0.0231 -0.1589 -0.0159 1359 ARG A CB    
1104 C  CG    . ARG A 142 ? 1.1135 1.1605 1.0767 -0.0242 -0.1436 -0.0209 1359 ARG A CG    
1105 C  CD    . ARG A 142 ? 1.0894 1.1325 1.0617 -0.0175 -0.1337 -0.0146 1359 ARG A CD    
1106 N  NE    . ARG A 142 ? 1.0639 1.0926 1.0277 -0.0184 -0.1200 -0.0180 1359 ARG A NE    
1107 C  CZ    . ARG A 142 ? 1.1121 1.1344 1.0785 -0.0141 -0.1108 -0.0129 1359 ARG A CZ    
1108 N  NH1   . ARG A 142 ? 0.9356 0.9627 0.9106 -0.0087 -0.1139 -0.0049 1359 ARG A NH1   
1109 N  NH2   . ARG A 142 ? 1.2678 1.2789 1.2296 -0.0154 -0.0983 -0.0161 1359 ARG A NH2   
1110 N  N     . TRP A 143 ? 0.9259 1.0184 0.8999 -0.0356 -0.1953 -0.0210 1360 TRP A N     
1111 C  CA    . TRP A 143 ? 1.0139 1.1254 0.9993 -0.0361 -0.2118 -0.0166 1360 TRP A CA    
1112 C  C     . TRP A 143 ? 1.0931 1.2069 1.0694 -0.0274 -0.2173 -0.0051 1360 TRP A C     
1113 O  O     . TRP A 143 ? 1.1005 1.2114 1.0531 -0.0284 -0.2272 -0.0031 1360 TRP A O     
1114 C  CB    . TRP A 143 ? 1.1649 1.2771 1.1370 -0.0464 -0.2236 -0.0250 1360 TRP A CB    
1115 C  CG    . TRP A 143 ? 1.2766 1.4111 1.2763 -0.0501 -0.2360 -0.0246 1360 TRP A CG    
1116 C  CD1   . TRP A 143 ? 1.3624 1.5124 1.3638 -0.0517 -0.2539 -0.0208 1360 TRP A CD1   
1117 C  CD2   . TRP A 143 ? 1.1931 1.3380 1.2244 -0.0524 -0.2312 -0.0269 1360 TRP A CD2   
1118 N  NE1   . TRP A 143 ? 1.2817 1.4519 1.3160 -0.0553 -0.2601 -0.0211 1360 TRP A NE1   
1119 C  CE2   . TRP A 143 ? 1.1576 1.3243 1.2098 -0.0557 -0.2457 -0.0247 1360 TRP A CE2   
1120 C  CE3   . TRP A 143 ? 1.1074 1.2455 1.1513 -0.0518 -0.2161 -0.0302 1360 TRP A CE3   
1121 C  CZ2   . TRP A 143 ? 1.0813 1.2624 1.1661 -0.0586 -0.2441 -0.0256 1360 TRP A CZ2   
1122 C  CZ3   . TRP A 143 ? 1.0857 1.2372 1.1595 -0.0544 -0.2154 -0.0310 1360 TRP A CZ3   
1123 C  CH2   . TRP A 143 ? 1.0919 1.2642 1.1856 -0.0578 -0.2284 -0.0287 1360 TRP A CH2   
1124 N  N     . GLU A 144 ? 1.2279 1.3450 1.2218 -0.0187 -0.2100 0.0027  1361 GLU A N     
1125 C  CA    . GLU A 144 ? 1.4162 1.5309 1.4021 -0.0094 -0.2111 0.0139  1361 GLU A CA    
1126 C  C     . GLU A 144 ? 1.5624 1.6969 1.5625 -0.0052 -0.2266 0.0223  1361 GLU A C     
1127 O  O     . GLU A 144 ? 1.6001 1.7509 1.6305 -0.0029 -0.2281 0.0241  1361 GLU A O     
1128 C  CB    . GLU A 144 ? 1.3654 1.4737 1.3644 -0.0023 -0.1966 0.0177  1361 GLU A CB    
1129 C  CG    . GLU A 144 ? 1.3660 1.4533 1.3463 -0.0035 -0.1823 0.0142  1361 GLU A CG    
1130 C  CD    . GLU A 144 ? 1.4613 1.5437 1.4563 0.0028  -0.1701 0.0177  1361 GLU A CD    
1131 O  OE1   . GLU A 144 ? 1.4334 1.5034 1.4243 0.0006  -0.1578 0.0128  1361 GLU A OE1   
1132 O  OE2   . GLU A 144 ? 1.5389 1.6298 1.5500 0.0099  -0.1729 0.0252  1361 GLU A OE2   
1133 N  N     . PHE A 145 ? 1.6521 1.7852 1.6299 -0.0038 -0.2378 0.0278  1362 PHE A N     
1134 C  CA    . PHE A 145 ? 1.6807 1.8326 1.6702 0.0012  -0.2540 0.0372  1362 PHE A CA    
1135 C  C     . PHE A 145 ? 1.6717 1.8236 1.6729 0.0140  -0.2485 0.0496  1362 PHE A C     
1136 O  O     . PHE A 145 ? 1.6439 1.7893 1.6276 0.0206  -0.2523 0.0593  1362 PHE A O     
1137 C  CB    . PHE A 145 ? 1.6721 1.8214 1.6309 -0.0022 -0.2689 0.0384  1362 PHE A CB    
1138 N  N     . LYS A 146 ? 1.6262 1.7840 1.6563 0.0174  -0.2387 0.0491  1363 LYS A N     
1139 C  CA    . LYS A 146 ? 1.5414 1.7022 1.5890 0.0292  -0.2344 0.0594  1363 LYS A CA    
1140 C  C     . LYS A 146 ? 1.5578 1.7388 1.6425 0.0305  -0.2345 0.0583  1363 LYS A C     
1141 O  O     . LYS A 146 ? 1.5692 1.7615 1.6651 0.0222  -0.2386 0.0506  1363 LYS A O     
1142 C  CB    . LYS A 146 ? 1.4224 1.5615 1.4601 0.0330  -0.2172 0.0597  1363 LYS A CB    
1143 N  N     . HIS A 147 ? 1.5278 1.7112 1.6311 0.0410  -0.2284 0.0657  1364 HIS A N     
1144 C  CA    . HIS A 147 ? 1.4752 1.6763 1.6127 0.0436  -0.2263 0.0654  1364 HIS A CA    
1145 C  C     . HIS A 147 ? 1.3435 1.5340 1.4863 0.0412  -0.2101 0.0573  1364 HIS A C     
1146 O  O     . HIS A 147 ? 1.3779 1.5518 1.5131 0.0464  -0.1990 0.0587  1364 HIS A O     
1147 C  CB    . HIS A 147 ? 1.6234 1.8331 1.7789 0.0567  -0.2280 0.0773  1364 HIS A CB    
1148 C  CG    . HIS A 147 ? 1.6833 1.9115 1.8739 0.0603  -0.2248 0.0775  1364 HIS A CG    
1149 N  ND1   . HIS A 147 ? 1.6869 1.9078 1.8880 0.0626  -0.2093 0.0732  1364 HIS A ND1   
1150 C  CD2   . HIS A 147 ? 1.6899 1.9437 1.9075 0.0619  -0.2346 0.0817  1364 HIS A CD2   
1151 C  CE1   . HIS A 147 ? 1.6750 1.9150 1.9061 0.0659  -0.2086 0.0748  1364 HIS A CE1   
1152 N  NE2   . HIS A 147 ? 1.6722 1.9330 1.9156 0.0654  -0.2235 0.0800  1364 HIS A NE2   
1153 N  N     . PRO A 148 ? 1.1572 1.3560 1.3120 0.0332  -0.2086 0.0489  1365 PRO A N     
1154 C  CA    . PRO A 148 ? 1.1104 1.2973 1.2645 0.0297  -0.1948 0.0408  1365 PRO A CA    
1155 C  C     . PRO A 148 ? 1.0951 1.2838 1.2693 0.0374  -0.1843 0.0428  1365 PRO A C     
1156 O  O     . PRO A 148 ? 1.0165 1.2198 1.2116 0.0443  -0.1867 0.0490  1365 PRO A O     
1157 C  CB    . PRO A 148 ? 0.9660 1.1619 1.1259 0.0187  -0.1986 0.0325  1365 PRO A CB    
1158 C  CG    . PRO A 148 ? 0.9789 1.1981 1.1591 0.0194  -0.2111 0.0376  1365 PRO A CG    
1159 C  CD    . PRO A 148 ? 1.0769 1.2970 1.2479 0.0270  -0.2202 0.0472  1365 PRO A CD    
1160 N  N     . GLN A 149 ? 1.0588 1.2320 1.2258 0.0362  -0.1722 0.0371  1366 GLN A N     
1161 C  CA    . GLN A 149 ? 0.8989 1.0697 1.0792 0.0423  -0.1614 0.0370  1366 GLN A CA    
1162 C  C     . GLN A 149 ? 0.7937 0.9534 0.9682 0.0366  -0.1520 0.0283  1366 GLN A C     
1163 O  O     . GLN A 149 ? 0.7060 0.8525 0.8626 0.0316  -0.1505 0.0242  1366 GLN A O     
1164 C  CB    . GLN A 149 ? 0.8753 1.0343 1.0506 0.0521  -0.1572 0.0432  1366 GLN A CB    
1165 C  CG    . GLN A 149 ? 0.8852 1.0466 1.0781 0.0607  -0.1493 0.0452  1366 GLN A CG    
1166 C  CD    . GLN A 149 ? 1.0709 1.2190 1.2587 0.0701  -0.1454 0.0512  1366 GLN A CD    
1167 O  OE1   . GLN A 149 ? 1.1603 1.2968 1.3311 0.0697  -0.1478 0.0541  1366 GLN A OE1   
1168 N  NE2   . GLN A 149 ? 1.0904 1.2390 1.2924 0.0787  -0.1385 0.0532  1366 GLN A NE2   
1169 N  N     . PRO A 150 ? 0.8142 0.9786 1.0035 0.0383  -0.1451 0.0260  1367 PRO A N     
1170 C  CA    . PRO A 150 ? 0.8308 0.9889 1.0173 0.0323  -0.1383 0.0185  1367 PRO A CA    
1171 C  C     . PRO A 150 ? 1.0919 1.2320 1.2606 0.0288  -0.1335 0.0134  1367 PRO A C     
1172 O  O     . PRO A 150 ? 1.3043 1.4423 1.4688 0.0216  -0.1328 0.0078  1367 PRO A O     
1173 C  CB    . PRO A 150 ? 0.7650 0.9262 0.9655 0.0386  -0.1303 0.0193  1367 PRO A CB    
1174 C  CG    . PRO A 150 ? 0.7232 0.9024 0.9422 0.0437  -0.1354 0.0262  1367 PRO A CG    
1175 C  CD    . PRO A 150 ? 0.7647 0.9467 0.9768 0.0431  -0.1462 0.0305  1367 PRO A CD    
1176 N  N     . PHE A 151 ? 0.9680 1.0951 1.1280 0.0334  -0.1296 0.0149  1368 PHE A N     
1177 C  CA    . PHE A 151 ? 0.8724 0.9850 1.0186 0.0289  -0.1254 0.0099  1368 PHE A CA    
1178 C  C     . PHE A 151 ? 0.9298 1.0333 1.0611 0.0285  -0.1277 0.0128  1368 PHE A C     
1179 O  O     . PHE A 151 ? 0.9046 0.9985 1.0248 0.0236  -0.1249 0.0090  1368 PHE A O     
1180 C  CB    . PHE A 151 ? 0.7660 0.8685 0.9133 0.0320  -0.1174 0.0072  1368 PHE A CB    
1181 C  CG    . PHE A 151 ? 0.7824 0.8904 0.9390 0.0314  -0.1139 0.0035  1368 PHE A CG    
1182 C  CD1   . PHE A 151 ? 0.8422 0.9489 0.9964 0.0250  -0.1125 -0.0017 1368 PHE A CD1   
1183 C  CD2   . PHE A 151 ? 0.8957 1.0090 1.0626 0.0377  -0.1110 0.0057  1368 PHE A CD2   
1184 C  CE1   . PHE A 151 ? 0.7542 0.8646 0.9152 0.0248  -0.1090 -0.0041 1368 PHE A CE1   
1185 C  CE2   . PHE A 151 ? 0.8991 1.0162 1.0722 0.0373  -0.1067 0.0029  1368 PHE A CE2   
1186 C  CZ    . PHE A 151 ? 0.7675 0.8830 0.9370 0.0308  -0.1060 -0.0017 1368 PHE A CZ    
1187 N  N     . LEU A 152 ? 0.9052 1.0123 1.0363 0.0337  -0.1327 0.0199  1369 LEU A N     
1188 C  CA    . LEU A 152 ? 0.8561 0.9517 0.9723 0.0353  -0.1329 0.0243  1369 LEU A CA    
1189 C  C     . LEU A 152 ? 0.8559 0.9542 0.9585 0.0309  -0.1406 0.0258  1369 LEU A C     
1190 O  O     . LEU A 152 ? 1.0355 1.1216 1.1213 0.0281  -0.1380 0.0254  1369 LEU A O     
1191 C  CB    . LEU A 152 ? 0.8627 0.9569 0.9847 0.0448  -0.1328 0.0321  1369 LEU A CB    
1192 C  CG    . LEU A 152 ? 0.7256 0.8147 0.8584 0.0488  -0.1246 0.0292  1369 LEU A CG    
1193 C  CD1   . LEU A 152 ? 0.4871 0.5795 0.6312 0.0587  -0.1246 0.0357  1369 LEU A CD1   
1194 C  CD2   . LEU A 152 ? 0.4811 0.5524 0.6045 0.0469  -0.1173 0.0262  1369 LEU A CD2   
1195 N  N     . ARG A 153 ? 0.8368 0.9504 0.9461 0.0301  -0.1498 0.0273  1370 ARG A N     
1196 C  CA    . ARG A 153 ? 0.8509 0.9678 0.9466 0.0244  -0.1585 0.0267  1370 ARG A CA    
1197 C  C     . ARG A 153 ? 0.9566 1.0878 1.0650 0.0182  -0.1632 0.0211  1370 ARG A C     
1198 O  O     . ARG A 153 ? 0.8708 1.0183 0.9949 0.0201  -0.1705 0.0245  1370 ARG A O     
1199 C  CB    . ARG A 153 ? 0.8362 0.9576 0.9261 0.0297  -0.1680 0.0360  1370 ARG A CB    
1200 C  CG    . ARG A 153 ? 0.7993 0.9146 0.8640 0.0248  -0.1744 0.0360  1370 ARG A CG    
1201 N  N     . THR A 154 ? 0.9685 1.0934 1.0721 0.0110  -0.1581 0.0128  1371 THR A N     
1202 C  CA    . THR A 154 ? 0.8799 1.0143 0.9927 0.0039  -0.1612 0.0068  1371 THR A CA    
1203 C  C     . THR A 154 ? 0.9027 1.0300 0.9967 -0.0044 -0.1644 0.0009  1371 THR A C     
1204 O  O     . THR A 154 ? 1.0496 1.1620 1.1251 -0.0049 -0.1592 -0.0006 1371 THR A O     
1205 C  CB    . THR A 154 ? 0.7617 0.8938 0.8858 0.0030  -0.1518 0.0022  1371 THR A CB    
1206 O  OG1   . THR A 154 ? 0.7568 0.8734 0.8671 -0.0001 -0.1446 -0.0029 1371 THR A OG1   
1207 C  CG2   . THR A 154 ? 0.6735 0.8073 0.8102 0.0114  -0.1466 0.0068  1371 THR A CG2   
1208 N  N     . ARG A 155 ? 0.8540 0.9913 0.9531 -0.0110 -0.1723 -0.0027 1372 ARG A N     
1209 C  CA    . ARG A 155 ? 0.8375 0.9667 0.9168 -0.0191 -0.1759 -0.0092 1372 ARG A CA    
1210 C  C     . ARG A 155 ? 0.9029 1.0203 0.9790 -0.0242 -0.1660 -0.0175 1372 ARG A C     
1211 O  O     . ARG A 155 ? 1.0145 1.1175 1.0703 -0.0271 -0.1622 -0.0219 1372 ARG A O     
1212 C  CB    . ARG A 155 ? 0.8644 1.0077 0.9490 -0.0250 -0.1894 -0.0104 1372 ARG A CB    
1213 C  CG    . ARG A 155 ? 1.1036 1.2563 1.1849 -0.0200 -0.2009 -0.0021 1372 ARG A CG    
1214 C  CD    . ARG A 155 ? 1.3175 1.4780 1.3912 -0.0274 -0.2159 -0.0048 1372 ARG A CD    
1215 N  NE    . ARG A 155 ? 1.3770 1.5603 1.4787 -0.0287 -0.2254 -0.0022 1372 ARG A NE    
1216 C  CZ    . ARG A 155 ? 1.3917 1.5908 1.5025 -0.0238 -0.2369 0.0063  1372 ARG A CZ    
1217 N  NH1   . ARG A 155 ? 1.3948 1.5877 1.4868 -0.0170 -0.2406 0.0131  1372 ARG A NH1   
1218 N  NH2   . ARG A 155 ? 1.3861 1.6071 1.5256 -0.0253 -0.2444 0.0085  1372 ARG A NH2   
1219 N  N     . GLU A 156 ? 0.8088 0.9313 0.9042 -0.0249 -0.1611 -0.0194 1373 GLU A N     
1220 C  CA    . GLU A 156 ? 0.9156 1.0262 1.0093 -0.0270 -0.1507 -0.0251 1373 GLU A CA    
1221 C  C     . GLU A 156 ? 0.9755 1.0837 1.0775 -0.0197 -0.1422 -0.0212 1373 GLU A C     
1222 O  O     . GLU A 156 ? 1.0728 1.1912 1.1897 -0.0149 -0.1432 -0.0163 1373 GLU A O     
1223 C  CB    . GLU A 156 ? 0.8572 0.9718 0.9634 -0.0335 -0.1504 -0.0302 1373 GLU A CB    
1224 C  CG    . GLU A 156 ? 0.8078 0.9104 0.9142 -0.0342 -0.1394 -0.0347 1373 GLU A CG    
1225 C  CD    . GLU A 156 ? 0.8258 0.9341 0.9501 -0.0368 -0.1372 -0.0358 1373 GLU A CD    
1226 O  OE1   . GLU A 156 ? 0.8268 0.9488 0.9650 -0.0383 -0.1429 -0.0332 1373 GLU A OE1   
1227 O  OE2   . GLU A 156 ? 0.8113 0.9106 0.9366 -0.0373 -0.1294 -0.0386 1373 GLU A OE2   
1228 N  N     . PHE A 157 ? 0.8335 0.9285 0.9262 -0.0189 -0.1339 -0.0236 1374 PHE A N     
1229 C  CA    . PHE A 157 ? 0.7580 0.8499 0.8585 -0.0134 -0.1267 -0.0213 1374 PHE A CA    
1230 C  C     . PHE A 157 ? 0.7953 0.8763 0.8927 -0.0154 -0.1184 -0.0262 1374 PHE A C     
1231 O  O     . PHE A 157 ? 0.8129 0.8859 0.8987 -0.0197 -0.1167 -0.0306 1374 PHE A O     
1232 C  CB    . PHE A 157 ? 0.7335 0.8220 0.8281 -0.0074 -0.1260 -0.0157 1374 PHE A CB    
1233 C  CG    . PHE A 157 ? 0.6298 0.7066 0.7058 -0.0089 -0.1234 -0.0163 1374 PHE A CG    
1234 C  CD1   . PHE A 157 ? 0.6877 0.7538 0.7606 -0.0087 -0.1145 -0.0184 1374 PHE A CD1   
1235 C  CD2   . PHE A 157 ? 0.7034 0.7802 0.7647 -0.0103 -0.1300 -0.0146 1374 PHE A CD2   
1236 C  CE1   . PHE A 157 ? 0.7560 0.8112 0.8123 -0.0099 -0.1104 -0.0186 1374 PHE A CE1   
1237 C  CE2   . PHE A 157 ? 0.7313 0.7959 0.7726 -0.0114 -0.1264 -0.0148 1374 PHE A CE2   
1238 C  CZ    . PHE A 157 ? 0.7550 0.8087 0.7942 -0.0111 -0.1157 -0.0168 1374 PHE A CZ    
1239 N  N     . LEU A 158 ? 0.7780 0.8583 0.8853 -0.0118 -0.1134 -0.0253 1375 LEU A N     
1240 C  CA    . LEU A 158 ? 0.7497 0.8215 0.8575 -0.0123 -0.1063 -0.0286 1375 LEU A CA    
1241 C  C     . LEU A 158 ? 0.8612 0.9255 0.9630 -0.0096 -0.1020 -0.0268 1375 LEU A C     
1242 O  O     . LEU A 158 ? 0.8880 0.9536 0.9899 -0.0058 -0.1035 -0.0225 1375 LEU A O     
1243 C  CB    . LEU A 158 ? 0.6091 0.6845 0.7300 -0.0101 -0.1044 -0.0283 1375 LEU A CB    
1244 C  CG    . LEU A 158 ? 0.6623 0.7461 0.7918 -0.0117 -0.1075 -0.0281 1375 LEU A CG    
1245 C  CD1   . LEU A 158 ? 0.5741 0.6580 0.7121 -0.0088 -0.1040 -0.0275 1375 LEU A CD1   
1246 C  CD2   . LEU A 158 ? 0.7311 0.8130 0.8575 -0.0181 -0.1085 -0.0323 1375 LEU A CD2   
1247 N  N     . TRP A 159 ? 0.8421 0.8983 0.9403 -0.0115 -0.0959 -0.0300 1376 TRP A N     
1248 C  CA    . TRP A 159 ? 0.6883 0.7383 0.7855 -0.0095 -0.0904 -0.0284 1376 TRP A CA    
1249 C  C     . TRP A 159 ? 0.6946 0.7399 0.7970 -0.0109 -0.0837 -0.0321 1376 TRP A C     
1250 O  O     . TRP A 159 ? 0.7528 0.7986 0.8585 -0.0128 -0.0834 -0.0356 1376 TRP A O     
1251 C  CB    . TRP A 159 ? 0.6877 0.7318 0.7694 -0.0098 -0.0895 -0.0260 1376 TRP A CB    
1252 C  CG    . TRP A 159 ? 0.6592 0.6964 0.7269 -0.0137 -0.0862 -0.0298 1376 TRP A CG    
1253 C  CD1   . TRP A 159 ? 0.7141 0.7499 0.7825 -0.0170 -0.0846 -0.0354 1376 TRP A CD1   
1254 C  CD2   . TRP A 159 ? 0.7785 0.8077 0.8275 -0.0146 -0.0837 -0.0284 1376 TRP A CD2   
1255 N  NE1   . TRP A 159 ? 0.7655 0.7925 0.8167 -0.0199 -0.0812 -0.0386 1376 TRP A NE1   
1256 C  CE2   . TRP A 159 ? 0.7670 0.7901 0.8051 -0.0185 -0.0807 -0.0343 1376 TRP A CE2   
1257 C  CE3   . TRP A 159 ? 0.7142 0.7396 0.7534 -0.0122 -0.0833 -0.0225 1376 TRP A CE3   
1258 C  CZ2   . TRP A 159 ? 0.7509 0.7643 0.7669 -0.0202 -0.0772 -0.0349 1376 TRP A CZ2   
1259 C  CZ3   . TRP A 159 ? 0.8131 0.8293 0.8309 -0.0137 -0.0801 -0.0221 1376 TRP A CZ3   
1260 C  CH2   . TRP A 159 ? 0.8345 0.8447 0.8400 -0.0178 -0.0770 -0.0286 1376 TRP A CH2   
1261 N  N     . GLN A 160 ? 0.7766 0.8173 0.8812 -0.0099 -0.0781 -0.0310 1377 GLN A N     
1262 C  CA    . GLN A 160 ? 0.7326 0.7681 0.8399 -0.0113 -0.0702 -0.0339 1377 GLN A CA    
1263 C  C     . GLN A 160 ? 0.8691 0.8968 0.9625 -0.0124 -0.0643 -0.0329 1377 GLN A C     
1264 O  O     . GLN A 160 ? 1.0195 1.0455 1.1065 -0.0113 -0.0654 -0.0286 1377 GLN A O     
1265 C  CB    . GLN A 160 ? 0.6970 0.7348 0.8213 -0.0096 -0.0676 -0.0334 1377 GLN A CB    
1266 C  CG    . GLN A 160 ? 0.8290 0.8657 0.9556 -0.0086 -0.0672 -0.0298 1377 GLN A CG    
1267 C  CD    . GLN A 160 ? 0.9467 0.9768 1.0710 -0.0099 -0.0582 -0.0286 1377 GLN A CD    
1268 O  OE1   . GLN A 160 ? 0.8668 0.8928 0.9856 -0.0113 -0.0515 -0.0305 1377 GLN A OE1   
1269 N  NE2   . GLN A 160 ? 1.1830 1.2112 1.3103 -0.0096 -0.0573 -0.0252 1377 GLN A NE2   
1270 N  N     . GLU A 161 ? 0.7828 0.8044 0.8704 -0.0143 -0.0576 -0.0366 1378 GLU A N     
1271 C  CA    . GLU A 161 ? 0.8028 0.8154 0.8775 -0.0152 -0.0488 -0.0363 1378 GLU A CA    
1272 C  C     . GLU A 161 ? 0.8451 0.8553 0.9323 -0.0148 -0.0383 -0.0385 1378 GLU A C     
1273 O  O     . GLU A 161 ? 0.8126 0.8231 0.9065 -0.0149 -0.0367 -0.0427 1378 GLU A O     
1274 C  CB    . GLU A 161 ? 0.7674 0.7733 0.8190 -0.0177 -0.0499 -0.0392 1378 GLU A CB    
1275 C  CG    . GLU A 161 ? 0.7899 0.7952 0.8403 -0.0200 -0.0522 -0.0455 1378 GLU A CG    
1276 C  CD    . GLU A 161 ? 0.8857 0.8823 0.9105 -0.0234 -0.0528 -0.0492 1378 GLU A CD    
1277 O  OE1   . GLU A 161 ? 0.8859 0.8735 0.8941 -0.0234 -0.0459 -0.0485 1378 GLU A OE1   
1278 O  OE2   . GLU A 161 ? 0.8352 0.8336 0.8560 -0.0264 -0.0604 -0.0529 1378 GLU A OE2   
1279 N  N     . GLY A 162 ? 0.8207 0.8293 0.9136 -0.0142 -0.0311 -0.0352 1379 GLY A N     
1280 C  CA    . GLY A 162 ? 0.7883 0.7961 0.8956 -0.0138 -0.0203 -0.0363 1379 GLY A CA    
1281 C  C     . GLY A 162 ? 0.8806 0.8777 0.9715 -0.0147 -0.0083 -0.0361 1379 GLY A C     
1282 O  O     . GLY A 162 ? 0.9714 0.9634 1.0466 -0.0154 -0.0079 -0.0322 1379 GLY A O     
1283 N  N     . HIS A 163 ? 0.8177 0.8108 0.9114 -0.0143 0.0018  -0.0401 1380 HIS A N     
1284 C  CA    . HIS A 163 ? 0.8159 0.7975 0.8925 -0.0148 0.0153  -0.0410 1380 HIS A CA    
1285 C  C     . HIS A 163 ? 0.8699 0.8535 0.9685 -0.0131 0.0286  -0.0413 1380 HIS A C     
1286 O  O     . HIS A 163 ? 0.9189 0.9083 1.0368 -0.0112 0.0279  -0.0441 1380 HIS A O     
1287 C  CB    . HIS A 163 ? 0.7899 0.7616 0.8413 -0.0159 0.0149  -0.0471 1380 HIS A CB    
1288 C  CG    . HIS A 163 ? 0.8194 0.7911 0.8517 -0.0179 0.0012  -0.0466 1380 HIS A CG    
1289 N  ND1   . HIS A 163 ? 0.8961 0.8596 0.9008 -0.0192 0.0008  -0.0445 1380 HIS A ND1   
1290 C  CD2   . HIS A 163 ? 0.8606 0.8405 0.8989 -0.0184 -0.0126 -0.0472 1380 HIS A CD2   
1291 C  CE1   . HIS A 163 ? 0.9223 0.8900 0.9183 -0.0204 -0.0135 -0.0440 1380 HIS A CE1   
1292 N  NE2   . HIS A 163 ? 0.8516 0.8294 0.8682 -0.0201 -0.0212 -0.0457 1380 HIS A NE2   
1293 N  N     . THR A 164 ? 0.7163 0.6958 0.8138 -0.0135 0.0405  -0.0374 1381 THR A N     
1294 C  CA    . THR A 164 ? 0.6244 0.6095 0.7493 -0.0123 0.0523  -0.0357 1381 THR A CA    
1295 C  C     . THR A 164 ? 0.7166 0.6903 0.8275 -0.0123 0.0708  -0.0349 1381 THR A C     
1296 O  O     . THR A 164 ? 0.7216 0.6849 0.8050 -0.0138 0.0731  -0.0324 1381 THR A O     
1297 C  CB    . THR A 164 ? 0.6695 0.6657 0.8186 -0.0137 0.0467  -0.0301 1381 THR A CB    
1298 O  OG1   . THR A 164 ? 0.7991 0.7886 0.9307 -0.0159 0.0467  -0.0252 1381 THR A OG1   
1299 C  CG2   . THR A 164 ? 0.5849 0.5915 0.7466 -0.0133 0.0296  -0.0312 1381 THR A CG2   
1300 N  N     . ALA A 165 ? 0.6926 0.6684 0.8230 -0.0101 0.0843  -0.0365 1382 ALA A N     
1301 C  CA    . ALA A 165 ? 0.8649 0.8304 0.9855 -0.0093 0.1047  -0.0363 1382 ALA A CA    
1302 C  C     . ALA A 165 ? 0.8290 0.8055 0.9879 -0.0078 0.1167  -0.0332 1382 ALA A C     
1303 O  O     . ALA A 165 ? 0.8460 0.8331 1.0325 -0.0051 0.1141  -0.0354 1382 ALA A O     
1304 C  CB    . ALA A 165 ? 0.9319 0.8841 1.0294 -0.0071 0.1118  -0.0441 1382 ALA A CB    
1305 N  N     . PHE A 166 ? 0.7393 0.7133 0.9001 -0.0097 0.1299  -0.0276 1383 PHE A N     
1306 C  CA    . PHE A 166 ? 0.7671 0.7526 0.9658 -0.0094 0.1419  -0.0237 1383 PHE A CA    
1307 C  C     . PHE A 166 ? 0.8992 0.8736 1.0872 -0.0085 0.1664  -0.0222 1383 PHE A C     
1308 O  O     . PHE A 166 ? 0.8132 0.7702 0.9616 -0.0089 0.1727  -0.0227 1383 PHE A O     
1309 C  CB    . PHE A 166 ? 0.7436 0.7392 0.9628 -0.0140 0.1344  -0.0172 1383 PHE A CB    
1310 C  CG    . PHE A 166 ? 0.7734 0.7766 0.9959 -0.0154 0.1114  -0.0181 1383 PHE A CG    
1311 C  CD1   . PHE A 166 ? 0.7219 0.7158 0.9127 -0.0168 0.1002  -0.0177 1383 PHE A CD1   
1312 C  CD2   . PHE A 166 ? 0.7958 0.8160 1.0537 -0.0150 0.1012  -0.0188 1383 PHE A CD2   
1313 C  CE1   . PHE A 166 ? 0.6985 0.6995 0.8935 -0.0177 0.0807  -0.0184 1383 PHE A CE1   
1314 C  CE2   . PHE A 166 ? 0.7297 0.7559 0.9890 -0.0162 0.0812  -0.0197 1383 PHE A CE2   
1315 C  CZ    . PHE A 166 ? 0.6326 0.6491 0.8610 -0.0174 0.0716  -0.0196 1383 PHE A CZ    
1316 N  N     . ALA A 167 ? 0.9683 0.9535 1.1929 -0.0074 0.1800  -0.0196 1384 ALA A N     
1317 C  CA    . ALA A 167 ? 0.9501 0.9266 1.1703 -0.0066 0.2055  -0.0169 1384 ALA A CA    
1318 C  C     . ALA A 167 ? 0.9742 0.9473 1.1896 -0.0119 0.2111  -0.0086 1384 ALA A C     
1319 O  O     . ALA A 167 ? 1.1444 1.1011 1.3297 -0.0120 0.2270  -0.0063 1384 ALA A O     
1320 C  CB    . ALA A 167 ? 0.8124 0.8030 1.0766 -0.0031 0.2190  -0.0167 1384 ALA A CB    
1321 N  N     . THR A 168 ? 0.7858 0.7725 1.0290 -0.0162 0.1989  -0.0041 1385 THR A N     
1322 C  CA    . THR A 168 ? 0.9403 0.9240 1.1844 -0.0216 0.2043  0.0040  1385 THR A CA    
1323 C  C     . THR A 168 ? 0.9023 0.8763 1.1153 -0.0242 0.1874  0.0059  1385 THR A C     
1324 O  O     . THR A 168 ? 0.8240 0.8025 1.0331 -0.0235 0.1668  0.0018  1385 THR A O     
1325 C  CB    . THR A 168 ? 0.9588 0.9628 1.2553 -0.0256 0.2021  0.0077  1385 THR A CB    
1326 O  OG1   . THR A 168 ? 1.1784 1.1975 1.4964 -0.0244 0.1814  0.0027  1385 THR A OG1   
1327 C  CG2   . THR A 168 ? 0.7578 0.7691 1.0839 -0.0242 0.2244  0.0095  1385 THR A CG2   
1328 N  N     . GLN A 169 ? 0.9864 0.9479 1.1803 -0.0272 0.1965  0.0131  1386 GLN A N     
1329 C  CA    . GLN A 169 ? 1.0489 1.0035 1.2217 -0.0295 0.1806  0.0164  1386 GLN A CA    
1330 C  C     . GLN A 169 ? 0.8868 0.8559 1.0953 -0.0337 0.1660  0.0178  1386 GLN A C     
1331 O  O     . GLN A 169 ? 0.7928 0.7608 0.9903 -0.0341 0.1477  0.0171  1386 GLN A O     
1332 C  CB    . GLN A 169 ? 1.1885 1.1251 1.3319 -0.0310 0.1939  0.0249  1386 GLN A CB    
1333 C  CG    . GLN A 169 ? 1.2681 1.1921 1.3706 -0.0296 0.1794  0.0261  1386 GLN A CG    
1334 C  CD    . GLN A 169 ? 1.3030 1.2074 1.3695 -0.0295 0.1930  0.0343  1386 GLN A CD    
1335 O  OE1   . GLN A 169 ? 1.2866 1.1778 1.3108 -0.0264 0.1911  0.0332  1386 GLN A OE1   
1336 N  NE2   . GLN A 169 ? 1.3516 1.2534 1.4341 -0.0333 0.2066  0.0428  1386 GLN A NE2   
1337 N  N     . LYS A 170 ? 0.8252 0.8082 1.0768 -0.0367 0.1732  0.0190  1387 LYS A N     
1338 C  CA    . LYS A 170 ? 0.7691 0.7651 1.0538 -0.0415 0.1590  0.0194  1387 LYS A CA    
1339 C  C     . LYS A 170 ? 0.8251 0.8319 1.1151 -0.0389 0.1367  0.0121  1387 LYS A C     
1340 O  O     . LYS A 170 ? 0.8835 0.8904 1.1705 -0.0408 0.1197  0.0115  1387 LYS A O     
1341 C  CB    . LYS A 170 ? 0.7819 0.7923 1.1134 -0.0456 0.1710  0.0218  1387 LYS A CB    
1342 C  CG    . LYS A 170 ? 0.8150 0.8406 1.1829 -0.0510 0.1546  0.0204  1387 LYS A CG    
1343 C  CD    . LYS A 170 ? 0.8405 0.8800 1.2551 -0.0565 0.1659  0.0236  1387 LYS A CD    
1344 C  CE    . LYS A 170 ? 0.9078 0.9692 1.3615 -0.0583 0.1479  0.0185  1387 LYS A CE    
1345 N  NZ    . LYS A 170 ? 0.9970 1.0733 1.4990 -0.0652 0.1559  0.0218  1387 LYS A NZ    
1346 N  N     . GLU A 171 ? 0.7853 0.8003 1.0831 -0.0344 0.1375  0.0066  1388 GLU A N     
1347 C  CA    . GLU A 171 ? 0.8300 0.8526 1.1275 -0.0312 0.1182  0.0002  1388 GLU A CA    
1348 C  C     . GLU A 171 ? 0.8744 0.8849 1.1335 -0.0300 0.1050  -0.0008 1388 GLU A C     
1349 O  O     . GLU A 171 ? 0.9565 0.9721 1.2187 -0.0307 0.0870  -0.0028 1388 GLU A O     
1350 C  CB    . GLU A 171 ? 0.9161 0.9422 1.2162 -0.0255 0.1248  -0.0046 1388 GLU A CB    
1351 C  CG    . GLU A 171 ? 0.8634 0.9063 1.2076 -0.0247 0.1330  -0.0045 1388 GLU A CG    
1352 C  CD    . GLU A 171 ? 0.8339 0.8753 1.1747 -0.0180 0.1430  -0.0087 1388 GLU A CD    
1353 O  OE1   . GLU A 171 ? 0.7789 0.8259 1.1229 -0.0141 0.1306  -0.0134 1388 GLU A OE1   
1354 O  OE2   . GLU A 171 ? 0.6926 0.7256 1.0260 -0.0166 0.1643  -0.0073 1388 GLU A OE2   
1355 N  N     . ALA A 172 ? 0.8448 0.8393 1.0675 -0.0282 0.1139  0.0006  1389 ALA A N     
1356 C  CA    . ALA A 172 ? 0.8950 0.8795 1.0822 -0.0267 0.1014  -0.0002 1389 ALA A CA    
1357 C  C     . ALA A 172 ? 0.9062 0.8880 1.0922 -0.0299 0.0919  0.0048  1389 ALA A C     
1358 O  O     . ALA A 172 ? 0.7969 0.7812 0.9774 -0.0291 0.0748  0.0026  1389 ALA A O     
1359 C  CB    . ALA A 172 ? 0.9233 0.8914 1.0721 -0.0245 0.1131  0.0004  1389 ALA A CB    
1360 N  N     . ASP A 173 ? 0.9169 0.8930 1.1089 -0.0334 0.1037  0.0115  1390 ASP A N     
1361 C  CA    . ASP A 173 ? 0.8224 0.7938 1.0150 -0.0365 0.0966  0.0165  1390 ASP A CA    
1362 C  C     . ASP A 173 ? 0.7408 0.7253 0.9608 -0.0384 0.0801  0.0123  1390 ASP A C     
1363 O  O     . ASP A 173 ? 0.7799 0.7620 0.9891 -0.0375 0.0656  0.0115  1390 ASP A O     
1364 C  CB    . ASP A 173 ? 0.6190 0.5843 0.8232 -0.0410 0.1136  0.0239  1390 ASP A CB    
1365 C  CG    . ASP A 173 ? 0.8386 0.7866 1.0083 -0.0392 0.1292  0.0302  1390 ASP A CG    
1366 O  OD1   . ASP A 173 ? 0.8208 0.7580 0.9546 -0.0357 0.1223  0.0315  1390 ASP A OD1   
1367 O  OD2   . ASP A 173 ? 0.7622 0.7076 0.9408 -0.0413 0.1486  0.0342  1390 ASP A OD2   
1368 N  N     . GLU A 174 ? 0.6478 0.6466 0.9032 -0.0407 0.0821  0.0093  1391 GLU A N     
1369 C  CA    . GLU A 174 ? 0.6643 0.6751 0.9453 -0.0431 0.0666  0.0054  1391 GLU A CA    
1370 C  C     . GLU A 174 ? 0.7409 0.7556 1.0086 -0.0385 0.0499  -0.0003 1391 GLU A C     
1371 O  O     . GLU A 174 ? 0.6556 0.6719 0.9250 -0.0393 0.0355  -0.0022 1391 GLU A O     
1372 C  CB    . GLU A 174 ? 0.6460 0.6728 0.9672 -0.0459 0.0711  0.0038  1391 GLU A CB    
1373 C  CG    . GLU A 174 ? 0.7906 0.8154 1.1287 -0.0507 0.0896  0.0095  1391 GLU A CG    
1374 C  CD    . GLU A 174 ? 0.8822 0.9256 1.2661 -0.0543 0.0918  0.0082  1391 GLU A CD    
1375 O  OE1   . GLU A 174 ? 0.8768 0.9335 1.2745 -0.0507 0.0843  0.0035  1391 GLU A OE1   
1376 O  OE2   . GLU A 174 ? 0.8795 0.9242 1.2864 -0.0607 0.1008  0.0124  1391 GLU A OE2   
1377 N  N     . GLU A 175 ? 0.7807 0.7954 1.0334 -0.0339 0.0523  -0.0030 1392 GLU A N     
1378 C  CA    . GLU A 175 ? 0.8211 0.8386 1.0609 -0.0301 0.0374  -0.0078 1392 GLU A CA    
1379 C  C     . GLU A 175 ? 0.9328 0.9399 1.1448 -0.0291 0.0291  -0.0059 1392 GLU A C     
1380 O  O     . GLU A 175 ? 0.8965 0.9073 1.1071 -0.0278 0.0148  -0.0086 1392 GLU A O     
1381 C  CB    . GLU A 175 ? 0.7408 0.7584 0.9695 -0.0260 0.0419  -0.0113 1392 GLU A CB    
1382 C  CG    . GLU A 175 ? 0.8115 0.8314 1.0276 -0.0229 0.0265  -0.0157 1392 GLU A CG    
1383 C  CD    . GLU A 175 ? 0.8028 0.8211 1.0074 -0.0195 0.0299  -0.0198 1392 GLU A CD    
1384 O  OE1   . GLU A 175 ? 0.7578 0.7853 0.9806 -0.0176 0.0269  -0.0230 1392 GLU A OE1   
1385 O  OE2   . GLU A 175 ? 0.9195 0.9267 1.0964 -0.0187 0.0352  -0.0196 1392 GLU A OE2   
1386 N  N     . VAL A 176 ? 0.9628 0.9571 1.1512 -0.0289 0.0380  -0.0011 1393 VAL A N     
1387 C  CA    . VAL A 176 ? 0.8506 0.8358 1.0142 -0.0272 0.0299  0.0018  1393 VAL A CA    
1388 C  C     . VAL A 176 ? 0.7639 0.7509 0.9423 -0.0291 0.0203  0.0025  1393 VAL A C     
1389 O  O     . VAL A 176 ? 0.7163 0.7044 0.8874 -0.0268 0.0075  0.0007  1393 VAL A O     
1390 C  CB    . VAL A 176 ? 0.7611 0.7319 0.9002 -0.0270 0.0414  0.0085  1393 VAL A CB    
1391 C  CG1   . VAL A 176 ? 0.8079 0.7708 0.9260 -0.0248 0.0322  0.0125  1393 VAL A CG1   
1392 C  CG2   . VAL A 176 ? 0.7575 0.7244 0.8760 -0.0249 0.0493  0.0066  1393 VAL A CG2   
1393 N  N     . LEU A 177 ? 0.7458 0.7336 0.9469 -0.0337 0.0268  0.0044  1394 LEU A N     
1394 C  CA    . LEU A 177 ? 0.7779 0.7649 0.9917 -0.0364 0.0182  0.0043  1394 LEU A CA    
1395 C  C     . LEU A 177 ? 0.8176 0.8172 1.0480 -0.0362 0.0042  -0.0029 1394 LEU A C     
1396 O  O     . LEU A 177 ? 0.7832 0.7808 1.0116 -0.0357 -0.0065 -0.0047 1394 LEU A O     
1397 C  CB    . LEU A 177 ? 0.7915 0.7748 1.0250 -0.0424 0.0289  0.0082  1394 LEU A CB    
1398 C  CG    . LEU A 177 ? 0.8602 0.8274 1.0733 -0.0423 0.0412  0.0167  1394 LEU A CG    
1399 C  CD1   . LEU A 177 ? 0.7320 0.6932 0.9648 -0.0488 0.0503  0.0211  1394 LEU A CD1   
1400 C  CD2   . LEU A 177 ? 0.8809 0.8377 1.0653 -0.0373 0.0328  0.0195  1394 LEU A CD2   
1401 N  N     . THR A 178 ? 0.8003 0.8122 1.0467 -0.0361 0.0046  -0.0068 1395 THR A N     
1402 C  CA    . THR A 178 ? 0.7690 0.7922 1.0283 -0.0353 -0.0091 -0.0127 1395 THR A CA    
1403 C  C     . THR A 178 ? 0.7395 0.7612 0.9762 -0.0301 -0.0191 -0.0148 1395 THR A C     
1404 O  O     . THR A 178 ? 0.7566 0.7805 0.9941 -0.0293 -0.0309 -0.0179 1395 THR A O     
1405 C  CB    . THR A 178 ? 0.7684 0.8045 1.0495 -0.0354 -0.0059 -0.0150 1395 THR A CB    
1406 O  OG1   . THR A 178 ? 0.6321 0.6686 0.9303 -0.0394 0.0076  -0.0116 1395 THR A OG1   
1407 C  CG2   . THR A 178 ? 0.8544 0.9023 1.1554 -0.0362 -0.0193 -0.0196 1395 THR A CG2   
1408 N  N     . ILE A 179 ? 0.6343 0.6518 0.8503 -0.0268 -0.0143 -0.0133 1396 ILE A N     
1409 C  CA    . ILE A 179 ? 0.7416 0.7583 0.9381 -0.0227 -0.0235 -0.0149 1396 ILE A CA    
1410 C  C     . ILE A 179 ? 0.8137 0.8223 0.9981 -0.0218 -0.0288 -0.0122 1396 ILE A C     
1411 O  O     . ILE A 179 ? 0.8673 0.8781 1.0471 -0.0193 -0.0390 -0.0144 1396 ILE A O     
1412 C  CB    . ILE A 179 ? 0.7380 0.7514 0.9150 -0.0203 -0.0180 -0.0145 1396 ILE A CB    
1413 C  CG1   . ILE A 179 ? 0.7086 0.7285 0.8983 -0.0204 -0.0117 -0.0177 1396 ILE A CG1   
1414 C  CG2   . ILE A 179 ? 0.7273 0.7415 0.8877 -0.0170 -0.0283 -0.0162 1396 ILE A CG2   
1415 C  CD1   . ILE A 179 ? 0.6464 0.6767 0.8494 -0.0189 -0.0213 -0.0220 1396 ILE A CD1   
1416 N  N     . LEU A 180 ? 0.7008 0.6994 0.8802 -0.0235 -0.0212 -0.0070 1397 LEU A N     
1417 C  CA    . LEU A 180 ? 0.7175 0.7073 0.8861 -0.0218 -0.0257 -0.0037 1397 LEU A CA    
1418 C  C     . LEU A 180 ? 0.6999 0.6911 0.8843 -0.0235 -0.0332 -0.0074 1397 LEU A C     
1419 O  O     . LEU A 180 ? 0.6942 0.6824 0.8707 -0.0204 -0.0408 -0.0079 1397 LEU A O     
1420 C  CB    . LEU A 180 ? 0.7666 0.7438 0.9254 -0.0228 -0.0154 0.0036  1397 LEU A CB    
1421 C  CG    . LEU A 180 ? 0.8816 0.8483 1.0229 -0.0190 -0.0189 0.0090  1397 LEU A CG    
1422 C  CD1   . LEU A 180 ? 1.0407 1.0102 1.1614 -0.0138 -0.0254 0.0095  1397 LEU A CD1   
1423 C  CD2   . LEU A 180 ? 0.9281 0.8814 1.0613 -0.0203 -0.0080 0.0170  1397 LEU A CD2   
1424 N  N     . ASP A 181 ? 0.6412 0.6370 0.8481 -0.0285 -0.0314 -0.0101 1398 ASP A N     
1425 C  CA    . ASP A 181 ? 0.6596 0.6571 0.8802 -0.0308 -0.0401 -0.0149 1398 ASP A CA    
1426 C  C     . ASP A 181 ? 0.7410 0.7467 0.9575 -0.0270 -0.0514 -0.0200 1398 ASP A C     
1427 O  O     . ASP A 181 ? 0.7572 0.7596 0.9706 -0.0258 -0.0592 -0.0229 1398 ASP A O     
1428 C  CB    . ASP A 181 ? 0.6610 0.6644 0.9082 -0.0374 -0.0376 -0.0170 1398 ASP A CB    
1429 C  CG    . ASP A 181 ? 0.9115 0.9130 1.1708 -0.0412 -0.0464 -0.0219 1398 ASP A CG    
1430 O  OD1   . ASP A 181 ? 0.9328 0.9443 1.2020 -0.0417 -0.0559 -0.0275 1398 ASP A OD1   
1431 O  OD2   . ASP A 181 ? 0.9985 0.9873 1.2558 -0.0435 -0.0441 -0.0202 1398 ASP A OD2   
1432 N  N     . LEU A 182 ? 0.8016 0.8165 1.0167 -0.0248 -0.0515 -0.0210 1399 LEU A N     
1433 C  CA    . LEU A 182 ? 0.7933 0.8149 1.0038 -0.0212 -0.0613 -0.0249 1399 LEU A CA    
1434 C  C     . LEU A 182 ? 0.7192 0.7356 0.9092 -0.0165 -0.0643 -0.0231 1399 LEU A C     
1435 O  O     . LEU A 182 ? 0.6064 0.6239 0.7931 -0.0140 -0.0720 -0.0259 1399 LEU A O     
1436 C  CB    . LEU A 182 ? 0.7016 0.7330 0.9165 -0.0201 -0.0605 -0.0262 1399 LEU A CB    
1437 C  CG    . LEU A 182 ? 0.6700 0.7100 0.9081 -0.0233 -0.0594 -0.0280 1399 LEU A CG    
1438 C  CD1   . LEU A 182 ? 0.5458 0.5925 0.7851 -0.0208 -0.0556 -0.0282 1399 LEU A CD1   
1439 C  CD2   . LEU A 182 ? 0.4809 0.5258 0.7300 -0.0245 -0.0704 -0.0321 1399 LEU A CD2   
1440 N  N     . TYR A 183 ? 0.6374 0.6483 0.8139 -0.0150 -0.0585 -0.0184 1400 TYR A N     
1441 C  CA    . TYR A 183 ? 0.6779 0.6856 0.8378 -0.0103 -0.0622 -0.0160 1400 TYR A CA    
1442 C  C     . TYR A 183 ? 0.7876 0.7875 0.9477 -0.0091 -0.0651 -0.0156 1400 TYR A C     
1443 O  O     . TYR A 183 ? 0.8345 0.8353 0.9894 -0.0052 -0.0712 -0.0170 1400 TYR A O     
1444 C  CB    . TYR A 183 ? 0.7329 0.7356 0.8776 -0.0092 -0.0564 -0.0106 1400 TYR A CB    
1445 C  CG    . TYR A 183 ? 0.8565 0.8650 0.9946 -0.0093 -0.0548 -0.0118 1400 TYR A CG    
1446 C  CD1   . TYR A 183 ? 0.7988 0.8163 0.9401 -0.0083 -0.0605 -0.0162 1400 TYR A CD1   
1447 C  CD2   . TYR A 183 ? 0.8643 0.8677 0.9916 -0.0103 -0.0469 -0.0085 1400 TYR A CD2   
1448 C  CE1   . TYR A 183 ? 0.7841 0.8047 0.9194 -0.0087 -0.0585 -0.0178 1400 TYR A CE1   
1449 C  CE2   . TYR A 183 ? 0.8236 0.8301 0.9433 -0.0106 -0.0450 -0.0106 1400 TYR A CE2   
1450 C  CZ    . TYR A 183 ? 0.8789 0.8938 1.0032 -0.0099 -0.0509 -0.0154 1400 TYR A CZ    
1451 O  OH    . TYR A 183 ? 0.8704 0.8864 0.9870 -0.0105 -0.0485 -0.0180 1400 TYR A OH    
1452 N  N     . ALA A 184 ? 0.8424 0.8337 1.0090 -0.0125 -0.0598 -0.0138 1401 ALA A N     
1453 C  CA    . ALA A 184 ? 0.7706 0.7519 0.9389 -0.0123 -0.0616 -0.0141 1401 ALA A CA    
1454 C  C     . ALA A 184 ? 0.7392 0.7243 0.9143 -0.0125 -0.0697 -0.0213 1401 ALA A C     
1455 O  O     . ALA A 184 ? 0.7007 0.6799 0.8697 -0.0089 -0.0733 -0.0227 1401 ALA A O     
1456 C  CB    . ALA A 184 ? 0.7084 0.6807 0.8865 -0.0178 -0.0542 -0.0119 1401 ALA A CB    
1457 N  N     . LYS A 185 ? 0.6997 0.6945 0.8865 -0.0159 -0.0724 -0.0257 1402 LYS A N     
1458 C  CA    . LYS A 185 ? 0.7157 0.7143 0.9064 -0.0159 -0.0810 -0.0322 1402 LYS A CA    
1459 C  C     . LYS A 185 ? 0.7748 0.7781 0.9528 -0.0098 -0.0855 -0.0327 1402 LYS A C     
1460 O  O     . LYS A 185 ? 0.7613 0.7616 0.9346 -0.0075 -0.0905 -0.0364 1402 LYS A O     
1461 C  CB    . LYS A 185 ? 0.7595 0.7681 0.9665 -0.0206 -0.0834 -0.0354 1402 LYS A CB    
1462 C  CG    . LYS A 185 ? 0.8415 0.8483 1.0578 -0.0245 -0.0905 -0.0415 1402 LYS A CG    
1463 C  CD    . LYS A 185 ? 0.8504 0.8658 1.0883 -0.0306 -0.0916 -0.0432 1402 LYS A CD    
1464 C  CE    . LYS A 185 ? 0.8494 0.8636 1.0973 -0.0340 -0.0809 -0.0382 1402 LYS A CE    
1465 N  NZ    . LYS A 185 ? 0.8623 0.8862 1.1348 -0.0399 -0.0815 -0.0398 1402 LYS A NZ    
1466 N  N     . VAL A 186 ? 0.7644 0.7743 0.9365 -0.0074 -0.0834 -0.0293 1403 VAL A N     
1467 C  CA    . VAL A 186 ? 0.8580 0.8724 1.0198 -0.0022 -0.0869 -0.0291 1403 VAL A CA    
1468 C  C     . VAL A 186 ? 0.7741 0.7803 0.9275 0.0021  -0.0872 -0.0276 1403 VAL A C     
1469 O  O     . VAL A 186 ? 0.7660 0.7728 0.9154 0.0055  -0.0908 -0.0302 1403 VAL A O     
1470 C  CB    . VAL A 186 ? 0.8390 0.8594 0.9951 -0.0012 -0.0842 -0.0255 1403 VAL A CB    
1471 C  CG1   . VAL A 186 ? 0.7321 0.7565 0.8791 0.0036  -0.0876 -0.0244 1403 VAL A CG1   
1472 C  CG2   . VAL A 186 ? 0.8034 0.8316 0.9673 -0.0040 -0.0839 -0.0277 1403 VAL A CG2   
1473 N  N     . TYR A 187 ? 0.7533 0.7514 0.9040 0.0023  -0.0826 -0.0231 1404 TYR A N     
1474 C  CA    . TYR A 187 ? 0.7631 0.7533 0.9068 0.0076  -0.0824 -0.0207 1404 TYR A CA    
1475 C  C     . TYR A 187 ? 0.6709 0.6507 0.8175 0.0071  -0.0835 -0.0256 1404 TYR A C     
1476 O  O     . TYR A 187 ? 0.6330 0.6104 0.7747 0.0119  -0.0855 -0.0275 1404 TYR A O     
1477 C  CB    . TYR A 187 ? 0.7717 0.7554 0.9101 0.0088  -0.0775 -0.0133 1404 TYR A CB    
1478 C  CG    . TYR A 187 ? 0.7980 0.7905 0.9282 0.0121  -0.0788 -0.0088 1404 TYR A CG    
1479 C  CD1   . TYR A 187 ? 0.7866 0.7847 0.9146 0.0087  -0.0771 -0.0076 1404 TYR A CD1   
1480 C  CD2   . TYR A 187 ? 0.6996 0.6951 0.8251 0.0186  -0.0819 -0.0061 1404 TYR A CD2   
1481 C  CE1   . TYR A 187 ? 0.7131 0.7183 0.8325 0.0109  -0.0792 -0.0045 1404 TYR A CE1   
1482 C  CE2   . TYR A 187 ? 0.6603 0.6650 0.7799 0.0207  -0.0844 -0.0024 1404 TYR A CE2   
1483 C  CZ    . TYR A 187 ? 0.6862 0.6951 0.8019 0.0164  -0.0835 -0.0019 1404 TYR A CZ    
1484 O  OH    . TYR A 187 ? 0.6878 0.7047 0.7966 0.0176  -0.0868 0.0008  1404 TYR A OH    
1485 N  N     . THR A 188 ? 0.6611 0.6348 0.8161 0.0010  -0.0824 -0.0283 1405 THR A N     
1486 C  CA    . THR A 188 ? 0.7300 0.6916 0.8859 0.0002  -0.0838 -0.0335 1405 THR A CA    
1487 C  C     . THR A 188 ? 0.7190 0.6855 0.8753 -0.0009 -0.0907 -0.0414 1405 THR A C     
1488 O  O     . THR A 188 ? 0.7619 0.7222 0.9104 0.0030  -0.0926 -0.0452 1405 THR A O     
1489 C  CB    . THR A 188 ? 0.7194 0.6706 0.8849 -0.0064 -0.0801 -0.0336 1405 THR A CB    
1490 O  OG1   . THR A 188 ? 0.7310 0.6908 0.9092 -0.0135 -0.0822 -0.0367 1405 THR A OG1   
1491 C  CG2   . THR A 188 ? 0.5601 0.5057 0.7230 -0.0051 -0.0727 -0.0247 1405 THR A CG2   
1492 N  N     . ASP A 189 ? 0.7183 0.6957 0.8828 -0.0055 -0.0941 -0.0435 1406 ASP A N     
1493 C  CA    . ASP A 189 ? 0.7370 0.7181 0.9026 -0.0074 -0.1016 -0.0505 1406 ASP A CA    
1494 C  C     . ASP A 189 ? 0.8207 0.8093 0.9759 -0.0017 -0.1045 -0.0509 1406 ASP A C     
1495 O  O     . ASP A 189 ? 0.9179 0.9042 1.0666 -0.0008 -0.1095 -0.0563 1406 ASP A O     
1496 C  CB    . ASP A 189 ? 0.8417 0.8324 1.0224 -0.0139 -0.1043 -0.0515 1406 ASP A CB    
1497 C  CG    . ASP A 189 ? 0.9878 0.9714 1.1820 -0.0211 -0.1023 -0.0528 1406 ASP A CG    
1498 O  OD1   . ASP A 189 ? 0.9976 0.9676 1.1886 -0.0213 -0.0979 -0.0519 1406 ASP A OD1   
1499 O  OD2   . ASP A 189 ? 0.9692 0.9610 1.1786 -0.0266 -0.1051 -0.0543 1406 ASP A OD2   
1500 N  N     . LEU A 190 ? 0.7817 0.7786 0.9345 0.0018  -0.1014 -0.0453 1407 LEU A N     
1501 C  CA    . LEU A 190 ? 0.7222 0.7269 0.8674 0.0065  -0.1031 -0.0448 1407 LEU A CA    
1502 C  C     . LEU A 190 ? 0.7471 0.7479 0.8834 0.0130  -0.0998 -0.0424 1407 LEU A C     
1503 O  O     . LEU A 190 ? 0.6488 0.6493 0.7776 0.0169  -0.1008 -0.0446 1407 LEU A O     
1504 C  CB    . LEU A 190 ? 0.6244 0.6410 0.7740 0.0057  -0.1022 -0.0409 1407 LEU A CB    
1505 C  CG    . LEU A 190 ? 0.7396 0.7625 0.8998 0.0008  -0.1048 -0.0425 1407 LEU A CG    
1506 C  CD1   . LEU A 190 ? 0.7563 0.7883 0.9194 0.0007  -0.1021 -0.0388 1407 LEU A CD1   
1507 C  CD2   . LEU A 190 ? 0.6639 0.6883 0.8234 0.0004  -0.1117 -0.0472 1407 LEU A CD2   
1508 N  N     . LEU A 191 ? 0.7706 0.7684 0.9077 0.0145  -0.0955 -0.0373 1408 LEU A N     
1509 C  CA    . LEU A 191 ? 0.7059 0.7022 0.8375 0.0212  -0.0927 -0.0335 1408 LEU A CA    
1510 C  C     . LEU A 191 ? 0.8026 0.7839 0.9316 0.0239  -0.0899 -0.0346 1408 LEU A C     
1511 O  O     . LEU A 191 ? 0.8763 0.8558 1.0025 0.0305  -0.0872 -0.0311 1408 LEU A O     
1512 C  CB    . LEU A 191 ? 0.6150 0.6181 0.7478 0.0219  -0.0909 -0.0265 1408 LEU A CB    
1513 C  CG    . LEU A 191 ? 0.6252 0.6418 0.7594 0.0199  -0.0931 -0.0260 1408 LEU A CG    
1514 C  CD1   . LEU A 191 ? 0.5114 0.5337 0.6446 0.0196  -0.0922 -0.0204 1408 LEU A CD1   
1515 C  CD2   . LEU A 191 ? 0.5527 0.5760 0.6846 0.0234  -0.0948 -0.0278 1408 LEU A CD2   
1516 N  N     . ALA A 192 ? 0.8335 0.8041 0.9648 0.0190  -0.0906 -0.0393 1409 ALA A N     
1517 C  CA    . ALA A 192 ? 0.7629 0.7164 0.8917 0.0206  -0.0878 -0.0416 1409 ALA A CA    
1518 C  C     . ALA A 192 ? 0.7742 0.7224 0.9030 0.0255  -0.0826 -0.0336 1409 ALA A C     
1519 O  O     . ALA A 192 ? 0.7431 0.6806 0.8683 0.0314  -0.0794 -0.0332 1409 ALA A O     
1520 C  CB    . ALA A 192 ? 0.7170 0.6642 0.8370 0.0250  -0.0884 -0.0478 1409 ALA A CB    
1521 N  N     . ILE A 193 ? 0.8293 0.7846 0.9616 0.0235  -0.0817 -0.0271 1410 ILE A N     
1522 C  CA    . ILE A 193 ? 0.7691 0.7207 0.8999 0.0274  -0.0780 -0.0183 1410 ILE A CA    
1523 C  C     . ILE A 193 ? 0.9119 0.8542 1.0464 0.0212  -0.0746 -0.0161 1410 ILE A C     
1524 O  O     . ILE A 193 ? 0.9212 0.8700 1.0603 0.0146  -0.0753 -0.0176 1410 ILE A O     
1525 C  CB    . ILE A 193 ? 0.8299 0.7971 0.9587 0.0300  -0.0799 -0.0124 1410 ILE A CB    
1526 C  CG1   . ILE A 193 ? 0.9121 0.8890 1.0396 0.0362  -0.0822 -0.0132 1410 ILE A CG1   
1527 C  CG2   . ILE A 193 ? 0.7616 0.7255 0.8870 0.0327  -0.0775 -0.0030 1410 ILE A CG2   
1528 C  CD1   . ILE A 193 ? 0.7896 0.7832 0.9170 0.0364  -0.0852 -0.0091 1410 ILE A CD1   
1529 N  N     . PRO A 194 ? 0.9412 0.8679 1.0749 0.0232  -0.0702 -0.0123 1411 PRO A N     
1530 C  CA    . PRO A 194 ? 0.9205 0.8383 1.0575 0.0175  -0.0654 -0.0083 1411 PRO A CA    
1531 C  C     . PRO A 194 ? 0.8854 0.8089 1.0167 0.0195  -0.0633 0.0015  1411 PRO A C     
1532 O  O     . PRO A 194 ? 1.1158 1.0457 1.2405 0.0265  -0.0654 0.0066  1411 PRO A O     
1533 C  CB    . PRO A 194 ? 1.0348 0.9321 1.1715 0.0201  -0.0613 -0.0076 1411 PRO A CB    
1534 C  CG    . PRO A 194 ? 1.0677 0.9660 1.1983 0.0305  -0.0625 -0.0052 1411 PRO A CG    
1535 C  CD    . PRO A 194 ? 0.9815 0.8978 1.1113 0.0316  -0.0682 -0.0103 1411 PRO A CD    
1536 N  N     . VAL A 195 ? 0.8527 0.7739 0.9865 0.0130  -0.0590 0.0040  1412 VAL A N     
1537 C  CA    . VAL A 195 ? 0.9003 0.8254 1.0259 0.0137  -0.0562 0.0125  1412 VAL A CA    
1538 C  C     . VAL A 195 ? 0.9084 0.8203 1.0357 0.0087  -0.0478 0.0174  1412 VAL A C     
1539 O  O     . VAL A 195 ? 0.7619 0.6640 0.8997 0.0035  -0.0447 0.0136  1412 VAL A O     
1540 C  CB    . VAL A 195 ? 0.7958 0.7380 0.9212 0.0106  -0.0590 0.0093  1412 VAL A CB    
1541 C  CG1   . VAL A 195 ? 0.7066 0.6615 0.8308 0.0149  -0.0664 0.0052  1412 VAL A CG1   
1542 C  CG2   . VAL A 195 ? 0.5867 0.5310 0.7248 0.0021  -0.0569 0.0028  1412 VAL A CG2   
1543 N  N     . VAL A 196 ? 0.8909 0.8022 1.0075 0.0099  -0.0439 0.0260  1413 VAL A N     
1544 C  CA    . VAL A 196 ? 0.9379 0.8375 1.0540 0.0052  -0.0343 0.0319  1413 VAL A CA    
1545 C  C     . VAL A 196 ? 0.9373 0.8471 1.0503 0.0008  -0.0311 0.0319  1413 VAL A C     
1546 O  O     . VAL A 196 ? 0.9092 0.8276 1.0090 0.0046  -0.0345 0.0344  1413 VAL A O     
1547 C  CB    . VAL A 196 ? 0.9909 0.8767 1.0933 0.0115  -0.0308 0.0437  1413 VAL A CB    
1548 C  CG1   . VAL A 196 ? 0.9627 0.8365 1.0623 0.0066  -0.0198 0.0509  1413 VAL A CG1   
1549 C  CG2   . VAL A 196 ? 0.9096 0.7835 1.0161 0.0167  -0.0327 0.0438  1413 VAL A CG2   
1550 N  N     . LYS A 197 ? 0.9131 0.8220 1.0390 -0.0072 -0.0243 0.0290  1414 LYS A N     
1551 C  CA    . LYS A 197 ? 0.8754 0.7917 1.0001 -0.0112 -0.0185 0.0294  1414 LYS A CA    
1552 C  C     . LYS A 197 ? 0.9376 0.8413 1.0489 -0.0111 -0.0079 0.0399  1414 LYS A C     
1553 O  O     . LYS A 197 ? 0.9970 0.8860 1.1116 -0.0125 -0.0018 0.0451  1414 LYS A O     
1554 C  CB    . LYS A 197 ? 0.7874 0.7100 0.9347 -0.0193 -0.0154 0.0223  1414 LYS A CB    
1555 C  CG    . LYS A 197 ? 0.6551 0.5882 0.8168 -0.0206 -0.0254 0.0121  1414 LYS A CG    
1556 C  CD    . LYS A 197 ? 0.6845 0.6312 0.8612 -0.0256 -0.0245 0.0066  1414 LYS A CD    
1557 C  CE    . LYS A 197 ? 0.7764 0.7247 0.9777 -0.0328 -0.0255 0.0007  1414 LYS A CE    
1558 N  NZ    . LYS A 197 ? 0.5423 0.5073 0.7591 -0.0358 -0.0285 -0.0053 1414 LYS A NZ    
1559 N  N     . GLY A 198 ? 0.8406 0.7486 0.9355 -0.0095 -0.0055 0.0430  1415 GLY A N     
1560 C  CA    . GLY A 198 ? 0.8762 0.7712 0.9540 -0.0088 0.0044  0.0535  1415 GLY A CA    
1561 C  C     . GLY A 198 ? 0.9348 0.8349 0.9958 -0.0089 0.0084  0.0542  1415 GLY A C     
1562 O  O     . GLY A 198 ? 1.0275 0.9410 1.0929 -0.0102 0.0046  0.0462  1415 GLY A O     
1563 N  N     . ARG A 199 ? 0.9554 0.8432 0.9960 -0.0075 0.0169  0.0639  1416 ARG A N     
1564 C  CA    . ARG A 199 ? 0.9583 0.8470 0.9758 -0.0068 0.0209  0.0655  1416 ARG A CA    
1565 C  C     . ARG A 199 ? 0.9924 0.8770 0.9823 0.0003  0.0120  0.0725  1416 ARG A C     
1566 O  O     . ARG A 199 ? 1.0366 0.9095 1.0196 0.0041  0.0119  0.0818  1416 ARG A O     
1567 C  CB    . ARG A 199 ? 0.7773 0.6546 0.7899 -0.0109 0.0385  0.0714  1416 ARG A CB    
1568 C  CG    . ARG A 199 ? 0.9294 0.8156 0.9637 -0.0172 0.0468  0.0635  1416 ARG A CG    
1569 C  CD    . ARG A 199 ? 1.1032 0.9818 1.1254 -0.0197 0.0641  0.0679  1416 ARG A CD    
1570 N  NE    . ARG A 199 ? 1.0780 0.9649 1.1289 -0.0258 0.0740  0.0620  1416 ARG A NE    
1571 C  CZ    . ARG A 199 ? 1.0210 0.9050 1.0697 -0.0285 0.0904  0.0636  1416 ARG A CZ    
1572 N  NH1   . ARG A 199 ? 0.9510 0.8223 0.9668 -0.0259 0.0993  0.0706  1416 ARG A NH1   
1573 N  NH2   . ARG A 199 ? 1.0486 0.9427 1.1279 -0.0335 0.0980  0.0583  1416 ARG A NH2   
1574 N  N     . LYS A 200 ? 0.8715 0.7657 0.8469 0.0020  0.0042  0.0680  1417 LYS A N     
1575 C  CA    . LYS A 200 ? 0.9024 0.7936 0.8508 0.0080  -0.0045 0.0749  1417 LYS A CA    
1576 C  C     . LYS A 200 ? 1.0073 0.8814 0.9306 0.0087  0.0065  0.0860  1417 LYS A C     
1577 O  O     . LYS A 200 ? 1.1131 0.9806 1.0351 0.0041  0.0210  0.0859  1417 LYS A O     
1578 C  CB    . LYS A 200 ? 0.8432 0.7468 0.7801 0.0079  -0.0136 0.0673  1417 LYS A CB    
1579 C  CG    . LYS A 200 ? 0.8840 0.8039 0.8423 0.0082  -0.0256 0.0582  1417 LYS A CG    
1580 C  CD    . LYS A 200 ? 1.0655 0.9878 1.0262 0.0146  -0.0373 0.0636  1417 LYS A CD    
1581 C  CE    . LYS A 200 ? 1.1473 1.0862 1.1214 0.0158  -0.0499 0.0560  1417 LYS A CE    
1582 N  NZ    . LYS A 200 ? 1.2455 1.1875 1.2189 0.0230  -0.0609 0.0624  1417 LYS A NZ    
1583 N  N     . THR A 201 ? 1.1666 1.0332 1.0709 0.0150  0.0001  0.0964  1418 THR A N     
1584 C  CA    . THR A 201 ? 1.1568 1.0071 1.0314 0.0164  0.0091  0.1076  1418 THR A CA    
1585 C  C     . THR A 201 ? 1.0309 0.8836 0.8782 0.0149  0.0087  0.1034  1418 THR A C     
1586 O  O     . THR A 201 ? 0.9866 0.8535 0.8389 0.0130  0.0005  0.0925  1418 THR A O     
1587 C  CB    . THR A 201 ? 1.2927 1.1346 1.1527 0.0244  0.0010  0.1206  1418 THR A CB    
1588 O  OG1   . THR A 201 ? 1.3458 1.1998 1.1927 0.0289  -0.0164 0.1190  1418 THR A OG1   
1589 C  CG2   . THR A 201 ? 1.2404 1.0798 1.1276 0.0266  0.0002  0.1230  1418 THR A CG2   
1590 N  N     . GLU A 202 ? 1.0672 0.9045 0.8846 0.0155  0.0186  0.1121  1419 GLU A N     
1591 C  CA    . GLU A 202 ? 1.2329 1.0692 1.0202 0.0138  0.0197  0.1079  1419 GLU A CA    
1592 C  C     . GLU A 202 ? 1.2974 1.1445 1.0691 0.0172  -0.0008 0.1049  1419 GLU A C     
1593 O  O     . GLU A 202 ? 1.4075 1.2606 1.1677 0.0142  -0.0043 0.0951  1419 GLU A O     
1594 C  CB    . GLU A 202 ? 1.3257 1.1416 1.0789 0.0150  0.0330  0.1194  1419 GLU A CB    
1595 C  CG    . GLU A 202 ? 1.4050 1.2106 1.1701 0.0101  0.0561  0.1211  1419 GLU A CG    
1596 C  CD    . GLU A 202 ? 1.4050 1.2198 1.1857 0.0040  0.0648  0.1074  1419 GLU A CD    
1597 O  OE1   . GLU A 202 ? 1.3831 1.2063 1.2016 0.0003  0.0693  0.1020  1419 GLU A OE1   
1598 O  OE2   . GLU A 202 ? 1.4519 1.2649 1.2069 0.0031  0.0670  0.1021  1419 GLU A OE2   
1599 N  N     . LYS A 203 ? 1.2668 1.1164 1.0397 0.0234  -0.0143 0.1129  1420 LYS A N     
1600 C  CA    . LYS A 203 ? 1.2115 1.0739 0.9746 0.0266  -0.0346 0.1108  1420 LYS A CA    
1601 C  C     . LYS A 203 ? 1.1023 0.9843 0.8951 0.0236  -0.0431 0.0973  1420 LYS A C     
1602 O  O     . LYS A 203 ? 1.0851 0.9768 0.8695 0.0211  -0.0525 0.0887  1420 LYS A O     
1603 C  CB    . LYS A 203 ? 1.2586 1.1191 1.0185 0.0350  -0.0455 0.1242  1420 LYS A CB    
1604 C  CG    . LYS A 203 ? 1.2262 1.0996 0.9742 0.0388  -0.0666 0.1247  1420 LYS A CG    
1605 C  CD    . LYS A 203 ? 1.1630 1.0374 0.9182 0.0480  -0.0766 0.1375  1420 LYS A CD    
1606 C  CE    . LYS A 203 ? 1.1955 1.0865 0.9452 0.0519  -0.0988 0.1380  1420 LYS A CE    
1607 N  NZ    . LYS A 203 ? 1.1438 1.0303 0.8823 0.0618  -0.1079 0.1545  1420 LYS A NZ    
1608 N  N     . GLU A 204 ? 1.0562 0.9429 0.8829 0.0234  -0.0398 0.0951  1421 GLU A N     
1609 C  CA    . GLU A 204 ? 1.1520 1.0564 1.0066 0.0219  -0.0487 0.0844  1421 GLU A CA    
1610 C  C     . GLU A 204 ? 1.1065 1.0152 0.9744 0.0149  -0.0397 0.0721  1421 GLU A C     
1611 O  O     . GLU A 204 ? 1.1524 1.0751 1.0405 0.0131  -0.0465 0.0629  1421 GLU A O     
1612 C  CB    . GLU A 204 ? 1.2532 1.1599 1.1351 0.0258  -0.0506 0.0880  1421 GLU A CB    
1613 C  CG    . GLU A 204 ? 1.2977 1.2007 1.1699 0.0339  -0.0593 0.1004  1421 GLU A CG    
1614 C  CD    . GLU A 204 ? 1.2572 1.1772 1.1321 0.0374  -0.0771 0.0984  1421 GLU A CD    
1615 O  OE1   . GLU A 204 ? 1.1797 1.1132 1.0794 0.0360  -0.0814 0.0894  1421 GLU A OE1   
1616 O  OE2   . GLU A 204 ? 1.2328 1.1528 1.0856 0.0416  -0.0868 0.1060  1421 GLU A OE2   
1617 N  N     . LYS A 205 ? 1.1066 1.0036 0.9643 0.0112  -0.0242 0.0724  1422 LYS A N     
1618 C  CA    . LYS A 205 ? 1.0859 0.9868 0.9546 0.0054  -0.0153 0.0614  1422 LYS A CA    
1619 C  C     . LYS A 205 ? 1.1623 1.0712 1.0171 0.0036  -0.0245 0.0524  1422 LYS A C     
1620 O  O     . LYS A 205 ? 1.1200 1.0267 0.9477 0.0056  -0.0336 0.0554  1422 LYS A O     
1621 C  CB    . LYS A 205 ? 0.9484 0.8344 0.8055 0.0027  0.0040  0.0650  1422 LYS A CB    
1622 C  CG    . LYS A 205 ? 1.0505 0.9386 0.9132 -0.0022 0.0149  0.0550  1422 LYS A CG    
1623 C  CD    . LYS A 205 ? 1.1902 1.0627 1.0237 -0.0032 0.0300  0.0589  1422 LYS A CD    
1624 C  CE    . LYS A 205 ? 1.3905 1.2493 1.2187 -0.0016 0.0403  0.0719  1422 LYS A CE    
1625 N  NZ    . LYS A 205 ? 1.3614 1.2054 1.1686 -0.0035 0.0601  0.0751  1422 LYS A NZ    
1626 N  N     . PHE A 206 ? 1.1162 1.0339 0.9899 -0.0003 -0.0224 0.0414  1423 PHE A N     
1627 C  CA    . PHE A 206 ? 1.1581 1.0795 1.0187 -0.0031 -0.0267 0.0320  1423 PHE A CA    
1628 C  C     . PHE A 206 ? 1.0244 0.9307 0.8499 -0.0042 -0.0173 0.0335  1423 PHE A C     
1629 O  O     . PHE A 206 ? 0.8383 0.7343 0.6620 -0.0053 -0.0004 0.0357  1423 PHE A O     
1630 C  CB    . PHE A 206 ? 1.2507 1.1803 1.1372 -0.0067 -0.0217 0.0214  1423 PHE A CB    
1631 C  CG    . PHE A 206 ? 1.3240 1.2551 1.1985 -0.0097 -0.0244 0.0115  1423 PHE A CG    
1632 C  CD1   . PHE A 206 ? 1.4128 1.3454 1.2653 -0.0098 -0.0378 0.0103  1423 PHE A CD1   
1633 C  CD2   . PHE A 206 ? 1.3471 1.2784 1.2337 -0.0126 -0.0141 0.0032  1423 PHE A CD2   
1634 C  CE1   . PHE A 206 ? 1.3977 1.3303 1.2390 -0.0135 -0.0405 0.0003  1423 PHE A CE1   
1635 C  CE2   . PHE A 206 ? 1.3735 1.3042 1.2489 -0.0153 -0.0160 -0.0063 1423 PHE A CE2   
1636 C  CZ    . PHE A 206 ? 1.3613 1.2919 1.2135 -0.0162 -0.0291 -0.0081 1423 PHE A CZ    
1637 N  N     . ALA A 207 ? 0.9733 0.8785 0.7708 -0.0041 -0.0284 0.0323  1424 ALA A N     
1638 C  CA    . ALA A 207 ? 1.0239 0.9130 0.7815 -0.0043 -0.0219 0.0353  1424 ALA A CA    
1639 C  C     . ALA A 207 ? 1.1970 1.0763 0.9493 -0.0078 -0.0029 0.0283  1424 ALA A C     
1640 O  O     . ALA A 207 ? 1.2427 1.1073 0.9756 -0.0071 0.0120  0.0340  1424 ALA A O     
1641 C  CB    . ALA A 207 ? 0.9889 0.8804 0.7196 -0.0048 -0.0392 0.0324  1424 ALA A CB    
1642 N  N     . GLY A 208 ? 1.2089 1.0961 0.9796 -0.0110 -0.0022 0.0165  1425 GLY A N     
1643 C  CA    . GLY A 208 ? 1.2259 1.1047 0.9941 -0.0135 0.0156  0.0093  1425 GLY A CA    
1644 C  C     . GLY A 208 ? 1.3086 1.1878 1.1055 -0.0133 0.0328  0.0123  1425 GLY A C     
1645 O  O     . GLY A 208 ? 1.3433 1.2150 1.1381 -0.0146 0.0498  0.0082  1425 GLY A O     
1646 N  N     . GLY A 209 ? 1.3211 1.2084 1.1450 -0.0118 0.0294  0.0192  1426 GLY A N     
1647 C  CA    . GLY A 209 ? 1.1935 1.0836 1.0488 -0.0127 0.0432  0.0207  1426 GLY A CA    
1648 C  C     . GLY A 209 ? 1.0932 0.9698 0.9380 -0.0123 0.0599  0.0303  1426 GLY A C     
1649 O  O     . GLY A 209 ? 1.0574 0.9220 0.8708 -0.0105 0.0599  0.0381  1426 GLY A O     
1650 N  N     . ASP A 210 ? 1.1328 1.0113 1.0046 -0.0142 0.0749  0.0301  1427 ASP A N     
1651 C  CA    . ASP A 210 ? 1.1447 1.0133 1.0173 -0.0146 0.0899  0.0404  1427 ASP A CA    
1652 C  C     . ASP A 210 ? 1.1740 1.0453 1.0606 -0.0136 0.0798  0.0485  1427 ASP A C     
1653 O  O     . ASP A 210 ? 1.3878 1.2474 1.2536 -0.0116 0.0808  0.0588  1427 ASP A O     
1654 C  CB    . ASP A 210 ? 1.2527 1.1251 1.1550 -0.0175 0.1079  0.0378  1427 ASP A CB    
1655 C  CG    . ASP A 210 ? 1.4376 1.2962 1.3305 -0.0184 0.1284  0.0471  1427 ASP A CG    
1656 O  OD1   . ASP A 210 ? 1.5419 1.3861 1.3968 -0.0168 0.1368  0.0491  1427 ASP A OD1   
1657 O  OD2   . ASP A 210 ? 1.4681 1.3296 1.3903 -0.0209 0.1360  0.0523  1427 ASP A OD2   
1658 N  N     . TYR A 211 ? 1.0109 0.8965 0.9317 -0.0146 0.0702  0.0440  1428 TYR A N     
1659 C  CA    . TYR A 211 ? 0.9952 0.8828 0.9285 -0.0132 0.0597  0.0498  1428 TYR A CA    
1660 C  C     . TYR A 211 ? 0.9444 0.8481 0.8999 -0.0129 0.0435  0.0416  1428 TYR A C     
1661 O  O     . TYR A 211 ? 0.9288 0.8422 0.8979 -0.0146 0.0432  0.0325  1428 TYR A O     
1662 C  CB    . TYR A 211 ? 1.1421 1.0251 1.0983 -0.0161 0.0724  0.0561  1428 TYR A CB    
1663 C  CG    . TYR A 211 ? 1.0491 0.9438 1.0439 -0.0206 0.0785  0.0491  1428 TYR A CG    
1664 C  CD1   . TYR A 211 ? 1.0001 0.9073 1.0237 -0.0215 0.0663  0.0440  1428 TYR A CD1   
1665 C  CD2   . TYR A 211 ? 0.9359 0.8290 0.9384 -0.0235 0.0966  0.0484  1428 TYR A CD2   
1666 C  CE1   . TYR A 211 ? 0.9734 0.8916 1.0309 -0.0253 0.0700  0.0383  1428 TYR A CE1   
1667 C  CE2   . TYR A 211 ? 1.0263 0.9317 1.0662 -0.0271 0.1008  0.0429  1428 TYR A CE2   
1668 C  CZ    . TYR A 211 ? 1.0149 0.9332 1.0820 -0.0281 0.0865  0.0378  1428 TYR A CZ    
1669 O  OH    . TYR A 211 ? 1.0155 0.9468 1.1193 -0.0316 0.0886  0.0326  1428 TYR A OH    
1670 N  N     . THR A 212 ? 1.0055 0.9113 0.9662 -0.0104 0.0313  0.0454  1429 THR A N     
1671 C  CA    . THR A 212 ? 0.8880 0.8077 0.8642 -0.0092 0.0157  0.0386  1429 THR A CA    
1672 C  C     . THR A 212 ? 0.9482 0.8697 0.9484 -0.0090 0.0119  0.0411  1429 THR A C     
1673 O  O     . THR A 212 ? 1.1177 1.0300 1.1104 -0.0065 0.0112  0.0496  1429 THR A O     
1674 C  CB    . THR A 212 ? 0.8376 0.7590 0.7898 -0.0054 0.0019  0.0393  1429 THR A CB    
1675 O  OG1   . THR A 212 ? 0.9948 0.9156 0.9275 -0.0068 0.0040  0.0338  1429 THR A OG1   
1676 C  CG2   . THR A 212 ? 0.7686 0.7034 0.7383 -0.0037 -0.0130 0.0346  1429 THR A CG2   
1677 N  N     . THR A 213 ? 0.9900 0.9219 1.0183 -0.0117 0.0102  0.0339  1430 THR A N     
1678 C  CA    . THR A 213 ? 0.9925 0.9263 1.0425 -0.0119 0.0050  0.0341  1430 THR A CA    
1679 C  C     . THR A 213 ? 0.9622 0.9053 1.0132 -0.0082 -0.0104 0.0301  1430 THR A C     
1680 O  O     . THR A 213 ? 0.9645 0.9150 1.0060 -0.0069 -0.0166 0.0259  1430 THR A O     
1681 C  CB    . THR A 213 ? 0.9896 0.9295 1.0696 -0.0171 0.0105  0.0286  1430 THR A CB    
1682 O  OG1   . THR A 213 ? 0.9877 0.9409 1.0773 -0.0176 0.0054  0.0198  1430 THR A OG1   
1683 C  CG2   . THR A 213 ? 0.9766 0.9090 1.0597 -0.0211 0.0272  0.0327  1430 THR A CG2   
1684 N  N     . THR A 214 ? 0.8599 0.8015 0.9224 -0.0066 -0.0157 0.0314  1431 THR A N     
1685 C  CA    . THR A 214 ? 0.7773 0.7268 0.8403 -0.0023 -0.0288 0.0287  1431 THR A CA    
1686 C  C     . THR A 214 ? 0.7517 0.6999 0.8328 -0.0019 -0.0322 0.0270  1431 THR A C     
1687 O  O     . THR A 214 ? 0.6685 0.6068 0.7581 -0.0044 -0.0255 0.0298  1431 THR A O     
1688 C  CB    . THR A 214 ? 0.8645 0.8102 0.9053 0.0032  -0.0342 0.0360  1431 THR A CB    
1689 O  OG1   . THR A 214 ? 0.8713 0.8251 0.9171 0.0076  -0.0457 0.0341  1431 THR A OG1   
1690 C  CG2   . THR A 214 ? 0.9695 0.8997 1.0028 0.0048  -0.0275 0.0459  1431 THR A CG2   
1691 N  N     . VAL A 215 ? 0.6906 0.6482 0.7772 0.0008  -0.0422 0.0221  1432 VAL A N     
1692 C  CA    . VAL A 215 ? 0.7530 0.7081 0.8497 0.0034  -0.0469 0.0209  1432 VAL A CA    
1693 C  C     . VAL A 215 ? 0.8277 0.7834 0.9124 0.0107  -0.0538 0.0260  1432 VAL A C     
1694 O  O     . VAL A 215 ? 0.8260 0.7918 0.9028 0.0126  -0.0596 0.0253  1432 VAL A O     
1695 C  CB    . VAL A 215 ? 0.6483 0.6133 0.7609 0.0012  -0.0520 0.0115  1432 VAL A CB    
1696 C  CG1   . VAL A 215 ? 0.6569 0.6222 0.7840 -0.0056 -0.0462 0.0074  1432 VAL A CG1   
1697 C  CG2   . VAL A 215 ? 0.7202 0.6986 0.8289 0.0027  -0.0583 0.0077  1432 VAL A CG2   
1698 N  N     . GLU A 216 ? 0.8986 0.8430 0.9824 0.0146  -0.0528 0.0317  1433 GLU A N     
1699 C  CA    . GLU A 216 ? 0.8258 0.7708 0.9012 0.0226  -0.0589 0.0378  1433 GLU A CA    
1700 C  C     . GLU A 216 ? 0.7836 0.7262 0.8705 0.0266  -0.0618 0.0349  1433 GLU A C     
1701 O  O     . GLU A 216 ? 0.7409 0.6733 0.8372 0.0237  -0.0572 0.0319  1433 GLU A O     
1702 C  CB    . GLU A 216 ? 0.8163 0.7487 0.8774 0.0258  -0.0550 0.0490  1433 GLU A CB    
1703 C  CG    . GLU A 216 ? 0.9846 0.9136 1.0330 0.0210  -0.0483 0.0519  1433 GLU A CG    
1704 C  CD    . GLU A 216 ? 1.1775 1.1141 1.2072 0.0235  -0.0543 0.0554  1433 GLU A CD    
1705 O  OE1   . GLU A 216 ? 1.2902 1.2293 1.3111 0.0188  -0.0509 0.0527  1433 GLU A OE1   
1706 O  OE2   . GLU A 216 ? 1.2152 1.1553 1.2393 0.0302  -0.0625 0.0605  1433 GLU A OE2   
1707 N  N     . ALA A 217 ? 0.8001 0.7523 0.8869 0.0327  -0.0691 0.0352  1434 ALA A N     
1708 C  CA    . ALA A 217 ? 0.8354 0.7850 0.9314 0.0379  -0.0707 0.0329  1434 ALA A CA    
1709 C  C     . ALA A 217 ? 0.8762 0.8257 0.9678 0.0474  -0.0741 0.0418  1434 ALA A C     
1710 O  O     . ALA A 217 ? 0.9406 0.8955 1.0222 0.0494  -0.0776 0.0487  1434 ALA A O     
1711 C  CB    . ALA A 217 ? 0.7545 0.7171 0.8589 0.0367  -0.0751 0.0236  1434 ALA A CB    
1712 N  N     . TYR A 218 ? 0.9224 0.8650 1.0211 0.0533  -0.0731 0.0416  1435 TYR A N     
1713 C  CA    . TYR A 218 ? 1.0398 0.9819 1.1379 0.0636  -0.0756 0.0503  1435 TYR A CA    
1714 C  C     . TYR A 218 ? 0.9588 0.9114 1.0673 0.0690  -0.0787 0.0456  1435 TYR A C     
1715 O  O     . TYR A 218 ? 0.9340 0.8813 1.0487 0.0675  -0.0753 0.0371  1435 TYR A O     
1716 C  CB    . TYR A 218 ? 1.2205 1.1407 1.3174 0.0675  -0.0691 0.0566  1435 TYR A CB    
1717 C  CG    . TYR A 218 ? 1.3738 1.2922 1.4699 0.0792  -0.0714 0.0676  1435 TYR A CG    
1718 C  CD1   . TYR A 218 ? 1.4064 1.3130 1.5104 0.0869  -0.0675 0.0683  1435 TYR A CD1   
1719 C  CD2   . TYR A 218 ? 1.4590 1.3873 1.5464 0.0827  -0.0777 0.0774  1435 TYR A CD2   
1720 C  CE1   . TYR A 218 ? 1.4926 1.3981 1.5981 0.0985  -0.0694 0.0791  1435 TYR A CE1   
1721 C  CE2   . TYR A 218 ? 1.5602 1.4885 1.6485 0.0939  -0.0810 0.0883  1435 TYR A CE2   
1722 C  CZ    . TYR A 218 ? 1.5329 1.4501 1.6314 0.1021  -0.0766 0.0895  1435 TYR A CZ    
1723 O  OH    . TYR A 218 ? 1.5053 1.4227 1.6068 0.1140  -0.0795 0.1008  1435 TYR A OH    
1724 N  N     . ILE A 219 ? 0.8099 0.7776 0.9202 0.0751  -0.0849 0.0509  1436 ILE A N     
1725 C  CA    . ILE A 219 ? 0.8667 0.8435 0.9884 0.0822  -0.0863 0.0490  1436 ILE A CA    
1726 C  C     . ILE A 219 ? 0.8369 0.8048 0.9616 0.0931  -0.0847 0.0586  1436 ILE A C     
1727 O  O     . ILE A 219 ? 0.8960 0.8689 1.0173 0.0977  -0.0897 0.0689  1436 ILE A O     
1728 C  CB    . ILE A 219 ? 0.7573 0.7576 0.8832 0.0815  -0.0938 0.0487  1436 ILE A CB    
1729 N  N     . SER A 220 ? 0.7109 0.6640 0.8407 0.0975  -0.0778 0.0553  1437 SER A N     
1730 C  CA    . SER A 220 ? 0.9552 0.8962 1.0883 0.1084  -0.0746 0.0640  1437 SER A CA    
1731 C  C     . SER A 220 ? 1.1789 1.1355 1.3246 0.1193  -0.0776 0.0686  1437 SER A C     
1732 O  O     . SER A 220 ? 1.3141 1.2694 1.4633 0.1290  -0.0790 0.0797  1437 SER A O     
1733 C  CB    . SER A 220 ? 0.9158 0.8322 1.0489 0.1085  -0.0654 0.0580  1437 SER A CB    
1734 O  OG    . SER A 220 ? 0.7876 0.7059 0.9263 0.1086  -0.0624 0.0471  1437 SER A OG    
1735 N  N     . ALA A 221 ? 1.2196 1.1904 1.3733 0.1184  -0.0778 0.0607  1438 ALA A N     
1736 C  CA    . ALA A 221 ? 1.1592 1.1464 1.3278 0.1284  -0.0793 0.0648  1438 ALA A CA    
1737 C  C     . ALA A 221 ? 1.1529 1.1575 1.3252 0.1321  -0.0892 0.0767  1438 ALA A C     
1738 O  O     . ALA A 221 ? 1.2936 1.3031 1.4770 0.1434  -0.0904 0.0858  1438 ALA A O     
1739 C  CB    . ALA A 221 ? 1.0985 1.1002 1.2732 0.1244  -0.0785 0.0552  1438 ALA A CB    
1740 N  N     . SER A 222 ? 1.0133 1.0276 1.1764 0.1226  -0.0967 0.0763  1439 SER A N     
1741 C  CA    . SER A 222 ? 1.0657 1.0936 1.2262 0.1236  -0.1073 0.0863  1439 SER A CA    
1742 C  C     . SER A 222 ? 1.1639 1.1747 1.3112 0.1265  -0.1075 0.0960  1439 SER A C     
1743 O  O     . SER A 222 ? 1.1628 1.1815 1.3088 0.1319  -0.1157 0.1071  1439 SER A O     
1744 C  CB    . SER A 222 ? 1.1027 1.1435 1.2551 0.1119  -0.1140 0.0809  1439 SER A CB    
1745 O  OG    . SER A 222 ? 1.1680 1.2119 1.3085 0.1107  -0.1226 0.0892  1439 SER A OG    
1746 N  N     . GLY A 223 ? 1.3163 1.3040 1.4530 0.1224  -0.0991 0.0924  1440 GLY A N     
1747 C  CA    . GLY A 223 ? 1.3548 1.3252 1.4768 0.1226  -0.0980 0.1011  1440 GLY A CA    
1748 C  C     . GLY A 223 ? 1.3377 1.3107 1.4423 0.1129  -0.1026 0.1017  1440 GLY A C     
1749 O  O     . GLY A 223 ? 1.3888 1.3524 1.4803 0.1149  -0.1038 0.1118  1440 GLY A O     
1750 N  N     . ARG A 224 ? 1.2742 1.2585 1.3773 0.1030  -0.1044 0.0916  1441 ARG A N     
1751 C  CA    . ARG A 224 ? 1.1900 1.1769 1.2764 0.0946  -0.1083 0.0918  1441 ARG A CA    
1752 C  C     . ARG A 224 ? 1.1400 1.1194 1.2226 0.0836  -0.1011 0.0807  1441 ARG A C     
1753 O  O     . ARG A 224 ? 1.0425 1.0234 1.1364 0.0813  -0.0974 0.0712  1441 ARG A O     
1754 C  CB    . ARG A 224 ? 1.1763 1.1871 1.2636 0.0936  -0.1202 0.0923  1441 ARG A CB    
1755 C  CG    . ARG A 224 ? 1.2707 1.2892 1.3594 0.1036  -0.1292 0.1052  1441 ARG A CG    
1756 C  CD    . ARG A 224 ? 1.3834 1.4237 1.4700 0.1010  -0.1423 0.1061  1441 ARG A CD    
1757 N  NE    . ARG A 224 ? 1.3926 1.4322 1.4638 0.1052  -0.1511 0.1183  1441 ARG A NE    
1758 C  CZ    . ARG A 224 ? 1.3264 1.3703 1.4050 0.1166  -0.1571 0.1302  1441 ARG A CZ    
1759 N  NH1   . ARG A 224 ? 1.2651 1.3139 1.3673 0.1252  -0.1541 0.1314  1441 ARG A NH1   
1760 N  NH2   . ARG A 224 ? 1.3633 1.4062 1.4249 0.1197  -0.1660 0.1412  1441 ARG A NH2   
1761 N  N     . ALA A 225 ? 1.0867 1.0580 1.1532 0.0772  -0.0990 0.0823  1442 ALA A N     
1762 C  CA    . ALA A 225 ? 0.9308 0.8958 0.9949 0.0671  -0.0921 0.0732  1442 ALA A CA    
1763 C  C     . ALA A 225 ? 0.8271 0.8067 0.8853 0.0599  -0.0969 0.0673  1442 ALA A C     
1764 O  O     . ALA A 225 ? 0.7764 0.7647 0.8244 0.0609  -0.1044 0.0720  1442 ALA A O     
1765 C  CB    . ALA A 225 ? 0.8730 0.8179 0.9256 0.0646  -0.0837 0.0786  1442 ALA A CB    
1766 N  N     . ILE A 226 ? 0.9585 0.9387 1.0217 0.0522  -0.0925 0.0571  1443 ILE A N     
1767 C  CA    . ILE A 226 ? 1.0004 0.9935 1.0603 0.0458  -0.0962 0.0506  1443 ILE A CA    
1768 C  C     . ILE A 226 ? 0.9904 0.9766 1.0491 0.0374  -0.0884 0.0438  1443 ILE A C     
1769 O  O     . ILE A 226 ? 0.9208 0.8993 0.9893 0.0356  -0.0824 0.0398  1443 ILE A O     
1770 C  CB    . ILE A 226 ? 0.8716 0.8808 0.9457 0.0470  -0.1020 0.0447  1443 ILE A CB    
1771 C  CG1   . ILE A 226 ? 1.0215 1.0423 1.0925 0.0402  -0.1056 0.0382  1443 ILE A CG1   
1772 C  CG2   . ILE A 226 ? 0.6064 0.6112 0.6942 0.0473  -0.0967 0.0384  1443 ILE A CG2   
1773 C  CD1   . ILE A 226 ? 1.1486 1.1868 1.2303 0.0419  -0.1131 0.0360  1443 ILE A CD1   
1774 N  N     . GLN A 227 ? 1.0094 0.9991 1.0564 0.0324  -0.0890 0.0422  1444 GLN A N     
1775 C  CA    . GLN A 227 ? 0.8741 0.8598 0.9206 0.0251  -0.0816 0.0361  1444 GLN A CA    
1776 C  C     . GLN A 227 ? 0.8117 0.8075 0.8732 0.0220  -0.0832 0.0265  1444 GLN A C     
1777 O  O     . GLN A 227 ? 1.1212 1.1292 1.1838 0.0220  -0.0899 0.0235  1444 GLN A O     
1778 C  CB    . GLN A 227 ? 0.8723 0.8582 0.9000 0.0219  -0.0819 0.0373  1444 GLN A CB    
1779 C  CG    . GLN A 227 ? 0.8780 0.8580 0.9020 0.0155  -0.0726 0.0330  1444 GLN A CG    
1780 C  CD    . GLN A 227 ? 0.9351 0.9172 0.9402 0.0129  -0.0744 0.0318  1444 GLN A CD    
1781 O  OE1   . GLN A 227 ? 0.9909 0.9817 0.9989 0.0096  -0.0773 0.0243  1444 GLN A OE1   
1782 N  NE2   . GLN A 227 ? 0.9826 0.9552 0.9667 0.0143  -0.0725 0.0392  1444 GLN A NE2   
1783 N  N     . GLY A 228 ? 0.7121 0.7031 0.7853 0.0192  -0.0776 0.0219  1445 GLY A N     
1784 C  CA    . GLY A 228 ? 0.6947 0.6945 0.7809 0.0172  -0.0798 0.0138  1445 GLY A CA    
1785 C  C     . GLY A 228 ? 0.8144 0.8188 0.9016 0.0113  -0.0774 0.0079  1445 GLY A C     
1786 O  O     . GLY A 228 ? 0.8768 0.8908 0.9699 0.0103  -0.0812 0.0026  1445 GLY A O     
1787 N  N     . ALA A 229 ? 0.7000 0.6970 0.7819 0.0077  -0.0702 0.0092  1446 ALA A N     
1788 C  CA    . ALA A 229 ? 0.7339 0.7334 0.8162 0.0028  -0.0658 0.0045  1446 ALA A CA    
1789 C  C     . ALA A 229 ? 0.7659 0.7552 0.8374 0.0008  -0.0571 0.0090  1446 ALA A C     
1790 O  O     . ALA A 229 ? 0.8572 0.8371 0.9251 0.0024  -0.0540 0.0151  1446 ALA A O     
1791 C  CB    . ALA A 229 ? 0.5740 0.5770 0.6745 -0.0001 -0.0641 -0.0016 1446 ALA A CB    
1792 N  N     . THR A 230 ? 0.6768 0.6667 0.7423 -0.0024 -0.0522 0.0061  1447 THR A N     
1793 C  CA    . THR A 230 ? 0.7260 0.7058 0.7813 -0.0045 -0.0416 0.0098  1447 THR A CA    
1794 C  C     . THR A 230 ? 0.8674 0.8494 0.9308 -0.0085 -0.0337 0.0042  1447 THR A C     
1795 O  O     . THR A 230 ? 0.7958 0.7863 0.8667 -0.0092 -0.0373 -0.0021 1447 THR A O     
1796 C  CB    . THR A 230 ? 0.7982 0.7719 0.8266 -0.0029 -0.0422 0.0148  1447 THR A CB    
1797 O  OG1   . THR A 230 ? 0.9247 0.9037 0.9433 -0.0043 -0.0456 0.0093  1447 THR A OG1   
1798 C  CG2   . THR A 230 ? 0.8159 0.7888 0.8371 0.0019  -0.0507 0.0212  1447 THR A CG2   
1799 N  N     . SER A 231 ? 0.8780 0.8518 0.9403 -0.0106 -0.0219 0.0073  1448 SER A N     
1800 C  CA    . SER A 231 ? 0.7529 0.7285 0.8262 -0.0138 -0.0121 0.0033  1448 SER A CA    
1801 C  C     . SER A 231 ? 0.8417 0.8058 0.8976 -0.0147 0.0006  0.0081  1448 SER A C     
1802 O  O     . SER A 231 ? 0.9431 0.8993 0.9998 -0.0154 0.0071  0.0145  1448 SER A O     
1803 C  CB    . SER A 231 ? 0.6092 0.5897 0.7109 -0.0161 -0.0106 0.0017  1448 SER A CB    
1804 O  OG    . SER A 231 ? 0.7303 0.7111 0.8445 -0.0191 0.0014  0.0007  1448 SER A OG    
1805 N  N     . HIS A 232 ? 0.7704 0.7320 0.8089 -0.0148 0.0044  0.0051  1449 HIS A N     
1806 C  CA    . HIS A 232 ? 0.7684 0.7175 0.7831 -0.0150 0.0157  0.0094  1449 HIS A CA    
1807 C  C     . HIS A 232 ? 0.8752 0.8226 0.9008 -0.0174 0.0318  0.0072  1449 HIS A C     
1808 O  O     . HIS A 232 ? 0.9799 0.9362 1.0250 -0.0182 0.0326  0.0007  1449 HIS A O     
1809 C  CB    . HIS A 232 ? 0.8013 0.7465 0.7857 -0.0138 0.0103  0.0072  1449 HIS A CB    
1810 C  CG    . HIS A 232 ? 0.9639 0.9158 0.9440 -0.0117 -0.0069 0.0070  1449 HIS A CG    
1811 N  ND1   . HIS A 232 ? 1.0175 0.9656 0.9839 -0.0090 -0.0139 0.0146  1449 HIS A ND1   
1812 C  CD2   . HIS A 232 ? 0.9699 0.9325 0.9594 -0.0117 -0.0178 0.0007  1449 HIS A CD2   
1813 C  CE1   . HIS A 232 ? 0.9914 0.9488 0.9603 -0.0073 -0.0283 0.0127  1449 HIS A CE1   
1814 N  NE2   . HIS A 232 ? 0.9577 0.9237 0.9401 -0.0092 -0.0306 0.0042  1449 HIS A NE2   
1815 N  N     . HIS A 233 ? 0.8599 0.7960 0.8728 -0.0180 0.0452  0.0133  1450 HIS A N     
1816 C  CA    . HIS A 233 ? 0.9398 0.8722 0.9563 -0.0196 0.0629  0.0119  1450 HIS A CA    
1817 C  C     . HIS A 233 ? 1.0196 0.9390 0.9975 -0.0183 0.0688  0.0118  1450 HIS A C     
1818 O  O     . HIS A 233 ? 1.0384 0.9457 0.9919 -0.0176 0.0732  0.0194  1450 HIS A O     
1819 C  CB    . HIS A 233 ? 0.9215 0.8506 0.9553 -0.0220 0.0762  0.0188  1450 HIS A CB    
1820 C  CG    . HIS A 233 ? 1.1027 1.0273 1.1382 -0.0232 0.0963  0.0186  1450 HIS A CG    
1821 N  ND1   . HIS A 233 ? 1.1149 1.0481 1.1686 -0.0231 0.1015  0.0112  1450 HIS A ND1   
1822 C  CD2   . HIS A 233 ? 1.1463 1.0582 1.1669 -0.0239 0.1135  0.0253  1450 HIS A CD2   
1823 C  CE1   . HIS A 233 ? 1.1524 1.0791 1.2041 -0.0236 0.1214  0.0130  1450 HIS A CE1   
1824 N  NE2   . HIS A 233 ? 1.1516 1.0653 1.1828 -0.0243 0.1293  0.0214  1450 HIS A NE2   
1825 N  N     . LEU A 234 ? 0.9553 0.8761 0.9264 -0.0179 0.0689  0.0033  1451 LEU A N     
1826 C  CA    . LEU A 234 ? 0.9651 0.8726 0.8981 -0.0172 0.0740  0.0015  1451 LEU A CA    
1827 C  C     . LEU A 234 ? 1.0968 0.9932 1.0222 -0.0176 0.0964  0.0041  1451 LEU A C     
1828 O  O     . LEU A 234 ? 1.1522 1.0340 1.0409 -0.0169 0.1029  0.0050  1451 LEU A O     
1829 C  CB    . LEU A 234 ? 0.9283 0.8387 0.8560 -0.0173 0.0675  -0.0093 1451 LEU A CB    
1830 C  CG    . LEU A 234 ? 0.9944 0.9149 0.9262 -0.0172 0.0463  -0.0121 1451 LEU A CG    
1831 C  CD1   . LEU A 234 ? 0.9859 0.9046 0.9020 -0.0162 0.0351  -0.0039 1451 LEU A CD1   
1832 C  CD2   . LEU A 234 ? 0.9134 0.8489 0.8842 -0.0172 0.0413  -0.0143 1451 LEU A CD2   
1833 N  N     . GLY A 235 ? 1.1633 1.0664 1.1224 -0.0186 0.1081  0.0055  1452 GLY A N     
1834 C  CA    . GLY A 235 ? 1.1548 1.0486 1.1100 -0.0189 0.1311  0.0086  1452 GLY A CA    
1835 C  C     . GLY A 235 ? 1.2045 1.0915 1.1429 -0.0174 0.1406  -0.0001 1452 GLY A C     
1836 O  O     . GLY A 235 ? 1.2504 1.1465 1.2074 -0.0167 0.1365  -0.0083 1452 GLY A O     
1837 N  N     . GLN A 236 ? 1.1990 1.0688 1.1011 -0.0166 0.1541  0.0018  1453 GLN A N     
1838 C  CA    . GLN A 236 ? 1.1269 0.9866 1.0085 -0.0152 0.1654  -0.0069 1453 GLN A CA    
1839 C  C     . GLN A 236 ? 1.2308 1.0774 1.0649 -0.0150 0.1546  -0.0115 1453 GLN A C     
1840 O  O     . GLN A 236 ? 1.2086 1.0422 1.0168 -0.0142 0.1651  -0.0186 1453 GLN A O     
1841 C  CB    . GLN A 236 ? 1.0955 0.9446 0.9726 -0.0144 0.1928  -0.0030 1453 GLN A CB    
1842 C  CG    . GLN A 236 ? 1.1480 1.0095 1.0705 -0.0136 0.2067  -0.0057 1453 GLN A CG    
1843 C  CD    . GLN A 236 ? 1.1900 1.0428 1.1126 -0.0127 0.2353  -0.0014 1453 GLN A CD    
1844 O  OE1   . GLN A 236 ? 1.2172 1.0517 1.1003 -0.0124 0.2470  0.0025  1453 GLN A OE1   
1845 N  NE2   . GLN A 236 ? 1.1887 1.0552 1.1565 -0.0122 0.2469  -0.0017 1453 GLN A NE2   
1846 N  N     . ASN A 237 ? 1.2906 1.1402 1.1127 -0.0158 0.1340  -0.0080 1454 ASN A N     
1847 C  CA    . ASN A 237 ? 1.3769 1.2151 1.1541 -0.0161 0.1228  -0.0115 1454 ASN A CA    
1848 C  C     . ASN A 237 ? 1.3170 1.1566 1.0918 -0.0171 0.1153  -0.0248 1454 ASN A C     
1849 O  O     . ASN A 237 ? 1.4879 1.3125 1.2283 -0.0176 0.1207  -0.0319 1454 ASN A O     
1850 C  CB    . ASN A 237 ? 1.4469 1.2908 1.2182 -0.0162 0.1020  -0.0041 1454 ASN A CB    
1851 C  CG    . ASN A 237 ? 1.4440 1.2846 1.2171 -0.0151 0.1090  0.0093  1454 ASN A CG    
1852 O  OD1   . ASN A 237 ? 1.5281 1.3545 1.2810 -0.0145 0.1269  0.0142  1454 ASN A OD1   
1853 N  ND2   . ASN A 237 ? 1.3519 1.2043 1.1491 -0.0148 0.0960  0.0153  1454 ASN A ND2   
1854 N  N     . PHE A 238 ? 1.2002 1.0565 1.0106 -0.0176 0.1036  -0.0285 1455 PHE A N     
1855 C  CA    . PHE A 238 ? 1.2159 1.0732 1.0251 -0.0188 0.0956  -0.0403 1455 PHE A CA    
1856 C  C     . PHE A 238 ? 1.2285 1.0794 1.0461 -0.0175 0.1147  -0.0480 1455 PHE A C     
1857 O  O     . PHE A 238 ? 1.2878 1.1287 1.0862 -0.0184 0.1151  -0.0581 1455 PHE A O     
1858 C  CB    . PHE A 238 ? 1.1603 1.0363 1.0031 -0.0194 0.0778  -0.0409 1455 PHE A CB    
1859 C  CG    . PHE A 238 ? 1.1884 1.0698 1.0198 -0.0206 0.0574  -0.0365 1455 PHE A CG    
1860 C  CD1   . PHE A 238 ? 1.3109 1.1997 1.1546 -0.0193 0.0528  -0.0260 1455 PHE A CD1   
1861 C  CD2   . PHE A 238 ? 1.1841 1.0631 0.9937 -0.0230 0.0430  -0.0429 1455 PHE A CD2   
1862 C  CE1   . PHE A 238 ? 1.3734 1.2672 1.2081 -0.0193 0.0347  -0.0215 1455 PHE A CE1   
1863 C  CE2   . PHE A 238 ? 1.3509 1.2368 1.1528 -0.0236 0.0242  -0.0383 1455 PHE A CE2   
1864 C  CZ    . PHE A 238 ? 1.3970 1.2904 1.2116 -0.0212 0.0202  -0.0274 1455 PHE A CZ    
1865 N  N     . SER A 239 ? 1.1573 1.0138 1.0050 -0.0154 0.1305  -0.0436 1456 SER A N     
1866 C  CA    . SER A 239 ? 1.1365 0.9866 0.9918 -0.0131 0.1507  -0.0498 1456 SER A CA    
1867 C  C     . SER A 239 ? 1.1859 1.0130 0.9941 -0.0130 0.1641  -0.0542 1456 SER A C     
1868 O  O     . SER A 239 ? 1.1799 0.9962 0.9744 -0.0125 0.1694  -0.0649 1456 SER A O     
1869 C  CB    . SER A 239 ? 1.0674 0.9278 0.9610 -0.0111 0.1660  -0.0427 1456 SER A CB    
1870 O  OG    . SER A 239 ? 1.1158 0.9726 0.9979 -0.0122 0.1706  -0.0324 1456 SER A OG    
1871 N  N     . ARG A 240 ? 1.2282 1.0460 1.0094 -0.0134 0.1698  -0.0460 1457 ARG A N     
1872 C  CA    . ARG A 240 ? 1.3029 1.0974 1.0347 -0.0131 0.1825  -0.0495 1457 ARG A CA    
1873 C  C     . ARG A 240 ? 1.3154 1.1005 1.0100 -0.0159 0.1650  -0.0588 1457 ARG A C     
1874 O  O     . ARG A 240 ? 1.4104 1.1763 1.0692 -0.0161 0.1743  -0.0675 1457 ARG A O     
1875 C  CB    . ARG A 240 ? 1.3641 1.1508 1.0739 -0.0128 0.1906  -0.0374 1457 ARG A CB    
1876 C  CG    . ARG A 240 ? 1.4088 1.2036 1.1552 -0.0111 0.2094  -0.0284 1457 ARG A CG    
1877 C  CD    . ARG A 240 ? 1.4779 1.2623 1.2015 -0.0111 0.2200  -0.0161 1457 ARG A CD    
1878 N  NE    . ARG A 240 ? 1.5524 1.3437 1.3122 -0.0103 0.2403  -0.0084 1457 ARG A NE    
1879 C  CZ    . ARG A 240 ? 1.5859 1.3690 1.3466 -0.0083 0.2672  -0.0096 1457 ARG A CZ    
1880 N  NH1   . ARG A 240 ? 1.6188 1.3843 1.3433 -0.0065 0.2776  -0.0190 1457 ARG A NH1   
1881 N  NH2   . ARG A 240 ? 1.5002 1.2923 1.2985 -0.0083 0.2839  -0.0019 1457 ARG A NH2   
1882 N  N     . MET A 241 ? 1.2678 1.0653 0.9691 -0.0184 0.1400  -0.0571 1458 MET A N     
1883 C  CA    . MET A 241 ? 1.3800 1.1715 1.0519 -0.0218 0.1221  -0.0661 1458 MET A CA    
1884 C  C     . MET A 241 ? 1.4083 1.1970 1.0908 -0.0227 0.1244  -0.0798 1458 MET A C     
1885 O  O     . MET A 241 ? 1.4614 1.2327 1.1091 -0.0248 0.1261  -0.0903 1458 MET A O     
1886 C  CB    . MET A 241 ? 1.4625 1.2706 1.1466 -0.0237 0.0964  -0.0606 1458 MET A CB    
1887 C  CG    . MET A 241 ? 1.6268 1.4319 1.2860 -0.0231 0.0906  -0.0491 1458 MET A CG    
1888 S  SD    . MET A 241 ? 1.7029 1.5182 1.3514 -0.0259 0.0590  -0.0478 1458 MET A SD    
1889 C  CE    . MET A 241 ? 1.6178 1.4564 1.3214 -0.0264 0.0480  -0.0506 1458 MET A CE    
1890 N  N     . PHE A 242 ? 1.3706 1.1748 1.0999 -0.0210 0.1255  -0.0798 1459 PHE A N     
1891 C  CA    . PHE A 242 ? 1.3267 1.1316 1.0725 -0.0215 0.1236  -0.0908 1459 PHE A CA    
1892 C  C     . PHE A 242 ? 1.3715 1.1694 1.1329 -0.0173 0.1479  -0.0951 1459 PHE A C     
1893 O  O     . PHE A 242 ? 1.3242 1.1238 1.1063 -0.0164 0.1483  -0.1025 1459 PHE A O     
1894 C  CB    . PHE A 242 ? 1.1832 1.0104 0.9695 -0.0221 0.1059  -0.0874 1459 PHE A CB    
1895 C  CG    . PHE A 242 ? 1.1961 1.0284 0.9679 -0.0266 0.0816  -0.0877 1459 PHE A CG    
1896 C  CD1   . PHE A 242 ? 1.3054 1.1344 1.0708 -0.0304 0.0704  -0.0980 1459 PHE A CD1   
1897 C  CD2   . PHE A 242 ? 1.1843 1.0242 0.9494 -0.0270 0.0706  -0.0777 1459 PHE A CD2   
1898 C  CE1   . PHE A 242 ? 1.3369 1.1721 1.0913 -0.0349 0.0482  -0.0982 1459 PHE A CE1   
1899 C  CE2   . PHE A 242 ? 1.2398 1.0858 0.9937 -0.0305 0.0485  -0.0776 1459 PHE A CE2   
1900 C  CZ    . PHE A 242 ? 1.3050 1.1495 1.0543 -0.0346 0.0372  -0.0879 1459 PHE A CZ    
1901 N  N     . ASP A 243 ? 1.4599 1.2493 1.2114 -0.0143 0.1686  -0.0905 1460 ASP A N     
1902 C  CA    . ASP A 243 ? 1.5924 1.3752 1.3584 -0.0096 0.1939  -0.0940 1460 ASP A CA    
1903 C  C     . ASP A 243 ? 1.5255 1.3278 1.3467 -0.0067 0.1928  -0.0927 1460 ASP A C     
1904 O  O     . ASP A 243 ? 1.6274 1.4261 1.4618 -0.0043 0.1987  -0.1009 1460 ASP A O     
1905 C  CB    . ASP A 243 ? 1.7563 1.5149 1.4865 -0.0098 0.2037  -0.1077 1460 ASP A CB    
1906 C  CG    . ASP A 243 ? 1.9166 1.6547 1.5895 -0.0124 0.2058  -0.1092 1460 ASP A CG    
1907 O  OD1   . ASP A 243 ? 2.0023 1.7368 1.6469 -0.0175 0.1850  -0.1127 1460 ASP A OD1   
1908 O  OD2   . ASP A 243 ? 1.9463 1.6725 1.6029 -0.0094 0.2282  -0.1064 1460 ASP A OD2   
1909 N  N     . ILE A 244 ? 1.3928 1.2153 1.2453 -0.0069 0.1843  -0.0820 1461 ILE A N     
1910 C  CA    . ILE A 244 ? 1.2377 1.0798 1.1425 -0.0040 0.1839  -0.0787 1461 ILE A CA    
1911 C  C     . ILE A 244 ? 1.3271 1.1722 1.2528 -0.0004 0.2069  -0.0723 1461 ILE A C     
1912 O  O     . ILE A 244 ? 1.3532 1.2068 1.2886 -0.0017 0.2077  -0.0625 1461 ILE A O     
1913 C  CB    . ILE A 244 ? 1.0852 0.9466 1.0115 -0.0066 0.1612  -0.0720 1461 ILE A CB    
1914 C  CG1   . ILE A 244 ? 1.1837 1.0401 1.0808 -0.0109 0.1402  -0.0769 1461 ILE A CG1   
1915 C  CG2   . ILE A 244 ? 0.7948 0.6742 0.7697 -0.0038 0.1582  -0.0710 1461 ILE A CG2   
1916 C  CD1   . ILE A 244 ? 1.1530 1.0263 1.0649 -0.0132 0.1185  -0.0702 1461 ILE A CD1   
1917 N  N     . VAL A 245 ? 1.3655 1.2034 1.2996 0.0041  0.2264  -0.0780 1462 VAL A N     
1918 C  CA    . VAL A 245 ? 1.2900 1.1279 1.2395 0.0078  0.2518  -0.0731 1462 VAL A CA    
1919 C  C     . VAL A 245 ? 1.2181 1.0667 1.2128 0.0135  0.2625  -0.0750 1462 VAL A C     
1920 O  O     . VAL A 245 ? 1.1428 0.9908 1.1454 0.0156  0.2552  -0.0823 1462 VAL A O     
1921 C  CB    . VAL A 245 ? 1.2234 1.0353 1.1247 0.0084  0.2713  -0.0777 1462 VAL A CB    
1922 C  CG1   . VAL A 245 ? 1.2178 1.0216 1.0794 0.0036  0.2625  -0.0727 1462 VAL A CG1   
1923 C  CG2   . VAL A 245 ? 1.1410 0.9345 1.0150 0.0094  0.2711  -0.0915 1462 VAL A CG2   
1924 N  N     . TYR A 246 ? 1.1300 0.9894 1.1564 0.0161  0.2795  -0.0676 1463 TYR A N     
1925 C  CA    . TYR A 246 ? 1.1222 0.9923 1.1928 0.0224  0.2937  -0.0678 1463 TYR A CA    
1926 C  C     . TYR A 246 ? 1.1465 1.0112 1.2196 0.0253  0.3234  -0.0641 1463 TYR A C     
1927 O  O     . TYR A 246 ? 1.0745 0.9329 1.1256 0.0216  0.3301  -0.0584 1463 TYR A O     
1928 C  CB    . TYR A 246 ? 1.1275 1.0262 1.2519 0.0223  0.2787  -0.0607 1463 TYR A CB    
1929 C  CG    . TYR A 246 ? 1.1460 1.0579 1.2845 0.0174  0.2756  -0.0502 1463 TYR A CG    
1930 C  CD1   . TYR A 246 ? 1.1233 1.0507 1.3038 0.0188  0.2901  -0.0427 1463 TYR A CD1   
1931 C  CD2   . TYR A 246 ? 1.1493 1.0576 1.2598 0.0113  0.2585  -0.0475 1463 TYR A CD2   
1932 C  CE1   . TYR A 246 ? 1.0565 0.9944 1.2497 0.0133  0.2874  -0.0333 1463 TYR A CE1   
1933 C  CE2   . TYR A 246 ? 1.1552 1.0730 1.2770 0.0069  0.2563  -0.0380 1463 TYR A CE2   
1934 C  CZ    . TYR A 246 ? 1.0294 0.9611 1.1917 0.0075  0.2705  -0.0312 1463 TYR A CZ    
1935 O  OH    . TYR A 246 ? 0.9364 0.8755 1.1085 0.0022  0.2673  -0.0222 1463 TYR A OH    
1936 N  N     . GLU A 247 ? 1.2643 1.1305 1.3640 0.0322  0.3422  -0.0669 1464 GLU A N     
1937 C  CA    . GLU A 247 ? 1.3966 1.2620 1.5085 0.0354  0.3714  -0.0621 1464 GLU A CA    
1938 C  C     . GLU A 247 ? 1.4221 1.3161 1.5879 0.0335  0.3687  -0.0504 1464 GLU A C     
1939 O  O     . GLU A 247 ? 1.3340 1.2494 1.5433 0.0348  0.3539  -0.0486 1464 GLU A O     
1940 C  CB    . GLU A 247 ? 1.4144 1.2713 1.5369 0.0442  0.3940  -0.0692 1464 GLU A CB    
1941 C  CG    . GLU A 247 ? 1.4902 1.3258 1.5818 0.0467  0.4254  -0.0708 1464 GLU A CG    
1942 C  CD    . GLU A 247 ? 1.5456 1.3812 1.6670 0.0563  0.4524  -0.0736 1464 GLU A CD    
1943 O  OE1   . GLU A 247 ? 1.5855 1.4120 1.6994 0.0590  0.4813  -0.0716 1464 GLU A OE1   
1944 O  OE2   . GLU A 247 ? 1.5200 1.3647 1.6728 0.0615  0.4453  -0.0773 1464 GLU A OE2   
1945 N  N     . HIS A 248 ? 1.4916 1.3851 1.6529 0.0299  0.3816  -0.0424 1465 HIS A N     
1946 C  CA    . HIS A 248 ? 1.5650 1.4843 1.7781 0.0272  0.3813  -0.0318 1465 HIS A CA    
1947 C  C     . HIS A 248 ? 1.5061 1.4409 1.7713 0.0343  0.3991  -0.0311 1465 HIS A C     
1948 O  O     . HIS A 248 ? 1.5063 1.4272 1.7606 0.0406  0.4238  -0.0356 1465 HIS A O     
1949 C  CB    . HIS A 248 ? 1.6515 1.5648 1.8492 0.0219  0.3947  -0.0231 1465 HIS A CB    
1950 N  N     . PRO A 249 ? 1.5067 1.4696 1.8276 0.0340  0.3861  -0.0262 1466 PRO A N     
1951 C  CA    . PRO A 249 ? 1.5915 1.5714 1.9651 0.0414  0.4015  -0.0248 1466 PRO A CA    
1952 C  C     . PRO A 249 ? 1.6164 1.5949 2.0018 0.0429  0.4346  -0.0196 1466 PRO A C     
1953 O  O     . PRO A 249 ? 1.7023 1.6748 2.0949 0.0512  0.4583  -0.0229 1466 PRO A O     
1954 C  CB    . PRO A 249 ? 1.5578 1.5686 1.9841 0.0382  0.3783  -0.0187 1466 PRO A CB    
1955 C  CG    . PRO A 249 ? 1.4859 1.4911 1.8804 0.0320  0.3486  -0.0211 1466 PRO A CG    
1956 C  CD    . PRO A 249 ? 1.4784 1.4585 1.8161 0.0275  0.3565  -0.0221 1466 PRO A CD    
1957 N  N     . GLU A 250 ? 1.4512 1.4343 1.8392 0.0351  0.4379  -0.0112 1467 GLU A N     
1958 C  CA    . GLU A 250 ? 1.2996 1.2776 1.6911 0.0357  0.4708  -0.0057 1467 GLU A CA    
1959 C  C     . GLU A 250 ? 1.3490 1.2919 1.6708 0.0368  0.4872  -0.0107 1467 GLU A C     
1960 O  O     . GLU A 250 ? 1.4083 1.3362 1.7148 0.0444  0.5097  -0.0167 1467 GLU A O     
1961 C  CB    . GLU A 250 ? 1.2127 1.2071 1.6330 0.0265  0.4686  0.0055  1467 GLU A CB    
1962 N  N     . THR A 251 ? 1.3204 1.2494 1.5980 0.0295  0.4746  -0.0088 1468 THR A N     
1963 C  CA    . THR A 251 ? 1.4394 1.3360 1.6487 0.0296  0.4873  -0.0123 1468 THR A CA    
1964 C  C     . THR A 251 ? 1.6833 1.5602 1.8546 0.0356  0.4842  -0.0256 1468 THR A C     
1965 O  O     . THR A 251 ? 1.8264 1.7082 1.9987 0.0355  0.4583  -0.0315 1468 THR A O     
1966 C  CB    . THR A 251 ? 1.3550 1.2434 1.5279 0.0212  0.4677  -0.0076 1468 THR A CB    
1967 N  N     . LYS A 252 ? 1.7472 1.6011 1.8852 0.0407  0.5117  -0.0305 1469 LYS A N     
1968 C  CA    . LYS A 252 ? 1.7754 1.6080 1.8756 0.0459  0.5101  -0.0441 1469 LYS A CA    
1969 C  C     . LYS A 252 ? 1.7780 1.5912 1.8172 0.0401  0.4868  -0.0492 1469 LYS A C     
1970 O  O     . LYS A 252 ? 1.7520 1.5537 1.7681 0.0419  0.4742  -0.0603 1469 LYS A O     
1971 C  CB    . LYS A 252 ? 1.8400 1.6508 1.9173 0.0528  0.5466  -0.0488 1469 LYS A CB    
1972 N  N     . GLU A 253 ? 1.7362 1.5473 1.7533 0.0332  0.4796  -0.0408 1470 GLU A N     
1973 C  CA    . GLU A 253 ? 1.6140 1.4063 1.5715 0.0282  0.4603  -0.0439 1470 GLU A CA    
1974 C  C     . GLU A 253 ? 1.4929 1.2979 1.4604 0.0249  0.4244  -0.0473 1470 GLU A C     
1975 O  O     . GLU A 253 ? 1.4575 1.2882 1.4775 0.0243  0.4116  -0.0432 1470 GLU A O     
1976 C  CB    . GLU A 253 ? 1.6129 1.4008 1.5499 0.0228  0.4644  -0.0320 1470 GLU A CB    
1977 N  N     . LYS A 254 ? 1.4708 1.2572 1.3868 0.0228  0.4088  -0.0555 1471 LYS A N     
1978 C  CA    . LYS A 254 ? 1.3191 1.1145 1.2365 0.0192  0.3754  -0.0588 1471 LYS A CA    
1979 C  C     . LYS A 254 ? 1.4469 1.2600 1.3829 0.0136  0.3572  -0.0473 1471 LYS A C     
1980 O  O     . LYS A 254 ? 1.5061 1.3120 1.4195 0.0106  0.3627  -0.0392 1471 LYS A O     
1981 C  CB    . LYS A 254 ? 1.2138 0.9849 1.0689 0.0169  0.3640  -0.0684 1471 LYS A CB    
1982 N  N     . GLU A 255 ? 1.4315 1.2666 1.4082 0.0125  0.3363  -0.0465 1472 GLU A N     
1983 C  CA    . GLU A 255 ? 1.3727 1.2242 1.3684 0.0075  0.3175  -0.0371 1472 GLU A CA    
1984 C  C     . GLU A 255 ? 1.3721 1.2257 1.3534 0.0047  0.2874  -0.0417 1472 GLU A C     
1985 O  O     . GLU A 255 ? 1.4452 1.3025 1.4373 0.0069  0.2780  -0.0498 1472 GLU A O     
1986 C  CB    . GLU A 255 ? 1.3116 1.1893 1.3714 0.0080  0.3194  -0.0310 1472 GLU A CB    
1987 C  CG    . GLU A 255 ? 1.3376 1.2162 1.4176 0.0102  0.3492  -0.0256 1472 GLU A CG    
1988 C  CD    . GLU A 255 ? 1.4917 1.3605 1.5481 0.0059  0.3592  -0.0161 1472 GLU A CD    
1989 O  OE1   . GLU A 255 ? 1.5445 1.4103 1.5786 0.0013  0.3404  -0.0124 1472 GLU A OE1   
1990 O  OE2   . GLU A 255 ? 1.5614 1.4251 1.6218 0.0075  0.3866  -0.0118 1472 GLU A OE2   
1991 N  N     . TYR A 256 ? 1.3460 1.1970 1.3040 0.0003  0.2731  -0.0360 1473 TYR A N     
1992 C  CA    . TYR A 256 ? 1.2619 1.1166 1.2082 -0.0025 0.2447  -0.0385 1473 TYR A CA    
1993 C  C     . TYR A 256 ? 1.2353 1.1136 1.2270 -0.0044 0.2292  -0.0325 1473 TYR A C     
1994 O  O     . TYR A 256 ? 1.3448 1.2321 1.3619 -0.0058 0.2367  -0.0239 1473 TYR A O     
1995 C  CB    . TYR A 256 ? 1.2791 1.1189 1.1764 -0.0055 0.2371  -0.0351 1473 TYR A CB    
1996 C  CG    . TYR A 256 ? 1.3808 1.1964 1.2284 -0.0042 0.2498  -0.0416 1473 TYR A CG    
1997 C  CD1   . TYR A 256 ? 1.4343 1.2368 1.2670 -0.0024 0.2762  -0.0380 1473 TYR A CD1   
1998 C  CD2   . TYR A 256 ? 1.4640 1.2692 1.2793 -0.0052 0.2360  -0.0518 1473 TYR A CD2   
1999 C  CE1   . TYR A 256 ? 1.5295 1.3082 1.3138 -0.0011 0.2887  -0.0446 1473 TYR A CE1   
2000 C  CE2   . TYR A 256 ? 1.5684 1.3500 1.3361 -0.0045 0.2472  -0.0590 1473 TYR A CE2   
2001 C  CZ    . TYR A 256 ? 1.6302 1.3981 1.3813 -0.0022 0.2737  -0.0555 1473 TYR A CZ    
2002 O  OH    . TYR A 256 ? 1.7664 1.5093 1.4672 -0.0014 0.2856  -0.0629 1473 TYR A OH    
2003 N  N     . VAL A 257 ? 1.0657 0.9529 1.0666 -0.0048 0.2078  -0.0374 1474 VAL A N     
2004 C  CA    . VAL A 257 ? 1.0643 0.9725 1.1045 -0.0064 0.1919  -0.0328 1474 VAL A CA    
2005 C  C     . VAL A 257 ? 1.1098 1.0180 1.1358 -0.0103 0.1786  -0.0255 1474 VAL A C     
2006 O  O     . VAL A 257 ? 1.1518 1.0447 1.1369 -0.0113 0.1790  -0.0241 1474 VAL A O     
2007 C  CB    . VAL A 257 ? 0.9080 0.8242 0.9610 -0.0050 0.1753  -0.0402 1474 VAL A CB    
2008 C  CG1   . VAL A 257 ? 0.9544 0.8695 1.0233 -0.0005 0.1899  -0.0462 1474 VAL A CG1   
2009 C  CG2   . VAL A 257 ? 0.7809 0.6855 0.7934 -0.0069 0.1603  -0.0454 1474 VAL A CG2   
2010 N  N     . PHE A 258 ? 0.9873 0.9119 1.0468 -0.0122 0.1675  -0.0205 1475 PHE A N     
2011 C  CA    . PHE A 258 ? 1.0130 0.9388 1.0650 -0.0153 0.1536  -0.0140 1475 PHE A CA    
2012 C  C     . PHE A 258 ? 0.9980 0.9344 1.0585 -0.0155 0.1300  -0.0177 1475 PHE A C     
2013 O  O     . PHE A 258 ? 0.9371 0.8877 1.0311 -0.0147 0.1245  -0.0203 1475 PHE A O     
2014 C  CB    . PHE A 258 ? 1.0075 0.9421 1.0909 -0.0179 0.1600  -0.0057 1475 PHE A CB    
2015 C  CG    . PHE A 258 ? 1.0903 1.0140 1.1646 -0.0185 0.1832  0.0002  1475 PHE A CG    
2016 C  CD1   . PHE A 258 ? 1.1605 1.0696 1.2017 -0.0198 0.1861  0.0070  1475 PHE A CD1   
2017 C  CD2   . PHE A 258 ? 1.0161 0.9446 1.1160 -0.0173 0.2027  -0.0003 1475 PHE A CD2   
2018 C  CE1   . PHE A 258 ? 1.1422 1.0402 1.1735 -0.0203 0.2084  0.0132  1475 PHE A CE1   
2019 C  CE2   . PHE A 258 ? 1.0687 0.9873 1.1608 -0.0178 0.2256  0.0054  1475 PHE A CE2   
2020 C  CZ    . PHE A 258 ? 1.1383 1.0410 1.1949 -0.0195 0.2288  0.0122  1475 PHE A CZ    
2021 N  N     . GLN A 259 ? 1.0756 1.0054 1.1062 -0.0162 0.1163  -0.0175 1476 GLN A N     
2022 C  CA    . GLN A 259 ? 1.0442 0.9824 1.0786 -0.0161 0.0956  -0.0216 1476 GLN A CA    
2023 C  C     . GLN A 259 ? 0.8714 0.8150 0.9094 -0.0176 0.0814  -0.0154 1476 GLN A C     
2024 O  O     . GLN A 259 ? 0.8565 0.7925 0.8803 -0.0185 0.0852  -0.0083 1476 GLN A O     
2025 C  CB    . GLN A 259 ? 1.0828 1.0108 1.0828 -0.0157 0.0898  -0.0281 1476 GLN A CB    
2026 C  CG    . GLN A 259 ? 1.0636 0.9835 1.0573 -0.0141 0.1038  -0.0355 1476 GLN A CG    
2027 C  CD    . GLN A 259 ? 1.0223 0.9294 0.9783 -0.0149 0.0981  -0.0426 1476 GLN A CD    
2028 O  OE1   . GLN A 259 ? 1.1350 1.0266 1.0573 -0.0152 0.1073  -0.0432 1476 GLN A OE1   
2029 N  NE2   . GLN A 259 ? 0.8449 0.7582 0.8058 -0.0156 0.0826  -0.0478 1476 GLN A NE2   
2030 N  N     . ASN A 260 ? 0.8174 0.7736 0.8758 -0.0175 0.0662  -0.0179 1477 ASN A N     
2031 C  CA    . ASN A 260 ? 0.8556 0.8166 0.9147 -0.0180 0.0503  -0.0144 1477 ASN A CA    
2032 C  C     . ASN A 260 ? 0.9110 0.8764 0.9627 -0.0171 0.0349  -0.0198 1477 ASN A C     
2033 O  O     . ASN A 260 ? 1.0727 1.0407 1.1299 -0.0165 0.0353  -0.0262 1477 ASN A O     
2034 C  CB    . ASN A 260 ? 0.7780 0.7506 0.8712 -0.0190 0.0462  -0.0120 1477 ASN A CB    
2035 C  CG    . ASN A 260 ? 0.7714 0.7428 0.8805 -0.0210 0.0606  -0.0072 1477 ASN A CG    
2036 O  OD1   . ASN A 260 ? 0.8046 0.7647 0.8961 -0.0215 0.0728  -0.0027 1477 ASN A OD1   
2037 N  ND2   . ASN A 260 ? 0.7898 0.7731 0.9332 -0.0223 0.0592  -0.0078 1477 ASN A ND2   
2038 N  N     . SER A 261 ? 0.8935 0.8595 0.9339 -0.0169 0.0220  -0.0168 1478 SER A N     
2039 C  CA    . SER A 261 ? 0.9328 0.9061 0.9737 -0.0163 0.0067  -0.0206 1478 SER A CA    
2040 C  C     . SER A 261 ? 0.8548 0.8343 0.9052 -0.0155 -0.0043 -0.0159 1478 SER A C     
2041 O  O     . SER A 261 ? 0.8883 0.8629 0.9344 -0.0153 -0.0019 -0.0095 1478 SER A O     
2042 C  CB    . SER A 261 ? 0.9785 0.9452 0.9894 -0.0167 0.0015  -0.0236 1478 SER A CB    
2043 O  OG    . SER A 261 ? 1.0643 1.0267 1.0552 -0.0161 -0.0047 -0.0177 1478 SER A OG    
2044 N  N     . TRP A 262 ? 0.7092 0.6985 0.7731 -0.0148 -0.0152 -0.0190 1479 TRP A N     
2045 C  CA    . TRP A 262 ? 0.7376 0.7323 0.8116 -0.0136 -0.0245 -0.0156 1479 TRP A CA    
2046 C  C     . TRP A 262 ? 0.7939 0.7967 0.8701 -0.0126 -0.0368 -0.0190 1479 TRP A C     
2047 O  O     . TRP A 262 ? 0.7571 0.7632 0.8366 -0.0132 -0.0374 -0.0243 1479 TRP A O     
2048 C  CB    . TRP A 262 ? 0.6135 0.6121 0.7130 -0.0145 -0.0208 -0.0147 1479 TRP A CB    
2049 C  CG    . TRP A 262 ? 0.7709 0.7736 0.8876 -0.0156 -0.0131 -0.0187 1479 TRP A CG    
2050 C  CD1   . TRP A 262 ? 0.8847 0.8828 1.0033 -0.0168 0.0006  -0.0181 1479 TRP A CD1   
2051 C  CD2   . TRP A 262 ? 0.6402 0.6524 0.7751 -0.0149 -0.0183 -0.0232 1479 TRP A CD2   
2052 N  NE1   . TRP A 262 ? 0.7601 0.7651 0.8988 -0.0166 0.0039  -0.0220 1479 TRP A NE1   
2053 C  CE2   . TRP A 262 ? 0.7235 0.7370 0.8719 -0.0154 -0.0080 -0.0249 1479 TRP A CE2   
2054 C  CE3   . TRP A 262 ? 0.7027 0.7220 0.8435 -0.0136 -0.0299 -0.0253 1479 TRP A CE3   
2055 C  CZ2   . TRP A 262 ? 0.7473 0.7692 0.9153 -0.0143 -0.0103 -0.0283 1479 TRP A CZ2   
2056 C  CZ3   . TRP A 262 ? 0.8245 0.8512 0.9822 -0.0129 -0.0318 -0.0287 1479 TRP A CZ3   
2057 C  CH2   . TRP A 262 ? 0.7765 0.8045 0.9478 -0.0131 -0.0226 -0.0299 1479 TRP A CH2   
2058 N  N     . GLY A 263 ? 0.8455 0.8512 0.9208 -0.0107 -0.0457 -0.0158 1480 GLY A N     
2059 C  CA    . GLY A 263 ? 0.8334 0.8467 0.9094 -0.0096 -0.0563 -0.0181 1480 GLY A CA    
2060 C  C     . GLY A 263 ? 0.6911 0.7087 0.7748 -0.0069 -0.0635 -0.0150 1480 GLY A C     
2061 O  O     . GLY A 263 ? 0.7738 0.7863 0.8546 -0.0054 -0.0623 -0.0100 1480 GLY A O     
2062 N  N     . ILE A 264 ? 0.7105 0.7362 0.8032 -0.0060 -0.0703 -0.0178 1481 ILE A N     
2063 C  CA    . ILE A 264 ? 0.6408 0.6703 0.7383 -0.0027 -0.0768 -0.0152 1481 ILE A CA    
2064 C  C     . ILE A 264 ? 0.6414 0.6795 0.7403 -0.0020 -0.0839 -0.0173 1481 ILE A C     
2065 O  O     . ILE A 264 ? 0.7272 0.7687 0.8308 -0.0040 -0.0837 -0.0215 1481 ILE A O     
2066 C  CB    . ILE A 264 ? 0.6339 0.6625 0.7459 -0.0020 -0.0754 -0.0158 1481 ILE A CB    
2067 C  CG1   . ILE A 264 ? 0.6882 0.7169 0.8014 0.0018  -0.0802 -0.0130 1481 ILE A CG1   
2068 C  CG2   . ILE A 264 ? 0.5912 0.6257 0.7156 -0.0031 -0.0766 -0.0207 1481 ILE A CG2   
2069 C  CD1   . ILE A 264 ? 0.6672 0.6936 0.7925 0.0019  -0.0798 -0.0150 1481 ILE A CD1   
2070 N  N     . THR A 265 ? 0.6629 0.7046 0.7591 0.0011  -0.0896 -0.0137 1482 THR A N     
2071 C  CA    . THR A 265 ? 0.6317 0.6823 0.7281 0.0015  -0.0962 -0.0142 1482 THR A CA    
2072 C  C     . THR A 265 ? 0.6721 0.7286 0.7793 0.0055  -0.0993 -0.0130 1482 THR A C     
2073 O  O     . THR A 265 ? 0.7503 0.8027 0.8625 0.0080  -0.0971 -0.0123 1482 THR A O     
2074 C  CB    . THR A 265 ? 0.6491 0.7005 0.7328 0.0018  -0.1007 -0.0104 1482 THR A CB    
2075 O  OG1   . THR A 265 ? 0.7304 0.7837 0.8163 0.0070  -0.1040 -0.0047 1482 THR A OG1   
2076 C  CG2   . THR A 265 ? 0.5710 0.6126 0.6399 -0.0005 -0.0959 -0.0098 1482 THR A CG2   
2077 N  N     . THR A 266 ? 0.7472 0.8129 0.8579 0.0058  -0.1042 -0.0130 1483 THR A N     
2078 C  CA    . THR A 266 ? 0.7917 0.8633 0.9122 0.0099  -0.1057 -0.0119 1483 THR A CA    
2079 C  C     . THR A 266 ? 0.7857 0.8578 0.9062 0.0154  -0.1077 -0.0065 1483 THR A C     
2080 O  O     . THR A 266 ? 0.7096 0.7851 0.8377 0.0198  -0.1076 -0.0054 1483 THR A O     
2081 C  CB    . THR A 266 ? 0.6457 0.7275 0.7721 0.0079  -0.1089 -0.0133 1483 THR A CB    
2082 O  OG1   . THR A 266 ? 0.7729 0.8580 0.8931 0.0041  -0.1129 -0.0132 1483 THR A OG1   
2083 C  CG2   . THR A 266 ? 0.4936 0.5740 0.6241 0.0053  -0.1058 -0.0177 1483 THR A CG2   
2084 N  N     . ARG A 267 ? 0.6614 0.7293 0.7727 0.0158  -0.1088 -0.0027 1484 ARG A N     
2085 C  CA    . ARG A 267 ? 0.7522 0.8170 0.8629 0.0217  -0.1095 0.0032  1484 ARG A CA    
2086 C  C     . ARG A 267 ? 0.7693 0.8255 0.8850 0.0248  -0.1044 0.0022  1484 ARG A C     
2087 O  O     . ARG A 267 ? 0.7486 0.8038 0.8684 0.0307  -0.1044 0.0056  1484 ARG A O     
2088 C  CB    . ARG A 267 ? 0.8796 0.9375 0.9767 0.0208  -0.1099 0.0073  1484 ARG A CB    
2089 C  CG    . ARG A 267 ? 1.0074 1.0580 1.1016 0.0266  -0.1091 0.0142  1484 ARG A CG    
2090 C  CD    . ARG A 267 ? 1.1394 1.1831 1.2174 0.0251  -0.1093 0.0185  1484 ARG A CD    
2091 N  NE    . ARG A 267 ? 1.3605 1.4096 1.4299 0.0196  -0.1127 0.0152  1484 ARG A NE    
2092 C  CZ    . ARG A 267 ? 1.4975 1.5525 1.5578 0.0197  -0.1204 0.0184  1484 ARG A CZ    
2093 N  NH1   . ARG A 267 ? 1.5069 1.5647 1.5668 0.0257  -0.1259 0.0262  1484 ARG A NH1   
2094 N  NH2   . ARG A 267 ? 1.4670 1.5247 1.5188 0.0137  -0.1229 0.0136  1484 ARG A NH2   
2095 N  N     . THR A 268 ? 0.5914 0.6415 0.7076 0.0208  -0.1002 -0.0027 1485 THR A N     
2096 C  CA    . THR A 268 ? 0.6500 0.6929 0.7713 0.0223  -0.0969 -0.0053 1485 THR A CA    
2097 C  C     . THR A 268 ? 0.6436 0.6909 0.7710 0.0275  -0.0980 -0.0056 1485 THR A C     
2098 O  O     . THR A 268 ? 0.7423 0.7827 0.8707 0.0321  -0.0962 -0.0043 1485 THR A O     
2099 C  CB    . THR A 268 ? 0.7045 0.7459 0.8288 0.0172  -0.0948 -0.0111 1485 THR A CB    
2100 O  OG1   . THR A 268 ? 0.7346 0.7852 0.8616 0.0155  -0.0970 -0.0138 1485 THR A OG1   
2101 C  CG2   . THR A 268 ? 0.7282 0.7643 0.8482 0.0128  -0.0916 -0.0107 1485 THR A CG2   
2102 N  N     . ILE A 269 ? 0.5870 0.6451 0.7184 0.0269  -0.1002 -0.0072 1486 ILE A N     
2103 C  CA    . ILE A 269 ? 0.7169 0.7795 0.8540 0.0316  -0.0996 -0.0076 1486 ILE A CA    
2104 C  C     . ILE A 269 ? 0.7392 0.8041 0.8794 0.0383  -0.1001 -0.0019 1486 ILE A C     
2105 O  O     . ILE A 269 ? 0.5675 0.6287 0.7105 0.0439  -0.0971 -0.0020 1486 ILE A O     
2106 C  CB    . ILE A 269 ? 0.7724 0.8462 0.9139 0.0290  -0.1010 -0.0093 1486 ILE A CB    
2107 C  CG1   . ILE A 269 ? 0.8743 0.9445 1.0136 0.0240  -0.0999 -0.0143 1486 ILE A CG1   
2108 C  CG2   . ILE A 269 ? 0.6955 0.7744 0.8428 0.0340  -0.0989 -0.0088 1486 ILE A CG2   
2109 C  CD1   . ILE A 269 ? 0.8739 0.9530 1.0167 0.0207  -0.1010 -0.0153 1486 ILE A CD1   
2110 N  N     . GLY A 270 ? 0.8074 0.8782 0.9467 0.0382  -0.1042 0.0030  1487 GLY A N     
2111 C  CA    . GLY A 270 ? 0.9345 1.0078 1.0777 0.0452  -0.1056 0.0095  1487 GLY A CA    
2112 C  C     . GLY A 270 ? 0.9905 1.0488 1.1302 0.0497  -0.1014 0.0109  1487 GLY A C     
2113 O  O     . GLY A 270 ? 0.9373 0.9934 1.0824 0.0567  -0.0986 0.0125  1487 GLY A O     
2114 N  N     . VAL A 271 ? 0.9887 1.0355 1.1199 0.0455  -0.0999 0.0098  1488 VAL A N     
2115 C  CA    . VAL A 271 ? 0.8606 0.8916 0.9892 0.0482  -0.0954 0.0106  1488 VAL A CA    
2116 C  C     . VAL A 271 ? 0.7022 0.7277 0.8349 0.0505  -0.0916 0.0049  1488 VAL A C     
2117 O  O     . VAL A 271 ? 0.6516 0.6692 0.7862 0.0569  -0.0886 0.0065  1488 VAL A O     
2118 C  CB    . VAL A 271 ? 0.8712 0.8921 0.9926 0.0418  -0.0934 0.0095  1488 VAL A CB    
2119 C  CG1   . VAL A 271 ? 0.7872 0.7917 0.9067 0.0445  -0.0890 0.0123  1488 VAL A CG1   
2120 C  CG2   . VAL A 271 ? 0.8650 0.8919 0.9792 0.0387  -0.0967 0.0136  1488 VAL A CG2   
2121 N  N     . MET A 272 ? 0.6740 0.7032 0.8072 0.0458  -0.0917 -0.0018 1489 MET A N     
2122 C  CA    . MET A 272 ? 0.7040 0.7276 0.8378 0.0478  -0.0887 -0.0076 1489 MET A CA    
2123 C  C     . MET A 272 ? 0.6145 0.6412 0.7529 0.0564  -0.0863 -0.0049 1489 MET A C     
2124 O  O     . MET A 272 ? 0.7676 0.7823 0.9047 0.0613  -0.0823 -0.0062 1489 MET A O     
2125 C  CB    . MET A 272 ? 0.6530 0.6834 0.7864 0.0426  -0.0903 -0.0131 1489 MET A CB    
2126 C  CG    . MET A 272 ? 0.7637 0.7875 0.8940 0.0435  -0.0882 -0.0196 1489 MET A CG    
2127 S  SD    . MET A 272 ? 0.8228 0.8588 0.9533 0.0418  -0.0893 -0.0221 1489 MET A SD    
2128 C  CE    . MET A 272 ? 0.6651 0.7166 0.8037 0.0445  -0.0898 -0.0152 1489 MET A CE    
2129 N  N     . ILE A 273 ? 0.5504 0.5929 0.6953 0.0585  -0.0886 -0.0008 1490 ILE A N     
2130 C  CA    . ILE A 273 ? 0.6606 0.7092 0.8136 0.0669  -0.0860 0.0028  1490 ILE A CA    
2131 C  C     . ILE A 273 ? 0.7809 0.8201 0.9350 0.0740  -0.0843 0.0081  1490 ILE A C     
2132 O  O     . ILE A 273 ? 0.7167 0.7459 0.8713 0.0804  -0.0786 0.0066  1490 ILE A O     
2133 C  CB    . ILE A 273 ? 0.7410 0.8097 0.9034 0.0664  -0.0902 0.0073  1490 ILE A CB    
2134 C  CG1   . ILE A 273 ? 0.8389 0.9147 1.0006 0.0601  -0.0904 0.0022  1490 ILE A CG1   
2135 C  CG2   . ILE A 273 ? 0.6724 0.7498 0.8471 0.0754  -0.0876 0.0123  1490 ILE A CG2   
2136 C  CD1   . ILE A 273 ? 0.8414 0.9335 1.0095 0.0554  -0.0961 0.0052  1490 ILE A CD1   
2137 N  N     . MET A 274 ? 0.8533 0.8936 1.0061 0.0729  -0.0887 0.0142  1491 MET A N     
2138 C  CA    . MET A 274 ? 0.7672 0.8000 0.9217 0.0806  -0.0877 0.0213  1491 MET A CA    
2139 C  C     . MET A 274 ? 0.7913 0.8024 0.9401 0.0821  -0.0814 0.0175  1491 MET A C     
2140 O  O     . MET A 274 ? 0.6970 0.6994 0.8491 0.0905  -0.0776 0.0212  1491 MET A O     
2141 C  CB    . MET A 274 ? 0.6932 0.7269 0.8423 0.0780  -0.0932 0.0281  1491 MET A CB    
2142 C  CG    . MET A 274 ? 0.7132 0.7666 0.8670 0.0774  -0.1008 0.0330  1491 MET A CG    
2143 S  SD    . MET A 274 ? 0.6836 0.7515 0.8548 0.0882  -0.1015 0.0391  1491 MET A SD    
2144 C  CE    . MET A 274 ? 0.6790 0.7636 0.8514 0.0872  -0.1132 0.0477  1491 MET A CE    
2145 N  N     . VAL A 275 ? 0.7234 0.7257 0.8648 0.0742  -0.0804 0.0099  1492 VAL A N     
2146 C  CA    . VAL A 275 ? 0.6317 0.6132 0.7682 0.0739  -0.0756 0.0056  1492 VAL A CA    
2147 C  C     . VAL A 275 ? 0.8103 0.7858 0.9460 0.0770  -0.0712 -0.0021 1492 VAL A C     
2148 O  O     . VAL A 275 ? 0.9841 0.9438 1.1184 0.0820  -0.0661 -0.0036 1492 VAL A O     
2149 C  CB    . VAL A 275 ? 0.6528 0.6279 0.7836 0.0637  -0.0772 0.0018  1492 VAL A CB    
2150 C  CG1   . VAL A 275 ? 0.5326 0.4877 0.6600 0.0609  -0.0732 -0.0053 1492 VAL A CG1   
2151 C  CG2   . VAL A 275 ? 0.6039 0.5797 0.7326 0.0620  -0.0791 0.0098  1492 VAL A CG2   
2152 N  N     . HIS A 276 ? 0.7167 0.7038 0.8523 0.0745  -0.0724 -0.0068 1493 HIS A N     
2153 C  CA    . HIS A 276 ? 0.6436 0.6220 0.7733 0.0751  -0.0686 -0.0155 1493 HIS A CA    
2154 C  C     . HIS A 276 ? 0.7050 0.6914 0.8385 0.0829  -0.0641 -0.0149 1493 HIS A C     
2155 O  O     . HIS A 276 ? 0.8670 0.8432 0.9936 0.0856  -0.0591 -0.0215 1493 HIS A O     
2156 C  CB    . HIS A 276 ? 0.8264 0.8075 0.9504 0.0658  -0.0726 -0.0222 1493 HIS A CB    
2157 C  CG    . HIS A 276 ? 0.8164 0.7871 0.9376 0.0581  -0.0754 -0.0248 1493 HIS A CG    
2158 N  ND1   . HIS A 276 ? 0.8468 0.7984 0.9639 0.0574  -0.0730 -0.0295 1493 HIS A ND1   
2159 C  CD2   . HIS A 276 ? 0.8555 0.8323 0.9785 0.0506  -0.0796 -0.0236 1493 HIS A CD2   
2160 C  CE1   . HIS A 276 ? 0.8765 0.8242 0.9947 0.0494  -0.0759 -0.0306 1493 HIS A CE1   
2161 N  NE2   . HIS A 276 ? 0.8071 0.7700 0.9288 0.0456  -0.0794 -0.0270 1493 HIS A NE2   
2162 N  N     . ALA A 277 ? 0.6060 0.6108 0.7500 0.0860  -0.0657 -0.0077 1494 ALA A N     
2163 C  CA    . ALA A 277 ? 0.7190 0.7340 0.8699 0.0929  -0.0608 -0.0065 1494 ALA A CA    
2164 C  C     . ALA A 277 ? 0.8623 0.8691 1.0187 0.1040  -0.0542 -0.0030 1494 ALA A C     
2165 O  O     . ALA A 277 ? 0.8630 0.8682 1.0252 0.1075  -0.0564 0.0038  1494 ALA A O     
2166 C  CB    . ALA A 277 ? 0.4973 0.5358 0.6598 0.0910  -0.0656 -0.0002 1494 ALA A CB    
2167 N  N     . ASP A 278 ? 0.8799 0.8808 1.0339 0.1102  -0.0458 -0.0074 1495 ASP A N     
2168 C  CA    . ASP A 278 ? 0.7425 0.7340 0.9020 0.1214  -0.0383 -0.0048 1495 ASP A CA    
2169 C  C     . ASP A 278 ? 0.7789 0.7900 0.9557 0.1299  -0.0338 0.0018  1495 ASP A C     
2170 O  O     . ASP A 278 ? 0.7480 0.7808 0.9344 0.1261  -0.0387 0.0060  1495 ASP A O     
2171 C  CB    . ASP A 278 ? 0.7354 0.7022 0.8790 0.1229  -0.0309 -0.0152 1495 ASP A CB    
2172 C  CG    . ASP A 278 ? 0.8325 0.8010 0.9666 0.1222  -0.0257 -0.0224 1495 ASP A CG    
2173 O  OD1   . ASP A 278 ? 0.8198 0.8081 0.9634 0.1236  -0.0245 -0.0182 1495 ASP A OD1   
2174 O  OD2   . ASP A 278 ? 0.8444 0.7935 0.9611 0.1201  -0.0229 -0.0323 1495 ASP A OD2   
2175 N  N     . ASN A 279 ? 0.9112 0.9145 1.0930 0.1412  -0.0241 0.0025  1496 ASN A N     
2176 C  CA    . ASN A 279 ? 0.8717 0.8941 1.0736 0.1504  -0.0189 0.0096  1496 ASN A CA    
2177 C  C     . ASN A 279 ? 0.8269 0.8566 1.0266 0.1500  -0.0111 0.0048  1496 ASN A C     
2178 O  O     . ASN A 279 ? 0.6122 0.6585 0.8296 0.1569  -0.0052 0.0101  1496 ASN A O     
2179 C  CB    . ASN A 279 ? 0.7158 0.7273 0.9262 0.1639  -0.0109 0.0136  1496 ASN A CB    
2180 C  CG    . ASN A 279 ? 0.8375 0.8543 1.0600 0.1668  -0.0193 0.0243  1496 ASN A CG    
2181 O  OD1   . ASN A 279 ? 0.8543 0.8879 1.0819 0.1599  -0.0305 0.0296  1496 ASN A OD1   
2182 N  ND2   . ASN A 279 ? 0.8852 0.8869 1.1113 0.1773  -0.0138 0.0276  1496 ASN A ND2   
2183 N  N     . GLN A 280 ? 0.8373 0.8565 1.0169 0.1419  -0.0115 -0.0043 1497 GLN A N     
2184 C  CA    . GLN A 280 ? 0.7417 0.7684 0.9175 0.1407  -0.0052 -0.0075 1497 GLN A CA    
2185 C  C     . GLN A 280 ? 0.8939 0.9353 1.0689 0.1290  -0.0147 -0.0068 1497 GLN A C     
2186 O  O     . GLN A 280 ? 1.0538 1.1014 1.2249 0.1266  -0.0105 -0.0087 1497 GLN A O     
2187 C  CB    . GLN A 280 ? 0.8151 0.8173 0.9668 0.1424  0.0034  -0.0183 1497 GLN A CB    
2188 N  N     . GLY A 281 ? 0.9208 0.9670 1.0989 0.1221  -0.0265 -0.0039 1498 GLY A N     
2189 C  CA    . GLY A 281 ? 0.8469 0.9061 1.0248 0.1116  -0.0345 -0.0034 1498 GLY A CA    
2190 C  C     . GLY A 281 ? 0.9090 0.9569 1.0722 0.1024  -0.0433 -0.0081 1498 GLY A C     
2191 O  O     . GLY A 281 ? 0.9409 0.9751 1.0992 0.1032  -0.0454 -0.0092 1498 GLY A O     
2192 N  N     . LEU A 282 ? 0.9392 0.9915 1.0957 0.0939  -0.0475 -0.0109 1499 LEU A N     
2193 C  CA    . LEU A 282 ? 0.8689 0.9124 1.0145 0.0854  -0.0553 -0.0149 1499 LEU A CA    
2194 C  C     . LEU A 282 ? 0.8429 0.8648 0.9715 0.0856  -0.0531 -0.0231 1499 LEU A C     
2195 O  O     . LEU A 282 ? 0.8583 0.8721 0.9776 0.0897  -0.0462 -0.0276 1499 LEU A O     
2196 C  CB    . LEU A 282 ? 0.7876 0.8404 0.9310 0.0773  -0.0597 -0.0159 1499 LEU A CB    
2197 C  CG    . LEU A 282 ? 0.7295 0.8018 0.8881 0.0745  -0.0637 -0.0093 1499 LEU A CG    
2198 C  CD1   . LEU A 282 ? 0.7871 0.8667 0.9440 0.0697  -0.0628 -0.0104 1499 LEU A CD1   
2199 C  CD2   . LEU A 282 ? 0.6327 0.7046 0.7917 0.0691  -0.0721 -0.0079 1499 LEU A CD2   
2200 N  N     . VAL A 283 ? 0.8330 0.8455 0.9569 0.0801  -0.0591 -0.0254 1500 VAL A N     
2201 C  CA    . VAL A 283 ? 0.7790 0.7737 0.8879 0.0766  -0.0601 -0.0339 1500 VAL A CA    
2202 C  C     . VAL A 283 ? 0.7956 0.7936 0.9040 0.0669  -0.0685 -0.0347 1500 VAL A C     
2203 O  O     . VAL A 283 ? 0.7511 0.7500 0.8660 0.0642  -0.0720 -0.0312 1500 VAL A O     
2204 C  CB    . VAL A 283 ? 0.7130 0.6893 0.8188 0.0805  -0.0570 -0.0364 1500 VAL A CB    
2205 C  CG1   . VAL A 283 ? 0.8365 0.7957 0.9274 0.0755  -0.0591 -0.0460 1500 VAL A CG1   
2206 C  CG2   . VAL A 283 ? 0.5682 0.5415 0.6769 0.0915  -0.0476 -0.0346 1500 VAL A CG2   
2207 N  N     . LEU A 284 ? 0.8038 0.8042 0.9047 0.0623  -0.0712 -0.0387 1501 LEU A N     
2208 C  CA    . LEU A 284 ? 0.8755 0.8814 0.9782 0.0540  -0.0784 -0.0389 1501 LEU A CA    
2209 C  C     . LEU A 284 ? 0.7996 0.7918 0.8959 0.0489  -0.0827 -0.0453 1501 LEU A C     
2210 O  O     . LEU A 284 ? 0.6632 0.6437 0.7479 0.0497  -0.0822 -0.0519 1501 LEU A O     
2211 C  CB    . LEU A 284 ? 0.8840 0.8992 0.9835 0.0520  -0.0795 -0.0389 1501 LEU A CB    
2212 C  CG    . LEU A 284 ? 0.7958 0.8259 0.9053 0.0550  -0.0761 -0.0322 1501 LEU A CG    
2213 C  CD1   . LEU A 284 ? 0.7020 0.7397 0.8085 0.0532  -0.0756 -0.0317 1501 LEU A CD1   
2214 C  CD2   . LEU A 284 ? 0.7283 0.7670 0.8493 0.0517  -0.0800 -0.0274 1501 LEU A CD2   
2215 N  N     . PRO A 285 ? 0.7124 0.7059 0.8159 0.0435  -0.0866 -0.0436 1502 PRO A N     
2216 C  CA    . PRO A 285 ? 0.6967 0.6814 0.7982 0.0372  -0.0913 -0.0491 1502 PRO A CA    
2217 C  C     . PRO A 285 ? 0.7310 0.7191 0.8262 0.0341  -0.0959 -0.0533 1502 PRO A C     
2218 O  O     . PRO A 285 ? 0.7398 0.7401 0.8380 0.0332  -0.0972 -0.0499 1502 PRO A O     
2219 C  CB    . PRO A 285 ? 0.6569 0.6476 0.7692 0.0323  -0.0931 -0.0445 1502 PRO A CB    
2220 C  CG    . PRO A 285 ? 0.6742 0.6714 0.7909 0.0370  -0.0896 -0.0374 1502 PRO A CG    
2221 C  CD    . PRO A 285 ? 0.7060 0.7097 0.8198 0.0428  -0.0869 -0.0365 1502 PRO A CD    
2222 N  N     . PRO A 286 ? 0.7282 0.7050 0.8140 0.0324  -0.0989 -0.0606 1503 PRO A N     
2223 C  CA    . PRO A 286 ? 0.7665 0.7460 0.8435 0.0306  -0.1041 -0.0640 1503 PRO A CA    
2224 C  C     . PRO A 286 ? 0.8312 0.8238 0.9179 0.0257  -0.1093 -0.0607 1503 PRO A C     
2225 O  O     . PRO A 286 ? 1.0187 1.0180 1.1006 0.0267  -0.1110 -0.0593 1503 PRO A O     
2226 C  CB    . PRO A 286 ? 0.8992 0.8639 0.9672 0.0274  -0.1087 -0.0729 1503 PRO A CB    
2227 C  CG    . PRO A 286 ? 0.8805 0.8320 0.9482 0.0304  -0.1026 -0.0744 1503 PRO A CG    
2228 C  CD    . PRO A 286 ? 0.8128 0.7728 0.8951 0.0316  -0.0983 -0.0661 1503 PRO A CD    
2229 N  N     . ARG A 287 ? 0.7168 0.7124 0.8167 0.0209  -0.1110 -0.0589 1504 ARG A N     
2230 C  CA    . ARG A 287 ? 0.7421 0.7481 0.8515 0.0164  -0.1156 -0.0570 1504 ARG A CA    
2231 C  C     . ARG A 287 ? 0.7769 0.7948 0.8916 0.0179  -0.1124 -0.0505 1504 ARG A C     
2232 O  O     . ARG A 287 ? 0.9407 0.9664 1.0618 0.0152  -0.1153 -0.0490 1504 ARG A O     
2233 C  CB    . ARG A 287 ? 0.7595 0.7637 0.8814 0.0104  -0.1176 -0.0581 1504 ARG A CB    
2234 C  CG    . ARG A 287 ? 0.6255 0.6204 0.7445 0.0066  -0.1238 -0.0655 1504 ARG A CG    
2235 C  CD    . ARG A 287 ? 0.7091 0.7054 0.8437 -0.0004 -0.1269 -0.0665 1504 ARG A CD    
2236 N  NE    . ARG A 287 ? 0.8052 0.8151 0.9518 -0.0023 -0.1285 -0.0625 1504 ARG A NE    
2237 C  CZ    . ARG A 287 ? 0.7826 0.7970 0.9458 -0.0078 -0.1298 -0.0621 1504 ARG A CZ    
2238 N  NH1   . ARG A 287 ? 0.8045 0.8111 0.9745 -0.0127 -0.1301 -0.0654 1504 ARG A NH1   
2239 N  NH2   . ARG A 287 ? 0.8092 0.8354 0.9829 -0.0084 -0.1298 -0.0583 1504 ARG A NH2   
2240 N  N     . VAL A 288 ? 0.7135 0.7331 0.8265 0.0222  -0.1067 -0.0469 1505 VAL A N     
2241 C  CA    . VAL A 288 ? 0.6444 0.6749 0.7619 0.0230  -0.1044 -0.0416 1505 VAL A CA    
2242 C  C     . VAL A 288 ? 0.7055 0.7390 0.8160 0.0276  -0.1014 -0.0401 1505 VAL A C     
2243 O  O     . VAL A 288 ? 0.7942 0.8367 0.9087 0.0275  -0.0999 -0.0361 1505 VAL A O     
2244 C  CB    . VAL A 288 ? 0.6385 0.6716 0.7627 0.0230  -0.1012 -0.0375 1505 VAL A CB    
2245 C  CG1   . VAL A 288 ? 0.5363 0.5667 0.6671 0.0181  -0.1025 -0.0380 1505 VAL A CG1   
2246 C  CG2   . VAL A 288 ? 0.6808 0.7081 0.8016 0.0279  -0.0976 -0.0368 1505 VAL A CG2   
2247 N  N     . ALA A 289 ? 0.5954 0.6211 0.6955 0.0313  -0.1000 -0.0433 1506 ALA A N     
2248 C  CA    . ALA A 289 ? 0.7158 0.7436 0.8091 0.0362  -0.0952 -0.0416 1506 ALA A CA    
2249 C  C     . ALA A 289 ? 0.8386 0.8706 0.9273 0.0349  -0.0973 -0.0405 1506 ALA A C     
2250 O  O     . ALA A 289 ? 0.8374 0.8641 0.9180 0.0334  -0.1024 -0.0441 1506 ALA A O     
2251 C  CB    . ALA A 289 ? 0.6815 0.6975 0.7627 0.0407  -0.0921 -0.0461 1506 ALA A CB    
2252 N  N     . CYS A 290 ? 0.9322 0.9736 1.0262 0.0356  -0.0937 -0.0354 1507 CYS A N     
2253 C  CA    . CYS A 290 ? 0.9629 1.0071 1.0524 0.0350  -0.0941 -0.0332 1507 CYS A CA    
2254 C  C     . CYS A 290 ? 0.8671 0.9025 0.9389 0.0384  -0.0938 -0.0360 1507 CYS A C     
2255 O  O     . CYS A 290 ? 0.8417 0.8744 0.9060 0.0371  -0.0990 -0.0368 1507 CYS A O     
2256 C  CB    . CYS A 290 ? 1.1514 1.2051 1.2487 0.0356  -0.0883 -0.0276 1507 CYS A CB    
2257 S  SG    . CYS A 290 ? 1.1984 1.2550 1.2923 0.0347  -0.0869 -0.0232 1507 CYS A SG    
2258 N  N     . ILE A 291 ? 0.8443 0.8745 0.9087 0.0431  -0.0878 -0.0376 1508 ILE A N     
2259 C  CA    . ILE A 291 ? 0.9243 0.9432 0.9687 0.0465  -0.0869 -0.0419 1508 ILE A CA    
2260 C  C     . ILE A 291 ? 0.9733 0.9815 1.0136 0.0469  -0.0889 -0.0487 1508 ILE A C     
2261 O  O     . ILE A 291 ? 1.0098 1.0177 1.0579 0.0493  -0.0840 -0.0485 1508 ILE A O     
2262 C  CB    . ILE A 291 ? 0.8135 0.8327 0.8506 0.0522  -0.0763 -0.0389 1508 ILE A CB    
2263 C  CG1   . ILE A 291 ? 0.7246 0.7545 0.7693 0.0508  -0.0736 -0.0316 1508 ILE A CG1   
2264 C  CG2   . ILE A 291 ? 0.7914 0.7973 0.8034 0.0556  -0.0752 -0.0433 1508 ILE A CG2   
2265 C  CD1   . ILE A 291 ? 0.6232 0.6528 0.6597 0.0557  -0.0628 -0.0281 1508 ILE A CD1   
2266 N  N     . GLN A 292 ? 0.9437 0.9431 0.9733 0.0442  -0.0968 -0.0545 1509 GLN A N     
2267 C  CA    . GLN A 292 ? 0.8726 0.8597 0.8972 0.0441  -0.0982 -0.0617 1509 GLN A CA    
2268 C  C     . GLN A 292 ? 0.8359 0.8102 0.8398 0.0497  -0.0921 -0.0663 1509 GLN A C     
2269 O  O     . GLN A 292 ? 0.9518 0.9170 0.9544 0.0528  -0.0868 -0.0698 1509 GLN A O     
2270 C  CB    . GLN A 292 ? 0.6608 0.6440 0.6850 0.0379  -0.1096 -0.0668 1509 GLN A CB    
2271 C  CG    . GLN A 292 ? 0.7175 0.7101 0.7631 0.0326  -0.1138 -0.0638 1509 GLN A CG    
2272 C  CD    . GLN A 292 ? 0.8982 0.8924 0.9463 0.0269  -0.1249 -0.0665 1509 GLN A CD    
2273 O  OE1   . GLN A 292 ? 0.9446 0.9356 0.9786 0.0271  -0.1305 -0.0688 1509 GLN A OE1   
2274 N  NE2   . GLN A 292 ? 0.9225 0.9221 0.9885 0.0220  -0.1279 -0.0655 1509 GLN A NE2   
2275 N  N     . VAL A 293 ? 0.7316 0.7041 0.7184 0.0515  -0.0920 -0.0659 1510 VAL A N     
2276 C  CA    . VAL A 293 ? 0.9583 0.9168 0.9207 0.0565  -0.0864 -0.0709 1510 VAL A CA    
2277 C  C     . VAL A 293 ? 0.9635 0.9282 0.9205 0.0615  -0.0768 -0.0640 1510 VAL A C     
2278 O  O     . VAL A 293 ? 0.8876 0.8598 0.8441 0.0595  -0.0804 -0.0588 1510 VAL A O     
2279 C  CB    . VAL A 293 ? 1.0028 0.9499 0.9440 0.0532  -0.0972 -0.0783 1510 VAL A CB    
2280 C  CG1   . VAL A 293 ? 1.1636 1.0934 1.0765 0.0583  -0.0911 -0.0850 1510 VAL A CG1   
2281 C  CG2   . VAL A 293 ? 0.9496 0.8939 0.9017 0.0467  -0.1076 -0.0840 1510 VAL A CG2   
2282 N  N     . VAL A 294 ? 1.0823 1.0427 1.0348 0.0680  -0.0642 -0.0639 1511 VAL A N     
2283 C  CA    . VAL A 294 ? 1.0932 1.0585 1.0403 0.0727  -0.0534 -0.0576 1511 VAL A CA    
2284 C  C     . VAL A 294 ? 1.1152 1.0634 1.0324 0.0783  -0.0461 -0.0634 1511 VAL A C     
2285 O  O     . VAL A 294 ? 1.1344 1.0702 1.0444 0.0816  -0.0420 -0.0705 1511 VAL A O     
2286 C  CB    . VAL A 294 ? 1.0391 1.0181 1.0110 0.0758  -0.0431 -0.0508 1511 VAL A CB    
2287 C  CG1   . VAL A 294 ? 0.9469 0.9191 0.9231 0.0809  -0.0365 -0.0550 1511 VAL A CG1   
2288 C  CG2   . VAL A 294 ? 1.0705 1.0555 1.0396 0.0796  -0.0318 -0.0439 1511 VAL A CG2   
2289 N  N     . ILE A 295 ? 1.1053 1.0513 1.0034 0.0792  -0.0447 -0.0605 1512 ILE A N     
2290 C  CA    . ILE A 295 ? 1.1458 1.0750 1.0112 0.0845  -0.0375 -0.0653 1512 ILE A CA    
2291 C  C     . ILE A 295 ? 1.1767 1.1111 1.0458 0.0912  -0.0191 -0.0584 1512 ILE A C     
2292 O  O     . ILE A 295 ? 1.2302 1.1764 1.1075 0.0905  -0.0155 -0.0490 1512 ILE A O     
2293 C  CB    . ILE A 295 ? 1.1299 1.0526 0.9694 0.0819  -0.0474 -0.0655 1512 ILE A CB    
2294 C  CG1   . ILE A 295 ? 1.1248 1.0460 0.9665 0.0748  -0.0664 -0.0714 1512 ILE A CG1   
2295 C  CG2   . ILE A 295 ? 0.9896 0.8937 0.7913 0.0877  -0.0391 -0.0702 1512 ILE A CG2   
2296 C  CD1   . ILE A 295 ? 1.1056 1.0220 0.9239 0.0725  -0.0781 -0.0712 1512 ILE A CD1   
2297 N  N     . VAL A 296 ? 0.9972 0.9228 0.8616 0.0978  -0.0068 -0.0629 1513 VAL A N     
2298 C  CA    . VAL A 296 ? 0.8704 0.7995 0.7367 0.1051  0.0123  -0.0572 1513 VAL A CA    
2299 C  C     . VAL A 296 ? 0.9010 0.8097 0.7270 0.1101  0.0203  -0.0626 1513 VAL A C     
2300 O  O     . VAL A 296 ? 0.9202 0.8106 0.7264 0.1125  0.0198  -0.0733 1513 VAL A O     
2301 C  CB    . VAL A 296 ? 0.8674 0.8014 0.7575 0.1104  0.0223  -0.0576 1513 VAL A CB    
2302 C  CG1   . VAL A 296 ? 0.7792 0.7165 0.6705 0.1185  0.0428  -0.0522 1513 VAL A CG1   
2303 C  CG2   . VAL A 296 ? 0.6896 0.6436 0.6174 0.1056  0.0143  -0.0518 1513 VAL A CG2   
2304 N  N     . PRO A 297 ? 1.0851 0.9948 0.8966 0.1117  0.0276  -0.0558 1514 PRO A N     
2305 C  CA    . PRO A 297 ? 1.1898 1.0792 0.9609 0.1175  0.0377  -0.0604 1514 PRO A CA    
2306 C  C     . PRO A 297 ? 1.1724 1.0580 0.9475 0.1265  0.0587  -0.0619 1514 PRO A C     
2307 O  O     . PRO A 297 ? 1.2205 1.1232 1.0248 0.1292  0.0709  -0.0531 1514 PRO A O     
2308 C  CB    . PRO A 297 ? 1.2213 1.1155 0.9812 0.1166  0.0408  -0.0501 1514 PRO A CB    
2309 C  CG    . PRO A 297 ? 1.1636 1.0823 0.9646 0.1119  0.0384  -0.0395 1514 PRO A CG    
2310 C  CD    . PRO A 297 ? 1.0829 1.0090 0.9091 0.1071  0.0243  -0.0444 1514 PRO A CD    
2311 N  N     . CYS A 298 ? 1.2669 1.1303 1.0141 0.1310  0.0625  -0.0734 1515 CYS A N     
2312 C  CA    . CYS A 298 ? 1.2866 1.1429 1.0362 0.1404  0.0818  -0.0768 1515 CYS A CA    
2313 C  C     . CYS A 298 ? 1.3481 1.1829 1.0543 0.1471  0.0966  -0.0811 1515 CYS A C     
2314 O  O     . CYS A 298 ? 1.4015 1.2247 1.0726 0.1442  0.0893  -0.0828 1515 CYS A O     
2315 C  CB    . CYS A 298 ? 1.2798 1.1264 1.0371 0.1407  0.0756  -0.0874 1515 CYS A CB    
2316 S  SG    . CYS A 298 ? 1.4195 1.2345 1.1313 0.1377  0.0631  -0.1044 1515 CYS A SG    
2317 N  N     . GLY A 299 ? 1.3217 1.1516 1.0305 0.1568  0.1180  -0.0822 1516 GLY A N     
2318 C  CA    . GLY A 299 ? 1.3008 1.1090 0.9687 0.1644  0.1353  -0.0869 1516 GLY A CA    
2319 C  C     . GLY A 299 ? 1.2970 1.1157 0.9637 0.1672  0.1509  -0.0743 1516 GLY A C     
2320 O  O     . GLY A 299 ? 1.3538 1.1547 0.9828 0.1731  0.1657  -0.0764 1516 GLY A O     
2321 N  N     . ILE A 300 ? 1.2852 1.1312 0.9906 0.1625  0.1477  -0.0614 1517 ILE A N     
2322 C  CA    . ILE A 300 ? 1.3311 1.1904 1.0448 0.1641  0.1630  -0.0479 1517 ILE A CA    
2323 C  C     . ILE A 300 ? 1.4072 1.2762 1.1475 0.1732  0.1877  -0.0438 1517 ILE A C     
2324 O  O     . ILE A 300 ? 0.9435 0.8311 0.7272 0.1734  0.1863  -0.0413 1517 ILE A O     
2325 C  CB    . ILE A 300 ? 1.2726 1.1563 1.0187 0.1547  0.1488  -0.0369 1517 ILE A CB    
2326 C  CG1   . ILE A 300 ? 1.0664 0.9408 0.7866 0.1467  0.1258  -0.0402 1517 ILE A CG1   
2327 C  CG2   . ILE A 300 ? 1.3784 1.2765 1.1386 0.1557  0.1659  -0.0230 1517 ILE A CG2   
2328 C  CD1   . ILE A 300 ? 0.9553 0.8514 0.7093 0.1377  0.1095  -0.0325 1517 ILE A CD1   
2329 N  N     . THR A 301 ? 1.4888 1.3454 1.2033 0.1811  0.2102  -0.0427 1518 THR A N     
2330 C  CA    . THR A 301 ? 1.5342 1.3991 1.2723 0.1908  0.2361  -0.0387 1518 THR A CA    
2331 C  C     . THR A 301 ? 1.5377 1.4271 1.3054 0.1884  0.2471  -0.0225 1518 THR A C     
2332 O  O     . THR A 301 ? 1.4996 1.3953 1.2640 0.1799  0.2359  -0.0154 1518 THR A O     
2333 C  CB    . THR A 301 ? 1.0760 0.9129 0.7701 0.2012  0.2569  -0.0469 1518 THR A CB    
2334 N  N     . ALA A 302 ? 1.6614 1.5648 1.4598 0.1958  0.2695  -0.0164 1519 ALA A N     
2335 C  CA    . ALA A 302 ? 1.7370 1.6626 1.5632 0.1933  0.2822  -0.0013 1519 ALA A CA    
2336 C  C     . ALA A 302 ? 1.7200 1.6296 1.5033 0.1923  0.2913  0.0031  1519 ALA A C     
2337 O  O     . ALA A 302 ? 1.7596 1.6837 1.5581 0.1863  0.2935  0.0154  1519 ALA A O     
2338 C  CB    . ALA A 302 ? 1.8317 1.7732 1.6947 0.2026  0.3070  0.0039  1519 ALA A CB    
2339 N  N     . THR A 303 ? 1.5797 1.4585 1.3081 0.1978  0.2958  -0.0067 1520 THR A N     
2340 C  CA    . THR A 303 ? 1.4731 1.3339 1.1546 0.1977  0.3037  -0.0027 1520 THR A CA    
2341 C  C     . THR A 303 ? 1.4926 1.3293 1.1241 0.1932  0.2807  -0.0124 1520 THR A C     
2342 O  O     . THR A 303 ? 1.4920 1.3038 1.0704 0.1968  0.2877  -0.0154 1520 THR A O     
2343 C  CB    . THR A 303 ? 1.5426 1.3883 1.1996 0.2094  0.3356  -0.0032 1520 THR A CB    
2344 O  OG1   . THR A 303 ? 1.7625 1.5839 1.3616 0.2097  0.3395  -0.0024 1520 THR A OG1   
2345 C  CG2   . THR A 303 ? 1.4464 1.2763 1.0932 0.2185  0.3410  -0.0180 1520 THR A CG2   
2346 N  N     . THR A 304 ? 1.4969 1.3403 1.1440 0.1856  0.2534  -0.0177 1521 THR A N     
2347 C  CA    . THR A 304 ? 1.4341 1.2633 1.0453 0.1788  0.2295  -0.0220 1521 THR A CA    
2348 C  C     . THR A 304 ? 1.5339 1.3705 1.1416 0.1736  0.2294  -0.0075 1521 THR A C     
2349 O  O     . THR A 304 ? 1.4969 1.3579 1.1483 0.1695  0.2327  0.0042  1521 THR A O     
2350 C  CB    . THR A 304 ? 1.2014 1.0405 0.8382 0.1713  0.2023  -0.0285 1521 THR A CB    
2351 N  N     . THR A 305 ? 1.6103 1.4249 1.1652 0.1740  0.2261  -0.0081 1522 THR A N     
2352 C  CA    . THR A 305 ? 1.5559 1.3725 1.0997 0.1707  0.2281  0.0062  1522 THR A CA    
2353 C  C     . THR A 305 ? 1.6142 1.4421 1.1734 0.1608  0.2007  0.0104  1522 THR A C     
2354 O  O     . THR A 305 ? 1.5555 1.3813 1.1135 0.1567  0.1773  0.0004  1522 THR A O     
2355 C  CB    . THR A 305 ? 1.4369 1.2243 0.9150 0.1761  0.2357  0.0049  1522 THR A CB    
2356 N  N     . ASP A 306 ? 1.6922 1.5314 1.2664 0.1568  0.2048  0.0255  1523 ASP A N     
2357 C  CA    . ASP A 306 ? 1.6325 1.4827 1.2240 0.1480  0.1819  0.0311  1523 ASP A CA    
2358 C  C     . ASP A 306 ? 1.6614 1.4931 1.2090 0.1468  0.1594  0.0249  1523 ASP A C     
2359 O  O     . ASP A 306 ? 1.6384 1.4781 1.2015 0.1404  0.1358  0.0227  1523 ASP A O     
2360 C  CB    . ASP A 306 ? 1.6852 1.5451 1.2922 0.1451  0.1932  0.0484  1523 ASP A CB    
2361 C  CG    . ASP A 306 ? 1.7516 1.6346 1.4110 0.1438  0.2105  0.0545  1523 ASP A CG    
2362 O  OD1   . ASP A 306 ? 1.7695 1.6634 1.4568 0.1447  0.2096  0.0459  1523 ASP A OD1   
2363 O  OD2   . ASP A 306 ? 1.7436 1.6337 1.4167 0.1418  0.2247  0.0682  1523 ASP A OD2   
2364 N  N     . ASP A 307 ? 1.7409 1.5483 1.2336 0.1528  0.1661  0.0224  1524 ASP A N     
2365 C  CA    . ASP A 307 ? 1.7570 1.5477 1.2082 0.1514  0.1427  0.0157  1524 ASP A CA    
2366 C  C     . ASP A 307 ? 1.6975 1.4839 1.1483 0.1502  0.1268  -0.0022 1524 ASP A C     
2367 O  O     . ASP A 307 ? 1.6351 1.4236 1.0875 0.1446  0.1010  -0.0070 1524 ASP A O     
2368 C  CB    . ASP A 307 ? 1.8463 1.6113 1.2357 0.1579  0.1527  0.0182  1524 ASP A CB    
2369 C  CG    . ASP A 307 ? 1.7995 1.5553 1.1570 0.1550  0.1297  0.0223  1524 ASP A CG    
2370 O  OD1   . ASP A 307 ? 1.6656 1.4379 1.0553 0.1486  0.1120  0.0280  1524 ASP A OD1   
2371 O  OD2   . ASP A 307 ? 1.8336 1.5661 1.1344 0.1595  0.1286  0.0195  1524 ASP A OD2   
2372 N  N     . GLU A 308 ? 1.6595 1.4393 1.1087 0.1556  0.1426  -0.0120 1525 GLU A N     
2373 C  CA    . GLU A 308 ? 1.6078 1.3853 1.0657 0.1541  0.1296  -0.0281 1525 GLU A CA    
2374 C  C     . GLU A 308 ? 1.4884 1.2914 1.0030 0.1469  0.1154  -0.0264 1525 GLU A C     
2375 O  O     . GLU A 308 ? 1.5291 1.3324 1.0482 0.1416  0.0928  -0.0352 1525 GLU A O     
2376 C  CB    . GLU A 308 ? 1.6409 1.4086 1.0942 0.1620  0.1518  -0.0369 1525 GLU A CB    
2377 C  CG    . GLU A 308 ? 1.8210 1.5709 1.2340 0.1704  0.1768  -0.0334 1525 GLU A CG    
2378 C  CD    . GLU A 308 ? 1.9653 1.7103 1.3851 0.1787  0.2014  -0.0402 1525 GLU A CD    
2379 O  OE1   . GLU A 308 ? 1.9834 1.7497 1.4510 0.1800  0.2159  -0.0326 1525 GLU A OE1   
2380 O  OE2   . GLU A 308 ? 2.0662 1.7856 1.4437 0.1839  0.2059  -0.0533 1525 GLU A OE2   
2381 N  N     . ARG A 309 ? 1.2786 1.1029 0.8366 0.1463  0.1285  -0.0154 1526 ARG A N     
2382 C  CA    . ARG A 309 ? 1.1458 0.9935 0.7552 0.1396  0.1157  -0.0138 1526 ARG A CA    
2383 C  C     . ARG A 309 ? 1.3523 1.2042 0.9617 0.1320  0.0914  -0.0106 1526 ARG A C     
2384 O  O     . ARG A 309 ? 1.2819 1.1413 0.9115 0.1267  0.0727  -0.0168 1526 ARG A O     
2385 C  CB    . ARG A 309 ? 1.0062 0.8757 0.6594 0.1394  0.1327  -0.0019 1526 ARG A CB    
2386 C  CG    . ARG A 309 ? 1.0793 0.9718 0.7830 0.1326  0.1193  -0.0015 1526 ARG A CG    
2387 C  CD    . ARG A 309 ? 1.2045 1.1146 0.9494 0.1351  0.1359  0.0018  1526 ARG A CD    
2388 N  NE    . ARG A 309 ? 1.3874 1.3070 1.1445 0.1355  0.1539  0.0152  1526 ARG A NE    
2389 C  CZ    . ARG A 309 ? 1.4739 1.4120 1.2698 0.1367  0.1693  0.0211  1526 ARG A CZ    
2390 N  NH1   . ARG A 309 ? 1.4327 1.3816 1.2578 0.1384  0.1683  0.0151  1526 ARG A NH1   
2391 N  NH2   . ARG A 309 ? 1.5181 1.4642 1.3244 0.1360  0.1854  0.0334  1526 ARG A NH2   
2392 N  N     . ARG A 310 ? 1.4888 1.3354 1.0755 0.1320  0.0920  -0.0004 1527 ARG A N     
2393 C  CA    . ARG A 310 ? 1.4062 1.2565 0.9930 0.1261  0.0701  0.0042  1527 ARG A CA    
2394 C  C     . ARG A 310 ? 1.4181 1.2547 0.9752 0.1248  0.0482  -0.0080 1527 ARG A C     
2395 O  O     . ARG A 310 ? 1.3332 1.1789 0.9092 0.1188  0.0274  -0.0104 1527 ARG A O     
2396 C  CB    . ARG A 310 ? 1.4148 1.2599 0.9811 0.1277  0.0776  0.0185  1527 ARG A CB    
2397 N  N     . ARG A 311 ? 1.4596 1.2743 0.9714 0.1299  0.0529  -0.0166 1528 ARG A N     
2398 C  CA    . ARG A 311 ? 1.5321 1.3329 1.0148 0.1279  0.0317  -0.0294 1528 ARG A CA    
2399 C  C     . ARG A 311 ? 1.5498 1.3597 1.0655 0.1230  0.0199  -0.0408 1528 ARG A C     
2400 O  O     . ARG A 311 ? 1.5048 1.3185 1.0269 0.1170  -0.0033 -0.0453 1528 ARG A O     
2401 C  CB    . ARG A 311 ? 1.4779 1.2523 0.9064 0.1344  0.0419  -0.0378 1528 ARG A CB    
2402 N  N     . LEU A 312 ? 1.5222 1.3367 1.0613 0.1257  0.0361  -0.0445 1529 LEU A N     
2403 C  CA    . LEU A 312 ? 1.4603 1.2829 1.0313 0.1217  0.0268  -0.0537 1529 LEU A CA    
2404 C  C     . LEU A 312 ? 1.2880 1.1343 0.9038 0.1148  0.0142  -0.0460 1529 LEU A C     
2405 O  O     . LEU A 312 ? 1.2290 1.0791 0.8571 0.1090  -0.0049 -0.0522 1529 LEU A O     
2406 C  CB    . LEU A 312 ? 1.4048 1.2274 0.9914 0.1274  0.0477  -0.0576 1529 LEU A CB    
2407 C  CG    . LEU A 312 ? 1.3138 1.1463 0.9377 0.1242  0.0407  -0.0645 1529 LEU A CG    
2408 C  CD1   . LEU A 312 ? 0.9878 0.8030 0.5902 0.1214  0.0250  -0.0800 1529 LEU A CD1   
2409 C  CD2   . LEU A 312 ? 1.3154 1.1535 0.9622 0.1305  0.0625  -0.0633 1529 LEU A CD2   
2410 N  N     . TYR A 313 ? 1.2359 1.0976 0.8765 0.1151  0.0252  -0.0328 1530 TYR A N     
2411 C  CA    . TYR A 313 ? 1.3676 1.2498 1.0473 0.1086  0.0143  -0.0255 1530 TYR A CA    
2412 C  C     . TYR A 313 ? 1.4558 1.3361 1.1241 0.1038  -0.0084 -0.0258 1530 TYR A C     
2413 O  O     . TYR A 313 ? 1.3297 1.2222 1.0258 0.0980  -0.0229 -0.0269 1530 TYR A O     
2414 C  CB    . TYR A 313 ? 1.4924 1.3865 1.1897 0.1093  0.0288  -0.0110 1530 TYR A CB    
2415 C  CG    . TYR A 313 ? 1.5545 1.4625 1.2865 0.1107  0.0459  -0.0082 1530 TYR A CG    
2416 C  CD1   . TYR A 313 ? 1.5157 1.4398 1.2770 0.1083  0.0541  0.0038  1530 TYR A CD1   
2417 C  CD2   . TYR A 313 ? 1.5258 1.4307 1.2621 0.1146  0.0536  -0.0173 1530 TYR A CD2   
2418 C  CE1   . TYR A 313 ? 1.4334 1.3719 1.2279 0.1092  0.0683  0.0065  1530 TYR A CE1   
2419 C  CE2   . TYR A 313 ? 1.4429 1.3621 1.2127 0.1166  0.0683  -0.0138 1530 TYR A CE2   
2420 C  CZ    . TYR A 313 ? 1.3813 1.3181 1.1803 0.1136  0.0750  -0.0020 1530 TYR A CZ    
2421 O  OH    . TYR A 313 ? 1.3351 1.2877 1.1690 0.1152  0.0882  0.0014  1530 TYR A OH    
2422 N  N     . GLU A 314 ? 1.5729 1.4380 1.1997 0.1065  -0.0117 -0.0245 1531 GLU A N     
2423 C  CA    . GLU A 314 ? 1.5439 1.4084 1.1600 0.1029  -0.0333 -0.0227 1531 GLU A CA    
2424 C  C     . GLU A 314 ? 1.5137 1.3738 1.1261 0.0988  -0.0524 -0.0365 1531 GLU A C     
2425 O  O     . GLU A 314 ? 1.5373 1.4081 1.1707 0.0933  -0.0701 -0.0365 1531 GLU A O     
2426 C  CB    . GLU A 314 ? 1.5784 1.4275 1.1494 0.1075  -0.0312 -0.0166 1531 GLU A CB    
2427 N  N     . SER A 315 ? 1.5068 1.3511 1.0950 0.1013  -0.0479 -0.0486 1532 SER A N     
2428 C  CA    . SER A 315 ? 1.5757 1.4157 1.1642 0.0964  -0.0654 -0.0621 1532 SER A CA    
2429 C  C     . SER A 315 ? 1.5782 1.4350 1.2147 0.0917  -0.0675 -0.0637 1532 SER A C     
2430 O  O     . SER A 315 ? 1.5719 1.4337 1.2229 0.0855  -0.0853 -0.0692 1532 SER A O     
2431 C  CB    . SER A 315 ? 1.5614 1.3790 1.1148 0.0997  -0.0592 -0.0756 1532 SER A CB    
2432 O  OG    . SER A 315 ? 1.5550 1.3651 1.0989 0.0941  -0.0797 -0.0881 1532 SER A OG    
2433 N  N     . CYS A 316 ? 1.4748 1.3411 1.1368 0.0943  -0.0498 -0.0583 1533 CYS A N     
2434 C  CA    . CYS A 316 ? 1.3690 1.2513 1.0747 0.0903  -0.0515 -0.0587 1533 CYS A CA    
2435 C  C     . CYS A 316 ? 1.2228 1.1219 0.9546 0.0847  -0.0647 -0.0508 1533 CYS A C     
2436 O  O     . CYS A 316 ? 1.1584 1.0661 0.9154 0.0794  -0.0757 -0.0545 1533 CYS A O     
2437 C  CB    . CYS A 316 ? 1.3596 1.2493 1.0856 0.0947  -0.0304 -0.0537 1533 CYS A CB    
2438 S  SG    . CYS A 316 ? 1.4923 1.3653 1.2027 0.1007  -0.0169 -0.0655 1533 CYS A SG    
2439 N  N     . ARG A 317 ? 1.2219 1.1246 0.9474 0.0860  -0.0630 -0.0397 1534 ARG A N     
2440 C  CA    . ARG A 317 ? 1.2207 1.1377 0.9700 0.0814  -0.0749 -0.0323 1534 ARG A CA    
2441 C  C     . ARG A 317 ? 1.1557 1.0694 0.8949 0.0777  -0.0965 -0.0380 1534 ARG A C     
2442 O  O     . ARG A 317 ? 1.0661 0.9918 0.8325 0.0728  -0.1082 -0.0376 1534 ARG A O     
2443 C  CB    . ARG A 317 ? 1.1408 1.0604 0.8851 0.0840  -0.0673 -0.0188 1534 ARG A CB    
2444 C  CG    . ARG A 317 ? 1.1153 1.0439 0.8821 0.0853  -0.0484 -0.0119 1534 ARG A CG    
2445 C  CD    . ARG A 317 ? 1.1224 1.0541 0.8894 0.0862  -0.0424 0.0016  1534 ARG A CD    
2446 N  NE    . ARG A 317 ? 1.0826 1.0273 0.8813 0.0847  -0.0286 0.0080  1534 ARG A NE    
2447 C  CZ    . ARG A 317 ? 1.1907 1.1342 0.9867 0.0882  -0.0096 0.0120  1534 ARG A CZ    
2448 N  NH1   . ARG A 317 ? 1.3064 1.2349 1.0674 0.0940  -0.0010 0.0101  1534 ARG A NH1   
2449 N  NH2   . ARG A 317 ? 1.2142 1.1713 1.0422 0.0859  0.0009  0.0177  1534 ARG A NH2   
2450 N  N     . GLU A 318 ? 1.1395 1.0369 0.8407 0.0798  -0.1020 -0.0445 1535 GLU A N     
2451 C  CA    . GLU A 318 ? 1.1556 1.0510 0.8483 0.0757  -0.1240 -0.0503 1535 GLU A CA    
2452 C  C     . GLU A 318 ? 1.2828 1.1811 0.9965 0.0700  -0.1321 -0.0617 1535 GLU A C     
2453 O  O     . GLU A 318 ? 1.2653 1.1729 0.9978 0.0646  -0.1483 -0.0629 1535 GLU A O     
2454 C  CB    . GLU A 318 ? 1.2095 1.0856 0.8534 0.0789  -0.1284 -0.0552 1535 GLU A CB    
2455 C  CG    . GLU A 318 ? 1.3105 1.1849 0.9432 0.0746  -0.1526 -0.0608 1535 GLU A CG    
2456 C  CD    . GLU A 318 ? 1.6615 1.5146 1.2456 0.0766  -0.1568 -0.0701 1535 GLU A CD    
2457 O  OE1   . GLU A 318 ? 1.7935 1.6432 1.3673 0.0720  -0.1770 -0.0783 1535 GLU A OE1   
2458 O  OE2   . GLU A 318 ? 1.7782 1.6177 1.3345 0.0826  -0.1396 -0.0696 1535 GLU A OE2   
2459 N  N     . LEU A 319 ? 1.3471 1.2378 1.0606 0.0714  -0.1197 -0.0694 1536 LEU A N     
2460 C  CA    . LEU A 319 ? 1.2474 1.1401 0.9829 0.0662  -0.1253 -0.0789 1536 LEU A CA    
2461 C  C     . LEU A 319 ? 1.1569 1.0694 0.9360 0.0627  -0.1254 -0.0721 1536 LEU A C     
2462 O  O     . LEU A 319 ? 1.1005 1.0199 0.9000 0.0568  -0.1379 -0.0757 1536 LEU A O     
2463 C  CB    . LEU A 319 ? 1.2953 1.1747 1.0215 0.0695  -0.1111 -0.0874 1536 LEU A CB    
2464 C  CG    . LEU A 319 ? 1.3193 1.1969 1.0640 0.0643  -0.1173 -0.0977 1536 LEU A CG    
2465 C  CD1   . LEU A 319 ? 1.3903 1.2620 1.1237 0.0577  -0.1380 -0.1063 1536 LEU A CD1   
2466 C  CD2   . LEU A 319 ? 1.3492 1.2119 1.0834 0.0687  -0.1028 -0.1056 1536 LEU A CD2   
2467 N  N     . GLU A 320 ? 1.0714 0.9930 0.8646 0.0661  -0.1115 -0.0623 1537 GLU A N     
2468 C  CA    . GLU A 320 ? 1.0850 1.0243 0.9162 0.0629  -0.1113 -0.0558 1537 GLU A CA    
2469 C  C     . GLU A 320 ? 1.1766 1.1251 1.0184 0.0588  -0.1269 -0.0517 1537 GLU A C     
2470 O  O     . GLU A 320 ? 1.0767 1.0354 0.9458 0.0540  -0.1338 -0.0527 1537 GLU A O     
2471 C  CB    . GLU A 320 ? 1.1481 1.0943 0.9881 0.0667  -0.0951 -0.0459 1537 GLU A CB    
2472 C  CG    . GLU A 320 ? 1.1474 1.1103 1.0187 0.0637  -0.0957 -0.0371 1537 GLU A CG    
2473 C  CD    . GLU A 320 ? 1.1895 1.1577 1.0675 0.0668  -0.0797 -0.0284 1537 GLU A CD    
2474 O  OE1   . GLU A 320 ? 1.1811 1.1621 1.0872 0.0641  -0.0768 -0.0234 1537 GLU A OE1   
2475 O  OE2   . GLU A 320 ? 1.1990 1.1581 1.0538 0.0717  -0.0697 -0.0268 1537 GLU A OE2   
2476 N  N     . GLN A 321 ? 1.3195 1.2636 1.1388 0.0610  -0.1328 -0.0472 1538 GLN A N     
2477 C  CA    . GLN A 321 ? 1.3250 1.2782 1.1551 0.0585  -0.1473 -0.0420 1538 GLN A CA    
2478 C  C     . GLN A 321 ? 1.1947 1.1483 1.0291 0.0532  -0.1646 -0.0509 1538 GLN A C     
2479 O  O     . GLN A 321 ? 1.1691 1.1353 1.0314 0.0493  -0.1730 -0.0491 1538 GLN A O     
2480 C  CB    . GLN A 321 ? 1.4287 1.3763 1.2323 0.0631  -0.1491 -0.0338 1538 GLN A CB    
2481 C  CG    . GLN A 321 ? 1.4474 1.3994 1.2581 0.0665  -0.1344 -0.0220 1538 GLN A CG    
2482 C  CD    . GLN A 321 ? 1.4134 1.3798 1.2635 0.0630  -0.1296 -0.0193 1538 GLN A CD    
2483 O  OE1   . GLN A 321 ? 1.3758 1.3518 1.2479 0.0595  -0.1402 -0.0184 1538 GLN A OE1   
2484 N  NE2   . GLN A 321 ? 1.3828 1.3510 1.2422 0.0639  -0.1137 -0.0182 1538 GLN A NE2   
2485 N  N     . THR A 322 ? 1.1891 1.1290 0.9977 0.0528  -0.1693 -0.0611 1539 THR A N     
2486 C  CA    . THR A 322 ? 1.2101 1.1508 1.0255 0.0466  -0.1862 -0.0700 1539 THR A CA    
2487 C  C     . THR A 322 ? 1.1827 1.1289 1.0286 0.0417  -0.1827 -0.0753 1539 THR A C     
2488 O  O     . THR A 322 ? 1.2436 1.1959 1.1074 0.0357  -0.1950 -0.0797 1539 THR A O     
2489 C  CB    . THR A 322 ? 1.2092 1.1326 0.9879 0.0463  -0.1942 -0.0803 1539 THR A CB    
2490 O  OG1   . THR A 322 ? 1.3850 1.3092 1.1758 0.0389  -0.2085 -0.0903 1539 THR A OG1   
2491 C  CG2   . THR A 322 ? 1.2803 1.1875 1.0359 0.0504  -0.1781 -0.0860 1539 THR A CG2   
2492 N  N     . PHE A 323 ? 1.1809 1.1264 1.0350 0.0443  -0.1660 -0.0741 1540 PHE A N     
2493 C  CA    . PHE A 323 ? 1.2141 1.1669 1.0991 0.0404  -0.1626 -0.0761 1540 PHE A CA    
2494 C  C     . PHE A 323 ? 1.2017 1.1722 1.1176 0.0383  -0.1646 -0.0673 1540 PHE A C     
2495 O  O     . PHE A 323 ? 1.1766 1.1544 1.1164 0.0331  -0.1703 -0.0695 1540 PHE A O     
2496 C  CB    . PHE A 323 ? 1.2456 1.1930 1.1301 0.0443  -0.1453 -0.0768 1540 PHE A CB    
2497 C  CG    . PHE A 323 ? 1.2587 1.1891 1.1245 0.0447  -0.1433 -0.0880 1540 PHE A CG    
2498 C  CD1   . PHE A 323 ? 1.2996 1.2238 1.1654 0.0387  -0.1557 -0.0975 1540 PHE A CD1   
2499 C  CD2   . PHE A 323 ? 1.2825 1.2026 1.1315 0.0509  -0.1285 -0.0891 1540 PHE A CD2   
2500 C  CE1   . PHE A 323 ? 1.3544 1.2606 1.2023 0.0386  -0.1536 -0.1086 1540 PHE A CE1   
2501 C  CE2   . PHE A 323 ? 1.3242 1.2268 1.1554 0.0519  -0.1257 -0.0999 1540 PHE A CE2   
2502 C  CZ    . PHE A 323 ? 1.3505 1.2453 1.1804 0.0456  -0.1383 -0.1099 1540 PHE A CZ    
2503 N  N     . VAL A 324 ? 1.2052 1.1817 1.1213 0.0422  -0.1586 -0.0574 1541 VAL A N     
2504 C  CA    . VAL A 324 ? 1.1412 1.1324 1.0847 0.0404  -0.1604 -0.0497 1541 VAL A CA    
2505 C  C     . VAL A 324 ? 1.1186 1.1156 1.0704 0.0369  -0.1769 -0.0506 1541 VAL A C     
2506 O  O     . VAL A 324 ? 1.0283 1.0354 1.0073 0.0329  -0.1805 -0.0505 1541 VAL A O     
2507 C  CB    . VAL A 324 ? 1.1401 1.1345 1.0805 0.0449  -0.1519 -0.0392 1541 VAL A CB    
2508 C  CG1   . VAL A 324 ? 1.0720 1.0792 1.0427 0.0427  -0.1492 -0.0333 1541 VAL A CG1   
2509 C  CG2   . VAL A 324 ? 1.1065 1.0943 1.0337 0.0488  -0.1369 -0.0384 1541 VAL A CG2   
2510 N  N     . LYS A 325 ? 1.1907 1.1821 1.1195 0.0387  -0.1870 -0.0509 1542 LYS A N     
2511 C  CA    . LYS A 325 ? 1.2559 1.2543 1.1929 0.0359  -0.2043 -0.0511 1542 LYS A CA    
2512 C  C     . LYS A 325 ? 1.3657 1.3647 1.3154 0.0290  -0.2131 -0.0613 1542 LYS A C     
2513 O  O     . LYS A 325 ? 1.4438 1.4535 1.4141 0.0253  -0.2248 -0.0610 1542 LYS A O     
2514 C  CB    . LYS A 325 ? 1.2609 1.2520 1.1667 0.0395  -0.2141 -0.0493 1542 LYS A CB    
2515 N  N     . ALA A 326 ? 1.3424 1.3303 1.2822 0.0273  -0.2068 -0.0699 1543 ALA A N     
2516 C  CA    . ALA A 326 ? 1.3285 1.3161 1.2840 0.0204  -0.2119 -0.0788 1543 ALA A CA    
2517 C  C     . ALA A 326 ? 1.2608 1.2585 1.2491 0.0180  -0.2034 -0.0757 1543 ALA A C     
2518 O  O     . ALA A 326 ? 1.2450 1.2426 1.2486 0.0123  -0.2055 -0.0816 1543 ALA A O     
2519 C  CB    . ALA A 326 ? 1.3649 1.3347 1.2974 0.0200  -0.2075 -0.0891 1543 ALA A CB    
2520 N  N     . GLY A 327 ? 1.1699 1.1755 1.1681 0.0219  -0.1939 -0.0665 1544 GLY A N     
2521 C  CA    . GLY A 327 ? 1.1556 1.1703 1.1812 0.0202  -0.1857 -0.0630 1544 GLY A CA    
2522 C  C     . GLY A 327 ? 1.1262 1.1352 1.1515 0.0212  -0.1722 -0.0646 1544 GLY A C     
2523 O  O     . GLY A 327 ? 1.1770 1.1931 1.2227 0.0199  -0.1656 -0.0614 1544 GLY A O     
2524 N  N     . ILE A 328 ? 1.0518 1.0482 1.0545 0.0240  -0.1674 -0.0691 1545 ILE A N     
2525 C  CA    . ILE A 328 ? 1.0826 1.0743 1.0862 0.0261  -0.1545 -0.0699 1545 ILE A CA    
2526 C  C     . ILE A 328 ? 0.9745 0.9686 0.9711 0.0319  -0.1438 -0.0627 1545 ILE A C     
2527 O  O     . ILE A 328 ? 0.9896 0.9804 0.9673 0.0354  -0.1443 -0.0604 1545 ILE A O     
2528 C  CB    . ILE A 328 ? 1.1746 1.1506 1.1616 0.0260  -0.1537 -0.0794 1545 ILE A CB    
2529 C  CG1   . ILE A 328 ? 1.2239 1.1889 1.1801 0.0290  -0.1574 -0.0832 1545 ILE A CG1   
2530 C  CG2   . ILE A 328 ? 1.1501 1.1240 1.1499 0.0190  -0.1624 -0.0862 1545 ILE A CG2   
2531 C  CD1   . ILE A 328 ? 1.1899 1.1386 1.1304 0.0269  -0.1606 -0.0946 1545 ILE A CD1   
2532 N  N     . ARG A 329 ? 0.7752 0.7752 0.7872 0.0326  -0.1342 -0.0589 1546 ARG A N     
2533 C  CA    . ARG A 329 ? 0.9538 0.9589 0.9662 0.0366  -0.1241 -0.0518 1546 ARG A CA    
2534 C  C     . ARG A 329 ? 1.1397 1.1358 1.1340 0.0419  -0.1148 -0.0534 1546 ARG A C     
2535 O  O     . ARG A 329 ? 1.2331 1.2277 1.2328 0.0436  -0.1073 -0.0549 1546 ARG A O     
2536 C  CB    . ARG A 329 ? 0.9345 0.9490 0.9698 0.0347  -0.1190 -0.0482 1546 ARG A CB    
2537 C  CG    . ARG A 329 ? 0.7905 0.8120 0.8433 0.0298  -0.1261 -0.0477 1546 ARG A CG    
2538 C  CD    . ARG A 329 ? 0.7955 0.8256 0.8659 0.0286  -0.1201 -0.0432 1546 ARG A CD    
2539 N  NE    . ARG A 329 ? 0.8413 0.8695 0.9186 0.0278  -0.1167 -0.0457 1546 ARG A NE    
2540 C  CZ    . ARG A 329 ? 0.8511 0.8757 0.9341 0.0244  -0.1210 -0.0500 1546 ARG A CZ    
2541 N  NH1   . ARG A 329 ? 0.7892 0.8132 0.8732 0.0213  -0.1294 -0.0528 1546 ARG A NH1   
2542 N  NH2   . ARG A 329 ? 0.8931 0.9150 0.9815 0.0242  -0.1170 -0.0510 1546 ARG A NH2   
2543 N  N     . CYS A 330 ? 1.0827 1.0735 1.0560 0.0452  -0.1141 -0.0521 1547 CYS A N     
2544 C  CA    . CYS A 330 ? 0.9772 0.9589 0.9314 0.0508  -0.1039 -0.0535 1547 CYS A CA    
2545 C  C     . CYS A 330 ? 1.0804 1.0671 1.0312 0.0541  -0.0954 -0.0448 1547 CYS A C     
2546 O  O     . CYS A 330 ? 1.3005 1.2896 1.2468 0.0534  -0.1005 -0.0400 1547 CYS A O     
2547 C  CB    . CYS A 330 ? 0.9884 0.9550 0.9142 0.0518  -0.1096 -0.0610 1547 CYS A CB    
2548 S  SG    . CYS A 330 ? 1.0534 1.0078 0.9494 0.0595  -0.0962 -0.0611 1547 CYS A SG    
2549 N  N     . GLU A 331 ? 0.9833 0.9716 0.9375 0.0580  -0.0822 -0.0424 1548 GLU A N     
2550 C  CA    . GLU A 331 ? 0.8726 0.8641 0.8224 0.0612  -0.0720 -0.0346 1548 GLU A CA    
2551 C  C     . GLU A 331 ? 0.9510 0.9323 0.8814 0.0674  -0.0604 -0.0373 1548 GLU A C     
2552 O  O     . GLU A 331 ? 1.0670 1.0417 0.9953 0.0694  -0.0583 -0.0442 1548 GLU A O     
2553 C  CB    . GLU A 331 ? 0.7847 0.7912 0.7623 0.0593  -0.0662 -0.0277 1548 GLU A CB    
2554 N  N     . GLY A 332 ? 1.0181 0.9965 0.9331 0.0708  -0.0524 -0.0319 1549 GLY A N     
2555 C  CA    . GLY A 332 ? 1.0890 1.0585 0.9861 0.0772  -0.0384 -0.0330 1549 GLY A CA    
2556 C  C     . GLY A 332 ? 1.0557 1.0372 0.9718 0.0792  -0.0238 -0.0246 1549 GLY A C     
2557 O  O     . GLY A 332 ? 1.2174 1.2100 1.1498 0.0756  -0.0245 -0.0168 1549 GLY A O     
2558 N  N     . ASP A 333 ? 0.9790 0.9583 0.8947 0.0847  -0.0106 -0.0263 1550 ASP A N     
2559 C  CA    . ASP A 333 ? 0.9790 0.9708 0.9152 0.0870  0.0039  -0.0187 1550 ASP A CA    
2560 C  C     . ASP A 333 ? 1.0793 1.0615 0.9909 0.0927  0.0183  -0.0158 1550 ASP A C     
2561 O  O     . ASP A 333 ? 1.0948 1.0642 0.9866 0.0987  0.0261  -0.0217 1550 ASP A O     
2562 C  CB    . ASP A 333 ? 1.0760 1.0742 1.0335 0.0899  0.0086  -0.0218 1550 ASP A CB    
2563 C  CG    . ASP A 333 ? 1.1222 1.1377 1.1079 0.0911  0.0205  -0.0137 1550 ASP A CG    
2564 O  OD1   . ASP A 333 ? 1.1084 1.1275 1.0926 0.0914  0.0303  -0.0066 1550 ASP A OD1   
2565 O  OD2   . ASP A 333 ? 1.0950 1.1206 1.1050 0.0917  0.0200  -0.0141 1550 ASP A OD2   
2566 N  N     . TYR A 334 ? 1.0926 1.0790 1.0032 0.0906  0.0219  -0.0069 1551 TYR A N     
2567 C  CA    . TYR A 334 ? 1.0621 1.0393 0.9487 0.0955  0.0362  -0.0023 1551 TYR A CA    
2568 C  C     . TYR A 334 ? 1.0661 1.0571 0.9765 0.0963  0.0531  0.0071  1551 TYR A C     
2569 O  O     . TYR A 334 ? 1.2188 1.2053 1.1153 0.0983  0.0649  0.0141  1551 TYR A O     
2570 C  CB    . TYR A 334 ? 0.9970 0.9650 0.8590 0.0931  0.0277  0.0014  1551 TYR A CB    
2571 C  CG    . TYR A 334 ? 1.0461 1.0056 0.8933 0.0906  0.0081  -0.0067 1551 TYR A CG    
2572 C  CD1   . TYR A 334 ? 1.1352 1.0772 0.9493 0.0943  0.0052  -0.0158 1551 TYR A CD1   
2573 C  CD2   . TYR A 334 ? 0.8665 0.8355 0.7339 0.0841  -0.0072 -0.0058 1551 TYR A CD2   
2574 C  CE1   . TYR A 334 ? 1.1230 1.0586 0.9265 0.0911  -0.0134 -0.0235 1551 TYR A CE1   
2575 C  CE2   . TYR A 334 ? 0.8481 0.8111 0.7056 0.0816  -0.0245 -0.0129 1551 TYR A CE2   
2576 C  CZ    . TYR A 334 ? 1.0042 0.9512 0.8308 0.0847  -0.0279 -0.0216 1551 TYR A CZ    
2577 O  OH    . TYR A 334 ? 1.0849 1.0270 0.9041 0.0813  -0.0456 -0.0288 1551 TYR A OH    
2578 N  N     . ARG A 335 ? 0.9621 0.9695 0.9078 0.0949  0.0546  0.0076  1552 ARG A N     
2579 C  CA    . ARG A 335 ? 0.8910 0.9138 0.8634 0.0949  0.0693  0.0161  1552 ARG A CA    
2580 C  C     . ARG A 335 ? 0.9786 0.9948 0.9378 0.1035  0.0891  0.0163  1552 ARG A C     
2581 O  O     . ARG A 335 ? 1.0312 1.0372 0.9764 0.1097  0.0913  0.0083  1552 ARG A O     
2582 C  CB    . ARG A 335 ? 0.7746 0.8167 0.7864 0.0917  0.0641  0.0158  1552 ARG A CB    
2583 C  CG    . ARG A 335 ? 0.7240 0.7717 0.7478 0.0833  0.0457  0.0151  1552 ARG A CG    
2584 C  CD    . ARG A 335 ? 0.6919 0.7567 0.7499 0.0806  0.0402  0.0143  1552 ARG A CD    
2585 N  NE    . ARG A 335 ? 0.9484 1.0073 1.0014 0.0841  0.0332  0.0061  1552 ARG A NE    
2586 C  CZ    . ARG A 335 ? 1.0157 1.0856 1.0921 0.0828  0.0265  0.0045  1552 ARG A CZ    
2587 N  NH1   . ARG A 335 ? 0.9456 1.0336 1.0513 0.0778  0.0250  0.0101  1552 ARG A NH1   
2588 N  NH2   . ARG A 335 ? 0.9241 0.9859 0.9937 0.0863  0.0211  -0.0025 1552 ARG A NH2   
2589 N  N     . ASP A 336 ? 0.9613 0.9812 0.9229 0.1040  0.1044  0.0254  1553 ASP A N     
2590 C  CA    . ASP A 336 ? 0.9681 0.9794 0.9124 0.1124  0.1251  0.0264  1553 ASP A CA    
2591 C  C     . ASP A 336 ? 0.9300 0.9581 0.9085 0.1166  0.1395  0.0286  1553 ASP A C     
2592 O  O     . ASP A 336 ? 0.8234 0.8444 0.7899 0.1251  0.1571  0.0275  1553 ASP A O     
2593 C  CB    . ASP A 336 ? 1.0977 1.1029 1.0245 0.1116  0.1365  0.0360  1553 ASP A CB    
2594 C  CG    . ASP A 336 ? 1.2351 1.2191 1.1183 0.1115  0.1263  0.0334  1553 ASP A CG    
2595 O  OD1   . ASP A 336 ? 1.2799 1.2627 1.1583 0.1067  0.1227  0.0412  1553 ASP A OD1   
2596 O  OD2   . ASP A 336 ? 1.3206 1.2890 1.1751 0.1161  0.1213  0.0236  1553 ASP A OD2   
2597 N  N     . ASN A 337 ? 0.9865 1.0369 1.0069 0.1109  0.1333  0.0323  1554 ASN A N     
2598 C  CA    . ASN A 337 ? 1.0485 1.1180 1.1054 0.1144  0.1456  0.0359  1554 ASN A CA    
2599 C  C     . ASN A 337 ? 1.1101 1.1832 1.1798 0.1185  0.1374  0.0283  1554 ASN A C     
2600 O  O     . ASN A 337 ? 1.1781 1.2715 1.2855 0.1192  0.1396  0.0315  1554 ASN A O     
2601 C  CB    . ASN A 337 ? 1.1661 1.2589 1.2626 0.1056  0.1442  0.0449  1554 ASN A CB    
2602 C  CG    . ASN A 337 ? 1.3419 1.4326 1.4319 0.1026  0.1573  0.0540  1554 ASN A CG    
2603 O  OD1   . ASN A 337 ? 1.3907 1.4773 1.4733 0.0949  0.1483  0.0571  1554 ASN A OD1   
2604 N  ND2   . ASN A 337 ? 1.3716 1.4647 1.4649 0.1088  0.1798  0.0590  1554 ASN A ND2   
2605 N  N     . TYR A 338 ? 1.0433 1.0966 1.0822 0.1215  0.1284  0.0186  1555 TYR A N     
2606 C  CA    . TYR A 338 ? 0.9031 0.9554 0.9497 0.1252  0.1204  0.0111  1555 TYR A CA    
2607 C  C     . TYR A 338 ? 0.9477 0.9742 0.9557 0.1329  0.1247  0.0014  1555 TYR A C     
2608 O  O     . TYR A 338 ? 1.0395 1.0477 1.0116 0.1308  0.1193  -0.0028 1555 TYR A O     
2609 C  CB    . TYR A 338 ? 0.8140 0.8714 0.8703 0.1166  0.0977  0.0087  1555 TYR A CB    
2610 C  CG    . TYR A 338 ? 0.8731 0.9560 0.9703 0.1101  0.0926  0.0162  1555 TYR A CG    
2611 C  CD1   . TYR A 338 ? 0.9989 1.1002 1.1295 0.1141  0.1017  0.0208  1555 TYR A CD1   
2612 C  CD2   . TYR A 338 ? 0.9306 1.0187 1.0331 0.1001  0.0783  0.0182  1555 TYR A CD2   
2613 C  CE1   . TYR A 338 ? 1.1564 1.2810 1.3235 0.1077  0.0956  0.0270  1555 TYR A CE1   
2614 C  CE2   . TYR A 338 ? 1.0446 1.1543 1.1822 0.0936  0.0732  0.0238  1555 TYR A CE2   
2615 C  CZ    . TYR A 338 ? 1.2155 1.3435 1.3848 0.0971  0.0812  0.0280  1555 TYR A CZ    
2616 O  OH    . TYR A 338 ? 1.3280 1.4778 1.5317 0.0901  0.0748  0.0331  1555 TYR A OH    
2617 N  N     . SER A 339 ? 0.8727 0.8977 0.8888 0.1417  0.1343  -0.0022 1556 SER A N     
2618 C  CA    . SER A 339 ? 0.8957 0.8953 0.8778 0.1492  0.1390  -0.0127 1556 SER A CA    
2619 C  C     . SER A 339 ? 0.8074 0.7940 0.7750 0.1448  0.1186  -0.0221 1556 SER A C     
2620 O  O     . SER A 339 ? 0.8724 0.8719 0.8644 0.1391  0.1038  -0.0206 1556 SER A O     
2621 C  CB    . SER A 339 ? 0.9810 0.9830 0.9798 0.1604  0.1559  -0.0133 1556 SER A CB    
2622 O  OG    . SER A 339 ? 0.9386 0.9557 0.9725 0.1605  0.1468  -0.0121 1556 SER A OG    
2623 N  N     . PRO A 340 ? 0.8122 0.7728 0.7398 0.1472  0.1177  -0.0322 1557 PRO A N     
2624 C  CA    . PRO A 340 ? 0.8087 0.7564 0.7250 0.1434  0.0998  -0.0419 1557 PRO A CA    
2625 C  C     . PRO A 340 ? 0.8300 0.7865 0.7777 0.1453  0.0956  -0.0426 1557 PRO A C     
2626 O  O     . PRO A 340 ? 0.8110 0.7740 0.7717 0.1382  0.0786  -0.0428 1557 PRO A O     
2627 C  CB    . PRO A 340 ? 0.8575 0.7760 0.7305 0.1489  0.1064  -0.0530 1557 PRO A CB    
2628 C  CG    . PRO A 340 ? 0.9713 0.8864 0.8237 0.1526  0.1229  -0.0481 1557 PRO A CG    
2629 C  CD    . PRO A 340 ? 0.8161 0.7581 0.7060 0.1526  0.1325  -0.0347 1557 PRO A CD    
2630 N  N     . GLY A 341 ? 0.8981 0.8560 0.8598 0.1553  0.1114  -0.0419 1558 GLY A N     
2631 C  CA    . GLY A 341 ? 0.8143 0.7800 0.8052 0.1581  0.1075  -0.0414 1558 GLY A CA    
2632 C  C     . GLY A 341 ? 0.9122 0.9063 0.9417 0.1521  0.0976  -0.0313 1558 GLY A C     
2633 O  O     . GLY A 341 ? 0.9175 0.9155 0.9615 0.1487  0.0841  -0.0318 1558 GLY A O     
2634 N  N     . TRP A 342 ? 0.8481 0.8612 0.8938 0.1503  0.1044  -0.0220 1559 TRP A N     
2635 C  CA    . TRP A 342 ? 0.7803 0.8187 0.8585 0.1427  0.0937  -0.0135 1559 TRP A CA    
2636 C  C     . TRP A 342 ? 0.8097 0.8441 0.8781 0.1323  0.0733  -0.0167 1559 TRP A C     
2637 O  O     . TRP A 342 ? 0.9271 0.9740 1.0175 0.1278  0.0610  -0.0142 1559 TRP A O     
2638 C  CB    . TRP A 342 ? 0.8791 0.9339 0.9696 0.1404  0.1035  -0.0045 1559 TRP A CB    
2639 C  CG    . TRP A 342 ? 0.8416 0.9225 0.9677 0.1325  0.0934  0.0037  1559 TRP A CG    
2640 C  CD1   . TRP A 342 ? 0.7556 0.8602 0.9202 0.1348  0.0982  0.0114  1559 TRP A CD1   
2641 C  CD2   . TRP A 342 ? 0.7552 0.8403 0.8811 0.1213  0.0765  0.0044  1559 TRP A CD2   
2642 N  NE1   . TRP A 342 ? 0.7548 0.8771 0.9409 0.1250  0.0846  0.0161  1559 TRP A NE1   
2643 C  CE2   . TRP A 342 ? 0.7561 0.8661 0.9186 0.1169  0.0720  0.0118  1559 TRP A CE2   
2644 C  CE3   . TRP A 342 ? 0.9071 0.9777 1.0062 0.1147  0.0648  -0.0006 1559 TRP A CE3   
2645 C  CZ2   . TRP A 342 ? 0.8752 0.9938 1.0458 0.1062  0.0572  0.0137  1559 TRP A CZ2   
2646 C  CZ3   . TRP A 342 ? 0.9497 1.0300 1.0593 0.1048  0.0506  0.0021  1559 TRP A CZ3   
2647 C  CH2   . TRP A 342 ? 0.8762 0.9793 1.0201 0.1006  0.0475  0.0088  1559 TRP A CH2   
2648 N  N     . LYS A 343 ? 0.7136 0.7307 0.7486 0.1287  0.0696  -0.0222 1560 LYS A N     
2649 C  CA    . LYS A 343 ? 0.8212 0.8347 0.8474 0.1193  0.0510  -0.0253 1560 LYS A CA    
2650 C  C     . LYS A 343 ? 0.8252 0.8281 0.8494 0.1192  0.0406  -0.0326 1560 LYS A C     
2651 O  O     . LYS A 343 ? 0.6909 0.7009 0.7275 0.1125  0.0265  -0.0318 1560 LYS A O     
2652 C  CB    . LYS A 343 ? 0.9001 0.8988 0.8922 0.1165  0.0499  -0.0284 1560 LYS A CB    
2653 C  CG    . LYS A 343 ? 0.8734 0.8816 0.8670 0.1158  0.0600  -0.0199 1560 LYS A CG    
2654 C  CD    . LYS A 343 ? 0.9039 0.8998 0.8668 0.1114  0.0542  -0.0211 1560 LYS A CD    
2655 C  CE    . LYS A 343 ? 0.9020 0.9038 0.8632 0.1115  0.0662  -0.0123 1560 LYS A CE    
2656 N  NZ    . LYS A 343 ? 0.9434 0.9246 0.8639 0.1158  0.0734  -0.0156 1560 LYS A NZ    
2657 N  N     . TYR A 344 ? 0.9230 0.9077 0.9309 0.1266  0.0480  -0.0399 1561 TYR A N     
2658 C  CA    . TYR A 344 ? 0.8176 0.7911 0.8257 0.1269  0.0400  -0.0464 1561 TYR A CA    
2659 C  C     . TYR A 344 ? 0.8048 0.7968 0.8479 0.1267  0.0355  -0.0394 1561 TYR A C     
2660 O  O     . TYR A 344 ? 0.6878 0.6809 0.7373 0.1207  0.0219  -0.0403 1561 TYR A O     
2661 C  CB    . TYR A 344 ? 0.6971 0.6499 0.6887 0.1362  0.0519  -0.0541 1561 TYR A CB    
2662 C  CG    . TYR A 344 ? 0.7308 0.6632 0.6849 0.1381  0.0586  -0.0616 1561 TYR A CG    
2663 C  CD1   . TYR A 344 ? 0.7750 0.7052 0.7083 0.1308  0.0506  -0.0624 1561 TYR A CD1   
2664 C  CD2   . TYR A 344 ? 0.7624 0.6770 0.7008 0.1475  0.0732  -0.0679 1561 TYR A CD2   
2665 C  CE1   . TYR A 344 ? 0.8595 0.7706 0.7558 0.1329  0.0562  -0.0689 1561 TYR A CE1   
2666 C  CE2   . TYR A 344 ? 0.9206 0.8149 0.8212 0.1494  0.0798  -0.0754 1561 TYR A CE2   
2667 C  CZ    . TYR A 344 ? 0.9348 0.8275 0.8136 0.1420  0.0707  -0.0758 1561 TYR A CZ    
2668 O  OH    . TYR A 344 ? 0.9694 0.8412 0.8082 0.1443  0.0766  -0.0830 1561 TYR A OH    
2669 N  N     . ASN A 345 ? 0.6340 0.6415 0.7003 0.1333  0.0467  -0.0321 1562 ASN A N     
2670 C  CA    . ASN A 345 ? 0.7780 0.8036 0.8770 0.1339  0.0418  -0.0251 1562 ASN A CA    
2671 C  C     . ASN A 345 ? 0.7883 0.8314 0.9010 0.1235  0.0284  -0.0197 1562 ASN A C     
2672 O  O     . ASN A 345 ? 0.7770 0.8271 0.9046 0.1204  0.0178  -0.0175 1562 ASN A O     
2673 C  CB    . ASN A 345 ? 0.8511 0.8915 0.9742 0.1432  0.0560  -0.0181 1562 ASN A CB    
2674 C  CG    . ASN A 345 ? 0.8514 0.9112 1.0077 0.1442  0.0494  -0.0104 1562 ASN A CG    
2675 O  OD1   . ASN A 345 ? 0.8994 0.9518 1.0598 0.1489  0.0465  -0.0117 1562 ASN A OD1   
2676 N  ND2   . ASN A 345 ? 0.7408 0.8250 0.9204 0.1392  0.0461  -0.0024 1562 ASN A ND2   
2677 N  N     . HIS A 346 ? 0.8263 0.8754 0.9332 0.1182  0.0295  -0.0175 1563 HIS A N     
2678 C  CA    . HIS A 346 ? 0.7213 0.7849 0.8399 0.1084  0.0179  -0.0132 1563 HIS A CA    
2679 C  C     . HIS A 346 ? 0.8219 0.8753 0.9286 0.1016  0.0031  -0.0184 1563 HIS A C     
2680 O  O     . HIS A 346 ? 0.8980 0.9605 1.0202 0.0974  -0.0068 -0.0159 1563 HIS A O     
2681 C  CB    . HIS A 346 ? 0.8080 0.8750 0.9187 0.1045  0.0228  -0.0103 1563 HIS A CB    
2682 C  CG    . HIS A 346 ? 0.9241 1.0056 1.0488 0.0950  0.0131  -0.0056 1563 HIS A CG    
2683 N  ND1   . HIS A 346 ? 0.9238 0.9982 1.0327 0.0877  0.0041  -0.0079 1563 HIS A ND1   
2684 C  CD2   . HIS A 346 ? 0.9056 1.0076 1.0588 0.0915  0.0102  0.0009  1563 HIS A CD2   
2685 C  CE1   . HIS A 346 ? 0.8827 0.9713 1.0090 0.0805  -0.0025 -0.0033 1563 HIS A CE1   
2686 N  NE2   . HIS A 346 ? 0.8492 0.9543 1.0015 0.0822  0.0006  0.0017  1563 HIS A NE2   
2687 N  N     . TRP A 347 ? 0.8125 0.8469 0.8917 0.1007  0.0015  -0.0258 1564 TRP A N     
2688 C  CA    . TRP A 347 ? 0.8576 0.8838 0.9275 0.0937  -0.0123 -0.0305 1564 TRP A CA    
2689 C  C     . TRP A 347 ? 0.9160 0.9350 0.9910 0.0956  -0.0164 -0.0337 1564 TRP A C     
2690 O  O     . TRP A 347 ? 0.8437 0.8624 0.9215 0.0893  -0.0275 -0.0348 1564 TRP A O     
2691 C  CB    . TRP A 347 ? 0.8464 0.8558 0.8868 0.0918  -0.0140 -0.0373 1564 TRP A CB    
2692 C  CG    . TRP A 347 ? 0.9359 0.9519 0.9712 0.0890  -0.0121 -0.0329 1564 TRP A CG    
2693 C  CD1   . TRP A 347 ? 0.9101 0.9209 0.9295 0.0932  -0.0013 -0.0322 1564 TRP A CD1   
2694 C  CD2   . TRP A 347 ? 0.9230 0.9516 0.9696 0.0816  -0.0199 -0.0278 1564 TRP A CD2   
2695 N  NE1   . TRP A 347 ? 0.7795 0.7987 0.7998 0.0887  -0.0023 -0.0265 1564 TRP A NE1   
2696 C  CE2   . TRP A 347 ? 0.8265 0.8564 0.8639 0.0816  -0.0137 -0.0239 1564 TRP A CE2   
2697 C  CE3   . TRP A 347 ? 0.9106 0.9481 0.9731 0.0751  -0.0308 -0.0262 1564 TRP A CE3   
2698 C  CZ2   . TRP A 347 ? 0.7444 0.7835 0.7889 0.0753  -0.0184 -0.0187 1564 TRP A CZ2   
2699 C  CZ3   . TRP A 347 ? 0.8280 0.8746 0.8967 0.0691  -0.0351 -0.0218 1564 TRP A CZ3   
2700 C  CH2   . TRP A 347 ? 0.7921 0.8393 0.8526 0.0692  -0.0291 -0.0180 1564 TRP A CH2   
2701 N  N     . GLU A 348 ? 0.7920 0.8055 0.8698 0.1044  -0.0069 -0.0344 1565 GLU A N     
2702 C  CA    . GLU A 348 ? 0.7971 0.8050 0.8834 0.1070  -0.0099 -0.0352 1565 GLU A CA    
2703 C  C     . GLU A 348 ? 0.7427 0.7701 0.8548 0.1046  -0.0163 -0.0269 1565 GLU A C     
2704 O  O     . GLU A 348 ? 0.7443 0.7698 0.8592 0.0999  -0.0259 -0.0272 1565 GLU A O     
2705 C  CB    . GLU A 348 ? 0.9526 0.9497 1.0368 0.1178  0.0026  -0.0374 1565 GLU A CB    
2706 C  CG    . GLU A 348 ? 1.1009 1.0712 1.1572 0.1187  0.0042  -0.0484 1565 GLU A CG    
2707 C  CD    . GLU A 348 ? 1.4105 1.3671 1.4606 0.1298  0.0187  -0.0519 1565 GLU A CD    
2708 O  OE1   . GLU A 348 ? 1.4782 1.4437 1.5497 0.1378  0.0256  -0.0456 1565 GLU A OE1   
2709 O  OE2   . GLU A 348 ? 1.5503 1.4869 1.5736 0.1308  0.0229  -0.0610 1565 GLU A OE2   
2710 N  N     . LEU A 349 ? 0.7524 0.7988 0.8829 0.1071  -0.0113 -0.0196 1566 LEU A N     
2711 C  CA    . LEU A 349 ? 0.8053 0.8709 0.9584 0.1036  -0.0190 -0.0123 1566 LEU A CA    
2712 C  C     . LEU A 349 ? 0.7848 0.8515 0.9324 0.0928  -0.0310 -0.0136 1566 LEU A C     
2713 O  O     . LEU A 349 ? 0.8146 0.8849 0.9697 0.0896  -0.0396 -0.0115 1566 LEU A O     
2714 C  CB    . LEU A 349 ? 0.8445 0.9311 1.0176 0.1055  -0.0129 -0.0052 1566 LEU A CB    
2715 C  CG    . LEU A 349 ? 0.8219 0.9157 1.0124 0.1164  -0.0026 -0.0006 1566 LEU A CG    
2716 C  CD1   . LEU A 349 ? 0.7210 0.8361 0.9313 0.1162  0.0036  0.0058  1566 LEU A CD1   
2717 C  CD2   . LEU A 349 ? 0.5127 0.6111 0.7187 0.1201  -0.0091 0.0036  1566 LEU A CD2   
2718 N  N     . LYS A 350 ? 0.7107 0.7733 0.8441 0.0878  -0.0313 -0.0170 1567 LYS A N     
2719 C  CA    . LYS A 350 ? 0.7960 0.8599 0.9257 0.0784  -0.0418 -0.0180 1567 LYS A CA    
2720 C  C     . LYS A 350 ? 0.9089 0.9572 1.0257 0.0756  -0.0486 -0.0240 1567 LYS A C     
2721 O  O     . LYS A 350 ? 1.0542 1.1044 1.1715 0.0685  -0.0570 -0.0244 1567 LYS A O     
2722 C  CB    . LYS A 350 ? 0.7617 0.8269 0.8824 0.0746  -0.0400 -0.0183 1567 LYS A CB    
2723 C  CG    . LYS A 350 ? 0.7252 0.8088 0.8634 0.0727  -0.0371 -0.0115 1567 LYS A CG    
2724 C  CD    . LYS A 350 ? 0.9404 1.0229 1.0687 0.0700  -0.0332 -0.0109 1567 LYS A CD    
2725 C  CE    . LYS A 350 ? 1.0575 1.1416 1.1843 0.0613  -0.0423 -0.0109 1567 LYS A CE    
2726 N  NZ    . LYS A 350 ? 1.0590 1.1563 1.1992 0.0568  -0.0403 -0.0052 1567 LYS A NZ    
2727 N  N     . GLY A 351 ? 0.7922 0.8249 0.8983 0.0807  -0.0448 -0.0290 1568 GLY A N     
2728 C  CA    . GLY A 351 ? 0.7792 0.7982 0.8784 0.0780  -0.0508 -0.0338 1568 GLY A CA    
2729 C  C     . GLY A 351 ? 0.9119 0.9193 0.9941 0.0722  -0.0564 -0.0408 1568 GLY A C     
2730 O  O     . GLY A 351 ? 0.8995 0.9011 0.9815 0.0671  -0.0635 -0.0433 1568 GLY A O     
2731 N  N     . VAL A 352 ? 0.9235 0.9273 0.9915 0.0728  -0.0535 -0.0437 1569 VAL A N     
2732 C  CA    . VAL A 352 ? 0.8153 0.8102 0.8669 0.0676  -0.0602 -0.0496 1569 VAL A CA    
2733 C  C     . VAL A 352 ? 0.8320 0.8078 0.8709 0.0679  -0.0619 -0.0580 1569 VAL A C     
2734 O  O     . VAL A 352 ? 0.8034 0.7678 0.8323 0.0741  -0.0542 -0.0617 1569 VAL A O     
2735 C  CB    . VAL A 352 ? 0.7135 0.7094 0.7518 0.0694  -0.0558 -0.0491 1569 VAL A CB    
2736 C  CG1   . VAL A 352 ? 0.7260 0.7128 0.7459 0.0649  -0.0636 -0.0545 1569 VAL A CG1   
2737 C  CG2   . VAL A 352 ? 0.6485 0.6623 0.7015 0.0683  -0.0537 -0.0408 1569 VAL A CG2   
2738 N  N     . PRO A 353 ? 0.8033 0.7744 0.8424 0.0611  -0.0713 -0.0617 1570 PRO A N     
2739 C  CA    . PRO A 353 ? 0.8372 0.7900 0.8675 0.0603  -0.0731 -0.0697 1570 PRO A CA    
2740 C  C     . PRO A 353 ? 0.8373 0.7736 0.8445 0.0641  -0.0691 -0.0777 1570 PRO A C     
2741 O  O     . PRO A 353 ? 0.9335 0.8539 0.9352 0.0669  -0.0652 -0.0832 1570 PRO A O     
2742 C  CB    . PRO A 353 ? 0.9269 0.8810 0.9605 0.0511  -0.0845 -0.0721 1570 PRO A CB    
2743 C  CG    . PRO A 353 ? 0.8663 0.8386 0.9165 0.0485  -0.0866 -0.0639 1570 PRO A CG    
2744 C  CD    . PRO A 353 ? 0.8938 0.8765 0.9448 0.0541  -0.0795 -0.0581 1570 PRO A CD    
2745 N  N     . VAL A 354 ? 0.7425 0.6801 0.7346 0.0643  -0.0697 -0.0788 1571 VAL A N     
2746 C  CA    . VAL A 354 ? 0.8082 0.7287 0.7743 0.0676  -0.0664 -0.0869 1571 VAL A CA    
2747 C  C     . VAL A 354 ? 0.9514 0.8779 0.9078 0.0733  -0.0578 -0.0824 1571 VAL A C     
2748 O  O     . VAL A 354 ? 1.0057 0.9459 0.9665 0.0708  -0.0610 -0.0762 1571 VAL A O     
2749 C  CB    . VAL A 354 ? 0.8732 0.7842 0.8231 0.0605  -0.0789 -0.0949 1571 VAL A CB    
2750 C  CG1   . VAL A 354 ? 0.6906 0.5835 0.6086 0.0641  -0.0757 -0.1034 1571 VAL A CG1   
2751 C  CG2   . VAL A 354 ? 0.9351 0.8393 0.8952 0.0543  -0.0863 -0.0998 1571 VAL A CG2   
2752 N  N     . ARG A 355 ? 0.8548 0.7696 0.7974 0.0808  -0.0463 -0.0857 1572 ARG A N     
2753 C  CA    . ARG A 355 ? 0.8486 0.7645 0.7763 0.0862  -0.0369 -0.0832 1572 ARG A CA    
2754 C  C     . ARG A 355 ? 0.9476 0.8426 0.8407 0.0867  -0.0381 -0.0933 1572 ARG A C     
2755 O  O     . ARG A 355 ? 0.9964 0.8731 0.8781 0.0875  -0.0379 -0.1027 1572 ARG A O     
2756 C  CB    . ARG A 355 ? 0.9700 0.8900 0.9090 0.0953  -0.0210 -0.0785 1572 ARG A CB    
2757 C  CG    . ARG A 355 ? 0.9127 0.8301 0.8344 0.1015  -0.0085 -0.0772 1572 ARG A CG    
2758 C  CD    . ARG A 355 ? 0.7717 0.6889 0.7035 0.1110  0.0072  -0.0753 1572 ARG A CD    
2759 N  NE    . ARG A 355 ? 1.0695 0.9627 0.9795 0.1163  0.0138  -0.0856 1572 ARG A NE    
2760 C  CZ    . ARG A 355 ? 1.2346 1.1217 1.1557 0.1232  0.0224  -0.0871 1572 ARG A CZ    
2761 N  NH1   . ARG A 355 ? 0.7446 0.6493 0.6985 0.1256  0.0242  -0.0783 1572 ARG A NH1   
2762 N  NH2   . ARG A 355 ? 1.5551 1.4175 1.4534 0.1279  0.0290  -0.0975 1572 ARG A NH2   
2763 N  N     . ILE A 356 ? 0.9654 0.8619 0.8407 0.0861  -0.0394 -0.0913 1573 ILE A N     
2764 C  CA    . ILE A 356 ? 0.9530 0.8301 0.7918 0.0871  -0.0405 -0.1000 1573 ILE A CA    
2765 C  C     . ILE A 356 ? 1.0050 0.8778 0.8282 0.0960  -0.0230 -0.0974 1573 ILE A C     
2766 O  O     . ILE A 356 ? 1.0597 0.9466 0.8895 0.0976  -0.0172 -0.0875 1573 ILE A O     
2767 C  CB    . ILE A 356 ? 0.9516 0.8315 0.7779 0.0803  -0.0558 -0.0997 1573 ILE A CB    
2768 C  CG1   . ILE A 356 ? 0.9775 0.8585 0.8170 0.0717  -0.0722 -0.1045 1573 ILE A CG1   
2769 C  CG2   . ILE A 356 ? 0.8788 0.7408 0.6638 0.0828  -0.0551 -0.1060 1573 ILE A CG2   
2770 C  CD1   . ILE A 356 ? 1.0953 0.9814 0.9275 0.0654  -0.0880 -0.1036 1573 ILE A CD1   
2771 N  N     . GLU A 357 ? 1.1194 0.9726 0.9235 0.1017  -0.0135 -0.1061 1574 GLU A N     
2772 C  CA    . GLU A 357 ? 1.2199 1.0642 1.0010 0.1101  0.0032  -0.1059 1574 GLU A CA    
2773 C  C     . GLU A 357 ? 1.3316 1.1581 1.0703 0.1081  -0.0034 -0.1134 1574 GLU A C     
2774 O  O     . GLU A 357 ? 1.4533 1.2606 1.1714 0.1051  -0.0119 -0.1256 1574 GLU A O     
2775 C  CB    . GLU A 357 ? 1.2401 1.0715 1.0223 0.1184  0.0184  -0.1114 1574 GLU A CB    
2776 C  CG    . GLU A 357 ? 1.2625 1.1119 1.0864 0.1210  0.0236  -0.1034 1574 GLU A CG    
2777 C  CD    . GLU A 357 ? 1.3266 1.1646 1.1537 0.1308  0.0398  -0.1071 1574 GLU A CD    
2778 O  OE1   . GLU A 357 ? 1.4539 1.2701 1.2503 0.1363  0.0499  -0.1157 1574 GLU A OE1   
2779 O  OE2   . GLU A 357 ? 1.2727 1.1234 1.1326 0.1333  0.0425  -0.1012 1574 GLU A OE2   
2780 N  N     . LEU A 358 ? 1.3262 1.1591 1.0521 0.1093  -0.0002 -0.1056 1575 LEU A N     
2781 C  CA    . LEU A 358 ? 1.3407 1.1576 1.0237 0.1087  -0.0051 -0.1104 1575 LEU A CA    
2782 C  C     . LEU A 358 ? 1.3597 1.1736 1.0251 0.1173  0.0153  -0.1044 1575 LEU A C     
2783 O  O     . LEU A 358 ? 1.3346 1.1660 1.0161 0.1180  0.0211  -0.0916 1575 LEU A O     
2784 C  CB    . LEU A 358 ? 1.3154 1.1432 0.9990 0.1009  -0.0244 -0.1053 1575 LEU A CB    
2785 C  CG    . LEU A 358 ? 1.3469 1.1563 0.9861 0.0989  -0.0357 -0.1129 1575 LEU A CG    
2786 C  CD1   . LEU A 358 ? 1.3091 1.1293 0.9564 0.0902  -0.0588 -0.1105 1575 LEU A CD1   
2787 C  CD2   . LEU A 358 ? 1.3043 1.1034 0.9067 0.1058  -0.0227 -0.1090 1575 LEU A CD2   
2788 N  N     . GLY A 359 ? 1.3258 1.1167 0.9585 0.1236  0.0270  -0.1138 1576 GLY A N     
2789 C  CA    . GLY A 359 ? 1.2648 1.0490 0.8753 0.1321  0.0477  -0.1096 1576 GLY A CA    
2790 C  C     . GLY A 359 ? 1.3280 1.0900 0.8850 0.1323  0.0436  -0.1161 1576 GLY A C     
2791 O  O     . GLY A 359 ? 1.4282 1.1840 0.9684 0.1251  0.0225  -0.1220 1576 GLY A O     
2792 N  N     . PHE A 360 ? 1.2947 1.0443 0.8242 0.1408  0.0643  -0.1152 1577 PHE A N     
2793 C  CA    . PHE A 360 ? 1.3367 1.0642 0.8111 0.1418  0.0620  -0.1204 1577 PHE A CA    
2794 C  C     . PHE A 360 ? 1.5282 1.2289 0.9704 0.1400  0.0524  -0.1392 1577 PHE A C     
2795 O  O     . PHE A 360 ? 1.6132 1.3025 1.0234 0.1343  0.0334  -0.1455 1577 PHE A O     
2796 C  CB    . PHE A 360 ? 1.4405 1.1606 0.8930 0.1517  0.0889  -0.1146 1577 PHE A CB    
2797 C  CG    . PHE A 360 ? 1.4772 1.2220 0.9588 0.1526  0.0989  -0.0960 1577 PHE A CG    
2798 C  CD1   . PHE A 360 ? 1.4688 1.2223 0.9438 0.1474  0.0861  -0.0860 1577 PHE A CD1   
2799 C  CD2   . PHE A 360 ? 1.4354 1.1944 0.9517 0.1587  0.1209  -0.0887 1577 PHE A CD2   
2800 C  CE1   . PHE A 360 ? 1.4959 1.2698 0.9970 0.1477  0.0955  -0.0696 1577 PHE A CE1   
2801 C  CE2   . PHE A 360 ? 1.4881 1.2693 1.0318 0.1584  0.1295  -0.0725 1577 PHE A CE2   
2802 C  CZ    . PHE A 360 ? 1.5172 1.3049 1.0528 0.1526  0.1171  -0.0632 1577 PHE A CZ    
2803 N  N     . LYS A 361 ? 1.6126 1.3029 1.0640 0.1446  0.0645  -0.1484 1578 LYS A N     
2804 C  CA    . LYS A 361 ? 1.6007 1.2645 1.0248 0.1421  0.0554  -0.1670 1578 LYS A CA    
2805 C  C     . LYS A 361 ? 1.5776 1.2484 1.0177 0.1300  0.0266  -0.1715 1578 LYS A C     
2806 O  O     . LYS A 361 ? 1.5691 1.2200 0.9777 0.1246  0.0114  -0.1851 1578 LYS A O     
2807 C  CB    . LYS A 361 ? 1.4687 1.1214 0.9059 0.1497  0.0746  -0.1743 1578 LYS A CB    
2808 N  N     . ASP A 362 ? 1.5316 1.2305 1.0197 0.1254  0.0184  -0.1604 1579 ASP A N     
2809 C  CA    . ASP A 362 ? 1.5090 1.2158 1.0148 0.1143  -0.0071 -0.1639 1579 ASP A CA    
2810 C  C     . ASP A 362 ? 1.5141 1.2227 0.9954 0.1081  -0.0268 -0.1618 1579 ASP A C     
2811 O  O     . ASP A 362 ? 1.4141 1.1130 0.8805 0.1004  -0.0469 -0.1723 1579 ASP A O     
2812 C  CB    . ASP A 362 ? 1.5058 1.2406 1.0674 0.1119  -0.0085 -0.1526 1579 ASP A CB    
2813 C  CG    . ASP A 362 ? 1.6328 1.3659 1.2197 0.1176  0.0074  -0.1548 1579 ASP A CG    
2814 O  OD1   . ASP A 362 ? 1.7638 1.4731 1.3322 0.1192  0.0105  -0.1684 1579 ASP A OD1   
2815 O  OD2   . ASP A 362 ? 1.6238 1.3782 1.2482 0.1206  0.0164  -0.1431 1579 ASP A OD2   
2816 N  N     . LEU A 363 ? 1.6419 1.3632 1.1199 0.1113  -0.0216 -0.1481 1580 LEU A N     
2817 C  CA    . LEU A 363 ? 1.6091 1.3324 1.0642 0.1067  -0.0397 -0.1444 1580 LEU A CA    
2818 C  C     . LEU A 363 ? 1.6512 1.3461 1.0472 0.1083  -0.0426 -0.1559 1580 LEU A C     
2819 O  O     . LEU A 363 ? 1.7844 1.4763 1.1590 0.1025  -0.0641 -0.1585 1580 LEU A O     
2820 C  CB    . LEU A 363 ? 1.5390 1.2813 1.0061 0.1100  -0.0319 -0.1261 1580 LEU A CB    
2821 C  CG    . LEU A 363 ? 1.5820 1.3175 1.0248 0.1194  -0.0082 -0.1184 1580 LEU A CG    
2822 C  CD1   . LEU A 363 ? 1.6604 1.3763 1.0460 0.1213  -0.0130 -0.1203 1580 LEU A CD1   
2823 C  CD2   . LEU A 363 ? 1.4934 1.2544 0.9733 0.1205  0.0006  -0.1005 1580 LEU A CD2   
2824 N  N     . GLN A 364 ? 1.5871 1.2609 0.9563 0.1161  -0.0220 -0.1633 1581 GLN A N     
2825 C  CA    . GLN A 364 ? 1.6364 1.2808 0.9461 0.1174  -0.0246 -0.1757 1581 GLN A CA    
2826 C  C     . GLN A 364 ? 1.7374 1.3663 1.0379 0.1092  -0.0440 -0.1938 1581 GLN A C     
2827 O  O     . GLN A 364 ? 1.8161 1.4241 1.0697 0.1066  -0.0559 -0.2046 1581 GLN A O     
2828 C  CB    . GLN A 364 ? 1.6443 1.2693 0.9273 0.1286  0.0049  -0.1788 1581 GLN A CB    
2829 N  N     . ASN A 365 ? 1.8044 1.4417 1.1473 0.1050  -0.0467 -0.1976 1582 ASN A N     
2830 C  CA    . ASN A 365 ? 1.8999 1.5271 1.2444 0.0953  -0.0667 -0.2127 1582 ASN A CA    
2831 C  C     . ASN A 365 ? 1.8601 1.5126 1.2421 0.0851  -0.0908 -0.2062 1582 ASN A C     
2832 O  O     . ASN A 365 ? 1.8181 1.4679 1.2154 0.0764  -0.1056 -0.2162 1582 ASN A O     
2833 C  CB    . ASN A 365 ? 1.8905 1.5057 1.2534 0.0975  -0.0528 -0.2223 1582 ASN A CB    
2834 C  CG    . ASN A 365 ? 1.9557 1.5398 1.2755 0.1061  -0.0330 -0.2336 1582 ASN A CG    
2835 O  OD1   . ASN A 365 ? 1.9163 1.4994 1.2203 0.1160  -0.0129 -0.2259 1582 ASN A OD1   
2836 N  ND2   . ASN A 365 ? 2.0504 1.6078 1.3504 0.1023  -0.0379 -0.2523 1582 ASN A ND2   
2837 N  N     . ASP A 366 ? 1.8731 1.5497 1.2723 0.0861  -0.0933 -0.1894 1583 ASP A N     
2838 C  CA    . ASP A 366 ? 1.8892 1.5897 1.3203 0.0777  -0.1153 -0.1821 1583 ASP A CA    
2839 C  C     . ASP A 366 ? 1.7578 1.4697 1.2371 0.0717  -0.1188 -0.1845 1583 ASP A C     
2840 O  O     . ASP A 366 ? 1.7958 1.5090 1.2861 0.0622  -0.1385 -0.1921 1583 ASP A O     
2841 C  CB    . ASP A 366 ? 1.9954 1.6879 1.3950 0.0706  -0.1409 -0.1895 1583 ASP A CB    
2842 C  CG    . ASP A 366 ? 2.0284 1.7458 1.4480 0.0669  -0.1582 -0.1761 1583 ASP A CG    
2843 O  OD1   . ASP A 366 ? 2.0227 1.7558 1.4779 0.0586  -0.1745 -0.1764 1583 ASP A OD1   
2844 O  OD2   . ASP A 366 ? 2.0669 1.7880 1.4674 0.0725  -0.1546 -0.1647 1583 ASP A OD2   
2845 N  N     . GLN A 367 ? 1.5697 1.2900 1.0778 0.0775  -0.0990 -0.1778 1584 GLN A N     
2846 C  CA    . GLN A 367 ? 1.4692 1.1971 1.0188 0.0737  -0.0987 -0.1797 1584 GLN A CA    
2847 C  C     . GLN A 367 ? 1.3633 1.1098 0.9471 0.0804  -0.0805 -0.1660 1584 GLN A C     
2848 O  O     . GLN A 367 ? 1.3102 1.0641 0.8874 0.0868  -0.0689 -0.1555 1584 GLN A O     
2849 C  CB    . GLN A 367 ? 1.5381 1.2393 1.0718 0.0736  -0.0936 -0.1962 1584 GLN A CB    
2850 C  CG    . GLN A 367 ? 1.5642 1.2512 1.0818 0.0851  -0.0677 -0.1971 1584 GLN A CG    
2851 C  CD    . GLN A 367 ? 1.6491 1.3067 1.1472 0.0857  -0.0622 -0.2140 1584 GLN A CD    
2852 O  OE1   . GLN A 367 ? 1.7344 1.3753 1.2100 0.0781  -0.0781 -0.2275 1584 GLN A OE1   
2853 N  NE2   . GLN A 367 ? 1.6540 1.3049 1.1613 0.0949  -0.0399 -0.2137 1584 GLN A NE2   
2854 N  N     . PHE A 368 ? 1.3073 1.0603 0.9270 0.0786  -0.0777 -0.1663 1585 PHE A N     
2855 C  CA    . PHE A 368 ? 1.1856 0.9553 0.8383 0.0847  -0.0613 -0.1547 1585 PHE A CA    
2856 C  C     . PHE A 368 ? 1.1319 0.8980 0.8109 0.0839  -0.0575 -0.1595 1585 PHE A C     
2857 O  O     . PHE A 368 ? 1.2104 0.9631 0.8855 0.0775  -0.0684 -0.1707 1585 PHE A O     
2858 C  CB    . PHE A 368 ? 1.1474 0.9449 0.8279 0.0815  -0.0683 -0.1402 1585 PHE A CB    
2859 C  CG    . PHE A 368 ? 1.2851 1.0930 0.9875 0.0715  -0.0884 -0.1412 1585 PHE A CG    
2860 C  CD1   . PHE A 368 ? 1.3668 1.1702 1.0499 0.0649  -0.1073 -0.1466 1585 PHE A CD1   
2861 C  CD2   . PHE A 368 ? 1.2943 1.1172 1.0368 0.0687  -0.0886 -0.1363 1585 PHE A CD2   
2862 C  CE1   . PHE A 368 ? 1.3566 1.1712 1.0630 0.0559  -0.1249 -0.1470 1585 PHE A CE1   
2863 C  CE2   . PHE A 368 ? 1.3215 1.1539 1.0844 0.0597  -0.1054 -0.1369 1585 PHE A CE2   
2864 C  CZ    . PHE A 368 ? 1.3078 1.1366 1.0542 0.0533  -0.1232 -0.1422 1585 PHE A CZ    
2865 N  N     . VAL A 369 ? 0.9611 0.7390 0.6670 0.0904  -0.0422 -0.1507 1586 VAL A N     
2866 C  CA    . VAL A 369 ? 1.0386 0.8147 0.7711 0.0913  -0.0372 -0.1526 1586 VAL A CA    
2867 C  C     . VAL A 369 ? 0.9363 0.7389 0.7099 0.0873  -0.0431 -0.1408 1586 VAL A C     
2868 O  O     . VAL A 369 ? 0.9608 0.7828 0.7471 0.0897  -0.0387 -0.1291 1586 VAL A O     
2869 C  CB    . VAL A 369 ? 1.1390 0.9066 0.8705 0.1030  -0.0146 -0.1522 1586 VAL A CB    
2870 C  CG1   . VAL A 369 ? 1.1130 0.8722 0.8646 0.1040  -0.0114 -0.1564 1586 VAL A CG1   
2871 C  CG2   . VAL A 369 ? 1.1522 0.8961 0.8401 0.1087  -0.0049 -0.1615 1586 VAL A CG2   
2872 N  N     . ALA A 370 ? 0.8785 0.6810 0.6718 0.0808  -0.0527 -0.1438 1587 ALA A N     
2873 C  CA    . ALA A 370 ? 0.9566 0.7816 0.7874 0.0776  -0.0567 -0.1334 1587 ALA A CA    
2874 C  C     . ALA A 370 ? 0.8995 0.7210 0.7511 0.0822  -0.0466 -0.1324 1587 ALA A C     
2875 O  O     . ALA A 370 ? 0.9613 0.7621 0.8045 0.0823  -0.0452 -0.1420 1587 ALA A O     
2876 C  CB    . ALA A 370 ? 0.9958 0.8270 0.8361 0.0663  -0.0757 -0.1351 1587 ALA A CB    
2877 N  N     . VAL A 371 ? 0.7952 0.6367 0.6740 0.0858  -0.0405 -0.1205 1588 VAL A N     
2878 C  CA    . VAL A 371 ? 0.7637 0.6059 0.6633 0.0921  -0.0302 -0.1166 1588 VAL A CA    
2879 C  C     . VAL A 371 ? 0.8746 0.7362 0.8056 0.0873  -0.0374 -0.1074 1588 VAL A C     
2880 O  O     . VAL A 371 ? 0.9807 0.8631 0.9238 0.0854  -0.0403 -0.0986 1588 VAL A O     
2881 C  CB    . VAL A 371 ? 0.8870 0.7357 0.7882 0.1031  -0.0135 -0.1103 1588 VAL A CB    
2882 C  CG1   . VAL A 371 ? 0.9148 0.7580 0.8318 0.1114  -0.0021 -0.1088 1588 VAL A CG1   
2883 C  CG2   . VAL A 371 ? 0.7933 0.6283 0.6603 0.1069  -0.0064 -0.1168 1588 VAL A CG2   
2884 N  N     . ARG A 372 ? 0.8160 0.6698 0.7597 0.0861  -0.0389 -0.1090 1589 ARG A N     
2885 C  CA    . ARG A 372 ? 0.8283 0.6970 0.7978 0.0809  -0.0461 -0.1014 1589 ARG A CA    
2886 C  C     . ARG A 372 ? 0.8553 0.7396 0.8466 0.0883  -0.0375 -0.0902 1589 ARG A C     
2887 O  O     . ARG A 372 ? 0.8921 0.7683 0.8860 0.0969  -0.0270 -0.0898 1589 ARG A O     
2888 C  CB    . ARG A 372 ? 0.8838 0.7363 0.8569 0.0760  -0.0508 -0.1071 1589 ARG A CB    
2889 C  CG    . ARG A 372 ? 0.9616 0.8067 0.9249 0.0650  -0.0640 -0.1156 1589 ARG A CG    
2890 C  CD    . ARG A 372 ? 0.9958 0.8226 0.9634 0.0610  -0.0657 -0.1214 1589 ARG A CD    
2891 N  NE    . ARG A 372 ? 0.8863 0.7234 0.8792 0.0599  -0.0657 -0.1120 1589 ARG A NE    
2892 C  CZ    . ARG A 372 ? 0.8416 0.6694 0.8438 0.0533  -0.0699 -0.1141 1589 ARG A CZ    
2893 N  NH1   . ARG A 372 ? 0.7207 0.5296 0.7111 0.0466  -0.0752 -0.1256 1589 ARG A NH1   
2894 N  NH2   . ARG A 372 ? 0.7992 0.6361 0.8218 0.0528  -0.0691 -0.1047 1589 ARG A NH2   
2895 N  N     . ARG A 373 ? 0.8416 0.7477 0.8500 0.0846  -0.0429 -0.0812 1590 ARG A N     
2896 C  CA    . ARG A 373 ? 0.8131 0.7354 0.8426 0.0905  -0.0369 -0.0708 1590 ARG A CA    
2897 C  C     . ARG A 373 ? 0.8577 0.7736 0.9005 0.0933  -0.0355 -0.0683 1590 ARG A C     
2898 O  O     . ARG A 373 ? 0.7893 0.7110 0.8448 0.1016  -0.0279 -0.0619 1590 ARG A O     
2899 C  CB    . ARG A 373 ? 0.6231 0.5679 0.6663 0.0848  -0.0439 -0.0630 1590 ARG A CB    
2900 C  CG    . ARG A 373 ? 0.5763 0.5383 0.6415 0.0890  -0.0407 -0.0528 1590 ARG A CG    
2901 C  CD    . ARG A 373 ? 0.6696 0.6361 0.7376 0.0989  -0.0286 -0.0498 1590 ARG A CD    
2902 N  NE    . ARG A 373 ? 0.8245 0.8104 0.9161 0.1018  -0.0278 -0.0397 1590 ARG A NE    
2903 C  CZ    . ARG A 373 ? 0.7734 0.7594 0.8787 0.1070  -0.0265 -0.0352 1590 ARG A CZ    
2904 N  NH1   . ARG A 373 ? 0.7335 0.6999 0.8321 0.1102  -0.0244 -0.0396 1590 ARG A NH1   
2905 N  NH2   . ARG A 373 ? 0.6364 0.6422 0.7622 0.1088  -0.0278 -0.0259 1590 ARG A NH2   
2906 N  N     . ASP A 374 ? 0.9736 0.8778 1.0146 0.0865  -0.0427 -0.0727 1591 ASP A N     
2907 C  CA    . ASP A 374 ? 1.0247 0.9221 1.0779 0.0883  -0.0417 -0.0691 1591 ASP A CA    
2908 C  C     . ASP A 374 ? 1.0128 0.8884 1.0588 0.0964  -0.0322 -0.0741 1591 ASP A C     
2909 O  O     . ASP A 374 ? 0.9550 0.8309 1.0134 0.1045  -0.0258 -0.0675 1591 ASP A O     
2910 C  CB    . ASP A 374 ? 1.0659 0.9587 1.1212 0.0775  -0.0516 -0.0714 1591 ASP A CB    
2911 C  CG    . ASP A 374 ? 0.9952 0.8687 1.0334 0.0710  -0.0558 -0.0839 1591 ASP A CG    
2912 O  OD1   . ASP A 374 ? 0.9078 0.7699 0.9287 0.0744  -0.0519 -0.0917 1591 ASP A OD1   
2913 O  OD2   . ASP A 374 ? 0.8945 0.7646 0.9367 0.0621  -0.0634 -0.0861 1591 ASP A OD2   
2914 N  N     . ASN A 375 ? 1.1505 1.0069 1.1761 0.0945  -0.0313 -0.0858 1592 ASN A N     
2915 C  CA    . ASN A 375 ? 1.0926 0.9231 1.1067 0.1004  -0.0229 -0.0936 1592 ASN A CA    
2916 C  C     . ASN A 375 ? 1.0135 0.8408 1.0173 0.1111  -0.0106 -0.0957 1592 ASN A C     
2917 O  O     . ASN A 375 ? 1.1606 0.9725 1.1638 0.1202  0.0000  -0.0973 1592 ASN A O     
2918 C  CB    . ASN A 375 ? 1.0421 0.8518 1.0379 0.0911  -0.0298 -0.1067 1592 ASN A CB    
2919 C  CG    . ASN A 375 ? 1.2627 1.0659 1.2698 0.0831  -0.0369 -0.1061 1592 ASN A CG    
2920 O  OD1   . ASN A 375 ? 1.3948 1.2083 1.4211 0.0847  -0.0365 -0.0956 1592 ASN A OD1   
2921 N  ND2   . ASN A 375 ? 1.3488 1.1346 1.3440 0.0742  -0.0433 -0.1172 1592 ASN A ND2   
2922 N  N     . GLY A 376 ? 0.9023 0.7424 0.8974 0.1104  -0.0108 -0.0957 1593 GLY A N     
2923 C  CA    . GLY A 376 ? 0.7445 0.5756 0.7216 0.1180  0.0004  -0.1010 1593 GLY A CA    
2924 C  C     . GLY A 376 ? 1.0239 0.8296 0.9711 0.1139  -0.0014 -0.1156 1593 GLY A C     
2925 O  O     . GLY A 376 ? 1.0329 0.8290 0.9599 0.1197  0.0078  -0.1212 1593 GLY A O     
2926 N  N     . ALA A 377 ? 1.0370 0.8319 0.9805 0.1037  -0.0133 -0.1219 1594 ALA A N     
2927 C  CA    . ALA A 377 ? 1.0464 0.8166 0.9626 0.0984  -0.0174 -0.1367 1594 ALA A CA    
2928 C  C     . ALA A 377 ? 1.0031 0.7780 0.8965 0.0950  -0.0222 -0.1409 1594 ALA A C     
2929 O  O     . ALA A 377 ? 1.0993 0.8944 0.9999 0.0889  -0.0319 -0.1349 1594 ALA A O     
2930 C  CB    . ALA A 377 ? 0.9536 0.7169 0.8769 0.0868  -0.0304 -0.1407 1594 ALA A CB    
2931 N  N     . LYS A 378 ? 0.9827 0.7364 0.8467 0.0989  -0.0157 -0.1516 1595 LYS A N     
2932 C  CA    . LYS A 378 ? 0.9984 0.7517 0.8348 0.0973  -0.0186 -0.1562 1595 LYS A CA    
2933 C  C     . LYS A 378 ? 1.0957 0.8287 0.9073 0.0875  -0.0316 -0.1705 1595 LYS A C     
2934 O  O     . LYS A 378 ? 1.1325 0.8404 0.9340 0.0870  -0.0296 -0.1813 1595 LYS A O     
2935 C  CB    . LYS A 378 ? 1.0327 0.7771 0.8507 0.1094  -0.0005 -0.1575 1595 LYS A CB    
2936 C  CG    . LYS A 378 ? 1.0612 0.8305 0.9019 0.1177  0.0106  -0.1429 1595 LYS A CG    
2937 C  CD    . LYS A 378 ? 1.2023 0.9615 1.0316 0.1308  0.0313  -0.1441 1595 LYS A CD    
2938 C  CE    . LYS A 378 ? 1.2574 1.0209 1.0635 0.1333  0.0371  -0.1431 1595 LYS A CE    
2939 N  NZ    . LYS A 378 ? 1.2320 1.0243 1.0637 0.1381  0.0449  -0.1280 1595 LYS A NZ    
2940 N  N     . GLN A 379 ? 1.1651 0.9087 0.9664 0.0801  -0.0449 -0.1704 1596 GLN A N     
2941 C  CA    . GLN A 379 ? 1.0968 0.8272 0.8777 0.0697  -0.0608 -0.1823 1596 GLN A CA    
2942 C  C     . GLN A 379 ? 1.0306 0.7641 0.7830 0.0699  -0.0652 -0.1833 1596 GLN A C     
2943 O  O     . GLN A 379 ? 1.1643 0.9207 0.9269 0.0708  -0.0667 -0.1718 1596 GLN A O     
2944 C  CB    . GLN A 379 ? 1.0742 0.8193 0.8815 0.0583  -0.0770 -0.1789 1596 GLN A CB    
2945 C  CG    . GLN A 379 ? 1.1792 0.9192 0.9707 0.0473  -0.0955 -0.1882 1596 GLN A CG    
2946 C  CD    . GLN A 379 ? 1.2641 1.0161 1.0847 0.0363  -0.1092 -0.1859 1596 GLN A CD    
2947 O  OE1   . GLN A 379 ? 1.1960 0.9623 1.0466 0.0372  -0.1049 -0.1758 1596 GLN A OE1   
2948 N  NE2   . GLN A 379 ? 1.3382 1.0843 1.1498 0.0258  -0.1257 -0.1953 1596 GLN A NE2   
2949 N  N     . THR A 380 ? 1.1471 0.8564 0.8626 0.0693  -0.0668 -0.1967 1597 THR A N     
2950 C  CA    . THR A 380 ? 1.2682 0.9770 0.9511 0.0700  -0.0709 -0.1980 1597 THR A CA    
2951 C  C     . THR A 380 ? 1.3007 1.0144 0.9792 0.0578  -0.0946 -0.2022 1597 THR A C     
2952 O  O     . THR A 380 ? 1.3014 1.0002 0.9756 0.0495  -0.1057 -0.2141 1597 THR A O     
2953 C  CB    . THR A 380 ? 1.2272 0.9067 0.8689 0.0767  -0.0593 -0.2101 1597 THR A CB    
2954 O  OG1   . THR A 380 ? 1.2649 0.9444 0.9143 0.0891  -0.0364 -0.2040 1597 THR A OG1   
2955 C  CG2   . THR A 380 ? 1.1406 0.8172 0.7443 0.0766  -0.0651 -0.2120 1597 THR A CG2   
2956 N  N     . ILE A 381 ? 1.1690 0.9038 0.8504 0.0568  -0.1022 -0.1920 1598 ILE A N     
2957 C  CA    . ILE A 381 ? 1.1868 0.9314 0.8694 0.0466  -0.1245 -0.1930 1598 ILE A CA    
2958 C  C     . ILE A 381 ? 1.2588 0.9977 0.9021 0.0484  -0.1301 -0.1948 1598 ILE A C     
2959 O  O     . ILE A 381 ? 1.2361 0.9813 0.8691 0.0567  -0.1186 -0.1856 1598 ILE A O     
2960 C  CB    . ILE A 381 ? 1.1503 0.9251 0.8725 0.0436  -0.1300 -0.1786 1598 ILE A CB    
2961 C  CG1   . ILE A 381 ? 1.0417 0.8220 0.8007 0.0421  -0.1242 -0.1759 1598 ILE A CG1   
2962 C  CG2   . ILE A 381 ? 1.2209 1.0054 0.9446 0.0342  -0.1521 -0.1796 1598 ILE A CG2   
2963 C  CD1   . ILE A 381 ? 1.3248 1.0930 1.0908 0.0325  -0.1351 -0.1869 1598 ILE A CD1   
2964 N  N     . LYS A 382 ? 1.3167 1.0444 0.9389 0.0403  -0.1483 -0.2060 1599 LYS A N     
2965 C  CA    . LYS A 382 ? 1.2805 1.0054 0.8667 0.0406  -0.1586 -0.2067 1599 LYS A CA    
2966 C  C     . LYS A 382 ? 1.3113 1.0651 0.9201 0.0401  -0.1665 -0.1908 1599 LYS A C     
2967 O  O     . LYS A 382 ? 1.2566 1.0290 0.9036 0.0339  -0.1754 -0.1858 1599 LYS A O     
2968 C  CB    . LYS A 382 ? 1.1715 0.8806 0.7357 0.0307  -0.1793 -0.2222 1599 LYS A CB    
2969 N  N     . ARG A 383 ? 1.3664 1.1233 0.9527 0.0472  -0.1611 -0.1824 1600 ARG A N     
2970 C  CA    . ARG A 383 ? 1.2895 1.0720 0.8975 0.0481  -0.1651 -0.1664 1600 ARG A CA    
2971 C  C     . ARG A 383 ? 1.4283 1.2250 1.0538 0.0385  -0.1897 -0.1661 1600 ARG A C     
2972 O  O     . ARG A 383 ? 1.2827 1.1022 0.9439 0.0367  -0.1931 -0.1552 1600 ARG A O     
2973 C  CB    . ARG A 383 ? 1.2199 0.9990 0.7945 0.0561  -0.1576 -0.1588 1600 ARG A CB    
2974 C  CG    . ARG A 383 ? 1.3534 1.1565 0.9520 0.0586  -0.1559 -0.1414 1600 ARG A CG    
2975 C  CD    . ARG A 383 ? 1.3820 1.1853 0.9739 0.0683  -0.1328 -0.1317 1600 ARG A CD    
2976 N  NE    . ARG A 383 ? 1.3631 1.1886 0.9799 0.0693  -0.1325 -0.1158 1600 ARG A NE    
2977 C  CZ    . ARG A 383 ? 1.4973 1.3254 1.1041 0.0759  -0.1191 -0.1047 1600 ARG A CZ    
2978 N  NH1   . ARG A 383 ? 1.5190 1.3300 1.0915 0.0827  -0.1040 -0.1072 1600 ARG A NH1   
2979 N  NH2   . ARG A 383 ? 1.5705 1.4176 1.2016 0.0758  -0.1200 -0.0911 1600 ARG A NH2   
2980 N  N     . ALA A 384 ? 1.5001 1.2834 1.1013 0.0323  -0.2069 -0.1784 1601 ALA A N     
2981 C  CA    . ALA A 384 ? 1.3568 1.1537 0.9748 0.0229  -0.2315 -0.1792 1601 ALA A CA    
2982 C  C     . ALA A 384 ? 1.3949 1.2070 1.0627 0.0161  -0.2335 -0.1780 1601 ALA A C     
2983 O  O     . ALA A 384 ? 1.3152 1.1502 1.0143 0.0134  -0.2421 -0.1682 1601 ALA A O     
2984 C  CB    . ALA A 384 ? 1.2959 1.0734 0.8800 0.0166  -0.2484 -0.1950 1601 ALA A CB    
2985 N  N     . GLN A 385 ? 1.4494 1.2480 1.1244 0.0137  -0.2246 -0.1875 1602 GLN A N     
2986 C  CA    . GLN A 385 ? 1.4760 1.2854 1.1943 0.0069  -0.2259 -0.1873 1602 GLN A CA    
2987 C  C     . GLN A 385 ? 1.3040 1.1318 1.0555 0.0122  -0.2110 -0.1731 1602 GLN A C     
2988 O  O     . GLN A 385 ? 1.1781 1.0147 0.9645 0.0074  -0.2102 -0.1717 1602 GLN A O     
2989 C  CB    . GLN A 385 ? 1.7110 1.4975 1.4239 0.0033  -0.2204 -0.2014 1602 GLN A CB    
2990 C  CG    . GLN A 385 ? 2.0002 1.7682 1.6862 -0.0048 -0.2372 -0.2175 1602 GLN A CG    
2991 C  CD    . GLN A 385 ? 2.2406 1.9815 1.9165 -0.0067 -0.2282 -0.2317 1602 GLN A CD    
2992 O  OE1   . GLN A 385 ? 2.3239 2.0572 2.0035 0.0008  -0.2076 -0.2292 1602 GLN A OE1   
2993 N  NE2   . GLN A 385 ? 2.3103 2.0363 1.9743 -0.0169 -0.2438 -0.2467 1602 GLN A NE2   
2994 N  N     . ALA A 386 ? 1.2397 1.0731 0.9805 0.0214  -0.1997 -0.1628 1603 ALA A N     
2995 C  CA    . ALA A 386 ? 1.1801 1.0295 0.9495 0.0263  -0.1852 -0.1502 1603 ALA A CA    
2996 C  C     . ALA A 386 ? 1.2904 1.1616 1.0998 0.0201  -0.1946 -0.1434 1603 ALA A C     
2997 O  O     . ALA A 386 ? 1.2667 1.1432 1.1048 0.0180  -0.1881 -0.1419 1603 ALA A O     
2998 C  CB    . ALA A 386 ? 1.0740 0.9287 0.8272 0.0350  -0.1764 -0.1395 1603 ALA A CB    
2999 N  N     . THR A 387 ? 1.3803 1.2636 1.1911 0.0173  -0.2098 -0.1392 1604 THR A N     
3000 C  CA    . THR A 387 ? 1.3656 1.2706 1.2136 0.0127  -0.2175 -0.1317 1604 THR A CA    
3001 C  C     . THR A 387 ? 1.2772 1.1828 1.1522 0.0042  -0.2217 -0.1383 1604 THR A C     
3002 O  O     . THR A 387 ? 1.2874 1.2086 1.1961 0.0019  -0.2196 -0.1315 1604 THR A O     
3003 C  CB    . THR A 387 ? 1.4614 1.3757 1.3033 0.0109  -0.2356 -0.1287 1604 THR A CB    
3004 O  OG1   . THR A 387 ? 1.5766 1.5104 1.4563 0.0054  -0.2444 -0.1239 1604 THR A OG1   
3005 C  CG2   . THR A 387 ? 1.4587 1.3574 1.2717 0.0062  -0.2503 -0.1416 1604 THR A CG2   
3006 N  N     . VAL A 388 ? 1.1803 1.0679 1.0404 -0.0006 -0.2261 -0.1514 1605 VAL A N     
3007 C  CA    . VAL A 388 ? 1.1506 1.0380 1.0363 -0.0098 -0.2313 -0.1577 1605 VAL A CA    
3008 C  C     . VAL A 388 ? 1.2377 1.1119 1.1279 -0.0077 -0.2145 -0.1605 1605 VAL A C     
3009 O  O     . VAL A 388 ? 1.1973 1.0751 1.1157 -0.0128 -0.2122 -0.1601 1605 VAL A O     
3010 C  CB    . VAL A 388 ? 1.1870 1.0628 1.0580 -0.0184 -0.2489 -0.1711 1605 VAL A CB    
3011 C  CG1   . VAL A 388 ? 1.2454 1.1235 1.1481 -0.0290 -0.2543 -0.1761 1605 VAL A CG1   
3012 C  CG2   . VAL A 388 ? 1.1778 1.0653 1.0394 -0.0192 -0.2667 -0.1683 1605 VAL A CG2   
3013 N  N     . GLU A 389 ? 1.3362 1.1949 1.1988 0.0004  -0.2019 -0.1627 1606 GLU A N     
3014 C  CA    . GLU A 389 ? 1.2347 1.0798 1.1005 0.0034  -0.1863 -0.1655 1606 GLU A CA    
3015 C  C     . GLU A 389 ? 1.1621 1.0225 1.0528 0.0091  -0.1728 -0.1526 1606 GLU A C     
3016 O  O     . GLU A 389 ? 1.2409 1.0993 1.1516 0.0079  -0.1655 -0.1518 1606 GLU A O     
3017 C  CB    . GLU A 389 ? 1.2686 1.0917 1.0970 0.0106  -0.1771 -0.1728 1606 GLU A CB    
3018 C  CG    . GLU A 389 ? 1.4650 1.2649 1.2668 0.0049  -0.1866 -0.1888 1606 GLU A CG    
3019 C  CD    . GLU A 389 ? 1.5259 1.3131 1.3438 -0.0026 -0.1873 -0.1976 1606 GLU A CD    
3020 O  OE1   . GLU A 389 ? 1.5763 1.3639 1.4150 0.0006  -0.1740 -0.1925 1606 GLU A OE1   
3021 O  OE2   . GLU A 389 ? 1.4697 1.2461 1.2789 -0.0117 -0.2016 -0.2093 1606 GLU A OE2   
3022 N  N     . MET A 390 ? 1.0157 0.8910 0.9058 0.0146  -0.1700 -0.1424 1607 MET A N     
3023 C  CA    . MET A 390 ? 0.9952 0.8835 0.9043 0.0203  -0.1569 -0.1310 1607 MET A CA    
3024 C  C     . MET A 390 ? 1.1025 1.0057 1.0467 0.0149  -0.1593 -0.1253 1607 MET A C     
3025 O  O     . MET A 390 ? 1.2077 1.1141 1.1672 0.0180  -0.1482 -0.1200 1607 MET A O     
3026 C  CB    . MET A 390 ? 1.0070 0.9065 0.9069 0.0264  -0.1540 -0.1220 1607 MET A CB    
3027 C  CG    . MET A 390 ? 1.0349 0.9448 0.9496 0.0328  -0.1390 -0.1117 1607 MET A CG    
3028 S  SD    . MET A 390 ? 1.0970 0.9919 1.0048 0.0399  -0.1218 -0.1151 1607 MET A SD    
3029 C  CE    . MET A 390 ? 1.0764 0.9535 0.9427 0.0451  -0.1191 -0.1222 1607 MET A CE    
3030 N  N     . PRO A 391 ? 1.1140 1.0273 1.0722 0.0074  -0.1729 -0.1255 1608 PRO A N     
3031 C  CA    . PRO A 391 ? 1.0594 0.9843 1.0502 0.0023  -0.1729 -0.1209 1608 PRO A CA    
3032 C  C     . PRO A 391 ? 0.9892 0.9003 0.9874 -0.0014 -0.1687 -0.1271 1608 PRO A C     
3033 O  O     . PRO A 391 ? 0.9613 0.8756 0.9764 0.0000  -0.1592 -0.1215 1608 PRO A O     
3034 C  CB    . PRO A 391 ? 1.0260 0.9632 1.0281 -0.0044 -0.1885 -0.1210 1608 PRO A CB    
3035 C  CG    . PRO A 391 ? 0.9905 0.9291 0.9692 0.0001  -0.1941 -0.1198 1608 PRO A CG    
3036 C  CD    . PRO A 391 ? 1.1171 1.0359 1.0648 0.0049  -0.1873 -0.1266 1608 PRO A CD    
3037 N  N     . LYS A 392 ? 1.0380 0.9330 1.0230 -0.0063 -0.1758 -0.1385 1609 LYS A N     
3038 C  CA    . LYS A 392 ? 1.0923 0.9705 1.0818 -0.0095 -0.1706 -0.1448 1609 LYS A CA    
3039 C  C     . LYS A 392 ? 1.1492 1.0214 1.1366 -0.0005 -0.1538 -0.1397 1609 LYS A C     
3040 O  O     . LYS A 392 ? 1.1467 1.0208 1.1539 -0.0009 -0.1469 -0.1347 1609 LYS A O     
3041 C  CB    . LYS A 392 ? 1.0884 0.9455 1.0547 -0.0136 -0.1779 -0.1589 1609 LYS A CB    
3042 N  N     . LEU A 393 ? 1.1262 0.9929 1.0904 0.0081  -0.1472 -0.1400 1610 LEU A N     
3043 C  CA    . LEU A 393 ? 1.0580 0.9204 1.0209 0.0175  -0.1315 -0.1351 1610 LEU A CA    
3044 C  C     . LEU A 393 ? 1.0943 0.9752 1.0828 0.0191  -0.1262 -0.1229 1610 LEU A C     
3045 O  O     . LEU A 393 ? 0.9194 0.7962 0.9200 0.0212  -0.1182 -0.1197 1610 LEU A O     
3046 C  CB    . LEU A 393 ? 0.9794 0.8390 0.9176 0.0261  -0.1253 -0.1350 1610 LEU A CB    
3047 C  CG    . LEU A 393 ? 0.9884 0.8436 0.9254 0.0364  -0.1087 -0.1308 1610 LEU A CG    
3048 C  CD1   . LEU A 393 ? 0.8027 0.6358 0.7368 0.0376  -0.1023 -0.1382 1610 LEU A CD1   
3049 C  CD2   . LEU A 393 ? 1.0523 0.9065 0.9670 0.0446  -0.1014 -0.1299 1610 LEU A CD2   
3050 N  N     . LEU A 394 ? 1.0492 0.9495 1.0454 0.0183  -0.1310 -0.1158 1611 LEU A N     
3051 C  CA    . LEU A 394 ? 0.8675 0.7843 0.8851 0.0198  -0.1259 -0.1049 1611 LEU A CA    
3052 C  C     . LEU A 394 ? 0.7849 0.7024 0.8237 0.0132  -0.1279 -0.1041 1611 LEU A C     
3053 O  O     . LEU A 394 ? 0.8924 0.8118 0.9432 0.0157  -0.1201 -0.0981 1611 LEU A O     
3054 C  CB    . LEU A 394 ? 0.9029 0.8377 0.9237 0.0197  -0.1305 -0.0986 1611 LEU A CB    
3055 C  CG    . LEU A 394 ? 1.0068 0.9428 1.0096 0.0272  -0.1252 -0.0963 1611 LEU A CG    
3056 C  CD1   . LEU A 394 ? 0.9964 0.9429 0.9949 0.0255  -0.1335 -0.0937 1611 LEU A CD1   
3057 C  CD2   . LEU A 394 ? 0.9469 0.8910 0.9586 0.0337  -0.1133 -0.0879 1611 LEU A CD2   
3058 N  N     . GLU A 395 ? 0.8622 0.7769 0.9051 0.0047  -0.1381 -0.1103 1612 GLU A N     
3059 C  CA    . GLU A 395 ? 0.8946 0.8058 0.9561 -0.0022 -0.1389 -0.1110 1612 GLU A CA    
3060 C  C     . GLU A 395 ? 0.8400 0.7333 0.8982 0.0011  -0.1291 -0.1126 1612 GLU A C     
3061 O  O     . GLU A 395 ? 0.8112 0.7067 0.8827 0.0027  -0.1217 -0.1055 1612 GLU A O     
3062 C  CB    . GLU A 395 ? 0.9586 0.8667 1.0227 -0.0118 -0.1515 -0.1194 1612 GLU A CB    
3063 C  CG    . GLU A 395 ? 0.9340 0.8620 1.0096 -0.0157 -0.1616 -0.1160 1612 GLU A CG    
3064 C  CD    . GLU A 395 ? 0.8679 0.7953 0.9507 -0.0256 -0.1751 -0.1237 1612 GLU A CD    
3065 N  N     . THR A 396 ? 0.6919 0.5668 0.7306 0.0030  -0.1285 -0.1217 1613 THR A N     
3066 C  CA    . THR A 396 ? 0.9607 0.8165 0.9959 0.0070  -0.1189 -0.1237 1613 THR A CA    
3067 C  C     . THR A 396 ? 0.8280 0.6912 0.8689 0.0164  -0.1076 -0.1131 1613 THR A C     
3068 O  O     . THR A 396 ? 0.7863 0.6440 0.8384 0.0177  -0.1011 -0.1085 1613 THR A O     
3069 C  CB    . THR A 396 ? 1.1187 0.9538 1.1288 0.0096  -0.1183 -0.1351 1613 THR A CB    
3070 O  OG1   . THR A 396 ? 1.3436 1.1861 1.3366 0.0160  -0.1178 -0.1343 1613 THR A OG1   
3071 C  CG2   . THR A 396 ? 1.0649 0.8892 1.0705 -0.0012 -0.1302 -0.1467 1613 THR A CG2   
3072 N  N     . ILE A 397 ? 0.7433 0.6197 0.7776 0.0228  -0.1056 -0.1085 1614 ILE A N     
3073 C  CA    . ILE A 397 ? 0.8050 0.6879 0.8447 0.0317  -0.0954 -0.0994 1614 ILE A CA    
3074 C  C     . ILE A 397 ? 0.8929 0.7869 0.9534 0.0289  -0.0951 -0.0904 1614 ILE A C     
3075 O  O     . ILE A 397 ? 0.9917 0.8808 1.0591 0.0331  -0.0882 -0.0853 1614 ILE A O     
3076 C  CB    . ILE A 397 ? 0.8638 0.7601 0.8954 0.0377  -0.0934 -0.0957 1614 ILE A CB    
3077 C  CG1   . ILE A 397 ? 0.8902 0.7720 0.9001 0.0440  -0.0881 -0.1027 1614 ILE A CG1   
3078 C  CG2   . ILE A 397 ? 0.9278 0.8377 0.9722 0.0439  -0.0863 -0.0849 1614 ILE A CG2   
3079 C  CD1   . ILE A 397 ? 0.9740 0.8668 0.9726 0.0472  -0.0881 -0.1008 1614 ILE A CD1   
3080 N  N     . HIS A 398 ? 0.8763 0.7840 0.9463 0.0219  -0.1025 -0.0884 1615 HIS A N     
3081 C  CA    . HIS A 398 ? 0.8082 0.7255 0.8958 0.0189  -0.1016 -0.0805 1615 HIS A CA    
3082 C  C     . HIS A 398 ? 0.8544 0.7562 0.9482 0.0165  -0.0980 -0.0811 1615 HIS A C     
3083 O  O     . HIS A 398 ? 0.8308 0.7318 0.9306 0.0206  -0.0916 -0.0737 1615 HIS A O     
3084 C  CB    . HIS A 398 ? 0.7246 0.6554 0.8217 0.0113  -0.1095 -0.0803 1615 HIS A CB    
3085 C  CG    . HIS A 398 ? 0.6808 0.6212 0.7939 0.0085  -0.1073 -0.0725 1615 HIS A CG    
3086 N  ND1   . HIS A 398 ? 0.6696 0.6050 0.7946 0.0016  -0.1077 -0.0728 1615 HIS A ND1   
3087 C  CD2   . HIS A 398 ? 0.6773 0.6313 0.7955 0.0114  -0.1043 -0.0644 1615 HIS A CD2   
3088 C  CE1   . HIS A 398 ? 0.6637 0.6086 0.7990 0.0010  -0.1042 -0.0650 1615 HIS A CE1   
3089 N  NE2   . HIS A 398 ? 0.7460 0.7020 0.8767 0.0068  -0.1027 -0.0602 1615 HIS A NE2   
3090 N  N     . THR A 399 ? 0.7942 0.6825 0.8859 0.0099  -0.1024 -0.0899 1616 THR A N     
3091 C  CA    . THR A 399 ? 0.8925 0.7649 0.9915 0.0064  -0.0988 -0.0905 1616 THR A CA    
3092 C  C     . THR A 399 ? 0.8341 0.6939 0.9273 0.0159  -0.0891 -0.0868 1616 THR A C     
3093 O  O     . THR A 399 ? 0.8437 0.7017 0.9461 0.0176  -0.0836 -0.0788 1616 THR A O     
3094 C  CB    . THR A 399 ? 0.9049 0.7629 1.0012 -0.0022 -0.1053 -0.1021 1616 THR A CB    
3095 O  OG1   . THR A 399 ? 0.7808 0.6531 0.8816 -0.0093 -0.1156 -0.1052 1616 THR A OG1   
3096 C  CG2   . THR A 399 ? 0.6911 0.5359 0.8003 -0.0084 -0.1020 -0.1013 1616 THR A CG2   
3097 N  N     . SER A 400 ? 0.6616 0.5152 0.7399 0.0234  -0.0863 -0.0912 1617 SER A N     
3098 C  CA    . SER A 400 ? 0.8874 0.7287 0.9625 0.0331  -0.0766 -0.0879 1617 SER A CA    
3099 C  C     . SER A 400 ? 0.9618 0.8188 1.0475 0.0392  -0.0725 -0.0747 1617 SER A C     
3100 O  O     . SER A 400 ? 0.9648 0.8150 1.0582 0.0411  -0.0680 -0.0681 1617 SER A O     
3101 C  CB    . SER A 400 ? 0.8814 0.7161 0.9399 0.0411  -0.0729 -0.0939 1617 SER A CB    
3102 O  OG    . SER A 400 ? 1.0572 0.8785 1.1016 0.0356  -0.0778 -0.1066 1617 SER A OG    
3103 N  N     . MET A 401 ? 0.8928 0.7710 0.9795 0.0404  -0.0755 -0.0708 1618 MET A N     
3104 C  CA    . MET A 401 ? 0.5852 0.4798 0.6812 0.0446  -0.0736 -0.0595 1618 MET A CA    
3105 C  C     . MET A 401 ? 0.8485 0.7425 0.9550 0.0394  -0.0740 -0.0534 1618 MET A C     
3106 O  O     . MET A 401 ? 0.7262 0.6207 0.8374 0.0446  -0.0700 -0.0446 1618 MET A O     
3107 C  CB    . MET A 401 ? 0.8305 0.7463 0.9267 0.0433  -0.0780 -0.0579 1618 MET A CB    
3108 C  CG    . MET A 401 ? 0.8293 0.7486 0.9154 0.0489  -0.0764 -0.0615 1618 MET A CG    
3109 S  SD    . MET A 401 ? 0.9906 0.9354 1.0824 0.0506  -0.0778 -0.0539 1618 MET A SD    
3110 C  CE    . MET A 401 ? 1.0842 1.0280 1.1611 0.0534  -0.0768 -0.0607 1618 MET A CE    
3111 N  N     . TYR A 402 ? 0.7569 0.6503 0.8674 0.0294  -0.0789 -0.0576 1619 TYR A N     
3112 C  CA    . TYR A 402 ? 0.7459 0.6392 0.8666 0.0241  -0.0779 -0.0516 1619 TYR A CA    
3113 C  C     . TYR A 402 ? 0.7824 0.6547 0.9040 0.0254  -0.0721 -0.0500 1619 TYR A C     
3114 O  O     . TYR A 402 ? 0.7949 0.6661 0.9200 0.0287  -0.0677 -0.0404 1619 TYR A O     
3115 C  CB    . TYR A 402 ? 0.7979 0.6966 0.9258 0.0133  -0.0836 -0.0561 1619 TYR A CB    
3116 C  CG    . TYR A 402 ? 0.8604 0.7591 0.9990 0.0081  -0.0806 -0.0494 1619 TYR A CG    
3117 C  CD1   . TYR A 402 ? 0.7621 0.6753 0.9036 0.0093  -0.0792 -0.0410 1619 TYR A CD1   
3118 C  CD2   . TYR A 402 ? 0.9340 0.8170 1.0790 0.0018  -0.0783 -0.0516 1619 TYR A CD2   
3119 C  CE1   . TYR A 402 ? 0.8250 0.7369 0.9736 0.0051  -0.0752 -0.0348 1619 TYR A CE1   
3120 C  CE2   . TYR A 402 ? 0.9221 0.8044 1.0764 -0.0028 -0.0739 -0.0446 1619 TYR A CE2   
3121 C  CZ    . TYR A 402 ? 0.9278 0.8245 1.0829 -0.0008 -0.0721 -0.0362 1619 TYR A CZ    
3122 O  OH    . TYR A 402 ? 0.8934 0.7882 1.0552 -0.0050 -0.0666 -0.0294 1619 TYR A OH    
3123 N  N     . GLU A 403 ? 0.7238 0.5781 0.8414 0.0229  -0.0720 -0.0592 1620 GLU A N     
3124 C  CA    . GLU A 403 ? 1.0232 0.8558 1.1435 0.0224  -0.0663 -0.0577 1620 GLU A CA    
3125 C  C     . GLU A 403 ? 1.0316 0.8575 1.1482 0.0345  -0.0592 -0.0501 1620 GLU A C     
3126 O  O     . GLU A 403 ? 0.8734 0.6918 0.9945 0.0367  -0.0544 -0.0412 1620 GLU A O     
3127 C  CB    . GLU A 403 ? 1.1076 0.9207 1.2243 0.0161  -0.0681 -0.0701 1620 GLU A CB    
3128 C  CG    . GLU A 403 ? 1.1286 0.9483 1.2529 0.0033  -0.0759 -0.0766 1620 GLU A CG    
3129 C  CD    . GLU A 403 ? 1.2671 1.0688 1.3866 -0.0031 -0.0797 -0.0899 1620 GLU A CD    
3130 O  OE1   . GLU A 403 ? 1.3985 1.2009 1.5282 -0.0145 -0.0852 -0.0946 1620 GLU A OE1   
3131 O  OE2   . GLU A 403 ? 1.3655 1.1524 1.4713 0.0032  -0.0771 -0.0959 1620 GLU A OE2   
3132 N  N     . ARG A 404 ? 1.0523 0.8821 1.1611 0.0430  -0.0585 -0.0527 1621 ARG A N     
3133 C  CA    . ARG A 404 ? 0.9325 0.7626 1.0411 0.0554  -0.0527 -0.0443 1621 ARG A CA    
3134 C  C     . ARG A 404 ? 0.9320 0.7766 1.0481 0.0569  -0.0533 -0.0312 1621 ARG A C     
3135 O  O     . ARG A 404 ? 1.1036 0.9384 1.2226 0.0611  -0.0490 -0.0228 1621 ARG A O     
3136 C  CB    . ARG A 404 ? 1.0147 0.8555 1.1171 0.0624  -0.0527 -0.0479 1621 ARG A CB    
3137 C  CG    . ARG A 404 ? 1.2263 1.0546 1.3254 0.0740  -0.0449 -0.0478 1621 ARG A CG    
3138 C  CD    . ARG A 404 ? 1.3407 1.1819 1.4353 0.0808  -0.0436 -0.0500 1621 ARG A CD    
3139 N  NE    . ARG A 404 ? 1.5020 1.3262 1.5835 0.0811  -0.0406 -0.0625 1621 ARG A NE    
3140 C  CZ    . ARG A 404 ? 1.6046 1.4154 1.6816 0.0914  -0.0318 -0.0646 1621 ARG A CZ    
3141 N  NH1   . ARG A 404 ? 1.6352 1.4492 1.7227 0.1022  -0.0258 -0.0543 1621 ARG A NH1   
3142 N  NH2   . ARG A 404 ? 1.5820 1.3754 1.6441 0.0910  -0.0290 -0.0769 1621 ARG A NH2   
3143 N  N     . ALA A 405 ? 0.8769 0.7430 0.9949 0.0528  -0.0588 -0.0295 1622 ALA A N     
3144 C  CA    . ALA A 405 ? 0.8624 0.7417 0.9846 0.0541  -0.0597 -0.0182 1622 ALA A CA    
3145 C  C     . ALA A 405 ? 0.8306 0.6973 0.9555 0.0493  -0.0569 -0.0128 1622 ALA A C     
3146 O  O     . ALA A 405 ? 0.8601 0.7236 0.9850 0.0550  -0.0541 -0.0024 1622 ALA A O     
3147 C  CB    . ALA A 405 ? 0.8275 0.7290 0.9507 0.0490  -0.0656 -0.0190 1622 ALA A CB    
3148 N  N     . GLU A 406 ? 0.9081 0.7663 1.0355 0.0391  -0.0573 -0.0195 1623 GLU A N     
3149 C  CA    . GLU A 406 ? 1.0560 0.9023 1.1874 0.0339  -0.0533 -0.0141 1623 GLU A CA    
3150 C  C     . GLU A 406 ? 1.0927 0.9165 1.2225 0.0403  -0.0468 -0.0098 1623 GLU A C     
3151 O  O     . GLU A 406 ? 1.0150 0.8327 1.1447 0.0427  -0.0427 0.0011  1623 GLU A O     
3152 C  CB    . GLU A 406 ? 1.0763 0.9199 1.2144 0.0213  -0.0551 -0.0222 1623 GLU A CB    
3153 C  CG    . GLU A 406 ? 1.1852 1.0070 1.3255 0.0166  -0.0532 -0.0304 1623 GLU A CG    
3154 C  CD    . GLU A 406 ? 1.2296 1.0522 1.3803 0.0034  -0.0555 -0.0358 1623 GLU A CD    
3155 O  OE1   . GLU A 406 ? 1.1467 0.9759 1.3040 -0.0010 -0.0529 -0.0287 1623 GLU A OE1   
3156 O  OE2   . GLU A 406 ? 1.2739 1.0911 1.4259 -0.0023 -0.0600 -0.0473 1623 GLU A OE2   
3157 N  N     . ARG A 407 ? 1.0348 0.8452 1.1618 0.0440  -0.0454 -0.0177 1624 ARG A N     
3158 C  CA    . ARG A 407 ? 1.0783 0.8667 1.2040 0.0518  -0.0385 -0.0136 1624 ARG A CA    
3159 C  C     . ARG A 407 ? 1.1328 0.9293 1.2579 0.0633  -0.0369 0.0004  1624 ARG A C     
3160 O  O     . ARG A 407 ? 1.2747 1.0587 1.4004 0.0663  -0.0324 0.0105  1624 ARG A O     
3161 C  CB    . ARG A 407 ? 0.9937 0.7698 1.1145 0.0565  -0.0369 -0.0244 1624 ARG A CB    
3162 C  CG    . ARG A 407 ? 1.0240 0.7827 1.1437 0.0463  -0.0375 -0.0378 1624 ARG A CG    
3163 C  CD    . ARG A 407 ? 0.9931 0.7363 1.1042 0.0521  -0.0348 -0.0483 1624 ARG A CD    
3164 N  NE    . ARG A 407 ? 0.9612 0.7127 1.0655 0.0465  -0.0413 -0.0611 1624 ARG A NE    
3165 C  CZ    . ARG A 407 ? 1.0807 0.8312 1.1862 0.0335  -0.0476 -0.0703 1624 ARG A CZ    
3166 N  NH1   . ARG A 407 ? 1.0186 0.7607 1.1337 0.0239  -0.0475 -0.0686 1624 ARG A NH1   
3167 N  NH2   . ARG A 407 ? 1.1250 0.8832 1.2224 0.0303  -0.0540 -0.0807 1624 ARG A NH2   
3168 N  N     . ASP A 408 ? 1.0348 0.8528 1.1590 0.0693  -0.0412 0.0018  1625 ASP A N     
3169 C  CA    . ASP A 408 ? 1.0392 0.8672 1.1642 0.0797  -0.0415 0.0147  1625 ASP A CA    
3170 C  C     . ASP A 408 ? 0.9498 0.7814 1.0733 0.0757  -0.0427 0.0252  1625 ASP A C     
3171 O  O     . ASP A 408 ? 0.8695 0.6941 0.9918 0.0826  -0.0403 0.0370  1625 ASP A O     
3172 C  CB    . ASP A 408 ? 1.0076 0.8599 1.1341 0.0845  -0.0464 0.0137  1625 ASP A CB    
3173 C  CG    . ASP A 408 ? 0.9381 0.7991 1.0684 0.0973  -0.0467 0.0254  1625 ASP A CG    
3174 O  OD1   . ASP A 408 ? 0.8921 0.7370 1.0243 0.1062  -0.0414 0.0310  1625 ASP A OD1   
3175 O  OD2   . ASP A 408 ? 0.8479 0.7319 0.9801 0.0982  -0.0525 0.0292  1625 ASP A OD2   
3176 N  N     . LEU A 409 ? 0.8523 0.6940 0.9753 0.0648  -0.0458 0.0213  1626 LEU A N     
3177 C  CA    . LEU A 409 ? 0.7953 0.6401 0.9150 0.0607  -0.0456 0.0304  1626 LEU A CA    
3178 C  C     . LEU A 409 ? 0.9437 0.7642 1.0628 0.0598  -0.0383 0.0366  1626 LEU A C     
3179 O  O     . LEU A 409 ? 0.9958 0.8132 1.1096 0.0636  -0.0365 0.0490  1626 LEU A O     
3180 C  CB    . LEU A 409 ? 0.7553 0.6123 0.8764 0.0493  -0.0484 0.0239  1626 LEU A CB    
3181 C  CG    . LEU A 409 ? 0.7146 0.5723 0.8316 0.0445  -0.0460 0.0324  1626 LEU A CG    
3182 C  CD1   . LEU A 409 ? 0.6286 0.4964 0.7370 0.0526  -0.0491 0.0437  1626 LEU A CD1   
3183 C  CD2   . LEU A 409 ? 0.7276 0.5977 0.8478 0.0345  -0.0478 0.0259  1626 LEU A CD2   
3184 N  N     . GLN A 410 ? 1.0035 0.8057 1.1273 0.0549  -0.0342 0.0282  1627 GLN A N     
3185 C  CA    . GLN A 410 ? 1.0474 0.8256 1.1719 0.0527  -0.0266 0.0339  1627 GLN A CA    
3186 C  C     . GLN A 410 ? 1.0866 0.8501 1.2084 0.0655  -0.0228 0.0429  1627 GLN A C     
3187 O  O     . GLN A 410 ? 1.1178 0.8673 1.2366 0.0677  -0.0176 0.0545  1627 GLN A O     
3188 C  CB    . GLN A 410 ? 1.1918 0.9550 1.3234 0.0423  -0.0241 0.0215  1627 GLN A CB    
3189 C  CG    . GLN A 410 ? 1.3305 1.1062 1.4679 0.0289  -0.0267 0.0155  1627 GLN A CG    
3190 C  CD    . GLN A 410 ? 1.4163 1.1902 1.5601 0.0206  -0.0305 -0.0003 1627 GLN A CD    
3191 O  OE1   . GLN A 410 ? 1.4415 1.2068 1.5826 0.0249  -0.0318 -0.0080 1627 GLN A OE1   
3192 N  NE2   . GLN A 410 ? 1.4347 1.2168 1.5869 0.0089  -0.0323 -0.0049 1627 GLN A NE2   
3193 N  N     . SER A 411 ? 1.1714 0.9401 1.2940 0.0749  -0.0253 0.0393  1628 SER A N     
3194 C  CA    . SER A 411 ? 1.1513 0.9107 1.2735 0.0890  -0.0223 0.0488  1628 SER A CA    
3195 C  C     . SER A 411 ? 1.2547 1.0290 1.3729 0.0964  -0.0263 0.0640  1628 SER A C     
3196 O  O     . SER A 411 ? 1.3264 1.0924 1.4446 0.1079  -0.0242 0.0750  1628 SER A O     
3197 C  CB    . SER A 411 ? 1.1862 0.9500 1.3117 0.0970  -0.0231 0.0406  1628 SER A CB    
3198 O  OG    . SER A 411 ? 1.3763 1.1461 1.5040 0.1115  -0.0235 0.0518  1628 SER A OG    
3199 N  N     . HIS A 412 ? 1.2554 1.0510 1.3698 0.0903  -0.0323 0.0648  1629 HIS A N     
3200 C  CA    . HIS A 412 ? 1.2100 1.0208 1.3184 0.0961  -0.0376 0.0776  1629 HIS A CA    
3201 C  C     . HIS A 412 ? 1.1366 0.9454 1.2357 0.0877  -0.0362 0.0836  1629 HIS A C     
3202 O  O     . HIS A 412 ? 1.0559 0.8796 1.1468 0.0891  -0.0417 0.0912  1629 HIS A O     
3203 C  CB    . HIS A 412 ? 1.2443 1.0836 1.3551 0.0976  -0.0463 0.0733  1629 HIS A CB    
3204 C  CG    . HIS A 412 ? 1.2818 1.1271 1.4010 0.1090  -0.0477 0.0726  1629 HIS A CG    
3205 N  ND1   . HIS A 412 ? 1.2849 1.1428 1.4064 0.1201  -0.0527 0.0837  1629 HIS A ND1   
3206 C  CD2   . HIS A 412 ? 1.2567 1.0979 1.3829 0.1111  -0.0444 0.0622  1629 HIS A CD2   
3207 C  CE1   . HIS A 412 ? 1.2430 1.1049 1.3748 0.1288  -0.0516 0.0805  1629 HIS A CE1   
3208 N  NE2   . HIS A 412 ? 1.2679 1.1189 1.4013 0.1237  -0.0460 0.0673  1629 HIS A NE2   
3209 N  N     . THR A 413 ? 0.9619 0.7511 1.0619 0.0792  -0.0285 0.0810  1630 THR A N     
3210 C  CA    . THR A 413 ? 1.0591 0.8427 1.1512 0.0720  -0.0242 0.0882  1630 THR A CA    
3211 C  C     . THR A 413 ? 1.1089 0.8639 1.1995 0.0742  -0.0150 0.0976  1630 THR A C     
3212 O  O     . THR A 413 ? 1.1422 0.8791 1.2412 0.0682  -0.0085 0.0907  1630 THR A O     
3213 C  CB    . THR A 413 ? 0.9235 0.7129 1.0208 0.0579  -0.0227 0.0768  1630 THR A CB    
3214 O  OG1   . THR A 413 ? 1.0918 0.9057 1.1909 0.0567  -0.0310 0.0683  1630 THR A OG1   
3215 C  CG2   . THR A 413 ? 0.7547 0.5409 0.8441 0.0511  -0.0173 0.0846  1630 THR A CG2   
3216 N  N     . LYS A 414 ? 0.9871 0.7380 1.0663 0.0821  -0.0147 0.1133  1631 LYS A N     
3217 C  CA    . LYS A 414 ? 1.0424 0.7663 1.1180 0.0861  -0.0061 0.1252  1631 LYS A CA    
3218 C  C     . LYS A 414 ? 1.2507 0.9703 1.3131 0.0800  -0.0011 0.1353  1631 LYS A C     
3219 O  O     . LYS A 414 ? 1.3133 1.0509 1.3639 0.0802  -0.0069 0.1391  1631 LYS A O     
3220 C  CB    . LYS A 414 ? 0.8292 0.5505 0.9020 0.1026  -0.0100 0.1370  1631 LYS A CB    
3221 N  N     . LEU A 415 ? 1.2860 0.9808 1.3500 0.0742  0.0103  0.1392  1632 LEU A N     
3222 C  CA    . LEU A 415 ? 1.1310 0.8176 1.1826 0.0687  0.0182  0.1500  1632 LEU A CA    
3223 C  C     . LEU A 415 ? 1.1310 0.7944 1.1713 0.0785  0.0237  0.1685  1632 LEU A C     
3224 O  O     . LEU A 415 ? 1.1852 0.8288 1.2339 0.0839  0.0274  0.1701  1632 LEU A O     
3225 C  CB    . LEU A 415 ? 1.0925 0.7693 1.1563 0.0534  0.0282  0.1416  1632 LEU A CB    
3226 N  N     . THR A 416 ? 1.0911 0.7557 1.1110 0.0810  0.0244  0.1824  1633 THR A N     
3227 C  CA    . THR A 416 ? 1.2002 0.8421 1.2062 0.0894  0.0303  0.2017  1633 THR A CA    
3228 C  C     . THR A 416 ? 1.2376 0.8754 1.2245 0.0829  0.0381  0.2111  1633 THR A C     
3229 O  O     . THR A 416 ? 1.1815 0.8377 1.1641 0.0748  0.0364  0.2036  1633 THR A O     
3230 C  CB    . THR A 416 ? 1.2707 0.9208 1.2665 0.1060  0.0186  0.2128  1633 THR A CB    
3231 N  N     . LYS A 417 ? 1.3304 0.9428 1.3058 0.0866  0.0478  0.2278  1634 LYS A N     
3232 C  CA    . LYS A 417 ? 1.3351 0.9425 1.2856 0.0844  0.0543  0.2409  1634 LYS A CA    
3233 C  C     . LYS A 417 ? 1.4048 1.0079 1.3310 0.0993  0.0474  0.2598  1634 LYS A C     
3234 O  O     . LYS A 417 ? 1.4885 1.0863 1.3885 0.0997  0.0513  0.2725  1634 LYS A O     
3235 C  CB    . LYS A 417 ? 1.3441 0.9248 1.2986 0.0746  0.0733  0.2462  1634 LYS A CB    
3236 C  CG    . LYS A 417 ? 1.3088 0.8912 1.2914 0.0597  0.0802  0.2284  1634 LYS A CG    
3237 C  CD    . LYS A 417 ? 1.3133 0.8772 1.2975 0.0480  0.0986  0.2340  1634 LYS A CD    
3238 C  CE    . LYS A 417 ? 1.3507 0.9089 1.3668 0.0345  0.1053  0.2191  1634 LYS A CE    
3239 N  NZ    . LYS A 417 ? 1.3951 0.9302 1.4165 0.0242  0.1242  0.2271  1634 LYS A NZ    
3240 N  N     . GLN A 418 ? 1.3408 0.9464 1.2747 0.1118  0.0370  0.2619  1635 GLN A N     
3241 C  CA    . GLN A 418 ? 1.2782 0.8794 1.1938 0.1274  0.0293  0.2807  1635 GLN A CA    
3242 C  C     . GLN A 418 ? 1.2195 0.8525 1.1328 0.1344  0.0102  0.2759  1635 GLN A C     
3243 O  O     . GLN A 418 ? 1.2290 0.8799 1.1634 0.1327  0.0036  0.2600  1635 GLN A O     
3244 C  CB    . GLN A 418 ? 1.1876 0.7642 1.1163 0.1376  0.0339  0.2893  1635 GLN A CB    
3245 N  N     . TRP A 419 ? 1.2787 0.9182 1.1652 0.1415  0.0016  0.2897  1636 TRP A N     
3246 C  CA    . TRP A 419 ? 1.3389 1.0090 1.2191 0.1464  -0.0170 0.2864  1636 TRP A CA    
3247 C  C     . TRP A 419 ? 1.3713 1.0522 1.2713 0.1598  -0.0290 0.2875  1636 TRP A C     
3248 O  O     . TRP A 419 ? 1.3144 1.0225 1.2264 0.1602  -0.0412 0.2762  1636 TRP A O     
3249 C  CB    . TRP A 419 ? 1.3429 1.0117 1.1869 0.1505  -0.0222 0.3026  1636 TRP A CB    
3250 C  CG    . TRP A 419 ? 1.3482 1.0447 1.1797 0.1556  -0.0420 0.3026  1636 TRP A CG    
3251 C  CD1   . TRP A 419 ? 1.3536 1.0523 1.1652 0.1677  -0.0545 0.3195  1636 TRP A CD1   
3252 C  CD2   . TRP A 419 ? 1.4066 1.1316 1.2429 0.1478  -0.0517 0.2855  1636 TRP A CD2   
3253 N  NE1   . TRP A 419 ? 1.4142 1.1417 1.2193 0.1676  -0.0722 0.3133  1636 TRP A NE1   
3254 C  CE2   . TRP A 419 ? 1.3972 1.1406 1.2171 0.1553  -0.0702 0.2925  1636 TRP A CE2   
3255 C  CE3   . TRP A 419 ? 1.4334 1.1701 1.2868 0.1352  -0.0470 0.2653  1636 TRP A CE3   
3256 C  CZ2   . TRP A 419 ? 1.3650 1.1366 1.1855 0.1501  -0.0832 0.2795  1636 TRP A CZ2   
3257 C  CZ3   . TRP A 419 ? 1.3143 1.0787 1.1675 0.1310  -0.0596 0.2531  1636 TRP A CZ3   
3258 C  CH2   . TRP A 419 ? 1.2908 1.0718 1.1279 0.1381  -0.0770 0.2601  1636 TRP A CH2   
3259 N  N     . ALA A 420 ? 1.4441 1.1033 1.3483 0.1711  -0.0246 0.3015  1637 ALA A N     
3260 C  CA    . ALA A 420 ? 1.3785 1.0454 1.3032 0.1851  -0.0336 0.3037  1637 ALA A CA    
3261 C  C     . ALA A 420 ? 1.3254 0.9987 1.2802 0.1798  -0.0298 0.2835  1637 ALA A C     
3262 O  O     . ALA A 420 ? 1.3165 1.0127 1.2876 0.1853  -0.0405 0.2761  1637 ALA A O     
3263 C  CB    . ALA A 420 ? 1.4442 1.0824 1.3668 0.1980  -0.0271 0.3231  1637 ALA A CB    
3264 N  N     . GLU A 421 ? 1.3740 1.0270 1.3364 0.1688  -0.0146 0.2745  1638 GLU A N     
3265 C  CA    . GLU A 421 ? 1.2872 0.9453 1.2746 0.1625  -0.0115 0.2546  1638 GLU A CA    
3266 C  C     . GLU A 421 ? 1.3703 1.0593 1.3594 0.1529  -0.0202 0.2388  1638 GLU A C     
3267 O  O     . GLU A 421 ? 1.3864 1.0905 1.3944 0.1529  -0.0245 0.2249  1638 GLU A O     
3268 C  CB    . GLU A 421 ? 1.1538 0.7836 1.1481 0.1517  0.0054  0.2488  1638 GLU A CB    
3269 C  CG    . GLU A 421 ? 1.1151 0.7358 1.1339 0.1525  0.0099  0.2358  1638 GLU A CG    
3270 C  CD    . GLU A 421 ? 1.4106 1.0043 1.4368 0.1404  0.0249  0.2288  1638 GLU A CD    
3271 O  OE1   . GLU A 421 ? 1.5664 1.1325 1.6000 0.1458  0.0334  0.2335  1638 GLU A OE1   
3272 O  OE2   . GLU A 421 ? 1.5161 1.1160 1.5417 0.1253  0.0283  0.2186  1638 GLU A OE2   
3273 N  N     . PHE A 422 ? 1.5066 1.2047 1.4751 0.1456  -0.0226 0.2412  1639 PHE A N     
3274 C  CA    . PHE A 422 ? 1.4782 1.2055 1.4460 0.1378  -0.0317 0.2280  1639 PHE A CA    
3275 C  C     . PHE A 422 ? 1.4807 1.2336 1.4554 0.1481  -0.0478 0.2283  1639 PHE A C     
3276 O  O     . PHE A 422 ? 1.4184 1.1914 1.4089 0.1449  -0.0532 0.2137  1639 PHE A O     
3277 C  CB    . PHE A 422 ? 1.4665 1.1952 1.4076 0.1303  -0.0306 0.2330  1639 PHE A CB    
3278 C  CG    . PHE A 422 ? 1.3740 1.1301 1.3116 0.1222  -0.0393 0.2200  1639 PHE A CG    
3279 C  CD1   . PHE A 422 ? 1.3052 1.0638 1.2484 0.1082  -0.0314 0.2057  1639 PHE A CD1   
3280 C  CD2   . PHE A 422 ? 1.3770 1.1557 1.3062 0.1283  -0.0553 0.2228  1639 PHE A CD2   
3281 C  CE1   . PHE A 422 ? 1.3374 1.1189 1.2775 0.1014  -0.0384 0.1944  1639 PHE A CE1   
3282 C  CE2   . PHE A 422 ? 1.4179 1.2191 1.3439 0.1205  -0.0626 0.2109  1639 PHE A CE2   
3283 C  CZ    . PHE A 422 ? 1.4475 1.2493 1.3783 0.1073  -0.0536 0.1968  1639 PHE A CZ    
3284 N  N     . LEU A 423 ? 1.4086 1.1608 1.3733 0.1611  -0.0556 0.2454  1640 LEU A N     
3285 C  CA    . LEU A 423 ? 1.2618 1.0414 1.2333 0.1701  -0.0722 0.2468  1640 LEU A CA    
3286 C  C     . LEU A 423 ? 1.2776 1.0595 1.2773 0.1800  -0.0722 0.2434  1640 LEU A C     
3287 O  O     . LEU A 423 ? 1.2378 1.0451 1.2527 0.1825  -0.0819 0.2360  1640 LEU A O     
3288 C  CB    . LEU A 423 ? 1.1800 0.9601 1.1303 0.1803  -0.0822 0.2667  1640 LEU A CB    
3289 C  CG    . LEU A 423 ? 1.2273 1.0090 1.1460 0.1716  -0.0847 0.2695  1640 LEU A CG    
3290 C  CD1   . LEU A 423 ? 1.2486 1.0097 1.1413 0.1795  -0.0834 0.2910  1640 LEU A CD1   
3291 C  CD2   . LEU A 423 ? 1.1503 0.9642 1.0653 0.1694  -0.1018 0.2631  1640 LEU A CD2   
3292 N  N     . GLN A 424 ? 1.3724 1.1268 1.3799 0.1843  -0.0598 0.2472  1641 GLN A N     
3293 C  CA    . GLN A 424 ? 1.3759 1.1285 1.4094 0.1916  -0.0564 0.2405  1641 GLN A CA    
3294 C  C     . GLN A 424 ? 1.2899 1.0555 1.3369 0.1802  -0.0544 0.2186  1641 GLN A C     
3295 O  O     . GLN A 424 ? 1.1748 0.9631 1.2371 0.1840  -0.0617 0.2113  1641 GLN A O     
3296 C  CB    . GLN A 424 ? 1.2334 0.9499 1.2699 0.1963  -0.0421 0.2472  1641 GLN A CB    
3297 N  N     . PHE A 425 ? 1.2990 1.0520 1.3402 0.1658  -0.0449 0.2086  1642 PHE A N     
3298 C  CA    . PHE A 425 ? 1.3317 1.0968 1.3833 0.1542  -0.0437 0.1886  1642 PHE A CA    
3299 C  C     . PHE A 425 ? 1.3292 1.1280 1.3811 0.1522  -0.0566 0.1828  1642 PHE A C     
3300 O  O     . PHE A 425 ? 1.3034 1.1171 1.3701 0.1505  -0.0590 0.1699  1642 PHE A O     
3301 C  CB    . PHE A 425 ? 1.4139 1.1644 1.4574 0.1389  -0.0339 0.1819  1642 PHE A CB    
3302 C  CG    . PHE A 425 ? 1.5853 1.3034 1.6337 0.1377  -0.0204 0.1830  1642 PHE A CG    
3303 C  CD1   . PHE A 425 ? 1.6333 1.3366 1.6938 0.1488  -0.0170 0.1856  1642 PHE A CD1   
3304 C  CD2   . PHE A 425 ? 1.6621 1.3641 1.7039 0.1252  -0.0105 0.1813  1642 PHE A CD2   
3305 C  CE1   . PHE A 425 ? 1.6713 1.3429 1.7359 0.1469  -0.0045 0.1858  1642 PHE A CE1   
3306 C  CE2   . PHE A 425 ? 1.6939 1.3659 1.7417 0.1228  0.0017  0.1819  1642 PHE A CE2   
3307 C  CZ    . PHE A 425 ? 1.6907 1.3467 1.7492 0.1334  0.0045  0.1839  1642 PHE A CZ    
3308 N  N     . LEU A 426 ? 1.3051 1.1151 1.3395 0.1517  -0.0649 0.1918  1643 LEU A N     
3309 C  CA    . LEU A 426 ? 1.2757 1.1160 1.3104 0.1485  -0.0771 0.1854  1643 LEU A CA    
3310 C  C     . LEU A 426 ? 1.3824 1.2420 1.4338 0.1607  -0.0871 0.1885  1643 LEU A C     
3311 O  O     . LEU A 426 ? 1.2443 1.1264 1.3078 0.1579  -0.0928 0.1778  1643 LEU A O     
3312 C  CB    . LEU A 426 ? 1.2297 1.0752 1.2394 0.1448  -0.0836 0.1936  1643 LEU A CB    
3313 C  CG    . LEU A 426 ? 1.1427 1.0173 1.1492 0.1402  -0.0965 0.1870  1643 LEU A CG    
3314 C  CD1   . LEU A 426 ? 1.2124 1.0829 1.1939 0.1305  -0.0950 0.1874  1643 LEU A CD1   
3315 C  CD2   . LEU A 426 ? 1.1369 1.0298 1.1453 0.1514  -0.1115 0.1976  1643 LEU A CD2   
3316 N  N     . GLU A 427 ? 1.4578 1.3086 1.5120 0.1746  -0.0882 0.2032  1644 GLU A N     
3317 C  CA    . GLU A 427 ? 1.3231 1.1921 1.3968 0.1874  -0.0965 0.2074  1644 GLU A CA    
3318 C  C     . GLU A 427 ? 1.3416 1.2103 1.4383 0.1887  -0.0887 0.1943  1644 GLU A C     
3319 O  O     . GLU A 427 ? 1.2643 1.1562 1.3782 0.1930  -0.0949 0.1900  1644 GLU A O     
3320 C  CB    . GLU A 427 ? 1.2370 1.0939 1.3088 0.2027  -0.0984 0.2270  1644 GLU A CB    
3321 N  N     . THR A 428 ? 1.3330 1.1753 1.4298 0.1847  -0.0748 0.1876  1645 THR A N     
3322 C  CA    . THR A 428 ? 1.3070 1.1452 1.4212 0.1849  -0.0668 0.1740  1645 THR A CA    
3323 C  C     . THR A 428 ? 1.4064 1.2596 1.5222 0.1715  -0.0676 0.1563  1645 THR A C     
3324 O  O     . THR A 428 ? 1.4895 1.3337 1.6136 0.1684  -0.0595 0.1437  1645 THR A O     
3325 C  CB    . THR A 428 ? 1.2610 1.0642 1.3743 0.1849  -0.0527 0.1726  1645 THR A CB    
3326 O  OG1   . THR A 428 ? 1.3599 1.1528 1.4636 0.1690  -0.0469 0.1614  1645 THR A OG1   
3327 C  CG2   . THR A 428 ? 1.2309 1.0144 1.3361 0.1943  -0.0507 0.1910  1645 THR A CG2   
3328 N  N     . LYS A 429 ? 1.2976 1.1710 1.4042 0.1632  -0.0766 0.1548  1646 LYS A N     
3329 C  CA    . LYS A 429 ? 1.1882 1.0798 1.2984 0.1525  -0.0791 0.1397  1646 LYS A CA    
3330 C  C     . LYS A 429 ? 1.1651 1.0415 1.2694 0.1394  -0.0702 0.1271  1646 LYS A C     
3331 O  O     . LYS A 429 ? 1.2448 1.1230 1.3581 0.1353  -0.0666 0.1140  1646 LYS A O     
3332 C  CB    . LYS A 429 ? 1.1326 1.0400 1.2631 0.1593  -0.0802 0.1334  1646 LYS A CB    
3333 N  N     . ASN A 430 ? 1.0311 0.8927 1.1203 0.1327  -0.0667 0.1315  1647 ASN A N     
3334 C  CA    . ASN A 430 ? 1.0542 0.9062 1.1397 0.1191  -0.0598 0.1201  1647 ASN A CA    
3335 C  C     . ASN A 430 ? 1.1346 0.9840 1.2025 0.1116  -0.0598 0.1261  1647 ASN A C     
3336 O  O     . ASN A 430 ? 1.1529 1.0084 1.2093 0.1164  -0.0660 0.1378  1647 ASN A O     
3337 C  CB    . ASN A 430 ? 1.0807 0.9070 1.1731 0.1185  -0.0488 0.1151  1647 ASN A CB    
3338 C  CG    . ASN A 430 ? 1.1878 0.9902 1.2765 0.1266  -0.0430 0.1285  1647 ASN A CG    
3339 O  OD1   . ASN A 430 ? 1.2450 1.0500 1.3350 0.1393  -0.0469 0.1400  1647 ASN A OD1   
3340 N  ND2   . ASN A 430 ? 1.2396 1.0180 1.3255 0.1195  -0.0333 0.1270  1647 ASN A ND2   
3341 N  N     . ILE A 431 ? 1.0800 0.9218 1.1459 0.0994  -0.0531 0.1174  1648 ILE A N     
3342 C  CA    . ILE A 431 ? 1.2128 1.0541 1.2637 0.0909  -0.0514 0.1204  1648 ILE A CA    
3343 C  C     . ILE A 431 ? 1.3614 1.1765 1.4086 0.0869  -0.0396 0.1252  1648 ILE A C     
3344 O  O     . ILE A 431 ? 1.4133 1.2123 1.4720 0.0862  -0.0329 0.1209  1648 ILE A O     
3345 C  CB    . ILE A 431 ? 1.1596 1.0164 1.2129 0.0796  -0.0528 0.1071  1648 ILE A CB    
3346 C  CG1   . ILE A 431 ? 1.0546 0.9040 1.1231 0.0735  -0.0470 0.0944  1648 ILE A CG1   
3347 C  CG2   . ILE A 431 ? 1.1870 1.0691 1.2416 0.0823  -0.0641 0.1036  1648 ILE A CG2   
3348 C  CD1   . ILE A 431 ? 1.0023 0.8610 1.0734 0.0618  -0.0460 0.0835  1648 ILE A CD1   
3349 N  N     . ILE A 432 ? 1.2655 1.0755 1.2958 0.0838  -0.0367 0.1341  1649 ILE A N     
3350 C  CA    . ILE A 432 ? 1.2326 1.0170 1.2564 0.0829  -0.0256 0.1439  1649 ILE A CA    
3351 C  C     . ILE A 432 ? 1.0981 0.8796 1.1152 0.0706  -0.0174 0.1412  1649 ILE A C     
3352 O  O     . ILE A 432 ? 1.0302 0.8235 1.0323 0.0683  -0.0206 0.1431  1649 ILE A O     
3353 C  CB    . ILE A 432 ? 1.2888 1.0654 1.2963 0.0942  -0.0284 0.1621  1649 ILE A CB    
3354 C  CG1   . ILE A 432 ? 1.2233 1.0060 1.2405 0.1073  -0.0369 0.1652  1649 ILE A CG1   
3355 C  CG2   . ILE A 432 ? 1.4053 1.1531 1.4070 0.0934  -0.0157 0.1727  1649 ILE A CG2   
3356 C  CD1   . ILE A 432 ? 1.1874 0.9913 1.1946 0.1150  -0.0505 0.1721  1649 ILE A CD1   
3357 N  N     . MET A 433 ? 0.9175 0.6828 0.9458 0.0627  -0.0066 0.1370  1650 MET A N     
3358 C  CA    . MET A 433 ? 1.0557 0.8140 1.0787 0.0526  0.0039  0.1385  1650 MET A CA    
3359 C  C     . MET A 433 ? 1.1700 0.9047 1.1786 0.0563  0.0130  0.1554  1650 MET A C     
3360 O  O     . MET A 433 ? 1.2815 0.9966 1.2967 0.0605  0.0174  0.1607  1650 MET A O     
3361 C  CB    . MET A 433 ? 1.2230 0.9778 1.2673 0.0411  0.0104  0.1257  1650 MET A CB    
3362 C  CG    . MET A 433 ? 1.3595 1.1242 1.4026 0.0308  0.0156  0.1215  1650 MET A CG    
3363 S  SD    . MET A 433 ? 1.4248 1.1946 1.4953 0.0177  0.0187  0.1049  1650 MET A SD    
3364 C  CE    . MET A 433 ? 1.3586 1.1345 1.4414 0.0232  0.0068  0.0938  1650 MET A CE    
3365 N  N     . ALA A 434 ? 1.1243 0.8599 1.1116 0.0556  0.0159  0.1643  1651 ALA A N     
3366 C  CA    . ALA A 434 ? 1.0413 0.7554 1.0102 0.0597  0.0243  0.1817  1651 ALA A CA    
3367 C  C     . ALA A 434 ? 1.1310 0.8430 1.0859 0.0510  0.0350  0.1845  1651 ALA A C     
3368 O  O     . ALA A 434 ? 1.1330 0.8635 1.0865 0.0453  0.0322  0.1749  1651 ALA A O     
3369 C  CB    . ALA A 434 ? 0.9867 0.7034 0.9356 0.0733  0.0134  0.1946  1651 ALA A CB    
3370 N  N     . PRO A 435 ? 1.1843 0.8734 1.1284 0.0503  0.0482  0.1979  1652 PRO A N     
3371 C  CA    . PRO A 435 ? 1.2509 0.9371 1.1796 0.0429  0.0601  0.2017  1652 PRO A CA    
3372 C  C     . PRO A 435 ? 1.3056 1.0001 1.2006 0.0494  0.0529  0.2092  1652 PRO A C     
3373 O  O     . PRO A 435 ? 1.3209 1.0077 1.1961 0.0600  0.0466  0.2226  1652 PRO A O     
3374 C  CB    . PRO A 435 ? 1.2830 0.9401 1.2104 0.0414  0.0762  0.2153  1652 PRO A CB    
3375 C  CG    . PRO A 435 ? 1.2266 0.8711 1.1546 0.0523  0.0696  0.2237  1652 PRO A CG    
3376 C  CD    . PRO A 435 ? 1.2079 0.8711 1.1561 0.0549  0.0549  0.2091  1652 PRO A CD    
3377 N  N     . PHE A 436 ? 1.3456 1.0545 1.2335 0.0428  0.0544  0.2009  1653 PHE A N     
3378 C  CA    . PHE A 436 ? 1.2337 0.9538 1.0915 0.0470  0.0456  0.2031  1653 PHE A CA    
3379 C  C     . PHE A 436 ? 1.0668 0.7801 0.9048 0.0404  0.0606  0.2059  1653 PHE A C     
3380 O  O     . PHE A 436 ? 1.0546 0.7697 0.9110 0.0306  0.0728  0.1975  1653 PHE A O     
3381 C  CB    . PHE A 436 ? 1.1980 0.9450 1.0670 0.0462  0.0306  0.1873  1653 PHE A CB    
3382 C  CG    . PHE A 436 ? 1.2122 0.9708 1.0522 0.0490  0.0211  0.1874  1653 PHE A CG    
3383 C  CD1   . PHE A 436 ? 1.2570 1.0064 1.0646 0.0571  0.0163  0.2022  1653 PHE A CD1   
3384 C  CD2   . PHE A 436 ? 1.2057 0.9837 1.0503 0.0435  0.0162  0.1727  1653 PHE A CD2   
3385 C  CE1   . PHE A 436 ? 1.3394 1.0991 1.1191 0.0589  0.0063  0.2014  1653 PHE A CE1   
3386 C  CE2   . PHE A 436 ? 1.2008 0.9882 1.0186 0.0452  0.0072  0.1716  1653 PHE A CE2   
3387 C  CZ    . PHE A 436 ? 1.3074 1.0858 1.0924 0.0526  0.0019  0.1856  1653 PHE A CZ    
3388 N  N     . CYS A 437 ? 1.0858 0.7911 0.8861 0.0460  0.0598  0.2181  1654 CYS A N     
3389 C  CA    . CYS A 437 ? 1.2726 0.9693 1.0474 0.0411  0.0747  0.2219  1654 CYS A CA    
3390 C  C     . CYS A 437 ? 1.2919 1.0077 1.0673 0.0347  0.0732  0.2061  1654 CYS A C     
3391 O  O     . CYS A 437 ? 1.3813 1.0917 1.1454 0.0289  0.0886  0.2055  1654 CYS A O     
3392 C  CB    . CYS A 437 ? 1.4208 1.1039 1.1515 0.0495  0.0721  0.2386  1654 CYS A CB    
3393 S  SG    . CYS A 437 ? 1.5369 1.2393 1.2395 0.0558  0.0487  0.2340  1654 CYS A SG    
3394 N  N     . GLY A 438 ? 1.2635 1.0005 1.0487 0.0365  0.0554  0.1944  1655 GLY A N     
3395 C  CA    . GLY A 438 ? 1.1520 0.9068 0.9387 0.0312  0.0524  0.1794  1655 GLY A CA    
3396 C  C     . GLY A 438 ? 1.3253 1.0830 1.0730 0.0341  0.0448  0.1803  1655 GLY A C     
3397 O  O     . GLY A 438 ? 1.3448 1.1193 1.0944 0.0316  0.0362  0.1673  1655 GLY A O     
3398 N  N     . GLU A 439 ? 1.3720 1.1136 1.0838 0.0398  0.0461  0.1953  1656 GLU A N     
3399 C  CA    . GLU A 439 ? 1.3701 1.1126 1.0415 0.0415  0.0396  0.1954  1656 GLU A CA    
3400 C  C     . GLU A 439 ? 1.3726 1.1332 1.0429 0.0467  0.0145  0.1909  1656 GLU A C     
3401 O  O     . GLU A 439 ? 1.2878 1.0550 0.9799 0.0519  0.0031  0.1939  1656 GLU A O     
3402 C  CB    . GLU A 439 ? 1.3469 1.0664 0.9777 0.0460  0.0481  0.2131  1656 GLU A CB    
3403 C  CG    . GLU A 439 ? 1.5198 1.2205 1.1547 0.0408  0.0745  0.2193  1656 GLU A CG    
3404 C  CD    . GLU A 439 ? 1.7763 1.4742 1.3938 0.0339  0.0908  0.2119  1656 GLU A CD    
3405 O  OE1   . GLU A 439 ? 1.8429 1.5233 1.4530 0.0309  0.1130  0.2199  1656 GLU A OE1   
3406 O  OE2   . GLU A 439 ? 1.8911 1.6036 1.5034 0.0315  0.0825  0.1980  1656 GLU A OE2   
3407 N  N     . ILE A 440 ? 1.4399 1.2084 1.0854 0.0450  0.0065  0.1833  1657 ILE A N     
3408 C  CA    . ILE A 440 ? 1.3941 1.1831 1.0442 0.0472  -0.0165 0.1755  1657 ILE A CA    
3409 C  C     . ILE A 440 ? 1.4011 1.1890 1.0334 0.0569  -0.0334 0.1895  1657 ILE A C     
3410 O  O     . ILE A 440 ? 1.3730 1.1758 1.0286 0.0615  -0.0489 0.1890  1657 ILE A O     
3411 C  CB    . ILE A 440 ? 1.4259 1.2219 1.0552 0.0415  -0.0193 0.1624  1657 ILE A CB    
3412 C  CG1   . ILE A 440 ? 1.5294 1.3288 1.1825 0.0331  -0.0035 0.1486  1657 ILE A CG1   
3413 C  CG2   . ILE A 440 ? 1.3689 1.1855 1.0019 0.0432  -0.0435 0.1552  1657 ILE A CG2   
3414 C  CD1   . ILE A 440 ? 1.6602 1.4403 1.2954 0.0294  0.0206  0.1524  1657 ILE A CD1   
3415 N  N     . SER A 441 ? 1.3902 1.1610 0.9809 0.0605  -0.0307 0.2025  1658 SER A N     
3416 C  CA    . SER A 441 ? 1.3171 1.0847 0.8904 0.0707  -0.0455 0.2186  1658 SER A CA    
3417 C  C     . SER A 441 ? 1.3330 1.1018 0.9418 0.0771  -0.0473 0.2264  1658 SER A C     
3418 O  O     . SER A 441 ? 1.4505 1.2311 1.0674 0.0848  -0.0659 0.2314  1658 SER A O     
3419 C  CB    . SER A 441 ? 1.3335 1.0769 0.8598 0.0737  -0.0366 0.2340  1658 SER A CB    
3420 O  OG    . SER A 441 ? 1.4227 1.1459 0.9520 0.0707  -0.0114 0.2397  1658 SER A OG    
3421 N  N     . CYS A 442 ? 1.2614 1.0176 0.8917 0.0743  -0.0282 0.2278  1659 CYS A N     
3422 C  CA    . CYS A 442 ? 1.4130 1.1658 1.0713 0.0809  -0.0294 0.2364  1659 CYS A CA    
3423 C  C     . CYS A 442 ? 1.3952 1.1705 1.0934 0.0806  -0.0409 0.2233  1659 CYS A C     
3424 O  O     . CYS A 442 ? 1.3019 1.0821 1.0167 0.0889  -0.0515 0.2294  1659 CYS A O     
3425 C  CB    . CYS A 442 ? 1.5149 1.2463 1.1847 0.0774  -0.0063 0.2417  1659 CYS A CB    
3426 S  SG    . CYS A 442 ? 1.5535 1.2812 1.2643 0.0832  -0.0068 0.2465  1659 CYS A SG    
3427 N  N     . GLU A 443 ? 1.5448 1.3340 1.2580 0.0716  -0.0389 0.2057  1660 GLU A N     
3428 C  CA    . GLU A 443 ? 1.5493 1.3608 1.2953 0.0713  -0.0511 0.1933  1660 GLU A CA    
3429 C  C     . GLU A 443 ? 1.5745 1.4027 1.3113 0.0779  -0.0736 0.1957  1660 GLU A C     
3430 O  O     . GLU A 443 ? 1.5065 1.3487 1.2692 0.0829  -0.0848 0.1942  1660 GLU A O     
3431 C  CB    . GLU A 443 ? 1.5006 1.3226 1.2590 0.0607  -0.0450 0.1754  1660 GLU A CB    
3432 C  CG    . GLU A 443 ? 1.4931 1.3344 1.2883 0.0592  -0.0527 0.1626  1660 GLU A CG    
3433 C  CD    . GLU A 443 ? 1.3199 1.1677 1.1310 0.0493  -0.0434 0.1470  1660 GLU A CD    
3434 O  OE1   . GLU A 443 ? 1.1670 1.0330 0.9977 0.0473  -0.0524 0.1353  1660 GLU A OE1   
3435 O  OE2   . GLU A 443 ? 1.3084 1.1432 1.1140 0.0438  -0.0268 0.1470  1660 GLU A OE2   
3436 N  N     . ASP A 444 ? 1.6560 1.4830 1.3562 0.0778  -0.0804 0.1990  1661 ASP A N     
3437 C  CA    . ASP A 444 ? 1.6403 1.4827 1.3296 0.0836  -0.1030 0.2025  1661 ASP A CA    
3438 C  C     . ASP A 444 ? 1.5990 1.4372 1.2916 0.0959  -0.1109 0.2200  1661 ASP A C     
3439 O  O     . ASP A 444 ? 1.5221 1.3784 1.2344 0.1019  -0.1270 0.2206  1661 ASP A O     
3440 C  CB    . ASP A 444 ? 1.6827 1.5209 1.3275 0.0805  -0.1079 0.2030  1661 ASP A CB    
3441 C  CG    . ASP A 444 ? 1.7147 1.5599 1.3569 0.0692  -0.1035 0.1845  1661 ASP A CG    
3442 O  OD1   . ASP A 444 ? 1.7945 1.6244 1.4081 0.0642  -0.0905 0.1832  1661 ASP A OD1   
3443 O  OD2   . ASP A 444 ? 1.6994 1.5646 1.3674 0.0657  -0.1123 0.1716  1661 ASP A OD2   
3444 N  N     . ARG A 445 ? 1.6089 1.4231 1.2826 0.1002  -0.0992 0.2350  1662 ARG A N     
3445 C  CA    . ARG A 445 ? 1.5499 1.3571 1.2255 0.1127  -0.1053 0.2531  1662 ARG A CA    
3446 C  C     . ARG A 445 ? 1.5541 1.3666 1.2738 0.1167  -0.1032 0.2505  1662 ARG A C     
3447 O  O     . ARG A 445 ? 1.6631 1.4838 1.3966 0.1271  -0.1157 0.2588  1662 ARG A O     
3448 C  CB    . ARG A 445 ? 1.4223 1.2000 1.0693 0.1156  -0.0905 0.2695  1662 ARG A CB    
3449 N  N     . ILE A 446 ? 1.4042 1.2126 1.1466 0.1085  -0.0877 0.2386  1663 ILE A N     
3450 C  CA    . ILE A 446 ? 1.3025 1.1151 1.0848 0.1108  -0.0850 0.2335  1663 ILE A CA    
3451 C  C     . ILE A 446 ? 1.3955 1.2361 1.1994 0.1132  -0.1025 0.2244  1663 ILE A C     
3452 O  O     . ILE A 446 ? 1.4222 1.2689 1.2467 0.1227  -0.1098 0.2297  1663 ILE A O     
3453 C  CB    . ILE A 446 ? 1.2461 1.0510 1.0453 0.0998  -0.0669 0.2208  1663 ILE A CB    
3454 C  CG1   . ILE A 446 ? 1.3744 1.1508 1.1625 0.0987  -0.0484 0.2316  1663 ILE A CG1   
3455 C  CG2   . ILE A 446 ? 0.9529 0.7691 0.7917 0.0994  -0.0679 0.2091  1663 ILE A CG2   
3456 C  CD1   . ILE A 446 ? 1.3740 1.1446 1.1753 0.0866  -0.0313 0.2196  1663 ILE A CD1   
3457 N  N     . LYS A 447 ? 1.5008 1.3582 1.3000 0.1049  -0.1086 0.2110  1664 LYS A N     
3458 C  CA    . LYS A 447 ? 1.5818 1.4662 1.4019 0.1055  -0.1241 0.2015  1664 LYS A CA    
3459 C  C     . LYS A 447 ? 1.6051 1.5012 1.4198 0.1162  -0.1430 0.2137  1664 LYS A C     
3460 O  O     . LYS A 447 ? 1.6363 1.5484 1.4785 0.1226  -0.1521 0.2135  1664 LYS A O     
3461 C  CB    . LYS A 447 ? 1.5289 1.4250 1.3396 0.0942  -0.1262 0.1865  1664 LYS A CB    
3462 C  CG    . LYS A 447 ? 1.3914 1.3139 1.2256 0.0921  -0.1390 0.1745  1664 LYS A CG    
3463 C  CD    . LYS A 447 ? 1.3438 1.2760 1.1571 0.0838  -0.1468 0.1655  1664 LYS A CD    
3464 C  CE    . LYS A 447 ? 1.3126 1.2660 1.1510 0.0778  -0.1523 0.1500  1664 LYS A CE    
3465 N  NZ    . LYS A 447 ? 1.2605 1.2148 1.0818 0.0670  -0.1504 0.1378  1664 LYS A NZ    
3466 N  N     . ALA A 448 ? 1.5857 1.4750 1.3650 0.1182  -0.1494 0.2242  1665 ALA A N     
3467 C  CA    . ALA A 448 ? 1.4694 1.3706 1.2419 0.1282  -0.1692 0.2365  1665 ALA A CA    
3468 C  C     . ALA A 448 ? 1.5093 1.4036 1.3007 0.1415  -0.1682 0.2510  1665 ALA A C     
3469 O  O     . ALA A 448 ? 1.5513 1.4640 1.3637 0.1501  -0.1823 0.2552  1665 ALA A O     
3470 C  CB    . ALA A 448 ? 1.3685 1.2592 1.0949 0.1278  -0.1747 0.2459  1665 ALA A CB    
3471 N  N     . GLU A 449 ? 1.4712 1.3390 1.2575 0.1433  -0.1508 0.2585  1666 GLU A N     
3472 C  CA    . GLU A 449 ? 1.4150 1.2708 1.2124 0.1565  -0.1490 0.2745  1666 GLU A CA    
3473 C  C     . GLU A 449 ? 1.3470 1.2054 1.1857 0.1591  -0.1415 0.2672  1666 GLU A C     
3474 O  O     . GLU A 449 ? 1.3246 1.1695 1.1744 0.1696  -0.1368 0.2788  1666 GLU A O     
3475 C  CB    . GLU A 449 ? 1.3355 1.1594 1.1049 0.1574  -0.1342 0.2877  1666 GLU A CB    
3476 C  CG    . GLU A 449 ? 1.3018 1.1225 1.0272 0.1570  -0.1428 0.2969  1666 GLU A CG    
3477 C  CD    . GLU A 449 ? 1.4063 1.1956 1.1017 0.1594  -0.1289 0.3127  1666 GLU A CD    
3478 O  OE1   . GLU A 449 ? 1.4612 1.2330 1.1711 0.1663  -0.1186 0.3225  1666 GLU A OE1   
3479 O  OE2   . GLU A 449 ? 1.4751 1.2562 1.1315 0.1550  -0.1283 0.3159  1666 GLU A OE2   
3480 N  N     . SER A 450 ? 1.2582 1.1329 1.1186 0.1505  -0.1406 0.2487  1667 SER A N     
3481 C  CA    . SER A 450 ? 1.2619 1.1427 1.1597 0.1540  -0.1366 0.2415  1667 SER A CA    
3482 C  C     . SER A 450 ? 1.3573 1.2686 1.2771 0.1587  -0.1532 0.2375  1667 SER A C     
3483 O  O     . SER A 450 ? 0.8706 0.7907 0.8206 0.1600  -0.1502 0.2288  1667 SER A O     
3484 C  CB    . SER A 450 ? 1.3021 1.1766 1.2115 0.1419  -0.1216 0.2246  1667 SER A CB    
3485 O  OG    . SER A 450 ? 1.4684 1.3492 1.3602 0.1299  -0.1219 0.2148  1667 SER A OG    
3486 N  N     . ALA A 451 ? 1.4014 1.3291 1.3060 0.1604  -0.1705 0.2432  1668 ALA A N     
3487 C  CA    . ALA A 451 ? 1.4246 1.3831 1.3498 0.1641  -0.1877 0.2406  1668 ALA A CA    
3488 C  C     . ALA A 451 ? 1.4354 1.3982 1.3804 0.1807  -0.1943 0.2556  1668 ALA A C     
3489 O  O     . ALA A 451 ? 1.4180 1.4046 1.3918 0.1855  -0.2032 0.2531  1668 ALA A O     
3490 C  CB    . ALA A 451 ? 1.3866 1.3600 1.2873 0.1585  -0.2043 0.2404  1668 ALA A CB    
3491 N  N     . GLY A 465 ? 1.0675 1.0406 1.0269 0.1311  -0.1645 0.1880  1682 GLY A N     
3492 C  CA    . GLY A 465 ? 1.2329 1.1859 1.1631 0.1233  -0.1552 0.1879  1682 GLY A CA    
3493 C  C     . GLY A 465 ? 1.3739 1.3139 1.3122 0.1148  -0.1380 0.1760  1682 GLY A C     
3494 O  O     . GLY A 465 ? 1.4994 1.4496 1.4616 0.1120  -0.1358 0.1645  1682 GLY A O     
3495 N  N     . ALA A 466 ? 1.3103 1.2279 1.2293 0.1105  -0.1257 0.1789  1683 ALA A N     
3496 C  CA    . ALA A 466 ? 1.1457 1.0505 1.0743 0.1027  -0.1096 0.1691  1683 ALA A CA    
3497 C  C     . ALA A 466 ? 1.1658 1.0651 1.0735 0.0916  -0.1029 0.1630  1683 ALA A C     
3498 O  O     . ALA A 466 ? 1.1574 1.0436 1.0382 0.0917  -0.1001 0.1723  1683 ALA A O     
3499 C  CB    . ALA A 466 ? 1.0593 0.9400 0.9917 0.1079  -0.0975 0.1782  1683 ALA A CB    
3500 N  N     . LYS A 467 ? 1.1647 1.0725 1.0846 0.0825  -0.0990 0.1479  1684 LYS A N     
3501 C  CA    . LYS A 467 ? 1.0862 0.9896 0.9911 0.0722  -0.0911 0.1407  1684 LYS A CA    
3502 C  C     . LYS A 467 ? 1.1295 1.0183 1.0464 0.0666  -0.0746 0.1361  1684 LYS A C     
3503 O  O     . LYS A 467 ? 0.9013 0.7871 0.8407 0.0687  -0.0713 0.1340  1684 LYS A O     
3504 C  CB    . LYS A 467 ? 0.8812 0.8048 0.7912 0.0659  -0.0989 0.1272  1684 LYS A CB    
3505 N  N     . SER A 468 ? 1.3712 1.2509 1.2733 0.0592  -0.0644 0.1342  1685 SER A N     
3506 C  CA    . SER A 468 ? 1.3859 1.2588 1.3037 0.0515  -0.0507 0.1263  1685 SER A CA    
3507 C  C     . SER A 468 ? 1.2914 1.1813 1.2331 0.0473  -0.0550 0.1115  1685 SER A C     
3508 O  O     . SER A 468 ? 1.3484 1.2549 1.2887 0.0468  -0.0653 0.1053  1685 SER A O     
3509 C  CB    . SER A 468 ? 1.4353 1.2993 1.3344 0.0444  -0.0391 0.1259  1685 SER A CB    
3510 O  OG    . SER A 468 ? 1.6111 1.4806 1.5286 0.0362  -0.0320 0.1135  1685 SER A OG    
3511 N  N     . LEU A 469 ? 1.0359 0.9210 0.9995 0.0441  -0.0475 0.1061  1686 LEU A N     
3512 C  CA    . LEU A 469 ? 0.8756 0.7736 0.8602 0.0390  -0.0490 0.0924  1686 LEU A CA    
3513 C  C     . LEU A 469 ? 0.8827 0.7776 0.8714 0.0296  -0.0379 0.0856  1686 LEU A C     
3514 O  O     . LEU A 469 ? 0.8845 0.7900 0.8698 0.0252  -0.0390 0.0784  1686 LEU A O     
3515 C  CB    . LEU A 469 ? 0.8345 0.7304 0.8414 0.0421  -0.0499 0.0897  1686 LEU A CB    
3516 C  CG    . LEU A 469 ? 0.8888 0.7937 0.8998 0.0512  -0.0612 0.0924  1686 LEU A CG    
3517 C  CD1   . LEU A 469 ? 0.9025 0.7998 0.8980 0.0594  -0.0643 0.1065  1686 LEU A CD1   
3518 C  CD2   . LEU A 469 ? 0.8841 0.7856 0.9158 0.0531  -0.0596 0.0874  1686 LEU A CD2   
3519 N  N     . CYS A 470 ? 0.9072 0.7874 0.9036 0.0266  -0.0266 0.0884  1687 CYS A N     
3520 C  CA    . CYS A 470 ? 0.9224 0.7989 0.9230 0.0182  -0.0147 0.0847  1687 CYS A CA    
3521 C  C     . CYS A 470 ? 1.0466 0.9033 1.0475 0.0168  -0.0025 0.0936  1687 CYS A C     
3522 O  O     . CYS A 470 ? 1.0757 0.9214 1.0793 0.0215  -0.0035 0.1000  1687 CYS A O     
3523 C  CB    . CYS A 470 ? 0.8712 0.7584 0.8969 0.0123  -0.0152 0.0719  1687 CYS A CB    
3524 S  SG    . CYS A 470 ? 0.9141 0.7962 0.9629 0.0135  -0.0180 0.0687  1687 CYS A SG    
3525 N  N     . ILE A 471 ? 1.0917 0.9437 1.0915 0.0101  0.0100  0.0938  1688 ILE A N     
3526 C  CA    . ILE A 471 ? 0.9569 0.7922 0.9648 0.0059  0.0236  0.0996  1688 ILE A CA    
3527 C  C     . ILE A 471 ? 0.9913 0.8328 1.0309 -0.0010 0.0243  0.0886  1688 ILE A C     
3528 O  O     . ILE A 471 ? 1.0896 0.9416 1.1406 -0.0072 0.0281  0.0809  1688 ILE A O     
3529 C  CB    . ILE A 471 ? 0.9370 0.7654 0.9295 0.0020  0.0376  0.1052  1688 ILE A CB    
3530 C  CG1   . ILE A 471 ? 0.9154 0.7424 0.8731 0.0086  0.0329  0.1126  1688 ILE A CG1   
3531 C  CG2   . ILE A 471 ? 0.8035 0.6133 0.8034 -0.0019 0.0522  0.1135  1688 ILE A CG2   
3532 C  CD1   . ILE A 471 ? 0.7900 0.6162 0.7299 0.0050  0.0433  0.1129  1688 ILE A CD1   
3533 N  N     . PRO A 472 ? 1.0459 0.8812 1.1000 0.0002  0.0203  0.0873  1689 PRO A N     
3534 C  CA    . PRO A 472 ? 0.9231 0.7665 1.0042 -0.0056 0.0170  0.0751  1689 PRO A CA    
3535 C  C     . PRO A 472 ? 0.9877 0.8290 1.0867 -0.0157 0.0288  0.0729  1689 PRO A C     
3536 O  O     . PRO A 472 ? 0.9726 0.7996 1.0685 -0.0185 0.0411  0.0816  1689 PRO A O     
3537 C  CB    . PRO A 472 ? 0.8135 0.6448 0.9011 -0.0019 0.0128  0.0761  1689 PRO A CB    
3538 C  CG    . PRO A 472 ? 0.9590 0.7810 1.0239 0.0079  0.0110  0.0882  1689 PRO A CG    
3539 C  CD    . PRO A 472 ? 1.0886 0.9078 1.1346 0.0070  0.0192  0.0970  1689 PRO A CD    
3540 N  N     . PHE A 473 ? 1.0132 0.8698 1.1315 -0.0210 0.0249  0.0615  1690 PHE A N     
3541 C  CA    . PHE A 473 ? 0.9383 0.7965 1.0796 -0.0308 0.0339  0.0581  1690 PHE A CA    
3542 C  C     . PHE A 473 ? 0.9756 0.8189 1.1335 -0.0357 0.0373  0.0588  1690 PHE A C     
3543 O  O     . PHE A 473 ? 0.9503 0.7838 1.1171 -0.0419 0.0499  0.0642  1690 PHE A O     
3544 C  CB    . PHE A 473 ? 0.9190 0.7973 1.0777 -0.0340 0.0263  0.0460  1690 PHE A CB    
3545 C  CG    . PHE A 473 ? 0.8990 0.7902 1.0471 -0.0319 0.0272  0.0450  1690 PHE A CG    
3546 C  CD1   . PHE A 473 ? 0.9788 0.8632 1.1045 -0.0291 0.0362  0.0538  1690 PHE A CD1   
3547 C  CD2   . PHE A 473 ? 0.8777 0.7865 1.0368 -0.0327 0.0193  0.0354  1690 PHE A CD2   
3548 C  CE1   . PHE A 473 ? 1.0162 0.9107 1.1306 -0.0275 0.0374  0.0517  1690 PHE A CE1   
3549 C  CE2   . PHE A 473 ? 0.8462 0.7650 0.9956 -0.0308 0.0209  0.0341  1690 PHE A CE2   
3550 C  CZ    . PHE A 473 ? 0.8329 0.7443 0.9599 -0.0284 0.0299  0.0417  1690 PHE A CZ    
3551 N  N     . GLU A 474 ? 0.9591 0.7998 1.1215 -0.0333 0.0267  0.0530  1691 GLU A N     
3552 C  CA    . GLU A 474 ? 0.9879 0.8108 1.1618 -0.0371 0.0296  0.0536  1691 GLU A CA    
3553 C  C     . GLU A 474 ? 1.0467 0.8499 1.1999 -0.0300 0.0353  0.0666  1691 GLU A C     
3554 O  O     . GLU A 474 ? 1.0883 0.8892 1.2261 -0.0205 0.0276  0.0687  1691 GLU A O     
3555 C  CB    . GLU A 474 ? 0.9456 0.7710 1.1292 -0.0368 0.0172  0.0421  1691 GLU A CB    
3556 N  N     . GLN A 475 ? 1.0443 0.8340 1.1972 -0.0341 0.0489  0.0761  1692 GLN A N     
3557 C  CA    . GLN A 475 ? 1.0353 0.8051 1.1678 -0.0271 0.0547  0.0899  1692 GLN A CA    
3558 C  C     . GLN A 475 ? 1.1502 0.9003 1.2924 -0.0275 0.0542  0.0894  1692 GLN A C     
3559 O  O     . GLN A 475 ? 1.1261 0.8738 1.2918 -0.0368 0.0552  0.0809  1692 GLN A O     
3560 C  CB    . GLN A 475 ? 0.9453 0.7060 1.0714 -0.0310 0.0708  0.1012  1692 GLN A CB    
3561 C  CG    . GLN A 475 ? 0.9855 0.7594 1.0918 -0.0275 0.0723  0.1045  1692 GLN A CG    
3562 C  CD    . GLN A 475 ? 0.9527 0.7170 1.0262 -0.0169 0.0713  0.1171  1692 GLN A CD    
3563 O  OE1   . GLN A 475 ? 1.1228 0.8666 1.1859 -0.0150 0.0802  0.1296  1692 GLN A OE1   
3564 N  NE2   . GLN A 475 ? 1.0056 0.7845 1.0629 -0.0100 0.0601  0.1143  1692 GLN A NE2   
3565 N  N     . PRO A 476 ? 1.2175 0.9533 1.3426 -0.0173 0.0521  0.0979  1693 PRO A N     
3566 C  CA    . PRO A 476 ? 1.2394 0.9544 1.3736 -0.0170 0.0525  0.0969  1693 PRO A CA    
3567 C  C     . PRO A 476 ? 1.3857 1.0781 1.5289 -0.0249 0.0672  0.1045  1693 PRO A C     
3568 O  O     . PRO A 476 ? 1.4630 1.1408 1.6228 -0.0306 0.0686  0.0988  1693 PRO A O     
3569 C  CB    . PRO A 476 ? 1.1431 0.8516 1.2566 -0.0024 0.0467  0.1054  1693 PRO A CB    
3570 C  CG    . PRO A 476 ? 1.0693 0.7879 1.1603 0.0032  0.0474  0.1159  1693 PRO A CG    
3571 C  CD    . PRO A 476 ? 1.1178 0.8561 1.2155 -0.0056 0.0488  0.1085  1693 PRO A CD    
3572 N  N     . ALA A 477 ? 1.3641 1.0529 1.4966 -0.0260 0.0787  0.1167  1694 ALA A N     
3573 C  CA    . ALA A 477 ? 1.3682 1.0363 1.5083 -0.0338 0.0947  0.1257  1694 ALA A CA    
3574 C  C     . ALA A 477 ? 1.4457 1.1205 1.5731 -0.0352 0.1054  0.1352  1694 ALA A C     
3575 O  O     . ALA A 477 ? 1.4195 1.1093 1.5269 -0.0281 0.0998  0.1368  1694 ALA A O     
3576 C  CB    . ALA A 477 ? 1.2250 0.8639 1.3542 -0.0267 0.0995  0.1378  1694 ALA A CB    
3577 N  N     . LYS A 478 ? 1.4454 1.1086 1.5846 -0.0449 0.1213  0.1411  1695 LYS A N     
3578 C  CA    . LYS A 478 ? 1.3475 1.0145 1.4747 -0.0466 0.1343  0.1504  1695 LYS A CA    
3579 C  C     . LYS A 478 ? 1.3350 0.9780 1.4332 -0.0384 0.1433  0.1694  1695 LYS A C     
3580 O  O     . LYS A 478 ? 1.2986 0.9178 1.4008 -0.0385 0.1484  0.1763  1695 LYS A O     
3581 C  CB    . LYS A 478 ? 1.2410 0.9101 1.3978 -0.0613 0.1481  0.1474  1695 LYS A CB    
3582 N  N     . ILE A 479 ? 1.3715 1.0202 1.4394 -0.0308 0.1441  0.1776  1696 ILE A N     
3583 C  CA    . ILE A 479 ? 1.4127 1.0407 1.4487 -0.0210 0.1491  0.1958  1696 ILE A CA    
3584 C  C     . ILE A 479 ? 1.5443 1.1502 1.5833 -0.0284 0.1708  0.2084  1696 ILE A C     
3585 O  O     . ILE A 479 ? 1.4935 1.1059 1.5370 -0.0362 0.1839  0.2086  1696 ILE A O     
3586 C  CB    . ILE A 479 ? 1.2522 0.8925 1.2539 -0.0121 0.1432  0.2002  1696 ILE A CB    
3587 N  N     . ASP A 480 ? 1.6255 1.2045 1.6621 -0.0254 0.1758  0.2197  1697 ASP A N     
3588 C  CA    . ASP A 480 ? 1.6265 1.1816 1.6673 -0.0326 0.1969  0.2326  1697 ASP A CA    
3589 C  C     . ASP A 480 ? 1.6208 1.1613 1.6204 -0.0228 0.2048  0.2525  1697 ASP A C     
3590 O  O     . ASP A 480 ? 1.7884 1.3118 1.7681 -0.0117 0.1995  0.2640  1697 ASP A O     
3591 C  CB    . ASP A 480 ? 1.6268 1.1584 1.6888 -0.0358 0.1990  0.2336  1697 ASP A CB    
3592 N  N     . PRO A 481 ? 1.4928 1.0386 1.4777 -0.0260 0.2175  0.2575  1698 PRO A N     
3593 C  CA    . PRO A 481 ? 1.4298 0.9655 1.3691 -0.0158 0.2216  0.2743  1698 PRO A CA    
3594 C  C     . PRO A 481 ? 1.6163 1.1186 1.5385 -0.0113 0.2336  0.2953  1698 PRO A C     
3595 O  O     . PRO A 481 ? 1.7828 1.2754 1.6646 -0.0006 0.2329  0.3101  1698 PRO A O     
3596 C  CB    . PRO A 481 ? 1.3690 0.9155 1.3032 -0.0231 0.2367  0.2728  1698 PRO A CB    
3597 C  CG    . PRO A 481 ? 1.3556 0.9254 1.3318 -0.0344 0.2340  0.2531  1698 PRO A CG    
3598 C  CD    . PRO A 481 ? 1.4654 1.0268 1.4752 -0.0392 0.2290  0.2478  1698 PRO A CD    
3599 N  N     . LYS A 482 ? 1.5025 0.9860 1.4528 -0.0193 0.2446  0.2977  1699 LYS A N     
3600 C  CA    . LYS A 482 ? 1.6168 1.0665 1.5506 -0.0141 0.2554  0.3184  1699 LYS A CA    
3601 C  C     . LYS A 482 ? 1.7565 1.1990 1.6688 0.0021  0.2374  0.3251  1699 LYS A C     
3602 O  O     . LYS A 482 ? 1.8385 1.2559 1.7250 0.0109  0.2432  0.3450  1699 LYS A O     
3603 C  CB    . LYS A 482 ? 1.5852 1.0163 1.5568 -0.0266 0.2692  0.3175  1699 LYS A CB    
3604 N  N     . VAL A 483 ? 1.7025 1.1673 1.6238 0.0069  0.2159  0.3097  1700 VAL A N     
3605 C  CA    . VAL A 483 ? 1.6443 1.1049 1.5540 0.0216  0.1986  0.3139  1700 VAL A CA    
3606 C  C     . VAL A 483 ? 1.5911 1.0806 1.4834 0.0304  0.1781  0.3058  1700 VAL A C     
3607 O  O     . VAL A 483 ? 1.5034 0.9905 1.3635 0.0434  0.1695  0.3184  1700 VAL A O     
3608 C  CB    . VAL A 483 ? 1.5686 1.0206 1.5136 0.0185  0.1945  0.3038  1700 VAL A CB    
3609 C  CG1   . VAL A 483 ? 1.5624 1.0382 1.5424 0.0058  0.1895  0.2798  1700 VAL A CG1   
3610 C  CG2   . VAL A 483 ? 1.5286 0.9790 1.4651 0.0340  0.1772  0.3064  1700 VAL A CG2   
3611 N  N     . ASP A 484 ? 1.6425 1.1593 1.5552 0.0229  0.1704  0.2856  1701 ASP A N     
3612 C  CA    . ASP A 484 ? 1.5720 1.1157 1.4762 0.0304  0.1497  0.2755  1701 ASP A CA    
3613 C  C     . ASP A 484 ? 1.6823 1.2339 1.5465 0.0375  0.1459  0.2844  1701 ASP A C     
3614 O  O     . ASP A 484 ? 1.8568 1.4076 1.7070 0.0314  0.1590  0.2875  1701 ASP A O     
3615 C  CB    . ASP A 484 ? 1.3478 0.9168 1.2813 0.0200  0.1448  0.2532  1701 ASP A CB    
3616 C  CG    . ASP A 484 ? 1.4099 0.9745 1.3797 0.0146  0.1428  0.2420  1701 ASP A CG    
3617 O  OD1   . ASP A 484 ? 1.5378 1.0817 1.5086 0.0212  0.1421  0.2501  1701 ASP A OD1   
3618 O  OD2   . ASP A 484 ? 1.2944 0.8751 1.2906 0.0041  0.1417  0.2253  1701 ASP A OD2   
3619 N  N     . LYS A 485 ? 1.5755 1.1340 1.4211 0.0505  0.1282  0.2886  1702 LYS A N     
3620 C  CA    . LYS A 485 ? 1.4830 1.0531 1.2921 0.0573  0.1193  0.2937  1702 LYS A CA    
3621 C  C     . LYS A 485 ? 1.4037 1.0020 1.2209 0.0619  0.0973  0.2796  1702 LYS A C     
3622 O  O     . LYS A 485 ? 1.3422 0.9459 1.1869 0.0634  0.0891  0.2711  1702 LYS A O     
3623 C  CB    . LYS A 485 ? 1.4220 0.9711 1.1961 0.0693  0.1194  0.3168  1702 LYS A CB    
3624 N  N     . CYS A 486 ? 1.4457 1.0616 1.2398 0.0629  0.0889  0.2758  1703 CYS A N     
3625 C  CA    . CYS A 486 ? 1.3886 1.0316 1.1894 0.0665  0.0685  0.2628  1703 CYS A CA    
3626 C  C     . CYS A 486 ? 1.3696 1.0121 1.1712 0.0797  0.0530  0.2708  1703 CYS A C     
3627 O  O     . CYS A 486 ? 1.4745 1.0998 1.2546 0.0888  0.0534  0.2890  1703 CYS A O     
3628 C  CB    . CYS A 486 ? 1.3237 0.9815 1.0944 0.0662  0.0620  0.2601  1703 CYS A CB    
3629 S  SG    . CYS A 486 ? 1.2677 0.9557 1.0374 0.0732  0.0347  0.2500  1703 CYS A SG    
3630 N  N     . VAL A 487 ? 1.2392 0.9005 1.0665 0.0812  0.0400  0.2575  1704 VAL A N     
3631 C  CA    . VAL A 487 ? 1.2731 0.9340 1.1096 0.0932  0.0279  0.2633  1704 VAL A CA    
3632 C  C     . VAL A 487 ? 1.2873 0.9547 1.0955 0.1052  0.0129  0.2760  1704 VAL A C     
3633 O  O     . VAL A 487 ? 1.1995 0.8608 1.0095 0.1171  0.0057  0.2872  1704 VAL A O     
3634 C  CB    . VAL A 487 ? 1.2084 0.8897 1.0770 0.0914  0.0184  0.2451  1704 VAL A CB    
3635 C  CG1   . VAL A 487 ? 1.0007 0.7110 0.8627 0.0904  0.0039  0.2345  1704 VAL A CG1   
3636 C  CG2   . VAL A 487 ? 1.1793 0.8545 1.0638 0.1029  0.0117  0.2503  1704 VAL A CG2   
3637 N  N     . HIS A 488 ? 1.3587 1.0378 1.1408 0.1026  0.0079  0.2748  1705 HIS A N     
3638 C  CA    . HIS A 488 ? 1.4613 1.1460 1.2160 0.1136  -0.0077 0.2872  1705 HIS A CA    
3639 C  C     . HIS A 488 ? 1.5081 1.1659 1.2318 0.1188  0.0015  0.3086  1705 HIS A C     
3640 O  O     . HIS A 488 ? 1.4784 1.1222 1.1848 0.1110  0.0174  0.3108  1705 HIS A O     
3641 C  CB    . HIS A 488 ? 1.5211 1.2273 1.2564 0.1095  -0.0189 0.2781  1705 HIS A CB    
3642 C  CG    . HIS A 488 ? 1.6432 1.3573 1.3527 0.1201  -0.0375 0.2896  1705 HIS A CG    
3643 N  ND1   . HIS A 488 ? 1.6376 1.3577 1.3602 0.1324  -0.0514 0.2979  1705 HIS A ND1   
3644 C  CD2   . HIS A 488 ? 1.6912 1.4080 1.3627 0.1204  -0.0447 0.2944  1705 HIS A CD2   
3645 C  CE1   . HIS A 488 ? 1.6564 1.3843 1.3520 0.1396  -0.0674 0.3076  1705 HIS A CE1   
3646 N  NE2   . HIS A 488 ? 1.6872 1.4127 1.3502 0.1323  -0.0642 0.3054  1705 HIS A NE2   
3647 N  N     . PRO A 489 ? 1.4848 1.1349 1.2014 0.1324  -0.0074 0.3252  1706 PRO A N     
3648 C  CA    . PRO A 489 ? 1.5077 1.1301 1.1943 0.1384  0.0016  0.3473  1706 PRO A CA    
3649 C  C     . PRO A 489 ? 1.5151 1.1368 1.1552 0.1379  -0.0014 0.3551  1706 PRO A C     
3650 O  O     . PRO A 489 ? 1.5496 1.1460 1.1626 0.1394  0.0114  0.3712  1706 PRO A O     
3651 C  CB    . PRO A 489 ? 1.4593 1.0788 1.1537 0.1543  -0.0108 0.3615  1706 PRO A CB    
3652 C  CG    . PRO A 489 ? 1.4204 1.0565 1.1580 0.1541  -0.0166 0.3457  1706 PRO A CG    
3653 C  CD    . PRO A 489 ? 1.4093 1.0716 1.1524 0.1427  -0.0218 0.3246  1706 PRO A CD    
3654 N  N     . ALA A 490 ? 1.5449 1.1912 1.1731 0.1357  -0.0168 0.3445  1707 ALA A N     
3655 C  CA    . ALA A 490 ? 1.6833 1.3259 1.2635 0.1359  -0.0202 0.3522  1707 ALA A CA    
3656 C  C     . ALA A 490 ? 1.7904 1.4228 1.3546 0.1230  0.0001  0.3448  1707 ALA A C     
3657 O  O     . ALA A 490 ? 1.7734 1.3881 1.2973 0.1234  0.0084  0.3568  1707 ALA A O     
3658 C  CB    . ALA A 490 ? 1.6613 1.3326 1.2328 0.1381  -0.0449 0.3438  1707 ALA A CB    
3659 N  N     . CYS A 491 ? 1.8372 1.4796 1.4326 0.1120  0.0092  0.3261  1708 CYS A N     
3660 C  CA    . CYS A 491 ? 1.8736 1.5054 1.4605 0.1004  0.0308  0.3203  1708 CYS A CA    
3661 C  C     . CYS A 491 ? 1.9261 1.5332 1.5302 0.0984  0.0522  0.3298  1708 CYS A C     
3662 O  O     . CYS A 491 ? 1.7816 1.3871 1.4190 0.1012  0.0508  0.3298  1708 CYS A O     
3663 C  CB    . CYS A 491 ? 1.7534 1.4076 1.3653 0.0895  0.0308  0.2966  1708 CYS A CB    
3664 S  SG    . CYS A 491 ? 1.7074 1.3661 1.3768 0.0839  0.0383  0.2847  1708 CYS A SG    
3665 N  N     . GLY A 492 ? 1.9802 1.5662 1.5589 0.0943  0.0718  0.3392  1709 GLY A N     
3666 C  CA    . GLY A 492 ? 1.9804 1.5422 1.5746 0.0909  0.0936  0.3484  1709 GLY A CA    
3667 C  C     . GLY A 492 ? 1.9816 1.5459 1.5982 0.0766  0.1128  0.3343  1709 GLY A C     
3668 O  O     . GLY A 492 ? 2.0207 1.5645 1.6449 0.0712  0.1343  0.3419  1709 GLY A O     
3669 N  N     . ARG A 493 ? 1.8354 1.4245 1.4633 0.0703  0.1057  0.3147  1710 ARG A N     
3670 C  CA    . ARG A 493 ? 1.7601 1.3556 1.4130 0.0574  0.1216  0.3002  1710 ARG A CA    
3671 C  C     . ARG A 493 ? 1.7467 1.3408 1.4479 0.0524  0.1268  0.2946  1710 ARG A C     
3672 O  O     . ARG A 493 ? 1.7527 1.3540 1.4745 0.0577  0.1118  0.2915  1710 ARG A O     
3673 C  CB    . ARG A 493 ? 1.6285 1.2510 1.2834 0.0537  0.1096  0.2810  1710 ARG A CB    
3674 N  N     . VAL A 494 ? 1.6914 1.2752 1.4101 0.0422  0.1488  0.2937  1711 VAL A N     
3675 C  CA    . VAL A 494 ? 1.5276 1.1131 1.2938 0.0345  0.1538  0.2844  1711 VAL A CA    
3676 C  C     . VAL A 494 ? 1.3933 1.0081 1.1865 0.0307  0.1393  0.2627  1711 VAL A C     
3677 O  O     . VAL A 494 ? 1.3241 0.9561 1.1047 0.0293  0.1344  0.2534  1711 VAL A O     
3678 C  CB    . VAL A 494 ? 1.1884 0.7607 0.9686 0.0231  0.1797  0.2869  1711 VAL A CB    
3679 N  N     . ALA A 495 ? 1.3662 0.9850 1.1950 0.0292  0.1326  0.2547  1712 ALA A N     
3680 C  CA    . ALA A 495 ? 1.3198 0.9646 1.1736 0.0265  0.1184  0.2353  1712 ALA A CA    
3681 C  C     . ALA A 495 ? 1.4286 1.0866 1.3021 0.0145  0.1286  0.2218  1712 ALA A C     
3682 O  O     . ALA A 495 ? 1.4053 1.0539 1.2995 0.0056  0.1450  0.2223  1712 ALA A O     
3683 C  CB    . ALA A 495 ? 1.1091 0.7518 0.9943 0.0276  0.1110  0.2305  1712 ALA A CB    
3684 N  N     . LYS A 496 ? 1.4348 1.1153 1.3044 0.0142  0.1185  0.2094  1713 LYS A N     
3685 C  CA    . LYS A 496 ? 1.3189 1.0140 1.2102 0.0040  0.1264  0.1959  1713 LYS A CA    
3686 C  C     . LYS A 496 ? 1.2420 0.9497 1.1749 -0.0013 0.1192  0.1819  1713 LYS A C     
3687 O  O     . LYS A 496 ? 1.2872 1.0006 1.2469 -0.0110 0.1290  0.1741  1713 LYS A O     
3688 C  CB    . LYS A 496 ? 1.3269 1.0388 1.1972 0.0057  0.1196  0.1883  1713 LYS A CB    
3689 N  N     . PHE A 497 ? 1.1661 0.8789 1.1049 0.0049  0.1023  0.1783  1714 PHE A N     
3690 C  CA    . PHE A 497 ? 1.1171 0.8417 1.0907 0.0006  0.0942  0.1643  1714 PHE A CA    
3691 C  C     . PHE A 497 ? 1.0193 0.7436 0.9910 0.0101  0.0781  0.1650  1714 PHE A C     
3692 O  O     . PHE A 497 ? 1.1342 0.8503 1.0808 0.0196  0.0734  0.1767  1714 PHE A O     
3693 C  CB    . PHE A 497 ? 1.0914 0.8405 1.0766 -0.0042 0.0889  0.1489  1714 PHE A CB    
3694 C  CG    . PHE A 497 ? 1.2003 0.9589 1.1559 0.0006  0.0841  0.1495  1714 PHE A CG    
3695 C  CD1   . PHE A 497 ? 1.2782 1.0411 1.2134 0.0101  0.0685  0.1521  1714 PHE A CD1   
3696 C  CD2   . PHE A 497 ? 1.1780 0.9410 1.1265 -0.0045 0.0955  0.1475  1714 PHE A CD2   
3697 C  CE1   . PHE A 497 ? 1.2881 1.0594 1.1958 0.0134  0.0631  0.1519  1714 PHE A CE1   
3698 C  CE2   . PHE A 497 ? 1.1403 0.9100 1.0596 -0.0005 0.0912  0.1469  1714 PHE A CE2   
3699 C  CZ    . PHE A 497 ? 1.2319 1.0056 1.1305 0.0079  0.0745  0.1488  1714 PHE A CZ    
3700 N  N     . TYR A 498 ? 0.9190 0.6517 0.9179 0.0076  0.0703  0.1530  1715 TYR A N     
3701 C  CA    . TYR A 498 ? 1.0564 0.7950 1.0561 0.0163  0.0545  0.1500  1715 TYR A CA    
3702 C  C     . TYR A 498 ? 1.1189 0.8824 1.1129 0.0184  0.0417  0.1404  1715 TYR A C     
3703 O  O     . TYR A 498 ? 1.1173 0.8951 1.1234 0.0110  0.0428  0.1292  1715 TYR A O     
3704 C  CB    . TYR A 498 ? 1.0266 0.7609 1.0552 0.0128  0.0528  0.1410  1715 TYR A CB    
3705 C  CG    . TYR A 498 ? 1.1635 0.8710 1.1937 0.0142  0.0617  0.1518  1715 TYR A CG    
3706 C  CD1   . TYR A 498 ? 1.1550 0.8508 1.1713 0.0261  0.0565  0.1624  1715 TYR A CD1   
3707 C  CD2   . TYR A 498 ? 1.2445 0.9380 1.2907 0.0039  0.0757  0.1522  1715 TYR A CD2   
3708 C  CE1   . TYR A 498 ? 1.0831 0.7524 1.1004 0.0281  0.0653  0.1731  1715 TYR A CE1   
3709 C  CE2   . TYR A 498 ? 1.2304 0.8973 1.2781 0.0047  0.0847  0.1624  1715 TYR A CE2   
3710 C  CZ    . TYR A 498 ? 1.1560 0.8102 1.1885 0.0170  0.0796  0.1728  1715 TYR A CZ    
3711 O  OH    . TYR A 498 ? 1.2328 0.8591 1.2670 0.0181  0.0891  0.1833  1715 TYR A OH    
3712 N  N     . THR A 499 ? 1.0748 0.8435 1.0515 0.0285  0.0296  0.1452  1716 THR A N     
3713 C  CA    . THR A 499 ? 1.0176 0.8090 0.9905 0.0309  0.0162  0.1365  1716 THR A CA    
3714 C  C     . THR A 499 ? 1.0565 0.8536 1.0398 0.0386  0.0035  0.1340  1716 THR A C     
3715 O  O     . THR A 499 ? 1.0688 0.8511 1.0539 0.0447  0.0044  0.1421  1716 THR A O     
3716 C  CB    . THR A 499 ? 1.0326 0.8272 0.9737 0.0353  0.0127  0.1444  1716 THR A CB    
3717 O  OG1   . THR A 499 ? 1.1602 0.9458 1.0884 0.0291  0.0268  0.1483  1716 THR A OG1   
3718 C  CG2   . THR A 499 ? 1.0201 0.8376 0.9587 0.0358  -0.0002 0.1344  1716 THR A CG2   
3719 N  N     . LEU A 500 ? 0.9757 0.7937 0.9663 0.0387  -0.0074 0.1230  1717 LEU A N     
3720 C  CA    . LEU A 500 ? 1.0335 0.8596 1.0347 0.0459  -0.0187 0.1197  1717 LEU A CA    
3721 C  C     . LEU A 500 ? 1.0998 0.9389 1.0844 0.0536  -0.0309 0.1248  1717 LEU A C     
3722 O  O     . LEU A 500 ? 1.0661 0.9196 1.0418 0.0502  -0.0353 0.1198  1717 LEU A O     
3723 C  CB    . LEU A 500 ? 1.0121 0.8521 1.0348 0.0404  -0.0222 0.1039  1717 LEU A CB    
3724 C  CG    . LEU A 500 ? 1.0155 0.8545 1.0549 0.0451  -0.0270 0.0991  1717 LEU A CG    
3725 C  CD1   . LEU A 500 ? 1.1047 0.9207 1.1526 0.0442  -0.0176 0.1026  1717 LEU A CD1   
3726 C  CD2   . LEU A 500 ? 0.9959 0.8505 1.0510 0.0396  -0.0312 0.0841  1717 LEU A CD2   
3727 N  N     . PHE A 501 ? 1.1144 0.9488 1.0963 0.0639  -0.0366 0.1343  1718 PHE A N     
3728 C  CA    . PHE A 501 ? 1.0601 0.9077 1.0295 0.0719  -0.0495 0.1402  1718 PHE A CA    
3729 C  C     . PHE A 501 ? 1.1377 0.9969 1.1263 0.0789  -0.0585 0.1361  1718 PHE A C     
3730 O  O     . PHE A 501 ? 1.1157 0.9648 1.1204 0.0814  -0.0538 0.1345  1718 PHE A O     
3731 C  CB    . PHE A 501 ? 0.9344 0.7681 0.8829 0.0797  -0.0495 0.1575  1718 PHE A CB    
3732 C  CG    . PHE A 501 ? 0.9906 0.8102 0.9180 0.0739  -0.0389 0.1634  1718 PHE A CG    
3733 C  CD1   . PHE A 501 ? 1.0282 0.8275 0.9615 0.0690  -0.0237 0.1654  1718 PHE A CD1   
3734 C  CD2   . PHE A 501 ? 0.9690 0.7947 0.8703 0.0732  -0.0437 0.1671  1718 PHE A CD2   
3735 C  CE1   . PHE A 501 ? 1.0988 0.8851 1.0137 0.0637  -0.0122 0.1715  1718 PHE A CE1   
3736 C  CE2   . PHE A 501 ? 1.0145 0.8260 0.8944 0.0683  -0.0323 0.1726  1718 PHE A CE2   
3737 C  CZ    . PHE A 501 ? 1.1019 0.8940 0.9892 0.0638  -0.0160 0.1753  1718 PHE A CZ    
3738 N  N     . GLY A 502 ? 1.0810 0.9608 1.0671 0.0820  -0.0710 0.1346  1719 GLY A N     
3739 C  CA    . GLY A 502 ? 1.0537 0.9470 1.0578 0.0891  -0.0795 0.1318  1719 GLY A CA    
3740 C  C     . GLY A 502 ? 1.0120 0.9271 1.0098 0.0918  -0.0934 0.1332  1719 GLY A C     
3741 O  O     . GLY A 502 ? 0.8545 0.7735 0.8332 0.0870  -0.0967 0.1341  1719 GLY A O     
3742 N  N     . ARG A 503 ? 1.1595 1.0884 1.1738 0.0992  -0.1013 0.1331  1720 ARG A N     
3743 C  CA    . ARG A 503 ? 1.1464 1.0989 1.1611 0.1006  -0.1150 0.1325  1720 ARG A CA    
3744 C  C     . ARG A 503 ? 1.2588 1.2250 1.2808 0.0906  -0.1152 0.1173  1720 ARG A C     
3745 O  O     . ARG A 503 ? 1.0539 1.0183 1.0912 0.0878  -0.1084 0.1079  1720 ARG A O     
3746 C  CB    . ARG A 503 ? 1.0340 0.9973 1.0671 0.1122  -0.1220 0.1383  1720 ARG A CB    
3747 C  CG    . ARG A 503 ? 1.0486 1.0027 1.0740 0.1236  -0.1254 0.1553  1720 ARG A CG    
3748 C  CD    . ARG A 503 ? 1.0731 1.0498 1.1019 0.1307  -0.1418 0.1629  1720 ARG A CD    
3749 N  NE    . ARG A 503 ? 1.1069 1.0753 1.1263 0.1417  -0.1463 0.1800  1720 ARG A NE    
3750 C  CZ    . ARG A 503 ? 1.2124 1.1748 1.2476 0.1540  -0.1438 0.1886  1720 ARG A CZ    
3751 N  NH1   . ARG A 503 ? 1.2301 1.1939 1.2897 0.1563  -0.1367 0.1805  1720 ARG A NH1   
3752 N  NH2   . ARG A 503 ? 1.2674 1.2213 1.2929 0.1642  -0.1481 0.2052  1720 ARG A NH2   
3753 N  N     . SER A 504 ? 1.4084 1.3874 1.4183 0.0853  -0.1234 0.1149  1721 SER A N     
3754 C  CA    . SER A 504 ? 1.4661 1.4533 1.4772 0.0750  -0.1220 0.1017  1721 SER A CA    
3755 C  C     . SER A 504 ? 1.5053 1.5154 1.5326 0.0747  -0.1315 0.0953  1721 SER A C     
3756 O  O     . SER A 504 ? 1.4465 1.4695 1.4811 0.0815  -0.1414 0.1014  1721 SER A O     
3757 C  CB    . SER A 504 ? 1.5430 1.5260 1.5283 0.0682  -0.1226 0.1018  1721 SER A CB    
3758 O  OG    . SER A 504 ? 1.5448 1.5256 1.5296 0.0585  -0.1148 0.0906  1721 SER A OG    
3759 N  N     . TYR A 505 ? 1.5327 1.5479 1.5671 0.0669  -0.1279 0.0832  1722 TYR A N     
3760 C  CA    . TYR A 505 ? 1.5374 1.5729 1.5837 0.0643  -0.1358 0.0766  1722 TYR A CA    
3761 C  C     . TYR A 505 ? 1.5389 1.5798 1.5676 0.0571  -0.1423 0.0739  1722 TYR A C     
3762 O  O     . TYR A 505 ? 1.4762 1.5046 1.4877 0.0515  -0.1360 0.0716  1722 TYR A O     
3763 C  CB    . TYR A 505 ? 1.5232 1.5607 1.5853 0.0602  -0.1289 0.0658  1722 TYR A CB    
3764 C  CG    . TYR A 505 ? 1.5029 1.5589 1.5845 0.0628  -0.1346 0.0631  1722 TYR A CG    
3765 C  CD1   . TYR A 505 ? 1.5374 1.6103 1.6199 0.0589  -0.1441 0.0610  1722 TYR A CD1   
3766 C  CD2   . TYR A 505 ? 1.4794 1.5354 1.5783 0.0689  -0.1300 0.0627  1722 TYR A CD2   
3767 C  CE1   . TYR A 505 ? 1.5959 1.6864 1.6982 0.0607  -0.1485 0.0591  1722 TYR A CE1   
3768 C  CE2   . TYR A 505 ? 1.5310 1.6039 1.6478 0.0715  -0.1336 0.0608  1722 TYR A CE2   
3769 C  CZ    . TYR A 505 ? 1.6245 1.7153 1.7441 0.0673  -0.1427 0.0594  1722 TYR A CZ    
3770 O  OH    . TYR A 505 ? 1.6858 1.7940 1.8252 0.0694  -0.1454 0.0580  1722 TYR A OH    
3771 O  OXT   . TYR A 505 ? 1.5387 1.5960 1.5704 0.0565  -0.1534 0.0736  1722 TYR A OXT   
3772 N  N     . LEU B 6   ? 1.1511 0.9302 1.4925 0.1156  0.2232  -0.0993 1223 LEU B N     
3773 C  CA    . LEU B 6   ? 1.1490 0.9032 1.4633 0.1078  0.2168  -0.1064 1223 LEU B CA    
3774 C  C     . LEU B 6   ? 1.2278 0.9461 1.5280 0.1114  0.2377  -0.1185 1223 LEU B C     
3775 O  O     . LEU B 6   ? 1.1714 0.8845 1.4971 0.1246  0.2528  -0.1153 1223 LEU B O     
3776 C  CB    . LEU B 6   ? 1.1038 0.8671 1.4390 0.1111  0.2006  -0.0942 1223 LEU B CB    
3777 C  CG    . LEU B 6   ? 1.1688 0.9295 1.4783 0.0976  0.1819  -0.0962 1223 LEU B CG    
3778 C  CD1   . LEU B 6   ? 1.1084 0.8804 1.3922 0.0854  0.1742  -0.1020 1223 LEU B CD1   
3779 C  CD2   . LEU B 6   ? 1.1498 0.9296 1.4814 0.1007  0.1642  -0.0814 1223 LEU B CD2   
3780 N  N     . GLU B 7   ? 1.3518 1.0452 1.6117 0.0997  0.2385  -0.1327 1224 GLU B N     
3781 C  CA    . GLU B 7   ? 1.3717 1.0284 1.6130 0.1015  0.2583  -0.1464 1224 GLU B CA    
3782 C  C     . GLU B 7   ? 1.4360 1.0668 1.6700 0.0985  0.2547  -0.1502 1224 GLU B C     
3783 O  O     . GLU B 7   ? 1.5516 1.1534 1.7838 0.1045  0.2723  -0.1577 1224 GLU B O     
3784 C  CB    . GLU B 7   ? 1.3863 1.0283 1.5845 0.0908  0.2648  -0.1619 1224 GLU B CB    
3785 N  N     . ALA B 8   ? 1.4472 1.0860 1.6772 0.0894  0.2338  -0.1453 1225 ALA B N     
3786 C  CA    . ALA B 8   ? 1.3689 0.9841 1.5944 0.0859  0.2304  -0.1475 1225 ALA B CA    
3787 C  C     . ALA B 8   ? 1.4049 1.0383 1.6637 0.0931  0.2181  -0.1296 1225 ALA B C     
3788 O  O     . ALA B 8   ? 1.3904 1.0540 1.6754 0.1010  0.2120  -0.1165 1225 ALA B O     
3789 C  CB    . ALA B 8   ? 1.2969 0.9008 1.4858 0.0676  0.2180  -0.1587 1225 ALA B CB    
3790 N  N     . THR B 9   ? 1.3856 0.9995 1.6428 0.0904  0.2145  -0.1290 1226 THR B N     
3791 C  CA    . THR B 9   ? 1.3753 1.0022 1.6610 0.0978  0.2042  -0.1118 1226 THR B CA    
3792 C  C     . THR B 9   ? 1.3310 0.9498 1.6035 0.0859  0.1901  -0.1109 1226 THR B C     
3793 O  O     . THR B 9   ? 1.3218 0.9147 1.5691 0.0745  0.1928  -0.1241 1226 THR B O     
3794 C  CB    . THR B 9   ? 1.3831 0.9945 1.6956 0.1144  0.2196  -0.1058 1226 THR B CB    
3795 O  OG1   . THR B 9   ? 1.4448 1.0729 1.7845 0.1224  0.2077  -0.0873 1226 THR B OG1   
3796 C  CG2   . THR B 9   ? 1.3460 0.9156 1.6418 0.1110  0.2325  -0.1179 1226 THR B CG2   
3797 N  N     . LYS B 10  ? 1.2607 0.9028 1.5511 0.0887  0.1748  -0.0949 1227 LYS B N     
3798 C  CA    . LYS B 10  ? 1.2381 0.8790 1.5203 0.0787  0.1606  -0.0906 1227 LYS B CA    
3799 C  C     . LYS B 10  ? 1.3775 0.9834 1.6576 0.0780  0.1694  -0.0935 1227 LYS B C     
3800 O  O     . LYS B 10  ? 1.4179 1.0105 1.6800 0.0644  0.1638  -0.0997 1227 LYS B O     
3801 C  CB    . LYS B 10  ? 1.0797 0.7503 1.3840 0.0857  0.1460  -0.0718 1227 LYS B CB    
3802 C  CG    . LYS B 10  ? 0.9347 0.6198 1.2283 0.0743  0.1278  -0.0668 1227 LYS B CG    
3803 C  CD    . LYS B 10  ? 0.9006 0.6085 1.2168 0.0844  0.1167  -0.0477 1227 LYS B CD    
3804 C  CE    . LYS B 10  ? 0.8158 0.5350 1.1230 0.0753  0.1009  -0.0409 1227 LYS B CE    
3805 N  NZ    . LYS B 10  ? 0.7929 0.5459 1.1081 0.0783  0.0870  -0.0315 1227 LYS B NZ    
3806 N  N     . GLU B 11  ? 1.5057 1.0956 1.8045 0.0922  0.1838  -0.0898 1228 GLU B N     
3807 C  CA    . GLU B 11  ? 1.4969 1.0547 1.7982 0.0935  0.1913  -0.0888 1228 GLU B CA    
3808 C  C     . GLU B 11  ? 1.6160 1.1388 1.8910 0.0820  0.2025  -0.1091 1228 GLU B C     
3809 O  O     . GLU B 11  ? 1.7926 1.2900 2.0613 0.0752  0.2037  -0.1114 1228 GLU B O     
3810 C  CB    . GLU B 11  ? 1.4796 1.0301 1.8100 0.1134  0.2039  -0.0784 1228 GLU B CB    
3811 C  CG    . GLU B 11  ? 1.6429 1.2196 2.0000 0.1248  0.1920  -0.0567 1228 GLU B CG    
3812 C  CD    . GLU B 11  ? 1.7842 1.3953 2.1584 0.1338  0.1884  -0.0510 1228 GLU B CD    
3813 O  OE1   . GLU B 11  ? 1.7037 1.3452 2.0782 0.1296  0.1712  -0.0435 1228 GLU B OE1   
3814 O  OE2   . GLU B 11  ? 1.8839 1.4909 2.2716 0.1448  0.2033  -0.0544 1228 GLU B OE2   
3815 N  N     . ASP B 12  ? 1.6649 1.1849 1.9240 0.0797  0.2111  -0.1237 1229 ASP B N     
3816 C  CA    . ASP B 12  ? 1.7602 1.2441 1.9935 0.0709  0.2236  -0.1437 1229 ASP B CA    
3817 C  C     . ASP B 12  ? 1.7504 1.2380 1.9507 0.0522  0.2138  -0.1582 1229 ASP B C     
3818 O  O     . ASP B 12  ? 1.7241 1.1852 1.9031 0.0389  0.2140  -0.1711 1229 ASP B O     
3819 C  CB    . ASP B 12  ? 1.9248 1.3957 2.1631 0.0843  0.2449  -0.1502 1229 ASP B CB    
3820 C  CG    . ASP B 12  ? 2.2303 1.6584 2.4436 0.0786  0.2614  -0.1705 1229 ASP B CG    
3821 O  OD1   . ASP B 12  ? 2.3250 1.7265 2.5339 0.0724  0.2618  -0.1736 1229 ASP B OD1   
3822 O  OD2   . ASP B 12  ? 2.3385 1.7599 2.5389 0.0816  0.2748  -0.1821 1229 ASP B OD2   
3823 N  N     . ASN B 13  ? 1.6397 1.1573 1.8346 0.0507  0.2056  -0.1571 1230 ASN B N     
3824 C  CA    . ASN B 13  ? 1.6497 1.1735 1.8141 0.0342  0.1951  -0.1692 1230 ASN B CA    
3825 C  C     . ASN B 13  ? 1.6065 1.1695 1.7797 0.0316  0.1759  -0.1563 1230 ASN B C     
3826 O  O     . ASN B 13  ? 1.6936 1.2805 1.8706 0.0369  0.1745  -0.1524 1230 ASN B O     
3827 C  CB    . ASN B 13  ? 1.6664 1.1811 1.8090 0.0345  0.2074  -0.1837 1230 ASN B CB    
3828 C  CG    . ASN B 13  ? 1.7458 1.2638 1.8543 0.0176  0.1963  -0.1963 1230 ASN B CG    
3829 O  OD1   . ASN B 13  ? 1.7413 1.2741 1.8467 0.0065  0.1782  -0.1927 1230 ASN B OD1   
3830 N  ND2   . ASN B 13  ? 1.8095 1.3141 1.8923 0.0161  0.2070  -0.2105 1230 ASN B ND2   
3831 N  N     . LEU B 14  ? 1.4490 1.0173 1.6252 0.0233  0.1620  -0.1499 1231 LEU B N     
3832 C  CA    . LEU B 14  ? 1.2739 0.8777 1.4587 0.0216  0.1446  -0.1373 1231 LEU B CA    
3833 C  C     . LEU B 14  ? 1.2806 0.9023 1.4441 0.0119  0.1354  -0.1449 1231 LEU B C     
3834 O  O     . LEU B 14  ? 1.2186 0.8693 1.3913 0.0171  0.1287  -0.1360 1231 LEU B O     
3835 C  CB    . LEU B 14  ? 1.1919 0.7950 1.3826 0.0144  0.1338  -0.1298 1231 LEU B CB    
3836 C  CG    . LEU B 14  ? 1.1415 0.7794 1.3448 0.0161  0.1182  -0.1145 1231 LEU B CG    
3837 C  CD1   . LEU B 14  ? 1.1560 0.8078 1.3847 0.0336  0.1219  -0.1003 1231 LEU B CD1   
3838 C  CD2   . LEU B 14  ? 1.0126 0.6508 1.2182 0.0076  0.1080  -0.1079 1231 LEU B CD2   
3839 N  N     . PRO B 15  ? 1.3575 0.9642 1.4932 -0.0021 0.1335  -0.1603 1232 PRO B N     
3840 C  CA    . PRO B 15  ? 1.2953 0.9220 1.4123 -0.0109 0.1221  -0.1647 1232 PRO B CA    
3841 C  C     . PRO B 15  ? 1.3701 1.0059 1.4815 -0.0032 0.1301  -0.1668 1232 PRO B C     
3842 O  O     . PRO B 15  ? 1.3955 1.0589 1.5087 -0.0028 0.1207  -0.1602 1232 PRO B O     
3843 C  CB    . PRO B 15  ? 1.2978 0.9027 1.3869 -0.0269 0.1191  -0.1811 1232 PRO B CB    
3844 C  CG    . PRO B 15  ? 1.3357 0.9178 1.4349 -0.0291 0.1228  -0.1810 1232 PRO B CG    
3845 C  CD    . PRO B 15  ? 1.4112 0.9849 1.5323 -0.0122 0.1381  -0.1731 1232 PRO B CD    
3846 N  N     . ASP B 16  ? 1.4490 1.0618 1.5541 0.0031  0.1480  -0.1757 1233 ASP B N     
3847 C  CA    . ASP B 16  ? 1.5720 1.1939 1.6728 0.0104  0.1572  -0.1771 1233 ASP B CA    
3848 C  C     . ASP B 16  ? 1.4602 1.1064 1.5950 0.0251  0.1594  -0.1609 1233 ASP B C     
3849 O  O     . ASP B 16  ? 1.5508 1.2166 1.6874 0.0288  0.1599  -0.1576 1233 ASP B O     
3850 C  CB    . ASP B 16  ? 1.7438 1.3334 1.8261 0.0127  0.1771  -0.1921 1233 ASP B CB    
3851 C  CG    . ASP B 16  ? 1.8728 1.4369 1.9198 -0.0026 0.1739  -0.2093 1233 ASP B CG    
3852 O  OD1   . ASP B 16  ? 1.9324 1.5069 1.9561 -0.0131 0.1623  -0.2142 1233 ASP B OD1   
3853 O  OD2   . ASP B 16  ? 1.9174 1.4511 1.9602 -0.0040 0.1828  -0.2179 1233 ASP B OD2   
3854 N  N     . TRP B 17  ? 1.3018 0.9475 1.4634 0.0330  0.1596  -0.1504 1234 TRP B N     
3855 C  CA    . TRP B 17  ? 1.1612 0.8342 1.3548 0.0449  0.1559  -0.1337 1234 TRP B CA    
3856 C  C     . TRP B 17  ? 1.1429 0.8468 1.3369 0.0387  0.1365  -0.1254 1234 TRP B C     
3857 O  O     . TRP B 17  ? 1.2815 1.0100 1.4897 0.0449  0.1337  -0.1173 1234 TRP B O     
3858 C  CB    . TRP B 17  ? 1.0195 0.6843 1.2376 0.0534  0.1577  -0.1237 1234 TRP B CB    
3859 C  CG    . TRP B 17  ? 1.0045 0.6982 1.2517 0.0625  0.1475  -0.1058 1234 TRP B CG    
3860 C  CD1   . TRP B 17  ? 0.9078 0.6141 1.1830 0.0772  0.1540  -0.0962 1234 TRP B CD1   
3861 C  CD2   . TRP B 17  ? 1.0518 0.7646 1.3030 0.0576  0.1291  -0.0954 1234 TRP B CD2   
3862 N  NE1   . TRP B 17  ? 0.9267 0.6584 1.2217 0.0814  0.1394  -0.0809 1234 TRP B NE1   
3863 C  CE2   . TRP B 17  ? 0.9915 0.7267 1.2709 0.0697  0.1247  -0.0803 1234 TRP B CE2   
3864 C  CE3   . TRP B 17  ? 1.0894 0.8029 1.3236 0.0443  0.1162  -0.0975 1234 TRP B CE3   
3865 C  CZ2   . TRP B 17  ? 0.8470 0.6031 1.1345 0.0688  0.1081  -0.0680 1234 TRP B CZ2   
3866 C  CZ3   . TRP B 17  ? 0.9811 0.7159 1.2253 0.0440  0.1012  -0.0849 1234 TRP B CZ3   
3867 C  CH2   . TRP B 17  ? 0.9009 0.6556 1.1699 0.0561  0.0974  -0.0706 1234 TRP B CH2   
3868 N  N     . TYR B 18  ? 0.9778 0.6807 1.1583 0.0268  0.1233  -0.1271 1235 TYR B N     
3869 C  CA    . TYR B 18  ? 1.0702 0.8006 1.2500 0.0210  0.1059  -0.1200 1235 TYR B CA    
3870 C  C     . TYR B 18  ? 1.1921 0.9340 1.3549 0.0171  0.1050  -0.1261 1235 TYR B C     
3871 O  O     . TYR B 18  ? 1.1650 0.9326 1.3369 0.0196  0.0973  -0.1178 1235 TYR B O     
3872 C  CB    . TYR B 18  ? 1.0720 0.7966 1.2397 0.0084  0.0944  -0.1225 1235 TYR B CB    
3873 C  CG    . TYR B 18  ? 0.9858 0.7369 1.1552 0.0030  0.0770  -0.1142 1235 TYR B CG    
3874 C  CD1   . TYR B 18  ? 0.9661 0.7324 1.1564 0.0089  0.0697  -0.0998 1235 TYR B CD1   
3875 C  CD2   . TYR B 18  ? 0.8979 0.6573 1.0468 -0.0079 0.0679  -0.1210 1235 TYR B CD2   
3876 C  CE1   . TYR B 18  ? 0.9409 0.7292 1.1312 0.0041  0.0551  -0.0930 1235 TYR B CE1   
3877 C  CE2   . TYR B 18  ? 0.9046 0.6869 1.0559 -0.0122 0.0531  -0.1136 1235 TYR B CE2   
3878 C  CZ    . TYR B 18  ? 0.9502 0.7465 1.1220 -0.0062 0.0473  -0.1000 1235 TYR B CZ    
3879 O  OH    . TYR B 18  ? 0.9427 0.7603 1.1153 -0.0101 0.0339  -0.0934 1235 TYR B OH    
3880 N  N     . SER B 19  ? 1.2096 0.9312 1.3469 0.0112  0.1136  -0.1404 1236 SER B N     
3881 C  CA    . SER B 19  ? 1.2197 0.9494 1.3375 0.0077  0.1137  -0.1460 1236 SER B CA    
3882 C  C     . SER B 19  ? 1.1978 0.9392 1.3321 0.0195  0.1248  -0.1403 1236 SER B C     
3883 O  O     . SER B 19  ? 1.2242 0.9873 1.3594 0.0194  0.1192  -0.1354 1236 SER B O     
3884 C  CB    . SER B 19  ? 1.2396 0.9425 1.3243 -0.0008 0.1208  -0.1628 1236 SER B CB    
3885 O  OG    . SER B 19  ? 1.4415 1.1441 1.5117 0.0020  0.1309  -0.1678 1236 SER B OG    
3886 N  N     . GLN B 20  ? 1.1566 0.8855 1.3076 0.0301  0.1402  -0.1398 1237 GLN B N     
3887 C  CA    . GLN B 20  ? 1.0586 0.8010 1.2308 0.0418  0.1508  -0.1333 1237 GLN B CA    
3888 C  C     . GLN B 20  ? 1.0165 0.7896 1.2187 0.0472  0.1382  -0.1176 1237 GLN B C     
3889 O  O     . GLN B 20  ? 1.0965 0.8894 1.3103 0.0512  0.1391  -0.1123 1237 GLN B O     
3890 C  CB    . GLN B 20  ? 1.1053 0.8273 1.2905 0.0525  0.1704  -0.1362 1237 GLN B CB    
3891 C  CG    . GLN B 20  ? 1.3504 1.0480 1.5090 0.0510  0.1883  -0.1510 1237 GLN B CG    
3892 C  CD    . GLN B 20  ? 1.5623 1.2681 1.7366 0.0620  0.2051  -0.1483 1237 GLN B CD    
3893 O  OE1   . GLN B 20  ? 1.5867 1.3091 1.7974 0.0733  0.2074  -0.1366 1237 GLN B OE1   
3894 N  NE2   . GLN B 20  ? 1.6740 1.3685 1.8210 0.0587  0.2168  -0.1587 1237 GLN B NE2   
3895 N  N     . VAL B 21  ? 0.9683 0.7457 1.1809 0.0461  0.1256  -0.1103 1238 VAL B N     
3896 C  CA    . VAL B 21  ? 0.9776 0.7823 1.2154 0.0511  0.1131  -0.0959 1238 VAL B CA    
3897 C  C     . VAL B 21  ? 0.9459 0.7713 1.1723 0.0429  0.0992  -0.0944 1238 VAL B C     
3898 O  O     . VAL B 21  ? 0.8260 0.6742 1.0686 0.0469  0.0944  -0.0864 1238 VAL B O     
3899 C  CB    . VAL B 21  ? 1.0443 0.8450 1.2932 0.0526  0.1050  -0.0884 1238 VAL B CB    
3900 C  CG1   . VAL B 21  ? 0.9974 0.8248 1.2587 0.0526  0.0874  -0.0760 1238 VAL B CG1   
3901 C  CG2   . VAL B 21  ? 1.1099 0.8991 1.3819 0.0653  0.1173  -0.0840 1238 VAL B CG2   
3902 N  N     . ILE B 22  ? 0.9220 0.7394 1.1207 0.0312  0.0928  -0.1023 1239 ILE B N     
3903 C  CA    . ILE B 22  ? 0.8666 0.7029 1.0549 0.0242  0.0800  -0.1005 1239 ILE B CA    
3904 C  C     . ILE B 22  ? 0.9507 0.7901 1.1271 0.0235  0.0876  -0.1055 1239 ILE B C     
3905 O  O     . ILE B 22  ? 0.9882 0.8465 1.1642 0.0212  0.0792  -0.1011 1239 ILE B O     
3906 C  CB    . ILE B 22  ? 0.8752 0.7051 1.0418 0.0124  0.0689  -0.1056 1239 ILE B CB    
3907 C  CG1   . ILE B 22  ? 0.8793 0.6834 1.0206 0.0061  0.0779  -0.1197 1239 ILE B CG1   
3908 C  CG2   . ILE B 22  ? 0.7866 0.6171 0.9668 0.0129  0.0609  -0.0984 1239 ILE B CG2   
3909 C  CD1   . ILE B 22  ? 0.8987 0.6964 1.0229 -0.0056 0.0669  -0.1247 1239 ILE B CD1   
3910 N  N     . THR B 23  ? 0.9201 0.7403 1.0856 0.0255  0.1039  -0.1146 1240 THR B N     
3911 C  CA    . THR B 23  ? 0.8410 0.6635 0.9951 0.0256  0.1129  -0.1182 1240 THR B CA    
3912 C  C     . THR B 23  ? 0.9155 0.7522 1.0995 0.0365  0.1228  -0.1103 1240 THR B C     
3913 O  O     . THR B 23  ? 0.9875 0.8408 1.1752 0.0364  0.1216  -0.1061 1240 THR B O     
3914 C  CB    . THR B 23  ? 0.7965 0.5918 0.9219 0.0225  0.1271  -0.1319 1240 THR B CB    
3915 O  OG1   . THR B 23  ? 0.9094 0.6884 1.0488 0.0309  0.1420  -0.1341 1240 THR B OG1   
3916 C  CG2   . THR B 23  ? 0.7566 0.5389 0.8521 0.0106  0.1165  -0.1406 1240 THR B CG2   
3917 N  N     . LYS B 24  ? 0.8386 0.6685 1.0447 0.0459  0.1331  -0.1083 1241 LYS B N     
3918 C  CA    . LYS B 24  ? 0.8959 0.7415 1.1335 0.0562  0.1417  -0.1004 1241 LYS B CA    
3919 C  C     . LYS B 24  ? 0.9669 0.8398 1.2316 0.0585  0.1255  -0.0876 1241 LYS B C     
3920 O  O     . LYS B 24  ? 1.0182 0.9088 1.3105 0.0655  0.1288  -0.0803 1241 LYS B O     
3921 C  CB    . LYS B 24  ? 0.7674 0.5980 1.0222 0.0667  0.1586  -0.1018 1241 LYS B CB    
3922 C  CG    . LYS B 24  ? 0.8020 0.6019 1.0269 0.0638  0.1739  -0.1159 1241 LYS B CG    
3923 C  CD    . LYS B 24  ? 0.9554 0.7424 1.1967 0.0754  0.1961  -0.1180 1241 LYS B CD    
3924 C  CE    . LYS B 24  ? 1.0874 0.8517 1.2965 0.0723  0.2141  -0.1315 1241 LYS B CE    
3925 N  NZ    . LYS B 24  ? 1.0815 0.8403 1.3102 0.0845  0.2380  -0.1320 1241 LYS B NZ    
3926 N  N     . GLY B 25  ? 0.9296 0.8064 1.1873 0.0529  0.1084  -0.0847 1242 GLY B N     
3927 C  CA    . GLY B 25  ? 1.0089 0.9102 1.2844 0.0534  0.0922  -0.0741 1242 GLY B CA    
3928 C  C     . GLY B 25  ? 1.0645 0.9802 1.3270 0.0456  0.0822  -0.0737 1242 GLY B C     
3929 O  O     . GLY B 25  ? 1.1147 1.0482 1.3877 0.0449  0.0678  -0.0661 1242 GLY B O     
3930 N  N     . GLU B 26  ? 1.1191 1.0264 1.3574 0.0398  0.0893  -0.0816 1243 GLU B N     
3931 C  CA    . GLU B 26  ? 1.1167 1.0364 1.3429 0.0333  0.0814  -0.0807 1243 GLU B CA    
3932 C  C     . GLU B 26  ? 1.0896 1.0157 1.3058 0.0268  0.0631  -0.0783 1243 GLU B C     
3933 O  O     . GLU B 26  ? 1.0967 1.0393 1.3163 0.0244  0.0526  -0.0732 1243 GLU B O     
3934 C  CB    . GLU B 26  ? 1.0290 0.9695 1.2812 0.0378  0.0825  -0.0730 1243 GLU B CB    
3935 C  CG    . GLU B 26  ? 1.1430 1.0790 1.3994 0.0416  0.1018  -0.0759 1243 GLU B CG    
3936 C  CD    . GLU B 26  ? 1.0780 1.0356 1.3609 0.0444  0.1032  -0.0685 1243 GLU B CD    
3937 O  OE1   . GLU B 26  ? 1.0453 1.0003 1.3351 0.0479  0.1202  -0.0700 1243 GLU B OE1   
3938 O  OE2   . GLU B 26  ? 0.8648 0.8408 1.1615 0.0428  0.0883  -0.0617 1243 GLU B OE2   
3939 N  N     . MET B 27  ? 1.0437 0.9561 1.2490 0.0241  0.0600  -0.0821 1244 MET B N     
3940 C  CA    . MET B 27  ? 0.9418 0.8594 1.1403 0.0185  0.0443  -0.0795 1244 MET B CA    
3941 C  C     . MET B 27  ? 0.9270 0.8370 1.0957 0.0086  0.0396  -0.0868 1244 MET B C     
3942 O  O     . MET B 27  ? 0.9018 0.8226 1.0653 0.0038  0.0267  -0.0838 1244 MET B O     
3943 C  CB    . MET B 27  ? 0.7255 0.6339 0.9330 0.0212  0.0433  -0.0777 1244 MET B CB    
3944 C  CG    . MET B 27  ? 0.7550 0.6764 0.9912 0.0301  0.0402  -0.0673 1244 MET B CG    
3945 S  SD    . MET B 27  ? 1.0352 0.9564 1.2754 0.0296  0.0283  -0.0608 1244 MET B SD    
3946 C  CE    . MET B 27  ? 1.0533 0.9466 1.2760 0.0247  0.0373  -0.0706 1244 MET B CE    
3947 N  N     . ILE B 28  ? 0.8951 0.7877 1.0443 0.0059  0.0499  -0.0962 1245 ILE B N     
3948 C  CA    . ILE B 28  ? 0.9156 0.7971 1.0359 -0.0035 0.0456  -0.1045 1245 ILE B CA    
3949 C  C     . ILE B 28  ? 0.9338 0.8048 1.0333 -0.0045 0.0567  -0.1117 1245 ILE B C     
3950 O  O     . ILE B 28  ? 1.0276 0.8896 1.1326 0.0015  0.0718  -0.1140 1245 ILE B O     
3951 C  CB    . ILE B 28  ? 0.9467 0.8102 1.0626 -0.0065 0.0464  -0.1103 1245 ILE B CB    
3952 C  CG1   . ILE B 28  ? 0.9437 0.8174 1.0747 -0.0074 0.0342  -0.1029 1245 ILE B CG1   
3953 C  CG2   . ILE B 28  ? 0.8650 0.7112 0.9496 -0.0158 0.0466  -0.1223 1245 ILE B CG2   
3954 C  CD1   . ILE B 28  ? 0.8791 0.7700 1.0050 -0.0126 0.0198  -0.0988 1245 ILE B CD1   
3955 N  N     . GLU B 29  ? 0.8554 0.7273 0.9308 -0.0117 0.0497  -0.1149 1246 GLU B N     
3956 C  CA    . GLU B 29  ? 0.9087 0.7660 0.9568 -0.0140 0.0594  -0.1230 1246 GLU B CA    
3957 C  C     . GLU B 29  ? 0.9963 0.8414 1.0156 -0.0237 0.0510  -0.1319 1246 GLU B C     
3958 O  O     . GLU B 29  ? 1.0310 0.8874 1.0488 -0.0292 0.0355  -0.1290 1246 GLU B O     
3959 C  CB    . GLU B 29  ? 0.9222 0.7915 0.9663 -0.0127 0.0605  -0.1178 1246 GLU B CB    
3960 C  CG    . GLU B 29  ? 0.9473 0.8010 0.9626 -0.0140 0.0726  -0.1249 1246 GLU B CG    
3961 C  CD    . GLU B 29  ? 1.0433 0.8816 1.0629 -0.0080 0.0922  -0.1300 1246 GLU B CD    
3962 O  OE1   . GLU B 29  ? 1.1307 0.9475 1.1222 -0.0108 0.1004  -0.1404 1246 GLU B OE1   
3963 O  OE2   . GLU B 29  ? 1.0082 0.8559 1.0593 -0.0002 0.0991  -0.1236 1246 GLU B OE2   
3964 N  N     . TYR B 30  ? 1.1064 0.9289 1.1032 -0.0258 0.0613  -0.1429 1247 TYR B N     
3965 C  CA    . TYR B 30  ? 1.1251 0.9342 1.0955 -0.0357 0.0530  -0.1527 1247 TYR B CA    
3966 C  C     . TYR B 30  ? 1.1641 0.9800 1.1094 -0.0414 0.0429  -0.1526 1247 TYR B C     
3967 O  O     . TYR B 30  ? 1.2057 1.0302 1.1484 -0.0374 0.0468  -0.1469 1247 TYR B O     
3968 C  CB    . TYR B 30  ? 1.1020 0.8828 1.0544 -0.0362 0.0673  -0.1654 1247 TYR B CB    
3969 C  CG    . TYR B 30  ? 1.1727 0.9450 1.1497 -0.0312 0.0754  -0.1655 1247 TYR B CG    
3970 C  CD1   . TYR B 30  ? 1.0847 0.8575 1.0738 -0.0359 0.0648  -0.1649 1247 TYR B CD1   
3971 C  CD2   . TYR B 30  ? 1.2820 1.0462 1.2715 -0.0213 0.0939  -0.1651 1247 TYR B CD2   
3972 C  CE1   . TYR B 30  ? 1.1112 0.8754 1.1221 -0.0308 0.0721  -0.1638 1247 TYR B CE1   
3973 C  CE2   . TYR B 30  ? 1.3265 1.0830 1.3393 -0.0158 0.1008  -0.1641 1247 TYR B CE2   
3974 C  CZ    . TYR B 30  ? 1.3084 1.0644 1.3310 -0.0205 0.0897  -0.1632 1247 TYR B CZ    
3975 O  OH    . TYR B 30  ? 1.4070 1.1540 1.4518 -0.0145 0.0968  -0.1612 1247 TYR B OH    
3976 N  N     . TYR B 31  ? 1.0857 0.8983 1.0141 -0.0509 0.0294  -0.1583 1248 TYR B N     
3977 C  CA    . TYR B 31  ? 1.1621 0.9869 1.0745 -0.0562 0.0149  -0.1555 1248 TYR B CA    
3978 C  C     . TYR B 31  ? 1.1385 0.9488 1.0205 -0.0664 0.0066  -0.1671 1248 TYR B C     
3979 O  O     . TYR B 31  ? 1.2552 1.0541 1.1390 -0.0717 0.0051  -0.1748 1248 TYR B O     
3980 C  CB    . TYR B 31  ? 1.2376 1.0868 1.1761 -0.0562 0.0006  -0.1448 1248 TYR B CB    
3981 C  CG    . TYR B 31  ? 1.2739 1.1378 1.2011 -0.0587 -0.0122 -0.1394 1248 TYR B CG    
3982 C  CD1   . TYR B 31  ? 1.2753 1.1416 1.1911 -0.0542 -0.0066 -0.1349 1248 TYR B CD1   
3983 C  CD2   . TYR B 31  ? 1.1971 1.0721 1.1260 -0.0653 -0.0292 -0.1383 1248 TYR B CD2   
3984 C  CE1   . TYR B 31  ? 1.2933 1.1715 1.1985 -0.0559 -0.0180 -0.1293 1248 TYR B CE1   
3985 C  CE2   . TYR B 31  ? 1.2476 1.1359 1.1677 -0.0667 -0.0406 -0.1329 1248 TYR B CE2   
3986 C  CZ    . TYR B 31  ? 1.3004 1.1896 1.2080 -0.0618 -0.0352 -0.1283 1248 TYR B CZ    
3987 O  OH    . TYR B 31  ? 1.3387 1.2400 1.2375 -0.0626 -0.0467 -0.1223 1248 TYR B OH    
3988 N  N     . ASP B 32  ? 1.2077 1.0191 1.0622 -0.0696 0.0002  -0.1678 1249 ASP B N     
3989 C  CA    . ASP B 32  ? 1.2324 1.0288 1.0525 -0.0790 -0.0074 -0.1794 1249 ASP B CA    
3990 C  C     . ASP B 32  ? 1.1403 0.9487 0.9658 -0.0883 -0.0283 -0.1798 1249 ASP B C     
3991 O  O     . ASP B 32  ? 1.0723 0.8729 0.8708 -0.0968 -0.0386 -0.1881 1249 ASP B O     
3992 C  CB    . ASP B 32  ? 1.3687 1.1604 1.1548 -0.0780 -0.0056 -0.1793 1249 ASP B CB    
3993 C  CG    . ASP B 32  ? 1.5288 1.3437 1.3222 -0.0754 -0.0164 -0.1662 1249 ASP B CG    
3994 O  OD1   . ASP B 32  ? 1.6192 1.4539 1.4462 -0.0718 -0.0206 -0.1563 1249 ASP B OD1   
3995 O  OD2   . ASP B 32  ? 1.5967 1.4089 1.3605 -0.0766 -0.0201 -0.1658 1249 ASP B OD2   
3996 N  N     . VAL B 33  ? 1.1681 0.9948 1.0278 -0.0870 -0.0346 -0.1713 1250 VAL B N     
3997 C  CA    . VAL B 33  ? 1.1903 1.0274 1.0612 -0.0956 -0.0512 -0.1720 1250 VAL B CA    
3998 C  C     . VAL B 33  ? 1.1556 0.9851 1.0497 -0.0965 -0.0450 -0.1748 1250 VAL B C     
3999 O  O     . VAL B 33  ? 1.1939 1.0298 1.1135 -0.0885 -0.0366 -0.1668 1250 VAL B O     
4000 C  CB    . VAL B 33  ? 1.2138 1.0790 1.1046 -0.0932 -0.0637 -0.1590 1250 VAL B CB    
4001 C  CG1   . VAL B 33  ? 1.1542 1.0306 1.0567 -0.1026 -0.0802 -0.1600 1250 VAL B CG1   
4002 C  CG2   . VAL B 33  ? 1.2503 1.1218 1.1201 -0.0901 -0.0672 -0.1542 1250 VAL B CG2   
4003 N  N     . SER B 34  ? 1.1068 0.9226 0.9923 -0.1065 -0.0497 -0.1857 1251 SER B N     
4004 C  CA    . SER B 34  ? 1.1670 0.9718 1.0724 -0.1070 -0.0419 -0.1885 1251 SER B CA    
4005 C  C     . SER B 34  ? 1.0716 0.8980 1.0116 -0.1059 -0.0490 -0.1769 1251 SER B C     
4006 O  O     . SER B 34  ? 1.1998 1.0470 1.1465 -0.1094 -0.0632 -0.1710 1251 SER B O     
4007 C  CB    . SER B 34  ? 1.3840 1.1676 1.2724 -0.1190 -0.0453 -0.2034 1251 SER B CB    
4008 O  OG    . SER B 34  ? 1.4847 1.2513 1.3352 -0.1220 -0.0437 -0.2143 1251 SER B OG    
4009 N  N     . GLY B 35  ? 0.9033 0.7244 0.8653 -0.1005 -0.0384 -0.1734 1252 GLY B N     
4010 C  CA    . GLY B 35  ? 0.8110 0.6499 0.8036 -0.0979 -0.0423 -0.1619 1252 GLY B CA    
4011 C  C     . GLY B 35  ? 0.9451 0.8028 0.9512 -0.0870 -0.0404 -0.1494 1252 GLY B C     
4012 O  O     . GLY B 35  ? 1.1008 0.9716 1.1310 -0.0833 -0.0420 -0.1398 1252 GLY B O     
4013 N  N     . CYS B 36  ? 0.9085 0.7672 0.8995 -0.0818 -0.0366 -0.1491 1253 CYS B N     
4014 C  CA    . CYS B 36  ? 0.9202 0.7976 0.9232 -0.0730 -0.0367 -0.1376 1253 CYS B CA    
4015 C  C     . CYS B 36  ? 1.0828 0.9518 1.0846 -0.0638 -0.0216 -0.1370 1253 CYS B C     
4016 O  O     . CYS B 36  ? 1.2037 1.0555 1.1846 -0.0644 -0.0131 -0.1455 1253 CYS B O     
4017 C  CB    . CYS B 36  ? 0.9610 0.8526 0.9508 -0.0757 -0.0483 -0.1352 1253 CYS B CB    
4018 S  SG    . CYS B 36  ? 1.0207 0.9217 1.0108 -0.0876 -0.0662 -0.1377 1253 CYS B SG    
4019 N  N     . TYR B 37  ? 1.0162 0.8974 1.0406 -0.0553 -0.0182 -0.1271 1254 TYR B N     
4020 C  CA    . TYR B 37  ? 0.9467 0.8225 0.9776 -0.0464 -0.0042 -0.1254 1254 TYR B CA    
4021 C  C     . TYR B 37  ? 0.9663 0.8622 1.0117 -0.0399 -0.0068 -0.1146 1254 TYR B C     
4022 O  O     . TYR B 37  ? 1.0711 0.9826 1.1301 -0.0401 -0.0168 -0.1075 1254 TYR B O     
4023 C  CB    . TYR B 37  ? 0.9551 0.8208 1.0041 -0.0423 0.0044  -0.1254 1254 TYR B CB    
4024 C  CG    . TYR B 37  ? 0.9926 0.8372 1.0304 -0.0492 0.0067  -0.1358 1254 TYR B CG    
4025 C  CD1   . TYR B 37  ? 1.0400 0.8625 1.0603 -0.0491 0.0189  -0.1461 1254 TYR B CD1   
4026 C  CD2   . TYR B 37  ? 0.9159 0.7617 0.9606 -0.0560 -0.0025 -0.1357 1254 TYR B CD2   
4027 C  CE1   . TYR B 37  ? 1.0718 0.8730 1.0811 -0.0559 0.0210  -0.1567 1254 TYR B CE1   
4028 C  CE2   . TYR B 37  ? 1.0697 0.8955 1.1055 -0.0632 -0.0005 -0.1456 1254 TYR B CE2   
4029 C  CZ    . TYR B 37  ? 1.0953 0.8982 1.1130 -0.0633 0.0109  -0.1564 1254 TYR B CZ    
4030 O  OH    . TYR B 37  ? 1.1011 0.8823 1.1090 -0.0711 0.0126  -0.1671 1254 TYR B OH    
4031 N  N     . ILE B 38  ? 0.8930 0.7876 0.9361 -0.0343 0.0032  -0.1137 1255 ILE B N     
4032 C  CA    . ILE B 38  ? 0.9531 0.8648 1.0101 -0.0287 0.0020  -0.1043 1255 ILE B CA    
4033 C  C     . ILE B 38  ? 0.9144 0.8330 1.0002 -0.0217 0.0049  -0.0978 1255 ILE B C     
4034 O  O     . ILE B 38  ? 0.8717 0.7807 0.9659 -0.0170 0.0163  -0.0997 1255 ILE B O     
4035 C  CB    . ILE B 38  ? 0.8804 0.7879 0.9257 -0.0258 0.0125  -0.1054 1255 ILE B CB    
4036 C  CG1   . ILE B 38  ? 0.8698 0.7689 0.8831 -0.0322 0.0095  -0.1115 1255 ILE B CG1   
4037 C  CG2   . ILE B 38  ? 0.7268 0.6517 0.7888 -0.0210 0.0108  -0.0959 1255 ILE B CG2   
4038 C  CD1   . ILE B 38  ? 0.8195 0.7080 0.8164 -0.0298 0.0230  -0.1144 1255 ILE B CD1   
4039 N  N     . LEU B 39  ? 0.8754 0.8103 0.9758 -0.0206 -0.0053 -0.0899 1256 LEU B N     
4040 C  CA    . LEU B 39  ? 0.8633 0.8067 0.9891 -0.0137 -0.0041 -0.0828 1256 LEU B CA    
4041 C  C     . LEU B 39  ? 0.8772 0.8294 1.0118 -0.0086 0.0008  -0.0787 1256 LEU B C     
4042 O  O     . LEU B 39  ? 0.8921 0.8563 1.0261 -0.0095 -0.0059 -0.0745 1256 LEU B O     
4043 C  CB    . LEU B 39  ? 0.6491 0.6049 0.7845 -0.0146 -0.0163 -0.0765 1256 LEU B CB    
4044 C  CG    . LEU B 39  ? 0.7258 0.6765 0.8524 -0.0213 -0.0227 -0.0797 1256 LEU B CG    
4045 C  CD1   . LEU B 39  ? 0.5779 0.5415 0.7169 -0.0203 -0.0318 -0.0721 1256 LEU B CD1   
4046 C  CD2   . LEU B 39  ? 0.5536 0.4866 0.6796 -0.0221 -0.0150 -0.0853 1256 LEU B CD2   
4047 N  N     . ARG B 40  ? 0.7883 0.7343 0.9323 -0.0034 0.0131  -0.0798 1257 ARG B N     
4048 C  CA    . ARG B 40  ? 0.6961 0.6517 0.8539 0.0013  0.0186  -0.0754 1257 ARG B CA    
4049 C  C     . ARG B 40  ? 0.8423 0.8143 1.0244 0.0054  0.0101  -0.0670 1257 ARG B C     
4050 O  O     . ARG B 40  ? 0.8907 0.8647 1.0779 0.0056  0.0020  -0.0645 1257 ARG B O     
4051 C  CB    . ARG B 40  ? 0.6851 0.6306 0.8493 0.0062  0.0348  -0.0787 1257 ARG B CB    
4052 C  CG    . ARG B 40  ? 0.7649 0.6905 0.9030 0.0024  0.0430  -0.0883 1257 ARG B CG    
4053 C  CD    . ARG B 40  ? 0.9031 0.8193 1.0444 0.0074  0.0608  -0.0914 1257 ARG B CD    
4054 N  NE    . ARG B 40  ? 0.9331 0.8624 1.0864 0.0101  0.0649  -0.0858 1257 ARG B NE    
4055 C  CZ    . ARG B 40  ? 0.9951 0.9241 1.1635 0.0159  0.0797  -0.0850 1257 ARG B CZ    
4056 N  NH1   . ARG B 40  ? 0.8989 0.8147 1.0714 0.0206  0.0920  -0.0895 1257 ARG B NH1   
4057 N  NH2   . ARG B 40  ? 1.0990 1.0409 1.2796 0.0172  0.0826  -0.0796 1257 ARG B NH2   
4058 N  N     . HIS B 41  ? 0.7506 0.7340 0.9471 0.0083  0.0119  -0.0626 1258 HIS B N     
4059 C  CA    . HIS B 41  ? 0.7471 0.7462 0.9625 0.0108  0.0014  -0.0555 1258 HIS B CA    
4060 C  C     . HIS B 41  ? 0.7261 0.7260 0.9599 0.0164  0.0004  -0.0523 1258 HIS B C     
4061 O  O     . HIS B 41  ? 0.6190 0.6261 0.8580 0.0171  -0.0106 -0.0478 1258 HIS B O     
4062 C  CB    . HIS B 41  ? 0.7986 0.8093 1.0281 0.0121  0.0034  -0.0520 1258 HIS B CB    
4063 C  CG    . HIS B 41  ? 0.9549 0.9665 1.2044 0.0173  0.0155  -0.0513 1258 HIS B CG    
4064 N  ND1   . HIS B 41  ? 0.9579 0.9831 1.2361 0.0221  0.0126  -0.0457 1258 HIS B ND1   
4065 C  CD2   . HIS B 41  ? 1.0234 1.0245 1.2689 0.0187  0.0308  -0.0555 1258 HIS B CD2   
4066 C  CE1   . HIS B 41  ? 0.9470 0.9714 1.2408 0.0265  0.0257  -0.0460 1258 HIS B CE1   
4067 N  NE2   . HIS B 41  ? 1.0256 1.0348 1.2995 0.0247  0.0377  -0.0520 1258 HIS B NE2   
4068 N  N     . TRP B 42  ? 0.9273 0.9181 1.1685 0.0207  0.0120  -0.0545 1259 TRP B N     
4069 C  CA    . TRP B 42  ? 0.8433 0.8355 1.1046 0.0274  0.0113  -0.0500 1259 TRP B CA    
4070 C  C     . TRP B 42  ? 0.7778 0.7625 1.0296 0.0257  0.0040  -0.0495 1259 TRP B C     
4071 O  O     . TRP B 42  ? 0.8403 0.8313 1.1053 0.0299  -0.0032 -0.0430 1259 TRP B O     
4072 C  CB    . TRP B 42  ? 0.8134 0.7968 1.0859 0.0331  0.0266  -0.0524 1259 TRP B CB    
4073 C  CG    . TRP B 42  ? 0.8381 0.8275 1.1379 0.0417  0.0255  -0.0455 1259 TRP B CG    
4074 C  CD1   . TRP B 42  ? 0.7354 0.7129 1.0392 0.0464  0.0293  -0.0450 1259 TRP B CD1   
4075 C  CD2   . TRP B 42  ? 0.8527 0.8614 1.1792 0.0467  0.0192  -0.0378 1259 TRP B CD2   
4076 N  NE1   . TRP B 42  ? 0.6361 0.6243 0.9665 0.0545  0.0256  -0.0367 1259 TRP B NE1   
4077 C  CE2   . TRP B 42  ? 0.7742 0.7823 1.1194 0.0548  0.0190  -0.0324 1259 TRP B CE2   
4078 C  CE3   . TRP B 42  ? 0.7864 0.8121 1.1232 0.0448  0.0135  -0.0349 1259 TRP B CE3   
4079 C  CZ2   . TRP B 42  ? 0.7718 0.7972 1.1452 0.0612  0.0121  -0.0242 1259 TRP B CZ2   
4080 C  CZ3   . TRP B 42  ? 0.6749 0.7174 1.0405 0.0504  0.0070  -0.0277 1259 TRP B CZ3   
4081 C  CH2   . TRP B 42  ? 0.6663 0.7092 1.0495 0.0585  0.0057  -0.0224 1259 TRP B CH2   
4082 N  N     . SER B 43  ? 0.7049 0.6775 0.9340 0.0193  0.0047  -0.0558 1260 SER B N     
4083 C  CA    . SER B 43  ? 0.8748 0.8421 1.0976 0.0169  -0.0022 -0.0547 1260 SER B CA    
4084 C  C     . SER B 43  ? 0.8578 0.8362 1.0727 0.0123  -0.0150 -0.0517 1260 SER B C     
4085 O  O     . SER B 43  ? 0.8645 0.8456 1.0826 0.0129  -0.0223 -0.0468 1260 SER B O     
4086 C  CB    . SER B 43  ? 0.7754 0.7234 0.9804 0.0118  0.0043  -0.0630 1260 SER B CB    
4087 O  OG    . SER B 43  ? 0.7101 0.6553 0.8949 0.0051  0.0051  -0.0698 1260 SER B OG    
4088 N  N     . PHE B 44  ? 0.8305 0.8152 1.0359 0.0084  -0.0171 -0.0538 1261 PHE B N     
4089 C  CA    . PHE B 44  ? 0.7828 0.7779 0.9821 0.0051  -0.0283 -0.0509 1261 PHE B CA    
4090 C  C     . PHE B 44  ? 0.7151 0.7226 0.9300 0.0100  -0.0357 -0.0434 1261 PHE B C     
4091 O  O     . PHE B 44  ? 0.6326 0.6455 0.8438 0.0086  -0.0443 -0.0402 1261 PHE B O     
4092 C  CB    . PHE B 44  ? 0.7025 0.7016 0.8902 0.0012  -0.0288 -0.0536 1261 PHE B CB    
4093 C  CG    . PHE B 44  ? 0.7662 0.7740 0.9469 -0.0020 -0.0392 -0.0512 1261 PHE B CG    
4094 C  CD1   . PHE B 44  ? 0.7556 0.7596 0.9206 -0.0077 -0.0426 -0.0545 1261 PHE B CD1   
4095 C  CD2   . PHE B 44  ? 0.6728 0.6925 0.8635 0.0008  -0.0460 -0.0458 1261 PHE B CD2   
4096 C  CE1   . PHE B 44  ? 0.6836 0.6962 0.8445 -0.0097 -0.0513 -0.0518 1261 PHE B CE1   
4097 C  CE2   . PHE B 44  ? 0.5306 0.5569 0.7150 -0.0013 -0.0542 -0.0438 1261 PHE B CE2   
4098 C  CZ    . PHE B 44  ? 0.6293 0.6524 0.7995 -0.0061 -0.0565 -0.0465 1261 PHE B CZ    
4099 N  N     . ALA B 45  ? 0.5922 0.6045 0.8245 0.0156  -0.0325 -0.0406 1262 ALA B N     
4100 C  CA    . ALA B 45  ? 0.5686 0.5925 0.8149 0.0200  -0.0410 -0.0337 1262 ALA B CA    
4101 C  C     . ALA B 45  ? 0.5702 0.5897 0.8182 0.0231  -0.0446 -0.0292 1262 ALA B C     
4102 O  O     . ALA B 45  ? 0.7328 0.7593 0.9810 0.0243  -0.0539 -0.0242 1262 ALA B O     
4103 C  CB    . ALA B 45  ? 0.6019 0.6336 0.8692 0.0250  -0.0376 -0.0316 1262 ALA B CB    
4104 N  N     . ILE B 46  ? 0.5889 0.5958 0.8374 0.0244  -0.0369 -0.0308 1263 ILE B N     
4105 C  CA    . ILE B 46  ? 0.8256 0.8267 1.0744 0.0267  -0.0398 -0.0259 1263 ILE B CA    
4106 C  C     . ILE B 46  ? 0.7845 0.7855 1.0173 0.0206  -0.0459 -0.0261 1263 ILE B C     
4107 O  O     . ILE B 46  ? 0.7956 0.8003 1.0278 0.0223  -0.0526 -0.0200 1263 ILE B O     
4108 C  CB    . ILE B 46  ? 0.8216 0.8064 1.0734 0.0287  -0.0295 -0.0280 1263 ILE B CB    
4109 C  CG1   . ILE B 46  ? 0.4910 0.4758 0.7585 0.0347  -0.0212 -0.0288 1263 ILE B CG1   
4110 C  CG2   . ILE B 46  ? 0.7124 0.6921 0.9694 0.0333  -0.0322 -0.0203 1263 ILE B CG2   
4111 C  CD1   . ILE B 46  ? 0.6675 0.6340 0.9359 0.0365  -0.0089 -0.0330 1263 ILE B CD1   
4112 N  N     . TRP B 47  ? 0.7250 0.7223 0.9446 0.0137  -0.0436 -0.0329 1264 TRP B N     
4113 C  CA    . TRP B 47  ? 0.6197 0.6198 0.8272 0.0081  -0.0496 -0.0329 1264 TRP B CA    
4114 C  C     . TRP B 47  ? 0.7299 0.7437 0.9376 0.0097  -0.0583 -0.0286 1264 TRP B C     
4115 O  O     . TRP B 47  ? 0.8131 0.8297 1.0157 0.0087  -0.0633 -0.0252 1264 TRP B O     
4116 C  CB    . TRP B 47  ? 0.6746 0.6707 0.8690 0.0009  -0.0474 -0.0405 1264 TRP B CB    
4117 C  CG    . TRP B 47  ? 0.8166 0.8166 1.0018 -0.0047 -0.0534 -0.0403 1264 TRP B CG    
4118 C  CD1   . TRP B 47  ? 0.8234 0.8313 1.0003 -0.0084 -0.0580 -0.0422 1264 TRP B CD1   
4119 C  CD2   . TRP B 47  ? 0.8844 0.8806 1.0696 -0.0068 -0.0545 -0.0374 1264 TRP B CD2   
4120 N  NE1   . TRP B 47  ? 0.8690 0.8794 1.0421 -0.0125 -0.0621 -0.0409 1264 TRP B NE1   
4121 C  CE2   . TRP B 47  ? 0.9139 0.9174 1.0921 -0.0119 -0.0597 -0.0380 1264 TRP B CE2   
4122 C  CE3   . TRP B 47  ? 0.7553 0.7423 0.9465 -0.0047 -0.0510 -0.0338 1264 TRP B CE3   
4123 C  CZ2   . TRP B 47  ? 0.8669 0.8700 1.0453 -0.0154 -0.0610 -0.0353 1264 TRP B CZ2   
4124 C  CZ3   . TRP B 47  ? 0.8033 0.7885 0.9929 -0.0083 -0.0523 -0.0309 1264 TRP B CZ3   
4125 C  CH2   . TRP B 47  ? 0.8442 0.8379 1.0280 -0.0139 -0.0570 -0.0318 1264 TRP B CH2   
4126 N  N     . LYS B 48  ? 0.6745 0.6962 0.8876 0.0117  -0.0594 -0.0292 1265 LYS B N     
4127 C  CA    . LYS B 48  ? 0.6983 0.7312 0.9102 0.0121  -0.0675 -0.0267 1265 LYS B CA    
4128 C  C     . LYS B 48  ? 0.7711 0.8080 0.9890 0.0173  -0.0735 -0.0200 1265 LYS B C     
4129 O  O     . LYS B 48  ? 0.6089 0.6506 0.8199 0.0171  -0.0800 -0.0176 1265 LYS B O     
4130 C  CB    . LYS B 48  ? 0.6687 0.7072 0.8857 0.0120  -0.0663 -0.0293 1265 LYS B CB    
4131 C  CG    . LYS B 48  ? 0.8006 0.8496 1.0212 0.0133  -0.0740 -0.0268 1265 LYS B CG    
4132 C  CD    . LYS B 48  ? 1.0050 1.0577 1.2292 0.0114  -0.0713 -0.0299 1265 LYS B CD    
4133 C  CE    . LYS B 48  ? 1.2922 1.3545 1.5291 0.0136  -0.0772 -0.0275 1265 LYS B CE    
4134 N  NZ    . LYS B 48  ? 1.4591 1.5244 1.7127 0.0149  -0.0712 -0.0280 1265 LYS B NZ    
4135 N  N     . ALA B 49  ? 0.7375 0.7715 0.9672 0.0224  -0.0713 -0.0169 1266 ALA B N     
4136 C  CA    . ALA B 49  ? 0.6750 0.7116 0.9091 0.0279  -0.0775 -0.0096 1266 ALA B CA    
4137 C  C     . ALA B 49  ? 0.7722 0.8020 0.9947 0.0268  -0.0779 -0.0062 1266 ALA B C     
4138 O  O     . ALA B 49  ? 0.8028 0.8365 1.0188 0.0285  -0.0845 -0.0016 1266 ALA B O     
4139 C  CB    . ALA B 49  ? 0.6979 0.7329 0.9489 0.0341  -0.0744 -0.0065 1266 ALA B CB    
4140 N  N     . ILE B 50  ? 0.7306 0.7498 0.9500 0.0235  -0.0705 -0.0086 1267 ILE B N     
4141 C  CA    . ILE B 50  ? 0.7082 0.7214 0.9184 0.0210  -0.0699 -0.0057 1267 ILE B CA    
4142 C  C     . ILE B 50  ? 0.7165 0.7371 0.9155 0.0167  -0.0742 -0.0072 1267 ILE B C     
4143 O  O     . ILE B 50  ? 0.7180 0.7403 0.9106 0.0179  -0.0774 -0.0021 1267 ILE B O     
4144 C  CB    . ILE B 50  ? 0.6039 0.6041 0.8140 0.0169  -0.0615 -0.0095 1267 ILE B CB    
4145 C  CG1   . ILE B 50  ? 0.5489 0.5405 0.7704 0.0224  -0.0563 -0.0076 1267 ILE B CG1   
4146 C  CG2   . ILE B 50  ? 0.7043 0.6988 0.9080 0.0136  -0.0603 -0.0060 1267 ILE B CG2   
4147 C  CD1   . ILE B 50  ? 0.5159 0.4927 0.7371 0.0183  -0.0470 -0.0136 1267 ILE B CD1   
4148 N  N     . ARG B 51  ? 0.6738 0.6984 0.8701 0.0122  -0.0737 -0.0137 1268 ARG B N     
4149 C  CA    . ARG B 51  ? 0.8397 0.8713 1.0273 0.0087  -0.0773 -0.0152 1268 ARG B CA    
4150 C  C     . ARG B 51  ? 0.9070 0.9459 1.0917 0.0129  -0.0839 -0.0112 1268 ARG B C     
4151 O  O     . ARG B 51  ? 0.9532 0.9940 1.1301 0.0125  -0.0855 -0.0087 1268 ARG B O     
4152 C  CB    . ARG B 51  ? 0.8334 0.8679 1.0195 0.0049  -0.0765 -0.0218 1268 ARG B CB    
4153 C  CG    . ARG B 51  ? 0.6931 0.7352 0.8718 0.0026  -0.0804 -0.0230 1268 ARG B CG    
4154 C  CD    . ARG B 51  ? 0.7792 0.8235 0.9565 0.0005  -0.0800 -0.0278 1268 ARG B CD    
4155 N  NE    . ARG B 51  ? 1.0330 1.0821 1.2145 0.0040  -0.0829 -0.0270 1268 ARG B NE    
4156 C  CZ    . ARG B 51  ? 1.0550 1.1051 1.2387 0.0033  -0.0813 -0.0299 1268 ARG B CZ    
4157 N  NH1   . ARG B 51  ? 1.0274 1.0735 1.2067 -0.0002 -0.0768 -0.0338 1268 ARG B NH1   
4158 N  NH2   . ARG B 51  ? 1.1756 1.2304 1.3652 0.0058  -0.0844 -0.0288 1268 ARG B NH2   
4159 N  N     . ASN B 52  ? 0.7942 0.8372 0.9850 0.0165  -0.0875 -0.0111 1269 ASN B N     
4160 C  CA    . ASN B 52  ? 0.7820 0.8312 0.9690 0.0196  -0.0948 -0.0088 1269 ASN B CA    
4161 C  C     . ASN B 52  ? 0.6848 0.7313 0.8671 0.0239  -0.0975 -0.0020 1269 ASN B C     
4162 O  O     . ASN B 52  ? 0.5360 0.5841 0.7072 0.0247  -0.1009 -0.0001 1269 ASN B O     
4163 C  CB    . ASN B 52  ? 0.7554 0.8103 0.9525 0.0213  -0.0984 -0.0106 1269 ASN B CB    
4164 C  CG    . ASN B 52  ? 0.7185 0.7759 0.9168 0.0171  -0.0958 -0.0165 1269 ASN B CG    
4165 O  OD1   . ASN B 52  ? 0.8571 0.9123 1.0478 0.0133  -0.0923 -0.0192 1269 ASN B OD1   
4166 N  ND2   . ASN B 52  ? 0.6480 0.7101 0.8561 0.0177  -0.0975 -0.0181 1269 ASN B ND2   
4167 N  N     . TRP B 53  ? 0.6847 0.7258 0.8740 0.0270  -0.0953 0.0021  1270 TRP B N     
4168 C  CA    . TRP B 53  ? 0.5799 0.6172 0.7634 0.0316  -0.0978 0.0099  1270 TRP B CA    
4169 C  C     . TRP B 53  ? 0.7536 0.7868 0.9245 0.0289  -0.0939 0.0119  1270 TRP B C     
4170 O  O     . TRP B 53  ? 0.8266 0.8603 0.9855 0.0312  -0.0972 0.0158  1270 TRP B O     
4171 C  CB    . TRP B 53  ? 0.7350 0.7656 0.9290 0.0354  -0.0946 0.0143  1270 TRP B CB    
4172 C  CG    . TRP B 53  ? 0.8742 0.9008 1.0615 0.0409  -0.0980 0.0234  1270 TRP B CG    
4173 C  CD1   . TRP B 53  ? 0.8069 0.8381 0.9950 0.0471  -0.1069 0.0284  1270 TRP B CD1   
4174 C  CD2   . TRP B 53  ? 0.8164 0.8337 0.9942 0.0406  -0.0929 0.0290  1270 TRP B CD2   
4175 N  NE1   . TRP B 53  ? 0.7891 0.8135 0.9663 0.0512  -0.1078 0.0371  1270 TRP B NE1   
4176 C  CE2   . TRP B 53  ? 0.7771 0.7926 0.9482 0.0473  -0.0985 0.0379  1270 TRP B CE2   
4177 C  CE3   . TRP B 53  ? 0.8638 0.8744 1.0386 0.0349  -0.0844 0.0276  1270 TRP B CE3   
4178 C  CZ2   . TRP B 53  ? 0.7432 0.7492 0.9035 0.0489  -0.0946 0.0459  1270 TRP B CZ2   
4179 C  CZ3   . TRP B 53  ? 0.9291 0.9313 1.0960 0.0359  -0.0805 0.0352  1270 TRP B CZ3   
4180 C  CH2   . TRP B 53  ? 0.8762 0.8756 1.0354 0.0430  -0.0849 0.0446  1270 TRP B CH2   
4181 N  N     . PHE B 54  ? 0.7224 0.7515 0.8958 0.0236  -0.0867 0.0088  1271 PHE B N     
4182 C  CA    . PHE B 54  ? 0.7893 0.8156 0.9554 0.0203  -0.0822 0.0110  1271 PHE B CA    
4183 C  C     . PHE B 54  ? 0.8683 0.9023 1.0260 0.0186  -0.0844 0.0084  1271 PHE B C     
4184 O  O     . PHE B 54  ? 0.8627 0.8964 1.0116 0.0194  -0.0828 0.0125  1271 PHE B O     
4185 C  CB    . PHE B 54  ? 0.8618 0.8825 1.0345 0.0142  -0.0754 0.0075  1271 PHE B CB    
4186 C  CG    . PHE B 54  ? 0.8020 0.8201 0.9715 0.0100  -0.0704 0.0103  1271 PHE B CG    
4187 C  CD1   . PHE B 54  ? 0.6807 0.6907 0.8479 0.0123  -0.0668 0.0182  1271 PHE B CD1   
4188 C  CD2   . PHE B 54  ? 0.8124 0.8365 0.9822 0.0039  -0.0692 0.0057  1271 PHE B CD2   
4189 C  CE1   . PHE B 54  ? 0.7418 0.7495 0.9079 0.0080  -0.0611 0.0213  1271 PHE B CE1   
4190 C  CE2   . PHE B 54  ? 0.8186 0.8421 0.9889 -0.0002 -0.0644 0.0085  1271 PHE B CE2   
4191 C  CZ    . PHE B 54  ? 0.8574 0.8726 1.0263 0.0015  -0.0598 0.0162  1271 PHE B CZ    
4192 N  N     . ASP B 55  ? 0.9283 0.9686 1.0886 0.0166  -0.0871 0.0020  1272 ASP B N     
4193 C  CA    . ASP B 55  ? 0.8092 0.8558 0.9627 0.0155  -0.0886 -0.0005 1272 ASP B CA    
4194 C  C     . ASP B 55  ? 0.7709 0.8183 0.9139 0.0205  -0.0932 0.0026  1272 ASP B C     
4195 O  O     . ASP B 55  ? 0.8113 0.8597 0.9452 0.0211  -0.0916 0.0040  1272 ASP B O     
4196 C  CB    . ASP B 55  ? 0.7488 0.8002 0.9067 0.0130  -0.0906 -0.0070 1272 ASP B CB    
4197 C  CG    . ASP B 55  ? 0.7437 0.8005 0.8972 0.0110  -0.0903 -0.0094 1272 ASP B CG    
4198 O  OD1   . ASP B 55  ? 0.6004 0.6587 0.7571 0.0067  -0.0871 -0.0110 1272 ASP B OD1   
4199 O  OD2   . ASP B 55  ? 0.8258 0.8850 0.9730 0.0138  -0.0937 -0.0099 1272 ASP B OD2   
4200 N  N     . ALA B 56  ? 0.7359 0.7829 0.8802 0.0242  -0.0990 0.0036  1273 ALA B N     
4201 C  CA    . ALA B 56  ? 0.7561 0.8030 0.8885 0.0286  -0.1049 0.0061  1273 ALA B CA    
4202 C  C     . ALA B 56  ? 0.8069 0.8479 0.9279 0.0312  -0.1013 0.0132  1273 ALA B C     
4203 O  O     . ALA B 56  ? 0.8365 0.8766 0.9430 0.0331  -0.1016 0.0142  1273 ALA B O     
4204 C  CB    . ALA B 56  ? 0.6633 0.7120 0.8017 0.0318  -0.1128 0.0066  1273 ALA B CB    
4205 N  N     . GLU B 57  ? 0.8002 0.8360 0.9272 0.0313  -0.0970 0.0182  1274 GLU B N     
4206 C  CA    . GLU B 57  ? 0.8857 0.9147 1.0025 0.0333  -0.0924 0.0259  1274 GLU B CA    
4207 C  C     . GLU B 57  ? 0.8357 0.8661 0.9467 0.0301  -0.0851 0.0253  1274 GLU B C     
4208 O  O     . GLU B 57  ? 0.9775 1.0061 1.0734 0.0330  -0.0839 0.0286  1274 GLU B O     
4209 C  CB    . GLU B 57  ? 0.9487 0.9705 1.0754 0.0330  -0.0877 0.0307  1274 GLU B CB    
4210 C  CG    . GLU B 57  ? 1.0539 1.0740 1.1860 0.0382  -0.0941 0.0338  1274 GLU B CG    
4211 C  CD    . GLU B 57  ? 1.1716 1.1905 1.2886 0.0446  -0.1013 0.0399  1274 GLU B CD    
4212 O  OE1   . GLU B 57  ? 1.1945 1.2084 1.2960 0.0458  -0.0978 0.0452  1274 GLU B OE1   
4213 O  OE2   . GLU B 57  ? 1.2127 1.2359 1.3335 0.0483  -0.1105 0.0395  1274 GLU B OE2   
4214 N  N     . ILE B 58  ? 0.7096 0.7434 0.8323 0.0244  -0.0803 0.0211  1275 ILE B N     
4215 C  CA    . ILE B 58  ? 0.7645 0.8012 0.8860 0.0213  -0.0733 0.0217  1275 ILE B CA    
4216 C  C     . ILE B 58  ? 0.8329 0.8756 0.9462 0.0230  -0.0754 0.0178  1275 ILE B C     
4217 O  O     . ILE B 58  ? 0.8310 0.8759 0.9401 0.0230  -0.0696 0.0195  1275 ILE B O     
4218 C  CB    . ILE B 58  ? 0.6379 0.6775 0.7745 0.0142  -0.0693 0.0182  1275 ILE B CB    
4219 C  CG1   . ILE B 58  ? 0.6082 0.6538 0.7512 0.0121  -0.0745 0.0102  1275 ILE B CG1   
4220 C  CG2   . ILE B 58  ? 0.6131 0.6440 0.7565 0.0123  -0.0660 0.0216  1275 ILE B CG2   
4221 C  CD1   . ILE B 58  ? 0.6031 0.6524 0.7574 0.0052  -0.0720 0.0060  1275 ILE B CD1   
4222 N  N     . THR B 59  ? 0.7643 0.8095 0.8766 0.0246  -0.0829 0.0126  1276 THR B N     
4223 C  CA    . THR B 59  ? 0.7581 0.8065 0.8618 0.0265  -0.0851 0.0086  1276 THR B CA    
4224 C  C     . THR B 59  ? 0.8049 0.8477 0.8898 0.0318  -0.0862 0.0121  1276 THR B C     
4225 O  O     . THR B 59  ? 0.8755 0.9181 0.9501 0.0337  -0.0822 0.0117  1276 THR B O     
4226 C  CB    . THR B 59  ? 0.6403 0.6916 0.7497 0.0258  -0.0926 0.0024  1276 THR B CB    
4227 O  OG1   . THR B 59  ? 0.7735 0.8294 0.8964 0.0211  -0.0904 -0.0010 1276 THR B OG1   
4228 C  CG2   . THR B 59  ? 0.6608 0.7124 0.7595 0.0283  -0.0962 -0.0018 1276 THR B CG2   
4229 N  N     . ARG B 60  ? 0.8015 0.8393 0.8813 0.0346  -0.0911 0.0159  1277 ARG B N     
4230 C  CA    . ARG B 60  ? 0.8672 0.8986 0.9266 0.0396  -0.0926 0.0203  1277 ARG B CA    
4231 C  C     . ARG B 60  ? 0.9108 0.9384 0.9625 0.0402  -0.0817 0.0266  1277 ARG B C     
4232 O  O     . ARG B 60  ? 0.9157 0.9388 0.9482 0.0439  -0.0793 0.0282  1277 ARG B O     
4233 C  CB    . ARG B 60  ? 1.0209 1.0489 1.0795 0.0426  -0.1004 0.0247  1277 ARG B CB    
4234 C  CG    . ARG B 60  ? 1.1495 1.1700 1.1855 0.0480  -0.1033 0.0307  1277 ARG B CG    
4235 C  CD    . ARG B 60  ? 1.1222 1.1400 1.1616 0.0512  -0.1102 0.0371  1277 ARG B CD    
4236 N  NE    . ARG B 60  ? 1.2909 1.3064 1.3451 0.0496  -0.1026 0.0426  1277 ARG B NE    
4237 C  CZ    . ARG B 60  ? 1.3019 1.3094 1.3489 0.0511  -0.0947 0.0513  1277 ARG B CZ    
4238 N  NH1   . ARG B 60  ? 1.2682 1.2696 1.2921 0.0547  -0.0926 0.0563  1277 ARG B NH1   
4239 N  NH2   . ARG B 60  ? 1.1961 1.2007 1.2585 0.0486  -0.0882 0.0550  1277 ARG B NH2   
4240 N  N     . LEU B 61  ? 0.9886 1.0177 1.0553 0.0362  -0.0745 0.0296  1278 LEU B N     
4241 C  CA    . LEU B 61  ? 0.9827 1.0091 1.0466 0.0356  -0.0632 0.0361  1278 LEU B CA    
4242 C  C     . LEU B 61  ? 0.9407 0.9731 1.0051 0.0345  -0.0560 0.0332  1278 LEU B C     
4243 O  O     . LEU B 61  ? 0.9109 0.9412 0.9696 0.0354  -0.0461 0.0388  1278 LEU B O     
4244 C  CB    . LEU B 61  ? 0.9656 0.9914 1.0474 0.0305  -0.0585 0.0393  1278 LEU B CB    
4245 C  CG    . LEU B 61  ? 0.9459 0.9625 1.0261 0.0327  -0.0612 0.0456  1278 LEU B CG    
4246 C  CD1   . LEU B 61  ? 0.9924 1.0083 1.0924 0.0272  -0.0584 0.0450  1278 LEU B CD1   
4247 C  CD2   . LEU B 61  ? 0.8577 0.8653 0.9213 0.0368  -0.0552 0.0555  1278 LEU B CD2   
4248 N  N     . GLY B 62  ? 0.8655 0.9053 0.9374 0.0331  -0.0599 0.0254  1279 GLY B N     
4249 C  CA    . GLY B 62  ? 0.5066 0.5532 0.5824 0.0326  -0.0536 0.0229  1279 GLY B CA    
4250 C  C     . GLY B 62  ? 0.8481 0.9047 0.9467 0.0268  -0.0522 0.0202  1279 GLY B C     
4251 O  O     . GLY B 62  ? 0.9758 1.0398 1.0807 0.0266  -0.0474 0.0189  1279 GLY B O     
4252 N  N     . VAL B 63  ? 0.7885 0.8456 0.8990 0.0223  -0.0565 0.0192  1280 VAL B N     
4253 C  CA    . VAL B 63  ? 0.6621 0.7276 0.7909 0.0164  -0.0572 0.0155  1280 VAL B CA    
4254 C  C     . VAL B 63  ? 0.6138 0.6833 0.7432 0.0173  -0.0643 0.0086  1280 VAL B C     
4255 O  O     . VAL B 63  ? 0.7937 0.8584 0.9138 0.0204  -0.0703 0.0061  1280 VAL B O     
4256 C  CB    . VAL B 63  ? 0.6465 0.7083 0.7851 0.0113  -0.0581 0.0164  1280 VAL B CB    
4257 C  CG1   . VAL B 63  ? 0.5725 0.6422 0.7277 0.0044  -0.0589 0.0123  1280 VAL B CG1   
4258 C  CG2   . VAL B 63  ? 0.5184 0.5733 0.6541 0.0113  -0.0511 0.0241  1280 VAL B CG2   
4259 N  N     . LYS B 64  ? 0.6715 0.7498 0.8128 0.0142  -0.0642 0.0059  1281 LYS B N     
4260 C  CA    . LYS B 64  ? 0.7563 0.8378 0.8977 0.0153  -0.0697 0.0006  1281 LYS B CA    
4261 C  C     . LYS B 64  ? 0.6436 0.7299 0.7972 0.0097  -0.0734 -0.0025 1281 LYS B C     
4262 O  O     . LYS B 64  ? 0.8051 0.8958 0.9692 0.0048  -0.0711 -0.0011 1281 LYS B O     
4263 C  CB    . LYS B 64  ? 0.8421 0.9287 0.9823 0.0193  -0.0661 0.0005  1281 LYS B CB    
4264 C  CG    . LYS B 64  ? 0.8803 0.9594 1.0033 0.0256  -0.0648 0.0004  1281 LYS B CG    
4265 C  CD    . LYS B 64  ? 1.0916 1.1741 1.2137 0.0293  -0.0562 0.0031  1281 LYS B CD    
4266 C  CE    . LYS B 64  ? 1.1679 1.2409 1.2694 0.0353  -0.0537 0.0026  1281 LYS B CE    
4267 N  NZ    . LYS B 64  ? 1.2568 1.3324 1.3576 0.0386  -0.0423 0.0067  1281 LYS B NZ    
4268 N  N     . GLU B 65  ? 0.5473 0.6322 0.6988 0.0101  -0.0790 -0.0068 1282 GLU B N     
4269 C  CA    . GLU B 65  ? 0.5905 0.6775 0.7491 0.0053  -0.0825 -0.0101 1282 GLU B CA    
4270 C  C     . GLU B 65  ? 0.7014 0.7967 0.8652 0.0048  -0.0841 -0.0112 1282 GLU B C     
4271 O  O     . GLU B 65  ? 0.7946 0.8913 0.9548 0.0094  -0.0843 -0.0114 1282 GLU B O     
4272 C  CB    . GLU B 65  ? 0.4522 0.5327 0.6060 0.0060  -0.0866 -0.0133 1282 GLU B CB    
4273 C  CG    . GLU B 65  ? 0.5470 0.6270 0.7054 0.0013  -0.0885 -0.0165 1282 GLU B CG    
4274 C  CD    . GLU B 65  ? 0.6439 0.7178 0.8000 0.0023  -0.0904 -0.0187 1282 GLU B CD    
4275 O  OE1   . GLU B 65  ? 0.6697 0.7406 0.8220 0.0062  -0.0915 -0.0175 1282 GLU B OE1   
4276 O  OE2   . GLU B 65  ? 0.6039 0.6762 0.7620 -0.0009 -0.0908 -0.0217 1282 GLU B OE2   
4277 N  N     . CYS B 66  ? 0.7356 0.8361 0.9077 -0.0006 -0.0854 -0.0120 1283 CYS B N     
4278 C  CA    . CYS B 66  ? 0.8041 0.9137 0.9822 -0.0015 -0.0885 -0.0124 1283 CYS B CA    
4279 C  C     . CYS B 66  ? 0.7950 0.9037 0.9739 -0.0075 -0.0929 -0.0159 1283 CYS B C     
4280 O  O     . CYS B 66  ? 0.7251 0.8260 0.9009 -0.0107 -0.0924 -0.0181 1283 CYS B O     
4281 C  CB    . CYS B 66  ? 0.7887 0.9088 0.9781 -0.0020 -0.0853 -0.0086 1283 CYS B CB    
4282 S  SG    . CYS B 66  ? 0.7787 0.9002 0.9780 -0.0104 -0.0835 -0.0079 1283 CYS B SG    
4283 N  N     . TYR B 67  ? 0.7312 0.8478 0.9140 -0.0090 -0.0973 -0.0161 1284 TYR B N     
4284 C  CA    . TYR B 67  ? 0.6899 0.8052 0.8706 -0.0151 -0.1019 -0.0197 1284 TYR B CA    
4285 C  C     . TYR B 67  ? 0.8524 0.9801 1.0417 -0.0178 -0.1070 -0.0185 1284 TYR B C     
4286 O  O     . TYR B 67  ? 1.0257 1.1592 1.2151 -0.0135 -0.1100 -0.0162 1284 TYR B O     
4287 C  CB    . TYR B 67  ? 0.6273 0.7347 0.7965 -0.0133 -0.1037 -0.0224 1284 TYR B CB    
4288 C  CG    . TYR B 67  ? 0.6430 0.7468 0.8066 -0.0192 -0.1071 -0.0265 1284 TYR B CG    
4289 C  CD1   . TYR B 67  ? 0.6234 0.7188 0.7850 -0.0237 -0.1045 -0.0302 1284 TYR B CD1   
4290 C  CD2   . TYR B 67  ? 0.5597 0.6677 0.7191 -0.0200 -0.1127 -0.0266 1284 TYR B CD2   
4291 C  CE1   . TYR B 67  ? 0.7315 0.8217 0.8858 -0.0293 -0.1068 -0.0349 1284 TYR B CE1   
4292 C  CE2   . TYR B 67  ? 0.6630 0.7666 0.8140 -0.0256 -0.1159 -0.0308 1284 TYR B CE2   
4293 C  CZ    . TYR B 67  ? 0.7573 0.8515 0.9052 -0.0304 -0.1126 -0.0355 1284 TYR B CZ    
4294 O  OH    . TYR B 67  ? 0.7576 0.8451 0.8949 -0.0360 -0.1149 -0.0408 1284 TYR B OH    
4295 N  N     . PHE B 68  ? 0.6654 0.7968 0.8624 -0.0253 -0.1087 -0.0200 1285 PHE B N     
4296 C  CA    . PHE B 68  ? 0.5059 0.6499 0.7124 -0.0299 -0.1155 -0.0196 1285 PHE B CA    
4297 C  C     . PHE B 68  ? 0.4835 0.6221 0.6784 -0.0352 -0.1224 -0.0248 1285 PHE B C     
4298 O  O     . PHE B 68  ? 0.5881 0.7130 0.7703 -0.0363 -0.1199 -0.0290 1285 PHE B O     
4299 C  CB    . PHE B 68  ? 0.7136 0.8641 0.9355 -0.0361 -0.1135 -0.0187 1285 PHE B CB    
4300 C  CG    . PHE B 68  ? 0.8300 0.9885 1.0643 -0.0313 -0.1067 -0.0128 1285 PHE B CG    
4301 C  CD1   . PHE B 68  ? 0.8112 0.9605 1.0383 -0.0254 -0.0986 -0.0109 1285 PHE B CD1   
4302 C  CD2   . PHE B 68  ? 0.8949 1.0703 1.1485 -0.0329 -0.1080 -0.0091 1285 PHE B CD2   
4303 C  CE1   . PHE B 68  ? 0.7957 0.9508 1.0313 -0.0210 -0.0915 -0.0058 1285 PHE B CE1   
4304 C  CE2   . PHE B 68  ? 0.7787 0.9610 1.0437 -0.0283 -0.0998 -0.0036 1285 PHE B CE2   
4305 C  CZ    . PHE B 68  ? 0.7560 0.9273 1.0104 -0.0223 -0.0912 -0.0021 1285 PHE B CZ    
4306 N  N     . PRO B 69  ? 0.6085 0.7574 0.8068 -0.0381 -0.1310 -0.0246 1286 PRO B N     
4307 C  CA    . PRO B 69  ? 0.7754 0.9179 0.9579 -0.0419 -0.1376 -0.0292 1286 PRO B CA    
4308 C  C     . PRO B 69  ? 0.7490 0.8806 0.9250 -0.0508 -0.1373 -0.0365 1286 PRO B C     
4309 O  O     . PRO B 69  ? 0.8052 0.9367 0.9919 -0.0558 -0.1343 -0.0378 1286 PRO B O     
4310 C  CB    . PRO B 69  ? 0.7858 0.9441 0.9757 -0.0429 -0.1480 -0.0263 1286 PRO B CB    
4311 C  CG    . PRO B 69  ? 0.8084 0.9793 1.0152 -0.0357 -0.1450 -0.0192 1286 PRO B CG    
4312 C  CD    . PRO B 69  ? 0.7617 0.9289 0.9769 -0.0362 -0.1352 -0.0193 1286 PRO B CD    
4313 N  N     . ILE B 70  ? 0.7474 0.8680 0.9043 -0.0524 -0.1395 -0.0412 1287 ILE B N     
4314 C  CA    . ILE B 70  ? 0.7766 0.8851 0.9239 -0.0605 -0.1396 -0.0491 1287 ILE B CA    
4315 C  C     . ILE B 70  ? 0.7958 0.9131 0.9479 -0.0695 -0.1499 -0.0521 1287 ILE B C     
4316 O  O     . ILE B 70  ? 0.8894 0.9978 1.0380 -0.0778 -0.1502 -0.0592 1287 ILE B O     
4317 C  CB    . ILE B 70  ? 0.8668 0.9610 0.9910 -0.0588 -0.1377 -0.0530 1287 ILE B CB    
4318 C  CG1   . ILE B 70  ? 0.8641 0.9421 0.9768 -0.0657 -0.1345 -0.0618 1287 ILE B CG1   
4319 C  CG2   . ILE B 70  ? 0.8374 0.9378 0.9503 -0.0583 -0.1473 -0.0515 1287 ILE B CG2   
4320 C  CD1   . ILE B 70  ? 0.9129 0.9789 1.0289 -0.0629 -0.1230 -0.0627 1287 ILE B CD1   
4321 N  N     . PHE B 71  ? 0.6557 0.7902 0.8166 -0.0680 -0.1588 -0.0471 1288 PHE B N     
4322 C  CA    . PHE B 71  ? 0.7269 0.8725 0.8931 -0.0762 -0.1711 -0.0495 1288 PHE B CA    
4323 C  C     . PHE B 71  ? 0.8227 0.9865 1.0179 -0.0789 -0.1727 -0.0452 1288 PHE B C     
4324 O  O     . PHE B 71  ? 0.8736 1.0474 1.0834 -0.0713 -0.1677 -0.0377 1288 PHE B O     
4325 C  CB    . PHE B 71  ? 0.8185 0.9716 0.9741 -0.0728 -0.1816 -0.0463 1288 PHE B CB    
4326 C  CG    . PHE B 71  ? 0.9445 1.0809 1.0703 -0.0735 -0.1827 -0.0516 1288 PHE B CG    
4327 C  CD1   . PHE B 71  ? 1.0048 1.1278 1.1163 -0.0828 -0.1839 -0.0614 1288 PHE B CD1   
4328 C  CD2   . PHE B 71  ? 0.8525 0.9857 0.9639 -0.0650 -0.1818 -0.0468 1288 PHE B CD2   
4329 C  CE1   . PHE B 71  ? 1.0247 1.1315 1.1071 -0.0831 -0.1836 -0.0664 1288 PHE B CE1   
4330 C  CE2   . PHE B 71  ? 0.8430 0.9606 0.9264 -0.0656 -0.1815 -0.0510 1288 PHE B CE2   
4331 C  CZ    . PHE B 71  ? 0.9967 1.1012 1.0649 -0.0745 -0.1821 -0.0609 1288 PHE B CZ    
4332 N  N     . VAL B 72  ? 0.8624 1.0305 1.0660 -0.0899 -0.1797 -0.0501 1289 VAL B N     
4333 C  CA    . VAL B 72  ? 0.8902 1.0768 1.1234 -0.0945 -0.1820 -0.0465 1289 VAL B CA    
4334 C  C     . VAL B 72  ? 0.9658 1.1663 1.2033 -0.1025 -0.1987 -0.0490 1289 VAL B C     
4335 O  O     . VAL B 72  ? 0.9528 1.1423 1.1740 -0.1113 -0.2052 -0.0578 1289 VAL B O     
4336 C  CB    . VAL B 72  ? 0.6536 0.8298 0.8952 -0.1019 -0.1729 -0.0505 1289 VAL B CB    
4337 C  CG1   . VAL B 72  ? 0.7007 0.8947 0.9734 -0.1081 -0.1739 -0.0470 1289 VAL B CG1   
4338 C  CG2   . VAL B 72  ? 0.7170 0.8803 0.9527 -0.0931 -0.1583 -0.0473 1289 VAL B CG2   
4339 N  N     . SER B 73  ? 0.8686 1.0929 1.1273 -0.0995 -0.2061 -0.0416 1290 SER B N     
4340 C  CA    . SER B 73  ? 1.0900 1.3231 1.3472 -0.1088 -0.2233 -0.0461 1290 SER B CA    
4341 C  C     . SER B 73  ? 1.1323 1.3747 1.4149 -0.1216 -0.2259 -0.0496 1290 SER B C     
4342 O  O     . SER B 73  ? 0.9931 1.2384 1.2967 -0.1216 -0.2143 -0.0462 1290 SER B O     
4343 C  CB    . SER B 73  ? 1.1540 1.4079 1.4177 -0.1031 -0.2367 -0.0389 1290 SER B CB    
4344 O  OG    . SER B 73  ? 0.9562 1.2359 1.2555 -0.1050 -0.2413 -0.0332 1290 SER B OG    
4345 N  N     . ARG B 74  ? 1.1359 1.3826 1.4157 -0.1329 -0.2416 -0.0563 1291 ARG B N     
4346 C  CA    . ARG B 74  ? 1.0715 1.3210 1.3695 -0.1479 -0.2450 -0.0627 1291 ARG B CA    
4347 C  C     . ARG B 74  ? 1.0208 1.2908 1.3593 -0.1484 -0.2384 -0.0549 1291 ARG B C     
4348 O  O     . ARG B 74  ? 1.0432 1.3067 1.3948 -0.1567 -0.2300 -0.0579 1291 ARG B O     
4349 C  CB    . ARG B 74  ? 1.0092 1.2678 1.3032 -0.1587 -0.2663 -0.0690 1291 ARG B CB    
4350 N  N     . ALA B 75  ? 0.9656 1.2592 1.3240 -0.1393 -0.2411 -0.0445 1292 ALA B N     
4351 C  CA    . ALA B 75  ? 0.8272 1.1426 1.2256 -0.1394 -0.2347 -0.0367 1292 ALA B CA    
4352 C  C     . ALA B 75  ? 0.9571 1.2597 1.3572 -0.1331 -0.2132 -0.0329 1292 ALA B C     
4353 O  O     . ALA B 75  ? 1.0058 1.3111 1.4280 -0.1398 -0.2046 -0.0320 1292 ALA B O     
4354 C  CB    . ALA B 75  ? 0.5743 0.9164 0.9915 -0.1294 -0.2419 -0.0264 1292 ALA B CB    
4355 N  N     . ALA B 76  ? 1.0922 1.3806 1.4690 -0.1203 -0.2043 -0.0303 1293 ALA B N     
4356 C  CA    . ALA B 76  ? 1.1376 1.4125 1.5120 -0.1143 -0.1856 -0.0273 1293 ALA B CA    
4357 C  C     . ALA B 76  ? 1.0224 1.2789 1.3928 -0.1253 -0.1794 -0.0343 1293 ALA B C     
4358 O  O     . ALA B 76  ? 0.9853 1.2407 1.3710 -0.1264 -0.1668 -0.0307 1293 ALA B O     
4359 C  CB    . ALA B 76  ? 1.1591 1.4179 1.5045 -0.1015 -0.1799 -0.0263 1293 ALA B CB    
4360 N  N     . LEU B 77  ? 0.9568 1.1988 1.3068 -0.1338 -0.1882 -0.0443 1294 LEU B N     
4361 C  CA    . LEU B 77  ? 0.9544 1.1746 1.2964 -0.1432 -0.1818 -0.0519 1294 LEU B CA    
4362 C  C     . LEU B 77  ? 1.0305 1.2607 1.4018 -0.1569 -0.1833 -0.0531 1294 LEU B C     
4363 O  O     . LEU B 77  ? 0.9593 1.1840 1.3438 -0.1586 -0.1700 -0.0498 1294 LEU B O     
4364 C  CB    . LEU B 77  ? 0.8652 1.0661 1.1757 -0.1477 -0.1900 -0.0629 1294 LEU B CB    
4365 C  CG    . LEU B 77  ? 0.8123 0.9840 1.1051 -0.1513 -0.1795 -0.0701 1294 LEU B CG    
4366 C  CD1   . LEU B 77  ? 0.6093 0.7710 0.8997 -0.1399 -0.1625 -0.0631 1294 LEU B CD1   
4367 C  CD2   . LEU B 77  ? 0.8583 1.0111 1.1179 -0.1530 -0.1857 -0.0802 1294 LEU B CD2   
4368 N  N     . GLU B 78  ? 1.0463 1.2920 1.4293 -0.1670 -0.1996 -0.0571 1295 GLU B N     
4369 C  CA    . GLU B 78  ? 1.0576 1.3091 1.4656 -0.1830 -0.2029 -0.0611 1295 GLU B CA    
4370 C  C     . GLU B 78  ? 1.0970 1.3741 1.5450 -0.1819 -0.1966 -0.0501 1295 GLU B C     
4371 O  O     . GLU B 78  ? 1.1230 1.4267 1.5981 -0.1870 -0.2079 -0.0476 1295 GLU B O     
4372 C  CB    . GLU B 78  ? 1.1322 1.3902 1.5365 -0.1949 -0.2239 -0.0703 1295 GLU B CB    
4373 C  CG    . GLU B 78  ? 1.2356 1.4715 1.5971 -0.1927 -0.2306 -0.0795 1295 GLU B CG    
4374 C  CD    . GLU B 78  ? 1.3511 1.5833 1.7029 -0.2079 -0.2484 -0.0920 1295 GLU B CD    
4375 O  OE1   . GLU B 78  ? 1.4418 1.6638 1.8021 -0.2220 -0.2473 -0.0996 1295 GLU B OE1   
4376 O  OE2   . GLU B 78  ? 1.3817 1.6196 1.7155 -0.2059 -0.2634 -0.0942 1295 GLU B OE2   
4377 N  N     . ARG B 79  ? 1.1700 1.4388 1.6214 -0.1748 -0.1778 -0.0434 1296 ARG B N     
4378 C  CA    . ARG B 79  ? 1.1921 1.4811 1.6777 -0.1726 -0.1677 -0.0327 1296 ARG B CA    
4379 C  C     . ARG B 79  ? 1.1892 1.4599 1.6748 -0.1725 -0.1481 -0.0293 1296 ARG B C     
4380 O  O     . ARG B 79  ? 1.2483 1.5094 1.7433 -0.1854 -0.1454 -0.0334 1296 ARG B O     
4381 C  CB    . ARG B 79  ? 1.1556 1.4618 1.6439 -0.1564 -0.1660 -0.0233 1296 ARG B CB    
4382 N  N     . ASP B 86  ? 1.1558 1.1699 1.4739 -0.2599 -0.1545 -0.1396 1303 ASP B N     
4383 C  CA    . ASP B 86  ? 1.1804 1.2054 1.5125 -0.2464 -0.1412 -0.1234 1303 ASP B CA    
4384 C  C     . ASP B 86  ? 1.3658 1.3951 1.6752 -0.2282 -0.1398 -0.1182 1303 ASP B C     
4385 O  O     . ASP B 86  ? 1.3167 1.3700 1.6374 -0.2189 -0.1402 -0.1071 1303 ASP B O     
4386 C  CB    . ASP B 86  ? 1.0914 1.1484 1.4598 -0.2512 -0.1450 -0.1136 1303 ASP B CB    
4387 N  N     . PHE B 87  ? 1.4420 1.4471 1.7205 -0.2236 -0.1375 -0.1268 1304 PHE B N     
4388 C  CA    . PHE B 87  ? 1.2806 1.2833 1.5342 -0.2081 -0.1354 -0.1247 1304 PHE B CA    
4389 C  C     . PHE B 87  ? 1.3446 1.3593 1.5819 -0.2097 -0.1516 -0.1314 1304 PHE B C     
4390 O  O     . PHE B 87  ? 1.1676 1.1722 1.3778 -0.2016 -0.1513 -0.1352 1304 PHE B O     
4391 C  CB    . PHE B 87  ? 0.9994 1.0178 1.2631 -0.1932 -0.1272 -0.1094 1304 PHE B CB    
4392 C  CG    . PHE B 87  ? 1.0086 1.0087 1.2724 -0.1851 -0.1103 -0.1029 1304 PHE B CG    
4393 C  CD1   . PHE B 87  ? 0.9727 0.9837 1.2573 -0.1806 -0.1018 -0.0899 1304 PHE B CD1   
4394 C  CD2   . PHE B 87  ? 1.1186 1.0911 1.3616 -0.1813 -0.1027 -0.1091 1304 PHE B CD2   
4395 C  CE1   . PHE B 87  ? 0.9659 0.9604 1.2491 -0.1728 -0.0874 -0.0830 1304 PHE B CE1   
4396 C  CE2   . PHE B 87  ? 1.1324 1.0896 1.3771 -0.1731 -0.0882 -0.1020 1304 PHE B CE2   
4397 C  CZ    . PHE B 87  ? 1.0422 1.0105 1.3064 -0.1690 -0.0813 -0.0888 1304 PHE B CZ    
4398 N  N     . ALA B 88  ? 1.6169 1.6532 1.8710 -0.2201 -0.1657 -0.1326 1305 ALA B N     
4399 C  CA    . ALA B 88  ? 1.6867 1.7389 1.9283 -0.2203 -0.1824 -0.1359 1305 ALA B CA    
4400 C  C     . ALA B 88  ? 1.7846 1.8149 1.9883 -0.2211 -0.1869 -0.1488 1305 ALA B C     
4401 O  O     . ALA B 88  ? 1.7995 1.8373 1.9846 -0.2126 -0.1929 -0.1470 1305 ALA B O     
4402 C  CB    . ALA B 88  ? 1.6477 1.7224 1.9145 -0.2345 -0.1977 -0.1376 1305 ALA B CB    
4403 N  N     . PRO B 89  ? 1.7616 1.7638 1.9513 -0.2303 -0.1832 -0.1613 1306 PRO B N     
4404 C  CA    . PRO B 89  ? 1.7156 1.6963 1.8667 -0.2296 -0.1858 -0.1734 1306 PRO B CA    
4405 C  C     . PRO B 89  ? 1.5769 1.5500 1.7071 -0.2124 -0.1748 -0.1681 1306 PRO B C     
4406 O  O     . PRO B 89  ? 1.6733 1.6394 1.7738 -0.2095 -0.1793 -0.1741 1306 PRO B O     
4407 C  CB    . PRO B 89  ? 1.7322 1.6819 1.8770 -0.2408 -0.1789 -0.1862 1306 PRO B CB    
4408 C  CG    . PRO B 89  ? 1.7270 1.6806 1.9068 -0.2451 -0.1706 -0.1788 1306 PRO B CG    
4409 C  CD    . PRO B 89  ? 1.7428 1.7328 1.9505 -0.2442 -0.1797 -0.1668 1306 PRO B CD    
4410 N  N     . GLU B 90  ? 1.3792 1.3538 1.5237 -0.2013 -0.1607 -0.1569 1307 GLU B N     
4411 C  CA    . GLU B 90  ? 1.2639 1.2291 1.3917 -0.1860 -0.1490 -0.1526 1307 GLU B CA    
4412 C  C     . GLU B 90  ? 1.1721 1.1613 1.3024 -0.1741 -0.1525 -0.1409 1307 GLU B C     
4413 O  O     . GLU B 90  ? 1.2584 1.2483 1.3932 -0.1621 -0.1417 -0.1320 1307 GLU B O     
4414 C  CB    . GLU B 90  ? 1.2072 1.1574 1.3470 -0.1809 -0.1320 -0.1479 1307 GLU B CB    
4415 N  N     . VAL B 91  ? 1.0586 1.0677 1.1876 -0.1768 -0.1676 -0.1401 1308 VAL B N     
4416 C  CA    . VAL B 91  ? 0.9737 1.0050 1.1074 -0.1656 -0.1708 -0.1287 1308 VAL B CA    
4417 C  C     . VAL B 91  ? 1.0254 1.0561 1.1305 -0.1630 -0.1798 -0.1325 1308 VAL B C     
4418 O  O     . VAL B 91  ? 1.0884 1.1204 1.1829 -0.1727 -0.1933 -0.1403 1308 VAL B O     
4419 C  CB    . VAL B 91  ? 1.0411 1.1006 1.2059 -0.1690 -0.1792 -0.1204 1308 VAL B CB    
4420 C  CG1   . VAL B 91  ? 1.0974 1.1782 1.2639 -0.1580 -0.1841 -0.1103 1308 VAL B CG1   
4421 C  CG2   . VAL B 91  ? 0.8503 0.9103 1.0412 -0.1685 -0.1672 -0.1139 1308 VAL B CG2   
4422 N  N     . ALA B 92  ? 0.9583 0.9873 1.0510 -0.1502 -0.1726 -0.1268 1309 ALA B N     
4423 C  CA    . ALA B 92  ? 1.0790 1.1062 1.1440 -0.1464 -0.1788 -0.1287 1309 ALA B CA    
4424 C  C     . ALA B 92  ? 1.1036 1.1571 1.1775 -0.1444 -0.1930 -0.1205 1309 ALA B C     
4425 O  O     . ALA B 92  ? 0.9345 1.0060 1.0316 -0.1378 -0.1912 -0.1097 1309 ALA B O     
4426 C  CB    . ALA B 92  ? 1.0680 1.0833 1.1189 -0.1340 -0.1650 -0.1252 1309 ALA B CB    
4427 N  N     . TRP B 93  ? 1.1833 1.2387 1.2386 -0.1503 -0.2073 -0.1258 1310 TRP B N     
4428 C  CA    . TRP B 93  ? 1.1765 1.2569 1.2404 -0.1491 -0.2227 -0.1184 1310 TRP B CA    
4429 C  C     . TRP B 93  ? 1.1512 1.2280 1.1852 -0.1417 -0.2266 -0.1162 1310 TRP B C     
4430 O  O     . TRP B 93  ? 1.1466 1.2073 1.1493 -0.1466 -0.2308 -0.1254 1310 TRP B O     
4431 C  CB    . TRP B 93  ? 1.1938 1.2839 1.2660 -0.1633 -0.2396 -0.1250 1310 TRP B CB    
4432 C  CG    . TRP B 93  ? 1.2121 1.3131 1.3203 -0.1699 -0.2375 -0.1236 1310 TRP B CG    
4433 C  CD1   . TRP B 93  ? 1.2409 1.3272 1.3549 -0.1805 -0.2324 -0.1326 1310 TRP B CD1   
4434 C  CD2   . TRP B 93  ? 1.2365 1.3644 1.3801 -0.1663 -0.2394 -0.1120 1310 TRP B CD2   
4435 N  NE1   . TRP B 93  ? 1.1990 1.3018 1.3501 -0.1841 -0.2308 -0.1268 1310 TRP B NE1   
4436 C  CE2   . TRP B 93  ? 1.1878 1.3165 1.3575 -0.1754 -0.2348 -0.1143 1310 TRP B CE2   
4437 C  CE3   . TRP B 93  ? 1.2800 1.4303 1.4358 -0.1560 -0.2435 -0.0999 1310 TRP B CE3   
4438 C  CZ2   . TRP B 93  ? 1.1868 1.3388 1.3936 -0.1745 -0.2337 -0.1047 1310 TRP B CZ2   
4439 C  CZ3   . TRP B 93  ? 1.2649 1.4379 1.4577 -0.1547 -0.2425 -0.0910 1310 TRP B CZ3   
4440 C  CH2   . TRP B 93  ? 1.2720 1.4461 1.4897 -0.1639 -0.2374 -0.0934 1310 TRP B CH2   
4441 N  N     . VAL B 94  ? 1.1014 1.1917 1.1437 -0.1299 -0.2245 -0.1042 1311 VAL B N     
4442 C  CA    . VAL B 94  ? 1.0717 1.1651 1.0922 -0.1235 -0.2320 -0.0993 1311 VAL B CA    
4443 C  C     . VAL B 94  ? 1.0466 1.1607 1.0745 -0.1291 -0.2528 -0.0973 1311 VAL B C     
4444 O  O     . VAL B 94  ? 1.0599 1.1963 1.1210 -0.1300 -0.2582 -0.0913 1311 VAL B O     
4445 C  CB    . VAL B 94  ? 1.0756 1.1754 1.1045 -0.1095 -0.2225 -0.0872 1311 VAL B CB    
4446 C  CG1   . VAL B 94  ? 1.0930 1.1931 1.0978 -0.1029 -0.2291 -0.0817 1311 VAL B CG1   
4447 C  CG2   . VAL B 94  ? 1.0459 1.1280 1.0722 -0.1047 -0.2033 -0.0890 1311 VAL B CG2   
4448 N  N     . THR B 95  ? 1.0553 1.1630 1.0524 -0.1324 -0.2645 -0.1016 1312 THR B N     
4449 C  CA    . THR B 95  ? 1.1959 1.3242 1.1987 -0.1370 -0.2861 -0.0990 1312 THR B CA    
4450 C  C     . THR B 95  ? 1.3945 1.5209 1.3658 -0.1310 -0.2956 -0.0944 1312 THR B C     
4451 O  O     . THR B 95  ? 1.5822 1.7245 1.5536 -0.1346 -0.3153 -0.0922 1312 THR B O     
4452 C  CB    . THR B 95  ? 1.2145 1.3400 1.2154 -0.1533 -0.2982 -0.1120 1312 THR B CB    
4453 O  OG1   . THR B 95  ? 1.2253 1.3261 1.1819 -0.1578 -0.2998 -0.1228 1312 THR B OG1   
4454 C  CG2   . THR B 95  ? 1.1722 1.2926 1.1976 -0.1604 -0.2869 -0.1182 1312 THR B CG2   
4455 N  N     . LYS B 96  ? 1.3341 1.4427 1.2799 -0.1220 -0.2826 -0.0920 1313 LYS B N     
4456 C  CA    . LYS B 96  ? 1.2896 1.3967 1.2072 -0.1154 -0.2902 -0.0854 1313 LYS B CA    
4457 C  C     . LYS B 96  ? 1.2141 1.3113 1.1258 -0.1025 -0.2724 -0.0772 1313 LYS B C     
4458 O  O     . LYS B 96  ? 1.1459 1.2270 1.0560 -0.1014 -0.2546 -0.0818 1313 LYS B O     
4459 C  CB    . LYS B 96  ? 1.3879 1.4757 1.2615 -0.1233 -0.2980 -0.0963 1313 LYS B CB    
4460 C  CG    . LYS B 96  ? 1.4775 1.5343 1.3214 -0.1238 -0.2793 -0.1059 1313 LYS B CG    
4461 C  CD    . LYS B 96  ? 1.5469 1.5840 1.3407 -0.1274 -0.2855 -0.1130 1313 LYS B CD    
4462 C  CE    . LYS B 96  ? 1.6168 1.6236 1.3856 -0.1315 -0.2683 -0.1266 1313 LYS B CE    
4463 N  NZ    . LYS B 96  ? 1.6367 1.6203 1.3584 -0.1269 -0.2603 -0.1278 1313 LYS B NZ    
4464 N  N     . SER B 97  ? 1.1724 1.2810 1.0853 -0.0928 -0.2776 -0.0644 1314 SER B N     
4465 C  CA    . SER B 97  ? 1.1026 1.2006 1.0037 -0.0813 -0.2638 -0.0562 1314 SER B CA    
4466 C  C     . SER B 97  ? 1.1945 1.2772 1.0514 -0.0805 -0.2687 -0.0562 1314 SER B C     
4467 O  O     . SER B 97  ? 1.1049 1.1981 0.9525 -0.0800 -0.2861 -0.0507 1314 SER B O     
4468 C  CB    . SER B 97  ? 0.9151 1.0326 0.8451 -0.0709 -0.2650 -0.0422 1314 SER B CB    
4469 O  OG    . SER B 97  ? 0.8881 1.0222 0.8182 -0.0697 -0.2842 -0.0351 1314 SER B OG    
4470 N  N     . GLY B 98  ? 1.1841 1.2422 1.0140 -0.0805 -0.2532 -0.0623 1315 GLY B N     
4471 C  CA    . GLY B 98  ? 1.2603 1.2994 1.0446 -0.0805 -0.2536 -0.0641 1315 GLY B CA    
4472 C  C     . GLY B 98  ? 1.3967 1.4326 1.1583 -0.0918 -0.2699 -0.0750 1315 GLY B C     
4473 O  O     . GLY B 98  ? 1.4731 1.4988 1.2326 -0.1010 -0.2660 -0.0884 1315 GLY B O     
4474 N  N     . ASP B 99  ? 1.4755 1.5198 1.2202 -0.0915 -0.2888 -0.0693 1316 ASP B N     
4475 C  CA    . ASP B 99  ? 1.4946 1.5405 1.2213 -0.1026 -0.3087 -0.0786 1316 ASP B CA    
4476 C  C     . ASP B 99  ? 1.4763 1.5531 1.2347 -0.1039 -0.3310 -0.0717 1316 ASP B C     
4477 O  O     . ASP B 99  ? 1.5121 1.5952 1.2619 -0.1137 -0.3507 -0.0786 1316 ASP B O     
4478 C  CB    . ASP B 99  ? 1.5684 1.5953 1.2409 -0.1021 -0.3135 -0.0794 1316 ASP B CB    
4479 C  CG    . ASP B 99  ? 1.6711 1.6666 1.3107 -0.1033 -0.2923 -0.0894 1316 ASP B CG    
4480 O  OD1   . ASP B 99  ? 1.6823 1.6704 1.3385 -0.1075 -0.2783 -0.0991 1316 ASP B OD1   
4481 O  OD2   . ASP B 99  ? 1.7590 1.7372 1.3564 -0.0995 -0.2891 -0.0869 1316 ASP B OD2   
4482 N  N     . SER B 100 ? 1.4942 1.5902 1.2890 -0.0943 -0.3280 -0.0585 1317 SER B N     
4483 C  CA    . SER B 100 ? 1.5441 1.6712 1.3757 -0.0936 -0.3454 -0.0505 1317 SER B CA    
4484 C  C     . SER B 100 ? 1.5639 1.7028 1.4351 -0.1018 -0.3427 -0.0583 1317 SER B C     
4485 O  O     . SER B 100 ? 1.6450 1.7796 1.5360 -0.0984 -0.3239 -0.0584 1317 SER B O     
4486 C  CB    . SER B 100 ? 1.5852 1.7232 1.4347 -0.0787 -0.3402 -0.0333 1317 SER B CB    
4487 O  OG    . SER B 100 ? 1.6684 1.8367 1.5565 -0.0758 -0.3543 -0.0242 1317 SER B OG    
4488 N  N     . GLU B 101 ? 1.4967 1.6507 1.3795 -0.1127 -0.3616 -0.0643 1318 GLU B N     
4489 C  CA    . GLU B 101 ? 1.4139 1.5792 1.3344 -0.1218 -0.3599 -0.0714 1318 GLU B CA    
4490 C  C     . GLU B 101 ? 1.4110 1.6032 1.3797 -0.1138 -0.3581 -0.0590 1318 GLU B C     
4491 O  O     . GLU B 101 ? 1.4884 1.6989 1.4669 -0.1056 -0.3691 -0.0465 1318 GLU B O     
4492 C  CB    . GLU B 101 ? 1.4182 1.5915 1.3372 -0.1368 -0.3813 -0.0817 1318 GLU B CB    
4493 C  CG    . GLU B 101 ? 1.5296 1.7011 1.4715 -0.1494 -0.3759 -0.0940 1318 GLU B CG    
4494 C  CD    . GLU B 101 ? 1.7320 1.8704 1.6371 -0.1574 -0.3658 -0.1098 1318 GLU B CD    
4495 O  OE1   . GLU B 101 ? 1.8351 1.9565 1.6957 -0.1584 -0.3719 -0.1144 1318 GLU B OE1   
4496 O  OE2   . GLU B 101 ? 1.7887 1.9174 1.7089 -0.1621 -0.3511 -0.1171 1318 GLU B OE2   
4497 N  N     . LEU B 102 ? 1.3575 1.5505 1.3550 -0.1156 -0.3434 -0.0620 1319 LEU B N     
4498 C  CA    . LEU B 102 ? 1.3837 1.5989 1.4245 -0.1078 -0.3382 -0.0511 1319 LEU B CA    
4499 C  C     . LEU B 102 ? 1.4003 1.6406 1.4788 -0.1174 -0.3508 -0.0529 1319 LEU B C     
4500 O  O     . LEU B 102 ? 1.4087 1.6444 1.4844 -0.1313 -0.3569 -0.0648 1319 LEU B O     
4501 C  CB    . LEU B 102 ? 1.3204 1.5222 1.3699 -0.1027 -0.3141 -0.0517 1319 LEU B CB    
4502 C  CG    . LEU B 102 ? 1.3158 1.5062 1.3485 -0.0888 -0.3022 -0.0429 1319 LEU B CG    
4503 C  CD1   . LEU B 102 ? 1.2538 1.4427 1.3094 -0.0826 -0.2832 -0.0400 1319 LEU B CD1   
4504 C  CD2   . LEU B 102 ? 1.3647 1.5716 1.4001 -0.0792 -0.3148 -0.0297 1319 LEU B CD2   
4505 N  N     . ALA B 103 ? 1.3869 1.6530 1.5020 -0.1096 -0.3533 -0.0409 1320 ALA B N     
4506 C  CA    . ALA B 103 ? 1.4050 1.6997 1.5591 -0.1173 -0.3668 -0.0400 1320 ALA B CA    
4507 C  C     . ALA B 103 ? 1.3255 1.6174 1.5016 -0.1282 -0.3564 -0.0491 1320 ALA B C     
4508 O  O     . ALA B 103 ? 1.3347 1.6268 1.5115 -0.1429 -0.3666 -0.0594 1320 ALA B O     
4509 C  CB    . ALA B 103 ? 1.4050 1.7261 1.5939 -0.1047 -0.3678 -0.0246 1320 ALA B CB    
4510 N  N     . GLU B 104 ? 1.2145 1.5026 1.4072 -0.1214 -0.3362 -0.0454 1321 GLU B N     
4511 C  CA    . GLU B 104 ? 1.1292 1.4107 1.3376 -0.1310 -0.3251 -0.0534 1321 GLU B CA    
4512 C  C     . GLU B 104 ? 1.0897 1.3391 1.2680 -0.1293 -0.3073 -0.0604 1321 GLU B C     
4513 O  O     . GLU B 104 ? 1.0221 1.2614 1.1858 -0.1171 -0.2965 -0.0547 1321 GLU B O     
4514 C  CB    . GLU B 104 ? 1.0311 1.3328 1.2834 -0.1261 -0.3150 -0.0447 1321 GLU B CB    
4515 N  N     . PRO B 105 ? 1.0658 1.2988 1.2361 -0.1413 -0.3038 -0.0725 1322 PRO B N     
4516 C  CA    . PRO B 105 ? 1.0769 1.2800 1.2209 -0.1395 -0.2868 -0.0790 1322 PRO B CA    
4517 C  C     . PRO B 105 ? 1.0812 1.2828 1.2472 -0.1335 -0.2676 -0.0743 1322 PRO B C     
4518 O  O     . PRO B 105 ? 1.1304 1.3487 1.3307 -0.1361 -0.2660 -0.0705 1322 PRO B O     
4519 C  CB    . PRO B 105 ? 1.1046 1.2922 1.2352 -0.1550 -0.2916 -0.0937 1322 PRO B CB    
4520 C  CG    . PRO B 105 ? 1.0211 1.2311 1.1691 -0.1656 -0.3131 -0.0951 1322 PRO B CG    
4521 C  CD    . PRO B 105 ? 0.9751 1.2155 1.1593 -0.1575 -0.3162 -0.0811 1322 PRO B CD    
4522 N  N     . ILE B 106 ? 1.0307 1.2124 1.1763 -0.1252 -0.2531 -0.0742 1323 ILE B N     
4523 C  CA    . ILE B 106 ? 0.9992 1.1772 1.1599 -0.1183 -0.2354 -0.0696 1323 ILE B CA    
4524 C  C     . ILE B 106 ? 1.0434 1.1952 1.1875 -0.1225 -0.2232 -0.0789 1323 ILE B C     
4525 O  O     . ILE B 106 ? 1.0814 1.2144 1.1954 -0.1249 -0.2238 -0.0866 1323 ILE B O     
4526 C  CB    . ILE B 106 ? 1.0507 1.2311 1.2077 -0.1033 -0.2285 -0.0596 1323 ILE B CB    
4527 C  CG1   . ILE B 106 ? 1.1699 1.3314 1.2907 -0.0990 -0.2271 -0.0623 1323 ILE B CG1   
4528 C  CG2   . ILE B 106 ? 1.1055 1.3114 1.2821 -0.0980 -0.2389 -0.0497 1323 ILE B CG2   
4529 C  CD1   . ILE B 106 ? 1.1608 1.3253 1.2775 -0.0854 -0.2229 -0.0522 1323 ILE B CD1   
4530 N  N     . ALA B 107 ? 0.9569 1.1072 1.1208 -0.1226 -0.2113 -0.0775 1324 ALA B N     
4531 C  CA    . ALA B 107 ? 0.9503 1.0780 1.1057 -0.1265 -0.1995 -0.0849 1324 ALA B CA    
4532 C  C     . ALA B 107 ? 1.0518 1.1685 1.1994 -0.1146 -0.1847 -0.0803 1324 ALA B C     
4533 O  O     . ALA B 107 ? 1.1111 1.2399 1.2722 -0.1055 -0.1808 -0.0709 1324 ALA B O     
4534 C  CB    . ALA B 107 ? 0.6880 0.8207 0.8709 -0.1345 -0.1960 -0.0854 1324 ALA B CB    
4535 N  N     . VAL B 108 ? 0.9232 1.0167 1.0496 -0.1149 -0.1765 -0.0873 1325 VAL B N     
4536 C  CA    . VAL B 108 ? 0.8010 0.8840 0.9238 -0.1051 -0.1624 -0.0836 1325 VAL B CA    
4537 C  C     . VAL B 108 ? 0.7948 0.8763 0.9384 -0.1061 -0.1531 -0.0816 1325 VAL B C     
4538 O  O     . VAL B 108 ? 0.8422 0.9143 0.9892 -0.1150 -0.1519 -0.0880 1325 VAL B O     
4539 C  CB    . VAL B 108 ? 0.8757 0.9361 0.9709 -0.1042 -0.1564 -0.0911 1325 VAL B CB    
4540 C  CG1   . VAL B 108 ? 0.8638 0.9180 0.9577 -0.0932 -0.1439 -0.0858 1325 VAL B CG1   
4541 C  CG2   . VAL B 108 ? 0.8773 0.9375 0.9490 -0.1053 -0.1662 -0.0939 1325 VAL B CG2   
4542 N  N     . ARG B 109 ? 0.8167 0.9061 0.9728 -0.0971 -0.1465 -0.0727 1326 ARG B N     
4543 C  CA    . ARG B 109 ? 0.8383 0.9303 1.0151 -0.0975 -0.1391 -0.0686 1326 ARG B CA    
4544 C  C     . ARG B 109 ? 0.8969 0.9678 1.0684 -0.1005 -0.1298 -0.0739 1326 ARG B C     
4545 O  O     . ARG B 109 ? 0.9049 0.9608 1.0599 -0.0958 -0.1241 -0.0768 1326 ARG B O     
4546 C  CB    . ARG B 109 ? 0.7860 0.8865 0.9708 -0.0862 -0.1331 -0.0590 1326 ARG B CB    
4547 C  CG    . ARG B 109 ? 0.7056 0.7946 0.8740 -0.0774 -0.1269 -0.0586 1326 ARG B CG    
4548 C  CD    . ARG B 109 ? 0.7304 0.8202 0.9071 -0.0691 -0.1181 -0.0517 1326 ARG B CD    
4549 N  NE    . ARG B 109 ? 0.9078 0.9893 1.0705 -0.0615 -0.1145 -0.0516 1326 ARG B NE    
4550 C  CZ    . ARG B 109 ? 0.9201 1.0088 1.0809 -0.0539 -0.1154 -0.0469 1326 ARG B CZ    
4551 N  NH1   . ARG B 109 ? 1.0211 1.1251 1.1926 -0.0517 -0.1193 -0.0415 1326 ARG B NH1   
4552 N  NH2   . ARG B 109 ? 0.7511 0.8312 0.9005 -0.0486 -0.1117 -0.0475 1326 ARG B NH2   
4553 N  N     . PRO B 110 ? 0.8463 0.9150 1.0322 -0.1082 -0.1277 -0.0751 1327 PRO B N     
4554 C  CA    . PRO B 110 ? 0.8526 0.9010 1.0364 -0.1097 -0.1175 -0.0783 1327 PRO B CA    
4555 C  C     . PRO B 110 ? 0.8748 0.9247 1.0730 -0.1036 -0.1079 -0.0692 1327 PRO B C     
4556 O  O     . PRO B 110 ? 0.8554 0.8892 1.0529 -0.1027 -0.0990 -0.0695 1327 PRO B O     
4557 C  CB    . PRO B 110 ? 0.7188 0.7624 0.9080 -0.1235 -0.1223 -0.0860 1327 PRO B CB    
4558 C  CG    . PRO B 110 ? 0.6871 0.7551 0.8943 -0.1279 -0.1322 -0.0818 1327 PRO B CG    
4559 C  CD    . PRO B 110 ? 0.7755 0.8593 0.9794 -0.1176 -0.1358 -0.0750 1327 PRO B CD    
4560 N  N     . THR B 111 ? 0.7802 0.8491 0.9910 -0.0992 -0.1097 -0.0610 1328 THR B N     
4561 C  CA    . THR B 111 ? 0.8131 0.8866 1.0362 -0.0931 -0.1016 -0.0516 1328 THR B CA    
4562 C  C     . THR B 111 ? 0.8302 0.9265 1.0651 -0.0908 -0.1069 -0.0459 1328 THR B C     
4563 O  O     . THR B 111 ? 0.7321 0.8391 0.9698 -0.0964 -0.1166 -0.0493 1328 THR B O     
4564 C  CB    . THR B 111 ? 0.7587 0.8237 0.9942 -0.1000 -0.0950 -0.0507 1328 THR B CB    
4565 O  OG1   . THR B 111 ? 0.8379 0.9097 1.0851 -0.0946 -0.0877 -0.0407 1328 THR B OG1   
4566 C  CG2   . THR B 111 ? 0.5864 0.6577 0.8339 -0.1132 -0.1019 -0.0558 1328 THR B CG2   
4567 N  N     . SER B 112 ? 0.8007 0.9044 1.0422 -0.0827 -0.1010 -0.0374 1329 SER B N     
4568 C  CA    . SER B 112 ? 0.9012 1.0243 1.1503 -0.0778 -0.1051 -0.0325 1329 SER B CA    
4569 C  C     . SER B 112 ? 0.9117 1.0492 1.1827 -0.0794 -0.1011 -0.0256 1329 SER B C     
4570 O  O     . SER B 112 ? 1.0233 1.1744 1.3005 -0.0726 -0.1006 -0.0201 1329 SER B O     
4571 C  CB    . SER B 112 ? 0.8636 0.9845 1.1001 -0.0659 -0.1022 -0.0291 1329 SER B CB    
4572 O  OG    . SER B 112 ? 0.9158 1.0263 1.1344 -0.0641 -0.1055 -0.0345 1329 SER B OG    
4573 N  N     . GLU B 113 ? 0.8625 0.9976 1.1464 -0.0884 -0.0980 -0.0260 1330 GLU B N     
4574 C  CA    . GLU B 113 ? 0.8836 1.0328 1.1897 -0.0901 -0.0926 -0.0189 1330 GLU B CA    
4575 C  C     . GLU B 113 ? 0.8912 1.0639 1.2141 -0.0922 -0.1013 -0.0180 1330 GLU B C     
4576 O  O     . GLU B 113 ? 0.8988 1.0861 1.2329 -0.0856 -0.0975 -0.0110 1330 GLU B O     
4577 C  CB    . GLU B 113 ? 0.6984 0.8388 1.0155 -0.1003 -0.0871 -0.0194 1330 GLU B CB    
4578 C  CG    . GLU B 113 ? 0.7582 0.8827 1.0679 -0.0948 -0.0743 -0.0138 1330 GLU B CG    
4579 C  CD    . GLU B 113 ? 0.8286 0.9294 1.1211 -0.0957 -0.0729 -0.0191 1330 GLU B CD    
4580 O  OE1   . GLU B 113 ? 0.7430 0.8384 1.0234 -0.0970 -0.0807 -0.0271 1330 GLU B OE1   
4581 O  OE2   . GLU B 113 ? 0.9014 0.9888 1.1925 -0.0944 -0.0634 -0.0146 1330 GLU B OE2   
4582 N  N     . THR B 114 ? 0.7584 0.9346 1.0824 -0.1009 -0.1130 -0.0249 1331 THR B N     
4583 C  CA    . THR B 114 ? 0.6683 0.8671 1.0093 -0.1042 -0.1237 -0.0244 1331 THR B CA    
4584 C  C     . THR B 114 ? 0.8843 1.0940 1.2194 -0.0927 -0.1276 -0.0205 1331 THR B C     
4585 O  O     . THR B 114 ? 1.1678 1.3982 1.5194 -0.0928 -0.1351 -0.0177 1331 THR B O     
4586 C  CB    . THR B 114 ? 0.6546 0.8501 0.9907 -0.1158 -0.1365 -0.0339 1331 THR B CB    
4587 O  OG1   . THR B 114 ? 0.7377 0.9108 1.0451 -0.1140 -0.1364 -0.0405 1331 THR B OG1   
4588 C  CG2   . THR B 114 ? 0.4845 0.6778 0.8375 -0.1292 -0.1349 -0.0367 1331 THR B CG2   
4589 N  N     . VAL B 115 ? 0.8522 1.0488 1.1656 -0.0828 -0.1230 -0.0201 1332 VAL B N     
4590 C  CA    . VAL B 115 ? 0.9072 1.1110 1.2143 -0.0719 -0.1253 -0.0165 1332 VAL B CA    
4591 C  C     . VAL B 115 ? 0.9387 1.1432 1.2485 -0.0617 -0.1134 -0.0095 1332 VAL B C     
4592 O  O     . VAL B 115 ? 1.1146 1.3335 1.4352 -0.0550 -0.1130 -0.0042 1332 VAL B O     
4593 C  CB    . VAL B 115 ? 0.9459 1.1350 1.2263 -0.0687 -0.1301 -0.0217 1332 VAL B CB    
4594 C  CG1   . VAL B 115 ? 0.8664 1.0353 1.1310 -0.0659 -0.1207 -0.0235 1332 VAL B CG1   
4595 C  CG2   . VAL B 115 ? 1.0634 1.2595 1.3387 -0.0584 -0.1326 -0.0177 1332 VAL B CG2   
4596 N  N     . MET B 116 ? 0.8360 1.0248 1.1358 -0.0601 -0.1037 -0.0092 1333 MET B N     
4597 C  CA    . MET B 116 ? 0.8398 1.0278 1.1378 -0.0503 -0.0935 -0.0032 1333 MET B CA    
4598 C  C     . MET B 116 ? 0.8386 1.0386 1.1582 -0.0516 -0.0852 0.0030  1333 MET B C     
4599 O  O     . MET B 116 ? 0.8837 1.0869 1.2040 -0.0430 -0.0771 0.0083  1333 MET B O     
4600 C  CB    . MET B 116 ? 0.8160 0.9836 1.0947 -0.0471 -0.0868 -0.0043 1333 MET B CB    
4601 C  CG    . MET B 116 ? 0.7574 0.9119 1.0170 -0.0470 -0.0929 -0.0105 1333 MET B CG    
4602 S  SD    . MET B 116 ? 0.9155 1.0487 1.1601 -0.0450 -0.0851 -0.0109 1333 MET B SD    
4603 C  CE    . MET B 116 ? 0.8724 1.0074 1.1145 -0.0346 -0.0763 -0.0037 1333 MET B CE    
4604 N  N     . TYR B 117 ? 0.7892 0.9957 1.1265 -0.0621 -0.0865 0.0025  1334 TYR B N     
4605 C  CA    . TYR B 117 ? 0.7813 0.9984 1.1392 -0.0625 -0.0762 0.0094  1334 TYR B CA    
4606 C  C     . TYR B 117 ? 0.7011 0.9421 1.0810 -0.0591 -0.0783 0.0138  1334 TYR B C     
4607 O  O     . TYR B 117 ? 0.6235 0.8714 1.0124 -0.0527 -0.0673 0.0203  1334 TYR B O     
4608 C  CB    . TYR B 117 ? 0.7116 0.9251 1.0821 -0.0750 -0.0739 0.0084  1334 TYR B CB    
4609 C  CG    . TYR B 117 ? 0.8138 1.0031 1.1642 -0.0746 -0.0667 0.0076  1334 TYR B CG    
4610 C  CD1   . TYR B 117 ? 0.9158 1.0926 1.2429 -0.0638 -0.0633 0.0084  1334 TYR B CD1   
4611 C  CD2   . TYR B 117 ? 0.7371 0.9161 1.0927 -0.0846 -0.0638 0.0061  1334 TYR B CD2   
4612 C  CE1   . TYR B 117 ? 0.8608 1.0174 1.1711 -0.0626 -0.0579 0.0083  1334 TYR B CE1   
4613 C  CE2   . TYR B 117 ? 0.7454 0.9024 1.0834 -0.0829 -0.0573 0.0063  1334 TYR B CE2   
4614 C  CZ    . TYR B 117 ? 0.8102 0.9570 1.1260 -0.0715 -0.0548 0.0077  1334 TYR B CZ    
4615 O  OH    . TYR B 117 ? 0.8411 0.9675 1.1406 -0.0689 -0.0495 0.0085  1334 TYR B OH    
4616 N  N     . PRO B 118 ? 0.6450 0.8991 1.0333 -0.0624 -0.0918 0.0107  1335 PRO B N     
4617 C  CA    . PRO B 118 ? 0.7191 0.9950 1.1260 -0.0561 -0.0942 0.0157  1335 PRO B CA    
4618 C  C     . PRO B 118 ? 0.8224 1.0935 1.2153 -0.0416 -0.0873 0.0190  1335 PRO B C     
4619 O  O     . PRO B 118 ? 0.8581 1.1419 1.2663 -0.0345 -0.0797 0.0250  1335 PRO B O     
4620 C  CB    . PRO B 118 ? 0.6930 0.9767 1.1002 -0.0607 -0.1118 0.0110  1335 PRO B CB    
4621 C  CG    . PRO B 118 ? 0.6324 0.9029 1.0298 -0.0728 -0.1172 0.0037  1335 PRO B CG    
4622 C  CD    . PRO B 118 ? 0.5974 0.8467 0.9785 -0.0717 -0.1053 0.0030  1335 PRO B CD    
4623 N  N     . ALA B 119 ? 0.7619 1.0143 1.1263 -0.0373 -0.0893 0.0148  1336 ALA B N     
4624 C  CA    . ALA B 119 ? 0.7531 0.9981 1.1026 -0.0248 -0.0827 0.0169  1336 ALA B CA    
4625 C  C     . ALA B 119 ? 0.7910 1.0309 1.1403 -0.0207 -0.0672 0.0212  1336 ALA B C     
4626 O  O     . ALA B 119 ? 0.8092 1.0523 1.1593 -0.0110 -0.0596 0.0250  1336 ALA B O     
4627 C  CB    . ALA B 119 ? 0.7599 0.9857 1.0809 -0.0228 -0.0876 0.0115  1336 ALA B CB    
4628 N  N     . TYR B 120 ? 0.7146 0.9449 1.0611 -0.0276 -0.0620 0.0209  1337 TYR B N     
4629 C  CA    . TYR B 120 ? 0.8721 1.0967 1.2161 -0.0236 -0.0472 0.0259  1337 TYR B CA    
4630 C  C     . TYR B 120 ? 0.9426 1.1865 1.3135 -0.0223 -0.0387 0.0323  1337 TYR B C     
4631 O  O     . TYR B 120 ? 0.9637 1.2064 1.3311 -0.0138 -0.0266 0.0366  1337 TYR B O     
4632 C  CB    . TYR B 120 ? 1.0056 1.2163 1.3430 -0.0313 -0.0434 0.0254  1337 TYR B CB    
4633 C  CG    . TYR B 120 ? 0.9986 1.1877 1.3077 -0.0292 -0.0464 0.0211  1337 TYR B CG    
4634 C  CD1   . TYR B 120 ? 0.9681 1.1525 1.2620 -0.0243 -0.0550 0.0163  1337 TYR B CD1   
4635 C  CD2   . TYR B 120 ? 0.9410 1.1150 1.2405 -0.0321 -0.0403 0.0224  1337 TYR B CD2   
4636 C  CE1   . TYR B 120 ? 0.9386 1.1054 1.2104 -0.0227 -0.0573 0.0127  1337 TYR B CE1   
4637 C  CE2   . TYR B 120 ? 0.8138 0.9702 1.0909 -0.0297 -0.0432 0.0192  1337 TYR B CE2   
4638 C  CZ    . TYR B 120 ? 0.8855 1.0392 1.1498 -0.0252 -0.0517 0.0142  1337 TYR B CZ    
4639 O  OH    . TYR B 120 ? 0.9353 1.0732 1.1805 -0.0230 -0.0544 0.0112  1337 TYR B OH    
4640 N  N     . ALA B 121 ? 0.9777 1.2400 1.3758 -0.0305 -0.0450 0.0329  1338 ALA B N     
4641 C  CA    . ALA B 121 ? 0.9593 1.2430 1.3877 -0.0293 -0.0375 0.0393  1338 ALA B CA    
4642 C  C     . ALA B 121 ? 0.8907 1.1840 1.3216 -0.0170 -0.0369 0.0415  1338 ALA B C     
4643 O  O     . ALA B 121 ? 0.9321 1.2331 1.3743 -0.0099 -0.0239 0.0471  1338 ALA B O     
4644 C  CB    . ALA B 121 ? 1.0745 1.3770 1.5327 -0.0414 -0.0469 0.0389  1338 ALA B CB    
4645 N  N     . LYS B 122 ? 0.8112 1.1024 1.2306 -0.0138 -0.0499 0.0373  1339 LYS B N     
4646 C  CA    . LYS B 122 ? 0.8028 1.1010 1.2241 -0.0020 -0.0499 0.0394  1339 LYS B CA    
4647 C  C     . LYS B 122 ? 0.8708 1.1516 1.2681 0.0090  -0.0376 0.0395  1339 LYS B C     
4648 O  O     . LYS B 122 ? 0.7624 1.0489 1.1663 0.0191  -0.0293 0.0431  1339 LYS B O     
4649 C  CB    . LYS B 122 ? 0.6781 0.9761 1.0910 -0.0021 -0.0667 0.0354  1339 LYS B CB    
4650 C  CG    . LYS B 122 ? 0.8346 1.1393 1.2505 0.0096  -0.0684 0.0380  1339 LYS B CG    
4651 C  CD    . LYS B 122 ? 0.9606 1.2650 1.3680 0.0081  -0.0852 0.0350  1339 LYS B CD    
4652 C  CE    . LYS B 122 ? 0.9521 1.2656 1.3698 -0.0052 -0.0978 0.0324  1339 LYS B CE    
4653 N  NZ    . LYS B 122 ? 0.9461 1.2490 1.3420 -0.0081 -0.1116 0.0272  1339 LYS B NZ    
4654 N  N     . TRP B 123 ? 0.9530 1.2120 1.3224 0.0073  -0.0364 0.0355  1340 TRP B N     
4655 C  CA    . TRP B 123 ? 0.8607 1.1021 1.2046 0.0166  -0.0276 0.0346  1340 TRP B CA    
4656 C  C     . TRP B 123 ? 0.8322 1.0697 1.1746 0.0190  -0.0110 0.0389  1340 TRP B C     
4657 O  O     . TRP B 123 ? 0.7791 1.0038 1.1013 0.0276  -0.0028 0.0384  1340 TRP B O     
4658 C  CB    . TRP B 123 ? 0.9149 1.1359 1.2303 0.0145  -0.0347 0.0287  1340 TRP B CB    
4659 C  CG    . TRP B 123 ? 0.9294 1.1494 1.2390 0.0143  -0.0484 0.0244  1340 TRP B CG    
4660 C  CD1   . TRP B 123 ? 0.9057 1.1359 1.2247 0.0195  -0.0539 0.0252  1340 TRP B CD1   
4661 C  CD2   . TRP B 123 ? 0.8022 1.0096 1.0949 0.0090  -0.0576 0.0191  1340 TRP B CD2   
4662 N  NE1   . TRP B 123 ? 0.8432 1.0671 1.1505 0.0173  -0.0659 0.0210  1340 TRP B NE1   
4663 C  CE2   . TRP B 123 ? 0.7897 1.0000 1.0812 0.0108  -0.0679 0.0170  1340 TRP B CE2   
4664 C  CE3   . TRP B 123 ? 0.7886 0.9824 1.0678 0.0033  -0.0576 0.0165  1340 TRP B CE3   
4665 C  CZ2   . TRP B 123 ? 0.8811 1.0812 1.1578 0.0067  -0.0772 0.0121  1340 TRP B CZ2   
4666 C  CZ3   . TRP B 123 ? 0.7132 0.8977 0.9796 -0.0003 -0.0669 0.0115  1340 TRP B CZ3   
4667 C  CH2   . TRP B 123 ? 0.8091 0.9966 1.0739 0.0012  -0.0761 0.0091  1340 TRP B CH2   
4668 N  N     . ILE B 124 ? 0.9297 1.1768 1.2914 0.0113  -0.0056 0.0430  1341 ILE B N     
4669 C  CA    . ILE B 124 ? 0.9971 1.2400 1.3570 0.0133  0.0115  0.0482  1341 ILE B CA    
4670 C  C     . ILE B 124 ? 0.9749 1.2397 1.3661 0.0165  0.0209  0.0541  1341 ILE B C     
4671 O  O     . ILE B 124 ? 1.0097 1.2907 1.4296 0.0083  0.0224  0.0580  1341 ILE B O     
4672 C  CB    . ILE B 124 ? 1.0812 1.3169 1.4399 0.0028  0.0129  0.0495  1341 ILE B CB    
4673 C  CG1   . ILE B 124 ? 0.9903 1.2051 1.3195 0.0013  0.0037  0.0439  1341 ILE B CG1   
4674 C  CG2   . ILE B 124 ? 1.1734 1.4037 1.5287 0.0050  0.0313  0.0561  1341 ILE B CG2   
4675 C  CD1   . ILE B 124 ? 0.9376 1.1467 1.2691 -0.0093 0.0010  0.0438  1341 ILE B CD1   
4676 N  N     . GLN B 125 ? 0.9255 1.1902 1.3117 0.0285  0.0280  0.0547  1342 GLN B N     
4677 C  CA    . GLN B 125 ? 0.8448 1.1289 1.2593 0.0343  0.0389  0.0604  1342 GLN B CA    
4678 C  C     . GLN B 125 ? 0.9049 1.1823 1.3123 0.0396  0.0604  0.0651  1342 GLN B C     
4679 O  O     . GLN B 125 ? 1.0823 1.3761 1.5152 0.0439  0.0727  0.0706  1342 GLN B O     
4680 C  CB    . GLN B 125 ? 0.7237 1.0122 1.1398 0.0450  0.0344  0.0585  1342 GLN B CB    
4681 N  N     . SER B 126 ? 0.6518 0.9059 1.0252 0.0400  0.0654  0.0633  1343 SER B N     
4682 C  CA    . SER B 126 ? 0.7205 0.9660 1.0824 0.0447  0.0856  0.0681  1343 SER B CA    
4683 C  C     . SER B 126 ? 0.8496 1.0738 1.1819 0.0395  0.0851  0.0675  1343 SER B C     
4684 O  O     . SER B 126 ? 0.8598 1.0745 1.1781 0.0346  0.0699  0.0625  1343 SER B O     
4685 C  CB    . SER B 126 ? 0.7716 1.0075 1.1143 0.0588  0.0960  0.0661  1343 SER B CB    
4686 O  OG    . SER B 126 ? 0.8114 1.0235 1.1148 0.0624  0.0886  0.0592  1343 SER B OG    
4687 N  N     . TYR B 127 ? 0.9964 1.2128 1.3189 0.0411  0.1026  0.0733  1344 TYR B N     
4688 C  CA    . TYR B 127 ? 0.9852 1.1791 1.2750 0.0388  0.1034  0.0739  1344 TYR B CA    
4689 C  C     . TYR B 127 ? 0.8980 1.0720 1.1503 0.0454  0.0938  0.0664  1344 TYR B C     
4690 O  O     . TYR B 127 ? 0.7717 0.9304 1.0020 0.0419  0.0855  0.0646  1344 TYR B O     
4691 C  CB    . TYR B 127 ? 1.0511 1.2384 1.3318 0.0421  0.1252  0.0818  1344 TYR B CB    
4692 C  CG    . TYR B 127 ? 1.1672 1.3438 1.4226 0.0553  0.1372  0.0800  1344 TYR B CG    
4693 C  CD1   . TYR B 127 ? 1.1748 1.3264 1.3854 0.0608  0.1366  0.0769  1344 TYR B CD1   
4694 C  CD2   . TYR B 127 ? 1.2680 1.4594 1.5443 0.0623  0.1486  0.0812  1344 TYR B CD2   
4695 C  CE1   . TYR B 127 ? 1.2412 1.3814 1.4266 0.0722  0.1471  0.0741  1344 TYR B CE1   
4696 C  CE2   . TYR B 127 ? 1.3422 1.5219 1.5943 0.0746  0.1604  0.0788  1344 TYR B CE2   
4697 C  CZ    . TYR B 127 ? 1.4069 1.5602 1.6124 0.0790  0.1595  0.0748  1344 TYR B CZ    
4698 O  OH    . TYR B 127 ? 1.5603 1.7005 1.7400 0.0906  0.1709  0.0713  1344 TYR B OH    
4699 N  N     . ARG B 128 ? 0.9062 1.0802 1.1523 0.0551  0.0952  0.0620  1345 ARG B N     
4700 C  CA    . ARG B 128 ? 0.8378 0.9928 1.0495 0.0615  0.0874  0.0545  1345 ARG B CA    
4701 C  C     . ARG B 128 ? 0.8670 1.0191 1.0758 0.0552  0.0668  0.0488  1345 ARG B C     
4702 O  O     . ARG B 128 ? 0.8383 0.9731 1.0179 0.0570  0.0591  0.0439  1345 ARG B O     
4703 C  CB    . ARG B 128 ? 0.7014 0.8590 0.9143 0.0718  0.0926  0.0508  1345 ARG B CB    
4704 C  CG    . ARG B 128 ? 0.7900 0.9507 1.0068 0.0793  0.1148  0.0560  1345 ARG B CG    
4705 C  CD    . ARG B 128 ? 0.8991 1.0556 1.1087 0.0913  0.1210  0.0510  1345 ARG B CD    
4706 N  NE    . ARG B 128 ? 1.0653 1.2447 1.3140 0.0936  0.1215  0.0531  1345 ARG B NE    
4707 C  CZ    . ARG B 128 ? 1.1565 1.3547 1.4363 0.0948  0.1359  0.0605  1345 ARG B CZ    
4708 N  NH1   . ARG B 128 ? 1.1682 1.3639 1.4435 0.0937  0.1526  0.0666  1345 ARG B NH1   
4709 N  NH2   . ARG B 128 ? 1.0405 1.2606 1.3568 0.0972  0.1338  0.0624  1345 ARG B NH2   
4710 N  N     . ASP B 129 ? 0.8337 1.0025 1.0722 0.0475  0.0579  0.0495  1346 ASP B N     
4711 C  CA    . ASP B 129 ? 0.7619 0.9302 1.0015 0.0413  0.0397  0.0444  1346 ASP B CA    
4712 C  C     . ASP B 129 ? 0.7810 0.9394 1.0111 0.0331  0.0347  0.0455  1346 ASP B C     
4713 O  O     . ASP B 129 ? 0.7942 0.9539 1.0295 0.0268  0.0213  0.0418  1346 ASP B O     
4714 C  CB    . ASP B 129 ? 0.7633 0.9532 1.0372 0.0365  0.0323  0.0447  1346 ASP B CB    
4715 C  CG    . ASP B 129 ? 0.8963 1.0966 1.1819 0.0450  0.0349  0.0441  1346 ASP B CG    
4716 O  OD1   . ASP B 129 ? 1.0349 1.2238 1.3007 0.0521  0.0313  0.0390  1346 ASP B OD1   
4717 O  OD2   . ASP B 129 ? 0.9460 1.1661 1.2621 0.0445  0.0402  0.0488  1346 ASP B OD2   
4718 N  N     . LEU B 130 ? 0.8806 1.0292 1.0981 0.0329  0.0456  0.0509  1347 LEU B N     
4719 C  CA    . LEU B 130 ? 0.8298 0.9686 1.0401 0.0256  0.0395  0.0519  1347 LEU B CA    
4720 C  C     . LEU B 130 ? 0.8765 0.9942 1.0509 0.0306  0.0386  0.0513  1347 LEU B C     
4721 O  O     . LEU B 130 ? 0.8821 0.9916 1.0363 0.0385  0.0473  0.0522  1347 LEU B O     
4722 C  CB    . LEU B 130 ? 0.6968 0.8410 0.9253 0.0184  0.0497  0.0598  1347 LEU B CB    
4723 C  CG    . LEU B 130 ? 0.6572 0.8230 0.9233 0.0111  0.0479  0.0602  1347 LEU B CG    
4724 C  CD1   . LEU B 130 ? 0.7381 0.9080 1.0203 0.0055  0.0617  0.0686  1347 LEU B CD1   
4725 C  CD2   . LEU B 130 ? 0.5461 0.7140 0.8207 0.0031  0.0310  0.0543  1347 LEU B CD2   
4726 N  N     . PRO B 131 ? 0.9187 1.0272 1.0847 0.0264  0.0277  0.0493  1348 PRO B N     
4727 C  CA    . PRO B 131 ? 0.8272 0.9411 1.0121 0.0171  0.0183  0.0477  1348 PRO B CA    
4728 C  C     . PRO B 131 ? 0.8976 1.0178 1.0893 0.0160  0.0043  0.0396  1348 PRO B C     
4729 O  O     . PRO B 131 ? 1.0582 1.1761 1.2377 0.0224  0.0005  0.0351  1348 PRO B O     
4730 C  CB    . PRO B 131 ? 0.7848 0.8822 0.9515 0.0159  0.0155  0.0500  1348 PRO B CB    
4731 C  CG    . PRO B 131 ? 0.7676 0.8531 0.9050 0.0247  0.0141  0.0482  1348 PRO B CG    
4732 C  CD    . PRO B 131 ? 0.8849 0.9751 1.0190 0.0311  0.0245  0.0489  1348 PRO B CD    
4733 N  N     . ILE B 132 ? 0.7311 0.8580 0.9411 0.0076  -0.0029 0.0377  1349 ILE B N     
4734 C  CA    . ILE B 132 ? 0.6716 0.8006 0.8837 0.0056  -0.0162 0.0307  1349 ILE B CA    
4735 C  C     . ILE B 132 ? 0.7867 0.9030 0.9894 0.0016  -0.0223 0.0291  1349 ILE B C     
4736 O  O     . ILE B 132 ? 0.8894 1.0041 1.1015 -0.0052 -0.0202 0.0316  1349 ILE B O     
4737 C  CB    . ILE B 132 ? 0.6791 0.8246 0.9168 -0.0007 -0.0208 0.0289  1349 ILE B CB    
4738 C  CG1   . ILE B 132 ? 0.8967 1.0568 1.1484 0.0037  -0.0141 0.0318  1349 ILE B CG1   
4739 C  CG2   . ILE B 132 ? 0.5859 0.7305 0.8201 -0.0020 -0.0341 0.0219  1349 ILE B CG2   
4740 C  CD1   . ILE B 132 ? 1.0194 1.1840 1.2686 0.0099  -0.0202 0.0276  1349 ILE B CD1   
4741 N  N     . ARG B 133 ? 0.9633 1.0704 1.1487 0.0058  -0.0296 0.0249  1350 ARG B N     
4742 C  CA    . ARG B 133 ? 0.9101 1.0055 1.0870 0.0036  -0.0351 0.0236  1350 ARG B CA    
4743 C  C     . ARG B 133 ? 0.8313 0.9278 1.0079 0.0030  -0.0458 0.0164  1350 ARG B C     
4744 O  O     . ARG B 133 ? 0.8512 0.9440 1.0152 0.0085  -0.0499 0.0135  1350 ARG B O     
4745 C  CB    . ARG B 133 ? 0.8661 0.9490 1.0216 0.0100  -0.0321 0.0272  1350 ARG B CB    
4746 C  CG    . ARG B 133 ? 0.9443 1.0281 1.0957 0.0135  -0.0203 0.0335  1350 ARG B CG    
4747 C  CD    . ARG B 133 ? 0.9889 1.0593 1.1207 0.0175  -0.0157 0.0395  1350 ARG B CD    
4748 N  NE    . ARG B 133 ? 1.0448 1.1072 1.1792 0.0132  -0.0180 0.0422  1350 ARG B NE    
4749 C  CZ    . ARG B 133 ? 1.0324 1.0837 1.1518 0.0166  -0.0240 0.0428  1350 ARG B CZ    
4750 N  NH1   . ARG B 133 ? 1.1700 1.2176 1.2709 0.0232  -0.0290 0.0404  1350 ARG B NH1   
4751 N  NH2   . ARG B 133 ? 0.9183 0.9621 1.0419 0.0135  -0.0252 0.0457  1350 ARG B NH2   
4752 N  N     . LEU B 134 ? 0.6297 0.7310 0.8199 -0.0041 -0.0503 0.0132  1351 LEU B N     
4753 C  CA    . LEU B 134 ? 0.7532 0.8561 0.9426 -0.0046 -0.0591 0.0070  1351 LEU B CA    
4754 C  C     . LEU B 134 ? 0.7411 0.8365 0.9313 -0.0100 -0.0632 0.0037  1351 LEU B C     
4755 O  O     . LEU B 134 ? 0.5528 0.6472 0.7519 -0.0163 -0.0608 0.0048  1351 LEU B O     
4756 C  CB    . LEU B 134 ? 0.7669 0.8837 0.9691 -0.0065 -0.0618 0.0053  1351 LEU B CB    
4757 C  CG    . LEU B 134 ? 0.8075 0.9324 1.0114 -0.0003 -0.0573 0.0080  1351 LEU B CG    
4758 C  CD1   . LEU B 134 ? 0.6059 0.7445 0.8237 -0.0017 -0.0617 0.0066  1351 LEU B CD1   
4759 C  CD2   . LEU B 134 ? 0.8928 1.0091 1.0788 0.0077  -0.0573 0.0068  1351 LEU B CD2   
4760 N  N     . ASN B 135 ? 0.7058 0.7959 0.8877 -0.0079 -0.0689 -0.0005 1352 ASN B N     
4761 C  CA    . ASN B 135 ? 0.6735 0.7558 0.8554 -0.0118 -0.0716 -0.0039 1352 ASN B CA    
4762 C  C     . ASN B 135 ? 0.7789 0.8642 0.9605 -0.0135 -0.0777 -0.0098 1352 ASN B C     
4763 O  O     . ASN B 135 ? 0.7752 0.8652 0.9531 -0.0096 -0.0805 -0.0107 1352 ASN B O     
4764 C  CB    . ASN B 135 ? 0.6314 0.7029 0.8040 -0.0073 -0.0712 -0.0022 1352 ASN B CB    
4765 C  CG    . ASN B 135 ? 0.7518 0.8161 0.9251 -0.0096 -0.0737 -0.0064 1352 ASN B CG    
4766 O  OD1   . ASN B 135 ? 0.7666 0.8286 0.9460 -0.0157 -0.0727 -0.0088 1352 ASN B OD1   
4767 N  ND2   . ASN B 135 ? 0.8910 0.9516 1.0585 -0.0051 -0.0767 -0.0077 1352 ASN B ND2   
4768 N  N     . GLN B 136 ? 0.7791 0.8607 0.9638 -0.0195 -0.0793 -0.0137 1353 GLN B N     
4769 C  CA    . GLN B 136 ? 0.6486 0.7301 0.8299 -0.0213 -0.0842 -0.0192 1353 GLN B CA    
4770 C  C     . GLN B 136 ? 0.7119 0.7815 0.8888 -0.0222 -0.0831 -0.0225 1353 GLN B C     
4771 O  O     . GLN B 136 ? 0.8835 0.9457 1.0635 -0.0252 -0.0798 -0.0223 1353 GLN B O     
4772 C  CB    . GLN B 136 ? 0.4189 0.5071 0.6062 -0.0282 -0.0876 -0.0220 1353 GLN B CB    
4773 C  CG    . GLN B 136 ? 0.5127 0.6142 0.7047 -0.0268 -0.0908 -0.0200 1353 GLN B CG    
4774 C  CD    . GLN B 136 ? 0.6582 0.7663 0.8550 -0.0337 -0.0965 -0.0233 1353 GLN B CD    
4775 O  OE1   . GLN B 136 ? 0.8795 0.9870 1.0688 -0.0340 -0.1015 -0.0266 1353 GLN B OE1   
4776 N  NE2   . GLN B 136 ? 0.6581 0.7723 0.8671 -0.0395 -0.0961 -0.0222 1353 GLN B NE2   
4777 N  N     . TRP B 137 ? 0.6311 0.6986 0.8019 -0.0192 -0.0852 -0.0252 1354 TRP B N     
4778 C  CA    . TRP B 137 ? 0.4761 0.5341 0.6438 -0.0202 -0.0839 -0.0292 1354 TRP B CA    
4779 C  C     . TRP B 137 ? 0.5816 0.6406 0.7450 -0.0250 -0.0866 -0.0344 1354 TRP B C     
4780 O  O     . TRP B 137 ? 0.7466 0.8097 0.9053 -0.0230 -0.0894 -0.0350 1354 TRP B O     
4781 C  CB    . TRP B 137 ? 0.5272 0.5833 0.6925 -0.0140 -0.0838 -0.0282 1354 TRP B CB    
4782 C  CG    . TRP B 137 ? 0.6185 0.6728 0.7860 -0.0094 -0.0824 -0.0233 1354 TRP B CG    
4783 C  CD1   . TRP B 137 ? 0.7260 0.7852 0.8915 -0.0051 -0.0841 -0.0194 1354 TRP B CD1   
4784 C  CD2   . TRP B 137 ? 0.4685 0.5144 0.6391 -0.0082 -0.0792 -0.0216 1354 TRP B CD2   
4785 N  NE1   . TRP B 137 ? 0.7119 0.7666 0.8774 -0.0015 -0.0828 -0.0153 1354 TRP B NE1   
4786 C  CE2   . TRP B 137 ? 0.6914 0.7384 0.8610 -0.0031 -0.0799 -0.0159 1354 TRP B CE2   
4787 C  CE3   . TRP B 137 ? 0.5202 0.5569 0.6936 -0.0106 -0.0755 -0.0242 1354 TRP B CE3   
4788 C  CZ2   . TRP B 137 ? 0.6855 0.7254 0.8571 -0.0001 -0.0779 -0.0118 1354 TRP B CZ2   
4789 C  CZ3   . TRP B 137 ? 0.5400 0.5692 0.7172 -0.0074 -0.0725 -0.0203 1354 TRP B CZ3   
4790 C  CH2   . TRP B 137 ? 0.5569 0.5883 0.7334 -0.0021 -0.0741 -0.0137 1354 TRP B CH2   
4791 N  N     . ASN B 138 ? 0.7140 0.7681 0.8775 -0.0314 -0.0861 -0.0382 1355 ASN B N     
4792 C  CA    . ASN B 138 ? 0.8071 0.8625 0.9638 -0.0360 -0.0901 -0.0431 1355 ASN B CA    
4793 C  C     . ASN B 138 ? 0.7908 0.8341 0.9428 -0.0418 -0.0878 -0.0495 1355 ASN B C     
4794 O  O     . ASN B 138 ? 0.6792 0.7131 0.8351 -0.0422 -0.0826 -0.0499 1355 ASN B O     
4795 C  CB    . ASN B 138 ? 0.8019 0.8699 0.9634 -0.0393 -0.0959 -0.0414 1355 ASN B CB    
4796 C  CG    . ASN B 138 ? 0.9840 1.0536 1.1560 -0.0446 -0.0950 -0.0404 1355 ASN B CG    
4797 O  OD1   . ASN B 138 ? 0.9891 1.0486 1.1612 -0.0496 -0.0923 -0.0441 1355 ASN B OD1   
4798 N  ND2   . ASN B 138 ? 1.1820 1.2637 1.3636 -0.0435 -0.0962 -0.0353 1355 ASN B ND2   
4799 N  N     . ASN B 139 ? 0.6277 0.6705 0.7702 -0.0462 -0.0918 -0.0545 1356 ASN B N     
4800 C  CA    . ASN B 139 ? 0.6607 0.6912 0.7947 -0.0523 -0.0903 -0.0621 1356 ASN B CA    
4801 C  C     . ASN B 139 ? 0.7369 0.7718 0.8739 -0.0610 -0.0966 -0.0648 1356 ASN B C     
4802 O  O     . ASN B 139 ? 0.8314 0.8797 0.9706 -0.0622 -0.1039 -0.0625 1356 ASN B O     
4803 C  CB    . ASN B 139 ? 0.6065 0.6318 0.7244 -0.0515 -0.0903 -0.0663 1356 ASN B CB    
4804 C  CG    . ASN B 139 ? 0.7651 0.8021 0.8775 -0.0518 -0.0984 -0.0643 1356 ASN B CG    
4805 O  OD1   . ASN B 139 ? 0.9378 0.9878 1.0601 -0.0492 -0.1023 -0.0583 1356 ASN B OD1   
4806 N  ND2   . ASN B 139 ? 0.7618 0.7933 0.8574 -0.0544 -0.1006 -0.0689 1356 ASN B ND2   
4807 N  N     . VAL B 140 ? 0.7921 0.8158 0.9304 -0.0672 -0.0937 -0.0697 1357 VAL B N     
4808 C  CA    . VAL B 140 ? 0.8134 0.8403 0.9542 -0.0771 -0.1004 -0.0739 1357 VAL B CA    
4809 C  C     . VAL B 140 ? 0.7595 0.7688 0.8860 -0.0835 -0.0990 -0.0841 1357 VAL B C     
4810 O  O     . VAL B 140 ? 0.7369 0.7309 0.8564 -0.0800 -0.0906 -0.0870 1357 VAL B O     
4811 C  CB    . VAL B 140 ? 0.8775 0.9091 1.0370 -0.0805 -0.0990 -0.0696 1357 VAL B CB    
4812 C  CG1   . VAL B 140 ? 0.8675 0.9148 1.0384 -0.0734 -0.0990 -0.0599 1357 VAL B CG1   
4813 C  CG2   . VAL B 140 ? 0.8715 0.8857 1.0334 -0.0803 -0.0894 -0.0707 1357 VAL B CG2   
4814 N  N     . VAL B 141 ? 0.7080 0.7196 0.8303 -0.0929 -0.1076 -0.0899 1358 VAL B N     
4815 C  CA    . VAL B 141 ? 0.8704 0.8642 0.9775 -0.1004 -0.1072 -0.1010 1358 VAL B CA    
4816 C  C     . VAL B 141 ? 1.0571 1.0509 1.1754 -0.1119 -0.1120 -0.1049 1358 VAL B C     
4817 O  O     . VAL B 141 ? 1.0938 1.1051 1.2230 -0.1165 -0.1217 -0.1021 1358 VAL B O     
4818 C  CB    . VAL B 141 ? 0.8735 0.8657 0.9574 -0.1016 -0.1135 -0.1065 1358 VAL B CB    
4819 C  CG1   . VAL B 141 ? 0.8655 0.8774 0.9530 -0.1041 -0.1262 -0.1029 1358 VAL B CG1   
4820 C  CG2   . VAL B 141 ? 0.9756 0.9484 1.0421 -0.1107 -0.1137 -0.1192 1358 VAL B CG2   
4821 N  N     . ARG B 142 ? 1.0367 1.0107 1.1539 -0.1162 -0.1046 -0.1110 1359 ARG B N     
4822 C  CA    . ARG B 142 ? 0.8684 0.8367 0.9934 -0.1285 -0.1080 -0.1171 1359 ARG B CA    
4823 C  C     . ARG B 142 ? 0.8554 0.8002 0.9581 -0.1337 -0.1058 -0.1301 1359 ARG B C     
4824 O  O     . ARG B 142 ? 1.0096 0.9355 1.1059 -0.1286 -0.0940 -0.1324 1359 ARG B O     
4825 C  CB    . ARG B 142 ? 0.8260 0.7899 0.9714 -0.1281 -0.0992 -0.1113 1359 ARG B CB    
4826 C  CG    . ARG B 142 ? 0.8592 0.8423 1.0222 -0.1201 -0.0977 -0.0980 1359 ARG B CG    
4827 C  CD    . ARG B 142 ? 0.9661 0.9391 1.1409 -0.1159 -0.0863 -0.0918 1359 ARG B CD    
4828 N  NE    . ARG B 142 ? 1.0032 0.9937 1.1943 -0.1109 -0.0856 -0.0801 1359 ARG B NE    
4829 C  CZ    . ARG B 142 ? 1.0973 1.0831 1.2989 -0.1067 -0.0770 -0.0723 1359 ARG B CZ    
4830 N  NH1   . ARG B 142 ? 1.1805 1.1451 1.3799 -0.1065 -0.0686 -0.0744 1359 ARG B NH1   
4831 N  NH2   . ARG B 142 ? 1.1351 1.1367 1.3485 -0.1022 -0.0764 -0.0623 1359 ARG B NH2   
4832 N  N     . TRP B 143 ? 0.8774 0.8232 0.9681 -0.1435 -0.1170 -0.1386 1360 TRP B N     
4833 C  CA    . TRP B 143 ? 1.1287 1.0521 1.1928 -0.1484 -0.1160 -0.1519 1360 TRP B CA    
4834 C  C     . TRP B 143 ? 1.2904 1.1912 1.3582 -0.1569 -0.1095 -0.1605 1360 TRP B C     
4835 O  O     . TRP B 143 ? 1.1778 1.0687 1.2365 -0.1693 -0.1164 -0.1718 1360 TRP B O     
4836 C  CB    . TRP B 143 ? 1.1475 1.0806 1.1968 -0.1562 -0.1320 -0.1575 1360 TRP B CB    
4837 C  CG    . TRP B 143 ? 1.1044 1.0193 1.1203 -0.1569 -0.1314 -0.1681 1360 TRP B CG    
4838 C  CD1   . TRP B 143 ? 1.0872 0.9833 1.0838 -0.1680 -0.1352 -0.1823 1360 TRP B CD1   
4839 C  CD2   . TRP B 143 ? 1.1290 1.0415 1.1249 -0.1464 -0.1261 -0.1656 1360 TRP B CD2   
4840 N  NE1   . TRP B 143 ? 1.1656 1.0470 1.1293 -0.1645 -0.1320 -0.1890 1360 TRP B NE1   
4841 C  CE2   . TRP B 143 ? 1.2094 1.1009 1.1729 -0.1512 -0.1260 -0.1785 1360 TRP B CE2   
4842 C  CE3   . TRP B 143 ? 1.1323 1.0573 1.1342 -0.1336 -0.1208 -0.1540 1360 TRP B CE3   
4843 C  CZ2   . TRP B 143 ? 1.2994 1.1827 1.2370 -0.1435 -0.1199 -0.1793 1360 TRP B CZ2   
4844 C  CZ3   . TRP B 143 ? 1.1894 1.1067 1.1675 -0.1266 -0.1154 -0.1550 1360 TRP B CZ3   
4845 C  CH2   . TRP B 143 ? 1.2754 1.1723 1.2219 -0.1313 -0.1145 -0.1672 1360 TRP B CH2   
4846 N  N     . GLU B 144 ? 1.3884 1.2806 1.4698 -0.1499 -0.0963 -0.1546 1361 GLU B N     
4847 C  CA    . GLU B 144 ? 1.3533 1.2243 1.4426 -0.1557 -0.0880 -0.1595 1361 GLU B CA    
4848 C  C     . GLU B 144 ? 1.3073 1.1500 1.3751 -0.1520 -0.0767 -0.1691 1361 GLU B C     
4849 O  O     . GLU B 144 ? 1.4109 1.2311 1.4704 -0.1607 -0.0742 -0.1806 1361 GLU B O     
4850 C  CB    . GLU B 144 ? 1.3686 1.2462 1.4841 -0.1493 -0.0802 -0.1464 1361 GLU B CB    
4851 C  CG    . GLU B 144 ? 1.4382 1.3389 1.5768 -0.1558 -0.0890 -0.1388 1361 GLU B CG    
4852 C  CD    . GLU B 144 ? 1.5216 1.4273 1.6821 -0.1489 -0.0803 -0.1256 1361 GLU B CD    
4853 O  OE1   . GLU B 144 ? 1.5412 1.4295 1.7004 -0.1415 -0.0684 -0.1236 1361 GLU B OE1   
4854 O  OE2   . GLU B 144 ? 1.5108 1.4378 1.6894 -0.1505 -0.0852 -0.1171 1361 GLU B OE2   
4855 N  N     . LYS B 146 ? 1.4216 1.1928 1.4553 -0.1587 -0.0549 -0.1972 1363 LYS B N     
4856 C  CA    . LYS B 146 ? 1.3574 1.0954 1.3856 -0.1605 -0.0421 -0.2068 1363 LYS B CA    
4857 C  C     . LYS B 146 ? 1.4660 1.1891 1.4716 -0.1502 -0.0308 -0.2120 1363 LYS B C     
4858 O  O     . LYS B 146 ? 1.5662 1.2954 1.5495 -0.1502 -0.0364 -0.2166 1363 LYS B O     
4859 C  CB    . LYS B 146 ? 1.2270 0.9605 1.2828 -0.1555 -0.0321 -0.1964 1363 LYS B CB    
4860 N  N     . HIS B 147 ? 1.4171 1.1192 1.4279 -0.1418 -0.0144 -0.2117 1364 HIS B N     
4861 C  CA    . HIS B 147 ? 1.3605 1.0525 1.3575 -0.1294 -0.0013 -0.2133 1364 HIS B CA    
4862 C  C     . HIS B 147 ? 1.2996 1.0165 1.3172 -0.1157 0.0004  -0.1960 1364 HIS B C     
4863 O  O     . HIS B 147 ? 1.3577 1.0753 1.3989 -0.1093 0.0064  -0.1861 1364 HIS B O     
4864 C  CB    . HIS B 147 ? 1.3306 0.9894 1.3261 -0.1260 0.0156  -0.2207 1364 HIS B CB    
4865 N  N     . PRO B 148 ? 1.1882 0.9249 1.1973 -0.1110 -0.0049 -0.1918 1365 PRO B N     
4866 C  CA    . PRO B 148 ? 1.0948 0.8572 1.1244 -0.1005 -0.0064 -0.1758 1365 PRO B CA    
4867 C  C     . PRO B 148 ? 1.0906 0.8468 1.1286 -0.0861 0.0087  -0.1705 1365 PRO B C     
4868 O  O     . PRO B 148 ? 1.1668 0.9029 1.1911 -0.0827 0.0205  -0.1789 1365 PRO B O     
4869 C  CB    . PRO B 148 ? 1.1007 0.8832 1.1161 -0.1020 -0.0174 -0.1749 1365 PRO B CB    
4870 C  CG    . PRO B 148 ? 1.1618 0.9247 1.1458 -0.1070 -0.0146 -0.1895 1365 PRO B CG    
4871 C  CD    . PRO B 148 ? 1.1739 0.9100 1.1533 -0.1158 -0.0105 -0.2013 1365 PRO B CD    
4872 N  N     . GLN B 149 ? 1.0707 0.8455 1.1316 -0.0775 0.0079  -0.1562 1366 GLN B N     
4873 C  CA    . GLN B 149 ? 1.0028 0.7765 1.0765 -0.0636 0.0197  -0.1492 1366 GLN B CA    
4874 C  C     . GLN B 149 ? 1.1412 0.9432 1.2289 -0.0565 0.0130  -0.1359 1366 GLN B C     
4875 O  O     . GLN B 149 ? 1.3021 1.1202 1.3992 -0.0603 0.0023  -0.1289 1366 GLN B O     
4876 C  CB    . GLN B 149 ? 1.0459 0.8046 1.1371 -0.0600 0.0278  -0.1457 1366 GLN B CB    
4877 C  CG    . GLN B 149 ? 1.1697 0.9115 1.2644 -0.0492 0.0437  -0.1472 1366 GLN B CG    
4878 C  CD    . GLN B 149 ? 1.2890 1.0174 1.4029 -0.0444 0.0507  -0.1414 1366 GLN B CD    
4879 O  OE1   . GLN B 149 ? 1.3130 1.0439 1.4362 -0.0498 0.0439  -0.1362 1366 GLN B OE1   
4880 N  NE2   . GLN B 149 ? 1.3977 1.1115 1.5181 -0.0339 0.0647  -0.1416 1366 GLN B NE2   
4881 N  N     . PRO B 150 ? 1.0629 0.8708 1.1526 -0.0466 0.0197  -0.1325 1367 PRO B N     
4882 C  CA    . PRO B 150 ? 1.1630 0.9966 1.2599 -0.0418 0.0125  -0.1228 1367 PRO B CA    
4883 C  C     . PRO B 150 ? 1.3286 1.1808 1.4448 -0.0399 0.0035  -0.1106 1367 PRO B C     
4884 O  O     . PRO B 150 ? 1.5527 1.4238 1.6676 -0.0416 -0.0063 -0.1064 1367 PRO B O     
4885 C  CB    . PRO B 150 ? 1.1087 0.9406 1.2113 -0.0309 0.0245  -0.1210 1367 PRO B CB    
4886 C  CG    . PRO B 150 ? 1.0691 0.8770 1.1532 -0.0334 0.0354  -0.1336 1367 PRO B CG    
4887 C  CD    . PRO B 150 ? 1.1096 0.9011 1.1836 -0.0440 0.0316  -0.1418 1367 PRO B CD    
4888 N  N     . PHE B 151 ? 1.1538 1.0016 1.2871 -0.0355 0.0066  -0.1042 1368 PHE B N     
4889 C  CA    . PHE B 151 ? 0.9279 0.7936 1.0748 -0.0340 -0.0022 -0.0930 1368 PHE B CA    
4890 C  C     . PHE B 151 ? 1.0370 0.8960 1.1875 -0.0413 -0.0054 -0.0924 1368 PHE B C     
4891 O  O     . PHE B 151 ? 1.0976 0.9706 1.2561 -0.0421 -0.0126 -0.0843 1368 PHE B O     
4892 C  CB    . PHE B 151 ? 0.9699 0.8421 1.1346 -0.0219 0.0014  -0.0827 1368 PHE B CB    
4893 C  CG    . PHE B 151 ? 1.0287 0.9106 1.1940 -0.0152 0.0039  -0.0822 1368 PHE B CG    
4894 C  CD1   . PHE B 151 ? 1.0421 0.9444 1.2069 -0.0150 -0.0046 -0.0778 1368 PHE B CD1   
4895 C  CD2   . PHE B 151 ? 0.9025 0.7727 1.0695 -0.0094 0.0156  -0.0862 1368 PHE B CD2   
4896 C  CE1   . PHE B 151 ? 1.0750 0.9858 1.2416 -0.0097 -0.0018 -0.0771 1368 PHE B CE1   
4897 C  CE2   . PHE B 151 ? 1.0142 0.8941 1.1838 -0.0038 0.0189  -0.0853 1368 PHE B CE2   
4898 C  CZ    . PHE B 151 ? 1.0325 0.9326 1.2019 -0.0044 0.0099  -0.0807 1368 PHE B CZ    
4899 N  N     . LEU B 152 ? 1.0489 0.8859 1.1930 -0.0470 0.0006  -0.1012 1369 LEU B N     
4900 C  CA    . LEU B 152 ? 0.9920 0.8190 1.1416 -0.0542 -0.0002 -0.1009 1369 LEU B CA    
4901 C  C     . LEU B 152 ? 1.0037 0.8309 1.1416 -0.0682 -0.0081 -0.1100 1369 LEU B C     
4902 O  O     . LEU B 152 ? 1.1402 0.9762 1.2857 -0.0746 -0.0148 -0.1057 1369 LEU B O     
4903 C  CB    . LEU B 152 ? 1.0325 0.8332 1.1854 -0.0511 0.0121  -0.1043 1369 LEU B CB    
4904 C  CG    . LEU B 152 ? 0.9384 0.7415 1.1023 -0.0363 0.0193  -0.0964 1369 LEU B CG    
4905 C  CD1   . LEU B 152 ? 0.8617 0.6392 1.0310 -0.0311 0.0323  -0.0987 1369 LEU B CD1   
4906 C  CD2   . LEU B 152 ? 0.8933 0.7160 1.0721 -0.0298 0.0129  -0.0815 1369 LEU B CD2   
4907 N  N     . ARG B 153 ? 0.8651 0.6847 0.9845 -0.0728 -0.0079 -0.1218 1370 ARG B N     
4908 C  CA    . ARG B 153 ? 0.9701 0.7914 1.0768 -0.0860 -0.0174 -0.1306 1370 ARG B CA    
4909 C  C     . ARG B 153 ? 1.0396 0.8740 1.1306 -0.0848 -0.0230 -0.1335 1370 ARG B C     
4910 O  O     . ARG B 153 ? 0.9936 0.8146 1.0654 -0.0860 -0.0189 -0.1435 1370 ARG B O     
4911 C  CB    . ARG B 153 ? 1.0815 0.8758 1.1772 -0.0949 -0.0125 -0.1439 1370 ARG B CB    
4912 C  CG    . ARG B 153 ? 1.2235 0.9985 1.3333 -0.0929 -0.0025 -0.1413 1370 ARG B CG    
4913 C  CD    . ARG B 153 ? 1.3347 1.0822 1.4338 -0.1039 0.0011  -0.1554 1370 ARG B CD    
4914 N  NE    . ARG B 153 ? 1.4401 1.1648 1.5237 -0.0990 0.0128  -0.1653 1370 ARG B NE    
4915 C  CZ    . ARG B 153 ? 1.4837 1.1911 1.5754 -0.0890 0.0266  -0.1627 1370 ARG B CZ    
4916 N  NH1   . ARG B 153 ? 1.5366 1.2468 1.6506 -0.0829 0.0296  -0.1501 1370 ARG B NH1   
4917 N  NH2   . ARG B 153 ? 1.4625 1.1498 1.5399 -0.0846 0.0379  -0.1724 1370 ARG B NH2   
4918 N  N     . THR B 154 ? 1.0975 0.9565 1.1952 -0.0830 -0.0321 -0.1247 1371 THR B N     
4919 C  CA    . THR B 154 ? 1.0108 0.8828 1.0946 -0.0824 -0.0385 -0.1260 1371 THR B CA    
4920 C  C     . THR B 154 ? 0.9422 0.8292 1.0245 -0.0918 -0.0523 -0.1265 1371 THR B C     
4921 O  O     . THR B 154 ? 0.9718 0.8695 1.0708 -0.0946 -0.0570 -0.1202 1371 THR B O     
4922 C  CB    . THR B 154 ? 0.9073 0.7961 0.9999 -0.0712 -0.0374 -0.1154 1371 THR B CB    
4923 O  OG1   . THR B 154 ? 1.0939 0.9922 1.2071 -0.0673 -0.0382 -0.1049 1371 THR B OG1   
4924 C  CG2   . THR B 154 ? 0.8160 0.6935 0.9043 -0.0628 -0.0258 -0.1172 1371 THR B CG2   
4925 N  N     . ARG B 155 ? 0.9361 0.8246 0.9986 -0.0959 -0.0584 -0.1331 1372 ARG B N     
4926 C  CA    . ARG B 155 ? 0.9763 0.8809 1.0378 -0.1041 -0.0727 -0.1330 1372 ARG B CA    
4927 C  C     . ARG B 155 ? 1.0092 0.9383 1.0812 -0.0972 -0.0782 -0.1214 1372 ARG B C     
4928 O  O     . ARG B 155 ? 1.0367 0.9817 1.1239 -0.1001 -0.0857 -0.1157 1372 ARG B O     
4929 C  CB    . ARG B 155 ? 1.0416 0.9379 1.0765 -0.1110 -0.0783 -0.1441 1372 ARG B CB    
4930 C  CG    . ARG B 155 ? 1.1920 1.0640 1.2163 -0.1201 -0.0749 -0.1570 1372 ARG B CG    
4931 C  CD    . ARG B 155 ? 1.2631 1.1328 1.2664 -0.1313 -0.0870 -0.1673 1372 ARG B CD    
4932 N  NE    . ARG B 155 ? 1.2317 1.0746 1.2080 -0.1349 -0.0807 -0.1811 1372 ARG B NE    
4933 C  CZ    . ARG B 155 ? 1.4070 1.2321 1.3765 -0.1462 -0.0824 -0.1930 1372 ARG B CZ    
4934 N  NH1   . ARG B 155 ? 1.4899 1.3223 1.4798 -0.1553 -0.0904 -0.1921 1372 ARG B NH1   
4935 N  NH2   . ARG B 155 ? 1.4580 1.2573 1.4002 -0.1485 -0.0757 -0.2060 1372 ARG B NH2   
4936 N  N     . GLU B 156 ? 0.9406 0.8722 1.0065 -0.0878 -0.0734 -0.1176 1373 GLU B N     
4937 C  CA    . GLU B 156 ? 0.8683 0.8196 0.9459 -0.0803 -0.0763 -0.1066 1373 GLU B CA    
4938 C  C     . GLU B 156 ? 0.8938 0.8431 0.9862 -0.0714 -0.0668 -0.1000 1373 GLU B C     
4939 O  O     . GLU B 156 ? 1.0461 0.9815 1.1345 -0.0671 -0.0570 -0.1030 1373 GLU B O     
4940 C  CB    . GLU B 156 ? 0.7081 0.6652 0.7704 -0.0764 -0.0786 -0.1058 1373 GLU B CB    
4941 C  CG    . GLU B 156 ? 0.7772 0.7540 0.8523 -0.0698 -0.0826 -0.0951 1373 GLU B CG    
4942 C  CD    . GLU B 156 ? 0.9259 0.9050 0.9923 -0.0626 -0.0794 -0.0920 1373 GLU B CD    
4943 O  OE1   . GLU B 156 ? 1.0552 1.0211 1.1061 -0.0619 -0.0727 -0.0975 1373 GLU B OE1   
4944 O  OE2   . GLU B 156 ? 0.9714 0.9646 1.0465 -0.0577 -0.0827 -0.0842 1373 GLU B OE2   
4945 N  N     . PHE B 157 ? 0.8166 0.7799 0.9260 -0.0682 -0.0696 -0.0909 1374 PHE B N     
4946 C  CA    . PHE B 157 ? 0.7482 0.7107 0.8697 -0.0594 -0.0623 -0.0842 1374 PHE B CA    
4947 C  C     . PHE B 157 ? 0.7597 0.7405 0.8917 -0.0544 -0.0671 -0.0746 1374 PHE B C     
4948 O  O     . PHE B 157 ? 0.8631 0.8567 0.9970 -0.0579 -0.0748 -0.0725 1374 PHE B O     
4949 C  CB    . PHE B 157 ? 0.7690 0.7184 0.9000 -0.0608 -0.0562 -0.0844 1374 PHE B CB    
4950 C  CG    . PHE B 157 ? 0.8990 0.8539 1.0402 -0.0674 -0.0609 -0.0817 1374 PHE B CG    
4951 C  CD1   . PHE B 157 ? 0.8159 0.7815 0.9708 -0.0630 -0.0615 -0.0718 1374 PHE B CD1   
4952 C  CD2   . PHE B 157 ? 1.0584 1.0069 1.1953 -0.0783 -0.0645 -0.0894 1374 PHE B CD2   
4953 C  CE1   . PHE B 157 ? 1.0123 0.9826 1.1772 -0.0692 -0.0641 -0.0689 1374 PHE B CE1   
4954 C  CE2   . PHE B 157 ? 1.0205 0.9749 1.1696 -0.0851 -0.0682 -0.0867 1374 PHE B CE2   
4955 C  CZ    . PHE B 157 ? 0.9922 0.9576 1.1559 -0.0804 -0.0673 -0.0762 1374 PHE B CZ    
4956 N  N     . LEU B 158 ? 0.6128 0.5945 0.7521 -0.0459 -0.0624 -0.0690 1375 LEU B N     
4957 C  CA    . LEU B 158 ? 0.6385 0.6344 0.7865 -0.0404 -0.0658 -0.0605 1375 LEU B CA    
4958 C  C     . LEU B 158 ? 0.8002 0.7961 0.9597 -0.0397 -0.0646 -0.0547 1375 LEU B C     
4959 O  O     . LEU B 158 ? 1.0793 1.0626 1.2425 -0.0396 -0.0589 -0.0553 1375 LEU B O     
4960 C  CB    . LEU B 158 ? 0.5624 0.5597 0.7121 -0.0321 -0.0625 -0.0577 1375 LEU B CB    
4961 C  CG    . LEU B 158 ? 0.5894 0.5826 0.7287 -0.0317 -0.0597 -0.0629 1375 LEU B CG    
4962 C  CD1   . LEU B 158 ? 0.7664 0.7621 0.9120 -0.0241 -0.0559 -0.0594 1375 LEU B CD1   
4963 C  CD2   . LEU B 158 ? 0.7049 0.7064 0.8337 -0.0354 -0.0664 -0.0644 1375 LEU B CD2   
4964 N  N     . TRP B 159 ? 0.6910 0.6998 0.8554 -0.0386 -0.0691 -0.0488 1376 TRP B N     
4965 C  CA    . TRP B 159 ? 0.7500 0.7589 0.9233 -0.0363 -0.0669 -0.0419 1376 TRP B CA    
4966 C  C     . TRP B 159 ? 0.7043 0.7272 0.8794 -0.0319 -0.0708 -0.0357 1376 TRP B C     
4967 O  O     . TRP B 159 ? 0.7445 0.7764 0.9155 -0.0309 -0.0751 -0.0368 1376 TRP B O     
4968 C  CB    . TRP B 159 ? 0.6932 0.6974 0.8713 -0.0444 -0.0658 -0.0431 1376 TRP B CB    
4969 C  CG    . TRP B 159 ? 0.7841 0.8005 0.9640 -0.0510 -0.0717 -0.0443 1376 TRP B CG    
4970 C  CD1   . TRP B 159 ? 0.8724 0.9010 1.0481 -0.0506 -0.0778 -0.0455 1376 TRP B CD1   
4971 C  CD2   . TRP B 159 ? 0.9283 0.9461 1.1168 -0.0590 -0.0720 -0.0440 1376 TRP B CD2   
4972 N  NE1   . TRP B 159 ? 0.9123 0.9509 1.0939 -0.0571 -0.0824 -0.0457 1376 TRP B NE1   
4973 C  CE2   . TRP B 159 ? 0.9407 0.9737 1.1311 -0.0627 -0.0790 -0.0450 1376 TRP B CE2   
4974 C  CE3   . TRP B 159 ? 0.8403 0.8480 1.0364 -0.0633 -0.0667 -0.0425 1376 TRP B CE3   
4975 C  CZ2   . TRP B 159 ? 0.8538 0.8941 1.0552 -0.0708 -0.0813 -0.0447 1376 TRP B CZ2   
4976 C  CZ3   . TRP B 159 ? 0.8394 0.8531 1.0455 -0.0720 -0.0684 -0.0424 1376 TRP B CZ3   
4977 C  CH2   . TRP B 159 ? 0.8588 0.8895 1.0683 -0.0758 -0.0758 -0.0436 1376 TRP B CH2   
4978 N  N     . GLN B 160 ? 0.7583 0.7818 0.9386 -0.0293 -0.0688 -0.0289 1377 GLN B N     
4979 C  CA    . GLN B 160 ? 0.6176 0.6531 0.7995 -0.0277 -0.0712 -0.0239 1377 GLN B CA    
4980 C  C     . GLN B 160 ? 0.6993 0.7354 0.8884 -0.0340 -0.0689 -0.0218 1377 GLN B C     
4981 O  O     . GLN B 160 ? 0.8222 0.8473 1.0147 -0.0371 -0.0645 -0.0216 1377 GLN B O     
4982 C  CB    . GLN B 160 ? 0.6770 0.7137 0.8568 -0.0194 -0.0707 -0.0175 1377 GLN B CB    
4983 C  CG    . GLN B 160 ? 0.9113 0.9384 1.0930 -0.0167 -0.0664 -0.0120 1377 GLN B CG    
4984 C  CD    . GLN B 160 ? 1.0583 1.0870 1.2428 -0.0189 -0.0631 -0.0064 1377 GLN B CD    
4985 O  OE1   . GLN B 160 ? 1.1743 1.2109 1.3559 -0.0158 -0.0638 -0.0024 1377 GLN B OE1   
4986 N  NE2   . GLN B 160 ? 1.0459 1.0660 1.2359 -0.0242 -0.0585 -0.0061 1377 GLN B NE2   
4987 N  N     . GLU B 161 ? 0.7515 0.8003 0.9441 -0.0363 -0.0717 -0.0209 1378 GLU B N     
4988 C  CA    . GLU B 161 ? 0.6908 0.7445 0.8930 -0.0413 -0.0692 -0.0174 1378 GLU B CA    
4989 C  C     . GLU B 161 ? 0.7391 0.8036 0.9419 -0.0355 -0.0681 -0.0110 1378 GLU B C     
4990 O  O     . GLU B 161 ? 0.7912 0.8655 0.9917 -0.0324 -0.0723 -0.0120 1378 GLU B O     
4991 C  CB    . GLU B 161 ? 0.7068 0.7672 0.9155 -0.0504 -0.0738 -0.0230 1378 GLU B CB    
4992 C  CG    . GLU B 161 ? 0.8070 0.8763 1.0105 -0.0496 -0.0810 -0.0273 1378 GLU B CG    
4993 C  CD    . GLU B 161 ? 0.8602 0.9398 1.0717 -0.0579 -0.0869 -0.0306 1378 GLU B CD    
4994 O  OE1   . GLU B 161 ? 0.8410 0.9269 1.0658 -0.0629 -0.0852 -0.0278 1378 GLU B OE1   
4995 O  OE2   . GLU B 161 ? 0.8229 0.9049 1.0275 -0.0594 -0.0933 -0.0357 1378 GLU B OE2   
4996 N  N     . GLY B 162 ? 0.7284 0.7893 0.9328 -0.0334 -0.0619 -0.0042 1379 GLY B N     
4997 C  CA    . GLY B 162 ? 0.7450 0.8136 0.9479 -0.0279 -0.0590 0.0019  1379 GLY B CA    
4998 C  C     . GLY B 162 ? 0.7664 0.8417 0.9820 -0.0333 -0.0536 0.0059  1379 GLY B C     
4999 O  O     . GLY B 162 ? 0.8653 0.9333 1.0875 -0.0391 -0.0494 0.0074  1379 GLY B O     
5000 N  N     . HIS B 163 ? 0.6874 0.7762 0.9075 -0.0313 -0.0531 0.0079  1380 HIS B N     
5001 C  CA    . HIS B 163 ? 0.6620 0.7614 0.8981 -0.0362 -0.0482 0.0116  1380 HIS B CA    
5002 C  C     . HIS B 163 ? 0.7350 0.8399 0.9676 -0.0287 -0.0414 0.0179  1380 HIS B C     
5003 O  O     . HIS B 163 ? 0.9942 1.1030 1.2181 -0.0216 -0.0442 0.0166  1380 HIS B O     
5004 C  CB    . HIS B 163 ? 0.6589 0.7725 0.9084 -0.0420 -0.0552 0.0066  1380 HIS B CB    
5005 C  CG    . HIS B 163 ? 0.8290 0.9368 1.0786 -0.0495 -0.0624 -0.0008 1380 HIS B CG    
5006 N  ND1   . HIS B 163 ? 0.8743 0.9832 1.1376 -0.0601 -0.0632 -0.0031 1380 HIS B ND1   
5007 C  CD2   . HIS B 163 ? 0.7961 0.8968 1.0336 -0.0480 -0.0687 -0.0068 1380 HIS B CD2   
5008 C  CE1   . HIS B 163 ? 0.8810 0.9825 1.1382 -0.0646 -0.0698 -0.0107 1380 HIS B CE1   
5009 N  NE2   . HIS B 163 ? 0.8106 0.9073 1.0522 -0.0571 -0.0726 -0.0127 1380 HIS B NE2   
5010 N  N     . THR B 164 ? 0.6642 0.7676 0.9022 -0.0301 -0.0318 0.0247  1381 THR B N     
5011 C  CA    . THR B 164 ? 0.7323 0.8361 0.9619 -0.0225 -0.0233 0.0312  1381 THR B CA    
5012 C  C     . THR B 164 ? 0.9089 1.0219 1.1562 -0.0268 -0.0132 0.0372  1381 THR B C     
5013 O  O     . THR B 164 ? 0.9243 1.0364 1.1860 -0.0357 -0.0109 0.0384  1381 THR B O     
5014 C  CB    . THR B 164 ? 0.7474 0.8341 0.9569 -0.0172 -0.0202 0.0352  1381 THR B CB    
5015 O  OG1   . THR B 164 ? 0.7639 0.8421 0.9795 -0.0227 -0.0135 0.0405  1381 THR B OG1   
5016 C  CG2   . THR B 164 ? 0.6531 0.7315 0.8508 -0.0147 -0.0302 0.0295  1381 THR B CG2   
5017 N  N     . ALA B 165 ? 0.8803 1.0013 1.1267 -0.0205 -0.0064 0.0408  1382 ALA B N     
5018 C  CA    . ALA B 165 ? 0.7827 0.9149 1.0471 -0.0230 0.0049  0.0470  1382 ALA B CA    
5019 C  C     . ALA B 165 ? 0.7987 0.9252 1.0463 -0.0137 0.0165  0.0533  1382 ALA B C     
5020 O  O     . ALA B 165 ? 0.8448 0.9699 1.0764 -0.0050 0.0143  0.0507  1382 ALA B O     
5021 C  CB    . ALA B 165 ? 0.5824 0.7357 0.8697 -0.0252 0.0009  0.0441  1382 ALA B CB    
5022 N  N     . PHE B 166 ? 0.8448 0.9670 1.0951 -0.0157 0.0292  0.0613  1383 PHE B N     
5023 C  CA    . PHE B 166 ? 0.9404 1.0546 1.1718 -0.0076 0.0418  0.0682  1383 PHE B CA    
5024 C  C     . PHE B 166 ? 1.0010 1.1269 1.2531 -0.0102 0.0569  0.0752  1383 PHE B C     
5025 O  O     . PHE B 166 ? 0.9752 1.1139 1.2569 -0.0195 0.0570  0.0755  1383 PHE B O     
5026 C  CB    . PHE B 166 ? 0.9621 1.0556 1.1713 -0.0063 0.0445  0.0735  1383 PHE B CB    
5027 C  CG    . PHE B 166 ? 0.9284 1.0108 1.1222 -0.0049 0.0307  0.0679  1383 PHE B CG    
5028 C  CD1   . PHE B 166 ? 0.9386 1.0204 1.1459 -0.0128 0.0220  0.0636  1383 PHE B CD1   
5029 C  CD2   . PHE B 166 ? 0.9011 0.9731 1.0665 0.0044  0.0269  0.0670  1383 PHE B CD2   
5030 C  CE1   . PHE B 166 ? 0.8986 0.9702 1.0925 -0.0108 0.0106  0.0587  1383 PHE B CE1   
5031 C  CE2   . PHE B 166 ? 0.6872 0.7503 0.8409 0.0058  0.0145  0.0624  1383 PHE B CE2   
5032 C  CZ    . PHE B 166 ? 0.6815 0.7448 0.8502 -0.0015 0.0070  0.0585  1383 PHE B CZ    
5033 N  N     . ALA B 167 ? 1.0150 1.1359 1.2509 -0.0022 0.0699  0.0809  1384 ALA B N     
5034 C  CA    . ALA B 167 ? 0.9181 1.0487 1.1722 -0.0038 0.0870  0.0887  1384 ALA B CA    
5035 C  C     . ALA B 167 ? 1.0968 1.2168 1.3529 -0.0105 0.0967  0.0975  1384 ALA B C     
5036 O  O     . ALA B 167 ? 1.2725 1.4036 1.5585 -0.0193 0.1039  0.1016  1384 ALA B O     
5037 C  CB    . ALA B 167 ? 0.7400 0.8685 0.9750 0.0077  0.0989  0.0910  1384 ALA B CB    
5038 N  N     . THR B 168 ? 1.0907 1.1893 1.3166 -0.0066 0.0968  0.1009  1385 THR B N     
5039 C  CA    . THR B 168 ? 1.0897 1.1760 1.3162 -0.0122 0.1062  0.1102  1385 THR B CA    
5040 C  C     . THR B 168 ? 1.0705 1.1476 1.3006 -0.0194 0.0934  0.1068  1385 THR B C     
5041 O  O     . THR B 168 ? 1.0546 1.1284 1.2741 -0.0170 0.0782  0.0988  1385 THR B O     
5042 C  CB    . THR B 168 ? 1.1543 1.2216 1.3457 -0.0033 0.1174  0.1190  1385 THR B CB    
5043 O  OG1   . THR B 168 ? 1.4621 1.5156 1.6540 -0.0090 0.1243  0.1282  1385 THR B OG1   
5044 C  CG2   . THR B 168 ? 1.0343 1.0887 1.1914 0.0057  0.1049  0.1141  1385 THR B CG2   
5045 N  N     . GLN B 169 ? 1.0935 1.1651 1.3386 -0.0282 0.1012  0.1134  1386 GLN B N     
5046 C  CA    . GLN B 169 ? 1.1134 1.1721 1.3602 -0.0346 0.0924  0.1115  1386 GLN B CA    
5047 C  C     . GLN B 169 ? 1.1078 1.1444 1.3203 -0.0260 0.0891  0.1152  1386 GLN B C     
5048 O  O     . GLN B 169 ? 1.0693 1.0960 1.2794 -0.0280 0.0784  0.1112  1386 GLN B O     
5049 C  CB    . GLN B 169 ? 1.0695 1.1261 1.3407 -0.0461 0.1033  0.1182  1386 GLN B CB    
5050 C  CG    . GLN B 169 ? 1.0583 1.1067 1.3415 -0.0556 0.0934  0.1128  1386 GLN B CG    
5051 C  CD    . GLN B 169 ? 0.9907 1.0371 1.3000 -0.0683 0.1038  0.1183  1386 GLN B CD    
5052 O  OE1   . GLN B 169 ? 0.9586 0.9909 1.2608 -0.0677 0.1179  0.1298  1386 GLN B OE1   
5053 N  NE2   . GLN B 169 ? 0.9077 0.9677 1.2469 -0.0801 0.0968  0.1102  1386 GLN B NE2   
5054 N  N     . LYS B 170 ? 1.0595 1.0880 1.2456 -0.0163 0.0979  0.1227  1387 LYS B N     
5055 C  CA    . LYS B 170 ? 1.0300 1.0386 1.1840 -0.0082 0.0934  0.1269  1387 LYS B CA    
5056 C  C     . LYS B 170 ? 1.0800 1.0901 1.2214 -0.0027 0.0753  0.1164  1387 LYS B C     
5057 O  O     . LYS B 170 ? 1.0366 1.0356 1.1705 -0.0017 0.0655  0.1153  1387 LYS B O     
5058 C  CB    . LYS B 170 ? 0.9791 0.9786 1.1050 0.0007  0.1061  0.1369  1387 LYS B CB    
5059 C  CG    . LYS B 170 ? 1.0076 0.9863 1.1017 0.0083  0.1016  0.1432  1387 LYS B CG    
5060 C  CD    . LYS B 170 ? 1.1175 1.0907 1.1766 0.0195  0.1045  0.1460  1387 LYS B CD    
5061 C  CE    . LYS B 170 ? 1.2603 1.2257 1.3096 0.0207  0.1249  0.1590  1387 LYS B CE    
5062 N  NZ    . LYS B 170 ? 1.3650 1.3085 1.3923 0.0240  0.1265  0.1709  1387 LYS B NZ    
5063 N  N     . GLU B 171 ? 1.0454 1.0689 1.1850 0.0013  0.0716  0.1091  1388 GLU B N     
5064 C  CA    . GLU B 171 ? 0.9280 0.9547 1.0604 0.0049  0.0551  0.0986  1388 GLU B CA    
5065 C  C     . GLU B 171 ? 0.9347 0.9632 1.0872 -0.0029 0.0445  0.0923  1388 GLU B C     
5066 O  O     . GLU B 171 ? 0.9777 0.9976 1.1201 -0.0003 0.0336  0.0892  1388 GLU B O     
5067 C  CB    . GLU B 171 ? 0.8799 0.9227 1.0170 0.0077  0.0541  0.0914  1388 GLU B CB    
5068 C  CG    . GLU B 171 ? 1.1113 1.1512 1.2258 0.0164  0.0639  0.0953  1388 GLU B CG    
5069 C  CD    . GLU B 171 ? 1.3097 1.3653 1.4331 0.0189  0.0647  0.0884  1388 GLU B CD    
5070 O  OE1   . GLU B 171 ? 1.3710 1.4234 1.4733 0.0266  0.0591  0.0832  1388 GLU B OE1   
5071 O  OE2   . GLU B 171 ? 1.3114 1.3823 1.4632 0.0134  0.0707  0.0883  1388 GLU B OE2   
5072 N  N     . ALA B 172 ? 0.8911 0.9305 1.0724 -0.0127 0.0478  0.0903  1389 ALA B N     
5073 C  CA    . ALA B 172 ? 0.8204 0.8621 1.0194 -0.0206 0.0375  0.0825  1389 ALA B CA    
5074 C  C     . ALA B 172 ? 0.8547 0.8777 1.0484 -0.0223 0.0366  0.0862  1389 ALA B C     
5075 O  O     . ALA B 172 ? 0.9623 0.9801 1.1531 -0.0219 0.0257  0.0800  1389 ALA B O     
5076 C  CB    . ALA B 172 ? 0.5693 0.6264 0.7994 -0.0313 0.0409  0.0800  1389 ALA B CB    
5077 N  N     . ASP B 173 ? 0.8185 0.8305 1.0112 -0.0239 0.0489  0.0969  1390 ASP B N     
5078 C  CA    . ASP B 173 ? 0.8912 0.8835 1.0784 -0.0244 0.0494  0.1021  1390 ASP B CA    
5079 C  C     . ASP B 173 ? 0.9645 0.9465 1.1261 -0.0135 0.0404  0.1026  1390 ASP B C     
5080 O  O     . ASP B 173 ? 1.1540 1.1277 1.3165 -0.0135 0.0321  0.0989  1390 ASP B O     
5081 C  CB    . ASP B 173 ? 0.9643 0.9460 1.1509 -0.0261 0.0653  0.1152  1390 ASP B CB    
5082 C  CG    . ASP B 173 ? 1.0924 1.0811 1.3093 -0.0391 0.0735  0.1149  1390 ASP B CG    
5083 O  OD1   . ASP B 173 ? 1.0213 1.0149 1.2573 -0.0476 0.0654  0.1053  1390 ASP B OD1   
5084 O  OD2   . ASP B 173 ? 1.2119 1.2010 1.4331 -0.0411 0.0880  0.1242  1390 ASP B OD2   
5085 N  N     . GLU B 174 ? 0.9464 0.9288 1.0852 -0.0042 0.0419  0.1069  1391 GLU B N     
5086 C  CA    . GLU B 174 ? 0.9300 0.9028 1.0446 0.0058  0.0328  0.1085  1391 GLU B CA    
5087 C  C     . GLU B 174 ? 0.9078 0.8882 1.0271 0.0064  0.0180  0.0965  1391 GLU B C     
5088 O  O     . GLU B 174 ? 0.9178 0.8898 1.0322 0.0099  0.0098  0.0961  1391 GLU B O     
5089 C  CB    . GLU B 174 ? 1.0517 1.0235 1.1398 0.0146  0.0367  0.1139  1391 GLU B CB    
5090 C  CG    . GLU B 174 ? 1.3474 1.3046 1.4224 0.0168  0.0497  0.1283  1391 GLU B CG    
5091 C  CD    . GLU B 174 ? 1.5282 1.4829 1.5747 0.0250  0.0560  0.1341  1391 GLU B CD    
5092 O  OE1   . GLU B 174 ? 1.4423 1.4088 1.4853 0.0269  0.0548  0.1269  1391 GLU B OE1   
5093 O  OE2   . GLU B 174 ? 1.6687 1.6083 1.6953 0.0297  0.0627  0.1462  1391 GLU B OE2   
5094 N  N     . GLU B 175 ? 0.8806 0.8770 1.0121 0.0025  0.0150  0.0872  1392 GLU B N     
5095 C  CA    . GLU B 175 ? 0.8239 0.8272 0.9609 0.0021  0.0022  0.0762  1392 GLU B CA    
5096 C  C     . GLU B 175 ? 0.8551 0.8519 1.0075 -0.0041 -0.0010 0.0729  1392 GLU B C     
5097 O  O     . GLU B 175 ? 0.8136 0.8068 0.9629 -0.0011 -0.0101 0.0684  1392 GLU B O     
5098 C  CB    . GLU B 175 ? 0.6513 0.6719 0.7993 -0.0011 0.0006  0.0681  1392 GLU B CB    
5099 C  CG    . GLU B 175 ? 0.7550 0.7817 0.9083 -0.0020 -0.0120 0.0573  1392 GLU B CG    
5100 C  CD    . GLU B 175 ? 0.9200 0.9630 1.0858 -0.0055 -0.0143 0.0500  1392 GLU B CD    
5101 O  OE1   . GLU B 175 ? 0.9809 1.0297 1.1368 0.0002  -0.0178 0.0471  1392 GLU B OE1   
5102 O  OE2   . GLU B 175 ? 0.9280 0.9774 1.1132 -0.0140 -0.0132 0.0471  1392 GLU B OE2   
5103 N  N     . VAL B 176 ? 0.8417 0.8373 1.0116 -0.0131 0.0065  0.0742  1393 VAL B N     
5104 C  CA    . VAL B 176 ? 0.7487 0.7357 0.9316 -0.0195 0.0041  0.0700  1393 VAL B CA    
5105 C  C     . VAL B 176 ? 0.8222 0.7927 0.9930 -0.0124 0.0020  0.0752  1393 VAL B C     
5106 O  O     . VAL B 176 ? 0.8041 0.7703 0.9776 -0.0117 -0.0050 0.0692  1393 VAL B O     
5107 C  CB    . VAL B 176 ? 0.6464 0.6307 0.8477 -0.0302 0.0137  0.0726  1393 VAL B CB    
5108 C  CG1   . VAL B 176 ? 0.7730 0.7427 0.9830 -0.0356 0.0126  0.0694  1393 VAL B CG1   
5109 C  CG2   . VAL B 176 ? 0.7434 0.7461 0.9619 -0.0383 0.0132  0.0660  1393 VAL B CG2   
5110 N  N     . LEU B 177 ? 0.7985 0.7598 0.9553 -0.0063 0.0082  0.0868  1394 LEU B N     
5111 C  CA    . LEU B 177 ? 0.7197 0.6655 0.8655 0.0011  0.0060  0.0936  1394 LEU B CA    
5112 C  C     . LEU B 177 ? 0.8636 0.8143 0.9972 0.0100  -0.0064 0.0896  1394 LEU B C     
5113 O  O     . LEU B 177 ? 0.8832 0.8267 1.0181 0.0138  -0.0120 0.0891  1394 LEU B O     
5114 C  CB    . LEU B 177 ? 0.8630 0.7978 0.9949 0.0054  0.0154  0.1079  1394 LEU B CB    
5115 C  CG    . LEU B 177 ? 0.8777 0.8072 1.0243 -0.0041 0.0286  0.1123  1394 LEU B CG    
5116 C  CD1   . LEU B 177 ? 0.9216 0.8392 1.0532 0.0002  0.0398  0.1276  1394 LEU B CD1   
5117 C  CD2   . LEU B 177 ? 0.8073 0.7255 0.9705 -0.0101 0.0283  0.1086  1394 LEU B CD2   
5118 N  N     . THR B 178 ? 0.9817 0.9448 1.1049 0.0131  -0.0103 0.0865  1395 THR B N     
5119 C  CA    . THR B 178 ? 0.8833 0.8515 0.9960 0.0204  -0.0222 0.0823  1395 THR B CA    
5120 C  C     . THR B 178 ? 0.7363 0.7100 0.8640 0.0171  -0.0297 0.0713  1395 THR B C     
5121 O  O     . THR B 178 ? 0.7739 0.7450 0.9004 0.0222  -0.0373 0.0702  1395 THR B O     
5122 C  CB    . THR B 178 ? 0.8320 0.8107 0.9314 0.0232  -0.0236 0.0801  1395 THR B CB    
5123 O  OG1   . THR B 178 ? 0.7647 0.7368 0.8490 0.0260  -0.0146 0.0904  1395 THR B OG1   
5124 C  CG2   . THR B 178 ? 0.7444 0.7272 0.8318 0.0301  -0.0362 0.0758  1395 THR B CG2   
5125 N  N     . ILE B 179 ? 0.7305 0.7116 0.8727 0.0086  -0.0273 0.0636  1396 ILE B N     
5126 C  CA    . ILE B 179 ? 0.6738 0.6588 0.8279 0.0049  -0.0332 0.0533  1396 ILE B CA    
5127 C  C     . ILE B 179 ? 0.8214 0.7926 0.9838 0.0038  -0.0312 0.0543  1396 ILE B C     
5128 O  O     . ILE B 179 ? 0.8286 0.7987 0.9950 0.0056  -0.0365 0.0488  1396 ILE B O     
5129 C  CB    . ILE B 179 ? 0.7505 0.7466 0.9162 -0.0039 -0.0318 0.0456  1396 ILE B CB    
5130 C  CG1   . ILE B 179 ? 0.6834 0.6927 0.8420 -0.0017 -0.0329 0.0449  1396 ILE B CG1   
5131 C  CG2   . ILE B 179 ? 0.8318 0.8298 1.0065 -0.0077 -0.0376 0.0352  1396 ILE B CG2   
5132 C  CD1   . ILE B 179 ? 0.5065 0.5225 0.6563 0.0043  -0.0424 0.0396  1396 ILE B CD1   
5133 N  N     . LEU B 180 ? 0.9081 0.8676 1.0740 0.0007  -0.0225 0.0612  1397 LEU B N     
5134 C  CA    . LEU B 180 ? 0.8328 0.7769 1.0060 0.0004  -0.0200 0.0623  1397 LEU B CA    
5135 C  C     . LEU B 180 ? 0.8094 0.7471 0.9741 0.0117  -0.0248 0.0687  1397 LEU B C     
5136 O  O     . LEU B 180 ? 0.7676 0.6995 0.9391 0.0141  -0.0273 0.0655  1397 LEU B O     
5137 C  CB    . LEU B 180 ? 0.8917 0.8232 1.0705 -0.0053 -0.0093 0.0690  1397 LEU B CB    
5138 C  CG    . LEU B 180 ? 0.9067 0.8210 1.0957 -0.0079 -0.0058 0.0673  1397 LEU B CG    
5139 C  CD1   . LEU B 180 ? 0.9361 0.8539 1.1373 -0.0181 -0.0071 0.0537  1397 LEU B CD1   
5140 C  CD2   . LEU B 180 ? 0.7474 0.6452 0.9380 -0.0098 0.0047  0.0780  1397 LEU B CD2   
5141 N  N     . ASP B 181 ? 0.8308 0.7703 0.9806 0.0187  -0.0264 0.0776  1398 ASP B N     
5142 C  CA    . ASP B 181 ? 0.9365 0.8729 1.0778 0.0294  -0.0335 0.0836  1398 ASP B CA    
5143 C  C     . ASP B 181 ? 0.8578 0.8054 1.0039 0.0316  -0.0435 0.0741  1398 ASP B C     
5144 O  O     . ASP B 181 ? 0.8785 0.8224 1.0305 0.0371  -0.0476 0.0749  1398 ASP B O     
5145 C  CB    . ASP B 181 ? 1.1484 1.0862 1.2695 0.0353  -0.0347 0.0929  1398 ASP B CB    
5146 C  CG    . ASP B 181 ? 1.3576 1.2880 1.4685 0.0460  -0.0406 0.1029  1398 ASP B CG    
5147 O  OD1   . ASP B 181 ? 1.2952 1.2342 1.4029 0.0516  -0.0517 0.1000  1398 ASP B OD1   
5148 O  OD2   . ASP B 181 ? 1.5349 1.4510 1.6415 0.0487  -0.0342 0.1142  1398 ASP B OD2   
5149 N  N     . LEU B 182 ? 0.8080 0.7691 0.9540 0.0270  -0.0464 0.0651  1399 LEU B N     
5150 C  CA    . LEU B 182 ? 0.7420 0.7132 0.8926 0.0286  -0.0549 0.0565  1399 LEU B CA    
5151 C  C     . LEU B 182 ? 0.8346 0.8015 1.0006 0.0251  -0.0529 0.0495  1399 LEU B C     
5152 O  O     . LEU B 182 ? 0.7310 0.7005 0.9026 0.0294  -0.0580 0.0466  1399 LEU B O     
5153 C  CB    . LEU B 182 ? 0.7034 0.6881 0.8502 0.0244  -0.0574 0.0490  1399 LEU B CB    
5154 C  CG    . LEU B 182 ? 0.7040 0.6949 0.8345 0.0288  -0.0613 0.0524  1399 LEU B CG    
5155 C  CD1   . LEU B 182 ? 0.7490 0.7522 0.8799 0.0245  -0.0629 0.0436  1399 LEU B CD1   
5156 C  CD2   . LEU B 182 ? 0.5426 0.5341 0.6665 0.0370  -0.0706 0.0554  1399 LEU B CD2   
5157 N  N     . TYR B 183 ? 0.8638 0.8240 1.0367 0.0172  -0.0452 0.0465  1400 TYR B N     
5158 C  CA    . TYR B 183 ? 0.7969 0.7502 0.9815 0.0136  -0.0425 0.0392  1400 TYR B CA    
5159 C  C     . TYR B 183 ? 0.8699 0.8099 1.0594 0.0205  -0.0404 0.0452  1400 TYR B C     
5160 O  O     . TYR B 183 ? 0.9382 0.8767 1.1355 0.0233  -0.0416 0.0405  1400 TYR B O     
5161 C  CB    . TYR B 183 ? 0.7345 0.6825 0.9244 0.0030  -0.0357 0.0347  1400 TYR B CB    
5162 C  CG    . TYR B 183 ? 0.8087 0.7707 0.9983 -0.0042 -0.0385 0.0268  1400 TYR B CG    
5163 C  CD1   . TYR B 183 ? 0.7095 0.6833 0.8971 -0.0026 -0.0453 0.0200  1400 TYR B CD1   
5164 C  CD2   . TYR B 183 ? 0.7566 0.7201 0.9493 -0.0125 -0.0342 0.0267  1400 TYR B CD2   
5165 C  CE1   . TYR B 183 ? 0.6812 0.6667 0.8686 -0.0084 -0.0478 0.0137  1400 TYR B CE1   
5166 C  CE2   . TYR B 183 ? 0.6631 0.6403 0.8573 -0.0184 -0.0373 0.0202  1400 TYR B CE2   
5167 C  CZ    . TYR B 183 ? 0.7081 0.6958 0.8990 -0.0160 -0.0442 0.0140  1400 TYR B CZ    
5168 O  OH    . TYR B 183 ? 0.6256 0.6263 0.8181 -0.0212 -0.0473 0.0085  1400 TYR B OH    
5169 N  N     . ALA B 184 ? 0.9548 0.8842 1.1404 0.0235  -0.0363 0.0560  1401 ALA B N     
5170 C  CA    . ALA B 184 ? 0.9921 0.9087 1.1819 0.0317  -0.0348 0.0637  1401 ALA B CA    
5171 C  C     . ALA B 184 ? 0.9357 0.8624 1.1255 0.0414  -0.0445 0.0656  1401 ALA B C     
5172 O  O     . ALA B 184 ? 0.8884 0.8101 1.0885 0.0474  -0.0447 0.0664  1401 ALA B O     
5173 C  CB    . ALA B 184 ? 0.8202 0.7246 1.0029 0.0341  -0.0295 0.0768  1401 ALA B CB    
5174 N  N     . LYS B 185 ? 0.9141 0.8549 1.0934 0.0431  -0.0523 0.0662  1402 LYS B N     
5175 C  CA    . LYS B 185 ? 0.8840 0.8354 1.0643 0.0509  -0.0626 0.0669  1402 LYS B CA    
5176 C  C     . LYS B 185 ? 0.8932 0.8525 1.0864 0.0485  -0.0641 0.0557  1402 LYS B C     
5177 O  O     . LYS B 185 ? 1.0837 1.0463 1.2871 0.0549  -0.0682 0.0563  1402 LYS B O     
5178 C  CB    . LYS B 185 ? 0.8875 0.8499 1.0518 0.0522  -0.0702 0.0691  1402 LYS B CB    
5179 C  CG    . LYS B 185 ? 0.9837 0.9383 1.1333 0.0579  -0.0706 0.0821  1402 LYS B CG    
5180 C  CD    . LYS B 185 ? 1.1105 1.0751 1.2446 0.0628  -0.0814 0.0846  1402 LYS B CD    
5181 C  CE    . LYS B 185 ? 1.3005 1.2566 1.4142 0.0662  -0.0794 0.0960  1402 LYS B CE    
5182 N  NZ    . LYS B 185 ? 1.4330 1.3974 1.5272 0.0658  -0.0845 0.0937  1402 LYS B NZ    
5183 N  N     . VAL B 186 ? 0.8291 0.7917 1.0223 0.0396  -0.0606 0.0458  1403 VAL B N     
5184 C  CA    . VAL B 186 ? 0.7202 0.6866 0.9237 0.0369  -0.0597 0.0355  1403 VAL B CA    
5185 C  C     . VAL B 186 ? 0.8086 0.7622 1.0244 0.0402  -0.0533 0.0359  1403 VAL B C     
5186 O  O     . VAL B 186 ? 0.7356 0.6928 0.9621 0.0451  -0.0548 0.0339  1403 VAL B O     
5187 C  CB    . VAL B 186 ? 0.6778 0.6464 0.8778 0.0266  -0.0562 0.0262  1403 VAL B CB    
5188 C  CG1   . VAL B 186 ? 0.6219 0.5870 0.8303 0.0234  -0.0521 0.0167  1403 VAL B CG1   
5189 C  CG2   . VAL B 186 ? 0.7393 0.7227 0.9311 0.0250  -0.0629 0.0236  1403 VAL B CG2   
5190 N  N     . TYR B 187 ? 0.9037 0.8416 1.1192 0.0378  -0.0456 0.0391  1404 TYR B N     
5191 C  CA    . TYR B 187 ? 0.8162 0.7389 1.0427 0.0401  -0.0378 0.0380  1404 TYR B CA    
5192 C  C     . TYR B 187 ? 0.7664 0.6872 1.0014 0.0522  -0.0404 0.0479  1404 TYR B C     
5193 O  O     . TYR B 187 ? 0.7665 0.6852 1.0142 0.0570  -0.0379 0.0452  1404 TYR B O     
5194 C  CB    . TYR B 187 ? 0.7474 0.6527 0.9716 0.0332  -0.0289 0.0382  1404 TYR B CB    
5195 C  CG    . TYR B 187 ? 0.6765 0.5797 0.9006 0.0228  -0.0248 0.0249  1404 TYR B CG    
5196 C  CD1   . TYR B 187 ? 0.6993 0.6109 0.9159 0.0134  -0.0270 0.0203  1404 TYR B CD1   
5197 C  CD2   . TYR B 187 ? 0.7070 0.6013 0.9379 0.0228  -0.0195 0.0167  1404 TYR B CD2   
5198 C  CE1   . TYR B 187 ? 0.6387 0.5498 0.8542 0.0040  -0.0252 0.0084  1404 TYR B CE1   
5199 C  CE2   . TYR B 187 ? 0.6931 0.5851 0.9206 0.0133  -0.0167 0.0043  1404 TYR B CE2   
5200 C  CZ    . TYR B 187 ? 0.7138 0.6147 0.9334 0.0038  -0.0204 0.0003  1404 TYR B CZ    
5201 O  OH    . TYR B 187 ? 0.6885 0.5882 0.9040 -0.0056 -0.0194 -0.0116 1404 TYR B OH    
5202 N  N     . THR B 188 ? 0.7580 0.6803 0.9860 0.0577  -0.0457 0.0595  1405 THR B N     
5203 C  CA    . THR B 188 ? 0.9132 0.8331 1.1486 0.0696  -0.0492 0.0705  1405 THR B CA    
5204 C  C     . THR B 188 ? 1.0126 0.9514 1.2531 0.0759  -0.0608 0.0711  1405 THR B C     
5205 O  O     . THR B 188 ? 1.0115 0.9525 1.2680 0.0836  -0.0620 0.0731  1405 THR B O     
5206 C  CB    . THR B 188 ? 0.8896 0.8005 1.1129 0.0730  -0.0497 0.0838  1405 THR B CB    
5207 O  OG1   . THR B 188 ? 0.8643 0.7870 1.0710 0.0700  -0.0567 0.0849  1405 THR B OG1   
5208 C  CG2   . THR B 188 ? 0.7457 0.6364 0.9679 0.0670  -0.0373 0.0844  1405 THR B CG2   
5209 N  N     . ASP B 189 ? 1.0278 0.9803 1.2559 0.0729  -0.0692 0.0696  1406 ASP B N     
5210 C  CA    . ASP B 189 ? 0.9429 0.9123 1.1739 0.0782  -0.0816 0.0711  1406 ASP B CA    
5211 C  C     . ASP B 189 ? 0.9131 0.8942 1.1572 0.0752  -0.0822 0.0602  1406 ASP B C     
5212 O  O     . ASP B 189 ? 1.0301 1.0231 1.2868 0.0809  -0.0898 0.0616  1406 ASP B O     
5213 C  CB    . ASP B 189 ? 0.8360 0.8123 1.0464 0.0760  -0.0895 0.0735  1406 ASP B CB    
5214 C  CG    . ASP B 189 ? 0.9652 0.9318 1.1618 0.0816  -0.0909 0.0868  1406 ASP B CG    
5215 O  OD1   . ASP B 189 ? 1.0755 1.0295 1.2790 0.0870  -0.0860 0.0947  1406 ASP B OD1   
5216 O  OD2   . ASP B 189 ? 1.0950 1.0652 1.2726 0.0809  -0.0963 0.0895  1406 ASP B OD2   
5217 N  N     . LEU B 190 ? 0.7483 0.7269 0.9901 0.0664  -0.0747 0.0498  1407 LEU B N     
5218 C  CA    . LEU B 190 ? 0.8585 0.8459 1.1104 0.0631  -0.0734 0.0396  1407 LEU B CA    
5219 C  C     . LEU B 190 ? 0.9051 0.8819 1.1705 0.0639  -0.0625 0.0353  1407 LEU B C     
5220 O  O     . LEU B 190 ? 1.0456 1.0291 1.3262 0.0674  -0.0618 0.0326  1407 LEU B O     
5221 C  CB    . LEU B 190 ? 0.9155 0.9068 1.1548 0.0533  -0.0726 0.0307  1407 LEU B CB    
5222 C  CG    . LEU B 190 ? 0.8112 0.8160 1.0403 0.0505  -0.0815 0.0287  1407 LEU B CG    
5223 C  CD1   . LEU B 190 ? 0.7240 0.7326 0.9439 0.0556  -0.0908 0.0376  1407 LEU B CD1   
5224 C  CD2   . LEU B 190 ? 0.7101 0.7115 0.9271 0.0418  -0.0767 0.0229  1407 LEU B CD2   
5225 N  N     . LEU B 191 ? 0.8175 0.7776 1.0777 0.0604  -0.0534 0.0343  1408 LEU B N     
5226 C  CA    . LEU B 191 ? 0.8317 0.7789 1.1016 0.0603  -0.0422 0.0286  1408 LEU B CA    
5227 C  C     . LEU B 191 ? 0.8060 0.7407 1.0869 0.0695  -0.0379 0.0375  1408 LEU B C     
5228 O  O     . LEU B 191 ? 0.8994 0.8218 1.1896 0.0712  -0.0280 0.0334  1408 LEU B O     
5229 C  CB    . LEU B 191 ? 0.8811 0.8166 1.1392 0.0496  -0.0349 0.0200  1408 LEU B CB    
5230 C  CG    . LEU B 191 ? 0.8023 0.7496 1.0523 0.0415  -0.0378 0.0103  1408 LEU B CG    
5231 C  CD1   . LEU B 191 ? 0.8798 0.8159 1.1207 0.0315  -0.0310 0.0009  1408 LEU B CD1   
5232 C  CD2   . LEU B 191 ? 0.7234 0.6813 0.9841 0.0453  -0.0384 0.0063  1408 LEU B CD2   
5233 N  N     . ALA B 192 ? 0.7675 0.7045 1.0469 0.0761  -0.0453 0.0496  1409 ALA B N     
5234 C  CA    . ALA B 192 ? 0.8293 0.7558 1.1197 0.0864  -0.0429 0.0601  1409 ALA B CA    
5235 C  C     . ALA B 192 ? 0.8332 0.7353 1.1227 0.0838  -0.0296 0.0584  1409 ALA B C     
5236 O  O     . ALA B 192 ? 0.8122 0.7022 1.1150 0.0913  -0.0229 0.0620  1409 ALA B O     
5237 C  CB    . ALA B 192 ? 0.7906 0.7274 1.1031 0.0957  -0.0447 0.0612  1409 ALA B CB    
5238 N  N     . ILE B 193 ? 0.8594 0.7539 1.1340 0.0731  -0.0261 0.0533  1410 ILE B N     
5239 C  CA    . ILE B 193 ? 0.8136 0.6850 1.0859 0.0679  -0.0145 0.0504  1410 ILE B CA    
5240 C  C     . ILE B 193 ? 0.6757 0.5392 0.9372 0.0664  -0.0154 0.0608  1410 ILE B C     
5241 O  O     . ILE B 193 ? 0.7046 0.5791 0.9537 0.0610  -0.0214 0.0615  1410 ILE B O     
5242 C  CB    . ILE B 193 ? 0.8025 0.6719 1.0677 0.0552  -0.0097 0.0353  1410 ILE B CB    
5243 C  CG1   . ILE B 193 ? 0.6304 0.5060 0.9038 0.0566  -0.0073 0.0252  1410 ILE B CG1   
5244 C  CG2   . ILE B 193 ? 0.8587 0.7046 1.1204 0.0481  0.0005  0.0322  1410 ILE B CG2   
5245 C  CD1   . ILE B 193 ? 0.7511 0.6249 1.0143 0.0444  -0.0038 0.0106  1410 ILE B CD1   
5246 N  N     . PRO B 194 ? 0.6715 0.5153 0.9370 0.0710  -0.0085 0.0690  1411 PRO B N     
5247 C  CA    . PRO B 194 ? 0.8244 0.6585 1.0791 0.0685  -0.0071 0.0788  1411 PRO B CA    
5248 C  C     . PRO B 194 ? 0.8506 0.6755 1.0985 0.0540  0.0000  0.0696  1411 PRO B C     
5249 O  O     . PRO B 194 ? 0.8454 0.6635 1.0976 0.0472  0.0058  0.0569  1411 PRO B O     
5250 C  CB    . PRO B 194 ? 0.7885 0.6027 1.0521 0.0785  -0.0009 0.0900  1411 PRO B CB    
5251 C  CG    . PRO B 194 ? 0.7197 0.5255 0.9975 0.0803  0.0064  0.0803  1411 PRO B CG    
5252 C  CD    . PRO B 194 ? 0.7082 0.5362 0.9886 0.0788  -0.0002 0.0698  1411 PRO B CD    
5253 N  N     . VAL B 195 ? 0.8783 0.7044 1.1151 0.0490  -0.0010 0.0760  1412 VAL B N     
5254 C  CA    . VAL B 195 ? 0.9951 0.8155 1.2278 0.0350  0.0048  0.0690  1412 VAL B CA    
5255 C  C     . VAL B 195 ? 0.9890 0.7998 1.2151 0.0339  0.0089  0.0819  1412 VAL B C     
5256 O  O     . VAL B 195 ? 1.0544 0.8675 1.2742 0.0434  0.0051  0.0954  1412 VAL B O     
5257 C  CB    . VAL B 195 ? 0.9863 0.8281 1.2128 0.0266  -0.0019 0.0589  1412 VAL B CB    
5258 C  CG1   . VAL B 195 ? 0.8618 0.7079 1.0936 0.0238  -0.0027 0.0444  1412 VAL B CG1   
5259 C  CG2   . VAL B 195 ? 0.9780 0.8393 1.1957 0.0332  -0.0118 0.0662  1412 VAL B CG2   
5260 N  N     . VAL B 196 ? 0.8783 0.6795 1.1051 0.0216  0.0162  0.0777  1413 VAL B N     
5261 C  CA    . VAL B 196 ? 0.8678 0.6604 1.0898 0.0182  0.0221  0.0888  1413 VAL B CA    
5262 C  C     . VAL B 196 ? 0.9058 0.7149 1.1234 0.0071  0.0201  0.0835  1413 VAL B C     
5263 O  O     . VAL B 196 ? 0.8459 0.6599 1.0689 -0.0034 0.0197  0.0698  1413 VAL B O     
5264 C  CB    . VAL B 196 ? 0.9642 0.7296 1.1946 0.0127  0.0339  0.0897  1413 VAL B CB    
5265 C  CG1   . VAL B 196 ? 0.8539 0.6011 1.0869 0.0257  0.0375  0.1015  1413 VAL B CG1   
5266 C  CG2   . VAL B 196 ? 1.0704 0.8310 1.3091 0.0027  0.0361  0.0722  1413 VAL B CG2   
5267 N  N     . LYS B 197 ? 0.8172 0.6349 1.0244 0.0101  0.0187  0.0943  1414 LYS B N     
5268 C  CA    . LYS B 197 ? 0.6820 0.5149 0.8859 0.0012  0.0184  0.0913  1414 LYS B CA    
5269 C  C     . LYS B 197 ? 1.0788 0.8985 1.2894 -0.0095 0.0297  0.0949  1414 LYS B C     
5270 O  O     . LYS B 197 ? 0.8793 0.6809 1.0887 -0.0063 0.0375  0.1070  1414 LYS B O     
5271 C  CB    . LYS B 197 ? 0.6775 0.5241 0.8661 0.0094  0.0131  0.1007  1414 LYS B CB    
5272 C  CG    . LYS B 197 ? 0.7972 0.6563 0.9790 0.0203  0.0013  0.0992  1414 LYS B CG    
5273 C  CD    . LYS B 197 ? 0.7724 0.6394 0.9363 0.0287  -0.0032 0.1103  1414 LYS B CD    
5274 C  CE    . LYS B 197 ? 1.0391 0.9271 1.1965 0.0320  -0.0149 0.1031  1414 LYS B CE    
5275 N  NZ    . LYS B 197 ? 1.0365 0.9344 1.1769 0.0333  -0.0163 0.1080  1414 LYS B NZ    
5276 N  N     . GLY B 198 ? 1.0142 0.8435 1.2329 -0.0222 0.0303  0.0849  1415 GLY B N     
5277 C  CA    . GLY B 198 ? 0.9148 0.7326 1.1430 -0.0333 0.0406  0.0878  1415 GLY B CA    
5278 C  C     . GLY B 198 ? 1.0668 0.9023 1.3033 -0.0458 0.0393  0.0790  1415 GLY B C     
5279 O  O     . GLY B 198 ? 1.1213 0.9771 1.3550 -0.0454 0.0306  0.0712  1415 GLY B O     
5280 N  N     . ARG B 199 ? 1.0646 0.8918 1.3128 -0.0572 0.0482  0.0810  1416 ARG B N     
5281 C  CA    . ARG B 199 ? 1.0354 0.8780 1.2966 -0.0707 0.0480  0.0739  1416 ARG B CA    
5282 C  C     . ARG B 199 ? 0.9860 0.8169 1.2610 -0.0836 0.0481  0.0614  1416 ARG B C     
5283 O  O     . ARG B 199 ? 1.1236 0.9302 1.4026 -0.0858 0.0556  0.0640  1416 ARG B O     
5284 C  CB    . ARG B 199 ? 1.1117 0.9552 1.3773 -0.0743 0.0587  0.0867  1416 ARG B CB    
5285 C  CG    . ARG B 199 ? 1.2394 1.1059 1.5175 -0.0841 0.0581  0.0826  1416 ARG B CG    
5286 C  CD    . ARG B 199 ? 1.4241 1.2928 1.7029 -0.0838 0.0700  0.0974  1416 ARG B CD    
5287 N  NE    . ARG B 199 ? 1.4811 1.3624 1.7413 -0.0709 0.0682  0.1046  1416 ARG B NE    
5288 C  CZ    . ARG B 199 ? 1.4707 1.3679 1.7319 -0.0713 0.0735  0.1102  1416 ARG B CZ    
5289 N  NH1   . ARG B 199 ? 1.4718 1.3763 1.7543 -0.0837 0.0810  0.1103  1416 ARG B NH1   
5290 N  NH2   . ARG B 199 ? 1.4286 1.3344 1.6701 -0.0593 0.0715  0.1154  1416 ARG B NH2   
5291 N  N     . LYS B 200 ? 0.8622 0.7090 1.1429 -0.0913 0.0394  0.0475  1417 LYS B N     
5292 C  CA    . LYS B 200 ? 0.7759 0.6129 1.0682 -0.1052 0.0385  0.0348  1417 LYS B CA    
5293 C  C     . LYS B 200 ? 0.9303 0.7618 1.2397 -0.1183 0.0474  0.0394  1417 LYS B C     
5294 O  O     . LYS B 200 ? 1.1069 0.9528 1.4221 -0.1192 0.0515  0.0487  1417 LYS B O     
5295 C  CB    . LYS B 200 ? 0.7978 0.6549 1.0915 -0.1112 0.0266  0.0203  1417 LYS B CB    
5296 C  CG    . LYS B 200 ? 0.8933 0.7580 1.1713 -0.0993 0.0180  0.0154  1417 LYS B CG    
5297 C  CD    . LYS B 200 ? 1.0173 0.8598 1.2885 -0.0964 0.0186  0.0079  1417 LYS B CD    
5298 C  CE    . LYS B 200 ? 1.0397 0.8920 1.2993 -0.0888 0.0097  -0.0003 1417 LYS B CE    
5299 N  NZ    . LYS B 200 ? 1.0871 0.9185 1.3415 -0.0869 0.0116  -0.0090 1417 LYS B NZ    
5300 N  N     . THR B 201 ? 0.9444 0.7544 1.2623 -0.1286 0.0512  0.0328  1418 THR B N     
5301 C  CA    . THR B 201 ? 0.9230 0.7294 1.2602 -0.1437 0.0582  0.0346  1418 THR B CA    
5302 C  C     . THR B 201 ? 0.8486 0.6820 1.1992 -0.1557 0.0491  0.0250  1418 THR B C     
5303 O  O     . THR B 201 ? 0.9310 0.7804 1.2746 -0.1534 0.0373  0.0151  1418 THR B O     
5304 C  CB    . THR B 201 ? 0.9975 0.7733 1.3406 -0.1530 0.0634  0.0277  1418 THR B CB    
5305 O  OG1   . THR B 201 ? 0.9182 0.6927 1.2561 -0.1573 0.0531  0.0097  1418 THR B OG1   
5306 C  CG2   . THR B 201 ? 1.0118 0.7600 1.3442 -0.1407 0.0733  0.0388  1418 THR B CG2   
5307 N  N     . GLU B 202 ? 0.8346 0.6728 1.2060 -0.1687 0.0547  0.0285  1419 GLU B N     
5308 C  CA    . GLU B 202 ? 0.9917 0.8576 1.3791 -0.1797 0.0459  0.0210  1419 GLU B CA    
5309 C  C     . GLU B 202 ? 0.9780 0.8429 1.3647 -0.1890 0.0330  0.0020  1419 GLU B C     
5310 O  O     . GLU B 202 ? 1.0386 0.9278 1.4297 -0.1929 0.0214  -0.0057 1419 GLU B O     
5311 C  CB    . GLU B 202 ? 0.9907 0.8615 1.4043 -0.1931 0.0549  0.0279  1419 GLU B CB    
5312 C  CG    . GLU B 202 ? 1.1030 0.9780 1.5146 -0.1831 0.0679  0.0467  1419 GLU B CG    
5313 C  CD    . GLU B 202 ? 1.1348 1.0439 1.5528 -0.1797 0.0645  0.0504  1419 GLU B CD    
5314 O  OE1   . GLU B 202 ? 1.1580 1.0891 1.5900 -0.1883 0.0537  0.0402  1419 GLU B OE1   
5315 O  OE2   . GLU B 202 ? 1.1986 1.1119 1.6069 -0.1679 0.0729  0.0639  1419 GLU B OE2   
5316 N  N     . LYS B 203 ? 0.9540 0.7903 1.3339 -0.1924 0.0348  -0.0057 1420 LYS B N     
5317 C  CA    . LYS B 203 ? 0.9198 0.7528 1.2945 -0.2005 0.0231  -0.0242 1420 LYS B CA    
5318 C  C     . LYS B 203 ? 0.9244 0.7690 1.2781 -0.1874 0.0135  -0.0291 1420 LYS B C     
5319 O  O     . LYS B 203 ? 0.9268 0.7885 1.2793 -0.1924 0.0010  -0.0398 1420 LYS B O     
5320 C  CB    . LYS B 203 ? 0.9121 0.7084 1.2826 -0.2061 0.0292  -0.0315 1420 LYS B CB    
5321 C  CG    . LYS B 203 ? 0.8927 0.6830 1.2507 -0.2112 0.0181  -0.0507 1420 LYS B CG    
5322 C  CD    . LYS B 203 ? 0.9704 0.7235 1.3207 -0.2146 0.0244  -0.0594 1420 LYS B CD    
5323 C  CE    . LYS B 203 ? 0.9414 0.6897 1.2743 -0.2170 0.0139  -0.0781 1420 LYS B CE    
5324 N  NZ    . LYS B 203 ? 1.0562 0.7737 1.3897 -0.2308 0.0168  -0.0915 1420 LYS B NZ    
5325 N  N     . GLU B 204 ? 1.0009 0.8364 1.3385 -0.1707 0.0189  -0.0209 1421 GLU B N     
5326 C  CA    . GLU B 204 ? 1.0371 0.8781 1.3551 -0.1583 0.0117  -0.0259 1421 GLU B CA    
5327 C  C     . GLU B 204 ? 1.0148 0.8844 1.3289 -0.1481 0.0065  -0.0185 1421 GLU B C     
5328 O  O     . GLU B 204 ? 1.0508 0.9277 1.3507 -0.1397 -0.0007 -0.0235 1421 GLU B O     
5329 C  CB    . GLU B 204 ? 1.0583 0.8742 1.3629 -0.1455 0.0196  -0.0216 1421 GLU B CB    
5330 C  CG    . GLU B 204 ? 1.0967 0.8828 1.3997 -0.1527 0.0235  -0.0323 1421 GLU B CG    
5331 C  CD    . GLU B 204 ? 1.1095 0.8955 1.3998 -0.1546 0.0143  -0.0490 1421 GLU B CD    
5332 O  OE1   . GLU B 204 ? 1.2372 1.0302 1.5139 -0.1417 0.0111  -0.0488 1421 GLU B OE1   
5333 O  OE2   . GLU B 204 ? 1.0767 0.8555 1.3700 -0.1692 0.0103  -0.0623 1421 GLU B OE2   
5334 N  N     . LYS B 205 ? 0.9678 0.8524 1.2938 -0.1486 0.0107  -0.0071 1422 LYS B N     
5335 C  CA    . LYS B 205 ? 0.7850 0.6961 1.1081 -0.1398 0.0066  -0.0008 1422 LYS B CA    
5336 C  C     . LYS B 205 ? 0.8713 0.8050 1.1978 -0.1457 -0.0064 -0.0115 1422 LYS B C     
5337 O  O     . LYS B 205 ? 0.9089 0.8410 1.2432 -0.1587 -0.0123 -0.0226 1422 LYS B O     
5338 C  CB    . LYS B 205 ? 0.6649 0.5852 1.0007 -0.1403 0.0158  0.0130  1422 LYS B CB    
5339 C  CG    . LYS B 205 ? 0.6665 0.6030 1.0258 -0.1553 0.0140  0.0100  1422 LYS B CG    
5340 C  CD    . LYS B 205 ? 0.7860 0.7375 1.1547 -0.1519 0.0226  0.0238  1422 LYS B CD    
5341 C  CE    . LYS B 205 ? 0.6989 0.6681 1.0952 -0.1663 0.0225  0.0228  1422 LYS B CE    
5342 N  NZ    . LYS B 205 ? 0.8082 0.7838 1.2130 -0.1629 0.0361  0.0380  1422 LYS B NZ    
5343 N  N     . PHE B 206 ? 0.9026 0.8560 1.2211 -0.1353 -0.0114 -0.0084 1423 PHE B N     
5344 C  CA    . PHE B 206 ? 0.8193 0.7973 1.1425 -0.1387 -0.0227 -0.0148 1423 PHE B CA    
5345 C  C     . PHE B 206 ? 0.8926 0.8860 1.2402 -0.1512 -0.0226 -0.0134 1423 PHE B C     
5346 O  O     . PHE B 206 ? 0.8561 0.8562 1.2147 -0.1496 -0.0136 -0.0021 1423 PHE B O     
5347 C  CB    . PHE B 206 ? 0.9252 0.9198 1.2384 -0.1250 -0.0246 -0.0085 1423 PHE B CB    
5348 C  CG    . PHE B 206 ? 0.9502 0.9681 1.2657 -0.1262 -0.0362 -0.0146 1423 PHE B CG    
5349 C  CD1   . PHE B 206 ? 0.9494 0.9662 1.2595 -0.1322 -0.0467 -0.0270 1423 PHE B CD1   
5350 C  CD2   . PHE B 206 ? 1.0118 1.0515 1.3336 -0.1208 -0.0362 -0.0076 1423 PHE B CD2   
5351 C  CE1   . PHE B 206 ? 0.8934 0.9306 1.2042 -0.1325 -0.0577 -0.0314 1423 PHE B CE1   
5352 C  CE2   . PHE B 206 ? 1.0102 1.0704 1.3345 -0.1209 -0.0467 -0.0122 1423 PHE B CE2   
5353 C  CZ    . PHE B 206 ? 0.9486 1.0077 1.2675 -0.1267 -0.0578 -0.0237 1423 PHE B CZ    
5354 N  N     . ALA B 207 ? 0.9936 0.9939 1.3492 -0.1631 -0.0331 -0.0247 1424 ALA B N     
5355 C  CA    . ALA B 207 ? 1.0082 1.0223 1.3906 -0.1776 -0.0347 -0.0251 1424 ALA B CA    
5356 C  C     . ALA B 207 ? 1.0683 1.1100 1.4659 -0.1732 -0.0326 -0.0150 1424 ALA B C     
5357 O  O     . ALA B 207 ? 1.1175 1.1654 1.5366 -0.1792 -0.0242 -0.0072 1424 ALA B O     
5358 C  CB    . ALA B 207 ? 0.8557 0.8751 1.2402 -0.1894 -0.0495 -0.0396 1424 ALA B CB    
5359 N  N     . GLY B 208 ? 1.0854 1.1430 1.4726 -0.1625 -0.0391 -0.0145 1425 GLY B N     
5360 C  CA    . GLY B 208 ? 1.1539 1.2369 1.5564 -0.1585 -0.0368 -0.0058 1425 GLY B CA    
5361 C  C     . GLY B 208 ? 1.1902 1.2696 1.5887 -0.1479 -0.0220 0.0075  1425 GLY B C     
5362 O  O     . GLY B 208 ? 1.3648 1.4633 1.7773 -0.1452 -0.0172 0.0152  1425 GLY B O     
5363 N  N     . GLY B 209 ? 1.0432 1.0987 1.4227 -0.1414 -0.0148 0.0105  1426 GLY B N     
5364 C  CA    . GLY B 209 ? 0.8583 0.9089 1.2288 -0.1303 -0.0025 0.0230  1426 GLY B CA    
5365 C  C     . GLY B 209 ? 0.8400 0.8817 1.2247 -0.1366 0.0116  0.0323  1426 GLY B C     
5366 O  O     . GLY B 209 ? 0.7940 0.8280 1.1942 -0.1498 0.0126  0.0288  1426 GLY B O     
5367 N  N     . ASP B 210 ? 0.8716 0.9135 1.2493 -0.1269 0.0229  0.0444  1427 ASP B N     
5368 C  CA    . ASP B 210 ? 0.8201 0.8470 1.2017 -0.1290 0.0380  0.0555  1427 ASP B CA    
5369 C  C     . ASP B 210 ? 0.9873 0.9848 1.3521 -0.1269 0.0395  0.0552  1427 ASP B C     
5370 O  O     . ASP B 210 ? 1.0049 0.9866 1.3806 -0.1370 0.0448  0.0553  1427 ASP B O     
5371 C  CB    . ASP B 210 ? 0.7852 0.8182 1.1567 -0.1171 0.0487  0.0680  1427 ASP B CB    
5372 C  CG    . ASP B 210 ? 1.0582 1.0788 1.4348 -0.1195 0.0661  0.0812  1427 ASP B CG    
5373 O  OD1   . ASP B 210 ? 1.0671 1.0918 1.4344 -0.1105 0.0761  0.0915  1427 ASP B OD1   
5374 O  OD2   . ASP B 210 ? 1.2030 1.2088 1.5915 -0.1301 0.0704  0.0814  1427 ASP B OD2   
5375 N  N     . TYR B 211 ? 0.9269 0.9165 1.2665 -0.1139 0.0348  0.0546  1428 TYR B N     
5376 C  CA    . TYR B 211 ? 0.8794 0.8433 1.2044 -0.1103 0.0352  0.0540  1428 TYR B CA    
5377 C  C     . TYR B 211 ? 0.9744 0.9396 1.2807 -0.1004 0.0239  0.0467  1428 TYR B C     
5378 O  O     . TYR B 211 ? 1.0642 1.0482 1.3666 -0.0957 0.0169  0.0435  1428 TYR B O     
5379 C  CB    . TYR B 211 ? 0.8307 0.7774 1.1450 -0.1028 0.0480  0.0688  1428 TYR B CB    
5380 C  CG    . TYR B 211 ? 0.8953 0.8502 1.1912 -0.0888 0.0498  0.0774  1428 TYR B CG    
5381 C  CD1   . TYR B 211 ? 1.0264 0.9768 1.3005 -0.0763 0.0425  0.0762  1428 TYR B CD1   
5382 C  CD2   . TYR B 211 ? 0.8866 0.8535 1.1874 -0.0883 0.0591  0.0864  1428 TYR B CD2   
5383 C  CE1   . TYR B 211 ? 1.0983 1.0554 1.3545 -0.0643 0.0431  0.0831  1428 TYR B CE1   
5384 C  CE2   . TYR B 211 ? 0.9999 0.9725 1.2813 -0.0757 0.0610  0.0933  1428 TYR B CE2   
5385 C  CZ    . TYR B 211 ? 1.0817 1.0490 1.3402 -0.0639 0.0524  0.0913  1428 TYR B CZ    
5386 O  OH    . TYR B 211 ? 1.0365 1.0087 1.2748 -0.0521 0.0532  0.0971  1428 TYR B OH    
5387 N  N     . THR B 212 ? 1.0071 0.9512 1.3030 -0.0974 0.0230  0.0443  1429 THR B N     
5388 C  CA    . THR B 212 ? 0.9211 0.8629 1.2020 -0.0895 0.0136  0.0367  1429 THR B CA    
5389 C  C     . THR B 212 ? 0.9907 0.9122 1.2574 -0.0787 0.0183  0.0445  1429 THR B C     
5390 O  O     . THR B 212 ? 1.0327 0.9335 1.3035 -0.0823 0.0251  0.0469  1429 THR B O     
5391 C  CB    . THR B 212 ? 0.7928 0.7296 1.0799 -0.0994 0.0067  0.0223  1429 THR B CB    
5392 O  OG1   . THR B 212 ? 0.7252 0.6829 1.0236 -0.1080 -0.0005 0.0149  1429 THR B OG1   
5393 C  CG2   . THR B 212 ? 0.7727 0.7020 1.0445 -0.0909 0.0004  0.0158  1429 THR B CG2   
5394 N  N     . THR B 213 ? 0.9691 0.8958 1.2200 -0.0657 0.0148  0.0489  1430 THR B N     
5395 C  CA    . THR B 213 ? 0.9047 0.8141 1.1435 -0.0552 0.0164  0.0550  1430 THR B CA    
5396 C  C     . THR B 213 ? 0.8230 0.7300 1.0578 -0.0520 0.0081  0.0444  1430 THR B C     
5397 O  O     . THR B 213 ? 0.8272 0.7480 1.0637 -0.0556 0.0006  0.0340  1430 THR B O     
5398 C  CB    . THR B 213 ? 0.8744 0.7884 1.0978 -0.0428 0.0170  0.0664  1430 THR B CB    
5399 O  OG1   . THR B 213 ? 0.7951 0.7270 1.0109 -0.0376 0.0076  0.0607  1430 THR B OG1   
5400 C  CG2   . THR B 213 ? 0.9905 0.9075 1.2158 -0.0455 0.0264  0.0766  1430 THR B CG2   
5401 N  N     . THR B 214 ? 0.7535 0.6431 0.9833 -0.0447 0.0101  0.0479  1431 THR B N     
5402 C  CA    . THR B 214 ? 0.8172 0.7012 1.0460 -0.0425 0.0052  0.0379  1431 THR B CA    
5403 C  C     . THR B 214 ? 0.8668 0.7383 1.0892 -0.0298 0.0063  0.0456  1431 THR B C     
5404 O  O     . THR B 214 ? 0.9167 0.7782 1.1362 -0.0247 0.0117  0.0582  1431 THR B O     
5405 C  CB    . THR B 214 ? 0.9165 0.7871 1.1554 -0.0544 0.0085  0.0279  1431 THR B CB    
5406 O  OG1   . THR B 214 ? 1.0273 0.8925 1.2634 -0.0525 0.0047  0.0173  1431 THR B OG1   
5407 C  CG2   . THR B 214 ? 0.9163 0.7636 1.1607 -0.0564 0.0190  0.0358  1431 THR B CG2   
5408 N  N     . VAL B 215 ? 0.9389 0.8119 1.1592 -0.0244 0.0008  0.0385  1432 VAL B N     
5409 C  CA    . VAL B 215 ? 0.9611 0.8212 1.1807 -0.0137 0.0020  0.0430  1432 VAL B CA    
5410 C  C     . VAL B 215 ? 0.9158 0.7604 1.1422 -0.0180 0.0059  0.0322  1432 VAL B C     
5411 O  O     . VAL B 215 ? 0.7356 0.5866 0.9622 -0.0248 0.0027  0.0195  1432 VAL B O     
5412 C  CB    . VAL B 215 ? 0.8864 0.7614 1.0998 -0.0026 -0.0066 0.0446  1432 VAL B CB    
5413 C  CG1   . VAL B 215 ? 0.8708 0.7548 1.0748 0.0033  -0.0093 0.0566  1432 VAL B CG1   
5414 C  CG2   . VAL B 215 ? 0.8049 0.6961 1.0176 -0.0067 -0.0133 0.0319  1432 VAL B CG2   
5415 N  N     . GLU B 216 ? 1.0290 0.8518 1.2596 -0.0142 0.0133  0.0373  1433 GLU B N     
5416 C  CA    . GLU B 216 ? 0.9346 0.7398 1.1705 -0.0171 0.0183  0.0270  1433 GLU B CA    
5417 C  C     . GLU B 216 ? 0.8582 0.6560 1.0965 -0.0032 0.0194  0.0313  1433 GLU B C     
5418 O  O     . GLU B 216 ? 0.7971 0.5929 1.0354 0.0072  0.0195  0.0450  1433 GLU B O     
5419 C  CB    . GLU B 216 ? 0.9952 0.7779 1.2368 -0.0267 0.0276  0.0267  1433 GLU B CB    
5420 C  CG    . GLU B 216 ? 0.9857 0.7766 1.2290 -0.0408 0.0269  0.0238  1433 GLU B CG    
5421 C  CD    . GLU B 216 ? 1.0712 0.8637 1.3156 -0.0537 0.0240  0.0067  1433 GLU B CD    
5422 O  OE1   . GLU B 216 ? 1.1711 0.9824 1.4156 -0.0617 0.0182  0.0030  1433 GLU B OE1   
5423 O  OE2   . GLU B 216 ? 1.0253 0.8001 1.2699 -0.0557 0.0277  -0.0030 1433 GLU B OE2   
5424 N  N     . ALA B 217 ? 0.8114 0.6055 1.0516 -0.0029 0.0203  0.0195  1434 ALA B N     
5425 C  CA    . ALA B 217 ? 0.9239 0.7121 1.1696 0.0097  0.0225  0.0216  1434 ALA B CA    
5426 C  C     . ALA B 217 ? 1.0138 0.7768 1.2637 0.0070  0.0326  0.0123  1434 ALA B C     
5427 O  O     . ALA B 217 ? 0.9992 0.7532 1.2455 -0.0058 0.0355  0.0011  1434 ALA B O     
5428 C  CB    . ALA B 217 ? 1.0465 0.8561 1.2908 0.0147  0.0149  0.0167  1434 ALA B CB    
5429 N  N     . TYR B 218 ? 1.0147 0.7669 1.2726 0.0192  0.0377  0.0166  1435 TYR B N     
5430 C  CA    . TYR B 218 ? 0.9788 0.7036 1.2415 0.0193  0.0492  0.0098  1435 TYR B CA    
5431 C  C     . TYR B 218 ? 0.9583 0.6857 1.2249 0.0269  0.0516  0.0018  1435 TYR B C     
5432 O  O     . TYR B 218 ? 1.0355 0.7769 1.3098 0.0394  0.0478  0.0098  1435 TYR B O     
5433 C  CB    . TYR B 218 ? 1.1866 0.8918 1.4575 0.0281  0.0559  0.0239  1435 TYR B CB    
5434 C  CG    . TYR B 218 ? 1.3828 1.0562 1.6596 0.0292  0.0690  0.0186  1435 TYR B CG    
5435 C  CD1   . TYR B 218 ? 1.4580 1.1198 1.7463 0.0446  0.0749  0.0277  1435 TYR B CD1   
5436 C  CD2   . TYR B 218 ? 1.4369 1.0915 1.7080 0.0150  0.0753  0.0045  1435 TYR B CD2   
5437 C  CE1   . TYR B 218 ? 1.5404 1.1714 1.8343 0.0465  0.0881  0.0228  1435 TYR B CE1   
5438 C  CE2   . TYR B 218 ? 1.4712 1.0945 1.7463 0.0158  0.0878  -0.0014 1435 TYR B CE2   
5439 C  CZ    . TYR B 218 ? 1.5119 1.1229 1.7983 0.0318  0.0948  0.0077  1435 TYR B CZ    
5440 O  OH    . TYR B 218 ? 1.4630 1.0412 1.7533 0.0330  0.1082  0.0016  1435 TYR B OH    
5441 N  N     . ILE B 219 ? 0.8263 0.5398 1.0875 0.0191  0.0581  -0.0140 1436 ILE B N     
5442 C  CA    . ILE B 219 ? 0.8800 0.5890 1.1440 0.0259  0.0646  -0.0226 1436 ILE B CA    
5443 C  C     . ILE B 219 ? 0.9967 0.6734 1.2671 0.0301  0.0784  -0.0241 1436 ILE B C     
5444 O  O     . ILE B 219 ? 0.9536 0.6078 1.2166 0.0192  0.0843  -0.0335 1436 ILE B O     
5445 C  CB    . ILE B 219 ? 0.7554 0.4703 1.0055 0.0150  0.0628  -0.0394 1436 ILE B CB    
5446 N  N     . SER B 220 ? 1.0334 0.7072 1.3184 0.0460  0.0833  -0.0149 1437 SER B N     
5447 C  CA    . SER B 220 ? 0.9475 0.5904 1.2409 0.0524  0.0967  -0.0136 1437 SER B CA    
5448 C  C     . SER B 220 ? 1.1701 0.7928 1.4590 0.0506  0.1092  -0.0308 1437 SER B C     
5449 O  O     . SER B 220 ? 1.3121 0.9033 1.6008 0.0491  0.1207  -0.0355 1437 SER B O     
5450 C  CB    . SER B 220 ? 0.8974 0.5456 1.2095 0.0710  0.0971  0.0030  1437 SER B CB    
5451 O  OG    . SER B 220 ? 1.0679 0.7340 1.3891 0.0806  0.0966  0.0010  1437 SER B OG    
5452 N  N     . ALA B 221 ? 1.2942 0.9327 1.5796 0.0517  0.1082  -0.0395 1438 ALA B N     
5453 C  CA    . ALA B 221 ? 1.3472 0.9670 1.6245 0.0496  0.1204  -0.0563 1438 ALA B CA    
5454 C  C     . ALA B 221 ? 1.4966 1.0921 1.7554 0.0328  0.1233  -0.0706 1438 ALA B C     
5455 O  O     . ALA B 221 ? 1.6327 1.1967 1.8885 0.0322  0.1362  -0.0795 1438 ALA B O     
5456 C  CB    . ALA B 221 ? 1.1849 0.8283 1.4565 0.0496  0.1166  -0.0634 1438 ALA B CB    
5457 N  N     . SER B 222 ? 1.4336 1.0435 1.6804 0.0190  0.1111  -0.0731 1439 SER B N     
5458 C  CA    . SER B 222 ? 1.3066 0.8984 1.5390 0.0018  0.1106  -0.0845 1439 SER B CA    
5459 C  C     . SER B 222 ? 1.3688 0.9417 1.6097 -0.0008 0.1133  -0.0758 1439 SER B C     
5460 O  O     . SER B 222 ? 1.4505 0.9985 1.6837 -0.0127 0.1180  -0.0863 1439 SER B O     
5461 C  CB    . SER B 222 ? 1.2761 0.8942 1.4969 -0.0107 0.0958  -0.0880 1439 SER B CB    
5462 O  OG    . SER B 222 ? 1.2372 0.8777 1.4676 -0.0089 0.0856  -0.0720 1439 SER B OG    
5463 N  N     . GLY B 223 ? 1.3771 0.9610 1.6328 0.0095  0.1102  -0.0571 1440 GLY B N     
5464 C  CA    . GLY B 223 ? 1.1762 0.7473 1.4379 0.0058  0.1108  -0.0468 1440 GLY B CA    
5465 C  C     . GLY B 223 ? 1.2000 0.7875 1.4547 -0.0091 0.0995  -0.0464 1440 GLY B C     
5466 O  O     . GLY B 223 ? 1.1647 0.7405 1.4228 -0.0160 0.1008  -0.0403 1440 GLY B O     
5467 N  N     . ARG B 224 ? 1.3060 0.9219 1.5528 -0.0134 0.0887  -0.0509 1441 ARG B N     
5468 C  CA    . ARG B 224 ? 1.3436 0.9742 1.5835 -0.0286 0.0787  -0.0540 1441 ARG B CA    
5469 C  C     . ARG B 224 ? 1.4247 1.0882 1.6674 -0.0238 0.0675  -0.0411 1441 ARG B C     
5470 O  O     . ARG B 224 ? 1.4899 1.1705 1.7351 -0.0117 0.0643  -0.0357 1441 ARG B O     
5471 C  CB    . ARG B 224 ? 1.1760 0.8090 1.4008 -0.0409 0.0750  -0.0734 1441 ARG B CB    
5472 C  CG    . ARG B 224 ? 1.1879 0.7874 1.4055 -0.0481 0.0850  -0.0889 1441 ARG B CG    
5473 C  CD    . ARG B 224 ? 1.1725 0.7714 1.3745 -0.0659 0.0788  -0.1066 1441 ARG B CD    
5474 N  NE    . ARG B 224 ? 1.1872 0.7519 1.3860 -0.0766 0.0868  -0.1178 1441 ARG B NE    
5475 C  CZ    . ARG B 224 ? 1.1908 0.7413 1.3733 -0.0886 0.0864  -0.1369 1441 ARG B CZ    
5476 N  NH1   . ARG B 224 ? 1.3433 0.9111 1.5107 -0.0910 0.0788  -0.1459 1441 ARG B NH1   
5477 N  NH2   . ARG B 224 ? 1.2207 0.7389 1.4008 -0.0983 0.0936  -0.1469 1441 ARG B NH2   
5478 N  N     . ALA B 225 ? 1.3304 1.0025 1.5728 -0.0343 0.0618  -0.0372 1442 ALA B N     
5479 C  CA    . ALA B 225 ? 1.3168 1.0174 1.5602 -0.0317 0.0520  -0.0258 1442 ALA B CA    
5480 C  C     . ALA B 225 ? 1.1820 0.9056 1.4168 -0.0412 0.0419  -0.0358 1442 ALA B C     
5481 O  O     . ALA B 225 ? 1.4366 1.1537 1.6647 -0.0529 0.0414  -0.0502 1442 ALA B O     
5482 C  CB    . ALA B 225 ? 1.3082 1.0036 1.5575 -0.0359 0.0539  -0.0138 1442 ALA B CB    
5483 N  N     . ILE B 226 ? 1.0338 0.7839 1.2679 -0.0357 0.0335  -0.0279 1443 ILE B N     
5484 C  CA    . ILE B 226 ? 0.9659 0.7383 1.1927 -0.0431 0.0240  -0.0356 1443 ILE B CA    
5485 C  C     . ILE B 226 ? 0.8833 0.6790 1.1120 -0.0404 0.0168  -0.0236 1443 ILE B C     
5486 O  O     . ILE B 226 ? 0.8866 0.6853 1.1189 -0.0293 0.0174  -0.0107 1443 ILE B O     
5487 C  CB    . ILE B 226 ? 0.8722 0.6511 1.0919 -0.0381 0.0221  -0.0447 1443 ILE B CB    
5488 C  CG1   . ILE B 226 ? 1.0147 0.8119 1.2253 -0.0476 0.0130  -0.0540 1443 ILE B CG1   
5489 C  CG2   . ILE B 226 ? 0.7163 0.5080 0.9407 -0.0231 0.0205  -0.0344 1443 ILE B CG2   
5490 C  CD1   . ILE B 226 ? 1.0313 0.8367 1.2335 -0.0431 0.0110  -0.0617 1443 ILE B CD1   
5491 N  N     . GLN B 227 ? 0.7590 0.5697 0.9852 -0.0510 0.0102  -0.0280 1444 GLN B N     
5492 C  CA    . GLN B 227 ? 0.7656 0.5989 0.9925 -0.0503 0.0037  -0.0193 1444 GLN B CA    
5493 C  C     . GLN B 227 ? 0.9355 0.7889 1.1565 -0.0420 -0.0036 -0.0193 1444 GLN B C     
5494 O  O     . GLN B 227 ? 0.9106 0.7713 1.1259 -0.0457 -0.0079 -0.0298 1444 GLN B O     
5495 C  CB    . GLN B 227 ? 0.7727 0.6132 1.0015 -0.0649 0.0002  -0.0256 1444 GLN B CB    
5496 C  CG    . GLN B 227 ? 0.9266 0.7872 1.1589 -0.0666 -0.0039 -0.0172 1444 GLN B CG    
5497 C  CD    . GLN B 227 ? 1.2175 1.0932 1.4506 -0.0780 -0.0111 -0.0263 1444 GLN B CD    
5498 O  OE1   . GLN B 227 ? 1.4026 1.2750 1.6306 -0.0834 -0.0145 -0.0386 1444 GLN B OE1   
5499 N  NE2   . GLN B 227 ? 1.2293 1.1213 1.4684 -0.0813 -0.0133 -0.0203 1444 GLN B NE2   
5500 N  N     . GLY B 228 ? 1.0409 0.9033 1.2624 -0.0314 -0.0053 -0.0076 1445 GLY B N     
5501 C  CA    . GLY B 228 ? 0.9838 0.8628 1.2014 -0.0231 -0.0117 -0.0073 1445 GLY B CA    
5502 C  C     . GLY B 228 ? 0.9459 0.8470 1.1591 -0.0257 -0.0195 -0.0067 1445 GLY B C     
5503 O  O     . GLY B 228 ? 1.0343 0.9480 1.2436 -0.0232 -0.0249 -0.0114 1445 GLY B O     
5504 N  N     . ALA B 229 ? 0.8485 0.7542 1.0631 -0.0303 -0.0193 -0.0009 1446 ALA B N     
5505 C  CA    . ALA B 229 ? 0.8408 0.7667 1.0525 -0.0326 -0.0253 0.0000  1446 ALA B CA    
5506 C  C     . ALA B 229 ? 0.8793 0.8049 1.0962 -0.0400 -0.0215 0.0050  1446 ALA B C     
5507 O  O     . ALA B 229 ? 0.9038 0.8137 1.1253 -0.0421 -0.0145 0.0094  1446 ALA B O     
5508 C  CB    . ALA B 229 ? 0.5420 0.4797 0.7481 -0.0218 -0.0298 0.0075  1446 ALA B CB    
5509 N  N     . THR B 230 ? 0.9005 0.8435 1.1177 -0.0438 -0.0255 0.0046  1447 THR B N     
5510 C  CA    . THR B 230 ? 0.8397 0.7855 1.0638 -0.0501 -0.0212 0.0104  1447 THR B CA    
5511 C  C     . THR B 230 ? 0.7236 0.6878 0.9448 -0.0465 -0.0236 0.0158  1447 THR B C     
5512 O  O     . THR B 230 ? 0.8728 0.8505 1.0893 -0.0435 -0.0303 0.0117  1447 THR B O     
5513 C  CB    . THR B 230 ? 0.7644 0.7115 0.9983 -0.0635 -0.0218 0.0020  1447 THR B CB    
5514 O  OG1   . THR B 230 ? 0.8107 0.7672 1.0409 -0.0656 -0.0299 -0.0086 1447 THR B OG1   
5515 C  CG2   . THR B 230 ? 0.7338 0.6591 0.9729 -0.0692 -0.0153 0.0003  1447 THR B CG2   
5516 N  N     . SER B 231 ? 0.6784 0.6424 0.9037 -0.0483 -0.0171 0.0245  1448 SER B N     
5517 C  CA    . SER B 231 ? 0.6705 0.6492 0.8929 -0.0448 -0.0164 0.0308  1448 SER B CA    
5518 C  C     . SER B 231 ? 0.7552 0.7354 0.9904 -0.0536 -0.0087 0.0353  1448 SER B C     
5519 O  O     . SER B 231 ? 0.7882 0.7553 1.0241 -0.0536 -0.0002 0.0437  1448 SER B O     
5520 C  CB    . SER B 231 ? 0.6776 0.6511 0.8857 -0.0329 -0.0151 0.0403  1448 SER B CB    
5521 O  OG    . SER B 231 ? 0.8076 0.7893 1.0111 -0.0301 -0.0109 0.0480  1448 SER B OG    
5522 N  N     . HIS B 232 ? 0.6928 0.6896 0.9393 -0.0609 -0.0114 0.0303  1449 HIS B N     
5523 C  CA    . HIS B 232 ? 0.6938 0.6951 0.9579 -0.0714 -0.0054 0.0325  1449 HIS B CA    
5524 C  C     . HIS B 232 ? 0.7100 0.7243 0.9764 -0.0681 0.0011  0.0414  1449 HIS B C     
5525 O  O     . HIS B 232 ? 0.7257 0.7516 0.9830 -0.0602 -0.0021 0.0419  1449 HIS B O     
5526 C  CB    . HIS B 232 ? 0.6884 0.7013 0.9663 -0.0821 -0.0130 0.0217  1449 HIS B CB    
5527 C  CG    . HIS B 232 ? 0.8607 0.8641 1.1323 -0.0842 -0.0207 0.0109  1449 HIS B CG    
5528 N  ND1   . HIS B 232 ? 0.8734 0.8584 1.1484 -0.0914 -0.0183 0.0067  1449 HIS B ND1   
5529 C  CD2   . HIS B 232 ? 0.8493 0.8587 1.1117 -0.0805 -0.0299 0.0032  1449 HIS B CD2   
5530 C  CE1   . HIS B 232 ? 0.8902 0.8699 1.1569 -0.0914 -0.0253 -0.0033 1449 HIS B CE1   
5531 N  NE2   . HIS B 232 ? 0.9183 0.9130 1.1774 -0.0849 -0.0323 -0.0053 1449 HIS B NE2   
5532 N  N     . HIS B 233 ? 0.7814 0.7939 1.0612 -0.0750 0.0109  0.0479  1450 HIS B N     
5533 C  CA    . HIS B 233 ? 0.9147 0.9427 1.2025 -0.0745 0.0179  0.0547  1450 HIS B CA    
5534 C  C     . HIS B 233 ? 0.9240 0.9676 1.2383 -0.0872 0.0162  0.0497  1450 HIS B C     
5535 O  O     . HIS B 233 ? 1.0881 1.1252 1.4181 -0.0979 0.0213  0.0507  1450 HIS B O     
5536 C  CB    . HIS B 233 ? 1.0191 1.0356 1.3021 -0.0716 0.0319  0.0679  1450 HIS B CB    
5537 C  CG    . HIS B 233 ? 1.1309 1.1629 1.4218 -0.0708 0.0410  0.0747  1450 HIS B CG    
5538 N  ND1   . HIS B 233 ? 1.1252 1.1715 1.4071 -0.0621 0.0386  0.0741  1450 HIS B ND1   
5539 C  CD2   . HIS B 233 ? 1.1673 1.2030 1.4759 -0.0779 0.0531  0.0819  1450 HIS B CD2   
5540 C  CE1   . HIS B 233 ? 1.1252 1.1828 1.4179 -0.0630 0.0493  0.0807  1450 HIS B CE1   
5541 N  NE2   . HIS B 233 ? 1.1603 1.2125 1.4699 -0.0726 0.0584  0.0858  1450 HIS B NE2   
5542 N  N     . LEU B 234 ? 0.8068 0.8706 1.1264 -0.0862 0.0086  0.0444  1451 LEU B N     
5543 C  CA    . LEU B 234 ? 0.8196 0.9019 1.1650 -0.0970 0.0050  0.0401  1451 LEU B CA    
5544 C  C     . LEU B 234 ? 0.8244 0.9194 1.1882 -0.0991 0.0170  0.0495  1451 LEU B C     
5545 O  O     . LEU B 234 ? 0.5790 0.6897 0.9693 -0.1094 0.0157  0.0476  1451 LEU B O     
5546 C  CB    . LEU B 234 ? 0.8472 0.9462 1.1909 -0.0936 -0.0076 0.0323  1451 LEU B CB    
5547 C  CG    . LEU B 234 ? 0.8549 0.9432 1.1768 -0.0880 -0.0176 0.0246  1451 LEU B CG    
5548 C  CD1   . LEU B 234 ? 0.7131 0.8186 1.0331 -0.0834 -0.0276 0.0196  1451 LEU B CD1   
5549 C  CD2   . LEU B 234 ? 0.8320 0.9065 1.1557 -0.0979 -0.0229 0.0166  1451 LEU B CD2   
5550 N  N     . GLY B 235 ? 0.8296 0.9194 1.1796 -0.0892 0.0281  0.0592  1452 GLY B N     
5551 C  CA    . GLY B 235 ? 0.7286 0.8286 1.0939 -0.0904 0.0420  0.0688  1452 GLY B CA    
5552 C  C     . GLY B 235 ? 0.8842 1.0114 1.2685 -0.0905 0.0385  0.0663  1452 GLY B C     
5553 O  O     . GLY B 235 ? 0.8069 0.9421 1.1800 -0.0819 0.0307  0.0619  1452 GLY B O     
5554 N  N     . GLN B 236 ? 0.9218 1.0635 1.3372 -0.1005 0.0442  0.0691  1453 GLN B N     
5555 C  CA    . GLN B 236 ? 0.8922 1.0618 1.3314 -0.1011 0.0417  0.0681  1453 GLN B CA    
5556 C  C     . GLN B 236 ? 0.8267 1.0099 1.2899 -0.1136 0.0270  0.0589  1453 GLN B C     
5557 O  O     . GLN B 236 ? 0.7860 0.9940 1.2752 -0.1164 0.0240  0.0587  1453 GLN B O     
5558 C  CB    . GLN B 236 ? 0.9480 1.1284 1.4076 -0.1020 0.0595  0.0789  1453 GLN B CB    
5559 C  CG    . GLN B 236 ? 1.0106 1.1950 1.4550 -0.0873 0.0698  0.0852  1453 GLN B CG    
5560 C  CD    . GLN B 236 ? 1.1545 1.3463 1.6167 -0.0884 0.0898  0.0964  1453 GLN B CD    
5561 O  OE1   . GLN B 236 ? 1.1845 1.3789 1.6720 -0.1006 0.0959  0.0999  1453 GLN B OE1   
5562 N  NE2   . GLN B 236 ? 1.2564 1.4509 1.7053 -0.0758 0.1009  0.1018  1453 GLN B NE2   
5563 N  N     . ASN B 237 ? 0.7784 0.9456 1.2331 -0.1209 0.0176  0.0513  1454 ASN B N     
5564 C  CA    . ASN B 237 ? 0.8467 1.0238 1.3209 -0.1339 0.0036  0.0419  1454 ASN B CA    
5565 C  C     . ASN B 237 ? 0.8928 1.0867 1.3642 -0.1288 -0.0115 0.0351  1454 ASN B C     
5566 O  O     . ASN B 237 ? 1.0322 1.2494 1.5292 -0.1349 -0.0191 0.0330  1454 ASN B O     
5567 C  CB    . ASN B 237 ? 0.8844 1.0368 1.3460 -0.1418 -0.0013 0.0349  1454 ASN B CB    
5568 C  CG    . ASN B 237 ? 0.8570 0.9910 1.3219 -0.1469 0.0137  0.0423  1454 ASN B CG    
5569 O  OD1   . ASN B 237 ? 0.9078 1.0518 1.3962 -0.1521 0.0247  0.0502  1454 ASN B OD1   
5570 N  ND2   . ASN B 237 ? 0.7368 0.8437 1.1789 -0.1450 0.0148  0.0406  1454 ASN B ND2   
5571 N  N     . PHE B 238 ? 0.9479 1.1309 1.3893 -0.1173 -0.0160 0.0321  1455 PHE B N     
5572 C  CA    . PHE B 238 ? 0.9525 1.1485 1.3892 -0.1127 -0.0301 0.0258  1455 PHE B CA    
5573 C  C     . PHE B 238 ? 0.8755 1.0931 1.3228 -0.1034 -0.0265 0.0317  1455 PHE B C     
5574 O  O     . PHE B 238 ? 0.7356 0.9717 1.1943 -0.1034 -0.0376 0.0284  1455 PHE B O     
5575 C  CB    . PHE B 238 ? 0.9045 1.0815 1.3078 -0.1046 -0.0355 0.0206  1455 PHE B CB    
5576 C  CG    . PHE B 238 ? 0.8604 1.0235 1.2562 -0.1135 -0.0449 0.0113  1455 PHE B CG    
5577 C  CD1   . PHE B 238 ? 0.9361 1.0761 1.3222 -0.1169 -0.0385 0.0112  1455 PHE B CD1   
5578 C  CD2   . PHE B 238 ? 0.8638 1.0357 1.2612 -0.1181 -0.0599 0.0027  1455 PHE B CD2   
5579 C  CE1   . PHE B 238 ? 1.0112 1.1368 1.3899 -0.1246 -0.0460 0.0020  1455 PHE B CE1   
5580 C  CE2   . PHE B 238 ? 0.9456 1.1030 1.3334 -0.1262 -0.0678 -0.0067 1455 PHE B CE2   
5581 C  CZ    . PHE B 238 ? 0.9954 1.1293 1.3742 -0.1294 -0.0604 -0.0074 1455 PHE B CZ    
5582 N  N     . SER B 239 ? 0.9016 1.1158 1.3435 -0.0948 -0.0113 0.0404  1456 SER B N     
5583 C  CA    . SER B 239 ? 0.8678 1.1018 1.3228 -0.0867 -0.0052 0.0462  1456 SER B CA    
5584 C  C     . SER B 239 ? 0.8835 1.1432 1.3785 -0.0964 -0.0068 0.0479  1456 SER B C     
5585 O  O     . SER B 239 ? 0.9488 1.2295 1.4587 -0.0933 -0.0145 0.0470  1456 SER B O     
5586 C  CB    . SER B 239 ? 0.8664 1.0905 1.3089 -0.0778 0.0132  0.0552  1456 SER B CB    
5587 O  OG    . SER B 239 ? 0.8971 1.1119 1.3478 -0.0861 0.0243  0.0604  1456 SER B OG    
5588 N  N     . ARG B 240 ? 0.7294 0.9878 1.2437 -0.1085 -0.0004 0.0505  1457 ARG B N     
5589 C  CA    . ARG B 240 ? 0.6642 0.9480 1.2196 -0.1191 -0.0025 0.0520  1457 ARG B CA    
5590 C  C     . ARG B 240 ? 0.7310 1.0268 1.2956 -0.1267 -0.0240 0.0425  1457 ARG B C     
5591 O  O     . ARG B 240 ? 0.8775 1.1999 1.4702 -0.1284 -0.0307 0.0434  1457 ARG B O     
5592 C  CB    . ARG B 240 ? 0.6609 0.9380 1.2339 -0.1320 0.0082  0.0559  1457 ARG B CB    
5593 C  CG    . ARG B 240 ? 0.7703 1.0371 1.3363 -0.1252 0.0305  0.0669  1457 ARG B CG    
5594 C  CD    . ARG B 240 ? 0.8720 1.1322 1.4571 -0.1382 0.0419  0.0718  1457 ARG B CD    
5595 N  NE    . ARG B 240 ? 1.0240 1.2863 1.6154 -0.1325 0.0640  0.0841  1457 ARG B NE    
5596 C  CZ    . ARG B 240 ? 1.1043 1.3432 1.6753 -0.1297 0.0792  0.0912  1457 ARG B CZ    
5597 N  NH1   . ARG B 240 ? 1.2270 1.4391 1.7724 -0.1319 0.0745  0.0874  1457 ARG B NH1   
5598 N  NH2   . ARG B 240 ? 1.0035 1.2456 1.5795 -0.1242 0.0996  0.1025  1457 ARG B NH2   
5599 N  N     . MET B 241 ? 0.9108 1.1872 1.4509 -0.1303 -0.0351 0.0336  1458 MET B N     
5600 C  CA    . MET B 241 ? 0.9011 1.1867 1.4449 -0.1370 -0.0555 0.0244  1458 MET B CA    
5601 C  C     . MET B 241 ? 0.8685 1.1706 1.4089 -0.1253 -0.0639 0.0248  1458 MET B C     
5602 O  O     . MET B 241 ? 0.8659 1.1904 1.4277 -0.1293 -0.0764 0.0231  1458 MET B O     
5603 C  CB    . MET B 241 ? 0.8423 1.1014 1.3566 -0.1414 -0.0633 0.0148  1458 MET B CB    
5604 N  N     . PHE B 242 ? 0.7749 1.0657 1.2888 -0.1108 -0.0577 0.0271  1459 PHE B N     
5605 C  CA    . PHE B 242 ? 0.7836 1.0842 1.2890 -0.0995 -0.0658 0.0265  1459 PHE B CA    
5606 C  C     . PHE B 242 ? 0.8950 1.2101 1.4128 -0.0877 -0.0537 0.0354  1459 PHE B C     
5607 O  O     . PHE B 242 ? 0.9226 1.2417 1.4302 -0.0762 -0.0570 0.0358  1459 PHE B O     
5608 C  CB    . PHE B 242 ? 0.7252 1.0023 1.1914 -0.0922 -0.0695 0.0211  1459 PHE B CB    
5609 C  CG    . PHE B 242 ? 0.7748 1.0422 1.2288 -0.1011 -0.0842 0.0115  1459 PHE B CG    
5610 C  CD1   . PHE B 242 ? 0.6543 0.9309 1.1045 -0.1001 -0.0997 0.0069  1459 PHE B CD1   
5611 C  CD2   . PHE B 242 ? 0.9002 1.1484 1.3459 -0.1105 -0.0820 0.0071  1459 PHE B CD2   
5612 C  CE1   . PHE B 242 ? 0.6125 0.8791 1.0488 -0.1082 -0.1126 -0.0022 1459 PHE B CE1   
5613 C  CE2   . PHE B 242 ? 0.9320 1.1698 1.3651 -0.1185 -0.0946 -0.0025 1459 PHE B CE2   
5614 C  CZ    . PHE B 242 ? 0.8170 1.0641 1.2446 -0.1174 -0.1097 -0.0074 1459 PHE B CZ    
5615 N  N     . ASP B 243 ? 0.7734 1.0956 1.3129 -0.0904 -0.0389 0.0425  1460 ASP B N     
5616 C  CA    . ASP B 243 ? 0.7737 1.1090 1.3262 -0.0797 -0.0247 0.0511  1460 ASP B CA    
5617 C  C     . ASP B 243 ? 0.9748 1.2933 1.4932 -0.0643 -0.0180 0.0517  1460 ASP B C     
5618 O  O     . ASP B 243 ? 1.0254 1.3530 1.5430 -0.0533 -0.0193 0.0528  1460 ASP B O     
5619 C  CB    . ASP B 243 ? 0.8213 1.1877 1.4074 -0.0787 -0.0325 0.0534  1460 ASP B CB    
5620 C  CG    . ASP B 243 ? 1.1389 1.5241 1.7554 -0.0747 -0.0153 0.0631  1460 ASP B CG    
5621 O  OD1   . ASP B 243 ? 1.2473 1.6297 1.8757 -0.0820 -0.0022 0.0673  1460 ASP B OD1   
5622 O  OD2   . ASP B 243 ? 1.2218 1.6238 1.8508 -0.0640 -0.0140 0.0668  1460 ASP B OD2   
5623 N  N     . ILE B 244 ? 0.9741 1.2672 1.4641 -0.0639 -0.0117 0.0506  1461 ILE B N     
5624 C  CA    . ILE B 244 ? 1.0199 1.2964 1.4788 -0.0506 -0.0034 0.0519  1461 ILE B CA    
5625 C  C     . ILE B 244 ? 0.9522 1.2280 1.4168 -0.0475 0.0170  0.0605  1461 ILE B C     
5626 O  O     . ILE B 244 ? 0.9967 1.2586 1.4547 -0.0529 0.0251  0.0632  1461 ILE B O     
5627 C  CB    . ILE B 244 ? 1.0249 1.2758 1.4499 -0.0508 -0.0093 0.0462  1461 ILE B CB    
5628 C  CG1   . ILE B 244 ? 0.9580 1.2100 1.3826 -0.0580 -0.0278 0.0379  1461 ILE B CG1   
5629 C  CG2   . ILE B 244 ? 0.9569 1.1958 1.3527 -0.0372 -0.0073 0.0454  1461 ILE B CG2   
5630 C  CD1   . ILE B 244 ? 0.7777 1.0079 1.1828 -0.0643 -0.0318 0.0329  1461 ILE B CD1   
5631 N  N     . VAL B 245 ? 0.8749 1.1658 1.3527 -0.0387 0.0258  0.0653  1462 VAL B N     
5632 C  CA    . VAL B 245 ? 0.8918 1.1857 1.3790 -0.0355 0.0465  0.0739  1462 VAL B CA    
5633 C  C     . VAL B 245 ? 0.8910 1.1818 1.3611 -0.0197 0.0558  0.0755  1462 VAL B C     
5634 O  O     . VAL B 245 ? 0.8723 1.1659 1.3352 -0.0123 0.0462  0.0710  1462 VAL B O     
5635 C  CB    . VAL B 245 ? 0.7229 1.0440 1.2569 -0.0438 0.0507  0.0791  1462 VAL B CB    
5636 N  N     . TYR B 246 ? 0.8409 1.1244 1.3033 -0.0148 0.0753  0.0820  1463 TYR B N     
5637 C  CA    . TYR B 246 ? 0.8615 1.1417 1.3091 -0.0005 0.0877  0.0839  1463 TYR B CA    
5638 C  C     . TYR B 246 ? 1.0326 1.3262 1.5049 0.0007  0.1086  0.0930  1463 TYR B C     
5639 O  O     . TYR B 246 ? 1.0797 1.3778 1.5707 -0.0093 0.1157  0.0983  1463 TYR B O     
5640 C  CB    . TYR B 246 ? 0.8788 1.1299 1.2793 0.0066  0.0910  0.0818  1463 TYR B CB    
5641 C  CG    . TYR B 246 ? 1.0179 1.2516 1.4028 0.0006  0.0991  0.0863  1463 TYR B CG    
5642 C  CD1   . TYR B 246 ? 1.0494 1.2740 1.4215 0.0058  0.1193  0.0936  1463 TYR B CD1   
5643 C  CD2   . TYR B 246 ? 0.9898 1.2146 1.3708 -0.0094 0.0868  0.0835  1463 TYR B CD2   
5644 C  CE1   . TYR B 246 ? 1.0433 1.2510 1.3997 0.0011  0.1264  0.0988  1463 TYR B CE1   
5645 C  CE2   . TYR B 246 ? 1.0956 1.3034 1.4625 -0.0140 0.0941  0.0882  1463 TYR B CE2   
5646 C  CZ    . TYR B 246 ? 1.1401 1.3395 1.4948 -0.0087 0.1136  0.0963  1463 TYR B CZ    
5647 O  OH    . TYR B 246 ? 1.1858 1.3675 1.5260 -0.0130 0.1207  0.1022  1463 TYR B OH    
5648 N  N     . GLU B 247 ? 1.1266 1.4258 1.5992 0.0131  0.1196  0.0946  1464 GLU B N     
5649 C  CA    . GLU B 247 ? 1.1123 1.4233 1.6062 0.0164  0.1421  0.1032  1464 GLU B CA    
5650 C  C     . GLU B 247 ? 1.0925 1.3796 1.5535 0.0187  0.1593  0.1075  1464 GLU B C     
5651 O  O     . GLU B 247 ? 1.0913 1.3554 1.5101 0.0271  0.1594  0.1037  1464 GLU B O     
5652 C  CB    . GLU B 247 ? 1.2353 1.5570 1.7367 0.0304  0.1491  0.1029  1464 GLU B CB    
5653 C  CG    . GLU B 247 ? 1.3841 1.7339 1.9317 0.0314  0.1640  0.1108  1464 GLU B CG    
5654 C  CD    . GLU B 247 ? 1.4653 1.8228 2.0181 0.0471  0.1729  0.1108  1464 GLU B CD    
5655 O  OE1   . GLU B 247 ? 1.4054 1.7518 1.9345 0.0553  0.1620  0.1037  1464 GLU B OE1   
5656 O  OE2   . GLU B 247 ? 1.4976 1.8720 2.0795 0.0512  0.1917  0.1180  1464 GLU B OE2   
5657 N  N     . HIS B 248 ? 1.1571 1.4488 1.6363 0.0109  0.1731  0.1157  1465 HIS B N     
5658 C  CA    . HIS B 248 ? 1.2974 1.5665 1.7448 0.0142  0.1912  0.1214  1465 HIS B CA    
5659 C  C     . HIS B 248 ? 1.2668 1.5345 1.7023 0.0289  0.2100  0.1234  1465 HIS B C     
5660 O  O     . HIS B 248 ? 1.2175 1.5081 1.6884 0.0317  0.2207  0.1272  1465 HIS B O     
5661 C  CB    . HIS B 248 ? 1.4066 1.6804 1.8774 0.0025  0.2038  0.1307  1465 HIS B CB    
5662 C  CG    . HIS B 248 ? 1.5103 1.7561 1.9433 0.0029  0.2152  0.1360  1465 HIS B CG    
5663 N  ND1   . HIS B 248 ? 1.5489 1.7748 1.9402 0.0156  0.2279  0.1373  1465 HIS B ND1   
5664 C  CD2   . HIS B 248 ? 1.5477 1.7814 1.9774 -0.0076 0.2155  0.1406  1465 HIS B CD2   
5665 C  CE1   . HIS B 248 ? 1.5866 1.7901 1.9502 0.0132  0.2347  0.1430  1465 HIS B CE1   
5666 N  NE2   . HIS B 248 ? 1.5750 1.7826 1.9618 -0.0005 0.2278  0.1454  1465 HIS B NE2   
5667 N  N     . PRO B 249 ? 1.2055 1.4473 1.5927 0.0386  0.2143  0.1208  1466 PRO B N     
5668 C  CA    . PRO B 249 ? 1.1195 1.3577 1.4923 0.0530  0.2318  0.1211  1466 PRO B CA    
5669 C  C     . PRO B 249 ? 1.0087 1.2562 1.4011 0.0545  0.2594  0.1315  1466 PRO B C     
5670 O  O     . PRO B 249 ? 1.0205 1.2828 1.4334 0.0628  0.2717  0.1325  1466 PRO B O     
5671 C  CB    . PRO B 249 ? 1.0841 1.2899 1.3983 0.0598  0.2290  0.1163  1466 PRO B CB    
5672 C  CG    . PRO B 249 ? 1.0813 1.2819 1.3887 0.0522  0.2026  0.1096  1466 PRO B CG    
5673 C  CD    . PRO B 249 ? 1.1655 1.3819 1.5104 0.0379  0.1993  0.1152  1466 PRO B CD    
5674 N  N     . GLU B 250 ? 1.1190 1.3586 1.5078 0.0467  0.2702  0.1398  1467 GLU B N     
5675 C  CA    . GLU B 250 ? 1.2014 1.4485 1.6075 0.0480  0.2983  0.1506  1467 GLU B CA    
5676 C  C     . GLU B 250 ? 1.3253 1.6082 1.7955 0.0414  0.3010  0.1546  1467 GLU B C     
5677 O  O     . GLU B 250 ? 1.3131 1.6126 1.8050 0.0503  0.3122  0.1552  1467 GLU B O     
5678 C  CB    . GLU B 250 ? 1.1710 1.3996 1.5575 0.0405  0.3080  0.1592  1467 GLU B CB    
5679 N  N     . THR B 251 ? 1.4231 1.7182 1.9248 0.0260  0.2910  0.1574  1468 THR B N     
5680 C  CA    . THR B 251 ? 1.3563 1.6865 1.9199 0.0178  0.2884  0.1600  1468 THR B CA    
5681 C  C     . THR B 251 ? 1.2482 1.5867 1.8216 0.0117  0.2573  0.1502  1468 THR B C     
5682 O  O     . THR B 251 ? 1.2982 1.6230 1.8560 0.0022  0.2419  0.1469  1468 THR B O     
5683 C  CB    . THR B 251 ? 1.3526 1.6907 1.9467 0.0036  0.3003  0.1699  1468 THR B CB    
5684 N  N     . LYS B 252 ? 1.1734 1.5357 1.7760 0.0166  0.2488  0.1466  1469 LYS B N     
5685 C  CA    . LYS B 252 ? 1.1626 1.5287 1.7647 0.0141  0.2200  0.1369  1469 LYS B CA    
5686 C  C     . LYS B 252 ? 1.1142 1.4915 1.7434 -0.0037 0.2021  0.1357  1469 LYS B C     
5687 O  O     . LYS B 252 ? 1.0419 1.4404 1.7002 -0.0080 0.1836  0.1316  1469 LYS B O     
5688 C  CB    . LYS B 252 ? 1.1570 1.5457 1.7844 0.0241  0.2159  0.1346  1469 LYS B CB    
5689 N  N     . GLU B 253 ? 1.1413 1.5030 1.7595 -0.0139 0.2072  0.1392  1470 GLU B N     
5690 C  CA    . GLU B 253 ? 1.0647 1.4326 1.7046 -0.0310 0.1909  0.1371  1470 GLU B CA    
5691 C  C     . GLU B 253 ? 1.0786 1.4318 1.6887 -0.0312 0.1658  0.1263  1470 GLU B C     
5692 O  O     . GLU B 253 ? 1.1650 1.4928 1.7293 -0.0225 0.1653  0.1229  1470 GLU B O     
5693 C  CB    . GLU B 253 ? 0.9904 1.3418 1.6237 -0.0409 0.2045  0.1440  1470 GLU B CB    
5694 N  N     . LYS B 254 ? 0.9990 1.3686 1.6348 -0.0409 0.1448  0.1207  1471 LYS B N     
5695 C  CA    . LYS B 254 ? 0.8917 1.2473 1.4999 -0.0417 0.1220  0.1107  1471 LYS B CA    
5696 C  C     . LYS B 254 ? 1.0486 1.3745 1.6238 -0.0475 0.1228  0.1099  1471 LYS B C     
5697 O  O     . LYS B 254 ? 1.1873 1.5114 1.7775 -0.0592 0.1294  0.1144  1471 LYS B O     
5698 C  CB    . LYS B 254 ? 0.5305 0.9083 1.1713 -0.0520 0.1001  0.1052  1471 LYS B CB    
5699 N  N     . GLU B 255 ? 0.9838 1.2862 1.5150 -0.0389 0.1171  0.1050  1472 GLU B N     
5700 C  CA    . GLU B 255 ? 0.9267 1.2009 1.4250 -0.0421 0.1172  0.1047  1472 GLU B CA    
5701 C  C     . GLU B 255 ? 0.8541 1.1200 1.3379 -0.0458 0.0943  0.0946  1472 GLU B C     
5702 O  O     . GLU B 255 ? 0.7298 0.9991 1.2037 -0.0385 0.0827  0.0883  1472 GLU B O     
5703 C  CB    . GLU B 255 ? 0.8977 1.1504 1.3555 -0.0290 0.1309  0.1081  1472 GLU B CB    
5704 C  CG    . GLU B 255 ? 1.0451 1.2922 1.5044 -0.0295 0.1547  0.1192  1472 GLU B CG    
5705 C  CD    . GLU B 255 ? 1.1822 1.4085 1.6282 -0.0383 0.1561  0.1227  1472 GLU B CD    
5706 O  OE1   . GLU B 255 ? 1.1656 1.3819 1.6041 -0.0375 0.1754  0.1323  1472 GLU B OE1   
5707 O  OE2   . GLU B 255 ? 1.2683 1.4873 1.7105 -0.0455 0.1389  0.1163  1472 GLU B OE2   
5708 N  N     . TYR B 256 ? 0.8861 1.1409 1.3695 -0.0572 0.0887  0.0933  1473 TYR B N     
5709 C  CA    . TYR B 256 ? 0.9068 1.1522 1.3762 -0.0612 0.0688  0.0838  1473 TYR B CA    
5710 C  C     . TYR B 256 ? 0.9028 1.1201 1.3291 -0.0537 0.0691  0.0828  1473 TYR B C     
5711 O  O     . TYR B 256 ? 0.8791 1.0813 1.2897 -0.0509 0.0833  0.0899  1473 TYR B O     
5712 C  CB    . TYR B 256 ? 0.9505 1.1989 1.4438 -0.0777 0.0618  0.0816  1473 TYR B CB    
5713 C  CG    . TYR B 256 ? 0.9641 1.2424 1.4996 -0.0851 0.0563  0.0808  1473 TYR B CG    
5714 C  CD1   . TYR B 256 ? 0.9025 1.1945 1.4438 -0.0843 0.0380  0.0731  1473 TYR B CD1   
5715 C  CD2   . TYR B 256 ? 0.9861 1.2797 1.5564 -0.0925 0.0694  0.0885  1473 TYR B CD2   
5716 C  CE1   . TYR B 256 ? 0.9492 1.2699 1.5292 -0.0906 0.0313  0.0730  1473 TYR B CE1   
5717 C  CE2   . TYR B 256 ? 0.8629 1.1865 1.4751 -0.0994 0.0631  0.0880  1473 TYR B CE2   
5718 C  CZ    . TYR B 256 ? 0.9161 1.2533 1.5326 -0.0982 0.0432  0.0802  1473 TYR B CZ    
5719 O  OH    . TYR B 256 ? 0.9015 1.2692 1.5588 -0.1044 0.0350  0.0801  1473 TYR B OH    
5720 N  N     . VAL B 257 ? 0.8944 1.1059 1.3018 -0.0496 0.0537  0.0745  1474 VAL B N     
5721 C  CA    . VAL B 257 ? 0.9939 1.1814 1.3632 -0.0426 0.0519  0.0729  1474 VAL B CA    
5722 C  C     . VAL B 257 ? 0.9678 1.1385 1.3318 -0.0516 0.0480  0.0720  1474 VAL B C     
5723 O  O     . VAL B 257 ? 1.0468 1.2236 1.4339 -0.0636 0.0432  0.0698  1474 VAL B O     
5724 C  CB    . VAL B 257 ? 0.9594 1.1471 1.3124 -0.0350 0.0380  0.0648  1474 VAL B CB    
5725 C  CG1   . VAL B 257 ? 0.9410 1.1362 1.2889 -0.0233 0.0455  0.0669  1474 VAL B CG1   
5726 C  CG2   . VAL B 257 ? 0.8992 1.1012 1.2728 -0.0427 0.0226  0.0577  1474 VAL B CG2   
5727 N  N     . PHE B 258 ? 0.6597 0.8087 0.9929 -0.0456 0.0495  0.0734  1475 PHE B N     
5728 C  CA    . PHE B 258 ? 0.7998 0.9306 1.1250 -0.0516 0.0460  0.0728  1475 PHE B CA    
5729 C  C     . PHE B 258 ? 0.8022 0.9252 1.1089 -0.0481 0.0305  0.0639  1475 PHE B C     
5730 O  O     . PHE B 258 ? 0.7379 0.8569 1.0226 -0.0377 0.0279  0.0626  1475 PHE B O     
5731 C  CB    . PHE B 258 ? 0.9134 1.0259 1.2199 -0.0474 0.0596  0.0827  1475 PHE B CB    
5732 C  CG    . PHE B 258 ? 1.0314 1.1490 1.3581 -0.0533 0.0759  0.0919  1475 PHE B CG    
5733 C  CD1   . PHE B 258 ? 1.0637 1.1734 1.4052 -0.0645 0.0798  0.0951  1475 PHE B CD1   
5734 C  CD2   . PHE B 258 ? 1.0622 1.1925 1.3946 -0.0480 0.0882  0.0974  1475 PHE B CD2   
5735 C  CE1   . PHE B 258 ? 0.9857 1.1003 1.3478 -0.0707 0.0955  0.1040  1475 PHE B CE1   
5736 C  CE2   . PHE B 258 ? 0.9805 1.1165 1.3335 -0.0535 0.1046  0.1064  1475 PHE B CE2   
5737 C  CZ    . PHE B 258 ? 0.9413 1.0697 1.3095 -0.0652 0.1081  0.1099  1475 PHE B CZ    
5738 N  N     . GLN B 259 ? 0.7346 0.8558 1.0511 -0.0571 0.0205  0.0573  1476 GLN B N     
5739 C  CA    . GLN B 259 ? 0.6502 0.7665 0.9536 -0.0551 0.0064  0.0483  1476 GLN B CA    
5740 C  C     . GLN B 259 ? 0.8621 0.9573 1.1535 -0.0577 0.0043  0.0471  1476 GLN B C     
5741 O  O     . GLN B 259 ? 0.9764 1.0637 1.2784 -0.0659 0.0098  0.0499  1476 GLN B O     
5742 C  CB    . GLN B 259 ? 0.5597 0.6919 0.8819 -0.0624 -0.0050 0.0402  1476 GLN B CB    
5743 C  CG    . GLN B 259 ? 0.6347 0.7889 0.9708 -0.0592 -0.0051 0.0411  1476 GLN B CG    
5744 C  CD    . GLN B 259 ? 0.8057 0.9759 1.1622 -0.0675 -0.0171 0.0344  1476 GLN B CD    
5745 O  OE1   . GLN B 259 ? 0.9531 1.1351 1.3354 -0.0770 -0.0155 0.0358  1476 GLN B OE1   
5746 N  NE2   . GLN B 259 ? 0.7156 0.8862 1.0607 -0.0643 -0.0293 0.0273  1476 GLN B NE2   
5747 N  N     . ASN B 260 ? 0.9362 1.0228 1.2071 -0.0506 -0.0035 0.0428  1477 ASN B N     
5748 C  CA    . ASN B 260 ? 0.8609 0.9302 1.1213 -0.0515 -0.0083 0.0394  1477 ASN B CA    
5749 C  C     . ASN B 260 ? 0.7935 0.8667 1.0511 -0.0518 -0.0209 0.0291  1477 ASN B C     
5750 O  O     . ASN B 260 ? 0.8704 0.9559 1.1257 -0.0474 -0.0261 0.0262  1477 ASN B O     
5751 C  CB    . ASN B 260 ? 0.7304 0.7848 0.9675 -0.0411 -0.0056 0.0448  1477 ASN B CB    
5752 C  CG    . ASN B 260 ? 0.8009 0.8497 1.0335 -0.0381 0.0070  0.0560  1477 ASN B CG    
5753 O  OD1   . ASN B 260 ? 0.8811 0.9319 1.1292 -0.0452 0.0157  0.0606  1477 ASN B OD1   
5754 N  ND2   . ASN B 260 ? 0.6410 0.6823 0.8513 -0.0277 0.0080  0.0607  1477 ASN B ND2   
5755 N  N     . SER B 261 ? 0.6652 0.7264 0.9220 -0.0568 -0.0251 0.0238  1478 SER B N     
5756 C  CA    . SER B 261 ? 0.6699 0.7296 0.9179 -0.0549 -0.0350 0.0152  1478 SER B CA    
5757 C  C     . SER B 261 ? 0.8094 0.8494 1.0474 -0.0531 -0.0341 0.0145  1478 SER B C     
5758 O  O     . SER B 261 ? 0.9656 0.9933 1.2074 -0.0565 -0.0275 0.0186  1478 SER B O     
5759 C  CB    . SER B 261 ? 0.6371 0.7067 0.8966 -0.0639 -0.0430 0.0066  1478 SER B CB    
5760 O  OG    . SER B 261 ? 0.7505 0.8128 1.0212 -0.0747 -0.0414 0.0039  1478 SER B OG    
5761 N  N     . TRP B 262 ? 0.8478 0.8850 1.0738 -0.0471 -0.0402 0.0101  1479 TRP B N     
5762 C  CA    . TRP B 262 ? 0.8252 0.8459 1.0428 -0.0432 -0.0396 0.0099  1479 TRP B CA    
5763 C  C     . TRP B 262 ? 0.9285 0.9497 1.1406 -0.0421 -0.0470 0.0012  1479 TRP B C     
5764 O  O     . TRP B 262 ? 1.0753 1.1088 1.2854 -0.0408 -0.0526 -0.0023 1479 TRP B O     
5765 C  CB    . TRP B 262 ? 0.7835 0.7993 0.9898 -0.0330 -0.0365 0.0187  1479 TRP B CB    
5766 C  CG    . TRP B 262 ? 0.8907 0.9191 1.0906 -0.0271 -0.0375 0.0221  1479 TRP B CG    
5767 C  CD1   . TRP B 262 ? 0.7425 0.7776 0.9451 -0.0275 -0.0315 0.0281  1479 TRP B CD1   
5768 C  CD2   . TRP B 262 ? 1.0590 1.0936 1.2487 -0.0199 -0.0439 0.0194  1479 TRP B CD2   
5769 N  NE1   . TRP B 262 ? 0.8239 0.8679 1.0173 -0.0205 -0.0336 0.0289  1479 TRP B NE1   
5770 C  CE2   . TRP B 262 ? 0.9481 0.9917 1.1336 -0.0162 -0.0417 0.0235  1479 TRP B CE2   
5771 C  CE3   . TRP B 262 ? 1.0668 1.0996 1.2512 -0.0165 -0.0506 0.0140  1479 TRP B CE3   
5772 C  CZ2   . TRP B 262 ? 0.7200 0.7695 0.8953 -0.0096 -0.0465 0.0216  1479 TRP B CZ2   
5773 C  CZ3   . TRP B 262 ? 0.9509 0.9908 1.1270 -0.0105 -0.0554 0.0128  1479 TRP B CZ3   
5774 C  CH2   . TRP B 262 ? 0.7766 0.8242 0.9479 -0.0072 -0.0537 0.0163  1479 TRP B CH2   
5775 N  N     . GLY B 263 ? 0.8834 0.8902 1.0932 -0.0420 -0.0461 -0.0019 1480 GLY B N     
5776 C  CA    . GLY B 263 ? 0.7885 0.7941 0.9940 -0.0424 -0.0511 -0.0108 1480 GLY B CA    
5777 C  C     . GLY B 263 ? 0.8370 0.8278 1.0384 -0.0372 -0.0485 -0.0109 1480 GLY B C     
5778 O  O     . GLY B 263 ? 0.9683 0.9468 1.1722 -0.0359 -0.0428 -0.0057 1480 GLY B O     
5779 N  N     . ILE B 264 ? 0.7282 0.7204 0.9242 -0.0335 -0.0521 -0.0160 1481 ILE B N     
5780 C  CA    . ILE B 264 ? 0.6752 0.6541 0.8703 -0.0293 -0.0490 -0.0178 1481 ILE B CA    
5781 C  C     . ILE B 264 ? 0.7606 0.7413 0.9511 -0.0303 -0.0519 -0.0267 1481 ILE B C     
5782 O  O     . ILE B 264 ? 0.8759 0.8693 1.0625 -0.0294 -0.0571 -0.0282 1481 ILE B O     
5783 C  CB    . ILE B 264 ? 0.5828 0.5607 0.7773 -0.0189 -0.0486 -0.0093 1481 ILE B CB    
5784 C  CG1   . ILE B 264 ? 0.6165 0.5785 0.8146 -0.0151 -0.0434 -0.0086 1481 ILE B CG1   
5785 C  CG2   . ILE B 264 ? 0.6258 0.6160 0.8161 -0.0130 -0.0545 -0.0100 1481 ILE B CG2   
5786 C  CD1   . ILE B 264 ? 0.5106 0.4712 0.7097 -0.0046 -0.0438 0.0009  1481 ILE B CD1   
5787 N  N     . THR B 265 ? 0.7152 0.6819 0.9052 -0.0320 -0.0476 -0.0325 1482 THR B N     
5788 C  CA    . THR B 265 ? 0.7883 0.7536 0.9716 -0.0348 -0.0486 -0.0420 1482 THR B CA    
5789 C  C     . THR B 265 ? 0.7793 0.7362 0.9629 -0.0275 -0.0438 -0.0432 1482 THR B C     
5790 O  O     . THR B 265 ? 0.6908 0.6440 0.8811 -0.0202 -0.0409 -0.0366 1482 THR B O     
5791 C  CB    . THR B 265 ? 0.8441 0.8001 1.0244 -0.0454 -0.0477 -0.0503 1482 THR B CB    
5792 O  OG1   . THR B 265 ? 0.9406 0.8769 1.1230 -0.0458 -0.0401 -0.0527 1482 THR B OG1   
5793 C  CG2   . THR B 265 ? 0.7118 0.6762 0.8973 -0.0525 -0.0515 -0.0476 1482 THR B CG2   
5794 N  N     . THR B 266 ? 0.8241 0.7786 1.0003 -0.0294 -0.0430 -0.0513 1483 THR B N     
5795 C  CA    . THR B 266 ? 0.9108 0.8583 1.0887 -0.0228 -0.0371 -0.0529 1483 THR B CA    
5796 C  C     . THR B 266 ? 0.8294 0.7570 1.0103 -0.0226 -0.0285 -0.0556 1483 THR B C     
5797 O  O     . THR B 266 ? 0.9112 0.8320 1.0961 -0.0163 -0.0221 -0.0564 1483 THR B O     
5798 C  CB    . THR B 266 ? 0.8583 0.8087 1.0261 -0.0246 -0.0375 -0.0601 1483 THR B CB    
5799 O  OG1   . THR B 266 ? 0.9137 0.8608 1.0701 -0.0342 -0.0403 -0.0675 1483 THR B OG1   
5800 C  CG2   . THR B 266 ? 0.8868 0.8546 1.0556 -0.0209 -0.0436 -0.0554 1483 THR B CG2   
5801 N  N     . ARG B 267 ? 0.8096 0.7282 0.9905 -0.0293 -0.0278 -0.0567 1484 ARG B N     
5802 C  CA    . ARG B 267 ? 0.9039 0.8022 1.0891 -0.0288 -0.0195 -0.0578 1484 ARG B CA    
5803 C  C     . ARG B 267 ? 0.8881 0.7848 1.0851 -0.0173 -0.0157 -0.0483 1484 ARG B C     
5804 O  O     . ARG B 267 ? 0.9508 0.8318 1.1521 -0.0131 -0.0074 -0.0498 1484 ARG B O     
5805 C  CB    . ARG B 267 ? 0.8974 0.7895 1.0835 -0.0380 -0.0206 -0.0580 1484 ARG B CB    
5806 C  CG    . ARG B 267 ? 0.9501 0.8277 1.1455 -0.0352 -0.0142 -0.0514 1484 ARG B CG    
5807 C  CD    . ARG B 267 ? 1.0038 0.8795 1.2014 -0.0451 -0.0159 -0.0505 1484 ARG B CD    
5808 N  NE    . ARG B 267 ? 1.1107 0.9832 1.3006 -0.0569 -0.0185 -0.0625 1484 ARG B NE    
5809 C  CZ    . ARG B 267 ? 1.2054 1.0689 1.3977 -0.0676 -0.0180 -0.0661 1484 ARG B CZ    
5810 N  NH1   . ARG B 267 ? 1.1821 1.0384 1.3846 -0.0679 -0.0136 -0.0579 1484 ARG B NH1   
5811 N  NH2   . ARG B 267 ? 1.3055 1.1671 1.4899 -0.0784 -0.0221 -0.0775 1484 ARG B NH2   
5812 N  N     . THR B 268 ? 0.7114 0.6237 0.9133 -0.0119 -0.0218 -0.0386 1485 THR B N     
5813 C  CA    . THR B 268 ? 0.8014 0.7150 1.0136 -0.0008 -0.0207 -0.0293 1485 THR B CA    
5814 C  C     . THR B 268 ? 0.7990 0.7073 1.0167 0.0056  -0.0145 -0.0331 1485 THR B C     
5815 O  O     . THR B 268 ? 0.9140 0.8105 1.1408 0.0122  -0.0082 -0.0296 1485 THR B O     
5816 C  CB    . THR B 268 ? 0.8681 0.8016 1.0809 0.0034  -0.0296 -0.0220 1485 THR B CB    
5817 O  OG1   . THR B 268 ? 0.7989 0.7446 1.0079 0.0024  -0.0331 -0.0275 1485 THR B OG1   
5818 C  CG2   . THR B 268 ? 0.8809 0.8198 1.0885 -0.0022 -0.0340 -0.0182 1485 THR B CG2   
5819 N  N     . ILE B 269 ? 0.7287 0.6446 0.9411 0.0039  -0.0152 -0.0400 1486 ILE B N     
5820 C  CA    . ILE B 269 ? 0.7683 0.6813 0.9871 0.0103  -0.0084 -0.0429 1486 ILE B CA    
5821 C  C     . ILE B 269 ? 0.7788 0.6691 0.9972 0.0099  0.0027  -0.0489 1486 ILE B C     
5822 O  O     . ILE B 269 ? 0.7638 0.6470 0.9945 0.0185  0.0095  -0.0457 1486 ILE B O     
5823 C  CB    . ILE B 269 ? 0.7224 0.6456 0.9333 0.0074  -0.0099 -0.0492 1486 ILE B CB    
5824 C  CG1   . ILE B 269 ? 0.7553 0.6994 0.9695 0.0095  -0.0200 -0.0426 1486 ILE B CG1   
5825 C  CG2   . ILE B 269 ? 0.6757 0.5943 0.8930 0.0133  -0.0004 -0.0528 1486 ILE B CG2   
5826 C  CD1   . ILE B 269 ? 0.6219 0.5752 0.8249 0.0040  -0.0236 -0.0480 1486 ILE B CD1   
5827 N  N     . GLY B 270 ? 0.7465 0.6248 0.9515 0.0000  0.0042  -0.0574 1487 GLY B N     
5828 C  CA    . GLY B 270 ? 0.7604 0.6147 0.9633 -0.0015 0.0145  -0.0642 1487 GLY B CA    
5829 C  C     . GLY B 270 ? 0.8082 0.6518 1.0245 0.0048  0.0183  -0.0555 1487 GLY B C     
5830 O  O     . GLY B 270 ? 0.7138 0.5440 0.9384 0.0122  0.0278  -0.0555 1487 GLY B O     
5831 N  N     . VAL B 271 ? 0.6119 0.4619 0.8308 0.0028  0.0113  -0.0470 1488 VAL B N     
5832 C  CA    . VAL B 271 ? 0.8434 0.6845 1.0737 0.0097  0.0141  -0.0365 1488 VAL B CA    
5833 C  C     . VAL B 271 ? 0.9777 0.8253 1.2222 0.0233  0.0157  -0.0290 1488 VAL B C     
5834 O  O     . VAL B 271 ? 0.9904 0.8229 1.2446 0.0306  0.0242  -0.0269 1488 VAL B O     
5835 C  CB    . VAL B 271 ? 0.8050 0.6559 1.0344 0.0066  0.0059  -0.0273 1488 VAL B CB    
5836 C  CG1   . VAL B 271 ? 0.7335 0.5727 0.9722 0.0135  0.0095  -0.0158 1488 VAL B CG1   
5837 C  CG2   . VAL B 271 ? 0.7898 0.6379 1.0086 -0.0071 0.0039  -0.0350 1488 VAL B CG2   
5838 N  N     . MET B 272 ? 0.8993 0.7692 1.1459 0.0266  0.0076  -0.0256 1489 MET B N     
5839 C  CA    . MET B 272 ? 0.7527 0.6326 1.0148 0.0386  0.0072  -0.0187 1489 MET B CA    
5840 C  C     . MET B 272 ? 0.7079 0.5748 0.9778 0.0435  0.0195  -0.0248 1489 MET B C     
5841 O  O     . MET B 272 ? 0.7637 0.6232 1.0483 0.0534  0.0246  -0.0184 1489 MET B O     
5842 C  CB    . MET B 272 ? 0.9036 0.8073 1.1650 0.0384  -0.0019 -0.0183 1489 MET B CB    
5843 C  CG    . MET B 272 ? 0.8476 0.7655 1.1268 0.0495  -0.0053 -0.0103 1489 MET B CG    
5844 S  SD    . MET B 272 ? 0.7657 0.7028 1.0492 0.0493  -0.0073 -0.0155 1489 MET B SD    
5845 C  CE    . MET B 272 ? 0.7170 0.6381 0.9901 0.0433  0.0062  -0.0294 1489 MET B CE    
5846 N  N     . ILE B 273 ? 0.7428 0.6047 1.0014 0.0368  0.0249  -0.0372 1490 ILE B N     
5847 C  CA    . ILE B 273 ? 0.7358 0.5838 0.9988 0.0412  0.0382  -0.0443 1490 ILE B CA    
5848 C  C     . ILE B 273 ? 0.8018 0.6257 1.0697 0.0446  0.0471  -0.0431 1490 ILE B C     
5849 O  O     . ILE B 273 ? 0.8187 0.6389 1.1044 0.0561  0.0530  -0.0365 1490 ILE B O     
5850 C  CB    . ILE B 273 ? 0.7034 0.5449 0.9468 0.0317  0.0426  -0.0584 1490 ILE B CB    
5851 C  CG1   . ILE B 273 ? 0.6695 0.5328 0.9094 0.0299  0.0362  -0.0592 1490 ILE B CG1   
5852 C  CG2   . ILE B 273 ? 0.6849 0.5053 0.9280 0.0352  0.0586  -0.0672 1490 ILE B CG2   
5853 C  CD1   . ILE B 273 ? 0.8145 0.6723 1.0313 0.0189  0.0364  -0.0710 1490 ILE B CD1   
5854 N  N     . MET B 274 ? 0.9468 0.7552 1.2007 0.0347  0.0473  -0.0482 1491 MET B N     
5855 C  CA    . MET B 274 ? 0.9809 0.7625 1.2374 0.0361  0.0573  -0.0494 1491 MET B CA    
5856 C  C     . MET B 274 ? 0.8910 0.6728 1.1651 0.0469  0.0559  -0.0342 1491 MET B C     
5857 O  O     . MET B 274 ? 0.8711 0.6337 1.1548 0.0542  0.0662  -0.0326 1491 MET B O     
5858 C  CB    . MET B 274 ? 0.9694 0.7356 1.2087 0.0218  0.0566  -0.0581 1491 MET B CB    
5859 C  CG    . MET B 274 ? 1.1320 0.8773 1.3580 0.0164  0.0672  -0.0743 1491 MET B CG    
5860 S  SD    . MET B 274 ? 1.4031 1.1349 1.6069 -0.0022 0.0638  -0.0877 1491 MET B SD    
5861 C  CE    . MET B 274 ? 1.3671 1.0806 1.5531 -0.0050 0.0750  -0.1059 1491 MET B CE    
5862 N  N     . VAL B 275 ? 0.8308 0.6338 1.1096 0.0495  0.0439  -0.0228 1492 VAL B N     
5863 C  CA    . VAL B 275 ? 0.7628 0.5628 1.0552 0.0596  0.0428  -0.0083 1492 VAL B CA    
5864 C  C     . VAL B 275 ? 0.8783 0.6864 1.1907 0.0740  0.0453  -0.0023 1492 VAL B C     
5865 O  O     . VAL B 275 ? 0.9261 0.7209 1.2520 0.0840  0.0520  0.0045  1492 VAL B O     
5866 C  CB    . VAL B 275 ? 0.7396 0.5565 1.0278 0.0579  0.0294  0.0024  1492 VAL B CB    
5867 C  CG1   . VAL B 275 ? 0.6591 0.4801 0.9620 0.0714  0.0257  0.0187  1492 VAL B CG1   
5868 C  CG2   . VAL B 275 ? 0.6634 0.4687 0.9379 0.0461  0.0292  0.0003  1492 VAL B CG2   
5869 N  N     . HIS B 276 ? 0.9371 0.7665 1.2531 0.0751  0.0410  -0.0052 1493 HIS B N     
5870 C  CA    . HIS B 276 ? 0.7572 0.6028 1.0949 0.0878  0.0389  0.0030  1493 HIS B CA    
5871 C  C     . HIS B 276 ? 0.7663 0.6109 1.1144 0.0920  0.0505  -0.0051 1493 HIS B C     
5872 O  O     . HIS B 276 ? 0.8455 0.6976 1.2164 0.1040  0.0528  0.0018  1493 HIS B O     
5873 C  CB    . HIS B 276 ? 0.7052 0.5790 1.0426 0.0865  0.0236  0.0084  1493 HIS B CB    
5874 C  CG    . HIS B 276 ? 0.7180 0.5968 1.0510 0.0873  0.0119  0.0201  1493 HIS B CG    
5875 N  ND1   . HIS B 276 ? 0.7971 0.6689 1.1408 0.0973  0.0113  0.0326  1493 HIS B ND1   
5876 C  CD2   . HIS B 276 ? 0.8216 0.7126 1.1405 0.0803  0.0006  0.0219  1493 HIS B CD2   
5877 C  CE1   . HIS B 276 ? 0.8390 0.7174 1.1731 0.0959  0.0003  0.0414  1493 HIS B CE1   
5878 N  NE2   . HIS B 276 ? 0.7508 0.6409 1.0702 0.0857  -0.0059 0.0348  1493 HIS B NE2   
5879 N  N     . ALA B 277 ? 0.8710 0.7066 1.2030 0.0829  0.0580  -0.0192 1494 ALA B N     
5880 C  CA    . ALA B 277 ? 0.9226 0.7585 1.2615 0.0865  0.0694  -0.0270 1494 ALA B CA    
5881 C  C     . ALA B 277 ? 0.9542 0.7675 1.3050 0.0957  0.0851  -0.0279 1494 ALA B C     
5882 O  O     . ALA B 277 ? 0.8772 0.6659 1.2182 0.0928  0.0906  -0.0309 1494 ALA B O     
5883 C  CB    . ALA B 277 ? 0.8421 0.6734 1.1564 0.0739  0.0724  -0.0415 1494 ALA B CB    
5884 N  N     . ASP B 278 ? 0.9954 0.8170 1.3692 0.1070  0.0925  -0.0249 1495 ASP B N     
5885 C  CA    . ASP B 278 ? 1.0102 0.8115 1.3985 0.1177  0.1082  -0.0248 1495 ASP B CA    
5886 C  C     . ASP B 278 ? 1.0090 0.7973 1.3899 0.1164  0.1258  -0.0391 1495 ASP B C     
5887 O  O     . ASP B 278 ? 0.9323 0.7185 1.2889 0.1047  0.1260  -0.0506 1495 ASP B O     
5888 C  CB    . ASP B 278 ? 0.9754 0.7934 1.3979 0.1333  0.1045  -0.0093 1495 ASP B CB    
5889 C  CG    . ASP B 278 ? 0.9026 0.7487 1.3453 0.1381  0.1030  -0.0072 1495 ASP B CG    
5890 O  OD1   . ASP B 278 ? 0.8696 0.7154 1.3064 0.1343  0.1135  -0.0181 1495 ASP B OD1   
5891 O  OD2   . ASP B 278 ? 0.8568 0.7253 1.3219 0.1458  0.0912  0.0058  1495 ASP B OD2   
5892 N  N     . ASN B 279 ? 1.1506 0.9278 1.5508 0.1285  0.1412  -0.0385 1496 ASN B N     
5893 C  CA    . ASN B 279 ? 1.1862 0.9478 1.5783 0.1285  0.1604  -0.0520 1496 ASN B CA    
5894 C  C     . ASN B 279 ? 1.0488 0.8349 1.4546 0.1318  0.1636  -0.0520 1496 ASN B C     
5895 O  O     . ASN B 279 ? 1.0098 0.7854 1.4102 0.1328  0.1806  -0.0621 1496 ASN B O     
5896 C  CB    . ASN B 279 ? 1.2048 0.9400 1.6102 0.1401  0.1779  -0.0525 1496 ASN B CB    
5897 C  CG    . ASN B 279 ? 1.2372 0.9412 1.6218 0.1334  0.1791  -0.0577 1496 ASN B CG    
5898 O  OD1   . ASN B 279 ? 1.2524 0.9470 1.6067 0.1186  0.1744  -0.0682 1496 ASN B OD1   
5899 N  ND2   . ASN B 279 ? 1.2822 0.9700 1.6840 0.1441  0.1849  -0.0500 1496 ASN B ND2   
5900 N  N     . GLN B 280 ? 1.0366 0.8541 1.4587 0.1329  0.1481  -0.0412 1497 GLN B N     
5901 C  CA    . GLN B 280 ? 1.0813 0.9224 1.5150 0.1334  0.1498  -0.0415 1497 GLN B CA    
5902 C  C     . GLN B 280 ? 0.9421 0.7967 1.3523 0.1196  0.1367  -0.0456 1497 GLN B C     
5903 O  O     . GLN B 280 ? 1.0326 0.9052 1.4486 0.1181  0.1377  -0.0464 1497 GLN B O     
5904 C  CB    . GLN B 280 ? 1.2074 1.0750 1.6823 0.1461  0.1437  -0.0267 1497 GLN B CB    
5905 C  CG    . GLN B 280 ? 1.3345 1.1893 1.8345 0.1611  0.1544  -0.0204 1497 GLN B CG    
5906 C  CD    . GLN B 280 ? 1.4071 1.2818 1.9359 0.1706  0.1387  -0.0033 1497 GLN B CD    
5907 O  OE1   . GLN B 280 ? 1.3997 1.3008 1.9601 0.1782  0.1348  0.0051  1497 GLN B OE1   
5908 N  NE2   . GLN B 280 ? 1.4760 1.3378 1.9938 0.1700  0.1293  0.0021  1497 GLN B NE2   
5909 N  N     . GLY B 281 ? 0.7900 0.6358 1.1748 0.1095  0.1254  -0.0480 1498 GLY B N     
5910 C  CA    . GLY B 281 ? 0.9286 0.7853 1.2905 0.0967  0.1133  -0.0520 1498 GLY B CA    
5911 C  C     . GLY B 281 ? 0.9303 0.7988 1.2904 0.0929  0.0934  -0.0431 1498 GLY B C     
5912 O  O     . GLY B 281 ? 0.9727 0.8312 1.3365 0.0962  0.0902  -0.0374 1498 GLY B O     
5913 N  N     . LEU B 282 ? 0.7937 0.6822 1.1466 0.0858  0.0809  -0.0421 1499 LEU B N     
5914 C  CA    . LEU B 282 ? 0.7803 0.6807 1.1305 0.0824  0.0628  -0.0340 1499 LEU B CA    
5915 C  C     . LEU B 282 ? 0.8553 0.7727 1.2343 0.0932  0.0549  -0.0205 1499 LEU B C     
5916 O  O     . LEU B 282 ? 1.0268 0.9547 1.4306 0.1019  0.0605  -0.0171 1499 LEU B O     
5917 C  CB    . LEU B 282 ? 0.7241 0.6403 1.0595 0.0728  0.0524  -0.0367 1499 LEU B CB    
5918 C  CG    . LEU B 282 ? 0.8605 0.7637 1.1646 0.0607  0.0533  -0.0476 1499 LEU B CG    
5919 C  CD1   . LEU B 282 ? 0.8463 0.7638 1.1422 0.0550  0.0504  -0.0512 1499 LEU B CD1   
5920 C  CD2   . LEU B 282 ? 0.8961 0.7947 1.1858 0.0540  0.0421  -0.0456 1499 LEU B CD2   
5921 N  N     . VAL B 283 ? 0.8582 0.7777 1.2343 0.0931  0.0422  -0.0124 1500 VAL B N     
5922 C  CA    . VAL B 283 ? 0.8425 0.7823 1.2392 0.1008  0.0295  0.0004  1500 VAL B CA    
5923 C  C     . VAL B 283 ? 0.8749 0.8216 1.2532 0.0931  0.0140  0.0033  1500 VAL B C     
5924 O  O     . VAL B 283 ? 0.9119 0.8449 1.2766 0.0907  0.0121  0.0054  1500 VAL B O     
5925 C  CB    . VAL B 283 ? 0.8557 0.7888 1.2733 0.1135  0.0321  0.0105  1500 VAL B CB    
5926 C  CG1   . VAL B 283 ? 0.8912 0.7981 1.2942 0.1123  0.0379  0.0096  1500 VAL B CG1   
5927 C  CG2   . VAL B 283 ? 0.8373 0.7909 1.2697 0.1199  0.0151  0.0241  1500 VAL B CG2   
5928 N  N     . LEU B 284 ? 0.8796 0.8471 1.2585 0.0894  0.0039  0.0037  1501 LEU B N     
5929 C  CA    . LEU B 284 ? 0.8281 0.8029 1.1881 0.0814  -0.0089 0.0041  1501 LEU B CA    
5930 C  C     . LEU B 284 ? 0.7835 0.7677 1.1495 0.0870  -0.0226 0.0160  1501 LEU B C     
5931 O  O     . LEU B 284 ? 0.8010 0.7994 1.1886 0.0949  -0.0280 0.0230  1501 LEU B O     
5932 C  CB    . LEU B 284 ? 0.9022 0.8934 1.2613 0.0758  -0.0125 -0.0010 1501 LEU B CB    
5933 C  CG    . LEU B 284 ? 0.8732 0.8582 1.2300 0.0724  0.0014  -0.0111 1501 LEU B CG    
5934 C  CD1   . LEU B 284 ? 0.6362 0.6373 0.9914 0.0668  -0.0027 -0.0146 1501 LEU B CD1   
5935 C  CD2   . LEU B 284 ? 1.0098 0.9728 1.3425 0.0655  0.0094  -0.0195 1501 LEU B CD2   
5936 N  N     . PRO B 285 ? 0.7546 0.7320 1.1019 0.0829  -0.0287 0.0188  1502 PRO B N     
5937 C  CA    . PRO B 285 ? 0.8316 0.8184 1.1789 0.0871  -0.0425 0.0296  1502 PRO B CA    
5938 C  C     . PRO B 285 ? 0.8742 0.8834 1.2269 0.0861  -0.0542 0.0300  1502 PRO B C     
5939 O  O     . PRO B 285 ? 0.7874 0.8022 1.1305 0.0780  -0.0545 0.0219  1502 PRO B O     
5940 C  CB    . PRO B 285 ? 0.8087 0.7847 1.1312 0.0797  -0.0442 0.0292  1502 PRO B CB    
5941 C  CG    . PRO B 285 ? 0.7618 0.7212 1.0750 0.0726  -0.0314 0.0190  1502 PRO B CG    
5942 C  CD    . PRO B 285 ? 0.6708 0.6353 0.9947 0.0725  -0.0245 0.0109  1502 PRO B CD    
5943 N  N     . PRO B 286 ? 0.8742 0.8962 1.2425 0.0942  -0.0644 0.0391  1503 PRO B N     
5944 C  CA    . PRO B 286 ? 0.8924 0.9356 1.2684 0.0927  -0.0760 0.0387  1503 PRO B CA    
5945 C  C     . PRO B 286 ? 0.7439 0.7905 1.0966 0.0832  -0.0829 0.0336  1503 PRO B C     
5946 O  O     . PRO B 286 ? 0.9082 0.9665 1.2642 0.0783  -0.0854 0.0279  1503 PRO B O     
5947 C  CB    . PRO B 286 ? 0.8985 0.9512 1.2874 0.1023  -0.0885 0.0506  1503 PRO B CB    
5948 C  CG    . PRO B 286 ? 0.8477 0.8875 1.2484 0.1110  -0.0794 0.0565  1503 PRO B CG    
5949 C  CD    . PRO B 286 ? 0.8700 0.8877 1.2511 0.1052  -0.0661 0.0503  1503 PRO B CD    
5950 N  N     . ARG B 287 ? 0.6399 0.6761 0.9701 0.0804  -0.0847 0.0356  1504 ARG B N     
5951 C  CA    . ARG B 287 ? 0.6424 0.6831 0.9522 0.0731  -0.0920 0.0323  1504 ARG B CA    
5952 C  C     . ARG B 287 ? 0.6114 0.6485 0.9109 0.0638  -0.0840 0.0217  1504 ARG B C     
5953 O  O     . ARG B 287 ? 0.8193 0.8618 1.1055 0.0581  -0.0894 0.0182  1504 ARG B O     
5954 C  CB    . ARG B 287 ? 0.6244 0.6561 0.9148 0.0739  -0.0959 0.0389  1504 ARG B CB    
5955 C  CG    . ARG B 287 ? 0.6991 0.7353 0.9936 0.0826  -0.1067 0.0501  1504 ARG B CG    
5956 C  CD    . ARG B 287 ? 0.8039 0.8498 1.0834 0.0808  -0.1202 0.0513  1504 ARG B CD    
5957 N  NE    . ARG B 287 ? 0.9884 1.0244 1.2448 0.0811  -0.1217 0.0572  1504 ARG B NE    
5958 C  CZ    . ARG B 287 ? 1.1702 1.2054 1.4052 0.0751  -0.1234 0.0538  1504 ARG B CZ    
5959 N  NH1   . ARG B 287 ? 1.1322 1.1755 1.3658 0.0685  -0.1245 0.0444  1504 ARG B NH1   
5960 N  NH2   . ARG B 287 ? 1.2403 1.2662 1.4559 0.0761  -0.1232 0.0602  1504 ARG B NH2   
5961 N  N     . VAL B 288 ? 0.5735 0.6012 0.8780 0.0625  -0.0716 0.0164  1505 VAL B N     
5962 C  CA    . VAL B 288 ? 0.6407 0.6657 0.9355 0.0542  -0.0649 0.0066  1505 VAL B CA    
5963 C  C     . VAL B 288 ? 0.7184 0.7483 1.0282 0.0546  -0.0580 0.0014  1505 VAL B C     
5964 O  O     . VAL B 288 ? 0.7000 0.7282 1.0010 0.0481  -0.0529 -0.0063 1505 VAL B O     
5965 C  CB    . VAL B 288 ? 0.6923 0.7000 0.9734 0.0498  -0.0561 0.0030  1505 VAL B CB    
5966 C  CG1   . VAL B 288 ? 0.6531 0.6564 0.9212 0.0491  -0.0614 0.0088  1505 VAL B CG1   
5967 C  CG2   . VAL B 288 ? 0.8583 0.8537 1.1510 0.0547  -0.0455 0.0030  1505 VAL B CG2   
5968 N  N     . ALA B 289 ? 0.7573 0.7933 1.0896 0.0621  -0.0573 0.0057  1506 ALA B N     
5969 C  CA    . ALA B 289 ? 0.7093 0.7496 1.0570 0.0626  -0.0484 0.0010  1506 ALA B CA    
5970 C  C     . ALA B 289 ? 0.7640 0.8193 1.1137 0.0578  -0.0546 -0.0017 1506 ALA B C     
5971 O  O     . ALA B 289 ? 0.6274 0.6959 0.9842 0.0592  -0.0669 0.0029  1506 ALA B O     
5972 C  CB    . ALA B 289 ? 0.5530 0.5969 0.9273 0.0726  -0.0455 0.0071  1506 ALA B CB    
5973 N  N     . CYS B 290 ? 0.8758 0.9280 1.2174 0.0517  -0.0464 -0.0093 1507 CYS B N     
5974 C  CA    . CYS B 290 ? 0.7709 0.8352 1.1151 0.0471  -0.0500 -0.0118 1507 CYS B CA    
5975 C  C     . CYS B 290 ? 0.8383 0.9186 1.2114 0.0518  -0.0538 -0.0074 1507 CYS B C     
5976 O  O     . CYS B 290 ? 0.8192 0.9121 1.1972 0.0502  -0.0657 -0.0052 1507 CYS B O     
5977 C  CB    . CYS B 290 ? 0.7598 0.8163 1.0935 0.0417  -0.0378 -0.0194 1507 CYS B CB    
5978 S  SG    . CYS B 290 ? 1.0155 1.0832 1.3526 0.0360  -0.0378 -0.0224 1507 CYS B SG    
5979 N  N     . ILE B 291 ? 0.8411 0.9210 1.2345 0.0579  -0.0440 -0.0059 1508 ILE B N     
5980 C  CA    . ILE B 291 ? 0.7307 0.8270 1.1562 0.0637  -0.0474 -0.0005 1508 ILE B CA    
5981 C  C     . ILE B 291 ? 0.7472 0.8416 1.1836 0.0728  -0.0507 0.0067  1508 ILE B C     
5982 O  O     . ILE B 291 ? 0.7842 0.8650 1.2197 0.0772  -0.0392 0.0062  1508 ILE B O     
5983 C  CB    . ILE B 291 ? 0.7128 0.8122 1.1572 0.0644  -0.0324 -0.0036 1508 ILE B CB    
5984 C  CG1   . ILE B 291 ? 0.6546 0.7495 1.0808 0.0555  -0.0262 -0.0108 1508 ILE B CG1   
5985 C  CG2   . ILE B 291 ? 0.7112 0.8317 1.1910 0.0681  -0.0379 0.0017  1508 ILE B CG2   
5986 C  CD1   . ILE B 291 ? 0.5679 0.6620 1.0061 0.0558  -0.0092 -0.0141 1508 ILE B CD1   
5987 N  N     . GLN B 292 ? 0.6332 0.7403 1.0792 0.0760  -0.0665 0.0136  1509 GLN B N     
5988 C  CA    . GLN B 292 ? 0.6732 0.7791 1.1297 0.0855  -0.0706 0.0220  1509 GLN B CA    
5989 C  C     . GLN B 292 ? 0.8233 0.9404 1.3163 0.0937  -0.0652 0.0262  1509 GLN B C     
5990 O  O     . GLN B 292 ? 0.8073 0.9167 1.3104 0.1024  -0.0587 0.0308  1509 GLN B O     
5991 C  CB    . GLN B 292 ? 0.6069 0.7209 1.0561 0.0861  -0.0900 0.0282  1509 GLN B CB    
5992 C  CG    . GLN B 292 ? 0.7427 0.8422 1.1571 0.0813  -0.0928 0.0264  1509 GLN B CG    
5993 C  CD    . GLN B 292 ? 0.8372 0.9446 1.2398 0.0800  -0.1107 0.0302  1509 GLN B CD    
5994 O  OE1   . GLN B 292 ? 0.7092 0.8322 1.1230 0.0781  -0.1213 0.0300  1509 GLN B OE1   
5995 N  NE2   . GLN B 292 ? 0.9595 1.0550 1.3385 0.0805  -0.1136 0.0334  1509 GLN B NE2   
5996 N  N     . VAL B 293 ? 0.7942 0.9292 1.3086 0.0911  -0.0675 0.0249  1510 VAL B N     
5997 C  CA    . VAL B 293 ? 0.6895 0.8399 1.2435 0.0980  -0.0634 0.0292  1510 VAL B CA    
5998 C  C     . VAL B 293 ? 0.6536 0.8080 1.2171 0.0923  -0.0498 0.0222  1510 VAL B C     
5999 O  O     . VAL B 293 ? 0.5868 0.7461 1.1399 0.0830  -0.0549 0.0176  1510 VAL B O     
6000 C  CB    . VAL B 293 ? 0.6005 0.7734 1.1765 0.1004  -0.0835 0.0365  1510 VAL B CB    
6001 C  CG1   . VAL B 293 ? 0.5402 0.7298 1.1596 0.1078  -0.0786 0.0412  1510 VAL B CG1   
6002 C  CG2   . VAL B 293 ? 0.6555 0.8238 1.2167 0.1055  -0.0982 0.0438  1510 VAL B CG2   
6003 N  N     . VAL B 294 ? 0.5813 0.7333 1.1646 0.0980  -0.0322 0.0217  1511 VAL B N     
6004 C  CA    . VAL B 294 ? 0.6573 0.8150 1.2538 0.0936  -0.0182 0.0166  1511 VAL B CA    
6005 C  C     . VAL B 294 ? 0.7689 0.9475 1.4126 0.1011  -0.0155 0.0228  1511 VAL B C     
6006 O  O     . VAL B 294 ? 0.9378 1.1152 1.5999 0.1120  -0.0103 0.0280  1511 VAL B O     
6007 C  CB    . VAL B 294 ? 0.5946 0.7296 1.1687 0.0922  0.0033  0.0088  1511 VAL B CB    
6008 C  CG1   . VAL B 294 ? 0.7538 0.8764 1.3360 0.1029  0.0156  0.0108  1511 VAL B CG1   
6009 C  CG2   . VAL B 294 ? 0.5765 0.7170 1.1617 0.0878  0.0179  0.0044  1511 VAL B CG2   
6010 N  N     . ILE B 295 ? 0.6412 0.8384 1.3057 0.0953  -0.0180 0.0223  1512 ILE B N     
6011 C  CA    . ILE B 295 ? 0.6718 0.8931 1.3852 0.1005  -0.0173 0.0281  1512 ILE B CA    
6012 C  C     . ILE B 295 ? 0.7569 0.9745 1.4841 0.1018  0.0087  0.0245  1512 ILE B C     
6013 O  O     . ILE B 295 ? 0.5989 0.8137 1.3158 0.0930  0.0176  0.0188  1512 ILE B O     
6014 C  CB    . ILE B 295 ? 0.6254 0.8695 1.3561 0.0923  -0.0346 0.0294  1512 ILE B CB    
6015 C  CG1   . ILE B 295 ? 0.4959 0.7408 1.2049 0.0891  -0.0597 0.0310  1512 ILE B CG1   
6016 C  CG2   . ILE B 295 ? 0.7572 1.0285 1.5426 0.0980  -0.0356 0.0363  1512 ILE B CG2   
6017 C  CD1   . ILE B 295 ? 0.5831 0.8438 1.3157 0.0977  -0.0776 0.0403  1512 ILE B CD1   
6018 N  N     . VAL B 296 ? 0.8652 1.0826 1.6165 0.1132  0.0218  0.0282  1513 VAL B N     
6019 C  CA    . VAL B 296 ? 0.9241 1.1398 1.6920 0.1153  0.0474  0.0253  1513 VAL B CA    
6020 C  C     . VAL B 296 ? 0.8879 1.1340 1.7120 0.1198  0.0462  0.0326  1513 VAL B C     
6021 O  O     . VAL B 296 ? 0.7581 1.0160 1.6118 0.1306  0.0394  0.0405  1513 VAL B O     
6022 C  CB    . VAL B 296 ? 0.8731 1.0654 1.6286 0.1247  0.0665  0.0228  1513 VAL B CB    
6023 C  CG1   . VAL B 296 ? 0.9115 1.0973 1.6734 0.1252  0.0945  0.0177  1513 VAL B CG1   
6024 C  CG2   . VAL B 296 ? 0.7433 0.9087 1.4477 0.1203  0.0623  0.0169  1513 VAL B CG2   
6025 N  N     . PRO B 297 ? 0.9127 1.1727 1.7542 0.1119  0.0518  0.0310  1514 PRO B N     
6026 C  CA    . PRO B 297 ? 0.8762 1.1657 1.7750 0.1158  0.0536  0.0377  1514 PRO B CA    
6027 C  C     . PRO B 297 ? 0.8648 1.1497 1.7856 0.1272  0.0805  0.0388  1514 PRO B C     
6028 O  O     . PRO B 297 ? 0.8298 1.0925 1.7243 0.1261  0.1029  0.0319  1514 PRO B O     
6029 C  CB    . PRO B 297 ? 0.8870 1.1863 1.7897 0.1024  0.0552  0.0343  1514 PRO B CB    
6030 C  CG    . PRO B 297 ? 0.8634 1.1340 1.7133 0.0952  0.0662  0.0255  1514 PRO B CG    
6031 C  CD    . PRO B 297 ? 0.8894 1.1391 1.6998 0.0989  0.0564  0.0235  1514 PRO B CD    
6032 N  N     . CYS B 298 ? 0.9215 1.2262 1.8887 0.1388  0.0779  0.0475  1515 CYS B N     
6033 C  CA    . CYS B 298 ? 0.8985 1.1992 1.8900 0.1521  0.1022  0.0496  1515 CYS B CA    
6034 C  C     . CYS B 298 ? 0.8148 1.1451 1.8646 0.1540  0.1128  0.0548  1515 CYS B C     
6035 O  O     . CYS B 298 ? 0.6560 1.0144 1.7366 0.1474  0.0961  0.0591  1515 CYS B O     
6036 C  CB    . CYS B 298 ? 0.9366 1.2358 1.9404 0.1669  0.0944  0.0568  1515 CYS B CB    
6037 S  SG    . CYS B 298 ? 1.1221 1.4036 2.0816 0.1666  0.0687  0.0576  1515 CYS B SG    
6038 N  N     . GLY B 299 ? 0.8452 1.1687 1.9112 0.1633  0.1414  0.0542  1516 GLY B N     
6039 C  CA    . GLY B 299 ? 0.9862 1.3387 2.1127 0.1676  0.1528  0.0604  1516 GLY B CA    
6040 C  C     . GLY B 299 ? 0.8897 1.2487 2.0208 0.1555  0.1672  0.0564  1516 GLY B C     
6041 O  O     . GLY B 299 ? 0.8713 1.2584 2.0563 0.1567  0.1741  0.0621  1516 GLY B O     
6042 N  N     . ILE B 300 ? 0.8785 1.2134 1.9570 0.1439  0.1717  0.0474  1517 ILE B N     
6043 C  CA    . ILE B 300 ? 0.8881 1.2276 1.9725 0.1338  0.1886  0.0447  1517 ILE B CA    
6044 C  C     . ILE B 300 ? 1.0467 1.3786 2.1471 0.1442  0.2239  0.0442  1517 ILE B C     
6045 O  O     . ILE B 300 ? 1.0903 1.3909 2.1502 0.1490  0.2412  0.0375  1517 ILE B O     
6046 C  CB    . ILE B 300 ? 0.8333 1.1480 1.8576 0.1202  0.1866  0.0360  1517 ILE B CB    
6047 N  N     . THR B 301 ? 1.1703 1.5310 2.3307 0.1476  0.2347  0.0511  1518 THR B N     
6048 C  CA    . THR B 301 ? 1.2571 1.6127 2.4369 0.1592  0.2650  0.0524  1518 THR B CA    
6049 C  C     . THR B 301 ? 1.3215 1.6671 2.4915 0.1533  0.2962  0.0478  1518 THR B C     
6050 O  O     . THR B 301 ? 1.4430 1.7968 2.6392 0.1550  0.3136  0.0520  1518 THR B O     
6051 C  CB    . THR B 301 ? 1.2021 1.5839 2.4294 0.1640  0.2547  0.0627  1518 THR B CB    
6052 N  N     . ALA B 302 ? 1.2669 1.5867 2.3810 0.1436  0.2991  0.0394  1519 ALA B N     
6053 C  CA    . ALA B 302 ? 1.3233 1.6242 2.4106 0.1383  0.3286  0.0341  1519 ALA B CA    
6054 C  C     . ALA B 302 ? 1.3400 1.6684 2.4806 0.1348  0.3448  0.0407  1519 ALA B C     
6055 O  O     . ALA B 302 ? 1.3033 1.6293 2.4596 0.1422  0.3690  0.0428  1519 ALA B O     
6056 C  CB    . ALA B 302 ? 1.3788 1.6491 2.4377 0.1503  0.3562  0.0277  1519 ALA B CB    
6057 N  N     . THR B 303 ? 1.3704 1.7175 2.5241 0.1210  0.3272  0.0437  1520 THR B N     
6058 C  CA    . THR B 303 ? 1.4032 1.7721 2.5966 0.1133  0.3357  0.0499  1520 THR B CA    
6059 C  C     . THR B 303 ? 1.4276 1.8181 2.6684 0.1205  0.3311  0.0581  1520 THR B C     
6060 O  O     . THR B 303 ? 1.5165 1.9175 2.7846 0.1175  0.3461  0.0627  1520 THR B O     
6061 C  CB    . THR B 303 ? 1.4123 1.7618 2.5839 0.1107  0.3722  0.0469  1520 THR B CB    
6062 N  N     . THR B 304 ? 1.3777 1.7748 2.6292 0.1301  0.3110  0.0605  1521 THR B N     
6063 C  CA    . THR B 304 ? 1.2792 1.7041 2.5794 0.1333  0.2963  0.0694  1521 THR B CA    
6064 C  C     . THR B 304 ? 1.4235 1.8746 2.7477 0.1190  0.2694  0.0729  1521 THR B C     
6065 O  O     . THR B 304 ? 1.5138 1.9889 2.8802 0.1166  0.2641  0.0795  1521 THR B O     
6066 C  CB    . THR B 304 ? 1.0800 1.5055 2.3835 0.1464  0.2793  0.0720  1521 THR B CB    
6067 N  N     . THR B 305 ? 1.3646 1.8108 2.6622 0.1092  0.2525  0.0681  1522 THR B N     
6068 C  CA    . THR B 305 ? 1.2671 1.7335 2.5801 0.0948  0.2263  0.0697  1522 THR B CA    
6069 C  C     . THR B 305 ? 1.1217 1.5723 2.3954 0.0848  0.2227  0.0626  1522 THR B C     
6070 O  O     . THR B 305 ? 0.9933 1.4231 2.2312 0.0910  0.2273  0.0573  1522 THR B O     
6071 C  CB    . THR B 305 ? 1.2553 1.7415 2.5880 0.0980  0.1913  0.0742  1522 THR B CB    
6072 N  N     . ASP B 306 ? 1.1288 1.5891 2.4100 0.0692  0.2147  0.0624  1523 ASP B N     
6073 C  CA    . ASP B 306 ? 1.2097 1.6564 2.4573 0.0581  0.2127  0.0564  1523 ASP B CA    
6074 C  C     . ASP B 306 ? 1.2913 1.7510 2.5414 0.0465  0.1774  0.0555  1523 ASP B C     
6075 O  O     . ASP B 306 ? 1.2777 1.7147 2.4736 0.0417  0.1630  0.0496  1523 ASP B O     
6076 C  CB    . ASP B 306 ? 1.1712 1.6101 2.4167 0.0489  0.2408  0.0562  1523 ASP B CB    
6077 C  CG    . ASP B 306 ? 1.1163 1.5260 2.2996 0.0377  0.2382  0.0498  1523 ASP B CG    
6078 O  OD1   . ASP B 306 ? 1.1437 1.5278 2.2902 0.0386  0.2644  0.0471  1523 ASP B OD1   
6079 O  OD2   . ASP B 306 ? 1.0272 1.4375 2.1950 0.0281  0.2104  0.0474  1523 ASP B OD2   
6080 N  N     . ASP B 307 ? 1.3281 1.8108 2.6137 0.0405  0.1595  0.0599  1524 ASP B N     
6081 C  CA    . ASP B 307 ? 1.3054 1.7980 2.5895 0.0289  0.1264  0.0579  1524 ASP B CA    
6082 C  C     . ASP B 307 ? 1.0787 1.5698 2.3439 0.0367  0.1004  0.0565  1524 ASP B C     
6083 O  O     . ASP B 307 ? 1.0091 1.4911 2.2441 0.0301  0.0817  0.0515  1524 ASP B O     
6084 C  CB    . ASP B 307 ? 1.4206 1.9379 2.7466 0.0217  0.1130  0.0624  1524 ASP B CB    
6085 N  N     . GLU B 308 ? 1.0370 1.5331 2.3147 0.0511  0.1004  0.0609  1525 GLU B N     
6086 C  CA    . GLU B 308 ? 0.9996 1.4912 2.2582 0.0610  0.0807  0.0608  1525 GLU B CA    
6087 C  C     . GLU B 308 ? 0.8466 1.3081 2.0497 0.0624  0.0852  0.0541  1525 GLU B C     
6088 O  O     . GLU B 308 ? 0.8842 1.3380 2.0584 0.0644  0.0620  0.0525  1525 GLU B O     
6089 C  CB    . GLU B 308 ? 0.9758 1.4717 2.2539 0.0773  0.0895  0.0669  1525 GLU B CB    
6090 C  CG    . GLU B 308 ? 0.7884 1.3095 2.1122 0.0773  0.0846  0.0739  1525 GLU B CG    
6091 C  CD    . GLU B 308 ? 0.9634 1.4874 2.3098 0.0722  0.1133  0.0746  1525 GLU B CD    
6092 O  OE1   . GLU B 308 ? 0.9437 1.4505 2.2673 0.0666  0.1332  0.0696  1525 GLU B OE1   
6093 O  OE2   . GLU B 308 ? 1.0437 1.5856 2.4291 0.0751  0.1181  0.0806  1525 GLU B OE2   
6094 N  N     . ARG B 309 ? 0.8161 1.2534 1.9878 0.0602  0.1126  0.0497  1526 ARG B N     
6095 C  CA    . ARG B 309 ? 0.9919 1.3931 2.0944 0.0604  0.1146  0.0426  1526 ARG B CA    
6096 C  C     . ARG B 309 ? 1.0047 1.3998 2.0741 0.0494  0.0867  0.0385  1526 ARG B C     
6097 O  O     . ARG B 309 ? 0.9143 1.2947 1.9466 0.0531  0.0712  0.0359  1526 ARG B O     
6098 C  CB    . ARG B 309 ? 1.0412 1.4200 2.1165 0.0570  0.1455  0.0387  1526 ARG B CB    
6099 N  N     . ARG B 310 ? 0.9913 1.3983 2.0769 0.0361  0.0799  0.0382  1527 ARG B N     
6100 C  CA    . ARG B 310 ? 0.9141 1.3158 1.9716 0.0256  0.0539  0.0340  1527 ARG B CA    
6101 C  C     . ARG B 310 ? 0.7906 1.2113 1.8667 0.0289  0.0231  0.0366  1527 ARG B C     
6102 O  O     . ARG B 310 ? 0.7999 1.2082 1.8380 0.0272  0.0031  0.0331  1527 ARG B O     
6103 C  CB    . ARG B 310 ? 0.9250 1.3332 1.9967 0.0105  0.0556  0.0328  1527 ARG B CB    
6104 C  CG    . ARG B 310 ? 0.9303 1.3110 1.9603 0.0048  0.0769  0.0289  1527 ARG B CG    
6105 C  CD    . ARG B 310 ? 0.9430 1.3299 1.9894 -0.0100 0.0778  0.0287  1527 ARG B CD    
6106 N  NE    . ARG B 310 ? 0.9270 1.3269 2.0156 -0.0112 0.1032  0.0336  1527 ARG B NE    
6107 C  CZ    . ARG B 310 ? 0.9286 1.3101 1.9969 -0.0122 0.1314  0.0336  1527 ARG B CZ    
6108 N  NH1   . ARG B 310 ? 1.0027 1.3529 2.0099 -0.0119 0.1360  0.0290  1527 ARG B NH1   
6109 N  NH2   . ARG B 310 ? 0.8217 1.2160 1.9302 -0.0132 0.1550  0.0386  1527 ARG B NH2   
6110 N  N     . ARG B 311 ? 0.7372 1.1883 1.8713 0.0338  0.0190  0.0433  1528 ARG B N     
6111 C  CA    . ARG B 311 ? 0.6247 1.0955 1.7783 0.0372  -0.0113 0.0467  1528 ARG B CA    
6112 C  C     . ARG B 311 ? 0.7712 1.2247 1.8876 0.0493  -0.0189 0.0470  1528 ARG B C     
6113 O  O     . ARG B 311 ? 0.7109 1.1605 1.8019 0.0476  -0.0442 0.0455  1528 ARG B O     
6114 C  CB    . ARG B 311 ? 0.4309 0.9324 1.6456 0.0420  -0.0109 0.0544  1528 ARG B CB    
6115 N  N     . LEU B 312 ? 0.8882 1.3298 2.0000 0.0614  0.0037  0.0488  1529 LEU B N     
6116 C  CA    . LEU B 312 ? 0.8240 1.2470 1.9019 0.0729  -0.0001 0.0492  1529 LEU B CA    
6117 C  C     . LEU B 312 ? 0.6716 1.0638 1.6841 0.0666  -0.0039 0.0415  1529 LEU B C     
6118 O  O     . LEU B 312 ? 0.6388 1.0231 1.6236 0.0689  -0.0235 0.0413  1529 LEU B O     
6119 C  CB    . LEU B 312 ? 0.8580 1.2732 1.9462 0.0860  0.0277  0.0516  1529 LEU B CB    
6120 C  CG    . LEU B 312 ? 0.8481 1.2373 1.8964 0.0968  0.0309  0.0504  1529 LEU B CG    
6121 C  CD1   . LEU B 312 ? 0.8327 1.2330 1.8900 0.1045  0.0046  0.0567  1529 LEU B CD1   
6122 C  CD2   . LEU B 312 ? 0.8884 1.2704 1.9516 0.1083  0.0609  0.0517  1529 LEU B CD2   
6123 N  N     . TYR B 313 ? 0.4874 0.8619 1.4746 0.0591  0.0152  0.0356  1530 TYR B N     
6124 C  CA    . TYR B 313 ? 0.6418 0.9895 1.5706 0.0524  0.0109  0.0287  1530 TYR B CA    
6125 C  C     . TYR B 313 ? 0.8070 1.1613 1.7256 0.0439  -0.0185 0.0273  1530 TYR B C     
6126 O  O     . TYR B 313 ? 0.9538 1.2906 1.8292 0.0434  -0.0302 0.0239  1530 TYR B O     
6127 C  CB    . TYR B 313 ? 0.8074 1.1407 1.7191 0.0444  0.0333  0.0241  1530 TYR B CB    
6128 C  CG    . TYR B 313 ? 0.9513 1.2650 1.8451 0.0524  0.0607  0.0225  1530 TYR B CG    
6129 C  CD1   . TYR B 313 ? 1.1434 1.4569 2.0484 0.0659  0.0663  0.0255  1530 TYR B CD1   
6130 C  CD2   . TYR B 313 ? 0.8822 1.1762 1.7463 0.0468  0.0805  0.0179  1530 TYR B CD2   
6131 C  CE1   . TYR B 313 ? 1.2006 1.4939 2.0871 0.0729  0.0912  0.0229  1530 TYR B CE1   
6132 C  CE2   . TYR B 313 ? 0.9932 1.2679 1.8376 0.0538  0.1047  0.0155  1530 TYR B CE2   
6133 C  CZ    . TYR B 313 ? 1.1217 1.3956 1.9771 0.0666  0.1101  0.0175  1530 TYR B CZ    
6134 O  OH    . TYR B 313 ? 1.0812 1.3340 1.9157 0.0734  0.1342  0.0140  1530 TYR B OH    
6135 N  N     . GLU B 314 ? 0.8514 1.2308 1.8103 0.0373  -0.0306 0.0296  1531 GLU B N     
6136 C  CA    . GLU B 314 ? 0.7987 1.1840 1.7492 0.0281  -0.0578 0.0271  1531 GLU B CA    
6137 C  C     . GLU B 314 ? 0.7435 1.1363 1.6924 0.0358  -0.0820 0.0308  1531 GLU B C     
6138 O  O     . GLU B 314 ? 0.7099 1.0917 1.6230 0.0323  -0.1002 0.0274  1531 GLU B O     
6139 C  CB    . GLU B 314 ? 0.7120 1.1214 1.7078 0.0177  -0.0620 0.0279  1531 GLU B CB    
6140 C  CG    . GLU B 314 ? 0.7907 1.2065 1.7812 0.0068  -0.0897 0.0242  1531 GLU B CG    
6141 C  CD    . GLU B 314 ? 0.9243 1.3121 1.8556 0.0009  -0.0950 0.0170  1531 GLU B CD    
6142 O  OE1   . GLU B 314 ? 0.9191 1.2838 1.8170 0.0012  -0.0757 0.0142  1531 GLU B OE1   
6143 O  OE2   . GLU B 314 ? 1.0396 1.4287 1.9575 -0.0038 -0.1193 0.0142  1531 GLU B OE2   
6144 N  N     . SER B 315 ? 0.7713 1.1821 1.7583 0.0469  -0.0822 0.0382  1532 SER B N     
6145 C  CA    . SER B 315 ? 0.7261 1.1416 1.7083 0.0554  -0.1042 0.0429  1532 SER B CA    
6146 C  C     . SER B 315 ? 0.7914 1.1777 1.7214 0.0619  -0.0997 0.0409  1532 SER B C     
6147 O  O     . SER B 315 ? 0.8531 1.2325 1.7548 0.0628  -0.1193 0.0411  1532 SER B O     
6148 C  CB    . SER B 315 ? 0.6340 1.0737 1.6680 0.0672  -0.1039 0.0522  1532 SER B CB    
6149 O  OG    . SER B 315 ? 0.7007 1.1478 1.7323 0.0737  -0.1292 0.0574  1532 SER B OG    
6150 N  N     . CYS B 316 ? 0.7695 1.1369 1.6835 0.0651  -0.0736 0.0384  1533 CYS B N     
6151 C  CA    . CYS B 316 ? 0.7609 1.0997 1.6250 0.0692  -0.0684 0.0354  1533 CYS B CA    
6152 C  C     . CYS B 316 ? 0.8390 1.1624 1.6585 0.0583  -0.0794 0.0285  1533 CYS B C     
6153 O  O     . CYS B 316 ? 0.8058 1.1139 1.5889 0.0606  -0.0888 0.0276  1533 CYS B O     
6154 C  CB    . CYS B 316 ? 0.7265 1.0487 1.5829 0.0733  -0.0386 0.0329  1533 CYS B CB    
6155 S  SG    . CYS B 316 ? 0.8022 1.1345 1.7019 0.0890  -0.0217 0.0402  1533 CYS B SG    
6156 N  N     . ARG B 317 ? 0.8575 1.1848 1.6808 0.0465  -0.0777 0.0239  1534 ARG B N     
6157 C  CA    . ARG B 317 ? 0.7708 1.0837 1.5545 0.0365  -0.0872 0.0175  1534 ARG B CA    
6158 C  C     . ARG B 317 ? 0.8108 1.1320 1.5893 0.0344  -0.1155 0.0181  1534 ARG B C     
6159 O  O     . ARG B 317 ? 0.9148 1.2195 1.6520 0.0320  -0.1241 0.0144  1534 ARG B O     
6160 C  CB    . ARG B 317 ? 0.7284 1.0424 1.5192 0.0249  -0.0778 0.0131  1534 ARG B CB    
6161 N  N     . GLU B 318 ? 0.7631 1.1095 1.5818 0.0356  -0.1304 0.0229  1535 GLU B N     
6162 C  CA    . GLU B 318 ? 0.8836 1.2353 1.6910 0.0340  -0.1578 0.0231  1535 GLU B CA    
6163 C  C     . GLU B 318 ? 0.8505 1.1932 1.6360 0.0456  -0.1645 0.0281  1535 GLU B C     
6164 O  O     . GLU B 318 ? 0.9018 1.2353 1.6546 0.0443  -0.1806 0.0265  1535 GLU B O     
6165 C  CB    . GLU B 318 ? 1.1289 1.5101 1.9819 0.0315  -0.1761 0.0266  1535 GLU B CB    
6166 N  N     . LEU B 319 ? 0.7920 1.1355 1.5937 0.0570  -0.1512 0.0341  1536 LEU B N     
6167 C  CA    . LEU B 319 ? 0.7951 1.1260 1.5725 0.0675  -0.1556 0.0387  1536 LEU B CA    
6168 C  C     . LEU B 319 ? 0.6947 0.9967 1.4195 0.0645  -0.1474 0.0327  1536 LEU B C     
6169 O  O     . LEU B 319 ? 0.6006 0.8922 1.2940 0.0659  -0.1602 0.0333  1536 LEU B O     
6170 C  CB    . LEU B 319 ? 0.8998 1.2344 1.7045 0.0804  -0.1412 0.0458  1536 LEU B CB    
6171 C  CG    . LEU B 319 ? 0.9004 1.2213 1.6843 0.0919  -0.1440 0.0517  1536 LEU B CG    
6172 C  CD1   . LEU B 319 ? 0.8213 1.1517 1.6001 0.0939  -0.1719 0.0571  1536 LEU B CD1   
6173 C  CD2   . LEU B 319 ? 0.9782 1.3032 1.7938 0.1049  -0.1291 0.0585  1536 LEU B CD2   
6174 N  N     . GLU B 320 ? 0.7394 1.0288 1.4542 0.0602  -0.1265 0.0270  1537 GLU B N     
6175 C  CA    . GLU B 320 ? 0.7503 1.0144 1.4177 0.0566  -0.1197 0.0212  1537 GLU B CA    
6176 C  C     . GLU B 320 ? 0.9047 1.1657 1.5461 0.0476  -0.1365 0.0166  1537 GLU B C     
6177 O  O     . GLU B 320 ? 0.8383 1.0832 1.4424 0.0478  -0.1411 0.0150  1537 GLU B O     
6178 C  CB    . GLU B 320 ? 0.7255 0.9788 1.3886 0.0530  -0.0959 0.0162  1537 GLU B CB    
6179 C  CG    . GLU B 320 ? 0.7047 0.9373 1.3253 0.0455  -0.0908 0.0091  1537 GLU B CG    
6180 C  CD    . GLU B 320 ? 0.6888 0.9142 1.3096 0.0415  -0.0690 0.0050  1537 GLU B CD    
6181 O  OE1   . GLU B 320 ? 0.6396 0.8461 1.2264 0.0383  -0.0604 0.0003  1537 GLU B OE1   
6182 O  OE2   . GLU B 320 ? 0.7118 0.9509 1.3674 0.0415  -0.0604 0.0069  1537 GLU B OE2   
6183 N  N     . GLN B 321 ? 1.0359 1.3120 1.6976 0.0396  -0.1458 0.0145  1538 GLN B N     
6184 C  CA    . GLN B 321 ? 1.1034 1.3747 1.7404 0.0307  -0.1607 0.0091  1538 GLN B CA    
6185 C  C     . GLN B 321 ? 1.0084 1.2819 1.6318 0.0348  -0.1824 0.0123  1538 GLN B C     
6186 O  O     . GLN B 321 ? 0.9734 1.2328 1.5597 0.0321  -0.1896 0.0088  1538 GLN B O     
6187 C  CB    . GLN B 321 ? 1.1225 1.4082 1.7860 0.0205  -0.1650 0.0056  1538 GLN B CB    
6188 C  CG    . GLN B 321 ? 1.1412 1.4192 1.8052 0.0140  -0.1448 0.0013  1538 GLN B CG    
6189 C  CD    . GLN B 321 ? 1.2356 1.4890 1.8570 0.0147  -0.1322 -0.0021 1538 GLN B CD    
6190 O  OE1   . GLN B 321 ? 1.2864 1.5272 1.8744 0.0113  -0.1408 -0.0060 1538 GLN B OE1   
6191 N  NE2   . GLN B 321 ? 1.2252 1.4713 1.8475 0.0193  -0.1119 -0.0009 1538 GLN B NE2   
6192 N  N     . THR B 322 ? 0.9905 1.2813 1.6430 0.0419  -0.1926 0.0195  1539 THR B N     
6193 C  CA    . THR B 322 ? 0.9857 1.2774 1.6225 0.0465  -0.2132 0.0236  1539 THR B CA    
6194 C  C     . THR B 322 ? 1.0124 1.2852 1.6180 0.0552  -0.2067 0.0274  1539 THR B C     
6195 O  O     . THR B 322 ? 0.9822 1.2471 1.5586 0.0567  -0.2198 0.0286  1539 THR B O     
6196 C  CB    . THR B 322 ? 0.9355 1.2522 1.6129 0.0519  -0.2280 0.0311  1539 THR B CB    
6197 O  OG1   . THR B 322 ? 0.8492 1.1747 1.5620 0.0590  -0.2118 0.0363  1539 THR B OG1   
6198 C  CG2   . THR B 322 ? 1.0387 1.3736 1.7387 0.0414  -0.2435 0.0267  1539 THR B CG2   
6199 N  N     . PHE B 323 ? 0.9175 1.1809 1.5257 0.0600  -0.1857 0.0284  1540 PHE B N     
6200 C  CA    . PHE B 323 ? 0.9130 1.1562 1.4893 0.0660  -0.1788 0.0305  1540 PHE B CA    
6201 C  C     . PHE B 323 ? 1.0180 1.2430 1.5535 0.0583  -0.1758 0.0230  1540 PHE B C     
6202 O  O     . PHE B 323 ? 1.0980 1.3106 1.6025 0.0603  -0.1817 0.0243  1540 PHE B O     
6203 C  CB    . PHE B 323 ? 0.7835 1.0203 1.3729 0.0729  -0.1578 0.0328  1540 PHE B CB    
6204 C  CG    . PHE B 323 ? 0.7768 1.0250 1.3966 0.0845  -0.1607 0.0424  1540 PHE B CG    
6205 C  CD1   . PHE B 323 ? 0.7153 0.9724 1.3369 0.0896  -0.1813 0.0497  1540 PHE B CD1   
6206 C  CD2   . PHE B 323 ? 0.7559 1.0052 1.4016 0.0907  -0.1428 0.0444  1540 PHE B CD2   
6207 C  CE1   . PHE B 323 ? 0.6841 0.9522 1.3345 0.1010  -0.1849 0.0596  1540 PHE B CE1   
6208 C  CE2   . PHE B 323 ? 0.7797 1.0396 1.4554 0.1023  -0.1451 0.0538  1540 PHE B CE2   
6209 C  CZ    . PHE B 323 ? 0.7551 1.0248 1.4339 0.1076  -0.1666 0.0618  1540 PHE B CZ    
6210 N  N     . VAL B 324 ? 0.9143 1.1372 1.4495 0.0497  -0.1662 0.0157  1541 VAL B N     
6211 C  CA    . VAL B 324 ? 0.8515 1.0584 1.3502 0.0429  -0.1643 0.0091  1541 VAL B CA    
6212 C  C     . VAL B 324 ? 1.0502 1.2582 1.5307 0.0399  -0.1841 0.0080  1541 VAL B C     
6213 O  O     . VAL B 324 ? 1.1300 1.3246 1.5777 0.0410  -0.1871 0.0078  1541 VAL B O     
6214 C  CB    . VAL B 324 ? 0.7329 0.9385 1.2363 0.0345  -0.1524 0.0025  1541 VAL B CB    
6215 C  CG1   . VAL B 324 ? 0.6056 0.7932 1.0709 0.0292  -0.1485 -0.0033 1541 VAL B CG1   
6216 C  CG2   . VAL B 324 ? 0.6803 0.8864 1.2040 0.0376  -0.1332 0.0036  1541 VAL B CG2   
6217 N  N     . LYS B 325 ? 1.1087 1.3328 1.6105 0.0361  -0.1979 0.0073  1542 LYS B N     
6218 C  CA    . LYS B 325 ? 1.1318 1.3565 1.6158 0.0325  -0.2174 0.0051  1542 LYS B CA    
6219 C  C     . LYS B 325 ? 1.0274 1.2508 1.4973 0.0410  -0.2298 0.0122  1542 LYS B C     
6220 O  O     . LYS B 325 ? 1.0177 1.2352 1.4607 0.0393  -0.2428 0.0103  1542 LYS B O     
6221 C  CB    . LYS B 325 ? 1.2119 1.4544 1.7250 0.0255  -0.2292 0.0021  1542 LYS B CB    
6222 C  CG    . LYS B 325 ? 1.2455 1.4850 1.7647 0.0158  -0.2171 -0.0053 1542 LYS B CG    
6223 C  CD    . LYS B 325 ? 1.2139 1.4695 1.7630 0.0073  -0.2269 -0.0087 1542 LYS B CD    
6224 C  CE    . LYS B 325 ? 1.1368 1.3884 1.6950 -0.0008 -0.2106 -0.0138 1542 LYS B CE    
6225 N  NZ    . LYS B 325 ? 1.1318 1.4000 1.7256 -0.0093 -0.2170 -0.0162 1542 LYS B NZ    
6226 N  N     . ALA B 326 ? 1.0348 1.2628 1.5218 0.0503  -0.2256 0.0204  1543 ALA B N     
6227 C  CA    . ALA B 326 ? 0.9961 1.2186 1.4664 0.0592  -0.2336 0.0283  1543 ALA B CA    
6228 C  C     . ALA B 326 ? 0.9436 1.1444 1.3802 0.0614  -0.2207 0.0283  1543 ALA B C     
6229 O  O     . ALA B 326 ? 0.9321 1.1260 1.3545 0.0689  -0.2239 0.0356  1543 ALA B O     
6230 C  CB    . ALA B 326 ? 1.0040 1.2393 1.5077 0.0690  -0.2340 0.0379  1543 ALA B CB    
6231 N  N     . GLY B 327 ? 0.8414 1.0316 1.2661 0.0553  -0.2062 0.0211  1544 GLY B N     
6232 C  CA    . GLY B 327 ? 0.7073 0.8787 1.1036 0.0567  -0.1943 0.0209  1544 GLY B CA    
6233 C  C     . GLY B 327 ? 0.8601 1.0259 1.2680 0.0625  -0.1785 0.0247  1544 GLY B C     
6234 O  O     . GLY B 327 ? 0.7414 0.8917 1.1275 0.0637  -0.1693 0.0250  1544 GLY B O     
6235 N  N     . ILE B 328 ? 0.9461 1.1240 1.3884 0.0662  -0.1749 0.0275  1545 ILE B N     
6236 C  CA    . ILE B 328 ? 0.9356 1.1069 1.3897 0.0719  -0.1584 0.0300  1545 ILE B CA    
6237 C  C     . ILE B 328 ? 0.9392 1.1069 1.3966 0.0654  -0.1424 0.0220  1545 ILE B C     
6238 O  O     . ILE B 328 ? 0.9191 1.0983 1.3932 0.0601  -0.1434 0.0182  1545 ILE B O     
6239 C  CB    . ILE B 328 ? 0.8402 1.0259 1.3304 0.0806  -0.1616 0.0378  1545 ILE B CB    
6240 C  CG1   . ILE B 328 ? 0.7953 0.9811 1.2794 0.0889  -0.1754 0.0474  1545 ILE B CG1   
6241 C  CG2   . ILE B 328 ? 0.8058 0.9859 1.3129 0.0852  -0.1419 0.0379  1545 ILE B CG2   
6242 C  CD1   . ILE B 328 ? 0.9522 1.1597 1.4680 0.0938  -0.1906 0.0538  1545 ILE B CD1   
6243 N  N     . ARG B 329 ? 0.8176 0.9688 1.2584 0.0656  -0.1278 0.0196  1546 ARG B N     
6244 C  CA    . ARG B 329 ? 0.6780 0.8236 1.1169 0.0598  -0.1126 0.0123  1546 ARG B CA    
6245 C  C     . ARG B 329 ? 0.7380 0.8903 1.2084 0.0644  -0.1009 0.0137  1546 ARG B C     
6246 O  O     . ARG B 329 ? 1.0458 1.1881 1.5180 0.0699  -0.0892 0.0151  1546 ARG B O     
6247 C  CB    . ARG B 329 ? 0.5220 0.6481 0.9311 0.0576  -0.1029 0.0088  1546 ARG B CB    
6248 C  CG    . ARG B 329 ? 0.5386 0.6585 0.9180 0.0528  -0.1117 0.0069  1546 ARG B CG    
6249 C  CD    . ARG B 329 ? 0.5831 0.6866 0.9380 0.0493  -0.1010 0.0025  1546 ARG B CD    
6250 N  NE    . ARG B 329 ? 0.7125 0.8048 1.0655 0.0545  -0.0936 0.0056  1546 ARG B NE    
6251 C  CZ    . ARG B 329 ? 0.7987 0.8870 1.1458 0.0594  -0.0998 0.0121  1546 ARG B CZ    
6252 N  NH1   . ARG B 329 ? 0.6730 0.7679 1.0134 0.0601  -0.1138 0.0158  1546 ARG B NH1   
6253 N  NH2   . ARG B 329 ? 0.8315 0.9080 1.1782 0.0638  -0.0916 0.0148  1546 ARG B NH2   
6254 N  N     . CYS B 330 ? 0.6918 0.8601 1.1875 0.0617  -0.1030 0.0129  1547 CYS B N     
6255 C  CA    . CYS B 330 ? 0.7195 0.8968 1.2488 0.0660  -0.0915 0.0147  1547 CYS B CA    
6256 C  C     . CYS B 330 ? 0.7555 0.9338 1.2890 0.0586  -0.0794 0.0084  1547 CYS B C     
6257 O  O     . CYS B 330 ? 0.8729 1.0579 1.4046 0.0510  -0.0870 0.0056  1547 CYS B O     
6258 C  CB    . CYS B 330 ? 0.6114 0.8106 1.1754 0.0706  -0.1048 0.0213  1547 CYS B CB    
6259 S  SG    . CYS B 330 ? 0.7409 0.9569 1.3529 0.0740  -0.0914 0.0232  1547 CYS B SG    
6260 N  N     . GLU B 331 ? 0.7323 0.9030 1.2711 0.0612  -0.0601 0.0065  1548 GLU B N     
6261 C  CA    . GLU B 331 ? 0.7451 0.9177 1.2927 0.0560  -0.0462 0.0023  1548 GLU B CA    
6262 C  C     . GLU B 331 ? 0.7907 0.9732 1.3752 0.0633  -0.0340 0.0059  1548 GLU B C     
6263 O  O     . GLU B 331 ? 0.8088 0.9874 1.4006 0.0723  -0.0302 0.0094  1548 GLU B O     
6264 C  CB    . GLU B 331 ? 0.4758 0.6273 0.9885 0.0514  -0.0330 -0.0045 1548 GLU B CB    
6265 N  N     . GLY B 332 ? 0.7208 0.9159 1.3300 0.0596  -0.0270 0.0054  1549 GLY B N     
6266 C  CA    . GLY B 332 ? 0.5930 0.7990 1.2398 0.0660  -0.0132 0.0087  1549 GLY B CA    
6267 C  C     . GLY B 332 ? 0.6072 0.8001 1.2440 0.0638  0.0107  0.0036  1549 GLY B C     
6268 O  O     . GLY B 332 ? 0.6968 0.8793 1.3065 0.0554  0.0136  -0.0015 1549 GLY B O     
6269 N  N     . ASP B 333 ? 0.6761 0.8679 1.3321 0.0718  0.0281  0.0049  1550 ASP B N     
6270 C  CA    . ASP B 333 ? 0.8578 1.0353 1.5024 0.0709  0.0526  -0.0001 1550 ASP B CA    
6271 C  C     . ASP B 333 ? 0.9421 1.1380 1.6275 0.0711  0.0646  0.0030  1550 ASP B C     
6272 O  O     . ASP B 333 ? 0.9900 1.1951 1.7089 0.0801  0.0741  0.0070  1550 ASP B O     
6273 C  CB    . ASP B 333 ? 1.0217 1.1803 1.6537 0.0797  0.0663  -0.0022 1550 ASP B CB    
6274 C  CG    . ASP B 333 ? 1.0804 1.2187 1.6872 0.0775  0.0893  -0.0093 1550 ASP B CG    
6275 O  OD1   . ASP B 333 ? 1.0715 1.2140 1.6820 0.0719  0.0991  -0.0105 1550 ASP B OD1   
6276 O  OD2   . ASP B 333 ? 1.0884 1.2057 1.6713 0.0814  0.0976  -0.0136 1550 ASP B OD2   
6277 N  N     . TYR B 334 ? 0.9971 1.1968 1.6793 0.0613  0.0662  0.0012  1551 TYR B N     
6278 C  CA    . TYR B 334 ? 1.0095 1.2268 1.7303 0.0594  0.0775  0.0043  1551 TYR B CA    
6279 C  C     . TYR B 334 ? 1.0600 1.2622 1.7649 0.0572  0.1037  0.0004  1551 TYR B C     
6280 O  O     . TYR B 334 ? 1.2639 1.4758 1.9880 0.0518  0.1130  0.0020  1551 TYR B O     
6281 C  CB    . TYR B 334 ? 0.9104 1.1446 1.6448 0.0494  0.0599  0.0060  1551 TYR B CB    
6282 C  CG    . TYR B 334 ? 0.8344 1.0775 1.5685 0.0493  0.0321  0.0079  1551 TYR B CG    
6283 C  CD1   . TYR B 334 ? 0.7868 1.0491 1.5568 0.0568  0.0211  0.0138  1551 TYR B CD1   
6284 C  CD2   . TYR B 334 ? 0.8735 1.1055 1.5706 0.0421  0.0171  0.0041  1551 TYR B CD2   
6285 C  CE1   . TYR B 334 ? 0.8436 1.1129 1.6103 0.0570  -0.0043 0.0159  1551 TYR B CE1   
6286 C  CE2   . TYR B 334 ? 0.8536 1.0926 1.5482 0.0422  -0.0072 0.0057  1551 TYR B CE2   
6287 C  CZ    . TYR B 334 ? 0.9207 1.1779 1.6488 0.0495  -0.0178 0.0116  1551 TYR B CZ    
6288 O  OH    . TYR B 334 ? 0.9541 1.2174 1.6773 0.0500  -0.0418 0.0136  1551 TYR B OH    
6289 N  N     . ARG B 335 ? 0.9290 1.1067 1.5977 0.0608  0.1156  -0.0047 1552 ARG B N     
6290 C  CA    . ARG B 335 ? 0.8965 1.0578 1.5452 0.0590  0.1400  -0.0088 1552 ARG B CA    
6291 C  C     . ARG B 335 ? 1.0148 1.1844 1.7000 0.0669  0.1624  -0.0060 1552 ARG B C     
6292 O  O     . ARG B 335 ? 1.0808 1.2534 1.7858 0.0771  0.1648  -0.0043 1552 ARG B O     
6293 C  CB    . ARG B 335 ? 0.9384 1.0711 1.5366 0.0599  0.1444  -0.0159 1552 ARG B CB    
6294 C  CG    . ARG B 335 ? 0.8708 0.9948 1.4317 0.0514  0.1260  -0.0187 1552 ARG B CG    
6295 C  CD    . ARG B 335 ? 0.8388 0.9376 1.3558 0.0525  0.1281  -0.0253 1552 ARG B CD    
6296 N  NE    . ARG B 335 ? 1.0091 1.1075 1.5321 0.0595  0.1180  -0.0246 1552 ARG B NE    
6297 C  CZ    . ARG B 335 ? 1.0426 1.1206 1.5385 0.0627  0.1221  -0.0298 1552 ARG B CZ    
6298 N  NH1   . ARG B 335 ? 1.0585 1.1155 1.5186 0.0593  0.1350  -0.0366 1552 ARG B NH1   
6299 N  NH2   . ARG B 335 ? 0.9978 1.0755 1.5016 0.0689  0.1131  -0.0281 1552 ARG B NH2   
6300 N  N     . ASP B 336 ? 1.1134 1.2855 1.8070 0.0625  0.1800  -0.0052 1553 ASP B N     
6301 C  CA    . ASP B 336 ? 1.2194 1.4041 1.9551 0.0692  0.2011  -0.0014 1553 ASP B CA    
6302 C  C     . ASP B 336 ? 1.1916 1.3533 1.9052 0.0766  0.2278  -0.0064 1553 ASP B C     
6303 O  O     . ASP B 336 ? 1.1925 1.3618 1.9396 0.0858  0.2449  -0.0039 1553 ASP B O     
6304 C  CB    . ASP B 336 ? 1.3052 1.5047 2.0647 0.0608  0.2090  0.0026  1553 ASP B CB    
6305 C  CG    . ASP B 336 ? 1.2969 1.5196 2.0821 0.0529  0.1833  0.0069  1553 ASP B CG    
6306 O  OD1   . ASP B 336 ? 1.2926 1.5117 2.0602 0.0422  0.1779  0.0061  1553 ASP B OD1   
6307 O  OD2   . ASP B 336 ? 1.2711 1.5146 2.0929 0.0576  0.1682  0.0110  1553 ASP B OD2   
6308 N  N     . ASN B 337 ? 1.1568 1.2906 1.8151 0.0731  0.2310  -0.0136 1554 ASN B N     
6309 C  CA    . ASN B 337 ? 1.1525 1.2608 1.7810 0.0779  0.2560  -0.0200 1554 ASN B CA    
6310 C  C     . ASN B 337 ? 1.1276 1.2191 1.7386 0.0860  0.2534  -0.0252 1554 ASN B C     
6311 O  O     . ASN B 337 ? 1.1209 1.1850 1.6876 0.0859  0.2635  -0.0331 1554 ASN B O     
6312 C  CB    . ASN B 337 ? 1.2745 1.3617 1.8519 0.0687  0.2614  -0.0248 1554 ASN B CB    
6313 C  CG    . ASN B 337 ? 1.3177 1.4180 1.9099 0.0606  0.2663  -0.0193 1554 ASN B CG    
6314 O  OD1   . ASN B 337 ? 1.2315 1.3578 1.8731 0.0605  0.2638  -0.0124 1554 ASN B OD1   
6315 N  ND2   . ASN B 337 ? 1.3528 1.4348 1.9022 0.0535  0.2728  -0.0221 1554 ASN B ND2   
6316 N  N     . TYR B 338 ? 1.1587 1.2656 1.8023 0.0926  0.2390  -0.0207 1555 TYR B N     
6317 C  CA    . TYR B 338 ? 1.1008 1.1928 1.7333 0.1008  0.2365  -0.0242 1555 TYR B CA    
6318 C  C     . TYR B 338 ? 1.0522 1.1637 1.7377 0.1125  0.2371  -0.0171 1555 TYR B C     
6319 O  O     . TYR B 338 ? 1.0505 1.1902 1.7756 0.1119  0.2224  -0.0090 1555 TYR B O     
6320 C  CB    . TYR B 338 ? 1.0864 1.1720 1.6896 0.0954  0.2102  -0.0260 1555 TYR B CB    
6321 C  CG    . TYR B 338 ? 1.0613 1.1261 1.6112 0.0853  0.2086  -0.0332 1555 TYR B CG    
6322 C  CD1   . TYR B 338 ? 1.0402 1.1132 1.5777 0.0755  0.1886  -0.0314 1555 TYR B CD1   
6323 C  CD2   . TYR B 338 ? 1.0010 1.0380 1.5130 0.0859  0.2267  -0.0418 1555 TYR B CD2   
6324 C  CE1   . TYR B 338 ? 1.0247 1.0802 1.5159 0.0671  0.1866  -0.0371 1555 TYR B CE1   
6325 C  CE2   . TYR B 338 ? 1.0368 1.0563 1.5007 0.0767  0.2235  -0.0479 1555 TYR B CE2   
6326 C  CZ    . TYR B 338 ? 1.0617 1.0913 1.5166 0.0676  0.2033  -0.0449 1555 TYR B CZ    
6327 O  OH    . TYR B 338 ? 1.0462 1.0600 1.4556 0.0592  0.1992  -0.0499 1555 TYR B OH    
6328 N  N     . SER B 339 ? 1.0615 1.1575 1.7474 0.1232  0.2532  -0.0201 1556 SER B N     
6329 C  CA    . SER B 339 ? 1.0781 1.1906 1.8125 0.1357  0.2528  -0.0128 1556 SER B CA    
6330 C  C     . SER B 339 ? 1.2569 1.3791 1.9967 0.1360  0.2228  -0.0077 1556 SER B C     
6331 O  O     . SER B 339 ? 1.3368 1.4431 2.0358 0.1295  0.2086  -0.0123 1556 SER B O     
6332 C  CB    . SER B 339 ? 1.0353 1.1244 1.7634 0.1471  0.2766  -0.0180 1556 SER B CB    
6333 O  OG    . SER B 339 ? 1.0920 1.1859 1.8468 0.1585  0.2684  -0.0126 1556 SER B OG    
6334 N  N     . PRO B 340 ? 1.3095 1.4593 2.0995 0.1429  0.2120  0.0022  1557 PRO B N     
6335 C  CA    . PRO B 340 ? 1.2931 1.4499 2.0869 0.1452  0.1852  0.0076  1557 PRO B CA    
6336 C  C     . PRO B 340 ? 1.2638 1.3921 2.0258 0.1508  0.1860  0.0034  1557 PRO B C     
6337 O  O     . PRO B 340 ? 1.3300 1.4508 2.0642 0.1457  0.1662  0.0027  1557 PRO B O     
6338 C  CB    . PRO B 340 ? 1.2970 1.4848 2.1530 0.1552  0.1812  0.0187  1557 PRO B CB    
6339 C  CG    . PRO B 340 ? 1.3602 1.5659 2.2434 0.1509  0.1953  0.0195  1557 PRO B CG    
6340 C  CD    . PRO B 340 ? 1.3728 1.5515 2.2172 0.1465  0.2206  0.0094  1557 PRO B CD    
6341 N  N     . GLY B 341 ? 1.1978 1.3096 1.9642 0.1611  0.2090  0.0005  1558 GLY B N     
6342 C  CA    . GLY B 341 ? 1.1225 1.2053 1.8598 0.1660  0.2111  -0.0041 1558 GLY B CA    
6343 C  C     . GLY B 341 ? 1.1537 1.2096 1.8321 0.1541  0.2097  -0.0151 1558 GLY B C     
6344 O  O     . GLY B 341 ? 1.2344 1.2737 1.8858 0.1525  0.1981  -0.0173 1558 GLY B O     
6345 N  N     . TRP B 342 ? 1.0182 1.0692 1.6766 0.1459  0.2223  -0.0219 1559 TRP B N     
6346 C  CA    . TRP B 342 ? 0.9728 1.0035 1.5777 0.1335  0.2177  -0.0311 1559 TRP B CA    
6347 C  C     . TRP B 342 ? 0.8693 0.9103 1.4631 0.1255  0.1884  -0.0273 1559 TRP B C     
6348 O  O     . TRP B 342 ? 0.8910 0.9134 1.4477 0.1202  0.1795  -0.0325 1559 TRP B O     
6349 C  CB    . TRP B 342 ? 1.0603 1.0914 1.6530 0.1263  0.2324  -0.0355 1559 TRP B CB    
6350 C  CG    . TRP B 342 ? 1.1469 1.1558 1.6849 0.1152  0.2308  -0.0449 1559 TRP B CG    
6351 C  CD1   . TRP B 342 ? 1.2018 1.1828 1.7033 0.1139  0.2496  -0.0552 1559 TRP B CD1   
6352 C  CD2   . TRP B 342 ? 1.1986 1.2116 1.7120 0.1038  0.2087  -0.0448 1559 TRP B CD2   
6353 N  NE1   . TRP B 342 ? 1.2585 1.2270 1.7149 0.1024  0.2395  -0.0612 1559 TRP B NE1   
6354 C  CE2   . TRP B 342 ? 1.2130 1.2010 1.6770 0.0964  0.2150  -0.0548 1559 TRP B CE2   
6355 C  CE3   . TRP B 342 ? 1.2224 1.2574 1.7503 0.0993  0.1845  -0.0376 1559 TRP B CE3   
6356 C  CZ2   . TRP B 342 ? 1.1860 1.1717 1.6177 0.0853  0.1980  -0.0568 1559 TRP B CZ2   
6357 C  CZ3   . TRP B 342 ? 1.1825 1.2134 1.6766 0.0884  0.1689  -0.0403 1559 TRP B CZ3   
6358 C  CH2   . TRP B 342 ? 1.1133 1.1205 1.5614 0.0818  0.1758  -0.0495 1559 TRP B CH2   
6359 N  N     . LYS B 343 ? 0.8077 0.8782 1.4339 0.1244  0.1733  -0.0184 1560 LYS B N     
6360 C  CA    . LYS B 343 ? 0.9103 0.9903 1.5259 0.1173  0.1463  -0.0150 1560 LYS B CA    
6361 C  C     . LYS B 343 ? 0.8964 0.9709 1.5131 0.1241  0.1333  -0.0109 1560 LYS B C     
6362 O  O     . LYS B 343 ? 0.8512 0.9163 1.4381 0.1181  0.1183  -0.0126 1560 LYS B O     
6363 C  CB    . LYS B 343 ? 0.9245 1.0361 1.5743 0.1144  0.1338  -0.0074 1560 LYS B CB    
6364 C  CG    . LYS B 343 ? 0.9480 1.0642 1.5929 0.1055  0.1437  -0.0108 1560 LYS B CG    
6365 C  CD    . LYS B 343 ? 0.9048 1.0516 1.5850 0.1016  0.1302  -0.0036 1560 LYS B CD    
6366 C  CE    . LYS B 343 ? 0.8450 0.9955 1.5251 0.0938  0.1435  -0.0060 1560 LYS B CE    
6367 N  NZ    . LYS B 343 ? 0.8928 1.0724 1.6245 0.0950  0.1440  0.0012  1560 LYS B NZ    
6368 N  N     . TYR B 344 ? 0.8196 0.9001 1.4714 0.1367  0.1392  -0.0047 1561 TYR B N     
6369 C  CA    . TYR B 344 ? 0.9000 0.9723 1.5522 0.1442  0.1293  0.0000  1561 TYR B CA    
6370 C  C     . TYR B 344 ? 0.9729 1.0122 1.5799 0.1403  0.1348  -0.0091 1561 TYR B C     
6371 O  O     . TYR B 344 ? 0.9315 0.9638 1.5168 0.1363  0.1188  -0.0082 1561 TYR B O     
6372 C  CB    . TYR B 344 ? 0.9408 1.0185 1.6342 0.1596  0.1405  0.0067  1561 TYR B CB    
6373 C  CG    . TYR B 344 ? 0.9896 1.1018 1.7347 0.1655  0.1330  0.0174  1561 TYR B CG    
6374 C  CD1   . TYR B 344 ? 0.9226 1.0595 1.6770 0.1566  0.1172  0.0201  1561 TYR B CD1   
6375 C  CD2   . TYR B 344 ? 1.0015 1.1215 1.7878 0.1803  0.1416  0.0248  1561 TYR B CD2   
6376 C  CE1   . TYR B 344 ? 0.8953 1.0640 1.6985 0.1612  0.1095  0.0294  1561 TYR B CE1   
6377 C  CE2   . TYR B 344 ? 0.9757 1.1289 1.8120 0.1859  0.1341  0.0348  1561 TYR B CE2   
6378 C  CZ    . TYR B 344 ? 1.0100 1.1876 1.8546 0.1758  0.1177  0.0369  1561 TYR B CZ    
6379 O  OH    . TYR B 344 ? 1.0787 1.2897 1.9748 0.1807  0.1093  0.0464  1561 TYR B OH    
6380 N  N     . ASN B 345 ? 0.8984 0.9169 1.4899 0.1407  0.1577  -0.0184 1562 ASN B N     
6381 C  CA    . ASN B 345 ? 0.8119 0.7982 1.3619 0.1368  0.1636  -0.0281 1562 ASN B CA    
6382 C  C     . ASN B 345 ? 0.8648 0.8466 1.3756 0.1225  0.1502  -0.0336 1562 ASN B C     
6383 O  O     . ASN B 345 ? 1.0728 1.0378 1.5565 0.1183  0.1423  -0.0368 1562 ASN B O     
6384 C  CB    . ASN B 345 ? 0.9716 0.9370 1.5119 0.1398  0.1910  -0.0377 1562 ASN B CB    
6385 C  CG    . ASN B 345 ? 1.0722 1.0034 1.5678 0.1343  0.1969  -0.0493 1562 ASN B CG    
6386 O  OD1   . ASN B 345 ? 1.1257 1.0448 1.5873 0.1248  0.2026  -0.0589 1562 ASN B OD1   
6387 N  ND2   . ASN B 345 ? 1.0606 0.9759 1.5563 0.1401  0.1954  -0.0483 1562 ASN B ND2   
6388 N  N     . HIS B 346 ? 0.7876 0.7841 1.2960 0.1150  0.1479  -0.0344 1563 HIS B N     
6389 C  CA    . HIS B 346 ? 0.7864 0.7800 1.2598 0.1023  0.1355  -0.0388 1563 HIS B CA    
6390 C  C     . HIS B 346 ? 0.7646 0.7661 1.2360 0.1000  0.1119  -0.0328 1563 HIS B C     
6391 O  O     . HIS B 346 ? 0.7629 0.7491 1.2036 0.0940  0.1048  -0.0370 1563 HIS B O     
6392 C  CB    . HIS B 346 ? 0.8895 0.9004 1.3698 0.0967  0.1371  -0.0380 1563 HIS B CB    
6393 C  CG    . HIS B 346 ? 0.8217 0.8315 1.2698 0.0846  0.1256  -0.0416 1563 HIS B CG    
6394 N  ND1   . HIS B 346 ? 0.8190 0.8086 1.2285 0.0777  0.1340  -0.0510 1563 HIS B ND1   
6395 C  CD2   . HIS B 346 ? 0.7664 0.7934 1.2165 0.0785  0.1070  -0.0370 1563 HIS B CD2   
6396 C  CE1   . HIS B 346 ? 0.8200 0.8151 1.2105 0.0684  0.1207  -0.0512 1563 HIS B CE1   
6397 N  NE2   . HIS B 346 ? 0.8033 0.8202 1.2176 0.0688  0.1049  -0.0431 1563 HIS B NE2   
6398 N  N     . TRP B 347 ? 0.7359 0.7613 1.2400 0.1046  0.0996  -0.0227 1564 TRP B N     
6399 C  CA    . TRP B 347 ? 0.7341 0.7673 1.2346 0.1026  0.0773  -0.0167 1564 TRP B CA    
6400 C  C     . TRP B 347 ? 0.8728 0.8916 1.3717 0.1096  0.0755  -0.0137 1564 TRP B C     
6401 O  O     . TRP B 347 ? 1.0390 1.0573 1.5252 0.1068  0.0598  -0.0102 1564 TRP B O     
6402 C  CB    . TRP B 347 ? 0.7759 0.8384 1.3088 0.1046  0.0636  -0.0077 1564 TRP B CB    
6403 C  CG    . TRP B 347 ? 0.7768 0.8516 1.3103 0.0966  0.0655  -0.0107 1564 TRP B CG    
6404 C  CD1   . TRP B 347 ? 0.6595 0.7497 1.2232 0.0990  0.0749  -0.0088 1564 TRP B CD1   
6405 C  CD2   . TRP B 347 ? 0.8181 0.8894 1.3208 0.0851  0.0590  -0.0160 1564 TRP B CD2   
6406 N  NE1   . TRP B 347 ? 0.7511 0.8469 1.3042 0.0894  0.0746  -0.0122 1564 TRP B NE1   
6407 C  CE2   . TRP B 347 ? 0.7735 0.8576 1.2889 0.0811  0.0648  -0.0166 1564 TRP B CE2   
6408 C  CE3   . TRP B 347 ? 0.6853 0.7444 1.1528 0.0781  0.0491  -0.0196 1564 TRP B CE3   
6409 C  CZ2   . TRP B 347 ? 0.8354 0.9190 1.3282 0.0708  0.0609  -0.0205 1564 TRP B CZ2   
6410 C  CZ3   . TRP B 347 ? 0.7563 0.8167 1.2029 0.0682  0.0448  -0.0236 1564 TRP B CZ3   
6411 C  CH2   . TRP B 347 ? 0.8178 0.8896 1.2763 0.0649  0.0507  -0.0239 1564 TRP B CH2   
6412 N  N     . GLU B 348 ? 0.8884 0.8950 1.4004 0.1188  0.0919  -0.0144 1565 GLU B N     
6413 C  CA    . GLU B 348 ? 0.8223 0.8082 1.3260 0.1239  0.0934  -0.0136 1565 GLU B CA    
6414 C  C     . GLU B 348 ? 0.8354 0.7964 1.2969 0.1139  0.0960  -0.0240 1565 GLU B C     
6415 O  O     . GLU B 348 ? 0.7447 0.6974 1.1906 0.1109  0.0851  -0.0221 1565 GLU B O     
6416 C  CB    . GLU B 348 ? 0.7559 0.7325 1.2828 0.1361  0.1122  -0.0130 1565 GLU B CB    
6417 C  CG    . GLU B 348 ? 0.9826 0.9779 1.5512 0.1489  0.1061  0.0000  1565 GLU B CG    
6418 C  CD    . GLU B 348 ? 1.0929 1.0761 1.6835 0.1618  0.1259  0.0005  1565 GLU B CD    
6419 O  OE1   . GLU B 348 ? 1.0077 0.9618 1.5750 0.1609  0.1408  -0.0087 1565 GLU B OE1   
6420 O  OE2   . GLU B 348 ? 1.2037 1.2060 1.8349 0.1728  0.1267  0.0096  1565 GLU B OE2   
6421 N  N     . LEU B 349 ? 0.7750 0.7241 1.2179 0.1085  0.1104  -0.0348 1566 LEU B N     
6422 C  CA    . LEU B 349 ? 0.7645 0.6921 1.1671 0.0980  0.1118  -0.0453 1566 LEU B CA    
6423 C  C     . LEU B 349 ? 0.7146 0.6515 1.0984 0.0878  0.0922  -0.0438 1566 LEU B C     
6424 O  O     . LEU B 349 ? 0.7565 0.6789 1.1166 0.0818  0.0868  -0.0474 1566 LEU B O     
6425 C  CB    . LEU B 349 ? 0.8078 0.7265 1.1940 0.0938  0.1279  -0.0557 1566 LEU B CB    
6426 C  CG    . LEU B 349 ? 0.9293 0.8281 1.3182 0.1009  0.1509  -0.0621 1566 LEU B CG    
6427 C  CD1   . LEU B 349 ? 0.9699 0.8668 1.3448 0.0968  0.1647  -0.0698 1566 LEU B CD1   
6428 C  CD2   . LEU B 349 ? 0.8498 0.7185 1.2146 0.0990  0.1552  -0.0699 1566 LEU B CD2   
6429 N  N     . LYS B 350 ? 0.7912 0.7518 1.1853 0.0854  0.0822  -0.0390 1567 LYS B N     
6430 C  CA    . LYS B 350 ? 0.7496 0.7192 1.1267 0.0765  0.0649  -0.0378 1567 LYS B CA    
6431 C  C     . LYS B 350 ? 0.7069 0.6835 1.0923 0.0795  0.0490  -0.0288 1567 LYS B C     
6432 O  O     . LYS B 350 ? 0.7414 0.7217 1.1103 0.0726  0.0358  -0.0280 1567 LYS B O     
6433 C  CB    . LYS B 350 ? 0.8252 0.8153 1.2100 0.0729  0.0607  -0.0363 1567 LYS B CB    
6434 C  CG    . LYS B 350 ? 0.7958 0.7780 1.1597 0.0662  0.0720  -0.0452 1567 LYS B CG    
6435 C  CD    . LYS B 350 ? 0.7510 0.7525 1.1238 0.0627  0.0675  -0.0424 1567 LYS B CD    
6436 C  CE    . LYS B 350 ? 0.8129 0.8109 1.1547 0.0524  0.0611  -0.0472 1567 LYS B CE    
6437 N  NZ    . LYS B 350 ? 0.5773 0.5936 0.9275 0.0485  0.0542  -0.0436 1567 LYS B NZ    
6438 N  N     . GLY B 351 ? 0.7112 0.6896 1.1214 0.0899  0.0505  -0.0214 1568 GLY B N     
6439 C  CA    . GLY B 351 ? 0.7786 0.7588 1.1929 0.0936  0.0374  -0.0126 1568 GLY B CA    
6440 C  C     . GLY B 351 ? 0.8082 0.8131 1.2392 0.0957  0.0205  -0.0032 1568 GLY B C     
6441 O  O     . GLY B 351 ? 0.8221 0.8282 1.2457 0.0954  0.0074  0.0028  1568 GLY B O     
6442 N  N     . VAL B 352 ? 0.7300 0.7540 1.1834 0.0977  0.0206  -0.0015 1569 VAL B N     
6443 C  CA    . VAL B 352 ? 0.7017 0.7491 1.1699 0.0982  0.0034  0.0060  1569 VAL B CA    
6444 C  C     . VAL B 352 ? 0.8157 0.8676 1.3041 0.1090  -0.0042 0.0170  1569 VAL B C     
6445 O  O     . VAL B 352 ? 0.8582 0.9098 1.3714 0.1186  0.0052  0.0203  1569 VAL B O     
6446 C  CB    . VAL B 352 ? 0.6944 0.7608 1.1845 0.0972  0.0061  0.0049  1569 VAL B CB    
6447 C  CG1   . VAL B 352 ? 0.5643 0.6542 1.0688 0.0963  -0.0132 0.0116  1569 VAL B CG1   
6448 C  CG2   . VAL B 352 ? 0.7236 0.7829 1.1918 0.0873  0.0152  -0.0051 1569 VAL B CG2   
6449 N  N     . PRO B 353 ? 0.8249 0.8805 1.3028 0.1081  -0.0207 0.0230  1570 PRO B N     
6450 C  CA    . PRO B 353 ? 0.7020 0.7590 1.1937 0.1184  -0.0287 0.0344  1570 PRO B CA    
6451 C  C     . PRO B 353 ? 0.6702 0.7457 1.2011 0.1287  -0.0305 0.0419  1570 PRO B C     
6452 O  O     . PRO B 353 ? 0.8066 0.8772 1.3528 0.1395  -0.0282 0.0497  1570 PRO B O     
6453 C  CB    . PRO B 353 ? 0.7887 0.8515 1.2612 0.1138  -0.0473 0.0385  1570 PRO B CB    
6454 C  CG    . PRO B 353 ? 0.7161 0.7692 1.1578 0.1017  -0.0442 0.0285  1570 PRO B CG    
6455 C  CD    . PRO B 353 ? 0.6882 0.7422 1.1365 0.0978  -0.0306 0.0194  1570 PRO B CD    
6456 N  N     . VAL B 354 ? 0.7498 0.8467 1.2990 0.1259  -0.0348 0.0405  1571 VAL B N     
6457 C  CA    . VAL B 354 ? 0.7373 0.8555 1.3272 0.1347  -0.0383 0.0480  1571 VAL B CA    
6458 C  C     . VAL B 354 ? 0.7676 0.8961 1.3765 0.1313  -0.0258 0.0414  1571 VAL B C     
6459 O  O     . VAL B 354 ? 0.6788 0.8109 1.2737 0.1206  -0.0269 0.0343  1571 VAL B O     
6460 C  CB    . VAL B 354 ? 0.6881 0.8274 1.2858 0.1348  -0.0622 0.0558  1571 VAL B CB    
6461 C  CG1   . VAL B 354 ? 0.7144 0.8802 1.3559 0.1400  -0.0665 0.0608  1571 VAL B CG1   
6462 C  CG2   . VAL B 354 ? 0.5342 0.6651 1.1206 0.1418  -0.0732 0.0653  1571 VAL B CG2   
6463 N  N     . ARG B 355 ? 0.8729 1.0068 1.5151 0.1409  -0.0139 0.0446  1572 ARG B N     
6464 C  CA    . ARG B 355 ? 0.8596 1.0079 1.5279 0.1395  -0.0028 0.0411  1572 ARG B CA    
6465 C  C     . ARG B 355 ? 0.7875 0.9656 1.4982 0.1453  -0.0161 0.0505  1572 ARG B C     
6466 O  O     . ARG B 355 ? 0.8019 0.9849 1.5317 0.1563  -0.0231 0.0602  1572 ARG B O     
6467 C  CB    . ARG B 355 ? 1.0130 1.1465 1.6902 0.1462  0.0224  0.0373  1572 ARG B CB    
6468 C  CG    . ARG B 355 ? 1.1460 1.2506 1.7834 0.1398  0.0369  0.0265  1572 ARG B CG    
6469 C  CD    . ARG B 355 ? 1.2125 1.3106 1.8596 0.1416  0.0615  0.0198  1572 ARG B CD    
6470 N  NE    . ARG B 355 ? 1.2060 1.2977 1.8780 0.1552  0.0755  0.0238  1572 ARG B NE    
6471 C  CZ    . ARG B 355 ? 1.1611 1.2734 1.8784 0.1655  0.0772  0.0320  1572 ARG B CZ    
6472 N  NH1   . ARG B 355 ? 1.1505 1.2923 1.8949 0.1631  0.0649  0.0371  1572 ARG B NH1   
6473 N  NH2   . ARG B 355 ? 1.1702 1.2733 1.9070 0.1784  0.0914  0.0350  1572 ARG B NH2   
6474 N  N     . ILE B 356 ? 0.8342 1.0322 1.5598 0.1377  -0.0205 0.0481  1573 ILE B N     
6475 C  CA    . ILE B 356 ? 0.7294 0.9577 1.4999 0.1418  -0.0319 0.0559  1573 ILE B CA    
6476 C  C     . ILE B 356 ? 0.6771 0.9146 1.4813 0.1442  -0.0112 0.0540  1573 ILE B C     
6477 O  O     . ILE B 356 ? 0.6008 0.8361 1.3963 0.1348  -0.0002 0.0460  1573 ILE B O     
6478 C  CB    . ILE B 356 ? 0.6919 0.9376 1.4592 0.1312  -0.0534 0.0553  1573 ILE B CB    
6479 C  CG1   . ILE B 356 ? 0.6320 0.8654 1.3594 0.1276  -0.0707 0.0555  1573 ILE B CG1   
6480 C  CG2   . ILE B 356 ? 0.6115 0.8881 1.4263 0.1366  -0.0673 0.0641  1573 ILE B CG2   
6481 C  CD1   . ILE B 356 ? 0.7242 0.9698 1.4634 0.1352  -0.0921 0.0660  1573 ILE B CD1   
6482 N  N     . GLU B 357 ? 0.7676 1.0144 1.6097 0.1574  -0.0054 0.0617  1574 GLU B N     
6483 C  CA    . GLU B 357 ? 0.6913 0.9538 1.5766 0.1619  0.0116  0.0627  1574 GLU B CA    
6484 C  C     . GLU B 357 ? 0.7452 1.0436 1.6730 0.1605  -0.0073 0.0698  1574 GLU B C     
6485 O  O     . GLU B 357 ? 0.8021 1.1152 1.7499 0.1681  -0.0264 0.0795  1574 GLU B O     
6486 C  CB    . GLU B 357 ? 0.6449 0.8977 1.5493 0.1775  0.0288  0.0671  1574 GLU B CB    
6487 C  CG    . GLU B 357 ? 0.7962 1.0117 1.6572 0.1776  0.0474  0.0587  1574 GLU B CG    
6488 C  CD    . GLU B 357 ? 0.9612 1.1622 1.8368 0.1930  0.0647  0.0621  1574 GLU B CD    
6489 O  OE1   . GLU B 357 ? 0.9717 1.1914 1.8946 0.2051  0.0673  0.0709  1574 GLU B OE1   
6490 O  OE2   . GLU B 357 ? 1.0208 1.1905 1.8600 0.1928  0.0761  0.0555  1574 GLU B OE2   
6491 N  N     . LEU B 358 ? 0.7951 1.1066 1.7350 0.1501  -0.0027 0.0649  1575 LEU B N     
6492 C  CA    . LEU B 358 ? 0.8310 1.1758 1.8102 0.1455  -0.0195 0.0695  1575 LEU B CA    
6493 C  C     . LEU B 358 ? 0.8226 1.1827 1.8432 0.1454  0.0015  0.0688  1575 LEU B C     
6494 O  O     . LEU B 358 ? 0.9177 1.2674 1.9216 0.1363  0.0180  0.0608  1575 LEU B O     
6495 C  CB    . LEU B 358 ? 0.8236 1.1681 1.7725 0.1302  -0.0377 0.0637  1575 LEU B CB    
6496 C  CG    . LEU B 358 ? 0.9335 1.3088 1.9141 0.1233  -0.0603 0.0670  1575 LEU B CG    
6497 C  CD1   . LEU B 358 ? 0.9926 1.3819 1.9875 0.1318  -0.0851 0.0766  1575 LEU B CD1   
6498 C  CD2   . LEU B 358 ? 0.9268 1.2950 1.8725 0.1076  -0.0711 0.0589  1575 LEU B CD2   
6499 N  N     . GLY B 359 ? 0.8281 1.2125 1.9027 0.1562  0.0018  0.0779  1576 GLY B N     
6500 C  CA    . GLY B 359 ? 0.8819 1.2851 2.0033 0.1572  0.0209  0.0790  1576 GLY B CA    
6501 C  C     . GLY B 359 ? 0.9713 1.4100 2.1360 0.1516  0.0018  0.0847  1576 GLY B C     
6502 O  O     . GLY B 359 ? 0.9582 1.4070 2.1148 0.1448  -0.0266 0.0860  1576 GLY B O     
6503 N  N     . PHE B 360 ? 1.0629 1.5148 2.2620 0.1526  0.0182  0.0870  1577 PHE B N     
6504 C  CA    . PHE B 360 ? 0.9837 1.4639 2.2144 0.1443  0.0026  0.0909  1577 PHE B CA    
6505 C  C     . PHE B 360 ? 0.9248 1.4199 2.1693 0.1520  -0.0220 0.1002  1577 PHE B C     
6506 O  O     . PHE B 360 ? 0.9713 1.4826 2.2181 0.1440  -0.0493 0.1016  1577 PHE B O     
6507 C  CB    . PHE B 360 ? 0.9068 1.3962 2.1705 0.1430  0.0284  0.0910  1577 PHE B CB    
6508 C  CG    . PHE B 360 ? 0.9692 1.4488 2.2207 0.1320  0.0478  0.0825  1577 PHE B CG    
6509 C  CD1   . PHE B 360 ? 1.0631 1.5472 2.3019 0.1168  0.0318  0.0776  1577 PHE B CD1   
6510 C  CD2   . PHE B 360 ? 1.0742 1.5386 2.3242 0.1370  0.0820  0.0793  1577 PHE B CD2   
6511 C  CE1   . PHE B 360 ? 1.0506 1.5252 2.2774 0.1068  0.0495  0.0704  1577 PHE B CE1   
6512 C  CE2   . PHE B 360 ? 1.1490 1.6037 2.3850 0.1271  0.1000  0.0720  1577 PHE B CE2   
6513 C  CZ    . PHE B 360 ? 1.0974 1.5578 2.3228 0.1120  0.0835  0.0680  1577 PHE B CZ    
6514 N  N     . LYS B 361 ? 0.8438 1.3322 2.0953 0.1676  -0.0127 0.1063  1578 LYS B N     
6515 C  CA    . LYS B 361 ? 0.8636 1.3638 2.1240 0.1761  -0.0362 0.1158  1578 LYS B CA    
6516 C  C     . LYS B 361 ? 0.8774 1.3691 2.1008 0.1733  -0.0630 0.1154  1578 LYS B C     
6517 O  O     . LYS B 361 ? 1.0492 1.5553 2.2756 0.1738  -0.0899 0.1214  1578 LYS B O     
6518 C  CB    . LYS B 361 ? 0.7408 1.2307 2.0112 0.1938  -0.0195 0.1222  1578 LYS B CB    
6519 N  N     . ASP B 362 ? 0.6936 1.1620 1.8814 0.1702  -0.0562 0.1082  1579 ASP B N     
6520 C  CA    . ASP B 362 ? 0.7761 1.2359 1.9284 0.1672  -0.0806 0.1076  1579 ASP B CA    
6521 C  C     . ASP B 362 ? 0.8958 1.3722 2.0459 0.1513  -0.1033 0.1037  1579 ASP B C     
6522 O  O     . ASP B 362 ? 0.9423 1.4267 2.0821 0.1499  -0.1310 0.1074  1579 ASP B O     
6523 C  CB    . ASP B 362 ? 0.7230 1.1538 1.8398 0.1683  -0.0666 0.1009  1579 ASP B CB    
6524 C  CG    . ASP B 362 ? 0.8550 1.2652 1.9687 0.1841  -0.0460 0.1042  1579 ASP B CG    
6525 O  OD1   . ASP B 362 ? 0.9697 1.3844 2.0975 0.1956  -0.0511 0.1136  1579 ASP B OD1   
6526 O  OD2   . ASP B 362 ? 0.8401 1.2242 1.9257 0.1831  -0.0243 0.0963  1579 ASP B OD2   
6527 N  N     . LEU B 363 ? 0.8760 1.3575 2.0362 0.1394  -0.0914 0.0963  1580 LEU B N     
6528 C  CA    . LEU B 363 ? 0.7933 1.2879 1.9510 0.1236  -0.1112 0.0916  1580 LEU B CA    
6529 C  C     . LEU B 363 ? 0.7449 1.2662 1.9336 0.1218  -0.1293 0.0975  1580 LEU B C     
6530 O  O     . LEU B 363 ? 0.7719 1.3027 1.9523 0.1117  -0.1540 0.0953  1580 LEU B O     
6531 C  CB    . LEU B 363 ? 0.7386 1.2308 1.9011 0.1118  -0.0918 0.0831  1580 LEU B CB    
6532 N  N     . GLN B 364 ? 0.7081 1.2411 1.9320 0.1314  -0.1173 0.1044  1581 GLN B N     
6533 C  CA    . GLN B 364 ? 0.7718 1.3319 2.0290 0.1310  -0.1338 0.1106  1581 GLN B CA    
6534 C  C     . GLN B 364 ? 0.8852 1.4493 2.1314 0.1401  -0.1596 0.1184  1581 GLN B C     
6535 O  O     . GLN B 364 ? 1.0120 1.5967 2.2714 0.1357  -0.1828 0.1212  1581 GLN B O     
6536 C  CB    . GLN B 364 ? 0.8316 1.4029 2.1318 0.1381  -0.1097 0.1150  1581 GLN B CB    
6537 C  CG    . GLN B 364 ? 0.9318 1.5240 2.2643 0.1485  -0.1205 0.1254  1581 GLN B CG    
6538 C  CD    . GLN B 364 ? 0.8863 1.4883 2.2610 0.1548  -0.0944 0.1290  1581 GLN B CD    
6539 O  OE1   . GLN B 364 ? 0.9055 1.5047 2.2899 0.1477  -0.0722 0.1235  1581 GLN B OE1   
6540 N  NE2   . GLN B 364 ? 0.7748 1.3882 2.1745 0.1684  -0.0967 0.1386  1581 GLN B NE2   
6541 N  N     . ASN B 365 ? 0.8964 1.4405 2.1170 0.1522  -0.1564 0.1219  1582 ASN B N     
6542 C  CA    . ASN B 365 ? 0.9398 1.4833 2.1428 0.1608  -0.1800 0.1296  1582 ASN B CA    
6543 C  C     . ASN B 365 ? 0.9351 1.4628 2.0908 0.1542  -0.1984 0.1249  1582 ASN B C     
6544 O  O     . ASN B 365 ? 0.9609 1.4828 2.0946 0.1617  -0.2156 0.1312  1582 ASN B O     
6545 C  CB    . ASN B 365 ? 1.0426 1.5726 2.2473 0.1791  -0.1653 0.1377  1582 ASN B CB    
6546 C  CG    . ASN B 365 ? 1.1390 1.6871 2.3894 0.1884  -0.1548 0.1450  1582 ASN B CG    
6547 O  OD1   . ASN B 365 ? 1.2328 1.7897 2.5122 0.1841  -0.1358 0.1415  1582 ASN B OD1   
6548 N  ND2   . ASN B 365 ? 1.1141 1.6674 2.3711 0.2015  -0.1665 0.1557  1582 ASN B ND2   
6549 N  N     . ASP B 366 ? 0.9833 1.5037 2.1228 0.1406  -0.1947 0.1145  1583 ASP B N     
6550 C  CA    . ASP B 366 ? 1.1473 1.6542 2.2436 0.1326  -0.2121 0.1090  1583 ASP B CA    
6551 C  C     . ASP B 366 ? 1.2746 1.7576 2.3374 0.1439  -0.2106 0.1129  1583 ASP B C     
6552 O  O     . ASP B 366 ? 1.3489 1.8276 2.3855 0.1470  -0.2319 0.1172  1583 ASP B O     
6553 C  CB    . ASP B 366 ? 1.2375 1.7602 2.3282 0.1252  -0.2433 0.1096  1583 ASP B CB    
6554 C  CG    . ASP B 366 ? 1.3026 1.8135 2.3543 0.1126  -0.2573 0.1006  1583 ASP B CG    
6555 O  OD1   . ASP B 366 ? 1.3286 1.8408 2.3847 0.0995  -0.2509 0.0915  1583 ASP B OD1   
6556 O  OD2   . ASP B 366 ? 1.3616 1.8606 2.3776 0.1162  -0.2736 0.1028  1583 ASP B OD2   
6557 N  N     . GLN B 367 ? 1.2149 1.6814 2.2777 0.1496  -0.1844 0.1110  1584 GLN B N     
6558 C  CA    . GLN B 367 ? 1.0959 1.5389 2.1338 0.1614  -0.1778 0.1149  1584 GLN B CA    
6559 C  C     . GLN B 367 ? 1.0566 1.4799 2.0846 0.1596  -0.1510 0.1067  1584 GLN B C     
6560 O  O     . GLN B 367 ? 0.9659 1.3925 1.9996 0.1486  -0.1393 0.0982  1584 GLN B O     
6561 C  CB    . GLN B 367 ? 1.0049 1.4504 2.0636 0.1777  -0.1725 0.1262  1584 GLN B CB    
6562 C  CG    . GLN B 367 ? 0.9332 1.3861 2.0310 0.1820  -0.1461 0.1259  1584 GLN B CG    
6563 C  CD    . GLN B 367 ? 0.9760 1.4250 2.0900 0.1992  -0.1364 0.1358  1584 GLN B CD    
6564 O  OE1   . GLN B 367 ? 0.9708 1.4129 2.1029 0.2057  -0.1098 0.1348  1584 GLN B OE1   
6565 N  NE2   . GLN B 367 ? 0.9931 1.4456 2.0997 0.2068  -0.1575 0.1455  1584 GLN B NE2   
6566 N  N     . PHE B 368 ? 1.0263 1.4216 2.0216 0.1675  -0.1397 0.1077  1585 PHE B N     
6567 C  CA    . PHE B 368 ? 0.9344 1.3024 1.9051 0.1661  -0.1108 0.0993  1585 PHE B CA    
6568 C  C     . PHE B 368 ? 0.7971 1.1425 1.7499 0.1792  -0.1040 0.1050  1585 PHE B C     
6569 O  O     . PHE B 368 ? 0.7021 1.0495 1.6502 0.1863  -0.1229 0.1141  1585 PHE B O     
6570 C  CB    . PHE B 368 ? 0.9777 1.3272 1.8996 0.1506  -0.1101 0.0874  1585 PHE B CB    
6571 C  CG    . PHE B 368 ? 0.9568 1.2957 1.8374 0.1472  -0.1319 0.0881  1585 PHE B CG    
6572 C  CD1   . PHE B 368 ? 0.9637 1.3209 1.8468 0.1402  -0.1578 0.0891  1585 PHE B CD1   
6573 C  CD2   . PHE B 368 ? 0.9441 1.2543 1.7832 0.1508  -0.1261 0.0876  1585 PHE B CD2   
6574 C  CE1   . PHE B 368 ? 0.9721 1.3185 1.8154 0.1376  -0.1766 0.0897  1585 PHE B CE1   
6575 C  CE2   . PHE B 368 ? 0.9304 1.2310 1.7321 0.1478  -0.1445 0.0888  1585 PHE B CE2   
6576 C  CZ    . PHE B 368 ? 0.9714 1.2898 1.7742 0.1416  -0.1693 0.0898  1585 PHE B CZ    
6577 N  N     . VAL B 369 ? 0.8186 1.1407 1.7588 0.1821  -0.0772 0.0996  1586 VAL B N     
6578 C  CA    . VAL B 369 ? 0.8562 1.1527 1.7747 0.1926  -0.0702 0.1035  1586 VAL B CA    
6579 C  C     . VAL B 369 ? 0.7170 0.9828 1.5796 0.1824  -0.0623 0.0928  1586 VAL B C     
6580 O  O     . VAL B 369 ? 0.5755 0.8333 1.4260 0.1734  -0.0462 0.0822  1586 VAL B O     
6581 C  CB    . VAL B 369 ? 0.9301 1.2224 1.8806 0.2067  -0.0468 0.1071  1586 VAL B CB    
6582 C  CG1   . VAL B 369 ? 1.0510 1.3427 2.0128 0.2014  -0.0217 0.0973  1586 VAL B CG1   
6583 C  CG2   . VAL B 369 ? 0.8434 1.1030 1.7645 0.2151  -0.0368 0.1085  1586 VAL B CG2   
6584 N  N     . ALA B 370 ? 0.7386 0.9887 1.5675 0.1835  -0.0746 0.0962  1587 ALA B N     
6585 C  CA    . ALA B 370 ? 0.7753 0.9965 1.5535 0.1752  -0.0678 0.0876  1587 ALA B CA    
6586 C  C     . ALA B 370 ? 0.8131 1.0087 1.5808 0.1856  -0.0544 0.0908  1587 ALA B C     
6587 O  O     . ALA B 370 ? 0.8535 1.0513 1.6357 0.1976  -0.0625 0.1024  1587 ALA B O     
6588 C  CB    . ALA B 370 ? 0.7477 0.9693 1.4935 0.1669  -0.0906 0.0880  1587 ALA B CB    
6589 N  N     . VAL B 371 ? 0.7243 0.8953 1.4670 0.1808  -0.0342 0.0807  1588 VAL B N     
6590 C  CA    . VAL B 371 ? 0.6596 0.8040 1.3935 0.1892  -0.0179 0.0812  1588 VAL B CA    
6591 C  C     . VAL B 371 ? 0.7922 0.9096 1.4764 0.1793  -0.0155 0.0731  1588 VAL B C     
6592 O  O     . VAL B 371 ? 0.5944 0.7087 1.2561 0.1667  -0.0121 0.0625  1588 VAL B O     
6593 C  CB    . VAL B 371 ? 0.6308 0.7718 1.3895 0.1947  0.0075  0.0762  1588 VAL B CB    
6594 C  CG1   . VAL B 371 ? 0.6290 0.8022 1.4376 0.2007  0.0041  0.0825  1588 VAL B CG1   
6595 C  CG2   . VAL B 371 ? 0.7131 0.8411 1.4468 0.1828  0.0235  0.0617  1588 VAL B CG2   
6596 N  N     . ARG B 372 ? 0.8812 0.9797 1.5496 0.1850  -0.0178 0.0791  1589 ARG B N     
6597 C  CA    . ARG B 372 ? 0.6855 0.7615 1.3099 0.1759  -0.0193 0.0740  1589 ARG B CA    
6598 C  C     . ARG B 372 ? 0.7227 0.7727 1.3294 0.1718  0.0033  0.0622  1589 ARG B C     
6599 O  O     . ARG B 372 ? 0.7121 0.7508 1.3352 0.1806  0.0196  0.0621  1589 ARG B O     
6600 C  CB    . ARG B 372 ? 0.7474 0.8127 1.3634 0.1835  -0.0291 0.0855  1589 ARG B CB    
6601 C  CG    . ARG B 372 ? 0.7516 0.8368 1.3699 0.1852  -0.0538 0.0962  1589 ARG B CG    
6602 C  CD    . ARG B 372 ? 0.9200 0.9923 1.5329 0.1954  -0.0600 0.1094  1589 ARG B CD    
6603 N  NE    . ARG B 372 ? 0.9725 1.0155 1.5492 0.1897  -0.0521 0.1056  1589 ARG B NE    
6604 C  CZ    . ARG B 372 ? 0.9490 0.9801 1.5058 0.1921  -0.0607 0.1148  1589 ARG B CZ    
6605 N  NH1   . ARG B 372 ? 0.9009 0.9458 1.4668 0.2005  -0.0784 0.1286  1589 ARG B NH1   
6606 N  NH2   . ARG B 372 ? 0.9162 0.9217 1.4436 0.1858  -0.0518 0.1105  1589 ARG B NH2   
6607 N  N     . ARG B 373 ? 0.8359 0.8764 1.4092 0.1583  0.0041  0.0518  1590 ARG B N     
6608 C  CA    . ARG B 373 ? 0.7941 0.8097 1.3475 0.1534  0.0235  0.0401  1590 ARG B CA    
6609 C  C     . ARG B 373 ? 0.7737 0.7619 1.3141 0.1579  0.0300  0.0423  1590 ARG B C     
6610 O  O     . ARG B 373 ? 0.7299 0.6967 1.2652 0.1588  0.0482  0.0347  1590 ARG B O     
6611 C  CB    . ARG B 373 ? 0.6518 0.6651 1.1735 0.1384  0.0209  0.0297  1590 ARG B CB    
6612 C  CG    . ARG B 373 ? 0.5728 0.5607 1.0697 0.1319  0.0380  0.0172  1590 ARG B CG    
6613 C  CD    . ARG B 373 ? 0.5841 0.5676 1.0979 0.1371  0.0578  0.0116  1590 ARG B CD    
6614 N  NE    . ARG B 373 ? 0.8676 0.8237 1.3546 0.1313  0.0734  -0.0006 1590 ARG B NE    
6615 C  CZ    . ARG B 373 ? 0.8624 0.7930 1.3400 0.1344  0.0816  -0.0021 1590 ARG B CZ    
6616 N  NH1   . ARG B 373 ? 0.7844 0.7124 1.2773 0.1441  0.0768  0.0087  1590 ARG B NH1   
6617 N  NH2   . ARG B 373 ? 0.8497 0.7565 1.3018 0.1275  0.0945  -0.0145 1590 ARG B NH2   
6618 N  N     . ASP B 374 ? 0.8153 0.8022 1.3479 0.1600  0.0159  0.0520  1591 ASP B N     
6619 C  CA    . ASP B 374 ? 0.9222 0.8821 1.4428 0.1637  0.0226  0.0548  1591 ASP B CA    
6620 C  C     . ASP B 374 ? 0.9656 0.9214 1.5169 0.1798  0.0302  0.0640  1591 ASP B C     
6621 O  O     . ASP B 374 ? 0.9987 0.9300 1.5490 0.1835  0.0471  0.0599  1591 ASP B O     
6622 C  CB    . ASP B 374 ? 0.9004 0.8581 1.3986 0.1594  0.0068  0.0619  1591 ASP B CB    
6623 C  CG    . ASP B 374 ? 0.9406 0.9193 1.4552 0.1681  -0.0115 0.0768  1591 ASP B CG    
6624 O  OD1   . ASP B 374 ? 0.9027 0.9022 1.4474 0.1757  -0.0150 0.0811  1591 ASP B OD1   
6625 O  OD2   . ASP B 374 ? 0.9014 0.8756 1.3980 0.1669  -0.0226 0.0841  1591 ASP B OD2   
6626 N  N     . ASN B 375 ? 0.9411 0.9209 1.5209 0.1895  0.0184  0.0757  1592 ASN B N     
6627 C  CA    . ASN B 375 ? 0.8819 0.8608 1.4926 0.2061  0.0223  0.0872  1592 ASN B CA    
6628 C  C     . ASN B 375 ? 0.9422 0.9264 1.5834 0.2131  0.0391  0.0825  1592 ASN B C     
6629 O  O     . ASN B 375 ? 1.0853 1.0554 1.7442 0.2250  0.0525  0.0861  1592 ASN B O     
6630 C  CB    . ASN B 375 ? 0.8997 0.9052 1.5299 0.2136  0.0005  0.1022  1592 ASN B CB    
6631 C  CG    . ASN B 375 ? 1.0400 1.0352 1.6494 0.2149  -0.0125 0.1126  1592 ASN B CG    
6632 O  OD1   . ASN B 375 ? 1.1168 1.0844 1.7019 0.2116  -0.0040 0.1101  1592 ASN B OD1   
6633 N  ND2   . ASN B 375 ? 1.1215 1.1387 1.7396 0.2193  -0.0335 0.1245  1592 ASN B ND2   
6634 N  N     . GLY B 376 ? 0.8315 0.8357 1.4802 0.2064  0.0394  0.0750  1593 GLY B N     
6635 C  CA    . GLY B 376 ? 0.8081 0.8278 1.4956 0.2156  0.0500  0.0759  1593 GLY B CA    
6636 C  C     . GLY B 376 ? 0.8837 0.9324 1.6088 0.2267  0.0336  0.0911  1593 GLY B C     
6637 O  O     . GLY B 376 ? 0.9563 1.0243 1.7190 0.2339  0.0396  0.0932  1593 GLY B O     
6638 N  N     . ALA B 377 ? 0.8126 0.8656 1.5283 0.2281  0.0129  0.1019  1594 ALA B N     
6639 C  CA    . ALA B 377 ? 0.7302 0.8107 1.4777 0.2381  -0.0059 0.1168  1594 ALA B CA    
6640 C  C     . ALA B 377 ? 0.8343 0.9483 1.6000 0.2312  -0.0173 0.1141  1594 ALA B C     
6641 O  O     . ALA B 377 ? 0.8821 0.9989 1.6222 0.2167  -0.0228 0.1049  1594 ALA B O     
6642 C  CB    . ALA B 377 ? 0.6300 0.7053 1.3550 0.2391  -0.0256 0.1275  1594 ALA B CB    
6643 N  N     . LYS B 378 ? 0.8716 1.0107 1.6833 0.2419  -0.0204 0.1225  1595 LYS B N     
6644 C  CA    . LYS B 378 ? 0.7762 0.9491 1.6162 0.2376  -0.0297 0.1216  1595 LYS B CA    
6645 C  C     . LYS B 378 ? 0.8010 0.9981 1.6543 0.2416  -0.0585 0.1347  1595 LYS B C     
6646 O  O     . LYS B 378 ? 0.8887 1.0849 1.7553 0.2551  -0.0656 0.1480  1595 LYS B O     
6647 C  CB    . LYS B 378 ? 0.7387 0.9247 1.6262 0.2472  -0.0122 0.1223  1595 LYS B CB    
6648 C  CG    . LYS B 378 ? 0.8173 0.9845 1.6954 0.2426  0.0162  0.1084  1595 LYS B CG    
6649 C  CD    . LYS B 378 ? 0.9645 1.1546 1.8904 0.2480  0.0291  0.1084  1595 LYS B CD    
6650 C  CE    . LYS B 378 ? 1.0693 1.2439 1.9804 0.2401  0.0550  0.0935  1595 LYS B CE    
6651 N  NZ    . LYS B 378 ? 1.1198 1.2575 2.0073 0.2453  0.0761  0.0880  1595 LYS B NZ    
6652 N  N     . GLN B 379 ? 0.8135 1.0306 1.6613 0.2299  -0.0754 0.1311  1596 GLN B N     
6653 C  CA    . GLN B 379 ? 0.8187 1.0589 1.6754 0.2317  -0.1041 0.1416  1596 GLN B CA    
6654 C  C     . GLN B 379 ? 0.9498 1.2202 1.8292 0.2220  -0.1134 0.1363  1596 GLN B C     
6655 O  O     . GLN B 379 ? 1.0429 1.3086 1.9009 0.2080  -0.1075 0.1238  1596 GLN B O     
6656 C  CB    . GLN B 379 ? 0.8252 1.0480 1.6323 0.2255  -0.1182 0.1423  1596 GLN B CB    
6657 C  CG    . GLN B 379 ? 0.9119 1.1555 1.7150 0.2220  -0.1474 0.1481  1596 GLN B CG    
6658 C  CD    . GLN B 379 ? 0.9321 1.1559 1.6828 0.2142  -0.1561 0.1460  1596 GLN B CD    
6659 O  OE1   . GLN B 379 ? 0.7331 0.9299 1.4531 0.2097  -0.1401 0.1392  1596 GLN B OE1   
6660 N  NE2   . GLN B 379 ? 1.0906 1.3275 1.8305 0.2122  -0.1814 0.1516  1596 GLN B NE2   
6661 N  N     . THR B 380 ? 0.9815 1.2824 1.9058 0.2295  -0.1273 0.1459  1597 THR B N     
6662 C  CA    . THR B 380 ? 0.9279 1.2595 1.8804 0.2205  -0.1367 0.1419  1597 THR B CA    
6663 C  C     . THR B 380 ? 0.7949 1.1392 1.7286 0.2125  -0.1673 0.1438  1597 THR B C     
6664 O  O     . THR B 380 ? 0.7790 1.1291 1.7132 0.2210  -0.1871 0.1555  1597 THR B O     
6665 C  CB    . THR B 380 ? 1.0603 1.4166 2.0656 0.2299  -0.1332 0.1491  1597 THR B CB    
6666 O  OG1   . THR B 380 ? 1.1552 1.5230 2.1624 0.2368  -0.1557 0.1610  1597 THR B OG1   
6667 C  CG2   . THR B 380 ? 1.0821 1.4211 2.1013 0.2415  -0.1041 0.1495  1597 THR B CG2   
6668 N  N     . ILE B 381 ? 0.8583 1.2055 1.7737 0.1965  -0.1708 0.1324  1598 ILE B N     
6669 C  CA    . ILE B 381 ? 0.9692 1.3241 1.8607 0.1872  -0.1975 0.1315  1598 ILE B CA    
6670 C  C     . ILE B 381 ? 1.0069 1.3937 1.9344 0.1789  -0.2095 0.1285  1598 ILE B C     
6671 O  O     . ILE B 381 ? 1.0157 1.4071 1.9593 0.1713  -0.1934 0.1198  1598 ILE B O     
6672 C  CB    . ILE B 381 ? 0.8858 1.2144 1.7207 0.1749  -0.1932 0.1206  1598 ILE B CB    
6673 C  CG1   . ILE B 381 ? 1.0150 1.3119 1.8166 0.1820  -0.1799 0.1231  1598 ILE B CG1   
6674 C  CG2   . ILE B 381 ? 0.6363 0.9726 1.4474 0.1663  -0.2201 0.1196  1598 ILE B CG2   
6675 C  CD1   . ILE B 381 ? 1.0367 1.3131 1.8308 0.1797  -0.1503 0.1139  1598 ILE B CD1   
6676 N  N     . LYS B 382 ? 1.0254 1.4307 1.9580 0.1790  -0.2361 0.1347  1599 LYS B N     
6677 C  CA    . LYS B 382 ? 1.1196 1.5486 2.0680 0.1667  -0.2492 0.1292  1599 LYS B CA    
6678 C  C     . LYS B 382 ? 1.0676 1.4898 1.9881 0.1517  -0.2559 0.1178  1599 LYS B C     
6679 O  O     . LYS B 382 ? 0.9699 1.3731 1.8458 0.1501  -0.2643 0.1166  1599 LYS B O     
6680 C  CB    . LYS B 382 ? 1.2222 1.6675 2.1720 0.1700  -0.2749 0.1376  1599 LYS B CB    
6681 C  CG    . LYS B 382 ? 1.2611 1.6909 2.1707 0.1768  -0.2920 0.1450  1599 LYS B CG    
6682 C  CD    . LYS B 382 ? 1.2647 1.7124 2.1750 0.1790  -0.3180 0.1523  1599 LYS B CD    
6683 C  CE    . LYS B 382 ? 1.2400 1.7077 2.1580 0.1635  -0.3330 0.1431  1599 LYS B CE    
6684 N  NZ    . LYS B 382 ? 1.2013 1.6737 2.0911 0.1605  -0.3622 0.1450  1599 LYS B NZ    
6685 N  N     . ARG B 383 ? 1.1051 1.5394 2.0453 0.1398  -0.2494 0.1087  1600 ARG B N     
6686 C  CA    . ARG B 383 ? 1.0109 1.4346 1.9206 0.1247  -0.2506 0.0966  1600 ARG B CA    
6687 C  C     . ARG B 383 ? 1.0686 1.4900 1.9437 0.1195  -0.2783 0.0959  1600 ARG B C     
6688 O  O     . ARG B 383 ? 1.0671 1.4664 1.8945 0.1119  -0.2770 0.0882  1600 ARG B O     
6689 C  CB    . ARG B 383 ? 0.8886 1.3313 1.8331 0.1133  -0.2452 0.0895  1600 ARG B CB    
6690 C  CG    . ARG B 383 ? 0.8354 1.2793 1.8110 0.1166  -0.2156 0.0887  1600 ARG B CG    
6691 C  CD    . ARG B 383 ? 0.8535 1.2686 1.7899 0.1100  -0.1924 0.0787  1600 ARG B CD    
6692 N  NE    . ARG B 383 ? 0.8614 1.2752 1.7818 0.0938  -0.1966 0.0686  1600 ARG B NE    
6693 C  CZ    . ARG B 383 ? 0.9475 1.3596 1.8764 0.0854  -0.1777 0.0616  1600 ARG B CZ    
6694 N  NH1   . ARG B 383 ? 0.8572 1.2688 1.8092 0.0914  -0.1527 0.0632  1600 ARG B NH1   
6695 N  NH2   . ARG B 383 ? 1.0621 1.4715 1.9749 0.0712  -0.1832 0.0531  1600 ARG B NH2   
6696 N  N     . ALA B 384 ? 1.1042 1.5429 1.9906 0.1226  -0.2995 0.1027  1601 ALA B N     
6697 C  CA    . ALA B 384 ? 1.0525 1.4887 1.9035 0.1180  -0.3257 0.1020  1601 ALA B CA    
6698 C  C     . ALA B 384 ? 1.0730 1.4846 1.8812 0.1245  -0.3280 0.1052  1601 ALA B C     
6699 O  O     . ALA B 384 ? 1.2218 1.6178 1.9864 0.1154  -0.3341 0.0973  1601 ALA B O     
6700 C  CB    . ALA B 384 ? 1.0198 1.4753 1.8860 0.1233  -0.3439 0.1105  1601 ALA B CB    
6701 N  N     . GLN B 385 ? 0.9850 1.3873 1.7946 0.1388  -0.3180 0.1155  1602 GLN B N     
6702 C  CA    . GLN B 385 ? 1.0226 1.3958 1.7826 0.1439  -0.3135 0.1182  1602 GLN B CA    
6703 C  C     . GLN B 385 ? 0.9634 1.3100 1.6945 0.1382  -0.2869 0.1086  1602 GLN B C     
6704 O  O     . GLN B 385 ? 0.9835 1.3056 1.6749 0.1413  -0.2812 0.1102  1602 GLN B O     
6705 C  CB    . GLN B 385 ? 1.0694 1.4419 1.8436 0.1614  -0.3131 0.1335  1602 GLN B CB    
6706 N  N     . ALA B 386 ? 0.8575 1.2082 1.6065 0.1296  -0.2711 0.0990  1603 ALA B N     
6707 C  CA    . ALA B 386 ? 0.8003 1.1272 1.5262 0.1259  -0.2455 0.0912  1603 ALA B CA    
6708 C  C     . ALA B 386 ? 1.0237 1.3263 1.6936 0.1198  -0.2476 0.0858  1603 ALA B C     
6709 O  O     . ALA B 386 ? 0.9356 1.2167 1.5790 0.1254  -0.2376 0.0888  1603 ALA B O     
6710 C  CB    . ALA B 386 ? 0.6510 0.9869 1.3999 0.1159  -0.2323 0.0815  1603 ALA B CB    
6711 N  N     . THR B 387 ? 1.1314 1.4373 1.7837 0.1084  -0.2608 0.0781  1604 THR B N     
6712 C  CA    . THR B 387 ? 1.0952 1.3788 1.6964 0.1024  -0.2610 0.0722  1604 THR B CA    
6713 C  C     . THR B 387 ? 1.0398 1.3095 1.6116 0.1114  -0.2680 0.0812  1604 THR B C     
6714 O  O     . THR B 387 ? 1.2259 1.4746 1.7575 0.1086  -0.2623 0.0780  1604 THR B O     
6715 C  CB    . THR B 387 ? 1.1259 1.4153 1.7128 0.0905  -0.2774 0.0639  1604 THR B CB    
6716 O  OG1   . THR B 387 ? 1.1939 1.4899 1.7702 0.0940  -0.3019 0.0698  1604 THR B OG1   
6717 C  CG2   . THR B 387 ? 1.1637 1.4728 1.7884 0.0825  -0.2772 0.0579  1604 THR B CG2   
6718 N  N     . VAL B 388 ? 0.9856 1.2667 1.5765 0.1221  -0.2803 0.0930  1605 VAL B N     
6719 C  CA    . VAL B 388 ? 0.9855 1.2536 1.5475 0.1307  -0.2885 0.1028  1605 VAL B CA    
6720 C  C     . VAL B 388 ? 1.1816 1.4363 1.7499 0.1419  -0.2709 0.1110  1605 VAL B C     
6721 O  O     . VAL B 388 ? 1.2716 1.5048 1.8067 0.1452  -0.2657 0.1147  1605 VAL B O     
6722 C  CB    . VAL B 388 ? 0.8288 1.1163 1.4028 0.1357  -0.3159 0.1114  1605 VAL B CB    
6723 C  CG1   . VAL B 388 ? 0.8521 1.1266 1.3990 0.1466  -0.3239 0.1240  1605 VAL B CG1   
6724 C  CG2   . VAL B 388 ? 0.7534 1.0499 1.3149 0.1237  -0.3336 0.1020  1605 VAL B CG2   
6725 N  N     . GLU B 389 ? 1.1898 1.4552 1.8000 0.1474  -0.2597 0.1133  1606 GLU B N     
6726 C  CA    . GLU B 389 ? 1.0844 1.3345 1.6985 0.1583  -0.2429 0.1205  1606 GLU B CA    
6727 C  C     . GLU B 389 ? 1.0108 1.2388 1.6057 0.1521  -0.2184 0.1107  1606 GLU B C     
6728 O  O     . GLU B 389 ? 1.1805 1.3869 1.7567 0.1570  -0.2068 0.1142  1606 GLU B O     
6729 C  CB    . GLU B 389 ? 1.0599 1.3280 1.7250 0.1689  -0.2402 0.1282  1606 GLU B CB    
6730 C  CG    . GLU B 389 ? 1.2919 1.5426 1.9586 0.1817  -0.2262 0.1374  1606 GLU B CG    
6731 C  CD    . GLU B 389 ? 1.6119 1.8769 2.3075 0.1964  -0.2397 0.1529  1606 GLU B CD    
6732 O  OE1   . GLU B 389 ? 1.6770 1.9526 2.3634 0.1975  -0.2639 0.1594  1606 GLU B OE1   
6733 O  OE2   . GLU B 389 ? 1.6839 1.9488 2.4105 0.2071  -0.2263 0.1585  1606 GLU B OE2   
6734 N  N     . MET B 390 ? 0.7660 0.9990 1.3648 0.1410  -0.2111 0.0987  1607 MET B N     
6735 C  CA    . MET B 390 ? 0.6419 0.8560 1.2252 0.1354  -0.1885 0.0895  1607 MET B CA    
6736 C  C     . MET B 390 ? 0.8322 1.0229 1.3687 0.1311  -0.1863 0.0870  1607 MET B C     
6737 O  O     . MET B 390 ? 0.8279 0.9993 1.3524 0.1316  -0.1685 0.0846  1607 MET B O     
6738 C  CB    . MET B 390 ? 0.7340 0.9587 1.3291 0.1244  -0.1832 0.0782  1607 MET B CB    
6739 C  CG    . MET B 390 ? 0.8208 1.0282 1.4026 0.1188  -0.1603 0.0688  1607 MET B CG    
6740 S  SD    . MET B 390 ? 0.9555 1.1532 1.5595 0.1296  -0.1384 0.0726  1607 MET B SD    
6741 C  CE    . MET B 390 ? 0.6729 0.9008 1.3329 0.1354  -0.1426 0.0776  1607 MET B CE    
6742 N  N     . PRO B 391 ? 0.9784 1.1690 1.4872 0.1267  -0.2028 0.0872  1608 PRO B N     
6743 C  CA    . PRO B 391 ? 0.9900 1.1584 1.4567 0.1239  -0.1988 0.0861  1608 PRO B CA    
6744 C  C     . PRO B 391 ? 1.0711 1.2256 1.5322 0.1346  -0.1951 0.0974  1608 PRO B C     
6745 O  O     . PRO B 391 ? 1.2700 1.4047 1.7163 0.1341  -0.1792 0.0958  1608 PRO B O     
6746 C  CB    . PRO B 391 ? 0.9804 1.1546 1.4240 0.1187  -0.2183 0.0849  1608 PRO B CB    
6747 C  CG    . PRO B 391 ? 1.0178 1.2146 1.4887 0.1144  -0.2286 0.0805  1608 PRO B CG    
6748 C  CD    . PRO B 391 ? 1.0359 1.2452 1.5487 0.1233  -0.2247 0.0872  1608 PRO B CD    
6749 N  N     . LYS B 392 ? 0.9734 1.1381 1.4472 0.1441  -0.2101 0.1089  1609 LYS B N     
6750 C  CA    . LYS B 392 ? 0.9108 1.0632 1.3844 0.1559  -0.2068 0.1215  1609 LYS B CA    
6751 C  C     . LYS B 392 ? 1.0180 1.1577 1.5075 0.1588  -0.1838 0.1191  1609 LYS B C     
6752 O  O     . LYS B 392 ? 1.1001 1.2171 1.5693 0.1595  -0.1715 0.1203  1609 LYS B O     
6753 C  CB    . LYS B 392 ? 0.6294 0.7999 1.1280 0.1669  -0.2248 0.1339  1609 LYS B CB    
6754 N  N     . LEU B 393 ? 0.9867 1.1402 1.5112 0.1593  -0.1770 0.1146  1610 LEU B N     
6755 C  CA    . LEU B 393 ? 0.9426 1.0843 1.4828 0.1626  -0.1548 0.1117  1610 LEU B CA    
6756 C  C     . LEU B 393 ? 0.8727 0.9906 1.3810 0.1539  -0.1392 0.1025  1610 LEU B C     
6757 O  O     . LEU B 393 ? 0.7814 0.8786 1.2819 0.1582  -0.1267 0.1052  1610 LEU B O     
6758 C  CB    . LEU B 393 ? 0.8654 1.0256 1.4417 0.1612  -0.1486 0.1054  1610 LEU B CB    
6759 C  CG    . LEU B 393 ? 0.8061 0.9571 1.4056 0.1683  -0.1272 0.1049  1610 LEU B CG    
6760 C  CD1   . LEU B 393 ? 0.7110 0.8602 1.3291 0.1836  -0.1298 0.1190  1610 LEU B CD1   
6761 C  CD2   . LEU B 393 ? 0.7757 0.9442 1.4082 0.1661  -0.1190 0.0982  1610 LEU B CD2   
6762 N  N     . LEU B 394 ? 0.8636 0.9841 1.3531 0.1416  -0.1408 0.0919  1611 LEU B N     
6763 C  CA    . LEU B 394 ? 0.8947 0.9955 1.3567 0.1330  -0.1270 0.0828  1611 LEU B CA    
6764 C  C     . LEU B 394 ? 0.9335 1.0163 1.3646 0.1337  -0.1292 0.0885  1611 LEU B C     
6765 O  O     . LEU B 394 ? 0.9563 1.0189 1.3753 0.1324  -0.1152 0.0865  1611 LEU B O     
6766 C  CB    . LEU B 394 ? 0.6905 0.7992 1.1414 0.1208  -0.1290 0.0714  1611 LEU B CB    
6767 C  CG    . LEU B 394 ? 0.7896 0.9136 1.2690 0.1185  -0.1236 0.0650  1611 LEU B CG    
6768 C  CD1   . LEU B 394 ? 0.9936 1.1323 1.4680 0.1092  -0.1351 0.0589  1611 LEU B CD1   
6769 C  CD2   . LEU B 394 ? 0.6560 0.7666 1.1351 0.1153  -0.1025 0.0565  1611 LEU B CD2   
6770 N  N     . GLU B 395 ? 0.8205 0.9097 1.2391 0.1358  -0.1464 0.0961  1612 GLU B N     
6771 C  CA    . GLU B 395 ? 0.8290 0.9013 1.2224 0.1391  -0.1478 0.1047  1612 GLU B CA    
6772 C  C     . GLU B 395 ? 0.9522 1.0102 1.3593 0.1489  -0.1365 0.1126  1612 GLU B C     
6773 O  O     . GLU B 395 ? 1.0916 1.1285 1.4844 0.1467  -0.1230 0.1113  1612 GLU B O     
6774 C  CB    . GLU B 395 ? 0.8118 0.8943 1.1946 0.1432  -0.1685 0.1139  1612 GLU B CB    
6775 C  CG    . GLU B 395 ? 0.7784 0.8663 1.1354 0.1336  -0.1784 0.1070  1612 GLU B CG    
6776 C  CD    . GLU B 395 ? 0.7721 0.8638 1.1112 0.1384  -0.1971 0.1167  1612 GLU B CD    
6777 N  N     . THR B 396 ? 0.9542 1.0239 1.3916 0.1596  -0.1415 0.1205  1613 THR B N     
6778 C  CA    . THR B 396 ? 0.8878 0.9448 1.3421 0.1706  -0.1312 0.1288  1613 THR B CA    
6779 C  C     . THR B 396 ? 0.8095 0.8479 1.2640 0.1662  -0.1089 0.1190  1613 THR B C     
6780 O  O     . THR B 396 ? 0.8702 0.8868 1.3197 0.1705  -0.0980 0.1235  1613 THR B O     
6781 C  CB    . THR B 396 ? 0.8709 0.9479 1.3638 0.1814  -0.1384 0.1357  1613 THR B CB    
6782 O  OG1   . THR B 396 ? 0.9522 1.0430 1.4420 0.1867  -0.1603 0.1467  1613 THR B OG1   
6783 C  CG2   . THR B 396 ? 0.8102 0.8741 1.3251 0.1935  -0.1248 0.1428  1613 THR B CG2   
6784 N  N     . ILE B 397 ? 0.8040 0.8495 1.2641 0.1576  -0.1018 0.1057  1614 ILE B N     
6785 C  CA    . ILE B 397 ? 0.8121 0.8403 1.2717 0.1536  -0.0814 0.0958  1614 ILE B CA    
6786 C  C     . ILE B 397 ? 1.0466 1.0528 1.4731 0.1456  -0.0755 0.0926  1614 ILE B C     
6787 O  O     . ILE B 397 ? 1.0457 1.0301 1.4689 0.1478  -0.0628 0.0935  1614 ILE B O     
6788 C  CB    . ILE B 397 ? 0.8474 0.8884 1.3169 0.1460  -0.0761 0.0831  1614 ILE B CB    
6789 C  CG1   . ILE B 397 ? 0.9341 0.9950 1.4420 0.1545  -0.0777 0.0865  1614 ILE B CG1   
6790 C  CG2   . ILE B 397 ? 0.7547 0.7765 1.2137 0.1392  -0.0568 0.0713  1614 ILE B CG2   
6791 C  CD1   . ILE B 397 ? 0.8434 0.9256 1.3610 0.1467  -0.0818 0.0782  1614 ILE B CD1   
6792 N  N     . HIS B 398 ? 1.0719 1.0837 1.4746 0.1367  -0.0850 0.0897  1615 HIS B N     
6793 C  CA    . HIS B 398 ? 0.8308 0.8250 1.2044 0.1283  -0.0797 0.0865  1615 HIS B CA    
6794 C  C     . HIS B 398 ? 0.8349 0.8102 1.2023 0.1351  -0.0766 0.0977  1615 HIS B C     
6795 O  O     . HIS B 398 ? 0.9691 0.9236 1.3309 0.1324  -0.0629 0.0947  1615 HIS B O     
6796 C  CB    . HIS B 398 ? 0.7893 0.7941 1.1408 0.1207  -0.0920 0.0846  1615 HIS B CB    
6797 C  CG    . HIS B 398 ? 0.7878 0.7769 1.1117 0.1134  -0.0876 0.0836  1615 HIS B CG    
6798 N  ND1   . HIS B 398 ? 0.7932 0.7723 1.1027 0.1175  -0.0912 0.0949  1615 HIS B ND1   
6799 C  CD2   . HIS B 398 ? 0.7219 0.7042 1.0313 0.1026  -0.0797 0.0733  1615 HIS B CD2   
6800 C  CE1   . HIS B 398 ? 0.8636 0.8307 1.1525 0.1091  -0.0847 0.0913  1615 HIS B CE1   
6801 N  NE2   . HIS B 398 ? 0.8411 0.8107 1.1303 0.1000  -0.0784 0.0782  1615 HIS B NE2   
6802 N  N     . THR B 399 ? 0.7666 0.7482 1.1355 0.1441  -0.0892 0.1111  1616 THR B N     
6803 C  CA    . THR B 399 ? 0.8016 0.7652 1.1639 0.1515  -0.0869 0.1239  1616 THR B CA    
6804 C  C     . THR B 399 ? 0.8466 0.7925 1.2271 0.1573  -0.0710 0.1240  1616 THR B C     
6805 O  O     . THR B 399 ? 0.7932 0.7157 1.1624 0.1551  -0.0599 0.1251  1616 THR B O     
6806 C  CB    . THR B 399 ? 0.8112 0.7870 1.1774 0.1624  -0.1039 0.1386  1616 THR B CB    
6807 O  OG1   . THR B 399 ? 0.8554 0.8504 1.2095 0.1569  -0.1189 0.1353  1616 THR B OG1   
6808 C  CG2   . THR B 399 ? 0.8808 0.8379 1.2288 0.1675  -0.1037 0.1521  1616 THR B CG2   
6809 N  N     . SER B 400 ? 0.8058 0.7621 1.2149 0.1636  -0.0685 0.1216  1617 SER B N     
6810 C  CA    . SER B 400 ? 0.9843 0.9230 1.4111 0.1709  -0.0530 0.1223  1617 SER B CA    
6811 C  C     . SER B 400 ? 0.9489 0.8679 1.3630 0.1599  -0.0363 0.1084  1617 SER B C     
6812 O  O     . SER B 400 ? 0.8736 0.7678 1.2855 0.1616  -0.0238 0.1095  1617 SER B O     
6813 C  CB    . SER B 400 ? 1.0903 1.0454 1.5518 0.1802  -0.0524 0.1223  1617 SER B CB    
6814 N  N     . MET B 401 ? 0.9139 0.8427 1.3184 0.1482  -0.0365 0.0952  1618 MET B N     
6815 C  CA    . MET B 401 ? 0.8774 0.7893 1.2662 0.1366  -0.0235 0.0820  1618 MET B CA    
6816 C  C     . MET B 401 ? 0.9743 0.8684 1.3394 0.1305  -0.0226 0.0856  1618 MET B C     
6817 O  O     . MET B 401 ? 1.0444 0.9147 1.4056 0.1282  -0.0100 0.0827  1618 MET B O     
6818 C  CB    . MET B 401 ? 0.8597 0.7881 1.2418 0.1261  -0.0266 0.0695  1618 MET B CB    
6819 C  CG    . MET B 401 ? 0.8011 0.7486 1.2073 0.1313  -0.0273 0.0667  1618 MET B CG    
6820 S  SD    . MET B 401 ? 0.8619 0.8229 1.2593 0.1187  -0.0270 0.0516  1618 MET B SD    
6821 C  CE    . MET B 401 ? 0.7083 0.6435 1.0872 0.1089  -0.0101 0.0385  1618 MET B CE    
6822 N  N     . TYR B 402 ? 0.9439 0.8483 1.2940 0.1285  -0.0355 0.0925  1619 TYR B N     
6823 C  CA    . TYR B 402 ? 0.9298 0.8192 1.2575 0.1215  -0.0334 0.0951  1619 TYR B CA    
6824 C  C     . TYR B 402 ? 0.9524 0.8191 1.2836 0.1292  -0.0261 0.1062  1619 TYR B C     
6825 O  O     . TYR B 402 ? 1.0495 0.8942 1.3740 0.1231  -0.0143 0.1023  1619 TYR B O     
6826 C  CB    . TYR B 402 ? 0.9403 0.8443 1.2508 0.1193  -0.0475 0.1011  1619 TYR B CB    
6827 C  CG    . TYR B 402 ? 0.9052 0.7942 1.1942 0.1125  -0.0437 0.1045  1619 TYR B CG    
6828 C  CD1   . TYR B 402 ? 0.9670 0.8528 1.2437 0.0993  -0.0380 0.0932  1619 TYR B CD1   
6829 C  CD2   . TYR B 402 ? 0.8962 0.7741 1.1785 0.1196  -0.0453 0.1197  1619 TYR B CD2   
6830 C  CE1   . TYR B 402 ? 0.9560 0.8294 1.2166 0.0929  -0.0338 0.0968  1619 TYR B CE1   
6831 C  CE2   . TYR B 402 ? 0.7283 0.5923 0.9927 0.1133  -0.0402 0.1234  1619 TYR B CE2   
6832 C  CZ    . TYR B 402 ? 0.8525 0.7149 1.1074 0.0999  -0.0343 0.1119  1619 TYR B CZ    
6833 O  OH    . TYR B 402 ? 1.0172 0.8673 1.2573 0.0937  -0.0289 0.1164  1619 TYR B OH    
6834 N  N     . GLU B 403 ? 0.9212 0.7927 1.2644 0.1427  -0.0332 0.1199  1620 GLU B N     
6835 C  CA    . GLU B 403 ? 1.0434 0.8936 1.3908 0.1519  -0.0273 0.1328  1620 GLU B CA    
6836 C  C     . GLU B 403 ? 0.9618 0.7911 1.3235 0.1528  -0.0102 0.1254  1620 GLU B C     
6837 O  O     . GLU B 403 ? 0.8302 0.6336 1.1866 0.1517  0.0004  0.1285  1620 GLU B O     
6838 C  CB    . GLU B 403 ? 0.9671 0.8298 1.3269 0.1672  -0.0398 0.1486  1620 GLU B CB    
6839 C  CG    . GLU B 403 ? 1.1439 1.0230 1.4843 0.1663  -0.0569 0.1564  1620 GLU B CG    
6840 C  CD    . GLU B 403 ? 1.1775 1.0717 1.5293 0.1804  -0.0721 0.1708  1620 GLU B CD    
6841 O  OE1   . GLU B 403 ? 1.0426 0.9402 1.3759 0.1830  -0.0839 0.1820  1620 GLU B OE1   
6842 O  OE2   . GLU B 403 ? 1.3023 1.2054 1.6818 0.1890  -0.0723 0.1710  1620 GLU B OE2   
6843 N  N     . ARG B 404 ? 1.0132 0.8523 1.3917 0.1537  -0.0064 0.1147  1621 ARG B N     
6844 C  CA    . ARG B 404 ? 1.0292 0.8473 1.4166 0.1527  0.0109  0.1049  1621 ARG B CA    
6845 C  C     . ARG B 404 ? 1.0792 0.8763 1.4458 0.1384  0.0200  0.0955  1621 ARG B C     
6846 O  O     . ARG B 404 ? 1.1925 0.9631 1.5569 0.1389  0.0301  0.0986  1621 ARG B O     
6847 C  CB    . ARG B 404 ? 1.0286 0.8613 1.4288 0.1513  0.0141  0.0918  1621 ARG B CB    
6848 C  CG    . ARG B 404 ? 1.1394 0.9832 1.5671 0.1654  0.0137  0.0978  1621 ARG B CG    
6849 C  CD    . ARG B 404 ? 1.1963 1.0479 1.6356 0.1632  0.0219  0.0841  1621 ARG B CD    
6850 N  NE    . ARG B 404 ? 1.2260 1.0956 1.6956 0.1770  0.0188  0.0916  1621 ARG B NE    
6851 C  CZ    . ARG B 404 ? 1.4735 1.3367 1.9632 0.1918  0.0206  0.1043  1621 ARG B CZ    
6852 N  NH1   . ARG B 404 ? 1.4786 1.3155 1.9598 0.1946  0.0266  0.1110  1621 ARG B NH1   
6853 N  NH2   . ARG B 404 ? 1.5934 1.4761 2.1133 0.2039  0.0171  0.1109  1621 ARG B NH2   
6854 N  N     . ALA B 405 ? 0.9742 0.7838 1.3258 0.1255  0.0155  0.0847  1622 ALA B N     
6855 C  CA    . ALA B 405 ? 1.0000 0.7944 1.3338 0.1110  0.0221  0.0748  1622 ALA B CA    
6856 C  C     . ALA B 405 ? 0.9727 0.7518 1.2960 0.1099  0.0224  0.0864  1622 ALA B C     
6857 O  O     . ALA B 405 ? 1.0036 0.7584 1.3222 0.1034  0.0332  0.0828  1622 ALA B O     
6858 C  CB    . ALA B 405 ? 1.0464 0.8614 1.3673 0.0996  0.0142  0.0648  1622 ALA B CB    
6859 N  N     . GLU B 406 ? 0.8434 0.6350 1.1631 0.1166  0.0110  0.1009  1623 GLU B N     
6860 C  CA    . GLU B 406 ? 0.9508 0.7277 1.2590 0.1162  0.0119  0.1133  1623 GLU B CA    
6861 C  C     . GLU B 406 ? 1.2283 0.9775 1.5471 0.1241  0.0235  0.1206  1623 GLU B C     
6862 O  O     . GLU B 406 ? 1.3904 1.1160 1.7028 0.1167  0.0337  0.1196  1623 GLU B O     
6863 C  CB    . GLU B 406 ? 1.0842 0.8787 1.3856 0.1241  -0.0024 0.1278  1623 GLU B CB    
6864 C  CG    . GLU B 406 ? 1.2841 1.0643 1.5711 0.1246  -0.0014 0.1420  1623 GLU B CG    
6865 C  CD    . GLU B 406 ? 1.4066 1.2058 1.6789 0.1279  -0.0158 0.1519  1623 GLU B CD    
6866 O  OE1   . GLU B 406 ? 1.4552 1.2570 1.7092 0.1182  -0.0165 0.1504  1623 GLU B OE1   
6867 O  OE2   . GLU B 406 ? 1.3735 1.1851 1.6529 0.1402  -0.0264 0.1607  1623 GLU B OE2   
6868 N  N     . ARG B 407 ? 1.2723 1.0237 1.6098 0.1386  0.0229  0.1265  1624 ARG B N     
6869 C  CA    . ARG B 407 ? 1.2684 0.9934 1.6185 0.1479  0.0343  0.1336  1624 ARG B CA    
6870 C  C     . ARG B 407 ? 1.3251 1.0249 1.6731 0.1369  0.0501  0.1188  1624 ARG B C     
6871 O  O     . ARG B 407 ? 1.3557 1.0295 1.6976 0.1329  0.0590  0.1225  1624 ARG B O     
6872 C  CB    . ARG B 407 ? 1.1396 0.8748 1.5138 0.1637  0.0324  0.1375  1624 ARG B CB    
6873 C  CG    . ARG B 407 ? 1.2063 0.9172 1.5964 0.1767  0.0429  0.1472  1624 ARG B CG    
6874 C  CD    . ARG B 407 ? 1.2843 1.0053 1.7008 0.1888  0.0453  0.1444  1624 ARG B CD    
6875 N  NE    . ARG B 407 ? 1.2856 1.0123 1.7021 0.1787  0.0517  0.1239  1624 ARG B NE    
6876 C  CZ    . ARG B 407 ? 1.1652 0.9106 1.5997 0.1842  0.0512  0.1178  1624 ARG B CZ    
6877 N  NH1   . ARG B 407 ? 0.9780 0.7401 1.4350 0.1998  0.0439  0.1303  1624 ARG B NH1   
6878 N  NH2   . ARG B 407 ? 1.2221 0.9696 1.6522 0.1740  0.0582  0.0995  1624 ARG B NH2   
6879 N  N     . ASP B 408 ? 1.2661 0.9745 1.6157 0.1297  0.0526  0.1012  1625 ASP B N     
6880 C  CA    . ASP B 408 ? 1.2352 0.9203 1.5819 0.1195  0.0666  0.0856  1625 ASP B CA    
6881 C  C     . ASP B 408 ? 1.1632 0.8344 1.4927 0.1046  0.0688  0.0836  1625 ASP B C     
6882 O  O     . ASP B 408 ? 1.2465 0.8886 1.5761 0.1025  0.0796  0.0852  1625 ASP B O     
6883 C  CB    . ASP B 408 ? 1.2426 0.9438 1.5889 0.1136  0.0659  0.0685  1625 ASP B CB    
6884 C  CG    . ASP B 408 ? 1.3953 1.0741 1.7448 0.1108  0.0809  0.0537  1625 ASP B CG    
6885 O  OD1   . ASP B 408 ? 1.2847 0.9665 1.6223 0.0980  0.0817  0.0380  1625 ASP B OD1   
6886 O  OD2   . ASP B 408 ? 1.6130 1.2713 1.9759 0.1214  0.0915  0.0576  1625 ASP B OD2   
6887 N  N     . LEU B 409 ? 1.0580 0.7501 1.3743 0.0959  0.0581  0.0833  1626 LEU B N     
6888 C  CA    . LEU B 409 ? 1.0025 0.6859 1.3047 0.0810  0.0599  0.0807  1626 LEU B CA    
6889 C  C     . LEU B 409 ? 1.1602 0.8236 1.4614 0.0847  0.0645  0.0967  1626 LEU B C     
6890 O  O     . LEU B 409 ? 1.2975 0.9395 1.5948 0.0742  0.0732  0.0937  1626 LEU B O     
6891 C  CB    . LEU B 409 ? 0.8886 0.6003 1.1788 0.0735  0.0476  0.0791  1626 LEU B CB    
6892 C  CG    . LEU B 409 ? 1.0133 0.7226 1.2911 0.0596  0.0479  0.0788  1626 LEU B CG    
6893 C  CD1   . LEU B 409 ? 1.1691 0.8955 1.4402 0.0474  0.0431  0.0631  1626 LEU B CD1   
6894 C  CD2   . LEU B 409 ? 1.0205 0.7422 1.2909 0.0656  0.0398  0.0955  1626 LEU B CD2   
6895 N  N     . GLN B 410 ? 1.1943 0.8645 1.4986 0.0989  0.0583  0.1143  1627 GLN B N     
6896 C  CA    . GLN B 410 ? 1.3018 0.9512 1.6020 0.1011  0.0635  0.1299  1627 GLN B CA    
6897 C  C     . GLN B 410 ? 1.3890 1.0066 1.7017 0.1078  0.0767  0.1326  1627 GLN B C     
6898 O  O     . GLN B 410 ? 1.3638 0.9570 1.6736 0.1052  0.0851  0.1408  1627 GLN B O     
6899 C  CB    . GLN B 410 ? 1.3749 1.0401 1.6683 0.1120  0.0520  0.1488  1627 GLN B CB    
6900 C  CG    . GLN B 410 ? 1.6003 1.2759 1.8755 0.1001  0.0478  0.1498  1627 GLN B CG    
6901 C  CD    . GLN B 410 ? 1.7642 1.4673 2.0289 0.1061  0.0329  0.1578  1627 GLN B CD    
6902 O  OE1   . GLN B 410 ? 1.8172 1.5265 2.0853 0.1208  0.0253  0.1699  1627 GLN B OE1   
6903 N  NE2   . GLN B 410 ? 1.7891 1.5093 2.0414 0.0949  0.0280  0.1507  1627 GLN B NE2   
6904 N  N     . SER B 411 ? 1.4966 1.1130 1.8237 0.1163  0.0799  0.1256  1628 SER B N     
6905 C  CA    . SER B 411 ? 1.5390 1.1219 1.8766 0.1201  0.0949  0.1243  1628 SER B CA    
6906 C  C     . SER B 411 ? 1.5372 1.0993 1.8678 0.1018  0.1054  0.1067  1628 SER B C     
6907 O  O     . SER B 411 ? 1.6802 1.2098 2.0168 0.1022  0.1188  0.1051  1628 SER B O     
6908 C  CB    . SER B 411 ? 1.5106 1.0962 1.8668 0.1355  0.0972  0.1227  1628 SER B CB    
6909 O  OG    . SER B 411 ? 1.5508 1.1363 1.9098 0.1291  0.1033  0.1021  1628 SER B OG    
6910 N  N     . HIS B 412 ? 1.1179 0.6971 1.4370 0.0861  0.0997  0.0932  1629 HIS B N     
6911 C  CA    . HIS B 412 ? 1.1541 0.7125 1.4679 0.0690  0.1088  0.0773  1629 HIS B CA    
6912 C  C     . HIS B 412 ? 1.0807 0.6459 1.3828 0.0526  0.1046  0.0771  1629 HIS B C     
6913 O  O     . HIS B 412 ? 0.9880 0.5528 1.2844 0.0366  0.1053  0.0610  1629 HIS B O     
6914 C  CB    . HIS B 412 ? 1.2247 0.7844 1.5384 0.0639  0.1115  0.0559  1629 HIS B CB    
6915 C  CG    . HIS B 412 ? 1.6259 1.1798 1.9523 0.0797  0.1174  0.0554  1629 HIS B CG    
6916 N  ND1   . HIS B 412 ? 1.6889 1.2289 2.0162 0.0771  0.1267  0.0375  1629 HIS B ND1   
6917 C  CD2   . HIS B 412 ? 1.6631 1.2342 2.0006 0.0969  0.1118  0.0682  1629 HIS B CD2   
6918 C  CE1   . HIS B 412 ? 1.6548 1.1970 1.9961 0.0940  0.1302  0.0420  1629 HIS B CE1   
6919 N  NE2   . HIS B 412 ? 1.7141 1.2769 2.0630 0.1059  0.1203  0.0605  1629 HIS B NE2   
6920 N  N     . THR B 413 ? 1.1174 0.6866 1.4162 0.0564  0.1012  0.0954  1630 THR B N     
6921 C  CA    . THR B 413 ? 1.1607 0.7300 1.4514 0.0416  0.1014  0.0972  1630 THR B CA    
6922 C  C     . THR B 413 ? 1.2701 0.8095 1.5639 0.0445  0.1121  0.1125  1630 THR B C     
6923 O  O     . THR B 413 ? 1.3403 0.8788 1.6339 0.0590  0.1106  0.1314  1630 THR B O     
6924 C  CB    . THR B 413 ? 1.0918 0.6943 1.3725 0.0413  0.0887  0.1039  1630 THR B CB    
6925 O  OG1   . THR B 413 ? 1.1129 0.7169 1.3899 0.0541  0.0861  0.1253  1630 THR B OG1   
6926 C  CG2   . THR B 413 ? 1.1153 0.7452 1.3951 0.0456  0.0782  0.0944  1630 THR B CG2   
6927 N  N     . LYS B 414 ? 1.2471 0.7615 1.5438 0.0305  0.1225  0.1042  1631 LYS B N     
6928 C  CA    . LYS B 414 ? 1.2770 0.7577 1.5784 0.0315  0.1349  0.1161  1631 LYS B CA    
6929 C  C     . LYS B 414 ? 1.3153 0.7951 1.6125 0.0167  0.1375  0.1216  1631 LYS B C     
6930 O  O     . LYS B 414 ? 1.3038 0.7992 1.5986 0.0009  0.1332  0.1089  1631 LYS B O     
6931 C  CB    . LYS B 414 ? 1.0368 0.4844 1.3466 0.0272  0.1468  0.1022  1631 LYS B CB    
6932 N  N     . LEU B 415 ? 1.4117 0.8744 1.7084 0.0225  0.1443  0.1416  1632 LEU B N     
6933 C  CA    . LEU B 415 ? 1.4019 0.8608 1.6959 0.0101  0.1494  0.1500  1632 LEU B CA    
6934 C  C     . LEU B 415 ? 1.4447 0.8643 1.7482 0.0008  0.1647  0.1491  1632 LEU B C     
6935 O  O     . LEU B 415 ? 1.7291 1.1210 2.0377 0.0117  0.1725  0.1552  1632 LEU B O     
6936 C  CB    . LEU B 415 ? 1.4312 0.8981 1.7148 0.0230  0.1470  0.1745  1632 LEU B CB    
6937 C  CG    . LEU B 415 ? 1.4059 0.8736 1.6837 0.0131  0.1522  0.1864  1632 LEU B CG    
6938 C  CD1   . LEU B 415 ? 1.3857 0.8852 1.6604 -0.0006 0.1443  0.1742  1632 LEU B CD1   
6939 C  CD2   . LEU B 415 ? 1.3592 0.8283 1.6238 0.0295  0.1507  0.2113  1632 LEU B CD2   
6940 N  N     . THR B 416 ? 1.4345 0.8517 1.7419 -0.0194 0.1689  0.1413  1633 THR B N     
6941 C  CA    . THR B 416 ? 1.4455 0.8261 1.7626 -0.0305 0.1834  0.1415  1633 THR B CA    
6942 C  C     . THR B 416 ? 1.4034 0.7911 1.7236 -0.0486 0.1866  0.1444  1633 THR B C     
6943 O  O     . THR B 416 ? 1.4852 0.9060 1.8015 -0.0547 0.1774  0.1408  1633 THR B O     
6944 C  CB    . THR B 416 ? 1.4932 0.8543 1.8179 -0.0403 0.1866  0.1182  1633 THR B CB    
6945 O  OG1   . THR B 416 ? 1.6762 1.0012 2.0105 -0.0529 0.2005  0.1180  1633 THR B OG1   
6946 C  CG2   . THR B 416 ? 1.3851 0.7738 1.7086 -0.0556 0.1760  0.0970  1633 THR B CG2   
6947 N  N     . LYS B 417 ? 1.3777 0.7335 1.7063 -0.0570 0.2006  0.1513  1634 LYS B N     
6948 C  CA    . LYS B 417 ? 1.3069 0.6635 1.6449 -0.0785 0.2059  0.1484  1634 LYS B CA    
6949 C  C     . LYS B 417 ? 1.2721 0.6006 1.6237 -0.0964 0.2128  0.1299  1634 LYS B C     
6950 O  O     . LYS B 417 ? 1.3322 0.6609 1.6950 -0.1166 0.2163  0.1246  1634 LYS B O     
6951 C  CB    . LYS B 417 ? 1.1900 0.5344 1.5268 -0.0758 0.2173  0.1738  1634 LYS B CB    
6952 C  CG    . LYS B 417 ? 1.1897 0.5539 1.5094 -0.0557 0.2115  0.1938  1634 LYS B CG    
6953 C  CD    . LYS B 417 ? 1.2333 0.5978 1.5496 -0.0589 0.2205  0.2143  1634 LYS B CD    
6954 C  CE    . LYS B 417 ? 1.3693 0.7085 1.6753 -0.0411 0.2288  0.2395  1634 LYS B CE    
6955 N  NZ    . LYS B 417 ? 1.4552 0.8106 1.7459 -0.0352 0.2298  0.2600  1634 LYS B NZ    
6956 N  N     . GLN B 418 ? 1.2513 0.5564 1.6025 -0.0897 0.2146  0.1193  1635 GLN B N     
6957 C  CA    . GLN B 418 ? 1.2434 0.5157 1.6045 -0.1048 0.2224  0.1020  1635 GLN B CA    
6958 C  C     . GLN B 418 ? 1.3384 0.6207 1.6961 -0.1108 0.2124  0.0751  1635 GLN B C     
6959 O  O     . GLN B 418 ? 1.5771 0.8702 1.9255 -0.0952 0.2058  0.0715  1635 GLN B O     
6960 C  CB    . GLN B 418 ? 1.2754 0.5044 1.6384 -0.0927 0.2360  0.1116  1635 GLN B CB    
6961 C  CG    . GLN B 418 ? 1.4371 0.6275 1.8115 -0.1107 0.2473  0.0987  1635 GLN B CG    
6962 C  CD    . GLN B 418 ? 1.5462 0.7176 1.9310 -0.1209 0.2599  0.1154  1635 GLN B CD    
6963 O  OE1   . GLN B 418 ? 1.5326 0.7179 1.9143 -0.1130 0.2612  0.1379  1635 GLN B OE1   
6964 N  NE2   . GLN B 418 ? 1.5840 0.7254 1.9794 -0.1388 0.2684  0.1038  1635 GLN B NE2   
6965 N  N     . TRP B 419 ? 1.2700 0.5463 1.6355 -0.1338 0.2120  0.0567  1636 TRP B N     
6966 C  CA    . TRP B 419 ? 1.3103 0.5997 1.6709 -0.1433 0.2010  0.0308  1636 TRP B CA    
6967 C  C     . TRP B 419 ? 1.2601 0.5218 1.6133 -0.1337 0.2052  0.0179  1636 TRP B C     
6968 O  O     . TRP B 419 ? 1.3316 0.6093 1.6747 -0.1301 0.1960  0.0029  1636 TRP B O     
6969 C  CB    . TRP B 419 ? 1.4330 0.7210 1.8051 -0.1709 0.1995  0.0167  1636 TRP B CB    
6970 C  CG    . TRP B 419 ? 1.4500 0.7460 1.8179 -0.1862 0.1885  -0.0113 1636 TRP B CG    
6971 C  CD1   . TRP B 419 ? 1.5050 0.7708 1.8757 -0.2027 0.1918  -0.0310 1636 TRP B CD1   
6972 C  CD2   . TRP B 419 ? 1.2918 0.6273 1.6512 -0.1871 0.1722  -0.0220 1636 TRP B CD2   
6973 N  NE1   . TRP B 419 ? 1.4116 0.6957 1.7744 -0.2134 0.1782  -0.0532 1636 TRP B NE1   
6974 C  CE2   . TRP B 419 ? 1.2847 0.6116 1.6409 -0.2038 0.1663  -0.0476 1636 TRP B CE2   
6975 C  CE3   . TRP B 419 ? 1.2975 0.6733 1.6507 -0.1755 0.1622  -0.0127 1636 TRP B CE3   
6976 C  CZ2   . TRP B 419 ? 1.1970 0.5544 1.5438 -0.2085 0.1508  -0.0627 1636 TRP B CZ2   
6977 C  CZ3   . TRP B 419 ? 1.2973 0.7027 1.6429 -0.1804 0.1476  -0.0280 1636 TRP B CZ3   
6978 C  CH2   . TRP B 419 ? 1.2250 0.6212 1.5674 -0.1965 0.1420  -0.0522 1636 TRP B CH2   
6979 N  N     . ALA B 420 ? 1.3577 0.5779 1.7156 -0.1283 0.2199  0.0245  1637 ALA B N     
6980 C  CA    . ALA B 420 ? 1.4837 0.6743 1.8361 -0.1191 0.2262  0.0121  1637 ALA B CA    
6981 C  C     . ALA B 420 ? 1.4465 0.6557 1.7903 -0.0942 0.2215  0.0191  1637 ALA B C     
6982 O  O     . ALA B 420 ? 1.4045 0.6162 1.7401 -0.0902 0.2179  0.0023  1637 ALA B O     
6983 C  CB    . ALA B 420 ? 1.4340 0.5755 1.7949 -0.1173 0.2439  0.0202  1637 ALA B CB    
6984 N  N     . GLU B 421 ? 1.4686 0.6899 1.8140 -0.0773 0.2218  0.0440  1638 GLU B N     
6985 C  CA    . GLU B 421 ? 1.5399 0.7834 1.8790 -0.0552 0.2151  0.0504  1638 GLU B CA    
6986 C  C     . GLU B 421 ? 1.5000 0.7890 1.8312 -0.0591 0.1987  0.0417  1638 GLU B C     
6987 O  O     . GLU B 421 ? 1.5097 0.8148 1.8352 -0.0466 0.1927  0.0366  1638 GLU B O     
6988 C  CB    . GLU B 421 ? 1.6493 0.8929 1.9911 -0.0357 0.2183  0.0789  1638 GLU B CB    
6989 C  CG    . GLU B 421 ? 1.8052 1.0592 2.1482 -0.0431 0.2178  0.0959  1638 GLU B CG    
6990 C  CD    . GLU B 421 ? 1.9503 1.2128 2.2901 -0.0220 0.2168  0.1227  1638 GLU B CD    
6991 O  OE1   . GLU B 421 ? 1.9227 1.1846 2.2617 -0.0023 0.2155  0.1271  1638 GLU B OE1   
6992 O  OE2   . GLU B 421 ? 2.0593 1.3293 2.3974 -0.0251 0.2175  0.1394  1638 GLU B OE2   
6993 N  N     . PHE B 422 ? 1.4939 0.8039 1.8257 -0.0762 0.1919  0.0402  1639 PHE B N     
6994 C  CA    . PHE B 422 ? 1.5217 0.8724 1.8463 -0.0814 0.1768  0.0296  1639 PHE B CA    
6995 C  C     . PHE B 422 ? 1.6102 0.9562 1.9280 -0.0864 0.1737  0.0046  1639 PHE B C     
6996 O  O     . PHE B 422 ? 1.4823 0.8521 1.7921 -0.0772 0.1651  -0.0009 1639 PHE B O     
6997 C  CB    . PHE B 422 ? 1.3993 0.7678 1.7288 -0.1012 0.1719  0.0293  1639 PHE B CB    
6998 C  CG    . PHE B 422 ? 1.1687 0.5770 1.4922 -0.1091 0.1565  0.0165  1639 PHE B CG    
6999 C  CD1   . PHE B 422 ? 1.1428 0.5871 1.4640 -0.1038 0.1479  0.0290  1639 PHE B CD1   
7000 C  CD2   . PHE B 422 ? 1.0810 0.4891 1.4005 -0.1223 0.1508  -0.0076 1639 PHE B CD2   
7001 C  CE1   . PHE B 422 ? 1.0136 0.4930 1.3303 -0.1105 0.1344  0.0183  1639 PHE B CE1   
7002 C  CE2   . PHE B 422 ? 1.0870 0.5310 1.4010 -0.1289 0.1365  -0.0177 1639 PHE B CE2   
7003 C  CZ    . PHE B 422 ? 1.0138 0.4930 1.3274 -0.1228 0.1287  -0.0044 1639 PHE B CZ    
7004 N  N     . LEU B 423 ? 1.5563 0.8681 1.8765 -0.0997 0.1821  -0.0102 1640 LEU B N     
7005 C  CA    . LEU B 423 ? 1.5725 0.8762 1.8834 -0.1081 0.1797  -0.0358 1640 LEU B CA    
7006 C  C     . LEU B 423 ? 1.5657 0.8496 1.8718 -0.0895 0.1878  -0.0388 1640 LEU B C     
7007 O  O     . LEU B 423 ? 1.6303 0.9231 1.9256 -0.0870 0.1834  -0.0543 1640 LEU B O     
7008 C  CB    . LEU B 423 ? 1.5970 0.8720 1.9124 -0.1307 0.1848  -0.0496 1640 LEU B CB    
7009 C  CG    . LEU B 423 ? 1.6486 0.9221 1.9583 -0.1539 0.1776  -0.0749 1640 LEU B CG    
7010 C  CD1   . LEU B 423 ? 1.7129 1.0301 2.0246 -0.1630 0.1627  -0.0723 1640 LEU B CD1   
7011 C  CD2   . LEU B 423 ? 1.6515 0.8899 1.9727 -0.1707 0.1874  -0.0770 1640 LEU B CD2   
7012 N  N     . GLN B 424 ? 1.5108 0.7724 1.8251 -0.0742 0.1992  -0.0219 1641 GLN B N     
7013 C  CA    . GLN B 424 ? 1.3913 0.6406 1.7051 -0.0529 0.2063  -0.0199 1641 GLN B CA    
7014 C  C     . GLN B 424 ? 1.3489 0.6383 1.6596 -0.0367 0.1954  -0.0121 1641 GLN B C     
7015 O  O     . GLN B 424 ? 1.1672 0.4625 1.4719 -0.0297 0.1945  -0.0242 1641 GLN B O     
7016 C  CB    . GLN B 424 ? 1.3317 0.5485 1.6569 -0.0409 0.2201  -0.0014 1641 GLN B CB    
7017 N  N     . PHE B 425 ? 1.2955 0.6113 1.6101 -0.0302 0.1880  0.0083  1642 PHE B N     
7018 C  CA    . PHE B 425 ? 1.2890 0.6450 1.6000 -0.0182 0.1758  0.0143  1642 PHE B CA    
7019 C  C     . PHE B 425 ? 1.3653 0.7437 1.6657 -0.0292 0.1662  -0.0064 1642 PHE B C     
7020 O  O     . PHE B 425 ? 1.3630 0.7592 1.6599 -0.0186 0.1617  -0.0107 1642 PHE B O     
7021 C  CB    . PHE B 425 ? 1.2627 0.6456 1.5746 -0.0173 0.1671  0.0337  1642 PHE B CB    
7022 C  CG    . PHE B 425 ? 1.3630 0.7292 1.6821 -0.0056 0.1745  0.0571  1642 PHE B CG    
7023 C  CD1   . PHE B 425 ? 1.1320 0.4719 1.4580 0.0106  0.1845  0.0641  1642 PHE B CD1   
7024 C  CD2   . PHE B 425 ? 1.3796 0.7565 1.6981 -0.0105 0.1716  0.0727  1642 PHE B CD2   
7025 C  CE1   . PHE B 425 ? 1.1516 0.4767 1.4832 0.0218  0.1903  0.0869  1642 PHE B CE1   
7026 C  CE2   . PHE B 425 ? 1.3916 0.7524 1.7139 0.0002  0.1785  0.0953  1642 PHE B CE2   
7027 C  CZ    . PHE B 425 ? 1.1467 0.4819 1.4753 0.0164  0.1871  0.1027  1642 PHE B CZ    
7028 N  N     . LEU B 426 ? 1.5018 0.8794 1.7979 -0.0506 0.1628  -0.0192 1643 LEU B N     
7029 C  CA    . LEU B 426 ? 1.4677 0.8673 1.7528 -0.0610 0.1524  -0.0377 1643 LEU B CA    
7030 C  C     . LEU B 426 ? 1.3576 0.7381 1.6345 -0.0579 0.1586  -0.0561 1643 LEU B C     
7031 O  O     . LEU B 426 ? 1.1365 0.5376 1.4035 -0.0570 0.1514  -0.0667 1643 LEU B O     
7032 C  CB    . LEU B 426 ? 1.5054 0.9071 1.7895 -0.0847 0.1472  -0.0472 1643 LEU B CB    
7033 C  CG    . LEU B 426 ? 1.3975 0.8238 1.6703 -0.0966 0.1347  -0.0649 1643 LEU B CG    
7034 C  CD1   . LEU B 426 ? 1.2621 0.7313 1.5349 -0.0916 0.1222  -0.0537 1643 LEU B CD1   
7035 C  CD2   . LEU B 426 ? 1.3714 0.7864 1.6442 -0.1206 0.1325  -0.0793 1643 LEU B CD2   
7036 N  N     . GLU B 427 ? 1.5633 0.9033 1.8434 -0.0561 0.1729  -0.0601 1644 GLU B N     
7037 C  CA    . GLU B 427 ? 1.5873 0.9075 1.8598 -0.0495 0.1813  -0.0757 1644 GLU B CA    
7038 C  C     . GLU B 427 ? 1.6150 0.9497 1.8930 -0.0256 0.1832  -0.0648 1644 GLU B C     
7039 O  O     . GLU B 427 ? 1.5974 0.9375 1.8674 -0.0205 0.1840  -0.0770 1644 GLU B O     
7040 C  CB    . GLU B 427 ? 1.5720 0.8434 1.8470 -0.0533 0.1969  -0.0826 1644 GLU B CB    
7041 N  N     . THR B 428 ? 1.6054 0.9471 1.8972 -0.0107 0.1838  -0.0415 1645 THR B N     
7042 C  CA    . THR B 428 ? 1.4760 0.8319 1.7765 0.0122  0.1846  -0.0295 1645 THR B CA    
7043 C  C     . THR B 428 ? 1.5123 0.9143 1.8096 0.0166  0.1696  -0.0259 1645 THR B C     
7044 O  O     . THR B 428 ? 1.3721 0.7906 1.6795 0.0343  0.1673  -0.0110 1645 THR B O     
7045 C  CB    . THR B 428 ? 1.3621 0.7078 1.6774 0.0269  0.1895  -0.0054 1645 THR B CB    
7046 O  OG1   . THR B 428 ? 1.2375 0.6155 1.5538 0.0278  0.1764  0.0113  1645 THR B OG1   
7047 C  CG2   . THR B 428 ? 1.3036 0.6058 1.6223 0.0193  0.2024  -0.0050 1645 THR B CG2   
7048 N  N     . LYS B 429 ? 1.6158 1.0390 1.9008 0.0011  0.1589  -0.0375 1646 LYS B N     
7049 C  CA    . LYS B 429 ? 1.6267 1.0897 1.9069 0.0041  0.1462  -0.0378 1646 LYS B CA    
7050 C  C     . LYS B 429 ? 1.6318 1.1242 1.9191 0.0117  0.1355  -0.0168 1646 LYS B C     
7051 O  O     . LYS B 429 ? 1.5798 1.0986 1.8703 0.0235  0.1287  -0.0104 1646 LYS B O     
7052 C  CB    . LYS B 429 ? 1.6876 1.1531 1.9684 0.0171  0.1513  -0.0452 1646 LYS B CB    
7053 N  N     . ASN B 430 ? 1.6564 1.1464 1.9446 0.0031  0.1332  -0.0076 1647 ASN B N     
7054 C  CA    . ASN B 430 ? 1.5202 1.0378 1.8110 0.0090  0.1231  0.0106  1647 ASN B CA    
7055 C  C     . ASN B 430 ? 1.3768 0.9009 1.6633 -0.0073 0.1183  0.0124  1647 ASN B C     
7056 O  O     . ASN B 430 ? 1.1197 0.6278 1.4035 -0.0235 0.1219  0.0001  1647 ASN B O     
7057 C  CB    . ASN B 430 ? 1.5097 1.0176 1.8113 0.0273  0.1279  0.0307  1647 ASN B CB    
7058 C  CG    . ASN B 430 ? 1.4128 0.8831 1.7200 0.0260  0.1408  0.0358  1647 ASN B CG    
7059 O  OD1   . ASN B 430 ? 1.5306 0.9759 1.8355 0.0141  0.1490  0.0213  1647 ASN B OD1   
7060 N  ND2   . ASN B 430 ? 1.2040 0.6688 1.5182 0.0392  0.1427  0.0568  1647 ASN B ND2   
7061 N  N     . ILE B 431 ? 1.3799 0.9284 1.6660 -0.0031 0.1098  0.0276  1648 ILE B N     
7062 C  CA    . ILE B 431 ? 1.3614 0.9230 1.6439 -0.0176 0.1046  0.0290  1648 ILE B CA    
7063 C  C     . ILE B 431 ? 1.4856 1.0353 1.7724 -0.0150 0.1100  0.0484  1648 ILE B C     
7064 O  O     . ILE B 431 ? 1.5642 1.1097 1.8535 0.0010  0.1119  0.0643  1648 ILE B O     
7065 C  CB    . ILE B 431 ? 1.3041 0.9043 1.5799 -0.0176 0.0909  0.0278  1648 ILE B CB    
7066 C  CG1   . ILE B 431 ? 1.1624 0.7816 1.4377 -0.0011 0.0849  0.0455  1648 ILE B CG1   
7067 C  CG2   . ILE B 431 ? 1.3739 0.9830 1.6450 -0.0186 0.0870  0.0102  1648 ILE B CG2   
7068 C  CD1   . ILE B 431 ? 1.4003 1.0297 1.6727 -0.0028 0.0822  0.0610  1648 ILE B CD1   
7069 N  N     . ILE B 432 ? 1.3851 0.9307 1.6731 -0.0309 0.1122  0.0475  1649 ILE B N     
7070 C  CA    . ILE B 432 ? 1.1970 0.7197 1.4904 -0.0329 0.1221  0.0616  1649 ILE B CA    
7071 C  C     . ILE B 432 ? 1.1940 0.7370 1.4854 -0.0399 0.1182  0.0721  1649 ILE B C     
7072 O  O     . ILE B 432 ? 1.1165 0.6748 1.4088 -0.0551 0.1136  0.0616  1649 ILE B O     
7073 C  CB    . ILE B 432 ? 1.1571 0.6473 1.4572 -0.0475 0.1324  0.0497  1649 ILE B CB    
7074 C  CG1   . ILE B 432 ? 1.1357 0.6059 1.4355 -0.0425 0.1368  0.0356  1649 ILE B CG1   
7075 C  CG2   . ILE B 432 ? 1.2302 0.6933 1.5368 -0.0477 0.1443  0.0659  1649 ILE B CG2   
7076 C  CD1   . ILE B 432 ? 1.1140 0.5897 1.4089 -0.0570 0.1318  0.0116  1649 ILE B CD1   
7077 N  N     . MET B 433 ? 1.2330 0.7750 1.5220 -0.0288 0.1208  0.0931  1650 MET B N     
7078 C  CA    . MET B 433 ? 1.2137 0.7673 1.5006 -0.0354 0.1214  0.1047  1650 MET B CA    
7079 C  C     . MET B 433 ? 1.0893 0.6131 1.3851 -0.0463 0.1350  0.1100  1650 MET B C     
7080 O  O     . MET B 433 ? 1.0104 0.5069 1.3078 -0.0377 0.1441  0.1216  1650 MET B O     
7081 C  CB    . MET B 433 ? 0.9420 0.5086 1.2183 -0.0185 0.1173  0.1246  1650 MET B CB    
7082 C  CG    . MET B 433 ? 1.3116 0.9124 1.5798 -0.0209 0.1077  0.1251  1650 MET B CG    
7083 S  SD    . MET B 433 ? 1.3070 0.9319 1.5616 -0.0006 0.0949  0.1341  1650 MET B SD    
7084 N  N     . ALA B 434 ? 1.1075 0.6379 1.4100 -0.0647 0.1363  0.1031  1651 ALA B N     
7085 C  CA    . ALA B 434 ? 1.0093 0.5139 1.3233 -0.0787 0.1486  0.1050  1651 ALA B CA    
7086 C  C     . ALA B 434 ? 1.0285 0.5512 1.3468 -0.0902 0.1500  0.1123  1651 ALA B C     
7087 O  O     . ALA B 434 ? 1.1797 0.7352 1.4940 -0.0916 0.1402  0.1085  1651 ALA B O     
7088 C  CB    . ALA B 434 ? 1.1211 0.6104 1.4441 -0.0940 0.1493  0.0827  1651 ALA B CB    
7089 N  N     . PRO B 435 ? 1.0794 0.5811 1.4060 -0.0977 0.1630  0.1235  1652 PRO B N     
7090 C  CA    . PRO B 435 ? 1.2934 0.8113 1.6269 -0.1095 0.1667  0.1307  1652 PRO B CA    
7091 C  C     . PRO B 435 ? 1.3669 0.8963 1.7166 -0.1315 0.1628  0.1116  1652 PRO B C     
7092 O  O     . PRO B 435 ? 1.3778 0.8848 1.7383 -0.1437 0.1662  0.0993  1652 PRO B O     
7093 C  CB    . PRO B 435 ? 1.3666 0.8533 1.7042 -0.1098 0.1833  0.1491  1652 PRO B CB    
7094 C  CG    . PRO B 435 ? 1.2705 0.7215 1.6107 -0.1065 0.1882  0.1438  1652 PRO B CG    
7095 C  CD    . PRO B 435 ? 1.1022 0.5640 1.4316 -0.0931 0.1759  0.1332  1652 PRO B CD    
7096 N  N     . PHE B 436 ? 1.3419 0.9059 1.6935 -0.1366 0.1555  0.1094  1653 PHE B N     
7097 C  CA    . PHE B 436 ? 1.3140 0.8962 1.6795 -0.1547 0.1475  0.0907  1653 PHE B CA    
7098 C  C     . PHE B 436 ? 1.3005 0.9041 1.6797 -0.1660 0.1513  0.0979  1653 PHE B C     
7099 O  O     . PHE B 436 ? 1.2689 0.8882 1.6400 -0.1561 0.1540  0.1133  1653 PHE B O     
7100 C  CB    . PHE B 436 ? 1.3084 0.9160 1.6629 -0.1484 0.1314  0.0768  1653 PHE B CB    
7101 C  CG    . PHE B 436 ? 1.3384 0.9644 1.7046 -0.1656 0.1216  0.0576  1653 PHE B CG    
7102 C  CD1   . PHE B 436 ? 1.3321 0.9401 1.7131 -0.1839 0.1241  0.0453  1653 PHE B CD1   
7103 C  CD2   . PHE B 436 ? 1.3761 1.0372 1.7378 -0.1633 0.1091  0.0519  1653 PHE B CD2   
7104 C  CE1   . PHE B 436 ? 1.3474 0.9736 1.7384 -0.1997 0.1132  0.0278  1653 PHE B CE1   
7105 C  CE2   . PHE B 436 ? 1.3587 1.0376 1.7305 -0.1782 0.0989  0.0353  1653 PHE B CE2   
7106 C  CZ    . PHE B 436 ? 1.3909 1.0530 1.7772 -0.1964 0.1005  0.0234  1653 PHE B CZ    
7107 N  N     . CYS B 437 ? 1.2936 0.8963 1.6939 -0.1868 0.1520  0.0867  1654 CYS B N     
7108 C  CA    . CYS B 437 ? 1.2055 0.8310 1.6242 -0.1995 0.1551  0.0913  1654 CYS B CA    
7109 C  C     . CYS B 437 ? 1.0913 0.7579 1.5077 -0.1969 0.1421  0.0856  1654 CYS B C     
7110 O  O     . CYS B 437 ? 1.1581 0.8462 1.5821 -0.1981 0.1464  0.0958  1654 CYS B O     
7111 C  CB    . CYS B 437 ? 1.2676 0.8823 1.7122 -0.2232 0.1579  0.0801  1654 CYS B CB    
7112 S  SG    . CYS B 437 ? 1.1584 0.7879 1.6112 -0.2386 0.1393  0.0518  1654 CYS B SG    
7113 N  N     . GLY B 438 ? 1.0325 0.7097 1.4377 -0.1923 0.1274  0.0706  1655 GLY B N     
7114 C  CA    . GLY B 438 ? 0.9753 0.6899 1.3796 -0.1907 0.1153  0.0650  1655 GLY B CA    
7115 C  C     . GLY B 438 ? 0.9408 0.6735 1.3650 -0.2095 0.1057  0.0487  1655 GLY B C     
7116 O  O     . GLY B 438 ? 0.9753 0.7386 1.3992 -0.2084 0.0942  0.0427  1655 GLY B O     
7117 N  N     . GLU B 439 ? 1.0240 0.7395 1.4665 -0.2270 0.1098  0.0422  1656 GLU B N     
7118 C  CA    . GLU B 439 ? 1.0486 0.7822 1.5112 -0.2457 0.0995  0.0272  1656 GLU B CA    
7119 C  C     . GLU B 439 ? 1.0523 0.7860 1.5012 -0.2463 0.0837  0.0071  1656 GLU B C     
7120 O  O     . GLU B 439 ? 0.9758 0.6869 1.4046 -0.2366 0.0837  0.0026  1656 GLU B O     
7121 C  CB    . GLU B 439 ? 1.0374 0.7513 1.5241 -0.2656 0.1081  0.0255  1656 GLU B CB    
7122 C  CG    . GLU B 439 ? 1.1575 0.8731 1.6599 -0.2671 0.1243  0.0452  1656 GLU B CG    
7123 C  CD    . GLU B 439 ? 1.2525 1.0083 1.7722 -0.2708 0.1210  0.0495  1656 GLU B CD    
7124 O  OE1   . GLU B 439 ? 1.3187 1.0934 1.8601 -0.2871 0.1108  0.0370  1656 GLU B OE1   
7125 O  OE2   . GLU B 439 ? 1.2561 1.0244 1.7674 -0.2569 0.1282  0.0652  1656 GLU B OE2   
7126 N  N     . ILE B 440 ? 1.1117 0.8727 1.5721 -0.2572 0.0703  -0.0045 1657 ILE B N     
7127 C  CA    . ILE B 440 ? 1.1395 0.9028 1.5862 -0.2589 0.0547  -0.0234 1657 ILE B CA    
7128 C  C     . ILE B 440 ? 1.1295 0.8619 1.5785 -0.2737 0.0546  -0.0383 1657 ILE B C     
7129 O  O     . ILE B 440 ? 1.0175 0.7291 1.4459 -0.2685 0.0518  -0.0490 1657 ILE B O     
7130 C  CB    . ILE B 440 ? 1.0988 0.9010 1.5561 -0.2651 0.0399  -0.0298 1657 ILE B CB    
7131 C  CG1   . ILE B 440 ? 1.1075 0.9367 1.5580 -0.2481 0.0404  -0.0164 1657 ILE B CG1   
7132 C  CG2   . ILE B 440 ? 0.9655 0.7684 1.4085 -0.2694 0.0234  -0.0501 1657 ILE B CG2   
7133 C  CD1   . ILE B 440 ? 0.8222 0.6893 1.2826 -0.2513 0.0270  -0.0207 1657 ILE B CD1   
7134 N  N     . SER B 441 ? 1.2636 0.9927 1.7384 -0.2928 0.0580  -0.0395 1658 SER B N     
7135 C  CA    . SER B 441 ? 1.2685 0.9644 1.7481 -0.3087 0.0602  -0.0524 1658 SER B CA    
7136 C  C     . SER B 441 ? 1.2685 0.9244 1.7268 -0.2967 0.0714  -0.0509 1658 SER B C     
7137 O  O     . SER B 441 ? 1.2581 0.8924 1.7005 -0.2985 0.0665  -0.0672 1658 SER B O     
7138 C  CB    . SER B 441 ? 1.3081 1.0042 1.8209 -0.3269 0.0685  -0.0458 1658 SER B CB    
7139 N  N     . CYS B 442 ? 1.2722 0.9199 1.7279 -0.2824 0.0858  -0.0310 1659 CYS B N     
7140 C  CA    . CYS B 442 ? 1.2616 0.8710 1.7026 -0.2715 0.0978  -0.0268 1659 CYS B CA    
7141 C  C     . CYS B 442 ? 1.3407 0.9486 1.7540 -0.2531 0.0917  -0.0321 1659 CYS B C     
7142 O  O     . CYS B 442 ? 1.4548 1.0316 1.8552 -0.2490 0.0957  -0.0396 1659 CYS B O     
7143 C  CB    . CYS B 442 ? 1.1701 0.7731 1.6160 -0.2616 0.1138  -0.0029 1659 CYS B CB    
7144 S  SG    . CYS B 442 ? 1.0686 0.6278 1.4989 -0.2462 0.1287  0.0071  1659 CYS B SG    
7145 N  N     . GLU B 443 ? 1.3599 1.0008 1.7646 -0.2422 0.0825  -0.0288 1660 GLU B N     
7146 C  CA    . GLU B 443 ? 1.2387 0.8820 1.6195 -0.2266 0.0755  -0.0350 1660 GLU B CA    
7147 C  C     . GLU B 443 ? 1.1478 0.7812 1.5201 -0.2367 0.0658  -0.0581 1660 GLU B C     
7148 O  O     . GLU B 443 ? 1.1278 0.7396 1.4824 -0.2279 0.0676  -0.0655 1660 GLU B O     
7149 C  CB    . GLU B 443 ? 1.1160 0.7985 1.4927 -0.2165 0.0668  -0.0278 1660 GLU B CB    
7150 C  CG    . GLU B 443 ? 1.1531 0.8407 1.5071 -0.1982 0.0615  -0.0293 1660 GLU B CG    
7151 C  CD    . GLU B 443 ? 1.1966 0.9180 1.5472 -0.1867 0.0564  -0.0183 1660 GLU B CD    
7152 O  OE1   . GLU B 443 ? 1.2075 0.9409 1.5699 -0.1875 0.0619  -0.0044 1660 GLU B OE1   
7153 O  OE2   . GLU B 443 ? 1.1817 0.9167 1.5175 -0.1772 0.0474  -0.0239 1660 GLU B OE2   
7154 N  N     . ASP B 444 ? 1.2033 0.8514 1.5882 -0.2554 0.0558  -0.0695 1661 ASP B N     
7155 C  CA    . ASP B 444 ? 1.2298 0.8682 1.6054 -0.2670 0.0456  -0.0919 1661 ASP B CA    
7156 C  C     . ASP B 444 ? 1.2963 0.8900 1.6680 -0.2727 0.0559  -0.1002 1661 ASP B C     
7157 O  O     . ASP B 444 ? 1.3438 0.9177 1.6953 -0.2689 0.0544  -0.1140 1661 ASP B O     
7158 C  CB    . ASP B 444 ? 1.2593 0.9225 1.6528 -0.2870 0.0326  -0.1005 1661 ASP B CB    
7159 C  CG    . ASP B 444 ? 1.3161 1.0237 1.7123 -0.2807 0.0216  -0.0939 1661 ASP B CG    
7160 O  OD1   . ASP B 444 ? 1.3307 1.0613 1.7503 -0.2875 0.0215  -0.0844 1661 ASP B OD1   
7161 O  OD2   . ASP B 444 ? 1.3338 1.0528 1.7095 -0.2687 0.0137  -0.0981 1661 ASP B OD2   
7162 N  N     . ARG B 445 ? 1.3149 0.8908 1.7057 -0.2811 0.0676  -0.0916 1662 ARG B N     
7163 C  CA    . ARG B 445 ? 1.2964 0.8271 1.6847 -0.2861 0.0788  -0.0984 1662 ARG B CA    
7164 C  C     . ARG B 445 ? 1.2155 0.7233 1.5846 -0.2639 0.0892  -0.0919 1662 ARG B C     
7165 O  O     . ARG B 445 ? 1.1138 0.5890 1.4703 -0.2637 0.0936  -0.1046 1662 ARG B O     
7166 C  CB    . ARG B 445 ? 1.2328 0.7492 1.6465 -0.2989 0.0904  -0.0881 1662 ARG B CB    
7167 N  N     . ILE B 446 ? 1.2571 0.7818 1.6236 -0.2451 0.0930  -0.0728 1663 ILE B N     
7168 C  CA    . ILE B 446 ? 1.2362 0.7438 1.5870 -0.2234 0.1013  -0.0653 1663 ILE B CA    
7169 C  C     . ILE B 446 ? 1.2432 0.7513 1.5731 -0.2169 0.0932  -0.0819 1663 ILE B C     
7170 O  O     . ILE B 446 ? 1.0508 0.5285 1.3697 -0.2101 0.1006  -0.0887 1663 ILE B O     
7171 C  CB    . ILE B 446 ? 1.1538 0.6841 1.5051 -0.2060 0.1037  -0.0426 1663 ILE B CB    
7172 C  CG1   . ILE B 446 ? 1.3636 0.8847 1.7320 -0.2099 0.1156  -0.0248 1663 ILE B CG1   
7173 C  CG2   . ILE B 446 ? 1.0060 0.5274 1.3408 -0.1830 0.1074  -0.0367 1663 ILE B CG2   
7174 C  CD1   . ILE B 446 ? 1.4029 0.9357 1.7675 -0.1911 0.1210  -0.0016 1663 ILE B CD1   
7175 N  N     . LYS B 447 ? 1.0899 0.6318 1.4140 -0.2188 0.0788  -0.0883 1664 LYS B N     
7176 C  CA    . LYS B 447 ? 1.3300 0.8721 1.6334 -0.2133 0.0718  -0.1037 1664 LYS B CA    
7177 C  C     . LYS B 447 ? 1.4693 0.9806 1.7655 -0.2279 0.0723  -0.1253 1664 LYS B C     
7178 O  O     . LYS B 447 ? 1.4932 0.9805 1.7733 -0.2199 0.0778  -0.1345 1664 LYS B O     
7179 C  CB    . LYS B 447 ? 1.4077 0.9899 1.7060 -0.2138 0.0562  -0.1069 1664 LYS B CB    
7180 C  CG    . LYS B 447 ? 1.3858 0.9694 1.6613 -0.2026 0.0518  -0.1171 1664 LYS B CG    
7181 C  CD    . LYS B 447 ? 1.4449 1.0318 1.7096 -0.2175 0.0397  -0.1379 1664 LYS B CD    
7182 C  CE    . LYS B 447 ? 1.4898 1.0814 1.7313 -0.2068 0.0353  -0.1470 1664 LYS B CE    
7183 N  NZ    . LYS B 447 ? 1.4452 1.0616 1.6792 -0.2176 0.0187  -0.1582 1664 LYS B NZ    
7184 N  N     . ALA B 448 ? 1.4825 0.9932 1.7912 -0.2495 0.0671  -0.1335 1665 ALA B N     
7185 C  CA    . ALA B 448 ? 1.5246 1.0076 1.8250 -0.2654 0.0652  -0.1558 1665 ALA B CA    
7186 C  C     . ALA B 448 ? 1.6394 1.0756 1.9364 -0.2613 0.0819  -0.1578 1665 ALA B C     
7187 O  O     . ALA B 448 ? 1.7430 1.1536 2.0210 -0.2607 0.0841  -0.1744 1665 ALA B O     
7188 C  CB    . ALA B 448 ? 1.4178 0.9095 1.7369 -0.2897 0.0567  -0.1622 1665 ALA B CB    
7189 N  N     . GLU B 449 ? 1.7036 1.1269 2.0179 -0.2579 0.0945  -0.1408 1666 GLU B N     
7190 C  CA    . GLU B 449 ? 1.7438 1.1218 2.0577 -0.2544 0.1109  -0.1408 1666 GLU B CA    
7191 C  C     . GLU B 449 ? 1.8388 1.2091 2.1424 -0.2284 0.1207  -0.1291 1666 GLU B C     
7192 O  O     . GLU B 449 ? 1.8671 1.2022 2.1724 -0.2210 0.1354  -0.1245 1666 GLU B O     
7193 C  CB    . GLU B 449 ? 1.6947 1.0600 2.0330 -0.2655 0.1199  -0.1286 1666 GLU B CB    
7194 C  CG    . GLU B 449 ? 1.6340 1.0026 1.9857 -0.2937 0.1108  -0.1426 1666 GLU B CG    
7195 C  CD    . GLU B 449 ? 1.6181 0.9868 1.9979 -0.3053 0.1178  -0.1279 1666 GLU B CD    
7196 O  OE1   . GLU B 449 ? 1.6727 1.0105 2.0592 -0.3001 0.1341  -0.1164 1666 GLU B OE1   
7197 O  OE2   . GLU B 449 ? 1.6078 1.0073 2.0035 -0.3196 0.1074  -0.1276 1666 GLU B OE2   
7198 N  N     . SER B 450 ? 1.9388 1.3406 2.2326 -0.2139 0.1130  -0.1240 1667 SER B N     
7199 C  CA    . SER B 450 ? 1.9298 1.3266 2.2138 -0.1903 0.1201  -0.1160 1667 SER B CA    
7200 C  C     . SER B 450 ? 1.8999 1.2948 2.1625 -0.1852 0.1162  -0.1337 1667 SER B C     
7201 O  O     . SER B 450 ? 1.9789 1.3766 2.2345 -0.1655 0.1205  -0.1275 1667 SER B O     
7202 C  CB    . SER B 450 ? 1.9277 1.3593 2.2175 -0.1759 0.1162  -0.0947 1667 SER B CB    
7203 O  OG    . SER B 450 ? 1.8815 1.3514 2.1700 -0.1837 0.1011  -0.0983 1667 SER B OG    
7204 N  N     . ALA B 451 ? 1.7402 1.1300 1.9919 -0.2021 0.1085  -0.1554 1668 ALA B N     
7205 C  CA    . ALA B 451 ? 1.5717 0.9619 1.8005 -0.1978 0.1044  -0.1718 1668 ALA B CA    
7206 C  C     . ALA B 451 ? 1.6438 0.9944 1.8621 -0.1871 0.1198  -0.1792 1668 ALA B C     
7207 O  O     . ALA B 451 ? 1.7240 1.0526 1.9245 -0.1944 0.1209  -0.1999 1668 ALA B O     
7208 C  CB    . ALA B 451 ? 1.4647 0.8591 1.6828 -0.2189 0.0914  -0.1924 1668 ALA B CB    
7209 N  N     . GLY B 465 ? 1.1692 0.6511 1.3852 -0.1606 0.0857  -0.1491 1682 GLY B N     
7210 C  CA    . GLY B 465 ? 1.2248 0.7198 1.4592 -0.1708 0.0814  -0.1380 1682 GLY B CA    
7211 C  C     . GLY B 465 ? 1.3309 0.8528 1.5759 -0.1560 0.0806  -0.1159 1682 GLY B C     
7212 O  O     . GLY B 465 ? 1.6078 1.1465 1.8448 -0.1419 0.0780  -0.1126 1682 GLY B O     
7213 N  N     . ALA B 466 ? 1.2063 0.7329 1.4681 -0.1591 0.0828  -0.1010 1683 ALA B N     
7214 C  CA    . ALA B 466 ? 1.1250 0.6723 1.3941 -0.1442 0.0835  -0.0797 1683 ALA B CA    
7215 C  C     . ALA B 466 ? 1.1978 0.7769 1.4764 -0.1527 0.0743  -0.0720 1683 ALA B C     
7216 O  O     . ALA B 466 ? 1.1788 0.7534 1.4694 -0.1680 0.0751  -0.0725 1683 ALA B O     
7217 C  CB    . ALA B 466 ? 1.0736 0.5951 1.3524 -0.1357 0.0973  -0.0649 1683 ALA B CB    
7218 N  N     . LYS B 467 ? 1.3255 0.9364 1.6000 -0.1429 0.0662  -0.0649 1684 LYS B N     
7219 C  CA    . LYS B 467 ? 1.2210 0.8627 1.5041 -0.1478 0.0589  -0.0561 1684 LYS B CA    
7220 C  C     . LYS B 467 ? 1.1763 0.8252 1.4639 -0.1336 0.0643  -0.0346 1684 LYS B C     
7221 O  O     . LYS B 467 ? 1.2678 0.9053 1.5502 -0.1181 0.0700  -0.0271 1684 LYS B O     
7222 C  CB    . LYS B 467 ? 1.0825 0.7550 1.3566 -0.1478 0.0453  -0.0640 1684 LYS B CB    
7223 N  N     . SER B 468 ? 1.1268 0.7943 1.4245 -0.1391 0.0627  -0.0247 1685 SER B N     
7224 C  CA    . SER B 468 ? 1.1079 0.7902 1.4051 -0.1258 0.0645  -0.0059 1685 SER B CA    
7225 C  C     . SER B 468 ? 1.1121 0.8169 1.3969 -0.1127 0.0554  -0.0069 1685 SER B C     
7226 O  O     . SER B 468 ? 1.0761 0.7956 1.3560 -0.1175 0.0461  -0.0199 1685 SER B O     
7227 C  CB    . SER B 468 ? 1.0797 0.7813 1.3884 -0.1348 0.0639  0.0022  1685 SER B CB    
7228 O  OG    . SER B 468 ? 1.1598 0.8896 1.4688 -0.1415 0.0522  -0.0074 1685 SER B OG    
7229 N  N     . LEU B 469 ? 1.1401 0.8464 1.4194 -0.0961 0.0579  0.0071  1686 LEU B N     
7230 C  CA    . LEU B 469 ? 1.0121 0.7413 1.2814 -0.0836 0.0494  0.0087  1686 LEU B CA    
7231 C  C     . LEU B 469 ? 0.8990 0.6515 1.1677 -0.0796 0.0464  0.0218  1686 LEU B C     
7232 O  O     . LEU B 469 ? 0.9156 0.6928 1.1827 -0.0829 0.0381  0.0173  1686 LEU B O     
7233 C  CB    . LEU B 469 ? 1.0279 0.7434 1.2916 -0.0675 0.0527  0.0131  1686 LEU B CB    
7234 C  CG    . LEU B 469 ? 1.0214 0.7092 1.2859 -0.0696 0.0590  0.0018  1686 LEU B CG    
7235 C  CD1   . LEU B 469 ? 0.9965 0.6663 1.2612 -0.0535 0.0660  0.0116  1686 LEU B CD1   
7236 C  CD2   . LEU B 469 ? 0.9090 0.6054 1.1664 -0.0738 0.0521  -0.0159 1686 LEU B CD2   
7237 N  N     . CYS B 470 ? 0.9264 0.6705 1.1955 -0.0724 0.0535  0.0382  1687 CYS B N     
7238 C  CA    . CYS B 470 ? 1.0315 0.7935 1.2994 -0.0710 0.0532  0.0505  1687 CYS B CA    
7239 C  C     . CYS B 470 ? 1.2111 0.9545 1.4821 -0.0700 0.0648  0.0661  1687 CYS B C     
7240 O  O     . CYS B 470 ? 1.3119 1.0293 1.5840 -0.0662 0.0719  0.0700  1687 CYS B O     
7241 C  CB    . CYS B 470 ? 1.0301 0.8103 1.2855 -0.0563 0.0458  0.0564  1687 CYS B CB    
7242 S  SG    . CYS B 470 ? 0.9775 0.7396 1.2254 -0.0386 0.0493  0.0697  1687 CYS B SG    
7243 N  N     . ILE B 471 ? 1.2286 0.9850 1.5007 -0.0730 0.0675  0.0754  1688 ILE B N     
7244 C  CA    . ILE B 471 ? 1.1687 0.9111 1.4389 -0.0690 0.0782  0.0934  1688 ILE B CA    
7245 C  C     . ILE B 471 ? 1.1724 0.9229 1.4251 -0.0515 0.0740  0.1052  1688 ILE B C     
7246 O  O     . ILE B 471 ? 1.1205 0.8933 1.3661 -0.0490 0.0697  0.1079  1688 ILE B O     
7247 C  CB    . ILE B 471 ? 1.0631 0.8144 1.3433 -0.0809 0.0850  0.0982  1688 ILE B CB    
7248 C  CG1   . ILE B 471 ? 1.0612 0.8151 1.3598 -0.0993 0.0839  0.0830  1688 ILE B CG1   
7249 C  CG2   . ILE B 471 ? 0.9978 0.7278 1.2777 -0.0791 0.0987  0.1155  1688 ILE B CG2   
7250 C  CD1   . ILE B 471 ? 0.9381 0.7165 1.2476 -0.1095 0.0839  0.0831  1688 ILE B CD1   
7251 N  N     . PRO B 472 ? 1.1408 0.8741 1.3866 -0.0390 0.0750  0.1125  1689 PRO B N     
7252 C  CA    . PRO B 472 ? 1.0044 0.7484 1.2346 -0.0227 0.0672  0.1205  1689 PRO B CA    
7253 C  C     . PRO B 472 ? 1.0568 0.8085 1.2741 -0.0180 0.0699  0.1358  1689 PRO B C     
7254 O  O     . PRO B 472 ? 1.1629 0.9008 1.3813 -0.0217 0.0811  0.1471  1689 PRO B O     
7255 C  CB    . PRO B 472 ? 1.0727 0.7933 1.3026 -0.0119 0.0697  0.1268  1689 PRO B CB    
7256 C  CG    . PRO B 472 ? 1.1141 0.8120 1.3588 -0.0230 0.0784  0.1189  1689 PRO B CG    
7257 C  CD    . PRO B 472 ? 1.0649 0.7672 1.3173 -0.0390 0.0842  0.1163  1689 PRO B CD    
7258 N  N     . PHE B 473 ? 1.0532 0.8259 1.2575 -0.0097 0.0602  0.1361  1690 PHE B N     
7259 C  CA    . PHE B 473 ? 1.0728 0.8513 1.2605 -0.0034 0.0622  0.1502  1690 PHE B CA    
7260 C  C     . PHE B 473 ? 1.1604 0.9177 1.3373 0.0080  0.0666  0.1675  1690 PHE B C     
7261 O  O     . PHE B 473 ? 1.0777 0.8244 1.2475 0.0076  0.0767  0.1813  1690 PHE B O     
7262 C  CB    . PHE B 473 ? 1.1058 0.9077 1.2802 0.0041  0.0499  0.1463  1690 PHE B CB    
7263 C  CG    . PHE B 473 ? 1.0761 0.8997 1.2582 -0.0053 0.0456  0.1319  1690 PHE B CG    
7264 C  CD1   . PHE B 473 ? 1.0997 0.9435 1.2719 0.0004  0.0348  0.1266  1690 PHE B CD1   
7265 C  CD2   . PHE B 473 ? 1.0587 0.8827 1.2582 -0.0196 0.0518  0.1240  1690 PHE B CD2   
7266 C  CE1   . PHE B 473 ? 1.1540 1.0170 1.3329 -0.0071 0.0308  0.1144  1690 PHE B CE1   
7267 C  CE2   . PHE B 473 ? 1.1152 0.9601 1.3219 -0.0274 0.0467  0.1117  1690 PHE B CE2   
7268 C  CZ    . PHE B 473 ? 1.2008 1.0648 1.3969 -0.0207 0.0366  0.1073  1690 PHE B CZ    
7269 N  N     . GLU B 474 ? 1.2622 1.0133 1.4384 0.0185  0.0594  0.1676  1691 GLU B N     
7270 C  CA    . GLU B 474 ? 1.3512 1.0809 1.5210 0.0298  0.0628  0.1835  1691 GLU B CA    
7271 C  C     . GLU B 474 ? 1.2641 0.9683 1.4501 0.0218  0.0753  0.1835  1691 GLU B C     
7272 O  O     . GLU B 474 ? 1.3212 1.0185 1.5216 0.0194  0.0743  0.1723  1691 GLU B O     
7273 C  CB    . GLU B 474 ? 1.4887 1.2234 1.6561 0.0435  0.0503  0.1828  1691 GLU B CB    
7274 C  CG    . GLU B 474 ? 1.7215 1.4370 1.8826 0.0573  0.0513  0.2002  1691 GLU B CG    
7275 C  CD    . GLU B 474 ? 1.8782 1.5867 2.0185 0.0617  0.0561  0.2188  1691 GLU B CD    
7276 O  OE1   . GLU B 474 ? 1.9948 1.7206 2.1196 0.0607  0.0522  0.2189  1691 GLU B OE1   
7277 O  OE2   . GLU B 474 ? 1.8209 1.5057 1.9595 0.0666  0.0645  0.2335  1691 GLU B OE2   
7278 N  N     . GLN B 475 ? 1.0984 0.7875 1.2820 0.0170  0.0880  0.1959  1692 GLN B N     
7279 C  CA    . GLN B 475 ? 1.1075 0.7716 1.3080 0.0079  0.1000  0.1947  1692 GLN B CA    
7280 C  C     . GLN B 475 ? 1.1223 0.7600 1.3216 0.0201  0.1033  0.2071  1692 GLN B C     
7281 O  O     . GLN B 475 ? 1.1896 0.8247 1.3725 0.0339  0.1006  0.2232  1692 GLN B O     
7282 C  CB    . GLN B 475 ? 1.1750 0.8325 1.3781 -0.0040 0.1137  0.2021  1692 GLN B CB    
7283 C  CG    . GLN B 475 ? 1.2119 0.8887 1.4281 -0.0209 0.1142  0.1872  1692 GLN B CG    
7284 C  CD    . GLN B 475 ? 1.1945 0.8600 1.4332 -0.0354 0.1179  0.1725  1692 GLN B CD    
7285 O  OE1   . GLN B 475 ? 1.0955 0.7370 1.3441 -0.0424 0.1298  0.1776  1692 GLN B OE1   
7286 N  NE2   . GLN B 475 ? 1.2852 0.9669 1.5307 -0.0400 0.1076  0.1539  1692 GLN B NE2   
7287 N  N     . PRO B 476 ? 1.1805 0.7980 1.3963 0.0160  0.1085  0.1995  1693 PRO B N     
7288 C  CA    . PRO B 476 ? 1.2666 0.8550 1.4836 0.0268  0.1148  0.2127  1693 PRO B CA    
7289 C  C     . PRO B 476 ? 1.5010 1.0649 1.7173 0.0215  0.1302  0.2278  1693 PRO B C     
7290 O  O     . PRO B 476 ? 1.7165 1.2628 1.9483 0.0081  0.1406  0.2206  1693 PRO B O     
7291 C  CB    . PRO B 476 ? 1.2122 0.7882 1.4472 0.0223  0.1161  0.1962  1693 PRO B CB    
7292 C  CG    . PRO B 476 ? 1.1936 0.7813 1.4378 0.0032  0.1170  0.1781  1693 PRO B CG    
7293 C  CD    . PRO B 476 ? 1.1655 0.7860 1.3981 0.0025  0.1080  0.1780  1693 PRO B CD    
7294 N  N     . ALA B 477 ? 1.5387 1.1001 1.7369 0.0311  0.1321  0.2482  1694 ALA B N     
7295 C  CA    . ALA B 477 ? 1.5497 1.0892 1.7442 0.0268  0.1476  0.2650  1694 ALA B CA    
7296 C  C     . ALA B 477 ? 1.5432 1.0954 1.7418 0.0093  0.1550  0.2596  1694 ALA B C     
7297 O  O     . ALA B 477 ? 1.5111 1.0826 1.7217 -0.0022 0.1498  0.2404  1694 ALA B O     
7298 C  CB    . ALA B 477 ? 1.4237 0.9274 1.6336 0.0245  0.1597  0.2679  1694 ALA B CB    
7299 N  N     . LYS B 478 ? 1.5340 1.0755 1.7235 0.0075  0.1674  0.2768  1695 LYS B N     
7300 C  CA    . LYS B 478 ? 1.4035 0.9576 1.5975 -0.0076 0.1760  0.2747  1695 LYS B CA    
7301 C  C     . LYS B 478 ? 1.4566 0.9885 1.6734 -0.0244 0.1919  0.2733  1695 LYS B C     
7302 O  O     . LYS B 478 ? 1.4482 0.9489 1.6664 -0.0216 0.2025  0.2862  1695 LYS B O     
7303 C  CB    . LYS B 478 ? 1.1907 0.7491 1.3595 0.0003  0.1811  0.2941  1695 LYS B CB    
7304 N  N     . ILE B 479 ? 1.3612 0.9098 1.5966 -0.0420 0.1928  0.2576  1696 ILE B N     
7305 C  CA    . ILE B 479 ? 1.3288 0.8602 1.5894 -0.0604 0.2050  0.2521  1696 ILE B CA    
7306 C  C     . ILE B 479 ? 1.4455 0.9625 1.7051 -0.0653 0.2235  0.2717  1696 ILE B C     
7307 O  O     . ILE B 479 ? 1.5506 1.0864 1.8016 -0.0658 0.2271  0.2790  1696 ILE B O     
7308 C  CB    . ILE B 479 ? 1.1420 0.6990 1.4220 -0.0770 0.1980  0.2297  1696 ILE B CB    
7309 N  N     . ASP B 480 ? 1.4211 0.9031 1.6890 -0.0685 0.2363  0.2808  1697 ASP B N     
7310 C  CA    . ASP B 480 ? 1.5488 1.0131 1.8181 -0.0744 0.2558  0.2998  1697 ASP B CA    
7311 C  C     . ASP B 480 ? 1.5278 0.9874 1.8295 -0.0986 0.2656  0.2888  1697 ASP B C     
7312 O  O     . ASP B 480 ? 1.5180 0.9502 1.8352 -0.1058 0.2701  0.2835  1697 ASP B O     
7313 C  CB    . ASP B 480 ? 1.6335 1.0604 1.8897 -0.0613 0.2645  0.3200  1697 ASP B CB    
7314 N  N     . PRO B 481 ? 1.5044 0.9891 1.8180 -0.1116 0.2694  0.2852  1698 PRO B N     
7315 C  CA    . PRO B 481 ? 1.3951 0.8816 1.7427 -0.1355 0.2744  0.2710  1698 PRO B CA    
7316 C  C     . PRO B 481 ? 1.6374 1.0879 2.0007 -0.1465 0.2929  0.2815  1698 PRO B C     
7317 O  O     . PRO B 481 ? 1.7259 1.1721 2.1180 -0.1666 0.2956  0.2682  1698 PRO B O     
7318 C  CB    . PRO B 481 ? 1.1733 0.6945 1.5278 -0.1432 0.2767  0.2711  1698 PRO B CB    
7319 C  CG    . PRO B 481 ? 1.2315 0.7724 1.5552 -0.1235 0.2679  0.2777  1698 PRO B CG    
7320 C  CD    . PRO B 481 ? 1.4262 0.9389 1.7234 -0.1050 0.2693  0.2935  1698 PRO B CD    
7321 N  N     . LYS B 482 ? 1.5913 1.0158 1.9364 -0.1345 0.3057  0.3050  1699 LYS B N     
7322 C  CA    . LYS B 482 ? 1.6076 0.9947 1.9669 -0.1440 0.3238  0.3158  1699 LYS B CA    
7323 C  C     . LYS B 482 ? 1.7708 1.1303 2.1425 -0.1482 0.3192  0.3017  1699 LYS B C     
7324 O  O     . LYS B 482 ? 1.9262 1.2554 2.3164 -0.1611 0.3328  0.3042  1699 LYS B O     
7325 C  CB    . LYS B 482 ? 1.5637 0.9276 1.8968 -0.1277 0.3371  0.3450  1699 LYS B CB    
7326 N  N     . VAL B 483 ? 1.7637 1.1310 2.1250 -0.1372 0.3016  0.2876  1700 VAL B N     
7327 C  CA    . VAL B 483 ? 1.7293 1.0681 2.0991 -0.1385 0.2988  0.2753  1700 VAL B CA    
7328 C  C     . VAL B 483 ? 1.6844 1.0458 2.0600 -0.1426 0.2799  0.2478  1700 VAL B C     
7329 O  O     . VAL B 483 ? 1.7473 1.0963 2.1419 -0.1577 0.2789  0.2296  1700 VAL B O     
7330 C  CB    . VAL B 483 ? 1.7052 1.0148 2.0534 -0.1160 0.3012  0.2923  1700 VAL B CB    
7331 C  CG1   . VAL B 483 ? 1.7043 1.0393 2.0250 -0.0938 0.2872  0.2986  1700 VAL B CG1   
7332 C  CG2   . VAL B 483 ? 1.6765 0.9571 2.0346 -0.1169 0.2992  0.2784  1700 VAL B CG2   
7333 N  N     . ASP B 484 ? 1.5340 0.9267 1.8922 -0.1291 0.2650  0.2445  1701 ASP B N     
7334 C  CA    . ASP B 484 ? 1.4789 0.8896 1.8384 -0.1293 0.2475  0.2207  1701 ASP B CA    
7335 C  C     . ASP B 484 ? 1.3944 0.8222 1.7774 -0.1527 0.2434  0.1996  1701 ASP B C     
7336 O  O     . ASP B 484 ? 1.3688 0.8239 1.7595 -0.1617 0.2436  0.2007  1701 ASP B O     
7337 C  CB    . ASP B 484 ? 1.5007 0.9446 1.8390 -0.1126 0.2335  0.2226  1701 ASP B CB    
7338 C  CG    . ASP B 484 ? 1.5154 0.9459 1.8304 -0.0895 0.2341  0.2416  1701 ASP B CG    
7339 O  OD1   . ASP B 484 ? 1.5489 0.9452 1.8648 -0.0840 0.2411  0.2476  1701 ASP B OD1   
7340 O  OD2   . ASP B 484 ? 1.4474 0.9008 1.7434 -0.0769 0.2275  0.2506  1701 ASP B OD2   
7341 N  N     . LYS B 485 ? 1.3423 0.7560 1.7355 -0.1613 0.2382  0.1797  1702 LYS B N     
7342 C  CA    . LYS B 485 ? 1.2667 0.6950 1.6798 -0.1828 0.2312  0.1573  1702 LYS B CA    
7343 C  C     . LYS B 485 ? 1.2939 0.7347 1.6984 -0.1781 0.2142  0.1364  1702 LYS B C     
7344 O  O     . LYS B 485 ? 1.2925 0.7163 1.6828 -0.1629 0.2121  0.1359  1702 LYS B O     
7345 C  CB    . LYS B 485 ? 1.1948 0.5894 1.6290 -0.2021 0.2419  0.1505  1702 LYS B CB    
7346 C  CG    . LYS B 485 ? 1.2302 0.6010 1.6740 -0.2071 0.2616  0.1714  1702 LYS B CG    
7347 C  CD    . LYS B 485 ? 1.2253 0.6168 1.6935 -0.2286 0.2656  0.1700  1702 LYS B CD    
7348 C  CE    . LYS B 485 ? 1.2656 0.6277 1.7477 -0.2377 0.2860  0.1865  1702 LYS B CE    
7349 N  NZ    . LYS B 485 ? 1.3886 0.7085 1.8781 -0.2453 0.2908  0.1767  1702 LYS B NZ    
7350 N  N     . CYS B 486 ? 1.2689 0.7384 1.6833 -0.1915 0.2028  0.1190  1703 CYS B N     
7351 C  CA    . CYS B 486 ? 1.2740 0.7568 1.6795 -0.1881 0.1869  0.0991  1703 CYS B CA    
7352 C  C     . CYS B 486 ? 1.2774 0.7241 1.6816 -0.1896 0.1890  0.0864  1703 CYS B C     
7353 O  O     . CYS B 486 ? 1.2972 0.7175 1.7161 -0.2051 0.1974  0.0813  1703 CYS B O     
7354 C  CB    . CYS B 486 ? 1.2924 0.8072 1.7107 -0.2049 0.1752  0.0826  1703 CYS B CB    
7355 S  SG    . CYS B 486 ? 1.3249 0.8462 1.7344 -0.2066 0.1578  0.0551  1703 CYS B SG    
7356 N  N     . VAL B 487 ? 1.2967 0.7432 1.6840 -0.1738 0.1814  0.0804  1704 VAL B N     
7357 C  CA    . VAL B 487 ? 1.2119 0.6230 1.5945 -0.1691 0.1856  0.0722  1704 VAL B CA    
7358 C  C     . VAL B 487 ? 1.2250 0.6224 1.6175 -0.1895 0.1829  0.0481  1704 VAL B C     
7359 O  O     . VAL B 487 ? 1.1714 0.5313 1.5648 -0.1913 0.1910  0.0417  1704 VAL B O     
7360 C  CB    . VAL B 487 ? 1.1945 0.6160 1.5585 -0.1473 0.1771  0.0714  1704 VAL B CB    
7361 C  CG1   . VAL B 487 ? 1.1469 0.6085 1.5053 -0.1491 0.1609  0.0588  1704 VAL B CG1   
7362 C  CG2   . VAL B 487 ? 1.2394 0.6280 1.5991 -0.1415 0.1810  0.0607  1704 VAL B CG2   
7363 N  N     . HIS B 488 ? 1.2874 0.7125 1.6880 -0.2058 0.1722  0.0348  1705 HIS B N     
7364 C  CA    . HIS B 488 ? 1.4376 0.8481 1.8458 -0.2256 0.1686  0.0117  1705 HIS B CA    
7365 C  C     . HIS B 488 ? 1.5151 0.9004 1.9438 -0.2438 0.1807  0.0152  1705 HIS B C     
7366 O  O     . HIS B 488 ? 1.4233 0.8249 1.8670 -0.2516 0.1844  0.0276  1705 HIS B O     
7367 C  CB    . HIS B 488 ? 1.3821 0.8291 1.7920 -0.2372 0.1517  -0.0046 1705 HIS B CB    
7368 C  CG    . HIS B 488 ? 1.3835 0.8155 1.7967 -0.2562 0.1458  -0.0293 1705 HIS B CG    
7369 N  ND1   . HIS B 488 ? 1.3810 0.7773 1.7826 -0.2538 0.1498  -0.0422 1705 HIS B ND1   
7370 C  CD2   . HIS B 488 ? 1.4042 0.8511 1.8310 -0.2782 0.1362  -0.0436 1705 HIS B CD2   
7371 C  CE1   . HIS B 488 ? 1.3981 0.7869 1.8031 -0.2736 0.1428  -0.0640 1705 HIS B CE1   
7372 N  NE2   . HIS B 488 ? 1.4111 0.8308 1.8317 -0.2889 0.1337  -0.0651 1705 HIS B NE2   
7373 N  N     . PRO B 489 ? 1.5530 0.8977 1.9831 -0.2509 0.1880  0.0044  1706 PRO B N     
7374 C  CA    . PRO B 489 ? 1.5120 0.8283 1.9619 -0.2676 0.2011  0.0088  1706 PRO B CA    
7375 C  C     . PRO B 489 ? 1.5702 0.9052 2.0420 -0.2942 0.1944  -0.0019 1706 PRO B C     
7376 O  O     . PRO B 489 ? 1.7656 1.0850 2.2574 -0.3082 0.2055  0.0056  1706 PRO B O     
7377 C  CB    . PRO B 489 ? 1.4326 0.7021 1.8756 -0.2679 0.2080  -0.0042 1706 PRO B CB    
7378 C  CG    . PRO B 489 ? 1.5091 0.7797 1.9298 -0.2440 0.2048  -0.0040 1706 PRO B CG    
7379 C  CD    . PRO B 489 ? 1.5092 0.8281 1.9221 -0.2399 0.1881  -0.0079 1706 PRO B CD    
7380 N  N     . ALA B 490 ? 1.5084 0.8752 1.9781 -0.3018 0.1770  -0.0189 1707 ALA B N     
7381 C  CA    . ALA B 490 ? 1.4062 0.7927 1.8987 -0.3269 0.1692  -0.0290 1707 ALA B CA    
7382 C  C     . ALA B 490 ? 1.5166 0.9422 2.0247 -0.3270 0.1693  -0.0114 1707 ALA B C     
7383 O  O     . ALA B 490 ? 1.8638 1.3005 2.3982 -0.3472 0.1696  -0.0122 1707 ALA B O     
7384 C  CB    . ALA B 490 ? 1.3617 0.7635 1.8456 -0.3362 0.1500  -0.0551 1707 ALA B CB    
7385 N  N     . CYS B 491 ? 1.6902 1.1410 2.1837 -0.3060 0.1672  0.0023  1708 CYS B N     
7386 C  CA    . CYS B 491 ? 1.6159 1.0975 2.1214 -0.3036 0.1713  0.0216  1708 CYS B CA    
7387 C  C     . CYS B 491 ? 1.7294 1.1862 2.2313 -0.2910 0.1904  0.0456  1708 CYS B C     
7388 O  O     . CYS B 491 ? 1.7829 1.2204 2.2635 -0.2719 0.1942  0.0519  1708 CYS B O     
7389 C  CB    . CYS B 491 ? 1.4412 0.9649 1.9329 -0.2894 0.1579  0.0225  1708 CYS B CB    
7390 S  SG    . CYS B 491 ? 1.4104 0.9328 1.8748 -0.2588 0.1636  0.0422  1708 CYS B SG    
7391 N  N     . GLY B 492 ? 1.1629 0.6222 1.6860 -0.3015 0.2021  0.0595  1709 GLY B N     
7392 C  CA    . GLY B 492 ? 1.1861 0.6213 1.7067 -0.2917 0.2212  0.0834  1709 GLY B CA    
7393 C  C     . GLY B 492 ? 1.2761 0.7423 1.7930 -0.2802 0.2247  0.1034  1709 GLY B C     
7394 O  O     . GLY B 492 ? 1.3392 0.7941 1.8580 -0.2760 0.2409  0.1249  1709 GLY B O     
7395 N  N     . ARG B 493 ? 1.2674 0.7727 1.7785 -0.2757 0.2096  0.0957  1710 ARG B N     
7396 C  CA    . ARG B 493 ? 1.2983 0.8350 1.8042 -0.2646 0.2115  0.1119  1710 ARG B CA    
7397 C  C     . ARG B 493 ? 1.3061 0.8269 1.7847 -0.2405 0.2196  0.1314  1710 ARG B C     
7398 O  O     . ARG B 493 ? 1.3053 0.8053 1.7653 -0.2279 0.2160  0.1279  1710 ARG B O     
7399 C  CB    . ARG B 493 ? 1.2094 0.7863 1.7108 -0.2622 0.1927  0.0984  1710 ARG B CB    
7400 C  CG    . ARG B 493 ? 1.2781 0.8785 1.8078 -0.2847 0.1842  0.0833  1710 ARG B CG    
7401 C  CD    . ARG B 493 ? 1.2262 0.8345 1.7491 -0.2884 0.1646  0.0589  1710 ARG B CD    
7402 N  NE    . ARG B 493 ? 1.2572 0.8939 1.8055 -0.3079 0.1538  0.0459  1710 ARG B NE    
7403 C  CZ    . ARG B 493 ? 1.2032 0.8442 1.7536 -0.3192 0.1378  0.0237  1710 ARG B CZ    
7404 N  NH1   . ARG B 493 ? 1.0674 0.6850 1.5954 -0.3132 0.1317  0.0108  1710 ARG B NH1   
7405 N  NH2   . ARG B 493 ? 1.1468 0.8159 1.7221 -0.3366 0.1281  0.0146  1710 ARG B NH2   
7406 N  N     . VAL B 494 ? 1.2773 0.8065 1.7538 -0.2341 0.2313  0.1526  1711 VAL B N     
7407 C  CA    . VAL B 494 ? 1.3174 0.8380 1.7650 -0.2103 0.2354  0.1704  1711 VAL B CA    
7408 C  C     . VAL B 494 ? 1.3897 0.9347 1.8172 -0.1957 0.2174  0.1604  1711 VAL B C     
7409 O  O     . VAL B 494 ? 1.4276 1.0058 1.8619 -0.2015 0.2057  0.1481  1711 VAL B O     
7410 C  CB    . VAL B 494 ? 1.3016 0.8314 1.7470 -0.2061 0.2496  0.1933  1711 VAL B CB    
7411 N  N     . ALA B 495 ? 1.3251 0.8539 1.7290 -0.1767 0.2148  0.1656  1712 ALA B N     
7412 C  CA    . ALA B 495 ? 1.2078 0.7579 1.5945 -0.1635 0.1981  0.1556  1712 ALA B CA    
7413 C  C     . ALA B 495 ? 1.2428 0.8266 1.6190 -0.1551 0.1948  0.1647  1712 ALA B C     
7414 O  O     . ALA B 495 ? 1.0320 0.6129 1.4001 -0.1482 0.2059  0.1844  1712 ALA B O     
7415 C  CB    . ALA B 495 ? 1.1789 0.7048 1.5459 -0.1449 0.1969  0.1604  1712 ALA B CB    
7416 N  N     . LYS B 496 ? 1.2728 0.8880 1.6497 -0.1567 0.1804  0.1501  1713 LYS B N     
7417 C  CA    . LYS B 496 ? 1.2170 0.8627 1.5824 -0.1474 0.1768  0.1575  1713 LYS B CA    
7418 C  C     . LYS B 496 ? 1.2654 0.9102 1.6025 -0.1253 0.1702  0.1645  1713 LYS B C     
7419 O  O     . LYS B 496 ? 1.2527 0.9080 1.5740 -0.1143 0.1731  0.1786  1713 LYS B O     
7420 C  CB    . LYS B 496 ? 1.1353 0.8151 1.5126 -0.1568 0.1641  0.1406  1713 LYS B CB    
7421 N  N     . PHE B 497 ? 1.3724 1.0041 1.7027 -0.1188 0.1620  0.1552  1714 PHE B N     
7422 C  CA    . PHE B 497 ? 1.2684 0.9032 1.5749 -0.0982 0.1541  0.1609  1714 PHE B CA    
7423 C  C     . PHE B 497 ? 1.2169 0.8327 1.5224 -0.0934 0.1486  0.1506  1714 PHE B C     
7424 O  O     . PHE B 497 ? 1.3072 0.9094 1.6276 -0.1062 0.1500  0.1375  1714 PHE B O     
7425 C  CB    . PHE B 497 ? 1.1713 0.8420 1.4700 -0.0941 0.1416  0.1540  1714 PHE B CB    
7426 C  CG    . PHE B 497 ? 1.1779 0.8678 1.4936 -0.1092 0.1337  0.1345  1714 PHE B CG    
7427 C  CD1   . PHE B 497 ? 1.2064 0.8856 1.5295 -0.1153 0.1276  0.1180  1714 PHE B CD1   
7428 C  CD2   . PHE B 497 ? 1.0655 0.7829 1.3898 -0.1171 0.1327  0.1328  1714 PHE B CD2   
7429 C  CE1   . PHE B 497 ? 1.2104 0.9057 1.5471 -0.1294 0.1194  0.1001  1714 PHE B CE1   
7430 C  CE2   . PHE B 497 ? 0.9990 0.7342 1.3396 -0.1306 0.1244  0.1157  1714 PHE B CE2   
7431 C  CZ    . PHE B 497 ? 1.1302 0.8539 1.4760 -0.1369 0.1170  0.0992  1714 PHE B CZ    
7432 N  N     . TYR B 498 ? 0.9725 0.5881 1.2605 -0.0752 0.1419  0.1558  1715 TYR B N     
7433 C  CA    . TYR B 498 ? 0.9687 0.5728 1.2563 -0.0692 0.1355  0.1445  1715 TYR B CA    
7434 C  C     . TYR B 498 ? 0.9773 0.6092 1.2634 -0.0704 0.1210  0.1269  1715 TYR B C     
7435 O  O     . TYR B 498 ? 0.9497 0.6077 1.2258 -0.0643 0.1135  0.1297  1715 TYR B O     
7436 C  CB    . TYR B 498 ? 1.0568 0.6484 1.3296 -0.0488 0.1350  0.1589  1715 TYR B CB    
7437 C  CG    . TYR B 498 ? 1.0037 0.5599 1.2793 -0.0457 0.1481  0.1724  1715 TYR B CG    
7438 C  CD1   . TYR B 498 ? 1.1485 0.6781 1.4346 -0.0484 0.1524  0.1636  1715 TYR B CD1   
7439 C  CD2   . TYR B 498 ? 1.0120 0.5594 1.2782 -0.0396 0.1568  0.1943  1715 TYR B CD2   
7440 C  CE1   . TYR B 498 ? 1.2153 0.7099 1.5045 -0.0450 0.1652  0.1764  1715 TYR B CE1   
7441 C  CE2   . TYR B 498 ? 1.0925 0.6053 1.3611 -0.0364 0.1694  0.2080  1715 TYR B CE2   
7442 C  CZ    . TYR B 498 ? 1.2112 0.6977 1.4920 -0.0390 0.1734  0.1989  1715 TYR B CZ    
7443 O  OH    . TYR B 498 ? 1.3885 0.8392 1.6721 -0.0353 0.1862  0.2124  1715 TYR B OH    
7444 N  N     . THR B 499 ? 1.0160 0.6412 1.3107 -0.0785 0.1176  0.1087  1716 THR B N     
7445 C  CA    . THR B 499 ? 1.2155 0.8632 1.5062 -0.0772 0.1043  0.0930  1716 THR B CA    
7446 C  C     . THR B 499 ? 1.2348 0.8654 1.5236 -0.0705 0.1025  0.0834  1716 THR B C     
7447 O  O     . THR B 499 ? 1.2833 0.8835 1.5771 -0.0709 0.1115  0.0843  1716 THR B O     
7448 C  CB    . THR B 499 ? 1.3099 0.9754 1.6108 -0.0949 0.0988  0.0770  1716 THR B CB    
7449 O  OG1   . THR B 499 ? 1.4345 1.0808 1.7435 -0.1058 0.1001  0.0614  1716 THR B OG1   
7450 C  CG2   . THR B 499 ? 1.3111 0.9843 1.6215 -0.1054 0.1049  0.0850  1716 THR B CG2   
7451 N  N     . LEU B 500 ? 1.0634 0.7141 1.3455 -0.0652 0.0913  0.0731  1717 LEU B N     
7452 C  CA    . LEU B 500 ? 1.0631 0.7044 1.3425 -0.0575 0.0887  0.0634  1717 LEU B CA    
7453 C  C     . LEU B 500 ? 1.0400 0.6804 1.3235 -0.0718 0.0856  0.0420  1717 LEU B C     
7454 O  O     . LEU B 500 ? 1.0310 0.6950 1.3141 -0.0807 0.0774  0.0335  1717 LEU B O     
7455 C  CB    . LEU B 500 ? 1.1101 0.7752 1.3795 -0.0428 0.0786  0.0667  1717 LEU B CB    
7456 C  CG    . LEU B 500 ? 1.0583 0.7145 1.3252 -0.0270 0.0780  0.0683  1717 LEU B CG    
7457 C  CD1   . LEU B 500 ? 1.0277 0.6577 1.2972 -0.0171 0.0876  0.0843  1717 LEU B CD1   
7458 C  CD2   . LEU B 500 ? 1.0185 0.7032 1.2772 -0.0165 0.0670  0.0726  1717 LEU B CD2   
7459 N  N     . PHE B 501 ? 1.1120 0.7242 1.3986 -0.0739 0.0923  0.0335  1718 PHE B N     
7460 C  CA    . PHE B 501 ? 1.1806 0.7869 1.4675 -0.0865 0.0899  0.0124  1718 PHE B CA    
7461 C  C     . PHE B 501 ? 1.1271 0.7232 1.4073 -0.0752 0.0903  0.0042  1718 PHE B C     
7462 O  O     . PHE B 501 ? 1.1437 0.7281 1.4242 -0.0599 0.0957  0.0148  1718 PHE B O     
7463 C  CB    . PHE B 501 ? 1.2108 0.7891 1.5070 -0.1024 0.0986  0.0060  1718 PHE B CB    
7464 C  CG    . PHE B 501 ? 1.1857 0.7692 1.4920 -0.1135 0.1014  0.0156  1718 PHE B CG    
7465 C  CD1   . PHE B 501 ? 1.2356 0.8101 1.5449 -0.1055 0.1100  0.0358  1718 PHE B CD1   
7466 C  CD2   . PHE B 501 ? 1.2855 0.8831 1.5988 -0.1317 0.0957  0.0050  1718 PHE B CD2   
7467 C  CE1   . PHE B 501 ? 1.3521 0.9307 1.6708 -0.1156 0.1144  0.0452  1718 PHE B CE1   
7468 C  CE2   . PHE B 501 ? 1.3315 0.9353 1.6571 -0.1419 0.0993  0.0142  1718 PHE B CE2   
7469 C  CZ    . PHE B 501 ? 1.4098 1.0036 1.7379 -0.1340 0.1096  0.0343  1718 PHE B CZ    
7470 N  N     . GLY B 502 ? 1.0751 0.6766 1.3495 -0.0827 0.0846  -0.0143 1719 GLY B N     
7471 C  CA    . GLY B 502 ? 1.1120 0.7020 1.3799 -0.0743 0.0868  -0.0244 1719 GLY B CA    
7472 C  C     . GLY B 502 ? 1.2235 0.8163 1.4831 -0.0871 0.0812  -0.0456 1719 GLY B C     
7473 O  O     . GLY B 502 ? 1.1622 0.7686 1.4221 -0.1017 0.0739  -0.0517 1719 GLY B O     
7474 N  N     . ARG B 503 ? 1.4206 0.9989 1.6727 -0.0813 0.0853  -0.0567 1720 ARG B N     
7475 C  CA    . ARG B 503 ? 1.4684 1.0515 1.7079 -0.0896 0.0795  -0.0759 1720 ARG B CA    
7476 C  C     . ARG B 503 ? 1.6100 1.2264 1.8435 -0.0809 0.0697  -0.0733 1720 ARG B C     
7477 O  O     . ARG B 503 ? 1.7176 1.3434 1.9551 -0.0651 0.0709  -0.0611 1720 ARG B O     
7478 C  CB    . ARG B 503 ? 1.3481 0.8997 1.5805 -0.0865 0.0899  -0.0887 1720 ARG B CB    
7479 C  CG    . ARG B 503 ? 1.3147 0.8298 1.5539 -0.0926 0.1012  -0.0898 1720 ARG B CG    
7480 C  CD    . ARG B 503 ? 1.3335 0.8254 1.5614 -0.1087 0.1027  -0.1120 1720 ARG B CD    
7481 N  NE    . ARG B 503 ? 1.4378 0.8891 1.6674 -0.1062 0.1174  -0.1163 1720 ARG B NE    
7482 C  CZ    . ARG B 503 ? 1.4797 0.9052 1.6959 -0.1107 0.1232  -0.1352 1720 ARG B CZ    
7483 N  NH1   . ARG B 503 ? 1.5145 0.9515 1.7134 -0.1184 0.1148  -0.1513 1720 ARG B NH1   
7484 N  NH2   . ARG B 503 ? 1.4036 0.7911 1.6227 -0.1070 0.1377  -0.1376 1720 ARG B NH2   
7485 N  N     . SER B 504 ? 1.6030 1.2383 1.8280 -0.0914 0.0593  -0.0837 1721 SER B N     
7486 C  CA    . SER B 504 ? 1.6145 1.2821 1.8360 -0.0839 0.0499  -0.0787 1721 SER B CA    
7487 C  C     . SER B 504 ? 1.6188 1.2976 1.8261 -0.0918 0.0417  -0.0941 1721 SER B C     
7488 O  O     . SER B 504 ? 1.5178 1.1852 1.7185 -0.1060 0.0399  -0.1077 1721 SER B O     
7489 C  CB    . SER B 504 ? 1.6731 1.3638 1.9038 -0.0851 0.0435  -0.0646 1721 SER B CB    
7490 O  OG    . SER B 504 ? 1.6914 1.4111 1.9183 -0.0772 0.0351  -0.0600 1721 SER B OG    
7491 N  N     . TYR B 505 ? 1.5714 1.2739 1.7739 -0.0829 0.0358  -0.0911 1722 TYR B N     
7492 C  CA    . TYR B 505 ? 1.5649 1.2833 1.7539 -0.0880 0.0269  -0.1018 1722 TYR B CA    
7493 C  C     . TYR B 505 ? 1.6265 1.3688 1.8190 -0.0981 0.0152  -0.0991 1722 TYR B C     
7494 O  O     . TYR B 505 ? 1.6376 1.3951 1.8415 -0.0943 0.0131  -0.0855 1722 TYR B O     
7495 C  CB    . TYR B 505 ? 1.5831 1.3184 1.7683 -0.0743 0.0257  -0.0976 1722 TYR B CB    
7496 C  CG    . TYR B 505 ? 1.6338 1.3523 1.8178 -0.0623 0.0367  -0.0993 1722 TYR B CG    
7497 C  CD1   . TYR B 505 ? 1.6666 1.3831 1.8369 -0.0605 0.0387  -0.1103 1722 TYR B CD1   
7498 C  CD2   . TYR B 505 ? 1.6229 1.3285 1.8200 -0.0521 0.0455  -0.0890 1722 TYR B CD2   
7499 C  CE1   . TYR B 505 ? 1.6478 1.3500 1.8191 -0.0491 0.0501  -0.1117 1722 TYR B CE1   
7500 C  CE2   . TYR B 505 ? 1.6062 1.2979 1.8051 -0.0403 0.0557  -0.0900 1722 TYR B CE2   
7501 C  CZ    . TYR B 505 ? 1.5970 1.2874 1.7839 -0.0389 0.0585  -0.1015 1722 TYR B CZ    
7502 O  OH    . TYR B 505 ? 1.5261 1.2034 1.7170 -0.0268 0.0700  -0.1021 1722 TYR B OH    
7503 O  OXT   . TYR B 505 ? 1.6993 1.4471 1.8832 -0.1094 0.0074  -0.1101 1722 TYR B OXT   
7504 O  "O4'" . HFG C .   ? 1.0226 1.0090 0.9671 -0.0166 -0.0714 -0.0184 1801 HFG A "O4'" 
7505 C  C21   . HFG C .   ? 1.0888 1.0662 1.0201 -0.0148 -0.0648 -0.0129 1801 HFG A C21   
7506 C  "C3'" . HFG C .   ? 1.0493 1.0180 0.9854 -0.0147 -0.0486 -0.0126 1801 HFG A "C3'" 
7507 C  "C2'" . HFG C .   ? 1.0112 0.9868 0.9770 -0.0152 -0.0439 -0.0172 1801 HFG A "C2'" 
7508 N  "N1'" . HFG C .   ? 1.0266 1.0043 0.9943 -0.0181 -0.0452 -0.0261 1801 HFG A "N1'" 
7509 C  "C6'" . HFG C .   ? 0.9806 0.9632 0.9746 -0.0178 -0.0393 -0.0293 1801 HFG A "C6'" 
7510 C  "C5'" . HFG C .   ? 0.9034 0.8973 0.9205 -0.0156 -0.0468 -0.0258 1801 HFG A "C5'" 
7511 C  "C4'" . HFG C .   ? 0.8206 0.8125 0.8358 -0.0132 -0.0466 -0.0177 1801 HFG A "C4'" 
7512 C  C39   . HFG C .   ? 0.8663 0.8530 0.8556 -0.0127 -0.0517 -0.0139 1801 HFG A C39   
7513 O  "O7'" . HFG C .   ? 0.9677 0.9508 0.9546 -0.0099 -0.0507 -0.0055 1801 HFG A "O7'" 
7514 C  "C1'" . HFG C .   ? 1.1461 1.1206 1.0557 -0.0124 -0.0724 -0.0050 1801 HFG A "C1'" 
7515 N  N3    . HFG C .   ? 1.0906 1.0706 0.9877 -0.0145 -0.0862 -0.0079 1801 HFG A N3    
7516 C  C4    . HFG C .   ? 1.1606 1.1330 1.0366 -0.0193 -0.0850 -0.0158 1801 HFG A C4    
7517 O  O11   . HFG C .   ? 1.1567 1.1172 1.0232 -0.0207 -0.0716 -0.0194 1801 HFG A O11   
7518 C  C10   . HFG C .   ? 1.2342 1.2141 1.1028 -0.0225 -0.1004 -0.0195 1801 HFG A C10   
7519 C  C5    . HFG C .   ? 1.2580 1.2298 1.1043 -0.0280 -0.1014 -0.0283 1801 HFG A C5    
7520 C  C2    . HFG C .   ? 1.0635 1.0565 0.9719 -0.0122 -0.0997 -0.0038 1801 HFG A C2    
7521 N  N1    . HFG C .   ? 1.0805 1.0819 0.9851 -0.0144 -0.1128 -0.0062 1801 HFG A N1    
7522 C  C9    . HFG C .   ? 1.1914 1.1866 1.0760 -0.0202 -0.1140 -0.0144 1801 HFG A C9    
7523 C  C8    . HFG C .   ? 1.3120 1.3164 1.1934 -0.0237 -0.1288 -0.0178 1801 HFG A C8    
7524 C  C7    . HFG C .   ? 1.5251 1.5219 1.3854 -0.0302 -0.1308 -0.0268 1801 HFG A C7    
7525 BR BR1   . HFG C .   ? 1.7246 1.7353 1.5855 -0.0367 -0.1519 -0.0321 1801 HFG A BR1   
7526 C  C6    . HFG C .   ? 1.4398 1.4193 1.2810 -0.0321 -0.1170 -0.0322 1801 HFG A C6    
7527 CL CL1   . HFG C .   ? 1.5225 1.4891 1.3323 -0.0397 -0.1188 -0.0441 1801 HFG A CL1   
7528 ZN ZN    . ZN  D .   ? 1.6140 1.3079 1.3182 0.0742  0.0282  0.2551  1802 ZN  A ZN    
7529 CL CL    . CL  E .   ? 1.3503 1.3104 1.2312 -0.0002 -0.0748 0.0250  1803 CL  A CL    
7530 CL CL    . CL  F .   ? 1.3499 1.4209 1.4140 0.0082  -0.1271 0.0053  1804 CL  A CL    
7531 C  C1    . GOL G .   ? 0.5805 0.6376 0.7546 -0.0005 -0.0834 -0.0340 1805 GOL A C1    
7532 O  O1    . GOL G .   ? 0.5814 0.6334 0.7533 -0.0023 -0.0785 -0.0359 1805 GOL A O1    
7533 C  C2    . GOL G .   ? 0.5951 0.6543 0.7817 0.0020  -0.0837 -0.0330 1805 GOL A C2    
7534 O  O2    . GOL G .   ? 0.6477 0.7036 0.8404 0.0029  -0.0791 -0.0333 1805 GOL A O2    
7535 C  C3    . GOL G .   ? 0.5730 0.6361 0.7600 0.0046  -0.0910 -0.0306 1805 GOL A C3    
7536 O  O3    . GOL G .   ? 0.8220 0.8868 1.0202 0.0075  -0.0925 -0.0288 1805 GOL A O3    
7537 O  "O4'" . HFG H .   ? 0.8198 0.8448 1.0634 -0.1045 -0.0731 -0.0471 1801 HFG B "O4'" 
7538 C  C21   . HFG H .   ? 0.8504 0.8707 1.1059 -0.1090 -0.0670 -0.0430 1801 HFG B C21   
7539 C  "C3'" . HFG H .   ? 0.8671 0.8966 1.1331 -0.1037 -0.0601 -0.0310 1801 HFG B "C3'" 
7540 C  "C2'" . HFG H .   ? 0.7945 0.8298 1.0501 -0.0899 -0.0587 -0.0245 1801 HFG B "C2'" 
7541 N  "N1'" . HFG H .   ? 0.6289 0.6811 0.8808 -0.0866 -0.0671 -0.0269 1801 HFG B "N1'" 
7542 C  "C6'" . HFG H .   ? 0.5731 0.6306 0.8176 -0.0746 -0.0648 -0.0201 1801 HFG B "C6'" 
7543 C  "C5'" . HFG H .   ? 0.6340 0.6759 0.8643 -0.0670 -0.0618 -0.0202 1801 HFG B "C5'" 
7544 C  "C4'" . HFG H .   ? 0.7517 0.7760 0.9845 -0.0694 -0.0541 -0.0178 1801 HFG B "C4'" 
7545 C  C39   . HFG H .   ? 0.8000 0.8180 1.0405 -0.0818 -0.0553 -0.0250 1801 HFG B C39   
7546 O  "O7'" . HFG H .   ? 0.6108 0.6103 0.8543 -0.0846 -0.0476 -0.0231 1801 HFG B "O7'" 
7547 C  "C1'" . HFG H .   ? 0.9206 0.9252 1.1812 -0.1212 -0.0656 -0.0500 1801 HFG B "C1'" 
7548 N  N3    . HFG H .   ? 0.8457 0.8498 1.0992 -0.1293 -0.0753 -0.0620 1801 HFG B N3    
7549 C  C4    . HFG H .   ? 0.8854 0.9107 1.1473 -0.1351 -0.0856 -0.0636 1801 HFG B C4    
7550 O  O11   . HFG H .   ? 0.8801 0.9239 1.1580 -0.1341 -0.0854 -0.0555 1801 HFG B O11   
7551 C  C10   . HFG H .   ? 0.8559 0.8791 1.1058 -0.1419 -0.0961 -0.0754 1801 HFG B C10   
7552 C  C5    . HFG H .   ? 0.7675 0.8114 1.0237 -0.1471 -0.1082 -0.0772 1801 HFG B C5    
7553 C  C2    . HFG H .   ? 0.7870 0.7704 1.0248 -0.1301 -0.0742 -0.0710 1801 HFG B C2    
7554 N  N1    . HFG H .   ? 0.8953 0.8751 1.1215 -0.1360 -0.0818 -0.0820 1801 HFG B N1    
7555 C  C9    . HFG H .   ? 0.9912 0.9912 1.2222 -0.1420 -0.0936 -0.0842 1801 HFG B C9    
7556 C  C8    . HFG H .   ? 1.2769 1.2735 1.4921 -0.1476 -0.1029 -0.0954 1801 HFG B C8    
7557 C  C7    . HFG H .   ? 1.4802 1.4972 1.6994 -0.1529 -0.1158 -0.0969 1801 HFG B C7    
7558 BR BR1   . HFG H .   ? 2.6017 2.6129 2.7944 -0.1592 -0.1290 -0.1111 1801 HFG B BR1   
7559 C  C6    . HFG H .   ? 0.9873 1.0283 1.2283 -0.1526 -0.1188 -0.0878 1801 HFG B C6    
7560 CL CL1   . HFG H .   ? 1.0850 1.1529 1.3343 -0.1583 -0.1353 -0.0887 1801 HFG B CL1   
7561 ZN ZN    . ZN  I .   ? 1.0722 0.6364 1.5118 -0.2372 0.1468  0.0408  1802 ZN  B ZN    
7562 CL CL    . CL  J .   ? 1.2420 1.1377 1.3944 -0.0741 -0.0379 -0.0903 1803 CL  B CL    
7563 C  C1    . GOL K .   ? 0.7014 0.7602 0.8661 0.0001  -0.0885 -0.0250 1804 GOL B C1    
7564 O  O1    . GOL K .   ? 0.5950 0.6577 0.7558 -0.0027 -0.0894 -0.0265 1804 GOL B O1    
7565 C  C2    . GOL K .   ? 0.7775 0.8388 0.9397 0.0044  -0.0916 -0.0215 1804 GOL B C2    
7566 O  O2    . GOL K .   ? 0.7906 0.8552 0.9500 0.0057  -0.0944 -0.0228 1804 GOL B O2    
7567 C  C3    . GOL K .   ? 0.8868 0.9449 1.0533 0.0078  -0.0926 -0.0194 1804 GOL B C3    
7568 O  O3    . GOL K .   ? 0.9991 1.0598 1.1676 0.0096  -0.0962 -0.0209 1804 GOL B O3    
7569 C  C1    . GOL L .   ? 1.4850 1.3848 1.6758 0.1071  -0.0715 0.1380  1805 GOL B C1    
7570 O  O1    . GOL L .   ? 1.4507 1.3348 1.6393 0.1155  -0.0690 0.1529  1805 GOL B O1    
7571 C  C2    . GOL L .   ? 1.5077 1.4236 1.7164 0.1132  -0.0817 0.1341  1805 GOL B C2    
7572 O  O2    . GOL L .   ? 1.5072 1.4418 1.7088 0.1099  -0.0921 0.1271  1805 GOL B O2    
7573 C  C3    . GOL L .   ? 1.4454 1.3563 1.6762 0.1098  -0.0712 0.1236  1805 GOL B C3    
7574 O  O3    . GOL L .   ? 1.3715 1.3012 1.6148 0.1096  -0.0784 0.1145  1805 GOL B O3    
7575 O  O     . HOH M .   ? 0.8266 0.7128 0.7337 -0.0161 0.1155  -0.0222 1901 HOH A O     
7576 O  O     . HOH M .   ? 0.7103 0.7782 0.9844 -0.0266 -0.1244 -0.0503 1902 HOH A O     
7577 O  O     . HOH M .   ? 1.0048 0.9501 1.0276 -0.0151 0.0597  -0.0419 1903 HOH A O     
7578 O  O     . HOH M .   ? 0.8301 0.8107 0.9429 0.0187  -0.1044 -0.0572 1904 HOH A O     
7579 O  O     . HOH M .   ? 0.5721 0.7003 0.7556 0.0370  -0.0603 0.0003  1905 HOH A O     
7580 O  O     . HOH M .   ? 0.4139 0.5552 0.6186 0.0182  -0.0623 0.0047  1906 HOH A O     
7581 O  O     . HOH M .   ? 0.6590 0.6636 0.6368 -0.0063 -0.0861 -0.0019 1907 HOH A O     
7582 O  O     . HOH M .   ? 1.5867 1.4625 1.6488 -0.0373 0.1424  0.0702  1908 HOH A O     
7583 O  O     . HOH M .   ? 1.2230 1.1774 1.0785 0.0119  -0.0897 0.0501  1909 HOH A O     
7584 O  O     . HOH N .   ? 0.8310 0.8764 0.9272 0.0346  -0.1144 0.0046  1901 HOH B O     
7585 O  O     . HOH N .   ? 0.6784 0.6449 0.8628 0.0107  0.0510  -0.0704 1902 HOH B O     
7586 O  O     . HOH N .   ? 0.7910 0.5853 1.1739 -0.1721 0.0841  0.0531  1903 HOH B O     
7587 O  O     . HOH N .   ? 0.7843 0.8849 0.9373 0.0230  -0.0309 0.0193  1904 HOH B O     
7588 O  O     . HOH N .   ? 0.8153 0.7885 1.0438 -0.0973 -0.0545 -0.0480 1905 HOH B O     
7589 O  O     . HOH N .   ? 1.3973 0.8208 1.8590 -0.3581 0.1116  -0.1094 1906 HOH B O     
7590 O  O     . HOH N .   ? 0.5839 0.4985 0.7937 -0.0578 -0.0284 -0.0334 1907 HOH B O     
# 
