data_3WLT # _entry.id 3WLT # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.281 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3WLT RCSB RCSB096496 WWPDB D_1000096496 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1EX1 . unspecified PDB 1IEQ . unspecified PDB 1IEV . unspecified PDB 1IEW . unspecified PDB 1IEX . unspecified PDB 1J8V . unspecified PDB 3WLH . unspecified PDB 3WLI . unspecified PDB 3WLJ . unspecified PDB 3WLK . unspecified PDB 3WLL . unspecified PDB 3WLM . unspecified PDB 3WLN . unspecified PDB 3WLO . unspecified PDB 3WLP . unspecified PDB 3WLQ . unspecified PDB 3WLR . unspecified PDB 3WLS . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3WLT _pdbx_database_status.recvd_initial_deposition_date 2013-11-12 _pdbx_database_status.deposit_site PDBJ _pdbx_database_status.process_site PDBJ _pdbx_database_status.methods_development_category ? _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Streltsov, V.A.' 1 'Luang, S.' 2 'Hrmova, M.' 3 # _citation.id primary _citation.title 'A landscape of the product and substrate trajectories in a glycoside hydrolase' _citation.journal_abbrev 'To be Published' _citation.journal_volume ? _citation.page_first ? _citation.page_last ? _citation.year ? _citation.journal_id_ASTM ? _citation.country ? _citation.journal_id_ISSN ? _citation.journal_id_CSD 0353 _citation.book_publisher ? _citation.pdbx_database_id_PubMed ? _citation.pdbx_database_id_DOI ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Streltsov, V.A.' 1 primary 'Luang, S.' 2 primary 'Ketudat-Cairns, J.R.' 3 primary 'Raab, M.' 4 primary 'Tvaroska, I.' 5 primary 'Fort, S.' 6 primary 'Jimenez-Barbero, J.' 7 primary 'Peisley, A.' 8 primary 'Varghese, J.N.' 9 primary 'Hrmova, M.' 10 # _cell.entry_id 3WLT _cell.length_a 100.524 _cell.length_b 100.524 _cell.length_c 182.076 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 3WLT _symmetry.space_group_name_H-M 'P 43 21 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 96 _symmetry.space_group_name_Hall ? # 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 'Beta-D-glucan exohydrolase isoenzyme ExoI' 65778.938 1 3.2.1.- W434A 'UNP RESIDUES 26-630' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 3 ? ? ? ? 3 non-polymer syn GLYCEROL 92.094 14 ? ? ? ? 4 non-polymer syn 'SULFATE ION' 96.063 1 ? ? ? ? 5 non-polymer man 1-THIO-BETA-D-GLUCOPYRANOSE 196.221 1 ? ? ? ? 6 non-polymer man O1-METHYL-GLUCOSE 194.182 1 ? ? ? ? 7 water nat water 18.015 776 ? ? ? ? # _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 ;HHAADYVLYKDATKPVEDRVADLLGRMTLAEKIGQMTQIERLVATPDVLRDNFIGSLLSGGGSVPRKGATAKEWQDMVDG FQKACMSTRLGIPMIYGIDAVHGQNNVYGATIFPHNVGLGATRDPYLVKRIGEATALEVRATGIQYAFAPCIAVCRDPRW GRCYESYSEDRRIVQSMTELIPGLQGDVPKDFTSGMPFVAGKNKVAACAKHFVGDGGTVDGINENNTIINREGLMNIHMP AYKNAMDKGVSTVMISYSSWNGVKMHANQDLVTGYLKDTLKFKGFVISDWEGIDRITTPAGSDYSYSVKASILAGLDMIM VPNKYQQFISILTGHVNGGVIPMSRIDDAVTRILRVKFTMGLFENPYADPAMAEQLGKQEHRDLAREAARKSLVLLKNGK TSTDAPLLPLPKKAPKILVAGSHADNLGYQCGGWTIEAQGDTGRTTVGTTILEAVKAAVDPSTVVVFAENPDAEFVKSGG FSYAIVAVGEHPYTETKGDNLNLTIPEPGLSTVQAVCGGVRCATVLISGRPVVVQPLLAASDALVAAWLPGSEGQGVTDA LFGDFGFTGRLPRTWFKSVDQLPMNVGDAHYDPLFRLGYGLTTNATKKY ; _entity_poly.pdbx_seq_one_letter_code_can ;HHAADYVLYKDATKPVEDRVADLLGRMTLAEKIGQMTQIERLVATPDVLRDNFIGSLLSGGGSVPRKGATAKEWQDMVDG FQKACMSTRLGIPMIYGIDAVHGQNNVYGATIFPHNVGLGATRDPYLVKRIGEATALEVRATGIQYAFAPCIAVCRDPRW GRCYESYSEDRRIVQSMTELIPGLQGDVPKDFTSGMPFVAGKNKVAACAKHFVGDGGTVDGINENNTIINREGLMNIHMP AYKNAMDKGVSTVMISYSSWNGVKMHANQDLVTGYLKDTLKFKGFVISDWEGIDRITTPAGSDYSYSVKASILAGLDMIM VPNKYQQFISILTGHVNGGVIPMSRIDDAVTRILRVKFTMGLFENPYADPAMAEQLGKQEHRDLAREAARKSLVLLKNGK TSTDAPLLPLPKKAPKILVAGSHADNLGYQCGGWTIEAQGDTGRTTVGTTILEAVKAAVDPSTVVVFAENPDAEFVKSGG FSYAIVAVGEHPYTETKGDNLNLTIPEPGLSTVQAVCGGVRCATVLISGRPVVVQPLLAASDALVAAWLPGSEGQGVTDA LFGDFGFTGRLPRTWFKSVDQLPMNVGDAHYDPLFRLGYGLTTNATKKY ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 HIS n 1 2 HIS n 1 3 ALA n 1 4 ALA n 1 5 ASP n 1 6 TYR n 1 7 VAL n 1 8 LEU n 1 9 TYR n 1 10 LYS n 1 11 ASP n 1 12 ALA n 1 13 THR n 1 14 LYS n 1 15 PRO n 1 16 VAL n 1 17 GLU n 1 18 ASP n 1 19 ARG n 1 20 VAL n 1 21 ALA n 1 22 ASP n 1 23 LEU n 1 24 LEU n 1 25 GLY n 1 26 ARG n 1 27 MET n 1 28 THR n 1 29 LEU n 1 30 ALA n 1 31 GLU n 1 32 LYS n 1 33 ILE n 1 34 GLY n 1 35 GLN n 1 36 MET n 1 37 THR n 1 38 GLN n 1 39 ILE n 1 40 GLU n 1 41 ARG n 1 42 LEU n 1 43 VAL n 1 44 ALA n 1 45 THR n 1 46 PRO n 1 47 ASP n 1 48 VAL n 1 49 LEU n 1 50 ARG n 1 51 ASP n 1 52 ASN n 1 53 PHE n 1 54 ILE n 1 55 GLY n 1 56 SER n 1 57 LEU n 1 58 LEU n 1 59 SER n 1 60 GLY n 1 61 GLY n 1 62 GLY n 1 63 SER n 1 64 VAL n 1 65 PRO n 1 66 ARG n 1 67 LYS n 1 68 GLY n 1 69 ALA n 1 70 THR n 1 71 ALA n 1 72 LYS n 1 73 GLU n 1 74 TRP n 1 75 GLN n 1 76 ASP n 1 77 MET n 1 78 VAL n 1 79 ASP n 1 80 GLY n 1 81 PHE n 1 82 GLN n 1 83 LYS n 1 84 ALA n 1 85 CYS n 1 86 MET n 1 87 SER n 1 88 THR n 1 89 ARG n 1 90 LEU n 1 91 GLY n 1 92 ILE n 1 93 PRO n 1 94 MET n 1 95 ILE n 1 96 TYR n 1 97 GLY n 1 98 ILE n 1 99 ASP n 1 100 ALA n 1 101 VAL n 1 102 HIS n 1 103 GLY n 1 104 GLN n 1 105 ASN n 1 106 ASN n 1 107 VAL n 1 108 TYR n 1 109 GLY n 1 110 ALA n 1 111 THR n 1 112 ILE n 1 113 PHE n 1 114 PRO n 1 115 HIS n 1 116 ASN n 1 117 VAL n 1 118 GLY n 1 119 LEU n 1 120 GLY n 1 121 ALA n 1 122 THR n 1 123 ARG n 1 124 ASP n 1 125 PRO n 1 126 TYR n 1 127 LEU n 1 128 VAL n 1 129 LYS n 1 130 ARG n 1 131 ILE n 1 132 GLY n 1 133 GLU n 1 134 ALA n 1 135 THR n 1 136 ALA n 1 137 LEU n 1 138 GLU n 1 139 VAL n 1 140 ARG n 1 141 ALA n 1 142 THR n 1 143 GLY n 1 144 ILE n 1 145 GLN n 1 146 TYR n 1 147 ALA n 1 148 PHE n 1 149 ALA n 1 150 PRO n 1 151 CYS n 1 152 ILE n 1 153 ALA n 1 154 VAL n 1 155 CYS n 1 156 ARG n 1 157 ASP n 1 158 PRO n 1 159 ARG n 1 160 TRP n 1 161 GLY n 1 162 ARG n 1 163 CYS n 1 164 TYR n 1 165 GLU n 1 166 SER n 1 167 TYR n 1 168 SER n 1 169 GLU n 1 170 ASP n 1 171 ARG n 1 172 ARG n 1 173 ILE n 1 174 VAL n 1 175 GLN n 1 176 SER n 1 177 MET n 1 178 THR n 1 179 GLU n 1 180 LEU n 1 181 ILE n 1 182 PRO n 1 183 GLY n 1 184 LEU n 1 185 GLN n 1 186 GLY n 1 187 ASP n 1 188 VAL n 1 189 PRO n 1 190 LYS n 1 191 ASP n 1 192 PHE n 1 193 THR n 1 194 SER n 1 195 GLY n 1 196 MET n 1 197 PRO n 1 198 PHE n 1 199 VAL n 1 200 ALA n 1 201 GLY n 1 202 LYS n 1 203 ASN n 1 204 LYS n 1 205 VAL n 1 206 ALA n 1 207 ALA n 1 208 CYS n 1 209 ALA n 1 210 LYS n 1 211 HIS n 1 212 PHE n 1 213 VAL n 1 214 GLY n 1 215 ASP n 1 216 GLY n 1 217 GLY n 1 218 THR n 1 219 VAL n 1 220 ASP n 1 221 GLY n 1 222 ILE n 1 223 ASN n 1 224 GLU n 1 225 ASN n 1 226 ASN n 1 227 THR n 1 228 ILE n 1 229 ILE n 1 230 ASN n 1 231 ARG n 1 232 GLU n 1 233 GLY n 1 234 LEU n 1 235 MET n 1 236 ASN n 1 237 ILE n 1 238 HIS n 1 239 MET n 1 240 PRO n 1 241 ALA n 1 242 TYR n 1 243 LYS n 1 244 ASN n 1 245 ALA n 1 246 MET n 1 247 ASP n 1 248 LYS n 1 249 GLY n 1 250 VAL n 1 251 SER n 1 252 THR n 1 253 VAL n 1 254 MET n 1 255 ILE n 1 256 SER n 1 257 TYR n 1 258 SER n 1 259 SER n 1 260 TRP n 1 261 ASN n 1 262 GLY n 1 263 VAL n 1 264 LYS n 1 265 MET n 1 266 HIS n 1 267 ALA n 1 268 ASN n 1 269 GLN n 1 270 ASP n 1 271 LEU n 1 272 VAL n 1 273 THR n 1 274 GLY n 1 275 TYR n 1 276 LEU n 1 277 LYS n 1 278 ASP n 1 279 THR n 1 280 LEU n 1 281 LYS n 1 282 PHE n 1 283 LYS n 1 284 GLY n 1 285 PHE n 1 286 VAL n 1 287 ILE n 1 288 SER n 1 289 ASP n 1 290 TRP n 1 291 GLU n 1 292 GLY n 1 293 ILE n 1 294 ASP n 1 295 ARG n 1 296 ILE n 1 297 THR n 1 298 THR n 1 299 PRO n 1 300 ALA n 1 301 GLY n 1 302 SER n 1 303 ASP n 1 304 TYR n 1 305 SER n 1 306 TYR n 1 307 SER n 1 308 VAL n 1 309 LYS n 1 310 ALA n 1 311 SER n 1 312 ILE n 1 313 LEU n 1 314 ALA n 1 315 GLY n 1 316 LEU n 1 317 ASP n 1 318 MET n 1 319 ILE n 1 320 MET n 1 321 VAL n 1 322 PRO n 1 323 ASN n 1 324 LYS n 1 325 TYR n 1 326 GLN n 1 327 GLN n 1 328 PHE n 1 329 ILE n 1 330 SER n 1 331 ILE n 1 332 LEU n 1 333 THR n 1 334 GLY n 1 335 HIS n 1 336 VAL n 1 337 ASN n 1 338 GLY n 1 339 GLY n 1 340 VAL n 1 341 ILE n 1 342 PRO n 1 343 MET n 1 344 SER n 1 345 ARG n 1 346 ILE n 1 347 ASP n 1 348 ASP n 1 349 ALA n 1 350 VAL n 1 351 THR n 1 352 ARG n 1 353 ILE n 1 354 LEU n 1 355 ARG n 1 356 VAL n 1 357 LYS n 1 358 PHE n 1 359 THR n 1 360 MET n 1 361 GLY n 1 362 LEU n 1 363 PHE n 1 364 GLU n 1 365 ASN n 1 366 PRO n 1 367 TYR n 1 368 ALA n 1 369 ASP n 1 370 PRO n 1 371 ALA n 1 372 MET n 1 373 ALA n 1 374 GLU n 1 375 GLN n 1 376 LEU n 1 377 GLY n 1 378 LYS n 1 379 GLN n 1 380 GLU n 1 381 HIS n 1 382 ARG n 1 383 ASP n 1 384 LEU n 1 385 ALA n 1 386 ARG n 1 387 GLU n 1 388 ALA n 1 389 ALA n 1 390 ARG n 1 391 LYS n 1 392 SER n 1 393 LEU n 1 394 VAL n 1 395 LEU n 1 396 LEU n 1 397 LYS n 1 398 ASN n 1 399 GLY n 1 400 LYS n 1 401 THR n 1 402 SER n 1 403 THR n 1 404 ASP n 1 405 ALA n 1 406 PRO n 1 407 LEU n 1 408 LEU n 1 409 PRO n 1 410 LEU n 1 411 PRO n 1 412 LYS n 1 413 LYS n 1 414 ALA n 1 415 PRO n 1 416 LYS n 1 417 ILE n 1 418 LEU n 1 419 VAL n 1 420 ALA n 1 421 GLY n 1 422 SER n 1 423 HIS n 1 424 ALA n 1 425 ASP n 1 426 ASN n 1 427 LEU n 1 428 GLY n 1 429 TYR n 1 430 GLN n 1 431 CYS n 1 432 GLY n 1 433 GLY n 1 434 TRP n 1 435 THR n 1 436 ILE n 1 437 GLU n 1 438 ALA n 1 439 GLN n 1 440 GLY n 1 441 ASP n 1 442 THR n 1 443 GLY n 1 444 ARG n 1 445 THR n 1 446 THR n 1 447 VAL n 1 448 GLY n 1 449 THR n 1 450 THR n 1 451 ILE n 1 452 LEU n 1 453 GLU n 1 454 ALA n 1 455 VAL n 1 456 LYS n 1 457 ALA n 1 458 ALA n 1 459 VAL n 1 460 ASP n 1 461 PRO n 1 462 SER n 1 463 THR n 1 464 VAL n 1 465 VAL n 1 466 VAL n 1 467 PHE n 1 468 ALA n 1 469 GLU n 1 470 ASN n 1 471 PRO n 1 472 ASP n 1 473 ALA n 1 474 GLU n 1 475 PHE n 1 476 VAL n 1 477 LYS n 1 478 SER n 1 479 GLY n 1 480 GLY n 1 481 PHE n 1 482 SER n 1 483 TYR n 1 484 ALA n 1 485 ILE n 1 486 VAL n 1 487 ALA n 1 488 VAL n 1 489 GLY n 1 490 GLU n 1 491 HIS n 1 492 PRO n 1 493 TYR n 1 494 THR n 1 495 GLU n 1 496 THR n 1 497 LYS n 1 498 GLY n 1 499 ASP n 1 500 ASN n 1 501 LEU n 1 502 ASN n 1 503 LEU n 1 504 THR n 1 505 ILE n 1 506 PRO n 1 507 GLU n 1 508 PRO n 1 509 GLY n 1 510 LEU n 1 511 SER n 1 512 THR n 1 513 VAL n 1 514 GLN n 1 515 ALA n 1 516 VAL n 1 517 CYS n 1 518 GLY n 1 519 GLY n 1 520 VAL n 1 521 ARG n 1 522 CYS n 1 523 ALA n 1 524 THR n 1 525 VAL n 1 526 LEU n 1 527 ILE n 1 528 SER n 1 529 GLY n 1 530 ARG n 1 531 PRO n 1 532 VAL n 1 533 VAL n 1 534 VAL n 1 535 GLN n 1 536 PRO n 1 537 LEU n 1 538 LEU n 1 539 ALA n 1 540 ALA n 1 541 SER n 1 542 ASP n 1 543 ALA n 1 544 LEU n 1 545 VAL n 1 546 ALA n 1 547 ALA n 1 548 TRP n 1 549 LEU n 1 550 PRO n 1 551 GLY n 1 552 SER n 1 553 GLU n 1 554 GLY n 1 555 GLN n 1 556 GLY n 1 557 VAL n 1 558 THR n 1 559 ASP n 1 560 ALA n 1 561 LEU n 1 562 PHE n 1 563 GLY n 1 564 ASP n 1 565 PHE n 1 566 GLY n 1 567 PHE n 1 568 THR n 1 569 GLY n 1 570 ARG n 1 571 LEU n 1 572 PRO n 1 573 ARG n 1 574 THR n 1 575 TRP n 1 576 PHE n 1 577 LYS n 1 578 SER n 1 579 VAL n 1 580 ASP n 1 581 GLN n 1 582 LEU n 1 583 PRO n 1 584 MET n 1 585 ASN n 1 586 VAL n 1 587 GLY n 1 588 ASP n 1 589 ALA n 1 590 HIS n 1 591 TYR n 1 592 ASP n 1 593 PRO n 1 594 LEU n 1 595 PHE n 1 596 ARG n 1 597 LEU n 1 598 GLY n 1 599 TYR n 1 600 GLY n 1 601 LEU n 1 602 THR n 1 603 THR n 1 604 ASN n 1 605 ALA n 1 606 THR n 1 607 LYS n 1 608 LYS n 1 609 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 ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name 'barley,two-rowed barley' _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 'Hordeum vulgare subsp. vulgare' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 112509 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Komagataella pastoris' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 4922 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain SMD11680H _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 plasmid _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name pPICZalphaBNH8/DEST _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code Q9XEI3_HORVD _struct_ref.pdbx_db_accession Q9XEI3 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;DYVLYKDATKPVEDRVADLLGRMTLAEKIGQMTQIERLVATPDVLRDNFIGSLLSGGGSVPRKGATAKEWQDMVDGFQKA CMSTRLGIPMIYGIDAVHGQNNVYGATIFPHNVGLGATRDPYLVKRIGEATALEVRATGIQYAFAPCIAVCRDPRWGRCY ESYSEDRRIVQSMTELIPGLQGDVPKDFTSGMPFVAGKNKVAACAKHFVGDGGTVDGINENNTIINREGLMNIHMPAYKN AMDKGVSTVMISYSSWNGVKMHANQDLVTGYLKDTLKFKGFVISDWEGIDRITTPAGSDYSYSVKASILAGLDMIMVPNN YQQFISILTGHVNGGVIPMSRIDDAVTRILRVKFTMGLFENPYADPAMAEQLGKQEHRDLAREAARKSLVLLKNGKTSTD APLLPLPKKAPKILVAGSHADNLGYQCGGWTIEWQGDTGRTTVGTTILEAVKAAVDPSTVVVFAENPDAEFVKSGGFSYA IVAVGEHPYTETKGDNLNLTIPEPGLSTVQAVCGGVRCATVLISGRPVVVQPLLAASDALVAAWLPGSEGQGVTDALFGD FGFTGRLPRTWFKSVDQLPMNVGDAHYDPLFRLGYGLTTNATKKY ; _struct_ref.pdbx_align_begin 26 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 3WLT _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 5 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 609 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q9XEI3 _struct_ref_seq.db_align_beg 26 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 630 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 605 # 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 3WLT HIS A 1 ? UNP Q9XEI3 ? ? 'EXPRESSION TAG' -3 1 1 3WLT HIS A 2 ? UNP Q9XEI3 ? ? 'EXPRESSION TAG' -2 2 1 3WLT ALA A 3 ? UNP Q9XEI3 ? ? 'EXPRESSION TAG' -1 3 1 3WLT ALA A 4 ? UNP Q9XEI3 ? ? 'EXPRESSION TAG' 0 4 1 3WLT LYS A 324 ? UNP Q9XEI3 ASN 345 'SEE REMARK 999' 320 5 1 3WLT ALA A 438 ? UNP Q9XEI3 TRP 459 'ENGINEERED MUTATION' 434 6 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 GS1 D-saccharide . 1-THIO-BETA-D-GLUCOPYRANOSE ? 'C6 H12 O5 S' 196.221 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 MGL saccharide . O1-METHYL-GLUCOSE ? 'C7 H14 O6' 194.182 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 SO4 non-polymer . 'SULFATE ION' ? 'O4 S -2' 96.063 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 # _exptl.entry_id 3WLT _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.52 _exptl_crystal.density_percent_sol 65.05 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 277 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.0 _exptl_crystal_grow.pdbx_details ;75mM HEPES-NaOH pH7.0, 1.2% PEG 400, 1.7M ammonium sulphate , VAPOR DIFFUSION, HANGING DROP, temperature 277K ; _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC QUANTUM 210r' _diffrn_detector.pdbx_collection_date ? _diffrn_detector.details 'collimating mirror' # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'double-crystal Si(111) monochromator' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.9615 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'AUSTRALIAN SYNCHROTRON BEAMLINE MX1' _diffrn_source.pdbx_synchrotron_site 'Australian Synchrotron' _diffrn_source.pdbx_synchrotron_beamline MX1 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.9615 # _reflns.entry_id 3WLT _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 88.00 _reflns.d_resolution_high 1.98 _reflns.number_obs 62175 _reflns.number_all 62175 _reflns.percent_possible_obs 97.0 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _reflns.R_free_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.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.98 _reflns_shell.d_res_low 2.03 _reflns_shell.percent_possible_all 98.2 _reflns_shell.Rmerge_I_obs 0.596 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.number_possible ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.meanI_over_sigI_all ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 3WLT _refine.ls_number_reflns_obs 62175 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 29.33 _refine.ls_d_res_high 1.98 _refine.ls_percent_reflns_obs 99.83 _refine.ls_R_factor_obs 0.16444 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.16213 _refine.ls_R_factor_R_free 0.20896 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 3324 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.955 _refine.correlation_coeff_Fo_to_Fc_free 0.923 _refine.B_iso_mean 29.378 _refine.aniso_B[1][1] 1.16 _refine.aniso_B[2][2] 1.16 _refine.aniso_B[3][3] -2.31 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'BABINET MODEL PARAMETERS FOR MASK CACLULATION' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model 1IEQ _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.122 _refine.pdbx_overall_ESU_R_Free 0.126 _refine.overall_SU_ML 0.067 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 5.024 _refine.overall_SU_R_Cruickshank_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_diffrn_id 1 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 4587 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 155 _refine_hist.number_atoms_solvent 776 _refine_hist.number_atoms_total 5518 _refine_hist.d_res_high 1.98 _refine_hist.d_res_low 29.33 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_restraint_function _refine_ls_restr.pdbx_refine_id r_bond_refined_d 0.025 0.022 ? 4868 ? 'X-RAY DIFFRACTION' r_bond_other_d ? ? ? ? ? 'X-RAY DIFFRACTION' r_angle_refined_deg 1.818 1.989 ? 6587 ? 'X-RAY DIFFRACTION' r_angle_other_deg ? ? ? ? ? 'X-RAY DIFFRACTION' r_dihedral_angle_1_deg 6.614 5.000 ? 605 ? 'X-RAY DIFFRACTION' r_dihedral_angle_2_deg 37.695 23.687 ? 198 ? 'X-RAY DIFFRACTION' r_dihedral_angle_3_deg 13.228 15.000 ? 782 ? 'X-RAY DIFFRACTION' r_dihedral_angle_4_deg 15.263 15.000 ? 33 ? 'X-RAY DIFFRACTION' r_chiral_restr 0.155 0.200 ? 742 ? 'X-RAY DIFFRACTION' r_gen_planes_refined 0.010 0.021 ? 3609 ? 'X-RAY DIFFRACTION' r_gen_planes_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbd_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbd_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbtor_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbtor_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_xyhbond_nbd_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_xyhbond_nbd_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_metal_ion_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_metal_ion_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_vdw_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_vdw_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_hbond_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_hbond_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_metal_ion_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_metal_ion_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_mcbond_it 1.001 1.500 ? 2999 ? 'X-RAY DIFFRACTION' r_mcbond_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_mcangle_it 1.599 2.000 ? 4831 ? 'X-RAY DIFFRACTION' r_mcangle_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_scbond_it 2.932 3.000 ? 1869 ? 'X-RAY DIFFRACTION' r_scbond_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_scangle_it 4.451 4.500 ? 1756 ? 'X-RAY DIFFRACTION' r_scangle_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_long_range_B_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_long_range_B_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_rigid_bond_restr ? ? ? ? ? 'X-RAY DIFFRACTION' r_sphericity_free ? ? ? ? ? 'X-RAY DIFFRACTION' r_sphericity_bonded ? ? ? ? ? 'X-RAY DIFFRACTION' # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.980 _refine_ls_shell.d_res_low 2.032 _refine_ls_shell.number_reflns_R_work 4490 _refine_ls_shell.R_factor_R_work 0.166 _refine_ls_shell.percent_reflns_obs 99.92 _refine_ls_shell.R_factor_R_free 0.220 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 248 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? # _struct.entry_id 3WLT _struct.title 'Crystal Structure Analysis of Plant Exohydrolase' _struct.pdbx_descriptor 'Beta-D-glucan exohydrolase isoenzyme ExoI (E.C.3.2.1.-)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3WLT _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text ;BETA BARREL, HYDROLASE, GRAIN DEVELOPMENT, mutant, Enzyme Function Initiative, Tim Barrel/Beta sheet, N-glycosylation, plant apoplast ; # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 2 ? E N N 3 ? F N N 3 ? G N N 3 ? H N N 3 ? I N N 3 ? J N N 3 ? K N N 4 ? L N N 3 ? M N N 3 ? N N N 3 ? O N N 3 ? P N N 3 ? Q N N 3 ? R N N 3 ? S N N 3 ? T N N 5 ? U N N 6 ? V N N 7 ? # _struct_biol.id 1 _struct_biol.details ? # 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 1 VAL A 7 ? ASP A 11 ? VAL A 3 ASP A 7 5 ? 5 HELX_P HELX_P2 2 PRO A 15 ? GLY A 25 ? PRO A 11 GLY A 21 1 ? 11 HELX_P HELX_P3 3 THR A 28 ? MET A 36 ? THR A 24 MET A 32 1 ? 9 HELX_P HELX_P4 4 LEU A 42 ? ALA A 44 ? LEU A 38 ALA A 40 5 ? 3 HELX_P HELX_P5 5 THR A 45 ? ASN A 52 ? THR A 41 ASN A 48 1 ? 8 HELX_P HELX_P6 6 THR A 70 ? SER A 87 ? THR A 66 SER A 83 1 ? 18 HELX_P HELX_P7 7 HIS A 115 ? THR A 122 ? HIS A 111 THR A 118 1 ? 8 HELX_P HELX_P8 8 ASP A 124 ? THR A 142 ? ASP A 120 THR A 138 1 ? 19 HELX_P HELX_P9 9 ARG A 162 ? SER A 166 ? ARG A 158 SER A 162 5 ? 5 HELX_P HELX_P10 10 ASP A 170 ? MET A 177 ? ASP A 166 MET A 173 1 ? 8 HELX_P HELX_P11 11 GLU A 179 ? GLY A 186 ? GLU A 175 GLY A 182 1 ? 8 HELX_P HELX_P12 12 GLY A 214 ? ILE A 222 ? GLY A 210 ILE A 218 5 ? 9 HELX_P HELX_P13 13 ASN A 230 ? HIS A 238 ? ASN A 226 HIS A 234 1 ? 9 HELX_P HELX_P14 14 MET A 239 ? LYS A 248 ? MET A 235 LYS A 244 1 ? 10 HELX_P HELX_P15 15 ASN A 268 ? THR A 273 ? ASN A 264 THR A 269 1 ? 6 HELX_P HELX_P16 16 ILE A 293 ? THR A 297 ? ILE A 289 THR A 293 5 ? 5 HELX_P HELX_P17 17 ASP A 303 ? GLY A 315 ? ASP A 299 GLY A 311 1 ? 13 HELX_P HELX_P18 18 LYS A 324 ? GLY A 338 ? LYS A 320 GLY A 334 1 ? 15 HELX_P HELX_P19 19 PRO A 342 ? MET A 360 ? PRO A 338 MET A 356 1 ? 19 HELX_P HELX_P20 20 ASP A 369 ? LEU A 376 ? ASP A 365 LEU A 372 5 ? 8 HELX_P HELX_P21 21 LYS A 378 ? LEU A 393 ? LYS A 374 LEU A 389 1 ? 16 HELX_P HELX_P22 22 ASN A 426 ? GLY A 432 ? ASN A 422 GLY A 428 1 ? 7 HELX_P HELX_P23 23 THR A 450 ? VAL A 459 ? THR A 446 VAL A 455 1 ? 10 HELX_P HELX_P24 24 ASP A 472 ? GLY A 479 ? ASP A 468 GLY A 475 1 ? 8 HELX_P HELX_P25 25 THR A 494 ? ASP A 499 ? THR A 490 ASP A 495 5 ? 6 HELX_P HELX_P26 26 GLY A 509 ? GLY A 518 ? GLY A 505 GLY A 514 1 ? 10 HELX_P HELX_P27 27 VAL A 534 ? SER A 541 ? VAL A 530 SER A 537 1 ? 8 HELX_P HELX_P28 28 GLY A 554 ? PHE A 562 ? GLY A 550 PHE A 558 1 ? 9 HELX_P HELX_P29 29 SER A 578 ? LEU A 582 ? SER A 574 LEU A 578 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 155 SG ? ? ? 1_555 A CYS 163 SG ? ? A CYS 151 A CYS 159 1_555 ? ? ? ? ? ? ? 2.170 ? disulf2 disulf ? ? A CYS 517 SG ? ? ? 1_555 A CYS 522 SG ? ? A CYS 513 A CYS 518 1_555 ? ? ? ? ? ? ? 1.998 ? covale1 covale ? ? A ASN 502 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 498 A NAG 702 1_555 ? ? ? ? ? ? ? 1.444 ? covale2 covale ? ? A ASN 225 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 221 A NAG 701 1_555 ? ? ? ? ? ? ? 1.444 ? covale3 covale ? ? A ASN 604 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 600 A NAG 703 1_555 ? ? ? ? ? ? ? 1.449 ? covale4 covale ? ? T GS1 . S1 ? ? ? 1_555 U MGL . C6 ? ? A GS1 719 A MGL 720 1_555 ? ? ? ? ? ? ? 1.778 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # 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 ALA 149 A . ? ALA 145 A PRO 150 A ? PRO 146 A 1 7.99 2 LYS 210 A . ? LYS 206 A HIS 211 A ? HIS 207 A 1 -5.55 3 PHE 212 A . ? PHE 208 A VAL 213 A ? VAL 209 A 1 -1.44 4 THR 298 A . ? THR 294 A PRO 299 A ? PRO 295 A 1 -7.72 5 VAL 321 A . ? VAL 317 A PRO 322 A ? PRO 318 A 1 -7.02 6 LEU 408 A . ? LEU 404 A PRO 409 A ? PRO 405 A 1 2.73 7 GLU 507 A . ? GLU 503 A PRO 508 A ? PRO 504 A 1 1.53 8 LEU 582 A . ? LEU 578 A PRO 583 A ? PRO 579 A 1 -0.22 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 5 ? B ? 3 ? C ? 3 ? D ? 6 ? # 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 A 1 2 ? parallel A 2 3 ? parallel A 3 4 ? parallel A 4 5 ? parallel B 1 2 ? parallel B 2 3 ? parallel C 1 2 ? parallel C 2 3 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? parallel D 3 4 ? parallel D 4 5 ? parallel D 5 6 ? 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 A 1 TYR A 146 ? ALA A 147 ? TYR A 142 ALA A 143 A 2 ILE A 95 ? ILE A 98 ? ILE A 91 ILE A 94 A 3 SER A 56 ? SER A 59 ? SER A 52 SER A 55 A 4 THR A 37 ? GLU A 40 ? THR A 33 GLU A 36 A 5 ILE A 319 ? MET A 320 ? ILE A 315 MET A 316 B 1 CYS A 208 ? PHE A 212 ? CYS A 204 PHE A 208 B 2 THR A 252 ? ILE A 255 ? THR A 248 ILE A 251 B 3 PHE A 285 ? ILE A 287 ? PHE A 281 ILE A 283 C 1 ASN A 226 ? THR A 227 ? ASN A 222 THR A 223 C 2 SER A 259 ? TRP A 260 ? SER A 255 TRP A 256 C 3 VAL A 263 ? LYS A 264 ? VAL A 259 LYS A 260 D 1 VAL A 394 ? ASN A 398 ? VAL A 390 ASN A 394 D 2 ALA A 543 ? ALA A 546 ? ALA A 539 ALA A 542 D 3 CYS A 522 ? ILE A 527 ? CYS A 518 ILE A 523 D 4 ALA A 484 ? GLY A 489 ? ALA A 480 GLY A 485 D 5 LYS A 416 ? ALA A 420 ? LYS A 412 ALA A 416 D 6 VAL A 464 ? ALA A 468 ? VAL A 460 ALA A 464 # 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 A 1 2 O TYR A 146 ? O TYR A 142 N ILE A 98 ? N ILE A 94 A 2 3 O GLY A 97 ? O GLY A 93 N LEU A 57 ? N LEU A 53 A 3 4 O SER A 56 ? O SER A 52 N ILE A 39 ? N ILE A 35 A 4 5 N GLN A 38 ? N GLN A 34 O ILE A 319 ? O ILE A 315 B 1 2 N PHE A 212 ? N PHE A 208 O MET A 254 ? O MET A 250 B 2 3 N VAL A 253 ? N VAL A 249 O ILE A 287 ? O ILE A 283 C 1 2 N THR A 227 ? N THR A 223 O SER A 259 ? O SER A 255 C 2 3 N TRP A 260 ? N TRP A 256 O VAL A 263 ? O VAL A 259 D 1 2 N VAL A 394 ? N VAL A 390 O ALA A 546 ? O ALA A 542 D 2 3 O VAL A 545 ? O VAL A 541 N LEU A 526 ? N LEU A 522 D 3 4 O VAL A 525 ? O VAL A 521 N VAL A 486 ? N VAL A 482 D 4 5 O ILE A 485 ? O ILE A 481 N ALA A 420 ? N ALA A 416 D 5 6 N VAL A 419 ? N VAL A 415 O VAL A 466 ? O VAL A 462 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 704' AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE GOL A 705' AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE GOL A 706' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GOL A 707' AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE GOL A 708' AC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 709' AC7 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 A 710' AC8 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 711' AC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE GOL A 712' BC1 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE GOL A 713' BC2 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE GOL A 714' BC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE GOL A 715' BC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 716' BC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 717' BC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 718' BC7 Software ? ? ? ? 5 'BINDING SITE FOR MONO-SACCHARIDE NAG A 701 BOUND TO ASN A 221' BC8 Software ? ? ? ? 5 'BINDING SITE FOR MONO-SACCHARIDE NAG A 702 BOUND TO ASN A 498' BC9 Software ? ? ? ? 4 'BINDING SITE FOR MONO-SACCHARIDE NAG A 703 BOUND TO ASN A 600' CC1 Software ? ? ? ? 19 'BINDING SITE FOR DI-SACCHARIDE GS1 A 719 AND MGL A 720' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 6 LYS A 309 ? LYS A 305 . ? 1_555 ? 2 AC1 6 VAL A 340 ? VAL A 336 . ? 1_555 ? 3 AC1 6 GLY A 480 ? GLY A 476 . ? 8_655 ? 4 AC1 6 HOH V . ? HOH A 1000 . ? 8_655 ? 5 AC1 6 HOH V . ? HOH A 1428 . ? 1_555 ? 6 AC1 6 HOH V . ? HOH A 1474 . ? 1_555 ? 7 AC2 3 PRO A 299 ? PRO A 295 . ? 1_555 ? 8 AC2 3 ALA A 300 ? ALA A 296 . ? 1_555 ? 9 AC2 3 HOH V . ? HOH A 1567 . ? 1_555 ? 10 AC3 4 ASP A 79 ? ASP A 75 . ? 1_555 ? 11 AC3 4 TYR A 367 ? TYR A 363 . ? 1_555 ? 12 AC3 4 GOL Q . ? GOL A 716 . ? 1_555 ? 13 AC3 4 HOH V . ? HOH A 1180 . ? 1_555 ? 14 AC4 5 ARG A 123 ? ARG A 119 . ? 1_555 ? 15 AC4 5 ILE A 173 ? ILE A 169 . ? 1_555 ? 16 AC4 5 ARG A 570 ? ARG A 566 . ? 1_555 ? 17 AC4 5 LEU A 597 ? LEU A 593 . ? 1_555 ? 18 AC4 5 HOH V . ? HOH A 1469 . ? 1_555 ? 19 AC5 4 ARG A 390 ? ARG A 386 . ? 1_555 ? 20 AC5 4 LYS A 391 ? LYS A 387 . ? 1_555 ? 21 AC5 4 PHE A 565 ? PHE A 561 . ? 1_555 ? 22 AC5 4 HOH V . ? HOH A 864 . ? 1_555 ? 23 AC6 6 GLU A 490 ? GLU A 486 . ? 1_555 ? 24 AC6 6 TYR A 493 ? TYR A 489 . ? 1_555 ? 25 AC6 6 GLY A 498 ? GLY A 494 . ? 1_555 ? 26 AC6 6 ASN A 500 ? ASN A 496 . ? 1_555 ? 27 AC6 6 ARG A 530 ? ARG A 526 . ? 1_555 ? 28 AC6 6 HOH V . ? HOH A 983 . ? 1_555 ? 29 AC7 7 PRO A 342 ? PRO A 338 . ? 1_555 ? 30 AC7 7 MET A 343 ? MET A 339 . ? 1_555 ? 31 AC7 7 SER A 344 ? SER A 340 . ? 1_555 ? 32 AC7 7 HOH V . ? HOH A 808 . ? 1_555 ? 33 AC7 7 HOH V . ? HOH A 823 . ? 8_655 ? 34 AC7 7 HOH V . ? HOH A 1477 . ? 1_555 ? 35 AC7 7 HOH V . ? HOH A 1549 . ? 1_555 ? 36 AC8 6 ARG A 26 ? ARG A 22 . ? 1_555 ? 37 AC8 6 THR A 28 ? THR A 24 . ? 1_555 ? 38 AC8 6 HOH V . ? HOH A 1127 . ? 6_555 ? 39 AC8 6 HOH V . ? HOH A 1188 . ? 1_555 ? 40 AC8 6 HOH V . ? HOH A 1507 . ? 1_555 ? 41 AC8 6 HOH V . ? HOH A 1536 . ? 6_555 ? 42 AC9 3 LYS A 283 ? LYS A 279 . ? 1_555 ? 43 AC9 3 ARG A 355 ? ARG A 351 . ? 1_555 ? 44 AC9 3 HOH V . ? HOH A 1093 . ? 1_555 ? 45 BC1 3 LYS A 281 ? LYS A 277 . ? 1_555 ? 46 BC1 3 LYS A 283 ? LYS A 279 . ? 1_555 ? 47 BC1 3 HOH V . ? HOH A 1563 . ? 1_555 ? 48 BC2 1 THR A 606 ? THR A 602 . ? 1_555 ? 49 BC3 4 ARG A 171 ? ARG A 167 . ? 1_555 ? 50 BC3 4 ARG A 172 ? ARG A 168 . ? 1_555 ? 51 BC3 4 ASN A 236 ? ASN A 232 . ? 1_555 ? 52 BC3 4 HOH V . ? HOH A 1321 . ? 1_555 ? 53 BC4 6 TYR A 367 ? TYR A 363 . ? 1_555 ? 54 BC4 6 ALA A 368 ? ALA A 364 . ? 1_555 ? 55 BC4 6 GOL G . ? GOL A 706 . ? 1_555 ? 56 BC4 6 HOH V . ? HOH A 811 . ? 1_555 ? 57 BC4 6 HOH V . ? HOH A 1004 . ? 1_555 ? 58 BC4 6 HOH V . ? HOH A 1079 . ? 1_555 ? 59 BC5 6 ASN A 337 ? ASN A 333 . ? 6_455 ? 60 BC5 6 ARG A 382 ? ARG A 378 . ? 1_555 ? 61 BC5 6 GLY A 448 ? GLY A 444 . ? 1_555 ? 62 BC5 6 THR A 449 ? THR A 445 . ? 1_555 ? 63 BC5 6 GLU A 553 ? GLU A 549 . ? 1_555 ? 64 BC5 6 HOH V . ? HOH A 1453 . ? 6_455 ? 65 BC6 6 LEU A 594 ? LEU A 590 . ? 1_555 ? 66 BC6 6 PHE A 595 ? PHE A 591 . ? 1_555 ? 67 BC6 6 ARG A 596 ? ARG A 592 . ? 1_555 ? 68 BC6 6 TYR A 599 ? TYR A 595 . ? 1_555 ? 69 BC6 6 HOH V . ? HOH A 923 . ? 1_555 ? 70 BC6 6 HOH V . ? HOH A 1571 . ? 1_555 ? 71 BC7 5 GLU A 224 ? GLU A 220 . ? 1_555 ? 72 BC7 5 ASN A 225 ? ASN A 221 . ? 1_555 ? 73 BC7 5 SER A 259 ? SER A 255 . ? 1_555 ? 74 BC7 5 HOH V . ? HOH A 1034 . ? 1_555 ? 75 BC7 5 HOH V . ? HOH A 1473 . ? 1_555 ? 76 BC8 5 ASP A 499 ? ASP A 495 . ? 1_555 ? 77 BC8 5 ASN A 500 ? ASN A 496 . ? 1_555 ? 78 BC8 5 ASN A 502 ? ASN A 498 . ? 1_555 ? 79 BC8 5 THR A 504 ? THR A 500 . ? 1_555 ? 80 BC8 5 HOH V . ? HOH A 1208 . ? 1_555 ? 81 BC9 4 THR A 45 ? THR A 41 . ? 4_455 ? 82 BC9 4 ASN A 604 ? ASN A 600 . ? 1_555 ? 83 BC9 4 HOH V . ? HOH A 888 . ? 4_455 ? 84 BC9 4 HOH V . ? HOH A 1390 . ? 4_455 ? 85 CC1 19 GLY A 60 ? GLY A 56 . ? 1_555 ? 86 CC1 19 GLY A 61 ? GLY A 57 . ? 1_555 ? 87 CC1 19 ASP A 99 ? ASP A 95 . ? 1_555 ? 88 CC1 19 ARG A 162 ? ARG A 158 . ? 1_555 ? 89 CC1 19 LYS A 210 ? LYS A 206 . ? 1_555 ? 90 CC1 19 HIS A 211 ? HIS A 207 . ? 1_555 ? 91 CC1 19 MET A 254 ? MET A 250 . ? 1_555 ? 92 CC1 19 TYR A 257 ? TYR A 253 . ? 1_555 ? 93 CC1 19 ASP A 289 ? ASP A 285 . ? 1_555 ? 94 CC1 19 TRP A 290 ? TRP A 286 . ? 1_555 ? 95 CC1 19 GLU A 495 ? GLU A 491 . ? 1_555 ? 96 CC1 19 HOH V . ? HOH A 801 . ? 1_555 ? 97 CC1 19 HOH V . ? HOH A 802 . ? 1_555 ? 98 CC1 19 HOH V . ? HOH A 803 . ? 1_555 ? 99 CC1 19 HOH V . ? HOH A 804 . ? 1_555 ? 100 CC1 19 HOH V . ? HOH A 805 . ? 1_555 ? 101 CC1 19 HOH V . ? HOH A 806 . ? 1_555 ? 102 CC1 19 HOH V . ? HOH A 807 . ? 1_555 ? 103 CC1 19 HOH V . ? HOH A 910 . ? 1_555 ? # _database_PDB_matrix.entry_id 3WLT _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 3WLT _atom_sites.fract_transf_matrix[1][1] 0.009948 _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] 0.009948 _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] 0.005492 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . HIS A 1 1 ? 23.672 -0.536 1.572 1.00 69.94 ? -3 HIS A N 1 ATOM 2 C CA . HIS A 1 1 ? 22.212 -0.846 1.445 1.00 70.41 ? -3 HIS A CA 1 ATOM 3 C C . HIS A 1 1 ? 21.449 0.055 0.466 1.00 69.98 ? -3 HIS A C 1 ATOM 4 O O . HIS A 1 1 ? 20.374 0.561 0.810 1.00 70.10 ? -3 HIS A O 1 ATOM 5 C CB . HIS A 1 1 ? 21.507 -0.886 2.819 1.00 70.86 ? -3 HIS A CB 1 ATOM 6 C CG . HIS A 1 1 ? 21.122 -2.266 3.281 1.00 73.84 ? -3 HIS A CG 1 ATOM 7 N ND1 . HIS A 1 1 ? 19.843 -2.769 3.146 1.00 75.28 ? -3 HIS A ND1 1 ATOM 8 C CD2 . HIS A 1 1 ? 21.847 -3.243 3.884 1.00 76.10 ? -3 HIS A CD2 1 ATOM 9 C CE1 . HIS A 1 1 ? 19.798 -3.996 3.637 1.00 76.47 ? -3 HIS A CE1 1 ATOM 10 N NE2 . HIS A 1 1 ? 21.000 -4.309 4.090 1.00 77.17 ? -3 HIS A NE2 1 ATOM 11 N N . HIS A 1 2 ? 22.054 0.300 -0.707 1.00 69.69 ? -2 HIS A N 1 ATOM 12 C CA . HIS A 1 2 ? 21.365 0.429 -2.045 1.00 69.40 ? -2 HIS A CA 1 ATOM 13 C C . HIS A 1 2 ? 21.836 1.453 -3.102 1.00 68.23 ? -2 HIS A C 1 ATOM 14 O O . HIS A 1 2 ? 22.348 1.045 -4.149 1.00 68.63 ? -2 HIS A O 1 ATOM 15 C CB . HIS A 1 2 ? 19.831 0.250 -2.004 1.00 70.23 ? -2 HIS A CB 1 ATOM 16 C CG . HIS A 1 2 ? 19.392 -1.162 -1.714 1.00 72.73 ? -2 HIS A CG 1 ATOM 17 N ND1 . HIS A 1 2 ? 18.289 -1.741 -2.309 1.00 73.86 ? -2 HIS A ND1 1 ATOM 18 C CD2 . HIS A 1 2 ? 19.912 -2.109 -0.891 1.00 73.20 ? -2 HIS A CD2 1 ATOM 19 C CE1 . HIS A 1 2 ? 18.139 -2.972 -1.852 1.00 73.87 ? -2 HIS A CE1 1 ATOM 20 N NE2 . HIS A 1 2 ? 19.110 -3.220 -0.989 1.00 73.36 ? -2 HIS A NE2 1 ATOM 21 N N . ALA A 1 3 ? 21.674 2.759 -2.867 1.00 66.03 ? -1 ALA A N 1 ATOM 22 C CA . ALA A 1 3 ? 22.190 3.766 -3.828 1.00 63.67 ? -1 ALA A CA 1 ATOM 23 C C . ALA A 1 3 ? 23.725 3.793 -3.860 1.00 62.21 ? -1 ALA A C 1 ATOM 24 O O . ALA A 1 3 ? 24.363 3.572 -2.834 1.00 62.38 ? -1 ALA A O 1 ATOM 25 C CB . ALA A 1 3 ? 21.650 5.142 -3.491 1.00 63.86 ? -1 ALA A CB 1 ATOM 26 N N . ALA A 1 4 ? 24.328 4.070 -5.019 1.00 59.80 ? 0 ALA A N 1 ATOM 27 C CA . ALA A 1 4 ? 25.800 4.035 -5.145 1.00 57.48 ? 0 ALA A CA 1 ATOM 28 C C . ALA A 1 4 ? 26.607 4.950 -4.181 1.00 55.17 ? 0 ALA A C 1 ATOM 29 O O . ALA A 1 4 ? 27.711 4.591 -3.773 1.00 54.50 ? 0 ALA A O 1 ATOM 30 C CB . ALA A 1 4 ? 26.224 4.269 -6.590 1.00 58.33 ? 0 ALA A CB 1 ATOM 31 N N . ASP A 1 5 ? 26.060 6.119 -3.837 1.00 52.35 ? 1 ASP A N 1 ATOM 32 C CA . ASP A 1 5 ? 26.675 7.012 -2.827 1.00 49.56 ? 1 ASP A CA 1 ATOM 33 C C . ASP A 1 5 ? 26.166 6.734 -1.364 1.00 46.51 ? 1 ASP A C 1 ATOM 34 O O . ASP A 1 5 ? 26.080 7.642 -0.545 1.00 44.86 ? 1 ASP A O 1 ATOM 35 C CB . ASP A 1 5 ? 26.414 8.466 -3.214 1.00 49.30 ? 1 ASP A CB 1 ATOM 36 C CG . ASP A 1 5 ? 24.951 8.869 -3.031 1.00 54.62 ? 1 ASP A CG 1 ATOM 37 O OD1 . ASP A 1 5 ? 24.084 7.952 -3.014 1.00 55.91 ? 1 ASP A OD1 1 ATOM 38 O OD2 . ASP A 1 5 ? 24.670 10.096 -2.868 1.00 57.03 ? 1 ASP A OD2 1 ATOM 39 N N . TYR A 1 6 ? 25.781 5.493 -1.067 1.00 43.90 ? 2 TYR A N 1 ATOM 40 C CA . TYR A 1 6 ? 25.228 5.143 0.254 1.00 40.00 ? 2 TYR A CA 1 ATOM 41 C C . TYR A 1 6 ? 26.271 5.346 1.365 1.00 38.02 ? 2 TYR A C 1 ATOM 42 O O . TYR A 1 6 ? 27.436 5.053 1.190 1.00 37.11 ? 2 TYR A O 1 ATOM 43 C CB . TYR A 1 6 ? 24.825 3.684 0.238 1.00 40.70 ? 2 TYR A CB 1 ATOM 44 C CG . TYR A 1 6 ? 24.287 3.101 1.523 1.00 36.04 ? 2 TYR A CG 1 ATOM 45 C CD1 . TYR A 1 6 ? 22.976 3.315 1.908 1.00 36.79 ? 2 TYR A CD1 1 ATOM 46 C CD2 . TYR A 1 6 ? 25.079 2.281 2.310 1.00 35.93 ? 2 TYR A CD2 1 ATOM 47 C CE1 . TYR A 1 6 ? 22.478 2.745 3.077 1.00 37.10 ? 2 TYR A CE1 1 ATOM 48 C CE2 . TYR A 1 6 ? 24.585 1.716 3.487 1.00 35.07 ? 2 TYR A CE2 1 ATOM 49 C CZ . TYR A 1 6 ? 23.298 1.976 3.859 1.00 32.37 ? 2 TYR A CZ 1 ATOM 50 O OH . TYR A 1 6 ? 22.788 1.391 4.994 1.00 33.95 ? 2 TYR A OH 1 ATOM 51 N N . VAL A 1 7 ? 25.822 5.827 2.520 1.00 36.32 ? 3 VAL A N 1 ATOM 52 C CA . VAL A 1 7 ? 26.674 5.995 3.668 1.00 34.03 ? 3 VAL A CA 1 ATOM 53 C C . VAL A 1 7 ? 25.874 5.406 4.834 1.00 32.75 ? 3 VAL A C 1 ATOM 54 O O . VAL A 1 7 ? 24.813 5.952 5.178 1.00 31.65 ? 3 VAL A O 1 ATOM 55 C CB . VAL A 1 7 ? 26.936 7.519 3.848 1.00 35.79 ? 3 VAL A CB 1 ATOM 56 C CG1 . VAL A 1 7 ? 27.559 7.823 5.171 1.00 33.67 ? 3 VAL A CG1 1 ATOM 57 C CG2 . VAL A 1 7 ? 27.846 8.026 2.716 1.00 34.40 ? 3 VAL A CG2 1 ATOM 58 N N . LEU A 1 8 ? 26.361 4.316 5.434 1.00 30.35 ? 4 LEU A N 1 ATOM 59 C CA . LEU A 1 8 ? 25.582 3.576 6.416 1.00 30.81 ? 4 LEU A CA 1 ATOM 60 C C . LEU A 1 8 ? 25.099 4.482 7.566 1.00 29.89 ? 4 LEU A C 1 ATOM 61 O O . LEU A 1 8 ? 23.952 4.359 8.001 1.00 28.22 ? 4 LEU A O 1 ATOM 62 C CB . LEU A 1 8 ? 26.359 2.363 6.972 1.00 30.56 ? 4 LEU A CB 1 ATOM 63 C CG . LEU A 1 8 ? 25.531 1.389 7.847 1.00 32.29 ? 4 LEU A CG 1 ATOM 64 C CD1 . LEU A 1 8 ? 26.087 -0.029 7.696 1.00 37.45 ? 4 LEU A CD1 1 ATOM 65 C CD2 . LEU A 1 8 ? 25.481 1.808 9.350 1.00 30.55 ? 4 LEU A CD2 1 ATOM 66 N N . TYR A 1 9 ? 25.957 5.372 8.074 1.00 27.97 ? 5 TYR A N 1 ATOM 67 C CA . TYR A 1 9 ? 25.508 6.126 9.262 1.00 27.05 ? 5 TYR A CA 1 ATOM 68 C C . TYR A 1 9 ? 24.307 7.066 8.984 1.00 27.46 ? 5 TYR A C 1 ATOM 69 O O . TYR A 1 9 ? 23.594 7.473 9.925 1.00 26.79 ? 5 TYR A O 1 ATOM 70 C CB . TYR A 1 9 ? 26.676 6.867 9.970 1.00 26.73 ? 5 TYR A CB 1 ATOM 71 C CG . TYR A 1 9 ? 27.149 8.134 9.294 1.00 24.32 ? 5 TYR A CG 1 ATOM 72 C CD1 . TYR A 1 9 ? 26.540 9.373 9.559 1.00 22.58 ? 5 TYR A CD1 1 ATOM 73 C CD2 . TYR A 1 9 ? 28.281 8.106 8.452 1.00 25.94 ? 5 TYR A CD2 1 ATOM 74 C CE1 . TYR A 1 9 ? 27.009 10.564 8.946 1.00 22.69 ? 5 TYR A CE1 1 ATOM 75 C CE2 . TYR A 1 9 ? 28.761 9.262 7.847 1.00 24.81 ? 5 TYR A CE2 1 ATOM 76 C CZ . TYR A 1 9 ? 28.112 10.491 8.070 1.00 25.75 ? 5 TYR A CZ 1 ATOM 77 O OH . TYR A 1 9 ? 28.610 11.633 7.451 1.00 22.44 ? 5 TYR A OH 1 ATOM 78 N N . LYS A 1 10 ? 24.085 7.418 7.715 1.00 28.06 ? 6 LYS A N 1 ATOM 79 C CA . LYS A 1 10 ? 22.965 8.307 7.334 1.00 28.46 ? 6 LYS A CA 1 ATOM 80 C C . LYS A 1 10 ? 21.671 7.530 7.096 1.00 29.20 ? 6 LYS A C 1 ATOM 81 O O . LYS A 1 10 ? 20.637 8.103 6.818 1.00 28.47 ? 6 LYS A O 1 ATOM 82 C CB . LYS A 1 10 ? 23.331 9.134 6.072 1.00 28.70 ? 6 LYS A CB 1 ATOM 83 C CG . LYS A 1 10 ? 24.478 10.154 6.322 1.00 28.03 ? 6 LYS A CG 1 ATOM 84 C CD . LYS A 1 10 ? 24.842 10.935 5.071 1.00 30.55 ? 6 LYS A CD 1 ATOM 85 C CE . LYS A 1 10 ? 25.783 12.119 5.436 1.00 34.86 ? 6 LYS A CE 1 ATOM 86 N NZ . LYS A 1 10 ? 26.263 12.718 4.162 1.00 41.77 ? 6 LYS A NZ 1 ATOM 87 N N . ASP A 1 11 ? 21.744 6.212 7.202 1.00 29.31 ? 7 ASP A N 1 ATOM 88 C CA . ASP A 1 11 ? 20.584 5.351 6.900 1.00 29.27 ? 7 ASP A CA 1 ATOM 89 C C . ASP A 1 11 ? 19.785 5.137 8.207 1.00 28.95 ? 7 ASP A C 1 ATOM 90 O O . ASP A 1 11 ? 20.243 4.449 9.148 1.00 28.91 ? 7 ASP A O 1 ATOM 91 C CB . ASP A 1 11 ? 21.118 4.004 6.366 1.00 29.46 ? 7 ASP A CB 1 ATOM 92 C CG . ASP A 1 11 ? 20.000 3.011 6.047 1.00 32.79 ? 7 ASP A CG 1 ATOM 93 O OD1 . ASP A 1 11 ? 20.354 2.014 5.398 1.00 30.67 ? 7 ASP A OD1 1 ATOM 94 O OD2 . ASP A 1 11 ? 18.815 3.210 6.468 1.00 29.30 ? 7 ASP A OD2 1 ATOM 95 N N . ALA A 1 12 ? 18.602 5.726 8.266 1.00 28.18 ? 8 ALA A N 1 ATOM 96 C CA . ALA A 1 12 ? 17.731 5.674 9.455 1.00 29.82 ? 8 ALA A CA 1 ATOM 97 C C . ALA A 1 12 ? 17.210 4.282 9.824 1.00 31.57 ? 8 ALA A C 1 ATOM 98 O O . ALA A 1 12 ? 16.732 4.084 10.952 1.00 30.85 ? 8 ALA A O 1 ATOM 99 C CB . ALA A 1 12 ? 16.547 6.607 9.231 1.00 29.77 ? 8 ALA A CB 1 ATOM 100 N N . THR A 1 13 ? 17.259 3.322 8.879 1.00 33.04 ? 9 THR A N 1 ATOM 101 C CA . THR A 1 13 ? 16.790 1.955 9.170 1.00 33.59 ? 9 THR A CA 1 ATOM 102 C C . THR A 1 13 ? 17.809 1.066 9.892 1.00 34.66 ? 9 THR A C 1 ATOM 103 O O . THR A 1 13 ? 17.472 -0.038 10.341 1.00 35.67 ? 9 THR A O 1 ATOM 104 C CB . THR A 1 13 ? 16.335 1.242 7.881 1.00 34.74 ? 9 THR A CB 1 ATOM 105 O OG1 . THR A 1 13 ? 17.472 0.950 7.056 1.00 32.25 ? 9 THR A OG1 1 ATOM 106 C CG2 . THR A 1 13 ? 15.365 2.150 7.149 1.00 34.45 ? 9 THR A CG2 1 ATOM 107 N N . LYS A 1 14 ? 19.051 1.542 10.025 1.00 33.51 ? 10 LYS A N 1 ATOM 108 C CA . LYS A 1 14 ? 20.124 0.737 10.613 1.00 32.47 ? 10 LYS A CA 1 ATOM 109 C C . LYS A 1 14 ? 20.141 0.874 12.142 1.00 32.18 ? 10 LYS A C 1 ATOM 110 O O . LYS A 1 14 ? 19.761 1.917 12.648 1.00 32.33 ? 10 LYS A O 1 ATOM 111 C CB . LYS A 1 14 ? 21.471 1.217 10.055 1.00 31.93 ? 10 LYS A CB 1 ATOM 112 C CG . LYS A 1 14 ? 21.692 0.816 8.612 1.00 34.80 ? 10 LYS A CG 1 ATOM 113 C CD . LYS A 1 14 ? 22.060 -0.697 8.540 1.00 35.55 ? 10 LYS A CD 1 ATOM 114 C CE . LYS A 1 14 ? 22.046 -1.185 7.111 1.00 41.42 ? 10 LYS A CE 1 ATOM 115 N NZ . LYS A 1 14 ? 22.735 -2.508 7.098 1.00 46.72 ? 10 LYS A NZ 1 ATOM 116 N N . PRO A 1 15 ? 20.623 -0.164 12.867 1.00 32.36 ? 11 PRO A N 1 ATOM 117 C CA . PRO A 1 15 ? 20.764 -0.136 14.328 1.00 32.12 ? 11 PRO A CA 1 ATOM 118 C C . PRO A 1 15 ? 21.655 0.998 14.745 1.00 30.31 ? 11 PRO A C 1 ATOM 119 O O . PRO A 1 15 ? 22.623 1.303 14.052 1.00 29.12 ? 11 PRO A O 1 ATOM 120 C CB . PRO A 1 15 ? 21.501 -1.437 14.629 1.00 32.69 ? 11 PRO A CB 1 ATOM 121 C CG . PRO A 1 15 ? 20.965 -2.391 13.604 1.00 34.61 ? 11 PRO A CG 1 ATOM 122 C CD . PRO A 1 15 ? 20.791 -1.533 12.340 1.00 33.84 ? 11 PRO A CD 1 ATOM 123 N N . VAL A 1 16 ? 21.347 1.583 15.904 1.00 28.94 ? 12 VAL A N 1 ATOM 124 C CA . VAL A 1 16 ? 22.088 2.750 16.398 1.00 27.32 ? 12 VAL A CA 1 ATOM 125 C C . VAL A 1 16 ? 23.560 2.371 16.545 1.00 27.47 ? 12 VAL A C 1 ATOM 126 O O . VAL A 1 16 ? 24.393 3.103 16.081 1.00 25.89 ? 12 VAL A O 1 ATOM 127 C CB . VAL A 1 16 ? 21.490 3.233 17.786 1.00 28.28 ? 12 VAL A CB 1 ATOM 128 C CG1 . VAL A 1 16 ? 22.487 4.124 18.530 1.00 25.25 ? 12 VAL A CG1 1 ATOM 129 C CG2 . VAL A 1 16 ? 20.115 3.906 17.565 1.00 27.32 ? 12 VAL A CG2 1 ATOM 130 N N . GLU A 1 17 ? 23.891 1.220 17.156 1.00 27.29 ? 13 GLU A N 1 ATOM 131 C CA . GLU A 1 17 ? 25.327 0.891 17.337 1.00 28.22 ? 13 GLU A CA 1 ATOM 132 C C . GLU A 1 17 ? 26.104 0.767 15.987 1.00 28.01 ? 13 GLU A C 1 ATOM 133 O O . GLU A 1 17 ? 27.280 1.106 15.907 1.00 28.10 ? 13 GLU A O 1 ATOM 134 C CB . GLU A 1 17 ? 25.552 -0.398 18.143 1.00 30.49 ? 13 GLU A CB 1 ATOM 135 C CG . GLU A 1 17 ? 24.986 -0.403 19.563 1.00 30.55 ? 13 GLU A CG 1 ATOM 136 C CD . GLU A 1 17 ? 25.521 0.764 20.382 1.00 36.06 ? 13 GLU A CD 1 ATOM 137 O OE1 . GLU A 1 17 ? 24.685 1.545 20.901 1.00 35.28 ? 13 GLU A OE1 1 ATOM 138 O OE2 . GLU A 1 17 ? 26.766 0.927 20.468 1.00 34.52 ? 13 GLU A OE2 1 ATOM 139 N N . ASP A 1 18 ? 25.440 0.282 14.952 1.00 27.61 ? 14 ASP A N 1 ATOM 140 C CA . ASP A 1 18 ? 26.110 0.141 13.668 1.00 29.08 ? 14 ASP A CA 1 ATOM 141 C C . ASP A 1 18 ? 26.308 1.538 13.087 1.00 26.73 ? 14 ASP A C 1 ATOM 142 O O . ASP A 1 18 ? 27.323 1.809 12.477 1.00 26.63 ? 14 ASP A O 1 ATOM 143 C CB . ASP A 1 18 ? 25.301 -0.681 12.681 1.00 29.20 ? 14 ASP A CB 1 ATOM 144 C CG . ASP A 1 18 ? 25.146 -2.119 13.113 1.00 35.52 ? 14 ASP A CG 1 ATOM 145 O OD1 . ASP A 1 18 ? 25.914 -2.603 13.982 1.00 37.80 ? 14 ASP A OD1 1 ATOM 146 O OD2 . ASP A 1 18 ? 24.239 -2.740 12.564 1.00 35.18 ? 14 ASP A OD2 1 ATOM 147 N N . ARG A 1 19 ? 25.330 2.422 13.270 1.00 26.18 ? 15 ARG A N 1 ATOM 148 C CA . ARG A 1 19 ? 25.501 3.823 12.797 1.00 25.18 ? 15 ARG A CA 1 ATOM 149 C C . ARG A 1 19 ? 26.629 4.545 13.541 1.00 25.77 ? 15 ARG A C 1 ATOM 150 O O . ARG A 1 19 ? 27.461 5.244 12.917 1.00 25.77 ? 15 ARG A O 1 ATOM 151 C CB . ARG A 1 19 ? 24.163 4.614 12.918 1.00 25.13 ? 15 ARG A CB 1 ATOM 152 C CG . ARG A 1 19 ? 23.041 3.981 12.089 1.00 26.10 ? 15 ARG A CG 1 ATOM 153 C CD . ARG A 1 19 ? 21.686 4.737 12.219 1.00 25.19 ? 15 ARG A CD 1 ATOM 154 N NE . ARG A 1 19 ? 21.753 6.034 11.530 1.00 24.20 ? 15 ARG A NE 1 ATOM 155 C CZ . ARG A 1 19 ? 20.790 6.942 11.573 1.00 27.98 ? 15 ARG A CZ 1 ATOM 156 N NH1 . ARG A 1 19 ? 19.710 6.710 12.335 1.00 24.84 ? 15 ARG A NH1 1 ATOM 157 N NH2 . ARG A 1 19 ? 20.904 8.085 10.881 1.00 21.72 ? 15 ARG A NH2 1 ATOM 158 N N . VAL A 1 20 ? 26.629 4.423 14.870 1.00 26.12 ? 16 VAL A N 1 ATOM 159 C CA . VAL A 1 20 ? 27.741 4.961 15.702 1.00 26.01 ? 16 VAL A CA 1 ATOM 160 C C . VAL A 1 20 ? 29.134 4.513 15.201 1.00 27.37 ? 16 VAL A C 1 ATOM 161 O O . VAL A 1 20 ? 29.997 5.364 14.971 1.00 26.98 ? 16 VAL A O 1 ATOM 162 C CB . VAL A 1 20 ? 27.594 4.581 17.181 1.00 26.41 ? 16 VAL A CB 1 ATOM 163 C CG1 . VAL A 1 20 ? 28.831 5.028 18.022 1.00 24.44 ? 16 VAL A CG1 1 ATOM 164 C CG2 . VAL A 1 20 ? 26.329 5.291 17.784 1.00 25.65 ? 16 VAL A CG2 1 ATOM 165 N N . ALA A 1 21 ? 29.312 3.199 15.015 1.00 27.98 ? 17 ALA A N 1 ATOM 166 C CA . ALA A 1 21 ? 30.602 2.631 14.607 1.00 28.35 ? 17 ALA A CA 1 ATOM 167 C C . ALA A 1 21 ? 30.950 3.096 13.201 1.00 28.22 ? 17 ALA A C 1 ATOM 168 O O . ALA A 1 21 ? 32.124 3.449 12.934 1.00 29.00 ? 17 ALA A O 1 ATOM 169 C CB . ALA A 1 21 ? 30.530 1.139 14.623 1.00 29.52 ? 17 ALA A CB 1 ATOM 170 N N . ASP A 1 22 ? 29.949 3.095 12.316 1.00 28.24 ? 18 ASP A N 1 ATOM 171 C CA . ASP A 1 22 ? 30.177 3.510 10.946 1.00 29.12 ? 18 ASP A CA 1 ATOM 172 C C . ASP A 1 22 ? 30.700 4.944 10.880 1.00 27.87 ? 18 ASP A C 1 ATOM 173 O O . ASP A 1 22 ? 31.644 5.253 10.141 1.00 27.40 ? 18 ASP A O 1 ATOM 174 C CB . ASP A 1 22 ? 28.942 3.359 10.052 1.00 28.40 ? 18 ASP A CB 1 ATOM 175 C CG . ASP A 1 22 ? 29.255 3.707 8.591 1.00 31.85 ? 18 ASP A CG 1 ATOM 176 O OD1 . ASP A 1 22 ? 29.878 2.868 7.919 1.00 32.41 ? 18 ASP A OD1 1 ATOM 177 O OD2 . ASP A 1 22 ? 28.946 4.819 8.116 1.00 31.98 ? 18 ASP A OD2 1 ATOM 178 N N . LEU A 1 23 ? 30.083 5.838 11.653 1.00 26.79 ? 19 LEU A N 1 ATOM 179 C CA . LEU A 1 23 ? 30.445 7.253 11.593 1.00 24.80 ? 19 LEU A CA 1 ATOM 180 C C . LEU A 1 23 ? 31.791 7.461 12.320 1.00 25.73 ? 19 LEU A C 1 ATOM 181 O O . LEU A 1 23 ? 32.705 8.143 11.818 1.00 26.17 ? 19 LEU A O 1 ATOM 182 C CB . LEU A 1 23 ? 29.318 8.103 12.234 1.00 25.21 ? 19 LEU A CB 1 ATOM 183 C CG . LEU A 1 23 ? 29.650 9.590 12.482 1.00 24.73 ? 19 LEU A CG 1 ATOM 184 C CD1 . LEU A 1 23 ? 30.110 10.279 11.119 1.00 24.38 ? 19 LEU A CD1 1 ATOM 185 C CD2 . LEU A 1 23 ? 28.405 10.323 13.084 1.00 21.90 ? 19 LEU A CD2 1 ATOM 186 N N . LEU A 1 24 ? 31.941 6.845 13.481 1.00 25.44 ? 20 LEU A N 1 ATOM 187 C CA . LEU A 1 24 ? 33.190 7.022 14.258 1.00 26.64 ? 20 LEU A CA 1 ATOM 188 C C . LEU A 1 24 ? 34.440 6.681 13.420 1.00 27.15 ? 20 LEU A C 1 ATOM 189 O O . LEU A 1 24 ? 35.468 7.352 13.521 1.00 26.66 ? 20 LEU A O 1 ATOM 190 C CB . LEU A 1 24 ? 33.175 6.066 15.457 1.00 26.17 ? 20 LEU A CB 1 ATOM 191 C CG . LEU A 1 24 ? 34.357 6.183 16.448 1.00 27.44 ? 20 LEU A CG 1 ATOM 192 C CD1 . LEU A 1 24 ? 34.513 7.607 17.128 1.00 26.13 ? 20 LEU A CD1 1 ATOM 193 C CD2 . LEU A 1 24 ? 34.212 5.043 17.485 1.00 26.76 ? 20 LEU A CD2 1 ATOM 194 N N . GLY A 1 25 ? 34.330 5.584 12.672 1.00 27.46 ? 21 GLY A N 1 ATOM 195 C CA . GLY A 1 25 ? 35.443 5.030 11.903 1.00 28.81 ? 21 GLY A CA 1 ATOM 196 C C . GLY A 1 25 ? 35.813 5.912 10.737 1.00 29.03 ? 21 GLY A C 1 ATOM 197 O O . GLY A 1 25 ? 36.828 5.672 10.116 1.00 29.46 ? 21 GLY A O 1 ATOM 198 N N . ARG A 1 26 ? 35.000 6.933 10.429 1.00 27.69 ? 22 ARG A N 1 ATOM 199 C CA . ARG A 1 26 ? 35.322 7.885 9.365 1.00 27.78 ? 22 ARG A CA 1 ATOM 200 C C . ARG A 1 26 ? 35.894 9.211 9.874 1.00 27.70 ? 22 ARG A C 1 ATOM 201 O O . ARG A 1 26 ? 36.290 10.064 9.074 1.00 27.50 ? 22 ARG A O 1 ATOM 202 C CB . ARG A 1 26 ? 34.038 8.249 8.594 1.00 27.70 ? 22 ARG A CB 1 ATOM 203 C CG . ARG A 1 26 ? 33.358 7.046 7.905 1.00 26.81 ? 22 ARG A CG 1 ATOM 204 C CD . ARG A 1 26 ? 31.976 7.469 7.403 1.00 27.91 ? 22 ARG A CD 1 ATOM 205 N NE . ARG A 1 26 ? 31.134 6.345 6.990 1.00 26.17 ? 22 ARG A NE 1 ATOM 206 C CZ . ARG A 1 26 ? 31.013 5.934 5.727 1.00 33.87 ? 22 ARG A CZ 1 ATOM 207 N NH1 . ARG A 1 26 ? 31.724 6.538 4.782 1.00 33.95 ? 22 ARG A NH1 1 ATOM 208 N NH2 . ARG A 1 26 ? 30.204 4.895 5.414 1.00 34.01 ? 22 ARG A NH2 1 ATOM 209 N N . MET A 1 27 ? 35.882 9.428 11.187 1.00 26.74 ? 23 MET A N 1 ATOM 210 C CA . MET A 1 27 ? 36.143 10.807 11.724 1.00 25.77 ? 23 MET A CA 1 ATOM 211 C C . MET A 1 27 ? 37.632 11.078 11.959 1.00 27.79 ? 23 MET A C 1 ATOM 212 O O . MET A 1 27 ? 38.341 10.206 12.434 1.00 28.81 ? 23 MET A O 1 ATOM 213 C CB . MET A 1 27 ? 35.418 10.962 13.064 1.00 25.73 ? 23 MET A CB 1 ATOM 214 C CG . MET A 1 27 ? 33.842 11.012 12.865 1.00 23.79 ? 23 MET A CG 1 ATOM 215 S SD . MET A 1 27 ? 33.004 10.881 14.487 1.00 26.25 ? 23 MET A SD 1 ATOM 216 C CE . MET A 1 27 ? 33.298 12.555 15.024 1.00 22.94 ? 23 MET A CE 1 ATOM 217 N N . THR A 1 28 ? 38.072 12.286 11.652 1.00 27.71 ? 24 THR A N 1 ATOM 218 C CA . THR A 1 28 ? 39.399 12.733 11.995 1.00 29.06 ? 24 THR A CA 1 ATOM 219 C C . THR A 1 28 ? 39.418 13.052 13.483 1.00 29.30 ? 24 THR A C 1 ATOM 220 O O . THR A 1 28 ? 38.365 13.178 14.139 1.00 28.15 ? 24 THR A O 1 ATOM 221 C CB . THR A 1 28 ? 39.759 14.035 11.216 1.00 29.48 ? 24 THR A CB 1 ATOM 222 O OG1 . THR A 1 28 ? 38.897 15.085 11.664 1.00 26.36 ? 24 THR A OG1 1 ATOM 223 C CG2 . THR A 1 28 ? 39.557 13.851 9.665 1.00 27.40 ? 24 THR A CG2 1 ATOM 224 N N . LEU A 1 29 ? 40.613 13.199 14.032 1.00 28.59 ? 25 LEU A N 1 ATOM 225 C CA . LEU A 1 29 ? 40.751 13.668 15.405 1.00 27.58 ? 25 LEU A CA 1 ATOM 226 C C . LEU A 1 29 ? 40.060 15.035 15.642 1.00 26.84 ? 25 LEU A C 1 ATOM 227 O O . LEU A 1 29 ? 39.396 15.239 16.673 1.00 24.50 ? 25 LEU A O 1 ATOM 228 C CB . LEU A 1 29 ? 42.240 13.742 15.795 1.00 28.76 ? 25 LEU A CB 1 ATOM 229 C CG . LEU A 1 29 ? 42.457 14.294 17.212 1.00 29.20 ? 25 LEU A CG 1 ATOM 230 C CD1 . LEU A 1 29 ? 41.893 13.354 18.207 1.00 26.09 ? 25 LEU A CD1 1 ATOM 231 C CD2 . LEU A 1 29 ? 44.014 14.507 17.456 1.00 28.85 ? 25 LEU A CD2 1 ATOM 232 N N . ALA A 1 30 ? 40.225 15.978 14.732 1.00 25.52 ? 26 ALA A N 1 ATOM 233 C CA . ALA A 1 30 ? 39.550 17.274 14.903 1.00 26.79 ? 26 ALA A CA 1 ATOM 234 C C . ALA A 1 30 ? 37.991 17.125 14.990 1.00 27.01 ? 26 ALA A C 1 ATOM 235 O O . ALA A 1 30 ? 37.312 17.853 15.767 1.00 25.44 ? 26 ALA A O 1 ATOM 236 C CB . ALA A 1 30 ? 39.941 18.261 13.762 1.00 26.71 ? 26 ALA A CB 1 ATOM 237 N N . GLU A 1 31 ? 37.452 16.211 14.177 1.00 26.53 ? 27 GLU A N 1 ATOM 238 C CA . GLU A 1 31 ? 35.987 15.940 14.155 1.00 25.66 ? 27 GLU A CA 1 ATOM 239 C C . GLU A 1 31 ? 35.527 15.279 15.445 1.00 25.20 ? 27 GLU A C 1 ATOM 240 O O . GLU A 1 31 ? 34.457 15.624 15.995 1.00 25.32 ? 27 GLU A O 1 ATOM 241 C CB . GLU A 1 31 ? 35.579 15.100 12.926 1.00 25.17 ? 27 GLU A CB 1 ATOM 242 C CG . GLU A 1 31 ? 35.665 15.936 11.635 1.00 22.87 ? 27 GLU A CG 1 ATOM 243 C CD . GLU A 1 31 ? 35.667 15.131 10.372 1.00 25.57 ? 27 GLU A CD 1 ATOM 244 O OE1 . GLU A 1 31 ? 35.990 13.917 10.383 1.00 24.82 ? 27 GLU A OE1 1 ATOM 245 O OE2 . GLU A 1 31 ? 35.280 15.720 9.340 1.00 26.52 ? 27 GLU A OE2 1 ATOM 246 N N . LYS A 1 32 ? 36.372 14.385 15.951 1.00 25.41 ? 28 LYS A N 1 ATOM 247 C CA . LYS A 1 32 ? 36.134 13.734 17.243 1.00 25.72 ? 28 LYS A CA 1 ATOM 248 C C . LYS A 1 32 ? 36.160 14.718 18.418 1.00 25.56 ? 28 LYS A C 1 ATOM 249 O O . LYS A 1 32 ? 35.241 14.795 19.242 1.00 24.18 ? 28 LYS A O 1 ATOM 250 C CB . LYS A 1 32 ? 37.184 12.632 17.451 1.00 25.81 ? 28 LYS A CB 1 ATOM 251 C CG . LYS A 1 32 ? 36.913 11.407 16.622 1.00 26.00 ? 28 LYS A CG 1 ATOM 252 C CD . LYS A 1 32 ? 38.036 10.356 16.805 1.00 26.60 ? 28 LYS A CD 1 ATOM 253 C CE . LYS A 1 32 ? 37.911 9.273 15.736 1.00 28.13 ? 28 LYS A CE 1 ATOM 254 N NZ . LYS A 1 32 ? 38.882 8.113 15.977 1.00 26.90 ? 28 LYS A NZ 1 ATOM 255 N N . ILE A 1 33 ? 37.221 15.512 18.496 1.00 25.00 ? 29 ILE A N 1 ATOM 256 C CA . ILE A 1 33 ? 37.331 16.443 19.631 1.00 24.87 ? 29 ILE A CA 1 ATOM 257 C C . ILE A 1 33 ? 36.229 17.517 19.493 1.00 24.29 ? 29 ILE A C 1 ATOM 258 O O . ILE A 1 33 ? 35.689 17.989 20.491 1.00 24.03 ? 29 ILE A O 1 ATOM 259 C CB . ILE A 1 33 ? 38.741 17.041 19.717 1.00 23.74 ? 29 ILE A CB 1 ATOM 260 C CG1 . ILE A 1 33 ? 39.708 15.998 20.347 1.00 24.37 ? 29 ILE A CG1 1 ATOM 261 C CG2 . ILE A 1 33 ? 38.748 18.302 20.562 1.00 24.30 ? 29 ILE A CG2 1 ATOM 262 C CD1 . ILE A 1 33 ? 41.218 16.451 20.144 1.00 26.07 ? 29 ILE A CD1 1 ATOM 263 N N . GLY A 1 34 ? 35.852 17.845 18.258 1.00 24.28 ? 30 GLY A N 1 ATOM 264 C CA . GLY A 1 34 ? 34.722 18.750 18.041 1.00 24.35 ? 30 GLY A CA 1 ATOM 265 C C . GLY A 1 34 ? 33.432 18.230 18.709 1.00 22.46 ? 30 GLY A C 1 ATOM 266 O O . GLY A 1 34 ? 32.683 19.005 19.320 1.00 23.23 ? 30 GLY A O 1 ATOM 267 N N . GLN A 1 35 ? 33.136 16.948 18.542 1.00 22.84 ? 31 GLN A N 1 ATOM 268 C CA . GLN A 1 35 ? 31.937 16.373 19.152 1.00 23.15 ? 31 GLN A CA 1 ATOM 269 C C . GLN A 1 35 ? 31.925 16.565 20.661 1.00 23.64 ? 31 GLN A C 1 ATOM 270 O O . GLN A 1 35 ? 30.880 16.705 21.275 1.00 23.06 ? 31 GLN A O 1 ATOM 271 C CB . GLN A 1 35 ? 31.791 14.882 18.799 1.00 23.82 ? 31 GLN A CB 1 ATOM 272 C CG . GLN A 1 35 ? 31.272 14.643 17.379 1.00 22.88 ? 31 GLN A CG 1 ATOM 273 C CD . GLN A 1 35 ? 29.920 15.364 17.149 1.00 22.61 ? 31 GLN A CD 1 ATOM 274 O OE1 . GLN A 1 35 ? 28.938 15.041 17.830 1.00 19.83 ? 31 GLN A OE1 1 ATOM 275 N NE2 . GLN A 1 35 ? 29.887 16.377 16.249 1.00 19.70 ? 31 GLN A NE2 1 ATOM 276 N N . MET A 1 36 ? 33.107 16.532 21.274 1.00 23.31 ? 32 MET A N 1 ATOM 277 C CA . MET A 1 36 ? 33.231 16.622 22.706 1.00 22.84 ? 32 MET A CA 1 ATOM 278 C C . MET A 1 36 ? 33.136 18.029 23.224 1.00 21.86 ? 32 MET A C 1 ATOM 279 O O . MET A 1 36 ? 33.252 18.257 24.432 1.00 22.57 ? 32 MET A O 1 ATOM 280 C CB . MET A 1 36 ? 34.598 16.065 23.112 1.00 22.53 ? 32 MET A CB 1 ATOM 281 C CG . MET A 1 36 ? 34.745 14.512 22.728 1.00 23.38 ? 32 MET A CG 1 ATOM 282 S SD . MET A 1 36 ? 36.475 13.864 23.025 1.00 24.99 ? 32 MET A SD 1 ATOM 283 C CE . MET A 1 36 ? 36.645 13.959 24.802 1.00 22.31 ? 32 MET A CE 1 ATOM 284 N N . THR A 1 37 ? 33.020 18.990 22.316 1.00 21.14 ? 33 THR A N 1 ATOM 285 C CA . THR A 1 37 ? 33.039 20.376 22.702 1.00 21.03 ? 33 THR A CA 1 ATOM 286 C C . THR A 1 37 ? 31.646 21.033 22.657 1.00 21.97 ? 33 THR A C 1 ATOM 287 O O . THR A 1 37 ? 30.991 21.052 21.580 1.00 20.65 ? 33 THR A O 1 ATOM 288 C CB . THR A 1 37 ? 33.991 21.160 21.692 1.00 23.18 ? 33 THR A CB 1 ATOM 289 O OG1 . THR A 1 37 ? 35.280 20.524 21.689 1.00 21.70 ? 33 THR A OG1 1 ATOM 290 C CG2 . THR A 1 37 ? 34.137 22.615 22.128 1.00 23.11 ? 33 THR A CG2 1 ATOM 291 N N . GLN A 1 38 ? 31.213 21.587 23.802 1.00 20.81 ? 34 GLN A N 1 ATOM 292 C CA . GLN A 1 38 ? 29.952 22.328 23.849 1.00 20.82 ? 34 GLN A CA 1 ATOM 293 C C . GLN A 1 38 ? 30.242 23.786 24.114 1.00 20.89 ? 34 GLN A C 1 ATOM 294 O O . GLN A 1 38 ? 31.025 24.092 25.037 1.00 21.47 ? 34 GLN A O 1 ATOM 295 C CB . GLN A 1 38 ? 29.056 21.790 25.020 1.00 20.86 ? 34 GLN A CB 1 ATOM 296 C CG . GLN A 1 38 ? 27.670 22.596 25.109 1.00 17.45 ? 34 GLN A CG 1 ATOM 297 C CD . GLN A 1 38 ? 26.840 22.074 26.280 1.00 20.98 ? 34 GLN A CD 1 ATOM 298 O OE1 . GLN A 1 38 ? 27.117 22.423 27.405 1.00 20.09 ? 34 GLN A OE1 1 ATOM 299 N NE2 . GLN A 1 38 ? 25.835 21.215 26.010 1.00 19.32 ? 34 GLN A NE2 1 ATOM 300 N N . ILE A 1 39 ? 29.615 24.701 23.343 1.00 22.11 ? 35 ILE A N 1 ATOM 301 C CA . ILE A 1 39 ? 29.938 26.123 23.489 1.00 22.27 ? 35 ILE A CA 1 ATOM 302 C C . ILE A 1 39 ? 28.671 26.945 23.714 1.00 21.62 ? 35 ILE A C 1 ATOM 303 O O . ILE A 1 39 ? 27.591 26.536 23.324 1.00 21.47 ? 35 ILE A O 1 ATOM 304 C CB . ILE A 1 39 ? 30.747 26.689 22.258 1.00 21.56 ? 35 ILE A CB 1 ATOM 305 C CG1 . ILE A 1 39 ? 29.865 26.769 20.978 1.00 23.29 ? 35 ILE A CG1 1 ATOM 306 C CG2 . ILE A 1 39 ? 32.031 25.827 22.044 1.00 20.47 ? 35 ILE A CG2 1 ATOM 307 C CD1 . ILE A 1 39 ? 30.608 27.457 19.734 1.00 19.96 ? 35 ILE A CD1 1 ATOM 308 N N . GLU A 1 40 ? 28.827 28.082 24.359 1.00 21.53 ? 36 GLU A N 1 ATOM 309 C CA . GLU A 1 40 ? 27.713 29.002 24.540 1.00 21.16 ? 36 GLU A CA 1 ATOM 310 C C . GLU A 1 40 ? 27.259 29.528 23.178 1.00 22.23 ? 36 GLU A C 1 ATOM 311 O O . GLU A 1 40 ? 28.105 29.881 22.312 1.00 21.61 ? 36 GLU A O 1 ATOM 312 C CB . GLU A 1 40 ? 28.194 30.191 25.399 1.00 22.36 ? 36 GLU A CB 1 ATOM 313 C CG . GLU A 1 40 ? 27.486 30.330 26.755 1.00 21.47 ? 36 GLU A CG 1 ATOM 314 C CD . GLU A 1 40 ? 26.017 30.867 26.662 1.00 24.05 ? 36 GLU A CD 1 ATOM 315 O OE1 . GLU A 1 40 ? 25.634 31.348 25.594 1.00 21.80 ? 36 GLU A OE1 1 ATOM 316 O OE2 . GLU A 1 40 ? 25.238 30.833 27.661 1.00 20.73 ? 36 GLU A OE2 1 ATOM 317 N N . ARG A 1 41 ? 25.935 29.660 22.985 1.00 21.75 ? 37 ARG A N 1 ATOM 318 C CA . ARG A 1 41 ? 25.448 30.402 21.793 1.00 21.31 ? 37 ARG A CA 1 ATOM 319 C C . ARG A 1 41 ? 26.113 31.775 21.726 1.00 23.34 ? 37 ARG A C 1 ATOM 320 O O . ARG A 1 41 ? 26.304 32.310 20.618 1.00 23.58 ? 37 ARG A O 1 ATOM 321 C CB . ARG A 1 41 ? 23.930 30.604 21.820 1.00 21.49 ? 37 ARG A CB 1 ATOM 322 C CG . ARG A 1 41 ? 23.378 31.248 23.153 1.00 18.89 ? 37 ARG A CG 1 ATOM 323 C CD . ARG A 1 41 ? 21.934 31.843 22.856 1.00 19.44 ? 37 ARG A CD 1 ATOM 324 N NE . ARG A 1 41 ? 22.000 33.088 22.033 1.00 21.27 ? 37 ARG A NE 1 ATOM 325 C CZ . ARG A 1 41 ? 22.270 34.309 22.517 1.00 21.72 ? 37 ARG A CZ 1 ATOM 326 N NH1 . ARG A 1 41 ? 22.396 34.487 23.841 1.00 21.60 ? 37 ARG A NH1 1 ATOM 327 N NH2 . ARG A 1 41 ? 22.234 35.393 21.685 1.00 20.73 ? 37 ARG A NH2 1 ATOM 328 N N . LEU A 1 42 ? 26.436 32.381 22.881 1.00 22.89 ? 38 LEU A N 1 ATOM 329 C CA . LEU A 1 42 ? 27.087 33.735 22.861 1.00 23.32 ? 38 LEU A CA 1 ATOM 330 C C . LEU A 1 42 ? 28.420 33.787 22.094 1.00 24.61 ? 38 LEU A C 1 ATOM 331 O O . LEU A 1 42 ? 28.809 34.861 21.612 1.00 24.23 ? 38 LEU A O 1 ATOM 332 C CB . LEU A 1 42 ? 27.326 34.314 24.271 1.00 23.29 ? 38 LEU A CB 1 ATOM 333 C CG . LEU A 1 42 ? 26.038 34.728 25.003 1.00 26.59 ? 38 LEU A CG 1 ATOM 334 C CD1 . LEU A 1 42 ? 26.274 34.870 26.531 1.00 27.45 ? 38 LEU A CD1 1 ATOM 335 C CD2 . LEU A 1 42 ? 25.388 36.010 24.380 1.00 29.15 ? 38 LEU A CD2 1 ATOM 336 N N . VAL A 1 43 ? 29.110 32.657 21.946 1.00 23.30 ? 39 VAL A N 1 ATOM 337 C CA . VAL A 1 43 ? 30.381 32.675 21.167 1.00 24.74 ? 39 VAL A CA 1 ATOM 338 C C . VAL A 1 43 ? 30.312 31.876 19.861 1.00 25.62 ? 39 VAL A C 1 ATOM 339 O O . VAL A 1 43 ? 31.344 31.683 19.199 1.00 26.34 ? 39 VAL A O 1 ATOM 340 C CB . VAL A 1 43 ? 31.581 32.125 22.005 1.00 23.52 ? 39 VAL A CB 1 ATOM 341 C CG1 . VAL A 1 43 ? 31.801 32.934 23.298 1.00 25.61 ? 39 VAL A CG1 1 ATOM 342 C CG2 . VAL A 1 43 ? 31.363 30.626 22.353 1.00 22.93 ? 39 VAL A CG2 1 ATOM 343 N N . ALA A 1 44 ? 29.116 31.383 19.513 1.00 23.48 ? 40 ALA A N 1 ATOM 344 C CA . ALA A 1 44 ? 28.917 30.609 18.321 1.00 24.03 ? 40 ALA A CA 1 ATOM 345 C C . ALA A 1 44 ? 28.643 31.515 17.117 1.00 25.97 ? 40 ALA A C 1 ATOM 346 O O . ALA A 1 44 ? 27.979 32.559 17.251 1.00 25.62 ? 40 ALA A O 1 ATOM 347 C CB . ALA A 1 44 ? 27.769 29.638 18.492 1.00 22.78 ? 40 ALA A CB 1 ATOM 348 N N . THR A 1 45 ? 29.208 31.122 15.962 1.00 26.07 ? 41 THR A N 1 ATOM 349 C CA . THR A 1 45 ? 28.882 31.747 14.658 1.00 26.34 ? 41 THR A CA 1 ATOM 350 C C . THR A 1 45 ? 28.903 30.573 13.683 1.00 25.10 ? 41 THR A C 1 ATOM 351 O O . THR A 1 45 ? 29.432 29.506 14.022 1.00 24.51 ? 41 THR A O 1 ATOM 352 C CB . THR A 1 45 ? 29.936 32.773 14.218 1.00 26.84 ? 41 THR A CB 1 ATOM 353 O OG1 . THR A 1 45 ? 31.156 32.083 13.936 1.00 27.20 ? 41 THR A OG1 1 ATOM 354 C CG2 . THR A 1 45 ? 30.200 33.843 15.308 1.00 29.70 ? 41 THR A CG2 1 ATOM 355 N N . PRO A 1 46 ? 28.339 30.731 12.469 1.00 26.94 ? 42 PRO A N 1 ATOM 356 C CA . PRO A 1 46 ? 28.386 29.635 11.499 1.00 26.41 ? 42 PRO A CA 1 ATOM 357 C C . PRO A 1 46 ? 29.819 29.166 11.192 1.00 27.10 ? 42 PRO A C 1 ATOM 358 O O . PRO A 1 46 ? 30.068 27.960 11.197 1.00 25.88 ? 42 PRO A O 1 ATOM 359 C CB . PRO A 1 46 ? 27.705 30.267 10.247 1.00 28.57 ? 42 PRO A CB 1 ATOM 360 C CG . PRO A 1 46 ? 26.642 31.140 10.831 1.00 28.10 ? 42 PRO A CG 1 ATOM 361 C CD . PRO A 1 46 ? 27.492 31.841 11.958 1.00 27.28 ? 42 PRO A CD 1 ATOM 362 N N . ASP A 1 47 ? 30.792 30.078 11.031 1.00 27.16 ? 43 ASP A N 1 ATOM 363 C CA . ASP A 1 47 ? 32.166 29.629 10.761 1.00 28.76 ? 43 ASP A CA 1 ATOM 364 C C . ASP A 1 47 ? 32.781 28.866 11.937 1.00 27.05 ? 43 ASP A C 1 ATOM 365 O O . ASP A 1 47 ? 33.517 27.895 11.743 1.00 27.23 ? 43 ASP A O 1 ATOM 366 C CB . ASP A 1 47 ? 33.100 30.808 10.366 1.00 29.91 ? 43 ASP A CB 1 ATOM 367 C CG . ASP A 1 47 ? 32.792 31.346 8.976 1.00 36.30 ? 43 ASP A CG 1 ATOM 368 O OD1 . ASP A 1 47 ? 32.413 30.542 8.090 1.00 41.21 ? 43 ASP A OD1 1 ATOM 369 O OD2 . ASP A 1 47 ? 32.897 32.576 8.786 1.00 43.99 ? 43 ASP A OD2 1 ATOM 370 N N . VAL A 1 48 ? 32.495 29.319 13.161 1.00 26.59 ? 44 VAL A N 1 ATOM 371 C CA . VAL A 1 48 ? 33.087 28.697 14.351 1.00 24.99 ? 44 VAL A CA 1 ATOM 372 C C . VAL A 1 48 ? 32.569 27.281 14.466 1.00 25.25 ? 44 VAL A C 1 ATOM 373 O O . VAL A 1 48 ? 33.308 26.353 14.752 1.00 23.61 ? 44 VAL A O 1 ATOM 374 C CB . VAL A 1 48 ? 32.765 29.548 15.631 1.00 25.32 ? 44 VAL A CB 1 ATOM 375 C CG1 . VAL A 1 48 ? 32.871 28.709 16.903 1.00 26.08 ? 44 VAL A CG1 1 ATOM 376 C CG2 . VAL A 1 48 ? 33.695 30.821 15.673 1.00 26.82 ? 44 VAL A CG2 1 ATOM 377 N N . LEU A 1 49 ? 31.257 27.115 14.259 1.00 23.87 ? 45 LEU A N 1 ATOM 378 C CA . LEU A 1 49 ? 30.649 25.787 14.368 1.00 23.06 ? 45 LEU A CA 1 ATOM 379 C C . LEU A 1 49 ? 31.177 24.815 13.307 1.00 24.56 ? 45 LEU A C 1 ATOM 380 O O . LEU A 1 49 ? 31.346 23.626 13.606 1.00 23.60 ? 45 LEU A O 1 ATOM 381 C CB . LEU A 1 49 ? 29.113 25.919 14.263 1.00 22.81 ? 45 LEU A CB 1 ATOM 382 C CG . LEU A 1 49 ? 28.481 26.665 15.451 1.00 24.42 ? 45 LEU A CG 1 ATOM 383 C CD1 . LEU A 1 49 ? 26.980 26.990 15.090 1.00 21.56 ? 45 LEU A CD1 1 ATOM 384 C CD2 . LEU A 1 49 ? 28.644 25.898 16.780 1.00 23.97 ? 45 LEU A CD2 1 ATOM 385 N N . ARG A 1 50 ? 31.350 25.299 12.055 1.00 24.46 ? 46 ARG A N 1 ATOM 386 C CA . ARG A 1 50 ? 31.886 24.448 10.940 1.00 26.64 ? 46 ARG A CA 1 ATOM 387 C C . ARG A 1 50 ? 33.355 24.161 11.132 1.00 26.76 ? 46 ARG A C 1 ATOM 388 O O . ARG A 1 50 ? 33.789 22.990 11.151 1.00 26.84 ? 46 ARG A O 1 ATOM 389 C CB . ARG A 1 50 ? 31.827 25.211 9.612 1.00 28.04 ? 46 ARG A CB 1 ATOM 390 C CG A ARG A 1 50 ? 30.544 25.357 8.958 0.60 25.39 ? 46 ARG A CG 1 ATOM 391 C CG B ARG A 1 50 ? 31.902 24.377 8.355 0.40 28.46 ? 46 ARG A CG 1 ATOM 392 C CD A ARG A 1 50 ? 30.794 26.097 7.628 0.60 27.28 ? 46 ARG A CD 1 ATOM 393 C CD B ARG A 1 50 ? 31.583 25.195 7.101 0.40 31.51 ? 46 ARG A CD 1 ATOM 394 N NE A ARG A 1 50 ? 29.478 26.538 7.205 0.60 37.55 ? 46 ARG A NE 1 ATOM 395 N NE B ARG A 1 50 ? 31.460 24.289 5.961 0.40 36.37 ? 46 ARG A NE 1 ATOM 396 C CZ A ARG A 1 50 ? 29.021 27.777 7.234 0.60 35.15 ? 46 ARG A CZ 1 ATOM 397 C CZ B ARG A 1 50 ? 32.453 23.976 5.134 0.40 40.85 ? 46 ARG A CZ 1 ATOM 398 N NH1 A ARG A 1 50 ? 27.780 27.969 6.839 0.60 39.97 ? 46 ARG A NH1 1 ATOM 399 N NH1 B ARG A 1 50 ? 32.231 23.129 4.131 0.40 41.69 ? 46 ARG A NH1 1 ATOM 400 N NH2 A ARG A 1 50 ? 29.785 28.808 7.607 0.60 33.45 ? 46 ARG A NH2 1 ATOM 401 N NH2 B ARG A 1 50 ? 33.672 24.504 5.301 0.40 41.69 ? 46 ARG A NH2 1 ATOM 402 N N . ASP A 1 51 ? 34.127 25.228 11.321 1.00 27.34 ? 47 ASP A N 1 ATOM 403 C CA . ASP A 1 51 ? 35.619 25.125 11.373 1.00 26.79 ? 47 ASP A CA 1 ATOM 404 C C . ASP A 1 51 ? 36.102 24.274 12.502 1.00 25.99 ? 47 ASP A C 1 ATOM 405 O O . ASP A 1 51 ? 37.143 23.582 12.400 1.00 26.11 ? 47 ASP A O 1 ATOM 406 C CB . ASP A 1 51 ? 36.270 26.521 11.483 1.00 28.01 ? 47 ASP A CB 1 ATOM 407 C CG . ASP A 1 51 ? 36.036 27.380 10.248 1.00 30.20 ? 47 ASP A CG 1 ATOM 408 O OD1 . ASP A 1 51 ? 36.259 28.599 10.316 1.00 31.02 ? 47 ASP A OD1 1 ATOM 409 O OD2 . ASP A 1 51 ? 35.587 26.836 9.238 1.00 32.19 ? 47 ASP A OD2 1 ATOM 410 N N . ASN A 1 52 ? 35.393 24.319 13.623 1.00 24.69 ? 48 ASN A N 1 ATOM 411 C CA . ASN A 1 52 ? 35.798 23.473 14.772 1.00 24.71 ? 48 ASN A CA 1 ATOM 412 C C . ASN A 1 52 ? 34.930 22.205 15.003 1.00 23.91 ? 48 ASN A C 1 ATOM 413 O O . ASN A 1 52 ? 35.117 21.506 16.003 1.00 22.61 ? 48 ASN A O 1 ATOM 414 C CB . ASN A 1 52 ? 35.748 24.315 16.063 1.00 25.81 ? 48 ASN A CB 1 ATOM 415 C CG . ASN A 1 52 ? 36.649 25.546 15.968 1.00 29.78 ? 48 ASN A CG 1 ATOM 416 O OD1 . ASN A 1 52 ? 37.851 25.422 16.141 1.00 25.97 ? 48 ASN A OD1 1 ATOM 417 N ND2 . ASN A 1 52 ? 36.074 26.710 15.659 1.00 24.65 ? 48 ASN A ND2 1 ATOM 418 N N . PHE A 1 53 ? 34.018 21.915 14.072 1.00 22.76 ? 49 PHE A N 1 ATOM 419 C CA . PHE A 1 53 ? 33.256 20.656 14.065 1.00 21.58 ? 49 PHE A CA 1 ATOM 420 C C . PHE A 1 53 ? 32.507 20.474 15.403 1.00 21.91 ? 49 PHE A C 1 ATOM 421 O O . PHE A 1 53 ? 32.480 19.391 15.959 1.00 20.64 ? 49 PHE A O 1 ATOM 422 C CB . PHE A 1 53 ? 34.208 19.490 13.844 1.00 22.26 ? 49 PHE A CB 1 ATOM 423 C CG . PHE A 1 53 ? 35.001 19.596 12.548 1.00 21.90 ? 49 PHE A CG 1 ATOM 424 C CD1 . PHE A 1 53 ? 34.384 19.393 11.302 1.00 21.63 ? 49 PHE A CD1 1 ATOM 425 C CD2 . PHE A 1 53 ? 36.369 19.889 12.586 1.00 22.61 ? 49 PHE A CD2 1 ATOM 426 C CE1 . PHE A 1 53 ? 35.121 19.433 10.077 1.00 26.52 ? 49 PHE A CE1 1 ATOM 427 C CE2 . PHE A 1 53 ? 37.114 19.974 11.363 1.00 25.41 ? 49 PHE A CE2 1 ATOM 428 C CZ . PHE A 1 53 ? 36.485 19.740 10.113 1.00 23.31 ? 49 PHE A CZ 1 ATOM 429 N N . ILE A 1 54 ? 31.968 21.581 15.910 1.00 20.78 ? 50 ILE A N 1 ATOM 430 C CA . ILE A 1 54 ? 31.378 21.658 17.260 1.00 20.80 ? 50 ILE A CA 1 ATOM 431 C C . ILE A 1 54 ? 30.210 20.677 17.435 1.00 21.33 ? 50 ILE A C 1 ATOM 432 O O . ILE A 1 54 ? 29.330 20.605 16.545 1.00 23.51 ? 50 ILE A O 1 ATOM 433 C CB . ILE A 1 54 ? 30.871 23.120 17.529 1.00 20.05 ? 50 ILE A CB 1 ATOM 434 C CG1 . ILE A 1 54 ? 32.098 24.082 17.561 1.00 19.06 ? 50 ILE A CG1 1 ATOM 435 C CG2 . ILE A 1 54 ? 30.043 23.229 18.849 1.00 20.09 ? 50 ILE A CG2 1 ATOM 436 C CD1 . ILE A 1 54 ? 33.165 23.680 18.665 1.00 19.90 ? 50 ILE A CD1 1 ATOM 437 N N . GLY A 1 55 ? 30.177 19.999 18.584 1.00 20.05 ? 51 GLY A N 1 ATOM 438 C CA . GLY A 1 55 ? 29.217 18.919 18.825 1.00 20.58 ? 51 GLY A CA 1 ATOM 439 C C . GLY A 1 55 ? 27.938 19.433 19.494 1.00 21.25 ? 51 GLY A C 1 ATOM 440 O O . GLY A 1 55 ? 26.895 18.780 19.413 1.00 20.47 ? 51 GLY A O 1 ATOM 441 N N . SER A 1 56 ? 28.037 20.546 20.228 1.00 20.62 ? 52 SER A N 1 ATOM 442 C CA . SER A 1 56 ? 26.891 20.976 21.045 1.00 20.26 ? 52 SER A CA 1 ATOM 443 C C . SER A 1 56 ? 26.927 22.449 21.359 1.00 20.45 ? 52 SER A C 1 ATOM 444 O O . SER A 1 56 ? 28.012 23.073 21.424 1.00 20.08 ? 52 SER A O 1 ATOM 445 C CB . SER A 1 56 ? 26.823 20.131 22.348 1.00 20.29 ? 52 SER A CB 1 ATOM 446 O OG . SER A 1 56 ? 25.725 20.498 23.178 1.00 21.20 ? 52 SER A OG 1 ATOM 447 N N . LEU A 1 57 ? 25.748 23.038 21.569 1.00 19.57 ? 53 LEU A N 1 ATOM 448 C CA . LEU A 1 57 ? 25.662 24.390 22.073 1.00 19.72 ? 53 LEU A CA 1 ATOM 449 C C . LEU A 1 57 ? 24.771 24.382 23.320 1.00 20.55 ? 53 LEU A C 1 ATOM 450 O O . LEU A 1 57 ? 23.983 23.466 23.482 1.00 20.19 ? 53 LEU A O 1 ATOM 451 C CB . LEU A 1 57 ? 24.944 25.316 21.084 1.00 20.71 ? 53 LEU A CB 1 ATOM 452 C CG . LEU A 1 57 ? 25.896 25.711 19.896 1.00 26.84 ? 53 LEU A CG 1 ATOM 453 C CD1 . LEU A 1 57 ? 25.696 24.708 18.759 1.00 26.07 ? 53 LEU A CD1 1 ATOM 454 C CD2 . LEU A 1 57 ? 25.513 27.063 19.418 1.00 29.78 ? 53 LEU A CD2 1 ATOM 455 N N . LEU A 1 58 ? 24.864 25.443 24.140 1.00 19.08 ? 54 LEU A N 1 ATOM 456 C CA . LEU A 1 58 ? 23.889 25.639 25.197 1.00 19.30 ? 54 LEU A CA 1 ATOM 457 C C . LEU A 1 58 ? 23.562 27.112 25.335 1.00 19.80 ? 54 LEU A C 1 ATOM 458 O O . LEU A 1 58 ? 24.357 27.993 24.890 1.00 20.47 ? 54 LEU A O 1 ATOM 459 C CB . LEU A 1 58 ? 24.428 25.115 26.548 1.00 18.48 ? 54 LEU A CB 1 ATOM 460 C CG . LEU A 1 58 ? 25.332 26.070 27.344 1.00 19.95 ? 54 LEU A CG 1 ATOM 461 C CD1 . LEU A 1 58 ? 25.155 25.771 28.860 1.00 19.98 ? 54 LEU A CD1 1 ATOM 462 C CD2 . LEU A 1 58 ? 26.868 26.076 26.924 1.00 19.86 ? 54 LEU A CD2 1 ATOM 463 N N . SER A 1 59 ? 22.425 27.368 25.971 1.00 18.22 ? 55 SER A N 1 ATOM 464 C CA . SER A 1 59 ? 22.128 28.661 26.617 1.00 19.80 ? 55 SER A CA 1 ATOM 465 C C . SER A 1 59 ? 22.359 28.446 28.099 1.00 20.84 ? 55 SER A C 1 ATOM 466 O O . SER A 1 59 ? 21.614 27.636 28.752 1.00 21.36 ? 55 SER A O 1 ATOM 467 C CB . SER A 1 59 ? 20.649 29.068 26.409 1.00 21.45 ? 55 SER A CB 1 ATOM 468 O OG . SER A 1 59 ? 20.467 29.628 25.091 1.00 22.03 ? 55 SER A OG 1 ATOM 469 N N . GLY A 1 60 ? 23.344 29.163 28.676 1.00 20.52 ? 56 GLY A N 1 ATOM 470 C CA . GLY A 1 60 ? 23.438 29.221 30.169 1.00 21.39 ? 56 GLY A CA 1 ATOM 471 C C . GLY A 1 60 ? 22.215 30.070 30.664 1.00 22.65 ? 56 GLY A C 1 ATOM 472 O O . GLY A 1 60 ? 21.408 30.538 29.855 1.00 21.76 ? 56 GLY A O 1 ATOM 473 N N . GLY A 1 61 ? 22.040 30.226 31.977 1.00 22.78 ? 57 GLY A N 1 ATOM 474 C CA . GLY A 1 61 ? 20.905 31.039 32.528 1.00 21.52 ? 57 GLY A CA 1 ATOM 475 C C . GLY A 1 61 ? 20.868 32.429 31.880 1.00 24.62 ? 57 GLY A C 1 ATOM 476 O O . GLY A 1 61 ? 21.889 33.122 31.787 1.00 24.11 ? 57 GLY A O 1 ATOM 477 N N . GLY A 1 62 ? 19.718 32.817 31.352 1.00 22.35 ? 58 GLY A N 1 ATOM 478 C CA . GLY A 1 62 ? 19.591 34.122 30.734 1.00 23.51 ? 58 GLY A CA 1 ATOM 479 C C . GLY A 1 62 ? 20.258 34.334 29.395 1.00 23.11 ? 58 GLY A C 1 ATOM 480 O O . GLY A 1 62 ? 20.293 35.475 28.904 1.00 23.40 ? 58 GLY A O 1 ATOM 481 N N . SER A 1 63 ? 20.767 33.268 28.777 1.00 22.08 ? 59 SER A N 1 ATOM 482 C CA . SER A 1 63 ? 21.395 33.453 27.434 1.00 21.85 ? 59 SER A CA 1 ATOM 483 C C . SER A 1 63 ? 20.312 33.188 26.383 1.00 21.49 ? 59 SER A C 1 ATOM 484 O O . SER A 1 63 ? 19.934 32.042 26.146 1.00 22.73 ? 59 SER A O 1 ATOM 485 C CB . SER A 1 63 ? 22.585 32.510 27.272 1.00 22.18 ? 59 SER A CB 1 ATOM 486 O OG . SER A 1 63 ? 23.147 32.619 25.960 1.00 22.97 ? 59 SER A OG 1 ATOM 487 N N . VAL A 1 64 ? 19.809 34.267 25.813 1.00 21.47 ? 60 VAL A N 1 ATOM 488 C CA . VAL A 1 64 ? 18.579 34.296 25.003 1.00 21.30 ? 60 VAL A CA 1 ATOM 489 C C . VAL A 1 64 ? 18.833 35.175 23.761 1.00 22.46 ? 60 VAL A C 1 ATOM 490 O O . VAL A 1 64 ? 19.638 36.135 23.840 1.00 22.81 ? 60 VAL A O 1 ATOM 491 C CB . VAL A 1 64 ? 17.367 34.816 25.833 1.00 20.50 ? 60 VAL A CB 1 ATOM 492 C CG1 . VAL A 1 64 ? 17.122 33.943 27.103 1.00 18.99 ? 60 VAL A CG1 1 ATOM 493 C CG2 . VAL A 1 64 ? 17.438 36.364 26.228 1.00 19.68 ? 60 VAL A CG2 1 ATOM 494 N N . PRO A 1 65 ? 18.115 34.904 22.643 1.00 23.28 ? 61 PRO A N 1 ATOM 495 C CA . PRO A 1 65 ? 18.401 35.670 21.437 1.00 22.94 ? 61 PRO A CA 1 ATOM 496 C C . PRO A 1 65 ? 18.008 37.158 21.604 1.00 24.79 ? 61 PRO A C 1 ATOM 497 O O . PRO A 1 65 ? 18.623 38.061 20.994 1.00 23.69 ? 61 PRO A O 1 ATOM 498 C CB . PRO A 1 65 ? 17.515 35.015 20.368 1.00 23.99 ? 61 PRO A CB 1 ATOM 499 C CG . PRO A 1 65 ? 16.484 34.187 21.077 1.00 23.76 ? 61 PRO A CG 1 ATOM 500 C CD . PRO A 1 65 ? 17.149 33.808 22.406 1.00 22.48 ? 61 PRO A CD 1 ATOM 501 N N . ARG A 1 66 ? 16.945 37.395 22.361 1.00 25.04 ? 62 ARG A N 1 ATOM 502 C CA . ARG A 1 66 ? 16.667 38.710 22.907 1.00 27.08 ? 62 ARG A CA 1 ATOM 503 C C . ARG A 1 66 ? 15.628 38.621 23.983 1.00 28.34 ? 62 ARG A C 1 ATOM 504 O O . ARG A 1 66 ? 14.934 37.597 24.116 1.00 23.99 ? 62 ARG A O 1 ATOM 505 C CB . ARG A 1 66 ? 16.212 39.663 21.852 1.00 29.80 ? 62 ARG A CB 1 ATOM 506 C CG . ARG A 1 66 ? 15.003 39.266 21.149 1.00 32.85 ? 62 ARG A CG 1 ATOM 507 C CD . ARG A 1 66 ? 14.540 40.411 20.195 1.00 39.20 ? 62 ARG A CD 1 ATOM 508 N NE . ARG A 1 66 ? 13.207 40.062 19.737 1.00 39.74 ? 62 ARG A NE 1 ATOM 509 C CZ . ARG A 1 66 ? 12.259 40.939 19.472 1.00 42.54 ? 62 ARG A CZ 1 ATOM 510 N NH1 . ARG A 1 66 ? 12.513 42.256 19.535 1.00 43.57 ? 62 ARG A NH1 1 ATOM 511 N NH2 . ARG A 1 66 ? 11.086 40.489 19.104 1.00 38.09 ? 62 ARG A NH2 1 ATOM 512 N N . LYS A 1 67 ? 15.480 39.698 24.763 1.00 29.03 ? 63 LYS A N 1 ATOM 513 C CA . LYS A 1 67 ? 14.433 39.654 25.796 1.00 29.86 ? 63 LYS A CA 1 ATOM 514 C C . LYS A 1 67 ? 13.098 39.565 25.089 1.00 26.47 ? 63 LYS A C 1 ATOM 515 O O . LYS A 1 67 ? 12.915 40.161 24.050 1.00 25.80 ? 63 LYS A O 1 ATOM 516 C CB . LYS A 1 67 ? 14.492 40.895 26.732 1.00 32.27 ? 63 LYS A CB 1 ATOM 517 C CG . LYS A 1 67 ? 15.797 40.876 27.646 1.00 38.12 ? 63 LYS A CG 1 ATOM 518 C CD . LYS A 1 67 ? 15.951 39.582 28.445 1.00 39.64 ? 63 LYS A CD 1 ATOM 519 C CE . LYS A 1 67 ? 15.039 39.592 29.649 1.00 44.21 ? 63 LYS A CE 1 ATOM 520 N NZ . LYS A 1 67 ? 15.583 40.407 30.753 1.00 48.87 ? 63 LYS A NZ 1 ATOM 521 N N . GLY A 1 68 ? 12.186 38.770 25.617 1.00 26.21 ? 64 GLY A N 1 ATOM 522 C CA . GLY A 1 68 ? 10.809 38.717 25.042 1.00 24.77 ? 64 GLY A CA 1 ATOM 523 C C . GLY A 1 68 ? 10.759 37.936 23.736 1.00 24.10 ? 64 GLY A C 1 ATOM 524 O O . GLY A 1 68 ? 9.737 37.967 23.058 1.00 24.74 ? 64 GLY A O 1 ATOM 525 N N . ALA A 1 69 ? 11.819 37.208 23.378 1.00 23.05 ? 65 ALA A N 1 ATOM 526 C CA . ALA A 1 69 ? 11.833 36.463 22.062 1.00 22.86 ? 65 ALA A CA 1 ATOM 527 C C . ALA A 1 69 ? 10.664 35.473 21.978 1.00 22.53 ? 65 ALA A C 1 ATOM 528 O O . ALA A 1 69 ? 10.315 34.817 22.991 1.00 22.58 ? 65 ALA A O 1 ATOM 529 C CB . ALA A 1 69 ? 13.122 35.668 21.927 1.00 21.84 ? 65 ALA A CB 1 ATOM 530 N N . THR A 1 70 ? 10.040 35.379 20.820 1.00 23.09 ? 66 THR A N 1 ATOM 531 C CA . THR A 1 70 ? 8.925 34.411 20.610 1.00 23.01 ? 66 THR A CA 1 ATOM 532 C C . THR A 1 70 ? 9.491 33.005 20.445 1.00 23.23 ? 66 THR A C 1 ATOM 533 O O . THR A 1 70 ? 10.731 32.816 20.257 1.00 22.13 ? 66 THR A O 1 ATOM 534 C CB . THR A 1 70 ? 8.183 34.754 19.337 1.00 23.65 ? 66 THR A CB 1 ATOM 535 O OG1 . THR A 1 70 ? 9.095 34.601 18.243 1.00 23.56 ? 66 THR A OG1 1 ATOM 536 C CG2 . THR A 1 70 ? 7.617 36.282 19.382 1.00 24.58 ? 66 THR A CG2 1 ATOM 537 N N . ALA A 1 71 ? 8.630 31.989 20.504 1.00 21.73 ? 67 ALA A N 1 ATOM 538 C CA . ALA A 1 71 ? 9.103 30.621 20.242 1.00 21.62 ? 67 ALA A CA 1 ATOM 539 C C . ALA A 1 71 ? 9.767 30.523 18.854 1.00 21.56 ? 67 ALA A C 1 ATOM 540 O O . ALA A 1 71 ? 10.782 29.825 18.636 1.00 21.55 ? 67 ALA A O 1 ATOM 541 C CB . ALA A 1 71 ? 7.895 29.642 20.348 1.00 22.19 ? 67 ALA A CB 1 ATOM 542 N N . LYS A 1 72 ? 9.191 31.204 17.883 1.00 22.10 ? 68 LYS A N 1 ATOM 543 C CA . LYS A 1 72 ? 9.755 31.152 16.540 1.00 24.41 ? 68 LYS A CA 1 ATOM 544 C C . LYS A 1 72 ? 11.166 31.759 16.482 1.00 23.49 ? 68 LYS A C 1 ATOM 545 O O . LYS A 1 72 ? 12.013 31.260 15.750 1.00 24.14 ? 68 LYS A O 1 ATOM 546 C CB . LYS A 1 72 ? 8.837 31.888 15.529 1.00 25.48 ? 68 LYS A CB 1 ATOM 547 C CG . LYS A 1 72 ? 9.445 31.893 14.119 1.00 30.52 ? 68 LYS A CG 1 ATOM 548 C CD . LYS A 1 72 ? 8.748 32.937 13.195 1.00 39.80 ? 68 LYS A CD 1 ATOM 549 C CE . LYS A 1 72 ? 9.167 32.798 11.711 1.00 42.40 ? 68 LYS A CE 1 ATOM 550 N NZ . LYS A 1 72 ? 10.628 32.720 11.319 1.00 42.36 ? 68 LYS A NZ 1 ATOM 551 N N . GLU A 1 73 ? 11.399 32.871 17.192 1.00 22.23 ? 69 GLU A N 1 ATOM 552 C CA . GLU A 1 73 ? 12.760 33.415 17.248 1.00 21.99 ? 69 GLU A CA 1 ATOM 553 C C . GLU A 1 73 ? 13.750 32.377 17.772 1.00 21.50 ? 69 GLU A C 1 ATOM 554 O O . GLU A 1 73 ? 14.877 32.250 17.294 1.00 20.23 ? 69 GLU A O 1 ATOM 555 C CB . GLU A 1 73 ? 12.871 34.683 18.132 1.00 21.25 ? 69 GLU A CB 1 ATOM 556 C CG . GLU A 1 73 ? 12.110 35.898 17.480 1.00 22.62 ? 69 GLU A CG 1 ATOM 557 C CD . GLU A 1 73 ? 12.204 37.102 18.402 1.00 25.79 ? 69 GLU A CD 1 ATOM 558 O OE1 . GLU A 1 73 ? 11.154 37.529 18.894 1.00 25.37 ? 69 GLU A OE1 1 ATOM 559 O OE2 . GLU A 1 73 ? 13.340 37.565 18.696 1.00 28.22 ? 69 GLU A OE2 1 ATOM 560 N N . TRP A 1 74 ? 13.361 31.692 18.823 1.00 20.23 ? 70 TRP A N 1 ATOM 561 C CA . TRP A 1 74 ? 14.275 30.657 19.345 1.00 20.30 ? 70 TRP A CA 1 ATOM 562 C C . TRP A 1 74 ? 14.473 29.564 18.284 1.00 19.79 ? 70 TRP A C 1 ATOM 563 O O . TRP A 1 74 ? 15.613 29.134 18.034 1.00 20.08 ? 70 TRP A O 1 ATOM 564 C CB . TRP A 1 74 ? 13.684 30.051 20.648 1.00 19.88 ? 70 TRP A CB 1 ATOM 565 C CG . TRP A 1 74 ? 13.876 30.856 21.884 1.00 18.81 ? 70 TRP A CG 1 ATOM 566 C CD1 . TRP A 1 74 ? 13.002 31.769 22.432 1.00 18.39 ? 70 TRP A CD1 1 ATOM 567 C CD2 . TRP A 1 74 ? 14.955 30.725 22.802 1.00 18.96 ? 70 TRP A CD2 1 ATOM 568 N NE1 . TRP A 1 74 ? 13.528 32.261 23.624 1.00 18.66 ? 70 TRP A NE1 1 ATOM 569 C CE2 . TRP A 1 74 ? 14.714 31.614 23.872 1.00 19.07 ? 70 TRP A CE2 1 ATOM 570 C CE3 . TRP A 1 74 ? 16.103 29.903 22.834 1.00 21.20 ? 70 TRP A CE3 1 ATOM 571 C CZ2 . TRP A 1 74 ? 15.575 31.725 24.948 1.00 19.11 ? 70 TRP A CZ2 1 ATOM 572 C CZ3 . TRP A 1 74 ? 16.993 30.023 23.888 1.00 20.85 ? 70 TRP A CZ3 1 ATOM 573 C CH2 . TRP A 1 74 ? 16.717 30.926 24.947 1.00 19.91 ? 70 TRP A CH2 1 ATOM 574 N N . GLN A 1 75 ? 13.405 29.110 17.613 1.00 19.95 ? 71 GLN A N 1 ATOM 575 C CA . GLN A 1 75 ? 13.583 28.044 16.617 1.00 21.27 ? 71 GLN A CA 1 ATOM 576 C C . GLN A 1 75 ? 14.554 28.486 15.501 1.00 22.28 ? 71 GLN A C 1 ATOM 577 O O . GLN A 1 75 ? 15.389 27.700 15.018 1.00 22.35 ? 71 GLN A O 1 ATOM 578 C CB . GLN A 1 75 ? 12.236 27.639 15.950 1.00 21.27 ? 71 GLN A CB 1 ATOM 579 C CG . GLN A 1 75 ? 11.264 26.941 16.948 1.00 23.06 ? 71 GLN A CG 1 ATOM 580 C CD . GLN A 1 75 ? 10.165 26.113 16.230 1.00 23.14 ? 71 GLN A CD 1 ATOM 581 O OE1 . GLN A 1 75 ? 9.323 25.488 16.891 1.00 28.19 ? 71 GLN A OE1 1 ATOM 582 N NE2 . GLN A 1 75 ? 10.235 26.043 14.912 1.00 19.62 ? 71 GLN A NE2 1 ATOM 583 N N . ASP A 1 76 ? 14.396 29.732 15.046 1.00 22.22 ? 72 ASP A N 1 ATOM 584 C CA . ASP A 1 76 ? 15.212 30.239 13.941 1.00 23.42 ? 72 ASP A CA 1 ATOM 585 C C . ASP A 1 76 ? 16.689 30.348 14.413 1.00 22.71 ? 72 ASP A C 1 ATOM 586 O O . ASP A 1 76 ? 17.605 30.100 13.653 1.00 22.36 ? 72 ASP A O 1 ATOM 587 C CB . ASP A 1 76 ? 14.751 31.657 13.567 1.00 23.11 ? 72 ASP A CB 1 ATOM 588 C CG . ASP A 1 76 ? 13.395 31.654 12.827 1.00 27.07 ? 72 ASP A CG 1 ATOM 589 O OD1 . ASP A 1 76 ? 12.958 30.585 12.367 1.00 26.49 ? 72 ASP A OD1 1 ATOM 590 O OD2 . ASP A 1 76 ? 12.827 32.717 12.654 1.00 28.08 ? 72 ASP A OD2 1 ATOM 591 N N . MET A 1 77 ? 16.903 30.760 15.645 1.00 22.26 ? 73 MET A N 1 ATOM 592 C CA . MET A 1 77 ? 18.291 30.788 16.175 1.00 22.48 ? 73 MET A CA 1 ATOM 593 C C . MET A 1 77 ? 18.923 29.385 16.187 1.00 21.50 ? 73 MET A C 1 ATOM 594 O O . MET A 1 77 ? 20.043 29.170 15.670 1.00 21.55 ? 73 MET A O 1 ATOM 595 C CB . MET A 1 77 ? 18.309 31.371 17.612 1.00 23.22 ? 73 MET A CB 1 ATOM 596 C CG . MET A 1 77 ? 19.707 31.334 18.213 1.00 22.39 ? 73 MET A CG 1 ATOM 597 S SD . MET A 1 77 ? 19.705 31.715 19.991 1.00 24.76 ? 73 MET A SD 1 ATOM 598 C CE . MET A 1 77 ? 18.974 30.193 20.666 1.00 22.99 ? 73 MET A CE 1 ATOM 599 N N . VAL A 1 78 ? 18.196 28.419 16.749 1.00 20.05 ? 74 VAL A N 1 ATOM 600 C CA . VAL A 1 78 ? 18.714 27.089 16.841 1.00 20.15 ? 74 VAL A CA 1 ATOM 601 C C . VAL A 1 78 ? 18.937 26.480 15.447 1.00 20.69 ? 74 VAL A C 1 ATOM 602 O O . VAL A 1 78 ? 20.021 25.863 15.191 1.00 20.16 ? 74 VAL A O 1 ATOM 603 C CB . VAL A 1 78 ? 17.822 26.142 17.749 1.00 20.79 ? 74 VAL A CB 1 ATOM 604 C CG1 . VAL A 1 78 ? 18.457 24.733 17.826 1.00 20.90 ? 74 VAL A CG1 1 ATOM 605 C CG2 . VAL A 1 78 ? 17.672 26.695 19.230 1.00 17.83 ? 74 VAL A CG2 1 ATOM 606 N N . ASP A 1 79 ? 17.966 26.650 14.545 1.00 19.13 ? 75 ASP A N 1 ATOM 607 C CA . ASP A 1 79 ? 18.112 26.149 13.179 1.00 21.60 ? 75 ASP A CA 1 ATOM 608 C C . ASP A 1 79 ? 19.304 26.793 12.461 1.00 23.18 ? 75 ASP A C 1 ATOM 609 O O . ASP A 1 79 ? 19.975 26.119 11.684 1.00 23.95 ? 75 ASP A O 1 ATOM 610 C CB . ASP A 1 79 ? 16.865 26.452 12.342 1.00 22.90 ? 75 ASP A CB 1 ATOM 611 C CG . ASP A 1 79 ? 15.706 25.479 12.653 1.00 24.01 ? 75 ASP A CG 1 ATOM 612 O OD1 . ASP A 1 79 ? 15.926 24.428 13.281 1.00 24.35 ? 75 ASP A OD1 1 ATOM 613 O OD2 . ASP A 1 79 ? 14.590 25.798 12.231 1.00 25.39 ? 75 ASP A OD2 1 ATOM 614 N N . GLY A 1 80 ? 19.553 28.086 12.700 1.00 23.90 ? 76 GLY A N 1 ATOM 615 C CA . GLY A 1 80 ? 20.730 28.775 12.084 1.00 24.06 ? 76 GLY A CA 1 ATOM 616 C C . GLY A 1 80 ? 22.067 28.152 12.501 1.00 24.47 ? 76 GLY A C 1 ATOM 617 O O . GLY A 1 80 ? 22.968 27.952 11.676 1.00 23.23 ? 76 GLY A O 1 ATOM 618 N N . PHE A 1 81 ? 22.194 27.800 13.775 1.00 24.07 ? 77 PHE A N 1 ATOM 619 C CA . PHE A 1 81 ? 23.372 27.089 14.264 1.00 23.13 ? 77 PHE A CA 1 ATOM 620 C C . PHE A 1 81 ? 23.412 25.668 13.627 1.00 24.35 ? 77 PHE A C 1 ATOM 621 O O . PHE A 1 81 ? 24.487 25.171 13.206 1.00 24.31 ? 77 PHE A O 1 ATOM 622 C CB . PHE A 1 81 ? 23.256 26.949 15.794 1.00 21.96 ? 77 PHE A CB 1 ATOM 623 C CG . PHE A 1 81 ? 23.406 28.301 16.543 1.00 23.40 ? 77 PHE A CG 1 ATOM 624 C CD1 . PHE A 1 81 ? 24.298 29.286 16.073 1.00 23.55 ? 77 PHE A CD1 1 ATOM 625 C CD2 . PHE A 1 81 ? 22.643 28.583 17.670 1.00 20.75 ? 77 PHE A CD2 1 ATOM 626 C CE1 . PHE A 1 81 ? 24.451 30.478 16.799 1.00 23.46 ? 77 PHE A CE1 1 ATOM 627 C CE2 . PHE A 1 81 ? 22.802 29.790 18.377 1.00 23.09 ? 77 PHE A CE2 1 ATOM 628 C CZ . PHE A 1 81 ? 23.711 30.702 17.950 1.00 22.26 ? 77 PHE A CZ 1 ATOM 629 N N . GLN A 1 82 ? 22.248 25.001 13.601 1.00 22.50 ? 78 GLN A N 1 ATOM 630 C CA . GLN A 1 82 ? 22.167 23.627 13.056 1.00 23.71 ? 78 GLN A CA 1 ATOM 631 C C . GLN A 1 82 ? 22.571 23.605 11.573 1.00 23.54 ? 78 GLN A C 1 ATOM 632 O O . GLN A 1 82 ? 23.290 22.680 11.155 1.00 21.83 ? 78 GLN A O 1 ATOM 633 C CB . GLN A 1 82 ? 20.788 22.990 13.217 1.00 22.66 ? 78 GLN A CB 1 ATOM 634 C CG . GLN A 1 82 ? 20.763 21.483 12.893 1.00 23.31 ? 78 GLN A CG 1 ATOM 635 C CD . GLN A 1 82 ? 21.520 20.681 13.951 1.00 26.24 ? 78 GLN A CD 1 ATOM 636 O OE1 . GLN A 1 82 ? 22.755 20.668 13.942 1.00 23.02 ? 78 GLN A OE1 1 ATOM 637 N NE2 . GLN A 1 82 ? 20.794 20.059 14.884 1.00 23.75 ? 78 GLN A NE2 1 ATOM 638 N N . LYS A 1 83 ? 22.126 24.596 10.814 1.00 23.79 ? 79 LYS A N 1 ATOM 639 C CA . LYS A 1 83 ? 22.459 24.666 9.381 1.00 28.05 ? 79 LYS A CA 1 ATOM 640 C C . LYS A 1 83 ? 24.014 24.677 9.180 1.00 27.62 ? 79 LYS A C 1 ATOM 641 O O . LYS A 1 83 ? 24.546 24.006 8.289 1.00 27.37 ? 79 LYS A O 1 ATOM 642 C CB . LYS A 1 83 ? 21.780 25.896 8.738 1.00 29.76 ? 79 LYS A CB 1 ATOM 643 C CG . LYS A 1 83 ? 22.024 26.020 7.201 1.00 40.48 ? 79 LYS A CG 1 ATOM 644 C CD . LYS A 1 83 ? 21.103 27.083 6.548 1.00 50.78 ? 79 LYS A CD 1 ATOM 645 C CE . LYS A 1 83 ? 21.033 26.953 4.988 1.00 55.64 ? 79 LYS A CE 1 ATOM 646 N NZ . LYS A 1 83 ? 20.303 28.150 4.355 1.00 60.61 ? 79 LYS A NZ 1 ATOM 647 N N . ALA A 1 84 ? 24.724 25.420 10.020 1.00 25.03 ? 80 ALA A N 1 ATOM 648 C CA . ALA A 1 84 ? 26.186 25.471 9.938 1.00 25.35 ? 80 ALA A CA 1 ATOM 649 C C . ALA A 1 84 ? 26.763 24.087 10.284 1.00 25.57 ? 80 ALA A C 1 ATOM 650 O O . ALA A 1 84 ? 27.631 23.573 9.577 1.00 25.44 ? 80 ALA A O 1 ATOM 651 C CB . ALA A 1 84 ? 26.758 26.561 10.908 1.00 24.76 ? 80 ALA A CB 1 ATOM 652 N N . CYS A 1 85 ? 26.259 23.433 11.348 1.00 24.27 ? 81 CYS A N 1 ATOM 653 C CA . CYS A 1 85 ? 26.781 22.118 11.714 1.00 23.86 ? 81 CYS A CA 1 ATOM 654 C C . CYS A 1 85 ? 26.460 21.091 10.612 1.00 25.42 ? 81 CYS A C 1 ATOM 655 O O . CYS A 1 85 ? 27.288 20.199 10.333 1.00 24.89 ? 81 CYS A O 1 ATOM 656 C CB . CYS A 1 85 ? 26.184 21.626 13.067 1.00 23.52 ? 81 CYS A CB 1 ATOM 657 S SG . CYS A 1 85 ? 26.691 22.689 14.414 1.00 24.47 ? 81 CYS A SG 1 ATOM 658 N N . MET A 1 86 ? 25.275 21.182 9.991 1.00 23.59 ? 82 MET A N 1 ATOM 659 C CA . MET A 1 86 ? 24.949 20.159 8.981 1.00 25.27 ? 82 MET A CA 1 ATOM 660 C C . MET A 1 86 ? 25.770 20.342 7.683 1.00 25.38 ? 82 MET A C 1 ATOM 661 O O . MET A 1 86 ? 25.733 19.464 6.784 1.00 26.47 ? 82 MET A O 1 ATOM 662 C CB . MET A 1 86 ? 23.455 20.152 8.652 1.00 24.44 ? 82 MET A CB 1 ATOM 663 C CG . MET A 1 86 ? 22.544 19.756 9.827 1.00 26.65 ? 82 MET A CG 1 ATOM 664 S SD . MET A 1 86 ? 22.947 18.081 10.361 1.00 30.66 ? 82 MET A SD 1 ATOM 665 C CE . MET A 1 86 ? 22.404 17.005 8.959 1.00 30.02 ? 82 MET A CE 1 ATOM 666 N N . SER A 1 87 ? 26.430 21.478 7.559 1.00 24.99 ? 83 SER A N 1 ATOM 667 C CA . SER A 1 87 ? 27.200 21.788 6.340 1.00 27.03 ? 83 SER A CA 1 ATOM 668 C C . SER A 1 87 ? 28.671 21.299 6.476 1.00 26.77 ? 83 SER A C 1 ATOM 669 O O . SER A 1 87 ? 29.454 21.436 5.515 1.00 26.19 ? 83 SER A O 1 ATOM 670 C CB . SER A 1 87 ? 27.213 23.298 6.035 1.00 26.77 ? 83 SER A CB 1 ATOM 671 O OG . SER A 1 87 ? 28.103 23.940 6.965 1.00 28.26 ? 83 SER A OG 1 ATOM 672 N N . THR A 1 88 ? 29.041 20.727 7.625 1.00 25.26 ? 84 THR A N 1 ATOM 673 C CA . THR A 1 88 ? 30.363 20.132 7.716 1.00 25.05 ? 84 THR A CA 1 ATOM 674 C C . THR A 1 88 ? 30.460 18.900 6.795 1.00 25.72 ? 84 THR A C 1 ATOM 675 O O . THR A 1 88 ? 29.448 18.364 6.300 1.00 25.57 ? 84 THR A O 1 ATOM 676 C CB . THR A 1 88 ? 30.729 19.701 9.159 1.00 23.67 ? 84 THR A CB 1 ATOM 677 O OG1 . THR A 1 88 ? 29.785 18.713 9.585 1.00 22.09 ? 84 THR A OG1 1 ATOM 678 C CG2 . THR A 1 88 ? 30.715 20.932 10.159 1.00 22.90 ? 84 THR A CG2 1 ATOM 679 N N . ARG A 1 89 ? 31.701 18.440 6.615 1.00 25.68 ? 85 ARG A N 1 ATOM 680 C CA . ARG A 1 89 ? 31.995 17.265 5.794 1.00 26.08 ? 85 ARG A CA 1 ATOM 681 C C . ARG A 1 89 ? 31.148 16.067 6.175 1.00 25.34 ? 85 ARG A C 1 ATOM 682 O O . ARG A 1 89 ? 30.531 15.440 5.306 1.00 25.64 ? 85 ARG A O 1 ATOM 683 C CB . ARG A 1 89 ? 33.458 16.892 5.955 1.00 26.19 ? 85 ARG A CB 1 ATOM 684 C CG . ARG A 1 89 ? 33.834 15.711 5.067 1.00 29.02 ? 85 ARG A CG 1 ATOM 685 C CD . ARG A 1 89 ? 35.275 15.406 5.335 1.00 30.95 ? 85 ARG A CD 1 ATOM 686 N NE . ARG A 1 89 ? 35.491 14.662 6.577 1.00 30.00 ? 85 ARG A NE 1 ATOM 687 C CZ . ARG A 1 89 ? 35.750 13.363 6.632 1.00 28.54 ? 85 ARG A CZ 1 ATOM 688 N NH1 . ARG A 1 89 ? 35.761 12.627 5.505 1.00 27.41 ? 85 ARG A NH1 1 ATOM 689 N NH2 . ARG A 1 89 ? 36.014 12.807 7.803 1.00 25.94 ? 85 ARG A NH2 1 ATOM 690 N N . LEU A 1 90 ? 31.039 15.764 7.464 1.00 23.67 ? 86 LEU A N 1 ATOM 691 C CA . LEU A 1 90 ? 30.213 14.604 7.858 1.00 23.43 ? 86 LEU A CA 1 ATOM 692 C C . LEU A 1 90 ? 28.738 14.955 8.180 1.00 23.71 ? 86 LEU A C 1 ATOM 693 O O . LEU A 1 90 ? 27.908 14.037 8.276 1.00 24.64 ? 86 LEU A O 1 ATOM 694 C CB . LEU A 1 90 ? 30.814 13.873 9.078 1.00 23.19 ? 86 LEU A CB 1 ATOM 695 C CG . LEU A 1 90 ? 32.241 13.368 8.772 1.00 25.17 ? 86 LEU A CG 1 ATOM 696 C CD1 . LEU A 1 90 ? 32.864 12.878 10.106 1.00 24.02 ? 86 LEU A CD1 1 ATOM 697 C CD2 . LEU A 1 90 ? 32.210 12.251 7.699 1.00 27.96 ? 86 LEU A CD2 1 ATOM 698 N N . GLY A 1 91 ? 28.459 16.238 8.408 1.00 22.58 ? 87 GLY A N 1 ATOM 699 C CA . GLY A 1 91 ? 27.086 16.740 8.631 1.00 23.43 ? 87 GLY A CA 1 ATOM 700 C C . GLY A 1 91 ? 26.521 16.150 9.924 1.00 24.07 ? 87 GLY A C 1 ATOM 701 O O . GLY A 1 91 ? 25.403 15.581 9.959 1.00 23.95 ? 87 GLY A O 1 ATOM 702 N N . ILE A 1 92 ? 27.314 16.195 10.990 1.00 22.40 ? 88 ILE A N 1 ATOM 703 C CA . ILE A 1 92 ? 26.810 15.700 12.268 1.00 23.17 ? 88 ILE A CA 1 ATOM 704 C C . ILE A 1 92 ? 26.011 16.837 12.943 1.00 23.31 ? 88 ILE A C 1 ATOM 705 O O . ILE A 1 92 ? 26.585 17.916 13.247 1.00 24.17 ? 88 ILE A O 1 ATOM 706 C CB . ILE A 1 92 ? 27.943 15.273 13.205 1.00 23.81 ? 88 ILE A CB 1 ATOM 707 C CG1 . ILE A 1 92 ? 28.823 14.187 12.505 1.00 25.50 ? 88 ILE A CG1 1 ATOM 708 C CG2 . ILE A 1 92 ? 27.319 14.781 14.618 1.00 22.92 ? 88 ILE A CG2 1 ATOM 709 C CD1 . ILE A 1 92 ? 30.166 13.856 13.280 1.00 22.71 ? 88 ILE A CD1 1 ATOM 710 N N . PRO A 1 93 ? 24.709 16.596 13.225 1.00 22.74 ? 89 PRO A N 1 ATOM 711 C CA . PRO A 1 93 ? 23.903 17.686 13.844 1.00 21.64 ? 89 PRO A CA 1 ATOM 712 C C . PRO A 1 93 ? 24.377 17.998 15.278 1.00 22.42 ? 89 PRO A C 1 ATOM 713 O O . PRO A 1 93 ? 24.799 17.079 16.005 1.00 20.45 ? 89 PRO A O 1 ATOM 714 C CB . PRO A 1 93 ? 22.501 17.061 13.932 1.00 21.44 ? 89 PRO A CB 1 ATOM 715 C CG . PRO A 1 93 ? 22.734 15.576 14.028 1.00 20.81 ? 89 PRO A CG 1 ATOM 716 C CD . PRO A 1 93 ? 23.906 15.373 13.027 1.00 22.14 ? 89 PRO A CD 1 ATOM 717 N N . MET A 1 94 ? 24.331 19.270 15.682 1.00 21.59 ? 90 MET A N 1 ATOM 718 C CA . MET A 1 94 ? 24.640 19.581 17.065 1.00 22.02 ? 90 MET A CA 1 ATOM 719 C C . MET A 1 94 ? 23.385 19.259 17.921 1.00 21.88 ? 90 MET A C 1 ATOM 720 O O . MET A 1 94 ? 22.242 19.204 17.430 1.00 20.69 ? 90 MET A O 1 ATOM 721 C CB . MET A 1 94 ? 25.098 21.068 17.238 1.00 21.50 ? 90 MET A CB 1 ATOM 722 C CG . MET A 1 94 ? 24.046 22.105 16.763 1.00 23.02 ? 90 MET A CG 1 ATOM 723 S SD . MET A 1 94 ? 22.849 22.444 18.147 1.00 22.52 ? 90 MET A SD 1 ATOM 724 C CE . MET A 1 94 ? 21.346 22.805 17.227 1.00 22.30 ? 90 MET A CE 1 ATOM 725 N N . ILE A 1 95 ? 23.606 19.099 19.206 1.00 21.28 ? 91 ILE A N 1 ATOM 726 C CA . ILE A 1 95 ? 22.467 19.002 20.165 1.00 19.89 ? 91 ILE A CA 1 ATOM 727 C C . ILE A 1 95 ? 22.549 20.298 20.988 1.00 20.19 ? 91 ILE A C 1 ATOM 728 O O . ILE A 1 95 ? 23.660 20.702 21.444 1.00 20.68 ? 91 ILE A O 1 ATOM 729 C CB . ILE A 1 95 ? 22.591 17.741 21.043 1.00 19.54 ? 91 ILE A CB 1 ATOM 730 C CG1 . ILE A 1 95 ? 21.420 17.603 22.017 1.00 19.02 ? 91 ILE A CG1 1 ATOM 731 C CG2 . ILE A 1 95 ? 23.976 17.703 21.838 1.00 19.64 ? 91 ILE A CG2 1 ATOM 732 C CD1 . ILE A 1 95 ? 21.437 16.180 22.736 1.00 17.64 ? 91 ILE A CD1 1 ATOM 733 N N . TYR A 1 96 ? 21.408 20.933 21.214 1.00 19.29 ? 92 TYR A N 1 ATOM 734 C CA . TYR A 1 96 ? 21.360 22.237 21.922 1.00 21.31 ? 92 TYR A CA 1 ATOM 735 C C . TYR A 1 96 ? 20.752 21.991 23.319 1.00 21.77 ? 92 TYR A C 1 ATOM 736 O O . TYR A 1 96 ? 19.651 21.462 23.424 1.00 21.55 ? 92 TYR A O 1 ATOM 737 C CB . TYR A 1 96 ? 20.502 23.266 21.118 1.00 19.72 ? 92 TYR A CB 1 ATOM 738 C CG . TYR A 1 96 ? 20.687 24.721 21.564 1.00 21.44 ? 92 TYR A CG 1 ATOM 739 C CD1 . TYR A 1 96 ? 20.226 25.161 22.833 1.00 17.94 ? 92 TYR A CD1 1 ATOM 740 C CD2 . TYR A 1 96 ? 21.316 25.658 20.703 1.00 21.60 ? 92 TYR A CD2 1 ATOM 741 C CE1 . TYR A 1 96 ? 20.390 26.526 23.233 1.00 18.60 ? 92 TYR A CE1 1 ATOM 742 C CE2 . TYR A 1 96 ? 21.484 26.989 21.078 1.00 20.20 ? 92 TYR A CE2 1 ATOM 743 C CZ . TYR A 1 96 ? 21.058 27.400 22.357 1.00 21.01 ? 92 TYR A CZ 1 ATOM 744 O OH . TYR A 1 96 ? 21.224 28.710 22.733 1.00 23.03 ? 92 TYR A OH 1 ATOM 745 N N . GLY A 1 97 ? 21.474 22.378 24.371 1.00 21.01 ? 93 GLY A N 1 ATOM 746 C CA . GLY A 1 97 ? 20.999 22.164 25.728 1.00 20.53 ? 93 GLY A CA 1 ATOM 747 C C . GLY A 1 97 ? 20.610 23.452 26.468 1.00 19.98 ? 93 GLY A C 1 ATOM 748 O O . GLY A 1 97 ? 21.100 24.556 26.163 1.00 18.24 ? 93 GLY A O 1 ATOM 749 N N . ILE A 1 98 ? 19.770 23.300 27.491 1.00 19.50 ? 94 ILE A N 1 ATOM 750 C CA . ILE A 1 98 ? 19.318 24.473 28.227 1.00 19.27 ? 94 ILE A CA 1 ATOM 751 C C . ILE A 1 98 ? 18.792 24.029 29.606 1.00 19.10 ? 94 ILE A C 1 ATOM 752 O O . ILE A 1 98 ? 18.335 22.884 29.748 1.00 18.69 ? 94 ILE A O 1 ATOM 753 C CB . ILE A 1 98 ? 18.197 25.233 27.437 1.00 18.67 ? 94 ILE A CB 1 ATOM 754 C CG1 . ILE A 1 98 ? 18.046 26.687 28.004 1.00 18.20 ? 94 ILE A CG1 1 ATOM 755 C CG2 . ILE A 1 98 ? 16.776 24.394 27.408 1.00 17.60 ? 94 ILE A CG2 1 ATOM 756 C CD1 . ILE A 1 98 ? 17.237 27.653 27.086 1.00 18.31 ? 94 ILE A CD1 1 ATOM 757 N N . ASP A 1 99 ? 18.792 24.932 30.594 1.00 18.47 ? 95 ASP A N 1 ATOM 758 C CA . ASP A 1 99 ? 18.227 24.571 31.906 1.00 19.20 ? 95 ASP A CA 1 ATOM 759 C C . ASP A 1 99 ? 16.703 24.797 31.821 1.00 19.99 ? 95 ASP A C 1 ATOM 760 O O . ASP A 1 99 ? 16.226 25.891 32.083 1.00 20.72 ? 95 ASP A O 1 ATOM 761 C CB . ASP A 1 99 ? 18.837 25.448 32.988 1.00 17.20 ? 95 ASP A CB 1 ATOM 762 C CG . ASP A 1 99 ? 20.287 25.157 33.155 1.00 21.42 ? 95 ASP A CG 1 ATOM 763 O OD1 . ASP A 1 99 ? 20.574 24.097 33.774 1.00 21.07 ? 95 ASP A OD1 1 ATOM 764 O OD2 . ASP A 1 99 ? 21.137 25.902 32.590 1.00 20.21 ? 95 ASP A OD2 1 ATOM 765 N N . ALA A 1 100 ? 15.974 23.757 31.431 1.00 20.61 ? 96 ALA A N 1 ATOM 766 C CA . ALA A 1 100 ? 14.520 23.783 31.558 1.00 20.69 ? 96 ALA A CA 1 ATOM 767 C C . ALA A 1 100 ? 14.287 22.913 32.804 1.00 19.61 ? 96 ALA A C 1 ATOM 768 O O . ALA A 1 100 ? 14.075 21.660 32.725 1.00 20.68 ? 96 ALA A O 1 ATOM 769 C CB . ALA A 1 100 ? 13.889 23.154 30.323 1.00 18.11 ? 96 ALA A CB 1 ATOM 770 N N . VAL A 1 101 ? 14.285 23.578 33.953 1.00 19.65 ? 97 VAL A N 1 ATOM 771 C CA . VAL A 1 101 ? 14.287 22.888 35.236 1.00 19.09 ? 97 VAL A CA 1 ATOM 772 C C . VAL A 1 101 ? 12.976 23.101 36.019 1.00 19.30 ? 97 VAL A C 1 ATOM 773 O O . VAL A 1 101 ? 12.754 22.403 37.014 1.00 20.10 ? 97 VAL A O 1 ATOM 774 C CB . VAL A 1 101 ? 15.489 23.261 36.125 1.00 19.14 ? 97 VAL A CB 1 ATOM 775 C CG1 . VAL A 1 101 ? 16.848 22.831 35.466 1.00 21.40 ? 97 VAL A CG1 1 ATOM 776 C CG2 . VAL A 1 101 ? 15.476 24.826 36.478 1.00 19.27 ? 97 VAL A CG2 1 ATOM 777 N N . HIS A 1 102 ? 12.097 24.001 35.559 1.00 18.18 ? 98 HIS A N 1 ATOM 778 C CA . HIS A 1 102 ? 10.715 24.079 36.117 1.00 19.60 ? 98 HIS A CA 1 ATOM 779 C C . HIS A 1 102 ? 9.863 24.688 35.010 1.00 19.75 ? 98 HIS A C 1 ATOM 780 O O . HIS A 1 102 ? 9.350 25.786 35.157 1.00 19.06 ? 98 HIS A O 1 ATOM 781 C CB . HIS A 1 102 ? 10.592 24.792 37.499 1.00 18.46 ? 98 HIS A CB 1 ATOM 782 C CG . HIS A 1 102 ? 10.988 26.257 37.532 1.00 20.62 ? 98 HIS A CG 1 ATOM 783 N ND1 . HIS A 1 102 ? 10.345 27.180 38.343 1.00 18.03 ? 98 HIS A ND1 1 ATOM 784 C CD2 . HIS A 1 102 ? 11.992 26.935 36.917 1.00 16.96 ? 98 HIS A CD2 1 ATOM 785 C CE1 . HIS A 1 102 ? 10.931 28.364 38.202 1.00 18.52 ? 98 HIS A CE1 1 ATOM 786 N NE2 . HIS A 1 102 ? 11.919 28.238 37.328 1.00 18.74 ? 98 HIS A NE2 1 ATOM 787 N N . GLY A 1 103 ? 9.774 23.929 33.902 1.00 19.12 ? 99 GLY A N 1 ATOM 788 C CA . GLY A 1 103 ? 9.280 24.439 32.648 1.00 19.60 ? 99 GLY A CA 1 ATOM 789 C C . GLY A 1 103 ? 10.487 24.921 31.825 1.00 19.81 ? 99 GLY A C 1 ATOM 790 O O . GLY A 1 103 ? 11.653 24.805 32.260 1.00 19.53 ? 99 GLY A O 1 ATOM 791 N N . GLN A 1 104 ? 10.211 25.502 30.670 1.00 19.14 ? 100 GLN A N 1 ATOM 792 C CA . GLN A 1 104 ? 11.294 26.022 29.796 1.00 19.49 ? 100 GLN A CA 1 ATOM 793 C C . GLN A 1 104 ? 11.603 27.466 30.259 1.00 19.74 ? 100 GLN A C 1 ATOM 794 O O . GLN A 1 104 ? 11.294 28.456 29.579 1.00 19.87 ? 100 GLN A O 1 ATOM 795 C CB . GLN A 1 104 ? 10.755 25.946 28.349 1.00 18.53 ? 100 GLN A CB 1 ATOM 796 C CG . GLN A 1 104 ? 11.564 26.604 27.166 1.00 18.36 ? 100 GLN A CG 1 ATOM 797 C CD . GLN A 1 104 ? 12.963 26.188 27.052 1.00 18.84 ? 100 GLN A CD 1 ATOM 798 O OE1 . GLN A 1 104 ? 13.568 26.117 25.904 1.00 22.25 ? 100 GLN A OE1 1 ATOM 799 N NE2 . GLN A 1 104 ? 13.584 26.036 28.194 1.00 15.77 ? 100 GLN A NE2 1 ATOM 800 N N . ASN A 1 105 ? 12.192 27.577 31.438 1.00 19.12 ? 101 ASN A N 1 ATOM 801 C CA . ASN A 1 105 ? 12.087 28.782 32.243 1.00 19.01 ? 101 ASN A CA 1 ATOM 802 C C . ASN A 1 105 ? 12.942 29.985 31.804 1.00 20.04 ? 101 ASN A C 1 ATOM 803 O O . ASN A 1 105 ? 12.752 31.081 32.369 1.00 18.88 ? 101 ASN A O 1 ATOM 804 C CB . ASN A 1 105 ? 12.472 28.443 33.698 1.00 18.32 ? 101 ASN A CB 1 ATOM 805 C CG . ASN A 1 105 ? 13.816 27.646 33.761 1.00 20.74 ? 101 ASN A CG 1 ATOM 806 O OD1 . ASN A 1 105 ? 14.948 28.186 33.516 1.00 22.57 ? 101 ASN A OD1 1 ATOM 807 N ND2 . ASN A 1 105 ? 13.689 26.394 33.977 1.00 14.36 ? 101 ASN A ND2 1 ATOM 808 N N . ASN A 1 106 ? 13.890 29.814 30.857 1.00 20.31 ? 102 ASN A N 1 ATOM 809 C CA . ASN A 1 106 ? 14.594 31.017 30.301 1.00 19.95 ? 102 ASN A CA 1 ATOM 810 C C . ASN A 1 106 ? 13.731 31.762 29.310 1.00 20.73 ? 102 ASN A C 1 ATOM 811 O O . ASN A 1 106 ? 14.052 32.906 28.899 1.00 21.26 ? 102 ASN A O 1 ATOM 812 C CB . ASN A 1 106 ? 15.873 30.630 29.555 1.00 19.97 ? 102 ASN A CB 1 ATOM 813 C CG . ASN A 1 106 ? 17.011 30.223 30.490 1.00 22.42 ? 102 ASN A CG 1 ATOM 814 O OD1 . ASN A 1 106 ? 17.527 29.104 30.421 1.00 25.03 ? 102 ASN A OD1 1 ATOM 815 N ND2 . ASN A 1 106 ? 17.431 31.122 31.294 1.00 19.46 ? 102 ASN A ND2 1 ATOM 816 N N . VAL A 1 107 ? 12.645 31.115 28.892 1.00 19.14 ? 103 VAL A N 1 ATOM 817 C CA . VAL A 1 107 ? 11.891 31.633 27.748 1.00 19.56 ? 103 VAL A CA 1 ATOM 818 C C . VAL A 1 107 ? 10.693 32.460 28.182 1.00 21.54 ? 103 VAL A C 1 ATOM 819 O O . VAL A 1 107 ? 9.882 32.019 29.002 1.00 20.61 ? 103 VAL A O 1 ATOM 820 C CB . VAL A 1 107 ? 11.448 30.452 26.808 1.00 19.54 ? 103 VAL A CB 1 ATOM 821 C CG1 . VAL A 1 107 ? 10.569 30.973 25.634 1.00 19.35 ? 103 VAL A CG1 1 ATOM 822 C CG2 . VAL A 1 107 ? 12.734 29.723 26.305 1.00 19.69 ? 103 VAL A CG2 1 ATOM 823 N N . TYR A 1 108 ? 10.554 33.654 27.606 1.00 21.37 ? 104 TYR A N 1 ATOM 824 C CA . TYR A 1 108 ? 9.361 34.503 27.860 1.00 20.72 ? 104 TYR A CA 1 ATOM 825 C C . TYR A 1 108 ? 8.059 33.791 27.452 1.00 22.04 ? 104 TYR A C 1 ATOM 826 O O . TYR A 1 108 ? 7.976 33.249 26.342 1.00 21.36 ? 104 TYR A O 1 ATOM 827 C CB . TYR A 1 108 ? 9.465 35.807 27.051 1.00 21.99 ? 104 TYR A CB 1 ATOM 828 C CG . TYR A 1 108 ? 8.380 36.785 27.472 1.00 23.88 ? 104 TYR A CG 1 ATOM 829 C CD1 . TYR A 1 108 ? 8.536 37.581 28.611 1.00 25.81 ? 104 TYR A CD1 1 ATOM 830 C CD2 . TYR A 1 108 ? 7.193 36.863 26.759 1.00 30.05 ? 104 TYR A CD2 1 ATOM 831 C CE1 . TYR A 1 108 ? 7.481 38.468 29.009 1.00 27.18 ? 104 TYR A CE1 1 ATOM 832 C CE2 . TYR A 1 108 ? 6.167 37.723 27.161 1.00 32.44 ? 104 TYR A CE2 1 ATOM 833 C CZ . TYR A 1 108 ? 6.337 38.514 28.271 1.00 30.99 ? 104 TYR A CZ 1 ATOM 834 O OH . TYR A 1 108 ? 5.296 39.337 28.640 1.00 37.31 ? 104 TYR A OH 1 ATOM 835 N N . GLY A 1 109 ? 7.026 33.805 28.315 1.00 21.89 ? 105 GLY A N 1 ATOM 836 C CA . GLY A 1 109 ? 5.758 33.132 27.950 1.00 21.26 ? 105 GLY A CA 1 ATOM 837 C C . GLY A 1 109 ? 5.741 31.607 28.172 1.00 21.30 ? 105 GLY A C 1 ATOM 838 O O . GLY A 1 109 ? 4.671 30.982 27.989 1.00 21.43 ? 105 GLY A O 1 ATOM 839 N N . ALA A 1 110 ? 6.852 31.017 28.631 1.00 21.35 ? 106 ALA A N 1 ATOM 840 C CA . ALA A 1 110 ? 6.855 29.565 28.961 1.00 20.94 ? 106 ALA A CA 1 ATOM 841 C C . ALA A 1 110 ? 6.114 29.318 30.282 1.00 20.41 ? 106 ALA A C 1 ATOM 842 O O . ALA A 1 110 ? 6.247 30.096 31.240 1.00 18.53 ? 106 ALA A O 1 ATOM 843 C CB . ALA A 1 110 ? 8.255 29.011 29.135 1.00 20.04 ? 106 ALA A CB 1 ATOM 844 N N . THR A 1 111 ? 5.389 28.212 30.339 1.00 19.25 ? 107 THR A N 1 ATOM 845 C CA . THR A 1 111 ? 4.738 27.859 31.602 1.00 19.51 ? 107 THR A CA 1 ATOM 846 C C . THR A 1 111 ? 5.795 27.637 32.686 1.00 19.17 ? 107 THR A C 1 ATOM 847 O O . THR A 1 111 ? 6.785 26.918 32.413 1.00 21.13 ? 107 THR A O 1 ATOM 848 C CB . THR A 1 111 ? 3.974 26.551 31.439 1.00 19.57 ? 107 THR A CB 1 ATOM 849 O OG1 . THR A 1 111 ? 2.985 26.727 30.389 1.00 20.64 ? 107 THR A OG1 1 ATOM 850 C CG2 . THR A 1 111 ? 3.263 26.252 32.748 1.00 19.79 ? 107 THR A CG2 1 ATOM 851 N N . ILE A 1 112 ? 5.648 28.266 33.870 1.00 18.91 ? 108 ILE A N 1 ATOM 852 C CA . ILE A 1 112 ? 6.629 28.067 34.943 1.00 19.25 ? 108 ILE A CA 1 ATOM 853 C C . ILE A 1 112 ? 6.020 27.191 36.064 1.00 19.27 ? 108 ILE A C 1 ATOM 854 O O . ILE A 1 112 ? 5.017 27.598 36.724 1.00 20.15 ? 108 ILE A O 1 ATOM 855 C CB . ILE A 1 112 ? 7.171 29.405 35.558 1.00 19.05 ? 108 ILE A CB 1 ATOM 856 C CG1 . ILE A 1 112 ? 7.743 30.344 34.444 1.00 17.20 ? 108 ILE A CG1 1 ATOM 857 C CG2 . ILE A 1 112 ? 8.303 29.063 36.674 1.00 19.41 ? 108 ILE A CG2 1 ATOM 858 C CD1 . ILE A 1 112 ? 9.013 29.698 33.683 1.00 16.73 ? 108 ILE A CD1 1 ATOM 859 N N . PHE A 1 113 ? 6.566 25.975 36.206 1.00 18.82 ? 109 PHE A N 1 ATOM 860 C CA . PHE A 1 113 ? 6.067 25.012 37.229 1.00 18.27 ? 109 PHE A CA 1 ATOM 861 C C . PHE A 1 113 ? 6.699 25.318 38.593 1.00 19.46 ? 109 PHE A C 1 ATOM 862 O O . PHE A 1 113 ? 7.765 25.941 38.656 1.00 20.58 ? 109 PHE A O 1 ATOM 863 C CB . PHE A 1 113 ? 6.429 23.556 36.732 1.00 19.44 ? 109 PHE A CB 1 ATOM 864 C CG . PHE A 1 113 ? 5.684 23.186 35.451 1.00 20.23 ? 109 PHE A CG 1 ATOM 865 C CD1 . PHE A 1 113 ? 4.411 22.654 35.540 1.00 18.59 ? 109 PHE A CD1 1 ATOM 866 C CD2 . PHE A 1 113 ? 6.237 23.441 34.183 1.00 19.12 ? 109 PHE A CD2 1 ATOM 867 C CE1 . PHE A 1 113 ? 3.665 22.299 34.366 1.00 19.53 ? 109 PHE A CE1 1 ATOM 868 C CE2 . PHE A 1 113 ? 5.501 23.127 32.964 1.00 22.01 ? 109 PHE A CE2 1 ATOM 869 C CZ . PHE A 1 113 ? 4.194 22.555 33.090 1.00 20.20 ? 109 PHE A CZ 1 ATOM 870 N N . PRO A 1 114 ? 6.109 24.808 39.704 1.00 19.59 ? 110 PRO A N 1 ATOM 871 C CA . PRO A 1 114 ? 6.757 24.915 41.024 1.00 18.53 ? 110 PRO A CA 1 ATOM 872 C C . PRO A 1 114 ? 8.145 24.312 40.958 1.00 19.81 ? 110 PRO A C 1 ATOM 873 O O . PRO A 1 114 ? 8.356 23.291 40.281 1.00 18.94 ? 110 PRO A O 1 ATOM 874 C CB . PRO A 1 114 ? 5.864 24.009 41.924 1.00 18.26 ? 110 PRO A CB 1 ATOM 875 C CG . PRO A 1 114 ? 4.420 24.125 41.266 1.00 17.76 ? 110 PRO A CG 1 ATOM 876 C CD . PRO A 1 114 ? 4.876 23.975 39.745 1.00 18.60 ? 110 PRO A CD 1 ATOM 877 N N . HIS A 1 115 ? 9.069 24.888 41.716 1.00 19.06 ? 111 HIS A N 1 ATOM 878 C CA . HIS A 1 115 ? 10.365 24.275 41.886 1.00 18.67 ? 111 HIS A CA 1 ATOM 879 C C . HIS A 1 115 ? 10.298 22.914 42.612 1.00 19.28 ? 111 HIS A C 1 ATOM 880 O O . HIS A 1 115 ? 9.280 22.557 43.240 1.00 20.09 ? 111 HIS A O 1 ATOM 881 C CB . HIS A 1 115 ? 11.319 25.255 42.615 1.00 18.18 ? 111 HIS A CB 1 ATOM 882 C CG . HIS A 1 115 ? 12.017 26.195 41.668 1.00 18.19 ? 111 HIS A CG 1 ATOM 883 N ND1 . HIS A 1 115 ? 12.844 25.736 40.667 1.00 20.41 ? 111 HIS A ND1 1 ATOM 884 C CD2 . HIS A 1 115 ? 12.009 27.554 41.565 1.00 17.48 ? 111 HIS A CD2 1 ATOM 885 C CE1 . HIS A 1 115 ? 13.337 26.764 39.993 1.00 21.04 ? 111 HIS A CE1 1 ATOM 886 N NE2 . HIS A 1 115 ? 12.861 27.888 40.525 1.00 19.29 ? 111 HIS A NE2 1 ATOM 887 N N . ASN A 1 116 ? 11.367 22.164 42.478 1.00 19.75 ? 112 ASN A N 1 ATOM 888 C CA . ASN A 1 116 ? 11.415 20.772 42.946 1.00 20.63 ? 112 ASN A CA 1 ATOM 889 C C . ASN A 1 116 ? 11.036 20.553 44.408 1.00 20.15 ? 112 ASN A C 1 ATOM 890 O O . ASN A 1 116 ? 10.364 19.594 44.699 1.00 21.86 ? 112 ASN A O 1 ATOM 891 C CB . ASN A 1 116 ? 12.812 20.182 42.725 1.00 19.72 ? 112 ASN A CB 1 ATOM 892 C CG . ASN A 1 116 ? 13.095 19.809 41.253 1.00 19.79 ? 112 ASN A CG 1 ATOM 893 O OD1 . ASN A 1 116 ? 14.237 19.361 40.923 1.00 24.67 ? 112 ASN A OD1 1 ATOM 894 N ND2 . ASN A 1 116 ? 12.125 19.990 40.381 1.00 17.00 ? 112 ASN A ND2 1 ATOM 895 N N . VAL A 1 117 ? 11.437 21.447 45.321 1.00 21.31 ? 113 VAL A N 1 ATOM 896 C CA . VAL A 1 117 ? 11.142 21.181 46.732 1.00 21.27 ? 113 VAL A CA 1 ATOM 897 C C . VAL A 1 117 ? 9.612 21.130 46.917 1.00 20.03 ? 113 VAL A C 1 ATOM 898 O O . VAL A 1 117 ? 9.111 20.227 47.598 1.00 20.83 ? 113 VAL A O 1 ATOM 899 C CB . VAL A 1 117 ? 11.821 22.187 47.687 1.00 21.56 ? 113 VAL A CB 1 ATOM 900 C CG1 . VAL A 1 117 ? 11.343 23.631 47.366 1.00 21.19 ? 113 VAL A CG1 1 ATOM 901 C CG2 . VAL A 1 117 ? 11.467 21.793 49.142 1.00 23.81 ? 113 VAL A CG2 1 ATOM 902 N N . GLY A 1 118 ? 8.864 22.025 46.239 1.00 20.08 ? 114 GLY A N 1 ATOM 903 C CA . GLY A 1 118 ? 7.394 21.971 46.293 1.00 18.82 ? 114 GLY A CA 1 ATOM 904 C C . GLY A 1 118 ? 6.855 20.727 45.620 1.00 19.82 ? 114 GLY A C 1 ATOM 905 O O . GLY A 1 118 ? 5.821 20.158 46.063 1.00 20.08 ? 114 GLY A O 1 ATOM 906 N N . LEU A 1 119 ? 7.488 20.289 44.534 1.00 20.53 ? 115 LEU A N 1 ATOM 907 C CA . LEU A 1 119 ? 7.027 19.005 43.917 1.00 19.47 ? 115 LEU A CA 1 ATOM 908 C C . LEU A 1 119 ? 7.250 17.842 44.889 1.00 20.29 ? 115 LEU A C 1 ATOM 909 O O . LEU A 1 119 ? 6.419 16.937 44.949 1.00 21.39 ? 115 LEU A O 1 ATOM 910 C CB . LEU A 1 119 ? 7.765 18.705 42.555 1.00 19.52 ? 115 LEU A CB 1 ATOM 911 C CG . LEU A 1 119 ? 7.524 19.818 41.506 1.00 20.96 ? 115 LEU A CG 1 ATOM 912 C CD1 . LEU A 1 119 ? 8.239 19.492 40.133 1.00 20.83 ? 115 LEU A CD1 1 ATOM 913 C CD2 . LEU A 1 119 ? 5.990 20.078 41.289 1.00 19.26 ? 115 LEU A CD2 1 ATOM 914 N N . GLY A 1 120 ? 8.359 17.855 45.628 1.00 19.88 ? 116 GLY A N 1 ATOM 915 C CA . GLY A 1 120 ? 8.563 16.835 46.691 1.00 20.77 ? 116 GLY A CA 1 ATOM 916 C C . GLY A 1 120 ? 7.414 16.845 47.691 1.00 22.18 ? 116 GLY A C 1 ATOM 917 O O . GLY A 1 120 ? 6.987 15.784 48.161 1.00 24.49 ? 116 GLY A O 1 ATOM 918 N N . ALA A 1 121 ? 6.915 18.028 48.039 1.00 20.94 ? 117 ALA A N 1 ATOM 919 C CA . ALA A 1 121 ? 5.713 18.139 48.942 1.00 21.62 ? 117 ALA A CA 1 ATOM 920 C C . ALA A 1 121 ? 4.437 17.456 48.394 1.00 22.53 ? 117 ALA A C 1 ATOM 921 O O . ALA A 1 121 ? 3.594 17.017 49.171 1.00 24.01 ? 117 ALA A O 1 ATOM 922 C CB . ALA A 1 121 ? 5.443 19.621 49.322 1.00 20.82 ? 117 ALA A CB 1 ATOM 923 N N . THR A 1 122 ? 4.310 17.300 47.074 1.00 22.02 ? 118 THR A N 1 ATOM 924 C CA . THR A 1 122 ? 3.129 16.606 46.513 1.00 21.90 ? 118 THR A CA 1 ATOM 925 C C . THR A 1 122 ? 3.119 15.095 46.726 1.00 23.29 ? 118 THR A C 1 ATOM 926 O O . THR A 1 122 ? 2.062 14.476 46.683 1.00 24.91 ? 118 THR A O 1 ATOM 927 C CB . THR A 1 122 ? 2.971 16.839 44.997 1.00 22.67 ? 118 THR A CB 1 ATOM 928 O OG1 . THR A 1 122 ? 4.001 16.090 44.308 1.00 22.96 ? 118 THR A OG1 1 ATOM 929 C CG2 . THR A 1 122 ? 3.040 18.380 44.657 1.00 21.66 ? 118 THR A CG2 1 ATOM 930 N N . ARG A 1 123 ? 4.280 14.497 46.968 1.00 24.22 ? 119 ARG A N 1 ATOM 931 C CA . ARG A 1 123 ? 4.411 13.020 46.934 1.00 25.24 ? 119 ARG A CA 1 ATOM 932 C C . ARG A 1 123 ? 3.690 12.397 45.734 1.00 26.64 ? 119 ARG A C 1 ATOM 933 O O . ARG A 1 123 ? 3.084 11.287 45.840 1.00 25.62 ? 119 ARG A O 1 ATOM 934 C CB . ARG A 1 123 ? 3.874 12.417 48.253 1.00 27.88 ? 119 ARG A CB 1 ATOM 935 C CG . ARG A 1 123 ? 4.513 12.975 49.527 1.00 26.14 ? 119 ARG A CG 1 ATOM 936 C CD . ARG A 1 123 ? 6.052 12.661 49.642 1.00 28.19 ? 119 ARG A CD 1 ATOM 937 N NE . ARG A 1 123 ? 6.440 12.791 51.045 1.00 29.26 ? 119 ARG A NE 1 ATOM 938 C CZ . ARG A 1 123 ? 6.659 13.936 51.673 1.00 31.64 ? 119 ARG A CZ 1 ATOM 939 N NH1 . ARG A 1 123 ? 6.604 15.115 51.010 1.00 22.52 ? 119 ARG A NH1 1 ATOM 940 N NH2 . ARG A 1 123 ? 6.952 13.906 52.978 1.00 25.63 ? 119 ARG A NH2 1 ATOM 941 N N . ASP A 1 124 ? 3.734 13.076 44.569 1.00 24.80 ? 120 ASP A N 1 ATOM 942 C CA . ASP A 1 124 ? 2.936 12.648 43.411 1.00 24.45 ? 120 ASP A CA 1 ATOM 943 C C . ASP A 1 124 ? 3.840 12.459 42.185 1.00 24.58 ? 120 ASP A C 1 ATOM 944 O O . ASP A 1 124 ? 4.003 13.374 41.382 1.00 23.34 ? 120 ASP A O 1 ATOM 945 C CB . ASP A 1 124 ? 1.802 13.688 43.164 1.00 25.20 ? 120 ASP A CB 1 ATOM 946 C CG . ASP A 1 124 ? 0.749 13.194 42.158 1.00 29.10 ? 120 ASP A CG 1 ATOM 947 O OD1 . ASP A 1 124 ? 1.064 12.284 41.363 1.00 28.73 ? 120 ASP A OD1 1 ATOM 948 O OD2 . ASP A 1 124 ? -0.345 13.769 42.153 1.00 33.11 ? 120 ASP A OD2 1 ATOM 949 N N . PRO A 1 125 ? 4.470 11.277 42.053 1.00 24.56 ? 121 PRO A N 1 ATOM 950 C CA . PRO A 1 125 ? 5.420 11.083 40.955 1.00 24.56 ? 121 PRO A CA 1 ATOM 951 C C . PRO A 1 125 ? 4.766 11.142 39.614 1.00 24.99 ? 121 PRO A C 1 ATOM 952 O O . PRO A 1 125 ? 5.407 11.568 38.660 1.00 25.15 ? 121 PRO A O 1 ATOM 953 C CB . PRO A 1 125 ? 6.012 9.677 41.256 1.00 25.55 ? 121 PRO A CB 1 ATOM 954 C CG . PRO A 1 125 ? 5.791 9.548 42.737 1.00 26.54 ? 121 PRO A CG 1 ATOM 955 C CD . PRO A 1 125 ? 4.452 10.102 42.968 1.00 25.07 ? 121 PRO A CD 1 ATOM 956 N N . TYR A 1 126 ? 3.494 10.742 39.505 1.00 24.18 ? 122 TYR A N 1 ATOM 957 C CA . TYR A 1 126 ? 2.807 10.848 38.218 1.00 24.65 ? 122 TYR A CA 1 ATOM 958 C C . TYR A 1 126 ? 2.574 12.296 37.788 1.00 23.62 ? 122 TYR A C 1 ATOM 959 O O . TYR A 1 126 ? 2.645 12.641 36.594 1.00 23.84 ? 122 TYR A O 1 ATOM 960 C CB . TYR A 1 126 ? 1.444 10.096 38.247 1.00 26.25 ? 122 TYR A CB 1 ATOM 961 C CG . TYR A 1 126 ? 0.806 10.096 36.887 1.00 27.35 ? 122 TYR A CG 1 ATOM 962 C CD1 . TYR A 1 126 ? 1.544 9.686 35.761 1.00 31.43 ? 122 TYR A CD1 1 ATOM 963 C CD2 . TYR A 1 126 ? -0.514 10.548 36.709 1.00 31.00 ? 122 TYR A CD2 1 ATOM 964 C CE1 . TYR A 1 126 ? 0.957 9.711 34.473 1.00 35.28 ? 122 TYR A CE1 1 ATOM 965 C CE2 . TYR A 1 126 ? -1.115 10.558 35.430 1.00 33.25 ? 122 TYR A CE2 1 ATOM 966 C CZ . TYR A 1 126 ? -0.359 10.154 34.329 1.00 37.22 ? 122 TYR A CZ 1 ATOM 967 O OH . TYR A 1 126 ? -0.913 10.200 33.065 1.00 39.65 ? 122 TYR A OH 1 ATOM 968 N N . LEU A 1 127 ? 2.228 13.156 38.735 1.00 24.49 ? 123 LEU A N 1 ATOM 969 C CA . LEU A 1 127 ? 2.162 14.582 38.447 1.00 23.33 ? 123 LEU A CA 1 ATOM 970 C C . LEU A 1 127 ? 3.516 15.052 37.859 1.00 22.59 ? 123 LEU A C 1 ATOM 971 O O . LEU A 1 127 ? 3.547 15.813 36.893 1.00 22.22 ? 123 LEU A O 1 ATOM 972 C CB . LEU A 1 127 ? 1.859 15.356 39.761 1.00 23.95 ? 123 LEU A CB 1 ATOM 973 C CG . LEU A 1 127 ? 1.980 16.903 39.714 1.00 24.59 ? 123 LEU A CG 1 ATOM 974 C CD1 . LEU A 1 127 ? 0.769 17.526 38.953 1.00 20.92 ? 123 LEU A CD1 1 ATOM 975 C CD2 . LEU A 1 127 ? 2.119 17.548 41.193 1.00 22.31 ? 123 LEU A CD2 1 ATOM 976 N N . VAL A 1 128 ? 4.622 14.625 38.467 1.00 21.20 ? 124 VAL A N 1 ATOM 977 C CA . VAL A 1 128 ? 5.964 15.065 38.035 1.00 21.04 ? 124 VAL A CA 1 ATOM 978 C C . VAL A 1 128 ? 6.269 14.523 36.639 1.00 21.73 ? 124 VAL A C 1 ATOM 979 O O . VAL A 1 128 ? 6.784 15.259 35.771 1.00 20.63 ? 124 VAL A O 1 ATOM 980 C CB . VAL A 1 128 ? 7.054 14.768 39.122 1.00 19.90 ? 124 VAL A CB 1 ATOM 981 C CG1 . VAL A 1 128 ? 8.507 15.044 38.625 1.00 19.68 ? 124 VAL A CG1 1 ATOM 982 C CG2 . VAL A 1 128 ? 6.789 15.664 40.378 1.00 21.38 ? 124 VAL A CG2 1 ATOM 983 N N . LYS A 1 129 ? 5.841 13.280 36.391 1.00 21.72 ? 125 LYS A N 1 ATOM 984 C CA . LYS A 1 129 ? 5.965 12.746 35.039 1.00 22.03 ? 125 LYS A CA 1 ATOM 985 C C . LYS A 1 129 ? 5.237 13.628 33.997 1.00 22.66 ? 125 LYS A C 1 ATOM 986 O O . LYS A 1 129 ? 5.802 13.991 32.978 1.00 22.14 ? 125 LYS A O 1 ATOM 987 C CB . LYS A 1 129 ? 5.404 11.334 34.988 1.00 22.95 ? 125 LYS A CB 1 ATOM 988 C CG . LYS A 1 129 ? 5.671 10.682 33.610 1.00 22.24 ? 125 LYS A CG 1 ATOM 989 C CD . LYS A 1 129 ? 5.054 9.227 33.576 1.00 25.56 ? 125 LYS A CD 1 ATOM 990 C CE . LYS A 1 129 ? 5.427 8.524 32.232 1.00 26.74 ? 125 LYS A CE 1 ATOM 991 N NZ . LYS A 1 129 ? 4.937 7.079 32.162 1.00 28.57 ? 125 LYS A NZ 1 ATOM 992 N N . ARG A 1 130 ? 3.996 14.008 34.284 1.00 21.14 ? 126 ARG A N 1 ATOM 993 C CA . ARG A 1 130 ? 3.204 14.860 33.393 1.00 21.30 ? 126 ARG A CA 1 ATOM 994 C C . ARG A 1 130 ? 3.863 16.241 33.250 1.00 20.29 ? 126 ARG A C 1 ATOM 995 O O . ARG A 1 130 ? 3.809 16.854 32.177 1.00 20.59 ? 126 ARG A O 1 ATOM 996 C CB . ARG A 1 130 ? 1.765 15.026 33.985 1.00 22.38 ? 126 ARG A CB 1 ATOM 997 C CG . ARG A 1 130 ? 0.950 13.646 33.936 1.00 25.93 ? 126 ARG A CG 1 ATOM 998 C CD . ARG A 1 130 ? 0.109 13.442 35.281 1.00 34.82 ? 126 ARG A CD 1 ATOM 999 N NE . ARG A 1 130 ? -0.841 14.481 35.311 1.00 35.82 ? 126 ARG A NE 1 ATOM 1000 C CZ . ARG A 1 130 ? -1.477 15.064 36.332 1.00 32.59 ? 126 ARG A CZ 1 ATOM 1001 N NH1 . ARG A 1 130 ? -1.477 14.677 37.616 1.00 31.01 ? 126 ARG A NH1 1 ATOM 1002 N NH2 . ARG A 1 130 ? -2.230 16.066 35.952 1.00 28.73 ? 126 ARG A NH2 1 ATOM 1003 N N . ILE A 1 131 ? 4.471 16.752 34.316 1.00 20.24 ? 127 ILE A N 1 ATOM 1004 C CA . ILE A 1 131 ? 5.233 18.029 34.168 1.00 18.64 ? 127 ILE A CA 1 ATOM 1005 C C . ILE A 1 131 ? 6.424 17.807 33.226 1.00 20.27 ? 127 ILE A C 1 ATOM 1006 O O . ILE A 1 131 ? 6.696 18.667 32.379 1.00 20.53 ? 127 ILE A O 1 ATOM 1007 C CB . ILE A 1 131 ? 5.701 18.557 35.541 1.00 19.22 ? 127 ILE A CB 1 ATOM 1008 C CG1 . ILE A 1 131 ? 4.483 18.996 36.382 1.00 19.33 ? 127 ILE A CG1 1 ATOM 1009 C CG2 . ILE A 1 131 ? 6.772 19.719 35.400 1.00 20.78 ? 127 ILE A CG2 1 ATOM 1010 C CD1 . ILE A 1 131 ? 4.894 19.376 37.873 1.00 18.76 ? 127 ILE A CD1 1 ATOM 1011 N N . GLY A 1 132 ? 7.127 16.659 33.337 1.00 19.57 ? 128 GLY A N 1 ATOM 1012 C CA . GLY A 1 132 ? 8.217 16.356 32.341 1.00 19.50 ? 128 GLY A CA 1 ATOM 1013 C C . GLY A 1 132 ? 7.667 16.342 30.915 1.00 20.07 ? 128 GLY A C 1 ATOM 1014 O O . GLY A 1 132 ? 8.311 16.838 29.990 1.00 18.39 ? 128 GLY A O 1 ATOM 1015 N N . GLU A 1 133 ? 6.483 15.723 30.713 1.00 19.81 ? 129 GLU A N 1 ATOM 1016 C CA . GLU A 1 133 ? 5.884 15.662 29.390 1.00 19.72 ? 129 GLU A CA 1 ATOM 1017 C C . GLU A 1 133 ? 5.593 17.054 28.850 1.00 20.38 ? 129 GLU A C 1 ATOM 1018 O O . GLU A 1 133 ? 5.894 17.343 27.706 1.00 21.01 ? 129 GLU A O 1 ATOM 1019 C CB . GLU A 1 133 ? 4.580 14.782 29.404 1.00 20.57 ? 129 GLU A CB 1 ATOM 1020 C CG . GLU A 1 133 ? 4.957 13.377 29.890 1.00 20.10 ? 129 GLU A CG 1 ATOM 1021 C CD . GLU A 1 133 ? 3.775 12.374 30.076 1.00 29.85 ? 129 GLU A CD 1 ATOM 1022 O OE1 . GLU A 1 133 ? 4.028 11.128 30.097 1.00 26.21 ? 129 GLU A OE1 1 ATOM 1023 O OE2 . GLU A 1 133 ? 2.635 12.842 30.230 1.00 28.68 ? 129 GLU A OE2 1 ATOM 1024 N N . ALA A 1 134 ? 4.965 17.899 29.646 1.00 19.99 ? 130 ALA A N 1 ATOM 1025 C CA . ALA A 1 134 ? 4.625 19.272 29.219 1.00 20.67 ? 130 ALA A CA 1 ATOM 1026 C C . ALA A 1 134 ? 5.871 20.085 28.979 1.00 20.23 ? 130 ALA A C 1 ATOM 1027 O O . ALA A 1 134 ? 5.938 20.867 28.029 1.00 20.45 ? 130 ALA A O 1 ATOM 1028 C CB . ALA A 1 134 ? 3.740 19.989 30.340 1.00 21.88 ? 130 ALA A CB 1 ATOM 1029 N N . THR A 1 135 ? 6.871 19.928 29.840 1.00 20.92 ? 131 THR A N 1 ATOM 1030 C CA . THR A 1 135 ? 8.139 20.661 29.675 1.00 20.03 ? 131 THR A CA 1 ATOM 1031 C C . THR A 1 135 ? 8.871 20.268 28.375 1.00 20.22 ? 131 THR A C 1 ATOM 1032 O O . THR A 1 135 ? 9.358 21.131 27.617 1.00 21.01 ? 131 THR A O 1 ATOM 1033 C CB . THR A 1 135 ? 9.077 20.365 30.895 1.00 20.40 ? 131 THR A CB 1 ATOM 1034 O OG1 . THR A 1 135 ? 8.471 20.846 32.108 1.00 21.16 ? 131 THR A OG1 1 ATOM 1035 C CG2 . THR A 1 135 ? 10.453 21.081 30.711 1.00 19.08 ? 131 THR A CG2 1 ATOM 1036 N N . ALA A 1 136 ? 8.887 18.973 28.041 1.00 20.25 ? 132 ALA A N 1 ATOM 1037 C CA . ALA A 1 136 ? 9.511 18.554 26.777 1.00 20.46 ? 132 ALA A CA 1 ATOM 1038 C C . ALA A 1 136 ? 8.850 19.283 25.594 1.00 20.22 ? 132 ALA A C 1 ATOM 1039 O O . ALA A 1 136 ? 9.522 19.671 24.639 1.00 20.65 ? 132 ALA A O 1 ATOM 1040 C CB . ALA A 1 136 ? 9.378 16.978 26.579 1.00 20.17 ? 132 ALA A CB 1 ATOM 1041 N N . LEU A 1 137 ? 7.532 19.416 25.640 1.00 21.07 ? 133 LEU A N 1 ATOM 1042 C CA . LEU A 1 137 ? 6.791 20.048 24.527 1.00 20.53 ? 133 LEU A CA 1 ATOM 1043 C C . LEU A 1 137 ? 7.157 21.528 24.444 1.00 20.18 ? 133 LEU A C 1 ATOM 1044 O O . LEU A 1 137 ? 7.302 22.047 23.327 1.00 20.63 ? 133 LEU A O 1 ATOM 1045 C CB . LEU A 1 137 ? 5.260 19.949 24.679 1.00 19.84 ? 133 LEU A CB 1 ATOM 1046 C CG . LEU A 1 137 ? 4.668 18.493 24.602 1.00 23.65 ? 133 LEU A CG 1 ATOM 1047 C CD1 . LEU A 1 137 ? 3.146 18.451 24.952 1.00 22.38 ? 133 LEU A CD1 1 ATOM 1048 C CD2 . LEU A 1 137 ? 4.882 17.892 23.181 1.00 24.43 ? 133 LEU A CD2 1 ATOM 1049 N N . GLU A 1 138 ? 7.287 22.193 25.595 1.00 18.21 ? 134 GLU A N 1 ATOM 1050 C CA . GLU A 1 138 ? 7.596 23.635 25.550 1.00 19.48 ? 134 GLU A CA 1 ATOM 1051 C C . GLU A 1 138 ? 9.063 23.856 25.223 1.00 19.17 ? 134 GLU A C 1 ATOM 1052 O O . GLU A 1 138 ? 9.422 24.892 24.631 1.00 19.57 ? 134 GLU A O 1 ATOM 1053 C CB . GLU A 1 138 ? 7.216 24.368 26.863 1.00 19.14 ? 134 GLU A CB 1 ATOM 1054 C CG . GLU A 1 138 ? 5.694 24.158 27.165 1.00 20.70 ? 134 GLU A CG 1 ATOM 1055 C CD . GLU A 1 138 ? 5.052 25.303 27.965 1.00 25.10 ? 134 GLU A CD 1 ATOM 1056 O OE1 . GLU A 1 138 ? 5.694 26.344 28.158 1.00 20.17 ? 134 GLU A OE1 1 ATOM 1057 O OE2 . GLU A 1 138 ? 3.881 25.168 28.363 1.00 23.46 ? 134 GLU A OE2 1 ATOM 1058 N N . VAL A 1 139 ? 9.916 22.920 25.596 1.00 19.69 ? 135 VAL A N 1 ATOM 1059 C CA . VAL A 1 139 ? 11.348 23.018 25.110 1.00 19.83 ? 135 VAL A CA 1 ATOM 1060 C C . VAL A 1 139 ? 11.439 22.811 23.575 1.00 20.04 ? 135 VAL A C 1 ATOM 1061 O O . VAL A 1 139 ? 12.085 23.575 22.868 1.00 20.23 ? 135 VAL A O 1 ATOM 1062 C CB . VAL A 1 139 ? 12.218 21.992 25.880 1.00 19.40 ? 135 VAL A CB 1 ATOM 1063 C CG1 . VAL A 1 139 ? 13.656 21.975 25.279 1.00 18.91 ? 135 VAL A CG1 1 ATOM 1064 C CG2 . VAL A 1 139 ? 12.289 22.422 27.390 1.00 18.01 ? 135 VAL A CG2 1 ATOM 1065 N N . ARG A 1 140 ? 10.741 21.785 23.052 1.00 20.11 ? 136 ARG A N 1 ATOM 1066 C CA . ARG A 1 140 ? 10.714 21.570 21.588 1.00 21.13 ? 136 ARG A CA 1 ATOM 1067 C C . ARG A 1 140 ? 9.989 22.699 20.846 1.00 21.80 ? 136 ARG A C 1 ATOM 1068 O O . ARG A 1 140 ? 10.287 22.952 19.667 1.00 21.41 ? 136 ARG A O 1 ATOM 1069 C CB . ARG A 1 140 ? 10.035 20.198 21.221 1.00 19.32 ? 136 ARG A CB 1 ATOM 1070 C CG . ARG A 1 140 ? 11.006 19.017 21.519 1.00 18.91 ? 136 ARG A CG 1 ATOM 1071 C CD . ARG A 1 140 ? 12.146 18.972 20.480 1.00 19.16 ? 136 ARG A CD 1 ATOM 1072 N NE . ARG A 1 140 ? 12.864 17.710 20.639 1.00 21.83 ? 136 ARG A NE 1 ATOM 1073 C CZ . ARG A 1 140 ? 13.668 17.193 19.695 1.00 23.83 ? 136 ARG A CZ 1 ATOM 1074 N NH1 . ARG A 1 140 ? 13.889 17.883 18.592 1.00 19.06 ? 136 ARG A NH1 1 ATOM 1075 N NH2 . ARG A 1 140 ? 14.215 15.996 19.863 1.00 23.21 ? 136 ARG A NH2 1 ATOM 1076 N N . ALA A 1 141 ? 9.056 23.388 21.537 1.00 20.46 ? 137 ALA A N 1 ATOM 1077 C CA . ALA A 1 141 ? 8.455 24.604 20.921 1.00 20.32 ? 137 ALA A CA 1 ATOM 1078 C C . ALA A 1 141 ? 9.520 25.631 20.522 1.00 20.26 ? 137 ALA A C 1 ATOM 1079 O O . ALA A 1 141 ? 9.343 26.427 19.571 1.00 19.98 ? 137 ALA A O 1 ATOM 1080 C CB . ALA A 1 141 ? 7.417 25.302 21.918 1.00 20.23 ? 137 ALA A CB 1 ATOM 1081 N N . THR A 1 142 ? 10.598 25.643 21.267 1.00 19.91 ? 138 THR A N 1 ATOM 1082 C CA . THR A 1 142 ? 11.699 26.610 21.012 1.00 20.37 ? 138 THR A CA 1 ATOM 1083 C C . THR A 1 142 ? 12.850 25.990 20.192 1.00 21.16 ? 138 THR A C 1 ATOM 1084 O O . THR A 1 142 ? 13.890 26.611 20.007 1.00 21.40 ? 138 THR A O 1 ATOM 1085 C CB . THR A 1 142 ? 12.241 27.201 22.332 1.00 21.83 ? 138 THR A CB 1 ATOM 1086 O OG1 . THR A 1 142 ? 12.830 26.161 23.152 1.00 20.31 ? 138 THR A OG1 1 ATOM 1087 C CG2 . THR A 1 142 ? 11.105 27.846 23.102 1.00 21.54 ? 138 THR A CG2 1 ATOM 1088 N N . GLY A 1 143 ? 12.668 24.753 19.698 1.00 21.08 ? 139 GLY A N 1 ATOM 1089 C CA . GLY A 1 143 ? 13.690 24.164 18.784 1.00 20.22 ? 139 GLY A CA 1 ATOM 1090 C C . GLY A 1 143 ? 14.787 23.453 19.582 1.00 22.50 ? 139 GLY A C 1 ATOM 1091 O O . GLY A 1 143 ? 15.796 22.962 19.013 1.00 23.50 ? 139 GLY A O 1 ATOM 1092 N N . ILE A 1 144 ? 14.626 23.380 20.900 1.00 18.87 ? 140 ILE A N 1 ATOM 1093 C CA . ILE A 1 144 ? 15.735 22.838 21.718 1.00 19.32 ? 140 ILE A CA 1 ATOM 1094 C C . ILE A 1 144 ? 15.488 21.375 22.045 1.00 20.88 ? 140 ILE A C 1 ATOM 1095 O O . ILE A 1 144 ? 14.311 20.963 22.242 1.00 19.99 ? 140 ILE A O 1 ATOM 1096 C CB . ILE A 1 144 ? 15.971 23.747 22.950 1.00 19.51 ? 140 ILE A CB 1 ATOM 1097 C CG1 . ILE A 1 144 ? 16.514 25.134 22.454 1.00 19.64 ? 140 ILE A CG1 1 ATOM 1098 C CG2 . ILE A 1 144 ? 16.849 23.041 24.053 1.00 17.66 ? 140 ILE A CG2 1 ATOM 1099 C CD1 . ILE A 1 144 ? 16.579 26.217 23.609 1.00 18.58 ? 140 ILE A CD1 1 ATOM 1100 N N . GLN A 1 145 ? 16.564 20.565 22.034 1.00 19.94 ? 141 GLN A N 1 ATOM 1101 C CA . GLN A 1 145 ? 16.369 19.099 22.106 1.00 20.13 ? 141 GLN A CA 1 ATOM 1102 C C . GLN A 1 145 ? 16.869 18.472 23.417 1.00 20.93 ? 141 GLN A C 1 ATOM 1103 O O . GLN A 1 145 ? 16.852 17.225 23.537 1.00 21.45 ? 141 GLN A O 1 ATOM 1104 C CB . GLN A 1 145 ? 17.138 18.407 20.928 1.00 20.80 ? 141 GLN A CB 1 ATOM 1105 C CG . GLN A 1 145 ? 16.934 19.114 19.558 1.00 24.38 ? 141 GLN A CG 1 ATOM 1106 C CD . GLN A 1 145 ? 18.084 20.073 19.176 1.00 24.67 ? 141 GLN A CD 1 ATOM 1107 O OE1 . GLN A 1 145 ? 18.848 20.539 20.031 1.00 22.40 ? 141 GLN A OE1 1 ATOM 1108 N NE2 . GLN A 1 145 ? 18.175 20.386 17.868 1.00 21.66 ? 141 GLN A NE2 1 ATOM 1109 N N . TYR A 1 146 ? 17.329 19.284 24.392 1.00 19.96 ? 142 TYR A N 1 ATOM 1110 C CA . TYR A 1 146 ? 18.088 18.706 25.519 1.00 20.05 ? 142 TYR A CA 1 ATOM 1111 C C . TYR A 1 146 ? 17.924 19.596 26.728 1.00 20.00 ? 142 TYR A C 1 ATOM 1112 O O . TYR A 1 146 ? 18.191 20.782 26.636 1.00 20.46 ? 142 TYR A O 1 ATOM 1113 C CB . TYR A 1 146 ? 19.563 18.637 25.088 1.00 18.78 ? 142 TYR A CB 1 ATOM 1114 C CG . TYR A 1 146 ? 20.600 18.191 26.104 1.00 20.33 ? 142 TYR A CG 1 ATOM 1115 C CD1 . TYR A 1 146 ? 20.280 17.343 27.185 1.00 23.16 ? 142 TYR A CD1 1 ATOM 1116 C CD2 . TYR A 1 146 ? 21.940 18.528 25.910 1.00 22.26 ? 142 TYR A CD2 1 ATOM 1117 C CE1 . TYR A 1 146 ? 21.280 16.916 28.091 1.00 21.77 ? 142 TYR A CE1 1 ATOM 1118 C CE2 . TYR A 1 146 ? 22.938 18.109 26.791 1.00 23.06 ? 142 TYR A CE2 1 ATOM 1119 C CZ . TYR A 1 146 ? 22.614 17.298 27.868 1.00 22.18 ? 142 TYR A CZ 1 ATOM 1120 O OH . TYR A 1 146 ? 23.615 16.916 28.764 1.00 21.05 ? 142 TYR A OH 1 ATOM 1121 N N . ALA A 1 147 ? 17.435 19.036 27.838 1.00 19.42 ? 143 ALA A N 1 ATOM 1122 C CA . ALA A 1 147 ? 17.219 19.819 29.070 1.00 18.75 ? 143 ALA A CA 1 ATOM 1123 C C . ALA A 1 147 ? 18.158 19.354 30.147 1.00 19.26 ? 143 ALA A C 1 ATOM 1124 O O . ALA A 1 147 ? 18.329 18.126 30.363 1.00 19.90 ? 143 ALA A O 1 ATOM 1125 C CB . ALA A 1 147 ? 15.763 19.629 29.578 1.00 18.38 ? 143 ALA A CB 1 ATOM 1126 N N . PHE A 1 148 ? 18.782 20.294 30.846 1.00 18.55 ? 144 PHE A N 1 ATOM 1127 C CA . PHE A 1 148 ? 19.712 19.892 31.940 1.00 18.83 ? 144 PHE A CA 1 ATOM 1128 C C . PHE A 1 148 ? 18.905 19.634 33.212 1.00 19.36 ? 144 PHE A C 1 ATOM 1129 O O . PHE A 1 148 ? 19.043 20.387 34.211 1.00 20.11 ? 144 PHE A O 1 ATOM 1130 C CB . PHE A 1 148 ? 20.720 21.052 32.217 1.00 18.41 ? 144 PHE A CB 1 ATOM 1131 C CG . PHE A 1 148 ? 21.618 21.388 31.031 1.00 18.27 ? 144 PHE A CG 1 ATOM 1132 C CD1 . PHE A 1 148 ? 22.326 20.388 30.373 1.00 22.18 ? 144 PHE A CD1 1 ATOM 1133 C CD2 . PHE A 1 148 ? 21.772 22.716 30.616 1.00 20.34 ? 144 PHE A CD2 1 ATOM 1134 C CE1 . PHE A 1 148 ? 23.186 20.698 29.264 1.00 24.06 ? 144 PHE A CE1 1 ATOM 1135 C CE2 . PHE A 1 148 ? 22.613 23.046 29.515 1.00 21.00 ? 144 PHE A CE2 1 ATOM 1136 C CZ . PHE A 1 148 ? 23.334 22.064 28.857 1.00 18.52 ? 144 PHE A CZ 1 ATOM 1137 N N . ALA A 1 149 ? 18.057 18.607 33.182 1.00 19.68 ? 145 ALA A N 1 ATOM 1138 C CA . ALA A 1 149 ? 17.198 18.285 34.301 1.00 20.18 ? 145 ALA A CA 1 ATOM 1139 C C . ALA A 1 149 ? 16.924 16.741 34.235 1.00 20.18 ? 145 ALA A C 1 ATOM 1140 O O . ALA A 1 149 ? 16.849 16.181 33.145 1.00 20.22 ? 145 ALA A O 1 ATOM 1141 C CB . ALA A 1 149 ? 15.843 19.065 34.160 1.00 18.53 ? 145 ALA A CB 1 ATOM 1142 N N . PRO A 1 150 ? 16.634 16.091 35.387 1.00 20.64 ? 146 PRO A N 1 ATOM 1143 C CA . PRO A 1 150 ? 16.378 16.649 36.711 1.00 19.50 ? 146 PRO A CA 1 ATOM 1144 C C . PRO A 1 150 ? 17.622 16.781 37.562 1.00 21.37 ? 146 PRO A C 1 ATOM 1145 O O . PRO A 1 150 ? 18.596 15.945 37.459 1.00 21.33 ? 146 PRO A O 1 ATOM 1146 C CB . PRO A 1 150 ? 15.482 15.597 37.371 1.00 21.42 ? 146 PRO A CB 1 ATOM 1147 C CG . PRO A 1 150 ? 15.956 14.255 36.739 1.00 18.65 ? 146 PRO A CG 1 ATOM 1148 C CD . PRO A 1 150 ? 16.273 14.660 35.292 1.00 19.53 ? 146 PRO A CD 1 ATOM 1149 N N . CYS A 1 151 ? 17.604 17.826 38.397 1.00 20.41 ? 147 CYS A N 1 ATOM 1150 C CA . CYS A 1 151 ? 18.509 17.875 39.538 1.00 21.14 ? 147 CYS A CA 1 ATOM 1151 C C . CYS A 1 151 ? 18.014 16.849 40.556 1.00 22.13 ? 147 CYS A C 1 ATOM 1152 O O . CYS A 1 151 ? 16.886 17.010 41.088 1.00 20.33 ? 147 CYS A O 1 ATOM 1153 C CB . CYS A 1 151 ? 18.495 19.274 40.179 1.00 21.64 ? 147 CYS A CB 1 ATOM 1154 S SG . CYS A 1 151 ? 19.692 19.341 41.601 1.00 23.09 ? 147 CYS A SG 1 ATOM 1155 N N . ILE A 1 152 ? 18.811 15.779 40.764 1.00 21.37 ? 148 ILE A N 1 ATOM 1156 C CA . ILE A 1 152 ? 18.482 14.758 41.770 1.00 21.94 ? 148 ILE A CA 1 ATOM 1157 C C . ILE A 1 152 ? 19.396 14.844 42.998 1.00 22.81 ? 148 ILE A C 1 ATOM 1158 O O . ILE A 1 152 ? 19.659 13.854 43.693 1.00 24.60 ? 148 ILE A O 1 ATOM 1159 C CB . ILE A 1 152 ? 18.455 13.304 41.155 1.00 21.75 ? 148 ILE A CB 1 ATOM 1160 C CG1 . ILE A 1 152 ? 19.772 12.905 40.451 1.00 22.00 ? 148 ILE A CG1 1 ATOM 1161 C CG2 . ILE A 1 152 ? 17.220 13.169 40.174 1.00 21.26 ? 148 ILE A CG2 1 ATOM 1162 C CD1 . ILE A 1 152 ? 19.791 11.297 40.143 1.00 21.17 ? 148 ILE A CD1 1 ATOM 1163 N N . ALA A 1 153 ? 19.877 16.035 43.279 1.00 22.79 ? 149 ALA A N 1 ATOM 1164 C CA . ALA A 1 153 ? 20.560 16.313 44.544 1.00 22.91 ? 149 ALA A CA 1 ATOM 1165 C C . ALA A 1 153 ? 19.638 15.929 45.709 1.00 23.96 ? 149 ALA A C 1 ATOM 1166 O O . ALA A 1 153 ? 18.408 16.067 45.595 1.00 22.07 ? 149 ALA A O 1 ATOM 1167 C CB . ALA A 1 153 ? 20.851 17.805 44.639 1.00 23.12 ? 149 ALA A CB 1 ATOM 1168 N N . VAL A 1 154 ? 20.228 15.460 46.808 1.00 23.06 ? 150 VAL A N 1 ATOM 1169 C CA . VAL A 1 154 ? 19.449 15.210 48.038 1.00 23.75 ? 150 VAL A CA 1 ATOM 1170 C C . VAL A 1 154 ? 19.986 16.262 49.015 1.00 24.46 ? 150 VAL A C 1 ATOM 1171 O O . VAL A 1 154 ? 21.102 16.108 49.547 1.00 25.13 ? 150 VAL A O 1 ATOM 1172 C CB . VAL A 1 154 ? 19.732 13.776 48.578 1.00 24.60 ? 150 VAL A CB 1 ATOM 1173 C CG1 . VAL A 1 154 ? 18.884 13.495 49.885 1.00 23.48 ? 150 VAL A CG1 1 ATOM 1174 C CG2 . VAL A 1 154 ? 19.412 12.724 47.525 1.00 23.35 ? 150 VAL A CG2 1 ATOM 1175 N N . CYS A 1 155 ? 19.287 17.375 49.152 1.00 24.25 ? 151 CYS A N 1 ATOM 1176 C CA . CYS A 1 155 ? 19.819 18.504 49.916 1.00 24.89 ? 151 CYS A CA 1 ATOM 1177 C C . CYS A 1 155 ? 19.716 18.170 51.406 1.00 25.85 ? 151 CYS A C 1 ATOM 1178 O O . CYS A 1 155 ? 18.599 17.960 51.924 1.00 25.31 ? 151 CYS A O 1 ATOM 1179 C CB . CYS A 1 155 ? 18.999 19.758 49.647 1.00 24.27 ? 151 CYS A CB 1 ATOM 1180 S SG . CYS A 1 155 ? 19.379 21.171 50.718 1.00 25.93 ? 151 CYS A SG 1 ATOM 1181 N N . ARG A 1 156 ? 20.865 18.171 52.069 1.00 26.87 ? 152 ARG A N 1 ATOM 1182 C CA . ARG A 1 156 ? 20.984 17.727 53.460 1.00 27.93 ? 152 ARG A CA 1 ATOM 1183 C C . ARG A 1 156 ? 21.149 18.907 54.414 1.00 28.29 ? 152 ARG A C 1 ATOM 1184 O O . ARG A 1 156 ? 21.220 18.718 55.650 1.00 29.81 ? 152 ARG A O 1 ATOM 1185 C CB . ARG A 1 156 ? 22.157 16.716 53.595 1.00 27.50 ? 152 ARG A CB 1 ATOM 1186 C CG . ARG A 1 156 ? 21.971 15.431 52.771 1.00 27.56 ? 152 ARG A CG 1 ATOM 1187 C CD . ARG A 1 156 ? 20.754 14.623 53.257 1.00 29.97 ? 152 ARG A CD 1 ATOM 1188 N NE . ARG A 1 156 ? 21.035 13.928 54.530 1.00 31.21 ? 152 ARG A NE 1 ATOM 1189 C CZ . ARG A 1 156 ? 20.187 13.142 55.211 1.00 31.80 ? 152 ARG A CZ 1 ATOM 1190 N NH1 . ARG A 1 156 ? 20.581 12.562 56.376 1.00 30.64 ? 152 ARG A NH1 1 ATOM 1191 N NH2 . ARG A 1 156 ? 18.956 12.897 54.755 1.00 32.14 ? 152 ARG A NH2 1 ATOM 1192 N N . ASP A 1 157 ? 21.170 20.117 53.847 1.00 27.95 ? 153 ASP A N 1 ATOM 1193 C CA . ASP A 1 157 ? 21.358 21.346 54.617 1.00 28.02 ? 153 ASP A CA 1 ATOM 1194 C C . ASP A 1 157 ? 20.732 22.534 53.845 1.00 26.60 ? 153 ASP A C 1 ATOM 1195 O O . ASP A 1 157 ? 21.275 22.953 52.823 1.00 27.21 ? 153 ASP A O 1 ATOM 1196 C CB . ASP A 1 157 ? 22.866 21.588 54.845 1.00 26.42 ? 153 ASP A CB 1 ATOM 1197 C CG . ASP A 1 157 ? 23.158 22.614 55.957 1.00 32.93 ? 153 ASP A CG 1 ATOM 1198 O OD1 . ASP A 1 157 ? 22.415 23.612 56.063 1.00 29.07 ? 153 ASP A OD1 1 ATOM 1199 O OD2 . ASP A 1 157 ? 24.150 22.418 56.757 1.00 32.62 ? 153 ASP A OD2 1 ATOM 1200 N N . PRO A 1 158 ? 19.611 23.096 54.361 1.00 25.43 ? 154 PRO A N 1 ATOM 1201 C CA . PRO A 1 158 ? 18.849 24.104 53.633 1.00 25.06 ? 154 PRO A CA 1 ATOM 1202 C C . PRO A 1 158 ? 19.612 25.414 53.522 1.00 25.74 ? 154 PRO A C 1 ATOM 1203 O O . PRO A 1 158 ? 19.155 26.320 52.822 1.00 24.72 ? 154 PRO A O 1 ATOM 1204 C CB . PRO A 1 158 ? 17.552 24.256 54.477 1.00 24.47 ? 154 PRO A CB 1 ATOM 1205 C CG . PRO A 1 158 ? 18.062 23.963 55.930 1.00 25.43 ? 154 PRO A CG 1 ATOM 1206 C CD . PRO A 1 158 ? 18.982 22.756 55.661 1.00 25.98 ? 154 PRO A CD 1 ATOM 1207 N N . ARG A 1 159 ? 20.779 25.538 54.195 1.00 25.11 ? 155 ARG A N 1 ATOM 1208 C CA . ARG A 1 159 ? 21.606 26.722 53.938 1.00 25.76 ? 155 ARG A CA 1 ATOM 1209 C C . ARG A 1 159 ? 22.171 26.781 52.505 1.00 25.24 ? 155 ARG A C 1 ATOM 1210 O O . ARG A 1 159 ? 22.637 27.843 52.053 1.00 26.39 ? 155 ARG A O 1 ATOM 1211 C CB . ARG A 1 159 ? 22.735 26.859 55.013 1.00 26.06 ? 155 ARG A CB 1 ATOM 1212 C CG . ARG A 1 159 ? 22.115 27.134 56.420 1.00 25.25 ? 155 ARG A CG 1 ATOM 1213 C CD . ARG A 1 159 ? 23.178 27.012 57.552 1.00 25.69 ? 155 ARG A CD 1 ATOM 1214 N NE . ARG A 1 159 ? 23.625 25.634 57.742 1.00 27.05 ? 155 ARG A NE 1 ATOM 1215 C CZ . ARG A 1 159 ? 24.605 25.294 58.590 1.00 32.84 ? 155 ARG A CZ 1 ATOM 1216 N NH1 . ARG A 1 159 ? 25.170 26.230 59.359 1.00 30.93 ? 155 ARG A NH1 1 ATOM 1217 N NH2 . ARG A 1 159 ? 24.978 24.021 58.715 1.00 29.27 ? 155 ARG A NH2 1 ATOM 1218 N N . TRP A 1 160 ? 22.085 25.674 51.777 1.00 25.60 ? 156 TRP A N 1 ATOM 1219 C CA . TRP A 1 160 ? 22.544 25.636 50.370 1.00 24.83 ? 156 TRP A CA 1 ATOM 1220 C C . TRP A 1 160 ? 21.609 26.483 49.461 1.00 24.38 ? 156 TRP A C 1 ATOM 1221 O O . TRP A 1 160 ? 20.379 26.326 49.526 1.00 23.60 ? 156 TRP A O 1 ATOM 1222 C CB . TRP A 1 160 ? 22.464 24.177 49.884 1.00 25.06 ? 156 TRP A CB 1 ATOM 1223 C CG . TRP A 1 160 ? 23.088 23.895 48.515 1.00 24.60 ? 156 TRP A CG 1 ATOM 1224 C CD1 . TRP A 1 160 ? 24.143 24.553 47.927 1.00 23.36 ? 156 TRP A CD1 1 ATOM 1225 C CD2 . TRP A 1 160 ? 22.713 22.829 47.620 1.00 22.37 ? 156 TRP A CD2 1 ATOM 1226 N NE1 . TRP A 1 160 ? 24.462 23.927 46.707 1.00 26.27 ? 156 TRP A NE1 1 ATOM 1227 C CE2 . TRP A 1 160 ? 23.586 22.887 46.499 1.00 27.57 ? 156 TRP A CE2 1 ATOM 1228 C CE3 . TRP A 1 160 ? 21.703 21.852 47.649 1.00 21.89 ? 156 TRP A CE3 1 ATOM 1229 C CZ2 . TRP A 1 160 ? 23.470 21.995 45.407 1.00 24.31 ? 156 TRP A CZ2 1 ATOM 1230 C CZ3 . TRP A 1 160 ? 21.592 20.964 46.599 1.00 22.80 ? 156 TRP A CZ3 1 ATOM 1231 C CH2 . TRP A 1 160 ? 22.479 21.049 45.479 1.00 22.37 ? 156 TRP A CH2 1 ATOM 1232 N N . GLY A 1 161 ? 22.180 27.325 48.595 1.00 22.65 ? 157 GLY A N 1 ATOM 1233 C CA . GLY A 1 161 ? 21.396 28.153 47.669 1.00 23.49 ? 157 GLY A CA 1 ATOM 1234 C C . GLY A 1 161 ? 20.669 27.396 46.558 1.00 23.80 ? 157 GLY A C 1 ATOM 1235 O O . GLY A 1 161 ? 19.910 28.004 45.818 1.00 24.36 ? 157 GLY A O 1 ATOM 1236 N N . ARG A 1 162 ? 20.880 26.079 46.456 1.00 21.48 ? 158 ARG A N 1 ATOM 1237 C CA . ARG A 1 162 ? 20.135 25.272 45.482 1.00 23.19 ? 158 ARG A CA 1 ATOM 1238 C C . ARG A 1 162 ? 19.220 24.273 46.153 1.00 23.17 ? 158 ARG A C 1 ATOM 1239 O O . ARG A 1 162 ? 18.731 23.368 45.495 1.00 22.80 ? 158 ARG A O 1 ATOM 1240 C CB . ARG A 1 162 ? 21.114 24.498 44.552 1.00 22.73 ? 158 ARG A CB 1 ATOM 1241 C CG . ARG A 1 162 ? 22.193 25.448 43.972 1.00 24.18 ? 158 ARG A CG 1 ATOM 1242 C CD . ARG A 1 162 ? 22.991 24.741 42.875 1.00 24.20 ? 158 ARG A CD 1 ATOM 1243 N NE . ARG A 1 162 ? 22.192 24.692 41.642 1.00 24.11 ? 158 ARG A NE 1 ATOM 1244 C CZ . ARG A 1 162 ? 22.704 24.387 40.446 1.00 26.67 ? 158 ARG A CZ 1 ATOM 1245 N NH1 . ARG A 1 162 ? 24.037 24.143 40.329 1.00 21.09 ? 158 ARG A NH1 1 ATOM 1246 N NH2 . ARG A 1 162 ? 21.911 24.390 39.375 1.00 20.45 ? 158 ARG A NH2 1 ATOM 1247 N N . CYS A 1 163 ? 18.964 24.434 47.455 1.00 23.30 ? 159 CYS A N 1 ATOM 1248 C CA . CYS A 1 163 ? 18.093 23.450 48.146 1.00 24.07 ? 159 CYS A CA 1 ATOM 1249 C C . CYS A 1 163 ? 16.714 23.330 47.471 1.00 23.13 ? 159 CYS A C 1 ATOM 1250 O O . CYS A 1 163 ? 16.123 22.234 47.461 1.00 21.62 ? 159 CYS A O 1 ATOM 1251 C CB . CYS A 1 163 ? 17.948 23.772 49.637 1.00 24.98 ? 159 CYS A CB 1 ATOM 1252 S SG . CYS A 1 163 ? 17.517 22.283 50.646 1.00 29.87 ? 159 CYS A SG 1 ATOM 1253 N N . TYR A 1 164 ? 16.208 24.416 46.861 1.00 21.54 ? 160 TYR A N 1 ATOM 1254 C CA . TYR A 1 164 ? 14.848 24.322 46.232 1.00 20.20 ? 160 TYR A CA 1 ATOM 1255 C C . TYR A 1 164 ? 14.913 23.455 44.979 1.00 21.00 ? 160 TYR A C 1 ATOM 1256 O O . TYR A 1 164 ? 13.856 23.050 44.484 1.00 20.28 ? 160 TYR A O 1 ATOM 1257 C CB . TYR A 1 164 ? 14.286 25.698 45.882 1.00 20.91 ? 160 TYR A CB 1 ATOM 1258 C CG . TYR A 1 164 ? 15.113 26.506 44.857 1.00 22.57 ? 160 TYR A CG 1 ATOM 1259 C CD1 . TYR A 1 164 ? 14.898 26.344 43.491 1.00 20.28 ? 160 TYR A CD1 1 ATOM 1260 C CD2 . TYR A 1 164 ? 16.065 27.428 45.281 1.00 20.78 ? 160 TYR A CD2 1 ATOM 1261 C CE1 . TYR A 1 164 ? 15.619 27.121 42.529 1.00 21.60 ? 160 TYR A CE1 1 ATOM 1262 C CE2 . TYR A 1 164 ? 16.819 28.212 44.348 1.00 23.23 ? 160 TYR A CE2 1 ATOM 1263 C CZ . TYR A 1 164 ? 16.579 28.039 42.981 1.00 23.01 ? 160 TYR A CZ 1 ATOM 1264 O OH . TYR A 1 164 ? 17.273 28.789 42.056 1.00 21.86 ? 160 TYR A OH 1 ATOM 1265 N N . GLU A 1 165 ? 16.140 23.186 44.449 1.00 19.44 ? 161 GLU A N 1 ATOM 1266 C CA . GLU A 1 165 ? 16.248 22.307 43.289 1.00 20.27 ? 161 GLU A CA 1 ATOM 1267 C C . GLU A 1 165 ? 16.282 20.814 43.662 1.00 21.34 ? 161 GLU A C 1 ATOM 1268 O O . GLU A 1 165 ? 16.367 19.919 42.778 1.00 21.78 ? 161 GLU A O 1 ATOM 1269 C CB . GLU A 1 165 ? 17.500 22.633 42.453 1.00 18.85 ? 161 GLU A CB 1 ATOM 1270 C CG . GLU A 1 165 ? 17.420 24.071 41.832 1.00 18.08 ? 161 GLU A CG 1 ATOM 1271 C CD . GLU A 1 165 ? 18.427 24.200 40.683 1.00 23.58 ? 161 GLU A CD 1 ATOM 1272 O OE1 . GLU A 1 165 ? 19.417 24.903 40.896 1.00 23.35 ? 161 GLU A OE1 1 ATOM 1273 O OE2 . GLU A 1 165 ? 18.201 23.600 39.594 1.00 22.98 ? 161 GLU A OE2 1 ATOM 1274 N N . SER A 1 166 ? 16.181 20.552 44.963 1.00 21.50 ? 162 SER A N 1 ATOM 1275 C CA . SER A 1 166 ? 16.123 19.171 45.457 1.00 22.03 ? 162 SER A CA 1 ATOM 1276 C C . SER A 1 166 ? 14.735 18.813 45.880 1.00 21.30 ? 162 SER A C 1 ATOM 1277 O O . SER A 1 166 ? 14.093 19.563 46.606 1.00 21.64 ? 162 SER A O 1 ATOM 1278 C CB . SER A 1 166 ? 17.043 19.043 46.649 1.00 23.05 ? 162 SER A CB 1 ATOM 1279 O OG . SER A 1 166 ? 16.951 17.729 47.223 1.00 24.77 ? 162 SER A OG 1 ATOM 1280 N N . TYR A 1 167 ? 14.227 17.682 45.412 1.00 21.52 ? 163 TYR A N 1 ATOM 1281 C CA . TYR A 1 167 ? 12.853 17.307 45.773 1.00 22.28 ? 163 TYR A CA 1 ATOM 1282 C C . TYR A 1 167 ? 12.734 17.072 47.286 1.00 23.15 ? 163 TYR A C 1 ATOM 1283 O O . TYR A 1 167 ? 11.630 17.230 47.856 1.00 23.47 ? 163 TYR A O 1 ATOM 1284 C CB . TYR A 1 167 ? 12.388 16.013 45.058 1.00 20.00 ? 163 TYR A CB 1 ATOM 1285 C CG . TYR A 1 167 ? 12.398 16.088 43.573 1.00 21.09 ? 163 TYR A CG 1 ATOM 1286 C CD1 . TYR A 1 167 ? 11.334 16.752 42.867 1.00 20.46 ? 163 TYR A CD1 1 ATOM 1287 C CD2 . TYR A 1 167 ? 13.430 15.478 42.837 1.00 21.65 ? 163 TYR A CD2 1 ATOM 1288 C CE1 . TYR A 1 167 ? 11.337 16.816 41.477 1.00 22.31 ? 163 TYR A CE1 1 ATOM 1289 C CE2 . TYR A 1 167 ? 13.426 15.547 41.417 1.00 23.06 ? 163 TYR A CE2 1 ATOM 1290 C CZ . TYR A 1 167 ? 12.397 16.216 40.771 1.00 22.38 ? 163 TYR A CZ 1 ATOM 1291 O OH . TYR A 1 167 ? 12.398 16.292 39.420 1.00 21.19 ? 163 TYR A OH 1 ATOM 1292 N N . SER A 1 168 ? 13.838 16.706 47.946 1.00 22.38 ? 164 SER A N 1 ATOM 1293 C CA . SER A 1 168 ? 13.731 16.277 49.365 1.00 23.41 ? 164 SER A CA 1 ATOM 1294 C C . SER A 1 168 ? 15.055 15.952 50.026 1.00 25.14 ? 164 SER A C 1 ATOM 1295 O O . SER A 1 168 ? 16.033 15.605 49.332 1.00 25.42 ? 164 SER A O 1 ATOM 1296 C CB . SER A 1 168 ? 12.841 15.014 49.456 1.00 24.20 ? 164 SER A CB 1 ATOM 1297 O OG . SER A 1 168 ? 12.652 14.591 50.829 1.00 24.30 ? 164 SER A OG 1 ATOM 1298 N N . GLU A 1 169 ? 15.120 16.043 51.363 1.00 25.07 ? 165 GLU A N 1 ATOM 1299 C CA . GLU A 1 169 ? 16.327 15.572 52.087 1.00 25.30 ? 165 GLU A CA 1 ATOM 1300 C C . GLU A 1 169 ? 16.299 14.046 52.227 1.00 26.25 ? 165 GLU A C 1 ATOM 1301 O O . GLU A 1 169 ? 17.308 13.443 52.610 1.00 26.73 ? 165 GLU A O 1 ATOM 1302 C CB . GLU A 1 169 ? 16.397 16.182 53.493 1.00 27.64 ? 165 GLU A CB 1 ATOM 1303 C CG . GLU A 1 169 ? 15.342 15.562 54.465 1.00 26.42 ? 165 GLU A CG 1 ATOM 1304 C CD . GLU A 1 169 ? 15.097 16.380 55.733 1.00 30.09 ? 165 GLU A CD 1 ATOM 1305 O OE1 . GLU A 1 169 ? 15.202 17.624 55.705 1.00 29.94 ? 165 GLU A OE1 1 ATOM 1306 O OE2 . GLU A 1 169 ? 14.735 15.781 56.772 1.00 30.92 ? 165 GLU A OE2 1 ATOM 1307 N N . ASP A 1 170 ? 15.162 13.430 51.889 1.00 24.93 ? 166 ASP A N 1 ATOM 1308 C CA . ASP A 1 170 ? 15.002 11.987 51.925 1.00 27.13 ? 166 ASP A CA 1 ATOM 1309 C C . ASP A 1 170 ? 15.193 11.441 50.518 1.00 26.33 ? 166 ASP A C 1 ATOM 1310 O O . ASP A 1 170 ? 14.331 11.611 49.652 1.00 25.98 ? 166 ASP A O 1 ATOM 1311 C CB . ASP A 1 170 ? 13.570 11.687 52.380 1.00 27.69 ? 166 ASP A CB 1 ATOM 1312 C CG . ASP A 1 170 ? 13.298 10.194 52.566 1.00 32.83 ? 166 ASP A CG 1 ATOM 1313 O OD1 . ASP A 1 170 ? 14.117 9.363 52.121 1.00 33.26 ? 166 ASP A OD1 1 ATOM 1314 O OD2 . ASP A 1 170 ? 12.265 9.895 53.206 1.00 30.35 ? 166 ASP A OD2 1 ATOM 1315 N N . ARG A 1 171 ? 16.280 10.703 50.311 1.00 25.81 ? 167 ARG A N 1 ATOM 1316 C CA . ARG A 1 171 ? 16.547 10.084 49.013 1.00 26.31 ? 167 ARG A CA 1 ATOM 1317 C C . ARG A 1 171 ? 15.374 9.265 48.460 1.00 26.97 ? 167 ARG A C 1 ATOM 1318 O O . ARG A 1 171 ? 15.207 9.191 47.262 1.00 26.68 ? 167 ARG A O 1 ATOM 1319 C CB . ARG A 1 171 ? 17.870 9.275 49.103 1.00 25.66 ? 167 ARG A CB 1 ATOM 1320 C CG . ARG A 1 171 ? 17.769 8.148 50.167 1.00 29.02 ? 167 ARG A CG 1 ATOM 1321 C CD . ARG A 1 171 ? 17.367 6.832 49.564 1.00 33.52 ? 167 ARG A CD 1 ATOM 1322 N NE . ARG A 1 171 ? 17.230 5.792 50.604 1.00 36.93 ? 167 ARG A NE 1 ATOM 1323 C CZ . ARG A 1 171 ? 16.820 4.538 50.370 1.00 41.52 ? 167 ARG A CZ 1 ATOM 1324 N NH1 . ARG A 1 171 ? 16.736 3.660 51.393 1.00 41.07 ? 167 ARG A NH1 1 ATOM 1325 N NH2 . ARG A 1 171 ? 16.545 4.122 49.121 1.00 34.61 ? 167 ARG A NH2 1 ATOM 1326 N N . ARG A 1 172 ? 14.542 8.637 49.315 1.00 26.97 ? 168 ARG A N 1 ATOM 1327 C CA . ARG A 1 172 ? 13.449 7.879 48.767 1.00 28.13 ? 168 ARG A CA 1 ATOM 1328 C C . ARG A 1 172 ? 12.452 8.762 48.002 1.00 26.82 ? 168 ARG A C 1 ATOM 1329 O O . ARG A 1 172 ? 11.869 8.327 47.027 1.00 25.59 ? 168 ARG A O 1 ATOM 1330 C CB . ARG A 1 172 ? 12.687 7.110 49.865 1.00 29.63 ? 168 ARG A CB 1 ATOM 1331 C CG . ARG A 1 172 ? 13.617 6.225 50.707 1.00 32.23 ? 168 ARG A CG 1 ATOM 1332 C CD . ARG A 1 172 ? 12.828 5.900 52.032 1.00 45.05 ? 168 ARG A CD 1 ATOM 1333 N NE . ARG A 1 172 ? 13.636 5.170 53.004 1.00 51.01 ? 168 ARG A NE 1 ATOM 1334 C CZ . ARG A 1 172 ? 14.498 5.760 53.835 1.00 56.55 ? 168 ARG A CZ 1 ATOM 1335 N NH1 . ARG A 1 172 ? 14.675 7.102 53.784 1.00 53.50 ? 168 ARG A NH1 1 ATOM 1336 N NH2 . ARG A 1 172 ? 15.191 5.014 54.707 1.00 55.41 ? 168 ARG A NH2 1 ATOM 1337 N N . ILE A 1 173 ? 12.267 9.995 48.451 1.00 25.13 ? 169 ILE A N 1 ATOM 1338 C CA . ILE A 1 173 ? 11.379 10.887 47.704 1.00 24.66 ? 169 ILE A CA 1 ATOM 1339 C C . ILE A 1 173 ? 12.018 11.305 46.383 1.00 23.97 ? 169 ILE A C 1 ATOM 1340 O O . ILE A 1 173 ? 11.353 11.296 45.330 1.00 24.57 ? 169 ILE A O 1 ATOM 1341 C CB . ILE A 1 173 ? 10.947 12.102 48.593 1.00 24.03 ? 169 ILE A CB 1 ATOM 1342 C CG1 . ILE A 1 173 ? 10.090 11.550 49.780 1.00 24.86 ? 169 ILE A CG1 1 ATOM 1343 C CG2 . ILE A 1 173 ? 10.133 13.157 47.734 1.00 22.70 ? 169 ILE A CG2 1 ATOM 1344 C CD1 . ILE A 1 173 ? 9.777 12.600 50.874 1.00 23.80 ? 169 ILE A CD1 1 ATOM 1345 N N . VAL A 1 174 ? 13.306 11.646 46.438 1.00 23.84 ? 170 VAL A N 1 ATOM 1346 C CA . VAL A 1 174 ? 14.049 12.019 45.228 1.00 22.70 ? 170 VAL A CA 1 ATOM 1347 C C . VAL A 1 174 ? 13.965 10.852 44.227 1.00 24.67 ? 170 VAL A C 1 ATOM 1348 O O . VAL A 1 174 ? 13.686 11.068 43.064 1.00 23.33 ? 170 VAL A O 1 ATOM 1349 C CB . VAL A 1 174 ? 15.509 12.353 45.585 1.00 23.73 ? 170 VAL A CB 1 ATOM 1350 C CG1 . VAL A 1 174 ? 16.353 12.587 44.301 1.00 20.52 ? 170 VAL A CG1 1 ATOM 1351 C CG2 . VAL A 1 174 ? 15.579 13.625 46.487 1.00 21.40 ? 170 VAL A CG2 1 ATOM 1352 N N . GLN A 1 175 ? 14.218 9.605 44.686 1.00 23.74 ? 171 GLN A N 1 ATOM 1353 C CA . GLN A 1 175 ? 14.094 8.434 43.797 1.00 24.87 ? 171 GLN A CA 1 ATOM 1354 C C . GLN A 1 175 ? 12.710 8.379 43.137 1.00 25.02 ? 171 GLN A C 1 ATOM 1355 O O . GLN A 1 175 ? 12.615 8.106 41.917 1.00 25.93 ? 171 GLN A O 1 ATOM 1356 C CB . GLN A 1 175 ? 14.264 7.113 44.604 1.00 24.52 ? 171 GLN A CB 1 ATOM 1357 C CG . GLN A 1 175 ? 15.748 6.793 44.954 1.00 26.83 ? 171 GLN A CG 1 ATOM 1358 C CD . GLN A 1 175 ? 15.873 5.517 45.751 1.00 29.95 ? 171 GLN A CD 1 ATOM 1359 O OE1 . GLN A 1 175 ? 16.269 4.453 45.224 1.00 31.04 ? 171 GLN A OE1 1 ATOM 1360 N NE2 . GLN A 1 175 ? 15.567 5.615 47.019 1.00 23.17 ? 171 GLN A NE2 1 ATOM 1361 N N . SER A 1 176 ? 11.641 8.535 43.938 1.00 24.04 ? 172 SER A N 1 ATOM 1362 C CA . SER A 1 176 ? 10.292 8.518 43.381 1.00 25.54 ? 172 SER A CA 1 ATOM 1363 C C . SER A 1 176 ? 10.105 9.566 42.267 1.00 24.21 ? 172 SER A C 1 ATOM 1364 O O . SER A 1 176 ? 9.403 9.326 41.288 1.00 24.58 ? 172 SER A O 1 ATOM 1365 C CB . SER A 1 176 ? 9.181 8.643 44.464 1.00 26.82 ? 172 SER A CB 1 ATOM 1366 O OG . SER A 1 176 ? 9.017 9.996 44.947 1.00 28.88 ? 172 SER A OG 1 ATOM 1367 N N . MET A 1 177 ? 10.738 10.717 42.408 1.00 24.36 ? 173 MET A N 1 ATOM 1368 C CA . MET A 1 177 ? 10.510 11.825 41.456 1.00 24.08 ? 173 MET A CA 1 ATOM 1369 C C . MET A 1 177 ? 11.404 11.755 40.185 1.00 24.41 ? 173 MET A C 1 ATOM 1370 O O . MET A 1 177 ? 11.288 12.618 39.280 1.00 22.90 ? 173 MET A O 1 ATOM 1371 C CB . MET A 1 177 ? 10.700 13.179 42.171 1.00 24.38 ? 173 MET A CB 1 ATOM 1372 C CG . MET A 1 177 ? 9.856 13.239 43.430 1.00 24.37 ? 173 MET A CG 1 ATOM 1373 S SD A MET A 1 177 ? 8.120 13.159 42.824 0.60 21.58 ? 173 MET A SD 1 ATOM 1374 S SD B MET A 1 177 ? 8.581 14.334 43.585 0.40 27.78 ? 173 MET A SD 1 ATOM 1375 C CE A MET A 1 177 ? 7.059 13.607 44.197 0.60 22.79 ? 173 MET A CE 1 ATOM 1376 C CE B MET A 1 177 ? 7.476 13.372 44.648 0.40 28.66 ? 173 MET A CE 1 ATOM 1377 N N . THR A 1 178 ? 12.212 10.709 40.092 1.00 23.09 ? 174 THR A N 1 ATOM 1378 C CA . THR A 1 178 ? 12.898 10.429 38.837 1.00 24.66 ? 174 THR A CA 1 ATOM 1379 C C . THR A 1 178 ? 11.937 10.128 37.677 1.00 24.43 ? 174 THR A C 1 ATOM 1380 O O . THR A 1 178 ? 12.390 10.030 36.564 1.00 23.75 ? 174 THR A O 1 ATOM 1381 C CB . THR A 1 178 ? 13.960 9.292 38.960 1.00 24.15 ? 174 THR A CB 1 ATOM 1382 O OG1 . THR A 1 178 ? 13.330 8.110 39.465 1.00 24.33 ? 174 THR A OG1 1 ATOM 1383 C CG2 . THR A 1 178 ? 15.057 9.715 39.938 1.00 22.86 ? 174 THR A CG2 1 ATOM 1384 N N . GLU A 1 179 ? 10.625 10.012 37.962 1.00 23.24 ? 175 GLU A N 1 ATOM 1385 C CA . GLU A 1 179 ? 9.591 9.941 36.928 1.00 22.00 ? 175 GLU A CA 1 ATOM 1386 C C . GLU A 1 179 ? 9.630 11.146 35.995 1.00 22.64 ? 175 GLU A C 1 ATOM 1387 O O . GLU A 1 179 ? 9.113 11.065 34.860 1.00 23.32 ? 175 GLU A O 1 ATOM 1388 C CB . GLU A 1 179 ? 8.207 9.849 37.584 1.00 22.29 ? 175 GLU A CB 1 ATOM 1389 C CG . GLU A 1 179 ? 7.925 8.401 38.140 1.00 23.78 ? 175 GLU A CG 1 ATOM 1390 C CD . GLU A 1 179 ? 7.924 7.361 37.006 1.00 30.60 ? 175 GLU A CD 1 ATOM 1391 O OE1 . GLU A 1 179 ? 8.945 6.722 36.848 1.00 30.83 ? 175 GLU A OE1 1 ATOM 1392 O OE2 . GLU A 1 179 ? 6.958 7.248 36.216 1.00 30.04 ? 175 GLU A OE2 1 ATOM 1393 N N . LEU A 1 180 ? 10.232 12.251 36.440 1.00 20.02 ? 176 LEU A N 1 ATOM 1394 C CA . LEU A 1 180 ? 10.419 13.373 35.485 1.00 21.00 ? 176 LEU A CA 1 ATOM 1395 C C . LEU A 1 180 ? 11.090 12.869 34.171 1.00 20.74 ? 176 LEU A C 1 ATOM 1396 O O . LEU A 1 180 ? 10.786 13.326 33.045 1.00 20.41 ? 176 LEU A O 1 ATOM 1397 C CB . LEU A 1 180 ? 11.313 14.460 36.101 1.00 20.39 ? 176 LEU A CB 1 ATOM 1398 C CG . LEU A 1 180 ? 11.331 15.743 35.205 1.00 21.48 ? 176 LEU A CG 1 ATOM 1399 C CD1 . LEU A 1 180 ? 10.092 16.651 35.487 1.00 21.06 ? 176 LEU A CD1 1 ATOM 1400 C CD2 . LEU A 1 180 ? 12.661 16.542 35.427 1.00 18.56 ? 176 LEU A CD2 1 ATOM 1401 N N . ILE A 1 181 ? 12.037 11.950 34.341 1.00 20.70 ? 177 ILE A N 1 ATOM 1402 C CA . ILE A 1 181 ? 12.891 11.497 33.208 1.00 21.05 ? 177 ILE A CA 1 ATOM 1403 C C . ILE A 1 181 ? 12.086 10.880 32.041 1.00 21.83 ? 177 ILE A C 1 ATOM 1404 O O . ILE A 1 181 ? 12.221 11.353 30.909 1.00 22.92 ? 177 ILE A O 1 ATOM 1405 C CB . ILE A 1 181 ? 14.046 10.586 33.698 1.00 20.36 ? 177 ILE A CB 1 ATOM 1406 C CG1 . ILE A 1 181 ? 15.065 11.441 34.477 1.00 21.01 ? 177 ILE A CG1 1 ATOM 1407 C CG2 . ILE A 1 181 ? 14.781 9.845 32.481 1.00 22.62 ? 177 ILE A CG2 1 ATOM 1408 C CD1 . ILE A 1 181 ? 16.013 10.607 35.402 1.00 21.15 ? 177 ILE A CD1 1 ATOM 1409 N N . PRO A 1 182 ? 11.247 9.830 32.295 1.00 22.86 ? 178 PRO A N 1 ATOM 1410 C CA . PRO A 1 182 ? 10.422 9.333 31.188 1.00 22.55 ? 178 PRO A CA 1 ATOM 1411 C C . PRO A 1 182 ? 9.315 10.314 30.797 1.00 22.23 ? 178 PRO A C 1 ATOM 1412 O O . PRO A 1 182 ? 8.737 10.165 29.711 1.00 24.13 ? 178 PRO A O 1 ATOM 1413 C CB . PRO A 1 182 ? 9.857 7.993 31.724 1.00 25.24 ? 178 PRO A CB 1 ATOM 1414 C CG . PRO A 1 182 ? 9.811 8.210 33.232 1.00 23.41 ? 178 PRO A CG 1 ATOM 1415 C CD . PRO A 1 182 ? 11.132 8.945 33.475 1.00 21.90 ? 178 PRO A CD 1 ATOM 1416 N N . GLY A 1 183 ? 9.024 11.334 31.616 1.00 21.95 ? 179 GLY A N 1 ATOM 1417 C CA . GLY A 1 183 ? 8.125 12.397 31.138 1.00 22.14 ? 179 GLY A CA 1 ATOM 1418 C C . GLY A 1 183 ? 8.870 13.214 30.046 1.00 21.43 ? 179 GLY A C 1 ATOM 1419 O O . GLY A 1 183 ? 8.344 13.451 28.936 1.00 22.44 ? 179 GLY A O 1 ATOM 1420 N N . LEU A 1 184 ? 10.102 13.609 30.335 1.00 20.13 ? 180 LEU A N 1 ATOM 1421 C CA . LEU A 1 184 ? 10.890 14.432 29.371 1.00 19.97 ? 180 LEU A CA 1 ATOM 1422 C C . LEU A 1 184 ? 11.247 13.617 28.117 1.00 21.15 ? 180 LEU A C 1 ATOM 1423 O O . LEU A 1 184 ? 11.185 14.144 26.980 1.00 20.51 ? 180 LEU A O 1 ATOM 1424 C CB . LEU A 1 184 ? 12.219 14.924 29.999 1.00 19.01 ? 180 LEU A CB 1 ATOM 1425 C CG . LEU A 1 184 ? 12.061 16.011 31.089 1.00 20.48 ? 180 LEU A CG 1 ATOM 1426 C CD1 . LEU A 1 184 ? 13.369 16.119 31.896 1.00 18.60 ? 180 LEU A CD1 1 ATOM 1427 C CD2 . LEU A 1 184 ? 11.717 17.401 30.405 1.00 16.71 ? 180 LEU A CD2 1 ATOM 1428 N N . GLN A 1 185 ? 11.666 12.380 28.340 1.00 20.06 ? 181 GLN A N 1 ATOM 1429 C CA . GLN A 1 185 ? 12.265 11.544 27.259 1.00 21.31 ? 181 GLN A CA 1 ATOM 1430 C C . GLN A 1 185 ? 11.288 10.583 26.574 1.00 22.49 ? 181 GLN A C 1 ATOM 1431 O O . GLN A 1 185 ? 11.536 10.149 25.447 1.00 22.18 ? 181 GLN A O 1 ATOM 1432 C CB . GLN A 1 185 ? 13.384 10.672 27.854 1.00 21.22 ? 181 GLN A CB 1 ATOM 1433 C CG . GLN A 1 185 ? 14.555 11.538 28.417 1.00 21.02 ? 181 GLN A CG 1 ATOM 1434 C CD . GLN A 1 185 ? 15.811 10.674 28.711 1.00 24.25 ? 181 GLN A CD 1 ATOM 1435 O OE1 . GLN A 1 185 ? 15.711 9.495 29.196 1.00 26.16 ? 181 GLN A OE1 1 ATOM 1436 N NE2 . GLN A 1 185 ? 16.963 11.220 28.415 1.00 17.75 ? 181 GLN A NE2 1 ATOM 1437 N N . GLY A 1 186 ? 10.189 10.260 27.238 1.00 22.85 ? 182 GLY A N 1 ATOM 1438 C CA . GLY A 1 186 ? 9.376 9.109 26.819 1.00 23.88 ? 182 GLY A CA 1 ATOM 1439 C C . GLY A 1 186 ? 9.698 7.875 27.671 1.00 25.86 ? 182 GLY A C 1 ATOM 1440 O O . GLY A 1 186 ? 10.810 7.720 28.183 1.00 24.75 ? 182 GLY A O 1 ATOM 1441 N N . ASP A 1 187 ? 8.718 6.976 27.800 1.00 25.92 ? 183 ASP A N 1 ATOM 1442 C CA . ASP A 1 187 ? 8.886 5.703 28.508 1.00 27.58 ? 183 ASP A CA 1 ATOM 1443 C C . ASP A 1 187 ? 9.809 4.780 27.747 1.00 27.32 ? 183 ASP A C 1 ATOM 1444 O O . ASP A 1 187 ? 9.753 4.722 26.524 1.00 27.44 ? 183 ASP A O 1 ATOM 1445 C CB . ASP A 1 187 ? 7.504 4.994 28.666 1.00 29.21 ? 183 ASP A CB 1 ATOM 1446 C CG . ASP A 1 187 ? 6.610 5.686 29.692 1.00 29.81 ? 183 ASP A CG 1 ATOM 1447 O OD1 . ASP A 1 187 ? 7.066 5.967 30.778 1.00 33.61 ? 183 ASP A OD1 1 ATOM 1448 O OD2 . ASP A 1 187 ? 5.435 5.885 29.441 1.00 39.87 ? 183 ASP A OD2 1 ATOM 1449 N N . VAL A 1 188 ? 10.646 4.037 28.455 1.00 28.65 ? 184 VAL A N 1 ATOM 1450 C CA . VAL A 1 188 ? 11.585 3.131 27.796 1.00 31.01 ? 184 VAL A CA 1 ATOM 1451 C C . VAL A 1 188 ? 10.827 1.855 27.401 1.00 33.73 ? 184 VAL A C 1 ATOM 1452 O O . VAL A 1 188 ? 9.803 1.555 27.990 1.00 33.71 ? 184 VAL A O 1 ATOM 1453 C CB . VAL A 1 188 ? 12.834 2.817 28.682 1.00 31.18 ? 184 VAL A CB 1 ATOM 1454 C CG1 . VAL A 1 188 ? 13.557 4.146 29.033 1.00 30.18 ? 184 VAL A CG1 1 ATOM 1455 C CG2 . VAL A 1 188 ? 12.456 2.006 29.986 1.00 31.53 ? 184 VAL A CG2 1 ATOM 1456 N N . PRO A 1 189 ? 11.288 1.151 26.379 1.00 36.57 ? 185 PRO A N 1 ATOM 1457 C CA . PRO A 1 189 ? 10.453 0.014 25.996 1.00 40.49 ? 185 PRO A CA 1 ATOM 1458 C C . PRO A 1 189 ? 10.547 -1.203 26.972 1.00 43.10 ? 185 PRO A C 1 ATOM 1459 O O . PRO A 1 189 ? 11.348 -1.195 27.906 1.00 41.79 ? 185 PRO A O 1 ATOM 1460 C CB . PRO A 1 189 ? 10.920 -0.267 24.565 1.00 40.73 ? 185 PRO A CB 1 ATOM 1461 C CG . PRO A 1 189 ? 12.345 0.086 24.561 1.00 39.37 ? 185 PRO A CG 1 ATOM 1462 C CD . PRO A 1 189 ? 12.400 1.365 25.442 1.00 36.23 ? 185 PRO A CD 1 ATOM 1463 N N . LYS A 1 190 ? 9.720 -2.234 26.771 1.00 47.31 ? 186 LYS A N 1 ATOM 1464 C CA . LYS A 1 190 ? 9.586 -3.334 27.771 1.00 49.92 ? 186 LYS A CA 1 ATOM 1465 C C . LYS A 1 190 ? 10.898 -3.999 28.231 1.00 50.35 ? 186 LYS A C 1 ATOM 1466 O O . LYS A 1 190 ? 11.062 -4.323 29.415 1.00 51.67 ? 186 LYS A O 1 ATOM 1467 C CB . LYS A 1 190 ? 8.632 -4.435 27.271 1.00 52.15 ? 186 LYS A CB 1 ATOM 1468 C CG . LYS A 1 190 ? 8.451 -4.481 25.736 1.00 56.86 ? 186 LYS A CG 1 ATOM 1469 C CD . LYS A 1 190 ? 7.061 -3.888 25.336 1.00 62.65 ? 186 LYS A CD 1 ATOM 1470 C CE . LYS A 1 190 ? 7.091 -3.126 23.992 1.00 64.92 ? 186 LYS A CE 1 ATOM 1471 N NZ . LYS A 1 190 ? 7.751 -1.762 24.064 1.00 62.87 ? 186 LYS A NZ 1 ATOM 1472 N N . ASP A 1 191 ? 11.823 -4.193 27.316 1.00 49.49 ? 187 ASP A N 1 ATOM 1473 C CA . ASP A 1 191 ? 12.973 -5.066 27.594 1.00 51.34 ? 187 ASP A CA 1 ATOM 1474 C C . ASP A 1 191 ? 14.253 -4.235 27.784 1.00 48.76 ? 187 ASP A C 1 ATOM 1475 O O . ASP A 1 191 ? 15.346 -4.683 27.461 1.00 49.92 ? 187 ASP A O 1 ATOM 1476 C CB . ASP A 1 191 ? 13.185 -5.948 26.361 1.00 53.02 ? 187 ASP A CB 1 ATOM 1477 C CG . ASP A 1 191 ? 13.516 -5.106 25.117 1.00 57.81 ? 187 ASP A CG 1 ATOM 1478 O OD1 . ASP A 1 191 ? 12.948 -3.983 25.014 1.00 62.80 ? 187 ASP A OD1 1 ATOM 1479 O OD2 . ASP A 1 191 ? 14.356 -5.535 24.279 1.00 63.89 ? 187 ASP A OD2 1 ATOM 1480 N N . PHE A 1 192 ? 14.088 -3.011 28.261 1.00 45.84 ? 188 PHE A N 1 ATOM 1481 C CA . PHE A 1 192 ? 15.120 -2.011 28.208 1.00 40.84 ? 188 PHE A CA 1 ATOM 1482 C C . PHE A 1 192 ? 16.297 -2.344 29.102 1.00 39.38 ? 188 PHE A C 1 ATOM 1483 O O . PHE A 1 192 ? 16.091 -2.640 30.278 1.00 39.45 ? 188 PHE A O 1 ATOM 1484 C CB . PHE A 1 192 ? 14.533 -0.672 28.677 1.00 40.43 ? 188 PHE A CB 1 ATOM 1485 C CG . PHE A 1 192 ? 15.482 0.466 28.480 1.00 36.73 ? 188 PHE A CG 1 ATOM 1486 C CD1 . PHE A 1 192 ? 15.747 0.910 27.198 1.00 37.67 ? 188 PHE A CD1 1 ATOM 1487 C CD2 . PHE A 1 192 ? 16.120 1.057 29.555 1.00 34.90 ? 188 PHE A CD2 1 ATOM 1488 C CE1 . PHE A 1 192 ? 16.619 1.990 26.964 1.00 35.46 ? 188 PHE A CE1 1 ATOM 1489 C CE2 . PHE A 1 192 ? 17.031 2.120 29.346 1.00 30.46 ? 188 PHE A CE2 1 ATOM 1490 C CZ . PHE A 1 192 ? 17.270 2.573 28.032 1.00 32.03 ? 188 PHE A CZ 1 ATOM 1491 N N . THR A 1 193 ? 17.523 -2.230 28.594 1.00 36.20 ? 189 THR A N 1 ATOM 1492 C CA . THR A 1 193 ? 18.690 -2.447 29.463 1.00 35.55 ? 189 THR A CA 1 ATOM 1493 C C . THR A 1 193 ? 19.073 -1.222 30.334 1.00 34.20 ? 189 THR A C 1 ATOM 1494 O O . THR A 1 193 ? 19.412 -0.160 29.777 1.00 32.06 ? 189 THR A O 1 ATOM 1495 C CB . THR A 1 193 ? 19.911 -2.862 28.644 1.00 35.96 ? 189 THR A CB 1 ATOM 1496 O OG1 . THR A 1 193 ? 19.593 -4.050 27.915 1.00 37.43 ? 189 THR A OG1 1 ATOM 1497 C CG2 . THR A 1 193 ? 21.115 -3.108 29.554 1.00 35.45 ? 189 THR A CG2 1 ATOM 1498 N N . SER A 1 194 ? 19.044 -1.368 31.665 1.00 32.58 ? 190 SER A N 1 ATOM 1499 C CA . SER A 1 194 ? 19.368 -0.237 32.572 1.00 32.13 ? 190 SER A CA 1 ATOM 1500 C C . SER A 1 194 ? 20.725 0.394 32.185 1.00 32.08 ? 190 SER A C 1 ATOM 1501 O O . SER A 1 194 ? 21.714 -0.343 31.977 1.00 30.33 ? 190 SER A O 1 ATOM 1502 C CB . SER A 1 194 ? 19.472 -0.696 34.013 1.00 32.62 ? 190 SER A CB 1 ATOM 1503 O OG . SER A 1 194 ? 19.777 0.394 34.871 1.00 31.27 ? 190 SER A OG 1 ATOM 1504 N N . GLY A 1 195 ? 20.768 1.732 32.082 1.00 29.20 ? 191 GLY A N 1 ATOM 1505 C CA . GLY A 1 195 ? 22.023 2.427 31.755 1.00 28.62 ? 191 GLY A CA 1 ATOM 1506 C C . GLY A 1 195 ? 22.126 2.856 30.298 1.00 27.88 ? 191 GLY A C 1 ATOM 1507 O O . GLY A 1 195 ? 22.898 3.732 29.991 1.00 26.69 ? 191 GLY A O 1 ATOM 1508 N N . MET A 1 196 ? 21.307 2.284 29.412 1.00 27.51 ? 192 MET A N 1 ATOM 1509 C CA . MET A 1 196 ? 21.252 2.762 28.000 1.00 27.84 ? 192 MET A CA 1 ATOM 1510 C C . MET A 1 196 ? 20.508 4.103 27.922 1.00 25.80 ? 192 MET A C 1 ATOM 1511 O O . MET A 1 196 ? 19.586 4.348 28.725 1.00 28.15 ? 192 MET A O 1 ATOM 1512 C CB . MET A 1 196 ? 20.568 1.720 27.077 1.00 26.43 ? 192 MET A CB 1 ATOM 1513 C CG . MET A 1 196 ? 21.463 0.439 26.858 1.00 29.01 ? 192 MET A CG 1 ATOM 1514 S SD . MET A 1 196 ? 22.920 0.808 25.849 1.00 33.99 ? 192 MET A SD 1 ATOM 1515 C CE . MET A 1 196 ? 22.188 0.872 24.225 1.00 29.75 ? 192 MET A CE 1 ATOM 1516 N N . PRO A 1 197 ? 20.870 4.950 26.957 1.00 25.67 ? 193 PRO A N 1 ATOM 1517 C CA . PRO A 1 197 ? 20.203 6.269 26.878 1.00 24.54 ? 193 PRO A CA 1 ATOM 1518 C C . PRO A 1 197 ? 18.945 6.055 26.052 1.00 25.63 ? 193 PRO A C 1 ATOM 1519 O O . PRO A 1 197 ? 18.902 5.107 25.255 1.00 25.10 ? 193 PRO A O 1 ATOM 1520 C CB . PRO A 1 197 ? 21.246 7.135 26.126 1.00 23.21 ? 193 PRO A CB 1 ATOM 1521 C CG . PRO A 1 197 ? 22.010 6.056 25.195 1.00 25.61 ? 193 PRO A CG 1 ATOM 1522 C CD . PRO A 1 197 ? 22.122 4.868 26.120 1.00 23.80 ? 193 PRO A CD 1 ATOM 1523 N N . PHE A 1 198 ? 17.923 6.890 26.214 1.00 23.30 ? 194 PHE A N 1 ATOM 1524 C CA . PHE A 1 198 ? 16.683 6.746 25.459 1.00 25.28 ? 194 PHE A CA 1 ATOM 1525 C C . PHE A 1 198 ? 16.027 8.097 25.293 1.00 25.21 ? 194 PHE A C 1 ATOM 1526 O O . PHE A 1 198 ? 15.951 8.846 26.270 1.00 24.73 ? 194 PHE A O 1 ATOM 1527 C CB . PHE A 1 198 ? 15.642 5.897 26.235 1.00 25.08 ? 194 PHE A CB 1 ATOM 1528 C CG . PHE A 1 198 ? 14.356 5.733 25.477 1.00 27.80 ? 194 PHE A CG 1 ATOM 1529 C CD1 . PHE A 1 198 ? 14.281 4.808 24.418 1.00 29.51 ? 194 PHE A CD1 1 ATOM 1530 C CD2 . PHE A 1 198 ? 13.240 6.525 25.775 1.00 27.37 ? 194 PHE A CD2 1 ATOM 1531 C CE1 . PHE A 1 198 ? 13.091 4.671 23.688 1.00 32.76 ? 194 PHE A CE1 1 ATOM 1532 C CE2 . PHE A 1 198 ? 12.018 6.377 25.062 1.00 27.25 ? 194 PHE A CE2 1 ATOM 1533 C CZ . PHE A 1 198 ? 11.948 5.464 24.014 1.00 27.86 ? 194 PHE A CZ 1 ATOM 1534 N N . VAL A 1 199 ? 15.557 8.398 24.085 1.00 24.35 ? 195 VAL A N 1 ATOM 1535 C CA . VAL A 1 199 ? 14.618 9.524 23.859 1.00 23.59 ? 195 VAL A CA 1 ATOM 1536 C C . VAL A 1 199 ? 13.673 9.026 22.764 1.00 24.83 ? 195 VAL A C 1 ATOM 1537 O O . VAL A 1 199 ? 14.139 8.438 21.779 1.00 22.79 ? 195 VAL A O 1 ATOM 1538 C CB . VAL A 1 199 ? 15.300 10.826 23.385 1.00 24.33 ? 195 VAL A CB 1 ATOM 1539 C CG1 . VAL A 1 199 ? 14.244 11.949 23.120 1.00 19.76 ? 195 VAL A CG1 1 ATOM 1540 C CG2 . VAL A 1 199 ? 16.377 11.299 24.417 1.00 22.04 ? 195 VAL A CG2 1 ATOM 1541 N N . ALA A 1 200 ? 12.370 9.246 22.921 1.00 25.12 ? 196 ALA A N 1 ATOM 1542 C CA . ALA A 1 200 ? 11.418 8.595 22.015 1.00 26.86 ? 196 ALA A CA 1 ATOM 1543 C C . ALA A 1 200 ? 11.458 9.123 20.578 1.00 28.56 ? 196 ALA A C 1 ATOM 1544 O O . ALA A 1 200 ? 11.215 8.342 19.609 1.00 29.73 ? 196 ALA A O 1 ATOM 1545 C CB . ALA A 1 200 ? 9.982 8.627 22.573 1.00 27.46 ? 196 ALA A CB 1 ATOM 1546 N N . GLY A 1 201 ? 11.760 10.413 20.416 1.00 27.60 ? 197 GLY A N 1 ATOM 1547 C CA . GLY A 1 201 ? 11.607 11.068 19.108 1.00 27.43 ? 197 GLY A CA 1 ATOM 1548 C C . GLY A 1 201 ? 11.554 12.588 19.221 1.00 27.77 ? 197 GLY A C 1 ATOM 1549 O O . GLY A 1 201 ? 11.903 13.163 20.274 1.00 25.56 ? 197 GLY A O 1 ATOM 1550 N N . LYS A 1 202 ? 11.054 13.236 18.167 1.00 27.22 ? 198 LYS A N 1 ATOM 1551 C CA . LYS A 1 202 ? 11.249 14.677 17.987 1.00 25.85 ? 198 LYS A CA 1 ATOM 1552 C C . LYS A 1 202 ? 10.346 15.510 18.903 1.00 26.70 ? 198 LYS A C 1 ATOM 1553 O O . LYS A 1 202 ? 10.527 16.746 19.006 1.00 27.94 ? 198 LYS A O 1 ATOM 1554 C CB . LYS A 1 202 ? 11.008 15.046 16.515 1.00 26.51 ? 198 LYS A CB 1 ATOM 1555 C CG . LYS A 1 202 ? 9.499 14.814 16.102 1.00 25.40 ? 198 LYS A CG 1 ATOM 1556 C CD . LYS A 1 202 ? 9.299 15.056 14.628 1.00 29.24 ? 198 LYS A CD 1 ATOM 1557 C CE . LYS A 1 202 ? 7.772 15.080 14.395 1.00 37.17 ? 198 LYS A CE 1 ATOM 1558 N NZ . LYS A 1 202 ? 7.581 15.377 12.972 1.00 42.19 ? 198 LYS A NZ 1 ATOM 1559 N N . ASN A 1 203 ? 9.390 14.865 19.573 1.00 24.91 ? 199 ASN A N 1 ATOM 1560 C CA . ASN A 1 203 ? 8.507 15.559 20.486 1.00 25.44 ? 199 ASN A CA 1 ATOM 1561 C C . ASN A 1 203 ? 8.943 15.398 21.938 1.00 24.30 ? 199 ASN A C 1 ATOM 1562 O O . ASN A 1 203 ? 8.285 15.910 22.875 1.00 23.19 ? 199 ASN A O 1 ATOM 1563 C CB . ASN A 1 203 ? 7.040 15.096 20.295 1.00 27.46 ? 199 ASN A CB 1 ATOM 1564 C CG . ASN A 1 203 ? 6.537 15.337 18.859 1.00 33.31 ? 199 ASN A CG 1 ATOM 1565 O OD1 . ASN A 1 203 ? 6.097 14.390 18.167 1.00 43.58 ? 199 ASN A OD1 1 ATOM 1566 N ND2 . ASN A 1 203 ? 6.642 16.561 18.394 1.00 29.49 ? 199 ASN A ND2 1 ATOM 1567 N N . LYS A 1 204 ? 10.082 14.722 22.120 1.00 23.25 ? 200 LYS A N 1 ATOM 1568 C CA . LYS A 1 204 ? 10.715 14.552 23.452 1.00 22.83 ? 200 LYS A CA 1 ATOM 1569 C C . LYS A 1 204 ? 12.124 15.178 23.451 1.00 22.92 ? 200 LYS A C 1 ATOM 1570 O O . LYS A 1 204 ? 12.621 15.641 22.399 1.00 23.75 ? 200 LYS A O 1 ATOM 1571 C CB . LYS A 1 204 ? 10.798 13.027 23.787 1.00 22.47 ? 200 LYS A CB 1 ATOM 1572 C CG . LYS A 1 204 ? 9.308 12.400 23.856 1.00 24.46 ? 200 LYS A CG 1 ATOM 1573 C CD . LYS A 1 204 ? 8.599 12.950 25.139 1.00 25.18 ? 200 LYS A CD 1 ATOM 1574 C CE . LYS A 1 204 ? 7.308 12.161 25.464 1.00 28.62 ? 200 LYS A CE 1 ATOM 1575 N NZ . LYS A 1 204 ? 6.630 12.747 26.706 1.00 24.57 ? 200 LYS A NZ 1 ATOM 1576 N N . VAL A 1 205 ? 12.751 15.207 24.622 1.00 21.99 ? 201 VAL A N 1 ATOM 1577 C CA . VAL A 1 205 ? 14.093 15.800 24.775 1.00 21.06 ? 201 VAL A CA 1 ATOM 1578 C C . VAL A 1 205 ? 14.965 14.849 25.554 1.00 20.83 ? 201 VAL A C 1 ATOM 1579 O O . VAL A 1 205 ? 14.476 14.025 26.321 1.00 20.34 ? 201 VAL A O 1 ATOM 1580 C CB . VAL A 1 205 ? 14.075 17.207 25.496 1.00 21.10 ? 201 VAL A CB 1 ATOM 1581 C CG1 . VAL A 1 205 ? 13.213 18.267 24.683 1.00 20.08 ? 201 VAL A CG1 1 ATOM 1582 C CG2 . VAL A 1 205 ? 13.569 17.096 26.960 1.00 19.49 ? 201 VAL A CG2 1 ATOM 1583 N N . ALA A 1 206 ? 16.265 14.905 25.301 1.00 19.86 ? 202 ALA A N 1 ATOM 1584 C CA . ALA A 1 206 ? 17.244 14.231 26.167 1.00 20.35 ? 202 ALA A CA 1 ATOM 1585 C C . ALA A 1 206 ? 17.216 14.915 27.520 1.00 20.34 ? 202 ALA A C 1 ATOM 1586 O O . ALA A 1 206 ? 17.131 16.145 27.580 1.00 18.90 ? 202 ALA A O 1 ATOM 1587 C CB . ALA A 1 206 ? 18.664 14.388 25.570 1.00 20.41 ? 202 ALA A CB 1 ATOM 1588 N N . ALA A 1 207 ? 17.316 14.116 28.590 1.00 19.91 ? 203 ALA A N 1 ATOM 1589 C CA . ALA A 1 207 ? 17.331 14.587 29.963 1.00 20.09 ? 203 ALA A CA 1 ATOM 1590 C C . ALA A 1 207 ? 18.764 14.480 30.501 1.00 21.12 ? 203 ALA A C 1 ATOM 1591 O O . ALA A 1 207 ? 19.669 14.013 29.798 1.00 20.82 ? 203 ALA A O 1 ATOM 1592 C CB . ALA A 1 207 ? 16.322 13.751 30.881 1.00 19.16 ? 203 ALA A CB 1 ATOM 1593 N N . CYS A 1 208 ? 18.966 14.953 31.732 1.00 20.49 ? 204 CYS A N 1 ATOM 1594 C CA . CYS A 1 208 ? 20.311 15.012 32.347 1.00 22.00 ? 204 CYS A CA 1 ATOM 1595 C C . CYS A 1 208 ? 20.150 14.870 33.860 1.00 22.28 ? 204 CYS A C 1 ATOM 1596 O O . CYS A 1 208 ? 19.652 15.798 34.498 1.00 22.05 ? 204 CYS A O 1 ATOM 1597 C CB . CYS A 1 208 ? 20.949 16.392 32.065 1.00 21.57 ? 204 CYS A CB 1 ATOM 1598 S SG . CYS A 1 208 ? 22.616 16.587 32.775 1.00 23.45 ? 204 CYS A SG 1 ATOM 1599 N N . ALA A 1 209 ? 20.582 13.749 34.435 1.00 22.58 ? 205 ALA A N 1 ATOM 1600 C CA . ALA A 1 209 ? 20.537 13.603 35.884 1.00 22.70 ? 205 ALA A CA 1 ATOM 1601 C C . ALA A 1 209 ? 21.750 14.378 36.447 1.00 22.69 ? 205 ALA A C 1 ATOM 1602 O O . ALA A 1 209 ? 22.920 14.108 36.067 1.00 23.12 ? 205 ALA A O 1 ATOM 1603 C CB . ALA A 1 209 ? 20.595 12.087 36.295 1.00 23.04 ? 205 ALA A CB 1 ATOM 1604 N N . LYS A 1 210 ? 21.519 15.332 37.347 1.00 21.81 ? 206 LYS A N 1 ATOM 1605 C CA . LYS A 1 210 ? 22.639 16.143 37.820 1.00 21.09 ? 206 LYS A CA 1 ATOM 1606 C C . LYS A 1 210 ? 22.496 16.447 39.335 1.00 22.06 ? 206 LYS A C 1 ATOM 1607 O O . LYS A 1 210 ? 21.410 16.330 39.886 1.00 23.42 ? 206 LYS A O 1 ATOM 1608 C CB . LYS A 1 210 ? 22.706 17.437 36.971 1.00 21.80 ? 206 LYS A CB 1 ATOM 1609 C CG . LYS A 1 210 ? 21.577 18.474 37.368 1.00 18.76 ? 206 LYS A CG 1 ATOM 1610 C CD . LYS A 1 210 ? 21.596 19.634 36.328 1.00 19.48 ? 206 LYS A CD 1 ATOM 1611 C CE . LYS A 1 210 ? 20.703 20.816 36.819 1.00 22.81 ? 206 LYS A CE 1 ATOM 1612 N NZ . LYS A 1 210 ? 20.751 21.983 35.852 1.00 21.82 ? 206 LYS A NZ 1 ATOM 1613 N N . HIS A 1 211 ? 23.571 16.814 40.043 1.00 21.94 ? 207 HIS A N 1 ATOM 1614 C CA . HIS A 1 211 ? 24.946 16.858 39.552 1.00 22.13 ? 207 HIS A CA 1 ATOM 1615 C C . HIS A 1 211 ? 25.703 15.744 40.316 1.00 23.16 ? 207 HIS A C 1 ATOM 1616 O O . HIS A 1 211 ? 25.644 15.664 41.542 1.00 24.05 ? 207 HIS A O 1 ATOM 1617 C CB . HIS A 1 211 ? 25.633 18.212 39.852 1.00 21.42 ? 207 HIS A CB 1 ATOM 1618 C CG . HIS A 1 211 ? 24.791 19.411 39.521 1.00 21.14 ? 207 HIS A CG 1 ATOM 1619 N ND1 . HIS A 1 211 ? 23.805 19.872 40.367 1.00 22.19 ? 207 HIS A ND1 1 ATOM 1620 C CD2 . HIS A 1 211 ? 24.803 20.258 38.453 1.00 21.45 ? 207 HIS A CD2 1 ATOM 1621 C CE1 . HIS A 1 211 ? 23.233 20.951 39.834 1.00 23.04 ? 207 HIS A CE1 1 ATOM 1622 N NE2 . HIS A 1 211 ? 23.794 21.186 38.656 1.00 20.87 ? 207 HIS A NE2 1 ATOM 1623 N N . PHE A 1 212 ? 26.375 14.893 39.562 1.00 22.58 ? 208 PHE A N 1 ATOM 1624 C CA . PHE A 1 212 ? 26.943 13.635 40.060 1.00 23.50 ? 208 PHE A CA 1 ATOM 1625 C C . PHE A 1 212 ? 28.270 13.979 40.756 1.00 23.46 ? 208 PHE A C 1 ATOM 1626 O O . PHE A 1 212 ? 29.167 14.501 40.101 1.00 23.57 ? 208 PHE A O 1 ATOM 1627 C CB . PHE A 1 212 ? 27.153 12.696 38.855 1.00 22.51 ? 208 PHE A CB 1 ATOM 1628 C CG . PHE A 1 212 ? 27.719 11.348 39.207 1.00 25.81 ? 208 PHE A CG 1 ATOM 1629 C CD1 . PHE A 1 212 ? 26.907 10.299 39.563 1.00 24.50 ? 208 PHE A CD1 1 ATOM 1630 C CD2 . PHE A 1 212 ? 29.100 11.135 39.121 1.00 24.79 ? 208 PHE A CD2 1 ATOM 1631 C CE1 . PHE A 1 212 ? 27.468 9.018 39.878 1.00 24.54 ? 208 PHE A CE1 1 ATOM 1632 C CE2 . PHE A 1 212 ? 29.666 9.920 39.467 1.00 26.99 ? 208 PHE A CE2 1 ATOM 1633 C CZ . PHE A 1 212 ? 28.846 8.834 39.814 1.00 23.88 ? 208 PHE A CZ 1 ATOM 1634 N N . VAL A 1 213 ? 28.414 13.696 42.066 1.00 24.64 ? 209 VAL A N 1 ATOM 1635 C CA . VAL A 1 213 ? 27.376 13.085 42.969 1.00 23.31 ? 209 VAL A CA 1 ATOM 1636 C C . VAL A 1 213 ? 27.669 13.724 44.364 1.00 24.91 ? 209 VAL A C 1 ATOM 1637 O O . VAL A 1 213 ? 28.809 14.133 44.673 1.00 25.53 ? 209 VAL A O 1 ATOM 1638 C CB . VAL A 1 213 ? 27.449 11.488 43.021 1.00 24.66 ? 209 VAL A CB 1 ATOM 1639 C CG1 . VAL A 1 213 ? 28.860 11.014 43.441 1.00 22.74 ? 209 VAL A CG1 1 ATOM 1640 C CG2 . VAL A 1 213 ? 26.372 10.866 43.972 1.00 20.68 ? 209 VAL A CG2 1 ATOM 1641 N N . GLY A 1 214 ? 26.642 13.877 45.187 1.00 26.17 ? 210 GLY A N 1 ATOM 1642 C CA . GLY A 1 214 ? 26.829 14.456 46.522 1.00 25.89 ? 210 GLY A CA 1 ATOM 1643 C C . GLY A 1 214 ? 26.778 15.981 46.535 1.00 25.67 ? 210 GLY A C 1 ATOM 1644 O O . GLY A 1 214 ? 27.224 16.611 47.508 1.00 25.55 ? 210 GLY A O 1 ATOM 1645 N N . ASP A 1 215 ? 26.239 16.579 45.468 1.00 24.03 ? 211 ASP A N 1 ATOM 1646 C CA . ASP A 1 215 ? 26.066 18.029 45.401 1.00 23.94 ? 211 ASP A CA 1 ATOM 1647 C C . ASP A 1 215 ? 25.210 18.569 46.549 1.00 23.49 ? 211 ASP A C 1 ATOM 1648 O O . ASP A 1 215 ? 25.415 19.698 47.001 1.00 24.30 ? 211 ASP A O 1 ATOM 1649 C CB . ASP A 1 215 ? 25.490 18.519 44.009 1.00 24.16 ? 211 ASP A CB 1 ATOM 1650 C CG . ASP A 1 215 ? 24.228 17.743 43.531 1.00 24.35 ? 211 ASP A CG 1 ATOM 1651 O OD1 . ASP A 1 215 ? 23.947 16.610 43.976 1.00 24.54 ? 211 ASP A OD1 1 ATOM 1652 O OD2 . ASP A 1 215 ? 23.501 18.283 42.637 1.00 26.13 ? 211 ASP A OD2 1 ATOM 1653 N N . GLY A 1 216 ? 24.265 17.761 47.039 1.00 24.18 ? 212 GLY A N 1 ATOM 1654 C CA . GLY A 1 216 ? 23.378 18.216 48.137 1.00 23.94 ? 212 GLY A CA 1 ATOM 1655 C C . GLY A 1 216 ? 24.051 17.907 49.509 1.00 25.93 ? 212 GLY A C 1 ATOM 1656 O O . GLY A 1 216 ? 23.422 18.093 50.544 1.00 24.95 ? 212 GLY A O 1 ATOM 1657 N N . GLY A 1 217 ? 25.266 17.351 49.513 1.00 25.75 ? 213 GLY A N 1 ATOM 1658 C CA . GLY A 1 217 ? 25.896 16.904 50.839 1.00 28.11 ? 213 GLY A CA 1 ATOM 1659 C C . GLY A 1 217 ? 26.991 17.835 51.355 1.00 29.40 ? 213 GLY A C 1 ATOM 1660 O O . GLY A 1 217 ? 27.767 17.479 52.278 1.00 30.51 ? 213 GLY A O 1 ATOM 1661 N N . THR A 1 218 ? 27.107 19.033 50.789 1.00 29.08 ? 214 THR A N 1 ATOM 1662 C CA . THR A 1 218 ? 28.357 19.788 51.032 1.00 30.08 ? 214 THR A CA 1 ATOM 1663 C C . THR A 1 218 ? 28.368 20.427 52.433 1.00 31.83 ? 214 THR A C 1 ATOM 1664 O O . THR A 1 218 ? 27.297 20.688 53.002 1.00 31.10 ? 214 THR A O 1 ATOM 1665 C CB . THR A 1 218 ? 28.608 20.907 49.967 1.00 30.64 ? 214 THR A CB 1 ATOM 1666 O OG1 . THR A 1 218 ? 27.527 21.852 50.015 1.00 30.70 ? 214 THR A OG1 1 ATOM 1667 C CG2 . THR A 1 218 ? 28.748 20.310 48.497 1.00 24.26 ? 214 THR A CG2 1 ATOM 1668 N N . VAL A 1 219 ? 29.580 20.686 52.970 1.00 32.35 ? 215 VAL A N 1 ATOM 1669 C CA . VAL A 1 219 ? 29.729 21.199 54.357 1.00 33.24 ? 215 VAL A CA 1 ATOM 1670 C C . VAL A 1 219 ? 28.984 22.537 54.503 1.00 31.90 ? 215 VAL A C 1 ATOM 1671 O O . VAL A 1 219 ? 29.200 23.434 53.674 1.00 31.59 ? 215 VAL A O 1 ATOM 1672 C CB . VAL A 1 219 ? 31.238 21.467 54.705 1.00 32.86 ? 215 VAL A CB 1 ATOM 1673 C CG1 . VAL A 1 219 ? 31.358 22.218 56.054 1.00 37.05 ? 215 VAL A CG1 1 ATOM 1674 C CG2 . VAL A 1 219 ? 32.023 20.161 54.797 1.00 36.61 ? 215 VAL A CG2 1 ATOM 1675 N N . ASP A 1 220 ? 28.141 22.655 55.535 1.00 31.75 ? 216 ASP A N 1 ATOM 1676 C CA . ASP A 1 220 ? 27.332 23.887 55.807 1.00 32.25 ? 216 ASP A CA 1 ATOM 1677 C C . ASP A 1 220 ? 26.484 24.351 54.602 1.00 31.05 ? 216 ASP A C 1 ATOM 1678 O O . ASP A 1 220 ? 26.158 25.543 54.517 1.00 30.81 ? 216 ASP A O 1 ATOM 1679 C CB . ASP A 1 220 ? 28.193 25.078 56.244 1.00 32.07 ? 216 ASP A CB 1 ATOM 1680 C CG . ASP A 1 220 ? 28.917 24.817 57.591 1.00 36.32 ? 216 ASP A CG 1 ATOM 1681 O OD1 . ASP A 1 220 ? 28.475 23.940 58.336 1.00 36.31 ? 216 ASP A OD1 1 ATOM 1682 O OD2 . ASP A 1 220 ? 29.897 25.507 57.867 1.00 39.50 ? 216 ASP A OD2 1 ATOM 1683 N N . GLY A 1 221 ? 26.148 23.428 53.698 1.00 29.99 ? 217 GLY A N 1 ATOM 1684 C CA . GLY A 1 221 ? 25.429 23.786 52.472 1.00 29.80 ? 217 GLY A CA 1 ATOM 1685 C C . GLY A 1 221 ? 26.211 24.764 51.581 1.00 31.19 ? 217 GLY A C 1 ATOM 1686 O O . GLY A 1 221 ? 25.626 25.485 50.779 1.00 31.28 ? 217 GLY A O 1 ATOM 1687 N N . ILE A 1 222 ? 27.544 24.808 51.701 1.00 29.67 ? 218 ILE A N 1 ATOM 1688 C CA . ILE A 1 222 ? 28.301 25.724 50.823 1.00 30.00 ? 218 ILE A CA 1 ATOM 1689 C C . ILE A 1 222 ? 28.307 25.181 49.379 1.00 29.52 ? 218 ILE A C 1 ATOM 1690 O O . ILE A 1 222 ? 28.715 24.047 49.145 1.00 29.43 ? 218 ILE A O 1 ATOM 1691 C CB . ILE A 1 222 ? 29.754 25.904 51.310 1.00 30.69 ? 218 ILE A CB 1 ATOM 1692 C CG1 . ILE A 1 222 ? 29.747 26.607 52.699 1.00 31.92 ? 218 ILE A CG1 1 ATOM 1693 C CG2 . ILE A 1 222 ? 30.549 26.687 50.272 1.00 31.70 ? 218 ILE A CG2 1 ATOM 1694 C CD1 . ILE A 1 222 ? 31.056 26.286 53.560 1.00 36.65 ? 218 ILE A CD1 1 ATOM 1695 N N . ASN A 1 223 ? 27.837 25.985 48.434 1.00 28.90 ? 219 ASN A N 1 ATOM 1696 C CA . ASN A 1 223 ? 27.677 25.543 47.046 1.00 29.18 ? 219 ASN A CA 1 ATOM 1697 C C . ASN A 1 223 ? 29.055 25.233 46.438 1.00 29.51 ? 219 ASN A C 1 ATOM 1698 O O . ASN A 1 223 ? 30.002 26.016 46.650 1.00 29.30 ? 219 ASN A O 1 ATOM 1699 C CB . ASN A 1 223 ? 27.076 26.711 46.276 1.00 28.80 ? 219 ASN A CB 1 ATOM 1700 C CG . ASN A 1 223 ? 26.633 26.326 44.861 1.00 29.03 ? 219 ASN A CG 1 ATOM 1701 O OD1 . ASN A 1 223 ? 26.754 27.126 43.923 1.00 34.90 ? 219 ASN A OD1 1 ATOM 1702 N ND2 . ASN A 1 223 ? 26.144 25.139 44.712 1.00 21.91 ? 219 ASN A ND2 1 ATOM 1703 N N . GLU A 1 224 ? 29.148 24.123 45.710 1.00 28.48 ? 220 GLU A N 1 ATOM 1704 C CA . GLU A 1 224 ? 30.373 23.709 45.000 1.00 29.79 ? 220 GLU A CA 1 ATOM 1705 C C . GLU A 1 224 ? 31.467 23.242 45.969 1.00 31.39 ? 220 GLU A C 1 ATOM 1706 O O . GLU A 1 224 ? 32.611 23.053 45.559 1.00 31.88 ? 220 GLU A O 1 ATOM 1707 C CB . GLU A 1 224 ? 30.943 24.842 44.171 1.00 30.58 ? 220 GLU A CB 1 ATOM 1708 C CG . GLU A 1 224 ? 29.891 25.494 43.204 1.00 32.05 ? 220 GLU A CG 1 ATOM 1709 C CD . GLU A 1 224 ? 30.518 26.434 42.165 1.00 36.97 ? 220 GLU A CD 1 ATOM 1710 O OE1 . GLU A 1 224 ? 31.770 26.431 41.940 1.00 34.83 ? 220 GLU A OE1 1 ATOM 1711 O OE2 . GLU A 1 224 ? 29.716 27.158 41.541 1.00 41.55 ? 220 GLU A OE2 1 ATOM 1712 N N . ASN A 1 225 ? 31.126 23.062 47.243 1.00 31.43 ? 221 ASN A N 1 ATOM 1713 C CA . ASN A 1 225 ? 32.186 22.769 48.238 1.00 32.35 ? 221 ASN A CA 1 ATOM 1714 C C . ASN A 1 225 ? 32.475 21.285 48.428 1.00 31.73 ? 221 ASN A C 1 ATOM 1715 O O . ASN A 1 225 ? 32.240 20.491 47.510 1.00 30.37 ? 221 ASN A O 1 ATOM 1716 C CB . ASN A 1 225 ? 31.837 23.443 49.554 1.00 32.23 ? 221 ASN A CB 1 ATOM 1717 C CG . ASN A 1 225 ? 33.075 23.876 50.303 1.00 36.86 ? 221 ASN A CG 1 ATOM 1718 O OD1 . ASN A 1 225 ? 33.440 23.251 51.302 1.00 36.00 ? 221 ASN A OD1 1 ATOM 1719 N ND2 . ASN A 1 225 ? 33.738 24.905 49.802 1.00 37.61 ? 221 ASN A ND2 1 ATOM 1720 N N . ASN A 1 226 ? 32.949 20.906 49.626 1.00 31.11 ? 222 ASN A N 1 ATOM 1721 C CA . ASN A 1 226 ? 33.352 19.533 49.912 1.00 31.55 ? 222 ASN A CA 1 ATOM 1722 C C . ASN A 1 226 ? 32.217 18.796 50.606 1.00 30.82 ? 222 ASN A C 1 ATOM 1723 O O . ASN A 1 226 ? 31.595 19.341 51.543 1.00 31.65 ? 222 ASN A O 1 ATOM 1724 C CB . ASN A 1 226 ? 34.560 19.557 50.872 1.00 32.13 ? 222 ASN A CB 1 ATOM 1725 C CG . ASN A 1 226 ? 35.340 18.262 50.863 1.00 34.18 ? 222 ASN A CG 1 ATOM 1726 O OD1 . ASN A 1 226 ? 35.138 17.382 50.007 1.00 34.31 ? 222 ASN A OD1 1 ATOM 1727 N ND2 . ASN A 1 226 ? 36.278 18.139 51.818 1.00 32.01 ? 222 ASN A ND2 1 ATOM 1728 N N . THR A 1 227 ? 31.919 17.595 50.131 1.00 29.42 ? 223 THR A N 1 ATOM 1729 C CA . THR A 1 227 ? 30.977 16.710 50.792 1.00 30.90 ? 223 THR A CA 1 ATOM 1730 C C . THR A 1 227 ? 31.802 15.657 51.571 1.00 32.32 ? 223 THR A C 1 ATOM 1731 O O . THR A 1 227 ? 32.485 14.815 50.975 1.00 32.26 ? 223 THR A O 1 ATOM 1732 C CB . THR A 1 227 ? 30.094 16.012 49.741 1.00 30.77 ? 223 THR A CB 1 ATOM 1733 O OG1 . THR A 1 227 ? 29.242 16.991 49.125 1.00 29.59 ? 223 THR A OG1 1 ATOM 1734 C CG2 . THR A 1 227 ? 29.243 14.922 50.359 1.00 29.78 ? 223 THR A CG2 1 ATOM 1735 N N . ILE A 1 228 ? 31.730 15.722 52.894 1.00 34.04 ? 224 ILE A N 1 ATOM 1736 C CA . ILE A 1 228 ? 32.548 14.849 53.750 1.00 35.44 ? 224 ILE A CA 1 ATOM 1737 C C . ILE A 1 228 ? 31.646 13.750 54.290 1.00 36.69 ? 224 ILE A C 1 ATOM 1738 O O . ILE A 1 228 ? 30.812 14.002 55.153 1.00 36.10 ? 224 ILE A O 1 ATOM 1739 C CB . ILE A 1 228 ? 33.238 15.663 54.882 1.00 36.03 ? 224 ILE A CB 1 ATOM 1740 C CG1 . ILE A 1 228 ? 34.192 16.704 54.258 1.00 36.53 ? 224 ILE A CG1 1 ATOM 1741 C CG2 . ILE A 1 228 ? 34.054 14.711 55.805 1.00 37.98 ? 224 ILE A CG2 1 ATOM 1742 C CD1 . ILE A 1 228 ? 34.574 17.889 55.165 1.00 38.29 ? 224 ILE A CD1 1 ATOM 1743 N N . ILE A 1 229 ? 31.777 12.538 53.748 1.00 37.27 ? 225 ILE A N 1 ATOM 1744 C CA . ILE A 1 229 ? 30.924 11.428 54.158 1.00 37.90 ? 225 ILE A CA 1 ATOM 1745 C C . ILE A 1 229 ? 31.621 10.175 53.692 1.00 38.79 ? 225 ILE A C 1 ATOM 1746 O O . ILE A 1 229 ? 32.290 10.203 52.643 1.00 37.91 ? 225 ILE A O 1 ATOM 1747 C CB . ILE A 1 229 ? 29.503 11.513 53.506 1.00 36.74 ? 225 ILE A CB 1 ATOM 1748 C CG1 . ILE A 1 229 ? 28.501 10.578 54.183 1.00 37.75 ? 225 ILE A CG1 1 ATOM 1749 C CG2 . ILE A 1 229 ? 29.572 11.268 51.991 1.00 36.54 ? 225 ILE A CG2 1 ATOM 1750 C CD1 . ILE A 1 229 ? 27.000 10.957 53.964 1.00 37.86 ? 225 ILE A CD1 1 ATOM 1751 N N . ASN A 1 230 ? 31.479 9.078 54.451 1.00 39.42 ? 226 ASN A N 1 ATOM 1752 C CA . ASN A 1 230 ? 32.114 7.814 54.048 1.00 39.69 ? 226 ASN A CA 1 ATOM 1753 C C . ASN A 1 230 ? 31.396 7.202 52.859 1.00 39.04 ? 226 ASN A C 1 ATOM 1754 O O . ASN A 1 230 ? 30.256 7.620 52.522 1.00 36.56 ? 226 ASN A O 1 ATOM 1755 C CB . ASN A 1 230 ? 32.226 6.805 55.236 1.00 40.76 ? 226 ASN A CB 1 ATOM 1756 C CG . ASN A 1 230 ? 30.882 6.393 55.804 1.00 43.08 ? 226 ASN A CG 1 ATOM 1757 O OD1 . ASN A 1 230 ? 29.824 6.652 55.227 1.00 43.12 ? 226 ASN A OD1 1 ATOM 1758 N ND2 . ASN A 1 230 ? 30.921 5.702 56.957 1.00 42.74 ? 226 ASN A ND2 1 ATOM 1759 N N . ARG A 1 231 ? 32.032 6.222 52.211 1.00 38.30 ? 227 ARG A N 1 ATOM 1760 C CA . ARG A 1 231 ? 31.408 5.609 51.013 1.00 38.14 ? 227 ARG A CA 1 ATOM 1761 C C . ARG A 1 231 ? 30.003 5.100 51.318 1.00 37.90 ? 227 ARG A C 1 ATOM 1762 O O . ARG A 1 231 ? 29.102 5.220 50.493 1.00 37.37 ? 227 ARG A O 1 ATOM 1763 C CB . ARG A 1 231 ? 32.283 4.506 50.381 1.00 38.44 ? 227 ARG A CB 1 ATOM 1764 C CG . ARG A 1 231 ? 31.745 3.895 49.058 1.00 39.45 ? 227 ARG A CG 1 ATOM 1765 C CD . ARG A 1 231 ? 32.757 2.883 48.423 1.00 40.61 ? 227 ARG A CD 1 ATOM 1766 N NE A ARG A 1 231 ? 32.363 2.251 47.163 0.60 39.23 ? 227 ARG A NE 1 ATOM 1767 N NE B ARG A 1 231 ? 33.333 3.460 47.198 0.40 37.33 ? 227 ARG A NE 1 ATOM 1768 C CZ A ARG A 1 231 ? 31.413 1.326 47.010 0.60 41.20 ? 227 ARG A CZ 1 ATOM 1769 C CZ B ARG A 1 231 ? 33.100 3.057 45.946 0.40 35.90 ? 227 ARG A CZ 1 ATOM 1770 N NH1 A ARG A 1 231 ? 30.676 0.909 48.031 0.60 43.10 ? 227 ARG A NH1 1 ATOM 1771 N NH1 B ARG A 1 231 ? 33.674 3.694 44.944 0.40 35.40 ? 227 ARG A NH1 1 ATOM 1772 N NH2 A ARG A 1 231 ? 31.185 0.816 45.805 0.60 43.02 ? 227 ARG A NH2 1 ATOM 1773 N NH2 B ARG A 1 231 ? 32.322 2.018 45.673 0.40 36.68 ? 227 ARG A NH2 1 ATOM 1774 N N . GLU A 1 232 ? 29.797 4.529 52.501 1.00 37.63 ? 228 GLU A N 1 ATOM 1775 C CA . GLU A 1 232 ? 28.481 3.930 52.789 1.00 37.08 ? 228 GLU A CA 1 ATOM 1776 C C . GLU A 1 232 ? 27.364 5.004 52.767 1.00 36.02 ? 228 GLU A C 1 ATOM 1777 O O . GLU A 1 232 ? 26.306 4.771 52.209 1.00 35.80 ? 228 GLU A O 1 ATOM 1778 C CB . GLU A 1 232 ? 28.500 3.114 54.097 1.00 38.98 ? 228 GLU A CB 1 ATOM 1779 C CG . GLU A 1 232 ? 27.124 2.797 54.659 1.00 42.68 ? 228 GLU A CG 1 ATOM 1780 C CD . GLU A 1 232 ? 27.186 1.788 55.804 1.00 51.37 ? 228 GLU A CD 1 ATOM 1781 O OE1 . GLU A 1 232 ? 28.299 1.569 56.339 1.00 54.11 ? 228 GLU A OE1 1 ATOM 1782 O OE2 . GLU A 1 232 ? 26.136 1.204 56.140 1.00 54.46 ? 228 GLU A OE2 1 ATOM 1783 N N . GLY A 1 233 ? 27.660 6.179 53.308 1.00 34.26 ? 229 GLY A N 1 ATOM 1784 C CA . GLY A 1 233 ? 26.741 7.292 53.354 1.00 33.47 ? 229 GLY A CA 1 ATOM 1785 C C . GLY A 1 233 ? 26.548 7.920 51.972 1.00 32.78 ? 229 GLY A C 1 ATOM 1786 O O . GLY A 1 233 ? 25.435 8.299 51.628 1.00 31.50 ? 229 GLY A O 1 ATOM 1787 N N . LEU A 1 234 ? 27.610 7.973 51.156 1.00 30.41 ? 230 LEU A N 1 ATOM 1788 C CA . LEU A 1 234 ? 27.471 8.470 49.786 1.00 30.54 ? 230 LEU A CA 1 ATOM 1789 C C . LEU A 1 234 ? 26.523 7.535 49.025 1.00 31.50 ? 230 LEU A C 1 ATOM 1790 O O . LEU A 1 234 ? 25.620 7.988 48.306 1.00 29.82 ? 230 LEU A O 1 ATOM 1791 C CB . LEU A 1 234 ? 28.847 8.563 49.090 1.00 29.92 ? 230 LEU A CB 1 ATOM 1792 C CG . LEU A 1 234 ? 28.768 9.170 47.668 1.00 29.84 ? 230 LEU A CG 1 ATOM 1793 C CD1 . LEU A 1 234 ? 28.646 10.688 47.780 1.00 26.99 ? 230 LEU A CD1 1 ATOM 1794 C CD2 . LEU A 1 234 ? 30.006 8.785 46.861 1.00 33.09 ? 230 LEU A CD2 1 ATOM 1795 N N . MET A 1 235 ? 26.700 6.227 49.227 1.00 30.32 ? 231 MET A N 1 ATOM 1796 C CA . MET A 1 235 ? 25.940 5.250 48.458 1.00 31.62 ? 231 MET A CA 1 ATOM 1797 C C . MET A 1 235 ? 24.525 5.103 48.974 1.00 31.44 ? 231 MET A C 1 ATOM 1798 O O . MET A 1 235 ? 23.657 4.719 48.222 1.00 33.20 ? 231 MET A O 1 ATOM 1799 C CB . MET A 1 235 ? 26.655 3.888 48.447 1.00 32.12 ? 231 MET A CB 1 ATOM 1800 C CG . MET A 1 235 ? 28.029 3.932 47.759 1.00 30.96 ? 231 MET A CG 1 ATOM 1801 S SD . MET A 1 235 ? 27.800 4.305 45.994 1.00 36.27 ? 231 MET A SD 1 ATOM 1802 C CE . MET A 1 235 ? 29.448 4.152 45.295 1.00 33.79 ? 231 MET A CE 1 ATOM 1803 N N . ASN A 1 236 ? 24.305 5.421 50.238 1.00 31.84 ? 232 ASN A N 1 ATOM 1804 C CA . ASN A 1 236 ? 22.990 5.299 50.871 1.00 33.88 ? 232 ASN A CA 1 ATOM 1805 C C . ASN A 1 236 ? 22.093 6.533 50.661 1.00 31.61 ? 232 ASN A C 1 ATOM 1806 O O . ASN A 1 236 ? 20.878 6.405 50.682 1.00 30.30 ? 232 ASN A O 1 ATOM 1807 C CB . ASN A 1 236 ? 23.167 5.098 52.389 1.00 35.68 ? 232 ASN A CB 1 ATOM 1808 C CG . ASN A 1 236 ? 21.847 4.868 53.114 1.00 44.22 ? 232 ASN A CG 1 ATOM 1809 O OD1 . ASN A 1 236 ? 21.018 4.036 52.678 1.00 53.28 ? 232 ASN A OD1 1 ATOM 1810 N ND2 . ASN A 1 236 ? 21.654 5.560 54.253 1.00 49.77 ? 232 ASN A ND2 1 ATOM 1811 N N . ILE A 1 237 ? 22.710 7.719 50.543 1.00 29.64 ? 233 ILE A N 1 ATOM 1812 C CA . ILE A 1 237 ? 21.946 8.982 50.508 1.00 29.11 ? 233 ILE A CA 1 ATOM 1813 C C . ILE A 1 237 ? 22.014 9.638 49.122 1.00 29.05 ? 233 ILE A C 1 ATOM 1814 O O . ILE A 1 237 ? 20.996 9.892 48.518 1.00 29.31 ? 233 ILE A O 1 ATOM 1815 C CB . ILE A 1 237 ? 22.477 9.967 51.533 1.00 28.54 ? 233 ILE A CB 1 ATOM 1816 C CG1 . ILE A 1 237 ? 22.239 9.448 52.987 1.00 31.79 ? 233 ILE A CG1 1 ATOM 1817 C CG2 . ILE A 1 237 ? 21.782 11.337 51.395 1.00 28.21 ? 233 ILE A CG2 1 ATOM 1818 C CD1 . ILE A 1 237 ? 22.947 10.358 54.018 1.00 33.04 ? 233 ILE A CD1 1 ATOM 1819 N N . HIS A 1 238 ? 23.230 9.840 48.608 1.00 27.10 ? 234 HIS A N 1 ATOM 1820 C CA . HIS A 1 238 ? 23.426 10.693 47.423 1.00 27.61 ? 234 HIS A CA 1 ATOM 1821 C C . HIS A 1 238 ? 23.372 10.002 46.082 1.00 27.87 ? 234 HIS A C 1 ATOM 1822 O O . HIS A 1 238 ? 23.061 10.653 45.041 1.00 25.54 ? 234 HIS A O 1 ATOM 1823 C CB . HIS A 1 238 ? 24.729 11.443 47.620 1.00 27.67 ? 234 HIS A CB 1 ATOM 1824 C CG . HIS A 1 238 ? 24.614 12.445 48.716 1.00 28.43 ? 234 HIS A CG 1 ATOM 1825 N ND1 . HIS A 1 238 ? 25.246 12.309 49.939 1.00 28.10 ? 234 HIS A ND1 1 ATOM 1826 C CD2 . HIS A 1 238 ? 23.848 13.562 48.798 1.00 22.34 ? 234 HIS A CD2 1 ATOM 1827 C CE1 . HIS A 1 238 ? 24.905 13.332 50.717 1.00 23.80 ? 234 HIS A CE1 1 ATOM 1828 N NE2 . HIS A 1 238 ? 24.051 14.096 50.047 1.00 28.07 ? 234 HIS A NE2 1 ATOM 1829 N N . MET A 1 239 ? 23.674 8.694 46.110 1.00 26.92 ? 235 MET A N 1 ATOM 1830 C CA . MET A 1 239 ? 23.715 7.849 44.909 1.00 27.23 ? 235 MET A CA 1 ATOM 1831 C C . MET A 1 239 ? 22.418 7.192 44.462 1.00 26.69 ? 235 MET A C 1 ATOM 1832 O O . MET A 1 239 ? 22.274 6.972 43.277 1.00 27.01 ? 235 MET A O 1 ATOM 1833 C CB . MET A 1 239 ? 24.779 6.742 45.052 1.00 27.59 ? 235 MET A CB 1 ATOM 1834 C CG . MET A 1 239 ? 25.138 6.007 43.762 1.00 26.78 ? 235 MET A CG 1 ATOM 1835 S SD . MET A 1 239 ? 25.947 7.089 42.535 1.00 28.35 ? 235 MET A SD 1 ATOM 1836 C CE . MET A 1 239 ? 27.623 7.193 43.251 1.00 28.98 ? 235 MET A CE 1 ATOM 1837 N N . PRO A 1 240 ? 21.539 6.719 45.392 1.00 26.88 ? 236 PRO A N 1 ATOM 1838 C CA . PRO A 1 240 ? 20.468 5.836 44.899 1.00 26.12 ? 236 PRO A CA 1 ATOM 1839 C C . PRO A 1 240 ? 19.658 6.320 43.672 1.00 26.14 ? 236 PRO A C 1 ATOM 1840 O O . PRO A 1 240 ? 19.329 5.517 42.750 1.00 27.21 ? 236 PRO A O 1 ATOM 1841 C CB . PRO A 1 240 ? 19.501 5.763 46.109 1.00 27.13 ? 236 PRO A CB 1 ATOM 1842 C CG . PRO A 1 240 ? 20.448 5.744 47.334 1.00 29.96 ? 236 PRO A CG 1 ATOM 1843 C CD . PRO A 1 240 ? 21.620 6.714 46.874 1.00 26.82 ? 236 PRO A CD 1 ATOM 1844 N N . ALA A 1 241 ? 19.282 7.600 43.660 1.00 24.63 ? 237 ALA A N 1 ATOM 1845 C CA . ALA A 1 241 ? 18.439 8.072 42.540 1.00 24.58 ? 237 ALA A CA 1 ATOM 1846 C C . ALA A 1 241 ? 19.157 8.042 41.168 1.00 24.94 ? 237 ALA A C 1 ATOM 1847 O O . ALA A 1 241 ? 18.488 7.971 40.113 1.00 25.66 ? 237 ALA A O 1 ATOM 1848 C CB . ALA A 1 241 ? 17.840 9.488 42.877 1.00 23.46 ? 237 ALA A CB 1 ATOM 1849 N N . TYR A 1 242 ? 20.494 8.039 41.164 1.00 24.88 ? 238 TYR A N 1 ATOM 1850 C CA . TYR A 1 242 ? 21.251 7.776 39.891 1.00 26.15 ? 238 TYR A CA 1 ATOM 1851 C C . TYR A 1 242 ? 20.963 6.396 39.314 1.00 27.09 ? 238 TYR A C 1 ATOM 1852 O O . TYR A 1 242 ? 20.844 6.247 38.111 1.00 27.39 ? 238 TYR A O 1 ATOM 1853 C CB . TYR A 1 242 ? 22.763 7.999 40.045 1.00 25.10 ? 238 TYR A CB 1 ATOM 1854 C CG . TYR A 1 242 ? 23.061 9.468 40.048 1.00 22.78 ? 238 TYR A CG 1 ATOM 1855 C CD1 . TYR A 1 242 ? 23.152 10.177 38.824 1.00 22.96 ? 238 TYR A CD1 1 ATOM 1856 C CD2 . TYR A 1 242 ? 23.167 10.176 41.258 1.00 22.11 ? 238 TYR A CD2 1 ATOM 1857 C CE1 . TYR A 1 242 ? 23.340 11.552 38.813 1.00 22.15 ? 238 TYR A CE1 1 ATOM 1858 C CE2 . TYR A 1 242 ? 23.354 11.581 41.272 1.00 24.08 ? 238 TYR A CE2 1 ATOM 1859 C CZ . TYR A 1 242 ? 23.419 12.257 40.045 1.00 23.73 ? 238 TYR A CZ 1 ATOM 1860 O OH . TYR A 1 242 ? 23.621 13.629 40.053 1.00 22.89 ? 238 TYR A OH 1 ATOM 1861 N N . LYS A 1 243 ? 20.785 5.385 40.174 1.00 27.84 ? 239 LYS A N 1 ATOM 1862 C CA . LYS A 1 243 ? 20.443 4.042 39.653 1.00 27.42 ? 239 LYS A CA 1 ATOM 1863 C C . LYS A 1 243 ? 19.017 4.012 39.089 1.00 26.30 ? 239 LYS A C 1 ATOM 1864 O O . LYS A 1 243 ? 18.778 3.425 38.040 1.00 27.08 ? 239 LYS A O 1 ATOM 1865 C CB . LYS A 1 243 ? 20.585 2.962 40.738 1.00 29.35 ? 239 LYS A CB 1 ATOM 1866 C CG . LYS A 1 243 ? 20.029 1.620 40.283 1.00 32.27 ? 239 LYS A CG 1 ATOM 1867 C CD . LYS A 1 243 ? 20.908 1.026 39.106 1.00 39.90 ? 239 LYS A CD 1 ATOM 1868 C CE . LYS A 1 243 ? 20.824 -0.511 39.095 1.00 46.93 ? 239 LYS A CE 1 ATOM 1869 N NZ . LYS A 1 243 ? 19.410 -0.961 38.782 1.00 47.49 ? 239 LYS A NZ 1 ATOM 1870 N N . ASN A 1 244 ? 18.056 4.654 39.761 1.00 26.13 ? 240 ASN A N 1 ATOM 1871 C CA . ASN A 1 244 ? 16.713 4.839 39.170 1.00 25.52 ? 240 ASN A CA 1 ATOM 1872 C C . ASN A 1 244 ? 16.777 5.548 37.795 1.00 25.05 ? 240 ASN A C 1 ATOM 1873 O O . ASN A 1 244 ? 16.085 5.168 36.848 1.00 24.22 ? 240 ASN A O 1 ATOM 1874 C CB . ASN A 1 244 ? 15.801 5.645 40.143 1.00 26.35 ? 240 ASN A CB 1 ATOM 1875 C CG . ASN A 1 244 ? 15.591 4.921 41.506 1.00 30.31 ? 240 ASN A CG 1 ATOM 1876 O OD1 . ASN A 1 244 ? 16.411 4.989 42.413 1.00 32.55 ? 240 ASN A OD1 1 ATOM 1877 N ND2 . ASN A 1 244 ? 14.472 4.252 41.624 1.00 37.34 ? 240 ASN A ND2 1 ATOM 1878 N N . ALA A 1 245 ? 17.607 6.579 37.699 1.00 24.01 ? 241 ALA A N 1 ATOM 1879 C CA . ALA A 1 245 ? 17.823 7.286 36.414 1.00 23.76 ? 241 ALA A CA 1 ATOM 1880 C C . ALA A 1 245 ? 18.366 6.359 35.323 1.00 24.22 ? 241 ALA A C 1 ATOM 1881 O O . ALA A 1 245 ? 17.865 6.387 34.194 1.00 23.68 ? 241 ALA A O 1 ATOM 1882 C CB . ALA A 1 245 ? 18.772 8.567 36.637 1.00 24.19 ? 241 ALA A CB 1 ATOM 1883 N N . MET A 1 246 ? 19.330 5.476 35.669 1.00 25.34 ? 242 MET A N 1 ATOM 1884 C CA . MET A 1 246 ? 19.806 4.416 34.735 1.00 25.42 ? 242 MET A CA 1 ATOM 1885 C C . MET A 1 246 ? 18.677 3.507 34.297 1.00 25.88 ? 242 MET A C 1 ATOM 1886 O O . MET A 1 246 ? 18.564 3.175 33.081 1.00 25.60 ? 242 MET A O 1 ATOM 1887 C CB . MET A 1 246 ? 20.904 3.509 35.353 1.00 26.58 ? 242 MET A CB 1 ATOM 1888 C CG . MET A 1 246 ? 22.155 4.208 35.936 1.00 25.54 ? 242 MET A CG 1 ATOM 1889 S SD . MET A 1 246 ? 23.169 5.065 34.694 1.00 29.82 ? 242 MET A SD 1 ATOM 1890 C CE . MET A 1 246 ? 22.652 6.791 34.945 1.00 28.46 ? 242 MET A CE 1 ATOM 1891 N N . ASP A 1 247 ? 17.849 3.086 35.262 1.00 25.89 ? 243 ASP A N 1 ATOM 1892 C CA . ASP A 1 247 ? 16.718 2.206 34.960 1.00 27.83 ? 243 ASP A CA 1 ATOM 1893 C C . ASP A 1 247 ? 15.719 2.830 33.997 1.00 28.01 ? 243 ASP A C 1 ATOM 1894 O O . ASP A 1 247 ? 15.084 2.116 33.224 1.00 26.72 ? 243 ASP A O 1 ATOM 1895 C CB . ASP A 1 247 ? 15.951 1.792 36.228 1.00 27.68 ? 243 ASP A CB 1 ATOM 1896 C CG . ASP A 1 247 ? 16.737 0.848 37.086 1.00 31.05 ? 243 ASP A CG 1 ATOM 1897 O OD1 . ASP A 1 247 ? 17.778 0.330 36.636 1.00 32.07 ? 243 ASP A OD1 1 ATOM 1898 O OD2 . ASP A 1 247 ? 16.355 0.692 38.246 1.00 32.11 ? 243 ASP A OD2 1 ATOM 1899 N N . LYS A 1 248 ? 15.622 4.164 34.049 1.00 26.57 ? 244 LYS A N 1 ATOM 1900 C CA . LYS A 1 248 ? 14.730 4.910 33.187 1.00 27.13 ? 244 LYS A CA 1 ATOM 1901 C C . LYS A 1 248 ? 15.407 5.480 31.942 1.00 26.67 ? 244 LYS A C 1 ATOM 1902 O O . LYS A 1 248 ? 14.798 6.239 31.208 1.00 27.46 ? 244 LYS A O 1 ATOM 1903 C CB . LYS A 1 248 ? 14.068 6.011 34.034 1.00 26.42 ? 244 LYS A CB 1 ATOM 1904 C CG . LYS A 1 248 ? 13.255 5.365 35.175 1.00 27.13 ? 244 LYS A CG 1 ATOM 1905 C CD . LYS A 1 248 ? 12.701 6.373 36.243 1.00 26.50 ? 244 LYS A CD 1 ATOM 1906 C CE . LYS A 1 248 ? 12.041 5.503 37.382 1.00 27.19 ? 244 LYS A CE 1 ATOM 1907 N NZ . LYS A 1 248 ? 11.272 6.430 38.322 1.00 29.54 ? 244 LYS A NZ 1 ATOM 1908 N N . GLY A 1 249 ? 16.655 5.110 31.676 1.00 26.47 ? 245 GLY A N 1 ATOM 1909 C CA . GLY A 1 249 ? 17.218 5.486 30.377 1.00 24.94 ? 245 GLY A CA 1 ATOM 1910 C C . GLY A 1 249 ? 17.668 6.948 30.268 1.00 24.06 ? 245 GLY A C 1 ATOM 1911 O O . GLY A 1 249 ? 17.689 7.503 29.162 1.00 24.24 ? 245 GLY A O 1 ATOM 1912 N N . VAL A 1 250 ? 18.027 7.590 31.381 1.00 23.78 ? 246 VAL A N 1 ATOM 1913 C CA . VAL A 1 250 ? 18.457 9.012 31.324 1.00 23.19 ? 246 VAL A CA 1 ATOM 1914 C C . VAL A 1 250 ? 19.623 9.116 30.296 1.00 23.15 ? 246 VAL A C 1 ATOM 1915 O O . VAL A 1 250 ? 20.510 8.283 30.296 1.00 23.45 ? 246 VAL A O 1 ATOM 1916 C CB . VAL A 1 250 ? 18.853 9.591 32.703 1.00 22.80 ? 246 VAL A CB 1 ATOM 1917 C CG1 . VAL A 1 250 ? 20.231 9.053 33.211 1.00 24.59 ? 246 VAL A CG1 1 ATOM 1918 C CG2 . VAL A 1 250 ? 18.851 11.139 32.673 1.00 23.25 ? 246 VAL A CG2 1 ATOM 1919 N N . SER A 1 251 ? 19.573 10.082 29.383 1.00 23.06 ? 247 SER A N 1 ATOM 1920 C CA . SER A 1 251 ? 20.541 10.110 28.261 1.00 22.79 ? 247 SER A CA 1 ATOM 1921 C C . SER A 1 251 ? 21.904 10.634 28.635 1.00 22.10 ? 247 SER A C 1 ATOM 1922 O O . SER A 1 251 ? 22.923 10.249 28.030 1.00 21.49 ? 247 SER A O 1 ATOM 1923 C CB . SER A 1 251 ? 19.988 10.953 27.104 1.00 23.84 ? 247 SER A CB 1 ATOM 1924 O OG . SER A 1 251 ? 18.902 10.276 26.492 1.00 23.88 ? 247 SER A OG 1 ATOM 1925 N N . THR A 1 252 ? 21.932 11.570 29.587 1.00 21.02 ? 248 THR A N 1 ATOM 1926 C CA . THR A 1 252 ? 23.182 12.179 29.992 1.00 20.75 ? 248 THR A CA 1 ATOM 1927 C C . THR A 1 252 ? 23.258 12.347 31.511 1.00 22.19 ? 248 THR A C 1 ATOM 1928 O O . THR A 1 252 ? 22.225 12.336 32.235 1.00 21.36 ? 248 THR A O 1 ATOM 1929 C CB . THR A 1 252 ? 23.356 13.595 29.354 1.00 21.82 ? 248 THR A CB 1 ATOM 1930 O OG1 . THR A 1 252 ? 22.442 14.523 29.991 1.00 20.98 ? 248 THR A OG1 1 ATOM 1931 C CG2 . THR A 1 252 ? 23.042 13.545 27.840 1.00 20.40 ? 248 THR A CG2 1 ATOM 1932 N N . VAL A 1 253 ? 24.489 12.513 31.997 1.00 21.52 ? 249 VAL A N 1 ATOM 1933 C CA . VAL A 1 253 ? 24.703 12.819 33.410 1.00 22.47 ? 249 VAL A CA 1 ATOM 1934 C C . VAL A 1 253 ? 25.684 14.005 33.458 1.00 21.96 ? 249 VAL A C 1 ATOM 1935 O O . VAL A 1 253 ? 26.739 13.982 32.798 1.00 21.86 ? 249 VAL A O 1 ATOM 1936 C CB . VAL A 1 253 ? 25.332 11.623 34.163 1.00 23.07 ? 249 VAL A CB 1 ATOM 1937 C CG1 . VAL A 1 253 ? 25.804 12.073 35.553 1.00 22.36 ? 249 VAL A CG1 1 ATOM 1938 C CG2 . VAL A 1 253 ? 24.310 10.419 34.264 1.00 23.53 ? 249 VAL A CG2 1 ATOM 1939 N N . MET A 1 254 ? 25.346 15.019 34.229 1.00 20.44 ? 250 MET A N 1 ATOM 1940 C CA . MET A 1 254 ? 26.281 16.127 34.437 1.00 21.50 ? 250 MET A CA 1 ATOM 1941 C C . MET A 1 254 ? 27.040 15.984 35.779 1.00 22.20 ? 250 MET A C 1 ATOM 1942 O O . MET A 1 254 ? 26.456 15.678 36.816 1.00 22.38 ? 250 MET A O 1 ATOM 1943 C CB . MET A 1 254 ? 25.537 17.501 34.421 1.00 20.46 ? 250 MET A CB 1 ATOM 1944 C CG . MET A 1 254 ? 26.425 18.742 34.621 1.00 22.78 ? 250 MET A CG 1 ATOM 1945 S SD . MET A 1 254 ? 25.488 20.344 34.680 1.00 23.08 ? 250 MET A SD 1 ATOM 1946 C CE . MET A 1 254 ? 24.628 20.274 33.135 1.00 19.39 ? 250 MET A CE 1 ATOM 1947 N N . ILE A 1 255 ? 28.328 16.282 35.743 1.00 21.17 ? 251 ILE A N 1 ATOM 1948 C CA . ILE A 1 255 ? 29.195 16.158 36.912 1.00 22.97 ? 251 ILE A CA 1 ATOM 1949 C C . ILE A 1 255 ? 29.094 17.386 37.799 1.00 22.86 ? 251 ILE A C 1 ATOM 1950 O O . ILE A 1 255 ? 28.981 18.519 37.316 1.00 24.02 ? 251 ILE A O 1 ATOM 1951 C CB . ILE A 1 255 ? 30.692 15.968 36.502 1.00 22.12 ? 251 ILE A CB 1 ATOM 1952 C CG1 . ILE A 1 255 ? 30.825 14.749 35.590 1.00 22.35 ? 251 ILE A CG1 1 ATOM 1953 C CG2 . ILE A 1 255 ? 31.619 15.784 37.767 1.00 21.48 ? 251 ILE A CG2 1 ATOM 1954 C CD1 . ILE A 1 255 ? 30.179 13.411 36.190 1.00 25.61 ? 251 ILE A CD1 1 ATOM 1955 N N . SER A 1 256 ? 29.164 17.159 39.112 1.00 22.73 ? 252 SER A N 1 ATOM 1956 C CA . SER A 1 256 ? 29.094 18.242 40.106 1.00 22.90 ? 252 SER A CA 1 ATOM 1957 C C . SER A 1 256 ? 30.406 19.063 40.257 1.00 24.41 ? 252 SER A C 1 ATOM 1958 O O . SER A 1 256 ? 31.507 18.512 40.211 1.00 24.04 ? 252 SER A O 1 ATOM 1959 C CB . SER A 1 256 ? 28.706 17.668 41.495 1.00 20.40 ? 252 SER A CB 1 ATOM 1960 O OG . SER A 1 256 ? 28.574 18.741 42.382 1.00 24.22 ? 252 SER A OG 1 ATOM 1961 N N . TYR A 1 257 ? 30.276 20.368 40.477 1.00 23.58 ? 253 TYR A N 1 ATOM 1962 C CA . TYR A 1 257 ? 31.432 21.164 40.907 1.00 25.84 ? 253 TYR A CA 1 ATOM 1963 C C . TYR A 1 257 ? 32.016 20.705 42.246 1.00 26.90 ? 253 TYR A C 1 ATOM 1964 O O . TYR A 1 257 ? 33.167 21.040 42.565 1.00 26.51 ? 253 TYR A O 1 ATOM 1965 C CB . TYR A 1 257 ? 30.993 22.593 41.163 1.00 24.16 ? 253 TYR A CB 1 ATOM 1966 C CG . TYR A 1 257 ? 30.648 23.450 39.956 1.00 25.37 ? 253 TYR A CG 1 ATOM 1967 C CD1 . TYR A 1 257 ? 31.551 23.666 38.930 1.00 25.13 ? 253 TYR A CD1 1 ATOM 1968 C CD2 . TYR A 1 257 ? 29.423 24.105 39.895 1.00 26.96 ? 253 TYR A CD2 1 ATOM 1969 C CE1 . TYR A 1 257 ? 31.237 24.546 37.877 1.00 24.21 ? 253 TYR A CE1 1 ATOM 1970 C CE2 . TYR A 1 257 ? 29.113 24.969 38.878 1.00 27.90 ? 253 TYR A CE2 1 ATOM 1971 C CZ . TYR A 1 257 ? 30.018 25.164 37.848 1.00 26.37 ? 253 TYR A CZ 1 ATOM 1972 O OH . TYR A 1 257 ? 29.682 26.046 36.826 1.00 26.68 ? 253 TYR A OH 1 ATOM 1973 N N . SER A 1 258 ? 31.189 20.022 43.055 1.00 27.65 ? 254 SER A N 1 ATOM 1974 C CA . SER A 1 258 ? 31.543 19.739 44.466 1.00 27.96 ? 254 SER A CA 1 ATOM 1975 C C . SER A 1 258 ? 32.618 18.665 44.512 1.00 27.95 ? 254 SER A C 1 ATOM 1976 O O . SER A 1 258 ? 32.963 18.071 43.485 1.00 28.08 ? 254 SER A O 1 ATOM 1977 C CB . SER A 1 258 ? 30.295 19.332 45.280 1.00 27.82 ? 254 SER A CB 1 ATOM 1978 O OG . SER A 1 258 ? 29.662 18.199 44.676 1.00 26.76 ? 254 SER A OG 1 ATOM 1979 N N . SER A 1 259 ? 33.184 18.455 45.700 1.00 29.02 ? 255 SER A N 1 ATOM 1980 C CA . SER A 1 259 ? 34.244 17.439 45.911 1.00 29.63 ? 255 SER A CA 1 ATOM 1981 C C . SER A 1 259 ? 33.680 16.329 46.843 1.00 30.05 ? 255 SER A C 1 ATOM 1982 O O . SER A 1 259 ? 32.705 16.565 47.551 1.00 30.04 ? 255 SER A O 1 ATOM 1983 C CB . SER A 1 259 ? 35.451 18.119 46.564 1.00 29.87 ? 255 SER A CB 1 ATOM 1984 O OG . SER A 1 259 ? 36.069 19.062 45.652 1.00 28.17 ? 255 SER A OG 1 ATOM 1985 N N . TRP A 1 260 ? 34.269 15.133 46.847 1.00 30.70 ? 256 TRP A N 1 ATOM 1986 C CA . TRP A 1 260 ? 33.877 14.123 47.836 1.00 31.40 ? 256 TRP A CA 1 ATOM 1987 C C . TRP A 1 260 ? 35.163 13.778 48.615 1.00 32.78 ? 256 TRP A C 1 ATOM 1988 O O . TRP A 1 260 ? 36.154 13.364 47.993 1.00 33.15 ? 256 TRP A O 1 ATOM 1989 C CB . TRP A 1 260 ? 33.327 12.881 47.124 1.00 31.49 ? 256 TRP A CB 1 ATOM 1990 C CG . TRP A 1 260 ? 33.023 11.773 48.078 1.00 32.79 ? 256 TRP A CG 1 ATOM 1991 C CD1 . TRP A 1 260 ? 32.350 11.883 49.271 1.00 34.91 ? 256 TRP A CD1 1 ATOM 1992 C CD2 . TRP A 1 260 ? 33.359 10.394 47.929 1.00 33.40 ? 256 TRP A CD2 1 ATOM 1993 N NE1 . TRP A 1 260 ? 32.258 10.648 49.879 1.00 33.80 ? 256 TRP A NE1 1 ATOM 1994 C CE2 . TRP A 1 260 ? 32.868 9.717 49.079 1.00 35.75 ? 256 TRP A CE2 1 ATOM 1995 C CE3 . TRP A 1 260 ? 34.034 9.657 46.943 1.00 34.74 ? 256 TRP A CE3 1 ATOM 1996 C CZ2 . TRP A 1 260 ? 33.032 8.324 49.266 1.00 36.98 ? 256 TRP A CZ2 1 ATOM 1997 C CZ3 . TRP A 1 260 ? 34.201 8.289 47.121 1.00 36.58 ? 256 TRP A CZ3 1 ATOM 1998 C CH2 . TRP A 1 260 ? 33.706 7.631 48.281 1.00 37.76 ? 256 TRP A CH2 1 ATOM 1999 N N . ASN A 1 261 ? 35.147 13.999 49.928 1.00 34.51 ? 257 ASN A N 1 ATOM 2000 C CA . ASN A 1 261 ? 36.332 13.802 50.780 1.00 35.21 ? 257 ASN A CA 1 ATOM 2001 C C . ASN A 1 261 ? 37.588 14.463 50.170 1.00 36.89 ? 257 ASN A C 1 ATOM 2002 O O . ASN A 1 261 ? 38.677 13.883 50.150 1.00 36.67 ? 257 ASN A O 1 ATOM 2003 C CB . ASN A 1 261 ? 36.517 12.304 51.064 1.00 35.59 ? 257 ASN A CB 1 ATOM 2004 C CG . ASN A 1 261 ? 35.327 11.698 51.863 1.00 33.44 ? 257 ASN A CG 1 ATOM 2005 O OD1 . ASN A 1 261 ? 34.718 12.377 52.685 1.00 32.92 ? 257 ASN A OD1 1 ATOM 2006 N ND2 . ASN A 1 261 ? 34.995 10.446 51.595 1.00 33.13 ? 257 ASN A ND2 1 ATOM 2007 N N . GLY A 1 262 ? 37.421 15.683 49.645 1.00 35.72 ? 258 GLY A N 1 ATOM 2008 C CA . GLY A 1 262 ? 38.556 16.435 49.097 1.00 34.30 ? 258 GLY A CA 1 ATOM 2009 C C . GLY A 1 262 ? 38.922 16.200 47.644 1.00 34.71 ? 258 GLY A C 1 ATOM 2010 O O . GLY A 1 262 ? 39.785 16.911 47.117 1.00 34.31 ? 258 GLY A O 1 ATOM 2011 N N . VAL A 1 263 ? 38.277 15.222 46.983 1.00 32.82 ? 259 VAL A N 1 ATOM 2012 C CA . VAL A 1 263 ? 38.574 14.927 45.575 1.00 31.12 ? 259 VAL A CA 1 ATOM 2013 C C . VAL A 1 263 ? 37.492 15.578 44.689 1.00 30.54 ? 259 VAL A C 1 ATOM 2014 O O . VAL A 1 263 ? 36.319 15.320 44.886 1.00 30.23 ? 259 VAL A O 1 ATOM 2015 C CB . VAL A 1 263 ? 38.585 13.398 45.296 1.00 31.65 ? 259 VAL A CB 1 ATOM 2016 C CG1 . VAL A 1 263 ? 38.715 13.122 43.787 1.00 31.37 ? 259 VAL A CG1 1 ATOM 2017 C CG2 . VAL A 1 263 ? 39.759 12.673 46.145 1.00 32.81 ? 259 VAL A CG2 1 ATOM 2018 N N . LYS A 1 264 ? 37.909 16.424 43.756 1.00 28.87 ? 260 LYS A N 1 ATOM 2019 C CA . LYS A 1 264 ? 36.976 17.096 42.827 1.00 28.62 ? 260 LYS A CA 1 ATOM 2020 C C . LYS A 1 264 ? 36.258 16.035 42.014 1.00 27.38 ? 260 LYS A C 1 ATOM 2021 O O . LYS A 1 264 ? 36.887 15.128 41.456 1.00 27.73 ? 260 LYS A O 1 ATOM 2022 C CB . LYS A 1 264 ? 37.776 18.005 41.896 1.00 27.54 ? 260 LYS A CB 1 ATOM 2023 C CG . LYS A 1 264 ? 38.431 19.188 42.589 1.00 28.06 ? 260 LYS A CG 1 ATOM 2024 C CD . LYS A 1 264 ? 37.403 20.408 42.683 1.00 28.18 ? 260 LYS A CD 1 ATOM 2025 C CE . LYS A 1 264 ? 38.009 21.578 43.489 1.00 30.98 ? 260 LYS A CE 1 ATOM 2026 N NZ . LYS A 1 264 ? 36.956 22.674 43.562 1.00 28.56 ? 260 LYS A NZ 1 ATOM 2027 N N . MET A 1 265 ? 34.929 16.096 41.989 1.00 26.34 ? 261 MET A N 1 ATOM 2028 C CA . MET A 1 265 ? 34.149 15.215 41.123 1.00 25.57 ? 261 MET A CA 1 ATOM 2029 C C . MET A 1 265 ? 34.612 15.260 39.641 1.00 25.99 ? 261 MET A C 1 ATOM 2030 O O . MET A 1 265 ? 34.573 14.216 38.975 1.00 25.45 ? 261 MET A O 1 ATOM 2031 C CB . MET A 1 265 ? 32.658 15.579 41.175 1.00 24.35 ? 261 MET A CB 1 ATOM 2032 C CG . MET A 1 265 ? 31.878 15.046 42.404 1.00 26.35 ? 261 MET A CG 1 ATOM 2033 S SD . MET A 1 265 ? 32.087 13.305 42.823 1.00 28.80 ? 261 MET A SD 1 ATOM 2034 C CE . MET A 1 265 ? 31.867 12.497 41.227 1.00 26.13 ? 261 MET A CE 1 ATOM 2035 N N . HIS A 1 266 ? 34.951 16.454 39.119 1.00 24.65 ? 262 HIS A N 1 ATOM 2036 C CA . HIS A 1 266 ? 35.372 16.600 37.703 1.00 23.96 ? 262 HIS A CA 1 ATOM 2037 C C . HIS A 1 266 ? 36.735 15.893 37.431 1.00 25.51 ? 262 HIS A C 1 ATOM 2038 O O . HIS A 1 266 ? 37.186 15.782 36.286 1.00 25.65 ? 262 HIS A O 1 ATOM 2039 C CB . HIS A 1 266 ? 35.446 18.064 37.271 1.00 24.65 ? 262 HIS A CB 1 ATOM 2040 C CG . HIS A 1 266 ? 34.097 18.690 37.029 1.00 25.05 ? 262 HIS A CG 1 ATOM 2041 N ND1 . HIS A 1 266 ? 33.627 19.008 35.760 1.00 27.45 ? 262 HIS A ND1 1 ATOM 2042 C CD2 . HIS A 1 266 ? 33.102 19.013 37.891 1.00 23.34 ? 262 HIS A CD2 1 ATOM 2043 C CE1 . HIS A 1 266 ? 32.405 19.533 35.862 1.00 22.77 ? 262 HIS A CE1 1 ATOM 2044 N NE2 . HIS A 1 266 ? 32.064 19.548 37.136 1.00 28.24 ? 262 HIS A NE2 1 ATOM 2045 N N . ALA A 1 267 ? 37.398 15.426 38.484 1.00 26.32 ? 263 ALA A N 1 ATOM 2046 C CA . ALA A 1 267 ? 38.676 14.687 38.281 1.00 27.48 ? 263 ALA A CA 1 ATOM 2047 C C . ALA A 1 267 ? 38.587 13.305 38.883 1.00 28.42 ? 263 ALA A C 1 ATOM 2048 O O . ALA A 1 267 ? 39.606 12.636 39.054 1.00 29.26 ? 263 ALA A O 1 ATOM 2049 C CB . ALA A 1 267 ? 39.895 15.500 38.910 1.00 28.70 ? 263 ALA A CB 1 ATOM 2050 N N . ASN A 1 268 ? 37.387 12.849 39.239 1.00 27.58 ? 264 ASN A N 1 ATOM 2051 C CA . ASN A 1 268 ? 37.225 11.572 39.981 1.00 27.83 ? 264 ASN A CA 1 ATOM 2052 C C . ASN A 1 268 ? 36.986 10.355 39.073 1.00 28.69 ? 264 ASN A C 1 ATOM 2053 O O . ASN A 1 268 ? 35.862 10.010 38.725 1.00 27.84 ? 264 ASN A O 1 ATOM 2054 C CB . ASN A 1 268 ? 36.152 11.660 41.092 1.00 28.92 ? 264 ASN A CB 1 ATOM 2055 C CG . ASN A 1 268 ? 36.295 10.486 42.119 1.00 31.36 ? 264 ASN A CG 1 ATOM 2056 O OD1 . ASN A 1 268 ? 36.602 9.365 41.716 1.00 30.98 ? 264 ASN A OD1 1 ATOM 2057 N ND2 . ASN A 1 268 ? 36.084 10.751 43.396 1.00 29.19 ? 264 ASN A ND2 1 ATOM 2058 N N . GLN A 1 269 ? 38.073 9.691 38.681 1.00 28.41 ? 265 GLN A N 1 ATOM 2059 C CA . GLN A 1 269 ? 37.985 8.571 37.766 1.00 28.90 ? 265 GLN A CA 1 ATOM 2060 C C . GLN A 1 269 ? 37.298 7.389 38.428 1.00 29.64 ? 265 GLN A C 1 ATOM 2061 O O . GLN A 1 269 ? 36.546 6.684 37.779 1.00 29.38 ? 265 GLN A O 1 ATOM 2062 C CB . GLN A 1 269 ? 39.408 8.158 37.317 1.00 30.02 ? 265 GLN A CB 1 ATOM 2063 C CG . GLN A 1 269 ? 39.438 7.169 36.187 1.00 29.24 ? 265 GLN A CG 1 ATOM 2064 C CD . GLN A 1 269 ? 40.887 6.755 35.870 1.00 37.83 ? 265 GLN A CD 1 ATOM 2065 O OE1 . GLN A 1 269 ? 41.511 7.264 34.952 1.00 39.81 ? 265 GLN A OE1 1 ATOM 2066 N NE2 . GLN A 1 269 ? 41.420 5.880 36.676 1.00 40.10 ? 265 GLN A NE2 1 ATOM 2067 N N . ASP A 1 270 ? 37.553 7.177 39.721 1.00 30.11 ? 266 ASP A N 1 ATOM 2068 C CA . ASP A 1 270 ? 36.954 6.052 40.436 1.00 31.53 ? 266 ASP A CA 1 ATOM 2069 C C . ASP A 1 270 ? 35.390 6.142 40.382 1.00 30.83 ? 266 ASP A C 1 ATOM 2070 O O . ASP A 1 270 ? 34.709 5.147 40.169 1.00 29.65 ? 266 ASP A O 1 ATOM 2071 C CB . ASP A 1 270 ? 37.401 6.073 41.894 1.00 33.42 ? 266 ASP A CB 1 ATOM 2072 C CG . ASP A 1 270 ? 38.837 5.561 42.097 1.00 40.20 ? 266 ASP A CG 1 ATOM 2073 O OD1 . ASP A 1 270 ? 39.336 5.701 43.241 1.00 46.98 ? 266 ASP A OD1 1 ATOM 2074 O OD2 . ASP A 1 270 ? 39.465 5.032 41.135 1.00 44.28 ? 266 ASP A OD2 1 ATOM 2075 N N . LEU A 1 271 ? 34.849 7.338 40.610 1.00 28.54 ? 267 LEU A N 1 ATOM 2076 C CA . LEU A 1 271 ? 33.397 7.504 40.595 1.00 28.45 ? 267 LEU A CA 1 ATOM 2077 C C . LEU A 1 271 ? 32.810 7.628 39.184 1.00 28.21 ? 267 LEU A C 1 ATOM 2078 O O . LEU A 1 271 ? 31.812 7.011 38.887 1.00 28.79 ? 267 LEU A O 1 ATOM 2079 C CB . LEU A 1 271 ? 32.986 8.707 41.486 1.00 26.75 ? 267 LEU A CB 1 ATOM 2080 C CG . LEU A 1 271 ? 33.026 8.455 43.026 1.00 29.36 ? 267 LEU A CG 1 ATOM 2081 C CD1 . LEU A 1 271 ? 32.555 9.694 43.812 1.00 28.94 ? 267 LEU A CD1 1 ATOM 2082 C CD2 . LEU A 1 271 ? 32.168 7.189 43.387 1.00 32.10 ? 267 LEU A CD2 1 ATOM 2083 N N . VAL A 1 272 ? 33.429 8.440 38.322 1.00 28.34 ? 268 VAL A N 1 ATOM 2084 C CA . VAL A 1 272 ? 32.882 8.641 36.957 1.00 27.76 ? 268 VAL A CA 1 ATOM 2085 C C . VAL A 1 272 ? 33.034 7.401 36.079 1.00 28.38 ? 268 VAL A C 1 ATOM 2086 O O . VAL A 1 272 ? 32.080 6.965 35.444 1.00 26.75 ? 268 VAL A O 1 ATOM 2087 C CB . VAL A 1 272 ? 33.520 9.897 36.265 1.00 27.27 ? 268 VAL A CB 1 ATOM 2088 C CG1 . VAL A 1 272 ? 33.020 10.051 34.800 1.00 28.46 ? 268 VAL A CG1 1 ATOM 2089 C CG2 . VAL A 1 272 ? 33.227 11.186 37.105 1.00 28.35 ? 268 VAL A CG2 1 ATOM 2090 N N . THR A 1 273 ? 34.245 6.844 36.005 1.00 26.79 ? 269 THR A N 1 ATOM 2091 C CA . THR A 1 273 ? 34.470 5.672 35.131 1.00 27.23 ? 269 THR A CA 1 ATOM 2092 C C . THR A 1 273 ? 34.201 4.393 35.917 1.00 28.16 ? 269 THR A C 1 ATOM 2093 O O . THR A 1 273 ? 33.446 3.520 35.476 1.00 28.85 ? 269 THR A O 1 ATOM 2094 C CB . THR A 1 273 ? 35.955 5.651 34.582 1.00 27.90 ? 269 THR A CB 1 ATOM 2095 O OG1 . THR A 1 273 ? 36.153 6.825 33.758 1.00 29.01 ? 269 THR A OG1 1 ATOM 2096 C CG2 . THR A 1 273 ? 36.186 4.364 33.705 1.00 28.61 ? 269 THR A CG2 1 ATOM 2097 N N . GLY A 1 274 ? 34.810 4.276 37.094 1.00 28.19 ? 270 GLY A N 1 ATOM 2098 C CA . GLY A 1 274 ? 34.723 3.000 37.878 1.00 30.12 ? 270 GLY A CA 1 ATOM 2099 C C . GLY A 1 274 ? 33.301 2.731 38.326 1.00 31.75 ? 270 GLY A C 1 ATOM 2100 O O . GLY A 1 274 ? 32.824 1.584 38.232 1.00 32.02 ? 270 GLY A O 1 ATOM 2101 N N . TYR A 1 275 ? 32.603 3.783 38.799 1.00 29.18 ? 271 TYR A N 1 ATOM 2102 C CA . TYR A 1 275 ? 31.230 3.565 39.285 1.00 28.74 ? 271 TYR A CA 1 ATOM 2103 C C . TYR A 1 275 ? 30.116 3.823 38.232 1.00 27.95 ? 271 TYR A C 1 ATOM 2104 O O . TYR A 1 275 ? 29.378 2.903 37.847 1.00 28.41 ? 271 TYR A O 1 ATOM 2105 C CB . TYR A 1 275 ? 30.961 4.317 40.599 1.00 27.67 ? 271 TYR A CB 1 ATOM 2106 C CG . TYR A 1 275 ? 29.776 3.687 41.324 1.00 30.86 ? 271 TYR A CG 1 ATOM 2107 C CD1 . TYR A 1 275 ? 29.921 2.468 42.009 1.00 33.13 ? 271 TYR A CD1 1 ATOM 2108 C CD2 . TYR A 1 275 ? 28.490 4.247 41.217 1.00 29.35 ? 271 TYR A CD2 1 ATOM 2109 C CE1 . TYR A 1 275 ? 28.840 1.874 42.642 1.00 32.82 ? 271 TYR A CE1 1 ATOM 2110 C CE2 . TYR A 1 275 ? 27.403 3.658 41.828 1.00 29.56 ? 271 TYR A CE2 1 ATOM 2111 C CZ . TYR A 1 275 ? 27.594 2.473 42.537 1.00 33.20 ? 271 TYR A CZ 1 ATOM 2112 O OH . TYR A 1 275 ? 26.520 1.880 43.119 1.00 33.40 ? 271 TYR A OH 1 ATOM 2113 N N . LEU A 1 276 ? 30.010 5.051 37.738 1.00 26.90 ? 272 LEU A N 1 ATOM 2114 C CA . LEU A 1 276 ? 28.878 5.373 36.868 1.00 26.61 ? 272 LEU A CA 1 ATOM 2115 C C . LEU A 1 276 ? 28.943 4.539 35.607 1.00 26.59 ? 272 LEU A C 1 ATOM 2116 O O . LEU A 1 276 ? 27.963 3.870 35.241 1.00 26.64 ? 272 LEU A O 1 ATOM 2117 C CB . LEU A 1 276 ? 28.902 6.880 36.540 1.00 26.13 ? 272 LEU A CB 1 ATOM 2118 C CG . LEU A 1 276 ? 27.875 7.441 35.539 1.00 26.40 ? 272 LEU A CG 1 ATOM 2119 C CD1 . LEU A 1 276 ? 26.455 7.096 35.976 1.00 25.62 ? 272 LEU A CD1 1 ATOM 2120 C CD2 . LEU A 1 276 ? 28.096 8.977 35.390 1.00 25.65 ? 272 LEU A CD2 1 ATOM 2121 N N . LYS A 1 277 ? 30.083 4.604 34.892 1.00 27.11 ? 273 LYS A N 1 ATOM 2122 C CA . LYS A 1 277 ? 30.218 3.841 33.676 1.00 26.51 ? 273 LYS A CA 1 ATOM 2123 C C . LYS A 1 277 ? 30.359 2.327 33.911 1.00 29.18 ? 273 LYS A C 1 ATOM 2124 O O . LYS A 1 277 ? 29.580 1.537 33.341 1.00 30.08 ? 273 LYS A O 1 ATOM 2125 C CB . LYS A 1 277 ? 31.375 4.369 32.808 1.00 26.62 ? 273 LYS A CB 1 ATOM 2126 C CG . LYS A 1 277 ? 31.110 5.819 32.275 1.00 22.84 ? 273 LYS A CG 1 ATOM 2127 C CD . LYS A 1 277 ? 32.236 6.321 31.407 1.00 25.42 ? 273 LYS A CD 1 ATOM 2128 C CE . LYS A 1 277 ? 31.796 7.634 30.642 1.00 26.98 ? 273 LYS A CE 1 ATOM 2129 N NZ . LYS A 1 277 ? 32.829 7.899 29.594 1.00 28.17 ? 273 LYS A NZ 1 ATOM 2130 N N . ASP A 1 278 ? 31.356 1.915 34.686 1.00 29.80 ? 274 ASP A N 1 ATOM 2131 C CA . ASP A 1 278 ? 31.691 0.462 34.750 1.00 32.58 ? 274 ASP A CA 1 ATOM 2132 C C . ASP A 1 278 ? 30.766 -0.393 35.663 1.00 34.13 ? 274 ASP A C 1 ATOM 2133 O O . ASP A 1 278 ? 30.713 -1.640 35.515 1.00 36.57 ? 274 ASP A O 1 ATOM 2134 C CB . ASP A 1 278 ? 33.160 0.259 35.183 1.00 32.61 ? 274 ASP A CB 1 ATOM 2135 C CG . ASP A 1 278 ? 34.176 0.786 34.150 1.00 36.06 ? 274 ASP A CG 1 ATOM 2136 O OD1 . ASP A 1 278 ? 33.769 1.238 33.052 1.00 39.53 ? 274 ASP A OD1 1 ATOM 2137 O OD2 . ASP A 1 278 ? 35.401 0.756 34.447 1.00 37.24 ? 274 ASP A OD2 1 ATOM 2138 N N . THR A 1 279 ? 30.115 0.240 36.641 1.00 32.48 ? 275 THR A N 1 ATOM 2139 C CA . THR A 1 279 ? 29.306 -0.498 37.627 1.00 33.60 ? 275 THR A CA 1 ATOM 2140 C C . THR A 1 279 ? 27.825 -0.277 37.351 1.00 33.29 ? 275 THR A C 1 ATOM 2141 O O . THR A 1 279 ? 27.091 -1.251 37.183 1.00 33.48 ? 275 THR A O 1 ATOM 2142 C CB . THR A 1 279 ? 29.662 -0.146 39.103 1.00 33.20 ? 275 THR A CB 1 ATOM 2143 O OG1 . THR A 1 279 ? 31.068 -0.318 39.296 1.00 34.88 ? 275 THR A OG1 1 ATOM 2144 C CG2 . THR A 1 279 ? 28.881 -1.050 40.133 1.00 34.23 ? 275 THR A CG2 1 ATOM 2145 N N . LEU A 1 280 ? 27.405 0.983 37.230 1.00 30.72 ? 276 LEU A N 1 ATOM 2146 C CA . LEU A 1 280 ? 26.000 1.258 36.827 1.00 30.72 ? 276 LEU A CA 1 ATOM 2147 C C . LEU A 1 280 ? 25.732 1.011 35.361 1.00 29.76 ? 276 LEU A C 1 ATOM 2148 O O . LEU A 1 280 ? 24.564 1.081 34.929 1.00 30.57 ? 276 LEU A O 1 ATOM 2149 C CB . LEU A 1 280 ? 25.584 2.695 37.172 1.00 30.22 ? 276 LEU A CB 1 ATOM 2150 C CG . LEU A 1 280 ? 25.625 3.004 38.666 1.00 34.46 ? 276 LEU A CG 1 ATOM 2151 C CD1 . LEU A 1 280 ? 25.172 4.470 38.899 1.00 33.31 ? 276 LEU A CD1 1 ATOM 2152 C CD2 . LEU A 1 280 ? 24.786 1.998 39.503 1.00 37.75 ? 276 LEU A CD2 1 ATOM 2153 N N . LYS A 1 281 ? 26.801 0.776 34.581 1.00 28.48 ? 277 LYS A N 1 ATOM 2154 C CA . LYS A 1 281 ? 26.682 0.498 33.151 1.00 28.73 ? 277 LYS A CA 1 ATOM 2155 C C . LYS A 1 281 ? 26.051 1.667 32.343 1.00 27.50 ? 277 LYS A C 1 ATOM 2156 O O . LYS A 1 281 ? 25.422 1.465 31.307 1.00 26.43 ? 277 LYS A O 1 ATOM 2157 C CB . LYS A 1 281 ? 25.912 -0.824 32.934 1.00 30.52 ? 277 LYS A CB 1 ATOM 2158 C CG . LYS A 1 281 ? 26.546 -2.064 33.712 1.00 34.05 ? 277 LYS A CG 1 ATOM 2159 C CD . LYS A 1 281 ? 27.999 -2.285 33.359 1.00 39.07 ? 277 LYS A CD 1 ATOM 2160 C CE . LYS A 1 281 ? 28.573 -3.551 34.104 1.00 42.83 ? 277 LYS A CE 1 ATOM 2161 N NZ . LYS A 1 281 ? 30.025 -3.694 33.824 1.00 43.09 ? 277 LYS A NZ 1 ATOM 2162 N N . PHE A 1 282 ? 26.235 2.889 32.814 1.00 26.53 ? 278 PHE A N 1 ATOM 2163 C CA . PHE A 1 282 ? 25.757 4.048 32.040 1.00 26.59 ? 278 PHE A CA 1 ATOM 2164 C C . PHE A 1 282 ? 26.399 4.099 30.641 1.00 25.92 ? 278 PHE A C 1 ATOM 2165 O O . PHE A 1 282 ? 27.621 4.027 30.522 1.00 27.19 ? 278 PHE A O 1 ATOM 2166 C CB . PHE A 1 282 ? 26.100 5.326 32.800 1.00 25.06 ? 278 PHE A CB 1 ATOM 2167 C CG . PHE A 1 282 ? 25.671 6.575 32.086 1.00 26.16 ? 278 PHE A CG 1 ATOM 2168 C CD1 . PHE A 1 282 ? 24.331 6.734 31.701 1.00 26.43 ? 278 PHE A CD1 1 ATOM 2169 C CD2 . PHE A 1 282 ? 26.579 7.597 31.828 1.00 23.34 ? 278 PHE A CD2 1 ATOM 2170 C CE1 . PHE A 1 282 ? 23.885 7.930 31.056 1.00 23.73 ? 278 PHE A CE1 1 ATOM 2171 C CE2 . PHE A 1 282 ? 26.172 8.801 31.166 1.00 23.06 ? 278 PHE A CE2 1 ATOM 2172 C CZ . PHE A 1 282 ? 24.823 8.940 30.765 1.00 23.55 ? 278 PHE A CZ 1 ATOM 2173 N N . LYS A 1 283 ? 25.588 4.219 29.590 1.00 25.15 ? 279 LYS A N 1 ATOM 2174 C CA . LYS A 1 283 ? 26.103 4.210 28.200 1.00 25.18 ? 279 LYS A CA 1 ATOM 2175 C C . LYS A 1 283 ? 25.759 5.507 27.453 1.00 24.59 ? 279 LYS A C 1 ATOM 2176 O O . LYS A 1 283 ? 26.020 5.622 26.232 1.00 24.76 ? 279 LYS A O 1 ATOM 2177 C CB . LYS A 1 283 ? 25.483 3.010 27.424 1.00 26.12 ? 279 LYS A CB 1 ATOM 2178 C CG . LYS A 1 283 ? 25.886 1.594 28.003 1.00 30.37 ? 279 LYS A CG 1 ATOM 2179 C CD . LYS A 1 283 ? 27.380 1.330 27.859 1.00 33.07 ? 279 LYS A CD 1 ATOM 2180 C CE . LYS A 1 283 ? 27.690 -0.160 28.275 1.00 36.47 ? 279 LYS A CE 1 ATOM 2181 N NZ . LYS A 1 283 ? 29.139 -0.239 28.705 1.00 38.25 ? 279 LYS A NZ 1 ATOM 2182 N N . GLY A 1 284 ? 25.146 6.467 28.151 1.00 23.52 ? 280 GLY A N 1 ATOM 2183 C CA . GLY A 1 284 ? 24.866 7.775 27.509 1.00 23.85 ? 280 GLY A CA 1 ATOM 2184 C C . GLY A 1 284 ? 26.149 8.597 27.668 1.00 24.17 ? 280 GLY A C 1 ATOM 2185 O O . GLY A 1 284 ? 27.203 8.024 27.954 1.00 24.21 ? 280 GLY A O 1 ATOM 2186 N N . PHE A 1 285 ? 26.071 9.919 27.560 1.00 22.07 ? 281 PHE A N 1 ATOM 2187 C CA . PHE A 1 285 ? 27.275 10.708 27.723 1.00 23.46 ? 281 PHE A CA 1 ATOM 2188 C C . PHE A 1 285 ? 27.322 11.480 29.020 1.00 23.85 ? 281 PHE A C 1 ATOM 2189 O O . PHE A 1 285 ? 26.278 11.913 29.548 1.00 24.46 ? 281 PHE A O 1 ATOM 2190 C CB . PHE A 1 285 ? 27.615 11.562 26.460 1.00 22.14 ? 281 PHE A CB 1 ATOM 2191 C CG . PHE A 1 285 ? 26.696 12.781 26.183 1.00 22.75 ? 281 PHE A CG 1 ATOM 2192 C CD1 . PHE A 1 285 ? 26.884 13.992 26.882 1.00 22.37 ? 281 PHE A CD1 1 ATOM 2193 C CD2 . PHE A 1 285 ? 25.751 12.763 25.118 1.00 22.63 ? 281 PHE A CD2 1 ATOM 2194 C CE1 . PHE A 1 285 ? 26.073 15.156 26.599 1.00 23.39 ? 281 PHE A CE1 1 ATOM 2195 C CE2 . PHE A 1 285 ? 24.966 13.933 24.770 1.00 19.01 ? 281 PHE A CE2 1 ATOM 2196 C CZ . PHE A 1 285 ? 25.137 15.141 25.527 1.00 21.06 ? 281 PHE A CZ 1 ATOM 2197 N N . VAL A 1 286 ? 28.542 11.689 29.497 1.00 23.47 ? 282 VAL A N 1 ATOM 2198 C CA . VAL A 1 286 ? 28.816 12.441 30.728 1.00 22.99 ? 282 VAL A CA 1 ATOM 2199 C C . VAL A 1 286 ? 29.287 13.845 30.345 1.00 23.55 ? 282 VAL A C 1 ATOM 2200 O O . VAL A 1 286 ? 30.254 14.006 29.595 1.00 23.97 ? 282 VAL A O 1 ATOM 2201 C CB . VAL A 1 286 ? 29.953 11.759 31.547 1.00 23.70 ? 282 VAL A CB 1 ATOM 2202 C CG1 . VAL A 1 286 ? 30.374 12.659 32.725 1.00 22.27 ? 282 VAL A CG1 1 ATOM 2203 C CG2 . VAL A 1 286 ? 29.489 10.369 32.058 1.00 21.00 ? 282 VAL A CG2 1 ATOM 2204 N N . ILE A 1 287 ? 28.621 14.861 30.889 1.00 21.79 ? 283 ILE A N 1 ATOM 2205 C CA . ILE A 1 287 ? 28.992 16.227 30.551 1.00 20.99 ? 283 ILE A CA 1 ATOM 2206 C C . ILE A 1 287 ? 29.524 16.958 31.780 1.00 22.28 ? 283 ILE A C 1 ATOM 2207 O O . ILE A 1 287 ? 29.057 16.719 32.913 1.00 21.00 ? 283 ILE A O 1 ATOM 2208 C CB . ILE A 1 287 ? 27.769 16.992 29.868 1.00 20.92 ? 283 ILE A CB 1 ATOM 2209 C CG1 . ILE A 1 287 ? 28.160 18.408 29.434 1.00 19.45 ? 283 ILE A CG1 1 ATOM 2210 C CG2 . ILE A 1 287 ? 26.516 17.072 30.842 1.00 19.62 ? 283 ILE A CG2 1 ATOM 2211 C CD1 . ILE A 1 287 ? 27.029 19.077 28.555 1.00 19.99 ? 283 ILE A CD1 1 ATOM 2212 N N . SER A 1 288 ? 30.490 17.877 31.574 1.00 22.88 ? 284 SER A N 1 ATOM 2213 C CA . SER A 1 288 ? 30.939 18.690 32.677 1.00 22.47 ? 284 SER A CA 1 ATOM 2214 C C . SER A 1 288 ? 29.881 19.730 33.088 1.00 23.52 ? 284 SER A C 1 ATOM 2215 O O . SER A 1 288 ? 28.981 20.052 32.309 1.00 23.25 ? 284 SER A O 1 ATOM 2216 C CB . SER A 1 288 ? 32.213 19.464 32.279 1.00 23.26 ? 284 SER A CB 1 ATOM 2217 O OG . SER A 1 288 ? 31.920 20.656 31.554 1.00 23.08 ? 284 SER A OG 1 ATOM 2218 N N . ASP A 1 289 ? 30.065 20.337 34.268 1.00 22.29 ? 285 ASP A N 1 ATOM 2219 C CA . ASP A 1 289 ? 29.330 21.567 34.552 1.00 23.32 ? 285 ASP A CA 1 ATOM 2220 C C . ASP A 1 289 ? 30.114 22.742 33.900 1.00 22.77 ? 285 ASP A C 1 ATOM 2221 O O . ASP A 1 289 ? 31.166 22.546 33.227 1.00 23.35 ? 285 ASP A O 1 ATOM 2222 C CB . ASP A 1 289 ? 29.098 21.741 36.086 1.00 22.43 ? 285 ASP A CB 1 ATOM 2223 C CG . ASP A 1 289 ? 27.859 22.587 36.410 1.00 24.52 ? 285 ASP A CG 1 ATOM 2224 O OD1 . ASP A 1 289 ? 27.480 23.433 35.580 1.00 25.38 ? 285 ASP A OD1 1 ATOM 2225 O OD2 . ASP A 1 289 ? 27.289 22.451 37.510 1.00 26.68 ? 285 ASP A OD2 1 ATOM 2226 N N . TRP A 1 290 ? 29.555 23.929 34.044 1.00 21.70 ? 286 TRP A N 1 ATOM 2227 C CA . TRP A 1 290 ? 30.014 25.164 33.352 1.00 22.42 ? 286 TRP A CA 1 ATOM 2228 C C . TRP A 1 290 ? 31.377 25.614 33.885 1.00 23.45 ? 286 TRP A C 1 ATOM 2229 O O . TRP A 1 290 ? 31.455 26.069 35.036 1.00 23.99 ? 286 TRP A O 1 ATOM 2230 C CB . TRP A 1 290 ? 28.976 26.242 33.656 1.00 20.98 ? 286 TRP A CB 1 ATOM 2231 C CG . TRP A 1 290 ? 29.267 27.694 33.235 1.00 22.68 ? 286 TRP A CG 1 ATOM 2232 C CD1 . TRP A 1 290 ? 30.117 28.604 33.848 1.00 24.15 ? 286 TRP A CD1 1 ATOM 2233 C CD2 . TRP A 1 290 ? 28.608 28.405 32.166 1.00 20.90 ? 286 TRP A CD2 1 ATOM 2234 N NE1 . TRP A 1 290 ? 30.087 29.812 33.152 1.00 22.28 ? 286 TRP A NE1 1 ATOM 2235 C CE2 . TRP A 1 290 ? 29.117 29.733 32.162 1.00 23.18 ? 286 TRP A CE2 1 ATOM 2236 C CE3 . TRP A 1 290 ? 27.629 28.038 31.209 1.00 21.07 ? 286 TRP A CE3 1 ATOM 2237 C CZ2 . TRP A 1 290 ? 28.718 30.686 31.203 1.00 26.81 ? 286 TRP A CZ2 1 ATOM 2238 C CZ3 . TRP A 1 290 ? 27.211 29.003 30.249 1.00 24.36 ? 286 TRP A CZ3 1 ATOM 2239 C CH2 . TRP A 1 290 ? 27.746 30.305 30.263 1.00 26.05 ? 286 TRP A CH2 1 ATOM 2240 N N . GLU A 1 291 ? 32.426 25.529 33.057 1.00 22.73 ? 287 GLU A N 1 ATOM 2241 C CA . GLU A 1 291 ? 33.822 25.744 33.555 1.00 23.45 ? 287 GLU A CA 1 ATOM 2242 C C . GLU A 1 291 ? 34.104 24.795 34.715 1.00 23.50 ? 287 GLU A C 1 ATOM 2243 O O . GLU A 1 291 ? 34.971 25.078 35.563 1.00 22.66 ? 287 GLU A O 1 ATOM 2244 C CB . GLU A 1 291 ? 34.074 27.209 34.035 1.00 23.86 ? 287 GLU A CB 1 ATOM 2245 C CG . GLU A 1 291 ? 33.713 28.244 32.957 1.00 26.41 ? 287 GLU A CG 1 ATOM 2246 C CD . GLU A 1 291 ? 33.793 29.695 33.459 1.00 33.15 ? 287 GLU A CD 1 ATOM 2247 O OE1 . GLU A 1 291 ? 33.746 29.937 34.669 1.00 35.18 ? 287 GLU A OE1 1 ATOM 2248 O OE2 . GLU A 1 291 ? 33.895 30.574 32.613 1.00 36.22 ? 287 GLU A OE2 1 ATOM 2249 N N . GLY A 1 292 ? 33.392 23.671 34.752 1.00 23.06 ? 288 GLY A N 1 ATOM 2250 C CA . GLY A 1 292 ? 33.651 22.668 35.796 1.00 24.38 ? 288 GLY A CA 1 ATOM 2251 C C . GLY A 1 292 ? 35.109 22.157 35.799 1.00 25.75 ? 288 GLY A C 1 ATOM 2252 O O . GLY A 1 292 ? 35.698 21.977 36.883 1.00 25.58 ? 288 GLY A O 1 ATOM 2253 N N . ILE A 1 293 ? 35.704 21.944 34.611 1.00 24.87 ? 289 ILE A N 1 ATOM 2254 C CA . ILE A 1 293 ? 37.089 21.429 34.594 1.00 25.19 ? 289 ILE A CA 1 ATOM 2255 C C . ILE A 1 293 ? 38.078 22.495 35.057 1.00 25.83 ? 289 ILE A C 1 ATOM 2256 O O . ILE A 1 293 ? 39.038 22.174 35.775 1.00 26.16 ? 289 ILE A O 1 ATOM 2257 C CB . ILE A 1 293 ? 37.467 20.797 33.244 1.00 25.68 ? 289 ILE A CB 1 ATOM 2258 C CG1 . ILE A 1 293 ? 37.739 21.874 32.154 1.00 25.04 ? 289 ILE A CG1 1 ATOM 2259 C CG2 . ILE A 1 293 ? 36.348 19.779 32.847 1.00 24.72 ? 289 ILE A CG2 1 ATOM 2260 C CD1 . ILE A 1 293 ? 38.319 21.225 30.842 1.00 27.70 ? 289 ILE A CD1 1 ATOM 2261 N N . ASP A 1 294 ? 37.798 23.757 34.739 1.00 26.02 ? 290 ASP A N 1 ATOM 2262 C CA . ASP A 1 294 ? 38.635 24.874 35.197 1.00 26.45 ? 290 ASP A CA 1 ATOM 2263 C C . ASP A 1 294 ? 38.748 24.888 36.706 1.00 28.48 ? 290 ASP A C 1 ATOM 2264 O O . ASP A 1 294 ? 39.813 25.234 37.272 1.00 27.78 ? 290 ASP A O 1 ATOM 2265 C CB . ASP A 1 294 ? 38.019 26.219 34.801 1.00 27.40 ? 290 ASP A CB 1 ATOM 2266 C CG . ASP A 1 294 ? 37.624 26.294 33.311 1.00 29.50 ? 290 ASP A CG 1 ATOM 2267 O OD1 . ASP A 1 294 ? 36.947 25.378 32.834 1.00 26.69 ? 290 ASP A OD1 1 ATOM 2268 O OD2 . ASP A 1 294 ? 37.983 27.271 32.634 1.00 30.99 ? 290 ASP A OD2 1 ATOM 2269 N N . ARG A 1 295 ? 37.632 24.580 37.365 1.00 27.40 ? 291 ARG A N 1 ATOM 2270 C CA . ARG A 1 295 ? 37.547 24.636 38.818 1.00 29.75 ? 291 ARG A CA 1 ATOM 2271 C C . ARG A 1 295 ? 38.126 23.440 39.543 1.00 31.06 ? 291 ARG A C 1 ATOM 2272 O O . ARG A 1 295 ? 38.043 23.372 40.766 1.00 31.99 ? 291 ARG A O 1 ATOM 2273 C CB . ARG A 1 295 ? 36.074 24.891 39.236 1.00 28.37 ? 291 ARG A CB 1 ATOM 2274 C CG . ARG A 1 295 ? 35.667 26.319 38.784 1.00 29.18 ? 291 ARG A CG 1 ATOM 2275 C CD . ARG A 1 295 ? 34.191 26.680 39.129 1.00 28.00 ? 291 ARG A CD 1 ATOM 2276 N NE . ARG A 1 295 ? 33.692 27.665 38.163 1.00 29.47 ? 291 ARG A NE 1 ATOM 2277 C CZ . ARG A 1 295 ? 32.474 28.207 38.168 1.00 30.65 ? 291 ARG A CZ 1 ATOM 2278 N NH1 . ARG A 1 295 ? 31.599 27.883 39.121 1.00 32.31 ? 291 ARG A NH1 1 ATOM 2279 N NH2 . ARG A 1 295 ? 32.127 29.067 37.201 1.00 28.12 ? 291 ARG A NH2 1 ATOM 2280 N N . ILE A 1 296 ? 38.730 22.505 38.804 1.00 31.61 ? 292 ILE A N 1 ATOM 2281 C CA . ILE A 1 296 ? 39.525 21.421 39.446 1.00 31.85 ? 292 ILE A CA 1 ATOM 2282 C C . ILE A 1 296 ? 40.694 22.000 40.252 1.00 33.30 ? 292 ILE A C 1 ATOM 2283 O O . ILE A 1 296 ? 41.013 21.524 41.361 1.00 31.10 ? 292 ILE A O 1 ATOM 2284 C CB . ILE A 1 296 ? 40.041 20.401 38.398 1.00 31.89 ? 292 ILE A CB 1 ATOM 2285 C CG1 . ILE A 1 296 ? 38.862 19.527 37.919 1.00 29.38 ? 292 ILE A CG1 1 ATOM 2286 C CG2 . ILE A 1 296 ? 41.131 19.475 38.980 1.00 32.84 ? 292 ILE A CG2 1 ATOM 2287 C CD1 . ILE A 1 296 ? 39.161 18.818 36.584 1.00 29.24 ? 292 ILE A CD1 1 ATOM 2288 N N . THR A 1 297 ? 41.288 23.047 39.690 1.00 33.28 ? 293 THR A N 1 ATOM 2289 C CA . THR A 1 297 ? 42.472 23.670 40.279 1.00 35.53 ? 293 THR A CA 1 ATOM 2290 C C . THR A 1 297 ? 42.089 24.859 41.161 1.00 37.45 ? 293 THR A C 1 ATOM 2291 O O . THR A 1 297 ? 40.996 25.423 41.067 1.00 36.05 ? 293 THR A O 1 ATOM 2292 C CB . THR A 1 297 ? 43.464 24.184 39.177 1.00 34.42 ? 293 THR A CB 1 ATOM 2293 O OG1 . THR A 1 297 ? 42.839 25.262 38.449 1.00 32.30 ? 293 THR A OG1 1 ATOM 2294 C CG2 . THR A 1 297 ? 43.856 23.058 38.220 1.00 34.15 ? 293 THR A CG2 1 ATOM 2295 N N . THR A 1 298 ? 43.049 25.255 42.000 1.00 40.82 ? 294 THR A N 1 ATOM 2296 C CA . THR A 1 298 ? 42.908 26.404 42.853 1.00 43.28 ? 294 THR A CA 1 ATOM 2297 C C . THR A 1 298 ? 44.148 27.273 42.627 1.00 43.33 ? 294 THR A C 1 ATOM 2298 O O . THR A 1 298 ? 45.263 26.793 42.800 1.00 45.04 ? 294 THR A O 1 ATOM 2299 C CB . THR A 1 298 ? 42.854 25.930 44.314 1.00 44.24 ? 294 THR A CB 1 ATOM 2300 O OG1 . THR A 1 298 ? 41.663 25.146 44.499 1.00 47.57 ? 294 THR A OG1 1 ATOM 2301 C CG2 . THR A 1 298 ? 42.853 27.117 45.263 1.00 46.42 ? 294 THR A CG2 1 ATOM 2302 N N . PRO A 1 299 ? 43.967 28.524 42.168 1.00 42.66 ? 295 PRO A N 1 ATOM 2303 C CA . PRO A 1 299 ? 42.691 29.088 41.709 1.00 40.53 ? 295 PRO A CA 1 ATOM 2304 C C . PRO A 1 299 ? 42.138 28.402 40.440 1.00 39.06 ? 295 PRO A C 1 ATOM 2305 O O . PRO A 1 299 ? 42.866 27.675 39.741 1.00 37.72 ? 295 PRO A O 1 ATOM 2306 C CB . PRO A 1 299 ? 43.023 30.540 41.398 1.00 41.50 ? 295 PRO A CB 1 ATOM 2307 C CG . PRO A 1 299 ? 44.541 30.615 41.362 1.00 43.40 ? 295 PRO A CG 1 ATOM 2308 C CD . PRO A 1 299 ? 45.088 29.477 42.108 1.00 42.69 ? 295 PRO A CD 1 ATOM 2309 N N . ALA A 1 300 ? 40.863 28.661 40.156 1.00 36.46 ? 296 ALA A N 1 ATOM 2310 C CA . ALA A 1 300 ? 40.184 28.059 38.989 1.00 35.43 ? 296 ALA A CA 1 ATOM 2311 C C . ALA A 1 300 ? 40.889 28.544 37.735 1.00 34.34 ? 296 ALA A C 1 ATOM 2312 O O . ALA A 1 300 ? 41.225 29.723 37.638 1.00 35.82 ? 296 ALA A O 1 ATOM 2313 C CB . ALA A 1 300 ? 38.692 28.473 38.949 1.00 32.96 ? 296 ALA A CB 1 ATOM 2314 N N . GLY A 1 301 ? 41.070 27.665 36.761 1.00 33.09 ? 297 GLY A N 1 ATOM 2315 C CA . GLY A 1 301 ? 41.612 28.107 35.492 1.00 32.67 ? 297 GLY A CA 1 ATOM 2316 C C . GLY A 1 301 ? 43.139 28.313 35.441 1.00 33.53 ? 297 GLY A C 1 ATOM 2317 O O . GLY A 1 301 ? 43.672 28.719 34.389 1.00 33.31 ? 297 GLY A O 1 ATOM 2318 N N . SER A 1 302 ? 43.843 27.969 36.525 1.00 33.05 ? 298 SER A N 1 ATOM 2319 C CA . SER A 1 302 ? 45.272 28.271 36.642 1.00 34.45 ? 298 SER A CA 1 ATOM 2320 C C . SER A 1 302 ? 46.163 27.206 35.995 1.00 35.05 ? 298 SER A C 1 ATOM 2321 O O . SER A 1 302 ? 47.365 27.405 35.864 1.00 35.11 ? 298 SER A O 1 ATOM 2322 C CB . SER A 1 302 ? 45.658 28.493 38.135 1.00 34.64 ? 298 SER A CB 1 ATOM 2323 O OG . SER A 1 302 ? 45.602 27.284 38.899 1.00 36.76 ? 298 SER A OG 1 ATOM 2324 N N . ASP A 1 303 ? 45.602 26.054 35.622 1.00 33.07 ? 299 ASP A N 1 ATOM 2325 C CA . ASP A 1 303 ? 46.380 25.087 34.859 1.00 33.07 ? 299 ASP A CA 1 ATOM 2326 C C . ASP A 1 303 ? 45.406 24.352 33.955 1.00 31.26 ? 299 ASP A C 1 ATOM 2327 O O . ASP A 1 303 ? 44.991 23.223 34.253 1.00 29.69 ? 299 ASP A O 1 ATOM 2328 C CB . ASP A 1 303 ? 47.087 24.103 35.773 1.00 33.45 ? 299 ASP A CB 1 ATOM 2329 C CG . ASP A 1 303 ? 48.064 23.208 35.007 1.00 37.10 ? 299 ASP A CG 1 ATOM 2330 O OD1 . ASP A 1 303 ? 47.995 23.106 33.754 1.00 33.26 ? 299 ASP A OD1 1 ATOM 2331 O OD2 . ASP A 1 303 ? 48.887 22.566 35.669 1.00 40.50 ? 299 ASP A OD2 1 ATOM 2332 N N . TYR A 1 304 ? 44.989 25.032 32.890 1.00 30.49 ? 300 TYR A N 1 ATOM 2333 C CA . TYR A 1 304 ? 43.912 24.475 32.057 1.00 29.71 ? 300 TYR A CA 1 ATOM 2334 C C . TYR A 1 304 ? 44.385 23.216 31.356 1.00 29.90 ? 300 TYR A C 1 ATOM 2335 O O . TYR A 1 304 ? 43.592 22.309 31.064 1.00 29.76 ? 300 TYR A O 1 ATOM 2336 C CB . TYR A 1 304 ? 43.450 25.500 31.056 1.00 29.16 ? 300 TYR A CB 1 ATOM 2337 C CG . TYR A 1 304 ? 42.093 25.177 30.447 1.00 29.69 ? 300 TYR A CG 1 ATOM 2338 C CD1 . TYR A 1 304 ? 40.936 25.144 31.244 1.00 29.21 ? 300 TYR A CD1 1 ATOM 2339 C CD2 . TYR A 1 304 ? 41.948 24.944 29.081 1.00 31.40 ? 300 TYR A CD2 1 ATOM 2340 C CE1 . TYR A 1 304 ? 39.675 24.863 30.692 1.00 28.26 ? 300 TYR A CE1 1 ATOM 2341 C CE2 . TYR A 1 304 ? 40.645 24.669 28.509 1.00 31.47 ? 300 TYR A CE2 1 ATOM 2342 C CZ . TYR A 1 304 ? 39.532 24.621 29.349 1.00 29.83 ? 300 TYR A CZ 1 ATOM 2343 O OH . TYR A 1 304 ? 38.252 24.410 28.855 1.00 25.03 ? 300 TYR A OH 1 ATOM 2344 N N . SER A 1 305 ? 45.686 23.152 31.054 1.00 29.62 ? 301 SER A N 1 ATOM 2345 C CA . SER A 1 305 ? 46.238 21.925 30.504 1.00 28.90 ? 301 SER A CA 1 ATOM 2346 C C . SER A 1 305 ? 45.941 20.763 31.432 1.00 29.42 ? 301 SER A C 1 ATOM 2347 O O . SER A 1 305 ? 45.553 19.700 30.970 1.00 30.01 ? 301 SER A O 1 ATOM 2348 C CB . SER A 1 305 ? 47.778 22.015 30.269 1.00 30.36 ? 301 SER A CB 1 ATOM 2349 O OG . SER A 1 305 ? 48.245 20.711 29.920 1.00 31.42 ? 301 SER A OG 1 ATOM 2350 N N . TYR A 1 306 ? 46.160 20.944 32.739 1.00 28.85 ? 302 TYR A N 1 ATOM 2351 C CA . TYR A 1 306 ? 45.838 19.890 33.726 1.00 29.79 ? 302 TYR A CA 1 ATOM 2352 C C . TYR A 1 306 ? 44.321 19.666 33.844 1.00 28.68 ? 302 TYR A C 1 ATOM 2353 O O . TYR A 1 306 ? 43.851 18.532 33.933 1.00 28.02 ? 302 TYR A O 1 ATOM 2354 C CB . TYR A 1 306 ? 46.432 20.232 35.153 1.00 29.84 ? 302 TYR A CB 1 ATOM 2355 C CG . TYR A 1 306 ? 46.026 19.216 36.199 1.00 35.13 ? 302 TYR A CG 1 ATOM 2356 C CD1 . TYR A 1 306 ? 46.620 17.957 36.217 1.00 36.12 ? 302 TYR A CD1 1 ATOM 2357 C CD2 . TYR A 1 306 ? 44.980 19.481 37.122 1.00 36.31 ? 302 TYR A CD2 1 ATOM 2358 C CE1 . TYR A 1 306 ? 46.239 16.993 37.152 1.00 39.59 ? 302 TYR A CE1 1 ATOM 2359 C CE2 . TYR A 1 306 ? 44.609 18.528 38.071 1.00 36.35 ? 302 TYR A CE2 1 ATOM 2360 C CZ . TYR A 1 306 ? 45.233 17.288 38.067 1.00 39.98 ? 302 TYR A CZ 1 ATOM 2361 O OH . TYR A 1 306 ? 44.871 16.316 38.971 1.00 45.97 ? 302 TYR A OH 1 ATOM 2362 N N . SER A 1 307 ? 43.552 20.747 33.879 1.00 28.03 ? 303 SER A N 1 ATOM 2363 C CA . SER A 1 307 ? 42.051 20.609 33.848 1.00 27.32 ? 303 SER A CA 1 ATOM 2364 C C . SER A 1 307 ? 41.589 19.627 32.759 1.00 26.43 ? 303 SER A C 1 ATOM 2365 O O . SER A 1 307 ? 40.791 18.722 33.010 1.00 27.30 ? 303 SER A O 1 ATOM 2366 C CB . SER A 1 307 ? 41.393 21.977 33.635 1.00 26.92 ? 303 SER A CB 1 ATOM 2367 O OG . SER A 1 307 ? 41.558 22.764 34.803 1.00 27.31 ? 303 SER A OG 1 ATOM 2368 N N . VAL A 1 308 ? 42.095 19.798 31.544 1.00 25.28 ? 304 VAL A N 1 ATOM 2369 C CA . VAL A 1 308 ? 41.682 18.964 30.391 1.00 25.16 ? 304 VAL A CA 1 ATOM 2370 C C . VAL A 1 308 ? 42.126 17.511 30.589 1.00 26.90 ? 304 VAL A C 1 ATOM 2371 O O . VAL A 1 308 ? 41.349 16.581 30.394 1.00 26.44 ? 304 VAL A O 1 ATOM 2372 C CB . VAL A 1 308 ? 42.228 19.523 29.070 1.00 24.06 ? 304 VAL A CB 1 ATOM 2373 C CG1 . VAL A 1 308 ? 41.847 18.584 27.882 1.00 21.75 ? 304 VAL A CG1 1 ATOM 2374 C CG2 . VAL A 1 308 ? 41.643 20.925 28.793 1.00 23.84 ? 304 VAL A CG2 1 ATOM 2375 N N . LYS A 1 309 ? 43.395 17.338 30.969 1.00 25.92 ? 305 LYS A N 1 ATOM 2376 C CA . LYS A 1 309 ? 43.933 16.015 31.179 1.00 28.23 ? 305 LYS A CA 1 ATOM 2377 C C . LYS A 1 309 ? 43.147 15.289 32.265 1.00 27.42 ? 305 LYS A C 1 ATOM 2378 O O . LYS A 1 309 ? 42.637 14.166 32.029 1.00 27.30 ? 305 LYS A O 1 ATOM 2379 C CB . LYS A 1 309 ? 45.420 16.138 31.635 1.00 28.64 ? 305 LYS A CB 1 ATOM 2380 C CG . LYS A 1 309 ? 46.057 14.804 31.919 1.00 34.95 ? 305 LYS A CG 1 ATOM 2381 C CD . LYS A 1 309 ? 47.578 14.992 32.296 1.00 36.99 ? 305 LYS A CD 1 ATOM 2382 C CE . LYS A 1 309 ? 47.937 14.143 33.476 1.00 40.16 ? 305 LYS A CE 1 ATOM 2383 N NZ . LYS A 1 309 ? 49.441 13.991 33.668 1.00 42.23 ? 305 LYS A NZ 1 ATOM 2384 N N . ALA A 1 310 ? 43.011 15.925 33.437 1.00 26.76 ? 306 ALA A N 1 ATOM 2385 C CA . ALA A 1 310 ? 42.382 15.248 34.582 1.00 27.27 ? 306 ALA A CA 1 ATOM 2386 C C . ALA A 1 310 ? 40.933 14.837 34.281 1.00 27.18 ? 306 ALA A C 1 ATOM 2387 O O . ALA A 1 310 ? 40.474 13.723 34.637 1.00 24.92 ? 306 ALA A O 1 ATOM 2388 C CB . ALA A 1 310 ? 42.385 16.162 35.797 1.00 28.15 ? 306 ALA A CB 1 ATOM 2389 N N . SER A 1 311 ? 40.196 15.767 33.659 1.00 25.68 ? 307 SER A N 1 ATOM 2390 C CA . SER A 1 311 ? 38.756 15.533 33.427 1.00 25.11 ? 307 SER A CA 1 ATOM 2391 C C . SER A 1 311 ? 38.484 14.482 32.364 1.00 24.26 ? 307 SER A C 1 ATOM 2392 O O . SER A 1 311 ? 37.615 13.634 32.511 1.00 25.09 ? 307 SER A O 1 ATOM 2393 C CB . SER A 1 311 ? 38.043 16.853 33.098 1.00 23.96 ? 307 SER A CB 1 ATOM 2394 O OG . SER A 1 311 ? 38.491 17.394 31.837 1.00 25.00 ? 307 SER A OG 1 ATOM 2395 N N . ILE A 1 312 ? 39.199 14.547 31.256 1.00 24.41 ? 308 ILE A N 1 ATOM 2396 C CA . ILE A 1 312 ? 38.980 13.573 30.183 1.00 24.12 ? 308 ILE A CA 1 ATOM 2397 C C . ILE A 1 312 ? 39.496 12.202 30.646 1.00 25.66 ? 308 ILE A C 1 ATOM 2398 O O . ILE A 1 312 ? 38.871 11.177 30.385 1.00 26.23 ? 308 ILE A O 1 ATOM 2399 C CB . ILE A 1 312 ? 39.725 14.040 28.873 1.00 25.06 ? 308 ILE A CB 1 ATOM 2400 C CG1 . ILE A 1 312 ? 39.159 15.396 28.347 1.00 23.90 ? 308 ILE A CG1 1 ATOM 2401 C CG2 . ILE A 1 312 ? 39.664 12.917 27.801 1.00 24.31 ? 308 ILE A CG2 1 ATOM 2402 C CD1 . ILE A 1 312 ? 37.528 15.382 28.131 1.00 22.35 ? 308 ILE A CD1 1 ATOM 2403 N N . LEU A 1 313 ? 40.645 12.167 31.356 1.00 25.39 ? 309 LEU A N 1 ATOM 2404 C CA . LEU A 1 313 ? 41.101 10.870 31.889 1.00 25.98 ? 309 LEU A CA 1 ATOM 2405 C C . LEU A 1 313 ? 40.125 10.335 32.960 1.00 25.67 ? 309 LEU A C 1 ATOM 2406 O O . LEU A 1 313 ? 39.974 9.107 33.132 1.00 27.00 ? 309 LEU A O 1 ATOM 2407 C CB . LEU A 1 313 ? 42.536 10.965 32.442 1.00 27.19 ? 309 LEU A CB 1 ATOM 2408 C CG . LEU A 1 313 ? 43.537 11.165 31.293 1.00 27.56 ? 309 LEU A CG 1 ATOM 2409 C CD1 . LEU A 1 313 ? 44.957 11.320 31.953 1.00 27.93 ? 309 LEU A CD1 1 ATOM 2410 C CD2 . LEU A 1 313 ? 43.509 9.997 30.246 1.00 28.60 ? 309 LEU A CD2 1 ATOM 2411 N N . ALA A 1 314 ? 39.460 11.229 33.678 1.00 23.91 ? 310 ALA A N 1 ATOM 2412 C CA . ALA A 1 314 ? 38.482 10.789 34.684 1.00 24.75 ? 310 ALA A CA 1 ATOM 2413 C C . ALA A 1 314 ? 37.284 10.089 34.032 1.00 25.00 ? 310 ALA A C 1 ATOM 2414 O O . ALA A 1 314 ? 36.609 9.282 34.689 1.00 26.75 ? 310 ALA A O 1 ATOM 2415 C CB . ALA A 1 314 ? 37.998 11.983 35.572 1.00 23.87 ? 310 ALA A CB 1 ATOM 2416 N N . GLY A 1 315 ? 37.043 10.384 32.748 1.00 24.16 ? 311 GLY A N 1 ATOM 2417 C CA . GLY A 1 315 ? 35.952 9.753 32.013 1.00 23.96 ? 311 GLY A CA 1 ATOM 2418 C C . GLY A 1 315 ? 34.861 10.702 31.514 1.00 23.46 ? 311 GLY A C 1 ATOM 2419 O O . GLY A 1 315 ? 33.833 10.236 30.969 1.00 23.30 ? 311 GLY A O 1 ATOM 2420 N N . LEU A 1 316 ? 35.045 12.014 31.681 1.00 24.24 ? 312 LEU A N 1 ATOM 2421 C CA . LEU A 1 316 ? 34.040 12.962 31.119 1.00 23.22 ? 312 LEU A CA 1 ATOM 2422 C C . LEU A 1 316 ? 34.065 12.861 29.618 1.00 24.21 ? 312 LEU A C 1 ATOM 2423 O O . LEU A 1 316 ? 35.160 12.722 29.015 1.00 22.99 ? 312 LEU A O 1 ATOM 2424 C CB . LEU A 1 316 ? 34.263 14.394 31.614 1.00 23.99 ? 312 LEU A CB 1 ATOM 2425 C CG . LEU A 1 316 ? 33.729 14.683 33.025 1.00 23.69 ? 312 LEU A CG 1 ATOM 2426 C CD1 . LEU A 1 316 ? 34.619 14.022 34.150 1.00 25.19 ? 312 LEU A CD1 1 ATOM 2427 C CD2 . LEU A 1 316 ? 33.673 16.201 33.252 1.00 23.92 ? 312 LEU A CD2 1 ATOM 2428 N N . ASP A 1 317 ? 32.881 12.996 28.982 1.00 23.01 ? 313 ASP A N 1 ATOM 2429 C CA . ASP A 1 317 ? 32.779 12.821 27.519 1.00 22.66 ? 313 ASP A CA 1 ATOM 2430 C C . ASP A 1 317 ? 32.600 14.124 26.778 1.00 22.48 ? 313 ASP A C 1 ATOM 2431 O O . ASP A 1 317 ? 33.159 14.297 25.706 1.00 22.55 ? 313 ASP A O 1 ATOM 2432 C CB . ASP A 1 317 ? 31.591 11.882 27.154 1.00 22.54 ? 313 ASP A CB 1 ATOM 2433 C CG . ASP A 1 317 ? 31.658 10.559 27.903 1.00 25.83 ? 313 ASP A CG 1 ATOM 2434 O OD1 . ASP A 1 317 ? 32.734 9.877 27.834 1.00 22.66 ? 313 ASP A OD1 1 ATOM 2435 O OD2 . ASP A 1 317 ? 30.636 10.157 28.528 1.00 23.30 ? 313 ASP A OD2 1 ATOM 2436 N N . MET A 1 318 ? 31.770 15.036 27.308 1.00 22.34 ? 314 MET A N 1 ATOM 2437 C CA . MET A 1 318 ? 31.552 16.314 26.649 1.00 22.53 ? 314 MET A CA 1 ATOM 2438 C C . MET A 1 318 ? 31.854 17.437 27.646 1.00 22.47 ? 314 MET A C 1 ATOM 2439 O O . MET A 1 318 ? 31.467 17.365 28.791 1.00 22.72 ? 314 MET A O 1 ATOM 2440 C CB . MET A 1 318 ? 30.076 16.466 26.195 1.00 21.93 ? 314 MET A CB 1 ATOM 2441 C CG . MET A 1 318 ? 29.777 17.819 25.453 1.00 22.96 ? 314 MET A CG 1 ATOM 2442 S SD . MET A 1 318 ? 28.022 17.945 24.986 1.00 23.02 ? 314 MET A SD 1 ATOM 2443 C CE . MET A 1 318 ? 27.984 16.652 23.691 1.00 17.87 ? 314 MET A CE 1 ATOM 2444 N N . ILE A 1 319 ? 32.517 18.483 27.183 1.00 21.76 ? 315 ILE A N 1 ATOM 2445 C CA . ILE A 1 319 ? 32.903 19.538 28.091 1.00 21.67 ? 315 ILE A CA 1 ATOM 2446 C C . ILE A 1 319 ? 32.101 20.785 27.766 1.00 21.76 ? 315 ILE A C 1 ATOM 2447 O O . ILE A 1 319 ? 32.095 21.290 26.613 1.00 21.63 ? 315 ILE A O 1 ATOM 2448 C CB . ILE A 1 319 ? 34.416 19.857 28.019 1.00 21.39 ? 315 ILE A CB 1 ATOM 2449 C CG1 . ILE A 1 319 ? 35.274 18.586 28.334 1.00 22.45 ? 315 ILE A CG1 1 ATOM 2450 C CG2 . ILE A 1 319 ? 34.789 21.101 28.963 1.00 20.50 ? 315 ILE A CG2 1 ATOM 2451 C CD1 . ILE A 1 319 ? 34.997 17.892 29.717 1.00 21.82 ? 315 ILE A CD1 1 ATOM 2452 N N . MET A 1 320 ? 31.465 21.287 28.812 1.00 21.35 ? 316 MET A N 1 ATOM 2453 C CA . MET A 1 320 ? 30.732 22.551 28.763 1.00 20.95 ? 316 MET A CA 1 ATOM 2454 C C . MET A 1 320 ? 31.775 23.631 28.937 1.00 22.27 ? 316 MET A C 1 ATOM 2455 O O . MET A 1 320 ? 32.071 24.025 30.076 1.00 23.50 ? 316 MET A O 1 ATOM 2456 C CB . MET A 1 320 ? 29.672 22.575 29.900 1.00 20.81 ? 316 MET A CB 1 ATOM 2457 C CG . MET A 1 320 ? 28.788 23.849 29.865 1.00 20.86 ? 316 MET A CG 1 ATOM 2458 S SD . MET A 1 320 ? 27.541 23.926 31.186 1.00 22.07 ? 316 MET A SD 1 ATOM 2459 C CE . MET A 1 320 ? 26.614 22.408 30.880 1.00 17.86 ? 316 MET A CE 1 ATOM 2460 N N . VAL A 1 321 ? 32.341 24.130 27.827 1.00 22.22 ? 317 VAL A N 1 ATOM 2461 C CA . VAL A 1 321 ? 33.622 24.887 27.936 1.00 22.25 ? 317 VAL A CA 1 ATOM 2462 C C . VAL A 1 321 ? 33.459 26.133 28.849 1.00 22.94 ? 317 VAL A C 1 ATOM 2463 O O . VAL A 1 321 ? 34.197 26.234 29.845 1.00 23.03 ? 317 VAL A O 1 ATOM 2464 C CB . VAL A 1 321 ? 34.314 25.154 26.567 1.00 22.15 ? 317 VAL A CB 1 ATOM 2465 C CG1 . VAL A 1 321 ? 35.704 25.882 26.768 1.00 22.40 ? 317 VAL A CG1 1 ATOM 2466 C CG2 . VAL A 1 321 ? 34.567 23.804 25.854 1.00 23.34 ? 317 VAL A CG2 1 ATOM 2467 N N . PRO A 1 322 ? 32.495 27.049 28.557 1.00 21.92 ? 318 PRO A N 1 ATOM 2468 C CA . PRO A 1 322 ? 31.630 27.095 27.359 1.00 22.45 ? 318 PRO A CA 1 ATOM 2469 C C . PRO A 1 322 ? 32.130 28.149 26.360 1.00 23.97 ? 318 PRO A C 1 ATOM 2470 O O . PRO A 1 322 ? 31.581 28.257 25.258 1.00 23.22 ? 318 PRO A O 1 ATOM 2471 C CB . PRO A 1 322 ? 30.272 27.550 27.953 1.00 22.35 ? 318 PRO A CB 1 ATOM 2472 C CG . PRO A 1 322 ? 30.689 28.596 28.997 1.00 23.20 ? 318 PRO A CG 1 ATOM 2473 C CD . PRO A 1 322 ? 32.001 27.970 29.603 1.00 22.22 ? 318 PRO A CD 1 ATOM 2474 N N . ASN A 1 323 ? 33.147 28.946 26.752 1.00 23.84 ? 319 ASN A N 1 ATOM 2475 C CA . ASN A 1 323 ? 33.555 30.117 25.941 1.00 26.16 ? 319 ASN A CA 1 ATOM 2476 C C . ASN A 1 323 ? 34.859 29.913 25.181 1.00 28.22 ? 319 ASN A C 1 ATOM 2477 O O . ASN A 1 323 ? 34.917 30.153 23.962 1.00 28.74 ? 319 ASN A O 1 ATOM 2478 C CB . ASN A 1 323 ? 33.653 31.386 26.805 1.00 25.87 ? 319 ASN A CB 1 ATOM 2479 C CG . ASN A 1 323 ? 32.346 31.740 27.447 1.00 27.61 ? 319 ASN A CG 1 ATOM 2480 O OD1 . ASN A 1 323 ? 31.268 31.621 26.828 1.00 28.75 ? 319 ASN A OD1 1 ATOM 2481 N ND2 . ASN A 1 323 ? 32.404 32.155 28.695 1.00 28.71 ? 319 ASN A ND2 1 ATOM 2482 N N . LYS A 1 324 ? 35.905 29.445 25.894 1.00 28.47 ? 320 LYS A N 1 ATOM 2483 C CA . LYS A 1 324 ? 37.228 29.226 25.304 1.00 29.33 ? 320 LYS A CA 1 ATOM 2484 C C . LYS A 1 324 ? 37.426 27.953 24.544 1.00 29.04 ? 320 LYS A C 1 ATOM 2485 O O . LYS A 1 324 ? 38.331 27.146 24.886 1.00 27.83 ? 320 LYS A O 1 ATOM 2486 C CB . LYS A 1 324 ? 38.306 29.328 26.403 1.00 32.18 ? 320 LYS A CB 1 ATOM 2487 C CG . LYS A 1 324 ? 38.571 30.747 26.762 1.00 36.93 ? 320 LYS A CG 1 ATOM 2488 C CD . LYS A 1 324 ? 39.157 31.530 25.483 1.00 44.09 ? 320 LYS A CD 1 ATOM 2489 C CE . LYS A 1 324 ? 40.418 30.890 24.675 1.00 44.98 ? 320 LYS A CE 1 ATOM 2490 N NZ . LYS A 1 324 ? 40.103 29.937 23.488 1.00 33.31 ? 320 LYS A NZ 1 ATOM 2491 N N . TYR A 1 325 ? 36.623 27.753 23.483 1.00 26.48 ? 321 TYR A N 1 ATOM 2492 C CA . TYR A 1 325 ? 36.689 26.505 22.743 1.00 27.13 ? 321 TYR A CA 1 ATOM 2493 C C . TYR A 1 325 ? 38.056 26.343 22.029 1.00 26.85 ? 321 TYR A C 1 ATOM 2494 O O . TYR A 1 325 ? 38.561 25.236 21.868 1.00 27.20 ? 321 TYR A O 1 ATOM 2495 C CB . TYR A 1 325 ? 35.563 26.412 21.695 1.00 25.32 ? 321 TYR A CB 1 ATOM 2496 C CG . TYR A 1 325 ? 35.527 27.597 20.780 1.00 27.04 ? 321 TYR A CG 1 ATOM 2497 C CD1 . TYR A 1 325 ? 36.353 27.666 19.635 1.00 25.95 ? 321 TYR A CD1 1 ATOM 2498 C CD2 . TYR A 1 325 ? 34.706 28.673 21.069 1.00 28.53 ? 321 TYR A CD2 1 ATOM 2499 C CE1 . TYR A 1 325 ? 36.345 28.812 18.780 1.00 25.52 ? 321 TYR A CE1 1 ATOM 2500 C CE2 . TYR A 1 325 ? 34.685 29.792 20.266 1.00 27.69 ? 321 TYR A CE2 1 ATOM 2501 C CZ . TYR A 1 325 ? 35.509 29.864 19.132 1.00 27.82 ? 321 TYR A CZ 1 ATOM 2502 O OH . TYR A 1 325 ? 35.468 31.007 18.375 1.00 30.28 ? 321 TYR A OH 1 ATOM 2503 N N . GLN A 1 326 ? 38.621 27.432 21.544 1.00 28.08 ? 322 GLN A N 1 ATOM 2504 C CA . GLN A 1 326 ? 39.835 27.285 20.749 1.00 28.98 ? 322 GLN A CA 1 ATOM 2505 C C . GLN A 1 326 ? 40.920 26.705 21.676 1.00 28.07 ? 322 GLN A C 1 ATOM 2506 O O . GLN A 1 326 ? 41.587 25.733 21.311 1.00 28.99 ? 322 GLN A O 1 ATOM 2507 C CB . GLN A 1 326 ? 40.285 28.634 20.182 1.00 30.88 ? 322 GLN A CB 1 ATOM 2508 C CG . GLN A 1 326 ? 41.556 28.524 19.246 1.00 36.76 ? 322 GLN A CG 1 ATOM 2509 C CD . GLN A 1 326 ? 42.198 29.922 19.082 1.00 44.74 ? 322 GLN A CD 1 ATOM 2510 O OE1 . GLN A 1 326 ? 41.610 30.772 18.436 1.00 46.27 ? 322 GLN A OE1 1 ATOM 2511 N NE2 . GLN A 1 326 ? 43.358 30.174 19.738 1.00 46.51 ? 322 GLN A NE2 1 ATOM 2512 N N . GLN A 1 327 ? 41.063 27.271 22.863 1.00 28.41 ? 323 GLN A N 1 ATOM 2513 C CA . GLN A 1 327 ? 42.049 26.733 23.859 1.00 29.74 ? 323 GLN A CA 1 ATOM 2514 C C . GLN A 1 327 ? 41.758 25.275 24.257 1.00 28.45 ? 323 GLN A C 1 ATOM 2515 O O . GLN A 1 327 ? 42.654 24.454 24.324 1.00 28.00 ? 323 GLN A O 1 ATOM 2516 C CB . GLN A 1 327 ? 42.072 27.601 25.098 1.00 30.95 ? 323 GLN A CB 1 ATOM 2517 C CG . GLN A 1 327 ? 43.296 27.312 25.907 1.00 38.51 ? 323 GLN A CG 1 ATOM 2518 C CD . GLN A 1 327 ? 43.310 27.915 27.311 1.00 45.87 ? 323 GLN A CD 1 ATOM 2519 O OE1 . GLN A 1 327 ? 42.328 28.477 27.802 1.00 49.80 ? 323 GLN A OE1 1 ATOM 2520 N NE2 . GLN A 1 327 ? 44.426 27.723 27.984 1.00 47.98 ? 323 GLN A NE2 1 ATOM 2521 N N . PHE A 1 328 ? 40.478 24.950 24.500 1.00 26.27 ? 324 PHE A N 1 ATOM 2522 C CA . PHE A 1 328 ? 40.101 23.606 24.916 1.00 23.75 ? 324 PHE A CA 1 ATOM 2523 C C . PHE A 1 328 ? 40.486 22.652 23.799 1.00 24.19 ? 324 PHE A C 1 ATOM 2524 O O . PHE A 1 328 ? 41.168 21.664 24.053 1.00 24.78 ? 324 PHE A O 1 ATOM 2525 C CB . PHE A 1 328 ? 38.543 23.508 25.248 1.00 23.35 ? 324 PHE A CB 1 ATOM 2526 C CG . PHE A 1 328 ? 38.091 22.092 25.419 1.00 23.40 ? 324 PHE A CG 1 ATOM 2527 C CD1 . PHE A 1 328 ? 38.441 21.372 26.591 1.00 23.07 ? 324 PHE A CD1 1 ATOM 2528 C CD2 . PHE A 1 328 ? 37.397 21.463 24.420 1.00 23.75 ? 324 PHE A CD2 1 ATOM 2529 C CE1 . PHE A 1 328 ? 38.043 20.036 26.726 1.00 23.48 ? 324 PHE A CE1 1 ATOM 2530 C CE2 . PHE A 1 328 ? 37.022 20.145 24.533 1.00 23.54 ? 324 PHE A CE2 1 ATOM 2531 C CZ . PHE A 1 328 ? 37.383 19.419 25.688 1.00 24.45 ? 324 PHE A CZ 1 ATOM 2532 N N . ILE A 1 329 ? 40.093 22.944 22.551 1.00 23.44 ? 325 ILE A N 1 ATOM 2533 C CA . ILE A 1 329 ? 40.370 22.020 21.437 1.00 25.40 ? 325 ILE A CA 1 ATOM 2534 C C . ILE A 1 329 ? 41.895 21.870 21.222 1.00 24.49 ? 325 ILE A C 1 ATOM 2535 O O . ILE A 1 329 ? 42.387 20.767 21.011 1.00 25.32 ? 325 ILE A O 1 ATOM 2536 C CB . ILE A 1 329 ? 39.670 22.448 20.101 1.00 25.06 ? 325 ILE A CB 1 ATOM 2537 C CG1 . ILE A 1 329 ? 38.138 22.225 20.250 1.00 27.08 ? 325 ILE A CG1 1 ATOM 2538 C CG2 . ILE A 1 329 ? 40.166 21.618 18.877 1.00 26.83 ? 325 ILE A CG2 1 ATOM 2539 C CD1 . ILE A 1 329 ? 37.328 23.008 19.167 1.00 24.23 ? 325 ILE A CD1 1 ATOM 2540 N N . SER A 1 330 ? 42.597 22.987 21.294 1.00 24.99 ? 326 SER A N 1 ATOM 2541 C CA . SER A 1 330 ? 44.049 22.972 21.063 1.00 25.88 ? 326 SER A CA 1 ATOM 2542 C C . SER A 1 330 ? 44.785 22.084 22.098 1.00 24.90 ? 326 SER A C 1 ATOM 2543 O O . SER A 1 330 ? 45.614 21.253 21.732 1.00 26.07 ? 326 SER A O 1 ATOM 2544 C CB . SER A 1 330 ? 44.608 24.387 21.138 1.00 25.69 ? 326 SER A CB 1 ATOM 2545 O OG . SER A 1 330 ? 46.026 24.312 20.800 1.00 30.05 ? 326 SER A OG 1 ATOM 2546 N N . ILE A 1 331 ? 44.427 22.243 23.368 1.00 26.21 ? 327 ILE A N 1 ATOM 2547 C CA . ILE A 1 331 ? 45.076 21.530 24.499 1.00 25.91 ? 327 ILE A CA 1 ATOM 2548 C C . ILE A 1 331 ? 44.755 20.066 24.427 1.00 26.96 ? 327 ILE A C 1 ATOM 2549 O O . ILE A 1 331 ? 45.654 19.244 24.582 1.00 25.52 ? 327 ILE A O 1 ATOM 2550 C CB . ILE A 1 331 ? 44.658 22.108 25.864 1.00 26.51 ? 327 ILE A CB 1 ATOM 2551 C CG1 . ILE A 1 331 ? 45.411 23.435 26.071 1.00 28.51 ? 327 ILE A CG1 1 ATOM 2552 C CG2 . ILE A 1 331 ? 44.974 21.120 27.055 1.00 24.89 ? 327 ILE A CG2 1 ATOM 2553 C CD1 . ILE A 1 331 ? 44.977 24.194 27.281 1.00 32.84 ? 327 ILE A CD1 1 ATOM 2554 N N . LEU A 1 332 ? 43.483 19.725 24.137 1.00 24.98 ? 328 LEU A N 1 ATOM 2555 C CA . LEU A 1 332 ? 43.114 18.327 24.061 1.00 25.38 ? 328 LEU A CA 1 ATOM 2556 C C . LEU A 1 332 ? 43.766 17.674 22.849 1.00 25.46 ? 328 LEU A C 1 ATOM 2557 O O . LEU A 1 332 ? 44.257 16.541 22.940 1.00 24.67 ? 328 LEU A O 1 ATOM 2558 C CB . LEU A 1 332 ? 41.545 18.155 23.993 1.00 24.55 ? 328 LEU A CB 1 ATOM 2559 C CG . LEU A 1 332 ? 41.026 16.706 23.973 1.00 26.15 ? 328 LEU A CG 1 ATOM 2560 C CD1 . LEU A 1 332 ? 41.644 15.846 25.108 1.00 26.08 ? 328 LEU A CD1 1 ATOM 2561 C CD2 . LEU A 1 332 ? 39.407 16.736 24.115 1.00 23.98 ? 328 LEU A CD2 1 ATOM 2562 N N . THR A 1 333 ? 43.758 18.371 21.703 1.00 26.22 ? 329 THR A N 1 ATOM 2563 C CA . THR A 1 333 ? 44.498 17.853 20.542 1.00 26.82 ? 329 THR A CA 1 ATOM 2564 C C . THR A 1 333 ? 45.987 17.550 20.890 1.00 26.21 ? 329 THR A C 1 ATOM 2565 O O . THR A 1 333 ? 46.527 16.502 20.513 1.00 28.12 ? 329 THR A O 1 ATOM 2566 C CB . THR A 1 333 ? 44.429 18.869 19.375 1.00 26.89 ? 329 THR A CB 1 ATOM 2567 O OG1 . THR A 1 333 ? 43.040 19.132 19.070 1.00 26.53 ? 329 THR A OG1 1 ATOM 2568 C CG2 . THR A 1 333 ? 45.145 18.300 18.093 1.00 29.28 ? 329 THR A CG2 1 ATOM 2569 N N . GLY A 1 334 ? 46.646 18.484 21.567 1.00 27.90 ? 330 GLY A N 1 ATOM 2570 C CA . GLY A 1 334 ? 48.064 18.303 21.969 1.00 27.54 ? 330 GLY A CA 1 ATOM 2571 C C . GLY A 1 334 ? 48.267 17.082 22.879 1.00 28.82 ? 330 GLY A C 1 ATOM 2572 O O . GLY A 1 334 ? 49.235 16.316 22.732 1.00 28.18 ? 330 GLY A O 1 ATOM 2573 N N . HIS A 1 335 ? 47.375 16.909 23.854 1.00 27.55 ? 331 HIS A N 1 ATOM 2574 C CA . HIS A 1 335 ? 47.429 15.729 24.737 1.00 28.63 ? 331 HIS A CA 1 ATOM 2575 C C . HIS A 1 335 ? 47.288 14.412 23.977 1.00 27.80 ? 331 HIS A C 1 ATOM 2576 O O . HIS A 1 335 ? 47.965 13.440 24.285 1.00 28.72 ? 331 HIS A O 1 ATOM 2577 C CB . HIS A 1 335 ? 46.313 15.831 25.836 1.00 28.02 ? 331 HIS A CB 1 ATOM 2578 C CG . HIS A 1 335 ? 46.694 16.759 26.943 1.00 30.44 ? 331 HIS A CG 1 ATOM 2579 N ND1 . HIS A 1 335 ? 45.779 17.439 27.718 1.00 32.14 ? 331 HIS A ND1 1 ATOM 2580 C CD2 . HIS A 1 335 ? 47.919 17.144 27.386 1.00 30.95 ? 331 HIS A CD2 1 ATOM 2581 C CE1 . HIS A 1 335 ? 46.418 18.189 28.605 1.00 31.14 ? 331 HIS A CE1 1 ATOM 2582 N NE2 . HIS A 1 335 ? 47.717 18.035 28.418 1.00 35.50 ? 331 HIS A NE2 1 ATOM 2583 N N . VAL A 1 336 ? 46.377 14.360 23.023 1.00 26.78 ? 332 VAL A N 1 ATOM 2584 C CA . VAL A 1 336 ? 46.216 13.154 22.245 1.00 27.41 ? 332 VAL A CA 1 ATOM 2585 C C . VAL A 1 336 ? 47.500 12.983 21.373 1.00 29.65 ? 332 VAL A C 1 ATOM 2586 O O . VAL A 1 336 ? 48.042 11.866 21.288 1.00 30.82 ? 332 VAL A O 1 ATOM 2587 C CB . VAL A 1 336 ? 44.933 13.204 21.376 1.00 26.13 ? 332 VAL A CB 1 ATOM 2588 C CG1 . VAL A 1 336 ? 44.842 11.976 20.478 1.00 26.56 ? 332 VAL A CG1 1 ATOM 2589 C CG2 . VAL A 1 336 ? 43.674 13.325 22.312 1.00 25.03 ? 332 VAL A CG2 1 ATOM 2590 N N . ASN A 1 337 ? 47.956 14.072 20.754 1.00 30.52 ? 333 ASN A N 1 ATOM 2591 C CA . ASN A 1 337 ? 49.150 14.035 19.837 1.00 31.91 ? 333 ASN A CA 1 ATOM 2592 C C . ASN A 1 337 ? 50.381 13.561 20.640 1.00 32.84 ? 333 ASN A C 1 ATOM 2593 O O . ASN A 1 337 ? 51.210 12.833 20.099 1.00 33.91 ? 333 ASN A O 1 ATOM 2594 C CB . ASN A 1 337 ? 49.433 15.407 19.139 1.00 31.84 ? 333 ASN A CB 1 ATOM 2595 C CG . ASN A 1 337 ? 48.475 15.721 17.971 1.00 33.91 ? 333 ASN A CG 1 ATOM 2596 O OD1 . ASN A 1 337 ? 47.823 14.821 17.432 1.00 31.31 ? 333 ASN A OD1 1 ATOM 2597 N ND2 . ASN A 1 337 ? 48.383 17.027 17.576 1.00 32.66 ? 333 ASN A ND2 1 ATOM 2598 N N . GLY A 1 338 ? 50.458 13.901 21.924 1.00 33.58 ? 334 GLY A N 1 ATOM 2599 C CA . GLY A 1 338 ? 51.583 13.500 22.774 1.00 35.21 ? 334 GLY A CA 1 ATOM 2600 C C . GLY A 1 338 ? 51.430 12.191 23.551 1.00 36.29 ? 334 GLY A C 1 ATOM 2601 O O . GLY A 1 338 ? 52.311 11.835 24.362 1.00 35.92 ? 334 GLY A O 1 ATOM 2602 N N . GLY A 1 339 ? 50.315 11.478 23.336 1.00 34.24 ? 335 GLY A N 1 ATOM 2603 C CA . GLY A 1 339 ? 50.126 10.181 23.971 1.00 33.70 ? 335 GLY A CA 1 ATOM 2604 C C . GLY A 1 339 ? 49.695 10.249 25.419 1.00 33.08 ? 335 GLY A C 1 ATOM 2605 O O . GLY A 1 339 ? 49.573 9.227 26.080 1.00 33.96 ? 335 GLY A O 1 ATOM 2606 N N . VAL A 1 340 ? 49.395 11.449 25.907 1.00 32.18 ? 336 VAL A N 1 ATOM 2607 C CA . VAL A 1 340 ? 48.966 11.643 27.277 1.00 31.67 ? 336 VAL A CA 1 ATOM 2608 C C . VAL A 1 340 ? 47.514 11.171 27.498 1.00 31.66 ? 336 VAL A C 1 ATOM 2609 O O . VAL A 1 340 ? 47.139 10.690 28.575 1.00 30.57 ? 336 VAL A O 1 ATOM 2610 C CB . VAL A 1 340 ? 49.075 13.133 27.636 1.00 31.78 ? 336 VAL A CB 1 ATOM 2611 C CG1 . VAL A 1 340 ? 48.331 13.430 28.952 1.00 32.17 ? 336 VAL A CG1 1 ATOM 2612 C CG2 . VAL A 1 340 ? 50.588 13.578 27.666 1.00 34.92 ? 336 VAL A CG2 1 ATOM 2613 N N . ILE A 1 341 ? 46.704 11.314 26.458 1.00 31.34 ? 337 ILE A N 1 ATOM 2614 C CA . ILE A 1 341 ? 45.312 10.799 26.460 1.00 29.51 ? 337 ILE A CA 1 ATOM 2615 C C . ILE A 1 341 ? 45.207 9.878 25.268 1.00 28.99 ? 337 ILE A C 1 ATOM 2616 O O . ILE A 1 341 ? 45.439 10.301 24.144 1.00 29.08 ? 337 ILE A O 1 ATOM 2617 C CB . ILE A 1 341 ? 44.272 11.967 26.340 1.00 29.09 ? 337 ILE A CB 1 ATOM 2618 C CG1 . ILE A 1 341 ? 44.324 12.872 27.593 1.00 29.59 ? 337 ILE A CG1 1 ATOM 2619 C CG2 . ILE A 1 341 ? 42.841 11.399 26.065 1.00 25.36 ? 337 ILE A CG2 1 ATOM 2620 C CD1 . ILE A 1 341 ? 43.540 14.229 27.441 1.00 30.02 ? 337 ILE A CD1 1 ATOM 2621 N N . PRO A 1 342 ? 44.909 8.598 25.503 1.00 28.45 ? 338 PRO A N 1 ATOM 2622 C CA . PRO A 1 342 ? 44.857 7.622 24.431 1.00 28.38 ? 338 PRO A CA 1 ATOM 2623 C C . PRO A 1 342 ? 43.626 7.793 23.494 1.00 29.38 ? 338 PRO A C 1 ATOM 2624 O O . PRO A 1 342 ? 42.567 8.308 23.932 1.00 27.70 ? 338 PRO A O 1 ATOM 2625 C CB . PRO A 1 342 ? 44.746 6.278 25.196 1.00 28.48 ? 338 PRO A CB 1 ATOM 2626 C CG . PRO A 1 342 ? 44.021 6.632 26.450 1.00 28.48 ? 338 PRO A CG 1 ATOM 2627 C CD . PRO A 1 342 ? 44.519 8.035 26.813 1.00 28.48 ? 338 PRO A CD 1 ATOM 2628 N N . MET A 1 343 ? 43.749 7.338 22.249 1.00 28.73 ? 339 MET A N 1 ATOM 2629 C CA . MET A 1 343 ? 42.631 7.376 21.311 1.00 30.91 ? 339 MET A CA 1 ATOM 2630 C C . MET A 1 343 ? 41.425 6.590 21.806 1.00 30.04 ? 339 MET A C 1 ATOM 2631 O O . MET A 1 343 ? 40.282 6.912 21.444 1.00 31.54 ? 339 MET A O 1 ATOM 2632 C CB . MET A 1 343 ? 43.040 6.923 19.888 1.00 31.68 ? 339 MET A CB 1 ATOM 2633 C CG . MET A 1 343 ? 41.964 7.238 18.810 1.00 37.30 ? 339 MET A CG 1 ATOM 2634 S SD . MET A 1 343 ? 41.619 9.032 18.443 1.00 40.24 ? 339 MET A SD 1 ATOM 2635 C CE . MET A 1 343 ? 43.139 9.810 18.725 1.00 38.58 ? 339 MET A CE 1 ATOM 2636 N N . SER A 1 344 ? 41.659 5.533 22.591 1.00 28.95 ? 340 SER A N 1 ATOM 2637 C CA . SER A 1 344 ? 40.572 4.749 23.121 1.00 29.43 ? 340 SER A CA 1 ATOM 2638 C C . SER A 1 344 ? 39.627 5.651 23.971 1.00 28.44 ? 340 SER A C 1 ATOM 2639 O O . SER A 1 344 ? 38.417 5.473 23.948 1.00 29.94 ? 340 SER A O 1 ATOM 2640 C CB . SER A 1 344 ? 41.112 3.602 23.969 1.00 29.52 ? 340 SER A CB 1 ATOM 2641 O OG . SER A 1 344 ? 41.857 4.127 25.039 1.00 30.10 ? 340 SER A OG 1 ATOM 2642 N N . ARG A 1 345 ? 40.187 6.623 24.682 1.00 28.00 ? 341 ARG A N 1 ATOM 2643 C CA . ARG A 1 345 ? 39.409 7.531 25.549 1.00 26.15 ? 341 ARG A CA 1 ATOM 2644 C C . ARG A 1 345 ? 38.563 8.499 24.708 1.00 26.38 ? 341 ARG A C 1 ATOM 2645 O O . ARG A 1 345 ? 37.366 8.689 24.968 1.00 25.40 ? 341 ARG A O 1 ATOM 2646 C CB . ARG A 1 345 ? 40.357 8.326 26.474 1.00 26.84 ? 341 ARG A CB 1 ATOM 2647 C CG . ARG A 1 345 ? 39.696 9.183 27.580 1.00 24.88 ? 341 ARG A CG 1 ATOM 2648 C CD . ARG A 1 345 ? 38.795 8.348 28.643 1.00 26.91 ? 341 ARG A CD 1 ATOM 2649 N NE . ARG A 1 345 ? 37.391 8.168 28.145 1.00 25.00 ? 341 ARG A NE 1 ATOM 2650 C CZ . ARG A 1 345 ? 36.478 9.156 28.114 1.00 26.60 ? 341 ARG A CZ 1 ATOM 2651 N NH1 . ARG A 1 345 ? 36.780 10.399 28.526 1.00 23.48 ? 341 ARG A NH1 1 ATOM 2652 N NH2 . ARG A 1 345 ? 35.263 8.895 27.673 1.00 23.78 ? 341 ARG A NH2 1 ATOM 2653 N N . ILE A 1 346 ? 39.180 9.098 23.689 1.00 25.38 ? 342 ILE A N 1 ATOM 2654 C CA . ILE A 1 346 ? 38.460 9.948 22.734 1.00 25.54 ? 342 ILE A CA 1 ATOM 2655 C C . ILE A 1 346 ? 37.345 9.155 22.059 1.00 25.93 ? 342 ILE A C 1 ATOM 2656 O O . ILE A 1 346 ? 36.202 9.669 21.936 1.00 25.49 ? 342 ILE A O 1 ATOM 2657 C CB . ILE A 1 346 ? 39.427 10.514 21.649 1.00 25.60 ? 342 ILE A CB 1 ATOM 2658 C CG1 . ILE A 1 346 ? 40.594 11.289 22.347 1.00 26.23 ? 342 ILE A CG1 1 ATOM 2659 C CG2 . ILE A 1 346 ? 38.654 11.355 20.606 1.00 26.43 ? 342 ILE A CG2 1 ATOM 2660 C CD1 . ILE A 1 346 ? 40.166 12.567 23.152 1.00 27.53 ? 342 ILE A CD1 1 ATOM 2661 N N . ASP A 1 347 ? 37.652 7.926 21.629 1.00 24.54 ? 343 ASP A N 1 ATOM 2662 C CA . ASP A 1 347 ? 36.679 7.138 20.848 1.00 25.67 ? 343 ASP A CA 1 ATOM 2663 C C . ASP A 1 347 ? 35.464 6.764 21.718 1.00 25.79 ? 343 ASP A C 1 ATOM 2664 O O . ASP A 1 347 ? 34.325 6.679 21.216 1.00 26.00 ? 343 ASP A O 1 ATOM 2665 C CB . ASP A 1 347 ? 37.295 5.875 20.270 1.00 26.27 ? 343 ASP A CB 1 ATOM 2666 C CG . ASP A 1 347 ? 38.171 6.153 19.043 1.00 29.65 ? 343 ASP A CG 1 ATOM 2667 O OD1 . ASP A 1 347 ? 38.180 7.291 18.553 1.00 29.31 ? 343 ASP A OD1 1 ATOM 2668 O OD2 . ASP A 1 347 ? 38.818 5.214 18.547 1.00 27.14 ? 343 ASP A OD2 1 ATOM 2669 N N . ASP A 1 348 ? 35.723 6.521 22.999 1.00 25.38 ? 344 ASP A N 1 ATOM 2670 C CA . ASP A 1 348 ? 34.670 6.185 23.953 1.00 25.29 ? 344 ASP A CA 1 ATOM 2671 C C . ASP A 1 348 ? 33.769 7.425 24.139 1.00 24.91 ? 344 ASP A C 1 ATOM 2672 O O . ASP A 1 348 ? 32.545 7.279 24.129 1.00 24.34 ? 344 ASP A O 1 ATOM 2673 C CB . ASP A 1 348 ? 35.242 5.703 25.301 1.00 25.91 ? 344 ASP A CB 1 ATOM 2674 C CG . ASP A 1 348 ? 34.159 5.518 26.401 1.00 27.39 ? 344 ASP A CG 1 ATOM 2675 O OD1 . ASP A 1 348 ? 33.269 4.666 26.278 1.00 28.02 ? 344 ASP A OD1 1 ATOM 2676 O OD2 . ASP A 1 348 ? 34.192 6.255 27.395 1.00 29.30 ? 344 ASP A OD2 1 ATOM 2677 N N . ALA A 1 349 ? 34.375 8.596 24.341 1.00 23.54 ? 345 ALA A N 1 ATOM 2678 C CA . ALA A 1 349 ? 33.603 9.853 24.562 1.00 24.44 ? 345 ALA A CA 1 ATOM 2679 C C . ALA A 1 349 ? 32.711 10.096 23.349 1.00 25.56 ? 345 ALA A C 1 ATOM 2680 O O . ALA A 1 349 ? 31.500 10.299 23.480 1.00 25.37 ? 345 ALA A O 1 ATOM 2681 C CB . ALA A 1 349 ? 34.552 11.060 24.791 1.00 23.85 ? 345 ALA A CB 1 ATOM 2682 N N . VAL A 1 350 ? 33.293 9.997 22.155 1.00 23.64 ? 346 VAL A N 1 ATOM 2683 C CA . VAL A 1 350 ? 32.525 10.204 20.914 1.00 23.46 ? 346 VAL A CA 1 ATOM 2684 C C . VAL A 1 350 ? 31.490 9.113 20.677 1.00 24.82 ? 346 VAL A C 1 ATOM 2685 O O . VAL A 1 350 ? 30.368 9.408 20.214 1.00 24.52 ? 346 VAL A O 1 ATOM 2686 C CB . VAL A 1 350 ? 33.470 10.359 19.674 1.00 23.56 ? 346 VAL A CB 1 ATOM 2687 C CG1 . VAL A 1 350 ? 32.595 10.532 18.352 1.00 22.06 ? 346 VAL A CG1 1 ATOM 2688 C CG2 . VAL A 1 350 ? 34.418 11.615 19.949 1.00 21.67 ? 346 VAL A CG2 1 ATOM 2689 N N . THR A 1 351 ? 31.821 7.855 20.984 1.00 23.87 ? 347 THR A N 1 ATOM 2690 C CA . THR A 1 351 ? 30.832 6.790 20.847 1.00 24.14 ? 347 THR A CA 1 ATOM 2691 C C . THR A 1 351 ? 29.551 7.194 21.645 1.00 24.12 ? 347 THR A C 1 ATOM 2692 O O . THR A 1 351 ? 28.447 7.081 21.155 1.00 24.83 ? 347 THR A O 1 ATOM 2693 C CB . THR A 1 351 ? 31.439 5.465 21.372 1.00 24.84 ? 347 THR A CB 1 ATOM 2694 O OG1 . THR A 1 351 ? 32.450 5.033 20.434 1.00 25.17 ? 347 THR A OG1 1 ATOM 2695 C CG2 . THR A 1 351 ? 30.401 4.342 21.536 1.00 24.86 ? 347 THR A CG2 1 ATOM 2696 N N . ARG A 1 352 ? 29.734 7.637 22.876 1.00 22.84 ? 348 ARG A N 1 ATOM 2697 C CA . ARG A 1 352 ? 28.603 7.944 23.790 1.00 22.37 ? 348 ARG A CA 1 ATOM 2698 C C . ARG A 1 352 ? 27.831 9.154 23.292 1.00 23.07 ? 348 ARG A C 1 ATOM 2699 O O . ARG A 1 352 ? 26.596 9.137 23.319 1.00 24.71 ? 348 ARG A O 1 ATOM 2700 C CB . ARG A 1 352 ? 29.191 8.201 25.179 1.00 22.71 ? 348 ARG A CB 1 ATOM 2701 C CG . ARG A 1 352 ? 29.671 6.877 25.868 1.00 22.72 ? 348 ARG A CG 1 ATOM 2702 C CD . ARG A 1 352 ? 30.655 7.174 27.006 1.00 24.01 ? 348 ARG A CD 1 ATOM 2703 N NE . ARG A 1 352 ? 30.984 5.892 27.626 1.00 25.02 ? 348 ARG A NE 1 ATOM 2704 C CZ . ARG A 1 352 ? 30.188 5.307 28.532 1.00 26.44 ? 348 ARG A CZ 1 ATOM 2705 N NH1 . ARG A 1 352 ? 29.060 5.892 28.922 1.00 23.87 ? 348 ARG A NH1 1 ATOM 2706 N NH2 . ARG A 1 352 ? 30.514 4.132 29.038 1.00 23.00 ? 348 ARG A NH2 1 ATOM 2707 N N . ILE A 1 353 ? 28.530 10.180 22.788 1.00 22.00 ? 349 ILE A N 1 ATOM 2708 C CA . ILE A 1 353 ? 27.836 11.366 22.289 1.00 21.71 ? 349 ILE A CA 1 ATOM 2709 C C . ILE A 1 353 ? 27.001 11.032 21.057 1.00 22.23 ? 349 ILE A C 1 ATOM 2710 O O . ILE A 1 353 ? 25.813 11.379 20.943 1.00 21.89 ? 349 ILE A O 1 ATOM 2711 C CB . ILE A 1 353 ? 28.886 12.495 21.995 1.00 22.44 ? 349 ILE A CB 1 ATOM 2712 C CG1 . ILE A 1 353 ? 29.523 12.971 23.325 1.00 20.05 ? 349 ILE A CG1 1 ATOM 2713 C CG2 . ILE A 1 353 ? 28.202 13.646 21.221 1.00 20.55 ? 349 ILE A CG2 1 ATOM 2714 C CD1 . ILE A 1 353 ? 30.816 13.851 23.073 1.00 17.53 ? 349 ILE A CD1 1 ATOM 2715 N N . LEU A 1 354 ? 27.613 10.321 20.099 1.00 21.36 ? 350 LEU A N 1 ATOM 2716 C CA . LEU A 1 354 ? 26.884 9.902 18.914 1.00 21.33 ? 350 LEU A CA 1 ATOM 2717 C C . LEU A 1 354 ? 25.769 8.923 19.266 1.00 21.51 ? 350 LEU A C 1 ATOM 2718 O O . LEU A 1 354 ? 24.714 8.962 18.635 1.00 23.82 ? 350 LEU A O 1 ATOM 2719 C CB . LEU A 1 354 ? 27.857 9.203 17.923 1.00 21.95 ? 350 LEU A CB 1 ATOM 2720 C CG . LEU A 1 354 ? 28.951 10.161 17.368 1.00 22.32 ? 350 LEU A CG 1 ATOM 2721 C CD1 . LEU A 1 354 ? 29.798 9.244 16.392 1.00 23.43 ? 350 LEU A CD1 1 ATOM 2722 C CD2 . LEU A 1 354 ? 28.352 11.379 16.638 1.00 20.71 ? 350 LEU A CD2 1 ATOM 2723 N N . ARG A 1 355 ? 26.008 8.001 20.216 1.00 21.16 ? 351 ARG A N 1 ATOM 2724 C CA . ARG A 1 355 ? 24.934 7.082 20.629 1.00 23.18 ? 351 ARG A CA 1 ATOM 2725 C C . ARG A 1 355 ? 23.670 7.883 21.049 1.00 22.36 ? 351 ARG A C 1 ATOM 2726 O O . ARG A 1 355 ? 22.516 7.555 20.666 1.00 21.59 ? 351 ARG A O 1 ATOM 2727 C CB . ARG A 1 355 ? 25.379 6.174 21.799 1.00 23.17 ? 351 ARG A CB 1 ATOM 2728 C CG . ARG A 1 355 ? 24.281 5.109 22.211 1.00 26.05 ? 351 ARG A CG 1 ATOM 2729 C CD . ARG A 1 355 ? 24.752 4.153 23.350 1.00 26.24 ? 351 ARG A CD 1 ATOM 2730 N NE . ARG A 1 355 ? 25.834 3.263 22.858 1.00 23.55 ? 351 ARG A NE 1 ATOM 2731 C CZ . ARG A 1 355 ? 27.085 3.216 23.337 1.00 27.71 ? 351 ARG A CZ 1 ATOM 2732 N NH1 . ARG A 1 355 ? 27.484 3.973 24.373 1.00 24.10 ? 351 ARG A NH1 1 ATOM 2733 N NH2 . ARG A 1 355 ? 27.963 2.371 22.777 1.00 28.13 ? 351 ARG A NH2 1 ATOM 2734 N N . VAL A 1 356 ? 23.879 8.923 21.861 1.00 21.62 ? 352 VAL A N 1 ATOM 2735 C CA . VAL A 1 356 ? 22.701 9.682 22.337 1.00 20.97 ? 352 VAL A CA 1 ATOM 2736 C C . VAL A 1 356 ? 22.018 10.388 21.158 1.00 20.84 ? 352 VAL A C 1 ATOM 2737 O O . VAL A 1 356 ? 20.771 10.350 21.028 1.00 19.80 ? 352 VAL A O 1 ATOM 2738 C CB . VAL A 1 356 ? 23.106 10.657 23.448 1.00 20.39 ? 352 VAL A CB 1 ATOM 2739 C CG1 . VAL A 1 356 ? 21.986 11.664 23.698 1.00 20.68 ? 352 VAL A CG1 1 ATOM 2740 C CG2 . VAL A 1 356 ? 23.501 9.867 24.717 1.00 19.09 ? 352 VAL A CG2 1 ATOM 2741 N N . LYS A 1 357 ? 22.827 11.039 20.289 1.00 19.85 ? 353 LYS A N 1 ATOM 2742 C CA . LYS A 1 357 ? 22.270 11.734 19.090 1.00 20.25 ? 353 LYS A CA 1 ATOM 2743 C C . LYS A 1 357 ? 21.532 10.813 18.116 1.00 21.01 ? 353 LYS A C 1 ATOM 2744 O O . LYS A 1 357 ? 20.429 11.131 17.695 1.00 20.84 ? 353 LYS A O 1 ATOM 2745 C CB . LYS A 1 357 ? 23.378 12.445 18.325 1.00 21.07 ? 353 LYS A CB 1 ATOM 2746 C CG . LYS A 1 357 ? 24.067 13.553 19.173 1.00 19.69 ? 353 LYS A CG 1 ATOM 2747 C CD . LYS A 1 357 ? 25.185 14.246 18.316 1.00 18.59 ? 353 LYS A CD 1 ATOM 2748 C CE . LYS A 1 357 ? 25.562 15.614 19.024 1.00 20.24 ? 353 LYS A CE 1 ATOM 2749 N NZ . LYS A 1 357 ? 26.522 16.405 18.112 1.00 19.77 ? 353 LYS A NZ 1 ATOM 2750 N N . PHE A 1 358 ? 22.121 9.650 17.782 1.00 21.93 ? 354 PHE A N 1 ATOM 2751 C CA . PHE A 1 358 ? 21.397 8.681 16.930 1.00 22.63 ? 354 PHE A CA 1 ATOM 2752 C C . PHE A 1 358 ? 20.121 8.135 17.602 1.00 22.87 ? 354 PHE A C 1 ATOM 2753 O O . PHE A 1 358 ? 19.056 8.044 16.960 1.00 22.71 ? 354 PHE A O 1 ATOM 2754 C CB . PHE A 1 358 ? 22.280 7.489 16.535 1.00 20.78 ? 354 PHE A CB 1 ATOM 2755 C CG . PHE A 1 358 ? 23.258 7.796 15.421 1.00 22.90 ? 354 PHE A CG 1 ATOM 2756 C CD1 . PHE A 1 358 ? 22.785 8.177 14.147 1.00 24.12 ? 354 PHE A CD1 1 ATOM 2757 C CD2 . PHE A 1 358 ? 24.625 7.755 15.669 1.00 21.33 ? 354 PHE A CD2 1 ATOM 2758 C CE1 . PHE A 1 358 ? 23.701 8.488 13.083 1.00 22.28 ? 354 PHE A CE1 1 ATOM 2759 C CE2 . PHE A 1 358 ? 25.543 8.045 14.667 1.00 24.66 ? 354 PHE A CE2 1 ATOM 2760 C CZ . PHE A 1 358 ? 25.087 8.407 13.378 1.00 22.76 ? 354 PHE A CZ 1 ATOM 2761 N N . THR A 1 359 ? 20.245 7.750 18.857 1.00 22.80 ? 355 THR A N 1 ATOM 2762 C CA . THR A 1 359 ? 19.090 7.177 19.597 1.00 23.16 ? 355 THR A CA 1 ATOM 2763 C C . THR A 1 359 ? 17.866 8.112 19.615 1.00 23.81 ? 355 THR A C 1 ATOM 2764 O O . THR A 1 359 ? 16.711 7.681 19.437 1.00 24.34 ? 355 THR A O 1 ATOM 2765 C CB . THR A 1 359 ? 19.522 6.828 21.052 1.00 23.41 ? 355 THR A CB 1 ATOM 2766 O OG1 . THR A 1 359 ? 20.554 5.838 20.992 1.00 24.80 ? 355 THR A OG1 1 ATOM 2767 C CG2 . THR A 1 359 ? 18.342 6.252 21.939 1.00 24.06 ? 355 THR A CG2 1 ATOM 2768 N N . MET A 1 360 ? 18.116 9.400 19.862 1.00 21.99 ? 356 MET A N 1 ATOM 2769 C CA . MET A 1 360 ? 17.032 10.365 20.060 1.00 22.19 ? 356 MET A CA 1 ATOM 2770 C C . MET A 1 360 ? 16.443 10.860 18.745 1.00 22.87 ? 356 MET A C 1 ATOM 2771 O O . MET A 1 360 ? 15.463 11.662 18.729 1.00 24.67 ? 356 MET A O 1 ATOM 2772 C CB . MET A 1 360 ? 17.542 11.577 20.889 1.00 22.45 ? 356 MET A CB 1 ATOM 2773 C CG . MET A 1 360 ? 18.510 12.529 20.049 1.00 21.31 ? 356 MET A CG 1 ATOM 2774 S SD . MET A 1 360 ? 19.296 13.749 21.144 1.00 22.98 ? 356 MET A SD 1 ATOM 2775 C CE . MET A 1 360 ? 17.817 14.695 21.571 1.00 20.13 ? 356 MET A CE 1 ATOM 2776 N N . GLY A 1 361 ? 17.015 10.422 17.629 1.00 22.11 ? 357 GLY A N 1 ATOM 2777 C CA . GLY A 1 361 ? 16.459 10.789 16.347 1.00 21.74 ? 357 GLY A CA 1 ATOM 2778 C C . GLY A 1 361 ? 17.050 12.038 15.752 1.00 21.72 ? 357 GLY A C 1 ATOM 2779 O O . GLY A 1 361 ? 16.519 12.590 14.766 1.00 21.06 ? 357 GLY A O 1 ATOM 2780 N N . LEU A 1 362 ? 18.141 12.528 16.328 1.00 22.20 ? 358 LEU A N 1 ATOM 2781 C CA . LEU A 1 362 ? 18.618 13.866 15.898 1.00 21.43 ? 358 LEU A CA 1 ATOM 2782 C C . LEU A 1 362 ? 19.112 13.926 14.442 1.00 22.88 ? 358 LEU A C 1 ATOM 2783 O O . LEU A 1 362 ? 19.003 14.972 13.789 1.00 22.66 ? 358 LEU A O 1 ATOM 2784 C CB . LEU A 1 362 ? 19.745 14.315 16.858 1.00 22.33 ? 358 LEU A CB 1 ATOM 2785 C CG . LEU A 1 362 ? 20.242 15.747 16.805 1.00 22.19 ? 358 LEU A CG 1 ATOM 2786 C CD1 . LEU A 1 362 ? 19.120 16.758 17.262 1.00 23.02 ? 358 LEU A CD1 1 ATOM 2787 C CD2 . LEU A 1 362 ? 21.499 15.848 17.731 1.00 18.29 ? 358 LEU A CD2 1 ATOM 2788 N N . PHE A 1 363 ? 19.673 12.827 13.916 1.00 21.31 ? 359 PHE A N 1 ATOM 2789 C CA . PHE A 1 363 ? 20.073 12.818 12.520 1.00 22.12 ? 359 PHE A CA 1 ATOM 2790 C C . PHE A 1 363 ? 18.864 12.777 11.585 1.00 23.68 ? 359 PHE A C 1 ATOM 2791 O O . PHE A 1 363 ? 18.993 13.124 10.425 1.00 24.91 ? 359 PHE A O 1 ATOM 2792 C CB . PHE A 1 363 ? 20.959 11.600 12.198 1.00 21.87 ? 359 PHE A CB 1 ATOM 2793 C CG . PHE A 1 363 ? 22.386 11.688 12.707 1.00 21.64 ? 359 PHE A CG 1 ATOM 2794 C CD1 . PHE A 1 363 ? 22.685 11.607 14.065 1.00 20.65 ? 359 PHE A CD1 1 ATOM 2795 C CD2 . PHE A 1 363 ? 23.460 11.835 11.787 1.00 24.20 ? 359 PHE A CD2 1 ATOM 2796 C CE1 . PHE A 1 363 ? 24.015 11.648 14.512 1.00 22.10 ? 359 PHE A CE1 1 ATOM 2797 C CE2 . PHE A 1 363 ? 24.780 11.889 12.227 1.00 22.55 ? 359 PHE A CE2 1 ATOM 2798 C CZ . PHE A 1 363 ? 25.063 11.763 13.592 1.00 22.58 ? 359 PHE A CZ 1 ATOM 2799 N N . GLU A 1 364 ? 17.689 12.322 12.057 1.00 23.43 ? 360 GLU A N 1 ATOM 2800 C CA . GLU A 1 364 ? 16.503 12.286 11.186 1.00 24.13 ? 360 GLU A CA 1 ATOM 2801 C C . GLU A 1 364 ? 15.701 13.569 11.303 1.00 26.01 ? 360 GLU A C 1 ATOM 2802 O O . GLU A 1 364 ? 14.984 13.949 10.360 1.00 26.26 ? 360 GLU A O 1 ATOM 2803 C CB . GLU A 1 364 ? 15.586 11.097 11.586 1.00 24.09 ? 360 GLU A CB 1 ATOM 2804 C CG . GLU A 1 364 ? 16.043 9.762 10.924 1.00 24.34 ? 360 GLU A CG 1 ATOM 2805 C CD . GLU A 1 364 ? 17.474 9.347 11.349 1.00 25.77 ? 360 GLU A CD 1 ATOM 2806 O OE1 . GLU A 1 364 ? 17.681 8.867 12.489 1.00 24.64 ? 360 GLU A OE1 1 ATOM 2807 O OE2 . GLU A 1 364 ? 18.416 9.526 10.555 1.00 27.12 ? 360 GLU A OE2 1 ATOM 2808 N N . ASN A 1 365 ? 15.768 14.217 12.473 1.00 24.31 ? 361 ASN A N 1 ATOM 2809 C CA . ASN A 1 365 ? 15.059 15.505 12.684 1.00 25.01 ? 361 ASN A CA 1 ATOM 2810 C C . ASN A 1 365 ? 16.022 16.534 13.321 1.00 23.90 ? 361 ASN A C 1 ATOM 2811 O O . ASN A 1 365 ? 15.910 16.859 14.522 1.00 23.87 ? 361 ASN A O 1 ATOM 2812 C CB . ASN A 1 365 ? 13.785 15.280 13.549 1.00 23.64 ? 361 ASN A CB 1 ATOM 2813 C CG . ASN A 1 365 ? 12.688 14.563 12.720 1.00 29.62 ? 361 ASN A CG 1 ATOM 2814 O OD1 . ASN A 1 365 ? 11.949 15.191 11.941 1.00 31.65 ? 361 ASN A OD1 1 ATOM 2815 N ND2 . ASN A 1 365 ? 12.657 13.270 12.827 1.00 26.84 ? 361 ASN A ND2 1 ATOM 2816 N N . PRO A 1 366 ? 16.996 17.023 12.522 1.00 24.32 ? 362 PRO A N 1 ATOM 2817 C CA . PRO A 1 366 ? 17.940 17.995 13.101 1.00 24.09 ? 362 PRO A CA 1 ATOM 2818 C C . PRO A 1 366 ? 17.327 19.396 13.294 1.00 23.33 ? 362 PRO A C 1 ATOM 2819 O O . PRO A 1 366 ? 17.893 20.234 14.065 1.00 23.07 ? 362 PRO A O 1 ATOM 2820 C CB . PRO A 1 366 ? 19.118 18.012 12.100 1.00 24.94 ? 362 PRO A CB 1 ATOM 2821 C CG . PRO A 1 366 ? 18.518 17.465 10.737 1.00 25.98 ? 362 PRO A CG 1 ATOM 2822 C CD . PRO A 1 366 ? 17.411 16.513 11.192 1.00 24.37 ? 362 PRO A CD 1 ATOM 2823 N N . TYR A 1 367 ? 16.264 19.687 12.548 1.00 21.80 ? 363 TYR A N 1 ATOM 2824 C CA . TYR A 1 367 ? 15.670 21.050 12.584 1.00 22.99 ? 363 TYR A CA 1 ATOM 2825 C C . TYR A 1 367 ? 14.392 21.140 13.400 1.00 23.73 ? 363 TYR A C 1 ATOM 2826 O O . TYR A 1 367 ? 13.723 20.121 13.639 1.00 25.23 ? 363 TYR A O 1 ATOM 2827 C CB . TYR A 1 367 ? 15.427 21.606 11.148 1.00 22.88 ? 363 TYR A CB 1 ATOM 2828 C CG . TYR A 1 367 ? 16.727 21.684 10.370 1.00 23.91 ? 363 TYR A CG 1 ATOM 2829 C CD1 . TYR A 1 367 ? 17.690 22.650 10.688 1.00 25.82 ? 363 TYR A CD1 1 ATOM 2830 C CD2 . TYR A 1 367 ? 17.014 20.774 9.337 1.00 26.97 ? 363 TYR A CD2 1 ATOM 2831 C CE1 . TYR A 1 367 ? 18.897 22.734 9.974 1.00 25.45 ? 363 TYR A CE1 1 ATOM 2832 C CE2 . TYR A 1 367 ? 18.239 20.854 8.628 1.00 28.21 ? 363 TYR A CE2 1 ATOM 2833 C CZ . TYR A 1 367 ? 19.173 21.835 8.980 1.00 27.89 ? 363 TYR A CZ 1 ATOM 2834 O OH . TYR A 1 367 ? 20.392 21.946 8.316 1.00 27.80 ? 363 TYR A OH 1 ATOM 2835 N N . ALA A 1 368 ? 14.039 22.361 13.805 1.00 22.69 ? 364 ALA A N 1 ATOM 2836 C CA . ALA A 1 368 ? 12.861 22.579 14.653 1.00 23.75 ? 364 ALA A CA 1 ATOM 2837 C C . ALA A 1 368 ? 11.582 22.337 13.859 1.00 23.99 ? 364 ALA A C 1 ATOM 2838 O O . ALA A 1 368 ? 11.561 22.489 12.610 1.00 24.32 ? 364 ALA A O 1 ATOM 2839 C CB . ALA A 1 368 ? 12.881 23.985 15.198 1.00 22.30 ? 364 ALA A CB 1 ATOM 2840 N N . ASP A 1 369 ? 10.499 22.027 14.576 1.00 23.94 ? 365 ASP A N 1 ATOM 2841 C CA . ASP A 1 369 ? 9.175 21.911 13.927 1.00 24.64 ? 365 ASP A CA 1 ATOM 2842 C C . ASP A 1 369 ? 8.339 23.183 14.185 1.00 25.02 ? 365 ASP A C 1 ATOM 2843 O O . ASP A 1 369 ? 7.913 23.438 15.334 1.00 23.98 ? 365 ASP A O 1 ATOM 2844 C CB . ASP A 1 369 ? 8.469 20.653 14.489 1.00 23.54 ? 365 ASP A CB 1 ATOM 2845 C CG . ASP A 1 369 ? 7.077 20.431 13.899 1.00 28.38 ? 365 ASP A CG 1 ATOM 2846 O OD1 . ASP A 1 369 ? 6.565 21.245 13.083 1.00 25.60 ? 365 ASP A OD1 1 ATOM 2847 O OD2 . ASP A 1 369 ? 6.500 19.435 14.353 1.00 27.12 ? 365 ASP A OD2 1 ATOM 2848 N N . PRO A 1 370 ? 8.088 23.988 13.138 1.00 26.10 ? 366 PRO A N 1 ATOM 2849 C CA . PRO A 1 370 ? 7.387 25.220 13.450 1.00 26.30 ? 366 PRO A CA 1 ATOM 2850 C C . PRO A 1 370 ? 5.959 24.976 13.981 1.00 26.96 ? 366 PRO A C 1 ATOM 2851 O O . PRO A 1 370 ? 5.425 25.859 14.649 1.00 27.08 ? 366 PRO A O 1 ATOM 2852 C CB . PRO A 1 370 ? 7.321 25.963 12.094 1.00 28.20 ? 366 PRO A CB 1 ATOM 2853 C CG . PRO A 1 370 ? 7.437 24.918 11.083 1.00 30.04 ? 366 PRO A CG 1 ATOM 2854 C CD . PRO A 1 370 ? 8.289 23.800 11.676 1.00 26.32 ? 366 PRO A CD 1 ATOM 2855 N N . ALA A 1 371 ? 5.363 23.814 13.719 1.00 27.12 ? 367 ALA A N 1 ATOM 2856 C CA . ALA A 1 371 ? 4.024 23.522 14.316 1.00 27.39 ? 367 ALA A CA 1 ATOM 2857 C C . ALA A 1 371 ? 4.109 23.339 15.836 1.00 26.83 ? 367 ALA A C 1 ATOM 2858 O O . ALA A 1 371 ? 3.086 23.368 16.516 1.00 27.39 ? 367 ALA A O 1 ATOM 2859 C CB . ALA A 1 371 ? 3.357 22.296 13.624 1.00 29.20 ? 367 ALA A CB 1 ATOM 2860 N N . MET A 1 372 ? 5.329 23.215 16.393 1.00 24.21 ? 368 MET A N 1 ATOM 2861 C CA . MET A 1 372 ? 5.448 23.025 17.836 1.00 24.02 ? 368 MET A CA 1 ATOM 2862 C C . MET A 1 372 ? 5.484 24.371 18.572 1.00 22.97 ? 368 MET A C 1 ATOM 2863 O O . MET A 1 372 ? 5.347 24.410 19.804 1.00 22.94 ? 368 MET A O 1 ATOM 2864 C CB . MET A 1 372 ? 6.679 22.187 18.218 1.00 22.63 ? 368 MET A CB 1 ATOM 2865 C CG . MET A 1 372 ? 6.586 20.717 17.750 1.00 27.40 ? 368 MET A CG 1 ATOM 2866 S SD . MET A 1 372 ? 5.317 19.835 18.748 1.00 34.44 ? 368 MET A SD 1 ATOM 2867 C CE . MET A 1 372 ? 6.356 19.550 20.190 1.00 31.58 ? 368 MET A CE 1 ATOM 2868 N N . ALA A 1 373 ? 5.631 25.479 17.843 1.00 21.98 ? 369 ALA A N 1 ATOM 2869 C CA . ALA A 1 373 ? 5.845 26.788 18.514 1.00 22.14 ? 369 ALA A CA 1 ATOM 2870 C C . ALA A 1 373 ? 4.715 27.097 19.469 1.00 23.48 ? 369 ALA A C 1 ATOM 2871 O O . ALA A 1 373 ? 4.963 27.622 20.563 1.00 23.06 ? 369 ALA A O 1 ATOM 2872 C CB . ALA A 1 373 ? 5.981 27.933 17.498 1.00 22.83 ? 369 ALA A CB 1 ATOM 2873 N N . GLU A 1 374 ? 3.475 26.745 19.065 1.00 23.92 ? 370 GLU A N 1 ATOM 2874 C CA . GLU A 1 374 ? 2.264 27.053 19.855 1.00 25.95 ? 370 GLU A CA 1 ATOM 2875 C C . GLU A 1 374 ? 2.123 26.238 21.139 1.00 26.09 ? 370 GLU A C 1 ATOM 2876 O O . GLU A 1 374 ? 1.226 26.549 21.950 1.00 26.75 ? 370 GLU A O 1 ATOM 2877 C CB . GLU A 1 374 ? 0.979 26.944 19.012 1.00 27.98 ? 370 GLU A CB 1 ATOM 2878 C CG . GLU A 1 374 ? 0.903 25.569 18.289 1.00 31.51 ? 370 GLU A CG 1 ATOM 2879 C CD . GLU A 1 374 ? -0.100 25.542 17.073 1.00 44.90 ? 370 GLU A CD 1 ATOM 2880 O OE1 . GLU A 1 374 ? -1.307 25.289 17.328 1.00 41.13 ? 370 GLU A OE1 1 ATOM 2881 O OE2 . GLU A 1 374 ? 0.339 25.709 15.870 1.00 48.49 ? 370 GLU A OE2 1 ATOM 2882 N N . GLN A 1 375 ? 3.012 25.260 21.374 1.00 24.43 ? 371 GLN A N 1 ATOM 2883 C CA . GLN A 1 375 ? 3.054 24.572 22.688 1.00 23.94 ? 371 GLN A CA 1 ATOM 2884 C C . GLN A 1 375 ? 3.539 25.446 23.829 1.00 23.83 ? 371 GLN A C 1 ATOM 2885 O O . GLN A 1 375 ? 3.290 25.146 24.988 1.00 23.95 ? 371 GLN A O 1 ATOM 2886 C CB . GLN A 1 375 ? 4.006 23.372 22.666 1.00 23.81 ? 371 GLN A CB 1 ATOM 2887 C CG . GLN A 1 375 ? 3.594 22.247 21.728 1.00 25.80 ? 371 GLN A CG 1 ATOM 2888 C CD . GLN A 1 375 ? 2.379 21.476 22.207 1.00 28.98 ? 371 GLN A CD 1 ATOM 2889 O OE1 . GLN A 1 375 ? 2.084 21.396 23.409 1.00 25.78 ? 371 GLN A OE1 1 ATOM 2890 N NE2 . GLN A 1 375 ? 1.672 20.897 21.271 1.00 33.20 ? 371 GLN A NE2 1 ATOM 2891 N N . LEU A 1 376 ? 4.238 26.537 23.508 1.00 23.44 ? 372 LEU A N 1 ATOM 2892 C CA . LEU A 1 376 ? 4.803 27.429 24.521 1.00 22.82 ? 372 LEU A CA 1 ATOM 2893 C C . LEU A 1 376 ? 3.666 28.077 25.302 1.00 23.25 ? 372 LEU A C 1 ATOM 2894 O O . LEU A 1 376 ? 2.749 28.683 24.708 1.00 22.22 ? 372 LEU A O 1 ATOM 2895 C CB . LEU A 1 376 ? 5.654 28.532 23.856 1.00 22.33 ? 372 LEU A CB 1 ATOM 2896 C CG . LEU A 1 376 ? 6.512 29.319 24.855 1.00 23.39 ? 372 LEU A CG 1 ATOM 2897 C CD1 . LEU A 1 376 ? 7.582 28.484 25.502 1.00 21.14 ? 372 LEU A CD1 1 ATOM 2898 C CD2 . LEU A 1 376 ? 7.119 30.597 24.141 1.00 23.80 ? 372 LEU A CD2 1 ATOM 2899 N N . GLY A 1 377 ? 3.709 27.952 26.630 1.00 22.76 ? 373 GLY A N 1 ATOM 2900 C CA . GLY A 1 377 ? 2.703 28.590 27.487 1.00 21.39 ? 373 GLY A CA 1 ATOM 2901 C C . GLY A 1 377 ? 1.275 28.100 27.273 1.00 24.03 ? 373 GLY A C 1 ATOM 2902 O O . GLY A 1 377 ? 0.331 28.766 27.661 1.00 22.89 ? 373 GLY A O 1 ATOM 2903 N N . LYS A 1 378 ? 1.093 26.916 26.672 1.00 24.19 ? 374 LYS A N 1 ATOM 2904 C CA . LYS A 1 378 ? -0.256 26.387 26.341 1.00 25.02 ? 374 LYS A CA 1 ATOM 2905 C C . LYS A 1 378 ? -1.126 26.274 27.622 1.00 24.56 ? 374 LYS A C 1 ATOM 2906 O O . LYS A 1 378 ? -0.632 25.798 28.654 1.00 22.48 ? 374 LYS A O 1 ATOM 2907 C CB . LYS A 1 378 ? -0.072 25.000 25.590 1.00 24.89 ? 374 LYS A CB 1 ATOM 2908 C CG A LYS A 1 378 ? -1.202 24.247 24.962 0.60 29.11 ? 374 LYS A CG 1 ATOM 2909 C CG B LYS A 1 378 ? -0.833 25.064 24.249 0.40 23.48 ? 374 LYS A CG 1 ATOM 2910 C CD A LYS A 1 378 ? -0.724 22.938 24.151 0.60 26.78 ? 374 LYS A CD 1 ATOM 2911 C CD B LYS A 1 378 ? -0.563 23.855 23.364 0.40 22.57 ? 374 LYS A CD 1 ATOM 2912 C CE A LYS A 1 378 ? -0.461 21.668 25.093 0.60 30.57 ? 374 LYS A CE 1 ATOM 2913 C CE B LYS A 1 378 ? -1.421 23.779 22.110 0.40 24.47 ? 374 LYS A CE 1 ATOM 2914 N NZ A LYS A 1 378 ? 0.066 20.183 24.669 0.60 16.61 ? 374 LYS A NZ 1 ATOM 2915 N NZ B LYS A 1 378 ? -2.350 24.925 21.718 0.40 21.50 ? 374 LYS A NZ 1 ATOM 2916 N N . GLN A 1 379 ? -2.383 26.709 27.567 1.00 23.67 ? 375 GLN A N 1 ATOM 2917 C CA . GLN A 1 379 ? -3.291 26.696 28.749 1.00 24.95 ? 375 GLN A CA 1 ATOM 2918 C C . GLN A 1 379 ? -3.369 25.286 29.402 1.00 25.08 ? 375 GLN A C 1 ATOM 2919 O O . GLN A 1 379 ? -3.453 25.179 30.614 1.00 24.47 ? 375 GLN A O 1 ATOM 2920 C CB . GLN A 1 379 ? -4.723 27.165 28.385 1.00 24.91 ? 375 GLN A CB 1 ATOM 2921 C CG . GLN A 1 379 ? -5.632 27.393 29.643 1.00 25.53 ? 375 GLN A CG 1 ATOM 2922 C CD . GLN A 1 379 ? -5.046 28.444 30.543 1.00 30.60 ? 375 GLN A CD 1 ATOM 2923 O OE1 . GLN A 1 379 ? -4.544 29.454 30.044 1.00 33.37 ? 375 GLN A OE1 1 ATOM 2924 N NE2 . GLN A 1 379 ? -4.936 28.145 31.857 1.00 28.77 ? 375 GLN A NE2 1 ATOM 2925 N N . GLU A 1 380 ? -3.316 24.215 28.611 1.00 23.44 ? 376 GLU A N 1 ATOM 2926 C CA . GLU A 1 380 ? -3.363 22.874 29.230 1.00 23.76 ? 376 GLU A CA 1 ATOM 2927 C C . GLU A 1 380 ? -2.169 22.690 30.172 1.00 23.51 ? 376 GLU A C 1 ATOM 2928 O O . GLU A 1 380 ? -2.277 22.051 31.254 1.00 23.29 ? 376 GLU A O 1 ATOM 2929 C CB . GLU A 1 380 ? -3.392 21.780 28.129 1.00 24.41 ? 376 GLU A CB 1 ATOM 2930 C CG . GLU A 1 380 ? -4.701 21.834 27.270 1.00 27.50 ? 376 GLU A CG 1 ATOM 2931 C CD . GLU A 1 380 ? -4.572 22.701 26.047 1.00 30.46 ? 376 GLU A CD 1 ATOM 2932 O OE1 . GLU A 1 380 ? -3.799 23.696 26.032 1.00 28.78 ? 376 GLU A OE1 1 ATOM 2933 O OE2 . GLU A 1 380 ? -5.233 22.401 25.043 1.00 35.90 ? 376 GLU A OE2 1 ATOM 2934 N N . HIS A 1 381 ? -1.024 23.270 29.795 1.00 20.93 ? 377 HIS A N 1 ATOM 2935 C CA . HIS A 1 381 ? 0.190 23.118 30.666 1.00 20.92 ? 377 HIS A CA 1 ATOM 2936 C C . HIS A 1 381 ? 0.082 24.020 31.874 1.00 19.88 ? 377 HIS A C 1 ATOM 2937 O O . HIS A 1 381 ? 0.522 23.654 32.972 1.00 21.46 ? 377 HIS A O 1 ATOM 2938 C CB . HIS A 1 381 ? 1.504 23.500 29.901 1.00 19.46 ? 377 HIS A CB 1 ATOM 2939 C CG . HIS A 1 381 ? 1.688 22.776 28.587 1.00 22.25 ? 377 HIS A CG 1 ATOM 2940 N ND1 . HIS A 1 381 ? 1.059 21.581 28.282 1.00 27.19 ? 377 HIS A ND1 1 ATOM 2941 C CD2 . HIS A 1 381 ? 2.477 23.063 27.533 1.00 19.39 ? 377 HIS A CD2 1 ATOM 2942 C CE1 . HIS A 1 381 ? 1.430 21.184 27.072 1.00 23.11 ? 377 HIS A CE1 1 ATOM 2943 N NE2 . HIS A 1 381 ? 2.277 22.079 26.588 1.00 29.39 ? 377 HIS A NE2 1 ATOM 2944 N N . ARG A 1 382 ? -0.440 25.234 31.693 1.00 20.15 ? 378 ARG A N 1 ATOM 2945 C CA . ARG A 1 382 ? -0.708 26.100 32.841 1.00 19.71 ? 378 ARG A CA 1 ATOM 2946 C C . ARG A 1 382 ? -1.714 25.424 33.820 1.00 20.01 ? 378 ARG A C 1 ATOM 2947 O O . ARG A 1 382 ? -1.545 25.545 35.039 1.00 19.17 ? 378 ARG A O 1 ATOM 2948 C CB . ARG A 1 382 ? -1.294 27.471 32.398 1.00 21.00 ? 378 ARG A CB 1 ATOM 2949 C CG . ARG A 1 382 ? -0.250 28.297 31.546 1.00 20.65 ? 378 ARG A CG 1 ATOM 2950 C CD . ARG A 1 382 ? -0.786 29.726 31.112 1.00 19.88 ? 378 ARG A CD 1 ATOM 2951 N NE . ARG A 1 382 ? 0.210 30.342 30.169 1.00 21.33 ? 378 ARG A NE 1 ATOM 2952 C CZ . ARG A 1 382 ? 1.338 30.932 30.569 1.00 23.90 ? 378 ARG A CZ 1 ATOM 2953 N NH1 . ARG A 1 382 ? 1.691 30.962 31.864 1.00 22.20 ? 378 ARG A NH1 1 ATOM 2954 N NH2 . ARG A 1 382 ? 2.148 31.474 29.686 1.00 23.42 ? 378 ARG A NH2 1 ATOM 2955 N N . ASP A 1 383 ? -2.768 24.782 33.303 1.00 19.59 ? 379 ASP A N 1 ATOM 2956 C CA . ASP A 1 383 ? -3.685 24.046 34.178 1.00 20.96 ? 379 ASP A CA 1 ATOM 2957 C C . ASP A 1 383 ? -2.940 22.982 35.016 1.00 20.62 ? 379 ASP A C 1 ATOM 2958 O O . ASP A 1 383 ? -3.227 22.794 36.205 1.00 20.41 ? 379 ASP A O 1 ATOM 2959 C CB . ASP A 1 383 ? -4.810 23.363 33.392 1.00 21.65 ? 379 ASP A CB 1 ATOM 2960 C CG . ASP A 1 383 ? -5.764 24.395 32.730 1.00 25.93 ? 379 ASP A CG 1 ATOM 2961 O OD1 . ASP A 1 383 ? -5.717 25.573 33.091 1.00 24.56 ? 379 ASP A OD1 1 ATOM 2962 O OD2 . ASP A 1 383 ? -6.499 24.000 31.811 1.00 29.02 ? 379 ASP A OD2 1 ATOM 2963 N N . LEU A 1 384 ? -1.965 22.316 34.394 1.00 20.46 ? 380 LEU A N 1 ATOM 2964 C CA . LEU A 1 384 ? -1.146 21.299 35.095 1.00 20.26 ? 380 LEU A CA 1 ATOM 2965 C C . LEU A 1 384 ? -0.269 21.993 36.123 1.00 20.20 ? 380 LEU A C 1 ATOM 2966 O O . LEU A 1 384 ? -0.209 21.555 37.260 1.00 20.76 ? 380 LEU A O 1 ATOM 2967 C CB . LEU A 1 384 ? -0.259 20.528 34.089 1.00 19.46 ? 380 LEU A CB 1 ATOM 2968 C CG . LEU A 1 384 ? 0.797 19.540 34.670 1.00 21.58 ? 380 LEU A CG 1 ATOM 2969 C CD1 . LEU A 1 384 ? 0.106 18.359 35.376 1.00 22.76 ? 380 LEU A CD1 1 ATOM 2970 C CD2 . LEU A 1 384 ? 1.653 18.986 33.504 1.00 21.36 ? 380 LEU A CD2 1 ATOM 2971 N N . ALA A 1 385 ? 0.368 23.113 35.767 1.00 20.21 ? 381 ALA A N 1 ATOM 2972 C CA . ALA A 1 385 ? 1.228 23.837 36.730 1.00 19.74 ? 381 ALA A CA 1 ATOM 2973 C C . ALA A 1 385 ? 0.381 24.271 37.920 1.00 20.48 ? 381 ALA A C 1 ATOM 2974 O O . ALA A 1 385 ? 0.837 24.326 39.069 1.00 20.74 ? 381 ALA A O 1 ATOM 2975 C CB . ALA A 1 385 ? 1.803 25.119 36.068 1.00 20.76 ? 381 ALA A CB 1 ATOM 2976 N N . ARG A 1 386 ? -0.832 24.693 37.612 1.00 20.01 ? 382 ARG A N 1 ATOM 2977 C CA . ARG A 1 386 ? -1.757 25.183 38.671 1.00 20.87 ? 382 ARG A CA 1 ATOM 2978 C C . ARG A 1 386 ? -2.150 24.062 39.669 1.00 21.39 ? 382 ARG A C 1 ATOM 2979 O O . ARG A 1 386 ? -2.198 24.278 40.874 1.00 21.23 ? 382 ARG A O 1 ATOM 2980 C CB . ARG A 1 386 ? -2.987 25.791 37.969 1.00 20.98 ? 382 ARG A CB 1 ATOM 2981 C CG . ARG A 1 386 ? -4.174 26.163 38.921 1.00 21.99 ? 382 ARG A CG 1 ATOM 2982 C CD . ARG A 1 386 ? -5.333 26.810 38.115 1.00 26.19 ? 382 ARG A CD 1 ATOM 2983 N NE . ARG A 1 386 ? -6.522 27.157 38.964 1.00 22.14 ? 382 ARG A NE 1 ATOM 2984 C CZ . ARG A 1 386 ? -7.577 27.828 38.518 1.00 26.49 ? 382 ARG A CZ 1 ATOM 2985 N NH1 . ARG A 1 386 ? -7.576 28.237 37.234 1.00 24.27 ? 382 ARG A NH1 1 ATOM 2986 N NH2 . ARG A 1 386 ? -8.637 28.067 39.344 1.00 24.71 ? 382 ARG A NH2 1 ATOM 2987 N N . GLU A 1 387 ? -2.453 22.884 39.145 1.00 22.69 ? 383 GLU A N 1 ATOM 2988 C CA . GLU A 1 387 ? -2.667 21.656 39.945 1.00 22.15 ? 383 GLU A CA 1 ATOM 2989 C C . GLU A 1 387 ? -1.423 21.399 40.789 1.00 21.78 ? 383 GLU A C 1 ATOM 2990 O O . GLU A 1 387 ? -1.539 21.162 41.991 1.00 23.13 ? 383 GLU A O 1 ATOM 2991 C CB . GLU A 1 387 ? -2.872 20.440 39.003 1.00 22.81 ? 383 GLU A CB 1 ATOM 2992 C CG . GLU A 1 387 ? -2.923 19.059 39.765 1.00 24.34 ? 383 GLU A CG 1 ATOM 2993 C CD . GLU A 1 387 ? -3.018 17.836 38.806 1.00 27.63 ? 383 GLU A CD 1 ATOM 2994 O OE1 . GLU A 1 387 ? -3.190 17.997 37.581 1.00 29.69 ? 383 GLU A OE1 1 ATOM 2995 O OE2 . GLU A 1 387 ? -2.866 16.701 39.283 1.00 26.95 ? 383 GLU A OE2 1 ATOM 2996 N N . ALA A 1 388 ? -0.230 21.446 40.188 1.00 19.66 ? 384 ALA A N 1 ATOM 2997 C CA . ALA A 1 388 ? 1.030 21.124 40.935 1.00 18.93 ? 384 ALA A CA 1 ATOM 2998 C C . ALA A 1 388 ? 1.269 22.177 42.030 1.00 19.88 ? 384 ALA A C 1 ATOM 2999 O O . ALA A 1 388 ? 1.692 21.857 43.130 1.00 19.45 ? 384 ALA A O 1 ATOM 3000 C CB . ALA A 1 388 ? 2.260 21.126 39.952 1.00 18.30 ? 384 ALA A CB 1 ATOM 3001 N N . ALA A 1 389 ? 1.012 23.453 41.715 1.00 19.13 ? 385 ALA A N 1 ATOM 3002 C CA . ALA A 1 389 ? 1.221 24.494 42.727 1.00 18.60 ? 385 ALA A CA 1 ATOM 3003 C C . ALA A 1 389 ? 0.305 24.230 43.931 1.00 20.13 ? 385 ALA A C 1 ATOM 3004 O O . ALA A 1 389 ? 0.743 24.287 45.084 1.00 19.55 ? 385 ALA A O 1 ATOM 3005 C CB . ALA A 1 389 ? 0.947 25.922 42.113 1.00 16.98 ? 385 ALA A CB 1 ATOM 3006 N N . ARG A 1 390 ? -0.975 24.008 43.662 1.00 19.76 ? 386 ARG A N 1 ATOM 3007 C CA . ARG A 1 390 ? -1.926 23.713 44.759 1.00 20.63 ? 386 ARG A CA 1 ATOM 3008 C C . ARG A 1 390 ? -1.498 22.455 45.597 1.00 20.98 ? 386 ARG A C 1 ATOM 3009 O O . ARG A 1 390 ? -1.553 22.454 46.842 1.00 20.93 ? 386 ARG A O 1 ATOM 3010 C CB . ARG A 1 390 ? -3.308 23.504 44.138 1.00 20.95 ? 386 ARG A CB 1 ATOM 3011 C CG . ARG A 1 390 ? -4.427 23.043 45.176 1.00 23.70 ? 386 ARG A CG 1 ATOM 3012 C CD . ARG A 1 390 ? -4.820 21.530 45.000 1.00 26.40 ? 386 ARG A CD 1 ATOM 3013 N NE . ARG A 1 390 ? -5.307 21.291 43.647 1.00 31.55 ? 386 ARG A NE 1 ATOM 3014 C CZ . ARG A 1 390 ? -5.648 20.085 43.201 1.00 34.26 ? 386 ARG A CZ 1 ATOM 3015 N NH1 . ARG A 1 390 ? -5.618 19.039 44.027 1.00 34.93 ? 386 ARG A NH1 1 ATOM 3016 N NH2 . ARG A 1 390 ? -6.033 19.946 41.956 1.00 34.39 ? 386 ARG A NH2 1 ATOM 3017 N N . LYS A 1 391 ? -1.082 21.394 44.925 1.00 21.14 ? 387 LYS A N 1 ATOM 3018 C CA . LYS A 1 391 ? -0.654 20.165 45.649 1.00 21.67 ? 387 LYS A CA 1 ATOM 3019 C C . LYS A 1 391 ? 0.612 20.341 46.455 1.00 21.67 ? 387 LYS A C 1 ATOM 3020 O O . LYS A 1 391 ? 0.824 19.601 47.423 1.00 21.60 ? 387 LYS A O 1 ATOM 3021 C CB . LYS A 1 391 ? -0.490 18.993 44.651 1.00 22.37 ? 387 LYS A CB 1 ATOM 3022 C CG . LYS A 1 391 ? -1.876 18.484 44.098 1.00 22.04 ? 387 LYS A CG 1 ATOM 3023 C CD . LYS A 1 391 ? -1.663 17.356 42.999 1.00 24.97 ? 387 LYS A CD 1 ATOM 3024 C CE . LYS A 1 391 ? -2.991 16.558 42.757 1.00 28.69 ? 387 LYS A CE 1 ATOM 3025 N NZ . LYS A 1 391 ? -2.743 15.467 41.745 1.00 27.63 ? 387 LYS A NZ 1 ATOM 3026 N N . SER A 1 392 ? 1.457 21.311 46.061 1.00 21.81 ? 388 SER A N 1 ATOM 3027 C CA . SER A 1 392 ? 2.778 21.535 46.698 1.00 21.52 ? 388 SER A CA 1 ATOM 3028 C C . SER A 1 392 ? 2.610 22.297 48.015 1.00 21.39 ? 388 SER A C 1 ATOM 3029 O O . SER A 1 392 ? 3.512 22.291 48.871 1.00 22.44 ? 388 SER A O 1 ATOM 3030 C CB . SER A 1 392 ? 3.710 22.387 45.795 1.00 21.39 ? 388 SER A CB 1 ATOM 3031 O OG . SER A 1 392 ? 3.335 23.786 45.810 1.00 23.25 ? 388 SER A OG 1 ATOM 3032 N N . LEU A 1 393 ? 1.496 22.988 48.184 1.00 20.74 ? 389 LEU A N 1 ATOM 3033 C CA . LEU A 1 393 ? 1.315 23.870 49.396 1.00 20.37 ? 389 LEU A CA 1 ATOM 3034 C C . LEU A 1 393 ? 1.231 23.044 50.694 1.00 21.41 ? 389 LEU A C 1 ATOM 3035 O O . LEU A 1 393 ? 0.488 22.049 50.748 1.00 21.58 ? 389 LEU A O 1 ATOM 3036 C CB . LEU A 1 393 ? 0.024 24.689 49.290 1.00 20.68 ? 389 LEU A CB 1 ATOM 3037 C CG . LEU A 1 393 ? -0.188 25.364 47.919 1.00 20.45 ? 389 LEU A CG 1 ATOM 3038 C CD1 . LEU A 1 393 ? -1.606 25.960 47.977 1.00 20.38 ? 389 LEU A CD1 1 ATOM 3039 C CD2 . LEU A 1 393 ? 0.849 26.509 47.734 1.00 19.96 ? 389 LEU A CD2 1 ATOM 3040 N N . VAL A 1 394 ? 1.979 23.440 51.718 1.00 20.71 ? 390 VAL A N 1 ATOM 3041 C CA . VAL A 1 394 ? 1.885 22.708 53.028 1.00 21.97 ? 390 VAL A CA 1 ATOM 3042 C C . VAL A 1 394 ? 1.282 23.636 54.062 1.00 22.38 ? 390 VAL A C 1 ATOM 3043 O O . VAL A 1 394 ? 1.821 24.694 54.319 1.00 23.06 ? 390 VAL A O 1 ATOM 3044 C CB . VAL A 1 394 ? 3.263 22.204 53.517 1.00 21.67 ? 390 VAL A CB 1 ATOM 3045 C CG1 . VAL A 1 394 ? 3.128 21.443 54.944 1.00 20.54 ? 390 VAL A CG1 1 ATOM 3046 C CG2 . VAL A 1 394 ? 3.835 21.272 52.454 1.00 21.10 ? 390 VAL A CG2 1 ATOM 3047 N N . LEU A 1 395 ? 0.133 23.248 54.620 1.00 22.27 ? 391 LEU A N 1 ATOM 3048 C CA . LEU A 1 395 ? -0.546 24.092 55.600 1.00 22.41 ? 391 LEU A CA 1 ATOM 3049 C C . LEU A 1 395 ? 0.126 23.796 56.925 1.00 23.63 ? 391 LEU A C 1 ATOM 3050 O O . LEU A 1 395 ? 0.102 22.641 57.371 1.00 23.92 ? 391 LEU A O 1 ATOM 3051 C CB . LEU A 1 395 ? -2.033 23.693 55.647 1.00 21.84 ? 391 LEU A CB 1 ATOM 3052 C CG . LEU A 1 395 ? -2.967 24.413 56.629 1.00 21.15 ? 391 LEU A CG 1 ATOM 3053 C CD1 . LEU A 1 395 ? -2.983 25.911 56.307 1.00 20.76 ? 391 LEU A CD1 1 ATOM 3054 C CD2 . LEU A 1 395 ? -4.360 23.805 56.451 1.00 21.13 ? 391 LEU A CD2 1 ATOM 3055 N N . LEU A 1 396 ? 0.730 24.823 57.548 1.00 22.57 ? 392 LEU A N 1 ATOM 3056 C CA . LEU A 1 396 ? 1.463 24.619 58.801 1.00 24.30 ? 392 LEU A CA 1 ATOM 3057 C C . LEU A 1 396 ? 0.623 24.973 60.005 1.00 25.50 ? 392 LEU A C 1 ATOM 3058 O O . LEU A 1 396 ? 0.898 24.485 61.093 1.00 25.76 ? 392 LEU A O 1 ATOM 3059 C CB . LEU A 1 396 ? 2.740 25.480 58.838 1.00 23.05 ? 392 LEU A CB 1 ATOM 3060 C CG . LEU A 1 396 ? 3.758 25.035 57.745 1.00 26.13 ? 392 LEU A CG 1 ATOM 3061 C CD1 . LEU A 1 396 ? 5.028 25.899 57.734 1.00 28.55 ? 392 LEU A CD1 1 ATOM 3062 C CD2 . LEU A 1 396 ? 4.138 23.514 57.925 1.00 23.30 ? 392 LEU A CD2 1 ATOM 3063 N N . LYS A 1 397 ? -0.347 25.865 59.832 1.00 24.51 ? 393 LYS A N 1 ATOM 3064 C CA . LYS A 1 397 ? -1.184 26.276 60.995 1.00 26.27 ? 393 LYS A CA 1 ATOM 3065 C C . LYS A 1 397 ? -2.521 26.734 60.430 1.00 25.59 ? 393 LYS A C 1 ATOM 3066 O O . LYS A 1 397 ? -2.540 27.381 59.363 1.00 23.50 ? 393 LYS A O 1 ATOM 3067 C CB . LYS A 1 397 ? -0.480 27.445 61.704 1.00 25.98 ? 393 LYS A CB 1 ATOM 3068 C CG . LYS A 1 397 ? -1.215 28.089 62.872 1.00 26.92 ? 393 LYS A CG 1 ATOM 3069 C CD . LYS A 1 397 ? -0.454 29.268 63.453 1.00 25.82 ? 393 LYS A CD 1 ATOM 3070 C CE . LYS A 1 397 ? -1.203 29.841 64.708 1.00 26.61 ? 393 LYS A CE 1 ATOM 3071 N NZ . LYS A 1 397 ? -0.374 30.919 65.387 1.00 26.05 ? 393 LYS A NZ 1 ATOM 3072 N N . ASN A 1 398 ? -3.626 26.442 61.099 1.00 25.53 ? 394 ASN A N 1 ATOM 3073 C CA . ASN A 1 398 ? -4.940 26.899 60.622 1.00 26.30 ? 394 ASN A CA 1 ATOM 3074 C C . ASN A 1 398 ? -5.775 27.215 61.868 1.00 29.58 ? 394 ASN A C 1 ATOM 3075 O O . ASN A 1 398 ? -6.675 26.434 62.183 1.00 30.19 ? 394 ASN A O 1 ATOM 3076 C CB . ASN A 1 398 ? -5.614 25.780 59.784 1.00 26.18 ? 394 ASN A CB 1 ATOM 3077 C CG . ASN A 1 398 ? -6.863 26.255 59.003 1.00 25.27 ? 394 ASN A CG 1 ATOM 3078 O OD1 . ASN A 1 398 ? -7.674 25.426 58.478 1.00 26.46 ? 394 ASN A OD1 1 ATOM 3079 N ND2 . ASN A 1 398 ? -7.034 27.564 58.911 1.00 21.16 ? 394 ASN A ND2 1 ATOM 3080 N N . GLY A 1 399 ? -5.391 28.256 62.625 1.00 29.86 ? 395 GLY A N 1 ATOM 3081 C CA . GLY A 1 399 ? -6.009 28.608 63.905 1.00 29.50 ? 395 GLY A CA 1 ATOM 3082 C C . GLY A 1 399 ? -4.990 28.786 65.013 1.00 30.32 ? 395 GLY A C 1 ATOM 3083 O O . GLY A 1 399 ? -4.149 27.910 65.231 1.00 31.20 ? 395 GLY A O 1 ATOM 3084 N N . LYS A 1 400 ? -5.072 29.906 65.757 1.00 32.10 ? 396 LYS A N 1 ATOM 3085 C CA . LYS A 1 400 ? -4.125 30.165 66.870 1.00 31.75 ? 396 LYS A CA 1 ATOM 3086 C C . LYS A 1 400 ? -4.341 29.269 68.082 1.00 33.38 ? 396 LYS A C 1 ATOM 3087 O O . LYS A 1 400 ? -3.415 29.044 68.910 1.00 33.20 ? 396 LYS A O 1 ATOM 3088 C CB . LYS A 1 400 ? -4.225 31.632 67.351 1.00 32.52 ? 396 LYS A CB 1 ATOM 3089 C CG . LYS A 1 400 ? -4.096 32.678 66.277 1.00 33.70 ? 396 LYS A CG 1 ATOM 3090 C CD . LYS A 1 400 ? -3.718 34.050 66.863 1.00 35.32 ? 396 LYS A CD 1 ATOM 3091 C CE . LYS A 1 400 ? -3.290 35.007 65.753 1.00 36.35 ? 396 LYS A CE 1 ATOM 3092 N NZ . LYS A 1 400 ? -3.437 36.460 66.149 1.00 35.91 ? 396 LYS A NZ 1 ATOM 3093 N N . THR A 1 401 ? -5.563 28.796 68.264 1.00 31.56 ? 397 THR A N 1 ATOM 3094 C CA . THR A 1 401 ? -5.792 27.900 69.361 1.00 33.17 ? 397 THR A CA 1 ATOM 3095 C C . THR A 1 401 ? -6.605 26.756 68.803 1.00 34.21 ? 397 THR A C 1 ATOM 3096 O O . THR A 1 401 ? -7.259 26.885 67.747 1.00 33.83 ? 397 THR A O 1 ATOM 3097 C CB . THR A 1 401 ? -6.554 28.605 70.529 1.00 33.76 ? 397 THR A CB 1 ATOM 3098 O OG1 . THR A 1 401 ? -7.932 28.706 70.195 1.00 33.94 ? 397 THR A OG1 1 ATOM 3099 C CG2 . THR A 1 401 ? -6.076 30.041 70.748 1.00 34.66 ? 397 THR A CG2 1 ATOM 3100 N N . SER A 1 402 ? -6.620 25.668 69.544 1.00 34.62 ? 398 SER A N 1 ATOM 3101 C CA . SER A 1 402 ? -7.303 24.493 69.146 1.00 37.37 ? 398 SER A CA 1 ATOM 3102 C C . SER A 1 402 ? -8.818 24.722 69.125 1.00 36.91 ? 398 SER A C 1 ATOM 3103 O O . SER A 1 402 ? -9.571 23.916 68.590 1.00 39.18 ? 398 SER A O 1 ATOM 3104 C CB . SER A 1 402 ? -6.957 23.381 70.150 1.00 37.96 ? 398 SER A CB 1 ATOM 3105 O OG . SER A 1 402 ? -7.611 23.645 71.394 1.00 41.71 ? 398 SER A OG 1 ATOM 3106 N N . THR A 1 403 ? -9.243 25.854 69.662 1.00 35.21 ? 399 THR A N 1 ATOM 3107 C CA . THR A 1 403 ? -10.642 26.133 69.898 1.00 34.09 ? 399 THR A CA 1 ATOM 3108 C C . THR A 1 403 ? -11.207 27.259 68.920 1.00 30.58 ? 399 THR A C 1 ATOM 3109 O O . THR A 1 403 ? -12.439 27.470 68.760 1.00 29.05 ? 399 THR A O 1 ATOM 3110 C CB . THR A 1 403 ? -10.662 26.405 71.397 1.00 35.60 ? 399 THR A CB 1 ATOM 3111 O OG1 . THR A 1 403 ? -11.439 25.412 72.113 1.00 45.31 ? 399 THR A OG1 1 ATOM 3112 C CG2 . THR A 1 403 ? -10.850 27.732 71.759 1.00 33.04 ? 399 THR A CG2 1 ATOM 3113 N N . ASP A 1 404 ? -10.297 27.915 68.217 1.00 27.15 ? 400 ASP A N 1 ATOM 3114 C CA . ASP A 1 404 ? -10.667 28.930 67.207 1.00 25.61 ? 400 ASP A CA 1 ATOM 3115 C C . ASP A 1 404 ? -11.387 28.254 66.011 1.00 25.38 ? 400 ASP A C 1 ATOM 3116 O O . ASP A 1 404 ? -11.149 27.083 65.680 1.00 23.23 ? 400 ASP A O 1 ATOM 3117 C CB . ASP A 1 404 ? -9.437 29.688 66.700 1.00 24.58 ? 400 ASP A CB 1 ATOM 3118 C CG . ASP A 1 404 ? -8.906 30.727 67.700 1.00 26.39 ? 400 ASP A CG 1 ATOM 3119 O OD1 . ASP A 1 404 ? -9.289 30.736 68.889 1.00 26.59 ? 400 ASP A OD1 1 ATOM 3120 O OD2 . ASP A 1 404 ? -8.105 31.574 67.266 1.00 26.49 ? 400 ASP A OD2 1 ATOM 3121 N N . ALA A 1 405 ? -12.268 29.006 65.366 1.00 23.49 ? 401 ALA A N 1 ATOM 3122 C CA . ALA A 1 405 ? -12.787 28.618 64.071 1.00 23.57 ? 401 ALA A CA 1 ATOM 3123 C C . ALA A 1 405 ? -11.569 28.485 63.109 1.00 25.48 ? 401 ALA A C 1 ATOM 3124 O O . ALA A 1 405 ? -10.702 29.318 63.092 1.00 24.43 ? 401 ALA A O 1 ATOM 3125 C CB . ALA A 1 405 ? -13.775 29.713 63.544 1.00 22.95 ? 401 ALA A CB 1 ATOM 3126 N N . PRO A 1 406 ? -11.519 27.418 62.323 1.00 25.20 ? 402 PRO A N 1 ATOM 3127 C CA . PRO A 1 406 ? -10.436 27.379 61.336 1.00 26.46 ? 402 PRO A CA 1 ATOM 3128 C C . PRO A 1 406 ? -10.562 28.511 60.309 1.00 25.46 ? 402 PRO A C 1 ATOM 3129 O O . PRO A 1 406 ? -11.637 28.768 59.804 1.00 24.52 ? 402 PRO A O 1 ATOM 3130 C CB . PRO A 1 406 ? -10.578 26.021 60.646 1.00 26.82 ? 402 PRO A CB 1 ATOM 3131 C CG . PRO A 1 406 ? -11.980 25.441 61.068 1.00 30.51 ? 402 PRO A CG 1 ATOM 3132 C CD . PRO A 1 406 ? -12.511 26.323 62.228 1.00 27.69 ? 402 PRO A CD 1 ATOM 3133 N N . LEU A 1 407 ? -9.491 29.263 60.088 1.00 23.63 ? 403 LEU A N 1 ATOM 3134 C CA . LEU A 1 407 ? -9.550 30.361 59.101 1.00 23.56 ? 403 LEU A CA 1 ATOM 3135 C C . LEU A 1 407 ? -9.767 29.855 57.647 1.00 23.85 ? 403 LEU A C 1 ATOM 3136 O O . LEU A 1 407 ? -10.567 30.422 56.853 1.00 22.45 ? 403 LEU A O 1 ATOM 3137 C CB . LEU A 1 407 ? -8.261 31.196 59.180 1.00 25.76 ? 403 LEU A CB 1 ATOM 3138 C CG . LEU A 1 407 ? -8.329 32.383 58.216 1.00 30.36 ? 403 LEU A CG 1 ATOM 3139 C CD1 . LEU A 1 407 ? -9.550 33.392 58.583 1.00 26.67 ? 403 LEU A CD1 1 ATOM 3140 C CD2 . LEU A 1 407 ? -7.062 33.120 58.242 1.00 33.84 ? 403 LEU A CD2 1 ATOM 3141 N N . LEU A 1 408 ? -9.065 28.782 57.277 1.00 22.83 ? 404 LEU A N 1 ATOM 3142 C CA . LEU A 1 408 ? -9.153 28.261 55.917 1.00 24.06 ? 404 LEU A CA 1 ATOM 3143 C C . LEU A 1 408 ? -10.027 27.023 55.903 1.00 25.19 ? 404 LEU A C 1 ATOM 3144 O O . LEU A 1 408 ? -9.932 26.192 56.810 1.00 25.77 ? 404 LEU A O 1 ATOM 3145 C CB . LEU A 1 408 ? -7.753 27.845 55.373 1.00 22.80 ? 404 LEU A CB 1 ATOM 3146 C CG . LEU A 1 408 ? -6.688 28.947 55.406 1.00 23.25 ? 404 LEU A CG 1 ATOM 3147 C CD1 . LEU A 1 408 ? -5.254 28.454 54.868 1.00 21.36 ? 404 LEU A CD1 1 ATOM 3148 C CD2 . LEU A 1 408 ? -7.158 30.253 54.625 1.00 20.25 ? 404 LEU A CD2 1 ATOM 3149 N N . PRO A 1 409 ? -10.836 26.875 54.853 1.00 26.06 ? 405 PRO A N 1 ATOM 3150 C CA . PRO A 1 409 ? -10.880 27.805 53.700 1.00 25.68 ? 405 PRO A CA 1 ATOM 3151 C C . PRO A 1 409 ? -11.633 29.090 53.945 1.00 25.82 ? 405 PRO A C 1 ATOM 3152 O O . PRO A 1 409 ? -12.613 29.139 54.740 1.00 23.24 ? 405 PRO A O 1 ATOM 3153 C CB . PRO A 1 409 ? -11.590 26.982 52.600 1.00 25.64 ? 405 PRO A CB 1 ATOM 3154 C CG . PRO A 1 409 ? -12.486 25.963 53.429 1.00 30.69 ? 405 PRO A CG 1 ATOM 3155 C CD . PRO A 1 409 ? -11.634 25.647 54.644 1.00 27.35 ? 405 PRO A CD 1 ATOM 3156 N N . LEU A 1 410 ? -11.191 30.135 53.236 1.00 23.54 ? 406 LEU A N 1 ATOM 3157 C CA . LEU A 1 410 ? -11.814 31.466 53.333 1.00 25.38 ? 406 LEU A CA 1 ATOM 3158 C C . LEU A 1 410 ? -13.065 31.510 52.434 1.00 25.68 ? 406 LEU A C 1 ATOM 3159 O O . LEU A 1 410 ? -13.090 30.838 51.398 1.00 24.58 ? 406 LEU A O 1 ATOM 3160 C CB . LEU A 1 410 ? -10.818 32.507 52.807 1.00 24.79 ? 406 LEU A CB 1 ATOM 3161 C CG . LEU A 1 410 ? -9.498 32.695 53.597 1.00 27.17 ? 406 LEU A CG 1 ATOM 3162 C CD1 . LEU A 1 410 ? -8.411 33.444 52.721 1.00 27.73 ? 406 LEU A CD1 1 ATOM 3163 C CD2 . LEU A 1 410 ? -9.751 33.431 54.868 1.00 30.44 ? 406 LEU A CD2 1 ATOM 3164 N N . PRO A 1 411 ? -14.081 32.345 52.803 1.00 25.54 ? 407 PRO A N 1 ATOM 3165 C CA . PRO A 1 411 ? -15.248 32.529 51.933 1.00 25.15 ? 407 PRO A CA 1 ATOM 3166 C C . PRO A 1 411 ? -14.898 33.412 50.736 1.00 24.81 ? 407 PRO A C 1 ATOM 3167 O O . PRO A 1 411 ? -14.205 34.437 50.882 1.00 23.08 ? 407 PRO A O 1 ATOM 3168 C CB . PRO A 1 411 ? -16.269 33.239 52.847 1.00 24.00 ? 407 PRO A CB 1 ATOM 3169 C CG . PRO A 1 411 ? -15.406 34.070 53.842 1.00 26.68 ? 407 PRO A CG 1 ATOM 3170 C CD . PRO A 1 411 ? -14.125 33.178 54.041 1.00 26.23 ? 407 PRO A CD 1 ATOM 3171 N N . LYS A 1 412 ? -15.400 33.052 49.554 1.00 24.38 ? 408 LYS A N 1 ATOM 3172 C CA . LYS A 1 412 ? -15.193 33.910 48.333 1.00 24.61 ? 408 LYS A CA 1 ATOM 3173 C C . LYS A 1 412 ? -16.065 35.177 48.330 1.00 24.35 ? 408 LYS A C 1 ATOM 3174 O O . LYS A 1 412 ? -15.831 36.161 47.590 1.00 24.79 ? 408 LYS A O 1 ATOM 3175 C CB . LYS A 1 412 ? -15.505 33.090 47.076 1.00 24.75 ? 408 LYS A CB 1 ATOM 3176 C CG . LYS A 1 412 ? -14.540 31.875 46.868 1.00 24.52 ? 408 LYS A CG 1 ATOM 3177 C CD . LYS A 1 412 ? -15.011 31.088 45.584 1.00 26.81 ? 408 LYS A CD 1 ATOM 3178 C CE . LYS A 1 412 ? -14.132 29.832 45.375 1.00 30.96 ? 408 LYS A CE 1 ATOM 3179 N NZ . LYS A 1 412 ? -14.511 29.226 44.051 1.00 27.03 ? 408 LYS A NZ 1 ATOM 3180 N N . LYS A 1 413 ? -17.107 35.152 49.139 1.00 24.95 ? 409 LYS A N 1 ATOM 3181 C CA . LYS A 1 413 ? -17.966 36.320 49.276 1.00 26.11 ? 409 LYS A CA 1 ATOM 3182 C C . LYS A 1 413 ? -17.786 36.982 50.648 1.00 27.75 ? 409 LYS A C 1 ATOM 3183 O O . LYS A 1 413 ? -18.072 36.364 51.704 1.00 28.67 ? 409 LYS A O 1 ATOM 3184 C CB . LYS A 1 413 ? -19.450 35.931 49.056 1.00 27.73 ? 409 LYS A CB 1 ATOM 3185 C CG . LYS A 1 413 ? -20.354 37.188 49.024 1.00 30.51 ? 409 LYS A CG 1 ATOM 3186 C CD . LYS A 1 413 ? -21.781 36.862 48.619 1.00 35.25 ? 409 LYS A CD 1 ATOM 3187 C CE . LYS A 1 413 ? -22.661 38.108 48.861 1.00 40.28 ? 409 LYS A CE 1 ATOM 3188 N NZ . LYS A 1 413 ? -24.058 37.845 48.302 1.00 45.94 ? 409 LYS A NZ 1 ATOM 3189 N N . ALA A 1 414 ? -17.349 38.240 50.625 1.00 27.29 ? 410 ALA A N 1 ATOM 3190 C CA . ALA A 1 414 ? -17.153 39.076 51.824 1.00 27.05 ? 410 ALA A CA 1 ATOM 3191 C C . ALA A 1 414 ? -17.218 40.538 51.371 1.00 26.66 ? 410 ALA A C 1 ATOM 3192 O O . ALA A 1 414 ? -16.926 40.815 50.200 1.00 27.09 ? 410 ALA A O 1 ATOM 3193 C CB . ALA A 1 414 ? -15.756 38.787 52.489 1.00 25.98 ? 410 ALA A CB 1 ATOM 3194 N N . PRO A 1 415 ? -17.607 41.484 52.266 1.00 25.89 ? 411 PRO A N 1 ATOM 3195 C CA . PRO A 1 415 ? -17.743 42.848 51.707 1.00 25.95 ? 411 PRO A CA 1 ATOM 3196 C C . PRO A 1 415 ? -16.444 43.434 51.194 1.00 25.43 ? 411 PRO A C 1 ATOM 3197 O O . PRO A 1 415 ? -16.428 44.017 50.129 1.00 25.24 ? 411 PRO A O 1 ATOM 3198 C CB . PRO A 1 415 ? -18.277 43.668 52.902 1.00 26.59 ? 411 PRO A CB 1 ATOM 3199 C CG . PRO A 1 415 ? -19.179 42.648 53.624 1.00 27.57 ? 411 PRO A CG 1 ATOM 3200 C CD . PRO A 1 415 ? -18.281 41.352 53.581 1.00 25.47 ? 411 PRO A CD 1 ATOM 3201 N N . LYS A 1 416 ? -15.345 43.196 51.907 1.00 25.83 ? 412 LYS A N 1 ATOM 3202 C CA . LYS A 1 416 ? -14.092 43.840 51.575 1.00 25.56 ? 412 LYS A CA 1 ATOM 3203 C C . LYS A 1 416 ? -12.977 43.001 52.189 1.00 24.26 ? 412 LYS A C 1 ATOM 3204 O O . LYS A 1 416 ? -13.064 42.563 53.367 1.00 23.33 ? 412 LYS A O 1 ATOM 3205 C CB . LYS A 1 416 ? -14.154 45.273 52.166 1.00 26.94 ? 412 LYS A CB 1 ATOM 3206 C CG . LYS A 1 416 ? -13.002 46.166 51.858 1.00 31.40 ? 412 LYS A CG 1 ATOM 3207 C CD . LYS A 1 416 ? -13.401 47.602 52.423 1.00 30.65 ? 412 LYS A CD 1 ATOM 3208 C CE . LYS A 1 416 ? -12.274 48.492 52.149 1.00 36.02 ? 412 LYS A CE 1 ATOM 3209 N NZ . LYS A 1 416 ? -12.459 49.774 52.913 1.00 34.65 ? 412 LYS A NZ 1 ATOM 3210 N N . ILE A 1 417 ? -11.949 42.706 51.388 1.00 23.24 ? 413 ILE A N 1 ATOM 3211 C CA . ILE A 1 417 ? -10.801 41.914 51.879 1.00 22.26 ? 413 ILE A CA 1 ATOM 3212 C C . ILE A 1 417 ? -9.490 42.618 51.544 1.00 23.29 ? 413 ILE A C 1 ATOM 3213 O O . ILE A 1 417 ? -9.455 43.473 50.641 1.00 21.71 ? 413 ILE A O 1 ATOM 3214 C CB . ILE A 1 417 ? -10.790 40.449 51.327 1.00 23.75 ? 413 ILE A CB 1 ATOM 3215 C CG1 . ILE A 1 417 ? -10.572 40.427 49.795 1.00 23.89 ? 413 ILE A CG1 1 ATOM 3216 C CG2 . ILE A 1 417 ? -12.156 39.710 51.649 1.00 20.93 ? 413 ILE A CG2 1 ATOM 3217 C CD1 . ILE A 1 417 ? -10.417 38.977 49.259 1.00 22.76 ? 413 ILE A CD1 1 ATOM 3218 N N . LEU A 1 418 ? -8.440 42.277 52.296 1.00 22.61 ? 414 LEU A N 1 ATOM 3219 C CA . LEU A 1 418 ? -7.135 42.856 52.071 1.00 22.23 ? 414 LEU A CA 1 ATOM 3220 C C . LEU A 1 418 ? -6.152 41.798 51.514 1.00 22.31 ? 414 LEU A C 1 ATOM 3221 O O . LEU A 1 418 ? -6.028 40.719 52.056 1.00 22.68 ? 414 LEU A O 1 ATOM 3222 C CB . LEU A 1 418 ? -6.564 43.374 53.416 1.00 22.21 ? 414 LEU A CB 1 ATOM 3223 C CG . LEU A 1 418 ? -5.153 43.977 53.393 1.00 23.75 ? 414 LEU A CG 1 ATOM 3224 C CD1 . LEU A 1 418 ? -5.054 45.218 52.420 1.00 21.80 ? 414 LEU A CD1 1 ATOM 3225 C CD2 . LEU A 1 418 ? -4.741 44.390 54.858 1.00 21.72 ? 414 LEU A CD2 1 ATOM 3226 N N . VAL A 1 419 ? -5.447 42.143 50.448 1.00 21.02 ? 415 VAL A N 1 ATOM 3227 C CA . VAL A 1 419 ? -4.303 41.347 49.987 1.00 21.48 ? 415 VAL A CA 1 ATOM 3228 C C . VAL A 1 419 ? -3.060 42.222 50.221 1.00 22.38 ? 415 VAL A C 1 ATOM 3229 O O . VAL A 1 419 ? -3.021 43.377 49.757 1.00 22.97 ? 415 VAL A O 1 ATOM 3230 C CB . VAL A 1 419 ? -4.476 41.010 48.462 1.00 21.46 ? 415 VAL A CB 1 ATOM 3231 C CG1 . VAL A 1 419 ? -3.236 40.256 47.907 1.00 19.83 ? 415 VAL A CG1 1 ATOM 3232 C CG2 . VAL A 1 419 ? -5.692 40.060 48.302 1.00 19.02 ? 415 VAL A CG2 1 ATOM 3233 N N . ALA A 1 420 ? -2.063 41.692 50.919 1.00 21.55 ? 416 ALA A N 1 ATOM 3234 C CA . ALA A 1 420 ? -0.899 42.514 51.274 1.00 22.47 ? 416 ALA A CA 1 ATOM 3235 C C . ALA A 1 420 ? 0.387 41.734 51.164 1.00 21.59 ? 416 ALA A C 1 ATOM 3236 O O . ALA A 1 420 ? 0.368 40.522 51.051 1.00 22.41 ? 416 ALA A O 1 ATOM 3237 C CB . ALA A 1 420 ? -1.007 43.045 52.742 1.00 21.47 ? 416 ALA A CB 1 ATOM 3238 N N . GLY A 1 421 ? 1.497 42.459 51.240 1.00 21.12 ? 417 GLY A N 1 ATOM 3239 C CA . GLY A 1 421 ? 2.821 41.868 51.311 1.00 21.55 ? 417 GLY A CA 1 ATOM 3240 C C . GLY A 1 421 ? 3.640 42.057 50.035 1.00 21.42 ? 417 GLY A C 1 ATOM 3241 O O . GLY A 1 421 ? 3.071 42.159 48.942 1.00 22.16 ? 417 GLY A O 1 ATOM 3242 N N . SER A 1 422 ? 4.974 42.112 50.178 1.00 20.39 ? 418 SER A N 1 ATOM 3243 C CA . SER A 1 422 ? 5.925 42.146 49.077 1.00 21.34 ? 418 SER A CA 1 ATOM 3244 C C . SER A 1 422 ? 5.792 40.988 48.040 1.00 21.83 ? 418 SER A C 1 ATOM 3245 O O . SER A 1 422 ? 6.247 41.131 46.890 1.00 22.52 ? 418 SER A O 1 ATOM 3246 C CB . SER A 1 422 ? 7.402 42.083 49.650 1.00 21.88 ? 418 SER A CB 1 ATOM 3247 O OG . SER A 1 422 ? 7.492 40.838 50.382 1.00 24.66 ? 418 SER A OG 1 ATOM 3248 N N . HIS A 1 423 ? 5.165 39.866 48.408 1.00 21.25 ? 419 HIS A N 1 ATOM 3249 C CA . HIS A 1 423 ? 5.070 38.730 47.479 1.00 20.32 ? 419 HIS A CA 1 ATOM 3250 C C . HIS A 1 423 ? 3.633 38.497 46.984 1.00 21.00 ? 419 HIS A C 1 ATOM 3251 O O . HIS A 1 423 ? 3.370 37.535 46.264 1.00 20.30 ? 419 HIS A O 1 ATOM 3252 C CB . HIS A 1 423 ? 5.574 37.467 48.187 1.00 20.81 ? 419 HIS A CB 1 ATOM 3253 C CG . HIS A 1 423 ? 7.071 37.450 48.403 1.00 21.52 ? 419 HIS A CG 1 ATOM 3254 N ND1 . HIS A 1 423 ? 7.739 38.435 49.110 1.00 19.94 ? 419 HIS A ND1 1 ATOM 3255 C CD2 . HIS A 1 423 ? 8.016 36.562 48.016 1.00 20.89 ? 419 HIS A CD2 1 ATOM 3256 C CE1 . HIS A 1 423 ? 9.044 38.170 49.131 1.00 21.65 ? 419 HIS A CE1 1 ATOM 3257 N NE2 . HIS A 1 423 ? 9.244 37.022 48.501 1.00 21.61 ? 419 HIS A NE2 1 ATOM 3258 N N . ALA A 1 424 ? 2.698 39.373 47.350 1.00 21.11 ? 420 ALA A N 1 ATOM 3259 C CA . ALA A 1 424 ? 1.310 39.200 46.907 1.00 22.41 ? 420 ALA A CA 1 ATOM 3260 C C . ALA A 1 424 ? 1.083 39.517 45.427 1.00 22.09 ? 420 ALA A C 1 ATOM 3261 O O . ALA A 1 424 ? 0.186 38.973 44.791 1.00 21.51 ? 420 ALA A O 1 ATOM 3262 C CB . ALA A 1 424 ? 0.420 40.054 47.767 1.00 22.71 ? 420 ALA A CB 1 ATOM 3263 N N . ASP A 1 425 ? 1.884 40.414 44.859 1.00 21.74 ? 421 ASP A N 1 ATOM 3264 C CA . ASP A 1 425 ? 1.695 40.826 43.471 1.00 22.49 ? 421 ASP A CA 1 ATOM 3265 C C . ASP A 1 425 ? 3.057 40.958 42.823 1.00 22.56 ? 421 ASP A C 1 ATOM 3266 O O . ASP A 1 425 ? 3.438 42.037 42.395 1.00 23.59 ? 421 ASP A O 1 ATOM 3267 C CB . ASP A 1 425 ? 0.953 42.193 43.395 1.00 21.77 ? 421 ASP A CB 1 ATOM 3268 C CG . ASP A 1 425 ? 0.504 42.556 41.982 1.00 24.60 ? 421 ASP A CG 1 ATOM 3269 O OD1 . ASP A 1 425 ? 0.080 41.675 41.202 1.00 21.90 ? 421 ASP A OD1 1 ATOM 3270 O OD2 . ASP A 1 425 ? 0.525 43.771 41.646 1.00 24.34 ? 421 ASP A OD2 1 ATOM 3271 N N . ASN A 1 426 ? 3.824 39.875 42.803 1.00 22.46 ? 422 ASN A N 1 ATOM 3272 C CA . ASN A 1 426 ? 5.172 39.947 42.226 1.00 21.92 ? 422 ASN A CA 1 ATOM 3273 C C . ASN A 1 426 ? 5.457 38.588 41.599 1.00 21.74 ? 422 ASN A C 1 ATOM 3274 O O . ASN A 1 426 ? 5.801 37.620 42.272 1.00 19.84 ? 422 ASN A O 1 ATOM 3275 C CB . ASN A 1 426 ? 6.205 40.334 43.305 1.00 23.06 ? 422 ASN A CB 1 ATOM 3276 C CG . ASN A 1 426 ? 7.591 40.533 42.746 1.00 24.06 ? 422 ASN A CG 1 ATOM 3277 O OD1 . ASN A 1 426 ? 7.992 39.854 41.808 1.00 22.47 ? 422 ASN A OD1 1 ATOM 3278 N ND2 . ASN A 1 426 ? 8.325 41.517 43.297 1.00 24.36 ? 422 ASN A ND2 1 ATOM 3279 N N . LEU A 1 427 ? 5.272 38.527 40.298 1.00 20.00 ? 423 LEU A N 1 ATOM 3280 C CA . LEU A 1 427 ? 5.411 37.247 39.581 1.00 21.66 ? 423 LEU A CA 1 ATOM 3281 C C . LEU A 1 427 ? 6.830 36.701 39.670 1.00 21.50 ? 423 LEU A C 1 ATOM 3282 O O . LEU A 1 427 ? 7.038 35.495 39.864 1.00 20.72 ? 423 LEU A O 1 ATOM 3283 C CB . LEU A 1 427 ? 5.029 37.438 38.110 1.00 20.69 ? 423 LEU A CB 1 ATOM 3284 C CG . LEU A 1 427 ? 4.880 36.132 37.291 1.00 25.13 ? 423 LEU A CG 1 ATOM 3285 C CD1 . LEU A 1 427 ? 3.822 35.189 37.907 1.00 24.94 ? 423 LEU A CD1 1 ATOM 3286 C CD2 . LEU A 1 427 ? 4.507 36.466 35.823 1.00 24.14 ? 423 LEU A CD2 1 ATOM 3287 N N . GLY A 1 428 ? 7.824 37.563 39.475 1.00 21.83 ? 424 GLY A N 1 ATOM 3288 C CA . GLY A 1 428 ? 9.238 37.047 39.583 1.00 20.08 ? 424 GLY A CA 1 ATOM 3289 C C . GLY A 1 428 ? 9.516 36.429 40.960 1.00 20.61 ? 424 GLY A C 1 ATOM 3290 O O . GLY A 1 428 ? 10.235 35.424 41.061 1.00 20.11 ? 424 GLY A O 1 ATOM 3291 N N . TYR A 1 429 ? 9.032 37.050 42.039 1.00 20.68 ? 425 TYR A N 1 ATOM 3292 C CA . TYR A 1 429 ? 9.254 36.483 43.390 1.00 20.51 ? 425 TYR A CA 1 ATOM 3293 C C . TYR A 1 429 ? 8.560 35.142 43.565 1.00 20.03 ? 425 TYR A C 1 ATOM 3294 O O . TYR A 1 429 ? 9.120 34.227 44.231 1.00 20.21 ? 425 TYR A O 1 ATOM 3295 C CB . TYR A 1 429 ? 8.700 37.408 44.502 1.00 19.60 ? 425 TYR A CB 1 ATOM 3296 C CG . TYR A 1 429 ? 9.590 38.615 44.802 1.00 20.90 ? 425 TYR A CG 1 ATOM 3297 C CD1 . TYR A 1 429 ? 10.699 38.940 43.988 1.00 20.73 ? 425 TYR A CD1 1 ATOM 3298 C CD2 . TYR A 1 429 ? 9.311 39.418 45.922 1.00 24.46 ? 425 TYR A CD2 1 ATOM 3299 C CE1 . TYR A 1 429 ? 11.559 40.061 44.347 1.00 23.21 ? 425 TYR A CE1 1 ATOM 3300 C CE2 . TYR A 1 429 ? 10.121 40.508 46.283 1.00 25.92 ? 425 TYR A CE2 1 ATOM 3301 C CZ . TYR A 1 429 ? 11.220 40.826 45.478 1.00 26.99 ? 425 TYR A CZ 1 ATOM 3302 O OH . TYR A 1 429 ? 11.983 41.905 45.861 1.00 27.67 ? 425 TYR A OH 1 ATOM 3303 N N . GLN A 1 430 ? 7.356 34.991 43.002 1.00 19.41 ? 426 GLN A N 1 ATOM 3304 C CA . GLN A 1 430 ? 6.686 33.687 43.198 1.00 21.57 ? 426 GLN A CA 1 ATOM 3305 C C . GLN A 1 430 ? 7.286 32.565 42.309 1.00 20.29 ? 426 GLN A C 1 ATOM 3306 O O . GLN A 1 430 ? 7.110 31.372 42.597 1.00 19.60 ? 426 GLN A O 1 ATOM 3307 C CB . GLN A 1 430 ? 5.129 33.773 43.051 1.00 22.61 ? 426 GLN A CB 1 ATOM 3308 C CG . GLN A 1 430 ? 4.649 33.928 41.693 1.00 25.08 ? 426 GLN A CG 1 ATOM 3309 C CD . GLN A 1 430 ? 3.080 34.049 41.622 1.00 26.29 ? 426 GLN A CD 1 ATOM 3310 O OE1 . GLN A 1 430 ? 2.497 34.880 42.304 1.00 24.79 ? 426 GLN A OE1 1 ATOM 3311 N NE2 . GLN A 1 430 ? 2.446 33.273 40.747 1.00 18.77 ? 426 GLN A NE2 1 ATOM 3312 N N . CYS A 1 431 ? 8.012 32.936 41.266 1.00 19.26 ? 427 CYS A N 1 ATOM 3313 C CA . CYS A 1 431 ? 8.753 31.938 40.463 1.00 19.54 ? 427 CYS A CA 1 ATOM 3314 C C . CYS A 1 431 ? 10.148 31.599 41.042 1.00 19.88 ? 427 CYS A C 1 ATOM 3315 O O . CYS A 1 431 ? 10.643 30.464 40.847 1.00 20.70 ? 427 CYS A O 1 ATOM 3316 C CB . CYS A 1 431 ? 8.935 32.455 39.007 1.00 19.72 ? 427 CYS A CB 1 ATOM 3317 S SG . CYS A 1 431 ? 7.365 32.548 38.094 1.00 20.54 ? 427 CYS A SG 1 ATOM 3318 N N . GLY A 1 432 ? 10.811 32.578 41.700 1.00 20.41 ? 428 GLY A N 1 ATOM 3319 C CA . GLY A 1 432 ? 12.173 32.348 42.303 1.00 18.75 ? 428 GLY A CA 1 ATOM 3320 C C . GLY A 1 432 ? 13.216 32.199 41.210 1.00 20.37 ? 428 GLY A C 1 ATOM 3321 O O . GLY A 1 432 ? 12.978 32.641 40.065 1.00 20.72 ? 428 GLY A O 1 ATOM 3322 N N . GLY A 1 433 ? 14.348 31.548 41.527 1.00 20.10 ? 429 GLY A N 1 ATOM 3323 C CA . GLY A 1 433 ? 15.518 31.533 40.626 1.00 19.43 ? 429 GLY A CA 1 ATOM 3324 C C . GLY A 1 433 ? 15.233 30.707 39.366 1.00 20.21 ? 429 GLY A C 1 ATOM 3325 O O . GLY A 1 433 ? 14.154 30.049 39.261 1.00 19.83 ? 429 GLY A O 1 ATOM 3326 N N . TRP A 1 434 ? 16.164 30.750 38.406 1.00 19.66 ? 430 TRP A N 1 ATOM 3327 C CA . TRP A 1 434 ? 16.006 30.048 37.117 1.00 20.22 ? 430 TRP A CA 1 ATOM 3328 C C . TRP A 1 434 ? 14.637 30.406 36.490 1.00 21.26 ? 430 TRP A C 1 ATOM 3329 O O . TRP A 1 434 ? 13.868 29.538 36.066 1.00 20.39 ? 430 TRP A O 1 ATOM 3330 C CB . TRP A 1 434 ? 16.118 28.516 37.305 1.00 20.02 ? 430 TRP A CB 1 ATOM 3331 C CG . TRP A 1 434 ? 17.521 28.061 37.660 1.00 21.72 ? 430 TRP A CG 1 ATOM 3332 C CD1 . TRP A 1 434 ? 17.962 27.581 38.879 1.00 26.25 ? 430 TRP A CD1 1 ATOM 3333 C CD2 . TRP A 1 434 ? 18.647 28.008 36.778 1.00 23.15 ? 430 TRP A CD2 1 ATOM 3334 N NE1 . TRP A 1 434 ? 19.312 27.255 38.808 1.00 23.64 ? 430 TRP A NE1 1 ATOM 3335 C CE2 . TRP A 1 434 ? 19.752 27.525 37.531 1.00 25.13 ? 430 TRP A CE2 1 ATOM 3336 C CE3 . TRP A 1 434 ? 18.848 28.371 35.419 1.00 22.23 ? 430 TRP A CE3 1 ATOM 3337 C CZ2 . TRP A 1 434 ? 21.032 27.347 36.962 1.00 27.22 ? 430 TRP A CZ2 1 ATOM 3338 C CZ3 . TRP A 1 434 ? 20.143 28.169 34.860 1.00 21.71 ? 430 TRP A CZ3 1 ATOM 3339 C CH2 . TRP A 1 434 ? 21.194 27.692 35.627 1.00 23.11 ? 430 TRP A CH2 1 ATOM 3340 N N . THR A 1 435 ? 14.353 31.701 36.418 1.00 20.47 ? 431 THR A N 1 ATOM 3341 C CA . THR A 1 435 ? 13.158 32.122 35.722 1.00 20.52 ? 431 THR A CA 1 ATOM 3342 C C . THR A 1 435 ? 13.601 33.418 34.995 1.00 22.06 ? 431 THR A C 1 ATOM 3343 O O . THR A 1 435 ? 13.891 34.419 35.669 1.00 22.06 ? 431 THR A O 1 ATOM 3344 C CB . THR A 1 435 ? 12.001 32.419 36.700 1.00 22.61 ? 431 THR A CB 1 ATOM 3345 O OG1 . THR A 1 435 ? 11.842 31.303 37.590 1.00 21.81 ? 431 THR A OG1 1 ATOM 3346 C CG2 . THR A 1 435 ? 10.703 32.678 35.890 1.00 20.44 ? 431 THR A CG2 1 ATOM 3347 N N . ILE A 1 436 ? 13.704 33.334 33.669 1.00 21.11 ? 432 ILE A N 1 ATOM 3348 C CA . ILE A 1 436 ? 14.141 34.429 32.777 1.00 21.32 ? 432 ILE A CA 1 ATOM 3349 C C . ILE A 1 436 ? 15.656 34.713 32.918 1.00 22.92 ? 432 ILE A C 1 ATOM 3350 O O . ILE A 1 436 ? 16.359 34.669 31.908 1.00 23.69 ? 432 ILE A O 1 ATOM 3351 C CB . ILE A 1 436 ? 13.285 35.720 32.860 1.00 22.20 ? 432 ILE A CB 1 ATOM 3352 C CG1 . ILE A 1 436 ? 11.781 35.409 32.689 1.00 21.95 ? 432 ILE A CG1 1 ATOM 3353 C CG2 . ILE A 1 436 ? 13.779 36.812 31.777 1.00 20.84 ? 432 ILE A CG2 1 ATOM 3354 C CD1 . ILE A 1 436 ? 11.378 34.675 31.318 1.00 23.49 ? 432 ILE A CD1 1 ATOM 3355 N N . GLU A 1 437 ? 16.163 34.886 34.156 1.00 22.96 ? 433 GLU A N 1 ATOM 3356 C CA . GLU A 1 437 ? 17.619 34.883 34.458 1.00 24.89 ? 433 GLU A CA 1 ATOM 3357 C C . GLU A 1 437 ? 17.959 33.760 35.356 1.00 24.31 ? 433 GLU A C 1 ATOM 3358 O O . GLU A 1 437 ? 17.059 33.250 36.017 1.00 24.25 ? 433 GLU A O 1 ATOM 3359 C CB . GLU A 1 437 ? 17.979 36.191 35.178 1.00 25.57 ? 433 GLU A CB 1 ATOM 3360 C CG . GLU A 1 437 ? 17.717 37.379 34.313 1.00 29.26 ? 433 GLU A CG 1 ATOM 3361 C CD . GLU A 1 437 ? 18.734 37.492 33.152 1.00 28.70 ? 433 GLU A CD 1 ATOM 3362 O OE1 . GLU A 1 437 ? 19.794 36.771 33.111 1.00 30.01 ? 433 GLU A OE1 1 ATOM 3363 O OE2 . GLU A 1 437 ? 18.421 38.302 32.277 1.00 29.03 ? 433 GLU A OE2 1 ATOM 3364 N N . ALA A 1 438 ? 19.257 33.405 35.525 1.00 25.35 ? 434 ALA A N 1 ATOM 3365 C CA . ALA A 1 438 ? 19.580 32.369 36.497 1.00 24.95 ? 434 ALA A CA 1 ATOM 3366 C C . ALA A 1 438 ? 19.187 32.678 37.902 1.00 24.71 ? 434 ALA A C 1 ATOM 3367 O O . ALA A 1 438 ? 18.762 31.795 38.676 1.00 25.22 ? 434 ALA A O 1 ATOM 3368 C CB . ALA A 1 438 ? 21.199 31.976 36.479 1.00 27.09 ? 434 ALA A CB 1 ATOM 3369 N N . GLN A 1 439 ? 19.441 33.939 38.293 1.00 24.06 ? 435 GLN A N 1 ATOM 3370 C CA . GLN A 1 439 ? 19.114 34.421 39.626 1.00 24.21 ? 435 GLN A CA 1 ATOM 3371 C C . GLN A 1 439 ? 17.624 34.768 39.783 1.00 24.90 ? 435 GLN A C 1 ATOM 3372 O O . GLN A 1 439 ? 17.210 35.162 40.874 1.00 24.09 ? 435 GLN A O 1 ATOM 3373 C CB . GLN A 1 439 ? 19.969 35.673 39.993 1.00 25.62 ? 435 GLN A CB 1 ATOM 3374 C CG . GLN A 1 439 ? 21.511 35.313 40.134 1.00 25.53 ? 435 GLN A CG 1 ATOM 3375 C CD . GLN A 1 439 ? 21.777 34.377 41.308 1.00 28.66 ? 435 GLN A CD 1 ATOM 3376 O OE1 . GLN A 1 439 ? 21.104 34.441 42.380 1.00 25.93 ? 435 GLN A OE1 1 ATOM 3377 N NE2 . GLN A 1 439 ? 22.801 33.531 41.147 1.00 26.98 ? 435 GLN A NE2 1 ATOM 3378 N N . GLY A 1 440 ? 16.823 34.533 38.738 1.00 23.89 ? 436 GLY A N 1 ATOM 3379 C CA . GLY A 1 440 ? 15.437 35.081 38.694 1.00 22.63 ? 436 GLY A CA 1 ATOM 3380 C C . GLY A 1 440 ? 15.479 36.604 38.735 1.00 23.61 ? 436 GLY A C 1 ATOM 3381 O O . GLY A 1 440 ? 16.571 37.205 38.507 1.00 22.02 ? 436 GLY A O 1 ATOM 3382 N N . ASP A 1 441 ? 14.334 37.233 39.094 1.00 22.32 ? 437 ASP A N 1 ATOM 3383 C CA . ASP A 1 441 ? 14.177 38.680 38.953 1.00 23.48 ? 437 ASP A CA 1 ATOM 3384 C C . ASP A 1 441 ? 12.881 39.074 39.646 1.00 24.25 ? 437 ASP A C 1 ATOM 3385 O O . ASP A 1 441 ? 12.113 38.212 40.132 1.00 24.31 ? 437 ASP A O 1 ATOM 3386 C CB . ASP A 1 441 ? 14.128 39.071 37.430 1.00 22.83 ? 437 ASP A CB 1 ATOM 3387 C CG . ASP A 1 441 ? 14.468 40.566 37.157 1.00 27.84 ? 437 ASP A CG 1 ATOM 3388 O OD1 . ASP A 1 441 ? 14.759 41.370 38.074 1.00 27.75 ? 437 ASP A OD1 1 ATOM 3389 O OD2 . ASP A 1 441 ? 14.462 40.893 35.973 1.00 29.39 ? 437 ASP A OD2 1 ATOM 3390 N N . THR A 1 442 ? 12.628 40.387 39.709 1.00 25.87 ? 438 THR A N 1 ATOM 3391 C CA . THR A 1 442 ? 11.471 40.938 40.417 1.00 23.56 ? 438 THR A CA 1 ATOM 3392 C C . THR A 1 442 ? 10.443 41.472 39.425 1.00 24.43 ? 438 THR A C 1 ATOM 3393 O O . THR A 1 442 ? 10.805 42.006 38.364 1.00 24.18 ? 438 THR A O 1 ATOM 3394 C CB . THR A 1 442 ? 11.914 42.089 41.358 1.00 24.87 ? 438 THR A CB 1 ATOM 3395 O OG1 . THR A 1 442 ? 10.781 42.607 42.052 1.00 23.07 ? 438 THR A OG1 1 ATOM 3396 C CG2 . THR A 1 442 ? 12.677 43.287 40.575 1.00 26.21 ? 438 THR A CG2 1 ATOM 3397 N N . GLY A 1 443 ? 9.153 41.304 39.727 1.00 23.09 ? 439 GLY A N 1 ATOM 3398 C CA . GLY A 1 443 ? 8.096 42.022 38.999 1.00 22.61 ? 439 GLY A CA 1 ATOM 3399 C C . GLY A 1 443 ? 7.545 41.143 37.877 1.00 23.65 ? 439 GLY A C 1 ATOM 3400 O O . GLY A 1 443 ? 7.611 39.882 37.943 1.00 22.08 ? 439 GLY A O 1 ATOM 3401 N N . ARG A 1 444 ? 7.006 41.782 36.836 1.00 22.92 ? 440 ARG A N 1 ATOM 3402 C CA . ARG A 1 444 ? 6.239 41.043 35.822 1.00 24.44 ? 440 ARG A CA 1 ATOM 3403 C C . ARG A 1 444 ? 7.205 40.618 34.688 1.00 25.62 ? 440 ARG A C 1 ATOM 3404 O O . ARG A 1 444 ? 7.290 41.269 33.632 1.00 24.18 ? 440 ARG A O 1 ATOM 3405 C CB . ARG A 1 444 ? 5.074 41.909 35.297 1.00 25.91 ? 440 ARG A CB 1 ATOM 3406 C CG . ARG A 1 444 ? 4.133 41.111 34.290 1.00 29.72 ? 440 ARG A CG 1 ATOM 3407 C CD . ARG A 1 444 ? 2.668 41.635 34.432 1.00 35.92 ? 440 ARG A CD 1 ATOM 3408 N NE A ARG A 1 444 ? 1.873 40.452 34.768 0.60 39.46 ? 440 ARG A NE 1 ATOM 3409 N NE B ARG A 1 444 ? 2.320 41.628 35.854 0.40 35.56 ? 440 ARG A NE 1 ATOM 3410 C CZ A ARG A 1 444 ? 1.666 39.998 36.004 0.60 36.12 ? 440 ARG A CZ 1 ATOM 3411 C CZ B ARG A 1 444 ? 1.093 41.508 36.353 0.40 35.48 ? 440 ARG A CZ 1 ATOM 3412 N NH1 A ARG A 1 444 ? 2.134 40.674 37.083 0.60 34.02 ? 440 ARG A NH1 1 ATOM 3413 N NH1 B ARG A 1 444 ? 0.039 41.408 35.547 0.40 35.31 ? 440 ARG A NH1 1 ATOM 3414 N NH2 A ARG A 1 444 ? 0.963 38.892 36.148 0.60 28.18 ? 440 ARG A NH2 1 ATOM 3415 N NH2 B ARG A 1 444 ? 0.928 41.483 37.672 0.40 34.41 ? 440 ARG A NH2 1 ATOM 3416 N N . THR A 1 445 ? 7.940 39.532 34.934 1.00 23.33 ? 441 THR A N 1 ATOM 3417 C CA . THR A 1 445 ? 9.045 39.165 34.079 1.00 24.56 ? 441 THR A CA 1 ATOM 3418 C C . THR A 1 445 ? 8.642 38.195 32.958 1.00 24.24 ? 441 THR A C 1 ATOM 3419 O O . THR A 1 445 ? 9.444 37.864 32.062 1.00 24.11 ? 441 THR A O 1 ATOM 3420 C CB . THR A 1 445 ? 10.152 38.442 34.900 1.00 24.60 ? 441 THR A CB 1 ATOM 3421 O OG1 . THR A 1 445 ? 9.600 37.305 35.555 1.00 26.15 ? 441 THR A OG1 1 ATOM 3422 C CG2 . THR A 1 445 ? 10.727 39.376 35.998 1.00 25.54 ? 441 THR A CG2 1 ATOM 3423 N N . THR A 1 446 ? 7.436 37.673 33.060 1.00 23.69 ? 442 THR A N 1 ATOM 3424 C CA . THR A 1 446 ? 6.925 36.733 32.053 1.00 23.19 ? 442 THR A CA 1 ATOM 3425 C C . THR A 1 446 ? 5.392 36.692 32.157 1.00 23.57 ? 442 THR A C 1 ATOM 3426 O O . THR A 1 446 ? 4.781 37.607 32.718 1.00 23.20 ? 442 THR A O 1 ATOM 3427 C CB . THR A 1 446 ? 7.565 35.300 32.237 1.00 22.69 ? 442 THR A CB 1 ATOM 3428 O OG1 . THR A 1 446 ? 7.164 34.451 31.151 1.00 25.22 ? 442 THR A OG1 1 ATOM 3429 C CG2 . THR A 1 446 ? 7.153 34.645 33.608 1.00 19.60 ? 442 THR A CG2 1 ATOM 3430 N N . VAL A 1 447 ? 4.757 35.709 31.527 1.00 21.81 ? 443 VAL A N 1 ATOM 3431 C CA . VAL A 1 447 ? 3.305 35.667 31.494 1.00 20.54 ? 443 VAL A CA 1 ATOM 3432 C C . VAL A 1 447 ? 2.817 34.784 32.682 1.00 21.67 ? 443 VAL A C 1 ATOM 3433 O O . VAL A 1 447 ? 3.320 33.664 32.852 1.00 21.96 ? 443 VAL A O 1 ATOM 3434 C CB . VAL A 1 447 ? 2.771 35.126 30.116 1.00 21.39 ? 443 VAL A CB 1 ATOM 3435 C CG1 . VAL A 1 447 ? 1.196 34.981 30.196 1.00 22.18 ? 443 VAL A CG1 1 ATOM 3436 C CG2 . VAL A 1 447 ? 3.151 36.112 28.888 1.00 22.38 ? 443 VAL A CG2 1 ATOM 3437 N N . GLY A 1 448 ? 1.893 35.269 33.526 1.00 19.37 ? 444 GLY A N 1 ATOM 3438 C CA . GLY A 1 448 ? 1.459 34.457 34.649 1.00 20.50 ? 444 GLY A CA 1 ATOM 3439 C C . GLY A 1 448 ? 0.376 35.191 35.426 1.00 22.22 ? 444 GLY A C 1 ATOM 3440 O O . GLY A 1 448 ? -0.177 36.222 34.943 1.00 21.34 ? 444 GLY A O 1 ATOM 3441 N N . THR A 1 449 ? 0.059 34.646 36.589 1.00 20.64 ? 445 THR A N 1 ATOM 3442 C CA . THR A 1 449 ? -0.989 35.218 37.466 1.00 21.08 ? 445 THR A CA 1 ATOM 3443 C C . THR A 1 449 ? -0.403 35.337 38.863 1.00 20.86 ? 445 THR A C 1 ATOM 3444 O O . THR A 1 449 ? 0.006 34.345 39.436 1.00 20.09 ? 445 THR A O 1 ATOM 3445 C CB . THR A 1 449 ? -2.263 34.293 37.468 1.00 20.83 ? 445 THR A CB 1 ATOM 3446 O OG1 . THR A 1 449 ? -2.760 34.157 36.112 1.00 18.95 ? 445 THR A OG1 1 ATOM 3447 C CG2 . THR A 1 449 ? -3.385 34.929 38.305 1.00 20.21 ? 445 THR A CG2 1 ATOM 3448 N N . THR A 1 450 ? -0.346 36.559 39.405 1.00 20.12 ? 446 THR A N 1 ATOM 3449 C CA . THR A 1 450 ? 0.200 36.723 40.761 1.00 20.07 ? 446 THR A CA 1 ATOM 3450 C C . THR A 1 450 ? -0.879 36.309 41.766 1.00 19.84 ? 446 THR A C 1 ATOM 3451 O O . THR A 1 450 ? -2.058 36.025 41.404 1.00 20.15 ? 446 THR A O 1 ATOM 3452 C CB . THR A 1 450 ? 0.563 38.177 41.023 1.00 20.13 ? 446 THR A CB 1 ATOM 3453 O OG1 . THR A 1 450 ? -0.638 39.018 40.939 1.00 19.49 ? 446 THR A OG1 1 ATOM 3454 C CG2 . THR A 1 450 ? 1.638 38.685 39.953 1.00 20.81 ? 446 THR A CG2 1 ATOM 3455 N N . ILE A 1 451 ? -0.528 36.304 43.037 1.00 19.56 ? 447 ILE A N 1 ATOM 3456 C CA . ILE A 1 451 ? -1.526 35.921 44.079 1.00 20.22 ? 447 ILE A CA 1 ATOM 3457 C C . ILE A 1 451 ? -2.663 36.917 44.079 1.00 20.15 ? 447 ILE A C 1 ATOM 3458 O O . ILE A 1 451 ? -3.844 36.555 44.158 1.00 20.59 ? 447 ILE A O 1 ATOM 3459 C CB . ILE A 1 451 ? -0.833 35.829 45.442 1.00 21.60 ? 447 ILE A CB 1 ATOM 3460 C CG1 . ILE A 1 451 ? 0.026 34.539 45.436 1.00 19.09 ? 447 ILE A CG1 1 ATOM 3461 C CG2 . ILE A 1 451 ? -1.875 35.669 46.590 1.00 21.23 ? 447 ILE A CG2 1 ATOM 3462 C CD1 . ILE A 1 451 ? 1.027 34.468 46.634 1.00 22.09 ? 447 ILE A CD1 1 ATOM 3463 N N . LEU A 1 452 ? -2.335 38.191 43.979 1.00 20.67 ? 448 LEU A N 1 ATOM 3464 C CA . LEU A 1 452 ? -3.407 39.217 43.973 1.00 20.82 ? 448 LEU A CA 1 ATOM 3465 C C . LEU A 1 452 ? -4.352 39.022 42.772 1.00 21.04 ? 448 LEU A C 1 ATOM 3466 O O . LEU A 1 452 ? -5.583 39.053 42.905 1.00 21.84 ? 448 LEU A O 1 ATOM 3467 C CB . LEU A 1 452 ? -2.739 40.614 43.889 1.00 21.46 ? 448 LEU A CB 1 ATOM 3468 C CG . LEU A 1 452 ? -3.665 41.784 43.570 1.00 19.60 ? 448 LEU A CG 1 ATOM 3469 C CD1 . LEU A 1 452 ? -4.702 41.932 44.774 1.00 20.46 ? 448 LEU A CD1 1 ATOM 3470 C CD2 . LEU A 1 452 ? -2.915 43.195 43.335 1.00 20.43 ? 448 LEU A CD2 1 ATOM 3471 N N . GLU A 1 453 ? -3.776 38.844 41.588 1.00 20.75 ? 449 GLU A N 1 ATOM 3472 C CA . GLU A 1 453 ? -4.582 38.528 40.385 1.00 21.24 ? 449 GLU A CA 1 ATOM 3473 C C . GLU A 1 453 ? -5.442 37.308 40.566 1.00 20.92 ? 449 GLU A C 1 ATOM 3474 O O . GLU A 1 453 ? -6.633 37.290 40.135 1.00 21.48 ? 449 GLU A O 1 ATOM 3475 C CB . GLU A 1 453 ? -3.674 38.358 39.144 1.00 22.41 ? 449 GLU A CB 1 ATOM 3476 C CG . GLU A 1 453 ? -3.103 39.680 38.699 1.00 24.62 ? 449 GLU A CG 1 ATOM 3477 C CD . GLU A 1 453 ? -1.898 39.591 37.756 1.00 32.91 ? 449 GLU A CD 1 ATOM 3478 O OE1 . GLU A 1 453 ? -1.259 38.523 37.505 1.00 24.28 ? 449 GLU A OE1 1 ATOM 3479 O OE2 . GLU A 1 453 ? -1.490 40.693 37.334 1.00 39.57 ? 449 GLU A OE2 1 ATOM 3480 N N . ALA A 1 454 ? -4.869 36.268 41.182 1.00 19.48 ? 450 ALA A N 1 ATOM 3481 C CA . ALA A 1 454 ? -5.637 35.023 41.446 1.00 18.92 ? 450 ALA A CA 1 ATOM 3482 C C . ALA A 1 454 ? -6.800 35.272 42.442 1.00 21.15 ? 450 ALA A C 1 ATOM 3483 O O . ALA A 1 454 ? -7.886 34.722 42.298 1.00 20.81 ? 450 ALA A O 1 ATOM 3484 C CB . ALA A 1 454 ? -4.711 33.951 42.019 1.00 17.41 ? 450 ALA A CB 1 ATOM 3485 N N . VAL A 1 455 ? -6.562 36.084 43.469 1.00 20.44 ? 451 VAL A N 1 ATOM 3486 C CA . VAL A 1 455 ? -7.646 36.412 44.401 1.00 21.12 ? 451 VAL A CA 1 ATOM 3487 C C . VAL A 1 455 ? -8.778 37.142 43.675 1.00 22.03 ? 451 VAL A C 1 ATOM 3488 O O . VAL A 1 455 ? -9.991 36.795 43.844 1.00 22.31 ? 451 VAL A O 1 ATOM 3489 C CB . VAL A 1 455 ? -7.104 37.334 45.525 1.00 20.13 ? 451 VAL A CB 1 ATOM 3490 C CG1 . VAL A 1 455 ? -8.290 37.864 46.382 1.00 21.71 ? 451 VAL A CG1 1 ATOM 3491 C CG2 . VAL A 1 455 ? -6.114 36.520 46.438 1.00 19.22 ? 451 VAL A CG2 1 ATOM 3492 N N . LYS A 1 456 ? -8.416 38.143 42.853 1.00 21.09 ? 452 LYS A N 1 ATOM 3493 C CA . LYS A 1 456 ? -9.456 38.888 42.125 1.00 22.88 ? 452 LYS A CA 1 ATOM 3494 C C . LYS A 1 456 ? -10.242 37.981 41.159 1.00 22.36 ? 452 LYS A C 1 ATOM 3495 O O . LYS A 1 456 ? -11.435 38.224 40.903 1.00 23.35 ? 452 LYS A O 1 ATOM 3496 C CB . LYS A 1 456 ? -8.793 40.012 41.296 1.00 22.60 ? 452 LYS A CB 1 ATOM 3497 C CG . LYS A 1 456 ? -8.238 41.121 42.235 1.00 24.91 ? 452 LYS A CG 1 ATOM 3498 C CD . LYS A 1 456 ? -7.464 42.114 41.332 1.00 30.06 ? 452 LYS A CD 1 ATOM 3499 C CE . LYS A 1 456 ? -6.950 43.244 42.155 1.00 34.10 ? 452 LYS A CE 1 ATOM 3500 N NZ . LYS A 1 456 ? -6.312 44.287 41.231 1.00 37.62 ? 452 LYS A NZ 1 ATOM 3501 N N . ALA A 1 457 ? -9.548 37.006 40.568 1.00 22.33 ? 453 ALA A N 1 ATOM 3502 C CA . ALA A 1 457 ? -10.193 36.027 39.654 1.00 22.53 ? 453 ALA A CA 1 ATOM 3503 C C . ALA A 1 457 ? -11.105 35.080 40.389 1.00 23.85 ? 453 ALA A C 1 ATOM 3504 O O . ALA A 1 457 ? -11.962 34.460 39.729 1.00 23.30 ? 453 ALA A O 1 ATOM 3505 C CB . ALA A 1 457 ? -9.153 35.218 38.853 1.00 21.68 ? 453 ALA A CB 1 ATOM 3506 N N . ALA A 1 458 ? -10.843 34.844 41.684 1.00 22.57 ? 454 ALA A N 1 ATOM 3507 C CA . ALA A 1 458 ? -11.594 33.834 42.424 1.00 23.61 ? 454 ALA A CA 1 ATOM 3508 C C . ALA A 1 458 ? -12.836 34.329 43.145 1.00 24.11 ? 454 ALA A C 1 ATOM 3509 O O . ALA A 1 458 ? -13.794 33.538 43.326 1.00 24.89 ? 454 ALA A O 1 ATOM 3510 C CB . ALA A 1 458 ? -10.678 33.140 43.499 1.00 25.05 ? 454 ALA A CB 1 ATOM 3511 N N . VAL A 1 459 ? -12.772 35.547 43.701 1.00 22.81 ? 455 VAL A N 1 ATOM 3512 C CA . VAL A 1 459 ? -13.832 35.996 44.651 1.00 22.39 ? 455 VAL A CA 1 ATOM 3513 C C . VAL A 1 459 ? -15.149 36.379 43.946 1.00 24.22 ? 455 VAL A C 1 ATOM 3514 O O . VAL A 1 459 ? -15.160 36.712 42.752 1.00 23.98 ? 455 VAL A O 1 ATOM 3515 C CB . VAL A 1 459 ? -13.376 37.177 45.537 1.00 19.99 ? 455 VAL A CB 1 ATOM 3516 C CG1 . VAL A 1 459 ? -12.234 36.723 46.484 1.00 19.65 ? 455 VAL A CG1 1 ATOM 3517 C CG2 . VAL A 1 459 ? -12.930 38.345 44.662 1.00 21.82 ? 455 VAL A CG2 1 ATOM 3518 N N . ASP A 1 460 ? -16.242 36.401 44.727 1.00 26.07 ? 456 ASP A N 1 ATOM 3519 C CA . ASP A 1 460 ? -17.589 36.751 44.242 1.00 25.87 ? 456 ASP A CA 1 ATOM 3520 C C . ASP A 1 460 ? -17.461 38.176 43.700 1.00 25.01 ? 456 ASP A C 1 ATOM 3521 O O . ASP A 1 460 ? -16.625 38.950 44.184 1.00 24.96 ? 456 ASP A O 1 ATOM 3522 C CB . ASP A 1 460 ? -18.531 36.738 45.445 1.00 25.96 ? 456 ASP A CB 1 ATOM 3523 C CG . ASP A 1 460 ? -19.979 36.929 45.072 1.00 30.78 ? 456 ASP A CG 1 ATOM 3524 O OD1 . ASP A 1 460 ? -20.484 38.085 45.025 1.00 30.08 ? 456 ASP A OD1 1 ATOM 3525 O OD2 . ASP A 1 460 ? -20.583 35.891 44.784 1.00 34.73 ? 456 ASP A OD2 1 ATOM 3526 N N . PRO A 1 461 ? -18.281 38.538 42.704 1.00 24.87 ? 457 PRO A N 1 ATOM 3527 C CA . PRO A 1 461 ? -18.217 39.878 42.176 1.00 25.18 ? 457 PRO A CA 1 ATOM 3528 C C . PRO A 1 461 ? -18.506 41.001 43.180 1.00 26.08 ? 457 PRO A C 1 ATOM 3529 O O . PRO A 1 461 ? -18.038 42.124 42.966 1.00 25.72 ? 457 PRO A O 1 ATOM 3530 C CB . PRO A 1 461 ? -19.317 39.878 41.067 1.00 25.97 ? 457 PRO A CB 1 ATOM 3531 C CG . PRO A 1 461 ? -20.104 38.636 41.255 1.00 24.27 ? 457 PRO A CG 1 ATOM 3532 C CD . PRO A 1 461 ? -19.087 37.664 41.812 1.00 25.28 ? 457 PRO A CD 1 ATOM 3533 N N . SER A 1 462 ? -19.286 40.711 44.222 1.00 25.81 ? 458 SER A N 1 ATOM 3534 C CA . SER A 1 462 ? -19.573 41.723 45.249 1.00 27.31 ? 458 SER A CA 1 ATOM 3535 C C . SER A 1 462 ? -18.385 41.927 46.228 1.00 26.86 ? 458 SER A C 1 ATOM 3536 O O . SER A 1 462 ? -18.395 42.862 47.020 1.00 27.45 ? 458 SER A O 1 ATOM 3537 C CB . SER A 1 462 ? -20.874 41.382 46.009 1.00 27.74 ? 458 SER A CB 1 ATOM 3538 O OG . SER A 1 462 ? -20.680 40.258 46.842 1.00 28.04 ? 458 SER A OG 1 ATOM 3539 N N . THR A 1 463 ? -17.366 41.062 46.170 1.00 25.50 ? 459 THR A N 1 ATOM 3540 C CA . THR A 1 463 ? -16.251 41.186 47.102 1.00 24.56 ? 459 THR A CA 1 ATOM 3541 C C . THR A 1 463 ? -15.279 42.252 46.627 1.00 25.16 ? 459 THR A C 1 ATOM 3542 O O . THR A 1 463 ? -14.681 42.127 45.535 1.00 25.15 ? 459 THR A O 1 ATOM 3543 C CB . THR A 1 463 ? -15.505 39.863 47.231 1.00 24.98 ? 459 THR A CB 1 ATOM 3544 O OG1 . THR A 1 463 ? -16.417 38.871 47.719 1.00 24.05 ? 459 THR A OG1 1 ATOM 3545 C CG2 . THR A 1 463 ? -14.269 40.017 48.203 1.00 22.24 ? 459 THR A CG2 1 ATOM 3546 N N . VAL A 1 464 ? -15.053 43.256 47.470 1.00 24.12 ? 460 VAL A N 1 ATOM 3547 C CA . VAL A 1 464 ? -14.126 44.297 47.110 1.00 24.05 ? 460 VAL A CA 1 ATOM 3548 C C . VAL A 1 464 ? -12.730 43.843 47.545 1.00 23.83 ? 460 VAL A C 1 ATOM 3549 O O . VAL A 1 464 ? -12.536 43.529 48.731 1.00 24.03 ? 460 VAL A O 1 ATOM 3550 C CB . VAL A 1 464 ? -14.504 45.640 47.764 1.00 22.21 ? 460 VAL A CB 1 ATOM 3551 C CG1 . VAL A 1 464 ? -13.374 46.778 47.478 1.00 25.32 ? 460 VAL A CG1 1 ATOM 3552 C CG2 . VAL A 1 464 ? -15.895 46.129 47.200 1.00 25.39 ? 460 VAL A CG2 1 ATOM 3553 N N . VAL A 1 465 ? -11.745 43.887 46.633 1.00 23.84 ? 461 VAL A N 1 ATOM 3554 C CA . VAL A 1 465 ? -10.366 43.435 46.978 1.00 23.37 ? 461 VAL A CA 1 ATOM 3555 C C . VAL A 1 465 ? -9.459 44.671 47.057 1.00 24.70 ? 461 VAL A C 1 ATOM 3556 O O . VAL A 1 465 ? -9.360 45.421 46.077 1.00 24.15 ? 461 VAL A O 1 ATOM 3557 C CB . VAL A 1 465 ? -9.837 42.518 45.860 1.00 24.09 ? 461 VAL A CB 1 ATOM 3558 C CG1 . VAL A 1 465 ? -8.346 42.034 46.182 1.00 21.97 ? 461 VAL A CG1 1 ATOM 3559 C CG2 . VAL A 1 465 ? -10.765 41.261 45.743 1.00 20.17 ? 461 VAL A CG2 1 ATOM 3560 N N . VAL A 1 466 ? -8.849 44.912 48.213 1.00 23.40 ? 462 VAL A N 1 ATOM 3561 C CA . VAL A 1 466 ? -7.904 46.001 48.355 1.00 22.75 ? 462 VAL A CA 1 ATOM 3562 C C . VAL A 1 466 ? -6.484 45.433 48.381 1.00 23.43 ? 462 VAL A C 1 ATOM 3563 O O . VAL A 1 466 ? -6.195 44.495 49.128 1.00 23.37 ? 462 VAL A O 1 ATOM 3564 C CB . VAL A 1 466 ? -8.157 46.790 49.665 1.00 24.08 ? 462 VAL A CB 1 ATOM 3565 C CG1 . VAL A 1 466 ? -7.115 47.867 49.855 1.00 22.69 ? 462 VAL A CG1 1 ATOM 3566 C CG2 . VAL A 1 466 ? -9.610 47.406 49.620 1.00 23.62 ? 462 VAL A CG2 1 ATOM 3567 N N . PHE A 1 467 ? -5.596 46.007 47.581 1.00 23.88 ? 463 PHE A N 1 ATOM 3568 C CA . PHE A 1 467 ? -4.175 45.673 47.675 1.00 23.98 ? 463 PHE A CA 1 ATOM 3569 C C . PHE A 1 467 ? -3.408 46.802 48.368 1.00 24.51 ? 463 PHE A C 1 ATOM 3570 O O . PHE A 1 467 ? -3.630 47.971 48.066 1.00 24.30 ? 463 PHE A O 1 ATOM 3571 C CB . PHE A 1 467 ? -3.586 45.413 46.278 1.00 24.41 ? 463 PHE A CB 1 ATOM 3572 C CG . PHE A 1 467 ? -2.082 45.204 46.291 1.00 22.92 ? 463 PHE A CG 1 ATOM 3573 C CD1 . PHE A 1 467 ? -1.524 44.101 46.899 1.00 25.07 ? 463 PHE A CD1 1 ATOM 3574 C CD2 . PHE A 1 467 ? -1.241 46.126 45.683 1.00 27.28 ? 463 PHE A CD2 1 ATOM 3575 C CE1 . PHE A 1 467 ? -0.149 43.935 46.940 1.00 27.57 ? 463 PHE A CE1 1 ATOM 3576 C CE2 . PHE A 1 467 ? 0.160 45.952 45.689 1.00 28.72 ? 463 PHE A CE2 1 ATOM 3577 C CZ . PHE A 1 467 ? 0.711 44.865 46.304 1.00 25.22 ? 463 PHE A CZ 1 ATOM 3578 N N . ALA A 1 468 ? -2.546 46.430 49.309 1.00 23.57 ? 464 ALA A N 1 ATOM 3579 C CA . ALA A 1 468 ? -1.562 47.342 49.875 1.00 24.67 ? 464 ALA A CA 1 ATOM 3580 C C . ALA A 1 468 ? -0.293 46.559 50.131 1.00 26.04 ? 464 ALA A C 1 ATOM 3581 O O . ALA A 1 468 ? -0.299 45.559 50.877 1.00 25.62 ? 464 ALA A O 1 ATOM 3582 C CB . ALA A 1 468 ? -2.087 47.962 51.211 1.00 24.26 ? 464 ALA A CB 1 ATOM 3583 N N . GLU A 1 469 ? 0.822 46.992 49.558 1.00 25.99 ? 465 GLU A N 1 ATOM 3584 C CA . GLU A 1 469 ? 2.014 46.146 49.665 1.00 25.95 ? 465 GLU A CA 1 ATOM 3585 C C . GLU A 1 469 ? 2.527 46.021 51.112 1.00 26.37 ? 465 GLU A C 1 ATOM 3586 O O . GLU A 1 469 ? 2.855 44.907 51.566 1.00 25.86 ? 465 GLU A O 1 ATOM 3587 C CB . GLU A 1 469 ? 3.114 46.697 48.749 1.00 27.23 ? 465 GLU A CB 1 ATOM 3588 C CG . GLU A 1 469 ? 4.328 45.759 48.789 1.00 27.95 ? 465 GLU A CG 1 ATOM 3589 C CD . GLU A 1 469 ? 5.400 46.121 47.809 1.00 35.66 ? 465 GLU A CD 1 ATOM 3590 O OE1 . GLU A 1 469 ? 5.060 46.763 46.800 1.00 39.08 ? 465 GLU A OE1 1 ATOM 3591 O OE2 . GLU A 1 469 ? 6.577 45.712 48.063 1.00 40.59 ? 465 GLU A OE2 1 ATOM 3592 N N . ASN A 1 470 ? 2.595 47.150 51.853 1.00 25.73 ? 466 ASN A N 1 ATOM 3593 C CA . ASN A 1 470 ? 3.092 47.177 53.220 1.00 26.06 ? 466 ASN A CA 1 ATOM 3594 C C . ASN A 1 470 ? 2.241 48.147 54.078 1.00 27.18 ? 466 ASN A C 1 ATOM 3595 O O . ASN A 1 470 ? 2.726 49.229 54.506 1.00 26.43 ? 466 ASN A O 1 ATOM 3596 C CB A ASN A 1 470 ? 4.547 47.702 53.210 0.50 27.96 ? 466 ASN A CB 1 ATOM 3597 C CB B ASN A 1 470 ? 4.602 47.529 53.336 0.50 27.23 ? 466 ASN A CB 1 ATOM 3598 C CG A ASN A 1 470 ? 5.271 47.448 54.509 0.50 27.44 ? 466 ASN A CG 1 ATOM 3599 C CG B ASN A 1 470 ? 5.531 46.460 52.728 0.50 26.17 ? 466 ASN A CG 1 ATOM 3600 O OD1 A ASN A 1 470 ? 6.320 48.058 54.801 0.50 33.40 ? 466 ASN A OD1 1 ATOM 3601 O OD1 B ASN A 1 470 ? 5.563 45.286 53.152 0.50 22.74 ? 466 ASN A OD1 1 ATOM 3602 N ND2 A ASN A 1 470 ? 4.742 46.532 55.295 0.50 29.32 ? 466 ASN A ND2 1 ATOM 3603 N ND2 B ASN A 1 470 ? 6.308 46.879 51.735 0.50 26.06 ? 466 ASN A ND2 1 ATOM 3604 N N . PRO A 1 471 ? 0.975 47.794 54.335 1.00 27.00 ? 467 PRO A N 1 ATOM 3605 C CA . PRO A 1 471 ? 0.102 48.695 55.135 1.00 26.72 ? 467 PRO A CA 1 ATOM 3606 C C . PRO A 1 471 ? 0.541 48.765 56.599 1.00 28.08 ? 467 PRO A C 1 ATOM 3607 O O . PRO A 1 471 ? 1.082 47.791 57.131 1.00 28.39 ? 467 PRO A O 1 ATOM 3608 C CB . PRO A 1 471 ? -1.282 47.997 55.053 1.00 27.19 ? 467 PRO A CB 1 ATOM 3609 C CG . PRO A 1 471 ? -0.948 46.472 54.887 1.00 25.73 ? 467 PRO A CG 1 ATOM 3610 C CD . PRO A 1 471 ? 0.300 46.529 53.938 1.00 25.26 ? 467 PRO A CD 1 ATOM 3611 N N . ASP A 1 472 ? 0.325 49.900 57.255 1.00 28.88 ? 468 ASP A N 1 ATOM 3612 C CA . ASP A 1 472 ? 0.553 49.981 58.699 1.00 29.71 ? 468 ASP A CA 1 ATOM 3613 C C . ASP A 1 472 ? -0.668 49.499 59.482 1.00 28.94 ? 468 ASP A C 1 ATOM 3614 O O . ASP A 1 472 ? -1.707 49.220 58.875 1.00 28.50 ? 468 ASP A O 1 ATOM 3615 C CB . ASP A 1 472 ? 1.033 51.354 59.140 1.00 31.01 ? 468 ASP A CB 1 ATOM 3616 C CG . ASP A 1 472 ? -0.010 52.443 58.977 1.00 33.99 ? 468 ASP A CG 1 ATOM 3617 O OD1 . ASP A 1 472 ? 0.388 53.617 59.043 1.00 36.22 ? 468 ASP A OD1 1 ATOM 3618 O OD2 . ASP A 1 472 ? -1.217 52.163 58.797 1.00 33.83 ? 468 ASP A OD2 1 ATOM 3619 N N . ALA A 1 473 ? -0.532 49.365 60.802 1.00 27.14 ? 469 ALA A N 1 ATOM 3620 C CA . ALA A 1 473 ? -1.546 48.699 61.612 1.00 27.26 ? 469 ALA A CA 1 ATOM 3621 C C . ALA A 1 473 ? -2.848 49.498 61.531 1.00 26.77 ? 469 ALA A C 1 ATOM 3622 O O . ALA A 1 473 ? -3.943 48.926 61.507 1.00 26.45 ? 469 ALA A O 1 ATOM 3623 C CB . ALA A 1 473 ? -1.046 48.558 63.131 1.00 29.09 ? 469 ALA A CB 1 ATOM 3624 N N . GLU A 1 474 ? -2.730 50.827 61.451 1.00 25.82 ? 470 GLU A N 1 ATOM 3625 C CA . GLU A 1 474 ? -3.934 51.692 61.428 1.00 26.14 ? 470 GLU A CA 1 ATOM 3626 C C . GLU A 1 474 ? -4.746 51.537 60.162 1.00 25.86 ? 470 GLU A C 1 ATOM 3627 O O . GLU A 1 474 ? -5.995 51.424 60.189 1.00 27.19 ? 470 GLU A O 1 ATOM 3628 C CB . GLU A 1 474 ? -3.551 53.197 61.624 1.00 26.02 ? 470 GLU A CB 1 ATOM 3629 C CG . GLU A 1 474 ? -4.768 54.097 61.495 1.00 31.44 ? 470 GLU A CG 1 ATOM 3630 C CD . GLU A 1 474 ? -4.439 55.599 61.530 1.00 37.30 ? 470 GLU A CD 1 ATOM 3631 O OE1 . GLU A 1 474 ? -5.319 56.384 61.100 1.00 37.17 ? 470 GLU A OE1 1 ATOM 3632 O OE2 . GLU A 1 474 ? -3.321 55.964 61.979 1.00 36.06 ? 470 GLU A OE2 1 ATOM 3633 N N . PHE A 1 475 ? -4.056 51.508 59.027 1.00 26.81 ? 471 PHE A N 1 ATOM 3634 C CA . PHE A 1 475 ? -4.727 51.251 57.768 1.00 27.21 ? 471 PHE A CA 1 ATOM 3635 C C . PHE A 1 475 ? -5.551 49.950 57.868 1.00 26.50 ? 471 PHE A C 1 ATOM 3636 O O . PHE A 1 475 ? -6.684 49.886 57.400 1.00 26.14 ? 471 PHE A O 1 ATOM 3637 C CB . PHE A 1 475 ? -3.670 51.111 56.665 1.00 27.53 ? 471 PHE A CB 1 ATOM 3638 C CG . PHE A 1 475 ? -4.229 50.742 55.316 1.00 28.41 ? 471 PHE A CG 1 ATOM 3639 C CD1 . PHE A 1 475 ? -4.476 49.426 54.992 1.00 30.58 ? 471 PHE A CD1 1 ATOM 3640 C CD2 . PHE A 1 475 ? -4.506 51.733 54.375 1.00 33.17 ? 471 PHE A CD2 1 ATOM 3641 C CE1 . PHE A 1 475 ? -4.997 49.052 53.722 1.00 31.71 ? 471 PHE A CE1 1 ATOM 3642 C CE2 . PHE A 1 475 ? -5.020 51.388 53.106 1.00 37.44 ? 471 PHE A CE2 1 ATOM 3643 C CZ . PHE A 1 475 ? -5.256 50.010 52.788 1.00 33.23 ? 471 PHE A CZ 1 ATOM 3644 N N . VAL A 1 476 ? -4.964 48.896 58.431 1.00 24.62 ? 472 VAL A N 1 ATOM 3645 C CA . VAL A 1 476 ? -5.691 47.605 58.507 1.00 24.91 ? 472 VAL A CA 1 ATOM 3646 C C . VAL A 1 476 ? -6.876 47.712 59.474 1.00 24.64 ? 472 VAL A C 1 ATOM 3647 O O . VAL A 1 476 ? -8.001 47.297 59.149 1.00 26.53 ? 472 VAL A O 1 ATOM 3648 C CB . VAL A 1 476 ? -4.746 46.494 58.976 1.00 23.37 ? 472 VAL A CB 1 ATOM 3649 C CG1 . VAL A 1 476 ? -5.495 45.134 59.009 1.00 25.49 ? 472 VAL A CG1 1 ATOM 3650 C CG2 . VAL A 1 476 ? -3.541 46.408 58.001 1.00 22.79 ? 472 VAL A CG2 1 ATOM 3651 N N . LYS A 1 477 ? -6.646 48.302 60.648 1.00 25.18 ? 473 LYS A N 1 ATOM 3652 C CA . LYS A 1 477 ? -7.745 48.415 61.653 1.00 26.25 ? 473 LYS A CA 1 ATOM 3653 C C . LYS A 1 477 ? -8.935 49.243 61.173 1.00 26.10 ? 473 LYS A C 1 ATOM 3654 O O . LYS A 1 477 ? -10.083 49.001 61.576 1.00 25.17 ? 473 LYS A O 1 ATOM 3655 C CB . LYS A 1 477 ? -7.249 48.978 62.968 1.00 26.09 ? 473 LYS A CB 1 ATOM 3656 C CG . LYS A 1 477 ? -6.385 47.982 63.739 1.00 31.28 ? 473 LYS A CG 1 ATOM 3657 C CD . LYS A 1 477 ? -5.851 48.605 65.037 1.00 40.98 ? 473 LYS A CD 1 ATOM 3658 C CE . LYS A 1 477 ? -4.405 48.166 65.304 1.00 50.35 ? 473 LYS A CE 1 ATOM 3659 N NZ . LYS A 1 477 ? -4.055 46.654 65.164 1.00 57.00 ? 473 LYS A NZ 1 ATOM 3660 N N . SER A 1 478 ? -8.634 50.213 60.314 1.00 25.76 ? 474 SER A N 1 ATOM 3661 C CA . SER A 1 478 ? -9.613 51.183 59.823 1.00 26.92 ? 474 SER A CA 1 ATOM 3662 C C . SER A 1 478 ? -10.312 50.713 58.554 1.00 27.27 ? 474 SER A C 1 ATOM 3663 O O . SER A 1 478 ? -11.291 51.334 58.132 1.00 26.12 ? 474 SER A O 1 ATOM 3664 C CB . SER A 1 478 ? -8.935 52.552 59.568 1.00 26.19 ? 474 SER A CB 1 ATOM 3665 O OG . SER A 1 478 ? -8.658 53.168 60.849 1.00 28.92 ? 474 SER A OG 1 ATOM 3666 N N . GLY A 1 479 ? -9.823 49.630 57.940 1.00 26.66 ? 475 GLY A N 1 ATOM 3667 C CA . GLY A 1 479 ? -10.270 49.342 56.602 1.00 27.24 ? 475 GLY A CA 1 ATOM 3668 C C . GLY A 1 479 ? -11.571 48.585 56.445 1.00 27.71 ? 475 GLY A C 1 ATOM 3669 O O . GLY A 1 479 ? -12.050 48.443 55.312 1.00 28.47 ? 475 GLY A O 1 ATOM 3670 N N . GLY A 1 480 ? -12.153 48.093 57.541 1.00 27.10 ? 476 GLY A N 1 ATOM 3671 C CA . GLY A 1 480 ? -13.378 47.300 57.407 1.00 27.62 ? 476 GLY A CA 1 ATOM 3672 C C . GLY A 1 480 ? -13.207 45.982 56.630 1.00 26.98 ? 476 GLY A C 1 ATOM 3673 O O . GLY A 1 480 ? -14.128 45.540 55.907 1.00 27.24 ? 476 GLY A O 1 ATOM 3674 N N . PHE A 1 481 ? -12.048 45.327 56.807 1.00 26.33 ? 477 PHE A N 1 ATOM 3675 C CA . PHE A 1 481 ? -11.749 44.065 56.093 1.00 25.49 ? 477 PHE A CA 1 ATOM 3676 C C . PHE A 1 481 ? -12.341 42.843 56.817 1.00 26.25 ? 477 PHE A C 1 ATOM 3677 O O . PHE A 1 481 ? -12.372 42.829 58.050 1.00 26.20 ? 477 PHE A O 1 ATOM 3678 C CB . PHE A 1 481 ? -10.250 43.894 56.001 1.00 25.57 ? 477 PHE A CB 1 ATOM 3679 C CG . PHE A 1 481 ? -9.605 44.975 55.219 1.00 24.29 ? 477 PHE A CG 1 ATOM 3680 C CD1 . PHE A 1 481 ? -9.925 45.136 53.865 1.00 24.98 ? 477 PHE A CD1 1 ATOM 3681 C CD2 . PHE A 1 481 ? -8.710 45.851 55.828 1.00 21.03 ? 477 PHE A CD2 1 ATOM 3682 C CE1 . PHE A 1 481 ? -9.368 46.177 53.094 1.00 22.62 ? 477 PHE A CE1 1 ATOM 3683 C CE2 . PHE A 1 481 ? -8.098 46.873 55.066 1.00 25.67 ? 477 PHE A CE2 1 ATOM 3684 C CZ . PHE A 1 481 ? -8.446 47.042 53.702 1.00 23.00 ? 477 PHE A CZ 1 ATOM 3685 N N . SER A 1 482 ? -12.843 41.853 56.070 1.00 25.39 ? 478 SER A N 1 ATOM 3686 C CA . SER A 1 482 ? -13.265 40.587 56.663 1.00 25.47 ? 478 SER A CA 1 ATOM 3687 C C . SER A 1 482 ? -12.106 39.682 57.042 1.00 25.84 ? 478 SER A C 1 ATOM 3688 O O . SER A 1 482 ? -12.209 38.879 58.001 1.00 25.03 ? 478 SER A O 1 ATOM 3689 C CB . SER A 1 482 ? -14.166 39.808 55.672 1.00 25.88 ? 478 SER A CB 1 ATOM 3690 O OG . SER A 1 482 ? -15.336 40.571 55.421 1.00 25.78 ? 478 SER A OG 1 ATOM 3691 N N . TYR A 1 483 ? -11.050 39.710 56.219 1.00 23.90 ? 479 TYR A N 1 ATOM 3692 C CA . TYR A 1 483 ? -9.831 38.938 56.513 1.00 23.22 ? 479 TYR A CA 1 ATOM 3693 C C . TYR A 1 483 ? -8.726 39.467 55.597 1.00 23.39 ? 479 TYR A C 1 ATOM 3694 O O . TYR A 1 483 ? -9.024 40.305 54.732 1.00 23.48 ? 479 TYR A O 1 ATOM 3695 C CB . TYR A 1 483 ? -10.063 37.441 56.205 1.00 23.45 ? 479 TYR A CB 1 ATOM 3696 C CG . TYR A 1 483 ? -10.611 37.143 54.843 1.00 25.71 ? 479 TYR A CG 1 ATOM 3697 C CD1 . TYR A 1 483 ? -9.751 37.083 53.705 1.00 24.29 ? 479 TYR A CD1 1 ATOM 3698 C CD2 . TYR A 1 483 ? -11.991 36.834 54.669 1.00 26.16 ? 479 TYR A CD2 1 ATOM 3699 C CE1 . TYR A 1 483 ? -10.266 36.797 52.434 1.00 22.94 ? 479 TYR A CE1 1 ATOM 3700 C CE2 . TYR A 1 483 ? -12.508 36.531 53.417 1.00 28.25 ? 479 TYR A CE2 1 ATOM 3701 C CZ . TYR A 1 483 ? -11.643 36.472 52.305 1.00 29.59 ? 479 TYR A CZ 1 ATOM 3702 O OH . TYR A 1 483 ? -12.164 36.163 51.072 1.00 30.83 ? 479 TYR A OH 1 ATOM 3703 N N . ALA A 1 484 ? -7.477 38.995 55.786 1.00 22.69 ? 480 ALA A N 1 ATOM 3704 C CA . ALA A 1 484 ? -6.403 39.391 54.886 1.00 22.47 ? 480 ALA A CA 1 ATOM 3705 C C . ALA A 1 484 ? -5.668 38.168 54.412 1.00 23.37 ? 480 ALA A C 1 ATOM 3706 O O . ALA A 1 484 ? -5.566 37.187 55.151 1.00 23.24 ? 480 ALA A O 1 ATOM 3707 C CB . ALA A 1 484 ? -5.401 40.330 55.604 1.00 21.59 ? 480 ALA A CB 1 ATOM 3708 N N . ILE A 1 485 ? -5.109 38.269 53.208 1.00 22.84 ? 481 ILE A N 1 ATOM 3709 C CA . ILE A 1 485 ? -4.167 37.287 52.697 1.00 22.99 ? 481 ILE A CA 1 ATOM 3710 C C . ILE A 1 485 ? -2.882 38.046 52.555 1.00 22.39 ? 481 ILE A C 1 ATOM 3711 O O . ILE A 1 485 ? -2.821 39.067 51.858 1.00 24.18 ? 481 ILE A O 1 ATOM 3712 C CB . ILE A 1 485 ? -4.595 36.727 51.321 1.00 22.60 ? 481 ILE A CB 1 ATOM 3713 C CG1 . ILE A 1 485 ? -5.906 35.900 51.470 1.00 23.32 ? 481 ILE A CG1 1 ATOM 3714 C CG2 . ILE A 1 485 ? -3.435 35.865 50.723 1.00 23.38 ? 481 ILE A CG2 1 ATOM 3715 C CD1 . ILE A 1 485 ? -6.655 35.717 50.111 1.00 23.94 ? 481 ILE A CD1 1 ATOM 3716 N N . VAL A 1 486 ? -1.854 37.604 53.254 1.00 21.57 ? 482 VAL A N 1 ATOM 3717 C CA . VAL A 1 486 ? -0.569 38.351 53.227 1.00 20.91 ? 482 VAL A CA 1 ATOM 3718 C C . VAL A 1 486 ? 0.565 37.421 52.798 1.00 22.08 ? 482 VAL A C 1 ATOM 3719 O O . VAL A 1 486 ? 0.759 36.333 53.381 1.00 22.33 ? 482 VAL A O 1 ATOM 3720 C CB . VAL A 1 486 ? -0.265 39.101 54.592 1.00 20.75 ? 482 VAL A CB 1 ATOM 3721 C CG1 A VAL A 1 486 ? -0.616 38.249 55.829 0.60 22.28 ? 482 VAL A CG1 1 ATOM 3722 C CG1 B VAL A 1 486 ? -1.473 39.745 55.124 0.40 19.40 ? 482 VAL A CG1 1 ATOM 3723 C CG2 A VAL A 1 486 ? 1.145 39.815 54.613 0.60 17.16 ? 482 VAL A CG2 1 ATOM 3724 C CG2 B VAL A 1 486 ? 0.256 38.111 55.624 0.40 23.05 ? 482 VAL A CG2 1 ATOM 3725 N N . ALA A 1 487 ? 1.355 37.879 51.824 1.00 21.65 ? 483 ALA A N 1 ATOM 3726 C CA . ALA A 1 487 ? 2.365 37.009 51.229 1.00 21.70 ? 483 ALA A CA 1 ATOM 3727 C C . ALA A 1 487 ? 3.727 37.654 51.293 1.00 20.95 ? 483 ALA A C 1 ATOM 3728 O O . ALA A 1 487 ? 3.885 38.814 50.866 1.00 22.38 ? 483 ALA A O 1 ATOM 3729 C CB . ALA A 1 487 ? 1.965 36.666 49.735 1.00 20.85 ? 483 ALA A CB 1 ATOM 3730 N N . VAL A 1 488 ? 4.703 36.921 51.845 1.00 21.26 ? 484 VAL A N 1 ATOM 3731 C CA . VAL A 1 488 ? 6.051 37.452 52.117 1.00 22.26 ? 484 VAL A CA 1 ATOM 3732 C C . VAL A 1 488 ? 7.019 36.300 51.907 1.00 22.38 ? 484 VAL A C 1 ATOM 3733 O O . VAL A 1 488 ? 6.586 35.160 51.705 1.00 22.11 ? 484 VAL A O 1 ATOM 3734 C CB . VAL A 1 488 ? 6.197 37.946 53.583 1.00 23.79 ? 484 VAL A CB 1 ATOM 3735 C CG1 . VAL A 1 488 ? 5.255 39.155 53.814 1.00 23.04 ? 484 VAL A CG1 1 ATOM 3736 C CG2 . VAL A 1 488 ? 5.907 36.774 54.608 1.00 22.27 ? 484 VAL A CG2 1 ATOM 3737 N N . GLY A 1 489 ? 8.306 36.580 51.927 1.00 21.54 ? 485 GLY A N 1 ATOM 3738 C CA . GLY A 1 489 ? 9.250 35.454 51.858 1.00 21.44 ? 485 GLY A CA 1 ATOM 3739 C C . GLY A 1 489 ? 10.585 35.838 51.216 1.00 21.88 ? 485 GLY A C 1 ATOM 3740 O O . GLY A 1 489 ? 11.000 36.991 51.263 1.00 22.38 ? 485 GLY A O 1 ATOM 3741 N N . GLU A 1 490 ? 11.246 34.842 50.633 1.00 21.70 ? 486 GLU A N 1 ATOM 3742 C CA . GLU A 1 490 ? 12.568 35.047 50.057 1.00 22.33 ? 486 GLU A CA 1 ATOM 3743 C C . GLU A 1 490 ? 12.535 35.737 48.720 1.00 21.78 ? 486 GLU A C 1 ATOM 3744 O O . GLU A 1 490 ? 11.594 35.603 47.959 1.00 20.59 ? 486 GLU A O 1 ATOM 3745 C CB . GLU A 1 490 ? 13.277 33.696 49.887 1.00 22.08 ? 486 GLU A CB 1 ATOM 3746 C CG . GLU A 1 490 ? 13.496 32.959 51.217 1.00 22.11 ? 486 GLU A CG 1 ATOM 3747 C CD . GLU A 1 490 ? 14.501 31.820 51.021 1.00 25.08 ? 486 GLU A CD 1 ATOM 3748 O OE1 . GLU A 1 490 ? 14.246 30.864 50.234 1.00 23.50 ? 486 GLU A OE1 1 ATOM 3749 O OE2 . GLU A 1 490 ? 15.565 31.903 51.640 1.00 22.30 ? 486 GLU A OE2 1 ATOM 3750 N N . HIS A 1 491 ? 13.637 36.395 48.405 1.00 21.52 ? 487 HIS A N 1 ATOM 3751 C CA . HIS A 1 491 ? 13.849 36.927 47.070 1.00 22.49 ? 487 HIS A CA 1 ATOM 3752 C C . HIS A 1 491 ? 14.439 35.850 46.200 1.00 21.38 ? 487 HIS A C 1 ATOM 3753 O O . HIS A 1 491 ? 14.917 34.856 46.739 1.00 22.46 ? 487 HIS A O 1 ATOM 3754 C CB . HIS A 1 491 ? 14.812 38.114 47.134 1.00 23.14 ? 487 HIS A CB 1 ATOM 3755 C CG . HIS A 1 491 ? 14.211 39.302 47.817 1.00 27.47 ? 487 HIS A CG 1 ATOM 3756 N ND1 . HIS A 1 491 ? 14.939 40.426 48.126 1.00 31.25 ? 487 HIS A ND1 1 ATOM 3757 C CD2 . HIS A 1 491 ? 12.968 39.504 48.325 1.00 28.17 ? 487 HIS A CD2 1 ATOM 3758 C CE1 . HIS A 1 491 ? 14.154 41.294 48.755 1.00 31.32 ? 487 HIS A CE1 1 ATOM 3759 N NE2 . HIS A 1 491 ? 12.962 40.745 48.912 1.00 29.89 ? 487 HIS A NE2 1 ATOM 3760 N N . PRO A 1 492 ? 14.397 36.014 44.866 1.00 20.62 ? 488 PRO A N 1 ATOM 3761 C CA . PRO A 1 492 ? 14.870 34.888 44.002 1.00 20.40 ? 488 PRO A CA 1 ATOM 3762 C C . PRO A 1 492 ? 16.382 34.764 44.121 1.00 22.28 ? 488 PRO A C 1 ATOM 3763 O O . PRO A 1 492 ? 17.050 35.805 44.274 1.00 20.82 ? 488 PRO A O 1 ATOM 3764 C CB . PRO A 1 492 ? 14.536 35.354 42.579 1.00 20.87 ? 488 PRO A CB 1 ATOM 3765 C CG . PRO A 1 492 ? 13.224 36.223 42.779 1.00 20.71 ? 488 PRO A CG 1 ATOM 3766 C CD . PRO A 1 492 ? 13.570 37.001 44.118 1.00 21.18 ? 488 PRO A CD 1 ATOM 3767 N N . TYR A 1 493 ? 16.920 33.543 44.006 1.00 20.75 ? 489 TYR A N 1 ATOM 3768 C CA . TYR A 1 493 ? 18.387 33.366 43.997 1.00 23.51 ? 489 TYR A CA 1 ATOM 3769 C C . TYR A 1 493 ? 18.701 32.007 43.360 1.00 24.27 ? 489 TYR A C 1 ATOM 3770 O O . TYR A 1 493 ? 17.795 31.153 43.219 1.00 23.23 ? 489 TYR A O 1 ATOM 3771 C CB . TYR A 1 493 ? 18.926 33.384 45.458 1.00 23.01 ? 489 TYR A CB 1 ATOM 3772 C CG . TYR A 1 493 ? 18.181 32.365 46.355 1.00 23.90 ? 489 TYR A CG 1 ATOM 3773 C CD1 . TYR A 1 493 ? 18.504 30.999 46.310 1.00 24.59 ? 489 TYR A CD1 1 ATOM 3774 C CD2 . TYR A 1 493 ? 17.132 32.778 47.211 1.00 21.76 ? 489 TYR A CD2 1 ATOM 3775 C CE1 . TYR A 1 493 ? 17.827 30.074 47.153 1.00 23.12 ? 489 TYR A CE1 1 ATOM 3776 C CE2 . TYR A 1 493 ? 16.439 31.873 48.006 1.00 23.12 ? 489 TYR A CE2 1 ATOM 3777 C CZ . TYR A 1 493 ? 16.779 30.525 47.964 1.00 22.67 ? 489 TYR A CZ 1 ATOM 3778 O OH . TYR A 1 493 ? 16.108 29.591 48.760 1.00 23.58 ? 489 TYR A OH 1 ATOM 3779 N N . THR A 1 494 ? 19.960 31.792 42.963 1.00 26.41 ? 490 THR A N 1 ATOM 3780 C CA . THR A 1 494 ? 20.463 30.442 42.812 1.00 29.93 ? 490 THR A CA 1 ATOM 3781 C C . THR A 1 494 ? 21.910 30.386 43.233 1.00 30.52 ? 490 THR A C 1 ATOM 3782 O O . THR A 1 494 ? 22.572 31.412 43.408 1.00 31.35 ? 490 THR A O 1 ATOM 3783 C CB . THR A 1 494 ? 20.794 29.914 41.420 1.00 32.72 ? 490 THR A CB 1 ATOM 3784 O OG1 . THR A 1 494 ? 20.617 30.882 40.388 1.00 37.79 ? 490 THR A OG1 1 ATOM 3785 C CG2 . THR A 1 494 ? 20.229 28.553 41.182 1.00 31.56 ? 490 THR A CG2 1 ATOM 3786 N N . GLU A 1 495 ? 22.379 29.153 43.279 1.00 31.46 ? 491 GLU A N 1 ATOM 3787 C CA . GLU A 1 495 ? 23.774 28.767 43.480 1.00 32.93 ? 491 GLU A CA 1 ATOM 3788 C C . GLU A 1 495 ? 24.327 29.556 44.629 1.00 32.97 ? 491 GLU A C 1 ATOM 3789 O O . GLU A 1 495 ? 23.626 29.739 45.626 1.00 31.60 ? 491 GLU A O 1 ATOM 3790 C CB . GLU A 1 495 ? 24.564 28.993 42.185 1.00 34.04 ? 491 GLU A CB 1 ATOM 3791 C CG . GLU A 1 495 ? 24.049 28.195 41.054 1.00 38.67 ? 491 GLU A CG 1 ATOM 3792 C CD . GLU A 1 495 ? 24.137 28.938 39.760 1.00 45.97 ? 491 GLU A CD 1 ATOM 3793 O OE1 . GLU A 1 495 ? 23.544 28.445 38.771 1.00 49.86 ? 491 GLU A OE1 1 ATOM 3794 O OE2 . GLU A 1 495 ? 24.808 29.999 39.721 1.00 47.22 ? 491 GLU A OE2 1 ATOM 3795 N N . THR A 1 496 ? 25.553 30.071 44.494 1.00 31.87 ? 492 THR A N 1 ATOM 3796 C CA . THR A 1 496 ? 26.265 30.630 45.638 1.00 32.44 ? 492 THR A CA 1 ATOM 3797 C C . THR A 1 496 ? 25.590 31.871 46.230 1.00 32.68 ? 492 THR A C 1 ATOM 3798 O O . THR A 1 496 ? 25.601 32.094 47.475 1.00 31.41 ? 492 THR A O 1 ATOM 3799 C CB . THR A 1 496 ? 27.739 30.866 45.284 1.00 33.73 ? 492 THR A CB 1 ATOM 3800 O OG1 . THR A 1 496 ? 28.267 29.670 44.670 1.00 33.79 ? 492 THR A OG1 1 ATOM 3801 C CG2 . THR A 1 496 ? 28.556 31.192 46.555 1.00 34.45 ? 492 THR A CG2 1 ATOM 3802 N N . LYS A 1 497 ? 24.949 32.665 45.369 1.00 32.15 ? 493 LYS A N 1 ATOM 3803 C CA . LYS A 1 497 ? 24.226 33.836 45.874 1.00 32.37 ? 493 LYS A CA 1 ATOM 3804 C C . LYS A 1 497 ? 23.129 33.426 46.853 1.00 31.19 ? 493 LYS A C 1 ATOM 3805 O O . LYS A 1 497 ? 22.770 34.192 47.737 1.00 32.19 ? 493 LYS A O 1 ATOM 3806 C CB . LYS A 1 497 ? 23.680 34.722 44.731 1.00 33.49 ? 493 LYS A CB 1 ATOM 3807 C CG . LYS A 1 497 ? 24.826 35.514 44.049 1.00 39.16 ? 493 LYS A CG 1 ATOM 3808 C CD . LYS A 1 497 ? 24.391 36.399 42.851 1.00 46.26 ? 493 LYS A CD 1 ATOM 3809 C CE . LYS A 1 497 ? 25.650 36.893 42.103 1.00 49.94 ? 493 LYS A CE 1 ATOM 3810 N NZ . LYS A 1 497 ? 25.326 37.594 40.807 1.00 54.80 ? 493 LYS A NZ 1 ATOM 3811 N N . GLY A 1 498 ? 22.637 32.203 46.733 1.00 28.57 ? 494 GLY A N 1 ATOM 3812 C CA . GLY A 1 498 ? 21.541 31.774 47.630 1.00 28.79 ? 494 GLY A CA 1 ATOM 3813 C C . GLY A 1 498 ? 22.034 31.088 48.904 1.00 28.61 ? 494 GLY A C 1 ATOM 3814 O O . GLY A 1 498 ? 21.236 30.792 49.805 1.00 28.08 ? 494 GLY A O 1 ATOM 3815 N N . ASP A 1 499 ? 23.333 30.788 48.970 1.00 27.29 ? 495 ASP A N 1 ATOM 3816 C CA . ASP A 1 499 ? 23.877 30.168 50.196 1.00 27.95 ? 495 ASP A CA 1 ATOM 3817 C C . ASP A 1 499 ? 23.591 31.203 51.289 1.00 28.80 ? 495 ASP A C 1 ATOM 3818 O O . ASP A 1 499 ? 23.857 32.412 51.103 1.00 29.03 ? 495 ASP A O 1 ATOM 3819 C CB . ASP A 1 499 ? 25.393 29.961 50.116 1.00 27.51 ? 495 ASP A CB 1 ATOM 3820 C CG . ASP A 1 499 ? 25.804 28.823 49.164 1.00 28.16 ? 495 ASP A CG 1 ATOM 3821 O OD1 . ASP A 1 499 ? 24.912 28.100 48.638 1.00 27.54 ? 495 ASP A OD1 1 ATOM 3822 O OD2 . ASP A 1 499 ? 27.040 28.610 48.971 1.00 29.25 ? 495 ASP A OD2 1 ATOM 3823 N N . ASN A 1 500 ? 23.068 30.753 52.420 1.00 28.36 ? 496 ASN A N 1 ATOM 3824 C CA . ASN A 1 500 ? 22.581 31.707 53.419 1.00 29.89 ? 496 ASN A CA 1 ATOM 3825 C C . ASN A 1 500 ? 22.651 31.030 54.785 1.00 29.72 ? 496 ASN A C 1 ATOM 3826 O O . ASN A 1 500 ? 21.961 30.050 55.034 1.00 29.02 ? 496 ASN A O 1 ATOM 3827 C CB . ASN A 1 500 ? 21.133 32.071 53.025 1.00 28.26 ? 496 ASN A CB 1 ATOM 3828 C CG . ASN A 1 500 ? 20.472 33.077 53.949 1.00 30.65 ? 496 ASN A CG 1 ATOM 3829 O OD1 . ASN A 1 500 ? 20.744 33.155 55.140 1.00 28.91 ? 496 ASN A OD1 1 ATOM 3830 N ND2 . ASN A 1 500 ? 19.517 33.811 53.390 1.00 26.85 ? 496 ASN A ND2 1 ATOM 3831 N N . LEU A 1 501 ? 23.467 31.588 55.682 1.00 30.46 ? 497 LEU A N 1 ATOM 3832 C CA . LEU A 1 501 ? 23.699 31.001 57.004 1.00 30.78 ? 497 LEU A CA 1 ATOM 3833 C C . LEU A 1 501 ? 22.637 31.365 58.062 1.00 31.36 ? 497 LEU A C 1 ATOM 3834 O O . LEU A 1 501 ? 22.604 30.715 59.106 1.00 31.35 ? 497 LEU A O 1 ATOM 3835 C CB . LEU A 1 501 ? 25.119 31.351 57.535 1.00 31.13 ? 497 LEU A CB 1 ATOM 3836 C CG . LEU A 1 501 ? 26.370 30.881 56.752 1.00 34.36 ? 497 LEU A CG 1 ATOM 3837 C CD1 . LEU A 1 501 ? 27.718 31.432 57.392 1.00 37.10 ? 497 LEU A CD1 1 ATOM 3838 C CD2 . LEU A 1 501 ? 26.399 29.358 56.614 1.00 32.73 ? 497 LEU A CD2 1 ATOM 3839 N N . ASN A 1 502 ? 21.810 32.382 57.822 1.00 30.81 ? 498 ASN A N 1 ATOM 3840 C CA . ASN A 1 502 ? 20.818 32.796 58.826 1.00 32.30 ? 498 ASN A CA 1 ATOM 3841 C C . ASN A 1 502 ? 19.377 32.435 58.514 1.00 31.20 ? 498 ASN A C 1 ATOM 3842 O O . ASN A 1 502 ? 18.541 32.382 59.427 1.00 31.90 ? 498 ASN A O 1 ATOM 3843 C CB . ASN A 1 502 ? 20.896 34.298 59.077 1.00 34.65 ? 498 ASN A CB 1 ATOM 3844 C CG . ASN A 1 502 ? 20.578 35.110 57.841 1.00 43.20 ? 498 ASN A CG 1 ATOM 3845 O OD1 . ASN A 1 502 ? 19.395 35.325 57.489 1.00 49.58 ? 498 ASN A OD1 1 ATOM 3846 N ND2 . ASN A 1 502 ? 21.630 35.571 57.159 1.00 51.96 ? 498 ASN A ND2 1 ATOM 3847 N N . LEU A 1 503 ? 19.064 32.264 57.231 1.00 29.34 ? 499 LEU A N 1 ATOM 3848 C CA . LEU A 1 503 ? 17.717 31.803 56.796 1.00 28.91 ? 499 LEU A CA 1 ATOM 3849 C C . LEU A 1 503 ? 16.551 32.563 57.431 1.00 28.98 ? 499 LEU A C 1 ATOM 3850 O O . LEU A 1 503 ? 15.597 31.922 57.883 1.00 29.18 ? 499 LEU A O 1 ATOM 3851 C CB . LEU A 1 503 ? 17.547 30.282 57.066 1.00 27.48 ? 499 LEU A CB 1 ATOM 3852 C CG . LEU A 1 503 ? 18.578 29.382 56.346 1.00 27.36 ? 499 LEU A CG 1 ATOM 3853 C CD1 . LEU A 1 503 ? 18.333 27.869 56.559 1.00 27.26 ? 499 LEU A CD1 1 ATOM 3854 C CD2 . LEU A 1 503 ? 18.590 29.712 54.818 1.00 29.00 ? 499 LEU A CD2 1 ATOM 3855 N N . THR A 1 504 ? 16.667 33.889 57.519 1.00 28.16 ? 500 THR A N 1 ATOM 3856 C CA . THR A 1 504 ? 15.590 34.727 57.997 1.00 30.44 ? 500 THR A CA 1 ATOM 3857 C C . THR A 1 504 ? 15.146 35.577 56.809 1.00 29.98 ? 500 THR A C 1 ATOM 3858 O O . THR A 1 504 ? 15.968 36.048 56.003 1.00 29.89 ? 500 THR A O 1 ATOM 3859 C CB . THR A 1 504 ? 16.032 35.655 59.155 1.00 31.63 ? 500 THR A CB 1 ATOM 3860 O OG1 . THR A 1 504 ? 16.900 36.624 58.588 1.00 39.02 ? 500 THR A OG1 1 ATOM 3861 C CG2 . THR A 1 504 ? 16.783 34.840 60.214 1.00 26.76 ? 500 THR A CG2 1 ATOM 3862 N N . ILE A 1 505 ? 13.851 35.728 56.636 1.00 29.16 ? 501 ILE A N 1 ATOM 3863 C CA . ILE A 1 505 ? 13.393 36.379 55.401 1.00 29.95 ? 501 ILE A CA 1 ATOM 3864 C C . ILE A 1 505 ? 13.690 37.882 55.464 1.00 32.10 ? 501 ILE A C 1 ATOM 3865 O O . ILE A 1 505 ? 13.722 38.448 56.566 1.00 30.56 ? 501 ILE A O 1 ATOM 3866 C CB . ILE A 1 505 ? 11.915 36.127 55.097 1.00 29.70 ? 501 ILE A CB 1 ATOM 3867 C CG1 . ILE A 1 505 ? 11.006 36.723 56.181 1.00 28.51 ? 501 ILE A CG1 1 ATOM 3868 C CG2 . ILE A 1 505 ? 11.670 34.615 54.873 1.00 29.24 ? 501 ILE A CG2 1 ATOM 3869 C CD1 . ILE A 1 505 ? 9.491 36.703 55.765 1.00 30.16 ? 501 ILE A CD1 1 ATOM 3870 N N . PRO A 1 506 ? 13.882 38.530 54.285 1.00 33.25 ? 502 PRO A N 1 ATOM 3871 C CA . PRO A 1 506 ? 14.117 39.982 54.280 1.00 34.74 ? 502 PRO A CA 1 ATOM 3872 C C . PRO A 1 506 ? 12.941 40.758 54.817 1.00 35.78 ? 502 PRO A C 1 ATOM 3873 O O . PRO A 1 506 ? 11.776 40.354 54.641 1.00 33.75 ? 502 PRO A O 1 ATOM 3874 C CB . PRO A 1 506 ? 14.302 40.354 52.787 1.00 35.50 ? 502 PRO A CB 1 ATOM 3875 C CG . PRO A 1 506 ? 13.912 39.124 51.978 1.00 35.99 ? 502 PRO A CG 1 ATOM 3876 C CD . PRO A 1 506 ? 13.819 37.930 52.929 1.00 33.77 ? 502 PRO A CD 1 ATOM 3877 N N . GLU A 1 507 ? 13.252 41.894 55.424 1.00 36.34 ? 503 GLU A N 1 ATOM 3878 C CA . GLU A 1 507 ? 12.232 42.857 55.784 1.00 38.09 ? 503 GLU A CA 1 ATOM 3879 C C . GLU A 1 507 ? 11.977 43.804 54.621 1.00 38.73 ? 503 GLU A C 1 ATOM 3880 O O . GLU A 1 507 ? 12.871 44.001 53.773 1.00 40.89 ? 503 GLU A O 1 ATOM 3881 C CB . GLU A 1 507 ? 12.614 43.565 57.086 1.00 38.92 ? 503 GLU A CB 1 ATOM 3882 C CG . GLU A 1 507 ? 12.505 42.536 58.248 1.00 39.40 ? 503 GLU A CG 1 ATOM 3883 C CD . GLU A 1 507 ? 11.093 41.861 58.269 1.00 40.43 ? 503 GLU A CD 1 ATOM 3884 O OE1 . GLU A 1 507 ? 10.163 42.655 58.561 1.00 30.97 ? 503 GLU A OE1 1 ATOM 3885 O OE2 . GLU A 1 507 ? 10.930 40.587 57.960 1.00 38.64 ? 503 GLU A OE2 1 ATOM 3886 N N . PRO A 1 508 ? 10.752 44.353 54.516 1.00 37.40 ? 504 PRO A N 1 ATOM 3887 C CA . PRO A 1 508 ? 9.669 44.149 55.423 1.00 36.43 ? 504 PRO A CA 1 ATOM 3888 C C . PRO A 1 508 ? 8.984 42.827 54.962 1.00 35.35 ? 504 PRO A C 1 ATOM 3889 O O . PRO A 1 508 ? 8.752 42.570 53.741 1.00 37.45 ? 504 PRO A O 1 ATOM 3890 C CB . PRO A 1 508 ? 8.808 45.396 55.205 1.00 36.79 ? 504 PRO A CB 1 ATOM 3891 C CG . PRO A 1 508 ? 8.863 45.565 53.710 1.00 37.45 ? 504 PRO A CG 1 ATOM 3892 C CD . PRO A 1 508 ? 10.370 45.255 53.418 1.00 38.48 ? 504 PRO A CD 1 ATOM 3893 N N . GLY A 1 509 ? 8.747 41.957 55.906 1.00 31.95 ? 505 GLY A N 1 ATOM 3894 C CA . GLY A 1 509 ? 8.061 40.713 55.630 1.00 28.45 ? 505 GLY A CA 1 ATOM 3895 C C . GLY A 1 509 ? 7.310 40.431 56.919 1.00 27.79 ? 505 GLY A C 1 ATOM 3896 O O . GLY A 1 509 ? 6.090 40.589 56.995 1.00 24.35 ? 505 GLY A O 1 ATOM 3897 N N . LEU A 1 510 ? 8.077 40.116 57.964 1.00 25.67 ? 506 LEU A N 1 ATOM 3898 C CA . LEU A 1 510 ? 7.516 39.928 59.301 1.00 25.97 ? 506 LEU A CA 1 ATOM 3899 C C . LEU A 1 510 ? 6.789 41.154 59.805 1.00 26.35 ? 506 LEU A C 1 ATOM 3900 O O . LEU A 1 510 ? 5.698 41.051 60.382 1.00 26.38 ? 506 LEU A O 1 ATOM 3901 C CB . LEU A 1 510 ? 8.642 39.536 60.293 1.00 26.06 ? 506 LEU A CB 1 ATOM 3902 C CG . LEU A 1 510 ? 8.203 39.359 61.752 1.00 26.99 ? 506 LEU A CG 1 ATOM 3903 C CD1 . LEU A 1 510 ? 7.180 38.186 61.902 1.00 24.59 ? 506 LEU A CD1 1 ATOM 3904 C CD2 . LEU A 1 510 ? 9.443 39.180 62.782 1.00 28.89 ? 506 LEU A CD2 1 ATOM 3905 N N . SER A 1 511 ? 7.362 42.342 59.633 1.00 26.02 ? 507 SER A N 1 ATOM 3906 C CA . SER A 1 511 ? 6.639 43.519 60.146 1.00 27.11 ? 507 SER A CA 1 ATOM 3907 C C . SER A 1 511 ? 5.284 43.750 59.448 1.00 26.96 ? 507 SER A C 1 ATOM 3908 O O . SER A 1 511 ? 4.321 44.161 60.076 1.00 25.31 ? 507 SER A O 1 ATOM 3909 C CB . SER A 1 511 ? 7.478 44.783 60.035 1.00 29.65 ? 507 SER A CB 1 ATOM 3910 O OG . SER A 1 511 ? 7.749 44.962 58.654 1.00 32.77 ? 507 SER A OG 1 ATOM 3911 N N . THR A 1 512 ? 5.194 43.471 58.157 1.00 25.05 ? 508 THR A N 1 ATOM 3912 C CA . THR A 1 512 ? 3.898 43.557 57.465 1.00 24.12 ? 508 THR A CA 1 ATOM 3913 C C . THR A 1 512 ? 2.892 42.467 57.970 1.00 23.92 ? 508 THR A C 1 ATOM 3914 O O . THR A 1 512 ? 1.733 42.768 58.201 1.00 23.52 ? 508 THR A O 1 ATOM 3915 C CB . THR A 1 512 ? 4.127 43.444 55.962 1.00 25.39 ? 508 THR A CB 1 ATOM 3916 O OG1 . THR A 1 512 ? 4.895 44.605 55.563 1.00 29.49 ? 508 THR A OG1 1 ATOM 3917 C CG2 . THR A 1 512 ? 2.774 43.433 55.149 1.00 21.39 ? 508 THR A CG2 1 ATOM 3918 N N . VAL A 1 513 ? 3.357 41.226 58.171 1.00 22.98 ? 509 VAL A N 1 ATOM 3919 C CA . VAL A 1 513 ? 2.486 40.173 58.714 1.00 22.72 ? 509 VAL A CA 1 ATOM 3920 C C . VAL A 1 513 ? 1.966 40.661 60.099 1.00 23.70 ? 509 VAL A C 1 ATOM 3921 O O . VAL A 1 513 ? 0.796 40.502 60.406 1.00 23.98 ? 509 VAL A O 1 ATOM 3922 C CB . VAL A 1 513 ? 3.273 38.843 58.818 1.00 23.29 ? 509 VAL A CB 1 ATOM 3923 C CG1 . VAL A 1 513 ? 2.521 37.811 59.676 1.00 22.92 ? 509 VAL A CG1 1 ATOM 3924 C CG2 . VAL A 1 513 ? 3.598 38.293 57.341 1.00 20.36 ? 509 VAL A CG2 1 ATOM 3925 N N . GLN A 1 514 ? 2.868 41.172 60.946 1.00 24.03 ? 510 GLN A N 1 ATOM 3926 C CA . GLN A 1 514 ? 2.461 41.613 62.287 1.00 24.23 ? 510 GLN A CA 1 ATOM 3927 C C . GLN A 1 514 ? 1.454 42.732 62.234 1.00 24.75 ? 510 GLN A C 1 ATOM 3928 O O . GLN A 1 514 ? 0.464 42.748 62.986 1.00 25.57 ? 510 GLN A O 1 ATOM 3929 C CB . GLN A 1 514 ? 3.700 42.023 63.085 1.00 25.51 ? 510 GLN A CB 1 ATOM 3930 C CG . GLN A 1 514 ? 4.541 40.773 63.494 1.00 24.36 ? 510 GLN A CG 1 ATOM 3931 C CD . GLN A 1 514 ? 5.843 41.168 64.089 1.00 29.87 ? 510 GLN A CD 1 ATOM 3932 O OE1 . GLN A 1 514 ? 6.366 42.221 63.780 1.00 30.63 ? 510 GLN A OE1 1 ATOM 3933 N NE2 . GLN A 1 514 ? 6.413 40.294 64.895 1.00 29.82 ? 510 GLN A NE2 1 ATOM 3934 N N . ALA A 1 515 ? 1.655 43.668 61.317 1.00 24.82 ? 511 ALA A N 1 ATOM 3935 C CA . ALA A 1 515 ? 0.703 44.812 61.200 1.00 26.03 ? 511 ALA A CA 1 ATOM 3936 C C . ALA A 1 515 ? -0.664 44.391 60.650 1.00 26.54 ? 511 ALA A C 1 ATOM 3937 O O . ALA A 1 515 ? -1.740 44.831 61.132 1.00 25.78 ? 511 ALA A O 1 ATOM 3938 C CB . ALA A 1 515 ? 1.359 45.929 60.320 1.00 25.58 ? 511 ALA A CB 1 ATOM 3939 N N . VAL A 1 516 ? -0.653 43.513 59.654 1.00 25.15 ? 512 VAL A N 1 ATOM 3940 C CA . VAL A 1 516 ? -1.892 42.953 59.119 1.00 24.41 ? 512 VAL A CA 1 ATOM 3941 C C . VAL A 1 516 ? -2.642 42.053 60.106 1.00 25.05 ? 512 VAL A C 1 ATOM 3942 O O . VAL A 1 516 ? -3.850 42.301 60.417 1.00 25.25 ? 512 VAL A O 1 ATOM 3943 C CB . VAL A 1 516 ? -1.635 42.231 57.755 1.00 24.94 ? 512 VAL A CB 1 ATOM 3944 C CG1 . VAL A 1 516 ? -2.897 41.542 57.235 1.00 24.98 ? 512 VAL A CG1 1 ATOM 3945 C CG2 . VAL A 1 516 ? -1.068 43.257 56.715 1.00 25.01 ? 512 VAL A CG2 1 ATOM 3946 N N . CYS A 1 517 ? -1.972 41.017 60.615 1.00 24.12 ? 513 CYS A N 1 ATOM 3947 C CA . CYS A 1 517 ? -2.644 40.048 61.486 1.00 24.14 ? 513 CYS A CA 1 ATOM 3948 C C . CYS A 1 517 ? -3.087 40.703 62.825 1.00 24.86 ? 513 CYS A C 1 ATOM 3949 O O . CYS A 1 517 ? -3.997 40.207 63.511 1.00 24.11 ? 513 CYS A O 1 ATOM 3950 C CB . CYS A 1 517 ? -1.717 38.899 61.784 1.00 24.84 ? 513 CYS A CB 1 ATOM 3951 S SG . CYS A 1 517 ? -1.177 38.099 60.202 1.00 27.91 ? 513 CYS A SG 1 ATOM 3952 N N . GLY A 1 518 ? -2.400 41.754 63.208 1.00 26.38 ? 514 GLY A N 1 ATOM 3953 C CA . GLY A 1 518 ? -2.741 42.467 64.473 1.00 29.02 ? 514 GLY A CA 1 ATOM 3954 C C . GLY A 1 518 ? -4.093 43.152 64.321 1.00 29.52 ? 514 GLY A C 1 ATOM 3955 O O . GLY A 1 518 ? -4.748 43.457 65.323 1.00 30.96 ? 514 GLY A O 1 ATOM 3956 N N . GLY A 1 519 ? -4.496 43.434 63.081 1.00 28.08 ? 515 GLY A N 1 ATOM 3957 C CA . GLY A 1 519 ? -5.739 44.154 62.833 1.00 27.75 ? 515 GLY A CA 1 ATOM 3958 C C . GLY A 1 519 ? -6.937 43.340 62.347 1.00 27.09 ? 515 GLY A C 1 ATOM 3959 O O . GLY A 1 519 ? -8.079 43.752 62.523 1.00 24.31 ? 515 GLY A O 1 ATOM 3960 N N . VAL A 1 520 ? -6.684 42.204 61.706 1.00 25.16 ? 516 VAL A N 1 ATOM 3961 C CA . VAL A 1 520 ? -7.766 41.403 61.126 1.00 25.63 ? 516 VAL A CA 1 ATOM 3962 C C . VAL A 1 520 ? -7.292 39.978 60.999 1.00 26.16 ? 516 VAL A C 1 ATOM 3963 O O . VAL A 1 520 ? -6.055 39.763 60.980 1.00 26.67 ? 516 VAL A O 1 ATOM 3964 C CB . VAL A 1 520 ? -8.217 42.028 59.735 1.00 26.43 ? 516 VAL A CB 1 ATOM 3965 C CG1 . VAL A 1 520 ? -7.171 41.790 58.650 1.00 25.65 ? 516 VAL A CG1 1 ATOM 3966 C CG2 . VAL A 1 520 ? -9.517 41.371 59.269 1.00 28.88 ? 516 VAL A CG2 1 ATOM 3967 N N . ARG A 1 521 ? -8.199 38.979 61.012 1.00 25.28 ? 517 ARG A N 1 ATOM 3968 C CA . ARG A 1 521 ? -7.763 37.584 60.820 1.00 25.43 ? 517 ARG A CA 1 ATOM 3969 C C . ARG A 1 521 ? -6.991 37.465 59.494 1.00 25.30 ? 517 ARG A C 1 ATOM 3970 O O . ARG A 1 521 ? -7.352 38.103 58.501 1.00 23.34 ? 517 ARG A O 1 ATOM 3971 C CB . ARG A 1 521 ? -8.929 36.573 60.882 1.00 25.11 ? 517 ARG A CB 1 ATOM 3972 C CG A ARG A 1 521 ? -9.382 36.356 62.246 0.40 23.64 ? 517 ARG A CG 1 ATOM 3973 C CG B ARG A 1 521 ? -10.158 36.797 59.841 0.60 25.87 ? 517 ARG A CG 1 ATOM 3974 C CD A ARG A 1 521 ? -10.353 35.244 62.345 0.40 23.34 ? 517 ARG A CD 1 ATOM 3975 C CD B ARG A 1 521 ? -11.625 36.210 60.305 0.60 22.22 ? 517 ARG A CD 1 ATOM 3976 N NE A ARG A 1 521 ? -9.727 33.959 62.651 0.40 23.84 ? 517 ARG A NE 1 ATOM 3977 N NE B ARG A 1 521 ? -12.561 36.144 59.145 0.60 23.91 ? 517 ARG A NE 1 ATOM 3978 C CZ A ARG A 1 521 ? -10.338 32.808 62.377 0.40 21.49 ? 517 ARG A CZ 1 ATOM 3979 C CZ B ARG A 1 521 ? -12.959 34.997 58.577 0.60 27.98 ? 517 ARG A CZ 1 ATOM 3980 N NH1 A ARG A 1 521 ? -11.555 32.849 61.743 0.40 8.54 ? 517 ARG A NH1 1 ATOM 3981 N NH1 B ARG A 1 521 ? -12.587 33.858 59.127 0.60 31.51 ? 517 ARG A NH1 1 ATOM 3982 N NH2 A ARG A 1 521 ? -9.706 31.665 62.668 0.40 17.43 ? 517 ARG A NH2 1 ATOM 3983 N NH2 B ARG A 1 521 ? -13.780 34.952 57.507 0.60 27.38 ? 517 ARG A NH2 1 ATOM 3984 N N . CYS A 1 522 ? -5.912 36.694 59.508 1.00 26.19 ? 518 CYS A N 1 ATOM 3985 C CA . CYS A 1 522 ? -4.989 36.669 58.341 1.00 26.98 ? 518 CYS A CA 1 ATOM 3986 C C . CYS A 1 522 ? -4.497 35.246 57.994 1.00 27.15 ? 518 CYS A C 1 ATOM 3987 O O . CYS A 1 522 ? -4.254 34.410 58.874 1.00 26.33 ? 518 CYS A O 1 ATOM 3988 C CB . CYS A 1 522 ? -3.747 37.527 58.618 1.00 27.06 ? 518 CYS A CB 1 ATOM 3989 S SG . CYS A 1 522 ? -2.657 36.787 59.921 1.00 30.87 ? 518 CYS A SG 1 ATOM 3990 N N . ALA A 1 523 ? -4.344 35.001 56.697 1.00 25.06 ? 519 ALA A N 1 ATOM 3991 C CA . ALA A 1 523 ? -3.693 33.807 56.189 1.00 24.60 ? 519 ALA A CA 1 ATOM 3992 C C . ALA A 1 523 ? -2.377 34.272 55.533 1.00 22.67 ? 519 ALA A C 1 ATOM 3993 O O . ALA A 1 523 ? -2.364 35.124 54.613 1.00 22.99 ? 519 ALA A O 1 ATOM 3994 C CB . ALA A 1 523 ? -4.650 33.146 55.093 1.00 24.64 ? 519 ALA A CB 1 ATOM 3995 N N . THR A 1 524 ? -1.273 33.814 56.086 1.00 22.82 ? 520 THR A N 1 ATOM 3996 C CA . THR A 1 524 ? 0.048 34.220 55.629 1.00 21.92 ? 520 THR A CA 1 ATOM 3997 C C . THR A 1 524 ? 0.528 33.171 54.636 1.00 21.64 ? 520 THR A C 1 ATOM 3998 O O . THR A 1 524 ? 0.512 31.955 54.937 1.00 22.34 ? 520 THR A O 1 ATOM 3999 C CB . THR A 1 524 ? 1.014 34.281 56.811 1.00 20.95 ? 520 THR A CB 1 ATOM 4000 O OG1 . THR A 1 524 ? 0.562 35.356 57.658 1.00 22.90 ? 520 THR A OG1 1 ATOM 4001 C CG2 . THR A 1 524 ? 2.491 34.599 56.328 1.00 20.81 ? 520 THR A CG2 1 ATOM 4002 N N . VAL A 1 525 ? 0.936 33.629 53.461 1.00 21.13 ? 521 VAL A N 1 ATOM 4003 C CA . VAL A 1 525 ? 1.439 32.716 52.436 1.00 21.19 ? 521 VAL A CA 1 ATOM 4004 C C . VAL A 1 525 ? 2.957 32.990 52.382 1.00 21.60 ? 521 VAL A C 1 ATOM 4005 O O . VAL A 1 525 ? 3.389 34.124 52.013 1.00 20.97 ? 521 VAL A O 1 ATOM 4006 C CB . VAL A 1 525 ? 0.779 33.005 51.069 1.00 20.09 ? 521 VAL A CB 1 ATOM 4007 C CG1 . VAL A 1 525 ? 1.414 32.142 49.972 1.00 22.25 ? 521 VAL A CG1 1 ATOM 4008 C CG2 . VAL A 1 525 ? -0.768 32.740 51.135 1.00 20.46 ? 521 VAL A CG2 1 ATOM 4009 N N . LEU A 1 526 ? 3.747 31.988 52.785 1.00 20.89 ? 522 LEU A N 1 ATOM 4010 C CA . LEU A 1 526 ? 5.183 32.167 52.852 1.00 20.79 ? 522 LEU A CA 1 ATOM 4011 C C . LEU A 1 526 ? 5.805 31.628 51.547 1.00 20.55 ? 522 LEU A C 1 ATOM 4012 O O . LEU A 1 526 ? 5.634 30.479 51.243 1.00 20.07 ? 522 LEU A O 1 ATOM 4013 C CB . LEU A 1 526 ? 5.744 31.355 54.029 1.00 21.98 ? 522 LEU A CB 1 ATOM 4014 C CG . LEU A 1 526 ? 7.267 31.322 54.141 1.00 22.75 ? 522 LEU A CG 1 ATOM 4015 C CD1 . LEU A 1 526 ? 7.916 32.697 54.213 1.00 22.50 ? 522 LEU A CD1 1 ATOM 4016 C CD2 . LEU A 1 526 ? 7.698 30.480 55.393 1.00 24.46 ? 522 LEU A CD2 1 ATOM 4017 N N . ILE A 1 527 ? 6.473 32.475 50.786 1.00 21.80 ? 523 ILE A N 1 ATOM 4018 C CA . ILE A 1 527 ? 7.114 32.048 49.520 1.00 21.97 ? 523 ILE A CA 1 ATOM 4019 C C . ILE A 1 527 ? 8.601 31.859 49.840 1.00 23.23 ? 523 ILE A C 1 ATOM 4020 O O . ILE A 1 527 ? 9.279 32.829 50.269 1.00 24.21 ? 523 ILE A O 1 ATOM 4021 C CB . ILE A 1 527 ? 6.953 33.173 48.481 1.00 21.92 ? 523 ILE A CB 1 ATOM 4022 C CG1 . ILE A 1 527 ? 5.460 33.328 48.153 1.00 24.06 ? 523 ILE A CG1 1 ATOM 4023 C CG2 . ILE A 1 527 ? 7.795 32.959 47.210 1.00 21.49 ? 523 ILE A CG2 1 ATOM 4024 C CD1 . ILE A 1 527 ? 4.822 32.162 47.278 1.00 24.40 ? 523 ILE A CD1 1 ATOM 4025 N N . SER A 1 528 ? 9.122 30.647 49.660 1.00 22.37 ? 524 SER A N 1 ATOM 4026 C CA . SER A 1 528 ? 10.566 30.436 49.975 1.00 23.09 ? 524 SER A CA 1 ATOM 4027 C C . SER A 1 528 ? 11.091 29.222 49.213 1.00 22.79 ? 524 SER A C 1 ATOM 4028 O O . SER A 1 528 ? 10.292 28.391 48.737 1.00 22.74 ? 524 SER A O 1 ATOM 4029 C CB . SER A 1 528 ? 10.759 30.178 51.502 1.00 23.13 ? 524 SER A CB 1 ATOM 4030 O OG . SER A 1 528 ? 10.138 28.928 51.813 1.00 23.17 ? 524 SER A OG 1 ATOM 4031 N N . GLY A 1 529 ? 12.427 29.099 49.124 1.00 22.50 ? 525 GLY A N 1 ATOM 4032 C CA . GLY A 1 529 ? 13.033 27.928 48.431 1.00 21.16 ? 525 GLY A CA 1 ATOM 4033 C C . GLY A 1 529 ? 13.299 26.751 49.379 1.00 21.41 ? 525 GLY A C 1 ATOM 4034 O O . GLY A 1 529 ? 13.838 25.720 48.988 1.00 21.49 ? 525 GLY A O 1 ATOM 4035 N N . ARG A 1 530 ? 12.866 26.895 50.636 1.00 21.40 ? 526 ARG A N 1 ATOM 4036 C CA . ARG A 1 530 ? 13.355 26.090 51.747 1.00 21.32 ? 526 ARG A CA 1 ATOM 4037 C C . ARG A 1 530 ? 12.721 26.558 53.054 1.00 22.50 ? 526 ARG A C 1 ATOM 4038 O O . ARG A 1 530 ? 12.165 27.686 53.154 1.00 24.00 ? 526 ARG A O 1 ATOM 4039 C CB . ARG A 1 530 ? 14.870 26.279 51.902 1.00 21.42 ? 526 ARG A CB 1 ATOM 4040 C CG . ARG A 1 530 ? 15.245 27.795 52.032 1.00 20.99 ? 526 ARG A CG 1 ATOM 4041 C CD . ARG A 1 530 ? 16.758 28.005 52.075 1.00 21.53 ? 526 ARG A CD 1 ATOM 4042 N NE . ARG A 1 530 ? 17.108 29.380 51.714 1.00 23.60 ? 526 ARG A NE 1 ATOM 4043 C CZ . ARG A 1 530 ? 18.316 29.775 51.285 1.00 23.79 ? 526 ARG A CZ 1 ATOM 4044 N NH1 . ARG A 1 530 ? 19.346 28.940 51.257 1.00 23.46 ? 526 ARG A NH1 1 ATOM 4045 N NH2 . ARG A 1 530 ? 18.506 31.046 50.959 1.00 23.74 ? 526 ARG A NH2 1 ATOM 4046 N N . PRO A 1 531 ? 12.840 25.726 54.095 1.00 24.39 ? 527 PRO A N 1 ATOM 4047 C CA . PRO A 1 531 ? 12.466 26.223 55.438 1.00 23.27 ? 527 PRO A CA 1 ATOM 4048 C C . PRO A 1 531 ? 13.326 27.420 55.801 1.00 23.48 ? 527 PRO A C 1 ATOM 4049 O O . PRO A 1 531 ? 14.558 27.453 55.508 1.00 22.52 ? 527 PRO A O 1 ATOM 4050 C CB . PRO A 1 531 ? 12.801 25.057 56.381 1.00 23.32 ? 527 PRO A CB 1 ATOM 4051 C CG . PRO A 1 531 ? 12.749 23.800 55.470 1.00 28.32 ? 527 PRO A CG 1 ATOM 4052 C CD . PRO A 1 531 ? 13.239 24.302 54.081 1.00 22.67 ? 527 PRO A CD 1 ATOM 4053 N N . VAL A 1 532 ? 12.675 28.380 56.455 1.00 22.86 ? 528 VAL A N 1 ATOM 4054 C CA . VAL A 1 532 ? 13.280 29.609 56.959 1.00 23.65 ? 528 VAL A CA 1 ATOM 4055 C C . VAL A 1 532 ? 12.739 29.796 58.387 1.00 24.68 ? 528 VAL A C 1 ATOM 4056 O O . VAL A 1 532 ? 11.734 29.180 58.774 1.00 25.73 ? 528 VAL A O 1 ATOM 4057 C CB . VAL A 1 532 ? 12.937 30.865 56.100 1.00 23.71 ? 528 VAL A CB 1 ATOM 4058 C CG1 . VAL A 1 532 ? 13.626 30.821 54.645 1.00 22.15 ? 528 VAL A CG1 1 ATOM 4059 C CG2 . VAL A 1 532 ? 11.350 31.096 55.976 1.00 24.54 ? 528 VAL A CG2 1 ATOM 4060 N N . VAL A 1 533 ? 13.421 30.604 59.180 1.00 24.83 ? 529 VAL A N 1 ATOM 4061 C CA . VAL A 1 533 ? 12.975 30.874 60.528 1.00 26.15 ? 529 VAL A CA 1 ATOM 4062 C C . VAL A 1 533 ? 11.514 31.322 60.475 1.00 26.23 ? 529 VAL A C 1 ATOM 4063 O O . VAL A 1 533 ? 11.192 32.295 59.817 1.00 27.06 ? 529 VAL A O 1 ATOM 4064 C CB . VAL A 1 533 ? 13.841 31.963 61.196 1.00 26.34 ? 529 VAL A CB 1 ATOM 4065 C CG1 . VAL A 1 533 ? 13.255 32.312 62.575 1.00 26.55 ? 529 VAL A CG1 1 ATOM 4066 C CG2 . VAL A 1 533 ? 15.341 31.468 61.345 1.00 26.84 ? 529 VAL A CG2 1 ATOM 4067 N N . VAL A 1 534 ? 10.645 30.633 61.209 1.00 26.40 ? 530 VAL A N 1 ATOM 4068 C CA . VAL A 1 534 ? 9.208 30.800 60.997 1.00 25.41 ? 530 VAL A CA 1 ATOM 4069 C C . VAL A 1 534 ? 8.420 31.005 62.283 1.00 26.03 ? 530 VAL A C 1 ATOM 4070 O O . VAL A 1 534 ? 7.260 31.389 62.227 1.00 23.84 ? 530 VAL A O 1 ATOM 4071 C CB . VAL A 1 534 ? 8.639 29.631 60.132 1.00 25.95 ? 530 VAL A CB 1 ATOM 4072 C CG1 . VAL A 1 534 ? 8.420 28.392 60.972 1.00 25.20 ? 530 VAL A CG1 1 ATOM 4073 C CG2 . VAL A 1 534 ? 7.331 30.077 59.383 1.00 25.44 ? 530 VAL A CG2 1 ATOM 4074 N N . GLN A 1 535 ? 9.049 30.822 63.448 1.00 24.20 ? 531 GLN A N 1 ATOM 4075 C CA . GLN A 1 535 ? 8.244 30.989 64.689 1.00 25.85 ? 531 GLN A CA 1 ATOM 4076 C C . GLN A 1 535 ? 7.617 32.384 64.794 1.00 25.02 ? 531 GLN A C 1 ATOM 4077 O O . GLN A 1 535 ? 6.418 32.513 65.169 1.00 25.89 ? 531 GLN A O 1 ATOM 4078 C CB . GLN A 1 535 ? 9.062 30.663 65.970 1.00 26.65 ? 531 GLN A CB 1 ATOM 4079 C CG . GLN A 1 535 ? 9.492 29.164 66.073 1.00 27.68 ? 531 GLN A CG 1 ATOM 4080 C CD . GLN A 1 535 ? 10.904 28.952 65.561 1.00 31.10 ? 531 GLN A CD 1 ATOM 4081 O OE1 . GLN A 1 535 ? 11.317 29.593 64.596 1.00 30.46 ? 531 GLN A OE1 1 ATOM 4082 N NE2 . GLN A 1 535 ? 11.673 28.040 66.223 1.00 29.36 ? 531 GLN A NE2 1 ATOM 4083 N N . PRO A 1 536 ? 8.385 33.443 64.468 1.00 26.18 ? 532 PRO A N 1 ATOM 4084 C CA . PRO A 1 536 ? 7.705 34.759 64.580 1.00 26.27 ? 532 PRO A CA 1 ATOM 4085 C C . PRO A 1 536 ? 6.510 34.953 63.606 1.00 25.82 ? 532 PRO A C 1 ATOM 4086 O O . PRO A 1 536 ? 5.452 35.497 64.011 1.00 25.26 ? 532 PRO A O 1 ATOM 4087 C CB . PRO A 1 536 ? 8.834 35.758 64.285 1.00 27.28 ? 532 PRO A CB 1 ATOM 4088 C CG . PRO A 1 536 ? 10.124 35.002 64.836 1.00 28.03 ? 532 PRO A CG 1 ATOM 4089 C CD . PRO A 1 536 ? 9.855 33.595 64.278 1.00 25.26 ? 532 PRO A CD 1 ATOM 4090 N N . LEU A 1 537 ? 6.639 34.508 62.357 1.00 24.21 ? 533 LEU A N 1 ATOM 4091 C CA . LEU A 1 537 ? 5.499 34.550 61.413 1.00 23.77 ? 533 LEU A CA 1 ATOM 4092 C C . LEU A 1 537 ? 4.326 33.708 61.921 1.00 24.32 ? 533 LEU A C 1 ATOM 4093 O O . LEU A 1 537 ? 3.144 34.124 61.820 1.00 24.63 ? 533 LEU A O 1 ATOM 4094 C CB . LEU A 1 537 ? 5.942 33.975 60.044 1.00 23.36 ? 533 LEU A CB 1 ATOM 4095 C CG . LEU A 1 537 ? 6.891 34.887 59.242 1.00 27.08 ? 533 LEU A CG 1 ATOM 4096 C CD1 . LEU A 1 537 ? 7.504 34.131 58.010 1.00 27.77 ? 533 LEU A CD1 1 ATOM 4097 C CD2 . LEU A 1 537 ? 6.102 36.163 58.804 1.00 23.33 ? 533 LEU A CD2 1 ATOM 4098 N N . LEU A 1 538 ? 4.631 32.511 62.435 1.00 24.40 ? 534 LEU A N 1 ATOM 4099 C CA . LEU A 1 538 ? 3.566 31.664 63.026 1.00 26.30 ? 534 LEU A CA 1 ATOM 4100 C C . LEU A 1 538 ? 2.808 32.348 64.183 1.00 26.39 ? 534 LEU A C 1 ATOM 4101 O O . LEU A 1 538 ? 1.569 32.284 64.258 1.00 27.06 ? 534 LEU A O 1 ATOM 4102 C CB . LEU A 1 538 ? 4.148 30.336 63.520 1.00 26.14 ? 534 LEU A CB 1 ATOM 4103 C CG . LEU A 1 538 ? 4.502 29.276 62.449 1.00 28.38 ? 534 LEU A CG 1 ATOM 4104 C CD1 . LEU A 1 538 ? 5.361 28.161 63.113 1.00 28.59 ? 534 LEU A CD1 1 ATOM 4105 C CD2 . LEU A 1 538 ? 3.262 28.655 61.739 1.00 28.01 ? 534 LEU A CD2 1 ATOM 4106 N N . ALA A 1 539 ? 3.560 32.986 65.076 1.00 27.10 ? 535 ALA A N 1 ATOM 4107 C CA . ALA A 1 539 ? 2.979 33.597 66.256 1.00 28.34 ? 535 ALA A CA 1 ATOM 4108 C C . ALA A 1 539 ? 1.983 34.670 65.875 1.00 28.28 ? 535 ALA A C 1 ATOM 4109 O O . ALA A 1 539 ? 1.005 34.856 66.595 1.00 28.45 ? 535 ALA A O 1 ATOM 4110 C CB . ALA A 1 539 ? 4.086 34.203 67.174 1.00 29.09 ? 535 ALA A CB 1 ATOM 4111 N N . ALA A 1 540 ? 2.255 35.430 64.797 1.00 25.71 ? 536 ALA A N 1 ATOM 4112 C CA . ALA A 1 540 ? 1.354 36.506 64.423 1.00 26.21 ? 536 ALA A CA 1 ATOM 4113 C C . ALA A 1 540 ? 0.095 36.019 63.696 1.00 24.64 ? 536 ALA A C 1 ATOM 4114 O O . ALA A 1 540 ? -0.900 36.742 63.677 1.00 23.76 ? 536 ALA A O 1 ATOM 4115 C CB . ALA A 1 540 ? 2.068 37.576 63.524 1.00 25.60 ? 536 ALA A CB 1 ATOM 4116 N N . SER A 1 541 ? 0.187 34.869 63.019 1.00 23.61 ? 537 SER A N 1 ATOM 4117 C CA . SER A 1 541 ? -0.770 34.482 61.963 1.00 23.56 ? 537 SER A CA 1 ATOM 4118 C C . SER A 1 541 ? -1.877 33.545 62.484 1.00 24.89 ? 537 SER A C 1 ATOM 4119 O O . SER A 1 541 ? -1.577 32.631 63.268 1.00 25.15 ? 537 SER A O 1 ATOM 4120 C CB . SER A 1 541 ? -0.021 33.698 60.842 1.00 23.37 ? 537 SER A CB 1 ATOM 4121 O OG . SER A 1 541 ? 0.967 34.523 60.215 1.00 23.94 ? 537 SER A OG 1 ATOM 4122 N N . ASP A 1 542 ? -3.105 33.717 62.003 1.00 24.00 ? 538 ASP A N 1 ATOM 4123 C CA . ASP A 1 542 ? -4.158 32.724 62.211 1.00 24.42 ? 538 ASP A CA 1 ATOM 4124 C C . ASP A 1 542 ? -3.890 31.468 61.397 1.00 24.50 ? 538 ASP A C 1 ATOM 4125 O O . ASP A 1 542 ? -3.950 30.357 61.951 1.00 24.31 ? 538 ASP A O 1 ATOM 4126 C CB . ASP A 1 542 ? -5.532 33.316 61.833 1.00 24.16 ? 538 ASP A CB 1 ATOM 4127 C CG . ASP A 1 542 ? -5.852 34.548 62.692 1.00 26.85 ? 538 ASP A CG 1 ATOM 4128 O OD1 . ASP A 1 542 ? -5.442 35.655 62.313 1.00 26.95 ? 538 ASP A OD1 1 ATOM 4129 O OD2 . ASP A 1 542 ? -6.467 34.379 63.771 1.00 24.04 ? 538 ASP A OD2 1 ATOM 4130 N N . ALA A 1 543 ? -3.598 31.623 60.085 1.00 22.87 ? 539 ALA A N 1 ATOM 4131 C CA . ALA A 1 543 ? -3.192 30.469 59.291 1.00 22.54 ? 539 ALA A CA 1 ATOM 4132 C C . ALA A 1 543 ? -1.879 30.803 58.590 1.00 22.75 ? 539 ALA A C 1 ATOM 4133 O O . ALA A 1 543 ? -1.605 31.961 58.320 1.00 21.07 ? 539 ALA A O 1 ATOM 4134 C CB . ALA A 1 543 ? -4.285 30.138 58.235 1.00 22.64 ? 539 ALA A CB 1 ATOM 4135 N N . LEU A 1 544 ? -1.087 29.776 58.299 1.00 22.94 ? 540 LEU A N 1 ATOM 4136 C CA . LEU A 1 544 ? 0.154 29.971 57.540 1.00 22.99 ? 540 LEU A CA 1 ATOM 4137 C C . LEU A 1 544 ? 0.403 28.796 56.609 1.00 23.45 ? 540 LEU A C 1 ATOM 4138 O O . LEU A 1 544 ? 0.352 27.619 57.019 1.00 24.21 ? 540 LEU A O 1 ATOM 4139 C CB . LEU A 1 544 ? 1.364 30.148 58.486 1.00 22.99 ? 540 LEU A CB 1 ATOM 4140 C CG . LEU A 1 544 ? 2.673 30.653 57.813 1.00 22.96 ? 540 LEU A CG 1 ATOM 4141 C CD1 . LEU A 1 544 ? 3.412 31.528 58.746 1.00 26.45 ? 540 LEU A CD1 1 ATOM 4142 C CD2 . LEU A 1 544 ? 3.598 29.440 57.434 1.00 23.44 ? 540 LEU A CD2 1 ATOM 4143 N N . VAL A 1 545 ? 0.777 29.129 55.370 1.00 23.29 ? 541 VAL A N 1 ATOM 4144 C CA . VAL A 1 545 ? 0.980 28.154 54.323 1.00 21.00 ? 541 VAL A CA 1 ATOM 4145 C C . VAL A 1 545 ? 2.405 28.290 53.812 1.00 22.34 ? 541 VAL A C 1 ATOM 4146 O O . VAL A 1 545 ? 2.827 29.417 53.478 1.00 21.58 ? 541 VAL A O 1 ATOM 4147 C CB . VAL A 1 545 ? -0.011 28.398 53.118 1.00 21.73 ? 541 VAL A CB 1 ATOM 4148 C CG1 . VAL A 1 545 ? 0.298 27.430 51.963 1.00 21.11 ? 541 VAL A CG1 1 ATOM 4149 C CG2 . VAL A 1 545 ? -1.491 28.264 53.531 1.00 21.69 ? 541 VAL A CG2 1 ATOM 4150 N N . ALA A 1 546 ? 3.132 27.157 53.725 1.00 21.43 ? 542 ALA A N 1 ATOM 4151 C CA . ALA A 1 546 ? 4.428 27.121 53.047 1.00 20.83 ? 542 ALA A CA 1 ATOM 4152 C C . ALA A 1 546 ? 4.129 26.828 51.582 1.00 20.21 ? 542 ALA A C 1 ATOM 4153 O O . ALA A 1 546 ? 3.716 25.685 51.229 1.00 21.69 ? 542 ALA A O 1 ATOM 4154 C CB . ALA A 1 546 ? 5.361 25.976 53.694 1.00 21.14 ? 542 ALA A CB 1 ATOM 4155 N N . ALA A 1 547 ? 4.242 27.854 50.732 1.00 20.23 ? 543 ALA A N 1 ATOM 4156 C CA . ALA A 1 547 ? 3.888 27.725 49.330 1.00 19.77 ? 543 ALA A CA 1 ATOM 4157 C C . ALA A 1 547 ? 5.128 27.482 48.458 1.00 20.52 ? 543 ALA A C 1 ATOM 4158 O O . ALA A 1 547 ? 4.985 27.316 47.252 1.00 20.74 ? 543 ALA A O 1 ATOM 4159 C CB . ALA A 1 547 ? 3.109 29.031 48.826 1.00 19.00 ? 543 ALA A CB 1 ATOM 4160 N N . TRP A 1 548 ? 6.331 27.444 49.069 1.00 20.18 ? 544 TRP A N 1 ATOM 4161 C CA . TRP A 1 548 ? 7.585 27.227 48.338 1.00 19.98 ? 544 TRP A CA 1 ATOM 4162 C C . TRP A 1 548 ? 7.717 28.270 47.199 1.00 19.52 ? 544 TRP A C 1 ATOM 4163 O O . TRP A 1 548 ? 7.541 29.421 47.467 1.00 19.99 ? 544 TRP A O 1 ATOM 4164 C CB . TRP A 1 548 ? 7.686 25.781 47.805 1.00 18.86 ? 544 TRP A CB 1 ATOM 4165 C CG . TRP A 1 548 ? 7.296 24.798 48.855 1.00 21.47 ? 544 TRP A CG 1 ATOM 4166 C CD1 . TRP A 1 548 ? 6.174 24.048 48.876 1.00 23.05 ? 544 TRP A CD1 1 ATOM 4167 C CD2 . TRP A 1 548 ? 8.035 24.486 50.058 1.00 20.14 ? 544 TRP A CD2 1 ATOM 4168 N NE1 . TRP A 1 548 ? 6.151 23.250 50.021 1.00 22.92 ? 544 TRP A NE1 1 ATOM 4169 C CE2 . TRP A 1 548 ? 7.264 23.522 50.777 1.00 25.54 ? 544 TRP A CE2 1 ATOM 4170 C CE3 . TRP A 1 548 ? 9.264 24.911 50.579 1.00 21.65 ? 544 TRP A CE3 1 ATOM 4171 C CZ2 . TRP A 1 548 ? 7.690 22.949 52.000 1.00 25.14 ? 544 TRP A CZ2 1 ATOM 4172 C CZ3 . TRP A 1 548 ? 9.682 24.388 51.867 1.00 23.56 ? 544 TRP A CZ3 1 ATOM 4173 C CH2 . TRP A 1 548 ? 8.859 23.414 52.551 1.00 24.84 ? 544 TRP A CH2 1 ATOM 4174 N N . LEU A 1 549 ? 8.074 27.848 45.983 1.00 19.77 ? 545 LEU A N 1 ATOM 4175 C CA . LEU A 1 549 ? 8.244 28.771 44.800 1.00 19.92 ? 545 LEU A CA 1 ATOM 4176 C C . LEU A 1 549 ? 7.301 28.184 43.732 1.00 19.61 ? 545 LEU A C 1 ATOM 4177 O O . LEU A 1 549 ? 7.743 27.411 42.852 1.00 20.50 ? 545 LEU A O 1 ATOM 4178 C CB . LEU A 1 549 ? 9.716 28.741 44.318 1.00 18.10 ? 545 LEU A CB 1 ATOM 4179 C CG . LEU A 1 549 ? 10.778 29.087 45.387 1.00 19.33 ? 545 LEU A CG 1 ATOM 4180 C CD1 . LEU A 1 549 ? 12.216 28.934 44.865 1.00 17.03 ? 545 LEU A CD1 1 ATOM 4181 C CD2 . LEU A 1 549 ? 10.509 30.606 45.754 1.00 21.30 ? 545 LEU A CD2 1 ATOM 4182 N N . PRO A 1 550 ? 6.028 28.576 43.786 1.00 19.05 ? 546 PRO A N 1 ATOM 4183 C CA . PRO A 1 550 ? 4.999 27.854 43.028 1.00 19.82 ? 546 PRO A CA 1 ATOM 4184 C C . PRO A 1 550 ? 4.918 28.153 41.562 1.00 18.76 ? 546 PRO A C 1 ATOM 4185 O O . PRO A 1 550 ? 4.170 27.472 40.866 1.00 18.99 ? 546 PRO A O 1 ATOM 4186 C CB . PRO A 1 550 ? 3.692 28.246 43.747 1.00 20.10 ? 546 PRO A CB 1 ATOM 4187 C CG . PRO A 1 550 ? 3.964 29.654 44.305 1.00 21.15 ? 546 PRO A CG 1 ATOM 4188 C CD . PRO A 1 550 ? 5.458 29.616 44.687 1.00 18.81 ? 546 PRO A CD 1 ATOM 4189 N N . GLY A 1 551 ? 5.619 29.179 41.061 1.00 18.67 ? 547 GLY A N 1 ATOM 4190 C CA . GLY A 1 551 ? 5.731 29.321 39.581 1.00 18.56 ? 547 GLY A CA 1 ATOM 4191 C C . GLY A 1 551 ? 4.740 30.343 39.032 1.00 20.15 ? 547 GLY A C 1 ATOM 4192 O O . GLY A 1 551 ? 4.239 31.196 39.791 1.00 21.32 ? 547 GLY A O 1 ATOM 4193 N N . SER A 1 552 ? 4.384 30.229 37.746 1.00 20.47 ? 548 SER A N 1 ATOM 4194 C CA . SER A 1 552 ? 3.618 31.293 37.092 1.00 21.06 ? 548 SER A CA 1 ATOM 4195 C C . SER A 1 552 ? 2.114 31.282 37.458 1.00 20.64 ? 548 SER A C 1 ATOM 4196 O O . SER A 1 552 ? 1.402 32.283 37.278 1.00 20.98 ? 548 SER A O 1 ATOM 4197 C CB . SER A 1 552 ? 3.815 31.241 35.568 1.00 19.37 ? 548 SER A CB 1 ATOM 4198 O OG . SER A 1 552 ? 3.413 29.926 35.041 1.00 21.50 ? 548 SER A OG 1 ATOM 4199 N N . GLU A 1 553 ? 1.630 30.144 37.929 1.00 20.20 ? 549 GLU A N 1 ATOM 4200 C CA . GLU A 1 553 ? 0.167 29.927 38.090 1.00 20.67 ? 549 GLU A CA 1 ATOM 4201 C C . GLU A 1 553 ? -0.326 30.171 39.510 1.00 21.18 ? 549 GLU A C 1 ATOM 4202 O O . GLU A 1 553 ? -0.577 29.239 40.270 1.00 20.94 ? 549 GLU A O 1 ATOM 4203 C CB . GLU A 1 553 ? -0.246 28.538 37.555 1.00 20.69 ? 549 GLU A CB 1 ATOM 4204 C CG . GLU A 1 553 ? 0.180 28.315 36.058 1.00 20.26 ? 549 GLU A CG 1 ATOM 4205 C CD . GLU A 1 553 ? -0.090 29.550 35.166 1.00 20.79 ? 549 GLU A CD 1 ATOM 4206 O OE1 . GLU A 1 553 ? -1.245 30.081 35.212 1.00 21.51 ? 549 GLU A OE1 1 ATOM 4207 O OE2 . GLU A 1 553 ? 0.834 29.994 34.432 1.00 20.27 ? 549 GLU A OE2 1 ATOM 4208 N N . GLY A 1 554 ? -0.469 31.445 39.893 1.00 21.12 ? 550 GLY A N 1 ATOM 4209 C CA . GLY A 1 554 ? -0.788 31.734 41.302 1.00 20.01 ? 550 GLY A CA 1 ATOM 4210 C C . GLY A 1 554 ? -2.201 31.294 41.688 1.00 21.03 ? 550 GLY A C 1 ATOM 4211 O O . GLY A 1 554 ? -2.500 31.234 42.868 1.00 20.64 ? 550 GLY A O 1 ATOM 4212 N N . GLN A 1 555 ? -3.085 30.989 40.724 1.00 20.69 ? 551 GLN A N 1 ATOM 4213 C CA . GLN A 1 555 ? -4.376 30.410 41.088 1.00 21.58 ? 551 GLN A CA 1 ATOM 4214 C C . GLN A 1 555 ? -4.265 29.069 41.808 1.00 22.43 ? 551 GLN A C 1 ATOM 4215 O O . GLN A 1 555 ? -5.225 28.683 42.481 1.00 22.11 ? 551 GLN A O 1 ATOM 4216 C CB . GLN A 1 555 ? -5.322 30.303 39.864 1.00 22.21 ? 551 GLN A CB 1 ATOM 4217 C CG . GLN A 1 555 ? -5.737 31.743 39.399 1.00 23.96 ? 551 GLN A CG 1 ATOM 4218 C CD . GLN A 1 555 ? -6.361 31.708 38.024 1.00 30.06 ? 551 GLN A CD 1 ATOM 4219 O OE1 . GLN A 1 555 ? -7.574 31.826 37.894 1.00 30.38 ? 551 GLN A OE1 1 ATOM 4220 N NE2 . GLN A 1 555 ? -5.542 31.499 37.005 1.00 23.25 ? 551 GLN A NE2 1 ATOM 4221 N N . GLY A 1 556 ? -3.103 28.389 41.701 1.00 21.31 ? 552 GLY A N 1 ATOM 4222 C CA . GLY A 1 556 ? -2.869 27.201 42.533 1.00 21.42 ? 552 GLY A CA 1 ATOM 4223 C C . GLY A 1 556 ? -2.965 27.553 44.022 1.00 21.53 ? 552 GLY A C 1 ATOM 4224 O O . GLY A 1 556 ? -3.472 26.788 44.830 1.00 21.91 ? 552 GLY A O 1 ATOM 4225 N N . VAL A 1 557 ? -2.464 28.736 44.392 1.00 21.78 ? 553 VAL A N 1 ATOM 4226 C CA . VAL A 1 557 ? -2.514 29.159 45.777 1.00 22.04 ? 553 VAL A CA 1 ATOM 4227 C C . VAL A 1 557 ? -3.987 29.387 46.220 1.00 22.64 ? 553 VAL A C 1 ATOM 4228 O O . VAL A 1 557 ? -4.457 28.840 47.250 1.00 22.64 ? 553 VAL A O 1 ATOM 4229 C CB . VAL A 1 557 ? -1.648 30.438 45.992 1.00 22.52 ? 553 VAL A CB 1 ATOM 4230 C CG1 A VAL A 1 557 ? -1.745 30.903 47.443 1.00 25.03 ? 553 VAL A CG1 1 ATOM 4231 C CG2 A VAL A 1 557 ? -0.144 30.187 45.563 1.00 18.83 ? 553 VAL A CG2 1 ATOM 4232 N N . THR A 1 558 ? -4.731 30.149 45.428 1.00 22.26 ? 554 THR A N 1 ATOM 4233 C CA . THR A 1 558 ? -6.095 30.503 45.836 1.00 21.99 ? 554 THR A CA 1 ATOM 4234 C C . THR A 1 558 ? -7.005 29.321 45.706 1.00 22.64 ? 554 THR A C 1 ATOM 4235 O O . THR A 1 558 ? -8.020 29.275 46.418 1.00 23.70 ? 554 THR A O 1 ATOM 4236 C CB . THR A 1 558 ? -6.611 31.708 45.032 1.00 23.33 ? 554 THR A CB 1 ATOM 4237 O OG1 . THR A 1 558 ? -6.398 31.469 43.633 1.00 23.58 ? 554 THR A OG1 1 ATOM 4238 C CG2 . THR A 1 558 ? -5.788 32.976 45.413 1.00 22.12 ? 554 THR A CG2 1 ATOM 4239 N N . ASP A 1 559 ? -6.687 28.351 44.823 1.00 21.27 ? 555 ASP A N 1 ATOM 4240 C CA . ASP A 1 559 ? -7.531 27.105 44.737 1.00 23.33 ? 555 ASP A CA 1 ATOM 4241 C C . ASP A 1 559 ? -7.640 26.420 46.125 1.00 23.67 ? 555 ASP A C 1 ATOM 4242 O O . ASP A 1 559 ? -8.684 25.890 46.467 1.00 24.56 ? 555 ASP A O 1 ATOM 4243 C CB . ASP A 1 559 ? -6.973 26.069 43.724 1.00 21.83 ? 555 ASP A CB 1 ATOM 4244 C CG . ASP A 1 559 ? -7.281 26.428 42.267 1.00 23.95 ? 555 ASP A CG 1 ATOM 4245 O OD1 . ASP A 1 559 ? -8.082 27.375 42.011 1.00 23.27 ? 555 ASP A OD1 1 ATOM 4246 O OD2 . ASP A 1 559 ? -6.633 25.829 41.361 1.00 23.86 ? 555 ASP A OD2 1 ATOM 4247 N N . ALA A 1 560 ? -6.559 26.451 46.909 1.00 21.41 ? 556 ALA A N 1 ATOM 4248 C CA . ALA A 1 560 ? -6.571 25.871 48.248 1.00 21.95 ? 556 ALA A CA 1 ATOM 4249 C C . ALA A 1 560 ? -7.071 26.903 49.311 1.00 23.03 ? 556 ALA A C 1 ATOM 4250 O O . ALA A 1 560 ? -7.842 26.539 50.180 1.00 22.22 ? 556 ALA A O 1 ATOM 4251 C CB . ALA A 1 560 ? -5.196 25.371 48.628 1.00 22.78 ? 556 ALA A CB 1 ATOM 4252 N N . LEU A 1 561 ? -6.717 28.173 49.175 1.00 21.60 ? 557 LEU A N 1 ATOM 4253 C CA . LEU A 1 561 ? -7.181 29.204 50.141 1.00 23.22 ? 557 LEU A CA 1 ATOM 4254 C C . LEU A 1 561 ? -8.684 29.335 50.235 1.00 23.59 ? 557 LEU A C 1 ATOM 4255 O O . LEU A 1 561 ? -9.210 29.483 51.358 1.00 22.88 ? 557 LEU A O 1 ATOM 4256 C CB . LEU A 1 561 ? -6.570 30.580 49.865 1.00 23.08 ? 557 LEU A CB 1 ATOM 4257 C CG . LEU A 1 561 ? -5.044 30.729 50.022 1.00 23.63 ? 557 LEU A CG 1 ATOM 4258 C CD1 . LEU A 1 561 ? -4.606 32.192 49.668 1.00 22.29 ? 557 LEU A CD1 1 ATOM 4259 C CD2 . LEU A 1 561 ? -4.559 30.396 51.447 1.00 21.29 ? 557 LEU A CD2 1 ATOM 4260 N N . PHE A 1 562 ? -9.366 29.253 49.084 1.00 22.35 ? 558 PHE A N 1 ATOM 4261 C CA . PHE A 1 562 ? -10.792 29.421 49.038 1.00 23.19 ? 558 PHE A CA 1 ATOM 4262 C C . PHE A 1 562 ? -11.513 28.063 49.021 1.00 23.57 ? 558 PHE A C 1 ATOM 4263 O O . PHE A 1 562 ? -12.752 28.002 48.863 1.00 22.73 ? 558 PHE A O 1 ATOM 4264 C CB . PHE A 1 562 ? -11.204 30.323 47.858 1.00 22.29 ? 558 PHE A CB 1 ATOM 4265 C CG . PHE A 1 562 ? -10.728 31.773 48.030 1.00 25.64 ? 558 PHE A CG 1 ATOM 4266 C CD1 . PHE A 1 562 ? -11.315 32.620 48.986 1.00 23.49 ? 558 PHE A CD1 1 ATOM 4267 C CD2 . PHE A 1 562 ? -9.702 32.282 47.214 1.00 28.79 ? 558 PHE A CD2 1 ATOM 4268 C CE1 . PHE A 1 562 ? -10.874 33.916 49.170 1.00 22.70 ? 558 PHE A CE1 1 ATOM 4269 C CE2 . PHE A 1 562 ? -9.258 33.631 47.379 1.00 28.38 ? 558 PHE A CE2 1 ATOM 4270 C CZ . PHE A 1 562 ? -9.843 34.443 48.359 1.00 28.81 ? 558 PHE A CZ 1 ATOM 4271 N N . GLY A 1 563 ? -10.766 26.965 49.199 1.00 21.85 ? 559 GLY A N 1 ATOM 4272 C CA . GLY A 1 563 ? -11.499 25.668 49.437 1.00 23.83 ? 559 GLY A CA 1 ATOM 4273 C C . GLY A 1 563 ? -12.021 24.940 48.176 1.00 25.21 ? 559 GLY A C 1 ATOM 4274 O O . GLY A 1 563 ? -12.783 23.974 48.272 1.00 24.72 ? 559 GLY A O 1 ATOM 4275 N N . ASP A 1 564 ? -11.612 25.370 46.993 1.00 24.69 ? 560 ASP A N 1 ATOM 4276 C CA . ASP A 1 564 ? -11.909 24.587 45.768 1.00 25.87 ? 560 ASP A CA 1 ATOM 4277 C C . ASP A 1 564 ? -11.296 23.204 45.872 1.00 26.28 ? 560 ASP A C 1 ATOM 4278 O O . ASP A 1 564 ? -11.895 22.238 45.381 1.00 26.36 ? 560 ASP A O 1 ATOM 4279 C CB . ASP A 1 564 ? -11.412 25.289 44.506 1.00 26.56 ? 560 ASP A CB 1 ATOM 4280 C CG . ASP A 1 564 ? -12.310 26.503 44.137 1.00 30.96 ? 560 ASP A CG 1 ATOM 4281 O OD1 . ASP A 1 564 ? -13.407 26.671 44.696 1.00 34.97 ? 560 ASP A OD1 1 ATOM 4282 O OD2 . ASP A 1 564 ? -11.901 27.290 43.309 1.00 37.79 ? 560 ASP A OD2 1 ATOM 4283 N N . PHE A 1 565 ? -10.140 23.107 46.542 1.00 25.59 ? 561 PHE A N 1 ATOM 4284 C CA . PHE A 1 565 ? -9.524 21.802 46.837 1.00 26.19 ? 561 PHE A CA 1 ATOM 4285 C C . PHE A 1 565 ? -9.065 21.839 48.269 1.00 26.52 ? 561 PHE A C 1 ATOM 4286 O O . PHE A 1 565 ? -8.852 22.926 48.815 1.00 25.90 ? 561 PHE A O 1 ATOM 4287 C CB . PHE A 1 565 ? -8.301 21.561 45.927 1.00 25.95 ? 561 PHE A CB 1 ATOM 4288 C CG . PHE A 1 565 ? -8.652 21.424 44.493 1.00 29.41 ? 561 PHE A CG 1 ATOM 4289 C CD1 . PHE A 1 565 ? -8.770 22.560 43.667 1.00 28.70 ? 561 PHE A CD1 1 ATOM 4290 C CD2 . PHE A 1 565 ? -8.899 20.147 43.949 1.00 31.41 ? 561 PHE A CD2 1 ATOM 4291 C CE1 . PHE A 1 565 ? -9.127 22.425 42.320 1.00 32.90 ? 561 PHE A CE1 1 ATOM 4292 C CE2 . PHE A 1 565 ? -9.261 20.011 42.586 1.00 33.28 ? 561 PHE A CE2 1 ATOM 4293 C CZ . PHE A 1 565 ? -9.382 21.149 41.785 1.00 30.31 ? 561 PHE A CZ 1 ATOM 4294 N N . GLY A 1 566 ? -8.924 20.668 48.905 1.00 26.65 ? 562 GLY A N 1 ATOM 4295 C CA . GLY A 1 566 ? -8.331 20.633 50.256 1.00 26.53 ? 562 GLY A CA 1 ATOM 4296 C C . GLY A 1 566 ? -6.802 20.742 50.203 1.00 26.08 ? 562 GLY A C 1 ATOM 4297 O O . GLY A 1 566 ? -6.169 20.404 49.165 1.00 26.76 ? 562 GLY A O 1 ATOM 4298 N N . PHE A 1 567 ? -6.186 21.196 51.287 1.00 23.38 ? 563 PHE A N 1 ATOM 4299 C CA . PHE A 1 567 ? -4.709 21.159 51.375 1.00 25.49 ? 563 PHE A CA 1 ATOM 4300 C C . PHE A 1 567 ? -4.292 19.711 51.544 1.00 26.12 ? 563 PHE A C 1 ATOM 4301 O O . PHE A 1 567 ? -4.957 18.967 52.337 1.00 26.00 ? 563 PHE A O 1 ATOM 4302 C CB . PHE A 1 567 ? -4.208 21.960 52.582 1.00 23.03 ? 563 PHE A CB 1 ATOM 4303 C CG . PHE A 1 567 ? -4.168 23.431 52.355 1.00 22.03 ? 563 PHE A CG 1 ATOM 4304 C CD1 . PHE A 1 567 ? -5.282 24.233 52.659 1.00 22.25 ? 563 PHE A CD1 1 ATOM 4305 C CD2 . PHE A 1 567 ? -3.012 24.040 51.846 1.00 22.40 ? 563 PHE A CD2 1 ATOM 4306 C CE1 . PHE A 1 567 ? -5.246 25.612 52.456 1.00 21.22 ? 563 PHE A CE1 1 ATOM 4307 C CE2 . PHE A 1 567 ? -2.961 25.390 51.656 1.00 20.20 ? 563 PHE A CE2 1 ATOM 4308 C CZ . PHE A 1 567 ? -4.115 26.193 51.969 1.00 20.69 ? 563 PHE A CZ 1 ATOM 4309 N N . THR A 1 568 ? -3.251 19.288 50.806 1.00 25.79 ? 564 THR A N 1 ATOM 4310 C CA . THR A 1 568 ? -2.742 17.873 50.876 1.00 25.46 ? 564 THR A CA 1 ATOM 4311 C C . THR A 1 568 ? -1.220 17.756 50.989 1.00 25.52 ? 564 THR A C 1 ATOM 4312 O O . THR A 1 568 ? -0.710 16.658 51.290 1.00 25.08 ? 564 THR A O 1 ATOM 4313 C CB . THR A 1 568 ? -3.168 17.022 49.663 1.00 25.90 ? 564 THR A CB 1 ATOM 4314 O OG1 . THR A 1 568 ? -2.776 17.710 48.469 1.00 26.95 ? 564 THR A OG1 1 ATOM 4315 C CG2 . THR A 1 568 ? -4.718 16.806 49.646 1.00 28.52 ? 564 THR A CG2 1 ATOM 4316 N N . GLY A 1 569 ? -0.493 18.876 50.738 1.00 24.53 ? 565 GLY A N 1 ATOM 4317 C CA . GLY A 1 569 ? 0.988 18.845 50.710 1.00 22.73 ? 565 GLY A CA 1 ATOM 4318 C C . GLY A 1 569 ? 1.546 18.445 52.090 1.00 23.96 ? 565 GLY A C 1 ATOM 4319 O O . GLY A 1 569 ? 0.925 18.755 53.141 1.00 23.31 ? 565 GLY A O 1 ATOM 4320 N N . ARG A 1 570 ? 2.676 17.720 52.088 1.00 23.06 ? 566 ARG A N 1 ATOM 4321 C CA . ARG A 1 570 ? 3.356 17.322 53.326 1.00 24.28 ? 566 ARG A CA 1 ATOM 4322 C C . ARG A 1 570 ? 4.823 17.720 53.222 1.00 25.26 ? 566 ARG A C 1 ATOM 4323 O O . ARG A 1 570 ? 5.408 17.561 52.137 1.00 23.43 ? 566 ARG A O 1 ATOM 4324 C CB . ARG A 1 570 ? 3.217 15.792 53.439 1.00 24.19 ? 566 ARG A CB 1 ATOM 4325 C CG A ARG A 1 570 ? 1.672 15.456 53.465 0.60 27.24 ? 566 ARG A CG 1 ATOM 4326 C CG B ARG A 1 570 ? 1.933 15.228 54.084 0.40 25.57 ? 566 ARG A CG 1 ATOM 4327 C CD A ARG A 1 570 ? 1.317 14.001 53.454 0.60 37.73 ? 566 ARG A CD 1 ATOM 4328 C CD B ARG A 1 570 ? 2.024 13.680 54.009 0.40 27.31 ? 566 ARG A CD 1 ATOM 4329 N NE A ARG A 1 570 ? 1.849 13.326 54.618 0.60 40.83 ? 566 ARG A NE 1 ATOM 4330 N NE B ARG A 1 570 ? 1.644 13.238 52.680 0.40 27.04 ? 566 ARG A NE 1 ATOM 4331 C CZ A ARG A 1 570 ? 2.917 12.548 54.585 0.60 43.45 ? 566 ARG A CZ 1 ATOM 4332 C CZ B ARG A 1 570 ? 1.844 12.037 52.182 0.40 28.77 ? 566 ARG A CZ 1 ATOM 4333 N NH1 A ARG A 1 570 ? 3.519 12.332 53.423 0.60 43.98 ? 566 ARG A NH1 1 ATOM 4334 N NH1 B ARG A 1 570 ? 1.422 11.765 50.956 0.40 26.22 ? 566 ARG A NH1 1 ATOM 4335 N NH2 A ARG A 1 570 ? 3.347 11.952 55.696 0.60 43.50 ? 566 ARG A NH2 1 ATOM 4336 N NH2 B ARG A 1 570 ? 2.450 11.115 52.909 0.40 32.67 ? 566 ARG A NH2 1 ATOM 4337 N N . LEU A 1 571 ? 5.415 18.258 54.305 1.00 23.92 ? 567 LEU A N 1 ATOM 4338 C CA . LEU A 1 571 ? 6.806 18.705 54.228 1.00 23.89 ? 567 LEU A CA 1 ATOM 4339 C C . LEU A 1 571 ? 7.720 17.628 53.649 1.00 24.66 ? 567 LEU A C 1 ATOM 4340 O O . LEU A 1 571 ? 7.690 16.454 54.076 1.00 24.76 ? 567 LEU A O 1 ATOM 4341 C CB . LEU A 1 571 ? 7.326 19.114 55.616 1.00 23.72 ? 567 LEU A CB 1 ATOM 4342 C CG . LEU A 1 571 ? 6.755 20.355 56.243 1.00 25.58 ? 567 LEU A CG 1 ATOM 4343 C CD1 . LEU A 1 571 ? 7.494 20.574 57.543 1.00 21.75 ? 567 LEU A CD1 1 ATOM 4344 C CD2 . LEU A 1 571 ? 6.956 21.605 55.280 1.00 21.08 ? 567 LEU A CD2 1 ATOM 4345 N N . PRO A 1 572 ? 8.496 17.990 52.621 1.00 24.06 ? 568 PRO A N 1 ATOM 4346 C CA . PRO A 1 572 ? 9.479 17.077 52.053 1.00 24.12 ? 568 PRO A CA 1 ATOM 4347 C C . PRO A 1 572 ? 10.837 17.255 52.725 1.00 24.99 ? 568 PRO A C 1 ATOM 4348 O O . PRO A 1 572 ? 11.813 16.659 52.277 1.00 25.44 ? 568 PRO A O 1 ATOM 4349 C CB . PRO A 1 572 ? 9.572 17.543 50.565 1.00 22.18 ? 568 PRO A CB 1 ATOM 4350 C CG . PRO A 1 572 ? 9.415 19.085 50.689 1.00 21.55 ? 568 PRO A CG 1 ATOM 4351 C CD . PRO A 1 572 ? 8.315 19.225 51.792 1.00 23.54 ? 568 PRO A CD 1 ATOM 4352 N N . ARG A 1 573 ? 10.888 18.096 53.752 1.00 25.82 ? 569 ARG A N 1 ATOM 4353 C CA . ARG A 1 573 ? 12.158 18.542 54.394 1.00 27.49 ? 569 ARG A CA 1 ATOM 4354 C C . ARG A 1 573 ? 11.783 18.717 55.844 1.00 26.55 ? 569 ARG A C 1 ATOM 4355 O O . ARG A 1 573 ? 10.651 19.079 56.144 1.00 26.69 ? 569 ARG A O 1 ATOM 4356 C CB . ARG A 1 573 ? 12.579 19.988 53.979 1.00 26.94 ? 569 ARG A CB 1 ATOM 4357 C CG . ARG A 1 573 ? 13.115 20.176 52.612 1.00 31.34 ? 569 ARG A CG 1 ATOM 4358 C CD . ARG A 1 573 ? 14.149 21.258 52.507 1.00 28.28 ? 569 ARG A CD 1 ATOM 4359 N NE . ARG A 1 573 ? 15.346 20.935 53.283 1.00 29.41 ? 569 ARG A NE 1 ATOM 4360 C CZ . ARG A 1 573 ? 16.290 20.086 52.909 1.00 29.82 ? 569 ARG A CZ 1 ATOM 4361 N NH1 . ARG A 1 573 ? 16.221 19.488 51.734 1.00 27.16 ? 569 ARG A NH1 1 ATOM 4362 N NH2 . ARG A 1 573 ? 17.319 19.833 53.716 1.00 30.76 ? 569 ARG A NH2 1 ATOM 4363 N N . THR A 1 574 ? 12.771 18.611 56.709 1.00 27.04 ? 570 THR A N 1 ATOM 4364 C CA . THR A 1 574 ? 12.639 18.986 58.100 1.00 27.49 ? 570 THR A CA 1 ATOM 4365 C C . THR A 1 574 ? 12.543 20.512 58.259 1.00 27.64 ? 570 THR A C 1 ATOM 4366 O O . THR A 1 574 ? 13.293 21.234 57.624 1.00 28.33 ? 570 THR A O 1 ATOM 4367 C CB . THR A 1 574 ? 13.918 18.462 58.867 1.00 28.53 ? 570 THR A CB 1 ATOM 4368 O OG1 . THR A 1 574 ? 13.873 17.026 58.892 1.00 27.14 ? 570 THR A OG1 1 ATOM 4369 C CG2 . THR A 1 574 ? 13.969 19.035 60.292 1.00 28.01 ? 570 THR A CG2 1 ATOM 4370 N N . TRP A 1 575 ? 11.627 20.996 59.103 1.00 26.25 ? 571 TRP A N 1 ATOM 4371 C CA . TRP A 1 575 ? 11.618 22.384 59.451 1.00 25.85 ? 571 TRP A CA 1 ATOM 4372 C C . TRP A 1 575 ? 12.293 22.530 60.798 1.00 26.85 ? 571 TRP A C 1 ATOM 4373 O O . TRP A 1 575 ? 11.774 22.046 61.825 1.00 28.05 ? 571 TRP A O 1 ATOM 4374 C CB . TRP A 1 575 ? 10.193 22.983 59.488 1.00 25.71 ? 571 TRP A CB 1 ATOM 4375 C CG . TRP A 1 575 ? 10.167 24.460 59.163 1.00 23.38 ? 571 TRP A CG 1 ATOM 4376 C CD1 . TRP A 1 575 ? 10.773 25.481 59.851 1.00 25.88 ? 571 TRP A CD1 1 ATOM 4377 C CD2 . TRP A 1 575 ? 9.576 25.042 57.999 1.00 23.97 ? 571 TRP A CD2 1 ATOM 4378 N NE1 . TRP A 1 575 ? 10.553 26.694 59.183 1.00 24.64 ? 571 TRP A NE1 1 ATOM 4379 C CE2 . TRP A 1 575 ? 9.815 26.437 58.051 1.00 24.21 ? 571 TRP A CE2 1 ATOM 4380 C CE3 . TRP A 1 575 ? 8.886 24.501 56.886 1.00 24.06 ? 571 TRP A CE3 1 ATOM 4381 C CZ2 . TRP A 1 575 ? 9.372 27.321 57.040 1.00 21.97 ? 571 TRP A CZ2 1 ATOM 4382 C CZ3 . TRP A 1 575 ? 8.421 25.403 55.881 1.00 23.65 ? 571 TRP A CZ3 1 ATOM 4383 C CH2 . TRP A 1 575 ? 8.673 26.770 55.977 1.00 25.92 ? 571 TRP A CH2 1 ATOM 4384 N N . PHE A 1 576 ? 13.444 23.201 60.781 1.00 28.10 ? 572 PHE A N 1 ATOM 4385 C CA . PHE A 1 576 ? 14.299 23.368 61.955 1.00 28.88 ? 572 PHE A CA 1 ATOM 4386 C C . PHE A 1 576 ? 13.711 24.391 62.914 1.00 29.39 ? 572 PHE A C 1 ATOM 4387 O O . PHE A 1 576 ? 12.945 25.288 62.527 1.00 27.13 ? 572 PHE A O 1 ATOM 4388 C CB . PHE A 1 576 ? 15.725 23.817 61.561 1.00 29.63 ? 572 PHE A CB 1 ATOM 4389 C CG . PHE A 1 576 ? 15.746 25.041 60.660 1.00 27.98 ? 572 PHE A CG 1 ATOM 4390 C CD1 . PHE A 1 576 ? 15.669 26.315 61.193 1.00 29.08 ? 572 PHE A CD1 1 ATOM 4391 C CD2 . PHE A 1 576 ? 15.822 24.887 59.282 1.00 28.11 ? 572 PHE A CD2 1 ATOM 4392 C CE1 . PHE A 1 576 ? 15.627 27.440 60.368 1.00 32.11 ? 572 PHE A CE1 1 ATOM 4393 C CE2 . PHE A 1 576 ? 15.797 25.999 58.427 1.00 30.47 ? 572 PHE A CE2 1 ATOM 4394 C CZ . PHE A 1 576 ? 15.672 27.276 58.953 1.00 28.11 ? 572 PHE A CZ 1 ATOM 4395 N N . LYS A 1 577 ? 14.115 24.283 64.180 1.00 28.61 ? 573 LYS A N 1 ATOM 4396 C CA . LYS A 1 577 ? 13.765 25.323 65.132 1.00 30.11 ? 573 LYS A CA 1 ATOM 4397 C C . LYS A 1 577 ? 14.732 26.506 65.002 1.00 29.95 ? 573 LYS A C 1 ATOM 4398 O O . LYS A 1 577 ? 14.342 27.644 65.184 1.00 29.25 ? 573 LYS A O 1 ATOM 4399 C CB . LYS A 1 577 ? 13.808 24.770 66.571 1.00 30.95 ? 573 LYS A CB 1 ATOM 4400 C CG . LYS A 1 577 ? 12.695 23.790 66.896 1.00 30.93 ? 573 LYS A CG 1 ATOM 4401 C CD . LYS A 1 577 ? 12.763 23.310 68.401 1.00 30.52 ? 573 LYS A CD 1 ATOM 4402 C CE . LYS A 1 577 ? 11.548 22.414 68.697 1.00 32.47 ? 573 LYS A CE 1 ATOM 4403 N NZ . LYS A 1 577 ? 11.742 21.831 70.090 1.00 36.63 ? 573 LYS A NZ 1 ATOM 4404 N N . SER A 1 578 ? 16.004 26.219 64.709 1.00 29.55 ? 574 SER A N 1 ATOM 4405 C CA . SER A 1 578 ? 17.056 27.230 64.749 1.00 30.98 ? 574 SER A CA 1 ATOM 4406 C C . SER A 1 578 ? 18.120 26.766 63.764 1.00 30.55 ? 574 SER A C 1 ATOM 4407 O O . SER A 1 578 ? 18.331 25.569 63.637 1.00 29.78 ? 574 SER A O 1 ATOM 4408 C CB . SER A 1 578 ? 17.682 27.288 66.178 1.00 31.63 ? 574 SER A CB 1 ATOM 4409 O OG . SER A 1 578 ? 18.927 28.019 66.127 1.00 39.43 ? 574 SER A OG 1 ATOM 4410 N N . VAL A 1 579 ? 18.812 27.692 63.102 1.00 30.56 ? 575 VAL A N 1 ATOM 4411 C CA . VAL A 1 579 ? 19.873 27.299 62.162 1.00 31.47 ? 575 VAL A CA 1 ATOM 4412 C C . VAL A 1 579 ? 21.091 26.674 62.891 1.00 33.43 ? 575 VAL A C 1 ATOM 4413 O O . VAL A 1 579 ? 21.843 25.917 62.298 1.00 31.38 ? 575 VAL A O 1 ATOM 4414 C CB . VAL A 1 579 ? 20.344 28.458 61.249 1.00 31.94 ? 575 VAL A CB 1 ATOM 4415 C CG1 . VAL A 1 579 ? 19.188 28.963 60.379 1.00 30.49 ? 575 VAL A CG1 1 ATOM 4416 C CG2 . VAL A 1 579 ? 20.984 29.586 62.066 1.00 33.94 ? 575 VAL A CG2 1 ATOM 4417 N N . ASP A 1 580 ? 21.226 26.984 64.191 1.00 34.71 ? 576 ASP A N 1 ATOM 4418 C CA . ASP A 1 580 ? 22.231 26.350 65.068 1.00 36.79 ? 576 ASP A CA 1 ATOM 4419 C C . ASP A 1 580 ? 22.121 24.846 65.094 1.00 35.98 ? 576 ASP A C 1 ATOM 4420 O O . ASP A 1 580 ? 23.097 24.155 65.391 1.00 36.32 ? 576 ASP A O 1 ATOM 4421 C CB . ASP A 1 580 ? 22.032 26.832 66.516 1.00 38.63 ? 576 ASP A CB 1 ATOM 4422 C CG . ASP A 1 580 ? 22.308 28.255 66.658 1.00 42.42 ? 576 ASP A CG 1 ATOM 4423 O OD1 . ASP A 1 580 ? 22.917 28.816 65.714 1.00 47.64 ? 576 ASP A OD1 1 ATOM 4424 O OD2 . ASP A 1 580 ? 21.901 28.820 67.692 1.00 50.79 ? 576 ASP A OD2 1 ATOM 4425 N N . GLN A 1 581 ? 20.930 24.331 64.836 1.00 33.09 ? 577 GLN A N 1 ATOM 4426 C CA . GLN A 1 581 ? 20.759 22.893 64.779 1.00 32.78 ? 577 GLN A CA 1 ATOM 4427 C C . GLN A 1 581 ? 21.328 22.257 63.498 1.00 32.48 ? 577 GLN A C 1 ATOM 4428 O O . GLN A 1 581 ? 21.548 21.039 63.451 1.00 31.61 ? 577 GLN A O 1 ATOM 4429 C CB . GLN A 1 581 ? 19.270 22.533 64.833 1.00 31.54 ? 577 GLN A CB 1 ATOM 4430 C CG . GLN A 1 581 ? 18.514 23.059 66.028 1.00 32.71 ? 577 GLN A CG 1 ATOM 4431 C CD . GLN A 1 581 ? 17.047 22.678 65.945 1.00 34.94 ? 577 GLN A CD 1 ATOM 4432 O OE1 . GLN A 1 581 ? 16.304 23.153 65.051 1.00 31.44 ? 577 GLN A OE1 1 ATOM 4433 N NE2 . GLN A 1 581 ? 16.619 21.788 66.835 1.00 31.73 ? 577 GLN A NE2 1 ATOM 4434 N N . LEU A 1 582 ? 21.521 23.042 62.441 1.00 30.49 ? 578 LEU A N 1 ATOM 4435 C CA . LEU A 1 582 ? 21.814 22.421 61.131 1.00 30.35 ? 578 LEU A CA 1 ATOM 4436 C C . LEU A 1 582 ? 23.257 21.852 61.033 1.00 31.62 ? 578 LEU A C 1 ATOM 4437 O O . LEU A 1 582 ? 24.175 22.474 61.552 1.00 32.07 ? 578 LEU A O 1 ATOM 4438 C CB . LEU A 1 582 ? 21.586 23.468 60.032 1.00 28.91 ? 578 LEU A CB 1 ATOM 4439 C CG . LEU A 1 582 ? 20.132 24.022 59.999 1.00 27.53 ? 578 LEU A CG 1 ATOM 4440 C CD1 . LEU A 1 582 ? 19.948 25.171 58.928 1.00 26.42 ? 578 LEU A CD1 1 ATOM 4441 C CD2 . LEU A 1 582 ? 19.137 22.895 59.720 1.00 24.87 ? 578 LEU A CD2 1 ATOM 4442 N N . PRO A 1 583 ? 23.460 20.742 60.296 1.00 31.91 ? 579 PRO A N 1 ATOM 4443 C CA . PRO A 1 583 ? 22.410 20.001 59.562 1.00 32.35 ? 579 PRO A CA 1 ATOM 4444 C C . PRO A 1 583 ? 21.561 19.134 60.482 1.00 33.25 ? 579 PRO A C 1 ATOM 4445 O O . PRO A 1 583 ? 22.072 18.618 61.458 1.00 33.58 ? 579 PRO A O 1 ATOM 4446 C CB . PRO A 1 583 ? 23.201 19.140 58.578 1.00 31.13 ? 579 PRO A CB 1 ATOM 4447 C CG . PRO A 1 583 ? 24.562 18.920 59.278 1.00 33.34 ? 579 PRO A CG 1 ATOM 4448 C CD . PRO A 1 583 ? 24.823 20.167 60.075 1.00 33.84 ? 579 PRO A CD 1 ATOM 4449 N N . MET A 1 584 ? 20.265 19.016 60.200 1.00 32.20 ? 580 MET A N 1 ATOM 4450 C CA . MET A 1 584 ? 19.415 18.155 60.982 1.00 33.82 ? 580 MET A CA 1 ATOM 4451 C C . MET A 1 584 ? 18.371 17.541 60.067 1.00 33.39 ? 580 MET A C 1 ATOM 4452 O O . MET A 1 584 ? 17.521 18.243 59.495 1.00 33.04 ? 580 MET A O 1 ATOM 4453 C CB . MET A 1 584 ? 18.837 18.935 62.196 1.00 34.03 ? 580 MET A CB 1 ATOM 4454 C CG . MET A 1 584 ? 17.930 18.119 63.102 1.00 33.45 ? 580 MET A CG 1 ATOM 4455 S SD . MET A 1 584 ? 17.217 19.180 64.389 1.00 32.62 ? 580 MET A SD 1 ATOM 4456 C CE . MET A 1 584 ? 15.982 20.100 63.369 1.00 31.22 ? 580 MET A CE 1 ATOM 4457 N N . ASN A 1 585 ? 18.483 16.234 59.870 1.00 34.40 ? 581 ASN A N 1 ATOM 4458 C CA . ASN A 1 585 ? 17.618 15.514 58.924 1.00 36.24 ? 581 ASN A CA 1 ATOM 4459 C C . ASN A 1 585 ? 16.882 14.378 59.623 1.00 37.98 ? 581 ASN A C 1 ATOM 4460 O O . ASN A 1 585 ? 17.412 13.816 60.592 1.00 36.46 ? 581 ASN A O 1 ATOM 4461 C CB . ASN A 1 585 ? 18.444 14.916 57.764 1.00 35.77 ? 581 ASN A CB 1 ATOM 4462 C CG . ASN A 1 585 ? 19.166 15.996 56.937 1.00 34.14 ? 581 ASN A CG 1 ATOM 4463 O OD1 . ASN A 1 585 ? 18.545 16.624 56.066 1.00 34.29 ? 581 ASN A OD1 1 ATOM 4464 N ND2 . ASN A 1 585 ? 20.466 16.238 57.226 1.00 28.47 ? 581 ASN A ND2 1 ATOM 4465 N N . VAL A 1 586 ? 15.709 14.017 59.083 1.00 39.18 ? 582 VAL A N 1 ATOM 4466 C CA . VAL A 1 586 ? 14.906 12.884 59.591 1.00 42.79 ? 582 VAL A CA 1 ATOM 4467 C C . VAL A 1 586 ? 15.766 11.625 59.689 1.00 44.00 ? 582 VAL A C 1 ATOM 4468 O O . VAL A 1 586 ? 16.574 11.311 58.790 1.00 43.45 ? 582 VAL A O 1 ATOM 4469 C CB . VAL A 1 586 ? 13.624 12.650 58.739 1.00 42.23 ? 582 VAL A CB 1 ATOM 4470 C CG1 . VAL A 1 586 ? 12.630 11.765 59.457 1.00 46.42 ? 582 VAL A CG1 1 ATOM 4471 C CG2 . VAL A 1 586 ? 12.923 13.935 58.532 1.00 46.74 ? 582 VAL A CG2 1 ATOM 4472 N N . GLY A 1 587 ? 15.635 10.925 60.811 1.00 46.00 ? 583 GLY A N 1 ATOM 4473 C CA . GLY A 1 587 ? 16.467 9.770 61.059 1.00 46.28 ? 583 GLY A CA 1 ATOM 4474 C C . GLY A 1 587 ? 17.721 10.067 61.848 1.00 47.44 ? 583 GLY A C 1 ATOM 4475 O O . GLY A 1 587 ? 18.389 9.123 62.324 1.00 46.35 ? 583 GLY A O 1 ATOM 4476 N N . ASP A 1 588 ? 18.046 11.354 62.020 1.00 47.54 ? 584 ASP A N 1 ATOM 4477 C CA . ASP A 1 588 ? 19.228 11.732 62.818 1.00 48.69 ? 584 ASP A CA 1 ATOM 4478 C C . ASP A 1 588 ? 19.002 11.311 64.255 1.00 50.80 ? 584 ASP A C 1 ATOM 4479 O O . ASP A 1 588 ? 17.842 11.246 64.725 1.00 50.79 ? 584 ASP A O 1 ATOM 4480 C CB . ASP A 1 588 ? 19.476 13.244 62.821 1.00 48.74 ? 584 ASP A CB 1 ATOM 4481 C CG . ASP A 1 588 ? 20.179 13.753 61.560 1.00 46.99 ? 584 ASP A CG 1 ATOM 4482 O OD1 . ASP A 1 588 ? 20.450 14.976 61.502 1.00 46.13 ? 584 ASP A OD1 1 ATOM 4483 O OD2 . ASP A 1 588 ? 20.445 12.962 60.640 1.00 41.77 ? 584 ASP A OD2 1 ATOM 4484 N N . ALA A 1 589 ? 20.103 11.071 64.965 1.00 52.51 ? 585 ALA A N 1 ATOM 4485 C CA . ALA A 1 589 ? 20.014 10.775 66.390 1.00 54.54 ? 585 ALA A CA 1 ATOM 4486 C C . ALA A 1 589 ? 19.476 11.973 67.181 1.00 55.00 ? 585 ALA A C 1 ATOM 4487 O O . ALA A 1 589 ? 18.630 11.769 68.054 1.00 55.98 ? 585 ALA A O 1 ATOM 4488 C CB . ALA A 1 589 ? 21.367 10.273 66.954 1.00 55.31 ? 585 ALA A CB 1 ATOM 4489 N N . HIS A 1 590 ? 19.909 13.199 66.848 1.00 54.53 ? 586 HIS A N 1 ATOM 4490 C CA . HIS A 1 590 ? 19.541 14.424 67.619 1.00 55.11 ? 586 HIS A CA 1 ATOM 4491 C C . HIS A 1 590 ? 18.238 15.181 67.212 1.00 52.83 ? 586 HIS A C 1 ATOM 4492 O O . HIS A 1 590 ? 18.104 16.376 67.532 1.00 54.09 ? 586 HIS A O 1 ATOM 4493 C CB . HIS A 1 590 ? 20.727 15.433 67.663 1.00 56.72 ? 586 HIS A CB 1 ATOM 4494 C CG . HIS A 1 590 ? 20.732 16.474 66.553 1.00 60.99 ? 586 HIS A CG 1 ATOM 4495 N ND1 . HIS A 1 590 ? 20.746 16.155 65.202 1.00 64.57 ? 586 HIS A ND1 1 ATOM 4496 C CD2 . HIS A 1 590 ? 20.755 17.836 66.609 1.00 63.67 ? 586 HIS A CD2 1 ATOM 4497 C CE1 . HIS A 1 590 ? 20.787 17.268 64.484 1.00 62.27 ? 586 HIS A CE1 1 ATOM 4498 N NE2 . HIS A 1 590 ? 20.792 18.304 65.311 1.00 59.17 ? 586 HIS A NE2 1 ATOM 4499 N N . TYR A 1 591 ? 17.282 14.489 66.591 1.00 48.78 ? 587 TYR A N 1 ATOM 4500 C CA . TYR A 1 591 ? 16.197 15.127 65.816 1.00 44.48 ? 587 TYR A CA 1 ATOM 4501 C C . TYR A 1 591 ? 15.175 15.905 66.651 1.00 42.00 ? 587 TYR A C 1 ATOM 4502 O O . TYR A 1 591 ? 14.340 15.303 67.335 1.00 42.17 ? 587 TYR A O 1 ATOM 4503 C CB . TYR A 1 591 ? 15.489 14.043 65.002 1.00 44.11 ? 587 TYR A CB 1 ATOM 4504 C CG . TYR A 1 591 ? 14.653 14.529 63.840 1.00 41.17 ? 587 TYR A CG 1 ATOM 4505 C CD1 . TYR A 1 591 ? 15.218 15.288 62.805 1.00 38.25 ? 587 TYR A CD1 1 ATOM 4506 C CD2 . TYR A 1 591 ? 13.324 14.148 63.728 1.00 38.17 ? 587 TYR A CD2 1 ATOM 4507 C CE1 . TYR A 1 591 ? 14.432 15.724 61.731 1.00 35.79 ? 587 TYR A CE1 1 ATOM 4508 C CE2 . TYR A 1 591 ? 12.532 14.584 62.669 1.00 36.76 ? 587 TYR A CE2 1 ATOM 4509 C CZ . TYR A 1 591 ? 13.094 15.361 61.675 1.00 36.15 ? 587 TYR A CZ 1 ATOM 4510 O OH . TYR A 1 591 ? 12.307 15.735 60.609 1.00 34.07 ? 587 TYR A OH 1 ATOM 4511 N N . ASP A 1 592 ? 15.233 17.239 66.576 1.00 38.35 ? 588 ASP A N 1 ATOM 4512 C CA . ASP A 1 592 ? 14.377 18.140 67.373 1.00 34.99 ? 588 ASP A CA 1 ATOM 4513 C C . ASP A 1 592 ? 13.736 19.213 66.444 1.00 32.85 ? 588 ASP A C 1 ATOM 4514 O O . ASP A 1 592 ? 14.051 20.401 66.539 1.00 31.65 ? 588 ASP A O 1 ATOM 4515 C CB . ASP A 1 592 ? 15.206 18.781 68.500 1.00 34.31 ? 588 ASP A CB 1 ATOM 4516 C CG . ASP A 1 592 ? 14.392 19.677 69.418 1.00 33.96 ? 588 ASP A CG 1 ATOM 4517 O OD1 . ASP A 1 592 ? 13.172 19.519 69.564 1.00 35.41 ? 588 ASP A OD1 1 ATOM 4518 O OD2 . ASP A 1 592 ? 14.986 20.585 70.021 1.00 38.59 ? 588 ASP A OD2 1 ATOM 4519 N N . PRO A 1 593 ? 12.850 18.777 65.544 1.00 32.14 ? 589 PRO A N 1 ATOM 4520 C CA . PRO A 1 593 ? 12.340 19.698 64.507 1.00 31.67 ? 589 PRO A CA 1 ATOM 4521 C C . PRO A 1 593 ? 11.265 20.605 65.065 1.00 31.29 ? 589 PRO A C 1 ATOM 4522 O O . PRO A 1 593 ? 10.588 20.254 66.031 1.00 29.70 ? 589 PRO A O 1 ATOM 4523 C CB . PRO A 1 593 ? 11.710 18.752 63.484 1.00 31.84 ? 589 PRO A CB 1 ATOM 4524 C CG . PRO A 1 593 ? 11.217 17.535 64.359 1.00 33.40 ? 589 PRO A CG 1 ATOM 4525 C CD . PRO A 1 593 ? 12.367 17.386 65.362 1.00 32.73 ? 589 PRO A CD 1 ATOM 4526 N N . LEU A 1 594 ? 11.057 21.751 64.429 1.00 31.36 ? 590 LEU A N 1 ATOM 4527 C CA . LEU A 1 594 ? 9.825 22.508 64.696 1.00 29.86 ? 590 LEU A CA 1 ATOM 4528 C C . LEU A 1 594 ? 8.643 21.745 64.045 1.00 29.84 ? 590 LEU A C 1 ATOM 4529 O O . LEU A 1 594 ? 7.546 21.593 64.666 1.00 29.95 ? 590 LEU A O 1 ATOM 4530 C CB . LEU A 1 594 ? 9.938 23.909 64.096 1.00 27.54 ? 590 LEU A CB 1 ATOM 4531 C CG . LEU A 1 594 ? 8.738 24.828 64.402 1.00 29.04 ? 590 LEU A CG 1 ATOM 4532 C CD1 . LEU A 1 594 ? 8.707 25.233 65.909 1.00 27.25 ? 590 LEU A CD1 1 ATOM 4533 C CD2 . LEU A 1 594 ? 8.903 26.062 63.469 1.00 27.28 ? 590 LEU A CD2 1 ATOM 4534 N N . PHE A 1 595 ? 8.853 21.292 62.795 1.00 28.19 ? 591 PHE A N 1 ATOM 4535 C CA . PHE A 1 595 ? 7.928 20.395 62.083 1.00 28.88 ? 591 PHE A CA 1 ATOM 4536 C C . PHE A 1 595 ? 8.757 19.325 61.413 1.00 29.75 ? 591 PHE A C 1 ATOM 4537 O O . PHE A 1 595 ? 9.724 19.635 60.676 1.00 29.56 ? 591 PHE A O 1 ATOM 4538 C CB . PHE A 1 595 ? 7.122 21.124 60.978 1.00 29.62 ? 591 PHE A CB 1 ATOM 4539 C CG . PHE A 1 595 ? 6.343 22.327 61.468 1.00 28.45 ? 591 PHE A CG 1 ATOM 4540 C CD1 . PHE A 1 595 ? 5.112 22.165 62.108 1.00 28.55 ? 591 PHE A CD1 1 ATOM 4541 C CD2 . PHE A 1 595 ? 6.830 23.601 61.259 1.00 28.73 ? 591 PHE A CD2 1 ATOM 4542 C CE1 . PHE A 1 595 ? 4.365 23.297 62.569 1.00 28.95 ? 591 PHE A CE1 1 ATOM 4543 C CE2 . PHE A 1 595 ? 6.106 24.705 61.692 1.00 27.38 ? 591 PHE A CE2 1 ATOM 4544 C CZ . PHE A 1 595 ? 4.868 24.538 62.352 1.00 28.12 ? 591 PHE A CZ 1 ATOM 4545 N N . ARG A 1 596 ? 8.409 18.074 61.697 1.00 29.91 ? 592 ARG A N 1 ATOM 4546 C CA . ARG A 1 596 ? 9.076 16.903 61.114 1.00 30.91 ? 592 ARG A CA 1 ATOM 4547 C C . ARG A 1 596 ? 8.758 16.743 59.629 1.00 29.21 ? 592 ARG A C 1 ATOM 4548 O O . ARG A 1 596 ? 7.703 17.160 59.134 1.00 27.55 ? 592 ARG A O 1 ATOM 4549 C CB . ARG A 1 596 ? 8.624 15.617 61.818 1.00 31.29 ? 592 ARG A CB 1 ATOM 4550 C CG . ARG A 1 596 ? 7.139 15.391 61.675 1.00 37.16 ? 592 ARG A CG 1 ATOM 4551 C CD . ARG A 1 596 ? 6.612 14.058 62.235 1.00 47.98 ? 592 ARG A CD 1 ATOM 4552 N NE . ARG A 1 596 ? 6.262 13.258 61.065 1.00 59.79 ? 592 ARG A NE 1 ATOM 4553 C CZ . ARG A 1 596 ? 5.066 13.239 60.463 1.00 60.61 ? 592 ARG A CZ 1 ATOM 4554 N NH1 . ARG A 1 596 ? 4.918 12.486 59.375 1.00 58.61 ? 592 ARG A NH1 1 ATOM 4555 N NH2 . ARG A 1 596 ? 4.024 13.942 60.954 1.00 61.89 ? 592 ARG A NH2 1 ATOM 4556 N N . LEU A 1 597 ? 9.658 16.080 58.934 1.00 28.25 ? 593 LEU A N 1 ATOM 4557 C CA . LEU A 1 597 ? 9.386 15.711 57.547 1.00 28.36 ? 593 LEU A CA 1 ATOM 4558 C C . LEU A 1 597 ? 8.089 14.903 57.502 1.00 28.86 ? 593 LEU A C 1 ATOM 4559 O O . LEU A 1 597 ? 7.864 14.062 58.395 1.00 27.77 ? 593 LEU A O 1 ATOM 4560 C CB . LEU A 1 597 ? 10.570 14.913 56.971 1.00 28.74 ? 593 LEU A CB 1 ATOM 4561 C CG . LEU A 1 597 ? 10.403 14.567 55.480 1.00 27.25 ? 593 LEU A CG 1 ATOM 4562 C CD1 . LEU A 1 597 ? 11.781 14.586 54.811 1.00 31.47 ? 593 LEU A CD1 1 ATOM 4563 C CD2 . LEU A 1 597 ? 9.729 13.225 55.320 1.00 33.29 ? 593 LEU A CD2 1 ATOM 4564 N N . GLY A 1 598 ? 7.219 15.194 56.519 1.00 26.77 ? 594 GLY A N 1 ATOM 4565 C CA . GLY A 1 598 ? 5.903 14.584 56.419 1.00 26.51 ? 594 GLY A CA 1 ATOM 4566 C C . GLY A 1 598 ? 4.754 15.338 57.099 1.00 25.72 ? 594 GLY A C 1 ATOM 4567 O O . GLY A 1 598 ? 3.592 15.028 56.853 1.00 26.90 ? 594 GLY A O 1 ATOM 4568 N N . TYR A 1 599 ? 5.052 16.329 57.917 1.00 25.44 ? 595 TYR A N 1 ATOM 4569 C CA . TYR A 1 599 ? 4.003 17.108 58.590 1.00 27.15 ? 595 TYR A CA 1 ATOM 4570 C C . TYR A 1 599 ? 3.171 17.900 57.563 1.00 28.27 ? 595 TYR A C 1 ATOM 4571 O O . TYR A 1 599 ? 3.731 18.509 56.650 1.00 26.32 ? 595 TYR A O 1 ATOM 4572 C CB . TYR A 1 599 ? 4.642 18.107 59.566 1.00 27.19 ? 595 TYR A CB 1 ATOM 4573 C CG . TYR A 1 599 ? 3.658 19.015 60.270 1.00 29.74 ? 595 TYR A CG 1 ATOM 4574 C CD1 . TYR A 1 599 ? 3.338 20.253 59.735 1.00 30.97 ? 595 TYR A CD1 1 ATOM 4575 C CD2 . TYR A 1 599 ? 3.059 18.646 61.489 1.00 31.03 ? 595 TYR A CD2 1 ATOM 4576 C CE1 . TYR A 1 599 ? 2.432 21.111 60.378 1.00 33.63 ? 595 TYR A CE1 1 ATOM 4577 C CE2 . TYR A 1 599 ? 2.128 19.542 62.153 1.00 32.42 ? 595 TYR A CE2 1 ATOM 4578 C CZ . TYR A 1 599 ? 1.825 20.741 61.562 1.00 33.73 ? 595 TYR A CZ 1 ATOM 4579 O OH . TYR A 1 599 ? 0.925 21.642 62.138 1.00 39.15 ? 595 TYR A OH 1 ATOM 4580 N N . GLY A 1 600 ? 1.850 17.947 57.724 1.00 26.74 ? 596 GLY A N 1 ATOM 4581 C CA . GLY A 1 600 ? 1.104 18.944 56.942 1.00 26.34 ? 596 GLY A CA 1 ATOM 4582 C C . GLY A 1 600 ? -0.342 18.810 57.412 1.00 27.23 ? 596 GLY A C 1 ATOM 4583 O O . GLY A 1 600 ? -0.872 17.691 57.484 1.00 27.00 ? 596 GLY A O 1 ATOM 4584 N N . LEU A 1 601 ? -0.944 19.920 57.813 1.00 25.68 ? 597 LEU A N 1 ATOM 4585 C CA . LEU A 1 601 ? -2.391 19.924 58.100 1.00 26.61 ? 597 LEU A CA 1 ATOM 4586 C C . LEU A 1 601 ? -3.190 19.757 56.832 1.00 27.36 ? 597 LEU A C 1 ATOM 4587 O O . LEU A 1 601 ? -2.691 19.995 55.709 1.00 26.66 ? 597 LEU A O 1 ATOM 4588 C CB . LEU A 1 601 ? -2.799 21.222 58.841 1.00 25.19 ? 597 LEU A CB 1 ATOM 4589 C CG . LEU A 1 601 ? -1.952 21.558 60.079 1.00 27.26 ? 597 LEU A CG 1 ATOM 4590 C CD1 . LEU A 1 601 ? -2.492 22.835 60.748 1.00 28.07 ? 597 LEU A CD1 1 ATOM 4591 C CD2 . LEU A 1 601 ? -2.063 20.316 61.041 1.00 30.40 ? 597 LEU A CD2 1 ATOM 4592 N N . THR A 1 602 ? -4.454 19.373 56.976 1.00 27.40 ? 598 THR A N 1 ATOM 4593 C CA . THR A 1 602 ? -5.306 19.230 55.808 1.00 28.23 ? 598 THR A CA 1 ATOM 4594 C C . THR A 1 602 ? -6.595 20.056 55.984 1.00 29.26 ? 598 THR A C 1 ATOM 4595 O O . THR A 1 602 ? -6.912 20.543 57.089 1.00 29.58 ? 598 THR A O 1 ATOM 4596 C CB . THR A 1 602 ? -5.677 17.749 55.593 1.00 30.09 ? 598 THR A CB 1 ATOM 4597 O OG1 . THR A 1 602 ? -6.372 17.274 56.741 1.00 29.43 ? 598 THR A OG1 1 ATOM 4598 C CG2 . THR A 1 602 ? -4.391 16.840 55.399 1.00 30.37 ? 598 THR A CG2 1 ATOM 4599 N N . THR A 1 603 ? -7.315 20.248 54.885 1.00 29.90 ? 599 THR A N 1 ATOM 4600 C CA . THR A 1 603 ? -8.640 20.816 54.903 1.00 29.54 ? 599 THR A CA 1 ATOM 4601 C C . THR A 1 603 ? -9.436 19.981 53.940 1.00 31.49 ? 599 THR A C 1 ATOM 4602 O O . THR A 1 603 ? -8.868 19.203 53.132 1.00 31.42 ? 599 THR A O 1 ATOM 4603 C CB . THR A 1 603 ? -8.694 22.286 54.417 1.00 29.56 ? 599 THR A CB 1 ATOM 4604 O OG1 . THR A 1 603 ? -8.096 22.384 53.103 1.00 27.79 ? 599 THR A OG1 1 ATOM 4605 C CG2 . THR A 1 603 ? -7.950 23.221 55.387 1.00 26.41 ? 599 THR A CG2 1 ATOM 4606 N N . ASN A 1 604 ? -10.743 20.122 54.031 1.00 33.80 ? 600 ASN A N 1 ATOM 4607 C CA . ASN A 1 604 ? -11.656 19.526 53.047 1.00 37.45 ? 600 ASN A CA 1 ATOM 4608 C C . ASN A 1 604 ? -12.161 20.581 52.055 1.00 37.62 ? 600 ASN A C 1 ATOM 4609 O O . ASN A 1 604 ? -12.381 21.721 52.464 1.00 37.67 ? 600 ASN A O 1 ATOM 4610 C CB . ASN A 1 604 ? -12.844 18.900 53.767 1.00 37.88 ? 600 ASN A CB 1 ATOM 4611 C CG . ASN A 1 604 ? -12.414 17.743 54.680 1.00 44.85 ? 600 ASN A CG 1 ATOM 4612 O OD1 . ASN A 1 604 ? -11.447 17.046 54.383 1.00 49.26 ? 600 ASN A OD1 1 ATOM 4613 N ND2 . ASN A 1 604 ? -13.114 17.550 55.778 1.00 52.96 ? 600 ASN A ND2 1 ATOM 4614 N N . ALA A 1 605 ? -12.389 20.195 50.794 1.00 38.75 ? 601 ALA A N 1 ATOM 4615 C CA . ALA A 1 605 ? -12.934 21.138 49.803 1.00 41.41 ? 601 ALA A CA 1 ATOM 4616 C C . ALA A 1 605 ? -14.314 21.657 50.227 1.00 43.80 ? 601 ALA A C 1 ATOM 4617 O O . ALA A 1 605 ? -15.081 20.914 50.853 1.00 43.35 ? 601 ALA A O 1 ATOM 4618 C CB . ALA A 1 605 ? -13.003 20.527 48.445 1.00 40.61 ? 601 ALA A CB 1 ATOM 4619 N N . THR A 1 606 ? -14.561 22.945 49.955 1.00 45.80 ? 602 THR A N 1 ATOM 4620 C CA . THR A 1 606 ? -15.906 23.542 49.867 1.00 48.66 ? 602 THR A CA 1 ATOM 4621 C C . THR A 1 606 ? -16.546 23.196 48.531 1.00 49.92 ? 602 THR A C 1 ATOM 4622 O O . THR A 1 606 ? -16.620 22.004 48.127 1.00 52.94 ? 602 THR A O 1 ATOM 4623 C CB . THR A 1 606 ? -15.866 25.095 49.891 1.00 49.13 ? 602 THR A CB 1 ATOM 4624 O OG1 . THR A 1 606 ? -14.839 25.579 50.750 1.00 48.21 ? 602 THR A OG1 1 ATOM 4625 C CG2 . THR A 1 606 ? -17.202 25.675 50.367 1.00 51.74 ? 602 THR A CG2 1 HETATM 4626 C C1 . NAG B 2 . ? 34.953 25.434 50.376 1.00 44.10 ? 701 NAG A C1 1 HETATM 4627 C C2 . NAG B 2 . ? 36.148 25.211 49.434 1.00 47.20 ? 701 NAG A C2 1 HETATM 4628 C C3 . NAG B 2 . ? 37.429 25.842 49.991 1.00 52.97 ? 701 NAG A C3 1 HETATM 4629 C C4 . NAG B 2 . ? 37.198 27.325 50.261 1.00 55.34 ? 701 NAG A C4 1 HETATM 4630 C C5 . NAG B 2 . ? 35.945 27.483 51.147 1.00 54.53 ? 701 NAG A C5 1 HETATM 4631 C C6 . NAG B 2 . ? 35.616 28.952 51.409 1.00 55.07 ? 701 NAG A C6 1 HETATM 4632 C C7 . NAG B 2 . ? 36.051 23.150 48.142 1.00 45.92 ? 701 NAG A C7 1 HETATM 4633 C C8 . NAG B 2 . ? 36.440 21.715 48.088 1.00 44.63 ? 701 NAG A C8 1 HETATM 4634 N N2 . NAG B 2 . ? 36.426 23.821 49.225 1.00 44.14 ? 701 NAG A N2 1 HETATM 4635 O O3 . NAG B 2 . ? 38.437 25.728 49.008 1.00 56.17 ? 701 NAG A O3 1 HETATM 4636 O O4 . NAG B 2 . ? 38.366 27.891 50.822 1.00 57.55 ? 701 NAG A O4 1 HETATM 4637 O O5 . NAG B 2 . ? 34.831 26.838 50.508 1.00 49.21 ? 701 NAG A O5 1 HETATM 4638 O O6 . NAG B 2 . ? 35.103 29.567 50.237 1.00 58.84 ? 701 NAG A O6 1 HETATM 4639 O O7 . NAG B 2 . ? 35.395 23.624 47.217 1.00 45.53 ? 701 NAG A O7 1 HETATM 4640 C C1 . NAG C 2 . ? 21.475 36.349 55.953 1.00 55.02 ? 702 NAG A C1 1 HETATM 4641 C C2 . NAG C 2 . ? 21.440 37.866 56.155 1.00 60.33 ? 702 NAG A C2 1 HETATM 4642 C C3 . NAG C 2 . ? 21.410 38.652 54.843 1.00 61.23 ? 702 NAG A C3 1 HETATM 4643 C C4 . NAG C 2 . ? 22.373 38.062 53.820 1.00 61.38 ? 702 NAG A C4 1 HETATM 4644 C C5 . NAG C 2 . ? 22.089 36.553 53.710 1.00 59.92 ? 702 NAG A C5 1 HETATM 4645 C C6 . NAG C 2 . ? 22.752 35.766 52.562 1.00 59.33 ? 702 NAG A C6 1 HETATM 4646 C C7 . NAG C 2 . ? 20.478 38.314 58.326 1.00 66.17 ? 702 NAG A C7 1 HETATM 4647 C C8 . NAG C 2 . ? 19.275 38.654 59.168 1.00 65.28 ? 702 NAG A C8 1 HETATM 4648 N N2 . NAG C 2 . ? 20.309 38.199 57.002 1.00 61.80 ? 702 NAG A N2 1 HETATM 4649 O O3 . NAG C 2 . ? 21.714 40.009 55.099 1.00 63.09 ? 702 NAG A O3 1 HETATM 4650 O O4 . NAG C 2 . ? 22.202 38.741 52.589 1.00 63.86 ? 702 NAG A O4 1 HETATM 4651 O O5 . NAG C 2 . ? 22.412 35.977 54.960 1.00 57.80 ? 702 NAG A O5 1 HETATM 4652 O O6 . NAG C 2 . ? 24.126 35.490 52.761 1.00 56.33 ? 702 NAG A O6 1 HETATM 4653 O O7 . NAG C 2 . ? 21.580 38.141 58.871 1.00 67.75 ? 702 NAG A O7 1 HETATM 4654 C C1 . NAG D 2 . ? -12.772 16.504 56.721 1.00 58.45 ? 703 NAG A C1 1 HETATM 4655 C C2 . NAG D 2 . ? -13.304 16.756 58.132 1.00 64.01 ? 703 NAG A C2 1 HETATM 4656 C C3 . NAG D 2 . ? -12.840 15.662 59.100 1.00 67.07 ? 703 NAG A C3 1 HETATM 4657 C C4 . NAG D 2 . ? -13.179 14.278 58.541 1.00 68.03 ? 703 NAG A C4 1 HETATM 4658 C C5 . NAG D 2 . ? -12.728 14.157 57.084 1.00 66.95 ? 703 NAG A C5 1 HETATM 4659 C C6 . NAG D 2 . ? -13.196 12.828 56.499 1.00 68.71 ? 703 NAG A C6 1 HETATM 4660 C C7 . NAG D 2 . ? -13.808 19.137 58.327 1.00 61.77 ? 703 NAG A C7 1 HETATM 4661 C C8 . NAG D 2 . ? -13.484 20.488 58.894 1.00 62.67 ? 703 NAG A C8 1 HETATM 4662 N N2 . NAG D 2 . ? -13.018 18.105 58.653 1.00 63.80 ? 703 NAG A N2 1 HETATM 4663 O O3 . NAG D 2 . ? -13.510 15.881 60.334 1.00 69.86 ? 703 NAG A O3 1 HETATM 4664 O O4 . NAG D 2 . ? -12.609 13.240 59.328 1.00 69.78 ? 703 NAG A O4 1 HETATM 4665 O O5 . NAG D 2 . ? -13.233 15.236 56.298 1.00 63.38 ? 703 NAG A O5 1 HETATM 4666 O O6 . NAG D 2 . ? -14.527 12.958 56.061 1.00 71.37 ? 703 NAG A O6 1 HETATM 4667 O O7 . NAG D 2 . ? -14.767 19.004 57.575 1.00 60.03 ? 703 NAG A O7 1 HETATM 4668 C C1 . GOL E 3 . ? 51.755 15.085 30.748 1.00 64.68 ? 704 GOL A C1 1 HETATM 4669 O O1 . GOL E 3 . ? 50.740 14.528 31.587 1.00 60.37 ? 704 GOL A O1 1 HETATM 4670 C C2 . GOL E 3 . ? 51.244 16.273 29.932 1.00 65.25 ? 704 GOL A C2 1 HETATM 4671 O O2 . GOL E 3 . ? 52.249 16.806 29.082 1.00 66.28 ? 704 GOL A O2 1 HETATM 4672 C C3 . GOL E 3 . ? 50.799 17.351 30.881 1.00 65.87 ? 704 GOL A C3 1 HETATM 4673 O O3 . GOL E 3 . ? 50.463 16.721 32.093 1.00 69.35 ? 704 GOL A O3 1 HETATM 4674 C C1 . GOL F 3 . ? 39.214 29.961 43.990 1.00 73.35 ? 705 GOL A C1 1 HETATM 4675 O O1 . GOL F 3 . ? 39.944 28.821 43.642 1.00 70.23 ? 705 GOL A O1 1 HETATM 4676 C C2 . GOL F 3 . ? 39.603 31.058 43.028 1.00 75.85 ? 705 GOL A C2 1 HETATM 4677 O O2 . GOL F 3 . ? 39.102 32.287 43.516 1.00 78.47 ? 705 GOL A O2 1 HETATM 4678 C C3 . GOL F 3 . ? 38.979 30.769 41.671 1.00 76.81 ? 705 GOL A C3 1 HETATM 4679 O O3 . GOL F 3 . ? 37.565 30.799 41.741 1.00 79.95 ? 705 GOL A O3 1 HETATM 4680 C C1 . GOL G 3 . ? 14.586 22.974 7.724 1.00 67.49 ? 706 GOL A C1 1 HETATM 4681 O O1 . GOL G 3 . ? 13.666 23.730 8.476 1.00 67.17 ? 706 GOL A O1 1 HETATM 4682 C C2 . GOL G 3 . ? 15.559 23.906 7.011 1.00 67.33 ? 706 GOL A C2 1 HETATM 4683 O O2 . GOL G 3 . ? 16.534 23.102 6.384 1.00 70.27 ? 706 GOL A O2 1 HETATM 4684 C C3 . GOL G 3 . ? 16.241 24.847 7.999 1.00 68.09 ? 706 GOL A C3 1 HETATM 4685 O O3 . GOL G 3 . ? 15.287 25.654 8.660 1.00 67.27 ? 706 GOL A O3 1 HETATM 4686 C C1 . GOL H 3 . ? 6.113 9.702 51.592 1.00 57.76 ? 707 GOL A C1 1 HETATM 4687 O O1 . GOL H 3 . ? 7.360 10.309 51.713 1.00 54.17 ? 707 GOL A O1 1 HETATM 4688 C C2 . GOL H 3 . ? 5.583 9.511 53.010 1.00 59.28 ? 707 GOL A C2 1 HETATM 4689 O O2 . GOL H 3 . ? 4.280 8.998 52.840 1.00 62.04 ? 707 GOL A O2 1 HETATM 4690 C C3 . GOL H 3 . ? 5.526 10.819 53.815 1.00 57.61 ? 707 GOL A C3 1 HETATM 4691 O O3 . GOL H 3 . ? 6.760 11.358 54.280 1.00 52.58 ? 707 GOL A O3 1 HETATM 4692 C C1 . GOL I 3 . ? -8.558 16.745 43.379 1.00 62.06 ? 708 GOL A C1 1 HETATM 4693 O O1 . GOL I 3 . ? -9.804 16.095 43.478 1.00 61.28 ? 708 GOL A O1 1 HETATM 4694 C C2 . GOL I 3 . ? -7.656 16.071 42.353 1.00 62.15 ? 708 GOL A C2 1 HETATM 4695 O O2 . GOL I 3 . ? -6.377 16.187 42.878 1.00 62.70 ? 708 GOL A O2 1 HETATM 4696 C C3 . GOL I 3 . ? -7.682 16.752 40.987 1.00 61.05 ? 708 GOL A C3 1 HETATM 4697 O O3 . GOL I 3 . ? -6.470 17.429 40.777 1.00 58.59 ? 708 GOL A O3 1 HETATM 4698 C C1 . GOL J 3 . ? 17.811 35.144 50.969 1.00 58.57 ? 709 GOL A C1 1 HETATM 4699 O O1 . GOL J 3 . ? 16.933 34.202 51.570 1.00 60.06 ? 709 GOL A O1 1 HETATM 4700 C C2 . GOL J 3 . ? 18.666 34.503 49.869 1.00 54.96 ? 709 GOL A C2 1 HETATM 4701 O O2 . GOL J 3 . ? 19.739 33.863 50.471 1.00 47.78 ? 709 GOL A O2 1 HETATM 4702 C C3 . GOL J 3 . ? 19.219 35.546 48.910 1.00 55.36 ? 709 GOL A C3 1 HETATM 4703 O O3 . GOL J 3 . ? 18.158 36.393 48.524 1.00 59.90 ? 709 GOL A O3 1 HETATM 4704 S S . SO4 K 4 . ? 45.568 4.312 21.867 0.50 28.46 ? 710 SO4 A S 1 HETATM 4705 O O1 . SO4 K 4 . ? 46.515 3.585 22.699 0.50 27.86 ? 710 SO4 A O1 1 HETATM 4706 O O2 . SO4 K 4 . ? 46.006 5.726 21.908 0.50 22.97 ? 710 SO4 A O2 1 HETATM 4707 O O3 . SO4 K 4 . ? 45.522 3.780 20.521 0.50 22.59 ? 710 SO4 A O3 1 HETATM 4708 O O4 . SO4 K 4 . ? 44.175 4.097 22.313 0.50 22.72 ? 710 SO4 A O4 1 HETATM 4709 C C1 . GOL L 3 . ? 39.831 10.364 7.903 1.00 57.22 ? 711 GOL A C1 1 HETATM 4710 O O1 . GOL L 3 . ? 40.865 10.503 8.858 1.00 60.68 ? 711 GOL A O1 1 HETATM 4711 C C2 . GOL L 3 . ? 39.651 8.877 7.637 1.00 58.21 ? 711 GOL A C2 1 HETATM 4712 O O2 . GOL L 3 . ? 38.535 8.701 6.805 1.00 57.77 ? 711 GOL A O2 1 HETATM 4713 C C3 . GOL L 3 . ? 39.354 8.132 8.931 1.00 58.99 ? 711 GOL A C3 1 HETATM 4714 O O3 . GOL L 3 . ? 40.433 8.324 9.808 1.00 60.52 ? 711 GOL A O3 1 HETATM 4715 C C1 . GOL M 3 . ? 31.104 0.411 23.867 1.00 72.16 ? 712 GOL A C1 1 HETATM 4716 O O1 . GOL M 3 . ? 30.509 0.632 22.598 1.00 73.18 ? 712 GOL A O1 1 HETATM 4717 C C2 . GOL M 3 . ? 30.099 -0.100 24.900 1.00 71.48 ? 712 GOL A C2 1 HETATM 4718 O O2 . GOL M 3 . ? 30.422 0.431 26.169 1.00 67.05 ? 712 GOL A O2 1 HETATM 4719 C C3 . GOL M 3 . ? 30.167 -1.621 24.963 1.00 73.67 ? 712 GOL A C3 1 HETATM 4720 O O3 . GOL M 3 . ? 31.162 -2.025 25.888 1.00 75.54 ? 712 GOL A O3 1 HETATM 4721 C C1 . GOL N 3 . ? 30.907 -2.394 30.127 1.00 67.26 ? 713 GOL A C1 1 HETATM 4722 O O1 . GOL N 3 . ? 31.311 -2.283 31.479 1.00 66.31 ? 713 GOL A O1 1 HETATM 4723 C C2 . GOL N 3 . ? 30.000 -3.589 29.794 1.00 68.55 ? 713 GOL A C2 1 HETATM 4724 O O2 . GOL N 3 . ? 28.742 -3.153 29.323 1.00 68.06 ? 713 GOL A O2 1 HETATM 4725 C C3 . GOL N 3 . ? 29.819 -4.600 30.928 1.00 69.49 ? 713 GOL A C3 1 HETATM 4726 O O3 . GOL N 3 . ? 28.840 -5.570 30.582 1.00 71.86 ? 713 GOL A O3 1 HETATM 4727 C C1 . GOL O 3 . ? -19.867 21.468 47.297 1.00 95.52 ? 714 GOL A C1 1 HETATM 4728 O O1 . GOL O 3 . ? -19.284 20.907 48.456 1.00 96.22 ? 714 GOL A O1 1 HETATM 4729 C C2 . GOL O 3 . ? -20.724 22.670 47.692 1.00 95.60 ? 714 GOL A C2 1 HETATM 4730 O O2 . GOL O 3 . ? -20.029 23.495 48.601 1.00 95.40 ? 714 GOL A O2 1 HETATM 4731 C C3 . GOL O 3 . ? -21.235 23.472 46.489 1.00 95.60 ? 714 GOL A C3 1 HETATM 4732 O O3 . GOL O 3 . ? -20.204 23.803 45.578 1.00 95.30 ? 714 GOL A O3 1 HETATM 4733 C C1 . GOL P 3 . ? 19.194 4.081 56.192 1.00 94.30 ? 715 GOL A C1 1 HETATM 4734 O O1 . GOL P 3 . ? 18.255 4.745 57.007 1.00 93.64 ? 715 GOL A O1 1 HETATM 4735 C C2 . GOL P 3 . ? 18.471 3.303 55.095 1.00 94.58 ? 715 GOL A C2 1 HETATM 4736 O O2 . GOL P 3 . ? 17.572 4.147 54.416 1.00 93.46 ? 715 GOL A O2 1 HETATM 4737 C C3 . GOL P 3 . ? 17.718 2.126 55.707 1.00 95.76 ? 715 GOL A C3 1 HETATM 4738 O O3 . GOL P 3 . ? 17.005 1.422 54.708 1.00 97.34 ? 715 GOL A O3 1 HETATM 4739 C C1 . GOL Q 3 . ? 10.571 21.777 8.047 1.00 69.84 ? 716 GOL A C1 1 HETATM 4740 O O1 . GOL Q 3 . ? 9.841 22.949 8.393 1.00 67.09 ? 716 GOL A O1 1 HETATM 4741 C C2 . GOL Q 3 . ? 11.540 21.333 9.151 1.00 69.33 ? 716 GOL A C2 1 HETATM 4742 O O2 . GOL Q 3 . ? 12.558 20.467 8.656 1.00 69.87 ? 716 GOL A O2 1 HETATM 4743 C C3 . GOL Q 3 . ? 10.769 20.634 10.258 1.00 67.36 ? 716 GOL A C3 1 HETATM 4744 O O3 . GOL Q 3 . ? 11.691 20.145 11.203 1.00 64.19 ? 716 GOL A O3 1 HETATM 4745 C C1 . GOL R 3 . ? -2.609 34.571 32.636 1.00 53.96 ? 717 GOL A C1 1 HETATM 4746 O O1 . GOL R 3 . ? -2.019 35.837 32.391 1.00 50.29 ? 717 GOL A O1 1 HETATM 4747 C C2 . GOL R 3 . ? -1.795 33.472 31.969 1.00 46.98 ? 717 GOL A C2 1 HETATM 4748 O O2 . GOL R 3 . ? -2.585 32.829 30.967 1.00 54.95 ? 717 GOL A O2 1 HETATM 4749 C C3 . GOL R 3 . ? -1.289 32.484 32.998 1.00 45.64 ? 717 GOL A C3 1 HETATM 4750 O O3 . GOL R 3 . ? -1.566 32.618 34.378 1.00 31.22 ? 717 GOL A O3 1 HETATM 4751 C C1 . GOL S 3 . ? 4.924 19.233 65.598 1.00 61.93 ? 718 GOL A C1 1 HETATM 4752 O O1 . GOL S 3 . ? 3.683 19.934 65.641 1.00 66.11 ? 718 GOL A O1 1 HETATM 4753 C C2 . GOL S 3 . ? 4.841 18.025 64.648 1.00 62.11 ? 718 GOL A C2 1 HETATM 4754 O O2 . GOL S 3 . ? 4.921 16.802 65.355 1.00 65.18 ? 718 GOL A O2 1 HETATM 4755 C C3 . GOL S 3 . ? 6.093 17.959 63.840 1.00 53.71 ? 718 GOL A C3 1 HETATM 4756 O O3 . GOL S 3 . ? 6.980 17.895 64.918 1.00 52.47 ? 718 GOL A O3 1 HETATM 4757 C C1 . GS1 T 5 . ? 25.897 25.783 36.174 0.80 21.02 ? 719 GS1 A C1 1 HETATM 4758 S S1 . GS1 T 5 . ? 26.161 27.359 36.984 0.80 24.18 ? 719 GS1 A S1 1 HETATM 4759 C C2 . GS1 T 5 . ? 24.899 24.951 37.031 0.80 19.39 ? 719 GS1 A C2 1 HETATM 4760 O O2 . GS1 T 5 . ? 25.605 24.374 38.133 0.80 18.69 ? 719 GS1 A O2 1 HETATM 4761 C C3 . GS1 T 5 . ? 24.207 23.849 36.187 0.80 18.07 ? 719 GS1 A C3 1 HETATM 4762 O O3 . GS1 T 5 . ? 23.123 23.203 36.959 0.80 18.46 ? 719 GS1 A O3 1 HETATM 4763 C C4 . GS1 T 5 . ? 23.719 24.386 34.813 0.80 20.24 ? 719 GS1 A C4 1 HETATM 4764 O O4 . GS1 T 5 . ? 23.126 23.318 34.064 0.80 18.82 ? 719 GS1 A O4 1 HETATM 4765 C C5 . GS1 T 5 . ? 24.874 25.110 34.070 0.80 19.36 ? 719 GS1 A C5 1 HETATM 4766 O O5 . GS1 T 5 . ? 25.328 26.162 34.934 0.80 20.76 ? 719 GS1 A O5 1 HETATM 4767 C C6 . GS1 T 5 . ? 24.678 25.755 32.695 0.80 21.36 ? 719 GS1 A C6 1 HETATM 4768 O O6 . GS1 T 5 . ? 23.512 26.622 32.741 0.80 19.75 ? 719 GS1 A O6 1 HETATM 4769 C C1 . MGL U 6 . ? 26.193 30.747 33.678 0.80 44.71 ? 720 MGL A C1 1 HETATM 4770 C C2 . MGL U 6 . ? 26.387 32.021 34.495 0.80 48.34 ? 720 MGL A C2 1 HETATM 4771 C C3 . MGL U 6 . ? 27.172 31.644 35.762 0.80 49.39 ? 720 MGL A C3 1 HETATM 4772 C C4 . MGL U 6 . ? 26.606 30.492 36.562 0.80 48.70 ? 720 MGL A C4 1 HETATM 4773 C C5 . MGL U 6 . ? 25.887 29.461 35.705 0.80 46.85 ? 720 MGL A C5 1 HETATM 4774 C C6 . MGL U 6 . ? 24.940 28.551 36.485 0.80 39.09 ? 720 MGL A C6 1 HETATM 4775 C C7 . MGL U 6 . ? 24.823 32.015 32.042 0.80 41.76 ? 720 MGL A C7 1 HETATM 4776 O O1 . MGL U 6 . ? 25.436 30.741 32.487 0.80 43.81 ? 720 MGL A O1 1 HETATM 4777 O O2 . MGL U 6 . ? 27.006 33.008 33.655 0.80 48.46 ? 720 MGL A O2 1 HETATM 4778 O O3 . MGL U 6 . ? 27.091 32.697 36.711 0.80 50.75 ? 720 MGL A O3 1 HETATM 4779 O O4 . MGL U 6 . ? 27.765 29.905 37.153 0.80 53.58 ? 720 MGL A O4 1 HETATM 4780 O O5 . MGL U 6 . ? 25.353 29.868 34.431 0.80 48.49 ? 720 MGL A O5 1 HETATM 4781 O O . HOH V 7 . ? 27.202 28.319 35.877 0.20 3.24 ? 801 HOH A O 1 HETATM 4782 O O . HOH V 7 . ? 24.105 25.081 32.195 0.20 14.40 ? 802 HOH A O 1 HETATM 4783 O O . HOH V 7 . ? 27.841 31.854 38.051 0.20 18.23 ? 803 HOH A O 1 HETATM 4784 O O . HOH V 7 . ? 26.311 30.526 36.311 0.20 3.40 ? 804 HOH A O 1 HETATM 4785 O O . HOH V 7 . ? 23.846 28.955 33.777 1.00 20.78 ? 805 HOH A O 1 HETATM 4786 O O . HOH V 7 . ? 29.124 29.152 37.745 1.00 40.02 ? 806 HOH A O 1 HETATM 4787 O O . HOH V 7 . ? 22.803 24.887 35.126 0.20 14.10 ? 807 HOH A O 1 HETATM 4788 O O . HOH V 7 . ? 45.821 5.489 20.952 0.50 27.97 ? 808 HOH A O 1 HETATM 4789 O O . HOH V 7 . ? -9.456 15.171 58.484 1.00 67.23 ? 809 HOH A O 1 HETATM 4790 O O . HOH V 7 . ? -0.236 21.218 64.331 1.00 47.65 ? 810 HOH A O 1 HETATM 4791 O O . HOH V 7 . ? 14.034 18.157 8.807 1.00 59.29 ? 811 HOH A O 1 HETATM 4792 O O . HOH V 7 . ? 44.536 6.620 15.467 1.00 59.61 ? 812 HOH A O 1 HETATM 4793 O O . HOH V 7 . ? -2.481 16.121 59.362 1.00 39.75 ? 813 HOH A O 1 HETATM 4794 O O . HOH V 7 . ? 9.583 13.567 64.757 1.00 47.96 ? 814 HOH A O 1 HETATM 4795 O O . HOH V 7 . ? 23.776 12.148 64.414 1.00 69.46 ? 815 HOH A O 1 HETATM 4796 O O . HOH V 7 . ? 26.191 15.607 58.984 1.00 59.25 ? 816 HOH A O 1 HETATM 4797 O O . HOH V 7 . ? 27.419 12.997 57.319 1.00 54.99 ? 817 HOH A O 1 HETATM 4798 O O . HOH V 7 . ? 6.970 23.262 68.611 1.00 46.39 ? 818 HOH A O 1 HETATM 4799 O O . HOH V 7 . ? -7.159 17.139 52.171 1.00 32.11 ? 819 HOH A O 1 HETATM 4800 O O . HOH V 7 . ? 3.229 30.452 67.941 1.00 38.74 ? 820 HOH A O 1 HETATM 4801 O O . HOH V 7 . ? 13.634 34.904 65.756 1.00 54.74 ? 821 HOH A O 1 HETATM 4802 O O . HOH V 7 . ? 17.496 31.170 68.316 1.00 65.83 ? 822 HOH A O 1 HETATM 4803 O O . HOH V 7 . ? -3.124 54.140 65.803 1.00 44.24 ? 823 HOH A O 1 HETATM 4804 O O . HOH V 7 . ? -0.721 55.286 61.424 1.00 43.14 ? 824 HOH A O 1 HETATM 4805 O O . HOH V 7 . ? -24.386 36.269 46.078 1.00 66.65 ? 825 HOH A O 1 HETATM 4806 O O . HOH V 7 . ? -8.302 45.566 38.735 1.00 53.21 ? 826 HOH A O 1 HETATM 4807 O O . HOH V 7 . ? 21.118 35.088 34.189 1.00 33.24 ? 827 HOH A O 1 HETATM 4808 O O . HOH V 7 . ? 5.776 43.560 41.477 1.00 34.93 ? 828 HOH A O 1 HETATM 4809 O O . HOH V 7 . ? 3.873 45.562 35.237 1.00 60.44 ? 829 HOH A O 1 HETATM 4810 O O . HOH V 7 . ? -18.577 33.539 45.140 1.00 45.72 ? 830 HOH A O 1 HETATM 4811 O O . HOH V 7 . ? -10.940 22.941 64.775 1.00 71.97 ? 831 HOH A O 1 HETATM 4812 O O . HOH V 7 . ? -9.285 22.119 62.753 1.00 62.77 ? 832 HOH A O 1 HETATM 4813 O O . HOH V 7 . ? -3.864 18.853 33.672 1.00 38.55 ? 833 HOH A O 1 HETATM 4814 O O . HOH V 7 . ? -7.399 30.240 33.309 1.00 35.25 ? 834 HOH A O 1 HETATM 4815 O O . HOH V 7 . ? 47.018 10.342 17.465 1.00 46.64 ? 835 HOH A O 1 HETATM 4816 O O . HOH V 7 . ? 46.620 8.734 19.368 1.00 40.25 ? 836 HOH A O 1 HETATM 4817 O O . HOH V 7 . ? 33.590 35.215 25.984 1.00 64.87 ? 837 HOH A O 1 HETATM 4818 O O . HOH V 7 . ? 33.017 30.907 40.302 1.00 47.85 ? 838 HOH A O 1 HETATM 4819 O O . HOH V 7 . ? 39.220 3.169 34.998 1.00 51.06 ? 839 HOH A O 1 HETATM 4820 O O . HOH V 7 . ? 43.369 4.530 34.871 1.00 46.06 ? 840 HOH A O 1 HETATM 4821 O O . HOH V 7 . ? 40.237 4.699 38.642 1.00 41.91 ? 841 HOH A O 1 HETATM 4822 O O . HOH V 7 . ? 42.055 18.890 42.303 1.00 41.28 ? 842 HOH A O 1 HETATM 4823 O O . HOH V 7 . ? 42.924 16.900 41.061 1.00 51.24 ? 843 HOH A O 1 HETATM 4824 O O . HOH V 7 . ? 13.033 -0.995 36.362 1.00 53.89 ? 844 HOH A O 1 HETATM 4825 O O . HOH V 7 . ? 16.916 1.159 42.728 1.00 52.26 ? 845 HOH A O 1 HETATM 4826 O O . HOH V 7 . ? 35.175 4.876 46.411 1.00 68.63 ? 846 HOH A O 1 HETATM 4827 O O . HOH V 7 . ? 29.511 -0.553 46.486 1.00 58.13 ? 847 HOH A O 1 HETATM 4828 O O . HOH V 7 . ? 33.882 2.842 42.098 1.00 45.33 ? 848 HOH A O 1 HETATM 4829 O O . HOH V 7 . ? 36.057 0.639 44.842 1.00 59.50 ? 849 HOH A O 1 HETATM 4830 O O . HOH V 7 . ? 35.107 4.190 54.103 1.00 49.76 ? 850 HOH A O 1 HETATM 4831 O O . HOH V 7 . ? 40.484 25.139 52.508 1.00 61.63 ? 851 HOH A O 1 HETATM 4832 O O . HOH V 7 . ? 39.334 19.886 49.127 1.00 67.29 ? 852 HOH A O 1 HETATM 4833 O O . HOH V 7 . ? 25.853 32.552 42.420 1.00 38.58 ? 853 HOH A O 1 HETATM 4834 O O . HOH V 7 . ? 34.045 20.219 57.939 1.00 49.66 ? 854 HOH A O 1 HETATM 4835 O O . HOH V 7 . ? 8.591 12.044 11.669 1.00 63.47 ? 855 HOH A O 1 HETATM 4836 O O . HOH V 7 . ? 22.549 -3.054 25.783 1.00 60.33 ? 856 HOH A O 1 HETATM 4837 O O . HOH V 7 . ? 5.712 3.715 35.550 1.00 80.49 ? 857 HOH A O 1 HETATM 4838 O O . HOH V 7 . ? 4.226 3.650 31.725 1.00 60.89 ? 858 HOH A O 1 HETATM 4839 O O . HOH V 7 . ? 12.228 1.685 36.660 1.00 43.56 ? 859 HOH A O 1 HETATM 4840 O O . HOH V 7 . ? 22.994 12.906 58.169 1.00 53.14 ? 860 HOH A O 1 HETATM 4841 O O . HOH V 7 . ? 24.880 11.808 56.945 1.00 58.67 ? 861 HOH A O 1 HETATM 4842 O O . HOH V 7 . ? 25.260 8.799 56.609 1.00 46.05 ? 862 HOH A O 1 HETATM 4843 O O . HOH V 7 . ? 18.717 8.960 54.191 1.00 35.59 ? 863 HOH A O 1 HETATM 4844 O O . HOH V 7 . ? -5.385 14.081 41.893 1.00 51.73 ? 864 HOH A O 1 HETATM 4845 O O . HOH V 7 . ? -2.662 13.217 48.658 1.00 56.65 ? 865 HOH A O 1 HETATM 4846 O O . HOH V 7 . ? -3.459 15.385 46.362 1.00 52.89 ? 866 HOH A O 1 HETATM 4847 O O . HOH V 7 . ? 17.004 29.764 10.732 1.00 39.49 ? 867 HOH A O 1 HETATM 4848 O O . HOH V 7 . ? 10.973 26.710 12.542 1.00 42.51 ? 868 HOH A O 1 HETATM 4849 O O . HOH V 7 . ? 6.108 32.633 11.265 1.00 32.86 ? 869 HOH A O 1 HETATM 4850 O O . HOH V 7 . ? 6.258 39.227 20.137 1.00 39.83 ? 870 HOH A O 1 HETATM 4851 O O . HOH V 7 . ? 3.426 34.283 25.122 1.00 37.13 ? 871 HOH A O 1 HETATM 4852 O O . HOH V 7 . ? 2.658 32.379 26.706 1.00 36.48 ? 872 HOH A O 1 HETATM 4853 O O . HOH V 7 . ? 10.233 41.225 28.613 1.00 43.68 ? 873 HOH A O 1 HETATM 4854 O O . HOH V 7 . ? 12.719 40.610 32.253 1.00 34.92 ? 874 HOH A O 1 HETATM 4855 O O . HOH V 7 . ? 8.518 41.253 26.592 1.00 54.59 ? 875 HOH A O 1 HETATM 4856 O O . HOH V 7 . ? 6.727 40.777 25.001 1.00 62.89 ? 876 HOH A O 1 HETATM 4857 O O . HOH V 7 . ? 7.643 34.013 23.915 1.00 31.40 ? 877 HOH A O 1 HETATM 4858 O O . HOH V 7 . ? 5.993 32.716 21.327 1.00 24.87 ? 878 HOH A O 1 HETATM 4859 O O . HOH V 7 . ? 6.351 32.017 17.747 1.00 23.29 ? 879 HOH A O 1 HETATM 4860 O O . HOH V 7 . ? 5.052 30.842 15.623 1.00 28.94 ? 880 HOH A O 1 HETATM 4861 O O . HOH V 7 . ? 4.346 30.322 20.722 1.00 29.08 ? 881 HOH A O 1 HETATM 4862 O O . HOH V 7 . ? 2.328 30.294 22.505 1.00 33.08 ? 882 HOH A O 1 HETATM 4863 O O . HOH V 7 . ? 6.156 28.726 14.051 1.00 26.10 ? 883 HOH A O 1 HETATM 4864 O O . HOH V 7 . ? 17.599 41.501 25.313 1.00 35.66 ? 884 HOH A O 1 HETATM 4865 O O . HOH V 7 . ? 17.022 43.898 26.869 1.00 52.69 ? 885 HOH A O 1 HETATM 4866 O O . HOH V 7 . ? 28.035 31.183 6.813 1.00 39.70 ? 886 HOH A O 1 HETATM 4867 O O . HOH V 7 . ? 30.442 32.934 10.440 1.00 37.07 ? 887 HOH A O 1 HETATM 4868 O O . HOH V 7 . ? 34.018 34.649 16.678 1.00 46.16 ? 888 HOH A O 1 HETATM 4869 O O . HOH V 7 . ? 39.111 31.580 19.411 1.00 47.51 ? 889 HOH A O 1 HETATM 4870 O O . HOH V 7 . ? 19.215 34.509 15.515 1.00 39.45 ? 890 HOH A O 1 HETATM 4871 O O . HOH V 7 . ? 23.122 36.937 28.308 1.00 38.90 ? 891 HOH A O 1 HETATM 4872 O O . HOH V 7 . ? 21.724 36.604 25.990 1.00 31.49 ? 892 HOH A O 1 HETATM 4873 O O . HOH V 7 . ? 22.271 39.247 29.606 1.00 40.45 ? 893 HOH A O 1 HETATM 4874 O O . HOH V 7 . ? 19.802 40.590 31.443 1.00 53.79 ? 894 HOH A O 1 HETATM 4875 O O . HOH V 7 . ? 19.199 39.610 27.562 1.00 31.40 ? 895 HOH A O 1 HETATM 4876 O O . HOH V 7 . ? 28.529 38.561 25.008 1.00 55.29 ? 896 HOH A O 1 HETATM 4877 O O . HOH V 7 . ? 39.748 5.852 11.843 1.00 56.43 ? 897 HOH A O 1 HETATM 4878 O O . HOH V 7 . ? 34.516 0.277 13.159 1.00 50.68 ? 898 HOH A O 1 HETATM 4879 O O . HOH V 7 . ? 25.554 -1.299 23.441 1.00 60.28 ? 899 HOH A O 1 HETATM 4880 O O . HOH V 7 . ? 25.728 -3.231 5.134 1.00 62.13 ? 900 HOH A O 1 HETATM 4881 O O . HOH V 7 . ? 19.491 -4.184 16.629 1.00 60.34 ? 901 HOH A O 1 HETATM 4882 O O . HOH V 7 . ? 12.053 9.023 12.336 1.00 41.18 ? 902 HOH A O 1 HETATM 4883 O O . HOH V 7 . ? 9.462 14.170 10.282 1.00 61.67 ? 903 HOH A O 1 HETATM 4884 O O . HOH V 7 . ? 20.657 11.156 3.919 1.00 62.53 ? 904 HOH A O 1 HETATM 4885 O O . HOH V 7 . ? 32.432 2.297 3.916 1.00 63.15 ? 905 HOH A O 1 HETATM 4886 O O . HOH V 7 . ? 28.527 -0.362 4.911 1.00 58.79 ? 906 HOH A O 1 HETATM 4887 O O . HOH V 7 . ? 25.987 4.089 -10.235 1.00 49.08 ? 907 HOH A O 1 HETATM 4888 O O . HOH V 7 . ? 28.028 5.642 -9.458 1.00 34.78 ? 908 HOH A O 1 HETATM 4889 O O . HOH V 7 . ? 28.195 9.717 -8.774 1.00 45.69 ? 909 HOH A O 1 HETATM 4890 O O . HOH V 7 . ? 25.513 32.843 29.396 1.00 26.17 ? 910 HOH A O 1 HETATM 4891 O O . HOH V 7 . ? 28.166 33.887 29.337 1.00 32.31 ? 911 HOH A O 1 HETATM 4892 O O . HOH V 7 . ? 30.653 33.679 30.598 1.00 38.78 ? 912 HOH A O 1 HETATM 4893 O O . HOH V 7 . ? 19.989 27.645 30.934 1.00 18.79 ? 913 HOH A O 1 HETATM 4894 O O . HOH V 7 . ? 16.146 30.894 33.803 1.00 17.41 ? 914 HOH A O 1 HETATM 4895 O O . HOH V 7 . ? 19.600 24.115 37.367 1.00 19.75 ? 915 HOH A O 1 HETATM 4896 O O . HOH V 7 . ? 26.778 26.196 40.937 1.00 31.20 ? 916 HOH A O 1 HETATM 4897 O O . HOH V 7 . ? 26.362 23.810 42.243 1.00 26.68 ? 917 HOH A O 1 HETATM 4898 O O . HOH V 7 . ? 27.720 21.514 42.926 1.00 27.77 ? 918 HOH A O 1 HETATM 4899 O O . HOH V 7 . ? 27.527 21.337 39.886 1.00 22.61 ? 919 HOH A O 1 HETATM 4900 O O . HOH V 7 . ? 27.233 21.927 45.670 1.00 27.59 ? 920 HOH A O 1 HETATM 4901 O O . HOH V 7 . ? 34.201 25.491 42.619 1.00 25.82 ? 921 HOH A O 1 HETATM 4902 O O . HOH V 7 . ? 7.389 25.550 30.171 1.00 17.69 ? 922 HOH A O 1 HETATM 4903 O O . HOH V 7 . ? 3.916 15.516 63.293 1.00 46.46 ? 923 HOH A O 1 HETATM 4904 O O . HOH V 7 . ? 8.779 28.444 40.403 1.00 17.31 ? 924 HOH A O 1 HETATM 4905 O O . HOH V 7 . ? 5.426 25.482 45.249 1.00 17.53 ? 925 HOH A O 1 HETATM 4906 O O . HOH V 7 . ? 2.501 37.179 43.697 1.00 17.67 ? 926 HOH A O 1 HETATM 4907 O O . HOH V 7 . ? 16.409 36.333 29.712 1.00 23.31 ? 927 HOH A O 1 HETATM 4908 O O . HOH V 7 . ? 10.585 21.942 39.182 1.00 16.79 ? 928 HOH A O 1 HETATM 4909 O O . HOH V 7 . ? 2.879 27.446 38.512 1.00 15.96 ? 929 HOH A O 1 HETATM 4910 O O . HOH V 7 . ? 27.667 18.245 15.832 1.00 19.04 ? 930 HOH A O 1 HETATM 4911 O O . HOH V 7 . ? 12.154 35.190 39.323 1.00 17.36 ? 931 HOH A O 1 HETATM 4912 O O . HOH V 7 . ? 10.204 21.027 34.373 1.00 17.82 ? 932 HOH A O 1 HETATM 4913 O O . HOH V 7 . ? 22.760 14.817 42.450 1.00 22.62 ? 933 HOH A O 1 HETATM 4914 O O . HOH V 7 . ? 30.312 15.879 45.865 1.00 28.48 ? 934 HOH A O 1 HETATM 4915 O O . HOH V 7 . ? 13.467 32.426 46.279 1.00 17.54 ? 935 HOH A O 1 HETATM 4916 O O . HOH V 7 . ? 16.234 16.267 43.826 1.00 19.58 ? 936 HOH A O 1 HETATM 4917 O O . HOH V 7 . ? 7.426 28.136 51.699 1.00 17.98 ? 937 HOH A O 1 HETATM 4918 O O . HOH V 7 . ? 13.146 19.771 36.720 1.00 17.40 ? 938 HOH A O 1 HETATM 4919 O O . HOH V 7 . ? 34.655 22.951 41.559 1.00 22.87 ? 939 HOH A O 1 HETATM 4920 O O . HOH V 7 . ? 35.316 29.022 28.792 1.00 23.52 ? 940 HOH A O 1 HETATM 4921 O O . HOH V 7 . ? 11.733 36.182 36.688 1.00 19.22 ? 941 HOH A O 1 HETATM 4922 O O . HOH V 7 . ? 15.412 19.613 38.153 1.00 18.34 ? 942 HOH A O 1 HETATM 4923 O O . HOH V 7 . ? 15.939 22.053 39.340 1.00 20.07 ? 943 HOH A O 1 HETATM 4924 O O . HOH V 7 . ? 24.749 19.338 52.993 1.00 26.64 ? 944 HOH A O 1 HETATM 4925 O O . HOH V 7 . ? 8.383 11.948 19.907 1.00 31.50 ? 945 HOH A O 1 HETATM 4926 O O . HOH V 7 . ? 23.698 13.223 44.591 1.00 23.24 ? 946 HOH A O 1 HETATM 4927 O O . HOH V 7 . ? 8.313 32.093 31.421 1.00 19.61 ? 947 HOH A O 1 HETATM 4928 O O . HOH V 7 . ? -1.836 21.293 49.340 1.00 17.62 ? 948 HOH A O 1 HETATM 4929 O O . HOH V 7 . ? -4.778 37.662 63.730 1.00 23.54 ? 949 HOH A O 1 HETATM 4930 O O . HOH V 7 . ? 13.324 23.003 40.301 1.00 18.84 ? 950 HOH A O 1 HETATM 4931 O O . HOH V 7 . ? 32.696 16.885 9.514 1.00 18.78 ? 951 HOH A O 1 HETATM 4932 O O . HOH V 7 . ? -15.673 43.272 55.172 1.00 19.06 ? 952 HOH A O 1 HETATM 4933 O O . HOH V 7 . ? 16.013 19.075 16.323 1.00 22.24 ? 953 HOH A O 1 HETATM 4934 O O . HOH V 7 . ? 42.874 12.482 12.343 1.00 33.69 ? 954 HOH A O 1 HETATM 4935 O O . HOH V 7 . ? 17.664 22.867 14.863 1.00 21.95 ? 955 HOH A O 1 HETATM 4936 O O . HOH V 7 . ? 11.895 34.164 25.159 1.00 16.08 ? 956 HOH A O 1 HETATM 4937 O O . HOH V 7 . ? 15.138 27.347 29.923 1.00 16.98 ? 957 HOH A O 1 HETATM 4938 O O . HOH V 7 . ? 29.698 21.057 13.660 1.00 17.01 ? 958 HOH A O 1 HETATM 4939 O O . HOH V 7 . ? 32.401 16.860 14.893 1.00 18.20 ? 959 HOH A O 1 HETATM 4940 O O . HOH V 7 . ? 7.719 17.930 16.251 1.00 22.96 ? 960 HOH A O 1 HETATM 4941 O O . HOH V 7 . ? -18.560 32.680 50.249 1.00 30.13 ? 961 HOH A O 1 HETATM 4942 O O . HOH V 7 . ? 33.924 20.351 6.922 1.00 20.01 ? 962 HOH A O 1 HETATM 4943 O O . HOH V 7 . ? 9.705 20.454 37.021 1.00 20.29 ? 963 HOH A O 1 HETATM 4944 O O . HOH V 7 . ? 5.945 8.134 26.984 1.00 28.52 ? 964 HOH A O 1 HETATM 4945 O O . HOH V 7 . ? -17.713 36.561 54.353 1.00 23.72 ? 965 HOH A O 1 HETATM 4946 O O . HOH V 7 . ? 37.590 20.447 16.544 1.00 23.32 ? 966 HOH A O 1 HETATM 4947 O O . HOH V 7 . ? -12.539 40.590 41.721 1.00 21.02 ? 967 HOH A O 1 HETATM 4948 O O . HOH V 7 . ? 21.699 31.304 14.786 1.00 18.07 ? 968 HOH A O 1 HETATM 4949 O O . HOH V 7 . ? 10.513 11.361 15.916 1.00 27.15 ? 969 HOH A O 1 HETATM 4950 O O . HOH V 7 . ? -8.550 30.041 42.504 1.00 20.61 ? 970 HOH A O 1 HETATM 4951 O O . HOH V 7 . ? 15.416 15.691 16.997 1.00 23.63 ? 971 HOH A O 1 HETATM 4952 O O . HOH V 7 . ? 10.140 18.715 17.169 1.00 18.19 ? 972 HOH A O 1 HETATM 4953 O O . HOH V 7 . ? -0.958 20.660 53.850 1.00 21.23 ? 973 HOH A O 1 HETATM 4954 O O . HOH V 7 . ? -8.754 24.181 51.230 1.00 21.36 ? 974 HOH A O 1 HETATM 4955 O O . HOH V 7 . ? 3.383 42.465 46.164 1.00 19.86 ? 975 HOH A O 1 HETATM 4956 O O . HOH V 7 . ? 42.426 15.971 12.774 1.00 24.07 ? 976 HOH A O 1 HETATM 4957 O O . HOH V 7 . ? 1.841 50.081 51.167 1.00 31.93 ? 977 HOH A O 1 HETATM 4958 O O . HOH V 7 . ? -16.794 30.627 49.348 1.00 30.98 ? 978 HOH A O 1 HETATM 4959 O O . HOH V 7 . ? 34.349 22.839 31.925 1.00 20.61 ? 979 HOH A O 1 HETATM 4960 O O . HOH V 7 . ? 4.420 40.837 38.906 1.00 18.56 ? 980 HOH A O 1 HETATM 4961 O O . HOH V 7 . ? 11.472 36.270 60.545 1.00 30.57 ? 981 HOH A O 1 HETATM 4962 O O . HOH V 7 . ? 14.888 31.312 44.375 1.00 17.17 ? 982 HOH A O 1 HETATM 4963 O O . HOH V 7 . ? 15.804 36.539 50.183 1.00 24.35 ? 983 HOH A O 1 HETATM 4964 O O . HOH V 7 . ? -0.351 17.324 47.889 1.00 20.77 ? 984 HOH A O 1 HETATM 4965 O O . HOH V 7 . ? 14.010 35.641 25.738 1.00 22.15 ? 985 HOH A O 1 HETATM 4966 O O . HOH V 7 . ? 20.544 11.305 44.016 1.00 19.49 ? 986 HOH A O 1 HETATM 4967 O O . HOH V 7 . ? 18.825 37.803 29.511 1.00 20.39 ? 987 HOH A O 1 HETATM 4968 O O . HOH V 7 . ? 15.859 7.749 14.031 1.00 27.67 ? 988 HOH A O 1 HETATM 4969 O O . HOH V 7 . ? 21.862 33.549 16.470 1.00 18.65 ? 989 HOH A O 1 HETATM 4970 O O . HOH V 7 . ? 13.488 20.590 17.821 1.00 21.24 ? 990 HOH A O 1 HETATM 4971 O O . HOH V 7 . ? 17.435 26.970 48.662 1.00 19.57 ? 991 HOH A O 1 HETATM 4972 O O . HOH V 7 . ? 2.907 26.689 16.119 1.00 27.61 ? 992 HOH A O 1 HETATM 4973 O O . HOH V 7 . ? 13.060 11.764 15.149 1.00 26.13 ? 993 HOH A O 1 HETATM 4974 O O . HOH V 7 . ? -0.240 29.375 24.394 1.00 31.90 ? 994 HOH A O 1 HETATM 4975 O O . HOH V 7 . ? 10.836 21.329 17.431 1.00 19.77 ? 995 HOH A O 1 HETATM 4976 O O . HOH V 7 . ? 21.918 -0.683 18.160 1.00 32.65 ? 996 HOH A O 1 HETATM 4977 O O . HOH V 7 . ? 27.806 14.831 5.033 1.00 24.90 ? 997 HOH A O 1 HETATM 4978 O O . HOH V 7 . ? 15.722 36.834 17.664 1.00 26.00 ? 998 HOH A O 1 HETATM 4979 O O . HOH V 7 . ? 8.665 35.747 15.668 1.00 26.63 ? 999 HOH A O 1 HETATM 4980 O O . HOH V 7 . ? -12.361 48.641 60.360 1.00 26.23 ? 1000 HOH A O 1 HETATM 4981 O O . HOH V 7 . ? 7.149 44.666 36.810 1.00 38.46 ? 1001 HOH A O 1 HETATM 4982 O O . HOH V 7 . ? 34.529 22.404 8.537 1.00 30.06 ? 1002 HOH A O 1 HETATM 4983 O O . HOH V 7 . ? 14.160 13.328 17.143 1.00 25.34 ? 1003 HOH A O 1 HETATM 4984 O O . HOH V 7 . ? 14.160 18.315 11.296 1.00 27.34 ? 1004 HOH A O 1 HETATM 4985 O O . HOH V 7 . ? 19.182 9.804 14.623 1.00 20.73 ? 1005 HOH A O 1 HETATM 4986 O O . HOH V 7 . ? 18.904 4.319 13.837 1.00 40.91 ? 1006 HOH A O 1 HETATM 4987 O O . HOH V 7 . ? 40.274 23.882 16.333 1.00 35.40 ? 1007 HOH A O 1 HETATM 4988 O O . HOH V 7 . ? 42.342 24.577 18.122 1.00 23.15 ? 1008 HOH A O 1 HETATM 4989 O O . HOH V 7 . ? 39.965 21.390 15.344 1.00 37.22 ? 1009 HOH A O 1 HETATM 4990 O O . HOH V 7 . ? 47.514 20.213 16.952 1.00 31.63 ? 1010 HOH A O 1 HETATM 4991 O O . HOH V 7 . ? 47.512 21.365 19.906 1.00 25.05 ? 1011 HOH A O 1 HETATM 4992 O O . HOH V 7 . ? 48.133 20.161 25.041 1.00 24.22 ? 1012 HOH A O 1 HETATM 4993 O O . HOH V 7 . ? 51.978 17.089 22.345 1.00 40.56 ? 1013 HOH A O 1 HETATM 4994 O O . HOH V 7 . ? 54.668 15.565 25.056 1.00 31.76 ? 1014 HOH A O 1 HETATM 4995 O O . HOH V 7 . ? 21.112 35.912 36.847 1.00 23.95 ? 1015 HOH A O 1 HETATM 4996 O O . HOH V 7 . ? 25.026 20.831 49.472 1.00 20.80 ? 1016 HOH A O 1 HETATM 4997 O O . HOH V 7 . ? 35.628 29.229 36.530 1.00 27.01 ? 1017 HOH A O 1 HETATM 4998 O O . HOH V 7 . ? 42.753 25.163 35.616 1.00 23.72 ? 1018 HOH A O 1 HETATM 4999 O O . HOH V 7 . ? 36.164 24.548 30.479 1.00 21.51 ? 1019 HOH A O 1 HETATM 5000 O O . HOH V 7 . ? 50.498 17.190 26.414 1.00 26.81 ? 1020 HOH A O 1 HETATM 5001 O O . HOH V 7 . ? 19.921 36.610 43.719 1.00 34.22 ? 1021 HOH A O 1 HETATM 5002 O O . HOH V 7 . ? 15.117 40.230 42.695 1.00 32.50 ? 1022 HOH A O 1 HETATM 5003 O O . HOH V 7 . ? 14.380 42.184 44.633 1.00 36.11 ? 1023 HOH A O 1 HETATM 5004 O O . HOH V 7 . ? 16.133 41.383 40.553 1.00 33.07 ? 1024 HOH A O 1 HETATM 5005 O O . HOH V 7 . ? 13.995 39.494 33.913 1.00 31.06 ? 1025 HOH A O 1 HETATM 5006 O O . HOH V 7 . ? 16.494 39.908 32.669 1.00 44.66 ? 1026 HOH A O 1 HETATM 5007 O O . HOH V 7 . ? 19.615 27.009 42.581 1.00 31.38 ? 1027 HOH A O 1 HETATM 5008 O O . HOH V 7 . ? 16.055 42.665 55.600 1.00 43.23 ? 1028 HOH A O 1 HETATM 5009 O O . HOH V 7 . ? 14.923 20.480 49.206 1.00 22.44 ? 1029 HOH A O 1 HETATM 5010 O O . HOH V 7 . ? 15.589 21.436 56.206 1.00 26.43 ? 1030 HOH A O 1 HETATM 5011 O O . HOH V 7 . ? 19.787 19.980 57.545 1.00 26.60 ? 1031 HOH A O 1 HETATM 5012 O O . HOH V 7 . ? 34.586 18.939 40.613 1.00 19.24 ? 1032 HOH A O 1 HETATM 5013 O O . HOH V 7 . ? 34.814 21.479 45.047 1.00 28.07 ? 1033 HOH A O 1 HETATM 5014 O O . HOH V 7 . ? 34.661 25.380 45.354 1.00 29.16 ? 1034 HOH A O 1 HETATM 5015 O O . HOH V 7 . ? 36.276 27.091 42.076 1.00 33.28 ? 1035 HOH A O 1 HETATM 5016 O O . HOH V 7 . ? 12.553 19.776 33.873 1.00 16.29 ? 1036 HOH A O 1 HETATM 5017 O O . HOH V 7 . ? 11.368 18.467 38.318 1.00 16.62 ? 1037 HOH A O 1 HETATM 5018 O O . HOH V 7 . ? 8.189 24.807 44.706 1.00 16.34 ? 1038 HOH A O 1 HETATM 5019 O O . HOH V 7 . ? 14.569 23.350 50.222 1.00 26.07 ? 1039 HOH A O 1 HETATM 5020 O O . HOH V 7 . ? 22.119 14.924 59.151 1.00 32.68 ? 1040 HOH A O 1 HETATM 5021 O O . HOH V 7 . ? 23.682 13.956 55.518 1.00 24.11 ? 1041 HOH A O 1 HETATM 5022 O O . HOH V 7 . ? 23.943 16.125 56.790 1.00 30.38 ? 1042 HOH A O 1 HETATM 5023 O O . HOH V 7 . ? 25.194 18.181 55.411 1.00 28.01 ? 1043 HOH A O 1 HETATM 5024 O O . HOH V 7 . ? 30.007 17.539 54.113 1.00 32.80 ? 1044 HOH A O 1 HETATM 5025 O O . HOH V 7 . ? 25.383 14.232 53.370 1.00 30.53 ? 1045 HOH A O 1 HETATM 5026 O O . HOH V 7 . ? 37.455 27.883 29.902 1.00 37.59 ? 1046 HOH A O 1 HETATM 5027 O O . HOH V 7 . ? 34.959 31.258 30.226 1.00 39.62 ? 1047 HOH A O 1 HETATM 5028 O O . HOH V 7 . ? 35.878 32.256 22.591 1.00 29.93 ? 1048 HOH A O 1 HETATM 5029 O O . HOH V 7 . ? 34.952 34.004 20.943 1.00 29.66 ? 1049 HOH A O 1 HETATM 5030 O O . HOH V 7 . ? 33.647 33.016 18.818 1.00 29.77 ? 1050 HOH A O 1 HETATM 5031 O O . HOH V 7 . ? 22.055 37.681 31.563 1.00 42.94 ? 1051 HOH A O 1 HETATM 5032 O O . HOH V 7 . ? 20.091 38.889 25.086 1.00 25.25 ? 1052 HOH A O 1 HETATM 5033 O O . HOH V 7 . ? 23.548 34.818 29.938 1.00 43.15 ? 1053 HOH A O 1 HETATM 5034 O O . HOH V 7 . ? 29.489 33.422 26.822 1.00 32.81 ? 1054 HOH A O 1 HETATM 5035 O O . HOH V 7 . ? 25.092 34.482 19.243 1.00 23.23 ? 1055 HOH A O 1 HETATM 5036 O O . HOH V 7 . ? 22.484 33.954 19.206 1.00 21.09 ? 1056 HOH A O 1 HETATM 5037 O O . HOH V 7 . ? 19.185 37.059 14.671 1.00 24.27 ? 1057 HOH A O 1 HETATM 5038 O O . HOH V 7 . ? 18.759 37.216 11.744 1.00 20.13 ? 1058 HOH A O 1 HETATM 5039 O O . HOH V 7 . ? 23.945 31.518 13.427 1.00 26.44 ? 1059 HOH A O 1 HETATM 5040 O O . HOH V 7 . ? 26.113 34.504 16.844 1.00 30.15 ? 1060 HOH A O 1 HETATM 5041 O O . HOH V 7 . ? 18.067 40.310 46.377 1.00 46.50 ? 1061 HOH A O 1 HETATM 5042 O O . HOH V 7 . ? 11.530 34.329 45.383 1.00 18.59 ? 1062 HOH A O 1 HETATM 5043 O O . HOH V 7 . ? 17.641 38.032 41.695 1.00 44.96 ? 1063 HOH A O 1 HETATM 5044 O O . HOH V 7 . ? 7.230 43.163 45.365 1.00 21.65 ? 1064 HOH A O 1 HETATM 5045 O O . HOH V 7 . ? 4.504 44.510 44.831 1.00 29.90 ? 1065 HOH A O 1 HETATM 5046 O O . HOH V 7 . ? 25.710 33.856 49.593 1.00 33.56 ? 1066 HOH A O 1 HETATM 5047 O O . HOH V 7 . ? 25.747 27.792 52.998 1.00 26.38 ? 1067 HOH A O 1 HETATM 5048 O O . HOH V 7 . ? 28.519 30.098 50.356 1.00 27.23 ? 1068 HOH A O 1 HETATM 5049 O O . HOH V 7 . ? 27.871 32.813 50.467 1.00 33.67 ? 1069 HOH A O 1 HETATM 5050 O O . HOH V 7 . ? 27.730 29.853 53.080 1.00 27.90 ? 1070 HOH A O 1 HETATM 5051 O O . HOH V 7 . ? 27.200 32.542 53.260 1.00 38.15 ? 1071 HOH A O 1 HETATM 5052 O O . HOH V 7 . ? 29.898 29.675 54.621 1.00 27.74 ? 1072 HOH A O 1 HETATM 5053 O O . HOH V 7 . ? 14.159 35.554 28.420 1.00 22.04 ? 1073 HOH A O 1 HETATM 5054 O O . HOH V 7 . ? 12.420 37.723 28.224 1.00 22.44 ? 1074 HOH A O 1 HETATM 5055 O O . HOH V 7 . ? -11.202 23.815 57.576 1.00 22.92 ? 1075 HOH A O 1 HETATM 5056 O O . HOH V 7 . ? 35.217 21.389 39.580 1.00 28.23 ? 1076 HOH A O 1 HETATM 5057 O O . HOH V 7 . ? 9.495 39.215 52.714 1.00 24.74 ? 1077 HOH A O 1 HETATM 5058 O O . HOH V 7 . ? 11.941 18.331 14.808 1.00 26.22 ? 1078 HOH A O 1 HETATM 5059 O O . HOH V 7 . ? 10.863 17.976 12.528 1.00 37.09 ? 1079 HOH A O 1 HETATM 5060 O O . HOH V 7 . ? 15.522 21.944 16.562 1.00 24.45 ? 1080 HOH A O 1 HETATM 5061 O O . HOH V 7 . ? 6.053 35.939 14.297 1.00 52.06 ? 1081 HOH A O 1 HETATM 5062 O O . HOH V 7 . ? 5.336 20.649 11.029 1.00 33.51 ? 1082 HOH A O 1 HETATM 5063 O O . HOH V 7 . ? 5.610 15.155 26.022 1.00 24.12 ? 1083 HOH A O 1 HETATM 5064 O O . HOH V 7 . ? 4.114 11.674 26.382 1.00 27.54 ? 1084 HOH A O 1 HETATM 5065 O O . HOH V 7 . ? 6.364 10.287 28.564 1.00 23.45 ? 1085 HOH A O 1 HETATM 5066 O O . HOH V 7 . ? 2.721 14.795 26.162 1.00 40.08 ? 1086 HOH A O 1 HETATM 5067 O O . HOH V 7 . ? 1.599 16.789 30.554 1.00 23.09 ? 1087 HOH A O 1 HETATM 5068 O O . HOH V 7 . ? 1.561 17.575 28.013 1.00 38.10 ? 1088 HOH A O 1 HETATM 5069 O O . HOH V 7 . ? -0.171 18.778 26.262 1.00 54.01 ? 1089 HOH A O 1 HETATM 5070 O O . HOH V 7 . ? 23.644 -0.351 29.936 1.00 23.05 ? 1090 HOH A O 1 HETATM 5071 O O . HOH V 7 . ? 20.734 5.655 31.365 1.00 23.11 ? 1091 HOH A O 1 HETATM 5072 O O . HOH V 7 . ? 22.257 0.359 36.102 1.00 25.67 ? 1092 HOH A O 1 HETATM 5073 O O . HOH V 7 . ? 29.977 2.916 25.051 1.00 29.98 ? 1093 HOH A O 1 HETATM 5074 O O . HOH V 7 . ? 37.412 17.016 8.048 1.00 22.09 ? 1094 HOH A O 1 HETATM 5075 O O . HOH V 7 . ? 36.529 19.162 6.295 1.00 28.37 ? 1095 HOH A O 1 HETATM 5076 O O . HOH V 7 . ? 35.582 6.494 30.631 1.00 31.64 ? 1096 HOH A O 1 HETATM 5077 O O . HOH V 7 . ? 18.095 39.066 37.705 1.00 36.68 ? 1097 HOH A O 1 HETATM 5078 O O . HOH V 7 . ? 16.711 38.498 43.860 1.00 34.30 ? 1098 HOH A O 1 HETATM 5079 O O . HOH V 7 . ? 33.513 28.050 7.658 1.00 31.43 ? 1099 HOH A O 1 HETATM 5080 O O . HOH V 7 . ? 29.055 18.647 12.462 1.00 19.86 ? 1100 HOH A O 1 HETATM 5081 O O . HOH V 7 . ? 31.517 17.105 12.081 1.00 20.73 ? 1101 HOH A O 1 HETATM 5082 O O . HOH V 7 . ? 23.024 15.146 46.687 1.00 20.13 ? 1102 HOH A O 1 HETATM 5083 O O . HOH V 7 . ? 19.633 9.458 45.868 1.00 20.13 ? 1103 HOH A O 1 HETATM 5084 O O . HOH V 7 . ? 18.204 10.815 52.259 1.00 23.95 ? 1104 HOH A O 1 HETATM 5085 O O . HOH V 7 . ? 4.690 32.322 31.032 1.00 21.74 ? 1105 HOH A O 1 HETATM 5086 O O . HOH V 7 . ? 1.857 38.289 33.511 1.00 31.36 ? 1106 HOH A O 1 HETATM 5087 O O . HOH V 7 . ? -2.943 30.697 37.565 1.00 20.47 ? 1107 HOH A O 1 HETATM 5088 O O . HOH V 7 . ? 18.864 0.471 17.258 1.00 37.71 ? 1108 HOH A O 1 HETATM 5089 O O . HOH V 7 . ? 18.658 2.942 23.746 1.00 31.03 ? 1109 HOH A O 1 HETATM 5090 O O . HOH V 7 . ? 20.209 3.265 21.472 1.00 28.22 ? 1110 HOH A O 1 HETATM 5091 O O . HOH V 7 . ? 22.252 1.371 20.906 1.00 27.58 ? 1111 HOH A O 1 HETATM 5092 O O . HOH V 7 . ? 18.403 0.171 24.256 1.00 39.04 ? 1112 HOH A O 1 HETATM 5093 O O . HOH V 7 . ? 13.162 7.896 29.667 1.00 21.00 ? 1113 HOH A O 1 HETATM 5094 O O . HOH V 7 . ? -8.501 32.212 40.857 1.00 25.95 ? 1114 HOH A O 1 HETATM 5095 O O . HOH V 7 . ? -5.425 23.403 41.568 1.00 23.64 ? 1115 HOH A O 1 HETATM 5096 O O . HOH V 7 . ? -7.391 32.005 64.723 1.00 28.00 ? 1116 HOH A O 1 HETATM 5097 O O . HOH V 7 . ? -3.573 25.256 63.701 1.00 27.16 ? 1117 HOH A O 1 HETATM 5098 O O . HOH V 7 . ? -1.392 24.588 64.773 1.00 33.77 ? 1118 HOH A O 1 HETATM 5099 O O . HOH V 7 . ? 1.008 24.910 63.716 1.00 31.57 ? 1119 HOH A O 1 HETATM 5100 O O . HOH V 7 . ? 4.603 25.856 66.269 1.00 31.21 ? 1120 HOH A O 1 HETATM 5101 O O . HOH V 7 . ? 6.264 28.100 66.629 1.00 27.26 ? 1121 HOH A O 1 HETATM 5102 O O . HOH V 7 . ? 0.878 16.382 59.915 1.00 26.48 ? 1122 HOH A O 1 HETATM 5103 O O . HOH V 7 . ? 5.384 30.571 66.970 1.00 25.40 ? 1123 HOH A O 1 HETATM 5104 O O . HOH V 7 . ? 1.783 29.378 66.431 1.00 28.58 ? 1124 HOH A O 1 HETATM 5105 O O . HOH V 7 . ? -0.882 36.600 67.644 1.00 35.45 ? 1125 HOH A O 1 HETATM 5106 O O . HOH V 7 . ? -4.156 36.175 34.933 1.00 34.39 ? 1126 HOH A O 1 HETATM 5107 O O . HOH V 7 . ? -7.292 38.394 37.809 1.00 27.82 ? 1127 HOH A O 1 HETATM 5108 O O . HOH V 7 . ? 0.844 49.105 47.646 1.00 25.99 ? 1128 HOH A O 1 HETATM 5109 O O . HOH V 7 . ? -0.429 15.492 45.840 1.00 23.71 ? 1129 HOH A O 1 HETATM 5110 O O . HOH V 7 . ? -1.233 12.561 39.416 1.00 34.63 ? 1130 HOH A O 1 HETATM 5111 O O . HOH V 7 . ? -4.325 19.503 35.740 1.00 33.21 ? 1131 HOH A O 1 HETATM 5112 O O . HOH V 7 . ? -5.718 22.981 37.037 1.00 30.00 ? 1132 HOH A O 1 HETATM 5113 O O . HOH V 7 . ? -5.833 27.627 34.850 1.00 21.96 ? 1133 HOH A O 1 HETATM 5114 O O . HOH V 7 . ? -9.725 18.300 47.451 1.00 41.91 ? 1134 HOH A O 1 HETATM 5115 O O . HOH V 7 . ? -11.312 17.254 50.240 1.00 46.35 ? 1135 HOH A O 1 HETATM 5116 O O . HOH V 7 . ? -14.968 40.938 43.161 1.00 19.62 ? 1136 HOH A O 1 HETATM 5117 O O . HOH V 7 . ? 11.176 5.606 46.479 1.00 33.51 ? 1137 HOH A O 1 HETATM 5118 O O . HOH V 7 . ? 4.404 7.855 37.078 1.00 28.58 ? 1138 HOH A O 1 HETATM 5119 O O . HOH V 7 . ? 8.045 6.829 41.252 1.00 27.47 ? 1139 HOH A O 1 HETATM 5120 O O . HOH V 7 . ? 6.325 5.839 34.137 1.00 35.23 ? 1140 HOH A O 1 HETATM 5121 O O . HOH V 7 . ? 9.075 4.659 35.244 1.00 30.56 ? 1141 HOH A O 1 HETATM 5122 O O . HOH V 7 . ? 2.808 6.365 34.696 1.00 54.93 ? 1142 HOH A O 1 HETATM 5123 O O . HOH V 7 . ? 1.897 7.398 31.601 1.00 48.57 ? 1143 HOH A O 1 HETATM 5124 O O . HOH V 7 . ? 7.005 8.613 24.338 1.00 34.72 ? 1144 HOH A O 1 HETATM 5125 O O . HOH V 7 . ? 14.159 8.515 18.595 1.00 29.82 ? 1145 HOH A O 1 HETATM 5126 O O . HOH V 7 . ? -10.258 45.879 58.966 1.00 25.69 ? 1146 HOH A O 1 HETATM 5127 O O . HOH V 7 . ? -4.259 19.678 47.388 1.00 29.33 ? 1147 HOH A O 1 HETATM 5128 O O . HOH V 7 . ? 1.283 15.160 49.837 1.00 22.32 ? 1148 HOH A O 1 HETATM 5129 O O . HOH V 7 . ? -14.805 26.883 47.406 1.00 36.70 ? 1149 HOH A O 1 HETATM 5130 O O . HOH V 7 . ? 6.035 42.579 52.863 1.00 19.50 ? 1150 HOH A O 1 HETATM 5131 O O . HOH V 7 . ? -4.403 42.832 39.991 1.00 25.73 ? 1151 HOH A O 1 HETATM 5132 O O . HOH V 7 . ? -1.602 42.803 39.500 1.00 35.02 ? 1152 HOH A O 1 HETATM 5133 O O . HOH V 7 . ? -6.412 48.345 45.837 1.00 28.49 ? 1153 HOH A O 1 HETATM 5134 O O . HOH V 7 . ? -12.399 44.669 43.964 1.00 23.31 ? 1154 HOH A O 1 HETATM 5135 O O . HOH V 7 . ? -11.287 42.932 42.093 1.00 29.38 ? 1155 HOH A O 1 HETATM 5136 O O . HOH V 7 . ? 9.648 34.366 61.094 1.00 21.81 ? 1156 HOH A O 1 HETATM 5137 O O . HOH V 7 . ? 12.047 28.200 62.274 1.00 21.69 ? 1157 HOH A O 1 HETATM 5138 O O . HOH V 7 . ? 5.394 37.554 65.668 1.00 22.66 ? 1158 HOH A O 1 HETATM 5139 O O . HOH V 7 . ? 33.530 3.661 9.250 1.00 26.88 ? 1159 HOH A O 1 HETATM 5140 O O . HOH V 7 . ? -0.407 52.087 55.341 1.00 27.39 ? 1160 HOH A O 1 HETATM 5141 O O . HOH V 7 . ? 47.383 23.798 23.330 1.00 30.90 ? 1161 HOH A O 1 HETATM 5142 O O . HOH V 7 . ? 34.112 2.429 14.550 1.00 25.93 ? 1162 HOH A O 1 HETATM 5143 O O . HOH V 7 . ? 39.344 17.184 10.029 1.00 26.51 ? 1163 HOH A O 1 HETATM 5144 O O . HOH V 7 . ? 17.948 30.505 63.719 1.00 26.69 ? 1164 HOH A O 1 HETATM 5145 O O . HOH V 7 . ? 37.723 5.320 27.777 1.00 24.65 ? 1165 HOH A O 1 HETATM 5146 O O . HOH V 7 . ? 12.373 34.547 58.870 1.00 26.48 ? 1166 HOH A O 1 HETATM 5147 O O . HOH V 7 . ? 32.871 3.125 24.078 1.00 34.61 ? 1167 HOH A O 1 HETATM 5148 O O . HOH V 7 . ? 37.204 3.208 23.189 1.00 28.31 ? 1168 HOH A O 1 HETATM 5149 O O . HOH V 7 . ? 36.681 3.591 15.042 1.00 32.97 ? 1169 HOH A O 1 HETATM 5150 O O . HOH V 7 . ? -11.030 39.225 61.129 1.00 28.71 ? 1170 HOH A O 1 HETATM 5151 O O . HOH V 7 . ? -19.907 40.841 49.491 1.00 26.75 ? 1171 HOH A O 1 HETATM 5152 O O . HOH V 7 . ? 18.816 32.609 62.102 1.00 28.17 ? 1172 HOH A O 1 HETATM 5153 O O . HOH V 7 . ? 33.032 2.985 28.323 1.00 31.73 ? 1173 HOH A O 1 HETATM 5154 O O . HOH V 7 . ? 2.116 49.501 61.971 1.00 32.98 ? 1174 HOH A O 1 HETATM 5155 O O . HOH V 7 . ? 39.928 8.668 41.116 1.00 39.66 ? 1175 HOH A O 1 HETATM 5156 O O . HOH V 7 . ? 34.336 8.086 4.874 1.00 28.49 ? 1176 HOH A O 1 HETATM 5157 O O . HOH V 7 . ? -6.622 58.518 61.861 1.00 29.42 ? 1177 HOH A O 1 HETATM 5158 O O . HOH V 7 . ? 47.107 9.496 22.047 1.00 26.97 ? 1178 HOH A O 1 HETATM 5159 O O . HOH V 7 . ? 49.263 22.173 23.343 1.00 26.26 ? 1179 HOH A O 1 HETATM 5160 O O . HOH V 7 . ? 12.785 24.275 10.979 1.00 23.58 ? 1180 HOH A O 1 HETATM 5161 O O . HOH V 7 . ? 24.273 28.898 60.212 1.00 28.25 ? 1181 HOH A O 1 HETATM 5162 O O . HOH V 7 . ? 40.852 19.077 10.203 1.00 32.57 ? 1182 HOH A O 1 HETATM 5163 O O . HOH V 7 . ? 4.931 33.379 13.619 1.00 45.93 ? 1183 HOH A O 1 HETATM 5164 O O . HOH V 7 . ? 13.064 34.700 13.872 1.00 27.14 ? 1184 HOH A O 1 HETATM 5165 O O . HOH V 7 . ? -0.289 52.348 62.314 1.00 31.00 ? 1185 HOH A O 1 HETATM 5166 O O . HOH V 7 . ? 37.495 29.099 14.743 1.00 33.21 ? 1186 HOH A O 1 HETATM 5167 O O . HOH V 7 . ? 34.609 10.844 55.027 1.00 42.67 ? 1187 HOH A O 1 HETATM 5168 O O . HOH V 7 . ? 36.167 9.604 6.141 1.00 27.66 ? 1188 HOH A O 1 HETATM 5169 O O . HOH V 7 . ? 37.272 10.708 47.843 1.00 29.30 ? 1189 HOH A O 1 HETATM 5170 O O . HOH V 7 . ? 3.074 38.090 67.072 1.00 34.52 ? 1190 HOH A O 1 HETATM 5171 O O . HOH V 7 . ? 26.453 -1.160 25.293 1.00 49.87 ? 1191 HOH A O 1 HETATM 5172 O O . HOH V 7 . ? 13.681 9.148 14.487 1.00 25.28 ? 1192 HOH A O 1 HETATM 5173 O O . HOH V 7 . ? 11.410 4.855 40.593 1.00 50.81 ? 1193 HOH A O 1 HETATM 5174 O O . HOH V 7 . ? 28.818 -0.228 11.411 1.00 29.25 ? 1194 HOH A O 1 HETATM 5175 O O . HOH V 7 . ? 36.710 8.982 49.787 1.00 31.87 ? 1195 HOH A O 1 HETATM 5176 O O . HOH V 7 . ? 4.492 45.754 62.237 1.00 27.54 ? 1196 HOH A O 1 HETATM 5177 O O . HOH V 7 . ? 30.135 16.545 2.704 1.00 38.55 ? 1197 HOH A O 1 HETATM 5178 O O . HOH V 7 . ? 8.652 5.265 21.826 1.00 38.61 ? 1198 HOH A O 1 HETATM 5179 O O . HOH V 7 . ? 8.309 6.030 24.557 1.00 26.00 ? 1199 HOH A O 1 HETATM 5180 O O . HOH V 7 . ? -6.798 40.305 64.352 1.00 25.54 ? 1200 HOH A O 1 HETATM 5181 O O . HOH V 7 . ? -14.761 28.801 50.795 1.00 34.33 ? 1201 HOH A O 1 HETATM 5182 O O . HOH V 7 . ? 24.285 28.436 62.990 1.00 33.20 ? 1202 HOH A O 1 HETATM 5183 O O . HOH V 7 . ? 16.900 11.364 56.095 1.00 35.63 ? 1203 HOH A O 1 HETATM 5184 O O . HOH V 7 . ? 24.354 13.433 8.452 1.00 32.79 ? 1204 HOH A O 1 HETATM 5185 O O . HOH V 7 . ? -1.215 38.941 65.246 1.00 27.65 ? 1205 HOH A O 1 HETATM 5186 O O . HOH V 7 . ? 38.687 19.329 46.452 1.00 33.54 ? 1206 HOH A O 1 HETATM 5187 O O . HOH V 7 . ? 36.748 20.453 53.349 1.00 36.27 ? 1207 HOH A O 1 HETATM 5188 O O . HOH V 7 . ? 24.955 33.828 54.875 1.00 31.17 ? 1208 HOH A O 1 HETATM 5189 O O . HOH V 7 . ? 30.292 9.190 57.056 1.00 33.14 ? 1209 HOH A O 1 HETATM 5190 O O . HOH V 7 . ? 23.563 22.995 5.973 1.00 23.95 ? 1210 HOH A O 1 HETATM 5191 O O . HOH V 7 . ? 38.313 16.211 52.885 1.00 40.08 ? 1211 HOH A O 1 HETATM 5192 O O . HOH V 7 . ? -17.434 28.591 44.584 1.00 64.83 ? 1212 HOH A O 1 HETATM 5193 O O . HOH V 7 . ? 23.043 3.535 45.990 1.00 28.53 ? 1213 HOH A O 1 HETATM 5194 O O . HOH V 7 . ? -16.179 47.020 55.251 1.00 32.19 ? 1214 HOH A O 1 HETATM 5195 O O . HOH V 7 . ? 33.397 1.549 16.999 1.00 35.28 ? 1215 HOH A O 1 HETATM 5196 O O . HOH V 7 . ? -20.829 39.800 51.638 1.00 39.36 ? 1216 HOH A O 1 HETATM 5197 O O . HOH V 7 . ? 28.427 2.700 4.151 1.00 32.06 ? 1217 HOH A O 1 HETATM 5198 O O . HOH V 7 . ? 40.773 16.757 43.299 1.00 30.93 ? 1218 HOH A O 1 HETATM 5199 O O . HOH V 7 . ? 18.251 -3.912 32.915 1.00 42.39 ? 1219 HOH A O 1 HETATM 5200 O O . HOH V 7 . ? 15.594 0.875 50.168 1.00 58.26 ? 1220 HOH A O 1 HETATM 5201 O O . HOH V 7 . ? 40.441 6.856 31.449 1.00 27.53 ? 1221 HOH A O 1 HETATM 5202 O O . HOH V 7 . ? -22.712 38.527 43.791 1.00 32.30 ? 1222 HOH A O 1 HETATM 5203 O O . HOH V 7 . ? 12.408 38.538 58.789 1.00 29.87 ? 1223 HOH A O 1 HETATM 5204 O O . HOH V 7 . ? -7.382 33.690 68.655 1.00 33.22 ? 1224 HOH A O 1 HETATM 5205 O O . HOH V 7 . ? 20.671 20.317 6.144 1.00 37.57 ? 1225 HOH A O 1 HETATM 5206 O O . HOH V 7 . ? 22.873 20.905 51.297 1.00 27.43 ? 1226 HOH A O 1 HETATM 5207 O O . HOH V 7 . ? 16.372 1.947 46.556 1.00 34.95 ? 1227 HOH A O 1 HETATM 5208 O O . HOH V 7 . ? 39.804 21.184 8.580 1.00 34.59 ? 1228 HOH A O 1 HETATM 5209 O O . HOH V 7 . ? 6.241 46.605 57.333 1.00 41.47 ? 1229 HOH A O 1 HETATM 5210 O O . HOH V 7 . ? -2.663 54.475 58.189 1.00 32.92 ? 1230 HOH A O 1 HETATM 5211 O O . HOH V 7 . ? 2.571 45.382 42.575 1.00 35.43 ? 1231 HOH A O 1 HETATM 5212 O O . HOH V 7 . ? 10.813 43.996 47.246 1.00 38.34 ? 1232 HOH A O 1 HETATM 5213 O O . HOH V 7 . ? 8.191 33.913 67.894 1.00 41.21 ? 1233 HOH A O 1 HETATM 5214 O O . HOH V 7 . ? -2.639 24.897 14.856 1.00 30.68 ? 1234 HOH A O 1 HETATM 5215 O O . HOH V 7 . ? -2.284 51.672 50.455 1.00 52.25 ? 1235 HOH A O 1 HETATM 5216 O O . HOH V 7 . ? 5.786 14.682 23.422 1.00 29.16 ? 1236 HOH A O 1 HETATM 5217 O O . HOH V 7 . ? 31.846 3.418 54.207 1.00 31.27 ? 1237 HOH A O 1 HETATM 5218 O O . HOH V 7 . ? 0.344 41.138 65.153 1.00 29.84 ? 1238 HOH A O 1 HETATM 5219 O O . HOH V 7 . ? 31.788 2.746 18.903 1.00 36.29 ? 1239 HOH A O 1 HETATM 5220 O O . HOH V 7 . ? -12.358 19.607 44.655 1.00 33.36 ? 1240 HOH A O 1 HETATM 5221 O O . HOH V 7 . ? -11.783 21.788 56.130 1.00 30.30 ? 1241 HOH A O 1 HETATM 5222 O O . HOH V 7 . ? -18.530 34.084 55.453 1.00 36.22 ? 1242 HOH A O 1 HETATM 5223 O O . HOH V 7 . ? 7.997 45.539 50.003 1.00 39.42 ? 1243 HOH A O 1 HETATM 5224 O O . HOH V 7 . ? 25.328 37.139 20.457 1.00 32.37 ? 1244 HOH A O 1 HETATM 5225 O O . HOH V 7 . ? 34.875 6.162 52.751 1.00 35.00 ? 1245 HOH A O 1 HETATM 5226 O O . HOH V 7 . ? -4.154 50.251 49.158 1.00 32.49 ? 1246 HOH A O 1 HETATM 5227 O O . HOH V 7 . ? 4.784 43.481 39.334 1.00 36.24 ? 1247 HOH A O 1 HETATM 5228 O O . HOH V 7 . ? 17.550 7.377 6.025 1.00 36.95 ? 1248 HOH A O 1 HETATM 5229 O O . HOH V 7 . ? 29.867 5.438 2.184 1.00 42.18 ? 1249 HOH A O 1 HETATM 5230 O O . HOH V 7 . ? -2.515 16.685 33.137 1.00 37.02 ? 1250 HOH A O 1 HETATM 5231 O O . HOH V 7 . ? 38.117 6.370 14.014 1.00 40.91 ? 1251 HOH A O 1 HETATM 5232 O O . HOH V 7 . ? 12.780 36.745 62.860 1.00 45.91 ? 1252 HOH A O 1 HETATM 5233 O O . HOH V 7 . ? 20.183 5.723 3.188 1.00 51.24 ? 1253 HOH A O 1 HETATM 5234 O O . HOH V 7 . ? -14.920 45.324 43.424 1.00 36.52 ? 1254 HOH A O 1 HETATM 5235 O O . HOH V 7 . ? 1.750 8.991 41.384 1.00 54.89 ? 1255 HOH A O 1 HETATM 5236 O O . HOH V 7 . ? 10.924 35.722 14.042 1.00 34.49 ? 1256 HOH A O 1 HETATM 5237 O O . HOH V 7 . ? 12.280 2.137 33.348 1.00 35.15 ? 1257 HOH A O 1 HETATM 5238 O O . HOH V 7 . ? 23.417 6.996 55.644 1.00 40.43 ? 1258 HOH A O 1 HETATM 5239 O O . HOH V 7 . ? 49.957 15.865 35.975 1.00 55.93 ? 1259 HOH A O 1 HETATM 5240 O O . HOH V 7 . ? -6.766 21.239 31.485 1.00 35.55 ? 1260 HOH A O 1 HETATM 5241 O O . HOH V 7 . ? 36.070 -0.499 36.507 1.00 44.34 ? 1261 HOH A O 1 HETATM 5242 O O . HOH V 7 . ? 48.224 19.062 39.873 1.00 61.12 ? 1262 HOH A O 1 HETATM 5243 O O . HOH V 7 . ? 43.078 26.425 16.462 1.00 34.02 ? 1263 HOH A O 1 HETATM 5244 O O . HOH V 7 . ? 50.624 18.584 18.667 1.00 37.86 ? 1264 HOH A O 1 HETATM 5245 O O . HOH V 7 . ? -0.724 31.873 67.779 1.00 37.96 ? 1265 HOH A O 1 HETATM 5246 O O . HOH V 7 . ? -4.765 25.587 71.905 1.00 53.88 ? 1266 HOH A O 1 HETATM 5247 O O . HOH V 7 . ? 27.000 16.099 54.441 1.00 49.39 ? 1267 HOH A O 1 HETATM 5248 O O . HOH V 7 . ? 10.962 26.790 68.623 1.00 31.16 ? 1268 HOH A O 1 HETATM 5249 O O . HOH V 7 . ? 14.010 28.077 11.144 1.00 39.05 ? 1269 HOH A O 1 HETATM 5250 O O . HOH V 7 . ? 39.686 9.026 43.900 1.00 46.42 ? 1270 HOH A O 1 HETATM 5251 O O . HOH V 7 . ? -0.618 42.428 67.618 1.00 45.14 ? 1271 HOH A O 1 HETATM 5252 O O . HOH V 7 . ? 13.111 2.982 43.999 1.00 52.47 ? 1272 HOH A O 1 HETATM 5253 O O . HOH V 7 . ? -1.944 14.891 52.985 1.00 36.61 ? 1273 HOH A O 1 HETATM 5254 O O . HOH V 7 . ? 1.856 21.597 18.282 1.00 34.04 ? 1274 HOH A O 1 HETATM 5255 O O . HOH V 7 . ? -19.446 38.431 55.113 1.00 43.24 ? 1275 HOH A O 1 HETATM 5256 O O . HOH V 7 . ? 13.374 39.958 60.843 1.00 53.65 ? 1276 HOH A O 1 HETATM 5257 O O . HOH V 7 . ? -16.915 21.374 53.466 1.00 43.39 ? 1277 HOH A O 1 HETATM 5258 O O . HOH V 7 . ? 27.296 25.159 60.921 1.00 40.61 ? 1278 HOH A O 1 HETATM 5259 O O . HOH V 7 . ? 37.776 22.120 51.831 1.00 66.46 ? 1279 HOH A O 1 HETATM 5260 O O . HOH V 7 . ? 13.215 3.969 47.293 1.00 35.58 ? 1280 HOH A O 1 HETATM 5261 O O . HOH V 7 . ? 42.105 19.453 16.286 1.00 31.14 ? 1281 HOH A O 1 HETATM 5262 O O . HOH V 7 . ? 17.818 -1.587 25.906 1.00 36.72 ? 1282 HOH A O 1 HETATM 5263 O O . HOH V 7 . ? 29.837 1.631 30.539 1.00 28.97 ? 1283 HOH A O 1 HETATM 5264 O O . HOH V 7 . ? 37.291 9.040 45.381 1.00 35.49 ? 1284 HOH A O 1 HETATM 5265 O O . HOH V 7 . ? -3.755 29.362 34.172 1.00 30.69 ? 1285 HOH A O 1 HETATM 5266 O O . HOH V 7 . ? 29.755 17.996 56.704 1.00 40.60 ? 1286 HOH A O 1 HETATM 5267 O O . HOH V 7 . ? 30.341 28.262 56.963 1.00 39.68 ? 1287 HOH A O 1 HETATM 5268 O O . HOH V 7 . ? -5.150 52.227 64.955 1.00 33.78 ? 1288 HOH A O 1 HETATM 5269 O O . HOH V 7 . ? 23.245 6.605 2.944 1.00 46.74 ? 1289 HOH A O 1 HETATM 5270 O O . HOH V 7 . ? -17.109 30.767 42.456 1.00 39.31 ? 1290 HOH A O 1 HETATM 5271 O O . HOH V 7 . ? 4.364 15.212 13.387 1.00 70.39 ? 1291 HOH A O 1 HETATM 5272 O O . HOH V 7 . ? 50.352 21.996 33.004 1.00 53.06 ? 1292 HOH A O 1 HETATM 5273 O O . HOH V 7 . ? 2.191 46.514 63.907 1.00 48.97 ? 1293 HOH A O 1 HETATM 5274 O O . HOH V 7 . ? 18.512 2.917 43.670 1.00 26.62 ? 1294 HOH A O 1 HETATM 5275 O O . HOH V 7 . ? 34.038 3.659 6.583 1.00 46.03 ? 1295 HOH A O 1 HETATM 5276 O O . HOH V 7 . ? 9.296 44.696 40.937 1.00 34.92 ? 1296 HOH A O 1 HETATM 5277 O O . HOH V 7 . ? 17.156 38.907 50.387 1.00 43.11 ? 1297 HOH A O 1 HETATM 5278 O O . HOH V 7 . ? -16.722 33.266 43.566 1.00 34.84 ? 1298 HOH A O 1 HETATM 5279 O O . HOH V 7 . ? 11.508 44.447 43.814 1.00 35.59 ? 1299 HOH A O 1 HETATM 5280 O O . HOH V 7 . ? 18.233 10.347 8.069 1.00 36.16 ? 1300 HOH A O 1 HETATM 5281 O O . HOH V 7 . ? -5.264 18.779 59.690 1.00 35.29 ? 1301 HOH A O 1 HETATM 5282 O O . HOH V 7 . ? -14.755 51.892 51.912 1.00 71.43 ? 1302 HOH A O 1 HETATM 5283 O O . HOH V 7 . ? 9.326 2.942 24.438 1.00 46.09 ? 1303 HOH A O 1 HETATM 5284 O O . HOH V 7 . ? 21.503 13.118 8.728 1.00 34.44 ? 1304 HOH A O 1 HETATM 5285 O O . HOH V 7 . ? 27.415 7.401 -7.752 1.00 46.92 ? 1305 HOH A O 1 HETATM 5286 O O . HOH V 7 . ? 13.243 6.597 10.904 1.00 52.16 ? 1306 HOH A O 1 HETATM 5287 O O . HOH V 7 . ? 23.909 13.972 3.107 1.00 56.92 ? 1307 HOH A O 1 HETATM 5288 O O . HOH V 7 . ? 6.768 10.543 46.494 1.00 27.22 ? 1308 HOH A O 1 HETATM 5289 O O . HOH V 7 . ? 8.669 11.533 13.972 1.00 40.53 ? 1309 HOH A O 1 HETATM 5290 O O . HOH V 7 . ? 16.201 31.311 65.504 1.00 40.09 ? 1310 HOH A O 1 HETATM 5291 O O . HOH V 7 . ? 20.634 2.173 45.867 1.00 40.15 ? 1311 HOH A O 1 HETATM 5292 O O . HOH V 7 . ? 21.329 33.383 62.784 1.00 46.72 ? 1312 HOH A O 1 HETATM 5293 O O . HOH V 7 . ? 25.989 20.543 56.492 1.00 27.78 ? 1313 HOH A O 1 HETATM 5294 O O . HOH V 7 . ? 2.052 48.100 43.402 1.00 43.48 ? 1314 HOH A O 1 HETATM 5295 O O . HOH V 7 . ? 0.903 10.941 30.751 1.00 44.21 ? 1315 HOH A O 1 HETATM 5296 O O . HOH V 7 . ? 35.044 13.192 44.030 1.00 28.86 ? 1316 HOH A O 1 HETATM 5297 O O . HOH V 7 . ? -4.484 14.238 52.592 1.00 39.74 ? 1317 HOH A O 1 HETATM 5298 O O . HOH V 7 . ? 8.747 43.137 63.329 1.00 37.82 ? 1318 HOH A O 1 HETATM 5299 O O . HOH V 7 . ? -7.835 51.577 55.822 1.00 36.05 ? 1319 HOH A O 1 HETATM 5300 O O . HOH V 7 . ? 10.768 0.151 32.592 1.00 47.21 ? 1320 HOH A O 1 HETATM 5301 O O . HOH V 7 . ? 18.615 6.374 53.390 1.00 50.26 ? 1321 HOH A O 1 HETATM 5302 O O . HOH V 7 . ? 27.051 17.861 4.914 1.00 32.79 ? 1322 HOH A O 1 HETATM 5303 O O . HOH V 7 . ? -9.433 50.463 52.146 1.00 49.66 ? 1323 HOH A O 1 HETATM 5304 O O . HOH V 7 . ? 19.289 9.156 23.672 1.00 30.80 ? 1324 HOH A O 1 HETATM 5305 O O . HOH V 7 . ? 7.640 27.443 68.907 1.00 35.92 ? 1325 HOH A O 1 HETATM 5306 O O . HOH V 7 . ? -0.090 11.630 46.521 1.00 46.79 ? 1326 HOH A O 1 HETATM 5307 O O . HOH V 7 . ? 24.174 -4.285 31.380 1.00 39.84 ? 1327 HOH A O 1 HETATM 5308 O O . HOH V 7 . ? 22.536 -2.765 33.066 1.00 33.33 ? 1328 HOH A O 1 HETATM 5309 O O . HOH V 7 . ? -0.516 51.095 52.581 1.00 37.91 ? 1329 HOH A O 1 HETATM 5310 O O . HOH V 7 . ? 2.482 40.550 66.430 1.00 36.58 ? 1330 HOH A O 1 HETATM 5311 O O . HOH V 7 . ? 3.718 14.669 21.717 1.00 39.58 ? 1331 HOH A O 1 HETATM 5312 O O . HOH V 7 . ? 19.374 11.251 58.548 1.00 36.71 ? 1332 HOH A O 1 HETATM 5313 O O . HOH V 7 . ? 20.915 38.153 37.179 1.00 43.43 ? 1333 HOH A O 1 HETATM 5314 O O . HOH V 7 . ? 29.752 1.615 50.420 1.00 44.56 ? 1334 HOH A O 1 HETATM 5315 O O . HOH V 7 . ? 28.941 34.868 18.584 1.00 36.92 ? 1335 HOH A O 1 HETATM 5316 O O . HOH V 7 . ? 30.259 0.394 8.996 1.00 34.94 ? 1336 HOH A O 1 HETATM 5317 O O . HOH V 7 . ? 36.235 30.027 8.211 1.00 46.76 ? 1337 HOH A O 1 HETATM 5318 O O . HOH V 7 . ? 38.148 24.653 44.740 1.00 53.19 ? 1338 HOH A O 1 HETATM 5319 O O . HOH V 7 . ? 32.381 -1.007 16.980 1.00 43.19 ? 1339 HOH A O 1 HETATM 5320 O O . HOH V 7 . ? 15.079 5.591 12.458 1.00 38.46 ? 1340 HOH A O 1 HETATM 5321 O O . HOH V 7 . ? 16.862 6.505 16.162 1.00 36.33 ? 1341 HOH A O 1 HETATM 5322 O O . HOH V 7 . ? 29.578 -0.997 17.546 1.00 50.73 ? 1342 HOH A O 1 HETATM 5323 O O . HOH V 7 . ? -5.134 33.699 70.320 1.00 32.88 ? 1343 HOH A O 1 HETATM 5324 O O . HOH V 7 . ? 22.617 14.135 65.644 1.00 46.72 ? 1344 HOH A O 1 HETATM 5325 O O . HOH V 7 . ? 39.652 27.120 16.957 1.00 37.97 ? 1345 HOH A O 1 HETATM 5326 O O . HOH V 7 . ? 10.990 5.039 43.377 1.00 49.45 ? 1346 HOH A O 1 HETATM 5327 O O . HOH V 7 . ? 11.561 11.306 11.319 1.00 46.70 ? 1347 HOH A O 1 HETATM 5328 O O . HOH V 7 . ? 17.773 14.452 7.947 1.00 52.89 ? 1348 HOH A O 1 HETATM 5329 O O . HOH V 7 . ? 23.022 0.701 42.834 1.00 60.02 ? 1349 HOH A O 1 HETATM 5330 O O . HOH V 7 . ? 24.504 24.896 62.344 1.00 28.02 ? 1350 HOH A O 1 HETATM 5331 O O . HOH V 7 . ? -6.975 22.629 58.964 1.00 30.19 ? 1351 HOH A O 1 HETATM 5332 O O . HOH V 7 . ? 21.321 21.767 68.454 1.00 49.26 ? 1352 HOH A O 1 HETATM 5333 O O . HOH V 7 . ? -22.966 35.759 43.706 1.00 50.04 ? 1353 HOH A O 1 HETATM 5334 O O . HOH V 7 . ? 27.069 32.527 60.761 1.00 55.42 ? 1354 HOH A O 1 HETATM 5335 O O . HOH V 7 . ? -0.030 17.861 22.334 1.00 56.75 ? 1355 HOH A O 1 HETATM 5336 O O . HOH V 7 . ? -18.978 45.808 45.725 1.00 54.18 ? 1356 HOH A O 1 HETATM 5337 O O . HOH V 7 . ? 8.949 40.671 66.338 1.00 42.96 ? 1357 HOH A O 1 HETATM 5338 O O . HOH V 7 . ? 12.552 7.990 16.677 1.00 35.54 ? 1358 HOH A O 1 HETATM 5339 O O . HOH V 7 . ? 13.988 2.127 39.134 1.00 39.79 ? 1359 HOH A O 1 HETATM 5340 O O . HOH V 7 . ? 24.150 17.255 5.611 1.00 52.89 ? 1360 HOH A O 1 HETATM 5341 O O . HOH V 7 . ? -6.083 41.669 37.908 1.00 47.34 ? 1361 HOH A O 1 HETATM 5342 O O . HOH V 7 . ? 15.748 -0.730 33.025 1.00 36.90 ? 1362 HOH A O 1 HETATM 5343 O O . HOH V 7 . ? -0.996 15.306 56.019 1.00 35.51 ? 1363 HOH A O 1 HETATM 5344 O O . HOH V 7 . ? 11.204 39.092 30.309 1.00 26.83 ? 1364 HOH A O 1 HETATM 5345 O O . HOH V 7 . ? 37.005 6.466 45.523 1.00 43.60 ? 1365 HOH A O 1 HETATM 5346 O O . HOH V 7 . ? -8.973 25.399 31.637 1.00 47.32 ? 1366 HOH A O 1 HETATM 5347 O O . HOH V 7 . ? 45.356 23.458 42.127 1.00 38.72 ? 1367 HOH A O 1 HETATM 5348 O O . HOH V 7 . ? 12.050 38.180 65.083 1.00 48.78 ? 1368 HOH A O 1 HETATM 5349 O O . HOH V 7 . ? 23.228 8.959 2.077 1.00 47.35 ? 1369 HOH A O 1 HETATM 5350 O O . HOH V 7 . ? -1.638 54.361 55.479 1.00 35.42 ? 1370 HOH A O 1 HETATM 5351 O O . HOH V 7 . ? 2.946 48.717 45.869 1.00 37.82 ? 1371 HOH A O 1 HETATM 5352 O O . HOH V 7 . ? 19.818 4.635 -0.694 1.00 61.96 ? 1372 HOH A O 1 HETATM 5353 O O . HOH V 7 . ? 32.794 26.295 47.594 1.00 35.46 ? 1373 HOH A O 1 HETATM 5354 O O . HOH V 7 . ? 12.313 24.511 71.957 1.00 62.85 ? 1374 HOH A O 1 HETATM 5355 O O . HOH V 7 . ? 26.820 29.703 60.757 1.00 40.29 ? 1375 HOH A O 1 HETATM 5356 O O . HOH V 7 . ? 38.232 3.458 37.647 1.00 43.55 ? 1376 HOH A O 1 HETATM 5357 O O . HOH V 7 . ? -5.323 31.499 34.394 1.00 39.49 ? 1377 HOH A O 1 HETATM 5358 O O . HOH V 7 . ? 30.442 -4.479 37.499 1.00 53.12 ? 1378 HOH A O 1 HETATM 5359 O O . HOH V 7 . ? 28.694 -1.903 44.231 1.00 56.35 ? 1379 HOH A O 1 HETATM 5360 O O . HOH V 7 . ? 21.403 -1.123 21.482 1.00 52.88 ? 1380 HOH A O 1 HETATM 5361 O O . HOH V 7 . ? -1.217 49.656 45.854 1.00 48.15 ? 1381 HOH A O 1 HETATM 5362 O O . HOH V 7 . ? -10.383 47.376 63.755 1.00 36.54 ? 1382 HOH A O 1 HETATM 5363 O O . HOH V 7 . ? 38.866 1.680 21.501 1.00 38.97 ? 1383 HOH A O 1 HETATM 5364 O O . HOH V 7 . ? 5.679 12.295 22.072 1.00 63.77 ? 1384 HOH A O 1 HETATM 5365 O O . HOH V 7 . ? 47.609 21.420 39.169 1.00 51.26 ? 1385 HOH A O 1 HETATM 5366 O O . HOH V 7 . ? 11.514 -1.648 30.179 1.00 48.36 ? 1386 HOH A O 1 HETATM 5367 O O . HOH V 7 . ? 19.455 25.178 69.112 1.00 45.84 ? 1387 HOH A O 1 HETATM 5368 O O . HOH V 7 . ? 26.391 37.157 29.398 1.00 57.63 ? 1388 HOH A O 1 HETATM 5369 O O . HOH V 7 . ? 36.053 29.994 12.697 1.00 40.00 ? 1389 HOH A O 1 HETATM 5370 O O . HOH V 7 . ? 33.239 33.826 13.437 1.00 35.10 ? 1390 HOH A O 1 HETATM 5371 O O . HOH V 7 . ? 40.449 5.331 16.426 1.00 32.74 ? 1391 HOH A O 1 HETATM 5372 O O . HOH V 7 . ? -15.628 36.709 56.202 1.00 31.94 ? 1392 HOH A O 1 HETATM 5373 O O . HOH V 7 . ? 45.784 27.703 32.521 1.00 31.50 ? 1393 HOH A O 1 HETATM 5374 O O . HOH V 7 . ? 35.524 8.590 54.618 1.00 42.33 ? 1394 HOH A O 1 HETATM 5375 O O . HOH V 7 . ? 30.837 29.976 44.267 1.00 52.46 ? 1395 HOH A O 1 HETATM 5376 O O . HOH V 7 . ? 30.173 31.302 39.080 1.00 56.22 ? 1396 HOH A O 1 HETATM 5377 O O . HOH V 7 . ? 17.017 19.489 57.193 1.00 35.81 ? 1397 HOH A O 1 HETATM 5378 O O . HOH V 7 . ? 29.279 7.143 -4.992 1.00 54.52 ? 1398 HOH A O 1 HETATM 5379 O O . HOH V 7 . ? 41.645 22.375 43.925 1.00 45.42 ? 1399 HOH A O 1 HETATM 5380 O O . HOH V 7 . ? 37.428 31.180 16.517 1.00 40.25 ? 1400 HOH A O 1 HETATM 5381 O O . HOH V 7 . ? -18.542 45.316 49.307 1.00 42.61 ? 1401 HOH A O 1 HETATM 5382 O O . HOH V 7 . ? -16.092 33.002 57.021 1.00 40.14 ? 1402 HOH A O 1 HETATM 5383 O O . HOH V 7 . ? 34.780 3.211 21.708 1.00 35.08 ? 1403 HOH A O 1 HETATM 5384 O O . HOH V 7 . ? 35.306 24.619 7.614 1.00 47.33 ? 1404 HOH A O 1 HETATM 5385 O O . HOH V 7 . ? 24.379 -2.193 28.319 1.00 47.28 ? 1405 HOH A O 1 HETATM 5386 O O . HOH V 7 . ? 13.335 43.399 50.935 1.00 51.26 ? 1406 HOH A O 1 HETATM 5387 O O . HOH V 7 . ? 17.900 -2.373 37.110 1.00 45.28 ? 1407 HOH A O 1 HETATM 5388 O O . HOH V 7 . ? -3.175 39.365 66.853 1.00 46.54 ? 1408 HOH A O 1 HETATM 5389 O O . HOH V 7 . ? 14.303 10.765 63.214 1.00 49.05 ? 1409 HOH A O 1 HETATM 5390 O O . HOH V 7 . ? 19.837 32.440 13.109 1.00 33.56 ? 1410 HOH A O 1 HETATM 5391 O O . HOH V 7 . ? 41.513 13.861 49.435 1.00 60.34 ? 1411 HOH A O 1 HETATM 5392 O O . HOH V 7 . ? 32.062 29.945 53.103 1.00 41.62 ? 1412 HOH A O 1 HETATM 5393 O O . HOH V 7 . ? 18.587 20.624 68.713 1.00 42.46 ? 1413 HOH A O 1 HETATM 5394 O O . HOH V 7 . ? 3.520 47.835 57.985 1.00 38.69 ? 1414 HOH A O 1 HETATM 5395 O O . HOH V 7 . ? 24.409 21.661 64.994 1.00 38.37 ? 1415 HOH A O 1 HETATM 5396 O O . HOH V 7 . ? 23.345 -1.602 40.868 1.00 63.35 ? 1416 HOH A O 1 HETATM 5397 O O . HOH V 7 . ? 23.737 -2.411 22.519 1.00 49.56 ? 1417 HOH A O 1 HETATM 5398 O O . HOH V 7 . ? 3.809 50.634 57.077 1.00 41.23 ? 1418 HOH A O 1 HETATM 5399 O O . HOH V 7 . ? 25.568 28.607 7.799 1.00 49.08 ? 1419 HOH A O 1 HETATM 5400 O O . HOH V 7 . ? 45.833 27.040 23.357 1.00 45.35 ? 1420 HOH A O 1 HETATM 5401 O O . HOH V 7 . ? -8.279 16.714 49.900 1.00 43.27 ? 1421 HOH A O 1 HETATM 5402 O O . HOH V 7 . ? 3.881 6.859 39.127 1.00 36.37 ? 1422 HOH A O 1 HETATM 5403 O O . HOH V 7 . ? 54.802 13.038 24.381 1.00 36.93 ? 1423 HOH A O 1 HETATM 5404 O O . HOH V 7 . ? 41.288 27.640 48.777 1.00 64.10 ? 1424 HOH A O 1 HETATM 5405 O O . HOH V 7 . ? -9.666 22.506 59.487 1.00 36.71 ? 1425 HOH A O 1 HETATM 5406 O O . HOH V 7 . ? 11.136 18.493 68.423 1.00 39.86 ? 1426 HOH A O 1 HETATM 5407 O O . HOH V 7 . ? 39.764 22.194 12.952 1.00 45.01 ? 1427 HOH A O 1 HETATM 5408 O O . HOH V 7 . ? 49.560 18.368 34.223 1.00 47.72 ? 1428 HOH A O 1 HETATM 5409 O O . HOH V 7 . ? 8.969 29.735 69.912 1.00 56.17 ? 1429 HOH A O 1 HETATM 5410 O O . HOH V 7 . ? 16.068 39.305 57.478 1.00 49.63 ? 1430 HOH A O 1 HETATM 5411 O O . HOH V 7 . ? 2.306 26.805 64.998 1.00 37.49 ? 1431 HOH A O 1 HETATM 5412 O O . HOH V 7 . ? 4.147 45.218 32.539 1.00 78.96 ? 1432 HOH A O 1 HETATM 5413 O O . HOH V 7 . ? 11.019 42.204 33.345 1.00 37.42 ? 1433 HOH A O 1 HETATM 5414 O O . HOH V 7 . ? 30.569 35.639 26.003 1.00 44.45 ? 1434 HOH A O 1 HETATM 5415 O O . HOH V 7 . ? 34.045 5.868 58.198 1.00 78.53 ? 1435 HOH A O 1 HETATM 5416 O O . HOH V 7 . ? -4.707 14.961 38.284 1.00 56.77 ? 1436 HOH A O 1 HETATM 5417 O O . HOH V 7 . ? 28.248 -1.388 20.511 1.00 51.18 ? 1437 HOH A O 1 HETATM 5418 O O . HOH V 7 . ? 9.725 4.517 31.895 1.00 52.73 ? 1438 HOH A O 1 HETATM 5419 O O . HOH V 7 . ? 29.081 1.454 18.591 1.00 32.08 ? 1439 HOH A O 1 HETATM 5420 O O . HOH V 7 . ? 23.109 31.801 10.808 1.00 41.42 ? 1440 HOH A O 1 HETATM 5421 O O . HOH V 7 . ? -5.041 37.548 68.125 1.00 43.10 ? 1441 HOH A O 1 HETATM 5422 O O . HOH V 7 . ? 34.242 23.915 53.914 1.00 48.02 ? 1442 HOH A O 1 HETATM 5423 O O . HOH V 7 . ? 9.062 11.963 59.443 1.00 41.69 ? 1443 HOH A O 1 HETATM 5424 O O . HOH V 7 . ? -10.380 48.066 45.664 1.00 42.49 ? 1444 HOH A O 1 HETATM 5425 O O . HOH V 7 . ? -4.140 27.663 73.511 1.00 57.20 ? 1445 HOH A O 1 HETATM 5426 O O . HOH V 7 . ? 8.666 25.197 69.418 1.00 46.47 ? 1446 HOH A O 1 HETATM 5427 O O . HOH V 7 . ? -16.956 28.411 47.353 1.00 49.38 ? 1447 HOH A O 1 HETATM 5428 O O . HOH V 7 . ? 28.195 19.974 58.020 1.00 45.48 ? 1448 HOH A O 1 HETATM 5429 O O . HOH V 7 . ? 31.648 21.388 59.727 1.00 72.15 ? 1449 HOH A O 1 HETATM 5430 O O . HOH V 7 . ? -17.503 47.255 50.569 1.00 54.18 ? 1450 HOH A O 1 HETATM 5431 O O . HOH V 7 . ? -10.673 42.672 63.269 1.00 42.52 ? 1451 HOH A O 1 HETATM 5432 O O . HOH V 7 . ? 19.287 16.462 7.128 1.00 49.11 ? 1452 HOH A O 1 HETATM 5433 O O . HOH V 7 . ? 46.540 14.387 15.152 1.00 53.59 ? 1453 HOH A O 1 HETATM 5434 O O . HOH V 7 . ? 50.028 26.448 34.606 1.00 55.36 ? 1454 HOH A O 1 HETATM 5435 O O . HOH V 7 . ? 16.843 25.095 68.586 1.00 47.05 ? 1455 HOH A O 1 HETATM 5436 O O . HOH V 7 . ? -14.503 22.370 54.379 1.00 46.04 ? 1456 HOH A O 1 HETATM 5437 O O . HOH V 7 . ? 14.790 5.799 20.994 1.00 40.17 ? 1457 HOH A O 1 HETATM 5438 O O . HOH V 7 . ? 5.700 23.194 65.936 1.00 35.80 ? 1458 HOH A O 1 HETATM 5439 O O . HOH V 7 . ? 10.596 5.725 19.905 1.00 45.34 ? 1459 HOH A O 1 HETATM 5440 O O . HOH V 7 . ? 10.363 43.101 35.773 1.00 43.62 ? 1460 HOH A O 1 HETATM 5441 O O . HOH V 7 . ? 25.530 2.245 51.318 1.00 40.23 ? 1461 HOH A O 1 HETATM 5442 O O . HOH V 7 . ? -14.544 27.650 41.307 1.00 52.51 ? 1462 HOH A O 1 HETATM 5443 O O . HOH V 7 . ? 28.451 26.486 3.823 1.00 59.22 ? 1463 HOH A O 1 HETATM 5444 O O . HOH V 7 . ? 6.856 31.817 69.177 1.00 49.39 ? 1464 HOH A O 1 HETATM 5445 O O . HOH V 7 . ? 15.206 43.994 37.617 1.00 43.52 ? 1465 HOH A O 1 HETATM 5446 O O . HOH V 7 . ? 27.477 7.370 56.977 1.00 44.22 ? 1466 HOH A O 1 HETATM 5447 O O . HOH V 7 . ? 4.170 18.614 14.161 1.00 42.74 ? 1467 HOH A O 1 HETATM 5448 O O . HOH V 7 . ? 29.767 29.239 59.490 1.00 55.74 ? 1468 HOH A O 1 HETATM 5449 O O . HOH V 7 . ? 9.713 8.915 52.413 1.00 42.62 ? 1469 HOH A O 1 HETATM 5450 O O . HOH V 7 . ? 46.749 6.247 18.870 1.00 44.01 ? 1470 HOH A O 1 HETATM 5451 O O . HOH V 7 . ? 31.136 30.269 49.773 1.00 45.96 ? 1471 HOH A O 1 HETATM 5452 O O . HOH V 7 . ? 31.585 32.956 48.526 1.00 50.68 ? 1472 HOH A O 1 HETATM 5453 O O . HOH V 7 . ? 33.178 28.782 48.638 1.00 50.41 ? 1473 HOH A O 1 HETATM 5454 O O . HOH V 7 . ? 48.904 18.805 31.998 1.00 42.60 ? 1474 HOH A O 1 HETATM 5455 O O . HOH V 7 . ? 9.875 38.579 66.746 1.00 45.90 ? 1475 HOH A O 1 HETATM 5456 O O . HOH V 7 . ? -0.515 19.197 30.261 1.00 42.50 ? 1476 HOH A O 1 HETATM 5457 O O . HOH V 7 . ? 48.487 6.934 22.726 1.00 49.13 ? 1477 HOH A O 1 HETATM 5458 O O . HOH V 7 . ? 10.679 45.690 59.033 1.00 50.19 ? 1478 HOH A O 1 HETATM 5459 O O . HOH V 7 . ? 27.911 -3.897 37.675 1.00 47.13 ? 1479 HOH A O 1 HETATM 5460 O O . HOH V 7 . ? 24.356 -2.921 9.708 1.00 59.12 ? 1480 HOH A O 1 HETATM 5461 O O . HOH V 7 . ? 50.869 10.987 17.810 1.00 52.47 ? 1481 HOH A O 1 HETATM 5462 O O . HOH V 7 . ? -1.089 45.908 41.692 1.00 43.64 ? 1482 HOH A O 1 HETATM 5463 O O . HOH V 7 . ? 4.355 48.164 60.461 1.00 47.40 ? 1483 HOH A O 1 HETATM 5464 O O . HOH V 7 . ? -10.127 19.715 58.458 1.00 50.21 ? 1484 HOH A O 1 HETATM 5465 O O . HOH V 7 . ? 43.551 0.907 23.384 1.00 84.72 ? 1485 HOH A O 1 HETATM 5466 O O . HOH V 7 . ? 18.714 1.480 20.073 1.00 42.96 ? 1486 HOH A O 1 HETATM 5467 O O . HOH V 7 . ? 36.601 3.130 27.290 1.00 47.42 ? 1487 HOH A O 1 HETATM 5468 O O . HOH V 7 . ? 35.207 5.663 4.855 1.00 48.37 ? 1488 HOH A O 1 HETATM 5469 O O . HOH V 7 . ? -10.279 31.538 39.537 1.00 44.42 ? 1489 HOH A O 1 HETATM 5470 O O . HOH V 7 . ? -5.643 46.081 43.019 1.00 55.86 ? 1490 HOH A O 1 HETATM 5471 O O . HOH V 7 . ? 23.177 4.261 -9.344 1.00 67.99 ? 1491 HOH A O 1 HETATM 5472 O O . HOH V 7 . ? 43.539 18.537 14.477 1.00 42.13 ? 1492 HOH A O 1 HETATM 5473 O O . HOH V 7 . ? 8.741 1.611 30.653 1.00 59.83 ? 1493 HOH A O 1 HETATM 5474 O O . HOH V 7 . ? 27.758 37.524 21.910 1.00 39.88 ? 1494 HOH A O 1 HETATM 5475 O O . HOH V 7 . ? 6.144 49.444 50.601 1.00 71.45 ? 1495 HOH A O 1 HETATM 5476 O O . HOH V 7 . ? 12.652 15.705 8.447 1.00 68.45 ? 1496 HOH A O 1 HETATM 5477 O O . HOH V 7 . ? -11.735 49.871 47.254 1.00 48.02 ? 1497 HOH A O 1 HETATM 5478 O O . HOH V 7 . ? 39.507 27.570 12.882 1.00 60.00 ? 1498 HOH A O 1 HETATM 5479 O O . HOH V 7 . ? -2.301 20.246 23.346 1.00 76.54 ? 1499 HOH A O 1 HETATM 5480 O O . HOH V 7 . ? 29.775 -2.198 13.216 1.00 49.71 ? 1500 HOH A O 1 HETATM 5481 O O . HOH V 7 . ? -8.712 25.847 65.592 1.00 41.87 ? 1501 HOH A O 1 HETATM 5482 O O . HOH V 7 . ? -15.462 49.392 49.564 1.00 52.63 ? 1502 HOH A O 1 HETATM 5483 O O . HOH V 7 . ? -6.047 21.385 61.408 1.00 38.59 ? 1503 HOH A O 1 HETATM 5484 O O . HOH V 7 . ? 38.622 2.989 31.286 1.00 44.25 ? 1504 HOH A O 1 HETATM 5485 O O . HOH V 7 . ? 6.888 41.155 31.032 1.00 40.45 ? 1505 HOH A O 1 HETATM 5486 O O . HOH V 7 . ? 38.133 23.166 9.562 1.00 45.85 ? 1506 HOH A O 1 HETATM 5487 O O . HOH V 7 . ? 42.210 9.858 11.084 1.00 64.37 ? 1507 HOH A O 1 HETATM 5488 O O . HOH V 7 . ? -17.134 44.394 44.165 1.00 34.85 ? 1508 HOH A O 1 HETATM 5489 O O . HOH V 7 . ? 41.695 12.278 36.286 1.00 36.44 ? 1509 HOH A O 1 HETATM 5490 O O . HOH V 7 . ? -19.117 24.463 52.527 1.00 51.03 ? 1510 HOH A O 1 HETATM 5491 O O . HOH V 7 . ? -1.786 13.823 44.295 1.00 46.20 ? 1511 HOH A O 1 HETATM 5492 O O . HOH V 7 . ? -2.293 38.071 34.721 1.00 46.52 ? 1512 HOH A O 1 HETATM 5493 O O . HOH V 7 . ? 10.178 8.715 16.735 1.00 36.84 ? 1513 HOH A O 1 HETATM 5494 O O . HOH V 7 . ? -5.058 54.503 57.606 1.00 36.06 ? 1514 HOH A O 1 HETATM 5495 O O . HOH V 7 . ? 10.680 42.821 61.437 1.00 51.99 ? 1515 HOH A O 1 HETATM 5496 O O . HOH V 7 . ? -6.595 21.862 39.567 1.00 40.49 ? 1516 HOH A O 1 HETATM 5497 O O . HOH V 7 . ? 35.145 34.062 30.037 1.00 66.65 ? 1517 HOH A O 1 HETATM 5498 O O . HOH V 7 . ? 23.432 29.336 9.509 1.00 37.15 ? 1518 HOH A O 1 HETATM 5499 O O . HOH V 7 . ? 31.317 1.049 52.458 1.00 55.10 ? 1519 HOH A O 1 HETATM 5500 O O . HOH V 7 . ? -3.954 19.924 31.549 1.00 40.74 ? 1520 HOH A O 1 HETATM 5501 O O . HOH V 7 . ? 2.366 16.285 20.467 1.00 75.01 ? 1521 HOH A O 1 HETATM 5502 O O . HOH V 7 . ? 35.584 0.664 48.466 1.00 75.36 ? 1522 HOH A O 1 HETATM 5503 O O . HOH V 7 . ? 30.242 -6.589 33.595 1.00 78.22 ? 1523 HOH A O 1 HETATM 5504 O O . HOH V 7 . ? 43.293 10.807 13.535 1.00 53.58 ? 1524 HOH A O 1 HETATM 5505 O O . HOH V 7 . ? 41.183 19.075 45.181 1.00 55.48 ? 1525 HOH A O 1 HETATM 5506 O O . HOH V 7 . ? 17.104 7.533 65.224 1.00 76.49 ? 1526 HOH A O 1 HETATM 5507 O O . HOH V 7 . ? 6.711 1.478 26.724 1.00 55.77 ? 1527 HOH A O 1 HETATM 5508 O O . HOH V 7 . ? -20.652 34.657 52.355 1.00 42.20 ? 1528 HOH A O 1 HETATM 5509 O O . HOH V 7 . ? -3.772 49.205 45.182 1.00 48.70 ? 1529 HOH A O 1 HETATM 5510 O O . HOH V 7 . ? -0.247 16.997 24.772 1.00 68.89 ? 1530 HOH A O 1 HETATM 5511 O O . HOH V 7 . ? 13.892 45.058 43.960 1.00 65.19 ? 1531 HOH A O 1 HETATM 5512 O O . HOH V 7 . ? 1.687 14.997 23.455 1.00 44.55 ? 1532 HOH A O 1 HETATM 5513 O O . HOH V 7 . ? 11.469 -7.821 28.945 1.00 59.15 ? 1533 HOH A O 1 HETATM 5514 O O . HOH V 7 . ? 24.140 34.901 37.428 1.00 47.73 ? 1534 HOH A O 1 HETATM 5515 O O . HOH V 7 . ? 7.055 10.190 22.131 1.00 50.30 ? 1535 HOH A O 1 HETATM 5516 O O . HOH V 7 . ? -7.857 43.488 37.243 1.00 49.17 ? 1536 HOH A O 1 HETATM 5517 O O . HOH V 7 . ? 19.194 8.720 3.911 1.00 53.88 ? 1537 HOH A O 1 HETATM 5518 O O . HOH V 7 . ? 53.438 9.502 21.708 1.00 61.20 ? 1538 HOH A O 1 HETATM 5519 O O . HOH V 7 . ? 26.536 18.323 62.657 1.00 39.86 ? 1539 HOH A O 1 HETATM 5520 O O . HOH V 7 . ? 5.072 8.525 46.229 1.00 46.16 ? 1540 HOH A O 1 HETATM 5521 O O . HOH V 7 . ? 40.841 9.611 14.643 1.00 40.85 ? 1541 HOH A O 1 HETATM 5522 O O . HOH V 7 . ? 37.536 3.165 17.614 1.00 29.27 ? 1542 HOH A O 1 HETATM 5523 O O . HOH V 7 . ? 40.237 3.327 20.069 1.00 31.13 ? 1543 HOH A O 1 HETATM 5524 O O . HOH V 7 . ? 38.051 30.498 21.746 1.00 30.86 ? 1544 HOH A O 1 HETATM 5525 O O . HOH V 7 . ? 16.005 34.490 16.202 1.00 33.61 ? 1545 HOH A O 1 HETATM 5526 O O . HOH V 7 . ? -10.701 26.385 41.363 1.00 37.45 ? 1546 HOH A O 1 HETATM 5527 O O . HOH V 7 . ? -7.307 52.598 63.308 1.00 34.19 ? 1547 HOH A O 1 HETATM 5528 O O . HOH V 7 . ? 17.706 18.567 55.997 1.00 53.79 ? 1548 HOH A O 1 HETATM 5529 O O . HOH V 7 . ? 42.834 3.110 19.572 1.00 45.06 ? 1549 HOH A O 1 HETATM 5530 O O . HOH V 7 . ? 25.627 9.723 0.415 1.00 55.37 ? 1550 HOH A O 1 HETATM 5531 O O . HOH V 7 . ? -3.478 46.393 62.556 1.00 28.46 ? 1551 HOH A O 1 HETATM 5532 O O . HOH V 7 . ? -17.516 14.735 58.216 1.00 43.75 ? 1552 HOH A O 1 HETATM 5533 O O . HOH V 7 . ? 0.997 14.600 29.627 1.00 48.43 ? 1553 HOH A O 1 HETATM 5534 O O . HOH V 7 . ? -12.027 40.830 62.223 1.00 36.28 ? 1554 HOH A O 1 HETATM 5535 O O . HOH V 7 . ? 47.830 24.164 39.565 1.00 63.97 ? 1555 HOH A O 1 HETATM 5536 O O . HOH V 7 . ? 49.178 21.184 27.409 1.00 43.67 ? 1556 HOH A O 1 HETATM 5537 O O . HOH V 7 . ? -15.250 22.485 45.940 1.00 61.41 ? 1557 HOH A O 1 HETATM 5538 O O . HOH V 7 . ? 52.065 16.229 24.689 1.00 36.38 ? 1558 HOH A O 1 HETATM 5539 O O . HOH V 7 . ? 22.796 1.820 49.761 1.00 52.63 ? 1559 HOH A O 1 HETATM 5540 O O . HOH V 7 . ? 39.109 29.511 33.425 1.00 43.53 ? 1560 HOH A O 1 HETATM 5541 O O . HOH V 7 . ? 17.777 -1.285 16.506 1.00 61.46 ? 1561 HOH A O 1 HETATM 5542 O O . HOH V 7 . ? 35.283 1.993 19.241 1.00 42.04 ? 1562 HOH A O 1 HETATM 5543 O O . HOH V 7 . ? 32.153 0.501 31.141 1.00 39.86 ? 1563 HOH A O 1 HETATM 5544 O O . HOH V 7 . ? 10.853 41.494 50.339 1.00 49.49 ? 1564 HOH A O 1 HETATM 5545 O O . HOH V 7 . ? -4.075 13.094 35.183 1.00 64.10 ? 1565 HOH A O 1 HETATM 5546 O O . HOH V 7 . ? 23.490 35.177 59.056 1.00 68.06 ? 1566 HOH A O 1 HETATM 5547 O O . HOH V 7 . ? 38.728 26.466 42.451 1.00 37.11 ? 1567 HOH A O 1 HETATM 5548 O O . HOH V 7 . ? -7.558 17.691 47.147 1.00 37.64 ? 1568 HOH A O 1 HETATM 5549 O O . HOH V 7 . ? -13.972 31.185 42.164 1.00 27.27 ? 1569 HOH A O 1 HETATM 5550 O O . HOH V 7 . ? -11.176 29.768 43.360 1.00 28.92 ? 1570 HOH A O 1 HETATM 5551 O O . HOH V 7 . ? 2.280 22.215 66.147 1.00 68.14 ? 1571 HOH A O 1 HETATM 5552 O O . HOH V 7 . ? -0.758 29.634 68.327 1.00 47.28 ? 1572 HOH A O 1 HETATM 5553 O O . HOH V 7 . ? -13.250 27.877 57.041 1.00 31.49 ? 1573 HOH A O 1 HETATM 5554 O O . HOH V 7 . ? 6.959 36.772 67.698 1.00 41.29 ? 1574 HOH A O 1 HETATM 5555 O O . HOH V 7 . ? 43.337 13.605 9.858 1.00 37.71 ? 1575 HOH A O 1 HETATM 5556 O O . HOH V 7 . ? 22.107 39.219 39.657 1.00 68.97 ? 1576 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . HIS A 1 ? 0.8269 0.9256 0.9047 -0.0150 0.0331 -0.0686 -3 HIS A N 2 C CA . HIS A 1 ? 0.8312 0.9312 0.9129 -0.0179 0.0343 -0.0741 -3 HIS A CA 3 C C . HIS A 1 ? 0.8217 0.9335 0.9036 -0.0187 0.0308 -0.0760 -3 HIS A C 4 O O . HIS A 1 ? 0.8226 0.9353 0.9055 -0.0200 0.0299 -0.0763 -3 HIS A O 5 C CB . HIS A 1 ? 0.8396 0.9305 0.9222 -0.0189 0.0362 -0.0721 -3 HIS A CB 6 C CG . HIS A 1 ? 0.8789 0.9615 0.9652 -0.0205 0.0413 -0.0762 -3 HIS A CG 7 N ND1 . HIS A 1 ? 0.8954 0.9789 0.9860 -0.0237 0.0432 -0.0821 -3 HIS A ND1 8 C CD2 . HIS A 1 ? 0.9107 0.9838 0.9968 -0.0193 0.0450 -0.0753 -3 HIS A CD2 9 C CE1 . HIS A 1 ? 0.9127 0.9871 1.0058 -0.0247 0.0481 -0.0846 -3 HIS A CE1 10 N NE2 . HIS A 1 ? 0.9247 0.9925 1.0150 -0.0218 0.0493 -0.0804 -3 HIS A NE2 11 N N . HIS A 2 ? 0.8156 0.9361 0.8961 -0.0175 0.0286 -0.0768 -2 HIS A N 12 C CA . HIS A 2 ? 0.8074 0.9400 0.8895 -0.0183 0.0269 -0.0822 -2 HIS A CA 13 C C . HIS A 2 ? 0.7902 0.9334 0.8689 -0.0163 0.0230 -0.0798 -2 HIS A C 14 O O . HIS A 2 ? 0.7931 0.9427 0.8720 -0.0157 0.0229 -0.0828 -2 HIS A O 15 C CB . HIS A 2 ? 0.8158 0.9508 0.9018 -0.0210 0.0277 -0.0873 -2 HIS A CB 16 C CG . HIS A 2 ? 0.8480 0.9768 0.9387 -0.0235 0.0323 -0.0933 -2 HIS A CG 17 N ND1 . HIS A 2 ? 0.8589 0.9935 0.9541 -0.0262 0.0335 -0.1010 -2 HIS A ND1 18 C CD2 . HIS A 2 ? 0.8575 0.9749 0.9490 -0.0236 0.0361 -0.0927 -2 HIS A CD2 19 C CE1 . HIS A 2 ? 0.8606 0.9869 0.9593 -0.0282 0.0380 -0.1049 -2 HIS A CE1 20 N NE2 . HIS A 2 ? 0.8584 0.9739 0.9548 -0.0266 0.0397 -0.0998 -2 HIS A NE2 21 N N . ALA A 3 ? 0.7627 0.9079 0.8382 -0.0154 0.0200 -0.0745 -1 ALA A N 22 C CA . ALA A 3 ? 0.7310 0.8852 0.8028 -0.0133 0.0167 -0.0715 -1 ALA A CA 23 C C . ALA A 3 ? 0.7143 0.8661 0.7833 -0.0116 0.0166 -0.0673 -1 ALA A C 24 O O . ALA A 3 ? 0.7198 0.8623 0.7881 -0.0114 0.0180 -0.0640 -1 ALA A O 25 C CB . ALA A 3 ? 0.7340 0.8894 0.8031 -0.0127 0.0139 -0.0667 -1 ALA A CB 26 N N . ALA A 4 ? 0.6815 0.8421 0.7486 -0.0102 0.0149 -0.0674 0 ALA A N 27 C CA . ALA A 4 ? 0.6533 0.8129 0.7180 -0.0086 0.0149 -0.0639 0 ALA A CA 28 C C . ALA A 4 ? 0.6272 0.7804 0.6884 -0.0078 0.0139 -0.0562 0 ALA A C 29 O O . ALA A 4 ? 0.6206 0.7693 0.6809 -0.0071 0.0149 -0.0540 0 ALA A O 30 C CB . ALA A 4 ? 0.6607 0.8316 0.7239 -0.0073 0.0133 -0.0652 0 ALA A CB 31 N N . ASP A 5 ? 0.5922 0.7454 0.6514 -0.0080 0.0118 -0.0524 1 ASP A N 32 C CA . ASP A 5 ? 0.5601 0.7068 0.6163 -0.0076 0.0109 -0.0457 1 ASP A CA 33 C C . ASP A 5 ? 0.5245 0.6608 0.5821 -0.0087 0.0125 -0.0450 1 ASP A C 34 O O . ASP A 5 ? 0.5056 0.6377 0.5613 -0.0088 0.0114 -0.0405 1 ASP A O 35 C CB . ASP A 5 ? 0.5563 0.7076 0.6091 -0.0071 0.0081 -0.0417 1 ASP A CB 36 C CG . ASP A 5 ? 0.6232 0.7751 0.6770 -0.0077 0.0074 -0.0432 1 ASP A CG 37 O OD1 . ASP A 5 ? 0.6384 0.7902 0.6958 -0.0087 0.0089 -0.0486 1 ASP A OD1 38 O OD2 . ASP A 5 ? 0.6547 0.8066 0.7056 -0.0072 0.0055 -0.0389 1 ASP A OD2 39 N N . TYR A 6 ? 0.4916 0.6239 0.5527 -0.0095 0.0152 -0.0496 2 TYR A N 40 C CA . TYR A 6 ? 0.4448 0.5676 0.5075 -0.0105 0.0170 -0.0492 2 TYR A CA 41 C C . TYR A 6 ? 0.4229 0.5382 0.4833 -0.0094 0.0174 -0.0438 2 TYR A C 42 O O . TYR A 6 ? 0.4117 0.5274 0.4710 -0.0082 0.0178 -0.0425 2 TYR A O 43 C CB . TYR A 6 ? 0.4533 0.5732 0.5200 -0.0115 0.0204 -0.0551 2 TYR A CB 44 C CG . TYR A 6 ? 0.3969 0.5069 0.4656 -0.0124 0.0230 -0.0553 2 TYR A CG 45 C CD1 . TYR A 6 ? 0.4061 0.5152 0.4766 -0.0141 0.0231 -0.0569 2 TYR A CD1 46 C CD2 . TYR A 6 ? 0.3982 0.5001 0.4669 -0.0115 0.0257 -0.0540 2 TYR A CD2 47 C CE1 . TYR A 6 ? 0.4124 0.5125 0.4847 -0.0150 0.0258 -0.0570 2 TYR A CE1 48 C CE2 . TYR A 6 ? 0.3899 0.4825 0.4601 -0.0121 0.0285 -0.0539 2 TYR A CE2 49 C CZ . TYR A 6 ? 0.3554 0.4472 0.4275 -0.0140 0.0284 -0.0553 2 TYR A CZ 50 O OH . TYR A 6 ? 0.3778 0.4607 0.4515 -0.0147 0.0314 -0.0553 2 TYR A OH 51 N N . VAL A 7 ? 0.4038 0.5128 0.4636 -0.0099 0.0173 -0.0408 3 VAL A N 52 C CA . VAL A 7 ? 0.3776 0.4798 0.4355 -0.0089 0.0177 -0.0361 3 VAL A CA 53 C C . VAL A 7 ? 0.3636 0.4575 0.4235 -0.0096 0.0200 -0.0370 3 VAL A C 54 O O . VAL A 7 ? 0.3497 0.4429 0.4101 -0.0107 0.0192 -0.0370 3 VAL A O 55 C CB . VAL A 7 ? 0.4005 0.5045 0.4549 -0.0088 0.0146 -0.0309 3 VAL A CB 56 C CG1 . VAL A 7 ? 0.3765 0.4737 0.4292 -0.0082 0.0148 -0.0264 3 VAL A CG1 57 C CG2 . VAL A 7 ? 0.3811 0.4928 0.4334 -0.0081 0.0128 -0.0297 3 VAL A CG2 58 N N . LEU A 8 ? 0.3348 0.4226 0.3958 -0.0088 0.0230 -0.0377 4 LEU A N 59 C CA . LEU A 8 ? 0.3425 0.4224 0.4057 -0.0095 0.0259 -0.0391 4 LEU A CA 60 C C . LEU A 8 ? 0.3326 0.4085 0.3944 -0.0097 0.0247 -0.0351 4 LEU A C 61 O O . LEU A 8 ? 0.3118 0.3849 0.3755 -0.0111 0.0257 -0.0369 4 LEU A O 62 C CB . LEU A 8 ? 0.3414 0.4147 0.4052 -0.0079 0.0294 -0.0391 4 LEU A CB 63 C CG . LEU A 8 ? 0.3653 0.4301 0.4316 -0.0086 0.0333 -0.0412 4 LEU A CG 64 C CD1 . LEU A 8 ? 0.4315 0.4920 0.4992 -0.0074 0.0371 -0.0438 4 LEU A CD1 65 C CD2 . LEU A 8 ? 0.3462 0.4040 0.4107 -0.0077 0.0335 -0.0364 4 LEU A CD2 66 N N . TYR A 9 ? 0.3096 0.3852 0.3680 -0.0085 0.0227 -0.0300 5 TYR A N 67 C CA . TYR A 9 ? 0.2999 0.3709 0.3571 -0.0086 0.0219 -0.0266 5 TYR A CA 68 C C . TYR A 9 ? 0.3039 0.3781 0.3613 -0.0102 0.0197 -0.0273 5 TYR A C 69 O O . TYR A 9 ? 0.2968 0.3669 0.3541 -0.0106 0.0197 -0.0259 5 TYR A O 70 C CB . TYR A 9 ? 0.2973 0.3672 0.3511 -0.0071 0.0203 -0.0214 5 TYR A CB 71 C CG . TYR A 9 ? 0.2656 0.3416 0.3169 -0.0075 0.0169 -0.0190 5 TYR A CG 72 C CD1 . TYR A 9 ? 0.2440 0.3203 0.2938 -0.0084 0.0146 -0.0169 5 TYR A CD1 73 C CD2 . TYR A 9 ? 0.2848 0.3659 0.3350 -0.0068 0.0162 -0.0186 5 TYR A CD2 74 C CE1 . TYR A 9 ? 0.2446 0.3258 0.2918 -0.0087 0.0119 -0.0144 5 TYR A CE1 75 C CE2 . TYR A 9 ? 0.2694 0.3559 0.3173 -0.0073 0.0135 -0.0162 5 TYR A CE2 76 C CZ . TYR A 9 ? 0.2820 0.3683 0.3283 -0.0082 0.0114 -0.0141 5 TYR A CZ 77 O OH . TYR A 9 ? 0.2393 0.3302 0.2832 -0.0087 0.0091 -0.0116 5 TYR A OH 78 N N . LYS A 10 ? 0.3090 0.3908 0.3666 -0.0108 0.0180 -0.0294 6 LYS A N 79 C CA . LYS A 10 ? 0.3127 0.3985 0.3702 -0.0117 0.0160 -0.0301 6 LYS A CA 80 C C . LYS A 10 ? 0.3204 0.4071 0.3818 -0.0132 0.0177 -0.0354 6 LYS A C 81 O O . LYS A 10 ? 0.3098 0.4002 0.3717 -0.0138 0.0164 -0.0366 6 LYS A O 82 C CB . LYS A 10 ? 0.3136 0.4078 0.3692 -0.0113 0.0133 -0.0294 6 LYS A CB 83 C CG . LYS A 10 ? 0.3066 0.4002 0.3582 -0.0104 0.0113 -0.0240 6 LYS A CG 84 C CD . LYS A 10 ? 0.3366 0.4379 0.3862 -0.0101 0.0091 -0.0231 6 LYS A CD 85 C CE . LYS A 10 ? 0.3929 0.4929 0.4388 -0.0098 0.0074 -0.0176 6 LYS A CE 86 N NZ . LYS A 10 ? 0.4785 0.5859 0.5226 -0.0094 0.0058 -0.0168 6 LYS A NZ 87 N N . ASP A 11 ? 0.3220 0.4054 0.3862 -0.0136 0.0209 -0.0386 7 ASP A N 88 C CA . ASP A 11 ? 0.3198 0.4041 0.3881 -0.0154 0.0230 -0.0444 7 ASP A CA 89 C C . ASP A 11 ? 0.3179 0.3946 0.3875 -0.0162 0.0250 -0.0438 7 ASP A C 90 O O . ASP A 11 ? 0.3200 0.3888 0.3897 -0.0157 0.0277 -0.0423 7 ASP A O 91 C CB . ASP A 11 ? 0.3218 0.4053 0.3923 -0.0156 0.0259 -0.0483 7 ASP A CB 92 C CG . ASP A 11 ? 0.3622 0.4463 0.4374 -0.0179 0.0286 -0.0548 7 ASP A CG 93 O OD1 . ASP A 11 ? 0.3345 0.4194 0.4116 -0.0182 0.0307 -0.0586 7 ASP A OD1 94 O OD2 . ASP A 11 ? 0.3175 0.4013 0.3945 -0.0194 0.0289 -0.0561 7 ASP A OD2 95 N N . ALA A 12 ? 0.3069 0.3864 0.3774 -0.0173 0.0239 -0.0448 8 ALA A N 96 C CA . ALA A 12 ? 0.3294 0.4028 0.4010 -0.0181 0.0254 -0.0442 8 ALA A CA 97 C C . ALA A 12 ? 0.3518 0.4201 0.4275 -0.0198 0.0298 -0.0483 8 ALA A C 98 O O . ALA A 12 ? 0.3447 0.4064 0.4211 -0.0202 0.0318 -0.0471 8 ALA A O 99 C CB . ALA A 12 ? 0.3268 0.4059 0.3986 -0.0187 0.0230 -0.0450 8 ALA A CB 100 N N . THR A 13 ? 0.3686 0.4398 0.4471 -0.0209 0.0316 -0.0534 9 THR A N 101 C CA . THR A 13 ? 0.3760 0.4418 0.4586 -0.0228 0.0363 -0.0576 9 THR A CA 102 C C . THR A 13 ? 0.3930 0.4493 0.4746 -0.0214 0.0395 -0.0553 9 THR A C 103 O O . THR A 13 ? 0.4070 0.4568 0.4914 -0.0226 0.0439 -0.0578 9 THR A O 104 C CB . THR A 13 ? 0.3870 0.4597 0.4733 -0.0249 0.0372 -0.0647 9 THR A CB 105 O OG1 . THR A 13 ? 0.3552 0.4301 0.4401 -0.0235 0.0367 -0.0649 9 THR A OG1 106 C CG2 . THR A 13 ? 0.3797 0.4628 0.4666 -0.0257 0.0338 -0.0668 9 THR A CG2 107 N N . LYS A 14 ? 0.3800 0.4355 0.4576 -0.0187 0.0376 -0.0504 10 LYS A N 108 C CA . LYS A 14 ? 0.3698 0.4178 0.4461 -0.0167 0.0404 -0.0481 10 LYS A CA 109 C C . LYS A 14 ? 0.3695 0.4092 0.4441 -0.0154 0.0416 -0.0433 10 LYS A C 110 O O . LYS A 14 ? 0.3715 0.4127 0.4444 -0.0153 0.0390 -0.0404 10 LYS A O 111 C CB . LYS A 14 ? 0.3627 0.4148 0.4357 -0.0144 0.0376 -0.0451 10 LYS A CB 112 C CG . LYS A 14 ? 0.3962 0.4552 0.4708 -0.0151 0.0373 -0.0497 10 LYS A CG 113 C CD . LYS A 14 ? 0.4069 0.4602 0.4835 -0.0149 0.0418 -0.0529 10 LYS A CD 114 C CE . LYS A 14 ? 0.4782 0.5384 0.5571 -0.0160 0.0418 -0.0585 10 LYS A CE 115 N NZ . LYS A 14 ? 0.5471 0.6012 0.6269 -0.0150 0.0459 -0.0603 10 LYS A NZ 116 N N . PRO A 15 ? 0.3746 0.4059 0.4492 -0.0141 0.0457 -0.0423 11 PRO A N 117 C CA . PRO A 15 ? 0.3747 0.3983 0.4473 -0.0122 0.0471 -0.0376 11 PRO A CA 118 C C . PRO A 15 ? 0.3523 0.3785 0.4207 -0.0099 0.0432 -0.0321 11 PRO A C 119 O O . PRO A 15 ? 0.3363 0.3672 0.4029 -0.0087 0.0410 -0.0313 11 PRO A O 120 C CB . PRO A 15 ? 0.3844 0.4006 0.4570 -0.0103 0.0516 -0.0374 11 PRO A CB 121 C CG . PRO A 15 ? 0.4070 0.4241 0.4837 -0.0129 0.0542 -0.0439 11 PRO A CG 122 C CD . PRO A 15 ? 0.3935 0.4217 0.4707 -0.0145 0.0497 -0.0465 11 PRO A CD 123 N N . VAL A 16 ? 0.3366 0.3595 0.4034 -0.0092 0.0427 -0.0285 12 VAL A N 124 C CA . VAL A 16 ? 0.3167 0.3419 0.3796 -0.0074 0.0390 -0.0236 12 VAL A CA 125 C C . VAL A 16 ? 0.3198 0.3437 0.3802 -0.0044 0.0395 -0.0208 12 VAL A C 126 O O . VAL A 16 ? 0.2987 0.3280 0.3571 -0.0037 0.0363 -0.0192 12 VAL A O 127 C CB . VAL A 16 ? 0.3307 0.3513 0.3925 -0.0069 0.0392 -0.0204 12 VAL A CB 128 C CG1 . VAL A 16 ? 0.2934 0.3147 0.3512 -0.0045 0.0365 -0.0153 12 VAL A CG1 129 C CG2 . VAL A 16 ? 0.3169 0.3407 0.3806 -0.0097 0.0376 -0.0227 12 VAL A CG2 130 N N . GLU A 17 ? 0.3197 0.3367 0.3803 -0.0025 0.0437 -0.0203 13 GLU A N 131 C CA . GLU A 17 ? 0.3326 0.3491 0.3905 0.0009 0.0441 -0.0175 13 GLU A CA 132 C C . GLU A 17 ? 0.3279 0.3504 0.3861 0.0008 0.0427 -0.0198 13 GLU A C 133 O O . GLU A 17 ? 0.3287 0.3547 0.3844 0.0028 0.0408 -0.0173 13 GLU A O 134 C CB . GLU A 17 ? 0.3642 0.3721 0.4220 0.0035 0.0491 -0.0166 13 GLU A CB 135 C CG . GLU A 17 ? 0.3674 0.3690 0.4244 0.0044 0.0510 -0.0137 13 GLU A CG 136 C CD . GLU A 17 ? 0.4372 0.4420 0.4908 0.0061 0.0473 -0.0091 13 GLU A CD 137 O OE1 . GLU A 17 ? 0.4272 0.4322 0.4810 0.0045 0.0457 -0.0085 13 GLU A OE1 138 O OE2 . GLU A 17 ? 0.4178 0.4252 0.4687 0.0088 0.0460 -0.0066 13 GLU A OE2 139 N N . ASP A 18 ? 0.3212 0.3455 0.3825 -0.0017 0.0437 -0.0247 14 ASP A N 140 C CA . ASP A 18 ? 0.3377 0.3679 0.3993 -0.0017 0.0425 -0.0270 14 ASP A CA 141 C C . ASP A 18 ? 0.3057 0.3444 0.3657 -0.0027 0.0374 -0.0257 14 ASP A C 142 O O . ASP A 18 ? 0.3032 0.3469 0.3616 -0.0016 0.0355 -0.0247 14 ASP A O 143 C CB . ASP A 18 ? 0.3378 0.3686 0.4033 -0.0042 0.0446 -0.0330 14 ASP A CB 144 C CG . ASP A 18 ? 0.4202 0.4422 0.4874 -0.0035 0.0501 -0.0349 14 ASP A CG 145 O OD1 . ASP A 18 ? 0.4517 0.4678 0.5168 -0.0003 0.0523 -0.0314 14 ASP A OD1 146 O OD2 . ASP A 18 ? 0.4149 0.4361 0.4857 -0.0062 0.0522 -0.0399 14 ASP A OD2 147 N N . ARG A 19 ? 0.2981 0.3382 0.3585 -0.0048 0.0354 -0.0255 15 ARG A N 148 C CA . ARG A 19 ? 0.2837 0.3309 0.3422 -0.0055 0.0308 -0.0237 15 ARG A CA 149 C C . ARG A 19 ? 0.2923 0.3396 0.3473 -0.0034 0.0289 -0.0186 15 ARG A C 150 O O . ARG A 19 ? 0.2909 0.3440 0.3441 -0.0032 0.0262 -0.0172 15 ARG A O 151 C CB . ARG A 19 ? 0.2824 0.3306 0.3418 -0.0077 0.0292 -0.0245 15 ARG A CB 152 C CG . ARG A 19 ? 0.2928 0.3429 0.3560 -0.0099 0.0307 -0.0300 15 ARG A CG 153 C CD . ARG A 19 ? 0.2804 0.3322 0.3446 -0.0118 0.0293 -0.0309 15 ARG A CD 154 N NE . ARG A 19 ? 0.2662 0.3250 0.3283 -0.0120 0.0251 -0.0295 15 ARG A NE 155 C CZ . ARG A 19 ? 0.3133 0.3745 0.3753 -0.0129 0.0231 -0.0293 15 ARG A CZ 156 N NH1 . ARG A 19 ? 0.2742 0.3315 0.3380 -0.0139 0.0247 -0.0304 15 ARG A NH1 157 N NH2 . ARG A 19 ? 0.2327 0.2999 0.2925 -0.0128 0.0197 -0.0278 15 ARG A NH2 158 N N . VAL A 20 ? 0.2991 0.3403 0.3530 -0.0020 0.0303 -0.0159 16 VAL A N 159 C CA . VAL A 20 ? 0.2987 0.3400 0.3494 0.0002 0.0290 -0.0114 16 VAL A CA 160 C C . VAL A 20 ? 0.3153 0.3598 0.3649 0.0022 0.0292 -0.0108 16 VAL A C 161 O O . VAL A 20 ? 0.3093 0.3590 0.3569 0.0023 0.0264 -0.0088 16 VAL A O 162 C CB . VAL A 20 ? 0.3064 0.3408 0.3563 0.0020 0.0312 -0.0089 16 VAL A CB 163 C CG1 . VAL A 20 ? 0.2822 0.3176 0.3289 0.0046 0.0300 -0.0047 16 VAL A CG1 164 C CG2 . VAL A 20 ? 0.2973 0.3295 0.3478 0.0001 0.0304 -0.0088 16 VAL A CG2 165 N N . ALA A 21 ? 0.3236 0.3648 0.3746 0.0036 0.0326 -0.0128 17 ALA A N 166 C CA . ALA A 21 ? 0.3279 0.3715 0.3778 0.0060 0.0333 -0.0124 17 ALA A CA 167 C C . ALA A 21 ? 0.3235 0.3751 0.3738 0.0044 0.0307 -0.0143 17 ALA A C 168 O O . ALA A 21 ? 0.3322 0.3889 0.3807 0.0056 0.0290 -0.0125 17 ALA A O 169 C CB . ALA A 21 ? 0.3442 0.3819 0.3956 0.0076 0.0377 -0.0146 17 ALA A CB 170 N N . ASP A 22 ? 0.3225 0.3756 0.3751 0.0018 0.0305 -0.0180 18 ASP A N 171 C CA . ASP A 22 ? 0.3309 0.3918 0.3838 0.0004 0.0282 -0.0199 18 ASP A CA 172 C C . ASP A 22 ? 0.3141 0.3805 0.3645 -0.0002 0.0243 -0.0165 18 ASP A C 173 O O . ASP A 22 ? 0.3065 0.3789 0.3558 0.0002 0.0228 -0.0159 18 ASP A O 174 C CB . ASP A 22 ? 0.3203 0.3829 0.3760 -0.0021 0.0284 -0.0244 18 ASP A CB 175 C CG . ASP A 22 ? 0.3610 0.4322 0.4167 -0.0030 0.0263 -0.0263 18 ASP A CG 176 O OD1 . ASP A 22 ? 0.3674 0.4403 0.4238 -0.0019 0.0277 -0.0285 18 ASP A OD1 177 O OD2 . ASP A 22 ? 0.3613 0.4376 0.4161 -0.0044 0.0232 -0.0255 18 ASP A OD2 178 N N . LEU A 23 ? 0.3013 0.3656 0.3509 -0.0013 0.0229 -0.0144 19 LEU A N 179 C CA . LEU A 23 ? 0.2755 0.3441 0.3228 -0.0022 0.0195 -0.0114 19 LEU A CA 180 C C . LEU A 23 ? 0.2878 0.3569 0.3328 -0.0004 0.0190 -0.0079 19 LEU A C 181 O O . LEU A 23 ? 0.2920 0.3667 0.3356 -0.0007 0.0170 -0.0064 19 LEU A O 182 C CB . LEU A 23 ? 0.2817 0.3474 0.3288 -0.0037 0.0183 -0.0105 19 LEU A CB 183 C CG . LEU A 23 ? 0.2757 0.3437 0.3203 -0.0046 0.0152 -0.0071 19 LEU A CG 184 C CD1 . LEU A 23 ? 0.2691 0.3444 0.3128 -0.0057 0.0131 -0.0072 19 LEU A CD1 185 C CD2 . LEU A 23 ? 0.2410 0.3057 0.2856 -0.0058 0.0144 -0.0066 19 LEU A CD2 186 N N . LEU A 24 ? 0.2860 0.3498 0.3308 0.0016 0.0210 -0.0067 20 LEU A N 187 C CA . LEU A 24 ? 0.3015 0.3665 0.3441 0.0036 0.0206 -0.0035 20 LEU A CA 188 C C . LEU A 24 ? 0.3062 0.3770 0.3484 0.0048 0.0205 -0.0038 20 LEU A C 189 O O . LEU A 24 ? 0.2989 0.3745 0.3395 0.0050 0.0187 -0.0015 20 LEU A O 190 C CB . LEU A 24 ? 0.2977 0.3562 0.3402 0.0064 0.0235 -0.0026 20 LEU A CB 191 C CG . LEU A 24 ? 0.3142 0.3740 0.3545 0.0090 0.0233 0.0007 20 LEU A CG 192 C CD1 . LEU A 24 ? 0.2974 0.3596 0.3359 0.0075 0.0202 0.0033 20 LEU A CD1 193 C CD2 . LEU A 24 ? 0.3079 0.3609 0.3481 0.0123 0.0268 0.0013 20 LEU A CD2 194 N N . GLY A 25 ? 0.3097 0.3799 0.3536 0.0056 0.0226 -0.0067 21 GLY A N 195 C CA . GLY A 25 ? 0.3253 0.4004 0.3690 0.0072 0.0231 -0.0074 21 GLY A CA 196 C C . GLY A 25 ? 0.3256 0.4085 0.3689 0.0051 0.0203 -0.0077 21 GLY A C 197 O O . GLY A 25 ? 0.3295 0.4175 0.3724 0.0062 0.0202 -0.0078 21 GLY A O 198 N N . ARG A 26 ? 0.3083 0.3922 0.3517 0.0023 0.0182 -0.0076 22 ARG A N 199 C CA . ARG A 26 ? 0.3074 0.3983 0.3499 0.0004 0.0157 -0.0072 22 ARG A CA 200 C C . ARG A 26 ? 0.3063 0.3994 0.3467 -0.0008 0.0133 -0.0036 22 ARG A C 201 O O . ARG A 26 ? 0.3022 0.4008 0.3417 -0.0024 0.0115 -0.0028 22 ARG A O 202 C CB . ARG A 26 ? 0.3059 0.3970 0.3495 -0.0018 0.0149 -0.0094 22 ARG A CB 203 C CG . ARG A 26 ? 0.2941 0.3843 0.3402 -0.0013 0.0171 -0.0138 22 ARG A CG 204 C CD . ARG A 26 ? 0.3076 0.3980 0.3549 -0.0034 0.0162 -0.0158 22 ARG A CD 205 N NE . ARG A 26 ? 0.2852 0.3738 0.3352 -0.0034 0.0185 -0.0204 22 ARG A NE 206 C CZ . ARG A 26 ? 0.3806 0.4744 0.4319 -0.0038 0.0186 -0.0239 22 ARG A CZ 207 N NH1 . ARG A 26 ? 0.3797 0.4808 0.4296 -0.0038 0.0166 -0.0229 22 ARG A NH1 208 N NH2 . ARG A 26 ? 0.3820 0.4740 0.4362 -0.0042 0.0208 -0.0285 22 ARG A NH2 209 N N . MET A 27 ? 0.2959 0.3846 0.3355 -0.0003 0.0134 -0.0016 23 MET A N 210 C CA . MET A 27 ? 0.2838 0.3736 0.3217 -0.0020 0.0112 0.0014 23 MET A CA 211 C C . MET A 27 ? 0.3082 0.4031 0.3448 -0.0014 0.0105 0.0033 23 MET A C 212 O O . MET A 27 ? 0.3209 0.4161 0.3577 0.0012 0.0119 0.0033 23 MET A O 213 C CB . MET A 27 ? 0.2856 0.3689 0.3232 -0.0018 0.0115 0.0024 23 MET A CB 214 C CG . MET A 27 ? 0.2620 0.3409 0.3008 -0.0030 0.0117 0.0007 23 MET A CG 215 S SD . MET A 27 ? 0.2958 0.3668 0.3346 -0.0021 0.0128 0.0016 23 MET A SD 216 C CE . MET A 27 ? 0.2543 0.3266 0.2908 -0.0041 0.0099 0.0046 23 MET A CE 217 N N . THR A 28 ? 0.3062 0.4050 0.3416 -0.0038 0.0085 0.0050 24 THR A N 218 C CA . THR A 28 ? 0.3220 0.4257 0.3564 -0.0039 0.0078 0.0067 24 THR A CA 219 C C . THR A 28 ? 0.3264 0.4267 0.3601 -0.0035 0.0076 0.0082 24 THR A C 220 O O . THR A 28 ? 0.3139 0.4080 0.3476 -0.0037 0.0077 0.0083 24 THR A O 221 C CB . THR A 28 ? 0.3261 0.4343 0.3596 -0.0072 0.0060 0.0080 24 THR A CB 222 O OG1 . THR A 28 ? 0.2884 0.3920 0.3210 -0.0093 0.0049 0.0091 24 THR A OG1 223 C CG2 . THR A 28 ? 0.2984 0.4102 0.3324 -0.0077 0.0060 0.0066 24 THR A CG2 224 N N . LEU A 29 ? 0.3161 0.4209 0.3492 -0.0029 0.0072 0.0094 25 LEU A N 225 C CA . LEU A 29 ? 0.3042 0.4073 0.3365 -0.0028 0.0067 0.0107 25 LEU A CA 226 C C . LEU A 29 ? 0.2961 0.3960 0.3276 -0.0062 0.0051 0.0116 25 LEU A C 227 O O . LEU A 29 ? 0.2683 0.3631 0.2994 -0.0059 0.0051 0.0121 25 LEU A O 228 C CB . LEU A 29 ? 0.3169 0.4272 0.3487 -0.0020 0.0063 0.0115 25 LEU A CB 229 C CG . LEU A 29 ? 0.3228 0.4327 0.3538 -0.0020 0.0056 0.0126 25 LEU A CG 230 C CD1 . LEU A 29 ? 0.2854 0.3899 0.3162 0.0017 0.0071 0.0126 25 LEU A CD1 231 C CD2 . LEU A 29 ? 0.3154 0.4344 0.3463 -0.0018 0.0050 0.0129 25 LEU A CD2 232 N N . ALA A 30 ? 0.2786 0.3813 0.3098 -0.0092 0.0040 0.0120 26 ALA A N 233 C CA . ALA A 30 ? 0.2962 0.3952 0.3265 -0.0122 0.0027 0.0130 26 ALA A CA 234 C C . ALA A 30 ? 0.3014 0.3932 0.3318 -0.0116 0.0030 0.0124 26 ALA A C 235 O O . ALA A 30 ? 0.2832 0.3703 0.3129 -0.0126 0.0024 0.0131 26 ALA A O 236 C CB . ALA A 30 ? 0.2942 0.3969 0.3238 -0.0153 0.0019 0.0138 26 ALA A CB 237 N N . GLU A 31 ? 0.2951 0.3864 0.3265 -0.0102 0.0040 0.0109 27 GLU A N 238 C CA . GLU A 31 ? 0.2857 0.3714 0.3177 -0.0097 0.0045 0.0099 27 GLU A CA 239 C C . GLU A 31 ? 0.2815 0.3622 0.3140 -0.0077 0.0055 0.0097 27 GLU A C 240 O O . GLU A 31 ? 0.2847 0.3603 0.3171 -0.0080 0.0054 0.0097 27 GLU A O 241 C CB . GLU A 31 ? 0.2786 0.3660 0.3119 -0.0089 0.0053 0.0078 27 GLU A CB 242 C CG . GLU A 31 ? 0.2483 0.3398 0.2808 -0.0110 0.0042 0.0083 27 GLU A CG 243 C CD . GLU A 31 ? 0.2808 0.3763 0.3144 -0.0101 0.0048 0.0063 27 GLU A CD 244 O OE1 . GLU A 31 ? 0.2707 0.3669 0.3056 -0.0081 0.0063 0.0046 27 GLU A OE1 245 O OE2 . GLU A 31 ? 0.2923 0.3900 0.3253 -0.0113 0.0040 0.0063 27 GLU A OE2 246 N N . LYS A 32 ? 0.2835 0.3659 0.3163 -0.0053 0.0067 0.0096 28 LYS A N 247 C CA . LYS A 32 ? 0.2887 0.3669 0.3215 -0.0029 0.0080 0.0099 28 LYS A CA 248 C C . LYS A 32 ? 0.2877 0.3644 0.3192 -0.0038 0.0067 0.0115 28 LYS A C 249 O O . LYS A 32 ? 0.2720 0.3434 0.3033 -0.0034 0.0070 0.0117 28 LYS A O 250 C CB . LYS A 32 ? 0.2889 0.3700 0.3219 0.0001 0.0095 0.0098 28 LYS A CB 251 C CG . LYS A 32 ? 0.2911 0.3712 0.3255 0.0017 0.0114 0.0080 28 LYS A CG 252 C CD . LYS A 32 ? 0.2977 0.3808 0.3321 0.0051 0.0130 0.0081 28 LYS A CD 253 C CE . LYS A 32 ? 0.3167 0.3997 0.3524 0.0062 0.0148 0.0059 28 LYS A CE 254 N NZ . LYS A 32 ? 0.3008 0.3852 0.3362 0.0101 0.0169 0.0060 28 LYS A NZ 255 N N . ILE A 33 ? 0.2792 0.3609 0.3098 -0.0052 0.0053 0.0125 29 ILE A N 256 C CA . ILE A 33 ? 0.2782 0.3590 0.3077 -0.0062 0.0042 0.0136 29 ILE A CA 257 C C . ILE A 33 ? 0.2726 0.3487 0.3015 -0.0088 0.0031 0.0137 29 ILE A C 258 O O . ILE A 33 ? 0.2708 0.3431 0.2990 -0.0089 0.0027 0.0142 29 ILE A O 259 C CB . ILE A 33 ? 0.2618 0.3495 0.2908 -0.0074 0.0031 0.0141 29 ILE A CB 260 C CG1 . ILE A 33 ? 0.2683 0.3602 0.2974 -0.0039 0.0042 0.0141 29 ILE A CG1 261 C CG2 . ILE A 33 ? 0.2696 0.3564 0.2975 -0.0098 0.0017 0.0147 29 ILE A CG2 262 C CD1 . ILE A 33 ? 0.2870 0.3875 0.3159 -0.0051 0.0033 0.0143 29 ILE A CD1 263 N N . GLY A 34 ? 0.2723 0.3488 0.3015 -0.0106 0.0027 0.0134 30 GLY A N 264 C CA . GLY A 34 ? 0.2748 0.3468 0.3033 -0.0123 0.0019 0.0136 30 GLY A CA 265 C C . GLY A 34 ? 0.2527 0.3189 0.2817 -0.0107 0.0027 0.0130 30 GLY A C 266 O O . GLY A 34 ? 0.2640 0.3262 0.2922 -0.0115 0.0020 0.0135 30 GLY A O 267 N N . GLN A 35 ? 0.2572 0.3228 0.2877 -0.0085 0.0043 0.0117 31 GLN A N 268 C CA . GLN A 35 ? 0.2627 0.3230 0.2940 -0.0072 0.0054 0.0110 31 GLN A CA 269 C C . GLN A 35 ? 0.2701 0.3275 0.3005 -0.0061 0.0055 0.0121 31 GLN A C 270 O O . GLN A 35 ? 0.2643 0.3172 0.2947 -0.0059 0.0057 0.0120 31 GLN A O 271 C CB . GLN A 35 ? 0.2707 0.3306 0.3038 -0.0051 0.0076 0.0094 31 GLN A CB 272 C CG . GLN A 35 ? 0.2578 0.3194 0.2922 -0.0061 0.0077 0.0075 31 GLN A CG 273 C CD . GLN A 35 ? 0.2552 0.3142 0.2896 -0.0076 0.0068 0.0070 31 GLN A CD 274 O OE1 . GLN A 35 ? 0.2212 0.2759 0.2564 -0.0069 0.0078 0.0064 31 GLN A OE1 275 N NE2 . GLN A 35 ? 0.2178 0.2794 0.2512 -0.0094 0.0051 0.0075 31 GLN A NE2 276 N N . MET A 36 ? 0.2651 0.3257 0.2948 -0.0053 0.0053 0.0130 32 MET A N 277 C CA . MET A 36 ? 0.2601 0.3191 0.2888 -0.0039 0.0054 0.0139 32 MET A CA 278 C C . MET A 36 ? 0.2483 0.3067 0.2756 -0.0061 0.0035 0.0146 32 MET A C 279 O O . MET A 36 ? 0.2578 0.3155 0.2843 -0.0052 0.0033 0.0151 32 MET A O 280 C CB . MET A 36 ? 0.2545 0.3185 0.2829 -0.0019 0.0059 0.0145 32 MET A CB 281 C CG . MET A 36 ? 0.2649 0.3288 0.2944 0.0010 0.0083 0.0139 32 MET A CG 282 S SD . MET A 36 ? 0.2833 0.3542 0.3122 0.0038 0.0088 0.0146 32 MET A SD 283 C CE . MET A 36 ? 0.2499 0.3203 0.2773 0.0063 0.0089 0.0160 32 MET A CE 284 N N . THR A 37 ? 0.2390 0.2979 0.2661 -0.0089 0.0022 0.0145 33 THR A N 285 C CA . THR A 37 ? 0.2385 0.2965 0.2641 -0.0113 0.0006 0.0151 33 THR A CA 286 C C . THR A 37 ? 0.2524 0.3047 0.2775 -0.0121 0.0002 0.0151 33 THR A C 287 O O . THR A 37 ? 0.2358 0.2874 0.2613 -0.0127 0.0002 0.0148 33 THR A O 288 C CB . THR A 37 ? 0.2645 0.3267 0.2897 -0.0141 -0.0003 0.0155 33 THR A CB 289 O OG1 . THR A 37 ? 0.2434 0.3116 0.2693 -0.0132 0.0001 0.0153 33 THR A OG1 290 C CG2 . THR A 37 ? 0.2644 0.3253 0.2882 -0.0168 -0.0016 0.0160 33 THR A CG2 291 N N . GLN A 38 ? 0.2392 0.2883 0.2633 -0.0119 -0.0003 0.0154 34 GLN A N 292 C CA . GLN A 38 ? 0.2412 0.2852 0.2646 -0.0125 -0.0008 0.0154 34 GLN A CA 293 C C . GLN A 38 ? 0.2430 0.2860 0.2647 -0.0149 -0.0022 0.0160 34 GLN A C 294 O O . GLN A 38 ? 0.2500 0.2945 0.2712 -0.0153 -0.0026 0.0160 34 GLN A O 295 C CB . GLN A 38 ? 0.2429 0.2833 0.2666 -0.0103 0.0000 0.0152 34 GLN A CB 296 C CG . GLN A 38 ? 0.2015 0.2369 0.2244 -0.0107 -0.0006 0.0151 34 GLN A CG 297 C CD . GLN A 38 ? 0.2472 0.2796 0.2705 -0.0086 0.0003 0.0149 34 GLN A CD 298 O OE1 . GLN A 38 ? 0.2364 0.2682 0.2587 -0.0081 -0.0001 0.0153 34 GLN A OE1 299 N NE2 . GLN A 38 ? 0.2262 0.2569 0.2510 -0.0074 0.0016 0.0142 34 GLN A NE2 300 N N . ILE A 39 ? 0.2597 0.3000 0.2804 -0.0164 -0.0028 0.0164 35 ILE A N 301 C CA . ILE A 39 ? 0.2629 0.3014 0.2818 -0.0189 -0.0037 0.0171 35 ILE A CA 302 C C . ILE A 39 ? 0.2571 0.2897 0.2746 -0.0186 -0.0041 0.0173 35 ILE A C 303 O O . ILE A 39 ? 0.2556 0.2867 0.2736 -0.0171 -0.0038 0.0172 35 ILE A O 304 C CB . ILE A 39 ? 0.2532 0.2943 0.2716 -0.0213 -0.0039 0.0178 35 ILE A CB 305 C CG1 . ILE A 39 ? 0.2757 0.3155 0.2937 -0.0209 -0.0037 0.0185 35 ILE A CG1 306 C CG2 . ILE A 39 ? 0.2367 0.2844 0.2566 -0.0213 -0.0035 0.0174 35 ILE A CG2 307 C CD1 . ILE A 39 ? 0.2331 0.2751 0.2502 -0.0232 -0.0037 0.0196 35 ILE A CD1 308 N N . GLU A 40 ? 0.2574 0.2872 0.2733 -0.0202 -0.0047 0.0175 36 GLU A N 309 C CA . GLU A 40 ? 0.2553 0.2793 0.2695 -0.0200 -0.0051 0.0179 36 GLU A CA 310 C C . GLU A 40 ? 0.2695 0.2923 0.2827 -0.0205 -0.0050 0.0191 36 GLU A C 311 O O . GLU A 40 ? 0.2612 0.2860 0.2740 -0.0224 -0.0048 0.0199 36 GLU A O 312 C CB . GLU A 40 ? 0.2718 0.2932 0.2845 -0.0220 -0.0055 0.0177 36 GLU A CB 313 C CG . GLU A 40 ? 0.2618 0.2801 0.2740 -0.0205 -0.0059 0.0168 36 GLU A CG 314 C CD . GLU A 40 ? 0.2968 0.3094 0.3076 -0.0191 -0.0060 0.0173 36 GLU A CD 315 O OE1 . GLU A 40 ? 0.2692 0.2801 0.2791 -0.0194 -0.0059 0.0184 36 GLU A OE1 316 O OE2 . GLU A 40 ? 0.2556 0.2659 0.2662 -0.0174 -0.0062 0.0167 36 GLU A OE2 317 N N . ARG A 41 ? 0.2647 0.2843 0.2773 -0.0187 -0.0051 0.0193 37 ARG A N 318 C CA . ARG A 41 ? 0.2603 0.2783 0.2711 -0.0188 -0.0051 0.0207 37 ARG A CA 319 C C . ARG A 41 ? 0.2879 0.3025 0.2963 -0.0213 -0.0050 0.0219 37 ARG A C 320 O O . ARG A 41 ? 0.2914 0.3060 0.2985 -0.0221 -0.0047 0.0234 37 ARG A O 321 C CB . ARG A 41 ? 0.2639 0.2787 0.2739 -0.0165 -0.0053 0.0207 37 ARG A CB 322 C CG . ARG A 41 ? 0.2331 0.2428 0.2419 -0.0160 -0.0056 0.0203 37 ARG A CG 323 C CD . ARG A 41 ? 0.2417 0.2480 0.2489 -0.0138 -0.0059 0.0208 37 ARG A CD 324 N NE . ARG A 41 ? 0.2669 0.2700 0.2711 -0.0145 -0.0057 0.0228 37 ARG A NE 325 C CZ . ARG A 41 ? 0.2753 0.2728 0.2771 -0.0157 -0.0056 0.0236 37 ARG A CZ 326 N NH1 . ARG A 41 ? 0.2745 0.2696 0.2765 -0.0163 -0.0059 0.0224 37 ARG A NH1 327 N NH2 . ARG A 41 ? 0.2649 0.2589 0.2638 -0.0160 -0.0051 0.0256 37 ARG A NH2 328 N N . LEU A 42 ? 0.2834 0.2950 0.2913 -0.0225 -0.0052 0.0213 38 LEU A N 329 C CA . LEU A 42 ? 0.2909 0.2987 0.2966 -0.0253 -0.0049 0.0221 38 LEU A CA 330 C C . LEU A 42 ? 0.3057 0.3174 0.3120 -0.0281 -0.0043 0.0226 38 LEU A C 331 O O . LEU A 42 ? 0.3026 0.3111 0.3070 -0.0303 -0.0036 0.0239 38 LEU A O 332 C CB . LEU A 42 ? 0.2915 0.2964 0.2969 -0.0265 -0.0051 0.0207 38 LEU A CB 333 C CG . LEU A 42 ? 0.3356 0.3352 0.3397 -0.0242 -0.0055 0.0205 38 LEU A CG 334 C CD1 . LEU A 42 ? 0.3465 0.3453 0.3509 -0.0247 -0.0059 0.0186 38 LEU A CD1 335 C CD2 . LEU A 42 ? 0.3713 0.3642 0.3722 -0.0242 -0.0050 0.0222 38 LEU A CD2 336 N N . VAL A 43 ? 0.2862 0.3044 0.2948 -0.0279 -0.0045 0.0219 39 VAL A N 337 C CA . VAL A 43 ? 0.3028 0.3254 0.3119 -0.0304 -0.0039 0.0224 39 VAL A CA 338 C C . VAL A 43 ? 0.3123 0.3391 0.3222 -0.0291 -0.0037 0.0232 39 VAL A C 339 O O . VAL A 43 ? 0.3196 0.3510 0.3302 -0.0307 -0.0033 0.0235 39 VAL A O 340 C CB . VAL A 43 ? 0.2848 0.3127 0.2960 -0.0318 -0.0042 0.0206 39 VAL A CB 341 C CG1 . VAL A 43 ? 0.3125 0.3375 0.3232 -0.0334 -0.0044 0.0194 39 VAL A CG1 342 C CG2 . VAL A 43 ? 0.2753 0.3074 0.2886 -0.0287 -0.0045 0.0196 39 VAL A CG2 343 N N . ALA A 44 ? 0.2854 0.3113 0.2953 -0.0262 -0.0040 0.0233 40 ALA A N 344 C CA . ALA A 44 ? 0.2907 0.3208 0.3014 -0.0248 -0.0038 0.0236 40 ALA A CA 345 C C . ALA A 44 ? 0.3167 0.3450 0.3249 -0.0251 -0.0034 0.0258 40 ALA A C 346 O O . ALA A 44 ? 0.3150 0.3376 0.3208 -0.0249 -0.0033 0.0269 40 ALA A O 347 C CB . ALA A 44 ? 0.2743 0.3049 0.2863 -0.0218 -0.0041 0.0224 40 ALA A CB 348 N N . THR A 45 ? 0.3162 0.3496 0.3248 -0.0254 -0.0030 0.0263 41 THR A N 349 C CA . THR A 45 ? 0.3205 0.3536 0.3268 -0.0249 -0.0025 0.0284 41 THR A CA 350 C C . THR A 45 ? 0.3018 0.3420 0.3100 -0.0233 -0.0026 0.0275 41 THR A C 351 O O . THR A 45 ? 0.2920 0.3362 0.3029 -0.0234 -0.0028 0.0256 41 THR A O 352 C CB . THR A 45 ? 0.3277 0.3597 0.3324 -0.0279 -0.0015 0.0304 41 THR A CB 353 O OG1 . THR A 45 ? 0.3294 0.3678 0.3361 -0.0295 -0.0013 0.0297 41 THR A OG1 354 C CG2 . THR A 45 ? 0.3665 0.3921 0.3700 -0.0302 -0.0011 0.0306 41 THR A CG2 355 N N . PRO A 46 ? 0.3249 0.3668 0.3317 -0.0217 -0.0025 0.0287 42 PRO A N 356 C CA . PRO A 46 ? 0.3153 0.3643 0.3238 -0.0205 -0.0026 0.0274 42 PRO A CA 357 C C . PRO A 46 ? 0.3219 0.3758 0.3318 -0.0225 -0.0022 0.0272 42 PRO A C 358 O O . PRO A 46 ? 0.3041 0.3625 0.3167 -0.0218 -0.0023 0.0251 42 PRO A O 359 C CB . PRO A 46 ? 0.3433 0.3931 0.3491 -0.0187 -0.0024 0.0294 42 PRO A CB 360 C CG . PRO A 46 ? 0.3403 0.3835 0.3440 -0.0175 -0.0026 0.0303 42 PRO A CG 361 C CD . PRO A 46 ? 0.3319 0.3696 0.3352 -0.0205 -0.0022 0.0310 42 PRO A CD 362 N N . ASP A 47 ? 0.3236 0.3764 0.3320 -0.0250 -0.0015 0.0293 43 ASP A N 363 C CA . ASP A 47 ? 0.3415 0.3997 0.3514 -0.0270 -0.0010 0.0289 43 ASP A CA 364 C C . ASP A 47 ? 0.3186 0.3780 0.3311 -0.0277 -0.0014 0.0267 43 ASP A C 365 O O . ASP A 47 ? 0.3184 0.3835 0.3329 -0.0275 -0.0014 0.0254 43 ASP A O 366 C CB . ASP A 47 ? 0.3572 0.4142 0.3650 -0.0300 0.0001 0.0314 43 ASP A CB 367 C CG . ASP A 47 ? 0.4387 0.4965 0.4439 -0.0290 0.0008 0.0339 43 ASP A CG 368 O OD1 . ASP A 47 ? 0.4990 0.5620 0.5048 -0.0267 0.0004 0.0331 43 ASP A OD1 369 O OD2 . ASP A 47 ? 0.5385 0.5917 0.5411 -0.0305 0.0018 0.0365 43 ASP A OD2 370 N N . VAL A 48 ? 0.3147 0.3688 0.3270 -0.0283 -0.0017 0.0264 44 VAL A N 371 C CA . VAL A 48 ? 0.2933 0.3486 0.3077 -0.0287 -0.0021 0.0246 44 VAL A CA 372 C C . VAL A 48 ? 0.2950 0.3528 0.3115 -0.0259 -0.0024 0.0226 44 VAL A C 373 O O . VAL A 48 ? 0.2722 0.3342 0.2906 -0.0255 -0.0022 0.0214 44 VAL A O 374 C CB . VAL A 48 ? 0.2999 0.3489 0.3133 -0.0297 -0.0023 0.0246 44 VAL A CB 375 C CG1 . VAL A 48 ? 0.3085 0.3583 0.3239 -0.0286 -0.0028 0.0226 44 VAL A CG1 376 C CG2 . VAL A 48 ? 0.3199 0.3672 0.3319 -0.0333 -0.0017 0.0259 44 VAL A CG2 377 N N . LEU A 49 ? 0.2785 0.3338 0.2947 -0.0237 -0.0026 0.0223 45 LEU A N 378 C CA . LEU A 49 ? 0.2670 0.3240 0.2854 -0.0213 -0.0026 0.0202 45 LEU A CA 379 C C . LEU A 49 ? 0.2834 0.3468 0.3032 -0.0207 -0.0021 0.0193 45 LEU A C 380 O O . LEU A 49 ? 0.2697 0.3353 0.2917 -0.0195 -0.0017 0.0175 45 LEU A O 381 C CB . LEU A 49 ? 0.2650 0.3188 0.2829 -0.0195 -0.0028 0.0199 45 LEU A CB 382 C CG . LEU A 49 ? 0.2878 0.3353 0.3046 -0.0196 -0.0032 0.0204 45 LEU A CG 383 C CD1 . LEU A 49 ? 0.2528 0.2978 0.2685 -0.0178 -0.0035 0.0204 45 LEU A CD1 384 C CD2 . LEU A 49 ? 0.2819 0.3284 0.3004 -0.0191 -0.0031 0.0189 45 LEU A CD2 385 N N . ARG A 50 ? 0.2816 0.3477 0.3001 -0.0213 -0.0021 0.0205 46 ARG A N 386 C CA . ARG A 50 ? 0.3066 0.3793 0.3263 -0.0207 -0.0017 0.0197 46 ARG A CA 387 C C . ARG A 50 ? 0.3066 0.3831 0.3272 -0.0221 -0.0013 0.0197 46 ARG A C 388 O O . ARG A 50 ? 0.3057 0.3857 0.3283 -0.0209 -0.0010 0.0180 46 ARG A O 389 C CB . ARG A 50 ? 0.3242 0.3991 0.3418 -0.0210 -0.0017 0.0214 46 ARG A CB 390 C CG A ARG A 50 ? 0.2913 0.3656 0.3080 -0.0192 -0.0020 0.0213 46 ARG A CG 391 C CG B ARG A 50 ? 0.3271 0.4086 0.3457 -0.0197 -0.0014 0.0202 46 ARG A CG 392 C CD A ARG A 50 ? 0.3149 0.3923 0.3292 -0.0194 -0.0017 0.0235 46 ARG A CD 393 C CD B ARG A 50 ? 0.3660 0.4493 0.3820 -0.0194 -0.0015 0.0221 46 ARG A CD 394 N NE A ARG A 50 ? 0.4461 0.5219 0.4588 -0.0174 -0.0021 0.0239 46 ARG A NE 395 N NE B ARG A 50 ? 0.4249 0.5148 0.4420 -0.0178 -0.0014 0.0203 46 ARG A NE 396 C CZ A ARG A 50 ? 0.4182 0.4893 0.4279 -0.0174 -0.0021 0.0265 46 ARG A CZ 397 C CZ B ARG A 50 ? 0.4796 0.5753 0.4970 -0.0183 -0.0010 0.0204 46 ARG A CZ 398 N NH1 A ARG A 50 ? 0.4798 0.5506 0.4883 -0.0150 -0.0025 0.0264 46 ARG A NH1 399 N NH1 B ARG A 50 ? 0.4880 0.5896 0.5065 -0.0166 -0.0009 0.0184 46 ARG A NH1 400 N NH2 A ARG A 50 ? 0.3987 0.4656 0.4065 -0.0197 -0.0015 0.0290 46 ARG A NH2 401 N NH2 B ARG A 50 ? 0.4904 0.5864 0.5071 -0.0205 -0.0005 0.0223 46 ARG A NH2 402 N N . ASP A 51 ? 0.3147 0.3902 0.3338 -0.0245 -0.0013 0.0216 47 ASP A N 403 C CA . ASP A 51 ? 0.3059 0.3862 0.3258 -0.0262 -0.0010 0.0218 47 ASP A CA 404 C C . ASP A 51 ? 0.2948 0.3760 0.3166 -0.0254 -0.0010 0.0201 47 ASP A C 405 O O . ASP A 51 ? 0.2940 0.3808 0.3171 -0.0252 -0.0007 0.0194 47 ASP A O 406 C CB . ASP A 51 ? 0.3225 0.4010 0.3406 -0.0295 -0.0008 0.0238 47 ASP A CB 407 C CG . ASP A 51 ? 0.3511 0.4293 0.3670 -0.0302 -0.0003 0.0260 47 ASP A CG 408 O OD1 . ASP A 51 ? 0.3632 0.4379 0.3773 -0.0327 0.0002 0.0278 47 ASP A OD1 409 O OD2 . ASP A 51 ? 0.3753 0.4564 0.3912 -0.0283 -0.0003 0.0257 47 ASP A OD2 410 N N . ASN A 52 ? 0.2800 0.3561 0.3018 -0.0247 -0.0014 0.0196 48 ASN A N 411 C CA . ASN A 52 ? 0.2795 0.3564 0.3029 -0.0234 -0.0013 0.0183 48 ASN A CA 412 C C . ASN A 52 ? 0.2694 0.3448 0.2942 -0.0203 -0.0008 0.0167 48 ASN A C 413 O O . ASN A 52 ? 0.2528 0.3277 0.2785 -0.0188 -0.0005 0.0159 48 ASN A O 414 C CB . ASN A 52 ? 0.2951 0.3678 0.3177 -0.0246 -0.0018 0.0187 48 ASN A CB 415 C CG . ASN A 52 ? 0.3454 0.4191 0.3669 -0.0281 -0.0019 0.0199 48 ASN A CG 416 O OD1 . ASN A 52 ? 0.2952 0.3741 0.3174 -0.0292 -0.0018 0.0195 48 ASN A OD1 417 N ND2 . ASN A 52 ? 0.2827 0.3517 0.3023 -0.0298 -0.0020 0.0212 48 ASN A ND2 418 N N . PHE A 53 ? 0.2550 0.3298 0.2800 -0.0194 -0.0007 0.0162 49 PHE A N 419 C CA . PHE A 53 ? 0.2396 0.3138 0.2663 -0.0169 0.0001 0.0142 49 PHE A CA 420 C C . PHE A 53 ? 0.2455 0.3143 0.2725 -0.0158 0.0003 0.0139 49 PHE A C 421 O O . PHE A 53 ? 0.2291 0.2975 0.2576 -0.0140 0.0013 0.0127 49 PHE A O 422 C CB . PHE A 53 ? 0.2462 0.3251 0.2744 -0.0156 0.0010 0.0131 49 PHE A CB 423 C CG . PHE A 53 ? 0.2397 0.3245 0.2677 -0.0166 0.0009 0.0134 49 PHE A CG 424 C CD1 . PHE A 53 ? 0.2356 0.3222 0.2638 -0.0162 0.0010 0.0125 49 PHE A CD1 425 C CD2 . PHE A 53 ? 0.2474 0.3365 0.2750 -0.0177 0.0008 0.0144 49 PHE A CD2 426 C CE1 . PHE A 53 ? 0.2958 0.3883 0.3236 -0.0167 0.0010 0.0128 49 PHE A CE1 427 C CE2 . PHE A 53 ? 0.2811 0.3760 0.3085 -0.0186 0.0008 0.0147 49 PHE A CE2 428 C CZ . PHE A 53 ? 0.2539 0.3504 0.2814 -0.0180 0.0009 0.0140 49 PHE A CZ 429 N N . ILE A 54 ? 0.2331 0.2979 0.2586 -0.0170 -0.0006 0.0150 50 ILE A N 430 C CA . ILE A 54 ? 0.2350 0.2949 0.2604 -0.0162 -0.0006 0.0149 50 ILE A CA 431 C C . ILE A 54 ? 0.2420 0.2995 0.2690 -0.0142 0.0003 0.0134 50 ILE A C 432 O O . ILE A 54 ? 0.2695 0.3271 0.2968 -0.0140 0.0003 0.0126 50 ILE A O 433 C CB . ILE A 54 ? 0.2276 0.2834 0.2509 -0.0178 -0.0016 0.0163 50 ILE A CB 434 C CG1 . ILE A 54 ? 0.2148 0.2725 0.2369 -0.0203 -0.0021 0.0176 50 ILE A CG1 435 C CG2 . ILE A 54 ? 0.2298 0.2805 0.2529 -0.0169 -0.0017 0.0161 50 ILE A CG2 436 C CD1 . ILE A 54 ? 0.2244 0.2844 0.2473 -0.0202 -0.0020 0.0172 50 ILE A CD1 437 N N . GLY A 55 ? 0.2263 0.2817 0.2540 -0.0127 0.0011 0.0130 51 GLY A N 438 C CA . GLY A 55 ? 0.2332 0.2862 0.2626 -0.0109 0.0025 0.0114 51 GLY A CA 439 C C . GLY A 55 ? 0.2434 0.2916 0.2724 -0.0108 0.0022 0.0115 51 GLY A C 440 O O . GLY A 55 ? 0.2336 0.2801 0.2640 -0.0099 0.0031 0.0100 51 GLY A O 441 N N . SER A 56 ? 0.2367 0.2828 0.2639 -0.0117 0.0010 0.0129 52 SER A N 442 C CA . SER A 56 ? 0.2338 0.2754 0.2605 -0.0112 0.0008 0.0129 52 SER A CA 443 C C . SER A 56 ? 0.2377 0.2772 0.2621 -0.0126 -0.0007 0.0143 52 SER A C 444 O O . SER A 56 ? 0.2328 0.2739 0.2561 -0.0140 -0.0014 0.0152 52 SER A O 445 C CB . SER A 56 ? 0.2347 0.2741 0.2622 -0.0094 0.0021 0.0127 52 SER A CB 446 O OG . SER A 56 ? 0.2476 0.2830 0.2748 -0.0089 0.0020 0.0127 52 SER A OG 447 N N . LEU A 57 ? 0.2280 0.2639 0.2517 -0.0124 -0.0011 0.0143 53 LEU A N 448 C CA . LEU A 57 ? 0.2316 0.2644 0.2531 -0.0134 -0.0023 0.0154 53 LEU A CA 449 C C . LEU A 57 ? 0.2435 0.2724 0.2649 -0.0121 -0.0021 0.0151 53 LEU A C 450 O O . LEU A 57 ? 0.2385 0.2671 0.2615 -0.0106 -0.0011 0.0141 53 LEU A O 451 C CB . LEU A 57 ? 0.2450 0.2767 0.2650 -0.0139 -0.0030 0.0160 53 LEU A CB 452 C CG . LEU A 57 ? 0.3219 0.3568 0.3411 -0.0155 -0.0033 0.0170 53 LEU A CG 453 C CD1 . LEU A 57 ? 0.3101 0.3493 0.3311 -0.0146 -0.0027 0.0159 53 LEU A CD1 454 C CD2 . LEU A 57 ? 0.3609 0.3930 0.3776 -0.0162 -0.0040 0.0185 53 LEU A CD2 455 N N . LEU A 58 ? 0.2264 0.2525 0.2459 -0.0127 -0.0030 0.0158 54 LEU A N 456 C CA . LEU A 58 ? 0.2307 0.2530 0.2498 -0.0115 -0.0030 0.0155 54 LEU A CA 457 C C . LEU A 58 ? 0.2390 0.2576 0.2556 -0.0124 -0.0041 0.0163 54 LEU A C 458 O O . LEU A 58 ? 0.2480 0.2665 0.2631 -0.0143 -0.0046 0.0171 54 LEU A O 459 C CB . LEU A 58 ? 0.2200 0.2426 0.2395 -0.0106 -0.0025 0.0153 54 LEU A CB 460 C CG . LEU A 58 ? 0.2393 0.2616 0.2571 -0.0119 -0.0034 0.0157 54 LEU A CG 461 C CD1 . LEU A 58 ? 0.2401 0.2614 0.2578 -0.0102 -0.0031 0.0154 54 LEU A CD1 462 C CD2 . LEU A 58 ? 0.2367 0.2633 0.2546 -0.0136 -0.0036 0.0159 54 LEU A CD2 463 N N . SER A 59 ? 0.2203 0.2356 0.2364 -0.0110 -0.0041 0.0160 55 SER A N 464 C CA . SER A 59 ? 0.2425 0.2536 0.2563 -0.0114 -0.0050 0.0165 55 SER A CA 465 C C . SER A 59 ? 0.2558 0.2662 0.2697 -0.0108 -0.0049 0.0159 55 SER A C 466 O O . SER A 59 ? 0.2620 0.2724 0.2771 -0.0088 -0.0042 0.0153 55 SER A O 467 C CB . SER A 59 ? 0.2646 0.2729 0.2776 -0.0098 -0.0052 0.0165 55 SER A CB 468 O OG . SER A 59 ? 0.2722 0.2807 0.2842 -0.0102 -0.0055 0.0173 55 SER A OG 469 N N . GLY A 60 ? 0.2523 0.2624 0.2650 -0.0123 -0.0054 0.0159 56 GLY A N 470 C CA . GLY A 60 ? 0.2637 0.2731 0.2760 -0.0115 -0.0056 0.0152 56 GLY A CA 471 C C . GLY A 60 ? 0.2818 0.2863 0.2925 -0.0105 -0.0060 0.0151 56 GLY A C 472 O O . GLY A 60 ? 0.2716 0.2736 0.2816 -0.0103 -0.0061 0.0156 56 GLY A O 473 N N . GLY A 61 ? 0.2840 0.2874 0.2941 -0.0095 -0.0061 0.0144 57 GLY A N 474 C CA . GLY A 61 ? 0.2701 0.2690 0.2786 -0.0084 -0.0065 0.0141 57 GLY A CA 475 C C . GLY A 61 ? 0.3114 0.3061 0.3177 -0.0100 -0.0071 0.0145 57 GLY A C 476 O O . GLY A 61 ? 0.3054 0.2999 0.3109 -0.0124 -0.0074 0.0143 57 GLY A O 477 N N . GLY A 62 ? 0.2840 0.2757 0.2894 -0.0087 -0.0072 0.0151 58 GLY A N 478 C CA . GLY A 62 ? 0.3010 0.2882 0.3040 -0.0097 -0.0075 0.0158 58 GLY A CA 479 C C . GLY A 62 ? 0.2958 0.2837 0.2985 -0.0115 -0.0073 0.0170 58 GLY A C 480 O O . GLY A 62 ? 0.3017 0.2853 0.3021 -0.0124 -0.0072 0.0179 58 GLY A O 481 N N . SER A 63 ? 0.2803 0.2732 0.2852 -0.0119 -0.0070 0.0171 59 SER A N 482 C CA . SER A 63 ? 0.2772 0.2713 0.2818 -0.0135 -0.0068 0.0183 59 SER A CA 483 C C . SER A 63 ? 0.2723 0.2671 0.2770 -0.0114 -0.0066 0.0191 59 SER A C 484 O O . SER A 63 ? 0.2860 0.2848 0.2929 -0.0103 -0.0064 0.0184 59 SER A O 485 C CB . SER A 63 ? 0.2789 0.2784 0.2857 -0.0149 -0.0065 0.0179 59 SER A CB 486 O OG . SER A 63 ? 0.2883 0.2895 0.2949 -0.0163 -0.0063 0.0190 59 SER A OG 487 N N . VAL A 64 ? 0.2742 0.2651 0.2763 -0.0110 -0.0067 0.0203 60 VAL A N 488 C CA . VAL A 64 ? 0.2723 0.2634 0.2737 -0.0084 -0.0067 0.0210 60 VAL A CA 489 C C . VAL A 64 ? 0.2884 0.2778 0.2873 -0.0089 -0.0064 0.0230 60 VAL A C 490 O O . VAL A 64 ? 0.2948 0.2801 0.2918 -0.0109 -0.0061 0.0239 60 VAL A O 491 C CB . VAL A 64 ? 0.2638 0.2512 0.2639 -0.0061 -0.0070 0.0206 60 VAL A CB 492 C CG1 . VAL A 64 ? 0.2434 0.2324 0.2458 -0.0056 -0.0071 0.0188 60 VAL A CG1 493 C CG2 . VAL A 64 ? 0.2570 0.2371 0.2535 -0.0065 -0.0070 0.0215 60 VAL A CG2 494 N N . PRO A 65 ? 0.2977 0.2902 0.2966 -0.0069 -0.0065 0.0237 61 PRO A N 495 C CA . PRO A 65 ? 0.2946 0.2860 0.2909 -0.0071 -0.0060 0.0259 61 PRO A CA 496 C C . PRO A 65 ? 0.3218 0.3057 0.3142 -0.0061 -0.0056 0.0276 61 PRO A C 497 O O . PRO A 65 ? 0.3100 0.2904 0.2998 -0.0073 -0.0048 0.0296 61 PRO A O 498 C CB . PRO A 65 ? 0.3057 0.3028 0.3030 -0.0046 -0.0063 0.0257 61 PRO A CB 499 C CG . PRO A 65 ? 0.3011 0.3007 0.3008 -0.0029 -0.0068 0.0235 61 PRO A CG 500 C CD . PRO A 65 ? 0.2850 0.2828 0.2864 -0.0049 -0.0067 0.0222 61 PRO A CD 501 N N . ARG A 66 ? 0.3261 0.3075 0.3178 -0.0038 -0.0060 0.0269 62 ARG A N 502 C CA . ARG A 66 ? 0.3557 0.3293 0.3440 -0.0032 -0.0056 0.0279 62 ARG A CA 503 C C . ARG A 66 ? 0.3718 0.3444 0.3606 -0.0011 -0.0063 0.0263 62 ARG A C 504 O O . ARG A 66 ? 0.3141 0.2921 0.3055 0.0004 -0.0069 0.0248 62 ARG A O 505 C CB . ARG A 66 ? 0.3923 0.3630 0.3770 -0.0010 -0.0050 0.0305 62 ARG A CB 506 C CG . ARG A 66 ? 0.4294 0.4047 0.4140 0.0028 -0.0055 0.0307 62 ARG A CG 507 C CD . ARG A 66 ? 0.5126 0.4841 0.4927 0.0056 -0.0047 0.0338 62 ARG A CD 508 N NE . ARG A 66 ? 0.5178 0.4944 0.4979 0.0098 -0.0054 0.0335 62 ARG A NE 509 C CZ . ARG A 66 ? 0.5554 0.5291 0.5319 0.0137 -0.0052 0.0352 62 ARG A CZ 510 N NH1 . ARG A 66 ? 0.5729 0.5376 0.5451 0.0140 -0.0039 0.0376 62 ARG A NH1 511 N NH2 . ARG A 66 ? 0.4967 0.4767 0.4740 0.0172 -0.0060 0.0343 62 ARG A NH2 512 N N . LYS A 67 ? 0.3838 0.3493 0.3700 -0.0008 -0.0060 0.0265 63 LYS A N 513 C CA . LYS A 67 ? 0.3944 0.3591 0.3809 0.0015 -0.0066 0.0251 63 LYS A CA 514 C C . LYS A 67 ? 0.3509 0.3184 0.3366 0.0055 -0.0069 0.0258 63 LYS A C 515 O O . LYS A 67 ? 0.3437 0.3100 0.3268 0.0070 -0.0064 0.0278 63 LYS A O 516 C CB . LYS A 67 ? 0.4287 0.3851 0.4122 0.0012 -0.0062 0.0250 63 LYS A CB 517 C CG . LYS A 67 ? 0.5028 0.4579 0.4877 -0.0029 -0.0061 0.0234 63 LYS A CG 518 C CD . LYS A 67 ? 0.5186 0.4801 0.5073 -0.0035 -0.0069 0.0213 63 LYS A CD 519 C CE . LYS A 67 ? 0.5769 0.5373 0.5656 -0.0014 -0.0074 0.0198 63 LYS A CE 520 N NZ . LYS A 67 ? 0.6380 0.5935 0.6255 -0.0030 -0.0073 0.0186 63 LYS A NZ 521 N N . GLY A 68 ? 0.3453 0.3171 0.3334 0.0072 -0.0075 0.0240 64 GLY A N 522 C CA . GLY A 68 ? 0.3261 0.3013 0.3137 0.0111 -0.0078 0.0242 64 GLY A CA 523 C C . GLY A 68 ? 0.3147 0.2970 0.3039 0.0114 -0.0079 0.0244 64 GLY A C 524 O O . GLY A 68 ? 0.3219 0.3077 0.3105 0.0145 -0.0082 0.0247 64 GLY A O 525 N N . ALA A 69 ? 0.2997 0.2847 0.2912 0.0083 -0.0078 0.0241 65 ALA A N 526 C CA . ALA A 69 ? 0.2945 0.2865 0.2875 0.0085 -0.0078 0.0242 65 ALA A CA 527 C C . ALA A 69 ? 0.2870 0.2861 0.2830 0.0104 -0.0082 0.0219 65 ALA A C 528 O O . ALA A 69 ? 0.2865 0.2863 0.2851 0.0099 -0.0082 0.0199 65 ALA A O 529 C CB . ALA A 69 ? 0.2801 0.2742 0.2756 0.0049 -0.0075 0.0236 65 ALA A CB 530 N N . THR A 70 ? 0.2924 0.2968 0.2881 0.0126 -0.0084 0.0221 66 THR A N 531 C CA . THR A 70 ? 0.2877 0.2998 0.2867 0.0140 -0.0087 0.0195 66 THR A CA 532 C C . THR A 70 ? 0.2874 0.3046 0.2908 0.0112 -0.0084 0.0173 66 THR A C 533 O O . THR A 70 ? 0.2738 0.2895 0.2774 0.0086 -0.0081 0.0181 66 THR A O 534 C CB . THR A 70 ? 0.2947 0.3119 0.2920 0.0172 -0.0091 0.0202 66 THR A CB 535 O OG1 . THR A 70 ? 0.2930 0.3123 0.2899 0.0159 -0.0089 0.0213 66 THR A OG1 536 C CG2 . THR A 70 ? 0.3102 0.3217 0.3022 0.0208 -0.0092 0.0230 66 THR A CG2 537 N N . ALA A 71 ? 0.2652 0.2884 0.2723 0.0115 -0.0082 0.0145 67 ALA A N 538 C CA . ALA A 71 ? 0.2609 0.2886 0.2721 0.0089 -0.0076 0.0123 67 ALA A CA 539 C C . ALA A 71 ? 0.2590 0.2906 0.2698 0.0085 -0.0077 0.0130 67 ALA A C 540 O O . ALA A 71 ? 0.2580 0.2902 0.2704 0.0060 -0.0073 0.0126 67 ALA A O 541 C CB . ALA A 71 ? 0.2647 0.2987 0.2799 0.0095 -0.0072 0.0090 67 ALA A CB 542 N N . LYS A 72 ? 0.2656 0.3001 0.2739 0.0111 -0.0084 0.0139 68 LYS A N 543 C CA . LYS A 72 ? 0.2938 0.3324 0.3013 0.0111 -0.0085 0.0147 68 LYS A CA 544 C C . LYS A 72 ? 0.2849 0.3176 0.2899 0.0092 -0.0082 0.0176 68 LYS A C 545 O O . LYS A 72 ? 0.2919 0.3274 0.2978 0.0076 -0.0080 0.0176 68 LYS A O 546 C CB . LYS A 72 ? 0.3068 0.3497 0.3115 0.0149 -0.0092 0.0156 68 LYS A CB 547 C CG . LYS A 72 ? 0.3696 0.4169 0.3731 0.0152 -0.0092 0.0167 68 LYS A CG 548 C CD . LYS A 72 ? 0.4878 0.5374 0.4871 0.0195 -0.0097 0.0190 68 LYS A CD 549 C CE . LYS A 72 ? 0.5189 0.5749 0.5172 0.0202 -0.0098 0.0196 68 LYS A CE 550 N NZ . LYS A 72 ? 0.5194 0.5727 0.5173 0.0173 -0.0092 0.0213 68 LYS A NZ 551 N N . GLU A 73 ? 0.2728 0.2976 0.2744 0.0095 -0.0082 0.0201 69 GLU A N 552 C CA . GLU A 73 ? 0.2721 0.2915 0.2718 0.0072 -0.0078 0.0224 69 GLU A CA 553 C C . GLU A 73 ? 0.2646 0.2846 0.2677 0.0038 -0.0075 0.0208 69 GLU A C 554 O O . GLU A 73 ? 0.2484 0.2688 0.2516 0.0017 -0.0071 0.0217 69 GLU A O 555 C CB . GLU A 73 ? 0.2670 0.2773 0.2631 0.0074 -0.0076 0.0246 69 GLU A CB 556 C CG . GLU A 73 ? 0.2864 0.2948 0.2781 0.0111 -0.0077 0.0271 69 GLU A CG 557 C CD . GLU A 73 ? 0.3308 0.3297 0.3193 0.0112 -0.0073 0.0288 69 GLU A CD 558 O OE1 . GLU A 73 ? 0.3265 0.3238 0.3137 0.0139 -0.0076 0.0286 69 GLU A OE1 559 O OE2 . GLU A 73 ? 0.3638 0.3572 0.3512 0.0083 -0.0066 0.0301 69 GLU A OE2 560 N N . TRP A 74 ? 0.2477 0.2674 0.2536 0.0032 -0.0074 0.0187 70 TRP A N 561 C CA . TRP A 74 ? 0.2474 0.2678 0.2563 0.0005 -0.0068 0.0174 70 TRP A CA 562 C C . TRP A 74 ? 0.2377 0.2650 0.2493 -0.0001 -0.0065 0.0158 70 TRP A C 563 O O . TRP A 74 ? 0.2408 0.2688 0.2533 -0.0021 -0.0062 0.0160 70 TRP A O 564 C CB . TRP A 74 ? 0.2416 0.2607 0.2529 0.0006 -0.0065 0.0155 70 TRP A CB 565 C CG . TRP A 74 ? 0.2309 0.2435 0.2402 0.0004 -0.0067 0.0166 70 TRP A CG 566 C CD1 . TRP A 74 ? 0.2276 0.2366 0.2347 0.0023 -0.0071 0.0172 70 TRP A CD1 567 C CD2 . TRP A 74 ? 0.2338 0.2433 0.2434 -0.0017 -0.0064 0.0169 70 TRP A CD2 568 N NE1 . TRP A 74 ? 0.2333 0.2367 0.2392 0.0013 -0.0071 0.0178 70 TRP A NE1 569 C CE2 . TRP A 74 ? 0.2376 0.2417 0.2452 -0.0012 -0.0067 0.0175 70 TRP A CE2 570 C CE3 . TRP A 74 ? 0.2610 0.2722 0.2725 -0.0038 -0.0059 0.0165 70 TRP A CE3 571 C CZ2 . TRP A 74 ? 0.2393 0.2402 0.2467 -0.0028 -0.0066 0.0176 70 TRP A CZ2 572 C CZ3 . TRP A 74 ? 0.2576 0.2658 0.2689 -0.0052 -0.0058 0.0168 70 TRP A CZ3 573 C CH2 . TRP A 74 ? 0.2481 0.2513 0.2573 -0.0048 -0.0062 0.0172 70 TRP A CH2 574 N N . GLN A 75 ? 0.2373 0.2702 0.2504 0.0016 -0.0067 0.0139 71 GLN A N 575 C CA . GLN A 75 ? 0.2509 0.2906 0.2668 0.0009 -0.0063 0.0119 71 GLN A CA 576 C C . GLN A 75 ? 0.2640 0.3050 0.2777 0.0005 -0.0066 0.0139 71 GLN A C 577 O O . GLN A 75 ? 0.2633 0.3072 0.2788 -0.0011 -0.0061 0.0131 71 GLN A O 578 C CB . GLN A 75 ? 0.2481 0.2944 0.2656 0.0028 -0.0065 0.0094 71 GLN A CB 579 C CG . GLN A 75 ? 0.2697 0.3161 0.2904 0.0028 -0.0059 0.0068 71 GLN A CG 580 C CD . GLN A 75 ? 0.2669 0.3215 0.2909 0.0035 -0.0056 0.0032 71 GLN A CD 581 O OE1 . GLN A 75 ? 0.3296 0.3851 0.3564 0.0032 -0.0049 0.0007 71 GLN A OE1 582 N NE2 . GLN A 75 ? 0.2204 0.2810 0.2441 0.0041 -0.0061 0.0026 71 GLN A NE2 583 N N . ASP A 76 ? 0.2652 0.3041 0.2748 0.0022 -0.0071 0.0166 72 ASP A N 584 C CA . ASP A 76 ? 0.2808 0.3210 0.2881 0.0021 -0.0071 0.0189 72 ASP A CA 585 C C . ASP A 76 ? 0.2734 0.3091 0.2804 -0.0010 -0.0066 0.0203 72 ASP A C 586 O O . ASP A 76 ? 0.2680 0.3064 0.2752 -0.0022 -0.0064 0.0208 72 ASP A O 587 C CB . ASP A 76 ? 0.2795 0.3165 0.2820 0.0046 -0.0074 0.0220 72 ASP A CB 588 C CG . ASP A 76 ? 0.3277 0.3709 0.3300 0.0081 -0.0079 0.0209 72 ASP A CG 589 O OD1 . ASP A 76 ? 0.3167 0.3673 0.3224 0.0082 -0.0081 0.0178 72 ASP A OD1 590 O OD2 . ASP A 76 ? 0.3425 0.3833 0.3411 0.0108 -0.0081 0.0232 72 ASP A OD2 591 N N . MET A 77 ? 0.2700 0.2993 0.2765 -0.0020 -0.0065 0.0209 73 MET A N 592 C CA . MET A 77 ? 0.2738 0.2999 0.2804 -0.0049 -0.0061 0.0218 73 MET A CA 593 C C . MET A 77 ? 0.2586 0.2892 0.2690 -0.0064 -0.0058 0.0195 73 MET A C 594 O O . MET A 77 ? 0.2585 0.2911 0.2691 -0.0081 -0.0055 0.0201 73 MET A O 595 C CB . MET A 77 ? 0.2857 0.3051 0.2915 -0.0056 -0.0062 0.0222 73 MET A CB 596 C CG . MET A 77 ? 0.2756 0.2930 0.2819 -0.0085 -0.0058 0.0225 73 MET A CG 597 S SD . MET A 77 ? 0.3078 0.3191 0.3139 -0.0092 -0.0060 0.0220 73 MET A SD 598 C CE . MET A 77 ? 0.2829 0.2978 0.2929 -0.0080 -0.0058 0.0192 73 MET A CE 599 N N . VAL A 78 ? 0.2388 0.2711 0.2521 -0.0058 -0.0056 0.0170 74 VAL A N 600 C CA . VAL A 78 ? 0.2379 0.2733 0.2546 -0.0070 -0.0049 0.0150 74 VAL A CA 601 C C . VAL A 78 ? 0.2421 0.2840 0.2599 -0.0069 -0.0048 0.0140 74 VAL A C 602 O O . VAL A 78 ? 0.2345 0.2782 0.2534 -0.0084 -0.0043 0.0138 74 VAL A O 603 C CB . VAL A 78 ? 0.2450 0.2803 0.2647 -0.0064 -0.0043 0.0125 74 VAL A CB 604 C CG1 . VAL A 78 ? 0.2444 0.2822 0.2673 -0.0075 -0.0032 0.0106 74 VAL A CG1 605 C CG2 . VAL A 78 ? 0.2098 0.2391 0.2284 -0.0063 -0.0044 0.0134 74 VAL A CG2 606 N N . ASP A 79 ? 0.2214 0.2669 0.2387 -0.0052 -0.0052 0.0134 75 ASP A N 607 C CA . ASP A 79 ? 0.2501 0.3023 0.2682 -0.0049 -0.0052 0.0124 75 ASP A CA 608 C C . ASP A 79 ? 0.2710 0.3232 0.2866 -0.0058 -0.0053 0.0151 75 ASP A C 609 O O . ASP A 79 ? 0.2787 0.3355 0.2956 -0.0065 -0.0050 0.0142 75 ASP A O 610 C CB . ASP A 79 ? 0.2654 0.3219 0.2827 -0.0025 -0.0058 0.0117 75 ASP A CB 611 C CG . ASP A 79 ? 0.2772 0.3368 0.2982 -0.0019 -0.0054 0.0079 75 ASP A CG 612 O OD1 . ASP A 79 ? 0.2807 0.3396 0.3049 -0.0035 -0.0045 0.0058 75 ASP A OD1 613 O OD2 . ASP A 79 ? 0.2938 0.3567 0.3142 0.0001 -0.0060 0.0072 75 ASP A OD2 614 N N . GLY A 80 ? 0.2830 0.3301 0.2951 -0.0058 -0.0055 0.0183 76 GLY A N 615 C CA . GLY A 80 ? 0.2860 0.3325 0.2957 -0.0071 -0.0053 0.0210 76 GLY A CA 616 C C . GLY A 80 ? 0.2905 0.3371 0.3021 -0.0097 -0.0049 0.0205 76 GLY A C 617 O O . GLY A 80 ? 0.2737 0.3239 0.2852 -0.0106 -0.0046 0.0210 76 GLY A O 618 N N . PHE A 81 ? 0.2861 0.3292 0.2992 -0.0106 -0.0047 0.0195 77 PHE A N 619 C CA . PHE A 81 ? 0.2733 0.3171 0.2883 -0.0125 -0.0043 0.0188 77 PHE A CA 620 C C . PHE A 81 ? 0.2858 0.3356 0.3039 -0.0120 -0.0038 0.0163 77 PHE A C 621 O O . PHE A 81 ? 0.2839 0.3369 0.3028 -0.0131 -0.0034 0.0162 77 PHE A O 622 C CB . PHE A 81 ? 0.2597 0.2991 0.2757 -0.0128 -0.0042 0.0182 77 PHE A CB 623 C CG . PHE A 81 ? 0.2808 0.3142 0.2940 -0.0137 -0.0046 0.0203 77 PHE A CG 624 C CD1 . PHE A 81 ? 0.2839 0.3161 0.2947 -0.0153 -0.0045 0.0225 77 PHE A CD1 625 C CD2 . PHE A 81 ? 0.2488 0.2778 0.2617 -0.0129 -0.0048 0.0199 77 PHE A CD2 626 C CE1 . PHE A 81 ? 0.2855 0.3119 0.2940 -0.0164 -0.0046 0.0239 77 PHE A CE1 627 C CE2 . PHE A 81 ? 0.2812 0.3045 0.2916 -0.0137 -0.0050 0.0214 77 PHE A CE2 628 C CZ . PHE A 81 ? 0.2718 0.2939 0.2802 -0.0156 -0.0049 0.0233 77 PHE A CZ 629 N N . GLN A 82 ? 0.2613 0.3126 0.2812 -0.0105 -0.0037 0.0140 78 GLN A N 630 C CA . GLN A 82 ? 0.2738 0.3301 0.2969 -0.0103 -0.0030 0.0111 78 GLN A CA 631 C C . GLN A 82 ? 0.2699 0.3321 0.2925 -0.0101 -0.0032 0.0111 78 GLN A C 632 O O . GLN A 82 ? 0.2464 0.3122 0.2708 -0.0107 -0.0026 0.0097 78 GLN A O 633 C CB . GLN A 82 ? 0.2595 0.3167 0.2848 -0.0091 -0.0027 0.0084 78 GLN A CB 634 C CG . GLN A 82 ? 0.2652 0.3262 0.2942 -0.0092 -0.0015 0.0050 78 GLN A CG 635 C CD . GLN A 82 ? 0.3030 0.3606 0.3336 -0.0100 -0.0003 0.0047 78 GLN A CD 636 O OE1 . GLN A 82 ? 0.2623 0.3200 0.2922 -0.0108 -0.0003 0.0061 78 GLN A OE1 637 N NE2 . GLN A 82 ? 0.2718 0.3265 0.3043 -0.0097 0.0007 0.0032 78 GLN A NE2 638 N N . LYS A 83 ? 0.2736 0.3368 0.2935 -0.0092 -0.0039 0.0128 79 LYS A N 639 C CA . LYS A 83 ? 0.3259 0.3950 0.3448 -0.0087 -0.0041 0.0132 79 LYS A CA 640 C C . LYS A 83 ? 0.3204 0.3901 0.3388 -0.0105 -0.0037 0.0148 79 LYS A C 641 O O . LYS A 83 ? 0.3151 0.3903 0.3346 -0.0106 -0.0034 0.0136 79 LYS A O 642 C CB . LYS A 83 ? 0.3488 0.4178 0.3641 -0.0070 -0.0048 0.0156 79 LYS A CB 643 C CG . LYS A 83 ? 0.4828 0.5584 0.4967 -0.0060 -0.0049 0.0163 79 LYS A CG 644 C CD . LYS A 83 ? 0.6142 0.6904 0.6246 -0.0035 -0.0054 0.0183 79 LYS A CD 645 C CE . LYS A 83 ? 0.6733 0.7580 0.6829 -0.0017 -0.0055 0.0181 79 LYS A CE 646 N NZ . LYS A 83 ? 0.7377 0.8225 0.7430 0.0012 -0.0058 0.0211 79 LYS A NZ 647 N N . ALA A 84 ? 0.2900 0.3543 0.3069 -0.0120 -0.0037 0.0171 80 ALA A N 648 C CA . ALA A 84 ? 0.2937 0.3590 0.3103 -0.0139 -0.0033 0.0184 80 ALA A CA 649 C C . ALA A 84 ? 0.2945 0.3623 0.3145 -0.0143 -0.0027 0.0159 80 ALA A C 650 O O . ALA A 84 ? 0.2912 0.3636 0.3118 -0.0147 -0.0024 0.0155 80 ALA A O 651 C CB . ALA A 84 ? 0.2890 0.3481 0.3036 -0.0156 -0.0033 0.0209 80 ALA A CB 652 N N . CYS A 85 ? 0.2785 0.3433 0.3004 -0.0138 -0.0025 0.0141 81 CYS A N 653 C CA . CYS A 85 ? 0.2719 0.3383 0.2966 -0.0138 -0.0016 0.0120 81 CYS A CA 654 C C . CYS A 85 ? 0.2890 0.3610 0.3157 -0.0128 -0.0011 0.0093 81 CYS A C 655 O O . CYS A 85 ? 0.2808 0.3558 0.3090 -0.0129 -0.0004 0.0082 81 CYS A O 656 C CB . CYS A 85 ? 0.2685 0.3303 0.2947 -0.0133 -0.0011 0.0109 81 CYS A CB 657 S SG . CYS A 85 ? 0.2832 0.3393 0.3073 -0.0144 -0.0017 0.0134 81 CYS A SG 658 N N . MET A 86 ? 0.2653 0.3388 0.2920 -0.0118 -0.0014 0.0081 82 MET A N 659 C CA . MET A 86 ? 0.2840 0.3633 0.3129 -0.0110 -0.0009 0.0050 82 MET A CA 660 C C . MET A 86 ? 0.2838 0.3689 0.3115 -0.0111 -0.0012 0.0058 82 MET A C 661 O O . MET A 86 ? 0.2952 0.3857 0.3247 -0.0106 -0.0008 0.0031 82 MET A O 662 C CB . MET A 86 ? 0.2727 0.3534 0.3023 -0.0099 -0.0012 0.0029 82 MET A CB 663 C CG . MET A 86 ? 0.3016 0.3777 0.3331 -0.0098 -0.0006 0.0015 82 MET A CG 664 S SD . MET A 86 ? 0.3515 0.4266 0.3868 -0.0103 0.0014 -0.0016 82 MET A SD 665 C CE . MET A 86 ? 0.3400 0.4225 0.3781 -0.0100 0.0021 -0.0062 82 MET A CE 666 N N . SER A 87 ? 0.2802 0.3643 0.3050 -0.0118 -0.0019 0.0092 83 SER A N 667 C CA . SER A 87 ? 0.3048 0.3942 0.3280 -0.0119 -0.0020 0.0105 83 SER A CA 668 C C . SER A 87 ? 0.3008 0.3915 0.3249 -0.0132 -0.0014 0.0108 83 SER A C 669 O O . SER A 87 ? 0.2922 0.3877 0.3153 -0.0134 -0.0014 0.0117 83 SER A O 670 C CB . SER A 87 ? 0.3034 0.3910 0.3228 -0.0121 -0.0026 0.0144 83 SER A CB 671 O OG . SER A 87 ? 0.3242 0.4068 0.3426 -0.0140 -0.0024 0.0168 83 SER A OG 672 N N . THR A 88 ? 0.2824 0.3695 0.3081 -0.0137 -0.0009 0.0101 84 THR A N 673 C CA . THR A 88 ? 0.2785 0.3679 0.3052 -0.0143 -0.0003 0.0100 84 THR A CA 674 C C . THR A 88 ? 0.2845 0.3795 0.3133 -0.0132 0.0004 0.0070 84 THR A C 675 O O . THR A 88 ? 0.2817 0.3781 0.3117 -0.0122 0.0006 0.0044 84 THR A O 676 C CB . THR A 88 ? 0.2622 0.3471 0.2900 -0.0145 0.0002 0.0099 84 THR A CB 677 O OG1 . THR A 88 ? 0.2422 0.3250 0.2722 -0.0132 0.0010 0.0072 84 THR A OG1 678 C CG2 . THR A 88 ? 0.2549 0.3344 0.2807 -0.0158 -0.0005 0.0126 84 THR A CG2 679 N N . ARG A 89 ? 0.2828 0.3810 0.3120 -0.0135 0.0009 0.0071 85 ARG A N 680 C CA . ARG A 89 ? 0.2855 0.3888 0.3166 -0.0124 0.0018 0.0043 85 ARG A CA 681 C C . ARG A 89 ? 0.2760 0.3769 0.3098 -0.0112 0.0028 0.0008 85 ARG A C 682 O O . ARG A 89 ? 0.2782 0.3825 0.3133 -0.0105 0.0032 -0.0021 85 ARG A O 683 C CB . ARG A 89 ? 0.2861 0.3917 0.3174 -0.0126 0.0023 0.0050 85 ARG A CB 684 C CG . ARG A 89 ? 0.3197 0.4305 0.3526 -0.0113 0.0032 0.0022 85 ARG A CG 685 C CD . ARG A 89 ? 0.3433 0.4564 0.3763 -0.0112 0.0037 0.0032 85 ARG A CD 686 N NE . ARG A 89 ? 0.3322 0.4410 0.3665 -0.0103 0.0047 0.0027 85 ARG A NE 687 C CZ . ARG A 89 ? 0.3132 0.4222 0.3492 -0.0084 0.0061 0.0003 85 ARG A CZ 688 N NH1 . ARG A 89 ? 0.2970 0.4105 0.3340 -0.0076 0.0068 -0.0022 85 ARG A NH1 689 N NH2 . ARG A 89 ? 0.2814 0.3864 0.3180 -0.0073 0.0071 0.0005 85 ARG A NH2 690 N N . LEU A 90 ? 0.2566 0.3518 0.2911 -0.0111 0.0035 0.0010 86 LEU A N 691 C CA . LEU A 90 ? 0.2536 0.3459 0.2908 -0.0102 0.0049 -0.0022 86 LEU A CA 692 C C . LEU A 90 ? 0.2582 0.3471 0.2957 -0.0104 0.0046 -0.0030 86 LEU A C 693 O O . LEU A 90 ? 0.2695 0.3571 0.3095 -0.0100 0.0058 -0.0061 86 LEU A O 694 C CB . LEU A 90 ? 0.2518 0.3397 0.2898 -0.0094 0.0063 -0.0019 86 LEU A CB 695 C CG . LEU A 90 ? 0.2755 0.3673 0.3134 -0.0087 0.0068 -0.0015 86 LEU A CG 696 C CD1 . LEU A 90 ? 0.2623 0.3500 0.3003 -0.0075 0.0079 -0.0004 86 LEU A CD1 697 C CD2 . LEU A 90 ? 0.3091 0.4047 0.3488 -0.0078 0.0080 -0.0049 86 LEU A CD2 698 N N . GLY A 91 ? 0.2451 0.3325 0.2804 -0.0111 0.0031 -0.0002 87 GLY A N 699 C CA . GLY A 91 ? 0.2567 0.3416 0.2918 -0.0111 0.0025 -0.0006 87 GLY A CA 700 C C . GLY A 91 ? 0.2663 0.3453 0.3031 -0.0108 0.0037 -0.0016 87 GLY A C 701 O O . GLY A 91 ? 0.2643 0.3426 0.3031 -0.0106 0.0044 -0.0043 87 GLY A O 702 N N . ILE A 92 ? 0.2465 0.3218 0.2827 -0.0109 0.0040 0.0004 88 ILE A N 703 C CA . ILE A 92 ? 0.2578 0.3275 0.2951 -0.0104 0.0051 0.0000 88 ILE A CA 704 C C . ILE A 92 ? 0.2613 0.3274 0.2969 -0.0108 0.0039 0.0018 88 ILE A C 705 O O . ILE A 92 ? 0.2733 0.3385 0.3066 -0.0114 0.0026 0.0046 88 ILE A O 706 C CB . ILE A 92 ? 0.2667 0.3343 0.3038 -0.0098 0.0060 0.0014 88 ILE A CB 707 C CG1 . ILE A 92 ? 0.2864 0.3576 0.3248 -0.0091 0.0072 -0.0001 88 ILE A CG1 708 C CG2 . ILE A 92 ? 0.2571 0.3185 0.2951 -0.0090 0.0073 0.0013 88 ILE A CG2 709 C CD1 . ILE A 92 ? 0.2514 0.3222 0.2891 -0.0081 0.0078 0.0016 88 ILE A CD1 710 N N . PRO A 93 ? 0.2543 0.3183 0.2914 -0.0105 0.0044 0.0000 89 PRO A N 711 C CA . PRO A 93 ? 0.2420 0.3028 0.2774 -0.0107 0.0032 0.0017 89 PRO A CA 712 C C . PRO A 93 ? 0.2539 0.3097 0.2883 -0.0106 0.0032 0.0039 89 PRO A C 713 O O . PRO A 93 ? 0.2292 0.2830 0.2647 -0.0100 0.0047 0.0034 89 PRO A O 714 C CB . PRO A 93 ? 0.2389 0.2991 0.2767 -0.0103 0.0041 -0.0012 89 PRO A CB 715 C CG . PRO A 93 ? 0.2300 0.2899 0.2707 -0.0102 0.0064 -0.0037 89 PRO A CG 716 C CD . PRO A 93 ? 0.2455 0.3099 0.2857 -0.0103 0.0061 -0.0036 89 PRO A CD 717 N N . MET A 94 ? 0.2450 0.2986 0.2768 -0.0110 0.0018 0.0062 90 MET A N 718 C CA . MET A 94 ? 0.2522 0.3014 0.2831 -0.0110 0.0018 0.0078 90 MET A CA 719 C C . MET A 94 ? 0.2512 0.2968 0.2833 -0.0101 0.0025 0.0067 90 MET A C 720 O O . MET A 94 ? 0.2355 0.2820 0.2686 -0.0099 0.0026 0.0051 90 MET A O 721 C CB . MET A 94 ? 0.2471 0.2950 0.2750 -0.0120 0.0001 0.0105 90 MET A CB 722 C CG . MET A 94 ? 0.2671 0.3140 0.2934 -0.0119 -0.0010 0.0110 90 MET A CG 723 S SD . MET A 94 ? 0.2628 0.3041 0.2889 -0.0111 -0.0010 0.0109 90 MET A SD 724 C CE . MET A 94 ? 0.2595 0.3024 0.2855 -0.0101 -0.0015 0.0099 90 MET A CE 725 N N . ILE A 95 ? 0.2449 0.2869 0.2768 -0.0096 0.0031 0.0075 91 ILE A N 726 C CA . ILE A 95 ? 0.2283 0.2666 0.2609 -0.0089 0.0038 0.0070 91 ILE A CA 727 C C . ILE A 95 ? 0.2340 0.2694 0.2638 -0.0091 0.0022 0.0092 91 ILE A C 728 O O . ILE A 95 ? 0.2407 0.2760 0.2691 -0.0095 0.0017 0.0107 91 ILE A O 729 C CB . ILE A 95 ? 0.2240 0.2602 0.2583 -0.0078 0.0060 0.0063 91 ILE A CB 730 C CG1 . ILE A 95 ? 0.2184 0.2509 0.2535 -0.0071 0.0070 0.0059 91 ILE A CG1 731 C CG2 . ILE A 95 ? 0.2258 0.2616 0.2587 -0.0072 0.0061 0.0083 91 ILE A CG2 732 C CD1 . ILE A 95 ? 0.2010 0.2312 0.2381 -0.0060 0.0099 0.0051 91 ILE A CD1 733 N N . TYR A 96 ? 0.2233 0.2568 0.2527 -0.0088 0.0016 0.0090 92 TYR A N 734 C CA . TYR A 96 ? 0.2509 0.2812 0.2776 -0.0090 0.0002 0.0108 92 TYR A CA 735 C C . TYR A 96 ? 0.2577 0.2845 0.2848 -0.0079 0.0010 0.0107 92 TYR A C 736 O O . TYR A 96 ? 0.2546 0.2810 0.2834 -0.0072 0.0019 0.0093 92 TYR A O 737 C CB . TYR A 96 ? 0.2312 0.2617 0.2564 -0.0090 -0.0010 0.0111 92 TYR A CB 738 C CG . TYR A 96 ? 0.2551 0.2822 0.2772 -0.0094 -0.0024 0.0131 92 TYR A CG 739 C CD1 . TYR A 96 ? 0.2124 0.2355 0.2337 -0.0088 -0.0025 0.0134 92 TYR A CD1 740 C CD2 . TYR A 96 ? 0.2576 0.2854 0.2776 -0.0105 -0.0033 0.0146 92 TYR A CD2 741 C CE1 . TYR A 96 ? 0.2229 0.2425 0.2413 -0.0093 -0.0036 0.0149 92 TYR A CE1 742 C CE2 . TYR A 96 ? 0.2421 0.2661 0.2593 -0.0111 -0.0041 0.0163 92 TYR A CE2 743 C CZ . TYR A 96 ? 0.2540 0.2738 0.2704 -0.0105 -0.0043 0.0163 92 TYR A CZ 744 O OH . TYR A 96 ? 0.2818 0.2976 0.2955 -0.0112 -0.0050 0.0176 92 TYR A OH 745 N N . GLY A 97 ? 0.2492 0.2741 0.2749 -0.0079 0.0007 0.0120 93 GLY A N 746 C CA . GLY A 97 ? 0.2441 0.2661 0.2698 -0.0066 0.0014 0.0120 93 GLY A CA 747 C C . GLY A 97 ? 0.2389 0.2578 0.2623 -0.0067 0.0000 0.0129 93 GLY A C 748 O O . GLY A 97 ? 0.2177 0.2362 0.2391 -0.0078 -0.0014 0.0138 93 GLY A O 749 N N . ILE A 98 ? 0.2336 0.2502 0.2572 -0.0054 0.0006 0.0127 94 ILE A N 750 C CA . ILE A 98 ? 0.2323 0.2459 0.2538 -0.0052 -0.0006 0.0132 94 ILE A CA 751 C C . ILE A 98 ? 0.2307 0.2424 0.2525 -0.0036 0.0004 0.0131 94 ILE A C 752 O O . ILE A 98 ? 0.2247 0.2370 0.2486 -0.0027 0.0022 0.0125 94 ILE A O 753 C CB . ILE A 98 ? 0.2253 0.2381 0.2461 -0.0051 -0.0015 0.0129 94 ILE A CB 754 C CG1 . ILE A 98 ? 0.2214 0.2307 0.2393 -0.0051 -0.0029 0.0138 94 ILE A CG1 755 C CG2 . ILE A 98 ? 0.2106 0.2242 0.2338 -0.0039 -0.0002 0.0114 94 ILE A CG2 756 C CD1 . ILE A 98 ? 0.2236 0.2320 0.2400 -0.0049 -0.0038 0.0141 94 ILE A CD1 757 N N . ASP A 99 ? 0.2242 0.2337 0.2439 -0.0032 -0.0005 0.0136 95 ASP A N 758 C CA . ASP A 99 ? 0.2338 0.2419 0.2537 -0.0015 0.0004 0.0136 95 ASP A CA 759 C C . ASP A 99 ? 0.2442 0.2507 0.2645 -0.0007 0.0005 0.0129 95 ASP A C 760 O O . ASP A 99 ? 0.2548 0.2593 0.2733 -0.0005 -0.0007 0.0130 95 ASP A O 761 C CB . ASP A 99 ? 0.2096 0.2166 0.2272 -0.0013 -0.0007 0.0141 95 ASP A CB 762 C CG . ASP A 99 ? 0.2623 0.2718 0.2796 -0.0019 -0.0007 0.0145 95 ASP A CG 763 O OD1 . ASP A 99 ? 0.2572 0.2681 0.2754 -0.0003 0.0007 0.0149 95 ASP A OD1 764 O OD2 . ASP A 99 ? 0.2471 0.2574 0.2635 -0.0037 -0.0020 0.0146 95 ASP A OD2 765 N N . ALA A 100 ? 0.2508 0.2585 0.2737 -0.0004 0.0022 0.0120 96 ALA A N 766 C CA . ALA A 100 ? 0.2518 0.2589 0.2756 0.0004 0.0026 0.0111 96 ALA A CA 767 C C . ALA A 100 ? 0.2380 0.2441 0.2628 0.0017 0.0046 0.0114 96 ALA A C 768 O O . ALA A 100 ? 0.2505 0.2573 0.2778 0.0018 0.0069 0.0108 96 ALA A O 769 C CB . ALA A 100 ? 0.2174 0.2271 0.2437 -0.0003 0.0034 0.0097 96 ALA A CB 770 N N . VAL A 101 ? 0.2399 0.2442 0.2626 0.0028 0.0040 0.0121 97 VAL A N 771 C CA . VAL A 101 ? 0.2330 0.2365 0.2558 0.0044 0.0057 0.0128 97 VAL A CA 772 C C . VAL A 101 ? 0.2360 0.2383 0.2589 0.0056 0.0062 0.0124 97 VAL A C 773 O O . VAL A 101 ? 0.2463 0.2480 0.2696 0.0070 0.0081 0.0130 97 VAL A O 774 C CB . VAL A 101 ? 0.2344 0.2379 0.2549 0.0050 0.0048 0.0139 97 VAL A CB 775 C CG1 . VAL A 101 ? 0.2623 0.2678 0.2831 0.0041 0.0047 0.0143 97 VAL A CG1 776 C CG2 . VAL A 101 ? 0.2374 0.2395 0.2551 0.0048 0.0023 0.0137 97 VAL A CG2 777 N N . HIS A 102 ? 0.2221 0.2242 0.2445 0.0054 0.0048 0.0116 98 HIS A N 778 C CA . HIS A 102 ? 0.2400 0.2418 0.2630 0.0065 0.0054 0.0109 98 HIS A CA 779 C C . HIS A 102 ? 0.2413 0.2444 0.2647 0.0060 0.0042 0.0097 98 HIS A C 780 O O . HIS A 102 ? 0.2335 0.2356 0.2549 0.0068 0.0026 0.0097 98 HIS A O 781 C CB . HIS A 102 ? 0.2270 0.2270 0.2475 0.0082 0.0048 0.0116 98 HIS A CB 782 C CG . HIS A 102 ? 0.2559 0.2543 0.2733 0.0082 0.0022 0.0117 98 HIS A CG 783 N ND1 . HIS A 102 ? 0.2242 0.2210 0.2396 0.0096 0.0012 0.0115 98 HIS A ND1 784 C CD2 . HIS A 102 ? 0.2103 0.2080 0.2261 0.0069 0.0005 0.0120 98 HIS A CD2 785 C CE1 . HIS A 102 ? 0.2320 0.2268 0.2448 0.0091 -0.0008 0.0116 98 HIS A CE1 786 N NE2 . HIS A 102 ? 0.2345 0.2299 0.2476 0.0073 -0.0012 0.0119 98 HIS A NE2 787 N N . GLY A 103 ? 0.2316 0.2371 0.2576 0.0047 0.0050 0.0087 99 GLY A N 788 C CA . GLY A 103 ? 0.2370 0.2445 0.2631 0.0041 0.0037 0.0077 99 GLY A CA 789 C C . GLY A 103 ? 0.2403 0.2475 0.2648 0.0031 0.0022 0.0087 99 GLY A C 790 O O . GLY A 103 ? 0.2376 0.2433 0.2612 0.0027 0.0022 0.0098 99 GLY A O 791 N N . GLN A 104 ? 0.2315 0.2403 0.2555 0.0029 0.0009 0.0082 100 GLN A N 792 C CA . GLN A 104 ? 0.2366 0.2452 0.2589 0.0018 -0.0004 0.0092 100 GLN A CA 793 C C . GLN A 104 ? 0.2422 0.2470 0.2607 0.0024 -0.0022 0.0107 100 GLN A C 794 O O . GLN A 104 ? 0.2447 0.2489 0.2613 0.0029 -0.0034 0.0111 100 GLN A O 795 C CB . GLN A 104 ? 0.2227 0.2351 0.2462 0.0016 -0.0008 0.0082 100 GLN A CB 796 C CG . GLN A 104 ? 0.2210 0.2340 0.2427 0.0009 -0.0021 0.0092 100 GLN A CG 797 C CD . GLN A 104 ? 0.2272 0.2398 0.2489 -0.0007 -0.0019 0.0099 100 GLN A CD 798 O OE1 . GLN A 104 ? 0.2696 0.2845 0.2914 -0.0017 -0.0022 0.0101 100 GLN A OE1 799 N NE2 . GLN A 104 ? 0.1893 0.1993 0.2106 -0.0009 -0.0014 0.0106 100 GLN A NE2 800 N N . ASN A 105 ? 0.2355 0.2378 0.2530 0.0025 -0.0021 0.0113 101 ASN A N 801 C CA . ASN A 105 ? 0.2363 0.2350 0.2509 0.0033 -0.0032 0.0119 101 ASN A CA 802 C C . ASN A 105 ? 0.2512 0.2472 0.2629 0.0023 -0.0047 0.0129 101 ASN A C 803 O O . ASN A 105 ? 0.2387 0.2311 0.2477 0.0030 -0.0055 0.0132 101 ASN A O 804 C CB . ASN A 105 ? 0.2280 0.2256 0.2425 0.0038 -0.0025 0.0120 101 ASN A CB 805 C CG . ASN A 105 ? 0.2579 0.2569 0.2733 0.0025 -0.0019 0.0125 101 ASN A CG 806 O OD1 . ASN A 105 ? 0.2817 0.2803 0.2957 0.0011 -0.0029 0.0130 101 ASN A OD1 807 N ND2 . ASN A 105 ? 0.1756 0.1765 0.1934 0.0029 -0.0002 0.0122 101 ASN A ND2 808 N N . ASN A 106 ? 0.2541 0.2515 0.2660 0.0006 -0.0048 0.0134 102 ASN A N 809 C CA . ASN A 106 ? 0.2513 0.2460 0.2606 -0.0005 -0.0059 0.0145 102 ASN A CA 810 C C . ASN A 106 ? 0.2620 0.2559 0.2697 0.0006 -0.0064 0.0150 102 ASN A C 811 O O . ASN A 106 ? 0.2708 0.2613 0.2757 0.0002 -0.0070 0.0161 102 ASN A O 812 C CB . ASN A 106 ? 0.2506 0.2474 0.2606 -0.0026 -0.0058 0.0149 102 ASN A CB 813 C CG . ASN A 106 ? 0.2813 0.2787 0.2918 -0.0037 -0.0055 0.0147 102 ASN A CG 814 O OD1 . ASN A 106 ? 0.3126 0.3133 0.3252 -0.0040 -0.0047 0.0145 102 ASN A OD1 815 N ND2 . ASN A 106 ? 0.2455 0.2400 0.2540 -0.0042 -0.0061 0.0148 102 ASN A ND2 816 N N . VAL A 107 ? 0.2402 0.2374 0.2498 0.0020 -0.0060 0.0141 103 VAL A N 817 C CA . VAL A 107 ? 0.2455 0.2437 0.2540 0.0033 -0.0065 0.0145 103 VAL A CA 818 C C . VAL A 107 ? 0.2719 0.2680 0.2786 0.0058 -0.0069 0.0145 103 VAL A C 819 O O . VAL A 107 ? 0.2593 0.2563 0.2674 0.0069 -0.0065 0.0134 103 VAL A O 820 C CB . VAL A 107 ? 0.2421 0.2465 0.2538 0.0033 -0.0058 0.0133 103 VAL A CB 821 C CG1 . VAL A 107 ? 0.2393 0.2461 0.2499 0.0051 -0.0064 0.0135 103 VAL A CG1 822 C CG2 . VAL A 107 ? 0.2430 0.2492 0.2562 0.0010 -0.0054 0.0134 103 VAL A CG2 823 N N . TYR A 108 ? 0.2718 0.2649 0.2752 0.0069 -0.0076 0.0160 104 TYR A N 824 C CA . TYR A 108 ? 0.2650 0.2561 0.2661 0.0098 -0.0080 0.0161 104 TYR A CA 825 C C . TYR A 108 ? 0.2788 0.2761 0.2824 0.0118 -0.0078 0.0147 104 TYR A C 826 O O . TYR A 108 ? 0.2681 0.2703 0.2731 0.0116 -0.0078 0.0143 104 TYR A O 827 C CB . TYR A 108 ? 0.2838 0.2709 0.2809 0.0110 -0.0083 0.0182 104 TYR A CB 828 C CG . TYR A 108 ? 0.3097 0.2936 0.3041 0.0142 -0.0086 0.0185 104 TYR A CG 829 C CD1 . TYR A 108 ? 0.3369 0.3145 0.3292 0.0142 -0.0087 0.0186 104 TYR A CD1 830 C CD2 . TYR A 108 ? 0.3867 0.3744 0.3807 0.0173 -0.0089 0.0185 104 TYR A CD2 831 C CE1 . TYR A 108 ? 0.3561 0.3308 0.3458 0.0174 -0.0089 0.0188 104 TYR A CE1 832 C CE2 . TYR A 108 ? 0.4186 0.4039 0.4101 0.0206 -0.0091 0.0188 104 TYR A CE2 833 C CZ . TYR A 108 ? 0.4032 0.3817 0.3925 0.0206 -0.0091 0.0190 104 TYR A CZ 834 O OH . TYR A 108 ? 0.4849 0.4610 0.4717 0.0242 -0.0093 0.0192 104 TYR A OH 835 N N . GLY A 109 ? 0.2767 0.2742 0.2807 0.0136 -0.0078 0.0137 105 GLY A N 836 C CA . GLY A 109 ? 0.2658 0.2697 0.2723 0.0152 -0.0075 0.0120 105 GLY A CA 837 C C . GLY A 109 ? 0.2631 0.2717 0.2744 0.0132 -0.0064 0.0099 105 GLY A C 838 O O . GLY A 109 ? 0.2622 0.2762 0.2760 0.0140 -0.0059 0.0081 105 GLY A O 839 N N . ALA A 110 ? 0.2641 0.2707 0.2764 0.0107 -0.0058 0.0102 106 ALA A N 840 C CA . ALA A 110 ? 0.2565 0.2664 0.2730 0.0091 -0.0043 0.0085 106 ALA A CA 841 C C . ALA A 110 ? 0.2496 0.2587 0.2671 0.0100 -0.0035 0.0077 106 ALA A C 842 O O . ALA A 110 ? 0.2282 0.2329 0.2431 0.0109 -0.0040 0.0087 106 ALA A O 843 C CB . ALA A 110 ? 0.2455 0.2535 0.2625 0.0068 -0.0038 0.0092 106 ALA A CB 844 N N . THR A 111 ? 0.2324 0.2456 0.2535 0.0096 -0.0020 0.0059 107 THR A N 845 C CA . THR A 111 ? 0.2355 0.2481 0.2578 0.0102 -0.0008 0.0053 107 THR A CA 846 C C . THR A 111 ? 0.2329 0.2412 0.2544 0.0094 -0.0003 0.0066 107 THR A C 847 O O . THR A 111 ? 0.2573 0.2655 0.2799 0.0076 0.0004 0.0069 107 THR A O 848 C CB . THR A 111 ? 0.2331 0.2505 0.2599 0.0092 0.0012 0.0031 107 THR A CB 849 O OG1 . THR A 111 ? 0.2445 0.2672 0.2723 0.0099 0.0005 0.0015 107 THR A OG1 850 C CG2 . THR A 111 ? 0.2358 0.2525 0.2636 0.0099 0.0025 0.0028 107 THR A CG2 851 N N . ILE A 112 ? 0.2314 0.2365 0.2508 0.0107 -0.0006 0.0073 108 ILE A N 852 C CA . ILE A 112 ? 0.2370 0.2391 0.2555 0.0102 -0.0001 0.0083 108 ILE A CA 853 C C . ILE A 112 ? 0.2363 0.2392 0.2568 0.0108 0.0019 0.0079 108 ILE A C 854 O O . ILE A 112 ? 0.2475 0.2506 0.2675 0.0125 0.0018 0.0075 108 ILE A O 855 C CB . ILE A 112 ? 0.2372 0.2348 0.2516 0.0111 -0.0019 0.0094 108 ILE A CB 856 C CG1 . ILE A 112 ? 0.2151 0.2111 0.2274 0.0104 -0.0035 0.0101 108 ILE A CG1 857 C CG2 . ILE A 112 ? 0.2426 0.2385 0.2565 0.0104 -0.0014 0.0102 108 ILE A CG2 858 C CD1 . ILE A 112 ? 0.2084 0.2055 0.2218 0.0080 -0.0033 0.0106 108 ILE A CD1 859 N N . PHE A 113 ? 0.2296 0.2332 0.2524 0.0096 0.0038 0.0080 109 PHE A N 860 C CA . PHE A 113 ? 0.2219 0.2259 0.2465 0.0101 0.0062 0.0079 109 PHE A CA 861 C C . PHE A 113 ? 0.2387 0.2400 0.2608 0.0114 0.0061 0.0094 109 PHE A C 862 O O . PHE A 113 ? 0.2542 0.2538 0.2739 0.0113 0.0045 0.0102 109 PHE A O 863 C CB . PHE A 113 ? 0.2351 0.2405 0.2631 0.0084 0.0087 0.0075 109 PHE A CB 864 C CG . PHE A 113 ? 0.2430 0.2518 0.2739 0.0071 0.0090 0.0055 109 PHE A CG 865 C CD1 . PHE A 113 ? 0.2204 0.2318 0.2541 0.0070 0.0107 0.0039 109 PHE A CD1 866 C CD2 . PHE A 113 ? 0.2286 0.2386 0.2592 0.0060 0.0075 0.0052 109 PHE A CD2 867 C CE1 . PHE A 113 ? 0.2298 0.2456 0.2665 0.0057 0.0110 0.0015 109 PHE A CE1 868 C CE2 . PHE A 113 ? 0.2630 0.2772 0.2963 0.0050 0.0076 0.0030 109 PHE A CE2 869 C CZ . PHE A 113 ? 0.2380 0.2553 0.2744 0.0049 0.0094 0.0011 109 PHE A CZ 870 N N . PRO A 114 ? 0.2400 0.2415 0.2629 0.0127 0.0079 0.0096 110 PRO A N 871 C CA . PRO A 114 ? 0.2279 0.2277 0.2485 0.0141 0.0081 0.0110 110 PRO A CA 872 C C . PRO A 114 ? 0.2443 0.2435 0.2647 0.0134 0.0086 0.0121 110 PRO A C 873 O O . PRO A 114 ? 0.2323 0.2323 0.2552 0.0121 0.0102 0.0120 110 PRO A O 874 C CB . PRO A 114 ? 0.2236 0.2242 0.2459 0.0152 0.0110 0.0112 110 PRO A CB 875 C CG . PRO A 114 ? 0.2158 0.2186 0.2404 0.0147 0.0112 0.0094 110 PRO A CG 876 C CD . PRO A 114 ? 0.2257 0.2294 0.2517 0.0125 0.0103 0.0085 110 PRO A CD 877 N N . HIS A 115 ? 0.2361 0.2344 0.2537 0.0142 0.0073 0.0129 111 HIS A N 878 C CA . HIS A 115 ? 0.2311 0.2298 0.2484 0.0141 0.0079 0.0140 111 HIS A CA 879 C C . HIS A 115 ? 0.2383 0.2373 0.2570 0.0154 0.0112 0.0153 111 HIS A C 880 O O . HIS A 115 ? 0.2483 0.2472 0.2678 0.0165 0.0129 0.0154 111 HIS A O 881 C CB . HIS A 115 ? 0.2261 0.2245 0.2401 0.0148 0.0057 0.0142 111 HIS A CB 882 C CG . HIS A 115 ? 0.2268 0.2246 0.2398 0.0128 0.0033 0.0135 111 HIS A CG 883 N ND1 . HIS A 115 ? 0.2542 0.2528 0.2684 0.0111 0.0033 0.0138 111 HIS A ND1 884 C CD2 . HIS A 115 ? 0.2190 0.2152 0.2299 0.0123 0.0010 0.0127 111 HIS A CD2 885 C CE1 . HIS A 115 ? 0.2629 0.2607 0.2758 0.0096 0.0012 0.0132 111 HIS A CE1 886 N NE2 . HIS A 115 ? 0.2420 0.2380 0.2528 0.0102 -0.0002 0.0126 111 HIS A NE2 887 N N . ASN A 116 ? 0.2441 0.2435 0.2630 0.0153 0.0121 0.0163 112 ASN A N 888 C CA . ASN A 116 ? 0.2549 0.2539 0.2751 0.0165 0.0156 0.0177 112 ASN A CA 889 C C . ASN A 116 ? 0.2492 0.2482 0.2681 0.0192 0.0172 0.0190 112 ASN A C 890 O O . ASN A 116 ? 0.2708 0.2687 0.2913 0.0198 0.0204 0.0197 112 ASN A O 891 C CB . ASN A 116 ? 0.2432 0.2430 0.2630 0.0167 0.0159 0.0187 112 ASN A CB 892 C CG . ASN A 116 ? 0.2435 0.2432 0.2654 0.0143 0.0158 0.0177 112 ASN A CG 893 O OD1 . ASN A 116 ? 0.3050 0.3055 0.3267 0.0143 0.0160 0.0184 112 ASN A OD1 894 N ND2 . ASN A 116 ? 0.2075 0.2069 0.2314 0.0124 0.0155 0.0161 112 ASN A ND2 895 N N . VAL A 117 ? 0.2645 0.2646 0.2804 0.0208 0.0152 0.0192 113 VAL A N 896 C CA . VAL A 117 ? 0.2644 0.2650 0.2788 0.0237 0.0169 0.0206 113 VAL A CA 897 C C . VAL A 117 ? 0.2485 0.2480 0.2644 0.0236 0.0183 0.0201 113 VAL A C 898 O O . VAL A 117 ? 0.2586 0.2576 0.2753 0.0251 0.0216 0.0215 113 VAL A O 899 C CB . VAL A 117 ? 0.2685 0.2712 0.2796 0.0253 0.0144 0.0205 113 VAL A CB 900 C CG1 . VAL A 117 ? 0.2642 0.2663 0.2745 0.0238 0.0111 0.0183 113 VAL A CG1 901 C CG2 . VAL A 117 ? 0.2971 0.3008 0.3066 0.0286 0.0164 0.0220 113 VAL A CG2 902 N N . GLY A 118 ? 0.2490 0.2484 0.2657 0.0219 0.0162 0.0181 114 GLY A N 903 C CA . GLY A 118 ? 0.2326 0.2317 0.2510 0.0217 0.0175 0.0173 114 GLY A CA 904 C C . GLY A 118 ? 0.2442 0.2428 0.2663 0.0202 0.0207 0.0172 114 GLY A C 905 O O . GLY A 118 ? 0.2468 0.2454 0.2706 0.0205 0.0234 0.0173 114 GLY A O 906 N N . LEU A 119 ? 0.2527 0.2509 0.2763 0.0183 0.0206 0.0168 115 LEU A N 907 C CA . LEU A 119 ? 0.2383 0.2357 0.2655 0.0167 0.0241 0.0165 115 LEU A CA 908 C C . LEU A 119 ? 0.2494 0.2450 0.2765 0.0185 0.0280 0.0188 115 LEU A C 909 O O . LEU A 119 ? 0.2629 0.2574 0.2926 0.0179 0.0315 0.0186 115 LEU A O 910 C CB . LEU A 119 ? 0.2386 0.2360 0.2673 0.0146 0.0233 0.0155 115 LEU A CB 911 C CG . LEU A 119 ? 0.2562 0.2553 0.2848 0.0129 0.0198 0.0135 115 LEU A CG 912 C CD1 . LEU A 119 ? 0.2539 0.2534 0.2840 0.0109 0.0192 0.0127 115 LEU A CD1 913 C CD2 . LEU A 119 ? 0.2335 0.2341 0.2641 0.0122 0.0200 0.0117 115 LEU A CD2 914 N N . GLY A 120 ? 0.2453 0.2407 0.2694 0.0208 0.0276 0.0208 116 GLY A N 915 C CA . GLY A 120 ? 0.2573 0.2513 0.2807 0.0234 0.0313 0.0235 116 GLY A CA 916 C C . GLY A 120 ? 0.2751 0.2691 0.2985 0.0246 0.0332 0.0240 116 GLY A C 917 O O . GLY A 120 ? 0.3047 0.2967 0.3292 0.0253 0.0374 0.0254 116 GLY A O 918 N N . ALA A 121 ? 0.2592 0.2553 0.2812 0.0250 0.0302 0.0228 117 ALA A N 919 C CA . ALA A 121 ? 0.2676 0.2642 0.2896 0.0261 0.0317 0.0229 117 ALA A CA 920 C C . ALA A 121 ? 0.2779 0.2739 0.3041 0.0237 0.0346 0.0216 117 ALA A C 921 O O . ALA A 121 ? 0.2965 0.2923 0.3234 0.0246 0.0375 0.0224 117 ALA A O 922 C CB . ALA A 121 ? 0.2575 0.2563 0.2772 0.0270 0.0277 0.0216 117 ALA A CB 923 N N . THR A 122 ? 0.2705 0.2665 0.2996 0.0207 0.0340 0.0195 118 THR A N 924 C CA . THR A 122 ? 0.2676 0.2637 0.3009 0.0182 0.0368 0.0177 118 THR A CA 925 C C . THR A 122 ? 0.2855 0.2785 0.3210 0.0177 0.0422 0.0191 118 THR A C 926 O O . THR A 122 ? 0.3050 0.2980 0.3437 0.0160 0.0453 0.0180 118 THR A O 927 C CB . THR A 122 ? 0.2759 0.2736 0.3118 0.0151 0.0348 0.0148 118 THR A CB 928 O OG1 . THR A 122 ? 0.2800 0.2756 0.3165 0.0142 0.0357 0.0152 118 THR A OG1 929 C CG2 . THR A 122 ? 0.2631 0.2632 0.2967 0.0156 0.0296 0.0136 118 THR A CG2 930 N N . ARG A 123 ? 0.2987 0.2891 0.3324 0.0193 0.0434 0.0215 119 ARG A N 931 C CA . ARG A 123 ? 0.3123 0.2989 0.3479 0.0188 0.0485 0.0227 119 ARG A CA 932 C C . ARG A 123 ? 0.3285 0.3147 0.3690 0.0147 0.0503 0.0196 119 ARG A C 933 O O . ARG A 123 ? 0.3156 0.2991 0.3589 0.0133 0.0553 0.0196 119 ARG A O 934 C CB . ARG A 123 ? 0.3466 0.3313 0.3814 0.0210 0.0528 0.0253 119 ARG A CB 935 C CG . ARG A 123 ? 0.3259 0.3116 0.3559 0.0253 0.0513 0.0283 119 ARG A CG 936 C CD . ARG A 123 ? 0.3533 0.3377 0.3803 0.0278 0.0509 0.0307 119 ARG A CD 937 N NE . ARG A 123 ? 0.3678 0.3530 0.3907 0.0322 0.0514 0.0339 119 ARG A NE 938 C CZ . ARG A 123 ? 0.3978 0.3868 0.4177 0.0341 0.0475 0.0337 119 ARG A CZ 939 N NH1 . ARG A 123 ? 0.2813 0.2729 0.3015 0.0321 0.0426 0.0308 119 ARG A NH1 940 N NH2 . ARG A 123 ? 0.3224 0.3125 0.3389 0.0381 0.0485 0.0365 119 ARG A NH2 941 N N . ASP A 124 ? 0.3038 0.2929 0.3455 0.0126 0.0465 0.0168 120 ASP A N 942 C CA . ASP A 124 ? 0.2974 0.2879 0.3437 0.0088 0.0476 0.0132 120 ASP A CA 943 C C . ASP A 124 ? 0.2989 0.2891 0.3458 0.0073 0.0461 0.0120 120 ASP A C 944 O O . ASP A 124 ? 0.2823 0.2757 0.3287 0.0066 0.0419 0.0104 120 ASP A O 945 C CB . ASP A 124 ? 0.3049 0.3002 0.3522 0.0078 0.0446 0.0106 120 ASP A CB 946 C CG . ASP A 124 ? 0.3518 0.3497 0.4041 0.0040 0.0462 0.0068 120 ASP A CG 947 O OD1 . ASP A 124 ? 0.3468 0.3432 0.4017 0.0019 0.0484 0.0055 120 ASP A OD1 948 O OD2 . ASP A 124 ? 0.4008 0.4028 0.4545 0.0035 0.0452 0.0049 120 ASP A OD2 949 N N . PRO A 125 ? 0.2997 0.2859 0.3475 0.0071 0.0497 0.0130 121 PRO A N 950 C CA . PRO A 125 ? 0.2997 0.2858 0.3478 0.0060 0.0483 0.0120 121 PRO A CA 951 C C . PRO A 125 ? 0.3027 0.2921 0.3545 0.0025 0.0472 0.0079 121 PRO A C 952 O O . PRO A 125 ? 0.3043 0.2957 0.3557 0.0019 0.0441 0.0068 121 PRO A O 953 C CB . PRO A 125 ? 0.3139 0.2945 0.3623 0.0068 0.0533 0.0140 121 PRO A CB 954 C CG . PRO A 125 ? 0.3279 0.3062 0.3741 0.0097 0.0557 0.0172 121 PRO A CG 955 C CD . PRO A 125 ? 0.3078 0.2891 0.3557 0.0082 0.0552 0.0154 121 PRO A CD 956 N N . TYR A 126 ? 0.2909 0.2815 0.3465 0.0001 0.0497 0.0054 122 TYR A N 957 C CA . TYR A 126 ? 0.2940 0.2892 0.3533 -0.0031 0.0484 0.0011 122 TYR A CA 958 C C . TYR A 126 ? 0.2797 0.2802 0.3373 -0.0025 0.0430 0.0001 122 TYR A C 959 O O . TYR A 126 ? 0.2811 0.2852 0.3397 -0.0039 0.0404 -0.0023 122 TYR A O 960 C CB . TYR A 126 ? 0.3124 0.3086 0.3764 -0.0059 0.0524 -0.0018 122 TYR A CB 961 C CG . TYR A 126 ? 0.3232 0.3248 0.3912 -0.0092 0.0513 -0.0065 122 TYR A CG 962 C CD1 . TYR A 126 ? 0.3746 0.3762 0.4435 -0.0106 0.0508 -0.0081 122 TYR A CD1 963 C CD2 . TYR A 126 ? 0.3666 0.3741 0.4371 -0.0107 0.0505 -0.0095 122 TYR A CD2 964 C CE1 . TYR A 126 ? 0.4202 0.4276 0.4926 -0.0134 0.0496 -0.0127 122 TYR A CE1 965 C CE2 . TYR A 126 ? 0.3918 0.4054 0.4660 -0.0134 0.0494 -0.0141 122 TYR A CE2 966 C CZ . TYR A 126 ? 0.4419 0.4554 0.5168 -0.0147 0.0488 -0.0156 122 TYR A CZ 967 O OH . TYR A 126 ? 0.4694 0.4896 0.5476 -0.0171 0.0475 -0.0201 122 TYR A OH 968 N N . LEU A 127 ? 0.2914 0.2926 0.3464 -0.0003 0.0413 0.0019 123 LEU A N 969 C CA . LEU A 127 ? 0.2763 0.2811 0.3289 0.0008 0.0363 0.0016 123 LEU A CA 970 C C . LEU A 127 ? 0.2683 0.2722 0.3180 0.0016 0.0332 0.0028 123 LEU A C 971 O O . LEU A 127 ? 0.2625 0.2696 0.3119 0.0010 0.0299 0.0013 123 LEU A O 972 C CB . LEU A 127 ? 0.2854 0.2897 0.3349 0.0035 0.0354 0.0038 123 LEU A CB 973 C CG . LEU A 127 ? 0.2940 0.3004 0.3400 0.0053 0.0304 0.0042 123 LEU A CG 974 C CD1 . LEU A 127 ? 0.2451 0.2567 0.2931 0.0042 0.0287 0.0012 123 LEU A CD1 975 C CD2 . LEU A 127 ? 0.2670 0.2715 0.3092 0.0084 0.0298 0.0070 123 LEU A CD2 976 N N . VAL A 128 ? 0.2527 0.2526 0.3002 0.0031 0.0343 0.0056 124 VAL A N 977 C CA . VAL A 128 ? 0.2518 0.2511 0.2965 0.0040 0.0316 0.0069 124 VAL A CA 978 C C . VAL A 128 ? 0.2593 0.2599 0.3066 0.0016 0.0317 0.0047 124 VAL A C 979 O O . VAL A 128 ? 0.2450 0.2478 0.2911 0.0013 0.0283 0.0041 124 VAL A O 980 C CB . VAL A 128 ? 0.2396 0.2354 0.2813 0.0066 0.0326 0.0104 124 VAL A CB 981 C CG1 . VAL A 128 ? 0.2375 0.2332 0.2769 0.0071 0.0303 0.0114 124 VAL A CG1 982 C CG2 . VAL A 128 ? 0.2593 0.2551 0.2979 0.0090 0.0312 0.0121 124 VAL A CG2 983 N N . LYS A 129 ? 0.2584 0.2578 0.3093 -0.0001 0.0357 0.0031 125 LYS A N 984 C CA . LYS A 129 ? 0.2607 0.2619 0.3144 -0.0025 0.0359 0.0004 125 LYS A CA 985 C C . LYS A 129 ? 0.2665 0.2734 0.3212 -0.0039 0.0326 -0.0025 125 LYS A C 986 O O . LYS A 129 ? 0.2593 0.2685 0.3135 -0.0044 0.0301 -0.0033 125 LYS A O 987 C CB . LYS A 129 ? 0.2717 0.2708 0.3295 -0.0046 0.0410 -0.0014 125 LYS A CB 988 C CG . LYS A 129 ? 0.2613 0.2619 0.3219 -0.0070 0.0415 -0.0045 125 LYS A CG 989 C CD . LYS A 129 ? 0.3027 0.3007 0.3677 -0.0094 0.0470 -0.0068 125 LYS A CD 990 C CE . LYS A 129 ? 0.3163 0.3155 0.3840 -0.0117 0.0477 -0.0099 125 LYS A CE 991 N NZ . LYS A 129 ? 0.3393 0.3351 0.4112 -0.0143 0.0533 -0.0124 125 LYS A NZ 992 N N . ARG A 130 ? 0.2459 0.2555 0.3019 -0.0042 0.0326 -0.0038 126 ARG A N 993 C CA . ARG A 130 ? 0.2457 0.2611 0.3025 -0.0049 0.0296 -0.0064 126 ARG A CA 994 C C . ARG A 130 ? 0.2342 0.2502 0.2866 -0.0029 0.0251 -0.0043 126 ARG A C 995 O O . ARG A 130 ? 0.2368 0.2566 0.2891 -0.0032 0.0224 -0.0057 126 ARG A O 996 C CB . ARG A 130 ? 0.2579 0.2760 0.3165 -0.0050 0.0306 -0.0077 126 ARG A CB 997 C CG . ARG A 130 ? 0.3011 0.3195 0.3649 -0.0079 0.0354 -0.0106 126 ARG A CG 998 C CD . ARG A 130 ? 0.4140 0.4306 0.4783 -0.0073 0.0381 -0.0095 126 ARG A CD 999 N NE . ARG A 130 ? 0.4252 0.4468 0.4890 -0.0064 0.0354 -0.0105 126 ARG A NE 1000 C CZ . ARG A 130 ? 0.3847 0.4065 0.4470 -0.0046 0.0351 -0.0091 126 ARG A CZ 1001 N NH1 . ARG A 130 ? 0.3665 0.3840 0.4279 -0.0036 0.0378 -0.0067 126 ARG A NH1 1002 N NH2 . ARG A 130 ? 0.3343 0.3614 0.3961 -0.0038 0.0321 -0.0106 126 ARG A NH2 1003 N N . ILE A 131 ? 0.2359 0.2482 0.2848 -0.0007 0.0242 -0.0012 127 ILE A N 1004 C CA . ILE A 131 ? 0.2172 0.2293 0.2620 0.0008 0.0202 0.0006 127 ILE A CA 1005 C C . ILE A 131 ? 0.2380 0.2498 0.2823 0.0000 0.0194 0.0008 127 ILE A C 1006 O O . ILE A 131 ? 0.2411 0.2550 0.2839 0.0000 0.0165 0.0006 127 ILE A O 1007 C CB . ILE A 131 ? 0.2269 0.2354 0.2682 0.0031 0.0197 0.0035 127 ILE A CB 1008 C CG1 . ILE A 131 ? 0.2279 0.2373 0.2693 0.0041 0.0200 0.0032 127 ILE A CG1 1009 C CG2 . ILE A 131 ? 0.2482 0.2558 0.2855 0.0041 0.0161 0.0053 127 ILE A CG2 1010 C CD1 . ILE A 131 ? 0.2229 0.2290 0.2610 0.0065 0.0199 0.0060 127 ILE A CD1 1011 N N . GLY A 132 ? 0.2296 0.2390 0.2752 -0.0006 0.0221 0.0013 128 GLY A N 1012 C CA . GLY A 132 ? 0.2285 0.2383 0.2741 -0.0015 0.0215 0.0011 128 GLY A CA 1013 C C . GLY A 132 ? 0.2334 0.2478 0.2815 -0.0033 0.0206 -0.0020 128 GLY A C 1014 O O . GLY A 132 ? 0.2118 0.2281 0.2587 -0.0035 0.0183 -0.0020 128 GLY A O 1015 N N . GLU A 133 ? 0.2282 0.2448 0.2799 -0.0047 0.0227 -0.0048 129 GLU A N 1016 C CA . GLU A 133 ? 0.2243 0.2464 0.2786 -0.0064 0.0220 -0.0081 129 GLU A CA 1017 C C . GLU A 133 ? 0.2323 0.2580 0.2841 -0.0052 0.0181 -0.0079 129 GLU A C 1018 O O . GLU A 133 ? 0.2392 0.2682 0.2908 -0.0056 0.0163 -0.0088 129 GLU A O 1019 C CB . GLU A 133 ? 0.2328 0.2572 0.2917 -0.0083 0.0251 -0.0115 129 GLU A CB 1020 C CG . GLU A 133 ? 0.2277 0.2473 0.2887 -0.0094 0.0294 -0.0115 129 GLU A CG 1021 C CD . GLU A 133 ? 0.3494 0.3698 0.4151 -0.0116 0.0334 -0.0146 129 GLU A CD 1022 O OE1 . GLU A 133 ? 0.3035 0.3205 0.3717 -0.0131 0.0373 -0.0155 129 GLU A OE1 1023 O OE2 . GLU A 133 ? 0.3329 0.3571 0.3997 -0.0118 0.0328 -0.0161 129 GLU A OE2 1024 N N . ALA A 134 ? 0.2281 0.2533 0.2781 -0.0037 0.0169 -0.0067 130 ALA A N 1025 C CA . ALA A 134 ? 0.2367 0.2646 0.2841 -0.0022 0.0135 -0.0063 130 ALA A CA 1026 C C . ALA A 134 ? 0.2333 0.2586 0.2768 -0.0013 0.0110 -0.0036 130 ALA A C 1027 O O . ALA A 134 ? 0.2357 0.2636 0.2776 -0.0009 0.0087 -0.0037 130 ALA A O 1028 C CB . ALA A 134 ? 0.2528 0.2796 0.2988 -0.0004 0.0131 -0.0053 130 ALA A CB 1029 N N . THR A 135 ? 0.2442 0.2647 0.2860 -0.0009 0.0116 -0.0013 131 THR A N 1030 C CA . THR A 135 ? 0.2348 0.2532 0.2732 -0.0005 0.0095 0.0010 131 THR A CA 1031 C C . THR A 135 ? 0.2361 0.2568 0.2754 -0.0018 0.0092 0.0002 131 THR A C 1032 O O . THR A 135 ? 0.2465 0.2683 0.2836 -0.0016 0.0069 0.0010 131 THR A O 1033 C CB . THR A 135 ? 0.2415 0.2553 0.2785 0.0002 0.0105 0.0033 131 THR A CB 1034 O OG1 . THR A 135 ? 0.2522 0.2641 0.2878 0.0016 0.0105 0.0042 131 THR A OG1 1035 C CG2 . THR A 135 ? 0.2263 0.2387 0.2601 0.0003 0.0084 0.0053 131 THR A CG2 1036 N N . ALA A 136 ? 0.2350 0.2568 0.2776 -0.0032 0.0117 -0.0016 132 ALA A N 1037 C CA . ALA A 136 ? 0.2364 0.2609 0.2801 -0.0044 0.0114 -0.0028 132 ALA A CA 1038 C C . ALA A 136 ? 0.2317 0.2613 0.2753 -0.0043 0.0093 -0.0043 132 ALA A C 1039 O O . ALA A 136 ? 0.2369 0.2684 0.2792 -0.0044 0.0077 -0.0038 132 ALA A O 1040 C CB . ALA A 136 ? 0.2312 0.2560 0.2790 -0.0059 0.0148 -0.0052 132 ALA A CB 1041 N N . LEU A 137 ? 0.2410 0.2734 0.2860 -0.0041 0.0095 -0.0061 133 LEU A N 1042 C CA . LEU A 137 ? 0.2323 0.2706 0.2773 -0.0036 0.0076 -0.0077 133 LEU A CA 1043 C C . LEU A 137 ? 0.2299 0.2665 0.2702 -0.0017 0.0047 -0.0047 133 LEU A C 1044 O O . LEU A 137 ? 0.2349 0.2749 0.2740 -0.0013 0.0031 -0.0047 133 LEU A O 1045 C CB . LEU A 137 ? 0.2214 0.2635 0.2688 -0.0034 0.0083 -0.0102 133 LEU A CB 1046 C CG . LEU A 137 ? 0.2672 0.3118 0.3198 -0.0057 0.0115 -0.0139 133 LEU A CG 1047 C CD1 . LEU A 137 ? 0.2489 0.2973 0.3040 -0.0057 0.0123 -0.0163 133 LEU A CD1 1048 C CD2 . LEU A 137 ? 0.2745 0.3244 0.3293 -0.0071 0.0116 -0.0167 133 LEU A CD2 1049 N N . GLU A 138 ? 0.2075 0.2392 0.2454 -0.0006 0.0043 -0.0024 134 GLU A N 1050 C CA . GLU A 138 ? 0.2258 0.2553 0.2593 0.0010 0.0018 0.0001 134 GLU A CA 1051 C C . GLU A 138 ? 0.2233 0.2503 0.2547 0.0002 0.0010 0.0021 134 GLU A C 1052 O O . GLU A 138 ? 0.2295 0.2561 0.2579 0.0009 -0.0007 0.0037 134 GLU A O 1053 C CB . GLU A 138 ? 0.2235 0.2488 0.2549 0.0024 0.0014 0.0016 134 GLU A CB 1054 C CG . GLU A 138 ? 0.2415 0.2700 0.2750 0.0033 0.0022 -0.0005 134 GLU A CG 1055 C CD . GLU A 138 ? 0.2989 0.3250 0.3296 0.0055 0.0010 0.0008 134 GLU A CD 1056 O OE1 . GLU A 138 ? 0.2392 0.2612 0.2661 0.0064 -0.0005 0.0031 134 GLU A OE1 1057 O OE2 . GLU A 138 ? 0.2768 0.3053 0.3091 0.0063 0.0017 -0.0006 134 GLU A OE2 1058 N N . VAL A 139 ? 0.2300 0.2553 0.2629 -0.0011 0.0025 0.0022 135 VAL A N 1059 C CA . VAL A 139 ? 0.2326 0.2569 0.2640 -0.0020 0.0019 0.0037 135 VAL A CA 1060 C C . VAL A 139 ? 0.2332 0.2625 0.2656 -0.0026 0.0014 0.0025 135 VAL A C 1061 O O . VAL A 139 ? 0.2363 0.2658 0.2663 -0.0026 -0.0001 0.0039 135 VAL A O 1062 C CB . VAL A 139 ? 0.2275 0.2494 0.2602 -0.0028 0.0037 0.0040 135 VAL A CB 1063 C CG1 . VAL A 139 ? 0.2215 0.2437 0.2532 -0.0037 0.0031 0.0052 135 VAL A CG1 1064 C CG2 . VAL A 139 ? 0.2120 0.2295 0.2429 -0.0018 0.0037 0.0057 135 VAL A CG2 1065 N N . ARG A 140 ? 0.2316 0.2649 0.2675 -0.0033 0.0028 -0.0004 136 ARG A N 1066 C CA . ARG A 140 ? 0.2424 0.2812 0.2793 -0.0037 0.0023 -0.0021 136 ARG A CA 1067 C C . ARG A 140 ? 0.2505 0.2925 0.2852 -0.0021 0.0003 -0.0017 136 ARG A C 1068 O O . ARG A 140 ? 0.2446 0.2903 0.2784 -0.0019 -0.0006 -0.0017 136 ARG A O 1069 C CB . ARG A 140 ? 0.2165 0.2593 0.2581 -0.0050 0.0045 -0.0059 136 ARG A CB 1070 C CG . ARG A 140 ? 0.2116 0.2518 0.2551 -0.0064 0.0066 -0.0062 136 ARG A CG 1071 C CD . ARG A 140 ? 0.2145 0.2566 0.2570 -0.0069 0.0058 -0.0056 136 ARG A CD 1072 N NE . ARG A 140 ? 0.2481 0.2886 0.2929 -0.0080 0.0081 -0.0066 136 ARG A NE 1073 C CZ . ARG A 140 ? 0.2723 0.3153 0.3177 -0.0087 0.0083 -0.0074 136 ARG A CZ 1074 N NH1 . ARG A 140 ? 0.2111 0.2582 0.2550 -0.0084 0.0063 -0.0071 136 ARG A NH1 1075 N NH2 . ARG A 140 ? 0.2644 0.3057 0.3119 -0.0094 0.0106 -0.0084 136 ARG A NH2 1076 N N . ALA A 141 ? 0.2344 0.2751 0.2681 -0.0006 -0.0002 -0.0012 137 ALA A N 1077 C CA . ALA A 141 ? 0.2329 0.2755 0.2636 0.0015 -0.0021 -0.0002 137 ALA A CA 1078 C C . ALA A 141 ? 0.2345 0.2739 0.2611 0.0019 -0.0035 0.0030 137 ALA A C 1079 O O . ALA A 141 ? 0.2311 0.2729 0.2553 0.0034 -0.0047 0.0040 137 ALA A O 1080 C CB . ALA A 141 ? 0.2329 0.2732 0.2624 0.0033 -0.0024 0.0003 137 ALA A CB 1081 N N . THR A 142 ? 0.2323 0.2664 0.2580 0.0006 -0.0032 0.0048 138 THR A N 1082 C CA . THR A 142 ? 0.2404 0.2711 0.2624 0.0004 -0.0042 0.0077 138 THR A CA 1083 C C . THR A 142 ? 0.2494 0.2823 0.2724 -0.0013 -0.0039 0.0076 138 THR A C 1084 O O . THR A 142 ? 0.2540 0.2846 0.2746 -0.0019 -0.0044 0.0098 138 THR A O 1085 C CB . THR A 142 ? 0.2617 0.2858 0.2818 0.0001 -0.0043 0.0095 138 THR A CB 1086 O OG1 . THR A 142 ? 0.2420 0.2651 0.2646 -0.0013 -0.0031 0.0087 138 THR A OG1 1087 C CG2 . THR A 142 ? 0.2591 0.2811 0.2781 0.0020 -0.0047 0.0095 138 THR A CG2 1088 N N . GLY A 143 ? 0.2456 0.2832 0.2722 -0.0020 -0.0028 0.0050 139 GLY A N 1089 C CA . GLY A 143 ? 0.2335 0.2739 0.2609 -0.0033 -0.0025 0.0047 139 GLY A CA 1090 C C . GLY A 143 ? 0.2631 0.3002 0.2916 -0.0048 -0.0014 0.0051 139 GLY A C 1091 O O . GLY A 143 ? 0.2751 0.3139 0.3041 -0.0059 -0.0011 0.0052 139 GLY A O 1092 N N . ILE A 144 ? 0.2185 0.2514 0.2472 -0.0047 -0.0009 0.0055 140 ILE A N 1093 C CA . ILE A 144 ? 0.2250 0.2550 0.2540 -0.0056 0.0000 0.0063 140 ILE A CA 1094 C C . ILE A 144 ? 0.2433 0.2741 0.2759 -0.0060 0.0022 0.0042 140 ILE A C 1095 O O . ILE A 144 ? 0.2312 0.2627 0.2657 -0.0056 0.0031 0.0023 140 ILE A O 1096 C CB . ILE A 144 ? 0.2299 0.2549 0.2564 -0.0053 -0.0007 0.0084 140 ILE A CB 1097 C CG1 . ILE A 144 ? 0.2331 0.2569 0.2561 -0.0055 -0.0024 0.0105 140 ILE A CG1 1098 C CG2 . ILE A 144 ? 0.2071 0.2298 0.2342 -0.0056 0.0005 0.0089 140 ILE A CG2 1099 C CD1 . ILE A 144 ? 0.2223 0.2410 0.2426 -0.0052 -0.0032 0.0122 140 ILE A CD1 1100 N N . GLN A 145 ? 0.2312 0.2620 0.2647 -0.0066 0.0032 0.0043 141 GLN A N 1101 C CA . GLN A 145 ? 0.2323 0.2636 0.2691 -0.0069 0.0056 0.0021 141 GLN A CA 1102 C C . GLN A 145 ? 0.2437 0.2710 0.2807 -0.0064 0.0073 0.0032 141 GLN A C 1103 O O . GLN A 145 ? 0.2496 0.2764 0.2891 -0.0064 0.0097 0.0018 141 GLN A O 1104 C CB . GLN A 145 ? 0.2391 0.2741 0.2771 -0.0077 0.0061 0.0009 141 GLN A CB 1105 C CG . GLN A 145 ? 0.2831 0.3227 0.3203 -0.0080 0.0043 0.0005 141 GLN A CG 1106 C CD . GLN A 145 ? 0.2879 0.3277 0.3220 -0.0081 0.0025 0.0031 141 GLN A CD 1107 O OE1 . GLN A 145 ? 0.2608 0.2972 0.2931 -0.0082 0.0021 0.0053 141 GLN A OE1 1108 N NE2 . GLN A 145 ? 0.2485 0.2926 0.2820 -0.0083 0.0015 0.0028 141 GLN A NE2 1109 N N . TYR A 146 ? 0.2332 0.2576 0.2676 -0.0057 0.0062 0.0055 142 TYR A N 1110 C CA . TYR A 146 ? 0.2353 0.2571 0.2694 -0.0049 0.0076 0.0068 142 TYR A CA 1111 C C . TYR A 146 ? 0.2364 0.2553 0.2683 -0.0041 0.0066 0.0084 142 TYR A C 1112 O O . TYR A 146 ? 0.2430 0.2619 0.2726 -0.0045 0.0044 0.0094 142 TYR A O 1113 C CB . TYR A 146 ? 0.2189 0.2425 0.2521 -0.0052 0.0070 0.0078 142 TYR A CB 1114 C CG . TYR A 146 ? 0.2393 0.2615 0.2716 -0.0041 0.0079 0.0093 142 TYR A CG 1115 C CD1 . TYR A 146 ? 0.2758 0.2952 0.3090 -0.0026 0.0102 0.0095 142 TYR A CD1 1116 C CD2 . TYR A 146 ? 0.2635 0.2878 0.2944 -0.0044 0.0068 0.0105 142 TYR A CD2 1117 C CE1 . TYR A 146 ? 0.2587 0.2775 0.2908 -0.0011 0.0110 0.0111 142 TYR A CE1 1118 C CE2 . TYR A 146 ? 0.2740 0.2982 0.3041 -0.0031 0.0075 0.0117 142 TYR A CE2 1119 C CZ . TYR A 146 ? 0.2635 0.2851 0.2941 -0.0013 0.0096 0.0121 142 TYR A CZ 1120 O OH . TYR A 146 ? 0.2494 0.2715 0.2789 0.0005 0.0103 0.0135 142 TYR A OH 1121 N N . ALA A 147 ? 0.2296 0.2461 0.2622 -0.0030 0.0083 0.0085 143 ALA A N 1122 C CA . ALA A 147 ? 0.2227 0.2367 0.2532 -0.0020 0.0075 0.0098 143 ALA A CA 1123 C C . ALA A 147 ? 0.2297 0.2426 0.2594 -0.0007 0.0085 0.0113 143 ALA A C 1124 O O . ALA A 147 ? 0.2375 0.2498 0.2687 0.0001 0.0109 0.0113 143 ALA A O 1125 C CB . ALA A 147 ? 0.2180 0.2306 0.2499 -0.0014 0.0086 0.0088 143 ALA A CB 1126 N N . PHE A 148 ? 0.2217 0.2342 0.2487 -0.0004 0.0067 0.0126 144 PHE A N 1127 C CA . PHE A 148 ? 0.2257 0.2381 0.2516 0.0012 0.0075 0.0139 144 PHE A CA 1128 C C . PHE A 148 ? 0.2332 0.2433 0.2590 0.0030 0.0089 0.0144 144 PHE A C 1129 O O . PHE A 148 ? 0.2435 0.2532 0.2673 0.0038 0.0078 0.0151 144 PHE A O 1130 C CB . PHE A 148 ? 0.2208 0.2346 0.2442 0.0006 0.0051 0.0147 144 PHE A CB 1131 C CG . PHE A 148 ? 0.2182 0.2345 0.2416 -0.0013 0.0038 0.0145 144 PHE A CG 1132 C CD1 . PHE A 148 ? 0.2664 0.2849 0.2912 -0.0012 0.0050 0.0144 144 PHE A CD1 1133 C CD2 . PHE A 148 ? 0.2450 0.2612 0.2668 -0.0031 0.0016 0.0145 144 PHE A CD2 1134 C CE1 . PHE A 148 ? 0.2894 0.3107 0.3141 -0.0029 0.0039 0.0143 144 PHE A CE1 1135 C CE2 . PHE A 148 ? 0.2525 0.2710 0.2742 -0.0049 0.0007 0.0145 144 PHE A CE2 1136 C CZ . PHE A 148 ? 0.2197 0.2411 0.2428 -0.0048 0.0017 0.0144 144 PHE A CZ 1137 N N . ALA A 149 ? 0.2371 0.2457 0.2651 0.0035 0.0114 0.0138 145 ALA A N 1138 C CA . ALA A 149 ? 0.2441 0.2505 0.2723 0.0050 0.0131 0.0143 145 ALA A CA 1139 C C . ALA A 149 ? 0.2438 0.2487 0.2744 0.0056 0.0168 0.0141 145 ALA A C 1140 O O . ALA A 149 ? 0.2434 0.2489 0.2761 0.0042 0.0176 0.0126 145 ALA A O 1141 C CB . ALA A 149 ? 0.2233 0.2290 0.2519 0.0041 0.0121 0.0130 145 ALA A CB 1142 N N . PRO A 150 ? 0.2504 0.2531 0.2808 0.0076 0.0193 0.0153 146 PRO A N 1143 C CA . PRO A 150 ? 0.2369 0.2388 0.2652 0.0094 0.0189 0.0166 146 PRO A CA 1144 C C . PRO A 150 ? 0.2610 0.2643 0.2866 0.0116 0.0182 0.0185 146 PRO A C 1145 O O . PRO A 150 ? 0.2603 0.2643 0.2858 0.0127 0.0196 0.0195 146 PRO A O 1146 C CB . PRO A 150 ? 0.2616 0.2607 0.2914 0.0105 0.0226 0.0170 146 PRO A CB 1147 C CG . PRO A 150 ? 0.2264 0.2242 0.2581 0.0105 0.0256 0.0169 146 PRO A CG 1148 C CD . PRO A 150 ? 0.2363 0.2366 0.2691 0.0079 0.0232 0.0150 146 PRO A CD 1149 N N . CYS A 151 ? 0.2493 0.2535 0.2727 0.0122 0.0161 0.0189 147 CYS A N 1150 C CA . CYS A 151 ? 0.2588 0.2647 0.2796 0.0148 0.0159 0.0205 147 CYS A CA 1151 C C . CYS A 151 ? 0.2722 0.2759 0.2930 0.0175 0.0194 0.0221 147 CYS A C 1152 O O . CYS A 151 ? 0.2498 0.2517 0.2709 0.0177 0.0201 0.0220 147 CYS A O 1153 C CB . CYS A 151 ? 0.2654 0.2726 0.2840 0.0145 0.0129 0.0200 147 CYS A CB 1154 S SG . CYS A 151 ? 0.2837 0.2944 0.2992 0.0177 0.0126 0.0215 147 CYS A SG 1155 N N . ILE A 152 ? 0.2626 0.2664 0.2831 0.0197 0.0218 0.0238 148 ILE A N 1156 C CA . ILE A 152 ? 0.2706 0.2722 0.2907 0.0228 0.0255 0.0258 148 ILE A CA 1157 C C . ILE A 152 ? 0.2818 0.2864 0.2986 0.0265 0.0252 0.0279 148 ILE A C 1158 O O . ILE A 152 ? 0.3051 0.3087 0.3208 0.0298 0.0283 0.0302 148 ILE A O 1159 C CB . ILE A 152 ? 0.2687 0.2669 0.2908 0.0230 0.0294 0.0263 148 ILE A CB 1160 C CG1 . ILE A 152 ? 0.2712 0.2714 0.2931 0.0234 0.0290 0.0265 148 ILE A CG1 1161 C CG2 . ILE A 152 ? 0.2622 0.2577 0.2879 0.0195 0.0302 0.0240 148 ILE A CG2 1162 C CD1 . ILE A 152 ? 0.2617 0.2578 0.2850 0.0247 0.0337 0.0275 148 ILE A CD1 1163 N N . ALA A 153 ? 0.2808 0.2891 0.2958 0.0260 0.0216 0.0270 149 ALA A N 1164 C CA . ALA A 153 ? 0.2821 0.2942 0.2941 0.0292 0.0209 0.0283 149 ALA A CA 1165 C C . ALA A 153 ? 0.2965 0.3064 0.3076 0.0319 0.0234 0.0299 149 ALA A C 1166 O O . ALA A 153 ? 0.2731 0.2796 0.2857 0.0302 0.0241 0.0291 149 ALA A O 1167 C CB . ALA A 153 ? 0.2840 0.2994 0.2949 0.0273 0.0167 0.0263 149 ALA A CB 1168 N N . VAL A 154 ? 0.2850 0.2973 0.2937 0.0361 0.0248 0.0321 150 VAL A N 1169 C CA . VAL A 154 ? 0.2946 0.3057 0.3019 0.0390 0.0270 0.0339 150 VAL A CA 1170 C C . VAL A 154 ? 0.3027 0.3195 0.3071 0.0405 0.0239 0.0332 150 VAL A C 1171 O O . VAL A 154 ? 0.3103 0.3319 0.3125 0.0434 0.0235 0.0342 150 VAL A O 1172 C CB . VAL A 154 ? 0.3065 0.3158 0.3126 0.0432 0.0315 0.0372 150 VAL A CB 1173 C CG1 . VAL A 154 ? 0.2933 0.3012 0.2978 0.0464 0.0342 0.0394 150 VAL A CG1 1174 C CG2 . VAL A 154 ? 0.2915 0.2953 0.3004 0.0415 0.0346 0.0374 150 VAL A CG2 1175 N N . CYS A 155 ? 0.3000 0.3167 0.3045 0.0383 0.0214 0.0311 151 CYS A N 1176 C CA . CYS A 155 ? 0.3072 0.3291 0.3095 0.0389 0.0181 0.0297 151 CYS A CA 1177 C C . CYS A 155 ? 0.3194 0.3438 0.3191 0.0435 0.0198 0.0318 151 CYS A C 1178 O O . CYS A 155 ? 0.3136 0.3348 0.3133 0.0445 0.0218 0.0327 151 CYS A O 1179 C CB . CYS A 155 ? 0.2996 0.3198 0.3027 0.0354 0.0154 0.0270 151 CYS A CB 1180 S SG . CYS A 155 ? 0.3199 0.3451 0.3202 0.0360 0.0119 0.0249 151 CYS A SG 1181 N N . ARG A 156 ? 0.3310 0.3615 0.3283 0.0464 0.0190 0.0323 152 ARG A N 1182 C CA . ARG A 156 ? 0.3443 0.3783 0.3386 0.0516 0.0207 0.0346 152 ARG A CA 1183 C C . ARG A 156 ? 0.3476 0.3872 0.3399 0.0522 0.0176 0.0323 152 ARG A C 1184 O O . ARG A 156 ? 0.3665 0.4101 0.3561 0.0565 0.0185 0.0338 152 ARG A O 1185 C CB . ARG A 156 ? 0.3381 0.3757 0.3310 0.0555 0.0225 0.0370 152 ARG A CB 1186 C CG . ARG A 156 ? 0.3403 0.3717 0.3350 0.0556 0.0263 0.0394 152 ARG A CG 1187 C CD . ARG A 156 ? 0.3729 0.3982 0.3676 0.0573 0.0305 0.0420 152 ARG A CD 1188 N NE . ARG A 156 ? 0.3888 0.4168 0.3801 0.0634 0.0332 0.0454 152 ARG A NE 1189 C CZ . ARG A 156 ? 0.3979 0.4218 0.3885 0.0661 0.0373 0.0484 152 ARG A CZ 1190 N NH1 . ARG A 156 ? 0.3834 0.4104 0.3703 0.0722 0.0397 0.0517 152 ARG A NH1 1191 N NH2 . ARG A 156 ? 0.4037 0.4205 0.3969 0.0631 0.0394 0.0481 152 ARG A NH2 1192 N N . ASP A 157 ? 0.3429 0.3827 0.3364 0.0478 0.0140 0.0288 153 ASP A N 1193 C CA . ASP A 157 ? 0.3427 0.3872 0.3346 0.0475 0.0109 0.0260 153 ASP A CA 1194 C C . ASP A 157 ? 0.3256 0.3658 0.3192 0.0424 0.0084 0.0229 153 ASP A C 1195 O O . ASP A 157 ? 0.3330 0.3726 0.3282 0.0388 0.0066 0.0213 153 ASP A O 1196 C CB . ASP A 157 ? 0.3201 0.3727 0.3108 0.0483 0.0089 0.0248 153 ASP A CB 1197 C CG . ASP A 157 ? 0.4012 0.4603 0.3897 0.0492 0.0064 0.0221 153 ASP A CG 1198 O OD1 . ASP A 157 ? 0.3531 0.4095 0.3419 0.0468 0.0048 0.0198 153 ASP A OD1 1199 O OD2 . ASP A 157 ? 0.3952 0.4625 0.3817 0.0526 0.0060 0.0222 153 ASP A OD2 1200 N N . PRO A 158 ? 0.3119 0.3494 0.3051 0.0423 0.0082 0.0222 154 PRO A N 1201 C CA . PRO A 158 ? 0.3083 0.3410 0.3029 0.0382 0.0063 0.0198 154 PRO A CA 1202 C C . PRO A 158 ? 0.3161 0.3515 0.3102 0.0354 0.0028 0.0163 154 PRO A C 1203 O O . PRO A 158 ? 0.3043 0.3356 0.2994 0.0320 0.0012 0.0144 154 PRO A O 1204 C CB . PRO A 158 ? 0.3018 0.3324 0.2956 0.0400 0.0073 0.0202 154 PRO A CB 1205 C CG . PRO A 158 ? 0.3127 0.3497 0.3037 0.0446 0.0080 0.0212 154 PRO A CG 1206 C CD . PRO A 158 ? 0.3190 0.3580 0.3101 0.0465 0.0100 0.0238 154 PRO A CD 1207 N N . ARG A 159 ? 0.3064 0.3488 0.2989 0.0369 0.0017 0.0154 155 ARG A N 1208 C CA . ARG A 159 ? 0.3137 0.3586 0.3063 0.0335 -0.0013 0.0118 155 ARG A CA 1209 C C . ARG A 159 ? 0.3072 0.3497 0.3019 0.0295 -0.0020 0.0115 155 ARG A C 1210 O O . ARG A 159 ? 0.3217 0.3640 0.3168 0.0259 -0.0042 0.0087 155 ARG A O 1211 C CB . ARG A 159 ? 0.3152 0.3692 0.3058 0.0358 -0.0024 0.0104 155 ARG A CB 1212 C CG . ARG A 159 ? 0.3048 0.3613 0.2932 0.0391 -0.0024 0.0099 155 ARG A CG 1213 C CD . ARG A 159 ? 0.3077 0.3745 0.2941 0.0425 -0.0030 0.0091 155 ARG A CD 1214 N NE . ARG A 159 ? 0.3240 0.3941 0.3097 0.0467 -0.0006 0.0129 155 ARG A NE 1215 C CZ . ARG A 159 ? 0.3948 0.4742 0.3787 0.0504 -0.0008 0.0129 155 ARG A CZ 1216 N NH1 . ARG A 159 ? 0.3687 0.4552 0.3514 0.0501 -0.0032 0.0091 155 ARG A NH1 1217 N NH2 . ARG A 159 ? 0.3492 0.4309 0.3322 0.0546 0.0017 0.0167 155 ARG A NH2 1218 N N . TRP A 160 ? 0.3121 0.3523 0.3082 0.0302 0.0001 0.0143 156 TRP A N 1219 C CA . TRP A 160 ? 0.3025 0.3404 0.3006 0.0267 -0.0003 0.0141 156 TRP A CA 1220 C C . TRP A 160 ? 0.2987 0.3297 0.2980 0.0230 -0.0013 0.0129 156 TRP A C 1221 O O . TRP A 160 ? 0.2902 0.3168 0.2898 0.0238 -0.0001 0.0138 156 TRP A O 1222 C CB . TRP A 160 ? 0.3055 0.3419 0.3047 0.0286 0.0025 0.0173 156 TRP A CB 1223 C CG . TRP A 160 ? 0.2993 0.3348 0.3006 0.0259 0.0023 0.0174 156 TRP A CG 1224 C CD1 . TRP A 160 ? 0.2825 0.3209 0.2841 0.0230 0.0003 0.0155 156 TRP A CD1 1225 C CD2 . TRP A 160 ? 0.2718 0.3033 0.2748 0.0260 0.0046 0.0195 156 TRP A CD2 1226 N NE1 . TRP A 160 ? 0.3193 0.3562 0.3227 0.0215 0.0010 0.0165 156 TRP A NE1 1227 C CE2 . TRP A 160 ? 0.3369 0.3695 0.3412 0.0233 0.0036 0.0188 156 TRP A CE2 1228 C CE3 . TRP A 160 ? 0.2668 0.2941 0.2706 0.0278 0.0075 0.0216 156 TRP A CE3 1229 C CZ2 . TRP A 160 ? 0.2960 0.3257 0.3022 0.0226 0.0053 0.0201 156 TRP A CZ2 1230 C CZ3 . TRP A 160 ? 0.2787 0.3030 0.2846 0.0269 0.0092 0.0227 156 TRP A CZ3 1231 C CH2 . TRP A 160 ? 0.2724 0.2980 0.2794 0.0244 0.0080 0.0219 156 TRP A CH2 1232 N N . GLY A 161 ? 0.2768 0.3071 0.2768 0.0192 -0.0031 0.0110 157 GLY A N 1233 C CA . GLY A 161 ? 0.2892 0.3132 0.2899 0.0160 -0.0039 0.0101 157 GLY A CA 1234 C C . GLY A 161 ? 0.2940 0.3137 0.2967 0.0155 -0.0024 0.0120 157 GLY A C 1235 O O . GLY A 161 ? 0.3025 0.3174 0.3056 0.0135 -0.0030 0.0115 157 GLY A O 1236 N N . ARG A 162 ? 0.2637 0.2851 0.2674 0.0175 -0.0004 0.0142 158 ARG A N 1237 C CA . ARG A 162 ? 0.2859 0.3034 0.2916 0.0171 0.0013 0.0156 158 ARG A CA 1238 C C . ARG A 162 ? 0.2860 0.3023 0.2919 0.0202 0.0039 0.0175 158 ARG A C 1239 O O . ARG A 162 ? 0.2816 0.2955 0.2893 0.0201 0.0058 0.0186 158 ARG A O 1240 C CB . ARG A 162 ? 0.2791 0.2985 0.2861 0.0162 0.0019 0.0165 158 ARG A CB 1241 C CG . ARG A 162 ? 0.2968 0.3184 0.3035 0.0132 -0.0005 0.0147 158 ARG A CG 1242 C CD . ARG A 162 ? 0.2961 0.3191 0.3044 0.0121 0.0001 0.0155 158 ARG A CD 1243 N NE . ARG A 162 ? 0.2959 0.3144 0.3058 0.0101 0.0005 0.0157 158 ARG A NE 1244 C CZ . ARG A 162 ? 0.3278 0.3467 0.3391 0.0083 0.0005 0.0158 158 ARG A CZ 1245 N NH1 . ARG A 162 ? 0.2556 0.2790 0.2668 0.0081 0.0002 0.0158 158 ARG A NH1 1246 N NH2 . ARG A 162 ? 0.2497 0.2651 0.2623 0.0067 0.0008 0.0158 158 ARG A NH2 1247 N N . CYS A 163 ? 0.2877 0.3056 0.2918 0.0227 0.0040 0.0175 159 CYS A N 1248 C CA . CYS A 163 ? 0.2979 0.3146 0.3021 0.0257 0.0069 0.0196 159 CYS A CA 1249 C C . CYS A 163 ? 0.2869 0.2986 0.2931 0.0244 0.0079 0.0196 159 CYS A C 1250 O O . CYS A 163 ? 0.2680 0.2781 0.2755 0.0256 0.0108 0.0212 159 CYS A O 1251 C CB . CYS A 163 ? 0.3094 0.3287 0.3112 0.0287 0.0067 0.0195 159 CYS A CB 1252 S SG . CYS A 163 ? 0.3713 0.3910 0.3726 0.0333 0.0108 0.0229 159 CYS A SG 1253 N N . TYR A 164 ? 0.2675 0.2770 0.2739 0.0218 0.0058 0.0177 160 TYR A N 1254 C CA . TYR A 164 ? 0.2512 0.2570 0.2594 0.0208 0.0067 0.0175 160 TYR A CA 1255 C C . TYR A 164 ? 0.2608 0.2655 0.2716 0.0191 0.0081 0.0180 160 TYR A C 1256 O O . TYR A 164 ? 0.2517 0.2544 0.2645 0.0185 0.0094 0.0179 160 TYR A O 1257 C CB . TYR A 164 ? 0.2611 0.2649 0.2686 0.0191 0.0043 0.0156 160 TYR A CB 1258 C CG . TYR A 164 ? 0.2823 0.2857 0.2896 0.0162 0.0020 0.0145 160 TYR A CG 1259 C CD1 . TYR A 164 ? 0.2533 0.2550 0.2624 0.0141 0.0020 0.0144 160 TYR A CD1 1260 C CD2 . TYR A 164 ? 0.2598 0.2646 0.2651 0.0156 0.0000 0.0134 160 TYR A CD2 1261 C CE1 . TYR A 164 ? 0.2702 0.2714 0.2790 0.0116 0.0002 0.0136 160 TYR A CE1 1262 C CE2 . TYR A 164 ? 0.2912 0.2953 0.2963 0.0127 -0.0018 0.0123 160 TYR A CE2 1263 C CZ . TYR A 164 ? 0.2884 0.2906 0.2952 0.0108 -0.0016 0.0127 160 TYR A CZ 1264 O OH . TYR A 164 ? 0.2742 0.2756 0.2807 0.0082 -0.0031 0.0120 160 TYR A OH 1265 N N . GLU A 165 ? 0.2404 0.2469 0.2513 0.0183 0.0076 0.0183 161 GLU A N 1266 C CA . GLU A 165 ? 0.2504 0.2560 0.2637 0.0169 0.0090 0.0187 161 GLU A CA 1267 C C . GLU A 165 ? 0.2637 0.2692 0.2779 0.0191 0.0124 0.0205 161 GLU A C 1268 O O . GLU A 165 ? 0.2689 0.2735 0.2853 0.0182 0.0141 0.0208 161 GLU A O 1269 C CB . GLU A 165 ? 0.2319 0.2393 0.2450 0.0151 0.0072 0.0181 161 GLU A CB 1270 C CG . GLU A 165 ? 0.2227 0.2292 0.2351 0.0125 0.0042 0.0165 161 GLU A CG 1271 C CD . GLU A 165 ? 0.2918 0.2995 0.3047 0.0102 0.0031 0.0161 161 GLU A CD 1272 O OE1 . GLU A 165 ? 0.2887 0.2984 0.3002 0.0094 0.0015 0.0156 161 GLU A OE1 1273 O OE2 . GLU A 165 ? 0.2838 0.2907 0.2987 0.0091 0.0040 0.0162 161 GLU A OE2 1274 N N . SER A 166 ? 0.2660 0.2722 0.2787 0.0220 0.0137 0.0218 162 SER A N 1275 C CA . SER A 166 ? 0.2728 0.2782 0.2859 0.0245 0.0174 0.0239 162 SER A CA 1276 C C . SER A 166 ? 0.2641 0.2668 0.2784 0.0250 0.0197 0.0243 162 SER A C 1277 O O . SER A 166 ? 0.2686 0.2717 0.2818 0.0257 0.0187 0.0238 162 SER A O 1278 C CB . SER A 166 ? 0.2856 0.2943 0.2960 0.0279 0.0176 0.0255 162 SER A CB 1279 O OG . SER A 166 ? 0.3078 0.3152 0.3181 0.0309 0.0215 0.0280 162 SER A OG 1280 N N . TYR A 167 ? 0.2669 0.2670 0.2836 0.0246 0.0230 0.0249 163 TYR A N 1281 C CA . TYR A 167 ? 0.2769 0.2746 0.2951 0.0247 0.0255 0.0249 163 TYR A CA 1282 C C . TYR A 167 ? 0.2885 0.2867 0.3044 0.0283 0.0273 0.0271 163 TYR A C 1283 O O . TYR A 167 ? 0.2927 0.2901 0.3090 0.0286 0.0282 0.0270 163 TYR A O 1284 C CB . TYR A 167 ? 0.2479 0.2426 0.2693 0.0234 0.0292 0.0250 163 TYR A CB 1285 C CG . TYR A 167 ? 0.2609 0.2555 0.2848 0.0201 0.0279 0.0228 163 TYR A CG 1286 C CD1 . TYR A 167 ? 0.2522 0.2472 0.2780 0.0175 0.0263 0.0204 163 TYR A CD1 1287 C CD2 . TYR A 167 ? 0.2679 0.2624 0.2922 0.0197 0.0283 0.0231 163 TYR A CD2 1288 C CE1 . TYR A 167 ? 0.2747 0.2703 0.3026 0.0147 0.0252 0.0184 163 TYR A CE1 1289 C CE2 . TYR A 167 ? 0.2849 0.2798 0.3115 0.0167 0.0271 0.0210 163 TYR A CE2 1290 C CZ . TYR A 167 ? 0.2756 0.2710 0.3038 0.0143 0.0255 0.0187 163 TYR A CZ 1291 O OH . TYR A 167 ? 0.2595 0.2559 0.2897 0.0117 0.0244 0.0168 163 TYR A OH 1292 N N . SER A 168 ? 0.2790 0.2789 0.2925 0.0311 0.0278 0.0291 164 SER A N 1293 C CA . SER A 168 ? 0.2926 0.2930 0.3038 0.0351 0.0302 0.0316 164 SER A CA 1294 C C . SER A 168 ? 0.3145 0.3179 0.3228 0.0386 0.0303 0.0336 164 SER A C 1295 O O . SER A 168 ? 0.3177 0.3217 0.3264 0.0382 0.0300 0.0337 164 SER A O 1296 C CB . SER A 168 ? 0.3034 0.2995 0.3166 0.0355 0.0352 0.0332 164 SER A CB 1297 O OG . SER A 168 ? 0.3054 0.3017 0.3163 0.0394 0.0379 0.0359 164 SER A OG 1298 N N . GLU A 169 ? 0.3137 0.3196 0.3192 0.0423 0.0308 0.0353 165 GLU A N 1299 C CA . GLU A 169 ? 0.3165 0.3258 0.3190 0.0464 0.0315 0.0376 165 GLU A CA 1300 C C . GLU A 169 ? 0.3297 0.3353 0.3324 0.0490 0.0368 0.0409 165 GLU A C 1301 O O . GLU A 169 ? 0.3357 0.3434 0.3363 0.0526 0.0380 0.0431 165 GLU A O 1302 C CB . GLU A 169 ? 0.3457 0.3596 0.3450 0.0498 0.0304 0.0381 165 GLU A CB 1303 C CG . GLU A 169 ? 0.3312 0.3427 0.3298 0.0524 0.0342 0.0406 165 GLU A CG 1304 C CD . GLU A 169 ? 0.3772 0.3930 0.3731 0.0549 0.0326 0.0403 165 GLU A CD 1305 O OE1 . GLU A 169 ? 0.3744 0.3932 0.3699 0.0530 0.0284 0.0373 165 GLU A OE1 1306 O OE2 . GLU A 169 ? 0.3883 0.4042 0.3824 0.0587 0.0357 0.0431 165 GLU A OE2 1307 N N . ASP A 170 ? 0.3140 0.3141 0.3193 0.0472 0.0399 0.0411 166 ASP A N 1308 C CA . ASP A 170 ? 0.3431 0.3384 0.3491 0.0489 0.0453 0.0439 166 ASP A CA 1309 C C . ASP A 170 ? 0.3332 0.3251 0.3423 0.0456 0.0460 0.0425 166 ASP A C 1310 O O . ASP A 170 ? 0.3284 0.3179 0.3408 0.0414 0.0456 0.0400 166 ASP A O 1311 C CB . ASP A 170 ? 0.3510 0.3426 0.3584 0.0483 0.0485 0.0444 166 ASP A CB 1312 C CG . ASP A 170 ? 0.4179 0.4038 0.4259 0.0500 0.0548 0.0475 166 ASP A CG 1313 O OD1 . ASP A 170 ? 0.4240 0.4078 0.4318 0.0511 0.0567 0.0488 166 ASP A OD1 1314 O OD2 . ASP A 170 ? 0.3871 0.3705 0.3955 0.0504 0.0579 0.0486 166 ASP A OD2 1315 N N . ARG A 171 ? 0.3269 0.3188 0.3349 0.0478 0.0473 0.0441 167 ARG A N 1316 C CA . ARG A 171 ? 0.3333 0.3221 0.3441 0.0451 0.0482 0.0429 167 ARG A CA 1317 C C . ARG A 171 ? 0.3427 0.3250 0.3571 0.0422 0.0522 0.0422 167 ARG A C 1318 O O . ARG A 171 ? 0.3384 0.3193 0.3559 0.0384 0.0516 0.0397 167 ARG A O 1319 C CB . ARG A 171 ? 0.3257 0.3152 0.3342 0.0490 0.0498 0.0454 167 ARG A CB 1320 C CG . ARG A 171 ? 0.3702 0.3562 0.3764 0.0539 0.0552 0.0496 167 ARG A CG 1321 C CD . ARG A 171 ? 0.4288 0.4072 0.4374 0.0530 0.0605 0.0504 167 ARG A CD 1322 N NE . ARG A 171 ? 0.4743 0.4486 0.4805 0.0577 0.0660 0.0547 167 ARG A NE 1323 C CZ . ARG A 171 ? 0.5344 0.5010 0.5420 0.0577 0.0718 0.0562 167 ARG A CZ 1324 N NH1 . ARG A 171 ? 0.5309 0.4937 0.5358 0.0623 0.0770 0.0605 167 ARG A NH1 1325 N NH2 . ARG A 171 ? 0.4469 0.4095 0.4585 0.0532 0.0727 0.0534 167 ARG A NH2 1326 N N . ARG A 172 ? 0.3439 0.3227 0.3580 0.0439 0.0564 0.0443 168 ARG A N 1327 C CA . ARG A 172 ? 0.3592 0.3324 0.3771 0.0407 0.0603 0.0432 168 ARG A CA 1328 C C . ARG A 172 ? 0.3410 0.3158 0.3623 0.0357 0.0571 0.0392 168 ARG A C 1329 O O . ARG A 172 ? 0.3250 0.2971 0.3500 0.0320 0.0586 0.0368 168 ARG A O 1330 C CB . ARG A 172 ? 0.3799 0.3490 0.3970 0.0431 0.0656 0.0463 168 ARG A CB 1331 C CG . ARG A 172 ? 0.4146 0.3820 0.4279 0.0488 0.0690 0.0508 168 ARG A CG 1332 C CD . ARG A 172 ? 0.5783 0.5438 0.5898 0.0517 0.0730 0.0539 168 ARG A CD 1333 N NE . ARG A 172 ? 0.6554 0.6200 0.6626 0.0579 0.0762 0.0587 168 ARG A NE 1334 C CZ . ARG A 172 ? 0.7249 0.6958 0.7279 0.0623 0.0732 0.0604 168 ARG A CZ 1335 N NH1 . ARG A 172 ? 0.6840 0.6618 0.6867 0.0608 0.0670 0.0576 168 ARG A NH1 1336 N NH2 . ARG A 172 ? 0.7120 0.6823 0.7110 0.0683 0.0766 0.0649 168 ARG A NH2 1337 N N . ILE A 173 ? 0.3185 0.2979 0.3384 0.0357 0.0530 0.0383 169 ILE A N 1338 C CA . ILE A 173 ? 0.3111 0.2921 0.3336 0.0315 0.0499 0.0346 169 ILE A CA 1339 C C . ILE A 173 ? 0.3014 0.2842 0.3253 0.0288 0.0464 0.0321 169 ILE A C 1340 O O . ILE A 173 ? 0.3081 0.2902 0.3354 0.0250 0.0461 0.0293 169 ILE A O 1341 C CB . ILE A 173 ? 0.3025 0.2874 0.3230 0.0326 0.0466 0.0344 169 ILE A CB 1342 C CG1 . ILE A 173 ? 0.3140 0.2969 0.3339 0.0348 0.0508 0.0367 169 ILE A CG1 1343 C CG2 . ILE A 173 ? 0.2843 0.2711 0.3071 0.0286 0.0429 0.0307 169 ILE A CG2 1344 C CD1 . ILE A 173 ? 0.3002 0.2869 0.3173 0.0369 0.0482 0.0371 169 ILE A CD1 1345 N N . VAL A 174 ? 0.2997 0.2852 0.3209 0.0307 0.0439 0.0330 170 VAL A N 1346 C CA . VAL A 174 ? 0.2844 0.2717 0.3065 0.0284 0.0408 0.0310 170 VAL A CA 1347 C C . VAL A 174 ? 0.3096 0.2931 0.3347 0.0265 0.0441 0.0302 170 VAL A C 1348 O O . VAL A 174 ? 0.2915 0.2755 0.3193 0.0230 0.0426 0.0275 170 VAL A O 1349 C CB . VAL A 174 ? 0.2973 0.2883 0.3161 0.0311 0.0384 0.0324 170 VAL A CB 1350 C CG1 . VAL A 174 ? 0.2557 0.2485 0.2756 0.0287 0.0358 0.0306 170 VAL A CG1 1351 C CG2 . VAL A 174 ? 0.2673 0.2624 0.2834 0.0323 0.0348 0.0323 170 VAL A CG2 1352 N N . GLN A 175 ? 0.2992 0.2790 0.3239 0.0291 0.0487 0.0327 171 GLN A N 1353 C CA . GLN A 175 ? 0.3140 0.2894 0.3417 0.0273 0.0524 0.0319 171 GLN A CA 1354 C C . GLN A 175 ? 0.3149 0.2888 0.3468 0.0230 0.0535 0.0288 171 GLN A C 1355 O O . GLN A 175 ? 0.3257 0.2991 0.3606 0.0198 0.0534 0.0260 171 GLN A O 1356 C CB . GLN A 175 ? 0.3116 0.2819 0.3381 0.0308 0.0582 0.0353 171 GLN A CB 1357 C CG . GLN A 175 ? 0.3416 0.3131 0.3645 0.0352 0.0581 0.0382 171 GLN A CG 1358 C CD . GLN A 175 ? 0.3835 0.3497 0.4048 0.0391 0.0640 0.0419 171 GLN A CD 1359 O OE1 . GLN A 175 ? 0.3984 0.3603 0.4205 0.0396 0.0674 0.0423 171 GLN A OE1 1360 N NE2 . GLN A 175 ? 0.2984 0.2648 0.3172 0.0422 0.0653 0.0446 171 GLN A NE2 1361 N N . SER A 176 ? 0.3026 0.2758 0.3348 0.0230 0.0548 0.0291 172 SER A N 1362 C CA . SER A 176 ? 0.3205 0.2932 0.3567 0.0191 0.0558 0.0261 172 SER A CA 1363 C C . SER A 176 ? 0.3016 0.2788 0.3393 0.0159 0.0508 0.0225 172 SER A C 1364 O O . SER A 176 ? 0.3050 0.2824 0.3465 0.0124 0.0514 0.0194 172 SER A O 1365 C CB . SER A 176 ? 0.3369 0.3091 0.3731 0.0197 0.0576 0.0270 172 SER A CB 1366 O OG . SER A 176 ? 0.3622 0.3390 0.3963 0.0206 0.0530 0.0269 172 SER A OG 1367 N N . MET A 177 ? 0.3032 0.2842 0.3381 0.0171 0.0461 0.0230 173 MET A N 1368 C CA . MET A 177 ? 0.2980 0.2829 0.3339 0.0145 0.0415 0.0201 173 MET A CA 1369 C C . MET A 177 ? 0.3016 0.2877 0.3382 0.0130 0.0398 0.0187 173 MET A C 1370 O O . MET A 177 ? 0.2813 0.2704 0.3185 0.0109 0.0362 0.0166 173 MET A O 1371 C CB . MET A 177 ? 0.3019 0.2898 0.3344 0.0161 0.0374 0.0210 173 MET A CB 1372 C CG . MET A 177 ? 0.3024 0.2896 0.3340 0.0179 0.0391 0.0223 173 MET A CG 1373 S SD A MET A 177 ? 0.2655 0.2530 0.3015 0.0144 0.0404 0.0191 173 MET A SD 1374 S SD B MET A 177 ? 0.3446 0.3342 0.3768 0.0167 0.0367 0.0204 173 MET A SD 1375 C CE A MET A 177 ? 0.2810 0.2690 0.3159 0.0161 0.0411 0.0202 173 MET A CE 1376 C CE B MET A 177 ? 0.3562 0.3431 0.3897 0.0176 0.0420 0.0217 173 MET A CE 1377 N N . THR A 178 ? 0.2858 0.2692 0.3223 0.0141 0.0425 0.0200 174 THR A N 1378 C CA . THR A 178 ? 0.3050 0.2892 0.3428 0.0125 0.0417 0.0184 174 THR A CA 1379 C C . THR A 178 ? 0.3006 0.2851 0.3426 0.0087 0.0425 0.0148 174 THR A C 1380 O O . THR A 178 ? 0.2911 0.2770 0.3343 0.0071 0.0414 0.0130 174 THR A O 1381 C CB . THR A 178 ? 0.2998 0.2810 0.3366 0.0147 0.0448 0.0205 174 THR A CB 1382 O OG1 . THR A 178 ? 0.3033 0.2795 0.3416 0.0152 0.0502 0.0213 174 THR A OG1 1383 C CG2 . THR A 178 ? 0.2844 0.2672 0.3170 0.0185 0.0432 0.0237 174 THR A CG2 1384 N N . GLU A 179 ? 0.2849 0.2687 0.3292 0.0073 0.0443 0.0135 175 GLU A N 1385 C CA . GLU A 179 ? 0.2673 0.2530 0.3155 0.0037 0.0444 0.0096 175 GLU A CA 1386 C C . GLU A 179 ? 0.2739 0.2647 0.3217 0.0024 0.0393 0.0078 175 GLU A C 1387 O O . GLU A 179 ? 0.2807 0.2741 0.3315 -0.0003 0.0389 0.0046 175 GLU A O 1388 C CB . GLU A 179 ? 0.2705 0.2557 0.3206 0.0028 0.0466 0.0089 175 GLU A CB 1389 C CG . GLU A 179 ? 0.2906 0.2704 0.3426 0.0028 0.0528 0.0097 175 GLU A CG 1390 C CD . GLU A 179 ? 0.3761 0.3545 0.4319 0.0000 0.0555 0.0067 175 GLU A CD 1391 O OE1 . GLU A 179 ? 0.3805 0.3559 0.4351 0.0013 0.0568 0.0081 175 GLU A OE1 1392 O OE2 . GLU A 179 ? 0.3670 0.3479 0.4266 -0.0034 0.0559 0.0028 175 GLU A OE2 1393 N N . LEU A 180 ? 0.2414 0.2337 0.2856 0.0042 0.0357 0.0097 176 LEU A N 1394 C CA . LEU A 180 ? 0.2527 0.2491 0.2962 0.0031 0.0312 0.0084 176 LEU A CA 1395 C C . LEU A 180 ? 0.2485 0.2461 0.2936 0.0015 0.0311 0.0068 176 LEU A C 1396 O O . LEU A 180 ? 0.2427 0.2437 0.2890 -0.0004 0.0289 0.0044 176 LEU A O 1397 C CB . LEU A 180 ? 0.2461 0.2432 0.2854 0.0052 0.0278 0.0107 176 LEU A CB 1398 C CG . LEU A 180 ? 0.2591 0.2596 0.2975 0.0039 0.0235 0.0095 176 LEU A CG 1399 C CD1 . LEU A 180 ? 0.2534 0.2551 0.2918 0.0038 0.0221 0.0086 176 LEU A CD1 1400 C CD2 . LEU A 180 ? 0.2231 0.2240 0.2580 0.0052 0.0207 0.0114 176 LEU A CD2 1401 N N . ILE A 181 ? 0.2490 0.2439 0.2936 0.0027 0.0334 0.0082 177 ILE A N 1402 C CA . ILE A 181 ? 0.2529 0.2487 0.2983 0.0017 0.0331 0.0071 177 ILE A CA 1403 C C . ILE A 181 ? 0.2609 0.2581 0.3104 -0.0012 0.0346 0.0033 177 ILE A C 1404 O O . ILE A 181 ? 0.2733 0.2743 0.3233 -0.0026 0.0320 0.0015 177 ILE A O 1405 C CB . ILE A 181 ? 0.2457 0.2384 0.2897 0.0040 0.0356 0.0095 177 ILE A CB 1406 C CG1 . ILE A 181 ? 0.2548 0.2487 0.2948 0.0065 0.0328 0.0125 177 ILE A CG1 1407 C CG2 . ILE A 181 ? 0.2736 0.2668 0.3191 0.0029 0.0363 0.0079 177 ILE A CG2 1408 C CD1 . ILE A 181 ? 0.2582 0.2493 0.2961 0.0098 0.0355 0.0155 177 ILE A CD1 1409 N N . PRO A 182 ? 0.2739 0.2682 0.3264 -0.0022 0.0388 0.0020 178 PRO A N 1410 C CA . PRO A 182 ? 0.2678 0.2644 0.3244 -0.0053 0.0399 -0.0022 178 PRO A CA 1411 C C . PRO A 182 ? 0.2617 0.2634 0.3194 -0.0068 0.0371 -0.0043 178 PRO A C 1412 O O . PRO A 182 ? 0.2835 0.2890 0.3441 -0.0091 0.0369 -0.0080 178 PRO A O 1413 C CB . PRO A 182 ? 0.3026 0.2943 0.3620 -0.0060 0.0455 -0.0028 178 PRO A CB 1414 C CG . PRO A 182 ? 0.2815 0.2699 0.3382 -0.0034 0.0464 0.0009 178 PRO A CG 1415 C CD . PRO A 182 ? 0.2635 0.2526 0.3159 -0.0007 0.0431 0.0041 178 PRO A CD 1416 N N . GLY A 183 ? 0.2589 0.2611 0.3140 -0.0053 0.0349 -0.0023 179 GLY A N 1417 C CA . GLY A 183 ? 0.2595 0.2667 0.3149 -0.0061 0.0317 -0.0041 179 GLY A CA 1418 C C . GLY A 183 ? 0.2499 0.2606 0.3036 -0.0061 0.0278 -0.0043 179 GLY A C 1419 O O . GLY A 183 ? 0.2606 0.2759 0.3160 -0.0076 0.0264 -0.0070 179 GLY A O 1420 N N . LEU A 184 ? 0.2353 0.2441 0.2856 -0.0045 0.0262 -0.0014 180 LEU A N 1421 C CA . LEU A 184 ? 0.2329 0.2446 0.2813 -0.0045 0.0227 -0.0011 180 LEU A CA 1422 C C . LEU A 184 ? 0.2464 0.2602 0.2972 -0.0061 0.0236 -0.0035 180 LEU A C 1423 O O . LEU A 184 ? 0.2368 0.2549 0.2877 -0.0070 0.0213 -0.0050 180 LEU A O 1424 C CB . LEU A 184 ? 0.2226 0.2322 0.2673 -0.0027 0.0212 0.0022 180 LEU A CB 1425 C CG . LEU A 184 ? 0.2427 0.2510 0.2844 -0.0011 0.0193 0.0044 180 LEU A CG 1426 C CD1 . LEU A 184 ? 0.2205 0.2268 0.2593 0.0006 0.0189 0.0072 180 LEU A CD1 1427 C CD2 . LEU A 184 ? 0.1945 0.2058 0.2347 -0.0016 0.0156 0.0039 180 LEU A CD2 1428 N N . GLN A 185 ? 0.2331 0.2437 0.2854 -0.0062 0.0270 -0.0036 181 GLN A N 1429 C CA . GLN A 185 ? 0.2479 0.2597 0.3020 -0.0073 0.0281 -0.0054 181 GLN A CA 1430 C C . GLN A 185 ? 0.2609 0.2741 0.3195 -0.0097 0.0308 -0.0096 181 GLN A C 1431 O O . GLN A 185 ? 0.2555 0.2714 0.3158 -0.0110 0.0309 -0.0121 181 GLN A O 1432 C CB . GLN A 185 ? 0.2487 0.2559 0.3017 -0.0058 0.0305 -0.0032 181 GLN A CB 1433 C CG . GLN A 185 ? 0.2476 0.2545 0.2964 -0.0036 0.0278 0.0005 181 GLN A CG 1434 C CD . GLN A 185 ? 0.2899 0.2940 0.3376 -0.0018 0.0298 0.0023 181 GLN A CD 1435 O OE1 . GLN A 185 ? 0.3149 0.3150 0.3640 -0.0012 0.0338 0.0024 181 GLN A OE1 1436 N NE2 . GLN A 185 ? 0.2076 0.2140 0.2530 -0.0010 0.0273 0.0038 181 GLN A NE2 1437 N N . GLY A 186 ? 0.2653 0.2770 0.3259 -0.0104 0.0331 -0.0106 182 GLY A N 1438 C CA . GLY A 186 ? 0.2768 0.2885 0.3420 -0.0128 0.0368 -0.0145 182 GLY A CA 1439 C C . GLY A 186 ? 0.3040 0.3086 0.3699 -0.0124 0.0416 -0.0132 182 GLY A C 1440 O O . GLY A 186 ? 0.2922 0.2930 0.3553 -0.0101 0.0419 -0.0099 182 GLY A O 1441 N N . ASP A 187 ? 0.3040 0.3071 0.3738 -0.0145 0.0455 -0.0160 183 ASP A N 1442 C CA . ASP A 187 ? 0.3271 0.3230 0.3979 -0.0144 0.0508 -0.0151 183 ASP A CA 1443 C C . ASP A 187 ? 0.3243 0.3180 0.3958 -0.0146 0.0526 -0.0162 183 ASP A C 1444 O O . ASP A 187 ? 0.3235 0.3219 0.3971 -0.0165 0.0514 -0.0199 183 ASP A O 1445 C CB . ASP A 187 ? 0.3463 0.3416 0.4217 -0.0173 0.0548 -0.0186 183 ASP A CB 1446 C CG . ASP A 187 ? 0.3540 0.3499 0.4286 -0.0167 0.0541 -0.0169 183 ASP A CG 1447 O OD1 . ASP A 187 ? 0.4046 0.3967 0.4758 -0.0139 0.0541 -0.0126 183 ASP A OD1 1448 O OD2 . ASP A 187 ? 0.4790 0.4794 0.5566 -0.0190 0.0540 -0.0201 183 ASP A OD2 1449 N N . VAL A 188 ? 0.3439 0.3310 0.4136 -0.0123 0.0556 -0.0131 184 VAL A N 1450 C CA . VAL A 188 ? 0.3745 0.3591 0.4445 -0.0120 0.0575 -0.0139 184 VAL A CA 1451 C C . VAL A 188 ? 0.4085 0.3899 0.4832 -0.0152 0.0627 -0.0181 184 VAL A C 1452 O O . VAL A 188 ? 0.4082 0.3874 0.4851 -0.0167 0.0656 -0.0190 184 VAL A O 1453 C CB . VAL A 188 ? 0.3799 0.3589 0.4458 -0.0080 0.0588 -0.0089 184 VAL A CB 1454 C CG1 . VAL A 188 ? 0.3673 0.3504 0.4290 -0.0055 0.0535 -0.0054 184 VAL A CG1 1455 C CG2 . VAL A 188 ? 0.3870 0.3583 0.4527 -0.0067 0.0640 -0.0064 184 VAL A CG2 1456 N N . PRO A 189 ? 0.4438 0.4254 0.5202 -0.0163 0.0638 -0.0210 185 PRO A N 1457 C CA . PRO A 189 ? 0.4928 0.4717 0.5741 -0.0198 0.0687 -0.0257 185 PRO A CA 1458 C C . PRO A 189 ? 0.5293 0.4977 0.6106 -0.0188 0.0752 -0.0236 185 PRO A C 1459 O O . PRO A 189 ? 0.5156 0.4794 0.5930 -0.0149 0.0758 -0.0184 185 PRO A O 1460 C CB . PRO A 189 ? 0.4939 0.4769 0.5768 -0.0212 0.0675 -0.0297 185 PRO A CB 1461 C CG . PRO A 189 ? 0.4782 0.4609 0.5567 -0.0175 0.0649 -0.0257 185 PRO A CG 1462 C CD . PRO A 189 ? 0.4390 0.4239 0.5137 -0.0151 0.0608 -0.0211 185 PRO A CD 1463 N N . LYS A 190 ? 0.5822 0.5473 0.6681 -0.0222 0.0803 -0.0277 186 LYS A N 1464 C CA . LYS A 190 ? 0.6186 0.5733 0.7048 -0.0216 0.0870 -0.0256 186 LYS A CA 1465 C C . LYS A 190 ? 0.6280 0.5749 0.7102 -0.0172 0.0894 -0.0211 186 LYS A C 1466 O O . LYS A 190 ? 0.6478 0.5879 0.7275 -0.0143 0.0926 -0.0165 186 LYS A O 1467 C CB . LYS A 190 ? 0.6459 0.5978 0.7379 -0.0265 0.0924 -0.0315 186 LYS A CB 1468 C CG . LYS A 190 ? 0.7018 0.6610 0.7976 -0.0300 0.0903 -0.0381 186 LYS A CG 1469 C CD . LYS A 190 ? 0.7708 0.7388 0.8707 -0.0342 0.0882 -0.0429 186 LYS A CD 1470 C CE . LYS A 190 ? 0.7956 0.7747 0.8964 -0.0354 0.0825 -0.0468 186 LYS A CE 1471 N NZ . LYS A 190 ? 0.7695 0.7540 0.8654 -0.0316 0.0759 -0.0423 186 LYS A NZ 1472 N N . ASP A 191 ? 0.6168 0.5651 0.6983 -0.0164 0.0880 -0.0223 187 ASP A N 1473 C CA . ASP A 191 ? 0.6438 0.5845 0.7225 -0.0126 0.0914 -0.0191 187 ASP A CA 1474 C C . ASP A 191 ? 0.6115 0.5559 0.6850 -0.0080 0.0864 -0.0144 187 ASP A C 1475 O O . ASP A 191 ? 0.6276 0.5701 0.6991 -0.0054 0.0869 -0.0133 187 ASP A O 1476 C CB . ASP A 191 ? 0.6642 0.6042 0.7460 -0.0150 0.0935 -0.0242 187 ASP A CB 1477 C CG . ASP A 191 ? 0.7213 0.6716 0.8035 -0.0161 0.0873 -0.0272 187 ASP A CG 1478 O OD1 . ASP A 191 ? 0.7818 0.7400 0.8643 -0.0175 0.0825 -0.0277 187 ASP A OD1 1479 O OD2 . ASP A 191 ? 0.7983 0.7489 0.8802 -0.0153 0.0872 -0.0287 187 ASP A OD2 1480 N N . PHE A 192 ? 0.5734 0.5234 0.6448 -0.0072 0.0816 -0.0121 188 PHE A N 1481 C CA . PHE A 192 ? 0.5096 0.4652 0.5770 -0.0042 0.0761 -0.0091 188 PHE A CA 1482 C C . PHE A 192 ? 0.4941 0.4450 0.5570 0.0011 0.0776 -0.0037 188 PHE A C 1483 O O . PHE A 192 ? 0.4974 0.4428 0.5587 0.0032 0.0807 -0.0003 188 PHE A O 1484 C CB . PHE A 192 ? 0.5027 0.4641 0.5692 -0.0047 0.0715 -0.0079 188 PHE A CB 1485 C CG . PHE A 192 ? 0.4550 0.4228 0.5180 -0.0026 0.0656 -0.0057 188 PHE A CG 1486 C CD1 . PHE A 192 ? 0.4643 0.4385 0.5284 -0.0044 0.0620 -0.0087 188 PHE A CD1 1487 C CD2 . PHE A 192 ? 0.4333 0.4008 0.4920 0.0011 0.0639 -0.0007 188 PHE A CD2 1488 C CE1 . PHE A 192 ? 0.4355 0.4154 0.4965 -0.0029 0.0568 -0.0067 188 PHE A CE1 1489 C CE2 . PHE A 192 ? 0.3761 0.3495 0.4319 0.0026 0.0586 0.0010 188 PHE A CE2 1490 C CZ . PHE A 192 ? 0.3936 0.3729 0.4506 0.0005 0.0552 -0.0020 188 PHE A CZ 1491 N N . THR A 193 ? 0.4537 0.4073 0.5143 0.0034 0.0752 -0.0027 189 THR A N 1492 C CA . THR A 193 ? 0.4481 0.3987 0.5041 0.0088 0.0760 0.0026 189 THR A CA 1493 C C . THR A 193 ? 0.4305 0.3861 0.4828 0.0113 0.0714 0.0065 189 THR A C 1494 O O . THR A 193 ? 0.4011 0.3642 0.4528 0.0103 0.0660 0.0058 189 THR A O 1495 C CB . THR A 193 ? 0.4531 0.4050 0.5081 0.0107 0.0756 0.0022 189 THR A CB 1496 O OG1 . THR A 193 ? 0.4724 0.4190 0.5306 0.0086 0.0802 -0.0015 189 THR A OG1 1497 C CG2 . THR A 193 ? 0.4490 0.3986 0.4992 0.0165 0.0765 0.0075 189 THR A CG2 1498 N N . SER A 194 ? 0.4122 0.3637 0.4619 0.0144 0.0737 0.0107 190 SER A N 1499 C CA . SER A 194 ? 0.4061 0.3622 0.4524 0.0168 0.0696 0.0141 190 SER A CA 1500 C C . SER A 194 ? 0.4042 0.3667 0.4478 0.0189 0.0652 0.0153 190 SER A C 1501 O O . SER A 194 ? 0.3831 0.3440 0.4254 0.0217 0.0670 0.0164 190 SER A O 1502 C CB . SER A 194 ? 0.4151 0.3660 0.4583 0.0211 0.0732 0.0188 190 SER A CB 1503 O OG . SER A 194 ? 0.3973 0.3533 0.4374 0.0232 0.0692 0.0216 190 SER A OG 1504 N N . GLY A 195 ? 0.3658 0.3352 0.4086 0.0176 0.0597 0.0151 191 GLY A N 1505 C CA . GLY A 195 ? 0.3571 0.3328 0.3975 0.0191 0.0554 0.0161 191 GLY A CA 1506 C C . GLY A 195 ? 0.3453 0.3260 0.3879 0.0156 0.0523 0.0125 191 GLY A C 1507 O O . GLY A 195 ? 0.3289 0.3154 0.3699 0.0158 0.0481 0.0129 191 GLY A O 1508 N N . MET A 196 ? 0.3401 0.3186 0.3864 0.0124 0.0543 0.0087 192 MET A N 1509 C CA . MET A 196 ? 0.3418 0.3257 0.3902 0.0090 0.0511 0.0051 192 MET A CA 1510 C C . MET A 196 ? 0.3143 0.3030 0.3630 0.0064 0.0468 0.0043 192 MET A C 1511 O O . MET A 196 ? 0.3446 0.3312 0.3936 0.0060 0.0475 0.0049 192 MET A O 1512 C CB . MET A 196 ? 0.3237 0.3046 0.3760 0.0063 0.0546 0.0009 192 MET A CB 1513 C CG . MET A 196 ? 0.3578 0.3344 0.4098 0.0088 0.0584 0.0012 192 MET A CG 1514 S SD . MET A 196 ? 0.4193 0.4027 0.4696 0.0100 0.0547 0.0012 192 MET A SD 1515 C CE . MET A 196 ? 0.3627 0.3503 0.4172 0.0052 0.0534 -0.0046 192 MET A CE 1516 N N . PRO A 197 ? 0.3106 0.3054 0.3592 0.0048 0.0427 0.0029 193 PRO A N 1517 C CA . PRO A 197 ? 0.2950 0.2940 0.3435 0.0028 0.0388 0.0024 193 PRO A CA 1518 C C . PRO A 197 ? 0.3074 0.3069 0.3596 -0.0006 0.0396 -0.0016 193 PRO A C 1519 O O . PRO A 197 ? 0.3002 0.2988 0.3549 -0.0017 0.0420 -0.0044 193 PRO A O 1520 C CB . PRO A 197 ? 0.2768 0.2817 0.3235 0.0027 0.0347 0.0029 193 PRO A CB 1521 C CG . PRO A 197 ? 0.3067 0.3116 0.3546 0.0031 0.0367 0.0013 193 PRO A CG 1522 C CD . PRO A 197 ? 0.2861 0.2845 0.3337 0.0057 0.0413 0.0029 193 PRO A CD 1523 N N . PHE A 198 ? 0.2770 0.2783 0.3298 -0.0022 0.0378 -0.0023 194 PHE A N 1524 C CA . PHE A 198 ? 0.3004 0.3034 0.3568 -0.0052 0.0383 -0.0063 194 PHE A CA 1525 C C . PHE A 198 ? 0.2982 0.3058 0.3539 -0.0064 0.0343 -0.0065 194 PHE A C 1526 O O . PHE A 198 ? 0.2932 0.2997 0.3466 -0.0051 0.0330 -0.0038 194 PHE A O 1527 C CB . PHE A 198 ? 0.2988 0.2966 0.3575 -0.0059 0.0426 -0.0072 194 PHE A CB 1528 C CG . PHE A 198 ? 0.3311 0.3315 0.3938 -0.0092 0.0433 -0.0117 194 PHE A CG 1529 C CD1 . PHE A 198 ? 0.3514 0.3525 0.4173 -0.0112 0.0454 -0.0157 194 PHE A CD1 1530 C CD2 . PHE A 198 ? 0.3246 0.3274 0.3879 -0.0103 0.0417 -0.0123 194 PHE A CD2 1531 C CE1 . PHE A 198 ? 0.3901 0.3948 0.4600 -0.0143 0.0458 -0.0204 194 PHE A CE1 1532 C CE2 . PHE A 198 ? 0.3206 0.3269 0.3878 -0.0133 0.0422 -0.0168 194 PHE A CE2 1533 C CZ . PHE A 198 ? 0.3267 0.3344 0.3973 -0.0154 0.0442 -0.0209 194 PHE A CZ 1534 N N . VAL A 199 ? 0.2849 0.2976 0.3425 -0.0085 0.0326 -0.0097 195 VAL A N 1535 C CA . VAL A 199 ? 0.2741 0.2909 0.3315 -0.0095 0.0296 -0.0105 195 VAL A CA 1536 C C . VAL A 199 ? 0.2871 0.3078 0.3485 -0.0120 0.0305 -0.0153 195 VAL A C 1537 O O . VAL A 199 ? 0.2602 0.2829 0.3228 -0.0128 0.0310 -0.0175 195 VAL A O 1538 C CB . VAL A 199 ? 0.2831 0.3039 0.3374 -0.0088 0.0251 -0.0086 195 VAL A CB 1539 C CG1 . VAL A 199 ? 0.2241 0.2487 0.2782 -0.0096 0.0224 -0.0094 195 VAL A CG1 1540 C CG2 . VAL A 199 ? 0.2564 0.2741 0.3069 -0.0066 0.0242 -0.0043 195 VAL A CG2 1541 N N . ALA A 200 ? 0.2897 0.3120 0.3529 -0.0133 0.0307 -0.0172 196 ALA A N 1542 C CA . ALA A 200 ? 0.3090 0.3352 0.3766 -0.0158 0.0322 -0.0222 196 ALA A CA 1543 C C . ALA A 200 ? 0.3279 0.3616 0.3956 -0.0164 0.0292 -0.0245 196 ALA A C 1544 O O . ALA A 200 ? 0.3406 0.3775 0.4115 -0.0183 0.0306 -0.0288 196 ALA A O 1545 C CB . ALA A 200 ? 0.3156 0.3422 0.3855 -0.0170 0.0335 -0.0240 196 ALA A CB 1546 N N . GLY A 201 ? 0.3160 0.3525 0.3802 -0.0150 0.0252 -0.0219 197 GLY A N 1547 C CA . GLY A 201 ? 0.3114 0.3554 0.3754 -0.0153 0.0223 -0.0237 197 GLY A CA 1548 C C . GLY A 201 ? 0.3164 0.3621 0.3766 -0.0137 0.0185 -0.0206 197 GLY A C 1549 O O . GLY A 201 ? 0.2908 0.3318 0.3484 -0.0124 0.0179 -0.0169 197 GLY A O 1550 N N . LYS A 202 ? 0.3071 0.3597 0.3673 -0.0137 0.0162 -0.0222 198 LYS A N 1551 C CA . LYS A 202 ? 0.2906 0.3448 0.3468 -0.0119 0.0127 -0.0191 198 LYS A CA 1552 C C . LYS A 202 ? 0.3024 0.3549 0.3573 -0.0110 0.0118 -0.0176 198 LYS A C 1553 O O . LYS A 202 ? 0.3194 0.3714 0.3706 -0.0094 0.0093 -0.0145 198 LYS A O 1554 C CB . LYS A 202 ? 0.2964 0.3585 0.3525 -0.0118 0.0108 -0.0211 198 LYS A CB 1555 C CG . LYS A 202 ? 0.2791 0.3474 0.3385 -0.0125 0.0112 -0.0254 198 LYS A CG 1556 C CD . LYS A 202 ? 0.3247 0.4018 0.3843 -0.0122 0.0095 -0.0277 198 LYS A CD 1557 C CE . LYS A 202 ? 0.4222 0.5058 0.4844 -0.0123 0.0095 -0.0314 198 LYS A CE 1558 N NZ . LYS A 202 ? 0.4828 0.5756 0.5447 -0.0115 0.0077 -0.0335 198 LYS A NZ 1559 N N . ASN A 203 ? 0.2791 0.3305 0.3369 -0.0119 0.0141 -0.0197 199 ASN A N 1560 C CA . ASN A 203 ? 0.2865 0.3365 0.3434 -0.0109 0.0135 -0.0185 199 ASN A CA 1561 C C . ASN A 203 ? 0.2750 0.3174 0.3308 -0.0105 0.0150 -0.0156 199 ASN A C 1562 O O . ASN A 203 ? 0.2619 0.3023 0.3168 -0.0096 0.0148 -0.0144 199 ASN A O 1563 C CB . ASN A 203 ? 0.3092 0.3642 0.3701 -0.0121 0.0148 -0.0227 199 ASN A CB 1564 C CG . ASN A 203 ? 0.3800 0.4439 0.4418 -0.0122 0.0131 -0.0258 199 ASN A CG 1565 O OD1 . ASN A 203 ? 0.5071 0.5756 0.5730 -0.0141 0.0148 -0.0302 199 ASN A OD1 1566 N ND2 . ASN A 203 ? 0.3320 0.3983 0.3902 -0.0101 0.0100 -0.0235 199 ASN A ND2 1567 N N . LYS A 204 ? 0.2631 0.3016 0.3186 -0.0107 0.0163 -0.0143 200 LYS A N 1568 C CA . LYS A 204 ? 0.2606 0.2923 0.3145 -0.0098 0.0176 -0.0112 200 LYS A CA 1569 C C . LYS A 204 ? 0.2636 0.2936 0.3138 -0.0087 0.0156 -0.0079 200 LYS A C 1570 O O . LYS A 204 ? 0.2733 0.3068 0.3224 -0.0088 0.0136 -0.0080 200 LYS A O 1571 C CB . LYS A 204 ? 0.2561 0.2846 0.3131 -0.0109 0.0217 -0.0128 200 LYS A CB 1572 C CG . LYS A 204 ? 0.2794 0.3096 0.3405 -0.0126 0.0241 -0.0164 200 LYS A CG 1573 C CD . LYS A 204 ? 0.2897 0.3173 0.3497 -0.0115 0.0241 -0.0145 200 LYS A CD 1574 C CE . LYS A 204 ? 0.3318 0.3599 0.3959 -0.0132 0.0273 -0.0175 200 LYS A CE 1575 N NZ . LYS A 204 ? 0.2817 0.3076 0.3444 -0.0119 0.0272 -0.0155 200 LYS A NZ 1576 N N . VAL A 205 ? 0.2541 0.2791 0.3024 -0.0075 0.0162 -0.0050 201 VAL A N 1577 C CA . VAL A 205 ? 0.2438 0.2676 0.2888 -0.0066 0.0144 -0.0020 201 VAL A CA 1578 C C . VAL A 205 ? 0.2421 0.2621 0.2872 -0.0058 0.0168 -0.0007 201 VAL A C 1579 O O . VAL A 205 ? 0.2364 0.2534 0.2831 -0.0056 0.0195 -0.0011 201 VAL A O 1580 C CB . VAL A 205 ? 0.2460 0.2683 0.2875 -0.0055 0.0118 0.0005 201 VAL A CB 1581 C CG1 . VAL A 205 ? 0.2321 0.2580 0.2730 -0.0057 0.0094 -0.0004 201 VAL A CG1 1582 C CG2 . VAL A 205 ? 0.2269 0.2454 0.2682 -0.0045 0.0132 0.0016 201 VAL A CG2 1583 N N . ALA A 206 ? 0.2303 0.2506 0.2737 -0.0054 0.0159 0.0008 202 ALA A N 1584 C CA . ALA A 206 ? 0.2378 0.2550 0.2803 -0.0040 0.0176 0.0027 202 ALA A CA 1585 C C . ALA A 206 ? 0.2394 0.2540 0.2795 -0.0026 0.0169 0.0051 202 ALA A C 1586 O O . ALA A 206 ? 0.2214 0.2371 0.2596 -0.0028 0.0142 0.0059 202 ALA A O 1587 C CB . ALA A 206 ? 0.2383 0.2577 0.2793 -0.0038 0.0162 0.0038 202 ALA A CB 1588 N N . ALA A 207 ? 0.2350 0.2462 0.2752 -0.0011 0.0195 0.0063 203 ALA A N 1589 C CA . ALA A 207 ? 0.2387 0.2478 0.2768 0.0006 0.0192 0.0085 203 ALA A CA 1590 C C . ALA A 207 ? 0.2525 0.2617 0.2883 0.0024 0.0191 0.0108 203 ALA A C 1591 O O . ALA A 207 ? 0.2481 0.2588 0.2841 0.0023 0.0193 0.0106 203 ALA A O 1592 C CB . ALA A 207 ? 0.2276 0.2331 0.2672 0.0013 0.0226 0.0083 203 ALA A CB 1593 N N . CYS A 208 ? 0.2457 0.2539 0.2792 0.0040 0.0185 0.0127 204 CYS A N 1594 C CA . CYS A 208 ? 0.2651 0.2745 0.2962 0.0059 0.0179 0.0147 204 CYS A CA 1595 C C . CYS A 208 ? 0.2698 0.2772 0.2994 0.0084 0.0193 0.0165 204 CYS A C 1596 O O . CYS A 208 ? 0.2674 0.2747 0.2958 0.0083 0.0176 0.0167 204 CYS A O 1597 C CB . CYS A 208 ? 0.2593 0.2718 0.2885 0.0046 0.0142 0.0148 204 CYS A CB 1598 S SG . CYS A 208 ? 0.2830 0.2985 0.3096 0.0063 0.0132 0.0167 204 CYS A SG 1599 N N . ALA A 209 ? 0.2742 0.2801 0.3037 0.0108 0.0222 0.0179 205 ALA A N 1600 C CA . ALA A 209 ? 0.2768 0.2813 0.3044 0.0137 0.0235 0.0199 205 ALA A CA 1601 C C . ALA A 209 ? 0.2762 0.2849 0.3010 0.0150 0.0209 0.0212 205 ALA A C 1602 O O . ALA A 209 ? 0.2810 0.2923 0.3052 0.0157 0.0206 0.0216 205 ALA A O 1603 C CB . ALA A 209 ? 0.2820 0.2832 0.3102 0.0162 0.0280 0.0213 205 ALA A CB 1604 N N . LYS A 210 ? 0.2654 0.2749 0.2884 0.0154 0.0191 0.0215 206 LYS A N 1605 C CA . LYS A 210 ? 0.2556 0.2694 0.2763 0.0161 0.0165 0.0220 206 LYS A CA 1606 C C . LYS A 210 ? 0.2685 0.2827 0.2869 0.0186 0.0165 0.0232 206 LYS A C 1607 O O . LYS A 210 ? 0.2867 0.2978 0.3054 0.0192 0.0179 0.0235 206 LYS A O 1608 C CB . LYS A 210 ? 0.2641 0.2795 0.2849 0.0126 0.0130 0.0203 206 LYS A CB 1609 C CG . LYS A 210 ? 0.2264 0.2397 0.2468 0.0114 0.0116 0.0195 206 LYS A CG 1610 C CD . LYS A 210 ? 0.2353 0.2493 0.2558 0.0081 0.0087 0.0180 206 LYS A CD 1611 C CE . LYS A 210 ? 0.2783 0.2905 0.2977 0.0074 0.0070 0.0173 206 LYS A CE 1612 N NZ . LYS A 210 ? 0.2659 0.2781 0.2850 0.0046 0.0046 0.0163 206 LYS A NZ 1613 N N . HIS A 211 ? 0.2663 0.2849 0.2825 0.0203 0.0151 0.0239 207 HIS A N 1614 C CA . HIS A 211 ? 0.2673 0.2905 0.2831 0.0201 0.0138 0.0237 207 HIS A CA 1615 C C . HIS A 211 ? 0.2800 0.3052 0.2946 0.0245 0.0163 0.0259 207 HIS A C 1616 O O . HIS A 211 ? 0.2917 0.3178 0.3044 0.0275 0.0170 0.0272 207 HIS A O 1617 C CB . HIS A 211 ? 0.2573 0.2849 0.2717 0.0185 0.0104 0.0225 207 HIS A CB 1618 C CG . HIS A 211 ? 0.2545 0.2796 0.2692 0.0152 0.0083 0.0208 207 HIS A CG 1619 N ND1 . HIS A 211 ? 0.2688 0.2915 0.2828 0.0158 0.0082 0.0208 207 HIS A ND1 1620 C CD2 . HIS A 211 ? 0.2583 0.2830 0.2739 0.0116 0.0063 0.0194 207 HIS A CD2 1621 C CE1 . HIS A 211 ? 0.2801 0.3008 0.2944 0.0128 0.0062 0.0193 207 HIS A CE1 1622 N NE2 . HIS A 211 ? 0.2521 0.2737 0.2673 0.0102 0.0051 0.0185 207 HIS A NE2 1623 N N . PHE A 212 ? 0.2722 0.2980 0.2876 0.0250 0.0176 0.0263 208 PHE A N 1624 C CA . PHE A 212 ? 0.2842 0.3102 0.2985 0.0295 0.0207 0.0285 208 PHE A CA 1625 C C . PHE A 212 ? 0.2819 0.3155 0.2940 0.0318 0.0189 0.0291 208 PHE A C 1626 O O . PHE A 212 ? 0.2817 0.3198 0.2941 0.0299 0.0166 0.0277 208 PHE A O 1627 C CB . PHE A 212 ? 0.2717 0.2955 0.2879 0.0288 0.0225 0.0283 208 PHE A CB 1628 C CG . PHE A 212 ? 0.3141 0.3372 0.3293 0.0333 0.0260 0.0305 208 PHE A CG 1629 C CD1 . PHE A 212 ? 0.2995 0.3163 0.3150 0.0353 0.0300 0.0320 208 PHE A CD1 1630 C CD2 . PHE A 212 ? 0.2997 0.3285 0.3137 0.0354 0.0254 0.0311 208 PHE A CD2 1631 C CE1 . PHE A 212 ? 0.3009 0.3162 0.3152 0.0398 0.0337 0.0344 208 PHE A CE1 1632 C CE2 . PHE A 212 ? 0.3282 0.3565 0.3409 0.0401 0.0286 0.0334 208 PHE A CE2 1633 C CZ . PHE A 212 ? 0.2911 0.3122 0.3039 0.0424 0.0329 0.0352 208 PHE A CZ 1634 N N . VAL A 213 ? 0.2971 0.3324 0.3068 0.0361 0.0201 0.0309 209 VAL A N 1635 C CA . VAL A 213 ? 0.2822 0.3124 0.2911 0.0387 0.0231 0.0328 209 VAL A CA 1636 C C . VAL A 213 ? 0.3017 0.3371 0.3078 0.0414 0.0217 0.0334 209 VAL A C 1637 O O . VAL A 213 ? 0.3075 0.3503 0.3122 0.0426 0.0196 0.0329 209 VAL A O 1638 C CB . VAL A 213 ? 0.3007 0.3269 0.3092 0.0428 0.0278 0.0356 209 VAL A CB 1639 C CG1 . VAL A 213 ? 0.2752 0.3077 0.2813 0.0473 0.0281 0.0372 209 VAL A CG1 1640 C CG2 . VAL A 213 ? 0.2525 0.2731 0.2602 0.0453 0.0313 0.0377 209 VAL A CG2 1641 N N . GLY A 214 ? 0.3188 0.3510 0.3243 0.0421 0.0225 0.0340 210 GLY A N 1642 C CA . GLY A 214 ? 0.3146 0.3517 0.3174 0.0447 0.0213 0.0344 210 GLY A CA 1643 C C . GLY A 214 ? 0.3107 0.3508 0.3138 0.0409 0.0171 0.0313 210 GLY A C 1644 O O . GLY A 214 ? 0.3079 0.3537 0.3090 0.0425 0.0154 0.0307 210 GLY A O 1645 N N . ASP A 215 ? 0.2903 0.3267 0.2958 0.0360 0.0156 0.0293 211 ASP A N 1646 C CA . ASP A 215 ? 0.2887 0.3264 0.2945 0.0323 0.0121 0.0266 211 ASP A CA 1647 C C . ASP A 215 ? 0.2837 0.3206 0.2880 0.0334 0.0119 0.0265 211 ASP A C 1648 O O . ASP A 215 ? 0.2934 0.3334 0.2967 0.0321 0.0092 0.0245 211 ASP A O 1649 C CB . ASP A 215 ? 0.2922 0.3253 0.3005 0.0273 0.0110 0.0248 211 ASP A CB 1650 C CG . ASP A 215 ? 0.2963 0.3224 0.3064 0.0270 0.0137 0.0258 211 ASP A CG 1651 O OD1 . ASP A 215 ? 0.2996 0.3235 0.3094 0.0301 0.0170 0.0279 211 ASP A OD1 1652 O OD2 . ASP A 215 ? 0.3195 0.3422 0.3312 0.0234 0.0127 0.0243 211 ASP A OD2 1653 N N . GLY A 216 ? 0.2941 0.3266 0.2982 0.0359 0.0149 0.0285 212 GLY A N 1654 C CA . GLY A 216 ? 0.2917 0.3233 0.2944 0.0372 0.0149 0.0286 212 GLY A CA 1655 C C . GLY A 216 ? 0.3160 0.3534 0.3157 0.0422 0.0156 0.0302 212 GLY A C 1656 O O . GLY A 216 ? 0.3041 0.3415 0.3023 0.0443 0.0161 0.0307 212 GLY A O 1657 N N . GLY A 217 ? 0.3125 0.3548 0.3113 0.0446 0.0159 0.0312 213 GLY A N 1658 C CA . GLY A 217 ? 0.3414 0.3897 0.3371 0.0503 0.0170 0.0332 213 GLY A CA 1659 C C . GLY A 217 ? 0.3551 0.4127 0.3494 0.0504 0.0135 0.0308 213 GLY A C 1660 O O . GLY A 217 ? 0.3676 0.4321 0.3595 0.0550 0.0140 0.0320 213 GLY A O 1661 N N . THR A 218 ? 0.3502 0.4086 0.3460 0.0454 0.0102 0.0274 214 THR A N 1662 C CA . THR A 218 ? 0.3602 0.4275 0.3553 0.0448 0.0073 0.0248 214 THR A CA 1663 C C . THR A 218 ? 0.3812 0.4543 0.3739 0.0471 0.0060 0.0236 214 THR A C 1664 O O . THR A 218 ? 0.3735 0.4425 0.3656 0.0474 0.0064 0.0238 214 THR A O 1665 C CB . THR A 218 ? 0.3668 0.4332 0.3641 0.0385 0.0043 0.0215 214 THR A CB 1666 O OG1 . THR A 218 ? 0.3692 0.4302 0.3669 0.0355 0.0032 0.0198 214 THR A OG1 1667 C CG2 . THR A 218 ? 0.2866 0.3487 0.2862 0.0361 0.0053 0.0224 214 THR A CG2 1668 N N . VAL A 219 ? 0.3848 0.4678 0.3764 0.0486 0.0043 0.0221 215 VAL A N 1669 C CA . VAL A 219 ? 0.3946 0.4847 0.3837 0.0514 0.0031 0.0208 215 VAL A CA 1670 C C . VAL A 219 ? 0.3785 0.4655 0.3683 0.0471 0.0008 0.0174 215 VAL A C 1671 O O . VAL A 219 ? 0.3743 0.4598 0.3661 0.0417 -0.0013 0.0145 215 VAL A O 1672 C CB . VAL A 219 ? 0.3860 0.4883 0.3744 0.0523 0.0011 0.0185 215 VAL A CB 1673 C CG1 . VAL A 219 ? 0.4370 0.5472 0.4235 0.0541 -0.0007 0.0160 215 VAL A CG1 1674 C CG2 . VAL A 219 ? 0.4324 0.5393 0.4195 0.0578 0.0033 0.0220 215 VAL A CG2 1675 N N . ASP A 220 ? 0.3774 0.4635 0.3654 0.0497 0.0014 0.0179 216 ASP A N 1676 C CA . ASP A 220 ? 0.3847 0.4676 0.3729 0.0464 -0.0005 0.0149 216 ASP A CA 1677 C C . ASP A 220 ? 0.3721 0.4450 0.3628 0.0412 -0.0007 0.0143 216 ASP A C 1678 O O . ASP A 220 ? 0.3696 0.4403 0.3608 0.0375 -0.0028 0.0111 216 ASP A O 1679 C CB . ASP A 220 ? 0.3800 0.4706 0.3680 0.0441 -0.0037 0.0102 216 ASP A CB 1680 C CG . ASP A 220 ? 0.4309 0.5327 0.4163 0.0493 -0.0039 0.0099 216 ASP A CG 1681 O OD1 . ASP A 220 ? 0.4314 0.5335 0.4148 0.0546 -0.0016 0.0134 216 ASP A OD1 1682 O OD2 . ASP A 220 ? 0.4684 0.5785 0.4538 0.0478 -0.0062 0.0063 216 ASP A OD2 1683 N N . GLY A 221 ? 0.3602 0.4272 0.3522 0.0412 0.0014 0.0172 217 GLY A N 1684 C CA . GLY A 221 ? 0.3597 0.4184 0.3541 0.0366 0.0012 0.0167 217 GLY A CA 1685 C C . GLY A 221 ? 0.3765 0.4364 0.3724 0.0315 -0.0014 0.0136 217 GLY A C 1686 O O . GLY A 221 ? 0.3792 0.4331 0.3763 0.0276 -0.0023 0.0123 217 GLY A O 1687 N N . ILE A 222 ? 0.3547 0.4225 0.3503 0.0317 -0.0026 0.0123 218 ILE A N 1688 C CA . ILE A 222 ? 0.3579 0.4267 0.3551 0.0266 -0.0048 0.0094 218 ILE A CA 1689 C C . ILE A 222 ? 0.3529 0.4167 0.3521 0.0244 -0.0038 0.0111 218 ILE A C 1690 O O . ILE A 222 ? 0.3511 0.4167 0.3505 0.0271 -0.0021 0.0136 218 ILE A O 1691 C CB . ILE A 222 ? 0.3633 0.4428 0.3600 0.0271 -0.0062 0.0073 218 ILE A CB 1692 C CG1 . ILE A 222 ? 0.3777 0.4625 0.3726 0.0286 -0.0075 0.0048 218 ILE A CG1 1693 C CG2 . ILE A 222 ? 0.3752 0.4553 0.3738 0.0216 -0.0079 0.0048 218 ILE A CG2 1694 C CD1 . ILE A 222 ? 0.4338 0.5313 0.4275 0.0319 -0.0081 0.0039 218 ILE A CD1 1695 N N . ASN A 223 ? 0.3465 0.4043 0.3471 0.0199 -0.0047 0.0099 219 ASN A N 1696 C CA . ASN A 223 ? 0.3512 0.4041 0.3536 0.0179 -0.0039 0.0113 219 ASN A CA 1697 C C . ASN A 223 ? 0.3530 0.4118 0.3563 0.0170 -0.0043 0.0111 219 ASN A C 1698 O O . ASN A 223 ? 0.3485 0.4129 0.3518 0.0149 -0.0061 0.0085 219 ASN A O 1699 C CB . ASN A 223 ? 0.3481 0.3949 0.3513 0.0133 -0.0052 0.0096 219 ASN A CB 1700 C CG . ASN A 223 ? 0.3523 0.3935 0.3572 0.0114 -0.0044 0.0111 219 ASN A CG 1701 O OD1 . ASN A 223 ? 0.4273 0.4660 0.4330 0.0076 -0.0055 0.0099 219 ASN A OD1 1702 N ND2 . ASN A 223 ? 0.2625 0.3019 0.2679 0.0141 -0.0023 0.0135 219 ASN A ND2 1703 N N . GLU A 224 ? 0.3401 0.3977 0.3444 0.0183 -0.0025 0.0134 220 GLU A N 1704 C CA . GLU A 224 ? 0.3547 0.4173 0.3599 0.0177 -0.0027 0.0135 220 GLU A CA 1705 C C . GLU A 224 ? 0.3723 0.4443 0.3762 0.0214 -0.0026 0.0135 220 GLU A C 1706 O O . GLU A 224 ? 0.3763 0.4542 0.3808 0.0210 -0.0031 0.0131 220 GLU A O 1707 C CB . GLU A 224 ? 0.3640 0.4273 0.3704 0.0124 -0.0047 0.0109 220 GLU A CB 1708 C CG . GLU A 224 ? 0.3853 0.4397 0.3927 0.0088 -0.0049 0.0108 220 GLU A CG 1709 C CD . GLU A 224 ? 0.4472 0.5016 0.4557 0.0038 -0.0064 0.0090 220 GLU A CD 1710 O OE1 . GLU A 224 ? 0.4178 0.4787 0.4268 0.0027 -0.0070 0.0081 220 GLU A OE1 1711 O OE2 . GLU A 224 ? 0.5074 0.5552 0.5160 0.0011 -0.0068 0.0087 220 GLU A OE2 1712 N N . ASN A 225 ? 0.3727 0.4466 0.3748 0.0252 -0.0021 0.0141 221 ASN A N 1713 C CA . ASN A 225 ? 0.3815 0.4655 0.3820 0.0289 -0.0024 0.0138 221 ASN A CA 1714 C C . ASN A 225 ? 0.3734 0.4592 0.3729 0.0344 0.0002 0.0174 221 ASN A C 1715 O O . ASN A 225 ? 0.3575 0.4381 0.3582 0.0344 0.0019 0.0194 221 ASN A O 1716 C CB . ASN A 225 ? 0.3797 0.4663 0.3785 0.0302 -0.0034 0.0123 221 ASN A CB 1717 C CG . ASN A 225 ? 0.4348 0.5328 0.4328 0.0309 -0.0052 0.0097 221 ASN A CG 1718 O OD1 . ASN A 225 ? 0.4224 0.5270 0.4184 0.0361 -0.0045 0.0109 221 ASN A OD1 1719 N ND2 . ASN A 225 ? 0.4429 0.5436 0.4424 0.0258 -0.0074 0.0062 221 ASN A ND2 1720 N N . ASN A 226 ? 0.3639 0.4570 0.3612 0.0393 0.0005 0.0180 222 ASN A N 1721 C CA . ASN A 226 ? 0.3691 0.4647 0.3649 0.0452 0.0031 0.0215 222 ASN A CA 1722 C C . ASN A 226 ? 0.3625 0.4517 0.3567 0.0492 0.0059 0.0247 222 ASN A C 1723 O O . ASN A 226 ? 0.3734 0.4626 0.3663 0.0498 0.0053 0.0240 222 ASN A O 1724 C CB . ASN A 226 ? 0.3729 0.4811 0.3668 0.0489 0.0020 0.0206 222 ASN A CB 1725 C CG . ASN A 226 ? 0.3979 0.5102 0.3906 0.0544 0.0042 0.0237 222 ASN A CG 1726 O OD1 . ASN A 226 ? 0.4014 0.5072 0.3949 0.0548 0.0064 0.0261 222 ASN A OD1 1727 N ND2 . ASN A 226 ? 0.3674 0.4909 0.3580 0.0588 0.0036 0.0234 222 ASN A ND2 1728 N N . THR A 227 ? 0.3467 0.4303 0.3410 0.0516 0.0090 0.0280 223 THR A N 1729 C CA . THR A 227 ? 0.3677 0.4457 0.3605 0.0558 0.0124 0.0314 223 THR A CA 1730 C C . THR A 227 ? 0.3847 0.4687 0.3746 0.0628 0.0146 0.0344 223 THR A C 1731 O O . THR A 227 ? 0.3837 0.4682 0.3738 0.0645 0.0160 0.0359 223 THR A O 1732 C CB . THR A 227 ? 0.3690 0.4363 0.3639 0.0537 0.0149 0.0329 223 THR A CB 1733 O OG1 . THR A 227 ? 0.3551 0.4173 0.3521 0.0480 0.0129 0.0304 223 THR A OG1 1734 C CG2 . THR A 227 ? 0.3588 0.4203 0.3523 0.0581 0.0190 0.0366 223 THR A CG2 1735 N N . ILE A 228 ? 0.4059 0.4944 0.3931 0.0670 0.0148 0.0352 224 ILE A N 1736 C CA . ILE A 228 ? 0.4223 0.5179 0.4063 0.0742 0.0166 0.0380 224 ILE A CA 1737 C C . ILE A 228 ? 0.4412 0.5293 0.4233 0.0788 0.0211 0.0426 224 ILE A C 1738 O O . ILE A 228 ? 0.4348 0.5212 0.4157 0.0799 0.0216 0.0431 224 ILE A O 1739 C CB . ILE A 228 ? 0.4264 0.5341 0.4084 0.0761 0.0137 0.0357 224 ILE A CB 1740 C CG1 . ILE A 228 ? 0.4296 0.5444 0.4139 0.0709 0.0097 0.0311 224 ILE A CG1 1741 C CG2 . ILE A 228 ? 0.4497 0.5654 0.4281 0.0844 0.0157 0.0390 224 ILE A CG2 1742 C CD1 . ILE A 228 ? 0.4489 0.5733 0.4325 0.0699 0.0062 0.0271 224 ILE A CD1 1743 N N . ILE A 229 ? 0.4503 0.5335 0.4323 0.0814 0.0246 0.0458 225 ILE A N 1744 C CA . ILE A 229 ? 0.4615 0.5365 0.4421 0.0854 0.0294 0.0501 225 ILE A CA 1745 C C . ILE A 229 ? 0.4735 0.5469 0.4533 0.0893 0.0326 0.0531 225 ILE A C 1746 O O . ILE A 229 ? 0.4614 0.5359 0.4432 0.0865 0.0312 0.0514 225 ILE A O 1747 C CB . ILE A 229 ? 0.4497 0.5130 0.4333 0.0801 0.0306 0.0495 225 ILE A CB 1748 C CG1 . ILE A 229 ? 0.4655 0.5213 0.4475 0.0838 0.0354 0.0535 225 ILE A CG1 1749 C CG2 . ILE A 229 ? 0.4478 0.5057 0.4347 0.0755 0.0306 0.0482 225 ILE A CG2 1750 C CD1 . ILE A 229 ? 0.4690 0.5162 0.4534 0.0790 0.0359 0.0523 225 ILE A CD1 1751 N N . ASN A 230 ? 0.4835 0.5543 0.4601 0.0959 0.0371 0.0577 226 ASN A N 1752 C CA . ASN A 230 ? 0.4881 0.5564 0.4635 0.1002 0.0407 0.0609 226 ASN A CA 1753 C C . ASN A 230 ? 0.4827 0.5390 0.4614 0.0960 0.0433 0.0610 226 ASN A C 1754 O O . ASN A 230 ? 0.4528 0.5022 0.4342 0.0907 0.0430 0.0593 226 ASN A O 1755 C CB . ASN A 230 ? 0.5030 0.5719 0.4737 0.1090 0.0450 0.0662 226 ASN A CB 1756 C CG . ASN A 230 ? 0.5358 0.5950 0.5060 0.1096 0.0489 0.0688 226 ASN A CG 1757 O OD1 . ASN A 230 ? 0.5380 0.5889 0.5114 0.1037 0.0490 0.0671 226 ASN A OD1 1758 N ND2 . ASN A 230 ? 0.5326 0.5929 0.4984 0.1171 0.0524 0.0733 226 ASN A ND2 1759 N N . ARG A 231 ? 0.4742 0.5282 0.4527 0.0984 0.0458 0.0627 227 ARG A N 1760 C CA . ARG A 231 ? 0.4747 0.5178 0.4566 0.0943 0.0483 0.0622 227 ARG A CA 1761 C C . ARG A 231 ? 0.4752 0.5073 0.4575 0.0936 0.0524 0.0641 227 ARG A C 1762 O O . ARG A 231 ? 0.4697 0.4947 0.4556 0.0878 0.0525 0.0620 227 ARG A O 1763 C CB . ARG A 231 ? 0.4792 0.5209 0.4603 0.0978 0.0510 0.0641 227 ARG A CB 1764 C CG . ARG A 231 ? 0.4943 0.5256 0.4790 0.0933 0.0533 0.0630 227 ARG A CG 1765 C CD . ARG A 231 ? 0.5093 0.5404 0.4932 0.0969 0.0556 0.0644 227 ARG A CD 1766 N NE A ARG A 231 ? 0.4939 0.5159 0.4810 0.0931 0.0578 0.0631 227 ARG A NE 1767 N NE B ARG A 231 ? 0.4655 0.5006 0.4524 0.0918 0.0516 0.0605 227 ARG A NE 1768 C CZ A ARG A 231 ? 0.5224 0.5328 0.5104 0.0928 0.0628 0.0646 227 ARG A CZ 1769 C CZ B ARG A 231 ? 0.4484 0.4772 0.4385 0.0879 0.0527 0.0587 227 ARG A CZ 1770 N NH1 A ARG A 231 ? 0.5488 0.5542 0.5348 0.0958 0.0664 0.0677 227 ARG A NH1 1771 N NH1 B ARG A 231 ? 0.4395 0.4734 0.4320 0.0836 0.0488 0.0553 227 ARG A NH1 1772 N NH2 A ARG A 231 ? 0.5465 0.5504 0.5377 0.0891 0.0643 0.0627 227 ARG A NH2 1773 N NH2 B ARG A 231 ? 0.4617 0.4792 0.4526 0.0881 0.0577 0.0602 227 ARG A NH2 1774 N N . GLU A 232 ? 0.4733 0.5045 0.4520 0.0996 0.0558 0.0681 228 GLU A N 1775 C CA . GLU A 232 ? 0.4698 0.4903 0.4490 0.0991 0.0604 0.0702 228 GLU A CA 1776 C C . GLU A 232 ? 0.4558 0.4752 0.4378 0.0928 0.0575 0.0669 228 GLU A C 1777 O O . GLU A 232 ? 0.4548 0.4655 0.4399 0.0885 0.0595 0.0661 228 GLU A O 1778 C CB . GLU A 232 ? 0.4956 0.5154 0.4701 0.1071 0.0650 0.0755 228 GLU A CB 1779 C CG . GLU A 232 ? 0.5453 0.5564 0.5200 0.1064 0.0689 0.0775 228 GLU A CG 1780 C CD . GLU A 232 ? 0.6577 0.6665 0.6277 0.1146 0.0744 0.0833 228 GLU A CD 1781 O OE1 . GLU A 232 ? 0.6913 0.7075 0.6573 0.1211 0.0742 0.0856 228 GLU A OE1 1782 O OE2 . GLU A 232 ? 0.6998 0.6996 0.6699 0.1145 0.0791 0.0856 228 GLU A OE2 1783 N N . GLY A 233 ? 0.4306 0.4592 0.4118 0.0922 0.0527 0.0648 229 GLY A N 1784 C CA . GLY A 233 ? 0.4199 0.4486 0.4033 0.0869 0.0495 0.0617 229 GLY A CA 1785 C C . GLY A 233 ? 0.4104 0.4370 0.3982 0.0795 0.0464 0.0574 229 GLY A C 1786 O O . GLY A 233 ? 0.3950 0.4163 0.3855 0.0748 0.0461 0.0556 229 GLY A O 1787 N N . LEU A 234 ? 0.3787 0.4094 0.3673 0.0786 0.0443 0.0559 230 LEU A N 1788 C CA . LEU A 234 ? 0.3798 0.4083 0.3723 0.0720 0.0417 0.0522 230 LEU A CA 1789 C C . LEU A 234 ? 0.3946 0.4124 0.3897 0.0699 0.0459 0.0529 230 LEU A C 1790 O O . LEU A 234 ? 0.3737 0.3874 0.3720 0.0644 0.0448 0.0503 230 LEU A O 1791 C CB . LEU A 234 ? 0.3697 0.4048 0.3623 0.0721 0.0393 0.0510 230 LEU A CB 1792 C CG . LEU A 234 ? 0.3679 0.4016 0.3643 0.0654 0.0364 0.0472 230 LEU A CG 1793 C CD1 . LEU A 234 ? 0.3299 0.3686 0.3271 0.0612 0.0315 0.0440 230 LEU A CD1 1794 C CD2 . LEU A 234 ? 0.4077 0.4453 0.4043 0.0662 0.0359 0.0469 230 LEU A CD2 1795 N N . MET A 235 ? 0.3818 0.3950 0.3753 0.0745 0.0508 0.0563 231 MET A N 1796 C CA . MET A 235 ? 0.4008 0.4040 0.3968 0.0724 0.0550 0.0566 231 MET A CA 1797 C C . MET A 235 ? 0.4004 0.3969 0.3974 0.0711 0.0579 0.0574 231 MET A C 1798 O O . MET A 235 ? 0.4239 0.4134 0.4242 0.0672 0.0599 0.0560 231 MET A O 1799 C CB . MET A 235 ? 0.4088 0.4087 0.4029 0.0777 0.0596 0.0599 231 MET A CB 1800 C CG . MET A 235 ? 0.3922 0.3984 0.3859 0.0786 0.0571 0.0589 231 MET A CG 1801 S SD . MET A 235 ? 0.4585 0.4624 0.4573 0.0708 0.0545 0.0541 231 MET A SD 1802 C CE . MET A 235 ? 0.4249 0.4359 0.4229 0.0729 0.0525 0.0537 231 MET A CE 1803 N N . ASN A 236 ? 0.4055 0.4048 0.3996 0.0744 0.0579 0.0594 232 ASN A N 1804 C CA . ASN A 236 ? 0.4330 0.4268 0.4276 0.0737 0.0607 0.0604 232 ASN A CA 1805 C C . ASN A 236 ? 0.4028 0.3983 0.4000 0.0681 0.0566 0.0567 232 ASN A C 1806 O O . ASN A 236 ? 0.3873 0.3773 0.3866 0.0656 0.0588 0.0563 232 ASN A O 1807 C CB . ASN A 236 ? 0.4562 0.4530 0.4463 0.0803 0.0626 0.0644 232 ASN A CB 1808 C CG . ASN A 236 ? 0.5662 0.5573 0.5565 0.0801 0.0661 0.0660 232 ASN A CG 1809 O OD1 . ASN A 236 ? 0.6832 0.6653 0.6758 0.0781 0.0705 0.0665 232 ASN A OD1 1810 N ND2 . ASN A 236 ? 0.6357 0.6320 0.6234 0.0824 0.0644 0.0668 232 ASN A ND2 1811 N N . ILE A 237 ? 0.3753 0.3786 0.3723 0.0665 0.0510 0.0541 233 ILE A N 1812 C CA . ILE A 237 ? 0.3674 0.3726 0.3660 0.0621 0.0471 0.0509 233 ILE A CA 1813 C C . ILE A 237 ? 0.3655 0.3710 0.3674 0.0563 0.0436 0.0470 233 ILE A C 1814 O O . ILE A 237 ? 0.3691 0.3706 0.3740 0.0520 0.0434 0.0449 233 ILE A O 1815 C CB . ILE A 237 ? 0.3585 0.3720 0.3541 0.0645 0.0435 0.0507 233 ILE A CB 1816 C CG1 . ILE A 237 ? 0.4006 0.4144 0.3928 0.0702 0.0468 0.0545 233 ILE A CG1 1817 C CG2 . ILE A 237 ? 0.3532 0.3683 0.3504 0.0598 0.0393 0.0471 233 ILE A CG2 1818 C CD1 . ILE A 237 ? 0.4144 0.4377 0.4033 0.0732 0.0432 0.0541 233 ILE A CD1 1819 N N . HIS A 238 ? 0.3392 0.3497 0.3407 0.0565 0.0411 0.0461 234 HIS A N 1820 C CA . HIS A 238 ? 0.3443 0.3566 0.3483 0.0512 0.0371 0.0425 234 HIS A CA 1821 C C . HIS A 238 ? 0.3481 0.3557 0.3550 0.0485 0.0386 0.0415 234 HIS A C 1822 O O . HIS A 238 ? 0.3178 0.3251 0.3274 0.0436 0.0360 0.0385 234 HIS A O 1823 C CB . HIS A 238 ? 0.3428 0.3636 0.3449 0.0523 0.0333 0.0417 234 HIS A CB 1824 C CG . HIS A 238 ? 0.3515 0.3771 0.3516 0.0532 0.0307 0.0412 234 HIS A CG 1825 N ND1 . HIS A 238 ? 0.3467 0.3776 0.3433 0.0584 0.0311 0.0432 234 HIS A ND1 1826 C CD2 . HIS A 238 ? 0.2742 0.2996 0.2751 0.0498 0.0280 0.0388 234 HIS A CD2 1827 C CE1 . HIS A 238 ? 0.2915 0.3258 0.2872 0.0579 0.0286 0.0418 234 HIS A CE1 1828 N NE2 . HIS A 238 ? 0.3459 0.3765 0.3441 0.0527 0.0268 0.0392 234 HIS A NE2 1829 N N . MET A 239 ? 0.3375 0.3416 0.3438 0.0518 0.0429 0.0440 235 MET A N 1830 C CA . MET A 239 ? 0.3421 0.3417 0.3510 0.0499 0.0450 0.0432 235 MET A CA 1831 C C . MET A 239 ? 0.3369 0.3285 0.3488 0.0472 0.0486 0.0425 235 MET A C 1832 O O . MET A 239 ? 0.3408 0.3301 0.3555 0.0437 0.0486 0.0403 235 MET A O 1833 C CB . MET A 239 ? 0.3473 0.3469 0.3540 0.0549 0.0480 0.0460 235 MET A CB 1834 C CG . MET A 239 ? 0.3374 0.3340 0.3464 0.0531 0.0493 0.0448 235 MET A CG 1835 S SD . MET A 239 ? 0.3543 0.3578 0.3650 0.0488 0.0436 0.0411 235 MET A SD 1836 C CE . MET A 239 ? 0.3606 0.3730 0.3674 0.0541 0.0419 0.0432 235 MET A CE 1837 N N . PRO A 240 ? 0.3409 0.3281 0.3521 0.0490 0.0521 0.0446 236 PRO A N 1838 C CA . PRO A 240 ? 0.3329 0.3123 0.3472 0.0466 0.0564 0.0440 236 PRO A CA 1839 C C . PRO A 240 ? 0.3320 0.3105 0.3505 0.0404 0.0543 0.0398 236 PRO A C 1840 O O . PRO A 240 ? 0.3462 0.3202 0.3676 0.0381 0.0570 0.0383 236 PRO A O 1841 C CB . PRO A 240 ? 0.3469 0.3237 0.3601 0.0483 0.0590 0.0460 236 PRO A CB 1842 C CG . PRO A 240 ? 0.3830 0.3638 0.3915 0.0544 0.0590 0.0497 236 PRO A CG 1843 C CD . PRO A 240 ? 0.3409 0.3298 0.3485 0.0539 0.0533 0.0479 236 PRO A CD 1844 N N . ALA A 241 ? 0.3113 0.2941 0.3302 0.0378 0.0498 0.0378 237 ALA A N 1845 C CA . ALA A 241 ? 0.3098 0.2920 0.3323 0.0325 0.0480 0.0341 237 ALA A CA 1846 C C . ALA A 241 ? 0.3132 0.2971 0.3374 0.0302 0.0462 0.0319 237 ALA A C 1847 O O . ALA A 241 ? 0.3216 0.3040 0.3491 0.0263 0.0462 0.0291 237 ALA A O 1848 C CB . ALA A 241 ? 0.2943 0.2804 0.3165 0.0306 0.0438 0.0327 237 ALA A CB 1849 N N . TYR A 242 ? 0.3120 0.2993 0.3339 0.0326 0.0448 0.0331 238 TYR A N 1850 C CA . TYR A 242 ? 0.3272 0.3157 0.3506 0.0310 0.0440 0.0315 238 TYR A CA 1851 C C . TYR A 242 ? 0.3404 0.3229 0.3659 0.0309 0.0487 0.0312 238 TYR A C 1852 O O . TYR A 242 ? 0.3434 0.3255 0.3716 0.0277 0.0483 0.0285 238 TYR A O 1853 C CB . TYR A 242 ? 0.3130 0.3069 0.3336 0.0339 0.0418 0.0329 238 TYR A CB 1854 C CG . TYR A 242 ? 0.2820 0.2819 0.3017 0.0320 0.0366 0.0316 238 TYR A CG 1855 C CD1 . TYR A 242 ? 0.2828 0.2851 0.3044 0.0280 0.0333 0.0288 238 TYR A CD1 1856 C CD2 . TYR A 242 ? 0.2733 0.2763 0.2904 0.0342 0.0350 0.0329 238 TYR A CD2 1857 C CE1 . TYR A 242 ? 0.2713 0.2781 0.2921 0.0260 0.0290 0.0276 238 TYR A CE1 1858 C CE2 . TYR A 242 ? 0.2969 0.3047 0.3133 0.0320 0.0304 0.0314 238 TYR A CE2 1859 C CZ . TYR A 242 ? 0.2913 0.3006 0.3097 0.0279 0.0275 0.0288 238 TYR A CZ 1860 O OH . TYR A 242 ? 0.2796 0.2928 0.2972 0.0258 0.0234 0.0274 238 TYR A OH 1861 N N . LYS A 243 ? 0.3519 0.3294 0.3763 0.0342 0.0535 0.0339 239 LYS A N 1862 C CA . LYS A 243 ? 0.3482 0.3190 0.3748 0.0337 0.0586 0.0335 239 LYS A CA 1863 C C . LYS A 243 ? 0.3337 0.3013 0.3644 0.0289 0.0597 0.0303 239 LYS A C 1864 O O . LYS A 243 ? 0.3433 0.3086 0.3771 0.0261 0.0612 0.0276 239 LYS A O 1865 C CB . LYS A 243 ? 0.3751 0.3406 0.3993 0.0386 0.0639 0.0374 239 LYS A CB 1866 C CG . LYS A 243 ? 0.4141 0.3713 0.4408 0.0376 0.0697 0.0368 239 LYS A CG 1867 C CD . LYS A 243 ? 0.5104 0.4674 0.5381 0.0372 0.0699 0.0352 239 LYS A CD 1868 C CE . LYS A 243 ? 0.6022 0.5504 0.6305 0.0390 0.0767 0.0363 239 LYS A CE 1869 N NZ . LYS A 243 ? 0.6098 0.5522 0.6423 0.0344 0.0801 0.0335 239 LYS A NZ 1870 N N . ASN A 244 ? 0.3313 0.2994 0.3622 0.0278 0.0589 0.0303 240 ASN A N 1871 C CA . ASN A 244 ? 0.3226 0.2897 0.3575 0.0231 0.0590 0.0269 240 ASN A CA 1872 C C . ASN A 244 ? 0.3143 0.2860 0.3514 0.0193 0.0547 0.0232 240 ASN A C 1873 O O . ASN A 244 ? 0.3030 0.2734 0.3437 0.0158 0.0559 0.0199 240 ASN A O 1874 C CB . ASN A 244 ? 0.3328 0.3013 0.3669 0.0231 0.0578 0.0276 240 ASN A CB 1875 C CG . ASN A 244 ? 0.3852 0.3492 0.4173 0.0268 0.0623 0.0313 240 ASN A CG 1876 O OD1 . ASN A 244 ? 0.4145 0.3796 0.4427 0.0311 0.0621 0.0347 240 ASN A OD1 1877 N ND2 . ASN A 244 ? 0.4750 0.4342 0.5096 0.0249 0.0665 0.0306 240 ASN A ND2 1878 N N . ALA A 245 ? 0.3001 0.2772 0.3349 0.0199 0.0499 0.0236 241 ALA A N 1879 C CA . ALA A 245 ? 0.2950 0.2765 0.3313 0.0168 0.0460 0.0206 241 ALA A CA 1880 C C . ALA A 245 ? 0.3006 0.2809 0.3387 0.0160 0.0478 0.0191 241 ALA A C 1881 O O . ALA A 245 ? 0.2925 0.2738 0.3335 0.0126 0.0470 0.0158 241 ALA A O 1882 C CB . ALA A 245 ? 0.2996 0.2869 0.3327 0.0179 0.0409 0.0217 241 ALA A CB 1883 N N . MET A 246 ? 0.3162 0.2941 0.3524 0.0195 0.0504 0.0215 242 MET A N 1884 C CA . MET A 246 ? 0.3175 0.2931 0.3554 0.0192 0.0530 0.0202 242 MET A CA 1885 C C . MET A 246 ? 0.3238 0.2942 0.3655 0.0165 0.0571 0.0176 242 MET A C 1886 O O . MET A 246 ? 0.3191 0.2899 0.3635 0.0136 0.0572 0.0142 242 MET A O 1887 C CB . MET A 246 ? 0.3340 0.3070 0.3690 0.0241 0.0560 0.0235 242 MET A CB 1888 C CG . MET A 246 ? 0.3203 0.2988 0.3514 0.0275 0.0526 0.0263 242 MET A CG 1889 S SD . MET A 246 ? 0.3720 0.3579 0.4033 0.0254 0.0474 0.0241 242 MET A SD 1890 C CE . MET A 246 ? 0.3532 0.3443 0.3840 0.0227 0.0420 0.0233 242 MET A CE 1891 N N . ASP A 247 ? 0.3254 0.2911 0.3672 0.0172 0.0606 0.0190 243 ASP A N 1892 C CA . ASP A 247 ? 0.3504 0.3110 0.3960 0.0143 0.0650 0.0165 243 ASP A CA 1893 C C . ASP A 247 ? 0.3502 0.3148 0.3994 0.0094 0.0624 0.0120 243 ASP A C 1894 O O . ASP A 247 ? 0.3333 0.2959 0.3863 0.0063 0.0650 0.0086 243 ASP A O 1895 C CB . ASP A 247 ? 0.3503 0.3059 0.3954 0.0157 0.0690 0.0189 243 ASP A CB 1896 C CG . ASP A 247 ? 0.3959 0.3460 0.4379 0.0205 0.0732 0.0231 243 ASP A CG 1897 O OD1 . ASP A 247 ? 0.4094 0.3589 0.4503 0.0225 0.0737 0.0236 243 ASP A OD1 1898 O OD2 . ASP A 247 ? 0.4109 0.3580 0.4512 0.0227 0.0757 0.0260 243 ASP A OD2 1899 N N . LYS A 248 ? 0.3303 0.3008 0.3784 0.0088 0.0572 0.0120 244 LYS A N 1900 C CA . LYS A 248 ? 0.3350 0.3099 0.3858 0.0049 0.0543 0.0083 244 LYS A CA 1901 C C . LYS A 248 ? 0.3274 0.3076 0.3782 0.0036 0.0502 0.0064 244 LYS A C 1902 O O . LYS A 248 ? 0.3355 0.3202 0.3878 0.0010 0.0472 0.0038 244 LYS A O 1903 C CB . LYS A 248 ? 0.3257 0.3030 0.3751 0.0052 0.0516 0.0096 244 LYS A CB 1904 C CG . LYS A 248 ? 0.3363 0.3086 0.3861 0.0061 0.0561 0.0111 244 LYS A CG 1905 C CD . LYS A 248 ? 0.3284 0.3025 0.3762 0.0072 0.0539 0.0129 244 LYS A CD 1906 C CE . LYS A 248 ? 0.3389 0.3074 0.3870 0.0084 0.0592 0.0149 244 LYS A CE 1907 N NZ . LYS A 248 ? 0.3683 0.3389 0.4151 0.0090 0.0574 0.0159 244 LYS A NZ 1908 N N . GLY A 249 ? 0.3256 0.3056 0.3747 0.0056 0.0502 0.0077 245 GLY A N 1909 C CA . GLY A 249 ? 0.3043 0.2892 0.3541 0.0041 0.0471 0.0055 245 GLY A CA 1910 C C . GLY A 249 ? 0.2921 0.2828 0.3394 0.0041 0.0416 0.0065 245 GLY A C 1911 O O . GLY A 249 ? 0.2925 0.2876 0.3408 0.0020 0.0387 0.0043 245 GLY A O 1912 N N . VAL A 250 ? 0.2896 0.2803 0.3337 0.0065 0.0402 0.0097 246 VAL A N 1913 C CA . VAL A 250 ? 0.2812 0.2768 0.3231 0.0063 0.0352 0.0105 246 VAL A CA 1914 C C . VAL A 250 ? 0.2796 0.2789 0.3210 0.0061 0.0332 0.0100 246 VAL A C 1915 O O . VAL A 250 ? 0.2841 0.2822 0.3249 0.0080 0.0351 0.0110 246 VAL A O 1916 C CB . VAL A 250 ? 0.2774 0.2728 0.3160 0.0091 0.0342 0.0138 246 VAL A CB 1917 C CG1 . VAL A 250 ? 0.3010 0.2963 0.3371 0.0125 0.0352 0.0164 246 VAL A CG1 1918 C CG2 . VAL A 250 ? 0.2823 0.2818 0.3193 0.0080 0.0295 0.0138 246 VAL A CG2 1919 N N . SER A 251 ? 0.2770 0.2805 0.3186 0.0039 0.0296 0.0085 247 SER A N 1920 C CA . SER A 251 ? 0.2724 0.2795 0.3140 0.0033 0.0281 0.0077 247 SER A CA 1921 C C . SER A 251 ? 0.2638 0.2734 0.3023 0.0051 0.0260 0.0102 247 SER A C 1922 O O . SER A 251 ? 0.2556 0.2673 0.2939 0.0056 0.0260 0.0102 247 SER A O 1923 C CB . SER A 251 ? 0.2840 0.2950 0.3267 0.0004 0.0252 0.0054 247 SER A CB 1924 O OG . SER A 251 ? 0.2838 0.2939 0.3298 -0.0013 0.0272 0.0024 247 SER A OG 1925 N N . THR A 252 ? 0.2507 0.2609 0.2870 0.0058 0.0241 0.0120 248 THR A N 1926 C CA . THR A 252 ? 0.2472 0.2604 0.2808 0.0072 0.0220 0.0140 248 THR A CA 1927 C C . THR A 252 ? 0.2667 0.2785 0.2981 0.0097 0.0224 0.0162 248 THR A C 1928 O O . THR A 252 ? 0.2570 0.2657 0.2887 0.0099 0.0235 0.0164 248 THR A O 1929 C CB . THR A 252 ? 0.2598 0.2768 0.2925 0.0048 0.0180 0.0134 248 THR A CB 1930 O OG1 . THR A 252 ? 0.2499 0.2655 0.2819 0.0041 0.0166 0.0135 248 THR A OG1 1931 C CG2 . THR A 252 ? 0.2406 0.2593 0.2754 0.0024 0.0174 0.0111 248 THR A CG2 1932 N N . VAL A 253 ? 0.2578 0.2727 0.2871 0.0116 0.0214 0.0179 249 VAL A N 1933 C CA . VAL A 253 ? 0.2706 0.2857 0.2976 0.0140 0.0212 0.0199 249 VAL A CA 1934 C C . VAL A 253 ? 0.2629 0.2832 0.2881 0.0132 0.0176 0.0200 249 VAL A C 1935 O O . VAL A 253 ? 0.2605 0.2845 0.2855 0.0129 0.0167 0.0198 249 VAL A O 1936 C CB . VAL A 253 ? 0.2789 0.2929 0.3048 0.0180 0.0244 0.0219 249 VAL A CB 1937 C CG1 . VAL A 253 ? 0.2700 0.2863 0.2931 0.0208 0.0236 0.0239 249 VAL A CG1 1938 C CG2 . VAL A 253 ? 0.2863 0.2940 0.3139 0.0188 0.0287 0.0219 249 VAL A CG2 1939 N N . MET A 254 ? 0.2441 0.2646 0.2679 0.0127 0.0158 0.0202 250 MET A N 1940 C CA . MET A 254 ? 0.2565 0.2817 0.2786 0.0119 0.0127 0.0202 250 MET A CA 1941 C C . MET A 254 ? 0.2652 0.2932 0.2852 0.0152 0.0130 0.0217 250 MET A C 1942 O O . MET A 254 ? 0.2686 0.2943 0.2877 0.0175 0.0145 0.0228 250 MET A O 1943 C CB . MET A 254 ? 0.2438 0.2679 0.2656 0.0091 0.0102 0.0191 250 MET A CB 1944 C CG . MET A 254 ? 0.2725 0.3004 0.2926 0.0077 0.0073 0.0187 250 MET A CG 1945 S SD . MET A 254 ? 0.2774 0.3027 0.2968 0.0049 0.0048 0.0176 250 MET A SD 1946 C CE . MET A 254 ? 0.2309 0.2535 0.2522 0.0026 0.0050 0.0168 250 MET A CE 1947 N N . ILE A 255 ? 0.2506 0.2841 0.2696 0.0154 0.0115 0.0217 251 ILE A N 1948 C CA . ILE A 255 ? 0.2726 0.3104 0.2895 0.0186 0.0116 0.0229 251 ILE A CA 1949 C C . ILE A 255 ? 0.2712 0.3108 0.2867 0.0177 0.0092 0.0222 251 ILE A C 1950 O O . ILE A 255 ? 0.2857 0.3254 0.3016 0.0140 0.0069 0.0206 251 ILE A O 1951 C CB . ILE A 255 ? 0.2598 0.3041 0.2765 0.0192 0.0109 0.0228 251 ILE A CB 1952 C CG1 . ILE A 255 ? 0.2629 0.3053 0.2809 0.0203 0.0133 0.0234 251 ILE A CG1 1953 C CG2 . ILE A 255 ? 0.2505 0.3005 0.2650 0.0232 0.0110 0.0240 251 ILE A CG2 1954 C CD1 . ILE A 255 ? 0.3060 0.3432 0.3237 0.0242 0.0171 0.0252 251 ILE A CD1 1955 N N . SER A 256 ? 0.2695 0.3107 0.2833 0.0211 0.0100 0.0233 252 SER A N 1956 C CA . SER A 256 ? 0.2715 0.3148 0.2838 0.0207 0.0080 0.0224 252 SER A CA 1957 C C . SER A 256 ? 0.2884 0.3392 0.2998 0.0195 0.0054 0.0210 252 SER A C 1958 O O . SER A 256 ? 0.2820 0.3383 0.2933 0.0214 0.0058 0.0215 252 SER A O 1959 C CB . SER A 256 ? 0.2406 0.2834 0.2511 0.0251 0.0098 0.0242 252 SER A CB 1960 O OG . SER A 256 ? 0.2887 0.3336 0.2979 0.0245 0.0078 0.0230 252 SER A OG 1961 N N . TYR A 257 ? 0.2778 0.3292 0.2890 0.0166 0.0030 0.0192 253 TYR A N 1962 C CA . TYR A 257 ? 0.3042 0.3629 0.3146 0.0156 0.0009 0.0175 253 TYR A CA 1963 C C . TYR A 257 ? 0.3162 0.3810 0.3248 0.0201 0.0014 0.0182 253 TYR A C 1964 O O . TYR A 257 ? 0.3088 0.3815 0.3169 0.0201 0.0000 0.0169 253 TYR A O 1965 C CB . TYR A 257 ? 0.2836 0.3405 0.2937 0.0122 -0.0012 0.0154 253 TYR A CB 1966 C CG . TYR A 257 ? 0.3001 0.3525 0.3114 0.0074 -0.0023 0.0143 253 TYR A CG 1967 C CD1 . TYR A 257 ? 0.2957 0.3509 0.3081 0.0046 -0.0030 0.0137 253 TYR A CD1 1968 C CD2 . TYR A 257 ? 0.3225 0.3682 0.3336 0.0059 -0.0026 0.0140 253 TYR A CD2 1969 C CE1 . TYR A 257 ? 0.2852 0.3364 0.2984 0.0004 -0.0040 0.0129 253 TYR A CE1 1970 C CE2 . TYR A 257 ? 0.3354 0.3773 0.3472 0.0020 -0.0036 0.0132 253 TYR A CE2 1971 C CZ . TYR A 257 ? 0.3149 0.3594 0.3277 -0.0007 -0.0042 0.0127 253 TYR A CZ 1972 O OH . TYR A 257 ? 0.3201 0.3605 0.3332 -0.0042 -0.0050 0.0122 253 TYR A OH 1973 N N . SER A 258 ? 0.3273 0.3887 0.3347 0.0238 0.0033 0.0201 254 SER A N 1974 C CA . SER A 258 ? 0.3301 0.3968 0.3353 0.0283 0.0038 0.0208 254 SER A CA 1975 C C . SER A 258 ? 0.3283 0.4007 0.3329 0.0322 0.0052 0.0225 254 SER A C 1976 O O . SER A 258 ? 0.3299 0.4012 0.3358 0.0316 0.0060 0.0231 254 SER A O 1977 C CB . SER A 258 ? 0.3306 0.3917 0.3347 0.0310 0.0057 0.0226 254 SER A CB 1978 O OG . SER A 258 ? 0.3190 0.3737 0.3241 0.0323 0.0086 0.0249 254 SER A OG 1979 N N . SER A 259 ? 0.3403 0.4195 0.3428 0.0365 0.0053 0.0231 255 SER A N 1980 C CA . SER A 259 ? 0.3464 0.4319 0.3477 0.0413 0.0067 0.0249 255 SER A CA 1981 C C . SER A 259 ? 0.3534 0.4359 0.3524 0.0473 0.0099 0.0284 255 SER A C 1982 O O . SER A 259 ? 0.3549 0.4334 0.3531 0.0478 0.0104 0.0287 255 SER A O 1983 C CB . SER A 259 ? 0.3458 0.4429 0.3462 0.0416 0.0042 0.0226 255 SER A CB 1984 O OG . SER A 259 ? 0.3227 0.4225 0.3253 0.0359 0.0017 0.0196 255 SER A OG 1985 N N . TRP A 260 ? 0.3614 0.4456 0.3593 0.0521 0.0124 0.0310 256 TRP A N 1986 C CA . TRP A 260 ? 0.3718 0.4539 0.3672 0.0583 0.0157 0.0345 256 TRP A CA 1987 C C . TRP A 260 ? 0.3866 0.4796 0.3794 0.0638 0.0155 0.0354 256 TRP A C 1988 O O . TRP A 260 ? 0.3897 0.4870 0.3829 0.0646 0.0155 0.0354 256 TRP A O 1989 C CB . TRP A 260 ? 0.3758 0.4487 0.3719 0.0596 0.0195 0.0372 256 TRP A CB 1990 C CG . TRP A 260 ? 0.3940 0.4643 0.3874 0.0660 0.0234 0.0411 256 TRP A CG 1991 C CD1 . TRP A 260 ? 0.4217 0.4914 0.4131 0.0686 0.0243 0.0424 256 TRP A CD1 1992 C CD2 . TRP A 260 ? 0.4031 0.4707 0.3953 0.0708 0.0273 0.0443 256 TRP A CD2 1993 N NE1 . TRP A 260 ? 0.4096 0.4763 0.3985 0.0748 0.0286 0.0464 256 TRP A NE1 1994 C CE2 . TRP A 260 ? 0.4346 0.4997 0.4240 0.0762 0.0306 0.0477 256 TRP A CE2 1995 C CE3 . TRP A 260 ? 0.4200 0.4868 0.4131 0.0712 0.0285 0.0447 256 TRP A CE3 1996 C CZ2 . TRP A 260 ? 0.4522 0.5135 0.4395 0.0821 0.0352 0.0517 256 TRP A CZ2 1997 C CZ3 . TRP A 260 ? 0.4451 0.5084 0.4364 0.0769 0.0329 0.0483 256 TRP A CZ3 1998 C CH2 . TRP A 260 ? 0.4621 0.5224 0.4504 0.0823 0.0363 0.0519 256 TRP A CH2 1999 N N . ASN A 261 ? 0.4076 0.5057 0.3979 0.0674 0.0152 0.0358 257 ASN A N 2000 C CA . ASN A 261 ? 0.4134 0.5234 0.4011 0.0727 0.0147 0.0363 257 ASN A CA 2001 C C . ASN A 261 ? 0.4309 0.5504 0.4203 0.0695 0.0114 0.0329 257 ASN A C 2002 O O . ASN A 261 ? 0.4259 0.5530 0.4143 0.0733 0.0118 0.0337 257 ASN A O 2003 C CB . ASN A 261 ? 0.4196 0.5278 0.4048 0.0800 0.0189 0.0410 257 ASN A CB 2004 C CG . ASN A 261 ? 0.3959 0.4956 0.3791 0.0834 0.0223 0.0444 257 ASN A CG 2005 O OD1 . ASN A 261 ? 0.3892 0.4897 0.3717 0.0828 0.0212 0.0435 257 ASN A OD1 2006 N ND2 . ASN A 261 ? 0.3949 0.4866 0.3773 0.0867 0.0266 0.0481 257 ASN A ND2 2007 N N . GLY A 262 ? 0.4153 0.5344 0.4073 0.0625 0.0083 0.0290 258 GLY A N 2008 C CA . GLY A 262 ? 0.3939 0.5217 0.3877 0.0588 0.0053 0.0255 258 GLY A CA 2009 C C . GLY A 262 ? 0.3993 0.5241 0.3956 0.0554 0.0055 0.0253 258 GLY A C 2010 O O . GLY A 262 ? 0.3915 0.5228 0.3895 0.0515 0.0030 0.0223 258 GLY A O 2011 N N . VAL A 263 ? 0.3784 0.4935 0.3750 0.0566 0.0084 0.0282 259 VAL A N 2012 C CA . VAL A 263 ? 0.3572 0.4691 0.3560 0.0536 0.0087 0.0280 259 VAL A CA 2013 C C . VAL A 263 ? 0.3523 0.4544 0.3536 0.0472 0.0080 0.0266 259 VAL A C 2014 O O . VAL A 263 ? 0.3514 0.4448 0.3524 0.0476 0.0097 0.0281 259 VAL A O 2015 C CB . VAL A 263 ? 0.3657 0.4732 0.3634 0.0588 0.0124 0.0317 259 VAL A CB 2016 C CG1 . VAL A 263 ? 0.3628 0.4661 0.3630 0.0553 0.0128 0.0312 259 VAL A CG1 2017 C CG2 . VAL A 263 ? 0.3779 0.4959 0.3728 0.0661 0.0133 0.0335 259 VAL A CG2 2018 N N . LYS A 264 ? 0.3298 0.4337 0.3333 0.0416 0.0056 0.0239 260 LYS A N 2019 C CA . LYS A 264 ? 0.3288 0.4241 0.3344 0.0358 0.0049 0.0226 260 LYS A CA 2020 C C . LYS A 264 ? 0.3158 0.4023 0.3222 0.0367 0.0077 0.0249 260 LYS A C 2021 O O . LYS A 264 ? 0.3197 0.4076 0.3263 0.0389 0.0092 0.0261 260 LYS A O 2022 C CB . LYS A 264 ? 0.3130 0.4128 0.3206 0.0304 0.0024 0.0198 260 LYS A CB 2023 C CG . LYS A 264 ? 0.3169 0.4248 0.3243 0.0282 -0.0003 0.0169 260 LYS A CG 2024 C CD . LYS A 264 ? 0.3204 0.4218 0.3284 0.0235 -0.0018 0.0151 260 LYS A CD 2025 C CE . LYS A 264 ? 0.3534 0.4624 0.3612 0.0213 -0.0042 0.0118 260 LYS A CE 2026 N NZ . LYS A 264 ? 0.3252 0.4268 0.3332 0.0174 -0.0052 0.0103 260 LYS A NZ 2027 N N . MET A 265 ? 0.3054 0.3829 0.3123 0.0354 0.0086 0.0254 261 MET A N 2028 C CA . MET A 265 ? 0.2981 0.3671 0.3062 0.0352 0.0111 0.0268 261 MET A CA 2029 C C . MET A 265 ? 0.3026 0.3718 0.3129 0.0316 0.0104 0.0256 261 MET A C 2030 O O . MET A 265 ? 0.2967 0.3626 0.3076 0.0331 0.0127 0.0268 261 MET A O 2031 C CB . MET A 265 ? 0.2852 0.3459 0.2940 0.0329 0.0115 0.0266 261 MET A CB 2032 C CG . MET A 265 ? 0.3122 0.3696 0.3192 0.0370 0.0137 0.0287 261 MET A CG 2033 S SD . MET A 265 ? 0.3443 0.4000 0.3498 0.0436 0.0182 0.0323 261 MET A SD 2034 C CE . MET A 265 ? 0.3117 0.3612 0.3199 0.0412 0.0200 0.0321 261 MET A CE 2035 N N . HIS A 266 ? 0.2843 0.3565 0.2957 0.0268 0.0074 0.0232 262 HIS A N 2036 C CA . HIS A 266 ? 0.2747 0.3474 0.2881 0.0232 0.0066 0.0221 262 HIS A CA 2037 C C . HIS A 266 ? 0.2920 0.3720 0.3052 0.0258 0.0071 0.0225 262 HIS A C 2038 O O . HIS A 266 ? 0.2930 0.3740 0.3076 0.0238 0.0069 0.0219 262 HIS A O 2039 C CB . HIS A 266 ? 0.2827 0.3567 0.2970 0.0177 0.0037 0.0197 262 HIS A CB 2040 C CG . HIS A 266 ? 0.2903 0.3563 0.3051 0.0148 0.0034 0.0192 262 HIS A CG 2041 N ND1 . HIS A 266 ? 0.3216 0.3833 0.3379 0.0111 0.0030 0.0186 262 HIS A ND1 2042 C CD2 . HIS A 266 ? 0.2704 0.3321 0.2843 0.0154 0.0035 0.0194 262 HIS A CD2 2043 C CE1 . HIS A 266 ? 0.2645 0.3199 0.2808 0.0096 0.0028 0.0184 262 HIS A CE1 2044 N NE2 . HIS A 266 ? 0.3343 0.3895 0.3492 0.0120 0.0031 0.0188 262 HIS A NE2 2045 N N . ALA A 267 ? 0.3011 0.3867 0.3124 0.0305 0.0077 0.0236 263 ALA A N 2046 C CA . ALA A 267 ? 0.3135 0.4064 0.3243 0.0336 0.0083 0.0242 263 ALA A CA 2047 C C . ALA A 267 ? 0.3267 0.4174 0.3357 0.0401 0.0116 0.0271 263 ALA A C 2048 O O . ALA A 267 ? 0.3356 0.4326 0.3435 0.0442 0.0124 0.0281 263 ALA A O 2049 C CB . ALA A 267 ? 0.3252 0.4298 0.3354 0.0333 0.0057 0.0224 263 ALA A CB 2050 N N . ASN A 268 ? 0.3192 0.4011 0.3278 0.0414 0.0137 0.0286 264 ASN A N 2051 C CA . ASN A 268 ? 0.3239 0.4029 0.3305 0.0477 0.0173 0.0317 264 ASN A CA 2052 C C . ASN A 268 ? 0.3368 0.4090 0.3442 0.0489 0.0205 0.0329 264 ASN A C 2053 O O . ASN A 268 ? 0.3287 0.3919 0.3373 0.0474 0.0224 0.0332 264 ASN A O 2054 C CB . ASN A 268 ? 0.3399 0.4139 0.3451 0.0491 0.0183 0.0329 264 ASN A CB 2055 C CG . ASN A 268 ? 0.3719 0.4456 0.3742 0.0565 0.0218 0.0363 264 ASN A CG 2056 O OD1 . ASN A 268 ? 0.3679 0.4392 0.3698 0.0596 0.0246 0.0381 264 ASN A OD1 2057 N ND2 . ASN A 268 ? 0.3443 0.4202 0.3444 0.0592 0.0217 0.0373 264 ASN A ND2 2058 N N . GLN A 269 ? 0.3318 0.4088 0.3388 0.0518 0.0212 0.0335 265 GLN A N 2059 C CA . GLN A 269 ? 0.3396 0.4109 0.3474 0.0529 0.0242 0.0343 265 GLN A CA 2060 C C . GLN A 269 ? 0.3521 0.4155 0.3584 0.0577 0.0286 0.0372 265 GLN A C 2061 O O . GLN A 269 ? 0.3513 0.4061 0.3589 0.0567 0.0312 0.0373 265 GLN A O 2062 C CB . GLN A 269 ? 0.3513 0.4307 0.3587 0.0555 0.0239 0.0343 265 GLN A CB 2063 C CG . GLN A 269 ? 0.3426 0.4171 0.3512 0.0558 0.0263 0.0344 265 GLN A CG 2064 C CD . GLN A 269 ? 0.4488 0.5319 0.4566 0.0591 0.0261 0.0346 265 GLN A CD 2065 O OE1 . GLN A 269 ? 0.4715 0.5599 0.4810 0.0557 0.0237 0.0325 265 GLN A OE1 2066 N NE2 . GLN A 269 ? 0.4779 0.5628 0.4829 0.0659 0.0285 0.0372 265 GLN A NE2 2067 N N . ASP A 270 ? 0.3582 0.4245 0.3614 0.0629 0.0295 0.0395 266 ASP A N 2068 C CA . ASP A 270 ? 0.3792 0.4381 0.3806 0.0679 0.0341 0.0427 266 ASP A CA 2069 C C . ASP A 270 ? 0.3733 0.4218 0.3764 0.0641 0.0354 0.0423 266 ASP A C 2070 O O . ASP A 270 ? 0.3612 0.4007 0.3647 0.0652 0.0394 0.0435 266 ASP A O 2071 C CB . ASP A 270 ? 0.4024 0.4672 0.4002 0.0735 0.0342 0.0450 266 ASP A CB 2072 C CG . ASP A 270 ? 0.4862 0.5598 0.4816 0.0792 0.0344 0.0464 266 ASP A CG 2073 O OD1 . ASP A 270 ? 0.5706 0.6514 0.5632 0.0837 0.0339 0.0479 266 ASP A OD1 2074 O OD2 . ASP A 270 ? 0.5373 0.6114 0.5337 0.0794 0.0351 0.0459 266 ASP A OD2 2075 N N . LEU A 271 ? 0.3434 0.3936 0.3475 0.0599 0.0322 0.0404 267 LEU A N 2076 C CA . LEU A 271 ? 0.3445 0.3862 0.3502 0.0565 0.0331 0.0399 267 LEU A CA 2077 C C . LEU A 271 ? 0.3418 0.3788 0.3510 0.0508 0.0326 0.0372 267 LEU A C 2078 O O . LEU A 271 ? 0.3516 0.3803 0.3622 0.0498 0.0354 0.0373 267 LEU A O 2079 C CB . LEU A 271 ? 0.3221 0.3671 0.3271 0.0548 0.0301 0.0391 267 LEU A CB 2080 C CG . LEU A 271 ? 0.3557 0.4026 0.3573 0.0604 0.0317 0.0419 267 LEU A CG 2081 C CD1 . LEU A 271 ? 0.3495 0.3994 0.3508 0.0582 0.0286 0.0405 267 LEU A CD1 2082 C CD2 . LEU A 271 ? 0.3938 0.4312 0.3947 0.0638 0.0370 0.0448 267 LEU A CD2 2083 N N . VAL A 272 ? 0.3412 0.3837 0.3518 0.0471 0.0290 0.0348 268 VAL A N 2084 C CA . VAL A 272 ? 0.3341 0.3730 0.3478 0.0419 0.0282 0.0324 268 VAL A CA 2085 C C . VAL A 272 ? 0.3429 0.3778 0.3576 0.0432 0.0314 0.0326 268 VAL A C 2086 O O . VAL A 272 ? 0.3238 0.3518 0.3406 0.0409 0.0333 0.0316 268 VAL A O 2087 C CB . VAL A 272 ? 0.3252 0.3710 0.3399 0.0376 0.0238 0.0300 268 VAL A CB 2088 C CG1 . VAL A 272 ? 0.3404 0.3831 0.3580 0.0328 0.0231 0.0277 268 VAL A CG1 2089 C CG2 . VAL A 272 ? 0.3383 0.3868 0.3522 0.0357 0.0208 0.0294 268 VAL A CG2 2090 N N . THR A 273 ? 0.3216 0.3612 0.3350 0.0468 0.0320 0.0336 269 THR A N 2091 C CA . THR A 273 ? 0.3282 0.3641 0.3424 0.0482 0.0350 0.0336 269 THR A CA 2092 C C . THR A 273 ? 0.3427 0.3721 0.3552 0.0535 0.0399 0.0364 269 THR A C 2093 O O . THR A 273 ? 0.3537 0.3748 0.3677 0.0530 0.0434 0.0361 269 THR A O 2094 C CB . THR A 273 ? 0.3341 0.3784 0.3477 0.0497 0.0334 0.0332 269 THR A CB 2095 O OG1 . THR A 273 ? 0.3458 0.3953 0.3613 0.0443 0.0292 0.0306 269 THR A OG1 2096 C CG2 . THR A 273 ? 0.3442 0.3842 0.3586 0.0516 0.0368 0.0332 269 THR A CG2 2097 N N . GLY A 274 ? 0.3428 0.3760 0.3522 0.0586 0.0404 0.0391 270 GLY A N 2098 C CA . GLY A 274 ? 0.3701 0.3974 0.3770 0.0647 0.0455 0.0425 270 GLY A CA 2099 C C . GLY A 274 ? 0.3936 0.4115 0.4014 0.0634 0.0483 0.0431 270 GLY A C 2100 O O . GLY A 274 ? 0.3998 0.4090 0.4077 0.0652 0.0531 0.0442 270 GLY A O 2101 N N . TYR A 275 ? 0.3603 0.3797 0.3686 0.0602 0.0456 0.0422 271 TYR A N 2102 C CA . TYR A 275 ? 0.3573 0.3683 0.3663 0.0591 0.0482 0.0428 271 TYR A CA 2103 C C . TYR A 275 ? 0.3477 0.3537 0.3607 0.0526 0.0477 0.0394 271 TYR A C 2104 O O . TYR A 275 ? 0.3555 0.3535 0.3703 0.0519 0.0516 0.0391 271 TYR A O 2105 C CB . TYR A 275 ? 0.3434 0.3577 0.3503 0.0605 0.0467 0.0442 271 TYR A CB 2106 C CG . TYR A 275 ? 0.3867 0.3923 0.3934 0.0617 0.0509 0.0461 271 TYR A CG 2107 C CD1 . TYR A 275 ? 0.4179 0.4187 0.4221 0.0675 0.0560 0.0497 271 TYR A CD1 2108 C CD2 . TYR A 275 ? 0.3681 0.3698 0.3772 0.0568 0.0502 0.0442 271 TYR A CD2 2109 C CE1 . TYR A 275 ? 0.4168 0.4094 0.4208 0.0683 0.0602 0.0515 271 TYR A CE1 2110 C CE2 . TYR A 275 ? 0.3732 0.3674 0.3824 0.0575 0.0542 0.0457 271 TYR A CE2 2111 C CZ . TYR A 275 ? 0.4217 0.4113 0.4284 0.0631 0.0592 0.0494 271 TYR A CZ 2112 O OH . TYR A 275 ? 0.4268 0.4087 0.4337 0.0636 0.0635 0.0509 271 TYR A OH 2113 N N . LEU A 276 ? 0.3323 0.3431 0.3469 0.0479 0.0431 0.0368 272 LEU A N 2114 C CA . LEU A 276 ? 0.3288 0.3355 0.3468 0.0423 0.0425 0.0339 272 LEU A CA 2115 C C . LEU A 276 ? 0.3288 0.3324 0.3492 0.0409 0.0444 0.0322 272 LEU A C 2116 O O . LEU A 276 ? 0.3310 0.3277 0.3536 0.0391 0.0475 0.0311 272 LEU A O 2117 C CB . LEU A 276 ? 0.3204 0.3332 0.3391 0.0381 0.0372 0.0318 272 LEU A CB 2118 C CG . LEU A 276 ? 0.3235 0.3340 0.3454 0.0325 0.0356 0.0287 272 LEU A CG 2119 C CD1 . LEU A 276 ? 0.3155 0.3192 0.3386 0.0317 0.0383 0.0288 272 LEU A CD1 2120 C CD2 . LEU A 276 ? 0.3122 0.3287 0.3338 0.0294 0.0306 0.0274 272 LEU A CD2 2121 N N . LYS A 277 ? 0.3336 0.3426 0.3537 0.0412 0.0425 0.0315 273 LYS A N 2122 C CA . LYS A 277 ? 0.3262 0.3329 0.3483 0.0400 0.0442 0.0297 273 LYS A CA 2123 C C . LYS A 277 ? 0.3624 0.3626 0.3836 0.0444 0.0496 0.0315 273 LYS A C 2124 O O . LYS A 277 ? 0.3753 0.3687 0.3989 0.0426 0.0529 0.0299 273 LYS A O 2125 C CB . LYS A 277 ? 0.3249 0.3394 0.3470 0.0391 0.0407 0.0284 273 LYS A CB 2126 C CG . LYS A 277 ? 0.2750 0.2943 0.2985 0.0339 0.0358 0.0262 273 LYS A CG 2127 C CD . LYS A 277 ? 0.3052 0.3320 0.3288 0.0327 0.0328 0.0251 273 LYS A CD 2128 C CE . LYS A 277 ? 0.3235 0.3530 0.3487 0.0272 0.0288 0.0228 273 LYS A CE 2129 N NZ . LYS A 277 ? 0.3363 0.3720 0.3619 0.0259 0.0267 0.0216 273 LYS A NZ 2130 N N . ASP A 278 ? 0.3705 0.3732 0.3885 0.0499 0.0507 0.0345 274 ASP A N 2131 C CA . ASP A 278 ? 0.4081 0.4049 0.4250 0.0545 0.0559 0.0363 274 ASP A CA 2132 C C . ASP A 278 ? 0.4311 0.4186 0.4473 0.0568 0.0611 0.0386 274 ASP A C 2133 O O . ASP A 278 ? 0.4645 0.4445 0.4805 0.0592 0.0661 0.0394 274 ASP A O 2134 C CB . ASP A 278 ? 0.4075 0.4107 0.4209 0.0603 0.0555 0.0389 274 ASP A CB 2135 C CG . ASP A 278 ? 0.4481 0.4597 0.4624 0.0584 0.0516 0.0367 274 ASP A CG 2136 O OD1 . ASP A 278 ? 0.4909 0.5028 0.5083 0.0530 0.0495 0.0334 274 ASP A OD1 2137 O OD2 . ASP A 278 ? 0.4615 0.4800 0.4734 0.0626 0.0506 0.0383 274 ASP A OD2 2138 N N . THR A 279 ? 0.4103 0.3980 0.4256 0.0564 0.0602 0.0399 275 THR A N 2139 C CA . THR A 279 ? 0.4276 0.4072 0.4419 0.0590 0.0650 0.0425 275 THR A CA 2140 C C . THR A 279 ? 0.4242 0.3986 0.4420 0.0534 0.0655 0.0399 275 THR A C 2141 O O . THR A 279 ? 0.4290 0.3947 0.4483 0.0528 0.0704 0.0396 275 THR A O 2142 C CB . THR A 279 ? 0.4226 0.4060 0.4328 0.0639 0.0645 0.0463 275 THR A CB 2143 O OG1 . THR A 279 ? 0.4428 0.4325 0.4499 0.0690 0.0636 0.0482 275 THR A OG1 2144 C CG2 . THR A 279 ? 0.4392 0.4138 0.4478 0.0672 0.0702 0.0496 275 THR A CG2 2145 N N . LEU A 280 ? 0.3895 0.3691 0.4086 0.0492 0.0608 0.0379 276 LEU A N 2146 C CA . LEU A 280 ? 0.3896 0.3653 0.4122 0.0438 0.0608 0.0351 276 LEU A CA 2147 C C . LEU A 280 ? 0.3767 0.3510 0.4030 0.0394 0.0607 0.0311 276 LEU A C 2148 O O . LEU A 280 ? 0.3869 0.3582 0.4164 0.0351 0.0613 0.0284 276 LEU A O 2149 C CB . LEU A 280 ? 0.3814 0.3627 0.4040 0.0411 0.0560 0.0342 276 LEU A CB 2150 C CG . LEU A 280 ? 0.4359 0.4184 0.4551 0.0449 0.0560 0.0376 276 LEU A CG 2151 C CD1 . LEU A 280 ? 0.4195 0.4072 0.4390 0.0418 0.0511 0.0362 276 LEU A CD1 2152 C CD2 . LEU A 280 ? 0.4804 0.4547 0.4993 0.0472 0.0618 0.0399 276 LEU A CD2 2153 N N . LYS A 281 ? 0.3595 0.3371 0.3855 0.0404 0.0598 0.0305 277 LYS A N 2154 C CA . LYS A 281 ? 0.3617 0.3388 0.3910 0.0367 0.0596 0.0267 277 LYS A CA 2155 C C . LYS A 281 ? 0.3437 0.3255 0.3755 0.0311 0.0550 0.0233 277 LYS A C 2156 O O . LYS A 281 ? 0.3296 0.3100 0.3647 0.0273 0.0554 0.0199 277 LYS A O 2157 C CB . LYS A 281 ? 0.3869 0.3545 0.4183 0.0363 0.0656 0.0257 277 LYS A CB 2158 C CG . LYS A 281 ? 0.4346 0.3963 0.4630 0.0423 0.0709 0.0294 277 LYS A CG 2159 C CD . LYS A 281 ? 0.4974 0.4635 0.5236 0.0461 0.0698 0.0305 277 LYS A CD 2160 C CE . LYS A 281 ? 0.5482 0.5080 0.5713 0.0525 0.0754 0.0343 277 LYS A CE 2161 N NZ . LYS A 281 ? 0.5505 0.5158 0.5711 0.0566 0.0740 0.0355 277 LYS A NZ 2162 N N . PHE A 282 ? 0.3300 0.3176 0.3603 0.0307 0.0507 0.0242 278 PHE A N 2163 C CA . PHE A 282 ? 0.3286 0.3207 0.3608 0.0260 0.0463 0.0214 278 PHE A CA 2164 C C . PHE A 282 ? 0.3183 0.3144 0.3519 0.0240 0.0444 0.0190 278 PHE A C 2165 O O . PHE A 282 ? 0.3337 0.3337 0.3656 0.0264 0.0435 0.0201 278 PHE A O 2166 C CB . PHE A 282 ? 0.3083 0.3059 0.3381 0.0264 0.0422 0.0230 278 PHE A CB 2167 C CG . PHE A 282 ? 0.3204 0.3220 0.3516 0.0220 0.0379 0.0207 278 PHE A CG 2168 C CD1 . PHE A 282 ? 0.3239 0.3227 0.3577 0.0186 0.0382 0.0184 278 PHE A CD1 2169 C CD2 . PHE A 282 ? 0.2829 0.2912 0.3128 0.0214 0.0337 0.0207 278 PHE A CD2 2170 C CE1 . PHE A 282 ? 0.2881 0.2906 0.3228 0.0150 0.0342 0.0165 278 PHE A CE1 2171 C CE2 . PHE A 282 ? 0.2780 0.2894 0.3088 0.0175 0.0300 0.0188 278 PHE A CE2 2172 C CZ . PHE A 282 ? 0.2845 0.2928 0.3176 0.0145 0.0303 0.0168 278 PHE A CZ 2173 N N . LYS A 283 ? 0.3077 0.3035 0.3444 0.0198 0.0438 0.0156 279 LYS A N 2174 C CA . LYS A 283 ? 0.3063 0.3059 0.3444 0.0180 0.0422 0.0131 279 LYS A CA 2175 C C . LYS A 283 ? 0.2967 0.3017 0.3357 0.0141 0.0377 0.0112 279 LYS A C 2176 O O . LYS A 283 ? 0.2973 0.3059 0.3376 0.0121 0.0362 0.0090 279 LYS A O 2177 C CB . LYS A 283 ? 0.3188 0.3135 0.3600 0.0167 0.0462 0.0102 279 LYS A CB 2178 C CG . LYS A 283 ? 0.3751 0.3633 0.4153 0.0206 0.0514 0.0120 279 LYS A CG 2179 C CD . LYS A 283 ? 0.4090 0.4005 0.4469 0.0241 0.0509 0.0137 279 LYS A CD 2180 C CE . LYS A 283 ? 0.4548 0.4392 0.4919 0.0282 0.0565 0.0151 279 LYS A CE 2181 N NZ . LYS A 283 ? 0.4772 0.4652 0.5107 0.0330 0.0559 0.0183 279 LYS A NZ 2182 N N . GLY A 284 ? 0.2833 0.2888 0.3215 0.0132 0.0356 0.0121 280 GLY A N 2183 C CA . GLY A 284 ? 0.2858 0.2960 0.3244 0.0100 0.0314 0.0108 280 GLY A CA 2184 C C . GLY A 284 ? 0.2890 0.3045 0.3249 0.0111 0.0283 0.0127 280 GLY A C 2185 O O . GLY A 284 ? 0.2896 0.3060 0.3242 0.0139 0.0294 0.0142 280 GLY A O 2186 N N . PHE A 285 ? 0.2615 0.2803 0.2966 0.0090 0.0246 0.0127 281 PHE A N 2187 C CA . PHE A 285 ? 0.2782 0.3021 0.3111 0.0096 0.0219 0.0141 281 PHE A CA 2188 C C . PHE A 285 ? 0.2838 0.3078 0.3146 0.0107 0.0206 0.0161 281 PHE A C 2189 O O . PHE A 285 ? 0.2924 0.3136 0.3233 0.0099 0.0205 0.0160 281 PHE A O 2190 C CB . PHE A 285 ? 0.2598 0.2883 0.2931 0.0066 0.0190 0.0128 281 PHE A CB 2191 C CG . PHE A 285 ? 0.2674 0.2960 0.3010 0.0037 0.0165 0.0120 281 PHE A CG 2192 C CD1 . PHE A 285 ? 0.2630 0.2927 0.2945 0.0032 0.0140 0.0133 281 PHE A CD1 2193 C CD2 . PHE A 285 ? 0.2654 0.2935 0.3009 0.0015 0.0164 0.0098 281 PHE A CD2 2194 C CE1 . PHE A 285 ? 0.2760 0.3054 0.3074 0.0008 0.0118 0.0127 281 PHE A CE1 2195 C CE2 . PHE A 285 ? 0.2194 0.2481 0.2547 -0.0007 0.0141 0.0092 281 PHE A CE2 2196 C CZ . PHE A 285 ? 0.2461 0.2750 0.2792 -0.0010 0.0118 0.0108 281 PHE A CZ 2197 N N . VAL A 286 ? 0.2782 0.3063 0.3071 0.0125 0.0196 0.0176 282 VAL A N 2198 C CA . VAL A 286 ? 0.2724 0.3021 0.2991 0.0136 0.0182 0.0191 282 VAL A CA 2199 C C . VAL A 286 ? 0.2782 0.3124 0.3042 0.0107 0.0145 0.0185 282 VAL A C 2200 O O . VAL A 286 ? 0.2821 0.3206 0.3081 0.0098 0.0133 0.0181 282 VAL A O 2201 C CB . VAL A 286 ? 0.2811 0.3134 0.3060 0.0177 0.0195 0.0210 282 VAL A CB 2202 C CG1 . VAL A 286 ? 0.2626 0.2983 0.2852 0.0186 0.0175 0.0221 282 VAL A CG1 2203 C CG2 . VAL A 286 ? 0.2487 0.2756 0.2737 0.0211 0.0237 0.0221 282 VAL A CG2 2204 N N . ILE A 287 ? 0.2566 0.2894 0.2819 0.0093 0.0128 0.0184 283 ILE A N 2205 C CA . ILE A 287 ? 0.2457 0.2816 0.2703 0.0064 0.0097 0.0178 283 ILE A CA 2206 C C . ILE A 287 ? 0.2619 0.3002 0.2845 0.0072 0.0083 0.0185 283 ILE A C 2207 O O . ILE A 287 ? 0.2466 0.2829 0.2684 0.0095 0.0094 0.0194 283 ILE A O 2208 C CB . ILE A 287 ? 0.2457 0.2782 0.2711 0.0034 0.0086 0.0166 283 ILE A CB 2209 C CG1 . ILE A 287 ? 0.2266 0.2614 0.2511 0.0005 0.0058 0.0163 283 ILE A CG1 2210 C CG2 . ILE A 287 ? 0.2307 0.2587 0.2560 0.0043 0.0094 0.0168 283 ILE A CG2 2211 C CD1 . ILE A 287 ? 0.2342 0.2661 0.2593 -0.0019 0.0049 0.0153 283 ILE A CD1 2212 N N . SER A 288 ? 0.2681 0.3111 0.2900 0.0053 0.0061 0.0181 284 SER A N 2213 C CA . SER A 288 ? 0.2626 0.3082 0.2829 0.0055 0.0046 0.0182 284 SER A CA 2214 C C . SER A 288 ? 0.2775 0.3189 0.2972 0.0038 0.0035 0.0177 284 SER A C 2215 O O . SER A 288 ? 0.2751 0.3127 0.2956 0.0018 0.0032 0.0172 284 SER A O 2216 C CB . SER A 288 ? 0.2707 0.3223 0.2908 0.0032 0.0027 0.0174 284 SER A CB 2217 O OG . SER A 288 ? 0.2689 0.3189 0.2891 -0.0008 0.0010 0.0165 284 SER A OG 2218 N N . ASP A 289 ? 0.2620 0.3049 0.2802 0.0044 0.0025 0.0176 285 ASP A N 2219 C CA . ASP A 289 ? 0.2762 0.3160 0.2937 0.0022 0.0010 0.0167 285 ASP A CA 2220 C C . ASP A 289 ? 0.2685 0.3108 0.2858 -0.0015 -0.0011 0.0156 285 ASP A C 2221 O O . ASP A 289 ? 0.2742 0.3209 0.2922 -0.0024 -0.0012 0.0155 285 ASP A O 2222 C CB . ASP A 289 ? 0.2654 0.3054 0.2814 0.0045 0.0010 0.0169 285 ASP A CB 2223 C CG . ASP A 289 ? 0.2939 0.3286 0.3093 0.0034 0.0003 0.0164 285 ASP A CG 2224 O OD1 . ASP A 289 ? 0.3056 0.3377 0.3212 0.0004 -0.0008 0.0157 285 ASP A OD1 2225 O OD2 . ASP A 289 ? 0.3219 0.3554 0.3364 0.0057 0.0009 0.0167 285 ASP A OD2 2226 N N . TRP A 290 ? 0.2563 0.2955 0.2728 -0.0037 -0.0023 0.0149 286 TRP A N 2227 C CA . TRP A 290 ? 0.2655 0.3048 0.2817 -0.0076 -0.0039 0.0140 286 TRP A CA 2228 C C . TRP A 290 ? 0.2765 0.3220 0.2924 -0.0087 -0.0048 0.0129 286 TRP A C 2229 O O . TRP A 290 ? 0.2833 0.3299 0.2982 -0.0082 -0.0054 0.0120 286 TRP A O 2230 C CB . TRP A 290 ? 0.2495 0.2832 0.2646 -0.0088 -0.0046 0.0135 286 TRP A CB 2231 C CG . TRP A 290 ? 0.2718 0.3039 0.2859 -0.0125 -0.0059 0.0126 286 TRP A CG 2232 C CD1 . TRP A 290 ? 0.2898 0.3243 0.3033 -0.0146 -0.0069 0.0112 286 TRP A CD1 2233 C CD2 . TRP A 290 ? 0.2509 0.2783 0.2648 -0.0145 -0.0061 0.0131 286 TRP A CD2 2234 N NE1 . TRP A 290 ? 0.2676 0.2985 0.2804 -0.0180 -0.0074 0.0108 286 TRP A NE1 2235 C CE2 . TRP A 290 ? 0.2806 0.3069 0.2933 -0.0177 -0.0069 0.0122 286 TRP A CE2 2236 C CE3 . TRP A 290 ? 0.2541 0.2782 0.2684 -0.0137 -0.0055 0.0141 286 TRP A CE3 2237 C CZ2 . TRP A 290 ? 0.3285 0.3501 0.3403 -0.0199 -0.0071 0.0128 286 TRP A CZ2 2238 C CZ3 . TRP A 290 ? 0.2973 0.3176 0.3106 -0.0158 -0.0059 0.0145 286 TRP A CZ3 2239 C CH2 . TRP A 290 ? 0.3196 0.3384 0.3316 -0.0186 -0.0066 0.0141 286 TRP A CH2 2240 N N . GLU A 291 ? 0.2658 0.3156 0.2824 -0.0104 -0.0049 0.0128 287 GLU A N 2241 C CA . GLU A 291 ? 0.2723 0.3296 0.2891 -0.0112 -0.0056 0.0116 287 GLU A CA 2242 C C . GLU A 291 ? 0.2717 0.3332 0.2881 -0.0070 -0.0051 0.0119 287 GLU A C 2243 O O . GLU A 291 ? 0.2592 0.3267 0.2752 -0.0068 -0.0058 0.0106 287 GLU A O 2244 C CB . GLU A 291 ? 0.2779 0.3349 0.2939 -0.0147 -0.0070 0.0098 287 GLU A CB 2245 C CG . GLU A 291 ? 0.3120 0.3636 0.3278 -0.0185 -0.0072 0.0098 287 GLU A CG 2246 C CD . GLU A 291 ? 0.3984 0.4479 0.4133 -0.0219 -0.0081 0.0080 287 GLU A CD 2247 O OE1 . GLU A 291 ? 0.4239 0.4745 0.4382 -0.0209 -0.0086 0.0067 287 GLU A OE1 2248 O OE2 . GLU A 291 ? 0.4383 0.4850 0.4531 -0.0253 -0.0081 0.0080 287 GLU A OE2 2249 N N . GLY A 292 ? 0.2670 0.3257 0.2835 -0.0035 -0.0036 0.0135 288 GLY A N 2250 C CA . GLY A 292 ? 0.2828 0.3449 0.2987 0.0010 -0.0025 0.0143 288 GLY A CA 2251 C C . GLY A 292 ? 0.2972 0.3679 0.3133 0.0022 -0.0025 0.0141 288 GLY A C 2252 O O . GLY A 292 ? 0.2935 0.3697 0.3087 0.0048 -0.0027 0.0139 288 GLY A O 2253 N N . ILE A 293 ? 0.2850 0.3575 0.3024 0.0005 -0.0024 0.0142 289 ILE A N 2254 C CA . ILE A 293 ? 0.2861 0.3673 0.3038 0.0019 -0.0024 0.0141 289 ILE A CA 2255 C C . ILE A 293 ? 0.2919 0.3800 0.3095 -0.0008 -0.0042 0.0119 289 ILE A C 2256 O O . ILE A 293 ? 0.2935 0.3896 0.3107 0.0015 -0.0044 0.0115 289 ILE A O 2257 C CB . ILE A 293 ? 0.2917 0.3733 0.3106 0.0014 -0.0016 0.0147 289 ILE A CB 2258 C CG1 . ILE A 293 ? 0.2833 0.3650 0.3032 -0.0039 -0.0029 0.0136 289 ILE A CG1 2259 C CG2 . ILE A 293 ? 0.2820 0.3563 0.3011 0.0038 0.0003 0.0163 289 ILE A CG2 2260 C CD1 . ILE A 293 ? 0.3157 0.3998 0.3368 -0.0042 -0.0022 0.0141 289 ILE A CD1 2261 N N . ASP A 294 ? 0.2953 0.3802 0.3132 -0.0055 -0.0054 0.0106 290 ASP A N 2262 C CA . ASP A 294 ? 0.2989 0.3892 0.3169 -0.0088 -0.0069 0.0082 290 ASP A CA 2263 C C . ASP A 294 ? 0.3236 0.4180 0.3405 -0.0061 -0.0074 0.0072 290 ASP A C 2264 O O . ASP A 294 ? 0.3118 0.4149 0.3289 -0.0068 -0.0083 0.0052 290 ASP A O 2265 C CB . ASP A 294 ? 0.3132 0.3969 0.3311 -0.0136 -0.0077 0.0071 290 ASP A CB 2266 C CG . ASP A 294 ? 0.3413 0.4197 0.3600 -0.0159 -0.0071 0.0084 290 ASP A CG 2267 O OD1 . ASP A 294 ? 0.3070 0.3817 0.3257 -0.0133 -0.0061 0.0103 290 ASP A OD1 2268 O OD2 . ASP A 294 ? 0.3602 0.4381 0.3793 -0.0203 -0.0076 0.0076 290 ASP A OD2 2269 N N . ARG A 295 ? 0.3123 0.4007 0.3279 -0.0033 -0.0068 0.0083 291 ARG A N 2270 C CA . ARG A 295 ? 0.3415 0.4329 0.3558 -0.0005 -0.0072 0.0076 291 ARG A CA 2271 C C . ARG A 295 ? 0.3562 0.4543 0.3697 0.0051 -0.0062 0.0089 291 ARG A C 2272 O O . ARG A 295 ? 0.3675 0.4684 0.3796 0.0080 -0.0064 0.0086 291 ARG A O 2273 C CB . ARG A 295 ? 0.3274 0.4096 0.3407 0.0000 -0.0068 0.0083 291 ARG A CB 2274 C CG . ARG A 295 ? 0.3393 0.4164 0.3530 -0.0053 -0.0080 0.0066 291 ARG A CG 2275 C CD . ARG A 295 ? 0.3277 0.3958 0.3403 -0.0049 -0.0078 0.0071 291 ARG A CD 2276 N NE . ARG A 295 ? 0.3483 0.4099 0.3613 -0.0092 -0.0082 0.0067 291 ARG A NE 2277 C CZ . ARG A 295 ? 0.3662 0.4199 0.3784 -0.0097 -0.0082 0.0070 291 ARG A CZ 2278 N NH1 . ARG A 295 ? 0.3883 0.4398 0.3995 -0.0065 -0.0079 0.0075 291 ARG A NH1 2279 N NH2 . ARG A 295 ? 0.3359 0.3842 0.3483 -0.0132 -0.0085 0.0069 291 ARG A NH2 2280 N N . ILE A 296 ? 0.3620 0.4627 0.3761 0.0067 -0.0052 0.0103 292 ILE A N 2281 C CA . ILE A 296 ? 0.3629 0.4713 0.3761 0.0122 -0.0043 0.0114 292 ILE A CA 2282 C C . ILE A 296 ? 0.3775 0.4972 0.3906 0.0119 -0.0060 0.0089 292 ILE A C 2283 O O . ILE A 296 ? 0.3481 0.4738 0.3596 0.0165 -0.0057 0.0093 292 ILE A O 2284 C CB . ILE A 296 ? 0.3628 0.4721 0.3768 0.0136 -0.0030 0.0131 292 ILE A CB 2285 C CG1 . ILE A 296 ? 0.3345 0.4336 0.3484 0.0155 -0.0009 0.0156 292 ILE A CG1 2286 C CG2 . ILE A 296 ? 0.3719 0.4907 0.3850 0.0188 -0.0023 0.0139 292 ILE A CG2 2287 C CD1 . ILE A 296 ? 0.3325 0.4305 0.3478 0.0151 0.0002 0.0165 292 ILE A CD1 2288 N N . THR A 297 ? 0.3757 0.4984 0.3904 0.0063 -0.0075 0.0063 293 THR A N 2289 C CA . THR A 297 ? 0.4003 0.5343 0.4155 0.0049 -0.0090 0.0033 293 THR A CA 2290 C C . THR A 297 ? 0.4250 0.5581 0.4398 0.0021 -0.0104 0.0006 293 THR A C 2291 O O . THR A 297 ? 0.4106 0.5339 0.4251 0.0000 -0.0103 0.0008 293 THR A O 2292 C CB . THR A 297 ? 0.3840 0.5225 0.4013 -0.0001 -0.0097 0.0016 293 THR A CB 2293 O OG1 . THR A 297 ? 0.3597 0.4898 0.3780 -0.0059 -0.0101 0.0007 293 THR A OG1 2294 C CG2 . THR A 297 ? 0.3802 0.5195 0.3980 0.0025 -0.0084 0.0041 293 THR A CG2 2295 N N . THR A 298 ? 0.4640 0.6081 0.4789 0.0021 -0.0116 -0.0023 294 THR A N 2296 C CA . THR A 298 ? 0.4948 0.6400 0.5096 -0.0009 -0.0130 -0.0057 294 THR A CA 2297 C C . THR A 298 ? 0.4916 0.6460 0.5086 -0.0060 -0.0142 -0.0096 294 THR A C 2298 O O . THR A 298 ? 0.5092 0.6752 0.5267 -0.0040 -0.0145 -0.0104 294 THR A O 2299 C CB . THR A 298 ? 0.5057 0.6568 0.5185 0.0049 -0.0131 -0.0056 294 THR A CB 2300 O OG1 . THR A 298 ? 0.5515 0.6934 0.5625 0.0092 -0.0117 -0.0019 294 THR A OG1 2301 C CG2 . THR A 298 ? 0.5323 0.6864 0.5451 0.0019 -0.0147 -0.0098 294 THR A CG2 2302 N N . PRO A 299 ? 0.4844 0.6335 0.5027 -0.0126 -0.0147 -0.0120 295 PRO A N 2303 C CA . PRO A 299 ? 0.4625 0.5975 0.4801 -0.0150 -0.0142 -0.0107 295 PRO A CA 2304 C C . PRO A 299 ? 0.4465 0.5734 0.4643 -0.0143 -0.0129 -0.0068 295 PRO A C 2305 O O . PRO A 299 ? 0.4276 0.5592 0.4462 -0.0133 -0.0124 -0.0055 295 PRO A O 2306 C CB . PRO A 299 ? 0.4746 0.6084 0.4938 -0.0223 -0.0148 -0.0143 295 PRO A CB 2307 C CG . PRO A 299 ? 0.4936 0.6406 0.5148 -0.0243 -0.0153 -0.0171 295 PRO A CG 2308 C CD . PRO A 299 ? 0.4813 0.6388 0.5018 -0.0181 -0.0156 -0.0163 295 PRO A CD 2309 N N . ALA A 300 ? 0.4178 0.5328 0.4346 -0.0149 -0.0124 -0.0052 296 ALA A N 2310 C CA . ALA A 300 ? 0.4075 0.5144 0.4244 -0.0143 -0.0113 -0.0018 296 ALA A CA 2311 C C . ALA A 300 ? 0.3929 0.5006 0.4115 -0.0191 -0.0112 -0.0024 296 ALA A C 2312 O O . ALA A 300 ? 0.4114 0.5190 0.4307 -0.0242 -0.0118 -0.0048 296 ALA A O 2313 C CB . ALA A 300 ? 0.3805 0.4755 0.3963 -0.0146 -0.0109 -0.0006 296 ALA A CB 2314 N N . GLY A 301 ? 0.3767 0.4846 0.3959 -0.0177 -0.0104 0.0000 297 GLY A N 2315 C CA . GLY A 301 ? 0.3710 0.4788 0.3916 -0.0221 -0.0102 -0.0002 297 GLY A CA 2316 C C . GLY A 301 ? 0.3776 0.4968 0.3998 -0.0244 -0.0107 -0.0025 297 GLY A C 2317 O O . GLY A 301 ? 0.3742 0.4940 0.3976 -0.0284 -0.0104 -0.0026 297 GLY A O 2318 N N . SER A 302 ? 0.3682 0.4970 0.3904 -0.0217 -0.0113 -0.0041 298 SER A N 2319 C CA . SER A 302 ? 0.3815 0.5223 0.4053 -0.0241 -0.0119 -0.0069 298 SER A CA 2320 C C . SER A 302 ? 0.3862 0.5346 0.4108 -0.0214 -0.0114 -0.0054 298 SER A C 2321 O O . SER A 302 ? 0.3832 0.5416 0.4093 -0.0235 -0.0118 -0.0075 298 SER A O 2322 C CB . SER A 302 ? 0.3813 0.5301 0.4047 -0.0225 -0.0130 -0.0098 298 SER A CB 2323 O OG . SER A 302 ? 0.4072 0.5603 0.4291 -0.0154 -0.0129 -0.0080 298 SER A OG 2324 N N . ASP A 303 ? 0.3630 0.5070 0.3865 -0.0167 -0.0105 -0.0021 299 ASP A N 2325 C CA . ASP A 303 ? 0.3609 0.5106 0.3851 -0.0144 -0.0098 -0.0006 299 ASP A CA 2326 C C . ASP A 303 ? 0.3415 0.4811 0.3650 -0.0125 -0.0086 0.0026 299 ASP A C 2327 O O . ASP A 303 ? 0.3227 0.4605 0.3450 -0.0070 -0.0077 0.0048 299 ASP A O 2328 C CB . ASP A 303 ? 0.3626 0.5223 0.3860 -0.0085 -0.0099 -0.0005 299 ASP A CB 2329 C CG . ASP A 303 ? 0.4061 0.5731 0.4303 -0.0063 -0.0092 0.0005 299 ASP A CG 2330 O OD1 . ASP A 303 ? 0.3586 0.5214 0.3837 -0.0085 -0.0086 0.0017 299 ASP A OD1 2331 O OD2 . ASP A 303 ? 0.4460 0.6231 0.4698 -0.0021 -0.0094 0.0001 299 ASP A OD2 2332 N N . TYR A 304 ? 0.3338 0.4666 0.3580 -0.0170 -0.0084 0.0029 300 TYR A N 2333 C CA . TYR A 304 ? 0.3274 0.4504 0.3511 -0.0156 -0.0074 0.0056 300 TYR A CA 2334 C C . TYR A 304 ? 0.3285 0.4550 0.3525 -0.0121 -0.0064 0.0072 300 TYR A C 2335 O O . TYR A 304 ? 0.3290 0.4494 0.3523 -0.0088 -0.0053 0.0092 300 TYR A O 2336 C CB . TYR A 304 ? 0.3226 0.4387 0.3467 -0.0209 -0.0074 0.0055 300 TYR A CB 2337 C CG . TYR A 304 ? 0.3331 0.4386 0.3564 -0.0197 -0.0067 0.0077 300 TYR A CG 2338 C CD1 . TYR A 304 ? 0.3297 0.4283 0.3517 -0.0176 -0.0066 0.0082 300 TYR A CD1 2339 C CD2 . TYR A 304 ? 0.3556 0.4583 0.3794 -0.0208 -0.0060 0.0090 300 TYR A CD2 2340 C CE1 . TYR A 304 ? 0.3209 0.4105 0.3424 -0.0166 -0.0059 0.0099 300 TYR A CE1 2341 C CE2 . TYR A 304 ? 0.3596 0.4532 0.3828 -0.0197 -0.0054 0.0107 300 TYR A CE2 2342 C CZ . TYR A 304 ? 0.3413 0.4287 0.3634 -0.0177 -0.0053 0.0110 300 TYR A CZ 2343 O OH . TYR A 304 ? 0.2833 0.3626 0.3050 -0.0169 -0.0048 0.0123 300 TYR A OH 2344 N N . SER A 305 ? 0.3213 0.4577 0.3465 -0.0130 -0.0066 0.0061 301 SER A N 2345 C CA . SER A 305 ? 0.3107 0.4514 0.3361 -0.0091 -0.0057 0.0075 301 SER A CA 2346 C C . SER A 305 ? 0.3179 0.4583 0.3417 -0.0025 -0.0048 0.0089 301 SER A C 2347 O O . SER A 305 ? 0.3268 0.4633 0.3502 0.0010 -0.0034 0.0109 301 SER A O 2348 C CB . SER A 305 ? 0.3246 0.4778 0.3513 -0.0103 -0.0062 0.0059 301 SER A CB 2349 O OG . SER A 305 ? 0.3367 0.4938 0.3632 -0.0054 -0.0052 0.0074 301 SER A OG 2350 N N . TYR A 306 ? 0.3093 0.4544 0.3323 -0.0007 -0.0055 0.0079 302 TYR A N 2351 C CA . TYR A 306 ? 0.3220 0.4666 0.3432 0.0059 -0.0045 0.0096 302 TYR A CA 2352 C C . TYR A 306 ? 0.3125 0.4445 0.3326 0.0069 -0.0035 0.0113 302 TYR A C 2353 O O . TYR A 306 ? 0.3058 0.4338 0.3249 0.0116 -0.0017 0.0135 302 TYR A O 2354 C CB . TYR A 306 ? 0.3201 0.4734 0.3404 0.0076 -0.0056 0.0080 302 TYR A CB 2355 C CG . TYR A 306 ? 0.3882 0.5404 0.4063 0.0145 -0.0044 0.0100 302 TYR A CG 2356 C CD1 . TYR A 306 ? 0.3996 0.5563 0.4167 0.0204 -0.0029 0.0119 302 TYR A CD1 2357 C CD2 . TYR A 306 ? 0.4057 0.5514 0.4225 0.0153 -0.0043 0.0104 302 TYR A CD2 2358 C CE1 . TYR A 306 ? 0.4449 0.5998 0.4597 0.0269 -0.0014 0.0142 302 TYR A CE1 2359 C CE2 . TYR A 306 ? 0.4074 0.5519 0.4219 0.0217 -0.0029 0.0126 302 TYR A CE2 2360 C CZ . TYR A 306 ? 0.4522 0.6010 0.4658 0.0274 -0.0013 0.0146 302 TYR A CZ 2361 O OH . TYR A 306 ? 0.5294 0.6764 0.5406 0.0339 0.0005 0.0171 302 TYR A OH 2362 N N . SER A 307 ? 0.3062 0.4323 0.3265 0.0026 -0.0044 0.0103 303 SER A N 2363 C CA . SER A 307 ? 0.3013 0.4157 0.3210 0.0031 -0.0036 0.0118 303 SER A CA 2364 C C . SER A 307 ? 0.2918 0.4007 0.3119 0.0046 -0.0019 0.0137 303 SER A C 2365 O O . SER A 307 ? 0.3049 0.4081 0.3242 0.0082 -0.0003 0.0153 303 SER A O 2366 C CB . SER A 307 ? 0.2980 0.4068 0.3180 -0.0023 -0.0048 0.0105 303 SER A CB 2367 O OG . SER A 307 ? 0.3021 0.4142 0.3215 -0.0031 -0.0060 0.0088 303 SER A OG 2368 N N . VAL A 308 ? 0.2761 0.3868 0.2976 0.0016 -0.0022 0.0132 304 VAL A N 2369 C CA . VAL A 308 ? 0.2760 0.3821 0.2981 0.0024 -0.0008 0.0145 304 VAL A CA 2370 C C . VAL A 308 ? 0.2972 0.4060 0.3188 0.0081 0.0010 0.0158 304 VAL A C 2371 O O . VAL A 308 ? 0.2936 0.3961 0.3150 0.0107 0.0028 0.0171 304 VAL A O 2372 C CB . VAL A 308 ? 0.2608 0.3693 0.2842 -0.0019 -0.0015 0.0137 304 VAL A CB 2373 C CG1 . VAL A 308 ? 0.2325 0.3372 0.2566 -0.0007 0.0000 0.0147 304 VAL A CG1 2374 C CG2 . VAL A 308 ? 0.2595 0.3634 0.2831 -0.0072 -0.0027 0.0129 304 VAL A CG2 2375 N N . LYS A 309 ? 0.2816 0.4002 0.3030 0.0099 0.0006 0.0153 305 LYS A N 2376 C CA . LYS A 309 ? 0.3100 0.4319 0.3306 0.0156 0.0023 0.0167 305 LYS A CA 2377 C C . LYS A 309 ? 0.3021 0.4187 0.3210 0.0203 0.0039 0.0184 305 LYS A C 2378 O O . LYS A 309 ? 0.3027 0.4134 0.3212 0.0237 0.0062 0.0199 305 LYS A O 2379 C CB . LYS A 309 ? 0.3110 0.4456 0.3315 0.0169 0.0013 0.0157 305 LYS A CB 2380 C CG . LYS A 309 ? 0.3900 0.5287 0.4092 0.0234 0.0030 0.0173 305 LYS A CG 2381 C CD . LYS A 309 ? 0.4112 0.5639 0.4305 0.0246 0.0018 0.0160 305 LYS A CD 2382 C CE . LYS A 309 ? 0.4506 0.6076 0.4676 0.0315 0.0029 0.0175 305 LYS A CE 2383 N NZ . LYS A 309 ? 0.4721 0.6433 0.4890 0.0340 0.0022 0.0166 305 LYS A NZ 2384 N N . ALA A 310 ? 0.2936 0.4117 0.3114 0.0204 0.0028 0.0179 306 ALA A N 2385 C CA . ALA A 310 ? 0.3019 0.4164 0.3179 0.0253 0.0044 0.0197 306 ALA A CA 2386 C C . ALA A 310 ? 0.3047 0.4071 0.3209 0.0251 0.0061 0.0208 306 ALA A C 2387 O O . ALA A 310 ? 0.2779 0.3757 0.2931 0.0296 0.0087 0.0228 306 ALA A O 2388 C CB . ALA A 310 ? 0.3122 0.4302 0.3272 0.0247 0.0027 0.0186 306 ALA A CB 2389 N N . SER A 311 ? 0.2869 0.3844 0.3044 0.0198 0.0048 0.0196 307 SER A N 2390 C CA . SER A 311 ? 0.2830 0.3701 0.3008 0.0192 0.0061 0.0203 307 SER A CA 2391 C C . SER A 311 ? 0.2735 0.3561 0.2923 0.0201 0.0082 0.0210 307 SER A C 2392 O O . SER A 311 ? 0.2862 0.3621 0.3049 0.0224 0.0105 0.0221 307 SER A O 2393 C CB . SER A 311 ? 0.2694 0.3529 0.2880 0.0138 0.0041 0.0188 307 SER A CB 2394 O OG . SER A 311 ? 0.2815 0.3670 0.3016 0.0097 0.0029 0.0177 307 SER A OG 2395 N N . ILE A 312 ? 0.2737 0.3601 0.2937 0.0181 0.0075 0.0201 308 ILE A N 2396 C CA . ILE A 312 ? 0.2709 0.3537 0.2920 0.0188 0.0094 0.0203 308 ILE A CA 2397 C C . ILE A 312 ? 0.2904 0.3743 0.3104 0.0247 0.0120 0.0219 308 ILE A C 2398 O O . ILE A 312 ? 0.2996 0.3772 0.3199 0.0267 0.0146 0.0225 308 ILE A O 2399 C CB . ILE A 312 ? 0.2806 0.3683 0.3031 0.0153 0.0079 0.0190 308 ILE A CB 2400 C CG1 . ILE A 312 ? 0.2664 0.3520 0.2897 0.0097 0.0058 0.0178 308 ILE A CG1 2401 C CG2 . ILE A 312 ? 0.2717 0.3569 0.2952 0.0167 0.0099 0.0190 308 ILE A CG2 2402 C CD1 . ILE A 312 ? 0.2499 0.3257 0.2736 0.0085 0.0065 0.0179 308 ILE A CD1 2403 N N . LEU A 313 ? 0.2847 0.3767 0.3034 0.0275 0.0114 0.0224 309 LEU A N 2404 C CA . LEU A 313 ? 0.2924 0.3852 0.3095 0.0338 0.0141 0.0242 309 LEU A CA 2405 C C . LEU A 313 ? 0.2914 0.3770 0.3071 0.0371 0.0163 0.0260 309 LEU A C 2406 O O . LEU A 313 ? 0.3099 0.3912 0.3247 0.0416 0.0195 0.0277 309 LEU A O 2407 C CB . LEU A 313 ? 0.3043 0.4084 0.3202 0.0366 0.0129 0.0244 309 LEU A CB 2408 C CG . LEU A 313 ? 0.3063 0.4171 0.3237 0.0342 0.0116 0.0229 309 LEU A CG 2409 C CD1 . LEU A 313 ? 0.3072 0.4304 0.3235 0.0369 0.0104 0.0228 309 LEU A CD1 2410 C CD2 . LEU A 313 ? 0.3206 0.4274 0.3386 0.0361 0.0141 0.0234 309 LEU A CD2 2411 N N . ALA A 314 ? 0.2696 0.3537 0.2851 0.0349 0.0148 0.0257 310 ALA A N 2412 C CA . ALA A 314 ? 0.2829 0.3603 0.2971 0.0377 0.0169 0.0273 310 ALA A CA 2413 C C . ALA A 314 ? 0.2891 0.3561 0.3046 0.0367 0.0194 0.0275 310 ALA A C 2414 O O . ALA A 314 ? 0.3136 0.3746 0.3282 0.0400 0.0223 0.0292 310 ALA A O 2415 C CB . ALA A 314 ? 0.2717 0.3498 0.2853 0.0354 0.0145 0.0266 310 ALA A CB 2416 N N . GLY A 315 ? 0.2782 0.3437 0.2960 0.0324 0.0184 0.0257 311 GLY A N 2417 C CA . GLY A 315 ? 0.2780 0.3349 0.2974 0.0310 0.0205 0.0252 311 GLY A CA 2418 C C . GLY A 315 ? 0.2724 0.3256 0.2935 0.0259 0.0187 0.0235 311 GLY A C 2419 O O . GLY A 315 ? 0.2720 0.3187 0.2946 0.0246 0.0204 0.0228 311 GLY A O 2420 N N . LEU A 316 ? 0.2810 0.3383 0.3018 0.0229 0.0155 0.0227 312 LEU A N 2421 C CA . LEU A 316 ? 0.2688 0.3225 0.2909 0.0182 0.0138 0.0213 312 LEU A CA 2422 C C . LEU A 316 ? 0.2807 0.3344 0.3046 0.0155 0.0136 0.0199 312 LEU A C 2423 O O . LEU A 316 ? 0.2634 0.3225 0.2874 0.0157 0.0131 0.0196 312 LEU A O 2424 C CB . LEU A 316 ? 0.2776 0.3350 0.2989 0.0156 0.0108 0.0207 312 LEU A CB 2425 C CG . LEU A 316 ? 0.2750 0.3305 0.2948 0.0173 0.0108 0.0216 312 LEU A CG 2426 C CD1 . LEU A 316 ? 0.2931 0.3531 0.3110 0.0222 0.0119 0.0231 312 LEU A CD1 2427 C CD2 . LEU A 316 ? 0.2773 0.3347 0.2967 0.0137 0.0078 0.0204 312 LEU A CD2 2428 N N . ASP A 317 ? 0.2668 0.3153 0.2922 0.0130 0.0138 0.0188 313 ASP A N 2429 C CA . ASP A 317 ? 0.2618 0.3103 0.2889 0.0107 0.0138 0.0173 313 ASP A CA 2430 C C . ASP A 317 ? 0.2589 0.3091 0.2863 0.0065 0.0109 0.0164 313 ASP A C 2431 O O . ASP A 317 ? 0.2583 0.3120 0.2863 0.0049 0.0101 0.0156 313 ASP A O 2432 C CB . ASP A 317 ? 0.2618 0.3040 0.2906 0.0110 0.0163 0.0165 313 ASP A CB 2433 C CG . ASP A 317 ? 0.3047 0.3437 0.3331 0.0151 0.0197 0.0176 313 ASP A CG 2434 O OD1 . ASP A 317 ? 0.2637 0.3057 0.2915 0.0177 0.0207 0.0183 313 ASP A OD1 2435 O OD2 . ASP A 317 ? 0.2744 0.3077 0.3031 0.0159 0.0217 0.0179 313 ASP A OD2 2436 N N . MET A 318 ? 0.2582 0.3056 0.2851 0.0050 0.0097 0.0164 314 MET A N 2437 C CA . MET A 318 ? 0.2604 0.3086 0.2872 0.0013 0.0073 0.0158 314 MET A CA 2438 C C . MET A 318 ? 0.2598 0.3092 0.2849 0.0005 0.0055 0.0164 314 MET A C 2439 O O . MET A 318 ? 0.2638 0.3111 0.2882 0.0023 0.0060 0.0169 314 MET A O 2440 C CB . MET A 318 ? 0.2541 0.2972 0.2819 -0.0001 0.0075 0.0149 314 MET A CB 2441 C CG . MET A 318 ? 0.2671 0.3106 0.2945 -0.0034 0.0052 0.0145 314 MET A CG 2442 S SD . MET A 318 ? 0.2692 0.3078 0.2975 -0.0043 0.0055 0.0135 314 MET A SD 2443 C CE . MET A 318 ? 0.2028 0.2429 0.2334 -0.0039 0.0073 0.0120 314 MET A CE 2444 N N . ILE A 319 ? 0.2497 0.3025 0.2744 -0.0022 0.0035 0.0161 315 ILE A N 2445 C CA . ILE A 319 ? 0.2486 0.3028 0.2719 -0.0033 0.0020 0.0162 315 ILE A CA 2446 C C . ILE A 319 ? 0.2512 0.3017 0.2740 -0.0064 0.0006 0.0159 315 ILE A C 2447 O O . ILE A 319 ? 0.2494 0.3000 0.2725 -0.0088 -0.0001 0.0157 315 ILE A O 2448 C CB . ILE A 319 ? 0.2428 0.3041 0.2659 -0.0042 0.0010 0.0160 315 ILE A CB 2449 C CG1 . ILE A 319 ? 0.2548 0.3203 0.2780 -0.0006 0.0025 0.0165 315 ILE A CG1 2450 C CG2 . ILE A 319 ? 0.2314 0.2944 0.2533 -0.0061 -0.0007 0.0156 315 ILE A CG2 2451 C CD1 . ILE A 319 ? 0.2475 0.3117 0.2699 0.0034 0.0037 0.0173 315 ILE A CD1 2452 N N . MET A 320 ? 0.2474 0.2948 0.2692 -0.0060 0.0002 0.0159 316 MET A N 2453 C CA . MET A 320 ? 0.2438 0.2874 0.2648 -0.0084 -0.0011 0.0156 316 MET A CA 2454 C C . MET A 320 ? 0.2598 0.3067 0.2798 -0.0109 -0.0025 0.0152 316 MET A C 2455 O O . MET A 320 ? 0.2752 0.3232 0.2945 -0.0106 -0.0031 0.0148 316 MET A O 2456 C CB . MET A 320 ? 0.2436 0.2829 0.2640 -0.0066 -0.0008 0.0157 316 MET A CB 2457 C CG . MET A 320 ? 0.2462 0.2810 0.2654 -0.0087 -0.0020 0.0154 316 MET A CG 2458 S SD . MET A 320 ? 0.2632 0.2935 0.2817 -0.0066 -0.0017 0.0154 316 MET A SD 2459 C CE . MET A 320 ? 0.2100 0.2385 0.2303 -0.0041 0.0005 0.0157 316 MET A CE 2460 N N . VAL A 321 ? 0.2584 0.3072 0.2787 -0.0136 -0.0031 0.0152 317 VAL A N 2461 C CA . VAL A 321 ? 0.2574 0.3108 0.2774 -0.0160 -0.0039 0.0146 317 VAL A CA 2462 C C . VAL A 321 ? 0.2673 0.3183 0.2860 -0.0179 -0.0049 0.0139 317 VAL A C 2463 O O . VAL A 321 ? 0.2672 0.3221 0.2858 -0.0176 -0.0054 0.0130 317 VAL A O 2464 C CB . VAL A 321 ? 0.2550 0.3112 0.2755 -0.0186 -0.0040 0.0149 317 VAL A CB 2465 C CG1 . VAL A 321 ? 0.2563 0.3180 0.2768 -0.0214 -0.0047 0.0141 317 VAL A CG1 2466 C CG2 . VAL A 321 ? 0.2685 0.3278 0.2903 -0.0163 -0.0030 0.0153 317 VAL A CG2 2467 N N . PRO A 322 ? 0.2568 0.3015 0.2745 -0.0194 -0.0053 0.0141 318 PRO A N 2468 C CA . PRO A 322 ? 0.2649 0.3057 0.2825 -0.0197 -0.0049 0.0151 318 PRO A CA 2469 C C . PRO A 322 ? 0.2844 0.3249 0.3014 -0.0232 -0.0053 0.0155 318 PRO A C 2470 O O . PRO A 322 ? 0.2757 0.3140 0.2924 -0.0234 -0.0050 0.0165 318 PRO A O 2471 C CB . PRO A 322 ? 0.2661 0.3006 0.2827 -0.0186 -0.0051 0.0152 318 PRO A CB 2472 C CG . PRO A 322 ? 0.2775 0.3113 0.2929 -0.0203 -0.0059 0.0142 318 PRO A CG 2473 C CD . PRO A 322 ? 0.2623 0.3033 0.2787 -0.0199 -0.0059 0.0134 318 PRO A CD 2474 N N . ASN A 323 ? 0.2820 0.3249 0.2987 -0.0258 -0.0057 0.0147 319 ASN A N 2475 C CA . ASN A 323 ? 0.3122 0.3535 0.3281 -0.0296 -0.0056 0.0151 319 ASN A CA 2476 C C . ASN A 323 ? 0.3358 0.3836 0.3528 -0.0315 -0.0053 0.0152 319 ASN A C 2477 O O . ASN A 323 ? 0.3427 0.3900 0.3594 -0.0328 -0.0048 0.0164 319 ASN A O 2478 C CB . ASN A 323 ? 0.3101 0.3481 0.3247 -0.0320 -0.0059 0.0140 319 ASN A CB 2479 C CG . ASN A 323 ? 0.3349 0.3662 0.3482 -0.0303 -0.0062 0.0141 319 ASN A CG 2480 O OD1 . ASN A 323 ? 0.3508 0.3780 0.3635 -0.0286 -0.0060 0.0154 319 ASN A OD1 2481 N ND2 . ASN A 323 ? 0.3490 0.3798 0.3620 -0.0305 -0.0067 0.0126 319 ASN A ND2 2482 N N . LYS A 324 ? 0.3364 0.3907 0.3546 -0.0314 -0.0055 0.0139 320 LYS A N 2483 C CA . LYS A 324 ? 0.3445 0.4061 0.3639 -0.0331 -0.0053 0.0136 320 LYS A CA 2484 C C . LYS A 324 ? 0.3390 0.4047 0.3595 -0.0305 -0.0049 0.0144 320 LYS A C 2485 O O . LYS A 324 ? 0.3211 0.3937 0.3427 -0.0291 -0.0049 0.0137 320 LYS A O 2486 C CB . LYS A 324 ? 0.3783 0.4461 0.3985 -0.0339 -0.0058 0.0116 320 LYS A CB 2487 C CG . LYS A 324 ? 0.4394 0.5049 0.4590 -0.0381 -0.0059 0.0104 320 LYS A CG 2488 C CD . LYS A 324 ? 0.5300 0.5954 0.5496 -0.0423 -0.0051 0.0112 320 LYS A CD 2489 C CE . LYS A 324 ? 0.5377 0.6121 0.5591 -0.0430 -0.0047 0.0113 320 LYS A CE 2490 N NZ . LYS A 324 ? 0.3898 0.4646 0.4112 -0.0405 -0.0043 0.0133 320 LYS A NZ 2491 N N . TYR A 325 ? 0.3080 0.3700 0.3281 -0.0298 -0.0045 0.0157 321 TYR A N 2492 C CA . TYR A 325 ? 0.3147 0.3801 0.3359 -0.0273 -0.0039 0.0161 321 TYR A CA 2493 C C . TYR A 325 ? 0.3084 0.3812 0.3306 -0.0288 -0.0037 0.0160 321 TYR A C 2494 O O . TYR A 325 ? 0.3108 0.3886 0.3341 -0.0266 -0.0033 0.0158 321 TYR A O 2495 C CB . TYR A 325 ? 0.2935 0.3543 0.3141 -0.0265 -0.0036 0.0172 321 TYR A CB 2496 C CG . TYR A 325 ? 0.3165 0.3750 0.3359 -0.0295 -0.0036 0.0183 321 TYR A CG 2497 C CD1 . TYR A 325 ? 0.3012 0.3640 0.3208 -0.0312 -0.0032 0.0189 321 TYR A CD1 2498 C CD2 . TYR A 325 ? 0.3381 0.3900 0.3559 -0.0305 -0.0038 0.0188 321 TYR A CD2 2499 C CE1 . TYR A 325 ? 0.2971 0.3573 0.3152 -0.0339 -0.0028 0.0203 321 TYR A CE1 2500 C CE2 . TYR A 325 ? 0.3291 0.3780 0.3452 -0.0331 -0.0035 0.0201 321 TYR A CE2 2501 C CZ . TYR A 325 ? 0.3293 0.3823 0.3456 -0.0348 -0.0029 0.0209 321 TYR A CZ 2502 O OH . TYR A 325 ? 0.3621 0.4117 0.3767 -0.0371 -0.0023 0.0225 321 TYR A OH 2503 N N . GLN A 326 ? 0.3240 0.3974 0.3457 -0.0326 -0.0037 0.0163 322 GLN A N 2504 C CA . GLN A 326 ? 0.3327 0.4131 0.3554 -0.0342 -0.0033 0.0163 322 GLN A CA 2505 C C . GLN A 326 ? 0.3182 0.4061 0.3422 -0.0333 -0.0036 0.0148 322 GLN A C 2506 O O . GLN A 326 ? 0.3275 0.4214 0.3525 -0.0314 -0.0033 0.0147 322 GLN A O 2507 C CB . GLN A 326 ? 0.3573 0.4367 0.3793 -0.0389 -0.0029 0.0169 322 GLN A CB 2508 C CG . GLN A 326 ? 0.4289 0.5160 0.4520 -0.0408 -0.0023 0.0170 322 GLN A CG 2509 C CD . GLN A 326 ? 0.5302 0.6167 0.5528 -0.0460 -0.0017 0.0171 322 GLN A CD 2510 O OE1 . GLN A 326 ? 0.5523 0.6326 0.5733 -0.0476 -0.0011 0.0187 322 GLN A OE1 2511 N NE2 . GLN A 326 ? 0.5501 0.6428 0.5741 -0.0484 -0.0018 0.0153 322 GLN A NE2 2512 N N . GLN A 327 ? 0.3227 0.4102 0.3465 -0.0343 -0.0042 0.0136 323 GLN A N 2513 C CA . GLN A 327 ? 0.3365 0.4319 0.3614 -0.0329 -0.0045 0.0121 323 GLN A CA 2514 C C . GLN A 327 ? 0.3198 0.4163 0.3449 -0.0276 -0.0043 0.0125 323 GLN A C 2515 O O . GLN A 327 ? 0.3114 0.4152 0.3374 -0.0256 -0.0042 0.0121 323 GLN A O 2516 C CB . GLN A 327 ? 0.3524 0.4467 0.3769 -0.0346 -0.0052 0.0106 323 GLN A CB 2517 C CG . GLN A 327 ? 0.4446 0.5486 0.4702 -0.0342 -0.0056 0.0088 323 GLN A CG 2518 C CD . GLN A 327 ? 0.5377 0.6422 0.5631 -0.0348 -0.0064 0.0069 323 GLN A CD 2519 O OE1 . GLN A 327 ? 0.5904 0.6873 0.6146 -0.0350 -0.0066 0.0069 323 GLN A OE1 2520 N NE2 . GLN A 327 ? 0.5608 0.6749 0.5872 -0.0345 -0.0068 0.0051 323 GLN A NE2 2521 N N . PHE A 328 ? 0.2949 0.3842 0.3192 -0.0252 -0.0042 0.0132 324 PHE A N 2522 C CA . PHE A 328 ? 0.2629 0.3520 0.2873 -0.0204 -0.0036 0.0136 324 PHE A CA 2523 C C . PHE A 328 ? 0.2672 0.3596 0.2925 -0.0190 -0.0028 0.0141 324 PHE A C 2524 O O . PHE A 328 ? 0.2728 0.3703 0.2986 -0.0160 -0.0023 0.0140 324 PHE A O 2525 C CB . PHE A 328 ? 0.2611 0.3413 0.2847 -0.0188 -0.0034 0.0142 324 PHE A CB 2526 C CG . PHE A 328 ? 0.2619 0.3412 0.2859 -0.0144 -0.0022 0.0147 324 PHE A CG 2527 C CD1 . PHE A 328 ? 0.2569 0.3389 0.2807 -0.0110 -0.0018 0.0146 324 PHE A CD1 2528 C CD2 . PHE A 328 ? 0.2673 0.3434 0.2918 -0.0135 -0.0014 0.0152 324 PHE A CD2 2529 C CE1 . PHE A 328 ? 0.2626 0.3429 0.2866 -0.0069 -0.0003 0.0152 324 PHE A CE1 2530 C CE2 . PHE A 328 ? 0.2648 0.3397 0.2899 -0.0098 0.0000 0.0154 324 PHE A CE2 2531 C CZ . PHE A 328 ? 0.2759 0.3526 0.3006 -0.0065 0.0006 0.0155 324 PHE A CZ 2532 N N . ILE A 329 ? 0.2585 0.3482 0.2838 -0.0209 -0.0026 0.0147 325 ILE A N 2533 C CA . ILE A 329 ? 0.2821 0.3748 0.3082 -0.0195 -0.0018 0.0150 325 ILE A CA 2534 C C . ILE A 329 ? 0.2672 0.3691 0.2941 -0.0201 -0.0019 0.0146 325 ILE A C 2535 O O . ILE A 329 ? 0.2761 0.3821 0.3037 -0.0172 -0.0012 0.0145 325 ILE A O 2536 C CB . ILE A 329 ? 0.2790 0.3681 0.3049 -0.0214 -0.0017 0.0157 325 ILE A CB 2537 C CG1 . ILE A 329 ? 0.3074 0.3887 0.3328 -0.0198 -0.0015 0.0159 325 ILE A CG1 2538 C CG2 . ILE A 329 ? 0.2997 0.3933 0.3264 -0.0205 -0.0010 0.0157 325 ILE A CG2 2539 C CD1 . ILE A 329 ? 0.2729 0.3502 0.2975 -0.0219 -0.0017 0.0166 325 ILE A CD1 2540 N N . SER A 330 ? 0.2726 0.3774 0.2995 -0.0239 -0.0025 0.0142 326 SER A N 2541 C CA . SER A 330 ? 0.2804 0.3946 0.3083 -0.0250 -0.0026 0.0136 326 SER A CA 2542 C C . SER A 330 ? 0.2657 0.3862 0.2941 -0.0214 -0.0026 0.0128 326 SER A C 2543 O O . SER A 330 ? 0.2782 0.4052 0.3073 -0.0193 -0.0021 0.0127 326 SER A O 2544 C CB . SER A 330 ? 0.2774 0.3932 0.3054 -0.0301 -0.0031 0.0130 326 SER A CB 2545 O OG . SER A 330 ? 0.3289 0.4546 0.3581 -0.0314 -0.0030 0.0123 326 SER A OG 2546 N N . ILE A 331 ? 0.2833 0.4016 0.3111 -0.0203 -0.0030 0.0123 327 ILE A N 2547 C CA . ILE A 331 ? 0.2775 0.4017 0.3053 -0.0166 -0.0031 0.0117 327 ILE A CA 2548 C C . ILE A 331 ? 0.2914 0.4141 0.3189 -0.0113 -0.0019 0.0127 327 ILE A C 2549 O O . ILE A 331 ? 0.2708 0.4003 0.2985 -0.0082 -0.0014 0.0126 327 ILE A O 2550 C CB . ILE A 331 ? 0.2862 0.4079 0.3131 -0.0167 -0.0038 0.0110 327 ILE A CB 2551 C CG1 . ILE A 331 ? 0.3098 0.4360 0.3374 -0.0217 -0.0048 0.0094 327 ILE A CG1 2552 C CG2 . ILE A 331 ? 0.2644 0.3904 0.2908 -0.0114 -0.0035 0.0110 327 ILE A CG2 2553 C CD1 . ILE A 331 ? 0.3658 0.4892 0.3927 -0.0227 -0.0056 0.0083 327 ILE A CD1 2554 N N . LEU A 332 ? 0.2694 0.3831 0.2964 -0.0103 -0.0012 0.0136 328 LEU A N 2555 C CA . LEU A 332 ? 0.2753 0.3868 0.3023 -0.0057 0.0003 0.0143 328 LEU A CA 2556 C C . LEU A 332 ? 0.2747 0.3904 0.3025 -0.0052 0.0010 0.0143 328 LEU A C 2557 O O . LEU A 332 ? 0.2637 0.3824 0.2914 -0.0011 0.0021 0.0145 328 LEU A O 2558 C CB . LEU A 332 ? 0.2683 0.3696 0.2949 -0.0052 0.0010 0.0148 328 LEU A CB 2559 C CG . LEU A 332 ? 0.2897 0.3874 0.3164 -0.0008 0.0029 0.0153 328 LEU A CG 2560 C CD1 . LEU A 332 ? 0.2880 0.3890 0.3139 0.0038 0.0039 0.0159 328 LEU A CD1 2561 C CD2 . LEU A 332 ? 0.2655 0.3535 0.2921 -0.0011 0.0034 0.0155 328 LEU A CD2 2562 N N . THR A 333 ? 0.2841 0.3998 0.3125 -0.0090 0.0005 0.0141 329 THR A N 2563 C CA . THR A 333 ? 0.2896 0.4106 0.3188 -0.0088 0.0010 0.0139 329 THR A CA 2564 C C . THR A 333 ? 0.2784 0.4095 0.3079 -0.0073 0.0009 0.0135 329 THR A C 2565 O O . THR A 333 ? 0.3013 0.4361 0.3310 -0.0040 0.0019 0.0135 329 THR A O 2566 C CB . THR A 333 ? 0.2906 0.4113 0.3200 -0.0135 0.0003 0.0140 329 THR A CB 2567 O OG1 . THR A 333 ? 0.2891 0.4010 0.3180 -0.0143 0.0004 0.0144 329 THR A OG1 2568 C CG2 . THR A 333 ? 0.3187 0.4450 0.3489 -0.0131 0.0009 0.0139 329 THR A CG2 2569 N N . GLY A 334 ? 0.2983 0.4341 0.3278 -0.0098 -0.0003 0.0129 330 GLY A N 2570 C CA . GLY A 334 ? 0.2899 0.4366 0.3200 -0.0086 -0.0005 0.0122 330 GLY A CA 2571 C C . GLY A 334 ? 0.3057 0.4543 0.3350 -0.0025 0.0003 0.0126 330 GLY A C 2572 O O . GLY A 334 ? 0.2950 0.4510 0.3245 0.0005 0.0009 0.0125 330 GLY A O 2573 N N . HIS A 335 ? 0.2922 0.4342 0.3204 -0.0004 0.0006 0.0131 331 HIS A N 2574 C CA . HIS A 335 ? 0.3062 0.4485 0.3333 0.0057 0.0018 0.0140 331 HIS A CA 2575 C C . HIS A 335 ? 0.2965 0.4361 0.3235 0.0095 0.0037 0.0147 331 HIS A C 2576 O O . HIS A 335 ? 0.3070 0.4510 0.3334 0.0143 0.0048 0.0152 331 HIS A O 2577 C CB . HIS A 335 ? 0.3014 0.4358 0.3274 0.0069 0.0020 0.0146 331 HIS A CB 2578 C CG . HIS A 335 ? 0.3306 0.4697 0.3563 0.0054 0.0005 0.0137 331 HIS A CG 2579 N ND1 . HIS A 335 ? 0.3543 0.4873 0.3793 0.0039 -0.0001 0.0136 331 HIS A ND1 2580 C CD2 . HIS A 335 ? 0.3334 0.4832 0.3594 0.0050 -0.0006 0.0125 331 HIS A CD2 2581 C CE1 . HIS A 335 ? 0.3396 0.4790 0.3645 0.0027 -0.0015 0.0124 331 HIS A CE1 2582 N NE2 . HIS A 335 ? 0.3911 0.5410 0.4167 0.0032 -0.0018 0.0116 331 HIS A NE2 2583 N N . VAL A 336 ? 0.2858 0.4181 0.3134 0.0076 0.0042 0.0148 332 VAL A N 2584 C CA . VAL A 336 ? 0.2947 0.4244 0.3225 0.0107 0.0061 0.0150 332 VAL A CA 2585 C C . VAL A 336 ? 0.3197 0.4588 0.3482 0.0106 0.0059 0.0144 332 VAL A C 2586 O O . VAL A 336 ? 0.3337 0.4754 0.3619 0.0151 0.0074 0.0146 332 VAL A O 2587 C CB . VAL A 336 ? 0.2811 0.4021 0.3096 0.0083 0.0065 0.0147 332 VAL A CB 2588 C CG1 . VAL A 336 ? 0.2871 0.4061 0.3160 0.0110 0.0084 0.0143 332 VAL A CG1 2589 C CG2 . VAL A 336 ? 0.2703 0.3825 0.2982 0.0086 0.0068 0.0152 332 VAL A CG2 2590 N N . ASN A 337 ? 0.3288 0.4727 0.3582 0.0058 0.0043 0.0137 333 ASN A N 2591 C CA . ASN A 337 ? 0.3431 0.4962 0.3733 0.0050 0.0040 0.0131 333 ASN A CA 2592 C C . ASN A 337 ? 0.3518 0.5143 0.3816 0.0088 0.0041 0.0131 333 ASN A C 2593 O O . ASN A 337 ? 0.3633 0.5318 0.3933 0.0114 0.0049 0.0129 333 ASN A O 2594 C CB . ASN A 337 ? 0.3407 0.4971 0.3719 -0.0012 0.0025 0.0126 333 ASN A CB 2595 C CG . ASN A 337 ? 0.3692 0.5187 0.4006 -0.0042 0.0026 0.0128 333 ASN A CG 2596 O OD1 . ASN A 337 ? 0.3379 0.4826 0.3693 -0.0017 0.0038 0.0128 333 ASN A OD1 2597 N ND2 . ASN A 337 ? 0.3533 0.5026 0.3850 -0.0095 0.0015 0.0128 333 ASN A ND2 2598 N N . GLY A 338 ? 0.3609 0.5248 0.3901 0.0096 0.0035 0.0132 334 GLY A N 2599 C CA . GLY A 338 ? 0.3786 0.5522 0.4072 0.0135 0.0034 0.0131 334 GLY A CA 2600 C C . GLY A 338 ? 0.3937 0.5645 0.4205 0.0207 0.0052 0.0144 334 GLY A C 2601 O O . GLY A 338 ? 0.3867 0.5655 0.4126 0.0247 0.0053 0.0146 334 GLY A O 2602 N N . GLY A 339 ? 0.3716 0.5315 0.3979 0.0224 0.0069 0.0153 335 GLY A N 2603 C CA . GLY A 339 ? 0.3666 0.5226 0.3912 0.0290 0.0092 0.0167 335 GLY A CA 2604 C C . GLY A 339 ? 0.3601 0.5135 0.3833 0.0314 0.0093 0.0178 335 GLY A C 2605 O O . GLY A 339 ? 0.3728 0.5232 0.3943 0.0371 0.0114 0.0193 335 GLY A O 2606 N N . VAL A 340 ? 0.3484 0.5021 0.3720 0.0270 0.0073 0.0170 336 VAL A N 2607 C CA . VAL A 340 ? 0.3431 0.4948 0.3653 0.0287 0.0071 0.0178 336 VAL A CA 2608 C C . VAL A 340 ? 0.3476 0.4863 0.3692 0.0298 0.0088 0.0190 336 VAL A C 2609 O O . VAL A 340 ? 0.3354 0.4709 0.3553 0.0338 0.0100 0.0204 336 VAL A O 2610 C CB . VAL A 340 ? 0.3429 0.4985 0.3660 0.0232 0.0045 0.0162 336 VAL A CB 2611 C CG1 . VAL A 340 ? 0.3496 0.5010 0.3715 0.0242 0.0043 0.0168 336 VAL A CG1 2612 C CG2 . VAL A 340 ? 0.3777 0.5475 0.4015 0.0224 0.0030 0.0148 336 VAL A CG2 2613 N N . ILE A 341 ? 0.3454 0.4770 0.3683 0.0261 0.0090 0.0184 337 ILE A N 2614 C CA . ILE A 341 ? 0.3263 0.4461 0.3491 0.0266 0.0108 0.0191 337 ILE A CA 2615 C C . ILE A 341 ? 0.3204 0.4370 0.3440 0.0275 0.0125 0.0188 337 ILE A C 2616 O O . ILE A 341 ? 0.3203 0.4394 0.3453 0.0239 0.0114 0.0176 337 ILE A O 2617 C CB . ILE A 341 ? 0.3225 0.4368 0.3461 0.0210 0.0091 0.0183 337 ILE A CB 2618 C CG1 . ILE A 341 ? 0.3282 0.4451 0.3509 0.0203 0.0075 0.0184 337 ILE A CG1 2619 C CG2 . ILE A 341 ? 0.2788 0.3819 0.3028 0.0211 0.0109 0.0186 337 ILE A CG2 2620 C CD1 . ILE A 341 ? 0.3346 0.4477 0.3582 0.0144 0.0055 0.0174 337 ILE A CD1 2621 N N . PRO A 342 ? 0.3156 0.4269 0.3384 0.0323 0.0154 0.0198 338 PRO A N 2622 C CA . PRO A 342 ? 0.3155 0.4237 0.3390 0.0335 0.0174 0.0192 338 PRO A CA 2623 C C . PRO A 342 ? 0.3302 0.4306 0.3556 0.0292 0.0175 0.0178 338 PRO A C 2624 O O . PRO A 342 ? 0.3108 0.4054 0.3364 0.0270 0.0171 0.0179 338 PRO A O 2625 C CB . PRO A 342 ? 0.3190 0.4223 0.3409 0.0399 0.0209 0.0209 338 PRO A CB 2626 C CG . PRO A 342 ? 0.3207 0.4198 0.3415 0.0403 0.0208 0.0222 338 PRO A CG 2627 C CD . PRO A 342 ? 0.3181 0.4251 0.3390 0.0368 0.0172 0.0216 338 PRO A CD 2628 N N . MET A 343 ? 0.3214 0.4221 0.3480 0.0285 0.0182 0.0165 339 MET A N 2629 C CA . MET A 343 ? 0.3506 0.4449 0.3788 0.0250 0.0184 0.0149 339 MET A CA 2630 C C . MET A 343 ? 0.3430 0.4272 0.3713 0.0267 0.0211 0.0151 339 MET A C 2631 O O . MET A 343 ? 0.3633 0.4422 0.3928 0.0234 0.0208 0.0139 339 MET A O 2632 C CB . MET A 343 ? 0.3591 0.4563 0.3884 0.0245 0.0188 0.0132 339 MET A CB 2633 C CG . MET A 343 ? 0.4310 0.5240 0.4621 0.0202 0.0183 0.0113 339 MET A CG 2634 S SD . MET A 343 ? 0.4672 0.5631 0.4987 0.0141 0.0147 0.0113 339 MET A SD 2635 C CE . MET A 343 ? 0.4430 0.5491 0.4736 0.0138 0.0126 0.0124 339 MET A CE 2636 N N . SER A 344 ? 0.3305 0.4120 0.3575 0.0318 0.0238 0.0164 340 SER A N 2637 C CA . SER A 344 ? 0.3398 0.4115 0.3668 0.0334 0.0268 0.0167 340 SER A CA 2638 C C . SER A 344 ? 0.3285 0.3969 0.3554 0.0309 0.0254 0.0174 340 SER A C 2639 O O . SER A 344 ? 0.3495 0.4106 0.3775 0.0293 0.0266 0.0167 340 SER A O 2640 C CB . SER A 344 ? 0.3422 0.4121 0.3672 0.0397 0.0299 0.0187 340 SER A CB 2641 O OG . SER A 344 ? 0.3483 0.4241 0.3713 0.0418 0.0284 0.0208 340 SER A OG 2642 N N . ARG A 345 ? 0.3213 0.3956 0.3470 0.0304 0.0228 0.0186 341 ARG A N 2643 C CA . ARG A 345 ? 0.2988 0.3706 0.3241 0.0283 0.0214 0.0192 341 ARG A CA 2644 C C . ARG A 345 ? 0.3016 0.3718 0.3287 0.0226 0.0193 0.0174 341 ARG A C 2645 O O . ARG A 345 ? 0.2912 0.3551 0.3188 0.0210 0.0196 0.0172 341 ARG A O 2646 C CB . ARG A 345 ? 0.3055 0.3850 0.3292 0.0291 0.0191 0.0204 341 ARG A CB 2647 C CG . ARG A 345 ? 0.2817 0.3591 0.3046 0.0279 0.0179 0.0211 341 ARG A CG 2648 C CD . ARG A 345 ? 0.3104 0.3799 0.3323 0.0315 0.0209 0.0227 341 ARG A CD 2649 N NE . ARG A 345 ? 0.2886 0.3494 0.3121 0.0289 0.0221 0.0217 341 ARG A NE 2650 C CZ . ARG A 345 ? 0.3092 0.3677 0.3336 0.0248 0.0202 0.0208 341 ARG A CZ 2651 N NH1 . ARG A 345 ? 0.2684 0.3315 0.2921 0.0227 0.0172 0.0207 341 ARG A NH1 2652 N NH2 . ARG A 345 ? 0.2754 0.3270 0.3013 0.0230 0.0215 0.0197 341 ARG A NH2 2653 N N . ILE A 346 ? 0.2868 0.3628 0.3147 0.0198 0.0172 0.0163 342 ILE A N 2654 C CA . ILE A 346 ? 0.2888 0.3637 0.3180 0.0150 0.0154 0.0148 342 ILE A CA 2655 C C . ILE A 346 ? 0.2955 0.3637 0.3263 0.0147 0.0175 0.0134 342 ILE A C 2656 O O . ILE A 346 ? 0.2909 0.3549 0.3225 0.0120 0.0169 0.0126 342 ILE A O 2657 C CB . ILE A 346 ? 0.2869 0.3693 0.3165 0.0127 0.0135 0.0141 342 ILE A CB 2658 C CG1 . ILE A 346 ? 0.2928 0.3826 0.3212 0.0127 0.0116 0.0152 342 ILE A CG1 2659 C CG2 . ILE A 346 ? 0.2974 0.3785 0.3281 0.0082 0.0120 0.0129 342 ILE A CG2 2660 C CD1 . ILE A 346 ? 0.3098 0.3986 0.3376 0.0099 0.0096 0.0157 342 ILE A CD1 2661 N N . ASP A 347 ? 0.2779 0.3452 0.3092 0.0174 0.0200 0.0128 343 ASP A N 2662 C CA . ASP A 347 ? 0.2935 0.3553 0.3266 0.0167 0.0220 0.0107 343 ASP A CA 2663 C C . ASP A 347 ? 0.2977 0.3513 0.3311 0.0173 0.0240 0.0110 343 ASP A C 2664 O O . ASP A 347 ? 0.3010 0.3505 0.3362 0.0150 0.0246 0.0091 343 ASP A O 2665 C CB . ASP A 347 ? 0.3008 0.3629 0.3344 0.0196 0.0245 0.0098 343 ASP A CB 2666 C CG . ASP A 347 ? 0.3410 0.4105 0.3749 0.0183 0.0228 0.0087 343 ASP A CG 2667 O OD1 . ASP A 347 ? 0.3353 0.4090 0.3695 0.0148 0.0199 0.0085 343 ASP A OD1 2668 O OD2 . ASP A 347 ? 0.3087 0.3795 0.3428 0.0207 0.0245 0.0080 343 ASP A OD2 2669 N N . ASP A 348 ? 0.2935 0.3456 0.3253 0.0205 0.0251 0.0132 344 ASP A N 2670 C CA . ASP A 348 ? 0.2948 0.3395 0.3265 0.0214 0.0272 0.0139 344 ASP A CA 2671 C C . ASP A 348 ? 0.2901 0.3343 0.3222 0.0176 0.0245 0.0136 344 ASP A C 2672 O O . ASP A 348 ? 0.2842 0.3230 0.3176 0.0161 0.0257 0.0125 344 ASP A O 2673 C CB . ASP A 348 ? 0.3037 0.3477 0.3331 0.0260 0.0288 0.0167 344 ASP A CB 2674 C CG . ASP A 348 ? 0.3249 0.3618 0.3540 0.0269 0.0307 0.0178 344 ASP A CG 2675 O OD1 . ASP A 348 ? 0.3348 0.3647 0.3652 0.0269 0.0338 0.0169 344 ASP A OD1 2676 O OD2 . ASP A 348 ? 0.3490 0.3876 0.3766 0.0273 0.0292 0.0194 344 ASP A OD2 2677 N N . ALA A 349 ? 0.2712 0.3210 0.3021 0.0162 0.0213 0.0145 345 ALA A N 2678 C CA . ALA A 349 ? 0.2828 0.3320 0.3137 0.0129 0.0188 0.0144 345 ALA A CA 2679 C C . ALA A 349 ? 0.2968 0.3447 0.3296 0.0095 0.0182 0.0122 345 ALA A C 2680 O O . ALA A 349 ? 0.2956 0.3391 0.3293 0.0080 0.0184 0.0115 345 ALA A O 2681 C CB . ALA A 349 ? 0.2737 0.3293 0.3031 0.0117 0.0157 0.0153 345 ALA A CB 2682 N N . VAL A 350 ? 0.2709 0.3228 0.3044 0.0085 0.0176 0.0110 346 VAL A N 2683 C CA . VAL A 350 ? 0.2681 0.3199 0.3033 0.0056 0.0170 0.0088 346 VAL A CA 2684 C C . VAL A 350 ? 0.2865 0.3329 0.3237 0.0060 0.0198 0.0069 346 VAL A C 2685 O O . VAL A 350 ? 0.2827 0.3275 0.3213 0.0038 0.0194 0.0053 346 VAL A O 2686 C CB . VAL A 350 ? 0.2672 0.3253 0.3026 0.0046 0.0157 0.0081 346 VAL A CB 2687 C CG1 . VAL A 350 ? 0.2476 0.3061 0.2846 0.0019 0.0152 0.0058 346 VAL A CG1 2688 C CG2 . VAL A 350 ? 0.2421 0.3055 0.2757 0.0033 0.0129 0.0099 346 VAL A CG2 2689 N N . THR A 351 ? 0.2752 0.3191 0.3127 0.0090 0.0229 0.0069 347 THR A N 2690 C CA . THR A 351 ? 0.2799 0.3179 0.3194 0.0092 0.0260 0.0049 347 THR A CA 2691 C C . THR A 351 ? 0.2810 0.3144 0.3210 0.0079 0.0262 0.0051 347 THR A C 2692 O O . THR A 351 ? 0.2900 0.3214 0.3320 0.0058 0.0268 0.0028 347 THR A O 2693 C CB . THR A 351 ? 0.2900 0.3247 0.3290 0.0131 0.0296 0.0057 347 THR A CB 2694 O OG1 . THR A 351 ? 0.2927 0.3317 0.3318 0.0139 0.0296 0.0048 347 THR A OG1 2695 C CG2 . THR A 351 ? 0.2922 0.3194 0.3332 0.0134 0.0336 0.0041 347 THR A CG2 2696 N N . ARG A 352 ? 0.2658 0.2982 0.3038 0.0094 0.0257 0.0078 348 ARG A N 2697 C CA . ARG A 352 ? 0.2614 0.2892 0.2995 0.0089 0.0261 0.0083 348 ARG A CA 2698 C C . ARG A 352 ? 0.2694 0.2993 0.3080 0.0054 0.0230 0.0073 348 ARG A C 2699 O O . ARG A 352 ? 0.2907 0.3175 0.3308 0.0040 0.0238 0.0059 348 ARG A O 2700 C CB . ARG A 352 ? 0.2665 0.2941 0.3021 0.0115 0.0259 0.0114 348 ARG A CB 2701 C CG . ARG A 352 ? 0.2681 0.2922 0.3030 0.0156 0.0296 0.0128 348 ARG A CG 2702 C CD . ARG A 352 ? 0.2844 0.3113 0.3164 0.0188 0.0288 0.0158 348 ARG A CD 2703 N NE . ARG A 352 ? 0.2988 0.3219 0.3299 0.0231 0.0327 0.0173 348 ARG A NE 2704 C CZ . ARG A 352 ? 0.3190 0.3357 0.3499 0.0247 0.0357 0.0184 348 ARG A CZ 2705 N NH1 . ARG A 352 ? 0.2871 0.3013 0.3188 0.0224 0.0350 0.0179 348 ARG A NH1 2706 N NH2 . ARG A 352 ? 0.2771 0.2900 0.3070 0.0287 0.0395 0.0199 348 ARG A NH2 2707 N N . ILE A 353 ? 0.2544 0.2896 0.2918 0.0041 0.0199 0.0078 349 ILE A N 2708 C CA . ILE A 353 ? 0.2503 0.2870 0.2877 0.0013 0.0172 0.0071 349 ILE A CA 2709 C C . ILE A 353 ? 0.2559 0.2931 0.2957 -0.0006 0.0176 0.0042 349 ILE A C 2710 O O . ILE A 353 ? 0.2518 0.2875 0.2925 -0.0021 0.0173 0.0030 349 ILE A O 2711 C CB . ILE A 353 ? 0.2584 0.3003 0.2939 0.0002 0.0141 0.0085 349 ILE A CB 2712 C CG1 . ILE A 353 ? 0.2288 0.2706 0.2623 0.0017 0.0135 0.0109 349 ILE A CG1 2713 C CG2 . ILE A 353 ? 0.2340 0.2773 0.2696 -0.0026 0.0118 0.0078 349 ILE A CG2 2714 C CD1 . ILE A 353 ? 0.1956 0.2431 0.2275 0.0007 0.0111 0.0119 349 ILE A CD1 2715 N N . LEU A 354 ? 0.2437 0.2835 0.2844 -0.0003 0.0185 0.0029 350 LEU A N 2716 C CA . LEU A 354 ? 0.2421 0.2831 0.2852 -0.0019 0.0191 -0.0003 350 LEU A CA 2717 C C . LEU A 354 ? 0.2453 0.2812 0.2907 -0.0018 0.0221 -0.0023 350 LEU A C 2718 O O . LEU A 354 ? 0.2737 0.3102 0.3210 -0.0037 0.0220 -0.0048 350 LEU A O 2719 C CB . LEU A 354 ? 0.2487 0.2932 0.2922 -0.0013 0.0197 -0.0014 350 LEU A CB 2720 C CG . LEU A 354 ? 0.2520 0.3024 0.2936 -0.0018 0.0168 0.0002 350 LEU A CG 2721 C CD1 . LEU A 354 ? 0.2646 0.3184 0.3071 -0.0009 0.0180 -0.0014 350 LEU A CD1 2722 C CD2 . LEU A 354 ? 0.2308 0.2842 0.2720 -0.0042 0.0141 0.0000 350 LEU A CD2 2723 N N . ARG A 355 ? 0.2426 0.2737 0.2879 0.0004 0.0250 -0.0013 351 ARG A N 2724 C CA . ARG A 355 ? 0.2692 0.2949 0.3167 0.0002 0.0283 -0.0030 351 ARG A CA 2725 C C . ARG A 355 ? 0.2590 0.2837 0.3070 -0.0015 0.0271 -0.0032 351 ARG A C 2726 O O . ARG A 355 ? 0.2486 0.2724 0.2992 -0.0033 0.0283 -0.0061 351 ARG A O 2727 C CB . ARG A 355 ? 0.2711 0.2913 0.3177 0.0032 0.0315 -0.0008 351 ARG A CB 2728 C CG . ARG A 355 ? 0.3090 0.3227 0.3580 0.0030 0.0357 -0.0025 351 ARG A CG 2729 C CD . ARG A 355 ? 0.3139 0.3216 0.3615 0.0064 0.0393 0.0000 351 ARG A CD 2730 N NE . ARG A 355 ? 0.2799 0.2877 0.3271 0.0085 0.0410 -0.0001 351 ARG A NE 2731 C CZ . ARG A 355 ? 0.3330 0.3422 0.3775 0.0118 0.0407 0.0029 351 ARG A CZ 2732 N NH1 . ARG A 355 ? 0.2878 0.2982 0.3296 0.0135 0.0388 0.0062 351 ARG A NH1 2733 N NH2 . ARG A 355 ? 0.3383 0.3477 0.3827 0.0137 0.0424 0.0023 351 ARG A NH2 2734 N N . VAL A 356 ? 0.2503 0.2754 0.2958 -0.0009 0.0248 -0.0003 352 VAL A N 2735 C CA . VAL A 356 ? 0.2424 0.2662 0.2880 -0.0022 0.0237 -0.0003 352 VAL A CA 2736 C C . VAL A 356 ? 0.2389 0.2671 0.2856 -0.0046 0.0214 -0.0026 352 VAL A C 2737 O O . VAL A 356 ? 0.2253 0.2530 0.2740 -0.0059 0.0220 -0.0047 352 VAL A O 2738 C CB . VAL A 356 ? 0.2362 0.2595 0.2790 -0.0010 0.0218 0.0030 352 VAL A CB 2739 C CG1 . VAL A 356 ? 0.2400 0.2631 0.2826 -0.0024 0.0200 0.0028 352 VAL A CG1 2740 C CG2 . VAL A 356 ? 0.2215 0.2405 0.2634 0.0017 0.0244 0.0050 352 VAL A CG2 2741 N N . LYS A 357 ? 0.2253 0.2583 0.2707 -0.0050 0.0189 -0.0021 353 LYS A N 2742 C CA . LYS A 357 ? 0.2286 0.2662 0.2746 -0.0068 0.0167 -0.0039 353 LYS A CA 2743 C C . LYS A 357 ? 0.2366 0.2759 0.2858 -0.0079 0.0185 -0.0079 353 LYS A C 2744 O O . LYS A 357 ? 0.2334 0.2745 0.2838 -0.0091 0.0178 -0.0099 353 LYS A O 2745 C CB . LYS A 357 ? 0.2382 0.2802 0.2821 -0.0070 0.0144 -0.0025 353 LYS A CB 2746 C CG . LYS A 357 ? 0.2220 0.2632 0.2629 -0.0065 0.0123 0.0010 353 LYS A CG 2747 C CD . LYS A 357 ? 0.2071 0.2530 0.2463 -0.0071 0.0103 0.0021 353 LYS A CD 2748 C CE . LYS A 357 ? 0.2292 0.2743 0.2656 -0.0075 0.0081 0.0050 353 LYS A CE 2749 N NZ . LYS A 357 ? 0.2222 0.2718 0.2570 -0.0085 0.0062 0.0060 353 LYS A NZ 2750 N N . PHE A 358 ? 0.2480 0.2868 0.2986 -0.0074 0.0208 -0.0094 354 PHE A N 2751 C CA . PHE A 358 ? 0.2553 0.2952 0.3093 -0.0087 0.0228 -0.0137 354 PHE A CA 2752 C C . PHE A 358 ? 0.2590 0.2947 0.3154 -0.0095 0.0253 -0.0155 354 PHE A C 2753 O O . PHE A 358 ? 0.2551 0.2936 0.3140 -0.0113 0.0255 -0.0190 354 PHE A O 2754 C CB . PHE A 358 ? 0.2319 0.2709 0.2868 -0.0078 0.0253 -0.0149 354 PHE A CB 2755 C CG . PHE A 358 ? 0.2571 0.3020 0.3109 -0.0077 0.0232 -0.0149 354 PHE A CG 2756 C CD1 . PHE A 358 ? 0.2702 0.3213 0.3249 -0.0092 0.0215 -0.0176 354 PHE A CD1 2757 C CD2 . PHE A 358 ? 0.2380 0.2828 0.2896 -0.0059 0.0230 -0.0122 354 PHE A CD2 2758 C CE1 . PHE A 358 ? 0.2455 0.3023 0.2989 -0.0090 0.0196 -0.0174 354 PHE A CE1 2759 C CE2 . PHE A 358 ? 0.2787 0.3290 0.3292 -0.0058 0.0212 -0.0121 354 PHE A CE2 2760 C CZ . PHE A 358 ? 0.2524 0.3085 0.3039 -0.0074 0.0196 -0.0146 354 PHE A CZ 2761 N N . THR A 359 ? 0.2602 0.2900 0.3160 -0.0082 0.0274 -0.0133 355 THR A N 2762 C CA . THR A 359 ? 0.2656 0.2909 0.3236 -0.0090 0.0302 -0.0147 355 THR A CA 2763 C C . THR A 359 ? 0.2727 0.3006 0.3313 -0.0104 0.0281 -0.0155 355 THR A C 2764 O O . THR A 359 ? 0.2783 0.3066 0.3399 -0.0121 0.0297 -0.0188 355 THR A O 2765 C CB . THR A 359 ? 0.2715 0.2903 0.3278 -0.0067 0.0323 -0.0112 355 THR A CB 2766 O OG1 . THR A 359 ? 0.2900 0.3063 0.3460 -0.0051 0.0346 -0.0108 355 THR A OG1 2767 C CG2 . THR A 359 ? 0.2807 0.2943 0.3391 -0.0074 0.0355 -0.0121 355 THR A CG2 2768 N N . MET A 360 ? 0.2501 0.2799 0.3056 -0.0096 0.0247 -0.0126 356 MET A N 2769 C CA . MET A 360 ? 0.2522 0.2836 0.3075 -0.0103 0.0228 -0.0126 356 MET A CA 2770 C C . MET A 360 ? 0.2583 0.2963 0.3145 -0.0117 0.0207 -0.0153 356 MET A C 2771 O O . MET A 360 ? 0.2803 0.3207 0.3365 -0.0120 0.0190 -0.0158 356 MET A O 2772 C CB . MET A 360 ? 0.2571 0.2872 0.3086 -0.0089 0.0202 -0.0084 356 MET A CB 2773 C CG . MET A 360 ? 0.2422 0.2765 0.2910 -0.0088 0.0169 -0.0069 356 MET A CG 2774 S SD . MET A 360 ? 0.2655 0.2975 0.3103 -0.0075 0.0146 -0.0024 356 MET A SD 2775 C CE . MET A 360 ? 0.2296 0.2610 0.2742 -0.0078 0.0134 -0.0026 356 MET A CE 2776 N N . GLY A 361 ? 0.2472 0.2888 0.3043 -0.0121 0.0207 -0.0172 357 GLY A N 2777 C CA . GLY A 361 ? 0.2397 0.2884 0.2978 -0.0131 0.0189 -0.0200 357 GLY A CA 2778 C C . GLY A 361 ? 0.2393 0.2918 0.2940 -0.0123 0.0153 -0.0174 357 GLY A C 2779 O O . GLY A 361 ? 0.2290 0.2873 0.2837 -0.0126 0.0135 -0.0189 357 GLY A O 2780 N N . LEU A 362 ? 0.2399 0.3083 0.2953 -0.0062 0.0026 -0.0371 358 LEU A N 2781 C CA . LEU A 362 ? 0.2278 0.3039 0.2825 -0.0058 -0.0020 -0.0335 358 LEU A CA 2782 C C . LEU A 362 ? 0.2426 0.3281 0.2988 -0.0050 -0.0025 -0.0349 358 LEU A C 2783 O O . LEU A 362 ? 0.2382 0.3296 0.2931 -0.0047 -0.0043 -0.0333 358 LEU A O 2784 C CB . LEU A 362 ? 0.2410 0.3137 0.2939 -0.0040 -0.0042 -0.0286 358 LEU A CB 2785 C CG . LEU A 362 ? 0.2374 0.3148 0.2907 -0.0047 -0.0076 -0.0252 358 LEU A CG 2786 C CD1 . LEU A 362 ? 0.2498 0.3246 0.3003 -0.0063 -0.0088 -0.0242 358 LEU A CD1 2787 C CD2 . LEU A 362 ? 0.1881 0.2644 0.2423 -0.0028 -0.0099 -0.0229 358 LEU A CD2 2788 N N . PHE A 363 ? 0.2221 0.3079 0.2798 -0.0039 -0.0001 -0.0374 359 PHE A N 2789 C CA . PHE A 363 ? 0.2295 0.3235 0.2874 -0.0025 -0.0001 -0.0389 359 PHE A CA 2790 C C . PHE A 363 ? 0.2472 0.3474 0.3049 -0.0030 -0.0004 -0.0449 359 PHE A C 2791 O O . PHE A 363 ? 0.2611 0.3688 0.3166 -0.0006 -0.0012 -0.0456 359 PHE A O 2792 C CB . PHE A 363 ? 0.2265 0.3189 0.2856 -0.0008 0.0028 -0.0405 359 PHE A CB 2793 C CG . PHE A 363 ? 0.2235 0.3151 0.2836 0.0013 0.0024 -0.0354 359 PHE A CG 2794 C CD1 . PHE A 363 ? 0.2134 0.2984 0.2730 0.0022 0.0016 -0.0327 359 PHE A CD1 2795 C CD2 . PHE A 363 ? 0.2532 0.3515 0.3148 0.0033 0.0028 -0.0339 359 PHE A CD2 2796 C CE1 . PHE A 363 ? 0.2305 0.3174 0.2919 0.0051 0.0003 -0.0296 359 PHE A CE1 2797 C CE2 . PHE A 363 ? 0.2306 0.3306 0.2955 0.0051 0.0024 -0.0306 359 PHE A CE2 2798 C CZ . PHE A 363 ? 0.2326 0.3277 0.2977 0.0062 0.0007 -0.0290 359 PHE A CZ 2799 N N . GLU A 364 ? 0.2440 0.3418 0.3043 -0.0055 0.0005 -0.0497 360 GLU A N 2800 C CA . GLU A 364 ? 0.2494 0.3560 0.3114 -0.0057 -0.0006 -0.0571 360 GLU A CA 2801 C C . GLU A 364 ? 0.2725 0.3836 0.3322 -0.0048 -0.0039 -0.0550 360 GLU A C 2802 O O . GLU A 364 ? 0.2727 0.3941 0.3311 -0.0022 -0.0064 -0.0591 360 GLU A O 2803 C CB . GLU A 364 ? 0.2480 0.3508 0.3165 -0.0097 0.0031 -0.0651 360 GLU A CB 2804 C CG . GLU A 364 ? 0.2508 0.3524 0.3216 -0.0101 0.0067 -0.0707 360 GLU A CG 2805 C CD . GLU A 364 ? 0.2732 0.3655 0.3403 -0.0081 0.0090 -0.0638 360 GLU A CD 2806 O OE1 . GLU A 364 ? 0.2630 0.3435 0.3298 -0.0088 0.0126 -0.0608 360 GLU A OE1 2807 O OE2 . GLU A 364 ? 0.2898 0.3869 0.3538 -0.0049 0.0074 -0.0613 360 GLU A OE2 2808 N N . ASN A 365 ? 0.2539 0.3575 0.3124 -0.0061 -0.0040 -0.0490 361 ASN A N 2809 C CA . ASN A 365 ? 0.2630 0.3689 0.3184 -0.0049 -0.0066 -0.0461 361 ASN A CA 2810 C C . ASN A 365 ? 0.2525 0.3520 0.3037 -0.0045 -0.0073 -0.0375 361 ASN A C 2811 O O . ASN A 365 ? 0.2546 0.3468 0.3055 -0.0062 -0.0073 -0.0345 361 ASN A O 2812 C CB . ASN A 365 ? 0.2449 0.3487 0.3046 -0.0077 -0.0056 -0.0500 361 ASN A CB 2813 C CG . ASN A 365 ? 0.3151 0.4294 0.3810 -0.0083 -0.0055 -0.0603 361 ASN A CG 2814 O OD1 . ASN A 365 ? 0.3374 0.4629 0.4022 -0.0051 -0.0088 -0.0633 361 ASN A OD1 2815 N ND2 . ASN A 365 ? 0.2789 0.3899 0.3509 -0.0118 -0.0018 -0.0659 361 ASN A ND2 2816 N N . PRO A 366 ? 0.2577 0.3600 0.3061 -0.0022 -0.0073 -0.0340 362 PRO A N 2817 C CA . PRO A 366 ? 0.2571 0.3542 0.3041 -0.0029 -0.0072 -0.0274 362 PRO A CA 2818 C C . PRO A 366 ? 0.2496 0.3450 0.2920 -0.0020 -0.0079 -0.0240 362 PRO A C 2819 O O . PRO A 366 ? 0.2483 0.3379 0.2905 -0.0038 -0.0079 -0.0197 362 PRO A O 2820 C CB . PRO A 366 ? 0.2666 0.3673 0.3136 -0.0012 -0.0054 -0.0256 362 PRO A CB 2821 C CG . PRO A 366 ? 0.2781 0.3865 0.3223 0.0023 -0.0051 -0.0302 362 PRO A CG 2822 C CD . PRO A 366 ? 0.2564 0.3655 0.3040 0.0004 -0.0065 -0.0367 362 PRO A CD 2823 N N . TYR A 367 ? 0.2296 0.3305 0.2682 0.0012 -0.0085 -0.0261 363 TYR A N 2824 C CA . TYR A 367 ? 0.2473 0.3463 0.2798 0.0037 -0.0085 -0.0223 363 TYR A CA 2825 C C . TYR A 367 ? 0.2567 0.3550 0.2899 0.0030 -0.0103 -0.0245 363 TYR A C 2826 O O . TYR A 367 ? 0.2728 0.3745 0.3114 0.0012 -0.0112 -0.0303 363 TYR A O 2827 C CB . TYR A 367 ? 0.2465 0.3516 0.2714 0.0103 -0.0074 -0.0216 363 TYR A CB 2828 C CG . TYR A 367 ? 0.2603 0.3642 0.2839 0.0112 -0.0041 -0.0183 363 TYR A CG 2829 C CD1 . TYR A 367 ? 0.2874 0.3832 0.3105 0.0091 -0.0004 -0.0121 363 TYR A CD1 2830 C CD2 . TYR A 367 ? 0.2967 0.4075 0.3204 0.0137 -0.0039 -0.0219 363 TYR A CD2 2831 C CE1 . TYR A 367 ? 0.2828 0.3779 0.3064 0.0094 0.0038 -0.0094 363 TYR A CE1 2832 C CE2 . TYR A 367 ? 0.3133 0.4227 0.3359 0.0147 0.0000 -0.0184 363 TYR A CE2 2833 C CZ . TYR A 367 ? 0.3116 0.4133 0.3348 0.0123 0.0041 -0.0121 363 TYR A CZ 2834 O OH . TYR A 367 ? 0.3105 0.4112 0.3347 0.0126 0.0091 -0.0090 363 TYR A OH 2835 N N . ALA A 368 ? 0.2469 0.3404 0.2749 0.0044 -0.0100 -0.0202 364 ALA A N 2836 C CA . ALA A 368 ? 0.2607 0.3528 0.2889 0.0041 -0.0112 -0.0215 364 ALA A CA 2837 C C . ALA A 368 ? 0.2597 0.3636 0.2882 0.0083 -0.0129 -0.0271 364 ALA A C 2838 O O . ALA A 368 ? 0.2628 0.3744 0.2870 0.0137 -0.0133 -0.0281 364 ALA A O 2839 C CB . ALA A 368 ? 0.2472 0.3309 0.2691 0.0050 -0.0101 -0.0155 364 ALA A CB 2840 N N . ASP A 369 ? 0.2569 0.3626 0.2902 0.0067 -0.0136 -0.0310 365 ASP A N 2841 C CA . ASP A 369 ? 0.2605 0.3796 0.2961 0.0107 -0.0155 -0.0375 365 ASP A CA 2842 C C . ASP A 369 ? 0.2676 0.3861 0.2968 0.0156 -0.0160 -0.0339 365 ASP A C 2843 O O . ASP A 369 ? 0.2564 0.3677 0.2871 0.0128 -0.0149 -0.0321 365 ASP A O 2844 C CB . ASP A 369 ? 0.2414 0.3640 0.2891 0.0053 -0.0147 -0.0455 365 ASP A CB 2845 C CG . ASP A 369 ? 0.2952 0.4340 0.3493 0.0080 -0.0167 -0.0546 365 ASP A CG 2846 O OD1 . ASP A 369 ? 0.2586 0.4072 0.3069 0.0156 -0.0198 -0.0549 365 ASP A OD1 2847 O OD2 . ASP A 369 ? 0.2747 0.4157 0.3401 0.0027 -0.0147 -0.0616 365 ASP A OD2 2848 N N . PRO A 370 ? 0.2820 0.4070 0.3025 0.0238 -0.0172 -0.0325 366 PRO A N 2849 C CA . PRO A 370 ? 0.2881 0.4100 0.3011 0.0290 -0.0168 -0.0280 366 PRO A CA 2850 C C . PRO A 370 ? 0.2908 0.4220 0.3116 0.0291 -0.0186 -0.0343 366 PRO A C 2851 O O . PRO A 370 ? 0.2956 0.4212 0.3121 0.0311 -0.0176 -0.0303 366 PRO A O 2852 C CB . PRO A 370 ? 0.3140 0.4421 0.3152 0.0397 -0.0173 -0.0260 366 PRO A CB 2853 C CG . PRO A 370 ? 0.3316 0.4725 0.3374 0.0407 -0.0198 -0.0332 366 PRO A CG 2854 C CD . PRO A 370 ? 0.2829 0.4181 0.2992 0.0301 -0.0187 -0.0352 366 PRO A CD 2855 N N . ALA A 371 ? 0.2844 0.4288 0.3171 0.0265 -0.0205 -0.0442 367 ALA A N 2856 C CA . ALA A 371 ? 0.2814 0.4346 0.3247 0.0250 -0.0208 -0.0510 367 ALA A CA 2857 C C . ALA A 371 ? 0.2779 0.4162 0.3252 0.0172 -0.0168 -0.0475 367 ALA A C 2858 O O . ALA A 371 ? 0.2821 0.4231 0.3355 0.0164 -0.0155 -0.0504 367 ALA A O 2859 C CB . ALA A 371 ? 0.2936 0.4652 0.3507 0.0233 -0.0230 -0.0642 367 ALA A CB 2860 N N . MET A 372 ? 0.2514 0.3740 0.2945 0.0125 -0.0146 -0.0412 368 MET A N 2861 C CA . MET A 372 ? 0.2531 0.3616 0.2979 0.0068 -0.0112 -0.0381 368 MET A CA 2862 C C . MET A 372 ? 0.2470 0.3443 0.2813 0.0096 -0.0108 -0.0299 368 MET A C 2863 O O . MET A 372 ? 0.2504 0.3370 0.2843 0.0068 -0.0084 -0.0275 368 MET A O 2864 C CB . MET A 372 ? 0.2387 0.3369 0.2843 0.0015 -0.0096 -0.0363 368 MET A CB 2865 C CG . MET A 372 ? 0.2930 0.3985 0.3494 -0.0023 -0.0082 -0.0445 368 MET A CG 2866 S SD . MET A 372 ? 0.3785 0.4834 0.4467 -0.0070 -0.0029 -0.0509 368 MET A SD 2867 C CE . MET A 372 ? 0.3520 0.4347 0.4131 -0.0099 0.0010 -0.0430 368 MET A CE 2868 N N . ALA A 373 ? 0.2372 0.3357 0.2620 0.0157 -0.0124 -0.0257 369 ALA A N 2869 C CA . ALA A 373 ? 0.2472 0.3324 0.2615 0.0177 -0.0110 -0.0179 369 ALA A CA 2870 C C . ALA A 373 ? 0.2644 0.3480 0.2799 0.0185 -0.0098 -0.0183 369 ALA A C 2871 O O . ALA A 373 ? 0.2653 0.3350 0.2757 0.0165 -0.0081 -0.0137 369 ALA A O 2872 C CB . ALA A 373 ? 0.2594 0.3454 0.2628 0.0252 -0.0111 -0.0135 369 ALA A CB 2873 N N . GLU A 374 ? 0.2625 0.3611 0.2852 0.0214 -0.0108 -0.0247 370 GLU A N 2874 C CA . GLU A 374 ? 0.2869 0.3868 0.3122 0.0230 -0.0091 -0.0258 370 GLU A CA 2875 C C . GLU A 374 ? 0.2891 0.3807 0.3216 0.0159 -0.0055 -0.0272 370 GLU A C 2876 O O . GLU A 374 ? 0.2978 0.3873 0.3313 0.0169 -0.0030 -0.0269 370 GLU A O 2877 C CB . GLU A 374 ? 0.3030 0.4242 0.3358 0.0286 -0.0114 -0.0333 370 GLU A CB 2878 C CG . GLU A 374 ? 0.3381 0.4742 0.3848 0.0246 -0.0128 -0.0433 370 GLU A CG 2879 C CD . GLU A 374 ? 0.4976 0.6582 0.5501 0.0319 -0.0172 -0.0520 370 GLU A CD 2880 O OE1 . GLU A 374 ? 0.4417 0.6150 0.5061 0.0319 -0.0167 -0.0594 370 GLU A OE1 2881 O OE2 . GLU A 374 ? 0.5429 0.7107 0.5887 0.0377 -0.0209 -0.0523 370 GLU A OE2 2882 N N . GLN A 375 ? 0.2689 0.3543 0.3048 0.0099 -0.0044 -0.0280 371 GLN A N 2883 C CA . GLN A 375 ? 0.2661 0.3392 0.3043 0.0049 0.0000 -0.0274 371 GLN A CA 2884 C C . GLN A 375 ? 0.2744 0.3302 0.3006 0.0059 0.0006 -0.0197 371 GLN A C 2885 O O . GLN A 375 ? 0.2796 0.3254 0.3050 0.0044 0.0043 -0.0187 371 GLN A O 2886 C CB . GLN A 375 ? 0.2646 0.3337 0.3066 0.0000 0.0010 -0.0290 371 GLN A CB 2887 C CG . GLN A 375 ? 0.2807 0.3641 0.3357 -0.0025 0.0016 -0.0378 371 GLN A CG 2888 C CD . GLN A 375 ? 0.3155 0.4029 0.3826 -0.0055 0.0072 -0.0443 371 GLN A CD 2889 O OE1 . GLN A 375 ? 0.2796 0.3548 0.3451 -0.0068 0.0124 -0.0415 371 GLN A OE1 2890 N NE2 . GLN A 375 ? 0.3589 0.4636 0.4388 -0.0066 0.0067 -0.0536 371 GLN A NE2 2891 N N . LEU A 376 ? 0.2741 0.3257 0.2906 0.0086 -0.0025 -0.0147 372 LEU A N 2892 C CA . LEU A 376 ? 0.2752 0.3110 0.2809 0.0089 -0.0024 -0.0089 372 LEU A CA 2893 C C . LEU A 376 ? 0.2830 0.3150 0.2855 0.0120 0.0001 -0.0075 372 LEU A C 2894 O O . LEU A 376 ? 0.2668 0.3076 0.2697 0.0164 0.0000 -0.0081 372 LEU A O 2895 C CB . LEU A 376 ? 0.2724 0.3054 0.2705 0.0107 -0.0047 -0.0049 372 LEU A CB 2896 C CG . LEU A 376 ? 0.2939 0.3113 0.2834 0.0092 -0.0049 -0.0009 372 LEU A CG 2897 C CD1 . LEU A 376 ? 0.2665 0.2789 0.2580 0.0051 -0.0062 -0.0020 372 LEU A CD1 2898 C CD2 . LEU A 376 ? 0.3026 0.3163 0.2855 0.0109 -0.0048 0.0027 372 LEU A CD2 2899 N N . GLY A 377 ? 0.2823 0.3017 0.2807 0.0108 0.0023 -0.0057 373 GLY A N 2900 C CA . GLY A 377 ? 0.2684 0.2821 0.2624 0.0139 0.0052 -0.0039 373 GLY A CA 2901 C C . GLY A 377 ? 0.2942 0.3200 0.2987 0.0150 0.0086 -0.0082 373 GLY A C 2902 O O . GLY A 377 ? 0.2807 0.3061 0.2831 0.0186 0.0107 -0.0071 373 GLY A O 2903 N N . LYS A 378 ? 0.2928 0.3249 0.3014 0.0164 -0.0050 -0.0135 374 LYS A N 2904 C CA . LYS A 378 ? 0.3014 0.3380 0.3114 0.0164 -0.0058 -0.0181 374 LYS A CA 2905 C C . LYS A 378 ? 0.2949 0.3306 0.3077 0.0136 -0.0055 -0.0200 374 LYS A C 2906 O O . LYS A 378 ? 0.2697 0.3012 0.2834 0.0111 -0.0041 -0.0190 374 LYS A O 2907 C CB . LYS A 378 ? 0.2993 0.3372 0.3094 0.0159 -0.0052 -0.0208 374 LYS A CB 2908 C CG A LYS A 378 ? 0.3505 0.3935 0.3622 0.0159 -0.0058 -0.0261 374 LYS A CG 2909 C CG B LYS A 378 ? 0.2795 0.3237 0.2888 0.0189 -0.0067 -0.0237 374 LYS A CG 2910 C CD A LYS A 378 ? 0.3209 0.3642 0.3322 0.0156 -0.0050 -0.0282 374 LYS A CD 2911 C CD B LYS A 378 ? 0.2677 0.3134 0.2767 0.0189 -0.0063 -0.0262 374 LYS A CD 2912 C CE A LYS A 378 ? 0.3701 0.4084 0.3831 0.0117 -0.0026 -0.0293 374 LYS A CE 2913 C CE B LYS A 378 ? 0.2894 0.3423 0.2981 0.0216 -0.0079 -0.0301 374 LYS A CE 2914 N NZ A LYS A 378 ? 0.1940 0.2304 0.2068 0.0106 -0.0009 -0.0311 374 LYS A NZ 2915 N NZ B LYS A 378 ? 0.2503 0.3083 0.2583 0.0248 -0.0097 -0.0305 374 LYS A NZ 2916 N N . GLN A 379 ? 0.2818 0.3216 0.2958 0.0143 -0.0066 -0.0226 375 GLN A N 2917 C CA . GLN A 379 ? 0.2973 0.3366 0.3140 0.0118 -0.0062 -0.0244 375 GLN A CA 2918 C C . GLN A 379 ? 0.2989 0.3361 0.3179 0.0084 -0.0044 -0.0269 375 GLN A C 2919 O O . GLN A 379 ? 0.2919 0.3258 0.3121 0.0062 -0.0033 -0.0264 375 GLN A O 2920 C CB . GLN A 379 ? 0.2944 0.3397 0.3122 0.0133 -0.0077 -0.0277 375 GLN A CB 2921 C CG . GLN A 379 ? 0.3016 0.3464 0.3219 0.0111 -0.0074 -0.0290 375 GLN A CG 2922 C CD . GLN A 379 ? 0.3679 0.4080 0.3869 0.0113 -0.0073 -0.0247 375 GLN A CD 2923 O OE1 . GLN A 379 ? 0.4040 0.4436 0.4205 0.0139 -0.0080 -0.0217 375 GLN A OE1 2924 N NE2 . GLN A 379 ? 0.3455 0.3816 0.3660 0.0084 -0.0060 -0.0241 375 GLN A NE2 2925 N N . GLU A 380 ? 0.2775 0.3162 0.2968 0.0081 -0.0039 -0.0295 376 GLU A N 2926 C CA . GLU A 380 ? 0.2819 0.3176 0.3031 0.0048 -0.0016 -0.0317 376 GLU A CA 2927 C C . GLU A 380 ? 0.2815 0.3106 0.3011 0.0038 0.0000 -0.0276 376 GLU A C 2928 O O . GLU A 380 ? 0.2796 0.3050 0.3004 0.0014 0.0020 -0.0280 376 GLU A O 2929 C CB . GLU A 380 ? 0.2893 0.3274 0.3107 0.0048 -0.0011 -0.0351 376 GLU A CB 2930 C CG . GLU A 380 ? 0.3252 0.3709 0.3487 0.0056 -0.0027 -0.0402 376 GLU A CG 2931 C CD . GLU A 380 ? 0.3619 0.4124 0.3829 0.0097 -0.0051 -0.0392 376 GLU A CD 2932 O OE1 . GLU A 380 ? 0.3423 0.3907 0.3604 0.0119 -0.0059 -0.0345 376 GLU A OE1 2933 O OE2 . GLU A 380 ? 0.4286 0.4852 0.4503 0.0110 -0.0062 -0.0433 376 GLU A OE2 2934 N N . HIS A 381 ? 0.2502 0.2779 0.2672 0.0058 -0.0008 -0.0237 377 HIS A N 2935 C CA . HIS A 381 ? 0.2523 0.2747 0.2680 0.0051 0.0005 -0.0200 377 HIS A CA 2936 C C . HIS A 381 ? 0.2395 0.2602 0.2557 0.0045 0.0003 -0.0181 377 HIS A C 2937 O O . HIS A 381 ? 0.2608 0.2778 0.2770 0.0031 0.0017 -0.0168 377 HIS A O 2938 C CB . HIS A 381 ? 0.2348 0.2568 0.2479 0.0072 -0.0001 -0.0166 377 HIS A CB 2939 C CG . HIS A 381 ? 0.2697 0.2937 0.2818 0.0084 -0.0001 -0.0182 377 HIS A CG 2940 N ND1 . HIS A 381 ? 0.3316 0.3564 0.3449 0.0071 0.0009 -0.0221 377 HIS A ND1 2941 C CD2 . HIS A 381 ? 0.2339 0.2591 0.2438 0.0107 -0.0008 -0.0163 377 HIS A CD2 2942 C CE1 . HIS A 381 ? 0.2799 0.3066 0.2917 0.0087 0.0006 -0.0228 377 HIS A CE1 2943 N NE2 . HIS A 381 ? 0.3599 0.3870 0.3697 0.0110 -0.0005 -0.0192 377 HIS A NE2 2944 N N . ARG A 382 ? 0.2419 0.2653 0.2583 0.0057 -0.0015 -0.0177 378 ARG A N 2945 C CA . ARG A 382 ? 0.2367 0.2586 0.2538 0.0051 -0.0018 -0.0165 378 ARG A CA 2946 C C . ARG A 382 ? 0.2399 0.2613 0.2593 0.0028 -0.0006 -0.0192 378 ARG A C 2947 O O . ARG A 382 ? 0.2302 0.2486 0.2497 0.0017 0.0002 -0.0179 378 ARG A O 2948 C CB . ARG A 382 ? 0.2520 0.2768 0.2689 0.0070 -0.0036 -0.0161 378 ARG A CB 2949 C CG . ARG A 382 ? 0.2486 0.2730 0.2631 0.0093 -0.0042 -0.0128 378 ARG A CG 2950 C CD . ARG A 382 ? 0.2385 0.2648 0.2521 0.0116 -0.0055 -0.0119 378 ARG A CD 2951 N NE . ARG A 382 ? 0.2578 0.2835 0.2692 0.0138 -0.0054 -0.0089 378 ARG A NE 2952 C CZ . ARG A 382 ? 0.2916 0.3138 0.3025 0.0134 -0.0048 -0.0057 378 ARG A CZ 2953 N NH1 . ARG A 382 ? 0.2706 0.2901 0.2828 0.0111 -0.0043 -0.0050 378 ARG A NH1 2954 N NH2 . ARG A 382 ? 0.2863 0.3081 0.2954 0.0152 -0.0044 -0.0032 378 ARG A NH2 2955 N N . ASP A 383 ? 0.2329 0.2573 0.2540 0.0022 -0.0004 -0.0231 379 ASP A N 2956 C CA . ASP A 383 ? 0.2497 0.2734 0.2732 -0.0002 0.0013 -0.0259 379 ASP A CA 2957 C C . ASP A 383 ? 0.2475 0.2658 0.2704 -0.0018 0.0039 -0.0246 379 ASP A C 2958 O O . ASP A 383 ? 0.2454 0.2610 0.2690 -0.0032 0.0054 -0.0245 379 ASP A O 2959 C CB . ASP A 383 ? 0.2563 0.2844 0.2821 -0.0010 0.0014 -0.0308 379 ASP A CB 2960 C CG . ASP A 383 ? 0.3082 0.3424 0.3347 0.0008 -0.0011 -0.0324 379 ASP A CG 2961 O OD1 . ASP A 383 ? 0.2912 0.3253 0.3167 0.0023 -0.0024 -0.0298 379 ASP A OD1 2962 O OD2 . ASP A 383 ? 0.3452 0.3844 0.3732 0.0011 -0.0016 -0.0362 379 ASP A OD2 2963 N N . LEU A 384 ? 0.2465 0.2631 0.2676 -0.0013 0.0046 -0.0236 380 LEU A N 2964 C CA . LEU A 384 ? 0.2461 0.2575 0.2659 -0.0021 0.0072 -0.0221 380 LEU A CA 2965 C C . LEU A 384 ? 0.2468 0.2557 0.2650 -0.0013 0.0068 -0.0182 380 LEU A C 2966 O O . LEU A 384 ? 0.2552 0.2607 0.2731 -0.0020 0.0086 -0.0175 380 LEU A O 2967 C CB . LEU A 384 ? 0.2368 0.2475 0.2549 -0.0012 0.0077 -0.0218 380 LEU A CB 2968 C CG . LEU A 384 ? 0.2661 0.2717 0.2821 -0.0012 0.0102 -0.0197 380 LEU A CG 2969 C CD1 . LEU A 384 ? 0.2819 0.2839 0.2990 -0.0033 0.0136 -0.0220 380 LEU A CD1 2970 C CD2 . LEU A 384 ? 0.2639 0.2697 0.2782 0.0000 0.0102 -0.0193 380 LEU A CD2 2971 N N . ALA A 385 ? 0.2467 0.2573 0.2639 0.0003 0.0046 -0.0158 381 ALA A N 2972 C CA . ALA A 385 ? 0.2418 0.2506 0.2579 0.0009 0.0041 -0.0126 381 ALA A CA 2973 C C . ALA A 385 ? 0.2508 0.2592 0.2683 -0.0001 0.0043 -0.0132 381 ALA A C 2974 O O . ALA A 385 ? 0.2550 0.2611 0.2717 -0.0001 0.0050 -0.0115 381 ALA A O 2975 C CB . ALA A 385 ? 0.2541 0.2651 0.2697 0.0023 0.0019 -0.0106 381 ALA A CB 2976 N N . ARG A 386 ? 0.2434 0.2544 0.2626 -0.0005 0.0034 -0.0155 382 ARG A N 2977 C CA . ARG A 386 ? 0.2538 0.2648 0.2743 -0.0013 0.0034 -0.0163 382 ARG A CA 2978 C C . ARG A 386 ? 0.2613 0.2692 0.2823 -0.0028 0.0061 -0.0174 382 ARG A C 2979 O O . ARG A 386 ? 0.2599 0.2660 0.2808 -0.0030 0.0067 -0.0164 382 ARG A O 2980 C CB . ARG A 386 ? 0.2532 0.2684 0.2755 -0.0012 0.0019 -0.0188 382 ARG A CB 2981 C CG . ARG A 386 ? 0.2651 0.2810 0.2892 -0.0021 0.0020 -0.0204 382 ARG A CG 2982 C CD . ARG A 386 ? 0.3162 0.3371 0.3418 -0.0014 0.0003 -0.0228 382 ARG A CD 2983 N NE . ARG A 386 ? 0.2638 0.2860 0.2914 -0.0022 0.0004 -0.0245 382 ARG A NE 2984 C CZ . ARG A 386 ? 0.3171 0.3437 0.3458 -0.0013 -0.0011 -0.0265 382 ARG A CZ 2985 N NH1 . ARG A 386 ? 0.2881 0.3182 0.3160 0.0006 -0.0028 -0.0269 382 ARG A NH1 2986 N NH2 . ARG A 386 ? 0.2936 0.3213 0.3241 -0.0021 -0.0008 -0.0280 382 ARG A NH2 2987 N N . GLU A 387 ? 0.2777 0.2851 0.2994 -0.0038 0.0080 -0.0196 383 GLU A N 2988 C CA . GLU A 387 ? 0.2721 0.2756 0.2939 -0.0052 0.0114 -0.0204 383 GLU A CA 2989 C C . GLU A 387 ? 0.2697 0.2692 0.2886 -0.0039 0.0125 -0.0169 383 GLU A C 2990 O O . GLU A 387 ? 0.2880 0.2847 0.3062 -0.0040 0.0143 -0.0161 383 GLU A O 2991 C CB . GLU A 387 ? 0.2803 0.2835 0.3030 -0.0063 0.0132 -0.0231 383 GLU A CB 2992 C CG . GLU A 387 ? 0.3016 0.2994 0.3238 -0.0075 0.0175 -0.0236 383 GLU A CG 2993 C CD . GLU A 387 ? 0.3434 0.3402 0.3663 -0.0087 0.0196 -0.0264 383 GLU A CD 2994 O OE1 . GLU A 387 ? 0.3677 0.3687 0.3917 -0.0087 0.0177 -0.0285 383 GLU A OE1 2995 O OE2 . GLU A 387 ? 0.3368 0.3285 0.3588 -0.0094 0.0234 -0.0264 383 GLU A OE2 2996 N N . ALA A 388 ? 0.2436 0.2431 0.2605 -0.0026 0.0115 -0.0149 384 ALA A N 2997 C CA . ALA A 388 ? 0.2362 0.2328 0.2504 -0.0011 0.0126 -0.0118 384 ALA A CA 2998 C C . ALA A 388 ? 0.2481 0.2453 0.2619 -0.0003 0.0111 -0.0099 384 ALA A C 2999 O O . ALA A 388 ? 0.2440 0.2389 0.2561 0.0006 0.0126 -0.0084 384 ALA A O 3000 C CB . ALA A 388 ? 0.2284 0.2259 0.2409 0.0002 0.0114 -0.0101 384 ALA A CB 3001 N N . ALA A 389 ? 0.2371 0.2376 0.2523 -0.0004 0.0084 -0.0100 385 ALA A N 3002 C CA . ALA A 389 ? 0.2302 0.2313 0.2453 0.0001 0.0070 -0.0086 385 ALA A CA 3003 C C . ALA A 389 ? 0.2499 0.2493 0.2655 -0.0004 0.0086 -0.0095 385 ALA A C 3004 O O . ALA A 389 ? 0.2435 0.2416 0.2577 0.0005 0.0091 -0.0081 385 ALA A O 3005 C CB . ALA A 389 ? 0.2081 0.2123 0.2247 0.0001 0.0042 -0.0088 385 ALA A CB 3006 N N . ARG A 390 ? 0.2445 0.2444 0.2620 -0.0018 0.0093 -0.0120 386 ARG A N 3007 C CA . ARG A 390 ? 0.2558 0.2540 0.2739 -0.0026 0.0111 -0.0130 386 ARG A CA 3008 C C . ARG A 390 ? 0.2624 0.2562 0.2784 -0.0020 0.0146 -0.0119 386 ARG A C 3009 O O . ARG A 390 ? 0.2628 0.2548 0.2776 -0.0012 0.0158 -0.0108 386 ARG A O 3010 C CB . ARG A 390 ? 0.2583 0.2583 0.2793 -0.0043 0.0115 -0.0163 386 ARG A CB 3011 C CG . ARG A 390 ? 0.2933 0.2916 0.3156 -0.0055 0.0141 -0.0178 386 ARG A CG 3012 C CD . ARG A 390 ? 0.3282 0.3236 0.3512 -0.0070 0.0179 -0.0196 386 ARG A CD 3013 N NE . ARG A 390 ? 0.3917 0.3901 0.4170 -0.0083 0.0172 -0.0226 386 ARG A NE 3014 C CZ . ARG A 390 ? 0.4262 0.4229 0.4526 -0.0099 0.0201 -0.0249 386 ARG A CZ 3015 N NH1 . ARG A 390 ? 0.4367 0.4282 0.4621 -0.0104 0.0241 -0.0244 386 ARG A NH1 3016 N NH2 . ARG A 390 ? 0.4260 0.4263 0.4545 -0.0109 0.0190 -0.0278 386 ARG A NH2 3017 N N . LYS A 391 ? 0.2654 0.2573 0.2806 -0.0021 0.0164 -0.0121 387 LYS A N 3018 C CA . LYS A 391 ? 0.2745 0.2616 0.2871 -0.0012 0.0201 -0.0108 387 LYS A CA 3019 C C . LYS A 391 ? 0.2758 0.2622 0.2851 0.0014 0.0197 -0.0076 387 LYS A C 3020 O O . LYS A 391 ? 0.2770 0.2599 0.2838 0.0029 0.0226 -0.0063 387 LYS A O 3021 C CB . LYS A 391 ? 0.2842 0.2692 0.2965 -0.0019 0.0222 -0.0119 387 LYS A CB 3022 C CG . LYS A 391 ? 0.2789 0.2640 0.2946 -0.0047 0.0238 -0.0158 387 LYS A CG 3023 C CD . LYS A 391 ? 0.3165 0.3000 0.3322 -0.0055 0.0257 -0.0173 387 LYS A CD 3024 C CE . LYS A 391 ? 0.3629 0.3454 0.3819 -0.0084 0.0286 -0.0214 387 LYS A CE 3025 N NZ . LYS A 391 ? 0.3501 0.3308 0.3690 -0.0092 0.0305 -0.0231 387 LYS A NZ 3026 N N . SER A 392 ? 0.2764 0.2664 0.2858 0.0022 0.0164 -0.0065 388 SER A N 3027 C CA . SER A 392 ? 0.2735 0.2640 0.2803 0.0046 0.0156 -0.0040 388 SER A CA 3028 C C . SER A 392 ? 0.2715 0.2630 0.2781 0.0054 0.0148 -0.0034 388 SER A C 3029 O O . SER A 392 ? 0.2855 0.2774 0.2897 0.0077 0.0148 -0.0017 388 SER A O 3030 C CB . SER A 392 ? 0.2703 0.2645 0.2778 0.0047 0.0124 -0.0033 388 SER A CB 3031 O OG . SER A 392 ? 0.2922 0.2894 0.3020 0.0038 0.0096 -0.0040 388 SER A OG 3032 N N . LEU A 393 ? 0.2622 0.2547 0.2711 0.0039 0.0139 -0.0050 389 LEU A N 3033 C CA . LEU A 393 ? 0.2571 0.2508 0.2659 0.0047 0.0127 -0.0046 389 LEU A CA 3034 C C . LEU A 393 ? 0.2723 0.2629 0.2784 0.0065 0.0157 -0.0036 389 LEU A C 3035 O O . LEU A 393 ? 0.2756 0.2627 0.2815 0.0059 0.0190 -0.0042 389 LEU A O 3036 C CB . LEU A 393 ? 0.2597 0.2547 0.2714 0.0028 0.0115 -0.0065 389 LEU A CB 3037 C CG . LEU A 393 ? 0.2552 0.2527 0.2692 0.0013 0.0092 -0.0077 389 LEU A CG 3038 C CD1 . LEU A 393 ? 0.2531 0.2517 0.2694 -0.0001 0.0086 -0.0097 389 LEU A CD1 3039 C CD2 . LEU A 393 ? 0.2481 0.2482 0.2621 0.0019 0.0063 -0.0065 389 LEU A CD2 3040 N N . VAL A 394 ? 0.2635 0.2555 0.2677 0.0087 0.0149 -0.0023 390 VAL A N 3041 C CA . VAL A 394 ? 0.2815 0.2708 0.2826 0.0111 0.0178 -0.0011 390 VAL A CA 3042 C C . VAL A 394 ? 0.2859 0.2768 0.2877 0.0113 0.0166 -0.0016 390 VAL A C 3043 O O . VAL A 394 ? 0.2931 0.2877 0.2955 0.0118 0.0135 -0.0018 390 VAL A O 3044 C CB . VAL A 394 ? 0.2787 0.2684 0.2761 0.0145 0.0184 0.0010 390 VAL A CB 3045 C CG1 . VAL A 394 ? 0.2668 0.2536 0.2603 0.0178 0.0218 0.0025 390 VAL A CG1 3046 C CG2 . VAL A 394 ? 0.2724 0.2603 0.2691 0.0143 0.0198 0.0016 390 VAL A CG2 3047 N N . LEU A 395 ? 0.2853 0.2734 0.2873 0.0108 0.0190 -0.0022 391 LEU A N 3048 C CA . LEU A 395 ? 0.2865 0.2759 0.2890 0.0111 0.0180 -0.0027 391 LEU A CA 3049 C C . LEU A 395 ? 0.3034 0.2925 0.3019 0.0148 0.0192 -0.0009 391 LEU A C 3050 O O . LEU A 395 ? 0.3093 0.2946 0.3050 0.0166 0.0231 0.0004 391 LEU A O 3051 C CB . LEU A 395 ? 0.2796 0.2664 0.2839 0.0091 0.0206 -0.0040 391 LEU A CB 3052 C CG . LEU A 395 ? 0.2703 0.2579 0.2753 0.0092 0.0202 -0.0047 391 LEU A CG 3053 C CD1 . LEU A 395 ? 0.2632 0.2550 0.2706 0.0081 0.0157 -0.0059 391 LEU A CD1 3054 C CD2 . LEU A 395 ? 0.2703 0.2553 0.2774 0.0070 0.0231 -0.0062 391 LEU A CD2 3055 N N . LEU A 396 ? 0.2887 0.2819 0.2870 0.0162 0.0162 -0.0010 392 LEU A N 3056 C CA . LEU A 396 ? 0.3116 0.3058 0.3061 0.0202 0.0168 0.0003 392 LEU A CA 3057 C C . LEU A 396 ? 0.3271 0.3209 0.3208 0.0213 0.0174 0.0001 392 LEU A C 3058 O O . LEU A 396 ? 0.3319 0.3251 0.3217 0.0249 0.0193 0.0015 392 LEU A O 3059 C CB . LEU A 396 ? 0.2938 0.2934 0.2885 0.0212 0.0131 0.0000 392 LEU A CB 3060 C CG . LEU A 396 ? 0.3325 0.3328 0.3275 0.0208 0.0128 0.0006 392 LEU A CG 3061 C CD1 . LEU A 396 ? 0.3610 0.3670 0.3568 0.0214 0.0094 -0.0001 392 LEU A CD1 3062 C CD2 . LEU A 396 ? 0.2993 0.2959 0.2900 0.0237 0.0167 0.0027 392 LEU A CD2 3063 N N . LYS A 397 ? 0.3132 0.3078 0.3102 0.0186 0.0158 -0.0016 393 LYS A N 3064 C CA . LYS A 397 ? 0.3357 0.3302 0.3321 0.0196 0.0163 -0.0019 393 LYS A CA 3065 C C . LYS A 397 ? 0.3262 0.3197 0.3263 0.0161 0.0160 -0.0036 393 LYS A C 3066 O O . LYS A 397 ? 0.2981 0.2934 0.3014 0.0135 0.0135 -0.0048 393 LYS A O 3067 C CB . LYS A 397 ? 0.3306 0.3299 0.3267 0.0212 0.0127 -0.0027 393 LYS A CB 3068 C CG . LYS A 397 ? 0.3424 0.3425 0.3380 0.0223 0.0123 -0.0034 393 LYS A CG 3069 C CD . LYS A 397 ? 0.3267 0.3318 0.3225 0.0234 0.0086 -0.0047 393 LYS A CD 3070 C CE . LYS A 397 ? 0.3368 0.3425 0.3317 0.0250 0.0085 -0.0053 393 LYS A CE 3071 N NZ . LYS A 397 ? 0.3280 0.3389 0.3229 0.0263 0.0051 -0.0070 393 LYS A NZ 3072 N N . ASN A 398 ? 0.3264 0.3176 0.3262 0.0162 0.0185 -0.0036 394 ASN A N 3073 C CA . ASN A 398 ? 0.3348 0.3260 0.3384 0.0131 0.0182 -0.0054 394 ASN A CA 3074 C C . ASN A 398 ? 0.3768 0.3677 0.3794 0.0145 0.0191 -0.0055 394 ASN A C 3075 O O . ASN A 398 ? 0.3855 0.3734 0.3881 0.0142 0.0228 -0.0053 394 ASN A O 3076 C CB . ASN A 398 ? 0.3340 0.3219 0.3391 0.0109 0.0215 -0.0058 394 ASN A CB 3077 C CG . ASN A 398 ? 0.3205 0.3098 0.3300 0.0075 0.0206 -0.0082 394 ASN A CG 3078 O OD1 . ASN A 398 ? 0.3355 0.3228 0.3469 0.0055 0.0234 -0.0092 394 ASN A OD1 3079 N ND2 . ASN A 398 ? 0.2667 0.2594 0.2778 0.0070 0.0169 -0.0092 394 ASN A ND2 3080 N N . GLY A 399 ? 0.3796 0.3735 0.3813 0.0162 0.0163 -0.0057 395 GLY A N 3081 C CA . GLY A 399 ? 0.3755 0.3697 0.3758 0.0181 0.0169 -0.0056 395 GLY A CA 3082 C C . GLY A 399 ? 0.3865 0.3825 0.3830 0.0220 0.0160 -0.0047 395 GLY A C 3083 O O . GLY A 399 ? 0.3990 0.3941 0.3925 0.0244 0.0177 -0.0030 395 GLY A O 3084 N N . LYS A 400 ? 0.4081 0.4070 0.4047 0.0229 0.0133 -0.0058 396 LYS A N 3085 C CA . LYS A 400 ? 0.4037 0.4056 0.3970 0.0267 0.0121 -0.0055 396 LYS A CA 3086 C C . LYS A 400 ? 0.4265 0.4263 0.4154 0.0307 0.0157 -0.0036 396 LYS A C 3087 O O . LYS A 400 ? 0.4248 0.4266 0.4099 0.0347 0.0157 -0.0028 396 LYS A O 3088 C CB . LYS A 400 ? 0.4118 0.4172 0.4066 0.0264 0.0085 -0.0076 396 LYS A CB 3089 C CG . LYS A 400 ? 0.4249 0.4318 0.4237 0.0228 0.0052 -0.0094 396 LYS A CG 3090 C CD . LYS A 400 ? 0.4439 0.4545 0.4434 0.0232 0.0018 -0.0115 396 LYS A CD 3091 C CE . LYS A 400 ? 0.4555 0.4672 0.4586 0.0200 -0.0009 -0.0129 396 LYS A CE 3092 N NZ . LYS A 400 ? 0.4488 0.4622 0.4533 0.0193 -0.0036 -0.0151 396 LYS A NZ 3093 N N . THR A 401 ? 0.4046 0.4008 0.3938 0.0300 0.0189 -0.0030 397 THR A N 3094 C CA . THR A 401 ? 0.4274 0.4208 0.4123 0.0337 0.0230 -0.0009 397 THR A CA 3095 C C . THR A 401 ? 0.4420 0.4300 0.4278 0.0317 0.0276 0.0001 397 THR A C 3096 O O . THR A 401 ? 0.4359 0.4233 0.4261 0.0274 0.0271 -0.0013 397 THR A O 3097 C CB . THR A 401 ? 0.4347 0.4294 0.4187 0.0355 0.0226 -0.0015 397 THR A CB 3098 O OG1 . THR A 401 ? 0.4366 0.4291 0.4239 0.0322 0.0240 -0.0023 397 THR A OG1 3099 C CG2 . THR A 401 ? 0.4439 0.4439 0.4291 0.0355 0.0174 -0.0038 397 THR A CG2 3100 N N . SER A 402 ? 0.4498 0.4341 0.4316 0.0349 0.0323 0.0025 398 SER A N 3101 C CA . SER A 402 ? 0.4863 0.4649 0.4686 0.0333 0.0374 0.0035 398 SER A CA 3102 C C . SER A 402 ? 0.4796 0.4570 0.4657 0.0301 0.0388 0.0021 398 SER A C 3103 O O . SER A 402 ? 0.5089 0.4825 0.4972 0.0274 0.0426 0.0019 398 SER A O 3104 C CB . SER A 402 ? 0.4972 0.4716 0.4734 0.0383 0.0424 0.0066 398 SER A CB 3105 O OG . SER A 402 ? 0.5454 0.5198 0.5195 0.0411 0.0438 0.0073 398 SER A OG 3106 N N . THR A 403 ? 0.4566 0.4376 0.4436 0.0303 0.0357 0.0008 399 THR A N 3107 C CA . THR A 403 ? 0.4416 0.4221 0.4314 0.0283 0.0370 -0.0003 399 THR A CA 3108 C C . THR A 403 ? 0.3940 0.3784 0.3893 0.0240 0.0326 -0.0033 399 THR A C 3109 O O . THR A 403 ? 0.3735 0.3581 0.3722 0.0215 0.0334 -0.0048 399 THR A O 3110 C CB . THR A 403 ? 0.4620 0.4431 0.4475 0.0329 0.0377 0.0010 399 THR A CB 3111 O OG1 . THR A 403 ? 0.5872 0.5634 0.5708 0.0343 0.0438 0.0028 399 THR A OG1 3112 C CG2 . THR A 403 ? 0.4278 0.4133 0.4144 0.0330 0.0333 -0.0007 399 THR A CG2 3113 N N . ASP A 404 ? 0.3493 0.3367 0.3454 0.0233 0.0282 -0.0041 400 ASP A N 3114 C CA . ASP A 404 ? 0.3273 0.3178 0.3279 0.0197 0.0243 -0.0065 400 ASP A CA 3115 C C . ASP A 404 ? 0.3236 0.3126 0.3281 0.0159 0.0262 -0.0076 400 ASP A C 3116 O O . ASP A 404 ? 0.2976 0.2834 0.3014 0.0155 0.0296 -0.0066 400 ASP A O 3117 C CB . ASP A 404 ? 0.3133 0.3068 0.3138 0.0199 0.0199 -0.0070 400 ASP A CB 3118 C CG . ASP A 404 ? 0.3360 0.3324 0.3343 0.0226 0.0169 -0.0072 400 ASP A CG 3119 O OD1 . ASP A 404 ? 0.3394 0.3355 0.3352 0.0253 0.0182 -0.0066 400 ASP A OD1 3120 O OD2 . ASP A 404 ? 0.3360 0.3352 0.3352 0.0220 0.0131 -0.0082 400 ASP A OD2 3121 N N . ALA A 405 ? 0.2976 0.2890 0.3060 0.0132 0.0242 -0.0097 401 ALA A N 3122 C CA . ALA A 405 ? 0.2972 0.2889 0.3095 0.0097 0.0247 -0.0113 401 ALA A CA 3123 C C . ALA A 405 ? 0.3215 0.3133 0.3333 0.0092 0.0227 -0.0109 401 ALA A C 3124 O O . ALA A 405 ? 0.3079 0.3017 0.3185 0.0103 0.0192 -0.0106 401 ALA A O 3125 C CB . ALA A 405 ? 0.2869 0.2824 0.3029 0.0077 0.0218 -0.0137 401 ALA A CB 3126 N N . PRO A 406 ? 0.3183 0.3081 0.3312 0.0076 0.0252 -0.0110 402 PRO A N 3127 C CA . PRO A 406 ? 0.3341 0.3245 0.3468 0.0071 0.0231 -0.0107 402 PRO A CA 3128 C C . PRO A 406 ? 0.3193 0.3135 0.3348 0.0053 0.0188 -0.0125 402 PRO A C 3129 O O . PRO A 406 ? 0.3057 0.3017 0.3244 0.0033 0.0186 -0.0144 402 PRO A O 3130 C CB . PRO A 406 ? 0.3394 0.3267 0.3530 0.0054 0.0268 -0.0110 402 PRO A CB 3131 C CG . PRO A 406 ? 0.3859 0.3716 0.4016 0.0039 0.0308 -0.0122 402 PRO A CG 3132 C CD . PRO A 406 ? 0.3500 0.3372 0.3648 0.0057 0.0298 -0.0118 402 PRO A CD 3133 N N . LEU A 407 ? 0.2959 0.2916 0.3102 0.0062 0.0155 -0.0118 403 LEU A N 3134 C CA . LEU A 407 ? 0.2933 0.2920 0.3099 0.0048 0.0118 -0.0131 403 LEU A CA 3135 C C . LEU A 407 ? 0.2959 0.2952 0.3151 0.0025 0.0121 -0.0143 403 LEU A C 3136 O O . LEU A 407 ? 0.2765 0.2781 0.2982 0.0011 0.0106 -0.0160 403 LEU A O 3137 C CB . LEU A 407 ? 0.3214 0.3212 0.3364 0.0061 0.0088 -0.0122 403 LEU A CB 3138 C CG . LEU A 407 ? 0.3781 0.3802 0.3952 0.0049 0.0056 -0.0133 403 LEU A CG 3139 C CD1 . LEU A 407 ? 0.3305 0.3339 0.3488 0.0048 0.0045 -0.0146 403 LEU A CD1 3140 C CD2 . LEU A 407 ? 0.4224 0.4252 0.4383 0.0057 0.0032 -0.0126 403 LEU A CD2 3141 N N . LEU A 408 ? 0.2840 0.2811 0.3021 0.0024 0.0139 -0.0134 404 LEU A N 3142 C CA . LEU A 408 ? 0.2988 0.2964 0.3190 0.0004 0.0141 -0.0146 404 LEU A CA 3143 C C . LEU A 408 ? 0.3132 0.3089 0.3349 -0.0011 0.0181 -0.0157 404 LEU A C 3144 O O . LEU A 408 ? 0.3223 0.3147 0.3421 -0.0001 0.0214 -0.0145 404 LEU A O 3145 C CB . LEU A 408 ? 0.2838 0.2803 0.3021 0.0010 0.0137 -0.0130 404 LEU A CB 3146 C CG . LEU A 408 ? 0.2894 0.2877 0.3065 0.0023 0.0102 -0.0119 404 LEU A CG 3147 C CD1 . LEU A 408 ? 0.2661 0.2637 0.2816 0.0030 0.0100 -0.0105 404 LEU A CD1 3148 C CD2 . LEU A 408 ? 0.2496 0.2509 0.2690 0.0013 0.0070 -0.0133 404 LEU A CD2 3149 N N . PRO A 409 ? 0.3224 0.3203 0.3475 -0.0033 0.0180 -0.0181 405 PRO A N 3150 C CA . PRO A 409 ? 0.3157 0.3175 0.3424 -0.0039 0.0143 -0.0193 405 PRO A CA 3151 C C . PRO A 409 ? 0.3162 0.3211 0.3439 -0.0034 0.0118 -0.0201 405 PRO A C 3152 O O . PRO A 409 ? 0.2831 0.2883 0.3117 -0.0035 0.0131 -0.0209 405 PRO A O 3153 C CB . PRO A 409 ? 0.3137 0.3169 0.3434 -0.0062 0.0158 -0.0220 405 PRO A CB 3154 C CG . PRO A 409 ? 0.3781 0.3791 0.4091 -0.0074 0.0202 -0.0231 405 PRO A CG 3155 C CD . PRO A 409 ? 0.3385 0.3349 0.3656 -0.0054 0.0219 -0.0199 405 PRO A CD 3156 N N . LEU A 410 ? 0.2867 0.2936 0.3141 -0.0028 0.0085 -0.0198 406 LEU A N 3157 C CA . LEU A 410 ? 0.3090 0.3184 0.3369 -0.0020 0.0060 -0.0203 406 LEU A CA 3158 C C . LEU A 410 ? 0.3105 0.3238 0.3415 -0.0030 0.0057 -0.0230 406 LEU A C 3159 O O . LEU A 410 ? 0.2956 0.3103 0.3280 -0.0041 0.0061 -0.0243 406 LEU A O 3160 C CB . LEU A 410 ? 0.3019 0.3115 0.3284 -0.0009 0.0031 -0.0189 406 LEU A CB 3161 C CG . LEU A 410 ? 0.3339 0.3408 0.3578 0.0001 0.0027 -0.0167 406 LEU A CG 3162 C CD1 . LEU A 410 ? 0.3411 0.3483 0.3643 0.0005 0.0004 -0.0157 406 LEU A CD1 3163 C CD2 . LEU A 410 ? 0.3757 0.3822 0.3986 0.0012 0.0023 -0.0164 406 LEU A CD2 3164 N N . PRO A 411 ? 0.3077 0.3233 0.3395 -0.0024 0.0048 -0.0241 407 PRO A N 3165 C CA . PRO A 411 ? 0.3002 0.3206 0.3348 -0.0029 0.0041 -0.0267 407 PRO A CA 3166 C C . PRO A 411 ? 0.2955 0.3179 0.3293 -0.0016 0.0012 -0.0264 407 PRO A C 3167 O O . PRO A 411 ? 0.2750 0.2956 0.3065 -0.0001 -0.0006 -0.0244 407 PRO A O 3168 C CB . PRO A 411 ? 0.2850 0.3068 0.3201 -0.0021 0.0039 -0.0273 407 PRO A CB 3169 C CG . PRO A 411 ? 0.3213 0.3394 0.3532 -0.0005 0.0029 -0.0246 407 PRO A CG 3170 C CD . PRO A 411 ? 0.3173 0.3316 0.3476 -0.0011 0.0042 -0.0228 407 PRO A CD 3171 N N . LYS A 412 ? 0.2881 0.3144 0.3238 -0.0021 0.0009 -0.0286 408 LYS A N 3172 C CA . LYS A 412 ? 0.2906 0.3192 0.3253 -0.0004 -0.0017 -0.0284 408 LYS A CA 3173 C C . LYS A 412 ? 0.2864 0.3179 0.3208 0.0017 -0.0034 -0.0288 408 LYS A C 3174 O O . LYS A 412 ? 0.2925 0.3245 0.3250 0.0038 -0.0053 -0.0277 408 LYS A O 3175 C CB . LYS A 412 ? 0.2904 0.3229 0.3271 -0.0011 -0.0015 -0.0309 408 LYS A CB 3176 C CG . LYS A 412 ? 0.2886 0.3180 0.3252 -0.0029 0.0002 -0.0303 408 LYS A CG 3177 C CD . LYS A 412 ? 0.3153 0.3491 0.3542 -0.0037 0.0004 -0.0335 408 LYS A CD 3178 C CE . LYS A 412 ? 0.3690 0.3995 0.4079 -0.0055 0.0024 -0.0331 408 LYS A CE 3179 N NZ . LYS A 412 ? 0.3171 0.3521 0.3580 -0.0060 0.0021 -0.0363 408 LYS A NZ 3180 N N . LYS A 413 ? 0.2929 0.3261 0.3289 0.0014 -0.0026 -0.0303 409 LYS A N 3181 C CA . LYS A 413 ? 0.3070 0.3427 0.3426 0.0035 -0.0041 -0.0306 409 LYS A CA 3182 C C . LYS A 413 ? 0.3296 0.3613 0.3634 0.0039 -0.0039 -0.0287 409 LYS A C 3183 O O . LYS A 413 ? 0.3413 0.3718 0.3762 0.0025 -0.0021 -0.0291 409 LYS A O 3184 C CB . LYS A 413 ? 0.3242 0.3663 0.3631 0.0031 -0.0036 -0.0343 409 LYS A CB 3185 C CG . LYS A 413 ? 0.3585 0.4039 0.3967 0.0059 -0.0053 -0.0346 409 LYS A CG 3186 C CD . LYS A 413 ? 0.4150 0.4680 0.4565 0.0059 -0.0052 -0.0385 409 LYS A CD 3187 C CE . LYS A 413 ? 0.4781 0.5337 0.5185 0.0089 -0.0067 -0.0385 409 LYS A CE 3188 N NZ . LYS A 413 ? 0.5457 0.6102 0.5895 0.0094 -0.0069 -0.0426 409 LYS A NZ 3189 N N . ALA A 414 ? 0.3254 0.3550 0.3566 0.0060 -0.0055 -0.0268 410 ALA A N 3190 C CA . ALA A 414 ? 0.3241 0.3502 0.3535 0.0067 -0.0057 -0.0252 410 ALA A CA 3191 C C . ALA A 414 ? 0.3200 0.3457 0.3472 0.0093 -0.0075 -0.0243 410 ALA A C 3192 O O . ALA A 414 ? 0.3254 0.3519 0.3519 0.0103 -0.0083 -0.0239 410 ALA A O 3193 C CB . ALA A 414 ? 0.3127 0.3337 0.3406 0.0056 -0.0052 -0.0232 410 ALA A CB 3194 N N . PRO A 415 ? 0.3112 0.3354 0.3372 0.0105 -0.0078 -0.0239 411 PRO A N 3195 C CA . PRO A 415 ? 0.3128 0.3364 0.3366 0.0132 -0.0090 -0.0230 411 PRO A CA 3196 C C . PRO A 415 ? 0.3085 0.3277 0.3302 0.0133 -0.0094 -0.0209 411 PRO A C 3197 O O . PRO A 415 ? 0.3063 0.3259 0.3268 0.0152 -0.0100 -0.0202 411 PRO A O 3198 C CB . PRO A 415 ? 0.3218 0.3439 0.3447 0.0141 -0.0091 -0.0230 411 PRO A CB 3199 C CG . PRO A 415 ? 0.3321 0.3577 0.3576 0.0128 -0.0080 -0.0248 411 PRO A CG 3200 C CD . PRO A 415 ? 0.3055 0.3299 0.3323 0.0101 -0.0070 -0.0246 411 PRO A CD 3201 N N . LYS A 416 ? 0.3148 0.3303 0.3364 0.0115 -0.0090 -0.0198 412 LYS A N 3202 C CA . LYS A 416 ? 0.3132 0.3247 0.3333 0.0115 -0.0092 -0.0181 412 LYS A CA 3203 C C . LYS A 416 ? 0.2971 0.3069 0.3179 0.0092 -0.0088 -0.0177 412 LYS A C 3204 O O . LYS A 416 ? 0.2851 0.2948 0.3065 0.0084 -0.0083 -0.0182 412 LYS A O 3205 C CB . LYS A 416 ? 0.3324 0.3406 0.3507 0.0129 -0.0095 -0.0175 412 LYS A CB 3206 C CG . LYS A 416 ? 0.3907 0.3946 0.4077 0.0128 -0.0094 -0.0160 412 LYS A CG 3207 C CD . LYS A 416 ? 0.3829 0.3836 0.3981 0.0145 -0.0093 -0.0159 412 LYS A CD 3208 C CE . LYS A 416 ? 0.4527 0.4488 0.4670 0.0141 -0.0088 -0.0147 412 LYS A CE 3209 N NZ . LYS A 416 ? 0.4370 0.4294 0.4501 0.0149 -0.0084 -0.0149 412 LYS A NZ 3210 N N . ILE A 417 ? 0.2845 0.2934 0.3053 0.0084 -0.0087 -0.0167 413 ILE A N 3211 C CA . ILE A 417 ? 0.2724 0.2800 0.2936 0.0066 -0.0083 -0.0162 413 ILE A CA 3212 C C . ILE A 417 ? 0.2866 0.2913 0.3071 0.0063 -0.0085 -0.0149 413 ILE A C 3213 O O . ILE A 417 ? 0.2672 0.2708 0.2869 0.0073 -0.0087 -0.0141 413 ILE A O 3214 C CB . ILE A 417 ? 0.2900 0.2999 0.3124 0.0055 -0.0075 -0.0166 413 ILE A CB 3215 C CG1 . ILE A 417 ? 0.2916 0.3024 0.3139 0.0060 -0.0079 -0.0161 413 ILE A CG1 3216 C CG2 . ILE A 417 ? 0.2528 0.2657 0.2766 0.0054 -0.0069 -0.0183 413 ILE A CG2 3217 C CD1 . ILE A 417 ? 0.2762 0.2889 0.2997 0.0048 -0.0071 -0.0167 413 ILE A CD1 3218 N N . LEU A 418 ? 0.2782 0.2818 0.2989 0.0051 -0.0084 -0.0146 414 LEU A N 3219 C CA . LEU A 418 ? 0.2742 0.2757 0.2948 0.0044 -0.0085 -0.0138 414 LEU A CA 3220 C C . LEU A 418 ? 0.2748 0.2772 0.2959 0.0034 -0.0081 -0.0131 414 LEU A C 3221 O O . LEU A 418 ? 0.2788 0.2825 0.3002 0.0029 -0.0078 -0.0133 414 LEU A O 3222 C CB . LEU A 418 ? 0.2743 0.2747 0.2950 0.0039 -0.0088 -0.0145 414 LEU A CB 3223 C CG . LEU A 418 ? 0.2941 0.2930 0.3153 0.0028 -0.0088 -0.0143 414 LEU A CG 3224 C CD1 . LEU A 418 ? 0.2704 0.2665 0.2914 0.0030 -0.0084 -0.0136 414 LEU A CD1 3225 C CD2 . LEU A 418 ? 0.2682 0.2672 0.2897 0.0025 -0.0093 -0.0157 414 LEU A CD2 3226 N N . VAL A 419 ? 0.2587 0.2602 0.2798 0.0032 -0.0080 -0.0121 415 VAL A N 3227 C CA . VAL A 419 ? 0.2641 0.2662 0.2856 0.0023 -0.0078 -0.0113 415 VAL A CA 3228 C C . VAL A 419 ? 0.2759 0.2763 0.2980 0.0014 -0.0078 -0.0110 415 VAL A C 3229 O O . VAL A 419 ? 0.2842 0.2823 0.3061 0.0016 -0.0075 -0.0106 415 VAL A O 3230 C CB . VAL A 419 ? 0.2639 0.2666 0.2850 0.0029 -0.0075 -0.0105 415 VAL A CB 3231 C CG1 . VAL A 419 ? 0.2429 0.2460 0.2644 0.0020 -0.0072 -0.0096 415 VAL A CG1 3232 C CG2 . VAL A 419 ? 0.2321 0.2372 0.2533 0.0034 -0.0075 -0.0115 415 VAL A CG2 3233 N N . ALA A 420 ? 0.2649 0.2663 0.2875 0.0005 -0.0079 -0.0113 416 ALA A N 3234 C CA . ALA A 420 ? 0.2764 0.2772 0.3001 -0.0005 -0.0079 -0.0117 416 ALA A CA 3235 C C . ALA A 420 ? 0.2644 0.2671 0.2889 -0.0012 -0.0078 -0.0114 416 ALA A C 3236 O O . ALA A 420 ? 0.2745 0.2787 0.2982 -0.0008 -0.0077 -0.0108 416 ALA A O 3237 C CB . ALA A 420 ? 0.2635 0.2646 0.2875 -0.0006 -0.0085 -0.0134 416 ALA A CB 3238 N N . GLY A 421 ? 0.2579 0.2606 0.2838 -0.0024 -0.0078 -0.0119 417 GLY A N 3239 C CA . GLY A 421 ? 0.2622 0.2674 0.2891 -0.0031 -0.0078 -0.0120 417 GLY A CA 3240 C C . GLY A 421 ? 0.2605 0.2650 0.2883 -0.0039 -0.0070 -0.0107 417 GLY A C 3241 O O . GLY A 421 ? 0.2709 0.2733 0.2978 -0.0034 -0.0064 -0.0093 417 GLY A O 3242 N N . SER A 422 ? 0.2461 0.2527 0.2757 -0.0050 -0.0069 -0.0114 418 SER A N 3243 C CA . SER A 422 ? 0.2579 0.2644 0.2885 -0.0058 -0.0060 -0.0103 418 SER A CA 3244 C C . SER A 422 ? 0.2646 0.2714 0.2935 -0.0047 -0.0058 -0.0082 418 SER A C 3245 O O . SER A 422 ? 0.2735 0.2793 0.3027 -0.0050 -0.0049 -0.0069 418 SER A O 3246 C CB . SER A 422 ? 0.2627 0.2731 0.2956 -0.0070 -0.0063 -0.0117 418 SER A CB 3247 O OG . SER A 422 ? 0.2972 0.3109 0.3287 -0.0055 -0.0072 -0.0119 418 SER A OG 3248 N N . HIS A 423 ? 0.2575 0.2653 0.2846 -0.0034 -0.0063 -0.0081 419 HIS A N 3249 C CA . HIS A 423 ? 0.2461 0.2542 0.2718 -0.0026 -0.0059 -0.0066 419 HIS A CA 3250 C C . HIS A 423 ? 0.2558 0.2620 0.2800 -0.0016 -0.0059 -0.0062 419 HIS A C 3251 O O . HIS A 423 ? 0.2472 0.2537 0.2703 -0.0010 -0.0056 -0.0055 419 HIS A O 3252 C CB . HIS A 423 ? 0.2518 0.2623 0.2767 -0.0018 -0.0061 -0.0067 419 HIS A CB 3253 C CG . HIS A 423 ? 0.2594 0.2727 0.2855 -0.0023 -0.0062 -0.0070 419 HIS A CG 3254 N ND1 . HIS A 423 ? 0.2382 0.2531 0.2665 -0.0034 -0.0066 -0.0085 419 HIS A ND1 3255 C CD2 . HIS A 423 ? 0.2509 0.2661 0.2767 -0.0018 -0.0058 -0.0062 419 HIS A CD2 3256 C CE1 . HIS A 423 ? 0.2584 0.2765 0.2878 -0.0036 -0.0066 -0.0088 419 HIS A CE1 3257 N NE2 . HIS A 423 ? 0.2584 0.2767 0.2861 -0.0025 -0.0062 -0.0072 419 HIS A NE2 3258 N N . ALA A 424 ? 0.2577 0.2624 0.2819 -0.0016 -0.0062 -0.0069 420 ALA A N 3259 C CA . ALA A 424 ? 0.2748 0.2788 0.2978 -0.0006 -0.0062 -0.0069 420 ALA A CA 3260 C C . ALA A 424 ? 0.2713 0.2744 0.2938 0.0001 -0.0058 -0.0057 420 ALA A C 3261 O O . ALA A 424 ? 0.2641 0.2678 0.2856 0.0011 -0.0059 -0.0058 420 ALA A O 3262 C CB . ALA A 424 ? 0.2789 0.2818 0.3020 -0.0004 -0.0066 -0.0079 420 ALA A CB 3263 N N . ASP A 425 ? 0.2672 0.2688 0.2902 -0.0002 -0.0052 -0.0048 421 ASP A N 3264 C CA . ASP A 425 ? 0.2773 0.2777 0.2993 0.0009 -0.0045 -0.0034 421 ASP A CA 3265 C C . ASP A 425 ? 0.2781 0.2782 0.3008 0.0002 -0.0036 -0.0022 421 ASP A C 3266 O O . ASP A 425 ? 0.2919 0.2896 0.3149 0.0001 -0.0025 -0.0014 421 ASP A O 3267 C CB . ASP A 425 ? 0.2694 0.2671 0.2907 0.0018 -0.0041 -0.0033 421 ASP A CB 3268 C CG . ASP A 425 ? 0.3061 0.3029 0.3256 0.0039 -0.0034 -0.0018 421 ASP A CG 3269 O OD1 . ASP A 425 ? 0.2715 0.2706 0.2900 0.0051 -0.0039 -0.0017 421 ASP A OD1 3270 O OD2 . ASP A 425 ? 0.3041 0.2978 0.3229 0.0047 -0.0023 -0.0008 421 ASP A OD2 3271 N N . ASN A 426 ? 0.2760 0.2783 0.2991 -0.0003 -0.0038 -0.0021 422 ASN A N 3272 C CA . ASN A 426 ? 0.2688 0.2712 0.2928 -0.0010 -0.0030 -0.0011 422 ASN A CA 3273 C C . ASN A 426 ? 0.2662 0.2707 0.2893 -0.0004 -0.0032 -0.0005 422 ASN A C 3274 O O . ASN A 426 ? 0.2415 0.2478 0.2647 -0.0008 -0.0036 -0.0011 422 ASN A O 3275 C CB . ASN A 426 ? 0.2821 0.2855 0.3085 -0.0029 -0.0030 -0.0022 422 ASN A CB 3276 C CG . ASN A 426 ? 0.2941 0.2981 0.3219 -0.0039 -0.0020 -0.0014 422 ASN A CG 3277 O OD1 . ASN A 426 ? 0.2740 0.2788 0.3011 -0.0032 -0.0016 -0.0001 422 ASN A OD1 3278 N ND2 . ASN A 426 ? 0.2972 0.3009 0.3275 -0.0056 -0.0013 -0.0024 422 ASN A ND2 3279 N N . LEU A 427 ? 0.2448 0.2487 0.2665 0.0009 -0.0027 0.0007 423 LEU A N 3280 C CA . LEU A 427 ? 0.2656 0.2713 0.2863 0.0016 -0.0028 0.0011 423 LEU A CA 3281 C C . LEU A 427 ? 0.2628 0.2698 0.2844 0.0008 -0.0024 0.0016 423 LEU A C 3282 O O . LEU A 427 ? 0.2526 0.2611 0.2736 0.0009 -0.0026 0.0013 423 LEU A O 3283 C CB . LEU A 427 ? 0.2539 0.2592 0.2730 0.0034 -0.0023 0.0022 423 LEU A CB 3284 C CG . LEU A 427 ? 0.3099 0.3171 0.3278 0.0044 -0.0026 0.0020 423 LEU A CG 3285 C CD1 . LEU A 427 ? 0.3071 0.3155 0.3249 0.0042 -0.0034 0.0001 423 LEU A CD1 3286 C CD2 . LEU A 427 ? 0.2979 0.3052 0.3140 0.0066 -0.0023 0.0030 423 LEU A CD2 3287 N N . GLY A 428 ? 0.2666 0.2731 0.2896 0.0000 -0.0015 0.0025 424 GLY A N 3288 C CA . GLY A 428 ? 0.2434 0.2521 0.2675 -0.0008 -0.0012 0.0028 424 GLY A CA 3289 C C . GLY A 428 ? 0.2491 0.2599 0.2739 -0.0015 -0.0021 0.0014 424 GLY A C 3290 O O . GLY A 428 ? 0.2423 0.2552 0.2667 -0.0011 -0.0021 0.0015 424 GLY A O 3291 N N . TYR A 429 ? 0.2500 0.2603 0.2757 -0.0022 -0.0027 0.0000 425 TYR A N 3292 C CA . TYR A 429 ? 0.2469 0.2594 0.2729 -0.0023 -0.0034 -0.0013 425 TYR A CA 3293 C C . TYR A 429 ? 0.2416 0.2541 0.2653 -0.0010 -0.0036 -0.0013 425 TYR A C 3294 O O . TYR A 429 ? 0.2435 0.2578 0.2665 -0.0004 -0.0037 -0.0014 425 TYR A O 3295 C CB . TYR A 429 ? 0.2353 0.2472 0.2623 -0.0031 -0.0040 -0.0029 425 TYR A CB 3296 C CG . TYR A 429 ? 0.2506 0.2631 0.2804 -0.0047 -0.0037 -0.0038 425 TYR A CG 3297 C CD1 . TYR A 429 ? 0.2476 0.2608 0.2790 -0.0056 -0.0027 -0.0030 425 TYR A CD1 3298 C CD2 . TYR A 429 ? 0.2953 0.3078 0.3263 -0.0055 -0.0042 -0.0056 425 TYR A CD2 3299 C CE1 . TYR A 429 ? 0.2777 0.2917 0.3123 -0.0076 -0.0021 -0.0043 425 TYR A CE1 3300 C CE2 . TYR A 429 ? 0.3126 0.3258 0.3465 -0.0073 -0.0038 -0.0070 425 TYR A CE2 3301 C CZ . TYR A 429 ? 0.3253 0.3392 0.3611 -0.0085 -0.0027 -0.0064 425 TYR A CZ 3302 O OH . TYR A 429 ? 0.3324 0.3471 0.3717 -0.0106 -0.0020 -0.0082 425 TYR A OH 3303 N N . GLN A 430 ? 0.2349 0.2454 0.2573 -0.0005 -0.0036 -0.0011 426 GLN A N 3304 C CA . GLN A 430 ? 0.2628 0.2732 0.2835 0.0003 -0.0034 -0.0015 426 GLN A CA 3305 C C . GLN A 430 ? 0.2469 0.2578 0.2664 0.0011 -0.0027 -0.0005 426 GLN A C 3306 O O . GLN A 430 ? 0.2386 0.2492 0.2568 0.0017 -0.0022 -0.0007 426 GLN A O 3307 C CB . GLN A 430 ? 0.2767 0.2856 0.2969 0.0005 -0.0036 -0.0023 426 GLN A CB 3308 C CG . GLN A 430 ? 0.3082 0.3167 0.3280 0.0011 -0.0036 -0.0019 426 GLN A CG 3309 C CD . GLN A 430 ? 0.3237 0.3319 0.3432 0.0014 -0.0039 -0.0031 426 GLN A CD 3310 O OE1 . GLN A 430 ? 0.3047 0.3123 0.3248 0.0012 -0.0044 -0.0037 426 GLN A OE1 3311 N NE2 . GLN A 430 ? 0.2285 0.2374 0.2474 0.0020 -0.0037 -0.0037 426 GLN A NE2 3312 N N . CYS A 431 ? 0.2335 0.2449 0.2535 0.0011 -0.0026 0.0006 427 CYS A N 3313 C CA . CYS A 431 ? 0.2372 0.2493 0.2561 0.0018 -0.0019 0.0015 427 CYS A CA 3314 C C . CYS A 431 ? 0.2406 0.2548 0.2599 0.0019 -0.0017 0.0020 427 CYS A C 3315 O O . CYS A 431 ? 0.2513 0.2660 0.2692 0.0029 -0.0011 0.0026 427 CYS A O 3316 C CB . CYS A 431 ? 0.2395 0.2512 0.2584 0.0021 -0.0017 0.0026 427 CYS A CB 3317 S SG . CYS A 431 ? 0.2507 0.2612 0.2685 0.0029 -0.0020 0.0020 427 CYS A SG 3318 N N . GLY A 432 ? 0.2461 0.2618 0.2674 0.0010 -0.0022 0.0016 428 GLY A N 3319 C CA . GLY A 432 ? 0.2238 0.2427 0.2459 0.0011 -0.0022 0.0016 428 GLY A CA 3320 C C . GLY A 432 ? 0.2438 0.2640 0.2663 0.0013 -0.0015 0.0029 428 GLY A C 3321 O O . GLY A 432 ? 0.2487 0.2673 0.2713 0.0010 -0.0011 0.0038 428 GLY A O 3322 N N . GLY A 433 ? 0.2393 0.2626 0.2616 0.0021 -0.0014 0.0031 429 GLY A N 3323 C CA . GLY A 433 ? 0.2299 0.2552 0.2531 0.0021 -0.0008 0.0041 429 GLY A CA 3324 C C . GLY A 433 ? 0.2413 0.2644 0.2622 0.0032 -0.0001 0.0056 429 GLY A C 3325 O O . GLY A 433 ? 0.2382 0.2585 0.2569 0.0039 -0.0001 0.0055 429 GLY A O 3326 N N . TRP A 434 ? 0.2337 0.2581 0.2551 0.0034 0.0005 0.0068 430 TRP A N 3327 C CA . TRP A 434 ? 0.2421 0.2649 0.2614 0.0045 0.0012 0.0081 430 TRP A CA 3328 C C . TRP A 434 ? 0.2566 0.2760 0.2750 0.0044 0.0010 0.0080 430 TRP A C 3329 O O . TRP A 434 ? 0.2469 0.2646 0.2631 0.0053 0.0011 0.0078 430 TRP A O 3330 C CB . TRP A 434 ? 0.2405 0.2633 0.2570 0.0063 0.0015 0.0083 430 TRP A CB 3331 C CG . TRP A 434 ? 0.2607 0.2871 0.2774 0.0072 0.0017 0.0088 430 TRP A CG 3332 C CD1 . TRP A 434 ? 0.3175 0.3461 0.3337 0.0081 0.0015 0.0081 430 TRP A CD1 3333 C CD2 . TRP A 434 ? 0.2778 0.3066 0.2951 0.0077 0.0023 0.0100 430 TRP A CD2 3334 N NE1 . TRP A 434 ? 0.2830 0.3156 0.2995 0.0092 0.0018 0.0087 430 TRP A NE1 3335 C CE2 . TRP A 434 ? 0.3016 0.3342 0.3189 0.0087 0.0023 0.0098 430 TRP A CE2 3336 C CE3 . TRP A 434 ? 0.2663 0.2943 0.2839 0.0075 0.0029 0.0112 430 TRP A CE3 3337 C CZ2 . TRP A 434 ? 0.3267 0.3628 0.3446 0.0094 0.0028 0.0108 430 TRP A CZ2 3338 C CZ3 . TRP A 434 ? 0.2586 0.2897 0.2767 0.0081 0.0036 0.0123 430 TRP A CZ3 3339 C CH2 . TRP A 434 ? 0.2748 0.3099 0.2933 0.0089 0.0035 0.0120 430 TRP A CH2 3340 N N . THR A 435 ? 0.2463 0.2648 0.2665 0.0032 0.0010 0.0079 431 THR A N 3341 C CA . THR A 435 ? 0.2482 0.2641 0.2673 0.0036 0.0009 0.0079 431 THR A CA 3342 C C . THR A 435 ? 0.2674 0.2827 0.2881 0.0031 0.0018 0.0091 431 THR A C 3343 O O . THR A 435 ? 0.2667 0.2820 0.2896 0.0015 0.0020 0.0087 431 THR A O 3344 C CB . THR A 435 ? 0.2750 0.2896 0.2944 0.0029 0.0000 0.0064 431 THR A CB 3345 O OG1 . THR A 435 ? 0.2651 0.2802 0.2835 0.0032 -0.0003 0.0055 431 THR A OG1 3346 C CG2 . THR A 435 ? 0.2486 0.2613 0.2666 0.0038 -0.0002 0.0063 431 THR A CG2 3347 N N . ILE A 436 ? 0.2560 0.2708 0.2752 0.0044 0.0025 0.0106 432 ILE A N 3348 C CA . ILE A 436 ? 0.2588 0.2724 0.2787 0.0045 0.0040 0.0122 432 ILE A CA 3349 C C . ILE A 436 ? 0.2776 0.2932 0.3001 0.0031 0.0051 0.0128 432 ILE A C 3350 O O . ILE A 436 ? 0.2873 0.3033 0.3094 0.0039 0.0063 0.0144 432 ILE A O 3351 C CB . ILE A 436 ? 0.2708 0.2816 0.2910 0.0042 0.0043 0.0122 432 ILE A CB 3352 C CG1 . ILE A 436 ? 0.2687 0.2786 0.2866 0.0057 0.0031 0.0113 432 ILE A CG1 3353 C CG2 . ILE A 436 ? 0.2542 0.2631 0.2746 0.0047 0.0066 0.0143 432 ILE A CG2 3354 C CD1 . ILE A 436 ? 0.2890 0.2994 0.3039 0.0083 0.0031 0.0121 432 ILE A CD1 3355 N N . GLU A 437 ? 0.2766 0.2941 0.3017 0.0013 0.0046 0.0113 433 GLU A N 3356 C CA . GLU A 437 ? 0.2991 0.3200 0.3268 0.0001 0.0053 0.0112 433 GLU A CA 3357 C C . GLU A 437 ? 0.2908 0.3149 0.3181 0.0005 0.0039 0.0101 433 GLU A C 3358 O O . GLU A 437 ? 0.2909 0.3140 0.3166 0.0011 0.0027 0.0091 433 GLU A O 3359 C CB . GLU A 437 ? 0.3063 0.3273 0.3378 -0.0024 0.0060 0.0100 433 GLU A CB 3360 C CG . GLU A 437 ? 0.3542 0.3714 0.3860 -0.0028 0.0079 0.0113 433 GLU A CG 3361 C CD . GLU A 437 ? 0.3469 0.3645 0.3793 -0.0025 0.0100 0.0133 433 GLU A CD 3362 O OE1 . GLU A 437 ? 0.3618 0.3834 0.3952 -0.0025 0.0099 0.0133 433 GLU A OE1 3363 O OE2 . GLU A 437 ? 0.3525 0.3664 0.3841 -0.0019 0.0118 0.0149 433 GLU A OE2 3364 N N . ALA A 438 ? 0.3021 0.3302 0.3310 0.0003 0.0042 0.0100 434 ALA A N 3365 C CA . ALA A 438 ? 0.2963 0.3275 0.3243 0.0013 0.0031 0.0089 434 ALA A CA 3366 C C . ALA A 438 ? 0.2926 0.3247 0.3217 0.0004 0.0019 0.0069 434 ALA A C 3367 O O . ALA A 438 ? 0.2998 0.3319 0.3267 0.0017 0.0010 0.0064 434 ALA A O 3368 C CB . ALA A 438 ? 0.3210 0.3576 0.3506 0.0015 0.0035 0.0091 434 ALA A CB 3369 N N . GLN A 439 ? 0.2830 0.3157 0.3156 -0.0018 0.0022 0.0057 435 GLN A N 3370 C CA . GLN A 439 ? 0.2840 0.3178 0.3181 -0.0028 0.0012 0.0035 435 GLN A CA 3371 C C . GLN A 439 ? 0.2950 0.3239 0.3274 -0.0029 0.0008 0.0035 435 GLN A C 3372 O O . GLN A 439 ? 0.2842 0.3135 0.3174 -0.0035 -0.0001 0.0018 435 GLN A O 3373 C CB . GLN A 439 ? 0.2994 0.3359 0.3383 -0.0054 0.0018 0.0018 435 GLN A CB 3374 C CG . GLN A 439 ? 0.2953 0.3383 0.3366 -0.0055 0.0020 0.0010 435 GLN A CG 3375 C CD . GLN A 439 ? 0.3337 0.3813 0.3737 -0.0036 0.0003 -0.0004 435 GLN A CD 3376 O OE1 . GLN A 439 ? 0.2995 0.3468 0.3387 -0.0033 -0.0009 -0.0018 435 GLN A OE1 3377 N NE2 . GLN A 439 ? 0.3111 0.3632 0.3506 -0.0020 0.0003 0.0001 435 GLN A NE2 3378 N N . GLY A 440 ? 0.2842 0.3094 0.3142 -0.0019 0.0012 0.0052 436 GLY A N 3379 C CA . GLY A 440 ? 0.2700 0.2911 0.2989 -0.0020 0.0010 0.0051 436 GLY A CA 3380 C C . GLY A 440 ? 0.2821 0.3016 0.3136 -0.0039 0.0018 0.0046 436 GLY A C 3381 O O . GLY A 440 ? 0.2604 0.2816 0.2947 -0.0052 0.0030 0.0046 436 GLY A O 3382 N N . ASP A 441 ? 0.2669 0.2834 0.2978 -0.0041 0.0015 0.0040 437 ASP A N 3383 C CA . ASP A 441 ? 0.2819 0.2956 0.3147 -0.0054 0.0027 0.0039 437 ASP A CA 3384 C C . ASP A 441 ? 0.2928 0.3041 0.3245 -0.0052 0.0018 0.0029 437 ASP A C 3385 O O . ASP A 441 ? 0.2939 0.3059 0.3237 -0.0041 0.0003 0.0024 437 ASP A O 3386 C CB . ASP A 441 ? 0.2751 0.2859 0.3066 -0.0045 0.0045 0.0063 437 ASP A CB 3387 C CG . ASP A 441 ? 0.3388 0.3467 0.3725 -0.0060 0.0067 0.0066 437 ASP A CG 3388 O OD1 . ASP A 441 ? 0.3365 0.3446 0.3732 -0.0082 0.0070 0.0048 437 ASP A OD1 3389 O OD2 . ASP A 441 ? 0.3597 0.3650 0.3920 -0.0049 0.0084 0.0088 437 ASP A OD2 3390 N N . THR A 442 ? 0.3138 0.3223 0.3468 -0.0063 0.0028 0.0027 438 THR A N 3391 C CA . THR A 442 ? 0.2856 0.2917 0.3179 -0.0062 0.0021 0.0016 438 THR A CA 3392 C C . THR A 442 ? 0.2988 0.3008 0.3286 -0.0046 0.0030 0.0033 438 THR A C 3393 O O . THR A 442 ? 0.2964 0.2964 0.3260 -0.0042 0.0049 0.0051 438 THR A O 3394 C CB . THR A 442 ? 0.3012 0.3070 0.3367 -0.0086 0.0027 -0.0003 438 THR A CB 3395 O OG1 . THR A 442 ? 0.2795 0.2831 0.3141 -0.0083 0.0020 -0.0013 438 THR A OG1 3396 C CG2 . THR A 442 ? 0.3183 0.3215 0.3561 -0.0101 0.0055 0.0005 438 THR A CG2 3397 N N . GLY A 443 ? 0.2827 0.2839 0.3106 -0.0033 0.0018 0.0029 439 GLY A N 3398 C CA . GLY A 443 ? 0.2786 0.2763 0.3043 -0.0016 0.0025 0.0041 439 GLY A CA 3399 C C . GLY A 443 ? 0.2924 0.2910 0.3153 0.0008 0.0020 0.0053 439 GLY A C 3400 O O . GLY A 443 ? 0.2717 0.2732 0.2942 0.0010 0.0008 0.0048 439 GLY A O 3401 N N . ARG A 444 ? 0.2846 0.2808 0.3054 0.0029 0.0031 0.0069 440 ARG A N 3402 C CA . ARG A 444 ? 0.3043 0.3019 0.3223 0.0055 0.0024 0.0075 440 ARG A CA 3403 C C . ARG A 444 ? 0.3192 0.3175 0.3367 0.0062 0.0035 0.0093 440 ARG A C 3404 O O . ARG A 444 ? 0.3022 0.2985 0.3181 0.0080 0.0051 0.0112 440 ARG A O 3405 C CB . ARG A 444 ? 0.3244 0.3199 0.3400 0.0080 0.0029 0.0082 440 ARG A CB 3406 C CG . ARG A 444 ? 0.3727 0.3709 0.3856 0.0110 0.0017 0.0081 440 ARG A CG 3407 C CD . ARG A 444 ? 0.4517 0.4499 0.4632 0.0129 0.0010 0.0073 440 ARG A CD 3408 N NE A ARG A 444 ? 0.4952 0.4972 0.5070 0.0126 -0.0011 0.0050 440 ARG A NE 3409 N NE B ARG A 444 ? 0.4466 0.4447 0.4600 0.0106 0.0000 0.0054 440 ARG A NE 3410 C CZ A ARG A 444 ? 0.4520 0.4547 0.4658 0.0103 -0.0021 0.0032 440 ARG A CZ 3411 C CZ B ARG A 444 ? 0.4451 0.4447 0.4582 0.0113 -0.0014 0.0037 440 ARG A CZ 3412 N NH1 A ARG A 444 ? 0.4256 0.4260 0.4411 0.0083 -0.0017 0.0031 440 ARG A NH1 3413 N NH1 B ARG A 444 ? 0.4429 0.4446 0.4540 0.0141 -0.0020 0.0034 440 ARG A NH1 3414 N NH2 A ARG A 444 ? 0.3502 0.3561 0.3643 0.0102 -0.0034 0.0013 440 ARG A NH2 3415 N NH2 B ARG A 444 ? 0.4311 0.4305 0.4460 0.0092 -0.0021 0.0022 440 ARG A NH2 3416 N N . THR A 445 ? 0.2889 0.2899 0.3075 0.0049 0.0027 0.0087 441 THR A N 3417 C CA . THR A 445 ? 0.3042 0.3061 0.3229 0.0051 0.0037 0.0101 441 THR A CA 3418 C C . THR A 445 ? 0.3004 0.3041 0.3165 0.0075 0.0031 0.0106 441 THR A C 3419 O O . THR A 445 ? 0.2988 0.3031 0.3143 0.0083 0.0039 0.0120 441 THR A O 3420 C CB . THR A 445 ? 0.3031 0.3074 0.3241 0.0029 0.0032 0.0092 441 THR A CB 3421 O OG1 . THR A 445 ? 0.3223 0.3286 0.3428 0.0029 0.0014 0.0076 441 THR A OG1 3422 C CG2 . THR A 445 ? 0.3142 0.3178 0.3383 0.0004 0.0038 0.0083 441 THR A CG2 3423 N N . THR A 446 ? 0.2935 0.2983 0.3083 0.0086 0.0016 0.0092 442 THR A N 3424 C CA . THR A 446 ? 0.2872 0.2941 0.2998 0.0107 0.0009 0.0089 442 THR A CA 3425 C C . THR A 446 ? 0.2921 0.2999 0.3036 0.0119 -0.0004 0.0071 442 THR A C 3426 O O . THR A 446 ? 0.2877 0.2941 0.2996 0.0118 -0.0004 0.0069 442 THR A O 3427 C CB . THR A 446 ? 0.2800 0.2890 0.2932 0.0096 0.0003 0.0081 442 THR A CB 3428 O OG1 . THR A 446 ? 0.3120 0.3229 0.3232 0.0115 -0.0001 0.0077 442 THR A OG1 3429 C CG2 . THR A 446 ? 0.2401 0.2497 0.2547 0.0077 -0.0008 0.0060 442 THR A CG2 3430 N N . VAL A 447 ? 0.2693 0.2798 0.2797 0.0132 -0.0014 0.0058 443 VAL A N 3431 C CA . VAL A 447 ? 0.2528 0.2652 0.2626 0.0144 -0.0025 0.0038 443 VAL A CA 3432 C C . VAL A 447 ? 0.2662 0.2794 0.2779 0.0120 -0.0034 0.0014 443 VAL A C 3433 O O . VAL A 447 ? 0.2695 0.2832 0.2818 0.0107 -0.0033 0.0007 443 VAL A O 3434 C CB . VAL A 447 ? 0.2632 0.2788 0.2709 0.0172 -0.0030 0.0031 443 VAL A CB 3435 C CG1 . VAL A 447 ? 0.2721 0.2907 0.2798 0.0182 -0.0044 0.0002 443 VAL A CG1 3436 C CG2 . VAL A 447 ? 0.2769 0.2914 0.2819 0.0204 -0.0019 0.0058 443 VAL A CG2 3437 N N . GLY A 448 ? 0.2369 0.2498 0.2494 0.0115 -0.0039 0.0002 444 GLY A N 3438 C CA . GLY A 448 ? 0.2505 0.2638 0.2646 0.0094 -0.0044 -0.0018 444 GLY A CA 3439 C C . GLY A 448 ? 0.2721 0.2853 0.2868 0.0093 -0.0049 -0.0029 444 GLY A C 3440 O O . GLY A 448 ? 0.2614 0.2746 0.2750 0.0113 -0.0051 -0.0023 444 GLY A O 3441 N N . THR A 449 ? 0.2517 0.2647 0.2678 0.0075 -0.0051 -0.0043 445 THR A N 3442 C CA . THR A 449 ? 0.2570 0.2700 0.2739 0.0072 -0.0055 -0.0055 445 THR A CA 3443 C C . THR A 449 ? 0.2547 0.2654 0.2726 0.0053 -0.0052 -0.0051 445 THR A C 3444 O O . THR A 449 ? 0.2447 0.2553 0.2632 0.0040 -0.0048 -0.0055 445 THR A O 3445 C CB . THR A 449 ? 0.2526 0.2685 0.2703 0.0071 -0.0059 -0.0084 445 THR A CB 3446 O OG1 . THR A 449 ? 0.2281 0.2471 0.2449 0.0091 -0.0064 -0.0092 445 THR A OG1 3447 C CG2 . THR A 449 ? 0.2444 0.2607 0.2628 0.0071 -0.0064 -0.0095 445 THR A CG2 3448 N N . THR A 450 ? 0.2458 0.2547 0.2639 0.0054 -0.0053 -0.0042 446 THR A N 3449 C CA . THR A 450 ? 0.2454 0.2528 0.2645 0.0037 -0.0052 -0.0042 446 THR A CA 3450 C C . THR A 450 ? 0.2420 0.2501 0.2617 0.0032 -0.0055 -0.0060 446 THR A C 3451 O O . THR A 450 ? 0.2454 0.2552 0.2650 0.0039 -0.0058 -0.0074 446 THR A O 3452 C CB . THR A 450 ? 0.2468 0.2520 0.2661 0.0037 -0.0050 -0.0032 446 THR A CB 3453 O OG1 . THR A 450 ? 0.2390 0.2439 0.2576 0.0050 -0.0053 -0.0037 446 THR A OG1 3454 C CG2 . THR A 450 ? 0.2560 0.2600 0.2748 0.0042 -0.0041 -0.0012 446 THR A CG2 3455 N N . ILE A 451 ? 0.2386 0.2458 0.2589 0.0021 -0.0054 -0.0062 447 ILE A N 3456 C CA . ILE A 451 ? 0.2466 0.2543 0.2674 0.0017 -0.0055 -0.0077 447 ILE A CA 3457 C C . ILE A 451 ? 0.2456 0.2534 0.2664 0.0026 -0.0061 -0.0084 447 ILE A C 3458 O O . ILE A 451 ? 0.2506 0.2599 0.2717 0.0028 -0.0061 -0.0099 447 ILE A O 3459 C CB . ILE A 451 ? 0.2642 0.2710 0.2853 0.0009 -0.0053 -0.0076 447 ILE A CB 3460 C CG1 . ILE A 451 ? 0.2326 0.2397 0.2532 0.0006 -0.0045 -0.0071 447 ILE A CG1 3461 C CG2 . ILE A 451 ? 0.2595 0.2663 0.2807 0.0008 -0.0052 -0.0089 447 ILE A CG2 3462 C CD1 . ILE A 451 ? 0.2707 0.2776 0.2912 0.0003 -0.0044 -0.0067 447 ILE A CD1 3463 N N . LEU A 452 ? 0.2529 0.2590 0.2733 0.0030 -0.0063 -0.0074 448 LEU A N 3464 C CA . LEU A 452 ? 0.2551 0.2610 0.2751 0.0042 -0.0067 -0.0078 448 LEU A CA 3465 C C . LEU A 452 ? 0.2574 0.2656 0.2766 0.0060 -0.0070 -0.0083 448 LEU A C 3466 O O . LEU A 452 ? 0.2668 0.2768 0.2862 0.0068 -0.0074 -0.0097 448 LEU A O 3467 C CB . LEU A 452 ? 0.2642 0.2672 0.2838 0.0045 -0.0064 -0.0065 448 LEU A CB 3468 C CG . LEU A 452 ? 0.2415 0.2434 0.2599 0.0064 -0.0064 -0.0063 448 LEU A CG 3469 C CD1 . LEU A 452 ? 0.2520 0.2544 0.2708 0.0062 -0.0070 -0.0079 448 LEU A CD1 3470 C CD2 . LEU A 452 ? 0.2535 0.2514 0.2713 0.0066 -0.0053 -0.0047 448 LEU A CD2 3471 N N . GLU A 453 ? 0.2538 0.2623 0.2723 0.0067 -0.0067 -0.0073 449 GLU A N 3472 C CA . GLU A 453 ? 0.2592 0.2708 0.2770 0.0085 -0.0071 -0.0081 449 GLU A CA 3473 C C . GLU A 453 ? 0.2537 0.2685 0.2728 0.0077 -0.0073 -0.0105 449 GLU A C 3474 O O . GLU A 453 ? 0.2596 0.2776 0.2788 0.0090 -0.0079 -0.0122 449 GLU A O 3475 C CB . GLU A 453 ? 0.2745 0.2859 0.2911 0.0094 -0.0067 -0.0066 449 GLU A CB 3476 C CG . GLU A 453 ? 0.3039 0.3124 0.3191 0.0107 -0.0060 -0.0043 449 GLU A CG 3477 C CD . GLU A 453 ? 0.4095 0.4169 0.4240 0.0109 -0.0052 -0.0024 449 GLU A CD 3478 O OE1 . GLU A 453 ? 0.2996 0.3082 0.3147 0.0099 -0.0052 -0.0025 449 GLU A OE1 3479 O OE2 . GLU A 453 ? 0.4951 0.4998 0.5084 0.0121 -0.0042 -0.0005 449 GLU A OE2 3480 N N . ALA A 454 ? 0.2354 0.2494 0.2555 0.0057 -0.0068 -0.0108 450 ALA A N 3481 C CA . ALA A 454 ? 0.2271 0.2433 0.2486 0.0045 -0.0063 -0.0131 450 ALA A CA 3482 C C . ALA A 454 ? 0.2546 0.2717 0.2772 0.0042 -0.0064 -0.0146 450 ALA A C 3483 O O . ALA A 454 ? 0.2489 0.2689 0.2728 0.0041 -0.0063 -0.0170 450 ALA A O 3484 C CB . ALA A 454 ? 0.2084 0.2227 0.2302 0.0028 -0.0053 -0.0126 450 ALA A CB 3485 N N . VAL A 455 ? 0.2466 0.2611 0.2688 0.0041 -0.0065 -0.0135 451 VAL A N 3486 C CA . VAL A 455 ? 0.2547 0.2699 0.2777 0.0040 -0.0067 -0.0148 451 VAL A CA 3487 C C . VAL A 455 ? 0.2654 0.2835 0.2882 0.0060 -0.0075 -0.0158 451 VAL A C 3488 O O . VAL A 455 ? 0.2674 0.2886 0.2916 0.0059 -0.0075 -0.0181 451 VAL A O 3489 C CB . VAL A 455 ? 0.2435 0.2556 0.2658 0.0039 -0.0068 -0.0135 451 VAL A CB 3490 C CG1 . VAL A 455 ? 0.2631 0.2760 0.2859 0.0043 -0.0070 -0.0146 451 VAL A CG1 3491 C CG2 . VAL A 455 ? 0.2324 0.2427 0.2550 0.0023 -0.0060 -0.0128 451 VAL A CG2 3492 N N . LYS A 456 ? 0.2543 0.2716 0.2754 0.0078 -0.0081 -0.0143 452 LYS A N 3493 C CA . LYS A 456 ? 0.2764 0.2964 0.2966 0.0104 -0.0089 -0.0150 452 LYS A CA 3494 C C . LYS A 456 ? 0.2677 0.2929 0.2889 0.0110 -0.0092 -0.0173 452 LYS A C 3495 O O . LYS A 456 ? 0.2789 0.3081 0.3004 0.0126 -0.0098 -0.0191 452 LYS A O 3496 C CB . LYS A 456 ? 0.2745 0.2921 0.2923 0.0126 -0.0089 -0.0125 452 LYS A CB 3497 C CG . LYS A 456 ? 0.3055 0.3183 0.3226 0.0121 -0.0084 -0.0108 452 LYS A CG 3498 C CD . LYS A 456 ? 0.3726 0.3823 0.3875 0.0138 -0.0078 -0.0083 452 LYS A CD 3499 C CE . LYS A 456 ? 0.4253 0.4303 0.4398 0.0132 -0.0071 -0.0071 452 LYS A CE 3500 N NZ . LYS A 456 ? 0.4717 0.4734 0.4842 0.0150 -0.0059 -0.0047 452 LYS A NZ 3501 N N . ALA A 457 ? 0.2671 0.2926 0.2888 0.0099 -0.0088 -0.0174 453 ALA A N 3502 C CA . ALA A 457 ? 0.2676 0.2980 0.2905 0.0100 -0.0090 -0.0201 453 ALA A CA 3503 C C . ALA A 457 ? 0.2825 0.3153 0.3083 0.0079 -0.0084 -0.0231 453 ALA A C 3504 O O . ALA A 457 ? 0.2734 0.3112 0.3008 0.0080 -0.0086 -0.0261 453 ALA A O 3505 C CB . ALA A 457 ? 0.2572 0.2869 0.2797 0.0094 -0.0086 -0.0194 453 ALA A CB 3506 N N . ALA A 458 ? 0.2672 0.2965 0.2938 0.0058 -0.0074 -0.0224 454 ALA A N 3507 C CA . ALA A 458 ? 0.2791 0.3096 0.3083 0.0035 -0.0061 -0.0249 454 ALA A CA 3508 C C . ALA A 458 ? 0.2843 0.3170 0.3147 0.0039 -0.0063 -0.0264 454 ALA A C 3509 O O . ALA A 458 ? 0.2922 0.3281 0.3254 0.0024 -0.0054 -0.0294 454 ALA A O 3510 C CB . ALA A 458 ? 0.2991 0.3246 0.3281 0.0014 -0.0045 -0.0234 454 ALA A CB 3511 N N . VAL A 459 ? 0.2692 0.2998 0.2979 0.0053 -0.0071 -0.0245 455 VAL A N 3512 C CA . VAL A 459 ? 0.2631 0.2949 0.2928 0.0054 -0.0071 -0.0256 455 VAL A CA 3513 C C . VAL A 459 ? 0.2840 0.3219 0.3146 0.0074 -0.0081 -0.0280 455 VAL A C 3514 O O . VAL A 459 ? 0.2804 0.3209 0.3098 0.0095 -0.0092 -0.0282 455 VAL A O 3515 C CB . VAL A 459 ? 0.2347 0.2623 0.2623 0.0064 -0.0075 -0.0230 455 VAL A CB 3516 C CG1 . VAL A 459 ? 0.2323 0.2551 0.2594 0.0045 -0.0065 -0.0213 455 VAL A CG1 3517 C CG2 . VAL A 459 ? 0.2592 0.2858 0.2842 0.0089 -0.0088 -0.0211 455 VAL A CG2 3518 N N . ASP A 460 ? 0.3060 0.3462 0.3384 0.0069 -0.0078 -0.0299 456 ASP A N 3519 C CA . ASP A 460 ? 0.3009 0.3476 0.3345 0.0088 -0.0087 -0.0326 456 ASP A CA 3520 C C . ASP A 460 ? 0.2914 0.3374 0.3215 0.0125 -0.0103 -0.0304 456 ASP A C 3521 O O . ASP A 460 ? 0.2935 0.3338 0.3211 0.0129 -0.0103 -0.0273 456 ASP A O 3522 C CB . ASP A 460 ? 0.3012 0.3486 0.3367 0.0077 -0.0078 -0.0339 456 ASP A CB 3523 C CG . ASP A 460 ? 0.3590 0.4140 0.3966 0.0091 -0.0086 -0.0372 456 ASP A CG 3524 O OD1 . ASP A 460 ? 0.3503 0.4067 0.3860 0.0122 -0.0099 -0.0365 456 ASP A OD1 3525 O OD2 . ASP A 460 ? 0.4064 0.4659 0.4475 0.0072 -0.0077 -0.0406 456 ASP A OD2 3526 N N . PRO A 461 ? 0.2877 0.3397 0.3176 0.0153 -0.0115 -0.0320 457 PRO A N 3527 C CA . PRO A 461 ? 0.2931 0.3442 0.3193 0.0193 -0.0126 -0.0298 457 PRO A CA 3528 C C . PRO A 461 ? 0.3063 0.3540 0.3308 0.0205 -0.0125 -0.0281 457 PRO A C 3529 O O . PRO A 461 ? 0.3042 0.3480 0.3253 0.0230 -0.0127 -0.0253 457 PRO A O 3530 C CB . PRO A 461 ? 0.3002 0.3599 0.3268 0.0223 -0.0138 -0.0327 457 PRO A CB 3531 C CG . PRO A 461 ? 0.2751 0.3404 0.3065 0.0194 -0.0134 -0.0370 457 PRO A CG 3532 C CD . PRO A 461 ? 0.2895 0.3491 0.3221 0.0152 -0.0119 -0.0360 457 PRO A CD 3533 N N . SER A 462 ? 0.3015 0.3507 0.3285 0.0188 -0.0121 -0.0299 458 SER A N 3534 C CA . SER A 462 ? 0.3221 0.3681 0.3476 0.0198 -0.0120 -0.0285 458 SER A CA 3535 C C . SER A 462 ? 0.3194 0.3575 0.3438 0.0177 -0.0112 -0.0257 458 SER A C 3536 O O . SER A 462 ? 0.3285 0.3631 0.3512 0.0186 -0.0112 -0.0243 458 SER A O 3537 C CB . SER A 462 ? 0.3249 0.3757 0.3534 0.0191 -0.0118 -0.0314 458 SER A CB 3538 O OG . SER A 462 ? 0.3282 0.3777 0.3595 0.0151 -0.0104 -0.0324 458 SER A OG 3539 N N . THR A 463 ? 0.3027 0.3383 0.3279 0.0151 -0.0106 -0.0251 459 THR A N 3540 C CA . THR A 463 ? 0.2932 0.3225 0.3175 0.0133 -0.0099 -0.0229 459 THR A CA 3541 C C . THR A 463 ? 0.3032 0.3280 0.3245 0.0149 -0.0103 -0.0202 459 THR A C 3542 O O . THR A 463 ? 0.3034 0.3283 0.3239 0.0155 -0.0104 -0.0194 459 THR A O 3543 C CB . THR A 463 ? 0.2982 0.3266 0.3242 0.0103 -0.0090 -0.0232 459 THR A CB 3544 O OG1 . THR A 463 ? 0.2844 0.3161 0.3132 0.0087 -0.0081 -0.0257 459 THR A OG1 3545 C CG2 . THR A 463 ? 0.2658 0.2883 0.2907 0.0089 -0.0084 -0.0210 459 THR A CG2 3546 N N . VAL A 464 ? 0.2920 0.3126 0.3118 0.0153 -0.0102 -0.0188 460 VAL A N 3547 C CA . VAL A 464 ? 0.2935 0.3094 0.3109 0.0164 -0.0100 -0.0165 460 VAL A CA 3548 C C . VAL A 464 ? 0.2916 0.3040 0.3097 0.0136 -0.0095 -0.0154 460 VAL A C 3549 O O . VAL A 464 ? 0.2943 0.3055 0.3134 0.0118 -0.0093 -0.0159 460 VAL A O 3550 C CB . VAL A 464 ? 0.2717 0.2847 0.2873 0.0181 -0.0099 -0.0158 460 VAL A CB 3551 C CG1 . VAL A 464 ? 0.3140 0.3208 0.3273 0.0187 -0.0092 -0.0134 460 VAL A CG1 3552 C CG2 . VAL A 464 ? 0.3111 0.3281 0.3256 0.0216 -0.0104 -0.0167 460 VAL A CG2 3553 N N . VAL A 465 ? 0.2926 0.3032 0.3099 0.0136 -0.0093 -0.0140 461 VAL A N 3554 C CA . VAL A 465 ? 0.2873 0.2952 0.3053 0.0112 -0.0088 -0.0131 461 VAL A CA 3555 C C . VAL A 465 ? 0.3063 0.3094 0.3230 0.0114 -0.0083 -0.0114 461 VAL A C 3556 O O . VAL A 465 ? 0.3003 0.3019 0.3153 0.0132 -0.0079 -0.0101 461 VAL A O 3557 C CB . VAL A 465 ? 0.2957 0.3054 0.3141 0.0108 -0.0087 -0.0128 461 VAL A CB 3558 C CG1 . VAL A 465 ? 0.2695 0.2767 0.2886 0.0085 -0.0083 -0.0118 461 VAL A CG1 3559 C CG2 . VAL A 465 ? 0.2439 0.2584 0.2640 0.0103 -0.0090 -0.0149 461 VAL A CG2 3560 N N . VAL A 466 ? 0.2904 0.2911 0.3078 0.0097 -0.0082 -0.0116 462 VAL A N 3561 C CA . VAL A 466 ? 0.2838 0.2801 0.3006 0.0093 -0.0075 -0.0106 462 VAL A CA 3562 C C . VAL A 466 ? 0.2921 0.2879 0.3102 0.0070 -0.0073 -0.0101 462 VAL A C 3563 O O . VAL A 466 ? 0.2903 0.2880 0.3097 0.0056 -0.0077 -0.0110 462 VAL A O 3564 C CB . VAL A 466 ? 0.3012 0.2956 0.3181 0.0090 -0.0076 -0.0115 462 VAL A CB 3565 C CG1 . VAL A 466 ? 0.2850 0.2750 0.3019 0.0080 -0.0067 -0.0110 462 VAL A CG1 3566 C CG2 . VAL A 466 ? 0.2957 0.2907 0.3111 0.0115 -0.0078 -0.0118 462 VAL A CG2 3567 N N . PHE A 467 ? 0.2987 0.2921 0.3165 0.0070 -0.0064 -0.0088 463 PHE A N 3568 C CA . PHE A 467 ? 0.2996 0.2926 0.3189 0.0048 -0.0061 -0.0085 463 PHE A CA 3569 C C . PHE A 467 ? 0.3072 0.2969 0.3273 0.0036 -0.0054 -0.0090 463 PHE A C 3570 O O . PHE A 467 ? 0.3060 0.2922 0.3251 0.0045 -0.0043 -0.0084 463 PHE A O 3571 C CB . PHE A 467 ? 0.3053 0.2982 0.3241 0.0053 -0.0054 -0.0069 463 PHE A CB 3572 C CG . PHE A 467 ? 0.2860 0.2784 0.3063 0.0032 -0.0049 -0.0066 463 PHE A CG 3573 C CD1 . PHE A 467 ? 0.3119 0.3071 0.3335 0.0018 -0.0057 -0.0074 463 PHE A CD1 3574 C CD2 . PHE A 467 ? 0.3422 0.3316 0.3627 0.0029 -0.0034 -0.0055 463 PHE A CD2 3575 C CE1 . PHE A 467 ? 0.3430 0.3385 0.3660 0.0002 -0.0053 -0.0072 463 PHE A CE1 3576 C CE2 . PHE A 467 ? 0.3598 0.3494 0.3822 0.0008 -0.0029 -0.0054 463 PHE A CE2 3577 C CZ . PHE A 467 ? 0.3140 0.3068 0.3376 -0.0004 -0.0040 -0.0063 463 PHE A CZ 3578 N N . ALA A 468 ? 0.2943 0.2852 0.3161 0.0016 -0.0059 -0.0101 464 ALA A N 3579 C CA . ALA A 468 ? 0.3084 0.2973 0.3318 -0.0001 -0.0052 -0.0110 464 ALA A CA 3580 C C . ALA A 468 ? 0.3243 0.3158 0.3494 -0.0018 -0.0056 -0.0115 464 ALA A C 3581 O O . ALA A 468 ? 0.3178 0.3126 0.3430 -0.0018 -0.0067 -0.0123 464 ALA A O 3582 C CB . ALA A 468 ? 0.3034 0.2916 0.3268 -0.0001 -0.0058 -0.0129 464 ALA A CB 3583 N N . GLU A 469 ? 0.3235 0.3139 0.3500 -0.0031 -0.0045 -0.0111 465 GLU A N 3584 C CA . GLU A 469 ? 0.3213 0.3150 0.3495 -0.0044 -0.0049 -0.0115 465 GLU A CA 3585 C C . GLU A 469 ? 0.3252 0.3218 0.3548 -0.0054 -0.0060 -0.0138 465 GLU A C 3586 O O . GLU A 469 ? 0.3176 0.3178 0.3471 -0.0051 -0.0070 -0.0141 465 GLU A O 3587 C CB . GLU A 469 ? 0.3377 0.3298 0.3673 -0.0058 -0.0033 -0.0107 465 GLU A CB 3588 C CG . GLU A 469 ? 0.3449 0.3410 0.3761 -0.0068 -0.0038 -0.0110 465 GLU A CG 3589 C CD . GLU A 469 ? 0.4423 0.4374 0.4750 -0.0080 -0.0022 -0.0100 465 GLU A CD 3590 O OE1 . GLU A 469 ? 0.4873 0.4785 0.5189 -0.0074 -0.0007 -0.0083 465 GLU A OE1 3591 O OE2 . GLU A 469 ? 0.5030 0.5014 0.5378 -0.0094 -0.0024 -0.0110 465 GLU A OE2 3592 N N . ASN A 470 ? 0.3173 0.3123 0.3481 -0.0064 -0.0058 -0.0157 466 ASN A N 3593 C CA . ASN A 470 ? 0.3199 0.3180 0.3521 -0.0072 -0.0069 -0.0183 466 ASN A CA 3594 C C . ASN A 470 ? 0.3351 0.3308 0.3668 -0.0068 -0.0070 -0.0198 466 ASN A C 3595 O O . ASN A 470 ? 0.3254 0.3198 0.3590 -0.0084 -0.0064 -0.0219 466 ASN A O 3596 C CB A ASN A 470 ? 0.3425 0.3419 0.3780 -0.0095 -0.0062 -0.0200 466 ASN A CB 3597 C CB B ASN A 470 ? 0.3329 0.3331 0.3684 -0.0094 -0.0065 -0.0201 466 ASN A CB 3598 C CG A ASN A 470 ? 0.3337 0.3381 0.3707 -0.0100 -0.0076 -0.0228 466 ASN A CG 3599 C CG B ASN A 470 ? 0.3183 0.3218 0.3543 -0.0095 -0.0066 -0.0189 466 ASN A CG 3600 O OD1 A ASN A 470 ? 0.4076 0.4138 0.4477 -0.0119 -0.0073 -0.0252 466 ASN A OD1 3601 O OD1 B ASN A 470 ? 0.2741 0.2811 0.3088 -0.0082 -0.0078 -0.0186 466 ASN A OD1 3602 N ND2 A ASN A 470 ? 0.3573 0.3643 0.3923 -0.0080 -0.0091 -0.0227 466 ASN A ND2 3603 N ND2 B ASN A 470 ? 0.3168 0.3189 0.3544 -0.0109 -0.0051 -0.0182 466 ASN A ND2 3604 N N . PRO A 471 ? 0.3338 0.3291 0.3632 -0.0049 -0.0077 -0.0190 467 PRO A N 3605 C CA . PRO A 471 ? 0.3312 0.3243 0.3598 -0.0043 -0.0078 -0.0203 467 PRO A CA 3606 C C . PRO A 471 ? 0.3471 0.3432 0.3767 -0.0048 -0.0090 -0.0231 467 PRO A C 3607 O O . PRO A 471 ? 0.3495 0.3500 0.3793 -0.0044 -0.0100 -0.0236 467 PRO A O 3608 C CB . PRO A 471 ? 0.3380 0.3313 0.3640 -0.0022 -0.0084 -0.0188 467 PRO A CB 3609 C CG . PRO A 471 ? 0.3183 0.3153 0.3441 -0.0018 -0.0090 -0.0178 467 PRO A CG 3610 C CD . PRO A 471 ? 0.3119 0.3087 0.3393 -0.0033 -0.0082 -0.0171 467 PRO A CD 3611 N N . ASP A 472 ? 0.3576 0.3517 0.3878 -0.0052 -0.0088 -0.0251 468 ASP A N 3612 C CA . ASP A 472 ? 0.3669 0.3641 0.3976 -0.0051 -0.0101 -0.0280 468 ASP A CA 3613 C C . ASP A 472 ? 0.3578 0.3558 0.3859 -0.0027 -0.0111 -0.0275 468 ASP A C 3614 O O . ASP A 472 ? 0.3535 0.3494 0.3798 -0.0015 -0.0107 -0.0252 468 ASP A O 3615 C CB . ASP A 472 ? 0.3833 0.3786 0.4162 -0.0070 -0.0095 -0.0309 468 ASP A CB 3616 C CG . ASP A 472 ? 0.4234 0.4130 0.4550 -0.0064 -0.0083 -0.0305 468 ASP A CG 3617 O OD1 . ASP A 472 ? 0.4522 0.4387 0.4855 -0.0082 -0.0071 -0.0324 468 ASP A OD1 3618 O OD2 . ASP A 472 ? 0.4228 0.4109 0.4516 -0.0043 -0.0085 -0.0284 468 ASP A OD2 3619 N N . ALA A 473 ? 0.3339 0.3353 0.3619 -0.0020 -0.0123 -0.0296 469 ALA A N 3620 C CA . ALA A 473 ? 0.3359 0.3385 0.3613 0.0004 -0.0130 -0.0290 469 ALA A CA 3621 C C . ALA A 473 ? 0.3314 0.3300 0.3555 0.0011 -0.0125 -0.0285 469 ALA A C 3622 O O . ALA A 473 ? 0.3281 0.3264 0.3503 0.0027 -0.0124 -0.0268 469 ALA A O 3623 C CB . ALA A 473 ? 0.3576 0.3647 0.3829 0.0014 -0.0143 -0.0317 469 ALA A CB 3624 N N . GLU A 474 ? 0.3202 0.3154 0.3454 -0.0001 -0.0119 -0.0300 470 GLU A N 3625 C CA . GLU A 474 ? 0.3261 0.3173 0.3497 0.0010 -0.0113 -0.0296 470 GLU A CA 3626 C C . GLU A 474 ? 0.3239 0.3124 0.3463 0.0018 -0.0103 -0.0266 470 GLU A C 3627 O O . GLU A 474 ? 0.3416 0.3295 0.3620 0.0036 -0.0104 -0.0255 470 GLU A O 3628 C CB . GLU A 474 ? 0.3253 0.3128 0.3503 -0.0005 -0.0105 -0.0319 470 GLU A CB 3629 C CG . GLU A 474 ? 0.3963 0.3791 0.4192 0.0009 -0.0096 -0.0312 470 GLU A CG 3630 C CD . GLU A 474 ? 0.4718 0.4497 0.4958 -0.0005 -0.0081 -0.0331 470 GLU A CD 3631 O OE1 . GLU A 474 ? 0.4724 0.4455 0.4945 0.0008 -0.0068 -0.0319 470 GLU A OE1 3632 O OE2 . GLU A 474 ? 0.4549 0.4339 0.4815 -0.0027 -0.0081 -0.0360 470 GLU A OE2 3633 N N . PHE A 475 ? 0.3360 0.3233 0.3594 0.0005 -0.0094 -0.0254 471 PHE A N 3634 C CA . PHE A 475 ? 0.3420 0.3276 0.3641 0.0015 -0.0087 -0.0227 471 PHE A CA 3635 C C . PHE A 475 ? 0.3322 0.3214 0.3532 0.0030 -0.0096 -0.0215 471 PHE A C 3636 O O . PHE A 475 ? 0.3283 0.3169 0.3478 0.0045 -0.0094 -0.0203 471 PHE A O 3637 C CB . PHE A 475 ? 0.3459 0.3309 0.3694 0.0000 -0.0078 -0.0216 471 PHE A CB 3638 C CG . PHE A 475 ? 0.3577 0.3418 0.3799 0.0012 -0.0071 -0.0189 471 PHE A CG 3639 C CD1 . PHE A 475 ? 0.3842 0.3717 0.4060 0.0018 -0.0079 -0.0178 471 PHE A CD1 3640 C CD2 . PHE A 475 ? 0.4198 0.3994 0.4410 0.0018 -0.0055 -0.0177 471 PHE A CD2 3641 C CE1 . PHE A 475 ? 0.3989 0.3862 0.4196 0.0029 -0.0074 -0.0157 471 PHE A CE1 3642 C CE2 . PHE A 475 ? 0.4745 0.4538 0.4942 0.0034 -0.0050 -0.0153 471 PHE A CE2 3643 C CZ . PHE A 475 ? 0.4197 0.4034 0.4394 0.0038 -0.0062 -0.0146 471 PHE A CZ 3644 N N . VAL A 476 ? 0.3070 0.2998 0.3286 0.0026 -0.0104 -0.0219 472 VAL A N 3645 C CA . VAL A 476 ? 0.3101 0.3056 0.3306 0.0037 -0.0107 -0.0208 472 VAL A CA 3646 C C . VAL A 476 ? 0.3069 0.3029 0.3262 0.0053 -0.0110 -0.0215 472 VAL A C 3647 O O . VAL A 476 ? 0.3311 0.3274 0.3496 0.0064 -0.0107 -0.0205 472 VAL A O 3648 C CB . VAL A 476 ? 0.2893 0.2882 0.3104 0.0033 -0.0110 -0.0210 472 VAL A CB 3649 C CG1 . VAL A 476 ? 0.3159 0.3167 0.3359 0.0044 -0.0107 -0.0198 472 VAL A CG1 3650 C CG2 . VAL A 476 ? 0.2815 0.2803 0.3041 0.0017 -0.0107 -0.0204 472 VAL A CG2 3651 N N . LYS A 477 ? 0.3138 0.3098 0.3330 0.0055 -0.0115 -0.0233 473 LYS A N 3652 C CA . LYS A 477 ? 0.3277 0.3242 0.3455 0.0072 -0.0118 -0.0239 473 LYS A CA 3653 C C . LYS A 477 ? 0.3269 0.3208 0.3439 0.0081 -0.0113 -0.0234 473 LYS A C 3654 O O . LYS A 477 ? 0.3152 0.3101 0.3312 0.0096 -0.0113 -0.0232 473 LYS A O 3655 C CB . LYS A 477 ? 0.3254 0.3227 0.3432 0.0073 -0.0125 -0.0262 473 LYS A CB 3656 C CG . LYS A 477 ? 0.3899 0.3909 0.4077 0.0075 -0.0131 -0.0267 473 LYS A CG 3657 C CD . LYS A 477 ? 0.5123 0.5148 0.5301 0.0080 -0.0140 -0.0294 473 LYS A CD 3658 C CE . LYS A 477 ? 0.6294 0.6354 0.6483 0.0073 -0.0147 -0.0306 473 LYS A CE 3659 N NZ . LYS A 477 ? 0.7130 0.7217 0.7311 0.0081 -0.0143 -0.0287 473 LYS A NZ 3660 N N . SER A 478 ? 0.3237 0.3143 0.3409 0.0075 -0.0108 -0.0232 474 SER A N 3661 C CA . SER A 478 ? 0.3397 0.3274 0.3557 0.0088 -0.0102 -0.0226 474 SER A CA 3662 C C . SER A 478 ? 0.3441 0.3324 0.3596 0.0097 -0.0098 -0.0207 474 SER A C 3663 O O . SER A 478 ? 0.3304 0.3173 0.3446 0.0115 -0.0094 -0.0201 474 SER A O 3664 C CB . SER A 478 ? 0.3320 0.3150 0.3482 0.0079 -0.0094 -0.0233 474 SER A CB 3665 O OG . SER A 478 ? 0.3665 0.3492 0.3830 0.0075 -0.0098 -0.0257 474 SER A OG 3666 N N . GLY A 479 ? 0.3353 0.3259 0.3518 0.0088 -0.0099 -0.0198 475 GLY A N 3667 C CA . GLY A 479 ? 0.3426 0.3336 0.3588 0.0095 -0.0094 -0.0183 475 GLY A CA 3668 C C . GLY A 479 ? 0.3475 0.3418 0.3634 0.0108 -0.0096 -0.0181 475 GLY A C 3669 O O . GLY A 479 ? 0.3569 0.3522 0.3726 0.0117 -0.0094 -0.0172 475 GLY A O 3670 N N . GLY A 480 ? 0.3390 0.3354 0.3551 0.0110 -0.0099 -0.0191 476 GLY A N 3671 C CA . GLY A 480 ? 0.3444 0.3443 0.3609 0.0119 -0.0098 -0.0192 476 GLY A CA 3672 C C . GLY A 480 ? 0.3349 0.3373 0.3527 0.0108 -0.0095 -0.0187 476 GLY A C 3673 O O . GLY A 480 ? 0.3372 0.3423 0.3555 0.0115 -0.0093 -0.0189 476 GLY A O 3674 N N . PHE A 481 ? 0.3268 0.3287 0.3451 0.0093 -0.0094 -0.0184 477 PHE A N 3675 C CA . PHE A 481 ? 0.3151 0.3190 0.3345 0.0082 -0.0089 -0.0179 477 PHE A CA 3676 C C . PHE A 481 ? 0.3238 0.3299 0.3438 0.0079 -0.0080 -0.0185 477 PHE A C 3677 O O . PHE A 481 ? 0.3235 0.3292 0.3430 0.0082 -0.0078 -0.0188 477 PHE A O 3678 C CB . PHE A 481 ? 0.3166 0.3190 0.3361 0.0070 -0.0090 -0.0172 477 PHE A CB 3679 C CG . PHE A 481 ? 0.3012 0.3012 0.3203 0.0069 -0.0093 -0.0167 477 PHE A CG 3680 C CD1 . PHE A 481 ? 0.3100 0.3101 0.3289 0.0076 -0.0092 -0.0159 477 PHE A CD1 3681 C CD2 . PHE A 481 ? 0.2608 0.2585 0.2797 0.0064 -0.0096 -0.0170 477 PHE A CD2 3682 C CE1 . PHE A 481 ? 0.2813 0.2786 0.2996 0.0079 -0.0090 -0.0150 477 PHE A CE1 3683 C CE2 . PHE A 481 ? 0.3206 0.3155 0.3395 0.0061 -0.0093 -0.0165 477 PHE A CE2 3684 C CZ . PHE A 481 ? 0.2870 0.2814 0.3053 0.0070 -0.0089 -0.0152 477 PHE A CZ 3685 N N . SER A 482 ? 0.3117 0.3200 0.3330 0.0074 -0.0073 -0.0187 478 SER A N 3686 C CA . SER A 482 ? 0.3120 0.3217 0.3341 0.0067 -0.0058 -0.0192 478 SER A CA 3687 C C . SER A 482 ? 0.3173 0.3257 0.3389 0.0058 -0.0050 -0.0183 478 SER A C 3688 O O . SER A 482 ? 0.3072 0.3154 0.3285 0.0058 -0.0036 -0.0183 478 SER A O 3689 C CB . SER A 482 ? 0.3155 0.3282 0.3395 0.0061 -0.0051 -0.0201 478 SER A CB 3690 O OG . SER A 482 ? 0.3134 0.3282 0.3378 0.0073 -0.0057 -0.0212 478 SER A OG 3691 N N . TYR A 483 ? 0.2930 0.3005 0.3144 0.0052 -0.0056 -0.0175 479 TYR A N 3692 C CA . TYR A 483 ? 0.2850 0.2916 0.3058 0.0047 -0.0051 -0.0166 479 TYR A CA 3693 C C . TYR A 483 ? 0.2874 0.2933 0.3082 0.0042 -0.0062 -0.0159 479 TYR A C 3694 O O . TYR A 483 ? 0.2885 0.2942 0.3096 0.0044 -0.0070 -0.0159 479 TYR A O 3695 C CB . TYR A 483 ? 0.2875 0.2947 0.3090 0.0039 -0.0032 -0.0166 479 TYR A CB 3696 C CG . TYR A 483 ? 0.3151 0.3238 0.3381 0.0032 -0.0032 -0.0172 479 TYR A CG 3697 C CD1 . TYR A 483 ? 0.2970 0.3056 0.3201 0.0027 -0.0038 -0.0165 479 TYR A CD1 3698 C CD2 . TYR A 483 ? 0.3195 0.3304 0.3441 0.0029 -0.0024 -0.0187 479 TYR A CD2 3699 C CE1 . TYR A 483 ? 0.2790 0.2894 0.3032 0.0023 -0.0039 -0.0172 479 TYR A CE1 3700 C CE2 . TYR A 483 ? 0.3447 0.3578 0.3708 0.0024 -0.0025 -0.0197 479 TYR A CE2 3701 C CZ . TYR A 483 ? 0.3618 0.3747 0.3876 0.0021 -0.0032 -0.0190 479 TYR A CZ 3702 O OH . TYR A 483 ? 0.3762 0.3918 0.4033 0.0019 -0.0034 -0.0202 479 TYR A OH 3703 N N . ALA A 484 ? 0.2788 0.2842 0.2991 0.0039 -0.0061 -0.0152 480 ALA A N 3704 C CA . ALA A 484 ? 0.2761 0.2810 0.2967 0.0033 -0.0068 -0.0145 480 ALA A CA 3705 C C . ALA A 484 ? 0.2873 0.2926 0.3078 0.0028 -0.0060 -0.0137 480 ALA A C 3706 O O . ALA A 484 ? 0.2859 0.2914 0.3057 0.0031 -0.0049 -0.0135 480 ALA A O 3707 C CB . ALA A 484 ? 0.2652 0.2695 0.2855 0.0033 -0.0078 -0.0148 480 ALA A CB 3708 N N . ILE A 485 ? 0.2806 0.2858 0.3016 0.0022 -0.0063 -0.0131 481 ILE A N 3709 C CA . ILE A 485 ? 0.2824 0.2879 0.3032 0.0018 -0.0057 -0.0122 481 ILE A CA 3710 C C . ILE A 485 ? 0.2748 0.2801 0.2958 0.0015 -0.0066 -0.0118 481 ILE A C 3711 O O . ILE A 485 ? 0.2975 0.3021 0.3191 0.0012 -0.0072 -0.0117 481 ILE A O 3712 C CB . ILE A 485 ? 0.2772 0.2831 0.2985 0.0014 -0.0053 -0.0121 481 ILE A CB 3713 C CG1 . ILE A 485 ? 0.2858 0.2925 0.3076 0.0014 -0.0041 -0.0132 481 ILE A CG1 3714 C CG2 . ILE A 485 ? 0.2872 0.2931 0.3082 0.0011 -0.0048 -0.0111 481 ILE A CG2 3715 C CD1 . ILE A 485 ? 0.2929 0.3010 0.3156 0.0012 -0.0042 -0.0139 481 ILE A CD1 3716 N N . VAL A 486 ? 0.2643 0.2703 0.2848 0.0016 -0.0065 -0.0116 482 VAL A N 3717 C CA . VAL A 486 ? 0.2554 0.2621 0.2768 0.0011 -0.0073 -0.0116 482 VAL A CA 3718 C C . VAL A 486 ? 0.2700 0.2778 0.2911 0.0011 -0.0068 -0.0107 482 VAL A C 3719 O O . VAL A 486 ? 0.2734 0.2820 0.2932 0.0021 -0.0061 -0.0104 482 VAL A O 3720 C CB . VAL A 486 ? 0.2531 0.2607 0.2746 0.0014 -0.0081 -0.0129 482 VAL A CB 3721 C CG1 A VAL A 486 ? 0.2728 0.2812 0.2926 0.0029 -0.0076 -0.0131 482 VAL A CG1 3722 C CG1 B VAL A 486 ? 0.2366 0.2429 0.2578 0.0018 -0.0083 -0.0137 482 VAL A CG1 3723 C CG2 A VAL A 486 ? 0.2067 0.2156 0.2296 0.0006 -0.0088 -0.0136 482 VAL A CG2 3724 C CG2 B VAL A 486 ? 0.2821 0.2915 0.3022 0.0027 -0.0077 -0.0129 482 VAL A CG2 3725 N N . ALA A 487 ? 0.2642 0.2720 0.2864 0.0002 -0.0071 -0.0102 483 ALA A N 3726 C CA . ALA A 487 ? 0.2645 0.2735 0.2865 0.0002 -0.0066 -0.0092 483 ALA A CA 3727 C C . ALA A 487 ? 0.2541 0.2646 0.2774 -0.0005 -0.0072 -0.0096 483 ALA A C 3728 O O . ALA A 487 ? 0.2719 0.2816 0.2968 -0.0016 -0.0074 -0.0099 483 ALA A O 3729 C CB . ALA A 487 ? 0.2543 0.2620 0.2761 0.0000 -0.0061 -0.0082 483 ALA A CB 3730 N N . VAL A 488 ? 0.2573 0.2703 0.2801 0.0003 -0.0071 -0.0096 484 VAL A N 3731 C CA . VAL A 488 ? 0.2684 0.2844 0.2930 -0.0003 -0.0078 -0.0105 484 VAL A CA 3732 C C . VAL A 488 ? 0.2696 0.2878 0.2931 0.0007 -0.0073 -0.0095 484 VAL A C 3733 O O . VAL A 488 ? 0.2672 0.2841 0.2886 0.0019 -0.0064 -0.0082 484 VAL A O 3734 C CB . VAL A 488 ? 0.2870 0.3052 0.3118 0.0002 -0.0087 -0.0124 484 VAL A CB 3735 C CG1 . VAL A 488 ? 0.2779 0.2937 0.3037 -0.0008 -0.0090 -0.0135 484 VAL A CG1 3736 C CG2 . VAL A 488 ? 0.2683 0.2877 0.2904 0.0027 -0.0083 -0.0121 484 VAL A CG2 3737 N N . GLY A 489 ? 0.2572 0.2786 0.2824 0.0003 -0.0077 -0.0102 485 GLY A N 3738 C CA . GLY A 489 ? 0.2556 0.2796 0.2795 0.0018 -0.0073 -0.0093 485 GLY A CA 3739 C C . GLY A 489 ? 0.2594 0.2862 0.2857 0.0006 -0.0075 -0.0096 485 GLY A C 3740 O O . GLY A 489 ? 0.2643 0.2923 0.2936 -0.0012 -0.0080 -0.0111 485 GLY A O 3741 N N . GLU A 490 ? 0.2571 0.2850 0.2823 0.0017 -0.0069 -0.0082 486 GLU A N 3742 C CA . GLU A 490 ? 0.2633 0.2945 0.2906 0.0009 -0.0069 -0.0083 486 GLU A CA 3743 C C . GLU A 490 ? 0.2566 0.2851 0.2858 -0.0013 -0.0063 -0.0075 486 GLU A C 3744 O O . GLU A 490 ? 0.2434 0.2677 0.2713 -0.0014 -0.0057 -0.0061 486 GLU A O 3745 C CB . GLU A 490 ? 0.2603 0.2934 0.2853 0.0031 -0.0064 -0.0069 486 GLU A CB 3746 C CG . GLU A 490 ? 0.2604 0.2966 0.2831 0.0059 -0.0067 -0.0075 486 GLU A CG 3747 C CD . GLU A 490 ? 0.2978 0.3367 0.3185 0.0082 -0.0060 -0.0063 486 GLU A CD 3748 O OE1 . GLU A 490 ? 0.2796 0.3151 0.2981 0.0090 -0.0048 -0.0042 486 GLU A OE1 3749 O OE2 . GLU A 490 ? 0.2603 0.3049 0.2819 0.0093 -0.0068 -0.0076 486 GLU A OE2 3750 N N . HIS A 491 ? 0.2515 0.2827 0.2836 -0.0027 -0.0062 -0.0083 487 HIS A N 3751 C CA . HIS A 491 ? 0.2639 0.2929 0.2976 -0.0043 -0.0052 -0.0071 487 HIS A CA 3752 C C . HIS A 491 ? 0.2501 0.2799 0.2822 -0.0031 -0.0046 -0.0052 487 HIS A C 3753 O O . HIS A 491 ? 0.2633 0.2961 0.2938 -0.0013 -0.0050 -0.0052 487 HIS A O 3754 C CB . HIS A 491 ? 0.2699 0.3013 0.3078 -0.0067 -0.0049 -0.0090 487 HIS A CB 3755 C CG . HIS A 491 ? 0.3248 0.3545 0.3644 -0.0082 -0.0051 -0.0109 487 HIS A CG 3756 N ND1 . HIS A 491 ? 0.3708 0.4023 0.4143 -0.0105 -0.0047 -0.0132 487 HIS A ND1 3757 C CD2 . HIS A 491 ? 0.3354 0.3618 0.3731 -0.0076 -0.0056 -0.0110 487 HIS A CD2 3758 C CE1 . HIS A 491 ? 0.3724 0.4014 0.4163 -0.0113 -0.0050 -0.0146 487 HIS A CE1 3759 N NE2 . HIS A 491 ? 0.3565 0.3826 0.3968 -0.0095 -0.0056 -0.0132 487 HIS A NE2 3760 N N . PRO A 492 ? 0.2414 0.2685 0.2736 -0.0037 -0.0036 -0.0035 488 PRO A N 3761 C CA . PRO A 492 ? 0.2391 0.2668 0.2694 -0.0023 -0.0030 -0.0017 488 PRO A CA 3762 C C . PRO A 492 ? 0.2604 0.2932 0.2927 -0.0024 -0.0030 -0.0023 488 PRO A C 3763 O O . PRO A 492 ? 0.2400 0.2750 0.2759 -0.0044 -0.0028 -0.0037 488 PRO A O 3764 C CB . PRO A 492 ? 0.2461 0.2703 0.2765 -0.0030 -0.0020 -0.0001 488 PRO A CB 3765 C CG . PRO A 492 ? 0.2455 0.2658 0.2756 -0.0037 -0.0022 -0.0006 488 PRO A CG 3766 C CD . PRO A 492 ? 0.2498 0.2724 0.2824 -0.0049 -0.0029 -0.0029 488 PRO A CD 3767 N N . TYR A 493 ? 0.2411 0.2759 0.2713 -0.0004 -0.0029 -0.0012 489 TYR A N 3768 C CA . TYR A 493 ? 0.2738 0.3140 0.3057 -0.0002 -0.0028 -0.0016 489 TYR A CA 3769 C C . TYR A 493 ? 0.2845 0.3246 0.3132 0.0022 -0.0023 0.0004 489 TYR A C 3770 O O . TYR A 493 ? 0.2737 0.3100 0.2989 0.0036 -0.0020 0.0016 489 TYR A O 3771 C CB . TYR A 493 ? 0.2653 0.3109 0.2982 0.0006 -0.0040 -0.0040 489 TYR A CB 3772 C CG . TYR A 493 ? 0.2784 0.3227 0.3072 0.0033 -0.0044 -0.0036 489 TYR A CG 3773 C CD1 . TYR A 493 ? 0.2880 0.3329 0.3133 0.0062 -0.0039 -0.0020 489 TYR A CD1 3774 C CD2 . TYR A 493 ? 0.2521 0.2941 0.2804 0.0030 -0.0050 -0.0046 489 TYR A CD2 3775 C CE1 . TYR A 493 ? 0.2713 0.3144 0.2927 0.0087 -0.0038 -0.0015 489 TYR A CE1 3776 C CE2 . TYR A 493 ? 0.2711 0.3116 0.2958 0.0054 -0.0050 -0.0041 489 TYR A CE2 3777 C CZ . TYR A 493 ? 0.2664 0.3072 0.2876 0.0081 -0.0042 -0.0025 489 TYR A CZ 3778 O OH . TYR A 493 ? 0.2800 0.3186 0.2974 0.0106 -0.0037 -0.0019 489 TYR A OH 3779 N N . THR A 494 ? 0.3097 0.3540 0.3397 0.0025 -0.0019 0.0006 490 THR A N 3780 C CA . THR A 494 ? 0.3549 0.4005 0.3817 0.0053 -0.0016 0.0020 490 THR A CA 3781 C C . THR A 494 ? 0.3594 0.4121 0.3881 0.0060 -0.0019 0.0009 490 THR A C 3782 O O . THR A 494 ? 0.3672 0.4238 0.4002 0.0039 -0.0022 -0.0009 490 THR A O 3783 C CB . THR A 494 ? 0.3912 0.4351 0.4168 0.0057 -0.0005 0.0041 490 THR A CB 3784 O OG1 . THR A 494 ? 0.4555 0.4971 0.4834 0.0034 0.0001 0.0046 490 THR A OG1 3785 C CG2 . THR A 494 ? 0.3792 0.4197 0.4003 0.0081 0.0001 0.0056 490 THR A CG2 3786 N N . GLU A 495 ? 0.3719 0.4261 0.3974 0.0090 -0.0016 0.0021 491 GLU A N 3787 C CA . GLU A 495 ? 0.3880 0.4491 0.4142 0.0107 -0.0017 0.0017 491 GLU A CA 3788 C C . GLU A 495 ? 0.3852 0.4527 0.4148 0.0100 -0.0030 -0.0013 491 GLU A C 3789 O O . GLU A 495 ? 0.3684 0.4350 0.3971 0.0103 -0.0037 -0.0024 491 GLU A O 3790 C CB . GLU A 495 ? 0.4010 0.4630 0.4293 0.0094 -0.0008 0.0027 491 GLU A CB 3791 C CG . GLU A 495 ? 0.4627 0.5190 0.4876 0.0103 0.0003 0.0053 491 GLU A CG 3792 C CD . GLU A 495 ? 0.5550 0.6094 0.5824 0.0079 0.0011 0.0062 491 GLU A CD 3793 O OE1 . GLU A 495 ? 0.6068 0.6563 0.6315 0.0085 0.0018 0.0080 491 GLU A OE1 3794 O OE2 . GLU A 495 ? 0.5681 0.6260 0.6000 0.0056 0.0012 0.0049 491 GLU A OE2 3795 N N . THR A 496 ? 0.3677 0.4419 0.4013 0.0090 -0.0031 -0.0028 492 THR A N 3796 C CA . THR A 496 ? 0.3713 0.4533 0.4081 0.0089 -0.0044 -0.0062 492 THR A CA 3797 C C . THR A 496 ? 0.3737 0.4543 0.4137 0.0057 -0.0050 -0.0085 492 THR A C 3798 O O . THR A 496 ? 0.3561 0.4408 0.3967 0.0066 -0.0064 -0.0111 492 THR A O 3799 C CB . THR A 496 ? 0.3836 0.4735 0.4245 0.0082 -0.0042 -0.0075 492 THR A CB 3800 O OG1 . THR A 496 ? 0.3854 0.4757 0.4227 0.0113 -0.0035 -0.0050 492 THR A OG1 3801 C CG2 . THR A 496 ? 0.3885 0.4882 0.4323 0.0090 -0.0058 -0.0114 492 THR A CG2 3802 N N . LYS A 497 ? 0.3684 0.4429 0.4102 0.0025 -0.0041 -0.0077 493 LYS A N 3803 C CA . LYS A 497 ? 0.3711 0.4433 0.4155 -0.0003 -0.0044 -0.0097 493 LYS A CA 3804 C C . LYS A 497 ? 0.3584 0.4277 0.3990 0.0017 -0.0054 -0.0096 493 LYS A C 3805 O O . LYS A 497 ? 0.3702 0.4402 0.4125 0.0006 -0.0063 -0.0119 493 LYS A O 3806 C CB . LYS A 497 ? 0.3869 0.4525 0.4331 -0.0034 -0.0029 -0.0084 493 LYS A CB 3807 C CG . LYS A 497 ? 0.4559 0.5250 0.5072 -0.0062 -0.0016 -0.0094 493 LYS A CG 3808 C CD . LYS A 497 ? 0.5475 0.6100 0.6002 -0.0088 0.0004 -0.0077 493 LYS A CD 3809 C CE . LYS A 497 ? 0.5915 0.6576 0.6486 -0.0109 0.0021 -0.0082 493 LYS A CE 3810 N NZ . LYS A 497 ? 0.6550 0.7145 0.7126 -0.0127 0.0045 -0.0059 493 LYS A NZ 3811 N N . GLY A 498 ? 0.3281 0.3940 0.3634 0.0048 -0.0052 -0.0070 494 GLY A N 3812 C CA . GLY A 498 ? 0.3332 0.3959 0.3649 0.0066 -0.0057 -0.0067 494 GLY A CA 3813 C C . GLY A 498 ? 0.3297 0.3980 0.3593 0.0102 -0.0066 -0.0078 494 GLY A C 3814 O O . GLY A 498 ? 0.3246 0.3909 0.3513 0.0119 -0.0069 -0.0078 494 GLY A O 3815 N N . ASP A 499 ? 0.3103 0.3856 0.3408 0.0116 -0.0069 -0.0086 495 ASP A N 3816 C CA . ASP A 499 ? 0.3173 0.3990 0.3456 0.0156 -0.0078 -0.0098 495 ASP A CA 3817 C C . ASP A 499 ? 0.3262 0.4107 0.3572 0.0142 -0.0092 -0.0131 495 ASP A C 3818 O O . ASP A 499 ? 0.3267 0.4132 0.3631 0.0104 -0.0097 -0.0156 495 ASP A O 3819 C CB . ASP A 499 ? 0.3082 0.3987 0.3384 0.0170 -0.0082 -0.0109 495 ASP A CB 3820 C CG . ASP A 499 ? 0.3182 0.4067 0.3450 0.0192 -0.0068 -0.0077 495 ASP A CG 3821 O OD1 . ASP A 499 ? 0.3144 0.3948 0.3372 0.0199 -0.0055 -0.0047 495 ASP A OD1 3822 O OD2 . ASP A 499 ? 0.3292 0.4247 0.3575 0.0204 -0.0070 -0.0084 495 ASP A OD2 3823 N N . ASN A 500 ? 0.3220 0.4065 0.3493 0.0174 -0.0097 -0.0132 496 ASN A N 3824 C CA . ASN A 500 ? 0.3401 0.4260 0.3694 0.0161 -0.0110 -0.0161 496 ASN A CA 3825 C C . ASN A 500 ? 0.3379 0.4281 0.3632 0.0210 -0.0117 -0.0167 496 ASN A C 3826 O O . ASN A 500 ? 0.3325 0.4178 0.3523 0.0242 -0.0106 -0.0139 496 ASN A O 3827 C CB . ASN A 500 ? 0.3229 0.3993 0.3516 0.0136 -0.0102 -0.0145 496 ASN A CB 3828 C CG . ASN A 500 ? 0.3525 0.4289 0.3830 0.0121 -0.0113 -0.0171 496 ASN A CG 3829 O OD1 . ASN A 500 ? 0.3288 0.4107 0.3589 0.0142 -0.0125 -0.0194 496 ASN A OD1 3830 N ND2 . ASN A 500 ? 0.3061 0.3759 0.3380 0.0087 -0.0108 -0.0166 496 ASN A ND2 3831 N N . LEU A 501 ? 0.3433 0.4427 0.3713 0.0217 -0.0134 -0.0204 497 LEU A N 3832 C CA . LEU A 501 ? 0.3468 0.4519 0.3710 0.0270 -0.0143 -0.0213 497 LEU A CA 3833 C C . LEU A 501 ? 0.3556 0.4579 0.3780 0.0276 -0.0148 -0.0222 497 LEU A C 3834 O O . LEU A 501 ? 0.3561 0.4610 0.3740 0.0326 -0.0149 -0.0219 497 LEU A O 3835 C CB . LEU A 501 ? 0.3458 0.4635 0.3734 0.0282 -0.0161 -0.0254 497 LEU A CB 3836 C CG . LEU A 501 ? 0.3845 0.5076 0.4136 0.0288 -0.0157 -0.0250 497 LEU A CG 3837 C CD1 . LEU A 501 ? 0.4130 0.5499 0.4467 0.0294 -0.0178 -0.0301 497 LEU A CD1 3838 C CD2 . LEU A 501 ? 0.3671 0.4873 0.3891 0.0341 -0.0142 -0.0207 497 LEU A CD2 3839 N N . ASN A 502 ? 0.3492 0.4465 0.3749 0.0231 -0.0149 -0.0231 498 ASN A N 3840 C CA . ASN A 502 ? 0.3693 0.4643 0.3936 0.0236 -0.0155 -0.0241 498 ASN A CA 3841 C C . ASN A 502 ? 0.3601 0.4444 0.3810 0.0230 -0.0139 -0.0207 498 ASN A C 3842 O O . ASN A 502 ? 0.3705 0.4527 0.3886 0.0249 -0.0139 -0.0206 498 ASN A O 3843 C CB . ASN A 502 ? 0.3961 0.4941 0.4264 0.0193 -0.0170 -0.0285 498 ASN A CB 3844 C CG . ASN A 502 ? 0.5050 0.5969 0.5395 0.0138 -0.0161 -0.0279 498 ASN A CG 3845 O OD1 . ASN A 502 ? 0.5890 0.6725 0.6224 0.0120 -0.0152 -0.0260 498 ASN A OD1 3846 N ND2 . ASN A 502 ? 0.6130 0.7092 0.6522 0.0111 -0.0162 -0.0296 498 ASN A ND2 3847 N N . LEU A 503 ? 0.3385 0.4164 0.3600 0.0204 -0.0125 -0.0181 499 LEU A N 3848 C CA . LEU A 503 ? 0.3372 0.4056 0.3557 0.0199 -0.0109 -0.0150 499 LEU A CA 3849 C C . LEU A 503 ? 0.3391 0.4040 0.3580 0.0185 -0.0113 -0.0160 499 LEU A C 3850 O O . LEU A 503 ? 0.3445 0.4048 0.3594 0.0205 -0.0103 -0.0142 499 LEU A O 3851 C CB . LEU A 503 ? 0.3220 0.3879 0.3343 0.0246 -0.0092 -0.0119 499 LEU A CB 3852 C CG . LEU A 503 ? 0.3201 0.3882 0.3311 0.0263 -0.0083 -0.0102 499 LEU A CG 3853 C CD1 . LEU A 503 ? 0.3223 0.3866 0.3270 0.0308 -0.0061 -0.0069 499 LEU A CD1 3854 C CD2 . LEU A 503 ? 0.3410 0.4055 0.3554 0.0220 -0.0079 -0.0093 499 LEU A CD2 3855 N N . THR A 504 ? 0.3265 0.3936 0.3501 0.0152 -0.0127 -0.0191 500 THR A N 3856 C CA . THR A 504 ? 0.3563 0.4198 0.3806 0.0135 -0.0131 -0.0202 500 THR A CA 3857 C C . THR A 504 ? 0.3511 0.4093 0.3788 0.0090 -0.0126 -0.0198 500 THR A C 3858 O O . THR A 504 ? 0.3481 0.4082 0.3794 0.0066 -0.0126 -0.0205 500 THR A O 3859 C CB . THR A 504 ? 0.3683 0.4384 0.3951 0.0136 -0.0150 -0.0243 500 THR A CB 3860 O OG1 . THR A 504 ? 0.4589 0.5323 0.4912 0.0100 -0.0156 -0.0269 500 THR A OG1 3861 C CG2 . THR A 504 ? 0.3053 0.3825 0.3290 0.0185 -0.0157 -0.0250 500 THR A CG2 3862 N N . ILE A 505 ? 0.3432 0.3949 0.3697 0.0081 -0.0120 -0.0184 501 ILE A N 3863 C CA . ILE A 505 ? 0.3543 0.4008 0.3830 0.0046 -0.0112 -0.0174 501 ILE A CA 3864 C C . ILE A 505 ? 0.3795 0.4274 0.4128 0.0014 -0.0120 -0.0204 501 ILE A C 3865 O O . ILE A 505 ? 0.3586 0.4096 0.3928 0.0017 -0.0131 -0.0231 501 ILE A O 3866 C CB . ILE A 505 ? 0.3542 0.3938 0.3805 0.0045 -0.0103 -0.0153 501 ILE A CB 3867 C CG1 . ILE A 505 ? 0.3395 0.3782 0.3654 0.0049 -0.0110 -0.0168 501 ILE A CG1 3868 C CG2 . ILE A 505 ? 0.3503 0.3880 0.3726 0.0071 -0.0091 -0.0125 501 ILE A CG2 3869 C CD1 . ILE A 505 ? 0.3631 0.3953 0.3875 0.0042 -0.0101 -0.0151 501 ILE A CD1 3870 N N . PRO A 506 ? 0.3939 0.4392 0.4301 -0.0016 -0.0111 -0.0199 502 PRO A N 3871 C CA . PRO A 506 ? 0.4114 0.4568 0.4518 -0.0048 -0.0112 -0.0225 502 PRO A CA 3872 C C . PRO A 506 ? 0.4261 0.4674 0.4660 -0.0053 -0.0114 -0.0233 502 PRO A C 3873 O O . PRO A 506 ? 0.4030 0.4395 0.4398 -0.0042 -0.0110 -0.0210 502 PRO A O 3874 C CB . PRO A 506 ? 0.4217 0.4633 0.4639 -0.0072 -0.0096 -0.0208 502 PRO A CB 3875 C CG . PRO A 506 ? 0.4301 0.4690 0.4686 -0.0052 -0.0091 -0.0172 502 PRO A CG 3876 C CD . PRO A 506 ? 0.4022 0.4439 0.4372 -0.0019 -0.0099 -0.0168 502 PRO A CD 3877 N N . GLU A 507 ? 0.4315 0.4747 0.4747 -0.0072 -0.0118 -0.0266 503 GLU A N 3878 C CA . GLU A 507 ? 0.4550 0.4939 0.4983 -0.0083 -0.0117 -0.0275 503 GLU A CA 3879 C C . GLU A 507 ? 0.4644 0.4975 0.5096 -0.0110 -0.0100 -0.0264 503 GLU A C 3880 O O . GLU A 507 ? 0.4907 0.5244 0.5384 -0.0128 -0.0089 -0.0263 503 GLU A O 3881 C CB . GLU A 507 ? 0.4633 0.5069 0.5087 -0.0086 -0.0130 -0.0317 503 GLU A CB 3882 C CG . GLU A 507 ? 0.4690 0.5171 0.5110 -0.0048 -0.0145 -0.0319 503 GLU A CG 3883 C CD . GLU A 507 ? 0.4854 0.5280 0.5228 -0.0026 -0.0142 -0.0286 503 GLU A CD 3884 O OE1 . GLU A 507 ? 0.3669 0.4058 0.4042 -0.0034 -0.0142 -0.0292 503 GLU A OE1 3885 O OE2 . GLU A 507 ? 0.4639 0.5060 0.4980 -0.0003 -0.0138 -0.0256 503 GLU A OE2 3886 N N . PRO A 508 ? 0.4500 0.4772 0.4936 -0.0111 -0.0095 -0.0254 504 PRO A N 3887 C CA . PRO A 508 ? 0.4390 0.4652 0.4798 -0.0092 -0.0106 -0.0255 504 PRO A CA 3888 C C . PRO A 508 ? 0.4272 0.4519 0.4642 -0.0068 -0.0105 -0.0220 504 PRO A C 3889 O O . PRO A 508 ? 0.4551 0.4766 0.4914 -0.0071 -0.0095 -0.0195 504 PRO A O 3890 C CB . PRO A 508 ? 0.4453 0.4658 0.4866 -0.0106 -0.0096 -0.0257 504 PRO A CB 3891 C CG . PRO A 508 ? 0.4549 0.4714 0.4966 -0.0118 -0.0079 -0.0232 504 PRO A CG 3892 C CD . PRO A 508 ? 0.4655 0.4866 0.5099 -0.0130 -0.0077 -0.0240 504 PRO A CD 3893 N N . GLY A 509 ? 0.3840 0.4113 0.4185 -0.0044 -0.0115 -0.0221 505 GLY A N 3894 C CA . GLY A 509 ? 0.3414 0.3670 0.3725 -0.0023 -0.0111 -0.0193 505 GLY A CA 3895 C C . GLY A 509 ? 0.3336 0.3600 0.3624 -0.0002 -0.0117 -0.0200 505 GLY A C 3896 O O . GLY A 509 ? 0.2917 0.3144 0.3192 0.0001 -0.0115 -0.0193 505 GLY A O 3897 N N . LEU A 510 ? 0.3051 0.3366 0.3337 0.0014 -0.0126 -0.0217 506 LEU A N 3898 C CA . LEU A 510 ? 0.3093 0.3420 0.3356 0.0037 -0.0132 -0.0226 506 LEU A CA 3899 C C . LEU A 510 ? 0.3142 0.3451 0.3417 0.0025 -0.0138 -0.0245 506 LEU A C 3900 O O . LEU A 510 ? 0.3161 0.3447 0.3414 0.0038 -0.0136 -0.0239 506 LEU A O 3901 C CB . LEU A 510 ? 0.3082 0.3478 0.3342 0.0059 -0.0142 -0.0244 506 LEU A CB 3902 C CG . LEU A 510 ? 0.3202 0.3618 0.3435 0.0089 -0.0148 -0.0254 506 LEU A CG 3903 C CD1 . LEU A 510 ? 0.2925 0.3304 0.3115 0.0114 -0.0134 -0.0223 506 LEU A CD1 3904 C CD2 . LEU A 510 ? 0.3416 0.3914 0.3649 0.0113 -0.0162 -0.0280 506 LEU A CD2 3905 N N . SER A 511 ? 0.3086 0.3402 0.3396 0.0000 -0.0142 -0.0268 507 SER A N 3906 C CA . SER A 511 ? 0.3229 0.3521 0.3548 -0.0011 -0.0145 -0.0287 507 SER A CA 3907 C C . SER A 511 ? 0.3237 0.3464 0.3542 -0.0015 -0.0135 -0.0264 507 SER A C 3908 O O . SER A 511 ? 0.3038 0.3247 0.3332 -0.0008 -0.0137 -0.0269 507 SER A O 3909 C CB . SER A 511 ? 0.3535 0.3838 0.3895 -0.0040 -0.0146 -0.0317 507 SER A CB 3910 O OG . SER A 511 ? 0.3935 0.4206 0.4311 -0.0061 -0.0133 -0.0300 507 SER A OG 3911 N N . THR A 512 ? 0.3005 0.3203 0.3311 -0.0024 -0.0125 -0.0240 508 THR A N 3912 C CA . THR A 512 ? 0.2908 0.3056 0.3199 -0.0023 -0.0117 -0.0219 508 THR A CA 3913 C C . THR A 512 ? 0.2893 0.3040 0.3154 0.0000 -0.0116 -0.0205 508 THR A C 3914 O O . THR A 512 ? 0.2855 0.2977 0.3105 0.0005 -0.0115 -0.0203 508 THR A O 3915 C CB . THR A 512 ? 0.3075 0.3200 0.3373 -0.0035 -0.0106 -0.0199 508 THR A CB 3916 O OG1 . THR A 512 ? 0.3587 0.3705 0.3914 -0.0057 -0.0102 -0.0212 508 THR A OG1 3917 C CG2 . THR A 512 ? 0.2588 0.2671 0.2869 -0.0030 -0.0099 -0.0178 508 THR A CG2 3918 N N . VAL A 513 ? 0.2771 0.2943 0.3017 0.0015 -0.0115 -0.0195 509 VAL A N 3919 C CA . VAL A 513 ? 0.2749 0.2917 0.2968 0.0036 -0.0109 -0.0182 509 VAL A CA 3920 C C . VAL A 513 ? 0.2872 0.3049 0.3082 0.0049 -0.0116 -0.0199 509 VAL A C 3921 O O . VAL A 513 ? 0.2920 0.3076 0.3115 0.0057 -0.0111 -0.0193 509 VAL A O 3922 C CB . VAL A 513 ? 0.2818 0.3011 0.3021 0.0052 -0.0104 -0.0171 509 VAL A CB 3923 C CG1 . VAL A 513 ? 0.2783 0.2970 0.2955 0.0077 -0.0094 -0.0161 509 VAL A CG1 3924 C CG2 . VAL A 513 ? 0.2450 0.2628 0.2659 0.0040 -0.0096 -0.0153 509 VAL A CG2 3925 N N . GLN A 514 ? 0.2899 0.3112 0.3117 0.0052 -0.0127 -0.0222 510 GLN A N 3926 C CA . GLN A 514 ? 0.2923 0.3150 0.3132 0.0067 -0.0135 -0.0240 510 GLN A CA 3927 C C . GLN A 514 ? 0.2998 0.3190 0.3215 0.0054 -0.0136 -0.0247 510 GLN A C 3928 O O . GLN A 514 ? 0.3111 0.3293 0.3311 0.0068 -0.0135 -0.0247 510 GLN A O 3929 C CB . GLN A 514 ? 0.3063 0.3343 0.3284 0.0070 -0.0148 -0.0268 510 GLN A CB 3930 C CG . GLN A 514 ? 0.2911 0.3234 0.3112 0.0097 -0.0147 -0.0260 510 GLN A CG 3931 C CD . GLN A 514 ? 0.3582 0.3966 0.3800 0.0099 -0.0162 -0.0290 510 GLN A CD 3932 O OE1 . GLN A 514 ? 0.3665 0.4056 0.3918 0.0072 -0.0169 -0.0314 510 GLN A OE1 3933 N NE2 . GLN A 514 ? 0.3569 0.3998 0.3762 0.0133 -0.0164 -0.0290 510 GLN A NE2 3934 N N . ALA A 515 ? 0.3006 0.3176 0.3248 0.0029 -0.0135 -0.0251 511 ALA A N 3935 C CA . ALA A 515 ? 0.3171 0.3302 0.3417 0.0020 -0.0134 -0.0257 511 ALA A CA 3936 C C . ALA A 515 ? 0.3252 0.3350 0.3481 0.0027 -0.0126 -0.0233 511 ALA A C 3937 O O . ALA A 515 ? 0.3165 0.3246 0.3383 0.0035 -0.0126 -0.0236 511 ALA A O 3938 C CB . ALA A 515 ? 0.3111 0.3223 0.3386 -0.0007 -0.0131 -0.0266 511 ALA A CB 3939 N N . VAL A 516 ? 0.3079 0.3172 0.3305 0.0025 -0.0118 -0.0212 512 VAL A N 3940 C CA . VAL A 516 ? 0.2996 0.3068 0.3210 0.0031 -0.0110 -0.0194 512 VAL A CA 3941 C C . VAL A 516 ? 0.3081 0.3164 0.3275 0.0050 -0.0105 -0.0191 512 VAL A C 3942 O O . VAL A 516 ? 0.3112 0.3181 0.3299 0.0057 -0.0103 -0.0192 512 VAL A O 3943 C CB . VAL A 516 ? 0.3065 0.3131 0.3281 0.0023 -0.0102 -0.0176 512 VAL A CB 3944 C CG1 . VAL A 516 ? 0.3077 0.3131 0.3284 0.0029 -0.0094 -0.0163 512 VAL A CG1 3945 C CG2 . VAL A 516 ? 0.3073 0.3122 0.3307 0.0007 -0.0103 -0.0176 512 VAL A CG2 3946 N N . CYS A 517 ? 0.2959 0.3064 0.3141 0.0061 -0.0102 -0.0187 513 CYS A N 3947 C CA . CYS A 517 ? 0.2968 0.3076 0.3129 0.0081 -0.0092 -0.0180 513 CYS A CA 3948 C C . CYS A 517 ? 0.3059 0.3176 0.3210 0.0095 -0.0098 -0.0195 513 CYS A C 3949 O O . CYS A 517 ? 0.2972 0.3083 0.3107 0.0110 -0.0088 -0.0189 513 CYS A O 3950 C CB . CYS A 517 ? 0.3054 0.3182 0.3201 0.0094 -0.0085 -0.0172 513 CYS A CB 3951 S SG . CYS A 517 ? 0.3443 0.3561 0.3599 0.0079 -0.0077 -0.0155 513 CYS A SG 3952 N N . GLY A 518 ? 0.3243 0.3373 0.3405 0.0090 -0.0113 -0.0214 514 GLY A N 3953 C CA . GLY A 518 ? 0.3578 0.3717 0.3732 0.0104 -0.0121 -0.0232 514 GLY A CA 3954 C C . GLY A 518 ? 0.3651 0.3760 0.3806 0.0099 -0.0119 -0.0232 514 GLY A C 3955 O O . GLY A 518 ? 0.3836 0.3947 0.3979 0.0114 -0.0120 -0.0240 514 GLY A O 3956 N N . GLY A 519 ? 0.3472 0.3556 0.3640 0.0082 -0.0115 -0.0222 515 GLY A N 3957 C CA . GLY A 519 ? 0.3438 0.3498 0.3608 0.0081 -0.0114 -0.0222 515 GLY A CA 3958 C C . GLY A 519 ? 0.3359 0.3411 0.3523 0.0085 -0.0101 -0.0206 515 GLY A C 3959 O O . GLY A 519 ? 0.3011 0.3054 0.3172 0.0091 -0.0100 -0.0208 515 GLY A O 3960 N N . VAL A 520 ? 0.3112 0.3170 0.3278 0.0081 -0.0092 -0.0192 516 VAL A N 3961 C CA . VAL A 520 ? 0.3173 0.3226 0.3340 0.0080 -0.0079 -0.0182 516 VAL A CA 3962 C C . VAL A 520 ? 0.3240 0.3300 0.3402 0.0080 -0.0066 -0.0171 516 VAL A C 3963 O O . VAL A 520 ? 0.3302 0.3369 0.3462 0.0079 -0.0070 -0.0169 516 VAL A O 3964 C CB . VAL A 520 ? 0.3273 0.3315 0.3453 0.0069 -0.0083 -0.0180 516 VAL A CB 3965 C CG1 . VAL A 520 ? 0.3172 0.3212 0.3360 0.0057 -0.0085 -0.0173 516 VAL A CG1 3966 C CG2 . VAL A 520 ? 0.3580 0.3628 0.3764 0.0070 -0.0073 -0.0177 516 VAL A CG2 3967 N N . ARG A 521 ? 0.3129 0.3187 0.3289 0.0083 -0.0048 -0.0165 517 ARG A N 3968 C CA . ARG A 521 ? 0.3150 0.3207 0.3304 0.0082 -0.0031 -0.0154 517 ARG A CA 3969 C C . ARG A 521 ? 0.3130 0.3186 0.3295 0.0068 -0.0037 -0.0150 517 ARG A C 3970 O O . ARG A 521 ? 0.2878 0.2933 0.3058 0.0057 -0.0046 -0.0153 517 ARG A O 3971 C CB . ARG A 521 ? 0.3111 0.3161 0.3267 0.0081 -0.0007 -0.0152 517 ARG A CB 3972 C CG A ARG A 521 ? 0.2931 0.2979 0.3071 0.0098 0.0005 -0.0151 517 ARG A CG 3973 C CG B ARG A 521 ? 0.3198 0.3254 0.3378 0.0067 -0.0008 -0.0161 517 ARG A CG 3974 C CD A ARG A 521 ? 0.2895 0.2934 0.3039 0.0096 0.0035 -0.0148 517 ARG A CD 3975 C CD B ARG A 521 ? 0.2732 0.2791 0.2920 0.0066 0.0014 -0.0167 517 ARG A CD 3976 N NE A ARG A 521 ? 0.2970 0.2994 0.3096 0.0104 0.0059 -0.0134 517 ARG A NE 3977 N NE B ARG A 521 ? 0.2933 0.3007 0.3146 0.0052 0.0015 -0.0179 517 ARG A NE 3978 C CZ A ARG A 521 ? 0.2674 0.2683 0.2808 0.0095 0.0089 -0.0132 517 ARG A CZ 3979 C CZ B ARG A 521 ? 0.3442 0.3519 0.3670 0.0039 0.0035 -0.0183 517 ARG A CZ 3980 N NH1 A ARG A 521 ? 0.1023 0.1039 0.1185 0.0076 0.0094 -0.0145 517 ARG A NH1 3981 N NH1 B ARG A 521 ? 0.3899 0.3956 0.4116 0.0040 0.0060 -0.0174 517 ARG A NH1 3982 N NH2 A ARG A 521 ? 0.2173 0.2162 0.2286 0.0106 0.0114 -0.0117 517 ARG A NH2 3983 N NH2 B ARG A 521 ? 0.3350 0.3450 0.3602 0.0027 0.0033 -0.0198 517 ARG A NH2 3984 N N . CYS A 522 ? 0.3245 0.3303 0.3401 0.0071 -0.0032 -0.0141 518 CYS A N 3985 C CA . CYS A 522 ? 0.3342 0.3402 0.3508 0.0060 -0.0039 -0.0136 518 CYS A CA 3986 C C . CYS A 522 ? 0.3368 0.3423 0.3525 0.0061 -0.0022 -0.0125 518 CYS A C 3987 O O . CYS A 522 ? 0.3271 0.3324 0.3409 0.0076 -0.0007 -0.0118 518 CYS A O 3988 C CB . CYS A 522 ? 0.3348 0.3420 0.3514 0.0061 -0.0056 -0.0141 518 CYS A CB 3989 S SG . CYS A 522 ? 0.3832 0.3922 0.3976 0.0083 -0.0052 -0.0138 518 CYS A SG 3990 N N . ALA A 523 ? 0.3101 0.3153 0.3269 0.0048 -0.0022 -0.0122 519 ALA A N 3991 C CA . ALA A 523 ? 0.3046 0.3094 0.3208 0.0048 -0.0008 -0.0112 519 ALA A CA 3992 C C . ALA A 523 ? 0.2796 0.2855 0.2961 0.0044 -0.0024 -0.0108 519 ALA A C 3993 O O . ALA A 523 ? 0.2832 0.2893 0.3012 0.0033 -0.0037 -0.0111 519 ALA A O 3994 C CB . ALA A 523 ? 0.3049 0.3089 0.3224 0.0034 0.0004 -0.0115 519 ALA A CB 3995 N N . THR A 524 ? 0.2817 0.2885 0.2969 0.0056 -0.0021 -0.0101 520 THR A N 3996 C CA . THR A 524 ? 0.2696 0.2780 0.2853 0.0053 -0.0035 -0.0099 520 THR A CA 3997 C C . THR A 524 ? 0.2663 0.2741 0.2817 0.0051 -0.0023 -0.0088 520 THR A C 3998 O O . THR A 524 ? 0.2762 0.2829 0.2897 0.0062 -0.0004 -0.0080 520 THR A O 3999 C CB . THR A 524 ? 0.2570 0.2677 0.2714 0.0070 -0.0040 -0.0102 520 THR A CB 4000 O OG1 . THR A 524 ? 0.2813 0.2926 0.2963 0.0071 -0.0052 -0.0116 520 THR A OG1 4001 C CG2 . THR A 524 ? 0.2540 0.2671 0.2695 0.0066 -0.0052 -0.0103 520 THR A CG2 4002 N N . VAL A 525 ? 0.2593 0.2673 0.2761 0.0037 -0.0032 -0.0087 521 VAL A N 4003 C CA . VAL A 525 ? 0.2603 0.2680 0.2768 0.0035 -0.0024 -0.0077 521 VAL A CA 4004 C C . VAL A 525 ? 0.2648 0.2746 0.2815 0.0038 -0.0033 -0.0073 521 VAL A C 4005 O O . VAL A 525 ? 0.2558 0.2667 0.2743 0.0028 -0.0047 -0.0078 521 VAL A O 4006 C CB . VAL A 525 ? 0.2463 0.2530 0.2642 0.0021 -0.0027 -0.0079 521 VAL A CB 4007 C CG1 . VAL A 525 ? 0.2737 0.2804 0.2913 0.0020 -0.0019 -0.0070 521 VAL A CG1 4008 C CG2 . VAL A 525 ? 0.2511 0.2567 0.2693 0.0018 -0.0018 -0.0087 521 VAL A CG2 4009 N N . LEU A 526 ? 0.2560 0.2666 0.2709 0.0054 -0.0023 -0.0065 522 LEU A N 4010 C CA . LEU A 526 ? 0.2538 0.2673 0.2689 0.0059 -0.0032 -0.0063 522 LEU A CA 4011 C C . LEU A 526 ? 0.2508 0.2641 0.2661 0.0054 -0.0027 -0.0053 522 LEU A C 4012 O O . LEU A 526 ? 0.2457 0.2573 0.2594 0.0061 -0.0012 -0.0043 522 LEU A O 4013 C CB . LEU A 526 ? 0.2692 0.2843 0.2817 0.0086 -0.0024 -0.0060 522 LEU A CB 4014 C CG . LEU A 526 ? 0.2775 0.2967 0.2901 0.0097 -0.0032 -0.0060 522 LEU A CG 4015 C CD1 . LEU A 526 ? 0.2723 0.2947 0.2879 0.0082 -0.0053 -0.0077 522 LEU A CD1 4016 C CD2 . LEU A 526 ? 0.2998 0.3206 0.3090 0.0131 -0.0023 -0.0055 522 LEU A CD2 4017 N N . ILE A 527 ? 0.2654 0.2801 0.2828 0.0040 -0.0039 -0.0055 523 ILE A N 4018 C CA . ILE A 527 ? 0.2675 0.2821 0.2851 0.0036 -0.0035 -0.0044 523 ILE A CA 4019 C C . ILE A 527 ? 0.2823 0.3005 0.2999 0.0046 -0.0038 -0.0042 523 ILE A C 4020 O O . ILE A 527 ? 0.2931 0.3141 0.3127 0.0040 -0.0049 -0.0053 523 ILE A O 4021 C CB . ILE A 527 ? 0.2663 0.2803 0.2862 0.0018 -0.0042 -0.0045 523 ILE A CB 4022 C CG1 . ILE A 527 ? 0.2944 0.3057 0.3141 0.0013 -0.0041 -0.0048 523 ILE A CG1 4023 C CG2 . ILE A 527 ? 0.2606 0.2750 0.2808 0.0015 -0.0039 -0.0034 523 ILE A CG2 4024 C CD1 . ILE A 527 ? 0.2997 0.3093 0.3181 0.0016 -0.0029 -0.0042 523 ILE A CD1 4025 N N . SER A 528 ? 0.2721 0.2903 0.2876 0.0062 -0.0026 -0.0030 524 SER A N 4026 C CA . SER A 528 ? 0.2799 0.3022 0.2952 0.0075 -0.0030 -0.0029 524 SER A CA 4027 C C . SER A 528 ? 0.2770 0.2986 0.2904 0.0087 -0.0016 -0.0013 524 SER A C 4028 O O . SER A 528 ? 0.2782 0.2959 0.2898 0.0089 -0.0002 -0.0004 524 SER A O 4029 C CB . SER A 528 ? 0.2803 0.3049 0.2938 0.0098 -0.0030 -0.0035 524 SER A CB 4030 O OG . SER A 528 ? 0.2829 0.3043 0.2930 0.0118 -0.0011 -0.0022 524 SER A OG 4031 N N . GLY A 529 ? 0.2719 0.2973 0.2855 0.0097 -0.0020 -0.0010 525 GLY A N 4032 C CA . GLY A 529 ? 0.2559 0.2808 0.2673 0.0112 -0.0006 0.0006 525 GLY A CA 4033 C C . GLY A 529 ? 0.2604 0.2853 0.2679 0.0146 0.0007 0.0014 525 GLY A C 4034 O O . GLY A 529 ? 0.2624 0.2867 0.2676 0.0164 0.0021 0.0028 525 GLY A O 4035 N N . ARG A 530 ? 0.2604 0.2857 0.2670 0.0158 0.0006 0.0007 526 ARG A N 4036 C CA . ARG A 530 ? 0.2600 0.2871 0.2631 0.0196 0.0016 0.0013 526 ARG A CA 4037 C C . ARG A 530 ? 0.2749 0.3025 0.2776 0.0203 0.0011 0.0002 526 ARG A C 4038 O O . ARG A 530 ? 0.2927 0.3207 0.2984 0.0178 -0.0005 -0.0014 526 ARG A O 4039 C CB . ARG A 530 ? 0.2588 0.2925 0.2626 0.0211 0.0003 0.0008 526 ARG A CB 4040 C CG . ARG A 530 ? 0.2501 0.2887 0.2586 0.0185 -0.0023 -0.0016 526 ARG A CG 4041 C CD . ARG A 530 ? 0.2541 0.2998 0.2642 0.0195 -0.0035 -0.0025 526 ARG A CD 4042 N NE . ARG A 530 ? 0.2776 0.3264 0.2928 0.0159 -0.0052 -0.0046 526 ARG A NE 4043 C CZ . ARG A 530 ? 0.2773 0.3314 0.2954 0.0151 -0.0059 -0.0056 526 ARG A CZ 4044 N NH1 . ARG A 530 ? 0.2723 0.3303 0.2888 0.0179 -0.0055 -0.0048 526 ARG A NH1 4045 N NH2 . ARG A 530 ? 0.2745 0.3302 0.2974 0.0116 -0.0069 -0.0075 526 ARG A NH2 4046 N N . PRO A 531 ? 0.3001 0.3278 0.2988 0.0241 0.0025 0.0011 527 PRO A N 4047 C CA . PRO A 531 ? 0.2855 0.3151 0.2837 0.0255 0.0018 -0.0001 527 PRO A CA 4048 C C . PRO A 531 ? 0.2847 0.3213 0.2862 0.0247 -0.0012 -0.0025 527 PRO A C 4049 O O . PRO A 531 ? 0.2705 0.3121 0.2730 0.0254 -0.0021 -0.0029 527 PRO A O 4050 C CB . PRO A 531 ? 0.2879 0.3174 0.2807 0.0305 0.0039 0.0016 527 PRO A CB 4051 C CG . PRO A 531 ? 0.3538 0.3780 0.3442 0.0310 0.0067 0.0039 527 PRO A CG 4052 C CD . PRO A 531 ? 0.2805 0.3061 0.2748 0.0275 0.0051 0.0032 527 PRO A CD 4053 N N . VAL A 532 ? 0.2761 0.3132 0.2793 0.0234 -0.0025 -0.0042 528 VAL A N 4054 C CA . VAL A 532 ? 0.2829 0.3261 0.2896 0.0223 -0.0050 -0.0070 528 VAL A CA 4055 C C . VAL A 532 ? 0.2962 0.3404 0.3010 0.0246 -0.0053 -0.0080 528 VAL A C 4056 O O . VAL A 532 ? 0.3122 0.3515 0.3139 0.0259 -0.0035 -0.0064 528 VAL A O 4057 C CB . VAL A 532 ? 0.2825 0.3243 0.2940 0.0175 -0.0063 -0.0084 528 VAL A CB 4058 C CG1 . VAL A 532 ? 0.2621 0.3038 0.2758 0.0154 -0.0062 -0.0076 528 VAL A CG1 4059 C CG2 . VAL A 532 ? 0.2952 0.3305 0.3065 0.0157 -0.0056 -0.0078 528 VAL A CG2 4060 N N . VAL A 533 ? 0.2954 0.3461 0.3019 0.0251 -0.0074 -0.0107 529 VAL A N 4061 C CA . VAL A 533 ? 0.3121 0.3645 0.3170 0.0274 -0.0079 -0.0119 529 VAL A CA 4062 C C . VAL A 533 ? 0.3150 0.3611 0.3205 0.0249 -0.0074 -0.0116 529 VAL A C 4063 O O . VAL A 533 ? 0.3247 0.3693 0.3341 0.0209 -0.0084 -0.0128 529 VAL A O 4064 C CB . VAL A 533 ? 0.3108 0.3713 0.3189 0.0270 -0.0106 -0.0158 529 VAL A CB 4065 C CG1 . VAL A 533 ? 0.3135 0.3754 0.3200 0.0292 -0.0113 -0.0172 529 VAL A CG1 4066 C CG2 . VAL A 533 ? 0.3147 0.3829 0.3222 0.0300 -0.0113 -0.0165 529 VAL A CG2 4067 N N . VAL A 534 ? 0.3196 0.3622 0.3212 0.0275 -0.0056 -0.0100 530 VAL A N 4068 C CA . VAL A 534 ? 0.3092 0.3453 0.3111 0.0252 -0.0046 -0.0093 530 VAL A CA 4069 C C . VAL A 534 ? 0.3177 0.3537 0.3176 0.0273 -0.0044 -0.0098 530 VAL A C 4070 O O . VAL A 534 ? 0.2911 0.3229 0.2919 0.0253 -0.0040 -0.0098 530 VAL A O 4071 C CB . VAL A 534 ? 0.3186 0.3486 0.3186 0.0250 -0.0018 -0.0064 530 VAL A CB 4072 C CG1 . VAL A 534 ? 0.3116 0.3394 0.3064 0.0292 0.0010 -0.0043 530 VAL A CG1 4073 C CG2 . VAL A 534 ? 0.3132 0.3379 0.3156 0.0211 -0.0015 -0.0064 530 VAL A CG2 4074 N N . GLN A 535 ? 0.2938 0.3346 0.2910 0.0313 -0.0048 -0.0105 531 GLN A N 4075 C CA . GLN A 535 ? 0.3157 0.3560 0.3106 0.0336 -0.0045 -0.0109 531 GLN A CA 4076 C C . GLN A 535 ? 0.3038 0.3443 0.3026 0.0302 -0.0066 -0.0135 531 GLN A C 4077 O O . GLN A 535 ? 0.3164 0.3529 0.3144 0.0299 -0.0057 -0.0130 531 GLN A O 4078 C CB . GLN A 535 ? 0.3249 0.3713 0.3162 0.0390 -0.0049 -0.0115 531 GLN A CB 4079 C CG . GLN A 535 ? 0.3403 0.3853 0.3263 0.0435 -0.0020 -0.0083 531 GLN A CG 4080 C CD . GLN A 535 ? 0.3815 0.4319 0.3683 0.0443 -0.0032 -0.0088 531 GLN A CD 4081 O OE1 . GLN A 535 ? 0.3715 0.4231 0.3629 0.0402 -0.0050 -0.0103 531 GLN A OE1 4082 N NE2 . GLN A 535 ? 0.3600 0.4136 0.3419 0.0500 -0.0021 -0.0075 531 GLN A NE2 4083 N N . PRO A 536 ? 0.3157 0.3606 0.3186 0.0276 -0.0092 -0.0162 532 PRO A N 4084 C CA . PRO A 536 ? 0.3160 0.3600 0.3221 0.0246 -0.0107 -0.0185 532 PRO A CA 4085 C C . PRO A 536 ? 0.3121 0.3491 0.3198 0.0211 -0.0097 -0.0170 532 PRO A C 4086 O O . PRO A 536 ? 0.3059 0.3403 0.3137 0.0204 -0.0097 -0.0175 532 PRO A O 4087 C CB . PRO A 536 ? 0.3256 0.3750 0.3361 0.0222 -0.0131 -0.0216 532 PRO A CB 4088 C CG . PRO A 536 ? 0.3335 0.3896 0.3419 0.0262 -0.0134 -0.0220 532 PRO A CG 4089 C CD . PRO A 536 ? 0.3012 0.3526 0.3059 0.0279 -0.0108 -0.0179 532 PRO A CD 4090 N N . LEU A 537 ? 0.2923 0.3266 0.3010 0.0191 -0.0088 -0.0154 533 LEU A N 4091 C CA . LEU A 537 ? 0.2883 0.3168 0.2981 0.0164 -0.0077 -0.0140 533 LEU A CA 4092 C C . LEU A 537 ? 0.2976 0.3221 0.3042 0.0182 -0.0055 -0.0123 533 LEU A C 4093 O O . LEU A 537 ? 0.3024 0.3236 0.3099 0.0166 -0.0053 -0.0124 533 LEU A O 4094 C CB . LEU A 537 ? 0.2834 0.3102 0.2940 0.0149 -0.0069 -0.0124 533 LEU A CB 4095 C CG . LEU A 537 ? 0.3284 0.3578 0.3427 0.0123 -0.0086 -0.0139 533 LEU A CG 4096 C CD1 . LEU A 537 ? 0.3374 0.3659 0.3518 0.0116 -0.0077 -0.0121 533 LEU A CD1 4097 C CD2 . LEU A 537 ? 0.2809 0.3077 0.2981 0.0092 -0.0094 -0.0150 533 LEU A CD2 4098 N N . LEU A 538 ? 0.2998 0.3245 0.3028 0.0215 -0.0037 -0.0106 534 LEU A N 4099 C CA . LEU A 538 ? 0.3262 0.3469 0.3261 0.0233 -0.0011 -0.0089 534 LEU A CA 4100 C C . LEU A 538 ? 0.3273 0.3486 0.3267 0.0244 -0.0017 -0.0101 534 LEU A C 4101 O O . LEU A 538 ? 0.3371 0.3546 0.3364 0.0236 -0.0003 -0.0096 534 LEU A O 4102 C CB . LEU A 538 ? 0.3256 0.3463 0.3212 0.0273 0.0012 -0.0069 534 LEU A CB 4103 C CG . LEU A 538 ? 0.3552 0.3731 0.3502 0.0268 0.0031 -0.0050 534 LEU A CG 4104 C CD1 . LEU A 538 ? 0.3590 0.3780 0.3494 0.0315 0.0050 -0.0033 534 LEU A CD1 4105 C CD2 . LEU A 538 ? 0.3523 0.3640 0.3478 0.0245 0.0057 -0.0038 534 LEU A CD2 4106 N N . ALA A 539 ? 0.3347 0.3611 0.3338 0.0262 -0.0037 -0.0120 535 ALA A N 4107 C CA . ALA A 539 ? 0.3504 0.3779 0.3486 0.0278 -0.0043 -0.0133 535 ALA A CA 4108 C C . ALA A 539 ? 0.3493 0.3744 0.3507 0.0242 -0.0054 -0.0145 535 ALA A C 4109 O O . ALA A 539 ? 0.3524 0.3759 0.3527 0.0251 -0.0048 -0.0146 535 ALA A O 4110 C CB . ALA A 539 ? 0.3577 0.3921 0.3556 0.0300 -0.0068 -0.0157 535 ALA A CB 4111 N N . ALA A 540 ? 0.3156 0.3405 0.3206 0.0206 -0.0069 -0.0156 536 ALA A N 4112 C CA . ALA A 540 ? 0.3218 0.3445 0.3296 0.0177 -0.0078 -0.0167 536 ALA A CA 4113 C C . ALA A 540 ? 0.3036 0.3214 0.3114 0.0163 -0.0060 -0.0149 536 ALA A C 4114 O O . ALA A 540 ? 0.2926 0.3086 0.3016 0.0150 -0.0063 -0.0156 536 ALA A O 4115 C CB . ALA A 540 ? 0.3125 0.3364 0.3240 0.0146 -0.0098 -0.0183 536 ALA A CB 4116 N N . SER A 541 ? 0.2914 0.3074 0.2984 0.0164 -0.0041 -0.0129 537 SER A N 4117 C CA . SER A 541 ? 0.2917 0.3039 0.2998 0.0142 -0.0027 -0.0119 537 SER A CA 4118 C C . SER A 541 ? 0.3100 0.3194 0.3162 0.0155 0.0000 -0.0107 537 SER A C 4119 O O . SER A 541 ? 0.3144 0.3237 0.3176 0.0182 0.0018 -0.0095 537 SER A O 4120 C CB . SER A 541 ? 0.2893 0.3010 0.2977 0.0134 -0.0021 -0.0107 537 SER A CB 4121 O OG . SER A 541 ? 0.2950 0.3090 0.3055 0.0119 -0.0042 -0.0117 537 SER A OG 4122 N N . ASP A 542 ? 0.2990 0.3062 0.3068 0.0136 0.0006 -0.0109 538 ASP A N 4123 C CA . ASP A 542 ? 0.3055 0.3100 0.3124 0.0139 0.0036 -0.0100 538 ASP A CA 4124 C C . ASP A 542 ? 0.3073 0.3098 0.3138 0.0134 0.0058 -0.0088 538 ASP A C 4125 O O . ASP A 542 ? 0.3063 0.3068 0.3104 0.0152 0.0088 -0.0075 538 ASP A O 4126 C CB . ASP A 542 ? 0.3016 0.3053 0.3109 0.0119 0.0034 -0.0111 538 ASP A CB 4127 C CG . ASP A 542 ? 0.3352 0.3404 0.3446 0.0127 0.0014 -0.0123 538 ASP A CG 4128 O OD1 . ASP A 542 ? 0.3355 0.3421 0.3463 0.0117 -0.0011 -0.0134 538 ASP A OD1 4129 O OD2 . ASP A 542 ? 0.3003 0.3050 0.3081 0.0143 0.0027 -0.0122 538 ASP A OD2 4130 N N . ALA A 543 ? 0.2858 0.2886 0.2945 0.0112 0.0046 -0.0091 539 ALA A N 4131 C CA . ALA A 543 ? 0.2824 0.2835 0.2906 0.0108 0.0065 -0.0080 539 ALA A CA 4132 C C . ALA A 543 ? 0.2842 0.2874 0.2928 0.0106 0.0044 -0.0079 539 ALA A C 4133 O O . ALA A 543 ? 0.2617 0.2669 0.2720 0.0096 0.0018 -0.0088 539 ALA A O 4134 C CB . ALA A 543 ? 0.2833 0.2829 0.2940 0.0082 0.0075 -0.0088 539 ALA A CB 4135 N N . LEU A 544 ? 0.2874 0.2897 0.2944 0.0115 0.0059 -0.0066 540 LEU A N 4136 C CA . LEU A 544 ? 0.2872 0.2915 0.2947 0.0112 0.0042 -0.0064 540 LEU A CA 4137 C C . LEU A 544 ? 0.2939 0.2962 0.3009 0.0108 0.0061 -0.0053 540 LEU A C 4138 O O . LEU A 544 ? 0.3052 0.3049 0.3097 0.0123 0.0090 -0.0042 540 LEU A O 4139 C CB . LEU A 544 ? 0.2869 0.2942 0.2924 0.0137 0.0032 -0.0061 540 LEU A CB 4140 C CG . LEU A 544 ? 0.2849 0.2954 0.2919 0.0131 0.0010 -0.0064 540 LEU A CG 4141 C CD1 . LEU A 544 ? 0.3278 0.3423 0.3348 0.0143 -0.0010 -0.0076 540 LEU A CD1 4142 C CD2 . LEU A 544 ? 0.2918 0.3020 0.2966 0.0146 0.0026 -0.0048 540 LEU A CD2 4143 N N . VAL A 545 ? 0.2909 0.2940 0.2998 0.0089 0.0047 -0.0056 541 VAL A N 4144 C CA . VAL A 545 ? 0.2625 0.2640 0.2713 0.0083 0.0061 -0.0050 541 VAL A CA 4145 C C . VAL A 545 ? 0.2788 0.2825 0.2874 0.0088 0.0047 -0.0043 541 VAL A C 4146 O O . VAL A 545 ? 0.2678 0.2740 0.2783 0.0078 0.0022 -0.0050 541 VAL A O 4147 C CB . VAL A 545 ? 0.2711 0.2718 0.2826 0.0057 0.0057 -0.0062 541 VAL A CB 4148 C CG1 . VAL A 545 ? 0.2637 0.2633 0.2751 0.0050 0.0070 -0.0058 541 VAL A CG1 4149 C CG2 . VAL A 545 ? 0.2708 0.2700 0.2831 0.0049 0.0071 -0.0073 541 VAL A CG2 4150 N N . ALA A 546 ? 0.2684 0.2711 0.2747 0.0104 0.0065 -0.0030 542 ALA A N 4151 C CA . ALA A 546 ? 0.2601 0.2649 0.2663 0.0107 0.0055 -0.0023 542 ALA A CA 4152 C C . ALA A 546 ? 0.2523 0.2555 0.2600 0.0087 0.0058 -0.0025 542 ALA A C 4153 O O . ALA A 546 ? 0.2725 0.2727 0.2791 0.0087 0.0082 -0.0021 542 ALA A O 4154 C CB . ALA A 546 ? 0.2654 0.2699 0.2679 0.0140 0.0075 -0.0007 542 ALA A CB 4155 N N . ALA A 547 ? 0.2511 0.2563 0.2614 0.0069 0.0035 -0.0031 543 ALA A N 4156 C CA . ALA A 547 ? 0.2451 0.2493 0.2567 0.0053 0.0035 -0.0034 543 ALA A CA 4157 C C . ALA A 547 ? 0.2544 0.2599 0.2656 0.0056 0.0031 -0.0024 543 ALA A C 4158 O O . ALA A 547 ? 0.2570 0.2620 0.2690 0.0047 0.0031 -0.0025 543 ALA A O 4159 C CB . ALA A 547 ? 0.2342 0.2394 0.2484 0.0035 0.0016 -0.0046 543 ALA A CB 4160 N N . TRP A 548 ? 0.2498 0.2573 0.2599 0.0072 0.0028 -0.0016 544 TRP A N 4161 C CA . TRP A 548 ? 0.2467 0.2560 0.2566 0.0077 0.0025 -0.0006 544 TRP A CA 4162 C C . TRP A 548 ? 0.2395 0.2502 0.2521 0.0058 0.0008 -0.0010 544 TRP A C 4163 O O . TRP A 548 ? 0.2444 0.2562 0.2588 0.0049 -0.0006 -0.0017 544 TRP A O 4164 C CB . TRP A 548 ? 0.2341 0.2409 0.2417 0.0087 0.0048 0.0003 544 TRP A CB 4165 C CG . TRP A 548 ? 0.2689 0.2731 0.2738 0.0105 0.0071 0.0007 544 TRP A CG 4166 C CD1 . TRP A 548 ? 0.2904 0.2907 0.2947 0.0099 0.0092 0.0003 544 TRP A CD1 4167 C CD2 . TRP A 548 ? 0.2525 0.2580 0.2549 0.0133 0.0076 0.0016 544 TRP A CD2 4168 N NE1 . TRP A 548 ? 0.2904 0.2887 0.2918 0.0121 0.0115 0.0011 544 TRP A NE1 4169 C CE2 . TRP A 548 ? 0.3230 0.3245 0.3230 0.0145 0.0105 0.0020 544 TRP A CE2 4170 C CE3 . TRP A 548 ? 0.2702 0.2801 0.2723 0.0149 0.0062 0.0020 544 TRP A CE3 4171 C CZ2 . TRP A 548 ? 0.3191 0.3205 0.3157 0.0178 0.0120 0.0032 544 TRP A CZ2 4172 C CZ3 . TRP A 548 ? 0.2951 0.3058 0.2941 0.0183 0.0073 0.0027 544 TRP A CZ3 4173 C CH2 . TRP A 548 ? 0.3138 0.3200 0.3098 0.0198 0.0102 0.0035 544 TRP A CH2 4174 N N . LEU A 549 ? 0.2428 0.2531 0.2553 0.0056 0.0012 -0.0003 545 LEU A N 4175 C CA . LEU A 549 ? 0.2437 0.2550 0.2582 0.0042 0.0000 -0.0003 545 LEU A CA 4176 C C . LEU A 549 ? 0.2407 0.2497 0.2548 0.0038 0.0007 -0.0006 545 LEU A C 4177 O O . LEU A 549 ? 0.2524 0.2611 0.2655 0.0042 0.0014 0.0001 545 LEU A O 4178 C CB . LEU A 549 ? 0.2198 0.2334 0.2344 0.0048 -0.0002 0.0008 545 LEU A CB 4179 C CG . LEU A 549 ? 0.2341 0.2510 0.2492 0.0055 -0.0009 0.0007 545 LEU A CG 4180 C CD1 . LEU A 549 ? 0.2040 0.2238 0.2194 0.0061 -0.0009 0.0015 545 LEU A CD1 4181 C CD2 . LEU A 549 ? 0.2580 0.2758 0.2757 0.0038 -0.0022 -0.0005 545 LEU A CD2 4182 N N . PRO A 550 ? 0.2336 0.2416 0.2485 0.0029 0.0004 -0.0017 546 PRO A N 4183 C CA . PRO A 550 ? 0.2439 0.2504 0.2586 0.0025 0.0013 -0.0027 546 PRO A CA 4184 C C . PRO A 550 ? 0.2301 0.2375 0.2453 0.0023 0.0006 -0.0027 546 PRO A C 4185 O O . PRO A 550 ? 0.2332 0.2401 0.2483 0.0022 0.0012 -0.0039 546 PRO A O 4186 C CB . PRO A 550 ? 0.2474 0.2533 0.2629 0.0019 0.0011 -0.0041 546 PRO A CB 4187 C CG . PRO A 550 ? 0.2599 0.2670 0.2765 0.0017 -0.0005 -0.0038 546 PRO A CG 4188 C CD . PRO A 550 ? 0.2302 0.2384 0.2462 0.0024 -0.0006 -0.0025 546 PRO A CD 4189 N N . GLY A 551 ? 0.2283 0.2370 0.2442 0.0024 -0.0005 -0.0017 547 GLY A N 4190 C CA . GLY A 551 ? 0.2267 0.2360 0.2425 0.0028 -0.0008 -0.0013 547 GLY A CA 4191 C C . GLY A 551 ? 0.2464 0.2561 0.2630 0.0028 -0.0018 -0.0020 547 GLY A C 4192 O O . GLY A 551 ? 0.2611 0.2705 0.2785 0.0023 -0.0023 -0.0024 547 GLY A O 4193 N N . SER A 552 ? 0.2504 0.2609 0.2664 0.0036 -0.0019 -0.0022 548 SER A N 4194 C CA . SER A 552 ? 0.2575 0.2688 0.2737 0.0043 -0.0028 -0.0024 548 SER A CA 4195 C C . SER A 552 ? 0.2518 0.2637 0.2687 0.0041 -0.0032 -0.0046 548 SER A C 4196 O O . SER A 552 ? 0.2559 0.2683 0.2729 0.0048 -0.0039 -0.0047 548 SER A O 4197 C CB . SER A 552 ? 0.2362 0.2486 0.2513 0.0058 -0.0028 -0.0018 548 SER A CB 4198 O OG . SER A 552 ? 0.2629 0.2764 0.2775 0.0059 -0.0025 -0.0035 548 SER A OG 4199 N N . GLU A 553 ? 0.2461 0.2579 0.2633 0.0032 -0.0025 -0.0062 549 GLU A N 4200 C CA . GLU A 553 ? 0.2514 0.2644 0.2695 0.0029 -0.0026 -0.0087 549 GLU A CA 4201 C C . GLU A 553 ? 0.2579 0.2698 0.2769 0.0019 -0.0024 -0.0091 549 GLU A C 4202 O O . GLU A 553 ? 0.2552 0.2660 0.2745 0.0009 -0.0012 -0.0100 549 GLU A O 4203 C CB . GLU A 553 ? 0.2513 0.2651 0.2697 0.0024 -0.0016 -0.0107 549 GLU A CB 4204 C CG . GLU A 553 ? 0.2457 0.2612 0.2631 0.0037 -0.0020 -0.0106 549 GLU A CG 4205 C CD . GLU A 553 ? 0.2519 0.2695 0.2687 0.0055 -0.0034 -0.0099 549 GLU A CD 4206 O OE1 . GLU A 553 ? 0.2601 0.2796 0.2777 0.0059 -0.0042 -0.0115 549 GLU A OE1 4207 O OE2 . GLU A 553 ? 0.2458 0.2630 0.2612 0.0067 -0.0036 -0.0078 549 GLU A OE2 4208 N N . GLY A 554 ? 0.2571 0.2688 0.2763 0.0023 -0.0033 -0.0083 550 GLY A N 4209 C CA . GLY A 554 ? 0.2433 0.2538 0.2631 0.0015 -0.0032 -0.0086 550 GLY A CA 4210 C C . GLY A 554 ? 0.2555 0.2670 0.2764 0.0010 -0.0028 -0.0109 550 GLY A C 4211 O O . GLY A 554 ? 0.2509 0.2613 0.2720 0.0003 -0.0023 -0.0112 550 GLY A O 4212 N N . GLN A 555 ? 0.2502 0.2641 0.2716 0.0013 -0.0030 -0.0127 551 GLN A N 4213 C CA . GLN A 555 ? 0.2605 0.2758 0.2835 0.0004 -0.0024 -0.0153 551 GLN A CA 4214 C C . GLN A 555 ? 0.2720 0.2852 0.2953 -0.0011 -0.0003 -0.0160 551 GLN A C 4215 O O . GLN A 555 ? 0.2674 0.2807 0.2920 -0.0021 0.0008 -0.0177 551 GLN A O 4216 C CB . GLN A 555 ? 0.2669 0.2861 0.2908 0.0011 -0.0030 -0.0177 551 GLN A CB 4217 C CG . GLN A 555 ? 0.2886 0.3098 0.3118 0.0031 -0.0048 -0.0171 551 GLN A CG 4218 C CD . GLN A 555 ? 0.3646 0.3899 0.3877 0.0046 -0.0057 -0.0189 551 GLN A CD 4219 O OE1 . GLN A 555 ? 0.3669 0.3959 0.3913 0.0051 -0.0062 -0.0213 551 GLN A OE1 4220 N NE2 . GLN A 555 ? 0.2788 0.3041 0.3006 0.0056 -0.0058 -0.0178 551 GLN A NE2 4221 N N . GLY A 556 ? 0.2588 0.2699 0.2808 -0.0011 0.0006 -0.0145 552 GLY A N 4222 C CA . GLY A 556 ? 0.2613 0.2696 0.2829 -0.0020 0.0029 -0.0145 552 GLY A CA 4223 C C . GLY A 556 ? 0.2633 0.2700 0.2847 -0.0020 0.0034 -0.0136 552 GLY A C 4224 O O . GLY A 556 ? 0.2686 0.2736 0.2902 -0.0027 0.0054 -0.0144 552 GLY A O 4225 N N . VAL A 557 ? 0.2666 0.2736 0.2874 -0.0012 0.0016 -0.0120 553 VAL A N 4226 C CA . VAL A 557 ? 0.2703 0.2762 0.2908 -0.0010 0.0017 -0.0114 553 VAL A CA 4227 C C . VAL A 557 ? 0.2771 0.2839 0.2991 -0.0016 0.0019 -0.0133 553 VAL A C 4228 O O . VAL A 557 ? 0.2776 0.2829 0.2996 -0.0019 0.0036 -0.0137 553 VAL A O 4229 C CB . VAL A 557 ? 0.2765 0.2828 0.2965 -0.0002 -0.0002 -0.0098 553 VAL A CB 4230 C CG1 A VAL A 557 ? 0.3086 0.3142 0.3283 0.0000 -0.0002 -0.0096 553 VAL A CG1 4231 C CG2 A VAL A 557 ? 0.2302 0.2362 0.2490 0.0002 -0.0002 -0.0081 553 VAL A CG2 4232 N N . THR A 558 ? 0.2711 0.2803 0.2942 -0.0015 0.0004 -0.0144 554 THR A N 4233 C CA . THR A 558 ? 0.2667 0.2774 0.2913 -0.0018 0.0004 -0.0162 554 THR A CA 4234 C C . THR A 558 ? 0.2742 0.2856 0.3004 -0.0031 0.0023 -0.0186 554 THR A C 4235 O O . THR A 558 ? 0.2871 0.2990 0.3146 -0.0037 0.0032 -0.0200 554 THR A O 4236 C CB . THR A 558 ? 0.2827 0.2961 0.3077 -0.0008 -0.0018 -0.0167 554 THR A CB 4237 O OG1 . THR A 558 ? 0.2854 0.3004 0.3103 -0.0004 -0.0023 -0.0170 554 THR A OG1 4238 C CG2 . THR A 558 ? 0.2683 0.2801 0.2919 0.0002 -0.0031 -0.0145 554 THR A CG2 4239 N N . ASP A 559 ? 0.2569 0.2683 0.2832 -0.0036 0.0033 -0.0193 555 ASP A N 4240 C CA . ASP A 559 ? 0.2822 0.2937 0.3105 -0.0053 0.0057 -0.0219 555 ASP A CA 4241 C C . ASP A 559 ? 0.2878 0.2958 0.3157 -0.0060 0.0084 -0.0214 555 ASP A C 4242 O O . ASP A 559 ? 0.2983 0.3066 0.3283 -0.0073 0.0103 -0.0235 555 ASP A O 4243 C CB . ASP A 559 ? 0.2635 0.2745 0.2915 -0.0058 0.0067 -0.0225 555 ASP A CB 4244 C CG . ASP A 559 ? 0.2885 0.3039 0.3175 -0.0053 0.0047 -0.0242 555 ASP A CG 4245 O OD1 . ASP A 559 ? 0.2783 0.2974 0.3083 -0.0046 0.0028 -0.0252 555 ASP A OD1 4246 O OD2 . ASP A 559 ? 0.2877 0.3029 0.3160 -0.0052 0.0048 -0.0242 555 ASP A OD2 4247 N N . ALA A 560 ? 0.2611 0.2659 0.2864 -0.0049 0.0087 -0.0185 556 ALA A N 4248 C CA . ALA A 560 ? 0.2694 0.2709 0.2937 -0.0048 0.0113 -0.0176 556 ALA A CA 4249 C C . ALA A 560 ? 0.2828 0.2851 0.3071 -0.0040 0.0101 -0.0172 556 ALA A C 4250 O O . ALA A 560 ? 0.2728 0.2740 0.2976 -0.0045 0.0122 -0.0178 556 ALA A O 4251 C CB . ALA A 560 ? 0.2820 0.2804 0.3032 -0.0034 0.0121 -0.0150 556 ALA A CB 4252 N N . LEU A 561 ? 0.2643 0.2684 0.2881 -0.0031 0.0071 -0.0163 557 LEU A N 4253 C CA . LEU A 561 ? 0.2845 0.2893 0.3083 -0.0024 0.0059 -0.0161 557 LEU A CA 4254 C C . LEU A 561 ? 0.2878 0.2945 0.3139 -0.0033 0.0064 -0.0183 557 LEU A C 4255 O O . LEU A 561 ? 0.2791 0.2851 0.3051 -0.0030 0.0072 -0.0183 557 LEU A O 4256 C CB . LEU A 561 ? 0.2826 0.2886 0.3057 -0.0014 0.0029 -0.0150 557 LEU A CB 4257 C CG . LEU A 561 ? 0.2906 0.2955 0.3119 -0.0005 0.0022 -0.0129 557 LEU A CG 4258 C CD1 . LEU A 561 ? 0.2731 0.2792 0.2945 -0.0001 -0.0004 -0.0123 557 LEU A CD1 4259 C CD2 . LEU A 561 ? 0.2621 0.2651 0.2816 0.0004 0.0034 -0.0118 557 LEU A CD2 4260 N N . PHE A 562 ? 0.2704 0.2800 0.2986 -0.0042 0.0058 -0.0204 558 PHE A N 4261 C CA . PHE A 562 ? 0.2793 0.2919 0.3100 -0.0049 0.0060 -0.0229 558 PHE A CA 4262 C C . PHE A 562 ? 0.2834 0.2958 0.3163 -0.0068 0.0092 -0.0252 558 PHE A C 4263 O O . PHE A 562 ? 0.2707 0.2863 0.3065 -0.0079 0.0096 -0.0280 558 PHE A O 4264 C CB . PHE A 562 ? 0.2661 0.2829 0.2977 -0.0042 0.0033 -0.0241 558 PHE A CB 4265 C CG . PHE A 562 ? 0.3093 0.3258 0.3390 -0.0024 0.0007 -0.0221 558 PHE A CG 4266 C CD1 . PHE A 562 ? 0.2822 0.2987 0.3118 -0.0017 0.0002 -0.0219 558 PHE A CD1 4267 C CD2 . PHE A 562 ? 0.3500 0.3659 0.3781 -0.0014 -0.0008 -0.0204 558 PHE A CD2 4268 C CE1 . PHE A 562 ? 0.2730 0.2886 0.3009 -0.0002 -0.0017 -0.0203 558 PHE A CE1 4269 C CE2 . PHE A 562 ? 0.3455 0.3606 0.3721 0.0000 -0.0027 -0.0187 558 PHE A CE2 4270 C CZ . PHE A 562 ? 0.3511 0.3659 0.3776 0.0005 -0.0031 -0.0187 558 PHE A CZ 4271 N N . GLY A 563 ? 0.2634 0.2719 0.2950 -0.0073 0.0116 -0.0242 559 GLY A N 4272 C CA . GLY A 563 ? 0.2883 0.2953 0.3220 -0.0093 0.0155 -0.0263 559 GLY A CA 4273 C C . GLY A 563 ? 0.3038 0.3136 0.3405 -0.0112 0.0161 -0.0296 559 GLY A C 4274 O O . GLY A 563 ? 0.2969 0.3062 0.3360 -0.0133 0.0193 -0.0321 559 GLY A O 4275 N N . ASP A 564 ? 0.2963 0.3090 0.3327 -0.0106 0.0133 -0.0299 560 ASP A N 4276 C CA . ASP A 564 ? 0.3097 0.3248 0.3484 -0.0120 0.0139 -0.0330 560 ASP A CA 4277 C C . ASP A 564 ? 0.3168 0.3270 0.3548 -0.0132 0.0175 -0.0326 560 ASP A C 4278 O O . ASP A 564 ? 0.3166 0.3275 0.3573 -0.0154 0.0198 -0.0359 560 ASP A O 4279 C CB . ASP A 564 ? 0.3176 0.3362 0.3554 -0.0105 0.0104 -0.0327 560 ASP A CB 4280 C CG . ASP A 564 ? 0.3710 0.3953 0.4101 -0.0094 0.0074 -0.0340 560 ASP A CG 4281 O OD1 . ASP A 564 ? 0.4203 0.4467 0.4616 -0.0101 0.0080 -0.0359 560 ASP A OD1 4282 O OD2 . ASP A 564 ? 0.4573 0.4836 0.4949 -0.0075 0.0047 -0.0331 560 ASP A OD2 4283 N N . PHE A 565 ? 0.3109 0.3162 0.3452 -0.0118 0.0181 -0.0288 561 PHE A N 4284 C CA . PHE A 565 ? 0.3209 0.3207 0.3537 -0.0123 0.0219 -0.0279 561 PHE A CA 4285 C C . PHE A 565 ? 0.3274 0.3229 0.3573 -0.0108 0.0234 -0.0247 561 PHE A C 4286 O O . PHE A 565 ? 0.3195 0.3164 0.3481 -0.0092 0.0208 -0.0228 561 PHE A O 4287 C CB . PHE A 565 ? 0.3188 0.3178 0.3493 -0.0113 0.0207 -0.0264 561 PHE A CB 4288 C CG . PHE A 565 ? 0.3605 0.3635 0.3934 -0.0124 0.0194 -0.0295 561 PHE A CG 4289 C CD1 . PHE A 565 ? 0.3496 0.3579 0.3831 -0.0113 0.0153 -0.0299 561 PHE A CD1 4290 C CD2 . PHE A 565 ? 0.3858 0.3873 0.4203 -0.0143 0.0224 -0.0322 561 PHE A CD2 4291 C CE1 . PHE A 565 ? 0.4007 0.4133 0.4360 -0.0119 0.0140 -0.0329 561 PHE A CE1 4292 C CE2 . PHE A 565 ? 0.4072 0.4133 0.4440 -0.0152 0.0210 -0.0355 561 PHE A CE2 4293 C CZ . PHE A 565 ? 0.3675 0.3794 0.4047 -0.0139 0.0167 -0.0358 561 PHE A CZ 4294 N N . GLY A 566 ? 0.3313 0.3215 0.3599 -0.0111 0.0278 -0.0240 562 GLY A N 4295 C CA . GLY A 566 ? 0.3323 0.3184 0.3572 -0.0089 0.0294 -0.0205 562 GLY A CA 4296 C C . GLY A 566 ? 0.3284 0.3132 0.3494 -0.0064 0.0278 -0.0173 562 GLY A C 4297 O O . GLY A 566 ? 0.3370 0.3220 0.3578 -0.0066 0.0270 -0.0175 562 GLY A O 4298 N N . PHE A 567 ? 0.2956 0.2793 0.3136 -0.0039 0.0272 -0.0145 563 PHE A N 4299 C CA . PHE A 567 ? 0.3238 0.3065 0.3382 -0.0014 0.0262 -0.0116 563 PHE A CA 4300 C C . PHE A 567 ? 0.3344 0.3117 0.3463 -0.0007 0.0307 -0.0105 563 PHE A C 4301 O O . PHE A 567 ? 0.3343 0.3077 0.3457 -0.0008 0.0349 -0.0106 563 PHE A O 4302 C CB . PHE A 567 ? 0.2932 0.2766 0.3051 0.0012 0.0247 -0.0094 563 PHE A CB 4303 C CG . PHE A 567 ? 0.2785 0.2666 0.2920 0.0010 0.0201 -0.0098 563 PHE A CG 4304 C CD1 . PHE A 567 ? 0.2798 0.2700 0.2956 -0.0001 0.0190 -0.0114 563 PHE A CD1 4305 C CD2 . PHE A 567 ? 0.2827 0.2730 0.2953 0.0019 0.0171 -0.0087 563 PHE A CD2 4306 C CE1 . PHE A 567 ? 0.2652 0.2590 0.2821 -0.0001 0.0150 -0.0117 563 PHE A CE1 4307 C CE2 . PHE A 567 ? 0.2532 0.2471 0.2672 0.0017 0.0134 -0.0090 563 PHE A CE2 4308 C CZ . PHE A 567 ? 0.2583 0.2537 0.2743 0.0008 0.0124 -0.0105 563 PHE A CZ 4309 N N . THR A 568 ? 0.3310 0.3077 0.3412 0.0001 0.0303 -0.0096 564 THR A N 4310 C CA . THR A 568 ? 0.3297 0.3008 0.3370 0.0012 0.0348 -0.0083 564 THR A CA 4311 C C . THR A 568 ? 0.3319 0.3027 0.3351 0.0044 0.0339 -0.0053 564 THR A C 4312 O O . THR A 568 ? 0.3290 0.2951 0.3289 0.0062 0.0376 -0.0037 564 THR A O 4313 C CB . THR A 568 ? 0.3348 0.3047 0.3446 -0.0015 0.0365 -0.0109 564 THR A CB 4314 O OG1 . THR A 568 ? 0.3461 0.3206 0.3574 -0.0023 0.0323 -0.0119 564 THR A OG1 4315 C CG2 . THR A 568 ? 0.3667 0.3364 0.3806 -0.0048 0.0387 -0.0143 564 THR A CG2 4316 N N . GLY A 569 ? 0.3176 0.2934 0.3211 0.0052 0.0292 -0.0047 565 GLY A N 4317 C CA . GLY A 569 ? 0.2955 0.2722 0.2959 0.0079 0.0280 -0.0023 565 GLY A CA 4318 C C . GLY A 569 ? 0.3132 0.2877 0.3093 0.0116 0.0302 0.0002 565 GLY A C 4319 O O . GLY A 569 ? 0.3052 0.2793 0.3010 0.0121 0.0308 0.0003 565 GLY A O 4320 N N . ARG A 570 ? 0.3036 0.2766 0.2961 0.0143 0.0315 0.0023 566 ARG A N 4321 C CA . ARG A 570 ? 0.3211 0.2927 0.3089 0.0186 0.0334 0.0048 566 ARG A CA 4322 C C . ARG A 570 ? 0.3325 0.3087 0.3186 0.0211 0.0304 0.0062 566 ARG A C 4323 O O . ARG A 570 ? 0.3088 0.2859 0.2957 0.0202 0.0294 0.0060 566 ARG A O 4324 C CB . ARG A 570 ? 0.3234 0.2879 0.3079 0.0198 0.0391 0.0060 566 ARG A CB 4325 C CG A ARG A 570 ? 0.3624 0.3229 0.3497 0.0165 0.0422 0.0040 566 ARG A CG 4326 C CG B ARG A 570 ? 0.3425 0.3017 0.3273 0.0187 0.0435 0.0054 566 ARG A CG 4327 C CD A ARG A 570 ? 0.4984 0.4513 0.4838 0.0166 0.0483 0.0043 566 ARG A CD 4328 C CD B ARG A 570 ? 0.3682 0.3199 0.3497 0.0200 0.0494 0.0066 566 ARG A CD 4329 N NE A ARG A 570 ? 0.5409 0.4899 0.5205 0.0213 0.0519 0.0075 566 ARG A NE 4330 N NE B ARG A 570 ? 0.3641 0.3143 0.3489 0.0162 0.0499 0.0042 566 ARG A NE 4331 C CZ A ARG A 570 ? 0.5765 0.5230 0.5515 0.0248 0.0538 0.0098 566 ARG A CZ 4332 C CZ B ARG A 570 ? 0.3885 0.3333 0.3715 0.0163 0.0540 0.0044 566 ARG A CZ 4333 N NH1 A ARG A 570 ? 0.5825 0.5300 0.5585 0.0236 0.0523 0.0092 566 ARG A NH1 4334 N NH1 B ARG A 570 ? 0.3550 0.2995 0.3416 0.0126 0.0539 0.0017 566 ARG A NH1 4335 N NH2 A ARG A 570 ? 0.5800 0.5232 0.5495 0.0296 0.0572 0.0128 566 ARG A NH2 4336 N NH2 B ARG A 570 ? 0.4414 0.3810 0.4189 0.0204 0.0582 0.0074 566 ARG A NH2 4337 N N . LEU A 571 ? 0.3150 0.2946 0.2991 0.0242 0.0289 0.0073 567 LEU A N 4338 C CA . LEU A 571 ? 0.3133 0.2981 0.2964 0.0263 0.0260 0.0081 567 LEU A CA 4339 C C . LEU A 571 ? 0.3247 0.3074 0.3048 0.0283 0.0280 0.0097 567 LEU A C 4340 O O . LEU A 571 ? 0.3291 0.3067 0.3052 0.0309 0.0323 0.0113 567 LEU A O 4341 C CB . LEU A 571 ? 0.3108 0.2991 0.2913 0.0301 0.0251 0.0090 567 LEU A CB 4342 C CG . LEU A 571 ? 0.3323 0.3241 0.3156 0.0287 0.0222 0.0074 567 LEU A CG 4343 C CD1 . LEU A 571 ? 0.2836 0.2793 0.2636 0.0331 0.0215 0.0082 567 LEU A CD1 4344 C CD2 . LEU A 571 ? 0.2721 0.2686 0.2603 0.0250 0.0178 0.0054 567 LEU A CD2 4345 N N . PRO A 572 ? 0.3152 0.3015 0.2973 0.0271 0.0253 0.0092 568 PRO A N 4346 C CA . PRO A 572 ? 0.3172 0.3025 0.2966 0.0292 0.0268 0.0107 568 PRO A CA 4347 C C . PRO A 572 ? 0.3275 0.3180 0.3041 0.0333 0.0253 0.0120 568 PRO A C 4348 O O . PRO A 572 ? 0.3337 0.3247 0.3082 0.0354 0.0259 0.0132 568 PRO A O 4349 C CB . PRO A 572 ? 0.2908 0.2780 0.2741 0.0255 0.0242 0.0093 568 PRO A CB 4350 C CG . PRO A 572 ? 0.2796 0.2723 0.2670 0.0233 0.0200 0.0077 568 PRO A CG 4351 C CD . PRO A 572 ? 0.3056 0.2961 0.2928 0.0233 0.0212 0.0072 568 PRO A CD 4352 N N . ARG A 573 ? 0.3365 0.3312 0.3135 0.0345 0.0233 0.0116 569 ARG A N 4353 C CA . ARG A 573 ? 0.3556 0.3574 0.3314 0.0379 0.0209 0.0119 569 ARG A CA 4354 C C . ARG A 573 ? 0.3443 0.3467 0.3178 0.0406 0.0215 0.0121 569 ARG A C 4355 O O . ARG A 573 ? 0.3463 0.3461 0.3215 0.0383 0.0218 0.0112 569 ARG A O 4356 C CB . ARG A 573 ? 0.3446 0.3534 0.3256 0.0348 0.0161 0.0097 569 ARG A CB 4357 C CG . ARG A 573 ? 0.3990 0.4091 0.3828 0.0323 0.0147 0.0093 569 ARG A CG 4358 C CD . ARG A 573 ? 0.3565 0.3744 0.3435 0.0317 0.0110 0.0081 569 ARG A CD 4359 N NE . ARG A 573 ? 0.3702 0.3931 0.3542 0.0362 0.0109 0.0087 569 ARG A NE 4360 C CZ . ARG A 573 ? 0.3760 0.3997 0.3574 0.0389 0.0120 0.0102 569 ARG A CZ 4361 N NH1 . ARG A 573 ? 0.3437 0.3632 0.3250 0.0373 0.0134 0.0111 569 ARG A NH1 4362 N NH2 . ARG A 573 ? 0.3871 0.4161 0.3656 0.0434 0.0118 0.0107 569 ARG A NH2 4363 N N . THR A 574 ? 0.3500 0.3570 0.3202 0.0453 0.0211 0.0129 570 THR A N 4364 C CA . THR A 574 ? 0.3554 0.3652 0.3237 0.0483 0.0207 0.0127 570 THR A CA 4365 C C . THR A 574 ? 0.3536 0.3695 0.3272 0.0451 0.0162 0.0098 570 THR A C 4366 O O . THR A 574 ? 0.3594 0.3806 0.3365 0.0431 0.0131 0.0084 570 THR A O 4367 C CB . THR A 574 ? 0.3686 0.3833 0.3320 0.0548 0.0211 0.0140 570 THR A CB 4368 O OG1 . THR A 574 ? 0.3553 0.3630 0.3130 0.0583 0.0259 0.0170 570 THR A OG1 4369 C CG2 . THR A 574 ? 0.3609 0.3807 0.3228 0.0581 0.0197 0.0132 570 THR A CG2 4370 N N . TRP A 575 ? 0.3363 0.3512 0.3101 0.0447 0.0161 0.0091 571 TRP A N 4371 C CA . TRP A 575 ? 0.3279 0.3485 0.3058 0.0426 0.0123 0.0065 571 TRP A CA 4372 C C . TRP A 575 ? 0.3395 0.3661 0.3144 0.0476 0.0114 0.0061 571 TRP A C 4373 O O . TRP A 575 ? 0.3570 0.3811 0.3278 0.0510 0.0137 0.0074 571 TRP A O 4374 C CB . TRP A 575 ? 0.3266 0.3433 0.3072 0.0389 0.0122 0.0054 571 TRP A CB 4375 C CG . TRP A 575 ? 0.2937 0.3147 0.2798 0.0349 0.0082 0.0027 571 TRP A CG 4376 C CD1 . TRP A 575 ? 0.3226 0.3504 0.3103 0.0355 0.0052 0.0006 571 TRP A CD1 4377 C CD2 . TRP A 575 ? 0.3005 0.3192 0.2909 0.0299 0.0072 0.0018 571 TRP A CD2 4378 N NE1 . TRP A 575 ? 0.3046 0.3338 0.2976 0.0309 0.0025 -0.0015 571 TRP A NE1 4379 C CE2 . TRP A 575 ? 0.3006 0.3243 0.2951 0.0276 0.0037 -0.0006 571 TRP A CE2 4380 C CE3 . TRP A 575 ? 0.3032 0.3165 0.2946 0.0272 0.0089 0.0026 571 TRP A CE3 4381 C CZ2 . TRP A 575 ? 0.2711 0.2937 0.2699 0.0231 0.0022 -0.0018 571 TRP A CZ2 4382 C CZ3 . TRP A 575 ? 0.2966 0.3097 0.2925 0.0228 0.0069 0.0012 571 TRP A CZ3 4383 C CH2 . TRP A 575 ? 0.3227 0.3402 0.3219 0.0210 0.0038 -0.0007 571 TRP A CH2 4384 N N . PHE A 576 ? 0.3520 0.3867 0.3290 0.0480 0.0081 0.0043 572 PHE A N 4385 C CA . PHE A 576 ? 0.3601 0.4024 0.3347 0.0528 0.0067 0.0033 572 PHE A CA 4386 C C . PHE A 576 ? 0.3652 0.4101 0.3415 0.0521 0.0048 0.0010 572 PHE A C 4387 O O . PHE A 576 ? 0.3357 0.3786 0.3164 0.0472 0.0034 -0.0005 572 PHE A O 4388 C CB . PHE A 576 ? 0.3659 0.4169 0.3432 0.0528 0.0038 0.0014 572 PHE A CB 4389 C CG . PHE A 576 ? 0.3419 0.3948 0.3263 0.0465 0.0008 -0.0012 572 PHE A CG 4390 C CD1 . PHE A 576 ? 0.3530 0.4107 0.3413 0.0445 -0.0021 -0.0044 572 PHE A CD1 4391 C CD2 . PHE A 576 ? 0.3439 0.3935 0.3307 0.0430 0.0012 -0.0003 572 PHE A CD2 4392 C CE1 . PHE A 576 ? 0.3891 0.4475 0.3835 0.0388 -0.0042 -0.0065 572 PHE A CE1 4393 C CE2 . PHE A 576 ? 0.3714 0.4220 0.3642 0.0376 -0.0010 -0.0023 572 PHE A CE2 4394 C CZ . PHE A 576 ? 0.3389 0.3935 0.3354 0.0354 -0.0035 -0.0053 572 PHE A CZ 4395 N N . LYS A 577 ? 0.3549 0.4047 0.3275 0.0575 0.0046 0.0007 573 LYS A N 4396 C CA . LYS A 577 ? 0.3719 0.4258 0.3462 0.0572 0.0022 -0.0020 573 LYS A CA 4397 C C . LYS A 577 ? 0.3650 0.4281 0.3447 0.0548 -0.0021 -0.0060 573 LYS A C 4398 O O . LYS A 577 ? 0.3542 0.4190 0.3381 0.0515 -0.0043 -0.0087 573 LYS A O 4399 C CB . LYS A 577 ? 0.3840 0.4400 0.3521 0.0641 0.0036 -0.0009 573 LYS A CB 4400 C CG . LYS A 577 ? 0.3885 0.4351 0.3517 0.0661 0.0082 0.0026 573 LYS A CG 4401 C CD . LYS A 577 ? 0.3848 0.4336 0.3414 0.0736 0.0097 0.0038 573 LYS A CD 4402 C CE . LYS A 577 ? 0.4143 0.4528 0.3666 0.0748 0.0147 0.0072 573 LYS A CE 4403 N NZ . LYS A 577 ? 0.4688 0.5092 0.4138 0.0828 0.0168 0.0089 573 LYS A NZ 4404 N N . SER A 578 ? 0.3579 0.4271 0.3376 0.0567 -0.0029 -0.0064 574 SER A N 4405 C CA . SER A 578 ? 0.3711 0.4502 0.3557 0.0553 -0.0066 -0.0104 574 SER A CA 4406 C C . SER A 578 ? 0.3645 0.4460 0.3501 0.0550 -0.0065 -0.0097 574 SER A C 4407 O O . SER A 578 ? 0.3573 0.4361 0.3380 0.0588 -0.0040 -0.0065 574 SER A O 4408 C CB . SER A 578 ? 0.3773 0.4655 0.3590 0.0611 -0.0080 -0.0124 574 SER A CB 4409 O OG . SER A 578 ? 0.4710 0.5698 0.4572 0.0603 -0.0112 -0.0164 574 SER A OG 4410 N N . VAL A 579 ? 0.3610 0.4475 0.3528 0.0507 -0.0090 -0.0126 575 VAL A N 4411 C CA . VAL A 579 ? 0.3711 0.4605 0.3642 0.0504 -0.0090 -0.0121 575 VAL A CA 4412 C C . VAL A 579 ? 0.3939 0.4925 0.3836 0.0567 -0.0095 -0.0126 575 VAL A C 4413 O O . VAL A 579 ? 0.3682 0.4679 0.3563 0.0585 -0.0085 -0.0109 575 VAL A O 4414 C CB . VAL A 579 ? 0.3734 0.4659 0.3741 0.0442 -0.0111 -0.0150 575 VAL A CB 4415 C CG1 . VAL A 579 ? 0.3572 0.4405 0.3606 0.0386 -0.0104 -0.0140 575 VAL A CG1 4416 C CG2 . VAL A 579 ? 0.3941 0.4965 0.3991 0.0436 -0.0141 -0.0200 575 VAL A CG2 4417 N N . ASP A 580 ? 0.4085 0.5137 0.3967 0.0604 -0.0109 -0.0150 576 ASP A N 4418 C CA . ASP A 580 ? 0.4333 0.5474 0.4172 0.0675 -0.0113 -0.0154 576 ASP A CA 4419 C C . ASP A 580 ? 0.4275 0.5359 0.4035 0.0732 -0.0077 -0.0104 576 ASP A C 4420 O O . ASP A 580 ? 0.4310 0.5455 0.4033 0.0789 -0.0075 -0.0099 576 ASP A O 4421 C CB . ASP A 580 ? 0.4551 0.5750 0.4375 0.0709 -0.0128 -0.0181 576 ASP A CB 4422 C CG . ASP A 580 ? 0.4984 0.6254 0.4881 0.0663 -0.0163 -0.0235 576 ASP A CG 4423 O OD1 . ASP A 580 ? 0.5616 0.6910 0.5574 0.0613 -0.0175 -0.0254 576 ASP A OD1 4424 O OD2 . ASP A 580 ? 0.6036 0.7333 0.5930 0.0675 -0.0175 -0.0258 576 ASP A OD2 4425 N N . GLN A 581 ? 0.3959 0.4925 0.3691 0.0720 -0.0048 -0.0069 577 GLN A N 4426 C CA . GLN A 581 ? 0.3966 0.4863 0.3626 0.0768 -0.0008 -0.0022 577 GLN A CA 4427 C C . GLN A 581 ? 0.3934 0.4805 0.3601 0.0753 0.0004 -0.0003 577 GLN A C 4428 O O . GLN A 581 ? 0.3857 0.4692 0.3463 0.0800 0.0035 0.0032 577 GLN A O 4429 C CB . GLN A 581 ? 0.3857 0.4634 0.3492 0.0753 0.0023 0.0006 577 GLN A CB 4430 C CG . GLN A 581 ? 0.4007 0.4790 0.3631 0.0766 0.0018 -0.0006 577 GLN A CG 4431 C CD . GLN A 581 ? 0.4334 0.4999 0.3941 0.0746 0.0050 0.0021 577 GLN A CD 4432 O OE1 . GLN A 581 ? 0.3894 0.4505 0.3548 0.0681 0.0047 0.0017 577 GLN A OE1 4433 N NE2 . GLN A 581 ? 0.3964 0.4589 0.3502 0.0803 0.0084 0.0049 577 GLN A NE2 4434 N N . LEU A 582 ? 0.3657 0.4537 0.3391 0.0688 -0.0016 -0.0022 578 LEU A N 4435 C CA . LEU A 582 ? 0.3652 0.4488 0.3391 0.0669 -0.0001 0.0000 578 LEU A CA 4436 C C . LEU A 582 ? 0.3793 0.4708 0.3513 0.0713 -0.0004 0.0001 578 LEU A C 4437 O O . LEU A 582 ? 0.3805 0.4830 0.3550 0.0727 -0.0033 -0.0032 578 LEU A O 4438 C CB . LEU A 582 ? 0.3449 0.4272 0.3263 0.0591 -0.0020 -0.0020 578 LEU A CB 4439 C CG . LEU A 582 ? 0.3295 0.4039 0.3127 0.0546 -0.0016 -0.0020 578 LEU A CG 4440 C CD1 . LEU A 582 ? 0.3132 0.3869 0.3037 0.0473 -0.0036 -0.0040 578 LEU A CD1 4441 C CD2 . LEU A 582 ? 0.3011 0.3645 0.2795 0.0556 0.0022 0.0019 578 LEU A CD2 4442 N N . PRO A 583 ? 0.3861 0.4722 0.3543 0.0731 0.0023 0.0035 579 PRO A N 4443 C CA . PRO A 583 ? 0.3967 0.4700 0.3627 0.0710 0.0057 0.0069 579 PRO A CA 4444 C C . PRO A 583 ? 0.4126 0.4789 0.3718 0.0755 0.0092 0.0096 579 PRO A C 4445 O O . PRO A 583 ? 0.4172 0.4876 0.3712 0.0821 0.0100 0.0105 579 PRO A O 4446 C CB . PRO A 583 ? 0.3820 0.4544 0.3464 0.0722 0.0072 0.0089 579 PRO A CB 4447 C CG . PRO A 583 ? 0.4072 0.4905 0.3690 0.0785 0.0060 0.0081 579 PRO A CG 4448 C CD . PRO A 583 ? 0.4087 0.5018 0.3752 0.0773 0.0021 0.0039 579 PRO A CD 4449 N N . MET A 584 ? 0.4026 0.4589 0.3620 0.0719 0.0113 0.0109 580 MET A N 4450 C CA . MET A 584 ? 0.4277 0.4765 0.3810 0.0757 0.0152 0.0136 580 MET A CA 4451 C C . MET A 584 ? 0.4260 0.4632 0.3795 0.0717 0.0185 0.0156 580 MET A C 4452 O O . MET A 584 ? 0.4209 0.4551 0.3795 0.0656 0.0172 0.0141 580 MET A O 4453 C CB . MET A 584 ? 0.4291 0.4808 0.3829 0.0763 0.0137 0.0118 580 MET A CB 4454 C CG . MET A 584 ? 0.4265 0.4706 0.3740 0.0803 0.0179 0.0146 580 MET A CG 4455 S SD . MET A 584 ? 0.4142 0.4621 0.3631 0.0803 0.0157 0.0122 580 MET A SD 4456 C CE . MET A 584 ? 0.3959 0.4379 0.3525 0.0706 0.0143 0.0104 580 MET A CE 4457 N N . ASN A 585 ? 0.4427 0.4737 0.3906 0.0753 0.0226 0.0188 581 ASN A N 4458 C CA . ASN A 585 ? 0.4695 0.4898 0.4175 0.0718 0.0260 0.0204 581 ASN A CA 4459 C C . ASN A 585 ? 0.4967 0.5080 0.4382 0.0756 0.0315 0.0233 581 ASN A C 4460 O O . ASN A 585 ? 0.4790 0.4919 0.4144 0.0825 0.0333 0.0252 581 ASN A O 4461 C CB . ASN A 585 ? 0.4638 0.4837 0.4116 0.0716 0.0264 0.0213 581 ASN A CB 4462 C CG . ASN A 585 ? 0.4383 0.4663 0.3927 0.0674 0.0216 0.0186 581 ASN A CG 4463 O OD1 . ASN A 585 ? 0.4390 0.4649 0.3988 0.0613 0.0201 0.0171 581 ASN A OD1 4464 N ND2 . ASN A 585 ? 0.3634 0.4010 0.3175 0.0708 0.0192 0.0178 581 ASN A ND2 4465 N N . VAL A 586 ? 0.5146 0.5165 0.4574 0.0714 0.0343 0.0237 582 VAL A N 4466 C CA . VAL A 586 ? 0.5655 0.5574 0.5029 0.0740 0.0402 0.0264 582 VAL A CA 4467 C C . VAL A 586 ? 0.5841 0.5732 0.5145 0.0804 0.0441 0.0295 582 VAL A C 4468 O O . VAL A 586 ? 0.5766 0.5670 0.5072 0.0802 0.0435 0.0297 582 VAL A O 4469 C CB . VAL A 586 ? 0.5602 0.5433 0.5012 0.0678 0.0425 0.0257 582 VAL A CB 4470 C CG1 . VAL A 586 ? 0.6177 0.5915 0.5545 0.0696 0.0484 0.0277 582 VAL A CG1 4471 C CG2 . VAL A 586 ? 0.6137 0.6006 0.5615 0.0620 0.0383 0.0227 582 VAL A CG2 4472 N N . GLY A 587 ? 0.6128 0.5983 0.5365 0.0863 0.0482 0.0321 583 GLY A N 4473 C CA . GLY A 587 ? 0.6198 0.6028 0.5359 0.0934 0.0520 0.0353 583 GLY A CA 4474 C C . GLY A 587 ? 0.6320 0.6258 0.5448 0.1000 0.0491 0.0355 583 GLY A C 4475 O O . GLY A 587 ? 0.6211 0.6135 0.5264 0.1074 0.0525 0.0385 583 GLY A O 4476 N N . ASP A 588 ? 0.6279 0.6324 0.5460 0.0978 0.0431 0.0323 584 ASP A N 4477 C CA . ASP A 588 ? 0.6393 0.6554 0.5551 0.1038 0.0399 0.0316 584 ASP A CA 4478 C C . ASP A 588 ? 0.6689 0.6837 0.5775 0.1109 0.0429 0.0338 584 ASP A C 4479 O O . ASP A 588 ? 0.6714 0.6790 0.5795 0.1095 0.0457 0.0345 584 ASP A O 4480 C CB . ASP A 588 ? 0.6338 0.6609 0.5571 0.0995 0.0333 0.0273 584 ASP A CB 4481 C CG . ASP A 588 ? 0.6080 0.6400 0.5375 0.0945 0.0296 0.0252 584 ASP A CG 4482 O OD1 . ASP A 588 ? 0.5922 0.6328 0.5279 0.0909 0.0246 0.0217 584 ASP A OD1 4483 O OD2 . ASP A 588 ? 0.5439 0.5711 0.4721 0.0941 0.0318 0.0269 584 ASP A OD2 4484 N N . ALA A 589 ? 0.6897 0.7123 0.5932 0.1188 0.0423 0.0346 585 ALA A N 4485 C CA . ALA A 589 ? 0.7175 0.7408 0.6139 0.1265 0.0447 0.0365 585 ALA A CA 4486 C C . ALA A 589 ? 0.7200 0.7494 0.6205 0.1242 0.0408 0.0333 585 ALA A C 4487 O O . ALA A 589 ? 0.7354 0.7593 0.6322 0.1264 0.0439 0.0349 585 ALA A O 4488 C CB . ALA A 589 ? 0.7268 0.7583 0.6165 0.1359 0.0446 0.0378 585 ALA A CB 4489 N N . HIS A 590 ? 0.7080 0.7476 0.6161 0.1194 0.0345 0.0290 586 HIS A N 4490 C CA . HIS A 590 ? 0.7116 0.7583 0.6239 0.1174 0.0304 0.0256 586 HIS A CA 4491 C C . HIS A 590 ? 0.6826 0.7233 0.6015 0.1088 0.0295 0.0239 586 HIS A C 4492 O O . HIS A 590 ? 0.6946 0.7421 0.6186 0.1057 0.0251 0.0203 586 HIS A O 4493 C CB . HIS A 590 ? 0.7255 0.7873 0.6424 0.1174 0.0241 0.0213 586 HIS A CB 4494 C CG . HIS A 590 ? 0.7754 0.8399 0.7021 0.1082 0.0198 0.0177 586 HIS A CG 4495 N ND1 . HIS A 590 ? 0.8217 0.8806 0.7513 0.1033 0.0207 0.0186 586 HIS A ND1 4496 C CD2 . HIS A 590 ? 0.8043 0.8766 0.7382 0.1033 0.0149 0.0133 586 HIS A CD2 4497 C CE1 . HIS A 590 ? 0.7883 0.8515 0.7262 0.0962 0.0166 0.0151 586 HIS A CE1 4498 N NE2 . HIS A 590 ? 0.7455 0.8165 0.6862 0.0959 0.0131 0.0119 586 HIS A NE2 4499 N N . TYR A 591 ? 0.6356 0.6639 0.5540 0.1055 0.0339 0.0263 587 TYR A N 4500 C CA . TYR A 591 ? 0.5805 0.6037 0.5059 0.0967 0.0328 0.0245 587 TYR A CA 4501 C C . TYR A 591 ? 0.5485 0.5714 0.4757 0.0949 0.0319 0.0231 587 TYR A C 4502 O O . TYR A 591 ? 0.5546 0.5703 0.4774 0.0975 0.0363 0.0255 587 TYR A O 4503 C CB . TYR A 591 ? 0.5805 0.5912 0.5044 0.0944 0.0381 0.0273 587 TYR A CB 4504 C CG . TYR A 591 ? 0.5422 0.5486 0.4734 0.0855 0.0368 0.0254 587 TYR A CG 4505 C CD1 . TYR A 591 ? 0.5012 0.5134 0.4387 0.0807 0.0323 0.0228 587 TYR A CD1 4506 C CD2 . TYR A 591 ? 0.5074 0.5039 0.4390 0.0823 0.0406 0.0263 587 TYR A CD2 4507 C CE1 . TYR A 591 ? 0.4693 0.4776 0.4128 0.0732 0.0313 0.0213 587 TYR A CE1 4508 C CE2 . TYR A 591 ? 0.4884 0.4817 0.4266 0.0746 0.0394 0.0244 587 TYR A CE2 4509 C CZ . TYR A 591 ? 0.4769 0.4760 0.4207 0.0703 0.0347 0.0220 587 TYR A CZ 4510 O OH . TYR A 591 ? 0.4497 0.4456 0.3993 0.0634 0.0338 0.0204 587 TYR A OH 4511 N N . ASP A 592 ? 0.4976 0.5282 0.4314 0.0906 0.0265 0.0192 588 ASP A N 4512 C CA . ASP A 592 ? 0.4539 0.4857 0.3898 0.0889 0.0249 0.0173 588 ASP A CA 4513 C C . ASP A 592 ? 0.4241 0.4554 0.3686 0.0801 0.0216 0.0144 588 ASP A C 4514 O O . ASP A 592 ? 0.4047 0.4438 0.3539 0.0776 0.0170 0.0110 588 ASP A O 4515 C CB . ASP A 592 ? 0.4419 0.4852 0.3764 0.0940 0.0214 0.0152 588 ASP A CB 4516 C CG . ASP A 592 ? 0.4365 0.4814 0.3725 0.0931 0.0198 0.0132 588 ASP A CG 4517 O OD1 . ASP A 592 ? 0.4577 0.4943 0.3933 0.0911 0.0226 0.0147 588 ASP A OD1 4518 O OD2 . ASP A 592 ? 0.4911 0.5461 0.4290 0.0943 0.0156 0.0100 588 ASP A OD2 4519 N N . PRO A 593 ? 0.4177 0.4398 0.3638 0.0755 0.0243 0.0157 589 PRO A N 4520 C CA . PRO A 593 ? 0.4092 0.4310 0.3629 0.0677 0.0214 0.0132 589 PRO A CA 4521 C C . PRO A 593 ? 0.4037 0.4250 0.3602 0.0649 0.0201 0.0115 589 PRO A C 4522 O O . PRO A 593 ? 0.3859 0.4038 0.3386 0.0680 0.0228 0.0128 589 PRO A O 4523 C CB . PRO A 593 ? 0.4147 0.4269 0.3682 0.0648 0.0252 0.0152 589 PRO A CB 4524 C CG . PRO A 593 ? 0.4391 0.4442 0.3857 0.0700 0.0310 0.0186 589 PRO A CG 4525 C CD . PRO A 593 ? 0.4301 0.4421 0.3715 0.0774 0.0302 0.0193 589 PRO A CD 4526 N N . LEU A 594 ? 0.4015 0.4256 0.3645 0.0592 0.0164 0.0086 590 LEU A N 4527 C CA . LEU A 594 ? 0.3823 0.4039 0.3482 0.0557 0.0158 0.0073 590 LEU A CA 4528 C C . LEU A 594 ? 0.3853 0.3971 0.3512 0.0528 0.0197 0.0091 590 LEU A C 4529 O O . LEU A 594 ? 0.3887 0.3960 0.3534 0.0530 0.0221 0.0098 590 LEU A O 4530 C CB . LEU A 594 ? 0.3492 0.3756 0.3217 0.0505 0.0111 0.0040 590 LEU A CB 4531 C CG . LEU A 594 ? 0.3677 0.3924 0.3433 0.0473 0.0101 0.0024 590 LEU A CG 4532 C CD1 . LEU A 594 ? 0.3446 0.3734 0.3175 0.0513 0.0093 0.0016 590 LEU A CD1 4533 C CD2 . LEU A 594 ? 0.3423 0.3701 0.3242 0.0418 0.0063 -0.0003 590 LEU A CD2 4534 N N . PHE A 595 ? 0.3648 0.3739 0.3325 0.0500 0.0203 0.0096 591 PHE A N 4535 C CA . PHE A 595 ? 0.3764 0.3770 0.3440 0.0476 0.0242 0.0110 591 PHE A CA 4536 C C . PHE A 595 ? 0.3890 0.3875 0.3539 0.0495 0.0263 0.0129 591 PHE A C 4537 O O . PHE A 595 ? 0.3844 0.3874 0.3512 0.0486 0.0235 0.0121 591 PHE A O 4538 C CB . PHE A 595 ? 0.3841 0.3834 0.3579 0.0411 0.0222 0.0090 591 PHE A CB 4539 C CG . PHE A 595 ? 0.3674 0.3692 0.3444 0.0388 0.0196 0.0069 591 PHE A CG 4540 C CD1 . PHE A 595 ? 0.3703 0.3678 0.3466 0.0386 0.0221 0.0072 591 PHE A CD1 4541 C CD2 . PHE A 595 ? 0.3676 0.3755 0.3484 0.0368 0.0150 0.0046 591 PHE A CD2 4542 C CE1 . PHE A 595 ? 0.3737 0.3733 0.3528 0.0367 0.0197 0.0053 591 PHE A CE1 4543 C CE2 . PHE A 595 ? 0.3490 0.3586 0.3326 0.0348 0.0129 0.0028 591 PHE A CE2 4544 C CZ . PHE A 595 ? 0.3601 0.3656 0.3427 0.0349 0.0151 0.0032 591 PHE A CZ 4545 N N . ARG A 596 ? 0.3949 0.3864 0.3552 0.0521 0.0315 0.0154 592 ARG A N 4546 C CA . ARG A 596 ? 0.4099 0.3978 0.3668 0.0542 0.0345 0.0174 592 ARG A CA 4547 C C . ARG A 596 ? 0.3880 0.3727 0.3492 0.0488 0.0344 0.0164 592 ARG A C 4548 O O . ARG A 596 ? 0.3663 0.3487 0.3318 0.0439 0.0339 0.0147 592 ARG A O 4549 C CB . ARG A 596 ? 0.4193 0.3993 0.3703 0.0582 0.0407 0.0203 592 ARG A CB 4550 C CG . ARG A 596 ? 0.4953 0.4681 0.4486 0.0541 0.0438 0.0198 592 ARG A CG 4551 C CD . ARG A 596 ? 0.6372 0.6008 0.5852 0.0571 0.0509 0.0225 592 ARG A CD 4552 N NE . ARG A 596 ? 0.7882 0.7455 0.7382 0.0534 0.0537 0.0223 592 ARG A NE 4553 C CZ . ARG A 596 ? 0.7984 0.7516 0.7530 0.0478 0.0550 0.0204 592 ARG A CZ 4554 N NH1 . ARG A 596 ? 0.7741 0.7225 0.7301 0.0448 0.0573 0.0198 592 ARG A NH1 4555 N NH2 . ARG A 596 ? 0.8133 0.7673 0.7709 0.0454 0.0541 0.0189 592 ARG A NH2 4556 N N . LEU A 597 ? 0.3765 0.3609 0.3359 0.0501 0.0351 0.0175 593 LEU A N 4557 C CA . LEU A 597 ? 0.3782 0.3588 0.3407 0.0458 0.0358 0.0168 593 LEU A CA 4558 C C . LEU A 597 ? 0.3876 0.3594 0.3497 0.0438 0.0405 0.0170 593 LEU A C 4559 O O . LEU A 597 ? 0.3769 0.3438 0.3343 0.0475 0.0450 0.0191 593 LEU A O 4560 C CB . LEU A 597 ? 0.3839 0.3646 0.3433 0.0486 0.0367 0.0184 593 LEU A CB 4561 C CG . LEU A 597 ? 0.3652 0.3428 0.3276 0.0443 0.0370 0.0175 593 LEU A CG 4562 C CD1 . LEU A 597 ? 0.4171 0.3996 0.3791 0.0458 0.0346 0.0179 593 LEU A CD1 4563 C CD2 . LEU A 597 ? 0.4458 0.4139 0.4054 0.0445 0.0428 0.0187 593 LEU A CD2 4564 N N . GLY A 598 ? 0.3599 0.3302 0.3272 0.0382 0.0397 0.0149 594 GLY A N 4565 C CA . GLY A 598 ? 0.3586 0.3219 0.3270 0.0354 0.0437 0.0142 594 GLY A CA 4566 C C . GLY A 598 ? 0.3474 0.3114 0.3185 0.0334 0.0429 0.0128 594 GLY A C 4567 O O . GLY A 598 ? 0.3630 0.3227 0.3365 0.0301 0.0454 0.0115 594 GLY A O 4568 N N . TYR A 599 ? 0.3420 0.3117 0.3130 0.0352 0.0395 0.0128 595 TYR A N 4569 C CA . TYR A 599 ? 0.3625 0.3331 0.3359 0.0335 0.0386 0.0115 595 TYR A CA 4570 C C . TYR A 599 ? 0.3741 0.3464 0.3537 0.0278 0.0357 0.0086 595 TYR A C 4571 O O . TYR A 599 ? 0.3471 0.3235 0.3294 0.0259 0.0320 0.0075 595 TYR A O 4572 C CB . TYR A 599 ? 0.3612 0.3384 0.3335 0.0365 0.0349 0.0116 595 TYR A CB 4573 C CG . TYR A 599 ? 0.3923 0.3710 0.3668 0.0350 0.0335 0.0102 595 TYR A CG 4574 C CD1 . TYR A 599 ? 0.4046 0.3877 0.3844 0.0311 0.0291 0.0077 595 TYR A CD1 4575 C CD2 . TYR A 599 ? 0.4107 0.3863 0.3820 0.0378 0.0368 0.0115 595 TYR A CD2 4576 C CE1 . TYR A 599 ? 0.4372 0.4216 0.4189 0.0299 0.0278 0.0065 595 TYR A CE1 4577 C CE2 . TYR A 599 ? 0.4270 0.4043 0.4005 0.0365 0.0354 0.0101 595 TYR A CE2 4578 C CZ . TYR A 599 ? 0.4404 0.4220 0.4191 0.0325 0.0309 0.0076 595 TYR A CZ 4579 O OH . TYR A 599 ? 0.5079 0.4910 0.4888 0.0312 0.0294 0.0062 595 TYR A OH 4580 N N . GLY A 600 ? 0.3547 0.3244 0.3368 0.0251 0.0374 0.0073 596 GLY A N 4581 C CA . GLY A 600 ? 0.3467 0.3196 0.3343 0.0206 0.0339 0.0046 596 GLY A CA 4582 C C . GLY A 600 ? 0.3585 0.3283 0.3478 0.0188 0.0366 0.0035 596 GLY A C 4583 O O . GLY A 600 ? 0.3580 0.3220 0.3461 0.0186 0.0415 0.0039 596 GLY A O 4584 N N . LEU A 601 ? 0.3370 0.3103 0.3286 0.0177 0.0337 0.0022 597 LEU A N 4585 C CA . LEU A 601 ? 0.3485 0.3199 0.3426 0.0154 0.0357 0.0008 597 LEU A CA 4586 C C . LEU A 601 ? 0.3567 0.3276 0.3553 0.0110 0.0358 -0.0018 597 LEU A C 4587 O O . LEU A 601 ? 0.3464 0.3198 0.3467 0.0095 0.0331 -0.0026 597 LEU A O 4588 C CB . LEU A 601 ? 0.3288 0.3043 0.3242 0.0156 0.0324 0.0001 597 LEU A CB 4589 C CG . LEU A 601 ? 0.3557 0.3330 0.3469 0.0200 0.0314 0.0020 597 LEU A CG 4590 C CD1 . LEU A 601 ? 0.3641 0.3453 0.3571 0.0197 0.0283 0.0008 597 LEU A CD1 4591 C CD2 . LEU A 601 ? 0.3989 0.3706 0.3856 0.0233 0.0371 0.0043 597 LEU A CD2 4592 N N . THR A 602 ? 0.3573 0.3257 0.3581 0.0088 0.0388 -0.0032 598 THR A N 4593 C CA . THR A 602 ? 0.3660 0.3351 0.3715 0.0047 0.0388 -0.0062 598 THR A CA 4594 C C . THR A 602 ? 0.3768 0.3489 0.3861 0.0025 0.0374 -0.0085 598 THR A C 4595 O O . THR A 602 ? 0.3811 0.3536 0.3893 0.0040 0.0375 -0.0076 598 THR A O 4596 C CB . THR A 602 ? 0.3917 0.3548 0.3969 0.0035 0.0446 -0.0066 598 THR A CB 4597 O OG1 . THR A 602 ? 0.3850 0.3442 0.3890 0.0044 0.0490 -0.0058 598 THR A OG1 4598 C CG2 . THR A 602 ? 0.3978 0.3574 0.3988 0.0061 0.0464 -0.0042 598 THR A CG2 4599 N N . THR A 603 ? 0.3825 0.3573 0.3962 -0.0009 0.0360 -0.0115 599 THR A N 4600 C CA . THR A 603 ? 0.3757 0.3534 0.3934 -0.0031 0.0354 -0.0141 599 THR A CA 4601 C C . THR A 603 ? 0.3993 0.3766 0.4207 -0.0065 0.0378 -0.0172 599 THR A C 4602 O O . THR A 603 ? 0.3992 0.3746 0.4201 -0.0070 0.0389 -0.0174 599 THR A O 4603 C CB . THR A 603 ? 0.3733 0.3570 0.3928 -0.0034 0.0297 -0.0150 599 THR A CB 4604 O OG1 . THR A 603 ? 0.3499 0.3357 0.3702 -0.0042 0.0272 -0.0156 599 THR A OG1 4605 C CG2 . THR A 603 ? 0.3342 0.3188 0.3506 -0.0004 0.0272 -0.0125 599 THR A CG2 4606 N N . ASN A 604 ? 0.4266 0.4057 0.4518 -0.0087 0.0387 -0.0198 600 ASN A N 4607 C CA . ASN A 604 ? 0.4708 0.4515 0.5007 -0.0123 0.0403 -0.0238 600 ASN A CA 4608 C C . ASN A 604 ? 0.4694 0.4573 0.5027 -0.0134 0.0353 -0.0265 600 ASN A C 4609 O O . ASN A 604 ? 0.4691 0.4602 0.5022 -0.0122 0.0321 -0.0258 600 ASN A O 4610 C CB . ASN A 604 ? 0.4761 0.4546 0.5084 -0.0141 0.0450 -0.0255 600 ASN A CB 4611 C CG . ASN A 604 ? 0.5683 0.5389 0.5971 -0.0128 0.0508 -0.0229 600 ASN A CG 4612 O OD1 . ASN A 604 ? 0.6263 0.5931 0.6522 -0.0118 0.0521 -0.0213 600 ASN A OD1 4613 N ND2 . ASN A 604 ? 0.6718 0.6398 0.7006 -0.0126 0.0544 -0.0224 600 ASN A ND2 4614 N N . ALA A 605 ? 0.4819 0.4724 0.5181 -0.0156 0.0349 -0.0295 601 ALA A N 4615 C CA . ALA A 605 ? 0.5122 0.5098 0.5513 -0.0162 0.0305 -0.0321 601 ALA A CA 4616 C C . ALA A 605 ? 0.5400 0.5415 0.5826 -0.0174 0.0304 -0.0346 601 ALA A C 4617 O O . ALA A 605 ? 0.5343 0.5337 0.5789 -0.0191 0.0346 -0.0360 601 ALA A O 4618 C CB . ALA A 605 ? 0.5006 0.5004 0.5421 -0.0181 0.0304 -0.0352 601 ALA A CB 4619 N N . THR A 606 ? 0.5635 0.5702 0.6064 -0.0161 0.0259 -0.0347 602 THR A N 4620 C CA . THR A 606 ? 0.5964 0.6091 0.6432 -0.0171 0.0248 -0.0379 602 THR A CA 4621 C C . THR A 606 ? 0.6093 0.6274 0.6600 -0.0190 0.0241 -0.0423 602 THR A C 4622 O O . THR A 606 ? 0.6475 0.6639 0.7002 -0.0214 0.0273 -0.0446 602 THR A O 4623 C CB . THR A 606 ? 0.6018 0.6180 0.6470 -0.0146 0.0201 -0.0363 602 THR A CB 4624 O OG1 . THR A 606 ? 0.5930 0.6049 0.6339 -0.0124 0.0193 -0.0321 602 THR A OG1 4625 C CG2 . THR A 606 ? 0.6325 0.6529 0.6805 -0.0150 0.0199 -0.0385 602 THR A CG2 # 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 HIS 1 -3 -3 HIS HIS A . n A 1 2 HIS 2 -2 -2 HIS HIS A . n A 1 3 ALA 3 -1 -1 ALA ALA A . n A 1 4 ALA 4 0 0 ALA ALA A . n A 1 5 ASP 5 1 1 ASP ASP A . n A 1 6 TYR 6 2 2 TYR TYR A . n A 1 7 VAL 7 3 3 VAL VAL A . n A 1 8 LEU 8 4 4 LEU LEU A . n A 1 9 TYR 9 5 5 TYR TYR A . n A 1 10 LYS 10 6 6 LYS LYS A . n A 1 11 ASP 11 7 7 ASP ASP A . n A 1 12 ALA 12 8 8 ALA ALA A . n A 1 13 THR 13 9 9 THR THR A . n A 1 14 LYS 14 10 10 LYS LYS A . n A 1 15 PRO 15 11 11 PRO PRO A . n A 1 16 VAL 16 12 12 VAL VAL A . n A 1 17 GLU 17 13 13 GLU GLU A . n A 1 18 ASP 18 14 14 ASP ASP A . n A 1 19 ARG 19 15 15 ARG ARG A . n A 1 20 VAL 20 16 16 VAL VAL A . n A 1 21 ALA 21 17 17 ALA ALA A . n A 1 22 ASP 22 18 18 ASP ASP A . n A 1 23 LEU 23 19 19 LEU LEU A . n A 1 24 LEU 24 20 20 LEU LEU A . n A 1 25 GLY 25 21 21 GLY GLY A . n A 1 26 ARG 26 22 22 ARG ARG A . n A 1 27 MET 27 23 23 MET MET A . n A 1 28 THR 28 24 24 THR THR A . n A 1 29 LEU 29 25 25 LEU LEU A . n A 1 30 ALA 30 26 26 ALA ALA A . n A 1 31 GLU 31 27 27 GLU GLU A . n A 1 32 LYS 32 28 28 LYS LYS A . n A 1 33 ILE 33 29 29 ILE ILE A . n A 1 34 GLY 34 30 30 GLY GLY A . n A 1 35 GLN 35 31 31 GLN GLN A . n A 1 36 MET 36 32 32 MET MET A . n A 1 37 THR 37 33 33 THR THR A . n A 1 38 GLN 38 34 34 GLN GLN A . n A 1 39 ILE 39 35 35 ILE ILE A . n A 1 40 GLU 40 36 36 GLU GLU A . n A 1 41 ARG 41 37 37 ARG ARG A . n A 1 42 LEU 42 38 38 LEU LEU A . n A 1 43 VAL 43 39 39 VAL VAL A . n A 1 44 ALA 44 40 40 ALA ALA A . n A 1 45 THR 45 41 41 THR THR A . n A 1 46 PRO 46 42 42 PRO PRO A . n A 1 47 ASP 47 43 43 ASP ASP A . n A 1 48 VAL 48 44 44 VAL VAL A . n A 1 49 LEU 49 45 45 LEU LEU A . n A 1 50 ARG 50 46 46 ARG ARG A . n A 1 51 ASP 51 47 47 ASP ASP A . n A 1 52 ASN 52 48 48 ASN ASN A . n A 1 53 PHE 53 49 49 PHE PHE A . n A 1 54 ILE 54 50 50 ILE ILE A . n A 1 55 GLY 55 51 51 GLY GLY A . n A 1 56 SER 56 52 52 SER SER A . n A 1 57 LEU 57 53 53 LEU LEU A . n A 1 58 LEU 58 54 54 LEU LEU A . n A 1 59 SER 59 55 55 SER SER A . n A 1 60 GLY 60 56 56 GLY GLY A . n A 1 61 GLY 61 57 57 GLY GLY A . n A 1 62 GLY 62 58 58 GLY GLY A . n A 1 63 SER 63 59 59 SER SER A . n A 1 64 VAL 64 60 60 VAL VAL A . n A 1 65 PRO 65 61 61 PRO PRO A . n A 1 66 ARG 66 62 62 ARG ARG A . n A 1 67 LYS 67 63 63 LYS LYS A . n A 1 68 GLY 68 64 64 GLY GLY A . n A 1 69 ALA 69 65 65 ALA ALA A . n A 1 70 THR 70 66 66 THR THR A . n A 1 71 ALA 71 67 67 ALA ALA A . n A 1 72 LYS 72 68 68 LYS LYS A . n A 1 73 GLU 73 69 69 GLU GLU A . n A 1 74 TRP 74 70 70 TRP TRP A . n A 1 75 GLN 75 71 71 GLN GLN A . n A 1 76 ASP 76 72 72 ASP ASP A . n A 1 77 MET 77 73 73 MET MET A . n A 1 78 VAL 78 74 74 VAL VAL A . n A 1 79 ASP 79 75 75 ASP ASP A . n A 1 80 GLY 80 76 76 GLY GLY A . n A 1 81 PHE 81 77 77 PHE PHE A . n A 1 82 GLN 82 78 78 GLN GLN A . n A 1 83 LYS 83 79 79 LYS LYS A . n A 1 84 ALA 84 80 80 ALA ALA A . n A 1 85 CYS 85 81 81 CYS CYS A . n A 1 86 MET 86 82 82 MET MET A . n A 1 87 SER 87 83 83 SER SER A . n A 1 88 THR 88 84 84 THR THR A . n A 1 89 ARG 89 85 85 ARG ARG A . n A 1 90 LEU 90 86 86 LEU LEU A . n A 1 91 GLY 91 87 87 GLY GLY A . n A 1 92 ILE 92 88 88 ILE ILE A . n A 1 93 PRO 93 89 89 PRO PRO A . n A 1 94 MET 94 90 90 MET MET A . n A 1 95 ILE 95 91 91 ILE ILE A . n A 1 96 TYR 96 92 92 TYR TYR A . n A 1 97 GLY 97 93 93 GLY GLY A . n A 1 98 ILE 98 94 94 ILE ILE A . n A 1 99 ASP 99 95 95 ASP ASP A . n A 1 100 ALA 100 96 96 ALA ALA A . n A 1 101 VAL 101 97 97 VAL VAL A . n A 1 102 HIS 102 98 98 HIS HIS A . n A 1 103 GLY 103 99 99 GLY GLY A . n A 1 104 GLN 104 100 100 GLN GLN A . n A 1 105 ASN 105 101 101 ASN ASN A . n A 1 106 ASN 106 102 102 ASN ASN A . n A 1 107 VAL 107 103 103 VAL VAL A . n A 1 108 TYR 108 104 104 TYR TYR A . n A 1 109 GLY 109 105 105 GLY GLY A . n A 1 110 ALA 110 106 106 ALA ALA A . n A 1 111 THR 111 107 107 THR THR A . n A 1 112 ILE 112 108 108 ILE ILE A . n A 1 113 PHE 113 109 109 PHE PHE A . n A 1 114 PRO 114 110 110 PRO PRO A . n A 1 115 HIS 115 111 111 HIS HIS A . n A 1 116 ASN 116 112 112 ASN ASN A . n A 1 117 VAL 117 113 113 VAL VAL A . n A 1 118 GLY 118 114 114 GLY GLY A . n A 1 119 LEU 119 115 115 LEU LEU A . n A 1 120 GLY 120 116 116 GLY GLY A . n A 1 121 ALA 121 117 117 ALA ALA A . n A 1 122 THR 122 118 118 THR THR A . n A 1 123 ARG 123 119 119 ARG ARG A . n A 1 124 ASP 124 120 120 ASP ASP A . n A 1 125 PRO 125 121 121 PRO PRO A . n A 1 126 TYR 126 122 122 TYR TYR A . n A 1 127 LEU 127 123 123 LEU LEU A . n A 1 128 VAL 128 124 124 VAL VAL A . n A 1 129 LYS 129 125 125 LYS LYS A . n A 1 130 ARG 130 126 126 ARG ARG A . n A 1 131 ILE 131 127 127 ILE ILE A . n A 1 132 GLY 132 128 128 GLY GLY A . n A 1 133 GLU 133 129 129 GLU GLU A . n A 1 134 ALA 134 130 130 ALA ALA A . n A 1 135 THR 135 131 131 THR THR A . n A 1 136 ALA 136 132 132 ALA ALA A . n A 1 137 LEU 137 133 133 LEU LEU A . n A 1 138 GLU 138 134 134 GLU GLU A . n A 1 139 VAL 139 135 135 VAL VAL A . n A 1 140 ARG 140 136 136 ARG ARG A . n A 1 141 ALA 141 137 137 ALA ALA A . n A 1 142 THR 142 138 138 THR THR A . n A 1 143 GLY 143 139 139 GLY GLY A . n A 1 144 ILE 144 140 140 ILE ILE A . n A 1 145 GLN 145 141 141 GLN GLN A . n A 1 146 TYR 146 142 142 TYR TYR A . n A 1 147 ALA 147 143 143 ALA ALA A . n A 1 148 PHE 148 144 144 PHE PHE A . n A 1 149 ALA 149 145 145 ALA ALA A . n A 1 150 PRO 150 146 146 PRO PRO A . n A 1 151 CYS 151 147 147 CYS CYS A . n A 1 152 ILE 152 148 148 ILE ILE A . n A 1 153 ALA 153 149 149 ALA ALA A . n A 1 154 VAL 154 150 150 VAL VAL A . n A 1 155 CYS 155 151 151 CYS CYS A . n A 1 156 ARG 156 152 152 ARG ARG A . n A 1 157 ASP 157 153 153 ASP ASP A . n A 1 158 PRO 158 154 154 PRO PRO A . n A 1 159 ARG 159 155 155 ARG ARG A . n A 1 160 TRP 160 156 156 TRP TRP A . n A 1 161 GLY 161 157 157 GLY GLY A . n A 1 162 ARG 162 158 158 ARG ARG A . n A 1 163 CYS 163 159 159 CYS CYS A . n A 1 164 TYR 164 160 160 TYR TYR A . n A 1 165 GLU 165 161 161 GLU GLU A . n A 1 166 SER 166 162 162 SER SER A . n A 1 167 TYR 167 163 163 TYR TYR A . n A 1 168 SER 168 164 164 SER SER A . n A 1 169 GLU 169 165 165 GLU GLU A . n A 1 170 ASP 170 166 166 ASP ASP A . n A 1 171 ARG 171 167 167 ARG ARG A . n A 1 172 ARG 172 168 168 ARG ARG A . n A 1 173 ILE 173 169 169 ILE ILE A . n A 1 174 VAL 174 170 170 VAL VAL A . n A 1 175 GLN 175 171 171 GLN GLN A . n A 1 176 SER 176 172 172 SER SER A . n A 1 177 MET 177 173 173 MET MET A . n A 1 178 THR 178 174 174 THR THR A . n A 1 179 GLU 179 175 175 GLU GLU A . n A 1 180 LEU 180 176 176 LEU LEU A . n A 1 181 ILE 181 177 177 ILE ILE A . n A 1 182 PRO 182 178 178 PRO PRO A . n A 1 183 GLY 183 179 179 GLY GLY A . n A 1 184 LEU 184 180 180 LEU LEU A . n A 1 185 GLN 185 181 181 GLN GLN A . n A 1 186 GLY 186 182 182 GLY GLY A . n A 1 187 ASP 187 183 183 ASP ASP A . n A 1 188 VAL 188 184 184 VAL VAL A . n A 1 189 PRO 189 185 185 PRO PRO A . n A 1 190 LYS 190 186 186 LYS LYS A . n A 1 191 ASP 191 187 187 ASP ASP A . n A 1 192 PHE 192 188 188 PHE PHE A . n A 1 193 THR 193 189 189 THR THR A . n A 1 194 SER 194 190 190 SER SER A . n A 1 195 GLY 195 191 191 GLY GLY A . n A 1 196 MET 196 192 192 MET MET A . n A 1 197 PRO 197 193 193 PRO PRO A . n A 1 198 PHE 198 194 194 PHE PHE A . n A 1 199 VAL 199 195 195 VAL VAL A . n A 1 200 ALA 200 196 196 ALA ALA A . n A 1 201 GLY 201 197 197 GLY GLY A . n A 1 202 LYS 202 198 198 LYS LYS A . n A 1 203 ASN 203 199 199 ASN ASN A . n A 1 204 LYS 204 200 200 LYS LYS A . n A 1 205 VAL 205 201 201 VAL VAL A . n A 1 206 ALA 206 202 202 ALA ALA A . n A 1 207 ALA 207 203 203 ALA ALA A . n A 1 208 CYS 208 204 204 CYS CYS A . n A 1 209 ALA 209 205 205 ALA ALA A . n A 1 210 LYS 210 206 206 LYS LYS A . n A 1 211 HIS 211 207 207 HIS HIS A . n A 1 212 PHE 212 208 208 PHE PHE A . n A 1 213 VAL 213 209 209 VAL VAL A . n A 1 214 GLY 214 210 210 GLY GLY A . n A 1 215 ASP 215 211 211 ASP ASP A . n A 1 216 GLY 216 212 212 GLY GLY A . n A 1 217 GLY 217 213 213 GLY GLY A . n A 1 218 THR 218 214 214 THR THR A . n A 1 219 VAL 219 215 215 VAL VAL A . n A 1 220 ASP 220 216 216 ASP ASP A . n A 1 221 GLY 221 217 217 GLY GLY A . n A 1 222 ILE 222 218 218 ILE ILE A . n A 1 223 ASN 223 219 219 ASN ASN A . n A 1 224 GLU 224 220 220 GLU GLU A . n A 1 225 ASN 225 221 221 ASN ASN A . n A 1 226 ASN 226 222 222 ASN ASN A . n A 1 227 THR 227 223 223 THR THR A . n A 1 228 ILE 228 224 224 ILE ILE A . n A 1 229 ILE 229 225 225 ILE ILE A . n A 1 230 ASN 230 226 226 ASN ASN A . n A 1 231 ARG 231 227 227 ARG ARG A . n A 1 232 GLU 232 228 228 GLU GLU A . n A 1 233 GLY 233 229 229 GLY GLY A . n A 1 234 LEU 234 230 230 LEU LEU A . n A 1 235 MET 235 231 231 MET MET A . n A 1 236 ASN 236 232 232 ASN ASN A . n A 1 237 ILE 237 233 233 ILE ILE A . n A 1 238 HIS 238 234 234 HIS HIS A . n A 1 239 MET 239 235 235 MET MET A . n A 1 240 PRO 240 236 236 PRO PRO A . n A 1 241 ALA 241 237 237 ALA ALA A . n A 1 242 TYR 242 238 238 TYR TYR A . n A 1 243 LYS 243 239 239 LYS LYS A . n A 1 244 ASN 244 240 240 ASN ASN A . n A 1 245 ALA 245 241 241 ALA ALA A . n A 1 246 MET 246 242 242 MET MET A . n A 1 247 ASP 247 243 243 ASP ASP A . n A 1 248 LYS 248 244 244 LYS LYS A . n A 1 249 GLY 249 245 245 GLY GLY A . n A 1 250 VAL 250 246 246 VAL VAL A . n A 1 251 SER 251 247 247 SER SER A . n A 1 252 THR 252 248 248 THR THR A . n A 1 253 VAL 253 249 249 VAL VAL A . n A 1 254 MET 254 250 250 MET MET A . n A 1 255 ILE 255 251 251 ILE ILE A . n A 1 256 SER 256 252 252 SER SER A . n A 1 257 TYR 257 253 253 TYR TYR A . n A 1 258 SER 258 254 254 SER SER A . n A 1 259 SER 259 255 255 SER SER A . n A 1 260 TRP 260 256 256 TRP TRP A . n A 1 261 ASN 261 257 257 ASN ASN A . n A 1 262 GLY 262 258 258 GLY GLY A . n A 1 263 VAL 263 259 259 VAL VAL A . n A 1 264 LYS 264 260 260 LYS LYS A . n A 1 265 MET 265 261 261 MET MET A . n A 1 266 HIS 266 262 262 HIS HIS A . n A 1 267 ALA 267 263 263 ALA ALA A . n A 1 268 ASN 268 264 264 ASN ASN A . n A 1 269 GLN 269 265 265 GLN GLN A . n A 1 270 ASP 270 266 266 ASP ASP A . n A 1 271 LEU 271 267 267 LEU LEU A . n A 1 272 VAL 272 268 268 VAL VAL A . n A 1 273 THR 273 269 269 THR THR A . n A 1 274 GLY 274 270 270 GLY GLY A . n A 1 275 TYR 275 271 271 TYR TYR A . n A 1 276 LEU 276 272 272 LEU LEU A . n A 1 277 LYS 277 273 273 LYS LYS A . n A 1 278 ASP 278 274 274 ASP ASP A . n A 1 279 THR 279 275 275 THR THR A . n A 1 280 LEU 280 276 276 LEU LEU A . n A 1 281 LYS 281 277 277 LYS LYS A . n A 1 282 PHE 282 278 278 PHE PHE A . n A 1 283 LYS 283 279 279 LYS LYS A . n A 1 284 GLY 284 280 280 GLY GLY A . n A 1 285 PHE 285 281 281 PHE PHE A . n A 1 286 VAL 286 282 282 VAL VAL A . n A 1 287 ILE 287 283 283 ILE ILE A . n A 1 288 SER 288 284 284 SER SER A . n A 1 289 ASP 289 285 285 ASP ASP A . n A 1 290 TRP 290 286 286 TRP TRP A . n A 1 291 GLU 291 287 287 GLU GLU A . n A 1 292 GLY 292 288 288 GLY GLY A . n A 1 293 ILE 293 289 289 ILE ILE A . n A 1 294 ASP 294 290 290 ASP ASP A . n A 1 295 ARG 295 291 291 ARG ARG A . n A 1 296 ILE 296 292 292 ILE ILE A . n A 1 297 THR 297 293 293 THR THR A . n A 1 298 THR 298 294 294 THR THR A . n A 1 299 PRO 299 295 295 PRO PRO A . n A 1 300 ALA 300 296 296 ALA ALA A . n A 1 301 GLY 301 297 297 GLY GLY A . n A 1 302 SER 302 298 298 SER SER A . n A 1 303 ASP 303 299 299 ASP ASP A . n A 1 304 TYR 304 300 300 TYR TYR A . n A 1 305 SER 305 301 301 SER SER A . n A 1 306 TYR 306 302 302 TYR TYR A . n A 1 307 SER 307 303 303 SER SER A . n A 1 308 VAL 308 304 304 VAL VAL A . n A 1 309 LYS 309 305 305 LYS LYS A . n A 1 310 ALA 310 306 306 ALA ALA A . n A 1 311 SER 311 307 307 SER SER A . n A 1 312 ILE 312 308 308 ILE ILE A . n A 1 313 LEU 313 309 309 LEU LEU A . n A 1 314 ALA 314 310 310 ALA ALA A . n A 1 315 GLY 315 311 311 GLY GLY A . n A 1 316 LEU 316 312 312 LEU LEU A . n A 1 317 ASP 317 313 313 ASP ASP A . n A 1 318 MET 318 314 314 MET MET A . n A 1 319 ILE 319 315 315 ILE ILE A . n A 1 320 MET 320 316 316 MET MET A . n A 1 321 VAL 321 317 317 VAL VAL A . n A 1 322 PRO 322 318 318 PRO PRO A . n A 1 323 ASN 323 319 319 ASN ASN A . n A 1 324 LYS 324 320 320 LYS LYS A . n A 1 325 TYR 325 321 321 TYR TYR A . n A 1 326 GLN 326 322 322 GLN GLN A . n A 1 327 GLN 327 323 323 GLN GLN A . n A 1 328 PHE 328 324 324 PHE PHE A . n A 1 329 ILE 329 325 325 ILE ILE A . n A 1 330 SER 330 326 326 SER SER A . n A 1 331 ILE 331 327 327 ILE ILE A . n A 1 332 LEU 332 328 328 LEU LEU A . n A 1 333 THR 333 329 329 THR THR A . n A 1 334 GLY 334 330 330 GLY GLY A . n A 1 335 HIS 335 331 331 HIS HIS A . n A 1 336 VAL 336 332 332 VAL VAL A . n A 1 337 ASN 337 333 333 ASN ASN A . n A 1 338 GLY 338 334 334 GLY GLY A . n A 1 339 GLY 339 335 335 GLY GLY A . n A 1 340 VAL 340 336 336 VAL VAL A . n A 1 341 ILE 341 337 337 ILE ILE A . n A 1 342 PRO 342 338 338 PRO PRO A . n A 1 343 MET 343 339 339 MET MET A . n A 1 344 SER 344 340 340 SER SER A . n A 1 345 ARG 345 341 341 ARG ARG A . n A 1 346 ILE 346 342 342 ILE ILE A . n A 1 347 ASP 347 343 343 ASP ASP A . n A 1 348 ASP 348 344 344 ASP ASP A . n A 1 349 ALA 349 345 345 ALA ALA A . n A 1 350 VAL 350 346 346 VAL VAL A . n A 1 351 THR 351 347 347 THR THR A . n A 1 352 ARG 352 348 348 ARG ARG A . n A 1 353 ILE 353 349 349 ILE ILE A . n A 1 354 LEU 354 350 350 LEU LEU A . n A 1 355 ARG 355 351 351 ARG ARG A . n A 1 356 VAL 356 352 352 VAL VAL A . n A 1 357 LYS 357 353 353 LYS LYS A . n A 1 358 PHE 358 354 354 PHE PHE A . n A 1 359 THR 359 355 355 THR THR A . n A 1 360 MET 360 356 356 MET MET A . n A 1 361 GLY 361 357 357 GLY GLY A . n A 1 362 LEU 362 358 358 LEU LEU A . n A 1 363 PHE 363 359 359 PHE PHE A . n A 1 364 GLU 364 360 360 GLU GLU A . n A 1 365 ASN 365 361 361 ASN ASN A . n A 1 366 PRO 366 362 362 PRO PRO A . n A 1 367 TYR 367 363 363 TYR TYR A . n A 1 368 ALA 368 364 364 ALA ALA A . n A 1 369 ASP 369 365 365 ASP ASP A . n A 1 370 PRO 370 366 366 PRO PRO A . n A 1 371 ALA 371 367 367 ALA ALA A . n A 1 372 MET 372 368 368 MET MET A . n A 1 373 ALA 373 369 369 ALA ALA A . n A 1 374 GLU 374 370 370 GLU GLU A . n A 1 375 GLN 375 371 371 GLN GLN A . n A 1 376 LEU 376 372 372 LEU LEU A . n A 1 377 GLY 377 373 373 GLY GLY A . n A 1 378 LYS 378 374 374 LYS LYS A . n A 1 379 GLN 379 375 375 GLN GLN A . n A 1 380 GLU 380 376 376 GLU GLU A . n A 1 381 HIS 381 377 377 HIS HIS A . n A 1 382 ARG 382 378 378 ARG ARG A . n A 1 383 ASP 383 379 379 ASP ASP A . n A 1 384 LEU 384 380 380 LEU LEU A . n A 1 385 ALA 385 381 381 ALA ALA A . n A 1 386 ARG 386 382 382 ARG ARG A . n A 1 387 GLU 387 383 383 GLU GLU A . n A 1 388 ALA 388 384 384 ALA ALA A . n A 1 389 ALA 389 385 385 ALA ALA A . n A 1 390 ARG 390 386 386 ARG ARG A . n A 1 391 LYS 391 387 387 LYS LYS A . n A 1 392 SER 392 388 388 SER SER A . n A 1 393 LEU 393 389 389 LEU LEU A . n A 1 394 VAL 394 390 390 VAL VAL A . n A 1 395 LEU 395 391 391 LEU LEU A . n A 1 396 LEU 396 392 392 LEU LEU A . n A 1 397 LYS 397 393 393 LYS LYS A . n A 1 398 ASN 398 394 394 ASN ASN A . n A 1 399 GLY 399 395 395 GLY GLY A . n A 1 400 LYS 400 396 396 LYS LYS A . n A 1 401 THR 401 397 397 THR THR A . n A 1 402 SER 402 398 398 SER SER A . n A 1 403 THR 403 399 399 THR THR A . n A 1 404 ASP 404 400 400 ASP ASP A . n A 1 405 ALA 405 401 401 ALA ALA A . n A 1 406 PRO 406 402 402 PRO PRO A . n A 1 407 LEU 407 403 403 LEU LEU A . n A 1 408 LEU 408 404 404 LEU LEU A . n A 1 409 PRO 409 405 405 PRO PRO A . n A 1 410 LEU 410 406 406 LEU LEU A . n A 1 411 PRO 411 407 407 PRO PRO A . n A 1 412 LYS 412 408 408 LYS LYS A . n A 1 413 LYS 413 409 409 LYS LYS A . n A 1 414 ALA 414 410 410 ALA ALA A . n A 1 415 PRO 415 411 411 PRO PRO A . n A 1 416 LYS 416 412 412 LYS LYS A . n A 1 417 ILE 417 413 413 ILE ILE A . n A 1 418 LEU 418 414 414 LEU LEU A . n A 1 419 VAL 419 415 415 VAL VAL A . n A 1 420 ALA 420 416 416 ALA ALA A . n A 1 421 GLY 421 417 417 GLY GLY A . n A 1 422 SER 422 418 418 SER SER A . n A 1 423 HIS 423 419 419 HIS HIS A . n A 1 424 ALA 424 420 420 ALA ALA A . n A 1 425 ASP 425 421 421 ASP ASP A . n A 1 426 ASN 426 422 422 ASN ASN A . n A 1 427 LEU 427 423 423 LEU LEU A . n A 1 428 GLY 428 424 424 GLY GLY A . n A 1 429 TYR 429 425 425 TYR TYR A . n A 1 430 GLN 430 426 426 GLN GLN A . n A 1 431 CYS 431 427 427 CYS CYS A . n A 1 432 GLY 432 428 428 GLY GLY A . n A 1 433 GLY 433 429 429 GLY GLY A . n A 1 434 TRP 434 430 430 TRP TRP A . n A 1 435 THR 435 431 431 THR THR A . n A 1 436 ILE 436 432 432 ILE ILE A . n A 1 437 GLU 437 433 433 GLU GLU A . n A 1 438 ALA 438 434 434 ALA ALA A . n A 1 439 GLN 439 435 435 GLN GLN A . n A 1 440 GLY 440 436 436 GLY GLY A . n A 1 441 ASP 441 437 437 ASP ASP A . n A 1 442 THR 442 438 438 THR THR A . n A 1 443 GLY 443 439 439 GLY GLY A . n A 1 444 ARG 444 440 440 ARG ARG A . n A 1 445 THR 445 441 441 THR THR A . n A 1 446 THR 446 442 442 THR THR A . n A 1 447 VAL 447 443 443 VAL VAL A . n A 1 448 GLY 448 444 444 GLY GLY A . n A 1 449 THR 449 445 445 THR THR A . n A 1 450 THR 450 446 446 THR THR A . n A 1 451 ILE 451 447 447 ILE ILE A . n A 1 452 LEU 452 448 448 LEU LEU A . n A 1 453 GLU 453 449 449 GLU GLU A . n A 1 454 ALA 454 450 450 ALA ALA A . n A 1 455 VAL 455 451 451 VAL VAL A . n A 1 456 LYS 456 452 452 LYS LYS A . n A 1 457 ALA 457 453 453 ALA ALA A . n A 1 458 ALA 458 454 454 ALA ALA A . n A 1 459 VAL 459 455 455 VAL VAL A . n A 1 460 ASP 460 456 456 ASP ASP A . n A 1 461 PRO 461 457 457 PRO PRO A . n A 1 462 SER 462 458 458 SER SER A . n A 1 463 THR 463 459 459 THR THR A . n A 1 464 VAL 464 460 460 VAL VAL A . n A 1 465 VAL 465 461 461 VAL VAL A . n A 1 466 VAL 466 462 462 VAL VAL A . n A 1 467 PHE 467 463 463 PHE PHE A . n A 1 468 ALA 468 464 464 ALA ALA A . n A 1 469 GLU 469 465 465 GLU GLU A . n A 1 470 ASN 470 466 466 ASN ASN A . n A 1 471 PRO 471 467 467 PRO PRO A . n A 1 472 ASP 472 468 468 ASP ASP A . n A 1 473 ALA 473 469 469 ALA ALA A . n A 1 474 GLU 474 470 470 GLU GLU A . n A 1 475 PHE 475 471 471 PHE PHE A . n A 1 476 VAL 476 472 472 VAL VAL A . n A 1 477 LYS 477 473 473 LYS LYS A . n A 1 478 SER 478 474 474 SER SER A . n A 1 479 GLY 479 475 475 GLY GLY A . n A 1 480 GLY 480 476 476 GLY GLY A . n A 1 481 PHE 481 477 477 PHE PHE A . n A 1 482 SER 482 478 478 SER SER A . n A 1 483 TYR 483 479 479 TYR TYR A . n A 1 484 ALA 484 480 480 ALA ALA A . n A 1 485 ILE 485 481 481 ILE ILE A . n A 1 486 VAL 486 482 482 VAL VAL A . n A 1 487 ALA 487 483 483 ALA ALA A . n A 1 488 VAL 488 484 484 VAL VAL A . n A 1 489 GLY 489 485 485 GLY GLY A . n A 1 490 GLU 490 486 486 GLU GLU A . n A 1 491 HIS 491 487 487 HIS HIS A . n A 1 492 PRO 492 488 488 PRO PRO A . n A 1 493 TYR 493 489 489 TYR TYR A . n A 1 494 THR 494 490 490 THR THR A . n A 1 495 GLU 495 491 491 GLU GLU A . n A 1 496 THR 496 492 492 THR THR A . n A 1 497 LYS 497 493 493 LYS LYS A . n A 1 498 GLY 498 494 494 GLY GLY A . n A 1 499 ASP 499 495 495 ASP ASP A . n A 1 500 ASN 500 496 496 ASN ASN A . n A 1 501 LEU 501 497 497 LEU LEU A . n A 1 502 ASN 502 498 498 ASN ASN A . n A 1 503 LEU 503 499 499 LEU LEU A . n A 1 504 THR 504 500 500 THR THR A . n A 1 505 ILE 505 501 501 ILE ILE A . n A 1 506 PRO 506 502 502 PRO PRO A . n A 1 507 GLU 507 503 503 GLU GLU A . n A 1 508 PRO 508 504 504 PRO PRO A . n A 1 509 GLY 509 505 505 GLY GLY A . n A 1 510 LEU 510 506 506 LEU LEU A . n A 1 511 SER 511 507 507 SER SER A . n A 1 512 THR 512 508 508 THR THR A . n A 1 513 VAL 513 509 509 VAL VAL A . n A 1 514 GLN 514 510 510 GLN GLN A . n A 1 515 ALA 515 511 511 ALA ALA A . n A 1 516 VAL 516 512 512 VAL VAL A . n A 1 517 CYS 517 513 513 CYS CYS A . n A 1 518 GLY 518 514 514 GLY GLY A . n A 1 519 GLY 519 515 515 GLY GLY A . n A 1 520 VAL 520 516 516 VAL VAL A . n A 1 521 ARG 521 517 517 ARG ARG A . n A 1 522 CYS 522 518 518 CYS CYS A . n A 1 523 ALA 523 519 519 ALA ALA A . n A 1 524 THR 524 520 520 THR THR A . n A 1 525 VAL 525 521 521 VAL VAL A . n A 1 526 LEU 526 522 522 LEU LEU A . n A 1 527 ILE 527 523 523 ILE ILE A . n A 1 528 SER 528 524 524 SER SER A . n A 1 529 GLY 529 525 525 GLY GLY A . n A 1 530 ARG 530 526 526 ARG ARG A . n A 1 531 PRO 531 527 527 PRO PRO A . n A 1 532 VAL 532 528 528 VAL VAL A . n A 1 533 VAL 533 529 529 VAL VAL A . n A 1 534 VAL 534 530 530 VAL VAL A . n A 1 535 GLN 535 531 531 GLN GLN A . n A 1 536 PRO 536 532 532 PRO PRO A . n A 1 537 LEU 537 533 533 LEU LEU A . n A 1 538 LEU 538 534 534 LEU LEU A . n A 1 539 ALA 539 535 535 ALA ALA A . n A 1 540 ALA 540 536 536 ALA ALA A . n A 1 541 SER 541 537 537 SER SER A . n A 1 542 ASP 542 538 538 ASP ASP A . n A 1 543 ALA 543 539 539 ALA ALA A . n A 1 544 LEU 544 540 540 LEU LEU A . n A 1 545 VAL 545 541 541 VAL VAL A . n A 1 546 ALA 546 542 542 ALA ALA A . n A 1 547 ALA 547 543 543 ALA ALA A . n A 1 548 TRP 548 544 544 TRP TRP A . n A 1 549 LEU 549 545 545 LEU LEU A . n A 1 550 PRO 550 546 546 PRO PRO A . n A 1 551 GLY 551 547 547 GLY GLY A . n A 1 552 SER 552 548 548 SER SER A . n A 1 553 GLU 553 549 549 GLU GLU A . n A 1 554 GLY 554 550 550 GLY GLY A . n A 1 555 GLN 555 551 551 GLN GLN A . n A 1 556 GLY 556 552 552 GLY GLY A . n A 1 557 VAL 557 553 553 VAL VAL A . n A 1 558 THR 558 554 554 THR THR A . n A 1 559 ASP 559 555 555 ASP ASP A . n A 1 560 ALA 560 556 556 ALA ALA A . n A 1 561 LEU 561 557 557 LEU LEU A . n A 1 562 PHE 562 558 558 PHE PHE A . n A 1 563 GLY 563 559 559 GLY GLY A . n A 1 564 ASP 564 560 560 ASP ASP A . n A 1 565 PHE 565 561 561 PHE PHE A . n A 1 566 GLY 566 562 562 GLY GLY A . n A 1 567 PHE 567 563 563 PHE PHE A . n A 1 568 THR 568 564 564 THR THR A . n A 1 569 GLY 569 565 565 GLY GLY A . n A 1 570 ARG 570 566 566 ARG ARG A . n A 1 571 LEU 571 567 567 LEU LEU A . n A 1 572 PRO 572 568 568 PRO PRO A . n A 1 573 ARG 573 569 569 ARG ARG A . n A 1 574 THR 574 570 570 THR THR A . n A 1 575 TRP 575 571 571 TRP TRP A . n A 1 576 PHE 576 572 572 PHE PHE A . n A 1 577 LYS 577 573 573 LYS LYS A . n A 1 578 SER 578 574 574 SER SER A . n A 1 579 VAL 579 575 575 VAL VAL A . n A 1 580 ASP 580 576 576 ASP ASP A . n A 1 581 GLN 581 577 577 GLN GLN A . n A 1 582 LEU 582 578 578 LEU LEU A . n A 1 583 PRO 583 579 579 PRO PRO A . n A 1 584 MET 584 580 580 MET MET A . n A 1 585 ASN 585 581 581 ASN ASN A . n A 1 586 VAL 586 582 582 VAL VAL A . n A 1 587 GLY 587 583 583 GLY GLY A . n A 1 588 ASP 588 584 584 ASP ASP A . n A 1 589 ALA 589 585 585 ALA ALA A . n A 1 590 HIS 590 586 586 HIS HIS A . n A 1 591 TYR 591 587 587 TYR TYR A . n A 1 592 ASP 592 588 588 ASP ASP A . n A 1 593 PRO 593 589 589 PRO PRO A . n A 1 594 LEU 594 590 590 LEU LEU A . n A 1 595 PHE 595 591 591 PHE PHE A . n A 1 596 ARG 596 592 592 ARG ARG A . n A 1 597 LEU 597 593 593 LEU LEU A . n A 1 598 GLY 598 594 594 GLY GLY A . n A 1 599 TYR 599 595 595 TYR TYR A . n A 1 600 GLY 600 596 596 GLY GLY A . n A 1 601 LEU 601 597 597 LEU LEU A . n A 1 602 THR 602 598 598 THR THR A . n A 1 603 THR 603 599 599 THR THR A . n A 1 604 ASN 604 600 600 ASN ASN A . n A 1 605 ALA 605 601 601 ALA ALA A . n A 1 606 THR 606 602 602 THR THR A . n A 1 607 LYS 607 603 ? ? ? A . n A 1 608 LYS 608 604 ? ? ? A . n A 1 609 TYR 609 605 ? ? ? A . n # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 502 A ASN 498 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 225 A ASN 221 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 604 A ASN 600 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V # _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 # _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 2015-03-25 # _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 ? # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 24.5522 16.4096 29.5882 0.0137 0.0366 0.0422 0.0026 0.0112 0.0148 0.3740 0.0827 0.4296 -0.1257 -0.1877 0.0957 -0.0663 0.0026 -0.0536 0.0277 0.0154 0.0230 0.0243 0.0712 0.0510 'X-RAY DIFFRACTION' 2 ? refined 10.5290 20.6487 15.7280 0.0098 0.1098 0.0526 -0.0004 -0.0118 -0.0348 0.8516 1.0398 1.1085 -0.7385 -0.7119 0.4976 0.0330 0.2419 -0.1141 -0.0172 -0.1142 0.0665 -0.0485 -0.1446 0.0812 'X-RAY DIFFRACTION' 3 ? refined 2.4701 31.9782 51.5091 0.0293 0.0373 0.0454 0.0036 -0.0019 -0.0066 0.3058 0.1636 0.3734 -0.2102 -0.2318 0.1333 -0.0412 -0.0319 0.0125 0.0215 0.0075 0.0060 0.0235 0.0369 0.0338 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 A -3 ? ? A 357 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 358 ? ? A 373 ? ? ? ? 'X-RAY DIFFRACTION' 3 3 A 374 ? ? A 602 ? ? ? ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal ADSC 'data collection' Quantum ? 1 MOLREP phasing . ? 2 REFMAC refinement 5.5.0109 ? 3 HKL-2000 'data reduction' . ? 4 HKL-2000 'data scaling' . ? 5 # _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details ;THE AUTHORS STATE THERE IS AN ERROR IN THE CDNA SEQUENCING OF AF102868 (GENBANK ACCESSION NUMBER). RESIDUE 320 (SEQUENCE DATABASE RESIDUE 345) IS LYS AND IS NOT ASN. ; _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.entry_id 3WLT # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O A HOH 1397 ? ? O A HOH 1548 ? ? 1.66 2 1 O4 A MGL 720 ? ? O A HOH 806 ? ? 1.66 3 1 O5 A MGL 720 ? ? O A HOH 805 ? ? 1.88 4 1 ND2 A ASN 466 ? A OG1 A THR 508 ? ? 1.95 5 1 O A HOH 899 ? ? O A HOH 1191 ? ? 2.06 6 1 O A HOH 954 ? ? O A HOH 1524 ? ? 2.10 7 1 OD1 A ASN 581 ? ? O A HOH 1548 ? ? 2.12 8 1 NZ A LYS 374 ? A O A HOH 1089 ? ? 2.14 9 1 CG2 A THR 490 ? ? O A HOH 1027 ? ? 2.17 10 1 NZ A LYS 63 ? ? O A HOH 1026 ? ? 2.18 11 1 O A HOH 1170 ? ? O A HOH 1554 ? ? 2.18 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 NZ _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 LYS _pdbx_validate_symm_contact.auth_seq_id_1 374 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 B _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O _pdbx_validate_symm_contact.auth_asym_id_2 A _pdbx_validate_symm_contact.auth_comp_id_2 HOH _pdbx_validate_symm_contact.auth_seq_id_2 1161 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 6_455 _pdbx_validate_symm_contact.dist 1.69 # loop_ _pdbx_validate_rmsd_bond.id _pdbx_validate_rmsd_bond.PDB_model_num _pdbx_validate_rmsd_bond.auth_atom_id_1 _pdbx_validate_rmsd_bond.auth_asym_id_1 _pdbx_validate_rmsd_bond.auth_comp_id_1 _pdbx_validate_rmsd_bond.auth_seq_id_1 _pdbx_validate_rmsd_bond.PDB_ins_code_1 _pdbx_validate_rmsd_bond.label_alt_id_1 _pdbx_validate_rmsd_bond.auth_atom_id_2 _pdbx_validate_rmsd_bond.auth_asym_id_2 _pdbx_validate_rmsd_bond.auth_comp_id_2 _pdbx_validate_rmsd_bond.auth_seq_id_2 _pdbx_validate_rmsd_bond.PDB_ins_code_2 _pdbx_validate_rmsd_bond.label_alt_id_2 _pdbx_validate_rmsd_bond.bond_value _pdbx_validate_rmsd_bond.bond_target_value _pdbx_validate_rmsd_bond.bond_deviation _pdbx_validate_rmsd_bond.bond_standard_deviation _pdbx_validate_rmsd_bond.linker_flag 1 1 CA A ALA 434 ? ? CB A ALA 434 ? ? 1.666 1.520 0.146 0.021 N 2 1 CD A GLU 503 ? ? OE2 A GLU 503 ? ? 1.321 1.252 0.069 0.011 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 NE A ARG 46 ? A CZ A ARG 46 ? A NH1 A ARG 46 ? A 117.15 120.30 -3.15 0.50 N 2 1 NE A ARG 126 ? ? CZ A ARG 126 ? ? NH1 A ARG 126 ? ? 127.26 120.30 6.96 0.50 N 3 1 NE A ARG 126 ? ? CZ A ARG 126 ? ? NH2 A ARG 126 ? ? 112.68 120.30 -7.62 0.50 N 4 1 CD A LYS 374 ? A CE A LYS 374 ? A NZ A LYS 374 ? A 128.41 111.70 16.71 2.30 N 5 1 CB A THR 490 ? ? CA A THR 490 ? ? C A THR 490 ? ? 91.93 111.60 -19.67 2.70 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 HIS A -2 ? ? 142.72 -68.38 2 1 HIS A 98 ? ? -154.76 64.00 3 1 ASN A 221 ? ? -90.18 -152.40 4 1 TYR A 271 ? ? -94.33 -61.85 5 1 ILE A 432 ? ? 71.57 -50.17 6 1 THR A 442 ? ? -160.37 -166.54 7 1 GLU A 491 ? ? 46.98 -136.80 8 1 ARG A 526 ? ? 176.72 165.28 9 1 TRP A 544 ? ? 54.57 -133.27 # _pdbx_validate_peptide_omega.id 1 _pdbx_validate_peptide_omega.PDB_model_num 1 _pdbx_validate_peptide_omega.auth_comp_id_1 HIS _pdbx_validate_peptide_omega.auth_asym_id_1 A _pdbx_validate_peptide_omega.auth_seq_id_1 -3 _pdbx_validate_peptide_omega.PDB_ins_code_1 ? _pdbx_validate_peptide_omega.label_alt_id_1 ? _pdbx_validate_peptide_omega.auth_comp_id_2 HIS _pdbx_validate_peptide_omega.auth_asym_id_2 A _pdbx_validate_peptide_omega.auth_seq_id_2 -2 _pdbx_validate_peptide_omega.PDB_ins_code_2 ? _pdbx_validate_peptide_omega.label_alt_id_2 ? _pdbx_validate_peptide_omega.omega 143.42 # 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 LYS 603 ? A LYS 607 2 1 Y 1 A LYS 604 ? A LYS 608 3 1 Y 1 A TYR 605 ? A TYR 609 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 GLYCEROL GOL 4 'SULFATE ION' SO4 5 1-THIO-BETA-D-GLUCOPYRANOSE GS1 6 O1-METHYL-GLUCOSE MGL 7 water HOH # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 701 1 NAG NAG A . C 2 NAG 1 702 2 NAG NAG A . D 2 NAG 1 703 3 NAG NAG A . E 3 GOL 1 704 1 GOL GOL A . F 3 GOL 1 705 2 GOL GOL A . G 3 GOL 1 706 3 GOL GOL A . H 3 GOL 1 707 4 GOL GOL A . I 3 GOL 1 708 5 GOL GOL A . J 3 GOL 1 709 6 GOL GOL A . K 4 SO4 1 710 1 SO4 SO4 A . L 3 GOL 1 711 7 GOL GOL A . M 3 GOL 1 712 8 GOL GOL A . N 3 GOL 1 713 9 GOL GOL A . O 3 GOL 1 714 10 GOL GOL A . P 3 GOL 1 715 11 GOL GOL A . Q 3 GOL 1 716 12 GOL GOL A . R 3 GOL 1 717 13 GOL GOL A . S 3 GOL 1 718 14 GOL GOL A . T 5 GS1 1 719 1 GS1 G6S A . U 6 MGL 2 720 1 MGL G6S A . V 7 HOH 1 801 1 HOH HOH A . V 7 HOH 2 802 2 HOH HOH A . V 7 HOH 3 803 3 HOH HOH A . V 7 HOH 4 804 4 HOH HOH A . V 7 HOH 5 805 5 HOH HOH A . V 7 HOH 6 806 6 HOH HOH A . V 7 HOH 7 807 7 HOH HOH A . V 7 HOH 8 808 8 HOH HOH A . V 7 HOH 9 809 9 HOH HOH A . V 7 HOH 10 810 10 HOH HOH A . V 7 HOH 11 811 11 HOH HOH A . V 7 HOH 12 812 12 HOH HOH A . V 7 HOH 13 813 13 HOH HOH A . V 7 HOH 14 814 14 HOH HOH A . V 7 HOH 15 815 15 HOH HOH A . V 7 HOH 16 816 16 HOH HOH A . V 7 HOH 17 817 17 HOH HOH A . V 7 HOH 18 818 18 HOH HOH A . V 7 HOH 19 819 19 HOH HOH A . V 7 HOH 20 820 20 HOH HOH A . V 7 HOH 21 821 21 HOH HOH A . V 7 HOH 22 822 22 HOH HOH A . V 7 HOH 23 823 23 HOH HOH A . V 7 HOH 24 824 24 HOH HOH A . V 7 HOH 25 825 25 HOH HOH A . V 7 HOH 26 826 26 HOH HOH A . V 7 HOH 27 827 27 HOH HOH A . V 7 HOH 28 828 28 HOH HOH A . V 7 HOH 29 829 29 HOH HOH A . V 7 HOH 30 830 30 HOH HOH A . V 7 HOH 31 831 31 HOH HOH A . V 7 HOH 32 832 32 HOH HOH A . V 7 HOH 33 833 33 HOH HOH A . V 7 HOH 34 834 34 HOH HOH A . V 7 HOH 35 835 35 HOH HOH A . V 7 HOH 36 836 36 HOH HOH A . V 7 HOH 37 837 37 HOH HOH A . V 7 HOH 38 838 38 HOH HOH A . V 7 HOH 39 839 39 HOH HOH A . V 7 HOH 40 840 40 HOH HOH A . V 7 HOH 41 841 41 HOH HOH A . V 7 HOH 42 842 42 HOH HOH A . V 7 HOH 43 843 43 HOH HOH A . V 7 HOH 44 844 44 HOH HOH A . V 7 HOH 45 845 45 HOH HOH A . V 7 HOH 46 846 46 HOH HOH A . V 7 HOH 47 847 47 HOH HOH A . V 7 HOH 48 848 48 HOH HOH A . V 7 HOH 49 849 49 HOH HOH A . V 7 HOH 50 850 50 HOH HOH A . V 7 HOH 51 851 51 HOH HOH A . V 7 HOH 52 852 52 HOH HOH A . V 7 HOH 53 853 53 HOH HOH A . V 7 HOH 54 854 54 HOH HOH A . V 7 HOH 55 855 55 HOH HOH A . V 7 HOH 56 856 56 HOH HOH A . V 7 HOH 57 857 57 HOH HOH A . V 7 HOH 58 858 58 HOH HOH A . V 7 HOH 59 859 59 HOH HOH A . V 7 HOH 60 860 60 HOH HOH A . V 7 HOH 61 861 61 HOH HOH A . V 7 HOH 62 862 62 HOH HOH A . V 7 HOH 63 863 63 HOH HOH A . V 7 HOH 64 864 64 HOH HOH A . V 7 HOH 65 865 65 HOH HOH A . V 7 HOH 66 866 66 HOH HOH A . V 7 HOH 67 867 67 HOH HOH A . V 7 HOH 68 868 68 HOH HOH A . V 7 HOH 69 869 69 HOH HOH A . V 7 HOH 70 870 70 HOH HOH A . V 7 HOH 71 871 71 HOH HOH A . V 7 HOH 72 872 72 HOH HOH A . V 7 HOH 73 873 73 HOH HOH A . V 7 HOH 74 874 74 HOH HOH A . V 7 HOH 75 875 75 HOH HOH A . V 7 HOH 76 876 76 HOH HOH A . V 7 HOH 77 877 77 HOH HOH A . V 7 HOH 78 878 78 HOH HOH A . V 7 HOH 79 879 79 HOH HOH A . V 7 HOH 80 880 80 HOH HOH A . V 7 HOH 81 881 81 HOH HOH A . V 7 HOH 82 882 82 HOH HOH A . V 7 HOH 83 883 83 HOH HOH A . V 7 HOH 84 884 84 HOH HOH A . V 7 HOH 85 885 85 HOH HOH A . V 7 HOH 86 886 86 HOH HOH A . V 7 HOH 87 887 87 HOH HOH A . V 7 HOH 88 888 88 HOH HOH A . V 7 HOH 89 889 89 HOH HOH A . V 7 HOH 90 890 90 HOH HOH A . V 7 HOH 91 891 91 HOH HOH A . V 7 HOH 92 892 92 HOH HOH A . V 7 HOH 93 893 93 HOH HOH A . V 7 HOH 94 894 94 HOH HOH A . V 7 HOH 95 895 95 HOH HOH A . V 7 HOH 96 896 96 HOH HOH A . V 7 HOH 97 897 97 HOH HOH A . V 7 HOH 98 898 98 HOH HOH A . V 7 HOH 99 899 99 HOH HOH A . V 7 HOH 100 900 100 HOH HOH A . V 7 HOH 101 901 101 HOH HOH A . V 7 HOH 102 902 102 HOH HOH A . V 7 HOH 103 903 103 HOH HOH A . V 7 HOH 104 904 104 HOH HOH A . V 7 HOH 105 905 105 HOH HOH A . V 7 HOH 106 906 106 HOH HOH A . V 7 HOH 107 907 107 HOH HOH A . V 7 HOH 108 908 108 HOH HOH A . V 7 HOH 109 909 109 HOH HOH A . V 7 HOH 110 910 110 HOH HOH A . V 7 HOH 111 911 111 HOH HOH A . V 7 HOH 112 912 112 HOH HOH A . V 7 HOH 113 913 113 HOH HOH A . V 7 HOH 114 914 114 HOH HOH A . V 7 HOH 115 915 115 HOH HOH A . V 7 HOH 116 916 116 HOH HOH A . V 7 HOH 117 917 117 HOH HOH A . V 7 HOH 118 918 118 HOH HOH A . V 7 HOH 119 919 119 HOH HOH A . V 7 HOH 120 920 120 HOH HOH A . V 7 HOH 121 921 121 HOH HOH A . V 7 HOH 122 922 122 HOH HOH A . V 7 HOH 123 923 123 HOH HOH A . V 7 HOH 124 924 124 HOH HOH A . V 7 HOH 125 925 125 HOH HOH A . V 7 HOH 126 926 126 HOH HOH A . V 7 HOH 127 927 127 HOH HOH A . V 7 HOH 128 928 128 HOH HOH A . V 7 HOH 129 929 129 HOH HOH A . V 7 HOH 130 930 130 HOH HOH A . V 7 HOH 131 931 131 HOH HOH A . V 7 HOH 132 932 132 HOH HOH A . V 7 HOH 133 933 133 HOH HOH A . V 7 HOH 134 934 134 HOH HOH A . V 7 HOH 135 935 135 HOH HOH A . V 7 HOH 136 936 136 HOH HOH A . V 7 HOH 137 937 137 HOH HOH A . V 7 HOH 138 938 138 HOH HOH A . V 7 HOH 139 939 139 HOH HOH A . V 7 HOH 140 940 140 HOH HOH A . V 7 HOH 141 941 141 HOH HOH A . V 7 HOH 142 942 142 HOH HOH A . V 7 HOH 143 943 143 HOH HOH A . V 7 HOH 144 944 144 HOH HOH A . V 7 HOH 145 945 145 HOH HOH A . V 7 HOH 146 946 146 HOH HOH A . V 7 HOH 147 947 147 HOH HOH A . V 7 HOH 148 948 148 HOH HOH A . V 7 HOH 149 949 149 HOH HOH A . V 7 HOH 150 950 150 HOH HOH A . V 7 HOH 151 951 151 HOH HOH A . V 7 HOH 152 952 152 HOH HOH A . V 7 HOH 153 953 153 HOH HOH A . V 7 HOH 154 954 154 HOH HOH A . V 7 HOH 155 955 155 HOH HOH A . V 7 HOH 156 956 156 HOH HOH A . V 7 HOH 157 957 157 HOH HOH A . V 7 HOH 158 958 158 HOH HOH A . V 7 HOH 159 959 159 HOH HOH A . V 7 HOH 160 960 160 HOH HOH A . V 7 HOH 161 961 161 HOH HOH A . V 7 HOH 162 962 162 HOH HOH A . V 7 HOH 163 963 163 HOH HOH A . V 7 HOH 164 964 164 HOH HOH A . V 7 HOH 165 965 165 HOH HOH A . V 7 HOH 166 966 166 HOH HOH A . V 7 HOH 167 967 167 HOH HOH A . V 7 HOH 168 968 168 HOH HOH A . V 7 HOH 169 969 169 HOH HOH A . V 7 HOH 170 970 170 HOH HOH A . V 7 HOH 171 971 171 HOH HOH A . V 7 HOH 172 972 172 HOH HOH A . V 7 HOH 173 973 173 HOH HOH A . V 7 HOH 174 974 174 HOH HOH A . V 7 HOH 175 975 175 HOH HOH A . V 7 HOH 176 976 176 HOH HOH A . V 7 HOH 177 977 177 HOH HOH A . V 7 HOH 178 978 178 HOH HOH A . V 7 HOH 179 979 179 HOH HOH A . V 7 HOH 180 980 180 HOH HOH A . V 7 HOH 181 981 181 HOH HOH A . V 7 HOH 182 982 182 HOH HOH A . V 7 HOH 183 983 183 HOH HOH A . V 7 HOH 184 984 184 HOH HOH A . V 7 HOH 185 985 185 HOH HOH A . V 7 HOH 186 986 186 HOH HOH A . V 7 HOH 187 987 187 HOH HOH A . V 7 HOH 188 988 188 HOH HOH A . V 7 HOH 189 989 189 HOH HOH A . V 7 HOH 190 990 190 HOH HOH A . V 7 HOH 191 991 191 HOH HOH A . V 7 HOH 192 992 192 HOH HOH A . V 7 HOH 193 993 193 HOH HOH A . V 7 HOH 194 994 194 HOH HOH A . V 7 HOH 195 995 195 HOH HOH A . V 7 HOH 196 996 196 HOH HOH A . V 7 HOH 197 997 197 HOH HOH A . V 7 HOH 198 998 198 HOH HOH A . V 7 HOH 199 999 199 HOH HOH A . V 7 HOH 200 1000 200 HOH HOH A . V 7 HOH 201 1001 201 HOH HOH A . V 7 HOH 202 1002 202 HOH HOH A . V 7 HOH 203 1003 203 HOH HOH A . V 7 HOH 204 1004 204 HOH HOH A . V 7 HOH 205 1005 205 HOH HOH A . V 7 HOH 206 1006 206 HOH HOH A . V 7 HOH 207 1007 207 HOH HOH A . V 7 HOH 208 1008 208 HOH HOH A . V 7 HOH 209 1009 209 HOH HOH A . V 7 HOH 210 1010 210 HOH HOH A . V 7 HOH 211 1011 211 HOH HOH A . V 7 HOH 212 1012 212 HOH HOH A . V 7 HOH 213 1013 213 HOH HOH A . V 7 HOH 214 1014 214 HOH HOH A . V 7 HOH 215 1015 215 HOH HOH A . V 7 HOH 216 1016 216 HOH HOH A . V 7 HOH 217 1017 217 HOH HOH A . V 7 HOH 218 1018 218 HOH HOH A . V 7 HOH 219 1019 219 HOH HOH A . V 7 HOH 220 1020 220 HOH HOH A . V 7 HOH 221 1021 221 HOH HOH A . V 7 HOH 222 1022 222 HOH HOH A . V 7 HOH 223 1023 223 HOH HOH A . V 7 HOH 224 1024 224 HOH HOH A . V 7 HOH 225 1025 225 HOH HOH A . V 7 HOH 226 1026 226 HOH HOH A . V 7 HOH 227 1027 227 HOH HOH A . V 7 HOH 228 1028 228 HOH HOH A . V 7 HOH 229 1029 229 HOH HOH A . V 7 HOH 230 1030 230 HOH HOH A . V 7 HOH 231 1031 231 HOH HOH A . V 7 HOH 232 1032 232 HOH HOH A . V 7 HOH 233 1033 233 HOH HOH A . V 7 HOH 234 1034 234 HOH HOH A . V 7 HOH 235 1035 235 HOH HOH A . V 7 HOH 236 1036 236 HOH HOH A . V 7 HOH 237 1037 237 HOH HOH A . V 7 HOH 238 1038 238 HOH HOH A . V 7 HOH 239 1039 239 HOH HOH A . V 7 HOH 240 1040 240 HOH HOH A . V 7 HOH 241 1041 241 HOH HOH A . V 7 HOH 242 1042 242 HOH HOH A . V 7 HOH 243 1043 243 HOH HOH A . V 7 HOH 244 1044 244 HOH HOH A . V 7 HOH 245 1045 245 HOH HOH A . V 7 HOH 246 1046 246 HOH HOH A . V 7 HOH 247 1047 247 HOH HOH A . V 7 HOH 248 1048 248 HOH HOH A . V 7 HOH 249 1049 249 HOH HOH A . V 7 HOH 250 1050 250 HOH HOH A . V 7 HOH 251 1051 251 HOH HOH A . V 7 HOH 252 1052 252 HOH HOH A . V 7 HOH 253 1053 253 HOH HOH A . V 7 HOH 254 1054 254 HOH HOH A . V 7 HOH 255 1055 255 HOH HOH A . V 7 HOH 256 1056 256 HOH HOH A . V 7 HOH 257 1057 257 HOH HOH A . V 7 HOH 258 1058 258 HOH HOH A . V 7 HOH 259 1059 259 HOH HOH A . V 7 HOH 260 1060 260 HOH HOH A . V 7 HOH 261 1061 261 HOH HOH A . V 7 HOH 262 1062 262 HOH HOH A . V 7 HOH 263 1063 263 HOH HOH A . V 7 HOH 264 1064 264 HOH HOH A . V 7 HOH 265 1065 265 HOH HOH A . V 7 HOH 266 1066 266 HOH HOH A . V 7 HOH 267 1067 267 HOH HOH A . V 7 HOH 268 1068 268 HOH HOH A . V 7 HOH 269 1069 269 HOH HOH A . V 7 HOH 270 1070 270 HOH HOH A . V 7 HOH 271 1071 271 HOH HOH A . V 7 HOH 272 1072 272 HOH HOH A . V 7 HOH 273 1073 273 HOH HOH A . V 7 HOH 274 1074 274 HOH HOH A . V 7 HOH 275 1075 275 HOH HOH A . V 7 HOH 276 1076 276 HOH HOH A . V 7 HOH 277 1077 277 HOH HOH A . V 7 HOH 278 1078 278 HOH HOH A . V 7 HOH 279 1079 279 HOH HOH A . V 7 HOH 280 1080 280 HOH HOH A . V 7 HOH 281 1081 281 HOH HOH A . V 7 HOH 282 1082 282 HOH HOH A . V 7 HOH 283 1083 283 HOH HOH A . V 7 HOH 284 1084 284 HOH HOH A . V 7 HOH 285 1085 285 HOH HOH A . V 7 HOH 286 1086 286 HOH HOH A . V 7 HOH 287 1087 287 HOH HOH A . V 7 HOH 288 1088 288 HOH HOH A . V 7 HOH 289 1089 289 HOH HOH A . V 7 HOH 290 1090 290 HOH HOH A . V 7 HOH 291 1091 291 HOH HOH A . V 7 HOH 292 1092 292 HOH HOH A . V 7 HOH 293 1093 293 HOH HOH A . V 7 HOH 294 1094 294 HOH HOH A . V 7 HOH 295 1095 295 HOH HOH A . V 7 HOH 296 1096 296 HOH HOH A . V 7 HOH 297 1097 297 HOH HOH A . V 7 HOH 298 1098 298 HOH HOH A . V 7 HOH 299 1099 299 HOH HOH A . V 7 HOH 300 1100 300 HOH HOH A . V 7 HOH 301 1101 301 HOH HOH A . V 7 HOH 302 1102 302 HOH HOH A . V 7 HOH 303 1103 303 HOH HOH A . V 7 HOH 304 1104 304 HOH HOH A . V 7 HOH 305 1105 305 HOH HOH A . V 7 HOH 306 1106 306 HOH HOH A . V 7 HOH 307 1107 307 HOH HOH A . V 7 HOH 308 1108 308 HOH HOH A . V 7 HOH 309 1109 309 HOH HOH A . V 7 HOH 310 1110 310 HOH HOH A . V 7 HOH 311 1111 311 HOH HOH A . V 7 HOH 312 1112 312 HOH HOH A . V 7 HOH 313 1113 313 HOH HOH A . V 7 HOH 314 1114 314 HOH HOH A . V 7 HOH 315 1115 315 HOH HOH A . V 7 HOH 316 1116 316 HOH HOH A . V 7 HOH 317 1117 317 HOH HOH A . V 7 HOH 318 1118 318 HOH HOH A . V 7 HOH 319 1119 319 HOH HOH A . V 7 HOH 320 1120 320 HOH HOH A . V 7 HOH 321 1121 321 HOH HOH A . V 7 HOH 322 1122 322 HOH HOH A . V 7 HOH 323 1123 323 HOH HOH A . V 7 HOH 324 1124 324 HOH HOH A . V 7 HOH 325 1125 325 HOH HOH A . V 7 HOH 326 1126 326 HOH HOH A . V 7 HOH 327 1127 327 HOH HOH A . V 7 HOH 328 1128 328 HOH HOH A . V 7 HOH 329 1129 329 HOH HOH A . V 7 HOH 330 1130 330 HOH HOH A . V 7 HOH 331 1131 331 HOH HOH A . V 7 HOH 332 1132 332 HOH HOH A . V 7 HOH 333 1133 333 HOH HOH A . V 7 HOH 334 1134 334 HOH HOH A . V 7 HOH 335 1135 335 HOH HOH A . V 7 HOH 336 1136 336 HOH HOH A . V 7 HOH 337 1137 337 HOH HOH A . V 7 HOH 338 1138 338 HOH HOH A . V 7 HOH 339 1139 339 HOH HOH A . V 7 HOH 340 1140 340 HOH HOH A . V 7 HOH 341 1141 341 HOH HOH A . V 7 HOH 342 1142 342 HOH HOH A . V 7 HOH 343 1143 343 HOH HOH A . V 7 HOH 344 1144 344 HOH HOH A . V 7 HOH 345 1145 345 HOH HOH A . V 7 HOH 346 1146 346 HOH HOH A . V 7 HOH 347 1147 347 HOH HOH A . V 7 HOH 348 1148 348 HOH HOH A . V 7 HOH 349 1149 349 HOH HOH A . V 7 HOH 350 1150 350 HOH HOH A . V 7 HOH 351 1151 351 HOH HOH A . V 7 HOH 352 1152 352 HOH HOH A . V 7 HOH 353 1153 353 HOH HOH A . V 7 HOH 354 1154 354 HOH HOH A . V 7 HOH 355 1155 355 HOH HOH A . V 7 HOH 356 1156 356 HOH HOH A . V 7 HOH 357 1157 357 HOH HOH A . V 7 HOH 358 1158 358 HOH HOH A . V 7 HOH 359 1159 359 HOH HOH A . V 7 HOH 360 1160 360 HOH HOH A . V 7 HOH 361 1161 361 HOH HOH A . V 7 HOH 362 1162 362 HOH HOH A . V 7 HOH 363 1163 363 HOH HOH A . V 7 HOH 364 1164 364 HOH HOH A . V 7 HOH 365 1165 365 HOH HOH A . V 7 HOH 366 1166 366 HOH HOH A . V 7 HOH 367 1167 367 HOH HOH A . V 7 HOH 368 1168 368 HOH HOH A . V 7 HOH 369 1169 369 HOH HOH A . V 7 HOH 370 1170 370 HOH HOH A . V 7 HOH 371 1171 371 HOH HOH A . V 7 HOH 372 1172 372 HOH HOH A . V 7 HOH 373 1173 373 HOH HOH A . V 7 HOH 374 1174 374 HOH HOH A . V 7 HOH 375 1175 375 HOH HOH A . V 7 HOH 376 1176 376 HOH HOH A . V 7 HOH 377 1177 377 HOH HOH A . V 7 HOH 378 1178 378 HOH HOH A . V 7 HOH 379 1179 379 HOH HOH A . V 7 HOH 380 1180 380 HOH HOH A . V 7 HOH 381 1181 381 HOH HOH A . V 7 HOH 382 1182 382 HOH HOH A . V 7 HOH 383 1183 383 HOH HOH A . V 7 HOH 384 1184 384 HOH HOH A . V 7 HOH 385 1185 385 HOH HOH A . V 7 HOH 386 1186 386 HOH HOH A . V 7 HOH 387 1187 387 HOH HOH A . V 7 HOH 388 1188 388 HOH HOH A . V 7 HOH 389 1189 389 HOH HOH A . V 7 HOH 390 1190 390 HOH HOH A . V 7 HOH 391 1191 391 HOH HOH A . V 7 HOH 392 1192 392 HOH HOH A . V 7 HOH 393 1193 393 HOH HOH A . V 7 HOH 394 1194 394 HOH HOH A . V 7 HOH 395 1195 395 HOH HOH A . V 7 HOH 396 1196 396 HOH HOH A . V 7 HOH 397 1197 397 HOH HOH A . V 7 HOH 398 1198 398 HOH HOH A . V 7 HOH 399 1199 399 HOH HOH A . V 7 HOH 400 1200 400 HOH HOH A . V 7 HOH 401 1201 401 HOH HOH A . V 7 HOH 402 1202 402 HOH HOH A . V 7 HOH 403 1203 403 HOH HOH A . V 7 HOH 404 1204 404 HOH HOH A . V 7 HOH 405 1205 405 HOH HOH A . V 7 HOH 406 1206 406 HOH HOH A . V 7 HOH 407 1207 407 HOH HOH A . V 7 HOH 408 1208 408 HOH HOH A . V 7 HOH 409 1209 409 HOH HOH A . V 7 HOH 410 1210 410 HOH HOH A . V 7 HOH 411 1211 411 HOH HOH A . V 7 HOH 412 1212 412 HOH HOH A . V 7 HOH 413 1213 413 HOH HOH A . V 7 HOH 414 1214 414 HOH HOH A . V 7 HOH 415 1215 415 HOH HOH A . V 7 HOH 416 1216 416 HOH HOH A . V 7 HOH 417 1217 417 HOH HOH A . V 7 HOH 418 1218 418 HOH HOH A . V 7 HOH 419 1219 419 HOH HOH A . V 7 HOH 420 1220 420 HOH HOH A . V 7 HOH 421 1221 421 HOH HOH A . V 7 HOH 422 1222 422 HOH HOH A . V 7 HOH 423 1223 423 HOH HOH A . V 7 HOH 424 1224 424 HOH HOH A . V 7 HOH 425 1225 425 HOH HOH A . V 7 HOH 426 1226 426 HOH HOH A . V 7 HOH 427 1227 427 HOH HOH A . V 7 HOH 428 1228 428 HOH HOH A . V 7 HOH 429 1229 429 HOH HOH A . V 7 HOH 430 1230 430 HOH HOH A . V 7 HOH 431 1231 431 HOH HOH A . V 7 HOH 432 1232 432 HOH HOH A . V 7 HOH 433 1233 433 HOH HOH A . V 7 HOH 434 1234 434 HOH HOH A . V 7 HOH 435 1235 435 HOH HOH A . V 7 HOH 436 1236 436 HOH HOH A . V 7 HOH 437 1237 437 HOH HOH A . V 7 HOH 438 1238 438 HOH HOH A . V 7 HOH 439 1239 439 HOH HOH A . V 7 HOH 440 1240 440 HOH HOH A . V 7 HOH 441 1241 441 HOH HOH A . V 7 HOH 442 1242 442 HOH HOH A . V 7 HOH 443 1243 443 HOH HOH A . V 7 HOH 444 1244 444 HOH HOH A . V 7 HOH 445 1245 445 HOH HOH A . V 7 HOH 446 1246 446 HOH HOH A . V 7 HOH 447 1247 447 HOH HOH A . V 7 HOH 448 1248 448 HOH HOH A . V 7 HOH 449 1249 449 HOH HOH A . V 7 HOH 450 1250 450 HOH HOH A . V 7 HOH 451 1251 451 HOH HOH A . V 7 HOH 452 1252 452 HOH HOH A . V 7 HOH 453 1253 453 HOH HOH A . V 7 HOH 454 1254 454 HOH HOH A . V 7 HOH 455 1255 455 HOH HOH A . V 7 HOH 456 1256 456 HOH HOH A . V 7 HOH 457 1257 457 HOH HOH A . V 7 HOH 458 1258 458 HOH HOH A . V 7 HOH 459 1259 459 HOH HOH A . V 7 HOH 460 1260 460 HOH HOH A . V 7 HOH 461 1261 461 HOH HOH A . V 7 HOH 462 1262 462 HOH HOH A . V 7 HOH 463 1263 463 HOH HOH A . V 7 HOH 464 1264 464 HOH HOH A . V 7 HOH 465 1265 465 HOH HOH A . V 7 HOH 466 1266 466 HOH HOH A . V 7 HOH 467 1267 467 HOH HOH A . V 7 HOH 468 1268 468 HOH HOH A . V 7 HOH 469 1269 469 HOH HOH A . V 7 HOH 470 1270 470 HOH HOH A . V 7 HOH 471 1271 471 HOH HOH A . V 7 HOH 472 1272 472 HOH HOH A . V 7 HOH 473 1273 473 HOH HOH A . V 7 HOH 474 1274 474 HOH HOH A . V 7 HOH 475 1275 475 HOH HOH A . V 7 HOH 476 1276 476 HOH HOH A . V 7 HOH 477 1277 477 HOH HOH A . V 7 HOH 478 1278 478 HOH HOH A . V 7 HOH 479 1279 479 HOH HOH A . V 7 HOH 480 1280 480 HOH HOH A . V 7 HOH 481 1281 481 HOH HOH A . V 7 HOH 482 1282 482 HOH HOH A . V 7 HOH 483 1283 483 HOH HOH A . V 7 HOH 484 1284 484 HOH HOH A . V 7 HOH 485 1285 485 HOH HOH A . V 7 HOH 486 1286 486 HOH HOH A . V 7 HOH 487 1287 487 HOH HOH A . V 7 HOH 488 1288 488 HOH HOH A . V 7 HOH 489 1289 489 HOH HOH A . V 7 HOH 490 1290 490 HOH HOH A . V 7 HOH 491 1291 491 HOH HOH A . V 7 HOH 492 1292 492 HOH HOH A . V 7 HOH 493 1293 493 HOH HOH A . V 7 HOH 494 1294 494 HOH HOH A . V 7 HOH 495 1295 495 HOH HOH A . V 7 HOH 496 1296 496 HOH HOH A . V 7 HOH 497 1297 497 HOH HOH A . V 7 HOH 498 1298 498 HOH HOH A . V 7 HOH 499 1299 499 HOH HOH A . V 7 HOH 500 1300 500 HOH HOH A . V 7 HOH 501 1301 501 HOH HOH A . V 7 HOH 502 1302 502 HOH HOH A . V 7 HOH 503 1303 503 HOH HOH A . V 7 HOH 504 1304 504 HOH HOH A . V 7 HOH 505 1305 505 HOH HOH A . V 7 HOH 506 1306 506 HOH HOH A . V 7 HOH 507 1307 507 HOH HOH A . V 7 HOH 508 1308 508 HOH HOH A . V 7 HOH 509 1309 509 HOH HOH A . V 7 HOH 510 1310 510 HOH HOH A . V 7 HOH 511 1311 511 HOH HOH A . V 7 HOH 512 1312 512 HOH HOH A . V 7 HOH 513 1313 513 HOH HOH A . V 7 HOH 514 1314 514 HOH HOH A . V 7 HOH 515 1315 515 HOH HOH A . V 7 HOH 516 1316 516 HOH HOH A . V 7 HOH 517 1317 517 HOH HOH A . V 7 HOH 518 1318 518 HOH HOH A . V 7 HOH 519 1319 519 HOH HOH A . V 7 HOH 520 1320 520 HOH HOH A . V 7 HOH 521 1321 521 HOH HOH A . V 7 HOH 522 1322 522 HOH HOH A . V 7 HOH 523 1323 523 HOH HOH A . V 7 HOH 524 1324 524 HOH HOH A . V 7 HOH 525 1325 525 HOH HOH A . V 7 HOH 526 1326 526 HOH HOH A . V 7 HOH 527 1327 527 HOH HOH A . V 7 HOH 528 1328 528 HOH HOH A . V 7 HOH 529 1329 529 HOH HOH A . V 7 HOH 530 1330 530 HOH HOH A . V 7 HOH 531 1331 531 HOH HOH A . V 7 HOH 532 1332 532 HOH HOH A . V 7 HOH 533 1333 533 HOH HOH A . V 7 HOH 534 1334 534 HOH HOH A . V 7 HOH 535 1335 535 HOH HOH A . V 7 HOH 536 1336 536 HOH HOH A . V 7 HOH 537 1337 537 HOH HOH A . V 7 HOH 538 1338 538 HOH HOH A . V 7 HOH 539 1339 539 HOH HOH A . V 7 HOH 540 1340 540 HOH HOH A . V 7 HOH 541 1341 541 HOH HOH A . V 7 HOH 542 1342 542 HOH HOH A . V 7 HOH 543 1343 543 HOH HOH A . V 7 HOH 544 1344 544 HOH HOH A . V 7 HOH 545 1345 545 HOH HOH A . V 7 HOH 546 1346 546 HOH HOH A . V 7 HOH 547 1347 547 HOH HOH A . V 7 HOH 548 1348 548 HOH HOH A . V 7 HOH 549 1349 549 HOH HOH A . V 7 HOH 550 1350 550 HOH HOH A . V 7 HOH 551 1351 551 HOH HOH A . V 7 HOH 552 1352 552 HOH HOH A . V 7 HOH 553 1353 553 HOH HOH A . V 7 HOH 554 1354 554 HOH HOH A . V 7 HOH 555 1355 555 HOH HOH A . V 7 HOH 556 1356 556 HOH HOH A . V 7 HOH 557 1357 557 HOH HOH A . V 7 HOH 558 1358 558 HOH HOH A . V 7 HOH 559 1359 559 HOH HOH A . V 7 HOH 560 1360 560 HOH HOH A . V 7 HOH 561 1361 561 HOH HOH A . V 7 HOH 562 1362 562 HOH HOH A . V 7 HOH 563 1363 563 HOH HOH A . V 7 HOH 564 1364 564 HOH HOH A . V 7 HOH 565 1365 565 HOH HOH A . V 7 HOH 566 1366 566 HOH HOH A . V 7 HOH 567 1367 567 HOH HOH A . V 7 HOH 568 1368 568 HOH HOH A . V 7 HOH 569 1369 569 HOH HOH A . V 7 HOH 570 1370 570 HOH HOH A . V 7 HOH 571 1371 571 HOH HOH A . V 7 HOH 572 1372 572 HOH HOH A . V 7 HOH 573 1373 573 HOH HOH A . V 7 HOH 574 1374 574 HOH HOH A . V 7 HOH 575 1375 575 HOH HOH A . V 7 HOH 576 1376 576 HOH HOH A . V 7 HOH 577 1377 577 HOH HOH A . V 7 HOH 578 1378 578 HOH HOH A . V 7 HOH 579 1379 579 HOH HOH A . V 7 HOH 580 1380 580 HOH HOH A . V 7 HOH 581 1381 581 HOH HOH A . V 7 HOH 582 1382 582 HOH HOH A . V 7 HOH 583 1383 583 HOH HOH A . V 7 HOH 584 1384 584 HOH HOH A . V 7 HOH 585 1385 585 HOH HOH A . V 7 HOH 586 1386 586 HOH HOH A . V 7 HOH 587 1387 587 HOH HOH A . V 7 HOH 588 1388 588 HOH HOH A . V 7 HOH 589 1389 589 HOH HOH A . V 7 HOH 590 1390 590 HOH HOH A . V 7 HOH 591 1391 591 HOH HOH A . V 7 HOH 592 1392 592 HOH HOH A . V 7 HOH 593 1393 593 HOH HOH A . V 7 HOH 594 1394 594 HOH HOH A . V 7 HOH 595 1395 595 HOH HOH A . V 7 HOH 596 1396 596 HOH HOH A . V 7 HOH 597 1397 597 HOH HOH A . V 7 HOH 598 1398 598 HOH HOH A . V 7 HOH 599 1399 599 HOH HOH A . V 7 HOH 600 1400 600 HOH HOH A . V 7 HOH 601 1401 601 HOH HOH A . V 7 HOH 602 1402 602 HOH HOH A . V 7 HOH 603 1403 603 HOH HOH A . V 7 HOH 604 1404 604 HOH HOH A . V 7 HOH 605 1405 605 HOH HOH A . V 7 HOH 606 1406 606 HOH HOH A . V 7 HOH 607 1407 607 HOH HOH A . V 7 HOH 608 1408 608 HOH HOH A . V 7 HOH 609 1409 609 HOH HOH A . V 7 HOH 610 1410 610 HOH HOH A . V 7 HOH 611 1411 611 HOH HOH A . V 7 HOH 612 1412 612 HOH HOH A . V 7 HOH 613 1413 613 HOH HOH A . V 7 HOH 614 1414 614 HOH HOH A . V 7 HOH 615 1415 615 HOH HOH A . V 7 HOH 616 1416 616 HOH HOH A . V 7 HOH 617 1417 617 HOH HOH A . V 7 HOH 618 1418 618 HOH HOH A . V 7 HOH 619 1419 619 HOH HOH A . V 7 HOH 620 1420 620 HOH HOH A . V 7 HOH 621 1421 621 HOH HOH A . V 7 HOH 622 1422 622 HOH HOH A . V 7 HOH 623 1423 623 HOH HOH A . V 7 HOH 624 1424 624 HOH HOH A . V 7 HOH 625 1425 625 HOH HOH A . V 7 HOH 626 1426 626 HOH HOH A . V 7 HOH 627 1427 627 HOH HOH A . V 7 HOH 628 1428 628 HOH HOH A . V 7 HOH 629 1429 629 HOH HOH A . V 7 HOH 630 1430 630 HOH HOH A . V 7 HOH 631 1431 631 HOH HOH A . V 7 HOH 632 1432 632 HOH HOH A . V 7 HOH 633 1433 633 HOH HOH A . V 7 HOH 634 1434 634 HOH HOH A . V 7 HOH 635 1435 635 HOH HOH A . V 7 HOH 636 1436 636 HOH HOH A . V 7 HOH 637 1437 637 HOH HOH A . V 7 HOH 638 1438 638 HOH HOH A . V 7 HOH 639 1439 639 HOH HOH A . V 7 HOH 640 1440 640 HOH HOH A . V 7 HOH 641 1441 641 HOH HOH A . V 7 HOH 642 1442 642 HOH HOH A . V 7 HOH 643 1443 643 HOH HOH A . V 7 HOH 644 1444 644 HOH HOH A . V 7 HOH 645 1445 645 HOH HOH A . V 7 HOH 646 1446 646 HOH HOH A . V 7 HOH 647 1447 647 HOH HOH A . V 7 HOH 648 1448 648 HOH HOH A . V 7 HOH 649 1449 649 HOH HOH A . V 7 HOH 650 1450 650 HOH HOH A . V 7 HOH 651 1451 651 HOH HOH A . V 7 HOH 652 1452 652 HOH HOH A . V 7 HOH 653 1453 653 HOH HOH A . V 7 HOH 654 1454 654 HOH HOH A . V 7 HOH 655 1455 655 HOH HOH A . V 7 HOH 656 1456 656 HOH HOH A . V 7 HOH 657 1457 657 HOH HOH A . V 7 HOH 658 1458 658 HOH HOH A . V 7 HOH 659 1459 659 HOH HOH A . V 7 HOH 660 1460 660 HOH HOH A . V 7 HOH 661 1461 661 HOH HOH A . V 7 HOH 662 1462 662 HOH HOH A . V 7 HOH 663 1463 663 HOH HOH A . V 7 HOH 664 1464 664 HOH HOH A . V 7 HOH 665 1465 665 HOH HOH A . V 7 HOH 666 1466 666 HOH HOH A . V 7 HOH 667 1467 667 HOH HOH A . V 7 HOH 668 1468 668 HOH HOH A . V 7 HOH 669 1469 669 HOH HOH A . V 7 HOH 670 1470 670 HOH HOH A . V 7 HOH 671 1471 671 HOH HOH A . V 7 HOH 672 1472 672 HOH HOH A . V 7 HOH 673 1473 673 HOH HOH A . V 7 HOH 674 1474 674 HOH HOH A . V 7 HOH 675 1475 675 HOH HOH A . V 7 HOH 676 1476 676 HOH HOH A . V 7 HOH 677 1477 677 HOH HOH A . V 7 HOH 678 1478 678 HOH HOH A . V 7 HOH 679 1479 679 HOH HOH A . V 7 HOH 680 1480 680 HOH HOH A . V 7 HOH 681 1481 681 HOH HOH A . V 7 HOH 682 1482 682 HOH HOH A . V 7 HOH 683 1483 683 HOH HOH A . V 7 HOH 684 1484 684 HOH HOH A . V 7 HOH 685 1485 685 HOH HOH A . V 7 HOH 686 1486 686 HOH HOH A . V 7 HOH 687 1487 687 HOH HOH A . V 7 HOH 688 1488 688 HOH HOH A . V 7 HOH 689 1489 689 HOH HOH A . V 7 HOH 690 1490 690 HOH HOH A . V 7 HOH 691 1491 691 HOH HOH A . V 7 HOH 692 1492 692 HOH HOH A . V 7 HOH 693 1493 693 HOH HOH A . V 7 HOH 694 1494 694 HOH HOH A . V 7 HOH 695 1495 695 HOH HOH A . V 7 HOH 696 1496 696 HOH HOH A . V 7 HOH 697 1497 697 HOH HOH A . V 7 HOH 698 1498 698 HOH HOH A . V 7 HOH 699 1499 699 HOH HOH A . V 7 HOH 700 1500 700 HOH HOH A . V 7 HOH 701 1501 701 HOH HOH A . V 7 HOH 702 1502 702 HOH HOH A . V 7 HOH 703 1503 703 HOH HOH A . V 7 HOH 704 1504 704 HOH HOH A . V 7 HOH 705 1505 705 HOH HOH A . V 7 HOH 706 1506 706 HOH HOH A . V 7 HOH 707 1507 707 HOH HOH A . V 7 HOH 708 1508 708 HOH HOH A . V 7 HOH 709 1509 709 HOH HOH A . V 7 HOH 710 1510 710 HOH HOH A . V 7 HOH 711 1511 711 HOH HOH A . V 7 HOH 712 1512 712 HOH HOH A . V 7 HOH 713 1513 713 HOH HOH A . V 7 HOH 714 1514 714 HOH HOH A . V 7 HOH 715 1515 715 HOH HOH A . V 7 HOH 716 1516 716 HOH HOH A . V 7 HOH 717 1517 717 HOH HOH A . V 7 HOH 718 1518 718 HOH HOH A . V 7 HOH 719 1519 719 HOH HOH A . V 7 HOH 720 1520 720 HOH HOH A . V 7 HOH 721 1521 721 HOH HOH A . V 7 HOH 722 1522 722 HOH HOH A . V 7 HOH 723 1523 723 HOH HOH A . V 7 HOH 724 1524 724 HOH HOH A . V 7 HOH 725 1525 725 HOH HOH A . V 7 HOH 726 1526 726 HOH HOH A . V 7 HOH 727 1527 727 HOH HOH A . V 7 HOH 728 1528 728 HOH HOH A . V 7 HOH 729 1529 729 HOH HOH A . V 7 HOH 730 1530 730 HOH HOH A . V 7 HOH 731 1531 731 HOH HOH A . V 7 HOH 732 1532 732 HOH HOH A . V 7 HOH 733 1533 733 HOH HOH A . V 7 HOH 734 1534 734 HOH HOH A . V 7 HOH 735 1535 735 HOH HOH A . V 7 HOH 736 1536 736 HOH HOH A . V 7 HOH 737 1537 737 HOH HOH A . V 7 HOH 738 1538 738 HOH HOH A . V 7 HOH 739 1539 739 HOH HOH A . V 7 HOH 740 1540 740 HOH HOH A . V 7 HOH 741 1541 741 HOH HOH A . V 7 HOH 742 1542 742 HOH HOH A . V 7 HOH 743 1543 743 HOH HOH A . V 7 HOH 744 1544 744 HOH HOH A . V 7 HOH 745 1545 745 HOH HOH A . V 7 HOH 746 1546 746 HOH HOH A . V 7 HOH 747 1547 747 HOH HOH A . V 7 HOH 748 1548 748 HOH HOH A . V 7 HOH 749 1549 749 HOH HOH A . V 7 HOH 750 1550 750 HOH HOH A . V 7 HOH 751 1551 751 HOH HOH A . V 7 HOH 752 1552 752 HOH HOH A . V 7 HOH 753 1553 753 HOH HOH A . V 7 HOH 754 1554 754 HOH HOH A . V 7 HOH 755 1555 755 HOH HOH A . V 7 HOH 756 1556 756 HOH HOH A . V 7 HOH 757 1557 757 HOH HOH A . V 7 HOH 758 1558 758 HOH HOH A . V 7 HOH 759 1559 759 HOH HOH A . V 7 HOH 760 1560 760 HOH HOH A . V 7 HOH 761 1561 761 HOH HOH A . V 7 HOH 762 1562 762 HOH HOH A . V 7 HOH 763 1563 763 HOH HOH A . V 7 HOH 764 1564 764 HOH HOH A . V 7 HOH 765 1565 765 HOH HOH A . V 7 HOH 766 1566 766 HOH HOH A . V 7 HOH 767 1567 767 HOH HOH A . V 7 HOH 768 1568 768 HOH HOH A . V 7 HOH 769 1569 769 HOH HOH A . V 7 HOH 770 1570 770 HOH HOH A . V 7 HOH 771 1571 771 HOH HOH A . V 7 HOH 772 1572 772 HOH HOH A . V 7 HOH 773 1573 773 HOH HOH A . V 7 HOH 774 1574 774 HOH HOH A . V 7 HOH 775 1575 775 HOH HOH A . V 7 HOH 776 1576 776 HOH HOH A . #