data_3WLP # _entry.id 3WLP # _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 3WLP RCSB RCSB096492 WWPDB D_1000096492 # 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 3WLQ . unspecified PDB 3WLR . unspecified PDB 3WLS . unspecified PDB 3WLT . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3WLP _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 3WLP _cell.length_a 99.939 _cell.length_b 99.939 _cell.length_c 182.871 _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 3WLP _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' 65475.617 1 3.2.1.- ? 'UNP RESIDUES 26-630' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 3 non-polymer man 1-THIO-BETA-D-GLUCOPYRANOSE 196.221 1 ? ? ? ? 4 non-polymer man O1-METHYL-GLUCOSE 194.182 1 ? ? ? ? 5 non-polymer syn GLYCEROL 92.094 10 ? ? ? ? 6 non-polymer syn 'SULFATE ION' 96.063 2 ? ? ? ? 7 water nat water 18.015 853 ? ? ? ? # _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 ;DYVLYKDATKPVEDRVADLLGRMTLAEKIGQMTQIERLVATPDVLRDNFIGSLLSGGGSVPRKGATAKEWQDMVDGFQKA CMSTRLGIPMIYGIDAVHGQNNVYGATIFPHNVGLGATRDPYLVKRIGEATALEVRATGIQYAFAPCIAVCRDPRWGRCY ESYSEDRRIVQSMTELIPGLQGDVPKDFTSGMPFVAGKNKVAACAKHFVGDGGTVDGINENNTIINREGLMNIHMPAYKN AMDKGVSTVMISYSSWNGVKMHANQDLVTGYLKDTLKFKGFVISDWEGIDRITTPAGSDYSYSVKASILAGLDMIMVPNK YQQFISILTGHVNGGVIPMSRIDDAVTRILRVKFTMGLFENPYADPAMAEQLGKQEHRDLAREAARKSLVLLKNGKTSTD APLLPLPKKAPKILVAGSHADNLGYQCGGWTIEWQGDTGRTTVGTTILEAVKAAVDPSTVVVFAENPDAEFVKSGGFSYA IVAVGEHPYTETKGDNLNLTIPEPGLSTVQAVCGGVRCATVLISGRPVVVQPLLAASDALVAAWLPGSEGQGVTDALFGD FGFTGRLPRTWFKSVDQLPMNVGDAHYDPLFRLGYGLTTNATKKY ; _entity_poly.pdbx_seq_one_letter_code_can ;DYVLYKDATKPVEDRVADLLGRMTLAEKIGQMTQIERLVATPDVLRDNFIGSLLSGGGSVPRKGATAKEWQDMVDGFQKA CMSTRLGIPMIYGIDAVHGQNNVYGATIFPHNVGLGATRDPYLVKRIGEATALEVRATGIQYAFAPCIAVCRDPRWGRCY ESYSEDRRIVQSMTELIPGLQGDVPKDFTSGMPFVAGKNKVAACAKHFVGDGGTVDGINENNTIINREGLMNIHMPAYKN AMDKGVSTVMISYSSWNGVKMHANQDLVTGYLKDTLKFKGFVISDWEGIDRITTPAGSDYSYSVKASILAGLDMIMVPNK YQQFISILTGHVNGGVIPMSRIDDAVTRILRVKFTMGLFENPYADPAMAEQLGKQEHRDLAREAARKSLVLLKNGKTSTD APLLPLPKKAPKILVAGSHADNLGYQCGGWTIEWQGDTGRTTVGTTILEAVKAAVDPSTVVVFAENPDAEFVKSGGFSYA IVAVGEHPYTETKGDNLNLTIPEPGLSTVQAVCGGVRCATVLISGRPVVVQPLLAASDALVAAWLPGSEGQGVTDALFGD FGFTGRLPRTWFKSVDQLPMNVGDAHYDPLFRLGYGLTTNATKKY ; _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 ASP n 1 2 TYR n 1 3 VAL n 1 4 LEU n 1 5 TYR n 1 6 LYS n 1 7 ASP n 1 8 ALA n 1 9 THR n 1 10 LYS n 1 11 PRO n 1 12 VAL n 1 13 GLU n 1 14 ASP n 1 15 ARG n 1 16 VAL n 1 17 ALA n 1 18 ASP n 1 19 LEU n 1 20 LEU n 1 21 GLY n 1 22 ARG n 1 23 MET n 1 24 THR n 1 25 LEU n 1 26 ALA n 1 27 GLU n 1 28 LYS n 1 29 ILE n 1 30 GLY n 1 31 GLN n 1 32 MET n 1 33 THR n 1 34 GLN n 1 35 ILE n 1 36 GLU n 1 37 ARG n 1 38 LEU n 1 39 VAL n 1 40 ALA n 1 41 THR n 1 42 PRO n 1 43 ASP n 1 44 VAL n 1 45 LEU n 1 46 ARG n 1 47 ASP n 1 48 ASN n 1 49 PHE n 1 50 ILE n 1 51 GLY n 1 52 SER n 1 53 LEU n 1 54 LEU n 1 55 SER n 1 56 GLY n 1 57 GLY n 1 58 GLY n 1 59 SER n 1 60 VAL n 1 61 PRO n 1 62 ARG n 1 63 LYS n 1 64 GLY n 1 65 ALA n 1 66 THR n 1 67 ALA n 1 68 LYS n 1 69 GLU n 1 70 TRP n 1 71 GLN n 1 72 ASP n 1 73 MET n 1 74 VAL n 1 75 ASP n 1 76 GLY n 1 77 PHE n 1 78 GLN n 1 79 LYS n 1 80 ALA n 1 81 CYS n 1 82 MET n 1 83 SER n 1 84 THR n 1 85 ARG n 1 86 LEU n 1 87 GLY n 1 88 ILE n 1 89 PRO n 1 90 MET n 1 91 ILE n 1 92 TYR n 1 93 GLY n 1 94 ILE n 1 95 ASP n 1 96 ALA n 1 97 VAL n 1 98 HIS n 1 99 GLY n 1 100 GLN n 1 101 ASN n 1 102 ASN n 1 103 VAL n 1 104 TYR n 1 105 GLY n 1 106 ALA n 1 107 THR n 1 108 ILE n 1 109 PHE n 1 110 PRO n 1 111 HIS n 1 112 ASN n 1 113 VAL n 1 114 GLY n 1 115 LEU n 1 116 GLY n 1 117 ALA n 1 118 THR n 1 119 ARG n 1 120 ASP n 1 121 PRO n 1 122 TYR n 1 123 LEU n 1 124 VAL n 1 125 LYS n 1 126 ARG n 1 127 ILE n 1 128 GLY n 1 129 GLU n 1 130 ALA n 1 131 THR n 1 132 ALA n 1 133 LEU n 1 134 GLU n 1 135 VAL n 1 136 ARG n 1 137 ALA n 1 138 THR n 1 139 GLY n 1 140 ILE n 1 141 GLN n 1 142 TYR n 1 143 ALA n 1 144 PHE n 1 145 ALA n 1 146 PRO n 1 147 CYS n 1 148 ILE n 1 149 ALA n 1 150 VAL n 1 151 CYS n 1 152 ARG n 1 153 ASP n 1 154 PRO n 1 155 ARG n 1 156 TRP n 1 157 GLY n 1 158 ARG n 1 159 CYS n 1 160 TYR n 1 161 GLU n 1 162 SER n 1 163 TYR n 1 164 SER n 1 165 GLU n 1 166 ASP n 1 167 ARG n 1 168 ARG n 1 169 ILE n 1 170 VAL n 1 171 GLN n 1 172 SER n 1 173 MET n 1 174 THR n 1 175 GLU n 1 176 LEU n 1 177 ILE n 1 178 PRO n 1 179 GLY n 1 180 LEU n 1 181 GLN n 1 182 GLY n 1 183 ASP n 1 184 VAL n 1 185 PRO n 1 186 LYS n 1 187 ASP n 1 188 PHE n 1 189 THR n 1 190 SER n 1 191 GLY n 1 192 MET n 1 193 PRO n 1 194 PHE n 1 195 VAL n 1 196 ALA n 1 197 GLY n 1 198 LYS n 1 199 ASN n 1 200 LYS n 1 201 VAL n 1 202 ALA n 1 203 ALA n 1 204 CYS n 1 205 ALA n 1 206 LYS n 1 207 HIS n 1 208 PHE n 1 209 VAL n 1 210 GLY n 1 211 ASP n 1 212 GLY n 1 213 GLY n 1 214 THR n 1 215 VAL n 1 216 ASP n 1 217 GLY n 1 218 ILE n 1 219 ASN n 1 220 GLU n 1 221 ASN n 1 222 ASN n 1 223 THR n 1 224 ILE n 1 225 ILE n 1 226 ASN n 1 227 ARG n 1 228 GLU n 1 229 GLY n 1 230 LEU n 1 231 MET n 1 232 ASN n 1 233 ILE n 1 234 HIS n 1 235 MET n 1 236 PRO n 1 237 ALA n 1 238 TYR n 1 239 LYS n 1 240 ASN n 1 241 ALA n 1 242 MET n 1 243 ASP n 1 244 LYS n 1 245 GLY n 1 246 VAL n 1 247 SER n 1 248 THR n 1 249 VAL n 1 250 MET n 1 251 ILE n 1 252 SER n 1 253 TYR n 1 254 SER n 1 255 SER n 1 256 TRP n 1 257 ASN n 1 258 GLY n 1 259 VAL n 1 260 LYS n 1 261 MET n 1 262 HIS n 1 263 ALA n 1 264 ASN n 1 265 GLN n 1 266 ASP n 1 267 LEU n 1 268 VAL n 1 269 THR n 1 270 GLY n 1 271 TYR n 1 272 LEU n 1 273 LYS n 1 274 ASP n 1 275 THR n 1 276 LEU n 1 277 LYS n 1 278 PHE n 1 279 LYS n 1 280 GLY n 1 281 PHE n 1 282 VAL n 1 283 ILE n 1 284 SER n 1 285 ASP n 1 286 TRP n 1 287 GLU n 1 288 GLY n 1 289 ILE n 1 290 ASP n 1 291 ARG n 1 292 ILE n 1 293 THR n 1 294 THR n 1 295 PRO n 1 296 ALA n 1 297 GLY n 1 298 SER n 1 299 ASP n 1 300 TYR n 1 301 SER n 1 302 TYR n 1 303 SER n 1 304 VAL n 1 305 LYS n 1 306 ALA n 1 307 SER n 1 308 ILE n 1 309 LEU n 1 310 ALA n 1 311 GLY n 1 312 LEU n 1 313 ASP n 1 314 MET n 1 315 ILE n 1 316 MET n 1 317 VAL n 1 318 PRO n 1 319 ASN n 1 320 LYS n 1 321 TYR n 1 322 GLN n 1 323 GLN n 1 324 PHE n 1 325 ILE n 1 326 SER n 1 327 ILE n 1 328 LEU n 1 329 THR n 1 330 GLY n 1 331 HIS n 1 332 VAL n 1 333 ASN n 1 334 GLY n 1 335 GLY n 1 336 VAL n 1 337 ILE n 1 338 PRO n 1 339 MET n 1 340 SER n 1 341 ARG n 1 342 ILE n 1 343 ASP n 1 344 ASP n 1 345 ALA n 1 346 VAL n 1 347 THR n 1 348 ARG n 1 349 ILE n 1 350 LEU n 1 351 ARG n 1 352 VAL n 1 353 LYS n 1 354 PHE n 1 355 THR n 1 356 MET n 1 357 GLY n 1 358 LEU n 1 359 PHE n 1 360 GLU n 1 361 ASN n 1 362 PRO n 1 363 TYR n 1 364 ALA n 1 365 ASP n 1 366 PRO n 1 367 ALA n 1 368 MET n 1 369 ALA n 1 370 GLU n 1 371 GLN n 1 372 LEU n 1 373 GLY n 1 374 LYS n 1 375 GLN n 1 376 GLU n 1 377 HIS n 1 378 ARG n 1 379 ASP n 1 380 LEU n 1 381 ALA n 1 382 ARG n 1 383 GLU n 1 384 ALA n 1 385 ALA n 1 386 ARG n 1 387 LYS n 1 388 SER n 1 389 LEU n 1 390 VAL n 1 391 LEU n 1 392 LEU n 1 393 LYS n 1 394 ASN n 1 395 GLY n 1 396 LYS n 1 397 THR n 1 398 SER n 1 399 THR n 1 400 ASP n 1 401 ALA n 1 402 PRO n 1 403 LEU n 1 404 LEU n 1 405 PRO n 1 406 LEU n 1 407 PRO n 1 408 LYS n 1 409 LYS n 1 410 ALA n 1 411 PRO n 1 412 LYS n 1 413 ILE n 1 414 LEU n 1 415 VAL n 1 416 ALA n 1 417 GLY n 1 418 SER n 1 419 HIS n 1 420 ALA n 1 421 ASP n 1 422 ASN n 1 423 LEU n 1 424 GLY n 1 425 TYR n 1 426 GLN n 1 427 CYS n 1 428 GLY n 1 429 GLY n 1 430 TRP n 1 431 THR n 1 432 ILE n 1 433 GLU n 1 434 TRP n 1 435 GLN n 1 436 GLY n 1 437 ASP n 1 438 THR n 1 439 GLY n 1 440 ARG n 1 441 THR n 1 442 THR n 1 443 VAL n 1 444 GLY n 1 445 THR n 1 446 THR n 1 447 ILE n 1 448 LEU n 1 449 GLU n 1 450 ALA n 1 451 VAL n 1 452 LYS n 1 453 ALA n 1 454 ALA n 1 455 VAL n 1 456 ASP n 1 457 PRO n 1 458 SER n 1 459 THR n 1 460 VAL n 1 461 VAL n 1 462 VAL n 1 463 PHE n 1 464 ALA n 1 465 GLU n 1 466 ASN n 1 467 PRO n 1 468 ASP n 1 469 ALA n 1 470 GLU n 1 471 PHE n 1 472 VAL n 1 473 LYS n 1 474 SER n 1 475 GLY n 1 476 GLY n 1 477 PHE n 1 478 SER n 1 479 TYR n 1 480 ALA n 1 481 ILE n 1 482 VAL n 1 483 ALA n 1 484 VAL n 1 485 GLY n 1 486 GLU n 1 487 HIS n 1 488 PRO n 1 489 TYR n 1 490 THR n 1 491 GLU n 1 492 THR n 1 493 LYS n 1 494 GLY n 1 495 ASP n 1 496 ASN n 1 497 LEU n 1 498 ASN n 1 499 LEU n 1 500 THR n 1 501 ILE n 1 502 PRO n 1 503 GLU n 1 504 PRO n 1 505 GLY n 1 506 LEU n 1 507 SER n 1 508 THR n 1 509 VAL n 1 510 GLN n 1 511 ALA n 1 512 VAL n 1 513 CYS n 1 514 GLY n 1 515 GLY n 1 516 VAL n 1 517 ARG n 1 518 CYS n 1 519 ALA n 1 520 THR n 1 521 VAL n 1 522 LEU n 1 523 ILE n 1 524 SER n 1 525 GLY n 1 526 ARG n 1 527 PRO n 1 528 VAL n 1 529 VAL n 1 530 VAL n 1 531 GLN n 1 532 PRO n 1 533 LEU n 1 534 LEU n 1 535 ALA n 1 536 ALA n 1 537 SER n 1 538 ASP n 1 539 ALA n 1 540 LEU n 1 541 VAL n 1 542 ALA n 1 543 ALA n 1 544 TRP n 1 545 LEU n 1 546 PRO n 1 547 GLY n 1 548 SER n 1 549 GLU n 1 550 GLY n 1 551 GLN n 1 552 GLY n 1 553 VAL n 1 554 THR n 1 555 ASP n 1 556 ALA n 1 557 LEU n 1 558 PHE n 1 559 GLY n 1 560 ASP n 1 561 PHE n 1 562 GLY n 1 563 PHE n 1 564 THR n 1 565 GLY n 1 566 ARG n 1 567 LEU n 1 568 PRO n 1 569 ARG n 1 570 THR n 1 571 TRP n 1 572 PHE n 1 573 LYS n 1 574 SER n 1 575 VAL n 1 576 ASP n 1 577 GLN n 1 578 LEU n 1 579 PRO n 1 580 MET n 1 581 ASN n 1 582 VAL n 1 583 GLY n 1 584 ASP n 1 585 ALA n 1 586 HIS n 1 587 TYR n 1 588 ASP n 1 589 PRO n 1 590 LEU n 1 591 PHE n 1 592 ARG n 1 593 LEU n 1 594 GLY n 1 595 TYR n 1 596 GLY n 1 597 LEU n 1 598 THR n 1 599 THR n 1 600 ASN n 1 601 ALA n 1 602 THR n 1 603 LYS n 1 604 LYS n 1 605 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 3WLP _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 605 _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 # _struct_ref_seq_dif.align_id 1 _struct_ref_seq_dif.pdbx_pdb_id_code 3WLP _struct_ref_seq_dif.mon_id LYS _struct_ref_seq_dif.pdbx_pdb_strand_id A _struct_ref_seq_dif.seq_num 320 _struct_ref_seq_dif.pdbx_pdb_ins_code ? _struct_ref_seq_dif.pdbx_seq_db_name UNP _struct_ref_seq_dif.pdbx_seq_db_accession_code Q9XEI3 _struct_ref_seq_dif.db_mon_id ASN _struct_ref_seq_dif.pdbx_seq_db_seq_num 345 _struct_ref_seq_dif.details 'SEE REMARK 999' _struct_ref_seq_dif.pdbx_auth_seq_num 320 _struct_ref_seq_dif.pdbx_ordinal 1 # 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 3WLP _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.51 _exptl_crystal.density_percent_sol 64.95 _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 mirrors' # _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 3WLP _reflns.observed_criterion_sigma_I 1.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 26.02 _reflns.d_resolution_high 1.57 _reflns.number_obs 118580 _reflns.number_all 118580 _reflns.percent_possible_obs 97 _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 1.57 _reflns_shell.d_res_low 1.61 _reflns_shell.percent_possible_all 98.2 _reflns_shell.Rmerge_I_obs 0.51 _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.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 3WLP _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 118576 _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 25.41 _refine.ls_d_res_high 1.57 _refine.ls_percent_reflns_obs 97.08 _refine.ls_R_factor_obs 0.16327 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.16222 _refine.ls_R_factor_R_free 0.18296 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 6275 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.969 _refine.correlation_coeff_Fo_to_Fc_free 0.963 _refine.B_iso_mean 23.246 _refine.aniso_B[1][1] -0.01 _refine.aniso_B[2][2] -0.01 _refine.aniso_B[3][3] 0.02 _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 WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' _refine.pdbx_starting_model 1IEQ _refine.pdbx_method_to_determine_struct ? _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 0.063 _refine.pdbx_overall_ESU_R_Free 0.064 _refine.overall_SU_ML 0.036 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 1.806 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_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_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 4566 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 108 _refine_hist.number_atoms_solvent 853 _refine_hist.number_atoms_total 5527 _refine_hist.d_res_high 1.57 _refine_hist.d_res_low 25.41 # 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_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.016 0.019 ? 4825 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.761 1.981 ? 6534 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.444 5.000 ? 602 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 39.282 23.869 ? 199 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 13.067 15.000 ? 796 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 17.401 15.000 ? 32 'X-RAY DIFFRACTION' ? r_chiral_restr 0.129 0.200 ? 745 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.009 0.021 ? 3582 '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 1.488 1.636 ? 2409 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 2.367 2.452 ? 3010 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 2.375 1.940 ? 2416 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined 7.318 16.655 ? 8591 '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 1.573 _refine_ls_shell.d_res_low 1.614 _refine_ls_shell.number_reflns_R_work 8782 _refine_ls_shell.R_factor_R_work 0.180 _refine_ls_shell.percent_reflns_obs 99.24 _refine_ls_shell.R_factor_R_free 0.207 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 503 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_obs ? # _struct.entry_id 3WLP _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 3WLP _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'BETA BARREL, HYDROLASE, GRAIN DEVELOPMENT, Enzyme Function Initiative, Tim Barrel/Beta sheet, N-glycosylation' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 5 ? F N N 5 ? G N N 5 ? H N N 5 ? I N N 5 ? J N N 5 ? K N N 5 ? L N N 5 ? M N N 5 ? N N N 5 ? O N N 6 ? P N N 6 ? Q 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 3 ? ASP A 7 ? VAL A 3 ASP A 7 5 ? 5 HELX_P HELX_P2 2 PRO A 11 ? GLY A 21 ? PRO A 11 GLY A 21 1 ? 11 HELX_P HELX_P3 3 THR A 24 ? MET A 32 ? THR A 24 MET A 32 1 ? 9 HELX_P HELX_P4 4 LEU A 38 ? ALA A 40 ? LEU A 38 ALA A 40 5 ? 3 HELX_P HELX_P5 5 THR A 41 ? ASN A 48 ? THR A 41 ASN A 48 1 ? 8 HELX_P HELX_P6 6 THR A 66 ? SER A 83 ? THR A 66 SER A 83 1 ? 18 HELX_P HELX_P7 7 HIS A 111 ? THR A 118 ? HIS A 111 THR A 118 1 ? 8 HELX_P HELX_P8 8 ASP A 120 ? ALA A 137 ? ASP A 120 ALA A 137 1 ? 18 HELX_P HELX_P9 9 ARG A 158 ? SER A 162 ? ARG A 158 SER A 162 5 ? 5 HELX_P HELX_P10 10 ASP A 166 ? THR A 174 ? ASP A 166 THR A 174 1 ? 9 HELX_P HELX_P11 11 GLU A 175 ? GLY A 182 ? GLU A 175 GLY A 182 1 ? 8 HELX_P HELX_P12 12 THR A 214 ? ILE A 218 ? THR A 214 ILE A 218 5 ? 5 HELX_P HELX_P13 13 ASN A 226 ? HIS A 234 ? ASN A 226 HIS A 234 1 ? 9 HELX_P HELX_P14 14 MET A 235 ? LYS A 244 ? MET A 235 LYS A 244 1 ? 10 HELX_P HELX_P15 15 ASN A 264 ? THR A 269 ? ASN A 264 THR A 269 1 ? 6 HELX_P HELX_P16 16 ILE A 289 ? THR A 293 ? ILE A 289 THR A 293 5 ? 5 HELX_P HELX_P17 17 ASP A 299 ? GLY A 311 ? ASP A 299 GLY A 311 1 ? 13 HELX_P HELX_P18 18 LYS A 320 ? GLY A 334 ? LYS A 320 GLY A 334 1 ? 15 HELX_P HELX_P19 19 PRO A 338 ? MET A 356 ? PRO A 338 MET A 356 1 ? 19 HELX_P HELX_P20 20 ASP A 365 ? LEU A 372 ? ASP A 365 LEU A 372 5 ? 8 HELX_P HELX_P21 21 LYS A 374 ? LEU A 389 ? LYS A 374 LEU A 389 1 ? 16 HELX_P HELX_P22 22 ASN A 422 ? GLY A 428 ? ASN A 422 GLY A 428 1 ? 7 HELX_P HELX_P23 23 THR A 446 ? VAL A 455 ? THR A 446 VAL A 455 1 ? 10 HELX_P HELX_P24 24 ASP A 468 ? GLY A 475 ? ASP A 468 GLY A 475 1 ? 8 HELX_P HELX_P25 25 THR A 490 ? ASP A 495 ? THR A 490 ASP A 495 1 ? 6 HELX_P HELX_P26 26 GLY A 505 ? VAL A 516 ? GLY A 505 VAL A 516 1 ? 12 HELX_P HELX_P27 27 VAL A 530 ? SER A 537 ? VAL A 530 SER A 537 1 ? 8 HELX_P HELX_P28 28 GLY A 550 ? PHE A 558 ? GLY A 550 PHE A 558 1 ? 9 HELX_P HELX_P29 29 SER A 574 ? LEU A 578 ? 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 151 SG ? ? ? 1_555 A CYS 159 SG ? ? A CYS 151 A CYS 159 1_555 ? ? ? ? ? ? ? 2.187 ? disulf2 disulf ? ? A CYS 513 SG ? ? ? 1_555 A CYS 518 SG ? ? A CYS 513 A CYS 518 1_555 ? ? ? ? ? ? ? 2.027 ? covale1 covale ? ? A ASN 600 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 600 A NAG 701 1_555 ? ? ? ? ? ? ? 1.451 ? covale2 covale ? ? C GS1 . S1 ? ? ? 1_555 D MGL . C6 ? ? A GS1 702 A MGL 703 1_555 ? ? ? ? ? ? ? 1.829 ? # 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 145 A . ? ALA 145 A PRO 146 A ? PRO 146 A 1 6.76 2 LYS 206 A . ? LYS 206 A HIS 207 A ? HIS 207 A 1 -9.30 3 PHE 208 A . ? PHE 208 A VAL 209 A ? VAL 209 A 1 -4.31 4 THR 294 A . ? THR 294 A PRO 295 A ? PRO 295 A 1 -3.88 5 VAL 317 A . ? VAL 317 A PRO 318 A ? PRO 318 A 1 -13.55 6 LEU 404 A . ? LEU 404 A PRO 405 A ? PRO 405 A 1 1.45 7 GLU 503 A . ? GLU 503 A PRO 504 A ? PRO 504 A 1 0.09 8 LEU 578 A . ? LEU 578 A PRO 579 A ? PRO 579 A 1 -3.34 # 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 142 ? ALA A 143 ? TYR A 142 ALA A 143 A 2 ILE A 91 ? ILE A 94 ? ILE A 91 ILE A 94 A 3 SER A 52 ? SER A 55 ? SER A 52 SER A 55 A 4 THR A 33 ? GLU A 36 ? THR A 33 GLU A 36 A 5 ILE A 315 ? MET A 316 ? ILE A 315 MET A 316 B 1 CYS A 204 ? PHE A 208 ? CYS A 204 PHE A 208 B 2 THR A 248 ? ILE A 251 ? THR A 248 ILE A 251 B 3 PHE A 281 ? ILE A 283 ? PHE A 281 ILE A 283 C 1 ASN A 222 ? THR A 223 ? ASN A 222 THR A 223 C 2 SER A 255 ? TRP A 256 ? SER A 255 TRP A 256 C 3 VAL A 259 ? LYS A 260 ? VAL A 259 LYS A 260 D 1 VAL A 390 ? ASN A 394 ? VAL A 390 ASN A 394 D 2 ALA A 539 ? TRP A 544 ? ALA A 539 TRP A 544 D 3 CYS A 518 ? ILE A 523 ? CYS A 518 ILE A 523 D 4 ALA A 480 ? GLY A 485 ? ALA A 480 GLY A 485 D 5 LYS A 412 ? ALA A 416 ? LYS A 412 ALA A 416 D 6 VAL A 460 ? ALA A 464 ? 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 142 ? O TYR A 142 N ILE A 94 ? N ILE A 94 A 2 3 O GLY A 93 ? O GLY A 93 N LEU A 53 ? N LEU A 53 A 3 4 O SER A 52 ? O SER A 52 N ILE A 35 ? N ILE A 35 A 4 5 N GLN A 34 ? N GLN A 34 O ILE A 315 ? O ILE A 315 B 1 2 N PHE A 208 ? N PHE A 208 O MET A 250 ? O MET A 250 B 2 3 N VAL A 249 ? N VAL A 249 O ILE A 283 ? O ILE A 283 C 1 2 N THR A 223 ? N THR A 223 O SER A 255 ? O SER A 255 C 2 3 N TRP A 256 ? N TRP A 256 O VAL A 259 ? O VAL A 259 D 1 2 N VAL A 390 ? N VAL A 390 O ALA A 542 ? O ALA A 542 D 2 3 O VAL A 541 ? O VAL A 541 N LEU A 522 ? N LEU A 522 D 3 4 O VAL A 521 ? O VAL A 521 N VAL A 482 ? N VAL A 482 D 4 5 O ALA A 483 ? O ALA A 483 N ALA A 416 ? N ALA A 416 D 5 6 N VAL A 415 ? N VAL A 415 O VAL A 462 ? 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 ? ? ? ? 1 'BINDING SITE FOR RESIDUE GOL A 704' AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE GOL A 705' AC3 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE GOL A 706' AC4 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE GOL A 707' AC5 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE GOL A 708' AC6 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE GOL A 709' AC7 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 710' AC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE GOL A 711' AC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE GOL A 712' BC1 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE GOL A 713' BC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 A 714' BC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 A 715' BC4 Software ? ? ? ? 5 'BINDING SITE FOR MONO-SACCHARIDE NAG A 701 BOUND TO ASN A 600' BC5 Software ? ? ? ? 18 'BINDING SITE FOR DI-SACCHARIDE GS1 A 702 AND MGL A 703' # 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 1 THR A 9 ? THR A 9 . ? 1_555 ? 2 AC2 3 LYS A 279 ? LYS A 279 . ? 1_555 ? 3 AC2 3 HOH Q . ? HOH A 1230 . ? 1_555 ? 4 AC2 3 HOH Q . ? HOH A 1493 . ? 1_555 ? 5 AC3 8 GLN A 435 ? GLN A 435 . ? 1_555 ? 6 AC3 8 ASP A 437 ? ASP A 437 . ? 1_555 ? 7 AC3 8 PRO A 488 ? PRO A 488 . ? 1_555 ? 8 AC3 8 LYS A 493 ? LYS A 493 . ? 1_555 ? 9 AC3 8 HOH Q . ? HOH A 861 . ? 1_555 ? 10 AC3 8 HOH Q . ? HOH A 1256 . ? 1_555 ? 11 AC3 8 HOH Q . ? HOH A 1478 . ? 1_555 ? 12 AC3 8 HOH Q . ? HOH A 1580 . ? 1_555 ? 13 AC4 9 ARG A 158 ? ARG A 158 . ? 1_555 ? 14 AC4 9 HIS A 207 ? HIS A 207 . ? 1_555 ? 15 AC4 9 ASP A 211 ? ASP A 211 . ? 1_555 ? 16 AC4 9 GLU A 220 ? GLU A 220 . ? 1_555 ? 17 AC4 9 SER A 252 ? SER A 252 . ? 1_555 ? 18 AC4 9 TYR A 253 ? TYR A 253 . ? 1_555 ? 19 AC4 9 ASP A 285 ? ASP A 285 . ? 1_555 ? 20 AC4 9 GS1 C . ? GS1 A 702 . ? 1_555 ? 21 AC4 9 HOH Q . ? HOH A 868 . ? 1_555 ? 22 AC5 10 GLU A 449 ? GLU A 449 . ? 6_555 ? 23 AC5 10 ALA A 453 ? ALA A 453 . ? 6_555 ? 24 AC5 10 GLN A 551 ? GLN A 551 . ? 6_555 ? 25 AC5 10 GOL J . ? GOL A 709 . ? 1_555 ? 26 AC5 10 HOH Q . ? HOH A 947 . ? 1_555 ? 27 AC5 10 HOH Q . ? HOH A 1024 . ? 1_555 ? 28 AC5 10 HOH Q . ? HOH A 1093 . ? 1_555 ? 29 AC5 10 HOH Q . ? HOH A 1142 . ? 6_555 ? 30 AC5 10 HOH Q . ? HOH A 1147 . ? 1_555 ? 31 AC5 10 HOH Q . ? HOH A 1235 . ? 6_555 ? 32 AC6 11 GLY A 21 ? GLY A 21 . ? 1_555 ? 33 AC6 11 ARG A 22 ? ARG A 22 . ? 1_555 ? 34 AC6 11 MET A 23 ? MET A 23 . ? 1_555 ? 35 AC6 11 THR A 24 ? THR A 24 . ? 1_555 ? 36 AC6 11 GLU A 449 ? GLU A 449 . ? 6_555 ? 37 AC6 11 GOL I . ? GOL A 708 . ? 1_555 ? 38 AC6 11 HOH Q . ? HOH A 817 . ? 6_555 ? 39 AC6 11 HOH Q . ? HOH A 1334 . ? 6_555 ? 40 AC6 11 HOH Q . ? HOH A 1465 . ? 1_555 ? 41 AC6 11 HOH Q . ? HOH A 1506 . ? 1_555 ? 42 AC6 11 HOH Q . ? HOH A 1557 . ? 1_555 ? 43 AC7 6 PRO A 338 ? PRO A 338 . ? 1_555 ? 44 AC7 6 MET A 339 ? MET A 339 . ? 1_555 ? 45 AC7 6 SER A 340 ? SER A 340 . ? 1_555 ? 46 AC7 6 HOH Q . ? HOH A 815 . ? 8_655 ? 47 AC7 6 HOH Q . ? HOH A 1297 . ? 1_555 ? 48 AC7 6 HOH Q . ? HOH A 1507 . ? 1_555 ? 49 AC8 4 LYS A 10 ? LYS A 10 . ? 1_555 ? 50 AC8 4 PRO A 11 ? PRO A 11 . ? 1_555 ? 51 AC8 4 ASP A 14 ? ASP A 14 . ? 1_555 ? 52 AC8 4 HOH Q . ? HOH A 1430 . ? 1_555 ? 53 AC9 4 LEU A 590 ? LEU A 590 . ? 1_555 ? 54 AC9 4 PHE A 591 ? PHE A 591 . ? 1_555 ? 55 AC9 4 ARG A 592 ? ARG A 592 . ? 1_555 ? 56 AC9 4 HOH Q . ? HOH A 1321 . ? 1_555 ? 57 BC1 7 GLN A 531 ? GLN A 531 . ? 1_555 ? 58 BC1 7 PRO A 532 ? PRO A 532 . ? 1_555 ? 59 BC1 7 HOH Q . ? HOH A 810 . ? 1_555 ? 60 BC1 7 HOH Q . ? HOH A 814 . ? 1_555 ? 61 BC1 7 HOH Q . ? HOH A 1260 . ? 1_555 ? 62 BC1 7 HOH Q . ? HOH A 1279 . ? 1_555 ? 63 BC1 7 HOH Q . ? HOH A 1641 . ? 1_555 ? 64 BC2 4 THR A 294 ? THR A 294 . ? 1_555 ? 65 BC2 4 PRO A 295 ? PRO A 295 . ? 1_555 ? 66 BC2 4 ALA A 296 ? ALA A 296 . ? 1_555 ? 67 BC2 4 HOH Q . ? HOH A 853 . ? 1_555 ? 68 BC3 5 LYS A 305 ? LYS A 305 . ? 8_565 ? 69 BC3 5 HOH Q . ? HOH A 829 . ? 8_565 ? 70 BC3 5 HOH Q . ? HOH A 1129 . ? 1_555 ? 71 BC3 5 HOH Q . ? HOH A 1173 . ? 4_455 ? 72 BC3 5 HOH Q . ? HOH A 1637 . ? 1_555 ? 73 BC4 5 THR A 598 ? THR A 598 . ? 1_555 ? 74 BC4 5 ASN A 600 ? ASN A 600 . ? 1_555 ? 75 BC4 5 HOH Q . ? HOH A 846 . ? 4_455 ? 76 BC4 5 HOH Q . ? HOH A 1370 . ? 4_455 ? 77 BC4 5 HOH Q . ? HOH A 1459 . ? 1_555 ? 78 BC5 18 GLY A 56 ? GLY A 56 . ? 1_555 ? 79 BC5 18 GLY A 57 ? GLY A 57 . ? 1_555 ? 80 BC5 18 ASP A 95 ? ASP A 95 . ? 1_555 ? 81 BC5 18 ARG A 158 ? ARG A 158 . ? 1_555 ? 82 BC5 18 LYS A 206 ? LYS A 206 . ? 1_555 ? 83 BC5 18 HIS A 207 ? HIS A 207 . ? 1_555 ? 84 BC5 18 MET A 250 ? MET A 250 . ? 1_555 ? 85 BC5 18 TYR A 253 ? TYR A 253 . ? 1_555 ? 86 BC5 18 ASP A 285 ? ASP A 285 . ? 1_555 ? 87 BC5 18 TRP A 286 ? TRP A 286 . ? 1_555 ? 88 BC5 18 MET A 316 ? MET A 316 . ? 1_555 ? 89 BC5 18 TRP A 430 ? TRP A 430 . ? 1_555 ? 90 BC5 18 TRP A 434 ? TRP A 434 . ? 1_555 ? 91 BC5 18 GOL H . ? GOL A 707 . ? 1_555 ? 92 BC5 18 HOH Q . ? HOH A 807 . ? 1_555 ? 93 BC5 18 HOH Q . ? HOH A 869 . ? 1_555 ? 94 BC5 18 HOH Q . ? HOH A 1126 . ? 1_555 ? 95 BC5 18 HOH Q . ? HOH A 1221 . ? 1_555 ? # _database_PDB_matrix.entry_id 3WLP _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 3WLP _atom_sites.fract_transf_matrix[1][1] 0.010006 _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] 0.010006 _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] 0.005468 _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 . ASP A 1 1 ? 25.730 8.793 -2.816 1.00 45.74 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? 25.538 7.317 -2.762 1.00 45.45 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? 25.295 6.857 -1.304 1.00 40.76 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? 25.376 7.668 -0.387 1.00 39.67 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? 26.746 6.619 -3.376 1.00 49.34 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? 26.374 5.343 -4.081 1.00 56.43 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? 25.326 5.337 -4.759 1.00 63.77 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? 27.125 4.351 -3.968 1.00 54.10 ? 1 ASP A OD2 1 ATOM 9 N N . TYR A 1 2 ? 24.982 5.574 -1.109 1.00 37.23 ? 2 TYR A N 1 ATOM 10 C CA . TYR A 1 2 ? 24.536 5.066 0.202 1.00 30.47 ? 2 TYR A CA 1 ATOM 11 C C . TYR A 1 2 ? 25.624 5.184 1.284 1.00 28.00 ? 2 TYR A C 1 ATOM 12 O O . TYR A 1 2 ? 26.773 4.788 1.077 1.00 28.46 ? 2 TYR A O 1 ATOM 13 C CB . TYR A 1 2 ? 24.097 3.609 0.091 1.00 32.11 ? 2 TYR A CB 1 ATOM 14 C CG . TYR A 1 2 ? 23.625 2.980 1.400 1.00 28.84 ? 2 TYR A CG 1 ATOM 15 C CD1 . TYR A 1 2 ? 22.322 3.198 1.872 1.00 28.52 ? 2 TYR A CD1 1 ATOM 16 C CD2 . TYR A 1 2 ? 24.457 2.129 2.128 1.00 27.17 ? 2 TYR A CD2 1 ATOM 17 C CE1 . TYR A 1 2 ? 21.885 2.620 3.050 1.00 27.07 ? 2 TYR A CE1 1 ATOM 18 C CE2 . TYR A 1 2 ? 24.031 1.534 3.310 1.00 26.78 ? 2 TYR A CE2 1 ATOM 19 C CZ . TYR A 1 2 ? 22.730 1.784 3.761 1.00 26.51 ? 2 TYR A CZ 1 ATOM 20 O OH . TYR A 1 2 ? 22.288 1.212 4.933 1.00 27.06 ? 2 TYR A OH 1 ATOM 21 N N . VAL A 1 3 ? 25.218 5.710 2.440 1.00 25.18 ? 3 VAL A N 1 ATOM 22 C CA . VAL A 1 3 ? 26.063 5.809 3.615 1.00 23.39 ? 3 VAL A CA 1 ATOM 23 C C . VAL A 1 3 ? 25.254 5.214 4.766 1.00 20.47 ? 3 VAL A C 1 ATOM 24 O O . VAL A 1 3 ? 24.196 5.769 5.109 1.00 22.89 ? 3 VAL A O 1 ATOM 25 C CB . VAL A 1 3 ? 26.401 7.300 3.866 1.00 25.70 ? 3 VAL A CB 1 ATOM 26 C CG1 . VAL A 1 3 ? 27.135 7.505 5.167 1.00 26.96 ? 3 VAL A CG1 1 ATOM 27 C CG2 . VAL A 1 3 ? 27.289 7.794 2.731 1.00 27.05 ? 3 VAL A CG2 1 ATOM 28 N N . LEU A 1 4 ? 25.752 4.130 5.370 1.00 20.16 ? 4 LEU A N 1 ATOM 29 C CA . LEU A 1 4 ? 24.955 3.365 6.369 1.00 19.46 ? 4 LEU A CA 1 ATOM 30 C C . LEU A 1 4 ? 24.491 4.292 7.523 1.00 19.62 ? 4 LEU A C 1 ATOM 31 O O . LEU A 1 4 ? 23.325 4.277 7.937 1.00 19.78 ? 4 LEU A O 1 ATOM 32 C CB . LEU A 1 4 ? 25.763 2.192 6.942 1.00 21.18 ? 4 LEU A CB 1 ATOM 33 C CG . LEU A 1 4 ? 24.932 1.179 7.757 1.00 23.89 ? 4 LEU A CG 1 ATOM 34 C CD1 . LEU A 1 4 ? 25.626 -0.189 7.760 1.00 25.67 ? 4 LEU A CD1 1 ATOM 35 C CD2 . LEU A 1 4 ? 24.719 1.624 9.175 1.00 22.35 ? 4 LEU A CD2 1 ATOM 36 N N . TYR A 1 5 ? 25.378 5.147 8.022 1.00 17.32 ? 5 TYR A N 1 ATOM 37 C CA . TYR A 1 5 ? 24.937 5.980 9.183 1.00 16.72 ? 5 TYR A CA 1 ATOM 38 C C . TYR A 1 5 ? 23.749 6.931 8.897 1.00 16.91 ? 5 TYR A C 1 ATOM 39 O O . TYR A 1 5 ? 23.058 7.358 9.851 1.00 16.50 ? 5 TYR A O 1 ATOM 40 C CB . TYR A 1 5 ? 26.105 6.730 9.848 1.00 15.98 ? 5 TYR A CB 1 ATOM 41 C CG . TYR A 1 5 ? 26.571 8.015 9.146 1.00 15.11 ? 5 TYR A CG 1 ATOM 42 C CD1 . TYR A 1 5 ? 25.994 9.275 9.411 1.00 15.43 ? 5 TYR A CD1 1 ATOM 43 C CD2 . TYR A 1 5 ? 27.666 7.984 8.287 1.00 16.45 ? 5 TYR A CD2 1 ATOM 44 C CE1 . TYR A 1 5 ? 26.455 10.454 8.807 1.00 15.44 ? 5 TYR A CE1 1 ATOM 45 C CE2 . TYR A 1 5 ? 28.135 9.133 7.669 1.00 16.65 ? 5 TYR A CE2 1 ATOM 46 C CZ . TYR A 1 5 ? 27.545 10.376 7.945 1.00 16.94 ? 5 TYR A CZ 1 ATOM 47 O OH . TYR A 1 5 ? 28.023 11.499 7.297 1.00 17.17 ? 5 TYR A OH 1 ATOM 48 N N . LYS A 1 6 ? 23.510 7.253 7.618 1.00 17.19 ? 6 LYS A N 1 ATOM 49 C CA . LYS A 1 6 ? 22.411 8.133 7.217 1.00 18.15 ? 6 LYS A CA 1 ATOM 50 C C . LYS A 1 6 ? 21.098 7.368 7.024 1.00 19.96 ? 6 LYS A C 1 ATOM 51 O O . LYS A 1 6 ? 20.058 7.986 6.772 1.00 22.04 ? 6 LYS A O 1 ATOM 52 C CB . LYS A 1 6 ? 22.785 8.913 5.942 1.00 20.25 ? 6 LYS A CB 1 ATOM 53 C CG . LYS A 1 6 ? 23.888 9.946 6.230 1.00 20.72 ? 6 LYS A CG 1 ATOM 54 C CD . LYS A 1 6 ? 24.180 10.807 5.016 1.00 22.08 ? 6 LYS A CD 1 ATOM 55 C CE . LYS A 1 6 ? 25.387 11.705 5.271 1.00 21.90 ? 6 LYS A CE 1 ATOM 56 N NZ A LYS A 1 6 ? 25.640 12.537 4.058 0.60 27.73 ? 6 LYS A NZ 1 ATOM 57 N NZ B LYS A 1 6 ? 25.016 12.998 5.898 0.40 18.44 ? 6 LYS A NZ 1 ATOM 58 N N . ASP A 1 7 ? 21.162 6.047 7.172 1.00 19.33 ? 7 ASP A N 1 ATOM 59 C CA . ASP A 1 7 ? 19.975 5.181 6.887 1.00 20.48 ? 7 ASP A CA 1 ATOM 60 C C . ASP A 1 7 ? 19.169 4.963 8.176 1.00 20.76 ? 7 ASP A C 1 ATOM 61 O O . ASP A 1 7 ? 19.599 4.226 9.104 1.00 21.10 ? 7 ASP A O 1 ATOM 62 C CB . ASP A 1 7 ? 20.519 3.880 6.259 1.00 20.97 ? 7 ASP A CB 1 ATOM 63 C CG . ASP A 1 7 ? 19.433 2.827 5.973 1.00 21.89 ? 7 ASP A CG 1 ATOM 64 O OD1 . ASP A 1 7 ? 19.816 1.754 5.445 1.00 22.30 ? 7 ASP A OD1 1 ATOM 65 O OD2 . ASP A 1 7 ? 18.254 3.068 6.284 1.00 23.36 ? 7 ASP A OD2 1 ATOM 66 N N . ALA A 1 8 ? 17.995 5.601 8.214 1.00 19.73 ? 8 ALA A N 1 ATOM 67 C CA . ALA A 1 8 ? 17.121 5.578 9.392 1.00 20.48 ? 8 ALA A CA 1 ATOM 68 C C . ALA A 1 8 ? 16.558 4.180 9.731 1.00 22.75 ? 8 ALA A C 1 ATOM 69 O O . ALA A 1 8 ? 16.092 3.945 10.867 1.00 24.65 ? 8 ALA A O 1 ATOM 70 C CB . ALA A 1 8 ? 15.994 6.579 9.204 1.00 19.92 ? 8 ALA A CB 1 ATOM 71 N N . THR A 1 9 ? 16.627 3.258 8.768 1.00 23.72 ? 9 THR A N 1 ATOM 72 C CA . THR A 1 9 ? 16.189 1.891 9.014 1.00 24.66 ? 9 THR A CA 1 ATOM 73 C C . THR A 1 9 ? 17.176 1.020 9.757 1.00 24.73 ? 9 THR A C 1 ATOM 74 O O . THR A 1 9 ? 16.821 -0.079 10.181 1.00 27.07 ? 9 THR A O 1 ATOM 75 C CB . THR A 1 9 ? 15.784 1.151 7.728 1.00 25.58 ? 9 THR A CB 1 ATOM 76 O OG1 . THR A 1 9 ? 16.965 0.743 7.007 1.00 26.54 ? 9 THR A OG1 1 ATOM 77 C CG2 . THR A 1 9 ? 14.867 2.020 6.889 1.00 26.37 ? 9 THR A CG2 1 ATOM 78 N N . LYS A 1 10 ? 18.424 1.474 9.910 1.00 21.79 ? 10 LYS A N 1 ATOM 79 C CA . LYS A 1 10 ? 19.453 0.651 10.530 1.00 21.82 ? 10 LYS A CA 1 ATOM 80 C C . LYS A 1 10 ? 19.484 0.779 12.060 1.00 21.44 ? 10 LYS A C 1 ATOM 81 O O . LYS A 1 10 ? 19.128 1.837 12.591 1.00 21.76 ? 10 LYS A O 1 ATOM 82 C CB . LYS A 1 10 ? 20.828 1.024 9.944 1.00 23.62 ? 10 LYS A CB 1 ATOM 83 C CG . LYS A 1 10 ? 20.989 0.674 8.476 1.00 25.35 ? 10 LYS A CG 1 ATOM 84 C CD . LYS A 1 10 ? 20.993 -0.823 8.307 1.00 28.93 ? 10 LYS A CD 1 ATOM 85 C CE . LYS A 1 10 ? 21.043 -1.176 6.834 1.00 31.29 ? 10 LYS A CE 1 ATOM 86 N NZ . LYS A 1 10 ? 20.924 -2.651 6.730 1.00 37.50 ? 10 LYS A NZ 1 ATOM 87 N N . PRO A 1 11 ? 19.932 -0.280 12.776 1.00 22.60 ? 11 PRO A N 1 ATOM 88 C CA . PRO A 1 11 ? 20.029 -0.234 14.244 1.00 21.88 ? 11 PRO A CA 1 ATOM 89 C C . PRO A 1 11 ? 20.992 0.866 14.685 1.00 20.33 ? 11 PRO A C 1 ATOM 90 O O . PRO A 1 11 ? 22.007 1.123 14.013 1.00 20.10 ? 11 PRO A O 1 ATOM 91 C CB . PRO A 1 11 ? 20.646 -1.591 14.591 1.00 22.85 ? 11 PRO A CB 1 ATOM 92 C CG . PRO A 1 11 ? 20.223 -2.472 13.447 1.00 23.83 ? 11 PRO A CG 1 ATOM 93 C CD . PRO A 1 11 ? 20.380 -1.592 12.260 1.00 23.36 ? 11 PRO A CD 1 ATOM 94 N N . VAL A 1 12 ? 20.671 1.491 15.822 1.00 19.33 ? 12 VAL A N 1 ATOM 95 C CA . VAL A 1 12 ? 21.511 2.579 16.361 1.00 17.87 ? 12 VAL A CA 1 ATOM 96 C C . VAL A 1 12 ? 22.976 2.188 16.482 1.00 19.08 ? 12 VAL A C 1 ATOM 97 O O . VAL A 1 12 ? 23.847 2.941 16.049 1.00 17.49 ? 12 VAL A O 1 ATOM 98 C CB . VAL A 1 12 ? 21.003 3.028 17.759 1.00 18.07 ? 12 VAL A CB 1 ATOM 99 C CG1 . VAL A 1 12 ? 22.029 3.881 18.486 1.00 18.95 ? 12 VAL A CG1 1 ATOM 100 C CG2 . VAL A 1 12 ? 19.676 3.779 17.587 1.00 19.76 ? 12 VAL A CG2 1 ATOM 101 N N . GLU A 1 13 ? 23.269 1.008 17.031 1.00 19.49 ? 13 GLU A N 1 ATOM 102 C CA . GLU A 1 13 ? 24.678 0.653 17.206 1.00 19.57 ? 13 GLU A CA 1 ATOM 103 C C . GLU A 1 13 ? 25.424 0.547 15.887 1.00 19.61 ? 13 GLU A C 1 ATOM 104 O O . GLU A 1 13 ? 26.617 0.899 15.827 1.00 19.27 ? 13 GLU A O 1 ATOM 105 C CB . GLU A 1 13 ? 24.866 -0.661 17.983 1.00 19.49 ? 13 GLU A CB 1 ATOM 106 C CG . GLU A 1 13 ? 24.355 -0.594 19.422 1.00 20.82 ? 13 GLU A CG 1 ATOM 107 C CD . GLU A 1 13 ? 24.981 0.530 20.237 1.00 21.60 ? 13 GLU A CD 1 ATOM 108 O OE1 . GLU A 1 13 ? 24.201 1.295 20.859 1.00 24.00 ? 13 GLU A OE1 1 ATOM 109 O OE2 . GLU A 1 13 ? 26.230 0.661 20.294 1.00 23.13 ? 13 GLU A OE2 1 ATOM 110 N N . ASP A 1 14 ? 24.749 0.043 14.855 1.00 20.17 ? 14 ASP A N 1 ATOM 111 C CA . ASP A 1 14 ? 25.386 -0.027 13.519 1.00 21.05 ? 14 ASP A CA 1 ATOM 112 C C . ASP A 1 14 ? 25.664 1.370 12.946 1.00 19.07 ? 14 ASP A C 1 ATOM 113 O O . ASP A 1 14 ? 26.702 1.617 12.331 1.00 19.80 ? 14 ASP A O 1 ATOM 114 C CB . ASP A 1 14 ? 24.529 -0.829 12.550 1.00 24.37 ? 14 ASP A CB 1 ATOM 115 C CG . ASP A 1 14 ? 24.436 -2.290 12.946 1.00 30.90 ? 14 ASP A CG 1 ATOM 116 O OD1 . ASP A 1 14 ? 25.342 -2.797 13.642 1.00 34.50 ? 14 ASP A OD1 1 ATOM 117 O OD2 . ASP A 1 14 ? 23.449 -2.915 12.569 1.00 36.53 ? 14 ASP A OD2 1 ATOM 118 N N . ARG A 1 15 ? 24.722 2.299 13.156 1.00 18.39 ? 15 ARG A N 1 ATOM 119 C CA . ARG A 1 15 ? 24.901 3.650 12.644 1.00 16.98 ? 15 ARG A CA 1 ATOM 120 C C . ARG A 1 15 ? 26.026 4.355 13.417 1.00 17.06 ? 15 ARG A C 1 ATOM 121 O O . ARG A 1 15 ? 26.847 5.090 12.809 1.00 17.94 ? 15 ARG A O 1 ATOM 122 C CB . ARG A 1 15 ? 23.580 4.438 12.808 1.00 17.66 ? 15 ARG A CB 1 ATOM 123 C CG . ARG A 1 15 ? 22.436 3.870 11.979 1.00 17.16 ? 15 ARG A CG 1 ATOM 124 C CD . ARG A 1 15 ? 21.142 4.649 12.161 1.00 17.91 ? 15 ARG A CD 1 ATOM 125 N NE . ARG A 1 15 ? 21.181 5.939 11.456 1.00 16.41 ? 15 ARG A NE 1 ATOM 126 C CZ . ARG A 1 15 ? 20.213 6.868 11.530 1.00 16.81 ? 15 ARG A CZ 1 ATOM 127 N NH1 . ARG A 1 15 ? 19.109 6.645 12.293 1.00 16.93 ? 15 ARG A NH1 1 ATOM 128 N NH2 . ARG A 1 15 ? 20.315 7.990 10.826 1.00 17.33 ? 15 ARG A NH2 1 ATOM 129 N N . VAL A 1 16 ? 26.062 4.156 14.739 1.00 16.42 ? 16 VAL A N 1 ATOM 130 C CA . VAL A 1 16 ? 27.139 4.755 15.570 1.00 16.59 ? 16 VAL A CA 1 ATOM 131 C C . VAL A 1 16 ? 28.504 4.249 15.072 1.00 16.65 ? 16 VAL A C 1 ATOM 132 O O . VAL A 1 16 ? 29.383 5.040 14.812 1.00 17.52 ? 16 VAL A O 1 ATOM 133 C CB . VAL A 1 16 ? 26.985 4.373 17.058 1.00 16.63 ? 16 VAL A CB 1 ATOM 134 C CG1 . VAL A 1 16 ? 28.210 4.825 17.852 1.00 16.79 ? 16 VAL A CG1 1 ATOM 135 C CG2 . VAL A 1 16 ? 25.731 5.014 17.669 1.00 17.20 ? 16 VAL A CG2 1 ATOM 136 N N . ALA A 1 17 ? 28.616 2.925 14.887 1.00 17.58 ? 17 ALA A N 1 ATOM 137 C CA . ALA A 1 17 ? 29.903 2.370 14.455 1.00 18.27 ? 17 ALA A CA 1 ATOM 138 C C . ALA A 1 17 ? 30.285 2.840 13.051 1.00 18.22 ? 17 ALA A C 1 ATOM 139 O O . ALA A 1 17 ? 31.461 3.155 12.792 1.00 18.79 ? 17 ALA A O 1 ATOM 140 C CB . ALA A 1 17 ? 29.822 0.856 14.499 1.00 18.38 ? 17 ALA A CB 1 ATOM 141 N N . ASP A 1 18 ? 29.315 2.895 12.142 1.00 17.88 ? 18 ASP A N 1 ATOM 142 C CA . ASP A 1 18 ? 29.592 3.335 10.792 1.00 17.16 ? 18 ASP A CA 1 ATOM 143 C C . ASP A 1 18 ? 30.098 4.778 10.730 1.00 17.65 ? 18 ASP A C 1 ATOM 144 O O . ASP A 1 18 ? 31.074 5.093 10.039 1.00 19.98 ? 18 ASP A O 1 ATOM 145 C CB . ASP A 1 18 ? 28.363 3.206 9.921 1.00 19.13 ? 18 ASP A CB 1 ATOM 146 C CG . ASP A 1 18 ? 28.669 3.515 8.493 1.00 19.79 ? 18 ASP A CG 1 ATOM 147 O OD1 . ASP A 1 18 ? 29.312 2.658 7.820 1.00 21.35 ? 18 ASP A OD1 1 ATOM 148 O OD2 . ASP A 1 18 ? 28.292 4.601 8.031 1.00 20.15 ? 18 ASP A OD2 1 ATOM 149 N N . LEU A 1 19 ? 29.440 5.667 11.477 1.00 16.51 ? 19 LEU A N 1 ATOM 150 C CA . LEU A 1 19 ? 29.872 7.064 11.535 1.00 15.02 ? 19 LEU A CA 1 ATOM 151 C C . LEU A 1 19 ? 31.231 7.224 12.223 1.00 15.57 ? 19 LEU A C 1 ATOM 152 O O . LEU A 1 19 ? 32.108 7.888 11.683 1.00 15.40 ? 19 LEU A O 1 ATOM 153 C CB . LEU A 1 19 ? 28.748 7.891 12.225 1.00 15.39 ? 19 LEU A CB 1 ATOM 154 C CG . LEU A 1 19 ? 29.083 9.379 12.389 1.00 14.73 ? 19 LEU A CG 1 ATOM 155 C CD1 . LEU A 1 19 ? 29.580 10.086 11.110 1.00 16.02 ? 19 LEU A CD1 1 ATOM 156 C CD2 . LEU A 1 19 ? 27.834 10.081 12.894 1.00 16.34 ? 19 LEU A CD2 1 ATOM 157 N N . LEU A 1 20 ? 31.398 6.605 13.389 1.00 16.19 ? 20 LEU A N 1 ATOM 158 C CA . LEU A 1 20 ? 32.660 6.735 14.135 1.00 16.77 ? 20 LEU A CA 1 ATOM 159 C C . LEU A 1 20 ? 33.857 6.340 13.275 1.00 17.48 ? 20 LEU A C 1 ATOM 160 O O . LEU A 1 20 ? 34.893 7.015 13.314 1.00 17.38 ? 20 LEU A O 1 ATOM 161 C CB . LEU A 1 20 ? 32.591 5.858 15.390 1.00 17.44 ? 20 LEU A CB 1 ATOM 162 C CG . LEU A 1 20 ? 33.818 5.958 16.321 1.00 17.34 ? 20 LEU A CG 1 ATOM 163 C CD1 . LEU A 1 20 ? 33.936 7.293 17.053 1.00 19.43 ? 20 LEU A CD1 1 ATOM 164 C CD2 . LEU A 1 20 ? 33.746 4.800 17.301 1.00 16.94 ? 20 LEU A CD2 1 ATOM 165 N N . GLY A 1 21 ? 33.670 5.291 12.472 1.00 18.41 ? 21 GLY A N 1 ATOM 166 C CA . GLY A 1 21 ? 34.775 4.764 11.631 1.00 19.44 ? 21 GLY A CA 1 ATOM 167 C C . GLY A 1 21 ? 35.192 5.703 10.526 1.00 19.95 ? 21 GLY A C 1 ATOM 168 O O . GLY A 1 21 ? 36.270 5.532 9.955 1.00 21.99 ? 21 GLY A O 1 ATOM 169 N N . ARG A 1 22 ? 34.385 6.722 10.249 1.00 18.22 ? 22 ARG A N 1 ATOM 170 C CA . ARG A 1 22 ? 34.644 7.704 9.195 1.00 17.38 ? 22 ARG A CA 1 ATOM 171 C C . ARG A 1 22 ? 35.270 8.992 9.723 1.00 17.14 ? 22 ARG A C 1 ATOM 172 O O . ARG A 1 22 ? 35.735 9.831 8.934 1.00 17.59 ? 22 ARG A O 1 ATOM 173 C CB . ARG A 1 22 ? 33.362 8.051 8.464 1.00 17.14 ? 22 ARG A CB 1 ATOM 174 C CG . ARG A 1 22 ? 32.676 6.859 7.830 1.00 19.08 ? 22 ARG A CG 1 ATOM 175 C CD . ARG A 1 22 ? 31.301 7.289 7.349 1.00 18.79 ? 22 ARG A CD 1 ATOM 176 N NE . ARG A 1 22 ? 30.517 6.158 6.860 1.00 19.83 ? 22 ARG A NE 1 ATOM 177 C CZ . ARG A 1 22 ? 30.448 5.738 5.601 1.00 23.17 ? 22 ARG A CZ 1 ATOM 178 N NH1 . ARG A 1 22 ? 31.140 6.356 4.653 1.00 27.30 ? 22 ARG A NH1 1 ATOM 179 N NH2 . ARG A 1 22 ? 29.676 4.685 5.289 1.00 24.33 ? 22 ARG A NH2 1 ATOM 180 N N . MET A 1 23 ? 35.232 9.173 11.044 1.00 17.63 ? 23 MET A N 1 ATOM 181 C CA . MET A 1 23 ? 35.524 10.495 11.628 1.00 16.39 ? 23 MET A CA 1 ATOM 182 C C . MET A 1 23 ? 37.025 10.787 11.821 1.00 16.86 ? 23 MET A C 1 ATOM 183 O O . MET A 1 23 ? 37.768 9.935 12.295 1.00 18.31 ? 23 MET A O 1 ATOM 184 C CB . MET A 1 23 ? 34.827 10.652 12.975 1.00 16.35 ? 23 MET A CB 1 ATOM 185 C CG . MET A 1 23 ? 33.315 10.710 12.793 1.00 15.08 ? 23 MET A CG 1 ATOM 186 S SD . MET A 1 23 ? 32.448 10.672 14.374 1.00 16.09 ? 23 MET A SD 1 ATOM 187 C CE . MET A 1 23 ? 32.755 12.316 14.976 1.00 15.12 ? 23 MET A CE 1 ATOM 188 N N . THR A 1 24 ? 37.428 12.003 11.486 1.00 15.82 ? 24 THR A N 1 ATOM 189 C CA . THR A 1 24 ? 38.777 12.466 11.871 1.00 16.54 ? 24 THR A CA 1 ATOM 190 C C . THR A 1 24 ? 38.863 12.795 13.366 1.00 16.38 ? 24 THR A C 1 ATOM 191 O O . THR A 1 24 ? 37.830 12.884 14.071 1.00 16.70 ? 24 THR A O 1 ATOM 192 C CB . THR A 1 24 ? 39.151 13.732 11.094 1.00 17.34 ? 24 THR A CB 1 ATOM 193 O OG1 . THR A 1 24 ? 38.336 14.827 11.542 1.00 17.11 ? 24 THR A OG1 1 ATOM 194 C CG2 . THR A 1 24 ? 39.030 13.557 9.565 1.00 16.74 ? 24 THR A CG2 1 ATOM 195 N N . LEU A 1 25 ? 40.069 13.039 13.878 1.00 16.74 ? 25 LEU A N 1 ATOM 196 C CA . LEU A 1 25 ? 40.213 13.311 15.280 1.00 16.56 ? 25 LEU A CA 1 ATOM 197 C C . LEU A 1 25 ? 39.527 14.691 15.534 1.00 16.43 ? 25 LEU A C 1 ATOM 198 O O . LEU A 1 25 ? 38.884 14.880 16.582 1.00 16.39 ? 25 LEU A O 1 ATOM 199 C CB . LEU A 1 25 ? 41.713 13.375 15.648 1.00 16.85 ? 25 LEU A CB 1 ATOM 200 C CG . LEU A 1 25 ? 41.966 13.818 17.116 1.00 17.40 ? 25 LEU A CG 1 ATOM 201 C CD1 . LEU A 1 25 ? 41.267 12.868 18.102 1.00 19.16 ? 25 LEU A CD1 1 ATOM 202 C CD2 . LEU A 1 25 ? 43.489 13.885 17.394 1.00 19.63 ? 25 LEU A CD2 1 ATOM 203 N N . ALA A 1 26 ? 39.637 15.636 14.602 1.00 16.68 ? 26 ALA A N 1 ATOM 204 C CA . ALA A 1 26 ? 38.992 16.956 14.766 1.00 15.30 ? 26 ALA A CA 1 ATOM 205 C C . ALA A 1 26 ? 37.467 16.780 14.858 1.00 15.40 ? 26 ALA A C 1 ATOM 206 O O . ALA A 1 26 ? 36.782 17.479 15.662 1.00 15.43 ? 26 ALA A O 1 ATOM 207 C CB . ALA A 1 26 ? 39.335 17.845 13.590 1.00 15.86 ? 26 ALA A CB 1 ATOM 208 N N . GLU A 1 27 ? 36.943 15.874 14.026 1.00 14.86 ? 27 GLU A N 1 ATOM 209 C CA . GLU A 1 27 ? 35.475 15.649 14.034 1.00 14.08 ? 27 GLU A CA 1 ATOM 210 C C . GLU A 1 27 ? 35.059 14.958 15.324 1.00 15.03 ? 27 GLU A C 1 ATOM 211 O O . GLU A 1 27 ? 33.982 15.262 15.919 1.00 15.01 ? 27 GLU A O 1 ATOM 212 C CB . GLU A 1 27 ? 35.010 14.862 12.813 1.00 13.60 ? 27 GLU A CB 1 ATOM 213 C CG . GLU A 1 27 ? 35.057 15.693 11.541 1.00 15.37 ? 27 GLU A CG 1 ATOM 214 C CD . GLU A 1 27 ? 35.073 14.881 10.272 1.00 15.25 ? 27 GLU A CD 1 ATOM 215 O OE1 . GLU A 1 27 ? 35.469 13.698 10.287 1.00 15.61 ? 27 GLU A OE1 1 ATOM 216 O OE2 . GLU A 1 27 ? 34.709 15.484 9.241 1.00 16.08 ? 27 GLU A OE2 1 ATOM 217 N N . LYS A 1 28 ? 35.887 14.044 15.818 1.00 14.80 ? 28 LYS A N 1 ATOM 218 C CA . LYS A 1 28 ? 35.612 13.400 17.116 1.00 15.40 ? 28 LYS A CA 1 ATOM 219 C C . LYS A 1 28 ? 35.650 14.401 18.312 1.00 15.33 ? 28 LYS A C 1 ATOM 220 O O . LYS A 1 28 ? 34.685 14.472 19.138 1.00 14.90 ? 28 LYS A O 1 ATOM 221 C CB . LYS A 1 28 ? 36.629 12.270 17.326 1.00 16.71 ? 28 LYS A CB 1 ATOM 222 C CG . LYS A 1 28 ? 36.353 11.071 16.426 1.00 18.29 ? 28 LYS A CG 1 ATOM 223 C CD . LYS A 1 28 ? 37.445 10.016 16.630 1.00 18.29 ? 28 LYS A CD 1 ATOM 224 C CE . LYS A 1 28 ? 37.227 8.878 15.639 1.00 20.51 ? 28 LYS A CE 1 ATOM 225 N NZ . LYS A 1 28 ? 38.341 7.844 15.795 1.00 19.47 ? 28 LYS A NZ 1 ATOM 226 N N . ILE A 1 29 ? 36.737 15.182 18.419 1.00 15.32 ? 29 ILE A N 1 ATOM 227 C CA . ILE A 1 29 ? 36.876 16.136 19.528 1.00 15.43 ? 29 ILE A CA 1 ATOM 228 C C . ILE A 1 29 ? 35.786 17.204 19.435 1.00 15.94 ? 29 ILE A C 1 ATOM 229 O O . ILE A 1 29 ? 35.238 17.633 20.460 1.00 15.45 ? 29 ILE A O 1 ATOM 230 C CB . ILE A 1 29 ? 38.316 16.691 19.561 1.00 17.15 ? 29 ILE A CB 1 ATOM 231 C CG1 . ILE A 1 29 ? 39.224 15.610 20.123 1.00 16.86 ? 29 ILE A CG1 1 ATOM 232 C CG2 . ILE A 1 29 ? 38.354 17.907 20.443 1.00 18.94 ? 29 ILE A CG2 1 ATOM 233 C CD1 . ILE A 1 29 ? 40.698 15.997 19.963 1.00 18.48 ? 29 ILE A CD1 1 ATOM 234 N N . GLY A 1 30 ? 35.381 17.536 18.207 1.00 15.25 ? 30 GLY A N 1 ATOM 235 C CA . GLY A 1 30 ? 34.243 18.476 18.021 1.00 14.96 ? 30 GLY A CA 1 ATOM 236 C C . GLY A 1 30 ? 32.977 17.960 18.674 1.00 14.19 ? 30 GLY A C 1 ATOM 237 O O . GLY A 1 30 ? 32.253 18.758 19.326 1.00 14.57 ? 30 GLY A O 1 ATOM 238 N N . GLN A 1 31 ? 32.676 16.671 18.506 1.00 14.53 ? 31 GLN A N 1 ATOM 239 C CA . GLN A 1 31 ? 31.438 16.123 19.129 1.00 13.37 ? 31 GLN A CA 1 ATOM 240 C C . GLN A 1 31 ? 31.457 16.271 20.652 1.00 13.91 ? 31 GLN A C 1 ATOM 241 O O . GLN A 1 31 ? 30.409 16.456 21.287 1.00 13.63 ? 31 GLN A O 1 ATOM 242 C CB . GLN A 1 31 ? 31.217 14.653 18.780 1.00 13.80 ? 31 GLN A CB 1 ATOM 243 C CG . GLN A 1 31 ? 30.732 14.440 17.357 1.00 14.10 ? 31 GLN A CG 1 ATOM 244 C CD . GLN A 1 31 ? 29.411 15.135 17.119 1.00 14.35 ? 31 GLN A CD 1 ATOM 245 O OE1 . GLN A 1 31 ? 28.427 14.810 17.798 1.00 15.12 ? 31 GLN A OE1 1 ATOM 246 N NE2 . GLN A 1 31 ? 29.394 16.136 16.221 1.00 14.43 ? 31 GLN A NE2 1 ATOM 247 N N . MET A 1 32 ? 32.652 16.180 21.244 1.00 14.06 ? 32 MET A N 1 ATOM 248 C CA . MET A 1 32 ? 32.803 16.267 22.668 1.00 13.97 ? 32 MET A CA 1 ATOM 249 C C . MET A 1 32 ? 32.757 17.699 23.186 1.00 13.28 ? 32 MET A C 1 ATOM 250 O O . MET A 1 32 ? 32.888 17.905 24.403 1.00 14.81 ? 32 MET A O 1 ATOM 251 C CB . MET A 1 32 ? 34.170 15.657 23.048 1.00 14.06 ? 32 MET A CB 1 ATOM 252 C CG . MET A 1 32 ? 34.280 14.193 22.641 1.00 14.10 ? 32 MET A CG 1 ATOM 253 S SD . MET A 1 32 ? 35.995 13.559 22.916 1.00 15.96 ? 32 MET A SD 1 ATOM 254 C CE . MET A 1 32 ? 36.165 13.656 24.696 1.00 15.33 ? 32 MET A CE 1 ATOM 255 N N . THR A 1 33 ? 32.581 18.697 22.321 1.00 13.19 ? 33 THR A N 1 ATOM 256 C CA . THR A 1 33 ? 32.640 20.105 22.717 1.00 13.58 ? 33 THR A CA 1 ATOM 257 C C . THR A 1 33 ? 31.240 20.748 22.706 1.00 13.12 ? 33 THR A C 1 ATOM 258 O O . THR A 1 33 ? 30.568 20.765 21.635 1.00 13.70 ? 33 THR A O 1 ATOM 259 C CB . THR A 1 33 ? 33.532 20.871 21.705 1.00 14.38 ? 33 THR A CB 1 ATOM 260 O OG1 . THR A 1 33 ? 34.827 20.238 21.688 1.00 14.21 ? 33 THR A OG1 1 ATOM 261 C CG2 . THR A 1 33 ? 33.704 22.315 22.108 1.00 14.47 ? 33 THR A CG2 1 ATOM 262 N N . GLN A 1 34 ? 30.814 21.267 23.870 1.00 12.84 ? 34 GLN A N 1 ATOM 263 C CA . GLN A 1 34 ? 29.559 22.024 23.942 1.00 13.23 ? 34 GLN A CA 1 ATOM 264 C C . GLN A 1 34 ? 29.887 23.482 24.198 1.00 13.62 ? 34 GLN A C 1 ATOM 265 O O . GLN A 1 34 ? 30.696 23.811 25.100 1.00 13.78 ? 34 GLN A O 1 ATOM 266 C CB . GLN A 1 34 ? 28.661 21.482 25.062 1.00 13.63 ? 34 GLN A CB 1 ATOM 267 C CG . GLN A 1 34 ? 27.337 22.275 25.164 1.00 12.61 ? 34 GLN A CG 1 ATOM 268 C CD . GLN A 1 34 ? 26.514 21.794 26.350 1.00 13.21 ? 34 GLN A CD 1 ATOM 269 O OE1 . GLN A 1 34 ? 26.819 22.097 27.494 1.00 13.96 ? 34 GLN A OE1 1 ATOM 270 N NE2 . GLN A 1 34 ? 25.484 20.973 26.074 1.00 13.28 ? 34 GLN A NE2 1 ATOM 271 N N . ILE A 1 35 ? 29.321 24.358 23.391 1.00 12.74 ? 35 ILE A N 1 ATOM 272 C CA . ILE A 1 35 ? 29.616 25.808 23.524 1.00 12.47 ? 35 ILE A CA 1 ATOM 273 C C . ILE A 1 35 ? 28.348 26.627 23.792 1.00 12.81 ? 35 ILE A C 1 ATOM 274 O O . ILE A 1 35 ? 27.237 26.207 23.437 1.00 13.64 ? 35 ILE A O 1 ATOM 275 C CB . ILE A 1 35 ? 30.389 26.379 22.295 1.00 13.01 ? 35 ILE A CB 1 ATOM 276 C CG1 . ILE A 1 35 ? 29.479 26.483 21.039 1.00 12.72 ? 35 ILE A CG1 1 ATOM 277 C CG2 . ILE A 1 35 ? 31.597 25.487 22.048 1.00 14.02 ? 35 ILE A CG2 1 ATOM 278 C CD1 . ILE A 1 35 ? 30.197 27.125 19.834 1.00 14.52 ? 35 ILE A CD1 1 ATOM 279 N N . GLU A 1 36 ? 28.539 27.776 24.420 1.00 13.45 ? 36 GLU A N 1 ATOM 280 C CA . GLU A 1 36 ? 27.406 28.697 24.630 1.00 13.16 ? 36 GLU A CA 1 ATOM 281 C C . GLU A 1 36 ? 26.937 29.292 23.319 1.00 14.20 ? 36 GLU A C 1 ATOM 282 O O . GLU A 1 36 ? 27.726 29.661 22.442 1.00 14.26 ? 36 GLU A O 1 ATOM 283 C CB . GLU A 1 36 ? 27.870 29.857 25.551 1.00 14.48 ? 36 GLU A CB 1 ATOM 284 C CG . GLU A 1 36 ? 27.158 30.016 26.899 1.00 14.46 ? 36 GLU A CG 1 ATOM 285 C CD . GLU A 1 36 ? 25.733 30.539 26.812 1.00 15.48 ? 36 GLU A CD 1 ATOM 286 O OE1 . GLU A 1 36 ? 25.325 31.105 25.772 1.00 15.69 ? 36 GLU A OE1 1 ATOM 287 O OE2 . GLU A 1 36 ? 25.033 30.474 27.848 1.00 15.87 ? 36 GLU A OE2 1 ATOM 288 N N . ARG A 1 37 ? 25.617 29.476 23.169 1.00 13.26 ? 37 ARG A N 1 ATOM 289 C CA . ARG A 1 37 ? 25.152 30.258 22.022 1.00 13.63 ? 37 ARG A CA 1 ATOM 290 C C . ARG A 1 37 ? 25.814 31.646 21.956 1.00 13.41 ? 37 ARG A C 1 ATOM 291 O O . ARG A 1 37 ? 25.968 32.164 20.830 1.00 14.67 ? 37 ARG A O 1 ATOM 292 C CB . ARG A 1 37 ? 23.610 30.419 22.040 1.00 13.02 ? 37 ARG A CB 1 ATOM 293 C CG . ARG A 1 37 ? 23.075 31.040 23.338 1.00 13.53 ? 37 ARG A CG 1 ATOM 294 C CD . ARG A 1 37 ? 21.698 31.686 23.140 1.00 13.54 ? 37 ARG A CD 1 ATOM 295 N NE . ARG A 1 37 ? 21.766 32.887 22.299 1.00 13.52 ? 37 ARG A NE 1 ATOM 296 C CZ . ARG A 1 37 ? 21.975 34.093 22.808 1.00 13.20 ? 37 ARG A CZ 1 ATOM 297 N NH1 . ARG A 1 37 ? 22.132 34.281 24.110 1.00 14.24 ? 37 ARG A NH1 1 ATOM 298 N NH2 . ARG A 1 37 ? 21.978 35.142 21.990 1.00 13.42 ? 37 ARG A NH2 1 ATOM 299 N N . LEU A 1 38 ? 26.222 32.195 23.109 1.00 14.49 ? 38 LEU A N 1 ATOM 300 C CA . LEU A 1 38 ? 26.844 33.540 23.124 1.00 16.21 ? 38 LEU A CA 1 ATOM 301 C C . LEU A 1 38 ? 28.155 33.585 22.361 1.00 17.55 ? 38 LEU A C 1 ATOM 302 O O . LEU A 1 38 ? 28.557 34.700 21.970 1.00 21.25 ? 38 LEU A O 1 ATOM 303 C CB . LEU A 1 38 ? 27.074 33.998 24.576 1.00 17.75 ? 38 LEU A CB 1 ATOM 304 C CG . LEU A 1 38 ? 25.760 34.354 25.304 1.00 20.34 ? 38 LEU A CG 1 ATOM 305 C CD1 . LEU A 1 38 ? 25.963 34.388 26.815 1.00 23.59 ? 38 LEU A CD1 1 ATOM 306 C CD2 . LEU A 1 38 ? 25.239 35.678 24.767 1.00 21.27 ? 38 LEU A CD2 1 ATOM 307 N N . VAL A 1 39 ? 28.834 32.440 22.174 1.00 15.44 ? 39 VAL A N 1 ATOM 308 C CA . VAL A 1 39 ? 30.117 32.438 21.381 1.00 15.85 ? 39 VAL A CA 1 ATOM 309 C C . VAL A 1 39 ? 29.991 31.732 20.032 1.00 15.96 ? 39 VAL A C 1 ATOM 310 O O . VAL A 1 39 ? 30.975 31.575 19.309 1.00 17.35 ? 39 VAL A O 1 ATOM 311 C CB . VAL A 1 39 ? 31.293 31.820 22.199 1.00 16.33 ? 39 VAL A CB 1 ATOM 312 C CG1 . VAL A 1 39 ? 31.526 32.633 23.459 1.00 17.57 ? 39 VAL A CG1 1 ATOM 313 C CG2 . VAL A 1 39 ? 31.016 30.342 22.516 1.00 16.54 ? 39 VAL A CG2 1 ATOM 314 N N . ALA A 1 40 ? 28.772 31.258 19.679 1.00 14.24 ? 40 ALA A N 1 ATOM 315 C CA . ALA A 1 40 ? 28.578 30.476 18.469 1.00 15.05 ? 40 ALA A CA 1 ATOM 316 C C . ALA A 1 40 ? 28.298 31.385 17.283 1.00 16.45 ? 40 ALA A C 1 ATOM 317 O O . ALA A 1 40 ? 27.640 32.416 17.419 1.00 19.12 ? 40 ALA A O 1 ATOM 318 C CB . ALA A 1 40 ? 27.401 29.530 18.631 1.00 15.04 ? 40 ALA A CB 1 ATOM 319 N N . THR A 1 41 ? 28.864 31.003 16.136 1.00 16.30 ? 41 THR A N 1 ATOM 320 C CA . THR A 1 41 ? 28.492 31.559 14.831 1.00 16.75 ? 41 THR A CA 1 ATOM 321 C C . THR A 1 41 ? 28.459 30.411 13.844 1.00 16.51 ? 41 THR A C 1 ATOM 322 O O . THR A 1 41 ? 28.972 29.328 14.127 1.00 17.18 ? 41 THR A O 1 ATOM 323 C CB . THR A 1 41 ? 29.511 32.583 14.318 1.00 16.38 ? 41 THR A CB 1 ATOM 324 O OG1 . THR A 1 41 ? 30.704 31.901 13.930 1.00 18.82 ? 41 THR A OG1 1 ATOM 325 C CG2 . THR A 1 41 ? 29.841 33.670 15.339 1.00 17.72 ? 41 THR A CG2 1 ATOM 326 N N . PRO A 1 42 ? 27.860 30.617 12.662 1.00 17.52 ? 42 PRO A N 1 ATOM 327 C CA . PRO A 1 42 ? 27.851 29.511 11.709 1.00 17.38 ? 42 PRO A CA 1 ATOM 328 C C . PRO A 1 42 ? 29.267 29.025 11.369 1.00 17.27 ? 42 PRO A C 1 ATOM 329 O O . PRO A 1 42 ? 29.496 27.795 11.310 1.00 18.01 ? 42 PRO A O 1 ATOM 330 C CB . PRO A 1 42 ? 27.158 30.124 10.481 1.00 19.75 ? 42 PRO A CB 1 ATOM 331 C CG . PRO A 1 42 ? 26.179 31.072 11.120 1.00 20.49 ? 42 PRO A CG 1 ATOM 332 C CD . PRO A 1 42 ? 26.962 31.723 12.259 1.00 19.30 ? 42 PRO A CD 1 ATOM 333 N N . ASP A 1 43 ? 30.227 29.943 11.198 1.00 18.14 ? 43 ASP A N 1 ATOM 334 C CA . ASP A 1 43 ? 31.582 29.522 10.846 1.00 19.31 ? 43 ASP A CA 1 ATOM 335 C C . ASP A 1 43 ? 32.233 28.775 11.994 1.00 17.30 ? 43 ASP A C 1 ATOM 336 O O . ASP A 1 43 ? 32.921 27.776 11.781 1.00 18.09 ? 43 ASP A O 1 ATOM 337 C CB . ASP A 1 43 ? 32.439 30.755 10.447 1.00 21.16 ? 43 ASP A CB 1 ATOM 338 C CG . ASP A 1 43 ? 32.040 31.337 9.076 1.00 27.92 ? 43 ASP A CG 1 ATOM 339 O OD1 . ASP A 1 43 ? 31.723 30.579 8.143 1.00 29.70 ? 43 ASP A OD1 1 ATOM 340 O OD2 . ASP A 1 43 ? 32.031 32.573 8.940 1.00 33.45 ? 43 ASP A OD2 1 ATOM 341 N N . VAL A 1 44 ? 32.014 29.219 13.250 1.00 16.00 ? 44 VAL A N 1 ATOM 342 C CA . VAL A 1 44 ? 32.630 28.549 14.383 1.00 15.08 ? 44 VAL A CA 1 ATOM 343 C C . VAL A 1 44 ? 32.112 27.103 14.463 1.00 15.51 ? 44 VAL A C 1 ATOM 344 O O . VAL A 1 44 ? 32.821 26.137 14.705 1.00 15.50 ? 44 VAL A O 1 ATOM 345 C CB . VAL A 1 44 ? 32.378 29.347 15.682 1.00 15.60 ? 44 VAL A CB 1 ATOM 346 C CG1 . VAL A 1 44 ? 32.599 28.492 16.923 1.00 15.57 ? 44 VAL A CG1 1 ATOM 347 C CG2 . VAL A 1 44 ? 33.232 30.628 15.692 1.00 16.20 ? 44 VAL A CG2 1 ATOM 348 N N . LEU A 1 45 ? 30.804 26.936 14.282 1.00 14.41 ? 45 LEU A N 1 ATOM 349 C CA . LEU A 1 45 ? 30.202 25.630 14.372 1.00 14.84 ? 45 LEU A CA 1 ATOM 350 C C . LEU A 1 45 ? 30.676 24.649 13.321 1.00 14.82 ? 45 LEU A C 1 ATOM 351 O O . LEU A 1 45 ? 30.888 23.465 13.635 1.00 15.01 ? 45 LEU A O 1 ATOM 352 C CB . LEU A 1 45 ? 28.655 25.760 14.347 1.00 15.22 ? 45 LEU A CB 1 ATOM 353 C CG . LEU A 1 45 ? 28.074 26.462 15.582 1.00 16.29 ? 45 LEU A CG 1 ATOM 354 C CD1 . LEU A 1 45 ? 26.586 26.717 15.292 1.00 16.32 ? 45 LEU A CD1 1 ATOM 355 C CD2 . LEU A 1 45 ? 28.231 25.663 16.877 1.00 16.50 ? 45 LEU A CD2 1 ATOM 356 N N . ARG A 1 46 ? 30.788 25.131 12.082 1.00 15.76 ? 46 ARG A N 1 ATOM 357 C CA . ARG A 1 46 ? 31.270 24.305 10.988 1.00 18.01 ? 46 ARG A CA 1 ATOM 358 C C . ARG A 1 46 ? 32.766 24.025 11.113 1.00 18.01 ? 46 ARG A C 1 ATOM 359 O O . ARG A 1 46 ? 33.220 22.875 11.053 1.00 18.51 ? 46 ARG A O 1 ATOM 360 C CB . ARG A 1 46 ? 31.081 25.120 9.731 1.00 21.80 ? 46 ARG A CB 1 ATOM 361 C CG A ARG A 1 46 ? 31.206 24.322 8.457 0.60 24.41 ? 46 ARG A CG 1 ATOM 362 C CG B ARG A 1 46 ? 29.993 24.715 8.821 0.40 20.16 ? 46 ARG A CG 1 ATOM 363 C CD A ARG A 1 46 ? 31.092 25.235 7.249 0.60 26.80 ? 46 ARG A CD 1 ATOM 364 C CD B ARG A 1 46 ? 30.285 25.380 7.495 0.40 20.05 ? 46 ARG A CD 1 ATOM 365 N NE A ARG A 1 46 ? 29.718 25.699 7.101 0.60 31.77 ? 46 ARG A NE 1 ATOM 366 N NE B ARG A 1 46 ? 30.337 26.832 7.612 0.40 21.22 ? 46 ARG A NE 1 ATOM 367 C CZ A ARG A 1 46 ? 29.309 26.964 7.220 0.60 34.95 ? 46 ARG A CZ 1 ATOM 368 C CZ B ARG A 1 46 ? 29.258 27.618 7.596 0.40 21.19 ? 46 ARG A CZ 1 ATOM 369 N NH1 A ARG A 1 46 ? 28.018 27.245 7.057 0.60 36.54 ? 46 ARG A NH1 1 ATOM 370 N NH1 B ARG A 1 46 ? 29.398 28.937 7.692 0.40 21.38 ? 46 ARG A NH1 1 ATOM 371 N NH2 A ARG A 1 46 ? 30.176 27.946 7.491 0.60 35.27 ? 46 ARG A NH2 1 ATOM 372 N NH2 B ARG A 1 46 ? 28.044 27.081 7.477 0.40 21.53 ? 46 ARG A NH2 1 ATOM 373 N N . ASP A 1 47 ? 33.539 25.085 11.336 1.00 17.96 ? 47 ASP A N 1 ATOM 374 C CA . ASP A 1 47 ? 35.001 24.950 11.326 1.00 19.34 ? 47 ASP A CA 1 ATOM 375 C C . ASP A 1 47 ? 35.548 24.052 12.438 1.00 18.05 ? 47 ASP A C 1 ATOM 376 O O . ASP A 1 47 ? 36.613 23.418 12.299 1.00 21.05 ? 47 ASP A O 1 ATOM 377 C CB . ASP A 1 47 ? 35.665 26.342 11.413 1.00 19.62 ? 47 ASP A CB 1 ATOM 378 C CG . ASP A 1 47 ? 35.460 27.198 10.176 1.00 21.87 ? 47 ASP A CG 1 ATOM 379 O OD1 . ASP A 1 47 ? 35.720 28.414 10.280 1.00 22.73 ? 47 ASP A OD1 1 ATOM 380 O OD2 . ASP A 1 47 ? 35.014 26.719 9.109 1.00 24.16 ? 47 ASP A OD2 1 ATOM 381 N N . ASN A 1 48 ? 34.857 24.047 13.602 1.00 15.29 ? 48 ASN A N 1 ATOM 382 C CA . ASN A 1 48 ? 35.303 23.293 14.742 1.00 15.04 ? 48 ASN A CA 1 ATOM 383 C C . ASN A 1 48 ? 34.475 22.026 14.943 1.00 13.91 ? 48 ASN A C 1 ATOM 384 O O . ASN A 1 48 ? 34.649 21.334 15.960 1.00 14.92 ? 48 ASN A O 1 ATOM 385 C CB . ASN A 1 48 ? 35.225 24.153 16.002 1.00 15.03 ? 48 ASN A CB 1 ATOM 386 C CG . ASN A 1 48 ? 36.175 25.339 15.919 1.00 16.26 ? 48 ASN A CG 1 ATOM 387 O OD1 . ASN A 1 48 ? 37.386 25.170 16.135 1.00 18.88 ? 48 ASN A OD1 1 ATOM 388 N ND2 . ASN A 1 48 ? 35.656 26.522 15.549 1.00 16.82 ? 48 ASN A ND2 1 ATOM 389 N N . PHE A 1 49 ? 33.567 21.739 13.998 1.00 14.51 ? 49 PHE A N 1 ATOM 390 C CA . PHE A 1 49 ? 32.781 20.482 14.011 1.00 14.30 ? 49 PHE A CA 1 ATOM 391 C C . PHE A 1 49 ? 32.059 20.295 15.364 1.00 13.83 ? 49 PHE A C 1 ATOM 392 O O . PHE A 1 49 ? 32.033 19.204 15.951 1.00 13.36 ? 49 PHE A O 1 ATOM 393 C CB . PHE A 1 49 ? 33.700 19.260 13.738 1.00 14.70 ? 49 PHE A CB 1 ATOM 394 C CG . PHE A 1 49 ? 34.485 19.380 12.458 1.00 15.58 ? 49 PHE A CG 1 ATOM 395 C CD1 . PHE A 1 49 ? 33.896 19.170 11.225 1.00 14.56 ? 49 PHE A CD1 1 ATOM 396 C CD2 . PHE A 1 49 ? 35.861 19.680 12.526 1.00 15.78 ? 49 PHE A CD2 1 ATOM 397 C CE1 . PHE A 1 49 ? 34.641 19.270 10.029 1.00 15.40 ? 49 PHE A CE1 1 ATOM 398 C CE2 . PHE A 1 49 ? 36.633 19.787 11.347 1.00 15.77 ? 49 PHE A CE2 1 ATOM 399 C CZ . PHE A 1 49 ? 36.014 19.573 10.097 1.00 15.39 ? 49 PHE A CZ 1 ATOM 400 N N . ILE A 1 50 ? 31.514 21.401 15.874 1.00 13.69 ? 50 ILE A N 1 ATOM 401 C CA . ILE A 1 50 ? 30.936 21.404 17.238 1.00 13.17 ? 50 ILE A CA 1 ATOM 402 C C . ILE A 1 50 ? 29.792 20.417 17.389 1.00 13.03 ? 50 ILE A C 1 ATOM 403 O O . ILE A 1 50 ? 28.887 20.316 16.523 1.00 14.00 ? 50 ILE A O 1 ATOM 404 C CB . ILE A 1 50 ? 30.470 22.848 17.587 1.00 13.19 ? 50 ILE A CB 1 ATOM 405 C CG1 . ILE A 1 50 ? 31.683 23.813 17.659 1.00 14.04 ? 50 ILE A CG1 1 ATOM 406 C CG2 . ILE A 1 50 ? 29.661 22.960 18.905 1.00 12.75 ? 50 ILE A CG2 1 ATOM 407 C CD1 . ILE A 1 50 ? 32.818 23.435 18.629 1.00 13.69 ? 50 ILE A CD1 1 ATOM 408 N N . GLY A 1 51 ? 29.779 19.770 18.552 1.00 12.85 ? 51 GLY A N 1 ATOM 409 C CA . GLY A 1 51 ? 28.738 18.725 18.817 1.00 13.10 ? 51 GLY A CA 1 ATOM 410 C C . GLY A 1 51 ? 27.489 19.224 19.531 1.00 13.04 ? 51 GLY A C 1 ATOM 411 O O . GLY A 1 51 ? 26.444 18.597 19.448 1.00 13.11 ? 51 GLY A O 1 ATOM 412 N N . SER A 1 52 ? 27.583 20.318 20.273 1.00 12.66 ? 52 SER A N 1 ATOM 413 C CA . SER A 1 52 ? 26.438 20.739 21.076 1.00 12.58 ? 52 SER A CA 1 ATOM 414 C C . SER A 1 52 ? 26.526 22.216 21.387 1.00 12.51 ? 52 SER A C 1 ATOM 415 O O . SER A 1 52 ? 27.612 22.794 21.457 1.00 12.05 ? 52 SER A O 1 ATOM 416 C CB . SER A 1 52 ? 26.441 19.912 22.385 1.00 13.13 ? 52 SER A CB 1 ATOM 417 O OG . SER A 1 52 ? 25.328 20.236 23.229 1.00 12.61 ? 52 SER A OG 1 ATOM 418 N N . LEU A 1 53 ? 25.349 22.821 21.609 1.00 12.84 ? 53 LEU A N 1 ATOM 419 C CA . LEU A 1 53 ? 25.255 24.172 22.110 1.00 13.57 ? 53 LEU A CA 1 ATOM 420 C C . LEU A 1 53 ? 24.397 24.164 23.353 1.00 12.45 ? 53 LEU A C 1 ATOM 421 O O . LEU A 1 53 ? 23.637 23.210 23.579 1.00 12.72 ? 53 LEU A O 1 ATOM 422 C CB . LEU A 1 53 ? 24.556 25.091 21.121 1.00 15.71 ? 53 LEU A CB 1 ATOM 423 C CG . LEU A 1 53 ? 25.492 25.467 19.956 1.00 17.95 ? 53 LEU A CG 1 ATOM 424 C CD1 . LEU A 1 53 ? 25.266 24.518 18.803 1.00 20.43 ? 53 LEU A CD1 1 ATOM 425 C CD2 . LEU A 1 53 ? 25.253 26.899 19.552 1.00 21.64 ? 53 LEU A CD2 1 ATOM 426 N N . LEU A 1 54 ? 24.573 25.200 24.187 1.00 11.99 ? 54 LEU A N 1 ATOM 427 C CA . LEU A 1 54 ? 23.584 25.422 25.269 1.00 11.27 ? 54 LEU A CA 1 ATOM 428 C C . LEU A 1 54 ? 23.252 26.877 25.420 1.00 12.48 ? 54 LEU A C 1 ATOM 429 O O . LEU A 1 54 ? 24.009 27.771 25.018 1.00 12.79 ? 54 LEU A O 1 ATOM 430 C CB . LEU A 1 54 ? 24.080 24.900 26.659 1.00 12.39 ? 54 LEU A CB 1 ATOM 431 C CG . LEU A 1 54 ? 25.029 25.791 27.457 1.00 11.85 ? 54 LEU A CG 1 ATOM 432 C CD1 . LEU A 1 54 ? 24.966 25.446 28.938 1.00 13.14 ? 54 LEU A CD1 1 ATOM 433 C CD2 . LEU A 1 54 ? 26.496 25.618 26.955 1.00 12.63 ? 54 LEU A CD2 1 ATOM 434 N N . SER A 1 55 ? 22.096 27.101 26.047 1.00 12.18 ? 55 SER A N 1 ATOM 435 C CA . SER A 1 55 ? 21.828 28.372 26.757 1.00 12.03 ? 55 SER A CA 1 ATOM 436 C C . SER A 1 55 ? 22.033 28.111 28.223 1.00 13.31 ? 55 SER A C 1 ATOM 437 O O . SER A 1 55 ? 21.283 27.317 28.814 1.00 13.56 ? 55 SER A O 1 ATOM 438 C CB . SER A 1 55 ? 20.341 28.780 26.575 1.00 12.36 ? 55 SER A CB 1 ATOM 439 O OG . SER A 1 55 ? 20.130 29.387 25.285 1.00 13.09 ? 55 SER A OG 1 ATOM 440 N N . GLY A 1 56 ? 23.017 28.790 28.826 1.00 13.12 ? 56 GLY A N 1 ATOM 441 C CA . GLY A 1 56 ? 23.090 28.837 30.309 1.00 13.01 ? 56 GLY A CA 1 ATOM 442 C C . GLY A 1 56 ? 21.934 29.678 30.830 1.00 12.97 ? 56 GLY A C 1 ATOM 443 O O . GLY A 1 56 ? 21.121 30.247 30.073 1.00 13.88 ? 56 GLY A O 1 ATOM 444 N N . GLY A 1 57 ? 21.871 29.813 32.148 1.00 13.55 ? 57 GLY A N 1 ATOM 445 C CA . GLY A 1 57 ? 20.759 30.600 32.742 1.00 13.58 ? 57 GLY A CA 1 ATOM 446 C C . GLY A 1 57 ? 20.732 32.026 32.210 1.00 13.54 ? 57 GLY A C 1 ATOM 447 O O . GLY A 1 57 ? 21.764 32.732 32.231 1.00 15.73 ? 57 GLY A O 1 ATOM 448 N N . GLY A 1 58 ? 19.579 32.434 31.679 1.00 13.52 ? 58 GLY A N 1 ATOM 449 C CA . GLY A 1 58 ? 19.431 33.769 31.151 1.00 13.30 ? 58 GLY A CA 1 ATOM 450 C C . GLY A 1 58 ? 20.005 33.997 29.746 1.00 14.04 ? 58 GLY A C 1 ATOM 451 O O . GLY A 1 58 ? 19.968 35.112 29.241 1.00 16.63 ? 58 GLY A O 1 ATOM 452 N N . SER A 1 59 ? 20.526 32.964 29.087 1.00 12.84 ? 59 SER A N 1 ATOM 453 C CA . SER A 1 59 ? 21.110 33.116 27.738 1.00 13.12 ? 59 SER A CA 1 ATOM 454 C C . SER A 1 59 ? 20.035 32.952 26.672 1.00 12.91 ? 59 SER A C 1 ATOM 455 O O . SER A 1 59 ? 19.599 31.834 26.340 1.00 14.44 ? 59 SER A O 1 ATOM 456 C CB . SER A 1 59 ? 22.262 32.126 27.562 1.00 13.94 ? 59 SER A CB 1 ATOM 457 O OG . SER A 1 59 ? 22.844 32.336 26.248 1.00 14.06 ? 59 SER A OG 1 ATOM 458 N N . VAL A 1 60 ? 19.569 34.101 26.170 1.00 13.42 ? 60 VAL A N 1 ATOM 459 C CA . VAL A 1 60 ? 18.383 34.129 25.320 1.00 13.39 ? 60 VAL A CA 1 ATOM 460 C C . VAL A 1 60 ? 18.625 34.990 24.057 1.00 14.95 ? 60 VAL A C 1 ATOM 461 O O . VAL A 1 60 ? 19.445 35.893 24.098 1.00 15.47 ? 60 VAL A O 1 ATOM 462 C CB . VAL A 1 60 ? 17.114 34.645 26.105 1.00 12.92 ? 60 VAL A CB 1 ATOM 463 C CG1 . VAL A 1 60 ? 16.853 33.804 27.340 1.00 13.54 ? 60 VAL A CG1 1 ATOM 464 C CG2 . VAL A 1 60 ? 17.275 36.104 26.513 1.00 13.97 ? 60 VAL A CG2 1 ATOM 465 N N . PRO A 1 61 ? 17.930 34.710 22.949 1.00 15.43 ? 61 PRO A N 1 ATOM 466 C CA . PRO A 1 61 ? 18.251 35.502 21.732 1.00 14.92 ? 61 PRO A CA 1 ATOM 467 C C . PRO A 1 61 ? 17.813 36.941 21.893 1.00 15.16 ? 61 PRO A C 1 ATOM 468 O O . PRO A 1 61 ? 18.456 37.831 21.322 1.00 15.61 ? 61 PRO A O 1 ATOM 469 C CB . PRO A 1 61 ? 17.493 34.741 20.615 1.00 15.60 ? 61 PRO A CB 1 ATOM 470 C CG . PRO A 1 61 ? 16.411 33.941 21.342 1.00 13.94 ? 61 PRO A CG 1 ATOM 471 C CD . PRO A 1 61 ? 17.052 33.545 22.666 1.00 13.55 ? 61 PRO A CD 1 ATOM 472 N N . ARG A 1 62 ? 16.734 37.200 22.635 1.00 15.77 ? 62 ARG A N 1 ATOM 473 C CA . ARG A 1 62 ? 16.459 38.563 23.187 1.00 18.04 ? 62 ARG A CA 1 ATOM 474 C C . ARG A 1 62 ? 15.400 38.420 24.229 1.00 18.12 ? 62 ARG A C 1 ATOM 475 O O . ARG A 1 62 ? 14.689 37.398 24.265 1.00 17.62 ? 62 ARG A O 1 ATOM 476 C CB . ARG A 1 62 ? 15.980 39.524 22.181 1.00 20.75 ? 62 ARG A CB 1 ATOM 477 C CG . ARG A 1 62 ? 14.754 39.152 21.464 1.00 19.40 ? 62 ARG A CG 1 ATOM 478 C CD . ARG A 1 62 ? 14.353 40.346 20.621 1.00 26.06 ? 62 ARG A CD 1 ATOM 479 N NE . ARG A 1 62 ? 13.070 40.019 20.045 1.00 27.85 ? 62 ARG A NE 1 ATOM 480 C CZ . ARG A 1 62 ? 12.274 40.921 19.496 1.00 26.98 ? 62 ARG A CZ 1 ATOM 481 N NH1 . ARG A 1 62 ? 12.643 42.210 19.434 1.00 30.28 ? 62 ARG A NH1 1 ATOM 482 N NH2 . ARG A 1 62 ? 11.127 40.526 19.050 1.00 23.86 ? 62 ARG A NH2 1 ATOM 483 N N . LYS A 1 63 ? 15.272 39.469 25.051 1.00 20.04 ? 63 LYS A N 1 ATOM 484 C CA . LYS A 1 63 ? 14.187 39.469 26.025 1.00 20.47 ? 63 LYS A CA 1 ATOM 485 C C . LYS A 1 63 ? 12.848 39.439 25.321 1.00 18.19 ? 63 LYS A C 1 ATOM 486 O O . LYS A 1 63 ? 12.657 40.105 24.331 1.00 18.44 ? 63 LYS A O 1 ATOM 487 C CB . LYS A 1 63 ? 14.245 40.777 26.846 1.00 25.78 ? 63 LYS A CB 1 ATOM 488 C CG . LYS A 1 63 ? 15.566 41.001 27.562 1.00 32.57 ? 63 LYS A CG 1 ATOM 489 C CD . LYS A 1 63 ? 15.911 39.859 28.496 1.00 32.22 ? 63 LYS A CD 1 ATOM 490 C CE . LYS A 1 63 ? 14.915 39.716 29.636 1.00 33.84 ? 63 LYS A CE 1 ATOM 491 N NZ . LYS A 1 63 ? 15.503 39.290 30.938 1.00 29.63 ? 63 LYS A NZ 1 ATOM 492 N N . GLY A 1 64 ? 11.918 38.628 25.847 1.00 16.65 ? 64 GLY A N 1 ATOM 493 C CA . GLY A 1 64 ? 10.572 38.598 25.259 1.00 16.14 ? 64 GLY A CA 1 ATOM 494 C C . GLY A 1 64 ? 10.480 37.803 23.963 1.00 14.90 ? 64 GLY A C 1 ATOM 495 O O . GLY A 1 64 ? 9.446 37.862 23.299 1.00 17.23 ? 64 GLY A O 1 ATOM 496 N N . ALA A 1 65 ? 11.571 37.117 23.575 1.00 15.10 ? 65 ALA A N 1 ATOM 497 C CA . ALA A 1 65 ? 11.579 36.384 22.291 1.00 14.88 ? 65 ALA A CA 1 ATOM 498 C C . ALA A 1 65 ? 10.401 35.406 22.180 1.00 14.24 ? 65 ALA A C 1 ATOM 499 O O . ALA A 1 65 ? 10.039 34.693 23.144 1.00 15.35 ? 65 ALA A O 1 ATOM 500 C CB . ALA A 1 65 ? 12.899 35.626 22.107 1.00 14.96 ? 65 ALA A CB 1 ATOM 501 N N . THR A 1 66 ? 9.781 35.360 21.010 1.00 13.70 ? 66 THR A N 1 ATOM 502 C CA . THR A 1 66 ? 8.711 34.370 20.777 1.00 14.34 ? 66 THR A CA 1 ATOM 503 C C . THR A 1 66 ? 9.267 32.962 20.606 1.00 14.29 ? 66 THR A C 1 ATOM 504 O O . THR A 1 66 ? 10.482 32.744 20.405 1.00 14.09 ? 66 THR A O 1 ATOM 505 C CB . THR A 1 66 ? 7.927 34.687 19.510 1.00 15.33 ? 66 THR A CB 1 ATOM 506 O OG1 . THR A 1 66 ? 8.792 34.533 18.389 1.00 15.77 ? 66 THR A OG1 1 ATOM 507 C CG2 . THR A 1 66 ? 7.366 36.149 19.527 1.00 15.85 ? 66 THR A CG2 1 ATOM 508 N N . ALA A 1 67 ? 8.385 31.976 20.655 1.00 13.73 ? 67 ALA A N 1 ATOM 509 C CA . ALA A 1 67 ? 8.793 30.592 20.363 1.00 13.51 ? 67 ALA A CA 1 ATOM 510 C C . ALA A 1 67 ? 9.441 30.476 18.984 1.00 13.76 ? 67 ALA A C 1 ATOM 511 O O . ALA A 1 67 ? 10.443 29.755 18.855 1.00 13.66 ? 67 ALA A O 1 ATOM 512 C CB . ALA A 1 67 ? 7.584 29.630 20.512 1.00 15.47 ? 67 ALA A CB 1 ATOM 513 N N . LYS A 1 68 ? 8.846 31.104 17.971 1.00 13.72 ? 68 LYS A N 1 ATOM 514 C CA . LYS A 1 68 ? 9.416 31.086 16.625 1.00 13.87 ? 68 LYS A CA 1 ATOM 515 C C . LYS A 1 68 ? 10.825 31.699 16.591 1.00 14.23 ? 68 LYS A C 1 ATOM 516 O O . LYS A 1 68 ? 11.702 31.174 15.879 1.00 14.16 ? 68 LYS A O 1 ATOM 517 C CB . LYS A 1 68 ? 8.465 31.813 15.604 1.00 16.17 ? 68 LYS A CB 1 ATOM 518 C CG A LYS A 1 68 ? 8.956 31.705 14.135 0.60 19.30 ? 68 LYS A CG 1 ATOM 519 C CG B LYS A 1 68 ? 9.067 32.213 14.259 0.40 16.77 ? 68 LYS A CG 1 ATOM 520 C CD A LYS A 1 68 ? 8.839 30.291 13.556 0.60 21.13 ? 68 LYS A CD 1 ATOM 521 C CD B LYS A 1 68 ? 8.014 32.812 13.315 0.40 16.72 ? 68 LYS A CD 1 ATOM 522 C CE A LYS A 1 68 ? 8.745 30.188 12.026 0.60 21.64 ? 68 LYS A CE 1 ATOM 523 C CE B LYS A 1 68 ? 7.351 31.746 12.430 0.40 17.74 ? 68 LYS A CE 1 ATOM 524 N NZ A LYS A 1 68 ? 9.967 29.574 11.475 0.60 25.62 ? 68 LYS A NZ 1 ATOM 525 N NZ B LYS A 1 68 ? 6.118 32.089 11.621 0.40 16.95 ? 68 LYS A NZ 1 ATOM 526 N N . GLU A 1 69 ? 11.068 32.767 17.350 1.00 14.05 ? 69 GLU A N 1 ATOM 527 C CA . GLU A 1 69 ? 12.418 33.329 17.438 1.00 13.52 ? 69 GLU A CA 1 ATOM 528 C C . GLU A 1 69 ? 13.403 32.294 17.979 1.00 13.73 ? 69 GLU A C 1 ATOM 529 O O . GLU A 1 69 ? 14.557 32.201 17.466 1.00 14.20 ? 69 GLU A O 1 ATOM 530 C CB . GLU A 1 69 ? 12.461 34.563 18.335 1.00 15.03 ? 69 GLU A CB 1 ATOM 531 C CG . GLU A 1 69 ? 11.854 35.791 17.683 1.00 15.71 ? 69 GLU A CG 1 ATOM 532 C CD . GLU A 1 69 ? 11.928 37.000 18.621 1.00 16.65 ? 69 GLU A CD 1 ATOM 533 O OE1 . GLU A 1 69 ? 10.863 37.518 19.029 1.00 18.38 ? 69 GLU A OE1 1 ATOM 534 O OE2 . GLU A 1 69 ? 13.053 37.407 18.949 1.00 17.62 ? 69 GLU A OE2 1 ATOM 535 N N . TRP A 1 70 ? 13.027 31.554 19.027 1.00 13.58 ? 70 TRP A N 1 ATOM 536 C CA . TRP A 1 70 ? 13.938 30.518 19.516 1.00 12.64 ? 70 TRP A CA 1 ATOM 537 C C . TRP A 1 70 ? 14.151 29.440 18.470 1.00 12.68 ? 70 TRP A C 1 ATOM 538 O O . TRP A 1 70 ? 15.291 29.017 18.254 1.00 12.60 ? 70 TRP A O 1 ATOM 539 C CB . TRP A 1 70 ? 13.337 29.893 20.805 1.00 12.73 ? 70 TRP A CB 1 ATOM 540 C CG . TRP A 1 70 ? 13.547 30.684 22.032 1.00 12.74 ? 70 TRP A CG 1 ATOM 541 C CD1 . TRP A 1 70 ? 12.700 31.648 22.566 1.00 12.93 ? 70 TRP A CD1 1 ATOM 542 C CD2 . TRP A 1 70 ? 14.622 30.547 22.973 1.00 11.86 ? 70 TRP A CD2 1 ATOM 543 N NE1 . TRP A 1 70 ? 13.200 32.131 23.749 1.00 12.38 ? 70 TRP A NE1 1 ATOM 544 C CE2 . TRP A 1 70 ? 14.376 31.475 24.033 1.00 12.32 ? 70 TRP A CE2 1 ATOM 545 C CE3 . TRP A 1 70 ? 15.772 29.729 23.028 1.00 12.42 ? 70 TRP A CE3 1 ATOM 546 C CZ2 . TRP A 1 70 ? 15.223 31.591 25.143 1.00 12.80 ? 70 TRP A CZ2 1 ATOM 547 C CZ3 . TRP A 1 70 ? 16.608 29.843 24.112 1.00 13.16 ? 70 TRP A CZ3 1 ATOM 548 C CH2 . TRP A 1 70 ? 16.357 30.795 25.154 1.00 12.40 ? 70 TRP A CH2 1 ATOM 549 N N . GLN A 1 71 ? 13.078 29.019 17.777 1.00 12.60 ? 71 GLN A N 1 ATOM 550 C CA . GLN A 1 71 ? 13.235 27.969 16.734 1.00 12.24 ? 71 GLN A CA 1 ATOM 551 C C . GLN A 1 71 ? 14.173 28.478 15.640 1.00 12.99 ? 71 GLN A C 1 ATOM 552 O O . GLN A 1 71 ? 15.033 27.685 15.165 1.00 14.13 ? 71 GLN A O 1 ATOM 553 C CB . GLN A 1 71 ? 11.883 27.639 16.081 1.00 12.69 ? 71 GLN A CB 1 ATOM 554 C CG . GLN A 1 71 ? 10.951 26.897 17.039 1.00 13.87 ? 71 GLN A CG 1 ATOM 555 C CD . GLN A 1 71 ? 9.808 26.172 16.313 1.00 15.29 ? 71 GLN A CD 1 ATOM 556 O OE1 . GLN A 1 71 ? 8.890 25.603 16.979 1.00 17.73 ? 71 GLN A OE1 1 ATOM 557 N NE2 . GLN A 1 71 ? 9.820 26.187 15.009 1.00 14.60 ? 71 GLN A NE2 1 ATOM 558 N N . ASP A 1 72 ? 14.051 29.758 15.258 1.00 13.76 ? 72 ASP A N 1 ATOM 559 C CA . ASP A 1 72 ? 14.917 30.294 14.172 1.00 13.68 ? 72 ASP A CA 1 ATOM 560 C C . ASP A 1 72 ? 16.378 30.338 14.619 1.00 13.80 ? 72 ASP A C 1 ATOM 561 O O . ASP A 1 72 ? 17.282 30.067 13.802 1.00 15.16 ? 72 ASP A O 1 ATOM 562 C CB . ASP A 1 72 ? 14.397 31.665 13.709 1.00 16.46 ? 72 ASP A CB 1 ATOM 563 C CG . ASP A 1 72 ? 13.029 31.561 13.003 1.00 15.95 ? 72 ASP A CG 1 ATOM 564 O OD1 . ASP A 1 72 ? 12.570 30.457 12.631 1.00 20.12 ? 72 ASP A OD1 1 ATOM 565 O OD2 . ASP A 1 72 ? 12.475 32.632 12.798 1.00 21.78 ? 72 ASP A OD2 1 ATOM 566 N N . MET A 1 73 ? 16.621 30.682 15.870 1.00 13.10 ? 73 MET A N 1 ATOM 567 C CA . MET A 1 73 ? 17.980 30.639 16.423 1.00 12.58 ? 73 MET A CA 1 ATOM 568 C C . MET A 1 73 ? 18.536 29.231 16.371 1.00 13.30 ? 73 MET A C 1 ATOM 569 O O . MET A 1 73 ? 19.668 29.003 15.873 1.00 13.51 ? 73 MET A O 1 ATOM 570 C CB . MET A 1 73 ? 17.988 31.197 17.869 1.00 14.10 ? 73 MET A CB 1 ATOM 571 C CG . MET A 1 73 ? 19.384 31.117 18.465 1.00 14.72 ? 73 MET A CG 1 ATOM 572 S SD . MET A 1 73 ? 19.392 31.378 20.238 1.00 15.83 ? 73 MET A SD 1 ATOM 573 C CE . MET A 1 73 ? 18.633 29.878 20.844 1.00 16.44 ? 73 MET A CE 1 ATOM 574 N N . VAL A 1 74 ? 17.768 28.260 16.892 1.00 12.83 ? 74 VAL A N 1 ATOM 575 C CA . VAL A 1 74 ? 18.293 26.898 16.958 1.00 13.10 ? 74 VAL A CA 1 ATOM 576 C C . VAL A 1 74 ? 18.520 26.365 15.538 1.00 13.78 ? 74 VAL A C 1 ATOM 577 O O . VAL A 1 74 ? 19.595 25.768 15.289 1.00 14.12 ? 74 VAL A O 1 ATOM 578 C CB . VAL A 1 74 ? 17.358 26.012 17.773 1.00 14.62 ? 74 VAL A CB 1 ATOM 579 C CG1 . VAL A 1 74 ? 17.911 24.584 17.820 1.00 16.39 ? 74 VAL A CG1 1 ATOM 580 C CG2 . VAL A 1 74 ? 17.265 26.540 19.213 1.00 14.32 ? 74 VAL A CG2 1 ATOM 581 N N . ASP A 1 75 ? 17.584 26.603 14.626 1.00 14.43 ? 75 ASP A N 1 ATOM 582 C CA . ASP A 1 75 ? 17.730 26.139 13.241 1.00 13.93 ? 75 ASP A CA 1 ATOM 583 C C . ASP A 1 75 ? 18.895 26.803 12.557 1.00 14.96 ? 75 ASP A C 1 ATOM 584 O O . ASP A 1 75 ? 19.541 26.137 11.741 1.00 15.42 ? 75 ASP A O 1 ATOM 585 C CB . ASP A 1 75 ? 16.455 26.454 12.473 1.00 15.08 ? 75 ASP A CB 1 ATOM 586 C CG . ASP A 1 75 ? 15.341 25.450 12.754 1.00 14.92 ? 75 ASP A CG 1 ATOM 587 O OD1 . ASP A 1 75 ? 15.539 24.398 13.352 1.00 16.74 ? 75 ASP A OD1 1 ATOM 588 O OD2 . ASP A 1 75 ? 14.210 25.827 12.324 1.00 18.64 ? 75 ASP A OD2 1 ATOM 589 N N . GLY A 1 76 ? 19.188 28.076 12.861 1.00 14.99 ? 76 GLY A N 1 ATOM 590 C CA . GLY A 1 76 ? 20.342 28.743 12.206 1.00 15.45 ? 76 GLY A CA 1 ATOM 591 C C . GLY A 1 76 ? 21.630 28.058 12.630 1.00 14.99 ? 76 GLY A C 1 ATOM 592 O O . GLY A 1 76 ? 22.549 27.836 11.790 1.00 16.86 ? 76 GLY A O 1 ATOM 593 N N . PHE A 1 77 ? 21.722 27.677 13.895 1.00 13.94 ? 77 PHE A N 1 ATOM 594 C CA . PHE A 1 77 ? 22.898 26.936 14.349 1.00 13.70 ? 77 PHE A CA 1 ATOM 595 C C . PHE A 1 77 ? 22.930 25.532 13.753 1.00 14.75 ? 77 PHE A C 1 ATOM 596 O O . PHE A 1 77 ? 23.994 25.041 13.325 1.00 15.24 ? 77 PHE A O 1 ATOM 597 C CB . PHE A 1 77 ? 22.910 26.820 15.880 1.00 13.52 ? 77 PHE A CB 1 ATOM 598 C CG . PHE A 1 77 ? 23.073 28.141 16.613 1.00 14.42 ? 77 PHE A CG 1 ATOM 599 C CD1 . PHE A 1 77 ? 23.962 29.160 16.170 1.00 15.39 ? 77 PHE A CD1 1 ATOM 600 C CD2 . PHE A 1 77 ? 22.336 28.364 17.769 1.00 14.79 ? 77 PHE A CD2 1 ATOM 601 C CE1 . PHE A 1 77 ? 24.117 30.342 16.945 1.00 15.88 ? 77 PHE A CE1 1 ATOM 602 C CE2 . PHE A 1 77 ? 22.468 29.540 18.518 1.00 15.95 ? 77 PHE A CE2 1 ATOM 603 C CZ . PHE A 1 77 ? 23.352 30.517 18.103 1.00 15.42 ? 77 PHE A CZ 1 ATOM 604 N N . GLN A 1 78 ? 21.770 24.877 13.678 1.00 13.55 ? 78 GLN A N 1 ATOM 605 C CA . GLN A 1 78 ? 21.747 23.554 13.106 1.00 13.24 ? 78 GLN A CA 1 ATOM 606 C C . GLN A 1 78 ? 22.123 23.553 11.626 1.00 14.46 ? 78 GLN A C 1 ATOM 607 O O . GLN A 1 78 ? 22.765 22.582 11.194 1.00 14.46 ? 78 GLN A O 1 ATOM 608 C CB . GLN A 1 78 ? 20.360 22.936 13.319 1.00 14.73 ? 78 GLN A CB 1 ATOM 609 C CG . GLN A 1 78 ? 20.278 21.442 13.007 1.00 13.99 ? 78 GLN A CG 1 ATOM 610 C CD . GLN A 1 78 ? 21.030 20.624 14.009 1.00 14.62 ? 78 GLN A CD 1 ATOM 611 O OE1 . GLN A 1 78 ? 22.280 20.598 13.964 1.00 14.48 ? 78 GLN A OE1 1 ATOM 612 N NE2 . GLN A 1 78 ? 20.323 19.987 14.948 1.00 13.74 ? 78 GLN A NE2 1 ATOM 613 N N . LYS A 1 79 ? 21.717 24.578 10.876 1.00 14.78 ? 79 LYS A N 1 ATOM 614 C CA . LYS A 1 79 ? 22.015 24.594 9.432 1.00 15.69 ? 79 LYS A CA 1 ATOM 615 C C . LYS A 1 79 ? 23.544 24.560 9.267 1.00 15.56 ? 79 LYS A C 1 ATOM 616 O O . LYS A 1 79 ? 24.045 23.843 8.358 1.00 16.03 ? 79 LYS A O 1 ATOM 617 C CB . LYS A 1 79 ? 21.410 25.857 8.774 1.00 17.25 ? 79 LYS A CB 1 ATOM 618 C CG . LYS A 1 79 ? 21.638 25.890 7.262 1.00 24.94 ? 79 LYS A CG 1 ATOM 619 C CD . LYS A 1 79 ? 20.624 26.833 6.604 1.00 29.87 ? 79 LYS A CD 1 ATOM 620 C CE . LYS A 1 79 ? 20.862 26.893 5.088 1.00 37.21 ? 79 LYS A CE 1 ATOM 621 N NZ . LYS A 1 79 ? 20.184 28.079 4.470 1.00 43.28 ? 79 LYS A NZ 1 ATOM 622 N N . ALA A 1 80 ? 24.270 25.264 10.136 1.00 15.02 ? 80 ALA A N 1 ATOM 623 C CA . ALA A 1 80 ? 25.737 25.298 10.022 1.00 15.01 ? 80 ALA A CA 1 ATOM 624 C C . ALA A 1 80 ? 26.294 23.919 10.327 1.00 15.36 ? 80 ALA A C 1 ATOM 625 O O . ALA A 1 80 ? 27.160 23.424 9.597 1.00 15.98 ? 80 ALA A O 1 ATOM 626 C CB . ALA A 1 80 ? 26.295 26.337 10.987 1.00 15.67 ? 80 ALA A CB 1 ATOM 627 N N . CYS A 1 81 ? 25.808 23.253 11.369 1.00 14.62 ? 81 CYS A N 1 ATOM 628 C CA . CYS A 1 81 ? 26.312 21.934 11.722 1.00 14.75 ? 81 CYS A CA 1 ATOM 629 C C . CYS A 1 81 ? 25.997 20.908 10.636 1.00 16.44 ? 81 CYS A C 1 ATOM 630 O O . CYS A 1 81 ? 26.833 20.064 10.327 1.00 16.56 ? 81 CYS A O 1 ATOM 631 C CB . CYS A 1 81 ? 25.712 21.498 13.093 1.00 14.53 ? 81 CYS A CB 1 ATOM 632 S SG . CYS A 1 81 ? 26.277 22.507 14.443 1.00 16.14 ? 81 CYS A SG 1 ATOM 633 N N . MET A 1 82 ? 24.811 20.987 10.028 1.00 15.88 ? 82 MET A N 1 ATOM 634 C CA . MET A 1 82 ? 24.428 20.032 8.986 1.00 17.03 ? 82 MET A CA 1 ATOM 635 C C . MET A 1 82 ? 25.243 20.247 7.704 1.00 17.47 ? 82 MET A C 1 ATOM 636 O O . MET A 1 82 ? 25.239 19.355 6.819 1.00 19.70 ? 82 MET A O 1 ATOM 637 C CB . MET A 1 82 ? 22.911 20.077 8.681 1.00 17.97 ? 82 MET A CB 1 ATOM 638 C CG . MET A 1 82 ? 22.025 19.672 9.862 1.00 20.07 ? 82 MET A CG 1 ATOM 639 S SD . MET A 1 82 ? 22.413 18.001 10.407 1.00 22.87 ? 82 MET A SD 1 ATOM 640 C CE . MET A 1 82 ? 22.013 16.962 8.983 1.00 22.29 ? 82 MET A CE 1 ATOM 641 N N . SER A 1 83 ? 25.944 21.379 7.628 1.00 16.53 ? 83 SER A N 1 ATOM 642 C CA . SER A 1 83 ? 26.731 21.715 6.412 1.00 16.55 ? 83 SER A CA 1 ATOM 643 C C . SER A 1 83 ? 28.158 21.167 6.483 1.00 16.72 ? 83 SER A C 1 ATOM 644 O O . SER A 1 83 ? 28.917 21.354 5.501 1.00 19.08 ? 83 SER A O 1 ATOM 645 C CB . SER A 1 83 ? 26.746 23.229 6.170 1.00 16.91 ? 83 SER A CB 1 ATOM 646 O OG . SER A 1 83 ? 27.643 23.897 7.034 1.00 19.64 ? 83 SER A OG 1 ATOM 647 N N . THR A 1 84 ? 28.543 20.555 7.602 1.00 15.46 ? 84 THR A N 1 ATOM 648 C CA . THR A 1 84 ? 29.885 19.962 7.712 1.00 14.38 ? 84 THR A CA 1 ATOM 649 C C . THR A 1 84 ? 29.970 18.751 6.784 1.00 15.75 ? 84 THR A C 1 ATOM 650 O O . THR A 1 84 ? 28.948 18.206 6.301 1.00 16.45 ? 84 THR A O 1 ATOM 651 C CB . THR A 1 84 ? 30.188 19.487 9.121 1.00 15.07 ? 84 THR A CB 1 ATOM 652 O OG1 . THR A 1 84 ? 29.185 18.519 9.518 1.00 14.47 ? 84 THR A OG1 1 ATOM 653 C CG2 . THR A 1 84 ? 30.199 20.701 10.124 1.00 15.48 ? 84 THR A CG2 1 ATOM 654 N N . ARG A 1 85 ? 31.210 18.296 6.570 1.00 14.71 ? 85 ARG A N 1 ATOM 655 C CA . ARG A 1 85 ? 31.436 17.115 5.726 1.00 15.22 ? 85 ARG A CA 1 ATOM 656 C C . ARG A 1 85 ? 30.525 15.908 6.069 1.00 15.31 ? 85 ARG A C 1 ATOM 657 O O . ARG A 1 85 ? 29.915 15.304 5.149 1.00 16.16 ? 85 ARG A O 1 ATOM 658 C CB . ARG A 1 85 ? 32.884 16.691 5.870 1.00 14.96 ? 85 ARG A CB 1 ATOM 659 C CG . ARG A 1 85 ? 33.321 15.538 4.950 1.00 15.20 ? 85 ARG A CG 1 ATOM 660 C CD . ARG A 1 85 ? 34.778 15.193 5.287 1.00 15.58 ? 85 ARG A CD 1 ATOM 661 N NE . ARG A 1 85 ? 34.957 14.412 6.519 1.00 16.38 ? 85 ARG A NE 1 ATOM 662 C CZ . ARG A 1 85 ? 35.091 13.091 6.560 1.00 16.90 ? 85 ARG A CZ 1 ATOM 663 N NH1 . ARG A 1 85 ? 34.991 12.369 5.429 1.00 18.05 ? 85 ARG A NH1 1 ATOM 664 N NH2 . ARG A 1 85 ? 35.298 12.469 7.717 1.00 17.10 ? 85 ARG A NH2 1 ATOM 665 N N . LEU A 1 86 ? 30.375 15.596 7.368 1.00 14.48 ? 86 LEU A N 1 ATOM 666 C CA . LEU A 1 86 ? 29.620 14.416 7.798 1.00 13.84 ? 86 LEU A CA 1 ATOM 667 C C . LEU A 1 86 ? 28.162 14.788 8.140 1.00 14.41 ? 86 LEU A C 1 ATOM 668 O O . LEU A 1 86 ? 27.329 13.894 8.213 1.00 16.60 ? 86 LEU A O 1 ATOM 669 C CB . LEU A 1 86 ? 30.268 13.706 8.990 1.00 14.60 ? 86 LEU A CB 1 ATOM 670 C CG . LEU A 1 86 ? 31.669 13.133 8.690 1.00 14.42 ? 86 LEU A CG 1 ATOM 671 C CD1 . LEU A 1 86 ? 32.257 12.534 9.942 1.00 16.11 ? 86 LEU A CD1 1 ATOM 672 C CD2 . LEU A 1 86 ? 31.531 12.070 7.578 1.00 16.45 ? 86 LEU A CD2 1 ATOM 673 N N . GLY A 1 87 ? 27.880 16.088 8.316 1.00 13.69 ? 87 GLY A N 1 ATOM 674 C CA . GLY A 1 87 ? 26.472 16.499 8.588 1.00 14.93 ? 87 GLY A CA 1 ATOM 675 C C . GLY A 1 87 ? 25.936 15.945 9.891 1.00 15.15 ? 87 GLY A C 1 ATOM 676 O O . GLY A 1 87 ? 24.818 15.422 9.943 1.00 17.77 ? 87 GLY A O 1 ATOM 677 N N . ILE A 1 88 ? 26.732 16.006 10.948 1.00 14.27 ? 88 ILE A N 1 ATOM 678 C CA . ILE A 1 88 ? 26.273 15.533 12.271 1.00 14.43 ? 88 ILE A CA 1 ATOM 679 C C . ILE A 1 88 ? 25.503 16.663 12.957 1.00 13.67 ? 88 ILE A C 1 ATOM 680 O O . ILE A 1 88 ? 26.063 17.710 13.213 1.00 12.82 ? 88 ILE A O 1 ATOM 681 C CB . ILE A 1 88 ? 27.468 15.089 13.168 1.00 14.19 ? 88 ILE A CB 1 ATOM 682 C CG1 . ILE A 1 88 ? 28.328 13.998 12.462 1.00 15.31 ? 88 ILE A CG1 1 ATOM 683 C CG2 . ILE A 1 88 ? 26.916 14.563 14.505 1.00 15.01 ? 88 ILE A CG2 1 ATOM 684 C CD1 . ILE A 1 88 ? 29.595 13.643 13.241 1.00 15.45 ? 88 ILE A CD1 1 ATOM 685 N N . PRO A 1 89 ? 24.208 16.465 13.264 1.00 13.46 ? 89 PRO A N 1 ATOM 686 C CA . PRO A 1 89 ? 23.442 17.557 13.894 1.00 12.79 ? 89 PRO A CA 1 ATOM 687 C C . PRO A 1 89 ? 23.940 17.802 15.308 1.00 12.32 ? 89 PRO A C 1 ATOM 688 O O . PRO A 1 89 ? 24.312 16.858 15.984 1.00 13.48 ? 89 PRO A O 1 ATOM 689 C CB . PRO A 1 89 ? 21.984 16.983 13.898 1.00 13.40 ? 89 PRO A CB 1 ATOM 690 C CG . PRO A 1 89 ? 22.190 15.487 14.024 1.00 13.68 ? 89 PRO A CG 1 ATOM 691 C CD . PRO A 1 89 ? 23.394 15.232 13.079 1.00 13.91 ? 89 PRO A CD 1 ATOM 692 N N . MET A 1 90 ? 23.920 19.076 15.698 1.00 12.01 ? 90 MET A N 1 ATOM 693 C CA . MET A 1 90 ? 24.151 19.387 17.098 1.00 12.44 ? 90 MET A CA 1 ATOM 694 C C . MET A 1 90 ? 22.898 19.104 17.929 1.00 12.22 ? 90 MET A C 1 ATOM 695 O O . MET A 1 90 ? 21.763 19.037 17.429 1.00 12.66 ? 90 MET A O 1 ATOM 696 C CB . MET A 1 90 ? 24.628 20.851 17.280 1.00 12.86 ? 90 MET A CB 1 ATOM 697 C CG . MET A 1 90 ? 23.630 21.936 16.871 1.00 12.32 ? 90 MET A CG 1 ATOM 698 S SD . MET A 1 90 ? 22.440 22.259 18.219 1.00 13.41 ? 90 MET A SD 1 ATOM 699 C CE . MET A 1 90 ? 21.026 22.748 17.230 1.00 17.18 ? 90 MET A CE 1 ATOM 700 N N . ILE A 1 91 ? 23.140 18.850 19.199 1.00 12.03 ? 91 ILE A N 1 ATOM 701 C CA . ILE A 1 91 ? 22.068 18.807 20.234 1.00 12.75 ? 91 ILE A CA 1 ATOM 702 C C . ILE A 1 91 ? 22.176 20.098 21.056 1.00 12.61 ? 91 ILE A C 1 ATOM 703 O O . ILE A 1 91 ? 23.279 20.509 21.476 1.00 12.67 ? 91 ILE A O 1 ATOM 704 C CB . ILE A 1 91 ? 22.204 17.521 21.084 1.00 12.60 ? 91 ILE A CB 1 ATOM 705 C CG1 . ILE A 1 91 ? 21.001 17.369 22.018 1.00 13.27 ? 91 ILE A CG1 1 ATOM 706 C CG2 . ILE A 1 91 ? 23.493 17.483 21.918 1.00 12.99 ? 91 ILE A CG2 1 ATOM 707 C CD1 . ILE A 1 91 ? 20.972 16.010 22.746 1.00 12.71 ? 91 ILE A CD1 1 ATOM 708 N N . TYR A 1 92 ? 21.018 20.759 21.291 1.00 10.90 ? 92 TYR A N 1 ATOM 709 C CA . TYR A 1 92 ? 20.996 22.069 22.010 1.00 11.00 ? 92 TYR A CA 1 ATOM 710 C C . TYR A 1 92 ? 20.359 21.803 23.383 1.00 11.46 ? 92 TYR A C 1 ATOM 711 O O . TYR A 1 92 ? 19.258 21.243 23.473 1.00 12.67 ? 92 TYR A O 1 ATOM 712 C CB . TYR A 1 92 ? 20.134 23.073 21.215 1.00 10.43 ? 92 TYR A CB 1 ATOM 713 C CG . TYR A 1 92 ? 20.312 24.506 21.679 1.00 10.85 ? 92 TYR A CG 1 ATOM 714 C CD1 . TYR A 1 92 ? 19.817 24.958 22.935 1.00 10.69 ? 92 TYR A CD1 1 ATOM 715 C CD2 . TYR A 1 92 ? 20.976 25.427 20.857 1.00 11.77 ? 92 TYR A CD2 1 ATOM 716 C CE1 . TYR A 1 92 ? 20.016 26.265 23.333 1.00 11.94 ? 92 TYR A CE1 1 ATOM 717 C CE2 . TYR A 1 92 ? 21.198 26.722 21.269 1.00 12.53 ? 92 TYR A CE2 1 ATOM 718 C CZ . TYR A 1 92 ? 20.710 27.151 22.504 1.00 12.17 ? 92 TYR A CZ 1 ATOM 719 O OH . TYR A 1 92 ? 20.933 28.454 22.871 1.00 13.31 ? 92 TYR A OH 1 ATOM 720 N N . GLY A 1 93 ? 21.103 22.139 24.435 1.00 11.58 ? 93 GLY A N 1 ATOM 721 C CA . GLY A 1 93 ? 20.611 21.935 25.803 1.00 11.98 ? 93 GLY A CA 1 ATOM 722 C C . GLY A 1 93 ? 20.271 23.223 26.537 1.00 11.61 ? 93 GLY A C 1 ATOM 723 O O . GLY A 1 93 ? 20.756 24.312 26.233 1.00 11.88 ? 93 GLY A O 1 ATOM 724 N N . ILE A 1 94 ? 19.357 23.069 27.504 1.00 11.53 ? 94 ILE A N 1 ATOM 725 C CA . ILE A 1 94 ? 18.958 24.236 28.301 1.00 11.12 ? 94 ILE A CA 1 ATOM 726 C C . ILE A 1 94 ? 18.437 23.759 29.668 1.00 11.07 ? 94 ILE A C 1 ATOM 727 O O . ILE A 1 94 ? 17.951 22.616 29.780 1.00 11.29 ? 94 ILE A O 1 ATOM 728 C CB . ILE A 1 94 ? 17.853 25.019 27.529 1.00 11.46 ? 94 ILE A CB 1 ATOM 729 C CG1 . ILE A 1 94 ? 17.709 26.442 28.106 1.00 11.69 ? 94 ILE A CG1 1 ATOM 730 C CG2 . ILE A 1 94 ? 16.497 24.249 27.570 1.00 12.38 ? 94 ILE A CG2 1 ATOM 731 C CD1 . ILE A 1 94 ? 16.873 27.358 27.167 1.00 11.53 ? 94 ILE A CD1 1 ATOM 732 N N . ASP A 1 95 ? 18.518 24.646 30.662 1.00 10.94 ? 95 ASP A N 1 ATOM 733 C CA . ASP A 1 95 ? 17.893 24.303 31.974 1.00 11.31 ? 95 ASP A CA 1 ATOM 734 C C . ASP A 1 95 ? 16.394 24.566 31.921 1.00 11.53 ? 95 ASP A C 1 ATOM 735 O O . ASP A 1 95 ? 15.934 25.658 32.255 1.00 12.26 ? 95 ASP A O 1 ATOM 736 C CB . ASP A 1 95 ? 18.536 25.118 33.093 1.00 11.42 ? 95 ASP A CB 1 ATOM 737 C CG . ASP A 1 95 ? 20.007 24.807 33.236 1.00 12.35 ? 95 ASP A CG 1 ATOM 738 O OD1 . ASP A 1 95 ? 20.319 23.754 33.806 1.00 13.34 ? 95 ASP A OD1 1 ATOM 739 O OD2 . ASP A 1 95 ? 20.821 25.590 32.676 1.00 12.89 ? 95 ASP A OD2 1 ATOM 740 N N . ALA A 1 96 ? 15.645 23.541 31.507 1.00 11.46 ? 96 ALA A N 1 ATOM 741 C CA . ALA A 1 96 ? 14.164 23.543 31.651 1.00 11.40 ? 96 ALA A CA 1 ATOM 742 C C . ALA A 1 96 ? 13.937 22.706 32.901 1.00 11.72 ? 96 ALA A C 1 ATOM 743 O O . ALA A 1 96 ? 13.732 21.484 32.819 1.00 12.30 ? 96 ALA A O 1 ATOM 744 C CB . ALA A 1 96 ? 13.503 22.948 30.411 1.00 12.63 ? 96 ALA A CB 1 ATOM 745 N N . VAL A 1 97 ? 13.986 23.388 34.068 1.00 11.80 ? 97 VAL A N 1 ATOM 746 C CA . VAL A 1 97 ? 13.990 22.707 35.369 1.00 11.91 ? 97 VAL A CA 1 ATOM 747 C C . VAL A 1 97 ? 12.696 22.898 36.158 1.00 12.08 ? 97 VAL A C 1 ATOM 748 O O . VAL A 1 97 ? 12.514 22.232 37.163 1.00 13.20 ? 97 VAL A O 1 ATOM 749 C CB . VAL A 1 97 ? 15.220 23.057 36.255 1.00 12.01 ? 97 VAL A CB 1 ATOM 750 C CG1 . VAL A 1 97 ? 16.514 22.554 35.587 1.00 12.58 ? 97 VAL A CG1 1 ATOM 751 C CG2 . VAL A 1 97 ? 15.317 24.573 36.520 1.00 12.53 ? 97 VAL A CG2 1 ATOM 752 N N . HIS A 1 98 ? 11.859 23.825 35.719 1.00 11.73 ? 98 HIS A N 1 ATOM 753 C CA . HIS A 1 98 ? 10.475 23.905 36.267 1.00 11.24 ? 98 HIS A CA 1 ATOM 754 C C . HIS A 1 98 ? 9.587 24.517 35.189 1.00 11.04 ? 98 HIS A C 1 ATOM 755 O O . HIS A 1 98 ? 9.065 25.650 35.329 1.00 11.48 ? 98 HIS A O 1 ATOM 756 C CB . HIS A 1 98 ? 10.396 24.628 37.629 1.00 10.90 ? 98 HIS A CB 1 ATOM 757 C CG . HIS A 1 98 ? 10.784 26.072 37.669 1.00 11.78 ? 98 HIS A CG 1 ATOM 758 N ND1 . HIS A 1 98 ? 10.156 26.971 38.514 1.00 12.37 ? 98 HIS A ND1 1 ATOM 759 C CD2 . HIS A 1 98 ? 11.782 26.758 37.058 1.00 11.29 ? 98 HIS A CD2 1 ATOM 760 C CE1 . HIS A 1 98 ? 10.728 28.165 38.400 1.00 12.73 ? 98 HIS A CE1 1 ATOM 761 N NE2 . HIS A 1 98 ? 11.733 28.062 37.527 1.00 12.12 ? 98 HIS A NE2 1 ATOM 762 N N . GLY A 1 99 ? 9.452 23.751 34.088 1.00 11.10 ? 99 GLY A N 1 ATOM 763 C CA . GLY A 1 99 ? 8.999 24.294 32.826 1.00 11.58 ? 99 GLY A CA 1 ATOM 764 C C . GLY A 1 99 ? 10.203 24.792 32.023 1.00 11.68 ? 99 GLY A C 1 ATOM 765 O O . GLY A 1 99 ? 11.360 24.639 32.443 1.00 12.09 ? 99 GLY A O 1 ATOM 766 N N . GLN A 1 100 ? 9.900 25.367 30.859 1.00 11.16 ? 100 GLN A N 1 ATOM 767 C CA . GLN A 1 100 ? 10.956 25.887 29.943 1.00 11.36 ? 100 GLN A CA 1 ATOM 768 C C . GLN A 1 100 ? 11.292 27.320 30.408 1.00 11.00 ? 100 GLN A C 1 ATOM 769 O O . GLN A 1 100 ? 10.969 28.344 29.783 1.00 11.83 ? 100 GLN A O 1 ATOM 770 C CB . GLN A 1 100 ? 10.373 25.790 28.494 1.00 10.97 ? 100 GLN A CB 1 ATOM 771 C CG . GLN A 1 100 ? 11.205 26.451 27.367 1.00 11.69 ? 100 GLN A CG 1 ATOM 772 C CD . GLN A 1 100 ? 12.673 26.017 27.230 1.00 12.00 ? 100 GLN A CD 1 ATOM 773 O OE1 . GLN A 1 100 ? 13.230 25.949 26.067 1.00 14.09 ? 100 GLN A OE1 1 ATOM 774 N NE2 . GLN A 1 100 ? 13.329 25.769 28.325 1.00 9.76 ? 100 GLN A NE2 1 ATOM 775 N N . ASN A 1 101 ? 11.917 27.359 31.593 1.00 10.84 ? 101 ASN A N 1 ATOM 776 C CA . ASN A 1 101 ? 11.923 28.579 32.409 1.00 10.31 ? 101 ASN A CA 1 ATOM 777 C C . ASN A 1 101 ? 12.717 29.793 31.957 1.00 11.21 ? 101 ASN A C 1 ATOM 778 O O . ASN A 1 101 ? 12.493 30.869 32.515 1.00 11.64 ? 101 ASN A O 1 ATOM 779 C CB . ASN A 1 101 ? 12.262 28.206 33.859 1.00 10.94 ? 101 ASN A CB 1 ATOM 780 C CG . ASN A 1 101 ? 13.549 27.423 33.946 1.00 11.53 ? 101 ASN A CG 1 ATOM 781 O OD1 . ASN A 1 101 ? 14.699 27.981 33.732 1.00 14.58 ? 101 ASN A OD1 1 ATOM 782 N ND2 . ASN A 1 101 ? 13.419 26.164 34.123 1.00 9.56 ? 101 ASN A ND2 1 ATOM 783 N N . ASN A 1 102 ? 13.648 29.644 31.011 1.00 11.58 ? 102 ASN A N 1 ATOM 784 C CA . ASN A 1 102 ? 14.331 30.833 30.472 1.00 11.74 ? 102 ASN A CA 1 ATOM 785 C C . ASN A 1 102 ? 13.452 31.607 29.495 1.00 12.09 ? 102 ASN A C 1 ATOM 786 O O . ASN A 1 102 ? 13.805 32.718 29.112 1.00 13.19 ? 102 ASN A O 1 ATOM 787 C CB . ASN A 1 102 ? 15.624 30.445 29.695 1.00 12.14 ? 102 ASN A CB 1 ATOM 788 C CG . ASN A 1 102 ? 16.768 30.024 30.596 1.00 13.00 ? 102 ASN A CG 1 ATOM 789 O OD1 . ASN A 1 102 ? 17.256 28.851 30.508 1.00 14.32 ? 102 ASN A OD1 1 ATOM 790 N ND2 . ASN A 1 102 ? 17.201 30.893 31.461 1.00 10.90 ? 102 ASN A ND2 1 ATOM 791 N N . VAL A 1 103 ? 12.330 31.009 29.053 1.00 11.71 ? 103 VAL A N 1 ATOM 792 C CA . VAL A 1 103 ? 11.564 31.507 27.901 1.00 12.10 ? 103 VAL A CA 1 ATOM 793 C C . VAL A 1 103 ? 10.346 32.314 28.343 1.00 12.16 ? 103 VAL A C 1 ATOM 794 O O . VAL A 1 103 ? 9.566 31.870 29.169 1.00 12.92 ? 103 VAL A O 1 ATOM 795 C CB . VAL A 1 103 ? 11.144 30.332 26.997 1.00 12.26 ? 103 VAL A CB 1 ATOM 796 C CG1 . VAL A 1 103 ? 10.291 30.813 25.804 1.00 13.37 ? 103 VAL A CG1 1 ATOM 797 C CG2 . VAL A 1 103 ? 12.402 29.603 26.493 1.00 13.78 ? 103 VAL A CG2 1 ATOM 798 N N . TYR A 1 104 ? 10.248 33.523 27.792 1.00 12.58 ? 104 TYR A N 1 ATOM 799 C CA . TYR A 1 104 ? 9.073 34.339 28.092 1.00 13.45 ? 104 TYR A CA 1 ATOM 800 C C . TYR A 1 104 ? 7.801 33.627 27.621 1.00 13.40 ? 104 TYR A C 1 ATOM 801 O O . TYR A 1 104 ? 7.718 33.148 26.496 1.00 14.30 ? 104 TYR A O 1 ATOM 802 C CB . TYR A 1 104 ? 9.253 35.710 27.372 1.00 14.61 ? 104 TYR A CB 1 ATOM 803 C CG . TYR A 1 104 ? 8.120 36.678 27.674 1.00 16.56 ? 104 TYR A CG 1 ATOM 804 C CD1 . TYR A 1 104 ? 8.117 37.503 28.801 1.00 18.53 ? 104 TYR A CD1 1 ATOM 805 C CD2 . TYR A 1 104 ? 7.024 36.658 26.841 1.00 18.46 ? 104 TYR A CD2 1 ATOM 806 C CE1 . TYR A 1 104 ? 6.995 38.332 29.042 1.00 19.85 ? 104 TYR A CE1 1 ATOM 807 C CE2 . TYR A 1 104 ? 5.930 37.457 27.072 1.00 22.64 ? 104 TYR A CE2 1 ATOM 808 C CZ . TYR A 1 104 ? 5.936 38.257 28.161 1.00 21.53 ? 104 TYR A CZ 1 ATOM 809 O OH . TYR A 1 104 ? 4.756 39.038 28.295 1.00 27.69 ? 104 TYR A OH 1 ATOM 810 N N . GLY A 1 105 ? 6.786 33.605 28.483 1.00 12.71 ? 105 GLY A N 1 ATOM 811 C CA . GLY A 1 105 ? 5.500 32.959 28.114 1.00 12.83 ? 105 GLY A CA 1 ATOM 812 C C . GLY A 1 105 ? 5.459 31.460 28.329 1.00 13.05 ? 105 GLY A C 1 ATOM 813 O O . GLY A 1 105 ? 4.409 30.840 28.078 1.00 14.22 ? 105 GLY A O 1 ATOM 814 N N . ALA A 1 106 ? 6.546 30.853 28.747 1.00 12.53 ? 106 ALA A N 1 ATOM 815 C CA . ALA A 1 106 ? 6.523 29.437 29.154 1.00 11.44 ? 106 ALA A CA 1 ATOM 816 C C . ALA A 1 106 ? 5.811 29.224 30.477 1.00 11.81 ? 106 ALA A C 1 ATOM 817 O O . ALA A 1 106 ? 5.971 30.007 31.388 1.00 12.76 ? 106 ALA A O 1 ATOM 818 C CB . ALA A 1 106 ? 7.948 28.861 29.267 1.00 11.62 ? 106 ALA A CB 1 ATOM 819 N N . THR A 1 107 ? 5.040 28.131 30.568 1.00 11.79 ? 107 THR A N 1 ATOM 820 C CA . THR A 1 107 ? 4.435 27.748 31.883 1.00 11.17 ? 107 THR A CA 1 ATOM 821 C C . THR A 1 107 ? 5.569 27.504 32.893 1.00 10.70 ? 107 THR A C 1 ATOM 822 O O . THR A 1 107 ? 6.554 26.805 32.570 1.00 12.01 ? 107 THR A O 1 ATOM 823 C CB . THR A 1 107 ? 3.667 26.431 31.707 1.00 11.97 ? 107 THR A CB 1 ATOM 824 O OG1 . THR A 1 107 ? 2.758 26.581 30.605 1.00 12.20 ? 107 THR A OG1 1 ATOM 825 C CG2 . THR A 1 107 ? 2.893 26.098 32.984 1.00 12.39 ? 107 THR A CG2 1 ATOM 826 N N . ILE A 1 108 ? 5.421 28.086 34.093 1.00 11.43 ? 108 ILE A N 1 ATOM 827 C CA . ILE A 1 108 ? 6.453 27.876 35.145 1.00 11.51 ? 108 ILE A CA 1 ATOM 828 C C . ILE A 1 108 ? 5.810 27.025 36.229 1.00 11.92 ? 108 ILE A C 1 ATOM 829 O O . ILE A 1 108 ? 4.810 27.431 36.874 1.00 12.05 ? 108 ILE A O 1 ATOM 830 C CB . ILE A 1 108 ? 6.950 29.220 35.732 1.00 10.94 ? 108 ILE A CB 1 ATOM 831 C CG1 . ILE A 1 108 ? 7.538 30.142 34.634 1.00 12.21 ? 108 ILE A CG1 1 ATOM 832 C CG2 . ILE A 1 108 ? 7.987 28.895 36.803 1.00 11.35 ? 108 ILE A CG2 1 ATOM 833 C CD1 . ILE A 1 108 ? 8.743 29.560 33.840 1.00 11.97 ? 108 ILE A CD1 1 ATOM 834 N N . PHE A 1 109 ? 6.310 25.801 36.381 1.00 11.35 ? 109 PHE A N 1 ATOM 835 C CA . PHE A 1 109 ? 5.802 24.842 37.380 1.00 10.43 ? 109 PHE A CA 1 ATOM 836 C C . PHE A 1 109 ? 6.437 25.121 38.739 1.00 11.98 ? 109 PHE A C 1 ATOM 837 O O . PHE A 1 109 ? 7.523 25.785 38.820 1.00 12.35 ? 109 PHE A O 1 ATOM 838 C CB . PHE A 1 109 ? 6.141 23.409 36.893 1.00 11.62 ? 109 PHE A CB 1 ATOM 839 C CG . PHE A 1 109 ? 5.375 23.032 35.653 1.00 11.86 ? 109 PHE A CG 1 ATOM 840 C CD1 . PHE A 1 109 ? 4.091 22.512 35.753 1.00 12.41 ? 109 PHE A CD1 1 ATOM 841 C CD2 . PHE A 1 109 ? 5.929 23.207 34.392 1.00 12.43 ? 109 PHE A CD2 1 ATOM 842 C CE1 . PHE A 1 109 ? 3.372 22.187 34.616 1.00 12.33 ? 109 PHE A CE1 1 ATOM 843 C CE2 . PHE A 1 109 ? 5.209 22.899 33.233 1.00 12.79 ? 109 PHE A CE2 1 ATOM 844 C CZ . PHE A 1 109 ? 3.914 22.375 33.353 1.00 12.90 ? 109 PHE A CZ 1 ATOM 845 N N . PRO A 1 110 ? 5.837 24.615 39.826 1.00 11.39 ? 110 PRO A N 1 ATOM 846 C CA . PRO A 1 110 ? 6.491 24.708 41.146 1.00 11.44 ? 110 PRO A CA 1 ATOM 847 C C . PRO A 1 110 ? 7.911 24.104 41.085 1.00 11.41 ? 110 PRO A C 1 ATOM 848 O O . PRO A 1 110 ? 8.133 23.114 40.398 1.00 11.90 ? 110 PRO A O 1 ATOM 849 C CB . PRO A 1 110 ? 5.606 23.831 42.040 1.00 11.82 ? 110 PRO A CB 1 ATOM 850 C CG . PRO A 1 110 ? 4.249 23.911 41.384 1.00 11.62 ? 110 PRO A CG 1 ATOM 851 C CD . PRO A 1 110 ? 4.517 23.929 39.881 1.00 11.91 ? 110 PRO A CD 1 ATOM 852 N N . HIS A 1 111 ? 8.836 24.704 41.836 1.00 11.35 ? 111 HIS A N 1 ATOM 853 C CA . HIS A 1 111 ? 10.167 24.069 42.000 1.00 11.98 ? 111 HIS A CA 1 ATOM 854 C C . HIS A 1 111 ? 10.090 22.721 42.710 1.00 12.50 ? 111 HIS A C 1 ATOM 855 O O . HIS A 1 111 ? 9.061 22.363 43.380 1.00 12.50 ? 111 HIS A O 1 ATOM 856 C CB . HIS A 1 111 ? 11.126 25.006 42.724 1.00 12.08 ? 111 HIS A CB 1 ATOM 857 C CG . HIS A 1 111 ? 11.836 25.957 41.813 1.00 11.87 ? 111 HIS A CG 1 ATOM 858 N ND1 . HIS A 1 111 ? 12.707 25.521 40.835 1.00 12.33 ? 111 HIS A ND1 1 ATOM 859 C CD2 . HIS A 1 111 ? 11.830 27.307 41.755 1.00 12.37 ? 111 HIS A CD2 1 ATOM 860 C CE1 . HIS A 1 111 ? 13.211 26.566 40.207 1.00 12.27 ? 111 HIS A CE1 1 ATOM 861 N NE2 . HIS A 1 111 ? 12.690 27.668 40.741 1.00 12.09 ? 111 HIS A NE2 1 ATOM 862 N N . ASN A 1 112 ? 11.162 21.956 42.568 1.00 12.37 ? 112 ASN A N 1 ATOM 863 C CA . ASN A 1 112 ? 11.147 20.558 43.021 1.00 12.12 ? 112 ASN A CA 1 ATOM 864 C C . ASN A 1 112 ? 10.785 20.368 44.514 1.00 12.30 ? 112 ASN A C 1 ATOM 865 O O . ASN A 1 112 ? 10.088 19.398 44.788 1.00 13.11 ? 112 ASN A O 1 ATOM 866 C CB . ASN A 1 112 ? 12.507 19.887 42.769 1.00 12.66 ? 112 ASN A CB 1 ATOM 867 C CG . ASN A 1 112 ? 12.776 19.594 41.323 1.00 13.45 ? 112 ASN A CG 1 ATOM 868 O OD1 . ASN A 1 112 ? 13.920 19.125 40.987 1.00 17.29 ? 112 ASN A OD1 1 ATOM 869 N ND2 . ASN A 1 112 ? 11.791 19.753 40.478 1.00 11.16 ? 112 ASN A ND2 1 ATOM 870 N N . VAL A 1 113 ? 11.188 21.264 45.430 1.00 12.96 ? 113 VAL A N 1 ATOM 871 C CA . VAL A 1 113 ? 10.856 21.035 46.855 1.00 13.91 ? 113 VAL A CA 1 ATOM 872 C C . VAL A 1 113 ? 9.326 20.955 47.039 1.00 13.96 ? 113 VAL A C 1 ATOM 873 O O . VAL A 1 113 ? 8.813 20.032 47.698 1.00 14.06 ? 113 VAL A O 1 ATOM 874 C CB . VAL A 1 113 ? 11.558 22.066 47.779 1.00 13.26 ? 113 VAL A CB 1 ATOM 875 C CG1 . VAL A 1 113 ? 11.090 23.493 47.483 1.00 15.39 ? 113 VAL A CG1 1 ATOM 876 C CG2 . VAL A 1 113 ? 11.281 21.718 49.257 1.00 14.75 ? 113 VAL A CG2 1 ATOM 877 N N . GLY A 1 114 ? 8.592 21.854 46.377 1.00 13.54 ? 114 GLY A N 1 ATOM 878 C CA . GLY A 1 114 ? 7.117 21.789 46.405 1.00 13.90 ? 114 GLY A CA 1 ATOM 879 C C . GLY A 1 114 ? 6.579 20.547 45.727 1.00 13.15 ? 114 GLY A C 1 ATOM 880 O O . GLY A 1 114 ? 5.605 19.925 46.220 1.00 13.11 ? 114 GLY A O 1 ATOM 881 N N . LEU A 1 115 ? 7.195 20.126 44.605 1.00 13.40 ? 115 LEU A N 1 ATOM 882 C CA . LEU A 1 115 ? 6.783 18.847 44.025 1.00 12.73 ? 115 LEU A CA 1 ATOM 883 C C . LEU A 1 115 ? 6.975 17.673 45.013 1.00 13.67 ? 115 LEU A C 1 ATOM 884 O O . LEU A 1 115 ? 6.152 16.762 45.022 1.00 13.50 ? 115 LEU A O 1 ATOM 885 C CB . LEU A 1 115 ? 7.508 18.596 42.685 1.00 13.36 ? 115 LEU A CB 1 ATOM 886 C CG . LEU A 1 115 ? 7.164 19.680 41.652 1.00 12.83 ? 115 LEU A CG 1 ATOM 887 C CD1 . LEU A 1 115 ? 7.900 19.318 40.354 1.00 13.39 ? 115 LEU A CD1 1 ATOM 888 C CD2 . LEU A 1 115 ? 5.653 19.840 41.404 1.00 13.58 ? 115 LEU A CD2 1 ATOM 889 N N . GLY A 1 116 ? 8.055 17.683 45.789 1.00 13.58 ? 116 GLY A N 1 ATOM 890 C CA . GLY A 1 116 ? 8.249 16.657 46.831 1.00 13.79 ? 116 GLY A CA 1 ATOM 891 C C . GLY A 1 116 ? 7.084 16.633 47.816 1.00 14.91 ? 116 GLY A C 1 ATOM 892 O O . GLY A 1 116 ? 6.672 15.549 48.262 1.00 15.47 ? 116 GLY A O 1 ATOM 893 N N . ALA A 1 117 ? 6.577 17.810 48.165 1.00 14.41 ? 117 ALA A N 1 ATOM 894 C CA . ALA A 1 117 ? 5.434 17.924 49.086 1.00 14.01 ? 117 ALA A CA 1 ATOM 895 C C . ALA A 1 117 ? 4.157 17.248 48.579 1.00 14.50 ? 117 ALA A C 1 ATOM 896 O O . ALA A 1 117 ? 3.316 16.819 49.372 1.00 15.92 ? 117 ALA A O 1 ATOM 897 C CB . ALA A 1 117 ? 5.179 19.412 49.406 1.00 14.06 ? 117 ALA A CB 1 ATOM 898 N N . THR A 1 118 ? 4.025 17.080 47.265 1.00 14.13 ? 118 THR A N 1 ATOM 899 C CA . THR A 1 118 ? 2.818 16.467 46.687 1.00 14.60 ? 118 THR A CA 1 ATOM 900 C C . THR A 1 118 ? 2.807 14.935 46.867 1.00 16.12 ? 118 THR A C 1 ATOM 901 O O . THR A 1 118 ? 1.751 14.309 46.738 1.00 17.18 ? 118 THR A O 1 ATOM 902 C CB . THR A 1 118 ? 2.706 16.720 45.161 1.00 14.40 ? 118 THR A CB 1 ATOM 903 O OG1 . THR A 1 118 ? 3.656 15.919 44.419 1.00 14.93 ? 118 THR A OG1 1 ATOM 904 C CG2 . THR A 1 118 ? 2.834 18.232 44.795 1.00 14.42 ? 118 THR A CG2 1 ATOM 905 N N . ARG A 1 119 ? 3.985 14.352 47.047 1.00 16.56 ? 119 ARG A N 1 ATOM 906 C CA . ARG A 1 119 ? 4.150 12.873 47.040 1.00 16.85 ? 119 ARG A CA 1 ATOM 907 C C . ARG A 1 119 ? 3.429 12.219 45.853 1.00 17.30 ? 119 ARG A C 1 ATOM 908 O O . ARG A 1 119 ? 2.899 11.086 45.977 1.00 19.34 ? 119 ARG A O 1 ATOM 909 C CB . ARG A 1 119 ? 3.580 12.279 48.347 1.00 17.57 ? 119 ARG A CB 1 ATOM 910 C CG . ARG A 1 119 ? 4.208 12.847 49.603 1.00 18.98 ? 119 ARG A CG 1 ATOM 911 C CD . ARG A 1 119 ? 5.693 12.515 49.725 1.00 19.22 ? 119 ARG A CD 1 ATOM 912 N NE . ARG A 1 119 ? 6.113 12.649 51.135 1.00 21.76 ? 119 ARG A NE 1 ATOM 913 C CZ . ARG A 1 119 ? 6.331 13.811 51.781 1.00 20.64 ? 119 ARG A CZ 1 ATOM 914 N NH1 . ARG A 1 119 ? 6.285 15.013 51.145 1.00 17.29 ? 119 ARG A NH1 1 ATOM 915 N NH2 . ARG A 1 119 ? 6.659 13.766 53.080 1.00 21.08 ? 119 ARG A NH2 1 ATOM 916 N N . ASP A 1 120 ? 3.420 12.896 44.684 1.00 16.44 ? 120 ASP A N 1 ATOM 917 C CA . ASP A 1 120 ? 2.659 12.435 43.526 1.00 16.92 ? 120 ASP A CA 1 ATOM 918 C C . ASP A 1 120 ? 3.603 12.250 42.331 1.00 16.08 ? 120 ASP A C 1 ATOM 919 O O . ASP A 1 120 ? 3.717 13.179 41.521 1.00 16.34 ? 120 ASP A O 1 ATOM 920 C CB . ASP A 1 120 ? 1.543 13.446 43.243 1.00 18.09 ? 120 ASP A CB 1 ATOM 921 C CG . ASP A 1 120 ? 0.484 12.923 42.266 1.00 18.62 ? 120 ASP A CG 1 ATOM 922 O OD1 . ASP A 1 120 ? 0.749 11.975 41.529 1.00 22.41 ? 120 ASP A OD1 1 ATOM 923 O OD2 . ASP A 1 120 ? -0.631 13.524 42.271 1.00 23.84 ? 120 ASP A OD2 1 ATOM 924 N N . PRO A 1 121 ? 4.243 11.075 42.205 1.00 16.74 ? 121 PRO A N 1 ATOM 925 C CA . PRO A 1 121 ? 5.131 10.863 41.048 1.00 16.10 ? 121 PRO A CA 1 ATOM 926 C C . PRO A 1 121 ? 4.416 10.919 39.694 1.00 16.95 ? 121 PRO A C 1 ATOM 927 O O . PRO A 1 121 ? 5.093 11.326 38.710 1.00 17.24 ? 121 PRO A O 1 ATOM 928 C CB . PRO A 1 121 ? 5.715 9.452 41.303 1.00 17.58 ? 121 PRO A CB 1 ATOM 929 C CG . PRO A 1 121 ? 5.606 9.276 42.805 1.00 18.52 ? 121 PRO A CG 1 ATOM 930 C CD . PRO A 1 121 ? 4.292 9.906 43.127 1.00 17.03 ? 121 PRO A CD 1 ATOM 931 N N . TYR A 1 122 ? 3.115 10.614 39.602 1.00 17.09 ? 122 TYR A N 1 ATOM 932 C CA . TYR A 1 122 ? 2.420 10.707 38.296 1.00 16.05 ? 122 TYR A CA 1 ATOM 933 C C . TYR A 1 122 ? 2.207 12.152 37.884 1.00 16.26 ? 122 TYR A C 1 ATOM 934 O O . TYR A 1 122 ? 2.296 12.503 36.698 1.00 15.86 ? 122 TYR A O 1 ATOM 935 C CB . TYR A 1 122 ? 1.066 9.908 38.315 1.00 19.46 ? 122 TYR A CB 1 ATOM 936 C CG . TYR A 1 122 ? 0.344 9.966 36.963 1.00 21.36 ? 122 TYR A CG 1 ATOM 937 C CD1 . TYR A 1 122 ? 1.010 9.588 35.804 1.00 24.68 ? 122 TYR A CD1 1 ATOM 938 C CD2 . TYR A 1 122 ? -0.976 10.436 36.851 1.00 23.68 ? 122 TYR A CD2 1 ATOM 939 C CE1 . TYR A 1 122 ? 0.410 9.684 34.558 1.00 26.08 ? 122 TYR A CE1 1 ATOM 940 C CE2 . TYR A 1 122 ? -1.604 10.493 35.602 1.00 25.11 ? 122 TYR A CE2 1 ATOM 941 C CZ . TYR A 1 122 ? -0.904 10.122 34.473 1.00 27.04 ? 122 TYR A CZ 1 ATOM 942 O OH . TYR A 1 122 ? -1.471 10.201 33.210 1.00 33.66 ? 122 TYR A OH 1 ATOM 943 N N . LEU A 1 123 ? 1.916 12.991 38.861 1.00 14.65 ? 123 LEU A N 1 ATOM 944 C CA . LEU A 1 123 ? 1.868 14.452 38.623 1.00 13.91 ? 123 LEU A CA 1 ATOM 945 C C . LEU A 1 123 ? 3.219 14.908 38.054 1.00 14.11 ? 123 LEU A C 1 ATOM 946 O O . LEU A 1 123 ? 3.240 15.661 37.041 1.00 13.95 ? 123 LEU A O 1 ATOM 947 C CB . LEU A 1 123 ? 1.553 15.140 39.939 1.00 15.18 ? 123 LEU A CB 1 ATOM 948 C CG . LEU A 1 123 ? 1.693 16.678 39.891 1.00 15.98 ? 123 LEU A CG 1 ATOM 949 C CD1 . LEU A 1 123 ? 0.489 17.269 39.138 1.00 16.74 ? 123 LEU A CD1 1 ATOM 950 C CD2 . LEU A 1 123 ? 1.784 17.248 41.308 1.00 18.99 ? 123 LEU A CD2 1 ATOM 951 N N . VAL A 1 124 ? 4.305 14.480 38.684 1.00 13.99 ? 124 VAL A N 1 ATOM 952 C CA . VAL A 1 124 ? 5.646 14.878 38.220 1.00 14.33 ? 124 VAL A CA 1 ATOM 953 C C . VAL A 1 124 ? 5.895 14.339 36.781 1.00 14.52 ? 124 VAL A C 1 ATOM 954 O O . VAL A 1 124 ? 6.445 15.069 35.921 1.00 14.06 ? 124 VAL A O 1 ATOM 955 C CB . VAL A 1 124 ? 6.722 14.516 39.237 1.00 15.21 ? 124 VAL A CB 1 ATOM 956 C CG1 . VAL A 1 124 ? 8.117 14.813 38.687 1.00 14.42 ? 124 VAL A CG1 1 ATOM 957 C CG2 . VAL A 1 124 ? 6.491 15.318 40.538 1.00 16.18 ? 124 VAL A CG2 1 ATOM 958 N N . LYS A 1 125 ? 5.483 13.094 36.501 1.00 14.60 ? 125 LYS A N 1 ATOM 959 C CA . LYS A 1 125 ? 5.607 12.581 35.125 1.00 14.34 ? 125 LYS A CA 1 ATOM 960 C C . LYS A 1 125 ? 4.863 13.490 34.115 1.00 14.63 ? 125 LYS A C 1 ATOM 961 O O . LYS A 1 125 ? 5.392 13.807 33.062 1.00 13.62 ? 125 LYS A O 1 ATOM 962 C CB . LYS A 1 125 ? 5.074 11.119 35.061 1.00 15.62 ? 125 LYS A CB 1 ATOM 963 C CG . LYS A 1 125 ? 5.380 10.489 33.693 1.00 15.70 ? 125 LYS A CG 1 ATOM 964 C CD . LYS A 1 125 ? 4.785 9.076 33.623 1.00 19.07 ? 125 LYS A CD 1 ATOM 965 C CE . LYS A 1 125 ? 5.127 8.489 32.265 1.00 19.77 ? 125 LYS A CE 1 ATOM 966 N NZ . LYS A 1 125 ? 4.425 7.153 32.153 1.00 22.97 ? 125 LYS A NZ 1 ATOM 967 N N . ARG A 1 126 ? 3.630 13.891 34.454 1.00 14.50 ? 126 ARG A N 1 ATOM 968 C CA . ARG A 1 126 ? 2.828 14.730 33.580 1.00 14.17 ? 126 ARG A CA 1 ATOM 969 C C . ARG A 1 126 ? 3.518 16.077 33.382 1.00 13.04 ? 126 ARG A C 1 ATOM 970 O O . ARG A 1 126 ? 3.529 16.622 32.284 1.00 14.01 ? 126 ARG A O 1 ATOM 971 C CB . ARG A 1 126 ? 1.401 14.882 34.133 1.00 15.81 ? 126 ARG A CB 1 ATOM 972 C CG . ARG A 1 126 ? 0.645 13.543 34.081 1.00 18.46 ? 126 ARG A CG 1 ATOM 973 C CD . ARG A 1 126 ? -0.286 13.319 35.309 1.00 29.05 ? 126 ARG A CD 1 ATOM 974 N NE . ARG A 1 126 ? -1.205 14.374 35.349 1.00 29.75 ? 126 ARG A NE 1 ATOM 975 C CZ . ARG A 1 126 ? -1.806 14.980 36.386 1.00 24.09 ? 126 ARG A CZ 1 ATOM 976 N NH1 . ARG A 1 126 ? -1.751 14.626 37.684 1.00 22.48 ? 126 ARG A NH1 1 ATOM 977 N NH2 . ARG A 1 126 ? -2.535 15.982 36.027 1.00 24.63 ? 126 ARG A NH2 1 ATOM 978 N N . ILE A 1 127 ? 4.159 16.584 34.439 1.00 13.43 ? 127 ILE A N 1 ATOM 979 C CA . ILE A 1 127 ? 4.946 17.851 34.334 1.00 13.28 ? 127 ILE A CA 1 ATOM 980 C C . ILE A 1 127 ? 6.133 17.647 33.363 1.00 13.19 ? 127 ILE A C 1 ATOM 981 O O . ILE A 1 127 ? 6.377 18.521 32.488 1.00 13.52 ? 127 ILE A O 1 ATOM 982 C CB . ILE A 1 127 ? 5.445 18.313 35.708 1.00 13.18 ? 127 ILE A CB 1 ATOM 983 C CG1 . ILE A 1 127 ? 4.226 18.817 36.503 1.00 13.42 ? 127 ILE A CG1 1 ATOM 984 C CG2 . ILE A 1 127 ? 6.439 19.476 35.530 1.00 13.41 ? 127 ILE A CG2 1 ATOM 985 C CD1 . ILE A 1 127 ? 4.548 19.167 37.951 1.00 13.55 ? 127 ILE A CD1 1 ATOM 986 N N . GLY A 1 128 ? 6.813 16.482 33.447 1.00 12.60 ? 128 GLY A N 1 ATOM 987 C CA . GLY A 1 128 ? 7.869 16.161 32.438 1.00 12.25 ? 128 GLY A CA 1 ATOM 988 C C . GLY A 1 128 ? 7.338 16.157 31.029 1.00 12.52 ? 128 GLY A C 1 ATOM 989 O O . GLY A 1 128 ? 7.951 16.723 30.079 1.00 13.37 ? 128 GLY A O 1 ATOM 990 N N . GLU A 1 129 ? 6.160 15.530 30.845 1.00 13.41 ? 129 GLU A N 1 ATOM 991 C CA . GLU A 1 129 ? 5.538 15.488 29.510 1.00 13.48 ? 129 GLU A CA 1 ATOM 992 C C . GLU A 1 129 ? 5.239 16.905 28.977 1.00 13.20 ? 129 GLU A C 1 ATOM 993 O O . GLU A 1 129 ? 5.537 17.222 27.823 1.00 14.44 ? 129 GLU A O 1 ATOM 994 C CB . GLU A 1 129 ? 4.237 14.648 29.556 1.00 15.12 ? 129 GLU A CB 1 ATOM 995 C CG . GLU A 1 129 ? 4.552 13.198 29.991 1.00 17.99 ? 129 GLU A CG 1 ATOM 996 C CD . GLU A 1 129 ? 3.368 12.261 30.176 1.00 23.47 ? 129 GLU A CD 1 ATOM 997 O OE1 . GLU A 1 129 ? 3.611 11.015 30.148 1.00 22.42 ? 129 GLU A OE1 1 ATOM 998 O OE2 . GLU A 1 129 ? 2.220 12.750 30.374 1.00 24.67 ? 129 GLU A OE2 1 ATOM 999 N N . ALA A 1 130 ? 4.681 17.759 29.824 1.00 12.80 ? 130 ALA A N 1 ATOM 1000 C CA . ALA A 1 130 ? 4.338 19.114 29.406 1.00 12.93 ? 130 ALA A CA 1 ATOM 1001 C C . ALA A 1 130 ? 5.590 19.926 29.159 1.00 12.48 ? 130 ALA A C 1 ATOM 1002 O O . ALA A 1 130 ? 5.640 20.718 28.182 1.00 12.36 ? 130 ALA A O 1 ATOM 1003 C CB . ALA A 1 130 ? 3.507 19.797 30.506 1.00 14.84 ? 130 ALA A CB 1 ATOM 1004 N N . THR A 1 131 ? 6.607 19.732 30.003 1.00 12.52 ? 131 THR A N 1 ATOM 1005 C CA . THR A 1 131 ? 7.884 20.457 29.825 1.00 12.28 ? 131 THR A CA 1 ATOM 1006 C C . THR A 1 131 ? 8.546 20.084 28.526 1.00 12.68 ? 131 THR A C 1 ATOM 1007 O O . THR A 1 131 ? 9.010 20.986 27.792 1.00 12.96 ? 131 THR A O 1 ATOM 1008 C CB . THR A 1 131 ? 8.800 20.168 31.022 1.00 11.70 ? 131 THR A CB 1 ATOM 1009 O OG1 . THR A 1 131 ? 8.149 20.678 32.195 1.00 12.00 ? 131 THR A OG1 1 ATOM 1010 C CG2 . THR A 1 131 ? 10.188 20.877 30.895 1.00 13.20 ? 131 THR A CG2 1 ATOM 1011 N N . ALA A 1 132 ? 8.529 18.794 28.176 1.00 13.16 ? 132 ALA A N 1 ATOM 1012 C CA . ALA A 1 132 ? 9.118 18.393 26.884 1.00 12.96 ? 132 ALA A CA 1 ATOM 1013 C C . ALA A 1 132 ? 8.475 19.123 25.699 1.00 12.40 ? 132 ALA A C 1 ATOM 1014 O O . ALA A 1 132 ? 9.161 19.570 24.761 1.00 12.47 ? 132 ALA A O 1 ATOM 1015 C CB . ALA A 1 132 ? 9.030 16.879 26.689 1.00 13.86 ? 132 ALA A CB 1 ATOM 1016 N N . LEU A 1 133 ? 7.137 19.248 25.739 1.00 13.14 ? 133 LEU A N 1 ATOM 1017 C CA . LEU A 1 133 ? 6.424 19.897 24.639 1.00 12.89 ? 133 LEU A CA 1 ATOM 1018 C C . LEU A 1 133 ? 6.798 21.384 24.564 1.00 12.92 ? 133 LEU A C 1 ATOM 1019 O O . LEU A 1 133 ? 6.987 21.931 23.455 1.00 12.80 ? 133 LEU A O 1 ATOM 1020 C CB . LEU A 1 133 ? 4.910 19.778 24.827 1.00 13.14 ? 133 LEU A CB 1 ATOM 1021 C CG . LEU A 1 133 ? 4.410 18.361 24.669 1.00 13.60 ? 133 LEU A CG 1 ATOM 1022 C CD1 . LEU A 1 133 ? 2.934 18.374 25.017 1.00 15.28 ? 133 LEU A CD1 1 ATOM 1023 C CD2 . LEU A 1 133 ? 4.497 17.942 23.213 1.00 15.85 ? 133 LEU A CD2 1 ATOM 1024 N N . GLU A 1 134 ? 6.933 22.043 25.725 1.00 12.17 ? 134 GLU A N 1 ATOM 1025 C CA . GLU A 1 134 ? 7.300 23.504 25.707 1.00 11.56 ? 134 GLU A CA 1 ATOM 1026 C C . GLU A 1 134 ? 8.772 23.734 25.344 1.00 11.92 ? 134 GLU A C 1 ATOM 1027 O O . GLU A 1 134 ? 9.081 24.818 24.766 1.00 12.35 ? 134 GLU A O 1 ATOM 1028 C CB . GLU A 1 134 ? 6.916 24.193 27.037 1.00 11.85 ? 134 GLU A CB 1 ATOM 1029 C CG . GLU A 1 134 ? 5.392 24.056 27.262 1.00 12.00 ? 134 GLU A CG 1 ATOM 1030 C CD . GLU A 1 134 ? 4.780 25.151 28.126 1.00 12.95 ? 134 GLU A CD 1 ATOM 1031 O OE1 . GLU A 1 134 ? 5.381 26.224 28.324 1.00 12.61 ? 134 GLU A OE1 1 ATOM 1032 O OE2 . GLU A 1 134 ? 3.617 24.921 28.601 1.00 13.49 ? 134 GLU A OE2 1 ATOM 1033 N N . VAL A 1 135 ? 9.635 22.779 25.676 1.00 11.43 ? 135 VAL A N 1 ATOM 1034 C CA . VAL A 1 135 ? 11.053 22.844 25.215 1.00 11.49 ? 135 VAL A CA 1 ATOM 1035 C C . VAL A 1 135 ? 11.066 22.668 23.702 1.00 12.43 ? 135 VAL A C 1 ATOM 1036 O O . VAL A 1 135 ? 11.716 23.460 22.971 1.00 12.28 ? 135 VAL A O 1 ATOM 1037 C CB . VAL A 1 135 ? 11.897 21.817 25.981 1.00 11.12 ? 135 VAL A CB 1 ATOM 1038 C CG1 . VAL A 1 135 ? 13.329 21.778 25.412 1.00 11.88 ? 135 VAL A CG1 1 ATOM 1039 C CG2 . VAL A 1 135 ? 11.915 22.182 27.491 1.00 12.07 ? 135 VAL A CG2 1 ATOM 1040 N N . ARG A 1 136 ? 10.363 21.643 23.212 1.00 12.46 ? 136 ARG A N 1 ATOM 1041 C CA . ARG A 1 136 ? 10.327 21.451 21.721 1.00 12.88 ? 136 ARG A CA 1 ATOM 1042 C C . ARG A 1 136 ? 9.598 22.586 20.985 1.00 12.61 ? 136 ARG A C 1 ATOM 1043 O O . ARG A 1 136 ? 9.902 22.881 19.825 1.00 12.69 ? 136 ARG A O 1 ATOM 1044 C CB . ARG A 1 136 ? 9.721 20.083 21.349 1.00 12.38 ? 136 ARG A CB 1 ATOM 1045 C CG . ARG A 1 136 ? 10.640 18.899 21.610 1.00 13.01 ? 136 ARG A CG 1 ATOM 1046 C CD . ARG A 1 136 ? 11.812 18.874 20.631 1.00 12.92 ? 136 ARG A CD 1 ATOM 1047 N NE . ARG A 1 136 ? 12.480 17.610 20.784 1.00 14.12 ? 136 ARG A NE 1 ATOM 1048 C CZ . ARG A 1 136 ? 13.216 17.060 19.809 1.00 14.23 ? 136 ARG A CZ 1 ATOM 1049 N NH1 . ARG A 1 136 ? 13.426 17.715 18.667 1.00 15.94 ? 136 ARG A NH1 1 ATOM 1050 N NH2 . ARG A 1 136 ? 13.710 15.834 20.007 1.00 15.38 ? 136 ARG A NH2 1 ATOM 1051 N N . ALA A 1 137 ? 8.684 23.309 21.686 1.00 12.70 ? 137 ALA A N 1 ATOM 1052 C CA . ALA A 1 137 ? 8.098 24.521 21.066 1.00 12.35 ? 137 ALA A CA 1 ATOM 1053 C C . ALA A 1 137 ? 9.140 25.548 20.696 1.00 13.14 ? 137 ALA A C 1 ATOM 1054 O O . ALA A 1 137 ? 8.904 26.391 19.805 1.00 12.64 ? 137 ALA A O 1 ATOM 1055 C CB . ALA A 1 137 ? 7.132 25.151 22.075 1.00 13.18 ? 137 ALA A CB 1 ATOM 1056 N N . THR A 1 138 ? 10.281 25.516 21.399 1.00 11.72 ? 138 THR A N 1 ATOM 1057 C CA . THR A 1 138 ? 11.361 26.513 21.172 1.00 12.12 ? 138 THR A CA 1 ATOM 1058 C C . THR A 1 138 ? 12.480 25.906 20.330 1.00 12.71 ? 138 THR A C 1 ATOM 1059 O O . THR A 1 138 ? 13.538 26.544 20.145 1.00 13.42 ? 138 THR A O 1 ATOM 1060 C CB . THR A 1 138 ? 11.887 27.076 22.512 1.00 12.63 ? 138 THR A CB 1 ATOM 1061 O OG1 . THR A 1 138 ? 12.487 26.025 23.303 1.00 13.52 ? 138 THR A OG1 1 ATOM 1062 C CG2 . THR A 1 138 ? 10.734 27.735 23.265 1.00 13.66 ? 138 THR A CG2 1 ATOM 1063 N N . GLY A 1 139 ? 12.264 24.678 19.826 1.00 12.14 ? 139 GLY A N 1 ATOM 1064 C CA . GLY A 1 139 ? 13.267 24.037 18.931 1.00 13.05 ? 139 GLY A CA 1 ATOM 1065 C C . GLY A 1 139 ? 14.356 23.303 19.683 1.00 13.49 ? 139 GLY A C 1 ATOM 1066 O O . GLY A 1 139 ? 15.245 22.745 19.065 1.00 16.08 ? 139 GLY A O 1 ATOM 1067 N N . ILE A 1 140 ? 14.311 23.268 21.012 1.00 12.01 ? 140 ILE A N 1 ATOM 1068 C CA . ILE A 1 140 ? 15.401 22.695 21.812 1.00 12.35 ? 140 ILE A CA 1 ATOM 1069 C C . ILE A 1 140 ? 15.129 21.235 22.090 1.00 12.47 ? 140 ILE A C 1 ATOM 1070 O O . ILE A 1 140 ? 13.937 20.814 22.276 1.00 12.75 ? 140 ILE A O 1 ATOM 1071 C CB . ILE A 1 140 ? 15.586 23.564 23.082 1.00 11.81 ? 140 ILE A CB 1 ATOM 1072 C CG1 . ILE A 1 140 ? 16.111 24.941 22.627 1.00 12.95 ? 140 ILE A CG1 1 ATOM 1073 C CG2 . ILE A 1 140 ? 16.551 22.937 24.094 1.00 11.77 ? 140 ILE A CG2 1 ATOM 1074 C CD1 . ILE A 1 140 ? 16.202 26.011 23.692 1.00 13.43 ? 140 ILE A CD1 1 ATOM 1075 N N . GLN A 1 141 ? 16.211 20.426 22.116 1.00 12.24 ? 141 GLN A N 1 ATOM 1076 C CA . GLN A 1 141 ? 16.018 18.947 22.165 1.00 11.62 ? 141 GLN A CA 1 ATOM 1077 C C . GLN A 1 141 ? 16.484 18.288 23.456 1.00 11.86 ? 141 GLN A C 1 ATOM 1078 O O . GLN A 1 141 ? 16.378 17.071 23.567 1.00 12.20 ? 141 GLN A O 1 ATOM 1079 C CB . GLN A 1 141 ? 16.773 18.267 20.999 1.00 12.76 ? 141 GLN A CB 1 ATOM 1080 C CG . GLN A 1 141 ? 16.548 18.929 19.627 1.00 12.28 ? 141 GLN A CG 1 ATOM 1081 C CD . GLN A 1 141 ? 17.640 19.925 19.244 1.00 13.45 ? 141 GLN A CD 1 ATOM 1082 O OE1 . GLN A 1 141 ? 18.404 20.394 20.098 1.00 14.75 ? 141 GLN A OE1 1 ATOM 1083 N NE2 . GLN A 1 141 ? 17.700 20.249 17.946 1.00 14.71 ? 141 GLN A NE2 1 ATOM 1084 N N . TYR A 1 142 ? 16.960 19.076 24.443 1.00 11.14 ? 142 TYR A N 1 ATOM 1085 C CA . TYR A 1 142 ? 17.711 18.511 25.561 1.00 12.23 ? 142 TYR A CA 1 ATOM 1086 C C . TYR A 1 142 ? 17.528 19.418 26.768 1.00 11.64 ? 142 TYR A C 1 ATOM 1087 O O . TYR A 1 142 ? 17.816 20.615 26.697 1.00 11.77 ? 142 TYR A O 1 ATOM 1088 C CB . TYR A 1 142 ? 19.197 18.444 25.120 1.00 12.22 ? 142 TYR A CB 1 ATOM 1089 C CG . TYR A 1 142 ? 20.237 17.956 26.126 1.00 12.40 ? 142 TYR A CG 1 ATOM 1090 C CD1 . TYR A 1 142 ? 19.889 17.122 27.201 1.00 12.55 ? 142 TYR A CD1 1 ATOM 1091 C CD2 . TYR A 1 142 ? 21.582 18.278 25.959 1.00 13.08 ? 142 TYR A CD2 1 ATOM 1092 C CE1 . TYR A 1 142 ? 20.822 16.685 28.109 1.00 12.94 ? 142 TYR A CE1 1 ATOM 1093 C CE2 . TYR A 1 142 ? 22.544 17.842 26.833 1.00 13.09 ? 142 TYR A CE2 1 ATOM 1094 C CZ . TYR A 1 142 ? 22.168 17.033 27.899 1.00 12.74 ? 142 TYR A CZ 1 ATOM 1095 O OH . TYR A 1 142 ? 23.166 16.635 28.774 1.00 14.32 ? 142 TYR A OH 1 ATOM 1096 N N . ALA A 1 143 ? 17.036 18.840 27.860 1.00 11.30 ? 143 ALA A N 1 ATOM 1097 C CA . ALA A 1 143 ? 16.849 19.577 29.102 1.00 10.78 ? 143 ALA A CA 1 ATOM 1098 C C . ALA A 1 143 ? 17.796 19.056 30.199 1.00 11.77 ? 143 ALA A C 1 ATOM 1099 O O . ALA A 1 143 ? 17.891 17.839 30.424 1.00 11.94 ? 143 ALA A O 1 ATOM 1100 C CB . ALA A 1 143 ? 15.376 19.383 29.568 1.00 12.33 ? 143 ALA A CB 1 ATOM 1101 N N . PHE A 1 144 ? 18.445 19.980 30.893 1.00 11.54 ? 144 PHE A N 1 ATOM 1102 C CA . PHE A 1 144 ? 19.368 19.604 31.994 1.00 12.58 ? 144 PHE A CA 1 ATOM 1103 C C . PHE A 1 144 ? 18.549 19.381 33.277 1.00 12.18 ? 144 PHE A C 1 ATOM 1104 O O . PHE A 1 144 ? 18.698 20.103 34.290 1.00 12.49 ? 144 PHE A O 1 ATOM 1105 C CB . PHE A 1 144 ? 20.394 20.737 32.222 1.00 12.29 ? 144 PHE A CB 1 ATOM 1106 C CG . PHE A 1 144 ? 21.262 21.051 31.034 1.00 12.26 ? 144 PHE A CG 1 ATOM 1107 C CD1 . PHE A 1 144 ? 21.937 20.030 30.338 1.00 13.04 ? 144 PHE A CD1 1 ATOM 1108 C CD2 . PHE A 1 144 ? 21.422 22.378 30.651 1.00 12.81 ? 144 PHE A CD2 1 ATOM 1109 C CE1 . PHE A 1 144 ? 22.826 20.376 29.279 1.00 13.18 ? 144 PHE A CE1 1 ATOM 1110 C CE2 . PHE A 1 144 ? 22.264 22.730 29.563 1.00 12.70 ? 144 PHE A CE2 1 ATOM 1111 C CZ . PHE A 1 144 ? 22.956 21.726 28.887 1.00 12.95 ? 144 PHE A CZ 1 ATOM 1112 N N . ALA A 1 145 ? 17.736 18.326 33.282 1.00 11.82 ? 145 ALA A N 1 ATOM 1113 C CA . ALA A 1 145 ? 16.867 17.979 34.407 1.00 12.53 ? 145 ALA A CA 1 ATOM 1114 C C . ALA A 1 145 ? 16.567 16.469 34.293 1.00 11.90 ? 145 ALA A C 1 ATOM 1115 O O . ALA A 1 145 ? 16.495 15.938 33.183 1.00 12.80 ? 145 ALA A O 1 ATOM 1116 C CB . ALA A 1 145 ? 15.528 18.749 34.260 1.00 12.59 ? 145 ALA A CB 1 ATOM 1117 N N . PRO A 1 146 ? 16.279 15.808 35.424 1.00 12.65 ? 146 PRO A N 1 ATOM 1118 C CA . PRO A 1 146 ? 16.080 16.362 36.748 1.00 12.61 ? 146 PRO A CA 1 ATOM 1119 C C . PRO A 1 146 ? 17.328 16.513 37.579 1.00 12.69 ? 146 PRO A C 1 ATOM 1120 O O . PRO A 1 146 ? 18.233 15.627 37.558 1.00 14.13 ? 146 PRO A O 1 ATOM 1121 C CB . PRO A 1 146 ? 15.206 15.291 37.454 1.00 14.37 ? 146 PRO A CB 1 ATOM 1122 C CG . PRO A 1 146 ? 15.589 13.990 36.781 1.00 14.48 ? 146 PRO A CG 1 ATOM 1123 C CD . PRO A 1 146 ? 15.917 14.395 35.337 1.00 12.67 ? 146 PRO A CD 1 ATOM 1124 N N . CYS A 1 147 ? 17.312 17.560 38.408 1.00 12.85 ? 147 CYS A N 1 ATOM 1125 C CA . CYS A 1 147 ? 18.203 17.584 39.578 1.00 13.44 ? 147 CYS A CA 1 ATOM 1126 C C . CYS A 1 147 ? 17.677 16.584 40.614 1.00 14.67 ? 147 CYS A C 1 ATOM 1127 O O . CYS A 1 147 ? 16.572 16.750 41.158 1.00 14.89 ? 147 CYS A O 1 ATOM 1128 C CB . CYS A 1 147 ? 18.258 18.995 40.179 1.00 13.62 ? 147 CYS A CB 1 ATOM 1129 S SG . CYS A 1 147 ? 19.357 19.020 41.631 1.00 15.43 ? 147 CYS A SG 1 ATOM 1130 N N . ILE A 1 148 ? 18.460 15.523 40.810 1.00 13.89 ? 148 ILE A N 1 ATOM 1131 C CA . ILE A 1 148 ? 18.132 14.449 41.791 1.00 13.96 ? 148 ILE A CA 1 ATOM 1132 C C . ILE A 1 148 ? 19.040 14.544 43.007 1.00 14.76 ? 148 ILE A C 1 ATOM 1133 O O . ILE A 1 148 ? 19.248 13.538 43.740 1.00 16.60 ? 148 ILE A O 1 ATOM 1134 C CB . ILE A 1 148 ? 18.078 13.022 41.163 1.00 14.56 ? 148 ILE A CB 1 ATOM 1135 C CG1 . ILE A 1 148 ? 19.407 12.676 40.460 1.00 14.75 ? 148 ILE A CG1 1 ATOM 1136 C CG2 . ILE A 1 148 ? 16.895 12.917 40.217 1.00 15.09 ? 148 ILE A CG2 1 ATOM 1137 C CD1 . ILE A 1 148 ? 19.496 11.180 40.143 1.00 15.90 ? 148 ILE A CD1 1 ATOM 1138 N N . ALA A 1 149 ? 19.504 15.757 43.317 1.00 14.30 ? 149 ALA A N 1 ATOM 1139 C CA . ALA A 1 149 ? 20.170 16.051 44.598 1.00 16.04 ? 149 ALA A CA 1 ATOM 1140 C C . ALA A 1 149 ? 19.230 15.718 45.766 1.00 16.15 ? 149 ALA A C 1 ATOM 1141 O O . ALA A 1 149 ? 18.010 15.902 45.666 1.00 17.04 ? 149 ALA A O 1 ATOM 1142 C CB . ALA A 1 149 ? 20.600 17.527 44.693 1.00 15.71 ? 149 ALA A CB 1 ATOM 1143 N N . VAL A 1 150 ? 19.804 15.134 46.818 1.00 16.83 ? 150 VAL A N 1 ATOM 1144 C CA . VAL A 1 150 ? 19.127 14.886 48.065 1.00 16.62 ? 150 VAL A CA 1 ATOM 1145 C C . VAL A 1 150 ? 19.653 15.935 49.027 1.00 17.50 ? 150 VAL A C 1 ATOM 1146 O O . VAL A 1 150 ? 20.753 15.779 49.627 1.00 17.66 ? 150 VAL A O 1 ATOM 1147 C CB . VAL A 1 150 ? 19.395 13.473 48.581 1.00 16.88 ? 150 VAL A CB 1 ATOM 1148 C CG1 . VAL A 1 150 ? 18.599 13.299 49.866 1.00 16.81 ? 150 VAL A CG1 1 ATOM 1149 C CG2 . VAL A 1 150 ? 18.990 12.428 47.547 1.00 17.94 ? 150 VAL A CG2 1 ATOM 1150 N N . CYS A 1 151 ? 18.916 17.035 49.167 1.00 17.04 ? 151 CYS A N 1 ATOM 1151 C CA . CYS A 1 151 ? 19.453 18.166 49.941 1.00 17.10 ? 151 CYS A CA 1 ATOM 1152 C C . CYS A 1 151 ? 19.389 17.858 51.457 1.00 17.87 ? 151 CYS A C 1 ATOM 1153 O O . CYS A 1 151 ? 18.310 17.667 52.030 1.00 19.02 ? 151 CYS A O 1 ATOM 1154 C CB . CYS A 1 151 ? 18.713 19.493 49.609 1.00 18.55 ? 151 CYS A CB 1 ATOM 1155 S SG . CYS A 1 151 ? 19.169 20.883 50.708 1.00 20.53 ? 151 CYS A SG 1 ATOM 1156 N N . ARG A 1 152 ? 20.570 17.791 52.084 1.00 17.32 ? 152 ARG A N 1 ATOM 1157 C CA . ARG A 1 152 ? 20.639 17.417 53.513 1.00 18.45 ? 152 ARG A CA 1 ATOM 1158 C C . ARG A 1 152 ? 20.883 18.625 54.417 1.00 19.20 ? 152 ARG A C 1 ATOM 1159 O O . ARG A 1 152 ? 20.983 18.459 55.644 1.00 20.58 ? 152 ARG A O 1 ATOM 1160 C CB . ARG A 1 152 ? 21.742 16.367 53.727 1.00 20.30 ? 152 ARG A CB 1 ATOM 1161 C CG . ARG A 1 152 ? 21.562 15.111 52.909 1.00 20.93 ? 152 ARG A CG 1 ATOM 1162 C CD . ARG A 1 152 ? 20.397 14.254 53.382 1.00 21.92 ? 152 ARG A CD 1 ATOM 1163 N NE . ARG A 1 152 ? 20.734 13.495 54.603 1.00 21.96 ? 152 ARG A NE 1 ATOM 1164 C CZ . ARG A 1 152 ? 19.880 12.725 55.272 1.00 23.21 ? 152 ARG A CZ 1 ATOM 1165 N NH1 . ARG A 1 152 ? 20.303 12.081 56.380 1.00 23.11 ? 152 ARG A NH1 1 ATOM 1166 N NH2 . ARG A 1 152 ? 18.640 12.548 54.872 1.00 22.60 ? 152 ARG A NH2 1 ATOM 1167 N N . ASP A 1 153 ? 20.970 19.832 53.863 1.00 19.16 ? 153 ASP A N 1 ATOM 1168 C CA . ASP A 1 153 ? 21.158 21.053 54.646 1.00 19.24 ? 153 ASP A CA 1 ATOM 1169 C C . ASP A 1 153 ? 20.513 22.213 53.928 1.00 18.77 ? 153 ASP A C 1 ATOM 1170 O O . ASP A 1 153 ? 20.960 22.568 52.832 1.00 18.01 ? 153 ASP A O 1 ATOM 1171 C CB . ASP A 1 153 ? 22.658 21.314 54.830 1.00 21.57 ? 153 ASP A CB 1 ATOM 1172 C CG . ASP A 1 153 ? 22.942 22.401 55.818 1.00 26.51 ? 153 ASP A CG 1 ATOM 1173 O OD1 . ASP A 1 153 ? 22.182 23.379 55.947 1.00 23.22 ? 153 ASP A OD1 1 ATOM 1174 O OD2 . ASP A 1 153 ? 23.985 22.277 56.522 1.00 31.30 ? 153 ASP A OD2 1 ATOM 1175 N N . PRO A 1 154 ? 19.407 22.760 54.482 1.00 17.74 ? 154 PRO A N 1 ATOM 1176 C CA . PRO A 1 154 ? 18.654 23.770 53.728 1.00 17.51 ? 154 PRO A CA 1 ATOM 1177 C C . PRO A 1 154 ? 19.392 25.095 53.559 1.00 18.02 ? 154 PRO A C 1 ATOM 1178 O O . PRO A 1 154 ? 18.920 25.986 52.866 1.00 18.32 ? 154 PRO A O 1 ATOM 1179 C CB . PRO A 1 154 ? 17.394 23.940 54.565 1.00 16.72 ? 154 PRO A CB 1 ATOM 1180 C CG . PRO A 1 154 ? 17.841 23.651 55.999 1.00 17.25 ? 154 PRO A CG 1 ATOM 1181 C CD . PRO A 1 154 ? 18.820 22.498 55.819 1.00 16.99 ? 154 PRO A CD 1 ATOM 1182 N N . ARG A 1 155 ? 20.600 25.239 54.142 1.00 19.68 ? 155 ARG A N 1 ATOM 1183 C CA . ARG A 1 155 ? 21.373 26.457 53.896 1.00 18.89 ? 155 ARG A CA 1 ATOM 1184 C C . ARG A 1 155 ? 21.931 26.460 52.446 1.00 18.41 ? 155 ARG A C 1 ATOM 1185 O O . ARG A 1 155 ? 22.384 27.492 51.977 1.00 20.28 ? 155 ARG A O 1 ATOM 1186 C CB . ARG A 1 155 ? 22.516 26.567 54.942 1.00 19.90 ? 155 ARG A CB 1 ATOM 1187 C CG . ARG A 1 155 ? 21.927 26.794 56.338 1.00 21.50 ? 155 ARG A CG 1 ATOM 1188 C CD . ARG A 1 155 ? 23.014 26.816 57.405 1.00 22.95 ? 155 ARG A CD 1 ATOM 1189 N NE . ARG A 1 155 ? 23.574 25.477 57.512 1.00 24.94 ? 155 ARG A NE 1 ATOM 1190 C CZ . ARG A 1 155 ? 24.542 25.153 58.373 1.00 28.53 ? 155 ARG A CZ 1 ATOM 1191 N NH1 . ARG A 1 155 ? 25.013 26.094 59.171 1.00 33.20 ? 155 ARG A NH1 1 ATOM 1192 N NH2 . ARG A 1 155 ? 25.002 23.911 58.448 1.00 29.47 ? 155 ARG A NH2 1 ATOM 1193 N N . TRP A 1 156 ? 21.919 25.294 51.786 1.00 17.77 ? 156 TRP A N 1 ATOM 1194 C CA . TRP A 1 156 ? 22.321 25.225 50.369 1.00 17.22 ? 156 TRP A CA 1 ATOM 1195 C C . TRP A 1 156 ? 21.421 26.121 49.515 1.00 17.45 ? 156 TRP A C 1 ATOM 1196 O O . TRP A 1 156 ? 20.181 26.022 49.587 1.00 17.38 ? 156 TRP A O 1 ATOM 1197 C CB . TRP A 1 156 ? 22.193 23.815 49.858 1.00 17.53 ? 156 TRP A CB 1 ATOM 1198 C CG . TRP A 1 156 ? 22.762 23.573 48.476 1.00 17.69 ? 156 TRP A CG 1 ATOM 1199 C CD1 . TRP A 1 156 ? 23.823 24.229 47.886 1.00 18.95 ? 156 TRP A CD1 1 ATOM 1200 C CD2 . TRP A 1 156 ? 22.371 22.526 47.584 1.00 16.64 ? 156 TRP A CD2 1 ATOM 1201 N NE1 . TRP A 1 156 ? 24.091 23.656 46.630 1.00 19.08 ? 156 TRP A NE1 1 ATOM 1202 C CE2 . TRP A 1 156 ? 23.256 22.577 46.451 1.00 18.10 ? 156 TRP A CE2 1 ATOM 1203 C CE3 . TRP A 1 156 ? 21.397 21.518 47.634 1.00 16.88 ? 156 TRP A CE3 1 ATOM 1204 C CZ2 . TRP A 1 156 ? 23.112 21.711 45.358 1.00 18.82 ? 156 TRP A CZ2 1 ATOM 1205 C CZ3 . TRP A 1 156 ? 21.271 20.640 46.588 1.00 18.48 ? 156 TRP A CZ3 1 ATOM 1206 C CH2 . TRP A 1 156 ? 22.121 20.742 45.437 1.00 18.53 ? 156 TRP A CH2 1 ATOM 1207 N N . GLY A 1 157 ? 22.031 26.942 48.667 1.00 17.99 ? 157 GLY A N 1 ATOM 1208 C CA . GLY A 1 157 ? 21.260 27.852 47.811 1.00 17.64 ? 157 GLY A CA 1 ATOM 1209 C C . GLY A 1 157 ? 20.503 27.169 46.714 1.00 17.15 ? 157 GLY A C 1 ATOM 1210 O O . GLY A 1 157 ? 19.748 27.866 46.004 1.00 18.66 ? 157 GLY A O 1 ATOM 1211 N N . ARG A 1 158 ? 20.715 25.869 46.520 1.00 16.39 ? 158 ARG A N 1 ATOM 1212 C CA . ARG A 1 158 ? 19.928 25.152 45.512 1.00 16.97 ? 158 ARG A CA 1 ATOM 1213 C C . ARG A 1 158 ? 18.965 24.160 46.135 1.00 15.98 ? 158 ARG A C 1 ATOM 1214 O O . ARG A 1 158 ? 18.470 23.277 45.450 1.00 16.18 ? 158 ARG A O 1 ATOM 1215 C CB . ARG A 1 158 ? 20.840 24.440 44.504 1.00 16.67 ? 158 ARG A CB 1 ATOM 1216 C CG . ARG A 1 158 ? 21.919 25.372 43.970 1.00 16.94 ? 158 ARG A CG 1 ATOM 1217 C CD . ARG A 1 158 ? 22.727 24.681 42.872 1.00 16.42 ? 158 ARG A CD 1 ATOM 1218 N NE . ARG A 1 158 ? 21.953 24.455 41.653 1.00 16.73 ? 158 ARG A NE 1 ATOM 1219 C CZ . ARG A 1 158 ? 22.489 24.108 40.492 1.00 15.35 ? 158 ARG A CZ 1 ATOM 1220 N NH1 . ARG A 1 158 ? 23.825 23.978 40.347 1.00 16.65 ? 158 ARG A NH1 1 ATOM 1221 N NH2 . ARG A 1 158 ? 21.678 23.915 39.467 1.00 14.50 ? 158 ARG A NH2 1 ATOM 1222 N N . CYS A 1 159 ? 18.701 24.262 47.464 1.00 16.66 ? 159 CYS A N 1 ATOM 1223 C CA . CYS A 1 159 ? 17.874 23.253 48.117 1.00 17.50 ? 159 CYS A CA 1 ATOM 1224 C C . CYS A 1 159 ? 16.463 23.119 47.445 1.00 14.97 ? 159 CYS A C 1 ATOM 1225 O O . CYS A 1 159 ? 15.943 22.018 47.421 1.00 15.09 ? 159 CYS A O 1 ATOM 1226 C CB . CYS A 1 159 ? 17.750 23.572 49.627 1.00 19.93 ? 159 CYS A CB 1 ATOM 1227 S SG . CYS A 1 159 ? 17.343 22.083 50.626 1.00 24.50 ? 159 CYS A SG 1 ATOM 1228 N N . TYR A 1 160 ? 15.921 24.217 46.913 1.00 15.37 ? 160 TYR A N 1 ATOM 1229 C CA . TYR A 1 160 ? 14.617 24.153 46.227 1.00 14.30 ? 160 TYR A CA 1 ATOM 1230 C C . TYR A 1 160 ? 14.627 23.287 44.969 1.00 13.91 ? 160 TYR A C 1 ATOM 1231 O O . TYR A 1 160 ? 13.552 22.847 44.513 1.00 13.63 ? 160 TYR A O 1 ATOM 1232 C CB . TYR A 1 160 ? 14.079 25.557 45.917 1.00 13.41 ? 160 TYR A CB 1 ATOM 1233 C CG . TYR A 1 160 ? 14.935 26.391 44.978 1.00 12.94 ? 160 TYR A CG 1 ATOM 1234 C CD1 . TYR A 1 160 ? 14.848 26.204 43.582 1.00 13.05 ? 160 TYR A CD1 1 ATOM 1235 C CD2 . TYR A 1 160 ? 15.838 27.324 45.467 1.00 13.89 ? 160 TYR A CD2 1 ATOM 1236 C CE1 . TYR A 1 160 ? 15.619 26.973 42.722 1.00 12.92 ? 160 TYR A CE1 1 ATOM 1237 C CE2 . TYR A 1 160 ? 16.616 28.136 44.616 1.00 13.66 ? 160 TYR A CE2 1 ATOM 1238 C CZ . TYR A 1 160 ? 16.520 27.921 43.244 1.00 14.48 ? 160 TYR A CZ 1 ATOM 1239 O OH . TYR A 1 160 ? 17.290 28.727 42.397 1.00 15.47 ? 160 TYR A OH 1 ATOM 1240 N N . GLU A 1 161 ? 15.830 22.986 44.419 1.00 13.79 ? 161 GLU A N 1 ATOM 1241 C CA . GLU A 1 161 ? 15.930 22.057 43.289 1.00 14.18 ? 161 GLU A CA 1 ATOM 1242 C C . GLU A 1 161 ? 15.982 20.597 43.711 1.00 13.49 ? 161 GLU A C 1 ATOM 1243 O O . GLU A 1 161 ? 16.038 19.722 42.846 1.00 13.75 ? 161 GLU A O 1 ATOM 1244 C CB . GLU A 1 161 ? 17.173 22.379 42.420 1.00 14.17 ? 161 GLU A CB 1 ATOM 1245 C CG . GLU A 1 161 ? 17.184 23.819 41.872 1.00 14.42 ? 161 GLU A CG 1 ATOM 1246 C CD . GLU A 1 161 ? 18.174 23.942 40.712 1.00 14.89 ? 161 GLU A CD 1 ATOM 1247 O OE1 . GLU A 1 161 ? 19.210 24.625 40.918 1.00 15.07 ? 161 GLU A OE1 1 ATOM 1248 O OE2 . GLU A 1 161 ? 17.888 23.373 39.634 1.00 15.10 ? 161 GLU A OE2 1 ATOM 1249 N N . SER A 1 162 ? 15.898 20.334 45.025 1.00 14.18 ? 162 SER A N 1 ATOM 1250 C CA . SER A 1 162 ? 15.857 18.965 45.511 1.00 14.76 ? 162 SER A CA 1 ATOM 1251 C C . SER A 1 162 ? 14.443 18.602 45.938 1.00 14.65 ? 162 SER A C 1 ATOM 1252 O O . SER A 1 162 ? 13.774 19.380 46.651 1.00 15.15 ? 162 SER A O 1 ATOM 1253 C CB . SER A 1 162 ? 16.799 18.846 46.690 1.00 15.12 ? 162 SER A CB 1 ATOM 1254 O OG . SER A 1 162 ? 16.626 17.575 47.330 1.00 15.60 ? 162 SER A OG 1 ATOM 1255 N N . TYR A 1 163 ? 13.956 17.476 45.433 1.00 15.26 ? 163 TYR A N 1 ATOM 1256 C CA . TYR A 1 163 ? 12.591 17.046 45.836 1.00 14.57 ? 163 TYR A CA 1 ATOM 1257 C C . TYR A 1 163 ? 12.437 16.813 47.351 1.00 15.61 ? 163 TYR A C 1 ATOM 1258 O O . TYR A 1 163 ? 11.339 16.966 47.888 1.00 15.76 ? 163 TYR A O 1 ATOM 1259 C CB . TYR A 1 163 ? 12.145 15.782 45.088 1.00 14.50 ? 163 TYR A CB 1 ATOM 1260 C CG . TYR A 1 163 ? 12.138 15.860 43.583 1.00 14.09 ? 163 TYR A CG 1 ATOM 1261 C CD1 . TYR A 1 163 ? 11.093 16.555 42.913 1.00 14.87 ? 163 TYR A CD1 1 ATOM 1262 C CD2 . TYR A 1 163 ? 13.143 15.251 42.823 1.00 14.91 ? 163 TYR A CD2 1 ATOM 1263 C CE1 . TYR A 1 163 ? 11.057 16.610 41.523 1.00 14.41 ? 163 TYR A CE1 1 ATOM 1264 C CE2 . TYR A 1 163 ? 13.103 15.286 41.423 1.00 14.92 ? 163 TYR A CE2 1 ATOM 1265 C CZ . TYR A 1 163 ? 12.058 15.977 40.787 1.00 14.70 ? 163 TYR A CZ 1 ATOM 1266 O OH . TYR A 1 163 ? 12.035 16.016 39.415 1.00 15.89 ? 163 TYR A OH 1 ATOM 1267 N N . SER A 1 164 ? 13.505 16.382 48.015 1.00 15.97 ? 164 SER A N 1 ATOM 1268 C CA . SER A 1 164 ? 13.370 15.964 49.434 1.00 16.67 ? 164 SER A CA 1 ATOM 1269 C C . SER A 1 164 ? 14.741 15.735 50.039 1.00 17.54 ? 164 SER A C 1 ATOM 1270 O O . SER A 1 164 ? 15.734 15.406 49.329 1.00 16.79 ? 164 SER A O 1 ATOM 1271 C CB . SER A 1 164 ? 12.560 14.670 49.470 1.00 16.53 ? 164 SER A CB 1 ATOM 1272 O OG . SER A 1 164 ? 12.352 14.275 50.849 1.00 16.86 ? 164 SER A OG 1 ATOM 1273 N N . GLU A 1 165 ? 14.787 15.818 51.372 1.00 16.50 ? 165 GLU A N 1 ATOM 1274 C CA . GLU A 1 165 ? 15.946 15.277 52.138 1.00 17.85 ? 165 GLU A CA 1 ATOM 1275 C C . GLU A 1 165 ? 15.929 13.727 52.258 1.00 17.54 ? 165 GLU A C 1 ATOM 1276 O O . GLU A 1 165 ? 16.940 13.140 52.681 1.00 19.55 ? 165 GLU A O 1 ATOM 1277 C CB . GLU A 1 165 ? 16.018 15.867 53.550 1.00 19.31 ? 165 GLU A CB 1 ATOM 1278 C CG . GLU A 1 165 ? 14.918 15.308 54.478 1.00 19.48 ? 165 GLU A CG 1 ATOM 1279 C CD . GLU A 1 165 ? 14.719 16.117 55.733 1.00 21.55 ? 165 GLU A CD 1 ATOM 1280 O OE1 . GLU A 1 165 ? 14.990 17.331 55.738 1.00 20.90 ? 165 GLU A OE1 1 ATOM 1281 O OE2 . GLU A 1 165 ? 14.248 15.496 56.722 1.00 22.13 ? 165 GLU A OE2 1 ATOM 1282 N N . ASP A 1 166 ? 14.791 13.114 51.926 1.00 18.29 ? 166 ASP A N 1 ATOM 1283 C CA . ASP A 1 166 ? 14.581 11.654 51.962 1.00 18.84 ? 166 ASP A CA 1 ATOM 1284 C C . ASP A 1 166 ? 14.770 11.122 50.536 1.00 18.62 ? 166 ASP A C 1 ATOM 1285 O O . ASP A 1 166 ? 13.967 11.397 49.605 1.00 17.64 ? 166 ASP A O 1 ATOM 1286 C CB . ASP A 1 166 ? 13.150 11.375 52.470 1.00 21.43 ? 166 ASP A CB 1 ATOM 1287 C CG . ASP A 1 166 ? 12.802 9.882 52.560 1.00 24.26 ? 166 ASP A CG 1 ATOM 1288 O OD1 . ASP A 1 166 ? 13.531 8.985 52.091 1.00 24.08 ? 166 ASP A OD1 1 ATOM 1289 O OD2 . ASP A 1 166 ? 11.740 9.607 53.190 1.00 31.31 ? 166 ASP A OD2 1 ATOM 1290 N N . ARG A 1 167 ? 15.835 10.343 50.365 1.00 18.89 ? 167 ARG A N 1 ATOM 1291 C CA . ARG A 1 167 ? 16.139 9.779 49.042 1.00 19.44 ? 167 ARG A CA 1 ATOM 1292 C C . ARG A 1 167 ? 15.000 8.953 48.473 1.00 19.48 ? 167 ARG A C 1 ATOM 1293 O O . ARG A 1 167 ? 14.901 8.810 47.248 1.00 18.68 ? 167 ARG A O 1 ATOM 1294 C CB . ARG A 1 167 ? 17.475 8.983 49.051 1.00 20.56 ? 167 ARG A CB 1 ATOM 1295 C CG . ARG A 1 167 ? 17.504 7.863 50.065 1.00 25.10 ? 167 ARG A CG 1 ATOM 1296 C CD . ARG A 1 167 ? 17.221 6.520 49.431 1.00 29.66 ? 167 ARG A CD 1 ATOM 1297 N NE . ARG A 1 167 ? 17.374 5.463 50.427 1.00 36.30 ? 167 ARG A NE 1 ATOM 1298 C CZ . ARG A 1 167 ? 16.897 4.235 50.277 1.00 38.25 ? 167 ARG A CZ 1 ATOM 1299 N NH1 . ARG A 1 167 ? 17.082 3.329 51.243 1.00 41.02 ? 167 ARG A NH1 1 ATOM 1300 N NH2 . ARG A 1 167 ? 16.261 3.899 49.164 1.00 33.09 ? 167 ARG A NH2 1 ATOM 1301 N N . ARG A 1 168 ? 14.149 8.362 49.333 1.00 19.79 ? 168 ARG A N 1 ATOM 1302 C CA . ARG A 1 168 ? 13.020 7.598 48.790 1.00 20.41 ? 168 ARG A CA 1 ATOM 1303 C C . ARG A 1 168 ? 12.058 8.478 47.959 1.00 17.97 ? 168 ARG A C 1 ATOM 1304 O O . ARG A 1 168 ? 11.516 8.033 46.953 1.00 19.78 ? 168 ARG A O 1 ATOM 1305 C CB . ARG A 1 168 ? 12.239 6.851 49.895 1.00 22.36 ? 168 ARG A CB 1 ATOM 1306 C CG . ARG A 1 168 ? 13.110 5.803 50.541 1.00 24.65 ? 168 ARG A CG 1 ATOM 1307 C CD . ARG A 1 168 ? 12.542 5.272 51.847 1.00 27.64 ? 168 ARG A CD 1 ATOM 1308 N NE A ARG A 1 168 ? 13.195 3.992 52.144 0.60 33.86 ? 168 ARG A NE 1 ATOM 1309 N NE B ARG A 1 168 ? 12.297 6.346 52.813 0.40 23.90 ? 168 ARG A NE 1 ATOM 1310 C CZ A ARG A 1 168 ? 14.174 3.801 53.034 0.60 37.42 ? 168 ARG A CZ 1 ATOM 1311 C CZ B ARG A 1 168 ? 11.639 6.196 53.964 0.40 24.81 ? 168 ARG A CZ 1 ATOM 1312 N NH1 A ARG A 1 168 ? 14.648 4.806 53.766 0.60 40.63 ? 168 ARG A NH1 1 ATOM 1313 N NH1 B ARG A 1 168 ? 11.466 7.232 54.771 0.40 23.51 ? 168 ARG A NH1 1 ATOM 1314 N NH2 A ARG A 1 168 ? 14.677 2.586 53.211 0.60 39.58 ? 168 ARG A NH2 1 ATOM 1315 N NH2 B ARG A 1 168 ? 11.182 4.995 54.327 0.40 25.71 ? 168 ARG A NH2 1 ATOM 1316 N N . ILE A 1 169 ? 11.833 9.685 48.433 1.00 19.13 ? 169 ILE A N 1 ATOM 1317 C CA . ILE A 1 169 ? 10.978 10.626 47.703 1.00 17.37 ? 169 ILE A CA 1 ATOM 1318 C C . ILE A 1 169 ? 11.667 11.070 46.402 1.00 17.66 ? 169 ILE A C 1 ATOM 1319 O O . ILE A 1 169 ? 11.048 11.032 45.327 1.00 18.16 ? 169 ILE A O 1 ATOM 1320 C CB . ILE A 1 169 ? 10.649 11.830 48.585 1.00 18.05 ? 169 ILE A CB 1 ATOM 1321 C CG1 . ILE A 1 169 ? 9.757 11.342 49.761 1.00 19.52 ? 169 ILE A CG1 1 ATOM 1322 C CG2 . ILE A 1 169 ? 9.859 12.879 47.781 1.00 19.21 ? 169 ILE A CG2 1 ATOM 1323 C CD1 . ILE A 1 169 ? 9.457 12.444 50.762 1.00 19.97 ? 169 ILE A CD1 1 ATOM 1324 N N . VAL A 1 170 ? 12.968 11.382 46.489 1.00 16.69 ? 170 VAL A N 1 ATOM 1325 C CA . VAL A 1 170 ? 13.736 11.701 45.255 1.00 16.24 ? 170 VAL A CA 1 ATOM 1326 C C . VAL A 1 170 ? 13.680 10.552 44.254 1.00 16.38 ? 170 VAL A C 1 ATOM 1327 O O . VAL A 1 170 ? 13.418 10.765 43.054 1.00 16.57 ? 170 VAL A O 1 ATOM 1328 C CB . VAL A 1 170 ? 15.182 12.074 45.584 1.00 15.31 ? 170 VAL A CB 1 ATOM 1329 C CG1 . VAL A 1 170 ? 15.975 12.329 44.301 1.00 15.29 ? 170 VAL A CG1 1 ATOM 1330 C CG2 . VAL A 1 170 ? 15.230 13.288 46.496 1.00 15.63 ? 170 VAL A CG2 1 ATOM 1331 N N . GLN A 1 171 ? 13.917 9.313 44.713 1.00 16.67 ? 171 GLN A N 1 ATOM 1332 C CA . GLN A 1 171 ? 13.756 8.162 43.814 1.00 17.38 ? 171 GLN A CA 1 ATOM 1333 C C . GLN A 1 171 ? 12.380 8.124 43.163 1.00 17.86 ? 171 GLN A C 1 ATOM 1334 O O . GLN A 1 171 ? 12.286 7.824 41.960 1.00 19.40 ? 171 GLN A O 1 ATOM 1335 C CB . GLN A 1 171 ? 13.948 6.844 44.588 1.00 17.77 ? 171 GLN A CB 1 ATOM 1336 C CG . GLN A 1 171 ? 15.380 6.632 45.041 1.00 18.98 ? 171 GLN A CG 1 ATOM 1337 C CD . GLN A 1 171 ? 15.528 5.324 45.814 1.00 20.84 ? 171 GLN A CD 1 ATOM 1338 O OE1 . GLN A 1 171 ? 15.915 4.285 45.268 1.00 24.72 ? 171 GLN A OE1 1 ATOM 1339 N NE2 . GLN A 1 171 ? 15.224 5.384 47.089 1.00 20.54 ? 171 GLN A NE2 1 ATOM 1340 N N . SER A 1 172 ? 11.302 8.342 43.945 1.00 17.29 ? 172 SER A N 1 ATOM 1341 C CA . SER A 1 172 ? 9.958 8.268 43.343 1.00 17.76 ? 172 SER A CA 1 ATOM 1342 C C . SER A 1 172 ? 9.756 9.330 42.232 1.00 17.47 ? 172 SER A C 1 ATOM 1343 O O . SER A 1 172 ? 9.050 9.061 41.243 1.00 18.85 ? 172 SER A O 1 ATOM 1344 C CB . SER A 1 172 ? 8.842 8.387 44.392 1.00 19.42 ? 172 SER A CB 1 ATOM 1345 O OG . SER A 1 172 ? 8.772 9.711 44.903 1.00 21.71 ? 172 SER A OG 1 ATOM 1346 N N . MET A 1 173 ? 10.399 10.488 42.408 1.00 16.99 ? 173 MET A N 1 ATOM 1347 C CA . MET A 1 173 ? 10.202 11.602 41.473 1.00 17.13 ? 173 MET A CA 1 ATOM 1348 C C . MET A 1 173 ? 11.076 11.509 40.225 1.00 17.77 ? 173 MET A C 1 ATOM 1349 O O . MET A 1 173 ? 10.971 12.346 39.327 1.00 17.61 ? 173 MET A O 1 ATOM 1350 C CB . MET A 1 173 ? 10.367 12.942 42.207 1.00 18.25 ? 173 MET A CB 1 ATOM 1351 C CG . MET A 1 173 ? 9.530 12.981 43.467 1.00 19.68 ? 173 MET A CG 1 ATOM 1352 S SD A MET A 1 173 ? 7.833 13.032 42.869 0.60 18.18 ? 173 MET A SD 1 ATOM 1353 S SD B MET A 1 173 ? 8.308 14.194 43.840 0.40 18.63 ? 173 MET A SD 1 ATOM 1354 C CE A MET A 1 173 ? 6.834 13.564 44.288 0.60 17.62 ? 173 MET A CE 1 ATOM 1355 C CE B MET A 1 173 ? 7.070 13.239 44.724 0.40 18.50 ? 173 MET A CE 1 ATOM 1356 N N . THR A 1 174 ? 11.899 10.468 40.141 1.00 17.37 ? 174 THR A N 1 ATOM 1357 C CA . THR A 1 174 ? 12.594 10.223 38.855 1.00 17.06 ? 174 THR A CA 1 ATOM 1358 C C . THR A 1 174 ? 11.604 9.900 37.728 1.00 16.76 ? 174 THR A C 1 ATOM 1359 O O . THR A 1 174 ? 12.006 9.771 36.578 1.00 17.01 ? 174 THR A O 1 ATOM 1360 C CB . THR A 1 174 ? 13.654 9.108 38.958 1.00 17.82 ? 174 THR A CB 1 ATOM 1361 O OG1 . THR A 1 174 ? 13.024 7.877 39.371 1.00 17.62 ? 174 THR A OG1 1 ATOM 1362 C CG2 . THR A 1 174 ? 14.809 9.494 39.878 1.00 17.61 ? 174 THR A CG2 1 ATOM 1363 N N . GLU A 1 175 ? 10.304 9.770 38.037 1.00 16.47 ? 175 GLU A N 1 ATOM 1364 C CA . GLU A 1 175 ? 9.278 9.705 37.012 1.00 16.23 ? 175 GLU A CA 1 ATOM 1365 C C . GLU A 1 175 ? 9.294 10.934 36.077 1.00 15.59 ? 175 GLU A C 1 ATOM 1366 O O . GLU A 1 175 ? 8.710 10.875 34.965 1.00 15.95 ? 175 GLU A O 1 ATOM 1367 C CB . GLU A 1 175 ? 7.860 9.567 37.612 1.00 16.98 ? 175 GLU A CB 1 ATOM 1368 C CG . GLU A 1 175 ? 7.549 8.170 38.125 1.00 19.38 ? 175 GLU A CG 1 ATOM 1369 C CD . GLU A 1 175 ? 7.543 7.164 36.992 1.00 19.20 ? 175 GLU A CD 1 ATOM 1370 O OE1 . GLU A 1 175 ? 8.564 6.491 36.821 1.00 22.52 ? 175 GLU A OE1 1 ATOM 1371 O OE2 . GLU A 1 175 ? 6.539 7.093 36.250 1.00 22.74 ? 175 GLU A OE2 1 ATOM 1372 N N . LEU A 1 176 ? 9.968 12.010 36.482 1.00 14.81 ? 176 LEU A N 1 ATOM 1373 C CA . LEU A 1 176 ? 10.139 13.114 35.547 1.00 14.54 ? 176 LEU A CA 1 ATOM 1374 C C . LEU A 1 176 ? 10.784 12.646 34.252 1.00 14.86 ? 176 LEU A C 1 ATOM 1375 O O . LEU A 1 176 ? 10.416 13.146 33.147 1.00 14.07 ? 176 LEU A O 1 ATOM 1376 C CB . LEU A 1 176 ? 10.985 14.221 36.148 1.00 13.87 ? 176 LEU A CB 1 ATOM 1377 C CG . LEU A 1 176 ? 10.995 15.531 35.314 1.00 13.53 ? 176 LEU A CG 1 ATOM 1378 C CD1 . LEU A 1 176 ? 9.726 16.385 35.560 1.00 13.97 ? 176 LEU A CD1 1 ATOM 1379 C CD2 . LEU A 1 176 ? 12.249 16.339 35.610 1.00 13.78 ? 176 LEU A CD2 1 ATOM 1380 N N . ILE A 1 177 ? 11.737 11.706 34.394 1.00 14.00 ? 177 ILE A N 1 ATOM 1381 C CA . ILE A 1 177 ? 12.521 11.219 33.230 1.00 14.51 ? 177 ILE A CA 1 ATOM 1382 C C . ILE A 1 177 ? 11.665 10.644 32.085 1.00 14.17 ? 177 ILE A C 1 ATOM 1383 O O . ILE A 1 177 ? 11.755 11.131 30.945 1.00 14.27 ? 177 ILE A O 1 ATOM 1384 C CB . ILE A 1 177 ? 13.689 10.301 33.689 1.00 15.32 ? 177 ILE A CB 1 ATOM 1385 C CG1 . ILE A 1 177 ? 14.649 11.163 34.524 1.00 15.89 ? 177 ILE A CG1 1 ATOM 1386 C CG2 . ILE A 1 177 ? 14.363 9.595 32.482 1.00 15.13 ? 177 ILE A CG2 1 ATOM 1387 C CD1 . ILE A 1 177 ? 15.640 10.385 35.402 1.00 16.96 ? 177 ILE A CD1 1 ATOM 1388 N N . PRO A 1 178 ? 10.805 9.630 32.352 1.00 13.90 ? 178 PRO A N 1 ATOM 1389 C CA . PRO A 1 178 ? 9.985 9.134 31.256 1.00 14.62 ? 178 PRO A CA 1 ATOM 1390 C C . PRO A 1 178 ? 8.912 10.128 30.836 1.00 14.63 ? 178 PRO A C 1 ATOM 1391 O O . PRO A 1 178 ? 8.367 9.995 29.746 1.00 15.66 ? 178 PRO A O 1 ATOM 1392 C CB . PRO A 1 178 ? 9.350 7.840 31.827 1.00 15.42 ? 178 PRO A CB 1 ATOM 1393 C CG . PRO A 1 178 ? 9.477 8.015 33.336 1.00 14.33 ? 178 PRO A CG 1 ATOM 1394 C CD . PRO A 1 178 ? 10.765 8.749 33.545 1.00 14.95 ? 178 PRO A CD 1 ATOM 1395 N N . GLY A 1 179 ? 8.614 11.127 31.682 1.00 14.17 ? 179 GLY A N 1 ATOM 1396 C CA . GLY A 1 179 ? 7.777 12.294 31.220 1.00 14.21 ? 179 GLY A CA 1 ATOM 1397 C C . GLY A 1 179 ? 8.479 13.054 30.097 1.00 13.69 ? 179 GLY A C 1 ATOM 1398 O O . GLY A 1 179 ? 7.922 13.290 29.003 1.00 14.80 ? 179 GLY A O 1 ATOM 1399 N N . LEU A 1 180 ? 9.701 13.470 30.406 1.00 13.98 ? 180 LEU A N 1 ATOM 1400 C CA . LEU A 1 180 ? 10.497 14.242 29.444 1.00 13.20 ? 180 LEU A CA 1 ATOM 1401 C C . LEU A 1 180 ? 10.849 13.458 28.181 1.00 13.44 ? 180 LEU A C 1 ATOM 1402 O O . LEU A 1 180 ? 10.807 13.994 27.061 1.00 13.01 ? 180 LEU A O 1 ATOM 1403 C CB . LEU A 1 180 ? 11.818 14.660 30.103 1.00 12.98 ? 180 LEU A CB 1 ATOM 1404 C CG . LEU A 1 180 ? 11.696 15.802 31.136 1.00 13.36 ? 180 LEU A CG 1 ATOM 1405 C CD1 . LEU A 1 180 ? 13.048 15.864 31.875 1.00 14.79 ? 180 LEU A CD1 1 ATOM 1406 C CD2 . LEU A 1 180 ? 11.394 17.185 30.519 1.00 13.29 ? 180 LEU A CD2 1 ATOM 1407 N N . GLN A 1 181 ? 11.227 12.168 28.371 1.00 13.14 ? 181 GLN A N 1 ATOM 1408 C CA . GLN A 1 181 ? 11.833 11.369 27.287 1.00 13.67 ? 181 GLN A CA 1 ATOM 1409 C C . GLN A 1 181 ? 10.883 10.389 26.616 1.00 14.46 ? 181 GLN A C 1 ATOM 1410 O O . GLN A 1 181 ? 11.128 9.945 25.483 1.00 15.45 ? 181 GLN A O 1 ATOM 1411 C CB . GLN A 1 181 ? 12.973 10.523 27.866 1.00 13.34 ? 181 GLN A CB 1 ATOM 1412 C CG . GLN A 1 181 ? 14.129 11.336 28.466 1.00 13.61 ? 181 GLN A CG 1 ATOM 1413 C CD . GLN A 1 181 ? 15.335 10.449 28.731 1.00 14.34 ? 181 GLN A CD 1 ATOM 1414 O OE1 . GLN A 1 181 ? 15.197 9.254 29.157 1.00 16.61 ? 181 GLN A OE1 1 ATOM 1415 N NE2 . GLN A 1 181 ? 16.508 10.970 28.479 1.00 11.70 ? 181 GLN A NE2 1 ATOM 1416 N N . GLY A 1 182 ? 9.778 10.088 27.288 1.00 15.20 ? 182 GLY A N 1 ATOM 1417 C CA . GLY A 1 182 ? 8.916 8.968 26.844 1.00 16.49 ? 182 GLY A CA 1 ATOM 1418 C C . GLY A 1 182 ? 9.193 7.739 27.668 1.00 17.06 ? 182 GLY A C 1 ATOM 1419 O O . GLY A 1 182 ? 10.291 7.531 28.164 1.00 16.96 ? 182 GLY A O 1 ATOM 1420 N N . ASP A 1 183 ? 8.161 6.893 27.833 1.00 18.25 ? 183 ASP A N 1 ATOM 1421 C CA . ASP A 1 183 ? 8.366 5.581 28.477 1.00 19.69 ? 183 ASP A CA 1 ATOM 1422 C C . ASP A 1 183 ? 9.234 4.609 27.676 1.00 19.86 ? 183 ASP A C 1 ATOM 1423 O O . ASP A 1 183 ? 9.107 4.514 26.455 1.00 20.59 ? 183 ASP A O 1 ATOM 1424 C CB . ASP A 1 183 ? 6.981 4.946 28.714 1.00 20.15 ? 183 ASP A CB 1 ATOM 1425 C CG . ASP A 1 183 ? 6.226 5.610 29.873 1.00 21.40 ? 183 ASP A CG 1 ATOM 1426 O OD1 . ASP A 1 183 ? 6.777 5.734 30.968 1.00 24.96 ? 183 ASP A OD1 1 ATOM 1427 O OD2 . ASP A 1 183 ? 5.028 5.917 29.712 1.00 29.98 ? 183 ASP A OD2 1 ATOM 1428 N N . VAL A 1 184 ? 10.118 3.911 28.390 1.00 19.97 ? 184 VAL A N 1 ATOM 1429 C CA . VAL A 1 184 ? 10.988 2.874 27.786 1.00 22.00 ? 184 VAL A CA 1 ATOM 1430 C C . VAL A 1 184 ? 10.141 1.639 27.440 1.00 25.77 ? 184 VAL A C 1 ATOM 1431 O O . VAL A 1 184 ? 9.128 1.369 28.099 1.00 27.46 ? 184 VAL A O 1 ATOM 1432 C CB . VAL A 1 184 ? 12.195 2.527 28.694 1.00 21.93 ? 184 VAL A CB 1 ATOM 1433 C CG1 . VAL A 1 184 ? 13.054 3.766 28.983 1.00 20.92 ? 184 VAL A CG1 1 ATOM 1434 C CG2 . VAL A 1 184 ? 11.762 1.866 30.004 1.00 21.63 ? 184 VAL A CG2 1 ATOM 1435 N N . PRO A 1 185 ? 10.526 0.928 26.384 1.00 27.66 ? 185 PRO A N 1 ATOM 1436 C CA . PRO A 1 185 ? 9.806 -0.350 26.062 1.00 32.77 ? 185 PRO A CA 1 ATOM 1437 C C . PRO A 1 185 ? 9.950 -1.431 27.148 1.00 36.69 ? 185 PRO A C 1 ATOM 1438 O O . PRO A 1 185 ? 10.835 -1.338 27.991 1.00 34.23 ? 185 PRO A O 1 ATOM 1439 C CB . PRO A 1 185 ? 10.460 -0.803 24.761 1.00 33.03 ? 185 PRO A CB 1 ATOM 1440 C CG . PRO A 1 185 ? 11.776 -0.147 24.744 1.00 29.98 ? 185 PRO A CG 1 ATOM 1441 C CD . PRO A 1 185 ? 11.613 1.199 25.445 1.00 28.75 ? 185 PRO A CD 1 ATOM 1442 N N . LYS A 1 186 ? 9.075 -2.445 27.134 1.00 43.14 ? 186 LYS A N 1 ATOM 1443 C CA . LYS A 1 186 ? 9.088 -3.474 28.194 1.00 47.23 ? 186 LYS A CA 1 ATOM 1444 C C . LYS A 1 186 ? 10.421 -4.234 28.272 1.00 46.23 ? 186 LYS A C 1 ATOM 1445 O O . LYS A 1 186 ? 10.862 -4.608 29.349 1.00 46.65 ? 186 LYS A O 1 ATOM 1446 C CB . LYS A 1 186 ? 7.904 -4.451 28.052 1.00 55.66 ? 186 LYS A CB 1 ATOM 1447 C CG . LYS A 1 186 ? 8.065 -5.526 26.975 1.00 62.71 ? 186 LYS A CG 1 ATOM 1448 C CD . LYS A 1 186 ? 7.411 -5.118 25.661 1.00 68.97 ? 186 LYS A CD 1 ATOM 1449 C CE . LYS A 1 186 ? 5.934 -5.487 25.659 1.00 72.34 ? 186 LYS A CE 1 ATOM 1450 N NZ . LYS A 1 186 ? 5.113 -4.420 25.025 1.00 75.31 ? 186 LYS A NZ 1 ATOM 1451 N N . ASP A 1 187 ? 11.059 -4.410 27.121 1.00 45.42 ? 187 ASP A N 1 ATOM 1452 C CA . ASP A 1 187 ? 12.312 -5.153 26.969 1.00 51.80 ? 187 ASP A CA 1 ATOM 1453 C C . ASP A 1 187 ? 13.581 -4.366 27.373 1.00 47.62 ? 187 ASP A C 1 ATOM 1454 O O . ASP A 1 187 ? 14.710 -4.822 27.142 1.00 43.84 ? 187 ASP A O 1 ATOM 1455 C CB . ASP A 1 187 ? 12.439 -5.521 25.486 1.00 58.95 ? 187 ASP A CB 1 ATOM 1456 C CG . ASP A 1 187 ? 11.993 -4.372 24.572 1.00 65.31 ? 187 ASP A CG 1 ATOM 1457 O OD1 . ASP A 1 187 ? 12.861 -3.607 24.085 1.00 69.08 ? 187 ASP A OD1 1 ATOM 1458 O OD2 . ASP A 1 187 ? 10.760 -4.205 24.390 1.00 68.09 ? 187 ASP A OD2 1 ATOM 1459 N N . PHE A 1 188 ? 13.407 -3.175 27.940 1.00 39.86 ? 188 PHE A N 1 ATOM 1460 C CA . PHE A 1 188 ? 14.513 -2.215 28.031 1.00 33.20 ? 188 PHE A CA 1 ATOM 1461 C C . PHE A 1 188 ? 15.673 -2.612 28.950 1.00 30.13 ? 188 PHE A C 1 ATOM 1462 O O . PHE A 1 188 ? 15.458 -3.038 30.077 1.00 32.06 ? 188 PHE A O 1 ATOM 1463 C CB . PHE A 1 188 ? 13.954 -0.868 28.498 1.00 29.58 ? 188 PHE A CB 1 ATOM 1464 C CG . PHE A 1 188 ? 14.900 0.271 28.320 1.00 26.82 ? 188 PHE A CG 1 ATOM 1465 C CD1 . PHE A 1 188 ? 15.139 0.781 27.055 1.00 28.41 ? 188 PHE A CD1 1 ATOM 1466 C CD2 . PHE A 1 188 ? 15.531 0.833 29.418 1.00 26.46 ? 188 PHE A CD2 1 ATOM 1467 C CE1 . PHE A 1 188 ? 16.012 1.850 26.860 1.00 27.05 ? 188 PHE A CE1 1 ATOM 1468 C CE2 . PHE A 1 188 ? 16.427 1.888 29.237 1.00 25.33 ? 188 PHE A CE2 1 ATOM 1469 C CZ . PHE A 1 188 ? 16.651 2.386 27.970 1.00 24.41 ? 188 PHE A CZ 1 ATOM 1470 N N . THR A 1 189 ? 16.904 -2.407 28.494 1.00 26.94 ? 189 THR A N 1 ATOM 1471 C CA . THR A 1 189 ? 18.076 -2.647 29.350 1.00 26.41 ? 189 THR A CA 1 ATOM 1472 C C . THR A 1 189 ? 18.472 -1.424 30.176 1.00 23.68 ? 189 THR A C 1 ATOM 1473 O O . THR A 1 189 ? 18.783 -0.349 29.598 1.00 23.51 ? 189 THR A O 1 ATOM 1474 C CB . THR A 1 189 ? 19.279 -3.061 28.490 1.00 27.06 ? 189 THR A CB 1 ATOM 1475 O OG1 . THR A 1 189 ? 18.946 -4.273 27.809 1.00 30.87 ? 189 THR A OG1 1 ATOM 1476 C CG2 . THR A 1 189 ? 20.545 -3.294 29.348 1.00 28.45 ? 189 THR A CG2 1 ATOM 1477 N N . SER A 1 190 ? 18.454 -1.579 31.506 1.00 22.78 ? 190 SER A N 1 ATOM 1478 C CA . SER A 1 190 ? 18.842 -0.492 32.416 1.00 21.50 ? 190 SER A CA 1 ATOM 1479 C C . SER A 1 190 ? 20.208 0.077 32.036 1.00 21.71 ? 190 SER A C 1 ATOM 1480 O O . SER A 1 190 ? 21.179 -0.675 31.807 1.00 22.22 ? 190 SER A O 1 ATOM 1481 C CB . SER A 1 190 ? 18.886 -1.005 33.855 1.00 23.18 ? 190 SER A CB 1 ATOM 1482 O OG . SER A 1 190 ? 19.212 0.044 34.759 1.00 22.01 ? 190 SER A OG 1 ATOM 1483 N N . GLY A 1 191 ? 20.272 1.408 31.975 1.00 18.52 ? 191 GLY A N 1 ATOM 1484 C CA . GLY A 1 191 ? 21.514 2.113 31.624 1.00 19.39 ? 191 GLY A CA 1 ATOM 1485 C C . GLY A 1 191 ? 21.599 2.567 30.176 1.00 19.02 ? 191 GLY A C 1 ATOM 1486 O O . GLY A 1 191 ? 22.433 3.417 29.848 1.00 18.80 ? 191 GLY A O 1 ATOM 1487 N N . MET A 1 192 ? 20.751 2.013 29.310 1.00 18.96 ? 192 MET A N 1 ATOM 1488 C CA . MET A 1 192 ? 20.707 2.497 27.934 1.00 19.04 ? 192 MET A CA 1 ATOM 1489 C C . MET A 1 192 ? 20.012 3.859 27.897 1.00 18.49 ? 192 MET A C 1 ATOM 1490 O O . MET A 1 192 ? 19.147 4.114 28.735 1.00 19.72 ? 192 MET A O 1 ATOM 1491 C CB . MET A 1 192 ? 20.017 1.512 27.030 1.00 21.38 ? 192 MET A CB 1 ATOM 1492 C CG . MET A 1 192 ? 20.871 0.266 26.733 1.00 21.84 ? 192 MET A CG 1 ATOM 1493 S SD . MET A 1 192 ? 22.307 0.613 25.703 1.00 24.58 ? 192 MET A SD 1 ATOM 1494 C CE . MET A 1 192 ? 21.619 0.792 24.085 1.00 24.79 ? 192 MET A CE 1 ATOM 1495 N N . PRO A 1 193 ? 20.380 4.713 26.949 1.00 17.33 ? 193 PRO A N 1 ATOM 1496 C CA . PRO A 1 193 ? 19.663 6.000 26.813 1.00 16.12 ? 193 PRO A CA 1 ATOM 1497 C C . PRO A 1 193 ? 18.403 5.780 26.004 1.00 17.62 ? 193 PRO A C 1 ATOM 1498 O O . PRO A 1 193 ? 18.315 4.881 25.151 1.00 18.98 ? 193 PRO A O 1 ATOM 1499 C CB . PRO A 1 193 ? 20.649 6.885 26.019 1.00 16.29 ? 193 PRO A CB 1 ATOM 1500 C CG . PRO A 1 193 ? 21.409 5.864 25.143 1.00 16.10 ? 193 PRO A CG 1 ATOM 1501 C CD . PRO A 1 193 ? 21.558 4.632 26.047 1.00 17.43 ? 193 PRO A CD 1 ATOM 1502 N N . PHE A 1 194 ? 17.419 6.636 26.235 1.00 15.74 ? 194 PHE A N 1 ATOM 1503 C CA . PHE A 1 194 ? 16.191 6.561 25.484 1.00 16.77 ? 194 PHE A CA 1 ATOM 1504 C C . PHE A 1 194 ? 15.561 7.938 25.299 1.00 15.72 ? 194 PHE A C 1 ATOM 1505 O O . PHE A 1 194 ? 15.478 8.695 26.259 1.00 16.53 ? 194 PHE A O 1 ATOM 1506 C CB . PHE A 1 194 ? 15.177 5.662 26.210 1.00 18.36 ? 194 PHE A CB 1 ATOM 1507 C CG . PHE A 1 194 ? 13.884 5.529 25.467 1.00 19.59 ? 194 PHE A CG 1 ATOM 1508 C CD1 . PHE A 1 194 ? 13.759 4.602 24.434 1.00 20.86 ? 194 PHE A CD1 1 ATOM 1509 C CD2 . PHE A 1 194 ? 12.777 6.345 25.786 1.00 19.00 ? 194 PHE A CD2 1 ATOM 1510 C CE1 . PHE A 1 194 ? 12.553 4.488 23.749 1.00 22.71 ? 194 PHE A CE1 1 ATOM 1511 C CE2 . PHE A 1 194 ? 11.589 6.230 25.096 1.00 19.95 ? 194 PHE A CE2 1 ATOM 1512 C CZ . PHE A 1 194 ? 11.462 5.303 24.085 1.00 20.86 ? 194 PHE A CZ 1 ATOM 1513 N N . VAL A 1 195 ? 15.087 8.228 24.092 1.00 15.81 ? 195 VAL A N 1 ATOM 1514 C CA . VAL A 1 195 ? 14.136 9.336 23.855 1.00 14.98 ? 195 VAL A CA 1 ATOM 1515 C C . VAL A 1 195 ? 13.193 8.850 22.765 1.00 16.40 ? 195 VAL A C 1 ATOM 1516 O O . VAL A 1 195 ? 13.639 8.260 21.765 1.00 16.73 ? 195 VAL A O 1 ATOM 1517 C CB . VAL A 1 195 ? 14.860 10.647 23.388 1.00 14.62 ? 195 VAL A CB 1 ATOM 1518 C CG1 . VAL A 1 195 ? 13.834 11.763 23.126 1.00 15.38 ? 195 VAL A CG1 1 ATOM 1519 C CG2 . VAL A 1 195 ? 15.870 11.107 24.436 1.00 15.47 ? 195 VAL A CG2 1 ATOM 1520 N N . ALA A 1 196 ? 11.882 9.091 22.922 1.00 16.08 ? 196 ALA A N 1 ATOM 1521 C CA . ALA A 1 196 ? 10.934 8.489 22.002 1.00 17.53 ? 196 ALA A CA 1 ATOM 1522 C C . ALA A 1 196 ? 10.886 9.046 20.599 1.00 20.30 ? 196 ALA A C 1 ATOM 1523 O O . ALA A 1 196 ? 10.513 8.309 19.656 1.00 22.81 ? 196 ALA A O 1 ATOM 1524 C CB . ALA A 1 196 ? 9.549 8.467 22.607 1.00 18.02 ? 196 ALA A CB 1 ATOM 1525 N N . GLY A 1 197 ? 11.274 10.293 20.416 1.00 18.75 ? 197 GLY A N 1 ATOM 1526 C CA . GLY A 1 197 ? 11.166 10.972 19.129 1.00 18.30 ? 197 GLY A CA 1 ATOM 1527 C C . GLY A 1 197 ? 11.057 12.483 19.290 1.00 19.68 ? 197 GLY A C 1 ATOM 1528 O O . GLY A 1 197 ? 11.408 13.023 20.344 1.00 17.44 ? 197 GLY A O 1 ATOM 1529 N N . LYS A 1 198 ? 10.509 13.146 18.261 1.00 18.74 ? 198 LYS A N 1 ATOM 1530 C CA . LYS A 1 198 ? 10.710 14.591 18.074 1.00 18.83 ? 198 LYS A CA 1 ATOM 1531 C C . LYS A 1 198 ? 9.838 15.399 19.025 1.00 17.80 ? 198 LYS A C 1 ATOM 1532 O O . LYS A 1 198 ? 10.014 16.639 19.128 1.00 17.75 ? 198 LYS A O 1 ATOM 1533 C CB . LYS A 1 198 ? 10.510 14.989 16.584 1.00 18.23 ? 198 LYS A CB 1 ATOM 1534 C CG . LYS A 1 198 ? 9.038 14.846 16.151 1.00 21.08 ? 198 LYS A CG 1 ATOM 1535 C CD . LYS A 1 198 ? 8.915 15.049 14.639 1.00 23.83 ? 198 LYS A CD 1 ATOM 1536 C CE . LYS A 1 198 ? 7.445 14.941 14.284 1.00 29.76 ? 198 LYS A CE 1 ATOM 1537 N NZ . LYS A 1 198 ? 7.159 15.518 12.938 1.00 37.00 ? 198 LYS A NZ 1 ATOM 1538 N N . ASN A 1 199 ? 8.877 14.754 19.706 1.00 17.60 ? 199 ASN A N 1 ATOM 1539 C CA . ASN A 1 199 ? 8.026 15.465 20.652 1.00 18.19 ? 199 ASN A CA 1 ATOM 1540 C C . ASN A 1 199 ? 8.476 15.316 22.109 1.00 16.95 ? 199 ASN A C 1 ATOM 1541 O O . ASN A 1 199 ? 7.797 15.761 23.046 1.00 18.80 ? 199 ASN A O 1 ATOM 1542 C CB . ASN A 1 199 ? 6.557 15.066 20.444 1.00 22.13 ? 199 ASN A CB 1 ATOM 1543 C CG . ASN A 1 199 ? 6.070 15.390 19.047 1.00 25.15 ? 199 ASN A CG 1 ATOM 1544 O OD1 . ASN A 1 199 ? 5.475 14.542 18.365 1.00 33.49 ? 199 ASN A OD1 1 ATOM 1545 N ND2 . ASN A 1 199 ? 6.397 16.568 18.571 1.00 23.80 ? 199 ASN A ND2 1 ATOM 1546 N N . LYS A 1 200 ? 9.647 14.667 22.288 1.00 15.71 ? 200 LYS A N 1 ATOM 1547 C CA . LYS A 1 200 ? 10.241 14.414 23.605 1.00 14.75 ? 200 LYS A CA 1 ATOM 1548 C C . LYS A 1 200 ? 11.648 15.020 23.570 1.00 13.67 ? 200 LYS A C 1 ATOM 1549 O O . LYS A 1 200 ? 12.117 15.440 22.499 1.00 14.07 ? 200 LYS A O 1 ATOM 1550 C CB . LYS A 1 200 ? 10.315 12.897 23.900 1.00 14.24 ? 200 LYS A CB 1 ATOM 1551 C CG . LYS A 1 200 ? 8.926 12.247 24.042 1.00 15.49 ? 200 LYS A CG 1 ATOM 1552 C CD . LYS A 1 200 ? 8.210 12.782 25.270 1.00 16.68 ? 200 LYS A CD 1 ATOM 1553 C CE . LYS A 1 200 ? 6.896 12.050 25.502 1.00 16.73 ? 200 LYS A CE 1 ATOM 1554 N NZ . LYS A 1 200 ? 6.235 12.552 26.750 1.00 15.93 ? 200 LYS A NZ 1 ATOM 1555 N N . VAL A 1 201 ? 12.246 15.122 24.739 1.00 13.57 ? 201 VAL A N 1 ATOM 1556 C CA . VAL A 1 201 ? 13.620 15.656 24.865 1.00 13.08 ? 201 VAL A CA 1 ATOM 1557 C C . VAL A 1 201 ? 14.545 14.685 25.583 1.00 13.71 ? 201 VAL A C 1 ATOM 1558 O O . VAL A 1 201 ? 14.093 13.842 26.389 1.00 13.66 ? 201 VAL A O 1 ATOM 1559 C CB . VAL A 1 201 ? 13.640 17.066 25.542 1.00 12.49 ? 201 VAL A CB 1 ATOM 1560 C CG1 . VAL A 1 201 ? 12.800 18.068 24.728 1.00 13.22 ? 201 VAL A CG1 1 ATOM 1561 C CG2 . VAL A 1 201 ? 13.176 17.003 27.019 1.00 13.74 ? 201 VAL A CG2 1 ATOM 1562 N N . ALA A 1 202 ? 15.849 14.746 25.279 1.00 12.21 ? 202 ALA A N 1 ATOM 1563 C CA . ALA A 1 202 ? 16.815 14.059 26.149 1.00 12.02 ? 202 ALA A CA 1 ATOM 1564 C C . ALA A 1 202 ? 16.816 14.702 27.546 1.00 12.40 ? 202 ALA A C 1 ATOM 1565 O O . ALA A 1 202 ? 16.748 15.967 27.674 1.00 12.70 ? 202 ALA A O 1 ATOM 1566 C CB . ALA A 1 202 ? 18.241 14.168 25.544 1.00 13.00 ? 202 ALA A CB 1 ATOM 1567 N N . ALA A 1 203 ? 16.913 13.871 28.577 1.00 12.33 ? 203 ALA A N 1 ATOM 1568 C CA . ALA A 1 203 ? 16.998 14.321 29.967 1.00 11.96 ? 203 ALA A CA 1 ATOM 1569 C C . ALA A 1 203 ? 18.425 14.230 30.544 1.00 12.44 ? 203 ALA A C 1 ATOM 1570 O O . ALA A 1 203 ? 19.324 13.736 29.844 1.00 13.55 ? 203 ALA A O 1 ATOM 1571 C CB . ALA A 1 203 ? 15.989 13.552 30.837 1.00 12.71 ? 203 ALA A CB 1 ATOM 1572 N N . CYS A 1 204 ? 18.616 14.669 31.790 1.00 12.79 ? 204 CYS A N 1 ATOM 1573 C CA . CYS A 1 204 ? 19.933 14.724 32.414 1.00 12.77 ? 204 CYS A CA 1 ATOM 1574 C C . CYS A 1 204 ? 19.768 14.576 33.913 1.00 13.08 ? 204 CYS A C 1 ATOM 1575 O O . CYS A 1 204 ? 19.280 15.483 34.542 1.00 13.29 ? 204 CYS A O 1 ATOM 1576 C CB . CYS A 1 204 ? 20.533 16.096 32.117 1.00 13.16 ? 204 CYS A CB 1 ATOM 1577 S SG . CYS A 1 204 ? 22.200 16.293 32.814 1.00 14.92 ? 204 CYS A SG 1 ATOM 1578 N N . ALA A 1 205 ? 20.190 13.451 34.463 1.00 13.85 ? 205 ALA A N 1 ATOM 1579 C CA . ALA A 1 205 ? 20.189 13.311 35.922 1.00 13.22 ? 205 ALA A CA 1 ATOM 1580 C C . ALA A 1 205 ? 21.400 14.065 36.445 1.00 13.86 ? 205 ALA A C 1 ATOM 1581 O O . ALA A 1 205 ? 22.544 13.807 35.989 1.00 14.52 ? 205 ALA A O 1 ATOM 1582 C CB . ALA A 1 205 ? 20.301 11.839 36.286 1.00 14.14 ? 205 ALA A CB 1 ATOM 1583 N N . LYS A 1 206 ? 21.189 14.990 37.379 1.00 13.82 ? 206 LYS A N 1 ATOM 1584 C CA . LYS A 1 206 ? 22.309 15.841 37.847 1.00 13.86 ? 206 LYS A CA 1 ATOM 1585 C C . LYS A 1 206 ? 22.191 16.102 39.352 1.00 14.46 ? 206 LYS A C 1 ATOM 1586 O O . LYS A 1 206 ? 21.083 15.972 39.903 1.00 14.80 ? 206 LYS A O 1 ATOM 1587 C CB . LYS A 1 206 ? 22.386 17.160 37.007 1.00 13.40 ? 206 LYS A CB 1 ATOM 1588 C CG . LYS A 1 206 ? 21.311 18.218 37.340 1.00 14.16 ? 206 LYS A CG 1 ATOM 1589 C CD . LYS A 1 206 ? 21.371 19.403 36.360 1.00 13.51 ? 206 LYS A CD 1 ATOM 1590 C CE . LYS A 1 206 ? 20.438 20.511 36.843 1.00 12.59 ? 206 LYS A CE 1 ATOM 1591 N NZ . LYS A 1 206 ? 20.437 21.655 35.855 1.00 12.37 ? 206 LYS A NZ 1 ATOM 1592 N N . HIS A 1 207 ? 23.252 16.481 40.056 1.00 14.42 ? 207 HIS A N 1 ATOM 1593 C CA . HIS A 1 207 ? 24.641 16.509 39.579 1.00 15.18 ? 207 HIS A CA 1 ATOM 1594 C C . HIS A 1 207 ? 25.384 15.385 40.303 1.00 15.16 ? 207 HIS A C 1 ATOM 1595 O O . HIS A 1 207 ? 25.323 15.270 41.535 1.00 16.65 ? 207 HIS A O 1 ATOM 1596 C CB . HIS A 1 207 ? 25.322 17.863 39.893 1.00 15.08 ? 207 HIS A CB 1 ATOM 1597 C CG . HIS A 1 207 ? 24.500 19.074 39.546 1.00 14.89 ? 207 HIS A CG 1 ATOM 1598 N ND1 . HIS A 1 207 ? 23.542 19.567 40.411 1.00 16.17 ? 207 HIS A ND1 1 ATOM 1599 C CD2 . HIS A 1 207 ? 24.490 19.883 38.450 1.00 15.20 ? 207 HIS A CD2 1 ATOM 1600 C CE1 . HIS A 1 207 ? 22.981 20.649 39.866 1.00 15.41 ? 207 HIS A CE1 1 ATOM 1601 N NE2 . HIS A 1 207 ? 23.528 20.853 38.678 1.00 15.11 ? 207 HIS A NE2 1 ATOM 1602 N N . PHE A 1 208 ? 26.080 14.549 39.521 1.00 15.27 ? 208 PHE A N 1 ATOM 1603 C CA . PHE A 1 208 ? 26.608 13.270 40.017 1.00 15.55 ? 208 PHE A CA 1 ATOM 1604 C C . PHE A 1 208 ? 27.923 13.560 40.742 1.00 16.12 ? 208 PHE A C 1 ATOM 1605 O O . PHE A 1 208 ? 28.855 14.082 40.144 1.00 16.98 ? 208 PHE A O 1 ATOM 1606 C CB . PHE A 1 208 ? 26.786 12.339 38.801 1.00 16.14 ? 208 PHE A CB 1 ATOM 1607 C CG . PHE A 1 208 ? 27.347 10.980 39.145 1.00 16.92 ? 208 PHE A CG 1 ATOM 1608 C CD1 . PHE A 1 208 ? 26.499 9.926 39.473 1.00 16.40 ? 208 PHE A CD1 1 ATOM 1609 C CD2 . PHE A 1 208 ? 28.728 10.781 39.084 1.00 16.45 ? 208 PHE A CD2 1 ATOM 1610 C CE1 . PHE A 1 208 ? 27.024 8.658 39.795 1.00 17.53 ? 208 PHE A CE1 1 ATOM 1611 C CE2 . PHE A 1 208 ? 29.265 9.504 39.392 1.00 16.95 ? 208 PHE A CE2 1 ATOM 1612 C CZ . PHE A 1 208 ? 28.418 8.452 39.704 1.00 17.82 ? 208 PHE A CZ 1 ATOM 1613 N N . VAL A 1 209 ? 28.051 13.254 42.039 1.00 15.70 ? 209 VAL A N 1 ATOM 1614 C CA . VAL A 1 209 ? 27.045 12.723 42.965 1.00 16.50 ? 209 VAL A CA 1 ATOM 1615 C C . VAL A 1 209 ? 27.327 13.339 44.327 1.00 17.06 ? 209 VAL A C 1 ATOM 1616 O O . VAL A 1 209 ? 28.443 13.754 44.613 1.00 19.20 ? 209 VAL A O 1 ATOM 1617 C CB . VAL A 1 209 ? 27.096 11.168 43.042 1.00 16.27 ? 209 VAL A CB 1 ATOM 1618 C CG1 . VAL A 1 209 ? 28.501 10.696 43.465 1.00 18.03 ? 209 VAL A CG1 1 ATOM 1619 C CG2 . VAL A 1 209 ? 26.038 10.560 43.969 1.00 17.23 ? 209 VAL A CG2 1 ATOM 1620 N N . GLY A 1 210 ? 26.276 13.488 45.142 1.00 18.06 ? 210 GLY A N 1 ATOM 1621 C CA . GLY A 1 210 ? 26.465 14.070 46.490 1.00 18.84 ? 210 GLY A CA 1 ATOM 1622 C C . GLY A 1 210 ? 26.397 15.580 46.550 1.00 18.84 ? 210 GLY A C 1 ATOM 1623 O O . GLY A 1 210 ? 26.841 16.202 47.509 1.00 19.70 ? 210 GLY A O 1 ATOM 1624 N N . ASP A 1 211 ? 25.815 16.202 45.501 1.00 18.06 ? 211 ASP A N 1 ATOM 1625 C CA . ASP A 1 211 ? 25.637 17.644 45.483 1.00 17.73 ? 211 ASP A CA 1 ATOM 1626 C C . ASP A 1 211 ? 24.797 18.187 46.619 1.00 17.69 ? 211 ASP A C 1 ATOM 1627 O O . ASP A 1 211 ? 25.040 19.304 47.054 1.00 18.51 ? 211 ASP A O 1 ATOM 1628 C CB . ASP A 1 211 ? 25.088 18.187 44.119 1.00 17.12 ? 211 ASP A CB 1 ATOM 1629 C CG . ASP A 1 211 ? 23.889 17.394 43.549 1.00 16.42 ? 211 ASP A CG 1 ATOM 1630 O OD1 . ASP A 1 211 ? 23.610 16.256 44.002 1.00 17.30 ? 211 ASP A OD1 1 ATOM 1631 O OD2 . ASP A 1 211 ? 23.220 17.960 42.611 1.00 16.18 ? 211 ASP A OD2 1 ATOM 1632 N N . GLY A 1 212 ? 23.872 17.360 47.119 1.00 19.02 ? 212 GLY A N 1 ATOM 1633 C CA . GLY A 1 212 ? 23.050 17.771 48.266 1.00 19.36 ? 212 GLY A CA 1 ATOM 1634 C C . GLY A 1 212 ? 23.698 17.521 49.627 1.00 21.93 ? 212 GLY A C 1 ATOM 1635 O O . GLY A 1 212 ? 23.077 17.699 50.664 1.00 20.81 ? 212 GLY A O 1 ATOM 1636 N N . GLY A 1 213 ? 24.957 17.088 49.628 1.00 21.50 ? 213 GLY A N 1 ATOM 1637 C CA . GLY A 1 213 ? 25.559 16.610 50.872 1.00 26.69 ? 213 GLY A CA 1 ATOM 1638 C C . GLY A 1 213 ? 26.165 17.710 51.708 1.00 35.35 ? 213 GLY A C 1 ATOM 1639 O O . GLY A 1 213 ? 26.128 17.639 52.981 1.00 39.82 ? 213 GLY A O 1 ATOM 1640 N N . THR A 1 214 ? 26.655 18.736 51.001 1.00 42.55 ? 214 THR A N 1 ATOM 1641 C CA . THR A 1 214 ? 27.887 19.504 51.354 1.00 59.16 ? 214 THR A CA 1 ATOM 1642 C C . THR A 1 214 ? 27.988 20.086 52.794 1.00 69.73 ? 214 THR A C 1 ATOM 1643 O O . THR A 1 214 ? 26.965 20.404 53.415 1.00 77.22 ? 214 THR A O 1 ATOM 1644 C CB . THR A 1 214 ? 28.280 20.569 50.258 1.00 59.26 ? 214 THR A CB 1 ATOM 1645 O OG1 . THR A 1 214 ? 27.183 21.455 49.974 1.00 62.39 ? 214 THR A OG1 1 ATOM 1646 C CG2 . THR A 1 214 ? 28.727 19.908 48.940 1.00 56.00 ? 214 THR A CG2 1 ATOM 1647 N N . VAL A 1 215 ? 29.226 20.190 53.305 1.00 75.87 ? 215 VAL A N 1 ATOM 1648 C CA . VAL A 1 215 ? 29.528 20.771 54.633 1.00 80.71 ? 215 VAL A CA 1 ATOM 1649 C C . VAL A 1 215 ? 29.070 22.240 54.706 1.00 85.67 ? 215 VAL A C 1 ATOM 1650 O O . VAL A 1 215 ? 29.369 23.035 53.804 1.00 81.56 ? 215 VAL A O 1 ATOM 1651 C CB . VAL A 1 215 ? 31.039 20.642 54.993 1.00 77.84 ? 215 VAL A CB 1 ATOM 1652 C CG1 . VAL A 1 215 ? 31.360 21.312 56.323 1.00 76.11 ? 215 VAL A CG1 1 ATOM 1653 C CG2 . VAL A 1 215 ? 31.455 19.182 55.042 1.00 76.91 ? 215 VAL A CG2 1 ATOM 1654 N N . ASP A 1 216 ? 28.335 22.573 55.777 1.00 92.96 ? 216 ASP A N 1 ATOM 1655 C CA . ASP A 1 216 ? 27.714 23.905 56.001 1.00 94.03 ? 216 ASP A CA 1 ATOM 1656 C C . ASP A 1 216 ? 26.682 24.301 54.931 1.00 91.41 ? 216 ASP A C 1 ATOM 1657 O O . ASP A 1 216 ? 26.244 25.453 54.883 1.00 86.40 ? 216 ASP A O 1 ATOM 1658 C CB . ASP A 1 216 ? 28.773 25.018 56.146 1.00 95.14 ? 216 ASP A CB 1 ATOM 1659 C CG . ASP A 1 216 ? 29.684 24.818 57.343 1.00 98.37 ? 216 ASP A CG 1 ATOM 1660 O OD1 . ASP A 1 216 ? 29.172 24.593 58.462 1.00 98.67 ? 216 ASP A OD1 1 ATOM 1661 O OD2 . ASP A 1 216 ? 30.919 24.902 57.162 1.00 99.20 ? 216 ASP A OD2 1 ATOM 1662 N N . GLY A 1 217 ? 26.295 23.341 54.090 1.00 90.72 ? 217 GLY A N 1 ATOM 1663 C CA . GLY A 1 217 ? 25.491 23.610 52.897 1.00 87.58 ? 217 GLY A CA 1 ATOM 1664 C C . GLY A 1 217 ? 26.211 24.501 51.893 1.00 90.59 ? 217 GLY A C 1 ATOM 1665 O O . GLY A 1 217 ? 25.567 25.132 51.054 1.00 90.12 ? 217 GLY A O 1 ATOM 1666 N N . ILE A 1 218 ? 27.544 24.565 51.989 1.00 92.60 ? 218 ILE A N 1 ATOM 1667 C CA . ILE A 1 218 ? 28.367 25.388 51.087 1.00 92.02 ? 218 ILE A CA 1 ATOM 1668 C C . ILE A 1 218 ? 28.407 24.762 49.684 1.00 93.25 ? 218 ILE A C 1 ATOM 1669 O O . ILE A 1 218 ? 28.869 23.631 49.492 1.00 95.82 ? 218 ILE A O 1 ATOM 1670 C CB . ILE A 1 218 ? 29.793 25.678 51.650 1.00 88.26 ? 218 ILE A CB 1 ATOM 1671 C CG1 . ILE A 1 218 ? 29.711 26.554 52.911 1.00 84.56 ? 218 ILE A CG1 1 ATOM 1672 C CG2 . ILE A 1 218 ? 30.666 26.363 50.603 1.00 85.69 ? 218 ILE A CG2 1 ATOM 1673 C CD1 . ILE A 1 218 ? 31.030 26.786 53.622 1.00 81.76 ? 218 ILE A CD1 1 ATOM 1674 N N . ASN A 1 219 ? 27.883 25.521 48.724 1.00 88.00 ? 219 ASN A N 1 ATOM 1675 C CA . ASN A 1 219 ? 27.784 25.148 47.313 1.00 79.90 ? 219 ASN A CA 1 ATOM 1676 C C . ASN A 1 219 ? 29.151 24.896 46.648 1.00 86.53 ? 219 ASN A C 1 ATOM 1677 O O . ASN A 1 219 ? 30.138 25.577 46.969 1.00 87.95 ? 219 ASN A O 1 ATOM 1678 C CB . ASN A 1 219 ? 27.049 26.284 46.597 1.00 63.09 ? 219 ASN A CB 1 ATOM 1679 C CG . ASN A 1 219 ? 26.681 25.955 45.165 1.00 57.28 ? 219 ASN A CG 1 ATOM 1680 O OD1 . ASN A 1 219 ? 25.858 25.083 44.901 1.00 34.76 ? 219 ASN A OD1 1 ATOM 1681 N ND2 . ASN A 1 219 ? 27.259 26.704 44.224 1.00 62.68 ? 219 ASN A ND2 1 ATOM 1682 N N . GLU A 1 220 ? 29.196 23.921 45.729 1.00 87.89 ? 220 GLU A N 1 ATOM 1683 C CA . GLU A 1 220 ? 30.409 23.589 44.953 1.00 84.43 ? 220 GLU A CA 1 ATOM 1684 C C . GLU A 1 220 ? 31.600 23.239 45.856 1.00 84.03 ? 220 GLU A C 1 ATOM 1685 O O . GLU A 1 220 ? 32.720 23.715 45.627 1.00 89.23 ? 220 GLU A O 1 ATOM 1686 C CB . GLU A 1 220 ? 30.803 24.745 44.021 1.00 83.63 ? 220 GLU A CB 1 ATOM 1687 C CG . GLU A 1 220 ? 29.669 25.343 43.208 1.00 86.12 ? 220 GLU A CG 1 ATOM 1688 C CD . GLU A 1 220 ? 30.048 26.652 42.533 1.00 90.29 ? 220 GLU A CD 1 ATOM 1689 O OE1 . GLU A 1 220 ? 31.215 26.777 42.082 1.00 90.21 ? 220 GLU A OE1 1 ATOM 1690 O OE2 . GLU A 1 220 ? 29.174 27.550 42.445 1.00 85.40 ? 220 GLU A OE2 1 ATOM 1691 N N . ASN A 1 221 ? 31.364 22.409 46.872 1.00 75.59 ? 221 ASN A N 1 ATOM 1692 C CA . ASN A 1 221 ? 32.360 22.203 47.927 1.00 68.53 ? 221 ASN A CA 1 ATOM 1693 C C . ASN A 1 221 ? 32.537 20.734 48.319 1.00 60.35 ? 221 ASN A C 1 ATOM 1694 O O . ASN A 1 221 ? 32.346 19.838 47.503 1.00 52.27 ? 221 ASN A O 1 ATOM 1695 C CB . ASN A 1 221 ? 32.011 23.071 49.149 1.00 73.23 ? 221 ASN A CB 1 ATOM 1696 C CG . ASN A 1 221 ? 33.229 23.734 49.783 1.00 78.75 ? 221 ASN A CG 1 ATOM 1697 O OD1 . ASN A 1 221 ? 33.196 24.102 50.959 1.00 81.75 ? 221 ASN A OD1 1 ATOM 1698 N ND2 . ASN A 1 221 ? 34.301 23.901 49.008 1.00 79.71 ? 221 ASN A ND2 1 ATOM 1699 N N . ASN A 1 222 ? 32.900 20.490 49.574 1.00 58.33 ? 222 ASN A N 1 ATOM 1700 C CA . ASN A 1 222 ? 33.232 19.142 50.023 1.00 58.17 ? 222 ASN A CA 1 ATOM 1701 C C . ASN A 1 222 ? 32.060 18.433 50.705 1.00 56.26 ? 222 ASN A C 1 ATOM 1702 O O . ASN A 1 222 ? 31.566 18.902 51.733 1.00 56.77 ? 222 ASN A O 1 ATOM 1703 C CB . ASN A 1 222 ? 34.458 19.187 50.952 1.00 58.93 ? 222 ASN A CB 1 ATOM 1704 C CG . ASN A 1 222 ? 35.280 17.904 50.919 1.00 62.08 ? 222 ASN A CG 1 ATOM 1705 O OD1 . ASN A 1 222 ? 35.014 16.982 50.137 1.00 61.22 ? 222 ASN A OD1 1 ATOM 1706 N ND2 . ASN A 1 222 ? 36.293 17.842 51.779 1.00 60.42 ? 222 ASN A ND2 1 ATOM 1707 N N . THR A 1 223 ? 31.596 17.326 50.125 1.00 50.16 ? 223 THR A N 1 ATOM 1708 C CA . THR A 1 223 ? 30.684 16.443 50.847 1.00 50.78 ? 223 THR A CA 1 ATOM 1709 C C . THR A 1 223 ? 31.502 15.377 51.574 1.00 49.56 ? 223 THR A C 1 ATOM 1710 O O . THR A 1 223 ? 32.185 14.562 50.945 1.00 48.81 ? 223 THR A O 1 ATOM 1711 C CB . THR A 1 223 ? 29.570 15.810 49.961 1.00 52.76 ? 223 THR A CB 1 ATOM 1712 O OG1 . THR A 1 223 ? 30.047 14.619 49.315 1.00 60.12 ? 223 THR A OG1 1 ATOM 1713 C CG2 . THR A 1 223 ? 29.090 16.793 48.921 1.00 45.19 ? 223 THR A CG2 1 ATOM 1714 N N . ILE A 1 224 ? 31.464 15.421 52.904 1.00 52.70 ? 224 ILE A N 1 ATOM 1715 C CA . ILE A 1 224 ? 32.173 14.427 53.717 1.00 53.48 ? 224 ILE A CA 1 ATOM 1716 C C . ILE A 1 224 ? 31.147 13.420 54.217 1.00 51.85 ? 224 ILE A C 1 ATOM 1717 O O . ILE A 1 224 ? 30.215 13.775 54.943 1.00 52.79 ? 224 ILE A O 1 ATOM 1718 C CB . ILE A 1 224 ? 32.966 15.057 54.895 1.00 58.31 ? 224 ILE A CB 1 ATOM 1719 C CG1 . ILE A 1 224 ? 33.735 16.307 54.423 1.00 60.27 ? 224 ILE A CG1 1 ATOM 1720 C CG2 . ILE A 1 224 ? 33.894 14.012 55.526 1.00 58.33 ? 224 ILE A CG2 1 ATOM 1721 C CD1 . ILE A 1 224 ? 34.339 17.146 55.532 1.00 65.32 ? 224 ILE A CD1 1 ATOM 1722 N N . ILE A 1 225 ? 31.306 12.175 53.780 1.00 47.60 ? 225 ILE A N 1 ATOM 1723 C CA . ILE A 1 225 ? 30.431 11.073 54.165 1.00 45.31 ? 225 ILE A CA 1 ATOM 1724 C C . ILE A 1 225 ? 31.119 9.782 53.740 1.00 46.16 ? 225 ILE A C 1 ATOM 1725 O O . ILE A 1 225 ? 31.825 9.756 52.728 1.00 43.19 ? 225 ILE A O 1 ATOM 1726 C CB . ILE A 1 225 ? 29.013 11.212 53.522 1.00 44.36 ? 225 ILE A CB 1 ATOM 1727 C CG1 . ILE A 1 225 ? 27.990 10.301 54.219 1.00 41.35 ? 225 ILE A CG1 1 ATOM 1728 C CG2 . ILE A 1 225 ? 29.048 11.022 51.992 1.00 41.10 ? 225 ILE A CG2 1 ATOM 1729 C CD1 . ILE A 1 225 ? 26.546 10.656 53.904 1.00 44.72 ? 225 ILE A CD1 1 ATOM 1730 N N . ASN A 1 226 ? 30.961 8.711 54.510 1.00 43.84 ? 226 ASN A N 1 ATOM 1731 C CA . ASN A 1 226 ? 31.544 7.446 54.066 1.00 46.42 ? 226 ASN A CA 1 ATOM 1732 C C . ASN A 1 226 ? 30.804 6.848 52.867 1.00 45.95 ? 226 ASN A C 1 ATOM 1733 O O . ASN A 1 226 ? 29.711 7.317 52.492 1.00 40.75 ? 226 ASN A O 1 ATOM 1734 C CB . ASN A 1 226 ? 31.713 6.436 55.221 1.00 49.95 ? 226 ASN A CB 1 ATOM 1735 C CG . ASN A 1 226 ? 30.420 6.152 55.972 1.00 55.20 ? 226 ASN A CG 1 ATOM 1736 O OD1 . ASN A 1 226 ? 29.349 6.682 55.647 1.00 53.53 ? 226 ASN A OD1 1 ATOM 1737 N ND2 . ASN A 1 226 ? 30.518 5.294 56.996 1.00 55.55 ? 226 ASN A ND2 1 ATOM 1738 N N . ARG A 1 227 ? 31.417 5.845 52.243 1.00 45.84 ? 227 ARG A N 1 ATOM 1739 C CA . ARG A 1 227 ? 30.787 5.144 51.128 1.00 47.34 ? 227 ARG A CA 1 ATOM 1740 C C . ARG A 1 227 ? 29.365 4.668 51.480 1.00 47.38 ? 227 ARG A C 1 ATOM 1741 O O . ARG A 1 227 ? 28.465 4.813 50.671 1.00 41.47 ? 227 ARG A O 1 ATOM 1742 C CB . ARG A 1 227 ? 31.655 3.984 50.600 1.00 51.06 ? 227 ARG A CB 1 ATOM 1743 C CG . ARG A 1 227 ? 31.311 3.580 49.166 1.00 57.65 ? 227 ARG A CG 1 ATOM 1744 C CD . ARG A 1 227 ? 31.952 2.265 48.722 1.00 63.19 ? 227 ARG A CD 1 ATOM 1745 N NE . ARG A 1 227 ? 32.090 2.192 47.260 1.00 67.56 ? 227 ARG A NE 1 ATOM 1746 C CZ . ARG A 1 227 ? 31.397 1.383 46.452 1.00 66.95 ? 227 ARG A CZ 1 ATOM 1747 N NH1 . ARG A 1 227 ? 30.486 0.543 46.937 1.00 64.84 ? 227 ARG A NH1 1 ATOM 1748 N NH2 . ARG A 1 227 ? 31.613 1.423 45.143 1.00 66.37 ? 227 ARG A NH2 1 ATOM 1749 N N . GLU A 1 228 ? 29.133 4.103 52.668 1.00 45.40 ? 228 GLU A N 1 ATOM 1750 C CA . GLU A 1 228 ? 27.772 3.632 52.939 1.00 46.11 ? 228 GLU A CA 1 ATOM 1751 C C . GLU A 1 228 ? 26.745 4.781 52.851 1.00 40.80 ? 228 GLU A C 1 ATOM 1752 O O . GLU A 1 228 ? 25.678 4.593 52.289 1.00 42.84 ? 228 GLU A O 1 ATOM 1753 C CB . GLU A 1 228 ? 27.664 2.802 54.232 1.00 54.67 ? 228 GLU A CB 1 ATOM 1754 C CG . GLU A 1 228 ? 27.938 3.554 55.529 1.00 64.07 ? 228 GLU A CG 1 ATOM 1755 C CD . GLU A 1 228 ? 28.078 2.632 56.733 1.00 72.40 ? 228 GLU A CD 1 ATOM 1756 O OE1 . GLU A 1 228 ? 28.391 1.431 56.546 1.00 75.40 ? 228 GLU A OE1 1 ATOM 1757 O OE2 . GLU A 1 228 ? 27.881 3.116 57.874 1.00 75.32 ? 228 GLU A OE2 1 ATOM 1758 N N . GLY A 1 229 ? 27.091 5.966 53.355 1.00 38.00 ? 229 GLY A N 1 ATOM 1759 C CA . GLY A 1 229 ? 26.235 7.151 53.274 1.00 33.76 ? 229 GLY A CA 1 ATOM 1760 C C . GLY A 1 229 ? 26.097 7.727 51.858 1.00 32.08 ? 229 GLY A C 1 ATOM 1761 O O . GLY A 1 229 ? 25.002 8.099 51.422 1.00 31.05 ? 229 GLY A O 1 ATOM 1762 N N . LEU A 1 230 ? 27.205 7.779 51.122 1.00 29.19 ? 230 LEU A N 1 ATOM 1763 C CA . LEU A 1 230 ? 27.130 8.139 49.690 1.00 27.54 ? 230 LEU A CA 1 ATOM 1764 C C . LEU A 1 230 ? 26.171 7.181 49.014 1.00 27.88 ? 230 LEU A C 1 ATOM 1765 O O . LEU A 1 230 ? 25.278 7.598 48.267 1.00 27.31 ? 230 LEU A O 1 ATOM 1766 C CB . LEU A 1 230 ? 28.513 8.074 49.002 1.00 27.68 ? 230 LEU A CB 1 ATOM 1767 C CG . LEU A 1 230 ? 28.507 8.715 47.594 1.00 31.75 ? 230 LEU A CG 1 ATOM 1768 C CD1 . LEU A 1 230 ? 28.500 10.235 47.738 1.00 30.57 ? 230 LEU A CD1 1 ATOM 1769 C CD2 . LEU A 1 230 ? 29.694 8.228 46.789 1.00 33.77 ? 230 LEU A CD2 1 ATOM 1770 N N . MET A 1 231 ? 26.350 5.881 49.249 1.00 26.80 ? 231 MET A N 1 ATOM 1771 C CA . MET A 1 231 ? 25.541 4.879 48.565 1.00 26.94 ? 231 MET A CA 1 ATOM 1772 C C . MET A 1 231 ? 24.122 4.736 49.073 1.00 28.78 ? 231 MET A C 1 ATOM 1773 O O . MET A 1 231 ? 23.262 4.255 48.343 1.00 32.97 ? 231 MET A O 1 ATOM 1774 C CB . MET A 1 231 ? 26.242 3.504 48.582 1.00 28.47 ? 231 MET A CB 1 ATOM 1775 C CG . MET A 1 231 ? 27.581 3.443 47.811 1.00 29.58 ? 231 MET A CG 1 ATOM 1776 S SD A MET A 1 231 ? 27.216 3.556 46.025 0.60 29.85 ? 231 MET A SD 1 ATOM 1777 S SD B MET A 1 231 ? 27.862 4.492 46.360 0.40 28.16 ? 231 MET A SD 1 ATOM 1778 C CE A MET A 1 231 ? 28.833 3.468 45.253 0.60 31.04 ? 231 MET A CE 1 ATOM 1779 C CE B MET A 1 231 ? 29.531 4.073 45.869 0.40 29.95 ? 231 MET A CE 1 ATOM 1780 N N . ASN A 1 232 ? 23.842 5.121 50.309 1.00 28.11 ? 232 ASN A N 1 ATOM 1781 C CA . ASN A 1 232 ? 22.491 4.898 50.795 1.00 30.28 ? 232 ASN A CA 1 ATOM 1782 C C . ASN A 1 232 ? 21.629 6.162 50.731 1.00 26.31 ? 232 ASN A C 1 ATOM 1783 O O . ASN A 1 232 ? 20.397 6.062 50.813 1.00 29.21 ? 232 ASN A O 1 ATOM 1784 C CB . ASN A 1 232 ? 22.501 4.175 52.172 1.00 33.54 ? 232 ASN A CB 1 ATOM 1785 C CG A ASN A 1 232 ? 21.128 4.068 52.837 0.60 37.74 ? 232 ASN A CG 1 ATOM 1786 C CG B ASN A 1 232 ? 23.133 4.988 53.268 0.40 34.44 ? 232 ASN A CG 1 ATOM 1787 O OD1 A ASN A 1 232 ? 20.323 3.186 52.511 0.60 40.27 ? 232 ASN A OD1 1 ATOM 1788 O OD1 B ASN A 1 232 ? 23.072 6.216 53.269 0.40 35.80 ? 232 ASN A OD1 1 ATOM 1789 N ND2 A ASN A 1 232 ? 20.887 4.922 53.828 0.60 37.59 ? 232 ASN A ND2 1 ATOM 1790 N ND2 B ASN A 1 232 ? 23.746 4.294 54.233 0.40 36.74 ? 232 ASN A ND2 1 ATOM 1791 N N . ILE A 1 233 ? 22.272 7.329 50.599 1.00 22.80 ? 233 ILE A N 1 ATOM 1792 C CA . ILE A 1 233 ? 21.523 8.607 50.524 1.00 20.45 ? 233 ILE A CA 1 ATOM 1793 C C . ILE A 1 233 ? 21.608 9.211 49.124 1.00 20.16 ? 233 ILE A C 1 ATOM 1794 O O . ILE A 1 233 ? 20.575 9.456 48.483 1.00 20.41 ? 233 ILE A O 1 ATOM 1795 C CB . ILE A 1 233 ? 22.018 9.626 51.547 1.00 21.47 ? 233 ILE A CB 1 ATOM 1796 C CG1 . ILE A 1 233 ? 21.780 9.083 52.976 1.00 23.25 ? 233 ILE A CG1 1 ATOM 1797 C CG2 . ILE A 1 233 ? 21.324 10.977 51.382 1.00 21.99 ? 233 ILE A CG2 1 ATOM 1798 C CD1 . ILE A 1 233 ? 22.497 9.958 53.974 1.00 25.27 ? 233 ILE A CD1 1 ATOM 1799 N N . HIS A 1 234 ? 22.834 9.442 48.668 1.00 20.86 ? 234 HIS A N 1 ATOM 1800 C CA . HIS A 1 234 ? 23.071 10.283 47.470 1.00 19.59 ? 234 HIS A CA 1 ATOM 1801 C C . HIS A 1 234 ? 23.047 9.586 46.125 1.00 20.26 ? 234 HIS A C 1 ATOM 1802 O O . HIS A 1 234 ? 22.759 10.237 45.106 1.00 18.46 ? 234 HIS A O 1 ATOM 1803 C CB . HIS A 1 234 ? 24.379 11.057 47.657 1.00 19.76 ? 234 HIS A CB 1 ATOM 1804 C CG . HIS A 1 234 ? 24.271 12.075 48.730 1.00 19.55 ? 234 HIS A CG 1 ATOM 1805 N ND1 . HIS A 1 234 ? 24.864 11.945 49.984 1.00 21.25 ? 234 HIS A ND1 1 ATOM 1806 C CD2 . HIS A 1 234 ? 23.462 13.156 48.804 1.00 17.67 ? 234 HIS A CD2 1 ATOM 1807 C CE1 . HIS A 1 234 ? 24.497 12.979 50.732 1.00 18.48 ? 234 HIS A CE1 1 ATOM 1808 N NE2 . HIS A 1 234 ? 23.671 13.737 50.024 1.00 22.62 ? 234 HIS A NE2 1 ATOM 1809 N N . MET A 1 235 ? 23.309 8.282 46.113 1.00 19.17 ? 235 MET A N 1 ATOM 1810 C CA . MET A 1 235 ? 23.427 7.512 44.889 1.00 19.40 ? 235 MET A CA 1 ATOM 1811 C C . MET A 1 235 ? 22.150 6.810 44.405 1.00 20.11 ? 235 MET A C 1 ATOM 1812 O O . MET A 1 235 ? 21.963 6.669 43.208 1.00 20.57 ? 235 MET A O 1 ATOM 1813 C CB . MET A 1 235 ? 24.540 6.442 45.076 1.00 19.18 ? 235 MET A CB 1 ATOM 1814 C CG . MET A 1 235 ? 24.869 5.669 43.819 1.00 19.11 ? 235 MET A CG 1 ATOM 1815 S SD . MET A 1 235 ? 25.614 6.715 42.531 1.00 21.39 ? 235 MET A SD 1 ATOM 1816 C CE . MET A 1 235 ? 27.240 6.933 43.252 1.00 22.04 ? 235 MET A CE 1 ATOM 1817 N N . PRO A 1 236 ? 21.279 6.313 45.298 1.00 21.01 ? 236 PRO A N 1 ATOM 1818 C CA . PRO A 1 236 ? 20.212 5.447 44.784 1.00 20.83 ? 236 PRO A CA 1 ATOM 1819 C C . PRO A 1 236 ? 19.354 5.953 43.623 1.00 19.28 ? 236 PRO A C 1 ATOM 1820 O O . PRO A 1 236 ? 19.016 5.169 42.712 1.00 20.55 ? 236 PRO A O 1 ATOM 1821 C CB . PRO A 1 236 ? 19.339 5.172 46.027 1.00 23.45 ? 236 PRO A CB 1 ATOM 1822 C CG . PRO A 1 236 ? 20.341 5.210 47.121 1.00 24.41 ? 236 PRO A CG 1 ATOM 1823 C CD . PRO A 1 236 ? 21.303 6.323 46.782 1.00 22.56 ? 236 PRO A CD 1 ATOM 1824 N N . ALA A 1 237 ? 18.978 7.236 43.646 1.00 18.75 ? 237 ALA A N 1 ATOM 1825 C CA . ALA A 1 237 ? 18.135 7.755 42.569 1.00 17.90 ? 237 ALA A CA 1 ATOM 1826 C C . ALA A 1 237 ? 18.807 7.695 41.165 1.00 17.44 ? 237 ALA A C 1 ATOM 1827 O O . ALA A 1 237 ? 18.099 7.647 40.148 1.00 17.83 ? 237 ALA A O 1 ATOM 1828 C CB . ALA A 1 237 ? 17.674 9.160 42.891 1.00 17.74 ? 237 ALA A CB 1 ATOM 1829 N N . TYR A 1 238 ? 20.144 7.652 41.136 1.00 17.78 ? 238 TYR A N 1 ATOM 1830 C CA . TYR A 1 238 ? 20.878 7.429 39.849 1.00 17.55 ? 238 TYR A CA 1 ATOM 1831 C C . TYR A 1 238 ? 20.555 6.037 39.277 1.00 17.94 ? 238 TYR A C 1 ATOM 1832 O O . TYR A 1 238 ? 20.425 5.880 38.054 1.00 17.88 ? 238 TYR A O 1 ATOM 1833 C CB . TYR A 1 238 ? 22.416 7.654 39.969 1.00 17.00 ? 238 TYR A CB 1 ATOM 1834 C CG . TYR A 1 238 ? 22.728 9.131 40.020 1.00 16.65 ? 238 TYR A CG 1 ATOM 1835 C CD1 . TYR A 1 238 ? 22.832 9.865 38.817 1.00 15.25 ? 238 TYR A CD1 1 ATOM 1836 C CD2 . TYR A 1 238 ? 22.800 9.838 41.228 1.00 16.88 ? 238 TYR A CD2 1 ATOM 1837 C CE1 . TYR A 1 238 ? 23.008 11.262 38.827 1.00 15.75 ? 238 TYR A CE1 1 ATOM 1838 C CE2 . TYR A 1 238 ? 22.980 11.229 41.263 1.00 16.51 ? 238 TYR A CE2 1 ATOM 1839 C CZ . TYR A 1 238 ? 23.077 11.940 40.054 1.00 16.57 ? 238 TYR A CZ 1 ATOM 1840 O OH . TYR A 1 238 ? 23.263 13.274 40.124 1.00 16.31 ? 238 TYR A OH 1 ATOM 1841 N N . LYS A 1 239 ? 20.419 5.030 40.139 1.00 18.28 ? 239 LYS A N 1 ATOM 1842 C CA . LYS A 1 239 ? 20.050 3.726 39.614 1.00 19.87 ? 239 LYS A CA 1 ATOM 1843 C C . LYS A 1 239 ? 18.620 3.756 39.068 1.00 18.34 ? 239 LYS A C 1 ATOM 1844 O O . LYS A 1 239 ? 18.354 3.216 37.984 1.00 19.49 ? 239 LYS A O 1 ATOM 1845 C CB . LYS A 1 239 ? 20.247 2.635 40.696 1.00 22.35 ? 239 LYS A CB 1 ATOM 1846 C CG . LYS A 1 239 ? 20.114 1.215 40.171 1.00 27.93 ? 239 LYS A CG 1 ATOM 1847 C CD . LYS A 1 239 ? 18.684 0.771 40.350 1.00 31.00 ? 239 LYS A CD 1 ATOM 1848 C CE . LYS A 1 239 ? 18.453 -0.704 40.059 1.00 34.93 ? 239 LYS A CE 1 ATOM 1849 N NZ . LYS A 1 239 ? 17.024 -0.993 40.401 1.00 37.03 ? 239 LYS A NZ 1 ATOM 1850 N N . ASN A 1 240 ? 17.689 4.408 39.788 1.00 18.39 ? 240 ASN A N 1 ATOM 1851 C CA . ASN A 1 240 ? 16.346 4.554 39.208 1.00 18.21 ? 240 ASN A CA 1 ATOM 1852 C C . ASN A 1 240 ? 16.389 5.274 37.828 1.00 17.40 ? 240 ASN A C 1 ATOM 1853 O O . ASN A 1 240 ? 15.665 4.899 36.893 1.00 18.65 ? 240 ASN A O 1 ATOM 1854 C CB . ASN A 1 240 ? 15.375 5.357 40.115 1.00 19.36 ? 240 ASN A CB 1 ATOM 1855 C CG . ASN A 1 240 ? 15.124 4.709 41.472 1.00 21.95 ? 240 ASN A CG 1 ATOM 1856 O OD1 . ASN A 1 240 ? 15.973 4.732 42.346 1.00 22.68 ? 240 ASN A OD1 1 ATOM 1857 N ND2 . ASN A 1 240 ? 13.905 4.227 41.671 1.00 29.09 ? 240 ASN A ND2 1 ATOM 1858 N N . ALA A 1 241 ? 17.251 6.284 37.718 1.00 17.18 ? 241 ALA A N 1 ATOM 1859 C CA . ALA A 1 241 ? 17.425 6.998 36.451 1.00 16.68 ? 241 ALA A CA 1 ATOM 1860 C C . ALA A 1 241 ? 17.950 6.071 35.349 1.00 16.43 ? 241 ALA A C 1 ATOM 1861 O O . ALA A 1 241 ? 17.492 6.167 34.218 1.00 17.61 ? 241 ALA A O 1 ATOM 1862 C CB . ALA A 1 241 ? 18.358 8.225 36.622 1.00 16.86 ? 241 ALA A CB 1 ATOM 1863 N N . MET A 1 242 ? 18.902 5.182 35.678 1.00 16.47 ? 242 MET A N 1 ATOM 1864 C CA . MET A 1 242 ? 19.318 4.170 34.698 1.00 17.05 ? 242 MET A CA 1 ATOM 1865 C C . MET A 1 242 ? 18.154 3.261 34.267 1.00 17.33 ? 242 MET A C 1 ATOM 1866 O O . MET A 1 242 ? 17.970 2.933 33.091 1.00 17.55 ? 242 MET A O 1 ATOM 1867 C CB . MET A 1 242 ? 20.405 3.230 35.282 1.00 17.64 ? 242 MET A CB 1 ATOM 1868 C CG . MET A 1 242 ? 21.665 3.882 35.827 1.00 18.90 ? 242 MET A CG 1 ATOM 1869 S SD . MET A 1 242 ? 22.664 4.684 34.571 1.00 19.24 ? 242 MET A SD 1 ATOM 1870 C CE . MET A 1 242 ? 22.148 6.397 34.828 1.00 19.75 ? 242 MET A CE 1 ATOM 1871 N N . ASP A 1 243 ? 17.371 2.820 35.253 1.00 17.79 ? 243 ASP A N 1 ATOM 1872 C CA . ASP A 1 243 ? 16.227 1.974 34.928 1.00 20.43 ? 243 ASP A CA 1 ATOM 1873 C C . ASP A 1 243 ? 15.214 2.605 33.987 1.00 19.79 ? 243 ASP A C 1 ATOM 1874 O O . ASP A 1 243 ? 14.472 1.904 33.284 1.00 20.63 ? 243 ASP A O 1 ATOM 1875 C CB . ASP A 1 243 ? 15.528 1.555 36.222 1.00 20.56 ? 243 ASP A CB 1 ATOM 1876 C CG . ASP A 1 243 ? 16.333 0.562 37.051 1.00 23.60 ? 243 ASP A CG 1 ATOM 1877 O OD1 . ASP A 1 243 ? 17.348 -0.030 36.578 1.00 24.68 ? 243 ASP A OD1 1 ATOM 1878 O OD2 . ASP A 1 243 ? 15.907 0.360 38.213 1.00 26.22 ? 243 ASP A OD2 1 ATOM 1879 N N . LYS A 1 244 ? 15.167 3.947 33.983 1.00 18.66 ? 244 LYS A N 1 ATOM 1880 C CA . LYS A 1 244 ? 14.217 4.684 33.181 1.00 18.84 ? 244 LYS A CA 1 ATOM 1881 C C . LYS A 1 244 ? 14.857 5.255 31.922 1.00 18.17 ? 244 LYS A C 1 ATOM 1882 O O . LYS A 1 244 ? 14.234 6.011 31.195 1.00 19.73 ? 244 LYS A O 1 ATOM 1883 C CB . LYS A 1 244 ? 13.611 5.776 34.079 1.00 17.87 ? 244 LYS A CB 1 ATOM 1884 C CG . LYS A 1 244 ? 12.830 5.155 35.231 1.00 20.32 ? 244 LYS A CG 1 ATOM 1885 C CD . LYS A 1 244 ? 12.240 6.151 36.233 1.00 21.13 ? 244 LYS A CD 1 ATOM 1886 C CE . LYS A 1 244 ? 11.671 5.329 37.393 1.00 22.99 ? 244 LYS A CE 1 ATOM 1887 N NZ . LYS A 1 244 ? 10.905 6.159 38.361 1.00 22.55 ? 244 LYS A NZ 1 ATOM 1888 N N . GLY A 1 245 ? 16.110 4.877 31.663 1.00 17.37 ? 245 GLY A N 1 ATOM 1889 C CA . GLY A 1 245 ? 16.772 5.257 30.406 1.00 17.18 ? 245 GLY A CA 1 ATOM 1890 C C . GLY A 1 245 ? 17.211 6.709 30.283 1.00 16.06 ? 245 GLY A C 1 ATOM 1891 O O . GLY A 1 245 ? 17.250 7.203 29.152 1.00 16.18 ? 245 GLY A O 1 ATOM 1892 N N . VAL A 1 246 ? 17.580 7.341 31.400 1.00 16.18 ? 246 VAL A N 1 ATOM 1893 C CA . VAL A 1 246 ? 18.060 8.730 31.298 1.00 14.71 ? 246 VAL A CA 1 ATOM 1894 C C . VAL A 1 246 ? 19.187 8.854 30.272 1.00 15.12 ? 246 VAL A C 1 ATOM 1895 O O . VAL A 1 246 ? 20.097 7.998 30.237 1.00 15.36 ? 246 VAL A O 1 ATOM 1896 C CB . VAL A 1 246 ? 18.486 9.289 32.677 1.00 14.93 ? 246 VAL A CB 1 ATOM 1897 C CG1 . VAL A 1 246 ? 19.849 8.742 33.149 1.00 15.90 ? 246 VAL A CG1 1 ATOM 1898 C CG2 . VAL A 1 246 ? 18.448 10.810 32.672 1.00 14.40 ? 246 VAL A CG2 1 ATOM 1899 N N . SER A 1 247 ? 19.141 9.888 29.424 1.00 14.21 ? 247 SER A N 1 ATOM 1900 C CA . SER A 1 247 ? 20.055 9.872 28.288 1.00 14.35 ? 247 SER A CA 1 ATOM 1901 C C . SER A 1 247 ? 21.444 10.375 28.636 1.00 14.62 ? 247 SER A C 1 ATOM 1902 O O . SER A 1 247 ? 22.421 9.964 27.989 1.00 15.02 ? 247 SER A O 1 ATOM 1903 C CB . SER A 1 247 ? 19.507 10.725 27.138 1.00 15.17 ? 247 SER A CB 1 ATOM 1904 O OG . SER A 1 247 ? 18.428 10.044 26.511 1.00 15.98 ? 247 SER A OG 1 ATOM 1905 N N . THR A 1 248 ? 21.527 11.292 29.611 1.00 14.13 ? 248 THR A N 1 ATOM 1906 C CA . THR A 1 248 ? 22.772 11.918 30.006 1.00 13.46 ? 248 THR A CA 1 ATOM 1907 C C . THR A 1 248 ? 22.833 12.069 31.515 1.00 13.63 ? 248 THR A C 1 ATOM 1908 O O . THR A 1 248 ? 21.800 12.019 32.226 1.00 13.15 ? 248 THR A O 1 ATOM 1909 C CB . THR A 1 248 ? 22.951 13.322 29.357 1.00 12.98 ? 248 THR A CB 1 ATOM 1910 O OG1 . THR A 1 248 ? 22.088 14.294 30.025 1.00 13.53 ? 248 THR A OG1 1 ATOM 1911 C CG2 . THR A 1 248 ? 22.656 13.284 27.885 1.00 13.23 ? 248 THR A CG2 1 ATOM 1912 N N . VAL A 1 249 ? 24.059 12.242 32.014 1.00 13.11 ? 249 VAL A N 1 ATOM 1913 C CA . VAL A 1 249 ? 24.326 12.532 33.429 1.00 13.84 ? 249 VAL A CA 1 ATOM 1914 C C . VAL A 1 249 ? 25.300 13.690 33.509 1.00 13.72 ? 249 VAL A C 1 ATOM 1915 O O . VAL A 1 249 ? 26.337 13.657 32.794 1.00 15.40 ? 249 VAL A O 1 ATOM 1916 C CB . VAL A 1 249 ? 24.915 11.297 34.152 1.00 14.66 ? 249 VAL A CB 1 ATOM 1917 C CG1 . VAL A 1 249 ? 25.399 11.667 35.561 1.00 15.44 ? 249 VAL A CG1 1 ATOM 1918 C CG2 . VAL A 1 249 ? 23.844 10.183 34.190 1.00 15.61 ? 249 VAL A CG2 1 ATOM 1919 N N . MET A 1 250 ? 25.005 14.700 34.325 1.00 13.02 ? 250 MET A N 1 ATOM 1920 C CA . MET A 1 250 ? 25.925 15.837 34.476 1.00 13.70 ? 250 MET A CA 1 ATOM 1921 C C . MET A 1 250 ? 26.679 15.682 35.808 1.00 14.59 ? 250 MET A C 1 ATOM 1922 O O . MET A 1 250 ? 26.065 15.372 36.834 1.00 15.68 ? 250 MET A O 1 ATOM 1923 C CB . MET A 1 250 ? 25.164 17.182 34.495 1.00 13.89 ? 250 MET A CB 1 ATOM 1924 C CG . MET A 1 250 ? 26.082 18.388 34.607 1.00 14.76 ? 250 MET A CG 1 ATOM 1925 S SD . MET A 1 250 ? 25.157 19.956 34.665 1.00 14.61 ? 250 MET A SD 1 ATOM 1926 C CE . MET A 1 250 ? 24.260 19.972 33.115 1.00 14.90 ? 250 MET A CE 1 ATOM 1927 N N . ILE A 1 251 ? 27.988 15.902 35.781 1.00 15.06 ? 251 ILE A N 1 ATOM 1928 C CA . ILE A 1 251 ? 28.834 15.779 36.984 1.00 15.14 ? 251 ILE A CA 1 ATOM 1929 C C . ILE A 1 251 ? 28.784 17.037 37.859 1.00 15.45 ? 251 ILE A C 1 ATOM 1930 O O . ILE A 1 251 ? 28.599 18.161 37.385 1.00 15.65 ? 251 ILE A O 1 ATOM 1931 C CB . ILE A 1 251 ? 30.267 15.561 36.490 1.00 15.18 ? 251 ILE A CB 1 ATOM 1932 C CG1 . ILE A 1 251 ? 30.354 14.356 35.557 1.00 16.13 ? 251 ILE A CG1 1 ATOM 1933 C CG2 . ILE A 1 251 ? 31.220 15.263 37.691 1.00 15.89 ? 251 ILE A CG2 1 ATOM 1934 C CD1 . ILE A 1 251 ? 29.853 13.042 36.160 1.00 15.99 ? 251 ILE A CD1 1 ATOM 1935 N N . SER A 1 252 ? 28.894 16.824 39.184 1.00 15.23 ? 252 SER A N 1 ATOM 1936 C CA . SER A 1 252 ? 28.873 17.898 40.147 1.00 16.84 ? 252 SER A CA 1 ATOM 1937 C C . SER A 1 252 ? 30.196 18.652 40.264 1.00 18.83 ? 252 SER A C 1 ATOM 1938 O O . SER A 1 252 ? 31.267 18.021 40.161 1.00 18.95 ? 252 SER A O 1 ATOM 1939 C CB . SER A 1 252 ? 28.543 17.259 41.504 1.00 17.13 ? 252 SER A CB 1 ATOM 1940 O OG . SER A 1 252 ? 28.336 18.273 42.466 1.00 18.57 ? 252 SER A OG 1 ATOM 1941 N N . TYR A 1 253 ? 30.100 19.961 40.541 1.00 19.56 ? 253 TYR A N 1 ATOM 1942 C CA . TYR A 1 253 ? 31.259 20.730 41.044 1.00 21.21 ? 253 TYR A CA 1 ATOM 1943 C C . TYR A 1 253 ? 31.797 20.201 42.363 1.00 21.38 ? 253 TYR A C 1 ATOM 1944 O O . TYR A 1 253 ? 32.951 20.458 42.688 1.00 23.40 ? 253 TYR A O 1 ATOM 1945 C CB . TYR A 1 253 ? 30.897 22.173 41.315 1.00 21.53 ? 253 TYR A CB 1 ATOM 1946 C CG . TYR A 1 253 ? 30.505 23.049 40.154 1.00 22.46 ? 253 TYR A CG 1 ATOM 1947 C CD1 . TYR A 1 253 ? 31.275 23.152 39.019 1.00 22.80 ? 253 TYR A CD1 1 ATOM 1948 C CD2 . TYR A 1 253 ? 29.348 23.812 40.227 1.00 23.97 ? 253 TYR A CD2 1 ATOM 1949 C CE1 . TYR A 1 253 ? 30.926 24.018 37.989 1.00 21.38 ? 253 TYR A CE1 1 ATOM 1950 C CE2 . TYR A 1 253 ? 28.982 24.677 39.198 1.00 24.03 ? 253 TYR A CE2 1 ATOM 1951 C CZ . TYR A 1 253 ? 29.787 24.771 38.093 1.00 23.15 ? 253 TYR A CZ 1 ATOM 1952 O OH . TYR A 1 253 ? 29.467 25.628 37.063 1.00 23.54 ? 253 TYR A OH 1 ATOM 1953 N N . SER A 1 254 ? 30.969 19.491 43.122 1.00 21.23 ? 254 SER A N 1 ATOM 1954 C CA . SER A 1 254 ? 31.380 19.050 44.456 1.00 23.15 ? 254 SER A CA 1 ATOM 1955 C C . SER A 1 254 ? 32.495 18.011 44.399 1.00 24.07 ? 254 SER A C 1 ATOM 1956 O O . SER A 1 254 ? 32.897 17.493 43.323 1.00 22.61 ? 254 SER A O 1 ATOM 1957 C CB . SER A 1 254 ? 30.147 18.614 45.293 1.00 24.53 ? 254 SER A CB 1 ATOM 1958 O OG . SER A 1 254 ? 29.445 17.511 44.760 1.00 24.71 ? 254 SER A OG 1 ATOM 1959 N N . SER A 1 255 ? 33.075 17.766 45.569 1.00 26.33 ? 255 SER A N 1 ATOM 1960 C CA . SER A 1 255 ? 34.050 16.721 45.742 1.00 28.83 ? 255 SER A CA 1 ATOM 1961 C C . SER A 1 255 ? 33.429 15.728 46.684 1.00 30.99 ? 255 SER A C 1 ATOM 1962 O O . SER A 1 255 ? 32.521 16.085 47.455 1.00 31.28 ? 255 SER A O 1 ATOM 1963 C CB . SER A 1 255 ? 35.283 17.292 46.411 1.00 29.29 ? 255 SER A CB 1 ATOM 1964 O OG . SER A 1 255 ? 35.913 18.269 45.594 1.00 29.90 ? 255 SER A OG 1 ATOM 1965 N N . TRP A 1 256 ? 33.914 14.499 46.632 1.00 31.24 ? 256 TRP A N 1 ATOM 1966 C CA . TRP A 1 256 ? 33.536 13.513 47.620 1.00 34.05 ? 256 TRP A CA 1 ATOM 1967 C C . TRP A 1 256 ? 34.787 13.131 48.390 1.00 37.65 ? 256 TRP A C 1 ATOM 1968 O O . TRP A 1 256 ? 35.748 12.619 47.801 1.00 38.22 ? 256 TRP A O 1 ATOM 1969 C CB . TRP A 1 256 ? 32.878 12.304 46.960 1.00 35.59 ? 256 TRP A CB 1 ATOM 1970 C CG . TRP A 1 256 ? 32.535 11.234 47.956 1.00 36.42 ? 256 TRP A CG 1 ATOM 1971 C CD1 . TRP A 1 256 ? 31.789 11.384 49.105 1.00 39.02 ? 256 TRP A CD1 1 ATOM 1972 C CD2 . TRP A 1 256 ? 32.935 9.860 47.910 1.00 37.86 ? 256 TRP A CD2 1 ATOM 1973 N NE1 . TRP A 1 256 ? 31.699 10.181 49.765 1.00 38.92 ? 256 TRP A NE1 1 ATOM 1974 C CE2 . TRP A 1 256 ? 32.392 9.228 49.062 1.00 38.86 ? 256 TRP A CE2 1 ATOM 1975 C CE3 . TRP A 1 256 ? 33.703 9.096 47.012 1.00 39.29 ? 256 TRP A CE3 1 ATOM 1976 C CZ2 . TRP A 1 256 ? 32.587 7.859 49.333 1.00 39.47 ? 256 TRP A CZ2 1 ATOM 1977 C CZ3 . TRP A 1 256 ? 33.898 7.741 47.277 1.00 40.10 ? 256 TRP A CZ3 1 ATOM 1978 C CH2 . TRP A 1 256 ? 33.333 7.133 48.432 1.00 42.99 ? 256 TRP A CH2 1 ATOM 1979 N N . ASN A 1 257 ? 34.772 13.411 49.699 1.00 39.68 ? 257 ASN A N 1 ATOM 1980 C CA . ASN A 1 257 ? 35.909 13.138 50.584 1.00 42.18 ? 257 ASN A CA 1 ATOM 1981 C C . ASN A 1 257 ? 37.205 13.686 49.980 1.00 41.95 ? 257 ASN A C 1 ATOM 1982 O O . ASN A 1 257 ? 38.224 12.981 49.892 1.00 42.57 ? 257 ASN A O 1 ATOM 1983 C CB . ASN A 1 257 ? 36.024 11.633 50.888 1.00 45.55 ? 257 ASN A CB 1 ATOM 1984 C CG . ASN A 1 257 ? 34.962 11.138 51.872 1.00 47.28 ? 257 ASN A CG 1 ATOM 1985 O OD1 . ASN A 1 257 ? 34.464 11.888 52.733 1.00 47.93 ? 257 ASN A OD1 1 ATOM 1986 N ND2 . ASN A 1 257 ? 34.616 9.860 51.751 1.00 47.70 ? 257 ASN A ND2 1 ATOM 1987 N N . GLY A 1 258 ? 37.132 14.940 49.531 1.00 38.73 ? 258 GLY A N 1 ATOM 1988 C CA . GLY A 1 258 ? 38.280 15.645 48.991 1.00 38.78 ? 258 GLY A CA 1 ATOM 1989 C C . GLY A 1 258 ? 38.631 15.402 47.523 1.00 36.94 ? 258 GLY A C 1 ATOM 1990 O O . GLY A 1 258 ? 39.513 16.087 46.999 1.00 40.97 ? 258 GLY A O 1 ATOM 1991 N N . VAL A 1 259 ? 37.997 14.428 46.860 1.00 32.37 ? 259 VAL A N 1 ATOM 1992 C CA . VAL A 1 259 ? 38.293 14.151 45.435 1.00 28.36 ? 259 VAL A CA 1 ATOM 1993 C C . VAL A 1 259 ? 37.249 14.839 44.542 1.00 25.61 ? 259 VAL A C 1 ATOM 1994 O O . VAL A 1 259 ? 36.050 14.575 44.690 1.00 27.83 ? 259 VAL A O 1 ATOM 1995 C CB . VAL A 1 259 ? 38.241 12.648 45.125 1.00 29.56 ? 259 VAL A CB 1 ATOM 1996 C CG1 . VAL A 1 259 ? 38.508 12.404 43.647 1.00 28.20 ? 259 VAL A CG1 1 ATOM 1997 C CG2 . VAL A 1 259 ? 39.254 11.888 45.990 1.00 32.75 ? 259 VAL A CG2 1 ATOM 1998 N N . LYS A 1 260 ? 37.716 15.709 43.643 1.00 23.30 ? 260 LYS A N 1 ATOM 1999 C CA . LYS A 1 260 ? 36.771 16.449 42.720 1.00 22.03 ? 260 LYS A CA 1 ATOM 2000 C C . LYS A 1 260 ? 35.981 15.461 41.887 1.00 21.70 ? 260 LYS A C 1 ATOM 2001 O O . LYS A 1 260 ? 36.545 14.537 41.301 1.00 20.96 ? 260 LYS A O 1 ATOM 2002 C CB . LYS A 1 260 ? 37.553 17.365 41.819 1.00 22.01 ? 260 LYS A CB 1 ATOM 2003 C CG . LYS A 1 260 ? 38.182 18.551 42.509 1.00 23.16 ? 260 LYS A CG 1 ATOM 2004 C CD . LYS A 1 260 ? 37.226 19.693 42.665 1.00 22.88 ? 260 LYS A CD 1 ATOM 2005 C CE . LYS A 1 260 ? 37.953 20.857 43.329 1.00 23.24 ? 260 LYS A CE 1 ATOM 2006 N NZ . LYS A 1 260 ? 36.967 21.928 43.597 1.00 25.48 ? 260 LYS A NZ 1 ATOM 2007 N N . MET A 1 261 ? 34.658 15.654 41.807 1.00 19.30 ? 261 MET A N 1 ATOM 2008 C CA . MET A 1 261 ? 33.846 14.738 41.016 1.00 19.34 ? 261 MET A CA 1 ATOM 2009 C C . MET A 1 261 ? 34.261 14.725 39.549 1.00 18.23 ? 261 MET A C 1 ATOM 2010 O O . MET A 1 261 ? 34.231 13.666 38.910 1.00 19.05 ? 261 MET A O 1 ATOM 2011 C CB . MET A 1 261 ? 32.339 15.065 41.159 1.00 19.10 ? 261 MET A CB 1 ATOM 2012 C CG . MET A 1 261 ? 31.729 14.546 42.473 1.00 19.78 ? 261 MET A CG 1 ATOM 2013 S SD . MET A 1 261 ? 31.839 12.775 42.766 1.00 20.99 ? 261 MET A SD 1 ATOM 2014 C CE . MET A 1 261 ? 31.509 12.049 41.142 1.00 19.82 ? 261 MET A CE 1 ATOM 2015 N N . HIS A 1 262 ? 34.644 15.890 39.047 1.00 18.12 ? 262 HIS A N 1 ATOM 2016 C CA . HIS A 1 262 ? 35.079 16.031 37.641 1.00 17.65 ? 262 HIS A CA 1 ATOM 2017 C C . HIS A 1 262 ? 36.416 15.320 37.357 1.00 18.23 ? 262 HIS A C 1 ATOM 2018 O O . HIS A 1 262 ? 36.837 15.196 36.184 1.00 18.65 ? 262 HIS A O 1 ATOM 2019 C CB . HIS A 1 262 ? 35.154 17.496 37.206 1.00 16.13 ? 262 HIS A CB 1 ATOM 2020 C CG . HIS A 1 262 ? 33.809 18.134 36.976 1.00 16.75 ? 262 HIS A CG 1 ATOM 2021 N ND1 . HIS A 1 262 ? 33.348 18.474 35.717 1.00 18.87 ? 262 HIS A ND1 1 ATOM 2022 C CD2 . HIS A 1 262 ? 32.841 18.486 37.850 1.00 16.06 ? 262 HIS A CD2 1 ATOM 2023 C CE1 . HIS A 1 262 ? 32.120 18.984 35.835 1.00 13.68 ? 262 HIS A CE1 1 ATOM 2024 N NE2 . HIS A 1 262 ? 31.812 19.042 37.121 1.00 19.42 ? 262 HIS A NE2 1 ATOM 2025 N N . ALA A 1 263 ? 37.068 14.816 38.420 1.00 19.12 ? 263 ALA A N 1 ATOM 2026 C CA . ALA A 1 263 ? 38.331 14.043 38.232 1.00 20.57 ? 263 ALA A CA 1 ATOM 2027 C C . ALA A 1 263 ? 38.213 12.654 38.828 1.00 21.26 ? 263 ALA A C 1 ATOM 2028 O O . ALA A 1 263 ? 39.235 11.953 39.007 1.00 23.40 ? 263 ALA A O 1 ATOM 2029 C CB . ALA A 1 263 ? 39.483 14.786 38.885 1.00 21.72 ? 263 ALA A CB 1 ATOM 2030 N N . ASN A 1 264 ? 37.002 12.229 39.162 1.00 20.95 ? 264 ASN A N 1 ATOM 2031 C CA . ASN A 1 264 ? 36.823 10.963 39.880 1.00 20.24 ? 264 ASN A CA 1 ATOM 2032 C C . ASN A 1 264 ? 36.553 9.804 38.955 1.00 20.67 ? 264 ASN A C 1 ATOM 2033 O O . ASN A 1 264 ? 35.406 9.469 38.664 1.00 20.62 ? 264 ASN A O 1 ATOM 2034 C CB . ASN A 1 264 ? 35.722 11.074 40.913 1.00 22.63 ? 264 ASN A CB 1 ATOM 2035 C CG . ASN A 1 264 ? 35.833 9.972 41.948 1.00 23.87 ? 264 ASN A CG 1 ATOM 2036 O OD1 . ASN A 1 264 ? 36.110 8.822 41.592 1.00 25.20 ? 264 ASN A OD1 1 ATOM 2037 N ND2 . ASN A 1 264 ? 35.675 10.320 43.235 1.00 28.91 ? 264 ASN A ND2 1 ATOM 2038 N N . GLN A 1 265 ? 37.644 9.155 38.513 1.00 21.35 ? 265 GLN A N 1 ATOM 2039 C CA . GLN A 1 265 ? 37.540 8.006 37.638 1.00 21.12 ? 265 GLN A CA 1 ATOM 2040 C C . GLN A 1 265 ? 36.818 6.852 38.337 1.00 21.20 ? 265 GLN A C 1 ATOM 2041 O O . GLN A 1 265 ? 36.049 6.140 37.693 1.00 21.79 ? 265 GLN A O 1 ATOM 2042 C CB . GLN A 1 265 ? 38.931 7.581 37.100 1.00 22.37 ? 265 GLN A CB 1 ATOM 2043 C CG . GLN A 1 265 ? 38.879 6.482 36.055 1.00 24.16 ? 265 GLN A CG 1 ATOM 2044 C CD . GLN A 1 265 ? 40.276 6.013 35.733 1.00 29.52 ? 265 GLN A CD 1 ATOM 2045 O OE1 . GLN A 1 265 ? 40.947 6.599 34.901 1.00 34.07 ? 265 GLN A OE1 1 ATOM 2046 N NE2 . GLN A 1 265 ? 40.727 4.980 36.436 1.00 33.59 ? 265 GLN A NE2 1 ATOM 2047 N N . ASP A 1 266 ? 37.057 6.664 39.636 1.00 21.96 ? 266 ASP A N 1 ATOM 2048 C CA . ASP A 1 266 ? 36.457 5.522 40.343 1.00 24.67 ? 266 ASP A CA 1 ATOM 2049 C C . ASP A 1 266 ? 34.922 5.611 40.294 1.00 22.43 ? 266 ASP A C 1 ATOM 2050 O O . ASP A 1 266 ? 34.261 4.612 40.025 1.00 22.32 ? 266 ASP A O 1 ATOM 2051 C CB . ASP A 1 266 ? 36.907 5.429 41.814 1.00 27.81 ? 266 ASP A CB 1 ATOM 2052 C CG . ASP A 1 266 ? 38.365 5.012 41.983 1.00 34.58 ? 266 ASP A CG 1 ATOM 2053 O OD1 . ASP A 1 266 ? 38.880 5.149 43.118 1.00 38.95 ? 266 ASP A OD1 1 ATOM 2054 O OD2 . ASP A 1 266 ? 39.000 4.556 41.017 1.00 38.03 ? 266 ASP A OD2 1 ATOM 2055 N N . LEU A 1 267 ? 34.375 6.816 40.521 1.00 22.32 ? 267 LEU A N 1 ATOM 2056 C CA . LEU A 1 267 ? 32.925 6.990 40.510 1.00 22.52 ? 267 LEU A CA 1 ATOM 2057 C C . LEU A 1 267 ? 32.325 7.164 39.103 1.00 20.36 ? 267 LEU A C 1 ATOM 2058 O O . LEU A 1 267 ? 31.296 6.565 38.801 1.00 21.20 ? 267 LEU A O 1 ATOM 2059 C CB . LEU A 1 267 ? 32.492 8.131 41.441 1.00 21.56 ? 267 LEU A CB 1 ATOM 2060 C CG . LEU A 1 267 ? 32.596 7.832 42.952 1.00 21.73 ? 267 LEU A CG 1 ATOM 2061 C CD1 . LEU A 1 267 ? 32.180 9.049 43.773 1.00 22.15 ? 267 LEU A CD1 1 ATOM 2062 C CD2 . LEU A 1 267 ? 31.740 6.608 43.304 1.00 23.75 ? 267 LEU A CD2 1 ATOM 2063 N N . VAL A 1 268 ? 32.977 7.934 38.252 1.00 19.91 ? 268 VAL A N 1 ATOM 2064 C CA . VAL A 1 268 ? 32.418 8.207 36.911 1.00 19.84 ? 268 VAL A CA 1 ATOM 2065 C C . VAL A 1 268 ? 32.556 6.995 35.986 1.00 18.96 ? 268 VAL A C 1 ATOM 2066 O O . VAL A 1 268 ? 31.582 6.563 35.346 1.00 19.73 ? 268 VAL A O 1 ATOM 2067 C CB . VAL A 1 268 ? 33.032 9.469 36.280 1.00 19.83 ? 268 VAL A CB 1 ATOM 2068 C CG1 . VAL A 1 268 ? 32.572 9.661 34.808 1.00 19.21 ? 268 VAL A CG1 1 ATOM 2069 C CG2 . VAL A 1 268 ? 32.691 10.692 37.116 1.00 19.18 ? 268 VAL A CG2 1 ATOM 2070 N N . THR A 1 269 ? 33.760 6.403 35.941 1.00 19.91 ? 269 THR A N 1 ATOM 2071 C CA . THR A 1 269 ? 33.965 5.234 35.115 1.00 19.68 ? 269 THR A CA 1 ATOM 2072 C C . THR A 1 269 ? 33.719 3.936 35.888 1.00 20.99 ? 269 THR A C 1 ATOM 2073 O O . THR A 1 269 ? 32.930 3.117 35.445 1.00 20.41 ? 269 THR A O 1 ATOM 2074 C CB . THR A 1 269 ? 35.358 5.220 34.426 1.00 19.60 ? 269 THR A CB 1 ATOM 2075 O OG1 . THR A 1 269 ? 35.479 6.379 33.574 1.00 20.91 ? 269 THR A OG1 1 ATOM 2076 C CG2 . THR A 1 269 ? 35.485 3.986 33.563 1.00 20.47 ? 269 THR A CG2 1 ATOM 2077 N N . GLY A 1 270 ? 34.350 3.789 37.051 1.00 22.17 ? 270 GLY A N 1 ATOM 2078 C CA . GLY A 1 270 ? 34.226 2.516 37.797 1.00 22.03 ? 270 GLY A CA 1 ATOM 2079 C C . GLY A 1 270 ? 32.812 2.220 38.209 1.00 23.12 ? 270 GLY A C 1 ATOM 2080 O O . GLY A 1 270 ? 32.339 1.069 38.089 1.00 24.79 ? 270 GLY A O 1 ATOM 2081 N N . TYR A 1 271 ? 32.089 3.244 38.678 1.00 22.53 ? 271 TYR A N 1 ATOM 2082 C CA . TYR A 1 271 ? 30.733 2.996 39.172 1.00 22.95 ? 271 TYR A CA 1 ATOM 2083 C C . TYR A 1 271 ? 29.643 3.318 38.128 1.00 21.65 ? 271 TYR A C 1 ATOM 2084 O O . TYR A 1 271 ? 28.961 2.399 37.663 1.00 22.12 ? 271 TYR A O 1 ATOM 2085 C CB . TYR A 1 271 ? 30.436 3.724 40.505 1.00 24.29 ? 271 TYR A CB 1 ATOM 2086 C CG . TYR A 1 271 ? 29.196 3.157 41.153 1.00 25.75 ? 271 TYR A CG 1 ATOM 2087 C CD1 . TYR A 1 271 ? 29.225 1.903 41.764 1.00 27.92 ? 271 TYR A CD1 1 ATOM 2088 C CD2 . TYR A 1 271 ? 27.967 3.857 41.126 1.00 25.98 ? 271 TYR A CD2 1 ATOM 2089 C CE1 . TYR A 1 271 ? 28.086 1.363 42.337 1.00 28.74 ? 271 TYR A CE1 1 ATOM 2090 C CE2 . TYR A 1 271 ? 26.825 3.314 41.695 1.00 27.12 ? 271 TYR A CE2 1 ATOM 2091 C CZ . TYR A 1 271 ? 26.889 2.072 42.298 1.00 29.75 ? 271 TYR A CZ 1 ATOM 2092 O OH . TYR A 1 271 ? 25.762 1.525 42.880 1.00 31.68 ? 271 TYR A OH 1 ATOM 2093 N N . LEU A 1 272 ? 29.523 4.580 37.705 1.00 21.12 ? 272 LEU A N 1 ATOM 2094 C CA . LEU A 1 272 ? 28.422 4.929 36.770 1.00 20.57 ? 272 LEU A CA 1 ATOM 2095 C C . LEU A 1 272 ? 28.465 4.139 35.474 1.00 19.77 ? 272 LEU A C 1 ATOM 2096 O O . LEU A 1 272 ? 27.482 3.512 35.057 1.00 19.64 ? 272 LEU A O 1 ATOM 2097 C CB . LEU A 1 272 ? 28.444 6.435 36.495 1.00 19.06 ? 272 LEU A CB 1 ATOM 2098 C CG . LEU A 1 272 ? 27.390 6.977 35.539 1.00 18.74 ? 272 LEU A CG 1 ATOM 2099 C CD1 . LEU A 1 272 ? 25.951 6.749 36.015 1.00 19.19 ? 272 LEU A CD1 1 ATOM 2100 C CD2 . LEU A 1 272 ? 27.730 8.454 35.353 1.00 18.75 ? 272 LEU A CD2 1 ATOM 2101 N N . LYS A 1 273 ? 29.633 4.135 34.808 1.00 19.83 ? 273 LYS A N 1 ATOM 2102 C CA . LYS A 1 273 ? 29.744 3.429 33.550 1.00 19.72 ? 273 LYS A CA 1 ATOM 2103 C C . LYS A 1 273 ? 29.889 1.899 33.751 1.00 21.42 ? 273 LYS A C 1 ATOM 2104 O O . LYS A 1 273 ? 29.141 1.140 33.177 1.00 21.43 ? 273 LYS A O 1 ATOM 2105 C CB . LYS A 1 273 ? 30.879 4.008 32.681 1.00 19.17 ? 273 LYS A CB 1 ATOM 2106 C CG . LYS A 1 273 ? 30.616 5.450 32.197 1.00 17.84 ? 273 LYS A CG 1 ATOM 2107 C CD . LYS A 1 273 ? 31.728 5.941 31.279 1.00 18.57 ? 273 LYS A CD 1 ATOM 2108 C CE . LYS A 1 273 ? 31.297 7.177 30.488 1.00 17.68 ? 273 LYS A CE 1 ATOM 2109 N NZ . LYS A 1 273 ? 32.411 7.549 29.564 1.00 19.35 ? 273 LYS A NZ 1 ATOM 2110 N N . ASP A 1 274 ? 30.826 1.472 34.593 1.00 23.52 ? 274 ASP A N 1 ATOM 2111 C CA . ASP A 1 274 ? 31.209 0.037 34.611 1.00 24.61 ? 274 ASP A CA 1 ATOM 2112 C C . ASP A 1 274 ? 30.331 -0.814 35.529 1.00 25.32 ? 274 ASP A C 1 ATOM 2113 O O . ASP A 1 274 ? 30.260 -2.044 35.331 1.00 28.09 ? 274 ASP A O 1 ATOM 2114 C CB . ASP A 1 274 ? 32.673 -0.137 35.011 1.00 26.53 ? 274 ASP A CB 1 ATOM 2115 C CG . ASP A 1 274 ? 33.650 0.412 33.963 1.00 28.63 ? 274 ASP A CG 1 ATOM 2116 O OD1 . ASP A 1 274 ? 33.267 0.755 32.818 1.00 29.01 ? 274 ASP A OD1 1 ATOM 2117 O OD2 . ASP A 1 274 ? 34.842 0.488 34.296 1.00 31.35 ? 274 ASP A OD2 1 ATOM 2118 N N . THR A 1 275 ? 29.669 -0.185 36.508 1.00 23.83 ? 275 THR A N 1 ATOM 2119 C CA . THR A 1 275 ? 28.838 -0.924 37.468 1.00 25.38 ? 275 THR A CA 1 ATOM 2120 C C . THR A 1 275 ? 27.353 -0.723 37.147 1.00 26.14 ? 275 THR A C 1 ATOM 2121 O O . THR A 1 275 ? 26.623 -1.703 36.984 1.00 26.08 ? 275 THR A O 1 ATOM 2122 C CB . THR A 1 275 ? 29.167 -0.561 38.933 1.00 26.41 ? 275 THR A CB 1 ATOM 2123 O OG1 . THR A 1 275 ? 30.562 -0.769 39.150 1.00 28.02 ? 275 THR A OG1 1 ATOM 2124 C CG2 . THR A 1 275 ? 28.381 -1.414 39.931 1.00 27.21 ? 275 THR A CG2 1 ATOM 2125 N N . LEU A 1 276 ? 26.912 0.534 37.038 1.00 24.26 ? 276 LEU A N 1 ATOM 2126 C CA . LEU A 1 276 ? 25.526 0.799 36.634 1.00 24.17 ? 276 LEU A CA 1 ATOM 2127 C C . LEU A 1 276 ? 25.234 0.553 35.152 1.00 23.57 ? 276 LEU A C 1 ATOM 2128 O O . LEU A 1 276 ? 24.068 0.543 34.721 1.00 23.30 ? 276 LEU A O 1 ATOM 2129 C CB . LEU A 1 276 ? 25.076 2.206 37.072 1.00 24.15 ? 276 LEU A CB 1 ATOM 2130 C CG . LEU A 1 276 ? 25.034 2.453 38.575 1.00 25.04 ? 276 LEU A CG 1 ATOM 2131 C CD1 . LEU A 1 276 ? 24.532 3.869 38.838 1.00 26.68 ? 276 LEU A CD1 1 ATOM 2132 C CD2 . LEU A 1 276 ? 24.142 1.426 39.298 1.00 26.82 ? 276 LEU A CD2 1 ATOM 2133 N N . LYS A 1 277 ? 26.303 0.334 34.382 1.00 21.37 ? 277 LYS A N 1 ATOM 2134 C CA . LYS A 1 277 ? 26.230 0.088 32.947 1.00 21.86 ? 277 LYS A CA 1 ATOM 2135 C C . LYS A 1 277 ? 25.545 1.239 32.178 1.00 20.11 ? 277 LYS A C 1 ATOM 2136 O O . LYS A 1 277 ? 24.865 1.022 31.181 1.00 19.97 ? 277 LYS A O 1 ATOM 2137 C CB . LYS A 1 277 ? 25.598 -1.281 32.601 1.00 24.88 ? 277 LYS A CB 1 ATOM 2138 C CG . LYS A 1 277 ? 26.227 -2.502 33.315 1.00 26.79 ? 277 LYS A CG 1 ATOM 2139 C CD . LYS A 1 277 ? 27.705 -2.643 33.001 1.00 29.80 ? 277 LYS A CD 1 ATOM 2140 C CE . LYS A 1 277 ? 28.299 -3.896 33.660 1.00 33.52 ? 277 LYS A CE 1 ATOM 2141 N NZ . LYS A 1 277 ? 29.728 -4.022 33.277 1.00 36.42 ? 277 LYS A NZ 1 ATOM 2142 N N . PHE A 1 278 ? 25.776 2.462 32.637 1.00 18.07 ? 278 PHE A N 1 ATOM 2143 C CA . PHE A 1 278 ? 25.288 3.667 31.891 1.00 17.58 ? 278 PHE A CA 1 ATOM 2144 C C . PHE A 1 278 ? 25.953 3.708 30.503 1.00 16.94 ? 278 PHE A C 1 ATOM 2145 O O . PHE A 1 278 ? 27.199 3.656 30.396 1.00 17.85 ? 278 PHE A O 1 ATOM 2146 C CB . PHE A 1 278 ? 25.647 4.915 32.659 1.00 16.86 ? 278 PHE A CB 1 ATOM 2147 C CG . PHE A 1 278 ? 25.163 6.199 31.990 1.00 16.90 ? 278 PHE A CG 1 ATOM 2148 C CD1 . PHE A 1 278 ? 23.802 6.344 31.595 1.00 16.57 ? 278 PHE A CD1 1 ATOM 2149 C CD2 . PHE A 1 278 ? 26.061 7.252 31.725 1.00 15.92 ? 278 PHE A CD2 1 ATOM 2150 C CE1 . PHE A 1 278 ? 23.376 7.521 30.977 1.00 16.26 ? 278 PHE A CE1 1 ATOM 2151 C CE2 . PHE A 1 278 ? 25.612 8.425 31.099 1.00 16.19 ? 278 PHE A CE2 1 ATOM 2152 C CZ . PHE A 1 278 ? 24.284 8.553 30.732 1.00 16.72 ? 278 PHE A CZ 1 ATOM 2153 N N . LYS A 1 279 ? 25.124 3.823 29.460 1.00 17.79 ? 279 LYS A N 1 ATOM 2154 C CA . LYS A 1 279 ? 25.569 3.821 28.050 1.00 17.35 ? 279 LYS A CA 1 ATOM 2155 C C . LYS A 1 279 ? 25.243 5.136 27.324 1.00 17.34 ? 279 LYS A C 1 ATOM 2156 O O . LYS A 1 279 ? 25.469 5.271 26.127 1.00 17.11 ? 279 LYS A O 1 ATOM 2157 C CB . LYS A 1 279 ? 24.977 2.660 27.268 1.00 18.87 ? 279 LYS A CB 1 ATOM 2158 C CG . LYS A 1 279 ? 25.300 1.281 27.862 1.00 20.41 ? 279 LYS A CG 1 ATOM 2159 C CD . LYS A 1 279 ? 26.792 1.022 27.898 1.00 22.33 ? 279 LYS A CD 1 ATOM 2160 C CE . LYS A 1 279 ? 27.082 -0.475 28.188 1.00 26.26 ? 279 LYS A CE 1 ATOM 2161 N NZ . LYS A 1 279 ? 28.518 -0.629 28.515 1.00 26.66 ? 279 LYS A NZ 1 ATOM 2162 N N . GLY A 1 280 ? 24.618 6.076 28.044 1.00 15.57 ? 280 GLY A N 1 ATOM 2163 C CA . GLY A 1 280 ? 24.462 7.438 27.483 1.00 16.12 ? 280 GLY A CA 1 ATOM 2164 C C . GLY A 1 280 ? 25.737 8.237 27.656 1.00 15.51 ? 280 GLY A C 1 ATOM 2165 O O . GLY A 1 280 ? 26.848 7.665 27.874 1.00 15.72 ? 280 GLY A O 1 ATOM 2166 N N . PHE A 1 281 ? 25.632 9.560 27.503 1.00 14.59 ? 281 PHE A N 1 ATOM 2167 C CA . PHE A 1 281 ? 26.818 10.398 27.689 1.00 14.07 ? 281 PHE A CA 1 ATOM 2168 C C . PHE A 1 281 ? 26.877 11.188 28.999 1.00 15.29 ? 281 PHE A C 1 ATOM 2169 O O . PHE A 1 281 ? 25.852 11.644 29.537 1.00 14.63 ? 281 PHE A O 1 ATOM 2170 C CB . PHE A 1 281 ? 27.139 11.270 26.435 1.00 13.17 ? 281 PHE A CB 1 ATOM 2171 C CG . PHE A 1 281 ? 26.245 12.479 26.175 1.00 13.47 ? 281 PHE A CG 1 ATOM 2172 C CD1 . PHE A 1 281 ? 26.434 13.681 26.863 1.00 12.85 ? 281 PHE A CD1 1 ATOM 2173 C CD2 . PHE A 1 281 ? 25.313 12.449 25.116 1.00 14.03 ? 281 PHE A CD2 1 ATOM 2174 C CE1 . PHE A 1 281 ? 25.670 14.845 26.551 1.00 13.79 ? 281 PHE A CE1 1 ATOM 2175 C CE2 . PHE A 1 281 ? 24.560 13.600 24.781 1.00 13.22 ? 281 PHE A CE2 1 ATOM 2176 C CZ . PHE A 1 281 ? 24.741 14.791 25.511 1.00 13.10 ? 281 PHE A CZ 1 ATOM 2177 N N . VAL A 1 282 ? 28.090 11.359 29.496 1.00 14.36 ? 282 VAL A N 1 ATOM 2178 C CA . VAL A 1 282 ? 28.374 12.078 30.711 1.00 14.45 ? 282 VAL A CA 1 ATOM 2179 C C . VAL A 1 282 ? 28.891 13.473 30.337 1.00 15.08 ? 282 VAL A C 1 ATOM 2180 O O . VAL A 1 282 ? 29.857 13.610 29.562 1.00 14.94 ? 282 VAL A O 1 ATOM 2181 C CB . VAL A 1 282 ? 29.469 11.343 31.539 1.00 16.07 ? 282 VAL A CB 1 ATOM 2182 C CG1 . VAL A 1 282 ? 29.843 12.164 32.788 1.00 15.96 ? 282 VAL A CG1 1 ATOM 2183 C CG2 . VAL A 1 282 ? 28.983 9.923 31.894 1.00 16.49 ? 282 VAL A CG2 1 ATOM 2184 N N . ILE A 1 283 ? 28.222 14.500 30.841 1.00 13.76 ? 283 ILE A N 1 ATOM 2185 C CA . ILE A 1 283 ? 28.561 15.874 30.524 1.00 13.73 ? 283 ILE A CA 1 ATOM 2186 C C . ILE A 1 283 ? 29.129 16.616 31.764 1.00 14.32 ? 283 ILE A C 1 ATOM 2187 O O . ILE A 1 283 ? 28.676 16.364 32.887 1.00 13.99 ? 283 ILE A O 1 ATOM 2188 C CB . ILE A 1 283 ? 27.319 16.614 29.912 1.00 14.32 ? 283 ILE A CB 1 ATOM 2189 C CG1 . ILE A 1 283 ? 27.697 18.017 29.427 1.00 14.29 ? 283 ILE A CG1 1 ATOM 2190 C CG2 . ILE A 1 283 ? 26.134 16.685 30.900 1.00 14.53 ? 283 ILE A CG2 1 ATOM 2191 C CD1 . ILE A 1 283 ? 26.621 18.718 28.594 1.00 14.90 ? 283 ILE A CD1 1 ATOM 2192 N N . SER A 1 284 ? 30.094 17.539 31.577 1.00 13.96 ? 284 SER A N 1 ATOM 2193 C CA . SER A 1 284 ? 30.591 18.323 32.708 1.00 13.69 ? 284 SER A CA 1 ATOM 2194 C C . SER A 1 284 ? 29.537 19.338 33.124 1.00 14.45 ? 284 SER A C 1 ATOM 2195 O O . SER A 1 284 ? 28.600 19.629 32.326 1.00 14.50 ? 284 SER A O 1 ATOM 2196 C CB . SER A 1 284 ? 31.907 19.104 32.347 1.00 14.32 ? 284 SER A CB 1 ATOM 2197 O OG . SER A 1 284 ? 31.626 20.261 31.555 1.00 14.03 ? 284 SER A OG 1 ATOM 2198 N N . ASP A 1 285 ? 29.724 19.917 34.302 1.00 14.34 ? 285 ASP A N 1 ATOM 2199 C CA . ASP A 1 285 ? 29.052 21.161 34.604 1.00 14.81 ? 285 ASP A CA 1 ATOM 2200 C C . ASP A 1 285 ? 29.778 22.370 33.986 1.00 14.43 ? 285 ASP A C 1 ATOM 2201 O O . ASP A 1 285 ? 30.813 22.228 33.313 1.00 14.71 ? 285 ASP A O 1 ATOM 2202 C CB . ASP A 1 285 ? 28.839 21.316 36.119 1.00 16.05 ? 285 ASP A CB 1 ATOM 2203 C CG . ASP A 1 285 ? 27.601 22.180 36.431 1.00 17.41 ? 285 ASP A CG 1 ATOM 2204 O OD1 . ASP A 1 285 ? 27.090 22.899 35.543 1.00 20.18 ? 285 ASP A OD1 1 ATOM 2205 O OD2 . ASP A 1 285 ? 27.162 22.120 37.555 1.00 22.92 ? 285 ASP A OD2 1 ATOM 2206 N N . TRP A 1 286 ? 29.237 23.563 34.197 1.00 14.21 ? 286 TRP A N 1 ATOM 2207 C CA . TRP A 1 286 ? 29.705 24.778 33.517 1.00 14.18 ? 286 TRP A CA 1 ATOM 2208 C C . TRP A 1 286 ? 31.065 25.167 34.049 1.00 15.37 ? 286 TRP A C 1 ATOM 2209 O O . TRP A 1 286 ? 31.228 25.507 35.233 1.00 15.84 ? 286 TRP A O 1 ATOM 2210 C CB . TRP A 1 286 ? 28.657 25.871 33.817 1.00 14.44 ? 286 TRP A CB 1 ATOM 2211 C CG . TRP A 1 286 ? 28.979 27.266 33.372 1.00 14.68 ? 286 TRP A CG 1 ATOM 2212 C CD1 . TRP A 1 286 ? 29.874 28.135 33.957 1.00 15.56 ? 286 TRP A CD1 1 ATOM 2213 C CD2 . TRP A 1 286 ? 28.394 27.975 32.267 1.00 14.84 ? 286 TRP A CD2 1 ATOM 2214 N NE1 . TRP A 1 286 ? 29.882 29.347 33.286 1.00 15.70 ? 286 TRP A NE1 1 ATOM 2215 C CE2 . TRP A 1 286 ? 28.978 29.275 32.244 1.00 15.13 ? 286 TRP A CE2 1 ATOM 2216 C CE3 . TRP A 1 286 ? 27.419 27.640 31.308 1.00 15.13 ? 286 TRP A CE3 1 ATOM 2217 C CZ2 . TRP A 1 286 ? 28.604 30.251 31.314 1.00 15.52 ? 286 TRP A CZ2 1 ATOM 2218 C CZ3 . TRP A 1 286 ? 27.055 28.619 30.343 1.00 15.32 ? 286 TRP A CZ3 1 ATOM 2219 C CH2 . TRP A 1 286 ? 27.660 29.892 30.345 1.00 15.09 ? 286 TRP A CH2 1 ATOM 2220 N N . GLU A 1 287 ? 32.057 25.085 33.156 1.00 15.76 ? 287 GLU A N 1 ATOM 2221 C CA . GLU A 1 287 ? 33.485 25.273 33.608 1.00 17.08 ? 287 GLU A CA 1 ATOM 2222 C C . GLU A 1 287 ? 33.815 24.311 34.746 1.00 17.72 ? 287 GLU A C 1 ATOM 2223 O O . GLU A 1 287 ? 34.668 24.619 35.619 1.00 17.18 ? 287 GLU A O 1 ATOM 2224 C CB . GLU A 1 287 ? 33.760 26.734 34.030 1.00 19.17 ? 287 GLU A CB 1 ATOM 2225 C CG . GLU A 1 287 ? 33.635 27.729 32.897 1.00 22.41 ? 287 GLU A CG 1 ATOM 2226 C CD . GLU A 1 287 ? 33.813 29.172 33.374 1.00 26.33 ? 287 GLU A CD 1 ATOM 2227 O OE1 . GLU A 1 287 ? 33.757 29.435 34.595 1.00 31.14 ? 287 GLU A OE1 1 ATOM 2228 O OE2 . GLU A 1 287 ? 33.977 30.034 32.510 1.00 34.42 ? 287 GLU A OE2 1 ATOM 2229 N N . GLY A 1 288 ? 33.152 23.161 34.793 1.00 15.66 ? 288 GLY A N 1 ATOM 2230 C CA . GLY A 1 288 ? 33.410 22.178 35.873 1.00 15.44 ? 288 GLY A CA 1 ATOM 2231 C C . GLY A 1 288 ? 34.853 21.643 35.830 1.00 16.21 ? 288 GLY A C 1 ATOM 2232 O O . GLY A 1 288 ? 35.453 21.375 36.894 1.00 18.19 ? 288 GLY A O 1 ATOM 2233 N N . ILE A 1 289 ? 35.412 21.508 34.641 1.00 16.80 ? 289 ILE A N 1 ATOM 2234 C CA . ILE A 1 289 ? 36.760 20.942 34.569 1.00 17.26 ? 289 ILE A CA 1 ATOM 2235 C C . ILE A 1 289 ? 37.760 22.001 35.041 1.00 18.48 ? 289 ILE A C 1 ATOM 2236 O O . ILE A 1 289 ? 38.755 21.657 35.724 1.00 17.74 ? 289 ILE A O 1 ATOM 2237 C CB . ILE A 1 289 ? 37.135 20.314 33.198 1.00 17.14 ? 289 ILE A CB 1 ATOM 2238 C CG1 . ILE A 1 289 ? 37.424 21.379 32.115 1.00 17.60 ? 289 ILE A CG1 1 ATOM 2239 C CG2 . ILE A 1 289 ? 36.055 19.308 32.799 1.00 17.91 ? 289 ILE A CG2 1 ATOM 2240 C CD1 . ILE A 1 289 ? 37.963 20.745 30.814 1.00 17.88 ? 289 ILE A CD1 1 ATOM 2241 N N . ASP A 1 290 ? 37.482 23.267 34.760 1.00 17.31 ? 290 ASP A N 1 ATOM 2242 C CA . ASP A 1 290 ? 38.323 24.388 35.238 1.00 19.42 ? 290 ASP A CA 1 ATOM 2243 C C . ASP A 1 290 ? 38.457 24.344 36.753 1.00 19.45 ? 290 ASP A C 1 ATOM 2244 O O . ASP A 1 290 ? 39.527 24.609 37.321 1.00 20.22 ? 290 ASP A O 1 ATOM 2245 C CB . ASP A 1 290 ? 37.783 25.768 34.834 1.00 19.86 ? 290 ASP A CB 1 ATOM 2246 C CG . ASP A 1 290 ? 37.361 25.857 33.367 1.00 20.98 ? 290 ASP A CG 1 ATOM 2247 O OD1 . ASP A 1 290 ? 36.675 24.947 32.893 1.00 20.24 ? 290 ASP A OD1 1 ATOM 2248 O OD2 . ASP A 1 290 ? 37.727 26.891 32.738 1.00 23.21 ? 290 ASP A OD2 1 ATOM 2249 N N . ARG A 1 291 ? 37.360 23.971 37.421 1.00 18.35 ? 291 ARG A N 1 ATOM 2250 C CA . ARG A 1 291 ? 37.292 24.023 38.885 1.00 19.54 ? 291 ARG A CA 1 ATOM 2251 C C . ARG A 1 291 ? 37.885 22.787 39.563 1.00 20.79 ? 291 ARG A C 1 ATOM 2252 O O . ARG A 1 291 ? 37.852 22.697 40.790 1.00 22.18 ? 291 ARG A O 1 ATOM 2253 C CB . ARG A 1 291 ? 35.838 24.286 39.305 1.00 20.65 ? 291 ARG A CB 1 ATOM 2254 C CG . ARG A 1 291 ? 35.396 25.685 38.886 1.00 22.47 ? 291 ARG A CG 1 ATOM 2255 C CD . ARG A 1 291 ? 33.886 25.931 39.010 1.00 26.88 ? 291 ARG A CD 1 ATOM 2256 N NE . ARG A 1 291 ? 33.574 27.065 38.112 1.00 34.05 ? 291 ARG A NE 1 ATOM 2257 C CZ . ARG A 1 291 ? 32.475 27.811 38.148 1.00 37.55 ? 291 ARG A CZ 1 ATOM 2258 N NH1 . ARG A 1 291 ? 31.545 27.567 39.069 1.00 37.00 ? 291 ARG A NH1 1 ATOM 2259 N NH2 . ARG A 1 291 ? 32.305 28.798 37.246 1.00 36.79 ? 291 ARG A NH2 1 ATOM 2260 N N . ILE A 1 292 ? 38.490 21.881 38.781 1.00 21.07 ? 292 ILE A N 1 ATOM 2261 C CA . ILE A 1 292 ? 39.292 20.761 39.335 1.00 21.25 ? 292 ILE A CA 1 ATOM 2262 C C . ILE A 1 292 ? 40.479 21.333 40.104 1.00 23.16 ? 292 ILE A C 1 ATOM 2263 O O . ILE A 1 292 ? 40.837 20.812 41.189 1.00 23.23 ? 292 ILE A O 1 ATOM 2264 C CB . ILE A 1 292 ? 39.785 19.798 38.241 1.00 21.52 ? 292 ILE A CB 1 ATOM 2265 C CG1 . ILE A 1 292 ? 38.619 18.940 37.740 1.00 20.34 ? 292 ILE A CG1 1 ATOM 2266 C CG2 . ILE A 1 292 ? 40.912 18.902 38.768 1.00 23.64 ? 292 ILE A CG2 1 ATOM 2267 C CD1 . ILE A 1 292 ? 38.928 18.217 36.442 1.00 20.00 ? 292 ILE A CD1 1 ATOM 2268 N N . THR A 1 293 ? 41.049 22.414 39.574 1.00 23.06 ? 293 THR A N 1 ATOM 2269 C CA . THR A 1 293 ? 42.237 23.062 40.181 1.00 25.65 ? 293 THR A CA 1 ATOM 2270 C C . THR A 1 293 ? 41.877 24.215 41.118 1.00 27.64 ? 293 THR A C 1 ATOM 2271 O O . THR A 1 293 ? 40.809 24.808 41.024 1.00 25.31 ? 293 THR A O 1 ATOM 2272 C CB . THR A 1 293 ? 43.202 23.615 39.088 1.00 26.11 ? 293 THR A CB 1 ATOM 2273 O OG1 . THR A 1 293 ? 42.546 24.667 38.365 1.00 24.46 ? 293 THR A OG1 1 ATOM 2274 C CG2 . THR A 1 293 ? 43.632 22.536 38.121 1.00 25.03 ? 293 THR A CG2 1 ATOM 2275 N N . THR A 1 294 ? 42.799 24.534 42.046 1.00 29.65 ? 294 THR A N 1 ATOM 2276 C CA . THR A 1 294 ? 42.678 25.718 42.884 1.00 34.30 ? 294 THR A CA 1 ATOM 2277 C C . THR A 1 294 ? 43.937 26.569 42.678 1.00 34.75 ? 294 THR A C 1 ATOM 2278 O O . THR A 1 294 ? 45.044 26.091 42.906 1.00 38.77 ? 294 THR A O 1 ATOM 2279 C CB . THR A 1 294 ? 42.509 25.318 44.370 1.00 37.04 ? 294 THR A CB 1 ATOM 2280 O OG1 . THR A 1 294 ? 41.440 24.361 44.480 1.00 39.87 ? 294 THR A OG1 1 ATOM 2281 C CG2 . THR A 1 294 ? 42.208 26.540 45.260 1.00 39.71 ? 294 THR A CG2 1 ATOM 2282 N N . PRO A 1 295 ? 43.790 27.805 42.177 1.00 34.42 ? 295 PRO A N 1 ATOM 2283 C CA . PRO A 1 295 ? 42.558 28.445 41.715 1.00 32.44 ? 295 PRO A CA 1 ATOM 2284 C C . PRO A 1 295 ? 41.969 27.733 40.485 1.00 28.99 ? 295 PRO A C 1 ATOM 2285 O O . PRO A 1 295 ? 42.670 26.982 39.792 1.00 28.04 ? 295 PRO A O 1 ATOM 2286 C CB . PRO A 1 295 ? 43.011 29.861 41.327 1.00 34.01 ? 295 PRO A CB 1 ATOM 2287 C CG . PRO A 1 295 ? 44.420 30.011 41.855 1.00 32.99 ? 295 PRO A CG 1 ATOM 2288 C CD . PRO A 1 295 ? 44.982 28.637 41.931 1.00 34.05 ? 295 PRO A CD 1 ATOM 2289 N N . ALA A 1 296 ? 40.688 27.981 40.220 1.00 26.84 ? 296 ALA A N 1 ATOM 2290 C CA . ALA A 1 296 ? 40.051 27.431 39.027 1.00 26.52 ? 296 ALA A CA 1 ATOM 2291 C C . ALA A 1 296 ? 40.773 27.950 37.813 1.00 26.25 ? 296 ALA A C 1 ATOM 2292 O O . ALA A 1 296 ? 41.142 29.122 37.753 1.00 28.66 ? 296 ALA A O 1 ATOM 2293 C CB . ALA A 1 296 ? 38.575 27.861 38.971 1.00 24.75 ? 296 ALA A CB 1 ATOM 2294 N N . GLY A 1 297 ? 40.942 27.102 36.817 1.00 23.40 ? 297 GLY A N 1 ATOM 2295 C CA . GLY A 1 297 ? 41.466 27.545 35.527 1.00 23.74 ? 297 GLY A CA 1 ATOM 2296 C C . GLY A 1 297 ? 42.974 27.719 35.462 1.00 25.23 ? 297 GLY A C 1 ATOM 2297 O O . GLY A 1 297 ? 43.487 28.114 34.396 1.00 27.84 ? 297 GLY A O 1 ATOM 2298 N N . SER A 1 298 ? 43.664 27.405 36.563 1.00 25.96 ? 298 SER A N 1 ATOM 2299 C CA . SER A 1 298 ? 45.121 27.682 36.664 1.00 25.29 ? 298 SER A CA 1 ATOM 2300 C C . SER A 1 298 ? 45.991 26.619 35.973 1.00 26.92 ? 298 SER A C 1 ATOM 2301 O O . SER A 1 298 ? 47.216 26.816 35.811 1.00 26.70 ? 298 SER A O 1 ATOM 2302 C CB . SER A 1 298 ? 45.526 27.867 38.135 1.00 26.08 ? 298 SER A CB 1 ATOM 2303 O OG . SER A 1 298 ? 45.372 26.654 38.847 1.00 25.23 ? 298 SER A OG 1 ATOM 2304 N N . ASP A 1 299 ? 45.400 25.495 35.575 1.00 25.35 ? 299 ASP A N 1 ATOM 2305 C CA . ASP A 1 299 ? 46.132 24.525 34.754 1.00 22.84 ? 299 ASP A CA 1 ATOM 2306 C C . ASP A 1 299 ? 45.103 23.807 33.893 1.00 22.80 ? 299 ASP A C 1 ATOM 2307 O O . ASP A 1 299 ? 44.725 22.667 34.168 1.00 21.50 ? 299 ASP A O 1 ATOM 2308 C CB . ASP A 1 299 ? 46.877 23.515 35.620 1.00 24.51 ? 299 ASP A CB 1 ATOM 2309 C CG . ASP A 1 299 ? 47.852 22.660 34.816 1.00 25.49 ? 299 ASP A CG 1 ATOM 2310 O OD1 . ASP A 1 299 ? 47.754 22.607 33.557 1.00 25.85 ? 299 ASP A OD1 1 ATOM 2311 O OD2 . ASP A 1 299 ? 48.710 22.021 35.485 1.00 30.71 ? 299 ASP A OD2 1 ATOM 2312 N N . TYR A 1 300 ? 44.669 24.499 32.839 1.00 21.62 ? 300 TYR A N 1 ATOM 2313 C CA . TYR A 1 300 ? 43.611 23.938 31.982 1.00 20.58 ? 300 TYR A CA 1 ATOM 2314 C C . TYR A 1 300 ? 44.053 22.670 31.260 1.00 21.74 ? 300 TYR A C 1 ATOM 2315 O O . TYR A 1 300 ? 43.279 21.744 31.051 1.00 20.00 ? 300 TYR A O 1 ATOM 2316 C CB . TYR A 1 300 ? 43.072 24.985 31.016 1.00 20.34 ? 300 TYR A CB 1 ATOM 2317 C CG . TYR A 1 300 ? 41.726 24.661 30.439 1.00 20.79 ? 300 TYR A CG 1 ATOM 2318 C CD1 . TYR A 1 300 ? 40.598 24.645 31.244 1.00 20.87 ? 300 TYR A CD1 1 ATOM 2319 C CD2 . TYR A 1 300 ? 41.572 24.414 29.070 1.00 22.30 ? 300 TYR A CD2 1 ATOM 2320 C CE1 . TYR A 1 300 ? 39.345 24.378 30.710 1.00 20.75 ? 300 TYR A CE1 1 ATOM 2321 C CE2 . TYR A 1 300 ? 40.320 24.140 28.535 1.00 21.90 ? 300 TYR A CE2 1 ATOM 2322 C CZ . TYR A 1 300 ? 39.213 24.124 29.358 1.00 21.74 ? 300 TYR A CZ 1 ATOM 2323 O OH . TYR A 1 300 ? 37.939 23.871 28.833 1.00 21.51 ? 300 TYR A OH 1 ATOM 2324 N N . SER A 1 301 ? 45.347 22.574 30.908 1.00 20.14 ? 301 SER A N 1 ATOM 2325 C CA . SER A 1 301 ? 45.853 21.309 30.382 1.00 21.54 ? 301 SER A CA 1 ATOM 2326 C C . SER A 1 301 ? 45.553 20.108 31.302 1.00 20.04 ? 301 SER A C 1 ATOM 2327 O O . SER A 1 301 ? 45.103 19.024 30.862 1.00 20.61 ? 301 SER A O 1 ATOM 2328 C CB . SER A 1 301 ? 47.367 21.474 30.179 1.00 22.93 ? 301 SER A CB 1 ATOM 2329 O OG . SER A 1 301 ? 47.906 20.275 29.667 1.00 25.29 ? 301 SER A OG 1 ATOM 2330 N N . TYR A 1 302 ? 45.825 20.277 32.609 1.00 20.67 ? 302 TYR A N 1 ATOM 2331 C CA . TYR A 1 302 ? 45.509 19.218 33.571 1.00 19.85 ? 302 TYR A CA 1 ATOM 2332 C C . TYR A 1 302 ? 43.983 18.983 33.688 1.00 20.18 ? 302 TYR A C 1 ATOM 2333 O O . TYR A 1 302 ? 43.532 17.849 33.740 1.00 19.91 ? 302 TYR A O 1 ATOM 2334 C CB . TYR A 1 302 ? 46.094 19.561 34.961 1.00 22.39 ? 302 TYR A CB 1 ATOM 2335 C CG . TYR A 1 302 ? 45.734 18.532 35.982 1.00 22.93 ? 302 TYR A CG 1 ATOM 2336 C CD1 . TYR A 1 302 ? 46.390 17.278 36.005 1.00 23.85 ? 302 TYR A CD1 1 ATOM 2337 C CD2 . TYR A 1 302 ? 44.721 18.764 36.912 1.00 24.20 ? 302 TYR A CD2 1 ATOM 2338 C CE1 . TYR A 1 302 ? 46.063 16.321 36.942 1.00 25.33 ? 302 TYR A CE1 1 ATOM 2339 C CE2 . TYR A 1 302 ? 44.377 17.795 37.847 1.00 24.67 ? 302 TYR A CE2 1 ATOM 2340 C CZ . TYR A 1 302 ? 45.049 16.567 37.843 1.00 25.02 ? 302 TYR A CZ 1 ATOM 2341 O OH . TYR A 1 302 ? 44.722 15.604 38.777 1.00 29.27 ? 302 TYR A OH 1 ATOM 2342 N N . SER A 1 303 ? 43.234 20.074 33.719 1.00 19.52 ? 303 SER A N 1 ATOM 2343 C CA . SER A 1 303 ? 41.763 19.940 33.770 1.00 19.23 ? 303 SER A CA 1 ATOM 2344 C C . SER A 1 303 ? 41.237 19.063 32.639 1.00 18.44 ? 303 SER A C 1 ATOM 2345 O O . SER A 1 303 ? 40.355 18.209 32.864 1.00 18.30 ? 303 SER A O 1 ATOM 2346 C CB . SER A 1 303 ? 41.116 21.321 33.623 1.00 17.75 ? 303 SER A CB 1 ATOM 2347 O OG . SER A 1 303 ? 41.287 22.108 34.788 1.00 18.36 ? 303 SER A OG 1 ATOM 2348 N N . VAL A 1 304 ? 41.725 19.274 31.423 1.00 17.29 ? 304 VAL A N 1 ATOM 2349 C CA . VAL A 1 304 ? 41.317 18.447 30.278 1.00 16.80 ? 304 VAL A CA 1 ATOM 2350 C C . VAL A 1 304 ? 41.747 17.021 30.465 1.00 17.68 ? 304 VAL A C 1 ATOM 2351 O O . VAL A 1 304 ? 40.967 16.102 30.284 1.00 18.00 ? 304 VAL A O 1 ATOM 2352 C CB . VAL A 1 304 ? 41.806 19.024 28.911 1.00 16.99 ? 304 VAL A CB 1 ATOM 2353 C CG1 . VAL A 1 304 ? 41.499 18.075 27.747 1.00 17.44 ? 304 VAL A CG1 1 ATOM 2354 C CG2 . VAL A 1 304 ? 41.283 20.460 28.685 1.00 17.36 ? 304 VAL A CG2 1 ATOM 2355 N N . LYS A 1 305 ? 43.045 16.815 30.795 1.00 18.58 ? 305 LYS A N 1 ATOM 2356 C CA . LYS A 1 305 ? 43.471 15.458 31.014 1.00 22.02 ? 305 LYS A CA 1 ATOM 2357 C C . LYS A 1 305 ? 42.685 14.702 32.092 1.00 19.96 ? 305 LYS A C 1 ATOM 2358 O O . LYS A 1 305 ? 42.262 13.550 31.864 1.00 20.25 ? 305 LYS A O 1 ATOM 2359 C CB . LYS A 1 305 ? 44.988 15.476 31.369 1.00 23.26 ? 305 LYS A CB 1 ATOM 2360 C CG . LYS A 1 305 ? 45.637 14.119 31.442 1.00 27.41 ? 305 LYS A CG 1 ATOM 2361 C CD . LYS A 1 305 ? 47.146 14.258 31.624 1.00 26.27 ? 305 LYS A CD 1 ATOM 2362 C CE . LYS A 1 305 ? 47.501 14.453 33.087 1.00 24.79 ? 305 LYS A CE 1 ATOM 2363 N NZ . LYS A 1 305 ? 49.002 14.276 33.237 1.00 25.78 ? 305 LYS A NZ 1 ATOM 2364 N N . ALA A 1 306 ? 42.532 15.327 33.263 1.00 19.33 ? 306 ALA A N 1 ATOM 2365 C CA . ALA A 1 306 ? 41.943 14.679 34.420 1.00 19.19 ? 306 ALA A CA 1 ATOM 2366 C C . ALA A 1 306 ? 40.485 14.306 34.167 1.00 18.37 ? 306 ALA A C 1 ATOM 2367 O O . ALA A 1 306 ? 40.051 13.200 34.506 1.00 20.80 ? 306 ALA A O 1 ATOM 2368 C CB . ALA A 1 306 ? 42.046 15.570 35.647 1.00 21.41 ? 306 ALA A CB 1 ATOM 2369 N N . SER A 1 307 ? 39.778 15.230 33.505 1.00 18.41 ? 307 SER A N 1 ATOM 2370 C CA . SER A 1 307 ? 38.339 15.036 33.292 1.00 18.68 ? 307 SER A CA 1 ATOM 2371 C C . SER A 1 307 ? 38.064 13.987 32.231 1.00 17.69 ? 307 SER A C 1 ATOM 2372 O O . SER A 1 307 ? 37.192 13.117 32.394 1.00 17.32 ? 307 SER A O 1 ATOM 2373 C CB . SER A 1 307 ? 37.659 16.370 32.961 1.00 16.79 ? 307 SER A CB 1 ATOM 2374 O OG . SER A 1 307 ? 38.121 16.918 31.749 1.00 16.27 ? 307 SER A OG 1 ATOM 2375 N N . ILE A 1 308 ? 38.810 14.037 31.123 1.00 16.83 ? 308 ILE A N 1 ATOM 2376 C CA . ILE A 1 308 ? 38.575 13.072 30.070 1.00 17.12 ? 308 ILE A CA 1 ATOM 2377 C C . ILE A 1 308 ? 39.020 11.674 30.514 1.00 17.64 ? 308 ILE A C 1 ATOM 2378 O O . ILE A 1 308 ? 38.335 10.682 30.257 1.00 19.33 ? 308 ILE A O 1 ATOM 2379 C CB . ILE A 1 308 ? 39.227 13.550 28.745 1.00 18.05 ? 308 ILE A CB 1 ATOM 2380 C CG1 . ILE A 1 308 ? 38.609 14.908 28.297 1.00 17.40 ? 308 ILE A CG1 1 ATOM 2381 C CG2 . ILE A 1 308 ? 39.146 12.455 27.684 1.00 18.34 ? 308 ILE A CG2 1 ATOM 2382 C CD1 . ILE A 1 308 ? 37.083 14.937 28.158 1.00 18.55 ? 308 ILE A CD1 1 ATOM 2383 N N . LEU A 1 309 ? 40.171 11.604 31.213 1.00 19.42 ? 309 LEU A N 1 ATOM 2384 C CA . LEU A 1 309 ? 40.593 10.320 31.742 1.00 20.74 ? 309 LEU A CA 1 ATOM 2385 C C . LEU A 1 309 ? 39.676 9.789 32.839 1.00 19.60 ? 309 LEU A C 1 ATOM 2386 O O . LEU A 1 309 ? 39.510 8.564 32.961 1.00 21.37 ? 309 LEU A O 1 ATOM 2387 C CB . LEU A 1 309 ? 42.053 10.373 32.189 1.00 20.89 ? 309 LEU A CB 1 ATOM 2388 C CG . LEU A 1 309 ? 43.022 10.494 31.010 1.00 24.46 ? 309 LEU A CG 1 ATOM 2389 C CD1 . LEU A 1 309 ? 44.374 10.541 31.693 1.00 25.30 ? 309 LEU A CD1 1 ATOM 2390 C CD2 . LEU A 1 309 ? 42.911 9.306 30.053 1.00 23.51 ? 309 LEU A CD2 1 ATOM 2391 N N . ALA A 1 310 ? 39.007 10.696 33.568 1.00 19.34 ? 310 ALA A N 1 ATOM 2392 C CA . ALA A 1 310 ? 38.030 10.268 34.574 1.00 19.54 ? 310 ALA A CA 1 ATOM 2393 C C . ALA A 1 310 ? 36.796 9.592 33.945 1.00 18.76 ? 310 ALA A C 1 ATOM 2394 O O . ALA A 1 310 ? 36.074 8.863 34.626 1.00 18.81 ? 310 ALA A O 1 ATOM 2395 C CB . ALA A 1 310 ? 37.598 11.434 35.441 1.00 19.19 ? 310 ALA A CB 1 ATOM 2396 N N . GLY A 1 311 ? 36.538 9.895 32.656 1.00 17.12 ? 311 GLY A N 1 ATOM 2397 C CA . GLY A 1 311 ? 35.431 9.281 31.920 1.00 17.89 ? 311 GLY A CA 1 ATOM 2398 C C . GLY A 1 311 ? 34.373 10.266 31.447 1.00 16.95 ? 311 GLY A C 1 ATOM 2399 O O . GLY A 1 311 ? 33.363 9.827 30.909 1.00 17.90 ? 311 GLY A O 1 ATOM 2400 N N . LEU A 1 312 ? 34.615 11.571 31.598 1.00 15.37 ? 312 LEU A N 1 ATOM 2401 C CA . LEU A 1 312 ? 33.599 12.541 31.038 1.00 15.43 ? 312 LEU A CA 1 ATOM 2402 C C . LEU A 1 312 ? 33.605 12.465 29.525 1.00 16.24 ? 312 LEU A C 1 ATOM 2403 O O . LEU A 1 312 ? 34.677 12.211 28.912 1.00 16.76 ? 312 LEU A O 1 ATOM 2404 C CB . LEU A 1 312 ? 33.816 13.985 31.494 1.00 16.23 ? 312 LEU A CB 1 ATOM 2405 C CG . LEU A 1 312 ? 33.314 14.303 32.935 1.00 16.47 ? 312 LEU A CG 1 ATOM 2406 C CD1 . LEU A 1 312 ? 34.172 13.620 34.017 1.00 18.17 ? 312 LEU A CD1 1 ATOM 2407 C CD2 . LEU A 1 312 ? 33.257 15.797 33.147 1.00 17.43 ? 312 LEU A CD2 1 ATOM 2408 N N . ASP A 1 313 ? 32.434 12.646 28.898 1.00 14.44 ? 313 ASP A N 1 ATOM 2409 C CA . ASP A 1 313 ? 32.314 12.467 27.427 1.00 14.13 ? 313 ASP A CA 1 ATOM 2410 C C . ASP A 1 313 ? 32.160 13.769 26.668 1.00 14.07 ? 313 ASP A C 1 ATOM 2411 O O . ASP A 1 313 ? 32.698 13.905 25.574 1.00 14.85 ? 313 ASP A O 1 ATOM 2412 C CB . ASP A 1 313 ? 31.091 11.586 27.111 1.00 14.46 ? 313 ASP A CB 1 ATOM 2413 C CG . ASP A 1 313 ? 31.161 10.248 27.817 1.00 15.76 ? 313 ASP A CG 1 ATOM 2414 O OD1 . ASP A 1 313 ? 32.217 9.545 27.690 1.00 16.38 ? 313 ASP A OD1 1 ATOM 2415 O OD2 . ASP A 1 313 ? 30.191 9.814 28.440 1.00 14.89 ? 313 ASP A OD2 1 ATOM 2416 N N . MET A 1 314 ? 31.375 14.718 27.250 1.00 14.52 ? 314 MET A N 1 ATOM 2417 C CA . MET A 1 314 ? 31.133 16.030 26.630 1.00 14.46 ? 314 MET A CA 1 ATOM 2418 C C . MET A 1 314 ? 31.467 17.089 27.632 1.00 14.04 ? 314 MET A C 1 ATOM 2419 O O . MET A 1 314 ? 31.075 16.978 28.805 1.00 13.81 ? 314 MET A O 1 ATOM 2420 C CB . MET A 1 314 ? 29.648 16.144 26.171 1.00 13.93 ? 314 MET A CB 1 ATOM 2421 C CG . MET A 1 314 ? 29.366 17.485 25.495 1.00 13.12 ? 314 MET A CG 1 ATOM 2422 S SD . MET A 1 314 ? 27.615 17.654 24.965 1.00 14.59 ? 314 MET A SD 1 ATOM 2423 C CE . MET A 1 314 ? 27.554 16.467 23.590 1.00 14.82 ? 314 MET A CE 1 ATOM 2424 N N . ILE A 1 315 ? 32.199 18.123 27.199 1.00 13.51 ? 315 ILE A N 1 ATOM 2425 C CA . ILE A 1 315 ? 32.586 19.187 28.095 1.00 14.25 ? 315 ILE A CA 1 ATOM 2426 C C . ILE A 1 315 ? 31.791 20.467 27.763 1.00 13.51 ? 315 ILE A C 1 ATOM 2427 O O . ILE A 1 315 ? 31.767 20.944 26.620 1.00 13.16 ? 315 ILE A O 1 ATOM 2428 C CB . ILE A 1 315 ? 34.120 19.437 27.992 1.00 13.68 ? 315 ILE A CB 1 ATOM 2429 C CG1 . ILE A 1 315 ? 34.912 18.168 28.369 1.00 15.19 ? 315 ILE A CG1 1 ATOM 2430 C CG2 . ILE A 1 315 ? 34.510 20.619 28.867 1.00 14.96 ? 315 ILE A CG2 1 ATOM 2431 C CD1 . ILE A 1 315 ? 34.590 17.505 29.694 1.00 14.38 ? 315 ILE A CD1 1 ATOM 2432 N N . MET A 1 316 ? 31.083 20.955 28.803 1.00 12.79 ? 316 MET A N 1 ATOM 2433 C CA . MET A 1 316 ? 30.373 22.242 28.778 1.00 13.64 ? 316 MET A CA 1 ATOM 2434 C C . MET A 1 316 ? 31.503 23.264 28.991 1.00 13.43 ? 316 MET A C 1 ATOM 2435 O O . MET A 1 316 ? 31.857 23.654 30.130 1.00 14.00 ? 316 MET A O 1 ATOM 2436 C CB . MET A 1 316 ? 29.278 22.226 29.869 1.00 13.68 ? 316 MET A CB 1 ATOM 2437 C CG . MET A 1 316 ? 28.486 23.533 29.864 1.00 13.16 ? 316 MET A CG 1 ATOM 2438 S SD . MET A 1 316 ? 27.311 23.608 31.255 1.00 14.02 ? 316 MET A SD 1 ATOM 2439 C CE . MET A 1 316 ? 26.351 22.129 30.939 1.00 15.56 ? 316 MET A CE 1 ATOM 2440 N N . VAL A 1 317 ? 32.032 23.729 27.870 1.00 13.83 ? 317 VAL A N 1 ATOM 2441 C CA . VAL A 1 317 ? 33.323 24.462 27.956 1.00 14.47 ? 317 VAL A CA 1 ATOM 2442 C C . VAL A 1 317 ? 33.173 25.730 28.826 1.00 14.79 ? 317 VAL A C 1 ATOM 2443 O O . VAL A 1 317 ? 33.908 25.887 29.812 1.00 15.61 ? 317 VAL A O 1 ATOM 2444 C CB . VAL A 1 317 ? 33.913 24.700 26.570 1.00 15.25 ? 317 VAL A CB 1 ATOM 2445 C CG1 . VAL A 1 317 ? 35.218 25.490 26.751 1.00 15.70 ? 317 VAL A CG1 1 ATOM 2446 C CG2 . VAL A 1 317 ? 34.167 23.356 25.882 1.00 16.90 ? 317 VAL A CG2 1 ATOM 2447 N N . PRO A 1 318 ? 32.169 26.618 28.553 1.00 14.25 ? 318 PRO A N 1 ATOM 2448 C CA . PRO A 1 318 ? 31.344 26.682 27.359 1.00 15.19 ? 318 PRO A CA 1 ATOM 2449 C C . PRO A 1 318 ? 31.835 27.791 26.395 1.00 15.07 ? 318 PRO A C 1 ATOM 2450 O O . PRO A 1 318 ? 31.255 27.940 25.338 1.00 15.20 ? 318 PRO A O 1 ATOM 2451 C CB . PRO A 1 318 ? 29.977 27.133 27.954 1.00 14.81 ? 318 PRO A CB 1 ATOM 2452 C CG . PRO A 1 318 ? 30.380 28.094 29.052 1.00 16.00 ? 318 PRO A CG 1 ATOM 2453 C CD . PRO A 1 318 ? 31.667 27.497 29.640 1.00 15.15 ? 318 PRO A CD 1 ATOM 2454 N N . ASN A 1 319 ? 32.860 28.586 26.777 1.00 16.23 ? 319 ASN A N 1 ATOM 2455 C CA . ASN A 1 319 ? 33.281 29.746 25.993 1.00 17.11 ? 319 ASN A CA 1 ATOM 2456 C C . ASN A 1 319 ? 34.618 29.534 25.268 1.00 18.03 ? 319 ASN A C 1 ATOM 2457 O O . ASN A 1 319 ? 34.699 29.816 24.075 1.00 19.14 ? 319 ASN A O 1 ATOM 2458 C CB . ASN A 1 319 ? 33.367 30.974 26.919 1.00 17.95 ? 319 ASN A CB 1 ATOM 2459 C CG . ASN A 1 319 ? 32.029 31.323 27.513 1.00 18.87 ? 319 ASN A CG 1 ATOM 2460 O OD1 . ASN A 1 319 ? 31.003 31.189 26.835 1.00 20.57 ? 319 ASN A OD1 1 ATOM 2461 N ND2 . ASN A 1 319 ? 32.008 31.651 28.798 1.00 21.74 ? 319 ASN A ND2 1 ATOM 2462 N N . LYS A 1 320 ? 35.627 28.994 25.968 1.00 20.78 ? 320 LYS A N 1 ATOM 2463 C CA . LYS A 1 320 ? 36.992 28.843 25.418 1.00 21.94 ? 320 LYS A CA 1 ATOM 2464 C C . LYS A 1 320 ? 37.149 27.568 24.610 1.00 20.49 ? 320 LYS A C 1 ATOM 2465 O O . LYS A 1 320 ? 38.026 26.709 24.846 1.00 19.82 ? 320 LYS A O 1 ATOM 2466 C CB . LYS A 1 320 ? 38.012 28.944 26.544 1.00 26.04 ? 320 LYS A CB 1 ATOM 2467 C CG . LYS A 1 320 ? 37.912 30.260 27.279 1.00 32.02 ? 320 LYS A CG 1 ATOM 2468 C CD . LYS A 1 320 ? 39.131 30.537 28.161 1.00 40.63 ? 320 LYS A CD 1 ATOM 2469 C CE . LYS A 1 320 ? 39.903 29.268 28.534 1.00 44.83 ? 320 LYS A CE 1 ATOM 2470 N NZ . LYS A 1 320 ? 39.205 28.273 29.402 1.00 42.52 ? 320 LYS A NZ 1 ATOM 2471 N N . TYR A 1 321 ? 36.324 27.424 23.569 1.00 17.75 ? 321 TYR A N 1 ATOM 2472 C CA . TYR A 1 321 ? 36.352 26.165 22.796 1.00 18.49 ? 321 TYR A CA 1 ATOM 2473 C C . TYR A 1 321 ? 37.681 25.949 22.042 1.00 17.86 ? 321 TYR A C 1 ATOM 2474 O O . TYR A 1 321 ? 38.083 24.813 21.833 1.00 18.28 ? 321 TYR A O 1 ATOM 2475 C CB . TYR A 1 321 ? 35.120 26.040 21.840 1.00 17.74 ? 321 TYR A CB 1 ATOM 2476 C CG . TYR A 1 321 ? 35.044 27.231 20.902 1.00 17.75 ? 321 TYR A CG 1 ATOM 2477 C CD1 . TYR A 1 321 ? 35.789 27.252 19.711 1.00 17.88 ? 321 TYR A CD1 1 ATOM 2478 C CD2 . TYR A 1 321 ? 34.295 28.382 21.221 1.00 17.32 ? 321 TYR A CD2 1 ATOM 2479 C CE1 . TYR A 1 321 ? 35.815 28.369 18.896 1.00 18.75 ? 321 TYR A CE1 1 ATOM 2480 C CE2 . TYR A 1 321 ? 34.298 29.500 20.390 1.00 17.74 ? 321 TYR A CE2 1 ATOM 2481 C CZ . TYR A 1 321 ? 35.060 29.476 19.225 1.00 17.06 ? 321 TYR A CZ 1 ATOM 2482 O OH . TYR A 1 321 ? 35.116 30.571 18.410 1.00 21.28 ? 321 TYR A OH 1 ATOM 2483 N N . GLN A 1 322 ? 38.281 27.024 21.523 1.00 20.30 ? 322 GLN A N 1 ATOM 2484 C CA . GLN A 1 322 ? 39.519 26.878 20.726 1.00 21.44 ? 322 GLN A CA 1 ATOM 2485 C C . GLN A 1 322 ? 40.626 26.295 21.616 1.00 19.98 ? 322 GLN A C 1 ATOM 2486 O O . GLN A 1 322 ? 41.295 25.328 21.208 1.00 21.86 ? 322 GLN A O 1 ATOM 2487 C CB . GLN A 1 322 ? 39.961 28.233 20.162 1.00 24.38 ? 322 GLN A CB 1 ATOM 2488 C CG . GLN A 1 322 ? 41.232 28.134 19.313 1.00 30.83 ? 322 GLN A CG 1 ATOM 2489 C CD . GLN A 1 322 ? 41.792 29.509 18.975 1.00 39.09 ? 322 GLN A CD 1 ATOM 2490 O OE1 . GLN A 1 322 ? 41.173 30.261 18.230 1.00 44.44 ? 322 GLN A OE1 1 ATOM 2491 N NE2 . GLN A 1 322 ? 42.961 29.851 19.539 1.00 43.18 ? 322 GLN A NE2 1 ATOM 2492 N N . GLN A 1 323 ? 40.722 26.810 22.832 1.00 20.45 ? 323 GLN A N 1 ATOM 2493 C CA . GLN A 1 323 ? 41.711 26.264 23.811 1.00 20.74 ? 323 GLN A CA 1 ATOM 2494 C C . GLN A 1 323 ? 41.368 24.847 24.214 1.00 20.44 ? 323 GLN A C 1 ATOM 2495 O O . GLN A 1 323 ? 42.231 23.960 24.233 1.00 18.47 ? 323 GLN A O 1 ATOM 2496 C CB . GLN A 1 323 ? 41.857 27.153 25.031 1.00 23.27 ? 323 GLN A CB 1 ATOM 2497 C CG . GLN A 1 323 ? 42.902 26.584 25.984 1.00 30.65 ? 323 GLN A CG 1 ATOM 2498 C CD . GLN A 1 323 ? 43.223 27.468 27.179 1.00 39.05 ? 323 GLN A CD 1 ATOM 2499 O OE1 . GLN A 1 323 ? 42.548 28.461 27.443 1.00 42.18 ? 323 GLN A OE1 1 ATOM 2500 N NE2 . GLN A 1 323 ? 44.264 27.089 27.924 1.00 40.75 ? 323 GLN A NE2 1 ATOM 2501 N N . PHE A 1 324 ? 40.070 24.579 24.474 1.00 17.59 ? 324 PHE A N 1 ATOM 2502 C CA . PHE A 1 324 ? 39.707 23.213 24.792 1.00 16.48 ? 324 PHE A CA 1 ATOM 2503 C C . PHE A 1 324 ? 40.104 22.211 23.695 1.00 15.44 ? 324 PHE A C 1 ATOM 2504 O O . PHE A 1 324 ? 40.736 21.163 23.961 1.00 16.40 ? 324 PHE A O 1 ATOM 2505 C CB . PHE A 1 324 ? 38.176 23.115 25.116 1.00 15.97 ? 324 PHE A CB 1 ATOM 2506 C CG . PHE A 1 324 ? 37.720 21.689 25.331 1.00 15.76 ? 324 PHE A CG 1 ATOM 2507 C CD1 . PHE A 1 324 ? 38.074 20.982 26.503 1.00 15.24 ? 324 PHE A CD1 1 ATOM 2508 C CD2 . PHE A 1 324 ? 37.028 21.001 24.325 1.00 15.84 ? 324 PHE A CD2 1 ATOM 2509 C CE1 . PHE A 1 324 ? 37.721 19.654 26.660 1.00 15.98 ? 324 PHE A CE1 1 ATOM 2510 C CE2 . PHE A 1 324 ? 36.655 19.674 24.480 1.00 15.80 ? 324 PHE A CE2 1 ATOM 2511 C CZ . PHE A 1 324 ? 37.000 19.008 25.646 1.00 16.16 ? 324 PHE A CZ 1 ATOM 2512 N N . ILE A 1 325 ? 39.673 22.476 22.450 1.00 15.47 ? 325 ILE A N 1 ATOM 2513 C CA . ILE A 1 325 ? 39.927 21.569 21.336 1.00 14.88 ? 325 ILE A CA 1 ATOM 2514 C C . ILE A 1 325 ? 41.474 21.451 21.123 1.00 14.58 ? 325 ILE A C 1 ATOM 2515 O O . ILE A 1 325 ? 41.966 20.357 20.915 1.00 17.16 ? 325 ILE A O 1 ATOM 2516 C CB . ILE A 1 325 ? 39.215 22.069 20.071 1.00 16.54 ? 325 ILE A CB 1 ATOM 2517 C CG1 . ILE A 1 325 ? 37.664 21.965 20.249 1.00 18.38 ? 325 ILE A CG1 1 ATOM 2518 C CG2 . ILE A 1 325 ? 39.676 21.272 18.875 1.00 18.39 ? 325 ILE A CG2 1 ATOM 2519 C CD1 . ILE A 1 325 ? 36.940 22.734 19.170 1.00 17.79 ? 325 ILE A CD1 1 ATOM 2520 N N . SER A 1 326 ? 42.164 22.585 21.217 1.00 14.96 ? 326 SER A N 1 ATOM 2521 C CA . SER A 1 326 ? 43.634 22.551 21.024 1.00 17.23 ? 326 SER A CA 1 ATOM 2522 C C . SER A 1 326 ? 44.346 21.676 22.051 1.00 17.52 ? 326 SER A C 1 ATOM 2523 O O . SER A 1 326 ? 45.221 20.838 21.675 1.00 18.65 ? 326 SER A O 1 ATOM 2524 C CB . SER A 1 326 ? 44.152 23.938 21.086 1.00 16.52 ? 326 SER A CB 1 ATOM 2525 O OG . SER A 1 326 ? 45.576 23.954 20.739 1.00 17.77 ? 326 SER A OG 1 ATOM 2526 N N . ILE A 1 327 ? 43.991 21.861 23.336 1.00 17.81 ? 327 ILE A N 1 ATOM 2527 C CA . ILE A 1 327 ? 44.611 21.075 24.412 1.00 16.66 ? 327 ILE A CA 1 ATOM 2528 C C . ILE A 1 327 ? 44.285 19.601 24.305 1.00 18.19 ? 327 ILE A C 1 ATOM 2529 O O . ILE A 1 327 ? 45.162 18.745 24.397 1.00 18.14 ? 327 ILE A O 1 ATOM 2530 C CB . ILE A 1 327 ? 44.213 21.665 25.779 1.00 17.84 ? 327 ILE A CB 1 ATOM 2531 C CG1 . ILE A 1 327 ? 44.883 23.055 25.924 1.00 19.63 ? 327 ILE A CG1 1 ATOM 2532 C CG2 . ILE A 1 327 ? 44.550 20.717 26.928 1.00 18.45 ? 327 ILE A CG2 1 ATOM 2533 C CD1 . ILE A 1 327 ? 44.518 23.813 27.171 1.00 25.65 ? 327 ILE A CD1 1 ATOM 2534 N N . LEU A 1 328 ? 43.008 19.260 24.045 1.00 15.52 ? 328 LEU A N 1 ATOM 2535 C CA . LEU A 1 328 ? 42.672 17.838 23.936 1.00 17.00 ? 328 LEU A CA 1 ATOM 2536 C C . LEU A 1 328 ? 43.371 17.196 22.724 1.00 16.37 ? 328 LEU A C 1 ATOM 2537 O O . LEU A 1 328 ? 43.830 16.056 22.831 1.00 17.01 ? 328 LEU A O 1 ATOM 2538 C CB . LEU A 1 328 ? 41.108 17.646 23.938 1.00 16.39 ? 328 LEU A CB 1 ATOM 2539 C CG . LEU A 1 328 ? 40.588 16.213 23.861 1.00 17.41 ? 328 LEU A CG 1 ATOM 2540 C CD1 . LEU A 1 328 ? 41.207 15.335 24.938 1.00 17.49 ? 328 LEU A CD1 1 ATOM 2541 C CD2 . LEU A 1 328 ? 39.058 16.277 24.022 1.00 16.57 ? 328 LEU A CD2 1 ATOM 2542 N N . THR A 1 329 ? 43.395 17.913 21.582 1.00 16.23 ? 329 THR A N 1 ATOM 2543 C CA . THR A 1 329 ? 44.040 17.399 20.372 1.00 16.60 ? 329 THR A CA 1 ATOM 2544 C C . THR A 1 329 ? 45.524 17.122 20.707 1.00 17.59 ? 329 THR A C 1 ATOM 2545 O O . THR A 1 329 ? 46.029 16.052 20.379 1.00 18.70 ? 329 THR A O 1 ATOM 2546 C CB . THR A 1 329 ? 43.953 18.400 19.226 1.00 17.51 ? 329 THR A CB 1 ATOM 2547 O OG1 . THR A 1 329 ? 42.569 18.584 18.886 1.00 17.97 ? 329 THR A OG1 1 ATOM 2548 C CG2 . THR A 1 329 ? 44.632 17.846 17.987 1.00 16.51 ? 329 THR A CG2 1 ATOM 2549 N N . GLY A 1 330 ? 46.129 18.060 21.413 1.00 18.53 ? 330 GLY A N 1 ATOM 2550 C CA . GLY A 1 330 ? 47.555 17.897 21.807 1.00 18.85 ? 330 GLY A CA 1 ATOM 2551 C C . GLY A 1 330 ? 47.771 16.678 22.680 1.00 19.50 ? 330 GLY A C 1 ATOM 2552 O O . GLY A 1 330 ? 48.740 15.911 22.517 1.00 21.03 ? 330 GLY A O 1 ATOM 2553 N N . HIS A 1 331 ? 46.900 16.489 23.681 1.00 17.95 ? 331 HIS A N 1 ATOM 2554 C CA . HIS A 1 331 ? 47.001 15.284 24.498 1.00 18.48 ? 331 HIS A CA 1 ATOM 2555 C C . HIS A 1 331 ? 46.867 14.017 23.714 1.00 18.75 ? 331 HIS A C 1 ATOM 2556 O O . HIS A 1 331 ? 47.555 13.040 24.006 1.00 19.99 ? 331 HIS A O 1 ATOM 2557 C CB . HIS A 1 331 ? 45.954 15.330 25.619 1.00 18.18 ? 331 HIS A CB 1 ATOM 2558 C CG . HIS A 1 331 ? 46.344 16.242 26.738 1.00 19.94 ? 331 HIS A CG 1 ATOM 2559 N ND1 . HIS A 1 331 ? 45.448 16.941 27.525 1.00 20.94 ? 331 HIS A ND1 1 ATOM 2560 C CD2 . HIS A 1 331 ? 47.582 16.568 27.194 1.00 19.95 ? 331 HIS A CD2 1 ATOM 2561 C CE1 . HIS A 1 331 ? 46.124 17.637 28.436 1.00 18.23 ? 331 HIS A CE1 1 ATOM 2562 N NE2 . HIS A 1 331 ? 47.418 17.447 28.234 1.00 23.77 ? 331 HIS A NE2 1 ATOM 2563 N N . VAL A 1 332 ? 45.904 13.961 22.777 1.00 17.64 ? 332 VAL A N 1 ATOM 2564 C CA . VAL A 1 332 ? 45.752 12.760 21.966 1.00 17.70 ? 332 VAL A CA 1 ATOM 2565 C C . VAL A 1 332 ? 46.998 12.535 21.099 1.00 19.55 ? 332 VAL A C 1 ATOM 2566 O O . VAL A 1 332 ? 47.525 11.412 21.050 1.00 20.48 ? 332 VAL A O 1 ATOM 2567 C CB . VAL A 1 332 ? 44.429 12.823 21.142 1.00 18.26 ? 332 VAL A CB 1 ATOM 2568 C CG1 . VAL A 1 332 ? 44.327 11.617 20.231 1.00 21.10 ? 332 VAL A CG1 1 ATOM 2569 C CG2 . VAL A 1 332 ? 43.247 12.878 22.122 1.00 19.96 ? 332 VAL A CG2 1 ATOM 2570 N N A ASN A 1 333 ? 47.471 13.589 20.461 0.60 19.63 ? 333 ASN A N 1 ATOM 2571 N N B ASN A 1 333 ? 47.453 13.612 20.449 0.40 19.76 ? 333 ASN A N 1 ATOM 2572 C CA . ASN A 1 333 ? 48.607 13.479 19.539 1.00 20.60 ? 333 ASN A CA 1 ATOM 2573 C C . ASN A 1 333 ? 49.880 13.054 20.273 1.00 21.57 ? 333 ASN A C 1 ATOM 2574 O O . ASN A 1 333 ? 50.741 12.366 19.684 1.00 23.32 ? 333 ASN A O 1 ATOM 2575 C CB A ASN A 1 333 ? 48.928 14.937 18.965 0.60 19.83 ? 333 ASN A CB 1 ATOM 2576 C CB B ASN A 1 333 ? 48.619 14.413 18.341 0.40 20.04 ? 333 ASN A CB 1 ATOM 2577 C CG A ASN A 1 333 ? 47.991 15.423 17.801 0.60 18.63 ? 333 ASN A CG 1 ATOM 2578 C CG B ASN A 1 333 ? 47.559 14.024 17.306 0.40 19.29 ? 333 ASN A CG 1 ATOM 2579 O OD1 A ASN A 1 333 ? 47.233 14.625 17.255 0.60 20.06 ? 333 ASN A OD1 1 ATOM 2580 O OD1 B ASN A 1 333 ? 47.158 12.845 17.186 0.40 19.34 ? 333 ASN A OD1 1 ATOM 2581 N ND2 A ASN A 1 333 ? 48.064 16.739 17.408 0.60 18.15 ? 333 ASN A ND2 1 ATOM 2582 N ND2 B ASN A 1 333 ? 47.107 15.012 16.533 0.40 17.95 ? 333 ASN A ND2 1 ATOM 2583 N N . GLY A 1 334 ? 49.937 13.362 21.564 1.00 20.17 ? 334 GLY A N 1 ATOM 2584 C CA . GLY A 1 334 ? 51.112 13.085 22.419 1.00 22.32 ? 334 GLY A CA 1 ATOM 2585 C C . GLY A 1 334 ? 50.992 11.746 23.127 1.00 23.62 ? 334 GLY A C 1 ATOM 2586 O O . GLY A 1 334 ? 51.896 11.347 23.885 1.00 25.28 ? 334 GLY A O 1 ATOM 2587 N N . GLY A 1 335 ? 49.884 11.031 22.905 1.00 21.98 ? 335 GLY A N 1 ATOM 2588 C CA . GLY A 1 335 ? 49.654 9.757 23.559 1.00 22.45 ? 335 GLY A CA 1 ATOM 2589 C C . GLY A 1 335 ? 49.271 9.788 25.022 1.00 22.35 ? 335 GLY A C 1 ATOM 2590 O O . GLY A 1 335 ? 49.275 8.735 25.694 1.00 25.36 ? 335 GLY A O 1 ATOM 2591 N N . VAL A 1 336 ? 48.938 10.977 25.553 1.00 21.85 ? 336 VAL A N 1 ATOM 2592 C CA . VAL A 1 336 ? 48.570 11.169 26.958 1.00 22.15 ? 336 VAL A CA 1 ATOM 2593 C C . VAL A 1 336 ? 47.139 10.682 27.210 1.00 22.60 ? 336 VAL A C 1 ATOM 2594 O O . VAL A 1 336 ? 46.800 10.219 28.301 1.00 24.36 ? 336 VAL A O 1 ATOM 2595 C CB . VAL A 1 336 ? 48.721 12.660 27.380 1.00 22.50 ? 336 VAL A CB 1 ATOM 2596 C CG1 . VAL A 1 336 ? 48.177 12.953 28.766 1.00 24.58 ? 336 VAL A CG1 1 ATOM 2597 C CG2 . VAL A 1 336 ? 50.178 13.113 27.271 1.00 24.36 ? 336 VAL A CG2 1 ATOM 2598 N N . ILE A 1 337 ? 46.279 10.875 26.204 1.00 21.66 ? 337 ILE A N 1 ATOM 2599 C CA . ILE A 1 337 ? 44.904 10.341 26.237 1.00 21.08 ? 337 ILE A CA 1 ATOM 2600 C C . ILE A 1 337 ? 44.773 9.382 25.065 1.00 20.81 ? 337 ILE A C 1 ATOM 2601 O O . ILE A 1 337 ? 45.010 9.754 23.930 1.00 22.72 ? 337 ILE A O 1 ATOM 2602 C CB . ILE A 1 337 ? 43.852 11.492 26.103 1.00 20.10 ? 337 ILE A CB 1 ATOM 2603 C CG1 . ILE A 1 337 ? 43.893 12.392 27.353 1.00 21.34 ? 337 ILE A CG1 1 ATOM 2604 C CG2 . ILE A 1 337 ? 42.438 10.901 25.916 1.00 21.64 ? 337 ILE A CG2 1 ATOM 2605 C CD1 . ILE A 1 337 ? 43.103 13.688 27.267 1.00 22.18 ? 337 ILE A CD1 1 ATOM 2606 N N . PRO A 1 338 ? 44.424 8.131 25.325 1.00 19.99 ? 338 PRO A N 1 ATOM 2607 C CA . PRO A 1 338 ? 44.374 7.174 24.221 1.00 20.74 ? 338 PRO A CA 1 ATOM 2608 C C . PRO A 1 338 ? 43.155 7.375 23.320 1.00 20.63 ? 338 PRO A C 1 ATOM 2609 O O . PRO A 1 338 ? 42.110 7.903 23.784 1.00 19.87 ? 338 PRO A O 1 ATOM 2610 C CB . PRO A 1 338 ? 44.279 5.825 24.919 1.00 21.90 ? 338 PRO A CB 1 ATOM 2611 C CG . PRO A 1 338 ? 43.660 6.132 26.246 1.00 22.78 ? 338 PRO A CG 1 ATOM 2612 C CD . PRO A 1 338 ? 44.037 7.543 26.614 1.00 20.78 ? 338 PRO A CD 1 ATOM 2613 N N . MET A 1 339 ? 43.284 6.954 22.075 1.00 21.10 ? 339 MET A N 1 ATOM 2614 C CA . MET A 1 339 ? 42.150 7.007 21.150 1.00 20.86 ? 339 MET A CA 1 ATOM 2615 C C . MET A 1 339 ? 40.926 6.231 21.642 1.00 21.28 ? 339 MET A C 1 ATOM 2616 O O . MET A 1 339 ? 39.800 6.602 21.315 1.00 20.25 ? 339 MET A O 1 ATOM 2617 C CB . MET A 1 339 ? 42.559 6.547 19.730 1.00 22.10 ? 339 MET A CB 1 ATOM 2618 C CG . MET A 1 339 ? 43.242 7.684 18.986 1.00 26.00 ? 339 MET A CG 1 ATOM 2619 S SD . MET A 1 339 ? 42.255 9.215 18.852 1.00 34.01 ? 339 MET A SD 1 ATOM 2620 C CE . MET A 1 339 ? 40.861 8.610 18.106 1.00 18.36 ? 339 MET A CE 1 ATOM 2621 N N . SER A 1 340 ? 41.118 5.172 22.420 1.00 20.18 ? 340 SER A N 1 ATOM 2622 C CA . SER A 1 340 ? 39.982 4.364 22.920 1.00 20.83 ? 340 SER A CA 1 ATOM 2623 C C . SER A 1 340 ? 39.082 5.251 23.772 1.00 21.15 ? 340 SER A C 1 ATOM 2624 O O . SER A 1 340 ? 37.865 5.067 23.788 1.00 20.77 ? 340 SER A O 1 ATOM 2625 C CB . SER A 1 340 ? 40.471 3.165 23.760 1.00 21.92 ? 340 SER A CB 1 ATOM 2626 O OG . SER A 1 340 ? 41.289 3.578 24.820 1.00 22.85 ? 340 SER A OG 1 ATOM 2627 N N . ARG A 1 341 ? 39.671 6.207 24.490 1.00 18.96 ? 341 ARG A N 1 ATOM 2628 C CA . ARG A 1 341 ? 38.875 7.110 25.385 1.00 17.86 ? 341 ARG A CA 1 ATOM 2629 C C . ARG A 1 341 ? 38.064 8.087 24.547 1.00 17.51 ? 341 ARG A C 1 ATOM 2630 O O . ARG A 1 341 ? 36.869 8.287 24.843 1.00 17.10 ? 341 ARG A O 1 ATOM 2631 C CB . ARG A 1 341 ? 39.826 7.841 26.345 1.00 18.94 ? 341 ARG A CB 1 ATOM 2632 C CG . ARG A 1 341 ? 39.195 8.718 27.428 1.00 19.38 ? 341 ARG A CG 1 ATOM 2633 C CD . ARG A 1 341 ? 38.316 7.961 28.445 1.00 19.82 ? 341 ARG A CD 1 ATOM 2634 N NE . ARG A 1 341 ? 36.939 7.726 27.995 1.00 18.34 ? 341 ARG A NE 1 ATOM 2635 C CZ . ARG A 1 341 ? 35.984 8.672 28.001 1.00 18.29 ? 341 ARG A CZ 1 ATOM 2636 N NH1 . ARG A 1 341 ? 36.273 9.891 28.421 1.00 18.00 ? 341 ARG A NH1 1 ATOM 2637 N NH2 . ARG A 1 341 ? 34.755 8.375 27.567 1.00 19.34 ? 341 ARG A NH2 1 ATOM 2638 N N . ILE A 1 342 ? 38.675 8.687 23.529 1.00 17.48 ? 342 ILE A N 1 ATOM 2639 C CA . ILE A 1 342 ? 37.954 9.581 22.568 1.00 16.73 ? 342 ILE A CA 1 ATOM 2640 C C . ILE A 1 342 ? 36.827 8.795 21.915 1.00 17.00 ? 342 ILE A C 1 ATOM 2641 O O . ILE A 1 342 ? 35.677 9.311 21.797 1.00 15.65 ? 342 ILE A O 1 ATOM 2642 C CB . ILE A 1 342 ? 38.928 10.118 21.482 1.00 17.47 ? 342 ILE A CB 1 ATOM 2643 C CG1 . ILE A 1 342 ? 40.077 10.929 22.103 1.00 17.72 ? 342 ILE A CG1 1 ATOM 2644 C CG2 . ILE A 1 342 ? 38.185 11.024 20.493 1.00 17.12 ? 342 ILE A CG2 1 ATOM 2645 C CD1 . ILE A 1 342 ? 39.592 12.042 23.050 1.00 17.48 ? 342 ILE A CD1 1 ATOM 2646 N N . ASP A 1 343 ? 37.128 7.559 21.470 1.00 17.46 ? 343 ASP A N 1 ATOM 2647 C CA . ASP A 1 343 ? 36.159 6.788 20.703 1.00 17.45 ? 343 ASP A CA 1 ATOM 2648 C C . ASP A 1 343 ? 34.975 6.400 21.609 1.00 18.19 ? 343 ASP A C 1 ATOM 2649 O O . ASP A 1 343 ? 33.826 6.375 21.122 1.00 17.21 ? 343 ASP A O 1 ATOM 2650 C CB . ASP A 1 343 ? 36.821 5.529 20.089 1.00 17.89 ? 343 ASP A CB 1 ATOM 2651 C CG . ASP A 1 343 ? 37.646 5.858 18.870 1.00 18.44 ? 343 ASP A CG 1 ATOM 2652 O OD1 . ASP A 1 343 ? 37.656 7.044 18.390 1.00 17.92 ? 343 ASP A OD1 1 ATOM 2653 O OD2 . ASP A 1 343 ? 38.282 4.884 18.344 1.00 21.28 ? 343 ASP A OD2 1 ATOM 2654 N N . ASP A 1 344 ? 35.215 6.146 22.901 1.00 18.16 ? 344 ASP A N 1 ATOM 2655 C CA . ASP A 1 344 ? 34.127 5.810 23.829 1.00 17.27 ? 344 ASP A CA 1 ATOM 2656 C C . ASP A 1 344 ? 33.230 7.053 24.006 1.00 17.85 ? 344 ASP A C 1 ATOM 2657 O O . ASP A 1 344 ? 31.994 6.957 23.987 1.00 15.85 ? 344 ASP A O 1 ATOM 2658 C CB . ASP A 1 344 ? 34.716 5.377 25.191 1.00 18.58 ? 344 ASP A CB 1 ATOM 2659 C CG . ASP A 1 344 ? 33.632 5.202 26.268 1.00 18.29 ? 344 ASP A CG 1 ATOM 2660 O OD1 . ASP A 1 344 ? 32.801 4.337 26.065 1.00 22.04 ? 344 ASP A OD1 1 ATOM 2661 O OD2 . ASP A 1 344 ? 33.691 5.905 27.268 1.00 21.06 ? 344 ASP A OD2 1 ATOM 2662 N N . ALA A 1 345 ? 33.873 8.210 24.169 1.00 16.55 ? 345 ALA A N 1 ATOM 2663 C CA . ALA A 1 345 ? 33.115 9.469 24.410 1.00 16.02 ? 345 ALA A CA 1 ATOM 2664 C C . ALA A 1 345 ? 32.219 9.728 23.207 1.00 15.71 ? 345 ALA A C 1 ATOM 2665 O O . ALA A 1 345 ? 31.015 10.029 23.368 1.00 16.20 ? 345 ALA A O 1 ATOM 2666 C CB . ALA A 1 345 ? 34.047 10.642 24.648 1.00 15.47 ? 345 ALA A CB 1 ATOM 2667 N N . VAL A 1 346 ? 32.778 9.616 22.002 1.00 15.23 ? 346 VAL A N 1 ATOM 2668 C CA . VAL A 1 346 ? 32.020 9.921 20.805 1.00 15.55 ? 346 VAL A CA 1 ATOM 2669 C C . VAL A 1 346 ? 30.937 8.836 20.562 1.00 15.69 ? 346 VAL A C 1 ATOM 2670 O O . VAL A 1 346 ? 29.815 9.153 20.108 1.00 15.78 ? 346 VAL A O 1 ATOM 2671 C CB . VAL A 1 346 ? 32.999 10.078 19.588 1.00 14.98 ? 346 VAL A CB 1 ATOM 2672 C CG1 . VAL A 1 346 ? 32.190 10.320 18.310 1.00 15.66 ? 346 VAL A CG1 1 ATOM 2673 C CG2 . VAL A 1 346 ? 33.935 11.259 19.824 1.00 16.62 ? 346 VAL A CG2 1 ATOM 2674 N N . THR A 1 347 ? 31.262 7.561 20.834 1.00 16.43 ? 347 THR A N 1 ATOM 2675 C CA . THR A 1 347 ? 30.265 6.519 20.723 1.00 15.92 ? 347 THR A CA 1 ATOM 2676 C C . THR A 1 347 ? 29.015 6.891 21.540 1.00 15.17 ? 347 THR A C 1 ATOM 2677 O O . THR A 1 347 ? 27.911 6.718 21.058 1.00 16.23 ? 347 THR A O 1 ATOM 2678 C CB . THR A 1 347 ? 30.863 5.174 21.188 1.00 17.45 ? 347 THR A CB 1 ATOM 2679 O OG1 . THR A 1 347 ? 31.820 4.746 20.191 1.00 17.66 ? 347 THR A OG1 1 ATOM 2680 C CG2 . THR A 1 347 ? 29.768 4.080 21.328 1.00 18.74 ? 347 THR A CG2 1 ATOM 2681 N N . ARG A 1 348 ? 29.224 7.333 22.771 1.00 14.92 ? 348 ARG A N 1 ATOM 2682 C CA . ARG A 1 348 ? 28.099 7.633 23.695 1.00 14.24 ? 348 ARG A CA 1 ATOM 2683 C C . ARG A 1 348 ? 27.326 8.841 23.205 1.00 14.83 ? 348 ARG A C 1 ATOM 2684 O O . ARG A 1 348 ? 26.074 8.832 23.221 1.00 14.74 ? 348 ARG A O 1 ATOM 2685 C CB . ARG A 1 348 ? 28.655 7.865 25.077 1.00 14.85 ? 348 ARG A CB 1 ATOM 2686 C CG . ARG A 1 348 ? 29.208 6.578 25.749 1.00 14.98 ? 348 ARG A CG 1 ATOM 2687 C CD . ARG A 1 348 ? 30.154 6.853 26.905 1.00 15.00 ? 348 ARG A CD 1 ATOM 2688 N NE . ARG A 1 348 ? 30.476 5.578 27.567 1.00 16.31 ? 348 ARG A NE 1 ATOM 2689 C CZ . ARG A 1 348 ? 29.667 4.969 28.442 1.00 17.52 ? 348 ARG A CZ 1 ATOM 2690 N NH1 . ARG A 1 348 ? 28.499 5.536 28.825 1.00 16.56 ? 348 ARG A NH1 1 ATOM 2691 N NH2 . ARG A 1 348 ? 30.019 3.789 28.934 1.00 19.06 ? 348 ARG A NH2 1 ATOM 2692 N N . ILE A 1 349 ? 28.028 9.887 22.773 1.00 14.01 ? 349 ILE A N 1 ATOM 2693 C CA . ILE A 1 349 ? 27.349 11.093 22.272 1.00 13.71 ? 349 ILE A CA 1 ATOM 2694 C C . ILE A 1 349 ? 26.518 10.767 21.022 1.00 14.30 ? 349 ILE A C 1 ATOM 2695 O O . ILE A 1 349 ? 25.279 11.105 20.897 1.00 14.37 ? 349 ILE A O 1 ATOM 2696 C CB . ILE A 1 349 ? 28.385 12.212 21.950 1.00 13.58 ? 349 ILE A CB 1 ATOM 2697 C CG1 . ILE A 1 349 ? 29.019 12.672 23.278 1.00 13.92 ? 349 ILE A CG1 1 ATOM 2698 C CG2 . ILE A 1 349 ? 27.710 13.388 21.175 1.00 13.69 ? 349 ILE A CG2 1 ATOM 2699 C CD1 . ILE A 1 349 ? 30.348 13.476 23.114 1.00 16.26 ? 349 ILE A CD1 1 ATOM 2700 N N . LEU A 1 350 ? 27.129 10.075 20.075 1.00 14.75 ? 350 LEU A N 1 ATOM 2701 C CA . LEU A 1 350 ? 26.390 9.631 18.885 1.00 14.60 ? 350 LEU A CA 1 ATOM 2702 C C . LEU A 1 350 ? 25.261 8.679 19.225 1.00 14.71 ? 350 LEU A C 1 ATOM 2703 O O . LEU A 1 350 ? 24.172 8.726 18.602 1.00 15.64 ? 350 LEU A O 1 ATOM 2704 C CB . LEU A 1 350 ? 27.344 8.911 17.894 1.00 14.51 ? 350 LEU A CB 1 ATOM 2705 C CG . LEU A 1 350 ? 28.398 9.846 17.299 1.00 14.41 ? 350 LEU A CG 1 ATOM 2706 C CD1 . LEU A 1 350 ? 29.229 9.005 16.307 1.00 15.81 ? 350 LEU A CD1 1 ATOM 2707 C CD2 . LEU A 1 350 ? 27.802 11.051 16.567 1.00 15.59 ? 350 LEU A CD2 1 ATOM 2708 N N . ARG A 1 351 ? 25.467 7.794 20.200 1.00 15.35 ? 351 ARG A N 1 ATOM 2709 C CA . ARG A 1 351 ? 24.378 6.873 20.577 1.00 15.43 ? 351 ARG A CA 1 ATOM 2710 C C . ARG A 1 351 ? 23.141 7.651 21.004 1.00 15.17 ? 351 ARG A C 1 ATOM 2711 O O . ARG A 1 351 ? 22.002 7.319 20.590 1.00 14.64 ? 351 ARG A O 1 ATOM 2712 C CB . ARG A 1 351 ? 24.835 5.935 21.687 1.00 14.95 ? 351 ARG A CB 1 ATOM 2713 C CG . ARG A 1 351 ? 23.718 4.951 22.130 1.00 15.62 ? 351 ARG A CG 1 ATOM 2714 C CD . ARG A 1 351 ? 24.190 4.021 23.255 1.00 16.11 ? 351 ARG A CD 1 ATOM 2715 N NE . ARG A 1 351 ? 25.238 3.087 22.753 1.00 16.47 ? 351 ARG A NE 1 ATOM 2716 C CZ . ARG A 1 351 ? 26.478 2.982 23.228 1.00 17.38 ? 351 ARG A CZ 1 ATOM 2717 N NH1 . ARG A 1 351 ? 26.966 3.663 24.280 1.00 17.91 ? 351 ARG A NH1 1 ATOM 2718 N NH2 . ARG A 1 351 ? 27.290 2.112 22.629 1.00 18.48 ? 351 ARG A NH2 1 ATOM 2719 N N . VAL A 1 352 ? 23.347 8.687 21.821 1.00 14.86 ? 352 VAL A N 1 ATOM 2720 C CA . VAL A 1 352 ? 22.175 9.487 22.287 1.00 14.00 ? 352 VAL A CA 1 ATOM 2721 C C . VAL A 1 352 ? 21.542 10.196 21.106 1.00 13.73 ? 352 VAL A C 1 ATOM 2722 O O . VAL A 1 352 ? 20.292 10.181 20.932 1.00 13.80 ? 352 VAL A O 1 ATOM 2723 C CB . VAL A 1 352 ? 22.608 10.482 23.384 1.00 13.70 ? 352 VAL A CB 1 ATOM 2724 C CG1 . VAL A 1 352 ? 21.496 11.511 23.683 1.00 15.00 ? 352 VAL A CG1 1 ATOM 2725 C CG2 . VAL A 1 352 ? 23.006 9.708 24.640 1.00 14.68 ? 352 VAL A CG2 1 ATOM 2726 N N . LYS A 1 353 ? 22.355 10.804 20.213 1.00 13.22 ? 353 LYS A N 1 ATOM 2727 C CA . LYS A 1 353 ? 21.797 11.529 19.064 1.00 13.23 ? 353 LYS A CA 1 ATOM 2728 C C . LYS A 1 353 ? 21.013 10.631 18.127 1.00 14.32 ? 353 LYS A C 1 ATOM 2729 O O . LYS A 1 353 ? 19.908 10.974 17.701 1.00 14.75 ? 353 LYS A O 1 ATOM 2730 C CB . LYS A 1 353 ? 22.954 12.202 18.271 1.00 13.71 ? 353 LYS A CB 1 ATOM 2731 C CG . LYS A 1 353 ? 23.529 13.412 19.057 1.00 13.12 ? 353 LYS A CG 1 ATOM 2732 C CD . LYS A 1 353 ? 24.598 14.097 18.217 1.00 12.99 ? 353 LYS A CD 1 ATOM 2733 C CE . LYS A 1 353 ? 25.080 15.341 18.969 1.00 12.03 ? 353 LYS A CE 1 ATOM 2734 N NZ . LYS A 1 353 ? 26.060 16.123 18.104 1.00 12.10 ? 353 LYS A NZ 1 ATOM 2735 N N . PHE A 1 354 ? 21.585 9.468 17.789 1.00 14.67 ? 354 PHE A N 1 ATOM 2736 C CA . PHE A 1 354 ? 20.853 8.578 16.892 1.00 14.39 ? 354 PHE A CA 1 ATOM 2737 C C . PHE A 1 354 ? 19.573 8.029 17.553 1.00 14.50 ? 354 PHE A C 1 ATOM 2738 O O . PHE A 1 354 ? 18.520 7.981 16.926 1.00 15.52 ? 354 PHE A O 1 ATOM 2739 C CB . PHE A 1 354 ? 21.743 7.383 16.486 1.00 14.91 ? 354 PHE A CB 1 ATOM 2740 C CG . PHE A 1 354 ? 22.706 7.694 15.360 1.00 14.45 ? 354 PHE A CG 1 ATOM 2741 C CD1 . PHE A 1 354 ? 22.253 8.029 14.064 1.00 14.51 ? 354 PHE A CD1 1 ATOM 2742 C CD2 . PHE A 1 354 ? 24.095 7.616 15.577 1.00 14.29 ? 354 PHE A CD2 1 ATOM 2743 C CE1 . PHE A 1 354 ? 23.177 8.325 13.014 1.00 15.50 ? 354 PHE A CE1 1 ATOM 2744 C CE2 . PHE A 1 354 ? 24.992 7.884 14.528 1.00 14.77 ? 354 PHE A CE2 1 ATOM 2745 C CZ . PHE A 1 354 ? 24.551 8.228 13.267 1.00 14.55 ? 354 PHE A CZ 1 ATOM 2746 N N . THR A 1 355 ? 19.692 7.613 18.818 1.00 15.02 ? 355 THR A N 1 ATOM 2747 C CA . THR A 1 355 ? 18.550 7.003 19.545 1.00 15.50 ? 355 THR A CA 1 ATOM 2748 C C . THR A 1 355 ? 17.369 7.957 19.613 1.00 15.46 ? 355 THR A C 1 ATOM 2749 O O . THR A 1 355 ? 16.226 7.531 19.415 1.00 16.30 ? 355 THR A O 1 ATOM 2750 C CB . THR A 1 355 ? 18.978 6.600 20.970 1.00 16.51 ? 355 THR A CB 1 ATOM 2751 O OG1 . THR A 1 355 ? 20.015 5.597 20.918 1.00 16.84 ? 355 THR A OG1 1 ATOM 2752 C CG2 . THR A 1 355 ? 17.807 6.058 21.819 1.00 18.01 ? 355 THR A CG2 1 ATOM 2753 N N . MET A 1 356 ? 17.644 9.253 19.800 1.00 15.02 ? 356 MET A N 1 ATOM 2754 C CA . MET A 1 356 ? 16.582 10.242 19.967 1.00 15.56 ? 356 MET A CA 1 ATOM 2755 C C . MET A 1 356 ? 15.963 10.708 18.662 1.00 15.14 ? 356 MET A C 1 ATOM 2756 O O . MET A 1 356 ? 14.969 11.455 18.702 1.00 16.25 ? 356 MET A O 1 ATOM 2757 C CB . MET A 1 356 ? 17.062 11.447 20.783 1.00 14.95 ? 356 MET A CB 1 ATOM 2758 C CG . MET A 1 356 ? 18.001 12.392 20.015 1.00 14.84 ? 356 MET A CG 1 ATOM 2759 S SD . MET A 1 356 ? 18.782 13.588 21.125 1.00 15.38 ? 356 MET A SD 1 ATOM 2760 C CE . MET A 1 356 ? 17.346 14.611 21.507 1.00 16.38 ? 356 MET A CE 1 ATOM 2761 N N . GLY A 1 357 ? 16.494 10.270 17.507 1.00 13.93 ? 357 GLY A N 1 ATOM 2762 C CA . GLY A 1 357 ? 15.976 10.671 16.218 1.00 15.10 ? 357 GLY A CA 1 ATOM 2763 C C . GLY A 1 357 ? 16.517 11.953 15.632 1.00 15.62 ? 357 GLY A C 1 ATOM 2764 O O . GLY A 1 357 ? 16.009 12.450 14.635 1.00 15.68 ? 357 GLY A O 1 ATOM 2765 N N . LEU A 1 358 ? 17.615 12.439 16.241 1.00 15.23 ? 358 LEU A N 1 ATOM 2766 C CA . LEU A 1 358 ? 18.137 13.742 15.876 1.00 13.98 ? 358 LEU A CA 1 ATOM 2767 C C . LEU A 1 358 ? 18.649 13.810 14.426 1.00 14.59 ? 358 LEU A C 1 ATOM 2768 O O . LEU A 1 358 ? 18.565 14.834 13.776 1.00 15.16 ? 358 LEU A O 1 ATOM 2769 C CB . LEU A 1 358 ? 19.264 14.151 16.868 1.00 14.11 ? 358 LEU A CB 1 ATOM 2770 C CG . LEU A 1 358 ? 19.719 15.605 16.795 1.00 13.75 ? 358 LEU A CG 1 ATOM 2771 C CD1 . LEU A 1 358 ? 18.632 16.586 17.257 1.00 15.13 ? 358 LEU A CD1 1 ATOM 2772 C CD2 . LEU A 1 358 ? 20.941 15.802 17.703 1.00 14.43 ? 358 LEU A CD2 1 ATOM 2773 N N . PHE A 1 359 ? 19.150 12.664 13.928 1.00 14.09 ? 359 PHE A N 1 ATOM 2774 C CA . PHE A 1 359 ? 19.571 12.659 12.508 1.00 13.90 ? 359 PHE A CA 1 ATOM 2775 C C . PHE A 1 359 ? 18.384 12.706 11.533 1.00 14.86 ? 359 PHE A C 1 ATOM 2776 O O . PHE A 1 359 ? 18.546 13.124 10.381 1.00 16.53 ? 359 PHE A O 1 ATOM 2777 C CB . PHE A 1 359 ? 20.446 11.438 12.179 1.00 14.43 ? 359 PHE A CB 1 ATOM 2778 C CG . PHE A 1 359 ? 21.865 11.526 12.701 1.00 14.49 ? 359 PHE A CG 1 ATOM 2779 C CD1 . PHE A 1 359 ? 22.161 11.379 14.061 1.00 14.74 ? 359 PHE A CD1 1 ATOM 2780 C CD2 . PHE A 1 359 ? 22.900 11.725 11.794 1.00 15.01 ? 359 PHE A CD2 1 ATOM 2781 C CE1 . PHE A 1 359 ? 23.483 11.427 14.514 1.00 14.49 ? 359 PHE A CE1 1 ATOM 2782 C CE2 . PHE A 1 359 ? 24.242 11.779 12.244 1.00 15.62 ? 359 PHE A CE2 1 ATOM 2783 C CZ . PHE A 1 359 ? 24.529 11.647 13.598 1.00 15.95 ? 359 PHE A CZ 1 ATOM 2784 N N . GLU A 1 360 ? 17.213 12.289 12.031 1.00 17.04 ? 360 GLU A N 1 ATOM 2785 C CA . GLU A 1 360 ? 15.998 12.246 11.191 1.00 17.20 ? 360 GLU A CA 1 ATOM 2786 C C . GLU A 1 360 ? 15.209 13.537 11.299 1.00 17.46 ? 360 GLU A C 1 ATOM 2787 O O . GLU A 1 360 ? 14.566 13.959 10.334 1.00 19.39 ? 360 GLU A O 1 ATOM 2788 C CB . GLU A 1 360 ? 15.115 11.039 11.530 1.00 17.52 ? 360 GLU A CB 1 ATOM 2789 C CG . GLU A 1 360 ? 15.577 9.703 10.908 1.00 18.70 ? 360 GLU A CG 1 ATOM 2790 C CD . GLU A 1 360 ? 16.999 9.286 11.321 1.00 17.97 ? 360 GLU A CD 1 ATOM 2791 O OE1 . GLU A 1 360 ? 17.128 8.781 12.423 1.00 19.89 ? 360 GLU A OE1 1 ATOM 2792 O OE2 . GLU A 1 360 ? 17.930 9.424 10.472 1.00 20.36 ? 360 GLU A OE2 1 ATOM 2793 N N . ASN A 1 361 ? 15.311 14.196 12.470 1.00 16.07 ? 361 ASN A N 1 ATOM 2794 C CA . ASN A 1 361 ? 14.602 15.474 12.696 1.00 16.42 ? 361 ASN A CA 1 ATOM 2795 C C . ASN A 1 361 ? 15.525 16.488 13.358 1.00 16.04 ? 361 ASN A C 1 ATOM 2796 O O . ASN A 1 361 ? 15.386 16.807 14.538 1.00 17.11 ? 361 ASN A O 1 ATOM 2797 C CB . ASN A 1 361 ? 13.330 15.258 13.565 1.00 18.08 ? 361 ASN A CB 1 ATOM 2798 C CG . ASN A 1 361 ? 12.193 14.662 12.752 1.00 20.27 ? 361 ASN A CG 1 ATOM 2799 O OD1 . ASN A 1 361 ? 11.488 15.387 12.034 1.00 24.13 ? 361 ASN A OD1 1 ATOM 2800 N ND2 . ASN A 1 361 ? 12.064 13.357 12.800 1.00 21.49 ? 361 ASN A ND2 1 ATOM 2801 N N . PRO A 1 362 ? 16.524 16.960 12.620 1.00 15.21 ? 362 PRO A N 1 ATOM 2802 C CA . PRO A 1 362 ? 17.453 17.930 13.207 1.00 16.05 ? 362 PRO A CA 1 ATOM 2803 C C . PRO A 1 362 ? 16.909 19.336 13.410 1.00 15.09 ? 362 PRO A C 1 ATOM 2804 O O . PRO A 1 362 ? 17.504 20.128 14.167 1.00 14.23 ? 362 PRO A O 1 ATOM 2805 C CB . PRO A 1 362 ? 18.622 17.924 12.222 1.00 17.26 ? 362 PRO A CB 1 ATOM 2806 C CG . PRO A 1 362 ? 18.037 17.457 10.917 1.00 17.78 ? 362 PRO A CG 1 ATOM 2807 C CD . PRO A 1 362 ? 16.915 16.528 11.250 1.00 16.46 ? 362 PRO A CD 1 ATOM 2808 N N . TYR A 1 363 ? 15.800 19.662 12.734 1.00 15.31 ? 363 TYR A N 1 ATOM 2809 C CA . TYR A 1 363 ? 15.267 21.053 12.720 1.00 14.83 ? 363 TYR A CA 1 ATOM 2810 C C . TYR A 1 363 ? 13.977 21.108 13.532 1.00 14.77 ? 363 TYR A C 1 ATOM 2811 O O . TYR A 1 363 ? 13.312 20.086 13.746 1.00 16.70 ? 363 TYR A O 1 ATOM 2812 C CB . TYR A 1 363 ? 15.030 21.543 11.269 1.00 15.23 ? 363 TYR A CB 1 ATOM 2813 C CG . TYR A 1 363 ? 16.315 21.629 10.489 1.00 16.05 ? 363 TYR A CG 1 ATOM 2814 C CD1 . TYR A 1 363 ? 17.233 22.618 10.793 1.00 16.46 ? 363 TYR A CD1 1 ATOM 2815 C CD2 . TYR A 1 363 ? 16.599 20.711 9.478 1.00 17.36 ? 363 TYR A CD2 1 ATOM 2816 C CE1 . TYR A 1 363 ? 18.427 22.728 10.078 1.00 17.28 ? 363 TYR A CE1 1 ATOM 2817 C CE2 . TYR A 1 363 ? 17.797 20.798 8.758 1.00 17.80 ? 363 TYR A CE2 1 ATOM 2818 C CZ . TYR A 1 363 ? 18.683 21.809 9.078 1.00 17.98 ? 363 TYR A CZ 1 ATOM 2819 O OH . TYR A 1 363 ? 19.883 21.941 8.354 1.00 20.66 ? 363 TYR A OH 1 ATOM 2820 N N . ALA A 1 364 ? 13.661 22.328 13.941 1.00 15.18 ? 364 ALA A N 1 ATOM 2821 C CA . ALA A 1 364 ? 12.446 22.565 14.749 1.00 15.10 ? 364 ALA A CA 1 ATOM 2822 C C . ALA A 1 364 ? 11.168 22.374 13.935 1.00 15.55 ? 364 ALA A C 1 ATOM 2823 O O . ALA A 1 364 ? 11.155 22.507 12.673 1.00 15.99 ? 364 ALA A O 1 ATOM 2824 C CB . ALA A 1 364 ? 12.507 23.984 15.248 1.00 16.34 ? 364 ALA A CB 1 ATOM 2825 N N . ASP A 1 365 ? 10.103 22.020 14.670 1.00 15.17 ? 365 ASP A N 1 ATOM 2826 C CA . ASP A 1 365 ? 8.781 21.902 14.034 1.00 15.30 ? 365 ASP A CA 1 ATOM 2827 C C . ASP A 1 365 ? 7.983 23.183 14.296 1.00 15.61 ? 365 ASP A C 1 ATOM 2828 O O . ASP A 1 365 ? 7.554 23.421 15.433 1.00 15.27 ? 365 ASP A O 1 ATOM 2829 C CB . ASP A 1 365 ? 8.072 20.685 14.615 1.00 16.29 ? 365 ASP A CB 1 ATOM 2830 C CG . ASP A 1 365 ? 6.698 20.481 14.018 1.00 18.30 ? 365 ASP A CG 1 ATOM 2831 O OD1 . ASP A 1 365 ? 6.274 21.286 13.169 1.00 19.34 ? 365 ASP A OD1 1 ATOM 2832 O OD2 . ASP A 1 365 ? 6.067 19.509 14.430 1.00 21.47 ? 365 ASP A OD2 1 ATOM 2833 N N . PRO A 1 366 ? 7.775 24.012 13.263 1.00 15.81 ? 366 PRO A N 1 ATOM 2834 C CA . PRO A 1 366 ? 7.018 25.243 13.519 1.00 15.01 ? 366 PRO A CA 1 ATOM 2835 C C . PRO A 1 366 ? 5.623 25.005 14.094 1.00 15.21 ? 366 PRO A C 1 ATOM 2836 O O . PRO A 1 366 ? 5.142 25.906 14.784 1.00 16.99 ? 366 PRO A O 1 ATOM 2837 C CB . PRO A 1 366 ? 6.979 25.961 12.160 1.00 17.81 ? 366 PRO A CB 1 ATOM 2838 C CG . PRO A 1 366 ? 7.247 24.876 11.158 1.00 21.02 ? 366 PRO A CG 1 ATOM 2839 C CD . PRO A 1 366 ? 8.088 23.814 11.825 1.00 16.68 ? 366 PRO A CD 1 ATOM 2840 N N . ALA A 1 367 ? 5.021 23.841 13.842 1.00 15.67 ? 367 ALA A N 1 ATOM 2841 C CA . ALA A 1 367 ? 3.694 23.532 14.424 1.00 17.32 ? 367 ALA A CA 1 ATOM 2842 C C . ALA A 1 367 ? 3.729 23.339 15.933 1.00 18.19 ? 367 ALA A C 1 ATOM 2843 O O . ALA A 1 367 ? 2.676 23.321 16.589 1.00 19.10 ? 367 ALA A O 1 ATOM 2844 C CB . ALA A 1 367 ? 3.104 22.276 13.757 1.00 18.27 ? 367 ALA A CB 1 ATOM 2845 N N . MET A 1 368 ? 4.926 23.232 16.511 1.00 15.32 ? 368 MET A N 1 ATOM 2846 C CA . MET A 1 368 ? 5.039 23.063 17.968 1.00 14.82 ? 368 MET A CA 1 ATOM 2847 C C . MET A 1 368 ? 5.118 24.388 18.718 1.00 15.04 ? 368 MET A C 1 ATOM 2848 O O . MET A 1 368 ? 5.013 24.378 19.959 1.00 14.80 ? 368 MET A O 1 ATOM 2849 C CB . MET A 1 368 ? 6.280 22.240 18.333 1.00 16.02 ? 368 MET A CB 1 ATOM 2850 C CG . MET A 1 368 ? 6.144 20.811 17.852 1.00 18.35 ? 368 MET A CG 1 ATOM 2851 S SD . MET A 1 368 ? 4.990 19.844 18.851 1.00 22.69 ? 368 MET A SD 1 ATOM 2852 C CE . MET A 1 368 ? 6.004 19.467 20.262 1.00 20.82 ? 368 MET A CE 1 ATOM 2853 N N . ALA A 1 369 ? 5.302 25.501 18.008 1.00 14.01 ? 369 ALA A N 1 ATOM 2854 C CA . ALA A 1 369 ? 5.484 26.795 18.678 1.00 15.47 ? 369 ALA A CA 1 ATOM 2855 C C . ALA A 1 369 ? 4.337 27.106 19.618 1.00 16.18 ? 369 ALA A C 1 ATOM 2856 O O . ALA A 1 369 ? 4.591 27.604 20.745 1.00 17.77 ? 369 ALA A O 1 ATOM 2857 C CB . ALA A 1 369 ? 5.705 27.905 17.661 1.00 17.58 ? 369 ALA A CB 1 ATOM 2858 N N . GLU A 1 370 ? 3.116 26.754 19.195 1.00 17.69 ? 370 GLU A N 1 ATOM 2859 C CA . GLU A 1 370 ? 1.893 27.040 19.970 1.00 19.00 ? 370 GLU A CA 1 ATOM 2860 C C . GLU A 1 370 ? 1.757 26.196 21.250 1.00 19.65 ? 370 GLU A C 1 ATOM 2861 O O . GLU A 1 370 ? 0.877 26.485 22.052 1.00 20.28 ? 370 GLU A O 1 ATOM 2862 C CB . GLU A 1 370 ? 0.652 26.896 19.070 1.00 22.34 ? 370 GLU A CB 1 ATOM 2863 C CG . GLU A 1 370 ? 0.591 25.507 18.452 1.00 25.81 ? 370 GLU A CG 1 ATOM 2864 C CD A GLU A 1 370 ? -0.277 25.439 17.181 0.60 27.53 ? 370 GLU A CD 1 ATOM 2865 C CD B GLU A 1 370 ? -0.333 24.543 19.165 0.40 30.18 ? 370 GLU A CD 1 ATOM 2866 O OE1 A GLU A 1 370 ? -1.457 25.124 17.348 0.60 25.22 ? 370 GLU A OE1 1 ATOM 2867 O OE1 B GLU A 1 370 ? 0.174 23.752 19.992 0.40 34.26 ? 370 GLU A OE1 1 ATOM 2868 O OE2 A GLU A 1 370 ? 0.234 25.630 16.030 0.60 28.22 ? 370 GLU A OE2 1 ATOM 2869 O OE2 B GLU A 1 370 ? -1.559 24.561 18.882 0.40 29.37 ? 370 GLU A OE2 1 ATOM 2870 N N . GLN A 1 371 ? 2.641 25.231 21.516 1.00 16.16 ? 371 GLN A N 1 ATOM 2871 C CA . GLN A 1 371 ? 2.620 24.508 22.801 1.00 15.14 ? 371 GLN A CA 1 ATOM 2872 C C . GLN A 1 371 ? 3.095 25.367 23.970 1.00 15.31 ? 371 GLN A C 1 ATOM 2873 O O . GLN A 1 371 ? 2.787 25.063 25.162 1.00 15.39 ? 371 GLN A O 1 ATOM 2874 C CB . GLN A 1 371 ? 3.507 23.260 22.773 1.00 16.60 ? 371 GLN A CB 1 ATOM 2875 C CG . GLN A 1 371 ? 3.088 22.270 21.696 1.00 17.74 ? 371 GLN A CG 1 ATOM 2876 C CD . GLN A 1 371 ? 1.807 21.540 22.046 1.00 20.33 ? 371 GLN A CD 1 ATOM 2877 O OE1 . GLN A 1 371 ? 1.590 21.154 23.188 1.00 20.69 ? 371 GLN A OE1 1 ATOM 2878 N NE2 . GLN A 1 371 ? 0.961 21.354 21.047 1.00 28.58 ? 371 GLN A NE2 1 ATOM 2879 N N . LEU A 1 372 ? 3.844 26.447 23.681 1.00 13.96 ? 372 LEU A N 1 ATOM 2880 C CA . LEU A 1 372 ? 4.422 27.283 24.722 1.00 13.67 ? 372 LEU A CA 1 ATOM 2881 C C . LEU A 1 372 ? 3.281 27.929 25.534 1.00 14.76 ? 372 LEU A C 1 ATOM 2882 O O . LEU A 1 372 ? 2.369 28.586 24.958 1.00 15.32 ? 372 LEU A O 1 ATOM 2883 C CB . LEU A 1 372 ? 5.348 28.339 24.071 1.00 14.00 ? 372 LEU A CB 1 ATOM 2884 C CG . LEU A 1 372 ? 6.164 29.134 25.077 1.00 15.29 ? 372 LEU A CG 1 ATOM 2885 C CD1 . LEU A 1 372 ? 7.299 28.261 25.638 1.00 15.62 ? 372 LEU A CD1 1 ATOM 2886 C CD2 . LEU A 1 372 ? 6.768 30.402 24.440 1.00 16.42 ? 372 LEU A CD2 1 ATOM 2887 N N . GLY A 1 373 ? 3.334 27.776 26.870 1.00 13.55 ? 373 GLY A N 1 ATOM 2888 C CA . GLY A 1 373 ? 2.306 28.409 27.737 1.00 13.30 ? 373 GLY A CA 1 ATOM 2889 C C . GLY A 1 373 ? 0.884 27.908 27.552 1.00 13.09 ? 373 GLY A C 1 ATOM 2890 O O . GLY A 1 373 ? -0.020 28.631 27.938 1.00 13.85 ? 373 GLY A O 1 ATOM 2891 N N . LYS A 1 374 ? 0.671 26.723 26.946 1.00 15.07 ? 374 LYS A N 1 ATOM 2892 C CA . LYS A 1 374 ? -0.693 26.247 26.637 1.00 15.81 ? 374 LYS A CA 1 ATOM 2893 C C . LYS A 1 374 ? -1.532 26.172 27.907 1.00 14.64 ? 374 LYS A C 1 ATOM 2894 O O . LYS A 1 374 ? -1.025 25.777 28.969 1.00 14.07 ? 374 LYS A O 1 ATOM 2895 C CB . LYS A 1 374 ? -0.606 24.781 26.046 1.00 18.90 ? 374 LYS A CB 1 ATOM 2896 C CG . LYS A 1 374 ? -0.771 24.602 24.589 1.00 26.59 ? 374 LYS A CG 1 ATOM 2897 C CD . LYS A 1 374 ? -1.039 23.121 24.279 1.00 26.19 ? 374 LYS A CD 1 ATOM 2898 C CE . LYS A 1 374 ? -0.586 22.046 25.266 1.00 28.87 ? 374 LYS A CE 1 ATOM 2899 N NZ . LYS A 1 374 ? -0.703 20.681 24.582 1.00 33.06 ? 374 LYS A NZ 1 ATOM 2900 N N . GLN A 1 375 ? -2.796 26.520 27.814 1.00 15.22 ? 375 GLN A N 1 ATOM 2901 C CA . GLN A 1 375 ? -3.649 26.517 28.960 1.00 14.77 ? 375 GLN A CA 1 ATOM 2902 C C . GLN A 1 375 ? -3.689 25.141 29.650 1.00 14.56 ? 375 GLN A C 1 ATOM 2903 O O . GLN A 1 375 ? -3.733 25.100 30.891 1.00 14.38 ? 375 GLN A O 1 ATOM 2904 C CB . GLN A 1 375 ? -5.070 26.982 28.566 1.00 17.00 ? 375 GLN A CB 1 ATOM 2905 C CG . GLN A 1 375 ? -5.971 27.234 29.783 1.00 17.82 ? 375 GLN A CG 1 ATOM 2906 C CD . GLN A 1 375 ? -5.377 28.285 30.725 1.00 21.80 ? 375 GLN A CD 1 ATOM 2907 O OE1 . GLN A 1 375 ? -4.969 29.361 30.314 1.00 25.12 ? 375 GLN A OE1 1 ATOM 2908 N NE2 . GLN A 1 375 ? -5.265 27.939 31.999 1.00 19.03 ? 375 GLN A NE2 1 ATOM 2909 N N . GLU A 1 376 ? -3.666 24.031 28.917 1.00 15.22 ? 376 GLU A N 1 ATOM 2910 C CA . GLU A 1 376 ? -3.724 22.714 29.571 1.00 16.19 ? 376 GLU A CA 1 ATOM 2911 C C . GLU A 1 376 ? -2.503 22.524 30.494 1.00 14.95 ? 376 GLU A C 1 ATOM 2912 O O . GLU A 1 376 ? -2.591 21.896 31.586 1.00 15.73 ? 376 GLU A O 1 ATOM 2913 C CB . GLU A 1 376 ? -3.726 21.632 28.499 1.00 17.89 ? 376 GLU A CB 1 ATOM 2914 C CG . GLU A 1 376 ? -4.957 21.729 27.577 1.00 23.82 ? 376 GLU A CG 1 ATOM 2915 C CD . GLU A 1 376 ? -4.830 22.609 26.313 1.00 25.47 ? 376 GLU A CD 1 ATOM 2916 O OE1 . GLU A 1 376 ? -4.066 23.599 26.236 1.00 19.64 ? 376 GLU A OE1 1 ATOM 2917 O OE2 . GLU A 1 376 ? -5.578 22.313 25.301 1.00 33.56 ? 376 GLU A OE2 1 ATOM 2918 N N . HIS A 1 377 ? -1.353 23.087 30.105 1.00 13.82 ? 377 HIS A N 1 ATOM 2919 C CA . HIS A 1 377 ? -0.168 22.972 30.920 1.00 12.62 ? 377 HIS A CA 1 ATOM 2920 C C . HIS A 1 377 ? -0.215 23.933 32.115 1.00 12.52 ? 377 HIS A C 1 ATOM 2921 O O . HIS A 1 377 ? 0.263 23.599 33.186 1.00 12.34 ? 377 HIS A O 1 ATOM 2922 C CB . HIS A 1 377 ? 1.102 23.330 30.122 1.00 13.42 ? 377 HIS A CB 1 ATOM 2923 C CG . HIS A 1 377 ? 1.393 22.427 28.957 1.00 14.90 ? 377 HIS A CG 1 ATOM 2924 N ND1 . HIS A 1 377 ? 0.735 21.242 28.661 1.00 18.72 ? 377 HIS A ND1 1 ATOM 2925 C CD2 . HIS A 1 377 ? 2.297 22.615 27.980 1.00 12.53 ? 377 HIS A CD2 1 ATOM 2926 C CE1 . HIS A 1 377 ? 1.269 20.712 27.556 1.00 16.10 ? 377 HIS A CE1 1 ATOM 2927 N NE2 . HIS A 1 377 ? 2.206 21.538 27.111 1.00 18.63 ? 377 HIS A NE2 1 ATOM 2928 N N . ARG A 1 378 ? -0.850 25.090 31.935 1.00 12.59 ? 378 ARG A N 1 ATOM 2929 C CA . ARG A 1 378 ? -1.072 25.983 33.069 1.00 13.11 ? 378 ARG A CA 1 ATOM 2930 C C . ARG A 1 378 ? -2.061 25.342 34.065 1.00 13.14 ? 378 ARG A C 1 ATOM 2931 O O . ARG A 1 378 ? -1.854 25.493 35.287 1.00 13.79 ? 378 ARG A O 1 ATOM 2932 C CB . ARG A 1 378 ? -1.544 27.350 32.564 1.00 12.19 ? 378 ARG A CB 1 ATOM 2933 C CG . ARG A 1 378 ? -0.511 28.064 31.746 1.00 12.74 ? 378 ARG A CG 1 ATOM 2934 C CD . ARG A 1 378 ? -0.983 29.491 31.482 1.00 12.86 ? 378 ARG A CD 1 ATOM 2935 N NE . ARG A 1 378 ? -0.066 30.142 30.517 1.00 13.51 ? 378 ARG A NE 1 ATOM 2936 C CZ . ARG A 1 378 ? 1.038 30.787 30.872 1.00 13.42 ? 378 ARG A CZ 1 ATOM 2937 N NH1 . ARG A 1 378 ? 1.424 30.897 32.156 1.00 14.26 ? 378 ARG A NH1 1 ATOM 2938 N NH2 . ARG A 1 378 ? 1.802 31.339 29.907 1.00 14.47 ? 378 ARG A NH2 1 ATOM 2939 N N . ASP A 1 379 ? -3.091 24.664 33.563 1.00 13.47 ? 379 ASP A N 1 ATOM 2940 C CA . ASP A 1 379 ? -4.004 23.925 34.461 1.00 13.95 ? 379 ASP A CA 1 ATOM 2941 C C . ASP A 1 379 ? -3.231 22.837 35.263 1.00 13.17 ? 379 ASP A C 1 ATOM 2942 O O . ASP A 1 379 ? -3.464 22.678 36.465 1.00 13.68 ? 379 ASP A O 1 ATOM 2943 C CB . ASP A 1 379 ? -5.099 23.262 33.666 1.00 15.21 ? 379 ASP A CB 1 ATOM 2944 C CG . ASP A 1 379 ? -6.093 24.271 33.040 1.00 17.17 ? 379 ASP A CG 1 ATOM 2945 O OD1 . ASP A 1 379 ? -6.057 25.435 33.393 1.00 19.34 ? 379 ASP A OD1 1 ATOM 2946 O OD2 . ASP A 1 379 ? -6.871 23.806 32.169 1.00 21.53 ? 379 ASP A OD2 1 ATOM 2947 N N . LEU A 1 380 ? -2.265 22.168 34.636 1.00 12.41 ? 380 LEU A N 1 ATOM 2948 C CA . LEU A 1 380 ? -1.430 21.183 35.323 1.00 12.39 ? 380 LEU A CA 1 ATOM 2949 C C . LEU A 1 380 ? -0.565 21.887 36.383 1.00 13.23 ? 380 LEU A C 1 ATOM 2950 O O . LEU A 1 380 ? -0.440 21.393 37.522 1.00 12.96 ? 380 LEU A O 1 ATOM 2951 C CB . LEU A 1 380 ? -0.587 20.435 34.269 1.00 13.66 ? 380 LEU A CB 1 ATOM 2952 C CG . LEU A 1 380 ? 0.454 19.485 34.839 1.00 13.73 ? 380 LEU A CG 1 ATOM 2953 C CD1 . LEU A 1 380 ? -0.236 18.318 35.571 1.00 16.44 ? 380 LEU A CD1 1 ATOM 2954 C CD2 . LEU A 1 380 ? 1.347 18.949 33.721 1.00 14.16 ? 380 LEU A CD2 1 ATOM 2955 N N . ALA A 1 381 ? 0.057 23.016 36.019 1.00 12.49 ? 381 ALA A N 1 ATOM 2956 C CA . ALA A 1 381 ? 0.907 23.728 36.984 1.00 12.48 ? 381 ALA A CA 1 ATOM 2957 C C . ALA A 1 381 ? 0.096 24.221 38.162 1.00 12.12 ? 381 ALA A C 1 ATOM 2958 O O . ALA A 1 381 ? 0.590 24.211 39.299 1.00 12.35 ? 381 ALA A O 1 ATOM 2959 C CB . ALA A 1 381 ? 1.600 24.914 36.271 1.00 11.85 ? 381 ALA A CB 1 ATOM 2960 N N . ARG A 1 382 ? -1.152 24.644 37.901 1.00 12.63 ? 382 ARG A N 1 ATOM 2961 C CA . ARG A 1 382 ? -2.109 25.094 38.960 1.00 12.64 ? 382 ARG A CA 1 ATOM 2962 C C . ARG A 1 382 ? -2.419 23.917 39.907 1.00 13.20 ? 382 ARG A C 1 ATOM 2963 O O . ARG A 1 382 ? -2.419 24.104 41.127 1.00 13.53 ? 382 ARG A O 1 ATOM 2964 C CB . ARG A 1 382 ? -3.342 25.655 38.253 1.00 13.05 ? 382 ARG A CB 1 ATOM 2965 C CG . ARG A 1 382 ? -4.459 26.082 39.200 1.00 13.28 ? 382 ARG A CG 1 ATOM 2966 C CD . ARG A 1 382 ? -5.559 26.669 38.336 1.00 13.80 ? 382 ARG A CD 1 ATOM 2967 N NE . ARG A 1 382 ? -6.700 27.002 39.167 1.00 14.01 ? 382 ARG A NE 1 ATOM 2968 C CZ . ARG A 1 382 ? -7.769 27.623 38.706 1.00 15.79 ? 382 ARG A CZ 1 ATOM 2969 N NH1 . ARG A 1 382 ? -7.805 28.027 37.437 1.00 18.31 ? 382 ARG A NH1 1 ATOM 2970 N NH2 . ARG A 1 382 ? -8.794 27.901 39.522 1.00 17.14 ? 382 ARG A NH2 1 ATOM 2971 N N . GLU A 1 383 ? -2.692 22.746 39.343 1.00 12.61 ? 383 GLU A N 1 ATOM 2972 C CA . GLU A 1 383 ? -2.896 21.522 40.136 1.00 12.87 ? 383 GLU A CA 1 ATOM 2973 C C . GLU A 1 383 ? -1.676 21.251 41.007 1.00 12.95 ? 383 GLU A C 1 ATOM 2974 O O . GLU A 1 383 ? -1.802 20.999 42.221 1.00 13.66 ? 383 GLU A O 1 ATOM 2975 C CB . GLU A 1 383 ? -3.207 20.345 39.175 1.00 13.63 ? 383 GLU A CB 1 ATOM 2976 C CG . GLU A 1 383 ? -3.300 19.012 39.892 1.00 15.98 ? 383 GLU A CG 1 ATOM 2977 C CD . GLU A 1 383 ? -3.355 17.822 38.934 1.00 19.14 ? 383 GLU A CD 1 ATOM 2978 O OE1 . GLU A 1 383 ? -3.477 17.980 37.680 1.00 21.97 ? 383 GLU A OE1 1 ATOM 2979 O OE2 . GLU A 1 383 ? -3.225 16.706 39.436 1.00 19.42 ? 383 GLU A OE2 1 ATOM 2980 N N . ALA A 1 384 ? -0.489 21.324 40.391 1.00 13.16 ? 384 ALA A N 1 ATOM 2981 C CA . ALA A 1 384 ? 0.745 20.992 41.124 1.00 13.26 ? 384 ALA A CA 1 ATOM 2982 C C . ALA A 1 384 ? 0.999 22.008 42.244 1.00 12.65 ? 384 ALA A C 1 ATOM 2983 O O . ALA A 1 384 ? 1.396 21.643 43.377 1.00 13.19 ? 384 ALA A O 1 ATOM 2984 C CB . ALA A 1 384 ? 1.956 20.970 40.159 1.00 14.54 ? 384 ALA A CB 1 ATOM 2985 N N . ALA A 1 385 ? 0.781 23.299 41.941 1.00 11.86 ? 385 ALA A N 1 ATOM 2986 C CA . ALA A 1 385 ? 0.982 24.334 42.956 1.00 12.43 ? 385 ALA A CA 1 ATOM 2987 C C . ALA A 1 385 ? 0.052 24.072 44.158 1.00 12.48 ? 385 ALA A C 1 ATOM 2988 O O . ALA A 1 385 ? 0.492 24.099 45.314 1.00 12.57 ? 385 ALA A O 1 ATOM 2989 C CB . ALA A 1 385 ? 0.752 25.735 42.364 1.00 13.56 ? 385 ALA A CB 1 ATOM 2990 N N . ARG A 1 386 ? -1.228 23.806 43.891 1.00 12.11 ? 386 ARG A N 1 ATOM 2991 C CA . ARG A 1 386 ? -2.182 23.559 44.990 1.00 12.69 ? 386 ARG A CA 1 ATOM 2992 C C . ARG A 1 386 ? -1.781 22.309 45.808 1.00 12.58 ? 386 ARG A C 1 ATOM 2993 O O . ARG A 1 386 ? -1.843 22.340 47.055 1.00 13.97 ? 386 ARG A O 1 ATOM 2994 C CB . ARG A 1 386 ? -3.559 23.367 44.369 1.00 13.64 ? 386 ARG A CB 1 ATOM 2995 C CG . ARG A 1 386 ? -4.680 23.022 45.395 1.00 15.49 ? 386 ARG A CG 1 ATOM 2996 C CD . ARG A 1 386 ? -5.104 21.531 45.304 1.00 19.04 ? 386 ARG A CD 1 ATOM 2997 N NE . ARG A 1 386 ? -5.571 21.108 43.989 1.00 21.38 ? 386 ARG A NE 1 ATOM 2998 C CZ . ARG A 1 386 ? -5.895 19.863 43.661 1.00 24.11 ? 386 ARG A CZ 1 ATOM 2999 N NH1 . ARG A 1 386 ? -5.784 18.891 44.546 1.00 24.14 ? 386 ARG A NH1 1 ATOM 3000 N NH2 . ARG A 1 386 ? -6.300 19.626 42.439 1.00 28.60 ? 386 ARG A NH2 1 ATOM 3001 N N . LYS A 1 387 ? -1.333 21.237 45.139 1.00 12.73 ? 387 LYS A N 1 ATOM 3002 C CA . LYS A 1 387 ? -0.930 20.015 45.841 1.00 13.40 ? 387 LYS A CA 1 ATOM 3003 C C . LYS A 1 387 ? 0.354 20.177 46.625 1.00 13.61 ? 387 LYS A C 1 ATOM 3004 O O . LYS A 1 387 ? 0.633 19.425 47.581 1.00 14.42 ? 387 LYS A O 1 ATOM 3005 C CB . LYS A 1 387 ? -0.792 18.867 44.816 1.00 13.51 ? 387 LYS A CB 1 ATOM 3006 C CG . LYS A 1 387 ? -2.162 18.373 44.310 1.00 14.04 ? 387 LYS A CG 1 ATOM 3007 C CD . LYS A 1 387 ? -2.007 17.291 43.248 1.00 16.16 ? 387 LYS A CD 1 ATOM 3008 C CE . LYS A 1 387 ? -3.369 16.687 42.943 1.00 18.03 ? 387 LYS A CE 1 ATOM 3009 N NZ . LYS A 1 387 ? -3.139 15.533 42.027 1.00 20.66 ? 387 LYS A NZ 1 ATOM 3010 N N . SER A 1 388 ? 1.176 21.155 46.245 1.00 13.17 ? 388 SER A N 1 ATOM 3011 C CA . SER A 1 388 ? 2.450 21.353 46.909 1.00 12.87 ? 388 SER A CA 1 ATOM 3012 C C . SER A 1 388 ? 2.298 22.104 48.232 1.00 12.58 ? 388 SER A C 1 ATOM 3013 O O . SER A 1 388 ? 3.253 22.112 49.042 1.00 13.14 ? 388 SER A O 1 ATOM 3014 C CB . SER A 1 388 ? 3.365 22.171 45.981 1.00 12.96 ? 388 SER A CB 1 ATOM 3015 O OG . SER A 1 388 ? 3.054 23.581 45.945 1.00 13.21 ? 388 SER A OG 1 ATOM 3016 N N . LEU A 1 389 ? 1.153 22.774 48.449 1.00 13.47 ? 389 LEU A N 1 ATOM 3017 C CA . LEU A 1 389 ? 1.026 23.667 49.634 1.00 13.30 ? 389 LEU A CA 1 ATOM 3018 C C . LEU A 1 389 ? 0.965 22.814 50.918 1.00 13.48 ? 389 LEU A C 1 ATOM 3019 O O . LEU A 1 389 ? 0.265 21.810 50.965 1.00 15.21 ? 389 LEU A O 1 ATOM 3020 C CB . LEU A 1 389 ? -0.296 24.460 49.521 1.00 13.35 ? 389 LEU A CB 1 ATOM 3021 C CG . LEU A 1 389 ? -0.537 25.226 48.218 1.00 13.53 ? 389 LEU A CG 1 ATOM 3022 C CD1 . LEU A 1 389 ? -1.892 25.898 48.346 1.00 13.70 ? 389 LEU A CD1 1 ATOM 3023 C CD2 . LEU A 1 389 ? 0.565 26.271 47.925 1.00 14.02 ? 389 LEU A CD2 1 ATOM 3024 N N . VAL A 1 390 ? 1.692 23.250 51.937 1.00 13.46 ? 390 VAL A N 1 ATOM 3025 C CA . VAL A 1 390 ? 1.643 22.521 53.229 1.00 13.81 ? 390 VAL A CA 1 ATOM 3026 C C . VAL A 1 390 ? 1.042 23.467 54.247 1.00 14.05 ? 390 VAL A C 1 ATOM 3027 O O . VAL A 1 390 ? 1.618 24.513 54.554 1.00 15.18 ? 390 VAL A O 1 ATOM 3028 C CB . VAL A 1 390 ? 3.036 22.051 53.650 1.00 13.51 ? 390 VAL A CB 1 ATOM 3029 C CG1 . VAL A 1 390 ? 2.933 21.361 55.037 1.00 15.06 ? 390 VAL A CG1 1 ATOM 3030 C CG2 . VAL A 1 390 ? 3.606 21.064 52.606 1.00 14.46 ? 390 VAL A CG2 1 ATOM 3031 N N . LEU A 1 391 ? -0.113 23.095 54.782 1.00 13.76 ? 391 LEU A N 1 ATOM 3032 C CA . LEU A 1 391 ? -0.784 23.879 55.829 1.00 14.07 ? 391 LEU A CA 1 ATOM 3033 C C . LEU A 1 391 ? -0.116 23.592 57.159 1.00 14.88 ? 391 LEU A C 1 ATOM 3034 O O . LEU A 1 391 ? -0.152 22.441 57.655 1.00 15.22 ? 391 LEU A O 1 ATOM 3035 C CB . LEU A 1 391 ? -2.250 23.498 55.836 1.00 14.68 ? 391 LEU A CB 1 ATOM 3036 C CG . LEU A 1 391 ? -3.170 24.255 56.826 1.00 13.40 ? 391 LEU A CG 1 ATOM 3037 C CD1 . LEU A 1 391 ? -3.127 25.785 56.542 1.00 14.87 ? 391 LEU A CD1 1 ATOM 3038 C CD2 . LEU A 1 391 ? -4.571 23.684 56.672 1.00 14.73 ? 391 LEU A CD2 1 ATOM 3039 N N . LEU A 1 392 ? 0.517 24.616 57.720 1.00 14.48 ? 392 LEU A N 1 ATOM 3040 C CA . LEU A 1 392 ? 1.282 24.477 58.987 1.00 14.94 ? 392 LEU A CA 1 ATOM 3041 C C . LEU A 1 392 ? 0.460 24.828 60.204 1.00 15.84 ? 392 LEU A C 1 ATOM 3042 O O . LEU A 1 392 ? 0.802 24.371 61.329 1.00 18.32 ? 392 LEU A O 1 ATOM 3043 C CB . LEU A 1 392 ? 2.596 25.256 58.990 1.00 15.37 ? 392 LEU A CB 1 ATOM 3044 C CG . LEU A 1 392 ? 3.626 24.825 57.904 1.00 16.60 ? 392 LEU A CG 1 ATOM 3045 C CD1 . LEU A 1 392 ? 4.818 25.752 57.999 1.00 17.83 ? 392 LEU A CD1 1 ATOM 3046 C CD2 . LEU A 1 392 ? 4.036 23.340 58.097 1.00 19.38 ? 392 LEU A CD2 1 ATOM 3047 N N . LYS A 1 393 ? -0.535 25.710 60.045 1.00 14.92 ? 393 LYS A N 1 ATOM 3048 C CA . LYS A 1 393 ? -1.332 26.193 61.196 1.00 15.88 ? 393 LYS A CA 1 ATOM 3049 C C . LYS A 1 393 ? -2.690 26.620 60.609 1.00 15.19 ? 393 LYS A C 1 ATOM 3050 O O . LYS A 1 393 ? -2.767 27.196 59.484 1.00 15.33 ? 393 LYS A O 1 ATOM 3051 C CB . LYS A 1 393 ? -0.603 27.374 61.859 1.00 16.18 ? 393 LYS A CB 1 ATOM 3052 C CG . LYS A 1 393 ? -1.356 27.963 63.064 1.00 16.55 ? 393 LYS A CG 1 ATOM 3053 C CD . LYS A 1 393 ? -0.520 29.061 63.677 1.00 17.88 ? 393 LYS A CD 1 ATOM 3054 C CE . LYS A 1 393 ? -1.244 29.624 64.903 1.00 17.71 ? 393 LYS A CE 1 ATOM 3055 N NZ . LYS A 1 393 ? -0.387 30.683 65.547 1.00 19.42 ? 393 LYS A NZ 1 ATOM 3056 N N . ASN A 1 394 ? -3.772 26.371 61.344 1.00 17.20 ? 394 ASN A N 1 ATOM 3057 C CA . ASN A 1 394 ? -5.096 26.800 60.920 1.00 16.64 ? 394 ASN A CA 1 ATOM 3058 C C . ASN A 1 394 ? -5.942 27.063 62.146 1.00 20.31 ? 394 ASN A C 1 ATOM 3059 O O . ASN A 1 394 ? -6.855 26.280 62.419 1.00 23.29 ? 394 ASN A O 1 ATOM 3060 C CB . ASN A 1 394 ? -5.750 25.722 60.045 1.00 17.68 ? 394 ASN A CB 1 ATOM 3061 C CG . ASN A 1 394 ? -6.986 26.210 59.292 1.00 16.39 ? 394 ASN A CG 1 ATOM 3062 O OD1 . ASN A 1 394 ? -7.832 25.400 58.829 1.00 18.74 ? 394 ASN A OD1 1 ATOM 3063 N ND2 . ASN A 1 394 ? -7.100 27.489 59.156 1.00 15.92 ? 394 ASN A ND2 1 ATOM 3064 N N . GLY A 1 395 ? -5.511 28.066 62.907 1.00 19.34 ? 395 GLY A N 1 ATOM 3065 C CA . GLY A 1 395 ? -6.188 28.549 64.145 1.00 20.08 ? 395 GLY A CA 1 ATOM 3066 C C . GLY A 1 395 ? -5.139 28.720 65.249 1.00 20.27 ? 395 GLY A C 1 ATOM 3067 O O . GLY A 1 395 ? -4.260 27.874 65.431 1.00 20.71 ? 395 GLY A O 1 ATOM 3068 N N . LYS A 1 396 ? -5.257 29.807 66.013 1.00 22.42 ? 396 LYS A N 1 ATOM 3069 C CA . LYS A 1 396 ? -4.240 30.096 67.078 1.00 22.22 ? 396 LYS A CA 1 ATOM 3070 C C . LYS A 1 396 ? -4.370 29.250 68.323 1.00 25.82 ? 396 LYS A C 1 ATOM 3071 O O . LYS A 1 396 ? -3.400 29.067 69.075 1.00 27.41 ? 396 LYS A O 1 ATOM 3072 C CB . LYS A 1 396 ? -4.320 31.542 67.466 1.00 26.40 ? 396 LYS A CB 1 ATOM 3073 C CG . LYS A 1 396 ? -3.833 32.460 66.374 1.00 28.12 ? 396 LYS A CG 1 ATOM 3074 C CD . LYS A 1 396 ? -3.578 33.838 66.924 1.00 28.68 ? 396 LYS A CD 1 ATOM 3075 C CE . LYS A 1 396 ? -3.217 34.760 65.771 1.00 29.24 ? 396 LYS A CE 1 ATOM 3076 N NZ . LYS A 1 396 ? -3.452 36.191 66.115 1.00 30.63 ? 396 LYS A NZ 1 ATOM 3077 N N . THR A 1 397 ? -5.573 28.765 68.596 1.00 22.01 ? 397 THR A N 1 ATOM 3078 C CA . THR A 1 397 ? -5.766 27.888 69.722 1.00 22.90 ? 397 THR A CA 1 ATOM 3079 C C . THR A 1 397 ? -6.564 26.688 69.274 1.00 23.56 ? 397 THR A C 1 ATOM 3080 O O . THR A 1 397 ? -7.210 26.722 68.213 1.00 24.06 ? 397 THR A O 1 ATOM 3081 C CB . THR A 1 397 ? -6.497 28.563 70.917 1.00 22.34 ? 397 THR A CB 1 ATOM 3082 O OG1 . THR A 1 397 ? -7.916 28.553 70.674 1.00 22.40 ? 397 THR A OG1 1 ATOM 3083 C CG2 . THR A 1 397 ? -6.063 30.039 71.096 1.00 21.81 ? 397 THR A CG2 1 ATOM 3084 N N . SER A 1 398 ? -6.586 25.666 70.118 1.00 26.29 ? 398 SER A N 1 ATOM 3085 C CA . SER A 1 398 ? -7.243 24.423 69.766 1.00 27.82 ? 398 SER A CA 1 ATOM 3086 C C . SER A 1 398 ? -8.765 24.640 69.754 1.00 27.24 ? 398 SER A C 1 ATOM 3087 O O . SER A 1 398 ? -9.507 23.774 69.284 1.00 29.91 ? 398 SER A O 1 ATOM 3088 C CB . SER A 1 398 ? -6.878 23.355 70.790 1.00 28.93 ? 398 SER A CB 1 ATOM 3089 O OG . SER A 1 398 ? -7.413 23.669 72.072 1.00 32.22 ? 398 SER A OG 1 ATOM 3090 N N . THR A 1 399 ? -9.228 25.800 70.229 1.00 22.87 ? 399 THR A N 1 ATOM 3091 C CA . THR A 1 399 ? -10.651 26.053 70.353 1.00 22.66 ? 399 THR A CA 1 ATOM 3092 C C . THR A 1 399 ? -11.152 27.139 69.352 1.00 20.47 ? 399 THR A C 1 ATOM 3093 O O . THR A 1 399 ? -12.359 27.430 69.281 1.00 19.61 ? 399 THR A O 1 ATOM 3094 C CB . THR A 1 399 ? -10.779 26.371 71.853 1.00 25.75 ? 399 THR A CB 1 ATOM 3095 O OG1 A THR A 1 399 ? -11.177 25.234 72.651 0.60 26.16 ? 399 THR A OG1 1 ATOM 3096 O OG1 B THR A 1 399 ? -12.167 26.334 72.204 0.40 27.82 ? 399 THR A OG1 1 ATOM 3097 C CG2 A THR A 1 399 ? -11.128 27.762 72.245 0.60 24.45 ? 399 THR A CG2 1 ATOM 3098 C CG2 B THR A 1 399 ? -10.293 27.721 72.164 0.40 19.27 ? 399 THR A CG2 1 ATOM 3099 N N . ASP A 1 400 ? -10.245 27.739 68.588 1.00 17.94 ? 400 ASP A N 1 ATOM 3100 C CA . ASP A 1 400 ? -10.652 28.764 67.616 1.00 16.25 ? 400 ASP A CA 1 ATOM 3101 C C . ASP A 1 400 ? -11.328 28.147 66.395 1.00 17.04 ? 400 ASP A C 1 ATOM 3102 O O . ASP A 1 400 ? -11.079 26.997 66.048 1.00 18.04 ? 400 ASP A O 1 ATOM 3103 C CB . ASP A 1 400 ? -9.421 29.536 67.094 1.00 17.52 ? 400 ASP A CB 1 ATOM 3104 C CG . ASP A 1 400 ? -8.909 30.579 68.081 1.00 17.99 ? 400 ASP A CG 1 ATOM 3105 O OD1 . ASP A 1 400 ? -9.300 30.611 69.277 1.00 18.04 ? 400 ASP A OD1 1 ATOM 3106 O OD2 . ASP A 1 400 ? -8.112 31.433 67.622 1.00 19.28 ? 400 ASP A OD2 1 ATOM 3107 N N . ALA A 1 401 ? -12.189 28.921 65.739 1.00 15.28 ? 401 ALA A N 1 ATOM 3108 C CA . ALA A 1 401 ? -12.717 28.536 64.423 1.00 15.35 ? 401 ALA A CA 1 ATOM 3109 C C . ALA A 1 401 ? -11.537 28.359 63.456 1.00 16.52 ? 401 ALA A C 1 ATOM 3110 O O . ALA A 1 401 ? -10.641 29.173 63.472 1.00 17.90 ? 401 ALA A O 1 ATOM 3111 C CB . ALA A 1 401 ? -13.610 29.633 63.909 1.00 15.84 ? 401 ALA A CB 1 ATOM 3112 N N . PRO A 1 402 ? -11.564 27.307 62.637 1.00 17.78 ? 402 PRO A N 1 ATOM 3113 C CA . PRO A 1 402 ? -10.488 27.203 61.615 1.00 19.74 ? 402 PRO A CA 1 ATOM 3114 C C . PRO A 1 402 ? -10.656 28.386 60.647 1.00 18.33 ? 402 PRO A C 1 ATOM 3115 O O . PRO A 1 402 ? -11.770 28.625 60.188 1.00 19.36 ? 402 PRO A O 1 ATOM 3116 C CB . PRO A 1 402 ? -10.786 25.872 60.935 1.00 21.83 ? 402 PRO A CB 1 ATOM 3117 C CG . PRO A 1 402 ? -12.261 25.594 61.168 1.00 22.75 ? 402 PRO A CG 1 ATOM 3118 C CD . PRO A 1 402 ? -12.609 26.254 62.502 1.00 20.69 ? 402 PRO A CD 1 ATOM 3119 N N . LEU A 1 403 ? -9.571 29.079 60.287 1.00 15.75 ? 403 LEU A N 1 ATOM 3120 C CA . LEU A 1 403 ? -9.674 30.225 59.386 1.00 15.99 ? 403 LEU A CA 1 ATOM 3121 C C . LEU A 1 403 ? -9.873 29.704 57.955 1.00 14.88 ? 403 LEU A C 1 ATOM 3122 O O . LEU A 1 403 ? -10.661 30.285 57.224 1.00 14.47 ? 403 LEU A O 1 ATOM 3123 C CB . LEU A 1 403 ? -8.398 31.121 59.441 1.00 19.05 ? 403 LEU A CB 1 ATOM 3124 C CG . LEU A 1 403 ? -8.456 32.302 58.422 1.00 19.78 ? 403 LEU A CG 1 ATOM 3125 C CD1 . LEU A 1 403 ? -9.642 33.259 58.644 1.00 21.56 ? 403 LEU A CD1 1 ATOM 3126 C CD2 . LEU A 1 403 ? -7.195 33.134 58.457 1.00 21.58 ? 403 LEU A CD2 1 ATOM 3127 N N . LEU A 1 404 ? -9.122 28.667 57.537 1.00 13.45 ? 404 LEU A N 1 ATOM 3128 C CA . LEU A 1 404 ? -9.239 28.162 56.173 1.00 14.02 ? 404 LEU A CA 1 ATOM 3129 C C . LEU A 1 404 ? -10.180 26.928 56.130 1.00 14.73 ? 404 LEU A C 1 ATOM 3130 O O . LEU A 1 404 ? -10.150 26.123 57.061 1.00 16.03 ? 404 LEU A O 1 ATOM 3131 C CB . LEU A 1 404 ? -7.861 27.736 55.609 1.00 14.45 ? 404 LEU A CB 1 ATOM 3132 C CG . LEU A 1 404 ? -6.854 28.881 55.622 1.00 13.86 ? 404 LEU A CG 1 ATOM 3133 C CD1 . LEU A 1 404 ? -5.478 28.392 55.112 1.00 14.73 ? 404 LEU A CD1 1 ATOM 3134 C CD2 . LEU A 1 404 ? -7.285 30.116 54.812 1.00 15.32 ? 404 LEU A CD2 1 ATOM 3135 N N . PRO A 1 405 ? -11.007 26.785 55.103 1.00 15.57 ? 405 PRO A N 1 ATOM 3136 C CA . PRO A 1 405 ? -11.124 27.674 53.942 1.00 15.83 ? 405 PRO A CA 1 ATOM 3137 C C . PRO A 1 405 ? -11.849 28.991 54.206 1.00 14.54 ? 405 PRO A C 1 ATOM 3138 O O . PRO A 1 405 ? -12.779 29.069 55.016 1.00 16.11 ? 405 PRO A O 1 ATOM 3139 C CB . PRO A 1 405 ? -11.865 26.802 52.925 1.00 16.97 ? 405 PRO A CB 1 ATOM 3140 C CG . PRO A 1 405 ? -12.779 25.936 53.774 1.00 20.45 ? 405 PRO A CG 1 ATOM 3141 C CD . PRO A 1 405 ? -11.935 25.636 55.001 1.00 18.42 ? 405 PRO A CD 1 ATOM 3142 N N . LEU A 1 406 ? -11.426 30.031 53.472 1.00 14.04 ? 406 LEU A N 1 ATOM 3143 C CA . LEU A 1 406 ? -12.061 31.338 53.598 1.00 15.05 ? 406 LEU A CA 1 ATOM 3144 C C . LEU A 1 406 ? -13.313 31.385 52.693 1.00 15.47 ? 406 LEU A C 1 ATOM 3145 O O . LEU A 1 406 ? -13.360 30.739 51.625 1.00 15.89 ? 406 LEU A O 1 ATOM 3146 C CB . LEU A 1 406 ? -11.094 32.358 53.009 1.00 16.04 ? 406 LEU A CB 1 ATOM 3147 C CG . LEU A 1 406 ? -9.750 32.495 53.731 1.00 18.56 ? 406 LEU A CG 1 ATOM 3148 C CD1 . LEU A 1 406 ? -8.758 33.285 52.855 1.00 21.27 ? 406 LEU A CD1 1 ATOM 3149 C CD2 . LEU A 1 406 ? -9.932 33.183 55.047 1.00 19.00 ? 406 LEU A CD2 1 ATOM 3150 N N . PRO A 1 407 ? -14.307 32.209 53.038 1.00 15.72 ? 407 PRO A N 1 ATOM 3151 C CA . PRO A 1 407 ? -15.484 32.353 52.197 1.00 14.66 ? 407 PRO A CA 1 ATOM 3152 C C . PRO A 1 407 ? -15.138 33.276 51.017 1.00 15.18 ? 407 PRO A C 1 ATOM 3153 O O . PRO A 1 407 ? -14.430 34.293 51.189 1.00 15.84 ? 407 PRO A O 1 ATOM 3154 C CB . PRO A 1 407 ? -16.529 33.014 53.153 1.00 15.53 ? 407 PRO A CB 1 ATOM 3155 C CG . PRO A 1 407 ? -15.683 33.750 54.124 1.00 16.85 ? 407 PRO A CG 1 ATOM 3156 C CD . PRO A 1 407 ? -14.397 32.957 54.302 1.00 15.84 ? 407 PRO A CD 1 ATOM 3157 N N . LYS A 1 408 ? -15.668 32.950 49.855 1.00 14.97 ? 408 LYS A N 1 ATOM 3158 C CA . LYS A 1 408 ? -15.473 33.779 48.670 1.00 14.99 ? 408 LYS A CA 1 ATOM 3159 C C . LYS A 1 408 ? -16.329 35.053 48.680 1.00 15.29 ? 408 LYS A C 1 ATOM 3160 O O . LYS A 1 408 ? -16.001 35.994 47.951 1.00 15.53 ? 408 LYS A O 1 ATOM 3161 C CB . LYS A 1 408 ? -15.779 32.970 47.399 1.00 15.24 ? 408 LYS A CB 1 ATOM 3162 C CG . LYS A 1 408 ? -14.796 31.826 47.125 1.00 15.00 ? 408 LYS A CG 1 ATOM 3163 C CD . LYS A 1 408 ? -15.234 31.038 45.900 1.00 16.20 ? 408 LYS A CD 1 ATOM 3164 C CE . LYS A 1 408 ? -14.221 29.926 45.607 1.00 17.43 ? 408 LYS A CE 1 ATOM 3165 N NZ . LYS A 1 408 ? -14.692 29.137 44.417 1.00 19.88 ? 408 LYS A NZ 1 ATOM 3166 N N . LYS A 1 409 ? -17.397 35.100 49.507 1.00 15.56 ? 409 LYS A N 1 ATOM 3167 C CA . LYS A 1 409 ? -18.262 36.300 49.588 1.00 16.37 ? 409 LYS A CA 1 ATOM 3168 C C . LYS A 1 409 ? -17.995 36.960 50.940 1.00 16.22 ? 409 LYS A C 1 ATOM 3169 O O . LYS A 1 409 ? -18.228 36.340 52.000 1.00 18.58 ? 409 LYS A O 1 ATOM 3170 C CB . LYS A 1 409 ? -19.764 35.934 49.450 1.00 18.40 ? 409 LYS A CB 1 ATOM 3171 C CG . LYS A 1 409 ? -20.628 37.173 49.363 1.00 23.20 ? 409 LYS A CG 1 ATOM 3172 C CD . LYS A 1 409 ? -22.055 36.803 49.051 1.00 27.73 ? 409 LYS A CD 1 ATOM 3173 C CE . LYS A 1 409 ? -22.890 38.080 49.048 1.00 32.51 ? 409 LYS A CE 1 ATOM 3174 N NZ . LYS A 1 409 ? -24.292 37.796 48.605 1.00 40.23 ? 409 LYS A NZ 1 ATOM 3175 N N . ALA A 1 410 ? -17.501 38.194 50.891 1.00 16.68 ? 410 ALA A N 1 ATOM 3176 C CA . ALA A 1 410 ? -17.295 39.015 52.120 1.00 15.81 ? 410 ALA A CA 1 ATOM 3177 C C . ALA A 1 410 ? -17.408 40.451 51.657 1.00 17.80 ? 410 ALA A C 1 ATOM 3178 O O . ALA A 1 410 ? -17.107 40.737 50.496 1.00 18.14 ? 410 ALA A O 1 ATOM 3179 C CB . ALA A 1 410 ? -15.892 38.725 52.723 1.00 16.47 ? 410 ALA A CB 1 ATOM 3180 N N . PRO A 1 411 ? -17.803 41.381 52.514 1.00 16.94 ? 411 PRO A N 1 ATOM 3181 C CA . PRO A 1 411 ? -17.898 42.752 51.997 1.00 16.50 ? 411 PRO A CA 1 ATOM 3182 C C . PRO A 1 411 ? -16.568 43.319 51.499 1.00 16.29 ? 411 PRO A C 1 ATOM 3183 O O . PRO A 1 411 ? -16.542 43.917 50.404 1.00 16.90 ? 411 PRO A O 1 ATOM 3184 C CB . PRO A 1 411 ? -18.482 43.554 53.200 1.00 17.43 ? 411 PRO A CB 1 ATOM 3185 C CG . PRO A 1 411 ? -19.299 42.504 53.882 1.00 17.81 ? 411 PRO A CG 1 ATOM 3186 C CD . PRO A 1 411 ? -18.434 41.251 53.845 1.00 18.47 ? 411 PRO A CD 1 ATOM 3187 N N . LYS A 1 412 ? -15.501 43.122 52.269 1.00 15.98 ? 412 LYS A N 1 ATOM 3188 C CA . LYS A 1 412 ? -14.214 43.726 51.929 1.00 16.10 ? 412 LYS A CA 1 ATOM 3189 C C . LYS A 1 412 ? -13.152 42.816 52.483 1.00 16.14 ? 412 LYS A C 1 ATOM 3190 O O . LYS A 1 412 ? -13.236 42.397 53.642 1.00 16.38 ? 412 LYS A O 1 ATOM 3191 C CB . LYS A 1 412 ? -14.086 45.061 52.643 1.00 17.29 ? 412 LYS A CB 1 ATOM 3192 C CG A LYS A 1 412 ? -13.084 45.986 51.994 0.60 19.46 ? 412 LYS A CG 1 ATOM 3193 C CG B LYS A 1 412 ? -14.686 46.270 52.000 0.40 17.15 ? 412 LYS A CG 1 ATOM 3194 C CD A LYS A 1 412 ? -13.252 47.367 52.585 0.60 21.12 ? 412 LYS A CD 1 ATOM 3195 C CD B LYS A 1 412 ? -14.407 47.531 52.821 0.40 17.19 ? 412 LYS A CD 1 ATOM 3196 C CE A LYS A 1 412 ? -12.051 48.224 52.292 0.60 23.83 ? 412 LYS A CE 1 ATOM 3197 C CE B LYS A 1 412 ? -13.074 48.156 52.489 0.40 18.37 ? 412 LYS A CE 1 ATOM 3198 N NZ A LYS A 1 412 ? -12.133 49.529 53.016 0.60 23.48 ? 412 LYS A NZ 1 ATOM 3199 N NZ B LYS A 1 412 ? -13.022 49.504 53.137 0.40 18.38 ? 412 LYS A NZ 1 ATOM 3200 N N . ILE A 1 413 ? -12.133 42.528 51.658 1.00 14.84 ? 413 ILE A N 1 ATOM 3201 C CA . ILE A 1 413 ? -10.969 41.754 52.119 1.00 14.34 ? 413 ILE A CA 1 ATOM 3202 C C . ILE A 1 413 ? -9.668 42.450 51.762 1.00 14.54 ? 413 ILE A C 1 ATOM 3203 O O . ILE A 1 413 ? -9.637 43.306 50.850 1.00 15.88 ? 413 ILE A O 1 ATOM 3204 C CB . ILE A 1 413 ? -10.971 40.283 51.587 1.00 14.45 ? 413 ILE A CB 1 ATOM 3205 C CG1 . ILE A 1 413 ? -10.721 40.255 50.060 1.00 15.11 ? 413 ILE A CG1 1 ATOM 3206 C CG2 . ILE A 1 413 ? -12.323 39.632 51.925 1.00 14.98 ? 413 ILE A CG2 1 ATOM 3207 C CD1 . ILE A 1 413 ? -10.542 38.857 49.461 1.00 16.86 ? 413 ILE A CD1 1 ATOM 3208 N N . LEU A 1 414 ? -8.621 42.129 52.512 1.00 13.24 ? 414 LEU A N 1 ATOM 3209 C CA . LEU A 1 414 ? -7.282 42.719 52.299 1.00 13.54 ? 414 LEU A CA 1 ATOM 3210 C C . LEU A 1 414 ? -6.307 41.657 51.758 1.00 14.09 ? 414 LEU A C 1 ATOM 3211 O O . LEU A 1 414 ? -6.212 40.556 52.292 1.00 13.81 ? 414 LEU A O 1 ATOM 3212 C CB . LEU A 1 414 ? -6.738 43.277 53.616 1.00 14.37 ? 414 LEU A CB 1 ATOM 3213 C CG . LEU A 1 414 ? -5.320 43.845 53.588 1.00 15.51 ? 414 LEU A CG 1 ATOM 3214 C CD1 . LEU A 1 414 ? -5.193 45.044 52.656 1.00 15.78 ? 414 LEU A CD1 1 ATOM 3215 C CD2 . LEU A 1 414 ? -4.933 44.240 54.996 1.00 15.58 ? 414 LEU A CD2 1 ATOM 3216 N N . VAL A 1 415 ? -5.595 42.007 50.691 1.00 13.29 ? 415 VAL A N 1 ATOM 3217 C CA . VAL A 1 415 ? -4.434 41.214 50.195 1.00 13.51 ? 415 VAL A CA 1 ATOM 3218 C C . VAL A 1 415 ? -3.222 42.108 50.399 1.00 14.16 ? 415 VAL A C 1 ATOM 3219 O O . VAL A 1 415 ? -3.211 43.274 49.972 1.00 14.68 ? 415 VAL A O 1 ATOM 3220 C CB . VAL A 1 415 ? -4.635 40.835 48.706 1.00 13.64 ? 415 VAL A CB 1 ATOM 3221 C CG1 . VAL A 1 415 ? -3.403 40.123 48.176 1.00 14.97 ? 415 VAL A CG1 1 ATOM 3222 C CG2 . VAL A 1 415 ? -5.895 39.940 48.560 1.00 14.84 ? 415 VAL A CG2 1 ATOM 3223 N N . ALA A 1 416 ? -2.204 41.560 51.050 1.00 13.59 ? 416 ALA A N 1 ATOM 3224 C CA . ALA A 1 416 ? -1.054 42.363 51.463 1.00 13.63 ? 416 ALA A CA 1 ATOM 3225 C C . ALA A 1 416 ? 0.221 41.577 51.371 1.00 13.59 ? 416 ALA A C 1 ATOM 3226 O O . ALA A 1 416 ? 0.213 40.339 51.229 1.00 14.00 ? 416 ALA A O 1 ATOM 3227 C CB . ALA A 1 416 ? -1.271 42.854 52.917 1.00 14.19 ? 416 ALA A CB 1 ATOM 3228 N N . GLY A 1 417 ? 1.342 42.315 51.457 1.00 13.81 ? 417 GLY A N 1 ATOM 3229 C CA . GLY A 1 417 ? 2.704 41.710 51.496 1.00 13.98 ? 417 GLY A CA 1 ATOM 3230 C C . GLY A 1 417 ? 3.445 41.836 50.193 1.00 14.19 ? 417 GLY A C 1 ATOM 3231 O O . GLY A 1 417 ? 2.849 41.978 49.119 1.00 14.54 ? 417 GLY A O 1 ATOM 3232 N N . SER A 1 418 ? 4.771 41.814 50.330 1.00 14.75 ? 418 SER A N 1 ATOM 3233 C CA . SER A 1 418 ? 5.672 41.924 49.205 1.00 14.36 ? 418 SER A CA 1 ATOM 3234 C C . SER A 1 418 ? 5.537 40.817 48.183 1.00 14.53 ? 418 SER A C 1 ATOM 3235 O O . SER A 1 418 ? 5.992 40.962 47.036 1.00 15.85 ? 418 SER A O 1 ATOM 3236 C CB . SER A 1 418 ? 7.096 41.930 49.746 1.00 15.98 ? 418 SER A CB 1 ATOM 3237 O OG . SER A 1 418 ? 7.355 40.770 50.529 1.00 17.53 ? 418 SER A OG 1 ATOM 3238 N N . HIS A 1 419 ? 4.947 39.689 48.587 1.00 12.90 ? 419 HIS A N 1 ATOM 3239 C CA . HIS A 1 419 ? 4.854 38.583 47.674 1.00 12.53 ? 419 HIS A CA 1 ATOM 3240 C C . HIS A 1 419 ? 3.426 38.334 47.195 1.00 13.45 ? 419 HIS A C 1 ATOM 3241 O O . HIS A 1 419 ? 3.202 37.335 46.479 1.00 13.12 ? 419 HIS A O 1 ATOM 3242 C CB . HIS A 1 419 ? 5.393 37.312 48.373 1.00 12.90 ? 419 HIS A CB 1 ATOM 3243 C CG . HIS A 1 419 ? 6.882 37.319 48.549 1.00 12.94 ? 419 HIS A CG 1 ATOM 3244 N ND1 . HIS A 1 419 ? 7.543 38.297 49.268 1.00 15.04 ? 419 HIS A ND1 1 ATOM 3245 C CD2 . HIS A 1 419 ? 7.819 36.413 48.164 1.00 13.74 ? 419 HIS A CD2 1 ATOM 3246 C CE1 . HIS A 1 419 ? 8.839 38.025 49.265 1.00 14.03 ? 419 HIS A CE1 1 ATOM 3247 N NE2 . HIS A 1 419 ? 9.035 36.889 48.620 1.00 13.83 ? 419 HIS A NE2 1 ATOM 3248 N N . ALA A 1 420 ? 2.483 39.221 47.533 1.00 12.60 ? 420 ALA A N 1 ATOM 3249 C CA . ALA A 1 420 ? 1.106 39.048 47.033 1.00 13.21 ? 420 ALA A CA 1 ATOM 3250 C C . ALA A 1 420 ? 0.932 39.366 45.583 1.00 13.74 ? 420 ALA A C 1 ATOM 3251 O O . ALA A 1 420 ? 0.033 38.819 44.949 1.00 14.00 ? 420 ALA A O 1 ATOM 3252 C CB . ALA A 1 420 ? 0.162 39.935 47.847 1.00 14.82 ? 420 ALA A CB 1 ATOM 3253 N N . ASP A 1 421 ? 1.755 40.256 45.018 1.00 13.17 ? 421 ASP A N 1 ATOM 3254 C CA . ASP A 1 421 ? 1.565 40.671 43.632 1.00 14.03 ? 421 ASP A CA 1 ATOM 3255 C C . ASP A 1 421 ? 2.950 40.846 43.018 1.00 13.90 ? 421 ASP A C 1 ATOM 3256 O O . ASP A 1 421 ? 3.349 41.950 42.609 1.00 16.88 ? 421 ASP A O 1 ATOM 3257 C CB . ASP A 1 421 ? 0.795 41.999 43.590 1.00 14.42 ? 421 ASP A CB 1 ATOM 3258 C CG . ASP A 1 421 ? 0.376 42.380 42.188 1.00 15.92 ? 421 ASP A CG 1 ATOM 3259 O OD1 . ASP A 1 421 ? -0.032 41.495 41.417 1.00 16.38 ? 421 ASP A OD1 1 ATOM 3260 O OD2 . ASP A 1 421 ? 0.447 43.581 41.834 1.00 18.56 ? 421 ASP A OD2 1 ATOM 3261 N N . ASN A 1 422 ? 3.675 39.727 42.960 1.00 12.65 ? 422 ASN A N 1 ATOM 3262 C CA . ASN A 1 422 ? 5.007 39.746 42.409 1.00 12.60 ? 422 ASN A CA 1 ATOM 3263 C C . ASN A 1 422 ? 5.291 38.409 41.758 1.00 12.53 ? 422 ASN A C 1 ATOM 3264 O O . ASN A 1 422 ? 5.639 37.453 42.442 1.00 13.55 ? 422 ASN A O 1 ATOM 3265 C CB . ASN A 1 422 ? 6.039 40.118 43.497 1.00 13.24 ? 422 ASN A CB 1 ATOM 3266 C CG . ASN A 1 422 ? 7.405 40.384 42.891 1.00 13.66 ? 422 ASN A CG 1 ATOM 3267 O OD1 . ASN A 1 422 ? 7.862 39.678 41.960 1.00 14.31 ? 422 ASN A OD1 1 ATOM 3268 N ND2 . ASN A 1 422 ? 8.095 41.445 43.391 1.00 15.26 ? 422 ASN A ND2 1 ATOM 3269 N N . LEU A 1 423 ? 5.097 38.340 40.440 1.00 12.61 ? 423 LEU A N 1 ATOM 3270 C CA . LEU A 1 423 ? 5.252 37.055 39.709 1.00 13.34 ? 423 LEU A CA 1 ATOM 3271 C C . LEU A 1 423 ? 6.670 36.506 39.853 1.00 12.93 ? 423 LEU A C 1 ATOM 3272 O O . LEU A 1 423 ? 6.877 35.312 40.063 1.00 12.63 ? 423 LEU A O 1 ATOM 3273 C CB . LEU A 1 423 ? 4.864 37.281 38.235 1.00 14.46 ? 423 LEU A CB 1 ATOM 3274 C CG . LEU A 1 423 ? 4.707 35.988 37.446 1.00 16.74 ? 423 LEU A CG 1 ATOM 3275 C CD1 . LEU A 1 423 ? 3.592 35.121 38.021 1.00 20.27 ? 423 LEU A CD1 1 ATOM 3276 C CD2 . LEU A 1 423 ? 4.329 36.418 36.039 1.00 18.72 ? 423 LEU A CD2 1 ATOM 3277 N N . GLY A 1 424 ? 7.665 37.390 39.715 1.00 12.08 ? 424 GLY A N 1 ATOM 3278 C CA . GLY A 1 424 ? 9.079 36.955 39.816 1.00 12.01 ? 424 GLY A CA 1 ATOM 3279 C C . GLY A 1 424 ? 9.352 36.279 41.173 1.00 13.29 ? 424 GLY A C 1 ATOM 3280 O O . GLY A 1 424 ? 10.011 35.233 41.272 1.00 13.17 ? 424 GLY A O 1 ATOM 3281 N N . TYR A 1 425 ? 8.825 36.880 42.234 1.00 12.54 ? 425 TYR A N 1 ATOM 3282 C CA . TYR A 1 425 ? 9.061 36.322 43.556 1.00 12.62 ? 425 TYR A CA 1 ATOM 3283 C C . TYR A 1 425 ? 8.359 34.973 43.711 1.00 13.18 ? 425 TYR A C 1 ATOM 3284 O O . TYR A 1 425 ? 8.891 34.099 44.404 1.00 13.84 ? 425 TYR A O 1 ATOM 3285 C CB . TYR A 1 425 ? 8.557 37.287 44.631 1.00 14.41 ? 425 TYR A CB 1 ATOM 3286 C CG . TYR A 1 425 ? 9.421 38.486 44.951 1.00 13.99 ? 425 TYR A CG 1 ATOM 3287 C CD1 . TYR A 1 425 ? 10.574 38.810 44.215 1.00 15.20 ? 425 TYR A CD1 1 ATOM 3288 C CD2 . TYR A 1 425 ? 9.013 39.300 45.999 1.00 14.64 ? 425 TYR A CD2 1 ATOM 3289 C CE1 . TYR A 1 425 ? 11.313 39.942 44.553 1.00 15.78 ? 425 TYR A CE1 1 ATOM 3290 C CE2 . TYR A 1 425 ? 9.768 40.419 46.365 1.00 16.35 ? 425 TYR A CE2 1 ATOM 3291 C CZ . TYR A 1 425 ? 10.894 40.732 45.608 1.00 16.43 ? 425 TYR A CZ 1 ATOM 3292 O OH . TYR A 1 425 ? 11.640 41.860 45.980 1.00 20.26 ? 425 TYR A OH 1 ATOM 3293 N N . GLN A 1 426 ? 7.179 34.810 43.093 1.00 12.93 ? 426 GLN A N 1 ATOM 3294 C CA . GLN A 1 426 ? 6.479 33.538 43.307 1.00 13.92 ? 426 GLN A CA 1 ATOM 3295 C C . GLN A 1 426 ? 7.100 32.400 42.495 1.00 12.84 ? 426 GLN A C 1 ATOM 3296 O O . GLN A 1 426 ? 6.906 31.239 42.806 1.00 13.44 ? 426 GLN A O 1 ATOM 3297 C CB . GLN A 1 426 ? 4.983 33.699 43.106 1.00 18.54 ? 426 GLN A CB 1 ATOM 3298 C CG . GLN A 1 426 ? 4.479 33.781 41.732 1.00 19.60 ? 426 GLN A CG 1 ATOM 3299 C CD . GLN A 1 426 ? 2.925 33.888 41.744 1.00 19.06 ? 426 GLN A CD 1 ATOM 3300 O OE1 . GLN A 1 426 ? 2.359 34.700 42.466 1.00 19.65 ? 426 GLN A OE1 1 ATOM 3301 N NE2 . GLN A 1 426 ? 2.267 33.110 40.903 1.00 14.00 ? 426 GLN A NE2 1 ATOM 3302 N N . CYS A 1 427 ? 7.888 32.764 41.470 1.00 13.12 ? 427 CYS A N 1 ATOM 3303 C CA . CYS A 1 427 ? 8.617 31.771 40.638 1.00 12.20 ? 427 CYS A CA 1 ATOM 3304 C C . CYS A 1 427 ? 10.004 31.436 41.215 1.00 11.93 ? 427 CYS A C 1 ATOM 3305 O O . CYS A 1 427 ? 10.486 30.318 41.062 1.00 12.73 ? 427 CYS A O 1 ATOM 3306 C CB . CYS A 1 427 ? 8.793 32.335 39.216 1.00 11.88 ? 427 CYS A CB 1 ATOM 3307 S SG . CYS A 1 427 ? 7.217 32.355 38.315 1.00 13.27 ? 427 CYS A SG 1 ATOM 3308 N N . GLY A 1 428 ? 10.648 32.388 41.870 1.00 12.44 ? 428 GLY A N 1 ATOM 3309 C CA . GLY A 1 428 ? 12.002 32.148 42.426 1.00 12.92 ? 428 GLY A CA 1 ATOM 3310 C C . GLY A 1 428 ? 13.084 32.003 41.343 1.00 11.96 ? 428 GLY A C 1 ATOM 3311 O O . GLY A 1 428 ? 12.940 32.475 40.198 1.00 12.87 ? 428 GLY A O 1 ATOM 3312 N N . GLY A 1 429 ? 14.179 31.371 41.720 1.00 12.51 ? 429 GLY A N 1 ATOM 3313 C CA . GLY A 1 429 ? 15.350 31.253 40.844 1.00 12.61 ? 429 GLY A CA 1 ATOM 3314 C C . GLY A 1 429 ? 15.082 30.485 39.574 1.00 12.58 ? 429 GLY A C 1 ATOM 3315 O O . GLY A 1 429 ? 14.024 29.818 39.441 1.00 12.35 ? 429 GLY A O 1 ATOM 3316 N N . TRP A 1 430 ? 16.049 30.538 38.651 1.00 12.57 ? 430 TRP A N 1 ATOM 3317 C CA . TRP A 1 430 ? 15.848 29.871 37.350 1.00 12.13 ? 430 TRP A CA 1 ATOM 3318 C C . TRP A 1 430 ? 14.508 30.215 36.701 1.00 12.62 ? 430 TRP A C 1 ATOM 3319 O O . TRP A 1 430 ? 13.761 29.351 36.256 1.00 12.61 ? 430 TRP A O 1 ATOM 3320 C CB . TRP A 1 430 ? 15.933 28.344 37.485 1.00 13.03 ? 430 TRP A CB 1 ATOM 3321 C CG . TRP A 1 430 ? 17.328 27.826 37.771 1.00 12.43 ? 430 TRP A CG 1 ATOM 3322 C CD1 . TRP A 1 430 ? 17.765 27.296 38.973 1.00 13.58 ? 430 TRP A CD1 1 ATOM 3323 C CD2 . TRP A 1 430 ? 18.423 27.730 36.866 1.00 12.81 ? 430 TRP A CD2 1 ATOM 3324 N NE1 . TRP A 1 430 ? 19.084 26.884 38.877 1.00 13.61 ? 430 TRP A NE1 1 ATOM 3325 C CE2 . TRP A 1 430 ? 19.499 27.118 37.578 1.00 12.99 ? 430 TRP A CE2 1 ATOM 3326 C CE3 . TRP A 1 430 ? 18.600 28.080 35.508 1.00 13.05 ? 430 TRP A CE3 1 ATOM 3327 C CZ2 . TRP A 1 430 ? 20.761 26.876 36.962 1.00 13.28 ? 430 TRP A CZ2 1 ATOM 3328 C CZ3 . TRP A 1 430 ? 19.841 27.848 34.919 1.00 13.10 ? 430 TRP A CZ3 1 ATOM 3329 C CH2 . TRP A 1 430 ? 20.888 27.237 35.630 1.00 13.15 ? 430 TRP A CH2 1 ATOM 3330 N N . THR A 1 431 ? 14.209 31.508 36.630 1.00 12.01 ? 431 THR A N 1 ATOM 3331 C CA . THR A 1 431 ? 13.005 31.964 35.909 1.00 12.08 ? 431 THR A CA 1 ATOM 3332 C C . THR A 1 431 ? 13.359 33.258 35.188 1.00 12.88 ? 431 THR A C 1 ATOM 3333 O O . THR A 1 431 ? 13.620 34.276 35.860 1.00 12.09 ? 431 THR A O 1 ATOM 3334 C CB . THR A 1 431 ? 11.816 32.237 36.873 1.00 12.16 ? 431 THR A CB 1 ATOM 3335 O OG1 . THR A 1 431 ? 11.660 31.084 37.761 1.00 12.68 ? 431 THR A OG1 1 ATOM 3336 C CG2 . THR A 1 431 ? 10.512 32.425 36.086 1.00 13.26 ? 431 THR A CG2 1 ATOM 3337 N N . ILE A 1 432 ? 13.424 33.165 33.837 1.00 12.56 ? 432 ILE A N 1 ATOM 3338 C CA . ILE A 1 432 ? 13.783 34.253 32.885 1.00 13.34 ? 432 ILE A CA 1 ATOM 3339 C C . ILE A 1 432 ? 15.286 34.598 32.989 1.00 13.92 ? 432 ILE A C 1 ATOM 3340 O O . ILE A 1 432 ? 16.035 34.508 32.007 1.00 14.54 ? 432 ILE A O 1 ATOM 3341 C CB . ILE A 1 432 ? 12.876 35.480 33.024 1.00 13.55 ? 432 ILE A CB 1 ATOM 3342 C CG1 . ILE A 1 432 ? 11.394 35.130 32.792 1.00 13.97 ? 432 ILE A CG1 1 ATOM 3343 C CG2 . ILE A 1 432 ? 13.342 36.566 32.044 1.00 14.04 ? 432 ILE A CG2 1 ATOM 3344 C CD1 . ILE A 1 432 ? 11.081 34.491 31.430 1.00 14.61 ? 432 ILE A CD1 1 ATOM 3345 N N . GLU A 1 433 ? 15.714 34.959 34.195 1.00 13.97 ? 433 GLU A N 1 ATOM 3346 C CA . GLU A 1 433 ? 17.150 35.071 34.528 1.00 14.96 ? 433 GLU A CA 1 ATOM 3347 C C . GLU A 1 433 ? 17.614 33.858 35.289 1.00 15.52 ? 433 GLU A C 1 ATOM 3348 O O . GLU A 1 433 ? 16.819 33.139 35.897 1.00 14.19 ? 433 GLU A O 1 ATOM 3349 C CB . GLU A 1 433 ? 17.383 36.313 35.395 1.00 17.51 ? 433 GLU A CB 1 ATOM 3350 C CG . GLU A 1 433 ? 16.880 37.615 34.811 1.00 22.47 ? 433 GLU A CG 1 ATOM 3351 C CD . GLU A 1 433 ? 17.667 38.094 33.619 1.00 26.05 ? 433 GLU A CD 1 ATOM 3352 O OE1 . GLU A 1 433 ? 18.726 37.522 33.277 1.00 25.95 ? 433 GLU A OE1 1 ATOM 3353 O OE2 . GLU A 1 433 ? 17.202 39.111 33.056 1.00 34.07 ? 433 GLU A OE2 1 ATOM 3354 N N . TRP A 1 434 ? 18.920 33.622 35.308 1.00 14.67 ? 434 TRP A N 1 ATOM 3355 C CA . TRP A 1 434 ? 19.479 32.552 36.130 1.00 14.35 ? 434 TRP A CA 1 ATOM 3356 C C . TRP A 1 434 ? 19.018 32.636 37.599 1.00 15.40 ? 434 TRP A C 1 ATOM 3357 O O . TRP A 1 434 ? 18.531 31.634 38.167 1.00 15.15 ? 434 TRP A O 1 ATOM 3358 C CB . TRP A 1 434 ? 21.031 32.597 36.002 1.00 14.76 ? 434 TRP A CB 1 ATOM 3359 C CG . TRP A 1 434 ? 21.702 31.654 36.964 1.00 15.16 ? 434 TRP A CG 1 ATOM 3360 C CD1 . TRP A 1 434 ? 21.390 30.340 37.204 1.00 15.59 ? 434 TRP A CD1 1 ATOM 3361 C CD2 . TRP A 1 434 ? 22.812 31.954 37.809 1.00 16.75 ? 434 TRP A CD2 1 ATOM 3362 N NE1 . TRP A 1 434 ? 22.223 29.809 38.171 1.00 17.36 ? 434 TRP A NE1 1 ATOM 3363 C CE2 . TRP A 1 434 ? 23.110 30.779 38.550 1.00 17.42 ? 434 TRP A CE2 1 ATOM 3364 C CE3 . TRP A 1 434 ? 23.570 33.122 38.026 1.00 17.04 ? 434 TRP A CE3 1 ATOM 3365 C CZ2 . TRP A 1 434 ? 24.113 30.740 39.507 1.00 18.28 ? 434 TRP A CZ2 1 ATOM 3366 C CZ3 . TRP A 1 434 ? 24.561 33.098 38.975 1.00 18.82 ? 434 TRP A CZ3 1 ATOM 3367 C CH2 . TRP A 1 434 ? 24.854 31.911 39.694 1.00 18.72 ? 434 TRP A CH2 1 ATOM 3368 N N . GLN A 1 435 ? 19.221 33.812 38.210 1.00 15.34 ? 435 GLN A N 1 ATOM 3369 C CA . GLN A 1 435 ? 18.874 34.031 39.611 1.00 16.06 ? 435 GLN A CA 1 ATOM 3370 C C . GLN A 1 435 ? 17.425 34.449 39.849 1.00 16.00 ? 435 GLN A C 1 ATOM 3371 O O . GLN A 1 435 ? 17.069 34.803 40.970 1.00 18.20 ? 435 GLN A O 1 ATOM 3372 C CB . GLN A 1 435 ? 19.811 35.088 40.179 1.00 18.62 ? 435 GLN A CB 1 ATOM 3373 C CG . GLN A 1 435 ? 21.246 34.599 40.135 1.00 20.01 ? 435 GLN A CG 1 ATOM 3374 C CD . GLN A 1 435 ? 22.197 35.623 40.644 1.00 25.85 ? 435 GLN A CD 1 ATOM 3375 O OE1 . GLN A 1 435 ? 22.582 35.594 41.824 1.00 30.50 ? 435 GLN A OE1 1 ATOM 3376 N NE2 . GLN A 1 435 ? 22.599 36.544 39.775 1.00 28.34 ? 435 GLN A NE2 1 ATOM 3377 N N . GLY A 1 436 ? 16.572 34.386 38.820 1.00 15.14 ? 436 GLY A N 1 ATOM 3378 C CA . GLY A 1 436 ? 15.244 34.957 38.891 1.00 15.34 ? 436 GLY A CA 1 ATOM 3379 C C . GLY A 1 436 ? 15.294 36.478 38.930 1.00 16.36 ? 436 GLY A C 1 ATOM 3380 O O . GLY A 1 436 ? 16.351 37.135 38.699 1.00 17.03 ? 436 GLY A O 1 ATOM 3381 N N . ASP A 1 437 ? 14.119 37.072 39.185 1.00 14.90 ? 437 ASP A N 1 ATOM 3382 C CA . ASP A 1 437 ? 13.979 38.535 39.102 1.00 16.08 ? 437 ASP A CA 1 ATOM 3383 C C . ASP A 1 437 ? 12.708 38.954 39.824 1.00 16.45 ? 437 ASP A C 1 ATOM 3384 O O . ASP A 1 437 ? 11.948 38.103 40.337 1.00 15.57 ? 437 ASP A O 1 ATOM 3385 C CB . ASP A 1 437 ? 13.986 38.959 37.612 1.00 17.60 ? 437 ASP A CB 1 ATOM 3386 C CG . ASP A 1 437 ? 14.320 40.438 37.388 1.00 19.94 ? 437 ASP A CG 1 ATOM 3387 O OD1 . ASP A 1 437 ? 14.609 41.194 38.345 1.00 22.29 ? 437 ASP A OD1 1 ATOM 3388 O OD2 . ASP A 1 437 ? 14.292 40.797 36.192 1.00 24.40 ? 437 ASP A OD2 1 ATOM 3389 N N . THR A 1 438 ? 12.494 40.268 39.916 1.00 17.18 ? 438 THR A N 1 ATOM 3390 C CA . THR A 1 438 ? 11.317 40.838 40.567 1.00 16.36 ? 438 THR A CA 1 ATOM 3391 C C . THR A 1 438 ? 10.296 41.364 39.560 1.00 15.73 ? 438 THR A C 1 ATOM 3392 O O . THR A 1 438 ? 10.631 41.891 38.499 1.00 17.20 ? 438 THR A O 1 ATOM 3393 C CB . THR A 1 438 ? 11.761 41.929 41.546 1.00 16.48 ? 438 THR A CB 1 ATOM 3394 O OG1 . THR A 1 438 ? 10.623 42.477 42.199 1.00 16.07 ? 438 THR A OG1 1 ATOM 3395 C CG2 . THR A 1 438 ? 12.481 43.082 40.782 1.00 17.28 ? 438 THR A CG2 1 ATOM 3396 N N . GLY A 1 439 ? 9.024 41.207 39.904 1.00 15.22 ? 439 GLY A N 1 ATOM 3397 C CA . GLY A 1 439 ? 7.931 41.791 39.152 1.00 16.23 ? 439 GLY A CA 1 ATOM 3398 C C . GLY A 1 439 ? 7.377 40.951 38.041 1.00 15.92 ? 439 GLY A C 1 ATOM 3399 O O . GLY A 1 439 ? 7.438 39.700 38.092 1.00 16.31 ? 439 GLY A O 1 ATOM 3400 N N . ARG A 1 440 ? 6.768 41.608 37.061 1.00 16.45 ? 440 ARG A N 1 ATOM 3401 C CA . ARG A 1 440 ? 6.013 40.866 36.042 1.00 16.88 ? 440 ARG A CA 1 ATOM 3402 C C . ARG A 1 440 ? 6.938 40.456 34.910 1.00 17.26 ? 440 ARG A C 1 ATOM 3403 O O . ARG A 1 440 ? 6.987 41.092 33.845 1.00 18.81 ? 440 ARG A O 1 ATOM 3404 C CB . ARG A 1 440 ? 4.823 41.708 35.550 1.00 21.65 ? 440 ARG A CB 1 ATOM 3405 C CG . ARG A 1 440 ? 3.955 40.904 34.594 1.00 24.92 ? 440 ARG A CG 1 ATOM 3406 C CD A ARG A 1 440 ? 2.514 41.405 34.477 1.00 32.58 ? 440 ARG A CD 1 ATOM 3407 N NE A ARG A 1 440 ? 1.721 40.226 34.851 1.00 41.11 ? 440 ARG A NE 1 ATOM 3408 C CZ A ARG A 1 440 ? 1.378 39.872 36.100 1.00 41.21 ? 440 ARG A CZ 1 ATOM 3409 N NH1 A ARG A 1 440 ? 1.692 40.642 37.173 1.00 38.60 ? 440 ARG A NH1 1 ATOM 3410 N NH2 A ARG A 1 440 ? 0.732 38.718 36.273 1.00 31.20 ? 440 ARG A NH2 1 ATOM 3411 N N . THR A 1 441 ? 7.706 39.374 35.156 1.00 16.71 ? 441 THR A N 1 ATOM 3412 C CA . THR A 1 441 ? 8.809 39.004 34.277 1.00 17.12 ? 441 THR A CA 1 ATOM 3413 C C . THR A 1 441 ? 8.379 38.060 33.147 1.00 16.31 ? 441 THR A C 1 ATOM 3414 O O . THR A 1 441 ? 9.150 37.800 32.232 1.00 16.92 ? 441 THR A O 1 ATOM 3415 C CB . THR A 1 441 ? 9.901 38.292 35.070 1.00 18.31 ? 441 THR A CB 1 ATOM 3416 O OG1 . THR A 1 441 ? 9.304 37.169 35.731 1.00 18.26 ? 441 THR A OG1 1 ATOM 3417 C CG2 . THR A 1 441 ? 10.424 39.203 36.185 1.00 19.79 ? 441 THR A CG2 1 ATOM 3418 N N . THR A 1 442 ? 7.137 37.564 33.219 1.00 14.67 ? 442 THR A N 1 ATOM 3419 C CA . THR A 1 442 ? 6.656 36.604 32.242 1.00 13.64 ? 442 THR A CA 1 ATOM 3420 C C . THR A 1 442 ? 5.124 36.590 32.310 1.00 13.11 ? 442 THR A C 1 ATOM 3421 O O . THR A 1 442 ? 4.540 37.483 32.921 1.00 14.78 ? 442 THR A O 1 ATOM 3422 C CB . THR A 1 442 ? 7.308 35.213 32.474 1.00 13.96 ? 442 THR A CB 1 ATOM 3423 O OG1 . THR A 1 442 ? 6.943 34.384 31.363 1.00 13.48 ? 442 THR A OG1 1 ATOM 3424 C CG2 . THR A 1 442 ? 6.856 34.508 33.788 1.00 13.97 ? 442 THR A CG2 1 ATOM 3425 N N . VAL A 1 443 ? 4.464 35.623 31.680 1.00 12.62 ? 443 VAL A N 1 ATOM 3426 C CA . VAL A 1 443 ? 2.994 35.538 31.705 1.00 12.87 ? 443 VAL A CA 1 ATOM 3427 C C . VAL A 1 443 ? 2.580 34.649 32.864 1.00 12.15 ? 443 VAL A C 1 ATOM 3428 O O . VAL A 1 443 ? 3.085 33.528 33.012 1.00 14.21 ? 443 VAL A O 1 ATOM 3429 C CB . VAL A 1 443 ? 2.480 34.998 30.369 1.00 13.13 ? 443 VAL A CB 1 ATOM 3430 C CG1 . VAL A 1 443 ? 0.959 34.779 30.365 1.00 14.56 ? 443 VAL A CG1 1 ATOM 3431 C CG2 . VAL A 1 443 ? 2.941 35.927 29.221 1.00 15.17 ? 443 VAL A CG2 1 ATOM 3432 N N . GLY A 1 444 ? 1.682 35.152 33.710 1.00 12.04 ? 444 GLY A N 1 ATOM 3433 C CA . GLY A 1 444 ? 1.196 34.313 34.818 1.00 12.31 ? 444 GLY A CA 1 ATOM 3434 C C . GLY A 1 444 ? 0.155 35.061 35.614 1.00 12.73 ? 444 GLY A C 1 ATOM 3435 O O . GLY A 1 444 ? -0.349 36.088 35.155 1.00 15.78 ? 444 GLY A O 1 ATOM 3436 N N . THR A 1 445 ? -0.117 34.532 36.803 1.00 11.86 ? 445 THR A N 1 ATOM 3437 C CA . THR A 1 445 ? -1.187 35.082 37.656 1.00 11.95 ? 445 THR A CA 1 ATOM 3438 C C . THR A 1 445 ? -0.639 35.166 39.056 1.00 11.76 ? 445 THR A C 1 ATOM 3439 O O . THR A 1 445 ? -0.276 34.139 39.650 1.00 11.55 ? 445 THR A O 1 ATOM 3440 C CB . THR A 1 445 ? -2.423 34.139 37.600 1.00 11.74 ? 445 THR A CB 1 ATOM 3441 O OG1 . THR A 1 445 ? -2.929 34.036 36.250 1.00 14.51 ? 445 THR A OG1 1 ATOM 3442 C CG2 . THR A 1 445 ? -3.556 34.680 38.464 1.00 12.91 ? 445 THR A CG2 1 ATOM 3443 N N . THR A 1 446 ? -0.573 36.399 39.591 1.00 12.15 ? 446 THR A N 1 ATOM 3444 C CA . THR A 1 446 ? -0.056 36.573 40.974 1.00 11.79 ? 446 THR A CA 1 ATOM 3445 C C . THR A 1 446 ? -1.132 36.147 41.995 1.00 12.15 ? 446 THR A C 1 ATOM 3446 O O . THR A 1 446 ? -2.294 35.817 41.614 1.00 12.30 ? 446 THR A O 1 ATOM 3447 C CB . THR A 1 446 ? 0.312 38.022 41.266 1.00 11.97 ? 446 THR A CB 1 ATOM 3448 O OG1 . THR A 1 446 ? -0.861 38.844 41.132 1.00 12.97 ? 446 THR A OG1 1 ATOM 3449 C CG2 . THR A 1 446 ? 1.383 38.488 40.306 1.00 13.03 ? 446 THR A CG2 1 ATOM 3450 N N . ILE A 1 447 ? -0.742 36.087 43.254 1.00 12.14 ? 447 ILE A N 1 ATOM 3451 C CA . ILE A 1 447 ? -1.715 35.724 44.284 1.00 11.92 ? 447 ILE A CA 1 ATOM 3452 C C . ILE A 1 447 ? -2.846 36.763 44.335 1.00 11.60 ? 447 ILE A C 1 ATOM 3453 O O . ILE A 1 447 ? -4.021 36.374 44.398 1.00 12.07 ? 447 ILE A O 1 ATOM 3454 C CB . ILE A 1 447 ? -1.011 35.582 45.638 1.00 12.57 ? 447 ILE A CB 1 ATOM 3455 C CG1 . ILE A 1 447 ? -0.100 34.349 45.566 1.00 13.41 ? 447 ILE A CG1 1 ATOM 3456 C CG2 . ILE A 1 447 ? -2.052 35.470 46.755 1.00 13.41 ? 447 ILE A CG2 1 ATOM 3457 C CD1 . ILE A 1 447 ? 0.856 34.279 46.793 1.00 14.19 ? 447 ILE A CD1 1 ATOM 3458 N N . LEU A 1 448 ? -2.525 38.063 44.211 1.00 11.89 ? 448 LEU A N 1 ATOM 3459 C CA . LEU A 1 448 ? -3.580 39.092 44.169 1.00 12.58 ? 448 LEU A CA 1 ATOM 3460 C C . LEU A 1 448 ? -4.544 38.872 43.001 1.00 12.89 ? 448 LEU A C 1 ATOM 3461 O O . LEU A 1 448 ? -5.754 38.948 43.156 1.00 13.36 ? 448 LEU A O 1 ATOM 3462 C CB . LEU A 1 448 ? -2.927 40.483 44.055 1.00 13.55 ? 448 LEU A CB 1 ATOM 3463 C CG . LEU A 1 448 ? -3.891 41.632 43.811 1.00 13.55 ? 448 LEU A CG 1 ATOM 3464 C CD1 . LEU A 1 448 ? -4.847 41.794 45.026 1.00 14.12 ? 448 LEU A CD1 1 ATOM 3465 C CD2 . LEU A 1 448 ? -3.078 42.925 43.623 1.00 14.31 ? 448 LEU A CD2 1 ATOM 3466 N N . GLU A 1 449 ? -3.986 38.629 41.825 1.00 12.72 ? 449 GLU A N 1 ATOM 3467 C CA . GLU A 1 449 ? -4.829 38.383 40.634 1.00 13.26 ? 449 GLU A CA 1 ATOM 3468 C C . GLU A 1 449 ? -5.699 37.151 40.831 1.00 12.96 ? 449 GLU A C 1 ATOM 3469 O O . GLU A 1 449 ? -6.866 37.173 40.409 1.00 13.43 ? 449 GLU A O 1 ATOM 3470 C CB . GLU A 1 449 ? -3.914 38.246 39.392 1.00 14.96 ? 449 GLU A CB 1 ATOM 3471 C CG . GLU A 1 449 ? -3.290 39.604 38.985 1.00 17.40 ? 449 GLU A CG 1 ATOM 3472 C CD . GLU A 1 449 ? -2.123 39.498 38.015 1.00 22.71 ? 449 GLU A CD 1 ATOM 3473 O OE1 . GLU A 1 449 ? -1.564 38.429 37.692 1.00 16.89 ? 449 GLU A OE1 1 ATOM 3474 O OE2 . GLU A 1 449 ? -1.663 40.583 37.583 1.00 28.18 ? 449 GLU A OE2 1 ATOM 3475 N N . ALA A 1 450 ? -5.141 36.108 41.446 1.00 12.06 ? 450 ALA A N 1 ATOM 3476 C CA . ALA A 1 450 ? -5.869 34.848 41.689 1.00 11.87 ? 450 ALA A CA 1 ATOM 3477 C C . ALA A 1 450 ? -7.016 35.101 42.681 1.00 12.14 ? 450 ALA A C 1 ATOM 3478 O O . ALA A 1 450 ? -8.118 34.582 42.475 1.00 13.05 ? 450 ALA A O 1 ATOM 3479 C CB . ALA A 1 450 ? -4.918 33.812 42.244 1.00 11.96 ? 450 ALA A CB 1 ATOM 3480 N N . VAL A 1 451 ? -6.783 35.922 43.708 1.00 11.86 ? 451 VAL A N 1 ATOM 3481 C CA . VAL A 1 451 ? -7.860 36.275 44.658 1.00 12.30 ? 451 VAL A CA 1 ATOM 3482 C C . VAL A 1 451 ? -8.986 36.989 43.897 1.00 13.26 ? 451 VAL A C 1 ATOM 3483 O O . VAL A 1 451 ? -10.190 36.635 44.067 1.00 12.70 ? 451 VAL A O 1 ATOM 3484 C CB . VAL A 1 451 ? -7.287 37.170 45.784 1.00 11.60 ? 451 VAL A CB 1 ATOM 3485 C CG1 . VAL A 1 451 ? -8.463 37.673 46.671 1.00 12.55 ? 451 VAL A CG1 1 ATOM 3486 C CG2 . VAL A 1 451 ? -6.340 36.308 46.671 1.00 12.64 ? 451 VAL A CG2 1 ATOM 3487 N N . LYS A 1 452 ? -8.621 37.990 43.082 1.00 13.02 ? 452 LYS A N 1 ATOM 3488 C CA . LYS A 1 452 ? -9.653 38.778 42.346 1.00 13.33 ? 452 LYS A CA 1 ATOM 3489 C C . LYS A 1 452 ? -10.441 37.853 41.402 1.00 13.96 ? 452 LYS A C 1 ATOM 3490 O O . LYS A 1 452 ? -11.656 38.047 41.213 1.00 15.58 ? 452 LYS A O 1 ATOM 3491 C CB . LYS A 1 452 ? -9.003 39.914 41.576 1.00 14.46 ? 452 LYS A CB 1 ATOM 3492 C CG . LYS A 1 452 ? -8.431 40.988 42.512 1.00 16.95 ? 452 LYS A CG 1 ATOM 3493 C CD . LYS A 1 452 ? -7.560 41.987 41.729 1.00 18.88 ? 452 LYS A CD 1 ATOM 3494 C CE A LYS A 1 452 ? -7.205 43.205 42.529 0.60 21.36 ? 452 LYS A CE 1 ATOM 3495 C CE B LYS A 1 452 ? -8.285 42.838 40.719 0.40 18.76 ? 452 LYS A CE 1 ATOM 3496 N NZ A LYS A 1 452 ? -6.627 44.210 41.587 0.60 22.34 ? 452 LYS A NZ 1 ATOM 3497 N NZ B LYS A 1 452 ? -7.340 43.903 40.279 0.40 22.16 ? 452 LYS A NZ 1 ATOM 3498 N N . ALA A 1 453 ? -9.782 36.834 40.841 1.00 13.50 ? 453 ALA A N 1 ATOM 3499 C CA . ALA A 1 453 ? -10.457 35.871 39.940 1.00 14.27 ? 453 ALA A CA 1 ATOM 3500 C C . ALA A 1 453 ? -11.326 34.866 40.693 1.00 14.08 ? 453 ALA A C 1 ATOM 3501 O O . ALA A 1 453 ? -12.182 34.222 40.053 1.00 16.69 ? 453 ALA A O 1 ATOM 3502 C CB . ALA A 1 453 ? -9.410 35.133 39.120 1.00 13.60 ? 453 ALA A CB 1 ATOM 3503 N N . ALA A 1 454 ? -11.119 34.709 42.004 1.00 13.37 ? 454 ALA A N 1 ATOM 3504 C CA . ALA A 1 454 ? -11.811 33.683 42.806 1.00 13.76 ? 454 ALA A CA 1 ATOM 3505 C C . ALA A 1 454 ? -13.060 34.177 43.485 1.00 14.04 ? 454 ALA A C 1 ATOM 3506 O O . ALA A 1 454 ? -14.030 33.410 43.642 1.00 16.01 ? 454 ALA A O 1 ATOM 3507 C CB . ALA A 1 454 ? -10.864 33.088 43.855 1.00 14.03 ? 454 ALA A CB 1 ATOM 3508 N N . VAL A 1 455 ? -13.040 35.423 43.944 1.00 13.78 ? 455 VAL A N 1 ATOM 3509 C CA . VAL A 1 455 ? -14.041 35.870 44.912 1.00 13.88 ? 455 VAL A CA 1 ATOM 3510 C C . VAL A 1 455 ? -15.372 36.253 44.242 1.00 14.46 ? 455 VAL A C 1 ATOM 3511 O O . VAL A 1 455 ? -15.446 36.565 43.062 1.00 14.33 ? 455 VAL A O 1 ATOM 3512 C CB . VAL A 1 455 ? -13.543 37.048 45.778 1.00 13.65 ? 455 VAL A CB 1 ATOM 3513 C CG1 . VAL A 1 455 ? -12.397 36.577 46.689 1.00 15.10 ? 455 VAL A CG1 1 ATOM 3514 C CG2 . VAL A 1 455 ? -13.111 38.255 44.926 1.00 14.36 ? 455 VAL A CG2 1 ATOM 3515 N N . ASP A 1 456 ? -16.456 36.225 45.022 1.00 15.54 ? 456 ASP A N 1 ATOM 3516 C CA . ASP A 1 456 ? -17.750 36.656 44.543 1.00 16.25 ? 456 ASP A CA 1 ATOM 3517 C C . ASP A 1 456 ? -17.671 38.058 43.969 1.00 15.96 ? 456 ASP A C 1 ATOM 3518 O O . ASP A 1 456 ? -16.896 38.885 44.459 1.00 15.58 ? 456 ASP A O 1 ATOM 3519 C CB . ASP A 1 456 ? -18.681 36.672 45.764 1.00 17.36 ? 456 ASP A CB 1 ATOM 3520 C CG . ASP A 1 456 ? -20.146 36.898 45.388 1.00 20.17 ? 456 ASP A CG 1 ATOM 3521 O OD1 . ASP A 1 456 ? -20.652 38.041 45.373 1.00 22.32 ? 456 ASP A OD1 1 ATOM 3522 O OD2 . ASP A 1 456 ? -20.791 35.895 45.029 1.00 24.34 ? 456 ASP A OD2 1 ATOM 3523 N N . PRO A 1 457 ? -18.524 38.403 42.995 1.00 16.91 ? 457 PRO A N 1 ATOM 3524 C CA . PRO A 1 457 ? -18.442 39.775 42.462 1.00 16.60 ? 457 PRO A CA 1 ATOM 3525 C C . PRO A 1 457 ? -18.746 40.857 43.496 1.00 17.33 ? 457 PRO A C 1 ATOM 3526 O O . PRO A 1 457 ? -18.282 41.971 43.321 1.00 17.43 ? 457 PRO A O 1 ATOM 3527 C CB . PRO A 1 457 ? -19.514 39.793 41.319 1.00 18.66 ? 457 PRO A CB 1 ATOM 3528 C CG . PRO A 1 457 ? -20.383 38.648 41.676 1.00 18.28 ? 457 PRO A CG 1 ATOM 3529 C CD . PRO A 1 457 ? -19.469 37.584 42.224 1.00 17.73 ? 457 PRO A CD 1 ATOM 3530 N N . SER A 1 458 ? -19.510 40.543 44.541 1.00 16.94 ? 458 SER A N 1 ATOM 3531 C CA . SER A 1 458 ? -19.781 41.557 45.589 1.00 16.86 ? 458 SER A CA 1 ATOM 3532 C C . SER A 1 458 ? -18.579 41.821 46.530 1.00 17.28 ? 458 SER A C 1 ATOM 3533 O O . SER A 1 458 ? -18.611 42.778 47.320 1.00 19.32 ? 458 SER A O 1 ATOM 3534 C CB . SER A 1 458 ? -21.041 41.210 46.410 1.00 19.12 ? 458 SER A CB 1 ATOM 3535 O OG . SER A 1 458 ? -20.841 40.066 47.215 1.00 20.45 ? 458 SER A OG 1 ATOM 3536 N N . THR A 1 459 ? -17.552 40.962 46.492 1.00 16.13 ? 459 THR A N 1 ATOM 3537 C CA . THR A 1 459 ? -16.429 41.100 47.407 1.00 15.58 ? 459 THR A CA 1 ATOM 3538 C C . THR A 1 459 ? -15.455 42.151 46.931 1.00 16.38 ? 459 THR A C 1 ATOM 3539 O O . THR A 1 459 ? -14.885 42.032 45.846 1.00 16.77 ? 459 THR A O 1 ATOM 3540 C CB . THR A 1 459 ? -15.697 39.754 47.519 1.00 14.98 ? 459 THR A CB 1 ATOM 3541 O OG1 . THR A 1 459 ? -16.628 38.774 48.033 1.00 15.08 ? 459 THR A OG1 1 ATOM 3542 C CG2 . THR A 1 459 ? -14.473 39.876 48.452 1.00 14.08 ? 459 THR A CG2 1 ATOM 3543 N N . VAL A 1 460 ? -15.202 43.165 47.753 1.00 15.55 ? 460 VAL A N 1 ATOM 3544 C CA . VAL A 1 460 ? -14.233 44.221 47.395 1.00 15.65 ? 460 VAL A CA 1 ATOM 3545 C C . VAL A 1 460 ? -12.859 43.792 47.862 1.00 16.55 ? 460 VAL A C 1 ATOM 3546 O O . VAL A 1 460 ? -12.677 43.448 49.023 1.00 17.18 ? 460 VAL A O 1 ATOM 3547 C CB . VAL A 1 460 ? -14.623 45.562 48.055 1.00 15.91 ? 460 VAL A CB 1 ATOM 3548 C CG1 . VAL A 1 460 ? -13.578 46.626 47.764 1.00 16.82 ? 460 VAL A CG1 1 ATOM 3549 C CG2 . VAL A 1 460 ? -15.969 46.038 47.490 1.00 16.46 ? 460 VAL A CG2 1 ATOM 3550 N N . VAL A 1 461 ? -11.899 43.777 46.948 1.00 15.35 ? 461 VAL A N 1 ATOM 3551 C CA . VAL A 1 461 ? -10.541 43.321 47.244 1.00 15.14 ? 461 VAL A CA 1 ATOM 3552 C C . VAL A 1 461 ? -9.661 44.570 47.278 1.00 16.27 ? 461 VAL A C 1 ATOM 3553 O O . VAL A 1 461 ? -9.543 45.314 46.270 1.00 18.74 ? 461 VAL A O 1 ATOM 3554 C CB . VAL A 1 461 ? -10.032 42.365 46.145 1.00 15.35 ? 461 VAL A CB 1 ATOM 3555 C CG1 . VAL A 1 461 ? -8.615 41.913 46.476 1.00 15.85 ? 461 VAL A CG1 1 ATOM 3556 C CG2 . VAL A 1 461 ? -10.910 41.136 46.053 1.00 16.06 ? 461 VAL A CG2 1 ATOM 3557 N N . VAL A 1 462 ? -9.041 44.819 48.435 1.00 15.70 ? 462 VAL A N 1 ATOM 3558 C CA . VAL A 1 462 ? -8.086 45.923 48.579 1.00 15.48 ? 462 VAL A CA 1 ATOM 3559 C C . VAL A 1 462 ? -6.671 45.350 48.626 1.00 15.89 ? 462 VAL A C 1 ATOM 3560 O O . VAL A 1 462 ? -6.429 44.375 49.358 1.00 16.38 ? 462 VAL A O 1 ATOM 3561 C CB . VAL A 1 462 ? -8.371 46.684 49.873 1.00 15.51 ? 462 VAL A CB 1 ATOM 3562 C CG1 . VAL A 1 462 ? -7.329 47.793 50.053 1.00 16.93 ? 462 VAL A CG1 1 ATOM 3563 C CG2 . VAL A 1 462 ? -9.793 47.257 49.813 1.00 16.53 ? 462 VAL A CG2 1 ATOM 3564 N N . PHE A 1 463 ? -5.762 45.894 47.810 1.00 15.95 ? 463 PHE A N 1 ATOM 3565 C CA . PHE A 1 463 ? -4.325 45.575 47.868 1.00 15.54 ? 463 PHE A CA 1 ATOM 3566 C C . PHE A 1 463 ? -3.533 46.661 48.578 1.00 16.43 ? 463 PHE A C 1 ATOM 3567 O O . PHE A 1 463 ? -3.665 47.864 48.227 1.00 18.41 ? 463 PHE A O 1 ATOM 3568 C CB . PHE A 1 463 ? -3.736 45.394 46.460 1.00 15.81 ? 463 PHE A CB 1 ATOM 3569 C CG . PHE A 1 463 ? -2.260 45.176 46.453 1.00 16.79 ? 463 PHE A CG 1 ATOM 3570 C CD1 . PHE A 1 463 ? -1.680 44.086 47.094 1.00 16.22 ? 463 PHE A CD1 1 ATOM 3571 C CD2 . PHE A 1 463 ? -1.430 46.073 45.809 1.00 18.90 ? 463 PHE A CD2 1 ATOM 3572 C CE1 . PHE A 1 463 ? -0.292 43.887 47.097 1.00 17.88 ? 463 PHE A CE1 1 ATOM 3573 C CE2 . PHE A 1 463 ? -0.032 45.860 45.794 1.00 20.91 ? 463 PHE A CE2 1 ATOM 3574 C CZ . PHE A 1 463 ? 0.551 44.774 46.443 1.00 19.11 ? 463 PHE A CZ 1 ATOM 3575 N N . ALA A 1 464 ? -2.699 46.234 49.532 1.00 16.02 ? 464 ALA A N 1 ATOM 3576 C CA . ALA A 1 464 ? -1.724 47.169 50.149 1.00 15.89 ? 464 ALA A CA 1 ATOM 3577 C C . ALA A 1 464 ? -0.462 46.355 50.382 1.00 17.26 ? 464 ALA A C 1 ATOM 3578 O O . ALA A 1 464 ? -0.487 45.368 51.143 1.00 17.87 ? 464 ALA A O 1 ATOM 3579 C CB . ALA A 1 464 ? -2.270 47.742 51.470 1.00 17.85 ? 464 ALA A CB 1 ATOM 3580 N N . GLU A 1 465 ? 0.663 46.765 49.771 1.00 16.70 ? 465 GLU A N 1 ATOM 3581 C CA . GLU A 1 465 ? 1.879 45.952 49.901 1.00 18.31 ? 465 GLU A CA 1 ATOM 3582 C C . GLU A 1 465 ? 2.382 45.846 51.340 1.00 18.47 ? 465 GLU A C 1 ATOM 3583 O O . GLU A 1 465 ? 2.699 44.753 51.848 1.00 19.39 ? 465 GLU A O 1 ATOM 3584 C CB . GLU A 1 465 ? 2.978 46.495 49.002 1.00 20.68 ? 465 GLU A CB 1 ATOM 3585 C CG . GLU A 1 465 ? 4.190 45.598 49.067 1.00 23.79 ? 465 GLU A CG 1 ATOM 3586 C CD . GLU A 1 465 ? 5.224 45.936 48.031 1.00 28.68 ? 465 GLU A CD 1 ATOM 3587 O OE1 . GLU A 1 465 ? 4.879 46.547 46.983 1.00 30.00 ? 465 GLU A OE1 1 ATOM 3588 O OE2 . GLU A 1 465 ? 6.369 45.508 48.293 1.00 29.29 ? 465 GLU A OE2 1 ATOM 3589 N N . ASN A 1 466 ? 2.461 46.999 52.025 1.00 17.32 ? 466 ASN A N 1 ATOM 3590 C CA . ASN A 1 466 ? 2.961 47.035 53.391 1.00 19.49 ? 466 ASN A CA 1 ATOM 3591 C C . ASN A 1 466 ? 2.145 48.001 54.254 1.00 19.70 ? 466 ASN A C 1 ATOM 3592 O O . ASN A 1 466 ? 2.644 49.086 54.659 1.00 20.34 ? 466 ASN A O 1 ATOM 3593 C CB A ASN A 1 466 ? 4.428 47.463 53.327 0.50 20.54 ? 466 ASN A CB 1 ATOM 3594 C CB B ASN A 1 466 ? 4.436 47.452 53.483 0.50 18.12 ? 466 ASN A CB 1 ATOM 3595 C CG A ASN A 1 466 ? 5.151 47.234 54.613 0.50 22.08 ? 466 ASN A CG 1 ATOM 3596 C CG B ASN A 1 466 ? 5.374 46.426 52.923 0.50 17.61 ? 466 ASN A CG 1 ATOM 3597 O OD1 A ASN A 1 466 ? 6.184 47.866 54.882 0.50 25.12 ? 466 ASN A OD1 1 ATOM 3598 O OD1 B ASN A 1 466 ? 5.445 45.278 53.404 0.50 17.05 ? 466 ASN A OD1 1 ATOM 3599 N ND2 A ASN A 1 466 ? 4.625 46.337 55.427 0.50 21.78 ? 466 ASN A ND2 1 ATOM 3600 N ND2 B ASN A 1 466 ? 6.101 46.819 51.888 0.50 18.71 ? 466 ASN A ND2 1 ATOM 3601 N N . PRO A 1 467 ? 0.886 47.638 54.568 1.00 18.47 ? 467 PRO A N 1 ATOM 3602 C CA . PRO A 1 467 ? 0.065 48.520 55.366 1.00 19.24 ? 467 PRO A CA 1 ATOM 3603 C C . PRO A 1 467 ? 0.508 48.597 56.827 1.00 20.07 ? 467 PRO A C 1 ATOM 3604 O O . PRO A 1 467 ? 1.053 47.634 57.396 1.00 21.14 ? 467 PRO A O 1 ATOM 3605 C CB . PRO A 1 467 ? -1.330 47.854 55.324 1.00 19.33 ? 467 PRO A CB 1 ATOM 3606 C CG . PRO A 1 467 ? -1.031 46.396 55.110 1.00 18.73 ? 467 PRO A CG 1 ATOM 3607 C CD . PRO A 1 467 ? 0.189 46.378 54.232 1.00 18.73 ? 467 PRO A CD 1 ATOM 3608 N N . ASP A 1 468 ? 0.264 49.746 57.433 1.00 24.03 ? 468 ASP A N 1 ATOM 3609 C CA . ASP A 1 468 ? 0.463 49.804 58.852 1.00 24.65 ? 468 ASP A CA 1 ATOM 3610 C C . ASP A 1 468 ? -0.747 49.284 59.614 1.00 23.81 ? 468 ASP A C 1 ATOM 3611 O O . ASP A 1 468 ? -1.838 49.014 59.038 1.00 23.00 ? 468 ASP A O 1 ATOM 3612 C CB . ASP A 1 468 ? 0.948 51.195 59.317 1.00 27.94 ? 468 ASP A CB 1 ATOM 3613 C CG . ASP A 1 468 ? -0.099 52.284 59.204 1.00 29.95 ? 468 ASP A CG 1 ATOM 3614 O OD1 . ASP A 1 468 ? 0.323 53.477 59.284 1.00 33.46 ? 468 ASP A OD1 1 ATOM 3615 O OD2 . ASP A 1 468 ? -1.325 52.042 59.110 1.00 27.34 ? 468 ASP A OD2 1 ATOM 3616 N N . ALA A 1 469 ? -0.556 49.096 60.905 1.00 23.60 ? 469 ALA A N 1 ATOM 3617 C CA . ALA A 1 469 ? -1.543 48.466 61.731 1.00 23.18 ? 469 ALA A CA 1 ATOM 3618 C C . ALA A 1 469 ? -2.855 49.278 61.742 1.00 22.97 ? 469 ALA A C 1 ATOM 3619 O O . ALA A 1 469 ? -3.952 48.733 61.764 1.00 21.96 ? 469 ALA A O 1 ATOM 3620 C CB . ALA A 1 469 ? -0.991 48.342 63.147 1.00 26.88 ? 469 ALA A CB 1 ATOM 3621 N N . GLU A 1 470 ? -2.730 50.602 61.758 1.00 24.47 ? 470 GLU A N 1 ATOM 3622 C CA . GLU A 1 470 ? -3.922 51.448 61.811 1.00 23.33 ? 470 GLU A CA 1 ATOM 3623 C C . GLU A 1 470 ? -4.770 51.333 60.535 1.00 21.60 ? 470 GLU A C 1 ATOM 3624 O O . GLU A 1 470 ? -5.991 51.304 60.596 1.00 21.61 ? 470 GLU A O 1 ATOM 3625 C CB . GLU A 1 470 ? -3.506 52.912 62.063 1.00 25.49 ? 470 GLU A CB 1 ATOM 3626 C CG . GLU A 1 470 ? -4.690 53.854 62.016 1.00 34.23 ? 470 GLU A CG 1 ATOM 3627 C CD . GLU A 1 470 ? -4.307 55.322 62.049 1.00 37.22 ? 470 GLU A CD 1 ATOM 3628 O OE1 . GLU A 1 470 ? -5.153 56.126 61.561 1.00 34.84 ? 470 GLU A OE1 1 ATOM 3629 O OE2 . GLU A 1 470 ? -3.192 55.645 62.553 1.00 34.64 ? 470 GLU A OE2 1 ATOM 3630 N N . PHE A 1 471 ? -4.107 51.274 59.382 1.00 20.81 ? 471 PHE A N 1 ATOM 3631 C CA . PHE A 1 471 ? -4.811 51.067 58.106 1.00 20.06 ? 471 PHE A CA 1 ATOM 3632 C C . PHE A 1 471 ? -5.650 49.772 58.160 1.00 19.06 ? 471 PHE A C 1 ATOM 3633 O O . PHE A 1 471 ? -6.813 49.755 57.745 1.00 20.01 ? 471 PHE A O 1 ATOM 3634 C CB . PHE A 1 471 ? -3.806 50.962 56.951 1.00 21.18 ? 471 PHE A CB 1 ATOM 3635 C CG . PHE A 1 471 ? -4.405 50.640 55.614 1.00 22.68 ? 471 PHE A CG 1 ATOM 3636 C CD1 . PHE A 1 471 ? -4.619 49.329 55.239 1.00 21.90 ? 471 PHE A CD1 1 ATOM 3637 C CD2 . PHE A 1 471 ? -4.684 51.636 54.697 1.00 25.80 ? 471 PHE A CD2 1 ATOM 3638 C CE1 . PHE A 1 471 ? -5.142 49.031 53.986 1.00 25.38 ? 471 PHE A CE1 1 ATOM 3639 C CE2 . PHE A 1 471 ? -5.183 51.346 53.442 1.00 27.12 ? 471 PHE A CE2 1 ATOM 3640 C CZ . PHE A 1 471 ? -5.433 50.030 53.089 1.00 26.38 ? 471 PHE A CZ 1 ATOM 3641 N N . VAL A 1 472 ? -5.033 48.696 58.652 1.00 18.71 ? 472 VAL A N 1 ATOM 3642 C CA . VAL A 1 472 ? -5.794 47.441 58.717 1.00 17.24 ? 472 VAL A CA 1 ATOM 3643 C C . VAL A 1 472 ? -6.980 47.479 59.705 1.00 17.41 ? 472 VAL A C 1 ATOM 3644 O O . VAL A 1 472 ? -8.083 47.046 59.374 1.00 18.21 ? 472 VAL A O 1 ATOM 3645 C CB . VAL A 1 472 ? -4.842 46.271 59.067 1.00 17.00 ? 472 VAL A CB 1 ATOM 3646 C CG1 . VAL A 1 472 ? -5.576 44.932 59.084 1.00 19.38 ? 472 VAL A CG1 1 ATOM 3647 C CG2 . VAL A 1 472 ? -3.650 46.289 58.093 1.00 18.93 ? 472 VAL A CG2 1 ATOM 3648 N N . LYS A 1 473 ? -6.749 48.042 60.898 1.00 19.14 ? 473 LYS A N 1 ATOM 3649 C CA . LYS A 1 473 ? -7.792 48.111 61.933 1.00 19.63 ? 473 LYS A CA 1 ATOM 3650 C C . LYS A 1 473 ? -8.963 48.967 61.490 1.00 19.11 ? 473 LYS A C 1 ATOM 3651 O O . LYS A 1 473 ? -10.095 48.720 61.888 1.00 20.61 ? 473 LYS A O 1 ATOM 3652 C CB . LYS A 1 473 ? -7.223 48.694 63.211 1.00 21.61 ? 473 LYS A CB 1 ATOM 3653 C CG . LYS A 1 473 ? -6.455 47.667 64.022 1.00 27.54 ? 473 LYS A CG 1 ATOM 3654 C CD . LYS A 1 473 ? -5.836 48.359 65.233 1.00 32.37 ? 473 LYS A CD 1 ATOM 3655 C CE . LYS A 1 473 ? -4.776 47.470 65.867 1.00 39.02 ? 473 LYS A CE 1 ATOM 3656 N NZ . LYS A 1 473 ? -3.921 48.251 66.809 1.00 46.42 ? 473 LYS A NZ 1 ATOM 3657 N N . SER A 1 474 ? -8.681 49.976 60.647 1.00 19.15 ? 474 SER A N 1 ATOM 3658 C CA . SER A 1 474 ? -9.739 50.897 60.222 1.00 19.67 ? 474 SER A CA 1 ATOM 3659 C C . SER A 1 474 ? -10.434 50.494 58.921 1.00 19.95 ? 474 SER A C 1 ATOM 3660 O O . SER A 1 474 ? -11.408 51.130 58.500 1.00 20.24 ? 474 SER A O 1 ATOM 3661 C CB . SER A 1 474 ? -9.190 52.334 60.065 1.00 20.44 ? 474 SER A CB 1 ATOM 3662 O OG A SER A 1 474 ? -8.472 52.792 61.213 0.60 22.70 ? 474 SER A OG 1 ATOM 3663 O OG B SER A 1 474 ? -8.391 52.516 58.936 0.40 18.22 ? 474 SER A OG 1 ATOM 3664 N N . GLY A 1 475 ? -9.986 49.397 58.294 1.00 19.68 ? 475 GLY A N 1 ATOM 3665 C CA . GLY A 1 475 ? -10.450 49.183 56.927 1.00 20.55 ? 475 GLY A CA 1 ATOM 3666 C C . GLY A 1 475 ? -11.708 48.391 56.721 1.00 19.30 ? 475 GLY A C 1 ATOM 3667 O O . GLY A 1 475 ? -12.128 48.211 55.567 1.00 21.92 ? 475 GLY A O 1 ATOM 3668 N N . GLY A 1 476 ? -12.296 47.873 57.798 1.00 18.33 ? 476 GLY A N 1 ATOM 3669 C CA . GLY A 1 476 ? -13.543 47.112 57.701 1.00 18.38 ? 476 GLY A CA 1 ATOM 3670 C C . GLY A 1 476 ? -13.391 45.804 56.926 1.00 18.51 ? 476 GLY A C 1 ATOM 3671 O O . GLY A 1 476 ? -14.321 45.400 56.197 1.00 19.17 ? 476 GLY A O 1 ATOM 3672 N N . PHE A 1 477 ? -12.247 45.172 57.139 1.00 17.86 ? 477 PHE A N 1 ATOM 3673 C CA . PHE A 1 477 ? -11.962 43.911 56.441 1.00 16.58 ? 477 PHE A CA 1 ATOM 3674 C C . PHE A 1 477 ? -12.562 42.724 57.163 1.00 16.35 ? 477 PHE A C 1 ATOM 3675 O O . PHE A 1 477 ? -12.589 42.674 58.408 1.00 17.34 ? 477 PHE A O 1 ATOM 3676 C CB . PHE A 1 477 ? -10.441 43.725 56.311 1.00 15.62 ? 477 PHE A CB 1 ATOM 3677 C CG . PHE A 1 477 ? -9.779 44.802 55.492 1.00 15.18 ? 477 PHE A CG 1 ATOM 3678 C CD1 . PHE A 1 477 ? -10.096 44.933 54.130 1.00 15.91 ? 477 PHE A CD1 1 ATOM 3679 C CD2 . PHE A 1 477 ? -8.849 45.672 56.068 1.00 16.23 ? 477 PHE A CD2 1 ATOM 3680 C CE1 . PHE A 1 477 ? -9.473 45.913 53.356 1.00 15.80 ? 477 PHE A CE1 1 ATOM 3681 C CE2 . PHE A 1 477 ? -8.219 46.669 55.295 1.00 16.33 ? 477 PHE A CE2 1 ATOM 3682 C CZ . PHE A 1 477 ? -8.546 46.782 53.936 1.00 16.18 ? 477 PHE A CZ 1 ATOM 3683 N N . SER A 1 478 ? -12.972 41.711 56.370 1.00 16.21 ? 478 SER A N 1 ATOM 3684 C CA . SER A 1 478 ? -13.422 40.428 56.943 1.00 14.91 ? 478 SER A CA 1 ATOM 3685 C C . SER A 1 478 ? -12.291 39.516 57.330 1.00 15.83 ? 478 SER A C 1 ATOM 3686 O O . SER A 1 478 ? -12.351 38.781 58.318 1.00 16.31 ? 478 SER A O 1 ATOM 3687 C CB . SER A 1 478 ? -14.351 39.736 55.940 1.00 15.73 ? 478 SER A CB 1 ATOM 3688 O OG . SER A 1 478 ? -15.591 40.447 55.788 1.00 17.81 ? 478 SER A OG 1 ATOM 3689 N N . TYR A 1 479 ? -11.207 39.616 56.553 1.00 14.29 ? 479 TYR A N 1 ATOM 3690 C CA . TYR A 1 479 ? -9.995 38.814 56.765 1.00 14.82 ? 479 TYR A CA 1 ATOM 3691 C C . TYR A 1 479 ? -8.942 39.365 55.813 1.00 14.07 ? 479 TYR A C 1 ATOM 3692 O O . TYR A 1 479 ? -9.250 40.203 54.945 1.00 14.19 ? 479 TYR A O 1 ATOM 3693 C CB . TYR A 1 479 ? -10.203 37.284 56.499 1.00 15.62 ? 479 TYR A CB 1 ATOM 3694 C CG . TYR A 1 479 ? -10.795 36.940 55.130 1.00 15.71 ? 479 TYR A CG 1 ATOM 3695 C CD1 . TYR A 1 479 ? -9.988 36.930 53.972 1.00 15.84 ? 479 TYR A CD1 1 ATOM 3696 C CD2 . TYR A 1 479 ? -12.180 36.633 54.974 1.00 16.13 ? 479 TYR A CD2 1 ATOM 3697 C CE1 . TYR A 1 479 ? -10.526 36.601 52.722 1.00 16.12 ? 479 TYR A CE1 1 ATOM 3698 C CE2 . TYR A 1 479 ? -12.728 36.353 53.719 1.00 17.01 ? 479 TYR A CE2 1 ATOM 3699 C CZ . TYR A 1 479 ? -11.888 36.297 52.596 1.00 16.14 ? 479 TYR A CZ 1 ATOM 3700 O OH . TYR A 1 479 ? -12.381 36.038 51.346 1.00 17.38 ? 479 TYR A OH 1 ATOM 3701 N N . ALA A 1 480 ? -7.717 38.883 56.004 1.00 14.11 ? 480 ALA A N 1 ATOM 3702 C CA . ALA A 1 480 ? -6.586 39.242 55.131 1.00 13.35 ? 480 ALA A CA 1 ATOM 3703 C C . ALA A 1 480 ? -5.848 38.022 54.684 1.00 13.66 ? 480 ALA A C 1 ATOM 3704 O O . ALA A 1 480 ? -5.739 37.057 55.430 1.00 14.39 ? 480 ALA A O 1 ATOM 3705 C CB . ALA A 1 480 ? -5.649 40.170 55.892 1.00 14.20 ? 480 ALA A CB 1 ATOM 3706 N N . ILE A 1 481 ? -5.294 38.113 53.461 1.00 13.21 ? 481 ILE A N 1 ATOM 3707 C CA . ILE A 1 481 ? -4.321 37.142 52.954 1.00 13.48 ? 481 ILE A CA 1 ATOM 3708 C C . ILE A 1 481 ? -3.037 37.941 52.780 1.00 13.85 ? 481 ILE A C 1 ATOM 3709 O O . ILE A 1 481 ? -3.023 38.946 52.057 1.00 14.21 ? 481 ILE A O 1 ATOM 3710 C CB . ILE A 1 481 ? -4.798 36.616 51.585 1.00 13.26 ? 481 ILE A CB 1 ATOM 3711 C CG1 . ILE A 1 481 ? -6.101 35.796 51.784 1.00 14.48 ? 481 ILE A CG1 1 ATOM 3712 C CG2 . ILE A 1 481 ? -3.661 35.794 50.936 1.00 13.45 ? 481 ILE A CG2 1 ATOM 3713 C CD1 . ILE A 1 481 ? -6.838 35.570 50.470 1.00 15.61 ? 481 ILE A CD1 1 ATOM 3714 N N . VAL A 1 482 ? -1.979 37.525 53.474 1.00 13.42 ? 482 VAL A N 1 ATOM 3715 C CA . VAL A 1 482 ? -0.694 38.237 53.455 1.00 13.06 ? 482 VAL A CA 1 ATOM 3716 C C . VAL A 1 482 ? 0.394 37.275 53.000 1.00 13.47 ? 482 VAL A C 1 ATOM 3717 O O . VAL A 1 482 ? 0.579 36.194 53.575 1.00 14.29 ? 482 VAL A O 1 ATOM 3718 C CB . VAL A 1 482 ? -0.308 38.851 54.839 1.00 14.11 ? 482 VAL A CB 1 ATOM 3719 C CG1 A VAL A 1 482 ? -0.466 37.851 55.972 0.60 13.91 ? 482 VAL A CG1 1 ATOM 3720 C CG1 B VAL A 1 482 ? 0.718 39.962 54.625 0.40 12.99 ? 482 VAL A CG1 1 ATOM 3721 C CG2 A VAL A 1 482 ? 1.104 39.456 54.844 0.60 13.25 ? 482 VAL A CG2 1 ATOM 3722 C CG2 B VAL A 1 482 ? -1.479 39.379 55.571 0.40 13.52 ? 482 VAL A CG2 1 ATOM 3723 N N . ALA A 1 483 ? 1.100 37.669 51.948 1.00 12.56 ? 483 ALA A N 1 ATOM 3724 C CA . ALA A 1 483 ? 2.118 36.791 51.343 1.00 12.64 ? 483 ALA A CA 1 ATOM 3725 C C . ALA A 1 483 ? 3.465 37.482 51.433 1.00 13.44 ? 483 ALA A C 1 ATOM 3726 O O . ALA A 1 483 ? 3.638 38.630 50.985 1.00 13.45 ? 483 ALA A O 1 ATOM 3727 C CB . ALA A 1 483 ? 1.767 36.545 49.873 1.00 14.18 ? 483 ALA A CB 1 ATOM 3728 N N . VAL A 1 484 ? 4.424 36.757 52.007 1.00 13.03 ? 484 VAL A N 1 ATOM 3729 C CA . VAL A 1 484 ? 5.798 37.240 52.236 1.00 13.28 ? 484 VAL A CA 1 ATOM 3730 C C . VAL A 1 484 ? 6.763 36.070 52.034 1.00 13.10 ? 484 VAL A C 1 ATOM 3731 O O . VAL A 1 484 ? 6.354 34.907 51.852 1.00 13.77 ? 484 VAL A O 1 ATOM 3732 C CB . VAL A 1 484 ? 5.969 37.825 53.675 1.00 13.89 ? 484 VAL A CB 1 ATOM 3733 C CG1 . VAL A 1 484 ? 5.037 39.033 53.859 1.00 14.65 ? 484 VAL A CG1 1 ATOM 3734 C CG2 . VAL A 1 484 ? 5.708 36.737 54.728 1.00 14.74 ? 484 VAL A CG2 1 ATOM 3735 N N . GLY A 1 485 ? 8.075 36.342 52.059 1.00 14.14 ? 485 GLY A N 1 ATOM 3736 C CA . GLY A 1 485 ? 9.032 35.235 52.005 1.00 13.36 ? 485 GLY A CA 1 ATOM 3737 C C . GLY A 1 485 ? 10.374 35.621 51.412 1.00 13.91 ? 485 GLY A C 1 ATOM 3738 O O . GLY A 1 485 ? 10.802 36.801 51.496 1.00 14.84 ? 485 GLY A O 1 ATOM 3739 N N . GLU A 1 486 ? 11.036 34.619 50.838 1.00 13.57 ? 486 GLU A N 1 ATOM 3740 C CA . GLU A 1 486 ? 12.402 34.808 50.293 1.00 13.56 ? 486 GLU A CA 1 ATOM 3741 C C . GLU A 1 486 ? 12.377 35.499 48.936 1.00 14.46 ? 486 GLU A C 1 ATOM 3742 O O . GLU A 1 486 ? 11.369 35.410 48.185 1.00 14.89 ? 486 GLU A O 1 ATOM 3743 C CB . GLU A 1 486 ? 13.055 33.446 50.126 1.00 13.28 ? 486 GLU A CB 1 ATOM 3744 C CG . GLU A 1 486 ? 13.315 32.704 51.450 1.00 14.92 ? 486 GLU A CG 1 ATOM 3745 C CD . GLU A 1 486 ? 14.244 31.543 51.255 1.00 14.85 ? 486 GLU A CD 1 ATOM 3746 O OE1 . GLU A 1 486 ? 13.938 30.579 50.532 1.00 15.51 ? 486 GLU A OE1 1 ATOM 3747 O OE2 . GLU A 1 486 ? 15.384 31.608 51.850 1.00 16.58 ? 486 GLU A OE2 1 ATOM 3748 N N . HIS A 1 487 ? 13.457 36.188 48.629 1.00 15.14 ? 487 HIS A N 1 ATOM 3749 C CA . HIS A 1 487 ? 13.644 36.735 47.264 1.00 15.86 ? 487 HIS A CA 1 ATOM 3750 C C . HIS A 1 487 ? 14.276 35.661 46.419 1.00 15.33 ? 487 HIS A C 1 ATOM 3751 O O . HIS A 1 487 ? 14.746 34.683 46.953 1.00 15.44 ? 487 HIS A O 1 ATOM 3752 C CB . HIS A 1 487 ? 14.476 38.025 47.292 1.00 17.62 ? 487 HIS A CB 1 ATOM 3753 C CG . HIS A 1 487 ? 13.827 39.142 48.053 1.00 19.26 ? 487 HIS A CG 1 ATOM 3754 N ND1 . HIS A 1 487 ? 14.555 40.196 48.567 1.00 25.72 ? 487 HIS A ND1 1 ATOM 3755 C CD2 . HIS A 1 487 ? 12.550 39.328 48.458 1.00 21.63 ? 487 HIS A CD2 1 ATOM 3756 C CE1 . HIS A 1 487 ? 13.729 41.027 49.193 1.00 23.54 ? 487 HIS A CE1 1 ATOM 3757 N NE2 . HIS A 1 487 ? 12.507 40.530 49.148 1.00 23.25 ? 487 HIS A NE2 1 ATOM 3758 N N . PRO A 1 488 ? 14.237 35.809 45.081 1.00 14.75 ? 488 PRO A N 1 ATOM 3759 C CA . PRO A 1 488 ? 14.782 34.744 44.222 1.00 14.98 ? 488 PRO A CA 1 ATOM 3760 C C . PRO A 1 488 ? 16.291 34.631 44.391 1.00 16.34 ? 488 PRO A C 1 ATOM 3761 O O . PRO A 1 488 ? 16.991 35.658 44.557 1.00 16.32 ? 488 PRO A O 1 ATOM 3762 C CB . PRO A 1 488 ? 14.446 35.264 42.817 1.00 15.36 ? 488 PRO A CB 1 ATOM 3763 C CG . PRO A 1 488 ? 13.189 36.084 43.000 1.00 15.38 ? 488 PRO A CG 1 ATOM 3764 C CD . PRO A 1 488 ? 13.467 36.806 44.316 1.00 15.45 ? 488 PRO A CD 1 ATOM 3765 N N . TYR A 1 489 ? 16.774 33.398 44.337 1.00 16.06 ? 489 TYR A N 1 ATOM 3766 C CA . TYR A 1 489 ? 18.226 33.182 44.451 1.00 16.68 ? 489 TYR A CA 1 ATOM 3767 C C . TYR A 1 489 ? 18.617 31.838 43.862 1.00 17.58 ? 489 TYR A C 1 ATOM 3768 O O . TYR A 1 489 ? 17.766 30.969 43.647 1.00 16.86 ? 489 TYR A O 1 ATOM 3769 C CB . TYR A 1 489 ? 18.662 33.226 45.947 1.00 16.98 ? 489 TYR A CB 1 ATOM 3770 C CG . TYR A 1 489 ? 17.947 32.208 46.804 1.00 16.31 ? 489 TYR A CG 1 ATOM 3771 C CD1 . TYR A 1 489 ? 18.343 30.867 46.815 1.00 17.05 ? 489 TYR A CD1 1 ATOM 3772 C CD2 . TYR A 1 489 ? 16.796 32.581 47.534 1.00 15.59 ? 489 TYR A CD2 1 ATOM 3773 C CE1 . TYR A 1 489 ? 17.676 29.912 47.583 1.00 16.12 ? 489 TYR A CE1 1 ATOM 3774 C CE2 . TYR A 1 489 ? 16.101 31.629 48.264 1.00 15.56 ? 489 TYR A CE2 1 ATOM 3775 C CZ . TYR A 1 489 ? 16.525 30.310 48.270 1.00 15.89 ? 489 TYR A CZ 1 ATOM 3776 O OH . TYR A 1 489 ? 15.852 29.345 48.992 1.00 16.15 ? 489 TYR A OH 1 ATOM 3777 N N . THR A 1 490 ? 19.939 31.688 43.663 1.00 18.42 ? 490 THR A N 1 ATOM 3778 C CA . THR A 1 490 ? 20.627 30.423 43.407 1.00 21.69 ? 490 THR A CA 1 ATOM 3779 C C . THR A 1 490 ? 21.784 30.325 44.404 1.00 25.32 ? 490 THR A C 1 ATOM 3780 O O . THR A 1 490 ? 21.978 31.233 45.232 1.00 28.47 ? 490 THR A O 1 ATOM 3781 C CB . THR A 1 490 ? 21.229 30.454 42.013 1.00 22.31 ? 490 THR A CB 1 ATOM 3782 O OG1 . THR A 1 490 ? 22.092 31.611 41.924 1.00 24.68 ? 490 THR A OG1 1 ATOM 3783 C CG2 . THR A 1 490 ? 20.126 30.585 40.983 1.00 21.34 ? 490 THR A CG2 1 ATOM 3784 N N . GLU A 1 491 ? 22.572 29.269 44.350 1.00 28.98 ? 491 GLU A N 1 ATOM 3785 C CA . GLU A 1 491 ? 23.709 29.204 45.286 1.00 42.04 ? 491 GLU A CA 1 ATOM 3786 C C . GLU A 1 491 ? 24.336 30.567 45.695 1.00 51.24 ? 491 GLU A C 1 ATOM 3787 O O . GLU A 1 491 ? 24.406 30.899 46.884 1.00 56.45 ? 491 GLU A O 1 ATOM 3788 C CB . GLU A 1 491 ? 24.802 28.316 44.713 1.00 45.84 ? 491 GLU A CB 1 ATOM 3789 C CG . GLU A 1 491 ? 24.389 27.583 43.452 1.00 52.33 ? 491 GLU A CG 1 ATOM 3790 C CD . GLU A 1 491 ? 24.862 28.269 42.189 1.00 57.51 ? 491 GLU A CD 1 ATOM 3791 O OE1 . GLU A 1 491 ? 25.811 29.099 42.251 1.00 64.20 ? 491 GLU A OE1 1 ATOM 3792 O OE2 . GLU A 1 491 ? 24.299 27.944 41.129 1.00 58.83 ? 491 GLU A OE2 1 ATOM 3793 N N . THR A 1 492 ? 24.811 31.338 44.716 1.00 57.61 ? 492 THR A N 1 ATOM 3794 C CA . THR A 1 492 ? 25.596 32.540 45.019 1.00 66.26 ? 492 THR A CA 1 ATOM 3795 C C . THR A 1 492 ? 24.691 33.732 45.331 1.00 68.92 ? 492 THR A C 1 ATOM 3796 O O . THR A 1 492 ? 24.267 34.460 44.420 1.00 72.79 ? 492 THR A O 1 ATOM 3797 C CB . THR A 1 492 ? 26.590 32.889 43.891 1.00 66.96 ? 492 THR A CB 1 ATOM 3798 O OG1 . THR A 1 492 ? 25.870 33.110 42.675 1.00 64.27 ? 492 THR A OG1 1 ATOM 3799 C CG2 . THR A 1 492 ? 27.612 31.764 43.696 1.00 68.22 ? 492 THR A CG2 1 ATOM 3800 N N . LYS A 1 493 ? 24.452 33.924 46.633 1.00 67.66 ? 493 LYS A N 1 ATOM 3801 C CA . LYS A 1 493 ? 23.419 34.818 47.219 1.00 61.73 ? 493 LYS A CA 1 ATOM 3802 C C . LYS A 1 493 ? 22.320 33.968 47.898 1.00 54.05 ? 493 LYS A C 1 ATOM 3803 O O . LYS A 1 493 ? 21.557 34.469 48.735 1.00 54.03 ? 493 LYS A O 1 ATOM 3804 C CB . LYS A 1 493 ? 22.819 35.800 46.190 1.00 63.13 ? 493 LYS A CB 1 ATOM 3805 C CG . LYS A 1 493 ? 21.564 36.541 46.641 1.00 61.08 ? 493 LYS A CG 1 ATOM 3806 C CD . LYS A 1 493 ? 20.572 36.692 45.500 1.00 60.36 ? 493 LYS A CD 1 ATOM 3807 C CE . LYS A 1 493 ? 19.450 37.657 45.849 1.00 57.80 ? 493 LYS A CE 1 ATOM 3808 N NZ . LYS A 1 493 ? 18.293 37.068 46.591 1.00 45.78 ? 493 LYS A NZ 1 ATOM 3809 N N . GLY A 1 494 ? 22.255 32.684 47.527 1.00 44.72 ? 494 GLY A N 1 ATOM 3810 C CA . GLY A 1 494 ? 21.282 31.765 48.073 1.00 39.30 ? 494 GLY A CA 1 ATOM 3811 C C . GLY A 1 494 ? 21.848 30.941 49.206 1.00 41.44 ? 494 GLY A C 1 ATOM 3812 O O . GLY A 1 494 ? 21.102 30.522 50.133 1.00 27.40 ? 494 GLY A O 1 ATOM 3813 N N . ASP A 1 495 ? 23.166 30.697 49.129 1.00 38.34 ? 495 ASP A N 1 ATOM 3814 C CA . ASP A 1 495 ? 23.854 30.029 50.222 1.00 43.30 ? 495 ASP A CA 1 ATOM 3815 C C . ASP A 1 495 ? 23.770 31.032 51.347 1.00 46.36 ? 495 ASP A C 1 ATOM 3816 O O . ASP A 1 495 ? 24.407 32.107 51.276 1.00 40.80 ? 495 ASP A O 1 ATOM 3817 C CB . ASP A 1 495 ? 25.326 29.741 49.915 1.00 42.42 ? 495 ASP A CB 1 ATOM 3818 C CG . ASP A 1 495 ? 25.525 28.696 48.821 1.00 41.30 ? 495 ASP A CG 1 ATOM 3819 O OD1 . ASP A 1 495 ? 24.702 27.774 48.643 1.00 33.19 ? 495 ASP A OD1 1 ATOM 3820 O OD2 . ASP A 1 495 ? 26.558 28.797 48.133 1.00 45.05 ? 495 ASP A OD2 1 ATOM 3821 N N . ASN A 1 496 ? 22.950 30.691 52.353 1.00 44.21 ? 496 ASN A N 1 ATOM 3822 C CA . ASN A 1 496 ? 22.663 31.624 53.439 1.00 47.12 ? 496 ASN A CA 1 ATOM 3823 C C . ASN A 1 496 ? 22.728 31.046 54.865 1.00 47.55 ? 496 ASN A C 1 ATOM 3824 O O . ASN A 1 496 ? 22.142 29.990 55.170 1.00 43.12 ? 496 ASN A O 1 ATOM 3825 C CB . ASN A 1 496 ? 21.345 32.372 53.205 1.00 47.39 ? 496 ASN A CB 1 ATOM 3826 C CG . ASN A 1 496 ? 21.066 33.389 54.301 1.00 47.82 ? 496 ASN A CG 1 ATOM 3827 O OD1 . ASN A 1 496 ? 20.337 33.093 55.243 1.00 40.52 ? 496 ASN A OD1 1 ATOM 3828 N ND2 . ASN A 1 496 ? 21.705 34.572 54.215 1.00 49.71 ? 496 ASN A ND2 1 ATOM 3829 N N . LEU A 1 497 ? 23.447 31.774 55.718 1.00 50.20 ? 497 LEU A N 1 ATOM 3830 C CA . LEU A 1 497 ? 23.709 31.380 57.082 1.00 51.64 ? 497 LEU A CA 1 ATOM 3831 C C . LEU A 1 497 ? 22.447 31.490 57.969 1.00 46.71 ? 497 LEU A C 1 ATOM 3832 O O . LEU A 1 497 ? 22.165 30.568 58.735 1.00 48.69 ? 497 LEU A O 1 ATOM 3833 C CB . LEU A 1 497 ? 24.906 32.183 57.654 1.00 59.05 ? 497 LEU A CB 1 ATOM 3834 C CG B LEU A 1 497 ? 25.099 33.709 57.436 1.00 64.20 ? 497 LEU A CG 1 ATOM 3835 C CD1 B LEU A 1 497 ? 26.237 34.239 58.310 1.00 63.93 ? 497 LEU A CD1 1 ATOM 3836 C CD2 B LEU A 1 497 ? 25.295 34.133 55.972 1.00 60.28 ? 497 LEU A CD2 1 ATOM 3837 N N . ASN A 1 498 ? 21.686 32.586 57.841 1.00 37.07 ? 498 ASN A N 1 ATOM 3838 C CA . ASN A 1 498 ? 20.675 32.943 58.849 1.00 33.67 ? 498 ASN A CA 1 ATOM 3839 C C . ASN A 1 498 ? 19.237 32.430 58.579 1.00 29.60 ? 498 ASN A C 1 ATOM 3840 O O . ASN A 1 498 ? 18.423 32.298 59.510 1.00 30.68 ? 498 ASN A O 1 ATOM 3841 C CB . ASN A 1 498 ? 20.685 34.461 59.061 1.00 36.97 ? 498 ASN A CB 1 ATOM 3842 C CG . ASN A 1 498 ? 20.334 35.235 57.779 1.00 42.70 ? 498 ASN A CG 1 ATOM 3843 O OD1 . ASN A 1 498 ? 19.152 35.381 57.439 1.00 35.98 ? 498 ASN A OD1 1 ATOM 3844 N ND2 . ASN A 1 498 ? 21.363 35.727 57.056 1.00 41.55 ? 498 ASN A ND2 1 ATOM 3845 N N . LEU A 1 499 ? 18.950 32.150 57.319 1.00 25.97 ? 499 LEU A N 1 ATOM 3846 C CA . LEU A 1 499 ? 17.638 31.640 56.899 1.00 20.97 ? 499 LEU A CA 1 ATOM 3847 C C . LEU A 1 499 ? 16.438 32.388 57.484 1.00 21.18 ? 499 LEU A C 1 ATOM 3848 O O . LEU A 1 499 ? 15.407 31.777 57.786 1.00 19.23 ? 499 LEU A O 1 ATOM 3849 C CB . LEU A 1 499 ? 17.502 30.122 57.106 1.00 20.91 ? 499 LEU A CB 1 ATOM 3850 C CG . LEU A 1 499 ? 18.563 29.226 56.438 1.00 20.72 ? 499 LEU A CG 1 ATOM 3851 C CD1 . LEU A 1 499 ? 18.198 27.768 56.640 1.00 21.43 ? 499 LEU A CD1 1 ATOM 3852 C CD2 . LEU A 1 499 ? 18.699 29.566 54.945 1.00 23.59 ? 499 LEU A CD2 1 ATOM 3853 N N . THR A 1 500 ? 16.574 33.708 57.562 1.00 20.55 ? 500 THR A N 1 ATOM 3854 C CA . THR A 1 500 ? 15.507 34.622 58.016 1.00 22.03 ? 500 THR A CA 1 ATOM 3855 C C . THR A 1 500 ? 15.012 35.398 56.795 1.00 21.74 ? 500 THR A C 1 ATOM 3856 O O . THR A 1 500 ? 15.830 35.958 56.037 1.00 24.40 ? 500 THR A O 1 ATOM 3857 C CB . THR A 1 500 ? 16.034 35.581 59.107 1.00 24.19 ? 500 THR A CB 1 ATOM 3858 O OG1 A THR A 1 500 ? 16.879 36.563 58.500 0.60 27.45 ? 500 THR A OG1 1 ATOM 3859 O OG1 B THR A 1 500 ? 16.359 34.819 60.277 0.40 23.68 ? 500 THR A OG1 1 ATOM 3860 C CG2 A THR A 1 500 ? 16.792 34.830 60.173 0.60 25.14 ? 500 THR A CG2 1 ATOM 3861 C CG2 B THR A 1 500 ? 15.044 36.670 59.514 0.40 20.75 ? 500 THR A CG2 1 ATOM 3862 N N . ILE A 1 501 ? 13.691 35.510 56.620 1.00 20.06 ? 501 ILE A N 1 ATOM 3863 C CA . ILE A 1 501 ? 13.183 36.210 55.435 1.00 20.36 ? 501 ILE A CA 1 ATOM 3864 C C . ILE A 1 501 ? 13.468 37.712 55.490 1.00 20.60 ? 501 ILE A C 1 ATOM 3865 O O . ILE A 1 501 ? 13.551 38.308 56.582 1.00 20.43 ? 501 ILE A O 1 ATOM 3866 C CB . ILE A 1 501 ? 11.684 35.938 55.187 1.00 19.23 ? 501 ILE A CB 1 ATOM 3867 C CG1 . ILE A 1 501 ? 10.804 36.491 56.326 1.00 19.64 ? 501 ILE A CG1 1 ATOM 3868 C CG2 . ILE A 1 501 ? 11.496 34.429 55.014 1.00 20.74 ? 501 ILE A CG2 1 ATOM 3869 C CD1 . ILE A 1 501 ? 9.326 36.528 55.971 1.00 19.43 ? 501 ILE A CD1 1 ATOM 3870 N N . PRO A 1 502 ? 13.637 38.333 54.317 1.00 21.73 ? 502 PRO A N 1 ATOM 3871 C CA . PRO A 1 502 ? 13.892 39.780 54.274 1.00 22.92 ? 502 PRO A CA 1 ATOM 3872 C C . PRO A 1 502 ? 12.767 40.596 54.816 1.00 25.12 ? 502 PRO A C 1 ATOM 3873 O O . PRO A 1 502 ? 11.588 40.246 54.691 1.00 22.39 ? 502 PRO A O 1 ATOM 3874 C CB . PRO A 1 502 ? 14.075 40.087 52.775 1.00 23.56 ? 502 PRO A CB 1 ATOM 3875 C CG . PRO A 1 502 ? 13.689 38.845 52.042 1.00 26.06 ? 502 PRO A CG 1 ATOM 3876 C CD . PRO A 1 502 ? 13.791 37.691 52.995 1.00 22.96 ? 502 PRO A CD 1 ATOM 3877 N N . GLU A 1 503 ? 13.133 41.714 55.415 1.00 24.93 ? 503 GLU A N 1 ATOM 3878 C CA . GLU A 1 503 ? 12.149 42.671 55.847 1.00 26.09 ? 503 GLU A CA 1 ATOM 3879 C C . GLU A 1 503 ? 11.878 43.686 54.762 1.00 27.24 ? 503 GLU A C 1 ATOM 3880 O O . GLU A 1 503 ? 12.739 43.911 53.911 1.00 30.79 ? 503 GLU A O 1 ATOM 3881 C CB . GLU A 1 503 ? 12.551 43.285 57.188 1.00 27.40 ? 503 GLU A CB 1 ATOM 3882 C CG . GLU A 1 503 ? 12.381 42.268 58.325 1.00 27.32 ? 503 GLU A CG 1 ATOM 3883 C CD . GLU A 1 503 ? 10.977 41.653 58.361 1.00 29.09 ? 503 GLU A CD 1 ATOM 3884 O OE1 . GLU A 1 503 ? 10.068 42.473 58.691 1.00 24.64 ? 503 GLU A OE1 1 ATOM 3885 O OE2 . GLU A 1 503 ? 10.812 40.395 58.028 1.00 27.67 ? 503 GLU A OE2 1 ATOM 3886 N N . PRO A 1 504 ? 10.658 44.250 54.716 1.00 27.87 ? 504 PRO A N 1 ATOM 3887 C CA . PRO A 1 504 ? 9.549 43.979 55.624 1.00 26.66 ? 504 PRO A CA 1 ATOM 3888 C C . PRO A 1 504 ? 8.871 42.710 55.089 1.00 26.19 ? 504 PRO A C 1 ATOM 3889 O O . PRO A 1 504 ? 8.641 42.533 53.873 1.00 29.43 ? 504 PRO A O 1 ATOM 3890 C CB . PRO A 1 504 ? 8.663 45.204 55.464 1.00 27.33 ? 504 PRO A CB 1 ATOM 3891 C CG . PRO A 1 504 ? 8.859 45.619 54.047 1.00 28.91 ? 504 PRO A CG 1 ATOM 3892 C CD . PRO A 1 504 ? 10.336 45.343 53.775 1.00 29.73 ? 504 PRO A CD 1 ATOM 3893 N N . GLY A 1 505 ? 8.640 41.807 55.999 1.00 22.04 ? 505 GLY A N 1 ATOM 3894 C CA . GLY A 1 505 ? 7.908 40.572 55.727 1.00 18.06 ? 505 GLY A CA 1 ATOM 3895 C C . GLY A 1 505 ? 7.221 40.244 57.030 1.00 17.51 ? 505 GLY A C 1 ATOM 3896 O O . GLY A 1 505 ? 5.985 40.305 57.104 1.00 16.37 ? 505 GLY A O 1 ATOM 3897 N N . LEU A 1 506 ? 8.034 39.908 58.047 1.00 17.28 ? 506 LEU A N 1 ATOM 3898 C CA . LEU A 1 506 ? 7.482 39.687 59.391 1.00 17.37 ? 506 LEU A CA 1 ATOM 3899 C C . LEU A 1 506 ? 6.726 40.915 59.915 1.00 17.07 ? 506 LEU A C 1 ATOM 3900 O O . LEU A 1 506 ? 5.621 40.778 60.501 1.00 16.92 ? 506 LEU A O 1 ATOM 3901 C CB . LEU A 1 506 ? 8.607 39.293 60.366 1.00 17.15 ? 506 LEU A CB 1 ATOM 3902 C CG . LEU A 1 506 ? 8.142 39.109 61.810 1.00 19.35 ? 506 LEU A CG 1 ATOM 3903 C CD1 . LEU A 1 506 ? 7.133 37.953 61.943 1.00 19.16 ? 506 LEU A CD1 1 ATOM 3904 C CD2 . LEU A 1 506 ? 9.410 38.844 62.642 1.00 19.16 ? 506 LEU A CD2 1 ATOM 3905 N N . SER A 1 507 ? 7.288 42.117 59.760 1.00 17.87 ? 507 SER A N 1 ATOM 3906 C CA . SER A 1 507 ? 6.617 43.331 60.238 1.00 18.02 ? 507 SER A CA 1 ATOM 3907 C C . SER A 1 507 ? 5.242 43.492 59.567 1.00 17.04 ? 507 SER A C 1 ATOM 3908 O O . SER A 1 507 ? 4.287 43.880 60.242 1.00 18.21 ? 507 SER A O 1 ATOM 3909 C CB . SER A 1 507 ? 7.465 44.607 60.010 1.00 20.25 ? 507 SER A CB 1 ATOM 3910 O OG . SER A 1 507 ? 7.723 44.773 58.631 1.00 24.49 ? 507 SER A OG 1 ATOM 3911 N N . THR A 1 508 ? 5.148 43.179 58.256 1.00 16.38 ? 508 THR A N 1 ATOM 3912 C CA . THR A 1 508 ? 3.852 43.286 57.582 1.00 16.91 ? 508 THR A CA 1 ATOM 3913 C C . THR A 1 508 ? 2.854 42.262 58.099 1.00 15.15 ? 508 THR A C 1 ATOM 3914 O O . THR A 1 508 ? 1.668 42.591 58.337 1.00 15.63 ? 508 THR A O 1 ATOM 3915 C CB . THR A 1 508 ? 4.050 43.139 56.076 1.00 18.27 ? 508 THR A CB 1 ATOM 3916 O OG1 . THR A 1 508 ? 4.853 44.262 55.680 1.00 25.15 ? 508 THR A OG1 1 ATOM 3917 C CG2 . THR A 1 508 ? 2.717 43.224 55.303 1.00 17.39 ? 508 THR A CG2 1 ATOM 3918 N N . VAL A 1 509 ? 3.330 41.039 58.329 1.00 16.35 ? 509 VAL A N 1 ATOM 3919 C CA . VAL A 1 509 ? 2.449 39.999 58.857 1.00 15.58 ? 509 VAL A CA 1 ATOM 3920 C C . VAL A 1 509 ? 1.947 40.419 60.255 1.00 16.12 ? 509 VAL A C 1 ATOM 3921 O O . VAL A 1 509 ? 0.759 40.297 60.559 1.00 16.15 ? 509 VAL A O 1 ATOM 3922 C CB . VAL A 1 509 ? 3.182 38.648 58.880 1.00 15.16 ? 509 VAL A CB 1 ATOM 3923 C CG1 . VAL A 1 509 ? 2.406 37.635 59.708 1.00 17.08 ? 509 VAL A CG1 1 ATOM 3924 C CG2 . VAL A 1 509 ? 3.406 38.152 57.446 1.00 15.63 ? 509 VAL A CG2 1 ATOM 3925 N N . GLN A 1 510 ? 2.843 40.932 61.087 1.00 16.02 ? 510 GLN A N 1 ATOM 3926 C CA . GLN A 1 510 ? 2.410 41.344 62.438 1.00 15.78 ? 510 GLN A CA 1 ATOM 3927 C C . GLN A 1 510 ? 1.428 42.521 62.384 1.00 16.34 ? 510 GLN A C 1 ATOM 3928 O O . GLN A 1 510 ? 0.433 42.526 63.124 1.00 16.68 ? 510 GLN A O 1 ATOM 3929 C CB . GLN A 1 510 ? 3.629 41.720 63.287 1.00 17.08 ? 510 GLN A CB 1 ATOM 3930 C CG . GLN A 1 510 ? 4.504 40.510 63.610 1.00 17.77 ? 510 GLN A CG 1 ATOM 3931 C CD . GLN A 1 510 ? 5.867 40.890 64.168 1.00 21.11 ? 510 GLN A CD 1 ATOM 3932 O OE1 . GLN A 1 510 ? 6.404 41.959 63.877 1.00 23.89 ? 510 GLN A OE1 1 ATOM 3933 N NE2 . GLN A 1 510 ? 6.408 40.022 64.976 1.00 21.79 ? 510 GLN A NE2 1 ATOM 3934 N N . ALA A 1 511 ? 1.636 43.489 61.484 1.00 16.92 ? 511 ALA A N 1 ATOM 3935 C CA . ALA A 1 511 ? 0.700 44.616 61.318 1.00 17.62 ? 511 ALA A CA 1 ATOM 3936 C C . ALA A 1 511 ? -0.694 44.165 60.839 1.00 18.32 ? 511 ALA A C 1 ATOM 3937 O O . ALA A 1 511 ? -1.741 44.577 61.384 1.00 18.70 ? 511 ALA A O 1 ATOM 3938 C CB . ALA A 1 511 ? 1.303 45.670 60.381 1.00 18.65 ? 511 ALA A CB 1 ATOM 3939 N N . VAL A 1 512 ? -0.701 43.274 59.839 1.00 15.92 ? 512 VAL A N 1 ATOM 3940 C CA . VAL A 1 512 ? -1.933 42.819 59.232 1.00 15.89 ? 512 VAL A CA 1 ATOM 3941 C C . VAL A 1 512 ? -2.680 41.952 60.244 1.00 17.83 ? 512 VAL A C 1 ATOM 3942 O O . VAL A 1 512 ? -3.881 42.195 60.499 1.00 17.41 ? 512 VAL A O 1 ATOM 3943 C CB . VAL A 1 512 ? -1.652 42.039 57.920 1.00 16.01 ? 512 VAL A CB 1 ATOM 3944 C CG1 . VAL A 1 512 ? -2.939 41.338 57.416 1.00 16.72 ? 512 VAL A CG1 1 ATOM 3945 C CG2 . VAL A 1 512 ? -1.124 43.023 56.854 1.00 18.03 ? 512 VAL A CG2 1 ATOM 3946 N N . CYS A 1 513 ? -2.011 40.951 60.800 1.00 17.75 ? 513 CYS A N 1 ATOM 3947 C CA . CYS A 1 513 ? -2.698 39.965 61.676 1.00 17.00 ? 513 CYS A CA 1 ATOM 3948 C C . CYS A 1 513 ? -3.098 40.597 62.996 1.00 18.76 ? 513 CYS A C 1 ATOM 3949 O O . CYS A 1 513 ? -4.050 40.146 63.631 1.00 18.79 ? 513 CYS A O 1 ATOM 3950 C CB . CYS A 1 513 ? -1.792 38.758 61.924 1.00 18.40 ? 513 CYS A CB 1 ATOM 3951 S SG . CYS A 1 513 ? -1.264 37.887 60.398 1.00 19.62 ? 513 CYS A SG 1 ATOM 3952 N N . GLY A 1 514 ? -2.421 41.673 63.379 1.00 17.54 ? 514 GLY A N 1 ATOM 3953 C CA . GLY A 1 514 ? -2.818 42.399 64.615 1.00 18.08 ? 514 GLY A CA 1 ATOM 3954 C C . GLY A 1 514 ? -4.135 43.115 64.431 1.00 19.47 ? 514 GLY A C 1 ATOM 3955 O O . GLY A 1 514 ? -4.802 43.444 65.430 1.00 22.07 ? 514 GLY A O 1 ATOM 3956 N N . GLY A 1 515 ? -4.523 43.368 63.185 1.00 18.22 ? 515 GLY A N 1 ATOM 3957 C CA . GLY A 1 515 ? -5.744 44.136 62.868 1.00 17.90 ? 515 GLY A CA 1 ATOM 3958 C C . GLY A 1 515 ? -6.958 43.339 62.428 1.00 18.29 ? 515 GLY A C 1 ATOM 3959 O O . GLY A 1 515 ? -8.100 43.804 62.542 1.00 19.68 ? 515 GLY A O 1 ATOM 3960 N N . VAL A 1 516 ? -6.731 42.153 61.848 1.00 16.57 ? 516 VAL A N 1 ATOM 3961 C CA . VAL A 1 516 ? -7.829 41.327 61.305 1.00 15.96 ? 516 VAL A CA 1 ATOM 3962 C C . VAL A 1 516 ? -7.310 39.864 61.245 1.00 15.92 ? 516 VAL A C 1 ATOM 3963 O O . VAL A 1 516 ? -6.077 39.634 61.217 1.00 16.64 ? 516 VAL A O 1 ATOM 3964 C CB . VAL A 1 516 ? -8.328 41.822 59.902 1.00 16.51 ? 516 VAL A CB 1 ATOM 3965 C CG1 . VAL A 1 516 ? -7.279 41.572 58.798 1.00 15.41 ? 516 VAL A CG1 1 ATOM 3966 C CG2 . VAL A 1 516 ? -9.721 41.319 59.529 1.00 17.38 ? 516 VAL A CG2 1 ATOM 3967 N N . ARG A 1 517 ? -8.216 38.883 61.273 1.00 15.96 ? 517 ARG A N 1 ATOM 3968 C CA . ARG A 1 517 ? -7.783 37.507 61.128 1.00 15.69 ? 517 ARG A CA 1 ATOM 3969 C C . ARG A 1 517 ? -7.034 37.347 59.783 1.00 16.18 ? 517 ARG A C 1 ATOM 3970 O O . ARG A 1 517 ? -7.458 37.919 58.769 1.00 15.58 ? 517 ARG A O 1 ATOM 3971 C CB . ARG A 1 517 ? -8.999 36.558 61.125 1.00 17.93 ? 517 ARG A CB 1 ATOM 3972 C CG B ARG A 1 517 ? -10.167 36.852 60.152 0.60 16.55 ? 517 ARG A CG 1 ATOM 3973 C CG C ARG A 1 517 ? -9.695 36.245 62.429 0.40 19.82 ? 517 ARG A CG 1 ATOM 3974 C CD B ARG A 1 517 ? -11.541 36.234 60.543 0.60 19.32 ? 517 ARG A CD 1 ATOM 3975 C CD C ARG A 1 517 ? -11.196 36.036 62.124 0.40 21.67 ? 517 ARG A CD 1 ATOM 3976 N NE B ARG A 1 517 ? -12.184 35.839 59.277 0.60 23.73 ? 517 ARG A NE 1 ATOM 3977 N NE C ARG A 1 517 ? -11.573 34.920 61.262 0.40 23.68 ? 517 ARG A NE 1 ATOM 3978 C CZ B ARG A 1 517 ? -13.310 35.151 59.135 0.60 25.96 ? 517 ARG A CZ 1 ATOM 3979 C CZ C ARG A 1 517 ? -12.322 35.024 60.167 0.40 23.35 ? 517 ARG A CZ 1 ATOM 3980 N NH1 B ARG A 1 517 ? -14.024 34.817 60.200 0.60 30.19 ? 517 ARG A NH1 1 ATOM 3981 N NH1 C ARG A 1 517 ? -12.760 36.216 59.785 0.40 23.58 ? 517 ARG A NH1 1 ATOM 3982 N NH2 B ARG A 1 517 ? -13.749 34.833 57.917 0.60 26.01 ? 517 ARG A NH2 1 ATOM 3983 N NH2 C ARG A 1 517 ? -12.600 33.933 59.428 0.40 21.26 ? 517 ARG A NH2 1 ATOM 3984 N N . CYS A 1 518 ? -5.968 36.566 59.807 1.00 16.35 ? 518 CYS A N 1 ATOM 3985 C CA . CYS A 1 518 ? -5.100 36.507 58.618 1.00 16.45 ? 518 CYS A CA 1 ATOM 3986 C C . CYS A 1 518 ? -4.666 35.102 58.264 1.00 16.61 ? 518 CYS A C 1 ATOM 3987 O O . CYS A 1 518 ? -4.341 34.271 59.123 1.00 17.66 ? 518 CYS A O 1 ATOM 3988 C CB . CYS A 1 518 ? -3.866 37.344 58.872 1.00 18.36 ? 518 CYS A CB 1 ATOM 3989 S SG . CYS A 1 518 ? -2.792 36.581 60.133 1.00 21.02 ? 518 CYS A SG 1 ATOM 3990 N N . ALA A 1 519 ? -4.568 34.873 56.958 1.00 14.97 ? 519 ALA A N 1 ATOM 3991 C CA . ALA A 1 519 ? -3.904 33.694 56.434 1.00 14.18 ? 519 ALA A CA 1 ATOM 3992 C C . ALA A 1 519 ? -2.586 34.142 55.808 1.00 13.72 ? 519 ALA A C 1 ATOM 3993 O O . ALA A 1 519 ? -2.580 35.007 54.897 1.00 14.42 ? 519 ALA A O 1 ATOM 3994 C CB . ALA A 1 519 ? -4.806 33.062 55.374 1.00 14.47 ? 519 ALA A CB 1 ATOM 3995 N N . THR A 1 520 ? -1.488 33.650 56.363 1.00 13.49 ? 520 THR A N 1 ATOM 3996 C CA . THR A 1 520 ? -0.144 34.014 55.846 1.00 13.22 ? 520 THR A CA 1 ATOM 3997 C C . THR A 1 520 ? 0.325 32.968 54.854 1.00 14.06 ? 520 THR A C 1 ATOM 3998 O O . THR A 1 520 ? 0.306 31.761 55.143 1.00 13.59 ? 520 THR A O 1 ATOM 3999 C CB . THR A 1 520 ? 0.845 34.121 57.013 1.00 13.88 ? 520 THR A CB 1 ATOM 4000 O OG1 . THR A 1 520 ? 0.384 35.192 57.862 1.00 15.63 ? 520 THR A OG1 1 ATOM 4001 C CG2 . THR A 1 520 ? 2.308 34.318 56.538 1.00 14.20 ? 520 THR A CG2 1 ATOM 4002 N N . VAL A 1 521 ? 0.749 33.434 53.676 1.00 13.56 ? 521 VAL A N 1 ATOM 4003 C CA . VAL A 1 521 ? 1.266 32.534 52.632 1.00 12.96 ? 521 VAL A CA 1 ATOM 4004 C C . VAL A 1 521 ? 2.752 32.815 52.561 1.00 13.56 ? 521 VAL A C 1 ATOM 4005 O O . VAL A 1 521 ? 3.160 33.931 52.240 1.00 14.35 ? 521 VAL A O 1 ATOM 4006 C CB . VAL A 1 521 ? 0.628 32.790 51.246 1.00 12.93 ? 521 VAL A CB 1 ATOM 4007 C CG1 . VAL A 1 521 ? 1.241 31.853 50.188 1.00 14.35 ? 521 VAL A CG1 1 ATOM 4008 C CG2 . VAL A 1 521 ? -0.887 32.597 51.300 1.00 14.14 ? 521 VAL A CG2 1 ATOM 4009 N N . LEU A 1 522 ? 3.538 31.815 52.948 1.00 12.64 ? 522 LEU A N 1 ATOM 4010 C CA . LEU A 1 522 ? 5.008 31.929 52.980 1.00 13.13 ? 522 LEU A CA 1 ATOM 4011 C C . LEU A 1 522 ? 5.592 31.334 51.701 1.00 12.37 ? 522 LEU A C 1 ATOM 4012 O O . LEU A 1 522 ? 5.416 30.152 51.408 1.00 13.63 ? 522 LEU A O 1 ATOM 4013 C CB . LEU A 1 522 ? 5.538 31.178 54.205 1.00 14.03 ? 522 LEU A CB 1 ATOM 4014 C CG . LEU A 1 522 ? 7.052 31.093 54.332 1.00 15.94 ? 522 LEU A CG 1 ATOM 4015 C CD1 . LEU A 1 522 ? 7.684 32.460 54.432 1.00 16.36 ? 522 LEU A CD1 1 ATOM 4016 C CD2 . LEU A 1 522 ? 7.373 30.258 55.578 1.00 16.61 ? 522 LEU A CD2 1 ATOM 4017 N N . ILE A 1 523 ? 6.263 32.213 50.940 1.00 12.75 ? 523 ILE A N 1 ATOM 4018 C CA . ILE A 1 523 ? 6.942 31.831 49.677 1.00 12.89 ? 523 ILE A CA 1 ATOM 4019 C C . ILE A 1 523 ? 8.415 31.643 49.987 1.00 14.02 ? 523 ILE A C 1 ATOM 4020 O O . ILE A 1 523 ? 9.045 32.580 50.476 1.00 15.05 ? 523 ILE A O 1 ATOM 4021 C CB . ILE A 1 523 ? 6.743 32.958 48.646 1.00 13.92 ? 523 ILE A CB 1 ATOM 4022 C CG1 . ILE A 1 523 ? 5.243 33.171 48.289 1.00 14.46 ? 523 ILE A CG1 1 ATOM 4023 C CG2 . ILE A 1 523 ? 7.613 32.734 47.389 1.00 14.48 ? 523 ILE A CG2 1 ATOM 4024 C CD1 . ILE A 1 523 ? 4.608 32.045 47.508 1.00 14.78 ? 523 ILE A CD1 1 ATOM 4025 N N . SER A 1 524 ? 8.925 30.441 49.819 1.00 12.71 ? 524 SER A N 1 ATOM 4026 C CA . SER A 1 524 ? 10.364 30.176 50.142 1.00 13.43 ? 524 SER A CA 1 ATOM 4027 C C . SER A 1 524 ? 10.819 28.971 49.353 1.00 14.10 ? 524 SER A C 1 ATOM 4028 O O . SER A 1 524 ? 10.020 28.144 48.876 1.00 13.28 ? 524 SER A O 1 ATOM 4029 C CB . SER A 1 524 ? 10.545 29.948 51.677 1.00 14.19 ? 524 SER A CB 1 ATOM 4030 O OG . SER A 1 524 ? 9.918 28.721 52.049 1.00 14.46 ? 524 SER A OG 1 ATOM 4031 N N . GLY A 1 525 ? 12.149 28.839 49.248 1.00 13.68 ? 525 GLY A N 1 ATOM 4032 C CA . GLY A 1 525 ? 12.762 27.644 48.610 1.00 14.76 ? 525 GLY A CA 1 ATOM 4033 C C . GLY A 1 525 ? 13.103 26.519 49.553 1.00 15.66 ? 525 GLY A C 1 ATOM 4034 O O . GLY A 1 525 ? 13.664 25.507 49.135 1.00 15.61 ? 525 GLY A O 1 ATOM 4035 N N . ARG A 1 526 ? 12.694 26.663 50.831 1.00 15.64 ? 526 ARG A N 1 ATOM 4036 C CA . ARG A 1 526 ? 13.239 25.832 51.919 1.00 16.19 ? 526 ARG A CA 1 ATOM 4037 C C . ARG A 1 526 ? 12.563 26.255 53.193 1.00 16.04 ? 526 ARG A C 1 ATOM 4038 O O . ARG A 1 526 ? 11.940 27.313 53.264 1.00 16.29 ? 526 ARG A O 1 ATOM 4039 C CB . ARG A 1 526 ? 14.749 26.100 52.047 1.00 16.61 ? 526 ARG A CB 1 ATOM 4040 C CG . ARG A 1 526 ? 15.059 27.582 52.118 1.00 16.67 ? 526 ARG A CG 1 ATOM 4041 C CD . ARG A 1 526 ? 16.575 27.746 52.318 1.00 19.05 ? 526 ARG A CD 1 ATOM 4042 N NE . ARG A 1 526 ? 16.909 29.116 52.010 1.00 21.05 ? 526 ARG A NE 1 ATOM 4043 C CZ . ARG A 1 526 ? 18.070 29.511 51.524 1.00 18.67 ? 526 ARG A CZ 1 ATOM 4044 N NH1 . ARG A 1 526 ? 19.086 28.655 51.340 1.00 19.83 ? 526 ARG A NH1 1 ATOM 4045 N NH2 . ARG A 1 526 ? 18.225 30.778 51.271 1.00 21.15 ? 526 ARG A NH2 1 ATOM 4046 N N . PRO A 1 527 ? 12.708 25.446 54.254 1.00 16.37 ? 527 PRO A N 1 ATOM 4047 C CA . PRO A 1 527 ? 12.360 25.976 55.589 1.00 17.01 ? 527 PRO A CA 1 ATOM 4048 C C . PRO A 1 527 ? 13.186 27.210 55.952 1.00 17.06 ? 527 PRO A C 1 ATOM 4049 O O . PRO A 1 527 ? 14.393 27.296 55.627 1.00 17.25 ? 527 PRO A O 1 ATOM 4050 C CB . PRO A 1 527 ? 12.720 24.825 56.528 1.00 18.46 ? 527 PRO A CB 1 ATOM 4051 C CG . PRO A 1 527 ? 13.721 24.007 55.757 1.00 20.93 ? 527 PRO A CG 1 ATOM 4052 C CD . PRO A 1 527 ? 13.260 24.083 54.314 1.00 17.17 ? 527 PRO A CD 1 ATOM 4053 N N . VAL A 1 528 ? 12.516 28.194 56.569 1.00 16.72 ? 528 VAL A N 1 ATOM 4054 C CA . VAL A 1 528 ? 13.106 29.441 57.007 1.00 17.16 ? 528 VAL A CA 1 ATOM 4055 C C . VAL A 1 528 ? 12.661 29.646 58.458 1.00 16.72 ? 528 VAL A C 1 ATOM 4056 O O . VAL A 1 528 ? 11.707 28.969 58.907 1.00 17.40 ? 528 VAL A O 1 ATOM 4057 C CB . VAL A 1 528 ? 12.703 30.642 56.126 1.00 16.93 ? 528 VAL A CB 1 ATOM 4058 C CG1 . VAL A 1 528 ? 13.371 30.526 54.742 1.00 17.74 ? 528 VAL A CG1 1 ATOM 4059 C CG2 . VAL A 1 528 ? 11.167 30.724 56.000 1.00 16.25 ? 528 VAL A CG2 1 ATOM 4060 N N . VAL A 1 529 ? 13.334 30.529 59.205 1.00 17.43 ? 529 VAL A N 1 ATOM 4061 C CA . VAL A 1 529 ? 12.919 30.778 60.607 1.00 17.51 ? 529 VAL A CA 1 ATOM 4062 C C . VAL A 1 529 ? 11.443 31.172 60.587 1.00 17.67 ? 529 VAL A C 1 ATOM 4063 O O . VAL A 1 529 ? 11.073 32.129 59.927 1.00 18.40 ? 529 VAL A O 1 ATOM 4064 C CB . VAL A 1 529 ? 13.769 31.896 61.233 1.00 19.28 ? 529 VAL A CB 1 ATOM 4065 C CG1 . VAL A 1 529 ? 13.192 32.288 62.602 1.00 19.80 ? 529 VAL A CG1 1 ATOM 4066 C CG2 . VAL A 1 529 ? 15.189 31.374 61.391 1.00 20.06 ? 529 VAL A CG2 1 ATOM 4067 N N . VAL A 1 530 ? 10.609 30.415 61.300 1.00 17.24 ? 530 VAL A N 1 ATOM 4068 C CA . VAL A 1 530 ? 9.137 30.584 61.137 1.00 16.58 ? 530 VAL A CA 1 ATOM 4069 C C . VAL A 1 530 ? 8.359 30.796 62.440 1.00 17.14 ? 530 VAL A C 1 ATOM 4070 O O . VAL A 1 530 ? 7.194 31.170 62.373 1.00 17.07 ? 530 VAL A O 1 ATOM 4071 C CB . VAL A 1 530 ? 8.554 29.381 60.324 1.00 17.79 ? 530 VAL A CB 1 ATOM 4072 C CG1 . VAL A 1 530 ? 8.388 28.149 61.183 1.00 17.83 ? 530 VAL A CG1 1 ATOM 4073 C CG2 . VAL A 1 530 ? 7.241 29.743 59.589 1.00 18.37 ? 530 VAL A CG2 1 ATOM 4074 N N . GLN A 1 531 ? 8.969 30.618 63.602 1.00 17.29 ? 531 GLN A N 1 ATOM 4075 C CA . GLN A 1 531 ? 8.184 30.804 64.837 1.00 17.73 ? 531 GLN A CA 1 ATOM 4076 C C . GLN A 1 531 ? 7.529 32.186 64.947 1.00 17.05 ? 531 GLN A C 1 ATOM 4077 O O . GLN A 1 531 ? 6.359 32.254 65.328 1.00 17.53 ? 531 GLN A O 1 ATOM 4078 C CB . GLN A 1 531 ? 9.000 30.480 66.113 1.00 18.16 ? 531 GLN A CB 1 ATOM 4079 C CG . GLN A 1 531 ? 9.449 29.028 66.221 1.00 19.72 ? 531 GLN A CG 1 ATOM 4080 C CD . GLN A 1 531 ? 10.841 28.788 65.653 1.00 20.35 ? 531 GLN A CD 1 ATOM 4081 O OE1 . GLN A 1 531 ? 11.261 29.447 64.679 1.00 21.17 ? 531 GLN A OE1 1 ATOM 4082 N NE2 . GLN A 1 531 ? 11.586 27.840 66.257 1.00 21.81 ? 531 GLN A NE2 1 ATOM 4083 N N . PRO A 1 532 ? 8.246 33.291 64.617 1.00 17.53 ? 532 PRO A N 1 ATOM 4084 C CA . PRO A 1 532 ? 7.573 34.606 64.711 1.00 17.83 ? 532 PRO A CA 1 ATOM 4085 C C . PRO A 1 532 ? 6.395 34.762 63.736 1.00 17.27 ? 532 PRO A C 1 ATOM 4086 O O . PRO A 1 532 ? 5.350 35.292 64.126 1.00 17.10 ? 532 PRO A O 1 ATOM 4087 C CB . PRO A 1 532 ? 8.688 35.607 64.444 1.00 19.90 ? 532 PRO A CB 1 ATOM 4088 C CG . PRO A 1 532 ? 9.934 34.853 64.855 1.00 19.15 ? 532 PRO A CG 1 ATOM 4089 C CD . PRO A 1 532 ? 9.713 33.424 64.444 1.00 17.46 ? 532 PRO A CD 1 ATOM 4090 N N . LEU A 1 533 ? 6.551 34.273 62.505 1.00 17.11 ? 533 LEU A N 1 ATOM 4091 C CA . LEU A 1 533 ? 5.421 34.297 61.567 1.00 16.25 ? 533 LEU A CA 1 ATOM 4092 C C . LEU A 1 533 ? 4.277 33.471 62.087 1.00 16.94 ? 533 LEU A C 1 ATOM 4093 O O . LEU A 1 533 ? 3.120 33.893 62.003 1.00 17.22 ? 533 LEU A O 1 ATOM 4094 C CB . LEU A 1 533 ? 5.886 33.741 60.191 1.00 16.57 ? 533 LEU A CB 1 ATOM 4095 C CG . LEU A 1 533 ? 6.778 34.664 59.381 1.00 17.74 ? 533 LEU A CG 1 ATOM 4096 C CD1 . LEU A 1 533 ? 7.477 33.878 58.263 1.00 18.40 ? 533 LEU A CD1 1 ATOM 4097 C CD2 . LEU A 1 533 ? 6.026 35.878 58.816 1.00 18.22 ? 533 LEU A CD2 1 ATOM 4098 N N . LEU A 1 534 ? 4.571 32.290 62.640 1.00 17.16 ? 534 LEU A N 1 ATOM 4099 C CA . LEU A 1 534 ? 3.480 31.459 63.182 1.00 17.65 ? 534 LEU A CA 1 ATOM 4100 C C . LEU A 1 534 ? 2.777 32.156 64.337 1.00 18.05 ? 534 LEU A C 1 ATOM 4101 O O . LEU A 1 534 ? 1.526 32.151 64.401 1.00 18.83 ? 534 LEU A O 1 ATOM 4102 C CB . LEU A 1 534 ? 4.009 30.103 63.665 1.00 18.44 ? 534 LEU A CB 1 ATOM 4103 C CG . LEU A 1 534 ? 4.413 29.112 62.578 1.00 18.38 ? 534 LEU A CG 1 ATOM 4104 C CD1 . LEU A 1 534 ? 5.252 28.027 63.191 1.00 20.17 ? 534 LEU A CD1 1 ATOM 4105 C CD2 . LEU A 1 534 ? 3.142 28.560 61.919 1.00 19.19 ? 534 LEU A CD2 1 ATOM 4106 N N . ALA A 1 535 ? 3.539 32.732 65.262 1.00 17.41 ? 535 ALA A N 1 ATOM 4107 C CA . ALA A 1 535 ? 2.928 33.391 66.441 1.00 18.33 ? 535 ALA A CA 1 ATOM 4108 C C . ALA A 1 535 ? 1.933 34.483 66.068 1.00 17.90 ? 535 ALA A C 1 ATOM 4109 O O . ALA A 1 535 ? 0.921 34.626 66.743 1.00 19.79 ? 535 ALA A O 1 ATOM 4110 C CB . ALA A 1 535 ? 4.023 33.950 67.328 1.00 18.27 ? 535 ALA A CB 1 ATOM 4111 N N . ALA A 1 536 ? 2.189 35.239 64.991 1.00 17.19 ? 536 ALA A N 1 ATOM 4112 C CA . ALA A 1 536 ? 1.277 36.295 64.568 1.00 16.38 ? 536 ALA A CA 1 ATOM 4113 C C . ALA A 1 536 ? 0.048 35.795 63.814 1.00 16.69 ? 536 ALA A C 1 ATOM 4114 O O . ALA A 1 536 ? -0.961 36.501 63.815 1.00 18.10 ? 536 ALA A O 1 ATOM 4115 C CB . ALA A 1 536 ? 1.994 37.294 63.670 1.00 18.49 ? 536 ALA A CB 1 ATOM 4116 N N . SER A 1 537 ? 0.147 34.631 63.169 1.00 16.98 ? 537 SER A N 1 ATOM 4117 C CA . SER A 1 537 ? -0.844 34.256 62.133 1.00 16.04 ? 537 SER A CA 1 ATOM 4118 C C . SER A 1 537 ? -1.951 33.371 62.650 1.00 16.21 ? 537 SER A C 1 ATOM 4119 O O . SER A 1 537 ? -1.680 32.479 63.468 1.00 17.93 ? 537 SER A O 1 ATOM 4120 C CB . SER A 1 537 ? -0.140 33.505 61.014 1.00 17.21 ? 537 SER A CB 1 ATOM 4121 O OG . SER A 1 537 ? 0.901 34.310 60.439 1.00 17.99 ? 537 SER A OG 1 ATOM 4122 N N . ASP A 1 538 ? -3.176 33.540 62.149 1.00 14.82 ? 538 ASP A N 1 ATOM 4123 C CA . ASP A 1 538 ? -4.231 32.555 62.425 1.00 14.96 ? 538 ASP A CA 1 ATOM 4124 C C . ASP A 1 538 ? -3.992 31.271 61.648 1.00 15.32 ? 538 ASP A C 1 ATOM 4125 O O . ASP A 1 538 ? -4.074 30.165 62.184 1.00 17.31 ? 538 ASP A O 1 ATOM 4126 C CB . ASP A 1 538 ? -5.585 33.165 62.062 1.00 15.21 ? 538 ASP A CB 1 ATOM 4127 C CG . ASP A 1 538 ? -5.888 34.402 62.909 1.00 17.14 ? 538 ASP A CG 1 ATOM 4128 O OD1 . ASP A 1 538 ? -5.546 35.526 62.492 1.00 16.69 ? 538 ASP A OD1 1 ATOM 4129 O OD2 . ASP A 1 538 ? -6.387 34.231 64.056 1.00 17.57 ? 538 ASP A OD2 1 ATOM 4130 N N . ALA A 1 539 ? -3.650 31.415 60.349 1.00 14.03 ? 539 ALA A N 1 ATOM 4131 C CA . ALA A 1 539 ? -3.307 30.287 59.503 1.00 13.67 ? 539 ALA A CA 1 ATOM 4132 C C . ALA A 1 539 ? -1.999 30.618 58.790 1.00 14.61 ? 539 ALA A C 1 ATOM 4133 O O . ALA A 1 539 ? -1.736 31.775 58.510 1.00 14.28 ? 539 ALA A O 1 ATOM 4134 C CB . ALA A 1 539 ? -4.406 29.986 58.460 1.00 14.74 ? 539 ALA A CB 1 ATOM 4135 N N . LEU A 1 540 ? -1.218 29.589 58.499 1.00 13.08 ? 540 LEU A N 1 ATOM 4136 C CA . LEU A 1 540 ? 0.045 29.785 57.747 1.00 13.40 ? 540 LEU A CA 1 ATOM 4137 C C . LEU A 1 540 ? 0.263 28.604 56.830 1.00 13.84 ? 540 LEU A C 1 ATOM 4138 O O . LEU A 1 540 ? 0.099 27.431 57.238 1.00 14.42 ? 540 LEU A O 1 ATOM 4139 C CB . LEU A 1 540 ? 1.217 29.972 58.732 1.00 14.56 ? 540 LEU A CB 1 ATOM 4140 C CG . LEU A 1 540 ? 2.528 30.404 58.006 1.00 14.48 ? 540 LEU A CG 1 ATOM 4141 C CD1 . LEU A 1 540 ? 3.386 31.344 58.866 1.00 17.10 ? 540 LEU A CD1 1 ATOM 4142 C CD2 . LEU A 1 540 ? 3.333 29.168 57.602 1.00 16.50 ? 540 LEU A CD2 1 ATOM 4143 N N . VAL A 1 541 ? 0.576 28.906 55.556 1.00 13.18 ? 541 VAL A N 1 ATOM 4144 C CA . VAL A 1 541 ? 0.795 27.931 54.500 1.00 13.19 ? 541 VAL A CA 1 ATOM 4145 C C . VAL A 1 541 ? 2.221 28.083 53.991 1.00 13.29 ? 541 VAL A C 1 ATOM 4146 O O . VAL A 1 541 ? 2.639 29.209 53.643 1.00 14.44 ? 541 VAL A O 1 ATOM 4147 C CB . VAL A 1 541 ? -0.178 28.266 53.352 1.00 13.08 ? 541 VAL A CB 1 ATOM 4148 C CG1 . VAL A 1 541 ? 0.052 27.368 52.153 1.00 13.79 ? 541 VAL A CG1 1 ATOM 4149 C CG2 . VAL A 1 541 ? -1.645 28.126 53.795 1.00 14.31 ? 541 VAL A CG2 1 ATOM 4150 N N . ALA A 1 542 ? 2.943 26.951 53.923 1.00 13.15 ? 542 ALA A N 1 ATOM 4151 C CA . ALA A 1 542 ? 4.238 26.946 53.234 1.00 13.31 ? 542 ALA A CA 1 ATOM 4152 C C . ALA A 1 542 ? 3.901 26.649 51.774 1.00 12.98 ? 542 ALA A C 1 ATOM 4153 O O . ALA A 1 542 ? 3.480 25.524 51.426 1.00 13.52 ? 542 ALA A O 1 ATOM 4154 C CB . ALA A 1 542 ? 5.160 25.875 53.834 1.00 13.86 ? 542 ALA A CB 1 ATOM 4155 N N . ALA A 1 543 ? 4.059 27.686 50.914 1.00 12.85 ? 543 ALA A N 1 ATOM 4156 C CA . ALA A 1 543 ? 3.727 27.555 49.489 1.00 12.44 ? 543 ALA A CA 1 ATOM 4157 C C . ALA A 1 543 ? 4.929 27.261 48.602 1.00 12.61 ? 543 ALA A C 1 ATOM 4158 O O . ALA A 1 543 ? 4.761 27.112 47.379 1.00 12.48 ? 543 ALA A O 1 ATOM 4159 C CB . ALA A 1 543 ? 2.945 28.787 48.970 1.00 12.20 ? 543 ALA A CB 1 ATOM 4160 N N . TRP A 1 544 ? 6.107 27.227 49.204 1.00 12.35 ? 544 TRP A N 1 ATOM 4161 C CA . TRP A 1 544 ? 7.368 26.967 48.469 1.00 12.21 ? 544 TRP A CA 1 ATOM 4162 C C . TRP A 1 544 ? 7.516 28.023 47.352 1.00 11.88 ? 544 TRP A C 1 ATOM 4163 O O . TRP A 1 544 ? 7.282 29.214 47.599 1.00 12.30 ? 544 TRP A O 1 ATOM 4164 C CB . TRP A 1 544 ? 7.450 25.526 47.946 1.00 13.24 ? 544 TRP A CB 1 ATOM 4165 C CG . TRP A 1 544 ? 7.065 24.537 49.021 1.00 13.42 ? 544 TRP A CG 1 ATOM 4166 C CD1 . TRP A 1 544 ? 5.919 23.846 49.060 1.00 14.16 ? 544 TRP A CD1 1 ATOM 4167 C CD2 . TRP A 1 544 ? 7.804 24.220 50.222 1.00 14.48 ? 544 TRP A CD2 1 ATOM 4168 N NE1 . TRP A 1 544 ? 5.877 23.051 50.207 1.00 14.77 ? 544 TRP A NE1 1 ATOM 4169 C CE2 . TRP A 1 544 ? 7.010 23.284 50.950 1.00 14.47 ? 544 TRP A CE2 1 ATOM 4170 C CE3 . TRP A 1 544 ? 9.031 24.628 50.748 1.00 14.62 ? 544 TRP A CE3 1 ATOM 4171 C CZ2 . TRP A 1 544 ? 7.429 22.746 52.200 1.00 15.49 ? 544 TRP A CZ2 1 ATOM 4172 C CZ3 . TRP A 1 544 ? 9.431 24.120 52.007 1.00 16.33 ? 544 TRP A CZ3 1 ATOM 4173 C CH2 . TRP A 1 544 ? 8.631 23.188 52.700 1.00 15.77 ? 544 TRP A CH2 1 ATOM 4174 N N . LEU A 1 545 ? 7.891 27.585 46.136 1.00 11.68 ? 545 LEU A N 1 ATOM 4175 C CA . LEU A 1 545 ? 8.051 28.522 44.983 1.00 12.09 ? 545 LEU A CA 1 ATOM 4176 C C . LEU A 1 545 ? 7.079 28.042 43.884 1.00 11.93 ? 545 LEU A C 1 ATOM 4177 O O . LEU A 1 545 ? 7.453 27.211 43.023 1.00 11.99 ? 545 LEU A O 1 ATOM 4178 C CB . LEU A 1 545 ? 9.515 28.550 44.479 1.00 11.86 ? 545 LEU A CB 1 ATOM 4179 C CG . LEU A 1 545 ? 10.486 29.001 45.574 1.00 12.88 ? 545 LEU A CG 1 ATOM 4180 C CD1 . LEU A 1 545 ? 11.931 28.758 45.082 1.00 13.50 ? 545 LEU A CD1 1 ATOM 4181 C CD2 . LEU A 1 545 ? 10.270 30.470 45.906 1.00 14.46 ? 545 LEU A CD2 1 ATOM 4182 N N . PRO A 1 546 ? 5.796 28.464 43.951 1.00 11.52 ? 546 PRO A N 1 ATOM 4183 C CA . PRO A 1 546 ? 4.734 27.739 43.231 1.00 11.89 ? 546 PRO A CA 1 ATOM 4184 C C . PRO A 1 546 ? 4.667 27.958 41.729 1.00 11.48 ? 546 PRO A C 1 ATOM 4185 O O . PRO A 1 546 ? 3.961 27.199 41.057 1.00 11.97 ? 546 PRO A O 1 ATOM 4186 C CB . PRO A 1 546 ? 3.436 28.166 43.957 1.00 12.47 ? 546 PRO A CB 1 ATOM 4187 C CG . PRO A 1 546 ? 3.780 29.535 44.461 1.00 12.02 ? 546 PRO A CG 1 ATOM 4188 C CD . PRO A 1 546 ? 5.223 29.445 44.921 1.00 11.70 ? 546 PRO A CD 1 ATOM 4189 N N . GLY A 1 547 ? 5.415 28.965 41.224 1.00 11.89 ? 547 GLY A N 1 ATOM 4190 C CA . GLY A 1 547 ? 5.488 29.163 39.746 1.00 11.23 ? 547 GLY A CA 1 ATOM 4191 C C . GLY A 1 547 ? 4.506 30.180 39.214 1.00 10.67 ? 547 GLY A C 1 ATOM 4192 O O . GLY A 1 547 ? 4.066 31.086 39.944 1.00 12.70 ? 547 GLY A O 1 ATOM 4193 N N . SER A 1 548 ? 4.174 30.082 37.932 1.00 11.57 ? 548 SER A N 1 ATOM 4194 C CA . SER A 1 548 ? 3.372 31.140 37.314 1.00 12.02 ? 548 SER A CA 1 ATOM 4195 C C . SER A 1 548 ? 1.885 31.106 37.677 1.00 11.96 ? 548 SER A C 1 ATOM 4196 O O . SER A 1 548 ? 1.201 32.103 37.459 1.00 12.57 ? 548 SER A O 1 ATOM 4197 C CB . SER A 1 548 ? 3.567 31.082 35.791 1.00 12.55 ? 548 SER A CB 1 ATOM 4198 O OG . SER A 1 548 ? 3.230 29.787 35.225 1.00 11.93 ? 548 SER A OG 1 ATOM 4199 N N . GLU A 1 549 ? 1.378 29.974 38.178 1.00 11.33 ? 549 GLU A N 1 ATOM 4200 C CA . GLU A 1 549 ? -0.063 29.782 38.347 1.00 12.29 ? 549 GLU A CA 1 ATOM 4201 C C . GLU A 1 549 ? -0.530 30.012 39.781 1.00 12.29 ? 549 GLU A C 1 ATOM 4202 O O . GLU A 1 549 ? -0.760 29.071 40.547 1.00 13.36 ? 549 GLU A O 1 ATOM 4203 C CB . GLU A 1 549 ? -0.472 28.392 37.796 1.00 12.38 ? 549 GLU A CB 1 ATOM 4204 C CG . GLU A 1 549 ? 0.021 28.213 36.341 1.00 13.17 ? 549 GLU A CG 1 ATOM 4205 C CD . GLU A 1 549 ? -0.355 29.388 35.425 1.00 14.02 ? 549 GLU A CD 1 ATOM 4206 O OE1 . GLU A 1 549 ? -1.517 29.887 35.436 1.00 14.65 ? 549 GLU A OE1 1 ATOM 4207 O OE2 . GLU A 1 549 ? 0.577 29.788 34.675 1.00 14.15 ? 549 GLU A OE2 1 ATOM 4208 N N . GLY A 1 550 ? -0.672 31.292 40.128 1.00 11.60 ? 550 GLY A N 1 ATOM 4209 C CA . GLY A 1 550 ? -1.049 31.670 41.493 1.00 12.39 ? 550 GLY A CA 1 ATOM 4210 C C . GLY A 1 550 ? -2.422 31.159 41.877 1.00 12.44 ? 550 GLY A C 1 ATOM 4211 O O . GLY A 1 550 ? -2.707 31.114 43.077 1.00 12.95 ? 550 GLY A O 1 ATOM 4212 N N . GLN A 1 551 ? -3.259 30.805 40.917 1.00 12.34 ? 551 GLN A N 1 ATOM 4213 C CA . GLN A 1 551 ? -4.561 30.269 41.299 1.00 13.11 ? 551 GLN A CA 1 ATOM 4214 C C . GLN A 1 551 ? -4.438 28.957 42.029 1.00 13.86 ? 551 GLN A C 1 ATOM 4215 O O . GLN A 1 551 ? -5.396 28.520 42.679 1.00 13.57 ? 551 GLN A O 1 ATOM 4216 C CB . GLN A 1 551 ? -5.505 30.123 40.111 1.00 13.58 ? 551 GLN A CB 1 ATOM 4217 C CG . GLN A 1 551 ? -5.857 31.505 39.596 1.00 14.76 ? 551 GLN A CG 1 ATOM 4218 C CD . GLN A 1 551 ? -6.589 31.450 38.243 1.00 15.55 ? 551 GLN A CD 1 ATOM 4219 O OE1 . GLN A 1 551 ? -7.853 31.679 38.175 1.00 20.72 ? 551 GLN A OE1 1 ATOM 4220 N NE2 . GLN A 1 551 ? -5.858 31.152 37.166 1.00 15.12 ? 551 GLN A NE2 1 ATOM 4221 N N . GLY A 1 552 ? -3.302 28.258 41.943 1.00 13.37 ? 552 GLY A N 1 ATOM 4222 C CA . GLY A 1 552 ? -3.127 27.060 42.776 1.00 13.80 ? 552 GLY A CA 1 ATOM 4223 C C . GLY A 1 552 ? -3.176 27.384 44.257 1.00 13.83 ? 552 GLY A C 1 ATOM 4224 O O . GLY A 1 552 ? -3.651 26.565 45.048 1.00 15.24 ? 552 GLY A O 1 ATOM 4225 N N . VAL A 1 553 ? -2.705 28.559 44.640 1.00 13.24 ? 553 VAL A N 1 ATOM 4226 C CA . VAL A 1 553 ? -2.765 28.976 46.056 1.00 12.31 ? 553 VAL A CA 1 ATOM 4227 C C . VAL A 1 553 ? -4.218 29.233 46.443 1.00 12.48 ? 553 VAL A C 1 ATOM 4228 O O . VAL A 1 553 ? -4.673 28.728 47.498 1.00 13.51 ? 553 VAL A O 1 ATOM 4229 C CB . VAL A 1 553 ? -1.881 30.241 46.267 1.00 12.71 ? 553 VAL A CB 1 ATOM 4230 C CG1 . VAL A 1 553 ? -1.998 30.773 47.707 1.00 14.14 ? 553 VAL A CG1 1 ATOM 4231 C CG2 . VAL A 1 553 ? -0.424 29.896 45.905 1.00 13.52 ? 553 VAL A CG2 1 ATOM 4232 N N . THR A 1 554 ? -4.927 30.035 45.653 1.00 12.39 ? 554 THR A N 1 ATOM 4233 C CA . THR A 1 554 ? -6.309 30.369 46.016 1.00 12.84 ? 554 THR A CA 1 ATOM 4234 C C . THR A 1 554 ? -7.260 29.178 45.939 1.00 13.54 ? 554 THR A C 1 ATOM 4235 O O . THR A 1 554 ? -8.273 29.142 46.654 1.00 15.40 ? 554 THR A O 1 ATOM 4236 C CB . THR A 1 554 ? -6.848 31.561 45.229 1.00 12.84 ? 554 THR A CB 1 ATOM 4237 O OG1 . THR A 1 554 ? -6.644 31.320 43.802 1.00 13.15 ? 554 THR A OG1 1 ATOM 4238 C CG2 . THR A 1 554 ? -6.085 32.843 45.652 1.00 14.15 ? 554 THR A CG2 1 ATOM 4239 N N . ASP A 1 555 ? -6.948 28.196 45.097 1.00 13.53 ? 555 ASP A N 1 ATOM 4240 C CA . ASP A 1 555 ? -7.773 26.950 45.021 1.00 13.41 ? 555 ASP A CA 1 ATOM 4241 C C . ASP A 1 555 ? -7.857 26.268 46.380 1.00 14.26 ? 555 ASP A C 1 ATOM 4242 O O . ASP A 1 555 ? -8.931 25.749 46.727 1.00 16.28 ? 555 ASP A O 1 ATOM 4243 C CB . ASP A 1 555 ? -7.159 25.987 44.003 1.00 13.30 ? 555 ASP A CB 1 ATOM 4244 C CG . ASP A 1 555 ? -7.492 26.354 42.565 1.00 14.85 ? 555 ASP A CG 1 ATOM 4245 O OD1 . ASP A 1 555 ? -8.315 27.254 42.303 1.00 15.90 ? 555 ASP A OD1 1 ATOM 4246 O OD2 . ASP A 1 555 ? -6.881 25.716 41.694 1.00 16.40 ? 555 ASP A OD2 1 ATOM 4247 N N . ALA A 1 556 ? -6.797 26.340 47.167 1.00 12.90 ? 556 ALA A N 1 ATOM 4248 C CA . ALA A 1 556 ? -6.857 25.793 48.519 1.00 12.92 ? 556 ALA A CA 1 ATOM 4249 C C . ALA A 1 556 ? -7.293 26.817 49.542 1.00 13.09 ? 556 ALA A C 1 ATOM 4250 O O . ALA A 1 556 ? -8.094 26.475 50.451 1.00 14.41 ? 556 ALA A O 1 ATOM 4251 C CB . ALA A 1 556 ? -5.480 25.219 48.902 1.00 14.46 ? 556 ALA A CB 1 ATOM 4252 N N . LEU A 1 557 ? -6.882 28.103 49.436 1.00 12.66 ? 557 LEU A N 1 ATOM 4253 C CA . LEU A 1 557 ? -7.338 29.088 50.444 1.00 12.96 ? 557 LEU A CA 1 ATOM 4254 C C . LEU A 1 557 ? -8.864 29.201 50.497 1.00 13.84 ? 557 LEU A C 1 ATOM 4255 O O . LEU A 1 557 ? -9.392 29.375 51.616 1.00 14.65 ? 557 LEU A O 1 ATOM 4256 C CB . LEU A 1 557 ? -6.752 30.485 50.198 1.00 14.08 ? 557 LEU A CB 1 ATOM 4257 C CG . LEU A 1 557 ? -5.246 30.608 50.294 1.00 14.06 ? 557 LEU A CG 1 ATOM 4258 C CD1 . LEU A 1 557 ? -4.896 32.052 49.923 1.00 14.37 ? 557 LEU A CD1 1 ATOM 4259 C CD2 . LEU A 1 557 ? -4.755 30.310 51.708 1.00 14.59 ? 557 LEU A CD2 1 ATOM 4260 N N . PHE A 1 558 ? -9.549 29.130 49.366 1.00 13.42 ? 558 PHE A N 1 ATOM 4261 C CA . PHE A 1 558 ? -11.003 29.297 49.340 1.00 14.17 ? 558 PHE A CA 1 ATOM 4262 C C . PHE A 1 558 ? -11.759 27.965 49.311 1.00 14.68 ? 558 PHE A C 1 ATOM 4263 O O . PHE A 1 558 ? -13.006 27.968 49.168 1.00 15.84 ? 558 PHE A O 1 ATOM 4264 C CB . PHE A 1 558 ? -11.421 30.193 48.155 1.00 14.24 ? 558 PHE A CB 1 ATOM 4265 C CG . PHE A 1 558 ? -10.939 31.614 48.277 1.00 14.19 ? 558 PHE A CG 1 ATOM 4266 C CD1 . PHE A 1 558 ? -11.490 32.483 49.216 1.00 14.77 ? 558 PHE A CD1 1 ATOM 4267 C CD2 . PHE A 1 558 ? -9.894 32.104 47.476 1.00 16.01 ? 558 PHE A CD2 1 ATOM 4268 C CE1 . PHE A 1 558 ? -11.039 33.792 49.356 1.00 15.62 ? 558 PHE A CE1 1 ATOM 4269 C CE2 . PHE A 1 558 ? -9.444 33.436 47.630 1.00 17.11 ? 558 PHE A CE2 1 ATOM 4270 C CZ . PHE A 1 558 ? -9.981 34.274 48.577 1.00 16.17 ? 558 PHE A CZ 1 ATOM 4271 N N . GLY A 1 559 ? -11.028 26.845 49.501 1.00 15.03 ? 559 GLY A N 1 ATOM 4272 C CA . GLY A 1 559 ? -11.715 25.534 49.718 1.00 15.88 ? 559 GLY A CA 1 ATOM 4273 C C . GLY A 1 559 ? -12.271 24.850 48.467 1.00 15.71 ? 559 GLY A C 1 ATOM 4274 O O . GLY A 1 559 ? -13.063 23.899 48.614 1.00 17.51 ? 559 GLY A O 1 ATOM 4275 N N . ASP A 1 560 ? -11.839 25.249 47.265 1.00 15.91 ? 560 ASP A N 1 ATOM 4276 C CA . ASP A 1 560 ? -12.209 24.448 46.097 1.00 16.14 ? 560 ASP A CA 1 ATOM 4277 C C . ASP A 1 560 ? -11.600 23.052 46.190 1.00 17.17 ? 560 ASP A C 1 ATOM 4278 O O . ASP A 1 560 ? -12.213 22.071 45.725 1.00 19.50 ? 560 ASP A O 1 ATOM 4279 C CB . ASP A 1 560 ? -11.805 25.130 44.809 1.00 19.88 ? 560 ASP A CB 1 ATOM 4280 C CG . ASP A 1 560 ? -12.632 26.380 44.529 1.00 22.20 ? 560 ASP A CG 1 ATOM 4281 O OD1 . ASP A 1 560 ? -13.721 26.537 45.064 1.00 25.87 ? 560 ASP A OD1 1 ATOM 4282 O OD2 . ASP A 1 560 ? -12.172 27.181 43.721 1.00 31.35 ? 560 ASP A OD2 1 ATOM 4283 N N . PHE A 1 561 ? -10.421 22.963 46.801 1.00 16.85 ? 561 PHE A N 1 ATOM 4284 C CA . PHE A 1 561 ? -9.733 21.714 47.102 1.00 17.33 ? 561 PHE A CA 1 ATOM 4285 C C . PHE A 1 561 ? -9.230 21.780 48.538 1.00 17.86 ? 561 PHE A C 1 ATOM 4286 O O . PHE A 1 561 ? -8.970 22.872 49.078 1.00 17.19 ? 561 PHE A O 1 ATOM 4287 C CB . PHE A 1 561 ? -8.556 21.461 46.154 1.00 17.59 ? 561 PHE A CB 1 ATOM 4288 C CG . PHE A 1 561 ? -8.963 21.342 44.720 1.00 18.12 ? 561 PHE A CG 1 ATOM 4289 C CD1 . PHE A 1 561 ? -9.104 22.497 43.936 1.00 19.27 ? 561 PHE A CD1 1 ATOM 4290 C CD2 . PHE A 1 561 ? -9.252 20.081 44.153 1.00 19.72 ? 561 PHE A CD2 1 ATOM 4291 C CE1 . PHE A 1 561 ? -9.503 22.413 42.627 1.00 21.10 ? 561 PHE A CE1 1 ATOM 4292 C CE2 . PHE A 1 561 ? -9.638 20.008 42.807 1.00 21.76 ? 561 PHE A CE2 1 ATOM 4293 C CZ . PHE A 1 561 ? -9.756 21.186 42.060 1.00 20.60 ? 561 PHE A CZ 1 ATOM 4294 N N . GLY A 1 562 ? -9.114 20.618 49.160 1.00 19.04 ? 562 GLY A N 1 ATOM 4295 C CA . GLY A 1 562 ? -8.511 20.550 50.478 1.00 19.47 ? 562 GLY A CA 1 ATOM 4296 C C . GLY A 1 562 ? -6.996 20.649 50.420 1.00 18.19 ? 562 GLY A C 1 ATOM 4297 O O . GLY A 1 562 ? -6.365 20.337 49.387 1.00 20.95 ? 562 GLY A O 1 ATOM 4298 N N . PHE A 1 563 ? -6.396 21.063 51.527 1.00 18.52 ? 563 PHE A N 1 ATOM 4299 C CA . PHE A 1 563 ? -4.918 20.966 51.639 1.00 16.66 ? 563 PHE A CA 1 ATOM 4300 C C . PHE A 1 563 ? -4.518 19.519 51.830 1.00 18.39 ? 563 PHE A C 1 ATOM 4301 O O . PHE A 1 563 ? -5.103 18.800 52.672 1.00 19.81 ? 563 PHE A O 1 ATOM 4302 C CB . PHE A 1 563 ? -4.405 21.755 52.826 1.00 16.26 ? 563 PHE A CB 1 ATOM 4303 C CG . PHE A 1 563 ? -4.409 23.238 52.616 1.00 15.69 ? 563 PHE A CG 1 ATOM 4304 C CD1 . PHE A 1 563 ? -5.531 24.025 52.891 1.00 16.22 ? 563 PHE A CD1 1 ATOM 4305 C CD2 . PHE A 1 563 ? -3.261 23.867 52.109 1.00 14.26 ? 563 PHE A CD2 1 ATOM 4306 C CE1 . PHE A 1 563 ? -5.496 25.400 52.717 1.00 15.45 ? 563 PHE A CE1 1 ATOM 4307 C CE2 . PHE A 1 563 ? -3.233 25.234 51.897 1.00 15.30 ? 563 PHE A CE2 1 ATOM 4308 C CZ . PHE A 1 563 ? -4.364 26.028 52.213 1.00 15.67 ? 563 PHE A CZ 1 ATOM 4309 N N . THR A 1 564 ? -3.549 19.084 51.035 1.00 16.81 ? 564 THR A N 1 ATOM 4310 C CA . THR A 1 564 ? -3.039 17.692 51.115 1.00 17.45 ? 564 THR A CA 1 ATOM 4311 C C . THR A 1 564 ? -1.506 17.579 51.170 1.00 17.31 ? 564 THR A C 1 ATOM 4312 O O . THR A 1 564 ? -0.963 16.490 51.409 1.00 18.62 ? 564 THR A O 1 ATOM 4313 C CB . THR A 1 564 ? -3.545 16.823 49.960 1.00 18.16 ? 564 THR A CB 1 ATOM 4314 O OG1 . THR A 1 564 ? -3.229 17.447 48.697 1.00 20.19 ? 564 THR A OG1 1 ATOM 4315 C CG2 . THR A 1 564 ? -5.079 16.627 50.074 1.00 20.60 ? 564 THR A CG2 1 ATOM 4316 N N . GLY A 1 565 ? -0.802 18.668 50.903 1.00 15.28 ? 565 GLY A N 1 ATOM 4317 C CA . GLY A 1 565 ? 0.655 18.624 50.885 1.00 15.51 ? 565 GLY A CA 1 ATOM 4318 C C . GLY A 1 565 ? 1.245 18.232 52.234 1.00 15.67 ? 565 GLY A C 1 ATOM 4319 O O . GLY A 1 565 ? 0.641 18.521 53.290 1.00 17.19 ? 565 GLY A O 1 ATOM 4320 N N . ARG A 1 566 ? 2.420 17.594 52.220 1.00 16.34 ? 566 ARG A N 1 ATOM 4321 C CA . ARG A 1 566 ? 3.118 17.192 53.482 1.00 17.17 ? 566 ARG A CA 1 ATOM 4322 C C . ARG A 1 566 ? 4.598 17.609 53.381 1.00 16.52 ? 566 ARG A C 1 ATOM 4323 O O . ARG A 1 566 ? 5.172 17.499 52.278 1.00 17.00 ? 566 ARG A O 1 ATOM 4324 C CB . ARG A 1 566 ? 3.031 15.656 53.666 1.00 19.75 ? 566 ARG A CB 1 ATOM 4325 C CG . ARG A 1 566 ? 1.601 15.225 54.030 1.00 22.29 ? 566 ARG A CG 1 ATOM 4326 C CD . ARG A 1 566 ? 1.388 13.718 54.138 1.00 29.28 ? 566 ARG A CD 1 ATOM 4327 N NE A ARG A 1 566 ? 1.523 13.124 52.822 0.60 31.70 ? 566 ARG A NE 1 ATOM 4328 N NE B ARG A 1 566 ? 2.309 13.010 55.022 0.40 27.04 ? 566 ARG A NE 1 ATOM 4329 C CZ A ARG A 1 566 ? 0.532 12.536 52.164 0.60 32.74 ? 566 ARG A CZ 1 ATOM 4330 C CZ B ARG A 1 566 ? 3.155 12.075 54.618 0.40 28.31 ? 566 ARG A CZ 1 ATOM 4331 N NH1 A ARG A 1 566 ? -0.696 12.384 52.709 0.60 33.04 ? 566 ARG A NH1 1 ATOM 4332 N NH1 B ARG A 1 566 ? 3.212 11.722 53.338 0.40 25.36 ? 566 ARG A NH1 1 ATOM 4333 N NH2 A ARG A 1 566 ? 0.789 12.077 50.974 0.60 27.74 ? 566 ARG A NH2 1 ATOM 4334 N NH2 B ARG A 1 566 ? 3.936 11.483 55.509 0.40 30.73 ? 566 ARG A NH2 1 ATOM 4335 N N . LEU A 1 567 ? 5.208 18.038 54.491 1.00 15.47 ? 567 LEU A N 1 ATOM 4336 C CA . LEU A 1 567 ? 6.628 18.511 54.388 1.00 16.35 ? 567 LEU A CA 1 ATOM 4337 C C . LEU A 1 567 ? 7.490 17.443 53.764 1.00 17.46 ? 567 LEU A C 1 ATOM 4338 O O . LEU A 1 567 ? 7.503 16.261 54.206 1.00 16.57 ? 567 LEU A O 1 ATOM 4339 C CB . LEU A 1 567 ? 7.231 18.874 55.773 1.00 16.32 ? 567 LEU A CB 1 ATOM 4340 C CG . LEU A 1 567 ? 6.602 20.086 56.423 1.00 16.07 ? 567 LEU A CG 1 ATOM 4341 C CD1 . LEU A 1 567 ? 7.300 20.369 57.741 1.00 17.19 ? 567 LEU A CD1 1 ATOM 4342 C CD2 . LEU A 1 567 ? 6.726 21.351 55.541 1.00 17.04 ? 567 LEU A CD2 1 ATOM 4343 N N . PRO A 1 568 ? 8.280 17.801 52.749 1.00 15.98 ? 568 PRO A N 1 ATOM 4344 C CA . PRO A 1 568 ? 9.248 16.852 52.166 1.00 16.42 ? 568 PRO A CA 1 ATOM 4345 C C . PRO A 1 568 ? 10.620 17.012 52.798 1.00 16.49 ? 568 PRO A C 1 ATOM 4346 O O . PRO A 1 568 ? 11.602 16.368 52.368 1.00 17.52 ? 568 PRO A O 1 ATOM 4347 C CB . PRO A 1 568 ? 9.289 17.299 50.690 1.00 15.86 ? 568 PRO A CB 1 ATOM 4348 C CG . PRO A 1 568 ? 9.166 18.824 50.787 1.00 15.02 ? 568 PRO A CG 1 ATOM 4349 C CD . PRO A 1 568 ? 8.133 19.042 51.921 1.00 14.81 ? 568 PRO A CD 1 ATOM 4350 N N . ARG A 1 569 ? 10.699 17.870 53.797 1.00 18.23 ? 569 ARG A N 1 ATOM 4351 C CA . ARG A 1 569 ? 11.926 17.994 54.574 1.00 19.74 ? 569 ARG A CA 1 ATOM 4352 C C . ARG A 1 569 ? 11.595 18.438 55.992 1.00 18.91 ? 569 ARG A C 1 ATOM 4353 O O . ARG A 1 569 ? 10.469 18.860 56.271 1.00 19.86 ? 569 ARG A O 1 ATOM 4354 C CB . ARG A 1 569 ? 12.981 18.875 53.886 1.00 24.14 ? 569 ARG A CB 1 ATOM 4355 C CG . ARG A 1 569 ? 12.490 20.179 53.296 1.00 23.02 ? 569 ARG A CG 1 ATOM 4356 C CD . ARG A 1 569 ? 13.599 20.891 52.508 1.00 21.08 ? 569 ARG A CD 1 ATOM 4357 N NE . ARG A 1 569 ? 14.865 20.740 53.204 1.00 21.57 ? 569 ARG A NE 1 ATOM 4358 C CZ . ARG A 1 569 ? 15.858 19.945 52.817 1.00 21.33 ? 569 ARG A CZ 1 ATOM 4359 N NH1 . ARG A 1 569 ? 15.804 19.300 51.640 1.00 22.31 ? 569 ARG A NH1 1 ATOM 4360 N NH2 . ARG A 1 569 ? 16.940 19.841 53.602 1.00 22.07 ? 569 ARG A NH2 1 ATOM 4361 N N . THR A 1 570 ? 12.608 18.348 56.840 1.00 19.67 ? 570 THR A N 1 ATOM 4362 C CA . THR A 1 570 ? 12.496 18.731 58.242 1.00 19.49 ? 570 THR A CA 1 ATOM 4363 C C . THR A 1 570 ? 12.461 20.260 58.408 1.00 18.68 ? 570 THR A C 1 ATOM 4364 O O . THR A 1 570 ? 13.219 20.983 57.751 1.00 19.93 ? 570 THR A O 1 ATOM 4365 C CB . THR A 1 570 ? 13.714 18.152 58.982 1.00 21.09 ? 570 THR A CB 1 ATOM 4366 O OG1 . THR A 1 570 ? 13.638 16.728 58.959 1.00 21.34 ? 570 THR A OG1 1 ATOM 4367 C CG2 . THR A 1 570 ? 13.797 18.657 60.453 1.00 22.39 ? 570 THR A CG2 1 ATOM 4368 N N . TRP A 1 571 ? 11.566 20.758 59.268 1.00 18.04 ? 571 TRP A N 1 ATOM 4369 C CA . TRP A 1 571 ? 11.585 22.182 59.530 1.00 18.02 ? 571 TRP A CA 1 ATOM 4370 C C . TRP A 1 571 ? 12.329 22.362 60.832 1.00 19.89 ? 571 TRP A C 1 ATOM 4371 O O . TRP A 1 571 ? 11.870 21.875 61.873 1.00 20.17 ? 571 TRP A O 1 ATOM 4372 C CB . TRP A 1 571 ? 10.162 22.729 59.619 1.00 18.10 ? 571 TRP A CB 1 ATOM 4373 C CG . TRP A 1 571 ? 10.126 24.191 59.274 1.00 16.88 ? 571 TRP A CG 1 ATOM 4374 C CD1 . TRP A 1 571 ? 10.727 25.219 59.946 1.00 17.65 ? 571 TRP A CD1 1 ATOM 4375 C CD2 . TRP A 1 571 ? 9.472 24.789 58.135 1.00 16.73 ? 571 TRP A CD2 1 ATOM 4376 N NE1 . TRP A 1 571 ? 10.496 26.434 59.320 1.00 16.22 ? 571 TRP A NE1 1 ATOM 4377 C CE2 . TRP A 1 571 ? 9.731 26.196 58.200 1.00 16.59 ? 571 TRP A CE2 1 ATOM 4378 C CE3 . TRP A 1 571 ? 8.737 24.273 57.062 1.00 17.08 ? 571 TRP A CE3 1 ATOM 4379 C CZ2 . TRP A 1 571 ? 9.266 27.092 57.239 1.00 16.63 ? 571 TRP A CZ2 1 ATOM 4380 C CZ3 . TRP A 1 571 ? 8.275 25.185 56.073 1.00 16.84 ? 571 TRP A CZ3 1 ATOM 4381 C CH2 . TRP A 1 571 ? 8.530 26.556 56.198 1.00 16.26 ? 571 TRP A CH2 1 ATOM 4382 N N . PHE A 1 572 ? 13.469 23.028 60.785 1.00 19.29 ? 572 PHE A N 1 ATOM 4383 C CA . PHE A 1 572 ? 14.296 23.217 62.007 1.00 20.14 ? 572 PHE A CA 1 ATOM 4384 C C . PHE A 1 572 ? 13.661 24.220 62.987 1.00 21.06 ? 572 PHE A C 1 ATOM 4385 O O . PHE A 1 572 ? 12.845 25.102 62.619 1.00 20.74 ? 572 PHE A O 1 ATOM 4386 C CB . PHE A 1 572 ? 15.689 23.698 61.591 1.00 21.98 ? 572 PHE A CB 1 ATOM 4387 C CG . PHE A 1 572 ? 15.662 24.940 60.730 1.00 20.23 ? 572 PHE A CG 1 ATOM 4388 C CD1 . PHE A 1 572 ? 15.518 26.193 61.288 1.00 20.41 ? 572 PHE A CD1 1 ATOM 4389 C CD2 . PHE A 1 572 ? 15.786 24.827 59.347 1.00 19.96 ? 572 PHE A CD2 1 ATOM 4390 C CE1 . PHE A 1 572 ? 15.454 27.356 60.500 1.00 20.73 ? 572 PHE A CE1 1 ATOM 4391 C CE2 . PHE A 1 572 ? 15.731 25.967 58.546 1.00 19.47 ? 572 PHE A CE2 1 ATOM 4392 C CZ . PHE A 1 572 ? 15.545 27.239 59.107 1.00 18.25 ? 572 PHE A CZ 1 ATOM 4393 N N . LYS A 1 573 ? 14.082 24.125 64.259 1.00 20.85 ? 573 LYS A N 1 ATOM 4394 C CA . LYS A 1 573 ? 13.742 25.160 65.230 1.00 21.59 ? 573 LYS A CA 1 ATOM 4395 C C . LYS A 1 573 ? 14.673 26.382 65.140 1.00 20.99 ? 573 LYS A C 1 ATOM 4396 O O . LYS A 1 573 ? 14.243 27.531 65.314 1.00 23.57 ? 573 LYS A O 1 ATOM 4397 C CB . LYS A 1 573 ? 13.770 24.583 66.662 1.00 21.43 ? 573 LYS A CB 1 ATOM 4398 C CG . LYS A 1 573 ? 12.662 23.598 66.968 1.00 23.67 ? 573 LYS A CG 1 ATOM 4399 C CD . LYS A 1 573 ? 12.763 23.084 68.405 1.00 24.83 ? 573 LYS A CD 1 ATOM 4400 C CE . LYS A 1 573 ? 11.553 22.216 68.721 1.00 26.49 ? 573 LYS A CE 1 ATOM 4401 N NZ . LYS A 1 573 ? 11.707 21.664 70.107 1.00 28.93 ? 573 LYS A NZ 1 ATOM 4402 N N . SER A 1 574 ? 15.957 26.122 64.889 1.00 22.29 ? 574 SER A N 1 ATOM 4403 C CA . SER A 1 574 ? 16.963 27.152 64.764 1.00 23.23 ? 574 SER A CA 1 ATOM 4404 C C . SER A 1 574 ? 18.107 26.692 63.847 1.00 22.44 ? 574 SER A C 1 ATOM 4405 O O . SER A 1 574 ? 18.391 25.495 63.747 1.00 23.59 ? 574 SER A O 1 ATOM 4406 C CB . SER A 1 574 ? 17.469 27.504 66.173 1.00 25.31 ? 574 SER A CB 1 ATOM 4407 O OG A SER A 1 574 ? 18.812 27.919 66.104 0.60 27.14 ? 574 SER A OG 1 ATOM 4408 O OG B SER A 1 574 ? 17.970 26.345 66.818 0.40 24.31 ? 574 SER A OG 1 ATOM 4409 N N . VAL A 1 575 ? 18.715 27.658 63.172 1.00 24.08 ? 575 VAL A N 1 ATOM 4410 C CA . VAL A 1 575 ? 19.806 27.387 62.222 1.00 24.78 ? 575 VAL A CA 1 ATOM 4411 C C . VAL A 1 575 ? 21.023 26.789 62.952 1.00 25.99 ? 575 VAL A C 1 ATOM 4412 O O . VAL A 1 575 ? 21.802 26.090 62.339 1.00 25.28 ? 575 VAL A O 1 ATOM 4413 C CB . VAL A 1 575 ? 20.206 28.617 61.365 1.00 26.85 ? 575 VAL A CB 1 ATOM 4414 C CG1 . VAL A 1 575 ? 19.048 29.045 60.433 1.00 28.00 ? 575 VAL A CG1 1 ATOM 4415 C CG2 . VAL A 1 575 ? 20.706 29.772 62.223 1.00 31.18 ? 575 VAL A CG2 1 ATOM 4416 N N . ASP A 1 576 ? 21.122 27.036 64.265 1.00 28.05 ? 576 ASP A N 1 ATOM 4417 C CA . ASP A 1 576 ? 22.155 26.454 65.140 1.00 29.57 ? 576 ASP A CA 1 ATOM 4418 C C . ASP A 1 576 ? 22.119 24.954 65.189 1.00 29.20 ? 576 ASP A C 1 ATOM 4419 O O . ASP A 1 576 ? 23.107 24.316 65.584 1.00 29.85 ? 576 ASP A O 1 ATOM 4420 C CB . ASP A 1 576 ? 21.907 26.875 66.598 1.00 36.20 ? 576 ASP A CB 1 ATOM 4421 C CG . ASP A 1 576 ? 22.220 28.291 66.850 1.00 42.07 ? 576 ASP A CG 1 ATOM 4422 O OD1 . ASP A 1 576 ? 22.858 28.912 65.970 1.00 46.11 ? 576 ASP A OD1 1 ATOM 4423 O OD2 . ASP A 1 576 ? 21.824 28.778 67.941 1.00 45.95 ? 576 ASP A OD2 1 ATOM 4424 N N . GLN A 1 577 ? 20.985 24.367 64.846 1.00 24.68 ? 577 GLN A N 1 ATOM 4425 C CA . GLN A 1 577 ? 20.838 22.927 64.853 1.00 24.13 ? 577 GLN A CA 1 ATOM 4426 C C . GLN A 1 577 ? 21.467 22.272 63.619 1.00 25.07 ? 577 GLN A C 1 ATOM 4427 O O . GLN A 1 577 ? 21.630 21.040 63.572 1.00 25.17 ? 577 GLN A O 1 ATOM 4428 C CB . GLN A 1 577 ? 19.363 22.531 64.901 1.00 25.11 ? 577 GLN A CB 1 ATOM 4429 C CG . GLN A 1 577 ? 18.572 22.990 66.120 1.00 24.76 ? 577 GLN A CG 1 ATOM 4430 C CD . GLN A 1 577 ? 17.109 22.635 66.005 1.00 28.19 ? 577 GLN A CD 1 ATOM 4431 O OE1 . GLN A 1 577 ? 16.404 23.144 65.117 1.00 26.92 ? 577 GLN A OE1 1 ATOM 4432 N NE2 . GLN A 1 577 ? 16.625 21.779 66.885 1.00 26.88 ? 577 GLN A NE2 1 ATOM 4433 N N . LEU A 1 578 ? 21.771 23.072 62.596 1.00 25.07 ? 578 LEU A N 1 ATOM 4434 C CA . LEU A 1 578 ? 22.021 22.506 61.276 1.00 24.83 ? 578 LEU A CA 1 ATOM 4435 C C . LEU A 1 578 ? 23.470 22.020 61.109 1.00 25.64 ? 578 LEU A C 1 ATOM 4436 O O . LEU A 1 578 ? 24.374 22.655 61.608 1.00 28.96 ? 578 LEU A O 1 ATOM 4437 C CB . LEU A 1 578 ? 21.675 23.522 60.196 1.00 25.49 ? 578 LEU A CB 1 ATOM 4438 C CG . LEU A 1 578 ? 20.189 23.917 60.149 1.00 24.82 ? 578 LEU A CG 1 ATOM 4439 C CD1 . LEU A 1 578 ? 20.041 24.890 58.996 1.00 24.59 ? 578 LEU A CD1 1 ATOM 4440 C CD2 . LEU A 1 578 ? 19.286 22.685 59.985 1.00 24.60 ? 578 LEU A CD2 1 ATOM 4441 N N . PRO A 1 579 ? 23.688 20.936 60.362 1.00 27.49 ? 579 PRO A N 1 ATOM 4442 C CA . PRO A 1 579 ? 22.726 20.067 59.703 1.00 27.29 ? 579 PRO A CA 1 ATOM 4443 C C . PRO A 1 579 ? 22.052 19.157 60.723 1.00 27.37 ? 579 PRO A C 1 ATOM 4444 O O . PRO A 1 579 ? 22.697 18.708 61.705 1.00 27.88 ? 579 PRO A O 1 ATOM 4445 C CB . PRO A 1 579 ? 23.589 19.275 58.698 1.00 28.07 ? 579 PRO A CB 1 ATOM 4446 C CG . PRO A 1 579 ? 24.938 19.238 59.360 1.00 29.51 ? 579 PRO A CG 1 ATOM 4447 C CD . PRO A 1 579 ? 25.082 20.575 60.015 1.00 28.14 ? 579 PRO A CD 1 ATOM 4448 N N . MET A 1 580 ? 20.766 18.913 60.494 1.00 25.63 ? 580 MET A N 1 ATOM 4449 C CA . MET A 1 580 ? 19.961 18.120 61.395 1.00 24.67 ? 580 MET A CA 1 ATOM 4450 C C . MET A 1 580 ? 19.010 17.213 60.636 1.00 25.57 ? 580 MET A C 1 ATOM 4451 O O . MET A 1 580 ? 18.020 17.677 60.048 1.00 27.37 ? 580 MET A O 1 ATOM 4452 C CB . MET A 1 580 ? 19.184 19.033 62.346 1.00 23.75 ? 580 MET A CB 1 ATOM 4453 C CG . MET A 1 580 ? 18.478 18.334 63.509 1.00 23.54 ? 580 MET A CG 1 ATOM 4454 S SD A MET A 1 580 ? 17.234 19.091 64.549 0.60 21.54 ? 580 MET A SD 1 ATOM 4455 S SD B MET A 1 580 ? 17.862 19.703 64.544 0.40 20.79 ? 580 MET A SD 1 ATOM 4456 C CE A MET A 1 580 ? 16.096 19.824 63.362 0.60 20.36 ? 580 MET A CE 1 ATOM 4457 C CE B MET A 1 580 ? 16.564 20.393 63.494 0.40 20.21 ? 580 MET A CE 1 ATOM 4458 N N . ASN A 1 581 ? 19.311 15.920 60.641 1.00 26.35 ? 581 ASN A N 1 ATOM 4459 C CA . ASN A 1 581 ? 18.523 14.950 59.915 1.00 26.60 ? 581 ASN A CA 1 ATOM 4460 C C . ASN A 1 581 ? 18.065 13.820 60.797 1.00 29.82 ? 581 ASN A C 1 ATOM 4461 O O . ASN A 1 581 ? 18.633 13.578 61.871 1.00 31.94 ? 581 ASN A O 1 ATOM 4462 C CB . ASN A 1 581 ? 19.335 14.373 58.742 1.00 25.74 ? 581 ASN A CB 1 ATOM 4463 C CG . ASN A 1 581 ? 19.462 15.352 57.580 1.00 25.99 ? 581 ASN A CG 1 ATOM 4464 O OD1 . ASN A 1 581 ? 18.541 15.504 56.782 1.00 25.08 ? 581 ASN A OD1 1 ATOM 4465 N ND2 . ASN A 1 581 ? 20.596 16.027 57.494 1.00 24.45 ? 581 ASN A ND2 1 ATOM 4466 N N . VAL A 1 582 ? 17.035 13.133 60.323 1.00 31.22 ? 582 VAL A N 1 ATOM 4467 C CA . VAL A 1 582 ? 16.445 11.983 61.012 1.00 33.22 ? 582 VAL A CA 1 ATOM 4468 C C . VAL A 1 582 ? 17.515 10.985 61.413 1.00 35.15 ? 582 VAL A C 1 ATOM 4469 O O . VAL A 1 582 ? 18.344 10.572 60.594 1.00 35.41 ? 582 VAL A O 1 ATOM 4470 C CB . VAL A 1 582 ? 15.375 11.309 60.124 1.00 33.66 ? 582 VAL A CB 1 ATOM 4471 C CG1 . VAL A 1 582 ? 14.814 10.053 60.796 1.00 38.41 ? 582 VAL A CG1 1 ATOM 4472 C CG2 . VAL A 1 582 ? 14.269 12.310 59.775 1.00 35.56 ? 582 VAL A CG2 1 ATOM 4473 N N . GLY A 1 583 ? 17.529 10.632 62.693 1.00 38.36 ? 583 GLY A N 1 ATOM 4474 C CA . GLY A 1 583 ? 18.511 9.688 63.162 1.00 38.57 ? 583 GLY A CA 1 ATOM 4475 C C . GLY A 1 583 ? 19.672 10.367 63.841 1.00 41.02 ? 583 GLY A C 1 ATOM 4476 O O . GLY A 1 583 ? 20.445 9.705 64.531 1.00 43.40 ? 583 GLY A O 1 ATOM 4477 N N . ASP A 1 584 ? 19.815 11.680 63.665 1.00 37.28 ? 584 ASP A N 1 ATOM 4478 C CA . ASP A 1 584 ? 20.877 12.401 64.371 1.00 37.44 ? 584 ASP A CA 1 ATOM 4479 C C . ASP A 1 584 ? 20.514 12.469 65.853 1.00 36.67 ? 584 ASP A C 1 ATOM 4480 O O . ASP A 1 584 ? 19.335 12.556 66.199 1.00 35.90 ? 584 ASP A O 1 ATOM 4481 C CB . ASP A 1 584 ? 21.079 13.824 63.852 1.00 36.62 ? 584 ASP A CB 1 ATOM 4482 C CG . ASP A 1 584 ? 21.740 13.881 62.482 1.00 38.56 ? 584 ASP A CG 1 ATOM 4483 O OD1 . ASP A 1 584 ? 21.661 14.965 61.872 1.00 34.99 ? 584 ASP A OD1 1 ATOM 4484 O OD2 . ASP A 1 584 ? 22.357 12.885 62.020 1.00 38.21 ? 584 ASP A OD2 1 ATOM 4485 N N . ALA A 1 585 ? 21.535 12.429 66.712 1.00 38.24 ? 585 ALA A N 1 ATOM 4486 C CA . ALA A 1 585 ? 21.322 12.425 68.158 1.00 39.09 ? 585 ALA A CA 1 ATOM 4487 C C . ALA A 1 585 ? 20.633 13.717 68.619 1.00 39.05 ? 585 ALA A C 1 ATOM 4488 O O . ALA A 1 585 ? 19.939 13.716 69.635 1.00 37.03 ? 585 ALA A O 1 ATOM 4489 C CB . ALA A 1 585 ? 22.637 12.210 68.901 1.00 40.28 ? 585 ALA A CB 1 ATOM 4490 N N . HIS A 1 586 ? 20.799 14.804 67.852 1.00 35.48 ? 586 HIS A N 1 ATOM 4491 C CA . HIS A 1 586 ? 20.186 16.087 68.206 1.00 32.75 ? 586 HIS A CA 1 ATOM 4492 C C . HIS A 1 586 ? 18.912 16.382 67.408 1.00 32.29 ? 586 HIS A C 1 ATOM 4493 O O . HIS A 1 586 ? 18.424 17.511 67.471 1.00 34.18 ? 586 HIS A O 1 ATOM 4494 C CB . HIS A 1 586 ? 21.193 17.233 68.048 1.00 32.73 ? 586 HIS A CB 1 ATOM 4495 C CG . HIS A 1 586 ? 21.555 17.529 66.618 1.00 33.42 ? 586 HIS A CG 1 ATOM 4496 N ND1 . HIS A 1 586 ? 22.123 16.594 65.773 1.00 32.35 ? 586 HIS A ND1 1 ATOM 4497 C CD2 . HIS A 1 586 ? 21.425 18.666 65.889 1.00 31.69 ? 586 HIS A CD2 1 ATOM 4498 C CE1 . HIS A 1 586 ? 22.295 17.136 64.574 1.00 33.07 ? 586 HIS A CE1 1 ATOM 4499 N NE2 . HIS A 1 586 ? 21.886 18.394 64.622 1.00 30.69 ? 586 HIS A NE2 1 ATOM 4500 N N . TYR A 1 587 ? 18.352 15.374 66.724 1.00 31.01 ? 587 TYR A N 1 ATOM 4501 C CA . TYR A 1 587 ? 17.131 15.604 65.918 1.00 30.05 ? 587 TYR A CA 1 ATOM 4502 C C . TYR A 1 587 ? 16.010 16.146 66.799 1.00 31.06 ? 587 TYR A C 1 ATOM 4503 O O . TYR A 1 587 ? 15.552 15.467 67.734 1.00 31.43 ? 587 TYR A O 1 ATOM 4504 C CB . TYR A 1 587 ? 16.677 14.348 65.175 1.00 30.19 ? 587 TYR A CB 1 ATOM 4505 C CG . TYR A 1 587 ? 15.646 14.639 64.093 1.00 29.77 ? 587 TYR A CG 1 ATOM 4506 C CD1 . TYR A 1 587 ? 16.008 15.330 62.938 1.00 31.87 ? 587 TYR A CD1 1 ATOM 4507 C CD2 . TYR A 1 587 ? 14.323 14.217 64.226 1.00 31.30 ? 587 TYR A CD2 1 ATOM 4508 C CE1 . TYR A 1 587 ? 15.068 15.610 61.957 1.00 29.22 ? 587 TYR A CE1 1 ATOM 4509 C CE2 . TYR A 1 587 ? 13.365 14.487 63.239 1.00 31.71 ? 587 TYR A CE2 1 ATOM 4510 C CZ . TYR A 1 587 ? 13.761 15.170 62.083 1.00 30.13 ? 587 TYR A CZ 1 ATOM 4511 O OH . TYR A 1 587 ? 12.802 15.452 61.110 1.00 28.93 ? 587 TYR A OH 1 ATOM 4512 N N . ASP A 1 588 ? 15.597 17.388 66.555 1.00 27.57 ? 588 ASP A N 1 ATOM 4513 C CA . ASP A 1 588 ? 14.616 18.053 67.404 1.00 27.97 ? 588 ASP A CA 1 ATOM 4514 C C . ASP A 1 588 ? 13.864 19.072 66.534 1.00 25.51 ? 588 ASP A C 1 ATOM 4515 O O . ASP A 1 588 ? 14.131 20.258 66.611 1.00 25.29 ? 588 ASP A O 1 ATOM 4516 C CB . ASP A 1 588 ? 15.304 18.719 68.598 1.00 29.91 ? 588 ASP A CB 1 ATOM 4517 C CG . ASP A 1 588 ? 14.321 19.434 69.533 1.00 31.46 ? 588 ASP A CG 1 ATOM 4518 O OD1 . ASP A 1 588 ? 13.102 19.139 69.496 1.00 32.41 ? 588 ASP A OD1 1 ATOM 4519 O OD2 . ASP A 1 588 ? 14.784 20.314 70.298 1.00 33.62 ? 588 ASP A OD2 1 ATOM 4520 N N . PRO A 1 589 ? 12.926 18.574 65.731 1.00 24.77 ? 589 PRO A N 1 ATOM 4521 C CA . PRO A 1 589 ? 12.443 19.499 64.692 1.00 24.62 ? 589 PRO A CA 1 ATOM 4522 C C . PRO A 1 589 ? 11.309 20.356 65.215 1.00 23.98 ? 589 PRO A C 1 ATOM 4523 O O . PRO A 1 589 ? 10.614 19.980 66.191 1.00 25.90 ? 589 PRO A O 1 ATOM 4524 C CB . PRO A 1 589 ? 11.951 18.539 63.614 1.00 25.97 ? 589 PRO A CB 1 ATOM 4525 C CG . PRO A 1 589 ? 11.424 17.363 64.387 1.00 28.89 ? 589 PRO A CG 1 ATOM 4526 C CD . PRO A 1 589 ? 12.438 17.200 65.499 1.00 27.25 ? 589 PRO A CD 1 ATOM 4527 N N . LEU A 1 590 ? 11.096 21.519 64.594 1.00 21.70 ? 590 LEU A N 1 ATOM 4528 C CA . LEU A 1 590 ? 9.846 22.221 64.788 1.00 21.22 ? 590 LEU A CA 1 ATOM 4529 C C . LEU A 1 590 ? 8.687 21.463 64.137 1.00 20.80 ? 590 LEU A C 1 ATOM 4530 O O . LEU A 1 590 ? 7.618 21.334 64.742 1.00 23.33 ? 590 LEU A O 1 ATOM 4531 C CB . LEU A 1 590 ? 9.934 23.651 64.227 1.00 21.32 ? 590 LEU A CB 1 ATOM 4532 C CG . LEU A 1 590 ? 8.745 24.543 64.490 1.00 21.40 ? 590 LEU A CG 1 ATOM 4533 C CD1 . LEU A 1 590 ? 8.731 24.945 65.974 1.00 22.14 ? 590 LEU A CD1 1 ATOM 4534 C CD2 . LEU A 1 590 ? 8.888 25.781 63.640 1.00 22.22 ? 590 LEU A CD2 1 ATOM 4535 N N . PHE A 1 591 ? 8.871 21.023 62.889 1.00 19.45 ? 591 PHE A N 1 ATOM 4536 C CA . PHE A 1 591 ? 7.900 20.124 62.247 1.00 20.05 ? 591 PHE A CA 1 ATOM 4537 C C . PHE A 1 591 ? 8.675 19.017 61.603 1.00 21.87 ? 591 PHE A C 1 ATOM 4538 O O . PHE A 1 591 ? 9.694 19.271 60.929 1.00 21.65 ? 591 PHE A O 1 ATOM 4539 C CB . PHE A 1 591 ? 7.083 20.869 61.150 1.00 20.17 ? 591 PHE A CB 1 ATOM 4540 C CG . PHE A 1 591 ? 6.292 22.042 61.645 1.00 19.66 ? 591 PHE A CG 1 ATOM 4541 C CD1 . PHE A 1 591 ? 5.050 21.886 62.307 1.00 21.26 ? 591 PHE A CD1 1 ATOM 4542 C CD2 . PHE A 1 591 ? 6.737 23.345 61.392 1.00 20.50 ? 591 PHE A CD2 1 ATOM 4543 C CE1 . PHE A 1 591 ? 4.318 22.989 62.732 1.00 20.52 ? 591 PHE A CE1 1 ATOM 4544 C CE2 . PHE A 1 591 ? 6.006 24.445 61.805 1.00 20.42 ? 591 PHE A CE2 1 ATOM 4545 C CZ . PHE A 1 591 ? 4.791 24.278 62.487 1.00 20.53 ? 591 PHE A CZ 1 ATOM 4546 N N . ARG A 1 592 ? 8.195 17.786 61.752 1.00 22.92 ? 592 ARG A N 1 ATOM 4547 C CA . ARG A 1 592 ? 8.918 16.675 61.184 1.00 23.18 ? 592 ARG A CA 1 ATOM 4548 C C . ARG A 1 592 ? 8.645 16.527 59.678 1.00 22.26 ? 592 ARG A C 1 ATOM 4549 O O . ARG A 1 592 ? 7.634 17.016 59.148 1.00 20.49 ? 592 ARG A O 1 ATOM 4550 C CB . ARG A 1 592 ? 8.578 15.370 61.957 1.00 26.03 ? 592 ARG A CB 1 ATOM 4551 C CG . ARG A 1 592 ? 7.195 14.858 61.633 1.00 32.67 ? 592 ARG A CG 1 ATOM 4552 C CD . ARG A 1 592 ? 6.541 13.901 62.628 1.00 42.65 ? 592 ARG A CD 1 ATOM 4553 N NE . ARG A 1 592 ? 5.188 13.595 62.134 1.00 50.53 ? 592 ARG A NE 1 ATOM 4554 C CZ . ARG A 1 592 ? 4.153 14.447 62.159 1.00 54.50 ? 592 ARG A CZ 1 ATOM 4555 N NH1 . ARG A 1 592 ? 2.974 14.096 61.654 1.00 56.63 ? 592 ARG A NH1 1 ATOM 4556 N NH2 . ARG A 1 592 ? 4.287 15.653 62.691 1.00 58.68 ? 592 ARG A NH2 1 ATOM 4557 N N . LEU A 1 593 ? 9.559 15.843 58.992 1.00 22.54 ? 593 LEU A N 1 ATOM 4558 C CA . LEU A 1 593 ? 9.286 15.296 57.685 1.00 21.38 ? 593 LEU A CA 1 ATOM 4559 C C . LEU A 1 593 ? 7.919 14.566 57.670 1.00 22.17 ? 593 LEU A C 1 ATOM 4560 O O . LEU A 1 593 ? 7.611 13.744 58.565 1.00 21.87 ? 593 LEU A O 1 ATOM 4561 C CB . LEU A 1 593 ? 10.428 14.345 57.328 1.00 24.68 ? 593 LEU A CB 1 ATOM 4562 C CG . LEU A 1 593 ? 10.339 13.517 56.073 1.00 25.35 ? 593 LEU A CG 1 ATOM 4563 C CD1 . LEU A 1 593 ? 10.503 14.470 54.924 1.00 27.10 ? 593 LEU A CD1 1 ATOM 4564 C CD2 . LEU A 1 593 ? 11.525 12.569 56.085 1.00 26.53 ? 593 LEU A CD2 1 ATOM 4565 N N . GLY A 1 594 ? 7.070 14.891 56.704 1.00 19.99 ? 594 GLY A N 1 ATOM 4566 C CA . GLY A 1 594 ? 5.757 14.327 56.575 1.00 18.46 ? 594 GLY A CA 1 ATOM 4567 C C . GLY A 1 594 ? 4.626 15.084 57.271 1.00 18.47 ? 594 GLY A C 1 ATOM 4568 O O . GLY A 1 594 ? 3.454 14.769 57.065 1.00 19.07 ? 594 GLY A O 1 ATOM 4569 N N . TYR A 1 595 ? 4.981 16.117 58.034 1.00 18.58 ? 595 TYR A N 1 ATOM 4570 C CA . TYR A 1 595 ? 3.947 16.900 58.754 1.00 18.90 ? 595 TYR A CA 1 ATOM 4571 C C . TYR A 1 595 ? 3.081 17.697 57.768 1.00 18.12 ? 595 TYR A C 1 ATOM 4572 O O . TYR A 1 595 ? 3.600 18.250 56.770 1.00 18.04 ? 595 TYR A O 1 ATOM 4573 C CB . TYR A 1 595 ? 4.591 17.891 59.723 1.00 19.56 ? 595 TYR A CB 1 ATOM 4574 C CG . TYR A 1 595 ? 3.623 18.830 60.427 1.00 20.83 ? 595 TYR A CG 1 ATOM 4575 C CD1 . TYR A 1 595 ? 3.362 20.105 59.897 1.00 21.78 ? 595 TYR A CD1 1 ATOM 4576 C CD2 . TYR A 1 595 ? 2.955 18.460 61.601 1.00 24.55 ? 595 TYR A CD2 1 ATOM 4577 C CE1 . TYR A 1 595 ? 2.494 20.983 60.520 1.00 23.61 ? 595 TYR A CE1 1 ATOM 4578 C CE2 . TYR A 1 595 ? 2.064 19.355 62.202 1.00 23.36 ? 595 TYR A CE2 1 ATOM 4579 C CZ . TYR A 1 595 ? 1.847 20.591 61.638 1.00 24.20 ? 595 TYR A CZ 1 ATOM 4580 O OH . TYR A 1 595 ? 0.988 21.534 62.215 1.00 26.43 ? 595 TYR A OH 1 ATOM 4581 N N . GLY A 1 596 ? 1.787 17.802 58.044 1.00 17.40 ? 596 GLY A N 1 ATOM 4582 C CA . GLY A 1 596 ? 0.948 18.758 57.302 1.00 17.17 ? 596 GLY A CA 1 ATOM 4583 C C . GLY A 1 596 ? -0.500 18.633 57.770 1.00 19.13 ? 596 GLY A C 1 ATOM 4584 O O . GLY A 1 596 ? -1.010 17.520 57.941 1.00 22.17 ? 596 GLY A O 1 ATOM 4585 N N . LEU A 1 597 ? -1.144 19.763 57.970 1.00 17.35 ? 597 LEU A N 1 ATOM 4586 C CA . LEU A 1 597 ? -2.561 19.764 58.317 1.00 17.91 ? 597 LEU A CA 1 ATOM 4587 C C . LEU A 1 597 ? -3.421 19.608 57.076 1.00 19.24 ? 597 LEU A C 1 ATOM 4588 O O . LEU A 1 597 ? -2.978 19.854 55.932 1.00 20.26 ? 597 LEU A O 1 ATOM 4589 C CB . LEU A 1 597 ? -2.915 21.049 59.079 1.00 17.27 ? 597 LEU A CB 1 ATOM 4590 C CG . LEU A 1 597 ? -2.100 21.316 60.355 1.00 18.73 ? 597 LEU A CG 1 ATOM 4591 C CD1 . LEU A 1 597 ? -2.552 22.627 60.961 1.00 18.67 ? 597 LEU A CD1 1 ATOM 4592 C CD2 . LEU A 1 597 ? -2.306 20.183 61.377 1.00 20.21 ? 597 LEU A CD2 1 ATOM 4593 N N . THR A 1 598 ? -4.688 19.249 57.276 1.00 21.59 ? 598 THR A N 1 ATOM 4594 C CA . THR A 1 598 ? -5.579 19.100 56.144 1.00 21.89 ? 598 THR A CA 1 ATOM 4595 C C . THR A 1 598 ? -6.830 19.975 56.307 1.00 22.08 ? 598 THR A C 1 ATOM 4596 O O . THR A 1 598 ? -7.186 20.435 57.400 1.00 22.83 ? 598 THR A O 1 ATOM 4597 C CB . THR A 1 598 ? -5.982 17.638 55.931 1.00 24.41 ? 598 THR A CB 1 ATOM 4598 O OG1 . THR A 1 598 ? -6.650 17.201 57.113 1.00 28.19 ? 598 THR A OG1 1 ATOM 4599 C CG2 . THR A 1 598 ? -4.747 16.720 55.631 1.00 26.38 ? 598 THR A CG2 1 ATOM 4600 N N . THR A 1 599 ? -7.481 20.218 55.183 1.00 21.59 ? 599 THR A N 1 ATOM 4601 C CA . THR A 1 599 ? -8.827 20.747 55.185 1.00 21.09 ? 599 THR A CA 1 ATOM 4602 C C . THR A 1 599 ? -9.622 19.895 54.203 1.00 23.27 ? 599 THR A C 1 ATOM 4603 O O . THR A 1 599 ? -9.050 19.160 53.355 1.00 23.86 ? 599 THR A O 1 ATOM 4604 C CB . THR A 1 599 ? -8.897 22.209 54.697 1.00 21.31 ? 599 THR A CB 1 ATOM 4605 O OG1 . THR A 1 599 ? -8.305 22.282 53.387 1.00 20.13 ? 599 THR A OG1 1 ATOM 4606 C CG2 . THR A 1 599 ? -8.154 23.157 55.638 1.00 19.81 ? 599 THR A CG2 1 ATOM 4607 N N . ASN A 1 600 ? -10.948 20.024 54.301 1.00 25.59 ? 600 ASN A N 1 ATOM 4608 C CA . ASN A 1 600 ? -11.866 19.460 53.310 1.00 26.66 ? 600 ASN A CA 1 ATOM 4609 C C . ASN A 1 600 ? -12.401 20.538 52.376 1.00 28.30 ? 600 ASN A C 1 ATOM 4610 O O . ASN A 1 600 ? -12.671 21.684 52.816 1.00 27.40 ? 600 ASN A O 1 ATOM 4611 C CB . ASN A 1 600 ? -13.027 18.750 54.031 1.00 31.11 ? 600 ASN A CB 1 ATOM 4612 C CG . ASN A 1 600 ? -12.580 17.447 54.669 1.00 32.71 ? 600 ASN A CG 1 ATOM 4613 O OD1 . ASN A 1 600 ? -11.786 16.721 54.089 1.00 36.95 ? 600 ASN A OD1 1 ATOM 4614 N ND2 . ASN A 1 600 ? -13.068 17.159 55.858 1.00 35.11 ? 600 ASN A ND2 1 ATOM 4615 N N . ALA A 1 601 ? -12.535 20.180 51.104 1.00 30.06 ? 601 ALA A N 1 ATOM 4616 C CA . ALA A 1 601 ? -13.138 21.097 50.126 1.00 32.56 ? 601 ALA A CA 1 ATOM 4617 C C . ALA A 1 601 ? -14.548 21.555 50.558 1.00 34.84 ? 601 ALA A C 1 ATOM 4618 O O . ALA A 1 601 ? -15.294 20.773 51.179 1.00 32.11 ? 601 ALA A O 1 ATOM 4619 C CB . ALA A 1 601 ? -13.156 20.472 48.744 1.00 32.36 ? 601 ALA A CB 1 ATOM 4620 N N . THR A 1 602 ? -14.877 22.821 50.282 1.00 34.88 ? 602 THR A N 1 ATOM 4621 C CA . THR A 1 602 ? -16.221 23.361 50.579 1.00 40.18 ? 602 THR A CA 1 ATOM 4622 C C . THR A 1 602 ? -17.057 23.425 49.314 1.00 44.25 ? 602 THR A C 1 ATOM 4623 O O . THR A 1 602 ? -17.094 22.453 48.558 1.00 48.05 ? 602 THR A O 1 ATOM 4624 C CB . THR A 1 602 ? -16.213 24.739 51.301 1.00 44.07 ? 602 THR A CB 1 ATOM 4625 O OG1 . THR A 1 602 ? -15.245 25.619 50.727 1.00 40.47 ? 602 THR A OG1 1 ATOM 4626 C CG2 . THR A 1 602 ? -15.916 24.585 52.813 1.00 45.80 ? 602 THR A CG2 1 HETATM 4627 C C1 . NAG B 2 . ? -12.677 15.922 56.509 1.00 40.13 ? 701 NAG A C1 1 HETATM 4628 C C2 . NAG B 2 . ? -12.476 16.177 58.002 1.00 43.80 ? 701 NAG A C2 1 HETATM 4629 C C3 . NAG B 2 . ? -12.260 14.867 58.766 1.00 45.02 ? 701 NAG A C3 1 HETATM 4630 C C4 . NAG B 2 . ? -13.325 13.839 58.405 1.00 48.02 ? 701 NAG A C4 1 HETATM 4631 C C5 . NAG B 2 . ? -13.412 13.641 56.902 1.00 48.81 ? 701 NAG A C5 1 HETATM 4632 C C6 . NAG B 2 . ? -14.566 12.678 56.633 1.00 50.11 ? 701 NAG A C6 1 HETATM 4633 C C7 . NAG B 2 . ? -11.449 18.361 58.516 1.00 51.58 ? 701 NAG A C7 1 HETATM 4634 C C8 . NAG B 2 . ? -10.153 19.132 58.644 1.00 44.88 ? 701 NAG A C8 1 HETATM 4635 N N2 . NAG B 2 . ? -11.331 17.067 58.177 1.00 46.60 ? 701 NAG A N2 1 HETATM 4636 O O3 . NAG B 2 . ? -12.328 15.096 60.153 1.00 45.79 ? 701 NAG A O3 1 HETATM 4637 O O4 . NAG B 2 . ? -13.015 12.590 58.984 1.00 51.95 ? 701 NAG A O4 1 HETATM 4638 O O5 . NAG B 2 . ? -13.626 14.889 56.241 1.00 43.50 ? 701 NAG A O5 1 HETATM 4639 O O6 . NAG B 2 . ? -14.786 12.612 55.248 1.00 59.56 ? 701 NAG A O6 1 HETATM 4640 O O7 . NAG B 2 . ? -12.549 18.904 58.727 1.00 53.36 ? 701 NAG A O7 1 HETATM 4641 C C1 . GS1 C 3 . ? 25.667 25.393 35.982 1.00 14.86 ? 702 GS1 A C1 1 HETATM 4642 S S1 . GS1 C 3 . ? 26.282 26.926 36.681 1.00 16.33 ? 702 GS1 A S1 1 HETATM 4643 C C2 . GS1 C 3 . ? 24.664 24.628 36.894 1.00 13.38 ? 702 GS1 A C2 1 HETATM 4644 O O2 . GS1 C 3 . ? 25.421 24.132 38.011 1.00 14.52 ? 702 GS1 A O2 1 HETATM 4645 C C3 . GS1 C 3 . ? 23.982 23.478 36.159 1.00 13.81 ? 702 GS1 A C3 1 HETATM 4646 O O3 . GS1 C 3 . ? 22.896 22.971 36.964 1.00 13.93 ? 702 GS1 A O3 1 HETATM 4647 C C4 . GS1 C 3 . ? 23.394 23.973 34.833 1.00 13.08 ? 702 GS1 A C4 1 HETATM 4648 O O4 . GS1 C 3 . ? 22.823 22.903 34.121 1.00 13.88 ? 702 GS1 A O4 1 HETATM 4649 C C5 . GS1 C 3 . ? 24.548 24.605 34.033 1.00 14.39 ? 702 GS1 A C5 1 HETATM 4650 O O5 . GS1 C 3 . ? 25.055 25.741 34.739 1.00 14.06 ? 702 GS1 A O5 1 HETATM 4651 C C6 . GS1 C 3 . ? 24.219 25.069 32.598 1.00 14.54 ? 702 GS1 A C6 1 HETATM 4652 O O6 . GS1 C 3 . ? 23.315 26.191 32.661 1.00 14.93 ? 702 GS1 A O6 1 HETATM 4653 C C1 . MGL D 4 . ? 26.320 31.238 35.779 1.00 18.02 ? 703 MGL A C1 1 HETATM 4654 C C2 . MGL D 4 . ? 26.364 31.137 34.252 1.00 16.48 ? 703 MGL A C2 1 HETATM 4655 C C3 . MGL D 4 . ? 25.090 30.442 33.773 1.00 16.25 ? 703 MGL A C3 1 HETATM 4656 C C4 . MGL D 4 . ? 24.946 29.070 34.426 1.00 15.43 ? 703 MGL A C4 1 HETATM 4657 C C5 . MGL D 4 . ? 24.947 29.263 35.945 1.00 15.12 ? 703 MGL A C5 1 HETATM 4658 C C6 . MGL D 4 . ? 24.781 27.968 36.753 1.00 14.41 ? 703 MGL A C6 1 HETATM 4659 C C7 A MGL D 4 . ? 28.823 31.451 35.726 0.60 24.42 ? 703 MGL A C7 1 HETATM 4660 C C7 B MGL D 4 . ? 27.595 32.203 37.687 0.40 17.66 ? 703 MGL A C7 1 HETATM 4661 O O1 . MGL D 4 . ? 27.575 31.628 36.383 1.00 20.17 ? 703 MGL A O1 1 HETATM 4662 O O2 . MGL D 4 . ? 26.484 32.468 33.744 1.00 19.60 ? 703 MGL A O2 1 HETATM 4663 O O3 . MGL D 4 . ? 25.265 30.286 32.360 1.00 16.83 ? 703 MGL A O3 1 HETATM 4664 O O4 . MGL D 4 . ? 23.681 28.514 34.026 1.00 14.16 ? 703 MGL A O4 1 HETATM 4665 O O5 . MGL D 4 . ? 26.157 29.933 36.363 1.00 16.39 ? 703 MGL A O5 1 HETATM 4666 C C1 . GOL E 5 . ? 15.097 -0.600 14.462 1.00 70.49 ? 704 GOL A C1 1 HETATM 4667 O O1 . GOL E 5 . ? 15.998 -1.272 13.574 1.00 65.67 ? 704 GOL A O1 1 HETATM 4668 C C2 . GOL E 5 . ? 15.531 0.855 14.604 1.00 69.66 ? 704 GOL A C2 1 HETATM 4669 O O2 . GOL E 5 . ? 14.940 1.602 13.540 1.00 68.59 ? 704 GOL A O2 1 HETATM 4670 C C3 . GOL E 5 . ? 15.073 1.409 15.953 1.00 71.92 ? 704 GOL A C3 1 HETATM 4671 O O3 . GOL E 5 . ? 15.923 2.494 16.350 1.00 68.68 ? 704 GOL A O3 1 HETATM 4672 C C1 . GOL F 5 . ? 26.374 -2.883 25.079 1.00 65.79 ? 705 GOL A C1 1 HETATM 4673 O O1 . GOL F 5 . ? 27.351 -1.837 25.167 1.00 65.88 ? 705 GOL A O1 1 HETATM 4674 C C2 . GOL F 5 . ? 25.102 -2.338 24.435 1.00 63.16 ? 705 GOL A C2 1 HETATM 4675 O O2 . GOL F 5 . ? 25.403 -1.155 23.699 1.00 57.20 ? 705 GOL A O2 1 HETATM 4676 C C3 . GOL F 5 . ? 24.529 -3.352 23.459 1.00 64.95 ? 705 GOL A C3 1 HETATM 4677 O O3 . GOL F 5 . ? 23.648 -2.664 22.562 1.00 61.76 ? 705 GOL A O3 1 HETATM 4678 C C1 . GOL G 5 . ? 15.843 39.361 42.157 1.00 47.86 ? 706 GOL A C1 1 HETATM 4679 O O1 . GOL G 5 . ? 15.156 40.345 42.944 1.00 45.25 ? 706 GOL A O1 1 HETATM 4680 C C2 . GOL G 5 . ? 17.040 38.883 42.952 1.00 47.09 ? 706 GOL A C2 1 HETATM 4681 O O2 . GOL G 5 . ? 16.565 38.254 44.165 1.00 45.29 ? 706 GOL A O2 1 HETATM 4682 C C3 . GOL G 5 . ? 17.918 37.947 42.134 1.00 41.86 ? 706 GOL A C3 1 HETATM 4683 O O3 . GOL G 5 . ? 19.282 38.281 42.440 1.00 44.20 ? 706 GOL A O3 1 HETATM 4684 C C1 . GOL H 5 . ? 26.433 21.794 40.669 1.00 25.40 ? 707 GOL A C1 1 HETATM 4685 O O1 . GOL H 5 . ? 27.458 21.032 39.992 1.00 22.26 ? 707 GOL A O1 1 HETATM 4686 C C2 . GOL H 5 . ? 26.448 21.382 42.158 1.00 31.00 ? 707 GOL A C2 1 HETATM 4687 O O2 . GOL H 5 . ? 26.732 20.000 42.273 1.00 44.30 ? 707 GOL A O2 1 HETATM 4688 C C3 . GOL H 5 . ? 27.619 22.065 42.855 1.00 30.26 ? 707 GOL A C3 1 HETATM 4689 O O3 . GOL H 5 . ? 27.803 21.681 44.240 1.00 46.90 ? 707 GOL A O3 1 HETATM 4690 C C1 . GOL I 5 . ? 43.314 13.354 8.943 1.00 40.87 ? 708 GOL A C1 1 HETATM 4691 O O1 . GOL I 5 . ? 42.559 12.169 9.098 1.00 41.52 ? 708 GOL A O1 1 HETATM 4692 C C2 . GOL I 5 . ? 42.720 14.325 9.941 1.00 41.06 ? 708 GOL A C2 1 HETATM 4693 O O2 . GOL I 5 . ? 43.586 14.455 11.070 1.00 45.94 ? 708 GOL A O2 1 HETATM 4694 C C3 . GOL I 5 . ? 42.528 15.708 9.347 1.00 48.91 ? 708 GOL A C3 1 HETATM 4695 O O3 . GOL I 5 . ? 41.541 16.398 10.133 1.00 44.47 ? 708 GOL A O3 1 HETATM 4696 C C1 . GOL J 5 . ? 40.073 8.644 9.698 1.00 49.18 ? 709 GOL A C1 1 HETATM 4697 O O1 . GOL J 5 . ? 38.984 7.747 9.886 1.00 50.74 ? 709 GOL A O1 1 HETATM 4698 C C2 . GOL J 5 . ? 40.157 9.124 8.258 1.00 51.72 ? 709 GOL A C2 1 HETATM 4699 O O2 . GOL J 5 . ? 38.905 8.942 7.582 1.00 48.60 ? 709 GOL A O2 1 HETATM 4700 C C3 . GOL J 5 . ? 40.542 10.590 8.296 1.00 46.19 ? 709 GOL A C3 1 HETATM 4701 O O3 . GOL J 5 . ? 41.882 10.813 7.796 1.00 50.85 ? 709 GOL A O3 1 HETATM 4702 C C1 . GOL K 5 . ? 44.623 3.199 22.912 1.00 46.57 ? 710 GOL A C1 1 HETATM 4703 O O1 . GOL K 5 . ? 43.573 3.551 22.016 1.00 28.43 ? 710 GOL A O1 1 HETATM 4704 C C2 . GOL K 5 . ? 45.902 3.652 22.242 1.00 44.39 ? 710 GOL A C2 1 HETATM 4705 O O2 . GOL K 5 . ? 46.670 2.510 21.823 1.00 57.97 ? 710 GOL A O2 1 HETATM 4706 C C3 . GOL K 5 . ? 45.420 4.414 21.025 1.00 42.51 ? 710 GOL A C3 1 HETATM 4707 O O3 . GOL K 5 . ? 45.670 5.812 21.191 1.00 38.81 ? 710 GOL A O3 1 HETATM 4708 C C1 . GOL L 5 . ? 20.300 -4.817 9.805 1.00 58.28 ? 711 GOL A C1 1 HETATM 4709 O O1 . GOL L 5 . ? 19.528 -3.702 9.342 1.00 60.79 ? 711 GOL A O1 1 HETATM 4710 C C2 . GOL L 5 . ? 21.674 -4.345 10.266 1.00 60.49 ? 711 GOL A C2 1 HETATM 4711 O O2 . GOL L 5 . ? 22.178 -5.221 11.284 1.00 63.48 ? 711 GOL A O2 1 HETATM 4712 C C3 . GOL L 5 . ? 22.644 -4.337 9.096 1.00 60.53 ? 711 GOL A C3 1 HETATM 4713 O O3 . GOL L 5 . ? 23.782 -3.529 9.432 1.00 62.47 ? 711 GOL A O3 1 HETATM 4714 C C1 . GOL M 5 . ? 5.226 16.683 65.572 1.00 51.18 ? 712 GOL A C1 1 HETATM 4715 O O1 . GOL M 5 . ? 5.487 15.361 65.104 1.00 60.64 ? 712 GOL A O1 1 HETATM 4716 C C2 . GOL M 5 . ? 6.232 17.648 64.986 1.00 43.60 ? 712 GOL A C2 1 HETATM 4717 O O2 . GOL M 5 . ? 6.045 17.613 63.582 1.00 39.41 ? 712 GOL A O2 1 HETATM 4718 C C3 . GOL M 5 . ? 5.875 19.027 65.516 1.00 50.79 ? 712 GOL A C3 1 HETATM 4719 O O3 . GOL M 5 . ? 4.456 19.134 65.719 1.00 52.41 ? 712 GOL A O3 1 HETATM 4720 C C1 . GOL N 5 . ? 13.968 34.214 66.586 1.00 66.67 ? 713 GOL A C1 1 HETATM 4721 O O1 . GOL N 5 . ? 13.847 35.641 66.565 1.00 70.24 ? 713 GOL A O1 1 HETATM 4722 C C2 . GOL N 5 . ? 12.582 33.601 66.727 1.00 64.13 ? 713 GOL A C2 1 HETATM 4723 O O2 . GOL N 5 . ? 12.576 32.232 66.308 1.00 60.73 ? 713 GOL A O2 1 HETATM 4724 C C3 . GOL N 5 . ? 12.133 33.671 68.179 1.00 63.21 ? 713 GOL A C3 1 HETATM 4725 O O3 . GOL N 5 . ? 10.738 33.368 68.250 1.00 53.42 ? 713 GOL A O3 1 HETATM 4726 S S . SO4 O 6 . ? 39.278 29.728 43.044 1.00 95.71 ? 714 SO4 A S 1 HETATM 4727 O O1 . SO4 O 6 . ? 39.587 28.333 43.444 1.00 92.06 ? 714 SO4 A O1 1 HETATM 4728 O O2 . SO4 O 6 . ? 40.182 30.654 43.769 1.00 95.90 ? 714 SO4 A O2 1 HETATM 4729 O O3 . SO4 O 6 . ? 39.467 29.914 41.587 1.00 92.72 ? 714 SO4 A O3 1 HETATM 4730 O O4 . SO4 O 6 . ? 37.865 30.031 43.369 1.00 100.05 ? 714 SO4 A O4 1 HETATM 4731 S S . SO4 P 6 . ? -16.243 48.754 60.750 1.00 73.85 ? 715 SO4 A S 1 HETATM 4732 O O1 . SO4 P 6 . ? -15.090 47.964 61.231 1.00 77.33 ? 715 SO4 A O1 1 HETATM 4733 O O2 . SO4 P 6 . ? -17.194 48.938 61.871 1.00 78.15 ? 715 SO4 A O2 1 HETATM 4734 O O3 . SO4 P 6 . ? -15.756 50.063 60.259 1.00 78.17 ? 715 SO4 A O3 1 HETATM 4735 O O4 . SO4 P 6 . ? -16.898 48.031 59.628 1.00 78.65 ? 715 SO4 A O4 1 HETATM 4736 O O . HOH Q 7 . ? 19.448 41.451 31.705 1.00 48.08 ? 801 HOH A O 1 HETATM 4737 O O . HOH Q 7 . ? 27.364 29.274 39.185 1.00 47.83 ? 802 HOH A O 1 HETATM 4738 O O . HOH Q 7 . ? 13.856 44.158 26.516 1.00 43.54 ? 803 HOH A O 1 HETATM 4739 O O . HOH Q 7 . ? 30.086 33.190 30.510 1.00 45.90 ? 804 HOH A O 1 HETATM 4740 O O . HOH Q 7 . ? 27.986 37.696 27.602 1.00 47.01 ? 805 HOH A O 1 HETATM 4741 O O . HOH Q 7 . ? 22.963 35.843 32.690 1.00 41.79 ? 806 HOH A O 1 HETATM 4742 O O . HOH Q 7 . ? 28.731 33.608 33.154 1.00 47.24 ? 807 HOH A O 1 HETATM 4743 O O . HOH Q 7 . ? 48.475 22.553 23.485 1.00 35.49 ? 808 HOH A O 1 HETATM 4744 O O . HOH Q 7 . ? -14.731 17.894 50.814 1.00 54.66 ? 809 HOH A O 1 HETATM 4745 O O . HOH Q 7 . ? 11.096 35.897 69.383 1.00 53.38 ? 810 HOH A O 1 HETATM 4746 O O . HOH Q 7 . ? 2.427 40.468 66.648 1.00 41.71 ? 811 HOH A O 1 HETATM 4747 O O . HOH Q 7 . ? -8.375 43.165 66.287 1.00 64.66 ? 812 HOH A O 1 HETATM 4748 O O . HOH Q 7 . ? -8.176 46.217 67.204 1.00 55.05 ? 813 HOH A O 1 HETATM 4749 O O . HOH Q 7 . ? 16.456 33.834 64.794 1.00 51.71 ? 814 HOH A O 1 HETATM 4750 O O . HOH Q 7 . ? -1.874 56.652 66.559 1.00 46.71 ? 815 HOH A O 1 HETATM 4751 O O . HOH Q 7 . ? -15.331 48.324 44.291 1.00 54.94 ? 816 HOH A O 1 HETATM 4752 O O . HOH Q 7 . ? -8.098 43.310 37.481 1.00 36.58 ? 817 HOH A O 1 HETATM 4753 O O . HOH Q 7 . ? 1.884 44.092 39.106 1.00 44.87 ? 818 HOH A O 1 HETATM 4754 O O . HOH Q 7 . ? 0.206 41.965 32.340 1.00 58.75 ? 819 HOH A O 1 HETATM 4755 O O . HOH Q 7 . ? -23.088 42.622 53.574 1.00 42.83 ? 820 HOH A O 1 HETATM 4756 O O . HOH Q 7 . ? -2.849 16.272 59.627 1.00 44.04 ? 821 HOH A O 1 HETATM 4757 O O . HOH Q 7 . ? -2.542 24.441 21.752 1.00 48.70 ? 822 HOH A O 1 HETATM 4758 O O . HOH Q 7 . ? 16.565 17.131 7.217 1.00 51.47 ? 823 HOH A O 1 HETATM 4759 O O . HOH Q 7 . ? 11.585 9.149 12.031 1.00 48.45 ? 824 HOH A O 1 HETATM 4760 O O . HOH Q 7 . ? 43.948 12.714 37.054 1.00 48.12 ? 825 HOH A O 1 HETATM 4761 O O . HOH Q 7 . ? 42.634 29.480 30.038 1.00 57.73 ? 826 HOH A O 1 HETATM 4762 O O . HOH Q 7 . ? 47.334 20.771 38.945 1.00 46.64 ? 827 HOH A O 1 HETATM 4763 O O . HOH Q 7 . ? 49.911 20.853 32.723 1.00 47.80 ? 828 HOH A O 1 HETATM 4764 O O . HOH Q 7 . ? 48.553 18.189 31.912 1.00 34.28 ? 829 HOH A O 1 HETATM 4765 O O . HOH Q 7 . ? 52.283 20.344 29.561 1.00 45.71 ? 830 HOH A O 1 HETATM 4766 O O . HOH Q 7 . ? 37.559 2.932 36.954 1.00 53.19 ? 831 HOH A O 1 HETATM 4767 O O . HOH Q 7 . ? 39.475 4.071 38.482 1.00 47.35 ? 832 HOH A O 1 HETATM 4768 O O . HOH Q 7 . ? 33.238 2.688 42.995 1.00 57.64 ? 833 HOH A O 1 HETATM 4769 O O . HOH Q 7 . ? 23.004 3.050 45.761 1.00 46.56 ? 834 HOH A O 1 HETATM 4770 O O . HOH Q 7 . ? 26.944 7.388 56.947 1.00 50.11 ? 835 HOH A O 1 HETATM 4771 O O . HOH Q 7 . ? 24.551 8.521 56.439 1.00 51.24 ? 836 HOH A O 1 HETATM 4772 O O . HOH Q 7 . ? 19.521 8.216 56.659 1.00 49.88 ? 837 HOH A O 1 HETATM 4773 O O . HOH Q 7 . ? 18.344 5.854 53.152 1.00 45.44 ? 838 HOH A O 1 HETATM 4774 O O . HOH Q 7 . ? 15.212 7.328 53.714 1.00 50.65 ? 839 HOH A O 1 HETATM 4775 O O . HOH Q 7 . ? 13.927 10.141 56.194 1.00 48.49 ? 840 HOH A O 1 HETATM 4776 O O . HOH Q 7 . ? 20.757 -1.503 38.281 1.00 51.21 ? 841 HOH A O 1 HETATM 4777 O O . HOH Q 7 . ? 20.594 1.267 44.153 1.00 47.76 ? 842 HOH A O 1 HETATM 4778 O O . HOH Q 7 . ? 18.808 1.489 47.968 1.00 50.65 ? 843 HOH A O 1 HETATM 4779 O O . HOH Q 7 . ? 1.294 9.022 41.569 1.00 41.95 ? 844 HOH A O 1 HETATM 4780 O O . HOH Q 7 . ? 34.062 34.150 16.752 1.00 32.53 ? 845 HOH A O 1 HETATM 4781 O O . HOH Q 7 . ? 28.777 37.385 14.820 1.00 46.08 ? 846 HOH A O 1 HETATM 4782 O O . HOH Q 7 . ? 31.064 35.789 18.552 1.00 44.69 ? 847 HOH A O 1 HETATM 4783 O O . HOH Q 7 . ? 29.071 35.521 18.662 1.00 46.18 ? 848 HOH A O 1 HETATM 4784 O O . HOH Q 7 . ? 37.836 3.201 10.423 1.00 49.98 ? 849 HOH A O 1 HETATM 4785 O O . HOH Q 7 . ? 27.920 4.724 -1.319 1.00 44.49 ? 850 HOH A O 1 HETATM 4786 O O . HOH Q 7 . ? 28.984 5.681 -5.422 1.00 50.30 ? 851 HOH A O 1 HETATM 4787 O O . HOH Q 7 . ? 18.889 4.166 0.066 1.00 57.46 ? 852 HOH A O 1 HETATM 4788 O O . HOH Q 7 . ? 40.567 31.488 39.335 1.00 48.87 ? 853 HOH A O 1 HETATM 4789 O O . HOH Q 7 . ? 26.081 20.594 56.222 1.00 41.83 ? 854 HOH A O 1 HETATM 4790 O O . HOH Q 7 . ? 29.025 17.295 53.643 1.00 52.22 ? 855 HOH A O 1 HETATM 4791 O O . HOH Q 7 . ? 23.986 28.965 59.837 1.00 37.85 ? 856 HOH A O 1 HETATM 4792 O O . HOH Q 7 . ? 20.108 29.736 65.523 1.00 40.63 ? 857 HOH A O 1 HETATM 4793 O O . HOH Q 7 . ? 38.165 23.869 45.084 1.00 45.27 ? 858 HOH A O 1 HETATM 4794 O O . HOH Q 7 . ? 35.883 26.825 42.062 1.00 47.72 ? 859 HOH A O 1 HETATM 4795 O O . HOH Q 7 . ? 38.442 18.874 46.521 1.00 47.63 ? 860 HOH A O 1 HETATM 4796 O O . HOH Q 7 . ? 16.134 41.304 40.597 1.00 47.58 ? 861 HOH A O 1 HETATM 4797 O O . HOH Q 7 . ? 13.506 45.603 38.530 1.00 53.64 ? 862 HOH A O 1 HETATM 4798 O O . HOH Q 7 . ? 13.577 43.242 35.013 1.00 51.16 ? 863 HOH A O 1 HETATM 4799 O O . HOH Q 7 . ? 10.725 42.302 33.575 1.00 45.54 ? 864 HOH A O 1 HETATM 4800 O O . HOH Q 7 . ? 6.132 41.315 31.259 1.00 42.03 ? 865 HOH A O 1 HETATM 4801 O O . HOH Q 7 . ? 1.689 38.102 33.677 1.00 25.30 ? 866 HOH A O 1 HETATM 4802 O O . HOH Q 7 . ? -2.271 37.918 34.830 1.00 42.36 ? 867 HOH A O 1 HETATM 4803 O O . HOH Q 7 . ? 26.210 24.385 42.289 1.00 31.96 ? 868 HOH A O 1 HETATM 4804 O O . HOH Q 7 . ? 26.136 26.183 40.163 1.00 34.33 ? 869 HOH A O 1 HETATM 4805 O O . HOH Q 7 . ? 22.074 27.535 40.057 1.00 22.94 ? 870 HOH A O 1 HETATM 4806 O O . HOH Q 7 . ? 21.492 34.177 43.995 1.00 26.94 ? 871 HOH A O 1 HETATM 4807 O O . HOH Q 7 . ? 27.592 34.935 40.384 1.00 54.53 ? 872 HOH A O 1 HETATM 4808 O O . HOH Q 7 . ? 14.145 5.801 12.202 1.00 39.60 ? 873 HOH A O 1 HETATM 4809 O O . HOH Q 7 . ? 5.246 10.032 53.968 1.00 61.42 ? 874 HOH A O 1 HETATM 4810 O O . HOH Q 7 . ? -11.637 32.830 61.963 1.00 25.20 ? 875 HOH A O 1 HETATM 4811 O O . HOH Q 7 . ? -9.416 31.502 63.039 1.00 24.72 ? 876 HOH A O 1 HETATM 4812 O O . HOH Q 7 . ? 2.102 43.976 36.459 1.00 46.26 ? 877 HOH A O 1 HETATM 4813 O O . HOH Q 7 . ? 24.415 12.060 65.729 1.00 45.48 ? 878 HOH A O 1 HETATM 4814 O O . HOH Q 7 . ? 17.860 30.383 63.876 1.00 31.03 ? 879 HOH A O 1 HETATM 4815 O O . HOH Q 7 . ? -8.716 16.510 50.258 1.00 45.63 ? 880 HOH A O 1 HETATM 4816 O O . HOH Q 7 . ? -12.973 23.292 41.196 1.00 50.22 ? 881 HOH A O 1 HETATM 4817 O O . HOH Q 7 . ? -15.265 22.249 46.471 1.00 49.48 ? 882 HOH A O 1 HETATM 4818 O O . HOH Q 7 . ? -1.826 54.258 55.692 1.00 39.59 ? 883 HOH A O 1 HETATM 4819 O O . HOH Q 7 . ? 0.274 44.658 65.201 1.00 45.99 ? 884 HOH A O 1 HETATM 4820 O O . HOH Q 7 . ? 6.302 48.057 43.414 1.00 58.22 ? 885 HOH A O 1 HETATM 4821 O O . HOH Q 7 . ? 3.795 50.429 56.853 1.00 45.50 ? 886 HOH A O 1 HETATM 4822 O O . HOH Q 7 . ? 4.358 48.105 60.768 1.00 49.56 ? 887 HOH A O 1 HETATM 4823 O O . HOH Q 7 . ? -17.312 44.439 44.408 1.00 39.53 ? 888 HOH A O 1 HETATM 4824 O O . HOH Q 7 . ? -18.913 33.647 45.422 1.00 42.22 ? 889 HOH A O 1 HETATM 4825 O O . HOH Q 7 . ? -5.564 46.209 43.169 1.00 47.31 ? 890 HOH A O 1 HETATM 4826 O O . HOH Q 7 . ? -7.514 45.381 44.205 1.00 50.19 ? 891 HOH A O 1 HETATM 4827 O O . HOH Q 7 . ? 5.371 36.368 45.183 1.00 24.64 ? 892 HOH A O 1 HETATM 4828 O O . HOH Q 7 . ? 7.955 45.312 50.421 1.00 40.69 ? 893 HOH A O 1 HETATM 4829 O O . HOH Q 7 . ? -17.263 47.252 50.750 1.00 42.72 ? 894 HOH A O 1 HETATM 4830 O O . HOH Q 7 . ? -14.631 28.155 60.483 1.00 40.46 ? 895 HOH A O 1 HETATM 4831 O O . HOH Q 7 . ? -5.891 32.121 74.390 1.00 42.36 ? 896 HOH A O 1 HETATM 4832 O O . HOH Q 7 . ? -8.304 27.871 73.928 1.00 42.31 ? 897 HOH A O 1 HETATM 4833 O O . HOH Q 7 . ? -6.418 35.591 66.422 1.00 29.37 ? 898 HOH A O 1 HETATM 4834 O O . HOH Q 7 . ? -8.564 25.765 65.953 1.00 37.26 ? 899 HOH A O 1 HETATM 4835 O O . HOH Q 7 . ? -8.010 24.412 63.866 1.00 38.87 ? 900 HOH A O 1 HETATM 4836 O O . HOH Q 7 . ? -6.071 21.304 61.532 1.00 41.26 ? 901 HOH A O 1 HETATM 4837 O O . HOH Q 7 . ? -10.126 18.351 47.798 1.00 34.16 ? 902 HOH A O 1 HETATM 4838 O O . HOH Q 7 . ? -0.161 18.465 26.596 1.00 36.05 ? 903 HOH A O 1 HETATM 4839 O O . HOH Q 7 . ? 3.652 18.583 13.550 1.00 49.78 ? 904 HOH A O 1 HETATM 4840 O O . HOH Q 7 . ? 13.404 22.958 8.168 1.00 53.51 ? 905 HOH A O 1 HETATM 4841 O O . HOH Q 7 . ? 16.842 14.677 7.690 1.00 55.88 ? 906 HOH A O 1 HETATM 4842 O O . HOH Q 7 . ? 7.731 12.259 11.713 1.00 51.60 ? 907 HOH A O 1 HETATM 4843 O O . HOH Q 7 . ? 28.746 -1.288 17.453 1.00 42.87 ? 908 HOH A O 1 HETATM 4844 O O . HOH Q 7 . ? 22.957 6.474 55.685 1.00 49.59 ? 909 HOH A O 1 HETATM 4845 O O . HOH Q 7 . ? 9.138 8.207 51.827 1.00 51.72 ? 910 HOH A O 1 HETATM 4846 O O . HOH Q 7 . ? 45.258 28.492 30.086 1.00 45.98 ? 911 HOH A O 1 HETATM 4847 O O . HOH Q 7 . ? 7.109 36.187 23.399 1.00 30.84 ? 912 HOH A O 1 HETATM 4848 O O . HOH Q 7 . ? 45.286 27.092 23.130 1.00 46.64 ? 913 HOH A O 1 HETATM 4849 O O . HOH Q 7 . ? 39.221 27.249 16.896 1.00 38.49 ? 914 HOH A O 1 HETATM 4850 O O . HOH Q 7 . ? 33.137 34.817 26.434 1.00 49.84 ? 915 HOH A O 1 HETATM 4851 O O . HOH Q 7 . ? 50.158 16.706 26.330 1.00 30.60 ? 916 HOH A O 1 HETATM 4852 O O . HOH Q 7 . ? 42.522 24.619 35.596 1.00 20.39 ? 917 HOH A O 1 HETATM 4853 O O . HOH Q 7 . ? 34.699 31.002 30.206 1.00 41.49 ? 918 HOH A O 1 HETATM 4854 O O . HOH Q 7 . ? 23.376 2.553 43.292 1.00 38.73 ? 919 HOH A O 1 HETATM 4855 O O . HOH Q 7 . ? 28.027 -1.540 44.435 1.00 59.06 ? 920 HOH A O 1 HETATM 4856 O O . HOH Q 7 . ? 41.551 21.835 43.655 1.00 37.17 ? 921 HOH A O 1 HETATM 4857 O O . HOH Q 7 . ? 36.022 8.346 49.824 1.00 43.60 ? 922 HOH A O 1 HETATM 4858 O O . HOH Q 7 . ? 36.989 10.207 47.815 1.00 40.69 ? 923 HOH A O 1 HETATM 4859 O O . HOH Q 7 . ? 36.846 8.631 45.348 1.00 41.17 ? 924 HOH A O 1 HETATM 4860 O O . HOH Q 7 . ? 34.731 12.575 44.023 1.00 34.54 ? 925 HOH A O 1 HETATM 4861 O O . HOH Q 7 . ? 34.187 5.009 55.738 1.00 58.70 ? 926 HOH A O 1 HETATM 4862 O O . HOH Q 7 . ? 35.143 7.646 54.147 1.00 52.99 ? 927 HOH A O 1 HETATM 4863 O O . HOH Q 7 . ? 24.772 20.533 49.568 1.00 26.94 ? 928 HOH A O 1 HETATM 4864 O O . HOH Q 7 . ? 7.978 11.535 14.189 1.00 40.57 ? 929 HOH A O 1 HETATM 4865 O O . HOH Q 7 . ? 8.826 14.395 10.588 1.00 52.97 ? 930 HOH A O 1 HETATM 4866 O O . HOH Q 7 . ? 23.688 -4.617 31.053 1.00 48.52 ? 931 HOH A O 1 HETATM 4867 O O . HOH Q 7 . ? 8.878 4.185 31.256 1.00 38.97 ? 932 HOH A O 1 HETATM 4868 O O . HOH Q 7 . ? 19.620 27.026 42.051 1.00 19.61 ? 933 HOH A O 1 HETATM 4869 O O . HOH Q 7 . ? -0.852 6.350 38.025 1.00 58.85 ? 934 HOH A O 1 HETATM 4870 O O . HOH Q 7 . ? 6.083 3.584 38.115 1.00 55.28 ? 935 HOH A O 1 HETATM 4871 O O . HOH Q 7 . ? 4.547 8.312 46.200 1.00 54.36 ? 936 HOH A O 1 HETATM 4872 O O . HOH Q 7 . ? 7.203 11.566 54.756 1.00 38.87 ? 937 HOH A O 1 HETATM 4873 O O . HOH Q 7 . ? 37.153 27.452 30.054 1.00 39.50 ? 938 HOH A O 1 HETATM 4874 O O . HOH Q 7 . ? 37.825 30.971 31.268 1.00 48.66 ? 939 HOH A O 1 HETATM 4875 O O . HOH Q 7 . ? 47.841 19.617 24.857 0.80 19.09 ? 940 HOH A O 1 HETATM 4876 O O . HOH Q 7 . ? 50.070 18.451 24.184 1.00 35.47 ? 941 HOH A O 1 HETATM 4877 O O . HOH Q 7 . ? 51.617 15.658 24.507 1.00 32.56 ? 942 HOH A O 1 HETATM 4878 O O . HOH Q 7 . ? 51.529 16.916 22.194 1.00 32.81 ? 943 HOH A O 1 HETATM 4879 O O . HOH Q 7 . ? 52.572 10.066 26.730 1.00 34.80 ? 944 HOH A O 1 HETATM 4880 O O . HOH Q 7 . ? 50.709 16.172 20.216 1.00 39.06 ? 945 HOH A O 1 HETATM 4881 O O . HOH Q 7 . ? 49.626 11.439 16.949 1.00 47.92 ? 946 HOH A O 1 HETATM 4882 O O . HOH Q 7 . ? 44.694 14.446 13.295 1.00 38.14 ? 947 HOH A O 1 HETATM 4883 O O . HOH Q 7 . ? 10.616 4.680 43.481 1.00 41.98 ? 948 HOH A O 1 HETATM 4884 O O . HOH Q 7 . ? -2.131 13.850 43.986 1.00 34.46 ? 949 HOH A O 1 HETATM 4885 O O . HOH Q 7 . ? 24.985 14.033 53.364 1.00 26.54 ? 950 HOH A O 1 HETATM 4886 O O . HOH Q 7 . ? 16.400 13.922 57.528 1.00 25.89 ? 951 HOH A O 1 HETATM 4887 O O . HOH Q 7 . ? 16.287 11.391 56.307 1.00 34.40 ? 952 HOH A O 1 HETATM 4888 O O . HOH Q 7 . ? 18.482 10.502 57.847 1.00 32.31 ? 953 HOH A O 1 HETATM 4889 O O . HOH Q 7 . ? 15.891 16.045 43.832 1.00 15.39 ? 954 HOH A O 1 HETATM 4890 O O . HOH Q 7 . ? 22.695 14.756 46.698 1.00 16.80 ? 955 HOH A O 1 HETATM 4891 O O . HOH Q 7 . ? 4.408 32.245 31.105 1.00 15.20 ? 956 HOH A O 1 HETATM 4892 O O . HOH Q 7 . ? 8.588 28.241 40.549 1.00 12.58 ? 957 HOH A O 1 HETATM 4893 O O . HOH Q 7 . ? 14.849 27.197 30.072 1.00 12.14 ? 958 HOH A O 1 HETATM 4894 O O . HOH Q 7 . ? 11.616 30.208 9.571 1.00 38.78 ? 959 HOH A O 1 HETATM 4895 O O . HOH Q 7 . ? 12.856 34.623 14.196 1.00 31.28 ? 960 HOH A O 1 HETATM 4896 O O . HOH Q 7 . ? 13.841 42.314 22.697 1.00 37.26 ? 961 HOH A O 1 HETATM 4897 O O . HOH Q 7 . ? 16.562 42.190 23.782 1.00 39.00 ? 962 HOH A O 1 HETATM 4898 O O . HOH Q 7 . ? 21.519 36.286 26.510 1.00 26.75 ? 963 HOH A O 1 HETATM 4899 O O . HOH Q 7 . ? 19.800 38.554 25.153 1.00 20.98 ? 964 HOH A O 1 HETATM 4900 O O . HOH Q 7 . ? 16.164 36.358 29.996 1.00 21.38 ? 965 HOH A O 1 HETATM 4901 O O . HOH Q 7 . ? 23.341 -2.301 4.322 1.00 48.25 ? 966 HOH A O 1 HETATM 4902 O O . HOH Q 7 . ? 7.150 25.369 30.359 1.00 12.46 ? 967 HOH A O 1 HETATM 4903 O O . HOH Q 7 . ? 5.207 25.203 45.313 1.00 12.18 ? 968 HOH A O 1 HETATM 4904 O O . HOH Q 7 . ? 12.841 19.554 36.729 1.00 13.01 ? 969 HOH A O 1 HETATM 4905 O O . HOH Q 7 . ? 10.259 21.777 39.287 1.00 13.42 ? 970 HOH A O 1 HETATM 4906 O O . HOH Q 7 . ? 27.205 18.080 15.833 1.00 12.91 ? 971 HOH A O 1 HETATM 4907 O O . HOH Q 7 . ? 19.658 27.298 30.989 1.00 12.46 ? 972 HOH A O 1 HETATM 4908 O O . HOH Q 7 . ? 2.605 27.338 38.636 1.00 11.82 ? 973 HOH A O 1 HETATM 4909 O O . HOH Q 7 . ? 13.082 22.730 40.438 1.00 13.23 ? 974 HOH A O 1 HETATM 4910 O O . HOH Q 7 . ? 7.161 27.923 51.821 1.00 14.40 ? 975 HOH A O 1 HETATM 4911 O O . HOH Q 7 . ? 7.933 24.583 44.895 1.00 13.33 ? 976 HOH A O 1 HETATM 4912 O O . HOH Q 7 . ? 19.327 23.713 37.398 1.00 13.73 ? 977 HOH A O 1 HETATM 4913 O O . HOH Q 7 . ? 11.975 34.976 39.450 1.00 14.42 ? 978 HOH A O 1 HETATM 4914 O O . HOH Q 7 . ? 10.981 18.290 38.371 1.00 13.51 ? 979 HOH A O 1 HETATM 4915 O O . HOH Q 7 . ? 9.894 20.900 34.473 1.00 13.24 ? 980 HOH A O 1 HETATM 4916 O O . HOH Q 7 . ? -8.721 29.919 42.853 1.00 15.92 ? 981 HOH A O 1 HETATM 4917 O O . HOH Q 7 . ? 15.939 30.787 33.978 1.00 14.67 ? 982 HOH A O 1 HETATM 4918 O O . HOH Q 7 . ? 28.663 18.437 12.386 1.00 13.93 ? 983 HOH A O 1 HETATM 4919 O O . HOH Q 7 . ? 32.098 16.641 9.415 1.00 14.41 ? 984 HOH A O 1 HETATM 4920 O O . HOH Q 7 . ? 11.629 34.049 25.345 1.00 13.02 ? 985 HOH A O 1 HETATM 4921 O O . HOH Q 7 . ? 11.460 35.996 36.891 1.00 15.70 ? 986 HOH A O 1 HETATM 4922 O O . HOH Q 7 . ? 15.614 21.747 39.466 1.00 14.48 ? 987 HOH A O 1 HETATM 4923 O O . HOH Q 7 . ? 31.878 16.680 14.815 1.00 12.85 ? 988 HOH A O 1 HETATM 4924 O O . HOH Q 7 . ? -3.143 30.596 37.851 1.00 14.50 ? 989 HOH A O 1 HETATM 4925 O O . HOH Q 7 . ? 9.285 20.251 37.142 1.00 14.38 ? 990 HOH A O 1 HETATM 4926 O O . HOH Q 7 . ? 13.998 35.424 28.624 1.00 15.80 ? 991 HOH A O 1 HETATM 4927 O O . HOH Q 7 . ? 2.328 37.089 43.749 1.00 13.51 ? 992 HOH A O 1 HETATM 4928 O O . HOH Q 7 . ? 8.034 31.943 31.570 1.00 13.13 ? 993 HOH A O 1 HETATM 4929 O O . HOH Q 7 . ? 21.233 31.136 14.991 1.00 16.17 ? 994 HOH A O 1 HETATM 4930 O O . HOH Q 7 . ? 14.761 31.139 44.549 1.00 14.65 ? 995 HOH A O 1 HETATM 4931 O O . HOH Q 7 . ? -2.041 21.136 49.572 1.00 14.65 ? 996 HOH A O 1 HETATM 4932 O O . HOH Q 7 . ? 3.060 42.348 46.369 1.00 17.08 ? 997 HOH A O 1 HETATM 4933 O O . HOH Q 7 . ? 11.371 34.161 45.583 1.00 14.51 ? 998 HOH A O 1 HETATM 4934 O O . HOH Q 7 . ? 15.123 19.331 38.229 1.00 13.42 ? 999 HOH A O 1 HETATM 4935 O O . HOH Q 7 . ? 10.429 21.338 17.515 1.00 15.17 ? 1000 HOH A O 1 HETATM 4936 O O . HOH Q 7 . ? 31.044 16.862 12.030 1.00 15.69 ? 1001 HOH A O 1 HETATM 4937 O O . HOH Q 7 . ? 4.184 40.732 39.029 1.00 17.52 ? 1002 HOH A O 1 HETATM 4938 O O . HOH Q 7 . ? 9.450 34.131 61.222 1.00 18.28 ? 1003 HOH A O 1 HETATM 4939 O O . HOH Q 7 . ? 34.303 18.332 40.524 1.00 17.54 ? 1004 HOH A O 1 HETATM 4940 O O . HOH Q 7 . ? 13.814 35.437 25.898 1.00 17.99 ? 1005 HOH A O 1 HETATM 4941 O O . HOH Q 7 . ? 12.190 19.539 34.010 1.00 13.69 ? 1006 HOH A O 1 HETATM 4942 O O . HOH Q 7 . ? 29.253 20.893 13.715 1.00 14.71 ? 1007 HOH A O 1 HETATM 4943 O O . HOH Q 7 . ? 13.262 32.302 46.487 1.00 15.31 ? 1008 HOH A O 1 HETATM 4944 O O . HOH Q 7 . ? 22.151 33.737 19.462 1.00 15.29 ? 1009 HOH A O 1 HETATM 4945 O O . HOH Q 7 . ? -15.156 40.747 43.377 1.00 16.88 ? 1010 HOH A O 1 HETATM 4946 O O . HOH Q 7 . ? 22.406 14.398 42.455 1.00 16.81 ? 1011 HOH A O 1 HETATM 4947 O O . HOH Q 7 . ? 33.339 20.230 6.795 1.00 17.60 ? 1012 HOH A O 1 HETATM 4948 O O . HOH Q 7 . ? 21.427 33.400 16.698 1.00 18.86 ? 1013 HOH A O 1 HETATM 4949 O O . HOH Q 7 . ? 18.601 9.755 14.541 1.00 16.82 ? 1014 HOH A O 1 HETATM 4950 O O . HOH Q 7 . ? 19.260 9.062 45.858 1.00 20.58 ? 1015 HOH A O 1 HETATM 4951 O O . HOH Q 7 . ? -6.078 27.691 35.182 1.00 20.61 ? 1016 HOH A O 1 HETATM 4952 O O . HOH Q 7 . ? 34.069 22.353 31.941 1.00 16.77 ? 1017 HOH A O 1 HETATM 4953 O O . HOH Q 7 . ? -13.221 33.083 37.786 1.00 17.18 ? 1018 HOH A O 1 HETATM 4954 O O . HOH Q 7 . ? 13.179 20.529 17.935 1.00 19.19 ? 1019 HOH A O 1 HETATM 4955 O O . HOH Q 7 . ? 20.707 36.122 37.119 1.00 19.08 ? 1020 HOH A O 1 HETATM 4956 O O . HOH Q 7 . ? -0.690 17.139 48.114 1.00 16.95 ? 1021 HOH A O 1 HETATM 4957 O O . HOH Q 7 . ? 20.623 35.695 34.070 1.00 18.92 ? 1022 HOH A O 1 HETATM 4958 O O . HOH Q 7 . ? 12.137 37.530 28.420 1.00 18.86 ? 1023 HOH A O 1 HETATM 4959 O O . HOH Q 7 . ? 42.390 12.216 12.219 1.00 23.19 ? 1024 HOH A O 1 HETATM 4960 O O . HOH Q 7 . ? -15.879 43.158 55.494 1.00 18.40 ? 1025 HOH A O 1 HETATM 4961 O O . HOH Q 7 . ? 5.866 10.202 28.648 1.00 19.16 ? 1026 HOH A O 1 HETATM 4962 O O . HOH Q 7 . ? 37.178 20.201 16.422 1.00 18.77 ? 1027 HOH A O 1 HETATM 4963 O O . HOH Q 7 . ? -1.635 32.460 34.462 1.00 21.48 ? 1028 HOH A O 1 HETATM 4964 O O . HOH Q 7 . ? -12.831 40.401 41.887 1.00 17.79 ? 1029 HOH A O 1 HETATM 4965 O O . HOH Q 7 . ? 23.450 12.920 44.585 1.00 18.00 ? 1030 HOH A O 1 HETATM 4966 O O . HOH Q 7 . ? 9.714 18.651 17.256 1.00 18.47 ? 1031 HOH A O 1 HETATM 4967 O O . HOH Q 7 . ? 12.741 7.718 29.705 1.00 17.40 ? 1032 HOH A O 1 HETATM 4968 O O . HOH Q 7 . ? -1.194 20.570 54.027 1.00 16.43 ? 1033 HOH A O 1 HETATM 4969 O O . HOH Q 7 . ? 11.995 27.996 62.400 1.00 19.37 ? 1034 HOH A O 1 HETATM 4970 O O . HOH Q 7 . ? 47.170 21.059 19.744 1.00 18.79 ? 1035 HOH A O 1 HETATM 4971 O O . HOH Q 7 . ? 5.764 32.678 21.679 1.00 20.53 ? 1036 HOH A O 1 HETATM 4972 O O . HOH Q 7 . ? -5.671 23.330 41.828 1.00 19.93 ? 1037 HOH A O 1 HETATM 4973 O O . HOH Q 7 . ? 6.813 43.017 45.485 1.00 18.67 ? 1038 HOH A O 1 HETATM 4974 O O . HOH Q 7 . ? 7.262 17.868 16.253 1.00 21.72 ? 1039 HOH A O 1 HETATM 4975 O O . HOH Q 7 . ? -8.750 32.116 41.086 1.00 17.53 ? 1040 HOH A O 1 HETATM 4976 O O . HOH Q 7 . ? 15.474 18.918 16.416 1.00 17.29 ? 1041 HOH A O 1 HETATM 4977 O O . HOH Q 7 . ? 34.182 22.246 8.558 1.00 23.49 ? 1042 HOH A O 1 HETATM 4978 O O . HOH Q 7 . ? 13.557 13.219 17.132 1.00 20.42 ? 1043 HOH A O 1 HETATM 4979 O O . HOH Q 7 . ? 20.222 5.378 31.333 1.00 20.16 ? 1044 HOH A O 1 HETATM 4980 O O . HOH Q 7 . ? -2.881 29.985 28.673 1.00 21.70 ? 1045 HOH A O 1 HETATM 4981 O O . HOH Q 7 . ? 34.988 28.577 28.883 1.00 20.82 ? 1046 HOH A O 1 HETATM 4982 O O . HOH Q 7 . ? 7.958 11.977 19.983 1.00 23.96 ? 1047 HOH A O 1 HETATM 4983 O O . HOH Q 7 . ? 14.949 15.602 17.121 1.00 18.98 ? 1048 HOH A O 1 HETATM 4984 O O . HOH Q 7 . ? 9.956 11.386 15.928 1.00 25.82 ? 1049 HOH A O 1 HETATM 4985 O O . HOH Q 7 . ? 17.187 22.737 15.038 1.00 19.90 ? 1050 HOH A O 1 HETATM 4986 O O . HOH Q 7 . ? -0.627 15.421 45.982 1.00 21.04 ? 1051 HOH A O 1 HETATM 4987 O O . HOH Q 7 . ? 24.828 34.249 19.424 1.00 20.32 ? 1052 HOH A O 1 HETATM 4988 O O . HOH Q 7 . ? 1.091 14.944 50.180 1.00 23.81 ? 1053 HOH A O 1 HETATM 4989 O O . HOH Q 7 . ? 35.829 24.155 30.508 1.00 19.09 ? 1054 HOH A O 1 HETATM 4990 O O . HOH Q 7 . ? 37.042 28.903 14.739 1.00 25.77 ? 1055 HOH A O 1 HETATM 4991 O O . HOH Q 7 . ? -1.157 28.570 22.491 1.00 25.19 ? 1056 HOH A O 1 HETATM 4992 O O . HOH Q 7 . ? 35.551 9.490 6.102 1.00 20.73 ? 1057 HOH A O 1 HETATM 4993 O O . HOH Q 7 . ? -13.128 31.495 57.606 1.00 18.93 ? 1058 HOH A O 1 HETATM 4994 O O . HOH Q 7 . ? 18.679 37.419 29.727 1.00 21.95 ? 1059 HOH A O 1 HETATM 4995 O O . HOH Q 7 . ? 5.366 30.405 67.161 1.00 24.50 ? 1060 HOH A O 1 HETATM 4996 O O . HOH Q 7 . ? 35.479 29.774 12.741 1.00 25.18 ? 1061 HOH A O 1 HETATM 4997 O O . HOH Q 7 . ? 49.553 20.659 20.864 1.00 23.45 ? 1062 HOH A O 1 HETATM 4998 O O . HOH Q 7 . ? 15.689 36.106 50.461 1.00 22.44 ? 1063 HOH A O 1 HETATM 4999 O O . HOH Q 7 . ? -9.125 24.102 51.498 1.00 18.24 ? 1064 HOH A O 1 HETATM 5000 O O . HOH Q 7 . ? -17.655 39.120 56.427 1.00 26.49 ? 1065 HOH A O 1 HETATM 5001 O O . HOH Q 7 . ? 14.601 20.270 49.222 1.00 17.28 ? 1066 HOH A O 1 HETATM 5002 O O . HOH Q 7 . ? -14.080 30.959 39.496 1.00 21.27 ? 1067 HOH A O 1 HETATM 5003 O O . HOH Q 7 . ? -18.850 32.628 50.455 1.00 25.45 ? 1068 HOH A O 1 HETATM 5004 O O . HOH Q 7 . ? 15.040 21.811 16.616 1.00 22.72 ? 1069 HOH A O 1 HETATM 5005 O O . HOH Q 7 . ? 17.755 10.341 52.359 1.00 23.29 ? 1070 HOH A O 1 HETATM 5006 O O . HOH Q 7 . ? 20.187 10.953 44.086 1.00 19.52 ? 1071 HOH A O 1 HETATM 5007 O O . HOH Q 7 . ? 39.492 21.090 15.320 1.00 21.83 ? 1072 HOH A O 1 HETATM 5008 O O . HOH Q 7 . ? -11.387 23.837 57.880 1.00 23.51 ? 1073 HOH A O 1 HETATM 5009 O O . HOH Q 7 . ? 2.673 26.669 16.218 1.00 20.85 ? 1074 HOH A O 1 HETATM 5010 O O . HOH Q 7 . ? -4.759 37.484 64.133 1.00 19.32 ? 1075 HOH A O 1 HETATM 5011 O O . HOH Q 7 . ? -11.413 29.688 43.628 1.00 23.48 ? 1076 HOH A O 1 HETATM 5012 O O . HOH Q 7 . ? 9.675 38.911 52.974 1.00 22.64 ? 1077 HOH A O 1 HETATM 5013 O O . HOH Q 7 . ? 33.691 7.901 4.794 1.00 21.23 ? 1078 HOH A O 1 HETATM 5014 O O . HOH Q 7 . ? 4.072 30.343 21.076 1.00 22.35 ? 1079 HOH A O 1 HETATM 5015 O O . HOH Q 7 . ? -17.832 36.537 54.750 1.00 21.58 ? 1080 HOH A O 1 HETATM 5016 O O . HOH Q 7 . ? 5.908 28.625 14.152 1.00 24.39 ? 1081 HOH A O 1 HETATM 5017 O O . HOH Q 7 . ? 33.604 2.123 14.322 1.00 25.67 ? 1082 HOH A O 1 HETATM 5018 O O . HOH Q 7 . ? 11.505 18.409 15.005 1.00 22.47 ? 1083 HOH A O 1 HETATM 5019 O O . HOH Q 7 . ? 17.170 26.640 48.822 1.00 20.23 ? 1084 HOH A O 1 HETATM 5020 O O . HOH Q 7 . ? 5.507 8.016 27.024 1.00 23.96 ? 1085 HOH A O 1 HETATM 5021 O O . HOH Q 7 . ? 47.355 7.185 28.143 1.00 36.89 ? 1086 HOH A O 1 HETATM 5022 O O . HOH Q 7 . ? 47.887 5.854 25.938 1.00 48.11 ? 1087 HOH A O 1 HETATM 5023 O O . HOH Q 7 . ? 29.897 0.240 8.954 1.00 33.91 ? 1088 HOH A O 1 HETATM 5024 O O . HOH Q 7 . ? 18.215 0.015 3.870 1.00 39.84 ? 1089 HOH A O 1 HETATM 5025 O O . HOH Q 7 . ? 19.781 5.669 3.321 1.00 53.82 ? 1090 HOH A O 1 HETATM 5026 O O . HOH Q 7 . ? 16.866 7.151 6.108 1.00 36.90 ? 1091 HOH A O 1 HETATM 5027 O O . HOH Q 7 . ? 22.743 8.900 2.065 1.00 46.89 ? 1092 HOH A O 1 HETATM 5028 O O . HOH Q 7 . ? 41.890 15.606 12.562 1.00 23.45 ? 1093 HOH A O 1 HETATM 5029 O O . HOH Q 7 . ? 4.794 30.777 15.609 1.00 21.18 ? 1094 HOH A O 1 HETATM 5030 O O . HOH Q 7 . ? -11.446 42.767 42.430 1.00 22.54 ? 1095 HOH A O 1 HETATM 5031 O O . HOH Q 7 . ? -6.583 48.146 46.109 1.00 24.60 ? 1096 HOH A O 1 HETATM 5032 O O . HOH Q 7 . ? 17.660 18.030 55.813 1.00 24.80 ? 1097 HOH A O 1 HETATM 5033 O O . HOH Q 7 . ? 46.624 8.901 21.916 1.00 21.78 ? 1098 HOH A O 1 HETATM 5034 O O . HOH Q 7 . ? 21.521 0.981 20.754 1.00 24.41 ? 1099 HOH A O 1 HETATM 5035 O O . HOH Q 7 . ? 33.394 32.650 18.949 1.00 22.27 ? 1100 HOH A O 1 HETATM 5036 O O . HOH Q 7 . ? 21.061 -0.679 18.233 1.00 25.83 ? 1101 HOH A O 1 HETATM 5037 O O . HOH Q 7 . ? 5.941 32.001 17.996 1.00 20.26 ? 1102 HOH A O 1 HETATM 5038 O O . HOH Q 7 . ? 29.319 1.225 30.362 1.00 24.84 ? 1103 HOH A O 1 HETATM 5039 O O . HOH Q 7 . ? -10.482 45.678 59.258 1.00 22.07 ? 1104 HOH A O 1 HETATM 5040 O O . HOH Q 7 . ? 12.218 34.275 58.782 1.00 19.94 ? 1105 HOH A O 1 HETATM 5041 O O . HOH Q 7 . ? -17.078 30.455 49.687 1.00 25.07 ? 1106 HOH A O 1 HETATM 5042 O O . HOH Q 7 . ? 37.182 4.814 27.593 1.00 25.95 ? 1107 HOH A O 1 HETATM 5043 O O . HOH Q 7 . ? 2.672 45.217 42.784 1.00 25.29 ? 1108 HOH A O 1 HETATM 5044 O O . HOH Q 7 . ? -14.261 31.068 42.370 1.00 25.87 ? 1109 HOH A O 1 HETATM 5045 O O . HOH Q 7 . ? 27.184 14.710 4.901 1.00 23.53 ? 1110 HOH A O 1 HETATM 5046 O O . HOH Q 7 . ? 5.210 15.051 26.055 1.00 24.67 ? 1111 HOH A O 1 HETATM 5047 O O . HOH Q 7 . ? -13.184 27.921 57.559 1.00 24.19 ? 1112 HOH A O 1 HETATM 5048 O O . HOH Q 7 . ? 1.237 16.680 30.635 1.00 23.14 ? 1113 HOH A O 1 HETATM 5049 O O . HOH Q 7 . ? 39.743 3.075 19.885 1.00 27.11 ? 1114 HOH A O 1 HETATM 5050 O O . HOH Q 7 . ? 14.331 23.167 50.383 1.00 22.21 ? 1115 HOH A O 1 HETATM 5051 O O . HOH Q 7 . ? -4.617 42.675 40.078 1.00 26.27 ? 1116 HOH A O 1 HETATM 5052 O O . HOH Q 7 . ? 6.597 8.559 24.394 1.00 27.73 ? 1117 HOH A O 1 HETATM 5053 O O . HOH Q 7 . ? 19.615 2.940 21.296 1.00 25.23 ? 1118 HOH A O 1 HETATM 5054 O O . HOH Q 7 . ? 36.642 2.816 23.029 1.00 27.16 ? 1119 HOH A O 1 HETATM 5055 O O . HOH Q 7 . ? 23.183 -0.722 29.852 1.00 22.58 ? 1120 HOH A O 1 HETATM 5056 O O . HOH Q 7 . ? -15.564 36.313 56.558 1.00 22.69 ? 1121 HOH A O 1 HETATM 5057 O O . HOH Q 7 . ? 1.872 49.845 51.182 1.00 31.95 ? 1122 HOH A O 1 HETATM 5058 O O . HOH Q 7 . ? 5.897 42.552 52.912 1.00 18.54 ? 1123 HOH A O 1 HETATM 5059 O O . HOH Q 7 . ? -7.275 31.802 65.013 1.00 22.59 ? 1124 HOH A O 1 HETATM 5060 O O . HOH Q 7 . ? 4.273 44.468 45.034 1.00 23.33 ? 1125 HOH A O 1 HETATM 5061 O O . HOH Q 7 . ? 25.042 32.096 30.088 1.00 20.89 ? 1126 HOH A O 1 HETATM 5062 O O . HOH Q 7 . ? 13.708 18.206 11.315 1.00 25.12 ? 1127 HOH A O 1 HETATM 5063 O O . HOH Q 7 . ? 28.183 -0.473 11.193 1.00 26.36 ? 1128 HOH A O 1 HETATM 5064 O O . HOH Q 7 . ? -12.432 48.502 60.538 1.00 29.52 ? 1129 HOH A O 1 HETATM 5065 O O . HOH Q 7 . ? 2.124 30.333 22.822 1.00 28.53 ? 1130 HOH A O 1 HETATM 5066 O O . HOH Q 7 . ? 18.658 32.547 62.320 1.00 27.29 ? 1131 HOH A O 1 HETATM 5067 O O . HOH Q 7 . ? 21.764 0.112 36.091 1.00 24.43 ? 1132 HOH A O 1 HETATM 5068 O O . HOH Q 7 . ? 0.767 49.010 47.893 1.00 25.96 ? 1133 HOH A O 1 HETATM 5069 O O . HOH Q 7 . ? -4.048 29.364 34.376 1.00 24.34 ? 1134 HOH A O 1 HETATM 5070 O O . HOH Q 7 . ? 35.239 20.688 39.570 1.00 24.72 ? 1135 HOH A O 1 HETATM 5071 O O . HOH Q 7 . ? 36.047 3.266 14.696 1.00 26.13 ? 1136 HOH A O 1 HETATM 5072 O O . HOH Q 7 . ? 7.723 5.937 24.530 1.00 26.12 ? 1137 HOH A O 1 HETATM 5073 O O . HOH Q 7 . ? 8.329 35.537 15.913 1.00 23.26 ? 1138 HOH A O 1 HETATM 5074 O O . HOH Q 7 . ? 17.444 19.546 58.079 1.00 28.19 ? 1139 HOH A O 1 HETATM 5075 O O . HOH Q 7 . ? 33.047 3.354 9.146 1.00 30.20 ? 1140 HOH A O 1 HETATM 5076 O O . HOH Q 7 . ? -6.170 58.477 62.441 1.00 27.72 ? 1141 HOH A O 1 HETATM 5077 O O . HOH Q 7 . ? -9.638 31.042 35.743 1.00 26.41 ? 1142 HOH A O 1 HETATM 5078 O O . HOH Q 7 . ? 4.125 34.735 20.651 1.00 27.55 ? 1143 HOH A O 1 HETATM 5079 O O . HOH Q 7 . ? -3.678 25.125 63.933 1.00 23.62 ? 1144 HOH A O 1 HETATM 5080 O O . HOH Q 7 . ? 4.573 45.641 62.375 1.00 26.50 ? 1145 HOH A O 1 HETATM 5081 O O . HOH Q 7 . ? 18.184 4.210 13.608 1.00 31.11 ? 1146 HOH A O 1 HETATM 5082 O O . HOH Q 7 . ? 38.792 16.915 9.921 1.00 21.55 ? 1147 HOH A O 1 HETATM 5083 O O . HOH Q 7 . ? 50.156 18.340 18.588 1.00 24.30 ? 1148 HOH A O 1 HETATM 5084 O O . HOH Q 7 . ? 34.676 22.298 41.720 1.00 23.98 ? 1149 HOH A O 1 HETATM 5085 O O . HOH Q 7 . ? 5.348 37.385 65.917 1.00 23.44 ? 1150 HOH A O 1 HETATM 5086 O O . HOH Q 7 . ? 6.321 27.868 66.786 1.00 30.22 ? 1151 HOH A O 1 HETATM 5087 O O . HOH Q 7 . ? -12.625 44.449 44.178 1.00 24.21 ? 1152 HOH A O 1 HETATM 5088 O O . HOH Q 7 . ? 11.417 36.178 60.660 1.00 24.40 ? 1153 HOH A O 1 HETATM 5089 O O . HOH Q 7 . ? 13.070 9.136 14.336 1.00 31.32 ? 1154 HOH A O 1 HETATM 5090 O O . HOH Q 7 . ? 18.848 39.323 27.635 1.00 25.22 ? 1155 HOH A O 1 HETATM 5091 O O . HOH Q 7 . ? 29.785 16.095 2.588 1.00 29.41 ? 1156 HOH A O 1 HETATM 5092 O O . HOH Q 7 . ? 15.488 21.002 56.108 1.00 24.93 ? 1157 HOH A O 1 HETATM 5093 O O . HOH Q 7 . ? 6.814 44.432 37.100 1.00 31.33 ? 1158 HOH A O 1 HETATM 5094 O O . HOH Q 7 . ? 37.002 30.963 16.706 1.00 29.14 ? 1159 HOH A O 1 HETATM 5095 O O . HOH Q 7 . ? 39.780 23.703 16.355 1.00 22.88 ? 1160 HOH A O 1 HETATM 5096 O O . HOH Q 7 . ? 36.849 2.770 17.368 1.00 27.03 ? 1161 HOH A O 1 HETATM 5097 O O . HOH Q 7 . ? 15.575 36.579 18.191 1.00 25.08 ? 1162 HOH A O 1 HETATM 5098 O O . HOH Q 7 . ? -6.785 33.703 68.441 1.00 31.27 ? 1163 HOH A O 1 HETATM 5099 O O . HOH Q 7 . ? 12.548 11.641 15.102 1.00 26.78 ? 1164 HOH A O 1 HETATM 5100 O O . HOH Q 7 . ? 33.020 28.022 7.668 1.00 29.10 ? 1165 HOH A O 1 HETATM 5101 O O . HOH Q 7 . ? 32.457 2.435 28.194 1.00 27.30 ? 1166 HOH A O 1 HETATM 5102 O O . HOH Q 7 . ? -3.370 46.204 62.858 1.00 32.26 ? 1167 HOH A O 1 HETATM 5103 O O . HOH Q 7 . ? -15.155 28.634 51.157 1.00 26.51 ? 1168 HOH A O 1 HETATM 5104 O O . HOH Q 7 . ? -13.267 31.051 60.540 1.00 20.27 ? 1169 HOH A O 1 HETATM 5105 O O . HOH Q 7 . ? 29.597 2.601 24.766 1.00 29.04 ? 1170 HOH A O 1 HETATM 5106 O O . HOH Q 7 . ? -1.640 12.445 39.673 1.00 29.74 ? 1171 HOH A O 1 HETATM 5107 O O . HOH Q 7 . ? -6.134 22.945 37.391 1.00 30.69 ? 1172 HOH A O 1 HETATM 5108 O O . HOH Q 7 . ? 4.816 33.077 13.818 1.00 27.46 ? 1173 HOH A O 1 HETATM 5109 O O . HOH Q 7 . ? 8.573 4.428 35.320 1.00 30.30 ? 1174 HOH A O 1 HETATM 5110 O O . HOH Q 7 . ? 3.956 7.837 37.075 1.00 28.19 ? 1175 HOH A O 1 HETATM 5111 O O . HOH Q 7 . ? 32.679 33.595 13.340 1.00 29.40 ? 1176 HOH A O 1 HETATM 5112 O O . HOH Q 7 . ? 8.467 28.419 14.508 1.00 44.94 ? 1177 HOH A O 1 HETATM 5113 O O . HOH Q 7 . ? 34.226 3.024 21.482 1.00 31.63 ? 1178 HOH A O 1 HETATM 5114 O O . HOH Q 7 . ? 40.072 9.382 14.236 1.00 28.71 ? 1179 HOH A O 1 HETATM 5115 O O . HOH Q 7 . ? 13.530 8.200 18.789 1.00 30.05 ? 1180 HOH A O 1 HETATM 5116 O O . HOH Q 7 . ? 39.724 29.456 23.465 1.00 28.10 ? 1181 HOH A O 1 HETATM 5117 O O . HOH Q 7 . ? -1.402 38.827 65.445 1.00 27.56 ? 1182 HOH A O 1 HETATM 5118 O O . HOH Q 7 . ? -20.105 40.819 49.718 1.00 29.32 ? 1183 HOH A O 1 HETATM 5119 O O . HOH Q 7 . ? 12.307 24.426 11.123 1.00 25.34 ? 1184 HOH A O 1 HETATM 5120 O O . HOH Q 7 . ? 22.986 29.235 9.509 1.00 29.80 ? 1185 HOH A O 1 HETATM 5121 O O . HOH Q 7 . ? 25.061 17.635 55.604 1.00 38.36 ? 1186 HOH A O 1 HETATM 5122 O O . HOH Q 7 . ? -2.185 14.581 53.008 1.00 34.21 ? 1187 HOH A O 1 HETATM 5123 O O . HOH Q 7 . ? -10.690 44.235 61.763 1.00 30.04 ? 1188 HOH A O 1 HETATM 5124 O O . HOH Q 7 . ? 32.421 19.197 2.996 1.00 32.57 ? 1189 HOH A O 1 HETATM 5125 O O . HOH Q 7 . ? 37.669 30.011 21.693 1.00 24.71 ? 1190 HOH A O 1 HETATM 5126 O O . HOH Q 7 . ? -4.626 31.682 31.771 1.00 29.39 ? 1191 HOH A O 1 HETATM 5127 O O . HOH Q 7 . ? 12.189 38.455 59.004 1.00 24.35 ? 1192 HOH A O 1 HETATM 5128 O O . HOH Q 7 . ? 13.748 28.389 11.364 1.00 26.67 ? 1193 HOH A O 1 HETATM 5129 O O . HOH Q 7 . ? -7.149 16.248 42.774 1.00 38.48 ? 1194 HOH A O 1 HETATM 5130 O O . HOH Q 7 . ? -1.880 42.708 39.594 1.00 27.61 ? 1195 HOH A O 1 HETATM 5131 O O . HOH Q 7 . ? -7.462 36.027 69.843 1.00 32.02 ? 1196 HOH A O 1 HETATM 5132 O O . HOH Q 7 . ? 39.375 8.003 40.899 1.00 34.46 ? 1197 HOH A O 1 HETATM 5133 O O . HOH Q 7 . ? -13.514 26.826 74.527 1.00 28.85 ? 1198 HOH A O 1 HETATM 5134 O O . HOH Q 7 . ? -1.349 24.405 65.208 1.00 30.72 ? 1199 HOH A O 1 HETATM 5135 O O . HOH Q 7 . ? 53.330 15.678 20.463 1.00 28.54 ? 1200 HOH A O 1 HETATM 5136 O O . HOH Q 7 . ? -6.843 40.252 64.538 1.00 22.80 ? 1201 HOH A O 1 HETATM 5137 O O . HOH Q 7 . ? -2.693 18.262 28.311 1.00 40.71 ? 1202 HOH A O 1 HETATM 5138 O O . HOH Q 7 . ? 52.864 10.803 19.821 1.00 34.65 ? 1203 HOH A O 1 HETATM 5139 O O . HOH Q 7 . ? 32.256 2.699 23.823 1.00 30.45 ? 1204 HOH A O 1 HETATM 5140 O O . HOH Q 7 . ? 18.795 34.262 15.816 1.00 27.95 ? 1205 HOH A O 1 HETATM 5141 O O . HOH Q 7 . ? 28.250 1.242 18.374 1.00 28.38 ? 1206 HOH A O 1 HETATM 5142 O O . HOH Q 7 . ? 46.891 23.449 22.990 0.80 21.84 ? 1207 HOH A O 1 HETATM 5143 O O . HOH Q 7 . ? -1.867 32.989 31.805 1.00 27.33 ? 1208 HOH A O 1 HETATM 5144 O O . HOH Q 7 . ? -16.487 46.736 55.653 1.00 30.06 ? 1209 HOH A O 1 HETATM 5145 O O . HOH Q 7 . ? -9.669 50.308 52.628 1.00 40.50 ? 1210 HOH A O 1 HETATM 5146 O O . HOH Q 7 . ? -4.654 19.418 47.570 1.00 33.12 ? 1211 HOH A O 1 HETATM 5147 O O . HOH Q 7 . ? 22.391 20.593 51.221 1.00 28.29 ? 1212 HOH A O 1 HETATM 5148 O O . HOH Q 7 . ? 22.955 22.853 5.976 1.00 27.84 ? 1213 HOH A O 1 HETATM 5149 O O . HOH Q 7 . ? -1.982 35.648 32.608 1.00 29.42 ? 1214 HOH A O 1 HETATM 5150 O O . HOH Q 7 . ? 15.866 21.667 58.597 1.00 48.82 ? 1215 HOH A O 1 HETATM 5151 O O . HOH Q 7 . ? 24.782 19.690 66.081 1.00 54.63 ? 1216 HOH A O 1 HETATM 5152 O O . HOH Q 7 . ? 18.707 20.073 68.335 1.00 32.59 ? 1217 HOH A O 1 HETATM 5153 O O . HOH Q 7 . ? -16.962 21.511 53.810 1.00 40.40 ? 1218 HOH A O 1 HETATM 5154 O O . HOH Q 7 . ? 18.493 0.397 17.327 1.00 28.00 ? 1219 HOH A O 1 HETATM 5155 O O . HOH Q 7 . ? 8.401 44.768 46.686 1.00 30.34 ? 1220 HOH A O 1 HETATM 5156 O O . HOH Q 7 . ? 23.895 33.610 33.914 1.00 25.81 ? 1221 HOH A O 1 HETATM 5157 O O . HOH Q 7 . ? 10.775 26.744 12.587 1.00 29.49 ? 1222 HOH A O 1 HETATM 5158 O O . HOH Q 7 . ? 3.626 11.464 26.474 1.00 31.36 ? 1223 HOH A O 1 HETATM 5159 O O . HOH Q 7 . ? 11.684 1.719 33.670 1.00 30.73 ? 1224 HOH A O 1 HETATM 5160 O O . HOH Q 7 . ? -0.651 51.924 55.464 1.00 28.93 ? 1225 HOH A O 1 HETATM 5161 O O . HOH Q 7 . ? 7.366 33.905 23.860 1.00 28.23 ? 1226 HOH A O 1 HETATM 5162 O O . HOH Q 7 . ? -4.628 19.472 35.521 1.00 34.62 ? 1227 HOH A O 1 HETATM 5163 O O . HOH Q 7 . ? 0.267 40.896 65.341 1.00 28.67 ? 1228 HOH A O 1 HETATM 5164 O O . HOH Q 7 . ? 23.800 13.160 8.466 1.00 27.66 ? 1229 HOH A O 1 HETATM 5165 O O . HOH Q 7 . ? 29.682 -0.021 25.940 1.00 38.25 ? 1230 HOH A O 1 HETATM 5166 O O . HOH Q 7 . ? -0.296 52.263 62.473 1.00 35.95 ? 1231 HOH A O 1 HETATM 5167 O O . HOH Q 7 . ? 41.751 24.426 18.240 1.00 23.84 ? 1232 HOH A O 1 HETATM 5168 O O . HOH Q 7 . ? 34.713 20.690 45.046 1.00 31.21 ? 1233 HOH A O 1 HETATM 5169 O O . HOH Q 7 . ? -10.821 25.952 41.668 1.00 32.98 ? 1234 HOH A O 1 HETATM 5170 O O . HOH Q 7 . ? -3.990 36.094 34.852 1.00 30.61 ? 1235 HOH A O 1 HETATM 5171 O O . HOH Q 7 . ? 0.881 15.902 60.171 1.00 31.79 ? 1236 HOH A O 1 HETATM 5172 O O . HOH Q 7 . ? 7.786 6.536 41.295 1.00 32.59 ? 1237 HOH A O 1 HETATM 5173 O O . HOH Q 7 . ? 16.203 34.411 16.788 1.00 28.71 ? 1238 HOH A O 1 HETATM 5174 O O . HOH Q 7 . ? 17.942 2.708 23.636 1.00 27.27 ? 1239 HOH A O 1 HETATM 5175 O O . HOH Q 7 . ? 6.551 10.410 46.599 1.00 27.90 ? 1240 HOH A O 1 HETATM 5176 O O . HOH Q 7 . ? 10.582 18.062 12.586 1.00 37.27 ? 1241 HOH A O 1 HETATM 5177 O O . HOH Q 7 . ? 15.198 7.693 13.850 1.00 27.10 ? 1242 HOH A O 1 HETATM 5178 O O . HOH Q 7 . ? 15.962 1.520 46.690 1.00 39.12 ? 1243 HOH A O 1 HETATM 5179 O O . HOH Q 7 . ? 39.969 5.228 16.167 1.00 29.36 ? 1244 HOH A O 1 HETATM 5180 O O . HOH Q 7 . ? 23.453 13.684 55.470 1.00 30.25 ? 1245 HOH A O 1 HETATM 5181 O O . HOH Q 7 . ? 25.754 34.245 16.815 1.00 26.67 ? 1246 HOH A O 1 HETATM 5182 O O . HOH Q 7 . ? 32.845 1.262 16.991 1.00 29.72 ? 1247 HOH A O 1 HETATM 5183 O O . HOH Q 7 . ? 27.708 2.585 4.030 1.00 30.20 ? 1248 HOH A O 1 HETATM 5184 O O . HOH Q 7 . ? 22.358 6.600 3.072 1.00 36.01 ? 1249 HOH A O 1 HETATM 5185 O O . HOH Q 7 . ? 23.342 13.924 3.376 1.00 45.76 ? 1250 HOH A O 1 HETATM 5186 O O . HOH Q 7 . ? 22.763 20.542 4.848 1.00 48.69 ? 1251 HOH A O 1 HETATM 5187 O O . HOH Q 7 . ? 26.885 -2.724 10.035 1.00 43.37 ? 1252 HOH A O 1 HETATM 5188 O O . HOH Q 7 . ? 54.333 12.663 24.311 1.00 26.31 ? 1253 HOH A O 1 HETATM 5189 O O . HOH Q 7 . ? -10.776 29.213 37.524 1.00 30.06 ? 1254 HOH A O 1 HETATM 5190 O O . HOH Q 7 . ? 19.602 32.633 13.487 1.00 33.02 ? 1255 HOH A O 1 HETATM 5191 O O . HOH Q 7 . ? 14.190 41.867 44.714 1.00 38.11 ? 1256 HOH A O 1 HETATM 5192 O O . HOH Q 7 . ? 15.492 3.052 21.898 1.00 35.15 ? 1257 HOH A O 1 HETATM 5193 O O . HOH Q 7 . ? 17.654 1.711 19.692 1.00 36.01 ? 1258 HOH A O 1 HETATM 5194 O O . HOH Q 7 . ? 25.298 21.782 65.197 1.00 50.44 ? 1259 HOH A O 1 HETATM 5195 O O . HOH Q 7 . ? 8.092 33.726 68.046 1.00 29.75 ? 1260 HOH A O 1 HETATM 5196 O O . HOH Q 7 . ? 22.521 15.264 59.313 1.00 34.44 ? 1261 HOH A O 1 HETATM 5197 O O . HOH Q 7 . ? 35.773 31.878 22.641 1.00 31.32 ? 1262 HOH A O 1 HETATM 5198 O O . HOH Q 7 . ? 40.087 4.205 27.172 1.00 26.67 ? 1263 HOH A O 1 HETATM 5199 O O . HOH Q 7 . ? 0.968 24.763 63.987 1.00 31.45 ? 1264 HOH A O 1 HETATM 5200 O O . HOH Q 7 . ? 41.493 18.979 16.219 1.00 31.04 ? 1265 HOH A O 1 HETATM 5201 O O . HOH Q 7 . ? -19.599 34.789 55.725 1.00 32.88 ? 1266 HOH A O 1 HETATM 5202 O O . HOH Q 7 . ? 18.169 2.555 43.632 1.00 29.45 ? 1267 HOH A O 1 HETATM 5203 O O . HOH Q 7 . ? 18.870 8.939 23.702 1.00 23.74 ? 1268 HOH A O 1 HETATM 5204 O O . HOH Q 7 . ? -5.541 18.827 60.098 1.00 32.74 ? 1269 HOH A O 1 HETATM 5205 O O . HOH Q 7 . ? 38.323 1.326 21.473 1.00 33.40 ? 1270 HOH A O 1 HETATM 5206 O O . HOH Q 7 . ? -10.882 31.446 39.528 1.00 34.32 ? 1271 HOH A O 1 HETATM 5207 O O . HOH Q 7 . ? -7.844 29.869 33.676 1.00 29.11 ? 1272 HOH A O 1 HETATM 5208 O O . HOH Q 7 . ? 28.967 -3.441 29.371 1.00 43.51 ? 1273 HOH A O 1 HETATM 5209 O O . HOH Q 7 . ? 11.061 38.991 30.544 1.00 24.32 ? 1274 HOH A O 1 HETATM 5210 O O . HOH Q 7 . ? -15.011 26.789 47.516 1.00 29.68 ? 1275 HOH A O 1 HETATM 5211 O O . HOH Q 7 . ? 47.026 24.862 30.722 1.00 33.19 ? 1276 HOH A O 1 HETATM 5212 O O . HOH Q 7 . ? 9.840 41.511 22.622 1.00 42.49 ? 1277 HOH A O 1 HETATM 5213 O O . HOH Q 7 . ? -11.167 38.968 61.233 1.00 25.84 ? 1278 HOH A O 1 HETATM 5214 O O . HOH Q 7 . ? 13.879 30.342 66.021 1.00 49.82 ? 1279 HOH A O 1 HETATM 5215 O O . HOH Q 7 . ? 8.981 24.744 69.649 1.00 42.97 ? 1280 HOH A O 1 HETATM 5216 O O . HOH Q 7 . ? -5.918 14.390 42.098 1.00 39.42 ? 1281 HOH A O 1 HETATM 5217 O O . HOH Q 7 . ? 6.790 31.606 69.305 1.00 32.42 ? 1282 HOH A O 1 HETATM 5218 O O . HOH Q 7 . ? 8.697 2.756 24.225 1.00 37.37 ? 1283 HOH A O 1 HETATM 5219 O O . HOH Q 7 . ? 10.784 26.575 68.751 1.00 33.91 ? 1284 HOH A O 1 HETATM 5220 O O . HOH Q 7 . ? 2.933 37.763 67.139 1.00 28.95 ? 1285 HOH A O 1 HETATM 5221 O O . HOH Q 7 . ? 15.273 43.838 38.335 1.00 39.51 ? 1286 HOH A O 1 HETATM 5222 O O . HOH Q 7 . ? 15.745 39.688 57.567 1.00 33.83 ? 1287 HOH A O 1 HETATM 5223 O O . HOH Q 7 . ? 24.550 25.314 62.429 1.00 34.21 ? 1288 HOH A O 1 HETATM 5224 O O . HOH Q 7 . ? 29.671 32.783 10.617 1.00 31.40 ? 1289 HOH A O 1 HETATM 5225 O O . HOH Q 7 . ? 23.638 31.368 13.622 1.00 25.60 ? 1290 HOH A O 1 HETATM 5226 O O . HOH Q 7 . ? 34.636 33.666 21.104 1.00 28.82 ? 1291 HOH A O 1 HETATM 5227 O O . HOH Q 7 . ? 35.101 32.493 12.643 1.00 29.04 ? 1292 HOH A O 1 HETATM 5228 O O . HOH Q 7 . ? 1.840 16.783 20.210 1.00 51.77 ? 1293 HOH A O 1 HETATM 5229 O O . HOH Q 7 . ? 2.155 47.782 43.488 1.00 37.34 ? 1294 HOH A O 1 HETATM 5230 O O . HOH Q 7 . ? 10.726 35.364 14.345 1.00 31.50 ? 1295 HOH A O 1 HETATM 5231 O O . HOH Q 7 . ? -15.646 28.896 54.058 1.00 32.93 ? 1296 HOH A O 1 HETATM 5232 O O . HOH Q 7 . ? 42.534 2.814 19.652 1.00 37.14 ? 1297 HOH A O 1 HETATM 5233 O O . HOH Q 7 . ? 1.398 17.353 27.947 1.00 34.65 ? 1298 HOH A O 1 HETATM 5234 O O . HOH Q 7 . ? -6.319 33.314 72.357 1.00 32.65 ? 1299 HOH A O 1 HETATM 5235 O O . HOH Q 7 . ? 1.783 29.286 66.578 1.00 33.76 ? 1300 HOH A O 1 HETATM 5236 O O . HOH Q 7 . ? 10.521 -0.561 32.421 1.00 36.91 ? 1301 HOH A O 1 HETATM 5237 O O . HOH Q 7 . ? 10.463 43.489 47.860 1.00 32.98 ? 1302 HOH A O 1 HETATM 5238 O O . HOH Q 7 . ? 36.228 33.224 15.295 1.00 34.12 ? 1303 HOH A O 1 HETATM 5239 O O . HOH Q 7 . ? -11.923 21.575 56.372 1.00 30.96 ? 1304 HOH A O 1 HETATM 5240 O O . HOH Q 7 . ? 24.160 -2.824 28.857 1.00 37.13 ? 1305 HOH A O 1 HETATM 5241 O O . HOH Q 7 . ? 23.337 34.219 30.453 1.00 24.38 ? 1306 HOH A O 1 HETATM 5242 O O . HOH Q 7 . ? -4.469 25.688 72.164 1.00 36.78 ? 1307 HOH A O 1 HETATM 5243 O O . HOH Q 7 . ? 26.048 36.536 29.581 1.00 42.81 ? 1308 HOH A O 1 HETATM 5244 O O . HOH Q 7 . ? -7.407 23.679 29.346 1.00 30.64 ? 1309 HOH A O 1 HETATM 5245 O O . HOH Q 7 . ? -6.838 21.038 31.607 1.00 38.78 ? 1310 HOH A O 1 HETATM 5246 O O . HOH Q 7 . ? 21.234 21.344 68.310 1.00 36.85 ? 1311 HOH A O 1 HETATM 5247 O O . HOH Q 7 . ? 6.615 10.182 22.087 1.00 36.67 ? 1312 HOH A O 1 HETATM 5248 O O . HOH Q 7 . ? 29.981 15.296 46.043 1.00 31.12 ? 1313 HOH A O 1 HETATM 5249 O O . HOH Q 7 . ? -15.104 45.233 43.516 1.00 38.74 ? 1314 HOH A O 1 HETATM 5250 O O . HOH Q 7 . ? -1.011 15.073 55.871 1.00 42.86 ? 1315 HOH A O 1 HETATM 5251 O O . HOH Q 7 . ? 35.896 28.762 36.508 1.00 33.87 ? 1316 HOH A O 1 HETATM 5252 O O . HOH Q 7 . ? 3.974 45.300 35.194 1.00 47.93 ? 1317 HOH A O 1 HETATM 5253 O O . HOH Q 7 . ? 26.512 17.743 4.941 1.00 31.69 ? 1318 HOH A O 1 HETATM 5254 O O . HOH Q 7 . ? -23.038 38.619 44.119 1.00 36.94 ? 1319 HOH A O 1 HETATM 5255 O O . HOH Q 7 . ? -8.927 25.698 31.921 1.00 33.89 ? 1320 HOH A O 1 HETATM 5256 O O . HOH Q 7 . ? 3.136 21.093 66.134 1.00 44.95 ? 1321 HOH A O 1 HETATM 5257 O O . HOH Q 7 . ? 25.183 36.946 20.558 1.00 30.49 ? 1322 HOH A O 1 HETATM 5258 O O . HOH Q 7 . ? 37.463 6.044 13.839 1.00 29.68 ? 1323 HOH A O 1 HETATM 5259 O O . HOH Q 7 . ? 41.261 11.875 36.631 1.00 33.82 ? 1324 HOH A O 1 HETATM 5260 O O . HOH Q 7 . ? 6.929 36.365 68.066 1.00 33.89 ? 1325 HOH A O 1 HETATM 5261 O O . HOH Q 7 . ? 20.301 20.269 6.276 1.00 37.44 ? 1326 HOH A O 1 HETATM 5262 O O . HOH Q 7 . ? -7.283 22.535 59.307 1.00 28.14 ? 1327 HOH A O 1 HETATM 5263 O O . HOH Q 7 . ? -9.277 24.618 35.861 1.00 53.07 ? 1328 HOH A O 1 HETATM 5264 O O . HOH Q 7 . ? -2.900 54.281 58.502 1.00 39.43 ? 1329 HOH A O 1 HETATM 5265 O O . HOH Q 7 . ? -11.359 46.543 63.166 1.00 32.53 ? 1330 HOH A O 1 HETATM 5266 O O . HOH Q 7 . ? 5.945 5.686 34.057 1.00 34.53 ? 1331 HOH A O 1 HETATM 5267 O O . HOH Q 7 . ? 5.890 46.467 57.489 1.00 29.83 ? 1332 HOH A O 1 HETATM 5268 O O . HOH Q 7 . ? 35.138 6.004 30.579 1.00 36.82 ? 1333 HOH A O 1 HETATM 5269 O O . HOH Q 7 . ? -11.395 43.820 39.096 1.00 66.61 ? 1334 HOH A O 1 HETATM 5270 O O . HOH Q 7 . ? 30.035 -6.737 33.834 1.00 57.86 ? 1335 HOH A O 1 HETATM 5271 O O . HOH Q 7 . ? 17.825 -4.161 32.713 1.00 37.36 ? 1336 HOH A O 1 HETATM 5272 O O . HOH Q 7 . ? -16.535 26.377 55.266 1.00 42.49 ? 1337 HOH A O 1 HETATM 5273 O O . HOH Q 7 . ? -10.263 22.503 59.925 1.00 32.88 ? 1338 HOH A O 1 HETATM 5274 O O . HOH Q 7 . ? 30.890 2.617 18.408 1.00 32.18 ? 1339 HOH A O 1 HETATM 5275 O O . HOH Q 7 . ? 5.035 42.937 40.551 1.00 33.23 ? 1340 HOH A O 1 HETATM 5276 O O . HOH Q 7 . ? 39.934 6.448 31.272 1.00 30.44 ? 1341 HOH A O 1 HETATM 5277 O O . HOH Q 7 . ? 2.131 25.963 12.084 1.00 44.87 ? 1342 HOH A O 1 HETATM 5278 O O . HOH Q 7 . ? -12.535 19.224 45.409 1.00 38.02 ? 1343 HOH A O 1 HETATM 5279 O O . HOH Q 7 . ? 8.982 44.860 40.968 1.00 40.18 ? 1344 HOH A O 1 HETATM 5280 O O . HOH Q 7 . ? 12.101 7.893 16.712 1.00 42.27 ? 1345 HOH A O 1 HETATM 5281 O O . HOH Q 7 . ? 14.725 33.165 69.903 1.00 59.04 ? 1346 HOH A O 1 HETATM 5282 O O . HOH Q 7 . ? -15.322 50.214 55.530 1.00 44.81 ? 1347 HOH A O 1 HETATM 5283 O O . HOH Q 7 . ? -18.009 47.342 53.542 1.00 36.37 ? 1348 HOH A O 1 HETATM 5284 O O . HOH Q 7 . ? 5.501 27.753 9.581 1.00 31.14 ? 1349 HOH A O 1 HETATM 5285 O O . HOH Q 7 . ? 7.745 27.328 69.086 1.00 38.73 ? 1350 HOH A O 1 HETATM 5286 O O . HOH Q 7 . ? 13.170 39.833 61.165 1.00 38.87 ? 1351 HOH A O 1 HETATM 5287 O O . HOH Q 7 . ? 33.230 21.183 4.341 1.00 40.25 ? 1352 HOH A O 1 HETATM 5288 O O . HOH Q 7 . ? 4.025 39.825 30.989 1.00 41.21 ? 1353 HOH A O 1 HETATM 5289 O O . HOH Q 7 . ? 18.833 38.144 38.062 1.00 28.99 ? 1354 HOH A O 1 HETATM 5290 O O . HOH Q 7 . ? 36.198 2.262 26.593 1.00 46.85 ? 1355 HOH A O 1 HETATM 5291 O O . HOH Q 7 . ? 2.454 32.316 26.973 1.00 31.74 ? 1356 HOH A O 1 HETATM 5292 O O . HOH Q 7 . ? -15.359 49.215 49.975 1.00 40.89 ? 1357 HOH A O 1 HETATM 5293 O O . HOH Q 7 . ? 4.729 25.585 66.419 1.00 36.13 ? 1358 HOH A O 1 HETATM 5294 O O . HOH Q 7 . ? -1.029 31.094 68.118 1.00 36.57 ? 1359 HOH A O 1 HETATM 5295 O O . HOH Q 7 . ? 33.705 24.717 42.582 1.00 35.15 ? 1360 HOH A O 1 HETATM 5296 O O . HOH Q 7 . ? 27.115 -4.392 37.295 1.00 41.76 ? 1361 HOH A O 1 HETATM 5297 O O . HOH Q 7 . ? -18.682 45.374 49.676 1.00 33.02 ? 1362 HOH A O 1 HETATM 5298 O O . HOH Q 7 . ? -0.960 36.516 67.707 1.00 30.87 ? 1363 HOH A O 1 HETATM 5299 O O . HOH Q 7 . ? 40.507 16.077 43.224 1.00 34.53 ? 1364 HOH A O 1 HETATM 5300 O O . HOH Q 7 . ? 5.987 35.692 14.617 1.00 32.93 ? 1365 HOH A O 1 HETATM 5301 O O . HOH Q 7 . ? -11.533 27.642 76.229 1.00 44.00 ? 1366 HOH A O 1 HETATM 5302 O O . HOH Q 7 . ? -9.523 23.762 75.950 1.00 44.62 ? 1367 HOH A O 1 HETATM 5303 O O . HOH Q 7 . ? -7.771 17.445 47.549 1.00 40.76 ? 1368 HOH A O 1 HETATM 5304 O O . HOH Q 7 . ? 32.938 17.043 1.926 1.00 30.51 ? 1369 HOH A O 1 HETATM 5305 O O . HOH Q 7 . ? 31.176 34.910 11.773 1.00 38.64 ? 1370 HOH A O 1 HETATM 5306 O O . HOH Q 7 . ? -0.642 11.728 47.244 1.00 42.89 ? 1371 HOH A O 1 HETATM 5307 O O . HOH Q 7 . ? 45.704 27.127 32.541 1.00 31.63 ? 1372 HOH A O 1 HETATM 5308 O O . HOH Q 7 . ? 47.315 23.689 39.461 1.00 40.58 ? 1373 HOH A O 1 HETATM 5309 O O . HOH Q 7 . ? 3.646 47.749 58.372 1.00 37.36 ? 1374 HOH A O 1 HETATM 5310 O O . HOH Q 7 . ? 10.736 5.403 46.502 1.00 34.11 ? 1375 HOH A O 1 HETATM 5311 O O . HOH Q 7 . ? 11.112 20.406 10.847 1.00 38.76 ? 1376 HOH A O 1 HETATM 5312 O O . HOH Q 7 . ? 4.153 34.168 17.962 1.00 36.12 ? 1377 HOH A O 1 HETATM 5313 O O . HOH Q 7 . ? 13.673 1.995 39.025 1.00 34.28 ? 1378 HOH A O 1 HETATM 5314 O O . HOH Q 7 . ? -24.863 36.030 50.771 1.00 43.54 ? 1379 HOH A O 1 HETATM 5315 O O . HOH Q 7 . ? -19.362 45.465 46.973 1.00 42.84 ? 1380 HOH A O 1 HETATM 5316 O O . HOH Q 7 . ? 38.996 21.927 12.774 1.00 37.54 ? 1381 HOH A O 1 HETATM 5317 O O . HOH Q 7 . ? -2.637 16.585 33.173 1.00 38.66 ? 1382 HOH A O 1 HETATM 5318 O O . HOH Q 7 . ? -8.777 32.486 71.184 1.00 26.91 ? 1383 HOH A O 1 HETATM 5319 O O . HOH Q 7 . ? 18.866 8.559 3.939 1.00 47.12 ? 1384 HOH A O 1 HETATM 5320 O O . HOH Q 7 . ? 35.549 30.327 8.213 1.00 33.48 ? 1385 HOH A O 1 HETATM 5321 O O . HOH Q 7 . ? 7.199 40.683 24.927 1.00 54.14 ? 1386 HOH A O 1 HETATM 5322 O O . HOH Q 7 . ? 8.990 42.834 63.328 1.00 36.78 ? 1387 HOH A O 1 HETATM 5323 O O . HOH Q 7 . ? 15.881 42.249 55.845 1.00 31.52 ? 1388 HOH A O 1 HETATM 5324 O O . HOH Q 7 . ? 16.675 33.972 51.855 1.00 37.99 ? 1389 HOH A O 1 HETATM 5325 O O . HOH Q 7 . ? 34.383 10.032 55.302 1.00 54.14 ? 1390 HOH A O 1 HETATM 5326 O O . HOH Q 7 . ? 27.659 -2.547 15.308 1.00 43.84 ? 1391 HOH A O 1 HETATM 5327 O O . HOH Q 7 . ? 21.070 12.782 8.650 1.00 33.55 ? 1392 HOH A O 1 HETATM 5328 O O . HOH Q 7 . ? 9.920 5.442 57.521 1.00 55.23 ? 1393 HOH A O 1 HETATM 5329 O O . HOH Q 7 . ? 27.517 33.550 29.984 1.00 36.61 ? 1394 HOH A O 1 HETATM 5330 O O . HOH Q 7 . ? 29.418 5.148 2.261 1.00 36.25 ? 1395 HOH A O 1 HETATM 5331 O O . HOH Q 7 . ? 30.549 35.153 26.356 1.00 48.12 ? 1396 HOH A O 1 HETATM 5332 O O . HOH Q 7 . ? 27.315 37.389 22.287 1.00 38.20 ? 1397 HOH A O 1 HETATM 5333 O O . HOH Q 7 . ? 42.059 18.284 42.078 1.00 39.59 ? 1398 HOH A O 1 HETATM 5334 O O . HOH Q 7 . ? 2.776 6.199 34.668 1.00 43.37 ? 1399 HOH A O 1 HETATM 5335 O O . HOH Q 7 . ? 5.569 29.457 11.410 1.00 32.25 ? 1400 HOH A O 1 HETATM 5336 O O . HOH Q 7 . ? 13.756 39.319 34.013 1.00 31.94 ? 1401 HOH A O 1 HETATM 5337 O O . HOH Q 7 . ? 7.346 22.629 68.708 1.00 45.55 ? 1402 HOH A O 1 HETATM 5338 O O . HOH Q 7 . ? 14.144 1.385 50.197 1.00 61.84 ? 1403 HOH A O 1 HETATM 5339 O O . HOH Q 7 . ? 19.103 17.186 71.380 1.00 59.85 ? 1404 HOH A O 1 HETATM 5340 O O . HOH Q 7 . ? -7.383 16.934 52.500 1.00 36.88 ? 1405 HOH A O 1 HETATM 5341 O O . HOH Q 7 . ? -9.162 45.776 39.580 1.00 53.63 ? 1406 HOH A O 1 HETATM 5342 O O . HOH Q 7 . ? 10.852 42.385 61.475 1.00 50.54 ? 1407 HOH A O 1 HETATM 5343 O O . HOH Q 7 . ? -17.296 28.466 44.866 1.00 37.28 ? 1408 HOH A O 1 HETATM 5344 O O . HOH Q 7 . ? 5.397 14.597 23.525 1.00 27.44 ? 1409 HOH A O 1 HETATM 5345 O O . HOH Q 7 . ? 9.860 14.030 65.195 1.00 54.53 ? 1410 HOH A O 1 HETATM 5346 O O . HOH Q 7 . ? 12.943 36.397 63.083 1.00 36.02 ? 1411 HOH A O 1 HETATM 5347 O O . HOH Q 7 . ? 49.121 8.979 18.396 1.00 52.82 ? 1412 HOH A O 1 HETATM 5348 O O . HOH Q 7 . ? 2.969 48.458 46.108 1.00 37.91 ? 1413 HOH A O 1 HETATM 5349 O O . HOH Q 7 . ? 12.797 40.499 32.244 1.00 33.55 ? 1414 HOH A O 1 HETATM 5350 O O . HOH Q 7 . ? -11.457 17.657 50.296 1.00 44.99 ? 1415 HOH A O 1 HETATM 5351 O O . HOH Q 7 . ? 38.967 8.234 43.832 1.00 45.56 ? 1416 HOH A O 1 HETATM 5352 O O . HOH Q 7 . ? 21.859 -3.177 17.938 1.00 41.48 ? 1417 HOH A O 1 HETATM 5353 O O . HOH Q 7 . ? 5.988 7.915 20.268 1.00 50.18 ? 1418 HOH A O 1 HETATM 5354 O O . HOH Q 7 . ? -21.054 39.558 52.107 1.00 34.56 ? 1419 HOH A O 1 HETATM 5355 O O . HOH Q 7 . ? 16.278 1.042 42.450 1.00 42.34 ? 1420 HOH A O 1 HETATM 5356 O O . HOH Q 7 . ? 16.455 6.068 16.037 1.00 39.01 ? 1421 HOH A O 1 HETATM 5357 O O . HOH Q 7 . ? -3.070 12.588 48.928 1.00 54.84 ? 1422 HOH A O 1 HETATM 5358 O O . HOH Q 7 . ? 46.776 10.026 17.506 1.00 53.35 ? 1423 HOH A O 1 HETATM 5359 O O . HOH Q 7 . ? 34.700 -2.887 32.111 1.00 54.86 ? 1424 HOH A O 1 HETATM 5360 O O . HOH Q 7 . ? 19.158 41.638 28.566 1.00 45.41 ? 1425 HOH A O 1 HETATM 5361 O O . HOH Q 7 . ? 17.522 -1.710 25.850 1.00 34.86 ? 1426 HOH A O 1 HETATM 5362 O O . HOH Q 7 . ? 2.357 31.934 70.106 1.00 41.21 ? 1427 HOH A O 1 HETATM 5363 O O . HOH Q 7 . ? 24.283 33.877 14.474 1.00 37.59 ? 1428 HOH A O 1 HETATM 5364 O O . HOH Q 7 . ? -2.740 54.493 65.014 1.00 42.81 ? 1429 HOH A O 1 HETATM 5365 O O . HOH Q 7 . ? 24.161 -3.110 7.010 1.00 48.15 ? 1430 HOH A O 1 HETATM 5366 O O . HOH Q 7 . ? 7.355 45.600 42.470 1.00 46.28 ? 1431 HOH A O 1 HETATM 5367 O O . HOH Q 7 . ? 17.983 8.281 54.124 1.00 38.20 ? 1432 HOH A O 1 HETATM 5368 O O . HOH Q 7 . ? 2.262 46.547 63.798 1.00 41.95 ? 1433 HOH A O 1 HETATM 5369 O O . HOH Q 7 . ? 31.347 31.888 33.523 1.00 35.12 ? 1434 HOH A O 1 HETATM 5370 O O . HOH Q 7 . ? -5.060 31.923 34.729 1.00 34.94 ? 1435 HOH A O 1 HETATM 5371 O O . HOH Q 7 . ? 32.702 0.671 10.259 1.00 46.74 ? 1436 HOH A O 1 HETATM 5372 O O . HOH Q 7 . ? 33.471 3.205 6.553 1.00 51.39 ? 1437 HOH A O 1 HETATM 5373 O O . HOH Q 7 . ? 34.519 24.640 7.481 1.00 37.62 ? 1438 HOH A O 1 HETATM 5374 O O . HOH Q 7 . ? 17.662 10.256 7.950 1.00 39.65 ? 1439 HOH A O 1 HETATM 5375 O O . HOH Q 7 . ? 42.133 9.271 36.158 1.00 49.80 ? 1440 HOH A O 1 HETATM 5376 O O . HOH Q 7 . ? 2.343 26.716 65.272 1.00 34.27 ? 1441 HOH A O 1 HETATM 5377 O O . HOH Q 7 . ? 11.814 38.294 65.313 1.00 42.91 ? 1442 HOH A O 1 HETATM 5378 O O . HOH Q 7 . ? 12.885 2.796 44.081 1.00 43.85 ? 1443 HOH A O 1 HETATM 5379 O O . HOH Q 7 . ? 21.522 39.916 35.155 1.00 53.23 ? 1444 HOH A O 1 HETATM 5380 O O . HOH Q 7 . ? 8.078 4.970 21.987 1.00 36.78 ? 1445 HOH A O 1 HETATM 5381 O O . HOH Q 7 . ? -4.833 33.469 70.462 1.00 34.57 ? 1446 HOH A O 1 HETATM 5382 O O . HOH Q 7 . ? -19.153 23.020 52.697 1.00 35.58 ? 1447 HOH A O 1 HETATM 5383 O O . HOH Q 7 . ? -0.885 10.070 45.324 1.00 47.80 ? 1448 HOH A O 1 HETATM 5384 O O . HOH Q 7 . ? 10.083 4.836 40.704 1.00 45.93 ? 1449 HOH A O 1 HETATM 5385 O O . HOH Q 7 . ? -4.453 50.348 49.456 1.00 37.84 ? 1450 HOH A O 1 HETATM 5386 O O . HOH Q 7 . ? 6.815 9.970 51.853 1.00 44.73 ? 1451 HOH A O 1 HETATM 5387 O O . HOH Q 7 . ? 19.720 39.031 31.490 1.00 32.99 ? 1452 HOH A O 1 HETATM 5388 O O . HOH Q 7 . ? 27.192 23.641 60.541 1.00 41.54 ? 1453 HOH A O 1 HETATM 5389 O O . HOH Q 7 . ? 38.587 31.405 19.436 1.00 38.12 ? 1454 HOH A O 1 HETATM 5390 O O . HOH Q 7 . ? -19.962 22.323 48.128 1.00 52.03 ? 1455 HOH A O 1 HETATM 5391 O O . HOH Q 7 . ? -14.511 22.590 54.821 1.00 38.72 ? 1456 HOH A O 1 HETATM 5392 O O . HOH Q 7 . ? -14.289 24.454 57.853 1.00 55.10 ? 1457 HOH A O 1 HETATM 5393 O O . HOH Q 7 . ? -14.688 22.908 59.859 1.00 48.55 ? 1458 HOH A O 1 HETATM 5394 O O . HOH Q 7 . ? -14.320 17.048 60.661 1.00 39.19 ? 1459 HOH A O 1 HETATM 5395 O O . HOH Q 7 . ? 2.924 30.453 68.120 1.00 36.45 ? 1460 HOH A O 1 HETATM 5396 O O . HOH Q 7 . ? 14.204 5.641 20.571 1.00 35.90 ? 1461 HOH A O 1 HETATM 5397 O O . HOH Q 7 . ? 16.343 0.262 50.097 1.00 49.17 ? 1462 HOH A O 1 HETATM 5398 O O . HOH Q 7 . ? 19.559 30.214 8.587 1.00 56.16 ? 1463 HOH A O 1 HETATM 5399 O O . HOH Q 7 . ? -6.647 21.412 39.945 1.00 34.19 ? 1464 HOH A O 1 HETATM 5400 O O . HOH Q 7 . ? 43.675 8.639 7.376 1.00 33.68 ? 1465 HOH A O 1 HETATM 5401 O O . HOH Q 7 . ? 1.881 8.956 30.983 1.00 49.68 ? 1466 HOH A O 1 HETATM 5402 O O . HOH Q 7 . ? -11.933 40.852 62.541 1.00 27.73 ? 1467 HOH A O 1 HETATM 5403 O O . HOH Q 7 . ? 14.336 29.363 68.625 1.00 51.75 ? 1468 HOH A O 1 HETATM 5404 O O . HOH Q 7 . ? 30.618 -2.703 31.070 1.00 46.04 ? 1469 HOH A O 1 HETATM 5405 O O . HOH Q 7 . ? -8.346 52.017 56.659 1.00 40.97 ? 1470 HOH A O 1 HETATM 5406 O O . HOH Q 7 . ? 1.356 21.548 18.216 1.00 41.57 ? 1471 HOH A O 1 HETATM 5407 O O . HOH Q 7 . ? 2.113 49.301 61.932 1.00 41.25 ? 1472 HOH A O 1 HETATM 5408 O O . HOH Q 7 . ? 29.257 -2.337 13.129 1.00 52.96 ? 1473 HOH A O 1 HETATM 5409 O O . HOH Q 7 . ? -18.798 50.507 56.749 1.00 44.81 ? 1474 HOH A O 1 HETATM 5410 O O . HOH Q 7 . ? 8.056 1.669 30.606 1.00 44.09 ? 1475 HOH A O 1 HETATM 5411 O O . HOH Q 7 . ? 9.178 22.919 8.606 1.00 44.52 ? 1476 HOH A O 1 HETATM 5412 O O . HOH Q 7 . ? 11.763 23.994 71.885 1.00 50.12 ? 1477 HOH A O 1 HETATM 5413 O O . HOH Q 7 . ? 17.853 39.930 45.890 1.00 41.44 ? 1478 HOH A O 1 HETATM 5414 O O . HOH Q 7 . ? 27.369 38.420 19.400 1.00 54.35 ? 1479 HOH A O 1 HETATM 5415 O O . HOH Q 7 . ? 32.330 1.995 4.304 1.00 50.60 ? 1480 HOH A O 1 HETATM 5416 O O . HOH Q 7 . ? 28.031 -1.667 20.449 1.00 44.53 ? 1481 HOH A O 1 HETATM 5417 O O . HOH Q 7 . ? 34.105 2.902 30.327 1.00 45.01 ? 1482 HOH A O 1 HETATM 5418 O O . HOH Q 7 . ? 10.840 46.487 40.070 1.00 57.05 ? 1483 HOH A O 1 HETATM 5419 O O . HOH Q 7 . ? 42.883 5.392 15.961 1.00 56.09 ? 1484 HOH A O 1 HETATM 5420 O O . HOH Q 7 . ? 22.768 -3.131 35.419 1.00 45.48 ? 1485 HOH A O 1 HETATM 5421 O O . HOH Q 7 . ? 9.037 40.380 66.314 1.00 40.17 ? 1486 HOH A O 1 HETATM 5422 O O . HOH Q 7 . ? 38.020 4.918 30.391 1.00 37.16 ? 1487 HOH A O 1 HETATM 5423 O O . HOH Q 7 . ? 41.547 6.331 39.921 1.00 56.55 ? 1488 HOH A O 1 HETATM 5424 O O . HOH Q 7 . ? 14.520 -1.530 33.824 1.00 51.25 ? 1489 HOH A O 1 HETATM 5425 O O . HOH Q 7 . ? -0.557 50.924 52.681 1.00 40.79 ? 1490 HOH A O 1 HETATM 5426 O O . HOH Q 7 . ? 15.995 31.270 65.633 1.00 47.74 ? 1491 HOH A O 1 HETATM 5427 O O . HOH Q 7 . ? 22.511 31.478 10.877 1.00 33.20 ? 1492 HOH A O 1 HETATM 5428 O O . HOH Q 7 . ? 23.670 -4.366 20.248 1.00 57.89 ? 1493 HOH A O 1 HETATM 5429 O O . HOH Q 7 . ? 12.149 2.595 9.787 1.00 55.59 ? 1494 HOH A O 1 HETATM 5430 O O . HOH Q 7 . ? 17.941 0.002 24.247 1.00 41.62 ? 1495 HOH A O 1 HETATM 5431 O O . HOH Q 7 . ? -1.779 49.416 46.343 1.00 40.27 ? 1496 HOH A O 1 HETATM 5432 O O . HOH Q 7 . ? 9.723 5.678 19.971 1.00 37.70 ? 1497 HOH A O 1 HETATM 5433 O O . HOH Q 7 . ? 9.530 8.673 16.808 1.00 36.82 ? 1498 HOH A O 1 HETATM 5434 O O . HOH Q 7 . ? 15.401 10.849 64.584 1.00 40.83 ? 1499 HOH A O 1 HETATM 5435 O O . HOH Q 7 . ? 3.315 6.717 39.492 1.00 39.66 ? 1500 HOH A O 1 HETATM 5436 O O . HOH Q 7 . ? 17.339 -1.647 16.403 1.00 51.50 ? 1501 HOH A O 1 HETATM 5437 O O . HOH Q 7 . ? 29.048 28.730 37.549 1.00 33.46 ? 1502 HOH A O 1 HETATM 5438 O O . HOH Q 7 . ? 31.912 -1.484 16.956 1.00 51.26 ? 1503 HOH A O 1 HETATM 5439 O O . HOH Q 7 . ? -25.417 34.110 53.624 1.00 59.15 ? 1504 HOH A O 1 HETATM 5440 O O . HOH Q 7 . ? 27.078 -0.277 4.345 1.00 55.05 ? 1505 HOH A O 1 HETATM 5441 O O . HOH Q 7 . ? 41.933 9.717 11.238 1.00 44.90 ? 1506 HOH A O 1 HETATM 5442 O O . HOH Q 7 . ? 46.124 5.586 18.426 1.00 44.63 ? 1507 HOH A O 1 HETATM 5443 O O . HOH Q 7 . ? 10.090 41.120 28.226 1.00 46.86 ? 1508 HOH A O 1 HETATM 5444 O O . HOH Q 7 . ? 35.703 30.234 38.814 1.00 42.97 ? 1509 HOH A O 1 HETATM 5445 O O . HOH Q 7 . ? 26.023 34.098 50.713 1.00 54.91 ? 1510 HOH A O 1 HETATM 5446 O O . HOH Q 7 . ? 17.723 34.613 54.348 1.00 43.37 ? 1511 HOH A O 1 HETATM 5447 O O . HOH Q 7 . ? 19.188 33.510 50.304 1.00 50.80 ? 1512 HOH A O 1 HETATM 5448 O O . HOH Q 7 . ? 18.462 35.981 48.874 1.00 52.17 ? 1513 HOH A O 1 HETATM 5449 O O . HOH Q 7 . ? -12.550 51.841 55.013 1.00 44.25 ? 1514 HOH A O 1 HETATM 5450 O O . HOH Q 7 . ? 4.167 9.637 51.847 1.00 59.36 ? 1515 HOH A O 1 HETATM 5451 O O . HOH Q 7 . ? 11.413 44.242 44.104 1.00 35.44 ? 1516 HOH A O 1 HETATM 5452 O O . HOH Q 7 . ? -21.689 24.652 53.596 1.00 38.54 ? 1517 HOH A O 1 HETATM 5453 O O . HOH Q 7 . ? -12.639 27.206 36.434 1.00 42.65 ? 1518 HOH A O 1 HETATM 5454 O O . HOH Q 7 . ? -14.963 50.864 52.398 1.00 40.99 ? 1519 HOH A O 1 HETATM 5455 O O . HOH Q 7 . ? 15.976 43.811 41.699 1.00 54.53 ? 1520 HOH A O 1 HETATM 5456 O O . HOH Q 7 . ? 38.354 25.659 42.259 1.00 41.25 ? 1521 HOH A O 1 HETATM 5457 O O . HOH Q 7 . ? 0.036 18.103 21.533 1.00 54.35 ? 1522 HOH A O 1 HETATM 5458 O O . HOH Q 7 . ? 5.325 35.675 70.437 1.00 42.47 ? 1523 HOH A O 1 HETATM 5459 O O . HOH Q 7 . ? 18.561 40.877 36.323 1.00 47.93 ? 1524 HOH A O 1 HETATM 5460 O O . HOH Q 7 . ? 27.855 25.896 3.659 1.00 55.85 ? 1525 HOH A O 1 HETATM 5461 O O . HOH Q 7 . ? 32.705 0.280 42.186 1.00 63.04 ? 1526 HOH A O 1 HETATM 5462 O O . HOH Q 7 . ? 34.860 1.763 18.992 1.00 31.46 ? 1527 HOH A O 1 HETATM 5463 O O . HOH Q 7 . ? 38.299 29.165 34.802 1.00 46.13 ? 1528 HOH A O 1 HETATM 5464 O O . HOH Q 7 . ? -10.652 48.051 45.972 1.00 35.07 ? 1529 HOH A O 1 HETATM 5465 O O . HOH Q 7 . ? 36.960 15.463 53.321 1.00 49.03 ? 1530 HOH A O 1 HETATM 5466 O O . HOH Q 7 . ? 12.971 3.815 47.442 1.00 41.94 ? 1531 HOH A O 1 HETATM 5467 O O . HOH Q 7 . ? -1.605 17.126 54.678 1.00 37.26 ? 1532 HOH A O 1 HETATM 5468 O O . HOH Q 7 . ? 35.113 5.223 5.056 1.00 39.82 ? 1533 HOH A O 1 HETATM 5469 O O . HOH Q 7 . ? 4.589 51.141 53.206 1.00 52.28 ? 1534 HOH A O 1 HETATM 5470 O O . HOH Q 7 . ? 2.598 36.330 69.915 1.00 46.01 ? 1535 HOH A O 1 HETATM 5471 O O . HOH Q 7 . ? 18.016 -2.635 37.079 1.00 44.17 ? 1536 HOH A O 1 HETATM 5472 O O . HOH Q 7 . ? 4.790 12.227 22.168 1.00 42.12 ? 1537 HOH A O 1 HETATM 5473 O O . HOH Q 7 . ? 20.101 19.984 57.874 1.00 22.03 ? 1538 HOH A O 1 HETATM 5474 O O . HOH Q 7 . ? 10.491 45.758 58.881 1.00 43.97 ? 1539 HOH A O 1 HETATM 5475 O O . HOH Q 7 . ? 11.757 1.458 36.790 1.00 37.97 ? 1540 HOH A O 1 HETATM 5476 O O . HOH Q 7 . ? 17.452 40.636 53.932 1.00 55.50 ? 1541 HOH A O 1 HETATM 5477 O O . HOH Q 7 . ? 31.701 0.025 30.789 1.00 36.48 ? 1542 HOH A O 1 HETATM 5478 O O . HOH Q 7 . ? 22.906 -1.979 40.459 1.00 53.88 ? 1543 HOH A O 1 HETATM 5479 O O . HOH Q 7 . ? 17.468 -4.027 39.708 1.00 55.44 ? 1544 HOH A O 1 HETATM 5480 O O . HOH Q 7 . ? -4.454 48.719 44.073 1.00 45.06 ? 1545 HOH A O 1 HETATM 5481 O O . HOH Q 7 . ? -2.650 51.673 50.841 1.00 49.66 ? 1546 HOH A O 1 HETATM 5482 O O . HOH Q 7 . ? -1.196 45.806 41.981 1.00 43.11 ? 1547 HOH A O 1 HETATM 5483 O O . HOH Q 7 . ? 26.677 0.021 48.172 1.00 62.91 ? 1548 HOH A O 1 HETATM 5484 O O . HOH Q 7 . ? 5.236 12.783 59.836 1.00 42.87 ? 1549 HOH A O 1 HETATM 5485 O O . HOH Q 7 . ? 17.492 19.684 70.867 1.00 50.22 ? 1550 HOH A O 1 HETATM 5486 O O . HOH Q 7 . ? -5.510 15.226 38.085 1.00 41.96 ? 1551 HOH A O 1 HETATM 5487 O O . HOH Q 7 . ? 2.836 6.543 43.971 1.00 55.04 ? 1552 HOH A O 1 HETATM 5488 O O . HOH Q 7 . ? 4.760 44.949 38.687 1.00 61.55 ? 1553 HOH A O 1 HETATM 5489 O O . HOH Q 7 . ? 4.898 20.788 11.038 1.00 37.70 ? 1554 HOH A O 1 HETATM 5490 O O . HOH Q 7 . ? 20.595 -3.006 3.630 1.00 57.93 ? 1555 HOH A O 1 HETATM 5491 O O . HOH Q 7 . ? -17.236 28.684 47.679 1.00 40.91 ? 1556 HOH A O 1 HETATM 5492 O O . HOH Q 7 . ? 40.346 6.511 11.850 1.00 52.59 ? 1557 HOH A O 1 HETATM 5493 O O . HOH Q 7 . ? 32.408 -0.322 28.047 1.00 50.57 ? 1558 HOH A O 1 HETATM 5494 O O . HOH Q 7 . ? 28.828 35.454 11.902 1.00 49.15 ? 1559 HOH A O 1 HETATM 5495 O O . HOH Q 7 . ? 35.201 22.796 4.022 1.00 38.57 ? 1560 HOH A O 1 HETATM 5496 O O . HOH Q 7 . ? -5.028 14.328 53.003 1.00 42.52 ? 1561 HOH A O 1 HETATM 5497 O O . HOH Q 7 . ? -0.387 11.557 55.890 1.00 56.32 ? 1562 HOH A O 1 HETATM 5498 O O . HOH Q 7 . ? 42.028 28.416 32.133 1.00 51.48 ? 1563 HOH A O 1 HETATM 5499 O O . HOH Q 7 . ? 41.128 30.399 25.422 1.00 49.87 ? 1564 HOH A O 1 HETATM 5500 O O . HOH Q 7 . ? 31.920 -2.299 14.283 1.00 46.62 ? 1565 HOH A O 1 HETATM 5501 O O . HOH Q 7 . ? -0.444 20.950 64.560 1.00 44.73 ? 1566 HOH A O 1 HETATM 5502 O O . HOH Q 7 . ? 3.211 29.087 7.980 1.00 44.68 ? 1567 HOH A O 1 HETATM 5503 O O . HOH Q 7 . ? 5.736 22.772 66.178 1.00 35.62 ? 1568 HOH A O 1 HETATM 5504 O O . HOH Q 7 . ? -4.091 16.946 61.600 1.00 45.72 ? 1569 HOH A O 1 HETATM 5505 O O . HOH Q 7 . ? 1.891 52.721 55.341 1.00 57.86 ? 1570 HOH A O 1 HETATM 5506 O O . HOH Q 7 . ? 17.939 -1.164 21.479 1.00 48.66 ? 1571 HOH A O 1 HETATM 5507 O O . HOH Q 7 . ? 1.622 9.840 50.330 1.00 45.70 ? 1572 HOH A O 1 HETATM 5508 O O . HOH Q 7 . ? 16.220 41.970 46.048 1.00 53.19 ? 1573 HOH A O 1 HETATM 5509 O O . HOH Q 7 . ? -5.058 26.674 74.041 1.00 58.39 ? 1574 HOH A O 1 HETATM 5510 O O . HOH Q 7 . ? 25.666 36.179 36.466 1.00 55.85 ? 1575 HOH A O 1 HETATM 5511 O O . HOH Q 7 . ? 42.581 16.164 40.648 1.00 46.06 ? 1576 HOH A O 1 HETATM 5512 O O . HOH Q 7 . ? -7.092 20.643 35.685 1.00 44.33 ? 1577 HOH A O 1 HETATM 5513 O O . HOH Q 7 . ? 13.045 -1.849 37.714 1.00 60.04 ? 1578 HOH A O 1 HETATM 5514 O O . HOH Q 7 . ? 16.372 4.218 4.445 1.00 56.15 ? 1579 HOH A O 1 HETATM 5515 O O . HOH Q 7 . ? 21.294 38.786 43.173 1.00 56.86 ? 1580 HOH A O 1 HETATM 5516 O O . HOH Q 7 . ? 30.490 36.651 23.011 1.00 50.69 ? 1581 HOH A O 1 HETATM 5517 O O . HOH Q 7 . ? 44.934 9.327 9.859 1.00 36.24 ? 1582 HOH A O 1 HETATM 5518 O O . HOH Q 7 . ? 7.302 -2.072 24.107 1.00 53.41 ? 1583 HOH A O 1 HETATM 5519 O O . HOH Q 7 . ? 0.651 14.504 29.587 1.00 42.35 ? 1584 HOH A O 1 HETATM 5520 O O . HOH Q 7 . ? 2.382 14.758 26.327 1.00 39.54 ? 1585 HOH A O 1 HETATM 5521 O O . HOH Q 7 . ? 6.117 44.584 64.351 1.00 47.08 ? 1586 HOH A O 1 HETATM 5522 O O . HOH Q 7 . ? 8.497 7.596 48.731 1.00 49.00 ? 1587 HOH A O 1 HETATM 5523 O O . HOH Q 7 . ? -3.887 39.326 66.831 1.00 40.17 ? 1588 HOH A O 1 HETATM 5524 O O . HOH Q 7 . ? -4.851 37.070 68.353 1.00 35.22 ? 1589 HOH A O 1 HETATM 5525 O O . HOH Q 7 . ? 29.093 33.003 27.225 1.00 36.26 ? 1590 HOH A O 1 HETATM 5526 O O . HOH Q 7 . ? -7.058 31.598 31.547 1.00 36.13 ? 1591 HOH A O 1 HETATM 5527 O O . HOH Q 7 . ? 2.232 9.531 28.128 1.00 45.82 ? 1592 HOH A O 1 HETATM 5528 O O . HOH Q 7 . ? -11.326 51.024 50.410 1.00 54.73 ? 1593 HOH A O 1 HETATM 5529 O O . HOH Q 7 . ? 10.204 41.084 51.092 1.00 40.57 ? 1594 HOH A O 1 HETATM 5530 O O . HOH Q 7 . ? 22.973 12.829 57.619 1.00 46.79 ? 1595 HOH A O 1 HETATM 5531 O O . HOH Q 7 . ? 26.709 14.177 1.960 1.00 42.58 ? 1596 HOH A O 1 HETATM 5532 O O . HOH Q 7 . ? 26.609 -3.694 17.396 1.00 58.66 ? 1597 HOH A O 1 HETATM 5533 O O . HOH Q 7 . ? -22.112 40.833 54.710 1.00 32.14 ? 1598 HOH A O 1 HETATM 5534 O O . HOH Q 7 . ? 6.261 1.510 26.701 1.00 50.27 ? 1599 HOH A O 1 HETATM 5535 O O . HOH Q 7 . ? 10.249 11.687 11.546 1.00 51.92 ? 1600 HOH A O 1 HETATM 5536 O O . HOH Q 7 . ? 20.947 24.217 68.748 1.00 53.76 ? 1601 HOH A O 1 HETATM 5537 O O . HOH Q 7 . ? -5.144 22.776 63.736 1.00 39.10 ? 1602 HOH A O 1 HETATM 5538 O O . HOH Q 7 . ? -4.854 13.252 34.608 1.00 44.20 ? 1603 HOH A O 1 HETATM 5539 O O . HOH Q 7 . ? 26.377 -3.720 20.191 1.00 61.28 ? 1604 HOH A O 1 HETATM 5540 O O . HOH Q 7 . ? 30.031 -0.069 23.073 1.00 59.84 ? 1605 HOH A O 1 HETATM 5541 O O . HOH Q 7 . ? 34.571 -1.281 22.308 1.00 57.95 ? 1606 HOH A O 1 HETATM 5542 O O . HOH Q 7 . ? 52.301 8.162 21.744 1.00 56.96 ? 1607 HOH A O 1 HETATM 5543 O O . HOH Q 7 . ? -15.223 30.297 56.395 1.00 42.05 ? 1608 HOH A O 1 HETATM 5544 O O . HOH Q 7 . ? 23.468 17.372 5.769 1.00 44.90 ? 1609 HOH A O 1 HETATM 5545 O O . HOH Q 7 . ? -6.460 33.715 30.885 1.00 36.41 ? 1610 HOH A O 1 HETATM 5546 O O . HOH Q 7 . ? -4.317 19.815 32.157 1.00 40.08 ? 1611 HOH A O 1 HETATM 5547 O O . HOH Q 7 . ? 21.997 -3.117 32.783 1.00 36.68 ? 1612 HOH A O 1 HETATM 5548 O O . HOH Q 7 . ? 35.572 -0.971 36.482 1.00 51.03 ? 1613 HOH A O 1 HETATM 5549 O O . HOH Q 7 . ? 4.910 33.039 70.941 1.00 37.95 ? 1614 HOH A O 1 HETATM 5550 O O . HOH Q 7 . ? 9.308 32.211 72.658 1.00 64.23 ? 1615 HOH A O 1 HETATM 5551 O O . HOH Q 7 . ? 10.371 4.040 33.177 1.00 42.83 ? 1616 HOH A O 1 HETATM 5552 O O . HOH Q 7 . ? 14.090 44.727 43.853 1.00 56.89 ? 1617 HOH A O 1 HETATM 5553 O O . HOH Q 7 . ? -18.698 32.587 56.911 1.00 34.13 ? 1618 HOH A O 1 HETATM 5554 O O . HOH Q 7 . ? -1.843 26.840 67.454 1.00 53.89 ? 1619 HOH A O 1 HETATM 5555 O O . HOH Q 7 . ? -4.229 24.217 68.148 1.00 48.94 ? 1620 HOH A O 1 HETATM 5556 O O . HOH Q 7 . ? 34.557 5.510 52.822 1.00 50.57 ? 1621 HOH A O 1 HETATM 5557 O O . HOH Q 7 . ? 41.796 12.907 48.898 1.00 55.01 ? 1622 HOH A O 1 HETATM 5558 O O . HOH Q 7 . ? -0.676 42.878 67.325 1.00 48.98 ? 1623 HOH A O 1 HETATM 5559 O O . HOH Q 7 . ? -4.933 16.369 46.436 1.00 50.82 ? 1624 HOH A O 1 HETATM 5560 O O . HOH Q 7 . ? 32.180 -3.613 38.008 1.00 57.55 ? 1625 HOH A O 1 HETATM 5561 O O . HOH Q 7 . ? 45.261 22.561 41.805 1.00 41.38 ? 1626 HOH A O 1 HETATM 5562 O O . HOH Q 7 . ? 26.915 -4.016 29.110 1.00 50.41 ? 1627 HOH A O 1 HETATM 5563 O O . HOH Q 7 . ? 17.492 -1.878 7.163 1.00 56.94 ? 1628 HOH A O 1 HETATM 5564 O O . HOH Q 7 . ? 21.819 -0.161 0.198 1.00 49.32 ? 1629 HOH A O 1 HETATM 5565 O O . HOH Q 7 . ? 19.585 1.189 0.987 1.00 53.04 ? 1630 HOH A O 1 HETATM 5566 O O . HOH Q 7 . ? 21.375 3.403 -3.739 1.00 51.69 ? 1631 HOH A O 1 HETATM 5567 O O . HOH Q 7 . ? 23.788 10.153 -2.146 1.00 44.54 ? 1632 HOH A O 1 HETATM 5568 O O . HOH Q 7 . ? 23.676 3.877 -5.351 1.00 50.73 ? 1633 HOH A O 1 HETATM 5569 O O . HOH Q 7 . ? -9.516 51.707 54.579 1.00 39.90 ? 1634 HOH A O 1 HETATM 5570 O O . HOH Q 7 . ? 17.218 38.756 18.991 1.00 38.69 ? 1635 HOH A O 1 HETATM 5571 O O . HOH Q 7 . ? 24.454 35.425 52.949 1.00 49.93 ? 1636 HOH A O 1 HETATM 5572 O O . HOH Q 7 . ? -13.613 46.045 62.067 1.00 35.13 ? 1637 HOH A O 1 HETATM 5573 O O . HOH Q 7 . ? 13.147 42.703 29.721 1.00 46.79 ? 1638 HOH A O 1 HETATM 5574 O O . HOH Q 7 . ? -24.543 39.622 55.123 1.00 43.65 ? 1639 HOH A O 1 HETATM 5575 O O . HOH Q 7 . ? 23.099 35.716 35.425 1.00 48.52 ? 1640 HOH A O 1 HETATM 5576 O O . HOH Q 7 . ? 11.201 30.958 69.280 1.00 55.24 ? 1641 HOH A O 1 HETATM 5577 O O . HOH Q 7 . ? -20.557 33.095 52.718 1.00 46.67 ? 1642 HOH A O 1 HETATM 5578 O O . HOH Q 7 . ? 44.690 11.760 14.116 1.00 43.89 ? 1643 HOH A O 1 HETATM 5579 O O . HOH Q 7 . ? 29.158 19.326 3.091 1.00 47.24 ? 1644 HOH A O 1 HETATM 5580 O O . HOH Q 7 . ? -2.428 29.838 71.983 1.00 57.68 ? 1645 HOH A O 1 HETATM 5581 O O . HOH Q 7 . ? 6.301 38.318 23.325 1.00 47.59 ? 1646 HOH A O 1 HETATM 5582 O O . HOH Q 7 . ? -2.531 32.274 70.351 1.00 57.62 ? 1647 HOH A O 1 HETATM 5583 O O . HOH Q 7 . ? 16.408 16.746 71.938 1.00 59.24 ? 1648 HOH A O 1 HETATM 5584 O O . HOH Q 7 . ? 9.325 1.980 37.442 1.00 49.76 ? 1649 HOH A O 1 HETATM 5585 O O . HOH Q 7 . ? 0.204 33.479 69.110 1.00 40.57 ? 1650 HOH A O 1 HETATM 5586 O O . HOH Q 7 . ? 34.545 3.947 47.896 1.00 57.98 ? 1651 HOH A O 1 HETATM 5587 O O . HOH Q 7 . ? -1.962 20.270 21.154 1.00 52.94 ? 1652 HOH A O 1 HETATM 5588 O O . HOH Q 7 . ? 15.272 35.205 62.740 1.00 55.90 ? 1653 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 . ASP A 1 ? 0.5390 0.6275 0.5712 -0.0071 0.0080 -0.0267 1 ASP A N 2 C CA . ASP A 1 ? 0.5343 0.6222 0.5703 -0.0081 0.0100 -0.0304 1 ASP A CA 3 C C . ASP A 1 ? 0.4771 0.5577 0.5140 -0.0086 0.0115 -0.0297 1 ASP A C 4 O O . ASP A 1 ? 0.4653 0.5420 0.4999 -0.0082 0.0108 -0.0264 1 ASP A O 5 C CB . ASP A 1 ? 0.5830 0.6721 0.6195 -0.0081 0.0104 -0.0312 1 ASP A CB 6 C CG . ASP A 1 ? 0.6705 0.7627 0.7108 -0.0089 0.0119 -0.0359 1 ASP A CG 7 O OD1 . ASP A 1 ? 0.7613 0.8586 0.8031 -0.0093 0.0117 -0.0388 1 ASP A OD1 8 O OD2 . ASP A 1 ? 0.6413 0.7311 0.6830 -0.0092 0.0134 -0.0369 1 ASP A OD2 9 N N . TYR A 2 ? 0.4318 0.5107 0.4720 -0.0095 0.0137 -0.0328 2 TYR A N 10 C CA . TYR A 2 ? 0.3480 0.4205 0.3892 -0.0100 0.0155 -0.0324 2 TYR A CA 11 C C . TYR A 2 ? 0.3195 0.3859 0.3585 -0.0091 0.0157 -0.0286 2 TYR A C 12 O O . TYR A 2 ? 0.3256 0.3916 0.3641 -0.0085 0.0159 -0.0280 2 TYR A O 13 C CB . TYR A 2 ? 0.3678 0.4393 0.4129 -0.0112 0.0183 -0.0365 2 TYR A CB 14 C CG . TYR A 2 ? 0.3283 0.3928 0.3745 -0.0116 0.0206 -0.0362 2 TYR A CG 15 C CD1 . TYR A 2 ? 0.3241 0.3884 0.3714 -0.0125 0.0209 -0.0372 2 TYR A CD1 16 C CD2 . TYR A 2 ? 0.3091 0.3677 0.3554 -0.0111 0.0226 -0.0351 2 TYR A CD2 17 C CE1 . TYR A 2 ? 0.3074 0.3654 0.3557 -0.0130 0.0232 -0.0369 2 TYR A CE1 18 C CE2 . TYR A 2 ? 0.3061 0.3582 0.3532 -0.0113 0.0250 -0.0347 2 TYR A CE2 19 C CZ . TYR A 2 ? 0.3024 0.3542 0.3506 -0.0123 0.0253 -0.0356 2 TYR A CZ 20 O OH . TYR A 2 ? 0.3112 0.3567 0.3601 -0.0125 0.0278 -0.0351 2 TYR A OH 21 N N . VAL A 3 ? 0.2856 0.3478 0.3234 -0.0089 0.0156 -0.0262 3 VAL A N 22 C CA . VAL A 3 ? 0.2654 0.3222 0.3013 -0.0080 0.0159 -0.0229 3 VAL A CA 23 C C . VAL A 3 ? 0.2296 0.2811 0.2669 -0.0082 0.0179 -0.0232 3 VAL A C 24 O O . VAL A 3 ? 0.2603 0.3118 0.2976 -0.0087 0.0174 -0.0232 3 VAL A O 25 C CB . VAL A 3 ? 0.2955 0.3528 0.3280 -0.0074 0.0135 -0.0195 3 VAL A CB 26 C CG1 . VAL A 3 ? 0.3138 0.3662 0.3445 -0.0066 0.0137 -0.0163 3 VAL A CG1 27 C CG2 . VAL A 3 ? 0.3115 0.3735 0.3426 -0.0072 0.0119 -0.0191 3 VAL A CG2 28 N N . LEU A 4 ? 0.2268 0.2740 0.2650 -0.0077 0.0202 -0.0233 4 LEU A N 29 C CA . LEU A 4 ? 0.2191 0.2611 0.2590 -0.0080 0.0228 -0.0239 4 LEU A CA 30 C C . LEU A 4 ? 0.2227 0.2621 0.2607 -0.0076 0.0218 -0.0211 4 LEU A C 31 O O . LEU A 4 ? 0.2247 0.2629 0.2640 -0.0085 0.0225 -0.0221 4 LEU A O 32 C CB . LEU A 4 ? 0.2425 0.2795 0.2827 -0.0069 0.0254 -0.0234 4 LEU A CB 33 C CG . LEU A 4 ? 0.2780 0.3095 0.3203 -0.0074 0.0288 -0.0246 4 LEU A CG 34 C CD1 . LEU A 4 ? 0.3015 0.3292 0.3447 -0.0065 0.0318 -0.0255 4 LEU A CD1 35 C CD2 . LEU A 4 ? 0.2606 0.2877 0.3010 -0.0064 0.0288 -0.0215 4 LEU A CD2 36 N N . TYR A 5 ? 0.1947 0.2336 0.2297 -0.0065 0.0200 -0.0177 5 TYR A N 37 C CA . TYR A 5 ? 0.1885 0.2248 0.2219 -0.0061 0.0193 -0.0152 5 TYR A CA 38 C C . TYR A 5 ? 0.1901 0.2289 0.2235 -0.0071 0.0177 -0.0158 5 TYR A C 39 O O . TYR A 5 ? 0.1859 0.2222 0.2188 -0.0070 0.0177 -0.0147 5 TYR A O 40 C CB . TYR A 5 ? 0.1805 0.2158 0.2108 -0.0048 0.0179 -0.0117 5 TYR A CB 41 C CG . TYR A 5 ? 0.1688 0.2083 0.1971 -0.0051 0.0151 -0.0106 5 TYR A CG 42 C CD1 . TYR A 5 ? 0.1733 0.2131 0.2000 -0.0055 0.0135 -0.0093 5 TYR A CD1 43 C CD2 . TYR A 5 ? 0.1850 0.2275 0.2126 -0.0049 0.0144 -0.0107 5 TYR A CD2 44 C CE1 . TYR A 5 ? 0.1731 0.2158 0.1976 -0.0057 0.0114 -0.0080 5 TYR A CE1 45 C CE2 . TYR A 5 ? 0.1870 0.2328 0.2127 -0.0053 0.0123 -0.0096 5 TYR A CE2 46 C CZ . TYR A 5 ? 0.1913 0.2369 0.2153 -0.0057 0.0109 -0.0081 5 TYR A CZ 47 O OH . TYR A 5 ? 0.1941 0.2424 0.2160 -0.0060 0.0092 -0.0070 5 TYR A OH 48 N N . LYS A 6 ? 0.1918 0.2358 0.2257 -0.0078 0.0165 -0.0177 6 LYS A N 49 C CA . LYS A 6 ? 0.2028 0.2501 0.2365 -0.0082 0.0150 -0.0184 6 LYS A CA 50 C C . LYS A 6 ? 0.2244 0.2728 0.2613 -0.0094 0.0166 -0.0219 6 LYS A C 51 O O . LYS A 6 ? 0.2496 0.3011 0.2866 -0.0096 0.0156 -0.0228 6 LYS A O 52 C CB . LYS A 6 ? 0.2281 0.2808 0.2604 -0.0081 0.0129 -0.0184 6 LYS A CB 53 C CG . LYS A 6 ? 0.2356 0.2871 0.2645 -0.0072 0.0114 -0.0148 6 LYS A CG 54 C CD . LYS A 6 ? 0.2518 0.3081 0.2790 -0.0071 0.0096 -0.0145 6 LYS A CD 55 C CE . LYS A 6 ? 0.2511 0.3060 0.2752 -0.0067 0.0085 -0.0113 6 LYS A CE 56 N NZ A LYS A 6 ? 0.3240 0.3832 0.3464 -0.0065 0.0071 -0.0109 6 LYS A NZ 57 N NZ B LYS A 6 ? 0.2087 0.2616 0.2303 -0.0064 0.0074 -0.0089 6 LYS A NZ 58 N N . ASP A 7 ? 0.2163 0.2623 0.2557 -0.0100 0.0192 -0.0239 7 ASP A N 59 C CA . ASP A 7 ? 0.2293 0.2765 0.2722 -0.0116 0.0211 -0.0280 7 ASP A CA 60 C C . ASP A 7 ? 0.2343 0.2766 0.2778 -0.0119 0.0228 -0.0274 7 ASP A C 61 O O . ASP A 7 ? 0.2406 0.2770 0.2842 -0.0115 0.0250 -0.0261 7 ASP A O 62 C CB . ASP A 7 ? 0.2348 0.2818 0.2800 -0.0122 0.0233 -0.0306 7 ASP A CB 63 C CG . ASP A 7 ? 0.2449 0.2927 0.2941 -0.0141 0.0260 -0.0353 7 ASP A CG 64 O OD1 . ASP A 7 ? 0.2495 0.2970 0.3008 -0.0148 0.0280 -0.0377 7 ASP A OD1 65 O OD2 . ASP A 7 ? 0.2629 0.3117 0.3132 -0.0150 0.0261 -0.0365 7 ASP A OD2 66 N N . ALA A 8 ? 0.2203 0.2653 0.2642 -0.0124 0.0219 -0.0283 8 ALA A N 67 C CA . ALA A 8 ? 0.2308 0.2721 0.2752 -0.0127 0.0231 -0.0277 8 ALA A CA 68 C C . ALA A 8 ? 0.2595 0.2976 0.3073 -0.0143 0.0268 -0.0306 8 ALA A C 69 O O . ALA A 8 ? 0.2851 0.3185 0.3331 -0.0144 0.0285 -0.0296 8 ALA A O 70 C CB . ALA A 8 ? 0.2223 0.2681 0.2663 -0.0128 0.0212 -0.0283 8 ALA A CB 71 N N . THR A 9 ? 0.2701 0.3106 0.3205 -0.0155 0.0283 -0.0342 9 THR A N 72 C CA . THR A 9 ? 0.2822 0.3191 0.3358 -0.0172 0.0323 -0.0371 9 THR A CA 73 C C . THR A 9 ? 0.2857 0.3151 0.3386 -0.0162 0.0348 -0.0349 9 THR A C 74 O O . THR A 9 ? 0.3162 0.3411 0.3712 -0.0173 0.0385 -0.0366 9 THR A O 75 C CB . THR A 9 ? 0.2909 0.3330 0.3480 -0.0191 0.0334 -0.0424 9 THR A CB 76 O OG1 . THR A 9 ? 0.3031 0.3454 0.3598 -0.0184 0.0333 -0.0423 9 THR A OG1 77 C CG2 . THR A 9 ? 0.2978 0.3485 0.3555 -0.0196 0.0307 -0.0446 9 THR A CG2 78 N N . LYS A 10 ? 0.2500 0.2781 0.2998 -0.0141 0.0330 -0.0313 10 LYS A N 79 C CA . LYS A 10 ? 0.2527 0.2747 0.3016 -0.0127 0.0352 -0.0292 10 LYS A CA 80 C C . LYS A 10 ? 0.2506 0.2666 0.2974 -0.0112 0.0361 -0.0255 10 LYS A C 81 O O . LYS A 10 ? 0.2547 0.2720 0.2999 -0.0108 0.0339 -0.0235 10 LYS A O 82 C CB . LYS A 10 ? 0.2755 0.2997 0.3221 -0.0111 0.0330 -0.0273 10 LYS A CB 83 C CG . LYS A 10 ? 0.2952 0.3245 0.3437 -0.0121 0.0326 -0.0308 10 LYS A CG 84 C CD . LYS A 10 ? 0.3407 0.3665 0.3919 -0.0130 0.0366 -0.0337 10 LYS A CD 85 C CE . LYS A 10 ? 0.3681 0.3995 0.4214 -0.0143 0.0362 -0.0377 10 LYS A CE 86 N NZ . LYS A 10 ? 0.4470 0.4745 0.5033 -0.0154 0.0405 -0.0408 10 LYS A NZ 87 N N . PRO A 11 ? 0.2674 0.2771 0.3143 -0.0103 0.0395 -0.0245 11 PRO A N 88 C CA . PRO A 11 ? 0.2608 0.2649 0.3056 -0.0085 0.0406 -0.0209 11 PRO A CA 89 C C . PRO A 11 ? 0.2418 0.2476 0.2830 -0.0063 0.0372 -0.0169 11 PRO A C 90 O O . PRO A 11 ? 0.2384 0.2470 0.2784 -0.0055 0.0353 -0.0164 11 PRO A O 91 C CB . PRO A 11 ? 0.2750 0.2730 0.3200 -0.0073 0.0446 -0.0205 11 PRO A CB 92 C CG . PRO A 11 ? 0.2859 0.2852 0.3344 -0.0097 0.0466 -0.0252 11 PRO A CG 93 C CD . PRO A 11 ? 0.2773 0.2844 0.3259 -0.0105 0.0427 -0.0266 11 PRO A CD 94 N N . VAL A 12 ? 0.2303 0.2342 0.2698 -0.0054 0.0365 -0.0143 12 VAL A N 95 C CA . VAL A 12 ? 0.2124 0.2178 0.2486 -0.0036 0.0335 -0.0108 12 VAL A CA 96 C C . VAL A 12 ? 0.2287 0.2330 0.2631 -0.0013 0.0338 -0.0087 12 VAL A C 97 O O . VAL A 12 ? 0.2079 0.2159 0.2406 -0.0007 0.0310 -0.0077 12 VAL A O 98 C CB . VAL A 12 ? 0.2164 0.2189 0.2513 -0.0027 0.0336 -0.0083 12 VAL A CB 99 C CG1 . VAL A 12 ? 0.2284 0.2317 0.2600 -0.0006 0.0314 -0.0048 12 VAL A CG1 100 C CG2 . VAL A 12 ? 0.2365 0.2417 0.2727 -0.0047 0.0323 -0.0100 12 VAL A CG2 101 N N . GLU A 13 ? 0.2355 0.2348 0.2701 0.0001 0.0372 -0.0081 13 GLU A N 102 C CA . GLU A 13 ? 0.2375 0.2362 0.2700 0.0028 0.0375 -0.0060 13 GLU A CA 103 C C . GLU A 13 ? 0.2365 0.2390 0.2696 0.0022 0.0363 -0.0078 13 GLU A C 104 O O . GLU A 13 ? 0.2321 0.2371 0.2632 0.0039 0.0345 -0.0061 13 GLU A O 105 C CB . GLU A 13 ? 0.2387 0.2309 0.2709 0.0049 0.0417 -0.0049 13 GLU A CB 106 C CG . GLU A 13 ? 0.2572 0.2456 0.2882 0.0061 0.0430 -0.0024 13 GLU A CG 107 C CD . GLU A 13 ? 0.2671 0.2584 0.2951 0.0079 0.0399 0.0007 13 GLU A CD 108 O OE1 . GLU A 13 ? 0.2974 0.2891 0.3253 0.0071 0.0387 0.0013 13 GLU A OE1 109 O OE2 . GLU A 13 ? 0.2864 0.2798 0.3125 0.0101 0.0387 0.0024 13 GLU A OE2 110 N N . ASP A 14 ? 0.2424 0.2457 0.2783 0.0000 0.0373 -0.0114 14 ASP A N 111 C CA . ASP A 14 ? 0.2518 0.2594 0.2885 -0.0007 0.0360 -0.0133 14 ASP A CA 112 C C . ASP A 14 ? 0.2251 0.2389 0.2605 -0.0013 0.0317 -0.0128 14 ASP A C 113 O O . ASP A 14 ? 0.2336 0.2507 0.2679 -0.0007 0.0301 -0.0123 14 ASP A O 114 C CB . ASP A 14 ? 0.2926 0.3004 0.3328 -0.0031 0.0380 -0.0176 14 ASP A CB 115 C CG . ASP A 14 ? 0.3771 0.3784 0.4186 -0.0025 0.0427 -0.0184 14 ASP A CG 116 O OD1 . ASP A 14 ? 0.4247 0.4222 0.4641 0.0002 0.0442 -0.0158 14 ASP A OD1 117 O OD2 . ASP A 14 ? 0.4478 0.4480 0.4922 -0.0048 0.0449 -0.0218 14 ASP A OD2 118 N N . ARG A 15 ? 0.2161 0.2313 0.2515 -0.0026 0.0301 -0.0127 15 ARG A N 119 C CA . ARG A 15 ? 0.1970 0.2173 0.2309 -0.0032 0.0264 -0.0121 15 ARG A CA 120 C C . ARG A 15 ? 0.1990 0.2192 0.2298 -0.0013 0.0248 -0.0086 15 ARG A C 121 O O . ARG A 15 ? 0.2094 0.2335 0.2389 -0.0013 0.0225 -0.0080 15 ARG A O 122 C CB . ARG A 15 ? 0.2051 0.2263 0.2396 -0.0046 0.0254 -0.0127 15 ARG A CB 123 C CG . ARG A 15 ? 0.1972 0.2200 0.2349 -0.0066 0.0266 -0.0165 15 ARG A CG 124 C CD . ARG A 15 ? 0.2061 0.2304 0.2442 -0.0078 0.0255 -0.0172 15 ARG A CD 125 N NE . ARG A 15 ? 0.1859 0.2152 0.2224 -0.0079 0.0222 -0.0166 15 ARG A NE 126 C CZ . ARG A 15 ? 0.1904 0.2217 0.2265 -0.0084 0.0207 -0.0166 15 ARG A CZ 127 N NH1 . ARG A 15 ? 0.1922 0.2213 0.2296 -0.0089 0.0220 -0.0173 15 ARG A NH1 128 N NH2 . ARG A 15 ? 0.1962 0.2315 0.2306 -0.0082 0.0180 -0.0160 15 ARG A NH2 129 N N . VAL A 16 ? 0.1926 0.2089 0.2224 0.0002 0.0261 -0.0064 16 VAL A N 130 C CA . VAL A 16 ? 0.1956 0.2123 0.2225 0.0021 0.0248 -0.0033 16 VAL A CA 131 C C . VAL A 16 ? 0.1960 0.2145 0.2223 0.0034 0.0249 -0.0031 16 VAL A C 132 O O . VAL A 16 ? 0.2062 0.2284 0.2310 0.0035 0.0227 -0.0022 16 VAL A O 133 C CB . VAL A 16 ? 0.1978 0.2101 0.2239 0.0039 0.0266 -0.0012 16 VAL A CB 134 C CG1 . VAL A 16 ? 0.2003 0.2140 0.2237 0.0061 0.0255 0.0015 16 VAL A CG1 135 C CG2 . VAL A 16 ? 0.2054 0.2164 0.2318 0.0027 0.0262 -0.0011 16 VAL A CG2 136 N N . ALA A 17 ? 0.2083 0.2240 0.2358 0.0043 0.0277 -0.0042 17 ALA A N 137 C CA . ALA A 17 ? 0.2167 0.2339 0.2435 0.0059 0.0280 -0.0040 17 ALA A CA 138 C C . ALA A 17 ? 0.2142 0.2366 0.2416 0.0043 0.0258 -0.0058 17 ALA A C 139 O O . ALA A 17 ? 0.2207 0.2465 0.2467 0.0052 0.0244 -0.0049 17 ALA A O 140 C CB . ALA A 17 ? 0.2192 0.2318 0.2473 0.0071 0.0317 -0.0049 17 ALA A CB 141 N N . ASP A 18 ? 0.2088 0.2323 0.2383 0.0019 0.0256 -0.0083 18 ASP A N 142 C CA . ASP A 18 ? 0.1979 0.2265 0.2278 0.0005 0.0237 -0.0100 18 ASP A CA 143 C C . ASP A 18 ? 0.2034 0.2359 0.2312 0.0002 0.0205 -0.0082 18 ASP A C 144 O O . ASP A 18 ? 0.2320 0.2683 0.2589 0.0002 0.0191 -0.0081 18 ASP A O 145 C CB . ASP A 18 ? 0.2215 0.2512 0.2540 -0.0017 0.0240 -0.0130 18 ASP A CB 146 C CG . ASP A 18 ? 0.2279 0.2631 0.2609 -0.0027 0.0223 -0.0148 18 ASP A CG 147 O OD1 . ASP A 18 ? 0.2471 0.2831 0.2810 -0.0023 0.0234 -0.0163 18 ASP A OD1 148 O OD2 . ASP A 18 ? 0.2316 0.2702 0.2639 -0.0038 0.0200 -0.0147 18 ASP A OD2 149 N N . LEU A 19 ? 0.1897 0.2211 0.2165 -0.0003 0.0195 -0.0069 19 LEU A N 150 C CA . LEU A 19 ? 0.1706 0.2048 0.1953 -0.0008 0.0169 -0.0052 19 LEU A CA 151 C C . LEU A 19 ? 0.1780 0.2128 0.2006 0.0008 0.0165 -0.0031 19 LEU A C 152 O O . LEU A 19 ? 0.1751 0.2136 0.1966 0.0004 0.0149 -0.0027 19 LEU A O 153 C CB . LEU A 19 ? 0.1761 0.2084 0.2004 -0.0015 0.0162 -0.0045 19 LEU A CB 154 C CG . LEU A 19 ? 0.1678 0.2021 0.1898 -0.0021 0.0139 -0.0027 19 LEU A CG 155 C CD1 . LEU A 19 ? 0.1829 0.2214 0.2042 -0.0032 0.0122 -0.0032 19 LEU A CD1 156 C CD2 . LEU A 19 ? 0.1889 0.2214 0.2108 -0.0028 0.0134 -0.0024 19 LEU A CD2 157 N N . LEU A 20 ? 0.1871 0.2188 0.2093 0.0026 0.0181 -0.0018 20 LEU A N 158 C CA . LEU A 20 ? 0.1947 0.2277 0.2150 0.0044 0.0177 0.0001 20 LEU A CA 159 C C . LEU A 20 ? 0.2024 0.2390 0.2226 0.0050 0.0175 -0.0006 20 LEU A C 160 O O . LEU A 20 ? 0.2005 0.2408 0.2192 0.0051 0.0160 0.0003 20 LEU A O 161 C CB . LEU A 20 ? 0.2045 0.2336 0.2245 0.0069 0.0199 0.0014 20 LEU A CB 162 C CG . LEU A 20 ? 0.2033 0.2344 0.2213 0.0092 0.0197 0.0034 20 LEU A CG 163 C CD1 . LEU A 20 ? 0.2296 0.2627 0.2459 0.0085 0.0176 0.0046 20 LEU A CD1 164 C CD2 . LEU A 20 ? 0.1997 0.2266 0.2174 0.0121 0.0224 0.0045 20 LEU A CD2 165 N N . GLY A 21 ? 0.2140 0.2497 0.2359 0.0051 0.0190 -0.0023 21 GLY A N 166 C CA . GLY A 21 ? 0.2260 0.2648 0.2480 0.0058 0.0191 -0.0031 21 GLY A CA 167 C C . GLY A 21 ? 0.2309 0.2747 0.2525 0.0039 0.0167 -0.0038 21 GLY A C 168 O O . GLY A 21 ? 0.2557 0.3030 0.2769 0.0045 0.0163 -0.0041 21 GLY A O 169 N N . ARG A 22 ? 0.2088 0.2531 0.2304 0.0018 0.0153 -0.0040 22 ARG A N 170 C CA . ARG A 22 ? 0.1970 0.2454 0.2180 0.0001 0.0133 -0.0044 22 ARG A CA 171 C C . ARG A 22 ? 0.1941 0.2443 0.2129 -0.0005 0.0116 -0.0025 22 ARG A C 172 O O . ARG A 22 ? 0.1989 0.2525 0.2168 -0.0019 0.0103 -0.0025 22 ARG A O 173 C CB . ARG A 22 ? 0.1936 0.2418 0.2157 -0.0016 0.0129 -0.0057 22 ARG A CB 174 C CG . ARG A 22 ? 0.2178 0.2650 0.2424 -0.0016 0.0145 -0.0081 22 ARG A CG 175 C CD . ARG A 22 ? 0.2136 0.2610 0.2393 -0.0031 0.0140 -0.0094 22 ARG A CD 176 N NE . ARG A 22 ? 0.2262 0.2727 0.2546 -0.0034 0.0158 -0.0122 22 ARG A NE 177 C CZ . ARG A 22 ? 0.2668 0.3167 0.2967 -0.0040 0.0158 -0.0146 22 ARG A CZ 178 N NH1 . ARG A 22 ? 0.3180 0.3724 0.3467 -0.0043 0.0141 -0.0144 22 ARG A NH1 179 N NH2 . ARG A 22 ? 0.2810 0.3299 0.3136 -0.0045 0.0177 -0.0174 22 ARG A NH2 180 N N . MET A 23 ? 0.2014 0.2492 0.2193 0.0004 0.0119 -0.0010 23 MET A N 181 C CA . MET A 23 ? 0.1860 0.2349 0.2021 -0.0006 0.0105 0.0004 23 MET A CA 182 C C . MET A 23 ? 0.1910 0.2439 0.2058 -0.0002 0.0099 0.0009 23 MET A C 183 O O . MET A 23 ? 0.2091 0.2628 0.2239 0.0018 0.0108 0.0011 23 MET A O 184 C CB . MET A 23 ? 0.1867 0.2320 0.2025 0.0001 0.0109 0.0015 23 MET A CB 185 C CG . MET A 23 ? 0.1714 0.2135 0.1882 -0.0008 0.0112 0.0009 23 MET A CG 186 S SD . MET A 23 ? 0.1857 0.2234 0.2023 0.0002 0.0120 0.0021 23 MET A SD 187 C CE . MET A 23 ? 0.1737 0.2126 0.1882 -0.0010 0.0102 0.0035 23 MET A CE 188 N N . THR A 24 ? 0.1774 0.2327 0.1910 -0.0021 0.0086 0.0012 24 THR A N 189 C CA . THR A 24 ? 0.1857 0.2449 0.1980 -0.0022 0.0080 0.0016 24 THR A CA 190 C C . THR A 24 ? 0.1842 0.2425 0.1957 -0.0014 0.0081 0.0026 24 THR A C 191 O O . THR A 24 ? 0.1895 0.2439 0.2011 -0.0011 0.0084 0.0032 24 THR A O 192 C CB . THR A 24 ? 0.1954 0.2569 0.2067 -0.0048 0.0070 0.0016 24 THR A CB 193 O OG1 . THR A 24 ? 0.1937 0.2522 0.2041 -0.0062 0.0065 0.0023 24 THR A OG1 194 C CG2 . THR A 24 ? 0.1871 0.2499 0.1989 -0.0056 0.0068 0.0007 24 THR A CG2 195 N N . LEU A 25 ? 0.1877 0.2501 0.1983 -0.0010 0.0078 0.0027 25 LEU A N 196 C CA . LEU A 25 ? 0.1855 0.2482 0.1955 -0.0001 0.0078 0.0034 25 LEU A CA 197 C C . LEU A 25 ? 0.1849 0.2453 0.1941 -0.0026 0.0071 0.0037 25 LEU A C 198 O O . LEU A 25 ? 0.1853 0.2431 0.1943 -0.0020 0.0072 0.0044 25 LEU A O 199 C CB . LEU A 25 ? 0.1874 0.2562 0.1966 0.0006 0.0076 0.0030 25 LEU A CB 200 C CG . LEU A 25 ? 0.1941 0.2644 0.2025 0.0014 0.0075 0.0034 25 LEU A CG 201 C CD1 . LEU A 25 ? 0.2176 0.2843 0.2261 0.0045 0.0085 0.0046 25 LEU A CD1 202 C CD2 . LEU A 25 ? 0.2201 0.2977 0.2280 0.0020 0.0072 0.0026 25 LEU A CD2 203 N N . ALA A 26 ? 0.1880 0.2491 0.1968 -0.0053 0.0065 0.0033 26 ALA A N 204 C CA . ALA A 26 ? 0.1717 0.2301 0.1795 -0.0075 0.0060 0.0037 26 ALA A CA 205 C C . ALA A 26 ? 0.1746 0.2277 0.1829 -0.0069 0.0062 0.0043 26 ALA A C 206 O O . ALA A 26 ? 0.1760 0.2264 0.1838 -0.0073 0.0060 0.0049 26 ALA A O 207 C CB . ALA A 26 ? 0.1786 0.2381 0.1857 -0.0100 0.0057 0.0034 26 ALA A CB 208 N N . GLU A 27 ? 0.1677 0.2198 0.1771 -0.0060 0.0065 0.0040 27 GLU A N 209 C CA . GLU A 27 ? 0.1590 0.2068 0.1691 -0.0056 0.0068 0.0042 27 GLU A CA 210 C C . GLU A 27 ? 0.1716 0.2172 0.1823 -0.0036 0.0075 0.0047 27 GLU A C 211 O O . GLU A 27 ? 0.1725 0.2147 0.1831 -0.0036 0.0076 0.0052 27 GLU A O 212 C CB . GLU A 27 ? 0.1525 0.2003 0.1639 -0.0053 0.0071 0.0033 27 GLU A CB 213 C CG . GLU A 27 ? 0.1747 0.2240 0.1853 -0.0071 0.0063 0.0031 27 GLU A CG 214 C CD . GLU A 27 ? 0.1721 0.2234 0.1839 -0.0068 0.0065 0.0019 27 GLU A CD 215 O OE1 . GLU A 27 ? 0.1760 0.2282 0.1890 -0.0055 0.0072 0.0012 27 GLU A OE1 216 O OE2 . GLU A 27 ? 0.1826 0.2345 0.1938 -0.0079 0.0060 0.0018 27 GLU A OE2 217 N N . LYS A 28 ? 0.1679 0.2155 0.1789 -0.0017 0.0082 0.0047 28 LYS A N 218 C CA . LYS A 28 ? 0.1761 0.2217 0.1872 0.0005 0.0091 0.0055 28 LYS A CA 219 C C . LYS A 28 ? 0.1755 0.2213 0.1854 0.0001 0.0085 0.0062 28 LYS A C 220 O O . LYS A 28 ? 0.1713 0.2137 0.1812 0.0006 0.0088 0.0069 28 LYS A O 221 C CB . LYS A 28 ? 0.1918 0.2399 0.2030 0.0029 0.0100 0.0056 28 LYS A CB 222 C CG . LYS A 28 ? 0.2120 0.2585 0.2246 0.0038 0.0111 0.0048 28 LYS A CG 223 C CD . LYS A 28 ? 0.2113 0.2601 0.2237 0.0064 0.0121 0.0050 28 LYS A CD 224 C CE . LYS A 28 ? 0.2394 0.2867 0.2533 0.0070 0.0134 0.0040 28 LYS A CE 225 N NZ . LYS A 28 ? 0.2257 0.2751 0.2391 0.0098 0.0145 0.0042 28 LYS A NZ 226 N N . ILE A 29 ? 0.1744 0.2242 0.1833 -0.0009 0.0077 0.0059 29 ILE A N 227 C CA . ILE A 29 ? 0.1759 0.2265 0.1838 -0.0015 0.0072 0.0062 29 ILE A CA 228 C C . ILE A 29 ? 0.1838 0.2305 0.1914 -0.0036 0.0067 0.0064 29 ILE A C 229 O O . ILE A 29 ? 0.1783 0.2232 0.1854 -0.0033 0.0066 0.0068 29 ILE A O 230 C CB . ILE A 29 ? 0.1960 0.2523 0.2032 -0.0025 0.0067 0.0053 29 ILE A CB 231 C CG1 . ILE A 29 ? 0.1911 0.2512 0.1984 0.0005 0.0072 0.0054 29 ILE A CG1 232 C CG2 . ILE A 29 ? 0.2188 0.2756 0.2252 -0.0040 0.0062 0.0051 29 ILE A CG2 233 C CD1 . ILE A 29 ? 0.2095 0.2762 0.2165 -0.0004 0.0067 0.0043 29 ILE A CD1 234 N N . GLY A 30 ? 0.1755 0.2208 0.1832 -0.0052 0.0064 0.0061 30 GLY A N 235 C CA . GLY A 30 ? 0.1733 0.2147 0.1804 -0.0066 0.0060 0.0064 30 GLY A CA 236 C C . GLY A 30 ? 0.1644 0.2023 0.1723 -0.0052 0.0064 0.0070 30 GLY A C 237 O O . GLY A 30 ? 0.1704 0.2058 0.1775 -0.0056 0.0062 0.0074 30 GLY A O 238 N N . GLN A 31 ? 0.1685 0.2058 0.1777 -0.0035 0.0072 0.0068 31 GLN A N 239 C CA . GLN A 31 ? 0.1548 0.1885 0.1648 -0.0023 0.0079 0.0072 31 GLN A CA 240 C C . GLN A 31 ? 0.1619 0.1951 0.1713 -0.0011 0.0081 0.0080 31 GLN A C 241 O O . GLN A 31 ? 0.1593 0.1896 0.1688 -0.0009 0.0083 0.0084 31 GLN A O 242 C CB . GLN A 31 ? 0.1599 0.1928 0.1715 -0.0008 0.0092 0.0068 31 GLN A CB 243 C CG . GLN A 31 ? 0.1634 0.1963 0.1760 -0.0019 0.0091 0.0057 31 GLN A CG 244 C CD . GLN A 31 ? 0.1673 0.1980 0.1799 -0.0030 0.0086 0.0055 31 GLN A CD 245 O OE1 . GLN A 31 ? 0.1777 0.2058 0.1911 -0.0023 0.0093 0.0056 31 GLN A OE1 246 N NE2 . GLN A 31 ? 0.1682 0.2000 0.1799 -0.0044 0.0075 0.0054 31 GLN A NE2 247 N N . MET A 32 ? 0.1631 0.1995 0.1718 -0.0003 0.0081 0.0082 32 MET A N 248 C CA . MET A 32 ? 0.1619 0.1989 0.1700 0.0011 0.0083 0.0088 32 MET A CA 249 C C . MET A 32 ? 0.1534 0.1907 0.1605 -0.0007 0.0073 0.0086 32 MET A C 250 O O . MET A 32 ? 0.1726 0.2110 0.1792 0.0003 0.0073 0.0089 32 MET A O 251 C CB . MET A 32 ? 0.1617 0.2032 0.1695 0.0028 0.0086 0.0089 32 MET A CB 252 C CG . MET A 32 ? 0.1621 0.2029 0.1707 0.0050 0.0099 0.0091 32 MET A CG 253 S SD . MET A 32 ? 0.1839 0.2307 0.1919 0.0073 0.0102 0.0091 32 MET A SD 254 C CE . MET A 32 ? 0.1757 0.2243 0.1825 0.0097 0.0105 0.0101 32 MET A CE 255 N N . THR A 33 ? 0.1527 0.1892 0.1594 -0.0031 0.0066 0.0081 33 THR A N 256 C CA . THR A 33 ? 0.1581 0.1944 0.1635 -0.0050 0.0059 0.0078 33 THR A CA 257 C C . THR A 33 ? 0.1538 0.1856 0.1590 -0.0056 0.0057 0.0083 33 THR A C 258 O O . THR A 33 ? 0.1619 0.1916 0.1672 -0.0062 0.0056 0.0084 33 THR A O 259 C CB . THR A 33 ? 0.1678 0.2061 0.1726 -0.0074 0.0055 0.0071 33 THR A CB 260 O OG1 . THR A 33 ? 0.1639 0.2070 0.1690 -0.0067 0.0057 0.0066 33 THR A OG1 261 C CG2 . THR A 33 ? 0.1694 0.2073 0.1730 -0.0095 0.0053 0.0066 33 THR A CG2 262 N N . GLN A 34 ? 0.1508 0.1814 0.1555 -0.0053 0.0056 0.0085 34 GLN A N 263 C CA . GLN A 34 ? 0.1573 0.1839 0.1615 -0.0059 0.0054 0.0088 34 GLN A CA 264 C C . GLN A 34 ? 0.1629 0.1891 0.1656 -0.0079 0.0051 0.0084 34 GLN A C 265 O O . GLN A 34 ? 0.1640 0.1929 0.1665 -0.0082 0.0050 0.0078 34 GLN A O 266 C CB . GLN A 34 ? 0.1627 0.1877 0.1675 -0.0040 0.0057 0.0094 34 GLN A CB 267 C CG . GLN A 34 ? 0.1512 0.1724 0.1555 -0.0045 0.0054 0.0097 34 GLN A CG 268 C CD . GLN A 34 ? 0.1591 0.1791 0.1639 -0.0028 0.0058 0.0102 34 GLN A CD 269 O OE1 . GLN A 34 ? 0.1684 0.1895 0.1727 -0.0023 0.0057 0.0102 34 GLN A OE1 270 N NE2 . GLN A 34 ? 0.1602 0.1783 0.1661 -0.0018 0.0063 0.0105 34 GLN A NE2 271 N N . ILE A 35 ? 0.1530 0.1762 0.1547 -0.0092 0.0049 0.0086 35 ILE A N 272 C CA . ILE A 35 ? 0.1505 0.1725 0.1507 -0.0112 0.0050 0.0082 35 ILE A CA 273 C C . ILE A 35 ? 0.1566 0.1742 0.1558 -0.0111 0.0049 0.0087 35 ILE A C 274 O O . ILE A 35 ? 0.1677 0.1833 0.1672 -0.0098 0.0047 0.0094 35 ILE A O 275 C CB . ILE A 35 ? 0.1575 0.1799 0.1568 -0.0132 0.0053 0.0079 35 ILE A CB 276 C CG1 . ILE A 35 ? 0.1551 0.1745 0.1537 -0.0129 0.0053 0.0089 35 ILE A CG1 277 C CG2 . ILE A 35 ? 0.1684 0.1955 0.1688 -0.0131 0.0053 0.0073 35 ILE A CG2 278 C CD1 . ILE A 35 ? 0.1783 0.1978 0.1757 -0.0147 0.0057 0.0089 35 ILE A CD1 279 N N . GLU A 36 ? 0.1656 0.1818 0.1636 -0.0124 0.0052 0.0082 36 GLU A N 280 C CA . GLU A 36 ? 0.1638 0.1756 0.1606 -0.0123 0.0053 0.0087 36 GLU A CA 281 C C . GLU A 36 ? 0.1786 0.1872 0.1738 -0.0127 0.0055 0.0096 36 GLU A C 282 O O . GLU A 36 ? 0.1794 0.1884 0.1739 -0.0142 0.0060 0.0095 36 GLU A O 283 C CB . GLU A 36 ? 0.1811 0.1921 0.1769 -0.0139 0.0057 0.0077 36 GLU A CB 284 C CG . GLU A 36 ? 0.1810 0.1912 0.1770 -0.0129 0.0054 0.0075 36 GLU A CG 285 C CD . GLU A 36 ? 0.1960 0.2015 0.1909 -0.0118 0.0054 0.0085 36 GLU A CD 286 O OE1 . GLU A 36 ? 0.2000 0.2024 0.1936 -0.0121 0.0057 0.0092 36 GLU A OE1 287 O OE2 . GLU A 36 ? 0.2009 0.2061 0.1962 -0.0106 0.0050 0.0084 36 GLU A OE2 288 N N . ARG A 37 ? 0.1678 0.1734 0.1624 -0.0113 0.0053 0.0104 37 ARG A N 289 C CA . ARG A 37 ? 0.1742 0.1768 0.1669 -0.0114 0.0057 0.0113 37 ARG A CA 290 C C . ARG A 37 ? 0.1731 0.1728 0.1636 -0.0135 0.0068 0.0113 37 ARG A C 291 O O . ARG A 37 ? 0.1902 0.1883 0.1790 -0.0140 0.0074 0.0121 37 ARG A O 292 C CB . ARG A 37 ? 0.1676 0.1676 0.1596 -0.0095 0.0053 0.0121 37 ARG A CB 293 C CG . ARG A 37 ? 0.1749 0.1727 0.1665 -0.0092 0.0053 0.0119 37 ARG A CG 294 C CD . ARG A 37 ? 0.1766 0.1711 0.1666 -0.0076 0.0053 0.0128 37 ARG A CD 295 N NE . ARG A 37 ? 0.1786 0.1695 0.1658 -0.0080 0.0062 0.0136 37 ARG A NE 296 C CZ . ARG A 37 ? 0.1764 0.1635 0.1617 -0.0091 0.0071 0.0136 37 ARG A CZ 297 N NH1 . ARG A 37 ? 0.1894 0.1763 0.1755 -0.0098 0.0071 0.0126 37 ARG A NH1 298 N NH2 . ARG A 37 ? 0.1813 0.1646 0.1639 -0.0093 0.0083 0.0147 37 ARG A NH2 299 N N . LEU A 38 ? 0.1869 0.1862 0.1774 -0.0146 0.0071 0.0103 38 LEU A N 300 C CA . LEU A 38 ? 0.2104 0.2066 0.1990 -0.0169 0.0085 0.0099 38 LEU A CA 301 C C . LEU A 38 ? 0.2266 0.2249 0.2152 -0.0191 0.0093 0.0094 38 LEU A C 302 O O . LEU A 38 ? 0.2752 0.2703 0.2620 -0.0209 0.0108 0.0094 38 LEU A O 303 C CB . LEU A 38 ? 0.2296 0.2261 0.2188 -0.0179 0.0087 0.0084 38 LEU A CB 304 C CG . LEU A 38 ? 0.2637 0.2569 0.2522 -0.0161 0.0083 0.0089 38 LEU A CG 305 C CD1 . LEU A 38 ? 0.3038 0.2990 0.2935 -0.0165 0.0080 0.0074 38 LEU A CD1 306 C CD2 . LEU A 38 ? 0.2785 0.2656 0.2641 -0.0164 0.0096 0.0098 38 LEU A CD2 307 N N . VAL A 39 ? 0.1975 0.2010 0.1882 -0.0189 0.0085 0.0089 39 VAL A N 308 C CA . VAL A 39 ? 0.2019 0.2079 0.1926 -0.0209 0.0091 0.0083 39 VAL A CA 309 C C . VAL A 39 ? 0.2029 0.2099 0.1935 -0.0198 0.0087 0.0095 39 VAL A C 310 O O . VAL A 39 ? 0.2196 0.2291 0.2105 -0.0211 0.0091 0.0092 39 VAL A O 311 C CB . VAL A 39 ? 0.2054 0.2171 0.1981 -0.0218 0.0088 0.0065 39 VAL A CB 312 C CG1 . VAL A 39 ? 0.2211 0.2325 0.2138 -0.0232 0.0093 0.0050 39 VAL A CG1 313 C CG2 . VAL A 39 ? 0.2061 0.2215 0.2008 -0.0193 0.0074 0.0068 39 VAL A CG2 314 N N . ALA A 40 ? 0.1816 0.1873 0.1723 -0.0173 0.0079 0.0107 40 ALA A N 315 C CA . ALA A 40 ? 0.1912 0.1986 0.1822 -0.0162 0.0075 0.0114 40 ALA A CA 316 C C . ALA A 40 ? 0.2108 0.2150 0.1993 -0.0163 0.0083 0.0127 40 ALA A C 317 O O . ALA A 40 ? 0.2468 0.2466 0.2332 -0.0160 0.0090 0.0136 40 ALA A O 318 C CB . ALA A 40 ? 0.1903 0.1984 0.1827 -0.0137 0.0064 0.0117 40 ALA A CB 319 N N . THR A 41 ? 0.2081 0.2147 0.1965 -0.0166 0.0084 0.0130 41 THR A N 320 C CA . THR A 41 ? 0.2152 0.2198 0.2014 -0.0159 0.0091 0.0145 41 THR A CA 321 C C . THR A 41 ? 0.2103 0.2193 0.1979 -0.0147 0.0082 0.0143 41 THR A C 322 O O . THR A 41 ? 0.2166 0.2294 0.2067 -0.0148 0.0074 0.0131 41 THR A O 323 C CB . THR A 41 ? 0.2118 0.2145 0.1959 -0.0182 0.0108 0.0148 41 THR A CB 324 O OG1 . THR A 41 ? 0.2407 0.2480 0.2264 -0.0197 0.0106 0.0139 41 THR A OG1 325 C CG2 . THR A 41 ? 0.2304 0.2293 0.2135 -0.0202 0.0120 0.0143 41 THR A CG2 326 N N . PRO A 42 ? 0.2237 0.2323 0.2097 -0.0133 0.0083 0.0155 42 PRO A N 327 C CA . PRO A 42 ? 0.2199 0.2331 0.2075 -0.0122 0.0074 0.0150 42 PRO A CA 328 C C . PRO A 42 ? 0.2170 0.2335 0.2057 -0.0141 0.0076 0.0142 42 PRO A C 329 O O . PRO A 42 ? 0.2242 0.2448 0.2155 -0.0137 0.0068 0.0130 42 PRO A O 330 C CB . PRO A 42 ? 0.2511 0.2632 0.2360 -0.0106 0.0079 0.0165 42 PRO A CB 331 C CG . PRO A 42 ? 0.2627 0.2701 0.2457 -0.0096 0.0082 0.0175 42 PRO A CG 332 C CD . PRO A 42 ? 0.2487 0.2530 0.2316 -0.0119 0.0091 0.0172 42 PRO A CD 333 N N . ASP A 43 ? 0.2291 0.2440 0.2161 -0.0161 0.0089 0.0147 43 ASP A N 334 C CA . ASP A 43 ? 0.2424 0.2610 0.2305 -0.0179 0.0091 0.0138 43 ASP A CA 335 C C . ASP A 43 ? 0.2152 0.2365 0.2058 -0.0187 0.0085 0.0122 43 ASP A C 336 O O . ASP A 43 ? 0.2231 0.2487 0.2156 -0.0187 0.0079 0.0112 43 ASP A O 337 C CB . ASP A 43 ? 0.2675 0.2836 0.2531 -0.0202 0.0109 0.0146 43 ASP A CB 338 C CG . ASP A 43 ? 0.3545 0.3690 0.3374 -0.0191 0.0118 0.0164 43 ASP A CG 339 O OD1 . ASP A 43 ? 0.3758 0.3936 0.3592 -0.0174 0.0109 0.0166 43 ASP A OD1 340 O OD2 . ASP A 43 ? 0.4271 0.4369 0.4071 -0.0199 0.0135 0.0177 43 ASP A OD2 341 N N . VAL A 44 ? 0.1995 0.2183 0.1902 -0.0191 0.0086 0.0118 44 VAL A N 342 C CA . VAL A 44 ? 0.1861 0.2078 0.1790 -0.0195 0.0080 0.0104 44 VAL A CA 343 C C . VAL A 44 ? 0.1900 0.2143 0.1851 -0.0173 0.0068 0.0100 44 VAL A C 344 O O . VAL A 44 ? 0.1879 0.2161 0.1848 -0.0171 0.0064 0.0090 44 VAL A O 345 C CB . VAL A 44 ? 0.1939 0.2125 0.1862 -0.0202 0.0084 0.0101 44 VAL A CB 346 C CG1 . VAL A 44 ? 0.1918 0.2134 0.1864 -0.0195 0.0075 0.0089 44 VAL A CG1 347 C CG2 . VAL A 44 ? 0.2027 0.2195 0.1933 -0.0231 0.0099 0.0098 44 VAL A CG2 348 N N . LEU A 45 ? 0.1767 0.1990 0.1717 -0.0155 0.0063 0.0107 45 LEU A N 349 C CA . LEU A 45 ? 0.1808 0.2051 0.1781 -0.0136 0.0055 0.0101 45 LEU A CA 350 C C . LEU A 45 ? 0.1788 0.2068 0.1773 -0.0132 0.0053 0.0096 45 LEU A C 351 O O . LEU A 45 ? 0.1799 0.2102 0.1804 -0.0124 0.0050 0.0087 45 LEU A O 352 C CB . LEU A 45 ? 0.1866 0.2082 0.1834 -0.0120 0.0052 0.0107 45 LEU A CB 353 C CG . LEU A 45 ? 0.2015 0.2197 0.1976 -0.0119 0.0053 0.0110 45 LEU A CG 354 C CD1 . LEU A 45 ? 0.2029 0.2189 0.1983 -0.0103 0.0050 0.0116 45 LEU A CD1 355 C CD2 . LEU A 45 ? 0.2032 0.2225 0.2013 -0.0115 0.0050 0.0102 45 LEU A CD2 356 N N . ARG A 46 ? 0.1911 0.2194 0.1881 -0.0137 0.0056 0.0101 46 ARG A N 357 C CA . ARG A 46 ? 0.2181 0.2502 0.2161 -0.0134 0.0054 0.0096 46 ARG A CA 358 C C . ARG A 46 ? 0.2168 0.2519 0.2154 -0.0148 0.0056 0.0089 46 ARG A C 359 O O . ARG A 46 ? 0.2215 0.2598 0.2221 -0.0141 0.0053 0.0079 46 ARG A O 360 C CB . ARG A 46 ? 0.2669 0.2985 0.2627 -0.0135 0.0057 0.0106 46 ARG A CB 361 C CG A ARG A 46 ? 0.2984 0.3339 0.2951 -0.0128 0.0054 0.0100 46 ARG A CG 362 C CG B ARG A 46 ? 0.2458 0.2784 0.2419 -0.0117 0.0053 0.0105 46 ARG A CG 363 C CD A ARG A 46 ? 0.3298 0.3648 0.3238 -0.0128 0.0059 0.0113 46 ARG A CD 364 C CD B ARG A 46 ? 0.2449 0.2783 0.2387 -0.0119 0.0057 0.0115 46 ARG A CD 365 N NE A ARG A 46 ? 0.3938 0.4266 0.3866 -0.0111 0.0058 0.0121 46 ARG A NE 366 N NE B ARG A 46 ? 0.2621 0.2914 0.2529 -0.0127 0.0067 0.0132 46 ARG A NE 367 C CZ A ARG A 46 ? 0.4364 0.4652 0.4265 -0.0111 0.0065 0.0137 46 ARG A CZ 368 C CZ B ARG A 46 ? 0.2635 0.2895 0.2523 -0.0114 0.0069 0.0144 46 ARG A CZ 369 N NH1 A ARG A 46 ? 0.4573 0.4848 0.4463 -0.0091 0.0062 0.0143 46 ARG A NH1 370 N NH1 B ARG A 46 ? 0.2683 0.2900 0.2541 -0.0122 0.0081 0.0160 46 ARG A NH1 371 N NH2 A ARG A 46 ? 0.4420 0.4680 0.4302 -0.0129 0.0076 0.0146 46 ARG A NH2 372 N NH2 B ARG A 46 ? 0.2670 0.2942 0.2568 -0.0094 0.0061 0.0140 46 ARG A NH2 373 N N . ASP A 47 ? 0.2171 0.2512 0.2141 -0.0167 0.0063 0.0092 47 ASP A N 374 C CA . ASP A 47 ? 0.2333 0.2709 0.2308 -0.0182 0.0066 0.0084 47 ASP A CA 375 C C . ASP A 47 ? 0.2154 0.2556 0.2149 -0.0176 0.0062 0.0073 47 ASP A C 376 O O . ASP A 47 ? 0.2516 0.2960 0.2521 -0.0178 0.0061 0.0064 47 ASP A O 377 C CB . ASP A 47 ? 0.2381 0.2739 0.2336 -0.0207 0.0077 0.0088 47 ASP A CB 378 C CG . ASP A 47 ? 0.2680 0.3018 0.2613 -0.0213 0.0085 0.0100 47 ASP A CG 379 O OD1 . ASP A 47 ? 0.2805 0.3112 0.2718 -0.0231 0.0098 0.0106 47 ASP A OD1 380 O OD2 . ASP A 47 ? 0.2967 0.3316 0.2899 -0.0199 0.0081 0.0105 47 ASP A OD2 381 N N . ASN A 48 ? 0.1811 0.2190 0.1810 -0.0167 0.0059 0.0074 48 ASN A N 382 C CA . ASN A 48 ? 0.1767 0.2168 0.1780 -0.0159 0.0057 0.0066 48 ASN A CA 383 C C . ASN A 48 ? 0.1619 0.2016 0.1648 -0.0134 0.0053 0.0067 48 ASN A C 384 O O . ASN A 48 ? 0.1740 0.2148 0.1780 -0.0122 0.0053 0.0064 48 ASN A O 385 C CB . ASN A 48 ? 0.1774 0.2157 0.1780 -0.0167 0.0059 0.0066 48 ASN A CB 386 C CG . ASN A 48 ? 0.1932 0.2322 0.1926 -0.0194 0.0066 0.0061 48 ASN A CG 387 O OD1 . ASN A 48 ? 0.2247 0.2680 0.2247 -0.0203 0.0067 0.0050 48 ASN A OD1 388 N ND2 . ASN A 48 ? 0.2023 0.2370 0.1998 -0.0207 0.0072 0.0068 48 ASN A ND2 389 N N . PHE A 49 ? 0.1699 0.2083 0.1731 -0.0127 0.0052 0.0070 49 PHE A N 390 C CA . PHE A 49 ? 0.1668 0.2049 0.1718 -0.0108 0.0052 0.0066 49 PHE A CA 391 C C . PHE A 49 ? 0.1614 0.1971 0.1669 -0.0097 0.0052 0.0069 49 PHE A C 392 O O . PHE A 49 ? 0.1548 0.1910 0.1618 -0.0082 0.0056 0.0066 49 PHE A O 393 C CB . PHE A 49 ? 0.1702 0.2119 0.1766 -0.0099 0.0054 0.0058 49 PHE A CB 394 C CG . PHE A 49 ? 0.1805 0.2251 0.1865 -0.0109 0.0053 0.0055 49 PHE A CG 395 C CD1 . PHE A 49 ? 0.1674 0.2122 0.1737 -0.0108 0.0052 0.0052 49 PHE A CD1 396 C CD2 . PHE A 49 ? 0.1821 0.2298 0.1875 -0.0120 0.0053 0.0052 49 PHE A CD2 397 C CE1 . PHE A 49 ? 0.1772 0.2249 0.1830 -0.0116 0.0051 0.0049 49 PHE A CE1 398 C CE2 . PHE A 49 ? 0.1812 0.2318 0.1863 -0.0130 0.0053 0.0049 49 PHE A CE2 399 C CZ . PHE A 49 ? 0.1764 0.2268 0.1816 -0.0127 0.0052 0.0049 49 PHE A CZ 400 N N . ILE A 50 ? 0.1610 0.1940 0.1652 -0.0104 0.0051 0.0075 50 ILE A N 401 C CA . ILE A 50 ? 0.1550 0.1859 0.1594 -0.0096 0.0051 0.0078 50 ILE A CA 402 C C . ILE A 50 ? 0.1533 0.1827 0.1592 -0.0079 0.0053 0.0077 50 ILE A C 403 O O . ILE A 50 ? 0.1658 0.1943 0.1720 -0.0078 0.0052 0.0075 50 ILE A O 404 C CB . ILE A 50 ? 0.1569 0.1848 0.1595 -0.0107 0.0050 0.0083 50 ILE A CB 405 C CG1 . ILE A 50 ? 0.1677 0.1969 0.1690 -0.0127 0.0052 0.0081 50 ILE A CG1 406 C CG2 . ILE A 50 ? 0.1520 0.1776 0.1547 -0.0098 0.0050 0.0086 50 ILE A CG2 407 C CD1 . ILE A 50 ? 0.1618 0.1945 0.1638 -0.0127 0.0053 0.0074 50 ILE A CD1 408 N N . GLY A 51 ? 0.1507 0.1799 0.1574 -0.0067 0.0057 0.0078 51 GLY A N 409 C CA . GLY A 51 ? 0.1540 0.1815 0.1623 -0.0052 0.0063 0.0076 51 GLY A CA 410 C C . GLY A 51 ? 0.1543 0.1788 0.1623 -0.0050 0.0062 0.0080 51 GLY A C 411 O O . GLY A 51 ? 0.1553 0.1784 0.1645 -0.0043 0.0067 0.0077 51 GLY A O 412 N N . SER A 52 ? 0.1503 0.1739 0.1569 -0.0056 0.0057 0.0086 52 SER A N 413 C CA . SER A 52 ? 0.1502 0.1711 0.1566 -0.0051 0.0057 0.0089 52 SER A CA 414 C C . SER A 52 ? 0.1504 0.1701 0.1549 -0.0063 0.0051 0.0093 52 SER A C 415 O O . SER A 52 ? 0.1445 0.1655 0.1480 -0.0074 0.0050 0.0092 52 SER A O 416 C CB . SER A 52 ? 0.1569 0.1777 0.1642 -0.0036 0.0063 0.0092 52 SER A CB 417 O OG . SER A 52 ? 0.1512 0.1696 0.1584 -0.0031 0.0063 0.0096 52 SER A OG 418 N N . LEU A 53 ? 0.1556 0.1726 0.1595 -0.0060 0.0049 0.0096 53 LEU A N 419 C CA . LEU A 53 ? 0.1662 0.1813 0.1683 -0.0068 0.0046 0.0100 53 LEU A CA 420 C C . LEU A 53 ? 0.1525 0.1659 0.1548 -0.0058 0.0046 0.0102 53 LEU A C 421 O O . LEU A 53 ? 0.1554 0.1688 0.1592 -0.0046 0.0049 0.0101 53 LEU A O 422 C CB . LEU A 53 ? 0.1944 0.2074 0.1949 -0.0072 0.0044 0.0103 53 LEU A CB 423 C CG . LEU A 53 ? 0.2227 0.2368 0.2223 -0.0085 0.0045 0.0104 53 LEU A CG 424 C CD1 . LEU A 53 ? 0.2531 0.2692 0.2539 -0.0079 0.0044 0.0101 53 LEU A CD1 425 C CD2 . LEU A 53 ? 0.2713 0.2825 0.2683 -0.0092 0.0046 0.0111 53 LEU A CD2 426 N N . LEU A 54 ? 0.1474 0.1597 0.1485 -0.0064 0.0045 0.0102 54 LEU A N 427 C CA . LEU A 54 ? 0.1389 0.1494 0.1400 -0.0055 0.0044 0.0104 54 LEU A CA 428 C C . LEU A 54 ? 0.1559 0.1636 0.1549 -0.0063 0.0042 0.0106 54 LEU A C 429 O O . LEU A 54 ? 0.1604 0.1676 0.1581 -0.0078 0.0044 0.0104 54 LEU A O 430 C CB . LEU A 54 ? 0.1522 0.1645 0.1541 -0.0047 0.0046 0.0103 54 LEU A CB 431 C CG . LEU A 54 ? 0.1453 0.1587 0.1461 -0.0058 0.0045 0.0098 54 LEU A CG 432 C CD1 . LEU A 54 ? 0.1610 0.1758 0.1624 -0.0044 0.0046 0.0098 54 LEU A CD1 433 C CD2 . LEU A 54 ? 0.1541 0.1708 0.1551 -0.0069 0.0046 0.0092 54 LEU A CD2 434 N N . SER A 55 ? 0.1527 0.1584 0.1516 -0.0053 0.0041 0.0108 55 SER A N 435 C CA . SER A 55 ? 0.1521 0.1554 0.1494 -0.0057 0.0040 0.0108 55 SER A CA 436 C C . SER A 55 ? 0.1677 0.1723 0.1658 -0.0052 0.0040 0.0104 55 SER A C 437 O O . SER A 55 ? 0.1702 0.1754 0.1695 -0.0037 0.0040 0.0106 55 SER A O 438 C CB . SER A 55 ? 0.1574 0.1580 0.1540 -0.0045 0.0038 0.0113 55 SER A CB 439 O OG . SER A 55 ? 0.1677 0.1668 0.1628 -0.0047 0.0039 0.0117 55 SER A OG 440 N N . GLY A 56 ? 0.1652 0.1707 0.1627 -0.0065 0.0042 0.0097 56 GLY A N 441 C CA . GLY A 56 ? 0.1632 0.1701 0.1610 -0.0059 0.0041 0.0091 56 GLY A CA 442 C C . GLY A 56 ? 0.1641 0.1678 0.1610 -0.0054 0.0040 0.0093 56 GLY A C 443 O O . GLY A 56 ? 0.1771 0.1774 0.1728 -0.0054 0.0040 0.0098 56 GLY A O 444 N N . GLY A 57 ? 0.1710 0.1757 0.1680 -0.0049 0.0039 0.0088 57 GLY A N 445 C CA . GLY A 57 ? 0.1727 0.1745 0.1689 -0.0043 0.0038 0.0088 57 GLY A CA 446 C C . GLY A 57 ? 0.1741 0.1721 0.1683 -0.0057 0.0041 0.0084 57 GLY A C 447 O O . GLY A 57 ? 0.2019 0.2001 0.1955 -0.0077 0.0046 0.0074 57 GLY A O 448 N N . GLY A 58 ? 0.1753 0.1698 0.1685 -0.0048 0.0040 0.0093 58 GLY A N 449 C CA . GLY A 58 ? 0.1747 0.1649 0.1656 -0.0057 0.0046 0.0093 58 GLY A CA 450 C C . GLY A 58 ? 0.1849 0.1739 0.1748 -0.0068 0.0051 0.0098 58 GLY A C 451 O O . GLY A 58 ? 0.2197 0.2047 0.2074 -0.0074 0.0059 0.0101 58 GLY A O 452 N N . SER A 59 ? 0.1682 0.1602 0.1594 -0.0069 0.0048 0.0101 59 SER A N 453 C CA . SER A 59 ? 0.1722 0.1636 0.1626 -0.0079 0.0053 0.0106 59 SER A CA 454 C C . SER A 59 ? 0.1703 0.1602 0.1599 -0.0062 0.0050 0.0118 59 SER A C 455 O O . SER A 59 ? 0.1882 0.1808 0.1795 -0.0050 0.0044 0.0120 59 SER A O 456 C CB . SER A 59 ? 0.1806 0.1762 0.1727 -0.0088 0.0051 0.0101 59 SER A CB 457 O OG . SER A 59 ? 0.1827 0.1777 0.1739 -0.0098 0.0056 0.0105 59 SER A OG 458 N N . VAL A 60 ? 0.1790 0.1648 0.1660 -0.0059 0.0056 0.0125 60 VAL A N 459 C CA . VAL A 60 ? 0.1793 0.1641 0.1653 -0.0038 0.0053 0.0136 60 VAL A CA 460 C C . VAL A 60 ? 0.2010 0.1829 0.1843 -0.0040 0.0062 0.0147 60 VAL A C 461 O O . VAL A 60 ? 0.2090 0.1880 0.1908 -0.0057 0.0074 0.0146 60 VAL A O 462 C CB . VAL A 60 ? 0.1743 0.1570 0.1595 -0.0020 0.0050 0.0137 60 VAL A CB 463 C CG1 . VAL A 60 ? 0.1804 0.1658 0.1681 -0.0018 0.0043 0.0128 60 VAL A CG1 464 C CG2 . VAL A 60 ? 0.1902 0.1680 0.1728 -0.0027 0.0061 0.0138 60 VAL A CG2 465 N N . PRO A 61 ? 0.2069 0.1898 0.1896 -0.0022 0.0059 0.0156 61 PRO A N 466 C CA . PRO A 61 ? 0.2022 0.1825 0.1821 -0.0022 0.0069 0.0168 61 PRO A CA 467 C C . PRO A 61 ? 0.2082 0.1828 0.1848 -0.0014 0.0081 0.0178 61 PRO A C 468 O O . PRO A 61 ? 0.2160 0.1870 0.1902 -0.0024 0.0096 0.0186 61 PRO A O 469 C CB . PRO A 61 ? 0.2095 0.1934 0.1899 -0.0002 0.0061 0.0173 61 PRO A CB 470 C CG . PRO A 61 ? 0.1868 0.1734 0.1695 0.0012 0.0049 0.0164 61 PRO A CG 471 C CD . PRO A 61 ? 0.1810 0.1680 0.1658 -0.0006 0.0048 0.0153 61 PRO A CD 472 N N . ARG A 62 ? 0.2165 0.1900 0.1928 0.0003 0.0077 0.0177 62 ARG A N 473 C CA . ARG A 62 ? 0.2481 0.2158 0.2216 0.0006 0.0089 0.0182 62 ARG A CA 474 C C . ARG A 62 ? 0.2485 0.2169 0.2230 0.0021 0.0079 0.0176 62 ARG A C 475 O O . ARG A 62 ? 0.2399 0.2128 0.2166 0.0034 0.0065 0.0172 62 ARG A O 476 C CB . ARG A 62 ? 0.2850 0.2487 0.2547 0.0026 0.0101 0.0201 62 ARG A CB 477 C CG . ARG A 62 ? 0.2672 0.2336 0.2363 0.0060 0.0091 0.0210 62 ARG A CG 478 C CD . ARG A 62 ? 0.3546 0.3162 0.3192 0.0083 0.0106 0.0231 62 ARG A CD 479 N NE . ARG A 62 ? 0.3763 0.3414 0.3404 0.0119 0.0095 0.0237 62 ARG A NE 480 C CZ . ARG A 62 ? 0.3676 0.3298 0.3279 0.0151 0.0103 0.0255 62 ARG A CZ 481 N NH1 . ARG A 62 ? 0.4129 0.3679 0.3695 0.0152 0.0126 0.0270 62 ARG A NH1 482 N NH2 . ARG A 62 ? 0.3265 0.2932 0.2869 0.0183 0.0091 0.0256 62 ARG A NH2 483 N N . LYS A 63 ? 0.2749 0.2388 0.2478 0.0020 0.0088 0.0175 63 LYS A N 484 C CA . LYS A 63 ? 0.2801 0.2443 0.2534 0.0037 0.0080 0.0170 63 LYS A CA 485 C C . LYS A 63 ? 0.2513 0.2164 0.2233 0.0071 0.0074 0.0181 63 LYS A C 486 O O . LYS A 63 ? 0.2563 0.2189 0.2254 0.0086 0.0083 0.0196 63 LYS A O 487 C CB . LYS A 63 ? 0.3499 0.3085 0.3211 0.0032 0.0094 0.0167 63 LYS A CB 488 C CG . LYS A 63 ? 0.4359 0.3936 0.4082 -0.0003 0.0102 0.0152 63 LYS A CG 489 C CD . LYS A 63 ? 0.4283 0.3917 0.4043 -0.0015 0.0087 0.0136 63 LYS A CD 490 C CE . LYS A 63 ? 0.4481 0.4127 0.4251 0.0000 0.0077 0.0130 63 LYS A CE 491 N NZ . LYS A 63 ? 0.3929 0.3605 0.3724 -0.0016 0.0072 0.0113 63 LYS A NZ 492 N N . GLY A 64 ? 0.2298 0.1990 0.2040 0.0084 0.0059 0.0174 64 GLY A N 493 C CA . GLY A 64 ? 0.2231 0.1940 0.1962 0.0117 0.0053 0.0181 64 GLY A CA 494 C C . GLY A 64 ? 0.2057 0.1809 0.1795 0.0124 0.0048 0.0184 64 GLY A C 495 O O . GLY A 64 ? 0.2350 0.2121 0.2077 0.0152 0.0044 0.0189 64 GLY A O 496 N N . ALA A 65 ? 0.2071 0.1840 0.1827 0.0101 0.0048 0.0180 65 ALA A N 497 C CA . ALA A 65 ? 0.2028 0.1837 0.1790 0.0106 0.0044 0.0182 65 ALA A CA 498 C C . ALA A 65 ? 0.1920 0.1786 0.1706 0.0123 0.0031 0.0171 65 ALA A C 499 O O . ALA A 65 ? 0.2045 0.1931 0.1858 0.0116 0.0025 0.0159 65 ALA A O 500 C CB . ALA A 65 ? 0.2025 0.1850 0.1809 0.0077 0.0045 0.0176 65 ALA A CB 501 N N . THR A 66 ? 0.1846 0.1739 0.1621 0.0144 0.0029 0.0175 66 THR A N 502 C CA . THR A 66 ? 0.1897 0.1853 0.1697 0.0156 0.0018 0.0161 66 THR A CA 503 C C . THR A 66 ? 0.1865 0.1861 0.1704 0.0133 0.0015 0.0145 66 THR A C 504 O O . THR A 66 ? 0.1843 0.1826 0.1686 0.0113 0.0019 0.0148 66 THR A O 505 C CB . THR A 66 ? 0.2021 0.2005 0.1799 0.0186 0.0017 0.0166 66 THR A CB 506 O OG1 . THR A 66 ? 0.2075 0.2067 0.1848 0.0179 0.0020 0.0172 66 THR A OG1 507 C CG2 . THR A 66 ? 0.2116 0.2057 0.1850 0.0215 0.0023 0.0185 66 THR A CG2 508 N N . ALA A 67 ? 0.1768 0.1814 0.1635 0.0137 0.0008 0.0128 67 ALA A N 509 C CA . ALA A 67 ? 0.1715 0.1798 0.1618 0.0118 0.0008 0.0113 67 ALA A CA 510 C C . ALA A 67 ? 0.1744 0.1845 0.1640 0.0117 0.0009 0.0116 67 ALA A C 511 O O . ALA A 67 ? 0.1724 0.1828 0.1637 0.0096 0.0011 0.0112 67 ALA A O 512 C CB . ALA A 67 ? 0.1937 0.2071 0.1870 0.0122 0.0004 0.0091 67 ALA A CB 513 N N . LYS A 68 ? 0.1741 0.1859 0.1612 0.0141 0.0007 0.0122 68 LYS A N 514 C CA . LYS A 68 ? 0.1757 0.1894 0.1618 0.0144 0.0008 0.0127 68 LYS A CA 515 C C . LYS A 68 ? 0.1826 0.1912 0.1668 0.0128 0.0016 0.0145 68 LYS A C 516 O O . LYS A 68 ? 0.1810 0.1910 0.1660 0.0115 0.0017 0.0143 68 LYS A O 517 C CB . LYS A 68 ? 0.2049 0.2213 0.1880 0.0180 0.0006 0.0134 68 LYS A CB 518 C CG A LYS A 68 ? 0.2439 0.2633 0.2261 0.0186 0.0007 0.0137 68 LYS A CG 519 C CG B LYS A 68 ? 0.2132 0.2301 0.1938 0.0189 0.0009 0.0147 68 LYS A CG 520 C CD A LYS A 68 ? 0.2635 0.2897 0.2497 0.0174 0.0001 0.0110 68 LYS A CD 521 C CD B LYS A 68 ? 0.2123 0.2328 0.1901 0.0229 0.0007 0.0153 68 LYS A CD 522 C CE A LYS A 68 ? 0.2684 0.3001 0.2537 0.0191 -0.0001 0.0108 68 LYS A CE 523 C CE B LYS A 68 ? 0.2213 0.2508 0.2020 0.0235 -0.0002 0.0127 68 LYS A CE 524 N NZ A LYS A 68 ? 0.3183 0.3501 0.3049 0.0168 0.0002 0.0106 68 LYS A NZ 525 N NZ B LYS A 68 ? 0.2099 0.2452 0.1888 0.0275 -0.0007 0.0124 68 LYS A NZ 526 N N . GLU A 69 ? 0.1831 0.1859 0.1648 0.0128 0.0021 0.0160 69 GLU A N 527 C CA . GLU A 69 ? 0.1785 0.1765 0.1587 0.0109 0.0031 0.0172 69 GLU A CA 528 C C . GLU A 69 ? 0.1797 0.1789 0.1633 0.0079 0.0029 0.0160 69 GLU A C 529 O O . GLU A 69 ? 0.1858 0.1845 0.1693 0.0063 0.0033 0.0163 69 GLU A O 530 C CB . GLU A 69 ? 0.2006 0.1924 0.1782 0.0110 0.0038 0.0185 69 GLU A CB 531 C CG . GLU A 69 ? 0.2116 0.2007 0.1848 0.0139 0.0046 0.0204 69 GLU A CG 532 C CD . GLU A 69 ? 0.2266 0.2089 0.1973 0.0138 0.0056 0.0214 69 GLU A CD 533 O OE1 . GLU A 69 ? 0.2493 0.2306 0.2186 0.0162 0.0054 0.0217 69 GLU A OE1 534 O OE2 . GLU A 69 ? 0.2402 0.2186 0.2105 0.0113 0.0066 0.0217 69 GLU A OE2 535 N N . TRP A 70 ? 0.1764 0.1768 0.1629 0.0072 0.0024 0.0146 70 TRP A N 536 C CA . TRP A 70 ? 0.1631 0.1647 0.1525 0.0049 0.0024 0.0136 70 TRP A CA 537 C C . TRP A 70 ? 0.1615 0.1675 0.1529 0.0045 0.0022 0.0126 70 TRP A C 538 O O . TRP A 70 ? 0.1601 0.1664 0.1523 0.0028 0.0025 0.0126 70 TRP A O 539 C CB . TRP A 70 ? 0.1633 0.1654 0.1551 0.0047 0.0021 0.0126 70 TRP A CB 540 C CG . TRP A 70 ? 0.1651 0.1632 0.1557 0.0042 0.0024 0.0132 70 TRP A CG 541 C CD1 . TRP A 70 ? 0.1690 0.1646 0.1577 0.0057 0.0023 0.0137 70 TRP A CD1 542 C CD2 . TRP A 70 ? 0.1542 0.1508 0.1457 0.0024 0.0027 0.0131 70 TRP A CD2 543 N NE1 . TRP A 70 ? 0.1632 0.1557 0.1515 0.0046 0.0026 0.0139 70 TRP A NE1 544 C CE2 . TRP A 70 ? 0.1615 0.1549 0.1516 0.0026 0.0028 0.0135 70 TRP A CE2 545 C CE3 . TRP A 70 ? 0.1601 0.1583 0.1534 0.0007 0.0029 0.0126 70 TRP A CE3 546 C CZ2 . TRP A 70 ? 0.1679 0.1599 0.1584 0.0011 0.0031 0.0132 70 TRP A CZ2 547 C CZ3 . TRP A 70 ? 0.1699 0.1668 0.1634 -0.0006 0.0031 0.0126 70 TRP A CZ3 548 C CH2 . TRP A 70 ? 0.1616 0.1556 0.1538 -0.0004 0.0032 0.0128 70 TRP A CH2 549 N N . GLN A 71 ? 0.1589 0.1688 0.1511 0.0061 0.0018 0.0117 71 GLN A N 550 C CA . GLN A 71 ? 0.1521 0.1667 0.1464 0.0057 0.0016 0.0103 71 GLN A CA 551 C C . GLN A 71 ? 0.1624 0.1766 0.1546 0.0055 0.0019 0.0116 71 GLN A C 552 O O . GLN A 71 ? 0.1757 0.1918 0.1695 0.0041 0.0020 0.0109 71 GLN A O 553 C CB . GLN A 71 ? 0.1558 0.1752 0.1510 0.0075 0.0012 0.0089 71 GLN A CB 554 C CG . GLN A 71 ? 0.1695 0.1902 0.1674 0.0072 0.0012 0.0073 71 GLN A CG 555 C CD . GLN A 71 ? 0.1847 0.2115 0.1847 0.0082 0.0009 0.0050 71 GLN A CD 556 O OE1 . GLN A 71 ? 0.2143 0.2427 0.2167 0.0080 0.0011 0.0034 71 GLN A OE1 557 N NE2 . GLN A 71 ? 0.1749 0.2054 0.1743 0.0091 0.0006 0.0046 71 GLN A NE2 558 N N . ASP A 72 ? 0.1742 0.1858 0.1626 0.0070 0.0021 0.0134 72 ASP A N 559 C CA . ASP A 72 ? 0.1743 0.1852 0.1604 0.0070 0.0026 0.0147 72 ASP A CA 560 C C . ASP A 72 ? 0.1768 0.1846 0.1630 0.0043 0.0032 0.0152 72 ASP A C 561 O O . ASP A 72 ? 0.1935 0.2028 0.1799 0.0033 0.0034 0.0153 72 ASP A O 562 C CB . ASP A 72 ? 0.2119 0.2201 0.1936 0.0094 0.0031 0.0168 72 ASP A CB 563 C CG . ASP A 72 ? 0.2039 0.2168 0.1853 0.0124 0.0024 0.0162 72 ASP A CG 564 O OD1 . ASP A 72 ? 0.2538 0.2724 0.2382 0.0124 0.0017 0.0141 72 ASP A OD1 565 O OD2 . ASP A 72 ? 0.2797 0.2904 0.2576 0.0148 0.0028 0.0179 72 ASP A OD2 566 N N . MET A 73 ? 0.1691 0.1733 0.1555 0.0032 0.0034 0.0154 73 MET A N 567 C CA . MET A 73 ? 0.1629 0.1651 0.1498 0.0007 0.0039 0.0154 73 MET A CA 568 C C . MET A 73 ? 0.1696 0.1758 0.1600 -0.0006 0.0035 0.0139 73 MET A C 569 O O . MET A 73 ? 0.1718 0.1789 0.1624 -0.0019 0.0038 0.0139 73 MET A O 570 C CB . MET A 73 ? 0.1835 0.1820 0.1702 0.0000 0.0042 0.0155 73 MET A CB 571 C CG . MET A 73 ? 0.1913 0.1890 0.1788 -0.0025 0.0046 0.0151 73 MET A CG 572 S SD . MET A 73 ? 0.2059 0.2012 0.1941 -0.0033 0.0046 0.0146 73 MET A SD 573 C CE . MET A 73 ? 0.2113 0.2103 0.2030 -0.0024 0.0037 0.0134 73 MET A CE 574 N N . VAL A 74 ? 0.1620 0.1704 0.1550 -0.0001 0.0030 0.0126 74 VAL A N 575 C CA . VAL A 74 ? 0.1634 0.1748 0.1596 -0.0011 0.0030 0.0112 74 VAL A CA 576 C C . VAL A 74 ? 0.1706 0.1855 0.1673 -0.0010 0.0029 0.0107 74 VAL A C 577 O O . VAL A 74 ? 0.1742 0.1904 0.1720 -0.0023 0.0031 0.0104 74 VAL A O 578 C CB . VAL A 74 ? 0.1814 0.1938 0.1801 -0.0006 0.0028 0.0100 74 VAL A CB 579 C CG1 . VAL A 74 ? 0.2021 0.2169 0.2039 -0.0016 0.0032 0.0088 74 VAL A CG1 580 C CG2 . VAL A 74 ? 0.1790 0.1881 0.1772 -0.0008 0.0029 0.0106 74 VAL A CG2 581 N N . ASP A 75 ? 0.1785 0.1954 0.1743 0.0006 0.0026 0.0106 75 ASP A N 582 C CA . ASP A 75 ? 0.1707 0.1916 0.1669 0.0009 0.0024 0.0099 75 ASP A CA 583 C C . ASP A 75 ? 0.1850 0.2046 0.1789 0.0002 0.0028 0.0114 75 ASP A C 584 O O . ASP A 75 ? 0.1894 0.2120 0.1844 -0.0004 0.0028 0.0107 75 ASP A O 585 C CB . ASP A 75 ? 0.1847 0.2083 0.1799 0.0032 0.0020 0.0097 75 ASP A CB 586 C CG . ASP A 75 ? 0.1805 0.2075 0.1788 0.0035 0.0017 0.0074 75 ASP A CG 587 O OD1 . ASP A 75 ? 0.2025 0.2298 0.2038 0.0021 0.0020 0.0061 75 ASP A OD1 588 O OD2 . ASP A 75 ? 0.2272 0.2565 0.2246 0.0055 0.0014 0.0071 75 ASP A OD2 589 N N . GLY A 76 ? 0.1879 0.2032 0.1787 0.0002 0.0033 0.0132 76 GLY A N 590 C CA . GLY A 76 ? 0.1948 0.2087 0.1835 -0.0008 0.0040 0.0145 76 GLY A CA 591 C C . GLY A 76 ? 0.1881 0.2025 0.1788 -0.0031 0.0041 0.0138 76 GLY A C 592 O O . GLY A 76 ? 0.2112 0.2276 0.2019 -0.0040 0.0043 0.0138 76 GLY A O 593 N N . PHE A 77 ? 0.1747 0.1879 0.1671 -0.0040 0.0040 0.0131 77 PHE A N 594 C CA . PHE A 77 ? 0.1706 0.1851 0.1650 -0.0057 0.0041 0.0123 77 PHE A CA 595 C C . PHE A 77 ? 0.1816 0.2002 0.1786 -0.0054 0.0037 0.0109 77 PHE A C 596 O O . PHE A 77 ? 0.1869 0.2076 0.1847 -0.0064 0.0039 0.0105 77 PHE A O 597 C CB . PHE A 77 ? 0.1686 0.1812 0.1640 -0.0062 0.0041 0.0120 77 PHE A CB 598 C CG . PHE A 77 ? 0.1821 0.1907 0.1752 -0.0068 0.0045 0.0129 77 PHE A CG 599 C CD1 . PHE A 77 ? 0.1958 0.2025 0.1866 -0.0081 0.0053 0.0138 77 PHE A CD1 600 C CD2 . PHE A 77 ? 0.1873 0.1939 0.1806 -0.0062 0.0044 0.0129 77 PHE A CD2 601 C CE1 . PHE A 77 ? 0.2039 0.2066 0.1928 -0.0090 0.0060 0.0143 77 PHE A CE1 602 C CE2 . PHE A 77 ? 0.2039 0.2068 0.1953 -0.0069 0.0048 0.0135 77 PHE A CE2 603 C CZ . PHE A 77 ? 0.1986 0.1995 0.1879 -0.0083 0.0057 0.0141 77 PHE A CZ 604 N N . GLN A 78 ? 0.1654 0.1856 0.1640 -0.0042 0.0034 0.0099 78 GLN A N 605 C CA . GLN A 78 ? 0.1592 0.1832 0.1605 -0.0041 0.0034 0.0083 78 GLN A CA 606 C C . GLN A 78 ? 0.1740 0.2010 0.1746 -0.0040 0.0033 0.0081 78 GLN A C 607 O O . GLN A 78 ? 0.1724 0.2021 0.1750 -0.0046 0.0034 0.0070 78 GLN A O 608 C CB . GLN A 78 ? 0.1771 0.2023 0.1804 -0.0031 0.0032 0.0069 78 GLN A CB 609 C CG . GLN A 78 ? 0.1655 0.1938 0.1720 -0.0033 0.0036 0.0049 78 GLN A CG 610 C CD . GLN A 78 ? 0.1736 0.2002 0.1817 -0.0041 0.0043 0.0047 78 GLN A CD 611 O OE1 . GLN A 78 ? 0.1720 0.1986 0.1797 -0.0048 0.0044 0.0053 78 GLN A OE1 612 N NE2 . GLN A 78 ? 0.1623 0.1878 0.1721 -0.0039 0.0048 0.0041 78 GLN A NE2 613 N N . LYS A 79 ? 0.1790 0.2057 0.1770 -0.0030 0.0031 0.0093 79 LYS A N 614 C CA . LYS A 79 ? 0.1896 0.2196 0.1868 -0.0026 0.0031 0.0093 79 LYS A CA 615 C C . LYS A 79 ? 0.1881 0.2179 0.1850 -0.0043 0.0035 0.0098 79 LYS A C 616 O O . LYS A 79 ? 0.1925 0.2260 0.1906 -0.0046 0.0034 0.0088 79 LYS A O 617 C CB . LYS A 79 ? 0.2109 0.2399 0.2045 -0.0010 0.0031 0.0110 79 LYS A CB 618 C CG . LYS A 79 ? 0.3074 0.3402 0.3000 -0.0002 0.0031 0.0111 79 LYS A CG 619 C CD . LYS A 79 ? 0.3708 0.4038 0.3603 0.0023 0.0031 0.0124 79 LYS A CD 620 C CE . LYS A 79 ? 0.4628 0.4999 0.4510 0.0034 0.0032 0.0128 79 LYS A CE 621 N NZ . LYS A 79 ? 0.5414 0.5776 0.5256 0.0060 0.0035 0.0149 79 LYS A NZ 622 N N . ALA A 80 ? 0.1830 0.2091 0.1786 -0.0055 0.0039 0.0109 80 ALA A N 623 C CA . ALA A 80 ? 0.1829 0.2092 0.1783 -0.0073 0.0043 0.0112 80 ALA A CA 624 C C . ALA A 80 ? 0.1853 0.2144 0.1839 -0.0078 0.0041 0.0095 80 ALA A C 625 O O . ALA A 80 ? 0.1921 0.2240 0.1913 -0.0084 0.0042 0.0090 80 ALA A O 626 C CB . ALA A 80 ? 0.1931 0.2154 0.1868 -0.0086 0.0049 0.0123 80 ALA A CB 627 N N . CYS A 81 ? 0.1755 0.2038 0.1760 -0.0074 0.0040 0.0088 81 CYS A N 628 C CA . CYS A 81 ? 0.1756 0.2058 0.1788 -0.0076 0.0041 0.0075 81 CYS A CA 629 C C . CYS A 81 ? 0.1953 0.2290 0.2003 -0.0070 0.0041 0.0060 81 CYS A C 630 O O . CYS A 81 ? 0.1957 0.2316 0.2021 -0.0074 0.0043 0.0052 81 CYS A O 631 C CB . CYS A 81 ? 0.1732 0.2013 0.1778 -0.0071 0.0043 0.0072 81 CYS A CB 632 S SG . CYS A 81 ? 0.1951 0.2201 0.1980 -0.0079 0.0043 0.0084 81 CYS A SG 633 N N . MET A 82 ? 0.1878 0.2225 0.1929 -0.0060 0.0038 0.0055 82 MET A N 634 C CA . MET A 82 ? 0.2005 0.2391 0.2075 -0.0056 0.0038 0.0036 82 MET A CA 635 C C . MET A 82 ? 0.2055 0.2470 0.2113 -0.0058 0.0036 0.0038 82 MET A C 636 O O . MET A 82 ? 0.2319 0.2772 0.2396 -0.0056 0.0036 0.0021 82 MET A O 637 C CB . MET A 82 ? 0.2118 0.2517 0.2192 -0.0044 0.0035 0.0027 82 MET A CB 638 C CG . MET A 82 ? 0.2386 0.2762 0.2476 -0.0043 0.0038 0.0021 82 MET A CG 639 S SD . MET A 82 ? 0.2729 0.3106 0.2855 -0.0050 0.0049 0.0003 82 MET A SD 640 C CE . MET A 82 ? 0.2630 0.3059 0.2780 -0.0049 0.0052 -0.0026 82 MET A CE 641 N N . SER A 83 ? 0.1951 0.2349 0.1981 -0.0063 0.0036 0.0058 83 SER A N 642 C CA . SER A 83 ? 0.1949 0.2373 0.1965 -0.0066 0.0036 0.0063 83 SER A CA 643 C C . SER A 83 ? 0.1964 0.2399 0.1990 -0.0079 0.0039 0.0059 83 SER A C 644 O O . SER A 83 ? 0.2259 0.2717 0.2275 -0.0083 0.0039 0.0062 83 SER A O 645 C CB . SER A 83 ? 0.2016 0.2414 0.1996 -0.0065 0.0038 0.0085 83 SER A CB 646 O OG . SER A 83 ? 0.2377 0.2741 0.2345 -0.0080 0.0043 0.0097 83 SER A OG 647 N N . THR A 84 ? 0.1804 0.2224 0.1846 -0.0084 0.0041 0.0054 84 THR A N 648 C CA . THR A 84 ? 0.1659 0.2096 0.1710 -0.0092 0.0043 0.0050 84 THR A CA 649 C C . THR A 84 ? 0.1812 0.2287 0.1884 -0.0086 0.0043 0.0033 84 THR A C 650 O O . THR A 84 ? 0.1893 0.2379 0.1978 -0.0078 0.0043 0.0020 84 THR A O 651 C CB . THR A 84 ? 0.1748 0.2166 0.1811 -0.0092 0.0046 0.0049 84 THR A CB 652 O OG1 . THR A 84 ? 0.1668 0.2079 0.1752 -0.0082 0.0048 0.0038 84 THR A OG1 653 C CG2 . THR A 84 ? 0.1819 0.2202 0.1862 -0.0099 0.0046 0.0064 84 THR A CG2 654 N N . ARG A 85 ? 0.1672 0.2167 0.1748 -0.0092 0.0045 0.0029 85 ARG A N 655 C CA . ARG A 85 ? 0.1719 0.2249 0.1815 -0.0087 0.0047 0.0012 85 ARG A CA 656 C C . ARG A 85 ? 0.1724 0.2247 0.1847 -0.0078 0.0052 -0.0005 85 ARG A C 657 O O . ARG A 85 ? 0.1817 0.2366 0.1955 -0.0074 0.0052 -0.0022 85 ARG A O 658 C CB . ARG A 85 ? 0.1679 0.2226 0.1778 -0.0091 0.0049 0.0011 85 ARG A CB 659 C CG . ARG A 85 ? 0.1691 0.2274 0.1808 -0.0086 0.0051 -0.0006 85 ARG A CG 660 C CD . ARG A 85 ? 0.1734 0.2333 0.1852 -0.0088 0.0054 -0.0005 85 ARG A CD 661 N NE . ARG A 85 ? 0.1839 0.2417 0.1967 -0.0079 0.0060 -0.0006 85 ARG A NE 662 C CZ . ARG A 85 ? 0.1897 0.2480 0.2044 -0.0067 0.0068 -0.0019 85 ARG A CZ 663 N NH1 . ARG A 85 ? 0.2030 0.2637 0.2191 -0.0065 0.0070 -0.0035 85 ARG A NH1 664 N NH2 . ARG A 85 ? 0.1927 0.2490 0.2080 -0.0055 0.0075 -0.0016 85 ARG A NH2 665 N N . LEU A 86 ? 0.1626 0.2118 0.1757 -0.0075 0.0056 -0.0002 86 LEU A N 666 C CA . LEU A 86 ? 0.1541 0.2021 0.1696 -0.0067 0.0065 -0.0017 86 LEU A CA 667 C C . LEU A 86 ? 0.1620 0.2079 0.1776 -0.0066 0.0064 -0.0018 86 LEU A C 668 O O . LEU A 86 ? 0.1891 0.2347 0.2069 -0.0063 0.0072 -0.0034 86 LEU A O 669 C CB . LEU A 86 ? 0.1643 0.2101 0.1804 -0.0061 0.0074 -0.0013 86 LEU A CB 670 C CG . LEU A 86 ? 0.1612 0.2094 0.1774 -0.0059 0.0077 -0.0014 86 LEU A CG 671 C CD1 . LEU A 86 ? 0.1832 0.2294 0.1996 -0.0048 0.0085 -0.0007 86 LEU A CD1 672 C CD2 . LEU A 86 ? 0.1854 0.2359 0.2036 -0.0056 0.0083 -0.0036 86 LEU A CD2 673 N N . GLY A 87 ? 0.1539 0.1987 0.1673 -0.0068 0.0056 -0.0002 87 GLY A N 674 C CA . GLY A 87 ? 0.1701 0.2135 0.1835 -0.0065 0.0054 -0.0003 87 GLY A CA 675 C C . GLY A 87 ? 0.1735 0.2137 0.1882 -0.0062 0.0062 -0.0004 87 GLY A C 676 O O . GLY A 87 ? 0.2063 0.2463 0.2227 -0.0059 0.0067 -0.0018 87 GLY A O 677 N N . ILE A 88 ? 0.1634 0.2013 0.1774 -0.0062 0.0064 0.0009 88 ILE A N 678 C CA . ILE A 88 ? 0.1662 0.2010 0.1812 -0.0057 0.0072 0.0011 88 ILE A CA 679 C C . ILE A 88 ? 0.1579 0.1904 0.1713 -0.0057 0.0065 0.0023 88 ILE A C 680 O O . ILE A 88 ? 0.1480 0.1799 0.1593 -0.0061 0.0059 0.0037 88 ILE A O 681 C CB . ILE A 88 ? 0.1635 0.1975 0.1783 -0.0052 0.0078 0.0019 88 ILE A CB 682 C CG1 . ILE A 88 ? 0.1764 0.2126 0.1926 -0.0050 0.0084 0.0009 88 ILE A CG1 683 C CG2 . ILE A 88 ? 0.1746 0.2055 0.1903 -0.0044 0.0087 0.0023 88 ILE A CG2 684 C CD1 . ILE A 88 ? 0.1784 0.2146 0.1940 -0.0042 0.0089 0.0018 88 ILE A CD1 685 N N . PRO A 89 ? 0.1552 0.1866 0.1696 -0.0053 0.0069 0.0016 89 PRO A N 686 C CA . PRO A 89 ? 0.1479 0.1774 0.1608 -0.0052 0.0062 0.0027 89 PRO A CA 687 C C . PRO A 89 ? 0.1431 0.1697 0.1552 -0.0050 0.0064 0.0041 89 PRO A C 688 O O . PRO A 89 ? 0.1577 0.1836 0.1710 -0.0046 0.0073 0.0039 89 PRO A O 689 C CB . PRO A 89 ? 0.1549 0.1845 0.1697 -0.0048 0.0067 0.0011 89 PRO A CB 690 C CG . PRO A 89 ? 0.1576 0.1872 0.1751 -0.0049 0.0082 -0.0003 89 PRO A CG 691 C CD . PRO A 89 ? 0.1598 0.1918 0.1771 -0.0052 0.0080 -0.0005 89 PRO A CD 692 N N . MET A 90 ? 0.1404 0.1656 0.1503 -0.0053 0.0056 0.0054 90 MET A N 693 C CA . MET A 90 ? 0.1469 0.1698 0.1561 -0.0051 0.0057 0.0064 90 MET A CA 694 C C . MET A 90 ? 0.1443 0.1654 0.1546 -0.0044 0.0061 0.0062 90 MET A C 695 O O . MET A 90 ? 0.1496 0.1710 0.1606 -0.0042 0.0061 0.0053 90 MET A O 696 C CB . MET A 90 ? 0.1534 0.1753 0.1601 -0.0058 0.0050 0.0076 90 MET A CB 697 C CG . MET A 90 ? 0.1476 0.1680 0.1527 -0.0057 0.0045 0.0081 90 MET A CG 698 S SD . MET A 90 ? 0.1623 0.1799 0.1674 -0.0049 0.0045 0.0084 90 MET A SD 699 C CE . MET A 90 ? 0.2101 0.2281 0.2146 -0.0041 0.0040 0.0081 90 MET A CE 700 N N . ILE A 91 ? 0.1424 0.1620 0.1529 -0.0039 0.0066 0.0068 91 ILE A N 701 C CA . ILE A 91 ? 0.1520 0.1696 0.1629 -0.0032 0.0070 0.0069 91 ILE A CA 702 C C . ILE A 91 ? 0.1514 0.1675 0.1603 -0.0034 0.0062 0.0081 91 ILE A C 703 O O . ILE A 91 ? 0.1525 0.1689 0.1602 -0.0037 0.0059 0.0087 91 ILE A O 704 C CB . ILE A 91 ? 0.1498 0.1666 0.1624 -0.0024 0.0084 0.0069 91 ILE A CB 705 C CG1 . ILE A 91 ? 0.1587 0.1735 0.1719 -0.0018 0.0090 0.0069 91 ILE A CG1 706 C CG2 . ILE A 91 ? 0.1549 0.1721 0.1666 -0.0018 0.0085 0.0079 91 ILE A CG2 707 C CD1 . ILE A 91 ? 0.1515 0.1651 0.1664 -0.0008 0.0109 0.0069 91 ILE A CD1 708 N N . TYR A 92 ? 0.1305 0.1451 0.1388 -0.0031 0.0058 0.0082 92 TYR A N 709 C CA . TYR A 92 ? 0.1329 0.1458 0.1391 -0.0033 0.0051 0.0091 92 TYR A CA 710 C C . TYR A 92 ? 0.1390 0.1505 0.1459 -0.0024 0.0055 0.0093 92 TYR A C 711 O O . TYR A 92 ? 0.1539 0.1652 0.1621 -0.0019 0.0060 0.0088 92 TYR A O 712 C CB . TYR A 92 ? 0.1264 0.1386 0.1312 -0.0033 0.0044 0.0092 92 TYR A CB 713 C CG . TYR A 92 ? 0.1333 0.1432 0.1356 -0.0036 0.0040 0.0101 92 TYR A CG 714 C CD1 . TYR A 92 ? 0.1321 0.1401 0.1340 -0.0032 0.0040 0.0104 92 TYR A CD1 715 C CD2 . TYR A 92 ? 0.1458 0.1552 0.1461 -0.0044 0.0038 0.0106 92 TYR A CD2 716 C CE1 . TYR A 92 ? 0.1494 0.1551 0.1491 -0.0036 0.0037 0.0110 92 TYR A CE1 717 C CE2 . TYR A 92 ? 0.1570 0.1638 0.1551 -0.0050 0.0038 0.0113 92 TYR A CE2 718 C CZ . TYR A 92 ? 0.1532 0.1582 0.1510 -0.0046 0.0038 0.0114 92 TYR A CZ 719 O OH . TYR A 92 ? 0.1693 0.1714 0.1649 -0.0053 0.0039 0.0119 92 TYR A OH 720 N N . GLY A 93 ? 0.1410 0.1521 0.1470 -0.0024 0.0055 0.0099 93 GLY A N 721 C CA . GLY A 93 ? 0.1462 0.1564 0.1527 -0.0015 0.0059 0.0103 93 GLY A CA 722 C C . GLY A 93 ? 0.1425 0.1511 0.1473 -0.0016 0.0052 0.0106 93 GLY A C 723 O O . GLY A 93 ? 0.1468 0.1549 0.1499 -0.0026 0.0046 0.0107 93 GLY A O 724 N N . ILE A 94 ? 0.1418 0.1494 0.1470 -0.0007 0.0055 0.0108 94 ILE A N 725 C CA . ILE A 94 ? 0.1375 0.1436 0.1413 -0.0006 0.0049 0.0110 94 ILE A CA 726 C C . ILE A 94 ? 0.1367 0.1428 0.1413 0.0006 0.0054 0.0113 94 ILE A C 727 O O . ILE A 94 ? 0.1388 0.1451 0.1450 0.0013 0.0063 0.0113 94 ILE A O 728 C CB . ILE A 94 ? 0.1427 0.1473 0.1456 -0.0007 0.0044 0.0109 94 ILE A CB 729 C CG1 . ILE A 94 ? 0.1470 0.1495 0.1478 -0.0008 0.0038 0.0111 94 ILE A CG1 730 C CG2 . ILE A 94 ? 0.1537 0.1585 0.1582 0.0003 0.0047 0.0105 94 ILE A CG2 731 C CD1 . ILE A 94 ? 0.1460 0.1468 0.1453 -0.0006 0.0034 0.0112 94 ILE A CD1 732 N N . ASP A 95 ? 0.1356 0.1412 0.1389 0.0007 0.0050 0.0115 95 ASP A N 733 C CA . ASP A 95 ? 0.1401 0.1456 0.1440 0.0019 0.0054 0.0118 95 ASP A CA 734 C C . ASP A 95 ? 0.1434 0.1473 0.1475 0.0023 0.0053 0.0116 95 ASP A C 735 O O . ASP A 95 ? 0.1535 0.1562 0.1563 0.0023 0.0046 0.0115 95 ASP A O 736 C CB . ASP A 95 ? 0.1417 0.1480 0.1444 0.0020 0.0050 0.0117 95 ASP A CB 737 C CG . ASP A 95 ? 0.1526 0.1616 0.1552 0.0017 0.0052 0.0117 95 ASP A CG 738 O OD1 . ASP A 95 ? 0.1642 0.1749 0.1677 0.0031 0.0059 0.0122 95 ASP A OD1 739 O OD2 . ASP A 95 ? 0.1596 0.1688 0.1613 0.0002 0.0047 0.0111 95 ASP A OD2 740 N N . ALA A 96 ? 0.1419 0.1460 0.1476 0.0027 0.0060 0.0115 96 ALA A N 741 C CA . ALA A 96 ? 0.1412 0.1445 0.1475 0.0032 0.0061 0.0111 96 ALA A CA 742 C C . ALA A 96 ? 0.1448 0.1483 0.1522 0.0042 0.0073 0.0116 96 ALA A C 743 O O . ALA A 96 ? 0.1515 0.1552 0.1606 0.0044 0.0087 0.0116 96 ALA A O 744 C CB . ALA A 96 ? 0.1562 0.1601 0.1638 0.0028 0.0064 0.0102 96 ALA A CB 745 N N . VAL A 97 ? 0.1463 0.1496 0.1525 0.0049 0.0069 0.0121 97 VAL A N 746 C CA . VAL A 97 ? 0.1473 0.1511 0.1540 0.0061 0.0079 0.0128 97 VAL A CA 747 C C . VAL A 97 ? 0.1496 0.1528 0.1565 0.0068 0.0081 0.0128 97 VAL A C 748 O O . VAL A 97 ? 0.1636 0.1671 0.1710 0.0079 0.0092 0.0135 97 VAL A O 749 C CB . VAL A 97 ? 0.1485 0.1538 0.1540 0.0066 0.0076 0.0134 97 VAL A CB 750 C CG1 . VAL A 97 ? 0.1554 0.1618 0.1610 0.0062 0.0078 0.0135 97 VAL A CG1 751 C CG2 . VAL A 97 ? 0.1558 0.1608 0.1596 0.0060 0.0061 0.0128 97 VAL A CG2 752 N N . HIS A 98 ? 0.1456 0.1481 0.1519 0.0064 0.0070 0.0121 98 HIS A N 753 C CA . HIS A 98 ? 0.1393 0.1416 0.1461 0.0070 0.0072 0.0118 98 HIS A CA 754 C C . HIS A 98 ? 0.1369 0.1391 0.1435 0.0066 0.0064 0.0108 98 HIS A C 755 O O . HIS A 98 ? 0.1432 0.1447 0.1483 0.0070 0.0053 0.0106 98 HIS A O 756 C CB . HIS A 98 ? 0.1354 0.1378 0.1410 0.0080 0.0068 0.0122 98 HIS A CB 757 C CG . HIS A 98 ? 0.1475 0.1492 0.1511 0.0077 0.0053 0.0119 98 HIS A CG 758 N ND1 . HIS A 98 ? 0.1554 0.1566 0.1579 0.0084 0.0047 0.0117 98 HIS A ND1 759 C CD2 . HIS A 98 ? 0.1418 0.1429 0.1442 0.0068 0.0046 0.0117 98 HIS A CD2 760 C CE1 . HIS A 98 ? 0.1609 0.1610 0.1617 0.0079 0.0038 0.0113 98 HIS A CE1 761 N NE2 . HIS A 98 ? 0.1533 0.1534 0.1540 0.0068 0.0038 0.0114 98 HIS A NE2 762 N N . GLY A 99 ? 0.1370 0.1398 0.1450 0.0059 0.0069 0.0102 99 GLY A N 763 C CA . GLY A 99 ? 0.1431 0.1464 0.1507 0.0055 0.0060 0.0093 99 GLY A CA 764 C C . GLY A 99 ? 0.1450 0.1477 0.1512 0.0049 0.0053 0.0098 99 GLY A C 765 O O . GLY A 99 ? 0.1504 0.1526 0.1563 0.0046 0.0055 0.0104 99 GLY A O 766 N N . GLN A 100 ? 0.1386 0.1416 0.1439 0.0048 0.0045 0.0093 100 GLN A N 767 C CA . GLN A 100 ? 0.1417 0.1441 0.1457 0.0041 0.0040 0.0097 100 GLN A CA 768 C C . GLN A 100 ? 0.1389 0.1389 0.1402 0.0044 0.0032 0.0104 100 GLN A C 769 O O . GLN A 100 ? 0.1504 0.1492 0.1498 0.0048 0.0026 0.0106 100 GLN A O 770 C CB . GLN A 100 ? 0.1362 0.1402 0.1404 0.0042 0.0037 0.0089 100 GLN A CB 771 C CG . GLN A 100 ? 0.1461 0.1496 0.1486 0.0038 0.0031 0.0094 100 GLN A CG 772 C CD . GLN A 100 ? 0.1500 0.1532 0.1527 0.0026 0.0035 0.0098 100 GLN A CD 773 O OE1 . GLN A 100 ? 0.1763 0.1803 0.1788 0.0021 0.0034 0.0097 100 GLN A OE1 774 N NE2 . GLN A 100 ? 0.1217 0.1242 0.1249 0.0023 0.0039 0.0102 100 GLN A NE2 775 N N . ASN A 101 ? 0.1371 0.1365 0.1384 0.0042 0.0034 0.0108 101 ASN A N 776 C CA . ASN A 101 ? 0.1316 0.1291 0.1309 0.0045 0.0029 0.0110 101 ASN A CA 777 C C . ASN A 101 ? 0.1445 0.1398 0.1415 0.0037 0.0026 0.0112 101 ASN A C 778 O O . ASN A 101 ? 0.1513 0.1445 0.1466 0.0040 0.0024 0.0112 101 ASN A O 779 C CB . ASN A 101 ? 0.1391 0.1373 0.1391 0.0047 0.0033 0.0111 101 ASN A CB 780 C CG . ASN A 101 ? 0.1459 0.1456 0.1468 0.0040 0.0038 0.0113 101 ASN A CG 781 O OD1 . ASN A 101 ? 0.1849 0.1844 0.1847 0.0030 0.0035 0.0112 101 ASN A OD1 782 N ND2 . ASN A 101 ? 0.1197 0.1209 0.1225 0.0044 0.0046 0.0115 101 ASN A ND2 783 N N . ASN A 102 ? 0.1492 0.1447 0.1461 0.0027 0.0027 0.0113 102 ASN A N 784 C CA . ASN A 102 ? 0.1527 0.1459 0.1473 0.0018 0.0027 0.0115 102 ASN A CA 785 C C . ASN A 102 ? 0.1585 0.1497 0.1512 0.0028 0.0025 0.0120 102 ASN A C 786 O O . ASN A 102 ? 0.1741 0.1624 0.1645 0.0024 0.0028 0.0123 102 ASN A O 787 C CB . ASN A 102 ? 0.1574 0.1516 0.1523 0.0004 0.0029 0.0115 102 ASN A CB 788 C CG . ASN A 102 ? 0.1673 0.1633 0.1633 -0.0006 0.0032 0.0111 102 ASN A CG 789 O OD1 . ASN A 102 ? 0.1826 0.1812 0.1803 -0.0006 0.0033 0.0111 102 ASN A OD1 790 N ND2 . ASN A 102 ? 0.1413 0.1364 0.1363 -0.0012 0.0032 0.0107 102 ASN A ND2 791 N N . VAL A 103 ? 0.1527 0.1457 0.1464 0.0041 0.0022 0.0118 103 VAL A N 792 C CA . VAL A 103 ? 0.1583 0.1509 0.1505 0.0053 0.0020 0.0122 103 VAL A CA 793 C C . VAL A 103 ? 0.1600 0.1513 0.1507 0.0071 0.0018 0.0123 103 VAL A C 794 O O . VAL A 103 ? 0.1687 0.1614 0.1609 0.0077 0.0016 0.0117 103 VAL A O 795 C CB . VAL A 103 ? 0.1584 0.1548 0.1527 0.0056 0.0019 0.0116 103 VAL A CB 796 C CG1 . VAL A 103 ? 0.1727 0.1698 0.1654 0.0072 0.0016 0.0118 103 VAL A CG1 797 C CG2 . VAL A 103 ? 0.1770 0.1744 0.1724 0.0039 0.0022 0.0115 103 VAL A CG2 798 N N . TYR A 104 ? 0.1673 0.1555 0.1550 0.0080 0.0020 0.0131 104 TYR A N 799 C CA . TYR A 104 ? 0.1795 0.1663 0.1654 0.0101 0.0018 0.0134 104 TYR A CA 800 C C . TYR A 104 ? 0.1770 0.1680 0.1643 0.0118 0.0012 0.0128 104 TYR A C 801 O O . TYR A 104 ? 0.1873 0.1810 0.1751 0.0121 0.0010 0.0126 104 TYR A O 802 C CB . TYR A 104 ? 0.1968 0.1793 0.1789 0.0110 0.0024 0.0146 104 TYR A CB 803 C CG . TYR A 104 ? 0.2231 0.2035 0.2028 0.0135 0.0024 0.0150 104 TYR A CG 804 C CD1 . TYR A 104 ? 0.2496 0.2264 0.2283 0.0133 0.0028 0.0149 104 TYR A CD1 805 C CD2 . TYR A 104 ? 0.2465 0.2293 0.2255 0.0160 0.0020 0.0153 104 TYR A CD2 806 C CE1 . TYR A 104 ? 0.2675 0.2426 0.2440 0.0159 0.0027 0.0153 104 TYR A CE1 807 C CE2 . TYR A 104 ? 0.3006 0.2823 0.2774 0.0187 0.0019 0.0157 104 TYR A CE2 808 C CZ . TYR A 104 ? 0.2883 0.2660 0.2640 0.0186 0.0023 0.0157 104 TYR A CZ 809 O OH . TYR A 104 ? 0.3673 0.3440 0.3407 0.0216 0.0022 0.0161 104 TYR A OH 810 N N . GLY A 105 ? 0.1676 0.1596 0.1556 0.0129 0.0009 0.0122 105 GLY A N 811 C CA . GLY A 105 ? 0.1671 0.1636 0.1566 0.0143 0.0004 0.0112 105 GLY A CA 812 C C . GLY A 105 ? 0.1675 0.1678 0.1607 0.0128 0.0005 0.0100 105 GLY A C 813 O O . GLY A 105 ? 0.1804 0.1847 0.1753 0.0136 0.0004 0.0088 105 GLY A O 814 N N . ALA A 106 ? 0.1606 0.1600 0.1553 0.0108 0.0009 0.0101 106 ALA A N 815 C CA . ALA A 106 ? 0.1448 0.1469 0.1429 0.0096 0.0014 0.0091 106 ALA A CA 816 C C . ALA A 106 ? 0.1491 0.1514 0.1483 0.0100 0.0016 0.0087 106 ALA A C 817 O O . ALA A 106 ? 0.1624 0.1623 0.1602 0.0103 0.0014 0.0094 106 ALA A O 818 C CB . ALA A 106 ? 0.1472 0.1483 0.1462 0.0078 0.0019 0.0095 106 ALA A CB 819 N N . THR A 107 ? 0.1469 0.1524 0.1488 0.0097 0.0022 0.0075 107 THR A N 820 C CA . THR A 107 ? 0.1384 0.1442 0.1417 0.0098 0.0027 0.0073 107 THR A CA 821 C C . THR A 107 ? 0.1333 0.1368 0.1367 0.0089 0.0032 0.0083 107 THR A C 822 O O . THR A 107 ? 0.1495 0.1529 0.1538 0.0078 0.0037 0.0085 107 THR A O 823 C CB . THR A 107 ? 0.1464 0.1556 0.1529 0.0091 0.0037 0.0058 107 THR A CB 824 O OG1 . THR A 107 ? 0.1482 0.1605 0.1548 0.0098 0.0032 0.0046 107 THR A OG1 825 C CG2 . THR A 107 ? 0.1512 0.1607 0.1589 0.0093 0.0044 0.0056 107 THR A CG2 826 N N . ILE A 108 ? 0.1432 0.1453 0.1456 0.0095 0.0030 0.0087 108 ILE A N 827 C CA . ILE A 108 ? 0.1447 0.1456 0.1472 0.0090 0.0034 0.0095 108 ILE A CA 828 C C . ILE A 108 ? 0.1487 0.1510 0.1531 0.0093 0.0043 0.0094 108 ILE A C 829 O O . ILE A 108 ? 0.1503 0.1530 0.1544 0.0102 0.0041 0.0091 108 ILE A O 830 C CB . ILE A 108 ? 0.1390 0.1376 0.1391 0.0093 0.0026 0.0100 108 ILE A CB 831 C CG1 . ILE A 108 ? 0.1565 0.1531 0.1545 0.0090 0.0020 0.0102 108 ILE A CG1 832 C CG2 . ILE A 108 ? 0.1441 0.1426 0.1445 0.0088 0.0030 0.0105 108 ILE A CG2 833 C CD1 . ILE A 108 ? 0.1531 0.1500 0.1517 0.0076 0.0023 0.0105 108 ILE A CD1 834 N N . PHE A 109 ? 0.1407 0.1435 0.1469 0.0086 0.0055 0.0097 109 PHE A N 835 C CA . PHE A 109 ? 0.1282 0.1318 0.1361 0.0089 0.0069 0.0098 109 PHE A CA 836 C C . PHE A 109 ? 0.1485 0.1515 0.1553 0.0096 0.0069 0.0109 109 PHE A C 837 O O . PHE A 109 ? 0.1539 0.1562 0.1592 0.0095 0.0061 0.0113 109 PHE A O 838 C CB . PHE A 109 ? 0.1426 0.1465 0.1525 0.0080 0.0086 0.0097 109 PHE A CB 839 C CG . PHE A 109 ? 0.1446 0.1499 0.1560 0.0071 0.0088 0.0082 109 PHE A CG 840 C CD1 . PHE A 109 ? 0.1505 0.1574 0.1637 0.0070 0.0097 0.0070 109 PHE A CD1 841 C CD2 . PHE A 109 ? 0.1519 0.1575 0.1630 0.0065 0.0080 0.0078 109 PHE A CD2 842 C CE1 . PHE A 109 ? 0.1482 0.1573 0.1629 0.0062 0.0099 0.0053 109 PHE A CE1 843 C CE2 . PHE A 109 ? 0.1553 0.1630 0.1677 0.0059 0.0081 0.0063 109 PHE A CE2 844 C CZ . PHE A 109 ? 0.1554 0.1650 0.1696 0.0058 0.0090 0.0049 109 PHE A CZ 845 N N . PRO A 110 ? 0.1405 0.1441 0.1481 0.0104 0.0080 0.0112 110 PRO A N 846 C CA . PRO A 110 ? 0.1414 0.1451 0.1481 0.0113 0.0081 0.0123 110 PRO A CA 847 C C . PRO A 110 ? 0.1410 0.1447 0.1477 0.0111 0.0087 0.0131 110 PRO A C 848 O O . PRO A 110 ? 0.1470 0.1504 0.1549 0.0106 0.0098 0.0132 110 PRO A O 849 C CB . PRO A 110 ? 0.1456 0.1499 0.1536 0.0120 0.0098 0.0126 110 PRO A CB 850 C CG . PRO A 110 ? 0.1425 0.1474 0.1516 0.0114 0.0097 0.0113 110 PRO A CG 851 C CD . PRO A 110 ? 0.1462 0.1508 0.1556 0.0103 0.0091 0.0105 110 PRO A CD 852 N N . HIS A 111 ? 0.1406 0.1449 0.1458 0.0117 0.0080 0.0136 111 HIS A N 853 C CA . HIS A 111 ? 0.1483 0.1535 0.1534 0.0120 0.0086 0.0144 111 HIS A CA 854 C C . HIS A 111 ? 0.1544 0.1600 0.1605 0.0132 0.0107 0.0157 111 HIS A C 855 O O . HIS A 111 ? 0.1543 0.1596 0.1610 0.0139 0.0117 0.0160 111 HIS A O 856 C CB . HIS A 111 ? 0.1497 0.1563 0.1532 0.0123 0.0075 0.0142 111 HIS A CB 857 C CG . HIS A 111 ? 0.1475 0.1535 0.1501 0.0108 0.0061 0.0133 111 HIS A CG 858 N ND1 . HIS A 111 ? 0.1532 0.1591 0.1561 0.0100 0.0063 0.0134 111 HIS A ND1 859 C CD2 . HIS A 111 ? 0.1545 0.1596 0.1558 0.0101 0.0049 0.0123 111 HIS A CD2 860 C CE1 . HIS A 111 ? 0.1531 0.1583 0.1550 0.0087 0.0052 0.0125 111 HIS A CE1 861 N NE2 . HIS A 111 ? 0.1513 0.1558 0.1521 0.0087 0.0044 0.0118 111 HIS A NE2 862 N N . ASN A 112 ? 0.1526 0.1587 0.1588 0.0136 0.0115 0.0165 112 ASN A N 863 C CA . ASN A 112 ? 0.1494 0.1549 0.1563 0.0148 0.0139 0.0179 112 ASN A CA 864 C C . ASN A 112 ? 0.1515 0.1581 0.1579 0.0168 0.0149 0.0191 112 ASN A C 865 O O . ASN A 112 ? 0.1619 0.1670 0.1692 0.0174 0.0170 0.0199 112 ASN A O 866 C CB . ASN A 112 ? 0.1561 0.1624 0.1627 0.0155 0.0145 0.0187 112 ASN A CB 867 C CG . ASN A 112 ? 0.1662 0.1711 0.1737 0.0138 0.0144 0.0179 112 ASN A CG 868 O OD1 . ASN A 112 ? 0.2147 0.2203 0.2219 0.0142 0.0147 0.0184 112 ASN A OD1 869 N ND2 . ASN A 112 ? 0.1373 0.1408 0.1460 0.0122 0.0141 0.0167 112 ASN A ND2 870 N N . VAL A 113 ? 0.1594 0.1684 0.1644 0.0178 0.0135 0.0190 113 VAL A N 871 C CA . VAL A 113 ? 0.1713 0.1817 0.1756 0.0199 0.0145 0.0202 113 VAL A CA 872 C C . VAL A 113 ? 0.1721 0.1808 0.1774 0.0195 0.0153 0.0200 113 VAL A C 873 O O . VAL A 113 ? 0.1735 0.1816 0.1792 0.0207 0.0175 0.0213 113 VAL A O 874 C CB . VAL A 113 ? 0.1623 0.1763 0.1651 0.0208 0.0128 0.0197 113 VAL A CB 875 C CG1 . VAL A 113 ? 0.1895 0.2031 0.1920 0.0191 0.0106 0.0178 113 VAL A CG1 876 C CG2 . VAL A 113 ? 0.1808 0.1968 0.1828 0.0233 0.0140 0.0211 113 VAL A CG2 877 N N . GLY A 114 ? 0.1669 0.1749 0.1726 0.0178 0.0137 0.0183 114 GLY A N 878 C CA . GLY A 114 ? 0.1714 0.1784 0.1782 0.0173 0.0143 0.0178 114 GLY A CA 879 C C . GLY A 114 ? 0.1621 0.1670 0.1707 0.0164 0.0165 0.0180 114 GLY A C 880 O O . GLY A 114 ? 0.1613 0.1657 0.1710 0.0166 0.0183 0.0183 114 GLY A O 881 N N . LEU A 115 ? 0.1654 0.1692 0.1747 0.0153 0.0166 0.0176 115 LEU A N 882 C CA . LEU A 115 ? 0.1569 0.1589 0.1680 0.0144 0.0190 0.0176 115 LEU A CA 883 C C . LEU A 115 ? 0.1691 0.1700 0.1802 0.0161 0.0220 0.0196 115 LEU A C 884 O O . LEU A 115 ? 0.1671 0.1663 0.1796 0.0156 0.0244 0.0196 115 LEU A O 885 C CB . LEU A 115 ? 0.1649 0.1661 0.1766 0.0131 0.0187 0.0169 115 LEU A CB 886 C CG . LEU A 115 ? 0.1579 0.1599 0.1696 0.0116 0.0162 0.0151 115 LEU A CG 887 C CD1 . LEU A 115 ? 0.1649 0.1664 0.1772 0.0105 0.0161 0.0145 115 LEU A CD1 888 C CD2 . LEU A 115 ? 0.1668 0.1692 0.1798 0.0107 0.0163 0.0136 115 LEU A CD2 889 N N . GLY A 116 ? 0.1683 0.1703 0.1776 0.0181 0.0218 0.0213 116 GLY A N 890 C CA . GLY A 116 ? 0.1713 0.1726 0.1800 0.0204 0.0246 0.0235 116 GLY A CA 891 C C . GLY A 116 ? 0.1855 0.1868 0.1944 0.0209 0.0258 0.0239 116 GLY A C 892 O O . GLY A 116 ? 0.1931 0.1922 0.2025 0.0216 0.0290 0.0253 116 GLY A O 893 N N . ALA A 117 ? 0.1785 0.1819 0.1870 0.0207 0.0234 0.0228 117 ALA A N 894 C CA . ALA A 117 ? 0.1732 0.1772 0.1819 0.0211 0.0242 0.0230 117 ALA A CA 895 C C . ALA A 117 ? 0.1794 0.1812 0.1903 0.0192 0.0262 0.0220 117 ALA A C 896 O O . ALA A 117 ? 0.1974 0.1989 0.2087 0.0197 0.0281 0.0226 117 ALA A O 897 C CB . ALA A 117 ? 0.1732 0.1798 0.1810 0.0211 0.0210 0.0217 117 ALA A CB 898 N N . THR A 118 ? 0.1746 0.1753 0.1871 0.0171 0.0259 0.0203 118 THR A N 899 C CA . THR A 118 ? 0.1801 0.1797 0.1950 0.0150 0.0277 0.0188 118 THR A CA 900 C C . THR A 118 ? 0.2001 0.1965 0.2161 0.0150 0.0319 0.0200 118 THR A C 901 O O . THR A 118 ? 0.2132 0.2086 0.2311 0.0134 0.0342 0.0189 118 THR A O 902 C CB . THR A 118 ? 0.1770 0.1768 0.1934 0.0127 0.0262 0.0165 118 THR A CB 903 O OG1 . THR A 118 ? 0.1843 0.1821 0.2009 0.0124 0.0274 0.0169 118 THR A OG1 904 C CG2 . THR A 118 ? 0.1770 0.1791 0.1920 0.0128 0.0224 0.0154 118 THR A CG2 905 N N . ARG A 119 ? 0.2066 0.2014 0.2213 0.0166 0.0330 0.0220 119 ARG A N 906 C CA . ARG A 119 ? 0.2113 0.2023 0.2266 0.0168 0.0371 0.0233 119 ARG A CA 907 C C . ARG A 119 ? 0.2167 0.2059 0.2349 0.0136 0.0387 0.0208 119 ARG A C 908 O O . ARG A 119 ? 0.2430 0.2292 0.2626 0.0129 0.0426 0.0210 119 ARG A O 909 C CB . ARG A 119 ? 0.2210 0.2107 0.2357 0.0183 0.0401 0.0253 119 ARG A CB 910 C CG . ARG A 119 ? 0.2391 0.2311 0.2511 0.0216 0.0389 0.0276 119 ARG A CG 911 C CD . ARG A 119 ? 0.2429 0.2347 0.2528 0.0241 0.0389 0.0297 119 ARG A CD 912 N NE . ARG A 119 ? 0.2752 0.2690 0.2826 0.0276 0.0392 0.0322 119 ARG A NE 913 C CZ . ARG A 119 ? 0.2600 0.2582 0.2660 0.0287 0.0360 0.0319 119 ARG A CZ 914 N NH1 . ARG A 119 ? 0.2166 0.2171 0.2232 0.0268 0.0323 0.0295 119 ARG A NH1 915 N NH2 . ARG A 119 ? 0.2657 0.2658 0.2696 0.0320 0.0367 0.0342 119 ARG A NH2 916 N N . ASP A 120 ? 0.2048 0.1960 0.2240 0.0118 0.0359 0.0185 120 ASP A N 917 C CA . ASP A 120 ? 0.2099 0.2008 0.2319 0.0089 0.0368 0.0157 120 ASP A CA 918 C C . ASP A 120 ? 0.1995 0.1899 0.2217 0.0082 0.0360 0.0150 120 ASP A C 919 O O . ASP A 120 ? 0.2019 0.1949 0.2240 0.0075 0.0327 0.0136 120 ASP A O 920 C CB . ASP A 120 ? 0.2233 0.2179 0.2463 0.0075 0.0344 0.0133 120 ASP A CB 921 C CG . ASP A 120 ? 0.2287 0.2240 0.2548 0.0046 0.0358 0.0102 120 ASP A CG 922 O OD1 . ASP A 120 ? 0.2769 0.2702 0.3045 0.0033 0.0379 0.0094 120 ASP A OD1 923 O OD2 . ASP A 120 ? 0.2935 0.2918 0.3205 0.0038 0.0346 0.0084 120 ASP A OD2 924 N N . PRO A 121 ? 0.2089 0.1959 0.2314 0.0085 0.0390 0.0160 121 PRO A N 925 C CA . PRO A 121 ? 0.2007 0.1873 0.2235 0.0078 0.0382 0.0153 121 PRO A CA 926 C C . PRO A 121 ? 0.2101 0.1984 0.2355 0.0048 0.0375 0.0118 121 PRO A C 927 O O . PRO A 121 ? 0.2133 0.2032 0.2385 0.0044 0.0352 0.0110 121 PRO A O 928 C CB . PRO A 121 ? 0.2211 0.2032 0.2438 0.0088 0.0423 0.0170 121 PRO A CB 929 C CG . PRO A 121 ? 0.2340 0.2147 0.2549 0.0112 0.0441 0.0198 121 PRO A CG 930 C CD . PRO A 121 ? 0.2141 0.1970 0.2362 0.0098 0.0432 0.0182 121 PRO A CD 931 N N . TYR A 122 ? 0.2109 0.1998 0.2387 0.0028 0.0391 0.0096 122 TYR A N 932 C CA . TYR A 122 ? 0.1959 0.1876 0.2262 0.0001 0.0382 0.0061 122 TYR A CA 933 C C . TYR A 122 ? 0.1974 0.1935 0.2267 0.0004 0.0339 0.0052 122 TYR A C 934 O O . TYR A 122 ? 0.1914 0.1899 0.2213 -0.0006 0.0320 0.0033 122 TYR A O 935 C CB . TYR A 122 ? 0.2381 0.2298 0.2715 -0.0023 0.0415 0.0036 122 TYR A CB 936 C CG . TYR A 122 ? 0.2600 0.2555 0.2961 -0.0049 0.0407 -0.0004 122 TYR A CG 937 C CD1 . TYR A 122 ? 0.3018 0.2973 0.3387 -0.0058 0.0405 -0.0016 122 TYR A CD1 938 C CD2 . TYR A 122 ? 0.2874 0.2872 0.3251 -0.0063 0.0399 -0.0030 122 TYR A CD2 939 C CE1 . TYR A 122 ? 0.3174 0.3170 0.3565 -0.0079 0.0395 -0.0053 122 TYR A CE1 940 C CE2 . TYR A 122 ? 0.3032 0.3074 0.3433 -0.0083 0.0390 -0.0067 122 TYR A CE2 941 C CZ . TYR A 122 ? 0.3274 0.3316 0.3682 -0.0091 0.0389 -0.0078 122 TYR A CZ 942 O OH . TYR A 122 ? 0.4090 0.4180 0.4519 -0.0109 0.0379 -0.0115 122 TYR A OH 943 N N . LEU A 123 ? 0.1774 0.1744 0.2050 0.0019 0.0324 0.0065 123 LEU A N 944 C CA . LEU A 123 ? 0.1674 0.1677 0.1934 0.0026 0.0283 0.0062 123 LEU A CA 945 C C . LEU A 123 ? 0.1706 0.1705 0.1948 0.0035 0.0262 0.0073 123 LEU A C 946 O O . LEU A 123 ? 0.1680 0.1702 0.1920 0.0030 0.0237 0.0060 123 LEU A O 947 C CB . LEU A 123 ? 0.1840 0.1846 0.2083 0.0043 0.0276 0.0079 123 LEU A CB 948 C CG . LEU A 123 ? 0.1940 0.1969 0.2162 0.0055 0.0237 0.0080 123 LEU A CG 949 C CD1 . LEU A 123 ? 0.2021 0.2084 0.2255 0.0044 0.0223 0.0054 123 LEU A CD1 950 C CD2 . LEU A 123 ? 0.2330 0.2355 0.2532 0.0074 0.0231 0.0101 123 LEU A CD2 951 N N . VAL A 124 ? 0.1704 0.1678 0.1932 0.0049 0.0272 0.0097 124 VAL A N 952 C CA . VAL A 124 ? 0.1754 0.1727 0.1965 0.0057 0.0253 0.0107 124 VAL A CA 953 C C . VAL A 124 ? 0.1772 0.1746 0.1999 0.0041 0.0256 0.0090 124 VAL A C 954 O O . VAL A 124 ? 0.1711 0.1701 0.1930 0.0039 0.0232 0.0085 124 VAL A O 955 C CB . VAL A 124 ? 0.1877 0.1831 0.2070 0.0079 0.0263 0.0135 124 VAL A CB 956 C CG1 . VAL A 124 ? 0.1781 0.1738 0.1960 0.0084 0.0246 0.0142 124 VAL A CG1 957 C CG2 . VAL A 124 ? 0.2003 0.1966 0.2179 0.0095 0.0252 0.0148 124 VAL A CG2 958 N N . LYS A 125 ? 0.1780 0.1738 0.2030 0.0028 0.0287 0.0079 125 LYS A N 959 C CA . LYS A 125 ? 0.1739 0.1703 0.2007 0.0011 0.0291 0.0058 125 LYS A CA 960 C C . LYS A 125 ? 0.1759 0.1765 0.2034 -0.0001 0.0264 0.0033 125 LYS A C 961 O O . LYS A 125 ? 0.1628 0.1647 0.1900 -0.0005 0.0248 0.0026 125 LYS A O 962 C CB . LYS A 125 ? 0.1899 0.1840 0.2194 -0.0004 0.0332 0.0045 125 LYS A CB 963 C CG . LYS A 125 ? 0.1902 0.1847 0.2215 -0.0021 0.0338 0.0024 125 LYS A CG 964 C CD . LYS A 125 ? 0.2329 0.2248 0.2670 -0.0039 0.0381 0.0007 125 LYS A CD 965 C CE . LYS A 125 ? 0.2408 0.2335 0.2767 -0.0055 0.0386 -0.0016 125 LYS A CE 966 N NZ . LYS A 125 ? 0.2812 0.2715 0.3201 -0.0077 0.0430 -0.0039 125 LYS A NZ 967 N N . ARG A 126 ? 0.1734 0.1759 0.2016 -0.0005 0.0262 0.0022 126 ARG A N 968 C CA . ARG A 126 ? 0.1677 0.1744 0.1964 -0.0012 0.0239 0.0000 126 ARG A CA 969 C C . ARG A 126 ? 0.1541 0.1616 0.1798 0.0003 0.0205 0.0014 126 ARG A C 970 O O . ARG A 126 ? 0.1656 0.1755 0.1911 0.0000 0.0187 0.0002 126 ARG A O 971 C CB . ARG A 126 ? 0.1875 0.1962 0.2173 -0.0016 0.0245 -0.0014 126 ARG A CB 972 C CG . ARG A 126 ? 0.2199 0.2283 0.2530 -0.0037 0.0281 -0.0035 126 ARG A CG 973 C CD . ARG A 126 ? 0.3541 0.3618 0.3879 -0.0037 0.0300 -0.0032 126 ARG A CD 974 N NE . ARG A 126 ? 0.3618 0.3735 0.3951 -0.0032 0.0276 -0.0041 126 ARG A NE 975 C CZ . ARG A 126 ? 0.2903 0.3024 0.3225 -0.0021 0.0271 -0.0031 126 ARG A CZ 976 N NH1 . ARG A 126 ? 0.2712 0.2802 0.3028 -0.0013 0.0289 -0.0011 126 ARG A NH1 977 N NH2 . ARG A 126 ? 0.2961 0.3122 0.3277 -0.0015 0.0246 -0.0044 126 ARG A NH2 978 N N . ILE A 127 ? 0.1605 0.1658 0.1839 0.0019 0.0198 0.0039 127 ILE A N 979 C CA . ILE A 127 ? 0.1595 0.1651 0.1802 0.0031 0.0169 0.0052 127 ILE A CA 980 C C . ILE A 127 ? 0.1586 0.1637 0.1789 0.0027 0.0165 0.0054 127 ILE A C 981 O O . ILE A 127 ? 0.1627 0.1692 0.1819 0.0027 0.0144 0.0050 127 ILE A O 982 C CB . ILE A 127 ? 0.1594 0.1633 0.1781 0.0046 0.0166 0.0075 127 ILE A CB 983 C CG1 . ILE A 127 ? 0.1621 0.1670 0.1808 0.0051 0.0163 0.0071 127 ILE A CG1 984 C CG2 . ILE A 127 ? 0.1632 0.1670 0.1794 0.0054 0.0141 0.0085 127 ILE A CG2 985 C CD1 . ILE A 127 ? 0.1647 0.1684 0.1818 0.0066 0.0163 0.0091 127 ILE A CD1 986 N N . GLY A 128 ? 0.1514 0.1546 0.1728 0.0024 0.0186 0.0059 128 GLY A N 987 C CA . GLY A 128 ? 0.1471 0.1502 0.1684 0.0019 0.0184 0.0058 128 GLY A CA 988 C C . GLY A 128 ? 0.1491 0.1548 0.1719 0.0006 0.0178 0.0034 128 GLY A C 989 O O . GLY A 128 ? 0.1597 0.1666 0.1815 0.0005 0.0160 0.0033 128 GLY A O 990 N N . GLU A 129 ? 0.1591 0.1660 0.1843 -0.0006 0.0193 0.0013 129 GLU A N 991 C CA . GLU A 129 ? 0.1583 0.1687 0.1852 -0.0018 0.0188 -0.0014 129 GLU A CA 992 C C . GLU A 129 ? 0.1545 0.1677 0.1794 -0.0010 0.0158 -0.0015 129 GLU A C 993 O O . GLU A 129 ? 0.1696 0.1848 0.1941 -0.0011 0.0145 -0.0022 129 GLU A O 994 C CB . GLU A 129 ? 0.1776 0.1895 0.2075 -0.0033 0.0211 -0.0039 129 GLU A CB 995 C CG . GLU A 129 ? 0.2144 0.2228 0.2462 -0.0042 0.0246 -0.0038 129 GLU A CG 996 C CD . GLU A 129 ? 0.2827 0.2916 0.3175 -0.0060 0.0275 -0.0063 129 GLU A CD 997 O OE1 . GLU A 129 ? 0.2696 0.2758 0.3063 -0.0071 0.0306 -0.0068 129 GLU A OE1 998 O OE2 . GLU A 129 ? 0.2967 0.3086 0.3322 -0.0062 0.0269 -0.0076 129 GLU A OE2 999 N N . ALA A 130 ? 0.1499 0.1630 0.1734 0.0001 0.0148 -0.0006 130 ALA A N 1000 C CA . ALA A 130 ? 0.1516 0.1666 0.1730 0.0012 0.0123 -0.0005 130 ALA A CA 1001 C C . ALA A 130 ? 0.1475 0.1607 0.1662 0.0020 0.0106 0.0015 130 ALA A C 1002 O O . ALA A 130 ? 0.1458 0.1606 0.1631 0.0024 0.0090 0.0012 130 ALA A O 1003 C CB . ALA A 130 ? 0.1762 0.1910 0.1966 0.0023 0.0118 0.0002 130 ALA A CB 1004 N N . THR A 131 ? 0.1493 0.1594 0.1672 0.0022 0.0112 0.0033 131 THR A N 1005 C CA . THR A 131 ? 0.1474 0.1561 0.1630 0.0026 0.0098 0.0049 131 THR A CA 1006 C C . THR A 131 ? 0.1520 0.1617 0.1680 0.0018 0.0097 0.0042 131 THR A C 1007 O O . THR A 131 ? 0.1560 0.1661 0.1702 0.0021 0.0082 0.0047 131 THR A O 1008 C CB . THR A 131 ? 0.1411 0.1473 0.1560 0.0031 0.0106 0.0067 131 THR A CB 1009 O OG1 . THR A 131 ? 0.1454 0.1509 0.1596 0.0039 0.0104 0.0073 131 THR A OG1 1010 C CG2 . THR A 131 ? 0.1612 0.1664 0.1740 0.0033 0.0093 0.0080 131 THR A CG2 1011 N N . ALA A 132 ? 0.1571 0.1674 0.1757 0.0009 0.0115 0.0031 132 ALA A N 1012 C CA . ALA A 132 ? 0.1539 0.1655 0.1730 0.0001 0.0114 0.0021 132 ALA A CA 1013 C C . ALA A 132 ? 0.1458 0.1607 0.1646 0.0002 0.0099 0.0008 132 ALA A C 1014 O O . ALA A 132 ? 0.1469 0.1626 0.1644 0.0002 0.0088 0.0011 132 ALA A O 1015 C CB . ALA A 132 ? 0.1643 0.1759 0.1864 -0.0010 0.0138 0.0007 132 ALA A CB 1016 N N . LEU A 133 ? 0.1542 0.1713 0.1739 0.0003 0.0099 -0.0006 133 LEU A N 1017 C CA . LEU A 133 ? 0.1499 0.1708 0.1690 0.0009 0.0086 -0.0019 133 LEU A CA 1018 C C . LEU A 133 ? 0.1520 0.1716 0.1675 0.0024 0.0066 0.0001 133 LEU A C 1019 O O . LEU A 133 ? 0.1503 0.1716 0.1644 0.0029 0.0056 0.0000 133 LEU A O 1020 C CB . LEU A 133 ? 0.1516 0.1755 0.1723 0.0010 0.0090 -0.0039 133 LEU A CB 1021 C CG . LEU A 133 ? 0.1554 0.1812 0.1799 -0.0008 0.0111 -0.0064 133 LEU A CG 1022 C CD1 . LEU A 133 ? 0.1753 0.2041 0.2012 -0.0008 0.0115 -0.0083 133 LEU A CD1 1023 C CD2 . LEU A 133 ? 0.1823 0.2119 0.2080 -0.0015 0.0111 -0.0085 133 LEU A CD2 1024 N N . GLU A 134 ? 0.1440 0.1605 0.1578 0.0030 0.0063 0.0018 134 GLU A N 1025 C CA . GLU A 134 ? 0.1381 0.1527 0.1485 0.0042 0.0047 0.0036 134 GLU A CA 1026 C C . GLU A 134 ? 0.1438 0.1563 0.1528 0.0037 0.0044 0.0049 134 GLU A C 1027 O O . GLU A 134 ? 0.1503 0.1621 0.1567 0.0044 0.0034 0.0059 134 GLU A O 1028 C CB . GLU A 134 ? 0.1429 0.1552 0.1521 0.0051 0.0045 0.0046 134 GLU A CB 1029 C CG . GLU A 134 ? 0.1435 0.1585 0.1540 0.0057 0.0047 0.0032 134 GLU A CG 1030 C CD . GLU A 134 ? 0.1567 0.1703 0.1651 0.0072 0.0039 0.0040 134 GLU A CD 1031 O OE1 . GLU A 134 ? 0.1543 0.1649 0.1599 0.0078 0.0030 0.0056 134 GLU A OE1 1032 O OE2 . GLU A 134 ? 0.1625 0.1780 0.1722 0.0075 0.0042 0.0029 134 GLU A OE2 1033 N N . VAL A 135 ? 0.1374 0.1491 0.1479 0.0026 0.0054 0.0050 135 VAL A N 1034 C CA . VAL A 135 ? 0.1389 0.1494 0.1484 0.0020 0.0052 0.0060 135 VAL A CA 1035 C C . VAL A 135 ? 0.1498 0.1630 0.1596 0.0018 0.0049 0.0050 135 VAL A C 1036 O O . VAL A 135 ? 0.1486 0.1615 0.1564 0.0019 0.0041 0.0058 135 VAL A O 1037 C CB . VAL A 135 ? 0.1341 0.1435 0.1451 0.0013 0.0064 0.0064 135 VAL A CB 1038 C CG1 . VAL A 135 ? 0.1440 0.1532 0.1543 0.0007 0.0062 0.0070 135 VAL A CG1 1039 C CG2 . VAL A 135 ? 0.1471 0.1544 0.1573 0.0019 0.0065 0.0075 135 VAL A CG2 1040 N N . ARG A 136 ? 0.1484 0.1643 0.1608 0.0013 0.0057 0.0031 136 ARG A N 1041 C CA . ARG A 136 ? 0.1524 0.1717 0.1653 0.0012 0.0054 0.0018 136 ARG A CA 1042 C C . ARG A 136 ? 0.1491 0.1703 0.1598 0.0026 0.0041 0.0019 136 ARG A C 1043 O O . ARG A 136 ? 0.1498 0.1729 0.1595 0.0029 0.0036 0.0019 136 ARG A O 1044 C CB . ARG A 136 ? 0.1440 0.1661 0.1604 0.0002 0.0068 -0.0007 136 ARG A CB 1045 C CG . ARG A 136 ? 0.1519 0.1723 0.1701 -0.0010 0.0082 -0.0008 136 ARG A CG 1046 C CD . ARG A 136 ? 0.1508 0.1718 0.1683 -0.0013 0.0078 -0.0004 136 ARG A CD 1047 N NE . ARG A 136 ? 0.1657 0.1856 0.1852 -0.0023 0.0094 -0.0009 136 ARG A NE 1048 C CZ . ARG A 136 ? 0.1663 0.1877 0.1866 -0.0028 0.0096 -0.0017 136 ARG A CZ 1049 N NH1 . ARG A 136 ? 0.1876 0.2115 0.2065 -0.0026 0.0083 -0.0018 136 ARG A NH1 1050 N NH2 . ARG A 136 ? 0.1807 0.2008 0.2029 -0.0035 0.0113 -0.0022 136 ARG A NH2 1051 N N . ALA A 137 ? 0.1507 0.1713 0.1604 0.0037 0.0037 0.0023 137 ALA A N 1052 C CA . ALA A 137 ? 0.1469 0.1685 0.1538 0.0055 0.0026 0.0029 137 ALA A CA 1053 C C . ALA A 137 ? 0.1590 0.1775 0.1626 0.0059 0.0020 0.0050 137 ALA A C 1054 O O . ALA A 137 ? 0.1531 0.1726 0.1544 0.0074 0.0014 0.0056 137 ALA A O 1055 C CB . ALA A 137 ? 0.1580 0.1785 0.1641 0.0067 0.0023 0.0032 137 ALA A CB 1056 N N . THR A 138 ? 0.1424 0.1573 0.1458 0.0047 0.0023 0.0062 138 THR A N 1057 C CA . THR A 138 ? 0.1493 0.1612 0.1499 0.0046 0.0020 0.0080 138 THR A CA 1058 C C . THR A 138 ? 0.1562 0.1691 0.1575 0.0033 0.0023 0.0079 138 THR A C 1059 O O . THR A 138 ? 0.1666 0.1773 0.1660 0.0028 0.0023 0.0091 138 THR A O 1060 C CB . THR A 138 ? 0.1575 0.1653 0.1571 0.0041 0.0022 0.0092 138 THR A CB 1061 O OG1 . THR A 138 ? 0.1680 0.1758 0.1700 0.0028 0.0028 0.0087 138 THR A OG1 1062 C CG2 . THR A 138 ? 0.1712 0.1780 0.1699 0.0054 0.0019 0.0093 138 THR A CG2 1063 N N . GLY A 139 ? 0.1468 0.1632 0.1510 0.0028 0.0027 0.0062 139 GLY A N 1064 C CA . GLY A 139 ? 0.1577 0.1756 0.1627 0.0018 0.0029 0.0058 139 GLY A CA 1065 C C . GLY A 139 ? 0.1633 0.1794 0.1697 0.0004 0.0036 0.0061 139 GLY A C 1066 O O . GLY A 139 ? 0.1956 0.2128 0.2027 -0.0004 0.0038 0.0058 139 GLY A O 1067 N N . ILE A 140 ? 0.1453 0.1591 0.1520 0.0003 0.0039 0.0066 140 ILE A N 1068 C CA . ILE A 140 ? 0.1499 0.1622 0.1573 -0.0005 0.0045 0.0071 140 ILE A CA 1069 C C . ILE A 140 ? 0.1501 0.1634 0.1605 -0.0008 0.0057 0.0059 140 ILE A C 1070 O O . ILE A 140 ? 0.1528 0.1670 0.1647 -0.0005 0.0062 0.0048 140 ILE A O 1071 C CB . ILE A 140 ? 0.1445 0.1540 0.1503 -0.0003 0.0043 0.0084 140 ILE A CB 1072 C CG1 . ILE A 140 ? 0.1604 0.1683 0.1632 -0.0004 0.0035 0.0094 140 ILE A CG1 1073 C CG2 . ILE A 140 ? 0.1439 0.1526 0.1505 -0.0007 0.0049 0.0088 140 ILE A CG2 1074 C CD1 . ILE A 140 ? 0.1680 0.1731 0.1690 -0.0004 0.0033 0.0103 140 ILE A CD1 1075 N N . GLN A 141 ? 0.1469 0.1602 0.1581 -0.0014 0.0064 0.0060 141 GLN A N 1076 C CA . GLN A 141 ? 0.1378 0.1517 0.1518 -0.0016 0.0079 0.0048 141 GLN A CA 1077 C C . GLN A 141 ? 0.1414 0.1532 0.1560 -0.0012 0.0091 0.0057 141 GLN A C 1078 O O . GLN A 141 ? 0.1451 0.1567 0.1617 -0.0012 0.0107 0.0050 141 GLN A O 1079 C CB . GLN A 141 ? 0.1514 0.1671 0.1663 -0.0022 0.0082 0.0040 141 GLN A CB 1080 C CG . GLN A 141 ? 0.1448 0.1630 0.1588 -0.0024 0.0070 0.0033 141 GLN A CG 1081 C CD . GLN A 141 ? 0.1605 0.1784 0.1720 -0.0025 0.0060 0.0048 141 GLN A CD 1082 O OE1 . GLN A 141 ? 0.1780 0.1940 0.1883 -0.0025 0.0058 0.0061 141 GLN A OE1 1083 N NE2 . GLN A 141 ? 0.1759 0.1961 0.1868 -0.0026 0.0053 0.0043 141 GLN A NE2 1084 N N . TYR A 142 ? 0.1334 0.1438 0.1461 -0.0007 0.0084 0.0072 142 TYR A N 1085 C CA . TYR A 142 ? 0.1476 0.1569 0.1603 0.0000 0.0093 0.0082 142 TYR A CA 1086 C C . TYR A 142 ? 0.1410 0.1492 0.1522 0.0005 0.0087 0.0093 142 TYR A C 1087 O O . TYR A 142 ? 0.1432 0.1514 0.1526 0.0002 0.0074 0.0097 142 TYR A O 1088 C CB . TYR A 142 ? 0.1472 0.1577 0.1592 -0.0003 0.0091 0.0087 142 TYR A CB 1089 C CG . TYR A 142 ? 0.1496 0.1601 0.1613 0.0007 0.0098 0.0097 142 TYR A CG 1090 C CD1 . TYR A 142 ? 0.1517 0.1609 0.1642 0.0020 0.0112 0.0103 142 TYR A CD1 1091 C CD2 . TYR A 142 ? 0.1581 0.1702 0.1687 0.0006 0.0091 0.0101 142 TYR A CD2 1092 C CE1 . TYR A 142 ? 0.1567 0.1663 0.1686 0.0033 0.0119 0.0114 142 TYR A CE1 1093 C CE2 . TYR A 142 ? 0.1580 0.1710 0.1682 0.0017 0.0097 0.0110 142 TYR A CE2 1094 C CZ . TYR A 142 ? 0.1539 0.1656 0.1646 0.0033 0.0111 0.0117 142 TYR A CZ 1095 O OH . TYR A 142 ? 0.1737 0.1868 0.1837 0.0048 0.0116 0.0127 142 TYR A OH 1096 N N . ALA A 143 ? 0.1368 0.1439 0.1488 0.0014 0.0098 0.0097 143 ALA A N 1097 C CA . ALA A 143 ? 0.1308 0.1371 0.1415 0.0021 0.0093 0.0106 143 ALA A CA 1098 C C . ALA A 143 ? 0.1434 0.1500 0.1538 0.0033 0.0101 0.0117 143 ALA A C 1099 O O . ALA A 143 ? 0.1454 0.1515 0.1570 0.0041 0.0118 0.0120 143 ALA A O 1100 C CB . ALA A 143 ? 0.1504 0.1559 0.1622 0.0024 0.0100 0.0101 143 ALA A CB 1101 N N . PHE A 144 ? 0.1408 0.1481 0.1496 0.0035 0.0091 0.0123 144 PHE A N 1102 C CA . PHE A 144 ? 0.1537 0.1623 0.1619 0.0048 0.0097 0.0132 144 PHE A CA 1103 C C . PHE A 144 ? 0.1489 0.1565 0.1572 0.0062 0.0105 0.0139 144 PHE A C 1104 O O . PHE A 144 ? 0.1530 0.1615 0.1602 0.0068 0.0098 0.0143 144 PHE A O 1105 C CB . PHE A 144 ? 0.1499 0.1604 0.1565 0.0043 0.0083 0.0131 144 PHE A CB 1106 C CG . PHE A 144 ? 0.1493 0.1607 0.1556 0.0028 0.0076 0.0125 144 PHE A CG 1107 C CD1 . PHE A 144 ? 0.1586 0.1710 0.1658 0.0031 0.0083 0.0125 144 PHE A CD1 1108 C CD2 . PHE A 144 ? 0.1568 0.1680 0.1618 0.0013 0.0064 0.0119 144 PHE A CD2 1109 C CE1 . PHE A 144 ? 0.1601 0.1738 0.1668 0.0018 0.0076 0.0119 144 PHE A CE1 1110 C CE2 . PHE A 144 ? 0.1553 0.1673 0.1599 -0.0001 0.0059 0.0114 144 PHE A CE2 1111 C CZ . PHE A 144 ? 0.1576 0.1711 0.1631 0.0002 0.0064 0.0114 144 PHE A CZ 1112 N N . ALA A 145 ? 0.1445 0.1505 0.1543 0.0067 0.0121 0.0141 145 ALA A N 1113 C CA . ALA A 145 ? 0.1537 0.1586 0.1638 0.0079 0.0133 0.0148 145 ALA A CA 1114 C C . ALA A 145 ? 0.1458 0.1489 0.1574 0.0085 0.0158 0.0151 145 ALA A C 1115 O O . ALA A 145 ? 0.1569 0.1594 0.1698 0.0074 0.0163 0.0141 145 ALA A O 1116 C CB . ALA A 145 ? 0.1546 0.1586 0.1650 0.0068 0.0124 0.0138 145 ALA A CB 1117 N N . PRO A 146 ? 0.1556 0.1577 0.1672 0.0101 0.0175 0.0163 146 PRO A N 1118 C CA . PRO A 146 ? 0.1553 0.1581 0.1657 0.0114 0.0172 0.0173 146 PRO A CA 1119 C C . PRO A 146 ? 0.1561 0.1613 0.1647 0.0133 0.0168 0.0185 146 PRO A C 1120 O O . PRO A 146 ? 0.1743 0.1799 0.1827 0.0147 0.0180 0.0194 146 PRO A O 1121 C CB . PRO A 146 ? 0.1781 0.1785 0.1894 0.0125 0.0199 0.0181 146 PRO A CB 1122 C CG . PRO A 146 ? 0.1797 0.1783 0.1921 0.0126 0.0221 0.0183 146 PRO A CG 1123 C CD . PRO A 146 ? 0.1562 0.1558 0.1692 0.0106 0.0204 0.0166 146 PRO A CD 1124 N N . CYS A 147 ? 0.1579 0.1650 0.1654 0.0136 0.0152 0.0185 147 CYS A N 1125 C CA . CYS A 147 ? 0.1650 0.1749 0.1710 0.0158 0.0153 0.0196 147 CYS A CA 1126 C C . CYS A 147 ? 0.1809 0.1895 0.1869 0.0181 0.0177 0.0213 147 CYS A C 1127 O O . CYS A 147 ? 0.1841 0.1913 0.1903 0.0180 0.0180 0.0214 147 CYS A O 1128 C CB . CYS A 147 ? 0.1668 0.1790 0.1717 0.0152 0.0132 0.0187 147 CYS A CB 1129 S SG . CYS A 147 ? 0.1886 0.2056 0.1919 0.0180 0.0132 0.0197 147 CYS A SG 1130 N N . ILE A 148 ? 0.1712 0.1800 0.1766 0.0203 0.0194 0.0227 148 ILE A N 1131 C CA . ILE A 148 ? 0.1727 0.1799 0.1777 0.0229 0.0222 0.0248 148 ILE A CA 1132 C C . ILE A 148 ? 0.1822 0.1934 0.1851 0.0261 0.0221 0.0262 148 ILE A C 1133 O O . ILE A 148 ? 0.2061 0.2168 0.2080 0.0291 0.0245 0.0284 148 ILE A O 1134 C CB . ILE A 148 ? 0.1814 0.1847 0.1873 0.0234 0.0251 0.0256 148 ILE A CB 1135 C CG1 . ILE A 148 ? 0.1834 0.1883 0.1888 0.0240 0.0248 0.0256 148 ILE A CG1 1136 C CG2 . ILE A 148 ? 0.1884 0.1882 0.1966 0.0204 0.0255 0.0240 148 ILE A CG2 1137 C CD1 . ILE A 148 ? 0.1990 0.2002 0.2048 0.0253 0.0281 0.0268 148 ILE A CD1 1138 N N . ALA A 149 ? 0.1753 0.1907 0.1775 0.0255 0.0195 0.0250 149 ALA A N 1139 C CA . ALA A 149 ? 0.1962 0.2164 0.1967 0.0281 0.0191 0.0258 149 ALA A CA 1140 C C . ALA A 149 ? 0.1982 0.2172 0.1982 0.0301 0.0207 0.0274 149 ALA A C 1141 O O . ALA A 149 ? 0.2102 0.2259 0.2113 0.0284 0.0209 0.0269 149 ALA A O 1142 C CB . ALA A 149 ? 0.1907 0.2150 0.1910 0.0264 0.0161 0.0237 149 ALA A CB 1143 N N . VAL A 150 ? 0.2065 0.2282 0.2048 0.0338 0.0220 0.0293 150 VAL A N 1144 C CA . VAL A 150 ? 0.2041 0.2259 0.2015 0.0362 0.0234 0.0310 150 VAL A CA 1145 C C . VAL A 150 ? 0.2135 0.2417 0.2097 0.0372 0.0212 0.0300 150 VAL A C 1146 O O . VAL A 150 ? 0.2142 0.2477 0.2089 0.0401 0.0212 0.0307 150 VAL A O 1147 C CB . VAL A 150 ? 0.2083 0.2286 0.2043 0.0401 0.0268 0.0340 150 VAL A CB 1148 C CG1 . VAL A 150 ? 0.2079 0.2280 0.2030 0.0423 0.0283 0.0357 150 VAL A CG1 1149 C CG2 . VAL A 150 ? 0.2235 0.2372 0.2208 0.0388 0.0291 0.0345 150 VAL A CG2 1150 N N . CYS A 151 ? 0.2074 0.2357 0.2044 0.0348 0.0194 0.0283 151 CYS A N 1151 C CA . CYS A 151 ? 0.2064 0.2408 0.2027 0.0350 0.0172 0.0267 151 CYS A CA 1152 C C . CYS A 151 ? 0.2155 0.2535 0.2101 0.0389 0.0183 0.0284 151 CYS A C 1153 O O . CYS A 151 ? 0.2309 0.2663 0.2256 0.0395 0.0194 0.0295 151 CYS A O 1154 C CB . CYS A 151 ? 0.2248 0.2579 0.2222 0.0314 0.0150 0.0242 151 CYS A CB 1155 S SG . CYS A 151 ? 0.2479 0.2877 0.2445 0.0316 0.0127 0.0220 151 CYS A SG 1156 N N . ARG A 152 ? 0.2068 0.2512 0.2000 0.0416 0.0180 0.0286 152 ARG A N 1157 C CA . ARG A 152 ? 0.2204 0.2690 0.2118 0.0459 0.0192 0.0305 152 ARG A CA 1158 C C . ARG A 152 ? 0.2277 0.2831 0.2188 0.0458 0.0169 0.0282 152 ARG A C 1159 O O . ARG A 152 ? 0.2441 0.3042 0.2336 0.0493 0.0175 0.0293 152 ARG A O 1160 C CB . ARG A 152 ? 0.2433 0.2951 0.2329 0.0500 0.0208 0.0326 152 ARG A CB 1161 C CG . ARG A 152 ? 0.2535 0.2985 0.2432 0.0505 0.0234 0.0349 152 ARG A CG 1162 C CD . ARG A 152 ? 0.2681 0.3073 0.2575 0.0519 0.0263 0.0376 152 ARG A CD 1163 N NE . ARG A 152 ? 0.2684 0.3107 0.2551 0.0573 0.0285 0.0405 152 ARG A NE 1164 C CZ . ARG A 152 ? 0.2859 0.3243 0.2717 0.0595 0.0315 0.0433 152 ARG A CZ 1165 N NH1 . ARG A 152 ? 0.2844 0.3262 0.2676 0.0648 0.0334 0.0461 152 ARG A NH1 1166 N NH2 . ARG A 152 ? 0.2799 0.3113 0.2674 0.0567 0.0327 0.0433 152 ARG A NH2 1167 N N . ASP A 153 ? 0.2266 0.2826 0.2190 0.0419 0.0145 0.0250 153 ASP A N 1168 C CA . ASP A 153 ? 0.2256 0.2874 0.2180 0.0412 0.0125 0.0224 153 ASP A CA 1169 C C . ASP A 153 ? 0.2205 0.2783 0.2144 0.0366 0.0108 0.0198 153 ASP A C 1170 O O . ASP A 153 ? 0.2112 0.2671 0.2060 0.0337 0.0099 0.0183 153 ASP A O 1171 C CB . ASP A 153 ? 0.2526 0.3225 0.2444 0.0421 0.0114 0.0207 153 ASP A CB 1172 C CG . ASP A 153 ? 0.3129 0.3898 0.3046 0.0420 0.0098 0.0179 153 ASP A CG 1173 O OD1 . ASP A 153 ? 0.2716 0.3465 0.2641 0.0394 0.0088 0.0161 153 ASP A OD1 1174 O OD2 . ASP A 153 ? 0.3711 0.4563 0.3617 0.0447 0.0096 0.0174 153 ASP A OD2 1175 N N . PRO A 154 ? 0.2080 0.2639 0.2022 0.0360 0.0105 0.0195 154 PRO A N 1176 C CA . PRO A 154 ? 0.2062 0.2573 0.2016 0.0321 0.0092 0.0175 154 PRO A CA 1177 C C . PRO A 154 ? 0.2115 0.2658 0.2072 0.0294 0.0072 0.0141 154 PRO A C 1178 O O . PRO A 154 ? 0.2164 0.2666 0.2129 0.0262 0.0063 0.0124 154 PRO A O 1179 C CB . PRO A 154 ? 0.1968 0.2463 0.1920 0.0329 0.0096 0.0182 154 PRO A CB 1180 C CG . PRO A 154 ? 0.2017 0.2580 0.1956 0.0367 0.0101 0.0189 154 PRO A CG 1181 C CD . PRO A 154 ? 0.1980 0.2563 0.1912 0.0392 0.0114 0.0209 154 PRO A CD 1182 N N . ARG A 155 ? 0.2303 0.2919 0.2255 0.0306 0.0068 0.0128 155 ARG A N 1183 C CA . ARG A 155 ? 0.2191 0.2836 0.2148 0.0276 0.0052 0.0092 155 ARG A CA 1184 C C . ARG A 155 ? 0.2141 0.2751 0.2105 0.0249 0.0050 0.0088 155 ARG A C 1185 O O . ARG A 155 ? 0.2375 0.2987 0.2344 0.0217 0.0040 0.0060 155 ARG A O 1186 C CB . ARG A 155 ? 0.2289 0.3032 0.2240 0.0297 0.0048 0.0077 155 ARG A CB 1187 C CG . ARG A 155 ? 0.2482 0.3261 0.2427 0.0320 0.0048 0.0076 155 ARG A CG 1188 C CD . ARG A 155 ? 0.2632 0.3517 0.2571 0.0344 0.0045 0.0061 155 ARG A CD 1189 N NE . ARG A 155 ? 0.2879 0.3790 0.2807 0.0384 0.0057 0.0092 155 ARG A NE 1190 C CZ . ARG A 155 ? 0.3306 0.4311 0.3224 0.0417 0.0058 0.0089 155 ARG A CZ 1191 N NH1 . ARG A 155 ? 0.3871 0.4952 0.3792 0.0411 0.0046 0.0054 155 ARG A NH1 1192 N NH2 . ARG A 155 ? 0.3424 0.4446 0.3328 0.0456 0.0072 0.0119 155 ARG A NH2 1193 N N . TRP A 156 ? 0.2070 0.2650 0.2033 0.0261 0.0061 0.0114 156 TRP A N 1194 C CA . TRP A 156 ? 0.2009 0.2553 0.1980 0.0237 0.0060 0.0111 156 TRP A CA 1195 C C . TRP A 156 ? 0.2058 0.2537 0.2035 0.0202 0.0053 0.0101 156 TRP A C 1196 O O . TRP A 156 ? 0.2064 0.2497 0.2042 0.0205 0.0057 0.0113 156 TRP A O 1197 C CB . TRP A 156 ? 0.2059 0.2573 0.2028 0.0256 0.0075 0.0141 156 TRP A CB 1198 C CG . TRP A 156 ? 0.2086 0.2575 0.2062 0.0237 0.0074 0.0140 156 TRP A CG 1199 C CD1 . TRP A 156 ? 0.2236 0.2752 0.2214 0.0214 0.0064 0.0118 156 TRP A CD1 1200 C CD2 . TRP A 156 ? 0.1968 0.2406 0.1948 0.0240 0.0087 0.0160 156 TRP A CD2 1201 N NE1 . TRP A 156 ? 0.2261 0.2744 0.2244 0.0204 0.0068 0.0125 156 TRP A NE1 1202 C CE2 . TRP A 156 ? 0.2151 0.2590 0.2135 0.0221 0.0082 0.0151 156 TRP A CE2 1203 C CE3 . TRP A 156 ? 0.2014 0.2408 0.1994 0.0256 0.0103 0.0185 156 TRP A CE3 1204 C CZ2 . TRP A 156 ? 0.2255 0.2651 0.2245 0.0217 0.0091 0.0164 156 TRP A CZ2 1205 C CZ3 . TRP A 156 ? 0.2228 0.2579 0.2215 0.0251 0.0114 0.0196 156 TRP A CZ3 1206 C CH2 . TRP A 156 ? 0.2232 0.2585 0.2224 0.0233 0.0107 0.0186 156 TRP A CH2 1207 N N . GLY A 157 ? 0.2127 0.2600 0.2108 0.0171 0.0045 0.0080 157 GLY A N 1208 C CA . GLY A 157 ? 0.2102 0.2513 0.2086 0.0141 0.0040 0.0072 157 GLY A CA 1209 C C . GLY A 157 ? 0.2059 0.2410 0.2046 0.0138 0.0045 0.0091 157 GLY A C 1210 O O . GLY A 157 ? 0.2266 0.2569 0.2255 0.0119 0.0041 0.0086 157 GLY A O 1211 N N . ARG A 158 ? 0.1960 0.2316 0.1950 0.0158 0.0055 0.0111 158 ARG A N 1212 C CA . ARG A 158 ? 0.2050 0.2351 0.2046 0.0154 0.0062 0.0127 158 ARG A CA 1213 C C . ARG A 158 ? 0.1930 0.2217 0.1927 0.0178 0.0075 0.0148 158 ARG A C 1214 O O . ARG A 158 ? 0.1963 0.2216 0.1967 0.0180 0.0085 0.0162 158 ARG A O 1215 C CB . ARG A 158 ? 0.2011 0.2315 0.2010 0.0150 0.0066 0.0132 158 ARG A CB 1216 C CG . ARG A 158 ? 0.2038 0.2363 0.2036 0.0127 0.0055 0.0111 158 ARG A CG 1217 C CD . ARG A 158 ? 0.1970 0.2295 0.1972 0.0122 0.0059 0.0115 158 ARG A CD 1218 N NE . ARG A 158 ? 0.2027 0.2297 0.2034 0.0109 0.0061 0.0122 158 ARG A NE 1219 C CZ . ARG A 158 ? 0.1853 0.2114 0.1864 0.0098 0.0062 0.0122 158 ARG A CZ 1220 N NH1 . ARG A 158 ? 0.2006 0.2307 0.2015 0.0098 0.0060 0.0116 158 ARG A NH1 1221 N NH2 . ARG A 158 ? 0.1758 0.1975 0.1775 0.0088 0.0063 0.0127 158 ARG A NH2 1222 N N . CYS A 159 ? 0.2008 0.2323 0.2000 0.0198 0.0076 0.0151 159 CYS A N 1223 C CA . CYS A 159 ? 0.2119 0.2421 0.2110 0.0222 0.0092 0.0173 159 CYS A CA 1224 C C . CYS A 159 ? 0.1814 0.2059 0.1815 0.0209 0.0096 0.0177 159 CYS A C 1225 O O . CYS A 159 ? 0.1834 0.2057 0.1840 0.0221 0.0114 0.0195 159 CYS A O 1226 C CB . CYS A 159 ? 0.2416 0.2759 0.2399 0.0243 0.0091 0.0173 159 CYS A CB 1227 S SG . CYS A 159 ? 0.2994 0.3341 0.2971 0.0283 0.0115 0.0205 159 CYS A SG 1228 N N . TYR A 160 ? 0.1871 0.2094 0.1875 0.0185 0.0083 0.0161 160 TYR A N 1229 C CA . TYR A 160 ? 0.1748 0.1925 0.1760 0.0174 0.0085 0.0163 160 TYR A CA 1230 C C . TYR A 160 ? 0.1704 0.1854 0.1726 0.0165 0.0094 0.0168 160 TYR A C 1231 O O . TYR A 160 ? 0.1675 0.1797 0.1707 0.0161 0.0101 0.0172 160 TYR A O 1232 C CB . TYR A 160 ? 0.1641 0.1803 0.1650 0.0155 0.0069 0.0145 160 TYR A CB 1233 C CG . TYR A 160 ? 0.1585 0.1743 0.1590 0.0134 0.0058 0.0131 160 TYR A CG 1234 C CD1 . TYR A 160 ? 0.1606 0.1735 0.1616 0.0120 0.0058 0.0131 160 TYR A CD1 1235 C CD2 . TYR A 160 ? 0.1699 0.1883 0.1695 0.0129 0.0049 0.0117 160 TYR A CD2 1236 C CE1 . TYR A 160 ? 0.1594 0.1718 0.1598 0.0101 0.0050 0.0120 160 TYR A CE1 1237 C CE2 . TYR A 160 ? 0.1674 0.1852 0.1666 0.0107 0.0042 0.0103 160 TYR A CE2 1238 C CZ . TYR A 160 ? 0.1787 0.1933 0.1783 0.0094 0.0043 0.0107 160 TYR A CZ 1239 O OH . TYR A 160 ? 0.1916 0.2054 0.1906 0.0073 0.0037 0.0095 160 TYR A OH 1240 N N . GLU A 161 ? 0.1685 0.1848 0.1705 0.0163 0.0093 0.0168 161 GLU A N 1241 C CA . GLU A 161 ? 0.1739 0.1880 0.1769 0.0157 0.0103 0.0174 161 GLU A CA 1242 C C . GLU A 161 ? 0.1651 0.1791 0.1685 0.0178 0.0125 0.0192 161 GLU A C 1243 O O . GLU A 161 ? 0.1687 0.1807 0.1730 0.0174 0.0136 0.0197 161 GLU A O 1244 C CB . GLU A 161 ? 0.1734 0.1889 0.1761 0.0144 0.0093 0.0165 161 GLU A CB 1245 C CG . GLU A 161 ? 0.1769 0.1918 0.1791 0.0121 0.0076 0.0148 161 GLU A CG 1246 C CD . GLU A 161 ? 0.1828 0.1979 0.1851 0.0105 0.0071 0.0141 161 GLU A CD 1247 O OE1 . GLU A 161 ? 0.1845 0.2023 0.1860 0.0099 0.0063 0.0131 161 GLU A OE1 1248 O OE2 . GLU A 161 ? 0.1860 0.1988 0.1890 0.0098 0.0075 0.0144 161 GLU A OE2 1249 N N . SER A 162 ? 0.1734 0.1892 0.1761 0.0201 0.0133 0.0204 162 SER A N 1250 C CA . SER A 162 ? 0.1811 0.1961 0.1837 0.0225 0.0158 0.0225 162 SER A CA 1251 C C . SER A 162 ? 0.1804 0.1926 0.1838 0.0226 0.0172 0.0231 162 SER A C 1252 O O . SER A 162 ? 0.1865 0.1996 0.1896 0.0226 0.0163 0.0226 162 SER A O 1253 C CB . SER A 162 ? 0.1846 0.2040 0.1857 0.0254 0.0161 0.0235 162 SER A CB 1254 O OG . SER A 162 ? 0.1913 0.2095 0.1919 0.0281 0.0188 0.0259 162 SER A OG 1255 N N . TYR A 163 ? 0.1889 0.1976 0.1934 0.0225 0.0195 0.0239 163 TYR A N 1256 C CA . TYR A 163 ? 0.1807 0.1868 0.1860 0.0224 0.0212 0.0243 163 TYR A CA 1257 C C . TYR A 163 ? 0.1938 0.2014 0.1979 0.0252 0.0224 0.0261 163 TYR A C 1258 O O . TYR A 163 ? 0.1958 0.2027 0.2003 0.0250 0.0229 0.0261 163 TYR A O 1259 C CB . TYR A 163 ? 0.1806 0.1829 0.1875 0.0216 0.0238 0.0247 163 TYR A CB 1260 C CG . TYR A 163 ? 0.1753 0.1763 0.1837 0.0190 0.0229 0.0229 163 TYR A CG 1261 C CD1 . TYR A 163 ? 0.1850 0.1855 0.1946 0.0166 0.0216 0.0209 163 TYR A CD1 1262 C CD2 . TYR A 163 ? 0.1859 0.1864 0.1942 0.0191 0.0234 0.0231 163 TYR A CD2 1263 C CE1 . TYR A 163 ? 0.1790 0.1787 0.1899 0.0145 0.0208 0.0193 163 TYR A CE1 1264 C CE2 . TYR A 163 ? 0.1858 0.1854 0.1956 0.0167 0.0227 0.0214 163 TYR A CE2 1265 C CZ . TYR A 163 ? 0.1828 0.1821 0.1937 0.0145 0.0214 0.0196 163 TYR A CZ 1266 O OH . TYR A 163 ? 0.1976 0.1965 0.2098 0.0124 0.0206 0.0180 163 TYR A OH 1267 N N . SER A 164 ? 0.1981 0.2080 0.2006 0.0279 0.0231 0.0277 164 SER A N 1268 C CA . SER A 164 ? 0.2070 0.2182 0.2081 0.0311 0.0248 0.0298 164 SER A CA 1269 C C . SER A 164 ? 0.2173 0.2325 0.2165 0.0342 0.0249 0.0312 164 SER A C 1270 O O . SER A 164 ? 0.2078 0.2233 0.2068 0.0342 0.0247 0.0311 164 SER A O 1271 C CB . SER A 164 ? 0.2066 0.2131 0.2084 0.0315 0.0285 0.0315 164 SER A CB 1272 O OG . SER A 164 ? 0.2109 0.2184 0.2112 0.0347 0.0303 0.0337 164 SER A OG 1273 N N . GLU A 165 ? 0.2036 0.2221 0.2012 0.0370 0.0252 0.0325 165 GLU A N 1274 C CA . GLU A 165 ? 0.2202 0.2425 0.2156 0.0410 0.0262 0.0344 165 GLU A CA 1275 C C . GLU A 165 ? 0.2178 0.2362 0.2125 0.0436 0.0301 0.0375 165 GLU A C 1276 O O . GLU A 165 ? 0.2431 0.2640 0.2359 0.0471 0.0312 0.0393 165 GLU A O 1277 C CB . GLU A 165 ? 0.2374 0.2652 0.2313 0.0435 0.0253 0.0348 165 GLU A CB 1278 C CG . GLU A 165 ? 0.2404 0.2658 0.2338 0.0452 0.0278 0.0368 165 GLU A CG 1279 C CD . GLU A 165 ? 0.2653 0.2958 0.2577 0.0467 0.0265 0.0365 165 GLU A CD 1280 O OE1 . GLU A 165 ? 0.2556 0.2900 0.2484 0.0451 0.0234 0.0339 165 GLU A OE1 1281 O OE2 . GLU A 165 ? 0.2731 0.3033 0.2643 0.0495 0.0288 0.0389 165 GLU A OE2 1282 N N . ASP A 166 ? 0.2288 0.2412 0.2248 0.0420 0.0324 0.0379 166 ASP A N 1283 C CA . ASP A 166 ? 0.2376 0.2450 0.2332 0.0438 0.0366 0.0405 166 ASP A CA 1284 C C . ASP A 166 ? 0.2357 0.2389 0.2329 0.0413 0.0372 0.0394 166 ASP A C 1285 O O . ASP A 166 ? 0.2234 0.2239 0.2231 0.0375 0.0364 0.0372 166 ASP A O 1286 C CB . ASP A 166 ? 0.2714 0.2750 0.2678 0.0431 0.0388 0.0411 166 ASP A CB 1287 C CG . ASP A 166 ? 0.3094 0.3070 0.3055 0.0445 0.0437 0.0437 166 ASP A CG 1288 O OD1 . ASP A 166 ? 0.3081 0.3033 0.3036 0.0458 0.0457 0.0449 166 ASP A OD1 1289 O OD2 . ASP A 166 ? 0.3993 0.3946 0.3957 0.0445 0.0459 0.0445 166 ASP A OD2 1290 N N . ARG A 167 ? 0.2396 0.2428 0.2355 0.0438 0.0386 0.0409 167 ARG A N 1291 C CA . ARG A 167 ? 0.2472 0.2468 0.2445 0.0418 0.0392 0.0400 167 ARG A CA 1292 C C . ARG A 167 ? 0.2494 0.2422 0.2487 0.0394 0.0422 0.0397 167 ARG A C 1293 O O . ARG A 167 ? 0.2394 0.2298 0.2407 0.0365 0.0419 0.0378 167 ARG A O 1294 C CB . ARG A 167 ? 0.2617 0.2624 0.2570 0.0454 0.0405 0.0419 167 ARG A CB 1295 C CG . ARG A 167 ? 0.3208 0.3192 0.3138 0.0499 0.0446 0.0455 167 ARG A CG 1296 C CD . ARG A 167 ? 0.3808 0.3717 0.3745 0.0496 0.0488 0.0466 167 ARG A CD 1297 N NE . ARG A 167 ? 0.4667 0.4551 0.4576 0.0544 0.0529 0.0504 167 ARG A NE 1298 C CZ . ARG A 167 ? 0.4938 0.4747 0.4848 0.0548 0.0576 0.0520 167 ARG A CZ 1299 N NH1 . ARG A 167 ? 0.5306 0.5093 0.5187 0.0595 0.0615 0.0558 167 ARG A NH1 1300 N NH2 . ARG A 167 ? 0.4291 0.4050 0.4231 0.0506 0.0586 0.0498 167 ARG A NH2 1301 N N . ARG A 168 ? 0.2543 0.2442 0.2532 0.0407 0.0453 0.0415 168 ARG A N 1302 C CA . ARG A 168 ? 0.2635 0.2472 0.2647 0.0380 0.0483 0.0408 168 ARG A CA 1303 C C . ARG A 168 ? 0.2314 0.2157 0.2355 0.0333 0.0457 0.0373 168 ARG A C 1304 O O . ARG A 168 ? 0.2548 0.2357 0.2612 0.0303 0.0468 0.0355 168 ARG A O 1305 C CB . ARG A 168 ? 0.2897 0.2700 0.2899 0.0400 0.0523 0.0433 168 ARG A CB 1306 C CG . ARG A 168 ? 0.3202 0.2987 0.3175 0.0447 0.0557 0.0469 168 ARG A CG 1307 C CD . ARG A 168 ? 0.3594 0.3359 0.3549 0.0476 0.0592 0.0499 168 ARG A CD 1308 N NE A ARG A 168 ? 0.4403 0.4127 0.4334 0.0515 0.0636 0.0533 168 ARG A NE 1309 N NE B ARG A 168 ? 0.3104 0.2927 0.3051 0.0485 0.0563 0.0499 168 ARG A NE 1310 C CZ A ARG A 168 ? 0.4856 0.4610 0.4752 0.0569 0.0641 0.0564 168 ARG A CZ 1311 C CZ B ARG A 168 ? 0.3224 0.3043 0.3158 0.0504 0.0583 0.0519 168 ARG A CZ 1312 N NH1 A ARG A 168 ? 0.5242 0.5072 0.5123 0.0588 0.0604 0.0564 168 ARG A NH1 1313 N NH1 B ARG A 168 ? 0.3043 0.2919 0.2971 0.0510 0.0553 0.0514 168 ARG A NH1 1314 N NH2 A ARG A 168 ? 0.5152 0.4860 0.5026 0.0605 0.0685 0.0595 168 ARG A NH2 1315 N NH2 B ARG A 168 ? 0.3361 0.3119 0.3288 0.0517 0.0636 0.0544 168 ARG A NH2 1316 N N . ILE A 169 ? 0.2448 0.2335 0.2485 0.0329 0.0423 0.0364 169 ILE A N 1317 C CA . ILE A 169 ? 0.2214 0.2112 0.2274 0.0291 0.0396 0.0333 169 ILE A CA 1318 C C . ILE A 169 ? 0.2244 0.2154 0.2313 0.0271 0.0370 0.0313 169 ILE A C 1319 O O . ILE A 169 ? 0.2306 0.2197 0.2397 0.0239 0.0368 0.0291 169 ILE A O 1320 C CB . ILE A 169 ? 0.2289 0.2228 0.2340 0.0296 0.0369 0.0330 169 ILE A CB 1321 C CG1 . ILE A 169 ? 0.2481 0.2406 0.2528 0.0311 0.0397 0.0348 169 ILE A CG1 1322 C CG2 . ILE A 169 ? 0.2426 0.2377 0.2497 0.0260 0.0339 0.0299 169 ILE A CG2 1323 C CD1 . ILE A 169 ? 0.2528 0.2495 0.2564 0.0320 0.0373 0.0346 169 ILE A CD1 1324 N N . VAL A 170 ? 0.2116 0.2057 0.2167 0.0290 0.0353 0.0320 170 VAL A N 1325 C CA . VAL A 170 ? 0.2053 0.2005 0.2112 0.0272 0.0332 0.0303 170 VAL A CA 1326 C C . VAL A 170 ? 0.2080 0.1988 0.2153 0.0260 0.0358 0.0300 170 VAL A C 1327 O O . VAL A 170 ? 0.2100 0.2002 0.2192 0.0231 0.0346 0.0277 170 VAL A O 1328 C CB . VAL A 170 ? 0.1928 0.1922 0.1966 0.0296 0.0314 0.0311 170 VAL A CB 1329 C CG1 . VAL A 170 ? 0.1920 0.1923 0.1965 0.0277 0.0296 0.0295 170 VAL A CG1 1330 C CG2 . VAL A 170 ? 0.1957 0.1998 0.1983 0.0302 0.0288 0.0308 170 VAL A CG2 1331 N N . GLN A 171 ? 0.2131 0.2007 0.2195 0.0285 0.0395 0.0322 171 GLN A N 1332 C CA . GLN A 171 ? 0.2232 0.2060 0.2312 0.0272 0.0425 0.0318 171 GLN A CA 1333 C C . GLN A 171 ? 0.2291 0.2095 0.2400 0.0235 0.0431 0.0294 171 GLN A C 1334 O O . GLN A 171 ? 0.2483 0.2274 0.2612 0.0210 0.0433 0.0273 171 GLN A O 1335 C CB . GLN A 171 ? 0.2300 0.2088 0.2365 0.0304 0.0470 0.0348 171 GLN A CB 1336 C CG . GLN A 171 ? 0.2455 0.2265 0.2491 0.0345 0.0469 0.0371 171 GLN A CG 1337 C CD . GLN A 171 ? 0.2711 0.2478 0.2729 0.0381 0.0517 0.0404 171 GLN A CD 1338 O OE1 . GLN A 171 ? 0.3216 0.2943 0.3235 0.0387 0.0545 0.0410 171 GLN A OE1 1339 N NE2 . GLN A 171 ? 0.2676 0.2451 0.2677 0.0407 0.0527 0.0425 171 GLN A NE2 1340 N N . SER A 172 ? 0.2219 0.2020 0.2331 0.0231 0.0438 0.0295 172 SER A N 1341 C CA . SER A 172 ? 0.2274 0.2059 0.2415 0.0196 0.0446 0.0270 172 SER A CA 1342 C C . SER A 172 ? 0.2221 0.2040 0.2377 0.0167 0.0406 0.0239 172 SER A C 1343 O O . SER A 172 ? 0.2391 0.2200 0.2572 0.0138 0.0412 0.0215 172 SER A O 1344 C CB . SER A 172 ? 0.2485 0.2266 0.2626 0.0197 0.0458 0.0275 172 SER A CB 1345 O OG . SER A 172 ? 0.2764 0.2590 0.2895 0.0202 0.0421 0.0273 172 SER A OG 1346 N N . MET A 173 ? 0.2153 0.2011 0.2293 0.0176 0.0369 0.0242 173 MET A N 1347 C CA . MET A 173 ? 0.2157 0.2044 0.2306 0.0153 0.0333 0.0217 173 MET A CA 1348 C C . MET A 173 ? 0.2236 0.2127 0.2389 0.0143 0.0323 0.0207 173 MET A C 1349 O O . MET A 173 ? 0.2207 0.2118 0.2366 0.0125 0.0296 0.0188 173 MET A O 1350 C CB . MET A 173 ? 0.2293 0.2216 0.2424 0.0163 0.0301 0.0221 173 MET A CB 1351 C CG . MET A 173 ? 0.2476 0.2397 0.2603 0.0174 0.0312 0.0232 173 MET A CG 1352 S SD A MET A 173 ? 0.2281 0.2194 0.2435 0.0143 0.0317 0.0206 173 MET A SD 1353 S SD B MET A 173 ? 0.2334 0.2278 0.2465 0.0163 0.0290 0.0217 173 MET A SD 1354 C CE A MET A 173 ? 0.2208 0.2133 0.2355 0.0154 0.0317 0.0214 173 MET A CE 1355 C CE B MET A 173 ? 0.2324 0.2242 0.2465 0.0165 0.0328 0.0225 173 MET A CE 1356 N N . THR A 174 ? 0.2194 0.2063 0.2343 0.0156 0.0345 0.0220 174 THR A N 1357 C CA . THR A 174 ? 0.2152 0.2022 0.2309 0.0144 0.0340 0.0207 174 THR A CA 1358 C C . THR A 174 ? 0.2108 0.1966 0.2294 0.0113 0.0347 0.0179 174 THR A C 1359 O O . THR A 174 ? 0.2135 0.1997 0.2329 0.0100 0.0341 0.0165 174 THR A O 1360 C CB . THR A 174 ? 0.2259 0.2106 0.2406 0.0167 0.0365 0.0225 174 THR A CB 1361 O OG1 . THR A 174 ? 0.2246 0.2048 0.2401 0.0171 0.0407 0.0233 174 THR A OG1 1362 C CG2 . THR A 174 ? 0.2233 0.2106 0.2351 0.0199 0.0352 0.0249 174 THR A CG2 1363 N N . GLU A 175 ? 0.2070 0.1918 0.2270 0.0100 0.0361 0.0170 175 GLU A N 1364 C CA . GLU A 175 ? 0.2029 0.1882 0.2256 0.0070 0.0362 0.0139 175 GLU A CA 1365 C C . GLU A 175 ? 0.1935 0.1828 0.2162 0.0058 0.0321 0.0122 175 GLU A C 1366 O O . GLU A 175 ? 0.1969 0.1874 0.2216 0.0035 0.0318 0.0096 175 GLU A O 1367 C CB . GLU A 175 ? 0.2121 0.1968 0.2363 0.0060 0.0378 0.0131 175 GLU A CB 1368 C CG . GLU A 175 ? 0.2437 0.2239 0.2689 0.0061 0.0426 0.0138 175 GLU A CG 1369 C CD . GLU A 175 ? 0.2412 0.2195 0.2687 0.0040 0.0449 0.0117 175 GLU A CD 1370 O OE1 . GLU A 175 ? 0.2844 0.2602 0.3110 0.0053 0.0462 0.0130 175 GLU A OE1 1371 O OE2 . GLU A 175 ? 0.2848 0.2645 0.3150 0.0012 0.0452 0.0085 175 GLU A OE2 1372 N N . LEU A 176 ? 0.1836 0.1750 0.2040 0.0072 0.0292 0.0135 176 LEU A N 1373 C CA . LEU A 176 ? 0.1793 0.1736 0.1994 0.0061 0.0259 0.0122 176 LEU A CA 1374 C C . LEU A 176 ? 0.1830 0.1775 0.2040 0.0051 0.0259 0.0110 176 LEU A C 1375 O O . LEU A 176 ? 0.1720 0.1685 0.1939 0.0035 0.0243 0.0090 176 LEU A O 1376 C CB . LEU A 176 ? 0.1711 0.1671 0.1887 0.0076 0.0233 0.0137 176 LEU A CB 1377 C CG . LEU A 176 ? 0.1663 0.1647 0.1832 0.0065 0.0200 0.0125 176 LEU A CG 1378 C CD1 . LEU A 176 ? 0.1715 0.1709 0.1885 0.0060 0.0189 0.0116 176 LEU A CD1 1379 C CD2 . LEU A 176 ? 0.1698 0.1693 0.1844 0.0076 0.0181 0.0137 176 LEU A CD2 1380 N N . ILE A 177 ? 0.1729 0.1653 0.1935 0.0062 0.0278 0.0123 177 ILE A N 1381 C CA . ILE A 177 ? 0.1791 0.1716 0.2004 0.0055 0.0279 0.0115 177 ILE A CA 1382 C C . ILE A 177 ? 0.1739 0.1664 0.1980 0.0031 0.0290 0.0086 177 ILE A C 1383 O O . ILE A 177 ? 0.1742 0.1692 0.1987 0.0018 0.0270 0.0070 177 ILE A O 1384 C CB . ILE A 177 ? 0.1905 0.1809 0.2107 0.0076 0.0298 0.0135 177 ILE A CB 1385 C CG1 . ILE A 177 ? 0.1980 0.1904 0.2155 0.0097 0.0277 0.0156 177 ILE A CG1 1386 C CG2 . ILE A 177 ? 0.1879 0.1779 0.2090 0.0068 0.0305 0.0124 177 ILE A CG2 1387 C CD1 . ILE A 177 ? 0.2125 0.2035 0.2283 0.0125 0.0296 0.0181 177 ILE A CD1 1388 N N . PRO A 178 ? 0.1707 0.1608 0.1967 0.0023 0.0323 0.0078 178 PRO A N 1389 C CA . PRO A 178 ? 0.1785 0.1695 0.2074 -0.0002 0.0333 0.0046 178 PRO A CA 1390 C C . PRO A 178 ? 0.1772 0.1720 0.2068 -0.0016 0.0309 0.0026 178 PRO A C 1391 O O . PRO A 178 ? 0.1887 0.1859 0.2203 -0.0034 0.0307 -0.0002 178 PRO A O 1392 C CB . PRO A 178 ? 0.1894 0.1764 0.2200 -0.0007 0.0377 0.0043 178 PRO A CB 1393 C CG . PRO A 178 ? 0.1770 0.1620 0.2055 0.0016 0.0382 0.0075 178 PRO A CG 1394 C CD . PRO A 178 ? 0.1854 0.1717 0.2110 0.0038 0.0355 0.0098 178 PRO A CD 1395 N N . GLY A 179 ? 0.1716 0.1673 0.1995 -0.0005 0.0290 0.0040 179 GLY A N 1396 C CA . GLY A 179 ? 0.1708 0.1704 0.1987 -0.0012 0.0262 0.0025 179 GLY A CA 1397 C C . GLY A 179 ? 0.1637 0.1657 0.1906 -0.0013 0.0234 0.0021 179 GLY A C 1398 O O . GLY A 179 ? 0.1764 0.1816 0.2045 -0.0025 0.0224 -0.0002 179 GLY A O 1399 N N . LEU A 180 ? 0.1685 0.1695 0.1931 0.0001 0.0222 0.0044 180 LEU A N 1400 C CA . LEU A 180 ? 0.1584 0.1614 0.1817 0.0001 0.0197 0.0043 180 LEU A CA 1401 C C . LEU A 180 ? 0.1607 0.1644 0.1856 -0.0011 0.0205 0.0026 180 LEU A C 1402 O O . LEU A 180 ? 0.1543 0.1608 0.1792 -0.0017 0.0188 0.0014 180 LEU A O 1403 C CB . LEU A 180 ? 0.1568 0.1586 0.1776 0.0016 0.0188 0.0068 180 LEU A CB 1404 C CG . LEU A 180 ? 0.1623 0.1642 0.1811 0.0027 0.0172 0.0082 180 LEU A CG 1405 C CD1 . LEU A 180 ? 0.1813 0.1825 0.1983 0.0041 0.0170 0.0103 180 LEU A CD1 1406 C CD2 . LEU A 180 ? 0.1611 0.1650 0.1787 0.0022 0.0145 0.0076 180 LEU A CD2 1407 N N . GLN A 181 ? 0.1572 0.1585 0.1834 -0.0011 0.0233 0.0028 181 GLN A N 1408 C CA . GLN A 181 ? 0.1635 0.1650 0.1909 -0.0019 0.0242 0.0015 181 GLN A CA 1409 C C . GLN A 181 ? 0.1723 0.1742 0.2029 -0.0038 0.0264 -0.0015 181 GLN A C 1410 O O . GLN A 181 ? 0.1839 0.1873 0.2158 -0.0048 0.0266 -0.0033 181 GLN A O 1411 C CB . GLN A 181 ? 0.1606 0.1589 0.1872 -0.0005 0.0260 0.0035 181 GLN A CB 1412 C CG . GLN A 181 ? 0.1649 0.1635 0.1886 0.0013 0.0240 0.0061 181 GLN A CG 1413 C CD . GLN A 181 ? 0.1751 0.1717 0.1981 0.0028 0.0256 0.0076 181 GLN A CD 1414 O OE1 . GLN A 181 ? 0.2045 0.1980 0.2285 0.0033 0.0288 0.0079 181 GLN A OE1 1415 N NE2 . GLN A 181 ? 0.1417 0.1400 0.1630 0.0035 0.0238 0.0086 181 GLN A NE2 1416 N N . GLY A 182 ? 0.1816 0.1826 0.2135 -0.0044 0.0281 -0.0022 182 GLY A N 1417 C CA . GLY A 182 ? 0.1968 0.1976 0.2320 -0.0064 0.0311 -0.0052 182 GLY A CA 1418 C C . GLY A 182 ? 0.2056 0.2012 0.2413 -0.0060 0.0349 -0.0040 182 GLY A C 1419 O O . GLY A 182 ? 0.2060 0.1987 0.2398 -0.0042 0.0352 -0.0014 182 GLY A O 1420 N N . ASP A 183 ? 0.2202 0.2146 0.2586 -0.0077 0.0380 -0.0061 183 ASP A N 1421 C CA . ASP A 183 ? 0.2402 0.2289 0.2792 -0.0076 0.0424 -0.0052 183 ASP A CA 1422 C C . ASP A 183 ? 0.2427 0.2293 0.2825 -0.0078 0.0442 -0.0060 183 ASP A C 1423 O O . ASP A 183 ? 0.2503 0.2401 0.2920 -0.0096 0.0435 -0.0090 183 ASP A O 1424 C CB . ASP A 183 ? 0.2453 0.2333 0.2872 -0.0099 0.0455 -0.0078 183 ASP A CB 1425 C CG . ASP A 183 ? 0.2613 0.2496 0.3021 -0.0091 0.0448 -0.0063 183 ASP A CG 1426 O OD1 . ASP A 183 ? 0.3083 0.2935 0.3466 -0.0067 0.0450 -0.0027 183 ASP A OD1 1427 O OD2 . ASP A 183 ? 0.3683 0.3600 0.4110 -0.0109 0.0445 -0.0088 183 ASP A OD2 1428 N N . VAL A 184 ? 0.2463 0.2279 0.2845 -0.0058 0.0464 -0.0032 184 VAL A N 1429 C CA . VAL A 184 ? 0.2729 0.2516 0.3115 -0.0056 0.0487 -0.0035 184 VAL A CA 1430 C C . VAL A 184 ? 0.3205 0.2964 0.3625 -0.0082 0.0532 -0.0067 184 VAL A C 1431 O O . VAL A 184 ? 0.3420 0.3162 0.3852 -0.0094 0.0555 -0.0073 184 VAL A O 1432 C CB . VAL A 184 ? 0.2744 0.2490 0.3099 -0.0022 0.0498 0.0006 184 VAL A CB 1433 C CG1 . VAL A 184 ? 0.2614 0.2395 0.2939 0.0000 0.0454 0.0032 184 VAL A CG1 1434 C CG2 . VAL A 184 ? 0.2726 0.2419 0.3075 -0.0010 0.0535 0.0027 184 VAL A CG2 1435 N N . PRO A 185 ? 0.3439 0.3197 0.3876 -0.0094 0.0544 -0.0090 185 PRO A N 1436 C CA . PRO A 185 ? 0.4085 0.3810 0.4556 -0.0121 0.0592 -0.0123 185 PRO A CA 1437 C C . PRO A 185 ? 0.4611 0.4255 0.5073 -0.0107 0.0642 -0.0098 185 PRO A C 1438 O O . PRO A 185 ? 0.4321 0.3936 0.4750 -0.0073 0.0640 -0.0056 185 PRO A O 1439 C CB . PRO A 185 ? 0.4108 0.3848 0.4592 -0.0129 0.0590 -0.0146 185 PRO A CB 1440 C CG . PRO A 185 ? 0.3729 0.3481 0.4180 -0.0099 0.0556 -0.0113 185 PRO A CG 1441 C CD . PRO A 185 ? 0.3570 0.3355 0.3998 -0.0086 0.0517 -0.0089 185 PRO A CD 1442 N N . LYS A 186 ? 0.5431 0.5040 0.5921 -0.0134 0.0689 -0.0125 186 LYS A N 1443 C CA . LYS A 186 ? 0.5979 0.5505 0.6460 -0.0121 0.0742 -0.0101 186 LYS A CA 1444 C C . LYS A 186 ? 0.5879 0.5352 0.6336 -0.0091 0.0762 -0.0072 186 LYS A C 1445 O O . LYS A 186 ? 0.5959 0.5377 0.6388 -0.0060 0.0785 -0.0032 186 LYS A O 1446 C CB . LYS A 186 ? 0.7044 0.6541 0.7564 -0.0160 0.0793 -0.0141 186 LYS A CB 1447 C CG . LYS A 186 ? 0.7935 0.7411 0.8483 -0.0183 0.0825 -0.0178 186 LYS A CG 1448 C CD . LYS A 186 ? 0.8689 0.8245 0.9273 -0.0219 0.0798 -0.0233 186 LYS A CD 1449 C CE . LYS A 186 ? 0.9099 0.8666 0.9723 -0.0261 0.0828 -0.0276 186 LYS A CE 1450 N NZ . LYS A 186 ? 0.9436 0.9101 1.0077 -0.0279 0.0782 -0.0307 186 LYS A NZ 1451 N N . ASP A 187 ? 0.5766 0.5259 0.6233 -0.0096 0.0751 -0.0093 187 ASP A N 1452 C CA . ASP A 187 ? 0.6594 0.6044 0.7042 -0.0070 0.0768 -0.0073 187 ASP A CA 1453 C C . ASP A 187 ? 0.6071 0.5544 0.6478 -0.0028 0.0728 -0.0029 187 ASP A C 1454 O O . ASP A 187 ? 0.5605 0.5058 0.5995 -0.0004 0.0733 -0.0014 187 ASP A O 1455 C CB . ASP A 187 ? 0.7481 0.6958 0.7958 -0.0096 0.0765 -0.0117 187 ASP A CB 1456 C CG . ASP A 187 ? 0.8251 0.7819 0.8744 -0.0118 0.0712 -0.0146 187 ASP A CG 1457 O OD1 . ASP A 187 ? 0.8719 0.8332 0.9195 -0.0102 0.0669 -0.0134 187 ASP A OD1 1458 O OD2 . ASP A 187 ? 0.8584 0.8181 0.9106 -0.0150 0.0715 -0.0179 187 ASP A OD2 1459 N N . PHE A 188 ? 0.5079 0.4596 0.5471 -0.0020 0.0688 -0.0012 188 PHE A N 1460 C CA . PHE A 188 ? 0.4231 0.3790 0.4592 0.0009 0.0642 0.0016 188 PHE A CA 1461 C C . PHE A 188 ? 0.3868 0.3388 0.4191 0.0054 0.0655 0.0061 188 PHE A C 1462 O O . PHE A 188 ? 0.4132 0.3607 0.4441 0.0073 0.0685 0.0087 188 PHE A O 1463 C CB . PHE A 188 ? 0.3758 0.3367 0.4112 0.0006 0.0601 0.0022 188 PHE A CB 1464 C CG . PHE A 188 ? 0.3399 0.3060 0.3730 0.0023 0.0551 0.0037 188 PHE A CG 1465 C CD1 . PHE A 188 ? 0.3580 0.3290 0.3923 0.0006 0.0520 0.0013 188 PHE A CD1 1466 C CD2 . PHE A 188 ? 0.3364 0.3027 0.3663 0.0055 0.0536 0.0075 188 PHE A CD2 1467 C CE1 . PHE A 188 ? 0.3401 0.3156 0.3723 0.0019 0.0476 0.0027 188 PHE A CE1 1468 C CE2 . PHE A 188 ? 0.3211 0.2923 0.3490 0.0067 0.0492 0.0087 188 PHE A CE2 1469 C CZ . PHE A 188 ? 0.3077 0.2831 0.3368 0.0048 0.0464 0.0063 188 PHE A CZ 1470 N N . THR A 189 ? 0.3461 0.3006 0.3768 0.0074 0.0632 0.0071 189 THR A N 1471 C CA . THR A 189 ? 0.3413 0.2938 0.3683 0.0120 0.0639 0.0113 189 THR A CA 1472 C C . THR A 189 ? 0.3060 0.2632 0.3303 0.0141 0.0598 0.0140 189 THR A C 1473 O O . THR A 189 ? 0.3018 0.2651 0.3262 0.0131 0.0552 0.0130 189 THR A O 1474 C CB . THR A 189 ? 0.3495 0.3027 0.3759 0.0133 0.0635 0.0111 189 THR A CB 1475 O OG1 . THR A 189 ? 0.3987 0.3468 0.4274 0.0117 0.0678 0.0087 189 THR A OG1 1476 C CG2 . THR A 189 ? 0.3688 0.3209 0.3913 0.0184 0.0640 0.0153 189 THR A CG2 1477 N N . SER A 190 ? 0.2963 0.2508 0.3184 0.0170 0.0616 0.0173 190 SER A N 1478 C CA . SER A 190 ? 0.2795 0.2384 0.2990 0.0192 0.0581 0.0198 190 SER A CA 1479 C C . SER A 190 ? 0.2810 0.2450 0.2988 0.0210 0.0546 0.0205 190 SER A C 1480 O O . SER A 190 ? 0.2885 0.2510 0.3050 0.0233 0.0562 0.0215 190 SER A O 1481 C CB . SER A 190 ? 0.3029 0.2581 0.3198 0.0229 0.0612 0.0235 190 SER A CB 1482 O OG . SER A 190 ? 0.2872 0.2471 0.3019 0.0249 0.0579 0.0255 190 SER A OG 1483 N N . GLY A 191 ? 0.2388 0.2086 0.2562 0.0199 0.0500 0.0200 191 GLY A N 1484 C CA . GLY A 191 ? 0.2485 0.2237 0.2645 0.0211 0.0465 0.0204 191 GLY A CA 1485 C C . GLY A 191 ? 0.2421 0.2204 0.2601 0.0179 0.0439 0.0173 191 GLY A C 1486 O O . GLY A 191 ? 0.2380 0.2212 0.2550 0.0180 0.0405 0.0173 191 GLY A O 1487 N N . MET A 192 ? 0.2413 0.2171 0.2620 0.0151 0.0456 0.0147 192 MET A N 1488 C CA . MET A 192 ? 0.2405 0.2198 0.2631 0.0121 0.0431 0.0117 192 MET A CA 1489 C C . MET A 192 ? 0.2321 0.2154 0.2551 0.0100 0.0395 0.0108 192 MET A C 1490 O O . MET A 192 ? 0.2481 0.2302 0.2711 0.0099 0.0399 0.0114 192 MET A O 1491 C CB . MET A 192 ? 0.2702 0.2464 0.2957 0.0098 0.0459 0.0089 192 MET A CB 1492 C CG . MET A 192 ? 0.2772 0.2500 0.3025 0.0116 0.0490 0.0093 192 MET A CG 1493 S SD . MET A 192 ? 0.3106 0.2883 0.3349 0.0123 0.0459 0.0090 192 MET A SD 1494 C CE . MET A 192 ? 0.3112 0.2917 0.3389 0.0080 0.0446 0.0046 192 MET A CE 1495 N N . PRO A 193 ? 0.2159 0.2036 0.2391 0.0086 0.0362 0.0094 193 PRO A N 1496 C CA . PRO A 193 ? 0.1993 0.1904 0.2228 0.0067 0.0330 0.0085 193 PRO A CA 1497 C C . PRO A 193 ? 0.2175 0.2083 0.2438 0.0038 0.0338 0.0055 193 PRO A C 1498 O O . PRO A 193 ? 0.2344 0.2241 0.2627 0.0027 0.0357 0.0035 193 PRO A O 1499 C CB . PRO A 193 ? 0.2004 0.1959 0.2228 0.0064 0.0297 0.0083 193 PRO A CB 1500 C CG . PRO A 193 ? 0.1979 0.1928 0.2211 0.0067 0.0313 0.0075 193 PRO A CG 1501 C CD . PRO A 193 ? 0.2165 0.2066 0.2392 0.0090 0.0350 0.0091 193 PRO A CD 1502 N N . PHE A 194 ? 0.1930 0.1853 0.2197 0.0026 0.0323 0.0049 194 PHE A N 1503 C CA . PHE A 194 ? 0.2049 0.1981 0.2342 0.0000 0.0326 0.0019 194 PHE A CA 1504 C C . PHE A 194 ? 0.1905 0.1874 0.2192 -0.0010 0.0293 0.0014 194 PHE A C 1505 O O . PHE A 194 ? 0.2014 0.1982 0.2284 0.0001 0.0281 0.0033 194 PHE A O 1506 C CB . PHE A 194 ? 0.2258 0.2151 0.2567 -0.0005 0.0362 0.0015 194 PHE A CB 1507 C CG . PHE A 194 ? 0.2399 0.2308 0.2737 -0.0033 0.0368 -0.0020 194 PHE A CG 1508 C CD1 . PHE A 194 ? 0.2551 0.2460 0.2915 -0.0050 0.0387 -0.0049 194 PHE A CD1 1509 C CD2 . PHE A 194 ? 0.2315 0.2246 0.2657 -0.0042 0.0354 -0.0027 194 PHE A CD2 1510 C CE1 . PHE A 194 ? 0.2768 0.2701 0.3161 -0.0076 0.0392 -0.0085 194 PHE A CE1 1511 C CE2 . PHE A 194 ? 0.2418 0.2373 0.2788 -0.0066 0.0358 -0.0061 194 PHE A CE2 1512 C CZ . PHE A 194 ? 0.2524 0.2483 0.2920 -0.0084 0.0377 -0.0091 194 PHE A CZ 1513 N N . VAL A 195 ? 0.1900 0.1903 0.2203 -0.0028 0.0280 -0.0012 195 VAL A N 1514 C CA . VAL A 195 ? 0.1784 0.1820 0.2087 -0.0037 0.0257 -0.0021 195 VAL A CA 1515 C C . VAL A 195 ? 0.1946 0.2006 0.2278 -0.0058 0.0265 -0.0057 195 VAL A C 1516 O O . VAL A 195 ? 0.1981 0.2051 0.2324 -0.0065 0.0270 -0.0073 195 VAL A O 1517 C CB . VAL A 195 ? 0.1737 0.1802 0.2016 -0.0031 0.0222 -0.0010 195 VAL A CB 1518 C CG1 . VAL A 195 ? 0.1825 0.1919 0.2101 -0.0037 0.0201 -0.0019 195 VAL A CG1 1519 C CG2 . VAL A 195 ? 0.1860 0.1907 0.2112 -0.0013 0.0214 0.0021 195 VAL A CG2 1520 N N . ALA A 196 ? 0.1897 0.1972 0.2242 -0.0068 0.0266 -0.0073 196 ALA A N 1521 C CA . ALA A 196 ? 0.2060 0.2162 0.2436 -0.0088 0.0279 -0.0111 196 ALA A CA 1522 C C . ALA A 196 ? 0.2393 0.2549 0.2771 -0.0094 0.0255 -0.0131 196 ALA A C 1523 O O . ALA A 196 ? 0.2693 0.2874 0.3099 -0.0110 0.0268 -0.0163 196 ALA A O 1524 C CB . ALA A 196 ? 0.2117 0.2222 0.2508 -0.0098 0.0290 -0.0124 196 ALA A CB 1525 N N . GLY A 197 ? 0.2199 0.2375 0.2551 -0.0082 0.0224 -0.0113 197 GLY A N 1526 C CA . GLY A 197 ? 0.2126 0.2353 0.2475 -0.0084 0.0201 -0.0127 197 GLY A CA 1527 C C . GLY A 197 ? 0.2306 0.2547 0.2626 -0.0070 0.0172 -0.0107 197 GLY A C 1528 O O . GLY A 197 ? 0.2040 0.2248 0.2339 -0.0060 0.0167 -0.0080 197 GLY A O 1529 N N . LYS A 198 ? 0.2172 0.2461 0.2489 -0.0069 0.0155 -0.0121 198 LYS A N 1530 C CA . LYS A 198 ? 0.2191 0.2490 0.2475 -0.0054 0.0128 -0.0100 198 LYS A CA 1531 C C . LYS A 198 ? 0.2067 0.2357 0.2340 -0.0046 0.0122 -0.0090 198 LYS A C 1532 O O . LYS A 198 ? 0.2072 0.2357 0.2315 -0.0033 0.0103 -0.0069 198 LYS A O 1533 C CB . LYS A 198 ? 0.2097 0.2451 0.2380 -0.0052 0.0114 -0.0117 198 LYS A CB 1534 C CG . LYS A 198 ? 0.2434 0.2839 0.2737 -0.0055 0.0116 -0.0148 198 LYS A CG 1535 C CD . LYS A 198 ? 0.2762 0.3226 0.3065 -0.0052 0.0105 -0.0166 198 LYS A CD 1536 C CE . LYS A 198 ? 0.3487 0.4009 0.3810 -0.0053 0.0107 -0.0199 198 LYS A CE 1537 N NZ . LYS A 198 ? 0.4386 0.4974 0.4700 -0.0040 0.0090 -0.0210 198 LYS A NZ 1538 N N . ASN A 199 ? 0.2035 0.2322 0.2330 -0.0054 0.0138 -0.0105 199 ASN A N 1539 C CA . ASN A 199 ? 0.2116 0.2395 0.2401 -0.0046 0.0133 -0.0096 199 ASN A CA 1540 C C . ASN A 199 ? 0.1979 0.2206 0.2256 -0.0043 0.0142 -0.0072 199 ASN A C 1541 O O . ASN A 199 ? 0.2218 0.2434 0.2489 -0.0037 0.0141 -0.0064 199 ASN A O 1542 C CB . ASN A 199 ? 0.2593 0.2913 0.2904 -0.0054 0.0141 -0.0128 199 ASN A CB 1543 C CG . ASN A 199 ? 0.2953 0.3335 0.3267 -0.0052 0.0128 -0.0150 199 ASN A CG 1544 O OD1 . ASN A 199 ? 0.3985 0.4408 0.4330 -0.0066 0.0141 -0.0184 199 ASN A OD1 1545 N ND2 . ASN A 199 ? 0.2790 0.3182 0.3073 -0.0034 0.0106 -0.0132 199 ASN A ND2 1546 N N . LYS A 200 ? 0.1832 0.2028 0.2109 -0.0045 0.0152 -0.0060 200 LYS A N 1547 C CA . LYS A 200 ? 0.1729 0.1880 0.1997 -0.0039 0.0163 -0.0037 200 LYS A CA 1548 C C . LYS A 200 ? 0.1605 0.1743 0.1848 -0.0030 0.0148 -0.0013 200 LYS A C 1549 O O . LYS A 200 ? 0.1651 0.1810 0.1886 -0.0031 0.0134 -0.0017 200 LYS A O 1550 C CB . LYS A 200 ? 0.1663 0.1791 0.1956 -0.0048 0.0194 -0.0046 200 LYS A CB 1551 C CG . LYS A 200 ? 0.1809 0.1946 0.2130 -0.0061 0.0213 -0.0071 200 LYS A CG 1552 C CD . LYS A 200 ? 0.1967 0.2092 0.2279 -0.0053 0.0211 -0.0058 200 LYS A CD 1553 C CE . LYS A 200 ? 0.1961 0.2094 0.2302 -0.0067 0.0234 -0.0082 200 LYS A CE 1554 N NZ . LYS A 200 ? 0.1867 0.1987 0.2198 -0.0059 0.0233 -0.0068 200 LYS A NZ 1555 N N . VAL A 201 ? 0.1606 0.1714 0.1835 -0.0021 0.0151 0.0009 201 VAL A N 1556 C CA . VAL A 201 ? 0.1555 0.1654 0.1761 -0.0014 0.0139 0.0029 201 VAL A CA 1557 C C . VAL A 201 ? 0.1642 0.1717 0.1851 -0.0007 0.0156 0.0041 201 VAL A C 1558 O O . VAL A 201 ? 0.1638 0.1692 0.1858 -0.0005 0.0177 0.0042 201 VAL A O 1559 C CB . VAL A 201 ? 0.1490 0.1584 0.1671 -0.0006 0.0120 0.0045 201 VAL A CB 1560 C CG1 . VAL A 201 ? 0.1578 0.1693 0.1751 -0.0007 0.0104 0.0036 201 VAL A CG1 1561 C CG2 . VAL A 201 ? 0.1656 0.1730 0.1836 0.0002 0.0128 0.0055 201 VAL A CG2 1562 N N . ALA A 202 ? 0.1455 0.1532 0.1652 -0.0004 0.0150 0.0050 202 ALA A N 1563 C CA . ALA A 202 ? 0.1439 0.1498 0.1631 0.0008 0.0163 0.0066 202 ALA A CA 1564 C C . ALA A 202 ? 0.1495 0.1545 0.1671 0.0020 0.0159 0.0084 202 ALA A C 1565 O O . ALA A 202 ? 0.1536 0.1594 0.1695 0.0018 0.0138 0.0087 202 ALA A O 1566 C CB . ALA A 202 ? 0.1562 0.1635 0.1743 0.0010 0.0154 0.0071 202 ALA A CB 1567 N N . ALA A 203 ? 0.1493 0.1522 0.1670 0.0033 0.0178 0.0095 203 ALA A N 1568 C CA . ALA A 203 ? 0.1452 0.1477 0.1614 0.0047 0.0176 0.0112 203 ALA A CA 1569 C C . ALA A 203 ? 0.1516 0.1548 0.1662 0.0063 0.0175 0.0128 203 ALA A C 1570 O O . ALA A 203 ? 0.1654 0.1694 0.1801 0.0063 0.0178 0.0126 203 ALA A O 1571 C CB . ALA A 203 ? 0.1552 0.1552 0.1725 0.0052 0.0198 0.0114 203 ALA A CB 1572 N N . CYS A 204 ? 0.1563 0.1600 0.1695 0.0077 0.0172 0.0142 204 CYS A N 1573 C CA . CYS A 204 ? 0.1561 0.1616 0.1676 0.0093 0.0169 0.0154 204 CYS A CA 1574 C C . CYS A 204 ? 0.1604 0.1656 0.1710 0.0114 0.0178 0.0169 204 CYS A C 1575 O O . CYS A 204 ? 0.1630 0.1688 0.1730 0.0111 0.0166 0.0169 204 CYS A O 1576 C CB . CYS A 204 ? 0.1605 0.1686 0.1708 0.0081 0.0143 0.0148 204 CYS A CB 1577 S SG . CYS A 204 ? 0.1821 0.1939 0.1907 0.0097 0.0137 0.0157 204 CYS A SG 1578 N N . ALA A 205 ? 0.1705 0.1748 0.1809 0.0136 0.0200 0.0183 205 ALA A N 1579 C CA . ALA A 205 ? 0.1628 0.1674 0.1719 0.0160 0.0210 0.0200 205 ALA A CA 1580 C C . ALA A 205 ? 0.1700 0.1791 0.1774 0.0171 0.0191 0.0204 205 ALA A C 1581 O O . ALA A 205 ? 0.1779 0.1890 0.1848 0.0177 0.0189 0.0204 205 ALA A O 1582 C CB . ALA A 205 ? 0.1753 0.1773 0.1845 0.0183 0.0242 0.0216 205 ALA A CB 1583 N N . LYS A 206 ? 0.1693 0.1801 0.1757 0.0174 0.0179 0.0205 206 LYS A N 1584 C CA . LYS A 206 ? 0.1686 0.1842 0.1736 0.0179 0.0161 0.0202 206 LYS A CA 1585 C C . LYS A 206 ? 0.1761 0.1936 0.1799 0.0200 0.0162 0.0212 206 LYS A C 1586 O O . LYS A 206 ? 0.1810 0.1960 0.1852 0.0203 0.0171 0.0218 206 LYS A O 1587 C CB . LYS A 206 ? 0.1625 0.1790 0.1677 0.0148 0.0136 0.0183 206 LYS A CB 1588 C CG . LYS A 206 ? 0.1725 0.1877 0.1778 0.0134 0.0125 0.0176 206 LYS A CG 1589 C CD . LYS A 206 ? 0.1643 0.1795 0.1696 0.0106 0.0106 0.0160 206 LYS A CD 1590 C CE . LYS A 206 ? 0.1531 0.1672 0.1580 0.0097 0.0096 0.0154 206 LYS A CE 1591 N NZ . LYS A 206 ? 0.1508 0.1641 0.1553 0.0072 0.0081 0.0141 206 LYS A NZ 1592 N N . HIS A 207 ? 0.1743 0.1968 0.1768 0.0215 0.0153 0.0213 207 HIS A N 1593 C CA . HIS A 207 ? 0.1827 0.2091 0.1848 0.0216 0.0146 0.0206 207 HIS A CA 1594 C C . HIS A 207 ? 0.1822 0.2108 0.1831 0.0255 0.0164 0.0225 207 HIS A C 1595 O O . HIS A 207 ? 0.2008 0.2313 0.2005 0.0281 0.0170 0.0237 207 HIS A O 1596 C CB . HIS A 207 ? 0.1801 0.2112 0.1815 0.0202 0.0123 0.0189 207 HIS A CB 1597 C CG . HIS A 207 ? 0.1783 0.2071 0.1804 0.0170 0.0109 0.0174 207 HIS A CG 1598 N ND1 . HIS A 207 ? 0.1949 0.2226 0.1968 0.0172 0.0107 0.0175 207 HIS A ND1 1599 C CD2 . HIS A 207 ? 0.1825 0.2099 0.1851 0.0139 0.0097 0.0159 207 HIS A CD2 1600 C CE1 . HIS A 207 ? 0.1858 0.2114 0.1881 0.0144 0.0094 0.0161 207 HIS A CE1 1601 N NE2 . HIS A 207 ? 0.1821 0.2073 0.1847 0.0124 0.0088 0.0152 207 HIS A NE2 1602 N N . PHE A 208 ? 0.1836 0.2119 0.1846 0.0262 0.0173 0.0229 208 PHE A N 1603 C CA . PHE A 208 ? 0.1875 0.2160 0.1873 0.0302 0.0195 0.0250 208 PHE A CA 1604 C C . PHE A 208 ? 0.1928 0.2288 0.1910 0.0325 0.0186 0.0250 208 PHE A C 1605 O O . PHE A 208 ? 0.2022 0.2421 0.2007 0.0311 0.0169 0.0233 208 PHE A O 1606 C CB . PHE A 208 ? 0.1958 0.2209 0.1966 0.0296 0.0208 0.0251 208 PHE A CB 1607 C CG . PHE A 208 ? 0.2062 0.2308 0.2057 0.0337 0.0235 0.0273 208 PHE A CG 1608 C CD1 . PHE A 208 ? 0.2016 0.2205 0.2011 0.0354 0.0265 0.0292 208 PHE A CD1 1609 C CD2 . PHE A 208 ? 0.1990 0.2286 0.1973 0.0358 0.0230 0.0274 208 PHE A CD2 1610 C CE1 . PHE A 208 ? 0.2169 0.2345 0.2149 0.0394 0.0293 0.0314 208 PHE A CE1 1611 C CE2 . PHE A 208 ? 0.2060 0.2350 0.2029 0.0400 0.0256 0.0296 208 PHE A CE2 1612 C CZ . PHE A 208 ? 0.2193 0.2419 0.2159 0.0418 0.0288 0.0317 208 PHE A CZ 1613 N N . VAL A 209 ? 0.1870 0.2258 0.1836 0.0362 0.0195 0.0266 209 VAL A N 1614 C CA . VAL A 209 ? 0.1985 0.2337 0.1946 0.0383 0.0215 0.0286 209 VAL A CA 1615 C C . VAL A 209 ? 0.2041 0.2453 0.1987 0.0405 0.0206 0.0287 209 VAL A C 1616 O O . VAL A 209 ? 0.2291 0.2774 0.2229 0.0415 0.0192 0.0277 209 VAL A O 1617 C CB . VAL A 209 ? 0.1972 0.2287 0.1922 0.0420 0.0248 0.0314 209 VAL A CB 1618 C CG1 . VAL A 209 ? 0.2182 0.2557 0.2112 0.0461 0.0252 0.0324 209 VAL A CG1 1619 C CG2 . VAL A 209 ? 0.2110 0.2382 0.2054 0.0440 0.0274 0.0336 209 VAL A CG2 1620 N N . GLY A 210 ? 0.2176 0.2565 0.2121 0.0408 0.0212 0.0295 210 GLY A N 1621 C CA . GLY A 210 ? 0.2259 0.2708 0.2191 0.0429 0.0203 0.0296 210 GLY A CA 1622 C C . GLY A 210 ? 0.2245 0.2726 0.2186 0.0395 0.0175 0.0266 210 GLY A C 1623 O O . GLY A 210 ? 0.2336 0.2880 0.2269 0.0407 0.0164 0.0258 210 GLY A O 1624 N N . ASP A 211 ? 0.2154 0.2592 0.2114 0.0351 0.0163 0.0249 211 ASP A N 1625 C CA . ASP A 211 ? 0.2105 0.2560 0.2072 0.0317 0.0139 0.0223 211 ASP A CA 1626 C C . ASP A 211 ? 0.2099 0.2559 0.2062 0.0323 0.0137 0.0224 211 ASP A C 1627 O O . ASP A 211 ? 0.2190 0.2690 0.2154 0.0310 0.0120 0.0203 211 ASP A O 1628 C CB . ASP A 211 ? 0.2039 0.2442 0.2023 0.0274 0.0130 0.0209 211 ASP A CB 1629 C CG . ASP A 211 ? 0.1971 0.2302 0.1964 0.0269 0.0146 0.0223 211 ASP A CG 1630 O OD1 . ASP A 211 ? 0.2092 0.2403 0.2079 0.0297 0.0168 0.0245 211 ASP A OD1 1631 O OD2 . ASP A 211 ? 0.1949 0.2243 0.1954 0.0236 0.0137 0.0210 211 ASP A OD2 1632 N N . GLY A 212 ? 0.2282 0.2703 0.2242 0.0344 0.0157 0.0247 212 GLY A N 1633 C CA . GLY A 212 ? 0.2325 0.2752 0.2280 0.0353 0.0157 0.0250 212 GLY A CA 1634 C C . GLY A 212 ? 0.2634 0.3127 0.2571 0.0395 0.0162 0.0261 212 GLY A C 1635 O O . GLY A 212 ? 0.2492 0.2994 0.2423 0.0410 0.0164 0.0267 212 GLY A O 1636 N N . GLY A 213 ? 0.2567 0.3108 0.2494 0.0418 0.0163 0.0264 213 GLY A N 1637 C CA . GLY A 213 ? 0.3210 0.3814 0.3118 0.0466 0.0172 0.0279 213 GLY A CA 1638 C C . GLY A 213 ? 0.4279 0.4967 0.4184 0.0465 0.0151 0.0254 213 GLY A C 1639 O O . GLY A 213 ? 0.4835 0.5569 0.4726 0.0499 0.0155 0.0263 213 GLY A O 1640 N N . THR A 214 ? 0.5181 0.5887 0.5099 0.0426 0.0129 0.0222 214 THR A N 1641 C CA . THR A 214 ? 0.7254 0.8053 0.7171 0.0424 0.0112 0.0194 214 THR A CA 1642 C C . THR A 214 ? 0.8570 0.9444 0.8479 0.0444 0.0105 0.0183 214 THR A C 1643 O O . THR A 214 ? 0.9527 1.0376 0.9436 0.0443 0.0106 0.0186 214 THR A O 1644 C CB . THR A 214 ? 0.7263 0.8054 0.7197 0.0371 0.0094 0.0160 214 THR A CB 1645 O OG1 . THR A 214 ? 0.7676 0.8408 0.7622 0.0335 0.0087 0.0149 214 THR A OG1 1646 C CG2 . THR A 214 ? 0.6861 0.7616 0.6800 0.0362 0.0099 0.0168 214 THR A CG2 1647 N N . VAL A 215 ? 0.9318 1.0289 0.9220 0.0464 0.0099 0.0168 215 VAL A N 1648 C CA . VAL A 215 ? 0.9902 1.0964 0.9798 0.0483 0.0091 0.0151 215 VAL A CA 1649 C C . VAL A 215 ? 1.0527 1.1585 1.0439 0.0436 0.0074 0.0114 215 VAL A C 1650 O O . VAL A 215 ? 1.0007 1.1048 0.9934 0.0391 0.0063 0.0087 215 VAL A O 1651 C CB . VAL A 215 ? 0.9505 1.0680 0.9392 0.0509 0.0086 0.0136 215 VAL A CB 1652 C CG1 . VAL A 215 ? 0.9252 1.0529 0.9136 0.0525 0.0076 0.0112 215 VAL A CG1 1653 C CG2 . VAL A 215 ? 0.9392 1.0571 0.9259 0.0562 0.0105 0.0174 215 VAL A CG2 1654 N N . ASP A 216 ? 1.1448 1.2517 1.1355 0.0448 0.0073 0.0115 216 ASP A N 1655 C CA . ASP A 216 ? 1.1583 1.2640 1.1503 0.0410 0.0060 0.0084 216 ASP A CA 1656 C C . ASP A 216 ? 1.1284 1.2232 1.1217 0.0368 0.0059 0.0087 216 ASP A C 1657 O O . ASP A 216 ? 1.0653 1.1582 1.0596 0.0333 0.0048 0.0061 216 ASP A O 1658 C CB . ASP A 216 ? 1.1693 1.2833 1.1624 0.0384 0.0044 0.0037 216 ASP A CB 1659 C CG . ASP A 216 ? 1.2064 1.3326 1.1985 0.0424 0.0043 0.0027 216 ASP A CG 1660 O OD1 . ASP A 216 ? 1.2098 1.3386 1.2007 0.0458 0.0047 0.0041 216 ASP A OD1 1661 O OD2 . ASP A 216 ? 1.2145 1.3480 1.2068 0.0422 0.0038 0.0005 216 ASP A OD2 1662 N N . GLY A 217 ? 1.1219 1.2098 1.1150 0.0373 0.0071 0.0117 217 GLY A N 1663 C CA . GLY A 217 ? 1.0850 1.1635 1.0793 0.0335 0.0069 0.0119 217 GLY A CA 1664 C C . GLY A 217 ? 1.1226 1.2012 1.1181 0.0293 0.0057 0.0088 217 GLY A C 1665 O O . GLY A 217 ? 1.1186 1.1906 1.1149 0.0258 0.0053 0.0081 217 GLY A O 1666 N N . ILE A 218 ? 1.1456 1.2317 1.1409 0.0297 0.0053 0.0071 218 ILE A N 1667 C CA . ILE A 218 ? 1.1376 1.2247 1.1340 0.0257 0.0043 0.0041 218 ILE A CA 1668 C C . ILE A 218 ? 1.1551 1.2360 1.1518 0.0245 0.0048 0.0058 218 ILE A C 1669 O O . ILE A 218 ? 1.1876 1.2697 1.1837 0.0273 0.0057 0.0079 218 ILE A O 1670 C CB . ILE A 218 ? 1.0864 1.1844 1.0828 0.0263 0.0037 0.0012 218 ILE A CB 1671 C CG1 . ILE A 218 ? 1.0375 1.1414 1.0340 0.0264 0.0030 -0.0014 218 ILE A CG1 1672 C CG2 . ILE A 218 ? 1.0533 1.1517 1.0509 0.0221 0.0031 -0.0016 218 ILE A CG2 1673 C CD1 . ILE A 218 ? 0.9981 1.1139 0.9947 0.0274 0.0025 -0.0044 218 ILE A CD1 1674 N N . ASN A 219 ? 1.0906 1.1649 1.0882 0.0205 0.0044 0.0048 219 ASN A N 1675 C CA . ASN A 219 ? 0.9898 1.0580 0.9879 0.0187 0.0047 0.0059 219 ASN A CA 1676 C C . ASN A 219 ? 1.0723 1.1448 1.0706 0.0182 0.0046 0.0050 219 ASN A C 1677 O O . ASN A 219 ? 1.0879 1.1671 1.0865 0.0170 0.0039 0.0021 219 ASN A O 1678 C CB . ASN A 219 ? 0.7788 0.8406 0.7775 0.0146 0.0041 0.0045 219 ASN A CB 1679 C CG . ASN A 219 ? 0.7074 0.7624 0.7065 0.0130 0.0044 0.0059 219 ASN A CG 1680 O OD1 . ASN A 219 ? 0.4237 0.4743 0.4228 0.0145 0.0051 0.0083 219 ASN A OD1 1681 N ND2 . ASN A 219 ? 0.7760 0.8301 0.7755 0.0097 0.0039 0.0040 219 ASN A ND2 1682 N N . GLU A 220 ? 1.0907 1.1598 1.0890 0.0190 0.0053 0.0071 220 GLU A N 1683 C CA . GLU A 220 ? 1.0457 1.1182 1.0442 0.0186 0.0052 0.0064 220 GLU A CA 1684 C C . GLU A 220 ? 1.0375 1.1199 1.0354 0.0215 0.0052 0.0057 220 GLU A C 1685 O O . GLU A 220 ? 1.1013 1.1894 1.0996 0.0199 0.0046 0.0032 220 GLU A O 1686 C CB . GLU A 220 ? 1.0356 1.1069 1.0350 0.0138 0.0044 0.0037 220 GLU A CB 1687 C CG . GLU A 220 ? 1.0700 1.1325 1.0698 0.0109 0.0043 0.0041 220 GLU A CG 1688 C CD . GLU A 220 ? 1.1230 1.1845 1.1232 0.0065 0.0037 0.0013 220 GLU A CD 1689 O OE1 . GLU A 220 ? 1.1204 1.1862 1.1210 0.0051 0.0036 -0.0002 220 GLU A OE1 1690 O OE2 . GLU A 220 ? 1.0627 1.1192 1.0629 0.0044 0.0035 0.0008 220 GLU A OE2 1691 N N . ASN A 221 ? 0.9303 1.0149 0.9270 0.0259 0.0060 0.0078 221 ASN A N 1692 C CA . ASN A 221 ? 0.8378 0.9325 0.8336 0.0292 0.0059 0.0070 221 ASN A CA 1693 C C . ASN A 221 ? 0.7342 0.8303 0.7285 0.0347 0.0073 0.0105 221 ASN A C 1694 O O . ASN A 221 ? 0.6338 0.7243 0.6280 0.0354 0.0084 0.0128 221 ASN A O 1695 C CB . ASN A 221 ? 0.8960 0.9946 0.8919 0.0292 0.0052 0.0053 221 ASN A CB 1696 C CG . ASN A 221 ? 0.9621 1.0717 0.9582 0.0289 0.0043 0.0017 221 ASN A CG 1697 O OD1 . ASN A 221 ? 0.9983 1.1136 0.9940 0.0304 0.0040 0.0005 221 ASN A OD1 1698 N ND2 . ASN A 221 ? 0.9730 1.0860 0.9697 0.0269 0.0039 -0.0002 221 ASN A ND2 1699 N N . ASN A 222 ? 0.7066 0.8101 0.6996 0.0387 0.0075 0.0108 222 ASN A N 1700 C CA . ASN A 222 ? 0.7045 0.8102 0.6956 0.0444 0.0091 0.0140 222 ASN A CA 1701 C C . ASN A 222 ? 0.6825 0.7826 0.6725 0.0475 0.0107 0.0175 222 ASN A C 1702 O O . ASN A 222 ? 0.6884 0.7907 0.6780 0.0482 0.0104 0.0172 222 ASN A O 1703 C CB . ASN A 222 ? 0.7102 0.8285 0.7003 0.0477 0.0086 0.0125 222 ASN A CB 1704 C CG . ASN A 222 ? 0.7497 0.8713 0.7380 0.0528 0.0099 0.0151 222 ASN A CG 1705 O OD1 . ASN A 222 ? 0.7413 0.8556 0.7292 0.0536 0.0113 0.0178 222 ASN A OD1 1706 N ND2 . ASN A 222 ? 0.7252 0.8582 0.7123 0.0564 0.0096 0.0141 222 ASN A ND2 1707 N N . THR A 223 ? 0.6079 0.7005 0.5973 0.0490 0.0126 0.0208 223 THR A N 1708 C CA . THR A 223 ? 0.6177 0.7059 0.6058 0.0526 0.0147 0.0243 223 THR A CA 1709 C C . THR A 223 ? 0.6012 0.6950 0.5867 0.0589 0.0163 0.0268 223 THR A C 1710 O O . THR A 223 ? 0.5921 0.6855 0.5771 0.0606 0.0173 0.0280 223 THR A O 1711 C CB . THR A 223 ? 0.6464 0.7231 0.6353 0.0509 0.0162 0.0264 223 THR A CB 1712 O OG1 . THR A 223 ? 0.7407 0.8148 0.7288 0.0531 0.0180 0.0285 223 THR A OG1 1713 C CG2 . THR A 223 ? 0.5512 0.6234 0.5424 0.0449 0.0145 0.0238 223 THR A CG2 1714 N N . ILE A 224 ? 0.6397 0.7391 0.6237 0.0625 0.0165 0.0275 224 ILE A N 1715 C CA . ILE A 224 ? 0.6486 0.7537 0.6298 0.0692 0.0182 0.0302 224 ILE A CA 1716 C C . ILE A 224 ? 0.6310 0.7286 0.6106 0.0725 0.0212 0.0346 224 ILE A C 1717 O O . ILE A 224 ? 0.6435 0.7393 0.6231 0.0722 0.0213 0.0349 224 ILE A O 1718 C CB . ILE A 224 ? 0.7058 0.8237 0.6860 0.0717 0.0168 0.0282 224 ILE A CB 1719 C CG1 . ILE A 224 ? 0.7277 0.8520 0.7102 0.0669 0.0138 0.0232 224 ILE A CG1 1720 C CG2 . ILE A 224 ? 0.7049 0.8295 0.6820 0.0788 0.0184 0.0308 224 ILE A CG2 1721 C CD1 . ILE A 224 ? 0.7877 0.9241 0.7700 0.0679 0.0122 0.0202 224 ILE A CD1 1722 N N . ILE A 225 ? 0.5793 0.6720 0.5575 0.0755 0.0237 0.0377 225 ILE A N 1723 C CA . ILE A 225 ? 0.5534 0.6383 0.5299 0.0787 0.0272 0.0419 225 ILE A CA 1724 C C . ILE A 225 ? 0.5655 0.6482 0.5401 0.0828 0.0297 0.0448 225 ILE A C 1725 O O . ILE A 225 ? 0.5275 0.6105 0.5031 0.0809 0.0288 0.0432 225 ILE A O 1726 C CB . ILE A 225 ? 0.5442 0.6181 0.5230 0.0738 0.0277 0.0418 225 ILE A CB 1727 C CG1 . ILE A 225 ? 0.5088 0.5761 0.4861 0.0768 0.0311 0.0457 225 ILE A CG1 1728 C CG2 . ILE A 225 ? 0.5044 0.5720 0.4853 0.0697 0.0275 0.0407 225 ILE A CG2 1729 C CD1 . ILE A 225 ? 0.5535 0.6126 0.5330 0.0721 0.0312 0.0450 225 ILE A CD1 1730 N N . ASN A 226 ? 0.5377 0.6184 0.5094 0.0885 0.0331 0.0489 226 ASN A N 1731 C CA . ASN A 226 ? 0.5722 0.6495 0.5419 0.0924 0.0359 0.0517 226 ASN A CA 1732 C C . ASN A 226 ? 0.5697 0.6349 0.5414 0.0887 0.0377 0.0522 226 ASN A C 1733 O O . ASN A 226 ? 0.5051 0.5641 0.4792 0.0836 0.0371 0.0509 226 ASN A O 1734 C CB . ASN A 226 ? 0.6179 0.6966 0.5835 0.1002 0.0393 0.0562 226 ASN A CB 1735 C CG . ASN A 226 ? 0.6868 0.7586 0.6517 0.1008 0.0418 0.0588 226 ASN A CG 1736 O OD1 . ASN A 226 ? 0.6667 0.7328 0.6344 0.0955 0.0410 0.0573 226 ASN A OD1 1737 N ND2 . ASN A 226 ? 0.6922 0.7649 0.6534 0.1077 0.0449 0.0630 226 ASN A ND2 1738 N N . ARG A 227 ? 0.5696 0.6319 0.5401 0.0911 0.0398 0.0539 227 ARG A N 1739 C CA . ARG A 227 ? 0.5918 0.6429 0.5639 0.0880 0.0419 0.0544 227 ARG A CA 1740 C C . ARG A 227 ? 0.5955 0.6370 0.5678 0.0873 0.0450 0.0565 227 ARG A C 1741 O O . ARG A 227 ? 0.5220 0.5566 0.4972 0.0821 0.0449 0.0550 227 ARG A O 1742 C CB . ARG A 227 ? 0.6402 0.6894 0.6105 0.0919 0.0444 0.0564 227 ARG A CB 1743 C CG . ARG A 227 ? 0.7256 0.7661 0.6985 0.0874 0.0452 0.0552 227 ARG A CG 1744 C CD . ARG A 227 ? 0.7979 0.8344 0.7688 0.0915 0.0485 0.0576 227 ARG A CD 1745 N NE . ARG A 227 ? 0.8536 0.8863 0.8271 0.0871 0.0477 0.0552 227 ARG A NE 1746 C CZ . ARG A 227 ? 0.8489 0.8713 0.8237 0.0850 0.0505 0.0557 227 ARG A CZ 1747 N NH1 . ARG A 227 ? 0.8253 0.8394 0.7991 0.0866 0.0547 0.0585 227 ARG A NH1 1748 N NH2 . ARG A 227 ? 0.8414 0.8620 0.8186 0.0811 0.0493 0.0532 227 ARG A NH2 1749 N N . GLU A 228 ? 0.5714 0.6128 0.5408 0.0925 0.0477 0.0600 228 GLU A N 1750 C CA . GLU A 228 ? 0.5834 0.6154 0.5532 0.0914 0.0508 0.0619 228 GLU A CA 1751 C C . GLU A 228 ? 0.5151 0.5468 0.4881 0.0853 0.0480 0.0588 228 GLU A C 1752 O O . GLU A 228 ? 0.5431 0.5665 0.5182 0.0814 0.0493 0.0583 228 GLU A O 1753 C CB . GLU A 228 ? 0.6933 0.7246 0.6592 0.0980 0.0547 0.0664 228 GLU A CB 1754 C CG . GLU A 228 ? 0.8096 0.8510 0.7736 0.1012 0.0526 0.0666 228 GLU A CG 1755 C CD . GLU A 228 ? 0.9165 0.9582 0.8761 0.1089 0.0565 0.0714 228 GLU A CD 1756 O OE1 . GLU A 228 ? 0.9572 0.9934 0.9144 0.1128 0.0604 0.0746 228 GLU A OE1 1757 O OE2 . GLU A 228 ? 0.9520 0.9997 0.9103 0.1111 0.0557 0.0721 228 GLU A OE2 1758 N N . GLY A 229 ? 0.4766 0.5174 0.4499 0.0846 0.0441 0.0565 229 GLY A N 1759 C CA . GLY A 229 ? 0.4218 0.4630 0.3980 0.0791 0.0412 0.0534 229 GLY A CA 1760 C C . GLY A 229 ? 0.4003 0.4386 0.3799 0.0728 0.0388 0.0499 229 GLY A C 1761 O O . GLY A 229 ? 0.3883 0.4212 0.3703 0.0683 0.0384 0.0486 229 GLY A O 1762 N N . LEU A 230 ? 0.3625 0.4045 0.3422 0.0727 0.0373 0.0486 230 LEU A N 1763 C CA . LEU A 230 ? 0.3416 0.3803 0.3243 0.0672 0.0356 0.0457 230 LEU A CA 1764 C C . LEU A 230 ? 0.3491 0.3773 0.3329 0.0657 0.0388 0.0470 230 LEU A C 1765 O O . LEU A 230 ? 0.3426 0.3662 0.3290 0.0607 0.0379 0.0451 230 LEU A O 1766 C CB . LEU A 230 ? 0.3419 0.3856 0.3242 0.0680 0.0343 0.0447 230 LEU A CB 1767 C CG . LEU A 230 ? 0.3931 0.4350 0.3784 0.0622 0.0319 0.0414 230 LEU A CG 1768 C CD1 . LEU A 230 ? 0.3758 0.4233 0.3625 0.0586 0.0281 0.0382 230 LEU A CD1 1769 C CD2 . LEU A 230 ? 0.4181 0.4622 0.4030 0.0633 0.0319 0.0411 230 LEU A CD2 1770 N N . MET A 231 ? 0.3374 0.3616 0.3191 0.0700 0.0426 0.0503 231 MET A N 1771 C CA . MET A 231 ? 0.3423 0.3563 0.3250 0.0685 0.0461 0.0513 231 MET A CA 1772 C C . MET A 231 ? 0.3673 0.3754 0.3508 0.0672 0.0482 0.0522 231 MET A C 1773 O O . MET A 231 ? 0.4222 0.4228 0.4077 0.0640 0.0501 0.0516 231 MET A O 1774 C CB . MET A 231 ? 0.3635 0.3746 0.3438 0.0735 0.0499 0.0544 231 MET A CB 1775 C CG . MET A 231 ? 0.3762 0.3917 0.3560 0.0744 0.0484 0.0533 231 MET A CG 1776 S SD A MET A 231 ? 0.3801 0.3903 0.3640 0.0677 0.0472 0.0499 231 MET A SD 1777 S SD B MET A 231 ? 0.3561 0.3744 0.3395 0.0679 0.0438 0.0486 231 MET A SD 1778 C CE A MET A 231 ? 0.3934 0.4094 0.3765 0.0693 0.0455 0.0489 231 MET A CE 1779 C CE B MET A 231 ? 0.3775 0.4012 0.3593 0.0712 0.0433 0.0487 231 MET A CE 1780 N N . ASN A 232 ? 0.3582 0.3698 0.3402 0.0694 0.0480 0.0535 232 ASN A N 1781 C CA . ASN A 232 ? 0.3874 0.3931 0.3700 0.0683 0.0503 0.0545 232 ASN A CA 1782 C C . ASN A 232 ? 0.3356 0.3433 0.3207 0.0635 0.0469 0.0515 232 ASN A C 1783 O O . ASN A 232 ? 0.3736 0.3762 0.3602 0.0612 0.0484 0.0514 232 ASN A O 1784 C CB . ASN A 232 ? 0.4299 0.4356 0.4090 0.0743 0.0537 0.0586 232 ASN A CB 1785 C CG A ASN A 232 ? 0.4845 0.4854 0.4641 0.0732 0.0560 0.0597 232 ASN A CG 1786 C CG B ASN A 232 ? 0.4387 0.4542 0.4158 0.0775 0.0511 0.0588 232 ASN A CG 1787 O OD1 A ASN A 232 ? 0.5191 0.5114 0.4995 0.0720 0.0597 0.0606 232 ASN A OD1 1788 O OD1 B ASN A 232 ? 0.4535 0.4745 0.4322 0.0744 0.0470 0.0559 232 ASN A OD1 1789 N ND2 A ASN A 232 ? 0.4809 0.4875 0.4598 0.0740 0.0539 0.0595 232 ASN A ND2 1790 N ND2 B ASN A 232 ? 0.4682 0.4861 0.4416 0.0839 0.0535 0.0623 232 ASN A ND2 1791 N N . ILE A 233 ? 0.2886 0.3036 0.2743 0.0620 0.0426 0.0489 233 ILE A N 1792 C CA . ILE A 233 ? 0.2575 0.2743 0.2454 0.0577 0.0393 0.0461 233 ILE A CA 1793 C C . ILE A 233 ? 0.2531 0.2692 0.2436 0.0528 0.0367 0.0428 233 ILE A C 1794 O O . ILE A 233 ? 0.2571 0.2687 0.2499 0.0487 0.0364 0.0412 233 ILE A O 1795 C CB . ILE A 233 ? 0.2679 0.2934 0.2545 0.0594 0.0365 0.0454 233 ILE A CB 1796 C CG1 . ILE A 233 ? 0.2910 0.3174 0.2750 0.0642 0.0391 0.0487 233 ILE A CG1 1797 C CG2 . ILE A 233 ? 0.2733 0.3002 0.2620 0.0548 0.0332 0.0423 233 ILE A CG2 1798 C CD1 . ILE A 233 ? 0.3138 0.3499 0.2963 0.0666 0.0364 0.0480 233 ILE A CD1 1799 N N . HIS A 234 ? 0.2606 0.2814 0.2506 0.0533 0.0348 0.0418 234 HIS A N 1800 C CA . HIS A 234 ? 0.2435 0.2653 0.2357 0.0488 0.0318 0.0386 234 HIS A CA 1801 C C . HIS A 234 ? 0.2532 0.2697 0.2470 0.0467 0.0329 0.0381 234 HIS A C 1802 O O . HIS A 234 ? 0.2300 0.2455 0.2259 0.0424 0.0309 0.0356 234 HIS A O 1803 C CB . HIS A 234 ? 0.2432 0.2734 0.2344 0.0497 0.0290 0.0373 234 HIS A CB 1804 C CG . HIS A 234 ? 0.2388 0.2746 0.2295 0.0501 0.0270 0.0365 234 HIS A CG 1805 N ND1 . HIS A 234 ? 0.2591 0.3008 0.2474 0.0547 0.0275 0.0380 234 HIS A ND1 1806 C CD2 . HIS A 234 ? 0.2145 0.2501 0.2066 0.0468 0.0250 0.0345 234 HIS A CD2 1807 C CE1 . HIS A 234 ? 0.2228 0.2682 0.2113 0.0537 0.0256 0.0366 234 HIS A CE1 1808 N NE2 . HIS A 234 ? 0.2757 0.3173 0.2664 0.0489 0.0241 0.0345 234 HIS A NE2 1809 N N . MET A 235 ? 0.2409 0.2538 0.2335 0.0496 0.0363 0.0404 235 MET A N 1810 C CA . MET A 235 ? 0.2450 0.2532 0.2389 0.0481 0.0377 0.0399 235 MET A CA 1811 C C . MET A 235 ? 0.2561 0.2562 0.2519 0.0457 0.0405 0.0399 235 MET A C 1812 O O . MET A 235 ? 0.2621 0.2593 0.2599 0.0426 0.0403 0.0380 235 MET A O 1813 C CB . MET A 235 ? 0.2428 0.2517 0.2343 0.0529 0.0400 0.0423 235 MET A CB 1814 C CG . MET A 235 ? 0.2428 0.2477 0.2354 0.0517 0.0413 0.0417 235 MET A CG 1815 S SD . MET A 235 ? 0.2695 0.2792 0.2640 0.0476 0.0369 0.0381 235 MET A SD 1816 C CE . MET A 235 ? 0.2757 0.2944 0.2674 0.0521 0.0354 0.0390 235 MET A CE 1817 N N . PRO A 236 ? 0.2689 0.2654 0.2640 0.0472 0.0432 0.0418 236 PRO A N 1818 C CA . PRO A 236 ? 0.2685 0.2573 0.2655 0.0451 0.0465 0.0417 236 PRO A CA 1819 C C . PRO A 236 ? 0.2485 0.2354 0.2487 0.0397 0.0448 0.0383 236 PRO A C 1820 O O . PRO A 236 ? 0.2656 0.2476 0.2675 0.0378 0.0469 0.0374 236 PRO A O 1821 C CB . PRO A 236 ? 0.3029 0.2893 0.2987 0.0470 0.0490 0.0438 236 PRO A CB 1822 C CG . PRO A 236 ? 0.3145 0.3060 0.3071 0.0521 0.0488 0.0464 236 PRO A CG 1823 C CD . PRO A 236 ? 0.2885 0.2875 0.2811 0.0512 0.0441 0.0443 236 PRO A CD 1824 N N . ALA A 237 ? 0.2402 0.2310 0.2413 0.0372 0.0412 0.0365 237 ALA A N 1825 C CA . ALA A 237 ? 0.2288 0.2183 0.2328 0.0325 0.0396 0.0335 237 ALA A CA 1826 C C . ALA A 237 ? 0.2226 0.2123 0.2277 0.0306 0.0384 0.0316 237 ALA A C 1827 O O . ALA A 237 ? 0.2275 0.2149 0.2350 0.0272 0.0384 0.0295 237 ALA A O 1828 C CB . ALA A 237 ? 0.2255 0.2188 0.2297 0.0308 0.0361 0.0321 237 ALA A CB 1829 N N . TYR A 238 ? 0.2263 0.2193 0.2299 0.0329 0.0375 0.0325 238 TYR A N 1830 C CA . TYR A 238 ? 0.2231 0.2163 0.2275 0.0315 0.0368 0.0310 238 TYR A CA 1831 C C . TYR A 238 ? 0.2297 0.2168 0.2352 0.0315 0.0407 0.0313 238 TYR A C 1832 O O . TYR A 238 ? 0.2288 0.2145 0.2363 0.0287 0.0404 0.0292 238 TYR A O 1833 C CB . TYR A 238 ? 0.2150 0.2135 0.2175 0.0341 0.0352 0.0317 238 TYR A CB 1834 C CG . TYR A 238 ? 0.2087 0.2129 0.2111 0.0324 0.0311 0.0302 238 TYR A CG 1835 C CD1 . TYR A 238 ? 0.1901 0.1955 0.1940 0.0289 0.0286 0.0277 238 TYR A CD1 1836 C CD2 . TYR A 238 ? 0.2109 0.2189 0.2117 0.0341 0.0299 0.0310 238 TYR A CD2 1837 C CE1 . TYR A 238 ? 0.1950 0.2047 0.1988 0.0270 0.0252 0.0262 238 TYR A CE1 1838 C CE2 . TYR A 238 ? 0.2046 0.2171 0.2055 0.0321 0.0265 0.0292 238 TYR A CE2 1839 C CZ . TYR A 238 ? 0.2047 0.2178 0.2072 0.0286 0.0242 0.0269 238 TYR A CZ 1840 O OH . TYR A 238 ? 0.2002 0.2170 0.2026 0.0268 0.0213 0.0253 238 TYR A OH 1841 N N . LYS A 239 ? 0.2357 0.2191 0.2399 0.0346 0.0444 0.0338 239 LYS A N 1842 C CA . LYS A 239 ? 0.2576 0.2345 0.2628 0.0342 0.0485 0.0339 239 LYS A CA 1843 C C . LYS A 239 ? 0.2383 0.2120 0.2466 0.0299 0.0492 0.0315 239 LYS A C 1844 O O . LYS A 239 ? 0.2531 0.2239 0.2635 0.0274 0.0504 0.0295 239 LYS A O 1845 C CB . LYS A 239 ? 0.2910 0.2642 0.2938 0.0387 0.0528 0.0374 239 LYS A CB 1846 C CG . LYS A 239 ? 0.3638 0.3300 0.3673 0.0389 0.0574 0.0378 239 LYS A CG 1847 C CD . LYS A 239 ? 0.4041 0.3646 0.4094 0.0365 0.0605 0.0371 239 LYS A CD 1848 C CE . LYS A 239 ? 0.4562 0.4089 0.4620 0.0368 0.0660 0.0377 239 LYS A CE 1849 N NZ . LYS A 239 ? 0.4837 0.4319 0.4913 0.0343 0.0689 0.0370 239 LYS A NZ 1850 N N . ASN A 240 ? 0.2386 0.2131 0.2472 0.0290 0.0484 0.0315 240 ASN A N 1851 C CA . ASN A 240 ? 0.2360 0.2085 0.2475 0.0249 0.0485 0.0288 240 ASN A CA 1852 C C . ASN A 240 ? 0.2240 0.1995 0.2375 0.0215 0.0452 0.0256 240 ASN A C 1853 O O . ASN A 240 ? 0.2396 0.2132 0.2558 0.0185 0.0462 0.0232 240 ASN A O 1854 C CB . ASN A 240 ? 0.2500 0.2241 0.2615 0.0244 0.0474 0.0290 240 ASN A CB 1855 C CG . ASN A 240 ? 0.2844 0.2556 0.2941 0.0274 0.0508 0.0320 240 ASN A CG 1856 O OD1 . ASN A 240 ? 0.2939 0.2669 0.3008 0.0312 0.0507 0.0346 240 ASN A OD1 1857 N ND2 . ASN A 240 ? 0.3755 0.3429 0.3868 0.0257 0.0536 0.0314 240 ASN A ND2 1858 N N . ALA A 241 ? 0.2199 0.2005 0.2322 0.0220 0.0413 0.0256 241 ALA A N 1859 C CA . ALA A 241 ? 0.2122 0.1956 0.2258 0.0192 0.0383 0.0231 241 ALA A CA 1860 C C . ALA A 241 ? 0.2093 0.1908 0.2240 0.0186 0.0398 0.0221 241 ALA A C 1861 O O . ALA A 241 ? 0.2235 0.2052 0.2404 0.0157 0.0391 0.0195 241 ALA A O 1862 C CB . ALA A 241 ? 0.2132 0.2021 0.2252 0.0199 0.0343 0.0234 241 ALA A CB 1863 N N . MET A 242 ? 0.2109 0.1908 0.2241 0.0217 0.0420 0.0241 242 MET A N 1864 C CA . MET A 242 ? 0.2187 0.1960 0.2329 0.0213 0.0441 0.0233 242 MET A CA 1865 C C . MET A 242 ? 0.2232 0.1954 0.2400 0.0190 0.0475 0.0216 242 MET A C 1866 O O . MET A 242 ? 0.2254 0.1970 0.2444 0.0164 0.0478 0.0190 242 MET A O 1867 C CB . MET A 242 ? 0.2277 0.2032 0.2395 0.0256 0.0466 0.0261 242 MET A CB 1868 C CG . MET A 242 ? 0.2427 0.2235 0.2518 0.0285 0.0440 0.0278 242 MET A CG 1869 S SD . MET A 242 ? 0.2450 0.2313 0.2546 0.0267 0.0399 0.0257 242 MET A SD 1870 C CE . MET A 242 ? 0.2499 0.2408 0.2597 0.0242 0.0356 0.0245 242 MET A CE 1871 N N . ASP A 243 ? 0.2302 0.1988 0.2467 0.0198 0.0503 0.0229 243 ASP A N 1872 C CA . ASP A 243 ? 0.2644 0.2284 0.2836 0.0172 0.0539 0.0211 243 ASP A CA 1873 C C . ASP A 243 ? 0.2544 0.2209 0.2765 0.0129 0.0517 0.0174 243 ASP A C 1874 O O . ASP A 243 ? 0.2649 0.2289 0.2898 0.0103 0.0541 0.0149 243 ASP A O 1875 C CB . ASP A 243 ? 0.2676 0.2278 0.2858 0.0187 0.0570 0.0233 243 ASP A CB 1876 C CG . ASP A 243 ? 0.3084 0.2645 0.3238 0.0231 0.0606 0.0268 243 ASP A CG 1877 O OD1 . ASP A 243 ? 0.3227 0.2779 0.3373 0.0248 0.0615 0.0274 243 ASP A OD1 1878 O OD2 . ASP A 243 ? 0.3427 0.2966 0.3568 0.0249 0.0628 0.0291 243 ASP A OD2 1879 N N . LYS A 244 ? 0.2385 0.2102 0.2602 0.0123 0.0474 0.0170 244 LYS A N 1880 C CA . LYS A 244 ? 0.2391 0.2137 0.2631 0.0089 0.0451 0.0139 244 LYS A CA 1881 C C . LYS A 244 ? 0.2292 0.2076 0.2536 0.0077 0.0419 0.0122 244 LYS A C 1882 O O . LYS A 244 ? 0.2474 0.2291 0.2732 0.0053 0.0395 0.0099 244 LYS A O 1883 C CB . LYS A 244 ? 0.2263 0.2034 0.2493 0.0091 0.0428 0.0148 244 LYS A CB 1884 C CG . LYS A 244 ? 0.2586 0.2320 0.2816 0.0100 0.0462 0.0162 244 LYS A CG 1885 C CD . LYS A 244 ? 0.2685 0.2441 0.2904 0.0105 0.0443 0.0171 244 LYS A CD 1886 C CE . LYS A 244 ? 0.2935 0.2649 0.3150 0.0119 0.0482 0.0190 244 LYS A CE 1887 N NZ . LYS A 244 ? 0.2875 0.2609 0.3084 0.0121 0.0469 0.0196 244 LYS A NZ 1888 N N . GLY A 245 ? 0.2196 0.1978 0.2426 0.0094 0.0420 0.0134 245 GLY A N 1889 C CA . GLY A 245 ? 0.2158 0.1974 0.2394 0.0083 0.0395 0.0117 245 GLY A CA 1890 C C . GLY A 245 ? 0.2005 0.1870 0.2226 0.0082 0.0350 0.0120 245 GLY A C 1891 O O . GLY A 245 ? 0.2008 0.1901 0.2238 0.0063 0.0329 0.0100 245 GLY A O 1892 N N . VAL A 246 ? 0.2024 0.1899 0.2223 0.0102 0.0338 0.0143 246 VAL A N 1893 C CA . VAL A 246 ? 0.1829 0.1747 0.2014 0.0100 0.0299 0.0144 246 VAL A CA 1894 C C . VAL A 246 ? 0.1874 0.1816 0.2056 0.0097 0.0284 0.0138 246 VAL A C 1895 O O . VAL A 246 ? 0.1909 0.1842 0.2085 0.0114 0.0299 0.0146 246 VAL A O 1896 C CB . VAL A 246 ? 0.1860 0.1789 0.2021 0.0123 0.0291 0.0167 246 VAL A CB 1897 C CG1 . VAL A 246 ? 0.1989 0.1923 0.2131 0.0153 0.0300 0.0188 246 VAL A CG1 1898 C CG2 . VAL A 246 ? 0.1785 0.1749 0.1938 0.0113 0.0255 0.0162 246 VAL A CG2 1899 N N . SER A 247 ? 0.1748 0.1720 0.1931 0.0078 0.0255 0.0123 247 SER A N 1900 C CA . SER A 247 ? 0.1759 0.1751 0.1943 0.0072 0.0244 0.0115 247 SER A CA 1901 C C . SER A 247 ? 0.1791 0.1809 0.1953 0.0088 0.0229 0.0129 247 SER A C 1902 O O . SER A 247 ? 0.1839 0.1868 0.2000 0.0092 0.0229 0.0128 247 SER A O 1903 C CB . SER A 247 ? 0.1852 0.1866 0.2045 0.0048 0.0222 0.0094 247 SER A CB 1904 O OG . SER A 247 ? 0.1951 0.1952 0.2169 0.0032 0.0238 0.0074 247 SER A OG 1905 N N . THR A 248 ? 0.1730 0.1762 0.1877 0.0095 0.0214 0.0141 248 THR A N 1906 C CA . THR A 248 ? 0.1641 0.1706 0.1768 0.0107 0.0198 0.0151 248 THR A CA 1907 C C . THR A 248 ? 0.1667 0.1734 0.1780 0.0128 0.0202 0.0168 248 THR A C 1908 O O . THR A 248 ? 0.1612 0.1658 0.1728 0.0130 0.0211 0.0172 248 THR A O 1909 C CB . THR A 248 ? 0.1573 0.1664 0.1695 0.0086 0.0169 0.0140 248 THR A CB 1910 O OG1 . THR A 248 ? 0.1646 0.1733 0.1764 0.0080 0.0159 0.0141 248 THR A OG1 1911 C CG2 . THR A 248 ? 0.1600 0.1691 0.1737 0.0065 0.0165 0.0123 248 THR A CG2 1912 N N . VAL A 249 ? 0.1595 0.1694 0.1691 0.0145 0.0196 0.0177 249 VAL A N 1913 C CA . VAL A 249 ? 0.1687 0.1804 0.1768 0.0167 0.0195 0.0191 249 VAL A CA 1914 C C . VAL A 249 ? 0.1660 0.1825 0.1729 0.0161 0.0170 0.0185 249 VAL A C 1915 O O . VAL A 249 ? 0.1865 0.2055 0.1932 0.0158 0.0164 0.0179 249 VAL A O 1916 C CB . VAL A 249 ? 0.1795 0.1908 0.1866 0.0203 0.0219 0.0210 249 VAL A CB 1917 C CG1 . VAL A 249 ? 0.1889 0.2035 0.1941 0.0228 0.0216 0.0224 249 VAL A CG1 1918 C CG2 . VAL A 249 ? 0.1930 0.1988 0.2013 0.0207 0.0249 0.0216 249 VAL A CG2 1919 N N . MET A 250 ? 0.1568 0.1748 0.1631 0.0157 0.0157 0.0184 250 MET A N 1920 C CA . MET A 250 ? 0.1643 0.1867 0.1695 0.0149 0.0136 0.0175 250 MET A CA 1921 C C . MET A 250 ? 0.1747 0.2011 0.1786 0.0178 0.0140 0.0185 250 MET A C 1922 O O . MET A 250 ? 0.1890 0.2142 0.1924 0.0197 0.0150 0.0197 250 MET A O 1923 C CB . MET A 250 ? 0.1670 0.1886 0.1723 0.0124 0.0120 0.0164 250 MET A CB 1924 C CG . MET A 250 ? 0.1769 0.2025 0.1814 0.0111 0.0102 0.0152 250 MET A CG 1925 S SD . MET A 250 ? 0.1757 0.1994 0.1799 0.0085 0.0087 0.0140 250 MET A SD 1926 C CE . MET A 250 ? 0.1805 0.1998 0.1857 0.0064 0.0086 0.0136 250 MET A CE 1927 N N . ILE A 251 ? 0.1792 0.2105 0.1823 0.0182 0.0131 0.0179 251 ILE A N 1928 C CA . ILE A 251 ? 0.1790 0.2155 0.1808 0.0212 0.0133 0.0186 251 ILE A CA 1929 C C . ILE A 251 ? 0.1821 0.2217 0.1833 0.0202 0.0118 0.0175 251 ILE A C 1930 O O . ILE A 251 ? 0.1846 0.2237 0.1864 0.0170 0.0103 0.0158 251 ILE A O 1931 C CB . ILE A 251 ? 0.1781 0.2193 0.1794 0.0218 0.0129 0.0180 251 ILE A CB 1932 C CG1 . ILE A 251 ? 0.1909 0.2290 0.1928 0.0226 0.0144 0.0189 251 ILE A CG1 1933 C CG2 . ILE A 251 ? 0.1855 0.2329 0.1853 0.0255 0.0133 0.0187 251 ILE A CG2 1934 C CD1 . ILE A 251 ? 0.1905 0.2251 0.1919 0.0261 0.0170 0.0212 251 ILE A CD1 1935 N N . SER A 252 ? 0.1787 0.2212 0.1788 0.0232 0.0123 0.0184 252 SER A N 1936 C CA . SER A 252 ? 0.1981 0.2441 0.1978 0.0227 0.0111 0.0173 252 SER A CA 1937 C C . SER A 252 ? 0.2210 0.2742 0.2204 0.0219 0.0097 0.0153 252 SER A C 1938 O O . SER A 252 ? 0.2212 0.2787 0.2201 0.0238 0.0100 0.0155 252 SER A O 1939 C CB . SER A 252 ? 0.2017 0.2488 0.2003 0.0265 0.0124 0.0192 252 SER A CB 1940 O OG . SER A 252 ? 0.2191 0.2692 0.2174 0.0260 0.0112 0.0181 252 SER A OG 1941 N N . TYR A 253 ? 0.2296 0.2843 0.2292 0.0193 0.0083 0.0132 253 TYR A N 1942 C CA . TYR A 253 ? 0.2481 0.3105 0.2474 0.0187 0.0072 0.0110 253 TYR A CA 1943 C C . TYR A 253 ? 0.2484 0.3173 0.2466 0.0229 0.0077 0.0116 253 TYR A C 1944 O O . TYR A 253 ? 0.2716 0.3481 0.2695 0.0233 0.0071 0.0100 253 TYR A O 1945 C CB . TYR A 253 ? 0.2521 0.3142 0.2518 0.0155 0.0061 0.0087 253 TYR A CB 1946 C CG . TYR A 253 ? 0.2653 0.3222 0.2657 0.0113 0.0055 0.0076 253 TYR A CG 1947 C CD1 . TYR A 253 ? 0.2695 0.3267 0.2703 0.0093 0.0053 0.0067 253 TYR A CD1 1948 C CD2 . TYR A 253 ? 0.2861 0.3378 0.2866 0.0097 0.0052 0.0075 253 TYR A CD2 1949 C CE1 . TYR A 253 ? 0.2528 0.3054 0.2540 0.0056 0.0049 0.0058 253 TYR A CE1 1950 C CE2 . TYR A 253 ? 0.2884 0.3354 0.2892 0.0062 0.0048 0.0066 253 TYR A CE2 1951 C CZ . TYR A 253 ? 0.2770 0.3245 0.2781 0.0043 0.0047 0.0058 253 TYR A CZ 1952 O OH . TYR A 253 ? 0.2835 0.3265 0.2846 0.0011 0.0044 0.0052 253 TYR A OH 1953 N N . SER A 254 ? 0.2476 0.3139 0.2451 0.0259 0.0088 0.0140 254 SER A N 1954 C CA . SER A 254 ? 0.2703 0.3428 0.2665 0.0301 0.0094 0.0149 254 SER A CA 1955 C C . SER A 254 ? 0.2808 0.3579 0.2760 0.0337 0.0102 0.0160 254 SER A C 1956 O O . SER A 254 ? 0.2628 0.3377 0.2584 0.0330 0.0106 0.0163 254 SER A O 1957 C CB . SER A 254 ? 0.2894 0.3576 0.2850 0.0323 0.0105 0.0172 254 SER A CB 1958 O OG . SER A 254 ? 0.2940 0.3551 0.2896 0.0335 0.0123 0.0198 254 SER A OG 1959 N N . SER A 255 ? 0.3074 0.3917 0.3012 0.0375 0.0105 0.0164 255 SER A N 1960 C CA . SER A 255 ? 0.3379 0.4270 0.3303 0.0419 0.0115 0.0179 255 SER A CA 1961 C C . SER A 255 ? 0.3667 0.4536 0.3573 0.0468 0.0135 0.0213 255 SER A C 1962 O O . SER A 255 ? 0.3710 0.4561 0.3616 0.0467 0.0136 0.0217 255 SER A O 1963 C CB . SER A 255 ? 0.3401 0.4407 0.3320 0.0429 0.0102 0.0154 255 SER A CB 1964 O OG . SER A 255 ? 0.3465 0.4495 0.3401 0.0382 0.0086 0.0120 255 SER A OG 1965 N N . TRP A 256 ? 0.3703 0.4573 0.3595 0.0510 0.0153 0.0238 256 TRP A N 1966 C CA . TRP A 256 ? 0.4069 0.4928 0.3939 0.0563 0.0176 0.0272 256 TRP A CA 1967 C C . TRP A 256 ? 0.4499 0.5459 0.4348 0.0614 0.0177 0.0276 256 TRP A C 1968 O O . TRP A 256 ? 0.4564 0.5550 0.4409 0.0628 0.0179 0.0276 256 TRP A O 1969 C CB . TRP A 256 ? 0.4297 0.5059 0.4165 0.0573 0.0202 0.0302 256 TRP A CB 1970 C CG . TRP A 256 ? 0.4417 0.5161 0.4261 0.0629 0.0230 0.0340 256 TRP A CG 1971 C CD1 . TRP A 256 ? 0.4749 0.5494 0.4584 0.0646 0.0236 0.0352 256 TRP A CD1 1972 C CD2 . TRP A 256 ? 0.4614 0.5335 0.4438 0.0676 0.0258 0.0371 256 TRP A CD2 1973 N NE1 . TRP A 256 ? 0.4752 0.5475 0.4562 0.0701 0.0267 0.0390 256 TRP A NE1 1974 C CE2 . TRP A 256 ? 0.4752 0.5459 0.4554 0.0721 0.0282 0.0403 256 TRP A CE2 1975 C CE3 . TRP A 256 ? 0.4799 0.5511 0.4620 0.0687 0.0267 0.0375 256 TRP A CE3 1976 C CZ2 . TRP A 256 ? 0.4848 0.5524 0.4624 0.0776 0.0317 0.0440 256 TRP A CZ2 1977 C CZ3 . TRP A 256 ? 0.4919 0.5602 0.4716 0.0741 0.0300 0.0411 256 TRP A CZ3 1978 C CH2 . TRP A 256 ? 0.5298 0.5962 0.5073 0.0785 0.0326 0.0444 256 TRP A CH2 1979 N N . ASN A 257 ? 0.4740 0.5760 0.4576 0.0642 0.0175 0.0278 257 ASN A N 1980 C CA . ASN A 257 ? 0.5028 0.6158 0.4843 0.0695 0.0175 0.0280 257 ASN A CA 1981 C C . ASN A 257 ? 0.4968 0.6180 0.4793 0.0675 0.0155 0.0245 257 ASN A C 1982 O O . ASN A 257 ? 0.5033 0.6298 0.4844 0.0713 0.0161 0.0253 257 ASN A O 1983 C CB . ASN A 257 ? 0.5472 0.6578 0.5258 0.0760 0.0206 0.0325 257 ASN A CB 1984 C CG . ASN A 257 ? 0.5712 0.6769 0.5482 0.0791 0.0228 0.0358 257 ASN A CG 1985 O OD1 . ASN A 257 ? 0.5784 0.6870 0.5557 0.0784 0.0217 0.0348 257 ASN A OD1 1986 N ND2 . ASN A 257 ? 0.5796 0.6778 0.5548 0.0826 0.0260 0.0398 257 ASN A ND2 1987 N N . GLY A 258 ? 0.4548 0.5767 0.4399 0.0615 0.0133 0.0207 258 GLY A N 1988 C CA . GLY A 258 ? 0.4526 0.5821 0.4389 0.0586 0.0114 0.0169 258 GLY A CA 1989 C C . GLY A 258 ? 0.4304 0.5553 0.4180 0.0558 0.0114 0.0166 258 GLY A C 1990 O O . GLY A 258 ? 0.4791 0.6096 0.4679 0.0527 0.0098 0.0133 258 GLY A O 1991 N N . VAL A 259 ? 0.3760 0.4911 0.3631 0.0567 0.0131 0.0198 259 VAL A N 1992 C CA . VAL A 259 ? 0.3262 0.4369 0.3145 0.0540 0.0132 0.0194 259 VAL A CA 1993 C C . VAL A 259 ? 0.2937 0.3952 0.2841 0.0481 0.0125 0.0184 259 VAL A C 1994 O O . VAL A 259 ? 0.3244 0.4180 0.3149 0.0481 0.0136 0.0204 259 VAL A O 1995 C CB . VAL A 259 ? 0.3438 0.4491 0.3304 0.0584 0.0156 0.0232 259 VAL A CB 1996 C CG1 . VAL A 259 ? 0.3276 0.4285 0.3155 0.0555 0.0156 0.0226 259 VAL A CG1 1997 C CG2 . VAL A 259 ? 0.3822 0.4961 0.3662 0.0650 0.0166 0.0247 259 VAL A CG2 1998 N N . LYS A 260 ? 0.2634 0.3663 0.2556 0.0433 0.0108 0.0154 260 LYS A N 1999 C CA . LYS A 260 ? 0.2495 0.3440 0.2436 0.0378 0.0102 0.0144 260 LYS A CA 2000 C C . LYS A 260 ? 0.2484 0.3334 0.2426 0.0382 0.0117 0.0171 260 LYS A C 2001 O O . LYS A 260 ? 0.2393 0.3241 0.2330 0.0401 0.0127 0.0182 260 LYS A O 2002 C CB . LYS A 260 ? 0.2477 0.3454 0.2432 0.0333 0.0086 0.0112 260 LYS A CB 2003 C CG . LYS A 260 ? 0.2593 0.3653 0.2553 0.0314 0.0071 0.0078 260 LYS A CG 2004 C CD . LYS A 260 ? 0.2569 0.3585 0.2539 0.0275 0.0064 0.0065 260 LYS A CD 2005 C CE . LYS A 260 ? 0.2585 0.3686 0.2561 0.0254 0.0052 0.0027 260 LYS A CE 2006 N NZ . LYS A 260 ? 0.2882 0.3936 0.2865 0.0221 0.0047 0.0016 260 LYS A NZ 2007 N N . MET A 261 ? 0.2204 0.2975 0.2153 0.0362 0.0121 0.0179 261 MET A N 2008 C CA . MET A 261 ? 0.2237 0.2921 0.2190 0.0363 0.0137 0.0200 261 MET A CA 2009 C C . MET A 261 ? 0.2099 0.2764 0.2064 0.0333 0.0131 0.0188 261 MET A C 2010 O O . MET A 261 ? 0.2216 0.2842 0.2180 0.0348 0.0146 0.0203 261 MET A O 2011 C CB . MET A 261 ? 0.2229 0.2841 0.2189 0.0343 0.0139 0.0205 261 MET A CB 2012 C CG . MET A 261 ? 0.2320 0.2927 0.2267 0.0381 0.0154 0.0228 261 MET A CG 2013 S SD . MET A 261 ? 0.2489 0.3070 0.2419 0.0436 0.0186 0.0264 261 MET A SD 2014 C CE . MET A 261 ? 0.2361 0.2864 0.2307 0.0412 0.0196 0.0265 261 MET A CE 2015 N N . HIS A 262 ? 0.2073 0.2764 0.2048 0.0293 0.0112 0.0161 262 HIS A N 2016 C CA . HIS A 262 ? 0.2014 0.2693 0.2000 0.0263 0.0106 0.0149 262 HIS A CA 2017 C C . HIS A 262 ? 0.2070 0.2806 0.2049 0.0287 0.0109 0.0148 262 HIS A C 2018 O O . HIS A 262 ? 0.2124 0.2851 0.2111 0.0269 0.0107 0.0141 262 HIS A O 2019 C CB . HIS A 262 ? 0.1814 0.2504 0.1810 0.0215 0.0088 0.0121 262 HIS A CB 2020 C CG . HIS A 262 ? 0.1914 0.2533 0.1917 0.0187 0.0086 0.0122 262 HIS A CG 2021 N ND1 . HIS A 262 ? 0.2196 0.2764 0.2209 0.0154 0.0082 0.0117 262 HIS A ND1 2022 C CD2 . HIS A 262 ? 0.1835 0.2431 0.1836 0.0190 0.0086 0.0127 262 HIS A CD2 2023 C CE1 . HIS A 262 ? 0.1556 0.2072 0.1572 0.0139 0.0081 0.0119 262 HIS A CE1 2024 N NE2 . HIS A 262 ? 0.2279 0.2812 0.2289 0.0159 0.0083 0.0124 262 HIS A NE2 2025 N N . ALA A 263 ? 0.2168 0.2964 0.2133 0.0330 0.0115 0.0157 263 ALA A N 2026 C CA . ALA A 263 ? 0.2335 0.3188 0.2291 0.0361 0.0120 0.0159 263 ALA A CA 2027 C C . ALA A 263 ? 0.2435 0.3270 0.2373 0.0417 0.0142 0.0191 263 ALA A C 2028 O O . ALA A 263 ? 0.2693 0.3582 0.2617 0.0456 0.0148 0.0198 263 ALA A O 2029 C CB . ALA A 263 ? 0.2447 0.3407 0.2399 0.0363 0.0105 0.0136 263 ALA A CB 2030 N N . ASN A 264 ? 0.2421 0.3181 0.2357 0.0425 0.0156 0.0212 264 ASN A N 2031 C CA . ASN A 264 ? 0.2345 0.3084 0.2263 0.0479 0.0182 0.0244 264 ASN A CA 2032 C C . ASN A 264 ? 0.2422 0.3088 0.2342 0.0486 0.0202 0.0261 264 ASN A C 2033 O O . ASN A 264 ? 0.2441 0.3024 0.2369 0.0472 0.0215 0.0270 264 ASN A O 2034 C CB . ASN A 264 ? 0.2660 0.3365 0.2573 0.0487 0.0189 0.0258 264 ASN A CB 2035 C CG . ASN A 264 ? 0.2823 0.3534 0.2711 0.0550 0.0214 0.0290 264 ASN A CG 2036 O OD1 . ASN A 264 ? 0.3005 0.3686 0.2883 0.0580 0.0235 0.0309 264 ASN A OD1 2037 N ND2 . ASN A 264 ? 0.3453 0.4204 0.3329 0.0572 0.0212 0.0296 264 ASN A ND2 2038 N N . GLN A 265 ? 0.2500 0.3201 0.2411 0.0510 0.0207 0.0262 265 GLN A N 2039 C CA . GLN A 265 ? 0.2492 0.3130 0.2404 0.0520 0.0228 0.0276 265 GLN A CA 2040 C C . GLN A 265 ? 0.2528 0.3102 0.2425 0.0561 0.0261 0.0309 265 GLN A C 2041 O O . GLN A 265 ? 0.2628 0.3119 0.2534 0.0551 0.0280 0.0317 265 GLN A O 2042 C CB . GLN A 265 ? 0.2632 0.3329 0.2537 0.0541 0.0225 0.0270 265 GLN A CB 2043 C CG . GLN A 265 ? 0.2879 0.3512 0.2787 0.0546 0.0245 0.0279 265 GLN A CG 2044 C CD . GLN A 265 ? 0.3541 0.4238 0.3438 0.0575 0.0244 0.0277 265 GLN A CD 2045 O OE1 . GLN A 265 ? 0.4099 0.4839 0.4008 0.0545 0.0224 0.0253 265 GLN A OE1 2046 N NE2 . GLN A 265 ? 0.4062 0.4767 0.3933 0.0636 0.0267 0.0303 265 GLN A NE2 2047 N N . ASP A 266 ? 0.2619 0.3233 0.2493 0.0607 0.0269 0.0327 266 ASP A N 2048 C CA . ASP A 266 ? 0.2988 0.3541 0.2844 0.0651 0.0304 0.0362 266 ASP A CA 2049 C C . ASP A 266 ? 0.2728 0.3193 0.2600 0.0618 0.0314 0.0364 266 ASP A C 2050 O O . ASP A 266 ? 0.2742 0.3124 0.2613 0.0625 0.0344 0.0381 266 ASP A O 2051 C CB . ASP A 266 ? 0.3375 0.3991 0.3202 0.0706 0.0310 0.0381 266 ASP A CB 2052 C CG . ASP A 266 ? 0.4212 0.4910 0.4016 0.0754 0.0310 0.0386 266 ASP A CG 2053 O OD1 . ASP A 266 ? 0.4748 0.5522 0.4531 0.0795 0.0307 0.0394 266 ASP A OD1 2054 O OD2 . ASP A 266 ? 0.4649 0.5343 0.4457 0.0752 0.0312 0.0380 266 ASP A OD2 2055 N N . LEU A 267 ? 0.2704 0.3187 0.2590 0.0580 0.0289 0.0346 267 LEU A N 2056 C CA . LEU A 267 ? 0.2748 0.3158 0.2650 0.0549 0.0296 0.0346 267 LEU A CA 2057 C C . LEU A 267 ? 0.2484 0.2839 0.2413 0.0497 0.0289 0.0326 267 LEU A C 2058 O O . LEU A 267 ? 0.2613 0.2891 0.2552 0.0486 0.0310 0.0333 267 LEU A O 2059 C CB . LEU A 267 ? 0.2614 0.3061 0.2516 0.0536 0.0275 0.0338 267 LEU A CB 2060 C CG . LEU A 267 ? 0.2633 0.3113 0.2510 0.0587 0.0289 0.0362 267 LEU A CG 2061 C CD1 . LEU A 267 ? 0.2672 0.3193 0.2553 0.0569 0.0266 0.0348 267 LEU A CD1 2062 C CD2 . LEU A 267 ? 0.2920 0.3318 0.2787 0.0615 0.0328 0.0394 267 LEU A CD2 2063 N N . VAL A 268 ? 0.2409 0.2806 0.2349 0.0466 0.0263 0.0301 268 VAL A N 2064 C CA . VAL A 268 ? 0.2406 0.2760 0.2372 0.0418 0.0254 0.0282 268 VAL A CA 2065 C C . VAL A 268 ? 0.2309 0.2616 0.2278 0.0427 0.0277 0.0288 268 VAL A C 2066 O O . VAL A 268 ? 0.2425 0.2664 0.2409 0.0405 0.0291 0.0285 268 VAL A O 2067 C CB . VAL A 268 ? 0.2384 0.2792 0.2359 0.0381 0.0221 0.0254 268 VAL A CB 2068 C CG1 . VAL A 268 ? 0.2311 0.2678 0.2308 0.0338 0.0214 0.0237 268 VAL A CG1 2069 C CG2 . VAL A 268 ? 0.2291 0.2730 0.2266 0.0366 0.0202 0.0246 268 VAL A CG2 2070 N N . THR A 269 ? 0.2422 0.2767 0.2376 0.0460 0.0282 0.0295 269 THR A N 2071 C CA . THR A 269 ? 0.2406 0.2709 0.2362 0.0471 0.0305 0.0300 269 THR A CA 2072 C C . THR A 269 ? 0.2595 0.2848 0.2532 0.0519 0.0344 0.0331 269 THR A C 2073 O O . THR A 269 ? 0.2544 0.2721 0.2491 0.0511 0.0370 0.0335 269 THR A O 2074 C CB . THR A 269 ? 0.2377 0.2740 0.2329 0.0479 0.0292 0.0290 269 THR A CB 2075 O OG1 . THR A 269 ? 0.2527 0.2922 0.2497 0.0430 0.0260 0.0262 269 THR A OG1 2076 C CG2 . THR A 269 ? 0.2504 0.2817 0.2458 0.0491 0.0317 0.0295 269 THR A CG2 2077 N N . GLY A 270 ? 0.2738 0.3036 0.2649 0.0566 0.0350 0.0351 270 GLY A N 2078 C CA . GLY A 270 ? 0.2743 0.2994 0.2631 0.0618 0.0390 0.0384 270 GLY A CA 2079 C C . GLY A 270 ? 0.2906 0.3078 0.2801 0.0606 0.0413 0.0395 270 GLY A C 2080 O O . GLY A 270 ? 0.3144 0.3238 0.3036 0.0621 0.0452 0.0411 270 GLY A O 2081 N N . TYR A 271 ? 0.2822 0.3009 0.2727 0.0579 0.0393 0.0385 271 TYR A N 2082 C CA . TYR A 271 ? 0.2897 0.3016 0.2808 0.0569 0.0414 0.0396 271 TYR A CA 2083 C C . TYR A 271 ? 0.2738 0.2807 0.2682 0.0511 0.0407 0.0370 271 TYR A C 2084 O O . TYR A 271 ? 0.2818 0.2814 0.2773 0.0504 0.0438 0.0373 271 TYR A O 2085 C CB . TYR A 271 ? 0.3058 0.3215 0.2957 0.0583 0.0403 0.0406 271 TYR A CB 2086 C CG . TYR A 271 ? 0.3268 0.3352 0.3165 0.0588 0.0435 0.0424 271 TYR A CG 2087 C CD1 . TYR A 271 ? 0.3565 0.3604 0.3439 0.0636 0.0478 0.0457 271 TYR A CD1 2088 C CD2 . TYR A 271 ? 0.3298 0.3357 0.3217 0.0545 0.0424 0.0409 271 TYR A CD2 2089 C CE1 . TYR A 271 ? 0.3692 0.3663 0.3566 0.0638 0.0511 0.0473 271 TYR A CE1 2090 C CE2 . TYR A 271 ? 0.3463 0.3459 0.3382 0.0548 0.0455 0.0425 271 TYR A CE2 2091 C CZ . TYR A 271 ? 0.3819 0.3770 0.3716 0.0593 0.0498 0.0456 271 TYR A CZ 2092 O OH . TYR A 271 ? 0.4084 0.3970 0.3982 0.0594 0.0531 0.0471 271 TYR A OH 2093 N N . LEU A 272 ? 0.2651 0.2760 0.2613 0.0470 0.0370 0.0345 272 LEU A N 2094 C CA . LEU A 272 ? 0.2586 0.2652 0.2576 0.0419 0.0363 0.0323 272 LEU A CA 2095 C C . LEU A 272 ? 0.2493 0.2520 0.2499 0.0403 0.0377 0.0311 272 LEU A C 2096 O O . LEU A 272 ? 0.2492 0.2456 0.2514 0.0386 0.0400 0.0306 272 LEU A O 2097 C CB . LEU A 272 ? 0.2374 0.2492 0.2375 0.0383 0.0322 0.0300 272 LEU A CB 2098 C CG . LEU A 272 ? 0.2335 0.2422 0.2363 0.0334 0.0310 0.0277 272 LEU A CG 2099 C CD1 . LEU A 272 ? 0.2407 0.2441 0.2444 0.0325 0.0328 0.0281 272 LEU A CD1 2100 C CD2 . LEU A 272 ? 0.2317 0.2460 0.2347 0.0308 0.0271 0.0259 272 LEU A CD2 2101 N N . LYS A 273 ? 0.2488 0.2555 0.2490 0.0409 0.0364 0.0304 273 LYS A N 2102 C CA . LYS A 273 ? 0.2480 0.2516 0.2497 0.0395 0.0375 0.0291 273 LYS A CA 2103 C C . LYS A 273 ? 0.2717 0.2699 0.2722 0.0432 0.0419 0.0311 273 LYS A C 2104 O O . LYS A 273 ? 0.2734 0.2653 0.2756 0.0417 0.0444 0.0305 273 LYS A O 2105 C CB . LYS A 273 ? 0.2389 0.2486 0.2408 0.0384 0.0346 0.0274 273 LYS A CB 2106 C CG . LYS A 273 ? 0.2204 0.2338 0.2238 0.0340 0.0308 0.0251 273 LYS A CG 2107 C CD . LYS A 273 ? 0.2277 0.2465 0.2313 0.0328 0.0284 0.0236 273 LYS A CD 2108 C CE . LYS A 273 ? 0.2155 0.2357 0.2207 0.0281 0.0254 0.0213 273 LYS A CE 2109 N NZ . LYS A 273 ? 0.2349 0.2600 0.2402 0.0271 0.0235 0.0199 273 LYS A NZ 2110 N N . ASP A 274 ? 0.2984 0.2991 0.2961 0.0482 0.0430 0.0336 274 ASP A N 2111 C CA . ASP A 274 ? 0.3144 0.3103 0.3105 0.0522 0.0471 0.0355 274 ASP A CA 2112 C C . ASP A 274 ? 0.3260 0.3148 0.3212 0.0544 0.0513 0.0380 274 ASP A C 2113 O O . ASP A 274 ? 0.3634 0.3457 0.3581 0.0562 0.0554 0.0391 274 ASP A O 2114 C CB . ASP A 274 ? 0.3376 0.3395 0.3308 0.0570 0.0466 0.0371 274 ASP A CB 2115 C CG . ASP A 274 ? 0.3618 0.3699 0.3561 0.0551 0.0433 0.0347 274 ASP A CG 2116 O OD1 . ASP A 274 ? 0.3662 0.3731 0.3632 0.0504 0.0419 0.0321 274 ASP A OD1 2117 O OD2 . ASP A 274 ? 0.3948 0.4094 0.3870 0.0585 0.0422 0.0355 274 ASP A OD2 2118 N N . THR A 275 ? 0.3070 0.2967 0.3017 0.0542 0.0505 0.0388 275 THR A N 2119 C CA . THR A 275 ? 0.3291 0.3125 0.3227 0.0564 0.0545 0.0413 275 THR A CA 2120 C C . THR A 275 ? 0.3394 0.3178 0.3360 0.0514 0.0550 0.0395 275 THR A C 2121 O O . THR A 275 ? 0.3409 0.3115 0.3383 0.0509 0.0590 0.0397 275 THR A O 2122 C CB . THR A 275 ? 0.3417 0.3296 0.3322 0.0607 0.0541 0.0441 275 THR A CB 2123 O OG1 . THR A 275 ? 0.3611 0.3545 0.3490 0.0653 0.0536 0.0455 275 THR A OG1 2124 C CG2 . THR A 275 ? 0.3545 0.3357 0.3435 0.0634 0.0586 0.0471 275 THR A CG2 2125 N N . LEU A 276 ? 0.3135 0.2962 0.3118 0.0477 0.0511 0.0374 276 LEU A N 2126 C CA . LEU A 276 ? 0.3127 0.2916 0.3140 0.0430 0.0512 0.0353 276 LEU A CA 2127 C C . LEU A 276 ? 0.3050 0.2815 0.3092 0.0390 0.0511 0.0323 276 LEU A C 2128 O O . LEU A 276 ? 0.3017 0.2748 0.3085 0.0353 0.0518 0.0304 276 LEU A O 2129 C CB . LEU A 276 ? 0.3106 0.2945 0.3124 0.0408 0.0473 0.0344 276 LEU A CB 2130 C CG . LEU A 276 ? 0.3222 0.3079 0.3215 0.0441 0.0476 0.0370 276 LEU A CG 2131 C CD1 . LEU A 276 ? 0.3411 0.3312 0.3413 0.0413 0.0438 0.0354 276 LEU A CD1 2132 C CD2 . LEU A 276 ? 0.3472 0.3257 0.3460 0.0458 0.0523 0.0391 276 LEU A CD2 2133 N N . LYS A 277 ? 0.2764 0.2552 0.2803 0.0398 0.0503 0.0317 277 LYS A N 2134 C CA . LYS A 277 ? 0.2822 0.2597 0.2886 0.0365 0.0501 0.0289 277 LYS A CA 2135 C C . LYS A 277 ? 0.2582 0.2389 0.2672 0.0315 0.0464 0.0258 277 LYS A C 2136 O O . LYS A 277 ? 0.2563 0.2347 0.2679 0.0281 0.0469 0.0233 277 LYS A O 2137 C CB . LYS A 277 ? 0.3227 0.2922 0.3304 0.0362 0.0550 0.0286 277 LYS A CB 2138 C CG . LYS A 277 ? 0.3493 0.3144 0.3542 0.0413 0.0592 0.0318 277 LYS A CG 2139 C CD . LYS A 277 ? 0.3867 0.3558 0.3896 0.0445 0.0581 0.0326 277 LYS A CD 2140 C CE . LYS A 277 ? 0.4363 0.4009 0.4363 0.0500 0.0625 0.0358 277 LYS A CE 2141 N NZ . LYS A 277 ? 0.4722 0.4414 0.4704 0.0530 0.0612 0.0363 277 LYS A NZ 2142 N N . PHE A 278 ? 0.2307 0.2170 0.2388 0.0313 0.0428 0.0261 278 PHE A N 2143 C CA . PHE A 278 ? 0.2227 0.2123 0.2327 0.0270 0.0391 0.0235 278 PHE A CA 2144 C C . PHE A 278 ? 0.2136 0.2055 0.2247 0.0253 0.0376 0.0214 278 PHE A C 2145 O O . PHE A 278 ? 0.2244 0.2196 0.2341 0.0273 0.0368 0.0221 278 PHE A O 2146 C CB . PHE A 278 ? 0.2123 0.2073 0.2208 0.0276 0.0359 0.0242 278 PHE A CB 2147 C CG . PHE A 278 ? 0.2114 0.2092 0.2213 0.0236 0.0324 0.0219 278 PHE A CG 2148 C CD1 . PHE A 278 ? 0.2075 0.2024 0.2196 0.0206 0.0327 0.0203 278 PHE A CD1 2149 C CD2 . PHE A 278 ? 0.1974 0.2008 0.2065 0.0230 0.0291 0.0213 278 PHE A CD2 2150 C CE1 . PHE A 278 ? 0.2024 0.1999 0.2155 0.0175 0.0296 0.0185 278 PHE A CE1 2151 C CE2 . PHE A 278 ? 0.1999 0.2052 0.2101 0.0196 0.0263 0.0194 278 PHE A CE2 2152 C CZ . PHE A 278 ? 0.2070 0.2094 0.2190 0.0171 0.0265 0.0182 278 PHE A CZ 2153 N N . LYS A 279 ? 0.2239 0.2145 0.2376 0.0216 0.0372 0.0189 279 LYS A N 2154 C CA . LYS A 279 ? 0.2173 0.2098 0.2323 0.0196 0.0359 0.0167 279 LYS A CA 2155 C C . LYS A 279 ? 0.2154 0.2119 0.2314 0.0163 0.0322 0.0148 279 LYS A C 2156 O O . LYS A 279 ? 0.2115 0.2099 0.2287 0.0144 0.0310 0.0129 279 LYS A O 2157 C CB . LYS A 279 ? 0.2373 0.2252 0.2545 0.0184 0.0390 0.0150 279 LYS A CB 2158 C CG . LYS A 279 ? 0.2588 0.2416 0.2750 0.0217 0.0433 0.0169 279 LYS A CG 2159 C CD . LYS A 279 ? 0.2830 0.2684 0.2970 0.0250 0.0429 0.0184 279 LYS A CD 2160 C CE . LYS A 279 ? 0.3350 0.3147 0.3481 0.0281 0.0475 0.0199 279 LYS A CE 2161 N NZ . LYS A 279 ? 0.3398 0.3228 0.3502 0.0322 0.0470 0.0220 279 LYS A NZ 2162 N N . GLY A 280 ? 0.1929 0.1903 0.2085 0.0156 0.0307 0.0152 280 GLY A N 2163 C CA . GLY A 280 ? 0.1985 0.1997 0.2144 0.0131 0.0272 0.0139 280 GLY A CA 2164 C C . GLY A 280 ? 0.1899 0.1957 0.2038 0.0141 0.0248 0.0148 280 GLY A C 2165 O O . GLY A 280 ? 0.1926 0.1996 0.2052 0.0165 0.0256 0.0159 280 GLY A O 2166 N N . PHE A 281 ? 0.1774 0.1860 0.1910 0.0122 0.0220 0.0141 281 PHE A N 2167 C CA . PHE A 281 ? 0.1698 0.1829 0.1817 0.0127 0.0199 0.0146 281 PHE A CA 2168 C C . PHE A 281 ? 0.1853 0.2000 0.1957 0.0137 0.0190 0.0158 281 PHE A C 2169 O O . PHE A 281 ? 0.1775 0.1904 0.1880 0.0130 0.0188 0.0158 281 PHE A O 2170 C CB . PHE A 281 ? 0.1574 0.1732 0.1697 0.0100 0.0176 0.0130 281 PHE A CB 2171 C CG . PHE A 281 ? 0.1612 0.1768 0.1737 0.0076 0.0158 0.0121 281 PHE A CG 2172 C CD1 . PHE A 281 ? 0.1533 0.1707 0.1644 0.0072 0.0142 0.0125 281 PHE A CD1 2173 C CD2 . PHE A 281 ? 0.1683 0.1824 0.1823 0.0057 0.0158 0.0107 281 PHE A CD2 2174 C CE1 . PHE A 281 ? 0.1653 0.1822 0.1763 0.0051 0.0126 0.0118 281 PHE A CE1 2175 C CE2 . PHE A 281 ? 0.1580 0.1723 0.1719 0.0038 0.0141 0.0100 281 PHE A CE2 2176 C CZ . PHE A 281 ? 0.1566 0.1720 0.1689 0.0036 0.0126 0.0107 281 PHE A CZ 2177 N N . VAL A 282 ? 0.1728 0.1914 0.1816 0.0154 0.0183 0.0165 282 VAL A N 2178 C CA . VAL A 282 ? 0.1734 0.1948 0.1808 0.0166 0.0174 0.0173 282 VAL A CA 2179 C C . VAL A 282 ? 0.1803 0.2054 0.1874 0.0141 0.0148 0.0159 282 VAL A C 2180 O O . VAL A 282 ? 0.1775 0.2055 0.1845 0.0133 0.0140 0.0151 282 VAL A O 2181 C CB . VAL A 282 ? 0.1935 0.2178 0.1994 0.0203 0.0185 0.0187 282 VAL A CB 2182 C CG1 . VAL A 282 ? 0.1912 0.2196 0.1956 0.0214 0.0174 0.0192 282 VAL A CG1 2183 C CG2 . VAL A 282 ? 0.2003 0.2200 0.2062 0.0229 0.0216 0.0203 282 VAL A CG2 2184 N N . ILE A 283 ? 0.1637 0.1884 0.1705 0.0128 0.0137 0.0156 283 ILE A N 2185 C CA . ILE A 283 ? 0.1627 0.1898 0.1691 0.0103 0.0116 0.0144 283 ILE A CA 2186 C C . ILE A 283 ? 0.1694 0.2002 0.1745 0.0111 0.0108 0.0144 283 ILE A C 2187 O O . ILE A 283 ? 0.1655 0.1958 0.1702 0.0130 0.0115 0.0154 283 ILE A O 2188 C CB . ILE A 283 ? 0.1712 0.1947 0.1783 0.0077 0.0109 0.0137 283 ILE A CB 2189 C CG1 . ILE A 283 ? 0.1705 0.1956 0.1770 0.0052 0.0091 0.0125 283 ILE A CG1 2190 C CG2 . ILE A 283 ? 0.1748 0.1955 0.1819 0.0085 0.0114 0.0143 283 ILE A CG2 2191 C CD1 . ILE A 283 ? 0.1792 0.2010 0.1860 0.0031 0.0084 0.0119 283 ILE A CD1 2192 N N . SER A 284 ? 0.1636 0.1984 0.1682 0.0095 0.0094 0.0132 284 SER A N 2193 C CA . SER A 284 ? 0.1593 0.1981 0.1630 0.0099 0.0087 0.0127 284 SER A CA 2194 C C . SER A 284 ? 0.1699 0.2058 0.1735 0.0083 0.0080 0.0123 284 SER A C 2195 O O . SER A 284 ? 0.1718 0.2033 0.1760 0.0065 0.0079 0.0122 284 SER A O 2196 C CB . SER A 284 ? 0.1655 0.2095 0.1689 0.0081 0.0076 0.0110 284 SER A CB 2197 O OG . SER A 284 ? 0.1625 0.2043 0.1661 0.0046 0.0067 0.0098 284 SER A OG 2198 N N . ASP A 285 ? 0.1677 0.2066 0.1707 0.0089 0.0076 0.0119 285 ASP A N 2199 C CA . ASP A 285 ? 0.1743 0.2114 0.1770 0.0068 0.0068 0.0110 285 ASP A CA 2200 C C . ASP A 285 ? 0.1691 0.2077 0.1716 0.0037 0.0058 0.0092 285 ASP A C 2201 O O . ASP A 285 ? 0.1716 0.2132 0.1743 0.0030 0.0057 0.0085 285 ASP A O 2202 C CB . ASP A 285 ? 0.1895 0.2288 0.1917 0.0087 0.0069 0.0113 285 ASP A CB 2203 C CG . ASP A 285 ? 0.2080 0.2433 0.2101 0.0074 0.0064 0.0111 285 ASP A CG 2204 O OD1 . ASP A 285 ? 0.2443 0.2759 0.2466 0.0050 0.0059 0.0105 285 ASP A OD1 2205 O OD2 . ASP A 285 ? 0.2777 0.3136 0.2795 0.0091 0.0067 0.0116 285 ASP A OD2 2206 N N . TRP A 286 ? 0.1671 0.2037 0.1692 0.0017 0.0053 0.0083 286 TRP A N 2207 C CA . TRP A 286 ? 0.1669 0.2033 0.1687 -0.0015 0.0048 0.0067 286 TRP A CA 2208 C C . TRP A 286 ? 0.1799 0.2226 0.1816 -0.0022 0.0046 0.0049 286 TRP A C 2209 O O . TRP A 286 ? 0.1848 0.2308 0.1863 -0.0016 0.0044 0.0040 286 TRP A O 2210 C CB . TRP A 286 ? 0.1718 0.2039 0.1730 -0.0028 0.0045 0.0064 286 TRP A CB 2211 C CG . TRP A 286 ? 0.1755 0.2064 0.1760 -0.0060 0.0044 0.0048 286 TRP A CG 2212 C CD1 . TRP A 286 ? 0.1856 0.2200 0.1859 -0.0077 0.0044 0.0028 286 TRP A CD1 2213 C CD2 . TRP A 286 ? 0.1795 0.2052 0.1793 -0.0078 0.0045 0.0051 286 TRP A CD2 2214 N NE1 . TRP A 286 ? 0.1887 0.2197 0.1882 -0.0106 0.0047 0.0018 286 TRP A NE1 2215 C CE2 . TRP A 286 ? 0.1834 0.2089 0.1824 -0.0106 0.0047 0.0034 286 TRP A CE2 2216 C CE3 . TRP A 286 ? 0.1846 0.2059 0.1843 -0.0073 0.0045 0.0066 286 TRP A CE3 2217 C CZ2 . TRP A 286 ? 0.1904 0.2110 0.1884 -0.0126 0.0051 0.0035 286 TRP A CZ2 2218 C CZ3 . TRP A 286 ? 0.1888 0.2059 0.1874 -0.0092 0.0046 0.0066 286 TRP A CZ3 2219 C CH2 . TRP A 286 ? 0.1864 0.2029 0.1840 -0.0116 0.0050 0.0052 286 TRP A CH2 2220 N N . GLU A 287 ? 0.1840 0.2289 0.1858 -0.0035 0.0046 0.0042 287 GLU A N 2221 C CA . GLU A 287 ? 0.1982 0.2504 0.2002 -0.0039 0.0045 0.0023 287 GLU A CA 2222 C C . GLU A 287 ? 0.2046 0.2620 0.2067 -0.0003 0.0046 0.0029 287 GLU A C 2223 O O . GLU A 287 ? 0.1956 0.2594 0.1976 -0.0001 0.0044 0.0012 287 GLU A O 2224 C CB . GLU A 287 ? 0.2244 0.2776 0.2262 -0.0070 0.0044 -0.0001 287 GLU A CB 2225 C CG . GLU A 287 ? 0.2672 0.3156 0.2686 -0.0105 0.0047 -0.0006 287 GLU A CG 2226 C CD . GLU A 287 ? 0.3171 0.3653 0.3181 -0.0135 0.0051 -0.0030 287 GLU A CD 2227 O OE1 . GLU A 287 ? 0.3769 0.4280 0.3781 -0.0128 0.0049 -0.0041 287 GLU A OE1 2228 O OE2 . GLU A 287 ? 0.4207 0.4658 0.4213 -0.0165 0.0057 -0.0036 287 GLU A OE2 2229 N N . GLY A 288 ? 0.1793 0.2341 0.1814 0.0027 0.0050 0.0052 288 GLY A N 2230 C CA . GLY A 288 ? 0.1753 0.2342 0.1770 0.0066 0.0054 0.0062 288 GLY A CA 2231 C C . GLY A 288 ? 0.1828 0.2489 0.1844 0.0079 0.0055 0.0055 288 GLY A C 2232 O O . GLY A 288 ? 0.2059 0.2782 0.2071 0.0105 0.0055 0.0052 288 GLY A O 2233 N N . ILE A 289 ? 0.1901 0.2559 0.1921 0.0064 0.0054 0.0052 289 ILE A N 2234 C CA . ILE A 289 ? 0.1937 0.2664 0.1956 0.0078 0.0055 0.0045 289 ILE A CA 2235 C C . ILE A 289 ? 0.2068 0.2865 0.2089 0.0057 0.0048 0.0016 289 ILE A C 2236 O O . ILE A 289 ? 0.1949 0.2825 0.1968 0.0079 0.0048 0.0008 289 ILE A O 2237 C CB . ILE A 289 ? 0.1926 0.2637 0.1950 0.0073 0.0058 0.0051 289 ILE A CB 2238 C CG1 . ILE A 289 ? 0.1987 0.2686 0.2015 0.0028 0.0052 0.0033 289 ILE A CG1 2239 C CG2 . ILE A 289 ? 0.2047 0.2688 0.2071 0.0091 0.0066 0.0076 289 ILE A CG2 2240 C CD1 . ILE A 289 ? 0.2022 0.2719 0.2054 0.0025 0.0054 0.0037 289 ILE A CD1 2241 N N . ASP A 290 ? 0.1928 0.2698 0.1952 0.0017 0.0045 0.0000 290 ASP A N 2242 C CA . ASP A 290 ? 0.2174 0.3003 0.2202 -0.0010 0.0042 -0.0032 290 ASP A CA 2243 C C . ASP A 290 ? 0.2159 0.3047 0.2184 0.0016 0.0040 -0.0039 290 ASP A C 2244 O O . ASP A 290 ? 0.2227 0.3201 0.2255 0.0015 0.0038 -0.0063 290 ASP A O 2245 C CB . ASP A 290 ? 0.2247 0.3022 0.2276 -0.0054 0.0042 -0.0046 290 ASP A CB 2246 C CG . ASP A 290 ? 0.2413 0.3119 0.2441 -0.0075 0.0045 -0.0034 290 ASP A CG 2247 O OD1 . ASP A 290 ? 0.2334 0.2997 0.2361 -0.0054 0.0045 -0.0009 290 ASP A OD1 2248 O OD2 . ASP A 290 ? 0.2698 0.3394 0.2727 -0.0113 0.0048 -0.0051 290 ASP A OD2 2249 N N . ARG A 291 ? 0.2035 0.2882 0.2055 0.0040 0.0041 -0.0019 291 ARG A N 2250 C CA . ARG A 291 ? 0.2171 0.3065 0.2187 0.0063 0.0040 -0.0023 291 ARG A CA 2251 C C . ARG A 291 ? 0.2312 0.3268 0.2320 0.0114 0.0042 -0.0009 291 ARG A C 2252 O O . ARG A 291 ? 0.2474 0.3475 0.2477 0.0140 0.0042 -0.0010 291 ARG A O 2253 C CB . ARG A 291 ? 0.2337 0.3160 0.2351 0.0064 0.0040 -0.0009 291 ARG A CB 2254 C CG . ARG A 291 ? 0.2581 0.3358 0.2599 0.0018 0.0038 -0.0027 291 ARG A CG 2255 C CD . ARG A 291 ? 0.3168 0.3864 0.3183 0.0018 0.0039 -0.0011 291 ARG A CD 2256 N NE . ARG A 291 ? 0.4094 0.4735 0.4110 -0.0024 0.0039 -0.0022 291 ARG A NE 2257 C CZ . ARG A 291 ? 0.4558 0.5138 0.4571 -0.0037 0.0039 -0.0020 291 ARG A CZ 2258 N NH1 . ARG A 291 ? 0.4494 0.5060 0.4504 -0.0014 0.0038 -0.0008 291 ARG A NH1 2259 N NH2 . ARG A 291 ? 0.4479 0.5010 0.4491 -0.0072 0.0041 -0.0028 291 ARG A NH2 2260 N N . ILE A 292 ? 0.2344 0.3309 0.2352 0.0128 0.0046 0.0002 292 ILE A N 2261 C CA . ILE A 292 ? 0.2348 0.3379 0.2346 0.0176 0.0050 0.0013 292 ILE A CA 2262 C C . ILE A 292 ? 0.2553 0.3697 0.2552 0.0176 0.0043 -0.0018 292 ILE A C 2263 O O . ILE A 292 ? 0.2542 0.3753 0.2532 0.0219 0.0045 -0.0014 292 ILE A O 2264 C CB . ILE A 292 ? 0.2387 0.3405 0.2384 0.0187 0.0055 0.0027 292 ILE A CB 2265 C CG1 . ILE A 292 ? 0.2271 0.3192 0.2266 0.0200 0.0064 0.0059 292 ILE A CG1 2266 C CG2 . ILE A 292 ? 0.2630 0.3736 0.2617 0.0232 0.0058 0.0030 292 ILE A CG2 2267 C CD1 . ILE A 292 ? 0.2236 0.3129 0.2234 0.0197 0.0069 0.0068 292 ILE A CD1 2268 N N . THR A 293 ? 0.2528 0.3693 0.2539 0.0129 0.0038 -0.0051 293 THR A N 2269 C CA . THR A 293 ? 0.2818 0.4094 0.2835 0.0119 0.0032 -0.0088 293 THR A CA 2270 C C . THR A 293 ? 0.3062 0.4354 0.3085 0.0096 0.0029 -0.0113 293 THR A C 2271 O O . THR A 293 ? 0.2794 0.4004 0.2818 0.0074 0.0030 -0.0107 293 THR A O 2272 C CB . THR A 293 ? 0.2864 0.4163 0.2892 0.0076 0.0031 -0.0114 293 THR A CB 2273 O OG1 . THR A 293 ? 0.2679 0.3898 0.2715 0.0025 0.0033 -0.0122 293 THR A OG1 2274 C CG2 . THR A 293 ? 0.2732 0.4022 0.2756 0.0097 0.0034 -0.0093 293 THR A CG2 2275 N N . THR A 294 ? 0.3280 0.4683 0.3305 0.0103 0.0025 -0.0143 294 THR A N 2276 C CA . THR A 294 ? 0.3856 0.5288 0.3890 0.0075 0.0023 -0.0176 294 THR A CA 2277 C C . THR A 294 ? 0.3879 0.5395 0.3928 0.0035 0.0022 -0.0224 294 THR A C 2278 O O . THR A 294 ? 0.4353 0.5973 0.4403 0.0057 0.0020 -0.0238 294 THR A O 2279 C CB . THR A 294 ? 0.4185 0.5680 0.4209 0.0123 0.0020 -0.0171 294 THR A CB 2280 O OG1 . THR A 294 ? 0.4573 0.5991 0.4583 0.0162 0.0024 -0.0124 294 THR A OG1 2281 C CG2 . THR A 294 ? 0.4513 0.6029 0.4547 0.0094 0.0018 -0.0205 294 THR A CG2 2282 N N . PRO A 295 ? 0.3849 0.5321 0.3910 -0.0023 0.0026 -0.0250 295 PRO A N 2283 C CA . PRO A 295 ? 0.3639 0.4987 0.3698 -0.0051 0.0030 -0.0235 295 PRO A CA 2284 C C . PRO A 295 ? 0.3238 0.4489 0.3289 -0.0044 0.0032 -0.0195 295 PRO A C 2285 O O . PRO A 295 ? 0.3109 0.4386 0.3160 -0.0032 0.0032 -0.0187 295 PRO A O 2286 C CB . PRO A 295 ? 0.3834 0.5181 0.3907 -0.0114 0.0038 -0.0277 295 PRO A CB 2287 C CG . PRO A 295 ? 0.3656 0.5138 0.3741 -0.0119 0.0037 -0.0319 295 PRO A CG 2288 C CD . PRO A 295 ? 0.3771 0.5317 0.3847 -0.0066 0.0030 -0.0297 295 PRO A CD 2289 N N . ALA A 296 ? 0.3002 0.4148 0.3048 -0.0052 0.0034 -0.0173 296 ALA A N 2290 C CA . ALA A 296 ? 0.2993 0.4050 0.3034 -0.0050 0.0036 -0.0140 296 ALA A CA 2291 C C . ALA A 296 ? 0.2959 0.4008 0.3006 -0.0091 0.0040 -0.0156 296 ALA A C 2292 O O . ALA A 296 ? 0.3260 0.4316 0.3314 -0.0134 0.0045 -0.0187 296 ALA A O 2293 C CB . ALA A 296 ? 0.2805 0.3759 0.2841 -0.0058 0.0037 -0.0122 296 ALA A CB 2294 N N . GLY A 297 ? 0.2605 0.3634 0.2650 -0.0080 0.0040 -0.0134 297 GLY A N 2295 C CA . GLY A 297 ? 0.2655 0.3662 0.2703 -0.0117 0.0045 -0.0143 297 GLY A CA 2296 C C . GLY A 297 ? 0.2807 0.3912 0.2865 -0.0133 0.0046 -0.0175 297 GLY A C 2297 O O . GLY A 297 ? 0.3142 0.4233 0.3203 -0.0166 0.0051 -0.0184 297 GLY A O 2298 N N . SER A 298 ? 0.2867 0.4069 0.2927 -0.0108 0.0041 -0.0191 298 SER A N 2299 C CA . SER A 298 ? 0.2743 0.4053 0.2814 -0.0125 0.0042 -0.0229 298 SER A CA 2300 C C . SER A 298 ? 0.2935 0.4291 0.3004 -0.0101 0.0040 -0.0218 298 SER A C 2301 O O . SER A 298 ? 0.2876 0.4317 0.2954 -0.0117 0.0041 -0.0248 298 SER A O 2302 C CB . SER A 298 ? 0.2810 0.4216 0.2884 -0.0109 0.0039 -0.0255 298 SER A CB 2303 O OG . SER A 298 ? 0.2694 0.4133 0.2758 -0.0048 0.0032 -0.0228 298 SER A OG 2304 N N . ASP A 299 ? 0.2757 0.4061 0.2815 -0.0063 0.0037 -0.0178 299 ASP A N 2305 C CA . ASP A 299 ? 0.2430 0.3761 0.2487 -0.0044 0.0037 -0.0167 299 ASP A CA 2306 C C . ASP A 299 ? 0.2463 0.3689 0.2512 -0.0030 0.0038 -0.0127 299 ASP A C 2307 O O . ASP A 299 ? 0.2305 0.3518 0.2345 0.0016 0.0038 -0.0099 299 ASP A O 2308 C CB . ASP A 299 ? 0.2611 0.4039 0.2662 0.0009 0.0033 -0.0165 299 ASP A CB 2309 C CG . ASP A 299 ? 0.2721 0.4193 0.2770 0.0025 0.0033 -0.0161 299 ASP A CG 2310 O OD1 . ASP A 299 ? 0.2786 0.4199 0.2838 0.0003 0.0035 -0.0151 299 ASP A OD1 2311 O OD2 . ASP A 299 ? 0.3351 0.4921 0.3397 0.0063 0.0030 -0.0167 299 ASP A OD2 2312 N N . TYR A 300 ? 0.2336 0.3488 0.2389 -0.0071 0.0042 -0.0127 300 TYR A N 2313 C CA . TYR A 300 ? 0.2239 0.3294 0.2286 -0.0062 0.0043 -0.0093 300 TYR A CA 2314 C C . TYR A 300 ? 0.2383 0.3450 0.2428 -0.0033 0.0043 -0.0076 300 TYR A C 2315 O O . TYR A 300 ? 0.2182 0.3195 0.2222 -0.0005 0.0044 -0.0048 300 TYR A O 2316 C CB . TYR A 300 ? 0.2233 0.3212 0.2281 -0.0108 0.0047 -0.0096 300 TYR A CB 2317 C CG . TYR A 300 ? 0.2325 0.3206 0.2368 -0.0100 0.0047 -0.0066 300 TYR A CG 2318 C CD1 . TYR A 300 ? 0.2350 0.3188 0.2389 -0.0084 0.0046 -0.0053 300 TYR A CD1 2319 C CD2 . TYR A 300 ? 0.2532 0.3367 0.2574 -0.0110 0.0049 -0.0054 300 TYR A CD2 2320 C CE1 . TYR A 300 ? 0.2366 0.3119 0.2401 -0.0078 0.0047 -0.0029 300 TYR A CE1 2321 C CE2 . TYR A 300 ? 0.2510 0.3263 0.2548 -0.0104 0.0050 -0.0030 300 TYR A CE2 2322 C CZ . TYR A 300 ? 0.2504 0.3217 0.2539 -0.0088 0.0049 -0.0018 300 TYR A CZ 2323 O OH . TYR A 300 ? 0.2501 0.3139 0.2534 -0.0082 0.0049 0.0003 300 TYR A OH 2324 N N . SER A 301 ? 0.2153 0.3296 0.2202 -0.0038 0.0042 -0.0094 301 SER A N 2325 C CA . SER A 301 ? 0.2324 0.3489 0.2370 -0.0004 0.0043 -0.0079 301 SER A CA 2326 C C . SER A 301 ? 0.2135 0.3309 0.2171 0.0054 0.0044 -0.0056 301 SER A C 2327 O O . SER A 301 ? 0.2224 0.3351 0.2255 0.0082 0.0048 -0.0029 301 SER A O 2328 C CB . SER A 301 ? 0.2466 0.3730 0.2517 -0.0015 0.0041 -0.0107 301 SER A CB 2329 O OG . SER A 301 ? 0.2758 0.4046 0.2805 0.0019 0.0041 -0.0093 301 SER A OG 2330 N N . TYR A 302 ? 0.2195 0.3432 0.2228 0.0072 0.0042 -0.0066 302 TYR A N 2331 C CA . TYR A 302 ? 0.2092 0.3336 0.2113 0.0128 0.0045 -0.0042 302 TYR A CA 2332 C C . TYR A 302 ? 0.2170 0.3310 0.2187 0.0135 0.0049 -0.0015 302 TYR A C 2333 O O . TYR A 302 ? 0.2151 0.3254 0.2160 0.0173 0.0057 0.0013 302 TYR A O 2334 C CB . TYR A 302 ? 0.2384 0.3723 0.2401 0.0145 0.0041 -0.0062 302 TYR A CB 2335 C CG . TYR A 302 ? 0.2455 0.3799 0.2457 0.0205 0.0046 -0.0035 302 TYR A CG 2336 C CD1 . TYR A 302 ? 0.2563 0.3946 0.2553 0.0256 0.0052 -0.0018 302 TYR A CD1 2337 C CD2 . TYR A 302 ? 0.2630 0.3936 0.2628 0.0212 0.0047 -0.0024 302 TYR A CD2 2338 C CE1 . TYR A 302 ? 0.2755 0.4139 0.2728 0.0313 0.0060 0.0010 302 TYR A CE1 2339 C CE2 . TYR A 302 ? 0.2694 0.4002 0.2676 0.0268 0.0055 0.0003 302 TYR A CE2 2340 C CZ . TYR A 302 ? 0.2731 0.4075 0.2701 0.0318 0.0062 0.0021 302 TYR A CZ 2341 O OH . TYR A 302 ? 0.3277 0.4618 0.3228 0.0375 0.0073 0.0050 302 TYR A OH 2342 N N . SER A 303 ? 0.2100 0.3194 0.2123 0.0097 0.0046 -0.0024 303 SER A N 2343 C CA . SER A 303 ? 0.2096 0.3094 0.2116 0.0100 0.0050 0.0000 303 SER A CA 2344 C C . SER A 303 ? 0.2019 0.2947 0.2040 0.0106 0.0056 0.0022 303 SER A C 2345 O O . SER A 303 ? 0.2020 0.2896 0.2036 0.0134 0.0063 0.0047 303 SER A O 2346 C CB . SER A 303 ? 0.1920 0.2875 0.1947 0.0053 0.0046 -0.0015 303 SER A CB 2347 O OG . SER A 303 ? 0.1981 0.2985 0.2008 0.0048 0.0043 -0.0034 303 SER A OG 2348 N N . VAL A 304 ? 0.1873 0.2798 0.1900 0.0079 0.0054 0.0013 304 VAL A N 2349 C CA . VAL A 304 ? 0.1829 0.2697 0.1858 0.0083 0.0059 0.0030 304 VAL A CA 2350 C C . VAL A 304 ? 0.1935 0.2826 0.1958 0.0131 0.0067 0.0046 304 VAL A C 2351 O O . VAL A 304 ? 0.1995 0.2827 0.2017 0.0151 0.0076 0.0068 304 VAL A O 2352 C CB . VAL A 304 ? 0.1851 0.2717 0.1887 0.0045 0.0055 0.0016 304 VAL A CB 2353 C CG1 . VAL A 304 ? 0.1922 0.2743 0.1961 0.0053 0.0060 0.0032 304 VAL A CG1 2354 C CG2 . VAL A 304 ? 0.1908 0.2739 0.1947 -0.0001 0.0051 0.0004 304 VAL A CG2 2355 N N . LYS A 305 ? 0.2021 0.2999 0.2040 0.0148 0.0065 0.0035 305 LYS A N 2356 C CA . LYS A 305 ? 0.2453 0.3451 0.2463 0.0198 0.0074 0.0052 305 LYS A CA 2357 C C . LYS A 305 ? 0.2206 0.3172 0.2205 0.0239 0.0084 0.0077 305 LYS A C 2358 O O . LYS A 305 ? 0.2261 0.3178 0.2256 0.0268 0.0098 0.0099 305 LYS A O 2359 C CB . LYS A 305 ? 0.2574 0.3683 0.2580 0.0213 0.0069 0.0034 305 LYS A CB 2360 C CG . LYS A 305 ? 0.3094 0.4233 0.3088 0.0265 0.0078 0.0050 305 LYS A CG 2361 C CD . LYS A 305 ? 0.2913 0.4166 0.2904 0.0275 0.0072 0.0029 305 LYS A CD 2362 C CE . LYS A 305 ? 0.2702 0.4031 0.2684 0.0303 0.0069 0.0023 305 LYS A CE 2363 N NZ . LYS A 305 ? 0.2789 0.4237 0.2767 0.0324 0.0065 0.0005 305 LYS A NZ 2364 N N . ALA A 306 ? 0.2118 0.3114 0.2113 0.0243 0.0080 0.0071 306 ALA A N 2365 C CA . ALA A 306 ? 0.2109 0.3091 0.2092 0.0285 0.0090 0.0093 306 ALA A CA 2366 C C . ALA A 306 ? 0.2039 0.2916 0.2025 0.0280 0.0100 0.0114 306 ALA A C 2367 O O . ALA A 306 ? 0.2362 0.3202 0.2339 0.0318 0.0116 0.0139 306 ALA A O 2368 C CB . ALA A 306 ? 0.2372 0.3410 0.2352 0.0283 0.0082 0.0079 306 ALA A CB 2369 N N . SER A 307 ? 0.2055 0.2885 0.2054 0.0233 0.0091 0.0103 307 SER A N 2370 C CA . SER A 307 ? 0.2118 0.2856 0.2122 0.0225 0.0098 0.0118 307 SER A CA 2371 C C . SER A 307 ? 0.2009 0.2695 0.2017 0.0231 0.0110 0.0131 307 SER A C 2372 O O . SER A 307 ? 0.1981 0.2609 0.1988 0.0251 0.0125 0.0150 307 SER A O 2373 C CB . SER A 307 ? 0.1886 0.2595 0.1899 0.0177 0.0086 0.0103 307 SER A CB 2374 O OG . SER A 307 ? 0.1817 0.2528 0.1838 0.0143 0.0078 0.0087 307 SER A OG 2375 N N . ILE A 308 ? 0.1893 0.2597 0.1907 0.0213 0.0104 0.0119 308 ILE A N 2376 C CA . ILE A 308 ? 0.1943 0.2601 0.1962 0.0217 0.0115 0.0127 308 ILE A CA 2377 C C . ILE A 308 ? 0.2010 0.2675 0.2018 0.0268 0.0133 0.0145 308 ILE A C 2378 O O . ILE A 308 ? 0.2243 0.2849 0.2253 0.0282 0.0150 0.0160 308 ILE A O 2379 C CB . ILE A 308 ? 0.2051 0.2728 0.2080 0.0185 0.0104 0.0110 308 ILE A CB 2380 C CG1 . ILE A 308 ? 0.1974 0.2628 0.2010 0.0138 0.0091 0.0096 308 ILE A CG1 2381 C CG2 . ILE A 308 ? 0.2098 0.2739 0.2132 0.0193 0.0115 0.0116 308 ILE A CG2 2382 C CD1 . ILE A 308 ? 0.2143 0.2719 0.2185 0.0127 0.0095 0.0105 308 ILE A CD1 2383 N N . LEU A 309 ? 0.2214 0.2956 0.2210 0.0295 0.0130 0.0144 309 LEU A N 2384 C CA . LEU A 309 ? 0.2383 0.3134 0.2364 0.0349 0.0148 0.0164 309 LEU A CA 2385 C C . LEU A 309 ? 0.2257 0.2964 0.2227 0.0379 0.0165 0.0187 309 LEU A C 2386 O O . LEU A 309 ? 0.2497 0.3165 0.2458 0.0415 0.0188 0.0208 309 LEU A O 2387 C CB . LEU A 309 ? 0.2373 0.3224 0.2342 0.0373 0.0141 0.0155 309 LEU A CB 2388 C CG . LEU A 309 ? 0.2809 0.3698 0.2787 0.0353 0.0132 0.0137 309 LEU A CG 2389 C CD1 . LEU A 309 ? 0.2885 0.3879 0.2850 0.0382 0.0126 0.0129 309 LEU A CD1 2390 C CD2 . LEU A 309 ? 0.2706 0.3541 0.2684 0.0368 0.0148 0.0149 309 LEU A CD2 2391 N N . ALA A 310 ? 0.2224 0.2929 0.2197 0.0361 0.0156 0.0183 310 ALA A N 2392 C CA . ALA A 310 ? 0.2266 0.2926 0.2232 0.0385 0.0171 0.0204 310 ALA A CA 2393 C C . ALA A 310 ? 0.2196 0.2758 0.2172 0.0374 0.0188 0.0215 310 ALA A C 2394 O O . ALA A 310 ? 0.2221 0.2738 0.2189 0.0400 0.0208 0.0236 310 ALA A O 2395 C CB . ALA A 310 ? 0.2214 0.2896 0.2181 0.0367 0.0156 0.0195 310 ALA A CB 2396 N N . GLY A 311 ? 0.1992 0.2525 0.1986 0.0334 0.0180 0.0200 311 GLY A N 2397 C CA . GLY A 311 ? 0.2113 0.2564 0.2119 0.0320 0.0194 0.0205 311 GLY A CA 2398 C C . GLY A 311 ? 0.2000 0.2418 0.2023 0.0274 0.0180 0.0191 311 GLY A C 2399 O O . GLY A 311 ? 0.2136 0.2493 0.2171 0.0262 0.0191 0.0192 311 GLY A O 2400 N N . LEU A 312 ? 0.1786 0.2244 0.1809 0.0250 0.0157 0.0177 312 LEU A N 2401 C CA . LEU A 312 ? 0.1801 0.2224 0.1837 0.0208 0.0145 0.0165 312 LEU A CA 2402 C C . LEU A 312 ? 0.1906 0.2311 0.1954 0.0183 0.0142 0.0153 312 LEU A C 2403 O O . LEU A 312 ? 0.1960 0.2400 0.2007 0.0186 0.0139 0.0148 312 LEU A O 2404 C CB . LEU A 312 ? 0.1891 0.2352 0.1924 0.0186 0.0125 0.0152 312 LEU A CB 2405 C CG . LEU A 312 ? 0.1923 0.2388 0.1947 0.0201 0.0126 0.0160 312 LEU A CG 2406 C CD1 . LEU A 312 ? 0.2127 0.2641 0.2137 0.0245 0.0135 0.0171 312 LEU A CD1 2407 C CD2 . LEU A 312 ? 0.2037 0.2523 0.2062 0.0171 0.0108 0.0143 312 LEU A CD2 2408 N N . ASP A 313 ? 0.1691 0.2045 0.1751 0.0159 0.0142 0.0149 313 ASP A N 2409 C CA . ASP A 313 ? 0.1653 0.1990 0.1726 0.0138 0.0140 0.0139 313 ASP A CA 2410 C C . ASP A 313 ? 0.1642 0.1986 0.1717 0.0102 0.0121 0.0125 313 ASP A C 2411 O O . ASP A 313 ? 0.1735 0.2094 0.1814 0.0087 0.0115 0.0115 313 ASP A O 2412 C CB . ASP A 313 ? 0.1710 0.1988 0.1795 0.0139 0.0158 0.0142 313 ASP A CB 2413 C CG . ASP A 313 ? 0.1882 0.2141 0.1963 0.0174 0.0182 0.0157 313 ASP A CG 2414 O OD1 . ASP A 313 ? 0.1956 0.2238 0.2031 0.0195 0.0189 0.0161 313 ASP A OD1 2415 O OD2 . ASP A 313 ? 0.1785 0.2004 0.1869 0.0182 0.0197 0.0166 313 ASP A OD2 2416 N N . MET A 314 ? 0.1705 0.2035 0.1778 0.0089 0.0113 0.0125 314 MET A N 2417 C CA . MET A 314 ? 0.1697 0.2026 0.1769 0.0058 0.0097 0.0114 314 MET A CA 2418 C C . MET A 314 ? 0.1640 0.1994 0.1702 0.0053 0.0088 0.0112 314 MET A C 2419 O O . MET A 314 ? 0.1613 0.1963 0.1671 0.0070 0.0092 0.0120 314 MET A O 2420 C CB . MET A 314 ? 0.1643 0.1925 0.1724 0.0045 0.0099 0.0113 314 MET A CB 2421 C CG . MET A 314 ? 0.1543 0.1820 0.1620 0.0018 0.0084 0.0105 314 MET A CG 2422 S SD . MET A 314 ? 0.1742 0.1973 0.1827 0.0008 0.0085 0.0104 314 MET A SD 2423 C CE . MET A 314 ? 0.1767 0.1995 0.1868 0.0008 0.0093 0.0097 314 MET A CE 2424 N N . ILE A 315 ? 0.1566 0.1946 0.1622 0.0031 0.0077 0.0101 315 ILE A N 2425 C CA . ILE A 315 ? 0.1653 0.2059 0.1701 0.0022 0.0069 0.0094 315 ILE A CA 2426 C C . ILE A 315 ? 0.1572 0.1943 0.1617 -0.0005 0.0062 0.0089 315 ILE A C 2427 O O . ILE A 315 ? 0.1533 0.1891 0.1577 -0.0026 0.0059 0.0085 315 ILE A O 2428 C CB . ILE A 315 ? 0.1562 0.2028 0.1607 0.0017 0.0065 0.0083 315 ILE A CB 2429 C CG1 . ILE A 315 ? 0.1741 0.2243 0.1786 0.0049 0.0073 0.0089 315 ILE A CG1 2430 C CG2 . ILE A 315 ? 0.1718 0.2212 0.1756 0.0003 0.0059 0.0070 315 ILE A CG2 2431 C CD1 . ILE A 315 ? 0.1640 0.2144 0.1681 0.0082 0.0080 0.0101 315 ILE A CD1 2432 N N . MET A 316 ? 0.1486 0.1844 0.1528 -0.0001 0.0061 0.0091 316 MET A N 2433 C CA . MET A 316 ? 0.1606 0.1934 0.1642 -0.0023 0.0056 0.0086 316 MET A CA 2434 C C . MET A 316 ? 0.1570 0.1934 0.1598 -0.0042 0.0052 0.0071 316 MET A C 2435 O O . MET A 316 ? 0.1634 0.2027 0.1660 -0.0039 0.0050 0.0064 316 MET A O 2436 C CB . MET A 316 ? 0.1619 0.1923 0.1654 -0.0009 0.0057 0.0094 316 MET A CB 2437 C CG . MET A 316 ? 0.1567 0.1838 0.1595 -0.0028 0.0052 0.0089 316 MET A CG 2438 S SD . MET A 316 ? 0.1683 0.1935 0.1710 -0.0011 0.0053 0.0095 316 MET A SD 2439 C CE . MET A 316 ? 0.1882 0.2109 0.1920 0.0010 0.0061 0.0109 316 MET A CE 2440 N N . VAL A 317 ? 0.1621 0.1985 0.1648 -0.0064 0.0050 0.0065 317 VAL A N 2441 C CA . VAL A 317 ? 0.1689 0.2097 0.1712 -0.0083 0.0050 0.0049 317 VAL A CA 2442 C C . VAL A 317 ? 0.1733 0.2135 0.1750 -0.0099 0.0049 0.0038 317 VAL A C 2443 O O . VAL A 317 ? 0.1821 0.2271 0.1840 -0.0098 0.0049 0.0025 317 VAL A O 2444 C CB . VAL A 317 ? 0.1789 0.2196 0.1811 -0.0104 0.0051 0.0045 317 VAL A CB 2445 C CG1 . VAL A 317 ? 0.1831 0.2284 0.1851 -0.0126 0.0052 0.0026 317 VAL A CG1 2446 C CG2 . VAL A 317 ? 0.1990 0.2412 0.2020 -0.0085 0.0051 0.0054 317 VAL A CG2 2447 N N . PRO A 318 ? 0.1686 0.2032 0.1695 -0.0112 0.0050 0.0041 318 PRO A N 2448 C CA . PRO A 318 ? 0.1823 0.2120 0.1828 -0.0116 0.0051 0.0053 318 PRO A CA 2449 C C . PRO A 318 ? 0.1817 0.2098 0.1811 -0.0146 0.0055 0.0047 318 PRO A C 2450 O O . PRO A 318 ? 0.1847 0.2093 0.1835 -0.0149 0.0056 0.0056 318 PRO A O 2451 C CB . PRO A 318 ? 0.1791 0.2043 0.1791 -0.0109 0.0049 0.0060 318 PRO A CB 2452 C CG . PRO A 318 ? 0.1939 0.2205 0.1934 -0.0121 0.0051 0.0046 318 PRO A CG 2453 C CD . PRO A 318 ? 0.1806 0.2139 0.1810 -0.0116 0.0050 0.0035 318 PRO A CD 2454 N N . ASN A 319 ? 0.1955 0.2264 0.1947 -0.0168 0.0059 0.0029 319 ASN A N 2455 C CA . ASN A 319 ? 0.2078 0.2364 0.2058 -0.0198 0.0068 0.0022 319 ASN A CA 2456 C C . ASN A 319 ? 0.2179 0.2509 0.2164 -0.0214 0.0071 0.0013 319 ASN A C 2457 O O . ASN A 319 ? 0.2329 0.2637 0.2307 -0.0226 0.0076 0.0019 319 ASN A O 2458 C CB . ASN A 319 ? 0.2190 0.2467 0.2165 -0.0218 0.0075 0.0007 319 ASN A CB 2459 C CG . ASN A 319 ? 0.2324 0.2553 0.2292 -0.0205 0.0072 0.0016 319 ASN A CG 2460 O OD1 . ASN A 319 ? 0.2557 0.2742 0.2518 -0.0192 0.0070 0.0034 319 ASN A OD1 2461 N ND2 . ASN A 319 ? 0.2681 0.2926 0.2653 -0.0204 0.0072 0.0003 319 ASN A ND2 2462 N N . LYS A 320 ? 0.2501 0.2897 0.2498 -0.0210 0.0068 -0.0001 320 LYS A N 2463 C CA . LYS A 320 ? 0.2629 0.3076 0.2631 -0.0224 0.0071 -0.0013 320 LYS A CA 2464 C C . LYS A 320 ? 0.2437 0.2903 0.2446 -0.0203 0.0066 -0.0001 320 LYS A C 2465 O O . LYS A 320 ? 0.2330 0.2855 0.2348 -0.0190 0.0062 -0.0007 320 LYS A O 2466 C CB . LYS A 320 ? 0.3123 0.3639 0.3134 -0.0230 0.0071 -0.0037 320 LYS A CB 2467 C CG . LYS A 320 ? 0.3887 0.4386 0.3894 -0.0255 0.0079 -0.0054 320 LYS A CG 2468 C CD . LYS A 320 ? 0.4949 0.5525 0.4965 -0.0269 0.0081 -0.0085 320 LYS A CD 2469 C CE . LYS A 320 ? 0.5450 0.6106 0.5477 -0.0240 0.0072 -0.0086 320 LYS A CE 2470 N NZ . LYS A 320 ? 0.5155 0.5816 0.5184 -0.0199 0.0062 -0.0070 320 LYS A NZ 2471 N N . TYR A 321 ? 0.2108 0.2525 0.2110 -0.0199 0.0065 0.0016 321 TYR A N 2472 C CA . TYR A 321 ? 0.2194 0.2625 0.2205 -0.0179 0.0061 0.0027 321 TYR A CA 2473 C C . TYR A 321 ? 0.2098 0.2577 0.2111 -0.0191 0.0063 0.0017 321 TYR A C 2474 O O . TYR A 321 ? 0.2137 0.2649 0.2159 -0.0172 0.0059 0.0020 321 TYR A O 2475 C CB . TYR A 321 ? 0.2120 0.2495 0.2125 -0.0171 0.0060 0.0044 321 TYR A CB 2476 C CG . TYR A 321 ? 0.2138 0.2478 0.2128 -0.0196 0.0067 0.0046 321 TYR A CG 2477 C CD1 . TYR A 321 ? 0.2150 0.2505 0.2137 -0.0209 0.0070 0.0045 321 TYR A CD1 2478 C CD2 . TYR A 321 ? 0.2104 0.2396 0.2080 -0.0207 0.0071 0.0049 321 TYR A CD2 2479 C CE1 . TYR A 321 ? 0.2276 0.2600 0.2247 -0.0232 0.0080 0.0048 321 TYR A CE1 2480 C CE2 . TYR A 321 ? 0.2175 0.2432 0.2134 -0.0228 0.0081 0.0052 321 TYR A CE2 2481 C CZ . TYR A 321 ? 0.2085 0.2358 0.2041 -0.0240 0.0086 0.0052 321 TYR A CZ 2482 O OH . TYR A 321 ? 0.2637 0.2874 0.2574 -0.0260 0.0098 0.0057 321 TYR A OH 2483 N N . GLN A 322 ? 0.2410 0.2887 0.2416 -0.0223 0.0071 0.0008 322 GLN A N 2484 C CA . GLN A 322 ? 0.2538 0.3061 0.2547 -0.0237 0.0074 -0.0002 322 GLN A CA 2485 C C . GLN A 322 ? 0.2325 0.2923 0.2345 -0.0228 0.0070 -0.0018 322 GLN A C 2486 O O . GLN A 322 ? 0.2546 0.3187 0.2573 -0.0214 0.0066 -0.0018 322 GLN A O 2487 C CB . GLN A 322 ? 0.2920 0.3424 0.2918 -0.0274 0.0086 -0.0010 322 GLN A CB 2488 C CG . GLN A 322 ? 0.3720 0.4272 0.3721 -0.0291 0.0091 -0.0020 322 GLN A CG 2489 C CD . GLN A 322 ? 0.4775 0.5313 0.4766 -0.0332 0.0107 -0.0032 322 GLN A CD 2490 O OE1 . GLN A 322 ? 0.5477 0.5955 0.5453 -0.0343 0.0117 -0.0019 322 GLN A OE1 2491 N NE2 . GLN A 322 ? 0.5271 0.5866 0.5271 -0.0354 0.0113 -0.0058 322 GLN A NE2 2492 N N . GLN A 323 ? 0.2378 0.2993 0.2401 -0.0233 0.0071 -0.0031 323 GLN A N 2493 C CA . GLN A 323 ? 0.2385 0.3078 0.2417 -0.0220 0.0067 -0.0047 323 GLN A CA 2494 C C . GLN A 323 ? 0.2342 0.3047 0.2379 -0.0176 0.0059 -0.0031 323 GLN A C 2495 O O . GLN A 323 ? 0.2071 0.2834 0.2113 -0.0158 0.0056 -0.0035 323 GLN A O 2496 C CB . GLN A 323 ? 0.2698 0.3411 0.2731 -0.0234 0.0070 -0.0066 323 GLN A CB 2497 C CG . GLN A 323 ? 0.3600 0.4404 0.3643 -0.0218 0.0065 -0.0083 323 GLN A CG 2498 C CD . GLN A 323 ? 0.4651 0.5491 0.4696 -0.0234 0.0068 -0.0108 323 GLN A CD 2499 O OE1 . GLN A 323 ? 0.5066 0.5855 0.5107 -0.0254 0.0073 -0.0112 323 GLN A OE1 2500 N NE2 . GLN A 323 ? 0.4833 0.5764 0.4886 -0.0223 0.0065 -0.0128 323 GLN A NE2 2501 N N . PHE A 324 ? 0.2001 0.2649 0.2035 -0.0158 0.0056 -0.0013 324 PHE A N 2502 C CA . PHE A 324 ? 0.1857 0.2508 0.1895 -0.0119 0.0053 0.0002 324 PHE A CA 2503 C C . PHE A 324 ? 0.1722 0.2383 0.1764 -0.0108 0.0053 0.0009 324 PHE A C 2504 O O . PHE A 324 ? 0.1827 0.2532 0.1873 -0.0081 0.0053 0.0010 324 PHE A O 2505 C CB . PHE A 324 ? 0.1816 0.2400 0.1851 -0.0106 0.0052 0.0019 324 PHE A CB 2506 C CG . PHE A 324 ? 0.1789 0.2367 0.1830 -0.0069 0.0053 0.0034 324 PHE A CG 2507 C CD1 . PHE A 324 ? 0.1711 0.2328 0.1753 -0.0040 0.0054 0.0036 324 PHE A CD1 2508 C CD2 . PHE A 324 ? 0.1812 0.2349 0.1856 -0.0063 0.0055 0.0047 324 PHE A CD2 2509 C CE1 . PHE A 324 ? 0.1807 0.2413 0.1851 -0.0006 0.0058 0.0051 324 PHE A CE1 2510 C CE2 . PHE A 324 ? 0.1809 0.2337 0.1858 -0.0032 0.0059 0.0058 324 PHE A CE2 2511 C CZ . PHE A 324 ? 0.1845 0.2403 0.1893 -0.0004 0.0062 0.0062 324 PHE A CZ 2512 N N . ILE A 325 ? 0.1739 0.2359 0.1780 -0.0125 0.0054 0.0014 325 ILE A N 2513 C CA . ILE A 325 ? 0.1661 0.2286 0.1705 -0.0115 0.0054 0.0020 325 ILE A CA 2514 C C . ILE A 325 ? 0.1599 0.2296 0.1646 -0.0121 0.0055 0.0005 325 ILE A C 2515 O O . ILE A 325 ? 0.1914 0.2641 0.1965 -0.0098 0.0054 0.0007 325 ILE A O 2516 C CB . ILE A 325 ? 0.1889 0.2465 0.1929 -0.0134 0.0055 0.0027 325 ILE A CB 2517 C CG1 . ILE A 325 ? 0.2144 0.2658 0.2183 -0.0122 0.0055 0.0041 325 ILE A CG1 2518 C CG2 . ILE A 325 ? 0.2116 0.2710 0.2161 -0.0129 0.0055 0.0028 325 ILE A CG2 2519 C CD1 . ILE A 325 ? 0.2085 0.2556 0.2116 -0.0141 0.0055 0.0046 325 ILE A CD1 2520 N N . SER A 326 ? 0.1639 0.2361 0.1683 -0.0152 0.0057 -0.0011 326 SER A N 2521 C CA . SER A 326 ? 0.1901 0.2697 0.1948 -0.0161 0.0057 -0.0028 326 SER A CA 2522 C C . SER A 326 ? 0.1915 0.2775 0.1967 -0.0129 0.0054 -0.0034 326 SER A C 2523 O O . SER A 326 ? 0.2040 0.2950 0.2095 -0.0113 0.0053 -0.0036 326 SER A O 2524 C CB . SER A 326 ? 0.1808 0.2615 0.1852 -0.0201 0.0063 -0.0046 326 SER A CB 2525 O OG . SER A 326 ? 0.1940 0.2821 0.1990 -0.0215 0.0065 -0.0065 326 SER A OG 2526 N N . ILE A 327 ? 0.1950 0.2814 0.2001 -0.0118 0.0053 -0.0035 327 ILE A N 2527 C CA . ILE A 327 ? 0.1784 0.2710 0.1836 -0.0084 0.0051 -0.0038 327 ILE A CA 2528 C C . ILE A 327 ? 0.1983 0.2894 0.2034 -0.0042 0.0051 -0.0017 327 ILE A C 2529 O O . ILE A 327 ? 0.1958 0.2924 0.2009 -0.0015 0.0052 -0.0019 327 ILE A O 2530 C CB . ILE A 327 ? 0.1933 0.2863 0.1983 -0.0083 0.0050 -0.0044 327 ILE A CB 2531 C CG1 . ILE A 327 ? 0.2147 0.3111 0.2200 -0.0125 0.0051 -0.0071 327 ILE A CG1 2532 C CG2 . ILE A 327 ? 0.1993 0.2976 0.2042 -0.0038 0.0048 -0.0040 327 ILE A CG2 2533 C CD1 . ILE A 327 ? 0.2909 0.3876 0.2961 -0.0131 0.0051 -0.0082 327 ILE A CD1 2534 N N . LEU A 328 ? 0.1671 0.2505 0.1722 -0.0034 0.0053 0.0002 328 LEU A N 2535 C CA . LEU A 328 ? 0.1864 0.2679 0.1915 0.0004 0.0058 0.0019 328 LEU A CA 2536 C C . LEU A 328 ? 0.1778 0.2611 0.1833 0.0005 0.0059 0.0017 328 LEU A C 2537 O O . LEU A 328 ? 0.1851 0.2708 0.1905 0.0039 0.0063 0.0023 328 LEU A O 2538 C CB . LEU A 328 ? 0.1815 0.2546 0.1867 0.0008 0.0061 0.0036 328 LEU A CB 2539 C CG . LEU A 328 ? 0.1953 0.2653 0.2008 0.0042 0.0070 0.0053 328 LEU A CG 2540 C CD1 . LEU A 328 ? 0.1952 0.2693 0.2000 0.0083 0.0076 0.0059 328 LEU A CD1 2541 C CD2 . LEU A 328 ? 0.1870 0.2497 0.1927 0.0040 0.0073 0.0064 328 LEU A CD2 2542 N N . THR A 329 ? 0.1764 0.2582 0.1822 -0.0030 0.0057 0.0010 329 THR A N 2543 C CA . THR A 329 ? 0.1803 0.2640 0.1864 -0.0032 0.0057 0.0007 329 THR A CA 2544 C C . THR A 329 ? 0.1900 0.2824 0.1960 -0.0020 0.0056 -0.0006 329 THR A C 2545 O O . THR A 329 ? 0.2032 0.2979 0.2093 0.0007 0.0059 -0.0002 329 THR A O 2546 C CB . THR A 329 ? 0.1925 0.2743 0.1986 -0.0072 0.0055 0.0001 329 THR A CB 2547 O OG1 . THR A 329 ? 0.2008 0.2752 0.2068 -0.0078 0.0056 0.0013 329 THR A OG1 2548 C CG2 . THR A 329 ? 0.1789 0.2630 0.1853 -0.0073 0.0056 -0.0002 329 THR A CG2 2549 N N . GLY A 330 ? 0.2004 0.2974 0.2063 -0.0038 0.0053 -0.0021 330 GLY A N 2550 C CA . GLY A 330 ? 0.2013 0.3076 0.2072 -0.0028 0.0052 -0.0038 330 GLY A CA 2551 C C . GLY A 330 ? 0.2088 0.3180 0.2142 0.0024 0.0054 -0.0028 330 GLY A C 2552 O O . GLY A 330 ? 0.2263 0.3413 0.2316 0.0048 0.0054 -0.0031 330 GLY A O 2553 N N . HIS A 331 ? 0.1904 0.2961 0.1954 0.0045 0.0056 -0.0014 331 HIS A N 2554 C CA . HIS A 331 ? 0.1969 0.3042 0.2011 0.0097 0.0061 0.0000 331 HIS A CA 2555 C C . HIS A 331 ? 0.2014 0.3053 0.2056 0.0124 0.0069 0.0016 331 HIS A C 2556 O O . HIS A 331 ? 0.2160 0.3239 0.2195 0.0164 0.0074 0.0021 331 HIS A O 2557 C CB . HIS A 331 ? 0.1946 0.2976 0.1984 0.0112 0.0064 0.0014 331 HIS A CB 2558 C CG . HIS A 331 ? 0.2152 0.3238 0.2188 0.0103 0.0058 -0.0002 331 HIS A CG 2559 N ND1 . HIS A 331 ? 0.2290 0.3340 0.2325 0.0092 0.0057 0.0000 331 HIS A ND1 2560 C CD2 . HIS A 331 ? 0.2121 0.3303 0.2156 0.0105 0.0054 -0.0023 331 HIS A CD2 2561 C CE1 . HIS A 331 ? 0.1923 0.3045 0.1958 0.0087 0.0052 -0.0019 331 HIS A CE1 2562 N NE2 . HIS A 331 ? 0.2598 0.3802 0.2633 0.0093 0.0050 -0.0035 331 HIS A NE2 2563 N N . VAL A 332 ? 0.1897 0.2860 0.1945 0.0105 0.0071 0.0024 332 VAL A N 2564 C CA . VAL A 332 ? 0.1915 0.2846 0.1965 0.0126 0.0080 0.0034 332 VAL A CA 2565 C C . VAL A 332 ? 0.2129 0.3120 0.2181 0.0125 0.0077 0.0022 332 VAL A C 2566 O O . VAL A 332 ? 0.2241 0.3251 0.2289 0.0161 0.0084 0.0028 332 VAL A O 2567 C CB . VAL A 332 ? 0.2011 0.2857 0.2070 0.0104 0.0082 0.0041 332 VAL A CB 2568 C CG1 . VAL A 332 ? 0.2378 0.3197 0.2442 0.0122 0.0091 0.0047 332 VAL A CG1 2569 C CG2 . VAL A 332 ? 0.2245 0.3038 0.2302 0.0113 0.0086 0.0054 332 VAL A CG2 2570 N N A ASN A 333 ? 0.2127 0.3148 0.2184 0.0085 0.0068 0.0005 333 ASN A N 2571 N N B ASN A 333 ? 0.2143 0.3163 0.2200 0.0084 0.0067 0.0005 333 ASN A N 2572 C CA . ASN A 333 ? 0.2230 0.3307 0.2289 0.0077 0.0065 -0.0008 333 ASN A CA 2573 C C . ASN A 333 ? 0.2326 0.3492 0.2379 0.0108 0.0064 -0.0016 333 ASN A C 2574 O O . ASN A 333 ? 0.2534 0.3741 0.2586 0.0125 0.0066 -0.0020 333 ASN A O 2575 C CB A ASN A 333 ? 0.2124 0.3222 0.2188 0.0024 0.0057 -0.0026 333 ASN A CB 2576 C CB B ASN A 333 ? 0.2160 0.3227 0.2226 0.0030 0.0060 -0.0019 333 ASN A CB 2577 C CG A ASN A 333 ? 0.1995 0.3022 0.2063 -0.0009 0.0057 -0.0021 333 ASN A CG 2578 C CG B ASN A 333 ? 0.2089 0.3081 0.2160 0.0024 0.0063 -0.0008 333 ASN A CG 2579 O OD1 A ASN A 333 ? 0.2191 0.3167 0.2263 0.0006 0.0061 -0.0009 333 ASN A OD1 2580 O OD1 B ASN A 333 ? 0.2106 0.3067 0.2178 0.0055 0.0070 0.0003 333 ASN A OD1 2581 N ND2 A ASN A 333 ? 0.1934 0.2961 0.2003 -0.0052 0.0054 -0.0032 333 ASN A ND2 2582 N ND2 B ASN A 333 ? 0.1928 0.2891 0.2002 -0.0014 0.0059 -0.0011 333 ASN A ND2 2583 N N . GLY A 334 ? 0.2141 0.3336 0.2188 0.0121 0.0063 -0.0017 334 GLY A N 2584 C CA . GLY A 334 ? 0.2384 0.3674 0.2424 0.0152 0.0062 -0.0026 334 GLY A CA 2585 C C . GLY A 334 ? 0.2555 0.3835 0.2582 0.0212 0.0072 -0.0004 334 GLY A C 2586 O O . GLY A 334 ? 0.2743 0.4100 0.2761 0.0249 0.0073 -0.0007 334 GLY A O 2587 N N . GLY A 335 ? 0.2379 0.3567 0.2405 0.0225 0.0082 0.0017 335 GLY A N 2588 C CA . GLY A 335 ? 0.2450 0.3614 0.2464 0.0280 0.0096 0.0040 335 GLY A CA 2589 C C . GLY A 335 ? 0.2441 0.3606 0.2444 0.0307 0.0100 0.0051 335 GLY A C 2590 O O . GLY A 335 ? 0.2829 0.3987 0.2818 0.0359 0.0114 0.0071 335 GLY A O 2591 N N . VAL A 336 ? 0.2373 0.3548 0.2382 0.0274 0.0089 0.0040 336 VAL A N 2592 C CA . VAL A 336 ? 0.2411 0.3594 0.2410 0.0294 0.0091 0.0048 336 VAL A CA 2593 C C . VAL A 336 ? 0.2503 0.3583 0.2500 0.0304 0.0103 0.0072 336 VAL A C 2594 O O . VAL A 336 ? 0.2733 0.3806 0.2719 0.0340 0.0112 0.0089 336 VAL A O 2595 C CB . VAL A 336 ? 0.2437 0.3665 0.2445 0.0251 0.0076 0.0024 336 VAL A CB 2596 C CG1 . VAL A 336 ? 0.2703 0.3932 0.2703 0.0266 0.0077 0.0031 336 VAL A CG1 2597 C CG2 . VAL A 336 ? 0.2637 0.3974 0.2646 0.0242 0.0067 -0.0003 336 VAL A CG2 2598 N N . ILE A 337 ? 0.2405 0.3411 0.2415 0.0268 0.0102 0.0072 337 ILE A N 2599 C CA . ILE A 337 ? 0.2363 0.3273 0.2375 0.0273 0.0115 0.0092 337 ILE A CA 2600 C C . ILE A 337 ? 0.2341 0.3206 0.2360 0.0278 0.0125 0.0096 337 ILE A C 2601 O O . ILE A 337 ? 0.2578 0.3448 0.2607 0.0246 0.0116 0.0082 337 ILE A O 2602 C CB . ILE A 337 ? 0.2250 0.3114 0.2274 0.0227 0.0105 0.0085 337 ILE A CB 2603 C CG1 . ILE A 337 ? 0.2396 0.3298 0.2413 0.0224 0.0097 0.0080 337 ILE A CG1 2604 C CG2 . ILE A 337 ? 0.2475 0.3244 0.2504 0.0229 0.0117 0.0101 337 ILE A CG2 2605 C CD1 . ILE A 337 ? 0.2510 0.3381 0.2537 0.0178 0.0087 0.0070 337 ILE A CD1 2606 N N . PRO A 338 ? 0.2254 0.3075 0.2265 0.0317 0.0145 0.0116 338 PRO A N 2607 C CA . PRO A 338 ? 0.2360 0.3142 0.2377 0.0322 0.0156 0.0117 338 PRO A CA 2608 C C . PRO A 338 ? 0.2365 0.3073 0.2400 0.0283 0.0157 0.0112 338 PRO A C 2609 O O . PRO A 338 ? 0.2280 0.2948 0.2320 0.0266 0.0155 0.0116 338 PRO A O 2610 C CB . PRO A 338 ? 0.2522 0.3272 0.2525 0.0375 0.0182 0.0139 338 PRO A CB 2611 C CG . PRO A 338 ? 0.2641 0.3378 0.2635 0.0387 0.0184 0.0153 338 PRO A CG 2612 C CD . PRO A 338 ? 0.2366 0.3168 0.2362 0.0358 0.0160 0.0137 338 PRO A CD 2613 N N . MET A 339 ? 0.2426 0.3122 0.2471 0.0271 0.0158 0.0103 339 MET A N 2614 C CA . MET A 339 ? 0.2410 0.3043 0.2473 0.0240 0.0160 0.0097 339 MET A CA 2615 C C . MET A 339 ? 0.2488 0.3044 0.2553 0.0254 0.0181 0.0111 339 MET A C 2616 O O . MET A 339 ? 0.2368 0.2880 0.2445 0.0226 0.0179 0.0106 339 MET A O 2617 C CB . MET A 339 ? 0.2561 0.3200 0.2634 0.0230 0.0160 0.0085 339 MET A CB 2618 C CG . MET A 339 ? 0.3036 0.3731 0.3112 0.0195 0.0138 0.0069 339 MET A CG 2619 S SD . MET A 339 ? 0.4056 0.4728 0.4138 0.0147 0.0121 0.0063 339 MET A SD 2620 C CE . MET A 339 ? 0.2093 0.2691 0.2190 0.0138 0.0132 0.0063 339 MET A CE 2621 N N . SER A 340 ? 0.2357 0.2898 0.2410 0.0297 0.0202 0.0127 340 SER A N 2622 C CA . SER A 340 ? 0.2465 0.2930 0.2520 0.0311 0.0226 0.0140 340 SER A CA 2623 C C . SER A 340 ? 0.2511 0.2961 0.2566 0.0295 0.0218 0.0145 340 SER A C 2624 O O . SER A 340 ? 0.2479 0.2869 0.2545 0.0282 0.0228 0.0147 340 SER A O 2625 C CB . SER A 340 ? 0.2612 0.3067 0.2648 0.0366 0.0252 0.0161 340 SER A CB 2626 O OG . SER A 340 ? 0.2717 0.3232 0.2733 0.0392 0.0243 0.0171 340 SER A OG 2627 N N . ARG A 341 ? 0.2217 0.2724 0.2262 0.0294 0.0199 0.0146 341 ARG A N 2628 C CA . ARG A 341 ? 0.2082 0.2579 0.2126 0.0280 0.0190 0.0150 341 ARG A CA 2629 C C . ARG A 341 ? 0.2038 0.2515 0.2098 0.0232 0.0174 0.0134 341 ARG A C 2630 O O . ARG A 341 ? 0.2000 0.2429 0.2066 0.0219 0.0178 0.0137 341 ARG A O 2631 C CB . ARG A 341 ? 0.2199 0.2769 0.2227 0.0293 0.0176 0.0150 341 ARG A CB 2632 C CG . ARG A 341 ? 0.2257 0.2826 0.2281 0.0285 0.0168 0.0154 341 ARG A CG 2633 C CD . ARG A 341 ? 0.2332 0.2850 0.2350 0.0315 0.0190 0.0176 341 ARG A CD 2634 N NE . ARG A 341 ? 0.2165 0.2605 0.2197 0.0294 0.0200 0.0177 341 ARG A NE 2635 C CZ . ARG A 341 ? 0.2163 0.2582 0.2205 0.0261 0.0188 0.0169 341 ARG A CZ 2636 N NH1 . ARG A 341 ? 0.2113 0.2576 0.2151 0.0244 0.0167 0.0161 341 ARG A NH1 2637 N NH2 . ARG A 341 ? 0.2313 0.2668 0.2368 0.0244 0.0198 0.0168 341 ARG A NH2 2638 N N . ILE A 342 ? 0.2021 0.2533 0.2087 0.0206 0.0158 0.0118 342 ILE A N 2639 C CA . ILE A 342 ? 0.1928 0.2422 0.2007 0.0163 0.0145 0.0105 342 ILE A CA 2640 C C . ILE A 342 ? 0.1978 0.2409 0.2071 0.0158 0.0159 0.0104 342 ILE A C 2641 O O . ILE A 342 ? 0.1817 0.2213 0.1918 0.0136 0.0155 0.0101 342 ILE A O 2642 C CB . ILE A 342 ? 0.2005 0.2546 0.2086 0.0142 0.0130 0.0090 342 ILE A CB 2643 C CG1 . ILE A 342 ? 0.2018 0.2627 0.2088 0.0142 0.0117 0.0087 342 ILE A CG1 2644 C CG2 . ILE A 342 ? 0.1964 0.2485 0.2055 0.0102 0.0118 0.0080 342 ILE A CG2 2645 C CD1 . ILE A 342 ? 0.1990 0.2597 0.2054 0.0127 0.0108 0.0088 342 ILE A CD1 2646 N N . ASP A 343 ? 0.2039 0.2458 0.2136 0.0178 0.0176 0.0104 343 ASP A N 2647 C CA . ASP A 343 ? 0.2050 0.2416 0.2163 0.0170 0.0191 0.0098 343 ASP A CA 2648 C C . ASP A 343 ? 0.2162 0.2472 0.2277 0.0178 0.0208 0.0108 343 ASP A C 2649 O O . ASP A 343 ? 0.2045 0.2318 0.2176 0.0157 0.0212 0.0099 343 ASP A O 2650 C CB . ASP A 343 ? 0.2106 0.2470 0.2222 0.0191 0.0208 0.0095 343 ASP A CB 2651 C CG . ASP A 343 ? 0.2160 0.2569 0.2280 0.0174 0.0192 0.0080 343 ASP A CG 2652 O OD1 . ASP A 343 ? 0.2083 0.2520 0.2204 0.0144 0.0170 0.0071 343 ASP A OD1 2653 O OD2 . ASP A 343 ? 0.2517 0.2930 0.2638 0.0192 0.0204 0.0076 343 ASP A OD2 2654 N N . ASP A 344 ? 0.2164 0.2473 0.2264 0.0208 0.0217 0.0126 344 ASP A N 2655 C CA . ASP A 344 ? 0.2067 0.2326 0.2168 0.0217 0.0235 0.0138 344 ASP A CA 2656 C C . ASP A 344 ? 0.2139 0.2397 0.2245 0.0187 0.0215 0.0132 344 ASP A C 2657 O O . ASP A 344 ? 0.1897 0.2111 0.2015 0.0173 0.0223 0.0129 344 ASP A O 2658 C CB . ASP A 344 ? 0.2238 0.2506 0.2317 0.0259 0.0247 0.0160 344 ASP A CB 2659 C CG . ASP A 344 ? 0.2216 0.2438 0.2294 0.0268 0.0263 0.0174 344 ASP A CG 2660 O OD1 . ASP A 344 ? 0.2707 0.2872 0.2796 0.0267 0.0287 0.0174 344 ASP A OD1 2661 O OD2 . ASP A 344 ? 0.2564 0.2810 0.2629 0.0275 0.0252 0.0183 344 ASP A OD2 2662 N N . ALA A 345 ? 0.1961 0.2268 0.2058 0.0176 0.0191 0.0130 345 ALA A N 2663 C CA . ALA A 345 ? 0.1894 0.2200 0.1993 0.0150 0.0174 0.0126 345 ALA A CA 2664 C C . ALA A 345 ? 0.1858 0.2140 0.1973 0.0119 0.0168 0.0111 345 ALA A C 2665 O O . ALA A 345 ? 0.1927 0.2177 0.2049 0.0106 0.0169 0.0110 345 ALA A O 2666 C CB . ALA A 345 ? 0.1811 0.2171 0.1897 0.0141 0.0152 0.0123 345 ALA A CB 2667 N N . VAL A 346 ? 0.1788 0.2089 0.1908 0.0108 0.0163 0.0100 346 VAL A N 2668 C CA . VAL A 346 ? 0.1828 0.2118 0.1962 0.0081 0.0157 0.0085 346 VAL A CA 2669 C C . VAL A 346 ? 0.1856 0.2099 0.2007 0.0083 0.0178 0.0079 346 VAL A C 2670 O O . VAL A 346 ? 0.1869 0.2096 0.2033 0.0064 0.0175 0.0069 346 VAL A O 2671 C CB . VAL A 346 ? 0.1743 0.2071 0.1878 0.0070 0.0146 0.0074 346 VAL A CB 2672 C CG1 . VAL A 346 ? 0.1827 0.2147 0.1975 0.0046 0.0140 0.0059 346 VAL A CG1 2673 C CG2 . VAL A 346 ? 0.1942 0.2312 0.2062 0.0062 0.0127 0.0077 346 VAL A CG2 2674 N N . THR A 347 ? 0.1955 0.2180 0.2108 0.0107 0.0200 0.0084 347 THR A N 2675 C CA . THR A 347 ? 0.1900 0.2079 0.2071 0.0108 0.0225 0.0077 347 THR A CA 2676 C C . THR A 347 ? 0.1814 0.1962 0.1987 0.0101 0.0228 0.0082 347 THR A C 2677 O O . THR A 347 ? 0.1950 0.2076 0.2141 0.0083 0.0234 0.0068 347 THR A O 2678 C CB . THR A 347 ? 0.2103 0.2259 0.2268 0.0139 0.0252 0.0088 347 THR A CB 2679 O OG1 . THR A 347 ? 0.2121 0.2302 0.2289 0.0142 0.0251 0.0078 347 THR A OG1 2680 C CG2 . THR A 347 ? 0.2281 0.2378 0.2463 0.0140 0.0284 0.0083 347 THR A CG2 2681 N N . ARG A 348 ? 0.1787 0.1939 0.1943 0.0116 0.0224 0.0100 348 ARG A N 2682 C CA . ARG A 348 ? 0.1709 0.1833 0.1867 0.0114 0.0228 0.0107 348 ARG A CA 2683 C C . ARG A 348 ? 0.1778 0.1914 0.1941 0.0085 0.0205 0.0095 348 ARG A C 2684 O O . ARG A 348 ? 0.1772 0.1883 0.1947 0.0073 0.0211 0.0088 348 ARG A O 2685 C CB . ARG A 348 ? 0.1790 0.1924 0.1927 0.0138 0.0228 0.0128 348 ARG A CB 2686 C CG . ARG A 348 ? 0.1816 0.1930 0.1945 0.0174 0.0255 0.0144 348 ARG A CG 2687 C CD . ARG A 348 ? 0.1816 0.1962 0.1921 0.0202 0.0250 0.0163 348 ARG A CD 2688 N NE . ARG A 348 ? 0.1994 0.2115 0.2090 0.0240 0.0280 0.0181 348 ARG A NE 2689 C CZ . ARG A 348 ? 0.2163 0.2238 0.2257 0.0255 0.0305 0.0194 348 ARG A CZ 2690 N NH1 . ARG A 348 ? 0.2046 0.2101 0.2147 0.0235 0.0301 0.0191 348 ARG A NH1 2691 N NH2 . ARG A 348 ? 0.2371 0.2418 0.2453 0.0290 0.0335 0.0211 348 ARG A NH2 2692 N N . ILE A 349 ? 0.1665 0.1840 0.1818 0.0074 0.0181 0.0093 349 ILE A N 2693 C CA . ILE A 349 ? 0.1623 0.1806 0.1777 0.0050 0.0161 0.0085 349 ILE A CA 2694 C C . ILE A 349 ? 0.1695 0.1871 0.1868 0.0033 0.0164 0.0066 349 ILE A C 2695 O O . ILE A 349 ? 0.1705 0.1867 0.1886 0.0020 0.0162 0.0058 349 ILE A O 2696 C CB . ILE A 349 ? 0.1599 0.1821 0.1738 0.0041 0.0139 0.0086 349 ILE A CB 2697 C CG1 . ILE A 349 ? 0.1644 0.1879 0.1767 0.0055 0.0135 0.0100 349 ILE A CG1 2698 C CG2 . ILE A 349 ? 0.1612 0.1838 0.1750 0.0017 0.0122 0.0078 349 ILE A CG2 2699 C CD1 . ILE A 349 ? 0.1930 0.2208 0.2039 0.0050 0.0120 0.0100 349 ILE A CD1 2700 N N . LEU A 350 ? 0.1745 0.1933 0.1926 0.0033 0.0169 0.0057 350 LEU A N 2701 C CA . LEU A 350 ? 0.1721 0.1907 0.1921 0.0018 0.0174 0.0036 350 LEU A CA 2702 C C . LEU A 350 ? 0.1740 0.1890 0.1958 0.0019 0.0197 0.0027 350 LEU A C 2703 O O . LEU A 350 ? 0.1852 0.2003 0.2086 0.0003 0.0197 0.0009 350 LEU A O 2704 C CB . LEU A 350 ? 0.1700 0.1906 0.1906 0.0020 0.0178 0.0026 350 LEU A CB 2705 C CG . LEU A 350 ? 0.1680 0.1925 0.1870 0.0014 0.0156 0.0030 350 LEU A CG 2706 C CD1 . LEU A 350 ? 0.1848 0.2112 0.2047 0.0017 0.0162 0.0019 350 LEU A CD1 2707 C CD2 . LEU A 350 ? 0.1824 0.2087 0.2011 -0.0005 0.0136 0.0024 350 LEU A CD2 2708 N N . ARG A 351 ? 0.1832 0.1952 0.2048 0.0037 0.0219 0.0039 351 ARG A N 2709 C CA . ARG A 351 ? 0.1849 0.1930 0.2084 0.0036 0.0245 0.0032 351 ARG A CA 2710 C C . ARG A 351 ? 0.1816 0.1893 0.2054 0.0024 0.0237 0.0030 351 ARG A C 2711 O O . ARG A 351 ? 0.1746 0.1814 0.2004 0.0009 0.0246 0.0010 351 ARG A O 2712 C CB . ARG A 351 ? 0.1803 0.1849 0.2028 0.0062 0.0270 0.0051 351 ARG A CB 2713 C CG . ARG A 351 ? 0.1898 0.1896 0.2140 0.0060 0.0303 0.0044 351 ARG A CG 2714 C CD . ARG A 351 ? 0.1977 0.1937 0.2207 0.0090 0.0331 0.0067 351 ARG A CD 2715 N NE . ARG A 351 ? 0.2024 0.1980 0.2252 0.0105 0.0345 0.0067 351 ARG A NE 2716 C CZ . ARG A 351 ? 0.2144 0.2111 0.2349 0.0134 0.0343 0.0088 351 ARG A CZ 2717 N NH1 . ARG A 351 ? 0.2212 0.2197 0.2394 0.0153 0.0330 0.0111 351 ARG A NH1 2718 N NH2 . ARG A 351 ? 0.2284 0.2247 0.2490 0.0146 0.0357 0.0084 351 ARG A NH2 2719 N N . VAL A 352 ? 0.1782 0.1867 0.1999 0.0030 0.0219 0.0048 352 VAL A N 2720 C CA . VAL A 352 ? 0.1673 0.1754 0.1891 0.0021 0.0210 0.0047 352 VAL A CA 2721 C C . VAL A 352 ? 0.1627 0.1735 0.1853 0.0000 0.0192 0.0028 352 VAL A C 2722 O O . VAL A 352 ? 0.1632 0.1737 0.1873 -0.0011 0.0196 0.0014 352 VAL A O 2723 C CB . VAL A 352 ? 0.1641 0.1728 0.1836 0.0031 0.0195 0.0069 352 VAL A CB 2724 C CG1 . VAL A 352 ? 0.1806 0.1893 0.1999 0.0021 0.0181 0.0067 352 VAL A CG1 2725 C CG2 . VAL A 352 ? 0.1775 0.1838 0.1963 0.0055 0.0215 0.0087 352 VAL A CG2 2726 N N . LYS A 353 ? 0.1556 0.1694 0.1773 -0.0004 0.0174 0.0027 353 LYS A N 2727 C CA . LYS A 353 ? 0.1547 0.1712 0.1768 -0.0020 0.0158 0.0012 353 LYS A CA 2728 C C . LYS A 353 ? 0.1674 0.1845 0.1921 -0.0030 0.0171 -0.0014 353 LYS A C 2729 O O . LYS A 353 ? 0.1722 0.1907 0.1977 -0.0040 0.0166 -0.0029 353 LYS A O 2730 C CB . LYS A 353 ? 0.1603 0.1796 0.1808 -0.0021 0.0140 0.0017 353 LYS A CB 2731 C CG . LYS A 353 ? 0.1538 0.1731 0.1718 -0.0018 0.0124 0.0037 353 LYS A CG 2732 C CD . LYS A 353 ? 0.1516 0.1737 0.1682 -0.0023 0.0109 0.0040 353 LYS A CD 2733 C CE . LYS A 353 ? 0.1402 0.1622 0.1546 -0.0024 0.0096 0.0055 353 LYS A CE 2734 N NZ . LYS A 353 ? 0.1407 0.1652 0.1537 -0.0033 0.0084 0.0057 353 LYS A NZ 2735 N N . PHE A 354 ? 0.1716 0.1881 0.1976 -0.0027 0.0188 -0.0022 354 PHE A N 2736 C CA . PHE A 354 ? 0.1669 0.1841 0.1956 -0.0040 0.0203 -0.0051 354 PHE A CA 2737 C C . PHE A 354 ? 0.1686 0.1832 0.1991 -0.0045 0.0223 -0.0062 354 PHE A C 2738 O O . PHE A 354 ? 0.1802 0.1969 0.2126 -0.0059 0.0224 -0.0087 354 PHE A O 2739 C CB . PHE A 354 ? 0.1736 0.1899 0.2032 -0.0035 0.0221 -0.0058 354 PHE A CB 2740 C CG . PHE A 354 ? 0.1667 0.1867 0.1956 -0.0036 0.0205 -0.0061 354 PHE A CG 2741 C CD1 . PHE A 354 ? 0.1657 0.1898 0.1956 -0.0050 0.0192 -0.0083 354 PHE A CD1 2742 C CD2 . PHE A 354 ? 0.1654 0.1852 0.1926 -0.0022 0.0202 -0.0043 354 PHE A CD2 2743 C CE1 . PHE A 354 ? 0.1774 0.2049 0.2065 -0.0050 0.0177 -0.0085 354 PHE A CE1 2744 C CE2 . PHE A 354 ? 0.1703 0.1937 0.1970 -0.0025 0.0188 -0.0047 354 PHE A CE2 2745 C CZ . PHE A 354 ? 0.1662 0.1932 0.1937 -0.0039 0.0176 -0.0067 354 PHE A CZ 2746 N N . THR A 355 ? 0.1767 0.1873 0.2066 -0.0033 0.0239 -0.0044 355 THR A N 2747 C CA . THR A 355 ? 0.1833 0.1909 0.2148 -0.0038 0.0263 -0.0051 355 THR A CA 2748 C C . THR A 355 ? 0.1820 0.1917 0.2136 -0.0048 0.0247 -0.0058 355 THR A C 2749 O O . THR A 355 ? 0.1917 0.2018 0.2257 -0.0062 0.0260 -0.0082 355 THR A O 2750 C CB . THR A 355 ? 0.1980 0.2012 0.2281 -0.0019 0.0280 -0.0024 355 THR A CB 2751 O OG1 . THR A 355 ? 0.2030 0.2041 0.2329 -0.0006 0.0299 -0.0018 355 THR A OG1 2752 C CG2 . THR A 355 ? 0.2176 0.2175 0.2491 -0.0023 0.0305 -0.0028 355 THR A CG2 2753 N N . MET A 356 ? 0.1766 0.1881 0.2059 -0.0042 0.0219 -0.0040 356 MET A N 2754 C CA . MET A 356 ? 0.1831 0.1961 0.2120 -0.0046 0.0203 -0.0043 356 MET A CA 2755 C C . MET A 356 ? 0.1760 0.1935 0.2058 -0.0058 0.0188 -0.0066 356 MET A C 2756 O O . MET A 356 ? 0.1896 0.2088 0.2192 -0.0060 0.0177 -0.0071 356 MET A O 2757 C CB . MET A 356 ? 0.1766 0.1890 0.2025 -0.0035 0.0183 -0.0015 356 MET A CB 2758 C CG . MET A 356 ? 0.1749 0.1899 0.1989 -0.0033 0.0159 -0.0007 356 MET A CG 2759 S SD . MET A 356 ? 0.1833 0.1970 0.2041 -0.0022 0.0142 0.0023 356 MET A SD 2760 C CE . MET A 356 ? 0.1960 0.2099 0.2165 -0.0024 0.0131 0.0021 356 MET A CE 2761 N N . GLY A 357 ? 0.1596 0.1794 0.1903 -0.0063 0.0188 -0.0081 357 GLY A N 2762 C CA . GLY A 357 ? 0.1726 0.1973 0.2040 -0.0071 0.0175 -0.0102 357 GLY A CA 2763 C C . GLY A 357 ? 0.1792 0.2063 0.2078 -0.0064 0.0147 -0.0087 357 GLY A C 2764 O O . GLY A 357 ? 0.1787 0.2098 0.2073 -0.0066 0.0135 -0.0100 357 GLY A O 2891 N N . LYS A 374 ? 0.1728 0.2140 0.1858 0.0112 -0.0021 -0.0087 374 LYS A N 2892 C CA . LYS A 374 ? 0.1804 0.2256 0.1948 0.0114 -0.0022 -0.0120 374 LYS A CA 2893 C C . LYS A 374 ? 0.1656 0.2093 0.1812 0.0100 -0.0017 -0.0135 374 LYS A C 2894 O O . LYS A 374 ? 0.1596 0.1996 0.1754 0.0084 -0.0008 -0.0128 374 LYS A O 2895 C CB . LYS A 374 ? 0.2186 0.2657 0.2339 0.0104 -0.0012 -0.0143 374 LYS A CB 2896 C CG . LYS A 374 ? 0.3145 0.3663 0.3295 0.0119 -0.0018 -0.0153 374 LYS A CG 2897 C CD . LYS A 374 ? 0.3083 0.3620 0.3249 0.0104 -0.0005 -0.0186 374 LYS A CD 2898 C CE . LYS A 374 ? 0.3434 0.3927 0.3606 0.0079 0.0014 -0.0189 374 LYS A CE 2899 N NZ . LYS A 374 ? 0.3955 0.4469 0.4139 0.0069 0.0027 -0.0219 374 LYS A NZ 2900 N N . GLN A 375 ? 0.1716 0.2185 0.1881 0.0108 -0.0023 -0.0155 375 GLN A N 2901 C CA . GLN A 375 ? 0.1658 0.2118 0.1836 0.0095 -0.0018 -0.0170 375 GLN A CA 2902 C C . GLN A 375 ? 0.1633 0.2076 0.1824 0.0070 0.0000 -0.0190 375 GLN A C 2903 O O . GLN A 375 ? 0.1621 0.2030 0.1814 0.0058 0.0007 -0.0186 375 GLN A O 2904 C CB . GLN A 375 ? 0.1921 0.2429 0.2107 0.0109 -0.0027 -0.0195 375 GLN A CB 2905 C CG . GLN A 375 ? 0.2025 0.2523 0.2223 0.0099 -0.0025 -0.0207 375 GLN A CG 2906 C CD . GLN A 375 ? 0.2549 0.3000 0.2734 0.0101 -0.0029 -0.0175 375 GLN A CD 2907 O OE1 . GLN A 375 ? 0.2977 0.3420 0.3147 0.0119 -0.0038 -0.0151 375 GLN A OE1 2908 N NE2 . GLN A 375 ? 0.2208 0.2623 0.2399 0.0082 -0.0019 -0.0175 375 GLN A NE2 2909 N N . GLU A 376 ? 0.1708 0.2170 0.1906 0.0064 0.0009 -0.0209 376 GLU A N 2910 C CA . GLU A 376 ? 0.1834 0.2273 0.2042 0.0041 0.0031 -0.0227 376 GLU A CA 2911 C C . GLU A 376 ? 0.1702 0.2084 0.1895 0.0035 0.0039 -0.0197 376 GLU A C 2912 O O . GLU A 376 ? 0.1812 0.2160 0.2006 0.0021 0.0056 -0.0201 376 GLU A O 2913 C CB . GLU A 376 ? 0.2038 0.2504 0.2254 0.0036 0.0040 -0.0251 376 GLU A CB 2914 C CG . GLU A 376 ? 0.2761 0.3295 0.2995 0.0042 0.0033 -0.0287 376 GLU A CG 2915 C CD . GLU A 376 ? 0.2959 0.3538 0.3182 0.0070 0.0010 -0.0277 376 GLU A CD 2916 O OE1 . GLU A 376 ? 0.2233 0.2792 0.2436 0.0087 -0.0003 -0.0240 376 GLU A OE1 2917 O OE2 . GLU A 376 ? 0.3959 0.4599 0.4195 0.0077 0.0007 -0.0309 376 GLU A OE2 2918 N N . HIS A 377 ? 0.1567 0.1939 0.1743 0.0047 0.0029 -0.0167 377 HIS A N 2919 C CA . HIS A 377 ? 0.1434 0.1764 0.1596 0.0044 0.0034 -0.0141 377 HIS A CA 2920 C C . HIS A 377 ? 0.1430 0.1738 0.1589 0.0044 0.0028 -0.0126 377 HIS A C 2921 O O . HIS A 377 ? 0.1419 0.1696 0.1573 0.0037 0.0038 -0.0117 377 HIS A O 2922 C CB . HIS A 377 ? 0.1539 0.1870 0.1688 0.0055 0.0025 -0.0116 377 HIS A CB 2923 C CG . HIS A 377 ? 0.1720 0.2071 0.1869 0.0056 0.0030 -0.0125 377 HIS A CG 2924 N ND1 . HIS A 377 ? 0.2198 0.2559 0.2358 0.0046 0.0045 -0.0155 377 HIS A ND1 2925 C CD2 . HIS A 377 ? 0.1420 0.1782 0.1559 0.0066 0.0023 -0.0110 377 HIS A CD2 2926 C CE1 . HIS A 377 ? 0.1861 0.2239 0.2017 0.0051 0.0045 -0.0157 377 HIS A CE1 2927 N NE2 . HIS A 377 ? 0.2185 0.2565 0.2329 0.0064 0.0031 -0.0129 377 HIS A NE2 2928 N N . ARG A 378 ? 0.1431 0.1758 0.1595 0.0053 0.0013 -0.0126 378 ARG A N 2929 C CA . ARG A 378 ? 0.1504 0.1811 0.1667 0.0051 0.0009 -0.0117 378 ARG A CA 2930 C C . ARG A 378 ? 0.1506 0.1806 0.1680 0.0039 0.0021 -0.0139 378 ARG A C 2931 O O . ARG A 378 ? 0.1598 0.1871 0.1769 0.0034 0.0025 -0.0130 378 ARG A O 2932 C CB . ARG A 378 ? 0.1381 0.1707 0.1543 0.0066 -0.0007 -0.0111 378 ARG A CB 2933 C CG . ARG A 378 ? 0.1456 0.1779 0.1605 0.0078 -0.0014 -0.0087 378 ARG A CG 2934 C CD . ARG A 378 ? 0.1470 0.1799 0.1615 0.0093 -0.0025 -0.0078 378 ARG A CD 2935 N NE . ARG A 378 ? 0.1559 0.1885 0.1690 0.0105 -0.0028 -0.0055 378 ARG A NE 2936 C CZ . ARG A 378 ? 0.1559 0.1857 0.1684 0.0101 -0.0026 -0.0033 378 ARG A CZ 2937 N NH1 . ARG A 378 ? 0.1671 0.1945 0.1802 0.0087 -0.0023 -0.0031 378 ARG A NH1 2938 N NH2 . ARG A 378 ? 0.1696 0.1993 0.1810 0.0112 -0.0026 -0.0015 378 ARG A NH2 2939 N N . ASP A 379 ? 0.1535 0.1861 0.1723 0.0034 0.0028 -0.0168 379 ASP A N 2940 C CA . ASP A 379 ? 0.1595 0.1912 0.1795 0.0018 0.0044 -0.0191 379 ASP A CA 2941 C C . ASP A 379 ? 0.1514 0.1787 0.1703 0.0008 0.0066 -0.0182 379 ASP A C 2942 O O . ASP A 379 ? 0.1587 0.1835 0.1775 0.0002 0.0077 -0.0182 379 ASP A O 2943 C CB . ASP A 379 ? 0.1735 0.2091 0.1953 0.0012 0.0051 -0.0227 379 ASP A CB 2944 C CG . ASP A 379 ? 0.1964 0.2368 0.2191 0.0025 0.0032 -0.0240 379 ASP A CG 2945 O OD1 . ASP A 379 ? 0.2243 0.2641 0.2462 0.0037 0.0017 -0.0221 379 ASP A OD1 2946 O OD2 . ASP A 379 ? 0.2497 0.2945 0.2738 0.0024 0.0033 -0.0271 379 ASP A OD2 2947 N N . LEU A 380 ? 0.1423 0.1689 0.1603 0.0010 0.0071 -0.0173 380 LEU A N 2948 C CA . LEU A 380 ? 0.1439 0.1665 0.1604 0.0007 0.0091 -0.0161 380 LEU A CA 2949 C C . LEU A 380 ? 0.1558 0.1760 0.1708 0.0015 0.0083 -0.0133 380 LEU A C 2950 O O . LEU A 380 ? 0.1537 0.1709 0.1677 0.0013 0.0098 -0.0128 380 LEU A O 2951 C CB . LEU A 380 ? 0.1601 0.1830 0.1759 0.0010 0.0095 -0.0158 380 LEU A CB 2952 C CG . LEU A 380 ? 0.1629 0.1819 0.1768 0.0012 0.0114 -0.0141 380 LEU A CG 2953 C CD1 . LEU A 380 ? 0.1982 0.2141 0.2122 0.0000 0.0146 -0.0159 380 LEU A CD1 2954 C CD2 . LEU A 380 ? 0.1683 0.1881 0.1815 0.0017 0.0114 -0.0136 380 LEU A CD2 2955 N N . ALA A 381 ? 0.1460 0.1678 0.1608 0.0025 0.0061 -0.0115 381 ALA A N 2956 C CA . ALA A 381 ? 0.1468 0.1670 0.1605 0.0030 0.0054 -0.0093 381 ALA A CA 2957 C C . ALA A 381 ? 0.1423 0.1616 0.1565 0.0026 0.0054 -0.0099 381 ALA A C 2958 O O . ALA A 381 ? 0.1462 0.1637 0.1595 0.0028 0.0059 -0.0088 381 ALA A O 2959 C CB . ALA A 381 ? 0.1382 0.1601 0.1519 0.0038 0.0034 -0.0077 381 ALA A CB 2960 N N . ARG A 382 ? 0.1477 0.1688 0.1635 0.0022 0.0049 -0.0117 382 ARG A N 2961 C CA . ARG A 382 ? 0.1477 0.1683 0.1642 0.0018 0.0050 -0.0126 382 ARG A CA 2962 C C . ARG A 382 ? 0.1559 0.1739 0.1719 0.0010 0.0074 -0.0135 382 ARG A C 2963 O O . ARG A 382 ? 0.1608 0.1771 0.1763 0.0011 0.0078 -0.0128 382 ARG A O 2964 C CB . ARG A 382 ? 0.1513 0.1750 0.1694 0.0018 0.0040 -0.0145 382 ARG A CB 2965 C CG . ARG A 382 ? 0.1539 0.1777 0.1729 0.0013 0.0040 -0.0159 382 ARG A CG 2966 C CD . ARG A 382 ? 0.1588 0.1863 0.1792 0.0018 0.0028 -0.0177 382 ARG A CD 2967 N NE . ARG A 382 ? 0.1609 0.1889 0.1824 0.0014 0.0029 -0.0193 382 ARG A NE 2968 C CZ . ARG A 382 ? 0.1820 0.2134 0.2045 0.0020 0.0019 -0.0209 382 ARG A CZ 2969 N NH1 . ARG A 382 ? 0.2130 0.2474 0.2354 0.0033 0.0006 -0.0210 382 ARG A NH1 2970 N NH2 . ARG A 382 ? 0.1986 0.2305 0.2221 0.0016 0.0020 -0.0224 382 ARG A NH2 2971 N N . GLU A 383 ? 0.1484 0.1661 0.1646 0.0003 0.0092 -0.0150 383 GLU A N 2972 C CA . GLU A 383 ? 0.1530 0.1675 0.1685 -0.0005 0.0121 -0.0157 383 GLU A CA 2973 C C . GLU A 383 ? 0.1558 0.1673 0.1689 0.0007 0.0128 -0.0130 383 GLU A C 2974 O O . GLU A 383 ? 0.1660 0.1749 0.1780 0.0009 0.0142 -0.0125 383 GLU A O 2975 C CB . GLU A 383 ? 0.1624 0.1770 0.1786 -0.0014 0.0140 -0.0177 383 GLU A CB 2976 C CG . GLU A 383 ? 0.1938 0.2043 0.2091 -0.0021 0.0177 -0.0182 383 GLU A CG 2977 C CD . GLU A 383 ? 0.2339 0.2439 0.2496 -0.0031 0.0198 -0.0201 383 GLU A CD 2978 O OE1 . GLU A 383 ? 0.2679 0.2816 0.2851 -0.0034 0.0184 -0.0214 383 GLU A OE1 2979 O OE2 . GLU A 383 ? 0.2393 0.2451 0.2536 -0.0034 0.0230 -0.0200 383 GLU A OE2 2980 N N . ALA A 384 ? 0.1586 0.1706 0.1707 0.0017 0.0118 -0.0112 384 ALA A N 2981 C CA . ALA A 384 ? 0.1613 0.1713 0.1710 0.0030 0.0124 -0.0089 384 ALA A CA 2982 C C . ALA A 384 ? 0.1536 0.1641 0.1630 0.0037 0.0110 -0.0077 384 ALA A C 2983 O O . ALA A 384 ? 0.1617 0.1703 0.1692 0.0047 0.0121 -0.0067 384 ALA A O 2984 C CB . ALA A 384 ? 0.1774 0.1887 0.1865 0.0038 0.0114 -0.0076 384 ALA A CB 2985 N N . ALA A 385 ? 0.1422 0.1552 0.1532 0.0034 0.0086 -0.0079 385 ALA A N 2986 C CA . ALA A 385 ? 0.1492 0.1628 0.1602 0.0038 0.0073 -0.0072 385 ALA A CA 2987 C C . ALA A 385 ? 0.1505 0.1623 0.1612 0.0035 0.0086 -0.0080 385 ALA A C 2988 O O . ALA A 385 ? 0.1523 0.1634 0.1618 0.0044 0.0090 -0.0071 385 ALA A O 2989 C CB . ALA A 385 ? 0.1623 0.1781 0.1750 0.0033 0.0050 -0.0074 385 ALA A CB 2990 N N . ARG A 386 ? 0.1455 0.1571 0.1576 0.0024 0.0095 -0.0099 386 ARG A N 2991 C CA . ARG A 386 ? 0.1534 0.1634 0.1655 0.0020 0.0109 -0.0109 386 ARG A CA 2992 C C . ARG A 386 ? 0.1539 0.1606 0.1636 0.0027 0.0137 -0.0101 386 ARG A C 2993 O O . ARG A 386 ? 0.1723 0.1777 0.1808 0.0035 0.0145 -0.0095 386 ARG A O 2994 C CB . ARG A 386 ? 0.1643 0.1753 0.1785 0.0005 0.0115 -0.0135 386 ARG A CB 2995 C CG . ARG A 386 ? 0.1881 0.1976 0.2026 -0.0003 0.0133 -0.0149 386 ARG A CG 2996 C CD . ARG A 386 ? 0.2342 0.2410 0.2483 -0.0012 0.0168 -0.0163 386 ARG A CD 2997 N NE . ARG A 386 ? 0.2625 0.2712 0.2784 -0.0024 0.0170 -0.0184 386 ARG A NE 2998 C CZ . ARG A 386 ? 0.2977 0.3046 0.3137 -0.0035 0.0200 -0.0199 386 ARG A CZ 2999 N NH1 . ARG A 386 ? 0.3002 0.3026 0.3144 -0.0035 0.0232 -0.0193 386 ARG A NH1 3000 N NH2 . ARG A 386 ? 0.3531 0.3626 0.3710 -0.0046 0.0198 -0.0221 386 ARG A NH2 3001 N N . LYS A 387 ? 0.1565 0.1617 0.1653 0.0029 0.0154 -0.0098 387 LYS A N 3002 C CA . LYS A 387 ? 0.1672 0.1687 0.1733 0.0039 0.0184 -0.0088 387 LYS A CA 3003 C C . LYS A 387 ? 0.1707 0.1722 0.1743 0.0062 0.0178 -0.0063 387 LYS A C 3004 O O . LYS A 387 ? 0.1827 0.1815 0.1836 0.0077 0.0201 -0.0052 387 LYS A O 3005 C CB . LYS A 387 ? 0.1693 0.1690 0.1750 0.0034 0.0204 -0.0094 387 LYS A CB 3006 C CG . LYS A 387 ? 0.1754 0.1747 0.1834 0.0011 0.0221 -0.0124 387 LYS A CG 3007 C CD . LYS A 387 ? 0.2026 0.2007 0.2106 0.0005 0.0240 -0.0133 387 LYS A CD 3008 C CE . LYS A 387 ? 0.2257 0.2234 0.2360 -0.0019 0.0263 -0.0167 387 LYS A CE 3009 N NZ . LYS A 387 ? 0.2597 0.2557 0.2698 -0.0025 0.0286 -0.0177 387 LYS A NZ 3010 N N . SER A 388 ? 0.1638 0.1685 0.1681 0.0066 0.0149 -0.0056 388 SER A N 3011 C CA . SER A 388 ? 0.1602 0.1662 0.1626 0.0086 0.0141 -0.0037 388 SER A CA 3012 C C . SER A 388 ? 0.1563 0.1632 0.1585 0.0092 0.0134 -0.0036 388 SER A C 3013 O O . SER A 388 ? 0.1637 0.1717 0.1640 0.0112 0.0132 -0.0023 388 SER A O 3014 C CB . SER A 388 ? 0.1598 0.1690 0.1634 0.0084 0.0115 -0.0033 388 SER A CB 3015 O OG . SER A 388 ? 0.1614 0.1731 0.1673 0.0073 0.0091 -0.0040 388 SER A OG 3016 N N . LEU A 389 ? 0.1669 0.1740 0.1711 0.0078 0.0128 -0.0050 389 LEU A N 3017 C CA . LEU A 389 ? 0.1642 0.1728 0.1685 0.0082 0.0117 -0.0050 389 LEU A CA 3018 C C . LEU A 389 ? 0.1681 0.1744 0.1697 0.0099 0.0141 -0.0042 389 LEU A C 3019 O O . LEU A 389 ? 0.1915 0.1944 0.1922 0.0097 0.0168 -0.0045 389 LEU A O 3020 C CB . LEU A 389 ? 0.1638 0.1728 0.1707 0.0064 0.0108 -0.0068 389 LEU A CB 3021 C CG . LEU A 389 ? 0.1647 0.1755 0.1741 0.0049 0.0088 -0.0076 389 LEU A CG 3022 C CD1 . LEU A 389 ? 0.1660 0.1771 0.1773 0.0037 0.0083 -0.0093 389 LEU A CD1 3023 C CD2 . LEU A 389 ? 0.1699 0.1832 0.1798 0.0053 0.0065 -0.0068 389 LEU A CD2 3024 N N . VAL A 390 ? 0.1676 0.1759 0.1679 0.0117 0.0132 -0.0034 390 VAL A N 3025 C CA . VAL A 390 ? 0.1737 0.1801 0.1710 0.0138 0.0155 -0.0025 390 VAL A CA 3026 C C . VAL A 390 ? 0.1758 0.1840 0.1742 0.0135 0.0143 -0.0034 390 VAL A C 3027 O O . VAL A 390 ? 0.1884 0.2003 0.1879 0.0137 0.0119 -0.0037 390 VAL A O 3028 C CB . VAL A 390 ? 0.1704 0.1783 0.1647 0.0168 0.0158 -0.0008 390 VAL A CB 3029 C CG1 . VAL A 390 ? 0.1918 0.1979 0.1826 0.0195 0.0182 0.0004 390 VAL A CG1 3030 C CG2 . VAL A 390 ? 0.1834 0.1893 0.1766 0.0171 0.0171 0.0001 390 VAL A CG2 3031 N N . LEU A 391 ? 0.1731 0.1784 0.1713 0.0130 0.0162 -0.0039 391 LEU A N 3032 C CA . LEU A 391 ? 0.1764 0.1829 0.1753 0.0129 0.0155 -0.0048 391 LEU A CA 3033 C C . LEU A 391 ? 0.1875 0.1948 0.1832 0.0159 0.0164 -0.0034 391 LEU A C 3034 O O . LEU A 391 ? 0.1940 0.1980 0.1865 0.0177 0.0194 -0.0021 391 LEU A O 3035 C CB . LEU A 391 ? 0.1848 0.1882 0.1846 0.0111 0.0174 -0.0059 391 LEU A CB 3036 C CG . LEU A 391 ? 0.1680 0.1724 0.1689 0.0107 0.0169 -0.0070 391 LEU A CG 3037 C CD1 . LEU A 391 ? 0.1843 0.1925 0.1882 0.0094 0.0132 -0.0082 391 LEU A CD1 3038 C CD2 . LEU A 391 ? 0.1856 0.1869 0.1874 0.0088 0.0192 -0.0084 391 LEU A CD2 3039 N N . LEU A 392 ? 0.1806 0.1923 0.1771 0.0166 0.0139 -0.0038 392 LEU A N 3040 C CA . LEU A 392 ? 0.1867 0.2007 0.1802 0.0198 0.0142 -0.0028 392 LEU A CA 3041 C C . LEU A 392 ? 0.1982 0.2123 0.1914 0.0202 0.0146 -0.0034 392 LEU A C 3042 O O . LEU A 392 ? 0.2305 0.2452 0.2205 0.0233 0.0159 -0.0023 392 LEU A O 3043 C CB . LEU A 392 ? 0.1901 0.2096 0.1844 0.0207 0.0116 -0.0031 392 LEU A CB 3044 C CG . LEU A 392 ? 0.2055 0.2255 0.1996 0.0209 0.0113 -0.0023 392 LEU A CG 3045 C CD1 . LEU A 392 ? 0.2187 0.2446 0.2141 0.0212 0.0087 -0.0032 392 LEU A CD1 3046 C CD2 . LEU A 392 ? 0.2432 0.2603 0.2330 0.0238 0.0142 -0.0002 392 LEU A CD2 3047 N N . LYS A 393 ? 0.1855 0.1996 0.1819 0.0176 0.0133 -0.0051 393 LYS A N 3048 C CA . LYS A 393 ? 0.1974 0.2121 0.1940 0.0178 0.0134 -0.0059 393 LYS A CA 3049 C C . LYS A 393 ? 0.1883 0.2010 0.1879 0.0146 0.0132 -0.0074 393 LYS A C 3050 O O . LYS A 393 ? 0.1889 0.2021 0.1913 0.0125 0.0115 -0.0083 393 LYS A O 3051 C CB . LYS A 393 ? 0.1989 0.2191 0.1967 0.0184 0.0106 -0.0069 393 LYS A CB 3052 C CG . LYS A 393 ? 0.2032 0.2245 0.2012 0.0187 0.0104 -0.0079 393 LYS A CG 3053 C CD . LYS A 393 ? 0.2177 0.2447 0.2169 0.0193 0.0079 -0.0091 393 LYS A CD 3054 C CE . LYS A 393 ? 0.2151 0.2434 0.2145 0.0197 0.0077 -0.0102 393 LYS A CE 3055 N NZ . LYS A 393 ? 0.2343 0.2686 0.2351 0.0203 0.0054 -0.0118 393 LYS A NZ 3056 N N . ASN A 394 ? 0.2146 0.2252 0.2137 0.0145 0.0149 -0.0078 394 ASN A N 3057 C CA . ASN A 394 ? 0.2069 0.2163 0.2089 0.0118 0.0146 -0.0095 394 ASN A CA 3058 C C . ASN A 394 ? 0.2536 0.2631 0.2552 0.0122 0.0153 -0.0101 394 ASN A C 3059 O O . ASN A 394 ? 0.2926 0.2989 0.2933 0.0119 0.0180 -0.0102 394 ASN A O 3060 C CB . ASN A 394 ? 0.2214 0.2269 0.2233 0.0105 0.0171 -0.0095 394 ASN A CB 3061 C CG . ASN A 394 ? 0.2040 0.2095 0.2093 0.0077 0.0164 -0.0116 394 ASN A CG 3062 O OD1 . ASN A 394 ? 0.2344 0.2374 0.2402 0.0063 0.0187 -0.0124 394 ASN A OD1 3063 N ND2 . ASN A 394 ? 0.1962 0.2047 0.2039 0.0069 0.0135 -0.0127 394 ASN A ND2 3064 N N . GLY A 395 ? 0.2399 0.2531 0.2420 0.0131 0.0131 -0.0105 395 GLY A N 3065 C CA . GLY A 395 ? 0.2490 0.2632 0.2509 0.0137 0.0131 -0.0113 395 GLY A CA 3066 C C . GLY A 395 ? 0.2510 0.2685 0.2508 0.0165 0.0125 -0.0105 395 GLY A C 3067 O O . GLY A 395 ? 0.2576 0.2749 0.2543 0.0189 0.0138 -0.0089 395 GLY A O 3068 N N . LYS A 396 ? 0.2766 0.2975 0.2778 0.0165 0.0106 -0.0119 396 LYS A N 3069 C CA . LYS A 396 ? 0.2732 0.2984 0.2727 0.0191 0.0097 -0.0118 396 LYS A CA 3070 C C . LYS A 396 ? 0.3203 0.3449 0.3160 0.0222 0.0121 -0.0105 396 LYS A C 3071 O O . LYS A 396 ? 0.3402 0.3681 0.3333 0.0252 0.0120 -0.0098 396 LYS A O 3072 C CB . LYS A 396 ? 0.3239 0.3529 0.3264 0.0180 0.0070 -0.0140 396 LYS A CB 3073 C CG . LYS A 396 ? 0.3442 0.3744 0.3500 0.0157 0.0048 -0.0151 396 LYS A CG 3074 C CD . LYS A 396 ? 0.3490 0.3834 0.3572 0.0150 0.0025 -0.0172 396 LYS A CD 3075 C CE . LYS A 396 ? 0.3550 0.3895 0.3664 0.0126 0.0008 -0.0181 396 LYS A CE 3076 N NZ . LYS A 396 ? 0.3710 0.4074 0.3852 0.0112 -0.0008 -0.0204 396 LYS A NZ 3077 N N . THR A 397 ? 0.2735 0.2942 0.2685 0.0216 0.0143 -0.0103 397 THR A N 3078 C CA . THR A 397 ? 0.2867 0.3059 0.2777 0.0245 0.0171 -0.0088 397 THR A CA 3079 C C . THR A 397 ? 0.2976 0.3105 0.2872 0.0237 0.0207 -0.0076 397 THR A C 3080 O O . THR A 397 ? 0.3038 0.3144 0.2961 0.0205 0.0206 -0.0086 397 THR A O 3081 C CB . THR A 397 ? 0.2788 0.2999 0.2701 0.0249 0.0167 -0.0100 397 THR A CB 3082 O OG1 . THR A 397 ? 0.2801 0.2977 0.2734 0.0222 0.0178 -0.0108 397 THR A OG1 3083 C CG2 . THR A 397 ? 0.2691 0.2960 0.2636 0.0240 0.0128 -0.0122 397 THR A CG2 3084 N N . SER A 398 ? 0.3345 0.3447 0.3198 0.0265 0.0241 -0.0057 398 SER A N 3085 C CA . SER A 398 ? 0.3566 0.3603 0.3401 0.0259 0.0282 -0.0045 398 SER A CA 3086 C C . SER A 398 ? 0.3491 0.3506 0.3353 0.0227 0.0292 -0.0063 398 SER A C 3087 O O . SER A 398 ? 0.3845 0.3812 0.3707 0.0211 0.0323 -0.0063 398 SER A O 3088 C CB . SER A 398 ? 0.3735 0.3746 0.3513 0.0301 0.0319 -0.0019 398 SER A CB 3089 O OG . SER A 398 ? 0.4151 0.4175 0.3917 0.0316 0.0324 -0.0020 398 SER A OG 3090 N N . THR A 399 ? 0.2916 0.2969 0.2804 0.0218 0.0265 -0.0081 399 THR A N 3091 C CA . THR A 399 ? 0.2886 0.2926 0.2798 0.0193 0.0272 -0.0099 399 THR A CA 3092 C C . THR A 399 ? 0.2584 0.2648 0.2547 0.0158 0.0238 -0.0123 399 THR A C 3093 O O . THR A 399 ? 0.2468 0.2528 0.2455 0.0136 0.0240 -0.0141 399 THR A O 3094 C CB . THR A 399 ? 0.3278 0.3337 0.3168 0.0217 0.0274 -0.0095 399 THR A CB 3095 O OG1 A THR A 399 ? 0.3358 0.3374 0.3209 0.0236 0.0320 -0.0078 399 THR A OG1 3096 O OG1 B THR A 399 ? 0.3543 0.3582 0.3446 0.0199 0.0293 -0.0108 399 THR A OG1 3097 C CG2 A THR A 399 ? 0.3087 0.3193 0.3009 0.0207 0.0239 -0.0117 399 THR A CG2 3098 C CG2 B THR A 399 ? 0.2431 0.2550 0.2342 0.0220 0.0232 -0.0109 399 THR A CG2 3099 N N . ASP A 400 ? 0.2250 0.2341 0.2227 0.0156 0.0208 -0.0125 400 ASP A N 3100 C CA . ASP A 400 ? 0.2015 0.2125 0.2035 0.0128 0.0179 -0.0145 400 ASP A CA 3101 C C . ASP A 400 ? 0.2119 0.2200 0.2155 0.0103 0.0192 -0.0151 400 ASP A C 3102 O O . ASP A 400 ? 0.2263 0.2312 0.2280 0.0107 0.0219 -0.0139 400 ASP A O 3103 C CB . ASP A 400 ? 0.2162 0.2304 0.2192 0.0132 0.0147 -0.0143 400 ASP A CB 3104 C CG . ASP A 400 ? 0.2206 0.2391 0.2238 0.0145 0.0125 -0.0149 400 ASP A CG 3105 O OD1 . ASP A 400 ? 0.2214 0.2406 0.2233 0.0159 0.0133 -0.0150 400 ASP A OD1 3106 O OD2 . ASP A 400 ? 0.2354 0.2567 0.2403 0.0141 0.0099 -0.0155 400 ASP A OD2 3107 N N . ALA A 401 ? 0.1880 0.1974 0.1952 0.0080 0.0175 -0.0171 401 ALA A N 3108 C CA . ALA A 401 ? 0.1887 0.1968 0.1979 0.0058 0.0180 -0.0181 401 ALA A CA 3109 C C . ALA A 401 ? 0.2036 0.2117 0.2123 0.0062 0.0170 -0.0169 401 ALA A C 3110 O O . ALA A 401 ? 0.2203 0.2308 0.2292 0.0071 0.0144 -0.0164 401 ALA A O 3111 C CB . ALA A 401 ? 0.1929 0.2034 0.2055 0.0041 0.0156 -0.0203 401 ALA A CB 3112 N N . PRO A 402 ? 0.2206 0.2261 0.2289 0.0054 0.0191 -0.0167 402 PRO A N 3113 C CA . PRO A 402 ? 0.2454 0.2511 0.2535 0.0056 0.0179 -0.0156 402 PRO A CA 3114 C C . PRO A 402 ? 0.2254 0.2341 0.2368 0.0042 0.0145 -0.0170 402 PRO A C 3115 O O . PRO A 402 ? 0.2375 0.2468 0.2511 0.0026 0.0144 -0.0188 402 PRO A O 3116 C CB . PRO A 402 ? 0.2732 0.2756 0.2807 0.0047 0.0211 -0.0157 402 PRO A CB 3117 C CG . PRO A 402 ? 0.2847 0.2861 0.2937 0.0029 0.0231 -0.0177 402 PRO A CG 3118 C CD . PRO A 402 ? 0.2585 0.2609 0.2669 0.0039 0.0226 -0.0177 402 PRO A CD 3119 N N . LEU A 403 ? 0.1921 0.2027 0.2036 0.0049 0.0121 -0.0161 403 LEU A N 3120 C CA . LEU A 403 ? 0.1936 0.2064 0.2077 0.0039 0.0093 -0.0171 403 LEU A CA 3121 C C . LEU A 403 ? 0.1794 0.1914 0.1945 0.0027 0.0097 -0.0175 403 LEU A C 3122 O O . LEU A 403 ? 0.1731 0.1864 0.1904 0.0016 0.0085 -0.0189 403 LEU A O 3123 C CB . LEU A 403 ? 0.2317 0.2464 0.2457 0.0048 0.0071 -0.0162 403 LEU A CB 3124 C CG . LEU A 403 ? 0.2397 0.2558 0.2561 0.0038 0.0047 -0.0169 403 LEU A CG 3125 C CD1 . LEU A 403 ? 0.2613 0.2783 0.2796 0.0031 0.0037 -0.0186 403 LEU A CD1 3126 C CD2 . LEU A 403 ? 0.2620 0.2797 0.2785 0.0043 0.0029 -0.0163 403 LEU A CD2 3127 N N . LEU A 404 ? 0.1623 0.1727 0.1758 0.0031 0.0112 -0.0163 404 LEU A N 3128 C CA . LEU A 404 ? 0.1695 0.1794 0.1839 0.0020 0.0115 -0.0167 404 LEU A CA 3129 C C . LEU A 404 ? 0.1792 0.1869 0.1936 0.0009 0.0147 -0.0179 404 LEU A C 3130 O O . LEU A 404 ? 0.1972 0.2024 0.2095 0.0016 0.0172 -0.0171 404 LEU A O 3131 C CB . LEU A 404 ? 0.1755 0.1849 0.1885 0.0029 0.0114 -0.0150 404 LEU A CB 3132 C CG . LEU A 404 ? 0.1673 0.1789 0.1805 0.0036 0.0086 -0.0141 404 LEU A CG 3133 C CD1 . LEU A 404 ? 0.1788 0.1903 0.1905 0.0045 0.0086 -0.0125 404 LEU A CD1 3134 C CD2 . LEU A 404 ? 0.1842 0.1978 0.2000 0.0027 0.0062 -0.0151 404 LEU A CD2 3135 N N . PRO A 405 ? 0.1889 0.1975 0.2054 -0.0007 0.0148 -0.0198 405 PRO A N 3136 C CA . PRO A 405 ? 0.1904 0.2020 0.2090 -0.0011 0.0121 -0.0206 405 PRO A CA 3137 C C . PRO A 405 ? 0.1727 0.1867 0.1929 -0.0011 0.0098 -0.0216 405 PRO A C 3138 O O . PRO A 405 ? 0.1924 0.2066 0.2132 -0.0014 0.0106 -0.0228 405 PRO A O 3139 C CB . PRO A 405 ? 0.2043 0.2162 0.2243 -0.0026 0.0137 -0.0226 405 PRO A CB 3140 C CG . PRO A 405 ? 0.2491 0.2591 0.2689 -0.0036 0.0168 -0.0239 405 PRO A CG 3141 C CD . PRO A 405 ? 0.2253 0.2322 0.2422 -0.0021 0.0180 -0.0215 405 PRO A CD 3142 N N . LEU A 406 ? 0.1656 0.1814 0.1866 -0.0005 0.0072 -0.0211 406 LEU A N 3143 C CA . LEU A 406 ? 0.1773 0.1951 0.1996 -0.0002 0.0052 -0.0219 406 LEU A CA 3144 C C . LEU A 406 ? 0.1812 0.2014 0.2054 -0.0009 0.0050 -0.0242 406 LEU A C 3145 O O . LEU A 406 ? 0.1860 0.2070 0.2107 -0.0013 0.0055 -0.0248 406 LEU A O 3146 C CB . LEU A 406 ? 0.1897 0.2078 0.2118 0.0006 0.0030 -0.0205 406 LEU A CB 3147 C CG . LEU A 406 ? 0.2226 0.2395 0.2432 0.0012 0.0028 -0.0186 406 LEU A CG 3148 C CD1 . LEU A 406 ? 0.2567 0.2739 0.2774 0.0016 0.0012 -0.0174 406 LEU A CD1 3149 C CD2 . LEU A 406 ? 0.2281 0.2451 0.2487 0.0016 0.0025 -0.0188 406 LEU A CD2 3150 N N . PRO A 407 ? 0.1833 0.2053 0.2087 -0.0007 0.0041 -0.0255 407 PRO A N 3151 C CA . PRO A 407 ? 0.1683 0.1934 0.1954 -0.0008 0.0036 -0.0278 407 PRO A CA 3152 C C . PRO A 407 ? 0.1744 0.2009 0.2016 0.0005 0.0014 -0.0270 407 PRO A C 3153 O O . PRO A 407 ? 0.1834 0.2086 0.2098 0.0014 0.0000 -0.0252 407 PRO A O 3154 C CB . PRO A 407 ? 0.1787 0.2049 0.2067 -0.0007 0.0033 -0.0292 407 PRO A CB 3155 C CG . PRO A 407 ? 0.1965 0.2204 0.2232 0.0000 0.0025 -0.0271 407 PRO A CG 3156 C CD . PRO A 407 ? 0.1852 0.2064 0.2103 -0.0002 0.0036 -0.0252 407 PRO A CD 3157 N N . LYS A 408 ? 0.1705 0.1997 0.1986 0.0005 0.0013 -0.0285 408 LYS A N 3158 C CA . LYS A 408 ? 0.1703 0.2011 0.1982 0.0020 -0.0005 -0.0277 408 LYS A CA 3159 C C . LYS A 408 ? 0.1733 0.2061 0.2016 0.0036 -0.0021 -0.0284 408 LYS A C 3160 O O . LYS A 408 ? 0.1766 0.2094 0.2041 0.0053 -0.0035 -0.0270 408 LYS A O 3161 C CB . LYS A 408 ? 0.1722 0.2060 0.2009 0.0018 -0.0001 -0.0293 408 LYS A CB 3162 C CG . LYS A 408 ? 0.1701 0.2017 0.1981 0.0006 0.0013 -0.0284 408 LYS A CG 3163 C CD . LYS A 408 ? 0.1838 0.2187 0.2129 0.0003 0.0018 -0.0304 408 LYS A CD 3164 C CE . LYS A 408 ? 0.2006 0.2330 0.2288 -0.0008 0.0033 -0.0294 408 LYS A CE 3165 N NZ . LYS A 408 ? 0.2299 0.2658 0.2595 -0.0013 0.0039 -0.0318 408 LYS A NZ 3166 N N . LYS A 409 ? 0.1759 0.2100 0.2052 0.0032 -0.0017 -0.0303 409 LYS A N 3167 C CA . LYS A 409 ? 0.1854 0.2215 0.2151 0.0049 -0.0031 -0.0309 409 LYS A CA 3168 C C . LYS A 409 ? 0.1847 0.2177 0.2139 0.0047 -0.0032 -0.0298 409 LYS A C 3169 O O . LYS A 409 ? 0.2147 0.2469 0.2443 0.0033 -0.0019 -0.0306 409 LYS A O 3170 C CB . LYS A 409 ? 0.2089 0.2497 0.2403 0.0048 -0.0028 -0.0344 409 LYS A CB 3171 C CG . LYS A 409 ? 0.2690 0.3122 0.3005 0.0070 -0.0044 -0.0349 409 LYS A CG 3172 C CD . LYS A 409 ? 0.3238 0.3728 0.3571 0.0071 -0.0042 -0.0385 409 LYS A CD 3173 C CE . LYS A 409 ? 0.3837 0.4350 0.4167 0.0098 -0.0058 -0.0389 409 LYS A CE 3174 N NZ . LYS A 409 ? 0.4785 0.5367 0.5134 0.0103 -0.0059 -0.0427 409 LYS A NZ 3175 N N . ALA A 410 ? 0.1915 0.2226 0.2196 0.0062 -0.0044 -0.0281 410 ALA A N 3176 C CA . ALA A 410 ? 0.1814 0.2101 0.2092 0.0061 -0.0047 -0.0273 410 ALA A CA 3177 C C . ALA A 410 ? 0.2070 0.2352 0.2341 0.0082 -0.0059 -0.0265 410 ALA A C 3178 O O . ALA A 410 ? 0.2115 0.2398 0.2379 0.0094 -0.0064 -0.0255 410 ALA A O 3179 C CB . ALA A 410 ? 0.1911 0.2166 0.2181 0.0050 -0.0041 -0.0255 410 ALA A CB 3180 N N . PRO A 411 ? 0.1963 0.2236 0.2236 0.0088 -0.0063 -0.0268 411 PRO A N 3181 C CA . PRO A 411 ? 0.1915 0.2176 0.2178 0.0109 -0.0071 -0.0259 411 PRO A CA 3182 C C . PRO A 411 ? 0.1904 0.2129 0.2156 0.0111 -0.0069 -0.0235 411 PRO A C 3183 O O . PRO A 411 ? 0.1986 0.2207 0.2227 0.0129 -0.0072 -0.0225 411 PRO A O 3184 C CB . PRO A 411 ? 0.2033 0.2288 0.2301 0.0111 -0.0072 -0.0267 411 PRO A CB 3185 C CG . PRO A 411 ? 0.2067 0.2352 0.2348 0.0098 -0.0068 -0.0288 411 PRO A CG 3186 C CD . PRO A 411 ? 0.2152 0.2430 0.2434 0.0078 -0.0059 -0.0282 411 PRO A CD 3187 N N . LYS A 412 ? 0.1872 0.2075 0.2126 0.0093 -0.0065 -0.0228 412 LYS A N 3188 C CA . LYS A 412 ? 0.1900 0.2072 0.2147 0.0091 -0.0062 -0.0209 412 LYS A CA 3189 C C . LYS A 412 ? 0.1904 0.2073 0.2154 0.0071 -0.0058 -0.0206 412 LYS A C 3190 O O . LYS A 412 ? 0.1931 0.2107 0.2187 0.0060 -0.0056 -0.0215 412 LYS A O 3191 C CB . LYS A 412 ? 0.2059 0.2204 0.2305 0.0094 -0.0061 -0.0208 412 LYS A CB 3192 C CG A LYS A 412 ? 0.2348 0.2459 0.2587 0.0097 -0.0056 -0.0192 412 LYS A CG 3193 C CG B LYS A 412 ? 0.2049 0.2179 0.2286 0.0116 -0.0062 -0.0203 412 LYS A CG 3194 C CD A LYS A 412 ? 0.2568 0.2652 0.2806 0.0102 -0.0052 -0.0194 412 LYS A CD 3195 C CD B LYS A 412 ? 0.2066 0.2163 0.2304 0.0114 -0.0057 -0.0204 412 LYS A CD 3196 C CE A LYS A 412 ? 0.2924 0.2970 0.3159 0.0096 -0.0041 -0.0182 412 LYS A CE 3197 C CE B LYS A 412 ? 0.2227 0.2289 0.2462 0.0106 -0.0047 -0.0190 412 LYS A CE 3198 N NZ A LYS A 412 ? 0.2889 0.2906 0.3127 0.0096 -0.0034 -0.0188 412 LYS A NZ 3199 N NZ B LYS A 412 ? 0.2240 0.2268 0.2476 0.0107 -0.0039 -0.0193 412 LYS A NZ 3200 N N . ILE A 413 ? 0.1745 0.1905 0.1989 0.0068 -0.0055 -0.0192 413 ILE A N 3201 C CA . ILE A 413 ? 0.1682 0.1839 0.1926 0.0052 -0.0051 -0.0187 413 ILE A CA 3202 C C . ILE A 413 ? 0.1715 0.1852 0.1957 0.0049 -0.0049 -0.0174 413 ILE A C 3203 O O . ILE A 413 ? 0.1893 0.2013 0.2129 0.0058 -0.0048 -0.0165 413 ILE A O 3204 C CB . ILE A 413 ? 0.1691 0.1865 0.1933 0.0048 -0.0047 -0.0187 413 ILE A CB 3205 C CG1 . ILE A 413 ? 0.1777 0.1952 0.2013 0.0056 -0.0049 -0.0176 413 ILE A CG1 3206 C CG2 . ILE A 413 ? 0.1750 0.1945 0.1998 0.0049 -0.0046 -0.0204 413 ILE A CG2 3207 C CD1 . ILE A 413 ? 0.1994 0.2183 0.2228 0.0050 -0.0044 -0.0176 413 ILE A CD1 3208 N N . LEU A 414 ? 0.1549 0.1686 0.1794 0.0036 -0.0046 -0.0173 414 LEU A N 3209 C CA . LEU A 414 ? 0.1591 0.1715 0.1837 0.0029 -0.0043 -0.0165 414 LEU A CA 3210 C C . LEU A 414 ? 0.1660 0.1793 0.1901 0.0024 -0.0041 -0.0156 414 LEU A C 3211 O O . LEU A 414 ? 0.1620 0.1769 0.1859 0.0021 -0.0040 -0.0158 414 LEU A O 3212 C CB . LEU A 414 ? 0.1693 0.1818 0.1948 0.0019 -0.0041 -0.0176 414 LEU A CB 3213 C CG . LEU A 414 ? 0.1837 0.1957 0.2098 0.0008 -0.0037 -0.0175 414 LEU A CG 3214 C CD1 . LEU A 414 ? 0.1882 0.1971 0.2144 0.0009 -0.0030 -0.0168 414 LEU A CD1 3215 C CD2 . LEU A 414 ? 0.1838 0.1972 0.2111 -0.0001 -0.0037 -0.0191 414 LEU A CD2 3216 N N . VAL A 415 ? 0.1564 0.1684 0.1802 0.0025 -0.0038 -0.0144 415 VAL A N 3217 C CA . VAL A 415 ? 0.1591 0.1719 0.1825 0.0019 -0.0036 -0.0135 415 VAL A CA 3218 C C . VAL A 415 ? 0.1673 0.1793 0.1915 0.0008 -0.0031 -0.0135 415 VAL A C 3219 O O . VAL A 415 ? 0.1746 0.1843 0.1990 0.0008 -0.0026 -0.0133 415 VAL A O 3220 C CB . VAL A 415 ? 0.1611 0.1736 0.1836 0.0028 -0.0036 -0.0123 415 VAL A CB 3221 C CG1 . VAL A 415 ? 0.1779 0.1910 0.2000 0.0022 -0.0033 -0.0113 415 VAL A CG1 3222 C CG2 . VAL A 415 ? 0.1759 0.1898 0.1980 0.0035 -0.0039 -0.0129 415 VAL A CG2 3223 N N . ALA A 416 ? 0.1593 0.1732 0.1837 0.0000 -0.0031 -0.0139 416 ALA A N 3224 C CA . ALA A 416 ? 0.1593 0.1736 0.1850 -0.0012 -0.0026 -0.0146 416 ALA A CA 3225 C C . ALA A 416 ? 0.1581 0.1747 0.1837 -0.0017 -0.0025 -0.0143 416 ALA A C 3226 O O . ALA A 416 ? 0.1632 0.1810 0.1876 -0.0009 -0.0028 -0.0136 416 ALA A O 3227 C CB . ALA A 416 ? 0.1657 0.1812 0.1924 -0.0016 -0.0028 -0.0165 416 ALA A CB 3228 N N . GLY A 417 ? 0.1602 0.1774 0.1870 -0.0029 -0.0020 -0.0151 417 GLY A N 3229 C CA . GLY A 417 ? 0.1613 0.1815 0.1883 -0.0034 -0.0019 -0.0153 417 GLY A CA 3230 C C . GLY A 417 ? 0.1644 0.1833 0.1913 -0.0039 -0.0013 -0.0141 417 GLY A C 3231 O O . GLY A 417 ? 0.1702 0.1861 0.1962 -0.0033 -0.0011 -0.0126 417 GLY A O 3232 N N . SER A 418 ? 0.1704 0.1920 0.1982 -0.0048 -0.0010 -0.0149 418 SER A N 3233 C CA . SER A 418 ? 0.1655 0.1865 0.1935 -0.0055 -0.0003 -0.0140 418 SER A CA 3234 C C . SER A 418 ? 0.1685 0.1890 0.1946 -0.0042 -0.0006 -0.0119 418 SER A C 3235 O O . SER A 418 ? 0.1857 0.2048 0.2116 -0.0045 0.0000 -0.0107 418 SER A O 3236 C CB . SER A 418 ? 0.1842 0.2095 0.2136 -0.0067 0.0000 -0.0157 418 SER A CB 3237 O OG . SER A 418 ? 0.2027 0.2320 0.2312 -0.0054 -0.0011 -0.0159 418 SER A OG 3238 N N . HIS A 419 ? 0.1479 0.1695 0.1727 -0.0029 -0.0015 -0.0114 419 HIS A N 3239 C CA . HIS A 419 ? 0.1439 0.1652 0.1671 -0.0018 -0.0017 -0.0098 419 HIS A CA 3240 C C . HIS A 419 ? 0.1567 0.1755 0.1788 -0.0009 -0.0019 -0.0090 419 HIS A C 3241 O O . HIS A 419 ? 0.1529 0.1717 0.1739 0.0000 -0.0020 -0.0080 419 HIS A O 3242 C CB . HIS A 419 ? 0.1479 0.1722 0.1701 -0.0009 -0.0020 -0.0099 419 HIS A CB 3243 C CG . HIS A 419 ? 0.1471 0.1747 0.1700 -0.0014 -0.0018 -0.0105 419 HIS A CG 3244 N ND1 . HIS A 419 ? 0.1724 0.2020 0.1971 -0.0027 -0.0017 -0.0123 419 HIS A ND1 3245 C CD2 . HIS A 419 ? 0.1569 0.1865 0.1788 -0.0008 -0.0018 -0.0098 419 HIS A CD2 3246 C CE1 . HIS A 419 ? 0.1582 0.1913 0.1833 -0.0028 -0.0016 -0.0129 419 HIS A CE1 3247 N NE2 . HIS A 419 ? 0.1563 0.1894 0.1796 -0.0016 -0.0017 -0.0112 419 HIS A NE2 3248 N N . ALA A 420 ? 0.1463 0.1634 0.1690 -0.0009 -0.0020 -0.0096 420 ALA A N 3249 C CA . ALA A 420 ? 0.1549 0.1703 0.1768 0.0001 -0.0022 -0.0091 420 ALA A CA 3250 C C . ALA A 420 ? 0.1624 0.1761 0.1836 0.0006 -0.0020 -0.0078 420 ALA A C 3251 O O . ALA A 420 ? 0.1659 0.1796 0.1864 0.0017 -0.0023 -0.0075 420 ALA A O 3252 C CB . ALA A 420 ? 0.1753 0.1897 0.1979 0.0001 -0.0024 -0.0102 420 ALA A CB 3253 N N . ASP A 421 ? 0.1554 0.1679 0.1771 0.0000 -0.0013 -0.0073 421 ASP A N 3254 C CA . ASP A 421 ? 0.1673 0.1778 0.1880 0.0009 -0.0008 -0.0058 421 ASP A CA 3255 C C . ASP A 421 ? 0.1656 0.1760 0.1865 0.0000 0.0000 -0.0051 421 ASP A C 3256 O O . ASP A 421 ? 0.2041 0.2121 0.2252 -0.0005 0.0012 -0.0047 421 ASP A O 3257 C CB . ASP A 421 ? 0.1732 0.1808 0.1939 0.0015 -0.0003 -0.0058 421 ASP A CB 3258 C CG . ASP A 421 ? 0.1933 0.1990 0.2124 0.0031 0.0001 -0.0042 421 ASP A CG 3259 O OD1 . ASP A 421 ? 0.1990 0.2063 0.2171 0.0043 -0.0006 -0.0036 421 ASP A OD1 3260 O OD2 . ASP A 421 ? 0.2279 0.2305 0.2466 0.0034 0.0014 -0.0034 421 ASP A OD2 3261 N N . ASN A 422 ? 0.1490 0.1618 0.1697 -0.0002 -0.0004 -0.0050 422 ASN A N 3262 C CA . ASN A 422 ? 0.1481 0.1616 0.1692 -0.0011 0.0002 -0.0045 422 ASN A CA 3263 C C . ASN A 422 ? 0.1469 0.1623 0.1669 -0.0003 -0.0003 -0.0037 422 ASN A C 3264 O O . ASN A 422 ? 0.1591 0.1767 0.1791 -0.0004 -0.0008 -0.0043 422 ASN A O 3265 C CB . ASN A 422 ? 0.1550 0.1703 0.1777 -0.0027 0.0006 -0.0060 422 ASN A CB 3266 C CG . ASN A 422 ? 0.1599 0.1758 0.1832 -0.0039 0.0015 -0.0058 422 ASN A CG 3267 O OD1 . ASN A 422 ? 0.1683 0.1848 0.1907 -0.0033 0.0015 -0.0046 422 ASN A OD1 3268 N ND2 . ASN A 422 ? 0.1796 0.1954 0.2047 -0.0056 0.0026 -0.0072 422 ASN A ND2 3269 N N . LEU A 423 ? 0.1487 0.1630 0.1676 0.0006 -0.0001 -0.0023 423 LEU A N 3270 C CA . LEU A 423 ? 0.1576 0.1736 0.1755 0.0014 -0.0005 -0.0017 423 LEU A CA 3271 C C . LEU A 423 ? 0.1517 0.1696 0.1699 0.0005 -0.0003 -0.0017 423 LEU A C 3272 O O . LEU A 423 ? 0.1475 0.1672 0.1652 0.0009 -0.0007 -0.0018 423 LEU A O 3273 C CB . LEU A 423 ? 0.1726 0.1874 0.1893 0.0026 -0.0003 -0.0004 423 LEU A CB 3274 C CG . LEU A 423 ? 0.2013 0.2178 0.2171 0.0035 -0.0008 -0.0001 423 LEU A CG 3275 C CD1 . LEU A 423 ? 0.2456 0.2631 0.2614 0.0039 -0.0015 -0.0013 423 LEU A CD1 3276 C CD2 . LEU A 423 ? 0.2269 0.2428 0.2416 0.0049 -0.0006 0.0011 423 LEU A CD2 3277 N N . GLY A 424 ? 0.1408 0.1584 0.1598 -0.0006 0.0005 -0.0016 424 GLY A N 3278 C CA . GLY A 424 ? 0.1388 0.1590 0.1584 -0.0014 0.0007 -0.0019 424 GLY A CA 3279 C C . GLY A 424 ? 0.1539 0.1769 0.1739 -0.0015 0.0001 -0.0032 424 GLY A C 3280 O O . GLY A 424 ? 0.1519 0.1772 0.1713 -0.0009 -0.0002 -0.0031 424 GLY A O 3281 N N . TYR A 425 ? 0.1443 0.1669 0.1652 -0.0019 -0.0001 -0.0044 425 TYR A N 3282 C CA . TYR A 425 ? 0.1444 0.1697 0.1654 -0.0017 -0.0006 -0.0056 425 TYR A CA 3283 C C . TYR A 425 ? 0.1521 0.1774 0.1714 -0.0001 -0.0010 -0.0050 425 TYR A C 3284 O O . TYR A 425 ? 0.1598 0.1874 0.1784 0.0006 -0.0012 -0.0052 425 TYR A O 3285 C CB . TYR A 425 ? 0.1668 0.1917 0.1891 -0.0024 -0.0006 -0.0070 425 TYR A CB 3286 C CG . TYR A 425 ? 0.1604 0.1862 0.1848 -0.0042 0.0001 -0.0084 425 TYR A CG 3287 C CD1 . TYR A 425 ? 0.1752 0.2019 0.2003 -0.0053 0.0009 -0.0084 425 TYR A CD1 3288 C CD2 . TYR A 425 ? 0.1684 0.1941 0.1940 -0.0049 0.0001 -0.0100 425 TYR A CD2 3289 C CE1 . TYR A 425 ? 0.1816 0.2091 0.2090 -0.0072 0.0019 -0.0101 425 TYR A CE1 3290 C CE2 . TYR A 425 ? 0.1889 0.2155 0.2166 -0.0068 0.0010 -0.0118 425 TYR A CE2 3291 C CZ . TYR A 425 ? 0.1894 0.2167 0.2180 -0.0080 0.0020 -0.0119 425 TYR A CZ 3292 O OH . TYR A 425 ? 0.2368 0.2650 0.2679 -0.0102 0.0033 -0.0140 425 TYR A OH 3293 N N . GLN A 426 ? 0.1500 0.1728 0.1686 0.0004 -0.0011 -0.0043 426 GLN A N 3294 C CA . GLN A 426 ? 0.1630 0.1856 0.1802 0.0015 -0.0012 -0.0041 426 GLN A CA 3295 C C . GLN A 426 ? 0.1495 0.1729 0.1656 0.0022 -0.0009 -0.0032 426 GLN A C 3296 O O . GLN A 426 ? 0.1575 0.1809 0.1724 0.0031 -0.0006 -0.0031 426 GLN A O 3297 C CB . GLN A 426 ? 0.2222 0.2428 0.2395 0.0018 -0.0014 -0.0043 426 GLN A CB 3298 C CG . GLN A 426 ? 0.2361 0.2557 0.2531 0.0021 -0.0014 -0.0036 426 GLN A CG 3299 C CD . GLN A 426 ? 0.2295 0.2480 0.2465 0.0025 -0.0016 -0.0043 426 GLN A CD 3300 O OE1 . GLN A 426 ? 0.2370 0.2549 0.2547 0.0023 -0.0019 -0.0049 426 GLN A OE1 3301 N NE2 . GLN A 426 ? 0.1656 0.1843 0.1820 0.0031 -0.0016 -0.0043 426 GLN A NE2 3302 N N . CYS A 427 ? 0.1528 0.1765 0.1692 0.0018 -0.0009 -0.0025 427 CYS A N 3303 C CA . CYS A 427 ? 0.1412 0.1658 0.1566 0.0024 -0.0006 -0.0016 427 CYS A CA 3304 C C . CYS A 427 ? 0.1369 0.1642 0.1521 0.0026 -0.0005 -0.0018 427 CYS A C 3305 O O . CYS A 427 ? 0.1472 0.1754 0.1612 0.0036 -0.0003 -0.0012 427 CYS A O 3306 C CB . CYS A 427 ? 0.1374 0.1612 0.1529 0.0021 -0.0006 -0.0007 427 CYS A CB 3307 S SG . CYS A 427 ? 0.1558 0.1776 0.1709 0.0027 -0.0008 -0.0005 427 CYS A SG 3308 N N . GLY A 428 ? 0.1424 0.1713 0.1590 0.0017 -0.0006 -0.0026 428 GLY A N 3309 C CA . GLY A 428 ? 0.1472 0.1798 0.1639 0.0019 -0.0006 -0.0032 428 GLY A CA 3310 C C . GLY A 428 ? 0.1346 0.1685 0.1514 0.0016 -0.0004 -0.0025 428 GLY A C 3311 O O . GLY A 428 ? 0.1467 0.1787 0.1638 0.0009 -0.0001 -0.0017 428 GLY A O 3312 N N . GLY A 429 ? 0.1405 0.1779 0.1568 0.0025 -0.0004 -0.0028 429 GLY A N 3313 C CA . GLY A 429 ? 0.1411 0.1805 0.1576 0.0022 -0.0002 -0.0024 429 GLY A CA 3314 C C . GLY A 429 ? 0.1419 0.1790 0.1569 0.0029 0.0000 -0.0008 429 GLY A C 3315 O O . GLY A 429 ? 0.1403 0.1747 0.1541 0.0037 0.0000 -0.0001 429 GLY A O 3316 N N . TRP A 430 ? 0.1412 0.1798 0.1566 0.0025 0.0002 -0.0004 430 TRP A N 3317 C CA . TRP A 430 ? 0.1366 0.1734 0.1508 0.0031 0.0004 0.0010 430 TRP A CA 3318 C C . TRP A 430 ? 0.1442 0.1772 0.1582 0.0028 0.0004 0.0017 430 TRP A C 3319 O O . TRP A 430 ? 0.1449 0.1763 0.1577 0.0038 0.0004 0.0022 430 TRP A O 3320 C CB . TRP A 430 ? 0.1486 0.1857 0.1607 0.0050 0.0005 0.0016 430 TRP A CB 3321 C CG . TRP A 430 ? 0.1398 0.1809 0.1514 0.0060 0.0005 0.0014 430 TRP A CG 3322 C CD1 . TRP A 430 ? 0.1539 0.1975 0.1646 0.0074 0.0005 0.0008 430 TRP A CD1 3323 C CD2 . TRP A 430 ? 0.1439 0.1871 0.1557 0.0059 0.0007 0.0017 430 TRP A CD2 3324 N NE1 . TRP A 430 ? 0.1531 0.2006 0.1634 0.0084 0.0005 0.0007 430 TRP A NE1 3325 C CE2 . TRP A 430 ? 0.1451 0.1924 0.1561 0.0073 0.0006 0.0012 430 TRP A CE2 3326 C CE3 . TRP A 430 ? 0.1471 0.1894 0.1594 0.0049 0.0009 0.0025 430 TRP A CE3 3327 C CZ2 . TRP A 430 ? 0.1476 0.1983 0.1588 0.0076 0.0007 0.0013 430 TRP A CZ2 3328 C CZ3 . TRP A 430 ? 0.1466 0.1920 0.1590 0.0050 0.0010 0.0027 430 TRP A CZ3 3329 C CH2 . TRP A 430 ? 0.1461 0.1955 0.1580 0.0063 0.0009 0.0020 430 TRP A CH2 3330 N N . THR A 431 ? 0.1365 0.1682 0.1518 0.0015 0.0006 0.0014 431 THR A N 3331 C CA . THR A 431 ? 0.1384 0.1670 0.1536 0.0016 0.0006 0.0021 431 THR A CA 3332 C C . THR A 431 ? 0.1486 0.1761 0.1646 0.0005 0.0013 0.0025 431 THR A C 3333 O O . THR A 431 ? 0.1382 0.1656 0.1556 -0.0008 0.0017 0.0017 431 THR A O 3334 C CB . THR A 431 ? 0.1399 0.1669 0.1553 0.0016 0.0002 0.0013 431 THR A CB 3335 O OG1 . THR A 431 ? 0.1464 0.1744 0.1609 0.0025 0.0000 0.0008 431 THR A OG1 3336 C CG2 . THR A 431 ? 0.1548 0.1794 0.1696 0.0022 0.0001 0.0018 431 THR A CG2 3337 N N . ILE A 432 ? 0.1451 0.1718 0.1602 0.0011 0.0016 0.0038 432 ILE A N 3338 C CA . ILE A 432 ? 0.1555 0.1807 0.1708 0.0005 0.0026 0.0048 432 ILE A CA 3339 C C . ILE A 432 ? 0.1617 0.1890 0.1783 -0.0010 0.0035 0.0043 432 ILE A C 3340 O O . ILE A 432 ? 0.1695 0.1974 0.1857 -0.0010 0.0041 0.0052 432 ILE A O 3341 C CB . ILE A 432 ? 0.1591 0.1812 0.1746 0.0003 0.0032 0.0049 432 ILE A CB 3342 C CG1 . ILE A 432 ? 0.1652 0.1860 0.1795 0.0019 0.0023 0.0052 432 ILE A CG1 3343 C CG2 . ILE A 432 ? 0.1661 0.1860 0.1814 -0.0001 0.0048 0.0061 432 ILE A CG2 3344 C CD1 . ILE A 432 ? 0.1737 0.1949 0.1864 0.0035 0.0020 0.0063 432 ILE A CD1 3345 N N . GLU A 433 ? 0.1613 0.1900 0.1795 -0.0022 0.0035 0.0027 433 GLU A N 3346 C CA . GLU A 433 ? 0.1722 0.2043 0.1919 -0.0036 0.0041 0.0016 433 GLU A CA 3347 C C . GLU A 433 ? 0.1781 0.2141 0.1974 -0.0026 0.0029 0.0008 433 GLU A C 3348 O O . GLU A 433 ? 0.1618 0.1973 0.1800 -0.0013 0.0020 0.0008 433 GLU A O 3349 C CB . GLU A 433 ? 0.2039 0.2359 0.2257 -0.0056 0.0050 -0.0001 433 GLU A CB 3350 C CG . GLU A 433 ? 0.2681 0.2956 0.2902 -0.0065 0.0066 0.0006 433 GLU A CG 3351 C CD . GLU A 433 ? 0.3137 0.3401 0.3358 -0.0072 0.0082 0.0017 433 GLU A CD 3352 O OE1 . GLU A 433 ? 0.3114 0.3410 0.3337 -0.0075 0.0082 0.0015 433 GLU A OE1 3353 O OE2 . GLU A 433 ? 0.4170 0.4390 0.4386 -0.0075 0.0098 0.0027 433 GLU A OE2 3354 N N . TRP A 434 ? 0.1658 0.2056 0.1859 -0.0030 0.0032 0.0000 434 TRP A N 3355 C CA . TRP A 434 ? 0.1606 0.2044 0.1801 -0.0017 0.0022 -0.0008 434 TRP A CA 3356 C C . TRP A 434 ? 0.1735 0.2182 0.1934 -0.0015 0.0016 -0.0022 434 TRP A C 3357 O O . TRP A 434 ? 0.1709 0.2156 0.1891 0.0003 0.0009 -0.0018 434 TRP A O 3358 C CB . TRP A 434 ? 0.1639 0.2124 0.1846 -0.0025 0.0027 -0.0019 434 TRP A CB 3359 C CG . TRP A 434 ? 0.1675 0.2208 0.1876 -0.0009 0.0018 -0.0029 434 TRP A CG 3360 C CD1 . TRP A 434 ? 0.1738 0.2271 0.1915 0.0016 0.0011 -0.0019 434 TRP A CD1 3361 C CD2 . TRP A 434 ? 0.1851 0.2442 0.2070 -0.0015 0.0018 -0.0052 434 TRP A CD2 3362 N NE1 . TRP A 434 ? 0.1946 0.2530 0.2121 0.0030 0.0006 -0.0031 434 TRP A NE1 3363 C CE2 . TRP A 434 ? 0.1931 0.2556 0.2132 0.0012 0.0009 -0.0053 434 TRP A CE2 3364 C CE3 . TRP A 434 ? 0.1868 0.2487 0.2118 -0.0040 0.0027 -0.0075 434 TRP A CE3 3365 C CZ2 . TRP A 434 ? 0.2016 0.2706 0.2226 0.0017 0.0006 -0.0074 434 TRP A CZ2 3366 C CZ3 . TRP A 434 ? 0.2067 0.2753 0.2330 -0.0040 0.0024 -0.0100 434 TRP A CZ3 3367 C CH2 . TRP A 434 ? 0.2048 0.2773 0.2291 -0.0009 0.0012 -0.0099 434 TRP A CH2 3368 N N . GLN A 435 ? 0.1718 0.2173 0.1939 -0.0034 0.0022 -0.0039 435 GLN A N 3369 C CA . GLN A 435 ? 0.1802 0.2271 0.2030 -0.0033 0.0016 -0.0055 435 GLN A CA 3370 C C . GLN A 435 ? 0.1811 0.2234 0.2035 -0.0034 0.0015 -0.0049 435 GLN A C 3371 O O . GLN A 435 ? 0.2084 0.2514 0.2316 -0.0036 0.0012 -0.0062 435 GLN A O 3372 C CB . GLN A 435 ? 0.2104 0.2609 0.2361 -0.0055 0.0024 -0.0080 435 GLN A CB 3373 C CG . GLN A 435 ? 0.2259 0.2823 0.2522 -0.0053 0.0023 -0.0091 435 GLN A CG 3374 C CD . GLN A 435 ? 0.2974 0.3579 0.3269 -0.0077 0.0032 -0.0121 435 GLN A CD 3375 O OE1 . GLN A 435 ? 0.3543 0.4198 0.3847 -0.0073 0.0026 -0.0144 435 GLN A OE1 3376 N NE2 . GLN A 435 ? 0.3290 0.3877 0.3602 -0.0101 0.0048 -0.0123 435 GLN A NE2 3377 N N . GLY A 436 ? 0.1720 0.2100 0.1932 -0.0030 0.0017 -0.0030 436 GLY A N 3378 C CA . GLY A 436 ? 0.1760 0.2099 0.1970 -0.0030 0.0017 -0.0026 436 GLY A CA 3379 C C . GLY A 436 ? 0.1889 0.2211 0.2117 -0.0050 0.0028 -0.0034 436 GLY A C 3380 O O . GLY A 436 ? 0.1963 0.2300 0.2208 -0.0067 0.0039 -0.0042 436 GLY A O 3381 N N . ASP A 437 ? 0.1716 0.2004 0.1943 -0.0050 0.0028 -0.0032 437 ASP A N 3382 C CA . ASP A 437 ? 0.1870 0.2129 0.2110 -0.0066 0.0041 -0.0037 437 ASP A CA 3383 C C . ASP A 437 ? 0.1926 0.2161 0.2165 -0.0061 0.0037 -0.0040 437 ASP A C 3384 O O . ASP A 437 ? 0.1816 0.2058 0.2044 -0.0047 0.0024 -0.0039 437 ASP A O 3385 C CB . ASP A 437 ? 0.2076 0.2303 0.2307 -0.0064 0.0053 -0.0017 437 ASP A CB 3386 C CG . ASP A 437 ? 0.2378 0.2576 0.2622 -0.0083 0.0075 -0.0021 437 ASP A CG 3387 O OD1 . ASP A 437 ? 0.2667 0.2871 0.2931 -0.0100 0.0082 -0.0042 437 ASP A OD1 3388 O OD2 . ASP A 437 ? 0.2957 0.3125 0.3189 -0.0079 0.0087 -0.0003 437 ASP A OD2 3389 N N . THR A 438 ? 0.2024 0.2231 0.2274 -0.0074 0.0050 -0.0045 438 THR A N 3390 C CA . THR A 438 ? 0.1928 0.2110 0.2177 -0.0070 0.0048 -0.0049 438 THR A CA 3391 C C . THR A 438 ? 0.1869 0.2004 0.2102 -0.0058 0.0054 -0.0029 438 THR A C 3392 O O . THR A 438 ? 0.2065 0.2176 0.2292 -0.0059 0.0068 -0.0016 438 THR A O 3393 C CB . THR A 438 ? 0.1935 0.2120 0.2208 -0.0092 0.0058 -0.0072 438 THR A CB 3394 O OG1 . THR A 438 ? 0.1891 0.2052 0.2163 -0.0088 0.0056 -0.0075 438 THR A OG1 3395 C CG2 . THR A 438 ? 0.2042 0.2200 0.2325 -0.0109 0.0083 -0.0071 438 THR A CG2 3396 N N . GLY A 439 ? 0.1811 0.1935 0.2035 -0.0045 0.0043 -0.0027 439 GLY A N 3397 C CA . GLY A 439 ? 0.1958 0.2044 0.2166 -0.0030 0.0047 -0.0012 439 GLY A CA 3398 C C . GLY A 439 ? 0.1923 0.2012 0.2112 -0.0009 0.0039 0.0005 439 GLY A C 3399 O O . GLY A 439 ? 0.1964 0.2082 0.2150 -0.0005 0.0026 0.0003 439 GLY A O 3400 N N . ARG A 440 ? 0.2006 0.2065 0.2179 0.0005 0.0047 0.0020 440 ARG A N 3401 C CA . ARG A 440 ? 0.2064 0.2132 0.2219 0.0028 0.0037 0.0032 440 ARG A CA 3402 C C . ARG A 440 ? 0.2112 0.2187 0.2259 0.0029 0.0042 0.0045 440 ARG A C 3403 O O . ARG A 440 ? 0.2321 0.2373 0.2453 0.0040 0.0054 0.0061 440 ARG A O 3404 C CB . ARG A 440 ? 0.2682 0.2722 0.2821 0.0048 0.0041 0.0041 440 ARG A CB 3405 C CG . ARG A 440 ? 0.3094 0.3155 0.3217 0.0072 0.0029 0.0048 440 ARG A CG 3406 C CD A ARG A 440 ? 0.4071 0.4125 0.4182 0.0095 0.0025 0.0048 440 ARG A CD 3407 N NE A ARG A 440 ? 0.5138 0.5228 0.5255 0.0096 0.0007 0.0033 440 ARG A NE 3408 C CZ A ARG A 440 ? 0.5142 0.5241 0.5275 0.0083 0.0000 0.0016 440 ARG A CZ 3409 N NH1 A ARG A 440 ? 0.4815 0.4893 0.4959 0.0068 0.0006 0.0011 440 ARG A NH1 3410 N NH2 A ARG A 440 ? 0.3863 0.3991 0.4000 0.0084 -0.0012 0.0003 440 ARG A NH2 3411 N N . THR A 441 ? 0.2029 0.2136 0.2184 0.0019 0.0034 0.0038 441 THR A N 3412 C CA . THR A 441 ? 0.2079 0.2196 0.2231 0.0016 0.0040 0.0047 441 THR A CA 3413 C C . THR A 441 ? 0.1977 0.2108 0.2112 0.0035 0.0031 0.0057 441 THR A C 3414 O O . THR A 441 ? 0.2054 0.2191 0.2183 0.0037 0.0036 0.0067 441 THR A O 3415 C CB . THR A 441 ? 0.2214 0.2361 0.2381 0.0000 0.0036 0.0034 441 THR A CB 3416 O OG1 . THR A 441 ? 0.2202 0.2369 0.2367 0.0006 0.0021 0.0025 441 THR A OG1 3417 C CG2 . THR A 441 ? 0.2396 0.2539 0.2582 -0.0020 0.0044 0.0020 441 THR A CG2 3418 N N . THR A 442 ? 0.1769 0.1907 0.1898 0.0049 0.0020 0.0052 442 THR A N 3419 C CA . THR A 442 ? 0.1635 0.1793 0.1753 0.0065 0.0012 0.0055 442 THR A CA 3420 C C . THR A 442 ? 0.1568 0.1730 0.1682 0.0080 0.0003 0.0048 442 THR A C 3421 O O . THR A 442 ? 0.1785 0.1929 0.1901 0.0080 0.0005 0.0046 442 THR A O 3422 C CB . THR A 442 ? 0.1665 0.1849 0.1788 0.0056 0.0005 0.0047 442 THR A CB 3423 O OG1 . THR A 442 ? 0.1603 0.1804 0.1715 0.0070 0.0001 0.0050 442 THR A OG1 3424 C CG2 . THR A 442 ? 0.1660 0.1853 0.1793 0.0049 -0.0002 0.0031 442 THR A CG2 3425 N N . VAL A 443 ? 0.1500 0.1687 0.1608 0.0091 -0.0005 0.0042 443 VAL A N 3426 C CA . VAL A 443 ? 0.1529 0.1727 0.1635 0.0104 -0.0013 0.0030 443 VAL A CA 3427 C C . VAL A 443 ? 0.1429 0.1637 0.1550 0.0091 -0.0018 0.0012 443 VAL A C 3428 O O . VAL A 443 ? 0.1685 0.1905 0.1810 0.0081 -0.0018 0.0006 443 VAL A O 3429 C CB . VAL A 443 ? 0.1556 0.1782 0.1652 0.0124 -0.0017 0.0030 443 VAL A CB 3430 C CG1 . VAL A 443 ? 0.1728 0.1978 0.1826 0.0136 -0.0026 0.0012 443 VAL A CG1 3431 C CG2 . VAL A 443 ? 0.1824 0.2038 0.1902 0.0141 -0.0010 0.0052 443 VAL A CG2 3432 N N . GLY A 444 ? 0.1416 0.1617 0.1542 0.0091 -0.0021 0.0003 444 GLY A N 3433 C CA . GLY A 444 ? 0.1443 0.1652 0.1581 0.0079 -0.0024 -0.0014 444 GLY A CA 3434 C C . GLY A 444 ? 0.1498 0.1699 0.1641 0.0081 -0.0026 -0.0023 444 GLY A C 3435 O O . GLY A 444 ? 0.1889 0.2083 0.2024 0.0095 -0.0027 -0.0016 444 GLY A O 3436 N N . THR A 445 ? 0.1385 0.1586 0.1537 0.0070 -0.0027 -0.0035 445 THR A N 3437 C CA . THR A 445 ? 0.1395 0.1592 0.1553 0.0071 -0.0029 -0.0046 445 THR A CA 3438 C C . THR A 445 ? 0.1374 0.1557 0.1539 0.0056 -0.0027 -0.0048 445 THR A C 3439 O O . THR A 445 ? 0.1344 0.1532 0.1512 0.0047 -0.0024 -0.0053 445 THR A O 3440 C CB . THR A 445 ? 0.1359 0.1581 0.1522 0.0073 -0.0032 -0.0066 445 THR A CB 3441 O OG1 . THR A 445 ? 0.1704 0.1948 0.1861 0.0089 -0.0035 -0.0068 445 THR A OG1 3442 C CG2 . THR A 445 ? 0.1505 0.1725 0.1674 0.0075 -0.0035 -0.0078 445 THR A CG2 3443 N N . THR A 446 ? 0.1427 0.1592 0.1595 0.0055 -0.0026 -0.0044 446 THR A N 3444 C CA . THR A 446 ? 0.1382 0.1539 0.1558 0.0042 -0.0025 -0.0049 446 THR A CA 3445 C C . THR A 446 ? 0.1424 0.1588 0.1605 0.0040 -0.0027 -0.0064 446 THR A C 3446 O O . THR A 446 ? 0.1440 0.1614 0.1621 0.0048 -0.0030 -0.0072 446 THR A O 3447 C CB . THR A 446 ? 0.1410 0.1547 0.1590 0.0038 -0.0021 -0.0044 446 THR A CB 3448 O OG1 . THR A 446 ? 0.1541 0.1668 0.1718 0.0050 -0.0023 -0.0046 446 THR A OG1 3449 C CG2 . THR A 446 ? 0.1550 0.1677 0.1725 0.0037 -0.0014 -0.0030 446 THR A CG2 3450 N N . ILE A 447 ? 0.1421 0.1584 0.1608 0.0031 -0.0026 -0.0069 447 ILE A N 3451 C CA . ILE A 447 ? 0.1390 0.1557 0.1581 0.0030 -0.0026 -0.0082 447 ILE A CA 3452 C C . ILE A 447 ? 0.1351 0.1511 0.1546 0.0036 -0.0031 -0.0088 447 ILE A C 3453 O O . ILE A 447 ? 0.1407 0.1576 0.1603 0.0040 -0.0032 -0.0099 447 ILE A O 3454 C CB . ILE A 447 ? 0.1472 0.1640 0.1664 0.0023 -0.0024 -0.0085 447 ILE A CB 3455 C CG1 . ILE A 447 ? 0.1579 0.1755 0.1763 0.0022 -0.0019 -0.0079 447 ILE A CG1 3456 C CG2 . ILE A 447 ? 0.1577 0.1745 0.1772 0.0023 -0.0024 -0.0097 447 ILE A CG2 3457 C CD1 . ILE A 447 ? 0.1675 0.1860 0.1858 0.0020 -0.0017 -0.0081 447 ILE A CD1 3458 N N . LEU A 448 ? 0.1392 0.1537 0.1588 0.0037 -0.0031 -0.0082 448 LEU A N 3459 C CA . LEU A 448 ? 0.1483 0.1618 0.1679 0.0047 -0.0033 -0.0085 448 LEU A CA 3460 C C . LEU A 448 ? 0.1520 0.1667 0.1709 0.0063 -0.0037 -0.0085 448 LEU A C 3461 O O . LEU A 448 ? 0.1576 0.1734 0.1767 0.0071 -0.0041 -0.0095 448 LEU A O 3462 C CB . LEU A 448 ? 0.1615 0.1724 0.1811 0.0046 -0.0028 -0.0076 448 LEU A CB 3463 C CG . LEU A 448 ? 0.1622 0.1715 0.1813 0.0060 -0.0027 -0.0075 448 LEU A CG 3464 C CD1 . LEU A 448 ? 0.1689 0.1787 0.1889 0.0059 -0.0031 -0.0090 448 LEU A CD1 3465 C CD2 . LEU A 448 ? 0.1728 0.1789 0.1918 0.0057 -0.0015 -0.0065 448 LEU A CD2 3466 N N . GLU A 449 ? 0.1500 0.1650 0.1681 0.0068 -0.0035 -0.0073 449 GLU A N 3467 C CA . GLU A 449 ? 0.1565 0.1734 0.1738 0.0086 -0.0039 -0.0075 449 GLU A CA 3468 C C . GLU A 449 ? 0.1514 0.1712 0.1696 0.0082 -0.0042 -0.0093 449 GLU A C 3469 O O . GLU A 449 ? 0.1567 0.1787 0.1749 0.0094 -0.0046 -0.0105 449 GLU A O 3470 C CB . GLU A 449 ? 0.1784 0.1951 0.1947 0.0090 -0.0036 -0.0059 449 GLU A CB 3471 C CG . GLU A 449 ? 0.2107 0.2244 0.2261 0.0098 -0.0029 -0.0041 449 GLU A CG 3472 C CD . GLU A 449 ? 0.2784 0.2915 0.2930 0.0097 -0.0023 -0.0025 449 GLU A CD 3473 O OE1 . GLU A 449 ? 0.2040 0.2188 0.2188 0.0089 -0.0025 -0.0026 449 GLU A OE1 3474 O OE2 . GLU A 449 ? 0.3489 0.3592 0.3626 0.0103 -0.0014 -0.0010 449 GLU A OE2 3475 N N . ALA A 450 ? 0.1399 0.1598 0.1586 0.0066 -0.0038 -0.0097 450 ALA A N 3476 C CA . ALA A 450 ? 0.1366 0.1583 0.1559 0.0059 -0.0034 -0.0115 450 ALA A CA 3477 C C . ALA A 450 ? 0.1396 0.1617 0.1598 0.0058 -0.0035 -0.0131 450 ALA A C 3478 O O . ALA A 450 ? 0.1502 0.1747 0.1710 0.0059 -0.0035 -0.0149 450 ALA A O 3479 C CB . ALA A 450 ? 0.1381 0.1589 0.1573 0.0046 -0.0026 -0.0112 450 ALA A CB 3480 N N . VAL A 451 ? 0.1367 0.1570 0.1570 0.0055 -0.0036 -0.0126 451 VAL A N 3481 C CA . VAL A 451 ? 0.1419 0.1625 0.1629 0.0055 -0.0038 -0.0140 451 VAL A CA 3482 C C . VAL A 451 ? 0.1535 0.1758 0.1745 0.0071 -0.0045 -0.0147 451 VAL A C 3483 O O . VAL A 451 ? 0.1453 0.1700 0.1672 0.0073 -0.0046 -0.0166 451 VAL A O 3484 C CB . VAL A 451 ? 0.1338 0.1522 0.1549 0.0050 -0.0039 -0.0133 451 VAL A CB 3485 C CG1 . VAL A 451 ? 0.1454 0.1642 0.1672 0.0052 -0.0041 -0.0147 451 VAL A CG1 3486 C CG2 . VAL A 451 ? 0.1471 0.1649 0.1681 0.0037 -0.0032 -0.0130 451 VAL A CG2 3487 N N . LYS A 452 ? 0.1512 0.1724 0.1712 0.0085 -0.0049 -0.0132 452 LYS A N 3488 C CA . LYS A 452 ? 0.1547 0.1775 0.1742 0.0108 -0.0055 -0.0135 452 LYS A CA 3489 C C . LYS A 452 ? 0.1612 0.1882 0.1810 0.0115 -0.0058 -0.0151 452 LYS A C 3490 O O . LYS A 452 ? 0.1806 0.2105 0.2007 0.0129 -0.0063 -0.0166 452 LYS A O 3491 C CB . LYS A 452 ? 0.1704 0.1907 0.1884 0.0123 -0.0054 -0.0113 452 LYS A CB 3492 C CG . LYS A 452 ? 0.2032 0.2196 0.2212 0.0116 -0.0049 -0.0103 452 LYS A CG 3493 C CD . LYS A 452 ? 0.2291 0.2424 0.2457 0.0126 -0.0042 -0.0081 452 LYS A CD 3494 C CE A LYS A 452 ? 0.2618 0.2713 0.2784 0.0120 -0.0034 -0.0076 452 LYS A CE 3495 C CE B LYS A 452 ? 0.2283 0.2415 0.2431 0.0156 -0.0041 -0.0072 452 LYS A CE 3496 N NZ A LYS A 452 ? 0.2759 0.2822 0.2909 0.0134 -0.0023 -0.0055 452 LYS A NZ 3497 N NZ B LYS A 452 ? 0.2732 0.2820 0.2867 0.0161 -0.0028 -0.0050 452 LYS A NZ 3498 N N . ALA A 453 ? 0.1552 0.1829 0.1751 0.0106 -0.0054 -0.0149 453 ALA A N 3499 C CA . ALA A 453 ? 0.1633 0.1951 0.1837 0.0109 -0.0055 -0.0168 453 ALA A CA 3500 C C . ALA A 453 ? 0.1597 0.1935 0.1819 0.0092 -0.0049 -0.0195 453 ALA A C 3501 O O . ALA A 453 ? 0.1911 0.2290 0.2142 0.0095 -0.0048 -0.0218 453 ALA A O 3502 C CB . ALA A 453 ? 0.1552 0.1867 0.1751 0.0104 -0.0051 -0.0158 453 ALA A CB 3503 N N . ALA A 454 ? 0.1514 0.1826 0.1741 0.0076 -0.0042 -0.0194 454 ALA A N 3504 C CA . ALA A 454 ? 0.1555 0.1876 0.1796 0.0058 -0.0031 -0.0217 454 ALA A CA 3505 C C . ALA A 454 ? 0.1583 0.1920 0.1833 0.0061 -0.0034 -0.0235 454 ALA A C 3506 O O . ALA A 454 ? 0.1818 0.2181 0.2083 0.0052 -0.0027 -0.0261 454 ALA A O 3507 C CB . ALA A 454 ? 0.1603 0.1887 0.1840 0.0042 -0.0020 -0.0205 454 ALA A CB 3508 N N . VAL A 455 ? 0.1558 0.1878 0.1801 0.0073 -0.0043 -0.0222 455 VAL A N 3509 C CA . VAL A 455 ? 0.1566 0.1892 0.1817 0.0073 -0.0044 -0.0236 455 VAL A CA 3510 C C . VAL A 455 ? 0.1622 0.1993 0.1879 0.0090 -0.0053 -0.0256 455 VAL A C 3511 O O . VAL A 455 ? 0.1600 0.1994 0.1851 0.0109 -0.0060 -0.0253 455 VAL A O 3512 C CB . VAL A 455 ? 0.1551 0.1843 0.1794 0.0077 -0.0049 -0.0217 455 VAL A CB 3513 C CG1 . VAL A 455 ? 0.1746 0.2005 0.1986 0.0059 -0.0041 -0.0205 455 VAL A CG1 3514 C CG2 . VAL A 455 ? 0.1648 0.1929 0.1878 0.0097 -0.0058 -0.0198 455 VAL A CG2 3515 N N . ASP A 456 ? 0.1748 0.2138 0.2018 0.0086 -0.0051 -0.0277 456 ASP A N 3516 C CA . ASP A 456 ? 0.1820 0.2257 0.2097 0.0104 -0.0059 -0.0299 456 ASP A CA 3517 C C . ASP A 456 ? 0.1791 0.2222 0.2050 0.0134 -0.0072 -0.0279 456 ASP A C 3518 O O . ASP A 456 ? 0.1763 0.2148 0.2009 0.0136 -0.0073 -0.0255 456 ASP A O 3519 C CB . ASP A 456 ? 0.1954 0.2397 0.2244 0.0094 -0.0055 -0.0317 456 ASP A CB 3520 C CG . ASP A 456 ? 0.2287 0.2788 0.2588 0.0108 -0.0062 -0.0347 456 ASP A CG 3521 O OD1 . ASP A 456 ? 0.2559 0.3069 0.2853 0.0133 -0.0073 -0.0343 456 ASP A OD1 3522 O OD2 . ASP A 456 ? 0.2795 0.3338 0.3115 0.0096 -0.0054 -0.0376 456 ASP A OD2 3523 N N . PRO A 457 ? 0.1897 0.2374 0.2153 0.0160 -0.0081 -0.0292 457 PRO A N 3524 C CA . PRO A 457 ? 0.1870 0.2334 0.2104 0.0194 -0.0090 -0.0269 457 PRO A CA 3525 C C . PRO A 457 ? 0.1974 0.2409 0.2203 0.0200 -0.0091 -0.0262 457 PRO A C 3526 O O . PRO A 457 ? 0.2005 0.2404 0.2214 0.0219 -0.0092 -0.0238 457 PRO A O 3527 C CB . PRO A 457 ? 0.2109 0.2641 0.2341 0.0223 -0.0099 -0.0290 457 PRO A CB 3528 C CG . PRO A 457 ? 0.2035 0.2614 0.2295 0.0200 -0.0095 -0.0328 457 PRO A CG 3529 C CD . PRO A 457 ? 0.1974 0.2517 0.2245 0.0162 -0.0082 -0.0324 457 PRO A CD 3530 N N . SER A 458 ? 0.1913 0.2362 0.2160 0.0184 -0.0089 -0.0284 458 SER A N 3531 C CA . SER A 458 ? 0.1914 0.2335 0.2158 0.0189 -0.0091 -0.0278 458 SER A CA 3532 C C . SER A 458 ? 0.1989 0.2348 0.2229 0.0169 -0.0084 -0.0256 458 SER A C 3533 O O . SER A 458 ? 0.2258 0.2589 0.2494 0.0173 -0.0084 -0.0249 458 SER A O 3534 C CB . SER A 458 ? 0.2181 0.2639 0.2444 0.0181 -0.0091 -0.0309 458 SER A CB 3535 O OG . SER A 458 ? 0.2346 0.2799 0.2626 0.0147 -0.0081 -0.0321 458 SER A OG 3536 N N . THR A 459 ? 0.1848 0.2190 0.2091 0.0147 -0.0078 -0.0248 459 THR A N 3537 C CA . THR A 459 ? 0.1795 0.2089 0.2036 0.0128 -0.0072 -0.0231 459 THR A CA 3538 C C . THR A 459 ? 0.1915 0.2171 0.2139 0.0140 -0.0072 -0.0205 459 THR A C 3539 O O . THR A 459 ? 0.1967 0.2222 0.2182 0.0147 -0.0072 -0.0193 459 THR A O 3540 C CB . THR A 459 ? 0.1717 0.2010 0.1965 0.0104 -0.0064 -0.0232 459 THR A CB 3541 O OG1 . THR A 459 ? 0.1715 0.2037 0.1978 0.0091 -0.0059 -0.0257 459 THR A OG1 3542 C CG2 . THR A 459 ? 0.1618 0.1870 0.1863 0.0088 -0.0059 -0.0216 459 THR A CG2 3543 N N . VAL A 460 ? 0.1821 0.2044 0.2043 0.0140 -0.0070 -0.0198 460 VAL A N 3544 C CA . VAL A 460 ? 0.1853 0.2034 0.2061 0.0147 -0.0066 -0.0175 460 VAL A CA 3545 C C . VAL A 460 ? 0.1972 0.2131 0.2186 0.0122 -0.0060 -0.0167 460 VAL A C 3546 O O . VAL A 460 ? 0.2049 0.2206 0.2273 0.0103 -0.0059 -0.0175 460 VAL A O 3547 C CB . VAL A 460 ? 0.1895 0.2050 0.2099 0.0157 -0.0064 -0.0174 460 VAL A CB 3548 C CG1 . VAL A 460 ? 0.2030 0.2137 0.2223 0.0160 -0.0054 -0.0154 460 VAL A CG1 3549 C CG2 . VAL A 460 ? 0.1959 0.2139 0.2155 0.0188 -0.0070 -0.0181 460 VAL A CG2 3550 N N . VAL A 461 ? 0.1828 0.1973 0.2033 0.0122 -0.0056 -0.0150 461 VAL A N 3551 C CA . VAL A 461 ? 0.1805 0.1935 0.2014 0.0101 -0.0051 -0.0143 461 VAL A CA 3552 C C . VAL A 461 ? 0.1962 0.2052 0.2166 0.0100 -0.0043 -0.0130 461 VAL A C 3553 O O . VAL A 461 ? 0.2286 0.2357 0.2477 0.0116 -0.0038 -0.0115 461 VAL A O 3554 C CB . VAL A 461 ? 0.1828 0.1972 0.2032 0.0101 -0.0051 -0.0135 461 VAL A CB 3555 C CG1 . VAL A 461 ? 0.1894 0.2026 0.2102 0.0081 -0.0047 -0.0128 461 VAL A CG1 3556 C CG2 . VAL A 461 ? 0.1902 0.2085 0.2113 0.0099 -0.0056 -0.0151 461 VAL A CG2 3557 N N . VAL A 462 ? 0.1890 0.1969 0.2106 0.0082 -0.0040 -0.0136 462 VAL A N 3558 C CA . VAL A 462 ? 0.1873 0.1917 0.2090 0.0075 -0.0030 -0.0129 462 VAL A CA 3559 C C . VAL A 462 ? 0.1922 0.1970 0.2145 0.0055 -0.0026 -0.0125 462 VAL A C 3560 O O . VAL A 462 ? 0.1973 0.2045 0.2204 0.0044 -0.0032 -0.0134 462 VAL A O 3561 C CB . VAL A 462 ? 0.1877 0.1912 0.2105 0.0068 -0.0028 -0.0143 462 VAL A CB 3562 C CG1 . VAL A 462 ? 0.2066 0.2067 0.2298 0.0056 -0.0015 -0.0141 462 VAL A CG1 3563 C CG2 . VAL A 462 ? 0.2009 0.2042 0.2229 0.0089 -0.0032 -0.0146 462 VAL A CG2 3564 N N . PHE A 463 ? 0.1940 0.1964 0.2158 0.0054 -0.0016 -0.0112 463 PHE A N 3565 C CA . PHE A 463 ? 0.1883 0.1911 0.2109 0.0035 -0.0012 -0.0111 463 PHE A CA 3566 C C . PHE A 463 ? 0.1999 0.2006 0.2237 0.0019 0.0000 -0.0119 463 PHE A C 3567 O O . PHE A 463 ? 0.2264 0.2234 0.2498 0.0024 0.0013 -0.0115 463 PHE A O 3568 C CB . PHE A 463 ? 0.1925 0.1945 0.2139 0.0041 -0.0006 -0.0093 463 PHE A CB 3569 C CG . PHE A 463 ? 0.2045 0.2068 0.2267 0.0023 0.0000 -0.0092 463 PHE A CG 3570 C CD1 . PHE A 463 ? 0.1959 0.2014 0.2189 0.0011 -0.0008 -0.0100 463 PHE A CD1 3571 C CD2 . PHE A 463 ? 0.2323 0.2316 0.2543 0.0018 0.0015 -0.0083 463 PHE A CD2 3572 C CE1 . PHE A 463 ? 0.2163 0.2229 0.2401 -0.0004 -0.0003 -0.0100 463 PHE A CE1 3573 C CE2 . PHE A 463 ? 0.2570 0.2573 0.2801 -0.0001 0.0021 -0.0085 463 PHE A CE2 3574 C CZ . PHE A 463 ? 0.2327 0.2368 0.2566 -0.0011 0.0011 -0.0094 463 PHE A CZ 3575 N N . ALA A 464 ? 0.1934 0.1966 0.2187 0.0001 -0.0003 -0.0132 464 ALA A N 3576 C CA . ALA A 464 ? 0.1916 0.1938 0.2185 -0.0018 0.0009 -0.0145 464 ALA A CA 3577 C C . ALA A 464 ? 0.2075 0.2130 0.2352 -0.0032 0.0006 -0.0150 464 ALA A C 3578 O O . ALA A 464 ? 0.2141 0.2231 0.2419 -0.0031 -0.0005 -0.0157 464 ALA A O 3579 C CB . ALA A 464 ? 0.2159 0.2184 0.2439 -0.0022 0.0007 -0.0165 464 ALA A CB 3580 N N . GLU A 465 ? 0.2006 0.2052 0.2289 -0.0044 0.0019 -0.0148 465 GLU A N 3581 C CA . GLU A 465 ? 0.2195 0.2278 0.2485 -0.0054 0.0015 -0.0152 465 GLU A CA 3582 C C . GLU A 465 ? 0.2196 0.2318 0.2503 -0.0065 0.0010 -0.0176 465 GLU A C 3583 O O . GLU A 465 ? 0.2302 0.2462 0.2605 -0.0061 -0.0001 -0.0178 465 GLU A O 3584 C CB . GLU A 465 ? 0.2498 0.2565 0.2793 -0.0066 0.0031 -0.0148 465 GLU A CB 3585 C CG . GLU A 465 ? 0.2876 0.2985 0.3177 -0.0074 0.0026 -0.0152 465 GLU A CG 3586 C CD . GLU A 465 ? 0.3499 0.3595 0.3803 -0.0085 0.0041 -0.0145 465 GLU A CD 3587 O OE1 . GLU A 465 ? 0.3685 0.3737 0.3977 -0.0079 0.0053 -0.0128 465 GLU A OE1 3588 O OE2 . GLU A 465 ? 0.3560 0.3694 0.3876 -0.0096 0.0040 -0.0156 465 GLU A OE2 3589 N N . ASN A 466 ? 0.2048 0.2160 0.2371 -0.0078 0.0019 -0.0195 466 ASN A N 3590 C CA . ASN A 466 ? 0.2304 0.2458 0.2645 -0.0088 0.0015 -0.0222 466 ASN A CA 3591 C C . ASN A 466 ? 0.2332 0.2471 0.2682 -0.0091 0.0018 -0.0237 466 ASN A C 3592 O O . ASN A 466 ? 0.2408 0.2541 0.2779 -0.0109 0.0031 -0.0259 466 ASN A O 3593 C CB A ASN A 466 ? 0.2423 0.2598 0.2784 -0.0110 0.0027 -0.0238 466 ASN A CB 3594 C CB B ASN A 466 ? 0.2115 0.2294 0.2477 -0.0110 0.0026 -0.0241 466 ASN A CB 3595 C CG A ASN A 466 ? 0.2592 0.2826 0.2969 -0.0117 0.0020 -0.0266 466 ASN A CG 3596 C CG B ASN A 466 ? 0.2042 0.2251 0.2398 -0.0107 0.0021 -0.0231 466 ASN A CG 3597 O OD1 A ASN A 466 ? 0.2962 0.3219 0.3363 -0.0137 0.0030 -0.0290 466 ASN A OD1 3598 O OD1 B ASN A 466 ? 0.1961 0.2208 0.2307 -0.0094 0.0006 -0.0228 466 ASN A OD1 3599 N ND2 A ASN A 466 ? 0.2549 0.2812 0.2914 -0.0099 0.0003 -0.0264 466 ASN A ND2 3600 N ND2 B ASN A 466 ? 0.2187 0.2376 0.2547 -0.0118 0.0035 -0.0225 466 ASN A ND2 3601 N N . PRO A 467 ? 0.2183 0.2314 0.2519 -0.0074 0.0007 -0.0229 467 PRO A N 3602 C CA . PRO A 467 ? 0.2284 0.2401 0.2627 -0.0075 0.0009 -0.0243 467 PRO A CA 3603 C C . PRO A 467 ? 0.2368 0.2530 0.2729 -0.0084 0.0004 -0.0271 467 PRO A C 3604 O O . PRO A 467 ? 0.2488 0.2697 0.2848 -0.0080 -0.0006 -0.0276 467 PRO A O 3605 C CB . PRO A 467 ? 0.2303 0.2413 0.2628 -0.0053 -0.0004 -0.0228 467 PRO A CB 3606 C CG . PRO A 467 ? 0.2222 0.2361 0.2534 -0.0046 -0.0014 -0.0216 467 PRO A CG 3607 C CD . PRO A 467 ? 0.2221 0.2360 0.2537 -0.0055 -0.0006 -0.0210 467 PRO A CD 3608 N N . ASP A 468 ? 0.2869 0.3016 0.3245 -0.0094 0.0013 -0.0291 468 ASP A N 3609 C CA . ASP A 468 ? 0.2928 0.3120 0.3319 -0.0099 0.0006 -0.0318 468 ASP A CA 3610 C C . ASP A 468 ? 0.2823 0.3023 0.3200 -0.0081 -0.0008 -0.0314 468 ASP A C 3611 O O . ASP A 468 ? 0.2737 0.2905 0.3096 -0.0066 -0.0011 -0.0292 468 ASP A O 3612 C CB . ASP A 468 ? 0.3339 0.3523 0.3756 -0.0121 0.0023 -0.0348 468 ASP A CB 3613 C CG . ASP A 468 ? 0.3612 0.3739 0.4028 -0.0120 0.0033 -0.0346 468 ASP A CG 3614 O OD1 . ASP A 468 ? 0.4058 0.4163 0.4494 -0.0139 0.0053 -0.0367 468 ASP A OD1 3615 O OD2 . ASP A 468 ? 0.3294 0.3401 0.3692 -0.0100 0.0024 -0.0328 468 ASP A OD2 3616 N N . ALA A 469 ? 0.2778 0.3024 0.3163 -0.0080 -0.0015 -0.0335 469 ALA A N 3617 C CA . ALA A 469 ? 0.2725 0.2985 0.3097 -0.0063 -0.0027 -0.0331 469 ALA A CA 3618 C C . ALA A 469 ? 0.2713 0.2932 0.3084 -0.0060 -0.0025 -0.0330 469 ALA A C 3619 O O . ALA A 469 ? 0.2593 0.2802 0.2948 -0.0044 -0.0032 -0.0316 469 ALA A O 3620 C CB . ALA A 469 ? 0.3171 0.3490 0.3553 -0.0063 -0.0033 -0.0357 469 ALA A CB 3621 N N . GLU A 470 ? 0.2905 0.3099 0.3293 -0.0074 -0.0013 -0.0346 470 GLU A N 3622 C CA . GLU A 470 ? 0.2774 0.2929 0.3160 -0.0068 -0.0009 -0.0346 470 GLU A CA 3623 C C . GLU A 470 ? 0.2578 0.2686 0.2944 -0.0054 -0.0007 -0.0316 470 GLU A C 3624 O O . GLU A 470 ? 0.2587 0.2682 0.2942 -0.0039 -0.0013 -0.0309 470 GLU A O 3625 C CB . GLU A 470 ? 0.3048 0.3181 0.3456 -0.0087 0.0008 -0.0370 470 GLU A CB 3626 C CG . GLU A 470 ? 0.4172 0.4258 0.4576 -0.0079 0.0015 -0.0368 470 GLU A CG 3627 C CD . GLU A 470 ? 0.4557 0.4607 0.4979 -0.0097 0.0037 -0.0388 470 GLU A CD 3628 O OE1 . GLU A 470 ? 0.4277 0.4272 0.4689 -0.0087 0.0048 -0.0377 470 GLU A OE1 3629 O OE2 . GLU A 470 ? 0.4213 0.4290 0.4659 -0.0119 0.0045 -0.0415 470 GLU A OE2 3630 N N . PHE A 471 ? 0.2485 0.2574 0.2847 -0.0058 0.0000 -0.0301 471 PHE A N 3631 C CA . PHE A 471 ? 0.2409 0.2463 0.2752 -0.0043 0.0001 -0.0274 471 PHE A CA 3632 C C . PHE A 471 ? 0.2279 0.2358 0.2606 -0.0026 -0.0016 -0.0261 471 PHE A C 3633 O O . PHE A 471 ? 0.2409 0.2470 0.2724 -0.0010 -0.0019 -0.0251 471 PHE A O 3634 C CB . PHE A 471 ? 0.2556 0.2596 0.2896 -0.0050 0.0010 -0.0260 471 PHE A CB 3635 C CG . PHE A 471 ? 0.2762 0.2775 0.3081 -0.0032 0.0010 -0.0233 471 PHE A CG 3636 C CD1 . PHE A 471 ? 0.2659 0.2697 0.2966 -0.0022 -0.0004 -0.0219 471 PHE A CD1 3637 C CD2 . PHE A 471 ? 0.3176 0.3139 0.3486 -0.0025 0.0025 -0.0221 471 PHE A CD2 3638 C CE1 . PHE A 471 ? 0.3112 0.3132 0.3401 -0.0006 -0.0004 -0.0197 471 PHE A CE1 3639 C CE2 . PHE A 471 ? 0.3358 0.3301 0.3646 -0.0006 0.0024 -0.0196 471 PHE A CE2 3640 C CZ . PHE A 471 ? 0.3255 0.3231 0.3535 0.0003 0.0008 -0.0186 471 PHE A CZ 3641 N N . VAL A 472 ? 0.2221 0.2340 0.2549 -0.0029 -0.0024 -0.0264 472 VAL A N 3642 C CA . VAL A 472 ? 0.2033 0.2170 0.2346 -0.0016 -0.0035 -0.0253 472 VAL A CA 3643 C C . VAL A 472 ? 0.2052 0.2197 0.2364 -0.0007 -0.0040 -0.0263 472 VAL A C 3644 O O . VAL A 472 ? 0.2159 0.2298 0.2461 0.0004 -0.0044 -0.0254 472 VAL A O 3645 C CB . VAL A 472 ? 0.1992 0.2167 0.2302 -0.0018 -0.0039 -0.0252 472 VAL A CB 3646 C CG1 . VAL A 472 ? 0.2295 0.2480 0.2588 -0.0005 -0.0044 -0.0240 472 VAL A CG1 3647 C CG2 . VAL A 472 ? 0.2237 0.2405 0.2549 -0.0027 -0.0033 -0.0244 472 VAL A CG2 3648 N N . LYS A 473 ? 0.2262 0.2424 0.2586 -0.0014 -0.0040 -0.0283 473 LYS A N 3649 C CA . LYS A 473 ? 0.2320 0.2492 0.2645 -0.0007 -0.0046 -0.0294 473 LYS A CA 3650 C C . LYS A 473 ? 0.2267 0.2405 0.2590 0.0001 -0.0044 -0.0291 473 LYS A C 3651 O O . LYS A 473 ? 0.2456 0.2600 0.2774 0.0011 -0.0049 -0.0293 473 LYS A O 3652 C CB . LYS A 473 ? 0.2558 0.2756 0.2898 -0.0016 -0.0045 -0.0318 473 LYS A CB 3653 C CG . LYS A 473 ? 0.3295 0.3539 0.3631 -0.0014 -0.0050 -0.0322 473 LYS A CG 3654 C CD . LYS A 473 ? 0.3890 0.4166 0.4242 -0.0022 -0.0050 -0.0349 473 LYS A CD 3655 C CE . LYS A 473 ? 0.4718 0.5044 0.5066 -0.0018 -0.0054 -0.0353 473 LYS A CE 3656 N NZ . LYS A 473 ? 0.5635 0.5999 0.6003 -0.0028 -0.0054 -0.0384 473 LYS A NZ 3657 N N . SER A 474 ? 0.2282 0.2385 0.2608 -0.0003 -0.0035 -0.0288 474 SER A N 3658 C CA . SER A 474 ? 0.2361 0.2429 0.2682 0.0009 -0.0031 -0.0284 474 SER A CA 3659 C C . SER A 474 ? 0.2408 0.2461 0.2712 0.0025 -0.0033 -0.0263 474 SER A C 3660 O O . SER A 474 ? 0.2454 0.2486 0.2751 0.0040 -0.0031 -0.0259 474 SER A O 3661 C CB . SER A 474 ? 0.2468 0.2499 0.2799 0.0000 -0.0015 -0.0292 474 SER A CB 3662 O OG A SER A 474 ? 0.2742 0.2791 0.3092 -0.0017 -0.0012 -0.0316 474 SER A OG 3663 O OG B SER A 474 ? 0.2197 0.2203 0.2524 -0.0004 -0.0005 -0.0278 474 SER A OG 3664 N N . GLY A 475 ? 0.2370 0.2439 0.2668 0.0024 -0.0037 -0.0251 475 GLY A N 3665 C CA . GLY A 475 ? 0.2490 0.2544 0.2774 0.0038 -0.0036 -0.0233 475 GLY A CA 3666 C C . GLY A 475 ? 0.2327 0.2402 0.2603 0.0052 -0.0046 -0.0231 475 GLY A C 3667 O O . GLY A 475 ? 0.2664 0.2734 0.2929 0.0065 -0.0046 -0.0219 475 GLY A O 3668 N N . GLY A 476 ? 0.2194 0.2294 0.2476 0.0050 -0.0051 -0.0244 476 GLY A N 3669 C CA . GLY A 476 ? 0.2195 0.2317 0.2473 0.0060 -0.0057 -0.0246 476 GLY A CA 3670 C C . GLY A 476 ? 0.2207 0.2345 0.2479 0.0058 -0.0058 -0.0237 476 GLY A C 3671 O O . GLY A 476 ? 0.2288 0.2438 0.2556 0.0069 -0.0061 -0.0237 476 GLY A O 3672 N N . PHE A 477 ? 0.2124 0.2265 0.2397 0.0046 -0.0055 -0.0233 477 PHE A N 3673 C CA . PHE A 477 ? 0.1960 0.2112 0.2226 0.0044 -0.0054 -0.0224 477 PHE A CA 3674 C C . PHE A 477 ? 0.1924 0.2097 0.2190 0.0040 -0.0052 -0.0231 477 PHE A C 3675 O O . PHE A 477 ? 0.2046 0.2227 0.2315 0.0037 -0.0050 -0.0240 477 PHE A O 3676 C CB . PHE A 477 ? 0.1841 0.1988 0.2107 0.0034 -0.0051 -0.0214 477 PHE A CB 3677 C CG . PHE A 477 ? 0.1793 0.1916 0.2059 0.0034 -0.0049 -0.0206 477 PHE A CG 3678 C CD1 . PHE A 477 ? 0.1892 0.2003 0.2150 0.0045 -0.0048 -0.0195 477 PHE A CD1 3679 C CD2 . PHE A 477 ? 0.1926 0.2039 0.2200 0.0025 -0.0045 -0.0211 477 PHE A CD2 3680 C CE1 . PHE A 477 ? 0.1888 0.1972 0.2142 0.0047 -0.0043 -0.0185 477 PHE A CE1 3681 C CE2 . PHE A 477 ? 0.1948 0.2033 0.2223 0.0023 -0.0038 -0.0205 477 PHE A CE2 3682 C CZ . PHE A 477 ? 0.1939 0.2007 0.2202 0.0035 -0.0036 -0.0190 477 PHE A CZ 3683 N N . SER A 478 ? 0.1904 0.2088 0.2167 0.0042 -0.0049 -0.0229 478 SER A N 3684 C CA . SER A 478 ? 0.1735 0.1932 0.1996 0.0036 -0.0041 -0.0235 478 SER A CA 3685 C C . SER A 478 ? 0.1856 0.2051 0.2109 0.0030 -0.0034 -0.0226 478 SER A C 3686 O O . SER A 478 ? 0.1917 0.2115 0.2165 0.0027 -0.0025 -0.0229 478 SER A O 3687 C CB . SER A 478 ? 0.1834 0.2045 0.2098 0.0038 -0.0039 -0.0241 478 SER A CB 3688 O OG . SER A 478 ? 0.2092 0.2314 0.2363 0.0047 -0.0045 -0.0254 478 SER A OG 3689 N N . TYR A 479 ? 0.1665 0.1851 0.1915 0.0029 -0.0036 -0.0214 479 TYR A N 3690 C CA . TYR A 479 ? 0.1735 0.1921 0.1975 0.0025 -0.0030 -0.0204 479 TYR A CA 3691 C C . TYR A 479 ? 0.1643 0.1821 0.1884 0.0024 -0.0036 -0.0193 479 TYR A C 3692 O O . TYR A 479 ? 0.1658 0.1828 0.1904 0.0027 -0.0041 -0.0192 479 TYR A O 3693 C CB . TYR A 479 ? 0.1839 0.2026 0.2071 0.0024 -0.0018 -0.0200 479 TYR A CB 3694 C CG . TYR A 479 ? 0.1848 0.2036 0.2083 0.0023 -0.0018 -0.0202 479 TYR A CG 3695 C CD1 . TYR A 479 ? 0.1867 0.2051 0.2099 0.0024 -0.0021 -0.0190 479 TYR A CD1 3696 C CD2 . TYR A 479 ? 0.1896 0.2094 0.2138 0.0022 -0.0014 -0.0216 479 TYR A CD2 3697 C CE1 . TYR A 479 ? 0.1899 0.2089 0.2134 0.0025 -0.0022 -0.0193 479 TYR A CE1 3698 C CE2 . TYR A 479 ? 0.2003 0.2211 0.2250 0.0023 -0.0015 -0.0221 479 TYR A CE2 3699 C CZ . TYR A 479 ? 0.1895 0.2099 0.2138 0.0025 -0.0019 -0.0209 479 TYR A CZ 3700 O OH . TYR A 479 ? 0.2046 0.2264 0.2292 0.0028 -0.0020 -0.0214 479 TYR A OH 3701 N N . ALA A 480 ? 0.1648 0.1831 0.1883 0.0022 -0.0033 -0.0185 480 ALA A N 3702 C CA . ALA A 480 ? 0.1554 0.1731 0.1789 0.0019 -0.0035 -0.0176 480 ALA A CA 3703 C C . ALA A 480 ? 0.1595 0.1776 0.1819 0.0020 -0.0030 -0.0165 480 ALA A C 3704 O O . ALA A 480 ? 0.1688 0.1876 0.1903 0.0023 -0.0023 -0.0165 480 ALA A O 3705 C CB . ALA A 480 ? 0.1657 0.1840 0.1900 0.0015 -0.0038 -0.0181 480 ALA A CB 3706 N N . ILE A 481 ? 0.1540 0.1715 0.1765 0.0018 -0.0031 -0.0156 481 ILE A N 3707 C CA . ILE A 481 ? 0.1576 0.1755 0.1791 0.0019 -0.0027 -0.0145 481 ILE A CA 3708 C C . ILE A 481 ? 0.1620 0.1802 0.1840 0.0014 -0.0030 -0.0142 481 ILE A C 3709 O O . ILE A 481 ? 0.1667 0.1838 0.1895 0.0011 -0.0033 -0.0140 481 ILE A O 3710 C CB . ILE A 481 ? 0.1551 0.1723 0.1763 0.0020 -0.0025 -0.0139 481 ILE A CB 3711 C CG1 . ILE A 481 ? 0.1706 0.1879 0.1917 0.0022 -0.0019 -0.0148 481 ILE A CG1 3712 C CG2 . ILE A 481 ? 0.1578 0.1752 0.1782 0.0020 -0.0021 -0.0128 481 ILE A CG2 3713 C CD1 . ILE A 481 ? 0.1847 0.2021 0.2061 0.0023 -0.0020 -0.0150 481 ILE A CD1 3714 N N . VAL A 482 ? 0.1561 0.1761 0.1777 0.0015 -0.0029 -0.0142 482 VAL A N 3715 C CA . VAL A 482 ? 0.1508 0.1720 0.1733 0.0008 -0.0031 -0.0144 482 VAL A CA 3716 C C . VAL A 482 ? 0.1560 0.1785 0.1775 0.0012 -0.0028 -0.0134 482 VAL A C 3717 O O . VAL A 482 ? 0.1664 0.1900 0.1865 0.0022 -0.0024 -0.0130 482 VAL A O 3718 C CB . VAL A 482 ? 0.1632 0.1866 0.1865 0.0006 -0.0033 -0.0159 482 VAL A CB 3719 C CG1 A VAL A 482 ? 0.1606 0.1857 0.1824 0.0018 -0.0031 -0.0160 482 VAL A CG1 3720 C CG1 B VAL A 482 ? 0.1482 0.1723 0.1732 -0.0006 -0.0034 -0.0167 482 VAL A CG1 3721 C CG2 A VAL A 482 ? 0.1512 0.1767 0.1756 -0.0002 -0.0034 -0.0166 482 VAL A CG2 3722 C CG2 B VAL A 482 ? 0.1558 0.1783 0.1796 0.0007 -0.0035 -0.0169 482 VAL A CG2 3723 N N . ALA A 483 ? 0.1444 0.1664 0.1664 0.0005 -0.0028 -0.0128 483 ALA A N 3724 C CA . ALA A 483 ? 0.1454 0.1684 0.1664 0.0009 -0.0026 -0.0118 483 ALA A CA 3725 C C . ALA A 483 ? 0.1544 0.1796 0.1766 0.0000 -0.0026 -0.0124 483 ALA A C 3726 O O . ALA A 483 ? 0.1544 0.1785 0.1781 -0.0012 -0.0025 -0.0129 483 ALA A O 3727 C CB . ALA A 483 ? 0.1658 0.1867 0.1864 0.0009 -0.0024 -0.0105 483 ALA A CB 3728 N N . VAL A 484 ? 0.1484 0.1767 0.1699 0.0008 -0.0026 -0.0126 484 VAL A N 3729 C CA . VAL A 484 ? 0.1501 0.1818 0.1728 0.0001 -0.0027 -0.0137 484 VAL A CA 3730 C C . VAL A 484 ? 0.1475 0.1815 0.1686 0.0014 -0.0026 -0.0128 484 VAL A C 3731 O O . VAL A 484 ? 0.1571 0.1898 0.1762 0.0028 -0.0023 -0.0113 484 VAL A O 3732 C CB . VAL A 484 ? 0.1563 0.1912 0.1801 0.0000 -0.0030 -0.0158 484 VAL A CB 3733 C CG1 . VAL A 484 ? 0.1664 0.1987 0.1917 -0.0012 -0.0030 -0.0167 484 VAL A CG1 3734 C CG2 . VAL A 484 ? 0.1673 0.2039 0.1889 0.0022 -0.0031 -0.0155 484 VAL A CG2 3735 N N . GLY A 485 ? 0.1592 0.1968 0.1813 0.0009 -0.0026 -0.0137 485 GLY A N 3736 C CA . GLY A 485 ? 0.1489 0.1893 0.1693 0.0025 -0.0026 -0.0130 485 GLY A CA 3737 C C . GLY A 485 ? 0.1544 0.1977 0.1763 0.0015 -0.0026 -0.0137 485 GLY A C 3738 O O . GLY A 485 ? 0.1649 0.2096 0.1893 -0.0005 -0.0025 -0.0155 485 GLY A O 3739 N N . GLU A 486 ? 0.1504 0.1946 0.1707 0.0027 -0.0024 -0.0124 486 GLU A N 3740 C CA . GLU A 486 ? 0.1487 0.1963 0.1701 0.0020 -0.0024 -0.0130 486 GLU A CA 3741 C C . GLU A 486 ? 0.1608 0.2051 0.1836 -0.0001 -0.0019 -0.0124 486 GLU A C 3742 O O . GLU A 486 ? 0.1681 0.2076 0.1902 -0.0002 -0.0017 -0.0108 486 GLU A O 3743 C CB . GLU A 486 ? 0.1454 0.1948 0.1643 0.0043 -0.0023 -0.0117 486 GLU A CB 3744 C CG . GLU A 486 ? 0.1655 0.2188 0.1826 0.0070 -0.0025 -0.0121 486 GLU A CG 3745 C CD . GLU A 486 ? 0.1646 0.2204 0.1794 0.0093 -0.0023 -0.0110 486 GLU A CD 3746 O OE1 . GLU A 486 ? 0.1748 0.2269 0.1875 0.0103 -0.0017 -0.0089 486 GLU A OE1 3747 O OE2 . GLU A 486 ? 0.1842 0.2463 0.1994 0.0103 -0.0027 -0.0126 486 GLU A OE2 3748 N N . HIS A 487 ? 0.1677 0.2148 0.1926 -0.0017 -0.0016 -0.0137 487 HIS A N 3749 C CA . HIS A 487 ? 0.1776 0.2216 0.2033 -0.0034 -0.0008 -0.0128 487 HIS A CA 3750 C C . HIS A 487 ? 0.1711 0.2160 0.1952 -0.0021 -0.0009 -0.0112 487 HIS A C 3751 O O . HIS A 487 ? 0.1719 0.2200 0.1946 -0.0003 -0.0014 -0.0112 487 HIS A O 3752 C CB . HIS A 487 ? 0.1982 0.2442 0.2271 -0.0059 0.0000 -0.0151 487 HIS A CB 3753 C CG . HIS A 487 ? 0.2190 0.2635 0.2495 -0.0073 0.0003 -0.0167 487 HIS A CG 3754 N ND1 . HIS A 487 ? 0.2988 0.3461 0.3322 -0.0094 0.0011 -0.0196 487 HIS A ND1 3755 C CD2 . HIS A 487 ? 0.2503 0.2913 0.2801 -0.0068 0.0000 -0.0162 487 HIS A CD2 3756 C CE1 . HIS A 487 ? 0.2717 0.3168 0.3060 -0.0102 0.0013 -0.0206 487 HIS A CE1 3757 N NE2 . HIS A 487 ? 0.2700 0.3114 0.3021 -0.0085 0.0006 -0.0185 487 HIS A NE2 3758 N N . PRO A 488 ? 0.1649 0.2066 0.1890 -0.0029 -0.0004 -0.0098 488 PRO A N 3759 C CA . PRO A 488 ? 0.1682 0.2105 0.1906 -0.0017 -0.0004 -0.0082 488 PRO A CA 3760 C C . PRO A 488 ? 0.1833 0.2311 0.2066 -0.0018 -0.0004 -0.0095 488 PRO A C 3761 O O . PRO A 488 ? 0.1815 0.2315 0.2073 -0.0038 0.0002 -0.0115 488 PRO A O 3762 C CB . PRO A 488 ? 0.1743 0.2124 0.1968 -0.0028 0.0002 -0.0068 488 PRO A CB 3763 C CG . PRO A 488 ? 0.1757 0.2099 0.1986 -0.0034 0.0003 -0.0068 488 PRO A CG 3764 C CD . PRO A 488 ? 0.1752 0.2121 0.1999 -0.0043 0.0003 -0.0091 488 PRO A CD 3765 N N . TYR A 489 ? 0.1796 0.2295 0.2010 0.0002 -0.0007 -0.0086 489 TYR A N 3766 C CA . TYR A 489 ? 0.1854 0.2410 0.2073 0.0005 -0.0008 -0.0098 489 TYR A CA 3767 C C . TYR A 489 ? 0.1975 0.2535 0.2169 0.0027 -0.0009 -0.0080 489 TYR A C 3768 O O . TYR A 489 ? 0.1905 0.2427 0.2076 0.0042 -0.0009 -0.0061 489 TYR A O 3769 C CB . TYR A 489 ? 0.1872 0.2484 0.2097 0.0015 -0.0013 -0.0120 489 TYR A CB 3770 C CG . TYR A 489 ? 0.1800 0.2403 0.1996 0.0043 -0.0018 -0.0109 489 TYR A CG 3771 C CD1 . TYR A 489 ? 0.1899 0.2515 0.2066 0.0072 -0.0018 -0.0095 489 TYR A CD1 3772 C CD2 . TYR A 489 ? 0.1718 0.2292 0.1914 0.0041 -0.0019 -0.0111 489 TYR A CD2 3773 C CE1 . TYR A 489 ? 0.1796 0.2396 0.1934 0.0098 -0.0017 -0.0083 489 TYR A CE1 3774 C CE2 . TYR A 489 ? 0.1727 0.2289 0.1896 0.0066 -0.0020 -0.0099 489 TYR A CE2 3775 C CZ . TYR A 489 ? 0.1775 0.2346 0.1915 0.0094 -0.0017 -0.0085 489 TYR A CZ 3776 O OH . TYR A 489 ? 0.1825 0.2377 0.1936 0.0119 -0.0013 -0.0073 489 TYR A OH 3777 N N . THR A 490 ? 0.2064 0.2673 0.2264 0.0029 -0.0009 -0.0088 490 THR A N 3778 C CA . THR A 490 ? 0.2478 0.3108 0.2655 0.0054 -0.0010 -0.0077 490 THR A CA 3779 C C . THR A 490 ? 0.2912 0.3618 0.3093 0.0067 -0.0014 -0.0098 490 THR A C 3780 O O . THR A 490 ? 0.3292 0.4032 0.3495 0.0054 -0.0016 -0.0122 490 THR A O 3781 C CB . THR A 490 ? 0.2557 0.3180 0.2739 0.0042 -0.0005 -0.0069 490 THR A CB 3782 O OG1 . THR A 490 ? 0.2834 0.3493 0.3049 0.0017 -0.0002 -0.0090 490 THR A OG1 3783 C CG2 . THR A 490 ? 0.2458 0.3015 0.2636 0.0032 -0.0002 -0.0050 490 THR A CG2 3784 N N . GLU A 491 ? 0.3371 0.4108 0.3531 0.0093 -0.0015 -0.0091 491 GLU A N 3785 C CA . GLU A 491 ? 0.4997 0.5815 0.5160 0.0109 -0.0020 -0.0113 491 GLU A CA 3786 C C . GLU A 491 ? 0.6132 0.7002 0.6336 0.0080 -0.0022 -0.0148 491 GLU A C 3787 O O . GLU A 491 ? 0.6774 0.7687 0.6986 0.0086 -0.0026 -0.0169 491 GLU A O 3788 C CB . GLU A 491 ? 0.5472 0.6325 0.5620 0.0129 -0.0020 -0.0106 491 GLU A CB 3789 C CG . GLU A 491 ? 0.6320 0.7112 0.6451 0.0130 -0.0014 -0.0078 491 GLU A CG 3790 C CD . GLU A 491 ? 0.6969 0.7756 0.7125 0.0100 -0.0011 -0.0081 491 GLU A CD 3791 O OE1 . GLU A 491 ? 0.7790 0.8631 0.7974 0.0082 -0.0011 -0.0105 491 GLU A OE1 3792 O OE2 . GLU A 491 ? 0.7158 0.7891 0.7304 0.0095 -0.0007 -0.0060 491 GLU A OE2 3793 N N . THR A 492 ? 0.6929 0.7797 0.7161 0.0049 -0.0015 -0.0155 492 THR A N 3794 C CA . THR A 492 ? 0.7994 0.8915 0.8266 0.0020 -0.0012 -0.0191 492 THR A CA 3795 C C . THR A 492 ? 0.8338 0.9218 0.8632 -0.0008 -0.0007 -0.0201 492 THR A C 3796 O O . THR A 492 ? 0.8842 0.9667 0.9149 -0.0035 0.0003 -0.0192 492 THR A O 3797 C CB . THR A 492 ? 0.8071 0.9008 0.8363 -0.0002 -0.0003 -0.0197 492 THR A CB 3798 O OG1 . THR A 492 ? 0.7758 0.8615 0.8046 -0.0018 0.0005 -0.0171 492 THR A OG1 3799 C CG2 . THR A 492 ? 0.8219 0.9208 0.8492 0.0027 -0.0009 -0.0193 492 THR A CG2 3800 N N . LYS A 493 ? 0.8166 0.9078 0.8464 0.0000 -0.0013 -0.0219 493 LYS A N 3801 C CA . LYS A 493 ? 0.7424 0.8298 0.7733 -0.0017 -0.0011 -0.0226 493 LYS A CA 3802 C C . LYS A 493 ? 0.6473 0.7314 0.6748 0.0014 -0.0020 -0.0204 493 LYS A C 3803 O O . LYS A 493 ? 0.6473 0.7302 0.6753 0.0010 -0.0021 -0.0212 493 LYS A O 3804 C CB . LYS A 493 ? 0.7620 0.8422 0.7946 -0.0050 0.0002 -0.0217 493 LYS A CB 3805 C CG . LYS A 493 ? 0.7375 0.8126 0.7706 -0.0061 0.0004 -0.0215 493 LYS A CG 3806 C CD . LYS A 493 ? 0.7316 0.7982 0.7635 -0.0069 0.0010 -0.0185 493 LYS A CD 3807 C CE . LYS A 493 ? 0.7005 0.7623 0.7333 -0.0083 0.0014 -0.0187 493 LYS A CE 3808 N NZ . LYS A 493 ? 0.5497 0.6093 0.5802 -0.0061 0.0003 -0.0175 493 LYS A NZ 3809 N N . GLY A 494 ? 0.5308 0.6133 0.5549 0.0043 -0.0023 -0.0176 494 GLY A N 3810 C CA . GLY A 494 ? 0.4646 0.5436 0.4852 0.0071 -0.0026 -0.0154 494 GLY A CA 3811 C C . GLY A 494 ? 0.4903 0.5753 0.5087 0.0108 -0.0032 -0.0160 494 GLY A C 3812 O O . GLY A 494 ? 0.3137 0.3974 0.3300 0.0129 -0.0033 -0.0153 494 GLY A O 3813 N N . ASP A 495 ? 0.4488 0.5405 0.4675 0.0118 -0.0034 -0.0173 495 ASP A N 3814 C CA . ASP A 495 ? 0.5099 0.6087 0.5266 0.0157 -0.0040 -0.0183 495 ASP A CA 3815 C C . ASP A 495 ? 0.5463 0.6495 0.5656 0.0145 -0.0045 -0.0215 495 ASP A C 3816 O O . ASP A 495 ? 0.4730 0.5806 0.4964 0.0114 -0.0045 -0.0247 495 ASP A O 3817 C CB . ASP A 495 ? 0.4962 0.6024 0.5134 0.0167 -0.0042 -0.0197 495 ASP A CB 3818 C CG . ASP A 495 ? 0.4841 0.5866 0.4987 0.0182 -0.0037 -0.0166 495 ASP A CG 3819 O OD1 . ASP A 495 ? 0.3846 0.4806 0.3957 0.0201 -0.0032 -0.0135 495 ASP A OD1 3820 O OD2 . ASP A 495 ? 0.5297 0.6362 0.5458 0.0173 -0.0038 -0.0177 495 ASP A OD2 3821 N N . ASN A 496 ? 0.5204 0.6221 0.5374 0.0168 -0.0046 -0.0207 496 ASN A N 3822 C CA . ASN A 496 ? 0.5555 0.6603 0.5747 0.0157 -0.0051 -0.0235 496 ASN A CA 3823 C C . ASN A 496 ? 0.5600 0.6701 0.5764 0.0200 -0.0056 -0.0240 496 ASN A C 3824 O O . ASN A 496 ? 0.5066 0.6129 0.5187 0.0235 -0.0052 -0.0210 496 ASN A O 3825 C CB . ASN A 496 ? 0.5611 0.6579 0.5817 0.0125 -0.0047 -0.0227 496 ASN A CB 3826 C CG . ASN A 496 ? 0.5646 0.6646 0.5876 0.0112 -0.0051 -0.0257 496 ASN A CG 3827 O OD1 . ASN A 496 ? 0.4732 0.5723 0.4942 0.0133 -0.0053 -0.0251 496 ASN A OD1 3828 N ND2 . ASN A 496 ? 0.5857 0.6898 0.6132 0.0078 -0.0050 -0.0293 496 ASN A ND2 3829 N N . LEU A 497 ? 0.5898 0.7087 0.6088 0.0197 -0.0064 -0.0280 497 LEU A N 3830 C CA . LEU A 497 ? 0.6065 0.7324 0.6232 0.0238 -0.0070 -0.0291 497 LEU A CA 3831 C C . LEU A 497 ? 0.5460 0.6674 0.5614 0.0245 -0.0069 -0.0282 497 LEU A C 3832 O O . LEU A 497 ? 0.5725 0.6939 0.5835 0.0289 -0.0068 -0.0262 497 LEU A O 3833 C CB . LEU A 497 ? 0.6952 0.8328 0.7157 0.0230 -0.0079 -0.0343 497 LEU A CB 3834 C CG B LEU A 497 ? 0.7577 0.8973 0.7844 0.0173 -0.0077 -0.0384 497 LEU A CG 3835 C CD1 B LEU A 497 ? 0.7491 0.9015 0.7787 0.0176 -0.0085 -0.0438 497 LEU A CD1 3836 C CD2 B LEU A 497 ? 0.7089 0.8433 0.7382 0.0131 -0.0068 -0.0378 497 LEU A CD2 3837 N N . ASN A 498 ? 0.4241 0.5414 0.4429 0.0202 -0.0068 -0.0294 498 ASN A N 3838 C CA . ASN A 498 ? 0.3817 0.4972 0.4002 0.0204 -0.0069 -0.0297 498 ASN A CA 3839 C C . ASN A 498 ? 0.3347 0.4396 0.3504 0.0206 -0.0062 -0.0258 498 ASN A C 3840 O O . ASN A 498 ? 0.3494 0.4529 0.3633 0.0223 -0.0061 -0.0252 498 ASN A O 3841 C CB . ASN A 498 ? 0.4210 0.5390 0.4448 0.0160 -0.0072 -0.0338 498 ASN A CB 3842 C CG . ASN A 498 ? 0.4949 0.6057 0.5217 0.0112 -0.0064 -0.0333 498 ASN A CG 3843 O OD1 . ASN A 498 ? 0.4129 0.5152 0.4391 0.0099 -0.0059 -0.0310 498 ASN A OD1 3844 N ND2 . ASN A 498 ? 0.4781 0.5924 0.5080 0.0087 -0.0061 -0.0353 498 ASN A ND2 3845 N N . LEU A 499 ? 0.2911 0.3891 0.3066 0.0190 -0.0055 -0.0233 499 LEU A N 3846 C CA . LEU A 499 ? 0.2316 0.3202 0.2449 0.0189 -0.0047 -0.0199 499 LEU A CA 3847 C C . LEU A 499 ? 0.2351 0.3201 0.2497 0.0172 -0.0047 -0.0205 499 LEU A C 3848 O O . LEU A 499 ? 0.2130 0.2929 0.2249 0.0187 -0.0042 -0.0183 499 LEU A O 3849 C CB . LEU A 499 ? 0.2333 0.3197 0.2414 0.0233 -0.0039 -0.0167 499 LEU A CB 3850 C CG . LEU A 499 ? 0.2308 0.3194 0.2371 0.0254 -0.0036 -0.0155 499 LEU A CG 3851 C CD1 . LEU A 499 ? 0.2429 0.3275 0.2439 0.0295 -0.0023 -0.0122 499 LEU A CD1 3852 C CD2 . LEU A 499 ? 0.2676 0.3526 0.2763 0.0218 -0.0036 -0.0151 499 LEU A CD2 3853 N N . THR A 500 ? 0.2250 0.3123 0.2437 0.0139 -0.0052 -0.0235 500 THR A N 3854 C CA . THR A 500 ? 0.2441 0.3282 0.2646 0.0117 -0.0053 -0.0245 500 THR A CA 3855 C C . THR A 500 ? 0.2417 0.3194 0.2647 0.0079 -0.0048 -0.0239 500 THR A C 3856 O O . THR A 500 ? 0.2741 0.3534 0.2995 0.0056 -0.0046 -0.0252 500 THR A O 3857 C CB . THR A 500 ? 0.2681 0.3597 0.2914 0.0111 -0.0059 -0.0286 500 THR A CB 3858 O OG1 A THR A 500 ? 0.3071 0.4014 0.3345 0.0077 -0.0058 -0.0313 500 THR A OG1 3859 O OG1 B THR A 500 ? 0.2607 0.3580 0.2811 0.0153 -0.0064 -0.0288 500 THR A OG1 3860 C CG2 A THR A 500 ? 0.2783 0.3777 0.2992 0.0152 -0.0065 -0.0294 500 THR A CG2 3861 C CG2 B THR A 500 ? 0.2248 0.3132 0.2504 0.0085 -0.0059 -0.0300 500 THR A CG2 3862 N N . ILE A 501 ? 0.2230 0.2939 0.2454 0.0071 -0.0045 -0.0223 501 ILE A N 3863 C CA . ILE A 501 ? 0.2281 0.2931 0.2524 0.0040 -0.0040 -0.0215 501 ILE A CA 3864 C C . ILE A 501 ? 0.2294 0.2958 0.2576 0.0008 -0.0038 -0.0245 501 ILE A C 3865 O O . ILE A 501 ? 0.2254 0.2959 0.2551 0.0006 -0.0042 -0.0271 501 ILE A O 3866 C CB . ILE A 501 ? 0.2167 0.2746 0.2394 0.0042 -0.0037 -0.0192 501 ILE A CB 3867 C CG1 . ILE A 501 ? 0.2217 0.2795 0.2449 0.0042 -0.0040 -0.0205 501 ILE A CG1 3868 C CG2 . ILE A 501 ? 0.2377 0.2938 0.2567 0.0070 -0.0034 -0.0165 501 ILE A CG2 3869 C CD1 . ILE A 501 ? 0.2215 0.2726 0.2440 0.0037 -0.0037 -0.0188 501 ILE A CD1 3870 N N . PRO A 502 ? 0.2442 0.3073 0.2741 -0.0017 -0.0031 -0.0242 502 PRO A N 3871 C CA . PRO A 502 ? 0.2580 0.3213 0.2916 -0.0050 -0.0024 -0.0269 502 PRO A CA 3872 C C . PRO A 502 ? 0.2867 0.3465 0.3211 -0.0059 -0.0023 -0.0274 502 PRO A C 3873 O O . PRO A 502 ? 0.2544 0.3093 0.2868 -0.0048 -0.0025 -0.0252 502 PRO A O 3874 C CB . PRO A 502 ? 0.2673 0.3262 0.3015 -0.0068 -0.0014 -0.0253 502 PRO A CB 3875 C CG . PRO A 502 ? 0.3011 0.3570 0.3321 -0.0046 -0.0018 -0.0219 502 PRO A CG 3876 C CD . PRO A 502 ? 0.2613 0.3211 0.2899 -0.0015 -0.0028 -0.0216 502 PRO A CD 3877 N N . GLU A 503 ? 0.2825 0.3450 0.3199 -0.0080 -0.0018 -0.0308 503 GLU A N 3878 C CA . GLU A 503 ? 0.2979 0.3568 0.3365 -0.0092 -0.0014 -0.0316 503 GLU A CA 3879 C C . GLU A 503 ? 0.3142 0.3668 0.3542 -0.0117 0.0001 -0.0310 503 GLU A C 3880 O O . GLU A 503 ? 0.3588 0.4114 0.3999 -0.0132 0.0011 -0.0312 503 GLU A O 3881 C CB . GLU A 503 ? 0.3117 0.3767 0.3526 -0.0098 -0.0016 -0.0356 503 GLU A CB 3882 C CG . GLU A 503 ? 0.3100 0.3796 0.3485 -0.0065 -0.0031 -0.0353 503 GLU A CG 3883 C CD . GLU A 503 ? 0.3353 0.3992 0.3707 -0.0045 -0.0036 -0.0321 503 GLU A CD 3884 O OE1 . GLU A 503 ? 0.2797 0.3404 0.3162 -0.0057 -0.0034 -0.0328 503 GLU A OE1 3885 O OE2 . GLU A 503 ? 0.3187 0.3815 0.3510 -0.0021 -0.0040 -0.0292 503 GLU A OE2 3886 N N . PRO A 504 ? 0.3242 0.3710 0.3637 -0.0120 0.0004 -0.0300 504 PRO A N 3887 C CA . PRO A 504 ? 0.3095 0.3558 0.3477 -0.0103 -0.0006 -0.0296 504 PRO A CA 3888 C C . PRO A 504 ? 0.3056 0.3493 0.3404 -0.0078 -0.0015 -0.0261 504 PRO A C 3889 O O . PRO A 504 ? 0.3482 0.3877 0.3820 -0.0079 -0.0011 -0.0237 504 PRO A O 3890 C CB . PRO A 504 ? 0.3195 0.3601 0.3588 -0.0118 0.0004 -0.0299 504 PRO A CB 3891 C CG . PRO A 504 ? 0.3411 0.3770 0.3805 -0.0130 0.0018 -0.0282 504 PRO A CG 3892 C CD . PRO A 504 ? 0.3495 0.3901 0.3901 -0.0140 0.0021 -0.0294 504 PRO A CD 3893 N N . GLY A 505 ? 0.2525 0.2993 0.2857 -0.0056 -0.0026 -0.0259 505 GLY A N 3894 C CA . GLY A 505 ? 0.2040 0.2484 0.2340 -0.0034 -0.0031 -0.0230 505 GLY A CA 3895 C C . GLY A 505 ? 0.1967 0.2428 0.2257 -0.0018 -0.0037 -0.0236 505 GLY A C 3896 O O . GLY A 505 ? 0.1838 0.2260 0.2121 -0.0015 -0.0037 -0.0226 505 GLY A O 3897 N N . LEU A 506 ? 0.1919 0.2440 0.2207 -0.0006 -0.0041 -0.0251 506 LEU A N 3898 C CA . LEU A 506 ? 0.1926 0.2469 0.2204 0.0011 -0.0046 -0.0259 506 LEU A CA 3899 C C . LEU A 506 ? 0.1886 0.2414 0.2186 -0.0006 -0.0046 -0.0278 506 LEU A C 3900 O O . LEU A 506 ? 0.1878 0.2385 0.2167 0.0004 -0.0048 -0.0272 506 LEU A O 3901 C CB . LEU A 506 ? 0.1874 0.2493 0.2149 0.0028 -0.0051 -0.0276 506 LEU A CB 3902 C CG . LEU A 506 ? 0.2147 0.2795 0.2410 0.0048 -0.0055 -0.0285 506 LEU A CG 3903 C CD1 . LEU A 506 ? 0.2148 0.2756 0.2375 0.0072 -0.0051 -0.0255 506 LEU A CD1 3904 C CD2 . LEU A 506 ? 0.2095 0.2827 0.2357 0.0066 -0.0060 -0.0306 506 LEU A CD2 3905 N N . SER A 507 ? 0.1974 0.2512 0.2305 -0.0031 -0.0042 -0.0302 507 SER A N 3906 C CA . SER A 507 ? 0.1992 0.2511 0.2343 -0.0047 -0.0039 -0.0321 507 SER A CA 3907 C C . SER A 507 ? 0.1895 0.2344 0.2237 -0.0048 -0.0036 -0.0297 507 SER A C 3908 O O . SER A 507 ? 0.2047 0.2482 0.2389 -0.0046 -0.0038 -0.0303 507 SER A O 3909 C CB . SER A 507 ? 0.2259 0.2790 0.2646 -0.0077 -0.0029 -0.0349 507 SER A CB 3910 O OG . SER A 507 ? 0.2809 0.3298 0.3198 -0.0090 -0.0020 -0.0333 507 SER A OG 3911 N N . THR A 508 ? 0.1828 0.2236 0.2160 -0.0050 -0.0032 -0.0273 508 THR A N 3912 C CA . THR A 508 ? 0.1918 0.2267 0.2240 -0.0048 -0.0031 -0.0253 508 THR A CA 3913 C C . THR A 508 ? 0.1703 0.2049 0.2002 -0.0027 -0.0037 -0.0239 508 THR A C 3914 O O . THR A 508 ? 0.1774 0.2093 0.2071 -0.0025 -0.0038 -0.0238 508 THR A O 3915 C CB . THR A 508 ? 0.2104 0.2419 0.2420 -0.0052 -0.0025 -0.0232 508 THR A CB 3916 O OG1 . THR A 508 ? 0.2969 0.3280 0.3307 -0.0073 -0.0015 -0.0247 508 THR A OG1 3917 C CG2 . THR A 508 ? 0.2014 0.2277 0.2318 -0.0047 -0.0024 -0.0213 508 THR A CG2 3918 N N . VAL A 509 ? 0.1853 0.2226 0.2134 -0.0011 -0.0040 -0.0230 509 VAL A N 3919 C CA . VAL A 509 ? 0.1765 0.2132 0.2023 0.0008 -0.0041 -0.0217 509 VAL A CA 3920 C C . VAL A 509 ? 0.1825 0.2212 0.2086 0.0012 -0.0045 -0.0235 509 VAL A C 3921 O O . VAL A 509 ? 0.1839 0.2203 0.2093 0.0018 -0.0044 -0.0230 509 VAL A O 3922 C CB . VAL A 509 ? 0.1711 0.2101 0.1946 0.0026 -0.0040 -0.0204 509 VAL A CB 3923 C CG1 . VAL A 509 ? 0.1964 0.2350 0.2175 0.0046 -0.0037 -0.0195 509 VAL A CG1 3924 C CG2 . VAL A 509 ? 0.1782 0.2144 0.2011 0.0022 -0.0036 -0.0186 509 VAL A CG2 3925 N N . GLN A 510 ? 0.1793 0.2227 0.2068 0.0010 -0.0047 -0.0257 510 GLN A N 3926 C CA . GLN A 510 ? 0.1753 0.2211 0.2032 0.0015 -0.0051 -0.0275 510 GLN A CA 3927 C C . GLN A 510 ? 0.1830 0.2252 0.2127 -0.0001 -0.0050 -0.0285 510 GLN A C 3928 O O . GLN A 510 ? 0.1877 0.2292 0.2168 0.0007 -0.0052 -0.0286 510 GLN A O 3929 C CB . GLN A 510 ? 0.1891 0.2414 0.2184 0.0015 -0.0055 -0.0302 510 GLN A CB 3930 C CG . GLN A 510 ? 0.1972 0.2538 0.2241 0.0040 -0.0056 -0.0294 510 GLN A CG 3931 C CD . GLN A 510 ? 0.2366 0.3003 0.2651 0.0039 -0.0060 -0.0322 510 GLN A CD 3932 O OE1 . GLN A 510 ? 0.2705 0.3352 0.3022 0.0014 -0.0059 -0.0345 510 GLN A OE1 3933 N NE2 . GLN A 510 ? 0.2443 0.3130 0.2706 0.0068 -0.0063 -0.0321 510 GLN A NE2 3934 N N . ALA A 511 ? 0.1906 0.2302 0.2222 -0.0021 -0.0046 -0.0289 511 ALA A N 3935 C CA . ALA A 511 ? 0.2003 0.2359 0.2333 -0.0033 -0.0043 -0.0295 511 ALA A CA 3936 C C . ALA A 511 ? 0.2112 0.2426 0.2424 -0.0023 -0.0044 -0.0273 511 ALA A C 3937 O O . ALA A 511 ? 0.2164 0.2464 0.2477 -0.0020 -0.0045 -0.0278 511 ALA A O 3938 C CB . ALA A 511 ? 0.2136 0.2468 0.2485 -0.0054 -0.0034 -0.0301 511 ALA A CB 3939 N N . VAL A 512 ? 0.1818 0.2115 0.2115 -0.0017 -0.0043 -0.0250 512 VAL A N 3940 C CA . VAL A 512 ? 0.1831 0.2093 0.2114 -0.0009 -0.0043 -0.0233 512 VAL A CA 3941 C C . VAL A 512 ? 0.2076 0.2352 0.2345 0.0005 -0.0045 -0.0232 512 VAL A C 3942 O O . VAL A 512 ? 0.2029 0.2289 0.2299 0.0007 -0.0045 -0.0234 512 VAL A O 3943 C CB . VAL A 512 ? 0.1855 0.2102 0.2128 -0.0007 -0.0040 -0.0212 512 VAL A CB 3944 C CG1 . VAL A 512 ? 0.1957 0.2180 0.2216 0.0002 -0.0040 -0.0199 512 VAL A CG1 3945 C CG2 . VAL A 512 ? 0.2114 0.2339 0.2398 -0.0020 -0.0036 -0.0211 512 VAL A CG2 3946 N N . CYS A 513 ? 0.2062 0.2366 0.2318 0.0015 -0.0044 -0.0229 513 CYS A N 3947 C CA . CYS A 513 ? 0.1970 0.2281 0.2208 0.0031 -0.0041 -0.0224 513 CYS A CA 3948 C C . CYS A 513 ? 0.2184 0.2514 0.2428 0.0033 -0.0044 -0.0242 513 CYS A C 3949 O O . CYS A 513 ? 0.2194 0.2518 0.2427 0.0042 -0.0041 -0.0239 513 CYS A O 3950 C CB . CYS A 513 ? 0.2147 0.2481 0.2364 0.0046 -0.0036 -0.0213 513 CYS A CB 3951 S SG . CYS A 513 ? 0.2312 0.2624 0.2520 0.0044 -0.0032 -0.0193 513 CYS A SG 3952 N N . GLY A 514 ? 0.2017 0.2369 0.2280 0.0024 -0.0049 -0.0261 514 GLY A N 3953 C CA . GLY A 514 ? 0.2075 0.2447 0.2348 0.0025 -0.0052 -0.0281 514 GLY A CA 3954 C C . GLY A 514 ? 0.2260 0.2596 0.2540 0.0018 -0.0053 -0.0283 514 GLY A C 3955 O O . GLY A 514 ? 0.2586 0.2931 0.2868 0.0022 -0.0054 -0.0295 514 GLY A O 3956 N N . GLY A 515 ? 0.2113 0.2412 0.2398 0.0010 -0.0051 -0.0272 515 GLY A N 3957 C CA . GLY A 515 ? 0.2082 0.2348 0.2373 0.0006 -0.0051 -0.0273 515 GLY A CA 3958 C C . GLY A 515 ? 0.2142 0.2388 0.2420 0.0015 -0.0050 -0.0259 515 GLY A C 3959 O O . GLY A 515 ? 0.2321 0.2554 0.2603 0.0016 -0.0051 -0.0264 515 GLY A O 3960 N N . VAL A 516 ? 0.1929 0.2174 0.2193 0.0019 -0.0046 -0.0243 516 VAL A N 3961 C CA . VAL A 516 ? 0.1861 0.2089 0.2115 0.0024 -0.0042 -0.0233 516 VAL A CA 3962 C C . VAL A 516 ? 0.1859 0.2095 0.2095 0.0030 -0.0035 -0.0220 516 VAL A C 3963 O O . VAL A 516 ? 0.1948 0.2196 0.2180 0.0031 -0.0035 -0.0216 516 VAL A O 3964 C CB . VAL A 516 ? 0.1937 0.2141 0.2197 0.0020 -0.0044 -0.0227 516 VAL A CB 3965 C CG1 . VAL A 516 ? 0.1800 0.1998 0.2058 0.0017 -0.0043 -0.0215 516 VAL A CG1 3966 C CG2 . VAL A 516 ? 0.2050 0.2246 0.2306 0.0025 -0.0042 -0.0227 516 VAL A CG2 3967 N N . ARG A 517 ? 0.1870 0.2097 0.2096 0.0034 -0.0026 -0.0216 517 ARG A N 3968 C CA . ARG A 517 ? 0.1843 0.2068 0.2051 0.0040 -0.0015 -0.0203 517 ARG A CA 3969 C C . ARG A 517 ? 0.1907 0.2125 0.2117 0.0035 -0.0017 -0.0193 517 ARG A C 3970 O O . ARG A 517 ? 0.1832 0.2037 0.2052 0.0029 -0.0023 -0.0194 517 ARG A O 3971 C CB . ARG A 517 ? 0.2134 0.2345 0.2335 0.0040 -0.0002 -0.0203 517 ARG A CB 3972 C CG B ARG A 517 ? 0.1958 0.2159 0.2173 0.0032 -0.0004 -0.0209 517 ARG A CG 3973 C CG C ARG A 517 ? 0.2374 0.2590 0.2568 0.0047 0.0008 -0.0208 517 ARG A CG 3974 C CD B ARG A 517 ? 0.2309 0.2506 0.2524 0.0030 0.0008 -0.0219 517 ARG A CD 3975 C CD C ARG A 517 ? 0.2609 0.2814 0.2811 0.0039 0.0014 -0.0217 517 ARG A CD 3976 N NE B ARG A 517 ? 0.2867 0.3060 0.3090 0.0024 0.0010 -0.0221 517 ARG A NE 3977 N NE C ARG A 517 ? 0.2869 0.3059 0.3067 0.0034 0.0029 -0.0213 517 ARG A NE 3978 C CZ B ARG A 517 ? 0.3148 0.3341 0.3375 0.0018 0.0022 -0.0232 517 ARG A CZ 3979 C CZ C ARG A 517 ? 0.2824 0.3013 0.3036 0.0026 0.0025 -0.0221 517 ARG A CZ 3980 N NH1 B ARG A 517 ? 0.3685 0.3878 0.3909 0.0018 0.0034 -0.0240 517 ARG A NH1 3981 N NH1 C ARG A 517 ? 0.2844 0.3042 0.3072 0.0024 0.0008 -0.0229 517 ARG A NH1 3982 N NH2 B ARG A 517 ? 0.3150 0.3346 0.3385 0.0013 0.0023 -0.0237 517 ARG A NH2 3983 N NH2 C ARG A 517 ? 0.2564 0.2743 0.2773 0.0020 0.0040 -0.0220 517 ARG A NH2 3984 N N . CYS A 518 ? 0.1931 0.2155 0.2127 0.0041 -0.0012 -0.0182 518 CYS A N 3985 C CA . CYS A 518 ? 0.1944 0.2164 0.2141 0.0037 -0.0015 -0.0173 518 CYS A CA 3986 C C . CYS A 518 ? 0.1972 0.2187 0.2151 0.0044 -0.0003 -0.0160 518 CYS A C 3987 O O . CYS A 518 ? 0.2110 0.2331 0.2271 0.0056 0.0007 -0.0155 518 CYS A O 3988 C CB . CYS A 518 ? 0.2176 0.2418 0.2382 0.0035 -0.0024 -0.0178 518 CYS A CB 3989 S SG . CYS A 518 ? 0.2509 0.2782 0.2696 0.0051 -0.0019 -0.0177 518 CYS A SG 3990 N N . ALA A 519 ? 0.1768 0.1971 0.1950 0.0038 -0.0003 -0.0153 519 ALA A N 3991 C CA . ALA A 519 ? 0.1675 0.1872 0.1842 0.0043 0.0007 -0.0141 519 ALA A CA 3992 C C . ALA A 519 ? 0.1610 0.1820 0.1781 0.0042 -0.0003 -0.0135 519 ALA A C 3993 O O . ALA A 519 ? 0.1696 0.1903 0.1882 0.0032 -0.0012 -0.0137 519 ALA A O 3994 C CB . ALA A 519 ? 0.1717 0.1895 0.1886 0.0037 0.0014 -0.0140 519 ALA A CB 3995 N N . THR A 520 ? 0.1580 0.1807 0.1737 0.0052 0.0000 -0.0130 520 THR A N 3996 C CA . THR A 520 ? 0.1538 0.1783 0.1700 0.0051 -0.0007 -0.0127 520 THR A CA 3997 C C . THR A 520 ? 0.1653 0.1888 0.1803 0.0054 0.0000 -0.0113 520 THR A C 3998 O O . THR A 520 ? 0.1602 0.1829 0.1731 0.0067 0.0013 -0.0105 520 THR A O 3999 C CB . THR A 520 ? 0.1613 0.1893 0.1769 0.0062 -0.0009 -0.0133 520 THR A CB 4000 O OG1 . THR A 520 ? 0.1825 0.2116 0.1997 0.0056 -0.0017 -0.0148 520 THR A OG1 4001 C CG2 . THR A 520 ? 0.1643 0.1949 0.1804 0.0061 -0.0015 -0.0132 520 THR A CG2 4002 N N . VAL A 521 ? 0.1586 0.1818 0.1748 0.0044 -0.0006 -0.0111 521 VAL A N 4003 C CA . VAL A 521 ? 0.1516 0.1741 0.1668 0.0047 -0.0001 -0.0099 521 VAL A CA 4004 C C . VAL A 521 ? 0.1583 0.1834 0.1736 0.0049 -0.0006 -0.0097 521 VAL A C 4005 O O . VAL A 521 ? 0.1674 0.1934 0.1845 0.0037 -0.0015 -0.0103 521 VAL A O 4006 C CB . VAL A 521 ? 0.1515 0.1720 0.1677 0.0036 -0.0004 -0.0097 521 VAL A CB 4007 C CG1 . VAL A 521 ? 0.1699 0.1901 0.1852 0.0039 0.0002 -0.0086 521 VAL A CG1 4008 C CG2 . VAL A 521 ? 0.1673 0.1861 0.1837 0.0034 0.0001 -0.0103 521 VAL A CG2 4009 N N . LEU A 522 ? 0.1469 0.1733 0.1603 0.0064 0.0000 -0.0090 522 LEU A N 4010 C CA . LEU A 522 ? 0.1519 0.1817 0.1652 0.0069 -0.0004 -0.0090 522 LEU A CA 4011 C C . LEU A 522 ? 0.1427 0.1717 0.1556 0.0068 -0.0002 -0.0078 522 LEU A C 4012 O O . LEU A 522 ? 0.1600 0.1871 0.1709 0.0078 0.0009 -0.0067 522 LEU A O 4013 C CB . LEU A 522 ? 0.1633 0.1955 0.1745 0.0092 0.0001 -0.0089 522 LEU A CB 4014 C CG . LEU A 522 ? 0.1861 0.2227 0.1969 0.0103 -0.0003 -0.0090 522 LEU A CG 4015 C CD1 . LEU A 522 ? 0.1893 0.2293 0.2030 0.0086 -0.0015 -0.0109 522 LEU A CD1 4016 C CD2 . LEU A 522 ? 0.1948 0.2336 0.2028 0.0132 0.0005 -0.0087 522 LEU A CD2 4017 N N . ILE A 523 ? 0.1466 0.1767 0.1613 0.0054 -0.0009 -0.0082 523 ILE A N 4018 C CA . ILE A 523 ? 0.1485 0.1783 0.1630 0.0052 -0.0008 -0.0072 523 ILE A CA 4019 C C . ILE A 523 ? 0.1615 0.1954 0.1757 0.0061 -0.0010 -0.0074 523 ILE A C 4020 O O . ILE A 523 ? 0.1731 0.2100 0.1889 0.0053 -0.0016 -0.0088 523 ILE A O 4021 C CB . ILE A 523 ? 0.1613 0.1897 0.1778 0.0033 -0.0013 -0.0074 523 ILE A CB 4022 C CG1 . ILE A 523 ? 0.1691 0.1943 0.1860 0.0028 -0.0013 -0.0073 523 ILE A CG1 4023 C CG2 . ILE A 523 ? 0.1683 0.1971 0.1848 0.0031 -0.0013 -0.0065 523 ILE A CG2 4024 C CD1 . ILE A 523 ? 0.1743 0.1974 0.1898 0.0034 -0.0007 -0.0064 523 ILE A CD1 4025 N N . SER A 524 ? 0.1456 0.1797 0.1576 0.0077 -0.0003 -0.0063 524 SER A N 4026 C CA . SER A 524 ? 0.1534 0.1920 0.1648 0.0090 -0.0005 -0.0065 524 SER A CA 4027 C C . SER A 524 ? 0.1629 0.2005 0.1722 0.0103 0.0003 -0.0049 524 SER A C 4028 O O . SER A 524 ? 0.1543 0.1879 0.1623 0.0106 0.0012 -0.0037 524 SER A O 4029 C CB . SER A 524 ? 0.1625 0.2041 0.1725 0.0111 -0.0004 -0.0071 524 SER A CB 4030 O OG . SER A 524 ? 0.1679 0.2066 0.1749 0.0131 0.0008 -0.0057 524 SER A OG 4031 N N . GLY A 525 ? 0.1564 0.1979 0.1655 0.0112 0.0000 -0.0050 525 GLY A N 4032 C CA . GLY A 525 ? 0.1710 0.2121 0.1779 0.0128 0.0007 -0.0035 525 GLY A CA 4033 C C . GLY A 525 ? 0.1830 0.2252 0.1866 0.0162 0.0017 -0.0027 525 GLY A C 4034 O O . GLY A 525 ? 0.1832 0.2251 0.1847 0.0179 0.0025 -0.0015 525 GLY A O 4035 N N . ARG A 526 ? 0.1827 0.2258 0.1856 0.0172 0.0018 -0.0033 526 ARG A N 4036 C CA . ARG A 526 ? 0.1900 0.2355 0.1897 0.0209 0.0025 -0.0027 526 ARG A CA 4037 C C . ARG A 526 ? 0.1879 0.2340 0.1875 0.0213 0.0024 -0.0036 526 ARG A C 4038 O O . ARG A 526 ? 0.1903 0.2361 0.1927 0.0188 0.0015 -0.0049 526 ARG A O 4039 C CB . ARG A 526 ? 0.1929 0.2453 0.1930 0.0220 0.0015 -0.0038 526 ARG A CB 4040 C CG . ARG A 526 ? 0.1908 0.2474 0.1950 0.0192 -0.0002 -0.0063 526 ARG A CG 4041 C CD . ARG A 526 ? 0.2184 0.2824 0.2231 0.0204 -0.0010 -0.0077 526 ARG A CD 4042 N NE . ARG A 526 ? 0.2413 0.3081 0.2503 0.0169 -0.0020 -0.0101 526 ARG A NE 4043 C CZ . ARG A 526 ? 0.2090 0.2805 0.2198 0.0160 -0.0025 -0.0114 526 ARG A CZ 4044 N NH1 . ARG A 526 ? 0.2232 0.2981 0.2322 0.0185 -0.0024 -0.0108 526 ARG A NH1 4045 N NH2 . ARG A 526 ? 0.2387 0.3115 0.2533 0.0127 -0.0030 -0.0135 526 ARG A NH2 4046 N N . PRO A 527 ? 0.1929 0.2400 0.1891 0.0249 0.0035 -0.0027 527 PRO A N 4047 C CA . PRO A 527 ? 0.2002 0.2497 0.1963 0.0257 0.0031 -0.0039 527 PRO A CA 4048 C C . PRO A 527 ? 0.1974 0.2540 0.1967 0.0246 0.0011 -0.0065 527 PRO A C 4049 O O . PRO A 527 ? 0.1980 0.2594 0.1980 0.0250 0.0003 -0.0072 527 PRO A O 4050 C CB . PRO A 527 ? 0.2198 0.2701 0.2113 0.0304 0.0046 -0.0023 527 PRO A CB 4051 C CG . PRO A 527 ? 0.2514 0.3024 0.2412 0.0320 0.0051 -0.0011 527 PRO A CG 4052 C CD . PRO A 527 ? 0.2047 0.2510 0.1968 0.0285 0.0051 -0.0007 527 PRO A CD 4053 N N . VAL A 528 ? 0.1922 0.2493 0.1937 0.0228 0.0003 -0.0081 528 VAL A N 4054 C CA . VAL A 528 ? 0.1947 0.2578 0.1995 0.0213 -0.0013 -0.0110 528 VAL A CA 4055 C C . VAL A 528 ? 0.1887 0.2540 0.1926 0.0229 -0.0014 -0.0119 528 VAL A C 4056 O O . VAL A 528 ? 0.1997 0.2606 0.2010 0.0244 -0.0002 -0.0102 528 VAL A O 4057 C CB . VAL A 528 ? 0.1913 0.2520 0.2002 0.0169 -0.0020 -0.0122 528 VAL A CB 4058 C CG1 . VAL A 528 ? 0.2015 0.2613 0.2113 0.0155 -0.0020 -0.0115 528 VAL A CG1 4059 C CG2 . VAL A 528 ? 0.1849 0.2389 0.1938 0.0155 -0.0015 -0.0112 528 VAL A CG2 4060 N N . VAL A 529 ? 0.1947 0.2669 0.2007 0.0227 -0.0026 -0.0148 529 VAL A N 4061 C CA . VAL A 529 ? 0.1950 0.2699 0.2003 0.0244 -0.0028 -0.0159 529 VAL A CA 4062 C C . VAL A 529 ? 0.1989 0.2673 0.2051 0.0221 -0.0024 -0.0153 529 VAL A C 4063 O O . VAL A 529 ? 0.2079 0.2740 0.2174 0.0185 -0.0030 -0.0164 529 VAL A O 4064 C CB . VAL A 529 ? 0.2136 0.2967 0.2221 0.0234 -0.0043 -0.0197 529 VAL A CB 4065 C CG1 . VAL A 529 ? 0.2195 0.3050 0.2278 0.0245 -0.0045 -0.0211 529 VAL A CG1 4066 C CG2 . VAL A 529 ? 0.2214 0.3120 0.2286 0.0263 -0.0046 -0.0204 529 VAL A CG2 4067 N N . VAL A 530 ? 0.1956 0.2608 0.1985 0.0245 -0.0013 -0.0136 530 VAL A N 4068 C CA . VAL A 530 ? 0.1892 0.2478 0.1928 0.0224 -0.0006 -0.0128 530 VAL A CA 4069 C C . VAL A 530 ? 0.1965 0.2556 0.1992 0.0236 -0.0005 -0.0134 530 VAL A C 4070 O O . VAL A 530 ? 0.1966 0.2513 0.2005 0.0216 -0.0003 -0.0134 530 VAL A O 4071 C CB . VAL A 530 ? 0.2077 0.2594 0.2087 0.0230 0.0011 -0.0099 530 VAL A CB 4072 C CG1 . VAL A 530 ? 0.2103 0.2607 0.2066 0.0269 0.0030 -0.0079 530 VAL A CG1 4073 C CG2 . VAL A 530 ? 0.2165 0.2621 0.2194 0.0198 0.0013 -0.0096 530 VAL A CG2 4074 N N . GLN A 531 ? 0.1971 0.2618 0.1979 0.0268 -0.0006 -0.0141 531 GLN A N 4075 C CA . GLN A 531 ? 0.2029 0.2681 0.2028 0.0280 -0.0004 -0.0146 531 GLN A CA 4076 C C . GLN A 531 ? 0.1928 0.2581 0.1969 0.0244 -0.0017 -0.0171 531 GLN A C 4077 O O . GLN A 531 ? 0.2002 0.2616 0.2040 0.0239 -0.0011 -0.0167 531 GLN A O 4078 C CB . GLN A 531 ? 0.2068 0.2791 0.2040 0.0323 -0.0005 -0.0153 531 GLN A CB 4079 C CG . GLN A 531 ? 0.2286 0.3000 0.2206 0.0367 0.0013 -0.0123 531 GLN A CG 4080 C CD . GLN A 531 ? 0.2351 0.3112 0.2270 0.0379 0.0006 -0.0126 531 GLN A CD 4081 O OE1 . GLN A 531 ? 0.2440 0.3207 0.2396 0.0344 -0.0006 -0.0140 531 GLN A OE1 4082 N NE2 . GLN A 531 ? 0.2540 0.3334 0.2414 0.0429 0.0015 -0.0113 531 GLN A NE2 4083 N N . PRO A 532 ? 0.1963 0.2657 0.2042 0.0219 -0.0032 -0.0198 532 PRO A N 4084 C CA . PRO A 532 ? 0.1991 0.2677 0.2108 0.0186 -0.0040 -0.0220 532 PRO A CA 4085 C C . PRO A 532 ? 0.1943 0.2550 0.2070 0.0159 -0.0035 -0.0206 532 PRO A C 4086 O O . PRO A 532 ? 0.1926 0.2509 0.2062 0.0149 -0.0036 -0.0211 532 PRO A O 4087 C CB . PRO A 532 ? 0.2222 0.2962 0.2375 0.0166 -0.0052 -0.0250 532 PRO A CB 4088 C CG . PRO A 532 ? 0.2113 0.2919 0.2245 0.0198 -0.0053 -0.0251 532 PRO A CG 4089 C CD . PRO A 532 ? 0.1928 0.2688 0.2018 0.0224 -0.0040 -0.0214 532 PRO A CD 4090 N N . LEU A 533 ? 0.1934 0.2506 0.2059 0.0151 -0.0031 -0.0188 533 LEU A N 4091 C CA . LEU A 533 ? 0.1847 0.2351 0.1978 0.0130 -0.0026 -0.0175 533 LEU A CA 4092 C C . LEU A 533 ? 0.1955 0.2422 0.2060 0.0145 -0.0014 -0.0159 533 LEU A C 4093 O O . LEU A 533 ? 0.1998 0.2430 0.2114 0.0130 -0.0013 -0.0160 533 LEU A O 4094 C CB . LEU A 533 ? 0.1896 0.2376 0.2023 0.0124 -0.0022 -0.0158 533 LEU A CB 4095 C CG . LEU A 533 ? 0.2027 0.2527 0.2184 0.0102 -0.0031 -0.0172 533 LEU A CG 4096 C CD1 . LEU A 533 ? 0.2118 0.2609 0.2265 0.0105 -0.0027 -0.0155 533 LEU A CD1 4097 C CD2 . LEU A 533 ? 0.2089 0.2557 0.2276 0.0071 -0.0035 -0.0181 533 LEU A CD2 4098 N N . LEU A 534 ? 0.1993 0.2466 0.2062 0.0177 -0.0002 -0.0143 534 LEU A N 4099 C CA . LEU A 534 ? 0.2077 0.2510 0.2120 0.0190 0.0015 -0.0128 534 LEU A CA 4100 C C . LEU A 534 ? 0.2121 0.2569 0.2170 0.0191 0.0010 -0.0143 534 LEU A C 4101 O O . LEU A 534 ? 0.2232 0.2639 0.2283 0.0181 0.0017 -0.0140 534 LEU A O 4102 C CB . LEU A 534 ? 0.2191 0.2627 0.2190 0.0228 0.0032 -0.0108 534 LEU A CB 4103 C CG . LEU A 534 ? 0.2198 0.2602 0.2182 0.0230 0.0043 -0.0089 534 LEU A CG 4104 C CD1 . LEU A 534 ? 0.2433 0.2856 0.2375 0.0272 0.0056 -0.0073 534 LEU A CD1 4105 C CD2 . LEU A 534 ? 0.2323 0.2660 0.2306 0.0214 0.0059 -0.0077 534 LEU A CD2 4106 N N . ALA A 535 ? 0.2018 0.2526 0.2072 0.0203 -0.0001 -0.0160 535 ALA A N 4107 C CA . ALA A 535 ? 0.2126 0.2654 0.2186 0.0205 -0.0005 -0.0176 535 ALA A CA 4108 C C . ALA A 535 ? 0.2069 0.2569 0.2163 0.0171 -0.0013 -0.0189 535 ALA A C 4109 O O . ALA A 535 ? 0.2314 0.2799 0.2406 0.0172 -0.0009 -0.0192 535 ALA A O 4110 C CB . ALA A 535 ? 0.2090 0.2695 0.2155 0.0220 -0.0018 -0.0198 535 ALA A CB 4111 N N . ALA A 536 ? 0.1973 0.2463 0.2097 0.0144 -0.0022 -0.0197 536 ALA A N 4112 C CA . ALA A 536 ? 0.1869 0.2331 0.2022 0.0116 -0.0028 -0.0208 536 ALA A CA 4113 C C . ALA A 536 ? 0.1931 0.2332 0.2077 0.0107 -0.0019 -0.0191 536 ALA A C 4114 O O . ALA A 536 ? 0.2111 0.2492 0.2274 0.0093 -0.0022 -0.0199 536 ALA A O 4115 C CB . ALA A 536 ? 0.2124 0.2594 0.2308 0.0091 -0.0038 -0.0221 536 ALA A CB 4116 N N . SER A 537 ? 0.1983 0.2360 0.2109 0.0116 -0.0008 -0.0170 537 SER A N 4117 C CA . SER A 537 ? 0.1880 0.2207 0.2008 0.0103 -0.0001 -0.0159 537 SER A CA 4118 C C . SER A 537 ? 0.1917 0.2217 0.2026 0.0112 0.0016 -0.0150 537 SER A C 4119 O O . SER A 537 ? 0.2142 0.2448 0.2223 0.0135 0.0028 -0.0141 537 SER A O 4120 C CB . SER A 537 ? 0.2034 0.2350 0.2154 0.0103 0.0004 -0.0145 537 SER A CB 4121 O OG . SER A 537 ? 0.2118 0.2459 0.2257 0.0092 -0.0009 -0.0152 537 SER A OG 4122 N N . ASP A 538 ? 0.1747 0.2015 0.1868 0.0096 0.0018 -0.0153 538 ASP A N 4123 C CA . ASP A 538 ? 0.1780 0.2019 0.1885 0.0101 0.0038 -0.0146 538 ASP A CA 4124 C C . ASP A 538 ? 0.1840 0.2053 0.1927 0.0105 0.0055 -0.0130 538 ASP A C 4125 O O . ASP A 538 ? 0.2107 0.2303 0.2167 0.0120 0.0076 -0.0119 538 ASP A O 4126 C CB . ASP A 538 ? 0.1811 0.2032 0.1937 0.0082 0.0034 -0.0158 538 ASP A CB 4127 C CG . ASP A 538 ? 0.2043 0.2286 0.2185 0.0079 0.0020 -0.0173 538 ASP A CG 4128 O OD1 . ASP A 538 ? 0.1974 0.2229 0.2137 0.0069 0.0003 -0.0182 538 ASP A OD1 4129 O OD2 . ASP A 538 ? 0.2099 0.2347 0.2231 0.0089 0.0027 -0.0176 538 ASP A OD2 4130 N N . ALA A 539 ? 0.1674 0.1881 0.1774 0.0092 0.0047 -0.0129 539 ALA A N 4131 C CA . ALA A 539 ? 0.1640 0.1827 0.1726 0.0095 0.0060 -0.0115 539 ALA A CA 4132 C C . ALA A 539 ? 0.1751 0.1959 0.1842 0.0095 0.0046 -0.0111 539 ALA A C 4133 O O . ALA A 539 ? 0.1695 0.1921 0.1808 0.0084 0.0028 -0.0121 539 ALA A O 4134 C CB . ALA A 539 ? 0.1780 0.1939 0.1880 0.0077 0.0067 -0.0120 539 ALA A CB 4135 N N . LEU A 540 ? 0.1566 0.1767 0.1636 0.0108 0.0058 -0.0097 540 LEU A N 4136 C CA . LEU A 540 ? 0.1599 0.1821 0.1673 0.0108 0.0046 -0.0093 540 LEU A CA 4137 C C . LEU A 540 ? 0.1668 0.1864 0.1727 0.0111 0.0061 -0.0080 540 LEU A C 4138 O O . LEU A 540 ? 0.1757 0.1931 0.1790 0.0126 0.0084 -0.0069 540 LEU A O 4139 C CB . LEU A 540 ? 0.1736 0.1998 0.1798 0.0128 0.0040 -0.0093 540 LEU A CB 4140 C CG . LEU A 540 ? 0.1712 0.2003 0.1785 0.0124 0.0026 -0.0094 540 LEU A CG 4141 C CD1 . LEU A 540 ? 0.2023 0.2366 0.2107 0.0129 0.0012 -0.0109 540 LEU A CD1 4142 C CD2 . LEU A 540 ? 0.1978 0.2264 0.2025 0.0142 0.0039 -0.0078 540 LEU A CD2 4143 N N . VAL A 541 ? 0.1579 0.1776 0.1654 0.0097 0.0051 -0.0080 541 VAL A N 4144 C CA . VAL A 541 ? 0.1590 0.1766 0.1656 0.0097 0.0062 -0.0070 541 VAL A CA 4145 C C . VAL A 541 ? 0.1594 0.1795 0.1659 0.0103 0.0051 -0.0064 541 VAL A C 4146 O O . VAL A 541 ? 0.1725 0.1949 0.1812 0.0091 0.0033 -0.0072 541 VAL A O 4147 C CB . VAL A 541 ? 0.1574 0.1734 0.1662 0.0075 0.0057 -0.0079 541 VAL A CB 4148 C CG1 . VAL A 541 ? 0.1670 0.1815 0.1754 0.0073 0.0066 -0.0072 541 VAL A CG1 4149 C CG2 . VAL A 541 ? 0.1734 0.1876 0.1828 0.0068 0.0068 -0.0089 541 VAL A CG2 4150 N N . ALA A 542 ? 0.1587 0.1782 0.1627 0.0120 0.0065 -0.0051 542 ALA A N 4151 C CA . ALA A 542 ? 0.1600 0.1818 0.1640 0.0124 0.0057 -0.0045 542 ALA A CA 4152 C C . ALA A 542 ? 0.1563 0.1756 0.1612 0.0108 0.0059 -0.0043 542 ALA A C 4153 O O . ALA A 542 ? 0.1646 0.1809 0.1681 0.0111 0.0078 -0.0037 542 ALA A O 4154 C CB . ALA A 542 ? 0.1678 0.1902 0.1685 0.0153 0.0071 -0.0032 542 ALA A CB 4155 N N . ALA A 543 ? 0.1533 0.1741 0.1608 0.0091 0.0041 -0.0050 543 ALA A N 4156 C CA . ALA A 543 ? 0.1483 0.1675 0.1568 0.0078 0.0041 -0.0049 543 ALA A CA 4157 C C . ALA A 543 ? 0.1502 0.1707 0.1583 0.0082 0.0038 -0.0040 543 ALA A C 4158 O O . ALA A 543 ? 0.1487 0.1682 0.1574 0.0073 0.0037 -0.0039 543 ALA A O 4159 C CB . ALA A 543 ? 0.1444 0.1637 0.1555 0.0060 0.0027 -0.0059 543 ALA A CB 4160 N N . TRP A 544 ? 0.1464 0.1694 0.1534 0.0095 0.0036 -0.0036 544 TRP A N 4161 C CA . TRP A 544 ? 0.1442 0.1691 0.1508 0.0100 0.0033 -0.0029 544 TRP A CA 4162 C C . TRP A 544 ? 0.1389 0.1645 0.1480 0.0081 0.0019 -0.0033 544 TRP A C 4163 O O . TRP A 544 ? 0.1433 0.1698 0.1543 0.0069 0.0009 -0.0042 544 TRP A O 4164 C CB . TRP A 544 ? 0.1588 0.1813 0.1632 0.0112 0.0049 -0.0017 544 TRP A CB 4165 C CG . TRP A 544 ? 0.1625 0.1830 0.1643 0.0131 0.0068 -0.0012 544 TRP A CG 4166 C CD1 . TRP A 544 ? 0.1734 0.1901 0.1746 0.0127 0.0085 -0.0013 544 TRP A CD1 4167 C CD2 . TRP A 544 ? 0.1760 0.1985 0.1755 0.0156 0.0073 -0.0006 544 TRP A CD2 4168 N NE1 . TRP A 544 ? 0.1825 0.1978 0.1809 0.0148 0.0104 -0.0005 544 TRP A NE1 4169 C CE2 . TRP A 544 ? 0.1779 0.1968 0.1751 0.0168 0.0095 0.0000 544 TRP A CE2 4170 C CE3 . TRP A 544 ? 0.1764 0.2035 0.1756 0.0170 0.0061 -0.0007 544 TRP A CE3 4171 C CZ2 . TRP A 544 ? 0.1916 0.2112 0.1857 0.0198 0.0107 0.0008 544 TRP A CZ2 4172 C CZ3 . TRP A 544 ? 0.1985 0.2271 0.1949 0.0200 0.0070 -0.0002 544 TRP A CZ3 4173 C CH2 . TRP A 544 ? 0.1936 0.2183 0.1874 0.0215 0.0093 0.0008 544 TRP A CH2 4174 N N . LEU A 545 ? 0.1365 0.1616 0.1455 0.0078 0.0021 -0.0026 545 LEU A N 4175 C CA . LEU A 545 ? 0.1410 0.1665 0.1519 0.0063 0.0011 -0.0027 545 LEU A CA 4176 C C . LEU A 545 ? 0.1398 0.1627 0.1507 0.0058 0.0015 -0.0025 545 LEU A C 4177 O O . LEU A 545 ? 0.1410 0.1635 0.1510 0.0062 0.0020 -0.0018 545 LEU A O 4178 C CB . LEU A 545 ? 0.1372 0.1654 0.1481 0.0065 0.0007 -0.0022 545 LEU A CB 4179 C CG . LEU A 545 ? 0.1488 0.1806 0.1600 0.0070 0.0003 -0.0030 545 LEU A CG 4180 C CD1 . LEU A 545 ? 0.1558 0.1906 0.1667 0.0075 0.0002 -0.0027 545 LEU A CD1 4181 C CD2 . LEU A 545 ? 0.1678 0.2003 0.1813 0.0053 -0.0005 -0.0042 545 LEU A CD2 4182 N N . PRO A 546 ? 0.1348 0.1561 0.1466 0.0050 0.0014 -0.0032 546 PRO A N 4183 C CA . PRO A 546 ? 0.1402 0.1597 0.1518 0.0048 0.0021 -0.0036 546 PRO A CA 4184 C C . PRO A 546 ? 0.1348 0.1545 0.1471 0.0044 0.0016 -0.0034 546 PRO A C 4185 O O . PRO A 546 ? 0.1413 0.1603 0.1534 0.0043 0.0022 -0.0039 546 PRO A O 4186 C CB . PRO A 546 ? 0.1476 0.1661 0.1600 0.0044 0.0021 -0.0046 546 PRO A CB 4187 C CG . PRO A 546 ? 0.1412 0.1609 0.1547 0.0040 0.0008 -0.0047 546 PRO A CG 4188 C CD . PRO A 546 ? 0.1368 0.1582 0.1496 0.0045 0.0008 -0.0041 546 PRO A CD 4189 N N . GLY A 547 ? 0.1393 0.1602 0.1523 0.0041 0.0006 -0.0028 547 GLY A N 4190 C CA . GLY A 547 ? 0.1307 0.1519 0.1440 0.0040 0.0002 -0.0023 547 GLY A CA 4191 C C . GLY A 547 ? 0.1235 0.1443 0.1377 0.0037 -0.0004 -0.0027 547 GLY A C 4192 O O . GLY A 547 ? 0.1492 0.1694 0.1641 0.0034 -0.0008 -0.0031 547 GLY A O 4193 N N . SER A 548 ? 0.1348 0.1560 0.1489 0.0041 -0.0006 -0.0025 548 SER A N 4194 C CA . SER A 548 ? 0.1403 0.1614 0.1549 0.0044 -0.0012 -0.0026 548 SER A CA 4195 C C . SER A 548 ? 0.1393 0.1605 0.1544 0.0046 -0.0013 -0.0040 548 SER A C 4196 O O . SER A 548 ? 0.1470 0.1680 0.1624 0.0051 -0.0018 -0.0041 548 SER A O 4197 C CB . SER A 548 ? 0.1469 0.1689 0.1609 0.0052 -0.0013 -0.0019 548 SER A CB 4198 O OG . SER A 548 ? 0.1388 0.1620 0.1526 0.0054 -0.0010 -0.0027 548 SER A OG 4199 N N . GLU A 549 ? 0.1313 0.1525 0.1465 0.0042 -0.0007 -0.0052 549 GLU A N 4200 C CA . GLU A 549 ? 0.1431 0.1648 0.1589 0.0042 -0.0006 -0.0069 549 GLU A CA 4201 C C . GLU A 549 ? 0.1433 0.1640 0.1596 0.0037 -0.0004 -0.0075 549 GLU A C 4202 O O . GLU A 549 ? 0.1572 0.1771 0.1732 0.0032 0.0007 -0.0083 549 GLU A O 4203 C CB . GLU A 549 ? 0.1440 0.1666 0.1599 0.0040 0.0004 -0.0082 549 GLU A CB 4204 C CG . GLU A 549 ? 0.1536 0.1777 0.1690 0.0046 0.0001 -0.0077 549 GLU A CG 4205 C CD . GLU A 549 ? 0.1639 0.1895 0.1794 0.0057 -0.0011 -0.0073 549 GLU A CD 4206 O OE1 . GLU A 549 ? 0.1712 0.1980 0.1874 0.0062 -0.0016 -0.0085 549 GLU A OE1 4207 O OE2 . GLU A 549 ? 0.1657 0.1913 0.1805 0.0063 -0.0015 -0.0056 549 GLU A OE2 4208 N N . GLY A 550 ? 0.1346 0.1549 0.1512 0.0039 -0.0012 -0.0071 550 GLY A N 4209 C CA . GLY A 550 ? 0.1448 0.1641 0.1618 0.0035 -0.0011 -0.0077 550 GLY A CA 4210 C C . GLY A 550 ? 0.1451 0.1649 0.1627 0.0033 -0.0007 -0.0095 550 GLY A C 4211 O O . GLY A 550 ? 0.1518 0.1708 0.1696 0.0029 -0.0003 -0.0100 550 GLY A O 4212 N N . GLN A 551 ? 0.1432 0.1646 0.1612 0.0036 -0.0007 -0.0106 551 GLN A N 4213 C CA . GLN A 551 ? 0.1523 0.1746 0.1712 0.0031 -0.0001 -0.0127 551 GLN A CA 4214 C C . GLN A 551 ? 0.1623 0.1832 0.1809 0.0022 0.0016 -0.0132 551 GLN A C 4215 O O . GLN A 551 ? 0.1585 0.1793 0.1777 0.0015 0.0025 -0.0148 551 GLN A O 4216 C CB . GLN A 551 ? 0.1570 0.1822 0.1767 0.0036 -0.0005 -0.0143 551 GLN A CB 4217 C CG . GLN A 551 ? 0.1716 0.1979 0.1912 0.0050 -0.0019 -0.0137 551 GLN A CG 4218 C CD . GLN A 551 ? 0.1804 0.2101 0.2002 0.0062 -0.0025 -0.0149 551 GLN A CD 4219 O OE1 . GLN A 551 ? 0.2447 0.2771 0.2654 0.0068 -0.0029 -0.0169 551 GLN A OE1 4220 N NE2 . GLN A 551 ? 0.1750 0.2054 0.1941 0.0067 -0.0025 -0.0140 551 GLN A NE2 4221 N N . GLY A 552 ? 0.1569 0.1766 0.1744 0.0021 0.0023 -0.0119 552 GLY A N 4222 C CA . GLY A 552 ? 0.1634 0.1810 0.1800 0.0017 0.0042 -0.0121 552 GLY A CA 4223 C C . GLY A 552 ? 0.1643 0.1807 0.1806 0.0017 0.0044 -0.0117 552 GLY A C 4224 O O . GLY A 552 ? 0.1828 0.1977 0.1986 0.0014 0.0062 -0.0124 552 GLY A O 4225 N N . VAL A 553 ? 0.1567 0.1735 0.1730 0.0022 0.0029 -0.0108 553 VAL A N 4226 C CA . VAL A 553 ? 0.1452 0.1613 0.1613 0.0023 0.0029 -0.0107 553 VAL A CA 4227 C C . VAL A 553 ? 0.1468 0.1632 0.1641 0.0018 0.0030 -0.0124 553 VAL A C 4228 O O . VAL A 553 ? 0.1604 0.1757 0.1773 0.0016 0.0043 -0.0129 553 VAL A O 4229 C CB . VAL A 553 ? 0.1499 0.1667 0.1662 0.0026 0.0014 -0.0096 553 VAL A CB 4230 C CG1 . VAL A 553 ? 0.1681 0.1847 0.1844 0.0027 0.0012 -0.0099 553 VAL A CG1 4231 C CG2 . VAL A 553 ? 0.1605 0.1775 0.1758 0.0030 0.0014 -0.0082 553 VAL A CG2 4232 N N . THR A 554 ? 0.1448 0.1627 0.1633 0.0018 0.0018 -0.0131 554 THR A N 4233 C CA . THR A 554 ? 0.1498 0.1685 0.1694 0.0015 0.0018 -0.0149 554 THR A CA 4234 C C . THR A 554 ? 0.1585 0.1775 0.1786 0.0006 0.0035 -0.0168 554 THR A C 4235 O O . THR A 554 ? 0.1817 0.2009 0.2026 0.0002 0.0041 -0.0182 554 THR A O 4236 C CB . THR A 554 ? 0.1490 0.1694 0.1695 0.0022 0.0001 -0.0152 554 THR A CB 4237 O OG1 . THR A 554 ? 0.1524 0.1742 0.1729 0.0026 -0.0002 -0.0150 554 THR A OG1 4238 C CG2 . THR A 554 ? 0.1660 0.1854 0.1862 0.0027 -0.0010 -0.0137 554 THR A CG2 4239 N N . ASP A 555 ? 0.1584 0.1774 0.1783 0.0003 0.0044 -0.0169 555 ASP A N 4240 C CA . ASP A 555 ? 0.1566 0.1755 0.1772 -0.0008 0.0066 -0.0190 555 ASP A CA 4241 C C . ASP A 555 ? 0.1687 0.1847 0.1883 -0.0012 0.0087 -0.0189 555 ASP A C 4242 O O . ASP A 555 ? 0.1940 0.2100 0.2146 -0.0023 0.0103 -0.0209 555 ASP A O 4243 C CB . ASP A 555 ? 0.1555 0.1742 0.1757 -0.0010 0.0075 -0.0189 555 ASP A CB 4244 C CG . ASP A 555 ? 0.1735 0.1957 0.1949 -0.0007 0.0061 -0.0199 555 ASP A CG 4245 O OD1 . ASP A 555 ? 0.1857 0.2105 0.2081 -0.0003 0.0046 -0.0209 555 ASP A OD1 4246 O OD2 . ASP A 555 ? 0.1933 0.2155 0.2142 -0.0007 0.0065 -0.0196 555 ASP A OD2 4247 N N . ALA A 556 ? 0.1528 0.1668 0.1706 -0.0004 0.0087 -0.0167 556 ALA A N 4248 C CA . ALA A 556 ? 0.1542 0.1658 0.1708 -0.0003 0.0106 -0.0163 556 ALA A CA 4249 C C . ALA A 556 ? 0.1561 0.1683 0.1731 0.0000 0.0094 -0.0164 556 ALA A C 4250 O O . ALA A 556 ? 0.1731 0.1843 0.1900 -0.0004 0.0110 -0.0173 556 ALA A O 4251 C CB . ALA A 556 ? 0.1753 0.1848 0.1894 0.0009 0.0114 -0.0140 556 ALA A CB 4252 N N . LEU A 557 ? 0.1499 0.1638 0.1674 0.0006 0.0069 -0.0156 557 LEU A N 4253 C CA . LEU A 557 ? 0.1533 0.1678 0.1713 0.0009 0.0059 -0.0159 557 LEU A CA 4254 C C . LEU A 557 ? 0.1636 0.1791 0.1832 0.0000 0.0062 -0.0181 557 LEU A C 4255 O O . LEU A 557 ? 0.1740 0.1891 0.1936 0.0000 0.0067 -0.0186 557 LEU A O 4256 C CB . LEU A 557 ? 0.1669 0.1826 0.1854 0.0014 0.0035 -0.0151 557 LEU A CB 4257 C CG . LEU A 557 ? 0.1672 0.1827 0.1845 0.0021 0.0030 -0.0133 557 LEU A CG 4258 C CD1 . LEU A 557 ? 0.1704 0.1869 0.1887 0.0021 0.0010 -0.0130 557 LEU A CD1 4259 C CD2 . LEU A 557 ? 0.1745 0.1894 0.1905 0.0027 0.0038 -0.0127 557 LEU A CD2 4260 N N . PHE A 558 ? 0.1572 0.1744 0.1782 -0.0005 0.0059 -0.0196 558 PHE A N 4261 C CA . PHE A 558 ? 0.1655 0.1847 0.1882 -0.0011 0.0060 -0.0220 558 PHE A CA 4262 C C . PHE A 558 ? 0.1719 0.1907 0.1952 -0.0025 0.0087 -0.0240 558 PHE A C 4263 O O . PHE A 558 ? 0.1853 0.2064 0.2104 -0.0033 0.0090 -0.0265 558 PHE A O 4264 C CB . PHE A 558 ? 0.1649 0.1872 0.1889 -0.0005 0.0039 -0.0227 558 PHE A CB 4265 C CG . PHE A 558 ? 0.1645 0.1867 0.1881 0.0007 0.0018 -0.0211 558 PHE A CG 4266 C CD1 . PHE A 558 ? 0.1716 0.1938 0.1956 0.0010 0.0011 -0.0215 558 PHE A CD1 4267 C CD2 . PHE A 558 ? 0.1880 0.2098 0.2108 0.0014 0.0006 -0.0193 558 PHE A CD2 4268 C CE1 . PHE A 558 ? 0.1828 0.2045 0.2064 0.0019 -0.0005 -0.0202 558 PHE A CE1 4269 C CE2 . PHE A 558 ? 0.2021 0.2234 0.2246 0.0023 -0.0008 -0.0180 558 PHE A CE2 4270 C CZ . PHE A 558 ? 0.1902 0.2112 0.2131 0.0025 -0.0013 -0.0185 558 PHE A CZ 4271 N N . GLY A 559 ? 0.1778 0.1937 0.1996 -0.0028 0.0108 -0.0229 559 GLY A N 4272 C CA . GLY A 559 ? 0.1890 0.2034 0.2111 -0.0043 0.0141 -0.0247 559 GLY A CA 4273 C C . GLY A 559 ? 0.1856 0.2019 0.2094 -0.0055 0.0149 -0.0271 559 GLY A C 4274 O O . GLY A 559 ? 0.2083 0.2240 0.2331 -0.0071 0.0178 -0.0294 559 GLY A O 4275 N N . ASP A 560 ? 0.1872 0.2059 0.2115 -0.0049 0.0129 -0.0268 560 ASP A N 4276 C CA . ASP A 560 ? 0.1890 0.2096 0.2147 -0.0060 0.0139 -0.0291 560 ASP A CA 4277 C C . ASP A 560 ? 0.2038 0.2204 0.2281 -0.0068 0.0171 -0.0286 560 ASP A C 4278 O O . ASP A 560 ? 0.2327 0.2497 0.2584 -0.0085 0.0195 -0.0313 560 ASP A O 4279 C CB . ASP A 560 ? 0.2352 0.2590 0.2612 -0.0049 0.0112 -0.0286 560 ASP A CB 4280 C CG . ASP A 560 ? 0.2628 0.2907 0.2901 -0.0039 0.0087 -0.0297 560 ASP A CG 4281 O OD1 . ASP A 560 ? 0.3082 0.3377 0.3369 -0.0046 0.0091 -0.0317 560 ASP A OD1 4282 O OD2 . ASP A 560 ? 0.3782 0.4078 0.4051 -0.0025 0.0064 -0.0284 560 ASP A OD2 4283 N N . PHE A 561 ? 0.2017 0.2148 0.2235 -0.0056 0.0172 -0.0254 561 PHE A N 4284 C CA . PHE A 561 ? 0.2100 0.2187 0.2297 -0.0057 0.0203 -0.0243 561 PHE A CA 4285 C C . PHE A 561 ? 0.2187 0.2240 0.2360 -0.0044 0.0211 -0.0219 561 PHE A C 4286 O O . PHE A 561 ? 0.2098 0.2164 0.2267 -0.0033 0.0186 -0.0205 561 PHE A O 4287 C CB . PHE A 561 ? 0.2137 0.2222 0.2324 -0.0048 0.0195 -0.0227 561 PHE A CB 4288 C CG . PHE A 561 ? 0.2186 0.2305 0.2394 -0.0058 0.0188 -0.0249 561 PHE A CG 4289 C CD1 . PHE A 561 ? 0.2313 0.2476 0.2534 -0.0051 0.0154 -0.0252 561 PHE A CD1 4290 C CD2 . PHE A 561 ? 0.2390 0.2498 0.2604 -0.0073 0.0217 -0.0270 561 PHE A CD2 4291 C CE1 . PHE A 561 ? 0.2526 0.2727 0.2765 -0.0056 0.0147 -0.0273 561 PHE A CE1 4292 C CE2 . PHE A 561 ? 0.2628 0.2777 0.2864 -0.0080 0.0209 -0.0294 561 PHE A CE2 4293 C CZ . PHE A 561 ? 0.2461 0.2658 0.2708 -0.0070 0.0172 -0.0295 561 PHE A CZ 4294 N N . GLY A 562 ? 0.2357 0.2367 0.2511 -0.0045 0.0247 -0.0214 562 GLY A N 4295 C CA . GLY A 562 ? 0.2431 0.2410 0.2556 -0.0028 0.0256 -0.0189 562 GLY A CA 4296 C C . GLY A 562 ? 0.2278 0.2253 0.2379 -0.0006 0.0242 -0.0159 562 GLY A C 4297 O O . GLY A 562 ? 0.2626 0.2605 0.2727 -0.0006 0.0238 -0.0156 562 GLY A O 4298 N N . PHE A 563 ? 0.2329 0.2298 0.2409 0.0012 0.0236 -0.0138 563 PHE A N 4299 C CA . PHE A 563 ? 0.2104 0.2070 0.2158 0.0035 0.0229 -0.0111 563 PHE A CA 4300 C C . PHE A 563 ? 0.2348 0.2268 0.2372 0.0045 0.0267 -0.0100 563 PHE A C 4301 O O . PHE A 563 ? 0.2544 0.2428 0.2554 0.0046 0.0300 -0.0101 563 PHE A O 4302 C CB . PHE A 563 ? 0.2053 0.2032 0.2093 0.0053 0.0213 -0.0096 563 PHE A CB 4303 C CG . PHE A 563 ? 0.1959 0.1980 0.2024 0.0048 0.0175 -0.0102 563 PHE A CG 4304 C CD1 . PHE A 563 ? 0.2014 0.2048 0.2100 0.0035 0.0165 -0.0119 563 PHE A CD1 4305 C CD2 . PHE A 563 ? 0.1769 0.1814 0.1834 0.0055 0.0150 -0.0091 563 PHE A CD2 4306 C CE1 . PHE A 563 ? 0.1900 0.1967 0.2005 0.0033 0.0133 -0.0123 563 PHE A CE1 4307 C CE2 . PHE A 563 ? 0.1883 0.1959 0.1969 0.0050 0.0120 -0.0096 563 PHE A CE2 4308 C CZ . PHE A 563 ? 0.1922 0.2007 0.2026 0.0039 0.0111 -0.0111 563 PHE A CZ 4309 N N . THR A 564 ? 0.2151 0.2070 0.2167 0.0052 0.0266 -0.0089 564 THR A N 4310 C CA . THR A 564 ? 0.2258 0.2131 0.2242 0.0065 0.0303 -0.0076 564 THR A CA 4311 C C . THR A 564 ? 0.2248 0.2126 0.2204 0.0093 0.0293 -0.0050 564 THR A C 4312 O O . THR A 564 ? 0.2436 0.2277 0.2360 0.0111 0.0323 -0.0035 564 THR A O 4313 C CB . THR A 564 ? 0.2349 0.2204 0.2348 0.0043 0.0323 -0.0096 564 THR A CB 4314 O OG1 . THR A 564 ? 0.2584 0.2479 0.2607 0.0034 0.0291 -0.0103 564 THR A OG1 4315 C CG2 . THR A 564 ? 0.2653 0.2498 0.2676 0.0017 0.0344 -0.0124 564 THR A CG2 4316 N N . GLY A 565 ? 0.1972 0.1896 0.1940 0.0097 0.0254 -0.0046 565 GLY A N 4317 C CA . GLY A 565 ? 0.2003 0.1941 0.1950 0.0121 0.0244 -0.0025 565 GLY A CA 4318 C C . GLY A 565 ? 0.2040 0.1966 0.1949 0.0153 0.0259 -0.0005 565 GLY A C 4319 O O . GLY A 565 ? 0.2235 0.2157 0.2139 0.0156 0.0264 -0.0007 565 GLY A O 4320 N N . ARG A 566 ? 0.2136 0.2058 0.2015 0.0179 0.0267 0.0014 566 ARG A N 4321 C CA . ARG A 566 ? 0.2257 0.2174 0.2094 0.0217 0.0280 0.0035 566 ARG A CA 4322 C C . ARG A 566 ? 0.2161 0.2126 0.1990 0.0238 0.0254 0.0045 566 ARG A C 4323 O O . ARG A 566 ? 0.2216 0.2190 0.2055 0.0231 0.0245 0.0045 566 ARG A O 4324 C CB . ARG A 566 ? 0.2617 0.2471 0.2416 0.0234 0.0328 0.0049 566 ARG A CB 4325 C CG . ARG A 566 ? 0.2953 0.2759 0.2756 0.0215 0.0360 0.0037 566 ARG A CG 4326 C CD . ARG A 566 ? 0.3873 0.3608 0.3643 0.0226 0.0413 0.0048 566 ARG A CD 4327 N NE A ARG A 566 ? 0.4181 0.3900 0.3963 0.0209 0.0420 0.0039 566 ARG A NE 4328 N NE B ARG A 566 ? 0.3614 0.3329 0.3329 0.0273 0.0435 0.0077 566 ARG A NE 4329 C CZ A ARG A 566 ? 0.4319 0.4002 0.4121 0.0178 0.0446 0.0019 566 ARG A CZ 4330 C CZ B ARG A 566 ? 0.3794 0.3482 0.3479 0.0295 0.0455 0.0093 566 ARG A CZ 4331 N NH1 A ARG A 566 ? 0.4363 0.4018 0.4174 0.0160 0.0471 0.0005 566 ARG A NH1 4332 N NH1 B ARG A 566 ? 0.3417 0.3097 0.3123 0.0272 0.0455 0.0082 566 ARG A NH1 4333 N NH2 A ARG A 566 ? 0.3683 0.3361 0.3496 0.0165 0.0448 0.0011 566 ARG A NH2 4334 N NH2 B ARG A 566 ? 0.4123 0.3796 0.3756 0.0342 0.0475 0.0120 566 ARG A NH2 4335 N N . LEU A 567 ? 0.2022 0.2021 0.1834 0.0265 0.0244 0.0054 567 LEU A N 4336 C CA . LEU A 567 ? 0.2115 0.2171 0.1925 0.0283 0.0218 0.0058 567 LEU A CA 4337 C C . LEU A 567 ? 0.2271 0.2309 0.2055 0.0303 0.0234 0.0073 567 LEU A C 4338 O O . LEU A 567 ? 0.2187 0.2181 0.1929 0.0330 0.0269 0.0090 567 LEU A O 4339 C CB . LEU A 567 ? 0.2106 0.2202 0.1893 0.0316 0.0210 0.0064 567 LEU A CB 4340 C CG . LEU A 567 ? 0.2055 0.2180 0.1870 0.0298 0.0189 0.0047 567 LEU A CG 4341 C CD1 . LEU A 567 ? 0.2189 0.2361 0.1982 0.0332 0.0182 0.0051 567 LEU A CD1 4342 C CD2 . LEU A 567 ? 0.2149 0.2313 0.2013 0.0264 0.0154 0.0028 567 LEU A CD2 4343 N N . PRO A 568 ? 0.2066 0.2136 0.1869 0.0292 0.0212 0.0069 568 PRO A N 4344 C CA . PRO A 568 ? 0.2134 0.2195 0.1911 0.0314 0.0224 0.0083 568 PRO A CA 4345 C C . PRO A 568 ? 0.2131 0.2247 0.1886 0.0350 0.0211 0.0092 568 PRO A C 4346 O O . PRO A 568 ? 0.2266 0.2390 0.2002 0.0371 0.0216 0.0103 568 PRO A O 4347 C CB . PRO A 568 ? 0.2047 0.2119 0.1862 0.0280 0.0205 0.0071 568 PRO A CB 4348 C CG . PRO A 568 ? 0.1912 0.2032 0.1765 0.0257 0.0170 0.0054 568 PRO A CG 4349 C CD . PRO A 568 ? 0.1891 0.1995 0.1741 0.0256 0.0179 0.0050 568 PRO A CD 4350 N N . ARG A 569 ? 0.2335 0.2495 0.2096 0.0357 0.0194 0.0085 569 ARG A N 4351 C CA . ARG A 569 ? 0.2514 0.2734 0.2254 0.0394 0.0183 0.0089 569 ARG A CA 4352 C C . ARG A 569 ? 0.2405 0.2647 0.2135 0.0410 0.0181 0.0086 569 ARG A C 4353 O O . ARG A 569 ? 0.2527 0.2743 0.2275 0.0387 0.0183 0.0078 569 ARG A O 4354 C CB . ARG A 569 ? 0.3038 0.3324 0.2810 0.0381 0.0150 0.0075 569 ARG A CB 4355 C CG . ARG A 569 ? 0.2874 0.3176 0.2698 0.0334 0.0124 0.0054 569 ARG A CG 4356 C CD . ARG A 569 ? 0.2600 0.2958 0.2451 0.0322 0.0100 0.0043 569 ARG A CD 4357 N NE . ARG A 569 ? 0.2650 0.3067 0.2479 0.0358 0.0095 0.0044 569 ARG A NE 4358 C CZ . ARG A 569 ? 0.2623 0.3053 0.2429 0.0383 0.0101 0.0055 569 ARG A CZ 4359 N NH1 . ARG A 569 ? 0.2762 0.3150 0.2567 0.0372 0.0111 0.0065 569 ARG A NH1 4360 N NH2 . ARG A 569 ? 0.2702 0.3195 0.2488 0.0420 0.0096 0.0054 569 ARG A NH2 4361 N N . THR A 570 ? 0.2492 0.2786 0.2194 0.0452 0.0177 0.0091 570 THR A N 4362 C CA . THR A 570 ? 0.2463 0.2790 0.2151 0.0475 0.0174 0.0088 570 THR A CA 4363 C C . THR A 570 ? 0.2324 0.2711 0.2062 0.0443 0.0139 0.0060 570 THR A C 4364 O O . THR A 570 ? 0.2456 0.2892 0.2226 0.0424 0.0115 0.0044 570 THR A O 4365 C CB . THR A 570 ? 0.2665 0.3041 0.2309 0.0532 0.0178 0.0100 570 THR A CB 4366 O OG1 . THR A 570 ? 0.2735 0.3046 0.2328 0.0565 0.0216 0.0129 570 THR A OG1 4367 C CG2 . THR A 570 ? 0.2815 0.3247 0.2446 0.0561 0.0170 0.0093 570 THR A CG2 4368 N N . TRP A 571 ? 0.2243 0.2624 0.1988 0.0436 0.0139 0.0053 571 TRP A N 4369 C CA . TRP A 571 ? 0.2207 0.2644 0.1995 0.0410 0.0109 0.0026 571 TRP A CA 4370 C C . TRP A 571 ? 0.2428 0.2935 0.2195 0.0449 0.0102 0.0020 571 TRP A C 4371 O O . TRP A 571 ? 0.2480 0.2972 0.2213 0.0479 0.0119 0.0031 571 TRP A O 4372 C CB . TRP A 571 ? 0.2223 0.2617 0.2035 0.0376 0.0110 0.0018 571 TRP A CB 4373 C CG . TRP A 571 ? 0.2039 0.2470 0.1903 0.0337 0.0081 -0.0008 571 TRP A CG 4374 C CD1 . TRP A 571 ? 0.2107 0.2609 0.1991 0.0337 0.0059 -0.0030 571 TRP A CD1 4375 C CD2 . TRP A 571 ? 0.2019 0.2418 0.1921 0.0292 0.0072 -0.0016 571 TRP A CD2 4376 N NE1 . TRP A 571 ? 0.1908 0.2417 0.1840 0.0295 0.0040 -0.0050 571 TRP A NE1 4377 C CE2 . TRP A 571 ? 0.1972 0.2419 0.1914 0.0269 0.0047 -0.0041 571 TRP A CE2 4378 C CE3 . TRP A 571 ? 0.2082 0.2420 0.1988 0.0272 0.0084 -0.0007 571 TRP A CE3 4379 C CZ2 . TRP A 571 ? 0.1970 0.2400 0.1950 0.0229 0.0035 -0.0052 571 TRP A CZ2 4380 C CZ3 . TRP A 571 ? 0.2041 0.2370 0.1988 0.0232 0.0069 -0.0019 571 TRP A CZ3 4381 C CH2 . TRP A 571 ? 0.1941 0.2313 0.1922 0.0214 0.0046 -0.0039 571 TRP A CH2 4382 N N . PHE A 572 ? 0.2319 0.2905 0.2105 0.0451 0.0078 0.0000 572 PHE A N 4383 C CA . PHE A 572 ? 0.2405 0.3074 0.2174 0.0490 0.0069 -0.0010 572 PHE A CA 4384 C C . PHE A 572 ? 0.2505 0.3201 0.2297 0.0477 0.0057 -0.0031 572 PHE A C 4385 O O . PHE A 572 ? 0.2460 0.3129 0.2292 0.0432 0.0048 -0.0045 572 PHE A O 4386 C CB . PHE A 572 ? 0.2603 0.3354 0.2395 0.0489 0.0047 -0.0031 572 PHE A CB 4387 C CG . PHE A 572 ? 0.2358 0.3119 0.2211 0.0433 0.0026 -0.0057 572 PHE A CG 4388 C CD1 . PHE A 572 ? 0.2353 0.3159 0.2243 0.0409 0.0009 -0.0087 572 PHE A CD1 4389 C CD2 . PHE A 572 ? 0.2330 0.3054 0.2200 0.0405 0.0027 -0.0050 572 PHE A CD2 4390 C CE1 . PHE A 572 ? 0.2375 0.3182 0.2318 0.0358 -0.0006 -0.0109 572 PHE A CE1 4391 C CE2 . PHE A 572 ? 0.2248 0.2978 0.2170 0.0356 0.0011 -0.0071 572 PHE A CE2 4392 C CZ . PHE A 572 ? 0.2071 0.2837 0.2028 0.0332 -0.0004 -0.0099 572 PHE A CZ 4393 N N . LYS A 573 ? 0.2468 0.3222 0.2232 0.0520 0.0056 -0.0035 573 LYS A N 4394 C CA . LYS A 573 ? 0.2538 0.3338 0.2326 0.0511 0.0041 -0.0061 573 LYS A CA 4395 C C . LYS A 573 ? 0.2416 0.3306 0.2252 0.0487 0.0012 -0.0101 573 LYS A C 4396 O O . LYS A 573 ? 0.2724 0.3629 0.2603 0.0451 -0.0002 -0.0127 573 LYS A O 4397 C CB . LYS A 573 ? 0.2525 0.3355 0.2263 0.0568 0.0053 -0.0051 573 LYS A CB 4398 C CG . LYS A 573 ? 0.2854 0.3592 0.2548 0.0585 0.0085 -0.0017 573 LYS A CG 4399 C CD . LYS A 573 ? 0.3008 0.3778 0.2650 0.0645 0.0098 -0.0005 573 LYS A CD 4400 C CE . LYS A 573 ? 0.3263 0.3936 0.2868 0.0655 0.0132 0.0026 573 LYS A CE 4401 N NZ . LYS A 573 ? 0.3582 0.4283 0.3129 0.0718 0.0148 0.0040 573 LYS A NZ 4402 N N . SER A 574 ? 0.2563 0.3514 0.2393 0.0508 0.0006 -0.0107 574 SER A N 4403 C CA . SER A 574 ? 0.2637 0.3677 0.2512 0.0487 -0.0018 -0.0145 574 SER A CA 4404 C C . SER A 574 ? 0.2529 0.3595 0.2402 0.0494 -0.0020 -0.0142 574 SER A C 4405 O O . SER A 574 ? 0.2697 0.3742 0.2523 0.0535 -0.0005 -0.0113 574 SER A O 4406 C CB . SER A 574 ? 0.2870 0.4008 0.2738 0.0521 -0.0028 -0.0171 574 SER A CB 4407 O OG A SER A 574 ? 0.3060 0.4300 0.2951 0.0524 -0.0044 -0.0202 574 SER A OG 4408 O OG B SER A 574 ? 0.2755 0.3919 0.2563 0.0586 -0.0016 -0.0148 574 SER A OG 4409 N N . VAL A 575 ? 0.2706 0.3812 0.2630 0.0453 -0.0036 -0.0172 575 VAL A N 4410 C CA . VAL A 575 ? 0.2784 0.3917 0.2715 0.0452 -0.0039 -0.0173 575 VAL A CA 4411 C C . VAL A 575 ? 0.2916 0.4145 0.2816 0.0508 -0.0042 -0.0180 575 VAL A C 4412 O O . VAL A 575 ? 0.2829 0.4067 0.2711 0.0526 -0.0039 -0.0168 575 VAL A O 4413 C CB . VAL A 575 ? 0.3018 0.4173 0.3011 0.0395 -0.0052 -0.0205 575 VAL A CB 4414 C CG1 . VAL A 575 ? 0.3190 0.4243 0.3206 0.0347 -0.0046 -0.0191 575 VAL A CG1 4415 C CG2 . VAL A 575 ? 0.3523 0.4772 0.3554 0.0383 -0.0067 -0.0252 575 VAL A CG2 4416 N N . ASP A 576 ? 0.3156 0.4454 0.3047 0.0537 -0.0048 -0.0199 576 ASP A N 4417 C CA . ASP A 576 ? 0.3328 0.4723 0.3183 0.0598 -0.0052 -0.0205 576 ASP A CA 4418 C C . ASP A 576 ? 0.3321 0.4668 0.3106 0.0655 -0.0031 -0.0159 576 ASP A C 4419 O O . ASP A 576 ? 0.3392 0.4809 0.3142 0.0709 -0.0031 -0.0158 576 ASP A O 4420 C CB . ASP A 576 ? 0.4151 0.5606 0.3999 0.0622 -0.0058 -0.0225 576 ASP A CB 4421 C CG . ASP A 576 ? 0.4846 0.6379 0.4757 0.0580 -0.0078 -0.0279 576 ASP A CG 4422 O OD1 . ASP A 576 ? 0.5335 0.6892 0.5292 0.0539 -0.0086 -0.0303 576 ASP A OD1 4423 O OD2 . ASP A 576 ? 0.5325 0.6895 0.5239 0.0589 -0.0083 -0.0297 576 ASP A OD2 4424 N N . GLN A 577 ? 0.2795 0.4024 0.2557 0.0647 -0.0011 -0.0122 577 GLN A N 4425 C CA . GLN A 577 ? 0.2768 0.3935 0.2464 0.0696 0.0014 -0.0077 577 GLN A CA 4426 C C . GLN A 577 ? 0.2898 0.4038 0.2589 0.0693 0.0020 -0.0061 577 GLN A C 4427 O O . GLN A 577 ? 0.2942 0.4045 0.2578 0.0739 0.0041 -0.0027 577 GLN A O 4428 C CB . GLN A 577 ? 0.2937 0.3988 0.2614 0.0684 0.0036 -0.0047 577 GLN A CB 4429 C CG . GLN A 577 ? 0.2891 0.3951 0.2565 0.0691 0.0036 -0.0055 577 GLN A CG 4430 C CD . GLN A 577 ? 0.3368 0.4312 0.3030 0.0671 0.0058 -0.0028 577 GLN A CD 4431 O OE1 . GLN A 577 ? 0.3213 0.4100 0.2916 0.0615 0.0054 -0.0033 577 GLN A OE1 4432 N NE2 . GLN A 577 ? 0.3233 0.4141 0.2839 0.0717 0.0082 -0.0001 577 GLN A NE2 4433 N N . LEU A 578 ? 0.2876 0.4028 0.2623 0.0639 0.0004 -0.0084 578 LEU A N 4434 C CA . LEU A 578 ? 0.2863 0.3962 0.2609 0.0625 0.0011 -0.0065 578 LEU A CA 4435 C C . LEU A 578 ? 0.2944 0.4123 0.2674 0.0663 0.0006 -0.0070 578 LEU A C 4436 O O . LEU A 578 ? 0.3322 0.4609 0.3073 0.0670 -0.0013 -0.0104 578 LEU A O 4437 C CB . LEU A 578 ? 0.2936 0.4006 0.2744 0.0554 -0.0001 -0.0083 578 LEU A CB 4438 C CG . LEU A 578 ? 0.2875 0.3858 0.2698 0.0517 0.0006 -0.0075 578 LEU A CG 4439 C CD1 . LEU A 578 ? 0.2833 0.3796 0.2713 0.0454 -0.0006 -0.0092 578 LEU A CD1 4440 C CD2 . LEU A 578 ? 0.2896 0.3777 0.2672 0.0537 0.0033 -0.0034 578 LEU A CD2 4441 N N . PRO A 579 ? 0.3208 0.4334 0.2903 0.0683 0.0022 -0.0039 579 PRO A N 4442 C CA . PRO A 579 ? 0.3233 0.4236 0.2902 0.0676 0.0047 -0.0002 579 PRO A CA 4443 C C . PRO A 579 ? 0.3278 0.4233 0.2888 0.0724 0.0072 0.0028 579 PRO A C 4444 O O . PRO A 579 ? 0.3337 0.4352 0.2904 0.0785 0.0075 0.0032 579 PRO A O 4445 C CB . PRO A 579 ? 0.3337 0.4335 0.2991 0.0690 0.0053 0.0012 579 PRO A CB 4446 C CG . PRO A 579 ? 0.3486 0.4601 0.3125 0.0738 0.0040 -0.0004 579 PRO A CG 4447 C CD . PRO A 579 ? 0.3268 0.4469 0.2954 0.0712 0.0015 -0.0046 579 PRO A CD 4448 N N . MET A 580 ? 0.3093 0.3945 0.2700 0.0699 0.0090 0.0047 580 MET A N 4449 C CA . MET A 580 ? 0.3008 0.3801 0.2564 0.0736 0.0118 0.0074 580 MET A CA 4450 C C . MET A 580 ? 0.3170 0.3839 0.2707 0.0720 0.0149 0.0104 580 MET A C 4451 O O . MET A 580 ? 0.3403 0.4018 0.2979 0.0666 0.0147 0.0098 580 MET A O 4452 C CB . MET A 580 ? 0.2879 0.3689 0.2456 0.0719 0.0108 0.0056 580 MET A CB 4453 C CG . MET A 580 ? 0.2884 0.3654 0.2407 0.0762 0.0135 0.0081 580 MET A CG 4454 S SD A MET A 580 ? 0.2631 0.3386 0.2169 0.0743 0.0133 0.0070 580 MET A SD 4455 S SD B MET A 580 ? 0.2505 0.3328 0.2067 0.0737 0.0111 0.0048 580 MET A SD 4456 C CE A MET A 580 ? 0.2485 0.3166 0.2086 0.0659 0.0126 0.0059 580 MET A CE 4457 C CE B MET A 580 ? 0.2440 0.3177 0.2060 0.0656 0.0108 0.0041 580 MET A CE 4458 N N . ASN A 581 ? 0.3300 0.3929 0.2781 0.0768 0.0178 0.0135 581 ASN A N 4459 C CA . ASN A 581 ? 0.3376 0.3892 0.2838 0.0756 0.0211 0.0161 581 ASN A CA 4460 C C . ASN A 581 ? 0.3828 0.4279 0.3222 0.0807 0.0252 0.0193 581 ASN A C 4461 O O . ASN A 581 ? 0.4095 0.4595 0.3446 0.0865 0.0256 0.0202 581 ASN A O 4462 C CB . ASN A 581 ? 0.3271 0.3780 0.2730 0.0756 0.0212 0.0167 581 ASN A CB 4463 C CG . ASN A 581 ? 0.3271 0.3807 0.2797 0.0695 0.0181 0.0141 581 ASN A CG 4464 O OD1 . ASN A 581 ? 0.3167 0.3639 0.2724 0.0646 0.0185 0.0139 581 ASN A OD1 4465 N ND2 . ASN A 581 ? 0.3036 0.3668 0.2586 0.0697 0.0152 0.0119 581 ASN A ND2 4466 N N . VAL A 582 ? 0.4044 0.4388 0.3430 0.0785 0.0284 0.0210 582 VAL A N 4467 C CA . VAL A 582 ? 0.4345 0.4607 0.3670 0.0824 0.0332 0.0241 582 VAL A CA 4468 C C . VAL A 582 ? 0.4607 0.4883 0.3865 0.0898 0.0352 0.0267 582 VAL A C 4469 O O . VAL A 582 ? 0.4638 0.4924 0.3892 0.0906 0.0350 0.0271 582 VAL A O 4470 C CB . VAL A 582 ? 0.4436 0.4584 0.3768 0.0784 0.0364 0.0251 582 VAL A CB 4471 C CG1 . VAL A 582 ? 0.5090 0.5145 0.4358 0.0824 0.0420 0.0283 582 VAL A CG1 4472 C CG2 . VAL A 582 ? 0.4658 0.4797 0.4055 0.0716 0.0344 0.0225 582 VAL A CG2 4473 N N . GLY A 583 ? 0.5029 0.5312 0.4233 0.0955 0.0371 0.0285 583 GLY A N 4474 C CA . GLY A 583 ? 0.5075 0.5372 0.4209 0.1032 0.0392 0.0311 583 GLY A CA 4475 C C . GLY A 583 ? 0.5340 0.5773 0.4473 0.1071 0.0354 0.0294 583 GLY A C 4476 O O . GLY A 583 ? 0.5652 0.6115 0.4723 0.1145 0.0369 0.0315 583 GLY A O 4477 N N . ASP A 584 ? 0.4816 0.5333 0.4017 0.1024 0.0307 0.0256 584 ASP A N 4478 C CA . ASP A 584 ? 0.4788 0.5441 0.3995 0.1057 0.0271 0.0233 584 ASP A CA 4479 C C . ASP A 584 ? 0.4696 0.5372 0.3865 0.1100 0.0281 0.0239 584 ASP A C 4480 O O . ASP A 584 ? 0.4621 0.5227 0.3794 0.1076 0.0297 0.0246 584 ASP A O 4481 C CB . ASP A 584 ? 0.4631 0.5363 0.3921 0.0992 0.0223 0.0188 584 ASP A CB 4482 C CG . ASP A 584 ? 0.4862 0.5602 0.4187 0.0959 0.0208 0.0178 584 ASP A CG 4483 O OD1 . ASP A 584 ? 0.4377 0.5150 0.3770 0.0898 0.0178 0.0147 584 ASP A OD1 4484 O OD2 . ASP A 584 ? 0.4839 0.5555 0.4125 0.0994 0.0227 0.0200 584 ASP A OD2 4485 N N . ALA A 585 ? 0.4874 0.5650 0.4007 0.1166 0.0270 0.0237 585 ALA A N 4486 C CA . ALA A 585 ? 0.4985 0.5792 0.4075 0.1218 0.0279 0.0244 585 ALA A CA 4487 C C . ALA A 585 ? 0.4946 0.5795 0.4096 0.1167 0.0250 0.0210 585 ALA A C 4488 O O . ALA A 585 ? 0.4705 0.5536 0.3828 0.1187 0.0264 0.0219 585 ALA A O 4489 C CB . ALA A 585 ? 0.5112 0.6035 0.4156 0.1299 0.0268 0.0243 585 ALA A CB 4490 N N . HIS A 586 ? 0.4452 0.5349 0.3679 0.1100 0.0211 0.0171 586 HIS A N 4491 C CA . HIS A 586 ? 0.4074 0.5009 0.3361 0.1048 0.0184 0.0137 586 HIS A CA 4492 C C . HIS A 586 ? 0.4037 0.4866 0.3368 0.0974 0.0191 0.0138 586 HIS A C 4493 O O . HIS A 586 ? 0.4248 0.5104 0.3636 0.0923 0.0166 0.0108 586 HIS A O 4494 C CB . HIS A 586 ? 0.4008 0.5073 0.3353 0.1026 0.0138 0.0089 586 HIS A CB 4495 C CG . HIS A 586 ? 0.4082 0.5136 0.3479 0.0970 0.0123 0.0075 586 HIS A CG 4496 N ND1 . HIS A 586 ? 0.3968 0.4987 0.3337 0.0989 0.0138 0.0098 586 HIS A ND1 4497 C CD2 . HIS A 586 ? 0.3833 0.4905 0.3305 0.0899 0.0096 0.0042 586 HIS A CD2 4498 C CE1 . HIS A 586 ? 0.4041 0.5056 0.3467 0.0930 0.0120 0.0080 586 HIS A CE1 4499 N NE2 . HIS A 586 ? 0.3709 0.4755 0.3196 0.0875 0.0095 0.0046 586 HIS A NE2 4500 N N . TYR A 587 ? 0.3921 0.4635 0.3225 0.0969 0.0225 0.0170 587 TYR A N 4501 C CA . TYR A 587 ? 0.3817 0.4437 0.3163 0.0900 0.0232 0.0169 587 TYR A CA 4502 C C . TYR A 587 ? 0.3948 0.4549 0.3304 0.0883 0.0235 0.0163 587 TYR A C 4503 O O . TYR A 587 ? 0.4026 0.4588 0.3329 0.0926 0.0266 0.0188 587 TYR A O 4504 C CB . TYR A 587 ? 0.3886 0.4388 0.3198 0.0902 0.0274 0.0203 587 TYR A CB 4505 C CG . TYR A 587 ? 0.3840 0.4267 0.3204 0.0828 0.0274 0.0194 587 TYR A CG 4506 C CD1 . TYR A 587 ? 0.4077 0.4533 0.3498 0.0778 0.0243 0.0171 587 TYR A CD1 4507 C CD2 . TYR A 587 ? 0.4069 0.4398 0.3424 0.0809 0.0306 0.0209 587 TYR A CD2 4508 C CE1 . TYR A 587 ? 0.3748 0.4141 0.3214 0.0715 0.0243 0.0163 587 TYR A CE1 4509 C CE2 . TYR A 587 ? 0.4126 0.4395 0.3528 0.0743 0.0305 0.0197 587 TYR A CE2 4510 C CZ . TYR A 587 ? 0.3896 0.4198 0.3352 0.0699 0.0273 0.0175 587 TYR A CZ 4511 O OH . TYR A 587 ? 0.3747 0.3995 0.3249 0.0638 0.0272 0.0165 587 TYR A OH 4512 N N . ASP A 588 ? 0.3473 0.4105 0.2896 0.0825 0.0203 0.0130 588 ASP A N 4513 C CA . ASP A 588 ? 0.3521 0.4148 0.2958 0.0808 0.0200 0.0119 588 ASP A CA 4514 C C . ASP A 588 ? 0.3193 0.3798 0.2702 0.0730 0.0179 0.0094 588 ASP A C 4515 O O . ASP A 588 ? 0.3126 0.3803 0.2682 0.0703 0.0145 0.0061 588 ASP A O 4516 C CB . ASP A 588 ? 0.3730 0.4471 0.3162 0.0844 0.0177 0.0098 588 ASP A CB 4517 C CG . ASP A 588 ? 0.3922 0.4664 0.3369 0.0829 0.0173 0.0086 588 ASP A CG 4518 O OD1 . ASP A 588 ? 0.4075 0.4724 0.3517 0.0808 0.0196 0.0102 588 ASP A OD1 4519 O OD2 . ASP A 588 ? 0.4156 0.4997 0.3622 0.0838 0.0145 0.0057 588 ASP A OD2 4520 N N . PRO A 589 ? 0.3131 0.3636 0.2644 0.0698 0.0201 0.0109 589 PRO A N 4521 C CA . PRO A 589 ? 0.3093 0.3587 0.2673 0.0630 0.0178 0.0086 589 PRO A CA 4522 C C . PRO A 589 ? 0.3006 0.3489 0.2615 0.0597 0.0171 0.0071 589 PRO A C 4523 O O . PRO A 589 ? 0.3270 0.3725 0.2847 0.0620 0.0192 0.0084 589 PRO A O 4524 C CB . PRO A 589 ? 0.3299 0.3698 0.2869 0.0613 0.0205 0.0107 589 PRO A CB 4525 C CG . PRO A 589 ? 0.3711 0.4046 0.3221 0.0654 0.0248 0.0138 589 PRO A CG 4526 C CD . PRO A 589 ? 0.3494 0.3900 0.2960 0.0717 0.0245 0.0144 589 PRO A CD 4527 N N . LEU A 590 ? 0.2690 0.3195 0.2359 0.0545 0.0142 0.0043 590 LEU A N 4528 C CA . LEU A 590 ? 0.2630 0.3104 0.2329 0.0508 0.0139 0.0032 590 LEU A CA 4529 C C . LEU A 590 ? 0.2612 0.2986 0.2305 0.0486 0.0167 0.0050 590 LEU A C 4530 O O . LEU A 590 ? 0.2949 0.3282 0.2632 0.0484 0.0184 0.0054 590 LEU A O 4531 C CB . LEU A 590 ? 0.2607 0.3124 0.2368 0.0460 0.0105 0.0000 590 LEU A CB 4532 C CG . LEU A 590 ? 0.2613 0.3110 0.2407 0.0425 0.0097 -0.0015 590 LEU A CG 4533 C CD1 . LEU A 590 ? 0.2695 0.3243 0.2476 0.0452 0.0093 -0.0025 590 LEU A CD1 4534 C CD2 . LEU A 590 ? 0.2690 0.3213 0.2541 0.0379 0.0070 -0.0041 590 LEU A CD2 4535 N N . PHE A 591 ? 0.2450 0.2790 0.2152 0.0468 0.0172 0.0056 591 PHE A N 4536 C CA . PHE A 591 ? 0.2559 0.2809 0.2251 0.0452 0.0202 0.0071 591 PHE A CA 4537 C C . PHE A 591 ? 0.2807 0.3034 0.2468 0.0475 0.0220 0.0091 591 PHE A C 4538 O O . PHE A 591 ? 0.2761 0.3031 0.2436 0.0474 0.0200 0.0085 591 PHE A O 4539 C CB . PHE A 591 ? 0.2563 0.2792 0.2309 0.0395 0.0186 0.0053 591 PHE A CB 4540 C CG . PHE A 591 ? 0.2480 0.2729 0.2260 0.0369 0.0167 0.0033 591 PHE A CG 4541 C CD1 . PHE A 591 ? 0.2699 0.2907 0.2473 0.0364 0.0186 0.0034 591 PHE A CD1 4542 C CD2 . PHE A 591 ? 0.2553 0.2860 0.2375 0.0346 0.0132 0.0010 591 PHE A CD2 4543 C CE1 . PHE A 591 ? 0.2588 0.2816 0.2393 0.0340 0.0167 0.0015 591 PHE A CE1 4544 C CE2 . PHE A 591 ? 0.2528 0.2851 0.2382 0.0322 0.0116 -0.0009 591 PHE A CE2 4545 C CZ . PHE A 591 ? 0.2557 0.2841 0.2402 0.0320 0.0132 -0.0007 591 PHE A CZ 4546 N N . ARG A 592 ? 0.2978 0.3133 0.2598 0.0495 0.0261 0.0114 592 ARG A N 4547 C CA . ARG A 592 ? 0.3031 0.3158 0.2617 0.0519 0.0282 0.0134 592 ARG A CA 4548 C C . ARG A 592 ? 0.2916 0.3006 0.2536 0.0477 0.0281 0.0127 592 ARG A C 4549 O O . ARG A 592 ? 0.2686 0.2753 0.2345 0.0431 0.0275 0.0111 592 ARG A O 4550 C CB . ARG A 592 ? 0.3435 0.3495 0.2960 0.0561 0.0332 0.0162 592 ARG A CB 4551 C CG . ARG A 592 ? 0.4303 0.4276 0.3836 0.0527 0.0364 0.0163 592 ARG A CG 4552 C CD . ARG A 592 ? 0.5604 0.5512 0.5087 0.0557 0.0412 0.0184 592 ARG A CD 4553 N NE . ARG A 592 ? 0.6619 0.6455 0.6125 0.0513 0.0438 0.0175 592 ARG A NE 4554 C CZ . ARG A 592 ? 0.7105 0.6949 0.6654 0.0471 0.0421 0.0153 592 ARG A CZ 4555 N NH1 . ARG A 592 ? 0.7387 0.7172 0.6957 0.0433 0.0445 0.0143 592 ARG A NH1 4556 N NH2 . ARG A 592 ? 0.7603 0.7517 0.7177 0.0468 0.0381 0.0139 592 ARG A NH2 4557 N N . LEU A 593 ? 0.2959 0.3046 0.2560 0.0494 0.0287 0.0138 593 LEU A N 4558 C CA . LEU A 593 ? 0.2823 0.2860 0.2440 0.0465 0.0299 0.0138 593 LEU A CA 4559 C C . LEU A 593 ? 0.2953 0.2905 0.2564 0.0446 0.0338 0.0141 593 LEU A C 4560 O O . LEU A 593 ? 0.2946 0.2852 0.2512 0.0477 0.0374 0.0159 593 LEU A O 4561 C CB . LEU A 593 ? 0.3255 0.3289 0.2834 0.0502 0.0313 0.0157 593 LEU A CB 4562 C CG . LEU A 593 ? 0.3356 0.3336 0.2938 0.0483 0.0332 0.0161 593 LEU A CG 4563 C CD1 . LEU A 593 ? 0.3546 0.3569 0.3183 0.0441 0.0294 0.0139 593 LEU A CD1 4564 C CD2 . LEU A 593 ? 0.3522 0.3503 0.3056 0.0532 0.0348 0.0183 593 LEU A CD2 4565 N N . GLY A 594 ? 0.2670 0.2602 0.2325 0.0397 0.0331 0.0123 594 GLY A N 4566 C CA . GLY A 594 ? 0.2497 0.2361 0.2156 0.0373 0.0363 0.0118 594 GLY A CA 4567 C C . GLY A 594 ? 0.2489 0.2357 0.2171 0.0351 0.0356 0.0104 594 GLY A C 4568 O O . GLY A 594 ? 0.2576 0.2397 0.2272 0.0324 0.0379 0.0094 594 GLY A O 4569 N N . TYR A 595 ? 0.2481 0.2409 0.2171 0.0361 0.0325 0.0100 595 TYR A N 4570 C CA . TYR A 595 ? 0.2512 0.2447 0.2222 0.0343 0.0317 0.0086 595 TYR A CA 4571 C C . TYR A 595 ? 0.2392 0.2333 0.2158 0.0292 0.0295 0.0061 595 TYR A C 4572 O O . TYR A 595 ? 0.2363 0.2336 0.2156 0.0275 0.0267 0.0052 595 TYR A O 4573 C CB . TYR A 595 ? 0.2572 0.2577 0.2283 0.0364 0.0286 0.0083 595 TYR A CB 4574 C CG . TYR A 595 ? 0.2720 0.2739 0.2455 0.0345 0.0273 0.0068 595 TYR A CG 4575 C CD1 . TYR A 595 ? 0.2811 0.2868 0.2596 0.0309 0.0237 0.0045 595 TYR A CD1 4576 C CD2 . TYR A 595 ? 0.3210 0.3202 0.2917 0.0363 0.0299 0.0076 595 TYR A CD2 4577 C CE1 . TYR A 595 ? 0.3032 0.3102 0.2839 0.0293 0.0225 0.0030 595 TYR A CE1 4578 C CE2 . TYR A 595 ? 0.3045 0.3053 0.2777 0.0345 0.0286 0.0060 595 TYR A CE2 4579 C CZ . TYR A 595 ? 0.3122 0.3168 0.2903 0.0309 0.0249 0.0037 595 TYR A CZ 4580 O OH . TYR A 595 ? 0.3391 0.3454 0.3198 0.0292 0.0234 0.0021 595 TYR A OH 4581 N N . GLY A 596 ? 0.2305 0.2219 0.2086 0.0270 0.0307 0.0049 596 GLY A N 4582 C CA . GLY A 596 ? 0.2253 0.2185 0.2084 0.0228 0.0282 0.0025 596 GLY A CA 4583 C C . GLY A 596 ? 0.2510 0.2408 0.2350 0.0210 0.0304 0.0013 596 GLY A C 4584 O O . GLY A 596 ? 0.2921 0.2764 0.2739 0.0213 0.0345 0.0019 596 GLY A O 4585 N N . LEU A 597 ? 0.2263 0.2192 0.2135 0.0191 0.0278 -0.0004 597 LEU A N 4586 C CA . LEU A 597 ? 0.2338 0.2244 0.2224 0.0170 0.0294 -0.0018 597 LEU A CA 4587 C C . LEU A 597 ? 0.2500 0.2392 0.2419 0.0135 0.0297 -0.0038 597 LEU A C 4588 O O . LEU A 597 ? 0.2616 0.2527 0.2554 0.0123 0.0277 -0.0043 597 LEU A O 4589 C CB . LEU A 597 ? 0.2237 0.2183 0.2141 0.0167 0.0265 -0.0028 597 LEU A CB 4590 C CG . LEU A 597 ? 0.2423 0.2395 0.2299 0.0201 0.0258 -0.0013 597 LEU A CG 4591 C CD1 . LEU A 597 ? 0.2393 0.2405 0.2294 0.0191 0.0230 -0.0029 597 LEU A CD1 4592 C CD2 . LEU A 597 ? 0.2640 0.2567 0.2471 0.0228 0.0301 0.0004 597 LEU A CD2 4593 N N . THR A 598 ? 0.2804 0.2667 0.2732 0.0116 0.0321 -0.0053 598 THR A N 4594 C CA . THR A 598 ? 0.2832 0.2691 0.2794 0.0083 0.0325 -0.0077 598 THR A CA 4595 C C . THR A 598 ? 0.2838 0.2720 0.2833 0.0060 0.0311 -0.0100 598 THR A C 4596 O O . THR A 598 ? 0.2932 0.2819 0.2922 0.0068 0.0309 -0.0099 598 THR A O 4597 C CB . THR A 598 ? 0.3176 0.2977 0.3123 0.0076 0.0374 -0.0079 598 THR A CB 4598 O OG1 . THR A 598 ? 0.3672 0.3440 0.3600 0.0082 0.0407 -0.0076 598 THR A OG1 4599 C CG2 . THR A 598 ? 0.3445 0.3221 0.3358 0.0100 0.0390 -0.0056 598 THR A CG2 4600 N N . THR A 599 ? 0.2758 0.2658 0.2788 0.0034 0.0299 -0.0123 599 THR A N 4601 C CA . THR A 599 ? 0.2678 0.2596 0.2739 0.0012 0.0294 -0.0150 599 THR A CA 4602 C C . THR A 599 ? 0.2953 0.2857 0.3033 -0.0013 0.0318 -0.0174 599 THR A C 4603 O O . THR A 599 ? 0.3033 0.2923 0.3108 -0.0014 0.0329 -0.0171 599 THR A O 4604 C CB . THR A 599 ? 0.2680 0.2648 0.2768 0.0007 0.0248 -0.0158 599 THR A CB 4605 O OG1 . THR A 599 ? 0.2522 0.2507 0.2621 0.0003 0.0231 -0.0158 599 THR A OG1 4606 C CG2 . THR A 599 ? 0.2489 0.2475 0.2564 0.0027 0.0224 -0.0140 599 THR A CG2 4607 N N . ASN A 600 ? 0.3234 0.3148 0.3339 -0.0034 0.0326 -0.0201 600 ASN A N 4608 C CA . ASN A 600 ? 0.3358 0.3279 0.3492 -0.0061 0.0342 -0.0234 600 ASN A CA 4609 C C . ASN A 600 ? 0.3534 0.3514 0.3703 -0.0072 0.0303 -0.0255 600 ASN A C 4610 O O . ASN A 600 ? 0.3409 0.3418 0.3586 -0.0065 0.0274 -0.0254 600 ASN A O 4611 C CB . ASN A 600 ? 0.3929 0.3824 0.4068 -0.0078 0.0383 -0.0254 600 ASN A CB 4612 C CG . ASN A 600 ? 0.4166 0.3994 0.4269 -0.0070 0.0432 -0.0236 600 ASN A CG 4613 O OD1 . ASN A 600 ? 0.4715 0.4519 0.4804 -0.0065 0.0444 -0.0225 600 ASN A OD1 4614 N ND2 . ASN A 600 ? 0.4485 0.4282 0.4573 -0.0067 0.0461 -0.0231 600 ASN A ND2 4615 N N . ALA A 601 ? 0.3744 0.3743 0.3933 -0.0085 0.0302 -0.0274 601 ALA A N 4616 C CA . ALA A 601 ? 0.4031 0.4088 0.4251 -0.0092 0.0269 -0.0296 601 ALA A CA 4617 C C . ALA A 601 ? 0.4303 0.4387 0.4548 -0.0105 0.0269 -0.0324 601 ALA A C 4618 O O . ALA A 601 ? 0.3964 0.4025 0.4212 -0.0120 0.0305 -0.0340 601 ALA A O 4619 C CB . ALA A 601 ? 0.3996 0.4069 0.4231 -0.0104 0.0274 -0.0315 601 ALA A CB 4620 N N . THR A 602 ? 0.4288 0.4417 0.4547 -0.0098 0.0232 -0.0328 602 THR A N 4621 C CA . THR A 602 ? 0.4939 0.5103 0.5223 -0.0107 0.0227 -0.0356 602 THR A CA 4622 C C . THR A 602 ? 0.5427 0.5645 0.5741 -0.0118 0.0218 -0.0391 602 THR A C 4623 O O . THR A 602 ? 0.5905 0.6123 0.6228 -0.0132 0.0238 -0.0409 602 THR A O 4624 C CB . THR A 602 ? 0.5430 0.5607 0.5708 -0.0090 0.0196 -0.0340 602 THR A CB 4625 O OG1 . THR A 602 ? 0.4973 0.5160 0.5242 -0.0072 0.0164 -0.0317 602 THR A OG1 4626 C CG2 . THR A 602 ? 0.5671 0.5805 0.5926 -0.0084 0.0213 -0.0319 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 ASP 1 1 1 ASP ASP A . n A 1 2 TYR 2 2 2 TYR TYR A . n A 1 3 VAL 3 3 3 VAL VAL A . n A 1 4 LEU 4 4 4 LEU LEU A . n A 1 5 TYR 5 5 5 TYR TYR A . n A 1 6 LYS 6 6 6 LYS LYS A . n A 1 7 ASP 7 7 7 ASP ASP A . n A 1 8 ALA 8 8 8 ALA ALA A . n A 1 9 THR 9 9 9 THR THR A . n A 1 10 LYS 10 10 10 LYS LYS A . n A 1 11 PRO 11 11 11 PRO PRO A . n A 1 12 VAL 12 12 12 VAL VAL A . n A 1 13 GLU 13 13 13 GLU GLU A . n A 1 14 ASP 14 14 14 ASP ASP A . n A 1 15 ARG 15 15 15 ARG ARG A . n A 1 16 VAL 16 16 16 VAL VAL A . n A 1 17 ALA 17 17 17 ALA ALA A . n A 1 18 ASP 18 18 18 ASP ASP A . n A 1 19 LEU 19 19 19 LEU LEU A . n A 1 20 LEU 20 20 20 LEU LEU A . n A 1 21 GLY 21 21 21 GLY GLY A . n A 1 22 ARG 22 22 22 ARG ARG A . n A 1 23 MET 23 23 23 MET MET A . n A 1 24 THR 24 24 24 THR THR A . n A 1 25 LEU 25 25 25 LEU LEU A . n A 1 26 ALA 26 26 26 ALA ALA A . n A 1 27 GLU 27 27 27 GLU GLU A . n A 1 28 LYS 28 28 28 LYS LYS A . n A 1 29 ILE 29 29 29 ILE ILE A . n A 1 30 GLY 30 30 30 GLY GLY A . n A 1 31 GLN 31 31 31 GLN GLN A . n A 1 32 MET 32 32 32 MET MET A . n A 1 33 THR 33 33 33 THR THR A . n A 1 34 GLN 34 34 34 GLN GLN A . n A 1 35 ILE 35 35 35 ILE ILE A . n A 1 36 GLU 36 36 36 GLU GLU A . n A 1 37 ARG 37 37 37 ARG ARG A . n A 1 38 LEU 38 38 38 LEU LEU A . n A 1 39 VAL 39 39 39 VAL VAL A . n A 1 40 ALA 40 40 40 ALA ALA A . n A 1 41 THR 41 41 41 THR THR A . n A 1 42 PRO 42 42 42 PRO PRO A . n A 1 43 ASP 43 43 43 ASP ASP A . n A 1 44 VAL 44 44 44 VAL VAL A . n A 1 45 LEU 45 45 45 LEU LEU A . n A 1 46 ARG 46 46 46 ARG ARG A . n A 1 47 ASP 47 47 47 ASP ASP A . n A 1 48 ASN 48 48 48 ASN ASN A . n A 1 49 PHE 49 49 49 PHE PHE A . n A 1 50 ILE 50 50 50 ILE ILE A . n A 1 51 GLY 51 51 51 GLY GLY A . n A 1 52 SER 52 52 52 SER SER A . n A 1 53 LEU 53 53 53 LEU LEU A . n A 1 54 LEU 54 54 54 LEU LEU A . n A 1 55 SER 55 55 55 SER SER A . n A 1 56 GLY 56 56 56 GLY GLY A . n A 1 57 GLY 57 57 57 GLY GLY A . n A 1 58 GLY 58 58 58 GLY GLY A . n A 1 59 SER 59 59 59 SER SER A . n A 1 60 VAL 60 60 60 VAL VAL A . n A 1 61 PRO 61 61 61 PRO PRO A . n A 1 62 ARG 62 62 62 ARG ARG A . n A 1 63 LYS 63 63 63 LYS LYS A . n A 1 64 GLY 64 64 64 GLY GLY A . n A 1 65 ALA 65 65 65 ALA ALA A . n A 1 66 THR 66 66 66 THR THR A . n A 1 67 ALA 67 67 67 ALA ALA A . n A 1 68 LYS 68 68 68 LYS LYS A . n A 1 69 GLU 69 69 69 GLU GLU A . n A 1 70 TRP 70 70 70 TRP TRP A . n A 1 71 GLN 71 71 71 GLN GLN A . n A 1 72 ASP 72 72 72 ASP ASP A . n A 1 73 MET 73 73 73 MET MET A . n A 1 74 VAL 74 74 74 VAL VAL A . n A 1 75 ASP 75 75 75 ASP ASP A . n A 1 76 GLY 76 76 76 GLY GLY A . n A 1 77 PHE 77 77 77 PHE PHE A . n A 1 78 GLN 78 78 78 GLN GLN A . n A 1 79 LYS 79 79 79 LYS LYS A . n A 1 80 ALA 80 80 80 ALA ALA A . n A 1 81 CYS 81 81 81 CYS CYS A . n A 1 82 MET 82 82 82 MET MET A . n A 1 83 SER 83 83 83 SER SER A . n A 1 84 THR 84 84 84 THR THR A . n A 1 85 ARG 85 85 85 ARG ARG A . n A 1 86 LEU 86 86 86 LEU LEU A . n A 1 87 GLY 87 87 87 GLY GLY A . n A 1 88 ILE 88 88 88 ILE ILE A . n A 1 89 PRO 89 89 89 PRO PRO A . n A 1 90 MET 90 90 90 MET MET A . n A 1 91 ILE 91 91 91 ILE ILE A . n A 1 92 TYR 92 92 92 TYR TYR A . n A 1 93 GLY 93 93 93 GLY GLY A . n A 1 94 ILE 94 94 94 ILE ILE A . n A 1 95 ASP 95 95 95 ASP ASP A . n A 1 96 ALA 96 96 96 ALA ALA A . n A 1 97 VAL 97 97 97 VAL VAL A . n A 1 98 HIS 98 98 98 HIS HIS A . n A 1 99 GLY 99 99 99 GLY GLY A . n A 1 100 GLN 100 100 100 GLN GLN A . n A 1 101 ASN 101 101 101 ASN ASN A . n A 1 102 ASN 102 102 102 ASN ASN A . n A 1 103 VAL 103 103 103 VAL VAL A . n A 1 104 TYR 104 104 104 TYR TYR A . n A 1 105 GLY 105 105 105 GLY GLY A . n A 1 106 ALA 106 106 106 ALA ALA A . n A 1 107 THR 107 107 107 THR THR A . n A 1 108 ILE 108 108 108 ILE ILE A . n A 1 109 PHE 109 109 109 PHE PHE A . n A 1 110 PRO 110 110 110 PRO PRO A . n A 1 111 HIS 111 111 111 HIS HIS A . n A 1 112 ASN 112 112 112 ASN ASN A . n A 1 113 VAL 113 113 113 VAL VAL A . n A 1 114 GLY 114 114 114 GLY GLY A . n A 1 115 LEU 115 115 115 LEU LEU A . n A 1 116 GLY 116 116 116 GLY GLY A . n A 1 117 ALA 117 117 117 ALA ALA A . n A 1 118 THR 118 118 118 THR THR A . n A 1 119 ARG 119 119 119 ARG ARG A . n A 1 120 ASP 120 120 120 ASP ASP A . n A 1 121 PRO 121 121 121 PRO PRO A . n A 1 122 TYR 122 122 122 TYR TYR A . n A 1 123 LEU 123 123 123 LEU LEU A . n A 1 124 VAL 124 124 124 VAL VAL A . n A 1 125 LYS 125 125 125 LYS LYS A . n A 1 126 ARG 126 126 126 ARG ARG A . n A 1 127 ILE 127 127 127 ILE ILE A . n A 1 128 GLY 128 128 128 GLY GLY A . n A 1 129 GLU 129 129 129 GLU GLU A . n A 1 130 ALA 130 130 130 ALA ALA A . n A 1 131 THR 131 131 131 THR THR A . n A 1 132 ALA 132 132 132 ALA ALA A . n A 1 133 LEU 133 133 133 LEU LEU A . n A 1 134 GLU 134 134 134 GLU GLU A . n A 1 135 VAL 135 135 135 VAL VAL A . n A 1 136 ARG 136 136 136 ARG ARG A . n A 1 137 ALA 137 137 137 ALA ALA A . n A 1 138 THR 138 138 138 THR THR A . n A 1 139 GLY 139 139 139 GLY GLY A . n A 1 140 ILE 140 140 140 ILE ILE A . n A 1 141 GLN 141 141 141 GLN GLN A . n A 1 142 TYR 142 142 142 TYR TYR A . n A 1 143 ALA 143 143 143 ALA ALA A . n A 1 144 PHE 144 144 144 PHE PHE A . n A 1 145 ALA 145 145 145 ALA ALA A . n A 1 146 PRO 146 146 146 PRO PRO A . n A 1 147 CYS 147 147 147 CYS CYS A . n A 1 148 ILE 148 148 148 ILE ILE A . n A 1 149 ALA 149 149 149 ALA ALA A . n A 1 150 VAL 150 150 150 VAL VAL A . n A 1 151 CYS 151 151 151 CYS CYS A . n A 1 152 ARG 152 152 152 ARG ARG A . n A 1 153 ASP 153 153 153 ASP ASP A . n A 1 154 PRO 154 154 154 PRO PRO A . n A 1 155 ARG 155 155 155 ARG ARG A . n A 1 156 TRP 156 156 156 TRP TRP A . n A 1 157 GLY 157 157 157 GLY GLY A . n A 1 158 ARG 158 158 158 ARG ARG A . n A 1 159 CYS 159 159 159 CYS CYS A . n A 1 160 TYR 160 160 160 TYR TYR A . n A 1 161 GLU 161 161 161 GLU GLU A . n A 1 162 SER 162 162 162 SER SER A . n A 1 163 TYR 163 163 163 TYR TYR A . n A 1 164 SER 164 164 164 SER SER A . n A 1 165 GLU 165 165 165 GLU GLU A . n A 1 166 ASP 166 166 166 ASP ASP A . n A 1 167 ARG 167 167 167 ARG ARG A . n A 1 168 ARG 168 168 168 ARG ARG A . n A 1 169 ILE 169 169 169 ILE ILE A . n A 1 170 VAL 170 170 170 VAL VAL A . n A 1 171 GLN 171 171 171 GLN GLN A . n A 1 172 SER 172 172 172 SER SER A . n A 1 173 MET 173 173 173 MET MET A . n A 1 174 THR 174 174 174 THR THR A . n A 1 175 GLU 175 175 175 GLU GLU A . n A 1 176 LEU 176 176 176 LEU LEU A . n A 1 177 ILE 177 177 177 ILE ILE A . n A 1 178 PRO 178 178 178 PRO PRO A . n A 1 179 GLY 179 179 179 GLY GLY A . n A 1 180 LEU 180 180 180 LEU LEU A . n A 1 181 GLN 181 181 181 GLN GLN A . n A 1 182 GLY 182 182 182 GLY GLY A . n A 1 183 ASP 183 183 183 ASP ASP A . n A 1 184 VAL 184 184 184 VAL VAL A . n A 1 185 PRO 185 185 185 PRO PRO A . n A 1 186 LYS 186 186 186 LYS LYS A . n A 1 187 ASP 187 187 187 ASP ASP A . n A 1 188 PHE 188 188 188 PHE PHE A . n A 1 189 THR 189 189 189 THR THR A . n A 1 190 SER 190 190 190 SER SER A . n A 1 191 GLY 191 191 191 GLY GLY A . n A 1 192 MET 192 192 192 MET MET A . n A 1 193 PRO 193 193 193 PRO PRO A . n A 1 194 PHE 194 194 194 PHE PHE A . n A 1 195 VAL 195 195 195 VAL VAL A . n A 1 196 ALA 196 196 196 ALA ALA A . n A 1 197 GLY 197 197 197 GLY GLY A . n A 1 198 LYS 198 198 198 LYS LYS A . n A 1 199 ASN 199 199 199 ASN ASN A . n A 1 200 LYS 200 200 200 LYS LYS A . n A 1 201 VAL 201 201 201 VAL VAL A . n A 1 202 ALA 202 202 202 ALA ALA A . n A 1 203 ALA 203 203 203 ALA ALA A . n A 1 204 CYS 204 204 204 CYS CYS A . n A 1 205 ALA 205 205 205 ALA ALA A . n A 1 206 LYS 206 206 206 LYS LYS A . n A 1 207 HIS 207 207 207 HIS HIS A . n A 1 208 PHE 208 208 208 PHE PHE A . n A 1 209 VAL 209 209 209 VAL VAL A . n A 1 210 GLY 210 210 210 GLY GLY A . n A 1 211 ASP 211 211 211 ASP ASP A . n A 1 212 GLY 212 212 212 GLY GLY A . n A 1 213 GLY 213 213 213 GLY GLY A . n A 1 214 THR 214 214 214 THR THR A . n A 1 215 VAL 215 215 215 VAL VAL A . n A 1 216 ASP 216 216 216 ASP ASP A . n A 1 217 GLY 217 217 217 GLY GLY A . n A 1 218 ILE 218 218 218 ILE ILE A . n A 1 219 ASN 219 219 219 ASN ASN A . n A 1 220 GLU 220 220 220 GLU GLU A . n A 1 221 ASN 221 221 221 ASN ASN A . n A 1 222 ASN 222 222 222 ASN ASN A . n A 1 223 THR 223 223 223 THR THR A . n A 1 224 ILE 224 224 224 ILE ILE A . n A 1 225 ILE 225 225 225 ILE ILE A . n A 1 226 ASN 226 226 226 ASN ASN A . n A 1 227 ARG 227 227 227 ARG ARG A . n A 1 228 GLU 228 228 228 GLU GLU A . n A 1 229 GLY 229 229 229 GLY GLY A . n A 1 230 LEU 230 230 230 LEU LEU A . n A 1 231 MET 231 231 231 MET MET A . n A 1 232 ASN 232 232 232 ASN ASN A . n A 1 233 ILE 233 233 233 ILE ILE A . n A 1 234 HIS 234 234 234 HIS HIS A . n A 1 235 MET 235 235 235 MET MET A . n A 1 236 PRO 236 236 236 PRO PRO A . n A 1 237 ALA 237 237 237 ALA ALA A . n A 1 238 TYR 238 238 238 TYR TYR A . n A 1 239 LYS 239 239 239 LYS LYS A . n A 1 240 ASN 240 240 240 ASN ASN A . n A 1 241 ALA 241 241 241 ALA ALA A . n A 1 242 MET 242 242 242 MET MET A . n A 1 243 ASP 243 243 243 ASP ASP A . n A 1 244 LYS 244 244 244 LYS LYS A . n A 1 245 GLY 245 245 245 GLY GLY A . n A 1 246 VAL 246 246 246 VAL VAL A . n A 1 247 SER 247 247 247 SER SER A . n A 1 248 THR 248 248 248 THR THR A . n A 1 249 VAL 249 249 249 VAL VAL A . n A 1 250 MET 250 250 250 MET MET A . n A 1 251 ILE 251 251 251 ILE ILE A . n A 1 252 SER 252 252 252 SER SER A . n A 1 253 TYR 253 253 253 TYR TYR A . n A 1 254 SER 254 254 254 SER SER A . n A 1 255 SER 255 255 255 SER SER A . n A 1 256 TRP 256 256 256 TRP TRP A . n A 1 257 ASN 257 257 257 ASN ASN A . n A 1 258 GLY 258 258 258 GLY GLY A . n A 1 259 VAL 259 259 259 VAL VAL A . n A 1 260 LYS 260 260 260 LYS LYS A . n A 1 261 MET 261 261 261 MET MET A . n A 1 262 HIS 262 262 262 HIS HIS A . n A 1 263 ALA 263 263 263 ALA ALA A . n A 1 264 ASN 264 264 264 ASN ASN A . n A 1 265 GLN 265 265 265 GLN GLN A . n A 1 266 ASP 266 266 266 ASP ASP A . n A 1 267 LEU 267 267 267 LEU LEU A . n A 1 268 VAL 268 268 268 VAL VAL A . n A 1 269 THR 269 269 269 THR THR A . n A 1 270 GLY 270 270 270 GLY GLY A . n A 1 271 TYR 271 271 271 TYR TYR A . n A 1 272 LEU 272 272 272 LEU LEU A . n A 1 273 LYS 273 273 273 LYS LYS A . n A 1 274 ASP 274 274 274 ASP ASP A . n A 1 275 THR 275 275 275 THR THR A . n A 1 276 LEU 276 276 276 LEU LEU A . n A 1 277 LYS 277 277 277 LYS LYS A . n A 1 278 PHE 278 278 278 PHE PHE A . n A 1 279 LYS 279 279 279 LYS LYS A . n A 1 280 GLY 280 280 280 GLY GLY A . n A 1 281 PHE 281 281 281 PHE PHE A . n A 1 282 VAL 282 282 282 VAL VAL A . n A 1 283 ILE 283 283 283 ILE ILE A . n A 1 284 SER 284 284 284 SER SER A . n A 1 285 ASP 285 285 285 ASP ASP A . n A 1 286 TRP 286 286 286 TRP TRP A . n A 1 287 GLU 287 287 287 GLU GLU A . n A 1 288 GLY 288 288 288 GLY GLY A . n A 1 289 ILE 289 289 289 ILE ILE A . n A 1 290 ASP 290 290 290 ASP ASP A . n A 1 291 ARG 291 291 291 ARG ARG A . n A 1 292 ILE 292 292 292 ILE ILE A . n A 1 293 THR 293 293 293 THR THR A . n A 1 294 THR 294 294 294 THR THR A . n A 1 295 PRO 295 295 295 PRO PRO A . n A 1 296 ALA 296 296 296 ALA ALA A . n A 1 297 GLY 297 297 297 GLY GLY A . n A 1 298 SER 298 298 298 SER SER A . n A 1 299 ASP 299 299 299 ASP ASP A . n A 1 300 TYR 300 300 300 TYR TYR A . n A 1 301 SER 301 301 301 SER SER A . n A 1 302 TYR 302 302 302 TYR TYR A . n A 1 303 SER 303 303 303 SER SER A . n A 1 304 VAL 304 304 304 VAL VAL A . n A 1 305 LYS 305 305 305 LYS LYS A . n A 1 306 ALA 306 306 306 ALA ALA A . n A 1 307 SER 307 307 307 SER SER A . n A 1 308 ILE 308 308 308 ILE ILE A . n A 1 309 LEU 309 309 309 LEU LEU A . n A 1 310 ALA 310 310 310 ALA ALA A . n A 1 311 GLY 311 311 311 GLY GLY A . n A 1 312 LEU 312 312 312 LEU LEU A . n A 1 313 ASP 313 313 313 ASP ASP A . n A 1 314 MET 314 314 314 MET MET A . n A 1 315 ILE 315 315 315 ILE ILE A . n A 1 316 MET 316 316 316 MET MET A . n A 1 317 VAL 317 317 317 VAL VAL A . n A 1 318 PRO 318 318 318 PRO PRO A . n A 1 319 ASN 319 319 319 ASN ASN A . n A 1 320 LYS 320 320 320 LYS LYS A . n A 1 321 TYR 321 321 321 TYR TYR A . n A 1 322 GLN 322 322 322 GLN GLN A . n A 1 323 GLN 323 323 323 GLN GLN A . n A 1 324 PHE 324 324 324 PHE PHE A . n A 1 325 ILE 325 325 325 ILE ILE A . n A 1 326 SER 326 326 326 SER SER A . n A 1 327 ILE 327 327 327 ILE ILE A . n A 1 328 LEU 328 328 328 LEU LEU A . n A 1 329 THR 329 329 329 THR THR A . n A 1 330 GLY 330 330 330 GLY GLY A . n A 1 331 HIS 331 331 331 HIS HIS A . n A 1 332 VAL 332 332 332 VAL VAL A . n A 1 333 ASN 333 333 333 ASN ASN A . n A 1 334 GLY 334 334 334 GLY GLY A . n A 1 335 GLY 335 335 335 GLY GLY A . n A 1 336 VAL 336 336 336 VAL VAL A . n A 1 337 ILE 337 337 337 ILE ILE A . n A 1 338 PRO 338 338 338 PRO PRO A . n A 1 339 MET 339 339 339 MET MET A . n A 1 340 SER 340 340 340 SER SER A . n A 1 341 ARG 341 341 341 ARG ARG A . n A 1 342 ILE 342 342 342 ILE ILE A . n A 1 343 ASP 343 343 343 ASP ASP A . n A 1 344 ASP 344 344 344 ASP ASP A . n A 1 345 ALA 345 345 345 ALA ALA A . n A 1 346 VAL 346 346 346 VAL VAL A . n A 1 347 THR 347 347 347 THR THR A . n A 1 348 ARG 348 348 348 ARG ARG A . n A 1 349 ILE 349 349 349 ILE ILE A . n A 1 350 LEU 350 350 350 LEU LEU A . n A 1 351 ARG 351 351 351 ARG ARG A . n A 1 352 VAL 352 352 352 VAL VAL A . n A 1 353 LYS 353 353 353 LYS LYS A . n A 1 354 PHE 354 354 354 PHE PHE A . n A 1 355 THR 355 355 355 THR THR A . n A 1 356 MET 356 356 356 MET MET A . n A 1 357 GLY 357 357 357 GLY GLY A . n A 1 358 LEU 358 358 358 LEU LEU A . n A 1 359 PHE 359 359 359 PHE PHE A . n A 1 360 GLU 360 360 360 GLU GLU A . n A 1 361 ASN 361 361 361 ASN ASN A . n A 1 362 PRO 362 362 362 PRO PRO A . n A 1 363 TYR 363 363 363 TYR TYR A . n A 1 364 ALA 364 364 364 ALA ALA A . n A 1 365 ASP 365 365 365 ASP ASP A . n A 1 366 PRO 366 366 366 PRO PRO A . n A 1 367 ALA 367 367 367 ALA ALA A . n A 1 368 MET 368 368 368 MET MET A . n A 1 369 ALA 369 369 369 ALA ALA A . n A 1 370 GLU 370 370 370 GLU GLU A . n A 1 371 GLN 371 371 371 GLN GLN A . n A 1 372 LEU 372 372 372 LEU LEU A . n A 1 373 GLY 373 373 373 GLY GLY A . n A 1 374 LYS 374 374 374 LYS LYS A . n A 1 375 GLN 375 375 375 GLN GLN A . n A 1 376 GLU 376 376 376 GLU GLU A . n A 1 377 HIS 377 377 377 HIS HIS A . n A 1 378 ARG 378 378 378 ARG ARG A . n A 1 379 ASP 379 379 379 ASP ASP A . n A 1 380 LEU 380 380 380 LEU LEU A . n A 1 381 ALA 381 381 381 ALA ALA A . n A 1 382 ARG 382 382 382 ARG ARG A . n A 1 383 GLU 383 383 383 GLU GLU A . n A 1 384 ALA 384 384 384 ALA ALA A . n A 1 385 ALA 385 385 385 ALA ALA A . n A 1 386 ARG 386 386 386 ARG ARG A . n A 1 387 LYS 387 387 387 LYS LYS A . n A 1 388 SER 388 388 388 SER SER A . n A 1 389 LEU 389 389 389 LEU LEU A . n A 1 390 VAL 390 390 390 VAL VAL A . n A 1 391 LEU 391 391 391 LEU LEU A . n A 1 392 LEU 392 392 392 LEU LEU A . n A 1 393 LYS 393 393 393 LYS LYS A . n A 1 394 ASN 394 394 394 ASN ASN A . n A 1 395 GLY 395 395 395 GLY GLY A . n A 1 396 LYS 396 396 396 LYS LYS A . n A 1 397 THR 397 397 397 THR THR A . n A 1 398 SER 398 398 398 SER SER A . n A 1 399 THR 399 399 399 THR THR A . n A 1 400 ASP 400 400 400 ASP ASP A . n A 1 401 ALA 401 401 401 ALA ALA A . n A 1 402 PRO 402 402 402 PRO PRO A . n A 1 403 LEU 403 403 403 LEU LEU A . n A 1 404 LEU 404 404 404 LEU LEU A . n A 1 405 PRO 405 405 405 PRO PRO A . n A 1 406 LEU 406 406 406 LEU LEU A . n A 1 407 PRO 407 407 407 PRO PRO A . n A 1 408 LYS 408 408 408 LYS LYS A . n A 1 409 LYS 409 409 409 LYS LYS A . n A 1 410 ALA 410 410 410 ALA ALA A . n A 1 411 PRO 411 411 411 PRO PRO A . n A 1 412 LYS 412 412 412 LYS LYS A . n A 1 413 ILE 413 413 413 ILE ILE A . n A 1 414 LEU 414 414 414 LEU LEU A . n A 1 415 VAL 415 415 415 VAL VAL A . n A 1 416 ALA 416 416 416 ALA ALA A . n A 1 417 GLY 417 417 417 GLY GLY A . n A 1 418 SER 418 418 418 SER SER A . n A 1 419 HIS 419 419 419 HIS HIS A . n A 1 420 ALA 420 420 420 ALA ALA A . n A 1 421 ASP 421 421 421 ASP ASP A . n A 1 422 ASN 422 422 422 ASN ASN A . n A 1 423 LEU 423 423 423 LEU LEU A . n A 1 424 GLY 424 424 424 GLY GLY A . n A 1 425 TYR 425 425 425 TYR TYR A . n A 1 426 GLN 426 426 426 GLN GLN A . n A 1 427 CYS 427 427 427 CYS CYS A . n A 1 428 GLY 428 428 428 GLY GLY A . n A 1 429 GLY 429 429 429 GLY GLY A . n A 1 430 TRP 430 430 430 TRP TRP A . n A 1 431 THR 431 431 431 THR THR A . n A 1 432 ILE 432 432 432 ILE ILE A . n A 1 433 GLU 433 433 433 GLU GLU A . n A 1 434 TRP 434 434 434 TRP TRP A . n A 1 435 GLN 435 435 435 GLN GLN A . n A 1 436 GLY 436 436 436 GLY GLY A . n A 1 437 ASP 437 437 437 ASP ASP A . n A 1 438 THR 438 438 438 THR THR A . n A 1 439 GLY 439 439 439 GLY GLY A . n A 1 440 ARG 440 440 440 ARG ARG A . n A 1 441 THR 441 441 441 THR THR A . n A 1 442 THR 442 442 442 THR THR A . n A 1 443 VAL 443 443 443 VAL VAL A . n A 1 444 GLY 444 444 444 GLY GLY A . n A 1 445 THR 445 445 445 THR THR A . n A 1 446 THR 446 446 446 THR THR A . n A 1 447 ILE 447 447 447 ILE ILE A . n A 1 448 LEU 448 448 448 LEU LEU A . n A 1 449 GLU 449 449 449 GLU GLU A . n A 1 450 ALA 450 450 450 ALA ALA A . n A 1 451 VAL 451 451 451 VAL VAL A . n A 1 452 LYS 452 452 452 LYS LYS A . n A 1 453 ALA 453 453 453 ALA ALA A . n A 1 454 ALA 454 454 454 ALA ALA A . n A 1 455 VAL 455 455 455 VAL VAL A . n A 1 456 ASP 456 456 456 ASP ASP A . n A 1 457 PRO 457 457 457 PRO PRO A . n A 1 458 SER 458 458 458 SER SER A . n A 1 459 THR 459 459 459 THR THR A . n A 1 460 VAL 460 460 460 VAL VAL A . n A 1 461 VAL 461 461 461 VAL VAL A . n A 1 462 VAL 462 462 462 VAL VAL A . n A 1 463 PHE 463 463 463 PHE PHE A . n A 1 464 ALA 464 464 464 ALA ALA A . n A 1 465 GLU 465 465 465 GLU GLU A . n A 1 466 ASN 466 466 466 ASN ASN A . n A 1 467 PRO 467 467 467 PRO PRO A . n A 1 468 ASP 468 468 468 ASP ASP A . n A 1 469 ALA 469 469 469 ALA ALA A . n A 1 470 GLU 470 470 470 GLU GLU A . n A 1 471 PHE 471 471 471 PHE PHE A . n A 1 472 VAL 472 472 472 VAL VAL A . n A 1 473 LYS 473 473 473 LYS LYS A . n A 1 474 SER 474 474 474 SER SER A . n A 1 475 GLY 475 475 475 GLY GLY A . n A 1 476 GLY 476 476 476 GLY GLY A . n A 1 477 PHE 477 477 477 PHE PHE A . n A 1 478 SER 478 478 478 SER SER A . n A 1 479 TYR 479 479 479 TYR TYR A . n A 1 480 ALA 480 480 480 ALA ALA A . n A 1 481 ILE 481 481 481 ILE ILE A . n A 1 482 VAL 482 482 482 VAL VAL A . n A 1 483 ALA 483 483 483 ALA ALA A . n A 1 484 VAL 484 484 484 VAL VAL A . n A 1 485 GLY 485 485 485 GLY GLY A . n A 1 486 GLU 486 486 486 GLU GLU A . n A 1 487 HIS 487 487 487 HIS HIS A . n A 1 488 PRO 488 488 488 PRO PRO A . n A 1 489 TYR 489 489 489 TYR TYR A . n A 1 490 THR 490 490 490 THR THR A . n A 1 491 GLU 491 491 491 GLU GLU A . n A 1 492 THR 492 492 492 THR THR A . n A 1 493 LYS 493 493 493 LYS LYS A . n A 1 494 GLY 494 494 494 GLY GLY A . n A 1 495 ASP 495 495 495 ASP ASP A . n A 1 496 ASN 496 496 496 ASN ASN A . n A 1 497 LEU 497 497 497 LEU LEU A . n A 1 498 ASN 498 498 498 ASN ASN A . n A 1 499 LEU 499 499 499 LEU LEU A . n A 1 500 THR 500 500 500 THR THR A . n A 1 501 ILE 501 501 501 ILE ILE A . n A 1 502 PRO 502 502 502 PRO PRO A . n A 1 503 GLU 503 503 503 GLU GLU A . n A 1 504 PRO 504 504 504 PRO PRO A . n A 1 505 GLY 505 505 505 GLY GLY A . n A 1 506 LEU 506 506 506 LEU LEU A . n A 1 507 SER 507 507 507 SER SER A . n A 1 508 THR 508 508 508 THR THR A . n A 1 509 VAL 509 509 509 VAL VAL A . n A 1 510 GLN 510 510 510 GLN GLN A . n A 1 511 ALA 511 511 511 ALA ALA A . n A 1 512 VAL 512 512 512 VAL VAL A . n A 1 513 CYS 513 513 513 CYS CYS A . n A 1 514 GLY 514 514 514 GLY GLY A . n A 1 515 GLY 515 515 515 GLY GLY A . n A 1 516 VAL 516 516 516 VAL VAL A . n A 1 517 ARG 517 517 517 ARG ARG A . n A 1 518 CYS 518 518 518 CYS CYS A . n A 1 519 ALA 519 519 519 ALA ALA A . n A 1 520 THR 520 520 520 THR THR A . n A 1 521 VAL 521 521 521 VAL VAL A . n A 1 522 LEU 522 522 522 LEU LEU A . n A 1 523 ILE 523 523 523 ILE ILE A . n A 1 524 SER 524 524 524 SER SER A . n A 1 525 GLY 525 525 525 GLY GLY A . n A 1 526 ARG 526 526 526 ARG ARG A . n A 1 527 PRO 527 527 527 PRO PRO A . n A 1 528 VAL 528 528 528 VAL VAL A . n A 1 529 VAL 529 529 529 VAL VAL A . n A 1 530 VAL 530 530 530 VAL VAL A . n A 1 531 GLN 531 531 531 GLN GLN A . n A 1 532 PRO 532 532 532 PRO PRO A . n A 1 533 LEU 533 533 533 LEU LEU A . n A 1 534 LEU 534 534 534 LEU LEU A . n A 1 535 ALA 535 535 535 ALA ALA A . n A 1 536 ALA 536 536 536 ALA ALA A . n A 1 537 SER 537 537 537 SER SER A . n A 1 538 ASP 538 538 538 ASP ASP A . n A 1 539 ALA 539 539 539 ALA ALA A . n A 1 540 LEU 540 540 540 LEU LEU A . n A 1 541 VAL 541 541 541 VAL VAL A . n A 1 542 ALA 542 542 542 ALA ALA A . n A 1 543 ALA 543 543 543 ALA ALA A . n A 1 544 TRP 544 544 544 TRP TRP A . n A 1 545 LEU 545 545 545 LEU LEU A . n A 1 546 PRO 546 546 546 PRO PRO A . n A 1 547 GLY 547 547 547 GLY GLY A . n A 1 548 SER 548 548 548 SER SER A . n A 1 549 GLU 549 549 549 GLU GLU A . n A 1 550 GLY 550 550 550 GLY GLY A . n A 1 551 GLN 551 551 551 GLN GLN A . n A 1 552 GLY 552 552 552 GLY GLY A . n A 1 553 VAL 553 553 553 VAL VAL A . n A 1 554 THR 554 554 554 THR THR A . n A 1 555 ASP 555 555 555 ASP ASP A . n A 1 556 ALA 556 556 556 ALA ALA A . n A 1 557 LEU 557 557 557 LEU LEU A . n A 1 558 PHE 558 558 558 PHE PHE A . n A 1 559 GLY 559 559 559 GLY GLY A . n A 1 560 ASP 560 560 560 ASP ASP A . n A 1 561 PHE 561 561 561 PHE PHE A . n A 1 562 GLY 562 562 562 GLY GLY A . n A 1 563 PHE 563 563 563 PHE PHE A . n A 1 564 THR 564 564 564 THR THR A . n A 1 565 GLY 565 565 565 GLY GLY A . n A 1 566 ARG 566 566 566 ARG ARG A . n A 1 567 LEU 567 567 567 LEU LEU A . n A 1 568 PRO 568 568 568 PRO PRO A . n A 1 569 ARG 569 569 569 ARG ARG A . n A 1 570 THR 570 570 570 THR THR A . n A 1 571 TRP 571 571 571 TRP TRP A . n A 1 572 PHE 572 572 572 PHE PHE A . n A 1 573 LYS 573 573 573 LYS LYS A . n A 1 574 SER 574 574 574 SER SER A . n A 1 575 VAL 575 575 575 VAL VAL A . n A 1 576 ASP 576 576 576 ASP ASP A . n A 1 577 GLN 577 577 577 GLN GLN A . n A 1 578 LEU 578 578 578 LEU LEU A . n A 1 579 PRO 579 579 579 PRO PRO A . n A 1 580 MET 580 580 580 MET MET A . n A 1 581 ASN 581 581 581 ASN ASN A . n A 1 582 VAL 582 582 582 VAL VAL A . n A 1 583 GLY 583 583 583 GLY GLY A . n A 1 584 ASP 584 584 584 ASP ASP A . n A 1 585 ALA 585 585 585 ALA ALA A . n A 1 586 HIS 586 586 586 HIS HIS A . n A 1 587 TYR 587 587 587 TYR TYR A . n A 1 588 ASP 588 588 588 ASP ASP A . n A 1 589 PRO 589 589 589 PRO PRO A . n A 1 590 LEU 590 590 590 LEU LEU A . n A 1 591 PHE 591 591 591 PHE PHE A . n A 1 592 ARG 592 592 592 ARG ARG A . n A 1 593 LEU 593 593 593 LEU LEU A . n A 1 594 GLY 594 594 594 GLY GLY A . n A 1 595 TYR 595 595 595 TYR TYR A . n A 1 596 GLY 596 596 596 GLY GLY A . n A 1 597 LEU 597 597 597 LEU LEU A . n A 1 598 THR 598 598 598 THR THR A . n A 1 599 THR 599 599 599 THR THR A . n A 1 600 ASN 600 600 600 ASN ASN A . n A 1 601 ALA 601 601 601 ALA ALA A . n A 1 602 THR 602 602 602 THR THR A . n A 1 603 LYS 603 603 ? ? ? A . n A 1 604 LYS 604 604 ? ? ? A . n A 1 605 TYR 605 605 ? ? ? A . n # _pdbx_struct_mod_residue.id 1 _pdbx_struct_mod_residue.label_asym_id A _pdbx_struct_mod_residue.label_comp_id ASN _pdbx_struct_mod_residue.label_seq_id 600 _pdbx_struct_mod_residue.auth_asym_id A _pdbx_struct_mod_residue.auth_comp_id ASN _pdbx_struct_mod_residue.auth_seq_id 600 _pdbx_struct_mod_residue.PDB_ins_code ? _pdbx_struct_mod_residue.parent_comp_id ASN _pdbx_struct_mod_residue.details '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 # _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 24.0650 16.1630 29.7520 0.0108 0.0255 0.0201 0.0068 0.0123 0.0137 0.2874 0.0438 0.3489 -0.0981 -0.1914 0.1108 -0.0496 -0.0223 -0.0436 0.0164 0.0206 0.0180 0.0244 0.0628 0.0290 'X-RAY DIFFRACTION' 2 ? refined 2.6270 31.4930 51.4580 0.0072 0.0301 0.0210 0.0053 0.0004 -0.0083 0.2641 0.0905 0.3329 -0.1336 -0.2188 0.1498 -0.0293 -0.0386 0.0213 0.0133 0.0064 0.0073 0.0216 0.0484 0.0229 # 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 1 ? ? A 357 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 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 5.7.0032 ? 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 3WLP # 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 O1 A GOL 708 ? ? O3 A GOL 709 ? ? 2.00 2 1 O A HOH 847 ? ? O A HOH 848 ? ? 2.01 3 1 ND2 A ASN 466 ? A OG1 A THR 508 ? ? 2.10 4 1 CD A LYS 68 ? A O A HOH 1177 ? ? 2.13 5 1 O A HOH 1273 ? ? O A HOH 1627 ? ? 2.15 # loop_ _pdbx_validate_symm_contact.id _pdbx_validate_symm_contact.PDB_model_num _pdbx_validate_symm_contact.auth_atom_id_1 _pdbx_validate_symm_contact.auth_asym_id_1 _pdbx_validate_symm_contact.auth_comp_id_1 _pdbx_validate_symm_contact.auth_seq_id_1 _pdbx_validate_symm_contact.PDB_ins_code_1 _pdbx_validate_symm_contact.label_alt_id_1 _pdbx_validate_symm_contact.site_symmetry_1 _pdbx_validate_symm_contact.auth_atom_id_2 _pdbx_validate_symm_contact.auth_asym_id_2 _pdbx_validate_symm_contact.auth_comp_id_2 _pdbx_validate_symm_contact.auth_seq_id_2 _pdbx_validate_symm_contact.PDB_ins_code_2 _pdbx_validate_symm_contact.label_alt_id_2 _pdbx_validate_symm_contact.site_symmetry_2 _pdbx_validate_symm_contact.dist 1 1 O A HOH 808 ? ? 1_555 O A HOH 1056 ? ? 6_555 1.23 2 1 O A HOH 961 ? ? 1_555 O A HOH 1196 ? ? 3_554 1.44 3 1 O A HOH 962 ? ? 1_555 O A HOH 1163 ? ? 3_554 1.48 4 1 O A HOH 962 ? ? 1_555 O A HOH 1383 ? ? 3_554 2.16 5 1 O A HOH 944 ? ? 1_555 O A HOH 1330 ? ? 8_655 2.17 # 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 126 ? ? CZ A ARG 126 ? ? NH1 A ARG 126 ? ? 127.40 120.30 7.10 0.50 N 2 1 NE A ARG 126 ? ? CZ A ARG 126 ? ? NH2 A ARG 126 ? ? 112.86 120.30 -7.44 0.50 N 3 1 CB A ASN 333 ? B CA A ASN 333 ? ? C A ASN 333 ? ? 122.86 110.40 12.46 2.00 N 4 1 NE A ARG 351 ? ? CZ A ARG 351 ? ? NH1 A ARG 351 ? ? 125.23 120.30 4.93 0.50 N 5 1 NE A ARG 351 ? ? CZ A ARG 351 ? ? NH2 A ARG 351 ? ? 117.29 120.30 -3.01 0.50 N 6 1 CB A TYR 425 ? ? CG A TYR 425 ? ? CD2 A TYR 425 ? ? 117.18 121.00 -3.82 0.60 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 98 ? ? -152.61 65.50 2 1 ASN A 221 ? ? -136.18 -150.38 3 1 TYR A 271 ? ? -98.10 -62.92 4 1 ASP A 299 ? ? -150.80 77.60 5 1 ASN A 394 ? ? -150.24 64.33 6 1 ILE A 432 ? ? 70.69 -57.07 7 1 THR A 442 ? ? -161.63 -168.21 8 1 LYS A 493 ? ? 111.34 -18.74 9 1 TRP A 544 ? ? 57.22 -134.99 10 1 ASP A 588 ? ? -151.97 77.86 # _pdbx_validate_peptide_omega.id 1 _pdbx_validate_peptide_omega.PDB_model_num 1 _pdbx_validate_peptide_omega.auth_comp_id_1 GLY _pdbx_validate_peptide_omega.auth_asym_id_1 A _pdbx_validate_peptide_omega.auth_seq_id_1 213 _pdbx_validate_peptide_omega.PDB_ins_code_1 ? _pdbx_validate_peptide_omega.label_alt_id_1 ? _pdbx_validate_peptide_omega.auth_comp_id_2 THR _pdbx_validate_peptide_omega.auth_asym_id_2 A _pdbx_validate_peptide_omega.auth_seq_id_2 214 _pdbx_validate_peptide_omega.PDB_ins_code_2 ? _pdbx_validate_peptide_omega.label_alt_id_2 ? _pdbx_validate_peptide_omega.omega -143.51 # 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 603 2 1 Y 1 A LYS 604 ? A LYS 604 3 1 Y 1 A TYR 605 ? A TYR 605 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 1-THIO-BETA-D-GLUCOPYRANOSE GS1 4 O1-METHYL-GLUCOSE MGL 5 GLYCEROL GOL 6 'SULFATE ION' SO4 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 3 GS1 1 702 1 GS1 G6S A . D 4 MGL 2 703 1 MGL G6S A . E 5 GOL 1 704 1 GOL GOL A . F 5 GOL 1 705 2 GOL GOL A . G 5 GOL 1 706 3 GOL GOL A . H 5 GOL 1 707 4 GOL GOL A . I 5 GOL 1 708 5 GOL GOL A . J 5 GOL 1 709 6 GOL GOL A . K 5 GOL 1 710 7 GOL GOL A . L 5 GOL 1 711 8 GOL GOL A . M 5 GOL 1 712 9 GOL GOL A . N 5 GOL 1 713 10 GOL GOL A . O 6 SO4 1 714 1 SO4 SO4 A . P 6 SO4 1 715 2 SO4 SO4 A . Q 7 HOH 1 801 1 HOH HOH A . Q 7 HOH 2 802 2 HOH HOH A . Q 7 HOH 3 803 3 HOH HOH A . Q 7 HOH 4 804 4 HOH HOH A . Q 7 HOH 5 805 5 HOH HOH A . Q 7 HOH 6 806 6 HOH HOH A . Q 7 HOH 7 807 7 HOH HOH A . Q 7 HOH 8 808 8 HOH HOH A . Q 7 HOH 9 809 9 HOH HOH A . Q 7 HOH 10 810 10 HOH HOH A . Q 7 HOH 11 811 11 HOH HOH A . Q 7 HOH 12 812 12 HOH HOH A . Q 7 HOH 13 813 13 HOH HOH A . Q 7 HOH 14 814 14 HOH HOH A . Q 7 HOH 15 815 15 HOH HOH A . Q 7 HOH 16 816 16 HOH HOH A . Q 7 HOH 17 817 17 HOH HOH A . Q 7 HOH 18 818 18 HOH HOH A . Q 7 HOH 19 819 19 HOH HOH A . Q 7 HOH 20 820 20 HOH HOH A . Q 7 HOH 21 821 21 HOH HOH A . Q 7 HOH 22 822 22 HOH HOH A . Q 7 HOH 23 823 23 HOH HOH A . Q 7 HOH 24 824 24 HOH HOH A . Q 7 HOH 25 825 25 HOH HOH A . Q 7 HOH 26 826 26 HOH HOH A . Q 7 HOH 27 827 27 HOH HOH A . Q 7 HOH 28 828 28 HOH HOH A . Q 7 HOH 29 829 29 HOH HOH A . Q 7 HOH 30 830 30 HOH HOH A . Q 7 HOH 31 831 31 HOH HOH A . Q 7 HOH 32 832 32 HOH HOH A . Q 7 HOH 33 833 33 HOH HOH A . Q 7 HOH 34 834 34 HOH HOH A . Q 7 HOH 35 835 35 HOH HOH A . Q 7 HOH 36 836 36 HOH HOH A . Q 7 HOH 37 837 37 HOH HOH A . Q 7 HOH 38 838 38 HOH HOH A . Q 7 HOH 39 839 39 HOH HOH A . Q 7 HOH 40 840 40 HOH HOH A . Q 7 HOH 41 841 41 HOH HOH A . Q 7 HOH 42 842 42 HOH HOH A . Q 7 HOH 43 843 43 HOH HOH A . Q 7 HOH 44 844 44 HOH HOH A . Q 7 HOH 45 845 45 HOH HOH A . Q 7 HOH 46 846 46 HOH HOH A . Q 7 HOH 47 847 47 HOH HOH A . Q 7 HOH 48 848 48 HOH HOH A . Q 7 HOH 49 849 49 HOH HOH A . Q 7 HOH 50 850 50 HOH HOH A . Q 7 HOH 51 851 51 HOH HOH A . Q 7 HOH 52 852 52 HOH HOH A . Q 7 HOH 53 853 53 HOH HOH A . Q 7 HOH 54 854 54 HOH HOH A . Q 7 HOH 55 855 55 HOH HOH A . Q 7 HOH 56 856 56 HOH HOH A . Q 7 HOH 57 857 57 HOH HOH A . Q 7 HOH 58 858 58 HOH HOH A . Q 7 HOH 59 859 59 HOH HOH A . Q 7 HOH 60 860 60 HOH HOH A . Q 7 HOH 61 861 61 HOH HOH A . Q 7 HOH 62 862 62 HOH HOH A . Q 7 HOH 63 863 63 HOH HOH A . Q 7 HOH 64 864 64 HOH HOH A . Q 7 HOH 65 865 65 HOH HOH A . Q 7 HOH 66 866 66 HOH HOH A . Q 7 HOH 67 867 67 HOH HOH A . Q 7 HOH 68 868 68 HOH HOH A . Q 7 HOH 69 869 69 HOH HOH A . Q 7 HOH 70 870 70 HOH HOH A . Q 7 HOH 71 871 71 HOH HOH A . Q 7 HOH 72 872 72 HOH HOH A . Q 7 HOH 73 873 73 HOH HOH A . Q 7 HOH 74 874 74 HOH HOH A . Q 7 HOH 75 875 75 HOH HOH A . Q 7 HOH 76 876 76 HOH HOH A . Q 7 HOH 77 877 77 HOH HOH A . Q 7 HOH 78 878 78 HOH HOH A . Q 7 HOH 79 879 79 HOH HOH A . Q 7 HOH 80 880 80 HOH HOH A . Q 7 HOH 81 881 81 HOH HOH A . Q 7 HOH 82 882 82 HOH HOH A . Q 7 HOH 83 883 83 HOH HOH A . Q 7 HOH 84 884 84 HOH HOH A . Q 7 HOH 85 885 85 HOH HOH A . Q 7 HOH 86 886 86 HOH HOH A . Q 7 HOH 87 887 87 HOH HOH A . Q 7 HOH 88 888 88 HOH HOH A . Q 7 HOH 89 889 89 HOH HOH A . Q 7 HOH 90 890 90 HOH HOH A . Q 7 HOH 91 891 91 HOH HOH A . Q 7 HOH 92 892 92 HOH HOH A . Q 7 HOH 93 893 93 HOH HOH A . Q 7 HOH 94 894 94 HOH HOH A . Q 7 HOH 95 895 95 HOH HOH A . Q 7 HOH 96 896 96 HOH HOH A . Q 7 HOH 97 897 97 HOH HOH A . Q 7 HOH 98 898 98 HOH HOH A . Q 7 HOH 99 899 99 HOH HOH A . Q 7 HOH 100 900 100 HOH HOH A . Q 7 HOH 101 901 101 HOH HOH A . Q 7 HOH 102 902 102 HOH HOH A . Q 7 HOH 103 903 103 HOH HOH A . Q 7 HOH 104 904 104 HOH HOH A . Q 7 HOH 105 905 105 HOH HOH A . Q 7 HOH 106 906 106 HOH HOH A . Q 7 HOH 107 907 107 HOH HOH A . Q 7 HOH 108 908 108 HOH HOH A . Q 7 HOH 109 909 109 HOH HOH A . Q 7 HOH 110 910 110 HOH HOH A . Q 7 HOH 111 911 111 HOH HOH A . Q 7 HOH 112 912 112 HOH HOH A . Q 7 HOH 113 913 113 HOH HOH A . Q 7 HOH 114 914 114 HOH HOH A . Q 7 HOH 115 915 115 HOH HOH A . Q 7 HOH 116 916 116 HOH HOH A . Q 7 HOH 117 917 117 HOH HOH A . Q 7 HOH 118 918 118 HOH HOH A . Q 7 HOH 119 919 119 HOH HOH A . Q 7 HOH 120 920 120 HOH HOH A . Q 7 HOH 121 921 121 HOH HOH A . Q 7 HOH 122 922 122 HOH HOH A . Q 7 HOH 123 923 123 HOH HOH A . Q 7 HOH 124 924 124 HOH HOH A . Q 7 HOH 125 925 125 HOH HOH A . Q 7 HOH 126 926 126 HOH HOH A . Q 7 HOH 127 927 127 HOH HOH A . Q 7 HOH 128 928 128 HOH HOH A . Q 7 HOH 129 929 129 HOH HOH A . Q 7 HOH 130 930 130 HOH HOH A . Q 7 HOH 131 931 131 HOH HOH A . Q 7 HOH 132 932 132 HOH HOH A . Q 7 HOH 133 933 133 HOH HOH A . Q 7 HOH 134 934 134 HOH HOH A . Q 7 HOH 135 935 135 HOH HOH A . Q 7 HOH 136 936 136 HOH HOH A . Q 7 HOH 137 937 137 HOH HOH A . Q 7 HOH 138 938 138 HOH HOH A . Q 7 HOH 139 939 139 HOH HOH A . Q 7 HOH 140 940 140 HOH HOH A . Q 7 HOH 141 941 141 HOH HOH A . Q 7 HOH 142 942 142 HOH HOH A . Q 7 HOH 143 943 143 HOH HOH A . Q 7 HOH 144 944 144 HOH HOH A . Q 7 HOH 145 945 145 HOH HOH A . Q 7 HOH 146 946 146 HOH HOH A . Q 7 HOH 147 947 147 HOH HOH A . Q 7 HOH 148 948 148 HOH HOH A . Q 7 HOH 149 949 149 HOH HOH A . Q 7 HOH 150 950 150 HOH HOH A . Q 7 HOH 151 951 151 HOH HOH A . Q 7 HOH 152 952 152 HOH HOH A . Q 7 HOH 153 953 153 HOH HOH A . Q 7 HOH 154 954 154 HOH HOH A . Q 7 HOH 155 955 155 HOH HOH A . Q 7 HOH 156 956 156 HOH HOH A . Q 7 HOH 157 957 157 HOH HOH A . Q 7 HOH 158 958 158 HOH HOH A . Q 7 HOH 159 959 159 HOH HOH A . Q 7 HOH 160 960 160 HOH HOH A . Q 7 HOH 161 961 161 HOH HOH A . Q 7 HOH 162 962 162 HOH HOH A . Q 7 HOH 163 963 163 HOH HOH A . Q 7 HOH 164 964 164 HOH HOH A . Q 7 HOH 165 965 165 HOH HOH A . Q 7 HOH 166 966 166 HOH HOH A . Q 7 HOH 167 967 167 HOH HOH A . Q 7 HOH 168 968 168 HOH HOH A . Q 7 HOH 169 969 169 HOH HOH A . Q 7 HOH 170 970 170 HOH HOH A . Q 7 HOH 171 971 171 HOH HOH A . Q 7 HOH 172 972 172 HOH HOH A . Q 7 HOH 173 973 173 HOH HOH A . Q 7 HOH 174 974 174 HOH HOH A . Q 7 HOH 175 975 175 HOH HOH A . Q 7 HOH 176 976 176 HOH HOH A . Q 7 HOH 177 977 177 HOH HOH A . Q 7 HOH 178 978 178 HOH HOH A . Q 7 HOH 179 979 179 HOH HOH A . Q 7 HOH 180 980 180 HOH HOH A . Q 7 HOH 181 981 181 HOH HOH A . Q 7 HOH 182 982 182 HOH HOH A . Q 7 HOH 183 983 183 HOH HOH A . Q 7 HOH 184 984 184 HOH HOH A . Q 7 HOH 185 985 185 HOH HOH A . Q 7 HOH 186 986 186 HOH HOH A . Q 7 HOH 187 987 187 HOH HOH A . Q 7 HOH 188 988 188 HOH HOH A . Q 7 HOH 189 989 189 HOH HOH A . Q 7 HOH 190 990 190 HOH HOH A . Q 7 HOH 191 991 191 HOH HOH A . Q 7 HOH 192 992 192 HOH HOH A . Q 7 HOH 193 993 193 HOH HOH A . Q 7 HOH 194 994 194 HOH HOH A . Q 7 HOH 195 995 195 HOH HOH A . Q 7 HOH 196 996 196 HOH HOH A . Q 7 HOH 197 997 197 HOH HOH A . Q 7 HOH 198 998 198 HOH HOH A . Q 7 HOH 199 999 199 HOH HOH A . Q 7 HOH 200 1000 200 HOH HOH A . Q 7 HOH 201 1001 201 HOH HOH A . Q 7 HOH 202 1002 202 HOH HOH A . Q 7 HOH 203 1003 203 HOH HOH A . Q 7 HOH 204 1004 204 HOH HOH A . Q 7 HOH 205 1005 205 HOH HOH A . Q 7 HOH 206 1006 206 HOH HOH A . Q 7 HOH 207 1007 207 HOH HOH A . Q 7 HOH 208 1008 208 HOH HOH A . Q 7 HOH 209 1009 209 HOH HOH A . Q 7 HOH 210 1010 210 HOH HOH A . Q 7 HOH 211 1011 211 HOH HOH A . Q 7 HOH 212 1012 212 HOH HOH A . Q 7 HOH 213 1013 213 HOH HOH A . Q 7 HOH 214 1014 214 HOH HOH A . Q 7 HOH 215 1015 215 HOH HOH A . Q 7 HOH 216 1016 216 HOH HOH A . Q 7 HOH 217 1017 217 HOH HOH A . Q 7 HOH 218 1018 218 HOH HOH A . Q 7 HOH 219 1019 219 HOH HOH A . Q 7 HOH 220 1020 220 HOH HOH A . Q 7 HOH 221 1021 221 HOH HOH A . Q 7 HOH 222 1022 222 HOH HOH A . Q 7 HOH 223 1023 223 HOH HOH A . Q 7 HOH 224 1024 224 HOH HOH A . Q 7 HOH 225 1025 225 HOH HOH A . Q 7 HOH 226 1026 226 HOH HOH A . Q 7 HOH 227 1027 227 HOH HOH A . Q 7 HOH 228 1028 228 HOH HOH A . Q 7 HOH 229 1029 229 HOH HOH A . Q 7 HOH 230 1030 230 HOH HOH A . Q 7 HOH 231 1031 231 HOH HOH A . Q 7 HOH 232 1032 232 HOH HOH A . Q 7 HOH 233 1033 233 HOH HOH A . Q 7 HOH 234 1034 234 HOH HOH A . Q 7 HOH 235 1035 235 HOH HOH A . Q 7 HOH 236 1036 236 HOH HOH A . Q 7 HOH 237 1037 237 HOH HOH A . Q 7 HOH 238 1038 238 HOH HOH A . Q 7 HOH 239 1039 239 HOH HOH A . Q 7 HOH 240 1040 240 HOH HOH A . Q 7 HOH 241 1041 241 HOH HOH A . Q 7 HOH 242 1042 242 HOH HOH A . Q 7 HOH 243 1043 243 HOH HOH A . Q 7 HOH 244 1044 244 HOH HOH A . Q 7 HOH 245 1045 245 HOH HOH A . Q 7 HOH 246 1046 246 HOH HOH A . Q 7 HOH 247 1047 247 HOH HOH A . Q 7 HOH 248 1048 248 HOH HOH A . Q 7 HOH 249 1049 249 HOH HOH A . Q 7 HOH 250 1050 250 HOH HOH A . Q 7 HOH 251 1051 251 HOH HOH A . Q 7 HOH 252 1052 252 HOH HOH A . Q 7 HOH 253 1053 253 HOH HOH A . Q 7 HOH 254 1054 254 HOH HOH A . Q 7 HOH 255 1055 255 HOH HOH A . Q 7 HOH 256 1056 256 HOH HOH A . Q 7 HOH 257 1057 257 HOH HOH A . Q 7 HOH 258 1058 258 HOH HOH A . Q 7 HOH 259 1059 259 HOH HOH A . Q 7 HOH 260 1060 260 HOH HOH A . Q 7 HOH 261 1061 261 HOH HOH A . Q 7 HOH 262 1062 262 HOH HOH A . Q 7 HOH 263 1063 263 HOH HOH A . Q 7 HOH 264 1064 264 HOH HOH A . Q 7 HOH 265 1065 265 HOH HOH A . Q 7 HOH 266 1066 266 HOH HOH A . Q 7 HOH 267 1067 267 HOH HOH A . Q 7 HOH 268 1068 268 HOH HOH A . Q 7 HOH 269 1069 269 HOH HOH A . Q 7 HOH 270 1070 270 HOH HOH A . Q 7 HOH 271 1071 271 HOH HOH A . Q 7 HOH 272 1072 272 HOH HOH A . Q 7 HOH 273 1073 273 HOH HOH A . Q 7 HOH 274 1074 274 HOH HOH A . Q 7 HOH 275 1075 275 HOH HOH A . Q 7 HOH 276 1076 276 HOH HOH A . Q 7 HOH 277 1077 277 HOH HOH A . Q 7 HOH 278 1078 278 HOH HOH A . Q 7 HOH 279 1079 279 HOH HOH A . Q 7 HOH 280 1080 280 HOH HOH A . Q 7 HOH 281 1081 281 HOH HOH A . Q 7 HOH 282 1082 282 HOH HOH A . Q 7 HOH 283 1083 283 HOH HOH A . Q 7 HOH 284 1084 284 HOH HOH A . Q 7 HOH 285 1085 285 HOH HOH A . Q 7 HOH 286 1086 286 HOH HOH A . Q 7 HOH 287 1087 287 HOH HOH A . Q 7 HOH 288 1088 288 HOH HOH A . Q 7 HOH 289 1089 289 HOH HOH A . Q 7 HOH 290 1090 290 HOH HOH A . Q 7 HOH 291 1091 291 HOH HOH A . Q 7 HOH 292 1092 292 HOH HOH A . Q 7 HOH 293 1093 293 HOH HOH A . Q 7 HOH 294 1094 294 HOH HOH A . Q 7 HOH 295 1095 295 HOH HOH A . Q 7 HOH 296 1096 296 HOH HOH A . Q 7 HOH 297 1097 297 HOH HOH A . Q 7 HOH 298 1098 298 HOH HOH A . Q 7 HOH 299 1099 299 HOH HOH A . Q 7 HOH 300 1100 300 HOH HOH A . Q 7 HOH 301 1101 301 HOH HOH A . Q 7 HOH 302 1102 302 HOH HOH A . Q 7 HOH 303 1103 303 HOH HOH A . Q 7 HOH 304 1104 304 HOH HOH A . Q 7 HOH 305 1105 305 HOH HOH A . Q 7 HOH 306 1106 306 HOH HOH A . Q 7 HOH 307 1107 307 HOH HOH A . Q 7 HOH 308 1108 308 HOH HOH A . Q 7 HOH 309 1109 309 HOH HOH A . Q 7 HOH 310 1110 310 HOH HOH A . Q 7 HOH 311 1111 311 HOH HOH A . Q 7 HOH 312 1112 312 HOH HOH A . Q 7 HOH 313 1113 313 HOH HOH A . Q 7 HOH 314 1114 314 HOH HOH A . Q 7 HOH 315 1115 315 HOH HOH A . Q 7 HOH 316 1116 316 HOH HOH A . Q 7 HOH 317 1117 317 HOH HOH A . Q 7 HOH 318 1118 318 HOH HOH A . Q 7 HOH 319 1119 319 HOH HOH A . Q 7 HOH 320 1120 320 HOH HOH A . Q 7 HOH 321 1121 321 HOH HOH A . Q 7 HOH 322 1122 322 HOH HOH A . Q 7 HOH 323 1123 323 HOH HOH A . Q 7 HOH 324 1124 324 HOH HOH A . Q 7 HOH 325 1125 325 HOH HOH A . Q 7 HOH 326 1126 326 HOH HOH A . Q 7 HOH 327 1127 327 HOH HOH A . Q 7 HOH 328 1128 328 HOH HOH A . Q 7 HOH 329 1129 329 HOH HOH A . Q 7 HOH 330 1130 330 HOH HOH A . Q 7 HOH 331 1131 331 HOH HOH A . Q 7 HOH 332 1132 332 HOH HOH A . Q 7 HOH 333 1133 333 HOH HOH A . Q 7 HOH 334 1134 334 HOH HOH A . Q 7 HOH 335 1135 335 HOH HOH A . Q 7 HOH 336 1136 336 HOH HOH A . Q 7 HOH 337 1137 337 HOH HOH A . Q 7 HOH 338 1138 338 HOH HOH A . Q 7 HOH 339 1139 339 HOH HOH A . Q 7 HOH 340 1140 340 HOH HOH A . Q 7 HOH 341 1141 341 HOH HOH A . Q 7 HOH 342 1142 342 HOH HOH A . Q 7 HOH 343 1143 343 HOH HOH A . Q 7 HOH 344 1144 344 HOH HOH A . Q 7 HOH 345 1145 345 HOH HOH A . Q 7 HOH 346 1146 346 HOH HOH A . Q 7 HOH 347 1147 347 HOH HOH A . Q 7 HOH 348 1148 348 HOH HOH A . Q 7 HOH 349 1149 349 HOH HOH A . Q 7 HOH 350 1150 350 HOH HOH A . Q 7 HOH 351 1151 351 HOH HOH A . Q 7 HOH 352 1152 352 HOH HOH A . Q 7 HOH 353 1153 353 HOH HOH A . Q 7 HOH 354 1154 354 HOH HOH A . Q 7 HOH 355 1155 355 HOH HOH A . Q 7 HOH 356 1156 356 HOH HOH A . Q 7 HOH 357 1157 357 HOH HOH A . Q 7 HOH 358 1158 358 HOH HOH A . Q 7 HOH 359 1159 359 HOH HOH A . Q 7 HOH 360 1160 360 HOH HOH A . Q 7 HOH 361 1161 361 HOH HOH A . Q 7 HOH 362 1162 362 HOH HOH A . Q 7 HOH 363 1163 363 HOH HOH A . Q 7 HOH 364 1164 364 HOH HOH A . Q 7 HOH 365 1165 365 HOH HOH A . Q 7 HOH 366 1166 366 HOH HOH A . Q 7 HOH 367 1167 367 HOH HOH A . Q 7 HOH 368 1168 368 HOH HOH A . Q 7 HOH 369 1169 369 HOH HOH A . Q 7 HOH 370 1170 370 HOH HOH A . Q 7 HOH 371 1171 371 HOH HOH A . Q 7 HOH 372 1172 372 HOH HOH A . Q 7 HOH 373 1173 373 HOH HOH A . Q 7 HOH 374 1174 374 HOH HOH A . Q 7 HOH 375 1175 375 HOH HOH A . Q 7 HOH 376 1176 376 HOH HOH A . Q 7 HOH 377 1177 377 HOH HOH A . Q 7 HOH 378 1178 378 HOH HOH A . Q 7 HOH 379 1179 379 HOH HOH A . Q 7 HOH 380 1180 380 HOH HOH A . Q 7 HOH 381 1181 381 HOH HOH A . Q 7 HOH 382 1182 382 HOH HOH A . Q 7 HOH 383 1183 383 HOH HOH A . Q 7 HOH 384 1184 384 HOH HOH A . Q 7 HOH 385 1185 385 HOH HOH A . Q 7 HOH 386 1186 386 HOH HOH A . Q 7 HOH 387 1187 387 HOH HOH A . Q 7 HOH 388 1188 388 HOH HOH A . Q 7 HOH 389 1189 389 HOH HOH A . Q 7 HOH 390 1190 390 HOH HOH A . Q 7 HOH 391 1191 391 HOH HOH A . Q 7 HOH 392 1192 392 HOH HOH A . Q 7 HOH 393 1193 393 HOH HOH A . Q 7 HOH 394 1194 394 HOH HOH A . Q 7 HOH 395 1195 395 HOH HOH A . Q 7 HOH 396 1196 396 HOH HOH A . Q 7 HOH 397 1197 397 HOH HOH A . Q 7 HOH 398 1198 398 HOH HOH A . Q 7 HOH 399 1199 399 HOH HOH A . Q 7 HOH 400 1200 400 HOH HOH A . Q 7 HOH 401 1201 401 HOH HOH A . Q 7 HOH 402 1202 402 HOH HOH A . Q 7 HOH 403 1203 403 HOH HOH A . Q 7 HOH 404 1204 404 HOH HOH A . Q 7 HOH 405 1205 405 HOH HOH A . Q 7 HOH 406 1206 406 HOH HOH A . Q 7 HOH 407 1207 407 HOH HOH A . Q 7 HOH 408 1208 408 HOH HOH A . Q 7 HOH 409 1209 409 HOH HOH A . Q 7 HOH 410 1210 410 HOH HOH A . Q 7 HOH 411 1211 411 HOH HOH A . Q 7 HOH 412 1212 412 HOH HOH A . Q 7 HOH 413 1213 413 HOH HOH A . Q 7 HOH 414 1214 414 HOH HOH A . Q 7 HOH 415 1215 415 HOH HOH A . Q 7 HOH 416 1216 416 HOH HOH A . Q 7 HOH 417 1217 417 HOH HOH A . Q 7 HOH 418 1218 418 HOH HOH A . Q 7 HOH 419 1219 419 HOH HOH A . Q 7 HOH 420 1220 420 HOH HOH A . Q 7 HOH 421 1221 421 HOH HOH A . Q 7 HOH 422 1222 422 HOH HOH A . Q 7 HOH 423 1223 423 HOH HOH A . Q 7 HOH 424 1224 424 HOH HOH A . Q 7 HOH 425 1225 425 HOH HOH A . Q 7 HOH 426 1226 426 HOH HOH A . Q 7 HOH 427 1227 427 HOH HOH A . Q 7 HOH 428 1228 428 HOH HOH A . Q 7 HOH 429 1229 429 HOH HOH A . Q 7 HOH 430 1230 430 HOH HOH A . Q 7 HOH 431 1231 431 HOH HOH A . Q 7 HOH 432 1232 432 HOH HOH A . Q 7 HOH 433 1233 433 HOH HOH A . Q 7 HOH 434 1234 434 HOH HOH A . Q 7 HOH 435 1235 435 HOH HOH A . Q 7 HOH 436 1236 436 HOH HOH A . Q 7 HOH 437 1237 437 HOH HOH A . Q 7 HOH 438 1238 438 HOH HOH A . Q 7 HOH 439 1239 439 HOH HOH A . Q 7 HOH 440 1240 440 HOH HOH A . Q 7 HOH 441 1241 441 HOH HOH A . Q 7 HOH 442 1242 442 HOH HOH A . Q 7 HOH 443 1243 443 HOH HOH A . Q 7 HOH 444 1244 444 HOH HOH A . Q 7 HOH 445 1245 445 HOH HOH A . Q 7 HOH 446 1246 446 HOH HOH A . Q 7 HOH 447 1247 447 HOH HOH A . Q 7 HOH 448 1248 448 HOH HOH A . Q 7 HOH 449 1249 449 HOH HOH A . Q 7 HOH 450 1250 450 HOH HOH A . Q 7 HOH 451 1251 451 HOH HOH A . Q 7 HOH 452 1252 452 HOH HOH A . Q 7 HOH 453 1253 453 HOH HOH A . Q 7 HOH 454 1254 454 HOH HOH A . Q 7 HOH 455 1255 455 HOH HOH A . Q 7 HOH 456 1256 456 HOH HOH A . Q 7 HOH 457 1257 457 HOH HOH A . Q 7 HOH 458 1258 458 HOH HOH A . Q 7 HOH 459 1259 459 HOH HOH A . Q 7 HOH 460 1260 460 HOH HOH A . Q 7 HOH 461 1261 461 HOH HOH A . Q 7 HOH 462 1262 462 HOH HOH A . Q 7 HOH 463 1263 463 HOH HOH A . Q 7 HOH 464 1264 464 HOH HOH A . Q 7 HOH 465 1265 465 HOH HOH A . Q 7 HOH 466 1266 466 HOH HOH A . Q 7 HOH 467 1267 467 HOH HOH A . Q 7 HOH 468 1268 468 HOH HOH A . Q 7 HOH 469 1269 469 HOH HOH A . Q 7 HOH 470 1270 470 HOH HOH A . Q 7 HOH 471 1271 471 HOH HOH A . Q 7 HOH 472 1272 472 HOH HOH A . Q 7 HOH 473 1273 473 HOH HOH A . Q 7 HOH 474 1274 474 HOH HOH A . Q 7 HOH 475 1275 475 HOH HOH A . Q 7 HOH 476 1276 476 HOH HOH A . Q 7 HOH 477 1277 477 HOH HOH A . Q 7 HOH 478 1278 478 HOH HOH A . Q 7 HOH 479 1279 479 HOH HOH A . Q 7 HOH 480 1280 480 HOH HOH A . Q 7 HOH 481 1281 481 HOH HOH A . Q 7 HOH 482 1282 482 HOH HOH A . Q 7 HOH 483 1283 483 HOH HOH A . Q 7 HOH 484 1284 484 HOH HOH A . Q 7 HOH 485 1285 485 HOH HOH A . Q 7 HOH 486 1286 486 HOH HOH A . Q 7 HOH 487 1287 487 HOH HOH A . Q 7 HOH 488 1288 488 HOH HOH A . Q 7 HOH 489 1289 489 HOH HOH A . Q 7 HOH 490 1290 490 HOH HOH A . Q 7 HOH 491 1291 491 HOH HOH A . Q 7 HOH 492 1292 492 HOH HOH A . Q 7 HOH 493 1293 493 HOH HOH A . Q 7 HOH 494 1294 494 HOH HOH A . Q 7 HOH 495 1295 495 HOH HOH A . Q 7 HOH 496 1296 496 HOH HOH A . Q 7 HOH 497 1297 497 HOH HOH A . Q 7 HOH 498 1298 498 HOH HOH A . Q 7 HOH 499 1299 499 HOH HOH A . Q 7 HOH 500 1300 500 HOH HOH A . Q 7 HOH 501 1301 501 HOH HOH A . Q 7 HOH 502 1302 502 HOH HOH A . Q 7 HOH 503 1303 503 HOH HOH A . Q 7 HOH 504 1304 504 HOH HOH A . Q 7 HOH 505 1305 505 HOH HOH A . Q 7 HOH 506 1306 506 HOH HOH A . Q 7 HOH 507 1307 507 HOH HOH A . Q 7 HOH 508 1308 508 HOH HOH A . Q 7 HOH 509 1309 509 HOH HOH A . Q 7 HOH 510 1310 510 HOH HOH A . Q 7 HOH 511 1311 511 HOH HOH A . Q 7 HOH 512 1312 512 HOH HOH A . Q 7 HOH 513 1313 513 HOH HOH A . Q 7 HOH 514 1314 514 HOH HOH A . Q 7 HOH 515 1315 515 HOH HOH A . Q 7 HOH 516 1316 516 HOH HOH A . Q 7 HOH 517 1317 517 HOH HOH A . Q 7 HOH 518 1318 518 HOH HOH A . Q 7 HOH 519 1319 519 HOH HOH A . Q 7 HOH 520 1320 520 HOH HOH A . Q 7 HOH 521 1321 521 HOH HOH A . Q 7 HOH 522 1322 522 HOH HOH A . Q 7 HOH 523 1323 523 HOH HOH A . Q 7 HOH 524 1324 524 HOH HOH A . Q 7 HOH 525 1325 525 HOH HOH A . Q 7 HOH 526 1326 526 HOH HOH A . Q 7 HOH 527 1327 527 HOH HOH A . Q 7 HOH 528 1328 528 HOH HOH A . Q 7 HOH 529 1329 529 HOH HOH A . Q 7 HOH 530 1330 530 HOH HOH A . Q 7 HOH 531 1331 531 HOH HOH A . Q 7 HOH 532 1332 532 HOH HOH A . Q 7 HOH 533 1333 533 HOH HOH A . Q 7 HOH 534 1334 534 HOH HOH A . Q 7 HOH 535 1335 535 HOH HOH A . Q 7 HOH 536 1336 536 HOH HOH A . Q 7 HOH 537 1337 537 HOH HOH A . Q 7 HOH 538 1338 538 HOH HOH A . Q 7 HOH 539 1339 539 HOH HOH A . Q 7 HOH 540 1340 540 HOH HOH A . Q 7 HOH 541 1341 541 HOH HOH A . Q 7 HOH 542 1342 542 HOH HOH A . Q 7 HOH 543 1343 543 HOH HOH A . Q 7 HOH 544 1344 544 HOH HOH A . Q 7 HOH 545 1345 545 HOH HOH A . Q 7 HOH 546 1346 546 HOH HOH A . Q 7 HOH 547 1347 547 HOH HOH A . Q 7 HOH 548 1348 548 HOH HOH A . Q 7 HOH 549 1349 549 HOH HOH A . Q 7 HOH 550 1350 550 HOH HOH A . Q 7 HOH 551 1351 551 HOH HOH A . Q 7 HOH 552 1352 552 HOH HOH A . Q 7 HOH 553 1353 553 HOH HOH A . Q 7 HOH 554 1354 554 HOH HOH A . Q 7 HOH 555 1355 555 HOH HOH A . Q 7 HOH 556 1356 556 HOH HOH A . Q 7 HOH 557 1357 557 HOH HOH A . Q 7 HOH 558 1358 558 HOH HOH A . Q 7 HOH 559 1359 559 HOH HOH A . Q 7 HOH 560 1360 560 HOH HOH A . Q 7 HOH 561 1361 561 HOH HOH A . Q 7 HOH 562 1362 562 HOH HOH A . Q 7 HOH 563 1363 563 HOH HOH A . Q 7 HOH 564 1364 564 HOH HOH A . Q 7 HOH 565 1365 565 HOH HOH A . Q 7 HOH 566 1366 566 HOH HOH A . Q 7 HOH 567 1367 567 HOH HOH A . Q 7 HOH 568 1368 568 HOH HOH A . Q 7 HOH 569 1369 569 HOH HOH A . Q 7 HOH 570 1370 570 HOH HOH A . Q 7 HOH 571 1371 571 HOH HOH A . Q 7 HOH 572 1372 572 HOH HOH A . Q 7 HOH 573 1373 573 HOH HOH A . Q 7 HOH 574 1374 574 HOH HOH A . Q 7 HOH 575 1375 575 HOH HOH A . Q 7 HOH 576 1376 576 HOH HOH A . Q 7 HOH 577 1377 577 HOH HOH A . Q 7 HOH 578 1378 578 HOH HOH A . Q 7 HOH 579 1379 579 HOH HOH A . Q 7 HOH 580 1380 580 HOH HOH A . Q 7 HOH 581 1381 581 HOH HOH A . Q 7 HOH 582 1382 582 HOH HOH A . Q 7 HOH 583 1383 583 HOH HOH A . Q 7 HOH 584 1384 584 HOH HOH A . Q 7 HOH 585 1385 585 HOH HOH A . Q 7 HOH 586 1386 586 HOH HOH A . Q 7 HOH 587 1387 587 HOH HOH A . Q 7 HOH 588 1388 588 HOH HOH A . Q 7 HOH 589 1389 589 HOH HOH A . Q 7 HOH 590 1390 590 HOH HOH A . Q 7 HOH 591 1391 591 HOH HOH A . Q 7 HOH 592 1392 592 HOH HOH A . Q 7 HOH 593 1393 593 HOH HOH A . Q 7 HOH 594 1394 594 HOH HOH A . Q 7 HOH 595 1395 595 HOH HOH A . Q 7 HOH 596 1396 596 HOH HOH A . Q 7 HOH 597 1397 597 HOH HOH A . Q 7 HOH 598 1398 598 HOH HOH A . Q 7 HOH 599 1399 599 HOH HOH A . Q 7 HOH 600 1400 600 HOH HOH A . Q 7 HOH 601 1401 601 HOH HOH A . Q 7 HOH 602 1402 602 HOH HOH A . Q 7 HOH 603 1403 603 HOH HOH A . Q 7 HOH 604 1404 604 HOH HOH A . Q 7 HOH 605 1405 605 HOH HOH A . Q 7 HOH 606 1406 606 HOH HOH A . Q 7 HOH 607 1407 607 HOH HOH A . Q 7 HOH 608 1408 608 HOH HOH A . Q 7 HOH 609 1409 609 HOH HOH A . Q 7 HOH 610 1410 610 HOH HOH A . Q 7 HOH 611 1411 611 HOH HOH A . Q 7 HOH 612 1412 612 HOH HOH A . Q 7 HOH 613 1413 613 HOH HOH A . Q 7 HOH 614 1414 614 HOH HOH A . Q 7 HOH 615 1415 615 HOH HOH A . Q 7 HOH 616 1416 616 HOH HOH A . Q 7 HOH 617 1417 617 HOH HOH A . Q 7 HOH 618 1418 618 HOH HOH A . Q 7 HOH 619 1419 619 HOH HOH A . Q 7 HOH 620 1420 620 HOH HOH A . Q 7 HOH 621 1421 621 HOH HOH A . Q 7 HOH 622 1422 622 HOH HOH A . Q 7 HOH 623 1423 623 HOH HOH A . Q 7 HOH 624 1424 624 HOH HOH A . Q 7 HOH 625 1425 625 HOH HOH A . Q 7 HOH 626 1426 626 HOH HOH A . Q 7 HOH 627 1427 627 HOH HOH A . Q 7 HOH 628 1428 628 HOH HOH A . Q 7 HOH 629 1429 629 HOH HOH A . Q 7 HOH 630 1430 630 HOH HOH A . Q 7 HOH 631 1431 631 HOH HOH A . Q 7 HOH 632 1432 632 HOH HOH A . Q 7 HOH 633 1433 633 HOH HOH A . Q 7 HOH 634 1434 634 HOH HOH A . Q 7 HOH 635 1435 635 HOH HOH A . Q 7 HOH 636 1436 636 HOH HOH A . Q 7 HOH 637 1437 637 HOH HOH A . Q 7 HOH 638 1438 638 HOH HOH A . Q 7 HOH 639 1439 639 HOH HOH A . Q 7 HOH 640 1440 640 HOH HOH A . Q 7 HOH 641 1441 641 HOH HOH A . Q 7 HOH 642 1442 642 HOH HOH A . Q 7 HOH 643 1443 643 HOH HOH A . Q 7 HOH 644 1444 644 HOH HOH A . Q 7 HOH 645 1445 645 HOH HOH A . Q 7 HOH 646 1446 646 HOH HOH A . Q 7 HOH 647 1447 647 HOH HOH A . Q 7 HOH 648 1448 648 HOH HOH A . Q 7 HOH 649 1449 649 HOH HOH A . Q 7 HOH 650 1450 650 HOH HOH A . Q 7 HOH 651 1451 651 HOH HOH A . Q 7 HOH 652 1452 652 HOH HOH A . Q 7 HOH 653 1453 653 HOH HOH A . Q 7 HOH 654 1454 654 HOH HOH A . Q 7 HOH 655 1455 655 HOH HOH A . Q 7 HOH 656 1456 656 HOH HOH A . Q 7 HOH 657 1457 657 HOH HOH A . Q 7 HOH 658 1458 658 HOH HOH A . Q 7 HOH 659 1459 659 HOH HOH A . Q 7 HOH 660 1460 660 HOH HOH A . Q 7 HOH 661 1461 661 HOH HOH A . Q 7 HOH 662 1462 662 HOH HOH A . Q 7 HOH 663 1463 663 HOH HOH A . Q 7 HOH 664 1464 664 HOH HOH A . Q 7 HOH 665 1465 665 HOH HOH A . Q 7 HOH 666 1466 666 HOH HOH A . Q 7 HOH 667 1467 667 HOH HOH A . Q 7 HOH 668 1468 668 HOH HOH A . Q 7 HOH 669 1469 669 HOH HOH A . Q 7 HOH 670 1470 670 HOH HOH A . Q 7 HOH 671 1471 671 HOH HOH A . Q 7 HOH 672 1472 672 HOH HOH A . Q 7 HOH 673 1473 673 HOH HOH A . Q 7 HOH 674 1474 674 HOH HOH A . Q 7 HOH 675 1475 675 HOH HOH A . Q 7 HOH 676 1476 676 HOH HOH A . Q 7 HOH 677 1477 677 HOH HOH A . Q 7 HOH 678 1478 678 HOH HOH A . Q 7 HOH 679 1479 679 HOH HOH A . Q 7 HOH 680 1480 680 HOH HOH A . Q 7 HOH 681 1481 681 HOH HOH A . Q 7 HOH 682 1482 682 HOH HOH A . Q 7 HOH 683 1483 683 HOH HOH A . Q 7 HOH 684 1484 684 HOH HOH A . Q 7 HOH 685 1485 685 HOH HOH A . Q 7 HOH 686 1486 686 HOH HOH A . Q 7 HOH 687 1487 687 HOH HOH A . Q 7 HOH 688 1488 688 HOH HOH A . Q 7 HOH 689 1489 689 HOH HOH A . Q 7 HOH 690 1490 690 HOH HOH A . Q 7 HOH 691 1491 691 HOH HOH A . Q 7 HOH 692 1492 692 HOH HOH A . Q 7 HOH 693 1493 693 HOH HOH A . Q 7 HOH 694 1494 694 HOH HOH A . Q 7 HOH 695 1495 695 HOH HOH A . Q 7 HOH 696 1496 696 HOH HOH A . Q 7 HOH 697 1497 697 HOH HOH A . Q 7 HOH 698 1498 698 HOH HOH A . Q 7 HOH 699 1499 699 HOH HOH A . Q 7 HOH 700 1500 700 HOH HOH A . Q 7 HOH 701 1501 701 HOH HOH A . Q 7 HOH 702 1502 702 HOH HOH A . Q 7 HOH 703 1503 703 HOH HOH A . Q 7 HOH 704 1504 704 HOH HOH A . Q 7 HOH 705 1505 705 HOH HOH A . Q 7 HOH 706 1506 706 HOH HOH A . Q 7 HOH 707 1507 707 HOH HOH A . Q 7 HOH 708 1508 708 HOH HOH A . Q 7 HOH 709 1509 709 HOH HOH A . Q 7 HOH 710 1510 710 HOH HOH A . Q 7 HOH 711 1511 711 HOH HOH A . Q 7 HOH 712 1512 712 HOH HOH A . Q 7 HOH 713 1513 713 HOH HOH A . Q 7 HOH 714 1514 714 HOH HOH A . Q 7 HOH 715 1515 715 HOH HOH A . Q 7 HOH 716 1516 716 HOH HOH A . Q 7 HOH 717 1517 717 HOH HOH A . Q 7 HOH 718 1518 718 HOH HOH A . Q 7 HOH 719 1519 719 HOH HOH A . Q 7 HOH 720 1520 720 HOH HOH A . Q 7 HOH 721 1521 721 HOH HOH A . Q 7 HOH 722 1522 722 HOH HOH A . Q 7 HOH 723 1523 723 HOH HOH A . Q 7 HOH 724 1524 724 HOH HOH A . Q 7 HOH 725 1525 725 HOH HOH A . Q 7 HOH 726 1526 726 HOH HOH A . Q 7 HOH 727 1527 727 HOH HOH A . Q 7 HOH 728 1528 728 HOH HOH A . Q 7 HOH 729 1529 729 HOH HOH A . Q 7 HOH 730 1530 730 HOH HOH A . Q 7 HOH 731 1531 731 HOH HOH A . Q 7 HOH 732 1532 732 HOH HOH A . Q 7 HOH 733 1533 733 HOH HOH A . Q 7 HOH 734 1534 734 HOH HOH A . Q 7 HOH 735 1535 735 HOH HOH A . Q 7 HOH 736 1536 736 HOH HOH A . Q 7 HOH 737 1537 737 HOH HOH A . Q 7 HOH 738 1538 738 HOH HOH A . Q 7 HOH 739 1539 739 HOH HOH A . Q 7 HOH 740 1540 740 HOH HOH A . Q 7 HOH 741 1541 741 HOH HOH A . Q 7 HOH 742 1542 742 HOH HOH A . Q 7 HOH 743 1543 743 HOH HOH A . Q 7 HOH 744 1544 744 HOH HOH A . Q 7 HOH 745 1545 745 HOH HOH A . Q 7 HOH 746 1546 746 HOH HOH A . Q 7 HOH 747 1547 747 HOH HOH A . Q 7 HOH 748 1548 748 HOH HOH A . Q 7 HOH 749 1549 749 HOH HOH A . Q 7 HOH 750 1550 750 HOH HOH A . Q 7 HOH 751 1551 751 HOH HOH A . Q 7 HOH 752 1552 752 HOH HOH A . Q 7 HOH 753 1553 753 HOH HOH A . Q 7 HOH 754 1554 754 HOH HOH A . Q 7 HOH 755 1555 755 HOH HOH A . Q 7 HOH 756 1556 756 HOH HOH A . Q 7 HOH 757 1557 757 HOH HOH A . Q 7 HOH 758 1558 758 HOH HOH A . Q 7 HOH 759 1559 759 HOH HOH A . Q 7 HOH 760 1560 760 HOH HOH A . Q 7 HOH 761 1561 761 HOH HOH A . Q 7 HOH 762 1562 762 HOH HOH A . Q 7 HOH 763 1563 763 HOH HOH A . Q 7 HOH 764 1564 764 HOH HOH A . Q 7 HOH 765 1565 765 HOH HOH A . Q 7 HOH 766 1566 766 HOH HOH A . Q 7 HOH 767 1567 767 HOH HOH A . Q 7 HOH 768 1568 768 HOH HOH A . Q 7 HOH 769 1569 769 HOH HOH A . Q 7 HOH 770 1570 770 HOH HOH A . Q 7 HOH 771 1571 771 HOH HOH A . Q 7 HOH 772 1572 772 HOH HOH A . Q 7 HOH 773 1573 773 HOH HOH A . Q 7 HOH 774 1574 774 HOH HOH A . Q 7 HOH 775 1575 775 HOH HOH A . Q 7 HOH 776 1576 776 HOH HOH A . Q 7 HOH 777 1577 777 HOH HOH A . Q 7 HOH 778 1578 778 HOH HOH A . Q 7 HOH 779 1579 779 HOH HOH A . Q 7 HOH 780 1580 780 HOH HOH A . Q 7 HOH 781 1581 781 HOH HOH A . Q 7 HOH 782 1582 782 HOH HOH A . Q 7 HOH 783 1583 783 HOH HOH A . Q 7 HOH 784 1584 784 HOH HOH A . Q 7 HOH 785 1585 785 HOH HOH A . Q 7 HOH 786 1586 786 HOH HOH A . Q 7 HOH 787 1587 787 HOH HOH A . Q 7 HOH 788 1588 788 HOH HOH A . Q 7 HOH 789 1589 789 HOH HOH A . Q 7 HOH 790 1590 790 HOH HOH A . Q 7 HOH 791 1591 791 HOH HOH A . Q 7 HOH 792 1592 792 HOH HOH A . Q 7 HOH 793 1593 793 HOH HOH A . Q 7 HOH 794 1594 794 HOH HOH A . Q 7 HOH 795 1595 795 HOH HOH A . Q 7 HOH 796 1596 796 HOH HOH A . Q 7 HOH 797 1597 797 HOH HOH A . Q 7 HOH 798 1598 798 HOH HOH A . Q 7 HOH 799 1599 799 HOH HOH A . Q 7 HOH 800 1600 800 HOH HOH A . Q 7 HOH 801 1601 801 HOH HOH A . Q 7 HOH 802 1602 802 HOH HOH A . Q 7 HOH 803 1603 803 HOH HOH A . Q 7 HOH 804 1604 804 HOH HOH A . Q 7 HOH 805 1605 805 HOH HOH A . Q 7 HOH 806 1606 806 HOH HOH A . Q 7 HOH 807 1607 807 HOH HOH A . Q 7 HOH 808 1608 808 HOH HOH A . Q 7 HOH 809 1609 809 HOH HOH A . Q 7 HOH 810 1610 810 HOH HOH A . Q 7 HOH 811 1611 811 HOH HOH A . Q 7 HOH 812 1612 812 HOH HOH A . Q 7 HOH 813 1613 813 HOH HOH A . Q 7 HOH 814 1614 814 HOH HOH A . Q 7 HOH 815 1615 815 HOH HOH A . Q 7 HOH 816 1616 816 HOH HOH A . Q 7 HOH 817 1617 817 HOH HOH A . Q 7 HOH 818 1618 818 HOH HOH A . Q 7 HOH 819 1619 819 HOH HOH A . Q 7 HOH 820 1620 820 HOH HOH A . Q 7 HOH 821 1621 821 HOH HOH A . Q 7 HOH 822 1622 822 HOH HOH A . Q 7 HOH 823 1623 823 HOH HOH A . Q 7 HOH 824 1624 824 HOH HOH A . Q 7 HOH 825 1625 825 HOH HOH A . Q 7 HOH 826 1626 826 HOH HOH A . Q 7 HOH 827 1627 827 HOH HOH A . Q 7 HOH 828 1628 828 HOH HOH A . Q 7 HOH 829 1629 829 HOH HOH A . Q 7 HOH 830 1630 830 HOH HOH A . Q 7 HOH 831 1631 831 HOH HOH A . Q 7 HOH 832 1632 832 HOH HOH A . Q 7 HOH 833 1633 833 HOH HOH A . Q 7 HOH 834 1634 834 HOH HOH A . Q 7 HOH 835 1635 835 HOH HOH A . Q 7 HOH 836 1636 836 HOH HOH A . Q 7 HOH 837 1637 837 HOH HOH A . Q 7 HOH 838 1638 838 HOH HOH A . Q 7 HOH 839 1639 839 HOH HOH A . Q 7 HOH 840 1640 840 HOH HOH A . Q 7 HOH 841 1641 841 HOH HOH A . Q 7 HOH 842 1642 842 HOH HOH A . Q 7 HOH 843 1643 843 HOH HOH A . Q 7 HOH 844 1644 844 HOH HOH A . Q 7 HOH 845 1645 845 HOH HOH A . Q 7 HOH 846 1646 846 HOH HOH A . Q 7 HOH 847 1647 847 HOH HOH A . Q 7 HOH 848 1648 848 HOH HOH A . Q 7 HOH 849 1649 849 HOH HOH A . Q 7 HOH 850 1650 850 HOH HOH A . Q 7 HOH 851 1651 851 HOH HOH A . Q 7 HOH 852 1652 852 HOH HOH A . Q 7 HOH 853 1653 853 HOH HOH A . #