data_3WLN # _entry.id 3WLN # _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 3WLN RCSB RCSB096490 WWPDB D_1000096490 # 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 3WLO . unspecified PDB 3WLP . unspecified PDB 3WLQ . unspecified PDB 3WLR . unspecified PDB 3WLS . unspecified PDB 3WLT . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3WLN _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 'Hrmova, M.' 2 # _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 3WLN _cell.length_a 100.703 _cell.length_b 100.703 _cell.length_c 181.878 _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 3WLN _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 nat '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 7 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 4 ? ? ? ? 4 non-polymer man ALPHA-L-FUCOSE 164.156 1 ? ? ? ? 5 non-polymer man 2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL 308.434 1 ? ? ? ? 6 water nat water 18.015 901 ? ? ? ? # _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_nat.entity_id 1 _entity_src_nat.pdbx_src_id 1 _entity_src_nat.pdbx_alt_source_flag sample _entity_src_nat.pdbx_beg_seq_num ? _entity_src_nat.pdbx_end_seq_num ? _entity_src_nat.common_name 'barley,two-rowed barley' _entity_src_nat.pdbx_organism_scientific 'Hordeum vulgare subsp. vulgare' _entity_src_nat.pdbx_ncbi_taxonomy_id 112509 _entity_src_nat.genus ? _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion ? _entity_src_nat.pdbx_fragment ? _entity_src_nat.pdbx_variant ? _entity_src_nat.pdbx_cell_line ? _entity_src_nat.pdbx_atcc ? _entity_src_nat.pdbx_cellular_location ? _entity_src_nat.pdbx_organ ? _entity_src_nat.pdbx_organelle ? _entity_src_nat.pdbx_cell ? _entity_src_nat.pdbx_plasmid_name ? _entity_src_nat.pdbx_plasmid_details ? _entity_src_nat.details ? # _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 3WLN _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 3WLN _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 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 FUC saccharide . ALPHA-L-FUCOSE ? 'C6 H12 O5' 164.156 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 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 SOG non-polymer . 2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL 1-S-OCTYL-BETA-D-THIOGLUCOSIDE 'C14 H28 O5 S' 308.434 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 3WLN _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.54 _exptl_crystal.density_percent_sol 65.29 _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 buffer, 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 315' _diffrn_detector.pdbx_collection_date 2008-11-12 _diffrn_detector.details 'collimating mirror, double-crystal Si(111) monochromator' # _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)' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.0 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'PHOTON FACTORY BEAMLINE BL-5A' _diffrn_source.pdbx_synchrotron_site 'Photon Factory' _diffrn_source.pdbx_synchrotron_beamline BL-5A _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.0 # _reflns.entry_id 3WLN _reflns.observed_criterion_sigma_I 1.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 88.05 _reflns.d_resolution_high 2.0 _reflns.number_obs 60745 _reflns.number_all 60745 _reflns.percent_possible_obs 99.9 _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 1.998 _reflns_shell.d_res_low 2.05 _reflns_shell.percent_possible_all 98.7 _reflns_shell.Rmerge_I_obs 0.990 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 1.3 _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.number_possible ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.meanI_over_sigI_all ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 3WLN _refine.ls_number_reflns_obs 60745 _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 41.44 _refine.ls_d_res_high 2.00 _refine.ls_percent_reflns_obs 99.88 _refine.ls_R_factor_obs 0.17123 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.16942 _refine.ls_R_factor_R_free 0.20485 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 3245 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.967 _refine.correlation_coeff_Fo_to_Fc_free 0.952 _refine.B_iso_mean 32.212 _refine.aniso_B[1][1] 0.21 _refine.aniso_B[2][2] 0.21 _refine.aniso_B[3][3] -0.41 _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 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 ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model 1IEQ _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.133 _refine.pdbx_overall_ESU_R_Free 0.127 _refine.overall_SU_ML 0.096 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 6.404 _refine.overall_SU_R_Cruickshank_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_diffrn_id 1 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 4566 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 172 _refine_hist.number_atoms_solvent 901 _refine_hist.number_atoms_total 5639 _refine_hist.d_res_high 2.00 _refine_hist.d_res_low 41.44 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_restraint_function _refine_ls_restr.pdbx_refine_id r_bond_refined_d 0.011 0.022 ? 4875 ? 'X-RAY DIFFRACTION' r_bond_other_d ? ? ? ? ? 'X-RAY DIFFRACTION' r_angle_refined_deg 1.372 2.004 ? 6640 ? 'X-RAY DIFFRACTION' r_angle_other_deg ? ? ? ? ? 'X-RAY DIFFRACTION' r_dihedral_angle_1_deg 6.233 5.000 ? 603 ? 'X-RAY DIFFRACTION' r_dihedral_angle_2_deg 38.447 24.124 ? 194 ? 'X-RAY DIFFRACTION' r_dihedral_angle_3_deg 13.903 15.000 ? 774 ? 'X-RAY DIFFRACTION' r_dihedral_angle_4_deg 15.748 15.000 ? 28 ? 'X-RAY DIFFRACTION' r_chiral_restr 0.090 0.200 ? 780 ? 'X-RAY DIFFRACTION' r_gen_planes_refined 0.004 0.020 ? 3580 ? 'X-RAY DIFFRACTION' r_gen_planes_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbd_refined 0.195 0.200 ? 2608 ? 'X-RAY DIFFRACTION' r_nbd_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbtor_refined 0.303 0.200 ? 3397 ? 'X-RAY DIFFRACTION' r_nbtor_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_xyhbond_nbd_refined 0.169 0.200 ? 719 ? '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 0.251 0.200 ? 54 ? 'X-RAY DIFFRACTION' r_symmetry_vdw_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_hbond_refined 0.228 0.200 ? 36 ? '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 0.504 1.500 ? 3060 ? 'X-RAY DIFFRACTION' r_mcbond_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_mcangle_it 0.839 2.000 ? 4812 ? 'X-RAY DIFFRACTION' r_mcangle_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_scbond_it 1.578 3.000 ? 2032 ? 'X-RAY DIFFRACTION' r_scbond_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_scangle_it 2.525 4.500 ? 1828 ? 'X-RAY DIFFRACTION' r_scangle_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_long_range_B_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_long_range_B_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_rigid_bond_restr ? ? ? ? ? 'X-RAY DIFFRACTION' r_sphericity_free ? ? ? ? ? 'X-RAY DIFFRACTION' r_sphericity_bonded ? ? ? ? ? 'X-RAY DIFFRACTION' # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.998 _refine_ls_shell.d_res_low 2.050 _refine_ls_shell.number_reflns_R_work 4333 _refine_ls_shell.R_factor_R_work 0.287 _refine_ls_shell.percent_reflns_obs 98.71 _refine_ls_shell.R_factor_R_free 0.312 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 261 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? # _struct.entry_id 3WLN _struct.title 'Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme EXO1 in complex with octyl-S-glucoside' _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 3WLN _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'BETA BARREL, HYDROLASE, GRAIN DEVELOPMENT, Tim Barrel/Beta sheet, N-glycosylation, plant apoplast' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 3 ? E N N 2 ? F N N 2 ? G N N 3 ? H N N 3 ? I N N 2 ? J N N 2 ? K N N 2 ? L N N 3 ? M N N 4 ? N N N 5 ? O N N 6 ? # _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 ? THR A 138 ? ASP A 120 THR A 138 1 ? 19 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 ? MET A 173 ? ASP A 166 MET A 173 1 ? 8 HELX_P HELX_P11 11 GLU A 175 ? GLY A 182 ? GLU A 175 GLY A 182 1 ? 8 HELX_P HELX_P12 12 GLY A 210 ? ILE A 218 ? GLY A 210 ILE A 218 5 ? 9 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 5 ? 6 HELX_P HELX_P26 26 GLY A 505 ? GLY A 514 ? GLY A 505 GLY A 514 1 ? 10 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 ? ? ? ? ? ? ? 2.106 ? disulf2 disulf ? ? A CYS 513 SG ? ? ? 1_555 A CYS 518 SG ? ? A CYS 513 A CYS 518 1_555 ? ? ? ? ? ? ? 2.015 ? covale1 covale ? ? A ASN 498 ND2 A ? ? 1_555 E NAG . C1 ? ? A ASN 498 A NAG 704 1_555 ? ? ? ? ? ? ? 1.430 ? covale2 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 701 A NAG 702 1_555 ? ? ? ? ? ? ? 1.442 ? covale3 covale ? ? A ASN 221 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 221 A NAG 701 1_555 ? ? ? ? ? ? ? 1.444 ? covale4 covale ? ? G BMA . O6 ? ? ? 1_555 H BMA . C1 ? ? A BMA 706 A BMA 707 1_555 ? ? ? ? ? ? ? 1.448 ? covale5 covale ? ? C NAG . O4 ? ? ? 1_555 D BMA . C1 ? ? A NAG 702 A BMA 703 1_555 ? ? ? ? ? ? ? 1.449 ? covale6 covale ? ? A ASN 600 ND2 ? ? ? 1_555 J NAG . C1 ? ? A ASN 600 A NAG 709 1_555 ? ? ? ? ? ? ? 1.451 ? covale7 covale ? ? F NAG . O4 ? ? ? 1_555 G BMA . C1 ? ? A NAG 705 A BMA 706 1_555 ? ? ? ? ? ? ? 1.451 ? covale8 covale ? ? H BMA . O2 ? ? ? 1_555 I NAG . C1 ? ? A BMA 707 A NAG 708 1_555 ? ? ? ? ? ? ? 1.452 ? covale9 covale ? ? J NAG . O3 ? ? ? 1_555 M FUC . C1 ? ? A NAG 709 A FUC 712 1_555 ? ? ? ? ? ? ? 1.453 ? covale10 covale ? ? K NAG . O4 ? ? ? 1_555 L BMA . C1 ? ? A NAG 710 A BMA 711 1_555 ? ? ? ? ? ? ? 1.458 ? covale11 covale ? ? J NAG . O4 ? ? ? 1_555 K NAG . C1 ? ? A NAG 709 A NAG 710 1_555 ? ? ? ? ? ? ? 1.460 ? covale12 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 704 A NAG 705 1_555 ? ? ? ? ? ? ? 1.467 ? covale13 covale ? ? A ASN 498 ND2 B ? ? 1_555 E NAG . C1 ? ? A ASN 498 A NAG 704 1_555 ? ? ? ? ? ? ? 1.473 ? # 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 4.19 2 LYS 206 A . ? LYS 206 A HIS 207 A ? HIS 207 A 1 -10.22 3 PHE 208 A . ? PHE 208 A VAL 209 A ? VAL 209 A 1 -7.80 4 THR 294 A . ? THR 294 A PRO 295 A ? PRO 295 A 1 -8.90 5 VAL 317 A . ? VAL 317 A PRO 318 A ? PRO 318 A 1 -8.00 6 LEU 404 A . ? LEU 404 A PRO 405 A ? PRO 405 A 1 2.80 7 GLU 503 A . ? GLU 503 A PRO 504 A ? PRO 504 A 1 -4.73 8 LEU 578 A . ? LEU 578 A PRO 579 A ? PRO 579 A 1 0.57 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 5 ? B ? 3 ? C ? 3 ? D ? 6 ? E ? 2 ? # 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 E 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id 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 E 1 TRP A 571 ? PHE A 572 ? TRP A 571 PHE A 572 E 2 PRO A 589 ? PHE A 591 ? PRO A 589 PHE A 591 # 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 ILE A 523 ? O ILE A 523 N VAL A 484 ? N VAL A 484 D 4 5 O ILE A 481 ? O ILE A 481 N LEU A 414 ? N LEU A 414 D 5 6 N VAL A 415 ? N VAL A 415 O VAL A 462 ? O VAL A 462 E 1 2 N TRP A 571 ? N TRP A 571 O PHE A 591 ? O PHE A 591 # 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 ? ? ? ? 14 'BINDING SITE FOR RESIDUE SOG A 713' AC2 Software ? ? ? ? 13 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 221 RESIDUES 701 TO 703' AC3 Software ? ? ? ? 17 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 498 RESIDUES 704 TO 708' AC4 Software ? ? ? ? 11 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 600 RESIDUES 709 TO 712' # 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 14 ASP A 95 ? ASP A 95 . ? 1_555 ? 2 AC1 14 PHE A 144 ? PHE A 144 . ? 1_555 ? 3 AC1 14 ARG A 158 ? ARG A 158 . ? 1_555 ? 4 AC1 14 LYS A 206 ? LYS A 206 . ? 1_555 ? 5 AC1 14 HIS A 207 ? HIS A 207 . ? 1_555 ? 6 AC1 14 MET A 250 ? MET A 250 . ? 1_555 ? 7 AC1 14 TYR A 253 ? TYR A 253 . ? 1_555 ? 8 AC1 14 ASP A 285 ? ASP A 285 . ? 1_555 ? 9 AC1 14 ARG A 291 ? ARG A 291 . ? 1_555 ? 10 AC1 14 MET A 316 ? MET A 316 . ? 1_555 ? 11 AC1 14 GLU A 491 ? GLU A 491 . ? 1_555 ? 12 AC1 14 HOH O . ? HOH A 801 . ? 1_555 ? 13 AC1 14 HOH O . ? HOH A 803 . ? 1_555 ? 14 AC1 14 HOH O . ? HOH A 809 . ? 1_555 ? 15 AC2 13 GLU A 220 ? GLU A 220 . ? 1_555 ? 16 AC2 13 ASN A 221 ? ASN A 221 . ? 1_555 ? 17 AC2 13 SER A 255 ? SER A 255 . ? 1_555 ? 18 AC2 13 THR A 294 ? THR A 294 . ? 1_555 ? 19 AC2 13 HOH O . ? HOH A 951 . ? 1_555 ? 20 AC2 13 HOH O . ? HOH A 1164 . ? 1_555 ? 21 AC2 13 HOH O . ? HOH A 1227 . ? 1_555 ? 22 AC2 13 HOH O . ? HOH A 1286 . ? 1_555 ? 23 AC2 13 HOH O . ? HOH A 1332 . ? 1_555 ? 24 AC2 13 HOH O . ? HOH A 1380 . ? 1_555 ? 25 AC2 13 HOH O . ? HOH A 1426 . ? 1_555 ? 26 AC2 13 HOH O . ? HOH A 1530 . ? 1_555 ? 27 AC2 13 HOH O . ? HOH A 1697 . ? 1_555 ? 28 AC3 17 TYR A 425 ? TYR A 425 . ? 1_555 ? 29 AC3 17 HIS A 487 ? HIS A 487 . ? 1_555 ? 30 AC3 17 LYS A 493 ? LYS A 493 . ? 1_555 ? 31 AC3 17 ASN A 496 ? ASN A 496 . ? 1_555 ? 32 AC3 17 ASN A 498 ? ASN A 498 . ? 1_555 ? 33 AC3 17 THR A 500 ? THR A 500 . ? 1_555 ? 34 AC3 17 PRO A 502 ? PRO A 502 . ? 1_555 ? 35 AC3 17 GLU A 503 ? GLU A 503 . ? 1_555 ? 36 AC3 17 HOH O . ? HOH A 810 . ? 1_555 ? 37 AC3 17 HOH O . ? HOH A 938 . ? 1_555 ? 38 AC3 17 HOH O . ? HOH A 1080 . ? 1_555 ? 39 AC3 17 HOH O . ? HOH A 1234 . ? 1_555 ? 40 AC3 17 HOH O . ? HOH A 1290 . ? 1_555 ? 41 AC3 17 HOH O . ? HOH A 1532 . ? 1_555 ? 42 AC3 17 HOH O . ? HOH A 1609 . ? 1_555 ? 43 AC3 17 HOH O . ? HOH A 1616 . ? 1_555 ? 44 AC3 17 HOH O . ? HOH A 1628 . ? 1_555 ? 45 AC4 11 THR A 598 ? THR A 598 . ? 1_555 ? 46 AC4 11 ASN A 600 ? ASN A 600 . ? 1_555 ? 47 AC4 11 HOH O . ? HOH A 971 . ? 1_555 ? 48 AC4 11 HOH O . ? HOH A 1241 . ? 1_555 ? 49 AC4 11 HOH O . ? HOH A 1307 . ? 1_555 ? 50 AC4 11 HOH O . ? HOH A 1314 . ? 1_555 ? 51 AC4 11 HOH O . ? HOH A 1436 . ? 1_555 ? 52 AC4 11 HOH O . ? HOH A 1518 . ? 1_555 ? 53 AC4 11 HOH O . ? HOH A 1528 . ? 1_555 ? 54 AC4 11 HOH O . ? HOH A 1608 . ? 1_555 ? 55 AC4 11 HOH O . ? HOH A 1690 . ? 1_555 ? # _database_PDB_matrix.entry_id 3WLN _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 3WLN _atom_sites.fract_transf_matrix[1][1] 0.009930 _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] 0.009930 _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] 0.005498 _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 ? 30.090 5.126 -2.341 1.00 45.85 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? 29.914 4.066 -1.323 1.00 45.97 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? 28.601 4.272 -0.600 1.00 44.95 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? 28.162 5.411 -0.417 1.00 44.20 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? 31.030 4.158 -0.267 1.00 45.61 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? 31.649 2.815 0.037 1.00 47.59 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? 32.428 2.714 0.996 1.00 49.61 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? 31.376 1.856 -0.717 1.00 52.31 ? 1 ASP A OD2 1 ATOM 9 N N . TYR A 1 2 ? 27.985 3.173 -0.169 1.00 44.86 ? 2 TYR A N 1 ATOM 10 C CA . TYR A 1 2 ? 26.921 3.242 0.842 1.00 43.41 ? 2 TYR A CA 1 ATOM 11 C C . TYR A 1 2 ? 27.528 3.723 2.172 1.00 41.33 ? 2 TYR A C 1 ATOM 12 O O . TYR A 1 2 ? 28.635 3.305 2.540 1.00 41.54 ? 2 TYR A O 1 ATOM 13 C CB . TYR A 1 2 ? 26.240 1.881 0.984 1.00 44.09 ? 2 TYR A CB 1 ATOM 14 C CG . TYR A 1 2 ? 25.435 1.676 2.254 1.00 43.13 ? 2 TYR A CG 1 ATOM 15 C CD1 . TYR A 1 2 ? 24.144 2.197 2.383 1.00 40.96 ? 2 TYR A CD1 1 ATOM 16 C CD2 . TYR A 1 2 ? 25.959 0.931 3.315 1.00 42.61 ? 2 TYR A CD2 1 ATOM 17 C CE1 . TYR A 1 2 ? 23.409 1.998 3.539 1.00 40.61 ? 2 TYR A CE1 1 ATOM 18 C CE2 . TYR A 1 2 ? 25.227 0.724 4.474 1.00 42.06 ? 2 TYR A CE2 1 ATOM 19 C CZ . TYR A 1 2 ? 23.957 1.259 4.575 1.00 41.39 ? 2 TYR A CZ 1 ATOM 20 O OH . TYR A 1 2 ? 23.242 1.045 5.718 1.00 41.97 ? 2 TYR A OH 1 ATOM 21 N N . VAL A 1 3 ? 26.814 4.611 2.867 1.00 39.55 ? 3 VAL A N 1 ATOM 22 C CA . VAL A 1 3 ? 27.296 5.201 4.118 1.00 37.33 ? 3 VAL A CA 1 ATOM 23 C C . VAL A 1 3 ? 26.357 4.801 5.265 1.00 36.84 ? 3 VAL A C 1 ATOM 24 O O . VAL A 1 3 ? 25.284 5.384 5.439 1.00 36.26 ? 3 VAL A O 1 ATOM 25 C CB . VAL A 1 3 ? 27.431 6.754 4.014 1.00 36.46 ? 3 VAL A CB 1 ATOM 26 C CG1 . VAL A 1 3 ? 27.946 7.364 5.323 1.00 34.93 ? 3 VAL A CG1 1 ATOM 27 C CG2 . VAL A 1 3 ? 28.348 7.143 2.869 1.00 36.85 ? 3 VAL A CG2 1 ATOM 28 N N . LEU A 1 4 ? 26.787 3.816 6.052 1.00 36.74 ? 4 LEU A N 1 ATOM 29 C CA . LEU A 1 4 ? 25.934 3.173 7.048 1.00 36.58 ? 4 LEU A CA 1 ATOM 30 C C . LEU A 1 4 ? 25.343 4.146 8.063 1.00 35.08 ? 4 LEU A C 1 ATOM 31 O O . LEU A 1 4 ? 24.161 4.062 8.348 1.00 35.10 ? 4 LEU A O 1 ATOM 32 C CB . LEU A 1 4 ? 26.677 2.021 7.750 1.00 37.15 ? 4 LEU A CB 1 ATOM 33 C CG . LEU A 1 4 ? 25.856 0.978 8.527 1.00 37.55 ? 4 LEU A CG 1 ATOM 34 C CD1 . LEU A 1 4 ? 26.571 -0.361 8.514 1.00 39.50 ? 4 LEU A CD1 1 ATOM 35 C CD2 . LEU A 1 4 ? 25.537 1.406 9.949 1.00 34.88 ? 4 LEU A CD2 1 ATOM 36 N N . TYR A 1 5 ? 26.152 5.078 8.576 1.00 33.69 ? 5 TYR A N 1 ATOM 37 C CA . TYR A 1 5 ? 25.706 5.967 9.655 1.00 32.66 ? 5 TYR A CA 1 ATOM 38 C C . TYR A 1 5 ? 24.586 6.910 9.233 1.00 32.69 ? 5 TYR A C 1 ATOM 39 O O . TYR A 1 5 ? 23.880 7.453 10.073 1.00 31.79 ? 5 TYR A O 1 ATOM 40 C CB . TYR A 1 5 ? 26.879 6.735 10.298 1.00 31.23 ? 5 TYR A CB 1 ATOM 41 C CG . TYR A 1 5 ? 27.315 8.019 9.594 1.00 29.93 ? 5 TYR A CG 1 ATOM 42 C CD1 . TYR A 1 5 ? 26.653 9.239 9.822 1.00 27.59 ? 5 TYR A CD1 1 ATOM 43 C CD2 . TYR A 1 5 ? 28.414 8.016 8.724 1.00 29.53 ? 5 TYR A CD2 1 ATOM 44 C CE1 . TYR A 1 5 ? 27.070 10.424 9.188 1.00 26.80 ? 5 TYR A CE1 1 ATOM 45 C CE2 . TYR A 1 5 ? 28.838 9.180 8.086 1.00 28.94 ? 5 TYR A CE2 1 ATOM 46 C CZ . TYR A 1 5 ? 28.169 10.377 8.318 1.00 29.09 ? 5 TYR A CZ 1 ATOM 47 O OH . TYR A 1 5 ? 28.608 11.513 7.674 1.00 28.10 ? 5 TYR A OH 1 ATOM 48 N N . LYS A 1 6 ? 24.439 7.101 7.927 1.00 34.12 ? 6 LYS A N 1 ATOM 49 C CA . LYS A 1 6 ? 23.385 7.958 7.388 1.00 34.77 ? 6 LYS A CA 1 ATOM 50 C C . LYS A 1 6 ? 22.074 7.200 7.178 1.00 35.86 ? 6 LYS A C 1 ATOM 51 O O . LYS A 1 6 ? 21.047 7.798 6.861 1.00 36.20 ? 6 LYS A O 1 ATOM 52 C CB . LYS A 1 6 ? 23.864 8.634 6.097 1.00 35.32 ? 6 LYS A CB 1 ATOM 53 C CG . LYS A 1 6 ? 24.749 9.840 6.393 1.00 35.13 ? 6 LYS A CG 1 ATOM 54 C CD . LYS A 1 6 ? 25.312 10.492 5.142 1.00 37.26 ? 6 LYS A CD 1 ATOM 55 C CE . LYS A 1 6 ? 25.994 11.809 5.523 1.00 36.98 ? 6 LYS A CE 1 ATOM 56 N NZ . LYS A 1 6 ? 26.789 12.358 4.382 1.00 38.66 ? 6 LYS A NZ 1 ATOM 57 N N . ASP A 1 7 ? 22.118 5.886 7.380 1.00 36.47 ? 7 ASP A N 1 ATOM 58 C CA . ASP A 1 7 ? 20.977 5.024 7.129 1.00 37.26 ? 7 ASP A CA 1 ATOM 59 C C . ASP A 1 7 ? 20.135 4.889 8.401 1.00 36.90 ? 7 ASP A C 1 ATOM 60 O O . ASP A 1 7 ? 20.541 4.220 9.357 1.00 36.98 ? 7 ASP A O 1 ATOM 61 C CB . ASP A 1 7 ? 21.466 3.667 6.628 1.00 38.32 ? 7 ASP A CB 1 ATOM 62 C CG . ASP A 1 7 ? 20.334 2.736 6.228 1.00 39.49 ? 7 ASP A CG 1 ATOM 63 O OD1 . ASP A 1 7 ? 19.147 3.048 6.469 1.00 40.00 ? 7 ASP A OD1 1 ATOM 64 O OD2 . ASP A 1 7 ? 20.646 1.666 5.683 1.00 41.58 ? 7 ASP A OD2 1 ATOM 65 N N . ALA A 1 8 ? 18.964 5.527 8.394 1.00 36.26 ? 8 ALA A N 1 ATOM 66 C CA . ALA A 1 8 ? 18.064 5.563 9.550 1.00 36.26 ? 8 ALA A CA 1 ATOM 67 C C . ALA A 1 8 ? 17.558 4.201 10.025 1.00 37.16 ? 8 ALA A C 1 ATOM 68 O O . ALA A 1 8 ? 17.163 4.059 11.178 1.00 37.45 ? 8 ALA A O 1 ATOM 69 C CB . ALA A 1 8 ? 16.882 6.491 9.267 1.00 35.90 ? 8 ALA A CB 1 ATOM 70 N N . THR A 1 9 ? 17.571 3.211 9.137 1.00 38.83 ? 9 THR A N 1 ATOM 71 C CA . THR A 1 9 ? 17.020 1.882 9.423 1.00 39.82 ? 9 THR A CA 1 ATOM 72 C C . THR A 1 9 ? 18.003 0.952 10.152 1.00 39.93 ? 9 THR A C 1 ATOM 73 O O . THR A 1 9 ? 17.657 -0.185 10.477 1.00 41.38 ? 9 THR A O 1 ATOM 74 C CB . THR A 1 9 ? 16.564 1.184 8.130 1.00 41.38 ? 9 THR A CB 1 ATOM 75 O OG1 . THR A 1 9 ? 17.711 0.820 7.346 1.00 41.60 ? 9 THR A OG1 1 ATOM 76 C CG2 . THR A 1 9 ? 15.655 2.091 7.314 1.00 41.77 ? 9 THR A CG2 1 ATOM 77 N N . LYS A 1 10 ? 19.225 1.433 10.384 1.00 38.53 ? 10 LYS A N 1 ATOM 78 C CA . LYS A 1 10 ? 20.297 0.636 10.978 1.00 37.91 ? 10 LYS A CA 1 ATOM 79 C C . LYS A 1 10 ? 20.343 0.811 12.507 1.00 36.37 ? 10 LYS A C 1 ATOM 80 O O . LYS A 1 10 ? 19.960 1.861 13.012 1.00 35.01 ? 10 LYS A O 1 ATOM 81 C CB . LYS A 1 10 ? 21.640 1.031 10.353 1.00 37.77 ? 10 LYS A CB 1 ATOM 82 C CG . LYS A 1 10 ? 21.812 0.613 8.897 1.00 39.01 ? 10 LYS A CG 1 ATOM 83 C CD . LYS A 1 10 ? 22.088 -0.868 8.776 1.00 40.39 ? 10 LYS A CD 1 ATOM 84 C CE . LYS A 1 10 ? 21.779 -1.357 7.372 1.00 43.39 ? 10 LYS A CE 1 ATOM 85 N NZ . LYS A 1 10 ? 22.080 -2.796 7.237 1.00 45.51 ? 10 LYS A NZ 1 ATOM 86 N N . PRO A 1 11 ? 20.779 -0.232 13.248 1.00 36.40 ? 11 PRO A N 1 ATOM 87 C CA . PRO A 1 11 ? 20.908 -0.110 14.702 1.00 35.49 ? 11 PRO A CA 1 ATOM 88 C C . PRO A 1 11 ? 21.840 1.024 15.118 1.00 34.03 ? 11 PRO A C 1 ATOM 89 O O . PRO A 1 11 ? 22.824 1.309 14.423 1.00 33.67 ? 11 PRO A O 1 ATOM 90 C CB . PRO A 1 11 ? 21.498 -1.466 15.111 1.00 36.75 ? 11 PRO A CB 1 ATOM 91 C CG . PRO A 1 11 ? 21.045 -2.395 14.042 1.00 37.67 ? 11 PRO A CG 1 ATOM 92 C CD . PRO A 1 11 ? 21.125 -1.591 12.789 1.00 37.73 ? 11 PRO A CD 1 ATOM 93 N N . VAL A 1 12 ? 21.521 1.655 16.245 1.00 32.52 ? 12 VAL A N 1 ATOM 94 C CA . VAL A 1 12 ? 22.293 2.786 16.768 1.00 30.67 ? 12 VAL A CA 1 ATOM 95 C C . VAL A 1 12 ? 23.783 2.437 16.881 1.00 30.63 ? 12 VAL A C 1 ATOM 96 O O . VAL A 1 12 ? 24.631 3.174 16.384 1.00 29.66 ? 12 VAL A O 1 ATOM 97 C CB . VAL A 1 12 ? 21.715 3.296 18.123 1.00 29.68 ? 12 VAL A CB 1 ATOM 98 C CG1 . VAL A 1 12 ? 22.720 4.167 18.888 1.00 27.27 ? 12 VAL A CG1 1 ATOM 99 C CG2 . VAL A 1 12 ? 20.398 4.057 17.884 1.00 30.16 ? 12 VAL A CG2 1 ATOM 100 N N . GLU A 1 13 ? 24.084 1.301 17.506 1.00 31.39 ? 13 GLU A N 1 ATOM 101 C CA . GLU A 1 13 ? 25.470 0.892 17.726 1.00 31.87 ? 13 GLU A CA 1 ATOM 102 C C . GLU A 1 13 ? 26.287 0.789 16.429 1.00 32.19 ? 13 GLU A C 1 ATOM 103 O O . GLU A 1 13 ? 27.450 1.175 16.393 1.00 31.92 ? 13 GLU A O 1 ATOM 104 C CB . GLU A 1 13 ? 25.535 -0.412 18.535 1.00 32.78 ? 13 GLU A CB 1 ATOM 105 C CG . GLU A 1 13 ? 24.922 -0.299 19.946 1.00 32.93 ? 13 GLU A CG 1 ATOM 106 C CD . GLU A 1 13 ? 25.512 0.846 20.764 1.00 34.21 ? 13 GLU A CD 1 ATOM 107 O OE1 . GLU A 1 13 ? 26.762 0.985 20.787 1.00 33.93 ? 13 GLU A OE1 1 ATOM 108 O OE2 . GLU A 1 13 ? 24.723 1.608 21.388 1.00 35.40 ? 13 GLU A OE2 1 ATOM 109 N N . ASP A 1 14 ? 25.653 0.276 15.379 1.00 33.19 ? 14 ASP A N 1 ATOM 110 C CA . ASP A 1 14 ? 26.234 0.182 14.039 1.00 33.50 ? 14 ASP A CA 1 ATOM 111 C C . ASP A 1 14 ? 26.500 1.551 13.425 1.00 31.68 ? 14 ASP A C 1 ATOM 112 O O . ASP A 1 14 ? 27.546 1.776 12.828 1.00 31.48 ? 14 ASP A O 1 ATOM 113 C CB . ASP A 1 14 ? 25.287 -0.579 13.114 1.00 34.77 ? 14 ASP A CB 1 ATOM 114 C CG . ASP A 1 14 ? 25.168 -2.042 13.463 1.00 38.79 ? 14 ASP A CG 1 ATOM 115 O OD1 . ASP A 1 14 ? 24.162 -2.645 13.056 1.00 43.35 ? 14 ASP A OD1 1 ATOM 116 O OD2 . ASP A 1 14 ? 26.067 -2.604 14.118 1.00 41.31 ? 14 ASP A OD2 1 ATOM 117 N N . ARG A 1 15 ? 25.533 2.452 13.559 1.00 30.63 ? 15 ARG A N 1 ATOM 118 C CA . ARG A 1 15 ? 25.676 3.817 13.052 1.00 29.06 ? 15 ARG A CA 1 ATOM 119 C C . ARG A 1 15 ? 26.762 4.565 13.814 1.00 28.25 ? 15 ARG A C 1 ATOM 120 O O . ARG A 1 15 ? 27.583 5.273 13.199 1.00 27.68 ? 15 ARG A O 1 ATOM 121 C CB . ARG A 1 15 ? 24.339 4.561 13.114 1.00 28.17 ? 15 ARG A CB 1 ATOM 122 C CG . ARG A 1 15 ? 23.247 3.905 12.269 1.00 28.65 ? 15 ARG A CG 1 ATOM 123 C CD . ARG A 1 15 ? 21.928 4.635 12.410 1.00 29.30 ? 15 ARG A CD 1 ATOM 124 N NE . ARG A 1 15 ? 21.939 5.893 11.653 1.00 29.49 ? 15 ARG A NE 1 ATOM 125 C CZ . ARG A 1 15 ? 21.002 6.842 11.735 1.00 28.48 ? 15 ARG A CZ 1 ATOM 126 N NH1 . ARG A 1 15 ? 19.958 6.686 12.544 1.00 25.27 ? 15 ARG A NH1 1 ATOM 127 N NH2 . ARG A 1 15 ? 21.112 7.955 11.002 1.00 25.53 ? 15 ARG A NH2 1 ATOM 128 N N . VAL A 1 16 ? 26.777 4.399 15.144 1.00 27.22 ? 16 VAL A N 1 ATOM 129 C CA . VAL A 1 16 ? 27.826 5.013 15.973 1.00 26.52 ? 16 VAL A CA 1 ATOM 130 C C . VAL A 1 16 ? 29.214 4.568 15.504 1.00 27.37 ? 16 VAL A C 1 ATOM 131 O O . VAL A 1 16 ? 30.084 5.417 15.281 1.00 26.50 ? 16 VAL A O 1 ATOM 132 C CB . VAL A 1 16 ? 27.650 4.740 17.511 1.00 26.50 ? 16 VAL A CB 1 ATOM 133 C CG1 . VAL A 1 16 ? 28.891 5.202 18.284 1.00 25.38 ? 16 VAL A CG1 1 ATOM 134 C CG2 . VAL A 1 16 ? 26.400 5.438 18.050 1.00 24.34 ? 16 VAL A CG2 1 ATOM 135 N N . ALA A 1 17 ? 29.401 3.248 15.354 1.00 28.38 ? 17 ALA A N 1 ATOM 136 C CA . ALA A 1 17 ? 30.698 2.674 15.004 1.00 29.61 ? 17 ALA A CA 1 ATOM 137 C C . ALA A 1 17 ? 31.132 3.084 13.604 1.00 30.39 ? 17 ALA A C 1 ATOM 138 O O . ALA A 1 17 ? 32.314 3.379 13.367 1.00 30.40 ? 17 ALA A O 1 ATOM 139 C CB . ALA A 1 17 ? 30.666 1.142 15.118 1.00 31.06 ? 17 ALA A CB 1 ATOM 140 N N . ASP A 1 18 ? 30.174 3.096 12.681 1.00 30.21 ? 18 ASP A N 1 ATOM 141 C CA . ASP A 1 18 ? 30.447 3.491 11.315 1.00 31.02 ? 18 ASP A CA 1 ATOM 142 C C . ASP A 1 18 ? 30.922 4.938 11.222 1.00 29.88 ? 18 ASP A C 1 ATOM 143 O O . ASP A 1 18 ? 31.881 5.216 10.514 1.00 30.54 ? 18 ASP A O 1 ATOM 144 C CB . ASP A 1 18 ? 29.229 3.276 10.415 1.00 31.14 ? 18 ASP A CB 1 ATOM 145 C CG . ASP A 1 18 ? 29.533 3.573 8.967 1.00 33.35 ? 18 ASP A CG 1 ATOM 146 O OD1 . ASP A 1 18 ? 29.180 4.677 8.499 1.00 34.49 ? 18 ASP A OD1 1 ATOM 147 O OD2 . ASP A 1 18 ? 30.151 2.717 8.299 1.00 34.10 ? 18 ASP A OD2 1 ATOM 148 N N . LEU A 1 19 ? 30.247 5.846 11.928 1.00 29.05 ? 19 LEU A N 1 ATOM 149 C CA . LEU A 1 19 ? 30.601 7.263 11.904 1.00 28.25 ? 19 LEU A CA 1 ATOM 150 C C . LEU A 1 19 ? 31.926 7.528 12.621 1.00 28.23 ? 19 LEU A C 1 ATOM 151 O O . LEU A 1 19 ? 32.804 8.189 12.068 1.00 28.56 ? 19 LEU A O 1 ATOM 152 C CB . LEU A 1 19 ? 29.483 8.122 12.527 1.00 27.32 ? 19 LEU A CB 1 ATOM 153 C CG . LEU A 1 19 ? 29.739 9.633 12.674 1.00 26.18 ? 19 LEU A CG 1 ATOM 154 C CD1 . LEU A 1 19 ? 30.249 10.250 11.362 1.00 27.46 ? 19 LEU A CD1 1 ATOM 155 C CD2 . LEU A 1 19 ? 28.486 10.363 13.178 1.00 25.59 ? 19 LEU A CD2 1 ATOM 156 N N . LEU A 1 20 ? 32.054 7.033 13.854 1.00 28.21 ? 20 LEU A N 1 ATOM 157 C CA . LEU A 1 20 ? 33.298 7.152 14.616 1.00 28.51 ? 20 LEU A CA 1 ATOM 158 C C . LEU A 1 20 ? 34.524 6.767 13.764 1.00 29.67 ? 20 LEU A C 1 ATOM 159 O O . LEU A 1 20 ? 35.538 7.470 13.764 1.00 30.08 ? 20 LEU A O 1 ATOM 160 C CB . LEU A 1 20 ? 33.247 6.276 15.869 1.00 28.65 ? 20 LEU A CB 1 ATOM 161 C CG . LEU A 1 20 ? 34.463 6.320 16.808 1.00 28.29 ? 20 LEU A CG 1 ATOM 162 C CD1 . LEU A 1 20 ? 34.591 7.703 17.473 1.00 27.84 ? 20 LEU A CD1 1 ATOM 163 C CD2 . LEU A 1 20 ? 34.375 5.218 17.859 1.00 29.12 ? 20 LEU A CD2 1 ATOM 164 N N . GLY A 1 21 ? 34.411 5.657 13.040 1.00 30.59 ? 21 GLY A N 1 ATOM 165 C CA . GLY A 1 21 ? 35.513 5.135 12.235 1.00 31.98 ? 21 GLY A CA 1 ATOM 166 C C . GLY A 1 21 ? 35.924 6.028 11.072 1.00 31.84 ? 21 GLY A C 1 ATOM 167 O O . GLY A 1 21 ? 36.964 5.814 10.473 1.00 32.82 ? 21 GLY A O 1 ATOM 168 N N . ARG A 1 22 ? 35.112 7.027 10.755 1.00 31.26 ? 22 ARG A N 1 ATOM 169 C CA . ARG A 1 22 ? 35.396 7.943 9.649 1.00 31.22 ? 22 ARG A CA 1 ATOM 170 C C . ARG A 1 22 ? 35.985 9.273 10.133 1.00 30.50 ? 22 ARG A C 1 ATOM 171 O O . ARG A 1 22 ? 36.450 10.070 9.319 1.00 30.92 ? 22 ARG A O 1 ATOM 172 C CB . ARG A 1 22 ? 34.106 8.244 8.872 1.00 31.10 ? 22 ARG A CB 1 ATOM 173 C CG . ARG A 1 22 ? 33.479 7.041 8.176 1.00 32.10 ? 22 ARG A CG 1 ATOM 174 C CD . ARG A 1 22 ? 32.066 7.392 7.695 1.00 32.11 ? 22 ARG A CD 1 ATOM 175 N NE . ARG A 1 22 ? 31.302 6.220 7.256 1.00 33.21 ? 22 ARG A NE 1 ATOM 176 C CZ . ARG A 1 22 ? 31.383 5.659 6.054 1.00 34.25 ? 22 ARG A CZ 1 ATOM 177 N NH1 . ARG A 1 22 ? 30.643 4.592 5.774 1.00 35.97 ? 22 ARG A NH1 1 ATOM 178 N NH2 . ARG A 1 22 ? 32.203 6.146 5.130 1.00 34.58 ? 22 ARG A NH2 1 ATOM 179 N N . MET A 1 23 ? 35.956 9.510 11.447 1.00 29.01 ? 23 MET A N 1 ATOM 180 C CA . MET A 1 23 ? 36.204 10.843 12.007 1.00 28.23 ? 23 MET A CA 1 ATOM 181 C C . MET A 1 23 ? 37.675 11.174 12.255 1.00 28.50 ? 23 MET A C 1 ATOM 182 O O . MET A 1 23 ? 38.427 10.330 12.722 1.00 29.61 ? 23 MET A O 1 ATOM 183 C CB . MET A 1 23 ? 35.424 11.015 13.320 1.00 27.44 ? 23 MET A CB 1 ATOM 184 C CG . MET A 1 23 ? 33.912 10.926 13.172 1.00 25.40 ? 23 MET A CG 1 ATOM 185 S SD . MET A 1 23 ? 33.062 10.951 14.759 1.00 25.99 ? 23 MET A SD 1 ATOM 186 C CE . MET A 1 23 ? 33.281 12.678 15.210 1.00 22.39 ? 23 MET A CE 1 ATOM 187 N N . THR A 1 24 ? 38.068 12.411 11.952 1.00 27.95 ? 24 THR A N 1 ATOM 188 C CA . THR A 1 24 ? 39.406 12.918 12.285 1.00 27.71 ? 24 THR A CA 1 ATOM 189 C C . THR A 1 24 ? 39.461 13.274 13.769 1.00 27.38 ? 24 THR A C 1 ATOM 190 O O . THR A 1 24 ? 38.421 13.382 14.421 1.00 26.43 ? 24 THR A O 1 ATOM 191 C CB . THR A 1 24 ? 39.758 14.188 11.482 1.00 27.86 ? 24 THR A CB 1 ATOM 192 O OG1 . THR A 1 24 ? 38.915 15.275 11.899 1.00 27.06 ? 24 THR A OG1 1 ATOM 193 C CG2 . THR A 1 24 ? 39.595 13.942 9.968 1.00 27.37 ? 24 THR A CG2 1 ATOM 194 N N . LEU A 1 25 ? 40.670 13.480 14.292 1.00 27.27 ? 25 LEU A N 1 ATOM 195 C CA . LEU A 1 25 ? 40.838 13.922 15.671 1.00 27.04 ? 25 LEU A CA 1 ATOM 196 C C . LEU A 1 25 ? 40.089 15.233 15.923 1.00 25.96 ? 25 LEU A C 1 ATOM 197 O O . LEU A 1 25 ? 39.386 15.364 16.925 1.00 25.40 ? 25 LEU A O 1 ATOM 198 C CB . LEU A 1 25 ? 42.324 14.070 16.024 1.00 27.81 ? 25 LEU A CB 1 ATOM 199 C CG . LEU A 1 25 ? 42.573 14.596 17.443 1.00 27.99 ? 25 LEU A CG 1 ATOM 200 C CD1 . LEU A 1 25 ? 41.857 13.711 18.507 1.00 29.22 ? 25 LEU A CD1 1 ATOM 201 C CD2 . LEU A 1 25 ? 44.071 14.740 17.724 1.00 28.31 ? 25 LEU A CD2 1 ATOM 202 N N . ALA A 1 26 ? 40.224 16.183 14.997 1.00 25.72 ? 26 ALA A N 1 ATOM 203 C CA . ALA A 1 26 ? 39.509 17.468 15.052 1.00 25.21 ? 26 ALA A CA 1 ATOM 204 C C . ALA A 1 26 ? 37.990 17.298 15.166 1.00 24.52 ? 26 ALA A C 1 ATOM 205 O O . ALA A 1 26 ? 37.319 18.018 15.934 1.00 24.49 ? 26 ALA A O 1 ATOM 206 C CB . ALA A 1 26 ? 39.855 18.310 13.826 1.00 25.67 ? 26 ALA A CB 1 ATOM 207 N N . GLU A 1 27 ? 37.452 16.361 14.388 1.00 24.43 ? 27 GLU A N 1 ATOM 208 C CA . GLU A 1 27 ? 36.007 16.089 14.350 1.00 23.52 ? 27 GLU A CA 1 ATOM 209 C C . GLU A 1 27 ? 35.555 15.423 15.649 1.00 23.42 ? 27 GLU A C 1 ATOM 210 O O . GLU A 1 27 ? 34.460 15.700 16.167 1.00 22.13 ? 27 GLU A O 1 ATOM 211 C CB . GLU A 1 27 ? 35.657 15.238 13.121 1.00 23.44 ? 27 GLU A CB 1 ATOM 212 C CG . GLU A 1 27 ? 35.705 16.055 11.823 1.00 23.45 ? 27 GLU A CG 1 ATOM 213 C CD . GLU A 1 27 ? 35.702 15.209 10.552 1.00 24.66 ? 27 GLU A CD 1 ATOM 214 O OE1 . GLU A 1 27 ? 36.136 14.041 10.589 1.00 25.10 ? 27 GLU A OE1 1 ATOM 215 O OE2 . GLU A 1 27 ? 35.274 15.728 9.495 1.00 26.29 ? 27 GLU A OE2 1 ATOM 216 N N . LYS A 1 28 ? 36.430 14.569 16.174 1.00 23.87 ? 28 LYS A N 1 ATOM 217 C CA . LYS A 1 28 ? 36.209 13.904 17.461 1.00 24.17 ? 28 LYS A CA 1 ATOM 218 C C . LYS A 1 28 ? 36.195 14.885 18.618 1.00 24.05 ? 28 LYS A C 1 ATOM 219 O O . LYS A 1 28 ? 35.234 14.923 19.395 1.00 23.03 ? 28 LYS A O 1 ATOM 220 C CB . LYS A 1 28 ? 37.263 12.828 17.697 1.00 24.54 ? 28 LYS A CB 1 ATOM 221 C CG . LYS A 1 28 ? 37.016 11.615 16.863 1.00 24.44 ? 28 LYS A CG 1 ATOM 222 C CD . LYS A 1 28 ? 38.052 10.562 17.091 1.00 24.06 ? 28 LYS A CD 1 ATOM 223 C CE . LYS A 1 28 ? 37.892 9.472 16.061 1.00 24.86 ? 28 LYS A CE 1 ATOM 224 N NZ . LYS A 1 28 ? 38.883 8.403 16.308 1.00 26.76 ? 28 LYS A NZ 1 ATOM 225 N N . ILE A 1 29 ? 37.250 15.690 18.718 1.00 24.31 ? 29 ILE A N 1 ATOM 226 C CA . ILE A 1 29 ? 37.327 16.700 19.771 1.00 23.97 ? 29 ILE A CA 1 ATOM 227 C C . ILE A 1 29 ? 36.194 17.732 19.636 1.00 23.65 ? 29 ILE A C 1 ATOM 228 O O . ILE A 1 29 ? 35.632 18.191 20.632 1.00 23.72 ? 29 ILE A O 1 ATOM 229 C CB . ILE A 1 29 ? 38.755 17.318 19.852 1.00 24.35 ? 29 ILE A CB 1 ATOM 230 C CG1 . ILE A 1 29 ? 39.711 16.269 20.443 1.00 24.85 ? 29 ILE A CG1 1 ATOM 231 C CG2 . ILE A 1 29 ? 38.752 18.631 20.673 1.00 24.20 ? 29 ILE A CG2 1 ATOM 232 C CD1 . ILE A 1 29 ? 41.213 16.562 20.279 1.00 26.01 ? 29 ILE A CD1 1 ATOM 233 N N . GLY A 1 30 ? 35.839 18.073 18.401 1.00 24.07 ? 30 GLY A N 1 ATOM 234 C CA . GLY A 1 30 ? 34.672 18.922 18.131 1.00 23.23 ? 30 GLY A CA 1 ATOM 235 C C . GLY A 1 30 ? 33.386 18.439 18.785 1.00 22.47 ? 30 GLY A C 1 ATOM 236 O O . GLY A 1 30 ? 32.673 19.236 19.377 1.00 22.76 ? 30 GLY A O 1 ATOM 237 N N . GLN A 1 31 ? 33.096 17.142 18.688 1.00 22.34 ? 31 GLN A N 1 ATOM 238 C CA . GLN A 1 31 ? 31.892 16.562 19.286 1.00 22.51 ? 31 GLN A CA 1 ATOM 239 C C . GLN A 1 31 ? 31.856 16.737 20.794 1.00 22.88 ? 31 GLN A C 1 ATOM 240 O O . GLN A 1 31 ? 30.779 16.904 21.377 1.00 22.46 ? 31 GLN A O 1 ATOM 241 C CB . GLN A 1 31 ? 31.750 15.076 18.941 1.00 22.88 ? 31 GLN A CB 1 ATOM 242 C CG . GLN A 1 31 ? 31.195 14.795 17.531 1.00 22.64 ? 31 GLN A CG 1 ATOM 243 C CD . GLN A 1 31 ? 29.857 15.474 17.269 1.00 22.51 ? 31 GLN A CD 1 ATOM 244 O OE1 . GLN A 1 31 ? 28.871 15.224 17.971 1.00 23.16 ? 31 GLN A OE1 1 ATOM 245 N NE2 . GLN A 1 31 ? 29.813 16.327 16.253 1.00 19.74 ? 31 GLN A NE2 1 ATOM 246 N N . MET A 1 32 ? 33.046 16.720 21.407 1.00 23.19 ? 32 MET A N 1 ATOM 247 C CA . MET A 1 32 ? 33.224 16.801 22.850 1.00 22.51 ? 32 MET A CA 1 ATOM 248 C C . MET A 1 32 ? 33.119 18.252 23.354 1.00 22.44 ? 32 MET A C 1 ATOM 249 O O . MET A 1 32 ? 33.186 18.525 24.569 1.00 22.35 ? 32 MET A O 1 ATOM 250 C CB . MET A 1 32 ? 34.586 16.216 23.207 1.00 23.39 ? 32 MET A CB 1 ATOM 251 C CG . MET A 1 32 ? 34.802 14.741 22.819 1.00 23.10 ? 32 MET A CG 1 ATOM 252 S SD . MET A 1 32 ? 36.504 14.167 23.203 1.00 24.89 ? 32 MET A SD 1 ATOM 253 C CE . MET A 1 32 ? 36.548 14.395 24.978 1.00 24.25 ? 32 MET A CE 1 ATOM 254 N N . THR A 1 33 ? 32.972 19.183 22.420 1.00 22.05 ? 33 THR A N 1 ATOM 255 C CA . THR A 1 33 ? 32.922 20.603 22.750 1.00 21.94 ? 33 THR A CA 1 ATOM 256 C C . THR A 1 33 ? 31.490 21.174 22.723 1.00 22.11 ? 33 THR A C 1 ATOM 257 O O . THR A 1 33 ? 30.823 21.141 21.689 1.00 21.98 ? 33 THR A O 1 ATOM 258 C CB . THR A 1 33 ? 33.845 21.414 21.791 1.00 22.46 ? 33 THR A CB 1 ATOM 259 O OG1 . THR A 1 33 ? 35.133 20.780 21.714 1.00 21.58 ? 33 THR A OG1 1 ATOM 260 C CG2 . THR A 1 33 ? 34.012 22.866 22.271 1.00 21.54 ? 33 THR A CG2 1 ATOM 261 N N . GLN A 1 34 ? 31.043 21.709 23.863 1.00 21.74 ? 34 GLN A N 1 ATOM 262 C CA . GLN A 1 34 ? 29.814 22.493 23.931 1.00 21.25 ? 34 GLN A CA 1 ATOM 263 C C . GLN A 1 34 ? 30.126 23.959 24.180 1.00 21.64 ? 34 GLN A C 1 ATOM 264 O O . GLN A 1 34 ? 30.872 24.294 25.107 1.00 22.15 ? 34 GLN A O 1 ATOM 265 C CB . GLN A 1 34 ? 28.882 21.970 25.023 1.00 20.84 ? 34 GLN A CB 1 ATOM 266 C CG . GLN A 1 34 ? 27.557 22.746 25.141 1.00 19.91 ? 34 GLN A CG 1 ATOM 267 C CD . GLN A 1 34 ? 26.702 22.212 26.256 1.00 20.63 ? 34 GLN A CD 1 ATOM 268 O OE1 . GLN A 1 34 ? 26.932 22.516 27.413 1.00 21.91 ? 34 GLN A OE1 1 ATOM 269 N NE2 . GLN A 1 34 ? 25.720 21.382 25.917 1.00 21.57 ? 34 GLN A NE2 1 ATOM 270 N N . ILE A 1 35 ? 29.558 24.832 23.348 1.00 21.53 ? 35 ILE A N 1 ATOM 271 C CA . ILE A 1 35 ? 29.819 26.267 23.452 1.00 21.95 ? 35 ILE A CA 1 ATOM 272 C C . ILE A 1 35 ? 28.522 27.058 23.626 1.00 21.87 ? 35 ILE A C 1 ATOM 273 O O . ILE A 1 35 ? 27.455 26.627 23.202 1.00 21.08 ? 35 ILE A O 1 ATOM 274 C CB . ILE A 1 35 ? 30.665 26.820 22.241 1.00 22.18 ? 35 ILE A CB 1 ATOM 275 C CG1 . ILE A 1 35 ? 29.825 26.891 20.945 1.00 23.19 ? 35 ILE A CG1 1 ATOM 276 C CG2 . ILE A 1 35 ? 31.942 25.994 22.074 1.00 22.47 ? 35 ILE A CG2 1 ATOM 277 C CD1 . ILE A 1 35 ? 30.587 27.421 19.708 1.00 22.39 ? 35 ILE A CD1 1 ATOM 278 N N . GLU A 1 36 ? 28.643 28.208 24.270 1.00 22.60 ? 36 GLU A N 1 ATOM 279 C CA . GLU A 1 36 ? 27.553 29.157 24.426 1.00 22.92 ? 36 GLU A CA 1 ATOM 280 C C . GLU A 1 36 ? 27.127 29.720 23.072 1.00 23.34 ? 36 GLU A C 1 ATOM 281 O O . GLU A 1 36 ? 27.982 30.058 22.237 1.00 23.82 ? 36 GLU A O 1 ATOM 282 C CB . GLU A 1 36 ? 28.011 30.322 25.320 1.00 23.19 ? 36 GLU A CB 1 ATOM 283 C CG . GLU A 1 36 ? 27.219 30.478 26.605 1.00 23.43 ? 36 GLU A CG 1 ATOM 284 C CD . GLU A 1 36 ? 25.826 31.129 26.408 1.00 24.68 ? 36 GLU A CD 1 ATOM 285 O OE1 . GLU A 1 36 ? 25.575 31.721 25.354 1.00 24.81 ? 36 GLU A OE1 1 ATOM 286 O OE2 . GLU A 1 36 ? 24.977 31.059 27.325 1.00 27.66 ? 36 GLU A OE2 1 ATOM 287 N N . ARG A 1 37 ? 25.812 29.850 22.862 1.00 22.66 ? 37 ARG A N 1 ATOM 288 C CA . ARG A 1 37 ? 25.311 30.599 21.692 1.00 23.18 ? 37 ARG A CA 1 ATOM 289 C C . ARG A 1 37 ? 25.988 31.967 21.541 1.00 24.12 ? 37 ARG A C 1 ATOM 290 O O . ARG A 1 37 ? 26.168 32.453 20.430 1.00 25.09 ? 37 ARG A O 1 ATOM 291 C CB . ARG A 1 37 ? 23.776 30.741 21.715 1.00 22.09 ? 37 ARG A CB 1 ATOM 292 C CG . ARG A 1 37 ? 23.230 31.370 22.979 1.00 20.54 ? 37 ARG A CG 1 ATOM 293 C CD . ARG A 1 37 ? 21.865 31.960 22.768 1.00 18.89 ? 37 ARG A CD 1 ATOM 294 N NE . ARG A 1 37 ? 21.860 33.095 21.842 1.00 18.15 ? 37 ARG A NE 1 ATOM 295 C CZ . ARG A 1 37 ? 21.987 34.362 22.227 1.00 20.38 ? 37 ARG A CZ 1 ATOM 296 N NH1 . ARG A 1 37 ? 21.954 35.341 21.334 1.00 20.43 ? 37 ARG A NH1 1 ATOM 297 N NH2 . ARG A 1 37 ? 22.163 34.653 23.510 1.00 19.49 ? 37 ARG A NH2 1 ATOM 298 N N . LEU A 1 38 ? 26.392 32.572 22.657 1.00 24.74 ? 38 LEU A N 1 ATOM 299 C CA . LEU A 1 38 ? 26.998 33.905 22.630 1.00 25.74 ? 38 LEU A CA 1 ATOM 300 C C . LEU A 1 38 ? 28.359 33.947 21.922 1.00 26.01 ? 38 LEU A C 1 ATOM 301 O O . LEU A 1 38 ? 28.768 35.009 21.432 1.00 26.34 ? 38 LEU A O 1 ATOM 302 C CB . LEU A 1 38 ? 27.079 34.505 24.046 1.00 26.23 ? 38 LEU A CB 1 ATOM 303 C CG . LEU A 1 38 ? 25.764 35.044 24.648 1.00 28.77 ? 38 LEU A CG 1 ATOM 304 C CD1 . LEU A 1 38 ? 25.877 35.340 26.156 1.00 27.69 ? 38 LEU A CD1 1 ATOM 305 C CD2 . LEU A 1 38 ? 25.305 36.302 23.909 1.00 30.60 ? 38 LEU A CD2 1 ATOM 306 N N . VAL A 1 39 ? 29.044 32.806 21.836 1.00 25.33 ? 39 VAL A N 1 ATOM 307 C CA . VAL A 1 39 ? 30.336 32.756 21.121 1.00 26.23 ? 39 VAL A CA 1 ATOM 308 C C . VAL A 1 39 ? 30.270 32.037 19.756 1.00 26.37 ? 39 VAL A C 1 ATOM 309 O O . VAL A 1 39 ? 31.263 31.942 19.040 1.00 26.75 ? 39 VAL A O 1 ATOM 310 C CB . VAL A 1 39 ? 31.478 32.161 22.002 1.00 26.49 ? 39 VAL A CB 1 ATOM 311 C CG1 . VAL A 1 39 ? 31.720 33.032 23.223 1.00 26.39 ? 39 VAL A CG1 1 ATOM 312 C CG2 . VAL A 1 39 ? 31.192 30.725 22.386 1.00 23.66 ? 39 VAL A CG2 1 ATOM 313 N N . ALA A 1 40 ? 29.081 31.547 19.416 1.00 26.12 ? 40 ALA A N 1 ATOM 314 C CA . ALA A 1 40 ? 28.872 30.718 18.249 1.00 26.02 ? 40 ALA A CA 1 ATOM 315 C C . ALA A 1 40 ? 28.554 31.548 17.019 1.00 27.28 ? 40 ALA A C 1 ATOM 316 O O . ALA A 1 40 ? 27.855 32.562 17.081 1.00 27.57 ? 40 ALA A O 1 ATOM 317 C CB . ALA A 1 40 ? 27.753 29.710 18.509 1.00 24.91 ? 40 ALA A CB 1 ATOM 318 N N . THR A 1 41 ? 29.044 31.049 15.892 1.00 27.88 ? 41 THR A N 1 ATOM 319 C CA . THR A 1 41 ? 29.024 31.695 14.603 1.00 28.46 ? 41 THR A CA 1 ATOM 320 C C . THR A 1 41 ? 28.959 30.510 13.607 1.00 28.50 ? 41 THR A C 1 ATOM 321 O O . THR A 1 41 ? 29.479 29.424 13.932 1.00 27.28 ? 41 THR A O 1 ATOM 322 C CB . THR A 1 41 ? 30.377 32.443 14.501 1.00 30.00 ? 41 THR A CB 1 ATOM 323 O OG1 . THR A 1 41 ? 30.190 33.860 14.588 1.00 32.85 ? 41 THR A OG1 1 ATOM 324 C CG2 . THR A 1 41 ? 31.121 32.085 13.325 1.00 27.29 ? 41 THR A CG2 1 ATOM 325 N N . PRO A 1 42 ? 28.338 30.694 12.404 1.00 28.53 ? 42 PRO A N 1 ATOM 326 C CA . PRO A 1 42 ? 28.369 29.619 11.396 1.00 28.44 ? 42 PRO A CA 1 ATOM 327 C C . PRO A 1 42 ? 29.780 29.071 11.111 1.00 28.03 ? 42 PRO A C 1 ATOM 328 O O . PRO A 1 42 ? 29.978 27.853 11.107 1.00 26.83 ? 42 PRO A O 1 ATOM 329 C CB . PRO A 1 42 ? 27.762 30.294 10.145 1.00 29.58 ? 42 PRO A CB 1 ATOM 330 C CG . PRO A 1 42 ? 26.810 31.298 10.713 1.00 29.01 ? 42 PRO A CG 1 ATOM 331 C CD . PRO A 1 42 ? 27.551 31.851 11.924 1.00 29.41 ? 42 PRO A CD 1 ATOM 332 N N . ASP A 1 43 ? 30.742 29.963 10.894 1.00 28.94 ? 43 ASP A N 1 ATOM 333 C CA . ASP A 1 43 ? 32.150 29.581 10.686 1.00 29.44 ? 43 ASP A CA 1 ATOM 334 C C . ASP A 1 43 ? 32.773 28.842 11.869 1.00 28.15 ? 43 ASP A C 1 ATOM 335 O O . ASP A 1 43 ? 33.469 27.841 11.681 1.00 27.50 ? 43 ASP A O 1 ATOM 336 C CB . ASP A 1 43 ? 33.009 30.817 10.370 1.00 31.31 ? 43 ASP A CB 1 ATOM 337 C CG . ASP A 1 43 ? 32.871 31.289 8.938 1.00 34.58 ? 43 ASP A CG 1 ATOM 338 O OD1 . ASP A 1 43 ? 33.096 32.494 8.706 1.00 40.11 ? 43 ASP A OD1 1 ATOM 339 O OD2 . ASP A 1 43 ? 32.563 30.473 8.037 1.00 37.37 ? 43 ASP A OD2 1 ATOM 340 N N . VAL A 1 44 ? 32.536 29.342 13.090 1.00 27.37 ? 44 VAL A N 1 ATOM 341 C CA . VAL A 1 44 ? 33.085 28.720 14.293 1.00 26.34 ? 44 VAL A CA 1 ATOM 342 C C . VAL A 1 44 ? 32.606 27.277 14.422 1.00 25.90 ? 44 VAL A C 1 ATOM 343 O O . VAL A 1 44 ? 33.408 26.360 14.658 1.00 25.38 ? 44 VAL A O 1 ATOM 344 C CB . VAL A 1 44 ? 32.753 29.541 15.582 1.00 26.09 ? 44 VAL A CB 1 ATOM 345 C CG1 . VAL A 1 44 ? 32.976 28.703 16.843 1.00 24.55 ? 44 VAL A CG1 1 ATOM 346 C CG2 . VAL A 1 44 ? 33.600 30.820 15.619 1.00 26.65 ? 44 VAL A CG2 1 ATOM 347 N N . LEU A 1 45 ? 31.301 27.089 14.228 1.00 25.53 ? 45 LEU A N 1 ATOM 348 C CA . LEU A 1 45 ? 30.656 25.789 14.386 1.00 25.24 ? 45 LEU A CA 1 ATOM 349 C C . LEU A 1 45 ? 31.129 24.812 13.325 1.00 25.90 ? 45 LEU A C 1 ATOM 350 O O . LEU A 1 45 ? 31.355 23.631 13.611 1.00 24.84 ? 45 LEU A O 1 ATOM 351 C CB . LEU A 1 45 ? 29.132 25.945 14.317 1.00 24.45 ? 45 LEU A CB 1 ATOM 352 C CG . LEU A 1 45 ? 28.441 26.711 15.459 1.00 25.06 ? 45 LEU A CG 1 ATOM 353 C CD1 . LEU A 1 45 ? 26.993 27.018 15.108 1.00 22.87 ? 45 LEU A CD1 1 ATOM 354 C CD2 . LEU A 1 45 ? 28.524 25.952 16.797 1.00 22.91 ? 45 LEU A CD2 1 ATOM 355 N N . ARG A 1 46 ? 31.264 25.320 12.097 1.00 27.20 ? 46 ARG A N 1 ATOM 356 C CA . ARG A 1 46 ? 31.732 24.542 10.956 1.00 28.90 ? 46 ARG A CA 1 ATOM 357 C C . ARG A 1 46 ? 33.221 24.201 11.128 1.00 27.98 ? 46 ARG A C 1 ATOM 358 O O . ARG A 1 46 ? 33.608 23.026 11.105 1.00 27.59 ? 46 ARG A O 1 ATOM 359 C CB . ARG A 1 46 ? 31.503 25.354 9.677 1.00 29.69 ? 46 ARG A CB 1 ATOM 360 C CG . ARG A 1 46 ? 31.457 24.566 8.391 1.00 32.85 ? 46 ARG A CG 1 ATOM 361 C CD . ARG A 1 46 ? 31.333 25.508 7.183 1.00 35.11 ? 46 ARG A CD 1 ATOM 362 N NE . ARG A 1 46 ? 29.977 26.075 7.114 1.00 43.74 ? 46 ARG A NE 1 ATOM 363 C CZ . ARG A 1 46 ? 29.656 27.369 7.252 1.00 46.49 ? 46 ARG A CZ 1 ATOM 364 N NH1 . ARG A 1 46 ? 30.590 28.301 7.457 1.00 46.20 ? 46 ARG A NH1 1 ATOM 365 N NH2 . ARG A 1 46 ? 28.377 27.736 7.166 1.00 47.89 ? 46 ARG A NH2 1 ATOM 366 N N . ASP A 1 47 ? 34.047 25.229 11.331 1.00 28.10 ? 47 ASP A N 1 ATOM 367 C CA . ASP A 1 47 ? 35.507 25.076 11.354 1.00 27.85 ? 47 ASP A CA 1 ATOM 368 C C . ASP A 1 47 ? 35.986 24.226 12.513 1.00 26.76 ? 47 ASP A C 1 ATOM 369 O O . ASP A 1 47 ? 36.994 23.523 12.408 1.00 27.01 ? 47 ASP A O 1 ATOM 370 C CB . ASP A 1 47 ? 36.201 26.439 11.408 1.00 28.77 ? 47 ASP A CB 1 ATOM 371 C CG . ASP A 1 47 ? 35.979 27.278 10.145 1.00 30.32 ? 47 ASP A CG 1 ATOM 372 O OD1 . ASP A 1 47 ? 35.515 26.746 9.112 1.00 29.56 ? 47 ASP A OD1 1 ATOM 373 O OD2 . ASP A 1 47 ? 36.287 28.492 10.188 1.00 30.50 ? 47 ASP A OD2 1 ATOM 374 N N . ASN A 1 48 ? 35.271 24.291 13.628 1.00 25.39 ? 48 ASN A N 1 ATOM 375 C CA . ASN A 1 48 ? 35.674 23.538 14.807 1.00 24.76 ? 48 ASN A CA 1 ATOM 376 C C . ASN A 1 48 ? 34.872 22.255 15.028 1.00 24.25 ? 48 ASN A C 1 ATOM 377 O O . ASN A 1 48 ? 35.077 21.570 16.032 1.00 24.61 ? 48 ASN A O 1 ATOM 378 C CB . ASN A 1 48 ? 35.658 24.452 16.040 1.00 24.11 ? 48 ASN A CB 1 ATOM 379 C CG . ASN A 1 48 ? 36.645 25.593 15.907 1.00 25.25 ? 48 ASN A CG 1 ATOM 380 O OD1 . ASN A 1 48 ? 37.852 25.405 16.101 1.00 25.34 ? 48 ASN A OD1 1 ATOM 381 N ND2 . ASN A 1 48 ? 36.150 26.766 15.529 1.00 22.75 ? 48 ASN A ND2 1 ATOM 382 N N . PHE A 1 49 ? 33.987 21.926 14.073 1.00 24.10 ? 49 PHE A N 1 ATOM 383 C CA . PHE A 1 49 ? 33.196 20.690 14.098 1.00 23.25 ? 49 PHE A CA 1 ATOM 384 C C . PHE A 1 49 ? 32.442 20.545 15.431 1.00 23.06 ? 49 PHE A C 1 ATOM 385 O O . PHE A 1 49 ? 32.424 19.463 16.036 1.00 22.79 ? 49 PHE A O 1 ATOM 386 C CB . PHE A 1 49 ? 34.105 19.468 13.843 1.00 23.71 ? 49 PHE A CB 1 ATOM 387 C CG . PHE A 1 49 ? 34.998 19.604 12.611 1.00 24.37 ? 49 PHE A CG 1 ATOM 388 C CD1 . PHE A 1 49 ? 36.335 19.974 12.738 1.00 24.19 ? 49 PHE A CD1 1 ATOM 389 C CD2 . PHE A 1 49 ? 34.490 19.365 11.327 1.00 23.86 ? 49 PHE A CD2 1 ATOM 390 C CE1 . PHE A 1 49 ? 37.181 20.095 11.589 1.00 23.41 ? 49 PHE A CE1 1 ATOM 391 C CE2 . PHE A 1 49 ? 35.308 19.481 10.184 1.00 26.18 ? 49 PHE A CE2 1 ATOM 392 C CZ . PHE A 1 49 ? 36.661 19.850 10.315 1.00 25.77 ? 49 PHE A CZ 1 ATOM 393 N N . ILE A 1 50 ? 31.833 21.644 15.882 1.00 23.05 ? 50 ILE A N 1 ATOM 394 C CA . ILE A 1 50 ? 31.262 21.736 17.250 1.00 22.35 ? 50 ILE A CA 1 ATOM 395 C C . ILE A 1 50 ? 30.103 20.759 17.460 1.00 22.50 ? 50 ILE A C 1 ATOM 396 O O . ILE A 1 50 ? 29.228 20.617 16.591 1.00 23.19 ? 50 ILE A O 1 ATOM 397 C CB . ILE A 1 50 ? 30.867 23.217 17.608 1.00 22.45 ? 50 ILE A CB 1 ATOM 398 C CG1 . ILE A 1 50 ? 32.112 24.131 17.639 1.00 21.03 ? 50 ILE A CG1 1 ATOM 399 C CG2 . ILE A 1 50 ? 30.023 23.303 18.905 1.00 20.30 ? 50 ILE A CG2 1 ATOM 400 C CD1 . ILE A 1 50 ? 33.210 23.709 18.635 1.00 19.72 ? 50 ILE A CD1 1 ATOM 401 N N . GLY A 1 51 ? 30.116 20.074 18.607 1.00 21.96 ? 51 GLY A N 1 ATOM 402 C CA . GLY A 1 51 ? 29.137 19.047 18.904 1.00 21.42 ? 51 GLY A CA 1 ATOM 403 C C . GLY A 1 51 ? 27.859 19.511 19.575 1.00 21.16 ? 51 GLY A C 1 ATOM 404 O O . GLY A 1 51 ? 26.828 18.854 19.461 1.00 20.68 ? 51 GLY A O 1 ATOM 405 N N . SER A 1 52 ? 27.924 20.629 20.289 1.00 21.23 ? 52 SER A N 1 ATOM 406 C CA . SER A 1 52 ? 26.799 21.069 21.105 1.00 20.82 ? 52 SER A CA 1 ATOM 407 C C . SER A 1 52 ? 26.859 22.561 21.349 1.00 21.07 ? 52 SER A C 1 ATOM 408 O O . SER A 1 52 ? 27.953 23.157 21.410 1.00 20.93 ? 52 SER A O 1 ATOM 409 C CB . SER A 1 52 ? 26.794 20.312 22.443 1.00 20.15 ? 52 SER A CB 1 ATOM 410 O OG . SER A 1 52 ? 25.665 20.640 23.245 1.00 21.11 ? 52 SER A OG 1 ATOM 411 N N . LEU A 1 53 ? 25.676 23.167 21.472 1.00 20.99 ? 53 LEU A N 1 ATOM 412 C CA . LEU A 1 53 ? 25.542 24.537 21.968 1.00 20.91 ? 53 LEU A CA 1 ATOM 413 C C . LEU A 1 53 ? 24.646 24.544 23.187 1.00 20.15 ? 53 LEU A C 1 ATOM 414 O O . LEU A 1 53 ? 23.901 23.597 23.417 1.00 19.83 ? 53 LEU A O 1 ATOM 415 C CB . LEU A 1 53 ? 24.938 25.466 20.918 1.00 21.34 ? 53 LEU A CB 1 ATOM 416 C CG . LEU A 1 53 ? 25.838 25.893 19.757 1.00 24.41 ? 53 LEU A CG 1 ATOM 417 C CD1 . LEU A 1 53 ? 25.736 24.893 18.626 1.00 21.22 ? 53 LEU A CD1 1 ATOM 418 C CD2 . LEU A 1 53 ? 25.391 27.237 19.282 1.00 26.07 ? 53 LEU A CD2 1 ATOM 419 N N . LEU A 1 54 ? 24.718 25.615 23.967 1.00 19.75 ? 54 LEU A N 1 ATOM 420 C CA . LEU A 1 54 ? 23.759 25.831 25.037 1.00 19.11 ? 54 LEU A CA 1 ATOM 421 C C . LEU A 1 54 ? 23.455 27.320 25.177 1.00 19.35 ? 54 LEU A C 1 ATOM 422 O O . LEU A 1 54 ? 24.204 28.166 24.700 1.00 18.70 ? 54 LEU A O 1 ATOM 423 C CB . LEU A 1 54 ? 24.298 25.297 26.393 1.00 18.59 ? 54 LEU A CB 1 ATOM 424 C CG . LEU A 1 54 ? 25.194 26.197 27.262 1.00 19.04 ? 54 LEU A CG 1 ATOM 425 C CD1 . LEU A 1 54 ? 25.083 25.833 28.767 1.00 17.11 ? 54 LEU A CD1 1 ATOM 426 C CD2 . LEU A 1 54 ? 26.669 26.230 26.797 1.00 16.69 ? 54 LEU A CD2 1 ATOM 427 N N . SER A 1 55 ? 22.334 27.604 25.838 1.00 19.51 ? 55 SER A N 1 ATOM 428 C CA . SER A 1 55 ? 22.060 28.896 26.444 1.00 20.34 ? 55 SER A CA 1 ATOM 429 C C . SER A 1 55 ? 22.284 28.668 27.923 1.00 20.29 ? 55 SER A C 1 ATOM 430 O O . SER A 1 55 ? 21.665 27.777 28.499 1.00 20.32 ? 55 SER A O 1 ATOM 431 C CB . SER A 1 55 ? 20.585 29.276 26.235 1.00 20.39 ? 55 SER A CB 1 ATOM 432 O OG . SER A 1 55 ? 20.375 29.775 24.933 1.00 21.93 ? 55 SER A OG 1 ATOM 433 N N . GLY A 1 56 ? 23.175 29.450 28.529 1.00 21.07 ? 56 GLY A N 1 ATOM 434 C CA . GLY A 1 56 ? 23.184 29.606 29.970 1.00 21.52 ? 56 GLY A CA 1 ATOM 435 C C . GLY A 1 56 ? 21.975 30.420 30.432 1.00 21.96 ? 56 GLY A C 1 ATOM 436 O O . GLY A 1 56 ? 21.225 30.944 29.609 1.00 21.48 ? 56 GLY A O 1 ATOM 437 N N . GLY A 1 57 ? 21.781 30.524 31.750 1.00 21.93 ? 57 GLY A N 1 ATOM 438 C CA . GLY A 1 57 ? 20.720 31.362 32.301 1.00 22.28 ? 57 GLY A CA 1 ATOM 439 C C . GLY A 1 57 ? 20.687 32.742 31.660 1.00 22.62 ? 57 GLY A C 1 ATOM 440 O O . GLY A 1 57 ? 21.698 33.458 31.654 1.00 23.15 ? 57 GLY A O 1 ATOM 441 N N . GLY A 1 58 ? 19.523 33.102 31.110 1.00 22.40 ? 58 GLY A N 1 ATOM 442 C CA . GLY A 1 58 ? 19.297 34.410 30.479 1.00 22.59 ? 58 GLY A CA 1 ATOM 443 C C . GLY A 1 58 ? 19.974 34.628 29.129 1.00 23.02 ? 58 GLY A C 1 ATOM 444 O O . GLY A 1 58 ? 20.003 35.758 28.624 1.00 23.25 ? 58 GLY A O 1 ATOM 445 N N . SER A 1 59 ? 20.533 33.566 28.542 1.00 22.52 ? 59 SER A N 1 ATOM 446 C CA . SER A 1 59 ? 21.174 33.667 27.217 1.00 22.64 ? 59 SER A CA 1 ATOM 447 C C . SER A 1 59 ? 20.107 33.437 26.155 1.00 22.61 ? 59 SER A C 1 ATOM 448 O O . SER A 1 59 ? 19.755 32.303 25.842 1.00 22.84 ? 59 SER A O 1 ATOM 449 C CB . SER A 1 59 ? 22.296 32.640 27.078 1.00 22.63 ? 59 SER A CB 1 ATOM 450 O OG . SER A 1 59 ? 23.023 32.821 25.868 1.00 23.21 ? 59 SER A OG 1 ATOM 451 N N . VAL A 1 60 ? 19.563 34.531 25.646 1.00 22.86 ? 60 VAL A N 1 ATOM 452 C CA . VAL A 1 60 ? 18.377 34.500 24.802 1.00 22.67 ? 60 VAL A CA 1 ATOM 453 C C . VAL A 1 60 ? 18.645 35.341 23.528 1.00 23.91 ? 60 VAL A C 1 ATOM 454 O O . VAL A 1 60 ? 19.455 36.258 23.559 1.00 24.25 ? 60 VAL A O 1 ATOM 455 C CB . VAL A 1 60 ? 17.106 34.988 25.594 1.00 22.23 ? 60 VAL A CB 1 ATOM 456 C CG1 . VAL A 1 60 ? 16.843 34.103 26.828 1.00 20.82 ? 60 VAL A CG1 1 ATOM 457 C CG2 . VAL A 1 60 ? 17.214 36.452 26.011 1.00 21.79 ? 60 VAL A CG2 1 ATOM 458 N N . PRO A 1 61 ? 17.999 35.002 22.399 1.00 24.88 ? 61 PRO A N 1 ATOM 459 C CA . PRO A 1 61 ? 18.226 35.794 21.173 1.00 25.95 ? 61 PRO A CA 1 ATOM 460 C C . PRO A 1 61 ? 17.751 37.255 21.281 1.00 28.21 ? 61 PRO A C 1 ATOM 461 O O . PRO A 1 61 ? 18.392 38.150 20.729 1.00 28.45 ? 61 PRO A O 1 ATOM 462 C CB . PRO A 1 61 ? 17.446 35.033 20.092 1.00 26.22 ? 61 PRO A CB 1 ATOM 463 C CG . PRO A 1 61 ? 16.508 34.108 20.824 1.00 24.52 ? 61 PRO A CG 1 ATOM 464 C CD . PRO A 1 61 ? 17.091 33.858 22.190 1.00 23.97 ? 61 PRO A CD 1 ATOM 465 N N . ARG A 1 62 ? 16.654 37.486 21.997 1.00 28.85 ? 62 ARG A N 1 ATOM 466 C CA . ARG A 1 62 ? 16.124 38.836 22.244 1.00 31.62 ? 62 ARG A CA 1 ATOM 467 C C . ARG A 1 62 ? 15.276 38.705 23.488 1.00 31.11 ? 62 ARG A C 1 ATOM 468 O O . ARG A 1 62 ? 14.722 37.638 23.728 1.00 30.26 ? 62 ARG A O 1 ATOM 469 C CB . ARG A 1 62 ? 15.142 39.272 21.143 1.00 32.08 ? 62 ARG A CB 1 ATOM 470 C CG . ARG A 1 62 ? 15.692 39.897 19.885 1.00 36.51 ? 62 ARG A CG 1 ATOM 471 C CD . ARG A 1 62 ? 14.576 40.698 19.160 1.00 35.61 ? 62 ARG A CD 1 ATOM 472 N NE . ARG A 1 62 ? 13.249 40.063 19.232 1.00 36.89 ? 62 ARG A NE 1 ATOM 473 C CZ . ARG A 1 62 ? 12.088 40.722 19.187 1.00 37.59 ? 62 ARG A CZ 1 ATOM 474 N NH1 . ARG A 1 62 ? 12.068 42.043 19.085 1.00 39.92 ? 62 ARG A NH1 1 ATOM 475 N NH2 . ARG A 1 62 ? 10.942 40.058 19.255 1.00 37.02 ? 62 ARG A NH2 1 ATOM 476 N N . LYS A 1 63 ? 15.118 39.793 24.245 1.00 32.32 ? 63 LYS A N 1 ATOM 477 C CA . LYS A 1 63 ? 14.043 39.864 25.240 1.00 32.68 ? 63 LYS A CA 1 ATOM 478 C C . LYS A 1 63 ? 12.709 39.725 24.535 1.00 31.70 ? 63 LYS A C 1 ATOM 479 O O . LYS A 1 63 ? 12.496 40.350 23.499 1.00 32.65 ? 63 LYS A O 1 ATOM 480 C CB . LYS A 1 63 ? 14.068 41.202 25.990 1.00 34.54 ? 63 LYS A CB 1 ATOM 481 C CG . LYS A 1 63 ? 15.338 41.414 26.823 1.00 38.90 ? 63 LYS A CG 1 ATOM 482 C CD . LYS A 1 63 ? 15.142 41.152 28.310 1.00 43.70 ? 63 LYS A CD 1 ATOM 483 C CE . LYS A 1 63 ? 15.226 39.690 28.639 1.00 43.24 ? 63 LYS A CE 1 ATOM 484 N NZ . LYS A 1 63 ? 15.218 39.562 30.116 1.00 45.68 ? 63 LYS A NZ 1 ATOM 485 N N . GLY A 1 64 ? 11.828 38.890 25.086 1.00 30.25 ? 64 GLY A N 1 ATOM 486 C CA . GLY A 1 64 ? 10.493 38.693 24.537 1.00 29.08 ? 64 GLY A CA 1 ATOM 487 C C . GLY A 1 64 ? 10.458 37.921 23.229 1.00 28.65 ? 64 GLY A C 1 ATOM 488 O O . GLY A 1 64 ? 9.439 37.935 22.543 1.00 29.69 ? 64 GLY A O 1 ATOM 489 N N . ALA A 1 65 ? 11.558 37.245 22.883 1.00 27.20 ? 65 ALA A N 1 ATOM 490 C CA . ALA A 1 65 ? 11.637 36.438 21.664 1.00 26.55 ? 65 ALA A CA 1 ATOM 491 C C . ALA A 1 65 ? 10.517 35.397 21.630 1.00 26.32 ? 65 ALA A C 1 ATOM 492 O O . ALA A 1 65 ? 10.226 34.757 22.644 1.00 25.98 ? 65 ALA A O 1 ATOM 493 C CB . ALA A 1 65 ? 13.015 35.751 21.548 1.00 25.21 ? 65 ALA A CB 1 ATOM 494 N N . THR A 1 66 ? 9.888 35.247 20.464 1.00 26.99 ? 66 THR A N 1 ATOM 495 C CA . THR A 1 66 ? 8.843 34.240 20.244 1.00 26.48 ? 66 THR A CA 1 ATOM 496 C C . THR A 1 66 ? 9.459 32.832 20.116 1.00 25.81 ? 66 THR A C 1 ATOM 497 O O . THR A 1 66 ? 10.662 32.701 19.896 1.00 25.26 ? 66 THR A O 1 ATOM 498 C CB . THR A 1 66 ? 8.053 34.559 18.960 1.00 27.66 ? 66 THR A CB 1 ATOM 499 O OG1 . THR A 1 66 ? 8.913 34.397 17.827 1.00 28.30 ? 66 THR A OG1 1 ATOM 500 C CG2 . THR A 1 66 ? 7.529 36.008 18.970 1.00 28.11 ? 66 THR A CG2 1 ATOM 501 N N . ALA A 1 67 ? 8.634 31.787 20.236 1.00 25.38 ? 67 ALA A N 1 ATOM 502 C CA . ALA A 1 67 ? 9.073 30.412 19.997 1.00 24.65 ? 67 ALA A CA 1 ATOM 503 C C . ALA A 1 67 ? 9.751 30.273 18.613 1.00 25.00 ? 67 ALA A C 1 ATOM 504 O O . ALA A 1 67 ? 10.793 29.619 18.503 1.00 24.56 ? 67 ALA A O 1 ATOM 505 C CB . ALA A 1 67 ? 7.918 29.441 20.128 1.00 24.59 ? 67 ALA A CB 1 ATOM 506 N N . LYS A 1 68 ? 9.174 30.899 17.582 1.00 25.41 ? 68 LYS A N 1 ATOM 507 C CA . LYS A 1 68 ? 9.772 30.887 16.235 1.00 25.59 ? 68 LYS A CA 1 ATOM 508 C C . LYS A 1 68 ? 11.179 31.511 16.153 1.00 25.36 ? 68 LYS A C 1 ATOM 509 O O . LYS A 1 68 ? 12.071 30.953 15.500 1.00 25.45 ? 68 LYS A O 1 ATOM 510 C CB A LYS A 1 68 ? 8.835 31.499 15.188 0.50 27.21 ? 68 LYS A CB 1 ATOM 511 C CB B LYS A 1 68 ? 8.830 31.580 15.246 0.50 26.79 ? 68 LYS A CB 1 ATOM 512 C CG A LYS A 1 68 ? 7.898 30.483 14.537 0.50 28.10 ? 68 LYS A CG 1 ATOM 513 C CG B LYS A 1 68 ? 9.300 31.578 13.802 0.50 26.30 ? 68 LYS A CG 1 ATOM 514 C CD A LYS A 1 68 ? 8.666 29.338 13.840 0.50 29.68 ? 68 LYS A CD 1 ATOM 515 C CD B LYS A 1 68 ? 8.465 32.534 12.982 0.50 26.47 ? 68 LYS A CD 1 ATOM 516 C CE A LYS A 1 68 ? 9.105 29.713 12.429 0.50 31.74 ? 68 LYS A CE 1 ATOM 517 C CE B LYS A 1 68 ? 8.867 32.539 11.517 0.50 25.71 ? 68 LYS A CE 1 ATOM 518 N NZ A LYS A 1 68 ? 10.185 28.796 12.002 0.50 32.60 ? 68 LYS A NZ 1 ATOM 519 N NZ B LYS A 1 68 ? 10.265 32.932 11.306 0.50 24.04 ? 68 LYS A NZ 1 ATOM 520 N N . GLU A 1 69 ? 11.367 32.659 16.802 1.00 24.77 ? 69 GLU A N 1 ATOM 521 C CA . GLU A 1 69 ? 12.704 33.249 16.961 1.00 24.74 ? 69 GLU A CA 1 ATOM 522 C C . GLU A 1 69 ? 13.727 32.275 17.534 1.00 23.84 ? 69 GLU A C 1 ATOM 523 O O . GLU A 1 69 ? 14.851 32.176 17.026 1.00 23.96 ? 69 GLU A O 1 ATOM 524 C CB . GLU A 1 69 ? 12.647 34.501 17.831 1.00 24.60 ? 69 GLU A CB 1 ATOM 525 C CG . GLU A 1 69 ? 12.002 35.693 17.147 1.00 27.03 ? 69 GLU A CG 1 ATOM 526 C CD . GLU A 1 69 ? 12.050 36.924 18.027 1.00 29.71 ? 69 GLU A CD 1 ATOM 527 O OE1 . GLU A 1 69 ? 13.169 37.450 18.267 1.00 30.19 ? 69 GLU A OE1 1 ATOM 528 O OE2 . GLU A 1 69 ? 10.972 37.365 18.480 1.00 29.92 ? 69 GLU A OE2 1 ATOM 529 N N . TRP A 1 70 ? 13.338 31.549 18.590 1.00 22.90 ? 70 TRP A N 1 ATOM 530 C CA . TRP A 1 70 ? 14.198 30.504 19.148 1.00 21.83 ? 70 TRP A CA 1 ATOM 531 C C . TRP A 1 70 ? 14.485 29.396 18.135 1.00 22.25 ? 70 TRP A C 1 ATOM 532 O O . TRP A 1 70 ? 15.636 28.962 17.993 1.00 21.12 ? 70 TRP A O 1 ATOM 533 C CB . TRP A 1 70 ? 13.587 29.911 20.423 1.00 21.11 ? 70 TRP A CB 1 ATOM 534 C CG . TRP A 1 70 ? 13.789 30.745 21.646 1.00 20.65 ? 70 TRP A CG 1 ATOM 535 C CD1 . TRP A 1 70 ? 12.963 31.748 22.106 1.00 20.96 ? 70 TRP A CD1 1 ATOM 536 C CD2 . TRP A 1 70 ? 14.867 30.645 22.588 1.00 20.59 ? 70 TRP A CD2 1 ATOM 537 N NE1 . TRP A 1 70 ? 13.469 32.282 23.271 1.00 19.64 ? 70 TRP A NE1 1 ATOM 538 C CE2 . TRP A 1 70 ? 14.632 31.621 23.597 1.00 21.13 ? 70 TRP A CE2 1 ATOM 539 C CE3 . TRP A 1 70 ? 16.012 29.823 22.684 1.00 18.93 ? 70 TRP A CE3 1 ATOM 540 C CZ2 . TRP A 1 70 ? 15.506 31.806 24.685 1.00 19.76 ? 70 TRP A CZ2 1 ATOM 541 C CZ3 . TRP A 1 70 ? 16.882 30.008 23.762 1.00 19.56 ? 70 TRP A CZ3 1 ATOM 542 C CH2 . TRP A 1 70 ? 16.622 30.998 24.755 1.00 20.04 ? 70 TRP A CH2 1 ATOM 543 N N . GLN A 1 71 ? 13.445 28.952 17.419 1.00 22.85 ? 71 GLN A N 1 ATOM 544 C CA . GLN A 1 71 ? 13.615 27.912 16.390 1.00 23.12 ? 71 GLN A CA 1 ATOM 545 C C . GLN A 1 71 ? 14.574 28.335 15.285 1.00 23.41 ? 71 GLN A C 1 ATOM 546 O O . GLN A 1 71 ? 15.439 27.552 14.883 1.00 23.41 ? 71 GLN A O 1 ATOM 547 C CB . GLN A 1 71 ? 12.268 27.510 15.787 1.00 23.59 ? 71 GLN A CB 1 ATOM 548 C CG . GLN A 1 71 ? 11.339 26.779 16.771 1.00 24.04 ? 71 GLN A CG 1 ATOM 549 C CD . GLN A 1 71 ? 10.222 26.072 16.032 1.00 25.31 ? 71 GLN A CD 1 ATOM 550 O OE1 . GLN A 1 71 ? 10.230 26.012 14.805 1.00 25.17 ? 71 GLN A OE1 1 ATOM 551 N NE2 . GLN A 1 71 ? 9.279 25.515 16.766 1.00 25.01 ? 71 GLN A NE2 1 ATOM 552 N N . ASP A 1 72 ? 14.414 29.569 14.806 1.00 24.09 ? 72 ASP A N 1 ATOM 553 C CA . ASP A 1 72 ? 15.257 30.135 13.753 1.00 25.41 ? 72 ASP A CA 1 ATOM 554 C C . ASP A 1 72 ? 16.704 30.233 14.219 1.00 24.82 ? 72 ASP A C 1 ATOM 555 O O . ASP A 1 72 ? 17.636 29.959 13.452 1.00 25.03 ? 72 ASP A O 1 ATOM 556 C CB . ASP A 1 72 ? 14.748 31.528 13.328 1.00 26.41 ? 72 ASP A CB 1 ATOM 557 C CG . ASP A 1 72 ? 13.388 31.479 12.624 1.00 29.09 ? 72 ASP A CG 1 ATOM 558 O OD1 . ASP A 1 72 ? 12.978 30.383 12.170 1.00 30.56 ? 72 ASP A OD1 1 ATOM 559 O OD2 . ASP A 1 72 ? 12.735 32.547 12.510 1.00 29.44 ? 72 ASP A OD2 1 ATOM 560 N N . MET A 1 73 ? 16.891 30.632 15.476 1.00 24.37 ? 73 MET A N 1 ATOM 561 C CA . MET A 1 73 ? 18.223 30.692 16.062 1.00 23.83 ? 73 MET A CA 1 ATOM 562 C C . MET A 1 73 ? 18.881 29.316 16.093 1.00 23.03 ? 73 MET A C 1 ATOM 563 O O . MET A 1 73 ? 19.982 29.148 15.584 1.00 22.78 ? 73 MET A O 1 ATOM 564 C CB . MET A 1 73 ? 18.193 31.284 17.471 1.00 23.69 ? 73 MET A CB 1 ATOM 565 C CG . MET A 1 73 ? 19.580 31.423 18.050 1.00 23.57 ? 73 MET A CG 1 ATOM 566 S SD . MET A 1 73 ? 19.622 31.641 19.828 1.00 23.07 ? 73 MET A SD 1 ATOM 567 C CE . MET A 1 73 ? 18.919 30.102 20.458 1.00 22.76 ? 73 MET A CE 1 ATOM 568 N N . VAL A 1 74 ? 18.193 28.342 16.687 1.00 22.61 ? 74 VAL A N 1 ATOM 569 C CA . VAL A 1 74 ? 18.703 26.978 16.788 1.00 21.75 ? 74 VAL A CA 1 ATOM 570 C C . VAL A 1 74 ? 18.955 26.366 15.387 1.00 22.30 ? 74 VAL A C 1 ATOM 571 O O . VAL A 1 74 ? 20.035 25.803 15.136 1.00 22.80 ? 74 VAL A O 1 ATOM 572 C CB . VAL A 1 74 ? 17.788 26.085 17.663 1.00 21.41 ? 74 VAL A CB 1 ATOM 573 C CG1 . VAL A 1 74 ? 18.355 24.677 17.754 1.00 20.93 ? 74 VAL A CG1 1 ATOM 574 C CG2 . VAL A 1 74 ? 17.612 26.689 19.095 1.00 19.35 ? 74 VAL A CG2 1 ATOM 575 N N . ASP A 1 75 ? 17.991 26.507 14.477 1.00 22.84 ? 75 ASP A N 1 ATOM 576 C CA . ASP A 1 75 ? 18.150 26.043 13.087 1.00 23.26 ? 75 ASP A CA 1 ATOM 577 C C . ASP A 1 75 ? 19.350 26.680 12.362 1.00 24.16 ? 75 ASP A C 1 ATOM 578 O O . ASP A 1 75 ? 20.032 25.999 11.597 1.00 23.74 ? 75 ASP A O 1 ATOM 579 C CB . ASP A 1 75 ? 16.878 26.295 12.267 1.00 24.03 ? 75 ASP A CB 1 ATOM 580 C CG . ASP A 1 75 ? 15.773 25.297 12.557 1.00 24.79 ? 75 ASP A CG 1 ATOM 581 O OD1 . ASP A 1 75 ? 16.021 24.271 13.238 1.00 24.44 ? 75 ASP A OD1 1 ATOM 582 O OD2 . ASP A 1 75 ? 14.634 25.557 12.111 1.00 27.21 ? 75 ASP A OD2 1 ATOM 583 N N . GLY A 1 76 ? 19.595 27.972 12.606 1.00 24.18 ? 76 GLY A N 1 ATOM 584 C CA . GLY A 1 76 ? 20.745 28.680 12.024 1.00 24.85 ? 76 GLY A CA 1 ATOM 585 C C . GLY A 1 76 ? 22.070 28.049 12.425 1.00 24.61 ? 76 GLY A C 1 ATOM 586 O O . GLY A 1 76 ? 22.951 27.861 11.589 1.00 25.29 ? 76 GLY A O 1 ATOM 587 N N . PHE A 1 77 ? 22.206 27.734 13.712 1.00 23.90 ? 77 PHE A N 1 ATOM 588 C CA . PHE A 1 77 ? 23.332 26.965 14.243 1.00 23.93 ? 77 PHE A CA 1 ATOM 589 C C . PHE A 1 77 ? 23.426 25.542 13.670 1.00 23.94 ? 77 PHE A C 1 ATOM 590 O O . PHE A 1 77 ? 24.506 25.087 13.296 1.00 23.93 ? 77 PHE A O 1 ATOM 591 C CB . PHE A 1 77 ? 23.217 26.887 15.775 1.00 23.40 ? 77 PHE A CB 1 ATOM 592 C CG . PHE A 1 77 ? 23.364 28.223 16.477 1.00 23.91 ? 77 PHE A CG 1 ATOM 593 C CD1 . PHE A 1 77 ? 22.589 28.516 17.596 1.00 23.70 ? 77 PHE A CD1 1 ATOM 594 C CD2 . PHE A 1 77 ? 24.268 29.190 16.011 1.00 25.11 ? 77 PHE A CD2 1 ATOM 595 C CE1 . PHE A 1 77 ? 22.736 29.732 18.272 1.00 24.11 ? 77 PHE A CE1 1 ATOM 596 C CE2 . PHE A 1 77 ? 24.407 30.412 16.680 1.00 25.08 ? 77 PHE A CE2 1 ATOM 597 C CZ . PHE A 1 77 ? 23.631 30.674 17.809 1.00 23.42 ? 77 PHE A CZ 1 ATOM 598 N N . GLN A 1 78 ? 22.289 24.844 13.617 1.00 24.09 ? 78 GLN A N 1 ATOM 599 C CA . GLN A 1 78 ? 22.218 23.499 13.031 1.00 24.37 ? 78 GLN A CA 1 ATOM 600 C C . GLN A 1 78 ? 22.660 23.464 11.570 1.00 25.50 ? 78 GLN A C 1 ATOM 601 O O . GLN A 1 78 ? 23.386 22.551 11.161 1.00 24.81 ? 78 GLN A O 1 ATOM 602 C CB . GLN A 1 78 ? 20.799 22.920 13.139 1.00 24.13 ? 78 GLN A CB 1 ATOM 603 C CG . GLN A 1 78 ? 20.717 21.410 12.888 1.00 24.20 ? 78 GLN A CG 1 ATOM 604 C CD . GLN A 1 78 ? 21.471 20.615 13.942 1.00 24.22 ? 78 GLN A CD 1 ATOM 605 O OE1 . GLN A 1 78 ? 22.690 20.656 13.993 1.00 23.81 ? 78 GLN A OE1 1 ATOM 606 N NE2 . GLN A 1 78 ? 20.745 19.896 14.789 1.00 24.04 ? 78 GLN A NE2 1 ATOM 607 N N . LYS A 1 79 ? 22.208 24.445 10.781 1.00 26.69 ? 79 LYS A N 1 ATOM 608 C CA . LYS A 1 79 ? 22.572 24.518 9.369 1.00 28.14 ? 79 LYS A CA 1 ATOM 609 C C . LYS A 1 79 ? 24.075 24.498 9.213 1.00 27.67 ? 79 LYS A C 1 ATOM 610 O O . LYS A 1 79 ? 24.595 23.795 8.353 1.00 27.62 ? 79 LYS A O 1 ATOM 611 C CB . LYS A 1 79 ? 22.057 25.808 8.737 1.00 29.91 ? 79 LYS A CB 1 ATOM 612 C CG . LYS A 1 79 ? 20.650 25.758 8.215 1.00 34.07 ? 79 LYS A CG 1 ATOM 613 C CD . LYS A 1 79 ? 20.393 26.932 7.236 1.00 39.81 ? 79 LYS A CD 1 ATOM 614 C CE . LYS A 1 79 ? 21.451 27.021 6.132 1.00 43.20 ? 79 LYS A CE 1 ATOM 615 N NZ . LYS A 1 79 ? 20.942 27.704 4.867 1.00 46.50 ? 79 LYS A NZ 1 ATOM 616 N N . ALA A 1 80 ? 24.767 25.279 10.047 1.00 27.03 ? 80 ALA A N 1 ATOM 617 C CA . ALA A 1 80 ? 26.220 25.347 10.017 1.00 27.57 ? 80 ALA A CA 1 ATOM 618 C C . ALA A 1 80 ? 26.844 23.976 10.335 1.00 27.19 ? 80 ALA A C 1 ATOM 619 O O . ALA A 1 80 ? 27.721 23.515 9.611 1.00 27.87 ? 80 ALA A O 1 ATOM 620 C CB . ALA A 1 80 ? 26.736 26.427 10.985 1.00 27.24 ? 80 ALA A CB 1 ATOM 621 N N . CYS A 1 81 ? 26.370 23.323 11.397 1.00 26.53 ? 81 CYS A N 1 ATOM 622 C CA . CYS A 1 81 ? 26.876 22.007 11.777 1.00 26.29 ? 81 CYS A CA 1 ATOM 623 C C . CYS A 1 81 ? 26.581 20.954 10.696 1.00 27.01 ? 81 CYS A C 1 ATOM 624 O O . CYS A 1 81 ? 27.409 20.077 10.418 1.00 27.87 ? 81 CYS A O 1 ATOM 625 C CB . CYS A 1 81 ? 26.314 21.578 13.137 1.00 25.35 ? 81 CYS A CB 1 ATOM 626 S SG . CYS A 1 81 ? 26.741 22.731 14.468 1.00 24.80 ? 81 CYS A SG 1 ATOM 627 N N . MET A 1 82 ? 25.411 21.055 10.070 1.00 26.93 ? 82 MET A N 1 ATOM 628 C CA . MET A 1 82 ? 25.046 20.107 9.033 1.00 27.31 ? 82 MET A CA 1 ATOM 629 C C . MET A 1 82 ? 25.893 20.286 7.770 1.00 27.67 ? 82 MET A C 1 ATOM 630 O O . MET A 1 82 ? 25.933 19.384 6.943 1.00 28.28 ? 82 MET A O 1 ATOM 631 C CB . MET A 1 82 ? 23.560 20.206 8.684 1.00 27.47 ? 82 MET A CB 1 ATOM 632 C CG . MET A 1 82 ? 22.593 19.761 9.790 1.00 28.50 ? 82 MET A CG 1 ATOM 633 S SD . MET A 1 82 ? 22.936 18.106 10.410 1.00 33.81 ? 82 MET A SD 1 ATOM 634 C CE . MET A 1 82 ? 22.360 17.109 9.038 1.00 33.52 ? 82 MET A CE 1 ATOM 635 N N . SER A 1 83 ? 26.541 21.446 7.627 1.00 27.43 ? 83 SER A N 1 ATOM 636 C CA . SER A 1 83 ? 27.374 21.760 6.443 1.00 28.19 ? 83 SER A CA 1 ATOM 637 C C . SER A 1 83 ? 28.809 21.209 6.538 1.00 27.59 ? 83 SER A C 1 ATOM 638 O O . SER A 1 83 ? 29.571 21.288 5.579 1.00 28.42 ? 83 SER A O 1 ATOM 639 C CB . SER A 1 83 ? 27.403 23.273 6.167 1.00 28.72 ? 83 SER A CB 1 ATOM 640 O OG . SER A 1 83 ? 28.218 23.948 7.115 1.00 30.23 ? 83 SER A OG 1 ATOM 641 N N . THR A 1 84 ? 29.177 20.645 7.682 1.00 25.69 ? 84 THR A N 1 ATOM 642 C CA . THR A 1 84 ? 30.484 20.010 7.817 1.00 25.48 ? 84 THR A CA 1 ATOM 643 C C . THR A 1 84 ? 30.581 18.781 6.895 1.00 26.09 ? 84 THR A C 1 ATOM 644 O O . THR A 1 84 ? 29.566 18.263 6.412 1.00 25.19 ? 84 THR A O 1 ATOM 645 C CB . THR A 1 84 ? 30.762 19.570 9.278 1.00 24.48 ? 84 THR A CB 1 ATOM 646 O OG1 . THR A 1 84 ? 29.751 18.646 9.702 1.00 24.47 ? 84 THR A OG1 1 ATOM 647 C CG2 . THR A 1 84 ? 30.771 20.780 10.230 1.00 23.96 ? 84 THR A CG2 1 ATOM 648 N N . ARG A 1 85 ? 31.811 18.316 6.683 1.00 26.42 ? 85 ARG A N 1 ATOM 649 C CA . ARG A 1 85 ? 32.085 17.116 5.893 1.00 27.33 ? 85 ARG A CA 1 ATOM 650 C C . ARG A 1 85 ? 31.201 15.917 6.272 1.00 27.03 ? 85 ARG A C 1 ATOM 651 O O . ARG A 1 85 ? 30.685 15.225 5.403 1.00 27.43 ? 85 ARG A O 1 ATOM 652 C CB . ARG A 1 85 ? 33.550 16.727 6.064 1.00 27.55 ? 85 ARG A CB 1 ATOM 653 C CG . ARG A 1 85 ? 33.953 15.587 5.190 1.00 27.72 ? 85 ARG A CG 1 ATOM 654 C CD . ARG A 1 85 ? 35.373 15.226 5.457 1.00 28.13 ? 85 ARG A CD 1 ATOM 655 N NE . ARG A 1 85 ? 35.568 14.543 6.738 1.00 27.64 ? 85 ARG A NE 1 ATOM 656 C CZ . ARG A 1 85 ? 35.825 13.244 6.878 1.00 26.89 ? 85 ARG A CZ 1 ATOM 657 N NH1 . ARG A 1 85 ? 35.886 12.435 5.817 1.00 26.99 ? 85 ARG A NH1 1 ATOM 658 N NH2 . ARG A 1 85 ? 36.036 12.757 8.093 1.00 27.57 ? 85 ARG A NH2 1 ATOM 659 N N . LEU A 1 86 ? 31.035 15.690 7.576 1.00 26.40 ? 86 LEU A N 1 ATOM 660 C CA . LEU A 1 86 ? 30.266 14.553 8.063 1.00 26.55 ? 86 LEU A CA 1 ATOM 661 C C . LEU A 1 86 ? 28.805 14.881 8.360 1.00 26.47 ? 86 LEU A C 1 ATOM 662 O O . LEU A 1 86 ? 27.983 13.967 8.481 1.00 27.21 ? 86 LEU A O 1 ATOM 663 C CB . LEU A 1 86 ? 30.941 13.921 9.293 1.00 25.56 ? 86 LEU A CB 1 ATOM 664 C CG . LEU A 1 86 ? 32.358 13.354 9.096 1.00 26.23 ? 86 LEU A CG 1 ATOM 665 C CD1 . LEU A 1 86 ? 32.901 12.852 10.417 1.00 23.88 ? 86 LEU A CD1 1 ATOM 666 C CD2 . LEU A 1 86 ? 32.381 12.239 8.064 1.00 26.75 ? 86 LEU A CD2 1 ATOM 667 N N . GLY A 1 87 ? 28.492 16.174 8.485 1.00 25.96 ? 87 GLY A N 1 ATOM 668 C CA . GLY A 1 87 ? 27.138 16.625 8.773 1.00 25.90 ? 87 GLY A CA 1 ATOM 669 C C . GLY A 1 87 ? 26.579 16.055 10.070 1.00 25.41 ? 87 GLY A C 1 ATOM 670 O O . GLY A 1 87 ? 25.458 15.551 10.093 1.00 25.81 ? 87 GLY A O 1 ATOM 671 N N . ILE A 1 88 ? 27.363 16.100 11.147 1.00 24.47 ? 88 ILE A N 1 ATOM 672 C CA . ILE A 1 88 ? 26.880 15.627 12.442 1.00 23.82 ? 88 ILE A CA 1 ATOM 673 C C . ILE A 1 88 ? 26.062 16.760 13.074 1.00 23.66 ? 88 ILE A C 1 ATOM 674 O O . ILE A 1 88 ? 26.590 17.859 13.291 1.00 23.37 ? 88 ILE A O 1 ATOM 675 C CB . ILE A 1 88 ? 28.025 15.185 13.389 1.00 23.79 ? 88 ILE A CB 1 ATOM 676 C CG1 . ILE A 1 88 ? 28.933 14.159 12.682 1.00 23.63 ? 88 ILE A CG1 1 ATOM 677 C CG2 . ILE A 1 88 ? 27.421 14.628 14.729 1.00 22.09 ? 88 ILE A CG2 1 ATOM 678 C CD1 . ILE A 1 88 ? 30.216 13.812 13.449 1.00 23.77 ? 88 ILE A CD1 1 ATOM 679 N N . PRO A 1 89 ? 24.762 16.517 13.330 1.00 23.63 ? 89 PRO A N 1 ATOM 680 C CA . PRO A 1 89 ? 23.956 17.593 13.924 1.00 23.05 ? 89 PRO A CA 1 ATOM 681 C C . PRO A 1 89 ? 24.413 17.943 15.344 1.00 22.72 ? 89 PRO A C 1 ATOM 682 O O . PRO A 1 89 ? 24.807 17.050 16.100 1.00 22.79 ? 89 PRO A O 1 ATOM 683 C CB . PRO A 1 89 ? 22.549 16.987 13.971 1.00 23.17 ? 89 PRO A CB 1 ATOM 684 C CG . PRO A 1 89 ? 22.762 15.512 13.935 1.00 23.73 ? 89 PRO A CG 1 ATOM 685 C CD . PRO A 1 89 ? 23.967 15.295 13.095 1.00 23.70 ? 89 PRO A CD 1 ATOM 686 N N . MET A 1 90 ? 24.360 19.226 15.695 1.00 22.38 ? 90 MET A N 1 ATOM 687 C CA . MET A 1 90 ? 24.631 19.629 17.069 1.00 22.24 ? 90 MET A CA 1 ATOM 688 C C . MET A 1 90 ? 23.388 19.321 17.921 1.00 22.13 ? 90 MET A C 1 ATOM 689 O O . MET A 1 90 ? 22.275 19.198 17.392 1.00 22.82 ? 90 MET A O 1 ATOM 690 C CB . MET A 1 90 ? 25.056 21.111 17.155 1.00 22.01 ? 90 MET A CB 1 ATOM 691 C CG . MET A 1 90 ? 23.982 22.131 16.732 1.00 22.48 ? 90 MET A CG 1 ATOM 692 S SD . MET A 1 90 ? 22.841 22.530 18.093 1.00 23.03 ? 90 MET A SD 1 ATOM 693 C CE . MET A 1 90 ? 21.306 22.706 17.201 1.00 21.27 ? 90 MET A CE 1 ATOM 694 N N . ILE A 1 91 ? 23.600 19.157 19.223 1.00 21.68 ? 91 ILE A N 1 ATOM 695 C CA . ILE A 1 91 ? 22.519 19.087 20.204 1.00 21.15 ? 91 ILE A CA 1 ATOM 696 C C . ILE A 1 91 ? 22.549 20.388 21.007 1.00 21.04 ? 91 ILE A C 1 ATOM 697 O O . ILE A 1 91 ? 23.615 20.823 21.456 1.00 21.60 ? 91 ILE A O 1 ATOM 698 C CB . ILE A 1 91 ? 22.651 17.815 21.115 1.00 21.38 ? 91 ILE A CB 1 ATOM 699 C CG1 . ILE A 1 91 ? 21.420 17.643 22.031 1.00 21.70 ? 91 ILE A CG1 1 ATOM 700 C CG2 . ILE A 1 91 ? 24.019 17.774 21.888 1.00 19.21 ? 91 ILE A CG2 1 ATOM 701 C CD1 . ILE A 1 91 ? 21.424 16.321 22.793 1.00 20.52 ? 91 ILE A CD1 1 ATOM 702 N N . TYR A 1 92 ? 21.394 21.037 21.148 1.00 20.61 ? 92 TYR A N 1 ATOM 703 C CA . TYR A 1 92 ? 21.327 22.327 21.852 1.00 20.32 ? 92 TYR A CA 1 ATOM 704 C C . TYR A 1 92 ? 20.750 22.098 23.235 1.00 19.74 ? 92 TYR A C 1 ATOM 705 O O . TYR A 1 92 ? 19.682 21.509 23.353 1.00 19.37 ? 92 TYR A O 1 ATOM 706 C CB . TYR A 1 92 ? 20.452 23.331 21.076 1.00 20.20 ? 92 TYR A CB 1 ATOM 707 C CG . TYR A 1 92 ? 20.650 24.795 21.475 1.00 20.29 ? 92 TYR A CG 1 ATOM 708 C CD1 . TYR A 1 92 ? 21.324 25.672 20.637 1.00 19.89 ? 92 TYR A CD1 1 ATOM 709 C CD2 . TYR A 1 92 ? 20.157 25.294 22.685 1.00 19.26 ? 92 TYR A CD2 1 ATOM 710 C CE1 . TYR A 1 92 ? 21.504 27.024 20.984 1.00 19.87 ? 92 TYR A CE1 1 ATOM 711 C CE2 . TYR A 1 92 ? 20.336 26.631 23.052 1.00 19.93 ? 92 TYR A CE2 1 ATOM 712 C CZ . TYR A 1 92 ? 21.006 27.485 22.194 1.00 21.10 ? 92 TYR A CZ 1 ATOM 713 O OH . TYR A 1 92 ? 21.178 28.800 22.531 1.00 21.90 ? 92 TYR A OH 1 ATOM 714 N N . GLY A 1 93 ? 21.460 22.544 24.276 1.00 19.43 ? 93 GLY A N 1 ATOM 715 C CA . GLY A 1 93 ? 20.995 22.372 25.644 1.00 19.10 ? 93 GLY A CA 1 ATOM 716 C C . GLY A 1 93 ? 20.567 23.648 26.349 1.00 19.10 ? 93 GLY A C 1 ATOM 717 O O . GLY A 1 93 ? 21.005 24.746 26.029 1.00 19.25 ? 93 GLY A O 1 ATOM 718 N N . ILE A 1 94 ? 19.711 23.492 27.339 1.00 19.67 ? 94 ILE A N 1 ATOM 719 C CA . ILE A 1 94 ? 19.221 24.629 28.102 1.00 19.66 ? 94 ILE A CA 1 ATOM 720 C C . ILE A 1 94 ? 18.759 24.173 29.491 1.00 19.59 ? 94 ILE A C 1 ATOM 721 O O . ILE A 1 94 ? 18.340 23.021 29.678 1.00 19.54 ? 94 ILE A O 1 ATOM 722 C CB . ILE A 1 94 ? 18.062 25.350 27.348 1.00 19.70 ? 94 ILE A CB 1 ATOM 723 C CG1 . ILE A 1 94 ? 17.881 26.793 27.866 1.00 19.83 ? 94 ILE A CG1 1 ATOM 724 C CG2 . ILE A 1 94 ? 16.774 24.492 27.398 1.00 19.68 ? 94 ILE A CG2 1 ATOM 725 C CD1 . ILE A 1 94 ? 17.112 27.721 26.922 1.00 19.07 ? 94 ILE A CD1 1 ATOM 726 N N . ASP A 1 95 ? 18.848 25.077 30.461 1.00 20.13 ? 95 ASP A N 1 ATOM 727 C CA . ASP A 1 95 ? 18.246 24.836 31.780 1.00 20.39 ? 95 ASP A CA 1 ATOM 728 C C . ASP A 1 95 ? 16.748 25.069 31.729 1.00 20.14 ? 95 ASP A C 1 ATOM 729 O O . ASP A 1 95 ? 16.273 26.170 32.004 1.00 20.35 ? 95 ASP A O 1 ATOM 730 C CB . ASP A 1 95 ? 18.879 25.736 32.821 1.00 20.14 ? 95 ASP A CB 1 ATOM 731 C CG . ASP A 1 95 ? 20.337 25.416 33.021 1.00 22.43 ? 95 ASP A CG 1 ATOM 732 O OD1 . ASP A 1 95 ? 21.185 26.152 32.474 1.00 22.79 ? 95 ASP A OD1 1 ATOM 733 O OD2 . ASP A 1 95 ? 20.621 24.388 33.680 1.00 22.87 ? 95 ASP A OD2 1 ATOM 734 N N . ALA A 1 96 ? 16.017 24.030 31.342 1.00 20.38 ? 96 ALA A N 1 ATOM 735 C CA . ALA A 1 96 ? 14.575 24.023 31.463 1.00 20.24 ? 96 ALA A CA 1 ATOM 736 C C . ALA A 1 96 ? 14.320 23.207 32.714 1.00 20.61 ? 96 ALA A C 1 ATOM 737 O O . ALA A 1 96 ? 14.138 21.978 32.654 1.00 20.61 ? 96 ALA A O 1 ATOM 738 C CB . ALA A 1 96 ? 13.930 23.389 30.259 1.00 19.29 ? 96 ALA A CB 1 ATOM 739 N N . VAL A 1 97 ? 14.280 23.905 33.850 1.00 20.85 ? 97 VAL A N 1 ATOM 740 C CA . VAL A 1 97 ? 14.294 23.249 35.149 1.00 20.53 ? 97 VAL A CA 1 ATOM 741 C C . VAL A 1 97 ? 12.980 23.402 35.927 1.00 20.57 ? 97 VAL A C 1 ATOM 742 O O . VAL A 1 97 ? 12.785 22.709 36.918 1.00 20.02 ? 97 VAL A O 1 ATOM 743 C CB . VAL A 1 97 ? 15.533 23.637 36.026 1.00 20.42 ? 97 VAL A CB 1 ATOM 744 C CG1 . VAL A 1 97 ? 16.822 23.207 35.350 1.00 20.87 ? 97 VAL A CG1 1 ATOM 745 C CG2 . VAL A 1 97 ? 15.553 25.142 36.335 1.00 20.62 ? 97 VAL A CG2 1 ATOM 746 N N . HIS A 1 98 ? 12.101 24.297 35.474 1.00 19.45 ? 98 HIS A N 1 ATOM 747 C CA . HIS A 1 98 ? 10.714 24.368 35.982 1.00 19.67 ? 98 HIS A CA 1 ATOM 748 C C . HIS A 1 98 ? 9.862 24.947 34.873 1.00 19.55 ? 98 HIS A C 1 ATOM 749 O O . HIS A 1 98 ? 9.316 26.038 34.962 1.00 20.01 ? 98 HIS A O 1 ATOM 750 C CB . HIS A 1 98 ? 10.589 25.112 37.340 1.00 19.49 ? 98 HIS A CB 1 ATOM 751 C CG . HIS A 1 98 ? 10.988 26.560 37.311 1.00 20.22 ? 98 HIS A CG 1 ATOM 752 N ND1 . HIS A 1 98 ? 10.353 27.520 38.077 1.00 20.88 ? 98 HIS A ND1 1 ATOM 753 C CD2 . HIS A 1 98 ? 11.968 27.209 36.635 1.00 19.40 ? 98 HIS A CD2 1 ATOM 754 C CE1 . HIS A 1 98 ? 10.925 28.692 37.870 1.00 21.02 ? 98 HIS A CE1 1 ATOM 755 N NE2 . HIS A 1 98 ? 11.891 28.535 36.984 1.00 20.38 ? 98 HIS A NE2 1 ATOM 756 N N . GLY A 1 99 ? 9.784 24.177 33.798 1.00 19.89 ? 99 GLY A N 1 ATOM 757 C CA . GLY A 1 99 ? 9.331 24.688 32.523 1.00 19.78 ? 99 GLY A CA 1 ATOM 758 C C . GLY A 1 99 ? 10.522 25.132 31.694 1.00 19.85 ? 99 GLY A C 1 ATOM 759 O O . GLY A 1 99 ? 11.666 24.981 32.108 1.00 19.33 ? 99 GLY A O 1 ATOM 760 N N . GLN A 1 100 ? 10.232 25.684 30.518 1.00 20.17 ? 100 GLN A N 1 ATOM 761 C CA . GLN A 1 100 ? 11.233 26.208 29.598 1.00 20.47 ? 100 GLN A CA 1 ATOM 762 C C . GLN A 1 100 ? 11.515 27.654 30.033 1.00 20.43 ? 100 GLN A C 1 ATOM 763 O O . GLN A 1 100 ? 11.212 28.626 29.335 1.00 20.63 ? 100 GLN A O 1 ATOM 764 C CB . GLN A 1 100 ? 10.692 26.085 28.150 1.00 20.56 ? 100 GLN A CB 1 ATOM 765 C CG . GLN A 1 100 ? 11.525 26.720 26.999 1.00 20.74 ? 100 GLN A CG 1 ATOM 766 C CD . GLN A 1 100 ? 12.981 26.287 26.954 1.00 20.85 ? 100 GLN A CD 1 ATOM 767 O OE1 . GLN A 1 100 ? 13.639 26.155 27.991 1.00 20.14 ? 100 GLN A OE1 1 ATOM 768 N NE2 . GLN A 1 100 ? 13.507 26.097 25.743 1.00 18.65 ? 100 GLN A NE2 1 ATOM 769 N N . ASN A 1 101 ? 12.092 27.761 31.224 1.00 20.38 ? 101 ASN A N 1 ATOM 770 C CA . ASN A 1 101 ? 12.087 28.972 32.042 1.00 20.05 ? 101 ASN A CA 1 ATOM 771 C C . ASN A 1 101 ? 12.870 30.196 31.535 1.00 20.80 ? 101 ASN A C 1 ATOM 772 O O . ASN A 1 101 ? 12.649 31.322 32.026 1.00 21.18 ? 101 ASN A O 1 ATOM 773 C CB . ASN A 1 101 ? 12.493 28.609 33.482 1.00 19.61 ? 101 ASN A CB 1 ATOM 774 C CG . ASN A 1 101 ? 13.797 27.823 33.551 1.00 20.22 ? 101 ASN A CG 1 ATOM 775 O OD1 . ASN A 1 101 ? 14.899 28.366 33.355 1.00 22.75 ? 101 ASN A OD1 1 ATOM 776 N ND2 . ASN A 1 101 ? 13.681 26.546 33.853 1.00 16.82 ? 101 ASN A ND2 1 ATOM 777 N N . ASN A 1 102 ? 13.756 30.006 30.547 1.00 20.48 ? 102 ASN A N 1 ATOM 778 C CA . ASN A 1 102 ? 14.483 31.144 29.960 1.00 20.46 ? 102 ASN A CA 1 ATOM 779 C C . ASN A 1 102 ? 13.609 31.923 28.980 1.00 20.56 ? 102 ASN A C 1 ATOM 780 O O . ASN A 1 102 ? 13.910 33.057 28.635 1.00 21.26 ? 102 ASN A O 1 ATOM 781 C CB . ASN A 1 102 ? 15.783 30.692 29.246 1.00 19.86 ? 102 ASN A CB 1 ATOM 782 C CG . ASN A 1 102 ? 16.928 30.392 30.209 1.00 20.48 ? 102 ASN A CG 1 ATOM 783 O OD1 . ASN A 1 102 ? 17.511 29.297 30.184 1.00 23.50 ? 102 ASN A OD1 1 ATOM 784 N ND2 . ASN A 1 102 ? 17.259 31.347 31.050 1.00 17.21 ? 102 ASN A ND2 1 ATOM 785 N N . VAL A 1 103 ? 12.519 31.299 28.553 1.00 20.40 ? 103 VAL A N 1 ATOM 786 C CA . VAL A 1 103 ? 11.754 31.741 27.387 1.00 20.98 ? 103 VAL A CA 1 ATOM 787 C C . VAL A 1 103 ? 10.538 32.542 27.815 1.00 21.29 ? 103 VAL A C 1 ATOM 788 O O . VAL A 1 103 ? 9.808 32.133 28.713 1.00 20.87 ? 103 VAL A O 1 ATOM 789 C CB . VAL A 1 103 ? 11.355 30.521 26.524 1.00 20.91 ? 103 VAL A CB 1 ATOM 790 C CG1 . VAL A 1 103 ? 10.425 30.922 25.341 1.00 21.40 ? 103 VAL A CG1 1 ATOM 791 C CG2 . VAL A 1 103 ? 12.609 29.850 26.003 1.00 19.72 ? 103 VAL A CG2 1 ATOM 792 N N . TYR A 1 104 ? 10.338 33.691 27.180 1.00 22.19 ? 104 TYR A N 1 ATOM 793 C CA . TYR A 1 104 ? 9.216 34.550 27.487 1.00 23.73 ? 104 TYR A CA 1 ATOM 794 C C . TYR A 1 104 ? 7.925 33.831 27.084 1.00 24.08 ? 104 TYR A C 1 ATOM 795 O O . TYR A 1 104 ? 7.825 33.295 25.977 1.00 24.33 ? 104 TYR A O 1 ATOM 796 C CB . TYR A 1 104 ? 9.334 35.902 26.766 1.00 25.79 ? 104 TYR A CB 1 ATOM 797 C CG . TYR A 1 104 ? 8.126 36.798 27.003 1.00 27.89 ? 104 TYR A CG 1 ATOM 798 C CD1 . TYR A 1 104 ? 8.063 37.630 28.119 1.00 28.20 ? 104 TYR A CD1 1 ATOM 799 C CD2 . TYR A 1 104 ? 7.035 36.783 26.126 1.00 29.73 ? 104 TYR A CD2 1 ATOM 800 C CE1 . TYR A 1 104 ? 6.959 38.435 28.358 1.00 29.18 ? 104 TYR A CE1 1 ATOM 801 C CE2 . TYR A 1 104 ? 5.924 37.586 26.357 1.00 31.16 ? 104 TYR A CE2 1 ATOM 802 C CZ . TYR A 1 104 ? 5.894 38.406 27.479 1.00 31.38 ? 104 TYR A CZ 1 ATOM 803 O OH . TYR A 1 104 ? 4.788 39.204 27.722 1.00 33.23 ? 104 TYR A OH 1 ATOM 804 N N . GLY A 1 105 ? 6.942 33.825 27.977 1.00 23.76 ? 105 GLY A N 1 ATOM 805 C CA . GLY A 1 105 ? 5.657 33.188 27.690 1.00 23.62 ? 105 GLY A CA 1 ATOM 806 C C . GLY A 1 105 ? 5.624 31.688 27.903 1.00 22.56 ? 105 GLY A C 1 ATOM 807 O O . GLY A 1 105 ? 4.583 31.059 27.712 1.00 23.53 ? 105 GLY A O 1 ATOM 808 N N . ALA A 1 106 ? 6.751 31.107 28.307 1.00 21.26 ? 106 ALA A N 1 ATOM 809 C CA . ALA A 1 106 ? 6.790 29.707 28.726 1.00 20.48 ? 106 ALA A CA 1 ATOM 810 C C . ALA A 1 106 ? 6.043 29.500 30.052 1.00 20.13 ? 106 ALA A C 1 ATOM 811 O O . ALA A 1 106 ? 6.118 30.336 30.951 1.00 20.04 ? 106 ALA A O 1 ATOM 812 C CB . ALA A 1 106 ? 8.239 29.236 28.880 1.00 19.46 ? 106 ALA A CB 1 ATOM 813 N N . THR A 1 107 ? 5.337 28.379 30.166 1.00 20.25 ? 107 THR A N 1 ATOM 814 C CA . THR A 1 107 ? 4.713 27.986 31.423 1.00 20.32 ? 107 THR A CA 1 ATOM 815 C C . THR A 1 107 ? 5.792 27.803 32.485 1.00 20.17 ? 107 THR A C 1 ATOM 816 O O . THR A 1 107 ? 6.746 27.058 32.254 1.00 20.15 ? 107 THR A O 1 ATOM 817 C CB . THR A 1 107 ? 3.968 26.643 31.276 1.00 20.47 ? 107 THR A CB 1 ATOM 818 O OG1 . THR A 1 107 ? 3.004 26.749 30.227 1.00 20.66 ? 107 THR A OG1 1 ATOM 819 C CG2 . THR A 1 107 ? 3.271 26.278 32.576 1.00 19.41 ? 107 THR A CG2 1 ATOM 820 N N . ILE A 1 108 ? 5.649 28.480 33.631 1.00 20.21 ? 108 ILE A N 1 ATOM 821 C CA . ILE A 1 108 ? 6.598 28.326 34.730 1.00 19.60 ? 108 ILE A CA 1 ATOM 822 C C . ILE A 1 108 ? 5.994 27.464 35.841 1.00 20.17 ? 108 ILE A C 1 ATOM 823 O O . ILE A 1 108 ? 5.021 27.867 36.499 1.00 21.02 ? 108 ILE A O 1 ATOM 824 C CB . ILE A 1 108 ? 7.117 29.689 35.303 1.00 19.80 ? 108 ILE A CB 1 ATOM 825 C CG1 . ILE A 1 108 ? 7.736 30.584 34.209 1.00 19.52 ? 108 ILE A CG1 1 ATOM 826 C CG2 . ILE A 1 108 ? 8.126 29.449 36.450 1.00 18.29 ? 108 ILE A CG2 1 ATOM 827 C CD1 . ILE A 1 108 ? 8.903 29.933 33.421 1.00 17.94 ? 108 ILE A CD1 1 ATOM 828 N N . PHE A 1 109 ? 6.567 26.272 36.021 1.00 19.33 ? 109 PHE A N 1 ATOM 829 C CA . PHE A 1 109 ? 6.088 25.310 37.011 1.00 19.94 ? 109 PHE A CA 1 ATOM 830 C C . PHE A 1 109 ? 6.715 25.608 38.371 1.00 20.20 ? 109 PHE A C 1 ATOM 831 O O . PHE A 1 109 ? 7.743 26.297 38.433 1.00 20.21 ? 109 PHE A O 1 ATOM 832 C CB . PHE A 1 109 ? 6.410 23.868 36.559 1.00 19.94 ? 109 PHE A CB 1 ATOM 833 C CG . PHE A 1 109 ? 5.681 23.460 35.306 1.00 21.37 ? 109 PHE A CG 1 ATOM 834 C CD1 . PHE A 1 109 ? 6.257 23.654 34.050 1.00 20.60 ? 109 PHE A CD1 1 ATOM 835 C CD2 . PHE A 1 109 ? 4.401 22.911 35.379 1.00 21.70 ? 109 PHE A CD2 1 ATOM 836 C CE1 . PHE A 1 109 ? 5.562 23.306 32.877 1.00 22.80 ? 109 PHE A CE1 1 ATOM 837 C CE2 . PHE A 1 109 ? 3.713 22.546 34.231 1.00 22.34 ? 109 PHE A CE2 1 ATOM 838 C CZ . PHE A 1 109 ? 4.290 22.752 32.973 1.00 21.31 ? 109 PHE A CZ 1 ATOM 839 N N . PRO A 1 110 ? 6.106 25.089 39.467 1.00 20.48 ? 110 PRO A N 1 ATOM 840 C CA . PRO A 1 110 ? 6.749 25.207 40.773 1.00 20.56 ? 110 PRO A CA 1 ATOM 841 C C . PRO A 1 110 ? 8.144 24.585 40.751 1.00 20.24 ? 110 PRO A C 1 ATOM 842 O O . PRO A 1 110 ? 8.363 23.551 40.087 1.00 21.25 ? 110 PRO A O 1 ATOM 843 C CB . PRO A 1 110 ? 5.819 24.406 41.707 1.00 20.85 ? 110 PRO A CB 1 ATOM 844 C CG . PRO A 1 110 ? 4.486 24.440 41.044 1.00 20.46 ? 110 PRO A CG 1 ATOM 845 C CD . PRO A 1 110 ? 4.817 24.366 39.552 1.00 20.65 ? 110 PRO A CD 1 ATOM 846 N N . HIS A 1 111 ? 9.079 25.219 41.457 1.00 19.69 ? 111 HIS A N 1 ATOM 847 C CA . HIS A 1 111 ? 10.409 24.674 41.657 1.00 18.97 ? 111 HIS A CA 1 ATOM 848 C C . HIS A 1 111 ? 10.373 23.346 42.416 1.00 19.82 ? 111 HIS A C 1 ATOM 849 O O . HIS A 1 111 ? 9.392 23.034 43.109 1.00 20.23 ? 111 HIS A O 1 ATOM 850 C CB . HIS A 1 111 ? 11.309 25.689 42.363 1.00 18.74 ? 111 HIS A CB 1 ATOM 851 C CG . HIS A 1 111 ? 12.039 26.606 41.420 1.00 18.82 ? 111 HIS A CG 1 ATOM 852 N ND1 . HIS A 1 111 ? 12.856 26.142 40.412 1.00 19.29 ? 111 HIS A ND1 1 ATOM 853 C CD2 . HIS A 1 111 ? 12.075 27.959 41.340 1.00 19.50 ? 111 HIS A CD2 1 ATOM 854 C CE1 . HIS A 1 111 ? 13.364 27.168 39.751 1.00 20.76 ? 111 HIS A CE1 1 ATOM 855 N NE2 . HIS A 1 111 ? 12.917 28.283 40.303 1.00 18.65 ? 111 HIS A NE2 1 ATOM 856 N N . ASN A 1 112 ? 11.443 22.568 42.278 1.00 19.40 ? 112 ASN A N 1 ATOM 857 C CA . ASN A 1 112 ? 11.489 21.217 42.819 1.00 20.54 ? 112 ASN A CA 1 ATOM 858 C C . ASN A 1 112 ? 11.062 21.002 44.260 1.00 20.68 ? 112 ASN A C 1 ATOM 859 O O . ASN A 1 112 ? 10.368 20.031 44.529 1.00 21.26 ? 112 ASN A O 1 ATOM 860 C CB . ASN A 1 112 ? 12.861 20.568 42.591 1.00 20.50 ? 112 ASN A CB 1 ATOM 861 C CG . ASN A 1 112 ? 13.089 20.199 41.139 1.00 20.02 ? 112 ASN A CG 1 ATOM 862 O OD1 . ASN A 1 112 ? 12.191 20.334 40.302 1.00 20.95 ? 112 ASN A OD1 1 ATOM 863 N ND2 . ASN A 1 112 ? 14.290 19.720 40.835 1.00 19.98 ? 112 ASN A ND2 1 ATOM 864 N N . VAL A 1 113 ? 11.487 21.872 45.185 1.00 21.02 ? 113 VAL A N 1 ATOM 865 C CA . VAL A 1 113 ? 11.114 21.690 46.593 1.00 21.15 ? 113 VAL A CA 1 ATOM 866 C C . VAL A 1 113 ? 9.593 21.600 46.757 1.00 21.79 ? 113 VAL A C 1 ATOM 867 O O . VAL A 1 113 ? 9.096 20.783 47.538 1.00 22.20 ? 113 VAL A O 1 ATOM 868 C CB . VAL A 1 113 ? 11.729 22.767 47.552 1.00 22.04 ? 113 VAL A CB 1 ATOM 869 C CG1 . VAL A 1 113 ? 11.263 24.196 47.190 1.00 21.69 ? 113 VAL A CG1 1 ATOM 870 C CG2 . VAL A 1 113 ? 11.387 22.455 49.029 1.00 21.04 ? 113 VAL A CG2 1 ATOM 871 N N . GLY A 1 114 ? 8.859 22.437 46.021 1.00 21.53 ? 114 GLY A N 1 ATOM 872 C CA . GLY A 1 114 ? 7.405 22.420 46.083 1.00 21.78 ? 114 GLY A CA 1 ATOM 873 C C . GLY A 1 114 ? 6.849 21.179 45.434 1.00 21.83 ? 114 GLY A C 1 ATOM 874 O O . GLY A 1 114 ? 5.863 20.616 45.905 1.00 23.73 ? 114 GLY A O 1 ATOM 875 N N . LEU A 1 115 ? 7.485 20.737 44.355 1.00 21.24 ? 115 LEU A N 1 ATOM 876 C CA . LEU A 1 115 ? 7.133 19.453 43.738 1.00 21.41 ? 115 LEU A CA 1 ATOM 877 C C . LEU A 1 115 ? 7.301 18.277 44.718 1.00 21.93 ? 115 LEU A C 1 ATOM 878 O O . LEU A 1 115 ? 6.447 17.400 44.784 1.00 21.90 ? 115 LEU A O 1 ATOM 879 C CB . LEU A 1 115 ? 7.925 19.228 42.429 1.00 20.72 ? 115 LEU A CB 1 ATOM 880 C CG . LEU A 1 115 ? 7.591 20.279 41.353 1.00 20.17 ? 115 LEU A CG 1 ATOM 881 C CD1 . LEU A 1 115 ? 8.318 19.953 40.056 1.00 19.08 ? 115 LEU A CD1 1 ATOM 882 C CD2 . LEU A 1 115 ? 6.041 20.425 41.142 1.00 19.54 ? 115 LEU A CD2 1 ATOM 883 N N . GLY A 1 116 ? 8.385 18.278 45.492 1.00 21.95 ? 116 GLY A N 1 ATOM 884 C CA . GLY A 1 116 ? 8.565 17.291 46.558 1.00 22.34 ? 116 GLY A CA 1 ATOM 885 C C . GLY A 1 116 ? 7.440 17.292 47.581 1.00 24.08 ? 116 GLY A C 1 ATOM 886 O O . GLY A 1 116 ? 7.052 16.227 48.088 1.00 25.35 ? 116 GLY A O 1 ATOM 887 N N . ALA A 1 117 ? 6.888 18.474 47.875 1.00 23.70 ? 117 ALA A N 1 ATOM 888 C CA . ALA A 1 117 ? 5.769 18.591 48.827 1.00 24.52 ? 117 ALA A CA 1 ATOM 889 C C . ALA A 1 117 ? 4.492 17.912 48.340 1.00 25.09 ? 117 ALA A C 1 ATOM 890 O O . ALA A 1 117 ? 3.623 17.573 49.135 1.00 25.38 ? 117 ALA A O 1 ATOM 891 C CB . ALA A 1 117 ? 5.492 20.055 49.184 1.00 23.93 ? 117 ALA A CB 1 ATOM 892 N N . THR A 1 118 ? 4.391 17.703 47.032 1.00 25.11 ? 118 THR A N 1 ATOM 893 C CA . THR A 1 118 ? 3.183 17.136 46.441 1.00 26.10 ? 118 THR A CA 1 ATOM 894 C C . THR A 1 118 ? 3.120 15.626 46.658 1.00 26.96 ? 118 THR A C 1 ATOM 895 O O . THR A 1 118 ? 2.036 15.036 46.595 1.00 28.02 ? 118 THR A O 1 ATOM 896 C CB . THR A 1 118 ? 3.074 17.391 44.919 1.00 25.43 ? 118 THR A CB 1 ATOM 897 O OG1 . THR A 1 118 ? 4.027 16.574 44.218 1.00 25.74 ? 118 THR A OG1 1 ATOM 898 C CG2 . THR A 1 118 ? 3.293 18.864 44.562 1.00 24.93 ? 118 THR A CG2 1 ATOM 899 N N . ARG A 1 119 ? 4.277 15.003 46.892 1.00 27.26 ? 119 ARG A N 1 ATOM 900 C CA . ARG A 1 119 ? 4.400 13.525 46.906 1.00 28.56 ? 119 ARG A CA 1 ATOM 901 C C . ARG A 1 119 ? 3.698 12.830 45.717 1.00 28.82 ? 119 ARG A C 1 ATOM 902 O O . ARG A 1 119 ? 3.144 11.732 45.862 1.00 30.19 ? 119 ARG A O 1 ATOM 903 C CB . ARG A 1 119 ? 3.860 12.931 48.218 1.00 29.29 ? 119 ARG A CB 1 ATOM 904 C CG . ARG A 1 119 ? 4.454 13.485 49.493 1.00 29.83 ? 119 ARG A CG 1 ATOM 905 C CD . ARG A 1 119 ? 5.953 13.174 49.652 1.00 29.21 ? 119 ARG A CD 1 ATOM 906 N NE . ARG A 1 119 ? 6.336 13.299 51.057 1.00 29.68 ? 119 ARG A NE 1 ATOM 907 C CZ . ARG A 1 119 ? 6.596 14.452 51.670 1.00 29.89 ? 119 ARG A CZ 1 ATOM 908 N NH1 . ARG A 1 119 ? 6.529 15.598 50.994 1.00 27.50 ? 119 ARG A NH1 1 ATOM 909 N NH2 . ARG A 1 119 ? 6.922 14.460 52.961 1.00 28.67 ? 119 ARG A NH2 1 ATOM 910 N N . ASP A 1 120 ? 3.714 13.468 44.554 1.00 28.13 ? 120 ASP A N 1 ATOM 911 C CA . ASP A 1 120 ? 2.963 12.982 43.397 1.00 28.56 ? 120 ASP A CA 1 ATOM 912 C C . ASP A 1 120 ? 3.923 12.833 42.200 1.00 27.78 ? 120 ASP A C 1 ATOM 913 O O . ASP A 1 120 ? 4.107 13.771 41.415 1.00 27.10 ? 120 ASP A O 1 ATOM 914 C CB . ASP A 1 120 ? 1.814 13.958 43.110 1.00 29.03 ? 120 ASP A CB 1 ATOM 915 C CG . ASP A 1 120 ? 0.804 13.426 42.091 1.00 30.87 ? 120 ASP A CG 1 ATOM 916 O OD1 . ASP A 1 120 ? 1.067 12.402 41.421 1.00 34.93 ? 120 ASP A OD1 1 ATOM 917 O OD2 . ASP A 1 120 ? -0.261 14.055 41.965 1.00 31.62 ? 120 ASP A OD2 1 ATOM 918 N N . PRO A 1 121 ? 4.578 11.658 42.083 1.00 27.69 ? 121 PRO A N 1 ATOM 919 C CA . PRO A 1 121 ? 5.530 11.435 40.997 1.00 26.82 ? 121 PRO A CA 1 ATOM 920 C C . PRO A 1 121 ? 4.893 11.494 39.607 1.00 26.55 ? 121 PRO A C 1 ATOM 921 O O . PRO A 1 121 ? 5.556 11.907 38.671 1.00 25.40 ? 121 PRO A O 1 ATOM 922 C CB . PRO A 1 121 ? 6.068 10.028 41.278 1.00 27.30 ? 121 PRO A CB 1 ATOM 923 C CG . PRO A 1 121 ? 5.806 9.799 42.747 1.00 28.84 ? 121 PRO A CG 1 ATOM 924 C CD . PRO A 1 121 ? 4.487 10.489 42.981 1.00 29.04 ? 121 PRO A CD 1 ATOM 925 N N . TYR A 1 122 ? 3.628 11.081 39.485 1.00 27.52 ? 122 TYR A N 1 ATOM 926 C CA . TYR A 1 122 ? 2.893 11.160 38.217 1.00 27.63 ? 122 TYR A CA 1 ATOM 927 C C . TYR A 1 122 ? 2.604 12.599 37.778 1.00 26.48 ? 122 TYR A C 1 ATOM 928 O O . TYR A 1 122 ? 2.691 12.911 36.589 1.00 25.83 ? 122 TYR A O 1 ATOM 929 C CB . TYR A 1 122 ? 1.604 10.329 38.249 1.00 29.91 ? 122 TYR A CB 1 ATOM 930 C CG . TYR A 1 122 ? 0.884 10.336 36.916 1.00 31.95 ? 122 TYR A CG 1 ATOM 931 C CD1 . TYR A 1 122 ? 1.540 9.926 35.742 1.00 33.00 ? 122 TYR A CD1 1 ATOM 932 C CD2 . TYR A 1 122 ? -0.439 10.792 36.814 1.00 33.02 ? 122 TYR A CD2 1 ATOM 933 C CE1 . TYR A 1 122 ? 0.887 9.955 34.501 1.00 35.01 ? 122 TYR A CE1 1 ATOM 934 C CE2 . TYR A 1 122 ? -1.104 10.816 35.586 1.00 34.18 ? 122 TYR A CE2 1 ATOM 935 C CZ . TYR A 1 122 ? -0.441 10.402 34.437 1.00 34.72 ? 122 TYR A CZ 1 ATOM 936 O OH . TYR A 1 122 ? -1.092 10.434 33.218 1.00 35.33 ? 122 TYR A OH 1 ATOM 937 N N . LEU A 1 123 ? 2.272 13.476 38.729 1.00 25.99 ? 123 LEU A N 1 ATOM 938 C CA . LEU A 1 123 ? 2.207 14.920 38.459 1.00 24.82 ? 123 LEU A CA 1 ATOM 939 C C . LEU A 1 123 ? 3.547 15.407 37.908 1.00 23.50 ? 123 LEU A C 1 ATOM 940 O O . LEU A 1 123 ? 3.589 16.141 36.923 1.00 23.46 ? 123 LEU A O 1 ATOM 941 C CB . LEU A 1 123 ? 1.848 15.700 39.733 1.00 25.04 ? 123 LEU A CB 1 ATOM 942 C CG . LEU A 1 123 ? 1.825 17.238 39.700 1.00 25.08 ? 123 LEU A CG 1 ATOM 943 C CD1 . LEU A 1 123 ? 0.587 17.747 38.964 1.00 24.80 ? 123 LEU A CD1 1 ATOM 944 C CD2 . LEU A 1 123 ? 1.884 17.834 41.130 1.00 23.60 ? 123 LEU A CD2 1 ATOM 945 N N . VAL A 1 124 ? 4.640 14.991 38.540 1.00 22.93 ? 124 VAL A N 1 ATOM 946 C CA . VAL A 1 124 ? 5.982 15.370 38.089 1.00 22.20 ? 124 VAL A CA 1 ATOM 947 C C . VAL A 1 124 ? 6.301 14.812 36.688 1.00 22.31 ? 124 VAL A C 1 ATOM 948 O O . VAL A 1 124 ? 6.909 15.500 35.865 1.00 20.97 ? 124 VAL A O 1 ATOM 949 C CB . VAL A 1 124 ? 7.063 15.034 39.153 1.00 22.01 ? 124 VAL A CB 1 ATOM 950 C CG1 . VAL A 1 124 ? 8.468 15.256 38.613 1.00 21.24 ? 124 VAL A CG1 1 ATOM 951 C CG2 . VAL A 1 124 ? 6.845 15.910 40.400 1.00 20.95 ? 124 VAL A CG2 1 ATOM 952 N N . LYS A 1 125 ? 5.861 13.579 36.417 1.00 23.71 ? 125 LYS A N 1 ATOM 953 C CA . LYS A 1 125 ? 6.017 13.004 35.082 1.00 23.59 ? 125 LYS A CA 1 ATOM 954 C C . LYS A 1 125 ? 5.307 13.886 34.052 1.00 23.95 ? 125 LYS A C 1 ATOM 955 O O . LYS A 1 125 ? 5.865 14.191 32.995 1.00 23.31 ? 125 LYS A O 1 ATOM 956 C CB . LYS A 1 125 ? 5.463 11.577 35.024 1.00 24.43 ? 125 LYS A CB 1 ATOM 957 C CG . LYS A 1 125 ? 5.839 10.858 33.733 1.00 24.62 ? 125 LYS A CG 1 ATOM 958 C CD . LYS A 1 125 ? 5.118 9.547 33.574 1.00 25.42 ? 125 LYS A CD 1 ATOM 959 C CE . LYS A 1 125 ? 5.504 8.887 32.264 1.00 25.63 ? 125 LYS A CE 1 ATOM 960 N NZ . LYS A 1 125 ? 4.938 7.499 32.230 1.00 27.44 ? 125 LYS A NZ 1 ATOM 961 N N . ARG A 1 126 ? 4.074 14.295 34.364 1.00 24.42 ? 126 ARG A N 1 ATOM 962 C CA . ARG A 1 126 ? 3.284 15.145 33.462 1.00 24.12 ? 126 ARG A CA 1 ATOM 963 C C . ARG A 1 126 ? 3.935 16.520 33.207 1.00 22.68 ? 126 ARG A C 1 ATOM 964 O O . ARG A 1 126 ? 3.902 17.043 32.079 1.00 21.63 ? 126 ARG A O 1 ATOM 965 C CB . ARG A 1 126 ? 1.856 15.286 33.992 1.00 24.98 ? 126 ARG A CB 1 ATOM 966 C CG . ARG A 1 126 ? 1.011 14.012 33.828 1.00 26.57 ? 126 ARG A CG 1 ATOM 967 C CD . ARG A 1 126 ? -0.435 14.258 34.249 1.00 27.66 ? 126 ARG A CD 1 ATOM 968 N NE . ARG A 1 126 ? -0.576 14.304 35.703 1.00 33.93 ? 126 ARG A NE 1 ATOM 969 C CZ . ARG A 1 126 ? -1.361 15.156 36.380 1.00 34.67 ? 126 ARG A CZ 1 ATOM 970 N NH1 . ARG A 1 126 ? -1.412 15.101 37.711 1.00 34.22 ? 126 ARG A NH1 1 ATOM 971 N NH2 . ARG A 1 126 ? -2.077 16.076 35.740 1.00 34.02 ? 126 ARG A NH2 1 ATOM 972 N N . ILE A 1 127 ? 4.537 17.083 34.254 1.00 21.55 ? 127 ILE A N 1 ATOM 973 C CA . ILE A 1 127 ? 5.322 18.316 34.140 1.00 20.88 ? 127 ILE A CA 1 ATOM 974 C C . ILE A 1 127 ? 6.489 18.112 33.158 1.00 20.60 ? 127 ILE A C 1 ATOM 975 O O . ILE A 1 127 ? 6.713 18.952 32.292 1.00 20.29 ? 127 ILE A O 1 ATOM 976 C CB . ILE A 1 127 ? 5.816 18.812 35.529 1.00 20.10 ? 127 ILE A CB 1 ATOM 977 C CG1 . ILE A 1 127 ? 4.623 19.344 36.323 1.00 20.55 ? 127 ILE A CG1 1 ATOM 978 C CG2 . ILE A 1 127 ? 6.894 19.911 35.363 1.00 18.67 ? 127 ILE A CG2 1 ATOM 979 C CD1 . ILE A 1 127 ? 4.870 19.559 37.798 1.00 19.48 ? 127 ILE A CD1 1 ATOM 980 N N . GLY A 1 128 ? 7.194 16.978 33.292 1.00 21.23 ? 128 GLY A N 1 ATOM 981 C CA . GLY A 1 128 ? 8.270 16.587 32.371 1.00 20.37 ? 128 GLY A CA 1 ATOM 982 C C . GLY A 1 128 ? 7.733 16.502 30.960 1.00 20.70 ? 128 GLY A C 1 ATOM 983 O O . GLY A 1 128 ? 8.363 16.973 30.018 1.00 19.07 ? 128 GLY A O 1 ATOM 984 N N . GLU A 1 129 ? 6.551 15.904 30.812 1.00 21.95 ? 129 GLU A N 1 ATOM 985 C CA . GLU A 1 129 ? 5.915 15.813 29.497 1.00 22.79 ? 129 GLU A CA 1 ATOM 986 C C . GLU A 1 129 ? 5.621 17.183 28.890 1.00 22.83 ? 129 GLU A C 1 ATOM 987 O O . GLU A 1 129 ? 5.970 17.432 27.729 1.00 22.37 ? 129 GLU A O 1 ATOM 988 C CB . GLU A 1 129 ? 4.666 14.944 29.561 1.00 24.09 ? 129 GLU A CB 1 ATOM 989 C CG . GLU A 1 129 ? 5.006 13.506 29.869 1.00 25.76 ? 129 GLU A CG 1 ATOM 990 C CD . GLU A 1 129 ? 3.794 12.627 30.064 1.00 30.23 ? 129 GLU A CD 1 ATOM 991 O OE1 . GLU A 1 129 ? 2.661 13.161 30.131 1.00 30.75 ? 129 GLU A OE1 1 ATOM 992 O OE2 . GLU A 1 129 ? 3.991 11.389 30.148 1.00 30.35 ? 129 GLU A OE2 1 ATOM 993 N N . ALA A 1 130 ? 5.005 18.072 29.684 1.00 22.67 ? 130 ALA A N 1 ATOM 994 C CA . ALA A 1 130 ? 4.666 19.426 29.233 1.00 22.13 ? 130 ALA A CA 1 ATOM 995 C C . ALA A 1 130 ? 5.918 20.221 28.929 1.00 21.74 ? 130 ALA A C 1 ATOM 996 O O . ALA A 1 130 ? 5.942 20.969 27.962 1.00 22.26 ? 130 ALA A O 1 ATOM 997 C CB . ALA A 1 130 ? 3.815 20.160 30.286 1.00 22.48 ? 130 ALA A CB 1 ATOM 998 N N . THR A 1 131 ? 6.947 20.058 29.768 1.00 21.40 ? 131 THR A N 1 ATOM 999 C CA . THR A 1 131 ? 8.228 20.743 29.615 1.00 20.69 ? 131 THR A CA 1 ATOM 1000 C C . THR A 1 131 ? 8.937 20.327 28.323 1.00 20.91 ? 131 THR A C 1 ATOM 1001 O O . THR A 1 131 ? 9.462 21.187 27.626 1.00 21.34 ? 131 THR A O 1 ATOM 1002 C CB . THR A 1 131 ? 9.171 20.517 30.841 1.00 20.59 ? 131 THR A CB 1 ATOM 1003 O OG1 . THR A 1 131 ? 8.528 20.956 32.054 1.00 20.85 ? 131 THR A OG1 1 ATOM 1004 C CG2 . THR A 1 131 ? 10.472 21.281 30.661 1.00 18.36 ? 131 THR A CG2 1 ATOM 1005 N N . ALA A 1 132 ? 8.945 19.028 27.989 1.00 20.99 ? 132 ALA A N 1 ATOM 1006 C CA . ALA A 1 132 ? 9.510 18.573 26.703 1.00 21.65 ? 132 ALA A CA 1 ATOM 1007 C C . ALA A 1 132 ? 8.865 19.277 25.503 1.00 22.16 ? 132 ALA A C 1 ATOM 1008 O O . ALA A 1 132 ? 9.554 19.690 24.570 1.00 22.64 ? 132 ALA A O 1 ATOM 1009 C CB . ALA A 1 132 ? 9.412 17.025 26.541 1.00 21.65 ? 132 ALA A CB 1 ATOM 1010 N N . LEU A 1 133 ? 7.543 19.413 25.535 1.00 22.88 ? 133 LEU A N 1 ATOM 1011 C CA . LEU A 1 133 ? 6.802 20.066 24.458 1.00 23.20 ? 133 LEU A CA 1 ATOM 1012 C C . LEU A 1 133 ? 7.161 21.549 24.307 1.00 22.95 ? 133 LEU A C 1 ATOM 1013 O O . LEU A 1 133 ? 7.356 22.025 23.177 1.00 23.32 ? 133 LEU A O 1 ATOM 1014 C CB . LEU A 1 133 ? 5.295 19.872 24.642 1.00 23.82 ? 133 LEU A CB 1 ATOM 1015 C CG . LEU A 1 133 ? 4.753 18.438 24.495 1.00 24.68 ? 133 LEU A CG 1 ATOM 1016 C CD1 . LEU A 1 133 ? 3.294 18.313 24.978 1.00 24.77 ? 133 LEU A CD1 1 ATOM 1017 C CD2 . LEU A 1 133 ? 4.871 17.947 23.078 1.00 24.32 ? 133 LEU A CD2 1 ATOM 1018 N N . GLU A 1 134 ? 7.256 22.263 25.433 1.00 22.78 ? 134 GLU A N 1 ATOM 1019 C CA . GLU A 1 134 ? 7.617 23.691 25.428 1.00 22.35 ? 134 GLU A CA 1 ATOM 1020 C C . GLU A 1 134 ? 9.084 23.962 25.069 1.00 21.30 ? 134 GLU A C 1 ATOM 1021 O O . GLU A 1 134 ? 9.390 24.980 24.456 1.00 20.54 ? 134 GLU A O 1 ATOM 1022 C CB . GLU A 1 134 ? 7.220 24.387 26.735 1.00 22.40 ? 134 GLU A CB 1 ATOM 1023 C CG . GLU A 1 134 ? 5.724 24.236 27.024 1.00 23.20 ? 134 GLU A CG 1 ATOM 1024 C CD . GLU A 1 134 ? 5.106 25.381 27.810 1.00 24.31 ? 134 GLU A CD 1 ATOM 1025 O OE1 . GLU A 1 134 ? 5.751 26.441 27.968 1.00 22.38 ? 134 GLU A OE1 1 ATOM 1026 O OE2 . GLU A 1 134 ? 3.945 25.206 28.262 1.00 23.06 ? 134 GLU A OE2 1 ATOM 1027 N N . VAL A 1 135 ? 9.973 23.044 25.439 1.00 20.49 ? 135 VAL A N 1 ATOM 1028 C CA . VAL A 1 135 ? 11.379 23.099 25.013 1.00 20.07 ? 135 VAL A CA 1 ATOM 1029 C C . VAL A 1 135 ? 11.461 22.849 23.487 1.00 20.22 ? 135 VAL A C 1 ATOM 1030 O O . VAL A 1 135 ? 12.149 23.592 22.761 1.00 20.42 ? 135 VAL A O 1 ATOM 1031 C CB . VAL A 1 135 ? 12.285 22.108 25.843 1.00 19.83 ? 135 VAL A CB 1 ATOM 1032 C CG1 . VAL A 1 135 ? 13.733 22.107 25.348 1.00 19.62 ? 135 VAL A CG1 1 ATOM 1033 C CG2 . VAL A 1 135 ? 12.275 22.462 27.342 1.00 19.01 ? 135 VAL A CG2 1 ATOM 1034 N N . ARG A 1 136 ? 10.740 21.838 22.998 1.00 19.71 ? 136 ARG A N 1 ATOM 1035 C CA . ARG A 1 136 ? 10.706 21.561 21.549 1.00 20.80 ? 136 ARG A CA 1 ATOM 1036 C C . ARG A 1 136 ? 10.011 22.667 20.747 1.00 21.15 ? 136 ARG A C 1 ATOM 1037 O O . ARG A 1 136 ? 10.320 22.860 19.562 1.00 20.42 ? 136 ARG A O 1 ATOM 1038 C CB . ARG A 1 136 ? 10.085 20.181 21.232 1.00 21.67 ? 136 ARG A CB 1 ATOM 1039 C CG . ARG A 1 136 ? 11.009 18.979 21.522 1.00 20.14 ? 136 ARG A CG 1 ATOM 1040 C CD . ARG A 1 136 ? 12.195 18.955 20.528 1.00 21.95 ? 136 ARG A CD 1 ATOM 1041 N NE . ARG A 1 136 ? 12.945 17.698 20.590 1.00 22.08 ? 136 ARG A NE 1 ATOM 1042 C CZ . ARG A 1 136 ? 13.784 17.261 19.647 1.00 24.68 ? 136 ARG A CZ 1 ATOM 1043 N NH1 . ARG A 1 136 ? 14.006 17.979 18.548 1.00 24.07 ? 136 ARG A NH1 1 ATOM 1044 N NH2 . ARG A 1 136 ? 14.405 16.094 19.800 1.00 24.64 ? 136 ARG A NH2 1 ATOM 1045 N N . ALA A 1 137 ? 9.082 23.381 21.402 1.00 20.87 ? 137 ALA A N 1 ATOM 1046 C CA . ALA A 1 137 ? 8.402 24.533 20.795 1.00 21.76 ? 137 ALA A CA 1 ATOM 1047 C C . ALA A 1 137 ? 9.417 25.594 20.364 1.00 21.22 ? 137 ALA A C 1 ATOM 1048 O O . ALA A 1 137 ? 9.195 26.343 19.414 1.00 21.88 ? 137 ALA A O 1 ATOM 1049 C CB . ALA A 1 137 ? 7.369 25.143 21.773 1.00 20.95 ? 137 ALA A CB 1 ATOM 1050 N N . THR A 1 138 ? 10.530 25.628 21.089 1.00 21.47 ? 138 THR A N 1 ATOM 1051 C CA . THR A 1 138 ? 11.626 26.581 20.858 1.00 21.19 ? 138 THR A CA 1 ATOM 1052 C C . THR A 1 138 ? 12.794 25.972 20.059 1.00 21.01 ? 138 THR A C 1 ATOM 1053 O O . THR A 1 138 ? 13.847 26.588 19.930 1.00 20.31 ? 138 THR A O 1 ATOM 1054 C CB . THR A 1 138 ? 12.110 27.207 22.206 1.00 20.46 ? 138 THR A CB 1 ATOM 1055 O OG1 . THR A 1 138 ? 12.747 26.213 23.029 1.00 20.61 ? 138 THR A OG1 1 ATOM 1056 C CG2 . THR A 1 138 ? 10.944 27.802 22.966 1.00 19.23 ? 138 THR A CG2 1 ATOM 1057 N N . GLY A 1 139 ? 12.600 24.760 19.533 1.00 21.41 ? 139 GLY A N 1 ATOM 1058 C CA . GLY A 1 139 ? 13.629 24.090 18.718 1.00 22.33 ? 139 GLY A CA 1 ATOM 1059 C C . GLY A 1 139 ? 14.764 23.456 19.512 1.00 22.27 ? 139 GLY A C 1 ATOM 1060 O O . GLY A 1 139 ? 15.761 23.009 18.945 1.00 23.34 ? 139 GLY A O 1 ATOM 1061 N N . ILE A 1 140 ? 14.637 23.403 20.830 1.00 21.34 ? 140 ILE A N 1 ATOM 1062 C CA . ILE A 1 140 ? 15.729 22.885 21.660 1.00 20.31 ? 140 ILE A CA 1 ATOM 1063 C C . ILE A 1 140 ? 15.492 21.406 21.991 1.00 20.65 ? 140 ILE A C 1 ATOM 1064 O O . ILE A 1 140 ? 14.343 20.984 22.196 1.00 20.61 ? 140 ILE A O 1 ATOM 1065 C CB . ILE A 1 140 ? 15.965 23.800 22.915 1.00 19.93 ? 140 ILE A CB 1 ATOM 1066 C CG1 . ILE A 1 140 ? 16.473 25.173 22.447 1.00 18.90 ? 140 ILE A CG1 1 ATOM 1067 C CG2 . ILE A 1 140 ? 16.925 23.160 23.918 1.00 18.96 ? 140 ILE A CG2 1 ATOM 1068 C CD1 . ILE A 1 140 ? 16.493 26.217 23.524 1.00 17.85 ? 140 ILE A CD1 1 ATOM 1069 N N . GLN A 1 141 ? 16.573 20.618 22.019 1.00 20.60 ? 141 GLN A N 1 ATOM 1070 C CA . GLN A 1 141 ? 16.453 19.148 22.100 1.00 21.31 ? 141 GLN A CA 1 ATOM 1071 C C . GLN A 1 141 ? 16.933 18.524 23.419 1.00 21.32 ? 141 GLN A C 1 ATOM 1072 O O . GLN A 1 141 ? 16.900 17.307 23.568 1.00 21.44 ? 141 GLN A O 1 ATOM 1073 C CB . GLN A 1 141 ? 17.191 18.468 20.934 1.00 21.41 ? 141 GLN A CB 1 ATOM 1074 C CG . GLN A 1 141 ? 16.977 19.081 19.554 1.00 22.03 ? 141 GLN A CG 1 ATOM 1075 C CD . GLN A 1 141 ? 18.061 20.099 19.163 1.00 22.09 ? 141 GLN A CD 1 ATOM 1076 O OE1 . GLN A 1 141 ? 18.768 20.643 20.014 1.00 20.14 ? 141 GLN A OE1 1 ATOM 1077 N NE2 . GLN A 1 141 ? 18.163 20.377 17.868 1.00 21.82 ? 141 GLN A NE2 1 ATOM 1078 N N . TYR A 1 142 ? 17.372 19.348 24.370 1.00 21.29 ? 142 TYR A N 1 ATOM 1079 C CA . TYR A 1 142 ? 18.115 18.848 25.532 1.00 21.29 ? 142 TYR A CA 1 ATOM 1080 C C . TYR A 1 142 ? 17.871 19.790 26.717 1.00 21.45 ? 142 TYR A C 1 ATOM 1081 O O . TYR A 1 142 ? 18.145 20.985 26.634 1.00 21.75 ? 142 TYR A O 1 ATOM 1082 C CB . TYR A 1 142 ? 19.600 18.771 25.128 1.00 21.15 ? 142 TYR A CB 1 ATOM 1083 C CG . TYR A 1 142 ? 20.649 18.320 26.136 1.00 20.62 ? 142 TYR A CG 1 ATOM 1084 C CD1 . TYR A 1 142 ? 21.990 18.671 25.950 1.00 20.67 ? 142 TYR A CD1 1 ATOM 1085 C CD2 . TYR A 1 142 ? 20.322 17.521 27.241 1.00 21.27 ? 142 TYR A CD2 1 ATOM 1086 C CE1 . TYR A 1 142 ? 22.989 18.247 26.835 1.00 20.83 ? 142 TYR A CE1 1 ATOM 1087 C CE2 . TYR A 1 142 ? 21.299 17.112 28.142 1.00 22.23 ? 142 TYR A CE2 1 ATOM 1088 C CZ . TYR A 1 142 ? 22.636 17.468 27.932 1.00 21.88 ? 142 TYR A CZ 1 ATOM 1089 O OH . TYR A 1 142 ? 23.599 17.058 28.834 1.00 21.55 ? 142 TYR A OH 1 ATOM 1090 N N . ALA A 1 143 ? 17.315 19.247 27.803 1.00 21.54 ? 143 ALA A N 1 ATOM 1091 C CA . ALA A 1 143 ? 17.106 19.998 29.053 1.00 20.76 ? 143 ALA A CA 1 ATOM 1092 C C . ALA A 1 143 ? 18.072 19.512 30.131 1.00 20.85 ? 143 ALA A C 1 ATOM 1093 O O . ALA A 1 143 ? 18.205 18.304 30.337 1.00 21.14 ? 143 ALA A O 1 ATOM 1094 C CB . ALA A 1 143 ? 15.668 19.823 29.536 1.00 21.01 ? 143 ALA A CB 1 ATOM 1095 N N . PHE A 1 144 ? 18.744 20.448 30.805 1.00 20.35 ? 144 PHE A N 1 ATOM 1096 C CA . PHE A 1 144 ? 19.582 20.119 31.961 1.00 20.43 ? 144 PHE A CA 1 ATOM 1097 C C . PHE A 1 144 ? 18.746 19.883 33.224 1.00 20.50 ? 144 PHE A C 1 ATOM 1098 O O . PHE A 1 144 ? 18.782 20.684 34.148 1.00 20.94 ? 144 PHE A O 1 ATOM 1099 C CB . PHE A 1 144 ? 20.606 21.229 32.223 1.00 20.07 ? 144 PHE A CB 1 ATOM 1100 C CG . PHE A 1 144 ? 21.475 21.560 31.036 1.00 20.70 ? 144 PHE A CG 1 ATOM 1101 C CD1 . PHE A 1 144 ? 21.639 22.879 30.639 1.00 20.76 ? 144 PHE A CD1 1 ATOM 1102 C CD2 . PHE A 1 144 ? 22.144 20.555 30.332 1.00 20.34 ? 144 PHE A CD2 1 ATOM 1103 C CE1 . PHE A 1 144 ? 22.443 23.208 29.532 1.00 22.61 ? 144 PHE A CE1 1 ATOM 1104 C CE2 . PHE A 1 144 ? 22.955 20.868 29.225 1.00 22.52 ? 144 PHE A CE2 1 ATOM 1105 C CZ . PHE A 1 144 ? 23.099 22.204 28.822 1.00 19.81 ? 144 PHE A CZ 1 ATOM 1106 N N . ALA A 1 145 ? 17.996 18.787 33.239 1.00 20.84 ? 145 ALA A N 1 ATOM 1107 C CA . ALA A 1 145 ? 17.075 18.454 34.320 1.00 21.07 ? 145 ALA A CA 1 ATOM 1108 C C . ALA A 1 145 ? 16.804 16.945 34.251 1.00 21.54 ? 145 ALA A C 1 ATOM 1109 O O . ALA A 1 145 ? 16.847 16.374 33.152 1.00 21.96 ? 145 ALA A O 1 ATOM 1110 C CB . ALA A 1 145 ? 15.783 19.235 34.182 1.00 20.13 ? 145 ALA A CB 1 ATOM 1111 N N . PRO A 1 146 ? 16.497 16.301 35.404 1.00 21.61 ? 146 PRO A N 1 ATOM 1112 C CA . PRO A 1 146 ? 16.293 16.852 36.768 1.00 21.60 ? 146 PRO A CA 1 ATOM 1113 C C . PRO A 1 146 ? 17.548 17.038 37.619 1.00 21.94 ? 146 PRO A C 1 ATOM 1114 O O . PRO A 1 146 ? 18.464 16.218 37.568 1.00 22.39 ? 146 PRO A O 1 ATOM 1115 C CB . PRO A 1 146 ? 15.420 15.795 37.447 1.00 21.52 ? 146 PRO A CB 1 ATOM 1116 C CG . PRO A 1 146 ? 15.845 14.505 36.805 1.00 22.55 ? 146 PRO A CG 1 ATOM 1117 C CD . PRO A 1 146 ? 16.300 14.839 35.377 1.00 22.46 ? 146 PRO A CD 1 ATOM 1118 N N . CYS A 1 147 ? 17.570 18.112 38.404 1.00 21.61 ? 147 CYS A N 1 ATOM 1119 C CA . CYS A 1 147 ? 18.460 18.182 39.546 1.00 22.25 ? 147 CYS A CA 1 ATOM 1120 C C . CYS A 1 147 ? 17.959 17.170 40.575 1.00 23.06 ? 147 CYS A C 1 ATOM 1121 O O . CYS A 1 147 ? 16.857 17.323 41.118 1.00 22.56 ? 147 CYS A O 1 ATOM 1122 C CB . CYS A 1 147 ? 18.480 19.577 40.158 1.00 21.77 ? 147 CYS A CB 1 ATOM 1123 S SG . CYS A 1 147 ? 19.573 19.654 41.595 1.00 23.78 ? 147 CYS A SG 1 ATOM 1124 N N . ILE A 1 148 ? 18.752 16.117 40.788 1.00 23.70 ? 148 ILE A N 1 ATOM 1125 C CA . ILE A 1 148 ? 18.455 15.098 41.798 1.00 23.86 ? 148 ILE A CA 1 ATOM 1126 C C . ILE A 1 148 ? 19.364 15.195 43.041 1.00 24.94 ? 148 ILE A C 1 ATOM 1127 O O . ILE A 1 148 ? 19.581 14.210 43.759 1.00 26.02 ? 148 ILE A O 1 ATOM 1128 C CB . ILE A 1 148 ? 18.383 13.659 41.187 1.00 24.64 ? 148 ILE A CB 1 ATOM 1129 C CG1 . ILE A 1 148 ? 19.661 13.299 40.390 1.00 25.02 ? 148 ILE A CG1 1 ATOM 1130 C CG2 . ILE A 1 148 ? 17.149 13.551 40.277 1.00 23.13 ? 148 ILE A CG2 1 ATOM 1131 C CD1 . ILE A 1 148 ? 19.861 11.785 40.191 1.00 22.96 ? 148 ILE A CD1 1 ATOM 1132 N N . ALA A 1 149 ? 19.862 16.404 43.311 1.00 24.30 ? 149 ALA A N 1 ATOM 1133 C CA . ALA A 1 149 ? 20.496 16.705 44.596 1.00 24.69 ? 149 ALA A CA 1 ATOM 1134 C C . ALA A 1 149 ? 19.538 16.366 45.729 1.00 25.10 ? 149 ALA A C 1 ATOM 1135 O O . ALA A 1 149 ? 18.322 16.560 45.609 1.00 24.67 ? 149 ALA A O 1 ATOM 1136 C CB . ALA A 1 149 ? 20.871 18.188 44.679 1.00 24.52 ? 149 ALA A CB 1 ATOM 1137 N N . VAL A 1 150 ? 20.103 15.859 46.819 1.00 25.51 ? 150 VAL A N 1 ATOM 1138 C CA . VAL A 1 150 ? 19.389 15.678 48.068 1.00 26.16 ? 150 VAL A CA 1 ATOM 1139 C C . VAL A 1 150 ? 19.935 16.775 49.000 1.00 26.77 ? 150 VAL A C 1 ATOM 1140 O O . VAL A 1 150 ? 20.995 16.607 49.604 1.00 27.43 ? 150 VAL A O 1 ATOM 1141 C CB . VAL A 1 150 ? 19.631 14.258 48.655 1.00 27.16 ? 150 VAL A CB 1 ATOM 1142 C CG1 . VAL A 1 150 ? 18.825 14.044 49.922 1.00 26.95 ? 150 VAL A CG1 1 ATOM 1143 C CG2 . VAL A 1 150 ? 19.309 13.178 47.616 1.00 25.49 ? 150 VAL A CG2 1 ATOM 1144 N N . CYS A 1 151 ? 19.225 17.902 49.074 1.00 26.60 ? 151 CYS A N 1 ATOM 1145 C CA . CYS A 1 151 ? 19.646 19.032 49.906 1.00 27.03 ? 151 CYS A CA 1 ATOM 1146 C C . CYS A 1 151 ? 19.530 18.688 51.389 1.00 28.07 ? 151 CYS A C 1 ATOM 1147 O O . CYS A 1 151 ? 18.423 18.477 51.931 1.00 28.44 ? 151 CYS A O 1 ATOM 1148 C CB . CYS A 1 151 ? 18.864 20.312 49.557 1.00 26.74 ? 151 CYS A CB 1 ATOM 1149 S SG . CYS A 1 151 ? 19.220 21.727 50.667 1.00 27.30 ? 151 CYS A SG 1 ATOM 1150 N N . ARG A 1 152 ? 20.692 18.623 52.035 1.00 28.46 ? 152 ARG A N 1 ATOM 1151 C CA . ARG A 1 152 ? 20.808 18.213 53.430 1.00 29.96 ? 152 ARG A CA 1 ATOM 1152 C C . ARG A 1 152 ? 21.001 19.408 54.362 1.00 29.99 ? 152 ARG A C 1 ATOM 1153 O O . ARG A 1 152 ? 21.115 19.230 55.572 1.00 31.25 ? 152 ARG A O 1 ATOM 1154 C CB . ARG A 1 152 ? 21.986 17.238 53.572 1.00 31.12 ? 152 ARG A CB 1 ATOM 1155 C CG . ARG A 1 152 ? 21.787 15.919 52.834 1.00 31.81 ? 152 ARG A CG 1 ATOM 1156 C CD . ARG A 1 152 ? 21.645 14.813 53.822 1.00 38.67 ? 152 ARG A CD 1 ATOM 1157 N NE . ARG A 1 152 ? 20.283 14.373 53.990 1.00 39.27 ? 152 ARG A NE 1 ATOM 1158 C CZ . ARG A 1 152 ? 19.823 13.677 55.024 1.00 38.32 ? 152 ARG A CZ 1 ATOM 1159 N NH1 . ARG A 1 152 ? 20.592 13.337 56.056 1.00 42.15 ? 152 ARG A NH1 1 ATOM 1160 N NH2 . ARG A 1 152 ? 18.552 13.338 55.027 1.00 38.57 ? 152 ARG A NH2 1 ATOM 1161 N N . ASP A 1 153 ? 21.021 20.618 53.793 1.00 28.86 ? 153 ASP A N 1 ATOM 1162 C CA . ASP A 1 153 ? 21.226 21.859 54.556 1.00 28.88 ? 153 ASP A CA 1 ATOM 1163 C C . ASP A 1 153 ? 20.606 23.047 53.791 1.00 27.50 ? 153 ASP A C 1 ATOM 1164 O O . ASP A 1 153 ? 21.131 23.445 52.734 1.00 27.14 ? 153 ASP A O 1 ATOM 1165 C CB . ASP A 1 153 ? 22.730 22.081 54.796 1.00 29.93 ? 153 ASP A CB 1 ATOM 1166 C CG . ASP A 1 153 ? 23.021 23.125 55.860 1.00 31.21 ? 153 ASP A CG 1 ATOM 1167 O OD1 . ASP A 1 153 ? 24.017 22.970 56.600 1.00 33.40 ? 153 ASP A OD1 1 ATOM 1168 O OD2 . ASP A 1 153 ? 22.266 24.110 55.964 1.00 31.10 ? 153 ASP A OD2 1 ATOM 1169 N N . PRO A 1 154 ? 19.500 23.626 54.320 1.00 26.88 ? 154 PRO A N 1 ATOM 1170 C CA . PRO A 1 154 ? 18.744 24.660 53.571 1.00 26.19 ? 154 PRO A CA 1 ATOM 1171 C C . PRO A 1 154 ? 19.499 25.987 53.375 1.00 26.15 ? 154 PRO A C 1 ATOM 1172 O O . PRO A 1 154 ? 19.016 26.858 52.672 1.00 25.20 ? 154 PRO A O 1 ATOM 1173 C CB . PRO A 1 154 ? 17.481 24.870 54.416 1.00 25.80 ? 154 PRO A CB 1 ATOM 1174 C CG . PRO A 1 154 ? 17.894 24.468 55.814 1.00 27.54 ? 154 PRO A CG 1 ATOM 1175 C CD . PRO A 1 154 ? 18.908 23.364 55.647 1.00 27.59 ? 154 PRO A CD 1 ATOM 1176 N N . ARG A 1 155 ? 20.672 26.135 53.995 1.00 26.97 ? 155 ARG A N 1 ATOM 1177 C CA . ARG A 1 155 ? 21.513 27.301 53.754 1.00 26.88 ? 155 ARG A CA 1 ATOM 1178 C C . ARG A 1 155 ? 22.098 27.302 52.324 1.00 26.94 ? 155 ARG A C 1 ATOM 1179 O O . ARG A 1 155 ? 22.664 28.305 51.867 1.00 27.33 ? 155 ARG A O 1 ATOM 1180 C CB . ARG A 1 155 ? 22.609 27.389 54.823 1.00 27.80 ? 155 ARG A CB 1 ATOM 1181 C CG . ARG A 1 155 ? 22.050 27.650 56.227 1.00 27.45 ? 155 ARG A CG 1 ATOM 1182 C CD . ARG A 1 155 ? 23.141 27.649 57.313 1.00 30.82 ? 155 ARG A CD 1 ATOM 1183 N NE . ARG A 1 155 ? 23.672 26.305 57.545 1.00 30.47 ? 155 ARG A NE 1 ATOM 1184 C CZ . ARG A 1 155 ? 24.578 25.994 58.462 1.00 31.82 ? 155 ARG A CZ 1 ATOM 1185 N NH1 . ARG A 1 155 ? 25.071 26.926 59.261 1.00 34.09 ? 155 ARG A NH1 1 ATOM 1186 N NH2 . ARG A 1 155 ? 24.981 24.737 58.582 1.00 32.99 ? 155 ARG A NH2 1 ATOM 1187 N N . TRP A 1 156 ? 21.964 26.173 51.633 1.00 26.41 ? 156 TRP A N 1 ATOM 1188 C CA . TRP A 1 156 ? 22.395 26.041 50.248 1.00 26.28 ? 156 TRP A CA 1 ATOM 1189 C C . TRP A 1 156 ? 21.479 26.826 49.313 1.00 25.78 ? 156 TRP A C 1 ATOM 1190 O O . TRP A 1 156 ? 20.254 26.698 49.380 1.00 25.73 ? 156 TRP A O 1 ATOM 1191 C CB . TRP A 1 156 ? 22.430 24.560 49.865 1.00 25.63 ? 156 TRP A CB 1 ATOM 1192 C CG . TRP A 1 156 ? 23.068 24.233 48.524 1.00 25.42 ? 156 TRP A CG 1 ATOM 1193 C CD1 . TRP A 1 156 ? 24.163 24.838 47.944 1.00 25.32 ? 156 TRP A CD1 1 ATOM 1194 C CD2 . TRP A 1 156 ? 22.682 23.172 47.639 1.00 24.41 ? 156 TRP A CD2 1 ATOM 1195 N NE1 . TRP A 1 156 ? 24.457 24.228 46.745 1.00 24.20 ? 156 TRP A NE1 1 ATOM 1196 C CE2 . TRP A 1 156 ? 23.570 23.201 46.533 1.00 24.86 ? 156 TRP A CE2 1 ATOM 1197 C CE3 . TRP A 1 156 ? 21.656 22.211 47.662 1.00 24.85 ? 156 TRP A CE3 1 ATOM 1198 C CZ2 . TRP A 1 156 ? 23.456 22.308 45.449 1.00 23.55 ? 156 TRP A CZ2 1 ATOM 1199 C CZ3 . TRP A 1 156 ? 21.545 21.317 46.585 1.00 23.71 ? 156 TRP A CZ3 1 ATOM 1200 C CH2 . TRP A 1 156 ? 22.442 21.377 45.496 1.00 23.53 ? 156 TRP A CH2 1 ATOM 1201 N N . GLY A 1 157 ? 22.078 27.626 48.432 1.00 26.04 ? 157 GLY A N 1 ATOM 1202 C CA . GLY A 1 157 ? 21.320 28.441 47.483 1.00 25.67 ? 157 GLY A CA 1 ATOM 1203 C C . GLY A 1 157 ? 20.561 27.663 46.430 1.00 24.83 ? 157 GLY A C 1 ATOM 1204 O O . GLY A 1 157 ? 19.743 28.235 45.705 1.00 25.36 ? 157 GLY A O 1 ATOM 1205 N N . ARG A 1 158 ? 20.827 26.360 46.329 1.00 24.85 ? 158 ARG A N 1 ATOM 1206 C CA . ARG A 1 158 ? 20.126 25.507 45.369 1.00 23.98 ? 158 ARG A CA 1 ATOM 1207 C C . ARG A 1 158 ? 19.208 24.508 46.055 1.00 24.70 ? 158 ARG A C 1 ATOM 1208 O O . ARG A 1 158 ? 18.746 23.551 45.437 1.00 24.99 ? 158 ARG A O 1 ATOM 1209 C CB . ARG A 1 158 ? 21.124 24.774 44.467 1.00 24.20 ? 158 ARG A CB 1 ATOM 1210 C CG . ARG A 1 158 ? 22.282 25.628 43.966 1.00 22.89 ? 158 ARG A CG 1 ATOM 1211 C CD . ARG A 1 158 ? 23.042 24.913 42.849 1.00 23.66 ? 158 ARG A CD 1 ATOM 1212 N NE . ARG A 1 158 ? 22.281 24.906 41.602 1.00 21.65 ? 158 ARG A NE 1 ATOM 1213 C CZ . ARG A 1 158 ? 22.785 24.619 40.399 1.00 22.73 ? 158 ARG A CZ 1 ATOM 1214 N NH1 . ARG A 1 158 ? 21.993 24.657 39.328 1.00 19.94 ? 158 ARG A NH1 1 ATOM 1215 N NH2 . ARG A 1 158 ? 24.075 24.305 40.265 1.00 22.18 ? 158 ARG A NH2 1 ATOM 1216 N N . CYS A 1 159 ? 18.943 24.713 47.341 1.00 25.69 ? 159 CYS A N 1 ATOM 1217 C CA . CYS A 1 159 ? 18.032 23.827 48.062 1.00 25.55 ? 159 CYS A CA 1 ATOM 1218 C C . CYS A 1 159 ? 16.651 23.713 47.375 1.00 24.99 ? 159 CYS A C 1 ATOM 1219 O O . CYS A 1 159 ? 16.049 22.631 47.345 1.00 24.51 ? 159 CYS A O 1 ATOM 1220 C CB . CYS A 1 159 ? 17.904 24.253 49.523 1.00 26.41 ? 159 CYS A CB 1 ATOM 1221 S SG . CYS A 1 159 ? 17.464 22.887 50.593 1.00 28.50 ? 159 CYS A SG 1 ATOM 1222 N N . TYR A 1 160 ? 16.174 24.806 46.781 1.00 24.30 ? 160 TYR A N 1 ATOM 1223 C CA . TYR A 1 160 ? 14.890 24.760 46.065 1.00 23.69 ? 160 TYR A CA 1 ATOM 1224 C C . TYR A 1 160 ? 14.889 23.854 44.825 1.00 23.17 ? 160 TYR A C 1 ATOM 1225 O O . TYR A 1 160 ? 13.822 23.418 44.383 1.00 23.28 ? 160 TYR A O 1 ATOM 1226 C CB . TYR A 1 160 ? 14.370 26.174 45.733 1.00 22.98 ? 160 TYR A CB 1 ATOM 1227 C CG . TYR A 1 160 ? 15.116 26.944 44.655 1.00 22.54 ? 160 TYR A CG 1 ATOM 1228 C CD1 . TYR A 1 160 ? 14.885 26.696 43.298 1.00 21.99 ? 160 TYR A CD1 1 ATOM 1229 C CD2 . TYR A 1 160 ? 16.012 27.951 44.993 1.00 22.35 ? 160 TYR A CD2 1 ATOM 1230 C CE1 . TYR A 1 160 ? 15.539 27.436 42.310 1.00 21.25 ? 160 TYR A CE1 1 ATOM 1231 C CE2 . TYR A 1 160 ? 16.672 28.681 44.024 1.00 21.75 ? 160 TYR A CE2 1 ATOM 1232 C CZ . TYR A 1 160 ? 16.432 28.418 42.681 1.00 21.81 ? 160 TYR A CZ 1 ATOM 1233 O OH . TYR A 1 160 ? 17.084 29.154 41.717 1.00 20.86 ? 160 TYR A OH 1 ATOM 1234 N N . GLU A 1 161 ? 16.076 23.580 44.273 1.00 22.53 ? 161 GLU A N 1 ATOM 1235 C CA . GLU A 1 161 ? 16.211 22.691 43.135 1.00 22.48 ? 161 GLU A CA 1 ATOM 1236 C C . GLU A 1 161 ? 16.252 21.221 43.543 1.00 23.00 ? 161 GLU A C 1 ATOM 1237 O O . GLU A 1 161 ? 16.372 20.337 42.691 1.00 22.93 ? 161 GLU A O 1 ATOM 1238 C CB . GLU A 1 161 ? 17.469 23.039 42.314 1.00 22.92 ? 161 GLU A CB 1 ATOM 1239 C CG . GLU A 1 161 ? 17.522 24.481 41.856 1.00 22.10 ? 161 GLU A CG 1 ATOM 1240 C CD . GLU A 1 161 ? 18.513 24.695 40.753 1.00 25.16 ? 161 GLU A CD 1 ATOM 1241 O OE1 . GLU A 1 161 ? 18.337 24.076 39.668 1.00 24.78 ? 161 GLU A OE1 1 ATOM 1242 O OE2 . GLU A 1 161 ? 19.447 25.490 40.975 1.00 25.33 ? 161 GLU A OE2 1 ATOM 1243 N N . SER A 1 162 ? 16.146 20.965 44.841 1.00 23.07 ? 162 SER A N 1 ATOM 1244 C CA . SER A 1 162 ? 16.093 19.609 45.361 1.00 23.72 ? 162 SER A CA 1 ATOM 1245 C C . SER A 1 162 ? 14.665 19.274 45.805 1.00 23.79 ? 162 SER A C 1 ATOM 1246 O O . SER A 1 162 ? 14.036 20.051 46.532 1.00 24.22 ? 162 SER A O 1 ATOM 1247 C CB . SER A 1 162 ? 17.093 19.456 46.515 1.00 24.03 ? 162 SER A CB 1 ATOM 1248 O OG . SER A 1 162 ? 16.850 18.275 47.279 1.00 24.53 ? 162 SER A OG 1 ATOM 1249 N N . TYR A 1 163 ? 14.150 18.130 45.357 1.00 23.85 ? 163 TYR A N 1 ATOM 1250 C CA . TYR A 1 163 ? 12.798 17.702 45.737 1.00 24.14 ? 163 TYR A CA 1 ATOM 1251 C C . TYR A 1 163 ? 12.650 17.463 47.235 1.00 25.13 ? 163 TYR A C 1 ATOM 1252 O O . TYR A 1 163 ? 11.564 17.653 47.790 1.00 25.61 ? 163 TYR A O 1 ATOM 1253 C CB . TYR A 1 163 ? 12.397 16.417 45.012 1.00 23.96 ? 163 TYR A CB 1 ATOM 1254 C CG . TYR A 1 163 ? 12.422 16.491 43.504 1.00 23.53 ? 163 TYR A CG 1 ATOM 1255 C CD1 . TYR A 1 163 ? 13.426 15.841 42.775 1.00 22.59 ? 163 TYR A CD1 1 ATOM 1256 C CD2 . TYR A 1 163 ? 11.420 17.169 42.802 1.00 20.82 ? 163 TYR A CD2 1 ATOM 1257 C CE1 . TYR A 1 163 ? 13.445 15.885 41.395 1.00 22.96 ? 163 TYR A CE1 1 ATOM 1258 C CE2 . TYR A 1 163 ? 11.419 17.206 41.421 1.00 22.31 ? 163 TYR A CE2 1 ATOM 1259 C CZ . TYR A 1 163 ? 12.442 16.573 40.717 1.00 22.84 ? 163 TYR A CZ 1 ATOM 1260 O OH . TYR A 1 163 ? 12.456 16.631 39.343 1.00 21.57 ? 163 TYR A OH 1 ATOM 1261 N N . SER A 1 164 ? 13.721 17.018 47.894 1.00 26.30 ? 164 SER A N 1 ATOM 1262 C CA . SER A 1 164 ? 13.640 16.655 49.319 1.00 26.93 ? 164 SER A CA 1 ATOM 1263 C C . SER A 1 164 ? 15.001 16.456 49.954 1.00 28.13 ? 164 SER A C 1 ATOM 1264 O O . SER A 1 164 ? 15.985 16.197 49.253 1.00 28.80 ? 164 SER A O 1 ATOM 1265 C CB . SER A 1 164 ? 12.857 15.358 49.478 1.00 27.45 ? 164 SER A CB 1 ATOM 1266 O OG . SER A 1 164 ? 12.577 15.094 50.839 1.00 27.75 ? 164 SER A OG 1 ATOM 1267 N N . GLU A 1 165 ? 15.044 16.564 51.281 1.00 28.66 ? 165 GLU A N 1 ATOM 1268 C CA . GLU A 1 165 ? 16.183 16.109 52.077 1.00 29.72 ? 165 GLU A CA 1 ATOM 1269 C C . GLU A 1 165 ? 16.170 14.575 52.216 1.00 30.50 ? 165 GLU A C 1 ATOM 1270 O O . GLU A 1 165 ? 17.142 13.976 52.686 1.00 31.79 ? 165 GLU A O 1 ATOM 1271 C CB . GLU A 1 165 ? 16.162 16.761 53.474 1.00 30.20 ? 165 GLU A CB 1 ATOM 1272 C CG . GLU A 1 165 ? 15.092 16.191 54.392 1.00 30.72 ? 165 GLU A CG 1 ATOM 1273 C CD . GLU A 1 165 ? 14.950 16.948 55.688 1.00 32.85 ? 165 GLU A CD 1 ATOM 1274 O OE1 . GLU A 1 165 ? 14.577 16.324 56.703 1.00 34.26 ? 165 GLU A OE1 1 ATOM 1275 O OE2 . GLU A 1 165 ? 15.196 18.172 55.697 1.00 34.89 ? 165 GLU A OE2 1 ATOM 1276 N N . ASP A 1 166 ? 15.061 13.959 51.811 1.00 30.22 ? 166 ASP A N 1 ATOM 1277 C CA . ASP A 1 166 ? 14.877 12.516 51.878 1.00 31.04 ? 166 ASP A CA 1 ATOM 1278 C C . ASP A 1 166 ? 15.085 11.922 50.486 1.00 30.15 ? 166 ASP A C 1 ATOM 1279 O O . ASP A 1 166 ? 14.293 12.163 49.575 1.00 28.60 ? 166 ASP A O 1 ATOM 1280 C CB . ASP A 1 166 ? 13.468 12.209 52.390 1.00 31.70 ? 166 ASP A CB 1 ATOM 1281 C CG . ASP A 1 166 ? 13.219 10.727 52.617 1.00 33.69 ? 166 ASP A CG 1 ATOM 1282 O OD1 . ASP A 1 166 ? 13.946 9.859 52.075 1.00 33.05 ? 166 ASP A OD1 1 ATOM 1283 O OD2 . ASP A 1 166 ? 12.257 10.431 53.349 1.00 37.46 ? 166 ASP A OD2 1 ATOM 1284 N N . ARG A 1 167 ? 16.155 11.142 50.344 1.00 30.67 ? 167 ARG A N 1 ATOM 1285 C CA . ARG A 1 167 ? 16.511 10.476 49.085 1.00 30.67 ? 167 ARG A CA 1 ATOM 1286 C C . ARG A 1 167 ? 15.364 9.678 48.461 1.00 30.63 ? 167 ARG A C 1 ATOM 1287 O O . ARG A 1 167 ? 15.259 9.593 47.240 1.00 30.30 ? 167 ARG A O 1 ATOM 1288 C CB . ARG A 1 167 ? 17.748 9.584 49.273 1.00 31.45 ? 167 ARG A CB 1 ATOM 1289 C CG . ARG A 1 167 ? 17.581 8.467 50.283 1.00 35.20 ? 167 ARG A CG 1 ATOM 1290 C CD . ARG A 1 167 ? 17.206 7.131 49.643 1.00 37.89 ? 167 ARG A CD 1 ATOM 1291 N NE . ARG A 1 167 ? 17.102 6.086 50.661 1.00 43.17 ? 167 ARG A NE 1 ATOM 1292 C CZ . ARG A 1 167 ? 16.670 4.844 50.446 1.00 45.48 ? 167 ARG A CZ 1 ATOM 1293 N NH1 . ARG A 1 167 ? 16.297 4.461 49.232 1.00 45.26 ? 167 ARG A NH1 1 ATOM 1294 N NH2 . ARG A 1 167 ? 16.615 3.978 51.453 1.00 47.15 ? 167 ARG A NH2 1 ATOM 1295 N N . ARG A 1 168 ? 14.509 9.093 49.298 1.00 31.91 ? 168 ARG A N 1 ATOM 1296 C CA . ARG A 1 168 ? 13.373 8.309 48.808 1.00 32.58 ? 168 ARG A CA 1 ATOM 1297 C C . ARG A 1 168 ? 12.383 9.167 48.026 1.00 30.96 ? 168 ARG A C 1 ATOM 1298 O O . ARG A 1 168 ? 11.764 8.693 47.064 1.00 30.64 ? 168 ARG A O 1 ATOM 1299 C CB . ARG A 1 168 ? 12.652 7.636 49.961 1.00 33.85 ? 168 ARG A CB 1 ATOM 1300 C CG . ARG A 1 168 ? 13.389 6.440 50.511 1.00 38.78 ? 168 ARG A CG 1 ATOM 1301 C CD . ARG A 1 168 ? 12.560 5.788 51.582 1.00 45.32 ? 168 ARG A CD 1 ATOM 1302 N NE . ARG A 1 168 ? 13.167 4.559 52.084 1.00 52.92 ? 168 ARG A NE 1 ATOM 1303 C CZ . ARG A 1 168 ? 13.897 4.488 53.197 1.00 57.51 ? 168 ARG A CZ 1 ATOM 1304 N NH1 . ARG A 1 168 ? 14.133 5.591 53.912 1.00 58.37 ? 168 ARG A NH1 1 ATOM 1305 N NH2 . ARG A 1 168 ? 14.393 3.317 53.595 1.00 59.81 ? 168 ARG A NH2 1 ATOM 1306 N N . ILE A 1 169 ? 12.216 10.418 48.458 1.00 29.66 ? 169 ILE A N 1 ATOM 1307 C CA . ILE A 1 169 ? 11.337 11.340 47.747 1.00 28.45 ? 169 ILE A CA 1 ATOM 1308 C C . ILE A 1 169 ? 12.019 11.782 46.453 1.00 27.21 ? 169 ILE A C 1 ATOM 1309 O O . ILE A 1 169 ? 11.385 11.831 45.396 1.00 26.90 ? 169 ILE A O 1 ATOM 1310 C CB . ILE A 1 169 ? 10.880 12.537 48.630 1.00 28.51 ? 169 ILE A CB 1 ATOM 1311 C CG1 . ILE A 1 169 ? 10.025 12.025 49.795 1.00 28.98 ? 169 ILE A CG1 1 ATOM 1312 C CG2 . ILE A 1 169 ? 10.114 13.577 47.778 1.00 26.02 ? 169 ILE A CG2 1 ATOM 1313 C CD1 . ILE A 1 169 ? 9.847 12.997 50.954 1.00 29.86 ? 169 ILE A CD1 1 ATOM 1314 N N . VAL A 1 170 ? 13.313 12.084 46.526 1.00 26.76 ? 170 VAL A N 1 ATOM 1315 C CA . VAL A 1 170 ? 14.073 12.412 45.318 1.00 26.15 ? 170 VAL A CA 1 ATOM 1316 C C . VAL A 1 170 ? 14.003 11.263 44.310 1.00 26.43 ? 170 VAL A C 1 ATOM 1317 O O . VAL A 1 170 ? 13.731 11.487 43.135 1.00 26.03 ? 170 VAL A O 1 ATOM 1318 C CB . VAL A 1 170 ? 15.543 12.797 45.626 1.00 26.39 ? 170 VAL A CB 1 ATOM 1319 C CG1 . VAL A 1 170 ? 16.335 13.055 44.323 1.00 24.37 ? 170 VAL A CG1 1 ATOM 1320 C CG2 . VAL A 1 170 ? 15.587 14.026 46.553 1.00 25.91 ? 170 VAL A CG2 1 ATOM 1321 N N . GLN A 1 171 ? 14.247 10.040 44.780 1.00 27.69 ? 171 GLN A N 1 ATOM 1322 C CA . GLN A 1 171 ? 14.084 8.826 43.958 1.00 28.31 ? 171 GLN A CA 1 ATOM 1323 C C . GLN A 1 171 ? 12.738 8.752 43.227 1.00 28.55 ? 171 GLN A C 1 ATOM 1324 O O . GLN A 1 171 ? 12.695 8.494 42.026 1.00 28.50 ? 171 GLN A O 1 ATOM 1325 C CB . GLN A 1 171 ? 14.260 7.572 44.821 1.00 29.22 ? 171 GLN A CB 1 ATOM 1326 C CG . GLN A 1 171 ? 15.716 7.210 45.081 1.00 29.21 ? 171 GLN A CG 1 ATOM 1327 C CD . GLN A 1 171 ? 15.860 5.946 45.901 1.00 31.34 ? 171 GLN A CD 1 ATOM 1328 O OE1 . GLN A 1 171 ? 16.299 4.905 45.400 1.00 33.19 ? 171 GLN A OE1 1 ATOM 1329 N NE2 . GLN A 1 171 ? 15.479 6.023 47.154 1.00 29.61 ? 171 GLN A NE2 1 ATOM 1330 N N . SER A 1 172 ? 11.642 8.982 43.953 1.00 28.98 ? 172 SER A N 1 ATOM 1331 C CA . SER A 1 172 ? 10.304 8.927 43.366 1.00 29.05 ? 172 SER A CA 1 ATOM 1332 C C . SER A 1 172 ? 10.107 9.965 42.270 1.00 27.84 ? 172 SER A C 1 ATOM 1333 O O . SER A 1 172 ? 9.392 9.715 41.295 1.00 27.22 ? 172 SER A O 1 ATOM 1334 C CB . SER A 1 172 ? 9.226 9.102 44.444 1.00 29.76 ? 172 SER A CB 1 ATOM 1335 O OG . SER A 1 172 ? 9.264 10.407 44.993 1.00 29.08 ? 172 SER A OG 1 ATOM 1336 N N . MET A 1 173 ? 10.735 11.127 42.447 1.00 26.62 ? 173 MET A N 1 ATOM 1337 C CA . MET A 1 173 ? 10.578 12.243 41.520 1.00 26.21 ? 173 MET A CA 1 ATOM 1338 C C . MET A 1 173 ? 11.430 12.124 40.243 1.00 25.18 ? 173 MET A C 1 ATOM 1339 O O . MET A 1 173 ? 11.325 12.974 39.350 1.00 23.94 ? 173 MET A O 1 ATOM 1340 C CB . MET A 1 173 ? 10.825 13.589 42.225 1.00 25.46 ? 173 MET A CB 1 ATOM 1341 C CG . MET A 1 173 ? 9.892 13.885 43.412 1.00 28.79 ? 173 MET A CG 1 ATOM 1342 S SD . MET A 1 173 ? 8.172 13.759 42.927 1.00 33.71 ? 173 MET A SD 1 ATOM 1343 C CE . MET A 1 173 ? 7.312 13.962 44.488 1.00 30.50 ? 173 MET A CE 1 ATOM 1344 N N . THR A 1 174 ? 12.250 11.074 40.151 1.00 25.60 ? 174 THR A N 1 ATOM 1345 C CA . THR A 1 174 ? 12.959 10.760 38.902 1.00 24.73 ? 174 THR A CA 1 ATOM 1346 C C . THR A 1 174 ? 11.989 10.464 37.737 1.00 25.22 ? 174 THR A C 1 ATOM 1347 O O . THR A 1 174 ? 12.424 10.273 36.595 1.00 23.67 ? 174 THR A O 1 ATOM 1348 C CB . THR A 1 174 ? 13.980 9.590 39.059 1.00 25.41 ? 174 THR A CB 1 ATOM 1349 O OG1 . THR A 1 174 ? 13.323 8.404 39.540 1.00 25.69 ? 174 THR A OG1 1 ATOM 1350 C CG2 . THR A 1 174 ? 15.097 9.976 40.010 1.00 25.21 ? 174 THR A CG2 1 ATOM 1351 N N . GLU A 1 175 ? 10.684 10.425 38.039 1.00 25.75 ? 175 GLU A N 1 ATOM 1352 C CA . GLU A 1 175 ? 9.636 10.304 37.014 1.00 25.94 ? 175 GLU A CA 1 ATOM 1353 C C . GLU A 1 175 ? 9.628 11.493 36.037 1.00 24.92 ? 175 GLU A C 1 ATOM 1354 O O . GLU A 1 175 ? 9.001 11.419 34.985 1.00 25.25 ? 175 GLU A O 1 ATOM 1355 C CB . GLU A 1 175 ? 8.255 10.135 37.642 1.00 26.50 ? 175 GLU A CB 1 ATOM 1356 C CG . GLU A 1 175 ? 7.957 8.743 38.163 1.00 28.76 ? 175 GLU A CG 1 ATOM 1357 C CD . GLU A 1 175 ? 7.995 7.698 37.063 1.00 31.10 ? 175 GLU A CD 1 ATOM 1358 O OE1 . GLU A 1 175 ? 9.019 7.000 36.951 1.00 32.07 ? 175 GLU A OE1 1 ATOM 1359 O OE2 . GLU A 1 175 ? 7.012 7.584 36.304 1.00 31.26 ? 175 GLU A OE2 1 ATOM 1360 N N . LEU A 1 176 ? 10.322 12.576 36.385 1.00 23.74 ? 176 LEU A N 1 ATOM 1361 C CA . LEU A 1 176 ? 10.530 13.683 35.444 1.00 22.72 ? 176 LEU A CA 1 ATOM 1362 C C . LEU A 1 176 ? 11.238 13.185 34.181 1.00 22.73 ? 176 LEU A C 1 ATOM 1363 O O . LEU A 1 176 ? 10.962 13.668 33.066 1.00 22.39 ? 176 LEU A O 1 ATOM 1364 C CB . LEU A 1 176 ? 11.360 14.808 36.074 1.00 22.12 ? 176 LEU A CB 1 ATOM 1365 C CG . LEU A 1 176 ? 11.362 16.094 35.227 1.00 21.05 ? 176 LEU A CG 1 ATOM 1366 C CD1 . LEU A 1 176 ? 10.106 16.943 35.489 1.00 19.67 ? 176 LEU A CD1 1 ATOM 1367 C CD2 . LEU A 1 176 ? 12.615 16.918 35.453 1.00 21.59 ? 176 LEU A CD2 1 ATOM 1368 N N . ILE A 1 177 ? 12.127 12.203 34.364 1.00 23.03 ? 177 ILE A N 1 ATOM 1369 C CA . ILE A 1 177 ? 12.942 11.661 33.277 1.00 22.42 ? 177 ILE A CA 1 ATOM 1370 C C . ILE A 1 177 ? 12.100 11.054 32.145 1.00 23.11 ? 177 ILE A C 1 ATOM 1371 O O . ILE A 1 177 ? 12.190 11.552 31.027 1.00 23.47 ? 177 ILE A O 1 ATOM 1372 C CB . ILE A 1 177 ? 14.090 10.742 33.816 1.00 23.30 ? 177 ILE A CB 1 ATOM 1373 C CG1 . ILE A 1 177 ? 15.110 11.609 34.585 1.00 21.85 ? 177 ILE A CG1 1 ATOM 1374 C CG2 . ILE A 1 177 ? 14.761 9.949 32.678 1.00 21.79 ? 177 ILE A CG2 1 ATOM 1375 C CD1 . ILE A 1 177 ? 15.991 10.859 35.598 1.00 22.36 ? 177 ILE A CD1 1 ATOM 1376 N N . PRO A 1 178 ? 11.278 9.997 32.416 1.00 23.68 ? 178 PRO A N 1 ATOM 1377 C CA . PRO A 1 178 ? 10.430 9.486 31.325 1.00 24.33 ? 178 PRO A CA 1 ATOM 1378 C C . PRO A 1 178 ? 9.340 10.469 30.866 1.00 24.18 ? 178 PRO A C 1 ATOM 1379 O O . PRO A 1 178 ? 8.784 10.299 29.784 1.00 26.24 ? 178 PRO A O 1 ATOM 1380 C CB . PRO A 1 178 ? 9.807 8.204 31.915 1.00 25.63 ? 178 PRO A CB 1 ATOM 1381 C CG . PRO A 1 178 ? 9.829 8.395 33.387 1.00 24.81 ? 178 PRO A CG 1 ATOM 1382 C CD . PRO A 1 178 ? 11.103 9.206 33.652 1.00 24.72 ? 178 PRO A CD 1 ATOM 1383 N N . GLY A 1 179 ? 9.032 11.488 31.665 1.00 23.61 ? 179 GLY A N 1 ATOM 1384 C CA . GLY A 1 179 ? 8.198 12.593 31.194 1.00 21.98 ? 179 GLY A CA 1 ATOM 1385 C C . GLY A 1 179 ? 8.895 13.393 30.100 1.00 21.57 ? 179 GLY A C 1 ATOM 1386 O O . GLY A 1 179 ? 8.338 13.590 29.007 1.00 21.37 ? 179 GLY A O 1 ATOM 1387 N N . LEU A 1 180 ? 10.120 13.842 30.392 1.00 20.38 ? 180 LEU A N 1 ATOM 1388 C CA . LEU A 1 180 ? 10.928 14.588 29.433 1.00 20.03 ? 180 LEU A CA 1 ATOM 1389 C C . LEU A 1 180 ? 11.313 13.764 28.200 1.00 20.68 ? 180 LEU A C 1 ATOM 1390 O O . LEU A 1 180 ? 11.260 14.266 27.075 1.00 20.40 ? 180 LEU A O 1 ATOM 1391 C CB . LEU A 1 180 ? 12.210 15.111 30.096 1.00 19.26 ? 180 LEU A CB 1 ATOM 1392 C CG . LEU A 1 180 ? 12.063 16.273 31.089 1.00 18.38 ? 180 LEU A CG 1 ATOM 1393 C CD1 . LEU A 1 180 ? 13.313 16.359 31.936 1.00 19.05 ? 180 LEU A CD1 1 ATOM 1394 C CD2 . LEU A 1 180 ? 11.750 17.612 30.381 1.00 17.49 ? 180 LEU A CD2 1 ATOM 1395 N N . GLN A 1 181 ? 11.698 12.506 28.418 1.00 21.19 ? 181 GLN A N 1 ATOM 1396 C CA . GLN A 1 181 ? 12.288 11.673 27.370 1.00 21.96 ? 181 GLN A CA 1 ATOM 1397 C C . GLN A 1 181 ? 11.330 10.688 26.721 1.00 23.69 ? 181 GLN A C 1 ATOM 1398 O O . GLN A 1 181 ? 11.601 10.208 25.627 1.00 24.09 ? 181 GLN A O 1 ATOM 1399 C CB . GLN A 1 181 ? 13.455 10.860 27.934 1.00 22.19 ? 181 GLN A CB 1 ATOM 1400 C CG . GLN A 1 181 ? 14.611 11.682 28.515 1.00 21.75 ? 181 GLN A CG 1 ATOM 1401 C CD . GLN A 1 181 ? 15.816 10.820 28.820 1.00 21.27 ? 181 GLN A CD 1 ATOM 1402 O OE1 . GLN A 1 181 ? 15.691 9.694 29.323 1.00 24.88 ? 181 GLN A OE1 1 ATOM 1403 N NE2 . GLN A 1 181 ? 16.976 11.330 28.528 1.00 18.73 ? 181 GLN A NE2 1 ATOM 1404 N N . GLY A 1 182 ? 10.229 10.366 27.401 1.00 24.62 ? 182 GLY A N 1 ATOM 1405 C CA . GLY A 1 182 ? 9.381 9.255 26.984 1.00 26.69 ? 182 GLY A CA 1 ATOM 1406 C C . GLY A 1 182 ? 9.699 8.014 27.802 1.00 28.03 ? 182 GLY A C 1 ATOM 1407 O O . GLY A 1 182 ? 10.810 7.857 28.309 1.00 27.02 ? 182 GLY A O 1 ATOM 1408 N N . ASP A 1 183 ? 8.707 7.145 27.951 1.00 30.22 ? 183 ASP A N 1 ATOM 1409 C CA . ASP A 1 183 ? 8.877 5.884 28.674 1.00 32.76 ? 183 ASP A CA 1 ATOM 1410 C C . ASP A 1 183 ? 9.788 4.940 27.906 1.00 33.71 ? 183 ASP A C 1 ATOM 1411 O O . ASP A 1 183 ? 9.687 4.833 26.687 1.00 34.04 ? 183 ASP A O 1 ATOM 1412 C CB . ASP A 1 183 ? 7.521 5.210 28.893 1.00 34.17 ? 183 ASP A CB 1 ATOM 1413 C CG . ASP A 1 183 ? 6.693 5.901 29.950 1.00 35.83 ? 183 ASP A CG 1 ATOM 1414 O OD1 . ASP A 1 183 ? 7.244 6.280 31.009 1.00 37.84 ? 183 ASP A OD1 1 ATOM 1415 O OD2 . ASP A 1 183 ? 5.478 6.048 29.732 1.00 39.22 ? 183 ASP A OD2 1 ATOM 1416 N N . VAL A 1 184 ? 10.685 4.268 28.619 1.00 34.97 ? 184 VAL A N 1 ATOM 1417 C CA . VAL A 1 184 ? 11.561 3.274 28.002 1.00 36.58 ? 184 VAL A CA 1 ATOM 1418 C C . VAL A 1 184 ? 10.773 2.003 27.644 1.00 39.68 ? 184 VAL A C 1 ATOM 1419 O O . VAL A 1 184 ? 9.710 1.734 28.246 1.00 40.28 ? 184 VAL A O 1 ATOM 1420 C CB . VAL A 1 184 ? 12.801 2.935 28.890 1.00 36.47 ? 184 VAL A CB 1 ATOM 1421 C CG1 . VAL A 1 184 ? 13.696 4.159 29.057 1.00 34.07 ? 184 VAL A CG1 1 ATOM 1422 C CG2 . VAL A 1 184 ? 12.392 2.343 30.259 1.00 36.65 ? 184 VAL A CG2 1 ATOM 1423 N N . PRO A 1 185 ? 11.259 1.242 26.639 1.00 41.62 ? 185 PRO A N 1 ATOM 1424 C CA . PRO A 1 185 ? 10.705 -0.065 26.293 1.00 44.24 ? 185 PRO A CA 1 ATOM 1425 C C . PRO A 1 185 ? 10.687 -1.077 27.441 1.00 46.69 ? 185 PRO A C 1 ATOM 1426 O O . PRO A 1 185 ? 11.401 -0.914 28.439 1.00 46.29 ? 185 PRO A O 1 ATOM 1427 C CB . PRO A 1 185 ? 11.639 -0.546 25.182 1.00 44.43 ? 185 PRO A CB 1 ATOM 1428 C CG . PRO A 1 185 ? 12.125 0.663 24.559 1.00 42.44 ? 185 PRO A CG 1 ATOM 1429 C CD . PRO A 1 185 ? 12.335 1.619 25.702 1.00 41.15 ? 185 PRO A CD 1 ATOM 1430 N N . LYS A 1 186 ? 9.855 -2.107 27.288 1.00 49.72 ? 186 LYS A N 1 ATOM 1431 C CA . LYS A 1 186 ? 9.762 -3.224 28.243 1.00 52.89 ? 186 LYS A CA 1 ATOM 1432 C C . LYS A 1 186 ? 11.127 -3.900 28.429 1.00 53.36 ? 186 LYS A C 1 ATOM 1433 O O . LYS A 1 186 ? 11.532 -4.221 29.548 1.00 54.23 ? 186 LYS A O 1 ATOM 1434 C CB . LYS A 1 186 ? 8.727 -4.277 27.772 1.00 55.15 ? 186 LYS A CB 1 ATOM 1435 C CG . LYS A 1 186 ? 7.440 -3.712 27.130 1.00 57.49 ? 186 LYS A CG 1 ATOM 1436 C CD . LYS A 1 186 ? 7.638 -3.380 25.638 1.00 59.61 ? 186 LYS A CD 1 ATOM 1437 C CE . LYS A 1 186 ? 7.091 -1.987 25.298 1.00 58.62 ? 186 LYS A CE 1 ATOM 1438 N NZ . LYS A 1 186 ? 7.776 -1.434 24.086 1.00 58.42 ? 186 LYS A NZ 1 ATOM 1439 N N . ASP A 1 187 ? 11.821 -4.094 27.314 1.00 53.30 ? 187 ASP A N 1 ATOM 1440 C CA . ASP A 1 187 ? 13.125 -4.762 27.257 1.00 54.06 ? 187 ASP A CA 1 ATOM 1441 C C . ASP A 1 187 ? 14.326 -3.986 27.860 1.00 51.38 ? 187 ASP A C 1 ATOM 1442 O O . ASP A 1 187 ? 15.429 -4.538 27.963 1.00 52.10 ? 187 ASP A O 1 ATOM 1443 C CB . ASP A 1 187 ? 13.441 -5.074 25.779 1.00 55.51 ? 187 ASP A CB 1 ATOM 1444 C CG . ASP A 1 187 ? 12.988 -3.946 24.831 1.00 56.82 ? 187 ASP A CG 1 ATOM 1445 O OD1 . ASP A 1 187 ? 11.764 -3.868 24.547 1.00 60.08 ? 187 ASP A OD1 1 ATOM 1446 O OD2 . ASP A 1 187 ? 13.845 -3.142 24.379 1.00 58.07 ? 187 ASP A OD2 1 ATOM 1447 N N . PHE A 1 188 ? 14.106 -2.735 28.264 1.00 47.84 ? 188 PHE A N 1 ATOM 1448 C CA . PHE A 1 188 ? 15.189 -1.748 28.429 1.00 44.26 ? 188 PHE A CA 1 ATOM 1449 C C . PHE A 1 188 ? 16.344 -2.128 29.367 1.00 43.29 ? 188 PHE A C 1 ATOM 1450 O O . PHE A 1 188 ? 16.117 -2.554 30.496 1.00 43.80 ? 188 PHE A O 1 ATOM 1451 C CB . PHE A 1 188 ? 14.608 -0.393 28.851 1.00 42.50 ? 188 PHE A CB 1 ATOM 1452 C CG . PHE A 1 188 ? 15.571 0.753 28.678 1.00 40.89 ? 188 PHE A CG 1 ATOM 1453 C CD1 . PHE A 1 188 ? 15.862 1.248 27.407 1.00 39.82 ? 188 PHE A CD1 1 ATOM 1454 C CD2 . PHE A 1 188 ? 16.196 1.327 29.781 1.00 39.40 ? 188 PHE A CD2 1 ATOM 1455 C CE1 . PHE A 1 188 ? 16.759 2.303 27.238 1.00 37.94 ? 188 PHE A CE1 1 ATOM 1456 C CE2 . PHE A 1 188 ? 17.092 2.376 29.622 1.00 37.23 ? 188 PHE A CE2 1 ATOM 1457 C CZ . PHE A 1 188 ? 17.364 2.866 28.342 1.00 37.12 ? 188 PHE A CZ 1 ATOM 1458 N N . THR A 1 189 ? 17.575 -1.937 28.894 1.00 40.88 ? 189 THR A N 1 ATOM 1459 C CA . THR A 1 189 ? 18.762 -2.150 29.721 1.00 39.74 ? 189 THR A CA 1 ATOM 1460 C C . THR A 1 189 ? 19.146 -0.905 30.540 1.00 37.31 ? 189 THR A C 1 ATOM 1461 O O . THR A 1 189 ? 19.510 0.137 29.980 1.00 35.53 ? 189 THR A O 1 ATOM 1462 C CB . THR A 1 189 ? 19.959 -2.649 28.880 1.00 40.09 ? 189 THR A CB 1 ATOM 1463 O OG1 . THR A 1 189 ? 19.620 -3.903 28.273 1.00 42.84 ? 189 THR A OG1 1 ATOM 1464 C CG2 . THR A 1 189 ? 21.204 -2.836 29.744 1.00 40.08 ? 189 THR A CG2 1 ATOM 1465 N N . SER A 1 190 ? 19.064 -1.027 31.867 1.00 36.12 ? 190 SER A N 1 ATOM 1466 C CA . SER A 1 190 ? 19.458 0.044 32.791 1.00 34.29 ? 190 SER A CA 1 ATOM 1467 C C . SER A 1 190 ? 20.814 0.658 32.407 1.00 33.16 ? 190 SER A C 1 ATOM 1468 O O . SER A 1 190 ? 21.787 -0.065 32.148 1.00 33.56 ? 190 SER A O 1 ATOM 1469 C CB . SER A 1 190 ? 19.518 -0.483 34.229 1.00 35.06 ? 190 SER A CB 1 ATOM 1470 O OG . SER A 1 190 ? 19.807 0.555 35.152 1.00 32.82 ? 190 SER A OG 1 ATOM 1471 N N . GLY A 1 191 ? 20.862 1.989 32.358 1.00 31.52 ? 191 GLY A N 1 ATOM 1472 C CA . GLY A 1 191 ? 22.087 2.711 32.009 1.00 29.92 ? 191 GLY A CA 1 ATOM 1473 C C . GLY A 1 191 ? 22.201 3.120 30.548 1.00 29.11 ? 191 GLY A C 1 ATOM 1474 O O . GLY A 1 191 ? 23.018 3.969 30.206 1.00 27.63 ? 191 GLY A O 1 ATOM 1475 N N . MET A 1 192 ? 21.383 2.526 29.687 1.00 29.18 ? 192 MET A N 1 ATOM 1476 C CA . MET A 1 192 ? 21.319 2.937 28.284 1.00 28.97 ? 192 MET A CA 1 ATOM 1477 C C . MET A 1 192 ? 20.604 4.287 28.145 1.00 27.32 ? 192 MET A C 1 ATOM 1478 O O . MET A 1 192 ? 19.690 4.577 28.913 1.00 26.91 ? 192 MET A O 1 ATOM 1479 C CB . MET A 1 192 ? 20.612 1.862 27.441 1.00 30.21 ? 192 MET A CB 1 ATOM 1480 C CG . MET A 1 192 ? 21.465 0.628 27.162 1.00 31.89 ? 192 MET A CG 1 ATOM 1481 S SD . MET A 1 192 ? 22.894 1.012 26.113 1.00 36.29 ? 192 MET A SD 1 ATOM 1482 C CE . MET A 1 192 ? 22.139 1.098 24.489 1.00 34.16 ? 192 MET A CE 1 ATOM 1483 N N . PRO A 1 193 ? 21.034 5.133 27.186 1.00 26.30 ? 193 PRO A N 1 ATOM 1484 C CA . PRO A 1 193 ? 20.298 6.399 27.012 1.00 25.11 ? 193 PRO A CA 1 ATOM 1485 C C . PRO A 1 193 ? 18.999 6.149 26.244 1.00 25.47 ? 193 PRO A C 1 ATOM 1486 O O . PRO A 1 193 ? 18.877 5.127 25.560 1.00 25.98 ? 193 PRO A O 1 ATOM 1487 C CB . PRO A 1 193 ? 21.268 7.263 26.187 1.00 24.17 ? 193 PRO A CB 1 ATOM 1488 C CG . PRO A 1 193 ? 22.064 6.279 25.399 1.00 24.74 ? 193 PRO A CG 1 ATOM 1489 C CD . PRO A 1 193 ? 22.178 5.021 26.254 1.00 26.33 ? 193 PRO A CD 1 ATOM 1490 N N . PHE A 1 194 ? 18.032 7.053 26.385 1.00 24.84 ? 194 PHE A N 1 ATOM 1491 C CA . PHE A 1 194 ? 16.754 6.947 25.675 1.00 25.73 ? 194 PHE A CA 1 ATOM 1492 C C . PHE A 1 194 ? 16.079 8.298 25.482 1.00 24.95 ? 194 PHE A C 1 ATOM 1493 O O . PHE A 1 194 ? 16.012 9.098 26.409 1.00 24.94 ? 194 PHE A O 1 ATOM 1494 C CB . PHE A 1 194 ? 15.772 6.005 26.396 1.00 26.53 ? 194 PHE A CB 1 ATOM 1495 C CG . PHE A 1 194 ? 14.471 5.824 25.660 1.00 27.37 ? 194 PHE A CG 1 ATOM 1496 C CD1 . PHE A 1 194 ? 14.369 4.892 24.629 1.00 27.62 ? 194 PHE A CD1 1 ATOM 1497 C CD2 . PHE A 1 194 ? 13.360 6.618 25.967 1.00 26.39 ? 194 PHE A CD2 1 ATOM 1498 C CE1 . PHE A 1 194 ? 13.165 4.727 23.926 1.00 30.15 ? 194 PHE A CE1 1 ATOM 1499 C CE2 . PHE A 1 194 ? 12.164 6.473 25.277 1.00 27.18 ? 194 PHE A CE2 1 ATOM 1500 C CZ . PHE A 1 194 ? 12.064 5.513 24.245 1.00 28.27 ? 194 PHE A CZ 1 ATOM 1501 N N . VAL A 1 195 ? 15.591 8.535 24.269 1.00 24.87 ? 195 VAL A N 1 ATOM 1502 C CA . VAL A 1 195 ? 14.651 9.619 23.976 1.00 24.45 ? 195 VAL A CA 1 ATOM 1503 C C . VAL A 1 195 ? 13.729 9.065 22.898 1.00 25.67 ? 195 VAL A C 1 ATOM 1504 O O . VAL A 1 195 ? 14.206 8.418 21.962 1.00 26.14 ? 195 VAL A O 1 ATOM 1505 C CB . VAL A 1 195 ? 15.347 10.911 23.467 1.00 23.27 ? 195 VAL A CB 1 ATOM 1506 C CG1 . VAL A 1 195 ? 14.322 11.997 23.175 1.00 21.86 ? 195 VAL A CG1 1 ATOM 1507 C CG2 . VAL A 1 195 ? 16.398 11.416 24.454 1.00 21.63 ? 195 VAL A CG2 1 ATOM 1508 N N . ALA A 1 196 ? 12.421 9.280 23.056 1.00 26.50 ? 196 ALA A N 1 ATOM 1509 C CA . ALA A 1 196 ? 11.409 8.650 22.199 1.00 27.88 ? 196 ALA A CA 1 ATOM 1510 C C . ALA A 1 196 ? 11.412 9.161 20.765 1.00 28.58 ? 196 ALA A C 1 ATOM 1511 O O . ALA A 1 196 ? 11.125 8.402 19.832 1.00 31.10 ? 196 ALA A O 1 ATOM 1512 C CB . ALA A 1 196 ? 10.007 8.788 22.807 1.00 27.61 ? 196 ALA A CB 1 ATOM 1513 N N . GLY A 1 197 ? 11.716 10.436 20.582 1.00 27.81 ? 197 GLY A N 1 ATOM 1514 C CA . GLY A 1 197 ? 11.710 11.020 19.248 1.00 28.28 ? 197 GLY A CA 1 ATOM 1515 C C . GLY A 1 197 ? 11.676 12.530 19.300 1.00 27.88 ? 197 GLY A C 1 ATOM 1516 O O . GLY A 1 197 ? 12.018 13.125 20.318 1.00 26.90 ? 197 GLY A O 1 ATOM 1517 N N . LYS A 1 198 ? 11.207 13.136 18.212 1.00 28.48 ? 198 LYS A N 1 ATOM 1518 C CA . LYS A 1 198 ? 11.324 14.578 17.987 1.00 28.26 ? 198 LYS A CA 1 ATOM 1519 C C . LYS A 1 198 ? 10.436 15.421 18.889 1.00 27.82 ? 198 LYS A C 1 ATOM 1520 O O . LYS A 1 198 ? 10.650 16.626 19.004 1.00 28.04 ? 198 LYS A O 1 ATOM 1521 C CB . LYS A 1 198 ? 11.078 14.928 16.513 1.00 28.72 ? 198 LYS A CB 1 ATOM 1522 C CG . LYS A 1 198 ? 9.664 14.638 16.033 1.00 30.13 ? 198 LYS A CG 1 ATOM 1523 C CD . LYS A 1 198 ? 9.478 15.076 14.601 1.00 32.02 ? 198 LYS A CD 1 ATOM 1524 C CE . LYS A 1 198 ? 8.006 15.089 14.255 1.00 34.72 ? 198 LYS A CE 1 ATOM 1525 N NZ . LYS A 1 198 ? 7.825 15.299 12.790 1.00 37.32 ? 198 LYS A NZ 1 ATOM 1526 N N . ASN A 1 199 ? 9.453 14.797 19.531 1.00 27.88 ? 199 ASN A N 1 ATOM 1527 C CA . ASN A 1 199 ? 8.581 15.519 20.457 1.00 27.48 ? 199 ASN A CA 1 ATOM 1528 C C . ASN A 1 199 ? 9.029 15.435 21.927 1.00 26.33 ? 199 ASN A C 1 ATOM 1529 O O . ASN A 1 199 ? 8.366 15.965 22.826 1.00 25.92 ? 199 ASN A O 1 ATOM 1530 C CB . ASN A 1 199 ? 7.129 15.075 20.281 1.00 28.56 ? 199 ASN A CB 1 ATOM 1531 C CG . ASN A 1 199 ? 6.591 15.383 18.887 1.00 31.34 ? 199 ASN A CG 1 ATOM 1532 O OD1 . ASN A 1 199 ? 5.994 14.521 18.247 1.00 33.84 ? 199 ASN A OD1 1 ATOM 1533 N ND2 . ASN A 1 199 ? 6.826 16.604 18.402 1.00 32.24 ? 199 ASN A ND2 1 ATOM 1534 N N . LYS A 1 200 ? 10.177 14.790 22.144 1.00 25.43 ? 200 LYS A N 1 ATOM 1535 C CA . LYS A 1 200 ? 10.776 14.621 23.471 1.00 23.77 ? 200 LYS A CA 1 ATOM 1536 C C . LYS A 1 200 ? 12.180 15.231 23.461 1.00 22.93 ? 200 LYS A C 1 ATOM 1537 O O . LYS A 1 200 ? 12.725 15.557 22.393 1.00 22.70 ? 200 LYS A O 1 ATOM 1538 C CB . LYS A 1 200 ? 10.816 13.134 23.875 1.00 23.96 ? 200 LYS A CB 1 ATOM 1539 C CG . LYS A 1 200 ? 9.428 12.457 24.041 1.00 24.79 ? 200 LYS A CG 1 ATOM 1540 C CD . LYS A 1 200 ? 8.701 13.026 25.261 1.00 23.55 ? 200 LYS A CD 1 ATOM 1541 C CE . LYS A 1 200 ? 7.353 12.355 25.499 1.00 25.09 ? 200 LYS A CE 1 ATOM 1542 N NZ . LYS A 1 200 ? 6.803 12.798 26.816 1.00 23.40 ? 200 LYS A NZ 1 ATOM 1543 N N . VAL A 1 201 ? 12.759 15.405 24.644 1.00 21.66 ? 201 VAL A N 1 ATOM 1544 C CA . VAL A 1 201 ? 14.107 15.965 24.778 1.00 20.59 ? 201 VAL A CA 1 ATOM 1545 C C . VAL A 1 201 ? 15.012 14.991 25.553 1.00 21.03 ? 201 VAL A C 1 ATOM 1546 O O . VAL A 1 201 ? 14.514 14.140 26.305 1.00 21.51 ? 201 VAL A O 1 ATOM 1547 C CB . VAL A 1 201 ? 14.078 17.354 25.497 1.00 19.93 ? 201 VAL A CB 1 ATOM 1548 C CG1 . VAL A 1 201 ? 13.342 18.388 24.660 1.00 19.18 ? 201 VAL A CG1 1 ATOM 1549 C CG2 . VAL A 1 201 ? 13.453 17.241 26.925 1.00 18.03 ? 201 VAL A CG2 1 ATOM 1550 N N . ALA A 1 202 ? 16.329 15.117 25.366 1.00 20.95 ? 202 ALA A N 1 ATOM 1551 C CA . ALA A 1 202 ? 17.309 14.466 26.243 1.00 20.90 ? 202 ALA A CA 1 ATOM 1552 C C . ALA A 1 202 ? 17.258 15.111 27.620 1.00 20.74 ? 202 ALA A C 1 ATOM 1553 O O . ALA A 1 202 ? 17.177 16.329 27.729 1.00 20.27 ? 202 ALA A O 1 ATOM 1554 C CB . ALA A 1 202 ? 18.733 14.573 25.663 1.00 20.56 ? 202 ALA A CB 1 ATOM 1555 N N . ALA A 1 203 ? 17.303 14.283 28.661 1.00 21.18 ? 203 ALA A N 1 ATOM 1556 C CA . ALA A 1 203 ? 17.347 14.761 30.036 1.00 21.10 ? 203 ALA A CA 1 ATOM 1557 C C . ALA A 1 203 ? 18.772 14.659 30.578 1.00 21.38 ? 203 ALA A C 1 ATOM 1558 O O . ALA A 1 203 ? 19.671 14.147 29.909 1.00 21.35 ? 203 ALA A O 1 ATOM 1559 C CB . ALA A 1 203 ? 16.357 13.959 30.924 1.00 20.91 ? 203 ALA A CB 1 ATOM 1560 N N . CYS A 1 204 ? 18.953 15.135 31.804 1.00 21.99 ? 204 CYS A N 1 ATOM 1561 C CA . CYS A 1 204 ? 20.253 15.227 32.434 1.00 22.23 ? 204 CYS A CA 1 ATOM 1562 C C . CYS A 1 204 ? 20.100 15.095 33.946 1.00 22.55 ? 204 CYS A C 1 ATOM 1563 O O . CYS A 1 204 ? 19.639 16.039 34.607 1.00 22.15 ? 204 CYS A O 1 ATOM 1564 C CB . CYS A 1 204 ? 20.883 16.576 32.103 1.00 21.45 ? 204 CYS A CB 1 ATOM 1565 S SG . CYS A 1 204 ? 22.509 16.818 32.820 1.00 23.54 ? 204 CYS A SG 1 ATOM 1566 N N . ALA A 1 205 ? 20.483 13.940 34.498 1.00 23.22 ? 205 ALA A N 1 ATOM 1567 C CA . ALA A 1 205 ? 20.540 13.791 35.948 1.00 23.79 ? 205 ALA A CA 1 ATOM 1568 C C . ALA A 1 205 ? 21.740 14.592 36.468 1.00 23.93 ? 205 ALA A C 1 ATOM 1569 O O . ALA A 1 205 ? 22.885 14.348 36.059 1.00 24.09 ? 205 ALA A O 1 ATOM 1570 C CB . ALA A 1 205 ? 20.640 12.318 36.345 1.00 24.67 ? 205 ALA A CB 1 ATOM 1571 N N . LYS A 1 206 ? 21.476 15.554 37.351 1.00 23.60 ? 206 LYS A N 1 ATOM 1572 C CA . LYS A 1 206 ? 22.537 16.409 37.884 1.00 23.65 ? 206 LYS A CA 1 ATOM 1573 C C . LYS A 1 206 ? 22.391 16.682 39.404 1.00 24.18 ? 206 LYS A C 1 ATOM 1574 O O . LYS A 1 206 ? 21.311 16.469 39.966 1.00 24.71 ? 206 LYS A O 1 ATOM 1575 C CB . LYS A 1 206 ? 22.592 17.711 37.076 1.00 22.73 ? 206 LYS A CB 1 ATOM 1576 C CG . LYS A 1 206 ? 21.379 18.623 37.244 1.00 23.31 ? 206 LYS A CG 1 ATOM 1577 C CD . LYS A 1 206 ? 21.483 19.865 36.366 1.00 21.71 ? 206 LYS A CD 1 ATOM 1578 C CE . LYS A 1 206 ? 20.410 20.874 36.776 1.00 21.34 ? 206 LYS A CE 1 ATOM 1579 N NZ . LYS A 1 206 ? 20.401 22.118 35.915 1.00 21.93 ? 206 LYS A NZ 1 ATOM 1580 N N . HIS A 1 207 ? 23.452 17.113 40.102 1.00 24.71 ? 207 HIS A N 1 ATOM 1581 C CA . HIS A 1 207 ? 24.842 17.173 39.635 1.00 25.20 ? 207 HIS A CA 1 ATOM 1582 C C . HIS A 1 207 ? 25.631 16.100 40.387 1.00 25.71 ? 207 HIS A C 1 ATOM 1583 O O . HIS A 1 207 ? 25.669 16.098 41.624 1.00 26.82 ? 207 HIS A O 1 ATOM 1584 C CB . HIS A 1 207 ? 25.463 18.556 39.901 1.00 25.07 ? 207 HIS A CB 1 ATOM 1585 C CG . HIS A 1 207 ? 24.557 19.711 39.582 1.00 26.14 ? 207 HIS A CG 1 ATOM 1586 N ND1 . HIS A 1 207 ? 23.592 20.169 40.459 1.00 25.77 ? 207 HIS A ND1 1 ATOM 1587 C CD2 . HIS A 1 207 ? 24.474 20.503 38.484 1.00 24.81 ? 207 HIS A CD2 1 ATOM 1588 C CE1 . HIS A 1 207 ? 22.951 21.186 39.912 1.00 24.80 ? 207 HIS A CE1 1 ATOM 1589 N NE2 . HIS A 1 207 ? 23.475 21.417 38.721 1.00 23.20 ? 207 HIS A NE2 1 ATOM 1590 N N . PHE A 1 208 ? 26.237 15.189 39.627 1.00 25.55 ? 208 PHE A N 1 ATOM 1591 C CA . PHE A 1 208 ? 26.885 13.980 40.146 1.00 26.02 ? 208 PHE A CA 1 ATOM 1592 C C . PHE A 1 208 ? 28.236 14.308 40.815 1.00 26.21 ? 208 PHE A C 1 ATOM 1593 O O . PHE A 1 208 ? 29.100 14.881 40.167 1.00 26.04 ? 208 PHE A O 1 ATOM 1594 C CB . PHE A 1 208 ? 27.064 12.998 38.971 1.00 25.38 ? 208 PHE A CB 1 ATOM 1595 C CG . PHE A 1 208 ? 27.646 11.660 39.349 1.00 27.90 ? 208 PHE A CG 1 ATOM 1596 C CD1 . PHE A 1 208 ? 26.808 10.603 39.737 1.00 25.89 ? 208 PHE A CD1 1 ATOM 1597 C CD2 . PHE A 1 208 ? 29.032 11.436 39.277 1.00 27.31 ? 208 PHE A CD2 1 ATOM 1598 C CE1 . PHE A 1 208 ? 27.332 9.365 40.076 1.00 30.35 ? 208 PHE A CE1 1 ATOM 1599 C CE2 . PHE A 1 208 ? 29.574 10.184 39.626 1.00 30.25 ? 208 PHE A CE2 1 ATOM 1600 C CZ . PHE A 1 208 ? 28.727 9.141 40.018 1.00 29.13 ? 208 PHE A CZ 1 ATOM 1601 N N . VAL A 1 209 ? 28.423 13.996 42.107 1.00 26.85 ? 209 VAL A N 1 ATOM 1602 C CA . VAL A 1 209 ? 27.391 13.497 43.036 1.00 26.93 ? 209 VAL A CA 1 ATOM 1603 C C . VAL A 1 209 ? 27.650 14.130 44.416 1.00 28.03 ? 209 VAL A C 1 ATOM 1604 O O . VAL A 1 209 ? 28.805 14.448 44.746 1.00 28.11 ? 209 VAL A O 1 ATOM 1605 C CB . VAL A 1 209 ? 27.362 11.920 43.116 1.00 27.83 ? 209 VAL A CB 1 ATOM 1606 C CG1 . VAL A 1 209 ? 28.713 11.339 43.564 1.00 28.49 ? 209 VAL A CG1 1 ATOM 1607 C CG2 . VAL A 1 209 ? 26.205 11.389 44.021 1.00 28.41 ? 209 VAL A CG2 1 ATOM 1608 N N . GLY A 1 210 ? 26.578 14.313 45.200 1.00 28.39 ? 210 GLY A N 1 ATOM 1609 C CA . GLY A 1 210 ? 26.658 14.824 46.582 1.00 29.30 ? 210 GLY A CA 1 ATOM 1610 C C . GLY A 1 210 ? 26.678 16.347 46.631 1.00 29.20 ? 210 GLY A C 1 ATOM 1611 O O . GLY A 1 210 ? 27.127 16.942 47.623 1.00 29.82 ? 210 GLY A O 1 ATOM 1612 N N . ASP A 1 211 ? 26.201 16.963 45.546 1.00 28.03 ? 211 ASP A N 1 ATOM 1613 C CA . ASP A 1 211 ? 26.013 18.414 45.461 1.00 27.91 ? 211 ASP A CA 1 ATOM 1614 C C . ASP A 1 211 ? 25.175 19.006 46.597 1.00 28.12 ? 211 ASP A C 1 ATOM 1615 O O . ASP A 1 211 ? 25.419 20.148 47.027 1.00 28.15 ? 211 ASP A O 1 ATOM 1616 C CB . ASP A 1 211 ? 25.458 18.840 44.077 1.00 26.61 ? 211 ASP A CB 1 ATOM 1617 C CG . ASP A 1 211 ? 24.233 18.047 43.631 1.00 26.08 ? 211 ASP A CG 1 ATOM 1618 O OD1 . ASP A 1 211 ? 24.014 16.913 44.087 1.00 28.93 ? 211 ASP A OD1 1 ATOM 1619 O OD2 . ASP A 1 211 ? 23.472 18.563 42.781 1.00 27.67 ? 211 ASP A OD2 1 ATOM 1620 N N . GLY A 1 212 ? 24.216 18.213 47.091 1.00 28.39 ? 212 GLY A N 1 ATOM 1621 C CA . GLY A 1 212 ? 23.364 18.612 48.215 1.00 28.56 ? 212 GLY A CA 1 ATOM 1622 C C . GLY A 1 212 ? 23.947 18.359 49.605 1.00 30.17 ? 212 GLY A C 1 ATOM 1623 O O . GLY A 1 212 ? 23.278 18.619 50.603 1.00 30.12 ? 212 GLY A O 1 ATOM 1624 N N . GLY A 1 213 ? 25.188 17.874 49.681 1.00 30.57 ? 213 GLY A N 1 ATOM 1625 C CA . GLY A 1 213 ? 25.778 17.516 50.973 1.00 32.48 ? 213 GLY A CA 1 ATOM 1626 C C . GLY A 1 213 ? 26.959 18.359 51.425 1.00 33.86 ? 213 GLY A C 1 ATOM 1627 O O . GLY A 1 213 ? 27.713 17.942 52.318 1.00 35.24 ? 213 GLY A O 1 ATOM 1628 N N . THR A 1 214 ? 27.123 19.546 50.839 1.00 32.93 ? 214 THR A N 1 ATOM 1629 C CA . THR A 1 214 ? 28.301 20.376 51.129 1.00 34.08 ? 214 THR A CA 1 ATOM 1630 C C . THR A 1 214 ? 28.277 20.976 52.548 1.00 35.60 ? 214 THR A C 1 ATOM 1631 O O . THR A 1 214 ? 27.199 21.239 53.107 1.00 35.73 ? 214 THR A O 1 ATOM 1632 C CB . THR A 1 214 ? 28.513 21.497 50.080 1.00 32.83 ? 214 THR A CB 1 ATOM 1633 O OG1 . THR A 1 214 ? 27.427 22.430 50.148 1.00 33.03 ? 214 THR A OG1 1 ATOM 1634 C CG2 . THR A 1 214 ? 28.599 20.920 48.674 1.00 31.68 ? 214 THR A CG2 1 ATOM 1635 N N . VAL A 1 215 ? 29.460 21.182 53.123 1.00 36.77 ? 215 VAL A N 1 ATOM 1636 C CA . VAL A 1 215 ? 29.556 21.749 54.477 1.00 38.65 ? 215 VAL A CA 1 ATOM 1637 C C . VAL A 1 215 ? 28.902 23.136 54.525 1.00 37.93 ? 215 VAL A C 1 ATOM 1638 O O . VAL A 1 215 ? 29.140 23.976 53.646 1.00 36.61 ? 215 VAL A O 1 ATOM 1639 C CB . VAL A 1 215 ? 31.018 21.731 55.045 1.00 40.25 ? 215 VAL A CB 1 ATOM 1640 C CG1 . VAL A 1 215 ? 32.010 22.241 54.033 1.00 41.00 ? 215 VAL A CG1 1 ATOM 1641 C CG2 . VAL A 1 215 ? 31.125 22.519 56.366 1.00 42.17 ? 215 VAL A CG2 1 ATOM 1642 N N . ASP A 1 216 ? 28.046 23.334 55.538 1.00 38.46 ? 216 ASP A N 1 ATOM 1643 C CA . ASP A 1 216 ? 27.315 24.589 55.760 1.00 38.01 ? 216 ASP A CA 1 ATOM 1644 C C . ASP A 1 216 ? 26.420 24.996 54.583 1.00 35.96 ? 216 ASP A C 1 ATOM 1645 O O . ASP A 1 216 ? 26.030 26.162 54.475 1.00 35.87 ? 216 ASP A O 1 ATOM 1646 C CB . ASP A 1 216 ? 28.284 25.729 56.111 1.00 39.24 ? 216 ASP A CB 1 ATOM 1647 C CG . ASP A 1 216 ? 28.995 25.511 57.435 1.00 42.58 ? 216 ASP A CG 1 ATOM 1648 O OD1 . ASP A 1 216 ? 28.491 24.719 58.265 1.00 43.49 ? 216 ASP A OD1 1 ATOM 1649 O OD2 . ASP A 1 216 ? 30.051 26.150 57.646 1.00 44.55 ? 216 ASP A OD2 1 ATOM 1650 N N . GLY A 1 217 ? 26.094 24.027 53.723 1.00 34.47 ? 217 GLY A N 1 ATOM 1651 C CA . GLY A 1 217 ? 25.354 24.268 52.490 1.00 32.43 ? 217 GLY A CA 1 ATOM 1652 C C . GLY A 1 217 ? 26.060 25.230 51.548 1.00 31.97 ? 217 GLY A C 1 ATOM 1653 O O . GLY A 1 217 ? 25.411 25.915 50.758 1.00 31.56 ? 217 GLY A O 1 ATOM 1654 N N . ILE A 1 218 ? 27.392 25.292 51.621 1.00 32.19 ? 218 ILE A N 1 ATOM 1655 C CA . ILE A 1 218 ? 28.157 26.198 50.758 1.00 31.27 ? 218 ILE A CA 1 ATOM 1656 C C . ILE A 1 218 ? 28.156 25.637 49.333 1.00 30.47 ? 218 ILE A C 1 ATOM 1657 O O . ILE A 1 218 ? 28.582 24.509 49.092 1.00 30.70 ? 218 ILE A O 1 ATOM 1658 C CB . ILE A 1 218 ? 29.603 26.462 51.286 1.00 32.77 ? 218 ILE A CB 1 ATOM 1659 C CG1 . ILE A 1 218 ? 29.567 27.128 52.670 1.00 32.07 ? 218 ILE A CG1 1 ATOM 1660 C CG2 . ILE A 1 218 ? 30.408 27.297 50.260 1.00 32.14 ? 218 ILE A CG2 1 ATOM 1661 C CD1 . ILE A 1 218 ? 30.874 27.028 53.483 1.00 34.83 ? 218 ILE A CD1 1 ATOM 1662 N N . ASN A 1 219 ? 27.642 26.425 48.395 1.00 29.34 ? 219 ASN A N 1 ATOM 1663 C CA . ASN A 1 219 ? 27.520 25.989 47.008 1.00 28.18 ? 219 ASN A CA 1 ATOM 1664 C C . ASN A 1 219 ? 28.891 25.688 46.414 1.00 28.41 ? 219 ASN A C 1 ATOM 1665 O O . ASN A 1 219 ? 29.843 26.447 46.635 1.00 29.25 ? 219 ASN A O 1 ATOM 1666 C CB . ASN A 1 219 ? 26.786 27.052 46.190 1.00 27.12 ? 219 ASN A CB 1 ATOM 1667 C CG . ASN A 1 219 ? 26.430 26.584 44.784 1.00 25.83 ? 219 ASN A CG 1 ATOM 1668 O OD1 . ASN A 1 219 ? 26.562 27.352 43.828 1.00 28.68 ? 219 ASN A OD1 1 ATOM 1669 N ND2 . ASN A 1 219 ? 25.964 25.341 44.650 1.00 22.08 ? 219 ASN A ND2 1 ATOM 1670 N N . GLU A 1 220 ? 28.981 24.561 45.701 1.00 27.90 ? 220 GLU A N 1 ATOM 1671 C CA . GLU A 1 220 ? 30.193 24.135 45.003 1.00 28.49 ? 220 GLU A CA 1 ATOM 1672 C C . GLU A 1 220 ? 31.305 23.675 45.949 1.00 30.32 ? 220 GLU A C 1 ATOM 1673 O O . GLU A 1 220 ? 32.452 23.525 45.527 1.00 30.98 ? 220 GLU A O 1 ATOM 1674 C CB . GLU A 1 220 ? 30.713 25.257 44.085 1.00 28.15 ? 220 GLU A CB 1 ATOM 1675 C CG . GLU A 1 220 ? 29.659 25.787 43.091 1.00 27.00 ? 220 GLU A CG 1 ATOM 1676 C CD . GLU A 1 220 ? 30.225 26.756 42.066 1.00 27.91 ? 220 GLU A CD 1 ATOM 1677 O OE1 . GLU A 1 220 ? 31.474 26.844 41.920 1.00 29.52 ? 220 GLU A OE1 1 ATOM 1678 O OE2 . GLU A 1 220 ? 29.402 27.416 41.386 1.00 29.79 ? 220 GLU A OE2 1 ATOM 1679 N N . ASN A 1 221 ? 30.970 23.444 47.217 1.00 30.90 ? 221 ASN A N 1 ATOM 1680 C CA . ASN A 1 221 ? 31.998 23.199 48.242 1.00 32.59 ? 221 ASN A CA 1 ATOM 1681 C C . ASN A 1 221 ? 32.296 21.708 48.493 1.00 32.90 ? 221 ASN A C 1 ATOM 1682 O O . ASN A 1 221 ? 32.042 20.859 47.629 1.00 32.09 ? 221 ASN A O 1 ATOM 1683 C CB . ASN A 1 221 ? 31.635 23.925 49.543 1.00 32.99 ? 221 ASN A CB 1 ATOM 1684 C CG . ASN A 1 221 ? 32.861 24.371 50.328 1.00 36.35 ? 221 ASN A CG 1 ATOM 1685 O OD1 . ASN A 1 221 ? 33.152 23.827 51.389 1.00 36.92 ? 221 ASN A OD1 1 ATOM 1686 N ND2 . ASN A 1 221 ? 33.591 25.356 49.789 1.00 38.54 ? 221 ASN A ND2 1 ATOM 1687 N N . ASN A 1 222 ? 32.836 21.395 49.666 1.00 34.56 ? 222 ASN A N 1 ATOM 1688 C CA . ASN A 1 222 ? 33.232 20.030 49.988 1.00 35.84 ? 222 ASN A CA 1 ATOM 1689 C C . ASN A 1 222 ? 32.089 19.275 50.675 1.00 36.43 ? 222 ASN A C 1 ATOM 1690 O O . ASN A 1 222 ? 31.485 19.778 51.629 1.00 36.48 ? 222 ASN A O 1 ATOM 1691 C CB . ASN A 1 222 ? 34.487 20.050 50.873 1.00 37.78 ? 222 ASN A CB 1 ATOM 1692 C CG . ASN A 1 222 ? 35.223 18.711 50.906 1.00 38.39 ? 222 ASN A CG 1 ATOM 1693 O OD1 . ASN A 1 222 ? 35.017 17.844 50.056 1.00 37.96 ? 222 ASN A OD1 1 ATOM 1694 N ND2 . ASN A 1 222 ? 36.099 18.550 51.893 1.00 40.50 ? 222 ASN A ND2 1 ATOM 1695 N N . THR A 1 223 ? 31.780 18.084 50.169 1.00 36.26 ? 223 THR A N 1 ATOM 1696 C CA . THR A 1 223 ? 30.866 17.167 50.844 1.00 37.24 ? 223 THR A CA 1 ATOM 1697 C C . THR A 1 223 ? 31.715 16.166 51.632 1.00 39.22 ? 223 THR A C 1 ATOM 1698 O O . THR A 1 223 ? 32.445 15.352 51.038 1.00 39.09 ? 223 THR A O 1 ATOM 1699 C CB . THR A 1 223 ? 29.946 16.443 49.826 1.00 36.05 ? 223 THR A CB 1 ATOM 1700 O OG1 . THR A 1 223 ? 29.161 17.417 49.131 1.00 36.15 ? 223 THR A OG1 1 ATOM 1701 C CG2 . THR A 1 223 ? 29.006 15.452 50.522 1.00 37.13 ? 223 THR A CG2 1 ATOM 1702 N N . ILE A 1 224 ? 31.646 16.265 52.963 1.00 40.67 ? 224 ILE A N 1 ATOM 1703 C CA . ILE A 1 224 ? 32.433 15.421 53.863 1.00 42.88 ? 224 ILE A CA 1 ATOM 1704 C C . ILE A 1 224 ? 31.524 14.348 54.471 1.00 43.33 ? 224 ILE A C 1 ATOM 1705 O O . ILE A 1 224 ? 30.765 14.618 55.395 1.00 43.61 ? 224 ILE A O 1 ATOM 1706 C CB . ILE A 1 224 ? 33.135 16.254 54.982 1.00 44.30 ? 224 ILE A CB 1 ATOM 1707 C CG1 . ILE A 1 224 ? 33.975 17.393 54.374 1.00 43.69 ? 224 ILE A CG1 1 ATOM 1708 C CG2 . ILE A 1 224 ? 33.972 15.341 55.911 1.00 45.84 ? 224 ILE A CG2 1 ATOM 1709 C CD1 . ILE A 1 224 ? 34.567 18.361 55.415 1.00 45.52 ? 224 ILE A CD1 1 ATOM 1710 N N . ILE A 1 225 ? 31.608 13.140 53.916 1.00 43.44 ? 225 ILE A N 1 ATOM 1711 C CA . ILE A 1 225 ? 30.752 12.007 54.276 1.00 43.41 ? 225 ILE A CA 1 ATOM 1712 C C . ILE A 1 225 ? 31.462 10.724 53.819 1.00 44.39 ? 225 ILE A C 1 ATOM 1713 O O . ILE A 1 225 ? 32.112 10.715 52.764 1.00 43.07 ? 225 ILE A O 1 ATOM 1714 C CB . ILE A 1 225 ? 29.320 12.137 53.634 1.00 42.06 ? 225 ILE A CB 1 ATOM 1715 C CG1 . ILE A 1 225 ? 28.309 11.178 54.288 1.00 42.03 ? 225 ILE A CG1 1 ATOM 1716 C CG2 . ILE A 1 225 ? 29.359 12.004 52.088 1.00 41.06 ? 225 ILE A CG2 1 ATOM 1717 C CD1 . ILE A 1 225 ? 26.843 11.482 53.937 1.00 40.54 ? 225 ILE A CD1 1 ATOM 1718 N N . ASN A 1 226 ? 31.360 9.653 54.607 1.00 45.52 ? 226 ASN A N 1 ATOM 1719 C CA . ASN A 1 226 ? 31.949 8.361 54.208 1.00 46.51 ? 226 ASN A CA 1 ATOM 1720 C C . ASN A 1 226 ? 31.241 7.760 52.983 1.00 45.55 ? 226 ASN A C 1 ATOM 1721 O O . ASN A 1 226 ? 30.176 8.244 52.580 1.00 43.73 ? 226 ASN A O 1 ATOM 1722 C CB . ASN A 1 226 ? 32.025 7.365 55.396 1.00 48.10 ? 226 ASN A CB 1 ATOM 1723 C CG . ASN A 1 226 ? 30.646 6.984 55.970 1.00 48.51 ? 226 ASN A CG 1 ATOM 1724 O OD1 . ASN A 1 226 ? 29.595 7.324 55.421 1.00 46.99 ? 226 ASN A OD1 1 ATOM 1725 N ND2 . ASN A 1 226 ? 30.662 6.256 57.081 1.00 49.16 ? 226 ASN A ND2 1 ATOM 1726 N N . ARG A 1 227 ? 31.836 6.728 52.385 1.00 46.86 ? 227 ARG A N 1 ATOM 1727 C CA . ARG A 1 227 ? 31.268 6.097 51.183 1.00 46.91 ? 227 ARG A CA 1 ATOM 1728 C C . ARG A 1 227 ? 29.850 5.585 51.445 1.00 46.47 ? 227 ARG A C 1 ATOM 1729 O O . ARG A 1 227 ? 28.973 5.738 50.604 1.00 45.13 ? 227 ARG A O 1 ATOM 1730 C CB . ARG A 1 227 ? 32.158 4.953 50.669 1.00 47.86 ? 227 ARG A CB 1 ATOM 1731 C CG . ARG A 1 227 ? 31.687 4.377 49.331 1.00 48.19 ? 227 ARG A CG 1 ATOM 1732 C CD . ARG A 1 227 ? 32.449 3.113 48.934 1.00 50.33 ? 227 ARG A CD 1 ATOM 1733 N NE . ARG A 1 227 ? 32.039 2.615 47.615 1.00 53.90 ? 227 ARG A NE 1 ATOM 1734 C CZ . ARG A 1 227 ? 32.517 3.055 46.448 1.00 56.04 ? 227 ARG A CZ 1 ATOM 1735 N NH1 . ARG A 1 227 ? 32.065 2.531 45.309 1.00 57.17 ? 227 ARG A NH1 1 ATOM 1736 N NH2 . ARG A 1 227 ? 33.438 4.022 46.401 1.00 56.58 ? 227 ARG A NH2 1 ATOM 1737 N N . GLU A 1 228 ? 29.637 4.984 52.616 1.00 47.53 ? 228 GLU A N 1 ATOM 1738 C CA . GLU A 1 228 ? 28.325 4.474 53.008 1.00 47.97 ? 228 GLU A CA 1 ATOM 1739 C C . GLU A 1 228 ? 27.236 5.554 52.929 1.00 45.94 ? 228 GLU A C 1 ATOM 1740 O O . GLU A 1 228 ? 26.170 5.311 52.376 1.00 45.07 ? 228 GLU A O 1 ATOM 1741 C CB . GLU A 1 228 ? 28.384 3.875 54.418 1.00 49.74 ? 228 GLU A CB 1 ATOM 1742 C CG . GLU A 1 228 ? 27.112 3.177 54.838 1.00 51.12 ? 228 GLU A CG 1 ATOM 1743 C CD . GLU A 1 228 ? 27.187 2.623 56.249 1.00 54.35 ? 228 GLU A CD 1 ATOM 1744 O OE1 . GLU A 1 228 ? 26.314 2.981 57.068 1.00 58.35 ? 228 GLU A OE1 1 ATOM 1745 O OE2 . GLU A 1 228 ? 28.120 1.845 56.544 1.00 56.85 ? 228 GLU A OE2 1 ATOM 1746 N N . GLY A 1 229 ? 27.527 6.737 53.473 1.00 45.41 ? 229 GLY A N 1 ATOM 1747 C CA . GLY A 1 229 ? 26.585 7.860 53.499 1.00 44.11 ? 229 GLY A CA 1 ATOM 1748 C C . GLY A 1 229 ? 26.371 8.493 52.136 1.00 42.29 ? 229 GLY A C 1 ATOM 1749 O O . GLY A 1 229 ? 25.259 8.911 51.804 1.00 41.33 ? 229 GLY A O 1 ATOM 1750 N N . LEU A 1 230 ? 27.443 8.575 51.350 1.00 41.92 ? 230 LEU A N 1 ATOM 1751 C CA . LEU A 1 230 ? 27.365 8.993 49.952 1.00 40.62 ? 230 LEU A CA 1 ATOM 1752 C C . LEU A 1 230 ? 26.414 8.052 49.200 1.00 40.21 ? 230 LEU A C 1 ATOM 1753 O O . LEU A 1 230 ? 25.492 8.498 48.525 1.00 38.86 ? 230 LEU A O 1 ATOM 1754 C CB . LEU A 1 230 ? 28.774 8.973 49.321 1.00 40.58 ? 230 LEU A CB 1 ATOM 1755 C CG . LEU A 1 230 ? 29.159 9.762 48.051 1.00 39.36 ? 230 LEU A CG 1 ATOM 1756 C CD1 . LEU A 1 230 ? 29.320 8.886 46.798 1.00 39.71 ? 230 LEU A CD1 1 ATOM 1757 C CD2 . LEU A 1 230 ? 28.310 11.009 47.788 1.00 36.49 ? 230 LEU A CD2 1 ATOM 1758 N N . MET A 1 231 ? 26.625 6.749 49.370 1.00 41.52 ? 231 MET A N 1 ATOM 1759 C CA . MET A 1 231 ? 25.871 5.730 48.645 1.00 41.70 ? 231 MET A CA 1 ATOM 1760 C C . MET A 1 231 ? 24.415 5.575 49.075 1.00 42.01 ? 231 MET A C 1 ATOM 1761 O O . MET A 1 231 ? 23.590 5.147 48.270 1.00 41.80 ? 231 MET A O 1 ATOM 1762 C CB . MET A 1 231 ? 26.590 4.372 48.691 1.00 43.01 ? 231 MET A CB 1 ATOM 1763 C CG . MET A 1 231 ? 27.926 4.338 47.945 1.00 42.25 ? 231 MET A CG 1 ATOM 1764 S SD . MET A 1 231 ? 27.790 4.788 46.202 1.00 41.85 ? 231 MET A SD 1 ATOM 1765 C CE . MET A 1 231 ? 29.507 5.154 45.807 1.00 41.33 ? 231 MET A CE 1 ATOM 1766 N N . ASN A 1 232 ? 24.091 5.892 50.327 1.00 42.70 ? 232 ASN A N 1 ATOM 1767 C CA . ASN A 1 232 ? 22.707 5.717 50.775 1.00 43.36 ? 232 ASN A CA 1 ATOM 1768 C C . ASN A 1 232 ? 21.870 7.005 50.822 1.00 40.97 ? 232 ASN A C 1 ATOM 1769 O O . ASN A 1 232 ? 20.641 6.941 50.913 1.00 40.41 ? 232 ASN A O 1 ATOM 1770 C CB . ASN A 1 232 ? 22.613 4.885 52.073 1.00 46.36 ? 232 ASN A CB 1 ATOM 1771 C CG . ASN A 1 232 ? 22.742 5.727 53.324 1.00 50.46 ? 232 ASN A CG 1 ATOM 1772 O OD1 . ASN A 1 232 ? 23.503 6.703 53.350 1.00 55.17 ? 232 ASN A OD1 1 ATOM 1773 N ND2 . ASN A 1 232 ? 21.999 5.361 54.377 1.00 53.66 ? 232 ASN A ND2 1 ATOM 1774 N N . ILE A 1 233 ? 22.537 8.159 50.730 1.00 39.04 ? 233 ILE A N 1 ATOM 1775 C CA . ILE A 1 233 ? 21.837 9.448 50.624 1.00 36.62 ? 233 ILE A CA 1 ATOM 1776 C C . ILE A 1 233 ? 21.900 10.025 49.212 1.00 34.88 ? 233 ILE A C 1 ATOM 1777 O O . ILE A 1 233 ? 20.866 10.249 48.588 1.00 34.07 ? 233 ILE A O 1 ATOM 1778 C CB . ILE A 1 233 ? 22.325 10.510 51.670 1.00 36.96 ? 233 ILE A CB 1 ATOM 1779 C CG1 . ILE A 1 233 ? 22.072 10.027 53.112 1.00 38.10 ? 233 ILE A CG1 1 ATOM 1780 C CG2 . ILE A 1 233 ? 21.647 11.887 51.434 1.00 34.71 ? 233 ILE A CG2 1 ATOM 1781 C CD1 . ILE A 1 233 ? 22.846 10.811 54.167 1.00 38.48 ? 233 ILE A CD1 1 ATOM 1782 N N . HIS A 1 234 ? 23.109 10.228 48.697 1.00 34.19 ? 234 HIS A N 1 ATOM 1783 C CA . HIS A 1 234 ? 23.304 11.096 47.539 1.00 31.98 ? 234 HIS A CA 1 ATOM 1784 C C . HIS A 1 234 ? 23.297 10.378 46.188 1.00 31.72 ? 234 HIS A C 1 ATOM 1785 O O . HIS A 1 234 ? 23.013 10.980 45.138 1.00 29.90 ? 234 HIS A O 1 ATOM 1786 C CB . HIS A 1 234 ? 24.588 11.899 47.738 1.00 32.22 ? 234 HIS A CB 1 ATOM 1787 C CG . HIS A 1 234 ? 24.494 12.891 48.852 1.00 32.22 ? 234 HIS A CG 1 ATOM 1788 N ND1 . HIS A 1 234 ? 25.151 12.731 50.053 1.00 33.89 ? 234 HIS A ND1 1 ATOM 1789 C CD2 . HIS A 1 234 ? 23.778 14.036 48.964 1.00 29.87 ? 234 HIS A CD2 1 ATOM 1790 C CE1 . HIS A 1 234 ? 24.858 13.743 50.852 1.00 32.93 ? 234 HIS A CE1 1 ATOM 1791 N NE2 . HIS A 1 234 ? 24.038 14.556 50.208 1.00 33.71 ? 234 HIS A NE2 1 ATOM 1792 N N . MET A 1 235 ? 23.598 9.084 46.237 1.00 32.17 ? 235 MET A N 1 ATOM 1793 C CA . MET A 1 235 ? 23.698 8.249 45.055 1.00 31.73 ? 235 MET A CA 1 ATOM 1794 C C . MET A 1 235 ? 22.379 7.593 44.600 1.00 31.18 ? 235 MET A C 1 ATOM 1795 O O . MET A 1 235 ? 22.140 7.510 43.395 1.00 30.95 ? 235 MET A O 1 ATOM 1796 C CB . MET A 1 235 ? 24.784 7.177 45.271 1.00 32.40 ? 235 MET A CB 1 ATOM 1797 C CG . MET A 1 235 ? 25.179 6.415 44.027 1.00 32.28 ? 235 MET A CG 1 ATOM 1798 S SD . MET A 1 235 ? 25.921 7.470 42.750 1.00 31.22 ? 235 MET A SD 1 ATOM 1799 C CE . MET A 1 235 ? 27.583 7.666 43.422 1.00 30.58 ? 235 MET A CE 1 ATOM 1800 N N . PRO A 1 236 ? 21.545 7.084 45.542 1.00 31.57 ? 236 PRO A N 1 ATOM 1801 C CA . PRO A 1 236 ? 20.414 6.249 45.110 1.00 31.14 ? 236 PRO A CA 1 ATOM 1802 C C . PRO A 1 236 ? 19.617 6.687 43.878 1.00 29.69 ? 236 PRO A C 1 ATOM 1803 O O . PRO A 1 236 ? 19.317 5.846 43.041 1.00 29.56 ? 236 PRO A O 1 ATOM 1804 C CB . PRO A 1 236 ? 19.537 6.188 46.368 1.00 31.95 ? 236 PRO A CB 1 ATOM 1805 C CG . PRO A 1 236 ? 20.556 6.163 47.470 1.00 32.78 ? 236 PRO A CG 1 ATOM 1806 C CD . PRO A 1 236 ? 21.594 7.168 47.020 1.00 32.24 ? 236 PRO A CD 1 ATOM 1807 N N . ALA A 1 237 ? 19.291 7.974 43.752 1.00 28.49 ? 237 ALA A N 1 ATOM 1808 C CA . ALA A 1 237 ? 18.456 8.447 42.648 1.00 27.65 ? 237 ALA A CA 1 ATOM 1809 C C . ALA A 1 237 ? 19.154 8.357 41.275 1.00 27.41 ? 237 ALA A C 1 ATOM 1810 O O . ALA A 1 237 ? 18.480 8.350 40.236 1.00 26.25 ? 237 ALA A O 1 ATOM 1811 C CB . ALA A 1 237 ? 17.948 9.875 42.914 1.00 26.81 ? 237 ALA A CB 1 ATOM 1812 N N . TYR A 1 238 ? 20.487 8.290 41.275 1.00 27.32 ? 238 TYR A N 1 ATOM 1813 C CA . TYR A 1 238 ? 21.238 8.074 40.022 1.00 27.97 ? 238 TYR A CA 1 ATOM 1814 C C . TYR A 1 238 ? 20.948 6.698 39.438 1.00 28.74 ? 238 TYR A C 1 ATOM 1815 O O . TYR A 1 238 ? 20.806 6.564 38.236 1.00 28.22 ? 238 TYR A O 1 ATOM 1816 C CB . TYR A 1 238 ? 22.740 8.362 40.193 1.00 27.96 ? 238 TYR A CB 1 ATOM 1817 C CG . TYR A 1 238 ? 22.995 9.859 40.198 1.00 28.18 ? 238 TYR A CG 1 ATOM 1818 C CD1 . TYR A 1 238 ? 23.065 10.571 41.402 1.00 29.47 ? 238 TYR A CD1 1 ATOM 1819 C CD2 . TYR A 1 238 ? 23.095 10.578 38.991 1.00 27.52 ? 238 TYR A CD2 1 ATOM 1820 C CE1 . TYR A 1 238 ? 23.272 11.965 41.411 1.00 28.10 ? 238 TYR A CE1 1 ATOM 1821 C CE2 . TYR A 1 238 ? 23.298 11.969 38.991 1.00 26.92 ? 238 TYR A CE2 1 ATOM 1822 C CZ . TYR A 1 238 ? 23.373 12.648 40.214 1.00 26.96 ? 238 TYR A CZ 1 ATOM 1823 O OH . TYR A 1 238 ? 23.563 14.011 40.241 1.00 26.23 ? 238 TYR A OH 1 ATOM 1824 N N . LYS A 1 239 ? 20.792 5.696 40.307 1.00 30.14 ? 239 LYS A N 1 ATOM 1825 C CA . LYS A 1 239 ? 20.423 4.356 39.874 1.00 31.58 ? 239 LYS A CA 1 ATOM 1826 C C . LYS A 1 239 ? 18.993 4.322 39.304 1.00 30.90 ? 239 LYS A C 1 ATOM 1827 O O . LYS A 1 239 ? 18.755 3.679 38.288 1.00 31.27 ? 239 LYS A O 1 ATOM 1828 C CB . LYS A 1 239 ? 20.601 3.346 41.016 1.00 33.31 ? 239 LYS A CB 1 ATOM 1829 C CG . LYS A 1 239 ? 20.276 1.890 40.655 1.00 37.32 ? 239 LYS A CG 1 ATOM 1830 C CD . LYS A 1 239 ? 21.113 1.351 39.484 1.00 40.88 ? 239 LYS A CD 1 ATOM 1831 C CE . LYS A 1 239 ? 21.062 -0.174 39.409 1.00 45.98 ? 239 LYS A CE 1 ATOM 1832 N NZ . LYS A 1 239 ? 19.655 -0.692 39.257 1.00 47.33 ? 239 LYS A NZ 1 ATOM 1833 N N . ASN A 1 240 ? 18.051 5.025 39.936 1.00 30.18 ? 240 ASN A N 1 ATOM 1834 C CA . ASN A 1 240 ? 16.711 5.210 39.342 1.00 29.66 ? 240 ASN A CA 1 ATOM 1835 C C . ASN A 1 240 ? 16.756 5.884 37.972 1.00 28.21 ? 240 ASN A C 1 ATOM 1836 O O . ASN A 1 240 ? 16.050 5.466 37.060 1.00 28.84 ? 240 ASN A O 1 ATOM 1837 C CB . ASN A 1 240 ? 15.767 5.982 40.272 1.00 29.52 ? 240 ASN A CB 1 ATOM 1838 C CG . ASN A 1 240 ? 15.611 5.313 41.606 1.00 31.24 ? 240 ASN A CG 1 ATOM 1839 O OD1 . ASN A 1 240 ? 16.407 5.532 42.511 1.00 32.43 ? 240 ASN A OD1 1 ATOM 1840 N ND2 . ASN A 1 240 ? 14.596 4.478 41.735 1.00 33.25 ? 240 ASN A ND2 1 ATOM 1841 N N . ALA A 1 241 ? 17.589 6.915 37.838 1.00 26.92 ? 241 ALA A N 1 ATOM 1842 C CA . ALA A 1 241 ? 17.822 7.580 36.548 1.00 25.90 ? 241 ALA A CA 1 ATOM 1843 C C . ALA A 1 241 ? 18.348 6.593 35.496 1.00 26.05 ? 241 ALA A C 1 ATOM 1844 O O . ALA A 1 241 ? 17.914 6.623 34.349 1.00 26.47 ? 241 ALA A O 1 ATOM 1845 C CB . ALA A 1 241 ? 18.784 8.786 36.717 1.00 24.23 ? 241 ALA A CB 1 ATOM 1846 N N . MET A 1 242 ? 19.268 5.711 35.889 1.00 27.14 ? 242 MET A N 1 ATOM 1847 C CA . MET A 1 242 ? 19.791 4.677 34.977 1.00 27.83 ? 242 MET A CA 1 ATOM 1848 C C . MET A 1 242 ? 18.676 3.769 34.481 1.00 28.81 ? 242 MET A C 1 ATOM 1849 O O . MET A 1 242 ? 18.576 3.483 33.284 1.00 28.46 ? 242 MET A O 1 ATOM 1850 C CB . MET A 1 242 ? 20.854 3.807 35.666 1.00 28.73 ? 242 MET A CB 1 ATOM 1851 C CG . MET A 1 242 ? 22.092 4.524 36.168 1.00 28.12 ? 242 MET A CG 1 ATOM 1852 S SD . MET A 1 242 ? 23.084 5.275 34.854 1.00 29.12 ? 242 MET A SD 1 ATOM 1853 C CE . MET A 1 242 ? 22.616 6.986 35.044 1.00 26.54 ? 242 MET A CE 1 ATOM 1854 N N . ASP A 1 243 ? 17.837 3.319 35.417 1.00 29.75 ? 243 ASP A N 1 ATOM 1855 C CA . ASP A 1 243 ? 16.706 2.444 35.104 1.00 30.88 ? 243 ASP A CA 1 ATOM 1856 C C . ASP A 1 243 ? 15.698 3.083 34.152 1.00 29.82 ? 243 ASP A C 1 ATOM 1857 O O . ASP A 1 243 ? 15.029 2.376 33.408 1.00 30.76 ? 243 ASP A O 1 ATOM 1858 C CB . ASP A 1 243 ? 15.990 2.021 36.385 1.00 31.93 ? 243 ASP A CB 1 ATOM 1859 C CG . ASP A 1 243 ? 16.849 1.157 37.275 1.00 34.08 ? 243 ASP A CG 1 ATOM 1860 O OD1 . ASP A 1 243 ? 17.914 0.675 36.822 1.00 34.85 ? 243 ASP A OD1 1 ATOM 1861 O OD2 . ASP A 1 243 ? 16.447 0.951 38.435 1.00 36.67 ? 243 ASP A OD2 1 ATOM 1862 N N . LYS A 1 244 ? 15.592 4.410 34.194 1.00 28.38 ? 244 LYS A N 1 ATOM 1863 C CA . LYS A 1 244 ? 14.643 5.158 33.356 1.00 27.57 ? 244 LYS A CA 1 ATOM 1864 C C . LYS A 1 244 ? 15.270 5.715 32.065 1.00 26.98 ? 244 LYS A C 1 ATOM 1865 O O . LYS A 1 244 ? 14.631 6.454 31.311 1.00 26.94 ? 244 LYS A O 1 ATOM 1866 C CB . LYS A 1 244 ? 13.971 6.245 34.201 1.00 27.00 ? 244 LYS A CB 1 ATOM 1867 C CG . LYS A 1 244 ? 13.044 5.636 35.264 1.00 26.87 ? 244 LYS A CG 1 ATOM 1868 C CD . LYS A 1 244 ? 12.623 6.619 36.353 1.00 26.30 ? 244 LYS A CD 1 ATOM 1869 C CE . LYS A 1 244 ? 11.973 5.840 37.500 1.00 27.70 ? 244 LYS A CE 1 ATOM 1870 N NZ . LYS A 1 244 ? 11.279 6.751 38.451 1.00 28.42 ? 244 LYS A NZ 1 ATOM 1871 N N . GLY A 1 245 ? 16.525 5.347 31.815 1.00 26.73 ? 245 GLY A N 1 ATOM 1872 C CA . GLY A 1 245 ? 17.204 5.702 30.581 1.00 26.02 ? 245 GLY A CA 1 ATOM 1873 C C . GLY A 1 245 ? 17.604 7.161 30.434 1.00 24.77 ? 245 GLY A C 1 ATOM 1874 O O . GLY A 1 245 ? 17.608 7.681 29.321 1.00 24.59 ? 245 GLY A O 1 ATOM 1875 N N . VAL A 1 246 ? 17.956 7.830 31.532 1.00 24.80 ? 246 VAL A N 1 ATOM 1876 C CA . VAL A 1 246 ? 18.465 9.205 31.440 1.00 23.77 ? 246 VAL A CA 1 ATOM 1877 C C . VAL A 1 246 ? 19.634 9.262 30.431 1.00 23.81 ? 246 VAL A C 1 ATOM 1878 O O . VAL A 1 246 ? 20.533 8.405 30.453 1.00 24.41 ? 246 VAL A O 1 ATOM 1879 C CB . VAL A 1 246 ? 18.876 9.796 32.801 1.00 23.82 ? 246 VAL A CB 1 ATOM 1880 C CG1 . VAL A 1 246 ? 20.264 9.238 33.283 1.00 24.65 ? 246 VAL A CG1 1 ATOM 1881 C CG2 . VAL A 1 246 ? 18.881 11.335 32.724 1.00 21.43 ? 246 VAL A CG2 1 ATOM 1882 N N . SER A 1 247 ? 19.591 10.254 29.544 1.00 23.21 ? 247 SER A N 1 ATOM 1883 C CA . SER A 1 247 ? 20.505 10.314 28.392 1.00 23.66 ? 247 SER A CA 1 ATOM 1884 C C . SER A 1 247 ? 21.888 10.844 28.739 1.00 23.31 ? 247 SER A C 1 ATOM 1885 O O . SER A 1 247 ? 22.889 10.423 28.143 1.00 23.61 ? 247 SER A O 1 ATOM 1886 C CB . SER A 1 247 ? 19.898 11.130 27.249 1.00 22.50 ? 247 SER A CB 1 ATOM 1887 O OG . SER A 1 247 ? 18.912 10.364 26.574 1.00 24.31 ? 247 SER A OG 1 ATOM 1888 N N . THR A 1 248 ? 21.920 11.775 29.696 1.00 23.17 ? 248 THR A N 1 ATOM 1889 C CA . THR A 1 248 ? 23.145 12.440 30.121 1.00 23.16 ? 248 THR A CA 1 ATOM 1890 C C . THR A 1 248 ? 23.202 12.594 31.651 1.00 23.31 ? 248 THR A C 1 ATOM 1891 O O . THR A 1 248 ? 22.175 12.542 32.345 1.00 23.14 ? 248 THR A O 1 ATOM 1892 C CB . THR A 1 248 ? 23.336 13.833 29.435 1.00 22.38 ? 248 THR A CB 1 ATOM 1893 O OG1 . THR A 1 248 ? 22.474 14.806 30.041 1.00 23.05 ? 248 THR A OG1 1 ATOM 1894 C CG2 . THR A 1 248 ? 23.026 13.778 27.931 1.00 22.69 ? 248 THR A CG2 1 ATOM 1895 N N . VAL A 1 249 ? 24.421 12.766 32.158 1.00 23.00 ? 249 VAL A N 1 ATOM 1896 C CA . VAL A 1 249 ? 24.668 13.100 33.550 1.00 22.85 ? 249 VAL A CA 1 ATOM 1897 C C . VAL A 1 249 ? 25.644 14.288 33.597 1.00 22.83 ? 249 VAL A C 1 ATOM 1898 O O . VAL A 1 249 ? 26.694 14.259 32.965 1.00 23.14 ? 249 VAL A O 1 ATOM 1899 C CB . VAL A 1 249 ? 25.235 11.875 34.360 1.00 23.44 ? 249 VAL A CB 1 ATOM 1900 C CG1 . VAL A 1 249 ? 25.665 12.294 35.756 1.00 23.14 ? 249 VAL A CG1 1 ATOM 1901 C CG2 . VAL A 1 249 ? 24.205 10.762 34.468 1.00 23.13 ? 249 VAL A CG2 1 ATOM 1902 N N . MET A 1 250 ? 25.282 15.343 34.319 1.00 22.78 ? 250 MET A N 1 ATOM 1903 C CA . MET A 1 250 ? 26.211 16.451 34.538 1.00 22.83 ? 250 MET A CA 1 ATOM 1904 C C . MET A 1 250 ? 26.957 16.277 35.851 1.00 23.41 ? 250 MET A C 1 ATOM 1905 O O . MET A 1 250 ? 26.366 15.957 36.878 1.00 23.76 ? 250 MET A O 1 ATOM 1906 C CB . MET A 1 250 ? 25.485 17.801 34.500 1.00 22.08 ? 250 MET A CB 1 ATOM 1907 C CG . MET A 1 250 ? 26.362 19.024 34.680 1.00 21.72 ? 250 MET A CG 1 ATOM 1908 S SD . MET A 1 250 ? 25.394 20.547 34.756 1.00 22.62 ? 250 MET A SD 1 ATOM 1909 C CE . MET A 1 250 ? 24.566 20.502 33.190 1.00 21.96 ? 250 MET A CE 1 ATOM 1910 N N . ILE A 1 251 ? 28.264 16.508 35.802 1.00 24.05 ? 251 ILE A N 1 ATOM 1911 C CA . ILE A 1 251 ? 29.115 16.439 36.989 1.00 24.53 ? 251 ILE A CA 1 ATOM 1912 C C . ILE A 1 251 ? 28.978 17.700 37.858 1.00 24.87 ? 251 ILE A C 1 ATOM 1913 O O . ILE A 1 251 ? 28.775 18.806 37.349 1.00 24.60 ? 251 ILE A O 1 ATOM 1914 C CB . ILE A 1 251 ? 30.598 16.155 36.579 1.00 25.65 ? 251 ILE A CB 1 ATOM 1915 C CG1 . ILE A 1 251 ? 30.669 14.920 35.653 1.00 24.93 ? 251 ILE A CG1 1 ATOM 1916 C CG2 . ILE A 1 251 ? 31.508 16.010 37.789 1.00 24.87 ? 251 ILE A CG2 1 ATOM 1917 C CD1 . ILE A 1 251 ? 30.016 13.626 36.235 1.00 24.94 ? 251 ILE A CD1 1 ATOM 1918 N N . SER A 1 252 ? 29.079 17.510 39.174 1.00 25.42 ? 252 SER A N 1 ATOM 1919 C CA . SER A 1 252 ? 29.006 18.590 40.150 1.00 25.84 ? 252 SER A CA 1 ATOM 1920 C C . SER A 1 252 ? 30.309 19.402 40.305 1.00 26.44 ? 252 SER A C 1 ATOM 1921 O O . SER A 1 252 ? 31.411 18.841 40.266 1.00 27.70 ? 252 SER A O 1 ATOM 1922 C CB . SER A 1 252 ? 28.604 18.009 41.514 1.00 25.19 ? 252 SER A CB 1 ATOM 1923 O OG . SER A 1 252 ? 28.397 19.049 42.447 1.00 27.07 ? 252 SER A OG 1 ATOM 1924 N N . TYR A 1 253 ? 30.165 20.713 40.503 1.00 26.58 ? 253 TYR A N 1 ATOM 1925 C CA . TYR A 1 253 ? 31.265 21.574 40.947 1.00 27.67 ? 253 TYR A CA 1 ATOM 1926 C C . TYR A 1 253 ? 31.845 21.138 42.291 1.00 29.07 ? 253 TYR A C 1 ATOM 1927 O O . TYR A 1 253 ? 33.036 21.389 42.574 1.00 30.14 ? 253 TYR A O 1 ATOM 1928 C CB . TYR A 1 253 ? 30.780 22.997 41.168 1.00 27.56 ? 253 TYR A CB 1 ATOM 1929 C CG . TYR A 1 253 ? 30.409 23.814 39.957 1.00 27.23 ? 253 TYR A CG 1 ATOM 1930 C CD1 . TYR A 1 253 ? 29.133 24.366 39.851 1.00 26.81 ? 253 TYR A CD1 1 ATOM 1931 C CD2 . TYR A 1 253 ? 31.339 24.089 38.948 1.00 27.64 ? 253 TYR A CD2 1 ATOM 1932 C CE1 . TYR A 1 253 ? 28.775 25.152 38.769 1.00 27.30 ? 253 TYR A CE1 1 ATOM 1933 C CE2 . TYR A 1 253 ? 30.984 24.879 37.849 1.00 26.20 ? 253 TYR A CE2 1 ATOM 1934 C CZ . TYR A 1 253 ? 29.706 25.408 37.780 1.00 25.74 ? 253 TYR A CZ 1 ATOM 1935 O OH . TYR A 1 253 ? 29.329 26.191 36.720 1.00 25.81 ? 253 TYR A OH 1 ATOM 1936 N N . SER A 1 254 ? 31.002 20.518 43.126 1.00 29.06 ? 254 SER A N 1 ATOM 1937 C CA . SER A 1 254 ? 31.372 20.164 44.496 1.00 30.53 ? 254 SER A CA 1 ATOM 1938 C C . SER A 1 254 ? 32.481 19.113 44.542 1.00 31.55 ? 254 SER A C 1 ATOM 1939 O O . SER A 1 254 ? 32.787 18.462 43.531 1.00 31.26 ? 254 SER A O 1 ATOM 1940 C CB . SER A 1 254 ? 30.142 19.707 45.310 1.00 30.53 ? 254 SER A CB 1 ATOM 1941 O OG . SER A 1 254 ? 29.471 18.610 44.703 1.00 30.86 ? 254 SER A OG 1 ATOM 1942 N N . SER A 1 255 ? 33.099 18.981 45.715 1.00 32.86 ? 255 SER A N 1 ATOM 1943 C CA . SER A 1 255 ? 34.095 17.944 45.954 1.00 34.00 ? 255 SER A CA 1 ATOM 1944 C C . SER A 1 255 ? 33.510 16.883 46.890 1.00 34.68 ? 255 SER A C 1 ATOM 1945 O O . SER A 1 255 ? 32.555 17.152 47.627 1.00 34.52 ? 255 SER A O 1 ATOM 1946 C CB . SER A 1 255 ? 35.363 18.550 46.570 1.00 35.24 ? 255 SER A CB 1 ATOM 1947 O OG . SER A 1 255 ? 35.937 19.520 45.711 1.00 35.11 ? 255 SER A OG 1 ATOM 1948 N N . TRP A 1 256 ? 34.075 15.679 46.850 1.00 35.51 ? 256 TRP A N 1 ATOM 1949 C CA . TRP A 1 256 ? 33.754 14.638 47.834 1.00 36.18 ? 256 TRP A CA 1 ATOM 1950 C C . TRP A 1 256 ? 34.999 14.247 48.631 1.00 37.75 ? 256 TRP A C 1 ATOM 1951 O O . TRP A 1 256 ? 35.949 13.662 48.084 1.00 37.92 ? 256 TRP A O 1 ATOM 1952 C CB . TRP A 1 256 ? 33.132 13.407 47.169 1.00 35.74 ? 256 TRP A CB 1 ATOM 1953 C CG . TRP A 1 256 ? 32.877 12.297 48.142 1.00 37.44 ? 256 TRP A CG 1 ATOM 1954 C CD1 . TRP A 1 256 ? 32.178 12.381 49.322 1.00 38.49 ? 256 TRP A CD1 1 ATOM 1955 C CD2 . TRP A 1 256 ? 33.318 10.933 48.031 1.00 38.56 ? 256 TRP A CD2 1 ATOM 1956 N NE1 . TRP A 1 256 ? 32.158 11.151 49.948 1.00 39.26 ? 256 TRP A NE1 1 ATOM 1957 C CE2 . TRP A 1 256 ? 32.847 10.246 49.180 1.00 40.04 ? 256 TRP A CE2 1 ATOM 1958 C CE3 . TRP A 1 256 ? 34.059 10.222 47.072 1.00 38.24 ? 256 TRP A CE3 1 ATOM 1959 C CZ2 . TRP A 1 256 ? 33.101 8.881 49.399 1.00 40.43 ? 256 TRP A CZ2 1 ATOM 1960 C CZ3 . TRP A 1 256 ? 34.308 8.866 47.288 1.00 39.89 ? 256 TRP A CZ3 1 ATOM 1961 C CH2 . TRP A 1 256 ? 33.827 8.211 48.450 1.00 41.18 ? 256 TRP A CH2 1 ATOM 1962 N N . ASN A 1 257 ? 34.984 14.577 49.926 1.00 38.81 ? 257 ASN A N 1 ATOM 1963 C CA . ASN A 1 257 ? 36.123 14.344 50.804 1.00 40.50 ? 257 ASN A CA 1 ATOM 1964 C C . ASN A 1 257 ? 37.393 14.984 50.208 1.00 41.14 ? 257 ASN A C 1 ATOM 1965 O O . ASN A 1 257 ? 38.492 14.389 50.206 1.00 41.98 ? 257 ASN A O 1 ATOM 1966 C CB . ASN A 1 257 ? 36.299 12.839 51.081 1.00 41.46 ? 257 ASN A CB 1 ATOM 1967 C CG . ASN A 1 257 ? 35.189 12.269 51.963 1.00 42.14 ? 257 ASN A CG 1 ATOM 1968 O OD1 . ASN A 1 257 ? 34.593 12.984 52.780 1.00 42.68 ? 257 ASN A OD1 1 ATOM 1969 N ND2 . ASN A 1 257 ? 34.913 10.972 51.807 1.00 41.12 ? 257 ASN A ND2 1 ATOM 1970 N N . GLY A 1 258 ? 37.214 16.200 49.689 1.00 39.76 ? 258 GLY A N 1 ATOM 1971 C CA . GLY A 1 258 ? 38.314 16.999 49.157 1.00 39.76 ? 258 GLY A CA 1 ATOM 1972 C C . GLY A 1 258 ? 38.698 16.719 47.712 1.00 38.67 ? 258 GLY A C 1 ATOM 1973 O O . GLY A 1 258 ? 39.612 17.360 47.188 1.00 38.96 ? 258 GLY A O 1 ATOM 1974 N N . VAL A 1 259 ? 38.032 15.761 47.059 1.00 37.47 ? 259 VAL A N 1 ATOM 1975 C CA . VAL A 1 259 ? 38.338 15.472 45.657 1.00 36.10 ? 259 VAL A CA 1 ATOM 1976 C C . VAL A 1 259 ? 37.242 16.066 44.772 1.00 34.58 ? 259 VAL A C 1 ATOM 1977 O O . VAL A 1 259 ? 36.050 15.753 44.931 1.00 33.89 ? 259 VAL A O 1 ATOM 1978 C CB . VAL A 1 259 ? 38.556 13.954 45.355 1.00 36.62 ? 259 VAL A CB 1 ATOM 1979 C CG1 . VAL A 1 259 ? 38.876 13.723 43.874 1.00 34.81 ? 259 VAL A CG1 1 ATOM 1980 C CG2 . VAL A 1 259 ? 39.670 13.364 46.248 1.00 38.95 ? 259 VAL A CG2 1 ATOM 1981 N N . LYS A 1 260 ? 37.674 16.939 43.864 1.00 33.58 ? 260 LYS A N 1 ATOM 1982 C CA . LYS A 1 260 ? 36.813 17.591 42.903 1.00 32.43 ? 260 LYS A CA 1 ATOM 1983 C C . LYS A 1 260 ? 36.082 16.517 42.110 1.00 31.64 ? 260 LYS A C 1 ATOM 1984 O O . LYS A 1 260 ? 36.723 15.610 41.570 1.00 32.23 ? 260 LYS A O 1 ATOM 1985 C CB . LYS A 1 260 ? 37.657 18.468 41.964 1.00 32.22 ? 260 LYS A CB 1 ATOM 1986 C CG . LYS A 1 260 ? 38.253 19.713 42.633 1.00 33.28 ? 260 LYS A CG 1 ATOM 1987 C CD . LYS A 1 260 ? 37.231 20.853 42.709 1.00 30.72 ? 260 LYS A CD 1 ATOM 1988 C CE . LYS A 1 260 ? 37.732 21.969 43.623 1.00 32.56 ? 260 LYS A CE 1 ATOM 1989 N NZ . LYS A 1 260 ? 36.717 23.057 43.726 1.00 29.76 ? 260 LYS A NZ 1 ATOM 1990 N N . MET A 1 261 ? 34.751 16.598 42.069 1.00 30.59 ? 261 MET A N 1 ATOM 1991 C CA . MET A 1 261 ? 33.960 15.695 41.220 1.00 29.52 ? 261 MET A CA 1 ATOM 1992 C C . MET A 1 261 ? 34.439 15.682 39.762 1.00 28.73 ? 261 MET A C 1 ATOM 1993 O O . MET A 1 261 ? 34.492 14.616 39.132 1.00 28.41 ? 261 MET A O 1 ATOM 1994 C CB . MET A 1 261 ? 32.460 16.008 41.303 1.00 28.58 ? 261 MET A CB 1 ATOM 1995 C CG . MET A 1 261 ? 31.763 15.495 42.593 1.00 29.18 ? 261 MET A CG 1 ATOM 1996 S SD . MET A 1 261 ? 32.010 13.732 42.984 1.00 31.96 ? 261 MET A SD 1 ATOM 1997 C CE . MET A 1 261 ? 31.706 12.946 41.396 1.00 27.89 ? 261 MET A CE 1 ATOM 1998 N N . HIS A 1 262 ? 34.796 16.858 39.234 1.00 28.29 ? 262 HIS A N 1 ATOM 1999 C CA . HIS A 1 262 ? 35.254 16.976 37.838 1.00 27.65 ? 262 HIS A CA 1 ATOM 2000 C C . HIS A 1 262 ? 36.610 16.300 37.566 1.00 28.68 ? 262 HIS A C 1 ATOM 2001 O O . HIS A 1 262 ? 37.010 16.192 36.406 1.00 27.97 ? 262 HIS A O 1 ATOM 2002 C CB . HIS A 1 262 ? 35.277 18.438 37.363 1.00 27.52 ? 262 HIS A CB 1 ATOM 2003 C CG . HIS A 1 262 ? 33.919 19.018 37.133 1.00 26.75 ? 262 HIS A CG 1 ATOM 2004 N ND1 . HIS A 1 262 ? 33.427 19.301 35.874 1.00 27.48 ? 262 HIS A ND1 1 ATOM 2005 C CD2 . HIS A 1 262 ? 32.940 19.357 38.004 1.00 25.25 ? 262 HIS A CD2 1 ATOM 2006 C CE1 . HIS A 1 262 ? 32.200 19.781 35.981 1.00 24.80 ? 262 HIS A CE1 1 ATOM 2007 N NE2 . HIS A 1 262 ? 31.886 19.837 37.264 1.00 26.05 ? 262 HIS A NE2 1 ATOM 2008 N N . ALA A 1 263 ? 37.299 15.861 38.632 1.00 29.63 ? 263 ALA A N 1 ATOM 2009 C CA . ALA A 1 263 ? 38.579 15.134 38.530 1.00 30.93 ? 263 ALA A CA 1 ATOM 2010 C C . ALA A 1 263 ? 38.504 13.706 39.105 1.00 32.02 ? 263 ALA A C 1 ATOM 2011 O O . ALA A 1 263 ? 39.502 12.992 39.132 1.00 33.39 ? 263 ALA A O 1 ATOM 2012 C CB . ALA A 1 263 ? 39.698 15.920 39.241 1.00 32.02 ? 263 ALA A CB 1 ATOM 2013 N N . ASN A 1 264 ? 37.329 13.300 39.586 1.00 31.76 ? 264 ASN A N 1 ATOM 2014 C CA . ASN A 1 264 ? 37.180 12.002 40.249 1.00 32.33 ? 264 ASN A CA 1 ATOM 2015 C C . ASN A 1 264 ? 36.928 10.834 39.287 1.00 32.12 ? 264 ASN A C 1 ATOM 2016 O O . ASN A 1 264 ? 35.785 10.543 38.931 1.00 31.35 ? 264 ASN A O 1 ATOM 2017 C CB . ASN A 1 264 ? 36.089 12.065 41.325 1.00 32.05 ? 264 ASN A CB 1 ATOM 2018 C CG . ASN A 1 264 ? 36.207 10.941 42.340 1.00 33.62 ? 264 ASN A CG 1 ATOM 2019 O OD1 . ASN A 1 264 ? 36.642 9.831 42.019 1.00 34.79 ? 264 ASN A OD1 1 ATOM 2020 N ND2 . ASN A 1 264 ? 35.831 11.228 43.577 1.00 34.99 ? 264 ASN A ND2 1 ATOM 2021 N N . GLN A 1 265 ? 38.007 10.167 38.884 1.00 32.82 ? 265 GLN A N 1 ATOM 2022 C CA . GLN A 1 265 ? 37.932 9.039 37.956 1.00 33.38 ? 265 GLN A CA 1 ATOM 2023 C C . GLN A 1 265 ? 37.240 7.840 38.592 1.00 34.43 ? 265 GLN A C 1 ATOM 2024 O O . GLN A 1 265 ? 36.482 7.125 37.925 1.00 34.13 ? 265 GLN A O 1 ATOM 2025 C CB . GLN A 1 265 ? 39.335 8.649 37.488 1.00 34.16 ? 265 GLN A CB 1 ATOM 2026 C CG . GLN A 1 265 ? 39.383 7.682 36.330 1.00 34.93 ? 265 GLN A CG 1 ATOM 2027 C CD . GLN A 1 265 ? 40.799 7.217 36.051 1.00 38.26 ? 265 GLN A CD 1 ATOM 2028 O OE1 . GLN A 1 265 ? 41.378 7.532 35.021 1.00 41.20 ? 265 GLN A OE1 1 ATOM 2029 N NE2 . GLN A 1 265 ? 41.366 6.485 36.977 1.00 41.34 ? 265 GLN A NE2 1 ATOM 2030 N N . ASP A 1 266 ? 37.500 7.630 39.879 1.00 35.71 ? 266 ASP A N 1 ATOM 2031 C CA . ASP A 1 266 ? 36.862 6.549 40.632 1.00 37.51 ? 266 ASP A CA 1 ATOM 2032 C C . ASP A 1 266 ? 35.335 6.602 40.581 1.00 35.67 ? 266 ASP A C 1 ATOM 2033 O O . ASP A 1 266 ? 34.690 5.585 40.365 1.00 35.84 ? 266 ASP A O 1 ATOM 2034 C CB . ASP A 1 266 ? 37.323 6.543 42.093 1.00 39.22 ? 266 ASP A CB 1 ATOM 2035 C CG . ASP A 1 266 ? 38.761 6.096 42.253 1.00 44.31 ? 266 ASP A CG 1 ATOM 2036 O OD1 . ASP A 1 266 ? 39.392 5.637 41.264 1.00 47.98 ? 266 ASP A OD1 1 ATOM 2037 O OD2 . ASP A 1 266 ? 39.273 6.204 43.392 1.00 50.29 ? 266 ASP A OD2 1 ATOM 2038 N N . LEU A 1 267 ? 34.767 7.779 40.803 1.00 34.18 ? 267 LEU A N 1 ATOM 2039 C CA . LEU A 1 267 ? 33.311 7.933 40.771 1.00 33.40 ? 267 LEU A CA 1 ATOM 2040 C C . LEU A 1 267 ? 32.715 8.035 39.353 1.00 32.00 ? 267 LEU A C 1 ATOM 2041 O O . LEU A 1 267 ? 31.701 7.402 39.054 1.00 31.92 ? 267 LEU A O 1 ATOM 2042 C CB . LEU A 1 267 ? 32.869 9.120 41.645 1.00 32.96 ? 267 LEU A CB 1 ATOM 2043 C CG . LEU A 1 267 ? 32.960 8.952 43.173 1.00 34.00 ? 267 LEU A CG 1 ATOM 2044 C CD1 . LEU A 1 267 ? 32.479 10.210 43.883 1.00 33.57 ? 267 LEU A CD1 1 ATOM 2045 C CD2 . LEU A 1 267 ? 32.173 7.738 43.673 1.00 36.03 ? 267 LEU A CD2 1 ATOM 2046 N N . VAL A 1 268 ? 33.337 8.821 38.480 1.00 31.12 ? 268 VAL A N 1 ATOM 2047 C CA . VAL A 1 268 ? 32.781 9.044 37.133 1.00 30.32 ? 268 VAL A CA 1 ATOM 2048 C C . VAL A 1 268 ? 32.953 7.797 36.244 1.00 30.27 ? 268 VAL A C 1 ATOM 2049 O O . VAL A 1 268 ? 32.004 7.340 35.618 1.00 29.82 ? 268 VAL A O 1 ATOM 2050 C CB . VAL A 1 268 ? 33.374 10.310 36.444 1.00 29.60 ? 268 VAL A CB 1 ATOM 2051 C CG1 . VAL A 1 268 ? 32.846 10.444 35.027 1.00 29.74 ? 268 VAL A CG1 1 ATOM 2052 C CG2 . VAL A 1 268 ? 33.062 11.581 37.264 1.00 29.58 ? 268 VAL A CG2 1 ATOM 2053 N N . THR A 1 269 ? 34.159 7.241 36.217 1.00 30.70 ? 269 THR A N 1 ATOM 2054 C CA . THR A 1 269 ? 34.436 6.057 35.412 1.00 31.31 ? 269 THR A CA 1 ATOM 2055 C C . THR A 1 269 ? 34.184 4.792 36.222 1.00 32.75 ? 269 THR A C 1 ATOM 2056 O O . THR A 1 269 ? 33.395 3.937 35.810 1.00 32.88 ? 269 THR A O 1 ATOM 2057 C CB . THR A 1 269 ? 35.871 6.093 34.836 1.00 31.70 ? 269 THR A CB 1 ATOM 2058 O OG1 . THR A 1 269 ? 36.006 7.249 33.996 1.00 29.25 ? 269 THR A OG1 1 ATOM 2059 C CG2 . THR A 1 269 ? 36.185 4.824 34.021 1.00 32.60 ? 269 THR A CG2 1 ATOM 2060 N N . GLY A 1 270 ? 34.832 4.693 37.384 1.00 33.71 ? 270 GLY A N 1 ATOM 2061 C CA . GLY A 1 270 ? 34.745 3.502 38.224 1.00 35.27 ? 270 GLY A CA 1 ATOM 2062 C C . GLY A 1 270 ? 33.323 3.173 38.627 1.00 35.29 ? 270 GLY A C 1 ATOM 2063 O O . GLY A 1 270 ? 32.912 2.013 38.550 1.00 36.49 ? 270 GLY A O 1 ATOM 2064 N N . TYR A 1 271 ? 32.568 4.188 39.053 1.00 34.06 ? 271 TYR A N 1 ATOM 2065 C CA . TYR A 1 271 ? 31.193 3.964 39.507 1.00 33.97 ? 271 TYR A CA 1 ATOM 2066 C C . TYR A 1 271 ? 30.108 4.225 38.449 1.00 32.62 ? 271 TYR A C 1 ATOM 2067 O O . TYR A 1 271 ? 29.391 3.297 38.057 1.00 33.05 ? 271 TYR A O 1 ATOM 2068 C CB . TYR A 1 271 ? 30.876 4.725 40.807 1.00 34.08 ? 271 TYR A CB 1 ATOM 2069 C CG . TYR A 1 271 ? 29.695 4.119 41.520 1.00 35.03 ? 271 TYR A CG 1 ATOM 2070 C CD1 . TYR A 1 271 ? 29.836 2.932 42.247 1.00 36.57 ? 271 TYR A CD1 1 ATOM 2071 C CD2 . TYR A 1 271 ? 28.430 4.700 41.438 1.00 33.74 ? 271 TYR A CD2 1 ATOM 2072 C CE1 . TYR A 1 271 ? 28.757 2.356 42.886 1.00 37.68 ? 271 TYR A CE1 1 ATOM 2073 C CE2 . TYR A 1 271 ? 27.339 4.128 42.071 1.00 33.70 ? 271 TYR A CE2 1 ATOM 2074 C CZ . TYR A 1 271 ? 27.508 2.958 42.786 1.00 36.72 ? 271 TYR A CZ 1 ATOM 2075 O OH . TYR A 1 271 ? 26.431 2.383 43.420 1.00 38.84 ? 271 TYR A OH 1 ATOM 2076 N N . LEU A 1 272 ? 29.981 5.472 38.001 1.00 30.70 ? 272 LEU A N 1 ATOM 2077 C CA . LEU A 1 272 ? 28.895 5.825 37.097 1.00 29.88 ? 272 LEU A CA 1 ATOM 2078 C C . LEU A 1 272 ? 28.923 4.976 35.831 1.00 30.38 ? 272 LEU A C 1 ATOM 2079 O O . LEU A 1 272 ? 27.924 4.325 35.507 1.00 30.58 ? 272 LEU A O 1 ATOM 2080 C CB . LEU A 1 272 ? 28.896 7.317 36.781 1.00 28.41 ? 272 LEU A CB 1 ATOM 2081 C CG . LEU A 1 272 ? 27.862 7.843 35.777 1.00 26.98 ? 272 LEU A CG 1 ATOM 2082 C CD1 . LEU A 1 272 ? 26.434 7.643 36.251 1.00 27.04 ? 272 LEU A CD1 1 ATOM 2083 C CD2 . LEU A 1 272 ? 28.164 9.308 35.497 1.00 26.20 ? 272 LEU A CD2 1 ATOM 2084 N N . LYS A 1 273 ? 30.070 4.947 35.150 1.00 30.79 ? 273 LYS A N 1 ATOM 2085 C CA . LYS A 1 273 ? 30.205 4.186 33.898 1.00 31.18 ? 273 LYS A CA 1 ATOM 2086 C C . LYS A 1 273 ? 30.339 2.668 34.074 1.00 33.28 ? 273 LYS A C 1 ATOM 2087 O O . LYS A 1 273 ? 29.574 1.913 33.471 1.00 33.66 ? 273 LYS A O 1 ATOM 2088 C CB . LYS A 1 273 ? 31.348 4.734 33.036 1.00 31.09 ? 273 LYS A CB 1 ATOM 2089 C CG . LYS A 1 273 ? 31.135 6.158 32.546 1.00 28.85 ? 273 LYS A CG 1 ATOM 2090 C CD . LYS A 1 273 ? 32.242 6.575 31.597 1.00 28.26 ? 273 LYS A CD 1 ATOM 2091 C CE . LYS A 1 273 ? 31.880 7.868 30.903 1.00 26.17 ? 273 LYS A CE 1 ATOM 2092 N NZ . LYS A 1 273 ? 32.842 8.188 29.798 1.00 26.99 ? 273 LYS A NZ 1 ATOM 2093 N N . ASP A 1 274 ? 31.301 2.224 34.891 1.00 34.72 ? 274 ASP A N 1 ATOM 2094 C CA . ASP A 1 274 ? 31.673 0.800 34.976 1.00 36.86 ? 274 ASP A CA 1 ATOM 2095 C C . ASP A 1 274 ? 30.809 -0.035 35.923 1.00 37.78 ? 274 ASP A C 1 ATOM 2096 O O . ASP A 1 274 ? 30.756 -1.257 35.772 1.00 39.59 ? 274 ASP A O 1 ATOM 2097 C CB . ASP A 1 274 ? 33.140 0.614 35.399 1.00 37.59 ? 274 ASP A CB 1 ATOM 2098 C CG . ASP A 1 274 ? 34.136 1.140 34.379 1.00 38.29 ? 274 ASP A CG 1 ATOM 2099 O OD1 . ASP A 1 274 ? 33.741 1.570 33.272 1.00 38.44 ? 274 ASP A OD1 1 ATOM 2100 O OD2 . ASP A 1 274 ? 35.343 1.119 34.699 1.00 40.65 ? 274 ASP A OD2 1 ATOM 2101 N N . THR A 1 275 ? 30.192 0.606 36.916 1.00 37.14 ? 275 THR A N 1 ATOM 2102 C CA . THR A 1 275 ? 29.363 -0.096 37.910 1.00 38.13 ? 275 THR A CA 1 ATOM 2103 C C . THR A 1 275 ? 27.860 0.072 37.609 1.00 37.19 ? 275 THR A C 1 ATOM 2104 O O . THR A 1 275 ? 27.125 -0.920 37.534 1.00 37.66 ? 275 THR A O 1 ATOM 2105 C CB . THR A 1 275 ? 29.713 0.331 39.381 1.00 38.58 ? 275 THR A CB 1 ATOM 2106 O OG1 . THR A 1 275 ? 31.096 0.060 39.641 1.00 39.80 ? 275 THR A OG1 1 ATOM 2107 C CG2 . THR A 1 275 ? 28.858 -0.420 40.412 1.00 39.27 ? 275 THR A CG2 1 ATOM 2108 N N . LEU A 1 276 ? 27.421 1.318 37.420 1.00 35.41 ? 276 LEU A N 1 ATOM 2109 C CA . LEU A 1 276 ? 26.031 1.601 37.049 1.00 34.51 ? 276 LEU A CA 1 ATOM 2110 C C . LEU A 1 276 ? 25.754 1.345 35.561 1.00 34.29 ? 276 LEU A C 1 ATOM 2111 O O . LEU A 1 276 ? 24.599 1.364 35.123 1.00 33.95 ? 276 LEU A O 1 ATOM 2112 C CB . LEU A 1 276 ? 25.645 3.037 37.414 1.00 33.25 ? 276 LEU A CB 1 ATOM 2113 C CG . LEU A 1 276 ? 25.564 3.431 38.890 1.00 33.36 ? 276 LEU A CG 1 ATOM 2114 C CD1 . LEU A 1 276 ? 25.073 4.871 38.996 1.00 30.38 ? 276 LEU A CD1 1 ATOM 2115 C CD2 . LEU A 1 276 ? 24.674 2.472 39.676 1.00 32.45 ? 276 LEU A CD2 1 ATOM 2116 N N . LYS A 1 277 ? 26.820 1.108 34.796 1.00 34.20 ? 277 LYS A N 1 ATOM 2117 C CA . LYS A 1 277 ? 26.726 0.774 33.372 1.00 33.96 ? 277 LYS A CA 1 ATOM 2118 C C . LYS A 1 277 ? 26.073 1.894 32.549 1.00 32.03 ? 277 LYS A C 1 ATOM 2119 O O . LYS A 1 277 ? 25.359 1.624 31.581 1.00 31.58 ? 277 LYS A O 1 ATOM 2120 C CB . LYS A 1 277 ? 26.017 -0.579 33.162 1.00 34.83 ? 277 LYS A CB 1 ATOM 2121 C CG . LYS A 1 277 ? 26.639 -1.761 33.914 1.00 38.31 ? 277 LYS A CG 1 ATOM 2122 C CD . LYS A 1 277 ? 28.034 -2.074 33.393 1.00 41.73 ? 277 LYS A CD 1 ATOM 2123 C CE . LYS A 1 277 ? 28.687 -3.212 34.167 1.00 45.98 ? 277 LYS A CE 1 ATOM 2124 N NZ . LYS A 1 277 ? 30.084 -3.374 33.682 1.00 48.87 ? 277 LYS A NZ 1 ATOM 2125 N N . PHE A 1 278 ? 26.333 3.146 32.938 1.00 30.68 ? 278 PHE A N 1 ATOM 2126 C CA . PHE A 1 278 ? 25.861 4.308 32.186 1.00 29.23 ? 278 PHE A CA 1 ATOM 2127 C C . PHE A 1 278 ? 26.520 4.348 30.812 1.00 29.00 ? 278 PHE A C 1 ATOM 2128 O O . PHE A 1 278 ? 27.754 4.332 30.703 1.00 29.12 ? 278 PHE A O 1 ATOM 2129 C CB . PHE A 1 278 ? 26.136 5.609 32.947 1.00 27.96 ? 278 PHE A CB 1 ATOM 2130 C CG . PHE A 1 278 ? 25.645 6.847 32.242 1.00 26.24 ? 278 PHE A CG 1 ATOM 2131 C CD1 . PHE A 1 278 ? 24.314 6.960 31.837 1.00 24.79 ? 278 PHE A CD1 1 ATOM 2132 C CD2 . PHE A 1 278 ? 26.515 7.907 31.990 1.00 25.14 ? 278 PHE A CD2 1 ATOM 2133 C CE1 . PHE A 1 278 ? 23.852 8.117 31.198 1.00 23.76 ? 278 PHE A CE1 1 ATOM 2134 C CE2 . PHE A 1 278 ? 26.076 9.061 31.337 1.00 23.69 ? 278 PHE A CE2 1 ATOM 2135 C CZ . PHE A 1 278 ? 24.742 9.171 30.943 1.00 24.12 ? 278 PHE A CZ 1 ATOM 2136 N N . LYS A 1 279 ? 25.680 4.394 29.779 1.00 28.80 ? 279 LYS A N 1 ATOM 2137 C CA . LYS A 1 279 ? 26.109 4.340 28.375 1.00 28.86 ? 279 LYS A CA 1 ATOM 2138 C C . LYS A 1 279 ? 25.789 5.634 27.622 1.00 27.60 ? 279 LYS A C 1 ATOM 2139 O O . LYS A 1 279 ? 26.100 5.761 26.422 1.00 28.11 ? 279 LYS A O 1 ATOM 2140 C CB . LYS A 1 279 ? 25.463 3.149 27.661 1.00 29.52 ? 279 LYS A CB 1 ATOM 2141 C CG . LYS A 1 279 ? 25.805 1.785 28.224 1.00 32.01 ? 279 LYS A CG 1 ATOM 2142 C CD . LYS A 1 279 ? 27.232 1.373 27.944 1.00 35.43 ? 279 LYS A CD 1 ATOM 2143 C CE . LYS A 1 279 ? 27.564 0.088 28.717 1.00 38.30 ? 279 LYS A CE 1 ATOM 2144 N NZ . LYS A 1 279 ? 29.027 -0.059 28.978 1.00 40.34 ? 279 LYS A NZ 1 ATOM 2145 N N . GLY A 1 280 ? 25.164 6.588 28.314 1.00 26.35 ? 280 GLY A N 1 ATOM 2146 C CA . GLY A 1 280 ? 24.921 7.914 27.747 1.00 25.24 ? 280 GLY A CA 1 ATOM 2147 C C . GLY A 1 280 ? 26.201 8.730 27.855 1.00 24.72 ? 280 GLY A C 1 ATOM 2148 O O . GLY A 1 280 ? 27.270 8.158 28.067 1.00 25.33 ? 280 GLY A O 1 ATOM 2149 N N . PHE A 1 281 ? 26.107 10.053 27.716 1.00 23.78 ? 281 PHE A N 1 ATOM 2150 C CA . PHE A 1 281 ? 27.294 10.898 27.887 1.00 24.02 ? 281 PHE A CA 1 ATOM 2151 C C . PHE A 1 281 ? 27.335 11.712 29.172 1.00 23.87 ? 281 PHE A C 1 ATOM 2152 O O . PHE A 1 281 ? 26.302 12.136 29.703 1.00 23.67 ? 281 PHE A O 1 ATOM 2153 C CB . PHE A 1 281 ? 27.659 11.744 26.632 1.00 23.29 ? 281 PHE A CB 1 ATOM 2154 C CG . PHE A 1 281 ? 26.741 12.927 26.339 1.00 22.05 ? 281 PHE A CG 1 ATOM 2155 C CD1 . PHE A 1 281 ? 26.900 14.155 27.001 1.00 21.47 ? 281 PHE A CD1 1 ATOM 2156 C CD2 . PHE A 1 281 ? 25.803 12.845 25.308 1.00 21.03 ? 281 PHE A CD2 1 ATOM 2157 C CE1 . PHE A 1 281 ? 26.075 15.261 26.689 1.00 21.34 ? 281 PHE A CE1 1 ATOM 2158 C CE2 . PHE A 1 281 ? 24.987 13.933 24.963 1.00 20.49 ? 281 PHE A CE2 1 ATOM 2159 C CZ . PHE A 1 281 ? 25.107 15.148 25.646 1.00 20.15 ? 281 PHE A CZ 1 ATOM 2160 N N . VAL A 1 282 ? 28.559 11.910 29.651 1.00 23.68 ? 282 VAL A N 1 ATOM 2161 C CA . VAL A 1 282 ? 28.827 12.656 30.858 1.00 23.45 ? 282 VAL A CA 1 ATOM 2162 C C . VAL A 1 282 ? 29.278 14.072 30.482 1.00 22.86 ? 282 VAL A C 1 ATOM 2163 O O . VAL A 1 282 ? 30.240 14.255 29.732 1.00 22.73 ? 282 VAL A O 1 ATOM 2164 C CB . VAL A 1 282 ? 29.915 11.940 31.699 1.00 24.43 ? 282 VAL A CB 1 ATOM 2165 C CG1 . VAL A 1 282 ? 30.353 12.803 32.869 1.00 23.14 ? 282 VAL A CG1 1 ATOM 2166 C CG2 . VAL A 1 282 ? 29.414 10.566 32.163 1.00 24.38 ? 282 VAL A CG2 1 ATOM 2167 N N . ILE A 1 283 ? 28.578 15.071 31.007 1.00 22.37 ? 283 ILE A N 1 ATOM 2168 C CA . ILE A 1 283 ? 28.881 16.453 30.683 1.00 21.49 ? 283 ILE A CA 1 ATOM 2169 C C . ILE A 1 283 ? 29.423 17.188 31.912 1.00 22.81 ? 283 ILE A C 1 ATOM 2170 O O . ILE A 1 283 ? 29.015 16.915 33.042 1.00 22.97 ? 283 ILE A O 1 ATOM 2171 C CB . ILE A 1 283 ? 27.637 17.184 30.025 1.00 21.16 ? 283 ILE A CB 1 ATOM 2172 C CG1 . ILE A 1 283 ? 28.046 18.551 29.444 1.00 19.70 ? 283 ILE A CG1 1 ATOM 2173 C CG2 . ILE A 1 283 ? 26.404 17.268 30.984 1.00 18.77 ? 283 ILE A CG2 1 ATOM 2174 C CD1 . ILE A 1 283 ? 26.933 19.247 28.608 1.00 19.65 ? 283 ILE A CD1 1 ATOM 2175 N N . SER A 1 284 ? 30.354 18.113 31.690 1.00 23.25 ? 284 SER A N 1 ATOM 2176 C CA . SER A 1 284 ? 30.785 19.009 32.751 1.00 23.60 ? 284 SER A CA 1 ATOM 2177 C C . SER A 1 284 ? 29.701 20.054 33.066 1.00 23.65 ? 284 SER A C 1 ATOM 2178 O O . SER A 1 284 ? 28.744 20.268 32.298 1.00 22.99 ? 284 SER A O 1 ATOM 2179 C CB . SER A 1 284 ? 32.075 19.743 32.357 1.00 23.48 ? 284 SER A CB 1 ATOM 2180 O OG . SER A 1 284 ? 31.767 20.884 31.555 1.00 23.41 ? 284 SER A OG 1 ATOM 2181 N N . ASP A 1 285 ? 29.882 20.719 34.195 1.00 23.66 ? 285 ASP A N 1 ATOM 2182 C CA . ASP A 1 285 ? 29.151 21.932 34.455 1.00 24.02 ? 285 ASP A CA 1 ATOM 2183 C C . ASP A 1 285 ? 29.916 23.108 33.834 1.00 24.32 ? 285 ASP A C 1 ATOM 2184 O O . ASP A 1 285 ? 31.023 22.942 33.288 1.00 25.18 ? 285 ASP A O 1 ATOM 2185 C CB . ASP A 1 285 ? 28.936 22.119 35.960 1.00 23.76 ? 285 ASP A CB 1 ATOM 2186 C CG . ASP A 1 285 ? 27.658 22.879 36.273 1.00 24.58 ? 285 ASP A CG 1 ATOM 2187 O OD1 . ASP A 1 285 ? 27.190 23.654 35.395 1.00 24.66 ? 285 ASP A OD1 1 ATOM 2188 O OD2 . ASP A 1 285 ? 27.115 22.681 37.383 1.00 23.95 ? 285 ASP A OD2 1 ATOM 2189 N N . TRP A 1 286 ? 29.317 24.287 33.937 1.00 23.92 ? 286 TRP A N 1 ATOM 2190 C CA . TRP A 1 286 ? 29.773 25.513 33.290 1.00 24.30 ? 286 TRP A CA 1 ATOM 2191 C C . TRP A 1 286 ? 31.093 25.949 33.886 1.00 25.31 ? 286 TRP A C 1 ATOM 2192 O O . TRP A 1 286 ? 31.139 26.355 35.040 1.00 25.76 ? 286 TRP A O 1 ATOM 2193 C CB . TRP A 1 286 ? 28.690 26.573 33.512 1.00 24.02 ? 286 TRP A CB 1 ATOM 2194 C CG . TRP A 1 286 ? 28.944 27.984 33.077 1.00 24.29 ? 286 TRP A CG 1 ATOM 2195 C CD1 . TRP A 1 286 ? 29.768 28.903 33.663 1.00 24.76 ? 286 TRP A CD1 1 ATOM 2196 C CD2 . TRP A 1 286 ? 28.268 28.664 32.015 1.00 23.26 ? 286 TRP A CD2 1 ATOM 2197 N NE1 . TRP A 1 286 ? 29.667 30.116 33.002 1.00 25.67 ? 286 TRP A NE1 1 ATOM 2198 C CE2 . TRP A 1 286 ? 28.746 29.993 31.994 1.00 24.79 ? 286 TRP A CE2 1 ATOM 2199 C CE3 . TRP A 1 286 ? 27.291 28.277 31.082 1.00 23.21 ? 286 TRP A CE3 1 ATOM 2200 C CZ2 . TRP A 1 286 ? 28.302 30.935 31.053 1.00 25.22 ? 286 TRP A CZ2 1 ATOM 2201 C CZ3 . TRP A 1 286 ? 26.860 29.214 30.138 1.00 23.22 ? 286 TRP A CZ3 1 ATOM 2202 C CH2 . TRP A 1 286 ? 27.358 30.520 30.139 1.00 23.86 ? 286 TRP A CH2 1 ATOM 2203 N N . GLU A 1 287 ? 32.165 25.856 33.096 1.00 25.29 ? 287 GLU A N 1 ATOM 2204 C CA . GLU A 1 287 ? 33.532 26.104 33.596 1.00 26.08 ? 287 GLU A CA 1 ATOM 2205 C C . GLU A 1 287 ? 33.906 25.164 34.745 1.00 25.86 ? 287 GLU A C 1 ATOM 2206 O O . GLU A 1 287 ? 34.778 25.484 35.554 1.00 26.08 ? 287 GLU A O 1 ATOM 2207 C CB . GLU A 1 287 ? 33.726 27.553 34.037 1.00 25.88 ? 287 GLU A CB 1 ATOM 2208 C CG . GLU A 1 287 ? 33.550 28.587 32.954 1.00 26.59 ? 287 GLU A CG 1 ATOM 2209 C CD . GLU A 1 287 ? 33.491 30.005 33.513 1.00 28.12 ? 287 GLU A CD 1 ATOM 2210 O OE1 . GLU A 1 287 ? 33.302 30.189 34.743 1.00 30.51 ? 287 GLU A OE1 1 ATOM 2211 O OE2 . GLU A 1 287 ? 33.631 30.941 32.716 1.00 30.38 ? 287 GLU A OE2 1 ATOM 2212 N N . GLY A 1 288 ? 33.249 24.008 34.805 1.00 25.08 ? 288 GLY A N 1 ATOM 2213 C CA . GLY A 1 288 ? 33.492 23.047 35.884 1.00 25.73 ? 288 GLY A CA 1 ATOM 2214 C C . GLY A 1 288 ? 34.921 22.526 35.925 1.00 26.92 ? 288 GLY A C 1 ATOM 2215 O O . GLY A 1 288 ? 35.511 22.389 37.000 1.00 27.29 ? 288 GLY A O 1 ATOM 2216 N N . ILE A 1 289 ? 35.480 22.231 34.749 1.00 26.78 ? 289 ILE A N 1 ATOM 2217 C CA . ILE A 1 289 ? 36.879 21.801 34.670 1.00 27.64 ? 289 ILE A CA 1 ATOM 2218 C C . ILE A 1 289 ? 37.857 22.911 35.115 1.00 29.10 ? 289 ILE A C 1 ATOM 2219 O O . ILE A 1 289 ? 38.860 22.612 35.771 1.00 29.98 ? 289 ILE A O 1 ATOM 2220 C CB . ILE A 1 289 ? 37.235 21.153 33.283 1.00 27.57 ? 289 ILE A CB 1 ATOM 2221 C CG1 . ILE A 1 289 ? 37.544 22.207 32.201 1.00 27.48 ? 289 ILE A CG1 1 ATOM 2222 C CG2 . ILE A 1 289 ? 36.117 20.196 32.851 1.00 25.62 ? 289 ILE A CG2 1 ATOM 2223 C CD1 . ILE A 1 289 ? 38.161 21.623 30.914 1.00 26.58 ? 289 ILE A CD1 1 ATOM 2224 N N . ASP A 1 290 ? 37.540 24.177 34.798 1.00 29.25 ? 290 ASP A N 1 ATOM 2225 C CA . ASP A 1 290 ? 38.345 25.339 35.232 1.00 30.65 ? 290 ASP A CA 1 ATOM 2226 C C . ASP A 1 290 ? 38.471 25.386 36.748 1.00 31.93 ? 290 ASP A C 1 ATOM 2227 O O . ASP A 1 290 ? 39.530 25.739 37.290 1.00 33.27 ? 290 ASP A O 1 ATOM 2228 C CB . ASP A 1 290 ? 37.715 26.671 34.784 1.00 30.33 ? 290 ASP A CB 1 ATOM 2229 C CG . ASP A 1 290 ? 37.318 26.690 33.314 1.00 29.16 ? 290 ASP A CG 1 ATOM 2230 O OD1 . ASP A 1 290 ? 36.681 25.739 32.846 1.00 26.13 ? 290 ASP A OD1 1 ATOM 2231 O OD2 . ASP A 1 290 ? 37.638 27.678 32.625 1.00 30.94 ? 290 ASP A OD2 1 ATOM 2232 N N . ARG A 1 291 ? 37.372 25.038 37.417 1.00 31.76 ? 291 ARG A N 1 ATOM 2233 C CA . ARG A 1 291 ? 37.241 25.167 38.863 1.00 32.65 ? 291 ARG A CA 1 ATOM 2234 C C . ARG A 1 291 ? 37.836 24.008 39.648 1.00 33.52 ? 291 ARG A C 1 ATOM 2235 O O . ARG A 1 291 ? 37.777 24.008 40.879 1.00 34.86 ? 291 ARG A O 1 ATOM 2236 C CB . ARG A 1 291 ? 35.776 25.413 39.239 1.00 31.80 ? 291 ARG A CB 1 ATOM 2237 C CG . ARG A 1 291 ? 35.261 26.725 38.675 1.00 30.75 ? 291 ARG A CG 1 ATOM 2238 C CD . ARG A 1 291 ? 33.799 26.968 38.937 1.00 29.22 ? 291 ARG A CD 1 ATOM 2239 N NE . ARG A 1 291 ? 33.295 27.949 37.978 1.00 29.05 ? 291 ARG A NE 1 ATOM 2240 C CZ . ARG A 1 291 ? 32.086 28.505 38.007 1.00 28.63 ? 291 ARG A CZ 1 ATOM 2241 N NH1 . ARG A 1 291 ? 31.231 28.199 38.977 1.00 29.65 ? 291 ARG A NH1 1 ATOM 2242 N NH2 . ARG A 1 291 ? 31.734 29.371 37.054 1.00 26.62 ? 291 ARG A NH2 1 ATOM 2243 N N . ILE A 1 292 ? 38.427 23.038 38.941 1.00 33.56 ? 292 ILE A N 1 ATOM 2244 C CA . ILE A 1 292 ? 39.201 21.960 39.580 1.00 33.69 ? 292 ILE A CA 1 ATOM 2245 C C . ILE A 1 292 ? 40.385 22.560 40.334 1.00 35.37 ? 292 ILE A C 1 ATOM 2246 O O . ILE A 1 292 ? 40.708 22.126 41.448 1.00 36.00 ? 292 ILE A O 1 ATOM 2247 C CB . ILE A 1 292 ? 39.712 20.910 38.552 1.00 33.52 ? 292 ILE A CB 1 ATOM 2248 C CG1 . ILE A 1 292 ? 38.558 20.050 38.030 1.00 31.16 ? 292 ILE A CG1 1 ATOM 2249 C CG2 . ILE A 1 292 ? 40.779 19.997 39.175 1.00 33.91 ? 292 ILE A CG2 1 ATOM 2250 C CD1 . ILE A 1 292 ? 38.906 19.279 36.733 1.00 32.10 ? 292 ILE A CD1 1 ATOM 2251 N N . THR A 1 293 ? 41.011 23.570 39.728 1.00 35.41 ? 293 THR A N 1 ATOM 2252 C CA . THR A 1 293 ? 42.153 24.267 40.328 1.00 37.01 ? 293 THR A CA 1 ATOM 2253 C C . THR A 1 293 ? 41.747 25.485 41.164 1.00 37.99 ? 293 THR A C 1 ATOM 2254 O O . THR A 1 293 ? 40.637 26.017 41.026 1.00 36.57 ? 293 THR A O 1 ATOM 2255 C CB . THR A 1 293 ? 43.162 24.746 39.255 1.00 37.27 ? 293 THR A CB 1 ATOM 2256 O OG1 . THR A 1 293 ? 42.538 25.734 38.427 1.00 35.82 ? 293 THR A OG1 1 ATOM 2257 C CG2 . THR A 1 293 ? 43.663 23.576 38.397 1.00 36.03 ? 293 THR A CG2 1 ATOM 2258 N N . THR A 1 294 ? 42.683 25.918 42.009 1.00 40.05 ? 294 THR A N 1 ATOM 2259 C CA . THR A 1 294 ? 42.578 27.144 42.793 1.00 41.88 ? 294 THR A CA 1 ATOM 2260 C C . THR A 1 294 ? 43.817 28.012 42.516 1.00 43.11 ? 294 THR A C 1 ATOM 2261 O O . THR A 1 294 ? 44.944 27.544 42.693 1.00 44.57 ? 294 THR A O 1 ATOM 2262 C CB . THR A 1 294 ? 42.451 26.830 44.307 1.00 42.88 ? 294 THR A CB 1 ATOM 2263 O OG1 . THR A 1 294 ? 41.235 26.106 44.530 1.00 42.51 ? 294 THR A OG1 1 ATOM 2264 C CG2 . THR A 1 294 ? 42.439 28.111 45.164 1.00 44.63 ? 294 THR A CG2 1 ATOM 2265 N N . PRO A 1 295 ? 43.616 29.252 42.023 1.00 42.95 ? 295 PRO A N 1 ATOM 2266 C CA . PRO A 1 295 ? 42.331 29.794 41.550 1.00 41.87 ? 295 PRO A CA 1 ATOM 2267 C C . PRO A 1 295 ? 41.767 29.070 40.313 1.00 40.42 ? 295 PRO A C 1 ATOM 2268 O O . PRO A 1 295 ? 42.501 28.349 39.625 1.00 40.76 ? 295 PRO A O 1 ATOM 2269 C CB . PRO A 1 295 ? 42.654 31.259 41.228 1.00 42.37 ? 295 PRO A CB 1 ATOM 2270 C CG . PRO A 1 295 ? 44.134 31.337 41.135 1.00 44.21 ? 295 PRO A CG 1 ATOM 2271 C CD . PRO A 1 295 ? 44.704 30.243 41.956 1.00 44.46 ? 295 PRO A CD 1 ATOM 2272 N N . ALA A 1 296 ? 40.473 29.254 40.044 1.00 39.21 ? 296 ALA A N 1 ATOM 2273 C CA . ALA A 1 296 ? 39.825 28.633 38.886 1.00 37.62 ? 296 ALA A CA 1 ATOM 2274 C C . ALA A 1 296 ? 40.516 29.071 37.596 1.00 37.68 ? 296 ALA A C 1 ATOM 2275 O O . ALA A 1 296 ? 40.912 30.231 37.464 1.00 38.37 ? 296 ALA A O 1 ATOM 2276 C CB . ALA A 1 296 ? 38.340 28.984 38.844 1.00 36.24 ? 296 ALA A CB 1 ATOM 2277 N N . GLY A 1 297 ? 40.679 28.132 36.666 1.00 37.07 ? 297 GLY A N 1 ATOM 2278 C CA . GLY A 1 297 ? 41.314 28.396 35.369 1.00 36.93 ? 297 GLY A CA 1 ATOM 2279 C C . GLY A 1 297 ? 42.810 28.710 35.381 1.00 38.14 ? 297 GLY A C 1 ATOM 2280 O O . GLY A 1 297 ? 43.350 29.132 34.358 1.00 38.41 ? 297 GLY A O 1 ATOM 2281 N N . SER A 1 298 ? 43.486 28.500 36.513 1.00 38.89 ? 298 SER A N 1 ATOM 2282 C CA . SER A 1 298 ? 44.915 28.845 36.631 1.00 39.90 ? 298 SER A CA 1 ATOM 2283 C C . SER A 1 298 ? 45.867 27.798 36.042 1.00 39.75 ? 298 SER A C 1 ATOM 2284 O O . SER A 1 298 ? 47.056 28.069 35.862 1.00 41.04 ? 298 SER A O 1 ATOM 2285 C CB . SER A 1 298 ? 45.299 29.184 38.078 1.00 41.44 ? 298 SER A CB 1 ATOM 2286 O OG . SER A 1 298 ? 45.124 28.077 38.945 1.00 41.52 ? 298 SER A OG 1 ATOM 2287 N N . ASP A 1 299 ? 45.346 26.609 35.749 1.00 38.02 ? 299 ASP A N 1 ATOM 2288 C CA . ASP A 1 299 ? 46.103 25.591 35.028 1.00 37.78 ? 299 ASP A CA 1 ATOM 2289 C C . ASP A 1 299 ? 45.148 24.812 34.139 1.00 36.07 ? 299 ASP A C 1 ATOM 2290 O O . ASP A 1 299 ? 44.731 23.689 34.477 1.00 35.65 ? 299 ASP A O 1 ATOM 2291 C CB . ASP A 1 299 ? 46.843 24.648 35.982 1.00 38.83 ? 299 ASP A CB 1 ATOM 2292 C CG . ASP A 1 299 ? 47.871 23.771 35.263 1.00 40.34 ? 299 ASP A CG 1 ATOM 2293 O OD1 . ASP A 1 299 ? 47.881 23.727 34.018 1.00 41.69 ? 299 ASP A OD1 1 ATOM 2294 O OD2 . ASP A 1 299 ? 48.672 23.109 35.943 1.00 42.98 ? 299 ASP A OD2 1 ATOM 2295 N N . TYR A 1 300 ? 44.786 25.422 33.012 1.00 34.64 ? 300 TYR A N 1 ATOM 2296 C CA . TYR A 1 300 ? 43.724 24.879 32.182 1.00 32.93 ? 300 TYR A CA 1 ATOM 2297 C C . TYR A 1 300 ? 44.143 23.585 31.493 1.00 32.36 ? 300 TYR A C 1 ATOM 2298 O O . TYR A 1 300 ? 43.309 22.729 31.192 1.00 31.11 ? 300 TYR A O 1 ATOM 2299 C CB . TYR A 1 300 ? 43.217 25.916 31.178 1.00 32.49 ? 300 TYR A CB 1 ATOM 2300 C CG . TYR A 1 300 ? 41.866 25.565 30.584 1.00 31.35 ? 300 TYR A CG 1 ATOM 2301 C CD1 . TYR A 1 300 ? 40.698 25.633 31.359 1.00 31.50 ? 300 TYR A CD1 1 ATOM 2302 C CD2 . TYR A 1 300 ? 41.748 25.171 29.252 1.00 32.04 ? 300 TYR A CD2 1 ATOM 2303 C CE1 . TYR A 1 300 ? 39.445 25.315 30.814 1.00 30.41 ? 300 TYR A CE1 1 ATOM 2304 C CE2 . TYR A 1 300 ? 40.493 24.846 28.696 1.00 30.55 ? 300 TYR A CE2 1 ATOM 2305 C CZ . TYR A 1 300 ? 39.347 24.925 29.479 1.00 30.02 ? 300 TYR A CZ 1 ATOM 2306 O OH . TYR A 1 300 ? 38.104 24.608 28.931 1.00 27.53 ? 300 TYR A OH 1 ATOM 2307 N N . SER A 1 301 ? 45.443 23.454 31.246 1.00 33.46 ? 301 SER A N 1 ATOM 2308 C CA . SER A 1 301 ? 46.019 22.221 30.721 1.00 33.60 ? 301 SER A CA 1 ATOM 2309 C C . SER A 1 301 ? 45.777 21.031 31.661 1.00 33.59 ? 301 SER A C 1 ATOM 2310 O O . SER A 1 301 ? 45.353 19.962 31.219 1.00 32.19 ? 301 SER A O 1 ATOM 2311 C CB . SER A 1 301 ? 47.508 22.410 30.470 1.00 34.84 ? 301 SER A CB 1 ATOM 2312 O OG . SER A 1 301 ? 48.121 21.170 30.198 1.00 36.07 ? 301 SER A OG 1 ATOM 2313 N N . TYR A 1 302 ? 46.028 21.234 32.957 1.00 34.51 ? 302 TYR A N 1 ATOM 2314 C CA . TYR A 1 302 ? 45.665 20.248 33.986 1.00 34.93 ? 302 TYR A CA 1 ATOM 2315 C C . TYR A 1 302 ? 44.148 20.011 34.046 1.00 32.81 ? 302 TYR A C 1 ATOM 2316 O O . TYR A 1 302 ? 43.695 18.866 34.103 1.00 31.92 ? 302 TYR A O 1 ATOM 2317 C CB . TYR A 1 302 ? 46.212 20.657 35.369 1.00 37.30 ? 302 TYR A CB 1 ATOM 2318 C CG . TYR A 1 302 ? 45.792 19.715 36.474 1.00 39.63 ? 302 TYR A CG 1 ATOM 2319 C CD1 . TYR A 1 302 ? 46.335 18.422 36.561 1.00 41.67 ? 302 TYR A CD1 1 ATOM 2320 C CD2 . TYR A 1 302 ? 44.844 20.105 37.427 1.00 39.79 ? 302 TYR A CD2 1 ATOM 2321 C CE1 . TYR A 1 302 ? 45.940 17.542 37.575 1.00 42.78 ? 302 TYR A CE1 1 ATOM 2322 C CE2 . TYR A 1 302 ? 44.443 19.232 38.446 1.00 41.07 ? 302 TYR A CE2 1 ATOM 2323 C CZ . TYR A 1 302 ? 44.996 17.954 38.507 1.00 41.56 ? 302 TYR A CZ 1 ATOM 2324 O OH . TYR A 1 302 ? 44.609 17.090 39.510 1.00 43.38 ? 302 TYR A OH 1 ATOM 2325 N N . SER A 1 303 ? 43.369 21.093 34.013 1.00 31.59 ? 303 SER A N 1 ATOM 2326 C CA . SER A 1 303 ? 41.897 21.001 33.989 1.00 29.79 ? 303 SER A CA 1 ATOM 2327 C C . SER A 1 303 ? 41.382 20.046 32.912 1.00 28.74 ? 303 SER A C 1 ATOM 2328 O O . SER A 1 303 ? 40.516 19.207 33.194 1.00 28.52 ? 303 SER A O 1 ATOM 2329 C CB . SER A 1 303 ? 41.265 22.381 33.792 1.00 28.91 ? 303 SER A CB 1 ATOM 2330 O OG . SER A 1 303 ? 41.389 23.167 34.962 1.00 29.48 ? 303 SER A OG 1 ATOM 2331 N N . VAL A 1 304 ? 41.923 20.176 31.695 1.00 28.40 ? 304 VAL A N 1 ATOM 2332 C CA . VAL A 1 304 ? 41.533 19.340 30.552 1.00 27.49 ? 304 VAL A CA 1 ATOM 2333 C C . VAL A 1 304 ? 41.989 17.893 30.763 1.00 28.43 ? 304 VAL A C 1 ATOM 2334 O O . VAL A 1 304 ? 41.195 16.967 30.647 1.00 27.64 ? 304 VAL A O 1 ATOM 2335 C CB . VAL A 1 304 ? 42.074 19.907 29.211 1.00 27.71 ? 304 VAL A CB 1 ATOM 2336 C CG1 . VAL A 1 304 ? 41.837 18.914 28.044 1.00 26.13 ? 304 VAL A CG1 1 ATOM 2337 C CG2 . VAL A 1 304 ? 41.440 21.252 28.913 1.00 26.91 ? 304 VAL A CG2 1 ATOM 2338 N N . LYS A 1 305 ? 43.268 17.719 31.092 1.00 29.34 ? 305 LYS A N 1 ATOM 2339 C CA . LYS A 1 305 ? 43.830 16.400 31.370 1.00 30.90 ? 305 LYS A CA 1 ATOM 2340 C C . LYS A 1 305 ? 43.035 15.648 32.459 1.00 30.25 ? 305 LYS A C 1 ATOM 2341 O O . LYS A 1 305 ? 42.596 14.521 32.234 1.00 29.88 ? 305 LYS A O 1 ATOM 2342 C CB . LYS A 1 305 ? 45.298 16.529 31.778 1.00 31.76 ? 305 LYS A CB 1 ATOM 2343 C CG . LYS A 1 305 ? 45.973 15.204 32.051 1.00 35.93 ? 305 LYS A CG 1 ATOM 2344 C CD . LYS A 1 305 ? 47.313 15.417 32.732 1.00 41.29 ? 305 LYS A CD 1 ATOM 2345 C CE . LYS A 1 305 ? 47.738 14.188 33.530 1.00 44.49 ? 305 LYS A CE 1 ATOM 2346 N NZ . LYS A 1 305 ? 48.998 14.410 34.285 1.00 44.04 ? 305 LYS A NZ 1 ATOM 2347 N N . ALA A 1 306 ? 42.843 16.292 33.611 1.00 29.80 ? 306 ALA A N 1 ATOM 2348 C CA . ALA A 1 306 ? 42.202 15.672 34.770 1.00 29.67 ? 306 ALA A CA 1 ATOM 2349 C C . ALA A 1 306 ? 40.734 15.307 34.538 1.00 28.51 ? 306 ALA A C 1 ATOM 2350 O O . ALA A 1 306 ? 40.286 14.243 34.952 1.00 28.62 ? 306 ALA A O 1 ATOM 2351 C CB . ALA A 1 306 ? 42.339 16.571 35.999 1.00 29.82 ? 306 ALA A CB 1 ATOM 2352 N N . SER A 1 307 ? 39.991 16.186 33.875 1.00 27.50 ? 307 SER A N 1 ATOM 2353 C CA . SER A 1 307 ? 38.573 15.951 33.628 1.00 26.88 ? 307 SER A CA 1 ATOM 2354 C C . SER A 1 307 ? 38.356 14.852 32.587 1.00 26.53 ? 307 SER A C 1 ATOM 2355 O O . SER A 1 307 ? 37.504 13.965 32.763 1.00 25.88 ? 307 SER A O 1 ATOM 2356 C CB . SER A 1 307 ? 37.886 17.246 33.191 1.00 26.13 ? 307 SER A CB 1 ATOM 2357 O OG . SER A 1 307 ? 38.535 17.799 32.052 1.00 28.02 ? 307 SER A OG 1 ATOM 2358 N N . ILE A 1 308 ? 39.132 14.919 31.506 1.00 26.71 ? 308 ILE A N 1 ATOM 2359 C CA . ILE A 1 308 ? 38.987 13.970 30.407 1.00 26.39 ? 308 ILE A CA 1 ATOM 2360 C C . ILE A 1 308 ? 39.471 12.593 30.843 1.00 27.51 ? 308 ILE A C 1 ATOM 2361 O O . ILE A 1 308 ? 38.802 11.607 30.570 1.00 27.32 ? 308 ILE A O 1 ATOM 2362 C CB . ILE A 1 308 ? 39.668 14.453 29.088 1.00 26.78 ? 308 ILE A CB 1 ATOM 2363 C CG1 . ILE A 1 308 ? 39.026 15.760 28.585 1.00 24.85 ? 308 ILE A CG1 1 ATOM 2364 C CG2 . ILE A 1 308 ? 39.603 13.350 27.993 1.00 26.03 ? 308 ILE A CG2 1 ATOM 2365 C CD1 . ILE A 1 308 ? 37.495 15.724 28.429 1.00 23.97 ? 308 ILE A CD1 1 ATOM 2366 N N . LEU A 1 309 ? 40.611 12.533 31.539 1.00 28.08 ? 309 LEU A N 1 ATOM 2367 C CA . LEU A 1 309 ? 41.071 11.275 32.143 1.00 29.18 ? 309 LEU A CA 1 ATOM 2368 C C . LEU A 1 309 ? 40.112 10.732 33.218 1.00 29.43 ? 309 LEU A C 1 ATOM 2369 O O . LEU A 1 309 ? 40.004 9.511 33.397 1.00 30.82 ? 309 LEU A O 1 ATOM 2370 C CB . LEU A 1 309 ? 42.509 11.383 32.679 1.00 29.81 ? 309 LEU A CB 1 ATOM 2371 C CG . LEU A 1 309 ? 43.566 11.501 31.562 1.00 29.72 ? 309 LEU A CG 1 ATOM 2372 C CD1 . LEU A 1 309 ? 44.952 11.563 32.170 1.00 28.55 ? 309 LEU A CD1 1 ATOM 2373 C CD2 . LEU A 1 309 ? 43.461 10.376 30.497 1.00 27.08 ? 309 LEU A CD2 1 ATOM 2374 N N . ALA A 1 310 ? 39.410 11.624 33.920 1.00 29.01 ? 310 ALA A N 1 ATOM 2375 C CA . ALA A 1 310 ? 38.408 11.204 34.906 1.00 28.92 ? 310 ALA A CA 1 ATOM 2376 C C . ALA A 1 310 ? 37.220 10.492 34.258 1.00 28.84 ? 310 ALA A C 1 ATOM 2377 O O . ALA A 1 310 ? 36.555 9.670 34.903 1.00 29.31 ? 310 ALA A O 1 ATOM 2378 C CB . ALA A 1 310 ? 37.923 12.389 35.725 1.00 28.62 ? 310 ALA A CB 1 ATOM 2379 N N . GLY A 1 311 ? 36.944 10.817 32.991 1.00 27.93 ? 311 GLY A N 1 ATOM 2380 C CA . GLY A 1 311 ? 35.909 10.123 32.232 1.00 27.94 ? 311 GLY A CA 1 ATOM 2381 C C . GLY A 1 311 ? 34.781 10.991 31.696 1.00 26.87 ? 311 GLY A C 1 ATOM 2382 O O . GLY A 1 311 ? 33.780 10.471 31.209 1.00 26.54 ? 311 GLY A O 1 ATOM 2383 N N . LEU A 1 312 ? 34.935 12.311 31.781 1.00 26.53 ? 312 LEU A N 1 ATOM 2384 C CA . LEU A 1 312 ? 33.926 13.218 31.229 1.00 25.73 ? 312 LEU A CA 1 ATOM 2385 C C . LEU A 1 312 ? 33.982 13.151 29.712 1.00 25.62 ? 312 LEU A C 1 ATOM 2386 O O . LEU A 1 312 ? 35.060 12.965 29.128 1.00 25.81 ? 312 LEU A O 1 ATOM 2387 C CB . LEU A 1 312 ? 34.108 14.646 31.754 1.00 25.34 ? 312 LEU A CB 1 ATOM 2388 C CG . LEU A 1 312 ? 33.618 14.916 33.185 1.00 25.23 ? 312 LEU A CG 1 ATOM 2389 C CD1 . LEU A 1 312 ? 34.526 14.305 34.289 1.00 23.69 ? 312 LEU A CD1 1 ATOM 2390 C CD2 . LEU A 1 312 ? 33.460 16.406 33.411 1.00 24.24 ? 312 LEU A CD2 1 ATOM 2391 N N . ASP A 1 313 ? 32.817 13.258 29.075 1.00 24.84 ? 313 ASP A N 1 ATOM 2392 C CA . ASP A 1 313 ? 32.719 13.075 27.618 1.00 24.12 ? 313 ASP A CA 1 ATOM 2393 C C . ASP A 1 313 ? 32.568 14.381 26.853 1.00 23.65 ? 313 ASP A C 1 ATOM 2394 O O . ASP A 1 313 ? 33.192 14.557 25.802 1.00 23.23 ? 313 ASP A O 1 ATOM 2395 C CB . ASP A 1 313 ? 31.557 12.128 27.258 1.00 23.83 ? 313 ASP A CB 1 ATOM 2396 C CG . ASP A 1 313 ? 31.615 10.826 28.023 1.00 24.22 ? 313 ASP A CG 1 ATOM 2397 O OD1 . ASP A 1 313 ? 30.572 10.409 28.584 1.00 22.20 ? 313 ASP A OD1 1 ATOM 2398 O OD2 . ASP A 1 313 ? 32.716 10.239 28.080 1.00 23.01 ? 313 ASP A OD2 1 ATOM 2399 N N . MET A 1 314 ? 31.712 15.266 27.378 1.00 23.28 ? 314 MET A N 1 ATOM 2400 C CA . MET A 1 314 ? 31.435 16.578 26.784 1.00 23.09 ? 314 MET A CA 1 ATOM 2401 C C . MET A 1 314 ? 31.732 17.695 27.790 1.00 22.92 ? 314 MET A C 1 ATOM 2402 O O . MET A 1 314 ? 31.304 17.634 28.939 1.00 22.79 ? 314 MET A O 1 ATOM 2403 C CB . MET A 1 314 ? 29.971 16.679 26.316 1.00 22.26 ? 314 MET A CB 1 ATOM 2404 C CG . MET A 1 314 ? 29.630 17.994 25.594 1.00 21.61 ? 314 MET A CG 1 ATOM 2405 S SD . MET A 1 314 ? 27.915 18.089 25.023 1.00 22.29 ? 314 MET A SD 1 ATOM 2406 C CE . MET A 1 314 ? 27.890 16.932 23.662 1.00 21.46 ? 314 MET A CE 1 ATOM 2407 N N . ILE A 1 315 ? 32.467 18.707 27.340 1.00 22.74 ? 315 ILE A N 1 ATOM 2408 C CA . ILE A 1 315 ? 32.815 19.847 28.175 1.00 22.41 ? 315 ILE A CA 1 ATOM 2409 C C . ILE A 1 315 ? 31.976 21.070 27.803 1.00 22.30 ? 315 ILE A C 1 ATOM 2410 O O . ILE A 1 315 ? 32.005 21.558 26.658 1.00 22.05 ? 315 ILE A O 1 ATOM 2411 C CB . ILE A 1 315 ? 34.346 20.144 28.122 1.00 23.04 ? 315 ILE A CB 1 ATOM 2412 C CG1 . ILE A 1 315 ? 35.155 18.881 28.474 1.00 23.24 ? 315 ILE A CG1 1 ATOM 2413 C CG2 . ILE A 1 315 ? 34.740 21.361 28.999 1.00 22.66 ? 315 ILE A CG2 1 ATOM 2414 C CD1 . ILE A 1 315 ? 34.811 18.249 29.815 1.00 23.44 ? 315 ILE A CD1 1 ATOM 2415 N N . MET A 1 316 ? 31.214 21.531 28.790 1.00 21.88 ? 316 MET A N 1 ATOM 2416 C CA . MET A 1 316 ? 30.529 22.800 28.736 1.00 21.84 ? 316 MET A CA 1 ATOM 2417 C C . MET A 1 316 ? 31.591 23.878 28.952 1.00 22.01 ? 316 MET A C 1 ATOM 2418 O O . MET A 1 316 ? 31.851 24.296 30.082 1.00 22.27 ? 316 MET A O 1 ATOM 2419 C CB . MET A 1 316 ? 29.422 22.841 29.808 1.00 20.84 ? 316 MET A CB 1 ATOM 2420 C CG . MET A 1 316 ? 28.603 24.136 29.826 1.00 20.49 ? 316 MET A CG 1 ATOM 2421 S SD . MET A 1 316 ? 27.341 24.135 31.126 1.00 22.51 ? 316 MET A SD 1 ATOM 2422 C CE . MET A 1 316 ? 26.529 22.552 30.842 1.00 16.74 ? 316 MET A CE 1 ATOM 2423 N N . VAL A 1 317 ? 32.202 24.337 27.859 1.00 22.32 ? 317 VAL A N 1 ATOM 2424 C CA . VAL A 1 317 ? 33.418 25.165 27.964 1.00 23.41 ? 317 VAL A CA 1 ATOM 2425 C C . VAL A 1 317 ? 33.254 26.417 28.880 1.00 24.10 ? 317 VAL A C 1 ATOM 2426 O O . VAL A 1 317 ? 33.986 26.537 29.862 1.00 24.67 ? 317 VAL A O 1 ATOM 2427 C CB . VAL A 1 317 ? 34.089 25.435 26.583 1.00 23.70 ? 317 VAL A CB 1 ATOM 2428 C CG1 . VAL A 1 317 ? 35.367 26.218 26.748 1.00 24.68 ? 317 VAL A CG1 1 ATOM 2429 C CG2 . VAL A 1 317 ? 34.396 24.113 25.883 1.00 23.13 ? 317 VAL A CG2 1 ATOM 2430 N N . PRO A 1 318 ? 32.282 27.318 28.589 1.00 24.04 ? 318 PRO A N 1 ATOM 2431 C CA . PRO A 1 318 ? 31.419 27.382 27.409 1.00 23.99 ? 318 PRO A CA 1 ATOM 2432 C C . PRO A 1 318 ? 31.899 28.405 26.367 1.00 24.94 ? 318 PRO A C 1 ATOM 2433 O O . PRO A 1 318 ? 31.334 28.483 25.271 1.00 25.15 ? 318 PRO A O 1 ATOM 2434 C CB . PRO A 1 318 ? 30.077 27.836 28.005 1.00 22.80 ? 318 PRO A CB 1 ATOM 2435 C CG . PRO A 1 318 ? 30.500 28.787 29.101 1.00 23.09 ? 318 PRO A CG 1 ATOM 2436 C CD . PRO A 1 318 ? 31.886 28.343 29.580 1.00 23.58 ? 318 PRO A CD 1 ATOM 2437 N N . ASN A 1 319 ? 32.912 29.192 26.716 1.00 26.03 ? 319 ASN A N 1 ATOM 2438 C CA . ASN A 1 319 ? 33.288 30.348 25.908 1.00 27.34 ? 319 ASN A CA 1 ATOM 2439 C C . ASN A 1 319 ? 34.578 30.146 25.143 1.00 27.96 ? 319 ASN A C 1 ATOM 2440 O O . ASN A 1 319 ? 34.619 30.312 23.912 1.00 28.75 ? 319 ASN A O 1 ATOM 2441 C CB . ASN A 1 319 ? 33.375 31.621 26.774 1.00 27.31 ? 319 ASN A CB 1 ATOM 2442 C CG . ASN A 1 319 ? 32.047 31.987 27.416 1.00 28.30 ? 319 ASN A CG 1 ATOM 2443 O OD1 . ASN A 1 319 ? 31.996 32.348 28.601 1.00 30.37 ? 319 ASN A OD1 1 ATOM 2444 N ND2 . ASN A 1 319 ? 30.962 31.884 26.648 1.00 25.64 ? 319 ASN A ND2 1 ATOM 2445 N N . LYS A 1 320 ? 35.631 29.777 25.871 1.00 28.22 ? 320 LYS A N 1 ATOM 2446 C CA . LYS A 1 320 ? 36.965 29.730 25.299 1.00 28.98 ? 320 LYS A CA 1 ATOM 2447 C C . LYS A 1 320 ? 37.245 28.355 24.672 1.00 28.40 ? 320 LYS A C 1 ATOM 2448 O O . LYS A 1 320 ? 38.136 27.625 25.111 1.00 28.37 ? 320 LYS A O 1 ATOM 2449 C CB . LYS A 1 320 ? 38.012 30.188 26.347 1.00 29.89 ? 320 LYS A CB 1 ATOM 2450 C CG A LYS A 1 320 ? 39.444 30.351 25.825 0.65 32.59 ? 320 LYS A CG 1 ATOM 2451 C CG B LYS A 1 320 ? 38.142 31.703 26.468 0.35 30.17 ? 320 LYS A CG 1 ATOM 2452 C CD A LYS A 1 320 ? 39.480 31.001 24.452 0.65 33.51 ? 320 LYS A CD 1 ATOM 2453 C CD B LYS A 1 320 ? 36.970 32.320 27.215 0.35 30.02 ? 320 LYS A CD 1 ATOM 2454 C CE A LYS A 1 320 ? 40.593 30.461 23.600 0.65 35.04 ? 320 LYS A CE 1 ATOM 2455 C CE B LYS A 1 320 ? 36.963 33.835 27.134 0.35 30.75 ? 320 LYS A CE 1 ATOM 2456 N NZ A LYS A 1 320 ? 41.958 31.037 23.871 0.65 38.04 ? 320 LYS A NZ 1 ATOM 2457 N NZ B LYS A 1 320 ? 35.762 34.389 27.815 0.35 30.27 ? 320 LYS A NZ 1 ATOM 2458 N N . TYR A 1 321 ? 36.461 28.032 23.632 1.00 27.57 ? 321 TYR A N 1 ATOM 2459 C CA . TYR A 1 321 ? 36.549 26.757 22.911 1.00 27.23 ? 321 TYR A CA 1 ATOM 2460 C C . TYR A 1 321 ? 37.898 26.611 22.222 1.00 28.07 ? 321 TYR A C 1 ATOM 2461 O O . TYR A 1 321 ? 38.377 25.490 22.057 1.00 28.23 ? 321 TYR A O 1 ATOM 2462 C CB . TYR A 1 321 ? 35.424 26.605 21.852 1.00 27.02 ? 321 TYR A CB 1 ATOM 2463 C CG . TYR A 1 321 ? 35.384 27.753 20.853 1.00 26.81 ? 321 TYR A CG 1 ATOM 2464 C CD1 . TYR A 1 321 ? 36.183 27.745 19.704 1.00 26.35 ? 321 TYR A CD1 1 ATOM 2465 C CD2 . TYR A 1 321 ? 34.579 28.862 21.088 1.00 25.71 ? 321 TYR A CD2 1 ATOM 2466 C CE1 . TYR A 1 321 ? 36.183 28.830 18.817 1.00 28.22 ? 321 TYR A CE1 1 ATOM 2467 C CE2 . TYR A 1 321 ? 34.563 29.931 20.220 1.00 26.84 ? 321 TYR A CE2 1 ATOM 2468 C CZ . TYR A 1 321 ? 35.367 29.915 19.085 1.00 28.86 ? 321 TYR A CZ 1 ATOM 2469 O OH . TYR A 1 321 ? 35.350 30.997 18.236 1.00 29.99 ? 321 TYR A OH 1 ATOM 2470 N N . GLN A 1 322 ? 38.497 27.724 21.798 1.00 28.85 ? 322 GLN A N 1 ATOM 2471 C CA . GLN A 1 322 ? 39.753 27.650 21.041 1.00 31.60 ? 322 GLN A CA 1 ATOM 2472 C C . GLN A 1 322 ? 40.843 27.047 21.936 1.00 31.08 ? 322 GLN A C 1 ATOM 2473 O O . GLN A 1 322 ? 41.546 26.111 21.528 1.00 31.03 ? 322 GLN A O 1 ATOM 2474 C CB . GLN A 1 322 ? 40.169 29.025 20.489 1.00 32.13 ? 322 GLN A CB 1 ATOM 2475 C CG . GLN A 1 322 ? 41.401 28.983 19.564 1.00 37.21 ? 322 GLN A CG 1 ATOM 2476 C CD . GLN A 1 322 ? 41.928 30.370 19.160 1.00 38.17 ? 322 GLN A CD 1 ATOM 2477 O OE1 . GLN A 1 322 ? 43.121 30.668 19.323 1.00 45.16 ? 322 GLN A OE1 1 ATOM 2478 N NE2 . GLN A 1 322 ? 41.039 31.216 18.620 1.00 42.57 ? 322 GLN A NE2 1 ATOM 2479 N N . GLN A 1 323 ? 40.952 27.578 23.159 1.00 31.07 ? 323 GLN A N 1 ATOM 2480 C CA . GLN A 1 323 ? 41.888 27.074 24.177 1.00 32.04 ? 323 GLN A CA 1 ATOM 2481 C C . GLN A 1 323 ? 41.613 25.605 24.535 1.00 29.96 ? 323 GLN A C 1 ATOM 2482 O O . GLN A 1 323 ? 42.539 24.787 24.555 1.00 30.45 ? 323 GLN A O 1 ATOM 2483 C CB . GLN A 1 323 ? 41.822 27.955 25.430 1.00 32.29 ? 323 GLN A CB 1 ATOM 2484 C CG . GLN A 1 323 ? 42.643 27.461 26.610 1.00 35.88 ? 323 GLN A CG 1 ATOM 2485 C CD . GLN A 1 323 ? 42.475 28.310 27.866 1.00 36.14 ? 323 GLN A CD 1 ATOM 2486 O OE1 . GLN A 1 323 ? 41.361 28.457 28.412 1.00 40.82 ? 323 GLN A OE1 1 ATOM 2487 N NE2 . GLN A 1 323 ? 43.584 28.855 28.346 1.00 39.22 ? 323 GLN A NE2 1 ATOM 2488 N N . PHE A 1 324 ? 40.346 25.276 24.800 1.00 27.81 ? 324 PHE A N 1 ATOM 2489 C CA . PHE A 1 324 ? 39.962 23.886 25.094 1.00 26.13 ? 324 PHE A CA 1 ATOM 2490 C C . PHE A 1 324 ? 40.364 22.929 23.964 1.00 25.60 ? 324 PHE A C 1 ATOM 2491 O O . PHE A 1 324 ? 41.011 21.901 24.211 1.00 25.22 ? 324 PHE A O 1 ATOM 2492 C CB . PHE A 1 324 ? 38.453 23.740 25.383 1.00 24.74 ? 324 PHE A CB 1 ATOM 2493 C CG . PHE A 1 324 ? 38.021 22.292 25.564 1.00 25.08 ? 324 PHE A CG 1 ATOM 2494 C CD1 . PHE A 1 324 ? 38.395 21.572 26.720 1.00 23.69 ? 324 PHE A CD1 1 ATOM 2495 C CD2 . PHE A 1 324 ? 37.309 21.631 24.564 1.00 22.77 ? 324 PHE A CD2 1 ATOM 2496 C CE1 . PHE A 1 324 ? 38.034 20.239 26.868 1.00 23.86 ? 324 PHE A CE1 1 ATOM 2497 C CE2 . PHE A 1 324 ? 36.934 20.300 24.713 1.00 22.36 ? 324 PHE A CE2 1 ATOM 2498 C CZ . PHE A 1 324 ? 37.299 19.598 25.852 1.00 22.67 ? 324 PHE A CZ 1 ATOM 2499 N N . ILE A 1 325 ? 39.969 23.259 22.732 1.00 24.75 ? 325 ILE A N 1 ATOM 2500 C CA . ILE A 1 325 ? 40.260 22.385 21.587 1.00 24.68 ? 325 ILE A CA 1 ATOM 2501 C C . ILE A 1 325 ? 41.761 22.252 21.387 1.00 25.18 ? 325 ILE A C 1 ATOM 2502 O O . ILE A 1 325 ? 42.266 21.146 21.208 1.00 25.52 ? 325 ILE A O 1 ATOM 2503 C CB . ILE A 1 325 ? 39.537 22.823 20.275 1.00 24.66 ? 325 ILE A CB 1 ATOM 2504 C CG1 . ILE A 1 325 ? 38.029 22.621 20.414 1.00 24.40 ? 325 ILE A CG1 1 ATOM 2505 C CG2 . ILE A 1 325 ? 40.042 22.009 19.065 1.00 24.30 ? 325 ILE A CG2 1 ATOM 2506 C CD1 . ILE A 1 325 ? 37.198 23.334 19.347 1.00 23.08 ? 325 ILE A CD1 1 ATOM 2507 N N . SER A 1 326 ? 42.478 23.367 21.468 1.00 25.92 ? 326 SER A N 1 ATOM 2508 C CA . SER A 1 326 ? 43.915 23.352 21.242 1.00 27.26 ? 326 SER A CA 1 ATOM 2509 C C . SER A 1 326 ? 44.616 22.481 22.294 1.00 27.79 ? 326 SER A C 1 ATOM 2510 O O . SER A 1 326 ? 45.453 21.646 21.942 1.00 28.00 ? 326 SER A O 1 ATOM 2511 C CB . SER A 1 326 ? 44.475 24.777 21.244 1.00 27.69 ? 326 SER A CB 1 ATOM 2512 O OG . SER A 1 326 ? 45.871 24.774 21.000 1.00 31.30 ? 326 SER A OG 1 ATOM 2513 N N . ILE A 1 327 ? 44.246 22.661 23.569 1.00 27.85 ? 327 ILE A N 1 ATOM 2514 C CA . ILE A 1 327 ? 44.874 21.934 24.683 1.00 28.34 ? 327 ILE A CA 1 ATOM 2515 C C . ILE A 1 327 ? 44.590 20.434 24.617 1.00 28.08 ? 327 ILE A C 1 ATOM 2516 O O . ILE A 1 327 ? 45.513 19.630 24.724 1.00 28.89 ? 327 ILE A O 1 ATOM 2517 C CB . ILE A 1 327 ? 44.521 22.549 26.061 1.00 28.75 ? 327 ILE A CB 1 ATOM 2518 C CG1 . ILE A 1 327 ? 45.331 23.835 26.249 1.00 30.66 ? 327 ILE A CG1 1 ATOM 2519 C CG2 . ILE A 1 327 ? 44.825 21.581 27.202 1.00 27.91 ? 327 ILE A CG2 1 ATOM 2520 C CD1 . ILE A 1 327 ? 44.920 24.653 27.417 1.00 33.89 ? 327 ILE A CD1 1 ATOM 2521 N N . LEU A 1 328 ? 43.335 20.065 24.390 1.00 26.62 ? 328 LEU A N 1 ATOM 2522 C CA . LEU A 1 328 ? 42.968 18.656 24.257 1.00 26.80 ? 328 LEU A CA 1 ATOM 2523 C C . LEU A 1 328 ? 43.683 18.002 23.069 1.00 27.34 ? 328 LEU A C 1 ATOM 2524 O O . LEU A 1 328 ? 44.235 16.904 23.192 1.00 28.64 ? 328 LEU A O 1 ATOM 2525 C CB . LEU A 1 328 ? 41.439 18.504 24.135 1.00 25.58 ? 328 LEU A CB 1 ATOM 2526 C CG . LEU A 1 328 ? 40.891 17.073 24.124 1.00 25.19 ? 328 LEU A CG 1 ATOM 2527 C CD1 . LEU A 1 328 ? 41.580 16.195 25.187 1.00 25.85 ? 328 LEU A CD1 1 ATOM 2528 C CD2 . LEU A 1 328 ? 39.366 17.052 24.277 1.00 24.52 ? 328 LEU A CD2 1 ATOM 2529 N N . THR A 1 329 ? 43.681 18.685 21.924 1.00 27.40 ? 329 THR A N 1 ATOM 2530 C CA . THR A 1 329 ? 44.431 18.220 20.764 1.00 27.92 ? 329 THR A CA 1 ATOM 2531 C C . THR A 1 329 ? 45.904 17.932 21.129 1.00 29.38 ? 329 THR A C 1 ATOM 2532 O O . THR A 1 329 ? 46.441 16.876 20.786 1.00 30.56 ? 329 THR A O 1 ATOM 2533 C CB . THR A 1 329 ? 44.313 19.220 19.577 1.00 27.99 ? 329 THR A CB 1 ATOM 2534 O OG1 . THR A 1 329 ? 42.930 19.401 19.246 1.00 26.56 ? 329 THR A OG1 1 ATOM 2535 C CG2 . THR A 1 329 ? 45.050 18.706 18.358 1.00 27.66 ? 329 THR A CG2 1 ATOM 2536 N N . GLY A 1 330 ? 46.545 18.865 21.829 1.00 30.17 ? 330 GLY A N 1 ATOM 2537 C CA . GLY A 1 330 ? 47.948 18.701 22.222 1.00 31.28 ? 330 GLY A CA 1 ATOM 2538 C C . GLY A 1 330 ? 48.158 17.481 23.105 1.00 32.08 ? 330 GLY A C 1 ATOM 2539 O O . GLY A 1 330 ? 49.088 16.714 22.888 1.00 32.84 ? 330 GLY A O 1 ATOM 2540 N N . HIS A 1 331 ? 47.284 17.302 24.098 1.00 31.30 ? 331 HIS A N 1 ATOM 2541 C CA . HIS A 1 331 ? 47.369 16.162 25.011 1.00 31.81 ? 331 HIS A CA 1 ATOM 2542 C C . HIS A 1 331 ? 47.221 14.829 24.277 1.00 31.72 ? 331 HIS A C 1 ATOM 2543 O O . HIS A 1 331 ? 47.922 13.867 24.584 1.00 32.53 ? 331 HIS A O 1 ATOM 2544 C CB . HIS A 1 331 ? 46.334 16.283 26.145 1.00 30.95 ? 331 HIS A CB 1 ATOM 2545 C CG . HIS A 1 331 ? 46.713 17.265 27.216 1.00 31.32 ? 331 HIS A CG 1 ATOM 2546 N ND1 . HIS A 1 331 ? 45.778 17.954 27.961 1.00 31.91 ? 331 HIS A ND1 1 ATOM 2547 C CD2 . HIS A 1 331 ? 47.923 17.674 27.668 1.00 32.81 ? 331 HIS A CD2 1 ATOM 2548 C CE1 . HIS A 1 331 ? 46.394 18.748 28.818 1.00 32.06 ? 331 HIS A CE1 1 ATOM 2549 N NE2 . HIS A 1 331 ? 47.698 18.599 28.660 1.00 33.73 ? 331 HIS A NE2 1 ATOM 2550 N N . VAL A 1 332 ? 46.312 14.775 23.305 1.00 30.99 ? 332 VAL A N 1 ATOM 2551 C CA . VAL A 1 332 ? 46.161 13.579 22.481 1.00 30.65 ? 332 VAL A CA 1 ATOM 2552 C C . VAL A 1 332 ? 47.385 13.382 21.572 1.00 32.10 ? 332 VAL A C 1 ATOM 2553 O O . VAL A 1 332 ? 47.908 12.264 21.453 1.00 32.82 ? 332 VAL A O 1 ATOM 2554 C CB . VAL A 1 332 ? 44.833 13.602 21.682 1.00 29.77 ? 332 VAL A CB 1 ATOM 2555 C CG1 . VAL A 1 332 ? 44.745 12.409 20.738 1.00 28.46 ? 332 VAL A CG1 1 ATOM 2556 C CG2 . VAL A 1 332 ? 43.636 13.617 22.655 1.00 27.82 ? 332 VAL A CG2 1 ATOM 2557 N N . ASN A 1 333 ? 47.852 14.465 20.954 1.00 32.59 ? 333 ASN A N 1 ATOM 2558 C CA . ASN A 1 333 ? 49.039 14.406 20.084 1.00 34.30 ? 333 ASN A CA 1 ATOM 2559 C C . ASN A 1 333 ? 50.291 13.952 20.829 1.00 35.79 ? 333 ASN A C 1 ATOM 2560 O O . ASN A 1 333 ? 51.141 13.277 20.261 1.00 36.76 ? 333 ASN A O 1 ATOM 2561 C CB . ASN A 1 333 ? 49.297 15.749 19.383 1.00 34.03 ? 333 ASN A CB 1 ATOM 2562 C CG . ASN A 1 333 ? 48.398 15.968 18.167 1.00 34.19 ? 333 ASN A CG 1 ATOM 2563 O OD1 . ASN A 1 333 ? 47.814 15.021 17.619 1.00 33.18 ? 333 ASN A OD1 1 ATOM 2564 N ND2 . ASN A 1 333 ? 48.287 17.222 17.738 1.00 31.94 ? 333 ASN A ND2 1 ATOM 2565 N N . GLY A 1 334 ? 50.393 14.321 22.102 1.00 36.29 ? 334 GLY A N 1 ATOM 2566 C CA . GLY A 1 334 ? 51.532 13.918 22.927 1.00 38.21 ? 334 GLY A CA 1 ATOM 2567 C C . GLY A 1 334 ? 51.339 12.625 23.706 1.00 38.61 ? 334 GLY A C 1 ATOM 2568 O O . GLY A 1 334 ? 52.192 12.256 24.507 1.00 39.97 ? 334 GLY A O 1 ATOM 2569 N N . GLY A 1 335 ? 50.220 11.937 23.485 1.00 37.64 ? 335 GLY A N 1 ATOM 2570 C CA . GLY A 1 335 ? 49.973 10.641 24.125 1.00 37.82 ? 335 GLY A CA 1 ATOM 2571 C C . GLY A 1 335 ? 49.565 10.669 25.591 1.00 38.12 ? 335 GLY A C 1 ATOM 2572 O O . GLY A 1 335 ? 49.456 9.616 26.228 1.00 38.73 ? 335 GLY A O 1 ATOM 2573 N N . VAL A 1 336 ? 49.304 11.867 26.118 1.00 37.10 ? 336 VAL A N 1 ATOM 2574 C CA . VAL A 1 336 ? 48.951 12.056 27.524 1.00 36.79 ? 336 VAL A CA 1 ATOM 2575 C C . VAL A 1 336 ? 47.507 11.606 27.790 1.00 35.37 ? 336 VAL A C 1 ATOM 2576 O O . VAL A 1 336 ? 47.190 11.112 28.876 1.00 35.09 ? 336 VAL A O 1 ATOM 2577 C CB . VAL A 1 336 ? 49.184 13.532 27.967 1.00 36.84 ? 336 VAL A CB 1 ATOM 2578 C CG1 . VAL A 1 336 ? 48.669 13.772 29.362 1.00 37.56 ? 336 VAL A CG1 1 ATOM 2579 C CG2 . VAL A 1 336 ? 50.675 13.888 27.886 1.00 38.95 ? 336 VAL A CG2 1 ATOM 2580 N N . ILE A 1 337 ? 46.646 11.791 26.786 1.00 33.96 ? 337 ILE A N 1 ATOM 2581 C CA . ILE A 1 337 ? 45.294 11.230 26.768 1.00 32.42 ? 337 ILE A CA 1 ATOM 2582 C C . ILE A 1 337 ? 45.206 10.245 25.588 1.00 32.28 ? 337 ILE A C 1 ATOM 2583 O O . ILE A 1 337 ? 45.478 10.621 24.441 1.00 32.26 ? 337 ILE A O 1 ATOM 2584 C CB . ILE A 1 337 ? 44.222 12.335 26.638 1.00 30.93 ? 337 ILE A CB 1 ATOM 2585 C CG1 . ILE A 1 337 ? 44.216 13.214 27.898 1.00 31.34 ? 337 ILE A CG1 1 ATOM 2586 C CG2 . ILE A 1 337 ? 42.836 11.727 26.379 1.00 29.06 ? 337 ILE A CG2 1 ATOM 2587 C CD1 . ILE A 1 337 ? 43.456 14.522 27.741 1.00 30.07 ? 337 ILE A CD1 1 ATOM 2588 N N . PRO A 1 338 ? 44.833 8.979 25.860 1.00 32.14 ? 338 PRO A N 1 ATOM 2589 C CA . PRO A 1 338 ? 44.853 8.003 24.773 1.00 32.12 ? 338 PRO A CA 1 ATOM 2590 C C . PRO A 1 338 ? 43.625 8.144 23.850 1.00 31.77 ? 338 PRO A C 1 ATOM 2591 O O . PRO A 1 338 ? 42.576 8.655 24.271 1.00 30.04 ? 338 PRO A O 1 ATOM 2592 C CB . PRO A 1 338 ? 44.821 6.673 25.510 1.00 32.75 ? 338 PRO A CB 1 ATOM 2593 C CG . PRO A 1 338 ? 44.041 6.967 26.762 1.00 32.15 ? 338 PRO A CG 1 ATOM 2594 C CD . PRO A 1 338 ? 44.378 8.384 27.130 1.00 32.08 ? 338 PRO A CD 1 ATOM 2595 N N . MET A 1 339 ? 43.781 7.699 22.605 1.00 31.94 ? 339 MET A N 1 ATOM 2596 C CA . MET A 1 339 ? 42.689 7.677 21.650 1.00 32.03 ? 339 MET A CA 1 ATOM 2597 C C . MET A 1 339 ? 41.480 6.928 22.150 1.00 31.18 ? 339 MET A C 1 ATOM 2598 O O . MET A 1 339 ? 40.351 7.325 21.867 1.00 30.14 ? 339 MET A O 1 ATOM 2599 C CB . MET A 1 339 ? 43.124 7.085 20.312 1.00 33.26 ? 339 MET A CB 1 ATOM 2600 C CG . MET A 1 339 ? 43.384 8.139 19.280 1.00 35.73 ? 339 MET A CG 1 ATOM 2601 S SD . MET A 1 339 ? 41.971 9.211 18.922 1.00 39.92 ? 339 MET A SD 1 ATOM 2602 C CE . MET A 1 339 ? 42.906 10.691 18.675 1.00 36.54 ? 339 MET A CE 1 ATOM 2603 N N . SER A 1 340 ? 41.709 5.842 22.882 1.00 31.70 ? 340 SER A N 1 ATOM 2604 C CA . SER A 1 340 ? 40.599 5.067 23.433 1.00 31.50 ? 340 SER A CA 1 ATOM 2605 C C . SER A 1 340 ? 39.677 5.941 24.289 1.00 30.59 ? 340 SER A C 1 ATOM 2606 O O . SER A 1 340 ? 38.457 5.747 24.298 1.00 30.11 ? 340 SER A O 1 ATOM 2607 C CB . SER A 1 340 ? 41.112 3.856 24.217 1.00 32.69 ? 340 SER A CB 1 ATOM 2608 O OG . SER A 1 340 ? 41.730 4.243 25.425 1.00 32.48 ? 340 SER A OG 1 ATOM 2609 N N . ARG A 1 341 ? 40.258 6.915 24.991 1.00 30.27 ? 341 ARG A N 1 ATOM 2610 C CA . ARG A 1 341 ? 39.471 7.810 25.848 1.00 29.21 ? 341 ARG A CA 1 ATOM 2611 C C . ARG A 1 341 ? 38.633 8.762 24.992 1.00 27.96 ? 341 ARG A C 1 ATOM 2612 O O . ARG A 1 341 ? 37.430 8.900 25.204 1.00 27.49 ? 341 ARG A O 1 ATOM 2613 C CB . ARG A 1 341 ? 40.376 8.558 26.840 1.00 29.38 ? 341 ARG A CB 1 ATOM 2614 C CG . ARG A 1 341 ? 39.660 9.500 27.816 1.00 28.21 ? 341 ARG A CG 1 ATOM 2615 C CD . ARG A 1 341 ? 38.812 8.776 28.884 1.00 28.76 ? 341 ARG A CD 1 ATOM 2616 N NE . ARG A 1 341 ? 37.418 8.570 28.459 1.00 27.08 ? 341 ARG A NE 1 ATOM 2617 C CZ . ARG A 1 341 ? 36.483 9.518 28.401 1.00 24.72 ? 341 ARG A CZ 1 ATOM 2618 N NH1 . ARG A 1 341 ? 35.256 9.209 27.999 1.00 23.35 ? 341 ARG A NH1 1 ATOM 2619 N NH2 . ARG A 1 341 ? 36.762 10.775 28.737 1.00 24.23 ? 341 ARG A NH2 1 ATOM 2620 N N . ILE A 1 342 ? 39.269 9.387 24.001 1.00 27.87 ? 342 ILE A N 1 ATOM 2621 C CA . ILE A 1 342 ? 38.564 10.221 23.023 1.00 26.65 ? 342 ILE A CA 1 ATOM 2622 C C . ILE A 1 342 ? 37.432 9.468 22.320 1.00 26.38 ? 342 ILE A C 1 ATOM 2623 O O . ILE A 1 342 ? 36.332 10.008 22.179 1.00 26.08 ? 342 ILE A O 1 ATOM 2624 C CB . ILE A 1 342 ? 39.538 10.838 21.966 1.00 26.49 ? 342 ILE A CB 1 ATOM 2625 C CG1 . ILE A 1 342 ? 40.614 11.706 22.659 1.00 26.76 ? 342 ILE A CG1 1 ATOM 2626 C CG2 . ILE A 1 342 ? 38.778 11.641 20.915 1.00 25.39 ? 342 ILE A CG2 1 ATOM 2627 C CD1 . ILE A 1 342 ? 40.055 12.858 23.508 1.00 25.59 ? 342 ILE A CD1 1 ATOM 2628 N N . ASP A 1 343 ? 37.715 8.236 21.883 1.00 27.29 ? 343 ASP A N 1 ATOM 2629 C CA . ASP A 1 343 ? 36.747 7.394 21.151 1.00 27.02 ? 343 ASP A CA 1 ATOM 2630 C C . ASP A 1 343 ? 35.553 6.984 22.021 1.00 27.17 ? 343 ASP A C 1 ATOM 2631 O O . ASP A 1 343 ? 34.429 6.855 21.523 1.00 26.63 ? 343 ASP A O 1 ATOM 2632 C CB . ASP A 1 343 ? 37.427 6.141 20.589 1.00 27.76 ? 343 ASP A CB 1 ATOM 2633 C CG . ASP A 1 343 ? 38.283 6.428 19.364 1.00 28.59 ? 343 ASP A CG 1 ATOM 2634 O OD1 . ASP A 1 343 ? 38.320 7.586 18.899 1.00 27.63 ? 343 ASP A OD1 1 ATOM 2635 O OD2 . ASP A 1 343 ? 38.930 5.488 18.859 1.00 29.36 ? 343 ASP A OD2 1 ATOM 2636 N N . ASP A 1 344 ? 35.801 6.773 23.317 1.00 27.20 ? 344 ASP A N 1 ATOM 2637 C CA . ASP A 1 344 ? 34.725 6.456 24.244 1.00 27.28 ? 344 ASP A CA 1 ATOM 2638 C C . ASP A 1 344 ? 33.785 7.658 24.402 1.00 26.15 ? 344 ASP A C 1 ATOM 2639 O O . ASP A 1 344 ? 32.558 7.509 24.340 1.00 26.18 ? 344 ASP A O 1 ATOM 2640 C CB . ASP A 1 344 ? 35.289 5.991 25.592 1.00 27.64 ? 344 ASP A CB 1 ATOM 2641 C CG . ASP A 1 344 ? 34.221 5.850 26.662 1.00 27.44 ? 344 ASP A CG 1 ATOM 2642 O OD1 . ASP A 1 344 ? 33.401 4.911 26.576 1.00 28.42 ? 344 ASP A OD1 1 ATOM 2643 O OD2 . ASP A 1 344 ? 34.211 6.674 27.603 1.00 26.20 ? 344 ASP A OD2 1 ATOM 2644 N N . ALA A 1 345 ? 34.364 8.845 24.588 1.00 25.83 ? 345 ALA A N 1 ATOM 2645 C CA . ALA A 1 345 ? 33.588 10.072 24.770 1.00 24.46 ? 345 ALA A CA 1 ATOM 2646 C C . ALA A 1 345 ? 32.707 10.331 23.551 1.00 24.07 ? 345 ALA A C 1 ATOM 2647 O O . ALA A 1 345 ? 31.511 10.609 23.696 1.00 23.10 ? 345 ALA A O 1 ATOM 2648 C CB . ALA A 1 345 ? 34.508 11.261 25.025 1.00 24.16 ? 345 ALA A CB 1 ATOM 2649 N N . VAL A 1 346 ? 33.310 10.232 22.363 1.00 24.12 ? 346 VAL A N 1 ATOM 2650 C CA . VAL A 1 346 ? 32.611 10.425 21.092 1.00 23.78 ? 346 VAL A CA 1 ATOM 2651 C C . VAL A 1 346 ? 31.579 9.314 20.845 1.00 24.10 ? 346 VAL A C 1 ATOM 2652 O O . VAL A 1 346 ? 30.492 9.596 20.363 1.00 24.09 ? 346 VAL A O 1 ATOM 2653 C CB . VAL A 1 346 ? 33.579 10.581 19.872 1.00 23.95 ? 346 VAL A CB 1 ATOM 2654 C CG1 . VAL A 1 346 ? 32.791 10.783 18.564 1.00 23.75 ? 346 VAL A CG1 1 ATOM 2655 C CG2 . VAL A 1 346 ? 34.521 11.759 20.076 1.00 22.49 ? 346 VAL A CG2 1 ATOM 2656 N N . THR A 1 347 ? 31.896 8.072 21.204 1.00 24.49 ? 347 THR A N 1 ATOM 2657 C CA . THR A 1 347 ? 30.898 6.989 21.109 1.00 24.88 ? 347 THR A CA 1 ATOM 2658 C C . THR A 1 347 ? 29.615 7.323 21.890 1.00 24.12 ? 347 THR A C 1 ATOM 2659 O O . THR A 1 347 ? 28.514 7.149 21.387 1.00 24.33 ? 347 THR A O 1 ATOM 2660 C CB . THR A 1 347 ? 31.478 5.636 21.593 1.00 25.52 ? 347 THR A CB 1 ATOM 2661 O OG1 . THR A 1 347 ? 32.484 5.218 20.678 1.00 26.13 ? 347 THR A OG1 1 ATOM 2662 C CG2 . THR A 1 347 ? 30.401 4.552 21.661 1.00 26.50 ? 347 THR A CG2 1 ATOM 2663 N N . ARG A 1 348 ? 29.777 7.832 23.106 1.00 24.04 ? 348 ARG A N 1 ATOM 2664 C CA . ARG A 1 348 ? 28.646 8.106 23.998 1.00 23.53 ? 348 ARG A CA 1 ATOM 2665 C C . ARG A 1 348 ? 27.805 9.290 23.531 1.00 23.36 ? 348 ARG A C 1 ATOM 2666 O O . ARG A 1 348 ? 26.571 9.257 23.653 1.00 23.20 ? 348 ARG A O 1 ATOM 2667 C CB . ARG A 1 348 ? 29.147 8.336 25.418 1.00 23.65 ? 348 ARG A CB 1 ATOM 2668 C CG . ARG A 1 348 ? 29.737 7.082 26.027 1.00 23.36 ? 348 ARG A CG 1 ATOM 2669 C CD . ARG A 1 348 ? 30.544 7.401 27.258 1.00 25.33 ? 348 ARG A CD 1 ATOM 2670 N NE . ARG A 1 348 ? 30.963 6.155 27.885 1.00 25.83 ? 348 ARG A NE 1 ATOM 2671 C CZ . ARG A 1 348 ? 30.220 5.490 28.759 1.00 24.91 ? 348 ARG A CZ 1 ATOM 2672 N NH1 . ARG A 1 348 ? 29.041 5.970 29.113 1.00 23.68 ? 348 ARG A NH1 1 ATOM 2673 N NH2 . ARG A 1 348 ? 30.658 4.347 29.271 1.00 26.46 ? 348 ARG A NH2 1 ATOM 2674 N N . ILE A 1 349 ? 28.477 10.312 22.992 1.00 22.58 ? 349 ILE A N 1 ATOM 2675 C CA . ILE A 1 349 ? 27.822 11.500 22.469 1.00 22.29 ? 349 ILE A CA 1 ATOM 2676 C C . ILE A 1 349 ? 26.993 11.154 21.231 1.00 22.81 ? 349 ILE A C 1 ATOM 2677 O O . ILE A 1 349 ? 25.823 11.522 21.135 1.00 22.84 ? 349 ILE A O 1 ATOM 2678 C CB . ILE A 1 349 ? 28.855 12.642 22.179 1.00 22.38 ? 349 ILE A CB 1 ATOM 2679 C CG1 . ILE A 1 349 ? 29.545 13.084 23.494 1.00 21.68 ? 349 ILE A CG1 1 ATOM 2680 C CG2 . ILE A 1 349 ? 28.183 13.828 21.467 1.00 21.01 ? 349 ILE A CG2 1 ATOM 2681 C CD1 . ILE A 1 349 ? 30.719 14.042 23.299 1.00 21.72 ? 349 ILE A CD1 1 ATOM 2682 N N . LEU A 1 350 ? 27.612 10.454 20.285 1.00 23.18 ? 350 LEU A N 1 ATOM 2683 C CA . LEU A 1 350 ? 26.920 9.946 19.115 1.00 23.41 ? 350 LEU A CA 1 ATOM 2684 C C . LEU A 1 350 ? 25.801 8.971 19.488 1.00 23.60 ? 350 LEU A C 1 ATOM 2685 O O . LEU A 1 350 ? 24.708 9.046 18.921 1.00 24.02 ? 350 LEU A O 1 ATOM 2686 C CB . LEU A 1 350 ? 27.912 9.273 18.165 1.00 24.01 ? 350 LEU A CB 1 ATOM 2687 C CG . LEU A 1 350 ? 28.991 10.167 17.526 1.00 23.67 ? 350 LEU A CG 1 ATOM 2688 C CD1 . LEU A 1 350 ? 29.839 9.284 16.612 1.00 21.59 ? 350 LEU A CD1 1 ATOM 2689 C CD2 . LEU A 1 350 ? 28.376 11.345 16.759 1.00 20.97 ? 350 LEU A CD2 1 ATOM 2690 N N . ARG A 1 351 ? 26.064 8.053 20.421 1.00 23.69 ? 351 ARG A N 1 ATOM 2691 C CA . ARG A 1 351 ? 24.998 7.146 20.887 1.00 24.43 ? 351 ARG A CA 1 ATOM 2692 C C . ARG A 1 351 ? 23.738 7.932 21.259 1.00 23.96 ? 351 ARG A C 1 ATOM 2693 O O . ARG A 1 351 ? 22.638 7.615 20.793 1.00 24.98 ? 351 ARG A O 1 ATOM 2694 C CB . ARG A 1 351 ? 25.444 6.278 22.066 1.00 24.47 ? 351 ARG A CB 1 ATOM 2695 C CG . ARG A 1 351 ? 24.398 5.236 22.452 1.00 25.94 ? 351 ARG A CG 1 ATOM 2696 C CD . ARG A 1 351 ? 24.863 4.335 23.573 1.00 26.97 ? 351 ARG A CD 1 ATOM 2697 N NE . ARG A 1 351 ? 25.918 3.440 23.123 1.00 27.49 ? 351 ARG A NE 1 ATOM 2698 C CZ . ARG A 1 351 ? 27.147 3.414 23.623 1.00 28.63 ? 351 ARG A CZ 1 ATOM 2699 N NH1 . ARG A 1 351 ? 27.490 4.218 24.624 1.00 28.06 ? 351 ARG A NH1 1 ATOM 2700 N NH2 . ARG A 1 351 ? 28.031 2.561 23.134 1.00 28.99 ? 351 ARG A NH2 1 ATOM 2701 N N . VAL A 1 352 ? 23.903 8.972 22.075 1.00 23.03 ? 352 VAL A N 1 ATOM 2702 C CA . VAL A 1 352 ? 22.762 9.776 22.500 1.00 22.68 ? 352 VAL A CA 1 ATOM 2703 C C . VAL A 1 352 ? 22.079 10.452 21.300 1.00 22.70 ? 352 VAL A C 1 ATOM 2704 O O . VAL A 1 352 ? 20.866 10.368 21.149 1.00 23.02 ? 352 VAL A O 1 ATOM 2705 C CB . VAL A 1 352 ? 23.166 10.779 23.620 1.00 21.96 ? 352 VAL A CB 1 ATOM 2706 C CG1 . VAL A 1 352 ? 22.048 11.759 23.910 1.00 20.95 ? 352 VAL A CG1 1 ATOM 2707 C CG2 . VAL A 1 352 ? 23.553 10.032 24.890 1.00 20.97 ? 352 VAL A CG2 1 ATOM 2708 N N . LYS A 1 353 ? 22.876 11.075 20.427 1.00 23.13 ? 353 LYS A N 1 ATOM 2709 C CA . LYS A 1 353 ? 22.362 11.783 19.232 1.00 22.86 ? 353 LYS A CA 1 ATOM 2710 C C . LYS A 1 353 ? 21.594 10.882 18.264 1.00 23.71 ? 353 LYS A C 1 ATOM 2711 O O . LYS A 1 353 ? 20.487 11.243 17.811 1.00 23.72 ? 353 LYS A O 1 ATOM 2712 C CB . LYS A 1 353 ? 23.497 12.492 18.490 1.00 22.44 ? 353 LYS A CB 1 ATOM 2713 C CG . LYS A 1 353 ? 24.067 13.698 19.227 1.00 20.81 ? 353 LYS A CG 1 ATOM 2714 C CD . LYS A 1 353 ? 25.114 14.401 18.362 1.00 19.54 ? 353 LYS A CD 1 ATOM 2715 C CE . LYS A 1 353 ? 25.580 15.687 19.011 1.00 19.89 ? 353 LYS A CE 1 ATOM 2716 N NZ . LYS A 1 353 ? 26.491 16.455 18.110 1.00 19.35 ? 353 LYS A NZ 1 ATOM 2717 N N . PHE A 1 354 ? 22.173 9.724 17.950 1.00 23.80 ? 354 PHE A N 1 ATOM 2718 C CA . PHE A 1 354 ? 21.508 8.735 17.088 1.00 24.65 ? 354 PHE A CA 1 ATOM 2719 C C . PHE A 1 354 ? 20.241 8.190 17.753 1.00 24.74 ? 354 PHE A C 1 ATOM 2720 O O . PHE A 1 354 ? 19.214 8.034 17.098 1.00 25.41 ? 354 PHE A O 1 ATOM 2721 C CB . PHE A 1 354 ? 22.427 7.548 16.749 1.00 24.68 ? 354 PHE A CB 1 ATOM 2722 C CG . PHE A 1 354 ? 23.412 7.815 15.634 1.00 25.05 ? 354 PHE A CG 1 ATOM 2723 C CD1 . PHE A 1 354 ? 24.781 7.801 15.886 1.00 23.43 ? 354 PHE A CD1 1 ATOM 2724 C CD2 . PHE A 1 354 ? 22.975 8.072 14.334 1.00 24.76 ? 354 PHE A CD2 1 ATOM 2725 C CE1 . PHE A 1 354 ? 25.698 8.046 14.874 1.00 23.40 ? 354 PHE A CE1 1 ATOM 2726 C CE2 . PHE A 1 354 ? 23.895 8.321 13.308 1.00 25.00 ? 354 PHE A CE2 1 ATOM 2727 C CZ . PHE A 1 354 ? 25.257 8.298 13.586 1.00 23.56 ? 354 PHE A CZ 1 ATOM 2728 N N . THR A 1 355 ? 20.326 7.903 19.052 1.00 24.50 ? 355 THR A N 1 ATOM 2729 C CA . THR A 1 355 ? 19.212 7.280 19.790 1.00 24.58 ? 355 THR A CA 1 ATOM 2730 C C . THR A 1 355 ? 17.981 8.190 19.778 1.00 24.41 ? 355 THR A C 1 ATOM 2731 O O . THR A 1 355 ? 16.851 7.726 19.588 1.00 24.82 ? 355 THR A O 1 ATOM 2732 C CB . THR A 1 355 ? 19.620 6.942 21.258 1.00 24.34 ? 355 THR A CB 1 ATOM 2733 O OG1 . THR A 1 355 ? 20.642 5.943 21.246 1.00 24.43 ? 355 THR A OG1 1 ATOM 2734 C CG2 . THR A 1 355 ? 18.437 6.429 22.081 1.00 23.59 ? 355 THR A CG2 1 ATOM 2735 N N . MET A 1 356 ? 18.209 9.486 19.962 1.00 23.82 ? 356 MET A N 1 ATOM 2736 C CA . MET A 1 356 ? 17.107 10.429 20.133 1.00 23.78 ? 356 MET A CA 1 ATOM 2737 C C . MET A 1 356 ? 16.468 10.858 18.813 1.00 22.88 ? 356 MET A C 1 ATOM 2738 O O . MET A 1 356 ? 15.480 11.600 18.810 1.00 23.88 ? 356 MET A O 1 ATOM 2739 C CB . MET A 1 356 ? 17.580 11.646 20.914 1.00 23.03 ? 356 MET A CB 1 ATOM 2740 C CG . MET A 1 356 ? 18.579 12.508 20.150 1.00 24.04 ? 356 MET A CG 1 ATOM 2741 S SD . MET A 1 356 ? 19.262 13.798 21.174 1.00 23.99 ? 356 MET A SD 1 ATOM 2742 C CE . MET A 1 356 ? 19.686 12.870 22.627 1.00 31.70 ? 356 MET A CE 1 ATOM 2743 N N . GLY A 1 357 ? 17.032 10.399 17.703 1.00 22.23 ? 357 GLY A N 1 ATOM 2744 C CA . GLY A 1 357 ? 16.525 10.750 16.378 1.00 20.39 ? 357 GLY A CA 1 ATOM 2745 C C . GLY A 1 357 ? 17.113 12.007 15.746 1.00 18.33 ? 357 GLY A C 1 ATOM 2746 O O . GLY A 1 357 ? 16.615 12.455 14.691 1.00 18.60 ? 357 GLY A O 1 ATOM 2747 N N . LEU A 1 358 ? 18.181 12.546 16.342 1.00 29.58 ? 358 LEU A N 1 ATOM 2748 C CA . LEU A 1 358 ? 18.730 13.846 15.949 1.00 27.65 ? 358 LEU A CA 1 ATOM 2749 C C . LEU A 1 358 ? 19.231 13.891 14.488 1.00 26.86 ? 358 LEU A C 1 ATOM 2750 O O . LEU A 1 358 ? 19.156 14.928 13.849 1.00 25.69 ? 358 LEU A O 1 ATOM 2751 C CB . LEU A 1 358 ? 19.885 14.237 16.874 1.00 26.85 ? 358 LEU A CB 1 ATOM 2752 C CG . LEU A 1 358 ? 20.060 15.595 17.553 1.00 28.05 ? 358 LEU A CG 1 ATOM 2753 C CD1 . LEU A 1 358 ? 21.541 15.928 17.654 1.00 24.76 ? 358 LEU A CD1 1 ATOM 2754 C CD2 . LEU A 1 358 ? 19.232 16.760 16.995 1.00 24.80 ? 358 LEU A CD2 1 ATOM 2755 N N . PHE A 1 359 ? 19.782 12.781 13.996 1.00 26.39 ? 359 PHE A N 1 ATOM 2756 C CA . PHE A 1 359 ? 20.234 12.704 12.601 1.00 26.77 ? 359 PHE A CA 1 ATOM 2757 C C . PHE A 1 359 ? 19.054 12.696 11.628 1.00 26.89 ? 359 PHE A C 1 ATOM 2758 O O . PHE A 1 359 ? 19.200 13.123 10.494 1.00 27.59 ? 359 PHE A O 1 ATOM 2759 C CB . PHE A 1 359 ? 21.097 11.476 12.370 1.00 26.14 ? 359 PHE A CB 1 ATOM 2760 C CG . PHE A 1 359 ? 22.514 11.601 12.881 1.00 25.80 ? 359 PHE A CG 1 ATOM 2761 C CD1 . PHE A 1 359 ? 22.796 11.531 14.253 1.00 25.37 ? 359 PHE A CD1 1 ATOM 2762 C CD2 . PHE A 1 359 ? 23.576 11.751 11.981 1.00 25.44 ? 359 PHE A CD2 1 ATOM 2763 C CE1 . PHE A 1 359 ? 24.115 11.623 14.728 1.00 26.56 ? 359 PHE A CE1 1 ATOM 2764 C CE2 . PHE A 1 359 ? 24.897 11.841 12.435 1.00 25.01 ? 359 PHE A CE2 1 ATOM 2765 C CZ . PHE A 1 359 ? 25.171 11.776 13.811 1.00 25.71 ? 359 PHE A CZ 1 ATOM 2766 N N . GLU A 1 360 ? 17.894 12.205 12.075 1.00 26.92 ? 360 GLU A N 1 ATOM 2767 C CA . GLU A 1 360 ? 16.679 12.172 11.250 1.00 26.74 ? 360 GLU A CA 1 ATOM 2768 C C . GLU A 1 360 ? 15.874 13.443 11.349 1.00 26.56 ? 360 GLU A C 1 ATOM 2769 O O . GLU A 1 360 ? 15.255 13.866 10.379 1.00 26.65 ? 360 GLU A O 1 ATOM 2770 C CB . GLU A 1 360 ? 15.788 10.979 11.617 1.00 26.90 ? 360 GLU A CB 1 ATOM 2771 C CG . GLU A 1 360 ? 16.246 9.672 11.001 1.00 26.64 ? 360 GLU A CG 1 ATOM 2772 C CD . GLU A 1 360 ? 17.628 9.241 11.470 1.00 26.89 ? 360 GLU A CD 1 ATOM 2773 O OE1 . GLU A 1 360 ? 17.749 8.702 12.596 1.00 27.16 ? 360 GLU A OE1 1 ATOM 2774 O OE2 . GLU A 1 360 ? 18.599 9.427 10.699 1.00 27.10 ? 360 GLU A OE2 1 ATOM 2775 N N . ASN A 1 361 ? 15.873 14.057 12.527 1.00 26.61 ? 361 ASN A N 1 ATOM 2776 C CA . ASN A 1 361 ? 15.169 15.320 12.724 1.00 25.97 ? 361 ASN A CA 1 ATOM 2777 C C . ASN A 1 361 ? 16.060 16.374 13.392 1.00 26.01 ? 361 ASN A C 1 ATOM 2778 O O . ASN A 1 361 ? 15.858 16.705 14.560 1.00 25.35 ? 361 ASN A O 1 ATOM 2779 C CB . ASN A 1 361 ? 13.882 15.080 13.521 1.00 26.42 ? 361 ASN A CB 1 ATOM 2780 C CG . ASN A 1 361 ? 12.804 14.400 12.693 1.00 25.81 ? 361 ASN A CG 1 ATOM 2781 O OD1 . ASN A 1 361 ? 12.072 15.053 11.945 1.00 27.52 ? 361 ASN A OD1 1 ATOM 2782 N ND2 . ASN A 1 361 ? 12.703 13.090 12.824 1.00 25.09 ? 361 ASN A ND2 1 ATOM 2783 N N . PRO A 1 362 ? 17.077 16.877 12.656 1.00 25.84 ? 362 PRO A N 1 ATOM 2784 C CA . PRO A 1 362 ? 18.000 17.901 13.191 1.00 25.39 ? 362 PRO A CA 1 ATOM 2785 C C . PRO A 1 362 ? 17.420 19.306 13.300 1.00 25.12 ? 362 PRO A C 1 ATOM 2786 O O . PRO A 1 362 ? 17.969 20.142 14.027 1.00 24.47 ? 362 PRO A O 1 ATOM 2787 C CB . PRO A 1 362 ? 19.153 17.890 12.187 1.00 25.50 ? 362 PRO A CB 1 ATOM 2788 C CG . PRO A 1 362 ? 18.538 17.399 10.901 1.00 25.93 ? 362 PRO A CG 1 ATOM 2789 C CD . PRO A 1 362 ? 17.451 16.449 11.289 1.00 25.49 ? 362 PRO A CD 1 ATOM 2790 N N . TYR A 1 363 ? 16.336 19.566 12.572 1.00 25.12 ? 363 TYR A N 1 ATOM 2791 C CA . TYR A 1 363 ? 15.733 20.893 12.540 1.00 25.81 ? 363 TYR A CA 1 ATOM 2792 C C . TYR A 1 363 ? 14.436 20.981 13.351 1.00 25.56 ? 363 TYR A C 1 ATOM 2793 O O . TYR A 1 363 ? 13.796 19.967 13.636 1.00 25.04 ? 363 TYR A O 1 ATOM 2794 C CB . TYR A 1 363 ? 15.521 21.371 11.086 1.00 26.75 ? 363 TYR A CB 1 ATOM 2795 C CG . TYR A 1 363 ? 16.818 21.508 10.325 1.00 27.36 ? 363 TYR A CG 1 ATOM 2796 C CD1 . TYR A 1 363 ? 17.207 20.541 9.393 1.00 28.31 ? 363 TYR A CD1 1 ATOM 2797 C CD2 . TYR A 1 363 ? 17.677 22.590 10.564 1.00 27.23 ? 363 TYR A CD2 1 ATOM 2798 C CE1 . TYR A 1 363 ? 18.424 20.655 8.696 1.00 29.63 ? 363 TYR A CE1 1 ATOM 2799 C CE2 . TYR A 1 363 ? 18.885 22.719 9.883 1.00 28.81 ? 363 TYR A CE2 1 ATOM 2800 C CZ . TYR A 1 363 ? 19.256 21.752 8.950 1.00 29.71 ? 363 TYR A CZ 1 ATOM 2801 O OH . TYR A 1 363 ? 20.456 21.889 8.270 1.00 29.81 ? 363 TYR A OH 1 ATOM 2802 N N . ALA A 1 364 ? 14.077 22.212 13.713 1.00 25.49 ? 364 ALA A N 1 ATOM 2803 C CA . ALA A 1 364 ? 12.910 22.480 14.531 1.00 25.92 ? 364 ALA A CA 1 ATOM 2804 C C . ALA A 1 364 ? 11.623 22.216 13.754 1.00 26.65 ? 364 ALA A C 1 ATOM 2805 O O . ALA A 1 364 ? 11.599 22.302 12.520 1.00 26.67 ? 364 ALA A O 1 ATOM 2806 C CB . ALA A 1 364 ? 12.937 23.902 15.018 1.00 25.20 ? 364 ALA A CB 1 ATOM 2807 N N . ASP A 1 365 ? 10.556 21.911 14.487 1.00 26.48 ? 365 ASP A N 1 ATOM 2808 C CA . ASP A 1 365 ? 9.231 21.768 13.900 1.00 27.12 ? 365 ASP A CA 1 ATOM 2809 C C . ASP A 1 365 ? 8.373 23.019 14.129 1.00 27.74 ? 365 ASP A C 1 ATOM 2810 O O . ASP A 1 365 ? 7.950 23.278 15.262 1.00 27.72 ? 365 ASP A O 1 ATOM 2811 C CB . ASP A 1 365 ? 8.553 20.538 14.497 1.00 26.76 ? 365 ASP A CB 1 ATOM 2812 C CG . ASP A 1 365 ? 7.183 20.256 13.892 1.00 26.50 ? 365 ASP A CG 1 ATOM 2813 O OD1 . ASP A 1 365 ? 6.705 21.029 13.032 1.00 25.80 ? 365 ASP A OD1 1 ATOM 2814 O OD2 . ASP A 1 365 ? 6.574 19.258 14.317 1.00 26.14 ? 365 ASP A OD2 1 ATOM 2815 N N . PRO A 1 366 ? 8.092 23.795 13.057 1.00 28.21 ? 366 PRO A N 1 ATOM 2816 C CA . PRO A 1 366 ? 7.340 25.030 13.311 1.00 28.49 ? 366 PRO A CA 1 ATOM 2817 C C . PRO A 1 366 ? 5.937 24.779 13.848 1.00 28.46 ? 366 PRO A C 1 ATOM 2818 O O . PRO A 1 366 ? 5.356 25.679 14.441 1.00 28.58 ? 366 PRO A O 1 ATOM 2819 C CB . PRO A 1 366 ? 7.279 25.716 11.934 1.00 28.64 ? 366 PRO A CB 1 ATOM 2820 C CG . PRO A 1 366 ? 7.505 24.624 10.950 1.00 28.92 ? 366 PRO A CG 1 ATOM 2821 C CD . PRO A 1 366 ? 8.414 23.631 11.629 1.00 28.00 ? 366 PRO A CD 1 ATOM 2822 N N . ALA A 1 367 ? 5.408 23.569 13.668 1.00 28.72 ? 367 ALA A N 1 ATOM 2823 C CA . ALA A 1 367 ? 4.076 23.259 14.193 1.00 28.88 ? 367 ALA A CA 1 ATOM 2824 C C . ALA A 1 367 ? 4.082 23.139 15.724 1.00 28.99 ? 367 ALA A C 1 ATOM 2825 O O . ALA A 1 367 ? 3.029 23.096 16.345 1.00 29.48 ? 367 ALA A O 1 ATOM 2826 C CB . ALA A 1 367 ? 3.523 21.999 13.567 1.00 28.69 ? 367 ALA A CB 1 ATOM 2827 N N . MET A 1 368 ? 5.270 23.069 16.316 1.00 28.78 ? 368 MET A N 1 ATOM 2828 C CA . MET A 1 368 ? 5.412 22.917 17.765 1.00 28.39 ? 368 MET A CA 1 ATOM 2829 C C . MET A 1 368 ? 5.424 24.261 18.468 1.00 27.95 ? 368 MET A C 1 ATOM 2830 O O . MET A 1 368 ? 5.250 24.313 19.681 1.00 28.21 ? 368 MET A O 1 ATOM 2831 C CB . MET A 1 368 ? 6.683 22.152 18.108 1.00 28.71 ? 368 MET A CB 1 ATOM 2832 C CG . MET A 1 368 ? 6.648 20.696 17.728 1.00 30.13 ? 368 MET A CG 1 ATOM 2833 S SD . MET A 1 368 ? 5.496 19.738 18.739 1.00 39.19 ? 368 MET A SD 1 ATOM 2834 C CE . MET A 1 368 ? 6.535 19.463 20.181 1.00 34.67 ? 368 MET A CE 1 ATOM 2835 N N . ALA A 1 369 ? 5.617 25.341 17.709 1.00 27.12 ? 369 ALA A N 1 ATOM 2836 C CA . ALA A 1 369 ? 5.768 26.683 18.281 1.00 27.55 ? 369 ALA A CA 1 ATOM 2837 C C . ALA A 1 369 ? 4.647 27.046 19.261 1.00 28.10 ? 369 ALA A C 1 ATOM 2838 O O . ALA A 1 369 ? 4.891 27.664 20.296 1.00 28.03 ? 369 ALA A O 1 ATOM 2839 C CB . ALA A 1 369 ? 5.884 27.731 17.185 1.00 26.75 ? 369 ALA A CB 1 ATOM 2840 N N . GLU A 1 370 ? 3.424 26.643 18.927 1.00 29.12 ? 370 GLU A N 1 ATOM 2841 C CA . GLU A 1 370 ? 2.244 26.935 19.751 1.00 29.81 ? 370 GLU A CA 1 ATOM 2842 C C . GLU A 1 370 ? 2.114 26.107 21.051 1.00 29.42 ? 370 GLU A C 1 ATOM 2843 O O . GLU A 1 370 ? 1.195 26.336 21.845 1.00 30.04 ? 370 GLU A O 1 ATOM 2844 C CB A GLU A 1 370 ? 0.964 26.734 18.912 0.50 29.58 ? 370 GLU A CB 1 ATOM 2845 C CB B GLU A 1 370 ? 0.967 26.964 18.912 0.50 30.02 ? 370 GLU A CB 1 ATOM 2846 C CG A GLU A 1 370 ? 0.646 25.259 18.587 0.50 30.00 ? 370 GLU A CG 1 ATOM 2847 C CG B GLU A 1 370 ? 0.544 28.390 18.583 0.50 32.19 ? 370 GLU A CG 1 ATOM 2848 C CD A GLU A 1 370 ? -0.724 25.029 17.937 0.50 30.50 ? 370 GLU A CD 1 ATOM 2849 C CD B GLU A 1 370 ? 0.985 28.887 17.210 0.50 35.91 ? 370 GLU A CD 1 ATOM 2850 O OE1 A GLU A 1 370 ? -1.380 24.025 18.283 0.50 30.86 ? 370 GLU A OE1 1 ATOM 2851 O OE1 B GLU A 1 370 ? 0.449 28.390 16.193 0.50 36.85 ? 370 GLU A OE1 1 ATOM 2852 O OE2 A GLU A 1 370 ? -1.145 25.829 17.078 0.50 31.62 ? 370 GLU A OE2 1 ATOM 2853 O OE2 B GLU A 1 370 ? 1.837 29.805 17.151 0.50 37.09 ? 370 GLU A OE2 1 ATOM 2854 N N . GLN A 1 371 ? 3.026 25.160 21.269 1.00 28.93 ? 371 GLN A N 1 ATOM 2855 C CA . GLN A 1 371 ? 3.082 24.426 22.539 1.00 28.63 ? 371 GLN A CA 1 ATOM 2856 C C . GLN A 1 371 ? 3.525 25.324 23.689 1.00 28.23 ? 371 GLN A C 1 ATOM 2857 O O . GLN A 1 371 ? 3.231 25.027 24.842 1.00 28.37 ? 371 GLN A O 1 ATOM 2858 C CB . GLN A 1 371 ? 4.030 23.223 22.476 1.00 28.65 ? 371 GLN A CB 1 ATOM 2859 C CG . GLN A 1 371 ? 3.573 22.080 21.599 1.00 29.15 ? 371 GLN A CG 1 ATOM 2860 C CD . GLN A 1 371 ? 2.294 21.455 22.084 1.00 31.28 ? 371 GLN A CD 1 ATOM 2861 O OE1 . GLN A 1 371 ? 2.128 21.186 23.271 1.00 29.82 ? 371 GLN A OE1 1 ATOM 2862 N NE2 . GLN A 1 371 ? 1.365 21.245 21.167 1.00 32.42 ? 371 GLN A NE2 1 ATOM 2863 N N . LEU A 1 372 ? 4.247 26.399 23.371 1.00 27.57 ? 372 LEU A N 1 ATOM 2864 C CA . LEU A 1 372 ? 4.738 27.334 24.382 1.00 27.50 ? 372 LEU A CA 1 ATOM 2865 C C . LEU A 1 372 ? 3.616 28.064 25.124 1.00 28.36 ? 372 LEU A C 1 ATOM 2866 O O . LEU A 1 372 ? 2.758 28.705 24.512 1.00 27.94 ? 372 LEU A O 1 ATOM 2867 C CB . LEU A 1 372 ? 5.701 28.342 23.768 1.00 26.40 ? 372 LEU A CB 1 ATOM 2868 C CG . LEU A 1 372 ? 6.519 29.185 24.744 1.00 25.14 ? 372 LEU A CG 1 ATOM 2869 C CD1 . LEU A 1 372 ? 7.689 28.406 25.301 1.00 24.08 ? 372 LEU A CD1 1 ATOM 2870 C CD2 . LEU A 1 372 ? 6.980 30.428 24.062 1.00 24.30 ? 372 LEU A CD2 1 ATOM 2871 N N . GLY A 1 373 ? 3.637 27.960 26.452 1.00 29.53 ? 373 GLY A N 1 ATOM 2872 C CA . GLY A 1 373 ? 2.634 28.600 27.299 1.00 30.75 ? 373 GLY A CA 1 ATOM 2873 C C . GLY A 1 373 ? 1.230 28.094 27.064 1.00 32.30 ? 373 GLY A C 1 ATOM 2874 O O . GLY A 1 373 ? 0.268 28.800 27.325 1.00 31.55 ? 373 GLY A O 1 ATOM 2875 N N . LYS A 1 374 ? 1.111 26.868 26.563 1.00 23.09 ? 374 LYS A N 1 ATOM 2876 C CA . LYS A 1 374 ? -0.204 26.297 26.175 1.00 26.26 ? 374 LYS A CA 1 ATOM 2877 C C . LYS A 1 374 ? -1.063 26.239 27.435 1.00 25.74 ? 374 LYS A C 1 ATOM 2878 O O . LYS A 1 374 ? -0.573 25.826 28.480 1.00 24.74 ? 374 LYS A O 1 ATOM 2879 C CB . LYS A 1 374 ? 0.002 24.887 25.634 1.00 27.15 ? 374 LYS A CB 1 ATOM 2880 C CG . LYS A 1 374 ? -0.953 24.405 24.593 1.00 31.71 ? 374 LYS A CG 1 ATOM 2881 C CD . LYS A 1 374 ? -0.838 22.882 24.467 1.00 35.65 ? 374 LYS A CD 1 ATOM 2882 C CE . LYS A 1 374 ? -1.389 22.362 23.160 1.00 43.09 ? 374 LYS A CE 1 ATOM 2883 N NZ . LYS A 1 374 ? -2.517 23.193 22.579 1.00 48.18 ? 374 LYS A NZ 1 ATOM 2884 N N . GLN A 1 375 ? -2.333 26.643 27.336 1.00 27.07 ? 375 GLN A N 1 ATOM 2885 C CA . GLN A 1 375 ? -3.238 26.682 28.503 1.00 27.21 ? 375 GLN A CA 1 ATOM 2886 C C . GLN A 1 375 ? -3.360 25.361 29.286 1.00 27.07 ? 375 GLN A C 1 ATOM 2887 O O . GLN A 1 375 ? -3.431 25.382 30.506 1.00 26.88 ? 375 GLN A O 1 ATOM 2888 C CB . GLN A 1 375 ? -4.631 27.233 28.130 1.00 28.38 ? 375 GLN A CB 1 ATOM 2889 C CG . GLN A 1 375 ? -5.526 27.621 29.347 1.00 28.40 ? 375 GLN A CG 1 ATOM 2890 C CD . GLN A 1 375 ? -4.855 28.610 30.313 1.00 29.68 ? 375 GLN A CD 1 ATOM 2891 O OE1 . GLN A 1 375 ? -4.313 29.638 29.894 1.00 30.72 ? 375 GLN A OE1 1 ATOM 2892 N NE2 . GLN A 1 375 ? -4.918 28.312 31.618 1.00 28.43 ? 375 GLN A NE2 1 ATOM 2893 N N . GLU A 1 376 ? -3.382 24.225 28.590 1.00 27.91 ? 376 GLU A N 1 ATOM 2894 C CA . GLU A 1 376 ? -3.340 22.915 29.247 1.00 27.92 ? 376 GLU A CA 1 ATOM 2895 C C . GLU A 1 376 ? -2.124 22.782 30.179 1.00 26.44 ? 376 GLU A C 1 ATOM 2896 O O . GLU A 1 376 ? -2.236 22.259 31.292 1.00 26.29 ? 376 GLU A O 1 ATOM 2897 C CB . GLU A 1 376 ? -3.316 21.793 28.209 1.00 28.85 ? 376 GLU A CB 1 ATOM 2898 C CG . GLU A 1 376 ? -4.621 21.593 27.435 1.00 32.91 ? 376 GLU A CG 1 ATOM 2899 C CD . GLU A 1 376 ? -4.786 22.521 26.224 1.00 35.26 ? 376 GLU A CD 1 ATOM 2900 O OE1 . GLU A 1 376 ? -3.955 23.442 26.003 1.00 33.68 ? 376 GLU A OE1 1 ATOM 2901 O OE2 . GLU A 1 376 ? -5.776 22.323 25.488 1.00 38.89 ? 376 GLU A OE2 1 ATOM 2902 N N . HIS A 1 377 ? -0.965 23.263 29.726 1.00 26.01 ? 377 HIS A N 1 ATOM 2903 C CA . HIS A 1 377 ? 0.251 23.222 30.545 1.00 24.72 ? 377 HIS A CA 1 ATOM 2904 C C . HIS A 1 377 ? 0.160 24.154 31.738 1.00 23.89 ? 377 HIS A C 1 ATOM 2905 O O . HIS A 1 377 ? 0.708 23.868 32.800 1.00 23.61 ? 377 HIS A O 1 ATOM 2906 C CB . HIS A 1 377 ? 1.492 23.595 29.737 1.00 24.07 ? 377 HIS A CB 1 ATOM 2907 C CG . HIS A 1 377 ? 1.734 22.739 28.530 1.00 25.46 ? 377 HIS A CG 1 ATOM 2908 N ND1 . HIS A 1 377 ? 1.032 21.580 28.265 1.00 27.84 ? 377 HIS A ND1 1 ATOM 2909 C CD2 . HIS A 1 377 ? 2.615 22.881 27.517 1.00 23.95 ? 377 HIS A CD2 1 ATOM 2910 C CE1 . HIS A 1 377 ? 1.466 21.051 27.136 1.00 26.04 ? 377 HIS A CE1 1 ATOM 2911 N NE2 . HIS A 1 377 ? 2.423 21.826 26.658 1.00 27.74 ? 377 HIS A NE2 1 ATOM 2912 N N . ARG A 1 378 ? -0.485 25.298 31.539 1.00 24.00 ? 378 ARG A N 1 ATOM 2913 C CA . ARG A 1 378 ? -0.738 26.244 32.609 1.00 23.54 ? 378 ARG A CA 1 ATOM 2914 C C . ARG A 1 378 ? -1.706 25.647 33.636 1.00 23.97 ? 378 ARG A C 1 ATOM 2915 O O . ARG A 1 378 ? -1.496 25.806 34.840 1.00 23.28 ? 378 ARG A O 1 ATOM 2916 C CB . ARG A 1 378 ? -1.306 27.549 32.052 1.00 24.10 ? 378 ARG A CB 1 ATOM 2917 C CG . ARG A 1 378 ? -0.292 28.353 31.270 1.00 23.77 ? 378 ARG A CG 1 ATOM 2918 C CD . ARG A 1 378 ? -0.776 29.771 30.987 1.00 24.32 ? 378 ARG A CD 1 ATOM 2919 N NE . ARG A 1 378 ? 0.114 30.393 30.014 1.00 24.18 ? 378 ARG A NE 1 ATOM 2920 C CZ . ARG A 1 378 ? 1.284 30.953 30.311 1.00 22.77 ? 378 ARG A CZ 1 ATOM 2921 N NH1 . ARG A 1 378 ? 1.712 31.009 31.568 1.00 22.63 ? 378 ARG A NH1 1 ATOM 2922 N NH2 . ARG A 1 378 ? 2.021 31.482 29.342 1.00 21.43 ? 378 ARG A NH2 1 ATOM 2923 N N . ASP A 1 379 ? -2.762 24.979 33.162 1.00 24.36 ? 379 ASP A N 1 ATOM 2924 C CA . ASP A 1 379 ? -3.658 24.237 34.059 1.00 24.50 ? 379 ASP A CA 1 ATOM 2925 C C . ASP A 1 379 ? -2.902 23.235 34.933 1.00 23.93 ? 379 ASP A C 1 ATOM 2926 O O . ASP A 1 379 ? -3.183 23.107 36.125 1.00 24.11 ? 379 ASP A O 1 ATOM 2927 C CB . ASP A 1 379 ? -4.754 23.529 33.276 1.00 25.08 ? 379 ASP A CB 1 ATOM 2928 C CG . ASP A 1 379 ? -5.702 24.508 32.570 1.00 28.63 ? 379 ASP A CG 1 ATOM 2929 O OD1 . ASP A 1 379 ? -5.717 25.720 32.898 1.00 29.43 ? 379 ASP A OD1 1 ATOM 2930 O OD2 . ASP A 1 379 ? -6.440 24.054 31.673 1.00 32.12 ? 379 ASP A OD2 1 ATOM 2931 N N . LEU A 1 380 ? -1.937 22.539 34.330 1.00 24.19 ? 380 LEU A N 1 ATOM 2932 C CA . LEU A 1 380 ? -1.076 21.594 35.025 1.00 23.50 ? 380 LEU A CA 1 ATOM 2933 C C . LEU A 1 380 ? -0.215 22.284 36.068 1.00 22.70 ? 380 LEU A C 1 ATOM 2934 O O . LEU A 1 380 ? -0.149 21.826 37.209 1.00 22.86 ? 380 LEU A O 1 ATOM 2935 C CB . LEU A 1 380 ? -0.193 20.833 34.026 1.00 24.21 ? 380 LEU A CB 1 ATOM 2936 C CG . LEU A 1 380 ? 0.823 19.801 34.547 1.00 24.08 ? 380 LEU A CG 1 ATOM 2937 C CD1 . LEU A 1 380 ? 0.126 18.637 35.211 1.00 24.22 ? 380 LEU A CD1 1 ATOM 2938 C CD2 . LEU A 1 380 ? 1.657 19.296 33.387 1.00 23.91 ? 380 LEU A CD2 1 ATOM 2939 N N . ALA A 1 381 ? 0.446 23.368 35.677 1.00 21.48 ? 381 ALA A N 1 ATOM 2940 C CA . ALA A 1 381 ? 1.267 24.154 36.607 1.00 21.23 ? 381 ALA A CA 1 ATOM 2941 C C . ALA A 1 381 ? 0.411 24.664 37.765 1.00 21.14 ? 381 ALA A C 1 ATOM 2942 O O . ALA A 1 381 ? 0.855 24.689 38.902 1.00 21.08 ? 381 ALA A O 1 ATOM 2943 C CB . ALA A 1 381 ? 1.924 25.320 35.883 1.00 20.34 ? 381 ALA A CB 1 ATOM 2944 N N . ARG A 1 382 ? -0.811 25.082 37.455 1.00 21.78 ? 382 ARG A N 1 ATOM 2945 C CA . ARG A 1 382 ? -1.769 25.514 38.470 1.00 22.28 ? 382 ARG A CA 1 ATOM 2946 C C . ARG A 1 382 ? -2.120 24.375 39.441 1.00 22.86 ? 382 ARG A C 1 ATOM 2947 O O . ARG A 1 382 ? -2.167 24.591 40.647 1.00 22.73 ? 382 ARG A O 1 ATOM 2948 C CB . ARG A 1 382 ? -3.044 26.035 37.796 1.00 22.42 ? 382 ARG A CB 1 ATOM 2949 C CG . ARG A 1 382 ? -4.104 26.586 38.741 1.00 21.97 ? 382 ARG A CG 1 ATOM 2950 C CD . ARG A 1 382 ? -5.253 27.097 37.912 1.00 22.79 ? 382 ARG A CD 1 ATOM 2951 N NE . ARG A 1 382 ? -6.407 27.468 38.725 1.00 23.82 ? 382 ARG A NE 1 ATOM 2952 C CZ . ARG A 1 382 ? -7.458 28.135 38.254 1.00 25.56 ? 382 ARG A CZ 1 ATOM 2953 N NH1 . ARG A 1 382 ? -7.490 28.511 36.970 1.00 26.40 ? 382 ARG A NH1 1 ATOM 2954 N NH2 . ARG A 1 382 ? -8.468 28.438 39.056 1.00 25.20 ? 382 ARG A NH2 1 ATOM 2955 N N . GLU A 1 383 ? -2.416 23.190 38.906 1.00 24.13 ? 383 GLU A N 1 ATOM 2956 C CA . GLU A 1 383 ? -2.590 21.988 39.733 1.00 24.81 ? 383 GLU A CA 1 ATOM 2957 C C . GLU A 1 383 ? -1.361 21.701 40.636 1.00 24.02 ? 383 GLU A C 1 ATOM 2958 O O . GLU A 1 383 ? -1.514 21.460 41.840 1.00 23.87 ? 383 GLU A O 1 ATOM 2959 C CB . GLU A 1 383 ? -2.890 20.779 38.850 1.00 26.11 ? 383 GLU A CB 1 ATOM 2960 C CG . GLU A 1 383 ? -3.063 19.459 39.629 1.00 27.33 ? 383 GLU A CG 1 ATOM 2961 C CD . GLU A 1 383 ? -3.086 18.234 38.736 1.00 29.20 ? 383 GLU A CD 1 ATOM 2962 O OE1 . GLU A 1 383 ? -3.338 18.376 37.517 1.00 33.74 ? 383 GLU A OE1 1 ATOM 2963 O OE2 . GLU A 1 383 ? -2.825 17.119 39.235 1.00 30.62 ? 383 GLU A OE2 1 ATOM 2964 N N . ALA A 1 384 ? -0.162 21.731 40.048 1.00 23.22 ? 384 ALA A N 1 ATOM 2965 C CA . ALA A 1 384 ? 1.090 21.489 40.777 1.00 23.06 ? 384 ALA A CA 1 ATOM 2966 C C . ALA A 1 384 ? 1.320 22.503 41.906 1.00 22.22 ? 384 ALA A C 1 ATOM 2967 O O . ALA A 1 384 ? 1.720 22.132 43.010 1.00 22.31 ? 384 ALA A O 1 ATOM 2968 C CB . ALA A 1 384 ? 2.286 21.482 39.806 1.00 22.37 ? 384 ALA A CB 1 ATOM 2969 N N . ALA A 1 385 ? 1.073 23.777 41.611 1.00 21.86 ? 385 ALA A N 1 ATOM 2970 C CA . ALA A 1 385 ? 1.241 24.866 42.575 1.00 21.35 ? 385 ALA A CA 1 ATOM 2971 C C . ALA A 1 385 ? 0.337 24.649 43.787 1.00 22.11 ? 385 ALA A C 1 ATOM 2972 O O . ALA A 1 385 ? 0.793 24.741 44.935 1.00 21.91 ? 385 ALA A O 1 ATOM 2973 C CB . ALA A 1 385 ? 0.941 26.219 41.917 1.00 20.16 ? 385 ALA A CB 1 ATOM 2974 N N . ARG A 1 386 ? -0.939 24.357 43.523 1.00 22.09 ? 386 ARG A N 1 ATOM 2975 C CA . ARG A 1 386 ? -1.902 24.070 44.577 1.00 22.67 ? 386 ARG A CA 1 ATOM 2976 C C . ARG A 1 386 ? -1.473 22.860 45.417 1.00 22.99 ? 386 ARG A C 1 ATOM 2977 O O . ARG A 1 386 ? -1.545 22.886 46.657 1.00 22.69 ? 386 ARG A O 1 ATOM 2978 C CB . ARG A 1 386 ? -3.294 23.855 43.963 1.00 23.47 ? 386 ARG A CB 1 ATOM 2979 C CG . ARG A 1 386 ? -4.417 23.533 44.959 1.00 25.53 ? 386 ARG A CG 1 ATOM 2980 C CD . ARG A 1 386 ? -4.786 22.064 44.895 1.00 28.64 ? 386 ARG A CD 1 ATOM 2981 N NE . ARG A 1 386 ? -5.190 21.674 43.545 1.00 32.21 ? 386 ARG A NE 1 ATOM 2982 C CZ . ARG A 1 386 ? -5.560 20.445 43.192 1.00 33.86 ? 386 ARG A CZ 1 ATOM 2983 N NH1 . ARG A 1 386 ? -5.574 19.467 44.090 1.00 36.89 ? 386 ARG A NH1 1 ATOM 2984 N NH2 . ARG A 1 386 ? -5.915 20.197 41.940 1.00 33.80 ? 386 ARG A NH2 1 ATOM 2985 N N . LYS A 1 387 ? -1.033 21.808 44.740 1.00 23.24 ? 387 LYS A N 1 ATOM 2986 C CA . LYS A 1 387 ? -0.647 20.564 45.405 1.00 23.98 ? 387 LYS A CA 1 ATOM 2987 C C . LYS A 1 387 ? 0.617 20.697 46.246 1.00 23.17 ? 387 LYS A C 1 ATOM 2988 O O . LYS A 1 387 ? 0.827 19.926 47.208 1.00 23.56 ? 387 LYS A O 1 ATOM 2989 C CB . LYS A 1 387 ? -0.534 19.422 44.391 1.00 24.47 ? 387 LYS A CB 1 ATOM 2990 C CG . LYS A 1 387 ? -1.888 18.899 43.960 1.00 24.85 ? 387 LYS A CG 1 ATOM 2991 C CD . LYS A 1 387 ? -1.767 17.856 42.873 1.00 25.77 ? 387 LYS A CD 1 ATOM 2992 C CE . LYS A 1 387 ? -3.103 17.236 42.562 1.00 25.75 ? 387 LYS A CE 1 ATOM 2993 N NZ . LYS A 1 387 ? -2.935 15.983 41.779 1.00 29.28 ? 387 LYS A NZ 1 ATOM 2994 N N . SER A 1 388 ? 1.421 21.698 45.899 1.00 22.19 ? 388 SER A N 1 ATOM 2995 C CA . SER A 1 388 ? 2.694 21.955 46.562 1.00 22.38 ? 388 SER A CA 1 ATOM 2996 C C . SER A 1 388 ? 2.542 22.720 47.874 1.00 22.01 ? 388 SER A C 1 ATOM 2997 O O . SER A 1 388 ? 3.452 22.681 48.707 1.00 22.78 ? 388 SER A O 1 ATOM 2998 C CB . SER A 1 388 ? 3.660 22.705 45.637 1.00 21.15 ? 388 SER A CB 1 ATOM 2999 O OG . SER A 1 388 ? 3.385 24.103 45.576 1.00 21.52 ? 388 SER A OG 1 ATOM 3000 N N . LEU A 1 389 ? 1.415 23.416 48.061 1.00 21.61 ? 389 LEU A N 1 ATOM 3001 C CA . LEU A 1 389 ? 1.252 24.296 49.229 1.00 21.52 ? 389 LEU A CA 1 ATOM 3002 C C . LEU A 1 389 ? 1.207 23.495 50.518 1.00 21.76 ? 389 LEU A C 1 ATOM 3003 O O . LEU A 1 389 ? 0.501 22.491 50.597 1.00 22.49 ? 389 LEU A O 1 ATOM 3004 C CB . LEU A 1 389 ? -0.016 25.145 49.132 1.00 21.75 ? 389 LEU A CB 1 ATOM 3005 C CG . LEU A 1 389 ? -0.317 25.879 47.825 1.00 22.17 ? 389 LEU A CG 1 ATOM 3006 C CD1 . LEU A 1 389 ? -1.699 26.482 47.941 1.00 20.00 ? 389 LEU A CD1 1 ATOM 3007 C CD2 . LEU A 1 389 ? 0.744 26.955 47.503 1.00 19.52 ? 389 LEU A CD2 1 ATOM 3008 N N . VAL A 1 390 ? 1.969 23.929 51.521 1.00 21.68 ? 390 VAL A N 1 ATOM 3009 C CA . VAL A 1 390 ? 1.894 23.289 52.828 1.00 22.14 ? 390 VAL A CA 1 ATOM 3010 C C . VAL A 1 390 ? 1.283 24.245 53.847 1.00 22.30 ? 390 VAL A C 1 ATOM 3011 O O . VAL A 1 390 ? 1.826 25.314 54.116 1.00 21.78 ? 390 VAL A O 1 ATOM 3012 C CB . VAL A 1 390 ? 3.249 22.723 53.340 1.00 22.69 ? 390 VAL A CB 1 ATOM 3013 C CG1 . VAL A 1 390 ? 3.038 21.983 54.676 1.00 21.97 ? 390 VAL A CG1 1 ATOM 3014 C CG2 . VAL A 1 390 ? 3.877 21.775 52.322 1.00 20.78 ? 390 VAL A CG2 1 ATOM 3015 N N . LEU A 1 391 ? 0.133 23.850 54.384 1.00 22.96 ? 391 LEU A N 1 ATOM 3016 C CA . LEU A 1 391 ? -0.555 24.647 55.391 1.00 22.93 ? 391 LEU A CA 1 ATOM 3017 C C . LEU A 1 391 ? 0.095 24.344 56.740 1.00 24.10 ? 391 LEU A C 1 ATOM 3018 O O . LEU A 1 391 ? 0.061 23.200 57.222 1.00 25.08 ? 391 LEU A O 1 ATOM 3019 C CB . LEU A 1 391 ? -2.041 24.300 55.398 1.00 23.23 ? 391 LEU A CB 1 ATOM 3020 C CG . LEU A 1 391 ? -3.000 25.027 56.344 1.00 23.40 ? 391 LEU A CG 1 ATOM 3021 C CD1 . LEU A 1 391 ? -3.083 26.504 55.965 1.00 22.29 ? 391 LEU A CD1 1 ATOM 3022 C CD2 . LEU A 1 391 ? -4.361 24.336 56.281 1.00 23.13 ? 391 LEU A CD2 1 ATOM 3023 N N . LEU A 1 392 ? 0.709 25.368 57.326 1.00 24.05 ? 392 LEU A N 1 ATOM 3024 C CA . LEU A 1 392 ? 1.461 25.206 58.573 1.00 25.02 ? 392 LEU A CA 1 ATOM 3025 C C . LEU A 1 392 ? 0.639 25.577 59.813 1.00 25.84 ? 392 LEU A C 1 ATOM 3026 O O . LEU A 1 392 ? 0.919 25.111 60.908 1.00 25.86 ? 392 LEU A O 1 ATOM 3027 C CB . LEU A 1 392 ? 2.745 26.038 58.524 1.00 24.83 ? 392 LEU A CB 1 ATOM 3028 C CG . LEU A 1 392 ? 3.808 25.648 57.487 1.00 24.43 ? 392 LEU A CG 1 ATOM 3029 C CD1 . LEU A 1 392 ? 4.972 26.630 57.584 1.00 25.94 ? 392 LEU A CD1 1 ATOM 3030 C CD2 . LEU A 1 392 ? 4.301 24.209 57.700 1.00 24.25 ? 392 LEU A CD2 1 ATOM 3031 N N . LYS A 1 393 ? -0.371 26.421 59.618 1.00 25.53 ? 393 LYS A N 1 ATOM 3032 C CA . LYS A 1 393 ? -1.215 26.925 60.715 1.00 26.86 ? 393 LYS A CA 1 ATOM 3033 C C . LYS A 1 393 ? -2.538 27.312 60.083 1.00 26.40 ? 393 LYS A C 1 ATOM 3034 O O . LYS A 1 393 ? -2.553 27.915 59.004 1.00 24.81 ? 393 LYS A O 1 ATOM 3035 C CB . LYS A 1 393 ? -0.584 28.180 61.333 1.00 26.62 ? 393 LYS A CB 1 ATOM 3036 C CG . LYS A 1 393 ? -1.294 28.698 62.574 1.00 27.87 ? 393 LYS A CG 1 ATOM 3037 C CD . LYS A 1 393 ? -0.609 29.911 63.131 1.00 26.05 ? 393 LYS A CD 1 ATOM 3038 C CE . LYS A 1 393 ? -1.313 30.354 64.389 1.00 28.43 ? 393 LYS A CE 1 ATOM 3039 N NZ . LYS A 1 393 ? -0.654 31.542 64.972 1.00 28.11 ? 393 LYS A NZ 1 ATOM 3040 N N . ASN A 1 394 ? -3.636 26.995 60.758 1.00 27.11 ? 394 ASN A N 1 ATOM 3041 C CA . ASN A 1 394 ? -4.955 27.435 60.320 1.00 27.53 ? 394 ASN A CA 1 ATOM 3042 C C . ASN A 1 394 ? -5.846 27.745 61.523 1.00 29.08 ? 394 ASN A C 1 ATOM 3043 O O . ASN A 1 394 ? -6.822 27.044 61.767 1.00 30.36 ? 394 ASN A O 1 ATOM 3044 C CB . ASN A 1 394 ? -5.601 26.365 59.455 1.00 27.45 ? 394 ASN A CB 1 ATOM 3045 C CG . ASN A 1 394 ? -6.800 26.884 58.666 1.00 27.34 ? 394 ASN A CG 1 ATOM 3046 O OD1 . ASN A 1 394 ? -6.944 28.093 58.434 1.00 26.94 ? 394 ASN A OD1 1 ATOM 3047 N ND2 . ASN A 1 394 ? -7.656 25.962 58.230 1.00 27.83 ? 394 ASN A ND2 1 ATOM 3048 N N . GLY A 1 395 ? -5.495 28.792 62.267 1.00 29.67 ? 395 GLY A N 1 ATOM 3049 C CA . GLY A 1 395 ? -6.166 29.153 63.509 1.00 31.14 ? 395 GLY A CA 1 ATOM 3050 C C . GLY A 1 395 ? -5.169 29.355 64.635 1.00 32.71 ? 395 GLY A C 1 ATOM 3051 O O . GLY A 1 395 ? -4.302 28.510 64.863 1.00 32.88 ? 395 GLY A O 1 ATOM 3052 N N . LYS A 1 396 ? -5.303 30.468 65.361 1.00 33.94 ? 396 LYS A N 1 ATOM 3053 C CA . LYS A 1 396 ? -4.376 30.793 66.454 1.00 35.16 ? 396 LYS A CA 1 ATOM 3054 C C . LYS A 1 396 ? -4.476 29.882 67.679 1.00 37.25 ? 396 LYS A C 1 ATOM 3055 O O . LYS A 1 396 ? -3.475 29.650 68.356 1.00 38.08 ? 396 LYS A O 1 ATOM 3056 C CB . LYS A 1 396 ? -4.527 32.256 66.877 1.00 35.53 ? 396 LYS A CB 1 ATOM 3057 C CG . LYS A 1 396 ? -4.172 33.258 65.786 1.00 35.10 ? 396 LYS A CG 1 ATOM 3058 C CD . LYS A 1 396 ? -3.928 34.646 66.361 1.00 34.40 ? 396 LYS A CD 1 ATOM 3059 C CE . LYS A 1 396 ? -3.339 35.554 65.291 1.00 33.49 ? 396 LYS A CE 1 ATOM 3060 N NZ . LYS A 1 396 ? -3.428 37.001 65.632 1.00 34.33 ? 396 LYS A NZ 1 ATOM 3061 N N . THR A 1 397 ? -5.677 29.396 67.993 1.00 38.05 ? 397 THR A N 1 ATOM 3062 C CA . THR A 1 397 ? -5.879 28.496 69.139 1.00 39.66 ? 397 THR A CA 1 ATOM 3063 C C . THR A 1 397 ? -6.678 27.282 68.678 1.00 40.31 ? 397 THR A C 1 ATOM 3064 O O . THR A 1 397 ? -7.275 27.306 67.604 1.00 39.97 ? 397 THR A O 1 ATOM 3065 C CB . THR A 1 397 ? -6.629 29.169 70.331 1.00 40.52 ? 397 THR A CB 1 ATOM 3066 O OG1 . THR A 1 397 ? -8.021 29.276 70.033 1.00 39.32 ? 397 THR A OG1 1 ATOM 3067 C CG2 . THR A 1 397 ? -6.078 30.555 70.638 1.00 40.88 ? 397 THR A CG2 1 ATOM 3068 N N . SER A 1 398 ? -6.699 26.230 69.488 1.00 41.65 ? 398 SER A N 1 ATOM 3069 C CA . SER A 1 398 ? -7.448 25.018 69.153 1.00 42.14 ? 398 SER A CA 1 ATOM 3070 C C . SER A 1 398 ? -8.953 25.274 69.029 1.00 41.99 ? 398 SER A C 1 ATOM 3071 O O . SER A 1 398 ? -9.672 24.506 68.392 1.00 43.20 ? 398 SER A O 1 ATOM 3072 C CB . SER A 1 398 ? -7.201 23.938 70.205 1.00 43.59 ? 398 SER A CB 1 ATOM 3073 O OG . SER A 1 398 ? -7.666 24.352 71.484 1.00 46.40 ? 398 SER A OG 1 ATOM 3074 N N . THR A 1 399 ? -9.421 26.356 69.638 1.00 40.72 ? 399 THR A N 1 ATOM 3075 C CA . THR A 1 399 ? -10.834 26.652 69.684 1.00 39.69 ? 399 THR A CA 1 ATOM 3076 C C . THR A 1 399 ? -11.286 27.717 68.657 1.00 36.50 ? 399 THR A C 1 ATOM 3077 O O . THR A 1 399 ? -12.477 27.989 68.527 1.00 35.79 ? 399 THR A O 1 ATOM 3078 C CB . THR A 1 399 ? -11.244 27.078 71.095 1.00 41.32 ? 399 THR A CB 1 ATOM 3079 O OG1 . THR A 1 399 ? -10.538 28.273 71.444 1.00 42.19 ? 399 THR A OG1 1 ATOM 3080 C CG2 . THR A 1 399 ? -10.950 25.966 72.126 1.00 44.14 ? 399 THR A CG2 1 ATOM 3081 N N . ASP A 1 400 ? -10.338 28.314 67.936 1.00 33.78 ? 400 ASP A N 1 ATOM 3082 C CA . ASP A 1 400 ? -10.669 29.263 66.876 1.00 31.13 ? 400 ASP A CA 1 ATOM 3083 C C . ASP A 1 400 ? -11.373 28.566 65.711 1.00 30.67 ? 400 ASP A C 1 ATOM 3084 O O . ASP A 1 400 ? -11.097 27.400 65.423 1.00 30.46 ? 400 ASP A O 1 ATOM 3085 C CB . ASP A 1 400 ? -9.412 29.982 66.364 1.00 30.33 ? 400 ASP A CB 1 ATOM 3086 C CG . ASP A 1 400 ? -8.924 31.078 67.316 1.00 29.78 ? 400 ASP A CG 1 ATOM 3087 O OD1 . ASP A 1 400 ? -9.338 31.091 68.476 1.00 30.15 ? 400 ASP A OD1 1 ATOM 3088 O OD2 . ASP A 1 400 ? -8.126 31.937 66.900 1.00 30.40 ? 400 ASP A OD2 1 ATOM 3089 N N . ALA A 1 401 ? -12.292 29.281 65.064 1.00 29.93 ? 401 ALA A N 1 ATOM 3090 C CA . ALA A 1 401 ? -12.770 28.914 63.726 1.00 29.76 ? 401 ALA A CA 1 ATOM 3091 C C . ALA A 1 401 ? -11.568 28.901 62.778 1.00 29.01 ? 401 ALA A C 1 ATOM 3092 O O . ALA A 1 401 ? -10.750 29.824 62.801 1.00 28.71 ? 401 ALA A O 1 ATOM 3093 C CB . ALA A 1 401 ? -13.811 29.916 63.239 1.00 28.93 ? 401 ALA A CB 1 ATOM 3094 N N . PRO A 1 402 ? -11.437 27.842 61.959 1.00 29.09 ? 402 PRO A N 1 ATOM 3095 C CA . PRO A 1 402 ? -10.359 27.784 60.965 1.00 28.35 ? 402 PRO A CA 1 ATOM 3096 C C . PRO A 1 402 ? -10.523 28.936 59.984 1.00 27.51 ? 402 PRO A C 1 ATOM 3097 O O . PRO A 1 402 ? -11.627 29.154 59.500 1.00 28.02 ? 402 PRO A O 1 ATOM 3098 C CB . PRO A 1 402 ? -10.613 26.455 60.247 1.00 28.44 ? 402 PRO A CB 1 ATOM 3099 C CG . PRO A 1 402 ? -11.456 25.666 61.175 1.00 30.63 ? 402 PRO A CG 1 ATOM 3100 C CD . PRO A 1 402 ? -12.300 26.650 61.918 1.00 30.11 ? 402 PRO A CD 1 ATOM 3101 N N . LEU A 1 403 ? -9.469 29.711 59.746 1.00 26.90 ? 403 LEU A N 1 ATOM 3102 C CA . LEU A 1 403 ? -9.545 30.796 58.766 1.00 27.00 ? 403 LEU A CA 1 ATOM 3103 C C . LEU A 1 403 ? -9.754 30.288 57.327 1.00 25.96 ? 403 LEU A C 1 ATOM 3104 O O . LEU A 1 403 ? -10.567 30.837 56.585 1.00 25.69 ? 403 LEU A O 1 ATOM 3105 C CB . LEU A 1 403 ? -8.316 31.728 58.835 1.00 26.75 ? 403 LEU A CB 1 ATOM 3106 C CG . LEU A 1 403 ? -8.395 32.924 57.855 1.00 28.19 ? 403 LEU A CG 1 ATOM 3107 C CD1 . LEU A 1 403 ? -9.576 33.830 58.168 1.00 29.33 ? 403 LEU A CD1 1 ATOM 3108 C CD2 . LEU A 1 403 ? -7.149 33.747 57.839 1.00 27.59 ? 403 LEU A CD2 1 ATOM 3109 N N . LEU A 1 404 ? -9.008 29.253 56.939 1.00 25.71 ? 404 LEU A N 1 ATOM 3110 C CA . LEU A 1 404 ? -9.080 28.700 55.591 1.00 25.58 ? 404 LEU A CA 1 ATOM 3111 C C . LEU A 1 404 ? -9.982 27.470 55.596 1.00 26.56 ? 404 LEU A C 1 ATOM 3112 O O . LEU A 1 404 ? -9.925 26.677 56.531 1.00 27.48 ? 404 LEU A O 1 ATOM 3113 C CB . LEU A 1 404 ? -7.682 28.336 55.060 1.00 24.74 ? 404 LEU A CB 1 ATOM 3114 C CG . LEU A 1 404 ? -6.639 29.456 55.060 1.00 23.31 ? 404 LEU A CG 1 ATOM 3115 C CD1 . LEU A 1 404 ? -5.285 28.964 54.524 1.00 21.70 ? 404 LEU A CD1 1 ATOM 3116 C CD2 . LEU A 1 404 ? -7.137 30.667 54.265 1.00 21.35 ? 404 LEU A CD2 1 ATOM 3117 N N . PRO A 1 405 ? -10.816 27.309 54.553 1.00 26.45 ? 405 PRO A N 1 ATOM 3118 C CA . PRO A 1 405 ? -10.878 28.201 53.383 1.00 25.70 ? 405 PRO A CA 1 ATOM 3119 C C . PRO A 1 405 ? -11.668 29.499 53.615 1.00 25.54 ? 405 PRO A C 1 ATOM 3120 O O . PRO A 1 405 ? -12.623 29.540 54.409 1.00 25.39 ? 405 PRO A O 1 ATOM 3121 C CB . PRO A 1 405 ? -11.553 27.345 52.303 1.00 26.08 ? 405 PRO A CB 1 ATOM 3122 C CG . PRO A 1 405 ? -12.288 26.260 53.033 1.00 27.69 ? 405 PRO A CG 1 ATOM 3123 C CD . PRO A 1 405 ? -11.787 26.200 54.472 1.00 27.50 ? 405 PRO A CD 1 ATOM 3124 N N . LEU A 1 406 ? -11.228 30.545 52.924 1.00 24.78 ? 406 LEU A N 1 ATOM 3125 C CA . LEU A 1 406 ? -11.831 31.861 53.002 1.00 25.23 ? 406 LEU A CA 1 ATOM 3126 C C . LEU A 1 406 ? -13.068 31.900 52.102 1.00 25.79 ? 406 LEU A C 1 ATOM 3127 O O . LEU A 1 406 ? -13.115 31.196 51.094 1.00 25.76 ? 406 LEU A O 1 ATOM 3128 C CB . LEU A 1 406 ? -10.820 32.919 52.554 1.00 24.50 ? 406 LEU A CB 1 ATOM 3129 C CG . LEU A 1 406 ? -9.604 33.139 53.456 1.00 24.68 ? 406 LEU A CG 1 ATOM 3130 C CD1 . LEU A 1 406 ? -8.458 33.752 52.665 1.00 26.62 ? 406 LEU A CD1 1 ATOM 3131 C CD2 . LEU A 1 406 ? -9.951 33.980 54.664 1.00 23.45 ? 406 LEU A CD2 1 ATOM 3132 N N . PRO A 1 407 ? -14.071 32.723 52.466 1.00 26.07 ? 407 PRO A N 1 ATOM 3133 C CA . PRO A 1 407 ? -15.227 32.900 51.585 1.00 26.43 ? 407 PRO A CA 1 ATOM 3134 C C . PRO A 1 407 ? -14.894 33.783 50.372 1.00 25.80 ? 407 PRO A C 1 ATOM 3135 O O . PRO A 1 407 ? -14.208 34.807 50.516 1.00 25.52 ? 407 PRO A O 1 ATOM 3136 C CB . PRO A 1 407 ? -16.255 33.574 52.493 1.00 26.87 ? 407 PRO A CB 1 ATOM 3137 C CG . PRO A 1 407 ? -15.418 34.329 53.515 1.00 27.26 ? 407 PRO A CG 1 ATOM 3138 C CD . PRO A 1 407 ? -14.173 33.520 53.708 1.00 26.05 ? 407 PRO A CD 1 ATOM 3139 N N . LYS A 1 408 ? -15.366 33.386 49.189 1.00 25.93 ? 408 LYS A N 1 ATOM 3140 C CA . LYS A 1 408 ? -15.221 34.209 47.977 1.00 25.64 ? 408 LYS A CA 1 ATOM 3141 C C . LYS A 1 408 ? -16.078 35.477 47.999 1.00 26.17 ? 408 LYS A C 1 ATOM 3142 O O . LYS A 1 408 ? -15.791 36.432 47.282 1.00 25.40 ? 408 LYS A O 1 ATOM 3143 C CB . LYS A 1 408 ? -15.545 33.405 46.721 1.00 26.20 ? 408 LYS A CB 1 ATOM 3144 C CG . LYS A 1 408 ? -14.558 32.308 46.424 1.00 26.06 ? 408 LYS A CG 1 ATOM 3145 C CD . LYS A 1 408 ? -15.128 31.389 45.340 1.00 28.27 ? 408 LYS A CD 1 ATOM 3146 C CE . LYS A 1 408 ? -14.246 30.191 45.163 1.00 28.67 ? 408 LYS A CE 1 ATOM 3147 N NZ . LYS A 1 408 ? -14.429 29.643 43.811 1.00 29.99 ? 408 LYS A NZ 1 ATOM 3148 N N . LYS A 1 409 ? -17.129 35.475 48.821 1.00 27.40 ? 409 LYS A N 1 ATOM 3149 C CA . LYS A 1 409 ? -18.010 36.629 48.963 1.00 27.81 ? 409 LYS A CA 1 ATOM 3150 C C . LYS A 1 409 ? -17.864 37.284 50.340 1.00 27.97 ? 409 LYS A C 1 ATOM 3151 O O . LYS A 1 409 ? -18.189 36.684 51.365 1.00 27.78 ? 409 LYS A O 1 ATOM 3152 C CB . LYS A 1 409 ? -19.473 36.242 48.703 1.00 29.87 ? 409 LYS A CB 1 ATOM 3153 C CG . LYS A 1 409 ? -20.419 37.447 48.655 1.00 30.79 ? 409 LYS A CG 1 ATOM 3154 C CD . LYS A 1 409 ? -21.814 37.050 48.243 1.00 34.36 ? 409 LYS A CD 1 ATOM 3155 C CE . LYS A 1 409 ? -22.690 38.285 48.111 1.00 36.19 ? 409 LYS A CE 1 ATOM 3156 N NZ . LYS A 1 409 ? -24.077 37.920 47.759 1.00 40.56 ? 409 LYS A NZ 1 ATOM 3157 N N . ALA A 1 410 ? -17.376 38.524 50.331 1.00 27.60 ? 410 ALA A N 1 ATOM 3158 C CA . ALA A 1 410 ? -17.204 39.348 51.520 1.00 27.57 ? 410 ALA A CA 1 ATOM 3159 C C . ALA A 1 410 ? -17.258 40.805 51.059 1.00 27.84 ? 410 ALA A C 1 ATOM 3160 O O . ALA A 1 410 ? -16.867 41.108 49.932 1.00 28.16 ? 410 ALA A O 1 ATOM 3161 C CB . ALA A 1 410 ? -15.853 39.054 52.198 1.00 26.32 ? 410 ALA A CB 1 ATOM 3162 N N . PRO A 1 411 ? -17.753 41.715 51.911 1.00 28.61 ? 411 PRO A N 1 ATOM 3163 C CA . PRO A 1 411 ? -17.866 43.100 51.436 1.00 29.00 ? 411 PRO A CA 1 ATOM 3164 C C . PRO A 1 411 ? -16.558 43.702 50.922 1.00 28.70 ? 411 PRO A C 1 ATOM 3165 O O . PRO A 1 411 ? -16.539 44.303 49.856 1.00 28.81 ? 411 PRO A O 1 ATOM 3166 C CB . PRO A 1 411 ? -18.417 43.846 52.664 1.00 29.81 ? 411 PRO A CB 1 ATOM 3167 C CG . PRO A 1 411 ? -19.215 42.789 53.383 1.00 30.08 ? 411 PRO A CG 1 ATOM 3168 C CD . PRO A 1 411 ? -18.308 41.565 53.272 1.00 28.88 ? 411 PRO A CD 1 ATOM 3169 N N . LYS A 1 412 ? -15.462 43.491 51.637 1.00 28.22 ? 412 LYS A N 1 ATOM 3170 C CA . LYS A 1 412 ? -14.207 44.141 51.297 1.00 28.05 ? 412 LYS A CA 1 ATOM 3171 C C . LYS A 1 412 ? -13.086 43.304 51.863 1.00 27.21 ? 412 LYS A C 1 ATOM 3172 O O . LYS A 1 412 ? -13.163 42.862 53.004 1.00 27.22 ? 412 LYS A O 1 ATOM 3173 C CB . LYS A 1 412 ? -14.190 45.528 51.917 1.00 29.28 ? 412 LYS A CB 1 ATOM 3174 C CG . LYS A 1 412 ? -13.134 46.479 51.436 1.00 29.64 ? 412 LYS A CG 1 ATOM 3175 C CD . LYS A 1 412 ? -13.434 47.840 52.084 1.00 31.09 ? 412 LYS A CD 1 ATOM 3176 C CE . LYS A 1 412 ? -12.326 48.822 51.825 1.00 32.73 ? 412 LYS A CE 1 ATOM 3177 N NZ . LYS A 1 412 ? -12.586 50.112 52.502 1.00 33.13 ? 412 LYS A NZ 1 ATOM 3178 N N . ILE A 1 413 ? -12.060 43.054 51.056 1.00 25.88 ? 413 ILE A N 1 ATOM 3179 C CA . ILE A 1 413 ? -10.925 42.264 51.511 1.00 25.07 ? 413 ILE A CA 1 ATOM 3180 C C . ILE A 1 413 ? -9.617 42.969 51.151 1.00 25.14 ? 413 ILE A C 1 ATOM 3181 O O . ILE A 1 413 ? -9.590 43.821 50.246 1.00 25.34 ? 413 ILE A O 1 ATOM 3182 C CB . ILE A 1 413 ? -10.955 40.799 50.936 1.00 24.49 ? 413 ILE A CB 1 ATOM 3183 C CG1 . ILE A 1 413 ? -10.685 40.784 49.416 1.00 24.24 ? 413 ILE A CG1 1 ATOM 3184 C CG2 . ILE A 1 413 ? -12.285 40.107 51.287 1.00 24.38 ? 413 ILE A CG2 1 ATOM 3185 C CD1 . ILE A 1 413 ? -10.328 39.397 48.852 1.00 22.86 ? 413 ILE A CD1 1 ATOM 3186 N N . LEU A 1 414 ? -8.548 42.614 51.862 1.00 24.48 ? 414 LEU A N 1 ATOM 3187 C CA . LEU A 1 414 ? -7.227 43.201 51.640 1.00 24.08 ? 414 LEU A CA 1 ATOM 3188 C C . LEU A 1 414 ? -6.197 42.187 51.130 1.00 23.42 ? 414 LEU A C 1 ATOM 3189 O O . LEU A 1 414 ? -6.041 41.110 51.698 1.00 23.12 ? 414 LEU A O 1 ATOM 3190 C CB . LEU A 1 414 ? -6.714 43.864 52.930 1.00 24.42 ? 414 LEU A CB 1 ATOM 3191 C CG . LEU A 1 414 ? -5.305 44.465 52.940 1.00 24.04 ? 414 LEU A CG 1 ATOM 3192 C CD1 . LEU A 1 414 ? -5.188 45.623 51.966 1.00 23.91 ? 414 LEU A CD1 1 ATOM 3193 C CD2 . LEU A 1 414 ? -4.918 44.915 54.342 1.00 24.70 ? 414 LEU A CD2 1 ATOM 3194 N N . VAL A 1 415 ? -5.501 42.546 50.053 1.00 23.49 ? 415 VAL A N 1 ATOM 3195 C CA . VAL A 1 415 ? -4.350 41.778 49.562 1.00 23.27 ? 415 VAL A CA 1 ATOM 3196 C C . VAL A 1 415 ? -3.143 42.679 49.794 1.00 23.75 ? 415 VAL A C 1 ATOM 3197 O O . VAL A 1 415 ? -3.181 43.863 49.442 1.00 24.18 ? 415 VAL A O 1 ATOM 3198 C CB . VAL A 1 415 ? -4.518 41.352 48.054 1.00 23.32 ? 415 VAL A CB 1 ATOM 3199 C CG1 . VAL A 1 415 ? -3.293 40.612 47.519 1.00 22.02 ? 415 VAL A CG1 1 ATOM 3200 C CG2 . VAL A 1 415 ? -5.743 40.464 47.878 1.00 23.37 ? 415 VAL A CG2 1 ATOM 3201 N N . ALA A 1 416 ? -2.090 42.129 50.410 1.00 22.83 ? 416 ALA A N 1 ATOM 3202 C CA . ALA A 1 416 ? -0.953 42.932 50.855 1.00 22.59 ? 416 ALA A CA 1 ATOM 3203 C C . ALA A 1 416 ? 0.357 42.160 50.787 1.00 22.21 ? 416 ALA A C 1 ATOM 3204 O O . ALA A 1 416 ? 0.363 40.931 50.701 1.00 21.31 ? 416 ALA A O 1 ATOM 3205 C CB . ALA A 1 416 ? -1.192 43.444 52.307 1.00 22.94 ? 416 ALA A CB 1 ATOM 3206 N N . GLY A 1 417 ? 1.465 42.891 50.867 1.00 22.81 ? 417 GLY A N 1 ATOM 3207 C CA . GLY A 1 417 ? 2.778 42.277 50.923 1.00 22.49 ? 417 GLY A CA 1 ATOM 3208 C C . GLY A 1 417 ? 3.549 42.472 49.621 1.00 23.15 ? 417 GLY A C 1 ATOM 3209 O O . GLY A 1 417 ? 2.966 42.667 48.537 1.00 23.21 ? 417 GLY A O 1 ATOM 3210 N N . SER A 1 418 ? 4.868 42.421 49.750 1.00 22.74 ? 418 SER A N 1 ATOM 3211 C CA . SER A 1 418 ? 5.802 42.557 48.648 1.00 23.30 ? 418 SER A CA 1 ATOM 3212 C C . SER A 1 418 ? 5.668 41.428 47.617 1.00 22.66 ? 418 SER A C 1 ATOM 3213 O O . SER A 1 418 ? 6.128 41.550 46.471 1.00 22.99 ? 418 SER A O 1 ATOM 3214 C CB . SER A 1 418 ? 7.211 42.522 49.227 1.00 23.18 ? 418 SER A CB 1 ATOM 3215 O OG . SER A 1 418 ? 7.382 41.328 49.976 1.00 22.86 ? 418 SER A OG 1 ATOM 3216 N N . HIS A 1 419 ? 5.066 40.315 48.024 1.00 22.35 ? 419 HIS A N 1 ATOM 3217 C CA . HIS A 1 419 ? 4.994 39.140 47.140 1.00 22.31 ? 419 HIS A CA 1 ATOM 3218 C C . HIS A 1 419 ? 3.587 38.877 46.623 1.00 22.33 ? 419 HIS A C 1 ATOM 3219 O O . HIS A 1 419 ? 3.372 37.872 45.945 1.00 22.60 ? 419 HIS A O 1 ATOM 3220 C CB . HIS A 1 419 ? 5.544 37.886 47.841 1.00 21.20 ? 419 HIS A CB 1 ATOM 3221 C CG . HIS A 1 419 ? 7.021 37.917 48.060 1.00 22.86 ? 419 HIS A CG 1 ATOM 3222 N ND1 . HIS A 1 419 ? 7.655 38.934 48.746 1.00 22.24 ? 419 HIS A ND1 1 ATOM 3223 C CD2 . HIS A 1 419 ? 7.996 37.070 47.658 1.00 22.29 ? 419 HIS A CD2 1 ATOM 3224 C CE1 . HIS A 1 419 ? 8.954 38.703 48.766 1.00 22.00 ? 419 HIS A CE1 1 ATOM 3225 N NE2 . HIS A 1 419 ? 9.186 37.576 48.116 1.00 22.34 ? 419 HIS A NE2 1 ATOM 3226 N N . ALA A 1 420 ? 2.641 39.765 46.952 1.00 22.68 ? 420 ALA A N 1 ATOM 3227 C CA . ALA A 1 420 ? 1.240 39.605 46.549 1.00 22.79 ? 420 ALA A CA 1 ATOM 3228 C C . ALA A 1 420 ? 0.996 39.894 45.068 1.00 22.83 ? 420 ALA A C 1 ATOM 3229 O O . ALA A 1 420 ? 0.106 39.291 44.440 1.00 22.30 ? 420 ALA A O 1 ATOM 3230 C CB . ALA A 1 420 ? 0.337 40.481 47.405 1.00 23.19 ? 420 ALA A CB 1 ATOM 3231 N N . ASP A 1 421 ? 1.767 40.836 44.518 1.00 22.89 ? 421 ASP A N 1 ATOM 3232 C CA . ASP A 1 421 ? 1.613 41.230 43.128 1.00 22.97 ? 421 ASP A CA 1 ATOM 3233 C C . ASP A 1 421 ? 2.990 41.323 42.467 1.00 23.29 ? 421 ASP A C 1 ATOM 3234 O O . ASP A 1 421 ? 3.383 42.372 41.954 1.00 24.60 ? 421 ASP A O 1 ATOM 3235 C CB . ASP A 1 421 ? 0.851 42.562 43.016 1.00 23.12 ? 421 ASP A CB 1 ATOM 3236 C CG . ASP A 1 421 ? 0.412 42.865 41.586 1.00 24.21 ? 421 ASP A CG 1 ATOM 3237 O OD1 . ASP A 1 421 ? 0.019 41.923 40.857 1.00 23.33 ? 421 ASP A OD1 1 ATOM 3238 O OD2 . ASP A 1 421 ? 0.469 44.038 41.184 1.00 27.12 ? 421 ASP A OD2 1 ATOM 3239 N N . ASN A 1 422 ? 3.726 40.220 42.493 1.00 22.72 ? 422 ASN A N 1 ATOM 3240 C CA . ASN A 1 422 ? 5.077 40.195 41.930 1.00 22.58 ? 422 ASN A CA 1 ATOM 3241 C C . ASN A 1 422 ? 5.382 38.828 41.335 1.00 22.20 ? 422 ASN A C 1 ATOM 3242 O O . ASN A 1 422 ? 5.743 37.876 42.051 1.00 20.71 ? 422 ASN A O 1 ATOM 3243 C CB . ASN A 1 422 ? 6.128 40.575 42.988 1.00 22.03 ? 422 ASN A CB 1 ATOM 3244 C CG . ASN A 1 422 ? 7.484 40.865 42.371 1.00 22.26 ? 422 ASN A CG 1 ATOM 3245 O OD1 . ASN A 1 422 ? 7.909 40.162 41.466 1.00 23.22 ? 422 ASN A OD1 1 ATOM 3246 N ND2 . ASN A 1 422 ? 8.167 41.899 42.859 1.00 21.24 ? 422 ASN A ND2 1 ATOM 3247 N N . LEU A 1 423 ? 5.206 38.749 40.021 1.00 22.45 ? 423 LEU A N 1 ATOM 3248 C CA . LEU A 1 423 ? 5.321 37.498 39.294 1.00 22.92 ? 423 LEU A CA 1 ATOM 3249 C C . LEU A 1 423 ? 6.722 36.928 39.361 1.00 22.38 ? 423 LEU A C 1 ATOM 3250 O O . LEU A 1 423 ? 6.881 35.732 39.558 1.00 22.40 ? 423 LEU A O 1 ATOM 3251 C CB . LEU A 1 423 ? 4.888 37.669 37.823 1.00 22.61 ? 423 LEU A CB 1 ATOM 3252 C CG . LEU A 1 423 ? 4.780 36.402 36.965 1.00 24.25 ? 423 LEU A CG 1 ATOM 3253 C CD1 . LEU A 1 423 ? 3.790 35.374 37.537 1.00 22.80 ? 423 LEU A CD1 1 ATOM 3254 C CD2 . LEU A 1 423 ? 4.401 36.764 35.548 1.00 23.85 ? 423 LEU A CD2 1 ATOM 3255 N N . GLY A 1 424 ? 7.723 37.782 39.159 1.00 23.34 ? 424 GLY A N 1 ATOM 3256 C CA . GLY A 1 424 ? 9.124 37.376 39.255 1.00 23.38 ? 424 GLY A CA 1 ATOM 3257 C C . GLY A 1 424 ? 9.454 36.763 40.608 1.00 22.73 ? 424 GLY A C 1 ATOM 3258 O O . GLY A 1 424 ? 10.109 35.721 40.672 1.00 22.32 ? 424 GLY A O 1 ATOM 3259 N N . TYR A 1 425 ? 9.001 37.405 41.690 1.00 22.70 ? 425 TYR A N 1 ATOM 3260 C CA . TYR A 1 425 ? 9.214 36.871 43.039 1.00 22.62 ? 425 TYR A CA 1 ATOM 3261 C C . TYR A 1 425 ? 8.577 35.495 43.236 1.00 22.63 ? 425 TYR A C 1 ATOM 3262 O O . TYR A 1 425 ? 9.160 34.646 43.909 1.00 22.76 ? 425 TYR A O 1 ATOM 3263 C CB . TYR A 1 425 ? 8.672 37.819 44.108 1.00 21.92 ? 425 TYR A CB 1 ATOM 3264 C CG . TYR A 1 425 ? 9.535 39.022 44.409 1.00 22.48 ? 425 TYR A CG 1 ATOM 3265 C CD1 . TYR A 1 425 ? 9.214 39.864 45.467 1.00 22.15 ? 425 TYR A CD1 1 ATOM 3266 C CD2 . TYR A 1 425 ? 10.686 39.307 43.660 1.00 22.23 ? 425 TYR A CD2 1 ATOM 3267 C CE1 . TYR A 1 425 ? 9.993 40.970 45.769 1.00 23.49 ? 425 TYR A CE1 1 ATOM 3268 C CE2 . TYR A 1 425 ? 11.487 40.409 43.959 1.00 23.82 ? 425 TYR A CE2 1 ATOM 3269 C CZ . TYR A 1 425 ? 11.125 41.244 45.012 1.00 24.07 ? 425 TYR A CZ 1 ATOM 3270 O OH . TYR A 1 425 ? 11.889 42.353 45.319 1.00 26.31 ? 425 TYR A OH 1 ATOM 3271 N N . GLN A 1 426 ? 7.374 35.282 42.692 1.00 22.48 ? 426 GLN A N 1 ATOM 3272 C CA . GLN A 1 426 ? 6.695 33.989 42.894 1.00 22.47 ? 426 GLN A CA 1 ATOM 3273 C C . GLN A 1 426 ? 7.285 32.852 42.038 1.00 21.59 ? 426 GLN A C 1 ATOM 3274 O O . GLN A 1 426 ? 7.037 31.676 42.303 1.00 20.99 ? 426 GLN A O 1 ATOM 3275 C CB . GLN A 1 426 ? 5.166 34.110 42.734 1.00 22.38 ? 426 GLN A CB 1 ATOM 3276 C CG . GLN A 1 426 ? 4.651 34.108 41.332 1.00 22.93 ? 426 GLN A CG 1 ATOM 3277 C CD . GLN A 1 426 ? 3.127 34.326 41.239 1.00 24.28 ? 426 GLN A CD 1 ATOM 3278 O OE1 . GLN A 1 426 ? 2.571 35.210 41.894 1.00 25.75 ? 426 GLN A OE1 1 ATOM 3279 N NE2 . GLN A 1 426 ? 2.459 33.525 40.404 1.00 23.46 ? 426 GLN A NE2 1 ATOM 3280 N N . CYS A 1 427 ? 8.080 33.213 41.029 1.00 21.26 ? 427 CYS A N 1 ATOM 3281 C CA . CYS A 1 427 ? 8.775 32.235 40.185 1.00 21.03 ? 427 CYS A CA 1 ATOM 3282 C C . CYS A 1 427 ? 10.156 31.876 40.736 1.00 21.38 ? 427 CYS A C 1 ATOM 3283 O O . CYS A 1 427 ? 10.613 30.734 40.586 1.00 22.07 ? 427 CYS A O 1 ATOM 3284 C CB . CYS A 1 427 ? 8.905 32.757 38.745 1.00 21.23 ? 427 CYS A CB 1 ATOM 3285 S SG . CYS A 1 427 ? 7.340 32.851 37.863 1.00 21.77 ? 427 CYS A SG 1 ATOM 3286 N N . GLY A 1 428 ? 10.805 32.842 41.391 1.00 21.35 ? 428 GLY A N 1 ATOM 3287 C CA . GLY A 1 428 ? 12.135 32.644 41.952 1.00 20.71 ? 428 GLY A CA 1 ATOM 3288 C C . GLY A 1 428 ? 13.192 32.578 40.861 1.00 21.39 ? 428 GLY A C 1 ATOM 3289 O O . GLY A 1 428 ? 12.963 33.021 39.713 1.00 21.11 ? 428 GLY A O 1 ATOM 3290 N N . GLY A 1 429 ? 14.336 31.993 41.211 1.00 20.94 ? 429 GLY A N 1 ATOM 3291 C CA . GLY A 1 429 ? 15.484 31.907 40.308 1.00 20.83 ? 429 GLY A CA 1 ATOM 3292 C C . GLY A 1 429 ? 15.216 31.046 39.085 1.00 20.76 ? 429 GLY A C 1 ATOM 3293 O O . GLY A 1 429 ? 14.200 30.325 39.028 1.00 20.05 ? 429 GLY A O 1 ATOM 3294 N N . TRP A 1 430 ? 16.130 31.121 38.109 1.00 21.10 ? 430 TRP A N 1 ATOM 3295 C CA . TRP A 1 430 ? 15.981 30.435 36.821 1.00 20.78 ? 430 TRP A CA 1 ATOM 3296 C C . TRP A 1 430 ? 14.631 30.756 36.187 1.00 21.07 ? 430 TRP A C 1 ATOM 3297 O O . TRP A 1 430 ? 13.874 29.843 35.825 1.00 20.66 ? 430 TRP A O 1 ATOM 3298 C CB . TRP A 1 430 ? 16.073 28.926 36.997 1.00 20.98 ? 430 TRP A CB 1 ATOM 3299 C CG . TRP A 1 430 ? 17.418 28.379 37.386 1.00 21.25 ? 430 TRP A CG 1 ATOM 3300 C CD1 . TRP A 1 430 ? 17.747 27.822 38.583 1.00 21.45 ? 430 TRP A CD1 1 ATOM 3301 C CD2 . TRP A 1 430 ? 18.595 28.291 36.563 1.00 22.44 ? 430 TRP A CD2 1 ATOM 3302 N NE1 . TRP A 1 430 ? 19.054 27.402 38.572 1.00 22.46 ? 430 TRP A NE1 1 ATOM 3303 C CE2 . TRP A 1 430 ? 19.605 27.685 37.349 1.00 22.95 ? 430 TRP A CE2 1 ATOM 3304 C CE3 . TRP A 1 430 ? 18.902 28.683 35.251 1.00 22.54 ? 430 TRP A CE3 1 ATOM 3305 C CZ2 . TRP A 1 430 ? 20.901 27.443 36.860 1.00 23.20 ? 430 TRP A CZ2 1 ATOM 3306 C CZ3 . TRP A 1 430 ? 20.199 28.452 34.767 1.00 23.05 ? 430 TRP A CZ3 1 ATOM 3307 C CH2 . TRP A 1 430 ? 21.179 27.838 35.570 1.00 23.23 ? 430 TRP A CH2 1 ATOM 3308 N N . THR A 1 431 ? 14.301 32.039 36.110 1.00 20.45 ? 431 THR A N 1 ATOM 3309 C CA . THR A 1 431 ? 13.095 32.470 35.402 1.00 20.52 ? 431 THR A CA 1 ATOM 3310 C C . THR A 1 431 ? 13.422 33.727 34.623 1.00 21.11 ? 431 THR A C 1 ATOM 3311 O O . THR A 1 431 ? 13.666 34.788 35.216 1.00 21.10 ? 431 THR A O 1 ATOM 3312 C CB . THR A 1 431 ? 11.886 32.730 36.345 1.00 20.04 ? 431 THR A CB 1 ATOM 3313 O OG1 . THR A 1 431 ? 11.800 31.679 37.316 1.00 19.65 ? 431 THR A OG1 1 ATOM 3314 C CG2 . THR A 1 431 ? 10.597 32.776 35.534 1.00 18.47 ? 431 THR A CG2 1 ATOM 3315 N N . ILE A 1 432 ? 13.475 33.577 33.299 1.00 21.33 ? 432 ILE A N 1 ATOM 3316 C CA . ILE A 1 432 ? 13.807 34.652 32.373 1.00 22.41 ? 432 ILE A CA 1 ATOM 3317 C C . ILE A 1 432 ? 15.289 35.030 32.484 1.00 23.45 ? 432 ILE A C 1 ATOM 3318 O O . ILE A 1 432 ? 16.038 34.892 31.509 1.00 23.88 ? 432 ILE A O 1 ATOM 3319 C CB . ILE A 1 432 ? 12.833 35.885 32.470 1.00 22.95 ? 432 ILE A CB 1 ATOM 3320 C CG1 . ILE A 1 432 ? 11.369 35.438 32.292 1.00 21.44 ? 432 ILE A CG1 1 ATOM 3321 C CG2 . ILE A 1 432 ? 13.253 37.019 31.476 1.00 22.69 ? 432 ILE A CG2 1 ATOM 3322 C CD1 . ILE A 1 432 ? 11.050 34.797 30.962 1.00 23.15 ? 432 ILE A CD1 1 ATOM 3323 N N . GLU A 1 433 ? 15.704 35.491 33.662 1.00 23.68 ? 433 GLU A N 1 ATOM 3324 C CA . GLU A 1 433 ? 17.116 35.701 33.952 1.00 24.92 ? 433 GLU A CA 1 ATOM 3325 C C . GLU A 1 433 ? 17.649 34.495 34.718 1.00 24.49 ? 433 GLU A C 1 ATOM 3326 O O . GLU A 1 433 ? 16.878 33.721 35.288 1.00 24.32 ? 433 GLU A O 1 ATOM 3327 C CB . GLU A 1 433 ? 17.330 36.994 34.769 1.00 25.90 ? 433 GLU A CB 1 ATOM 3328 C CG . GLU A 1 433 ? 16.728 38.265 34.136 1.00 27.91 ? 433 GLU A CG 1 ATOM 3329 C CD . GLU A 1 433 ? 17.413 38.712 32.845 1.00 32.10 ? 433 GLU A CD 1 ATOM 3330 O OE1 . GLU A 1 433 ? 18.516 38.208 32.493 1.00 33.34 ? 433 GLU A OE1 1 ATOM 3331 O OE2 . GLU A 1 433 ? 16.831 39.591 32.170 1.00 34.17 ? 433 GLU A OE2 1 ATOM 3332 N N . TRP A 1 434 ? 18.967 34.328 34.713 1.00 24.74 ? 434 TRP A N 1 ATOM 3333 C CA . TRP A 1 434 ? 19.625 33.322 35.542 1.00 24.33 ? 434 TRP A CA 1 ATOM 3334 C C . TRP A 1 434 ? 19.193 33.417 37.019 1.00 24.43 ? 434 TRP A C 1 ATOM 3335 O O . TRP A 1 434 ? 18.787 32.417 37.634 1.00 23.21 ? 434 TRP A O 1 ATOM 3336 C CB . TRP A 1 434 ? 21.146 33.497 35.405 1.00 25.15 ? 434 TRP A CB 1 ATOM 3337 C CG . TRP A 1 434 ? 21.996 32.597 36.258 1.00 24.79 ? 434 TRP A CG 1 ATOM 3338 C CD1 . TRP A 1 434 ? 21.832 31.252 36.459 1.00 23.80 ? 434 TRP A CD1 1 ATOM 3339 C CD2 . TRP A 1 434 ? 23.170 32.976 36.993 1.00 25.43 ? 434 TRP A CD2 1 ATOM 3340 N NE1 . TRP A 1 434 ? 22.827 30.777 37.278 1.00 23.88 ? 434 TRP A NE1 1 ATOM 3341 C CE2 . TRP A 1 434 ? 23.660 31.809 37.625 1.00 25.23 ? 434 TRP A CE2 1 ATOM 3342 C CE3 . TRP A 1 434 ? 23.854 34.195 37.186 1.00 26.11 ? 434 TRP A CE3 1 ATOM 3343 C CZ2 . TRP A 1 434 ? 24.803 31.817 38.440 1.00 26.31 ? 434 TRP A CZ2 1 ATOM 3344 C CZ3 . TRP A 1 434 ? 24.989 34.211 37.999 1.00 26.55 ? 434 TRP A CZ3 1 ATOM 3345 C CH2 . TRP A 1 434 ? 25.462 33.021 38.609 1.00 27.18 ? 434 TRP A CH2 1 ATOM 3346 N N . GLN A 1 435 ? 19.271 34.633 37.572 1.00 24.77 ? 435 GLN A N 1 ATOM 3347 C CA . GLN A 1 435 ? 18.999 34.873 38.981 1.00 24.93 ? 435 GLN A CA 1 ATOM 3348 C C . GLN A 1 435 ? 17.507 35.038 39.288 1.00 24.61 ? 435 GLN A C 1 ATOM 3349 O O . GLN A 1 435 ? 17.136 35.215 40.435 1.00 25.24 ? 435 GLN A O 1 ATOM 3350 C CB . GLN A 1 435 ? 19.790 36.100 39.477 1.00 25.75 ? 435 GLN A CB 1 ATOM 3351 C CG . GLN A 1 435 ? 21.302 35.865 39.668 1.00 25.13 ? 435 GLN A CG 1 ATOM 3352 C CD . GLN A 1 435 ? 21.608 34.857 40.772 1.00 26.06 ? 435 GLN A CD 1 ATOM 3353 O OE1 . GLN A 1 435 ? 20.955 34.843 41.841 1.00 24.39 ? 435 GLN A OE1 1 ATOM 3354 N NE2 . GLN A 1 435 ? 22.599 33.998 40.523 1.00 24.62 ? 435 GLN A NE2 1 ATOM 3355 N N . GLY A 1 436 ? 16.658 34.929 38.267 1.00 24.63 ? 436 GLY A N 1 ATOM 3356 C CA . GLY A 1 436 ? 15.279 35.389 38.348 1.00 23.99 ? 436 GLY A CA 1 ATOM 3357 C C . GLY A 1 436 ? 15.275 36.907 38.359 1.00 24.70 ? 436 GLY A C 1 ATOM 3358 O O . GLY A 1 436 ? 16.294 37.543 38.097 1.00 25.40 ? 436 GLY A O 1 ATOM 3359 N N . ASP A 1 437 ? 14.137 37.501 38.678 1.00 24.67 ? 437 ASP A N 1 ATOM 3360 C CA . ASP A 1 437 ? 14.007 38.935 38.550 1.00 25.74 ? 437 ASP A CA 1 ATOM 3361 C C . ASP A 1 437 ? 12.733 39.371 39.260 1.00 25.15 ? 437 ASP A C 1 ATOM 3362 O O . ASP A 1 437 ? 11.988 38.546 39.777 1.00 24.44 ? 437 ASP A O 1 ATOM 3363 C CB . ASP A 1 437 ? 13.976 39.326 37.059 1.00 26.33 ? 437 ASP A CB 1 ATOM 3364 C CG . ASP A 1 437 ? 14.360 40.787 36.813 1.00 29.60 ? 437 ASP A CG 1 ATOM 3365 O OD1 . ASP A 1 437 ? 14.558 41.564 37.772 1.00 33.02 ? 437 ASP A OD1 1 ATOM 3366 O OD2 . ASP A 1 437 ? 14.467 41.159 35.640 1.00 32.52 ? 437 ASP A OD2 1 ATOM 3367 N N . THR A 1 438 ? 12.497 40.676 39.277 1.00 25.16 ? 438 THR A N 1 ATOM 3368 C CA . THR A 1 438 ? 11.367 41.248 39.971 1.00 24.37 ? 438 THR A CA 1 ATOM 3369 C C . THR A 1 438 ? 10.291 41.712 38.974 1.00 24.83 ? 438 THR A C 1 ATOM 3370 O O . THR A 1 438 ? 10.608 42.158 37.871 1.00 25.66 ? 438 THR A O 1 ATOM 3371 C CB . THR A 1 438 ? 11.824 42.418 40.873 1.00 24.66 ? 438 THR A CB 1 ATOM 3372 O OG1 . THR A 1 438 ? 10.692 42.959 41.554 1.00 24.70 ? 438 THR A OG1 1 ATOM 3373 C CG2 . THR A 1 438 ? 12.547 43.541 40.045 1.00 25.41 ? 438 THR A CG2 1 ATOM 3374 N N . GLY A 1 439 ? 9.023 41.587 39.358 1.00 24.25 ? 439 GLY A N 1 ATOM 3375 C CA . GLY A 1 439 ? 7.941 42.224 38.605 1.00 25.21 ? 439 GLY A CA 1 ATOM 3376 C C . GLY A 1 439 ? 7.422 41.337 37.490 1.00 25.65 ? 439 GLY A C 1 ATOM 3377 O O . GLY A 1 439 ? 7.541 40.109 37.549 1.00 24.96 ? 439 GLY A O 1 ATOM 3378 N N . ARG A 1 440 ? 6.859 41.967 36.469 1.00 26.61 ? 440 ARG A N 1 ATOM 3379 C CA . ARG A 1 440 ? 6.129 41.270 35.423 1.00 28.05 ? 440 ARG A CA 1 ATOM 3380 C C . ARG A 1 440 ? 7.075 40.880 34.272 1.00 27.98 ? 440 ARG A C 1 ATOM 3381 O O . ARG A 1 440 ? 7.136 41.531 33.225 1.00 29.26 ? 440 ARG A O 1 ATOM 3382 C CB . ARG A 1 440 ? 4.936 42.127 34.963 1.00 28.89 ? 440 ARG A CB 1 ATOM 3383 C CG . ARG A 1 440 ? 4.071 41.494 33.901 1.00 33.53 ? 440 ARG A CG 1 ATOM 3384 C CD . ARG A 1 440 ? 2.599 41.869 34.074 1.00 41.04 ? 440 ARG A CD 1 ATOM 3385 N NE . ARG A 1 440 ? 1.876 40.678 34.521 1.00 46.33 ? 440 ARG A NE 1 ATOM 3386 C CZ . ARG A 1 440 ? 1.633 40.326 35.787 1.00 46.22 ? 440 ARG A CZ 1 ATOM 3387 N NH1 . ARG A 1 440 ? 2.015 41.097 36.813 1.00 45.47 ? 440 ARG A NH1 1 ATOM 3388 N NH2 . ARG A 1 440 ? 0.987 39.182 36.013 1.00 44.67 ? 440 ARG A NH2 1 ATOM 3389 N N . THR A 1 441 ? 7.819 39.806 34.495 1.00 27.31 ? 441 THR A N 1 ATOM 3390 C CA . THR A 1 441 ? 8.898 39.398 33.591 1.00 27.04 ? 441 THR A CA 1 ATOM 3391 C C . THR A 1 441 ? 8.420 38.426 32.509 1.00 26.23 ? 441 THR A C 1 ATOM 3392 O O . THR A 1 441 ? 9.157 38.118 31.577 1.00 26.05 ? 441 THR A O 1 ATOM 3393 C CB . THR A 1 441 ? 10.027 38.724 34.390 1.00 26.83 ? 441 THR A CB 1 ATOM 3394 O OG1 . THR A 1 441 ? 9.498 37.593 35.099 1.00 27.20 ? 441 THR A OG1 1 ATOM 3395 C CG2 . THR A 1 441 ? 10.640 39.711 35.392 1.00 27.38 ? 441 THR A CG2 1 ATOM 3396 N N . THR A 1 442 ? 7.194 37.925 32.654 1.00 24.96 ? 442 THR A N 1 ATOM 3397 C CA . THR A 1 442 ? 6.679 36.910 31.737 1.00 24.43 ? 442 THR A CA 1 ATOM 3398 C C . THR A 1 442 ? 5.148 36.875 31.786 1.00 24.61 ? 442 THR A C 1 ATOM 3399 O O . THR A 1 442 ? 4.531 37.747 32.402 1.00 24.37 ? 442 THR A O 1 ATOM 3400 C CB . THR A 1 442 ? 7.363 35.520 31.967 1.00 23.41 ? 442 THR A CB 1 ATOM 3401 O OG1 . THR A 1 442 ? 7.100 34.666 30.853 1.00 24.04 ? 442 THR A OG1 1 ATOM 3402 C CG2 . THR A 1 442 ? 6.918 34.870 33.263 1.00 20.76 ? 442 THR A CG2 1 ATOM 3403 N N . VAL A 1 443 ? 4.543 35.915 31.089 1.00 24.64 ? 443 VAL A N 1 ATOM 3404 C CA . VAL A 1 443 ? 3.094 35.736 31.122 1.00 24.74 ? 443 VAL A CA 1 ATOM 3405 C C . VAL A 1 443 ? 2.740 34.870 32.336 1.00 23.98 ? 443 VAL A C 1 ATOM 3406 O O . VAL A 1 443 ? 3.319 33.787 32.529 1.00 23.90 ? 443 VAL A O 1 ATOM 3407 C CB . VAL A 1 443 ? 2.530 35.111 29.807 1.00 25.05 ? 443 VAL A CB 1 ATOM 3408 C CG1 . VAL A 1 443 ? 1.029 34.855 29.938 1.00 24.80 ? 443 VAL A CG1 1 ATOM 3409 C CG2 . VAL A 1 443 ? 2.800 36.025 28.604 1.00 26.41 ? 443 VAL A CG2 1 ATOM 3410 N N . GLY A 1 444 ? 1.797 35.354 33.141 1.00 23.79 ? 444 GLY A N 1 ATOM 3411 C CA . GLY A 1 444 ? 1.435 34.718 34.394 1.00 23.34 ? 444 GLY A CA 1 ATOM 3412 C C . GLY A 1 444 ? 0.330 35.438 35.139 1.00 23.83 ? 444 GLY A C 1 ATOM 3413 O O . GLY A 1 444 ? -0.233 36.413 34.638 1.00 24.42 ? 444 GLY A O 1 ATOM 3414 N N . THR A 1 445 ? 0.010 34.910 36.324 1.00 23.35 ? 445 THR A N 1 ATOM 3415 C CA . THR A 1 445 ? -1.044 35.413 37.188 1.00 23.37 ? 445 THR A CA 1 ATOM 3416 C C . THR A 1 445 ? -0.482 35.545 38.604 1.00 22.90 ? 445 THR A C 1 ATOM 3417 O O . THR A 1 445 ? -0.083 34.544 39.220 1.00 22.51 ? 445 THR A O 1 ATOM 3418 C CB . THR A 1 445 ? -2.300 34.469 37.166 1.00 23.18 ? 445 THR A CB 1 ATOM 3419 O OG1 . THR A 1 445 ? -2.788 34.371 35.823 1.00 24.07 ? 445 THR A OG1 1 ATOM 3420 C CG2 . THR A 1 445 ? -3.408 35.017 38.028 1.00 23.16 ? 445 THR A CG2 1 ATOM 3421 N N . THR A 1 446 ? -0.410 36.780 39.109 1.00 22.67 ? 446 THR A N 1 ATOM 3422 C CA . THR A 1 446 ? 0.080 36.993 40.468 1.00 22.59 ? 446 THR A CA 1 ATOM 3423 C C . THR A 1 446 ? -0.983 36.546 41.487 1.00 22.09 ? 446 THR A C 1 ATOM 3424 O O . THR A 1 446 ? -2.121 36.249 41.126 1.00 22.50 ? 446 THR A O 1 ATOM 3425 C CB . THR A 1 446 ? 0.503 38.469 40.732 1.00 23.12 ? 446 THR A CB 1 ATOM 3426 O OG1 . THR A 1 446 ? -0.643 39.329 40.636 1.00 24.61 ? 446 THR A OG1 1 ATOM 3427 C CG2 . THR A 1 446 ? 1.595 38.936 39.722 1.00 22.06 ? 446 THR A CG2 1 ATOM 3428 N N . ILE A 1 447 ? -0.611 36.512 42.756 1.00 21.61 ? 447 ILE A N 1 ATOM 3429 C CA . ILE A 1 447 ? -1.575 36.209 43.815 1.00 21.64 ? 447 ILE A CA 1 ATOM 3430 C C . ILE A 1 447 ? -2.731 37.227 43.825 1.00 22.38 ? 447 ILE A C 1 ATOM 3431 O O . ILE A 1 447 ? -3.896 36.835 43.904 1.00 22.74 ? 447 ILE A O 1 ATOM 3432 C CB . ILE A 1 447 ? -0.863 36.055 45.188 1.00 21.27 ? 447 ILE A CB 1 ATOM 3433 C CG1 . ILE A 1 447 ? 0.037 34.807 45.155 1.00 19.78 ? 447 ILE A CG1 1 ATOM 3434 C CG2 . ILE A 1 447 ? -1.866 35.955 46.335 1.00 21.01 ? 447 ILE A CG2 1 ATOM 3435 C CD1 . ILE A 1 447 ? 1.099 34.756 46.273 1.00 20.00 ? 447 ILE A CD1 1 ATOM 3436 N N . LEU A 1 448 ? -2.411 38.518 43.705 1.00 22.80 ? 448 LEU A N 1 ATOM 3437 C CA . LEU A 1 448 ? -3.432 39.568 43.606 1.00 23.10 ? 448 LEU A CA 1 ATOM 3438 C C . LEU A 1 448 ? -4.411 39.317 42.448 1.00 23.95 ? 448 LEU A C 1 ATOM 3439 O O . LEU A 1 448 ? -5.637 39.359 42.629 1.00 24.21 ? 448 LEU A O 1 ATOM 3440 C CB . LEU A 1 448 ? -2.799 40.965 43.486 1.00 23.11 ? 448 LEU A CB 1 ATOM 3441 C CG . LEU A 1 448 ? -3.756 42.142 43.210 1.00 23.79 ? 448 LEU A CG 1 ATOM 3442 C CD1 . LEU A 1 448 ? -4.753 42.320 44.354 1.00 23.60 ? 448 LEU A CD1 1 ATOM 3443 C CD2 . LEU A 1 448 ? -3.009 43.440 42.949 1.00 25.02 ? 448 LEU A CD2 1 ATOM 3444 N N . GLU A 1 449 ? -3.861 39.048 41.272 1.00 23.94 ? 449 GLU A N 1 ATOM 3445 C CA . GLU A 1 449 ? -4.663 38.783 40.078 1.00 25.17 ? 449 GLU A CA 1 ATOM 3446 C C . GLU A 1 449 ? -5.508 37.526 40.260 1.00 24.13 ? 449 GLU A C 1 ATOM 3447 O O . GLU A 1 449 ? -6.660 37.475 39.822 1.00 24.58 ? 449 GLU A O 1 ATOM 3448 C CB . GLU A 1 449 ? -3.757 38.634 38.841 1.00 25.47 ? 449 GLU A CB 1 ATOM 3449 C CG . GLU A 1 449 ? -3.122 39.936 38.367 1.00 27.62 ? 449 GLU A CG 1 ATOM 3450 C CD . GLU A 1 449 ? -2.062 39.726 37.265 1.00 28.41 ? 449 GLU A CD 1 ATOM 3451 O OE1 . GLU A 1 449 ? -1.237 38.787 37.324 1.00 27.96 ? 449 GLU A OE1 1 ATOM 3452 O OE2 . GLU A 1 449 ? -2.066 40.521 36.309 1.00 35.85 ? 449 GLU A OE2 1 ATOM 3453 N N . ALA A 1 450 ? -4.924 36.514 40.895 1.00 22.89 ? 450 ALA A N 1 ATOM 3454 C CA . ALA A 1 450 ? -5.632 35.278 41.199 1.00 22.72 ? 450 ALA A CA 1 ATOM 3455 C C . ALA A 1 450 ? -6.802 35.544 42.154 1.00 22.56 ? 450 ALA A C 1 ATOM 3456 O O . ALA A 1 450 ? -7.901 35.005 41.967 1.00 23.08 ? 450 ALA A O 1 ATOM 3457 C CB . ALA A 1 450 ? -4.668 34.246 41.776 1.00 21.96 ? 450 ALA A CB 1 ATOM 3458 N N . VAL A 1 451 ? -6.580 36.410 43.143 1.00 21.84 ? 451 VAL A N 1 ATOM 3459 C CA . VAL A 1 451 ? -7.620 36.777 44.092 1.00 22.33 ? 451 VAL A CA 1 ATOM 3460 C C . VAL A 1 451 ? -8.786 37.481 43.366 1.00 23.41 ? 451 VAL A C 1 ATOM 3461 O O . VAL A 1 451 ? -9.950 37.111 43.546 1.00 23.55 ? 451 VAL A O 1 ATOM 3462 C CB . VAL A 1 451 ? -7.071 37.662 45.242 1.00 22.36 ? 451 VAL A CB 1 ATOM 3463 C CG1 . VAL A 1 451 ? -8.223 38.226 46.055 1.00 23.10 ? 451 VAL A CG1 1 ATOM 3464 C CG2 . VAL A 1 451 ? -6.120 36.852 46.151 1.00 21.54 ? 451 VAL A CG2 1 ATOM 3465 N N . LYS A 1 452 ? -8.450 38.468 42.530 1.00 23.97 ? 452 LYS A N 1 ATOM 3466 C CA . LYS A 1 452 ? -9.436 39.200 41.713 1.00 25.32 ? 452 LYS A CA 1 ATOM 3467 C C . LYS A 1 452 ? -10.229 38.303 40.758 1.00 25.61 ? 452 LYS A C 1 ATOM 3468 O O . LYS A 1 452 ? -11.436 38.519 40.549 1.00 26.31 ? 452 LYS A O 1 ATOM 3469 C CB . LYS A 1 452 ? -8.756 40.333 40.954 1.00 25.25 ? 452 LYS A CB 1 ATOM 3470 C CG . LYS A 1 452 ? -8.276 41.416 41.902 1.00 28.12 ? 452 LYS A CG 1 ATOM 3471 C CD . LYS A 1 452 ? -7.148 42.236 41.313 1.00 31.68 ? 452 LYS A CD 1 ATOM 3472 C CE . LYS A 1 452 ? -7.674 43.464 40.611 1.00 37.42 ? 452 LYS A CE 1 ATOM 3473 N NZ . LYS A 1 452 ? -6.642 44.562 40.690 1.00 40.03 ? 452 LYS A NZ 1 ATOM 3474 N N . ALA A 1 453 ? -9.553 37.291 40.210 1.00 24.97 ? 453 ALA A N 1 ATOM 3475 C CA . ALA A 1 453 ? -10.180 36.301 39.335 1.00 25.35 ? 453 ALA A CA 1 ATOM 3476 C C . ALA A 1 453 ? -11.043 35.264 40.071 1.00 25.30 ? 453 ALA A C 1 ATOM 3477 O O . ALA A 1 453 ? -11.835 34.571 39.430 1.00 26.25 ? 453 ALA A O 1 ATOM 3478 C CB . ALA A 1 453 ? -9.121 35.598 38.479 1.00 24.08 ? 453 ALA A CB 1 ATOM 3479 N N . ALA A 1 454 ? -10.906 35.174 41.395 1.00 24.57 ? 454 ALA A N 1 ATOM 3480 C CA . ALA A 1 454 ? -11.561 34.138 42.202 1.00 24.67 ? 454 ALA A CA 1 ATOM 3481 C C . ALA A 1 454 ? -12.819 34.612 42.921 1.00 25.87 ? 454 ALA A C 1 ATOM 3482 O O . ALA A 1 454 ? -13.800 33.873 43.036 1.00 26.81 ? 454 ALA A O 1 ATOM 3483 C CB . ALA A 1 454 ? -10.568 33.538 43.236 1.00 23.88 ? 454 ALA A CB 1 ATOM 3484 N N . VAL A 1 455 ? -12.791 35.843 43.409 1.00 25.51 ? 455 VAL A N 1 ATOM 3485 C CA . VAL A 1 455 ? -13.831 36.307 44.315 1.00 25.98 ? 455 VAL A CA 1 ATOM 3486 C C . VAL A 1 455 ? -15.126 36.677 43.585 1.00 26.83 ? 455 VAL A C 1 ATOM 3487 O O . VAL A 1 455 ? -15.116 36.998 42.387 1.00 26.73 ? 455 VAL A O 1 ATOM 3488 C CB . VAL A 1 455 ? -13.348 37.494 45.177 1.00 25.72 ? 455 VAL A CB 1 ATOM 3489 C CG1 . VAL A 1 455 ? -12.196 37.060 46.119 1.00 24.52 ? 455 VAL A CG1 1 ATOM 3490 C CG2 . VAL A 1 455 ? -12.947 38.702 44.284 1.00 26.24 ? 455 VAL A CG2 1 ATOM 3491 N N . ASP A 1 456 ? -16.225 36.626 44.337 1.00 26.77 ? 456 ASP A N 1 ATOM 3492 C CA . ASP A 1 456 ? -17.523 37.118 43.926 1.00 28.01 ? 456 ASP A CA 1 ATOM 3493 C C . ASP A 1 456 ? -17.413 38.559 43.392 1.00 27.99 ? 456 ASP A C 1 ATOM 3494 O O . ASP A 1 456 ? -16.611 39.341 43.907 1.00 27.66 ? 456 ASP A O 1 ATOM 3495 C CB . ASP A 1 456 ? -18.484 37.035 45.126 1.00 28.25 ? 456 ASP A CB 1 ATOM 3496 C CG . ASP A 1 456 ? -19.927 37.234 44.742 1.00 30.57 ? 456 ASP A CG 1 ATOM 3497 O OD1 . ASP A 1 456 ? -20.602 36.229 44.463 1.00 33.34 ? 456 ASP A OD1 1 ATOM 3498 O OD2 . ASP A 1 456 ? -20.408 38.387 44.724 1.00 30.97 ? 456 ASP A OD2 1 ATOM 3499 N N . PRO A 1 457 ? -18.191 38.897 42.338 1.00 28.69 ? 457 PRO A N 1 ATOM 3500 C CA . PRO A 1 457 ? -18.211 40.259 41.789 1.00 29.42 ? 457 PRO A CA 1 ATOM 3501 C C . PRO A 1 457 ? -18.504 41.350 42.809 1.00 29.59 ? 457 PRO A C 1 ATOM 3502 O O . PRO A 1 457 ? -18.053 42.482 42.635 1.00 29.82 ? 457 PRO A O 1 ATOM 3503 C CB . PRO A 1 457 ? -19.333 40.206 40.732 1.00 30.35 ? 457 PRO A CB 1 ATOM 3504 C CG . PRO A 1 457 ? -20.091 38.956 41.022 1.00 30.61 ? 457 PRO A CG 1 ATOM 3505 C CD . PRO A 1 457 ? -19.066 38.005 41.554 1.00 28.72 ? 457 PRO A CD 1 ATOM 3506 N N . SER A 1 458 ? -19.252 41.018 43.861 1.00 29.60 ? 458 SER A N 1 ATOM 3507 C CA . SER A 1 458 ? -19.583 41.999 44.895 1.00 29.68 ? 458 SER A CA 1 ATOM 3508 C C . SER A 1 458 ? -18.462 42.208 45.932 1.00 28.49 ? 458 SER A C 1 ATOM 3509 O O . SER A 1 458 ? -18.534 43.130 46.749 1.00 29.59 ? 458 SER A O 1 ATOM 3510 C CB . SER A 1 458 ? -20.902 41.623 45.578 1.00 30.49 ? 458 SER A CB 1 ATOM 3511 O OG . SER A 1 458 ? -20.726 40.523 46.445 1.00 29.91 ? 458 SER A OG 1 ATOM 3512 N N . THR A 1 459 ? -17.439 41.354 45.903 1.00 26.96 ? 459 THR A N 1 ATOM 3513 C CA . THR A 1 459 ? -16.303 41.464 46.818 1.00 25.92 ? 459 THR A CA 1 ATOM 3514 C C . THR A 1 459 ? -15.351 42.567 46.363 1.00 25.94 ? 459 THR A C 1 ATOM 3515 O O . THR A 1 459 ? -14.764 42.487 45.282 1.00 26.08 ? 459 THR A O 1 ATOM 3516 C CB . THR A 1 459 ? -15.541 40.114 46.935 1.00 24.75 ? 459 THR A CB 1 ATOM 3517 O OG1 . THR A 1 459 ? -16.420 39.106 47.453 1.00 25.17 ? 459 THR A OG1 1 ATOM 3518 C CG2 . THR A 1 459 ? -14.309 40.229 47.832 1.00 23.24 ? 459 THR A CG2 1 ATOM 3519 N N . VAL A 1 460 ? -15.209 43.604 47.178 1.00 26.55 ? 460 VAL A N 1 ATOM 3520 C CA . VAL A 1 460 ? -14.242 44.660 46.878 1.00 26.48 ? 460 VAL A CA 1 ATOM 3521 C C . VAL A 1 460 ? -12.864 44.176 47.299 1.00 25.80 ? 460 VAL A C 1 ATOM 3522 O O . VAL A 1 460 ? -12.660 43.756 48.447 1.00 25.47 ? 460 VAL A O 1 ATOM 3523 C CB . VAL A 1 460 ? -14.583 45.997 47.557 1.00 27.42 ? 460 VAL A CB 1 ATOM 3524 C CG1 . VAL A 1 460 ? -13.545 47.076 47.172 1.00 27.44 ? 460 VAL A CG1 1 ATOM 3525 C CG2 . VAL A 1 460 ? -15.995 46.461 47.162 1.00 28.11 ? 460 VAL A CG2 1 ATOM 3526 N N . VAL A 1 461 ? -11.928 44.200 46.353 1.00 25.84 ? 461 VAL A N 1 ATOM 3527 C CA . VAL A 1 461 ? -10.547 43.823 46.631 1.00 25.19 ? 461 VAL A CA 1 ATOM 3528 C C . VAL A 1 461 ? -9.649 45.061 46.677 1.00 25.84 ? 461 VAL A C 1 ATOM 3529 O O . VAL A 1 461 ? -9.611 45.842 45.729 1.00 26.19 ? 461 VAL A O 1 ATOM 3530 C CB . VAL A 1 461 ? -10.010 42.829 45.584 1.00 25.06 ? 461 VAL A CB 1 ATOM 3531 C CG1 . VAL A 1 461 ? -8.574 42.419 45.934 1.00 22.33 ? 461 VAL A CG1 1 ATOM 3532 C CG2 . VAL A 1 461 ? -10.917 41.608 45.491 1.00 23.70 ? 461 VAL A CG2 1 ATOM 3533 N N . VAL A 1 462 ? -8.958 45.255 47.797 1.00 26.01 ? 462 VAL A N 1 ATOM 3534 C CA . VAL A 1 462 ? -8.018 46.373 47.945 1.00 26.33 ? 462 VAL A CA 1 ATOM 3535 C C . VAL A 1 462 ? -6.590 45.838 47.950 1.00 26.12 ? 462 VAL A C 1 ATOM 3536 O O . VAL A 1 462 ? -6.280 44.855 48.635 1.00 25.72 ? 462 VAL A O 1 ATOM 3537 C CB . VAL A 1 462 ? -8.311 47.209 49.224 1.00 27.24 ? 462 VAL A CB 1 ATOM 3538 C CG1 . VAL A 1 462 ? -7.263 48.312 49.424 1.00 26.94 ? 462 VAL A CG1 1 ATOM 3539 C CG2 . VAL A 1 462 ? -9.709 47.817 49.150 1.00 26.86 ? 462 VAL A CG2 1 ATOM 3540 N N . PHE A 1 463 ? -5.722 46.450 47.156 1.00 26.24 ? 463 PHE A N 1 ATOM 3541 C CA . PHE A 1 463 ? -4.306 46.100 47.224 1.00 26.36 ? 463 PHE A CA 1 ATOM 3542 C C . PHE A 1 463 ? -3.522 47.205 47.912 1.00 26.98 ? 463 PHE A C 1 ATOM 3543 O O . PHE A 1 463 ? -3.679 48.379 47.583 1.00 27.73 ? 463 PHE A O 1 ATOM 3544 C CB . PHE A 1 463 ? -3.700 45.788 45.851 1.00 26.01 ? 463 PHE A CB 1 ATOM 3545 C CG . PHE A 1 463 ? -2.202 45.550 45.891 1.00 26.33 ? 463 PHE A CG 1 ATOM 3546 C CD1 . PHE A 1 463 ? -1.677 44.433 46.534 1.00 25.56 ? 463 PHE A CD1 1 ATOM 3547 C CD2 . PHE A 1 463 ? -1.322 46.445 45.289 1.00 29.14 ? 463 PHE A CD2 1 ATOM 3548 C CE1 . PHE A 1 463 ? -0.305 44.212 46.573 1.00 26.84 ? 463 PHE A CE1 1 ATOM 3549 C CE2 . PHE A 1 463 ? 0.073 46.227 45.324 1.00 27.66 ? 463 PHE A CE2 1 ATOM 3550 C CZ . PHE A 1 463 ? 0.573 45.111 45.969 1.00 25.85 ? 463 PHE A CZ 1 ATOM 3551 N N . ALA A 1 464 ? -2.691 46.816 48.878 1.00 27.03 ? 464 ALA A N 1 ATOM 3552 C CA . ALA A 1 464 ? -1.717 47.731 49.471 1.00 28.10 ? 464 ALA A CA 1 ATOM 3553 C C . ALA A 1 464 ? -0.465 46.922 49.753 1.00 28.06 ? 464 ALA A C 1 ATOM 3554 O O . ALA A 1 464 ? -0.532 45.923 50.470 1.00 27.87 ? 464 ALA A O 1 ATOM 3555 C CB . ALA A 1 464 ? -2.262 48.364 50.755 1.00 28.45 ? 464 ALA A CB 1 ATOM 3556 N N . GLU A 1 465 ? 0.666 47.329 49.183 1.00 28.30 ? 465 GLU A N 1 ATOM 3557 C CA . GLU A 1 465 ? 1.885 46.542 49.303 1.00 28.63 ? 465 GLU A CA 1 ATOM 3558 C C . GLU A 1 465 ? 2.420 46.482 50.743 1.00 28.53 ? 465 GLU A C 1 ATOM 3559 O O . GLU A 1 465 ? 2.749 45.407 51.249 1.00 28.28 ? 465 GLU A O 1 ATOM 3560 C CB . GLU A 1 465 ? 2.969 47.038 48.339 1.00 29.16 ? 465 GLU A CB 1 ATOM 3561 C CG . GLU A 1 465 ? 4.222 46.176 48.407 1.00 30.80 ? 465 GLU A CG 1 ATOM 3562 C CD . GLU A 1 465 ? 5.255 46.510 47.352 1.00 34.56 ? 465 GLU A CD 1 ATOM 3563 O OE1 . GLU A 1 465 ? 4.900 47.099 46.311 1.00 36.62 ? 465 GLU A OE1 1 ATOM 3564 O OE2 . GLU A 1 465 ? 6.432 46.152 47.561 1.00 37.88 ? 465 GLU A OE2 1 ATOM 3565 N N . ASN A 1 466 ? 2.498 47.636 51.396 1.00 29.75 ? 466 ASN A N 1 ATOM 3566 C CA . ASN A 1 466 ? 3.002 47.710 52.764 1.00 29.95 ? 466 ASN A CA 1 ATOM 3567 C C . ASN A 1 466 ? 2.141 48.658 53.610 1.00 30.67 ? 466 ASN A C 1 ATOM 3568 O O . ASN A 1 466 ? 2.595 49.743 54.000 1.00 31.08 ? 466 ASN A O 1 ATOM 3569 C CB A ASN A 1 466 ? 4.495 48.100 52.811 0.65 30.96 ? 466 ASN A CB 1 ATOM 3570 C CB B ASN A 1 466 ? 4.461 48.182 52.749 0.35 30.24 ? 466 ASN A CB 1 ATOM 3571 C CG A ASN A 1 466 ? 5.386 47.175 51.963 0.65 32.24 ? 466 ASN A CG 1 ATOM 3572 C CG B ASN A 1 466 ? 5.172 47.931 54.058 0.35 29.73 ? 466 ASN A CG 1 ATOM 3573 O OD1 A ASN A 1 466 ? 6.037 47.628 51.017 0.65 34.81 ? 466 ASN A OD1 1 ATOM 3574 O OD1 B ASN A 1 466 ? 4.791 47.048 54.822 0.35 28.56 ? 466 ASN A OD1 1 ATOM 3575 N ND2 A ASN A 1 466 ? 5.411 45.879 52.297 0.65 32.60 ? 466 ASN A ND2 1 ATOM 3576 N ND2 B ASN A 1 466 ? 6.214 48.711 54.325 0.35 30.33 ? 466 ASN A ND2 1 ATOM 3577 N N . PRO A 1 467 ? 0.884 48.252 53.903 1.00 30.15 ? 467 PRO A N 1 ATOM 3578 C CA . PRO A 1 467 ? 0.013 49.178 54.629 1.00 31.75 ? 467 PRO A CA 1 ATOM 3579 C C . PRO A 1 467 ? 0.381 49.259 56.110 1.00 32.67 ? 467 PRO A C 1 ATOM 3580 O O . PRO A 1 467 ? 0.844 48.261 56.684 1.00 32.92 ? 467 PRO A O 1 ATOM 3581 C CB . PRO A 1 467 ? -1.377 48.557 54.459 1.00 30.88 ? 467 PRO A CB 1 ATOM 3582 C CG . PRO A 1 467 ? -1.116 47.082 54.318 1.00 29.90 ? 467 PRO A CG 1 ATOM 3583 C CD . PRO A 1 467 ? 0.215 46.964 53.623 1.00 29.41 ? 467 PRO A CD 1 ATOM 3584 N N . ASP A 1 468 ? 0.177 50.421 56.728 1.00 33.97 ? 468 ASP A N 1 ATOM 3585 C CA . ASP A 1 468 ? 0.375 50.513 58.165 1.00 34.69 ? 468 ASP A CA 1 ATOM 3586 C C . ASP A 1 468 ? -0.821 49.956 58.929 1.00 34.19 ? 468 ASP A C 1 ATOM 3587 O O . ASP A 1 468 ? -1.863 49.646 58.330 1.00 33.22 ? 468 ASP A O 1 ATOM 3588 C CB . ASP A 1 468 ? 0.784 51.921 58.648 1.00 36.76 ? 468 ASP A CB 1 ATOM 3589 C CG . ASP A 1 468 ? -0.258 53.007 58.374 1.00 38.71 ? 468 ASP A CG 1 ATOM 3590 O OD1 . ASP A 1 468 ? 0.150 54.182 58.380 1.00 42.11 ? 468 ASP A OD1 1 ATOM 3591 O OD2 . ASP A 1 468 ? -1.458 52.737 58.170 1.00 40.45 ? 468 ASP A OD2 1 ATOM 3592 N N . ALA A 1 469 ? -0.635 49.802 60.239 1.00 33.77 ? 469 ALA A N 1 ATOM 3593 C CA . ALA A 1 469 ? -1.623 49.210 61.113 1.00 33.41 ? 469 ALA A CA 1 ATOM 3594 C C . ALA A 1 469 ? -2.945 49.975 61.065 1.00 33.69 ? 469 ALA A C 1 ATOM 3595 O O . ALA A 1 469 ? -4.013 49.363 61.077 1.00 33.11 ? 469 ALA A O 1 ATOM 3596 C CB . ALA A 1 469 ? -1.089 49.162 62.540 1.00 33.90 ? 469 ALA A CB 1 ATOM 3597 N N . GLU A 1 470 ? -2.865 51.304 61.018 1.00 34.65 ? 470 GLU A N 1 ATOM 3598 C CA . GLU A 1 470 ? -4.057 52.149 61.034 1.00 35.38 ? 470 GLU A CA 1 ATOM 3599 C C . GLU A 1 470 ? -4.906 51.963 59.768 1.00 34.32 ? 470 GLU A C 1 ATOM 3600 O O . GLU A 1 470 ? -6.136 51.907 59.845 1.00 34.48 ? 470 GLU A O 1 ATOM 3601 C CB . GLU A 1 470 ? -3.676 53.620 61.210 1.00 36.74 ? 470 GLU A CB 1 ATOM 3602 C CG . GLU A 1 470 ? -4.873 54.498 61.433 1.00 39.40 ? 470 GLU A CG 1 ATOM 3603 C CD . GLU A 1 470 ? -4.590 55.978 61.261 1.00 43.87 ? 470 GLU A CD 1 ATOM 3604 O OE1 . GLU A 1 470 ? -5.460 56.659 60.653 1.00 44.19 ? 470 GLU A OE1 1 ATOM 3605 O OE2 . GLU A 1 470 ? -3.523 56.456 61.739 1.00 44.31 ? 470 GLU A OE2 1 ATOM 3606 N N . PHE A 1 471 ? -4.236 51.883 58.621 1.00 33.46 ? 471 PHE A N 1 ATOM 3607 C CA . PHE A 1 471 ? -4.879 51.649 57.329 1.00 33.36 ? 471 PHE A CA 1 ATOM 3608 C C . PHE A 1 471 ? -5.727 50.382 57.368 1.00 31.90 ? 471 PHE A C 1 ATOM 3609 O O . PHE A 1 471 ? -6.877 50.383 56.914 1.00 32.13 ? 471 PHE A O 1 ATOM 3610 C CB . PHE A 1 471 ? -3.817 51.539 56.221 1.00 32.99 ? 471 PHE A CB 1 ATOM 3611 C CG . PHE A 1 471 ? -4.376 51.213 54.863 1.00 33.73 ? 471 PHE A CG 1 ATOM 3612 C CD1 . PHE A 1 471 ? -4.679 52.227 53.961 1.00 35.87 ? 471 PHE A CD1 1 ATOM 3613 C CD2 . PHE A 1 471 ? -4.603 49.892 54.478 1.00 32.62 ? 471 PHE A CD2 1 ATOM 3614 C CE1 . PHE A 1 471 ? -5.196 51.920 52.694 1.00 34.59 ? 471 PHE A CE1 1 ATOM 3615 C CE2 . PHE A 1 471 ? -5.119 49.593 53.230 1.00 32.63 ? 471 PHE A CE2 1 ATOM 3616 C CZ . PHE A 1 471 ? -5.409 50.608 52.338 1.00 33.30 ? 471 PHE A CZ 1 ATOM 3617 N N . VAL A 1 472 ? -5.141 49.309 57.901 1.00 30.36 ? 472 VAL A N 1 ATOM 3618 C CA . VAL A 1 472 ? -5.825 48.027 58.065 1.00 29.03 ? 472 VAL A CA 1 ATOM 3619 C C . VAL A 1 472 ? -6.995 48.121 59.058 1.00 29.48 ? 472 VAL A C 1 ATOM 3620 O O . VAL A 1 472 ? -8.120 47.719 58.717 1.00 28.91 ? 472 VAL A O 1 ATOM 3621 C CB . VAL A 1 472 ? -4.828 46.919 58.480 1.00 28.30 ? 472 VAL A CB 1 ATOM 3622 C CG1 . VAL A 1 472 ? -5.515 45.563 58.574 1.00 27.42 ? 472 VAL A CG1 1 ATOM 3623 C CG2 . VAL A 1 472 ? -3.699 46.854 57.463 1.00 28.62 ? 472 VAL A CG2 1 ATOM 3624 N N . LYS A 1 473 ? -6.748 48.672 60.255 1.00 29.83 ? 473 LYS A N 1 ATOM 3625 C CA . LYS A 1 473 ? -7.797 48.765 61.290 1.00 31.01 ? 473 LYS A CA 1 ATOM 3626 C C . LYS A 1 473 ? -8.991 49.602 60.821 1.00 30.87 ? 473 LYS A C 1 ATOM 3627 O O . LYS A 1 473 ? -10.147 49.304 61.169 1.00 30.55 ? 473 LYS A O 1 ATOM 3628 C CB . LYS A 1 473 ? -7.259 49.345 62.613 1.00 32.41 ? 473 LYS A CB 1 ATOM 3629 C CG . LYS A 1 473 ? -6.416 48.390 63.485 1.00 33.36 ? 473 LYS A CG 1 ATOM 3630 C CD . LYS A 1 473 ? -5.998 49.087 64.799 1.00 35.43 ? 473 LYS A CD 1 ATOM 3631 C CE . LYS A 1 473 ? -5.165 48.195 65.761 1.00 39.71 ? 473 LYS A CE 1 ATOM 3632 N NZ . LYS A 1 473 ? -3.920 47.598 65.127 1.00 43.71 ? 473 LYS A NZ 1 ATOM 3633 N N . SER A 1 474 ? -8.698 50.649 60.045 1.00 30.49 ? 474 SER A N 1 ATOM 3634 C CA . SER A 1 474 ? -9.709 51.587 59.542 1.00 31.62 ? 474 SER A CA 1 ATOM 3635 C C . SER A 1 474 ? -10.390 51.145 58.236 1.00 30.60 ? 474 SER A C 1 ATOM 3636 O O . SER A 1 474 ? -11.358 51.766 57.813 1.00 31.17 ? 474 SER A O 1 ATOM 3637 C CB . SER A 1 474 ? -9.100 52.984 59.373 1.00 32.35 ? 474 SER A CB 1 ATOM 3638 O OG . SER A 1 474 ? -8.789 53.551 60.641 1.00 34.33 ? 474 SER A OG 1 ATOM 3639 N N . GLY A 1 475 ? -9.905 50.060 57.636 1.00 29.29 ? 475 GLY A N 1 ATOM 3640 C CA . GLY A 1 475 ? -10.302 49.653 56.294 1.00 28.57 ? 475 GLY A CA 1 ATOM 3641 C C . GLY A 1 475 ? -11.620 48.937 56.057 1.00 29.06 ? 475 GLY A C 1 ATOM 3642 O O . GLY A 1 475 ? -12.059 48.834 54.912 1.00 28.51 ? 475 GLY A O 1 ATOM 3643 N N . GLY A 1 476 ? -12.247 48.418 57.110 1.00 29.27 ? 476 GLY A N 1 ATOM 3644 C CA . GLY A 1 476 ? -13.508 47.678 56.963 1.00 29.63 ? 476 GLY A CA 1 ATOM 3645 C C . GLY A 1 476 ? -13.346 46.358 56.231 1.00 28.88 ? 476 GLY A C 1 ATOM 3646 O O . GLY A 1 476 ? -14.241 45.924 55.483 1.00 28.76 ? 476 GLY A O 1 ATOM 3647 N N . PHE A 1 477 ? -12.202 45.714 56.460 1.00 28.23 ? 477 PHE A N 1 ATOM 3648 C CA . PHE A 1 477 ? -11.865 44.451 55.802 1.00 27.60 ? 477 PHE A CA 1 ATOM 3649 C C . PHE A 1 477 ? -12.423 43.248 56.549 1.00 27.58 ? 477 PHE A C 1 ATOM 3650 O O . PHE A 1 477 ? -12.494 43.241 57.784 1.00 28.16 ? 477 PHE A O 1 ATOM 3651 C CB . PHE A 1 477 ? -10.349 44.305 55.655 1.00 26.74 ? 477 PHE A CB 1 ATOM 3652 C CG . PHE A 1 477 ? -9.719 45.376 54.813 1.00 27.24 ? 477 PHE A CG 1 ATOM 3653 C CD1 . PHE A 1 477 ? -8.798 46.271 55.373 1.00 25.46 ? 477 PHE A CD1 1 ATOM 3654 C CD2 . PHE A 1 477 ? -10.053 45.498 53.456 1.00 25.71 ? 477 PHE A CD2 1 ATOM 3655 C CE1 . PHE A 1 477 ? -8.212 47.255 54.586 1.00 27.94 ? 477 PHE A CE1 1 ATOM 3656 C CE2 . PHE A 1 477 ? -9.479 46.487 52.665 1.00 25.37 ? 477 PHE A CE2 1 ATOM 3657 C CZ . PHE A 1 477 ? -8.553 47.361 53.224 1.00 26.93 ? 477 PHE A CZ 1 ATOM 3658 N N . SER A 1 478 ? -12.839 42.246 55.785 1.00 26.96 ? 478 SER A N 1 ATOM 3659 C CA . SER A 1 478 ? -13.321 40.991 56.348 1.00 27.19 ? 478 SER A CA 1 ATOM 3660 C C . SER A 1 478 ? -12.146 40.092 56.726 1.00 26.41 ? 478 SER A C 1 ATOM 3661 O O . SER A 1 478 ? -12.202 39.351 57.718 1.00 26.18 ? 478 SER A O 1 ATOM 3662 C CB . SER A 1 478 ? -14.232 40.279 55.344 1.00 26.70 ? 478 SER A CB 1 ATOM 3663 O OG . SER A 1 478 ? -15.382 41.079 55.087 1.00 28.05 ? 478 SER A OG 1 ATOM 3664 N N . TYR A 1 479 ? -11.104 40.141 55.901 1.00 25.63 ? 479 TYR A N 1 ATOM 3665 C CA . TYR A 1 479 ? -9.868 39.392 56.123 1.00 25.19 ? 479 TYR A CA 1 ATOM 3666 C C . TYR A 1 479 ? -8.807 39.955 55.189 1.00 24.83 ? 479 TYR A C 1 ATOM 3667 O O . TYR A 1 479 ? -9.114 40.780 54.325 1.00 26.18 ? 479 TYR A O 1 ATOM 3668 C CB . TYR A 1 479 ? -10.076 37.891 55.869 1.00 24.82 ? 479 TYR A CB 1 ATOM 3669 C CG . TYR A 1 479 ? -10.648 37.532 54.499 1.00 24.99 ? 479 TYR A CG 1 ATOM 3670 C CD1 . TYR A 1 479 ? -9.818 37.435 53.368 1.00 22.83 ? 479 TYR A CD1 1 ATOM 3671 C CD2 . TYR A 1 479 ? -12.018 37.272 54.340 1.00 24.11 ? 479 TYR A CD2 1 ATOM 3672 C CE1 . TYR A 1 479 ? -10.343 37.095 52.114 1.00 23.67 ? 479 TYR A CE1 1 ATOM 3673 C CE2 . TYR A 1 479 ? -12.548 36.944 53.102 1.00 24.28 ? 479 TYR A CE2 1 ATOM 3674 C CZ . TYR A 1 479 ? -11.701 36.838 51.991 1.00 23.93 ? 479 TYR A CZ 1 ATOM 3675 O OH . TYR A 1 479 ? -12.218 36.512 50.757 1.00 24.88 ? 479 TYR A OH 1 ATOM 3676 N N . ALA A 1 480 ? -7.569 39.513 55.372 1.00 24.24 ? 480 ALA A N 1 ATOM 3677 C CA . ALA A 1 480 ? -6.467 39.866 54.499 1.00 23.66 ? 480 ALA A CA 1 ATOM 3678 C C . ALA A 1 480 ? -5.682 38.630 54.057 1.00 23.08 ? 480 ALA A C 1 ATOM 3679 O O . ALA A 1 480 ? -5.540 37.656 54.807 1.00 22.79 ? 480 ALA A O 1 ATOM 3680 C CB . ALA A 1 480 ? -5.543 40.846 55.190 1.00 23.58 ? 480 ALA A CB 1 ATOM 3681 N N . ILE A 1 481 ? -5.188 38.684 52.826 1.00 22.50 ? 481 ILE A N 1 ATOM 3682 C CA . ILE A 1 481 ? -4.174 37.760 52.348 1.00 22.27 ? 481 ILE A CA 1 ATOM 3683 C C . ILE A 1 481 ? -2.876 38.567 52.209 1.00 22.48 ? 481 ILE A C 1 ATOM 3684 O O . ILE A 1 481 ? -2.824 39.575 51.500 1.00 23.13 ? 481 ILE A O 1 ATOM 3685 C CB . ILE A 1 481 ? -4.590 37.102 50.991 1.00 22.30 ? 481 ILE A CB 1 ATOM 3686 C CG1 . ILE A 1 481 ? -5.842 36.233 51.187 1.00 21.81 ? 481 ILE A CG1 1 ATOM 3687 C CG2 . ILE A 1 481 ? -3.398 36.311 50.390 1.00 20.61 ? 481 ILE A CG2 1 ATOM 3688 C CD1 . ILE A 1 481 ? -6.711 36.021 49.881 1.00 22.59 ? 481 ILE A CD1 1 ATOM 3689 N N . VAL A 1 482 ? -1.835 38.139 52.908 1.00 22.14 ? 482 VAL A N 1 ATOM 3690 C CA . VAL A 1 482 ? -0.578 38.864 52.885 1.00 22.58 ? 482 VAL A CA 1 ATOM 3691 C C . VAL A 1 482 ? 0.537 37.911 52.457 1.00 22.13 ? 482 VAL A C 1 ATOM 3692 O O . VAL A 1 482 ? 0.728 36.844 53.045 1.00 22.15 ? 482 VAL A O 1 ATOM 3693 C CB . VAL A 1 482 ? -0.324 39.645 54.228 1.00 23.07 ? 482 VAL A CB 1 ATOM 3694 C CG1 . VAL A 1 482 ? -0.541 38.749 55.432 1.00 25.47 ? 482 VAL A CG1 1 ATOM 3695 C CG2 . VAL A 1 482 ? 1.063 40.335 54.236 1.00 22.91 ? 482 VAL A CG2 1 ATOM 3696 N N . ALA A 1 483 ? 1.229 38.286 51.386 1.00 21.93 ? 483 ALA A N 1 ATOM 3697 C CA . ALA A 1 483 ? 2.254 37.445 50.798 1.00 21.38 ? 483 ALA A CA 1 ATOM 3698 C C . ALA A 1 483 ? 3.622 38.105 50.903 1.00 21.67 ? 483 ALA A C 1 ATOM 3699 O O . ALA A 1 483 ? 3.809 39.253 50.484 1.00 22.08 ? 483 ALA A O 1 ATOM 3700 C CB . ALA A 1 483 ? 1.894 37.105 49.329 1.00 20.96 ? 483 ALA A CB 1 ATOM 3701 N N . VAL A 1 484 ? 4.563 37.374 51.491 1.00 21.38 ? 484 VAL A N 1 ATOM 3702 C CA . VAL A 1 484 ? 5.930 37.850 51.735 1.00 21.71 ? 484 VAL A CA 1 ATOM 3703 C C . VAL A 1 484 ? 6.921 36.707 51.517 1.00 21.46 ? 484 VAL A C 1 ATOM 3704 O O . VAL A 1 484 ? 6.515 35.567 51.307 1.00 21.30 ? 484 VAL A O 1 ATOM 3705 C CB . VAL A 1 484 ? 6.106 38.413 53.175 1.00 22.32 ? 484 VAL A CB 1 ATOM 3706 C CG1 . VAL A 1 484 ? 5.229 39.670 53.380 1.00 21.57 ? 484 VAL A CG1 1 ATOM 3707 C CG2 . VAL A 1 484 ? 5.810 37.327 54.244 1.00 21.90 ? 484 VAL A CG2 1 ATOM 3708 N N . GLY A 1 485 ? 8.212 37.010 51.542 1.00 21.64 ? 485 GLY A N 1 ATOM 3709 C CA . GLY A 1 485 ? 9.208 35.958 51.460 1.00 21.24 ? 485 GLY A CA 1 ATOM 3710 C C . GLY A 1 485 ? 10.545 36.353 50.875 1.00 21.62 ? 485 GLY A C 1 ATOM 3711 O O . GLY A 1 485 ? 10.963 37.521 50.932 1.00 21.54 ? 485 GLY A O 1 ATOM 3712 N N . GLU A 1 486 ? 11.217 35.348 50.321 1.00 21.44 ? 486 GLU A N 1 ATOM 3713 C CA . GLU A 1 486 ? 12.559 35.492 49.765 1.00 21.26 ? 486 GLU A CA 1 ATOM 3714 C C . GLU A 1 486 ? 12.513 36.143 48.403 1.00 22.34 ? 486 GLU A C 1 ATOM 3715 O O . GLU A 1 486 ? 11.519 36.018 47.658 1.00 21.93 ? 486 GLU A O 1 ATOM 3716 C CB . GLU A 1 486 ? 13.216 34.124 49.609 1.00 21.30 ? 486 GLU A CB 1 ATOM 3717 C CG . GLU A 1 486 ? 13.506 33.384 50.912 1.00 21.11 ? 486 GLU A CG 1 ATOM 3718 C CD . GLU A 1 486 ? 14.464 32.233 50.702 1.00 21.86 ? 486 GLU A CD 1 ATOM 3719 O OE1 . GLU A 1 486 ? 14.123 31.271 49.977 1.00 22.38 ? 486 GLU A OE1 1 ATOM 3720 O OE2 . GLU A 1 486 ? 15.577 32.306 51.238 1.00 23.90 ? 486 GLU A OE2 1 ATOM 3721 N N . HIS A 1 487 ? 13.606 36.816 48.067 1.00 22.67 ? 487 HIS A N 1 ATOM 3722 C CA . HIS A 1 487 ? 13.789 37.343 46.728 1.00 23.30 ? 487 HIS A CA 1 ATOM 3723 C C . HIS A 1 487 ? 14.387 36.243 45.828 1.00 22.87 ? 487 HIS A C 1 ATOM 3724 O O . HIS A 1 487 ? 14.915 35.247 46.328 1.00 23.00 ? 487 HIS A O 1 ATOM 3725 C CB . HIS A 1 487 ? 14.629 38.622 46.762 1.00 24.42 ? 487 HIS A CB 1 ATOM 3726 C CG . HIS A 1 487 ? 13.968 39.746 47.502 1.00 26.13 ? 487 HIS A CG 1 ATOM 3727 N ND1 . HIS A 1 487 ? 14.618 40.917 47.813 1.00 28.07 ? 487 HIS A ND1 1 ATOM 3728 C CD2 . HIS A 1 487 ? 12.715 39.869 48.007 1.00 26.65 ? 487 HIS A CD2 1 ATOM 3729 C CE1 . HIS A 1 487 ? 13.796 41.718 48.469 1.00 28.53 ? 487 HIS A CE1 1 ATOM 3730 N NE2 . HIS A 1 487 ? 12.635 41.105 48.601 1.00 27.53 ? 487 HIS A NE2 1 ATOM 3731 N N . PRO A 1 488 ? 14.231 36.379 44.504 1.00 22.65 ? 488 PRO A N 1 ATOM 3732 C CA . PRO A 1 488 ? 14.806 35.360 43.615 1.00 22.33 ? 488 PRO A CA 1 ATOM 3733 C C . PRO A 1 488 ? 16.330 35.240 43.725 1.00 22.89 ? 488 PRO A C 1 ATOM 3734 O O . PRO A 1 488 ? 17.035 36.247 43.834 1.00 24.09 ? 488 PRO A O 1 ATOM 3735 C CB . PRO A 1 488 ? 14.380 35.844 42.219 1.00 21.64 ? 488 PRO A CB 1 ATOM 3736 C CG . PRO A 1 488 ? 13.123 36.663 42.475 1.00 22.17 ? 488 PRO A CG 1 ATOM 3737 C CD . PRO A 1 488 ? 13.474 37.398 43.749 1.00 21.96 ? 488 PRO A CD 1 ATOM 3738 N N . TYR A 1 489 ? 16.830 34.011 43.689 1.00 22.80 ? 489 TYR A N 1 ATOM 3739 C CA . TYR A 1 489 ? 18.262 33.759 43.720 1.00 22.91 ? 489 TYR A CA 1 ATOM 3740 C C . TYR A 1 489 ? 18.570 32.428 43.051 1.00 22.59 ? 489 TYR A C 1 ATOM 3741 O O . TYR A 1 489 ? 17.702 31.554 42.944 1.00 22.54 ? 489 TYR A O 1 ATOM 3742 C CB . TYR A 1 489 ? 18.793 33.753 45.174 1.00 23.67 ? 489 TYR A CB 1 ATOM 3743 C CG . TYR A 1 489 ? 18.055 32.767 46.077 1.00 23.46 ? 489 TYR A CG 1 ATOM 3744 C CD1 . TYR A 1 489 ? 18.345 31.394 46.031 1.00 23.00 ? 489 TYR A CD1 1 ATOM 3745 C CD2 . TYR A 1 489 ? 17.068 33.208 46.969 1.00 22.89 ? 489 TYR A CD2 1 ATOM 3746 C CE1 . TYR A 1 489 ? 17.677 30.487 46.838 1.00 22.55 ? 489 TYR A CE1 1 ATOM 3747 C CE2 . TYR A 1 489 ? 16.381 32.300 47.776 1.00 22.75 ? 489 TYR A CE2 1 ATOM 3748 C CZ . TYR A 1 489 ? 16.694 30.943 47.699 1.00 23.03 ? 489 TYR A CZ 1 ATOM 3749 O OH . TYR A 1 489 ? 16.028 30.031 48.486 1.00 23.63 ? 489 TYR A OH 1 ATOM 3750 N N . THR A 1 490 ? 19.818 32.278 42.626 1.00 23.03 ? 490 THR A N 1 ATOM 3751 C CA . THR A 1 490 ? 20.298 31.066 41.996 1.00 23.56 ? 490 THR A CA 1 ATOM 3752 C C . THR A 1 490 ? 21.740 30.797 42.438 1.00 24.99 ? 490 THR A C 1 ATOM 3753 O O . THR A 1 490 ? 22.552 31.720 42.526 1.00 26.01 ? 490 THR A O 1 ATOM 3754 C CB . THR A 1 490 ? 20.243 31.217 40.452 1.00 23.55 ? 490 THR A CB 1 ATOM 3755 O OG1 . THR A 1 490 ? 18.920 31.594 40.069 1.00 21.51 ? 490 THR A OG1 1 ATOM 3756 C CG2 . THR A 1 490 ? 20.631 29.920 39.733 1.00 23.26 ? 490 THR A CG2 1 ATOM 3757 N N . GLU A 1 491 ? 22.047 29.531 42.697 1.00 25.12 ? 491 GLU A N 1 ATOM 3758 C CA . GLU A 1 491 ? 23.417 29.092 42.973 1.00 26.12 ? 491 GLU A CA 1 ATOM 3759 C C . GLU A 1 491 ? 24.001 29.853 44.176 1.00 26.81 ? 491 GLU A C 1 ATOM 3760 O O . GLU A 1 491 ? 23.308 30.017 45.185 1.00 26.22 ? 491 GLU A O 1 ATOM 3761 C CB . GLU A 1 491 ? 24.276 29.143 41.691 1.00 26.27 ? 491 GLU A CB 1 ATOM 3762 C CG . GLU A 1 491 ? 23.761 28.150 40.647 1.00 25.39 ? 491 GLU A CG 1 ATOM 3763 C CD . GLU A 1 491 ? 24.484 28.176 39.314 1.00 26.81 ? 491 GLU A CD 1 ATOM 3764 O OE1 . GLU A 1 491 ? 25.675 27.830 39.299 1.00 27.46 ? 491 GLU A OE1 1 ATOM 3765 O OE2 . GLU A 1 491 ? 23.841 28.471 38.272 1.00 26.17 ? 491 GLU A OE2 1 ATOM 3766 N N . THR A 1 492 ? 25.236 30.340 44.074 1.00 28.13 ? 492 THR A N 1 ATOM 3767 C CA . THR A 1 492 ? 25.928 30.918 45.246 1.00 29.06 ? 492 THR A CA 1 ATOM 3768 C C . THR A 1 492 ? 25.252 32.180 45.777 1.00 29.43 ? 492 THR A C 1 ATOM 3769 O O . THR A 1 492 ? 25.335 32.471 46.963 1.00 29.82 ? 492 THR A O 1 ATOM 3770 C CB . THR A 1 492 ? 27.415 31.141 44.956 1.00 30.18 ? 492 THR A CB 1 ATOM 3771 O OG1 . THR A 1 492 ? 27.966 29.911 44.475 1.00 30.40 ? 492 THR A OG1 1 ATOM 3772 C CG2 . THR A 1 492 ? 28.187 31.575 46.226 1.00 30.68 ? 492 THR A CG2 1 ATOM 3773 N N . LYS A 1 493 ? 24.557 32.910 44.907 1.00 29.26 ? 493 LYS A N 1 ATOM 3774 C CA . LYS A 1 493 ? 23.805 34.099 45.335 1.00 29.97 ? 493 LYS A CA 1 ATOM 3775 C C . LYS A 1 493 ? 22.722 33.779 46.361 1.00 28.90 ? 493 LYS A C 1 ATOM 3776 O O . LYS A 1 493 ? 22.305 34.661 47.121 1.00 29.90 ? 493 LYS A O 1 ATOM 3777 C CB . LYS A 1 493 ? 23.198 34.834 44.130 1.00 29.98 ? 493 LYS A CB 1 ATOM 3778 C CG . LYS A 1 493 ? 24.196 35.720 43.386 1.00 34.62 ? 493 LYS A CG 1 ATOM 3779 C CD . LYS A 1 493 ? 24.190 37.154 43.956 1.00 41.32 ? 493 LYS A CD 1 ATOM 3780 C CE . LYS A 1 493 ? 25.456 37.947 43.584 1.00 46.04 ? 493 LYS A CE 1 ATOM 3781 N NZ . LYS A 1 493 ? 25.466 38.392 42.147 1.00 48.70 ? 493 LYS A NZ 1 ATOM 3782 N N . GLY A 1 494 ? 22.265 32.526 46.374 1.00 27.74 ? 494 GLY A N 1 ATOM 3783 C CA . GLY A 1 494 ? 21.257 32.081 47.332 1.00 26.75 ? 494 GLY A CA 1 ATOM 3784 C C . GLY A 1 494 ? 21.770 31.484 48.633 1.00 27.05 ? 494 GLY A C 1 ATOM 3785 O O . GLY A 1 494 ? 20.972 31.196 49.538 1.00 26.84 ? 494 GLY A O 1 ATOM 3786 N N . ASP A 1 495 ? 23.087 31.271 48.725 1.00 27.45 ? 495 ASP A N 1 ATOM 3787 C CA . ASP A 1 495 ? 23.713 30.778 49.950 1.00 28.26 ? 495 ASP A CA 1 ATOM 3788 C C . ASP A 1 495 ? 23.442 31.823 51.021 1.00 29.14 ? 495 ASP A C 1 ATOM 3789 O O . ASP A 1 495 ? 23.639 33.023 50.794 1.00 29.32 ? 495 ASP A O 1 ATOM 3790 C CB . ASP A 1 495 ? 25.229 30.589 49.783 1.00 29.06 ? 495 ASP A CB 1 ATOM 3791 C CG . ASP A 1 495 ? 25.596 29.354 48.976 1.00 27.97 ? 495 ASP A CG 1 ATOM 3792 O OD1 . ASP A 1 495 ? 24.693 28.617 48.516 1.00 27.09 ? 495 ASP A OD1 1 ATOM 3793 O OD2 . ASP A 1 495 ? 26.811 29.115 48.795 1.00 27.58 ? 495 ASP A OD2 1 ATOM 3794 N N . ASN A 1 496 ? 22.972 31.362 52.179 1.00 29.38 ? 496 ASN A N 1 ATOM 3795 C CA . ASN A 1 496 ? 22.397 32.246 53.185 1.00 29.75 ? 496 ASN A CA 1 ATOM 3796 C C . ASN A 1 496 ? 22.494 31.592 54.563 1.00 31.06 ? 496 ASN A C 1 ATOM 3797 O O . ASN A 1 496 ? 21.877 30.555 54.800 1.00 30.29 ? 496 ASN A O 1 ATOM 3798 C CB . ASN A 1 496 ? 20.935 32.524 52.821 1.00 28.25 ? 496 ASN A CB 1 ATOM 3799 C CG . ASN A 1 496 ? 20.311 33.605 53.670 1.00 29.01 ? 496 ASN A CG 1 ATOM 3800 O OD1 . ASN A 1 496 ? 20.705 33.828 54.812 1.00 28.54 ? 496 ASN A OD1 1 ATOM 3801 N ND2 . ASN A 1 496 ? 19.308 34.285 53.112 1.00 29.03 ? 496 ASN A ND2 1 ATOM 3802 N N . LEU A 1 497 ? 23.264 32.212 55.461 1.00 33.09 ? 497 LEU A N 1 ATOM 3803 C CA . LEU A 1 497 ? 23.512 31.656 56.800 1.00 34.96 ? 497 LEU A CA 1 ATOM 3804 C C . LEU A 1 497 ? 22.458 32.010 57.856 1.00 35.71 ? 497 LEU A C 1 ATOM 3805 O O . LEU A 1 497 ? 22.364 31.329 58.876 1.00 36.64 ? 497 LEU A O 1 ATOM 3806 C CB . LEU A 1 497 ? 24.897 32.069 57.308 1.00 36.14 ? 497 LEU A CB 1 ATOM 3807 C CG . LEU A 1 497 ? 26.124 31.592 56.519 1.00 36.38 ? 497 LEU A CG 1 ATOM 3808 C CD1 . LEU A 1 497 ? 27.391 32.122 57.168 1.00 36.99 ? 497 LEU A CD1 1 ATOM 3809 C CD2 . LEU A 1 497 ? 26.160 30.068 56.382 1.00 35.13 ? 497 LEU A CD2 1 ATOM 3810 N N A ASN A 1 498 ? 21.689 33.066 57.626 0.50 35.32 ? 498 ASN A N 1 ATOM 3811 N N B ASN A 1 498 ? 21.684 33.064 57.580 0.50 35.47 ? 498 ASN A N 1 ATOM 3812 C CA A ASN A 1 498 ? 20.687 33.476 58.602 0.50 35.80 ? 498 ASN A CA 1 ATOM 3813 C CA B ASN A 1 498 ? 20.677 33.645 58.487 0.50 36.10 ? 498 ASN A CA 1 ATOM 3814 C C . ASN A 1 498 ? 19.267 33.061 58.263 1.00 34.16 ? 498 ASN A C 1 ATOM 3815 O O . ASN A 1 498 ? 18.455 32.939 59.177 1.00 34.04 ? 498 ASN A O 1 ATOM 3816 C CB A ASN A 1 498 ? 20.744 34.978 58.867 0.50 36.96 ? 498 ASN A CB 1 ATOM 3817 C CB B ASN A 1 498 ? 20.611 35.183 58.292 0.50 37.19 ? 498 ASN A CB 1 ATOM 3818 C CG A ASN A 1 498 ? 20.515 35.787 57.620 0.50 39.35 ? 498 ASN A CG 1 ATOM 3819 C CG B ASN A 1 498 ? 21.982 35.825 57.937 0.50 42.41 ? 498 ASN A CG 1 ATOM 3820 O OD1 A ASN A 1 498 ? 19.378 35.959 57.162 0.50 38.36 ? 498 ASN A OD1 1 ATOM 3821 O OD1 B ASN A 1 498 ? 23.029 35.349 58.399 0.50 44.88 ? 498 ASN A OD1 1 ATOM 3822 N ND2 A ASN A 1 498 ? 21.610 36.281 57.051 0.50 46.26 ? 498 ASN A ND2 1 ATOM 3823 N ND2 B ASN A 1 498 ? 21.971 36.954 57.168 0.50 48.09 ? 498 ASN A ND2 1 ATOM 3824 N N . LEU A 1 499 ? 18.968 32.796 56.991 1.00 31.98 ? 499 LEU A N 1 ATOM 3825 C CA . LEU A 1 499 ? 17.634 32.353 56.549 1.00 30.04 ? 499 LEU A CA 1 ATOM 3826 C C . LEU A 1 499 ? 16.457 33.143 57.142 1.00 30.20 ? 499 LEU A C 1 ATOM 3827 O O . LEU A 1 499 ? 15.452 32.562 57.561 1.00 29.40 ? 499 LEU A O 1 ATOM 3828 C CB . LEU A 1 499 ? 17.443 30.846 56.770 1.00 29.34 ? 499 LEU A CB 1 ATOM 3829 C CG . LEU A 1 499 ? 18.472 29.967 56.063 1.00 28.49 ? 499 LEU A CG 1 ATOM 3830 C CD1 . LEU A 1 499 ? 18.223 28.515 56.371 1.00 26.68 ? 499 LEU A CD1 1 ATOM 3831 C CD2 . LEU A 1 499 ? 18.431 30.233 54.553 1.00 26.53 ? 499 LEU A CD2 1 ATOM 3832 N N . THR A 1 500 ? 16.591 34.463 57.192 1.00 31.30 ? 500 THR A N 1 ATOM 3833 C CA . THR A 1 500 ? 15.466 35.302 57.590 1.00 32.47 ? 500 THR A CA 1 ATOM 3834 C C . THR A 1 500 ? 14.995 36.073 56.369 1.00 31.95 ? 500 THR A C 1 ATOM 3835 O O . THR A 1 500 ? 15.813 36.517 55.563 1.00 32.06 ? 500 THR A O 1 ATOM 3836 C CB . THR A 1 500 ? 15.792 36.253 58.787 1.00 34.16 ? 500 THR A CB 1 ATOM 3837 O OG1 . THR A 1 500 ? 16.580 37.348 58.327 1.00 38.30 ? 500 THR A OG1 1 ATOM 3838 C CG2 . THR A 1 500 ? 16.556 35.524 59.872 1.00 33.20 ? 500 THR A CG2 1 ATOM 3839 N N . ILE A 1 501 ? 13.684 36.213 56.207 1.00 31.58 ? 501 ILE A N 1 ATOM 3840 C CA . ILE A 1 501 ? 13.178 36.898 55.021 1.00 31.42 ? 501 ILE A CA 1 ATOM 3841 C C . ILE A 1 501 ? 13.536 38.391 55.038 1.00 32.73 ? 501 ILE A C 1 ATOM 3842 O O . ILE A 1 501 ? 13.643 38.987 56.110 1.00 32.94 ? 501 ILE A O 1 ATOM 3843 C CB . ILE A 1 501 ? 11.659 36.657 54.777 1.00 30.81 ? 501 ILE A CB 1 ATOM 3844 C CG1 . ILE A 1 501 ? 10.788 37.301 55.867 1.00 31.37 ? 501 ILE A CG1 1 ATOM 3845 C CG2 . ILE A 1 501 ? 11.385 35.165 54.617 1.00 29.88 ? 501 ILE A CG2 1 ATOM 3846 C CD1 . ILE A 1 501 ? 9.364 37.490 55.438 1.00 31.44 ? 501 ILE A CD1 1 ATOM 3847 N N . PRO A 1 502 ? 13.757 38.990 53.847 1.00 33.22 ? 502 PRO A N 1 ATOM 3848 C CA . PRO A 1 502 ? 14.018 40.431 53.783 1.00 34.68 ? 502 PRO A CA 1 ATOM 3849 C C . PRO A 1 502 ? 12.850 41.263 54.307 1.00 35.26 ? 502 PRO A C 1 ATOM 3850 O O . PRO A 1 502 ? 11.689 40.836 54.251 1.00 34.39 ? 502 PRO A O 1 ATOM 3851 C CB . PRO A 1 502 ? 14.207 40.698 52.276 1.00 34.13 ? 502 PRO A CB 1 ATOM 3852 C CG . PRO A 1 502 ? 13.589 39.546 51.595 1.00 32.84 ? 502 PRO A CG 1 ATOM 3853 C CD . PRO A 1 502 ? 13.793 38.373 52.506 1.00 32.51 ? 502 PRO A CD 1 ATOM 3854 N N . GLU A 1 503 ? 13.174 42.440 54.813 1.00 37.03 ? 503 GLU A N 1 ATOM 3855 C CA . GLU A 1 503 ? 12.165 43.392 55.231 1.00 38.29 ? 503 GLU A CA 1 ATOM 3856 C C . GLU A 1 503 ? 11.883 44.392 54.104 1.00 38.64 ? 503 GLU A C 1 ATOM 3857 O O . GLU A 1 503 ? 12.748 44.621 53.256 1.00 39.34 ? 503 GLU A O 1 ATOM 3858 C CB . GLU A 1 503 ? 12.574 44.083 56.536 1.00 39.55 ? 503 GLU A CB 1 ATOM 3859 C CG . GLU A 1 503 ? 12.408 43.180 57.760 1.00 40.90 ? 503 GLU A CG 1 ATOM 3860 C CD . GLU A 1 503 ? 11.002 42.586 57.844 1.00 41.54 ? 503 GLU A CD 1 ATOM 3861 O OE1 . GLU A 1 503 ? 10.072 43.376 58.114 1.00 39.69 ? 503 GLU A OE1 1 ATOM 3862 O OE2 . GLU A 1 503 ? 10.829 41.348 57.608 1.00 41.66 ? 503 GLU A OE2 1 ATOM 3863 N N . PRO A 1 504 ? 10.657 44.962 54.067 1.00 38.52 ? 504 PRO A N 1 ATOM 3864 C CA . PRO A 1 504 ? 9.549 44.625 54.960 1.00 37.54 ? 504 PRO A CA 1 ATOM 3865 C C . PRO A 1 504 ? 8.867 43.319 54.544 1.00 35.52 ? 504 PRO A C 1 ATOM 3866 O O . PRO A 1 504 ? 8.657 43.049 53.347 1.00 35.15 ? 504 PRO A O 1 ATOM 3867 C CB . PRO A 1 504 ? 8.610 45.824 54.819 1.00 38.28 ? 504 PRO A CB 1 ATOM 3868 C CG . PRO A 1 504 ? 8.847 46.319 53.431 1.00 38.83 ? 504 PRO A CG 1 ATOM 3869 C CD . PRO A 1 504 ? 10.296 46.036 53.120 1.00 38.97 ? 504 PRO A CD 1 ATOM 3870 N N . GLY A 1 505 ? 8.546 42.510 55.539 1.00 33.70 ? 505 GLY A N 1 ATOM 3871 C CA . GLY A 1 505 ? 7.912 41.234 55.310 1.00 31.04 ? 505 GLY A CA 1 ATOM 3872 C C . GLY A 1 505 ? 7.174 40.903 56.576 1.00 30.16 ? 505 GLY A C 1 ATOM 3873 O O . GLY A 1 505 ? 5.944 40.910 56.607 1.00 29.58 ? 505 GLY A O 1 ATOM 3874 N N . LEU A 1 506 ? 7.952 40.627 57.624 1.00 29.96 ? 506 LEU A N 1 ATOM 3875 C CA . LEU A 1 506 ? 7.430 40.409 58.952 1.00 29.17 ? 506 LEU A CA 1 ATOM 3876 C C . LEU A 1 506 ? 6.633 41.621 59.437 1.00 29.20 ? 506 LEU A C 1 ATOM 3877 O O . LEU A 1 506 ? 5.519 41.457 59.923 1.00 28.77 ? 506 LEU A O 1 ATOM 3878 C CB . LEU A 1 506 ? 8.565 40.071 59.934 1.00 30.02 ? 506 LEU A CB 1 ATOM 3879 C CG . LEU A 1 506 ? 8.105 39.827 61.379 1.00 29.49 ? 506 LEU A CG 1 ATOM 3880 C CD1 . LEU A 1 506 ? 7.098 38.676 61.437 1.00 26.07 ? 506 LEU A CD1 1 ATOM 3881 C CD2 . LEU A 1 506 ? 9.299 39.572 62.289 1.00 31.16 ? 506 LEU A CD2 1 ATOM 3882 N N . SER A 1 507 ? 7.191 42.827 59.289 1.00 29.51 ? 507 SER A N 1 ATOM 3883 C CA . SER A 1 507 ? 6.495 44.051 59.722 1.00 29.94 ? 507 SER A CA 1 ATOM 3884 C C . SER A 1 507 ? 5.136 44.221 59.020 1.00 28.96 ? 507 SER A C 1 ATOM 3885 O O . SER A 1 507 ? 4.153 44.630 59.649 1.00 28.80 ? 507 SER A O 1 ATOM 3886 C CB . SER A 1 507 ? 7.370 45.298 59.526 1.00 31.04 ? 507 SER A CB 1 ATOM 3887 O OG . SER A 1 507 ? 7.704 45.456 58.158 1.00 32.26 ? 507 SER A OG 1 ATOM 3888 N N . THR A 1 508 ? 5.069 43.883 57.728 1.00 27.30 ? 508 THR A N 1 ATOM 3889 C CA . THR A 1 508 ? 3.795 43.959 57.002 1.00 26.52 ? 508 THR A CA 1 ATOM 3890 C C . THR A 1 508 ? 2.783 42.923 57.544 1.00 25.41 ? 508 THR A C 1 ATOM 3891 O O . THR A 1 508 ? 1.623 43.253 57.793 1.00 25.14 ? 508 THR A O 1 ATOM 3892 C CB . THR A 1 508 ? 3.998 43.813 55.475 1.00 26.59 ? 508 THR A CB 1 ATOM 3893 O OG1 . THR A 1 508 ? 4.907 44.825 55.039 1.00 29.31 ? 508 THR A OG1 1 ATOM 3894 C CG2 . THR A 1 508 ? 2.663 43.973 54.699 1.00 25.16 ? 508 THR A CG2 1 ATOM 3895 N N . VAL A 1 509 ? 3.231 41.681 57.731 1.00 24.13 ? 509 VAL A N 1 ATOM 3896 C CA . VAL A 1 509 ? 2.402 40.635 58.332 1.00 23.11 ? 509 VAL A CA 1 ATOM 3897 C C . VAL A 1 509 ? 1.889 41.076 59.704 1.00 24.84 ? 509 VAL A C 1 ATOM 3898 O O . VAL A 1 509 ? 0.713 40.944 59.987 1.00 24.55 ? 509 VAL A O 1 ATOM 3899 C CB . VAL A 1 509 ? 3.156 39.269 58.407 1.00 23.13 ? 509 VAL A CB 1 ATOM 3900 C CG1 . VAL A 1 509 ? 2.394 38.242 59.260 1.00 20.62 ? 509 VAL A CG1 1 ATOM 3901 C CG2 . VAL A 1 509 ? 3.360 38.717 56.995 1.00 20.30 ? 509 VAL A CG2 1 ATOM 3902 N N . GLN A 1 510 ? 2.779 41.608 60.539 1.00 26.23 ? 510 GLN A N 1 ATOM 3903 C CA . GLN A 1 510 ? 2.393 42.130 61.844 1.00 28.12 ? 510 GLN A CA 1 ATOM 3904 C C . GLN A 1 510 ? 1.395 43.291 61.766 1.00 28.87 ? 510 GLN A C 1 ATOM 3905 O O . GLN A 1 510 ? 0.414 43.313 62.515 1.00 29.68 ? 510 GLN A O 1 ATOM 3906 C CB . GLN A 1 510 ? 3.633 42.515 62.652 1.00 28.72 ? 510 GLN A CB 1 ATOM 3907 C CG . GLN A 1 510 ? 4.434 41.308 63.139 1.00 29.05 ? 510 GLN A CG 1 ATOM 3908 C CD . GLN A 1 510 ? 5.822 41.679 63.677 1.00 31.35 ? 510 GLN A CD 1 ATOM 3909 O OE1 . GLN A 1 510 ? 6.325 42.777 63.437 1.00 33.99 ? 510 GLN A OE1 1 ATOM 3910 N NE2 . GLN A 1 510 ? 6.444 40.753 64.405 1.00 32.39 ? 510 GLN A NE2 1 ATOM 3911 N N . ALA A 1 511 ? 1.636 44.249 60.872 1.00 29.28 ? 511 ALA A N 1 ATOM 3912 C CA . ALA A 1 511 ? 0.729 45.399 60.734 1.00 30.14 ? 511 ALA A CA 1 ATOM 3913 C C . ALA A 1 511 ? -0.644 44.956 60.237 1.00 29.73 ? 511 ALA A C 1 ATOM 3914 O O . ALA A 1 511 ? -1.669 45.398 60.751 1.00 30.53 ? 511 ALA A O 1 ATOM 3915 C CB . ALA A 1 511 ? 1.329 46.470 59.816 1.00 30.47 ? 511 ALA A CB 1 ATOM 3916 N N . VAL A 1 512 ? -0.659 44.056 59.260 1.00 28.09 ? 512 VAL A N 1 ATOM 3917 C CA . VAL A 1 512 ? -1.902 43.526 58.704 1.00 27.48 ? 512 VAL A CA 1 ATOM 3918 C C . VAL A 1 512 ? -2.688 42.645 59.686 1.00 28.03 ? 512 VAL A C 1 ATOM 3919 O O . VAL A 1 512 ? -3.869 42.909 59.970 1.00 28.21 ? 512 VAL A O 1 ATOM 3920 C CB . VAL A 1 512 ? -1.637 42.797 57.360 1.00 26.57 ? 512 VAL A CB 1 ATOM 3921 C CG1 . VAL A 1 512 ? -2.869 42.025 56.887 1.00 25.88 ? 512 VAL A CG1 1 ATOM 3922 C CG2 . VAL A 1 512 ? -1.182 43.818 56.309 1.00 26.13 ? 512 VAL A CG2 1 ATOM 3923 N N . CYS A 1 513 ? -2.025 41.613 60.206 1.00 27.95 ? 513 CYS A N 1 ATOM 3924 C CA . CYS A 1 513 ? -2.657 40.638 61.080 1.00 28.23 ? 513 CYS A CA 1 ATOM 3925 C C . CYS A 1 513 ? -3.094 41.250 62.417 1.00 29.22 ? 513 CYS A C 1 ATOM 3926 O O . CYS A 1 513 ? -4.043 40.771 63.047 1.00 29.62 ? 513 CYS A O 1 ATOM 3927 C CB . CYS A 1 513 ? -1.709 39.467 61.304 1.00 28.09 ? 513 CYS A CB 1 ATOM 3928 S SG . CYS A 1 513 ? -1.249 38.672 59.778 1.00 28.84 ? 513 CYS A SG 1 ATOM 3929 N N . GLY A 1 514 ? -2.407 42.309 62.834 1.00 29.43 ? 514 GLY A N 1 ATOM 3930 C CA . GLY A 1 514 ? -2.796 43.050 64.023 1.00 30.46 ? 514 GLY A CA 1 ATOM 3931 C C . GLY A 1 514 ? -4.130 43.762 63.881 1.00 30.47 ? 514 GLY A C 1 ATOM 3932 O O . GLY A 1 514 ? -4.762 44.084 64.881 1.00 31.18 ? 514 GLY A O 1 ATOM 3933 N N . GLY A 1 515 ? -4.573 43.994 62.643 1.00 29.84 ? 515 GLY A N 1 ATOM 3934 C CA . GLY A 1 515 ? -5.807 44.753 62.412 1.00 30.23 ? 515 GLY A CA 1 ATOM 3935 C C . GLY A 1 515 ? -6.984 43.965 61.872 1.00 29.99 ? 515 GLY A C 1 ATOM 3936 O O . GLY A 1 515 ? -8.122 44.407 61.969 1.00 30.37 ? 515 GLY A O 1 ATOM 3937 N N . VAL A 1 516 ? -6.713 42.799 61.295 1.00 29.08 ? 516 VAL A N 1 ATOM 3938 C CA . VAL A 1 516 ? -7.756 41.976 60.698 1.00 29.27 ? 516 VAL A CA 1 ATOM 3939 C C . VAL A 1 516 ? -7.211 40.557 60.626 1.00 29.23 ? 516 VAL A C 1 ATOM 3940 O O . VAL A 1 516 ? -5.996 40.365 60.641 1.00 28.38 ? 516 VAL A O 1 ATOM 3941 C CB . VAL A 1 516 ? -8.171 42.504 59.290 1.00 28.93 ? 516 VAL A CB 1 ATOM 3942 C CG1 . VAL A 1 516 ? -7.129 42.126 58.217 1.00 28.25 ? 516 VAL A CG1 1 ATOM 3943 C CG2 . VAL A 1 516 ? -9.535 41.974 58.893 1.00 28.88 ? 516 VAL A CG2 1 ATOM 3944 N N . ARG A 1 517 ? -8.082 39.555 60.588 1.00 30.16 ? 517 ARG A N 1 ATOM 3945 C CA . ARG A 1 517 ? -7.555 38.202 60.538 1.00 31.41 ? 517 ARG A CA 1 ATOM 3946 C C . ARG A 1 517 ? -6.945 37.948 59.163 1.00 29.69 ? 517 ARG A C 1 ATOM 3947 O O . ARG A 1 517 ? -7.394 38.498 58.158 1.00 28.85 ? 517 ARG A O 1 ATOM 3948 C CB . ARG A 1 517 ? -8.570 37.147 60.979 1.00 32.55 ? 517 ARG A CB 1 ATOM 3949 C CG . ARG A 1 517 ? -9.668 36.932 60.037 1.00 36.86 ? 517 ARG A CG 1 ATOM 3950 C CD . ARG A 1 517 ? -10.901 36.518 60.789 1.00 42.25 ? 517 ARG A CD 1 ATOM 3951 N NE . ARG A 1 517 ? -12.020 37.008 60.016 1.00 45.30 ? 517 ARG A NE 1 ATOM 3952 C CZ . ARG A 1 517 ? -12.705 36.295 59.136 1.00 46.76 ? 517 ARG A CZ 1 ATOM 3953 N NH1 . ARG A 1 517 ? -12.443 35.013 58.924 1.00 47.61 ? 517 ARG A NH1 1 ATOM 3954 N NH2 . ARG A 1 517 ? -13.684 36.881 58.484 1.00 50.36 ? 517 ARG A NH2 1 ATOM 3955 N N . CYS A 1 518 ? -5.881 37.156 59.145 1.00 29.21 ? 518 CYS A N 1 ATOM 3956 C CA . CYS A 1 518 ? -4.995 37.123 57.990 1.00 28.12 ? 518 CYS A CA 1 ATOM 3957 C C . CYS A 1 518 ? -4.550 35.730 57.646 1.00 27.80 ? 518 CYS A C 1 ATOM 3958 O O . CYS A 1 518 ? -4.298 34.922 58.534 1.00 28.03 ? 518 CYS A O 1 ATOM 3959 C CB . CYS A 1 518 ? -3.752 37.973 58.261 1.00 27.76 ? 518 CYS A CB 1 ATOM 3960 S SG . CYS A 1 518 ? -2.702 37.292 59.564 1.00 29.33 ? 518 CYS A SG 1 ATOM 3961 N N . ALA A 1 519 ? -4.475 35.465 56.342 1.00 26.38 ? 519 ALA A N 1 ATOM 3962 C CA . ALA A 1 519 ? -3.784 34.310 55.804 1.00 25.63 ? 519 ALA A CA 1 ATOM 3963 C C . ALA A 1 519 ? -2.446 34.777 55.226 1.00 24.85 ? 519 ALA A C 1 ATOM 3964 O O . ALA A 1 519 ? -2.402 35.558 54.269 1.00 24.02 ? 519 ALA A O 1 ATOM 3965 C CB . ALA A 1 519 ? -4.641 33.625 54.725 1.00 25.10 ? 519 ALA A CB 1 ATOM 3966 N N . THR A 1 520 ? -1.354 34.325 55.835 1.00 24.35 ? 520 THR A N 1 ATOM 3967 C CA . THR A 1 520 ? -0.025 34.661 55.341 1.00 23.43 ? 520 THR A CA 1 ATOM 3968 C C . THR A 1 520 ? 0.439 33.621 54.331 1.00 22.58 ? 520 THR A C 1 ATOM 3969 O O . THR A 1 520 ? 0.423 32.422 54.609 1.00 22.60 ? 520 THR A O 1 ATOM 3970 C CB . THR A 1 520 ? 0.962 34.808 56.500 1.00 24.25 ? 520 THR A CB 1 ATOM 3971 O OG1 . THR A 1 520 ? 0.566 35.936 57.294 1.00 25.64 ? 520 THR A OG1 1 ATOM 3972 C CG2 . THR A 1 520 ? 2.407 34.993 56.002 1.00 22.78 ? 520 THR A CG2 1 ATOM 3973 N N . VAL A 1 521 ? 0.849 34.086 53.154 1.00 21.44 ? 521 VAL A N 1 ATOM 3974 C CA . VAL A 1 521 ? 1.403 33.204 52.156 1.00 21.42 ? 521 VAL A CA 1 ATOM 3975 C C . VAL A 1 521 ? 2.905 33.478 52.091 1.00 21.71 ? 521 VAL A C 1 ATOM 3976 O O . VAL A 1 521 ? 3.344 34.567 51.693 1.00 21.41 ? 521 VAL A O 1 ATOM 3977 C CB . VAL A 1 521 ? 0.732 33.395 50.769 1.00 21.11 ? 521 VAL A CB 1 ATOM 3978 C CG1 . VAL A 1 521 ? 1.434 32.566 49.706 1.00 20.42 ? 521 VAL A CG1 1 ATOM 3979 C CG2 . VAL A 1 521 ? -0.766 33.060 50.827 1.00 20.60 ? 521 VAL A CG2 1 ATOM 3980 N N . LEU A 1 522 ? 3.681 32.481 52.497 1.00 21.57 ? 522 LEU A N 1 ATOM 3981 C CA . LEU A 1 522 ? 5.135 32.592 52.494 1.00 21.48 ? 522 LEU A CA 1 ATOM 3982 C C . LEU A 1 522 ? 5.760 32.026 51.209 1.00 20.58 ? 522 LEU A C 1 ATOM 3983 O O . LEU A 1 522 ? 5.609 30.858 50.901 1.00 20.08 ? 522 LEU A O 1 ATOM 3984 C CB . LEU A 1 522 ? 5.719 31.894 53.731 1.00 21.82 ? 522 LEU A CB 1 ATOM 3985 C CG . LEU A 1 522 ? 7.233 31.872 53.927 1.00 22.12 ? 522 LEU A CG 1 ATOM 3986 C CD1 . LEU A 1 522 ? 7.847 33.273 54.052 1.00 22.21 ? 522 LEU A CD1 1 ATOM 3987 C CD2 . LEU A 1 522 ? 7.546 31.047 55.155 1.00 23.66 ? 522 LEU A CD2 1 ATOM 3988 N N . ILE A 1 523 ? 6.478 32.877 50.490 1.00 20.36 ? 523 ILE A N 1 ATOM 3989 C CA . ILE A 1 523 ? 7.124 32.506 49.240 1.00 20.93 ? 523 ILE A CA 1 ATOM 3990 C C . ILE A 1 523 ? 8.599 32.326 49.566 1.00 21.08 ? 523 ILE A C 1 ATOM 3991 O O . ILE A 1 523 ? 9.249 33.260 50.022 1.00 21.77 ? 523 ILE A O 1 ATOM 3992 C CB . ILE A 1 523 ? 6.937 33.633 48.162 1.00 20.54 ? 523 ILE A CB 1 ATOM 3993 C CG1 . ILE A 1 523 ? 5.441 33.867 47.837 1.00 20.32 ? 523 ILE A CG1 1 ATOM 3994 C CG2 . ILE A 1 523 ? 7.768 33.343 46.898 1.00 21.07 ? 523 ILE A CG2 1 ATOM 3995 C CD1 . ILE A 1 523 ? 4.750 32.736 47.009 1.00 18.30 ? 523 ILE A CD1 1 ATOM 3996 N N . SER A 1 524 ? 9.113 31.111 49.388 1.00 20.97 ? 524 SER A N 1 ATOM 3997 C CA . SER A 1 524 ? 10.502 30.828 49.734 1.00 21.39 ? 524 SER A CA 1 ATOM 3998 C C . SER A 1 524 ? 10.997 29.622 48.961 1.00 21.27 ? 524 SER A C 1 ATOM 3999 O O . SER A 1 524 ? 10.203 28.819 48.485 1.00 20.34 ? 524 SER A O 1 ATOM 4000 C CB . SER A 1 524 ? 10.671 30.598 51.252 1.00 21.95 ? 524 SER A CB 1 ATOM 4001 O OG . SER A 1 524 ? 10.025 29.404 51.672 1.00 22.82 ? 524 SER A OG 1 ATOM 4002 N N . GLY A 1 525 ? 12.312 29.500 48.833 1.00 21.58 ? 525 GLY A N 1 ATOM 4003 C CA . GLY A 1 525 ? 12.894 28.328 48.193 1.00 21.79 ? 525 GLY A CA 1 ATOM 4004 C C . GLY A 1 525 ? 13.199 27.231 49.198 1.00 22.14 ? 525 GLY A C 1 ATOM 4005 O O . GLY A 1 525 ? 13.745 26.211 48.838 1.00 22.01 ? 525 GLY A O 1 ATOM 4006 N N . ARG A 1 526 ? 12.821 27.439 50.459 1.00 22.72 ? 526 ARG A N 1 ATOM 4007 C CA . ARG A 1 526 ? 13.317 26.624 51.567 1.00 23.68 ? 526 ARG A CA 1 ATOM 4008 C C . ARG A 1 526 ? 12.651 27.080 52.863 1.00 24.16 ? 526 ARG A C 1 ATOM 4009 O O . ARG A 1 526 ? 12.067 28.163 52.903 1.00 23.61 ? 526 ARG A O 1 ATOM 4010 C CB . ARG A 1 526 ? 14.832 26.838 51.708 1.00 24.15 ? 526 ARG A CB 1 ATOM 4011 C CG . ARG A 1 526 ? 15.194 28.317 51.688 1.00 24.66 ? 526 ARG A CG 1 ATOM 4012 C CD . ARG A 1 526 ? 16.649 28.567 51.866 1.00 25.83 ? 526 ARG A CD 1 ATOM 4013 N NE . ARG A 1 526 ? 16.988 29.920 51.427 1.00 26.09 ? 526 ARG A NE 1 ATOM 4014 C CZ . ARG A 1 526 ? 18.194 30.293 51.017 1.00 24.75 ? 526 ARG A CZ 1 ATOM 4015 N NH1 . ARG A 1 526 ? 19.203 29.425 51.006 1.00 25.57 ? 526 ARG A NH1 1 ATOM 4016 N NH2 . ARG A 1 526 ? 18.391 31.542 50.631 1.00 25.52 ? 526 ARG A NH2 1 ATOM 4017 N N . PRO A 1 527 ? 12.745 26.258 53.925 1.00 25.12 ? 527 PRO A N 1 ATOM 4018 C CA . PRO A 1 527 ? 12.414 26.750 55.264 1.00 25.91 ? 527 PRO A CA 1 ATOM 4019 C C . PRO A 1 527 ? 13.264 27.972 55.621 1.00 26.13 ? 527 PRO A C 1 ATOM 4020 O O . PRO A 1 527 ? 14.473 28.023 55.321 1.00 26.39 ? 527 PRO A O 1 ATOM 4021 C CB . PRO A 1 527 ? 12.784 25.581 56.190 1.00 26.69 ? 527 PRO A CB 1 ATOM 4022 C CG . PRO A 1 527 ? 12.764 24.386 55.319 1.00 28.17 ? 527 PRO A CG 1 ATOM 4023 C CD . PRO A 1 527 ? 13.176 24.848 53.944 1.00 25.71 ? 527 PRO A CD 1 ATOM 4024 N N . VAL A 1 528 ? 12.611 28.952 56.229 1.00 25.62 ? 528 VAL A N 1 ATOM 4025 C CA . VAL A 1 528 ? 13.253 30.165 56.714 1.00 25.54 ? 528 VAL A CA 1 ATOM 4026 C C . VAL A 1 528 ? 12.721 30.371 58.132 1.00 26.41 ? 528 VAL A C 1 ATOM 4027 O O . VAL A 1 528 ? 11.757 29.708 58.526 1.00 26.34 ? 528 VAL A O 1 ATOM 4028 C CB . VAL A 1 528 ? 12.955 31.396 55.785 1.00 25.31 ? 528 VAL A CB 1 ATOM 4029 C CG1 . VAL A 1 528 ? 13.625 31.220 54.403 1.00 24.22 ? 528 VAL A CG1 1 ATOM 4030 C CG2 . VAL A 1 528 ? 11.439 31.638 55.650 1.00 23.17 ? 528 VAL A CG2 1 ATOM 4031 N N . VAL A 1 529 ? 13.352 31.259 58.900 1.00 27.01 ? 529 VAL A N 1 ATOM 4032 C CA . VAL A 1 529 ? 12.906 31.553 60.254 1.00 27.90 ? 529 VAL A CA 1 ATOM 4033 C C . VAL A 1 529 ? 11.447 31.995 60.150 1.00 27.25 ? 529 VAL A C 1 ATOM 4034 O O . VAL A 1 529 ? 11.120 32.939 59.417 1.00 26.94 ? 529 VAL A O 1 ATOM 4035 C CB . VAL A 1 529 ? 13.803 32.596 60.979 1.00 28.42 ? 529 VAL A CB 1 ATOM 4036 C CG1 . VAL A 1 529 ? 13.280 32.867 62.416 1.00 30.76 ? 529 VAL A CG1 1 ATOM 4037 C CG2 . VAL A 1 529 ? 15.247 32.105 61.041 1.00 29.49 ? 529 VAL A CG2 1 ATOM 4038 N N . VAL A 1 530 ? 10.574 31.277 60.856 1.00 27.02 ? 530 VAL A N 1 ATOM 4039 C CA . VAL A 1 530 ? 9.128 31.427 60.672 1.00 25.98 ? 530 VAL A CA 1 ATOM 4040 C C . VAL A 1 530 ? 8.327 31.647 61.964 1.00 27.03 ? 530 VAL A C 1 ATOM 4041 O O . VAL A 1 530 ? 7.151 32.007 61.892 1.00 26.58 ? 530 VAL A O 1 ATOM 4042 C CB . VAL A 1 530 ? 8.551 30.231 59.845 1.00 25.36 ? 530 VAL A CB 1 ATOM 4043 C CG1 . VAL A 1 530 ? 8.389 29.004 60.716 1.00 26.34 ? 530 VAL A CG1 1 ATOM 4044 C CG2 . VAL A 1 530 ? 7.241 30.595 59.174 1.00 23.96 ? 530 VAL A CG2 1 ATOM 4045 N N . GLN A 1 531 ? 8.941 31.468 63.138 1.00 28.06 ? 531 GLN A N 1 ATOM 4046 C CA . GLN A 1 531 ? 8.188 31.667 64.398 1.00 28.99 ? 531 GLN A CA 1 ATOM 4047 C C . GLN A 1 531 ? 7.471 33.027 64.485 1.00 29.33 ? 531 GLN A C 1 ATOM 4048 O O . GLN A 1 531 ? 6.289 33.075 64.835 1.00 29.58 ? 531 GLN A O 1 ATOM 4049 C CB . GLN A 1 531 ? 9.050 31.447 65.657 1.00 30.26 ? 531 GLN A CB 1 ATOM 4050 C CG . GLN A 1 531 ? 9.439 30.016 65.898 1.00 30.06 ? 531 GLN A CG 1 ATOM 4051 C CD . GLN A 1 531 ? 10.792 29.668 65.298 1.00 30.30 ? 531 GLN A CD 1 ATOM 4052 O OE1 . GLN A 1 531 ? 11.188 30.183 64.239 1.00 29.93 ? 531 GLN A OE1 1 ATOM 4053 N NE2 . GLN A 1 531 ? 11.505 28.776 65.966 1.00 29.87 ? 531 GLN A NE2 1 ATOM 4054 N N . PRO A 1 532 ? 8.191 34.139 64.217 1.00 29.73 ? 532 PRO A N 1 ATOM 4055 C CA . PRO A 1 532 ? 7.534 35.450 64.258 1.00 29.66 ? 532 PRO A CA 1 ATOM 4056 C C . PRO A 1 532 ? 6.373 35.623 63.271 1.00 28.86 ? 532 PRO A C 1 ATOM 4057 O O . PRO A 1 532 ? 5.370 36.252 63.624 1.00 29.10 ? 532 PRO A O 1 ATOM 4058 C CB . PRO A 1 532 ? 8.686 36.421 63.971 1.00 29.78 ? 532 PRO A CB 1 ATOM 4059 C CG . PRO A 1 532 ? 9.914 35.667 64.458 1.00 30.63 ? 532 PRO A CG 1 ATOM 4060 C CD . PRO A 1 532 ? 9.643 34.276 63.982 1.00 29.84 ? 532 PRO A CD 1 ATOM 4061 N N . LEU A 1 533 ? 6.505 35.083 62.059 1.00 28.25 ? 533 LEU A N 1 ATOM 4062 C CA . LEU A 1 533 ? 5.424 35.105 61.079 1.00 27.22 ? 533 LEU A CA 1 ATOM 4063 C C . LEU A 1 533 ? 4.226 34.286 61.567 1.00 27.77 ? 533 LEU A C 1 ATOM 4064 O O . LEU A 1 533 ? 3.081 34.713 61.439 1.00 28.24 ? 533 LEU A O 1 ATOM 4065 C CB . LEU A 1 533 ? 5.903 34.553 59.727 1.00 26.21 ? 533 LEU A CB 1 ATOM 4066 C CG . LEU A 1 533 ? 6.831 35.429 58.886 1.00 26.16 ? 533 LEU A CG 1 ATOM 4067 C CD1 . LEU A 1 533 ? 7.368 34.601 57.701 1.00 23.99 ? 533 LEU A CD1 1 ATOM 4068 C CD2 . LEU A 1 533 ? 6.129 36.709 58.399 1.00 24.90 ? 533 LEU A CD2 1 ATOM 4069 N N . LEU A 1 534 ? 4.511 33.104 62.101 1.00 27.99 ? 534 LEU A N 1 ATOM 4070 C CA . LEU A 1 534 ? 3.514 32.242 62.728 1.00 29.04 ? 534 LEU A CA 1 ATOM 4071 C C . LEU A 1 534 ? 2.747 32.929 63.881 1.00 29.58 ? 534 LEU A C 1 ATOM 4072 O O . LEU A 1 534 ? 1.509 32.884 63.924 1.00 29.78 ? 534 LEU A O 1 ATOM 4073 C CB . LEU A 1 534 ? 4.213 30.973 63.236 1.00 29.68 ? 534 LEU A CB 1 ATOM 4074 C CG . LEU A 1 534 ? 3.993 29.584 62.603 1.00 30.29 ? 534 LEU A CG 1 ATOM 4075 C CD1 . LEU A 1 534 ? 3.297 29.522 61.261 1.00 25.98 ? 534 LEU A CD1 1 ATOM 4076 C CD2 . LEU A 1 534 ? 5.272 28.784 62.588 1.00 29.73 ? 534 LEU A CD2 1 ATOM 4077 N N . ALA A 1 535 ? 3.479 33.563 64.800 1.00 29.85 ? 535 ALA A N 1 ATOM 4078 C CA . ALA A 1 535 ? 2.873 34.214 65.959 1.00 30.28 ? 535 ALA A CA 1 ATOM 4079 C C . ALA A 1 535 ? 1.847 35.278 65.552 1.00 29.73 ? 535 ALA A C 1 ATOM 4080 O O . ALA A 1 535 ? 0.789 35.397 66.186 1.00 30.33 ? 535 ALA A O 1 ATOM 4081 C CB . ALA A 1 535 ? 3.951 34.811 66.884 1.00 30.96 ? 535 ALA A CB 1 ATOM 4082 N N . ALA A 1 536 ? 2.148 36.027 64.491 1.00 28.12 ? 536 ALA A N 1 ATOM 4083 C CA . ALA A 1 536 ? 1.265 37.098 64.025 1.00 28.00 ? 536 ALA A CA 1 ATOM 4084 C C . ALA A 1 536 ? 0.035 36.597 63.245 1.00 27.03 ? 536 ALA A C 1 ATOM 4085 O O . ALA A 1 536 ? -1.013 37.245 63.244 1.00 27.84 ? 536 ALA A O 1 ATOM 4086 C CB . ALA A 1 536 ? 2.063 38.125 63.184 1.00 27.53 ? 536 ALA A CB 1 ATOM 4087 N N . SER A 1 537 ? 0.157 35.442 62.600 1.00 26.53 ? 537 SER A N 1 ATOM 4088 C CA . SER A 1 537 ? -0.816 35.008 61.586 1.00 26.02 ? 537 SER A CA 1 ATOM 4089 C C . SER A 1 537 ? -1.910 34.079 62.122 1.00 26.23 ? 537 SER A C 1 ATOM 4090 O O . SER A 1 537 ? -1.646 33.237 62.978 1.00 26.81 ? 537 SER A O 1 ATOM 4091 C CB . SER A 1 537 ? -0.091 34.320 60.424 1.00 25.14 ? 537 SER A CB 1 ATOM 4092 O OG . SER A 1 537 ? 0.988 35.116 59.953 1.00 25.73 ? 537 SER A OG 1 ATOM 4093 N N . ASP A 1 538 ? -3.127 34.228 61.592 1.00 25.63 ? 538 ASP A N 1 ATOM 4094 C CA . ASP A 1 538 ? -4.214 33.277 61.855 1.00 25.72 ? 538 ASP A CA 1 ATOM 4095 C C . ASP A 1 538 ? -3.974 31.983 61.080 1.00 25.40 ? 538 ASP A C 1 ATOM 4096 O O . ASP A 1 538 ? -4.075 30.896 61.629 1.00 26.18 ? 538 ASP A O 1 ATOM 4097 C CB . ASP A 1 538 ? -5.562 33.875 61.465 1.00 25.35 ? 538 ASP A CB 1 ATOM 4098 C CG . ASP A 1 538 ? -5.926 35.061 62.310 1.00 26.19 ? 538 ASP A CG 1 ATOM 4099 O OD1 . ASP A 1 538 ? -5.577 36.191 61.910 1.00 28.69 ? 538 ASP A OD1 1 ATOM 4100 O OD2 . ASP A 1 538 ? -6.527 34.858 63.380 1.00 22.76 ? 538 ASP A OD2 1 ATOM 4101 N N . ALA A 1 539 ? -3.642 32.112 59.803 1.00 23.81 ? 539 ALA A N 1 ATOM 4102 C CA . ALA A 1 539 ? -3.244 30.972 58.998 1.00 23.71 ? 539 ALA A CA 1 ATOM 4103 C C . ALA A 1 539 ? -1.935 31.309 58.313 1.00 23.17 ? 539 ALA A C 1 ATOM 4104 O O . ALA A 1 539 ? -1.629 32.482 58.071 1.00 22.67 ? 539 ALA A O 1 ATOM 4105 C CB . ALA A 1 539 ? -4.312 30.643 57.968 1.00 22.92 ? 539 ALA A CB 1 ATOM 4106 N N . LEU A 1 540 ? -1.146 30.285 58.025 1.00 23.35 ? 540 LEU A N 1 ATOM 4107 C CA . LEU A 1 540 ? 0.094 30.493 57.296 1.00 23.54 ? 540 LEU A CA 1 ATOM 4108 C C . LEU A 1 540 ? 0.347 29.316 56.378 1.00 23.25 ? 540 LEU A C 1 ATOM 4109 O O . LEU A 1 540 ? 0.294 28.150 56.807 1.00 23.99 ? 540 LEU A O 1 ATOM 4110 C CB . LEU A 1 540 ? 1.283 30.735 58.241 1.00 23.64 ? 540 LEU A CB 1 ATOM 4111 C CG . LEU A 1 540 ? 2.615 31.212 57.625 1.00 24.78 ? 540 LEU A CG 1 ATOM 4112 C CD1 . LEU A 1 540 ? 3.361 32.147 58.582 1.00 26.43 ? 540 LEU A CD1 1 ATOM 4113 C CD2 . LEU A 1 540 ? 3.536 30.064 57.189 1.00 26.10 ? 540 LEU A CD2 1 ATOM 4114 N N . VAL A 1 541 ? 0.636 29.655 55.123 1.00 21.98 ? 541 VAL A N 1 ATOM 4115 C CA . VAL A 1 541 ? 0.917 28.692 54.056 1.00 21.20 ? 541 VAL A CA 1 ATOM 4116 C C . VAL A 1 541 ? 2.361 28.812 53.550 1.00 21.14 ? 541 VAL A C 1 ATOM 4117 O O . VAL A 1 541 ? 2.818 29.912 53.198 1.00 20.92 ? 541 VAL A O 1 ATOM 4118 C CB . VAL A 1 541 ? -0.061 28.916 52.873 1.00 20.56 ? 541 VAL A CB 1 ATOM 4119 C CG1 . VAL A 1 541 ? 0.264 27.975 51.670 1.00 19.17 ? 541 VAL A CG1 1 ATOM 4120 C CG2 . VAL A 1 541 ? -1.507 28.762 53.340 1.00 18.86 ? 541 VAL A CG2 1 ATOM 4121 N N . ALA A 1 542 ? 3.079 27.684 53.524 1.00 21.21 ? 542 ALA A N 1 ATOM 4122 C CA . ALA A 1 542 ? 4.365 27.611 52.823 1.00 21.39 ? 542 ALA A CA 1 ATOM 4123 C C . ALA A 1 542 ? 4.066 27.288 51.365 1.00 20.75 ? 542 ALA A C 1 ATOM 4124 O O . ALA A 1 542 ? 3.696 26.142 51.037 1.00 19.97 ? 542 ALA A O 1 ATOM 4125 C CB . ALA A 1 542 ? 5.273 26.525 53.441 1.00 21.77 ? 542 ALA A CB 1 ATOM 4126 N N . ALA A 1 543 ? 4.162 28.318 50.516 1.00 20.68 ? 543 ALA A N 1 ATOM 4127 C CA . ALA A 1 543 ? 3.855 28.216 49.080 1.00 20.63 ? 543 ALA A CA 1 ATOM 4128 C C . ALA A 1 543 ? 5.076 27.947 48.187 1.00 20.69 ? 543 ALA A C 1 ATOM 4129 O O . ALA A 1 543 ? 4.914 27.784 46.976 1.00 20.58 ? 543 ALA A O 1 ATOM 4130 C CB . ALA A 1 543 ? 3.128 29.495 48.581 1.00 20.65 ? 543 ALA A CB 1 ATOM 4131 N N . TRP A 1 544 ? 6.275 27.914 48.780 1.00 20.55 ? 544 TRP A N 1 ATOM 4132 C CA . TRP A 1 544 ? 7.535 27.671 48.073 1.00 20.35 ? 544 TRP A CA 1 ATOM 4133 C C . TRP A 1 544 ? 7.698 28.679 46.926 1.00 20.11 ? 544 TRP A C 1 ATOM 4134 O O . TRP A 1 544 ? 7.472 29.865 47.129 1.00 19.62 ? 544 TRP A O 1 ATOM 4135 C CB . TRP A 1 544 ? 7.640 26.210 47.598 1.00 20.85 ? 544 TRP A CB 1 ATOM 4136 C CG . TRP A 1 544 ? 7.243 25.229 48.667 1.00 21.51 ? 544 TRP A CG 1 ATOM 4137 C CD1 . TRP A 1 544 ? 6.100 24.478 48.705 1.00 21.74 ? 544 TRP A CD1 1 ATOM 4138 C CD2 . TRP A 1 544 ? 7.964 24.930 49.878 1.00 22.83 ? 544 TRP A CD2 1 ATOM 4139 N NE1 . TRP A 1 544 ? 6.068 23.723 49.854 1.00 22.33 ? 544 TRP A NE1 1 ATOM 4140 C CE2 . TRP A 1 544 ? 7.193 23.979 50.595 1.00 23.27 ? 544 TRP A CE2 1 ATOM 4141 C CE3 . TRP A 1 544 ? 9.189 25.372 50.426 1.00 22.51 ? 544 TRP A CE3 1 ATOM 4142 C CZ2 . TRP A 1 544 ? 7.608 23.446 51.827 1.00 23.84 ? 544 TRP A CZ2 1 ATOM 4143 C CZ3 . TRP A 1 544 ? 9.595 24.858 51.659 1.00 23.83 ? 544 TRP A CZ3 1 ATOM 4144 C CH2 . TRP A 1 544 ? 8.805 23.896 52.344 1.00 24.35 ? 544 TRP A CH2 1 ATOM 4145 N N . LEU A 1 545 ? 8.094 28.205 45.741 1.00 20.01 ? 545 LEU A N 1 ATOM 4146 C CA . LEU A 1 545 ? 8.207 29.063 44.542 1.00 20.17 ? 545 LEU A CA 1 ATOM 4147 C C . LEU A 1 545 ? 7.246 28.552 43.467 1.00 19.90 ? 545 LEU A C 1 ATOM 4148 O O . LEU A 1 545 ? 7.653 27.841 42.557 1.00 20.41 ? 545 LEU A O 1 ATOM 4149 C CB . LEU A 1 545 ? 9.660 29.117 44.049 1.00 19.30 ? 545 LEU A CB 1 ATOM 4150 C CG . LEU A 1 545 ? 10.650 29.624 45.113 1.00 20.75 ? 545 LEU A CG 1 ATOM 4151 C CD1 . LEU A 1 545 ? 12.086 29.332 44.675 1.00 18.75 ? 545 LEU A CD1 1 ATOM 4152 C CD2 . LEU A 1 545 ? 10.435 31.145 45.418 1.00 18.30 ? 545 LEU A CD2 1 ATOM 4153 N N . PRO A 1 546 ? 5.950 28.900 43.592 1.00 20.43 ? 546 PRO A N 1 ATOM 4154 C CA . PRO A 1 546 ? 4.884 28.205 42.851 1.00 20.13 ? 546 PRO A CA 1 ATOM 4155 C C . PRO A 1 546 ? 4.864 28.417 41.324 1.00 20.15 ? 546 PRO A C 1 ATOM 4156 O O . PRO A 1 546 ? 4.196 27.660 40.619 1.00 20.09 ? 546 PRO A O 1 ATOM 4157 C CB . PRO A 1 546 ? 3.602 28.744 43.512 1.00 20.27 ? 546 PRO A CB 1 ATOM 4158 C CG . PRO A 1 546 ? 3.991 30.122 43.963 1.00 20.22 ? 546 PRO A CG 1 ATOM 4159 C CD . PRO A 1 546 ? 5.405 29.969 44.457 1.00 20.00 ? 546 PRO A CD 1 ATOM 4160 N N . GLY A 1 547 ? 5.587 29.422 40.824 1.00 19.94 ? 547 GLY A N 1 ATOM 4161 C CA . GLY A 1 547 ? 5.701 29.638 39.384 1.00 19.91 ? 547 GLY A CA 1 ATOM 4162 C C . GLY A 1 547 ? 4.720 30.649 38.813 1.00 20.19 ? 547 GLY A C 1 ATOM 4163 O O . GLY A 1 547 ? 4.195 31.495 39.540 1.00 20.81 ? 547 GLY A O 1 ATOM 4164 N N . SER A 1 548 ? 4.439 30.536 37.519 1.00 20.38 ? 548 SER A N 1 ATOM 4165 C CA . SER A 1 548 ? 3.630 31.556 36.832 1.00 21.35 ? 548 SER A CA 1 ATOM 4166 C C . SER A 1 548 ? 2.138 31.524 37.198 1.00 21.68 ? 548 SER A C 1 ATOM 4167 O O . SER A 1 548 ? 1.430 32.521 37.019 1.00 22.31 ? 548 SER A O 1 ATOM 4168 C CB . SER A 1 548 ? 3.823 31.484 35.310 1.00 21.05 ? 548 SER A CB 1 ATOM 4169 O OG . SER A 1 548 ? 3.541 30.186 34.798 1.00 20.59 ? 548 SER A OG 1 ATOM 4170 N N . GLU A 1 549 ? 1.667 30.390 37.714 1.00 22.17 ? 549 GLU A N 1 ATOM 4171 C CA . GLU A 1 549 ? 0.217 30.166 37.843 1.00 22.76 ? 549 GLU A CA 1 ATOM 4172 C C . GLU A 1 549 ? -0.301 30.373 39.269 1.00 22.59 ? 549 GLU A C 1 ATOM 4173 O O . GLU A 1 549 ? -0.595 29.408 39.988 1.00 22.60 ? 549 GLU A O 1 ATOM 4174 C CB . GLU A 1 549 ? -0.175 28.790 37.283 1.00 22.93 ? 549 GLU A CB 1 ATOM 4175 C CG . GLU A 1 549 ? 0.214 28.553 35.790 1.00 23.82 ? 549 GLU A CG 1 ATOM 4176 C CD . GLU A 1 549 ? -0.038 29.757 34.878 1.00 25.37 ? 549 GLU A CD 1 ATOM 4177 O OE1 . GLU A 1 549 ? -1.169 30.308 34.904 1.00 26.38 ? 549 GLU A OE1 1 ATOM 4178 O OE2 . GLU A 1 549 ? 0.901 30.144 34.132 1.00 25.21 ? 549 GLU A OE2 1 ATOM 4179 N N . GLY A 1 550 ? -0.432 31.645 39.653 1.00 22.80 ? 550 GLY A N 1 ATOM 4180 C CA . GLY A 1 550 ? -0.753 32.034 41.030 1.00 21.91 ? 550 GLY A CA 1 ATOM 4181 C C . GLY A 1 550 ? -2.139 31.640 41.490 1.00 22.42 ? 550 GLY A C 1 ATOM 4182 O O . GLY A 1 550 ? -2.443 31.678 42.686 1.00 21.21 ? 550 GLY A O 1 ATOM 4183 N N . GLN A 1 551 ? -2.989 31.271 40.541 1.00 22.81 ? 551 GLN A N 1 ATOM 4184 C CA . GLN A 1 551 ? -4.319 30.756 40.870 1.00 23.38 ? 551 GLN A CA 1 ATOM 4185 C C . GLN A 1 551 ? -4.284 29.419 41.598 1.00 23.00 ? 551 GLN A C 1 ATOM 4186 O O . GLN A 1 551 ? -5.255 29.056 42.233 1.00 23.00 ? 551 GLN A O 1 ATOM 4187 C CB . GLN A 1 551 ? -5.199 30.666 39.619 1.00 23.90 ? 551 GLN A CB 1 ATOM 4188 C CG . GLN A 1 551 ? -5.690 32.034 39.187 1.00 26.04 ? 551 GLN A CG 1 ATOM 4189 C CD . GLN A 1 551 ? -6.307 32.044 37.809 1.00 30.06 ? 551 GLN A CD 1 ATOM 4190 O OE1 . GLN A 1 551 ? -7.522 32.229 37.665 1.00 32.83 ? 551 GLN A OE1 1 ATOM 4191 N NE2 . GLN A 1 551 ? -5.480 31.840 36.784 1.00 28.01 ? 551 GLN A NE2 1 ATOM 4192 N N . GLY A 1 552 ? -3.172 28.687 41.491 1.00 22.86 ? 552 GLY A N 1 ATOM 4193 C CA . GLY A 1 552 ? -2.949 27.504 42.315 1.00 22.57 ? 552 GLY A CA 1 ATOM 4194 C C . GLY A 1 552 ? -3.004 27.807 43.813 1.00 22.88 ? 552 GLY A C 1 ATOM 4195 O O . GLY A 1 552 ? -3.532 27.008 44.595 1.00 23.09 ? 552 GLY A O 1 ATOM 4196 N N . VAL A 1 553 ? -2.462 28.967 44.198 1.00 22.00 ? 553 VAL A N 1 ATOM 4197 C CA . VAL A 1 553 ? -2.539 29.481 45.572 1.00 21.14 ? 553 VAL A CA 1 ATOM 4198 C C . VAL A 1 553 ? -3.986 29.759 46.018 1.00 21.28 ? 553 VAL A C 1 ATOM 4199 O O . VAL A 1 553 ? -4.412 29.282 47.054 1.00 20.99 ? 553 VAL A O 1 ATOM 4200 C CB . VAL A 1 553 ? -1.691 30.763 45.759 1.00 20.87 ? 553 VAL A CB 1 ATOM 4201 C CG1 . VAL A 1 553 ? -1.804 31.286 47.206 1.00 19.27 ? 553 VAL A CG1 1 ATOM 4202 C CG2 . VAL A 1 553 ? -0.226 30.514 45.385 1.00 20.22 ? 553 VAL A CG2 1 ATOM 4203 N N . THR A 1 554 ? -4.732 30.521 45.228 1.00 21.50 ? 554 THR A N 1 ATOM 4204 C CA . THR A 1 554 ? -6.113 30.866 45.588 1.00 21.82 ? 554 THR A CA 1 ATOM 4205 C C . THR A 1 554 ? -7.083 29.680 45.483 1.00 22.52 ? 554 THR A C 1 ATOM 4206 O O . THR A 1 554 ? -8.122 29.676 46.142 1.00 22.95 ? 554 THR A O 1 ATOM 4207 C CB . THR A 1 554 ? -6.606 32.075 44.781 1.00 21.93 ? 554 THR A CB 1 ATOM 4208 O OG1 . THR A 1 554 ? -6.423 31.809 43.381 1.00 22.74 ? 554 THR A OG1 1 ATOM 4209 C CG2 . THR A 1 554 ? -5.790 33.309 45.166 1.00 20.11 ? 554 THR A CG2 1 ATOM 4210 N N . ASP A 1 555 ? -6.726 28.680 44.672 1.00 22.43 ? 555 ASP A N 1 ATOM 4211 C CA . ASP A 1 555 ? -7.496 27.433 44.552 1.00 23.35 ? 555 ASP A CA 1 ATOM 4212 C C . ASP A 1 555 ? -7.618 26.748 45.908 1.00 23.97 ? 555 ASP A C 1 ATOM 4213 O O . ASP A 1 555 ? -8.659 26.157 46.236 1.00 25.08 ? 555 ASP A O 1 ATOM 4214 C CB . ASP A 1 555 ? -6.838 26.465 43.548 1.00 22.84 ? 555 ASP A CB 1 ATOM 4215 C CG . ASP A 1 555 ? -7.179 26.781 42.105 1.00 24.18 ? 555 ASP A CG 1 ATOM 4216 O OD1 . ASP A 1 555 ? -7.978 27.719 41.845 1.00 24.99 ? 555 ASP A OD1 1 ATOM 4217 O OD2 . ASP A 1 555 ? -6.643 26.088 41.218 1.00 24.30 ? 555 ASP A OD2 1 ATOM 4218 N N . ALA A 1 556 ? -6.552 26.833 46.699 1.00 23.53 ? 556 ALA A N 1 ATOM 4219 C CA . ALA A 1 556 ? -6.559 26.293 48.063 1.00 23.80 ? 556 ALA A CA 1 ATOM 4220 C C . ALA A 1 556 ? -7.094 27.303 49.102 1.00 23.63 ? 556 ALA A C 1 ATOM 4221 O O . ALA A 1 556 ? -7.912 26.943 49.951 1.00 23.98 ? 556 ALA A O 1 ATOM 4222 C CB . ALA A 1 556 ? -5.173 25.781 48.446 1.00 23.35 ? 556 ALA A CB 1 ATOM 4223 N N . LEU A 1 557 ? -6.661 28.560 49.014 1.00 22.83 ? 557 LEU A N 1 ATOM 4224 C CA . LEU A 1 557 ? -7.129 29.594 49.940 1.00 23.05 ? 557 LEU A CA 1 ATOM 4225 C C . LEU A 1 557 ? -8.653 29.718 50.006 1.00 23.62 ? 557 LEU A C 1 ATOM 4226 O O . LEU A 1 557 ? -9.207 29.929 51.095 1.00 23.46 ? 557 LEU A O 1 ATOM 4227 C CB . LEU A 1 557 ? -6.526 30.964 49.613 1.00 22.35 ? 557 LEU A CB 1 ATOM 4228 C CG . LEU A 1 557 ? -5.019 31.145 49.777 1.00 23.09 ? 557 LEU A CG 1 ATOM 4229 C CD1 . LEU A 1 557 ? -4.630 32.567 49.338 1.00 22.15 ? 557 LEU A CD1 1 ATOM 4230 C CD2 . LEU A 1 557 ? -4.554 30.854 51.213 1.00 22.57 ? 557 LEU A CD2 1 ATOM 4231 N N . PHE A 1 558 ? -9.321 29.603 48.848 1.00 23.98 ? 558 PHE A N 1 ATOM 4232 C CA . PHE A 1 558 ? -10.768 29.796 48.776 1.00 24.13 ? 558 PHE A CA 1 ATOM 4233 C C . PHE A 1 558 ? -11.560 28.485 48.789 1.00 25.30 ? 558 PHE A C 1 ATOM 4234 O O . PHE A 1 558 ? -12.794 28.484 48.658 1.00 25.21 ? 558 PHE A O 1 ATOM 4235 C CB . PHE A 1 558 ? -11.146 30.679 47.584 1.00 24.58 ? 558 PHE A CB 1 ATOM 4236 C CG . PHE A 1 558 ? -10.722 32.109 47.746 1.00 24.89 ? 558 PHE A CG 1 ATOM 4237 C CD1 . PHE A 1 558 ? -9.664 32.617 47.006 1.00 26.11 ? 558 PHE A CD1 1 ATOM 4238 C CD2 . PHE A 1 558 ? -11.359 32.937 48.670 1.00 24.36 ? 558 PHE A CD2 1 ATOM 4239 C CE1 . PHE A 1 558 ? -9.255 33.931 47.154 1.00 26.52 ? 558 PHE A CE1 1 ATOM 4240 C CE2 . PHE A 1 558 ? -10.963 34.243 48.831 1.00 24.93 ? 558 PHE A CE2 1 ATOM 4241 C CZ . PHE A 1 558 ? -9.892 34.748 48.068 1.00 24.75 ? 558 PHE A CZ 1 ATOM 4242 N N . GLY A 1 559 ? -10.853 27.377 48.976 1.00 24.89 ? 559 GLY A N 1 ATOM 4243 C CA . GLY A 1 559 ? -11.495 26.083 49.163 1.00 26.69 ? 559 GLY A CA 1 ATOM 4244 C C . GLY A 1 559 ? -12.012 25.366 47.920 1.00 27.74 ? 559 GLY A C 1 ATOM 4245 O O . GLY A 1 559 ? -12.769 24.419 48.041 1.00 28.58 ? 559 GLY A O 1 ATOM 4246 N N . ASP A 1 560 ? -11.611 25.798 46.726 1.00 28.11 ? 560 ASP A N 1 ATOM 4247 C CA . ASP A 1 560 ? -11.910 25.010 45.514 1.00 29.78 ? 560 ASP A CA 1 ATOM 4248 C C . ASP A 1 560 ? -11.299 23.613 45.606 1.00 29.89 ? 560 ASP A C 1 ATOM 4249 O O . ASP A 1 560 ? -11.853 22.639 45.077 1.00 30.94 ? 560 ASP A O 1 ATOM 4250 C CB . ASP A 1 560 ? -11.445 25.732 44.251 1.00 30.03 ? 560 ASP A CB 1 ATOM 4251 C CG . ASP A 1 560 ? -12.297 26.954 43.943 1.00 33.08 ? 560 ASP A CG 1 ATOM 4252 O OD1 . ASP A 1 560 ? -13.452 27.029 44.429 1.00 35.98 ? 560 ASP A OD1 1 ATOM 4253 O OD2 . ASP A 1 560 ? -11.815 27.847 43.220 1.00 37.18 ? 560 ASP A OD2 1 ATOM 4254 N N . PHE A 1 561 ? -10.170 23.525 46.307 1.00 28.83 ? 561 PHE A N 1 ATOM 4255 C CA . PHE A 1 561 ? -9.536 22.252 46.619 1.00 29.15 ? 561 PHE A CA 1 ATOM 4256 C C . PHE A 1 561 ? -9.091 22.305 48.058 1.00 28.73 ? 561 PHE A C 1 ATOM 4257 O O . PHE A 1 561 ? -8.851 23.398 48.583 1.00 28.55 ? 561 PHE A O 1 ATOM 4258 C CB . PHE A 1 561 ? -8.332 22.035 45.704 1.00 28.18 ? 561 PHE A CB 1 ATOM 4259 C CG . PHE A 1 561 ? -8.709 21.865 44.268 1.00 29.46 ? 561 PHE A CG 1 ATOM 4260 C CD1 . PHE A 1 561 ? -8.813 22.977 43.421 1.00 28.62 ? 561 PHE A CD1 1 ATOM 4261 C CD2 . PHE A 1 561 ? -9.011 20.593 43.766 1.00 29.25 ? 561 PHE A CD2 1 ATOM 4262 C CE1 . PHE A 1 561 ? -9.194 22.824 42.086 1.00 28.49 ? 561 PHE A CE1 1 ATOM 4263 C CE2 . PHE A 1 561 ? -9.386 20.431 42.436 1.00 31.47 ? 561 PHE A CE2 1 ATOM 4264 C CZ . PHE A 1 561 ? -9.477 21.558 41.596 1.00 30.04 ? 561 PHE A CZ 1 ATOM 4265 N N . GLY A 1 562 ? -9.016 21.142 48.706 1.00 28.96 ? 562 GLY A N 1 ATOM 4266 C CA . GLY A 1 562 ? -8.407 21.056 50.041 1.00 28.43 ? 562 GLY A CA 1 ATOM 4267 C C . GLY A 1 562 ? -6.888 21.131 49.983 1.00 26.78 ? 562 GLY A C 1 ATOM 4268 O O . GLY A 1 562 ? -6.283 20.760 48.970 1.00 26.79 ? 562 GLY A O 1 ATOM 4269 N N . PHE A 1 563 ? -6.267 21.602 51.070 1.00 26.29 ? 563 PHE A N 1 ATOM 4270 C CA . PHE A 1 563 ? -4.797 21.601 51.220 1.00 25.15 ? 563 PHE A CA 1 ATOM 4271 C C . PHE A 1 563 ? -4.286 20.188 51.414 1.00 25.39 ? 563 PHE A C 1 ATOM 4272 O O . PHE A 1 563 ? -4.823 19.464 52.242 1.00 26.10 ? 563 PHE A O 1 ATOM 4273 C CB . PHE A 1 563 ? -4.370 22.430 52.441 1.00 24.93 ? 563 PHE A CB 1 ATOM 4274 C CG . PHE A 1 563 ? -4.280 23.902 52.177 1.00 23.69 ? 563 PHE A CG 1 ATOM 4275 C CD1 . PHE A 1 563 ? -5.375 24.735 52.431 1.00 24.36 ? 563 PHE A CD1 1 ATOM 4276 C CD2 . PHE A 1 563 ? -3.100 24.458 51.679 1.00 21.59 ? 563 PHE A CD2 1 ATOM 4277 C CE1 . PHE A 1 563 ? -5.294 26.110 52.199 1.00 23.00 ? 563 PHE A CE1 1 ATOM 4278 C CE2 . PHE A 1 563 ? -3.008 25.819 51.443 1.00 20.86 ? 563 PHE A CE2 1 ATOM 4279 C CZ . PHE A 1 563 ? -4.118 26.654 51.703 1.00 21.70 ? 563 PHE A CZ 1 ATOM 4280 N N . THR A 1 564 ? -3.262 19.780 50.659 1.00 24.86 ? 564 THR A N 1 ATOM 4281 C CA . THR A 1 564 ? -2.743 18.398 50.773 1.00 25.52 ? 564 THR A CA 1 ATOM 4282 C C . THR A 1 564 ? -1.222 18.291 50.889 1.00 25.27 ? 564 THR A C 1 ATOM 4283 O O . THR A 1 564 ? -0.703 17.230 51.241 1.00 25.22 ? 564 THR A O 1 ATOM 4284 C CB . THR A 1 564 ? -3.212 17.456 49.611 1.00 26.18 ? 564 THR A CB 1 ATOM 4285 O OG1 . THR A 1 564 ? -2.908 18.052 48.345 1.00 26.19 ? 564 THR A OG1 1 ATOM 4286 C CG2 . THR A 1 564 ? -4.704 17.165 49.688 1.00 27.76 ? 564 THR A CG2 1 ATOM 4287 N N . GLY A 1 565 ? -0.509 19.370 50.581 1.00 24.51 ? 565 GLY A N 1 ATOM 4288 C CA . GLY A 1 565 ? 0.961 19.357 50.613 1.00 24.34 ? 565 GLY A CA 1 ATOM 4289 C C . GLY A 1 565 ? 1.495 19.009 51.995 1.00 25.60 ? 565 GLY A C 1 ATOM 4290 O O . GLY A 1 565 ? 0.899 19.380 53.010 1.00 25.82 ? 565 GLY A O 1 ATOM 4291 N N . ARG A 1 566 ? 2.613 18.286 52.017 1.00 25.62 ? 566 ARG A N 1 ATOM 4292 C CA . ARG A 1 566 ? 3.328 17.944 53.242 1.00 26.49 ? 566 ARG A CA 1 ATOM 4293 C C . ARG A 1 566 ? 4.813 18.299 53.085 1.00 26.16 ? 566 ARG A C 1 ATOM 4294 O O . ARG A 1 566 ? 5.380 18.143 51.998 1.00 24.87 ? 566 ARG A O 1 ATOM 4295 C CB . ARG A 1 566 ? 3.144 16.457 53.544 1.00 27.97 ? 566 ARG A CB 1 ATOM 4296 C CG . ARG A 1 566 ? 1.664 16.094 53.775 1.00 30.54 ? 566 ARG A CG 1 ATOM 4297 C CD . ARG A 1 566 ? 1.450 14.692 54.277 1.00 35.37 ? 566 ARG A CD 1 ATOM 4298 N NE . ARG A 1 566 ? 1.964 13.670 53.368 1.00 38.65 ? 566 ARG A NE 1 ATOM 4299 C CZ . ARG A 1 566 ? 1.240 13.046 52.438 1.00 41.46 ? 566 ARG A CZ 1 ATOM 4300 N NH1 . ARG A 1 566 ? 1.809 12.115 51.679 1.00 41.29 ? 566 ARG A NH1 1 ATOM 4301 N NH2 . ARG A 1 566 ? -0.055 13.335 52.276 1.00 42.16 ? 566 ARG A NH2 1 ATOM 4302 N N . LEU A 1 567 ? 5.440 18.768 54.163 1.00 25.71 ? 567 LEU A N 1 ATOM 4303 C CA . LEU A 1 567 ? 6.837 19.202 54.096 1.00 25.46 ? 567 LEU A CA 1 ATOM 4304 C C . LEU A 1 567 ? 7.751 18.120 53.515 1.00 25.93 ? 567 LEU A C 1 ATOM 4305 O O . LEU A 1 567 ? 7.760 16.988 54.001 1.00 27.07 ? 567 LEU A O 1 ATOM 4306 C CB . LEU A 1 567 ? 7.345 19.633 55.478 1.00 26.03 ? 567 LEU A CB 1 ATOM 4307 C CG . LEU A 1 567 ? 6.750 20.891 56.125 1.00 25.63 ? 567 LEU A CG 1 ATOM 4308 C CD1 . LEU A 1 567 ? 7.487 21.203 57.405 1.00 27.48 ? 567 LEU A CD1 1 ATOM 4309 C CD2 . LEU A 1 567 ? 6.828 22.074 55.185 1.00 24.15 ? 567 LEU A CD2 1 ATOM 4310 N N . PRO A 1 568 ? 8.508 18.459 52.450 1.00 25.51 ? 568 PRO A N 1 ATOM 4311 C CA . PRO A 1 568 ? 9.506 17.535 51.908 1.00 26.23 ? 568 PRO A CA 1 ATOM 4312 C C . PRO A 1 568 ? 10.877 17.724 52.578 1.00 27.28 ? 568 PRO A C 1 ATOM 4313 O O . PRO A 1 568 ? 11.855 17.059 52.200 1.00 27.22 ? 568 PRO A O 1 ATOM 4314 C CB . PRO A 1 568 ? 9.595 17.958 50.442 1.00 24.75 ? 568 PRO A CB 1 ATOM 4315 C CG . PRO A 1 568 ? 9.341 19.442 50.484 1.00 23.83 ? 568 PRO A CG 1 ATOM 4316 C CD . PRO A 1 568 ? 8.440 19.714 51.673 1.00 23.99 ? 568 PRO A CD 1 ATOM 4317 N N . ARG A 1 569 ? 10.920 18.650 53.543 1.00 27.40 ? 569 ARG A N 1 ATOM 4318 C CA . ARG A 1 569 ? 12.130 19.077 54.254 1.00 27.76 ? 569 ARG A CA 1 ATOM 4319 C C . ARG A 1 569 ? 11.745 19.267 55.710 1.00 27.83 ? 569 ARG A C 1 ATOM 4320 O O . ARG A 1 569 ? 10.590 19.566 56.015 1.00 27.64 ? 569 ARG A O 1 ATOM 4321 C CB . ARG A 1 569 ? 12.570 20.469 53.795 1.00 26.99 ? 569 ARG A CB 1 ATOM 4322 C CG . ARG A 1 569 ? 13.101 20.617 52.438 1.00 27.33 ? 569 ARG A CG 1 ATOM 4323 C CD . ARG A 1 569 ? 14.088 21.772 52.424 1.00 27.11 ? 569 ARG A CD 1 ATOM 4324 N NE . ARG A 1 569 ? 15.293 21.431 53.186 1.00 30.03 ? 569 ARG A NE 1 ATOM 4325 C CZ . ARG A 1 569 ? 16.225 20.565 52.785 1.00 29.52 ? 569 ARG A CZ 1 ATOM 4326 N NH1 . ARG A 1 569 ? 17.269 20.306 53.561 1.00 30.37 ? 569 ARG A NH1 1 ATOM 4327 N NH2 . ARG A 1 569 ? 16.114 19.951 51.615 1.00 28.47 ? 569 ARG A NH2 1 ATOM 4328 N N . THR A 1 570 ? 12.729 19.159 56.592 1.00 28.40 ? 570 THR A N 1 ATOM 4329 C CA . THR A 1 570 ? 12.590 19.528 58.001 1.00 28.33 ? 570 THR A CA 1 ATOM 4330 C C . THR A 1 570 ? 12.499 21.055 58.113 1.00 27.87 ? 570 THR A C 1 ATOM 4331 O O . THR A 1 570 ? 13.260 21.770 57.459 1.00 26.75 ? 570 THR A O 1 ATOM 4332 C CB . THR A 1 570 ? 13.816 19.031 58.807 1.00 29.32 ? 570 THR A CB 1 ATOM 4333 O OG1 . THR A 1 570 ? 13.805 17.602 58.846 1.00 30.45 ? 570 THR A OG1 1 ATOM 4334 C CG2 . THR A 1 570 ? 13.823 19.571 60.250 1.00 29.81 ? 570 THR A CG2 1 ATOM 4335 N N . TRP A 1 571 ? 11.567 21.553 58.928 1.00 28.01 ? 571 TRP A N 1 ATOM 4336 C CA . TRP A 1 571 ? 11.567 22.975 59.277 1.00 28.07 ? 571 TRP A CA 1 ATOM 4337 C C . TRP A 1 571 ? 12.250 23.158 60.623 1.00 29.61 ? 571 TRP A C 1 ATOM 4338 O O . TRP A 1 571 ? 11.783 22.641 61.648 1.00 30.52 ? 571 TRP A O 1 ATOM 4339 C CB . TRP A 1 571 ? 10.157 23.557 59.324 1.00 27.67 ? 571 TRP A CB 1 ATOM 4340 C CG . TRP A 1 571 ? 10.130 25.001 58.952 1.00 27.04 ? 571 TRP A CG 1 ATOM 4341 C CD1 . TRP A 1 571 ? 10.688 26.041 59.641 1.00 26.90 ? 571 TRP A CD1 1 ATOM 4342 C CD2 . TRP A 1 571 ? 9.527 25.568 57.780 1.00 26.33 ? 571 TRP A CD2 1 ATOM 4343 N NE1 . TRP A 1 571 ? 10.485 27.221 58.960 1.00 25.87 ? 571 TRP A NE1 1 ATOM 4344 C CE2 . TRP A 1 571 ? 9.757 26.964 57.826 1.00 25.41 ? 571 TRP A CE2 1 ATOM 4345 C CE3 . TRP A 1 571 ? 8.809 25.031 56.696 1.00 25.88 ? 571 TRP A CE3 1 ATOM 4346 C CZ2 . TRP A 1 571 ? 9.292 27.837 56.831 1.00 24.47 ? 571 TRP A CZ2 1 ATOM 4347 C CZ3 . TRP A 1 571 ? 8.349 25.902 55.700 1.00 24.05 ? 571 TRP A CZ3 1 ATOM 4348 C CH2 . TRP A 1 571 ? 8.595 27.289 55.776 1.00 23.93 ? 571 TRP A CH2 1 ATOM 4349 N N . PHE A 1 572 ? 13.351 23.903 60.612 1.00 29.66 ? 572 PHE A N 1 ATOM 4350 C CA . PHE A 1 572 ? 14.180 24.115 61.798 1.00 31.01 ? 572 PHE A CA 1 ATOM 4351 C C . PHE A 1 572 ? 13.610 25.189 62.750 1.00 31.20 ? 572 PHE A C 1 ATOM 4352 O O . PHE A 1 572 ? 12.904 26.101 62.324 1.00 30.03 ? 572 PHE A O 1 ATOM 4353 C CB . PHE A 1 572 ? 15.609 24.502 61.363 1.00 30.98 ? 572 PHE A CB 1 ATOM 4354 C CG . PHE A 1 572 ? 15.649 25.703 60.468 1.00 30.24 ? 572 PHE A CG 1 ATOM 4355 C CD1 . PHE A 1 572 ? 15.533 26.998 61.003 1.00 30.32 ? 572 PHE A CD1 1 ATOM 4356 C CD2 . PHE A 1 572 ? 15.760 25.550 59.078 1.00 27.93 ? 572 PHE A CD2 1 ATOM 4357 C CE1 . PHE A 1 572 ? 15.533 28.116 60.171 1.00 27.76 ? 572 PHE A CE1 1 ATOM 4358 C CE2 . PHE A 1 572 ? 15.766 26.664 58.239 1.00 26.06 ? 572 PHE A CE2 1 ATOM 4359 C CZ . PHE A 1 572 ? 15.649 27.948 58.785 1.00 26.41 ? 572 PHE A CZ 1 ATOM 4360 N N . LYS A 1 573 ? 13.935 25.071 64.038 1.00 33.01 ? 573 LYS A N 1 ATOM 4361 C CA . LYS A 1 573 ? 13.654 26.129 65.014 1.00 33.57 ? 573 LYS A CA 1 ATOM 4362 C C . LYS A 1 573 ? 14.621 27.316 64.859 1.00 33.90 ? 573 LYS A C 1 ATOM 4363 O O . LYS A 1 573 ? 14.212 28.480 64.940 1.00 33.49 ? 573 LYS A O 1 ATOM 4364 C CB . LYS A 1 573 ? 13.703 25.580 66.446 1.00 35.42 ? 573 LYS A CB 1 ATOM 4365 C CG . LYS A 1 573 ? 12.584 24.589 66.769 1.00 35.41 ? 573 LYS A CG 1 ATOM 4366 C CD . LYS A 1 573 ? 12.684 24.031 68.180 1.00 36.57 ? 573 LYS A CD 1 ATOM 4367 C CE . LYS A 1 573 ? 11.419 23.233 68.501 1.00 36.71 ? 573 LYS A CE 1 ATOM 4368 N NZ . LYS A 1 573 ? 11.435 22.622 69.862 1.00 40.76 ? 573 LYS A NZ 1 ATOM 4369 N N . SER A 1 574 ? 15.903 27.024 64.644 1.00 34.38 ? 574 SER A N 1 ATOM 4370 C CA . SER A 1 574 ? 16.877 28.081 64.386 1.00 34.59 ? 574 SER A CA 1 ATOM 4371 C C . SER A 1 574 ? 18.026 27.584 63.523 1.00 34.57 ? 574 SER A C 1 ATOM 4372 O O . SER A 1 574 ? 18.295 26.384 63.471 1.00 34.18 ? 574 SER A O 1 ATOM 4373 C CB . SER A 1 574 ? 17.423 28.646 65.705 1.00 36.62 ? 574 SER A CB 1 ATOM 4374 O OG . SER A 1 574 ? 18.133 27.657 66.403 1.00 38.94 ? 574 SER A OG 1 ATOM 4375 N N . VAL A 1 575 ? 18.715 28.514 62.863 1.00 34.26 ? 575 VAL A N 1 ATOM 4376 C CA . VAL A 1 575 ? 19.811 28.134 61.972 1.00 34.63 ? 575 VAL A CA 1 ATOM 4377 C C . VAL A 1 575 ? 20.995 27.490 62.688 1.00 36.55 ? 575 VAL A C 1 ATOM 4378 O O . VAL A 1 575 ? 21.725 26.713 62.086 1.00 36.87 ? 575 VAL A O 1 ATOM 4379 C CB . VAL A 1 575 ? 20.287 29.289 61.041 1.00 33.75 ? 575 VAL A CB 1 ATOM 4380 C CG1 . VAL A 1 575 ? 19.145 29.749 60.147 1.00 31.98 ? 575 VAL A CG1 1 ATOM 4381 C CG2 . VAL A 1 575 ? 20.880 30.447 61.839 1.00 34.71 ? 575 VAL A CG2 1 ATOM 4382 N N . ASP A 1 576 ? 21.192 27.793 63.967 1.00 38.56 ? 576 ASP A N 1 ATOM 4383 C CA . ASP A 1 576 ? 22.310 27.171 64.672 1.00 40.97 ? 576 ASP A CA 1 ATOM 4384 C C . ASP A 1 576 ? 22.094 25.677 64.984 1.00 40.89 ? 576 ASP A C 1 ATOM 4385 O O . ASP A 1 576 ? 23.010 24.989 65.404 1.00 41.76 ? 576 ASP A O 1 ATOM 4386 C CB . ASP A 1 576 ? 22.810 28.005 65.864 1.00 43.21 ? 576 ASP A CB 1 ATOM 4387 C CG . ASP A 1 576 ? 21.737 28.331 66.848 1.00 46.69 ? 576 ASP A CG 1 ATOM 4388 O OD1 . ASP A 1 576 ? 20.698 27.632 66.870 1.00 50.86 ? 576 ASP A OD1 1 ATOM 4389 O OD2 . ASP A 1 576 ? 21.935 29.296 67.626 1.00 51.87 ? 576 ASP A OD2 1 ATOM 4390 N N . GLN A 1 577 ? 20.895 25.174 64.709 1.00 39.33 ? 577 GLN A N 1 ATOM 4391 C CA . GLN A 1 577 ? 20.656 23.723 64.697 1.00 39.41 ? 577 GLN A CA 1 ATOM 4392 C C . GLN A 1 577 ? 21.257 23.011 63.471 1.00 38.78 ? 577 GLN A C 1 ATOM 4393 O O . GLN A 1 577 ? 21.442 21.800 63.492 1.00 39.53 ? 577 GLN A O 1 ATOM 4394 C CB . GLN A 1 577 ? 19.158 23.451 64.686 1.00 38.26 ? 577 GLN A CB 1 ATOM 4395 C CG . GLN A 1 577 ? 18.410 23.898 65.927 1.00 37.91 ? 577 GLN A CG 1 ATOM 4396 C CD . GLN A 1 577 ? 16.969 23.486 65.850 1.00 35.75 ? 577 GLN A CD 1 ATOM 4397 O OE1 . GLN A 1 577 ? 16.249 23.907 64.946 1.00 36.03 ? 577 GLN A OE1 1 ATOM 4398 N NE2 . GLN A 1 577 ? 16.537 22.633 66.777 1.00 35.17 ? 577 GLN A NE2 1 ATOM 4399 N N . LEU A 1 578 ? 21.531 23.757 62.402 1.00 37.38 ? 578 LEU A N 1 ATOM 4400 C CA . LEU A 1 578 ? 21.846 23.151 61.102 1.00 36.77 ? 578 LEU A CA 1 ATOM 4401 C C . LEU A 1 578 ? 23.303 22.666 60.991 1.00 38.33 ? 578 LEU A C 1 ATOM 4402 O O . LEU A 1 578 ? 24.207 23.294 61.553 1.00 38.87 ? 578 LEU A O 1 ATOM 4403 C CB . LEU A 1 578 ? 21.470 24.096 59.951 1.00 34.75 ? 578 LEU A CB 1 ATOM 4404 C CG . LEU A 1 578 ? 19.999 24.526 59.852 1.00 33.31 ? 578 LEU A CG 1 ATOM 4405 C CD1 . LEU A 1 578 ? 19.822 25.646 58.823 1.00 29.78 ? 578 LEU A CD1 1 ATOM 4406 C CD2 . LEU A 1 578 ? 19.029 23.349 59.588 1.00 30.92 ? 578 LEU A CD2 1 ATOM 4407 N N . PRO A 1 579 ? 23.537 21.548 60.267 1.00 38.80 ? 579 PRO A N 1 ATOM 4408 C CA . PRO A 1 579 ? 22.548 20.734 59.552 1.00 38.35 ? 579 PRO A CA 1 ATOM 4409 C C . PRO A 1 579 ? 21.739 19.843 60.500 1.00 39.55 ? 579 PRO A C 1 ATOM 4410 O O . PRO A 1 579 ? 22.262 19.400 61.515 1.00 41.33 ? 579 PRO A O 1 ATOM 4411 C CB . PRO A 1 579 ? 23.417 19.887 58.615 1.00 38.31 ? 579 PRO A CB 1 ATOM 4412 C CG . PRO A 1 579 ? 24.699 19.691 59.406 1.00 40.08 ? 579 PRO A CG 1 ATOM 4413 C CD . PRO A 1 579 ? 24.906 21.011 60.107 1.00 40.12 ? 579 PRO A CD 1 ATOM 4414 N N . MET A 1 580 ? 20.474 19.599 60.171 1.00 39.57 ? 580 MET A N 1 ATOM 4415 C CA . MET A 1 580 ? 19.589 18.782 61.001 1.00 41.34 ? 580 MET A CA 1 ATOM 4416 C C . MET A 1 580 ? 18.529 18.102 60.126 1.00 41.63 ? 580 MET A C 1 ATOM 4417 O O . MET A 1 580 ? 17.671 18.777 59.561 1.00 39.94 ? 580 MET A O 1 ATOM 4418 C CB . MET A 1 580 ? 18.928 19.663 62.078 1.00 41.76 ? 580 MET A CB 1 ATOM 4419 C CG . MET A 1 580 ? 18.042 18.913 63.086 1.00 42.24 ? 580 MET A CG 1 ATOM 4420 S SD . MET A 1 580 ? 17.289 20.009 64.311 1.00 40.83 ? 580 MET A SD 1 ATOM 4421 C CE . MET A 1 580 ? 16.050 20.867 63.318 1.00 37.32 ? 580 MET A CE 1 ATOM 4422 N N . ASN A 1 581 ? 18.598 16.771 60.007 1.00 44.31 ? 581 ASN A N 1 ATOM 4423 C CA . ASN A 1 581 ? 17.677 16.024 59.119 1.00 45.23 ? 581 ASN A CA 1 ATOM 4424 C C . ASN A 1 581 ? 16.939 14.880 59.829 1.00 47.81 ? 581 ASN A C 1 ATOM 4425 O O . ASN A 1 581 ? 17.441 14.340 60.819 1.00 48.98 ? 581 ASN A O 1 ATOM 4426 C CB . ASN A 1 581 ? 18.418 15.470 57.882 1.00 44.88 ? 581 ASN A CB 1 ATOM 4427 C CG . ASN A 1 581 ? 19.137 16.544 57.090 1.00 42.06 ? 581 ASN A CG 1 ATOM 4428 O OD1 . ASN A 1 581 ? 20.322 16.813 57.319 1.00 41.47 ? 581 ASN A OD1 1 ATOM 4429 N ND2 . ASN A 1 581 ? 18.429 17.169 56.158 1.00 40.58 ? 581 ASN A ND2 1 ATOM 4430 N N . VAL A 1 582 ? 15.753 14.521 59.313 1.00 49.24 ? 582 VAL A N 1 ATOM 4431 C CA . VAL A 1 582 ? 14.969 13.378 59.849 1.00 52.19 ? 582 VAL A CA 1 ATOM 4432 C C . VAL A 1 582 ? 15.853 12.160 59.986 1.00 54.51 ? 582 VAL A C 1 ATOM 4433 O O . VAL A 1 582 ? 16.450 11.715 59.006 1.00 54.96 ? 582 VAL A O 1 ATOM 4434 C CB . VAL A 1 582 ? 13.732 12.966 58.973 1.00 51.43 ? 582 VAL A CB 1 ATOM 4435 C CG1 . VAL A 1 582 ? 12.438 13.489 59.558 1.00 52.08 ? 582 VAL A CG1 1 ATOM 4436 C CG2 . VAL A 1 582 ? 13.899 13.353 57.497 1.00 50.59 ? 582 VAL A CG2 1 ATOM 4437 N N . GLY A 1 583 ? 15.951 11.630 61.197 1.00 57.06 ? 583 GLY A N 1 ATOM 4438 C CA . GLY A 1 583 ? 16.816 10.491 61.454 1.00 59.79 ? 583 GLY A CA 1 ATOM 4439 C C . GLY A 1 583 ? 18.041 10.843 62.273 1.00 61.70 ? 583 GLY A C 1 ATOM 4440 O O . GLY A 1 583 ? 18.703 9.950 62.804 1.00 63.66 ? 583 GLY A O 1 ATOM 4441 N N . ASP A 1 584 ? 18.349 12.137 62.376 1.00 61.26 ? 584 ASP A N 1 ATOM 4442 C CA . ASP A 1 584 ? 19.530 12.609 63.125 1.00 62.73 ? 584 ASP A CA 1 ATOM 4443 C C . ASP A 1 584 ? 19.428 12.313 64.609 1.00 64.42 ? 584 ASP A C 1 ATOM 4444 O O . ASP A 1 584 ? 18.326 12.128 65.136 1.00 64.85 ? 584 ASP A O 1 ATOM 4445 C CB . ASP A 1 584 ? 19.726 14.120 62.938 1.00 61.91 ? 584 ASP A CB 1 ATOM 4446 C CG . ASP A 1 584 ? 20.541 14.468 61.694 1.00 61.61 ? 584 ASP A CG 1 ATOM 4447 O OD1 . ASP A 1 584 ? 20.769 13.578 60.832 1.00 62.32 ? 584 ASP A OD1 1 ATOM 4448 O OD2 . ASP A 1 584 ? 20.952 15.648 61.592 1.00 61.17 ? 584 ASP A OD2 1 ATOM 4449 N N . ALA A 1 585 ? 20.575 12.299 65.284 1.00 65.40 ? 585 ALA A N 1 ATOM 4450 C CA . ALA A 1 585 ? 20.609 12.089 66.730 1.00 66.81 ? 585 ALA A CA 1 ATOM 4451 C C . ALA A 1 585 ? 19.921 13.210 67.518 1.00 65.71 ? 585 ALA A C 1 ATOM 4452 O O . ALA A 1 585 ? 19.264 12.942 68.538 1.00 66.95 ? 585 ALA A O 1 ATOM 4453 C CB . ALA A 1 585 ? 22.044 11.887 67.223 1.00 68.71 ? 585 ALA A CB 1 ATOM 4454 N N . HIS A 1 586 ? 20.066 14.457 67.061 1.00 62.73 ? 586 HIS A N 1 ATOM 4455 C CA . HIS A 1 586 ? 19.537 15.593 67.837 1.00 61.37 ? 586 HIS A CA 1 ATOM 4456 C C . HIS A 1 586 ? 18.474 16.412 67.109 1.00 57.49 ? 586 HIS A C 1 ATOM 4457 O O . HIS A 1 586 ? 18.373 17.643 67.264 1.00 56.68 ? 586 HIS A O 1 ATOM 4458 C CB . HIS A 1 586 ? 20.664 16.442 68.441 1.00 62.75 ? 586 HIS A CB 1 ATOM 4459 C CG . HIS A 1 586 ? 21.236 15.852 69.697 1.00 67.50 ? 586 HIS A CG 1 ATOM 4460 N ND1 . HIS A 1 586 ? 20.688 16.079 70.944 1.00 70.79 ? 586 HIS A ND1 1 ATOM 4461 C CD2 . HIS A 1 586 ? 22.287 15.017 69.896 1.00 70.96 ? 586 HIS A CD2 1 ATOM 4462 C CE1 . HIS A 1 586 ? 21.384 15.423 71.858 1.00 73.76 ? 586 HIS A CE1 1 ATOM 4463 N NE2 . HIS A 1 586 ? 22.360 14.771 71.248 1.00 74.63 ? 586 HIS A NE2 1 ATOM 4464 N N . TYR A 1 587 ? 17.684 15.674 66.327 1.00 54.32 ? 587 TYR A N 1 ATOM 4465 C CA . TYR A 1 587 ? 16.474 16.132 65.674 1.00 49.75 ? 587 TYR A CA 1 ATOM 4466 C C . TYR A 1 587 ? 15.487 16.838 66.614 1.00 48.46 ? 587 TYR A C 1 ATOM 4467 O O . TYR A 1 587 ? 14.880 16.215 67.487 1.00 49.82 ? 587 TYR A O 1 ATOM 4468 C CB . TYR A 1 587 ? 15.787 14.933 65.012 1.00 49.30 ? 587 TYR A CB 1 ATOM 4469 C CG . TYR A 1 587 ? 14.879 15.310 63.867 1.00 46.29 ? 587 TYR A CG 1 ATOM 4470 C CD1 . TYR A 1 587 ? 15.355 16.092 62.817 1.00 43.86 ? 587 TYR A CD1 1 ATOM 4471 C CD2 . TYR A 1 587 ? 13.553 14.883 63.829 1.00 44.86 ? 587 TYR A CD2 1 ATOM 4472 C CE1 . TYR A 1 587 ? 14.533 16.450 61.757 1.00 42.67 ? 587 TYR A CE1 1 ATOM 4473 C CE2 . TYR A 1 587 ? 12.711 15.238 62.767 1.00 43.82 ? 587 TYR A CE2 1 ATOM 4474 C CZ . TYR A 1 587 ? 13.212 16.021 61.728 1.00 42.75 ? 587 TYR A CZ 1 ATOM 4475 O OH . TYR A 1 587 ? 12.408 16.383 60.657 1.00 40.95 ? 587 TYR A OH 1 ATOM 4476 N N . ASP A 1 588 ? 15.326 18.143 66.416 1.00 45.25 ? 588 ASP A N 1 ATOM 4477 C CA . ASP A 1 588 ? 14.395 18.940 67.200 1.00 43.38 ? 588 ASP A CA 1 ATOM 4478 C C . ASP A 1 588 ? 13.767 20.002 66.290 1.00 40.26 ? 588 ASP A C 1 ATOM 4479 O O . ASP A 1 588 ? 14.111 21.182 66.367 1.00 38.81 ? 588 ASP A O 1 ATOM 4480 C CB . ASP A 1 588 ? 15.113 19.553 68.412 1.00 44.75 ? 588 ASP A CB 1 ATOM 4481 C CG . ASP A 1 588 ? 14.184 20.360 69.314 1.00 44.86 ? 588 ASP A CG 1 ATOM 4482 O OD1 . ASP A 1 588 ? 12.967 20.086 69.355 1.00 44.16 ? 588 ASP A OD1 1 ATOM 4483 O OD2 . ASP A 1 588 ? 14.684 21.282 69.987 1.00 45.56 ? 588 ASP A OD2 1 ATOM 4484 N N . PRO A 1 589 ? 12.844 19.568 65.409 1.00 38.63 ? 589 PRO A N 1 ATOM 4485 C CA . PRO A 1 589 ? 12.286 20.454 64.389 1.00 36.36 ? 589 PRO A CA 1 ATOM 4486 C C . PRO A 1 589 ? 11.164 21.333 64.921 1.00 35.55 ? 589 PRO A C 1 ATOM 4487 O O . PRO A 1 589 ? 10.508 20.975 65.903 1.00 36.49 ? 589 PRO A O 1 ATOM 4488 C CB . PRO A 1 589 ? 11.711 19.473 63.372 1.00 35.63 ? 589 PRO A CB 1 ATOM 4489 C CG . PRO A 1 589 ? 11.257 18.318 64.205 1.00 37.46 ? 589 PRO A CG 1 ATOM 4490 C CD . PRO A 1 589 ? 12.277 18.201 65.320 1.00 39.22 ? 589 PRO A CD 1 ATOM 4491 N N . LEU A 1 590 ? 10.949 22.476 64.278 1.00 33.66 ? 590 LEU A N 1 ATOM 4492 C CA . LEU A 1 590 ? 9.711 23.225 64.474 1.00 32.86 ? 590 LEU A CA 1 ATOM 4493 C C . LEU A 1 590 ? 8.565 22.422 63.845 1.00 32.89 ? 590 LEU A C 1 ATOM 4494 O O . LEU A 1 590 ? 7.515 22.233 64.477 1.00 33.34 ? 590 LEU A O 1 ATOM 4495 C CB . LEU A 1 590 ? 9.799 24.618 63.850 1.00 31.39 ? 590 LEU A CB 1 ATOM 4496 C CG . LEU A 1 590 ? 8.651 25.592 64.135 1.00 31.37 ? 590 LEU A CG 1 ATOM 4497 C CD1 . LEU A 1 590 ? 8.532 25.899 65.619 1.00 32.19 ? 590 LEU A CD1 1 ATOM 4498 C CD2 . LEU A 1 590 ? 8.867 26.858 63.340 1.00 30.15 ? 590 LEU A CD2 1 ATOM 4499 N N . PHE A 1 591 ? 8.776 21.954 62.609 1.00 31.86 ? 591 PHE A N 1 ATOM 4500 C CA . PHE A 1 591 ? 7.863 21.028 61.927 1.00 31.82 ? 591 PHE A CA 1 ATOM 4501 C C . PHE A 1 591 ? 8.683 19.895 61.312 1.00 32.83 ? 591 PHE A C 1 ATOM 4502 O O . PHE A 1 591 ? 9.654 20.144 60.575 1.00 31.99 ? 591 PHE A O 1 ATOM 4503 C CB . PHE A 1 591 ? 7.051 21.726 60.820 1.00 30.16 ? 591 PHE A CB 1 ATOM 4504 C CG . PHE A 1 591 ? 6.267 22.935 61.281 1.00 29.63 ? 591 PHE A CG 1 ATOM 4505 C CD1 . PHE A 1 591 ? 6.705 24.220 60.972 1.00 27.73 ? 591 PHE A CD1 1 ATOM 4506 C CD2 . PHE A 1 591 ? 5.094 22.788 62.022 1.00 29.91 ? 591 PHE A CD2 1 ATOM 4507 C CE1 . PHE A 1 591 ? 5.986 25.338 61.400 1.00 27.76 ? 591 PHE A CE1 1 ATOM 4508 C CE2 . PHE A 1 591 ? 4.371 23.899 62.455 1.00 29.80 ? 591 PHE A CE2 1 ATOM 4509 C CZ . PHE A 1 591 ? 4.814 25.176 62.132 1.00 28.62 ? 591 PHE A CZ 1 ATOM 4510 N N . ARG A 1 592 ? 8.304 18.653 61.608 1.00 34.56 ? 592 ARG A N 1 ATOM 4511 C CA . ARG A 1 592 ? 9.010 17.481 61.065 1.00 36.31 ? 592 ARG A CA 1 ATOM 4512 C C . ARG A 1 592 ? 8.735 17.319 59.565 1.00 34.17 ? 592 ARG A C 1 ATOM 4513 O O . ARG A 1 592 ? 7.720 17.812 59.055 1.00 31.91 ? 592 ARG A O 1 ATOM 4514 C CB . ARG A 1 592 ? 8.626 16.197 61.818 1.00 37.80 ? 592 ARG A CB 1 ATOM 4515 C CG . ARG A 1 592 ? 7.131 16.005 61.996 1.00 40.90 ? 592 ARG A CG 1 ATOM 4516 C CD . ARG A 1 592 ? 6.722 14.527 62.227 1.00 43.26 ? 592 ARG A CD 1 ATOM 4517 N NE . ARG A 1 592 ? 6.324 13.899 60.950 1.00 51.88 ? 592 ARG A NE 1 ATOM 4518 C CZ . ARG A 1 592 ? 5.108 13.987 60.389 1.00 52.82 ? 592 ARG A CZ 1 ATOM 4519 N NH1 . ARG A 1 592 ? 4.117 14.671 60.983 1.00 52.51 ? 592 ARG A NH1 1 ATOM 4520 N NH2 . ARG A 1 592 ? 4.876 13.372 59.229 1.00 51.67 ? 592 ARG A NH2 1 ATOM 4521 N N . LEU A 1 593 ? 9.639 16.631 58.865 1.00 34.04 ? 593 LEU A N 1 ATOM 4522 C CA . LEU A 1 593 ? 9.380 16.221 57.486 1.00 33.03 ? 593 LEU A CA 1 ATOM 4523 C C . LEU A 1 593 ? 8.049 15.457 57.459 1.00 33.17 ? 593 LEU A C 1 ATOM 4524 O O . LEU A 1 593 ? 7.802 14.598 58.320 1.00 34.13 ? 593 LEU A O 1 ATOM 4525 C CB . LEU A 1 593 ? 10.522 15.338 56.942 1.00 33.74 ? 593 LEU A CB 1 ATOM 4526 C CG . LEU A 1 593 ? 10.449 14.989 55.440 1.00 34.35 ? 593 LEU A CG 1 ATOM 4527 C CD1 . LEU A 1 593 ? 11.813 15.017 54.811 1.00 35.04 ? 593 LEU A CD1 1 ATOM 4528 C CD2 . LEU A 1 593 ? 9.771 13.635 55.163 1.00 35.94 ? 593 LEU A CD2 1 ATOM 4529 N N . GLY A 1 594 ? 7.191 15.790 56.494 1.00 31.58 ? 594 GLY A N 1 ATOM 4530 C CA . GLY A 1 594 ? 5.903 15.119 56.357 1.00 31.74 ? 594 GLY A CA 1 ATOM 4531 C C . GLY A 1 594 ? 4.747 15.856 57.012 1.00 31.59 ? 594 GLY A C 1 ATOM 4532 O O . GLY A 1 594 ? 3.596 15.489 56.812 1.00 31.46 ? 594 GLY A O 1 ATOM 4533 N N . TYR A 1 595 ? 5.045 16.902 57.780 1.00 31.39 ? 595 TYR A N 1 ATOM 4534 C CA . TYR A 1 595 ? 4.000 17.716 58.416 1.00 31.42 ? 595 TYR A CA 1 ATOM 4535 C C . TYR A 1 595 ? 3.203 18.512 57.392 1.00 30.09 ? 595 TYR A C 1 ATOM 4536 O O . TYR A 1 595 ? 3.760 19.096 56.462 1.00 29.10 ? 595 TYR A O 1 ATOM 4537 C CB . TYR A 1 595 ? 4.606 18.667 59.459 1.00 31.93 ? 595 TYR A CB 1 ATOM 4538 C CG . TYR A 1 595 ? 3.613 19.606 60.113 1.00 32.02 ? 595 TYR A CG 1 ATOM 4539 C CD1 . TYR A 1 595 ? 2.953 19.253 61.301 1.00 34.50 ? 595 TYR A CD1 1 ATOM 4540 C CD2 . TYR A 1 595 ? 3.334 20.857 59.551 1.00 32.01 ? 595 TYR A CD2 1 ATOM 4541 C CE1 . TYR A 1 595 ? 2.020 20.131 61.902 1.00 33.91 ? 595 TYR A CE1 1 ATOM 4542 C CE2 . TYR A 1 595 ? 2.416 21.730 60.138 1.00 31.40 ? 595 TYR A CE2 1 ATOM 4543 C CZ . TYR A 1 595 ? 1.767 21.362 61.306 1.00 33.12 ? 595 TYR A CZ 1 ATOM 4544 O OH . TYR A 1 595 ? 0.872 22.246 61.883 1.00 35.06 ? 595 TYR A OH 1 ATOM 4545 N N . GLY A 1 596 ? 1.890 18.557 57.575 1.00 30.34 ? 596 GLY A N 1 ATOM 4546 C CA . GLY A 1 596 ? 1.050 19.429 56.735 1.00 29.29 ? 596 GLY A CA 1 ATOM 4547 C C . GLY A 1 596 ? -0.363 19.378 57.264 1.00 29.67 ? 596 GLY A C 1 ATOM 4548 O O . GLY A 1 596 ? -0.905 18.300 57.455 1.00 30.98 ? 596 GLY A O 1 ATOM 4549 N N . LEU A 1 597 ? -0.950 20.537 57.531 1.00 29.08 ? 597 LEU A N 1 ATOM 4550 C CA . LEU A 1 597 ? -2.366 20.597 57.906 1.00 29.33 ? 597 LEU A CA 1 ATOM 4551 C C . LEU A 1 597 ? -3.222 20.418 56.653 1.00 29.64 ? 597 LEU A C 1 ATOM 4552 O O . LEU A 1 597 ? -2.772 20.706 55.530 1.00 27.54 ? 597 LEU A O 1 ATOM 4553 C CB . LEU A 1 597 ? -2.695 21.920 58.610 1.00 28.73 ? 597 LEU A CB 1 ATOM 4554 C CG . LEU A 1 597 ? -1.970 22.177 59.938 1.00 28.66 ? 597 LEU A CG 1 ATOM 4555 C CD1 . LEU A 1 597 ? -2.364 23.525 60.513 1.00 27.94 ? 597 LEU A CD1 1 ATOM 4556 C CD2 . LEU A 1 597 ? -2.204 21.066 60.968 1.00 29.94 ? 597 LEU A CD2 1 ATOM 4557 N N . THR A 1 598 ? -4.441 19.920 56.828 1.00 30.72 ? 598 THR A N 1 ATOM 4558 C CA . THR A 1 598 ? -5.324 19.723 55.675 1.00 32.02 ? 598 THR A CA 1 ATOM 4559 C C . THR A 1 598 ? -6.583 20.581 55.779 1.00 32.34 ? 598 THR A C 1 ATOM 4560 O O . THR A 1 598 ? -6.975 20.991 56.869 1.00 32.21 ? 598 THR A O 1 ATOM 4561 C CB . THR A 1 598 ? -5.705 18.228 55.479 1.00 33.00 ? 598 THR A CB 1 ATOM 4562 O OG1 . THR A 1 598 ? -6.524 17.790 56.567 1.00 34.53 ? 598 THR A OG1 1 ATOM 4563 C CG2 . THR A 1 598 ? -4.447 17.343 55.402 1.00 33.44 ? 598 THR A CG2 1 ATOM 4564 N N . THR A 1 599 ? -7.177 20.892 54.633 1.00 32.74 ? 599 THR A N 1 ATOM 4565 C CA . THR A 1 599 ? -8.546 21.397 54.610 1.00 34.09 ? 599 THR A CA 1 ATOM 4566 C C . THR A 1 599 ? -9.353 20.526 53.659 1.00 35.77 ? 599 THR A C 1 ATOM 4567 O O . THR A 1 599 ? -8.798 19.686 52.950 1.00 35.80 ? 599 THR A O 1 ATOM 4568 C CB . THR A 1 599 ? -8.652 22.875 54.155 1.00 33.04 ? 599 THR A CB 1 ATOM 4569 O OG1 . THR A 1 599 ? -8.125 23.018 52.823 1.00 32.23 ? 599 THR A OG1 1 ATOM 4570 C CG2 . THR A 1 599 ? -7.936 23.822 55.125 1.00 31.63 ? 599 THR A CG2 1 ATOM 4571 N N . ASN A 1 600 ? -10.667 20.721 53.659 1.00 37.80 ? 600 ASN A N 1 ATOM 4572 C CA . ASN A 1 600 ? -11.528 20.103 52.656 1.00 40.20 ? 600 ASN A CA 1 ATOM 4573 C C . ASN A 1 600 ? -12.151 21.167 51.738 1.00 40.10 ? 600 ASN A C 1 ATOM 4574 O O . ASN A 1 600 ? -12.381 22.310 52.163 1.00 39.23 ? 600 ASN A O 1 ATOM 4575 C CB . ASN A 1 600 ? -12.598 19.218 53.319 1.00 41.75 ? 600 ASN A CB 1 ATOM 4576 C CG . ASN A 1 600 ? -12.015 17.930 53.912 1.00 44.79 ? 600 ASN A CG 1 ATOM 4577 O OD1 . ASN A 1 600 ? -12.164 17.675 55.104 1.00 46.36 ? 600 ASN A OD1 1 ATOM 4578 N ND2 . ASN A 1 600 ? -11.348 17.119 53.069 1.00 48.20 ? 600 ASN A ND2 1 ATOM 4579 N N . ALA A 1 601 ? -12.397 20.781 50.486 1.00 41.00 ? 601 ALA A N 1 ATOM 4580 C CA . ALA A 1 601 ? -13.038 21.643 49.488 1.00 41.74 ? 601 ALA A CA 1 ATOM 4581 C C . ALA A 1 601 ? -14.427 22.134 49.946 1.00 43.03 ? 601 ALA A C 1 ATOM 4582 O O . ALA A 1 601 ? -15.228 21.343 50.453 1.00 44.36 ? 601 ALA A O 1 ATOM 4583 C CB . ALA A 1 601 ? -13.133 20.905 48.144 1.00 41.62 ? 601 ALA A CB 1 ATOM 4584 N N . THR A 1 602 ? -14.687 23.438 49.800 1.00 43.36 ? 602 THR A N 1 ATOM 4585 C CA . THR A 1 602 ? -16.023 24.010 50.072 1.00 44.97 ? 602 THR A CA 1 ATOM 4586 C C . THR A 1 602 ? -16.818 24.193 48.797 1.00 45.55 ? 602 THR A C 1 ATOM 4587 O O . THR A 1 602 ? -16.800 23.330 47.920 1.00 46.91 ? 602 THR A O 1 ATOM 4588 C CB . THR A 1 602 ? -15.983 25.373 50.817 1.00 44.56 ? 602 THR A CB 1 ATOM 4589 O OG1 . THR A 1 602 ? -14.926 26.195 50.310 1.00 43.52 ? 602 THR A OG1 1 ATOM 4590 C CG2 . THR A 1 602 ? -15.784 25.174 52.333 1.00 46.33 ? 602 THR A CG2 1 HETATM 4591 C C1 . NAG B 2 . ? 34.750 25.780 50.538 1.00 47.05 ? 701 NAG A C1 1 HETATM 4592 C C2 . NAG B 2 . ? 35.993 25.637 49.636 1.00 48.73 ? 701 NAG A C2 1 HETATM 4593 C C3 . NAG B 2 . ? 37.204 26.372 50.223 1.00 51.67 ? 701 NAG A C3 1 HETATM 4594 C C4 . NAG B 2 . ? 36.848 27.813 50.586 1.00 53.52 ? 701 NAG A C4 1 HETATM 4595 C C5 . NAG B 2 . ? 35.646 27.784 51.544 1.00 51.59 ? 701 NAG A C5 1 HETATM 4596 C C6 . NAG B 2 . ? 35.170 29.166 51.981 1.00 51.03 ? 701 NAG A C6 1 HETATM 4597 C C7 . NAG B 2 . ? 36.000 23.570 48.318 1.00 46.77 ? 701 NAG A C7 1 HETATM 4598 C C8 . NAG B 2 . ? 36.337 22.108 48.283 1.00 45.91 ? 701 NAG A C8 1 HETATM 4599 N N2 . NAG B 2 . ? 36.317 24.236 49.433 1.00 46.90 ? 701 NAG A N2 1 HETATM 4600 O O3 . NAG B 2 . ? 38.307 26.340 49.341 1.00 52.27 ? 701 NAG A O3 1 HETATM 4601 O O4 . NAG B 2 . ? 37.971 28.422 51.185 1.00 58.78 ? 701 NAG A O4 1 HETATM 4602 O O5 . NAG B 2 . ? 34.558 27.133 50.917 1.00 48.60 ? 701 NAG A O5 1 HETATM 4603 O O6 . NAG B 2 . ? 34.868 29.946 50.841 1.00 51.27 ? 701 NAG A O6 1 HETATM 4604 O O7 . NAG B 2 . ? 35.458 24.095 47.343 1.00 46.50 ? 701 NAG A O7 1 HETATM 4605 C C1 . NAG C 2 . ? 38.320 29.672 50.557 1.00 64.43 ? 702 NAG A C1 1 HETATM 4606 C C2 . NAG C 2 . ? 39.064 30.521 51.594 1.00 67.14 ? 702 NAG A C2 1 HETATM 4607 C C3 . NAG C 2 . ? 39.592 31.829 51.007 1.00 69.20 ? 702 NAG A C3 1 HETATM 4608 C C4 . NAG C 2 . ? 40.277 31.633 49.651 1.00 71.12 ? 702 NAG A C4 1 HETATM 4609 C C5 . NAG C 2 . ? 39.498 30.684 48.721 1.00 69.71 ? 702 NAG A C5 1 HETATM 4610 C C6 . NAG C 2 . ? 40.358 30.283 47.522 1.00 70.12 ? 702 NAG A C6 1 HETATM 4611 C C7 . NAG C 2 . ? 38.528 30.459 53.976 1.00 67.11 ? 702 NAG A C7 1 HETATM 4612 C C8 . NAG C 2 . ? 38.776 31.599 54.925 1.00 67.74 ? 702 NAG A C8 1 HETATM 4613 N N2 . NAG C 2 . ? 38.200 30.802 52.730 1.00 67.28 ? 702 NAG A N2 1 HETATM 4614 O O3 . NAG C 2 . ? 40.508 32.411 51.911 1.00 69.34 ? 702 NAG A O3 1 HETATM 4615 O O4 . NAG C 2 . ? 40.444 32.909 49.050 1.00 74.86 ? 702 NAG A O4 1 HETATM 4616 O O5 . NAG C 2 . ? 39.105 29.495 49.391 1.00 67.09 ? 702 NAG A O5 1 HETATM 4617 O O6 . NAG C 2 . ? 39.553 29.814 46.464 1.00 70.77 ? 702 NAG A O6 1 HETATM 4618 O O7 . NAG C 2 . ? 38.628 29.289 54.354 1.00 66.53 ? 702 NAG A O7 1 HETATM 4619 C C1 . BMA D 3 . ? 41.845 33.189 48.809 1.00 77.58 ? 703 BMA A C1 1 HETATM 4620 C C2 . BMA D 3 . ? 41.976 34.308 47.765 1.00 78.35 ? 703 BMA A C2 1 HETATM 4621 C C3 . BMA D 3 . ? 43.450 34.660 47.502 1.00 79.02 ? 703 BMA A C3 1 HETATM 4622 C C4 . BMA D 3 . ? 44.284 34.746 48.790 1.00 79.89 ? 703 BMA A C4 1 HETATM 4623 C C5 . BMA D 3 . ? 43.998 33.555 49.731 1.00 79.98 ? 703 BMA A C5 1 HETATM 4624 C C6 . BMA D 3 . ? 44.774 33.566 51.059 1.00 80.49 ? 703 BMA A C6 1 HETATM 4625 O O2 . BMA D 3 . ? 41.235 35.441 48.169 1.00 78.56 ? 703 BMA A O2 1 HETATM 4626 O O3 . BMA D 3 . ? 43.543 35.865 46.769 1.00 78.09 ? 703 BMA A O3 1 HETATM 4627 O O4 . BMA D 3 . ? 45.654 34.794 48.447 1.00 80.82 ? 703 BMA A O4 1 HETATM 4628 O O5 . BMA D 3 . ? 42.600 33.474 49.983 1.00 78.89 ? 703 BMA A O5 1 HETATM 4629 O O6 . BMA D 3 . ? 45.014 34.876 51.545 1.00 80.85 ? 703 BMA A O6 1 HETATM 4630 C C1 . NAG E 2 . ? 21.313 37.000 55.851 1.00 59.52 ? 704 NAG A C1 1 HETATM 4631 C C2 . NAG E 2 . ? 21.088 38.529 55.812 1.00 65.69 ? 704 NAG A C2 1 HETATM 4632 C C3 . NAG E 2 . ? 20.773 39.101 54.413 1.00 67.63 ? 704 NAG A C3 1 HETATM 4633 C C4 . NAG E 2 . ? 21.555 38.461 53.252 1.00 69.23 ? 704 NAG A C4 1 HETATM 4634 C C5 . NAG E 2 . ? 21.717 36.943 53.465 1.00 66.65 ? 704 NAG A C5 1 HETATM 4635 C C6 . NAG E 2 . ? 22.662 36.304 52.438 1.00 66.35 ? 704 NAG A C6 1 HETATM 4636 C C7 . NAG E 2 . ? 20.374 39.420 57.984 1.00 67.76 ? 704 NAG A C7 1 HETATM 4637 C C8 . NAG E 2 . ? 19.395 39.166 59.099 1.00 67.45 ? 704 NAG A C8 1 HETATM 4638 N N2 . NAG E 2 . ? 20.062 38.947 56.769 1.00 66.35 ? 704 NAG A N2 1 HETATM 4639 O O3 . NAG E 2 . ? 21.038 40.491 54.418 1.00 68.22 ? 704 NAG A O3 1 HETATM 4640 O O4 . NAG E 2 . ? 20.904 38.769 52.014 1.00 74.46 ? 704 NAG A O4 1 HETATM 4641 O O5 . NAG E 2 . ? 22.180 36.637 54.782 1.00 63.02 ? 704 NAG A O5 1 HETATM 4642 O O6 . NAG E 2 . ? 23.996 36.736 52.609 1.00 66.19 ? 704 NAG A O6 1 HETATM 4643 O O7 . NAG E 2 . ? 21.419 40.035 58.218 1.00 68.97 ? 704 NAG A O7 1 HETATM 4644 C C1 . NAG F 2 . ? 21.765 39.433 51.029 1.00 79.48 ? 705 NAG A C1 1 HETATM 4645 C C2 . NAG F 2 . ? 21.006 39.840 49.739 1.00 81.47 ? 705 NAG A C2 1 HETATM 4646 C C3 . NAG F 2 . ? 21.984 40.442 48.706 1.00 82.68 ? 705 NAG A C3 1 HETATM 4647 C C4 . NAG F 2 . ? 22.798 41.589 49.328 1.00 83.68 ? 705 NAG A C4 1 HETATM 4648 C C5 . NAG F 2 . ? 23.476 41.059 50.607 1.00 83.06 ? 705 NAG A C5 1 HETATM 4649 C C6 . NAG F 2 . ? 24.379 42.075 51.314 1.00 83.52 ? 705 NAG A C6 1 HETATM 4650 C C7 . NAG F 2 . ? 20.386 37.808 48.320 1.00 83.19 ? 705 NAG A C7 1 HETATM 4651 C C8 . NAG F 2 . ? 19.188 36.984 47.918 1.00 82.54 ? 705 NAG A C8 1 HETATM 4652 N N2 . NAG F 2 . ? 20.125 38.784 49.210 1.00 82.33 ? 705 NAG A N2 1 HETATM 4653 O O3 . NAG F 2 . ? 21.316 40.867 47.534 1.00 82.13 ? 705 NAG A O3 1 HETATM 4654 O O4 . NAG F 2 . ? 23.743 42.083 48.390 1.00 85.66 ? 705 NAG A O4 1 HETATM 4655 O O5 . NAG F 2 . ? 22.490 40.566 51.513 1.00 81.25 ? 705 NAG A O5 1 HETATM 4656 O O6 . NAG F 2 . ? 23.614 43.161 51.794 1.00 83.88 ? 705 NAG A O6 1 HETATM 4657 O O7 . NAG F 2 . ? 21.501 37.554 47.836 1.00 83.55 ? 705 NAG A O7 1 HETATM 4658 C C1 . BMA G 3 . ? 23.458 43.439 47.960 1.00 87.21 ? 706 BMA A C1 1 HETATM 4659 C C2 . BMA G 3 . ? 24.765 44.087 47.480 1.00 87.99 ? 706 BMA A C2 1 HETATM 4660 C C3 . BMA G 3 . ? 24.526 45.514 46.959 1.00 88.44 ? 706 BMA A C3 1 HETATM 4661 C C4 . BMA G 3 . ? 23.357 45.566 45.969 1.00 88.58 ? 706 BMA A C4 1 HETATM 4662 C C5 . BMA G 3 . ? 22.118 44.851 46.534 1.00 88.31 ? 706 BMA A C5 1 HETATM 4663 C C6 . BMA G 3 . ? 20.997 44.796 45.489 1.00 88.18 ? 706 BMA A C6 1 HETATM 4664 O O2 . BMA G 3 . ? 25.365 43.282 46.481 1.00 87.81 ? 706 BMA A O2 1 HETATM 4665 O O3 . BMA G 3 . ? 25.696 46.053 46.368 1.00 88.40 ? 706 BMA A O3 1 HETATM 4666 O O4 . BMA G 3 . ? 23.069 46.916 45.664 1.00 88.89 ? 706 BMA A O4 1 HETATM 4667 O O5 . BMA G 3 . ? 22.454 43.530 46.953 1.00 87.83 ? 706 BMA A O5 1 HETATM 4668 O O6 . BMA G 3 . ? 19.707 44.673 46.069 1.00 88.09 ? 706 BMA A O6 1 HETATM 4669 C C1 . BMA H 3 . ? 19.287 43.290 45.974 1.00 87.57 ? 707 BMA A C1 1 HETATM 4670 C C2 . BMA H 3 . ? 18.093 42.913 46.863 1.00 86.85 ? 707 BMA A C2 1 HETATM 4671 C C3 . BMA H 3 . ? 18.177 41.383 46.953 1.00 86.10 ? 707 BMA A C3 1 HETATM 4672 C C4 . BMA H 3 . ? 18.114 40.746 45.554 1.00 86.08 ? 707 BMA A C4 1 HETATM 4673 C C5 . BMA H 3 . ? 19.155 41.379 44.607 1.00 86.59 ? 707 BMA A C5 1 HETATM 4674 C C6 . BMA H 3 . ? 19.021 40.936 43.152 1.00 86.43 ? 707 BMA A C6 1 HETATM 4675 O O2 . BMA H 3 . ? 16.858 43.276 46.265 1.00 86.58 ? 707 BMA A O2 1 HETATM 4676 O O3 . BMA H 3 . ? 17.189 40.853 47.804 1.00 85.42 ? 707 BMA A O3 1 HETATM 4677 O O4 . BMA H 3 . ? 18.299 39.351 45.663 1.00 85.65 ? 707 BMA A O4 1 HETATM 4678 O O5 . BMA H 3 . ? 19.064 42.798 44.657 1.00 87.41 ? 707 BMA A O5 1 HETATM 4679 O O6 . BMA H 3 . ? 19.754 41.808 42.319 1.00 85.94 ? 707 BMA A O6 1 HETATM 4680 C C1 . NAG I 2 . ? 16.094 44.314 46.933 1.00 86.11 ? 708 NAG A C1 1 HETATM 4681 C C2 . NAG I 2 . ? 14.742 44.470 46.214 1.00 85.53 ? 708 NAG A C2 1 HETATM 4682 C C3 . NAG I 2 . ? 13.931 45.625 46.822 1.00 85.81 ? 708 NAG A C3 1 HETATM 4683 C C4 . NAG I 2 . ? 13.803 45.454 48.339 1.00 86.02 ? 708 NAG A C4 1 HETATM 4684 C C5 . NAG I 2 . ? 15.170 45.164 48.991 1.00 85.96 ? 708 NAG A C5 1 HETATM 4685 C C6 . NAG I 2 . ? 15.057 44.850 50.488 1.00 85.54 ? 708 NAG A C6 1 HETATM 4686 C C7 . NAG I 2 . ? 14.807 43.607 43.897 1.00 82.71 ? 708 NAG A C7 1 HETATM 4687 C C8 . NAG I 2 . ? 15.427 43.853 42.551 1.00 82.66 ? 708 NAG A C8 1 HETATM 4688 N N2 . NAG I 2 . ? 14.894 44.620 44.768 1.00 84.29 ? 708 NAG A N2 1 HETATM 4689 O O3 . NAG I 2 . ? 12.639 45.693 46.251 1.00 85.74 ? 708 NAG A O3 1 HETATM 4690 O O4 . NAG I 2 . ? 13.198 46.601 48.903 1.00 85.80 ? 708 NAG A O4 1 HETATM 4691 O O5 . NAG I 2 . ? 15.857 44.105 48.324 1.00 86.38 ? 708 NAG A O5 1 HETATM 4692 O O6 . NAG I 2 . ? 13.965 43.995 50.758 1.00 84.48 ? 708 NAG A O6 1 HETATM 4693 O O7 . NAG I 2 . ? 14.268 42.525 44.142 1.00 80.83 ? 708 NAG A O7 1 HETATM 4694 C C1 . NAG J 2 . ? -10.861 15.880 53.645 1.00 60.81 ? 709 NAG A C1 1 HETATM 4695 C C2 . NAG J 2 . ? -11.315 14.772 52.694 1.00 64.67 ? 709 NAG A C2 1 HETATM 4696 C C3 . NAG J 2 . ? -10.586 13.451 52.947 1.00 65.78 ? 709 NAG A C3 1 HETATM 4697 C C4 . NAG J 2 . ? -9.065 13.627 52.899 1.00 65.29 ? 709 NAG A C4 1 HETATM 4698 C C5 . NAG J 2 . ? -8.574 14.838 53.704 1.00 63.41 ? 709 NAG A C5 1 HETATM 4699 C C6 . NAG J 2 . ? -7.345 15.402 53.000 1.00 62.89 ? 709 NAG A C6 1 HETATM 4700 C C7 . NAG J 2 . ? -13.606 14.666 51.817 1.00 67.05 ? 709 NAG A C7 1 HETATM 4701 C C8 . NAG J 2 . ? -14.997 14.166 52.094 1.00 67.47 ? 709 NAG A C8 1 HETATM 4702 N N2 . NAG J 2 . ? -12.751 14.583 52.839 1.00 65.88 ? 709 NAG A N2 1 HETATM 4703 O O3 . NAG J 2 . ? -10.928 12.521 51.936 1.00 67.87 ? 709 NAG A O3 1 HETATM 4704 O O4 . NAG J 2 . ? -8.418 12.432 53.338 1.00 66.66 ? 709 NAG A O4 1 HETATM 4705 O O5 . NAG J 2 . ? -9.452 15.950 53.805 1.00 62.39 ? 709 NAG A O5 1 HETATM 4706 O O6 . NAG J 2 . ? -6.213 15.260 53.809 1.00 62.28 ? 709 NAG A O6 1 HETATM 4707 O O7 . NAG J 2 . ? -13.309 15.121 50.705 1.00 67.59 ? 709 NAG A O7 1 HETATM 4708 C C1 . NAG K 2 . ? -7.253 12.023 52.559 1.00 68.27 ? 710 NAG A C1 1 HETATM 4709 C C2 . NAG K 2 . ? -6.481 10.961 53.362 1.00 68.81 ? 710 NAG A C2 1 HETATM 4710 C C3 . NAG K 2 . ? -5.310 10.341 52.581 1.00 69.46 ? 710 NAG A C3 1 HETATM 4711 C C4 . NAG K 2 . ? -5.793 9.882 51.193 1.00 70.57 ? 710 NAG A C4 1 HETATM 4712 C C5 . NAG K 2 . ? -6.403 11.102 50.483 1.00 70.11 ? 710 NAG A C5 1 HETATM 4713 C C6 . NAG K 2 . ? -6.809 10.829 49.035 1.00 70.22 ? 710 NAG A C6 1 HETATM 4714 C C7 . NAG K 2 . ? -6.480 11.090 55.810 1.00 69.69 ? 710 NAG A C7 1 HETATM 4715 C C8 . NAG K 2 . ? -5.441 10.813 56.860 1.00 69.43 ? 710 NAG A C8 1 HETATM 4716 N N2 . NAG K 2 . ? -6.031 11.525 54.628 1.00 69.13 ? 710 NAG A N2 1 HETATM 4717 O O3 . NAG K 2 . ? -4.802 9.253 53.317 1.00 69.09 ? 710 NAG A O3 1 HETATM 4718 O O4 . NAG K 2 . ? -4.913 9.079 50.364 1.00 72.05 ? 710 NAG A O4 1 HETATM 4719 O O5 . NAG K 2 . ? -7.527 11.580 51.230 1.00 69.07 ? 710 NAG A O5 1 HETATM 4720 O O6 . NAG K 2 . ? -8.200 11.000 48.881 1.00 70.95 ? 710 NAG A O6 1 HETATM 4721 O O7 . NAG K 2 . ? -7.676 10.914 56.061 1.00 69.73 ? 710 NAG A O7 1 HETATM 4722 C C1 . BMA L 3 . ? -3.468 9.179 50.529 1.00 73.80 ? 711 BMA A C1 1 HETATM 4723 C C2 . BMA L 3 . ? -2.758 7.806 50.666 1.00 74.44 ? 711 BMA A C2 1 HETATM 4724 C C3 . BMA L 3 . ? -2.492 7.115 49.315 1.00 74.48 ? 711 BMA A C3 1 HETATM 4725 C C4 . BMA L 3 . ? -2.927 7.996 48.144 1.00 74.40 ? 711 BMA A C4 1 HETATM 4726 C C5 . BMA L 3 . ? -2.325 9.396 48.352 1.00 73.86 ? 711 BMA A C5 1 HETATM 4727 C C6 . BMA L 3 . ? -2.519 10.350 47.169 1.00 72.96 ? 711 BMA A C6 1 HETATM 4728 O O2 . BMA L 3 . ? -3.410 6.920 51.561 1.00 74.49 ? 711 BMA A O2 1 HETATM 4729 O O3 . BMA L 3 . ? -3.103 5.845 49.243 1.00 74.58 ? 711 BMA A O3 1 HETATM 4730 O O4 . BMA L 3 . ? -2.511 7.403 46.930 1.00 74.29 ? 711 BMA A O4 1 HETATM 4731 O O5 . BMA L 3 . ? -2.848 10.002 49.531 1.00 74.53 ? 711 BMA A O5 1 HETATM 4732 O O6 . BMA L 3 . ? -1.431 11.244 47.079 1.00 70.42 ? 711 BMA A O6 1 HETATM 4733 C C1 . FUC M 4 . ? -11.818 11.445 52.339 1.00 69.05 ? 712 FUC A C1 1 HETATM 4734 C C2 . FUC M 4 . ? -12.186 10.681 51.069 1.00 69.62 ? 712 FUC A C2 1 HETATM 4735 C C3 . FUC M 4 . ? -10.990 9.858 50.592 1.00 70.20 ? 712 FUC A C3 1 HETATM 4736 C C4 . FUC M 4 . ? -10.458 8.939 51.700 1.00 70.40 ? 712 FUC A C4 1 HETATM 4737 C C5 . FUC M 4 . ? -10.202 9.755 52.975 1.00 70.25 ? 712 FUC A C5 1 HETATM 4738 C C6 . FUC M 4 . ? -9.729 8.923 54.168 1.00 70.52 ? 712 FUC A C6 1 HETATM 4739 O O2 . FUC M 4 . ? -12.542 11.597 50.062 1.00 69.73 ? 712 FUC A O2 1 HETATM 4740 O O3 . FUC M 4 . ? -11.357 9.121 49.452 1.00 70.58 ? 712 FUC A O3 1 HETATM 4741 O O4 . FUC M 4 . ? -11.377 7.898 51.956 1.00 71.28 ? 712 FUC A O4 1 HETATM 4742 O O5 . FUC M 4 . ? -11.343 10.535 53.334 1.00 69.68 ? 712 FUC A O5 1 HETATM 4743 C C1 . SOG N 5 . ? 25.635 25.879 36.038 1.00 47.75 ? 713 SOG A C1 1 HETATM 4744 C C2 . SOG N 5 . ? 24.674 25.065 36.938 1.00 44.28 ? 713 SOG A C2 1 HETATM 4745 C C3 . SOG N 5 . ? 24.010 23.892 36.214 1.00 41.90 ? 713 SOG A C3 1 HETATM 4746 C C4 . SOG N 5 . ? 23.477 24.345 34.857 1.00 39.60 ? 713 SOG A C4 1 HETATM 4747 C C5 . SOG N 5 . ? 24.634 24.877 34.014 1.00 41.41 ? 713 SOG A C5 1 HETATM 4748 C C6 . SOG N 5 . ? 24.215 25.256 32.576 1.00 39.43 ? 713 SOG A C6 1 HETATM 4749 C "C1'" . SOG N 5 . ? 27.182 27.584 36.827 1.00 53.61 ? 713 SOG A "C1'" 1 HETATM 4750 C "C2'" . SOG N 5 . ? 27.299 29.083 37.112 1.00 55.06 ? 713 SOG A "C2'" 1 HETATM 4751 C "C3'" . SOG N 5 . ? 28.568 29.428 37.890 1.00 56.01 ? 713 SOG A "C3'" 1 HETATM 4752 C "C4'" . SOG N 5 . ? 28.864 30.928 37.888 1.00 56.58 ? 713 SOG A "C4'" 1 HETATM 4753 C "C5'" . SOG N 5 . ? 29.226 31.462 36.504 1.00 57.83 ? 713 SOG A "C5'" 1 HETATM 4754 C "C6'" . SOG N 5 . ? 28.954 32.960 36.385 1.00 59.02 ? 713 SOG A "C6'" 1 HETATM 4755 C "C7'" . SOG N 5 . ? 28.402 33.306 35.005 1.00 59.43 ? 713 SOG A "C7'" 1 HETATM 4756 C "C8'" . SOG N 5 . ? 27.991 34.763 34.909 1.00 60.04 ? 713 SOG A "C8'" 1 HETATM 4757 S S1 . SOG N 5 . ? 25.818 27.204 36.568 1.00 52.30 ? 713 SOG A S1 1 HETATM 4758 O O2 . SOG N 5 . ? 25.407 24.536 38.045 1.00 42.57 ? 713 SOG A O2 1 HETATM 4759 O O3 . SOG N 5 . ? 22.966 23.301 37.004 1.00 38.14 ? 713 SOG A O3 1 HETATM 4760 O O4 . SOG N 5 . ? 22.868 23.237 34.213 1.00 36.50 ? 713 SOG A O4 1 HETATM 4761 O O5 . SOG N 5 . ? 25.178 26.028 34.678 1.00 45.60 ? 713 SOG A O5 1 HETATM 4762 O O6 . SOG N 5 . ? 23.778 26.624 32.514 1.00 35.94 ? 713 SOG A O6 1 HETATM 4763 O O . HOH O 6 . ? 25.009 28.734 35.297 1.00 35.75 ? 801 HOH A O 1 HETATM 4764 O O . HOH O 6 . ? 26.090 30.848 34.497 1.00 57.55 ? 802 HOH A O 1 HETATM 4765 O O . HOH O 6 . ? 25.753 33.365 33.726 1.00 51.85 ? 803 HOH A O 1 HETATM 4766 O O . HOH O 6 . ? 24.494 32.682 31.963 1.00 39.50 ? 804 HOH A O 1 HETATM 4767 O O . HOH O 6 . ? 29.440 30.281 41.132 1.00 54.08 ? 805 HOH A O 1 HETATM 4768 O O . HOH O 6 . ? 27.005 31.018 41.437 1.00 29.77 ? 806 HOH A O 1 HETATM 4769 O O . HOH O 6 . ? 32.497 29.917 44.430 1.00 50.78 ? 807 HOH A O 1 HETATM 4770 O O . HOH O 6 . ? 25.850 33.000 41.991 1.00 36.94 ? 808 HOH A O 1 HETATM 4771 O O . HOH O 6 . ? 23.886 29.103 33.246 1.00 23.55 ? 809 HOH A O 1 HETATM 4772 O O . HOH O 6 . ? 20.833 38.291 45.074 1.00 48.24 ? 810 HOH A O 1 HETATM 4773 O O . HOH O 6 . ? 20.007 27.880 30.783 1.00 19.45 ? 811 HOH A O 1 HETATM 4774 O O . HOH O 6 . ? 25.357 33.155 29.264 1.00 29.85 ? 812 HOH A O 1 HETATM 4775 O O . HOH O 6 . ? 27.384 21.617 39.772 1.00 27.32 ? 813 HOH A O 1 HETATM 4776 O O . HOH O 6 . ? 12.634 20.149 33.842 1.00 18.57 ? 814 HOH A O 1 HETATM 4777 O O . HOH O 6 . ? 5.899 32.539 20.921 1.00 34.21 ? 815 HOH A O 1 HETATM 4778 O O . HOH O 6 . ? 8.249 32.269 31.072 1.00 21.52 ? 816 HOH A O 1 HETATM 4779 O O . HOH O 6 . ? 16.036 22.430 39.362 1.00 24.40 ? 817 HOH A O 1 HETATM 4780 O O . HOH O 6 . ? 11.361 18.808 38.257 1.00 20.11 ? 818 HOH A O 1 HETATM 4781 O O . HOH O 6 . ? 10.529 22.304 38.978 1.00 20.91 ? 819 HOH A O 1 HETATM 4782 O O . HOH O 6 . ? 12.032 35.432 38.913 1.00 19.14 ? 820 HOH A O 1 HETATM 4783 O O . HOH O 6 . ? 30.391 16.270 45.849 1.00 33.70 ? 821 HOH A O 1 HETATM 4784 O O . HOH O 6 . ? 5.355 25.710 45.065 1.00 21.17 ? 822 HOH A O 1 HETATM 4785 O O . HOH O 6 . ? 11.473 36.374 36.376 1.00 23.32 ? 823 HOH A O 1 HETATM 4786 O O . HOH O 6 . ? -1.479 32.828 34.094 1.00 27.19 ? 824 HOH A O 1 HETATM 4787 O O . HOH O 6 . ? 2.461 37.479 43.343 1.00 19.60 ? 825 HOH A O 1 HETATM 4788 O O . HOH O 6 . ? 9.642 20.678 36.907 1.00 21.20 ? 826 HOH A O 1 HETATM 4789 O O . HOH O 6 . ? -11.292 30.657 70.233 1.00 33.95 ? 827 HOH A O 1 HETATM 4790 O O . HOH O 6 . ? -4.453 19.984 47.131 1.00 32.36 ? 828 HOH A O 1 HETATM 4791 O O . HOH O 6 . ? 11.511 34.704 45.110 1.00 22.60 ? 829 HOH A O 1 HETATM 4792 O O . HOH O 6 . ? -8.868 24.721 50.973 1.00 26.98 ? 830 HOH A O 1 HETATM 4793 O O . HOH O 6 . ? 13.352 23.444 40.176 1.00 20.64 ? 831 HOH A O 1 HETATM 4794 O O . HOH O 6 . ? 26.320 24.041 42.253 1.00 27.42 ? 832 HOH A O 1 HETATM 4795 O O . HOH O 6 . ? 16.031 7.738 14.262 1.00 26.83 ? 833 HOH A O 1 HETATM 4796 O O . HOH O 6 . ? 22.972 15.601 46.756 1.00 22.48 ? 834 HOH A O 1 HETATM 4797 O O . HOH O 6 . ? 13.208 20.099 36.603 1.00 14.16 ? 835 HOH A O 1 HETATM 4798 O O . HOH O 6 . ? 13.326 32.958 46.009 1.00 20.00 ? 836 HOH A O 1 HETATM 4799 O O . HOH O 6 . ? 24.652 19.832 53.052 1.00 28.42 ? 837 HOH A O 1 HETATM 4800 O O . HOH O 6 . ? 3.246 42.894 45.831 1.00 25.22 ? 838 HOH A O 1 HETATM 4801 O O . HOH O 6 . ? 34.120 23.026 31.955 1.00 23.70 ? 839 HOH A O 1 HETATM 4802 O O . HOH O 6 . ? 16.199 16.639 43.924 1.00 19.83 ? 840 HOH A O 1 HETATM 4803 O O . HOH O 6 . ? 24.985 21.324 49.491 1.00 24.63 ? 841 HOH A O 1 HETATM 4804 O O . HOH O 6 . ? 9.615 35.023 60.737 1.00 23.85 ? 842 HOH A O 1 HETATM 4805 O O . HOH O 6 . ? -8.466 32.638 40.602 1.00 26.31 ? 843 HOH A O 1 HETATM 4806 O O . HOH O 6 . ? 6.268 6.230 34.143 1.00 42.63 ? 844 HOH A O 1 HETATM 4807 O O . HOH O 6 . ? 2.407 8.864 30.952 1.00 46.82 ? 845 HOH A O 1 HETATM 4808 O O . HOH O 6 . ? 9.346 39.803 52.404 1.00 30.91 ? 846 HOH A O 1 HETATM 4809 O O . HOH O 6 . ? 13.789 35.714 28.123 1.00 25.91 ? 847 HOH A O 1 HETATM 4810 O O . HOH O 6 . ? -11.017 30.411 43.144 1.00 29.11 ? 848 HOH A O 1 HETATM 4811 O O . HOH O 6 . ? 4.429 45.033 44.290 1.00 33.13 ? 849 HOH A O 1 HETATM 4812 O O . HOH O 6 . ? 4.594 32.362 30.730 1.00 22.57 ? 850 HOH A O 1 HETATM 4813 O O . HOH O 6 . ? 18.437 37.885 29.190 1.00 33.25 ? 851 HOH A O 1 HETATM 4814 O O . HOH O 6 . ? 12.241 37.767 27.813 1.00 25.05 ? 852 HOH A O 1 HETATM 4815 O O . HOH O 6 . ? 11.768 34.145 24.785 1.00 20.42 ? 853 HOH A O 1 HETATM 4816 O O . HOH O 6 . ? 12.046 18.272 14.913 1.00 26.94 ? 854 HOH A O 1 HETATM 4817 O O . HOH O 6 . ? -13.911 31.474 41.925 1.00 32.51 ? 855 HOH A O 1 HETATM 4818 O O . HOH O 6 . ? 15.416 21.950 56.096 1.00 30.70 ? 856 HOH A O 1 HETATM 4819 O O . HOH O 6 . ? 7.729 17.800 16.078 1.00 28.08 ? 857 HOH A O 1 HETATM 4820 O O . HOH O 6 . ? 29.648 21.058 13.698 1.00 23.75 ? 858 HOH A O 1 HETATM 4821 O O . HOH O 6 . ? -9.574 31.041 35.076 1.00 38.50 ? 859 HOH A O 1 HETATM 4822 O O . HOH O 6 . ? 10.912 21.169 17.345 1.00 22.93 ? 860 HOH A O 1 HETATM 4823 O O . HOH O 6 . ? 22.691 15.077 42.631 1.00 22.80 ? 861 HOH A O 1 HETATM 4824 O O . HOH O 6 . ? 34.403 23.461 41.618 1.00 27.93 ? 862 HOH A O 1 HETATM 4825 O O . HOH O 6 . ? 32.730 16.857 9.707 1.00 22.17 ? 863 HOH A O 1 HETATM 4826 O O . HOH O 6 . ? 15.491 31.640 65.279 1.00 44.46 ? 864 HOH A O 1 HETATM 4827 O O . HOH O 6 . ? 13.445 20.712 17.902 1.00 25.84 ? 865 HOH A O 1 HETATM 4828 O O . HOH O 6 . ? 16.014 34.310 16.167 1.00 29.61 ? 866 HOH A O 1 HETATM 4829 O O . HOH O 6 . ? -10.741 26.472 41.145 1.00 46.27 ? 867 HOH A O 1 HETATM 4830 O O . HOH O 6 . ? 19.814 20.546 57.631 1.00 29.61 ? 868 HOH A O 1 HETATM 4831 O O . HOH O 6 . ? 1.998 30.023 22.252 1.00 46.03 ? 869 HOH A O 1 HETATM 4832 O O . HOH O 6 . ? 35.921 24.963 30.350 1.00 27.69 ? 870 HOH A O 1 HETATM 4833 O O . HOH O 6 . ? 27.601 21.855 42.956 1.00 28.13 ? 871 HOH A O 1 HETATM 4834 O O . HOH O 6 . ? 27.774 14.582 5.121 1.00 27.35 ? 872 HOH A O 1 HETATM 4835 O O . HOH O 6 . ? 10.780 17.964 12.528 1.00 38.64 ? 873 HOH A O 1 HETATM 4836 O O . HOH O 6 . ? 21.483 31.247 14.759 1.00 23.80 ? 874 HOH A O 1 HETATM 4837 O O . HOH O 6 . ? 15.535 36.632 17.379 1.00 28.52 ? 875 HOH A O 1 HETATM 4838 O O . HOH O 6 . ? 19.533 10.038 46.100 1.00 27.57 ? 876 HOH A O 1 HETATM 4839 O O . HOH O 6 . ? -2.307 16.728 32.944 1.00 40.26 ? 877 HOH A O 1 HETATM 4840 O O . HOH O 6 . ? 9.424 43.334 18.800 1.00 37.23 ? 878 HOH A O 1 HETATM 4841 O O . HOH O 6 . ? -12.510 48.885 59.953 1.00 31.30 ? 879 HOH A O 1 HETATM 4842 O O . HOH O 6 . ? 10.159 18.630 17.060 1.00 25.18 ? 880 HOH A O 1 HETATM 4843 O O . HOH O 6 . ? 22.294 34.041 19.000 1.00 24.32 ? 881 HOH A O 1 HETATM 4844 O O . HOH O 6 . ? -0.020 19.747 24.884 1.00 39.56 ? 882 HOH A O 1 HETATM 4845 O O . HOH O 6 . ? -1.519 30.374 26.157 1.00 58.01 ? 883 HOH A O 1 HETATM 4846 O O . HOH O 6 . ? 17.476 19.674 56.699 1.00 41.33 ? 884 HOH A O 1 HETATM 4847 O O . HOH O 6 . ? 29.834 1.886 30.760 1.00 34.03 ? 885 HOH A O 1 HETATM 4848 O O . HOH O 6 . ? 32.545 26.731 47.556 1.00 32.24 ? 886 HOH A O 1 HETATM 4849 O O . HOH O 6 . ? 39.451 17.454 10.174 1.00 30.95 ? 887 HOH A O 1 HETATM 4850 O O . HOH O 6 . ? 48.072 20.713 25.183 1.00 32.57 ? 888 HOH A O 1 HETATM 4851 O O . HOH O 6 . ? 47.477 21.912 20.374 1.00 28.30 ? 889 HOH A O 1 HETATM 4852 O O . HOH O 6 . ? 39.933 8.195 9.851 1.00 44.36 ? 890 HOH A O 1 HETATM 4853 O O . HOH O 6 . ? 25.683 28.313 52.857 1.00 26.78 ? 891 HOH A O 1 HETATM 4854 O O . HOH O 6 . ? 24.025 13.311 2.998 1.00 45.61 ? 892 HOH A O 1 HETATM 4855 O O . HOH O 6 . ? 27.232 22.323 45.718 1.00 27.51 ? 893 HOH A O 1 HETATM 4856 O O . HOH O 6 . ? -21.645 37.108 52.077 1.00 52.88 ? 894 HOH A O 1 HETATM 4857 O O . HOH O 6 . ? 33.123 3.341 28.778 1.00 30.87 ? 895 HOH A O 1 HETATM 4858 O O . HOH O 6 . ? 23.845 -0.077 30.361 1.00 29.98 ? 896 HOH A O 1 HETATM 4859 O O . HOH O 6 . ? 18.866 11.662 58.319 1.00 40.25 ? 897 HOH A O 1 HETATM 4860 O O . HOH O 6 . ? -12.879 33.264 37.345 1.00 25.20 ? 898 HOH A O 1 HETATM 4861 O O . HOH O 6 . ? -3.864 23.205 16.285 1.00 57.19 ? 899 HOH A O 1 HETATM 4862 O O . HOH O 6 . ? 2.783 38.679 66.673 1.00 38.32 ? 900 HOH A O 1 HETATM 4863 O O . HOH O 6 . ? -1.289 39.652 64.857 1.00 32.21 ? 901 HOH A O 1 HETATM 4864 O O . HOH O 6 . ? 37.452 20.612 16.661 1.00 22.59 ? 902 HOH A O 1 HETATM 4865 O O . HOH O 6 . ? -7.455 30.148 32.961 1.00 43.98 ? 903 HOH A O 1 HETATM 4866 O O . HOH O 6 . ? 23.584 14.520 55.741 1.00 38.35 ? 904 HOH A O 1 HETATM 4867 O O . HOH O 6 . ? -1.564 43.003 38.920 1.00 55.65 ? 905 HOH A O 1 HETATM 4868 O O . HOH O 6 . ? 2.425 32.368 26.261 1.00 39.27 ? 906 HOH A O 1 HETATM 4869 O O . HOH O 6 . ? 14.028 28.064 10.931 1.00 37.89 ? 907 HOH A O 1 HETATM 4870 O O . HOH O 6 . ? -17.216 28.635 44.201 1.00 46.39 ? 908 HOH A O 1 HETATM 4871 O O . HOH O 6 . ? 40.322 3.548 20.472 1.00 35.40 ? 909 HOH A O 1 HETATM 4872 O O . HOH O 6 . ? 11.144 26.492 12.300 1.00 43.25 ? 910 HOH A O 1 HETATM 4873 O O . HOH O 6 . ? 27.391 30.544 52.842 1.00 30.93 ? 911 HOH A O 1 HETATM 4874 O O . HOH O 6 . ? 12.325 35.081 58.425 1.00 30.91 ? 912 HOH A O 1 HETATM 4875 O O . HOH O 6 . ? 0.352 31.782 26.554 1.00 41.81 ? 913 HOH A O 1 HETATM 4876 O O . HOH O 6 . ? -16.717 28.798 61.709 1.00 24.20 ? 914 HOH A O 1 HETATM 4877 O O . HOH O 6 . ? 42.408 16.157 13.000 1.00 29.67 ? 915 HOH A O 1 HETATM 4878 O O . HOH O 6 . ? -11.124 24.335 57.307 1.00 30.81 ? 916 HOH A O 1 HETATM 4879 O O . HOH O 6 . ? -6.508 21.505 31.026 1.00 51.71 ? 917 HOH A O 1 HETATM 4880 O O . HOH O 6 . ? 33.957 20.284 6.973 1.00 21.72 ? 918 HOH A O 1 HETATM 4881 O O . HOH O 6 . ? 42.488 25.613 35.609 1.00 29.98 ? 919 HOH A O 1 HETATM 4882 O O . HOH O 6 . ? 46.673 14.579 15.182 1.00 57.36 ? 920 HOH A O 1 HETATM 4883 O O . HOH O 6 . ? 23.814 16.577 56.868 1.00 36.77 ? 921 HOH A O 1 HETATM 4884 O O . HOH O 6 . ? 20.894 20.562 6.078 1.00 42.15 ? 922 HOH A O 1 HETATM 4885 O O . HOH O 6 . ? -17.018 28.892 47.177 1.00 47.20 ? 923 HOH A O 1 HETATM 4886 O O . HOH O 6 . ? 2.475 45.671 42.178 1.00 37.34 ? 924 HOH A O 1 HETATM 4887 O O . HOH O 6 . ? 45.214 13.503 36.157 1.00 57.37 ? 925 HOH A O 1 HETATM 4888 O O . HOH O 6 . ? 28.760 -1.297 24.988 1.00 63.26 ? 926 HOH A O 1 HETATM 4889 O O . HOH O 6 . ? 4.004 16.143 63.222 1.00 56.58 ? 927 HOH A O 1 HETATM 4890 O O . HOH O 6 . ? 42.872 12.640 12.636 1.00 27.68 ? 928 HOH A O 1 HETATM 4891 O O . HOH O 6 . ? 12.631 37.151 62.592 1.00 38.78 ? 929 HOH A O 1 HETATM 4892 O O . HOH O 6 . ? 34.523 22.328 8.607 1.00 30.88 ? 930 HOH A O 1 HETATM 4893 O O . HOH O 6 . ? 15.966 25.061 8.012 1.00 53.06 ? 931 HOH A O 1 HETATM 4894 O O . HOH O 6 . ? -6.949 16.673 42.374 1.00 48.59 ? 932 HOH A O 1 HETATM 4895 O O . HOH O 6 . ? -11.329 43.110 41.823 1.00 32.99 ? 933 HOH A O 1 HETATM 4896 O O . HOH O 6 . ? -12.586 40.817 41.496 1.00 28.79 ? 934 HOH A O 1 HETATM 4897 O O . HOH O 6 . ? 6.912 45.019 36.282 1.00 38.98 ? 935 HOH A O 1 HETATM 4898 O O . HOH O 6 . ? 19.686 32.061 12.744 1.00 40.60 ? 936 HOH A O 1 HETATM 4899 O O . HOH O 6 . ? 8.561 35.414 15.294 1.00 31.12 ? 937 HOH A O 1 HETATM 4900 O O . HOH O 6 . ? 16.571 38.825 43.649 1.00 34.55 ? 938 HOH A O 1 HETATM 4901 O O . HOH O 6 . ? 16.035 36.728 29.340 1.00 25.00 ? 939 HOH A O 1 HETATM 4902 O O . HOH O 6 . ? -10.544 47.649 63.220 1.00 40.45 ? 940 HOH A O 1 HETATM 4903 O O . HOH O 6 . ? 37.794 30.800 21.713 1.00 33.46 ? 941 HOH A O 1 HETATM 4904 O O . HOH O 6 . ? 11.054 39.487 29.789 1.00 36.50 ? 942 HOH A O 1 HETATM 4905 O O . HOH O 6 . ? -9.851 50.944 51.705 1.00 39.40 ? 943 HOH A O 1 HETATM 4906 O O . HOH O 6 . ? 40.242 10.299 8.681 1.00 39.51 ? 944 HOH A O 1 HETATM 4907 O O . HOH O 6 . ? 42.319 19.599 42.457 1.00 49.81 ? 945 HOH A O 1 HETATM 4908 O O . HOH O 6 . ? 7.539 28.415 68.826 1.00 41.44 ? 946 HOH A O 1 HETATM 4909 O O . HOH O 6 . ? 51.914 16.598 24.953 1.00 44.93 ? 947 HOH A O 1 HETATM 4910 O O . HOH O 6 . ? 40.429 5.103 27.888 1.00 39.36 ? 948 HOH A O 1 HETATM 4911 O O . HOH O 6 . ? 51.951 17.504 22.105 1.00 54.67 ? 949 HOH A O 1 HETATM 4912 O O . HOH O 6 . ? 36.812 2.091 25.871 1.00 44.17 ? 950 HOH A O 1 HETATM 4913 O O . HOH O 6 . ? 34.683 21.982 45.249 1.00 28.20 ? 951 HOH A O 1 HETATM 4914 O O . HOH O 6 . ? 17.374 27.515 48.500 1.00 18.09 ? 952 HOH A O 1 HETATM 4915 O O . HOH O 6 . ? 14.861 20.841 49.051 1.00 25.92 ? 953 HOH A O 1 HETATM 4916 O O . HOH O 6 . ? 16.612 12.001 56.156 1.00 41.13 ? 954 HOH A O 1 HETATM 4917 O O . HOH O 6 . ? 4.460 10.607 52.684 1.00 44.51 ? 955 HOH A O 1 HETATM 4918 O O . HOH O 6 . ? 11.934 28.687 62.080 1.00 24.21 ? 956 HOH A O 1 HETATM 4919 O O . HOH O 6 . ? 34.871 21.795 39.514 1.00 30.26 ? 957 HOH A O 1 HETATM 4920 O O . HOH O 6 . ? 11.087 5.183 40.784 1.00 39.64 ? 958 HOH A O 1 HETATM 4921 O O . HOH O 6 . ? 13.788 35.666 25.351 1.00 23.04 ? 959 HOH A O 1 HETATM 4922 O O . HOH O 6 . ? 19.930 36.928 42.938 1.00 39.05 ? 960 HOH A O 1 HETATM 4923 O O . HOH O 6 . ? 6.953 43.492 44.958 1.00 26.15 ? 961 HOH A O 1 HETATM 4924 O O . HOH O 6 . ? 17.871 31.252 63.389 1.00 27.78 ? 962 HOH A O 1 HETATM 4925 O O . HOH O 6 . ? 32.319 16.914 14.971 1.00 17.87 ? 963 HOH A O 1 HETATM 4926 O O . HOH O 6 . ? 10.187 21.255 34.206 1.00 20.46 ? 964 HOH A O 1 HETATM 4927 O O . HOH O 6 . ? 13.172 8.047 29.682 1.00 19.73 ? 965 HOH A O 1 HETATM 4928 O O . HOH O 6 . ? 2.780 27.689 38.207 1.00 18.98 ? 966 HOH A O 1 HETATM 4929 O O . HOH O 6 . ? 39.255 34.211 24.886 1.00 78.31 ? 967 HOH A O 1 HETATM 4930 O O . HOH O 6 . ? 4.317 41.191 38.565 1.00 23.83 ? 968 HOH A O 1 HETATM 4931 O O . HOH O 6 . ? -1.048 21.271 53.523 1.00 23.37 ? 969 HOH A O 1 HETATM 4932 O O . HOH O 6 . ? 25.038 14.763 53.462 1.00 33.73 ? 970 HOH A O 1 HETATM 4933 O O . HOH O 6 . ? -4.065 14.632 52.622 1.00 40.29 ? 971 HOH A O 1 HETATM 4934 O O . HOH O 6 . ? 15.121 27.524 29.717 1.00 18.58 ? 972 HOH A O 1 HETATM 4935 O O . HOH O 6 . ? 8.191 25.141 44.549 1.00 19.05 ? 973 HOH A O 1 HETATM 4936 O O . HOH O 6 . ? 7.426 25.717 30.017 1.00 19.69 ? 974 HOH A O 1 HETATM 4937 O O . HOH O 6 . ? -1.852 21.727 49.162 1.00 21.84 ? 975 HOH A O 1 HETATM 4938 O O . HOH O 6 . ? 7.351 28.696 51.446 1.00 16.44 ? 976 HOH A O 1 HETATM 4939 O O . HOH O 6 . ? 34.553 19.324 40.557 1.00 24.82 ? 977 HOH A O 1 HETATM 4940 O O . HOH O 6 . ? 14.815 31.627 44.018 1.00 21.32 ? 978 HOH A O 1 HETATM 4941 O O . HOH O 6 . ? 19.289 9.745 14.703 1.00 25.44 ? 979 HOH A O 1 HETATM 4942 O O . HOH O 6 . ? 8.687 28.748 40.193 1.00 19.41 ? 980 HOH A O 1 HETATM 4943 O O . HOH O 6 . ? -19.930 41.047 48.992 1.00 27.67 ? 981 HOH A O 1 HETATM 4944 O O . HOH O 6 . ? 5.859 43.089 52.403 1.00 29.47 ? 982 HOH A O 1 HETATM 4945 O O . HOH O 6 . ? -8.393 30.284 42.244 1.00 24.49 ? 983 HOH A O 1 HETATM 4946 O O . HOH O 6 . ? 16.019 19.026 16.313 1.00 23.75 ? 984 HOH A O 1 HETATM 4947 O O . HOH O 6 . ? 6.298 31.815 17.535 1.00 27.17 ? 985 HOH A O 1 HETATM 4948 O O . HOH O 6 . ? 24.833 34.589 18.926 1.00 29.55 ? 986 HOH A O 1 HETATM 4949 O O . HOH O 6 . ? 15.478 20.020 38.092 1.00 20.22 ? 987 HOH A O 1 HETATM 4950 O O . HOH O 6 . ? 16.219 31.280 33.519 1.00 22.46 ? 988 HOH A O 1 HETATM 4951 O O . HOH O 6 . ? 5.372 31.353 66.710 1.00 28.69 ? 989 HOH A O 1 HETATM 4952 O O . HOH O 6 . ? 6.335 10.327 28.697 1.00 24.80 ? 990 HOH A O 1 HETATM 4953 O O . HOH O 6 . ? -15.797 43.576 55.060 1.00 29.84 ? 991 HOH A O 1 HETATM 4954 O O . HOH O 6 . ? 22.766 21.394 51.371 1.00 37.95 ? 992 HOH A O 1 HETATM 4955 O O . HOH O 6 . ? -13.094 32.006 57.015 1.00 26.90 ? 993 HOH A O 1 HETATM 4956 O O . HOH O 6 . ? 5.647 15.343 26.066 1.00 27.20 ? 994 HOH A O 1 HETATM 4957 O O . HOH O 6 . ? 14.161 13.327 17.201 1.00 28.89 ? 995 HOH A O 1 HETATM 4958 O O . HOH O 6 . ? 29.089 -0.380 11.849 1.00 34.11 ? 996 HOH A O 1 HETATM 4959 O O . HOH O 6 . ? 20.446 11.653 44.071 1.00 25.94 ? 997 HOH A O 1 HETATM 4960 O O . HOH O 6 . ? -1.361 27.802 22.125 1.00 27.91 ? 998 HOH A O 1 HETATM 4961 O O . HOH O 6 . ? 17.685 22.714 14.919 1.00 20.43 ? 999 HOH A O 1 HETATM 4962 O O . HOH O 6 . ? -5.643 27.729 34.625 1.00 29.55 ? 1000 HOH A O 1 HETATM 4963 O O . HOH O 6 . ? -4.619 38.207 63.420 1.00 25.79 ? 1001 HOH A O 1 HETATM 4964 O O . HOH O 6 . ? -7.375 32.496 64.247 1.00 33.30 ? 1002 HOH A O 1 HETATM 4965 O O . HOH O 6 . ? -10.442 46.319 58.659 1.00 30.43 ? 1003 HOH A O 1 HETATM 4966 O O . HOH O 6 . ? -6.523 48.489 45.363 1.00 31.53 ? 1004 HOH A O 1 HETATM 4967 O O . HOH O 6 . ? 8.535 11.908 19.817 1.00 35.29 ? 1005 HOH A O 1 HETATM 4968 O O . HOH O 6 . ? 15.471 15.624 17.100 1.00 27.95 ? 1006 HOH A O 1 HETATM 4969 O O . HOH O 6 . ? -0.396 17.672 47.683 1.00 24.25 ? 1007 HOH A O 1 HETATM 4970 O O . HOH O 6 . ? -7.606 26.054 27.473 1.00 35.99 ? 1008 HOH A O 1 HETATM 4971 O O . HOH O 6 . ? -8.525 16.940 49.529 1.00 43.18 ? 1009 HOH A O 1 HETATM 4972 O O . HOH O 6 . ? -11.786 22.351 55.724 1.00 40.30 ? 1010 HOH A O 1 HETATM 4973 O O . HOH O 6 . ? 21.383 36.914 25.730 1.00 51.72 ? 1011 HOH A O 1 HETATM 4974 O O . HOH O 6 . ? 36.698 9.387 50.053 1.00 42.54 ? 1012 HOH A O 1 HETATM 4975 O O . HOH O 6 . ? 6.261 28.749 66.341 1.00 30.98 ? 1013 HOH A O 1 HETATM 4976 O O . HOH O 6 . ? 6.061 8.276 27.152 1.00 30.02 ? 1014 HOH A O 1 HETATM 4977 O O . HOH O 6 . ? -7.721 34.146 68.352 1.00 36.20 ? 1015 HOH A O 1 HETATM 4978 O O . HOH O 6 . ? 36.114 29.786 12.558 1.00 32.41 ? 1016 HOH A O 1 HETATM 4979 O O . HOH O 6 . ? -17.933 36.728 54.015 1.00 22.56 ? 1017 HOH A O 1 HETATM 4980 O O . HOH O 6 . ? 35.375 29.493 36.735 1.00 31.85 ? 1018 HOH A O 1 HETATM 4981 O O . HOH O 6 . ? 1.574 16.936 30.377 1.00 42.55 ? 1019 HOH A O 1 HETATM 4982 O O . HOH O 6 . ? 37.826 5.639 28.136 1.00 33.19 ? 1020 HOH A O 1 HETATM 4983 O O . HOH O 6 . ? 47.096 9.873 22.443 1.00 34.65 ? 1021 HOH A O 1 HETATM 4984 O O . HOH O 6 . ? -5.437 23.604 41.458 1.00 32.81 ? 1022 HOH A O 1 HETATM 4985 O O . HOH O 6 . ? 20.775 5.907 31.584 1.00 24.92 ? 1023 HOH A O 1 HETATM 4986 O O . HOH O 6 . ? -6.588 37.377 35.483 1.00 46.03 ? 1024 HOH A O 1 HETATM 4987 O O . HOH O 6 . ? -7.074 58.749 61.358 1.00 33.86 ? 1025 HOH A O 1 HETATM 4988 O O . HOH O 6 . ? 29.751 18.086 54.174 1.00 36.83 ? 1026 HOH A O 1 HETATM 4989 O O . HOH O 6 . ? 32.783 3.574 24.347 1.00 33.13 ? 1027 HOH A O 1 HETATM 4990 O O . HOH O 6 . ? 11.307 36.988 60.107 1.00 30.38 ? 1028 HOH A O 1 HETATM 4991 O O . HOH O 6 . ? -13.293 31.492 59.812 1.00 30.35 ? 1029 HOH A O 1 HETATM 4992 O O . HOH O 6 . ? 18.186 11.126 52.288 1.00 25.74 ? 1030 HOH A O 1 HETATM 4993 O O . HOH O 6 . ? 15.632 21.912 16.461 1.00 25.01 ? 1031 HOH A O 1 HETATM 4994 O O . HOH O 6 . ? 7.121 8.520 24.598 1.00 33.38 ? 1032 HOH A O 1 HETATM 4995 O O . HOH O 6 . ? -3.469 25.803 63.496 1.00 31.93 ? 1033 HOH A O 1 HETATM 4996 O O . HOH O 6 . ? -13.364 28.185 56.886 1.00 35.45 ? 1034 HOH A O 1 HETATM 4997 O O . HOH O 6 . ? 24.087 31.570 13.317 1.00 36.79 ? 1035 HOH A O 1 HETATM 4998 O O . HOH O 6 . ? 22.136 0.634 36.219 1.00 30.75 ? 1036 HOH A O 1 HETATM 4999 O O . HOH O 6 . ? 33.708 32.857 18.766 1.00 31.01 ? 1037 HOH A O 1 HETATM 5000 O O . HOH O 6 . ? 19.225 34.431 50.072 1.00 35.55 ? 1038 HOH A O 1 HETATM 5001 O O . HOH O 6 . ? 25.976 21.119 56.325 1.00 27.73 ? 1039 HOH A O 1 HETATM 5002 O O . HOH O 6 . ? 29.235 33.741 26.742 1.00 41.92 ? 1040 HOH A O 1 HETATM 5003 O O . HOH O 6 . ? 14.603 23.883 50.090 1.00 36.90 ? 1041 HOH A O 1 HETATM 5004 O O . HOH O 6 . ? -1.099 16.039 56.013 1.00 36.61 ? 1042 HOH A O 1 HETATM 5005 O O . HOH O 6 . ? 9.002 37.923 16.292 1.00 34.78 ? 1043 HOH A O 1 HETATM 5006 O O . HOH O 6 . ? 41.158 23.184 43.969 1.00 35.70 ? 1044 HOH A O 1 HETATM 5007 O O . HOH O 6 . ? -16.983 30.964 49.037 1.00 31.28 ? 1045 HOH A O 1 HETATM 5008 O O . HOH O 6 . ? 0.316 41.584 64.782 1.00 36.89 ? 1046 HOH A O 1 HETATM 5009 O O . HOH O 6 . ? 36.461 19.011 6.488 1.00 31.68 ? 1047 HOH A O 1 HETATM 5010 O O . HOH O 6 . ? 37.320 3.444 23.568 1.00 35.96 ? 1048 HOH A O 1 HETATM 5011 O O . HOH O 6 . ? -12.567 44.822 43.545 1.00 27.28 ? 1049 HOH A O 1 HETATM 5012 O O . HOH O 6 . ? 46.295 6.501 21.869 1.00 49.15 ? 1050 HOH A O 1 HETATM 5013 O O . HOH O 6 . ? 4.608 30.290 15.134 1.00 62.00 ? 1051 HOH A O 1 HETATM 5014 O O . HOH O 6 . ? 5.961 14.786 23.404 1.00 33.99 ? 1052 HOH A O 1 HETATM 5015 O O . HOH O 6 . ? 23.728 22.800 5.839 1.00 33.54 ? 1053 HOH A O 1 HETATM 5016 O O . HOH O 6 . ? 4.013 11.657 26.479 1.00 33.97 ? 1054 HOH A O 1 HETATM 5017 O O . HOH O 6 . ? 30.158 10.093 57.233 1.00 41.52 ? 1055 HOH A O 1 HETATM 5018 O O . HOH O 6 . ? 33.775 3.448 9.666 1.00 35.99 ? 1056 HOH A O 1 HETATM 5019 O O . HOH O 6 . ? 5.364 38.338 65.383 1.00 27.23 ? 1057 HOH A O 1 HETATM 5020 O O . HOH O 6 . ? 37.936 16.700 53.123 1.00 39.37 ? 1058 HOH A O 1 HETATM 5021 O O . HOH O 6 . ? 25.124 18.732 55.584 1.00 38.79 ? 1059 HOH A O 1 HETATM 5022 O O . HOH O 6 . ? 25.564 34.402 16.331 1.00 42.91 ? 1060 HOH A O 1 HETATM 5023 O O . HOH O 6 . ? 27.797 18.257 15.896 1.00 20.33 ? 1061 HOH A O 1 HETATM 5024 O O . HOH O 6 . ? 19.905 27.734 42.661 1.00 22.49 ? 1062 HOH A O 1 HETATM 5025 O O . HOH O 6 . ? -2.960 31.022 37.367 1.00 25.75 ? 1063 HOH A O 1 HETATM 5026 O O . HOH O 6 . ? 20.599 36.957 36.382 1.00 21.87 ? 1064 HOH A O 1 HETATM 5027 O O . HOH O 6 . ? 31.573 17.044 12.209 1.00 21.21 ? 1065 HOH A O 1 HETATM 5028 O O . HOH O 6 . ? 20.401 36.443 33.417 1.00 25.74 ? 1066 HOH A O 1 HETATM 5029 O O . HOH O 6 . ? -14.884 41.281 42.870 1.00 24.03 ? 1067 HOH A O 1 HETATM 5030 O O . HOH O 6 . ? 29.191 18.616 12.513 1.00 23.16 ? 1068 HOH A O 1 HETATM 5031 O O . HOH O 6 . ? 34.611 8.143 5.112 1.00 31.71 ? 1069 HOH A O 1 HETATM 5032 O O . HOH O 6 . ? 15.827 36.969 49.664 1.00 29.41 ? 1070 HOH A O 1 HETATM 5033 O O . HOH O 6 . ? 35.032 29.451 28.780 1.00 29.64 ? 1071 HOH A O 1 HETATM 5034 O O . HOH O 6 . ? 44.338 4.477 22.518 1.00 38.22 ? 1072 HOH A O 1 HETATM 5035 O O . HOH O 6 . ? 33.883 25.846 42.573 1.00 28.47 ? 1073 HOH A O 1 HETATM 5036 O O . HOH O 6 . ? 0.980 15.602 49.597 1.00 31.08 ? 1074 HOH A O 1 HETATM 5037 O O . HOH O 6 . ? 23.625 13.770 44.801 1.00 24.05 ? 1075 HOH A O 1 HETATM 5038 O O . HOH O 6 . ? -17.168 44.663 43.756 1.00 32.60 ? 1076 HOH A O 1 HETATM 5039 O O . HOH O 6 . ? -14.857 29.311 50.587 1.00 34.98 ? 1077 HOH A O 1 HETATM 5040 O O . HOH O 6 . ? 14.208 18.107 11.229 1.00 28.08 ? 1078 HOH A O 1 HETATM 5041 O O . HOH O 6 . ? 5.896 28.491 13.787 1.00 38.95 ? 1079 HOH A O 1 HETATM 5042 O O . HOH O 6 . ? 15.050 40.473 42.427 1.00 38.73 ? 1080 HOH A O 1 HETATM 5043 O O . HOH O 6 . ? -1.756 15.768 53.283 1.00 38.71 ? 1081 HOH A O 1 HETATM 5044 O O . HOH O 6 . ? 34.880 13.546 44.261 1.00 38.67 ? 1082 HOH A O 1 HETATM 5045 O O . HOH O 6 . ? 34.500 2.644 14.914 1.00 31.72 ? 1083 HOH A O 1 HETATM 5046 O O . HOH O 6 . ? 28.417 30.598 50.221 1.00 31.84 ? 1084 HOH A O 1 HETATM 5047 O O . HOH O 6 . ? 13.206 11.605 15.072 1.00 31.85 ? 1085 HOH A O 1 HETATM 5048 O O . HOH O 6 . ? -18.593 32.656 49.788 1.00 32.05 ? 1086 HOH A O 1 HETATM 5049 O O . HOH O 6 . ? -18.465 46.071 49.610 1.00 34.93 ? 1087 HOH A O 1 HETATM 5050 O O . HOH O 6 . ? -6.820 23.150 58.767 1.00 36.12 ? 1088 HOH A O 1 HETATM 5051 O O . HOH O 6 . ? 1.997 38.448 33.186 1.00 29.82 ? 1089 HOH A O 1 HETATM 5052 O O . HOH O 6 . ? 19.074 0.363 17.592 1.00 43.08 ? 1090 HOH A O 1 HETATM 5053 O O . HOH O 6 . ? 18.608 33.289 61.817 1.00 30.69 ? 1091 HOH A O 1 HETATM 5054 O O . HOH O 6 . ? 13.708 39.850 33.298 1.00 39.76 ? 1092 HOH A O 1 HETATM 5055 O O . HOH O 6 . ? 12.370 39.062 58.481 1.00 33.69 ? 1093 HOH A O 1 HETATM 5056 O O . HOH O 6 . ? 47.510 25.644 30.999 1.00 44.90 ? 1094 HOH A O 1 HETATM 5057 O O . HOH O 6 . ? 24.213 29.582 59.946 1.00 29.07 ? 1095 HOH A O 1 HETATM 5058 O O . HOH O 6 . ? 21.838 -0.486 18.547 1.00 33.81 ? 1096 HOH A O 1 HETATM 5059 O O . HOH O 6 . ? 40.158 7.231 31.839 1.00 32.61 ? 1097 HOH A O 1 HETATM 5060 O O . HOH O 6 . ? -4.428 19.796 35.331 1.00 44.27 ? 1098 HOH A O 1 HETATM 5061 O O . HOH O 6 . ? -5.910 23.234 37.115 1.00 35.85 ? 1099 HOH A O 1 HETATM 5062 O O . HOH O 6 . ? 13.803 9.011 14.582 1.00 36.13 ? 1100 HOH A O 1 HETATM 5063 O O . HOH O 6 . ? -4.231 43.080 39.535 1.00 37.69 ? 1101 HOH A O 1 HETATM 5064 O O . HOH O 6 . ? 50.481 17.522 26.649 1.00 42.13 ? 1102 HOH A O 1 HETATM 5065 O O . HOH O 6 . ? 38.607 20.131 46.454 1.00 33.98 ? 1103 HOH A O 1 HETATM 5066 O O . HOH O 6 . ? 31.717 2.969 19.007 1.00 40.43 ? 1104 HOH A O 1 HETATM 5067 O O . HOH O 6 . ? 12.821 24.007 10.837 1.00 29.46 ? 1105 HOH A O 1 HETATM 5068 O O . HOH O 6 . ? -0.069 29.397 23.838 1.00 60.12 ? 1106 HOH A O 1 HETATM 5069 O O . HOH O 6 . ? 35.784 27.638 41.839 1.00 33.82 ? 1107 HOH A O 1 HETATM 5070 O O . HOH O 6 . ? 33.610 1.541 17.355 1.00 46.15 ? 1108 HOH A O 1 HETATM 5071 O O . HOH O 6 . ? -0.628 52.647 54.710 1.00 38.55 ? 1109 HOH A O 1 HETATM 5072 O O . HOH O 6 . ? 7.550 33.952 23.582 1.00 35.62 ? 1110 HOH A O 1 HETATM 5073 O O . HOH O 6 . ? 36.395 9.605 6.523 1.00 32.36 ? 1111 HOH A O 1 HETATM 5074 O O . HOH O 6 . ? 5.497 36.809 44.712 1.00 37.82 ? 1112 HOH A O 1 HETATM 5075 O O . HOH O 6 . ? 26.961 33.090 53.113 1.00 39.68 ? 1113 HOH A O 1 HETATM 5076 O O . HOH O 6 . ? 22.146 1.370 21.263 1.00 29.90 ? 1114 HOH A O 1 HETATM 5077 O O . HOH O 6 . ? -0.471 53.016 61.926 1.00 44.64 ? 1115 HOH A O 1 HETATM 5078 O O . HOH O 6 . ? 36.826 3.703 15.463 1.00 34.35 ? 1116 HOH A O 1 HETATM 5079 O O . HOH O 6 . ? 11.094 6.005 46.549 1.00 44.60 ? 1117 HOH A O 1 HETATM 5080 O O . HOH O 6 . ? 44.935 24.124 42.205 1.00 38.81 ? 1118 HOH A O 1 HETATM 5081 O O . HOH O 6 . ? -14.066 35.017 56.857 1.00 39.39 ? 1119 HOH A O 1 HETATM 5082 O O . HOH O 6 . ? 43.299 15.106 10.299 1.00 54.59 ? 1120 HOH A O 1 HETATM 5083 O O . HOH O 6 . ? 0.764 16.887 59.878 1.00 36.28 ? 1121 HOH A O 1 HETATM 5084 O O . HOH O 6 . ? 2.855 26.414 16.108 1.00 37.17 ? 1122 HOH A O 1 HETATM 5085 O O . HOH O 6 . ? 4.501 46.370 61.624 1.00 43.31 ? 1123 HOH A O 1 HETATM 5086 O O . HOH O 6 . ? 35.630 6.942 31.083 1.00 33.18 ? 1124 HOH A O 1 HETATM 5087 O O . HOH O 6 . ? 34.790 34.270 21.030 1.00 36.81 ? 1125 HOH A O 1 HETATM 5088 O O . HOH O 6 . ? 35.268 24.540 7.722 1.00 50.25 ? 1126 HOH A O 1 HETATM 5089 O O . HOH O 6 . ? 30.836 0.468 9.540 1.00 47.11 ? 1127 HOH A O 1 HETATM 5090 O O . HOH O 6 . ? 1.655 30.038 65.951 1.00 35.46 ? 1128 HOH A O 1 HETATM 5091 O O . HOH O 6 . ? 37.199 28.060 30.031 1.00 27.96 ? 1129 HOH A O 1 HETATM 5092 O O . HOH O 6 . ? 20.283 3.305 21.758 1.00 33.09 ? 1130 HOH A O 1 HETATM 5093 O O . HOH O 6 . ? -10.554 31.601 72.638 1.00 39.59 ? 1131 HOH A O 1 HETATM 5094 O O . HOH O 6 . ? 18.240 -1.398 26.259 1.00 40.19 ? 1132 HOH A O 1 HETATM 5095 O O . HOH O 6 . ? 18.545 -3.610 33.426 1.00 40.32 ? 1133 HOH A O 1 HETATM 5096 O O . HOH O 6 . ? 29.890 30.411 54.410 1.00 39.37 ? 1134 HOH A O 1 HETATM 5097 O O . HOH O 6 . ? -11.337 44.904 60.584 1.00 40.87 ? 1135 HOH A O 1 HETATM 5098 O O . HOH O 6 . ? 24.410 26.236 62.282 1.00 39.57 ? 1136 HOH A O 1 HETATM 5099 O O . HOH O 6 . ? 39.951 9.370 41.319 1.00 48.26 ? 1137 HOH A O 1 HETATM 5100 O O . HOH O 6 . ? 11.572 44.974 43.302 1.00 41.50 ? 1138 HOH A O 1 HETATM 5101 O O . HOH O 6 . ? 39.169 22.382 15.580 1.00 40.22 ? 1139 HOH A O 1 HETATM 5102 O O . HOH O 6 . ? 6.860 11.038 46.474 1.00 37.38 ? 1140 HOH A O 1 HETATM 5103 O O . HOH O 6 . ? 5.863 32.495 11.009 1.00 37.54 ? 1141 HOH A O 1 HETATM 5104 O O . HOH O 6 . ? 5.412 43.775 41.064 1.00 40.29 ? 1142 HOH A O 1 HETATM 5105 O O . HOH O 6 . ? 4.671 26.847 66.039 1.00 38.15 ? 1143 HOH A O 1 HETATM 5106 O O . HOH O 6 . ? 22.910 3.994 45.992 1.00 43.11 ? 1144 HOH A O 1 HETATM 5107 O O . HOH O 6 . ? 30.414 32.823 10.437 1.00 35.02 ? 1145 HOH A O 1 HETATM 5108 O O . HOH O 6 . ? 42.070 19.596 16.482 1.00 26.47 ? 1146 HOH A O 1 HETATM 5109 O O . HOH O 6 . ? 37.237 9.656 45.707 1.00 41.32 ? 1147 HOH A O 1 HETATM 5110 O O . HOH O 6 . ? 17.692 15.155 21.519 1.00 32.50 ? 1148 HOH A O 1 HETATM 5111 O O . HOH O 6 . ? -1.543 13.134 39.444 1.00 42.87 ? 1149 HOH A O 1 HETATM 5112 O O . HOH O 6 . ? 18.632 3.226 43.970 1.00 44.89 ? 1150 HOH A O 1 HETATM 5113 O O . HOH O 6 . ? 35.726 32.451 22.621 1.00 34.46 ? 1151 HOH A O 1 HETATM 5114 O O . HOH O 6 . ? 8.124 7.172 41.246 1.00 37.30 ? 1152 HOH A O 1 HETATM 5115 O O . HOH O 6 . ? -4.371 50.850 48.691 1.00 39.00 ? 1153 HOH A O 1 HETATM 5116 O O . HOH O 6 . ? 40.669 17.296 43.313 1.00 34.97 ? 1154 HOH A O 1 HETATM 5117 O O . HOH O 6 . ? 2.745 14.676 26.189 1.00 35.96 ? 1155 HOH A O 1 HETATM 5118 O O . HOH O 6 . ? 30.229 3.009 25.355 1.00 35.44 ? 1156 HOH A O 1 HETATM 5119 O O . HOH O 6 . ? 1.643 22.127 18.447 1.00 48.76 ? 1157 HOH A O 1 HETATM 5120 O O . HOH O 6 . ? 2.092 27.377 64.714 1.00 44.07 ? 1158 HOH A O 1 HETATM 5121 O O . HOH O 6 . ? -19.784 34.089 42.823 1.00 40.07 ? 1159 HOH A O 1 HETATM 5122 O O . HOH O 6 . ? 24.355 35.399 29.311 1.00 35.61 ? 1160 HOH A O 1 HETATM 5123 O O . HOH O 6 . ? 18.726 2.993 23.953 1.00 39.58 ? 1161 HOH A O 1 HETATM 5124 O O . HOH O 6 . ? 37.463 29.022 14.770 1.00 38.08 ? 1162 HOH A O 1 HETATM 5125 O O . HOH O 6 . ? 24.765 34.503 54.633 1.00 39.44 ? 1163 HOH A O 1 HETATM 5126 O O . HOH O 6 . ? 34.476 25.867 45.378 1.00 31.32 ? 1164 HOH A O 1 HETATM 5127 O O . HOH O 6 . ? 15.916 2.055 46.949 1.00 42.81 ? 1165 HOH A O 1 HETATM 5128 O O . HOH O 6 . ? 8.445 6.041 24.741 1.00 28.77 ? 1166 HOH A O 1 HETATM 5129 O O . HOH O 6 . ? 8.836 45.151 40.486 1.00 37.89 ? 1167 HOH A O 1 HETATM 5130 O O . HOH O 6 . ? -0.980 51.567 51.931 1.00 47.91 ? 1168 HOH A O 1 HETATM 5131 O O . HOH O 6 . ? 24.226 19.972 63.539 1.00 64.24 ? 1169 HOH A O 1 HETATM 5132 O O . HOH O 6 . ? 40.342 5.304 38.879 1.00 50.31 ? 1170 HOH A O 1 HETATM 5133 O O . HOH O 6 . ? 23.559 29.078 9.262 1.00 37.11 ? 1171 HOH A O 1 HETATM 5134 O O . HOH O 6 . ? 14.230 8.511 18.826 1.00 35.37 ? 1172 HOH A O 1 HETATM 5135 O O . HOH O 6 . ? 29.089 2.184 5.488 1.00 41.19 ? 1173 HOH A O 1 HETATM 5136 O O . HOH O 6 . ? -3.699 29.496 34.100 1.00 36.20 ? 1174 HOH A O 1 HETATM 5137 O O . HOH O 6 . ? 18.371 9.482 54.678 1.00 43.81 ? 1175 HOH A O 1 HETATM 5138 O O . HOH O 6 . ? -9.127 51.647 53.518 1.00 51.27 ? 1176 HOH A O 1 HETATM 5139 O O . HOH O 6 . ? -2.940 25.799 21.951 1.00 29.90 ? 1177 HOH A O 1 HETATM 5140 O O . HOH O 6 . ? 14.899 1.267 50.125 1.00 50.97 ? 1178 HOH A O 1 HETATM 5141 O O . HOH O 6 . ? 4.305 8.138 36.973 1.00 33.53 ? 1179 HOH A O 1 HETATM 5142 O O . HOH O 6 . ? -20.846 39.949 51.378 1.00 35.42 ? 1180 HOH A O 1 HETATM 5143 O O . HOH O 6 . ? 9.248 4.704 35.317 1.00 38.14 ? 1181 HOH A O 1 HETATM 5144 O O . HOH O 6 . ? 22.775 37.199 29.002 1.00 50.20 ? 1182 HOH A O 1 HETATM 5145 O O . HOH O 6 . ? 15.827 31.706 9.652 1.00 33.25 ? 1183 HOH A O 1 HETATM 5146 O O . HOH O 6 . ? 17.017 5.992 16.071 1.00 46.74 ? 1184 HOH A O 1 HETATM 5147 O O . HOH O 6 . ? 29.133 1.522 18.775 1.00 43.47 ? 1185 HOH A O 1 HETATM 5148 O O . HOH O 6 . ? -2.980 54.960 57.699 1.00 36.25 ? 1186 HOH A O 1 HETATM 5149 O O . HOH O 6 . ? 34.940 6.711 53.082 1.00 47.38 ? 1187 HOH A O 1 HETATM 5150 O O . HOH O 6 . ? 17.767 38.690 40.934 1.00 58.96 ? 1188 HOH A O 1 HETATM 5151 O O . HOH O 6 . ? 40.479 5.473 16.849 1.00 40.08 ? 1189 HOH A O 1 HETATM 5152 O O . HOH O 6 . ? 36.243 33.472 50.378 1.00 54.15 ? 1190 HOH A O 1 HETATM 5153 O O . HOH O 6 . ? 49.730 15.621 36.534 1.00 44.35 ? 1191 HOH A O 1 HETATM 5154 O O . HOH O 6 . ? 54.562 13.851 24.898 1.00 45.85 ? 1192 HOH A O 1 HETATM 5155 O O . HOH O 6 . ? 4.197 30.188 20.610 1.00 38.04 ? 1193 HOH A O 1 HETATM 5156 O O . HOH O 6 . ? 45.599 28.267 32.619 1.00 53.48 ? 1194 HOH A O 1 HETATM 5157 O O . HOH O 6 . ? 6.477 41.323 30.546 1.00 47.42 ? 1195 HOH A O 1 HETATM 5158 O O . HOH O 6 . ? 1.054 14.851 57.973 1.00 47.52 ? 1196 HOH A O 1 HETATM 5159 O O . HOH O 6 . ? 38.495 26.819 42.333 1.00 38.59 ? 1197 HOH A O 1 HETATM 5160 O O . HOH O 6 . ? 8.011 34.590 67.619 1.00 34.88 ? 1198 HOH A O 1 HETATM 5161 O O . HOH O 6 . ? 47.829 7.235 27.863 1.00 34.43 ? 1199 HOH A O 1 HETATM 5162 O O . HOH O 6 . ? 24.581 13.397 8.466 1.00 40.33 ? 1200 HOH A O 1 HETATM 5163 O O . HOH O 6 . ? -2.902 33.084 32.327 1.00 38.56 ? 1201 HOH A O 1 HETATM 5164 O O . HOH O 6 . ? 37.578 30.244 34.891 1.00 47.23 ? 1202 HOH A O 1 HETATM 5165 O O . HOH O 6 . ? 24.184 29.386 62.879 1.00 48.77 ? 1203 HOH A O 1 HETATM 5166 O O . HOH O 6 . ? 27.887 33.257 49.979 1.00 38.04 ? 1204 HOH A O 1 HETATM 5167 O O . HOH O 6 . ? 42.505 10.397 36.632 1.00 48.47 ? 1205 HOH A O 1 HETATM 5168 O O . HOH O 6 . ? 9.223 2.891 24.557 1.00 53.15 ? 1206 HOH A O 1 HETATM 5169 O O . HOH O 6 . ? 13.303 40.708 60.559 1.00 46.25 ? 1207 HOH A O 1 HETATM 5170 O O . HOH O 6 . ? 36.432 21.129 53.440 1.00 47.78 ? 1208 HOH A O 1 HETATM 5171 O O . HOH O 6 . ? 48.568 21.904 27.544 1.00 49.29 ? 1209 HOH A O 1 HETATM 5172 O O . HOH O 6 . ? -1.094 37.196 67.165 1.00 36.65 ? 1210 HOH A O 1 HETATM 5173 O O . HOH O 6 . ? 37.468 31.173 16.530 1.00 49.16 ? 1211 HOH A O 1 HETATM 5174 O O . HOH O 6 . ? 9.824 4.804 31.934 1.00 46.40 ? 1212 HOH A O 1 HETATM 5175 O O . HOH O 6 . ? -6.089 22.308 61.400 1.00 43.22 ? 1213 HOH A O 1 HETATM 5176 O O . HOH O 6 . ? 6.919 37.485 67.396 1.00 43.09 ? 1214 HOH A O 1 HETATM 5177 O O . HOH O 6 . ? 5.157 33.305 13.378 1.00 46.83 ? 1215 HOH A O 1 HETATM 5178 O O . HOH O 6 . ? 48.337 19.899 39.696 1.00 53.50 ? 1216 HOH A O 1 HETATM 5179 O O . HOH O 6 . ? -0.952 15.749 45.618 1.00 39.40 ? 1217 HOH A O 1 HETATM 5180 O O . HOH O 6 . ? -5.385 19.440 59.600 1.00 43.81 ? 1218 HOH A O 1 HETATM 5181 O O . HOH O 6 . ? 3.927 7.254 39.505 1.00 50.33 ? 1219 HOH A O 1 HETATM 5182 O O . HOH O 6 . ? -5.126 52.466 64.604 1.00 49.06 ? 1220 HOH A O 1 HETATM 5183 O O . HOH O 6 . ? -2.541 52.289 49.944 1.00 52.38 ? 1221 HOH A O 1 HETATM 5184 O O . HOH O 6 . ? 1.090 25.443 63.615 1.00 43.13 ? 1222 HOH A O 1 HETATM 5185 O O . HOH O 6 . ? 18.491 38.976 37.239 1.00 43.11 ? 1223 HOH A O 1 HETATM 5186 O O . HOH O 6 . ? 25.102 2.558 51.580 1.00 52.05 ? 1224 HOH A O 1 HETATM 5187 O O . HOH O 6 . ? 1.386 17.542 27.787 1.00 53.31 ? 1225 HOH A O 1 HETATM 5188 O O . HOH O 6 . ? -19.046 23.293 52.183 1.00 42.66 ? 1226 HOH A O 1 HETATM 5189 O O . HOH O 6 . ? 33.085 28.992 48.751 1.00 46.90 ? 1227 HOH A O 1 HETATM 5190 O O . HOH O 6 . ? 27.284 17.229 5.095 1.00 41.64 ? 1228 HOH A O 1 HETATM 5191 O O . HOH O 6 . ? 33.433 1.989 42.426 1.00 48.12 ? 1229 HOH A O 1 HETATM 5192 O O . HOH O 6 . ? -17.579 33.200 43.661 1.00 51.38 ? 1230 HOH A O 1 HETATM 5193 O O . HOH O 6 . ? 5.490 20.707 10.600 1.00 45.93 ? 1231 HOH A O 1 HETATM 5194 O O . HOH O 6 . ? -7.683 36.469 67.798 1.00 62.21 ? 1232 HOH A O 1 HETATM 5195 O O . HOH O 6 . ? 27.265 7.908 56.986 1.00 47.89 ? 1233 HOH A O 1 HETATM 5196 O O . HOH O 6 . ? 10.417 44.282 47.225 1.00 50.43 ? 1234 HOH A O 1 HETATM 5197 O O . HOH O 6 . ? 26.335 -1.008 24.528 1.00 36.34 ? 1235 HOH A O 1 HETATM 5198 O O . HOH O 6 . ? -8.405 18.331 47.340 1.00 47.54 ? 1236 HOH A O 1 HETATM 5199 O O . HOH O 6 . ? 17.910 7.231 6.275 1.00 43.10 ? 1237 HOH A O 1 HETATM 5200 O O . HOH O 6 . ? 39.635 22.278 12.883 1.00 48.51 ? 1238 HOH A O 1 HETATM 5201 O O . HOH O 6 . ? 5.222 24.205 65.817 1.00 53.30 ? 1239 HOH A O 1 HETATM 5202 O O . HOH O 6 . ? 26.197 7.177 -0.107 1.00 49.28 ? 1240 HOH A O 1 HETATM 5203 O O . HOH O 6 . ? 0.194 12.957 46.351 1.00 45.11 ? 1241 HOH A O 1 HETATM 5204 O O . HOH O 6 . ? -22.697 39.071 43.605 1.00 39.13 ? 1242 HOH A O 1 HETATM 5205 O O . HOH O 6 . ? -12.411 19.905 44.495 1.00 35.72 ? 1243 HOH A O 1 HETATM 5206 O O . HOH O 6 . ? 6.180 35.242 14.343 1.00 53.54 ? 1244 HOH A O 1 HETATM 5207 O O . HOH O 6 . ? 20.645 2.682 45.725 1.00 47.56 ? 1245 HOH A O 1 HETATM 5208 O O . HOH O 6 . ? 9.058 43.674 62.658 1.00 47.08 ? 1246 HOH A O 1 HETATM 5209 O O . HOH O 6 . ? -6.687 32.039 30.837 1.00 31.62 ? 1247 HOH A O 1 HETATM 5210 O O . HOH O 6 . ? 43.549 11.029 14.592 1.00 56.48 ? 1248 HOH A O 1 HETATM 5211 O O . HOH O 6 . ? 6.719 47.688 56.952 1.00 63.50 ? 1249 HOH A O 1 HETATM 5212 O O . HOH O 6 . ? 24.592 -1.827 23.615 1.00 48.78 ? 1250 HOH A O 1 HETATM 5213 O O . HOH O 6 . ? 18.267 36.484 54.823 1.00 57.89 ? 1251 HOH A O 1 HETATM 5214 O O . HOH O 6 . ? -16.404 47.380 54.790 1.00 39.70 ? 1252 HOH A O 1 HETATM 5215 O O . HOH O 6 . ? 18.590 1.903 20.214 1.00 32.27 ? 1253 HOH A O 1 HETATM 5216 O O . HOH O 6 . ? -10.373 31.677 39.244 1.00 39.23 ? 1254 HOH A O 1 HETATM 5217 O O . HOH O 6 . ? 38.272 3.886 37.998 1.00 54.24 ? 1255 HOH A O 1 HETATM 5218 O O . HOH O 6 . ? 26.877 36.080 46.490 1.00 47.45 ? 1256 HOH A O 1 HETATM 5219 O O . HOH O 6 . ? 10.742 27.534 68.432 1.00 35.74 ? 1257 HOH A O 1 HETATM 5220 O O . HOH O 6 . ? -7.932 27.214 32.024 1.00 50.25 ? 1258 HOH A O 1 HETATM 5221 O O . HOH O 6 . ? 41.464 12.840 41.319 1.00 52.06 ? 1259 HOH A O 1 HETATM 5222 O O . HOH O 6 . ? 12.824 7.952 16.929 1.00 46.74 ? 1260 HOH A O 1 HETATM 5223 O O . HOH O 6 . ? 7.368 50.066 52.184 1.00 71.64 ? 1261 HOH A O 1 HETATM 5224 O O . HOH O 6 . ? 21.351 19.326 65.280 1.00 49.39 ? 1262 HOH A O 1 HETATM 5225 O O . HOH O 6 . ? -7.909 45.476 43.481 1.00 49.82 ? 1263 HOH A O 1 HETATM 5226 O O . HOH O 6 . ? 11.456 19.840 10.859 1.00 51.31 ? 1264 HOH A O 1 HETATM 5227 O O . HOH O 6 . ? -24.466 40.748 44.493 1.00 48.61 ? 1265 HOH A O 1 HETATM 5228 O O . HOH O 6 . ? 34.144 34.535 16.246 1.00 39.60 ? 1266 HOH A O 1 HETATM 5229 O O . HOH O 6 . ? -1.142 30.969 67.744 1.00 51.40 ? 1267 HOH A O 1 HETATM 5230 O O . HOH O 6 . ? 22.905 -3.329 18.178 1.00 58.35 ? 1268 HOH A O 1 HETATM 5231 O O . HOH O 6 . ? 12.140 7.479 54.467 1.00 57.39 ? 1269 HOH A O 1 HETATM 5232 O O . HOH O 6 . ? 15.747 41.076 56.891 1.00 50.47 ? 1270 HOH A O 1 HETATM 5233 O O . HOH O 6 . ? -8.566 42.561 65.609 1.00 63.24 ? 1271 HOH A O 1 HETATM 5234 O O . HOH O 6 . ? 7.152 10.503 22.045 1.00 52.45 ? 1272 HOH A O 1 HETATM 5235 O O . HOH O 6 . ? 23.880 -3.051 10.437 1.00 60.98 ? 1273 HOH A O 1 HETATM 5236 O O . HOH O 6 . ? -4.101 36.558 34.720 1.00 41.01 ? 1274 HOH A O 1 HETATM 5237 O O . HOH O 6 . ? 47.207 25.543 39.624 1.00 54.68 ? 1275 HOH A O 1 HETATM 5238 O O . HOH O 6 . ? 34.755 2.373 31.101 1.00 49.89 ? 1276 HOH A O 1 HETATM 5239 O O . HOH O 6 . ? 10.710 43.630 35.650 1.00 59.74 ? 1277 HOH A O 1 HETATM 5240 O O . HOH O 6 . ? -10.986 43.211 62.489 1.00 57.10 ? 1278 HOH A O 1 HETATM 5241 O O . HOH O 6 . ? -14.788 27.312 47.023 1.00 35.67 ? 1279 HOH A O 1 HETATM 5242 O O . HOH O 6 . ? 6.072 18.491 63.778 1.00 36.23 ? 1280 HOH A O 1 HETATM 5243 O O . HOH O 6 . ? -3.676 32.462 30.108 1.00 35.90 ? 1281 HOH A O 1 HETATM 5244 O O . HOH O 6 . ? -15.975 31.481 60.660 1.00 34.83 ? 1282 HOH A O 1 HETATM 5245 O O . HOH O 6 . ? 18.937 4.211 13.982 1.00 43.06 ? 1283 HOH A O 1 HETATM 5246 O O . HOH O 6 . ? 41.525 25.981 18.648 1.00 57.67 ? 1284 HOH A O 1 HETATM 5247 O O . HOH O 6 . ? -4.604 26.180 71.840 1.00 46.53 ? 1285 HOH A O 1 HETATM 5248 O O . HOH O 6 . ? 39.378 29.429 43.395 1.00 50.83 ? 1286 HOH A O 1 HETATM 5249 O O . HOH O 6 . ? 34.413 31.532 30.273 1.00 34.45 ? 1287 HOH A O 1 HETATM 5250 O O . HOH O 6 . ? 14.328 2.433 39.378 1.00 44.26 ? 1288 HOH A O 1 HETATM 5251 O O . HOH O 6 . ? -5.812 21.709 22.967 1.00 33.29 ? 1289 HOH A O 1 HETATM 5252 O O . HOH O 6 . ? 21.779 34.933 49.879 1.00 43.66 ? 1290 HOH A O 1 HETATM 5253 O O . HOH O 6 . ? 34.370 4.733 54.408 1.00 59.82 ? 1291 HOH A O 1 HETATM 5254 O O . HOH O 6 . ? 33.448 33.774 13.242 1.00 44.38 ? 1292 HOH A O 1 HETATM 5255 O O . HOH O 6 . ? 3.473 33.536 24.723 1.00 48.08 ? 1293 HOH A O 1 HETATM 5256 O O . HOH O 6 . ? 24.731 -2.393 29.191 1.00 56.92 ? 1294 HOH A O 1 HETATM 5257 O O . HOH O 6 . ? -8.711 27.951 29.310 1.00 42.45 ? 1295 HOH A O 1 HETATM 5258 O O . HOH O 6 . ? 18.802 -2.865 7.704 1.00 57.17 ? 1296 HOH A O 1 HETATM 5259 O O . HOH O 6 . ? 29.369 -2.819 30.121 1.00 59.43 ? 1297 HOH A O 1 HETATM 5260 O O . HOH O 6 . ? 10.475 41.867 49.799 1.00 42.38 ? 1298 HOH A O 1 HETATM 5261 O O . HOH O 6 . ? 39.227 7.735 12.544 1.00 60.15 ? 1299 HOH A O 1 HETATM 5262 O O . HOH O 6 . ? 22.583 -2.635 33.348 1.00 43.23 ? 1300 HOH A O 1 HETATM 5263 O O . HOH O 6 . ? 22.684 -2.922 4.349 1.00 53.51 ? 1301 HOH A O 1 HETATM 5264 O O . HOH O 6 . ? 46.897 13.784 39.845 1.00 56.45 ? 1302 HOH A O 1 HETATM 5265 O O . HOH O 6 . ? 33.637 0.915 11.041 1.00 61.13 ? 1303 HOH A O 1 HETATM 5266 O O . HOH O 6 . ? 54.412 16.169 25.631 1.00 45.59 ? 1304 HOH A O 1 HETATM 5267 O O . HOH O 6 . ? 7.846 45.913 49.813 1.00 44.25 ? 1305 HOH A O 1 HETATM 5268 O O . HOH O 6 . ? 6.123 29.673 10.989 1.00 52.34 ? 1306 HOH A O 1 HETATM 5269 O O . HOH O 6 . ? -2.146 10.685 53.813 1.00 62.87 ? 1307 HOH A O 1 HETATM 5270 O O . HOH O 6 . ? 21.330 22.123 68.141 1.00 47.43 ? 1308 HOH A O 1 HETATM 5271 O O . HOH O 6 . ? 17.639 41.527 24.932 1.00 70.38 ? 1309 HOH A O 1 HETATM 5272 O O . HOH O 6 . ? -3.458 46.701 62.124 1.00 42.80 ? 1310 HOH A O 1 HETATM 5273 O O . HOH O 6 . ? 38.856 31.262 42.312 1.00 40.70 ? 1311 HOH A O 1 HETATM 5274 O O . HOH O 6 . ? 23.216 6.280 3.506 1.00 45.16 ? 1312 HOH A O 1 HETATM 5275 O O . HOH O 6 . ? 39.736 26.916 17.340 1.00 35.86 ? 1313 HOH A O 1 HETATM 5276 O O . HOH O 6 . ? -0.139 12.924 48.801 1.00 41.20 ? 1314 HOH A O 1 HETATM 5277 O O . HOH O 6 . ? 9.487 41.457 28.314 1.00 52.90 ? 1315 HOH A O 1 HETATM 5278 O O . HOH O 6 . ? 33.947 34.984 25.994 1.00 58.87 ? 1316 HOH A O 1 HETATM 5279 O O . HOH O 6 . ? -7.229 23.929 28.839 1.00 47.15 ? 1317 HOH A O 1 HETATM 5280 O O . HOH O 6 . ? 24.714 5.655 1.520 1.00 47.65 ? 1318 HOH A O 1 HETATM 5281 O O . HOH O 6 . ? 28.749 6.856 -3.902 1.00 46.18 ? 1319 HOH A O 1 HETATM 5282 O O . HOH O 6 . ? 12.393 -1.440 31.563 1.00 55.25 ? 1320 HOH A O 1 HETATM 5283 O O . HOH O 6 . ? 40.963 9.685 14.935 1.00 40.83 ? 1321 HOH A O 1 HETATM 5284 O O . HOH O 6 . ? 37.669 22.971 52.053 1.00 45.05 ? 1322 HOH A O 1 HETATM 5285 O O . HOH O 6 . ? 12.382 33.127 66.075 1.00 52.07 ? 1323 HOH A O 1 HETATM 5286 O O . HOH O 6 . ? 5.778 11.452 54.187 1.00 35.80 ? 1324 HOH A O 1 HETATM 5287 O O . HOH O 6 . ? 22.565 15.660 59.396 1.00 39.43 ? 1325 HOH A O 1 HETATM 5288 O O . HOH O 6 . ? 15.188 -0.987 33.569 1.00 53.28 ? 1326 HOH A O 1 HETATM 5289 O O . HOH O 6 . ? 21.088 24.641 68.769 1.00 49.30 ? 1327 HOH A O 1 HETATM 5290 O O . HOH O 6 . ? 44.254 7.851 34.228 1.00 50.71 ? 1328 HOH A O 1 HETATM 5291 O O . HOH O 6 . ? -3.896 19.670 32.494 1.00 54.26 ? 1329 HOH A O 1 HETATM 5292 O O . HOH O 6 . ? 41.446 12.590 36.807 1.00 41.47 ? 1330 HOH A O 1 HETATM 5293 O O . HOH O 6 . ? 12.050 40.921 31.664 1.00 46.55 ? 1331 HOH A O 1 HETATM 5294 O O . HOH O 6 . ? 40.791 31.626 44.548 1.00 57.21 ? 1332 HOH A O 1 HETATM 5295 O O . HOH O 6 . ? -1.093 17.097 61.415 1.00 56.96 ? 1333 HOH A O 1 HETATM 5296 O O . HOH O 6 . ? 3.407 47.827 57.130 1.00 45.79 ? 1334 HOH A O 1 HETATM 5297 O O . HOH O 6 . ? -2.244 18.690 27.719 1.00 61.12 ? 1335 HOH A O 1 HETATM 5298 O O . HOH O 6 . ? -6.497 21.645 39.612 1.00 53.29 ? 1336 HOH A O 1 HETATM 5299 O O . HOH O 6 . ? -16.029 29.332 53.213 1.00 43.69 ? 1337 HOH A O 1 HETATM 5300 O O . HOH O 6 . ? 23.225 -2.190 35.851 1.00 52.10 ? 1338 HOH A O 1 HETATM 5301 O O . HOH O 6 . ? 21.438 13.578 9.031 1.00 48.64 ? 1339 HOH A O 1 HETATM 5302 O O . HOH O 6 . ? -6.674 21.103 35.766 1.00 53.64 ? 1340 HOH A O 1 HETATM 5303 O O . HOH O 6 . ? 24.846 22.161 64.954 1.00 48.92 ? 1341 HOH A O 1 HETATM 5304 O O . HOH O 6 . ? 31.343 35.852 26.078 1.00 50.43 ? 1342 HOH A O 1 HETATM 5305 O O . HOH O 6 . ? -24.350 36.459 50.298 1.00 58.77 ? 1343 HOH A O 1 HETATM 5306 O O . HOH O 6 . ? -20.629 34.474 51.853 1.00 47.02 ? 1344 HOH A O 1 HETATM 5307 O O . HOH O 6 . ? 5.494 49.959 49.858 1.00 43.39 ? 1345 HOH A O 1 HETATM 5308 O O . HOH O 6 . ? 28.050 21.002 58.060 1.00 55.92 ? 1346 HOH A O 1 HETATM 5309 O O . HOH O 6 . ? 50.445 19.601 24.912 1.00 53.30 ? 1347 HOH A O 1 HETATM 5310 O O . HOH O 6 . ? 38.310 23.367 9.567 1.00 50.42 ? 1348 HOH A O 1 HETATM 5311 O O . HOH O 6 . ? 13.278 4.406 47.461 1.00 41.84 ? 1349 HOH A O 1 HETATM 5312 O O . HOH O 6 . ? 1.857 9.022 41.457 1.00 48.73 ? 1350 HOH A O 1 HETATM 5313 O O . HOH O 6 . ? 36.302 30.342 8.346 1.00 48.28 ? 1351 HOH A O 1 HETATM 5314 O O . HOH O 6 . ? 6.981 6.488 43.899 1.00 55.75 ? 1352 HOH A O 1 HETATM 5315 O O . HOH O 6 . ? 11.119 18.553 68.543 1.00 53.55 ? 1353 HOH A O 1 HETATM 5316 O O . HOH O 6 . ? 23.335 2.655 43.543 1.00 52.17 ? 1354 HOH A O 1 HETATM 5317 O O . HOH O 6 . ? 15.024 11.656 64.597 1.00 54.81 ? 1355 HOH A O 1 HETATM 5318 O O . HOH O 6 . ? 38.835 31.911 19.642 1.00 47.39 ? 1356 HOH A O 1 HETATM 5319 O O . HOH O 6 . ? 5.979 37.214 22.525 1.00 55.96 ? 1357 HOH A O 1 HETATM 5320 O O . HOH O 6 . ? 49.029 19.028 32.304 1.00 47.09 ? 1358 HOH A O 1 HETATM 5321 O O . HOH O 6 . ? -1.511 37.595 31.686 1.00 50.37 ? 1359 HOH A O 1 HETATM 5322 O O . HOH O 6 . ? -6.537 36.599 65.490 1.00 55.89 ? 1360 HOH A O 1 HETATM 5323 O O . HOH O 6 . ? -0.692 33.131 67.398 1.00 42.15 ? 1361 HOH A O 1 HETATM 5324 O O . HOH O 6 . ? -0.028 17.471 23.330 1.00 50.59 ? 1362 HOH A O 1 HETATM 5325 O O . HOH O 6 . ? 30.198 33.638 30.548 1.00 46.01 ? 1363 HOH A O 1 HETATM 5326 O O . HOH O 6 . ? 11.597 5.271 43.565 1.00 51.67 ? 1364 HOH A O 1 HETATM 5327 O O . HOH O 6 . ? 7.733 9.434 48.783 1.00 47.07 ? 1365 HOH A O 1 HETATM 5328 O O . HOH O 6 . ? 41.242 29.974 31.754 1.00 45.21 ? 1366 HOH A O 1 HETATM 5329 O O . HOH O 6 . ? 23.641 14.752 66.211 1.00 57.34 ? 1367 HOH A O 1 HETATM 5330 O O . HOH O 6 . ? 29.150 -3.613 27.692 1.00 53.70 ? 1368 HOH A O 1 HETATM 5331 O O . HOH O 6 . ? -6.879 17.707 40.311 1.00 55.89 ? 1369 HOH A O 1 HETATM 5332 O O . HOH O 6 . ? 16.836 35.236 51.030 1.00 58.26 ? 1370 HOH A O 1 HETATM 5333 O O . HOH O 6 . ? -7.363 38.947 37.421 1.00 37.15 ? 1371 HOH A O 1 HETATM 5334 O O . HOH O 6 . ? -23.196 36.152 43.596 1.00 45.83 ? 1372 HOH A O 1 HETATM 5335 O O . HOH O 6 . ? -8.314 52.555 55.611 1.00 46.29 ? 1373 HOH A O 1 HETATM 5336 O O . HOH O 6 . ? 38.842 29.867 33.290 1.00 43.04 ? 1374 HOH A O 1 HETATM 5337 O O . HOH O 6 . ? 12.175 25.203 71.717 1.00 49.27 ? 1375 HOH A O 1 HETATM 5338 O O . HOH O 6 . ? 24.096 14.774 61.159 1.00 58.43 ? 1376 HOH A O 1 HETATM 5339 O O . HOH O 6 . ? -5.285 13.638 42.731 1.00 59.56 ? 1377 HOH A O 1 HETATM 5340 O O . HOH O 6 . ? 27.001 16.241 54.366 1.00 45.39 ? 1378 HOH A O 1 HETATM 5341 O O . HOH O 6 . ? 16.986 1.601 42.879 1.00 45.44 ? 1379 HOH A O 1 HETATM 5342 O O . HOH O 6 . ? 36.276 32.787 52.550 1.00 50.62 ? 1380 HOH A O 1 HETATM 5343 O O . HOH O 6 . ? 4.394 18.112 13.617 1.00 51.38 ? 1381 HOH A O 1 HETATM 5344 O O . HOH O 6 . ? 31.478 -2.090 31.594 1.00 48.23 ? 1382 HOH A O 1 HETATM 5345 O O . HOH O 6 . ? 32.893 2.173 4.229 1.00 63.83 ? 1383 HOH A O 1 HETATM 5346 O O . HOH O 6 . ? 34.937 23.355 53.735 1.00 58.96 ? 1384 HOH A O 1 HETATM 5347 O O . HOH O 6 . ? -0.484 18.813 30.299 1.00 59.40 ? 1385 HOH A O 1 HETATM 5348 O O . HOH O 6 . ? 17.026 29.675 10.388 1.00 50.45 ? 1386 HOH A O 1 HETATM 5349 O O . HOH O 6 . ? 35.142 4.499 30.344 1.00 53.55 ? 1387 HOH A O 1 HETATM 5350 O O . HOH O 6 . ? -11.144 39.752 60.785 1.00 35.42 ? 1388 HOH A O 1 HETATM 5351 O O . HOH O 6 . ? 32.252 0.621 31.362 1.00 42.51 ? 1389 HOH A O 1 HETATM 5352 O O . HOH O 6 . ? 48.218 12.305 36.641 1.00 60.74 ? 1390 HOH A O 1 HETATM 5353 O O . HOH O 6 . ? 25.444 -3.580 8.372 1.00 55.33 ? 1391 HOH A O 1 HETATM 5354 O O . HOH O 6 . ? 4.229 40.328 30.135 1.00 59.70 ? 1392 HOH A O 1 HETATM 5355 O O . HOH O 6 . ? 8.681 45.065 45.820 1.00 43.67 ? 1393 HOH A O 1 HETATM 5356 O O . HOH O 6 . ? -9.253 42.863 70.790 1.00 47.14 ? 1394 HOH A O 1 HETATM 5357 O O . HOH O 6 . ? 36.768 7.093 45.730 1.00 45.65 ? 1395 HOH A O 1 HETATM 5358 O O . HOH O 6 . ? 39.585 9.722 43.952 1.00 53.12 ? 1396 HOH A O 1 HETATM 5359 O O . HOH O 6 . ? 21.441 16.927 64.413 1.00 60.97 ? 1397 HOH A O 1 HETATM 5360 O O . HOH O 6 . ? 8.856 2.089 31.101 1.00 56.93 ? 1398 HOH A O 1 HETATM 5361 O O . HOH O 6 . ? 5.186 34.404 22.834 1.00 68.31 ? 1399 HOH A O 1 HETATM 5362 O O . HOH O 6 . ? 17.955 28.040 8.761 1.00 58.72 ? 1400 HOH A O 1 HETATM 5363 O O . HOH O 6 . ? 9.171 45.780 37.823 1.00 57.93 ? 1401 HOH A O 1 HETATM 5364 O O . HOH O 6 . ? 17.199 23.748 6.548 1.00 61.77 ? 1402 HOH A O 1 HETATM 5365 O O . HOH O 6 . ? 19.521 -3.501 10.097 1.00 53.50 ? 1403 HOH A O 1 HETATM 5366 O O . HOH O 6 . ? 27.402 25.598 60.891 1.00 56.44 ? 1404 HOH A O 1 HETATM 5367 O O . HOH O 6 . ? 46.810 6.438 19.105 1.00 45.69 ? 1405 HOH A O 1 HETATM 5368 O O . HOH O 6 . ? 12.431 2.193 37.489 1.00 44.17 ? 1406 HOH A O 1 HETATM 5369 O O . HOH O 6 . ? -4.923 37.794 67.799 1.00 53.93 ? 1407 HOH A O 1 HETATM 5370 O O . HOH O 6 . ? 33.889 3.069 7.174 1.00 47.96 ? 1408 HOH A O 1 HETATM 5371 O O . HOH O 6 . ? 18.516 0.340 24.475 1.00 42.66 ? 1409 HOH A O 1 HETATM 5372 O O . HOH O 6 . ? 20.958 34.479 62.245 1.00 43.83 ? 1410 HOH A O 1 HETATM 5373 O O . HOH O 6 . ? -5.743 46.277 42.551 1.00 45.03 ? 1411 HOH A O 1 HETATM 5374 O O . HOH O 6 . ? -10.462 29.404 36.873 1.00 45.22 ? 1412 HOH A O 1 HETATM 5375 O O . HOH O 6 . ? 22.499 -3.105 26.109 1.00 51.21 ? 1413 HOH A O 1 HETATM 5376 O O . HOH O 6 . ? 39.333 8.502 7.504 1.00 50.69 ? 1414 HOH A O 1 HETATM 5377 O O . HOH O 6 . ? 9.258 12.673 59.723 1.00 54.83 ? 1415 HOH A O 1 HETATM 5378 O O . HOH O 6 . ? 9.638 42.093 22.518 1.00 53.52 ? 1416 HOH A O 1 HETATM 5379 O O . HOH O 6 . ? 16.235 13.857 68.951 1.00 66.95 ? 1417 HOH A O 1 HETATM 5380 O O . HOH O 6 . ? 18.525 9.990 8.178 1.00 41.80 ? 1418 HOH A O 1 HETATM 5381 O O . HOH O 6 . ? -5.815 41.853 37.858 1.00 41.61 ? 1419 HOH A O 1 HETATM 5382 O O . HOH O 6 . ? 38.087 5.903 14.634 1.00 43.23 ? 1420 HOH A O 1 HETATM 5383 O O . HOH O 6 . ? 38.541 3.307 31.842 1.00 47.84 ? 1421 HOH A O 1 HETATM 5384 O O . HOH O 6 . ? 48.260 6.887 23.974 1.00 56.00 ? 1422 HOH A O 1 HETATM 5385 O O . HOH O 6 . ? 7.037 10.857 52.267 1.00 55.84 ? 1423 HOH A O 1 HETATM 5386 O O . HOH O 6 . ? -19.240 38.838 55.150 1.00 41.50 ? 1424 HOH A O 1 HETATM 5387 O O . HOH O 6 . ? 32.878 35.830 21.530 1.00 47.13 ? 1425 HOH A O 1 HETATM 5388 O O . HOH O 6 . ? 40.873 27.386 49.517 1.00 62.54 ? 1426 HOH A O 1 HETATM 5389 O O . HOH O 6 . ? -6.776 51.822 48.376 1.00 48.26 ? 1427 HOH A O 1 HETATM 5390 O O . HOH O 6 . ? 17.447 -0.059 40.925 1.00 65.57 ? 1428 HOH A O 1 HETATM 5391 O O . HOH O 6 . ? 47.593 22.501 39.314 1.00 53.76 ? 1429 HOH A O 1 HETATM 5392 O O . HOH O 6 . ? -2.482 29.941 28.155 1.00 49.81 ? 1430 HOH A O 1 HETATM 5393 O O . HOH O 6 . ? 10.826 0.013 32.812 1.00 45.37 ? 1431 HOH A O 1 HETATM 5394 O O . HOH O 6 . ? 9.914 12.728 62.810 1.00 55.86 ? 1432 HOH A O 1 HETATM 5395 O O . HOH O 6 . ? 28.951 35.495 18.367 1.00 40.34 ? 1433 HOH A O 1 HETATM 5396 O O . HOH O 6 . ? 4.333 9.589 50.338 1.00 56.42 ? 1434 HOH A O 1 HETATM 5397 O O . HOH O 6 . ? -14.960 51.741 52.035 1.00 50.62 ? 1435 HOH A O 1 HETATM 5398 O O . HOH O 6 . ? -7.248 17.857 51.896 1.00 31.02 ? 1436 HOH A O 1 HETATM 5399 O O . HOH O 6 . ? 8.811 21.233 70.052 1.00 48.84 ? 1437 HOH A O 1 HETATM 5400 O O . HOH O 6 . ? 10.785 42.858 33.037 1.00 55.45 ? 1438 HOH A O 1 HETATM 5401 O O . HOH O 6 . ? -2.395 38.436 34.334 1.00 56.80 ? 1439 HOH A O 1 HETATM 5402 O O . HOH O 6 . ? 24.103 -4.076 31.549 1.00 49.44 ? 1440 HOH A O 1 HETATM 5403 O O . HOH O 6 . ? -11.618 17.869 49.901 1.00 45.00 ? 1441 HOH A O 1 HETATM 5404 O O . HOH O 6 . ? 47.735 10.880 17.674 1.00 51.20 ? 1442 HOH A O 1 HETATM 5405 O O . HOH O 6 . ? 8.769 11.447 14.037 1.00 45.77 ? 1443 HOH A O 1 HETATM 5406 O O . HOH O 6 . ? 26.129 33.517 60.815 1.00 57.52 ? 1444 HOH A O 1 HETATM 5407 O O . HOH O 6 . ? -2.033 50.144 45.589 1.00 44.36 ? 1445 HOH A O 1 HETATM 5408 O O . HOH O 6 . ? 41.626 4.963 32.672 1.00 47.98 ? 1446 HOH A O 1 HETATM 5409 O O . HOH O 6 . ? 3.914 12.450 54.289 1.00 56.29 ? 1447 HOH A O 1 HETATM 5410 O O . HOH O 6 . ? -15.385 25.070 55.457 1.00 59.58 ? 1448 HOH A O 1 HETATM 5411 O O . HOH O 6 . ? -0.442 46.239 64.571 1.00 60.96 ? 1449 HOH A O 1 HETATM 5412 O O . HOH O 6 . ? -15.813 37.058 59.031 1.00 31.16 ? 1450 HOH A O 1 HETATM 5413 O O . HOH O 6 . ? -15.342 39.632 59.040 1.00 39.95 ? 1451 HOH A O 1 HETATM 5414 O O . HOH O 6 . ? 17.708 4.069 54.983 1.00 59.66 ? 1452 HOH A O 1 HETATM 5415 O O . HOH O 6 . ? 38.497 27.322 27.833 1.00 65.70 ? 1453 HOH A O 1 HETATM 5416 O O . HOH O 6 . ? -7.342 55.824 59.197 1.00 54.23 ? 1454 HOH A O 1 HETATM 5417 O O . HOH O 6 . ? 19.437 24.258 37.290 1.00 24.88 ? 1455 HOH A O 1 HETATM 5418 O O . HOH O 6 . ? 39.785 20.684 50.501 1.00 58.46 ? 1456 HOH A O 1 HETATM 5419 O O . HOH O 6 . ? 10.408 11.121 15.909 1.00 28.30 ? 1457 HOH A O 1 HETATM 5420 O O . HOH O 6 . ? -8.778 46.643 38.823 1.00 56.83 ? 1458 HOH A O 1 HETATM 5421 O O . HOH O 6 . ? 42.518 9.726 12.378 1.00 65.18 ? 1459 HOH A O 1 HETATM 5422 O O . HOH O 6 . ? 50.376 22.274 32.999 1.00 68.19 ? 1460 HOH A O 1 HETATM 5423 O O . HOH O 6 . ? 13.350 35.656 65.497 1.00 44.22 ? 1461 HOH A O 1 HETATM 5424 O O . HOH O 6 . ? 46.125 4.126 22.226 1.00 45.31 ? 1462 HOH A O 1 HETATM 5425 O O . HOH O 6 . ? -1.164 18.630 63.653 1.00 63.06 ? 1463 HOH A O 1 HETATM 5426 O O . HOH O 6 . ? 2.704 6.769 34.628 1.00 54.91 ? 1464 HOH A O 1 HETATM 5427 O O . HOH O 6 . ? 17.420 3.905 4.625 1.00 56.53 ? 1465 HOH A O 1 HETATM 5428 O O . HOH O 6 . ? 8.962 7.329 48.566 1.00 62.08 ? 1466 HOH A O 1 HETATM 5429 O O . HOH O 6 . ? 26.863 26.416 41.246 1.00 30.42 ? 1467 HOH A O 1 HETATM 5430 O O . HOH O 6 . ? 24.066 15.609 6.047 1.00 55.72 ? 1468 HOH A O 1 HETATM 5431 O O . HOH O 6 . ? 22.767 37.812 37.067 1.00 45.63 ? 1469 HOH A O 1 HETATM 5432 O O . HOH O 6 . ? 50.911 17.070 31.043 1.00 51.55 ? 1470 HOH A O 1 HETATM 5433 O O . HOH O 6 . ? 14.781 17.372 71.914 1.00 52.11 ? 1471 HOH A O 1 HETATM 5434 O O . HOH O 6 . ? 2.554 16.569 20.148 1.00 43.68 ? 1472 HOH A O 1 HETATM 5435 O O . HOH O 6 . ? 28.549 -2.300 16.186 1.00 63.51 ? 1473 HOH A O 1 HETATM 5436 O O . HOH O 6 . ? 35.226 9.044 54.729 1.00 48.87 ? 1474 HOH A O 1 HETATM 5437 O O . HOH O 6 . ? 0.851 11.035 30.806 1.00 51.50 ? 1475 HOH A O 1 HETATM 5438 O O . HOH O 6 . ? 42.137 17.236 10.496 1.00 46.63 ? 1476 HOH A O 1 HETATM 5439 O O . HOH O 6 . ? -1.046 27.261 66.888 1.00 53.09 ? 1477 HOH A O 1 HETATM 5440 O O . HOH O 6 . ? 2.617 25.563 11.661 1.00 57.68 ? 1478 HOH A O 1 HETATM 5441 O O . HOH O 6 . ? 16.127 1.297 13.628 1.00 58.53 ? 1479 HOH A O 1 HETATM 5442 O O . HOH O 6 . ? 8.900 25.828 69.133 1.00 43.12 ? 1480 HOH A O 1 HETATM 5443 O O . HOH O 6 . ? 37.183 11.207 47.848 1.00 34.92 ? 1481 HOH A O 1 HETATM 5444 O O . HOH O 6 . ? 16.892 39.089 56.218 1.00 47.75 ? 1482 HOH A O 1 HETATM 5445 O O . HOH O 6 . ? 24.022 -1.675 40.394 1.00 61.60 ? 1483 HOH A O 1 HETATM 5446 O O . HOH O 6 . ? 2.172 50.015 61.351 1.00 45.35 ? 1484 HOH A O 1 HETATM 5447 O O . HOH O 6 . ? 12.321 1.998 33.937 1.00 43.98 ? 1485 HOH A O 1 HETATM 5448 O O . HOH O 6 . ? 2.197 47.396 63.237 1.00 40.59 ? 1486 HOH A O 1 HETATM 5449 O O . HOH O 6 . ? -5.470 34.137 70.139 1.00 48.11 ? 1487 HOH A O 1 HETATM 5450 O O . HOH O 6 . ? 17.055 22.997 69.896 1.00 65.79 ? 1488 HOH A O 1 HETATM 5451 O O . HOH O 6 . ? 15.640 8.275 53.965 1.00 60.14 ? 1489 HOH A O 1 HETATM 5452 O O . HOH O 6 . ? 18.531 20.714 68.219 1.00 47.58 ? 1490 HOH A O 1 HETATM 5453 O O . HOH O 6 . ? 11.327 11.323 11.222 1.00 52.42 ? 1491 HOH A O 1 HETATM 5454 O O . HOH O 6 . ? 30.200 29.061 56.636 1.00 45.60 ? 1492 HOH A O 1 HETATM 5455 O O . HOH O 6 . ? -24.093 41.887 48.065 1.00 59.53 ? 1493 HOH A O 1 HETATM 5456 O O . HOH O 6 . ? 33.650 6.663 58.618 1.00 56.23 ? 1494 HOH A O 1 HETATM 5457 O O . HOH O 6 . ? 25.389 34.110 49.184 1.00 35.39 ? 1495 HOH A O 1 HETATM 5458 O O . HOH O 6 . ? -3.063 29.174 71.839 1.00 64.43 ? 1496 HOH A O 1 HETATM 5459 O O . HOH O 6 . ? 34.111 4.135 43.435 1.00 57.50 ? 1497 HOH A O 1 HETATM 5460 O O . HOH O 6 . ? -15.701 37.084 55.670 1.00 35.37 ? 1498 HOH A O 1 HETATM 5461 O O . HOH O 6 . ? 27.866 0.663 -1.845 1.00 48.71 ? 1499 HOH A O 1 HETATM 5462 O O . HOH O 6 . ? 5.240 12.622 21.950 1.00 61.64 ? 1500 HOH A O 1 HETATM 5463 O O . HOH O 6 . ? 35.574 5.266 5.795 1.00 52.21 ? 1501 HOH A O 1 HETATM 5464 O O . HOH O 6 . ? 19.288 34.710 10.238 1.00 44.29 ? 1502 HOH A O 1 HETATM 5465 O O . HOH O 6 . ? 20.927 23.584 5.191 1.00 66.42 ? 1503 HOH A O 1 HETATM 5466 O O . HOH O 6 . ? 2.644 9.421 28.314 1.00 59.08 ? 1504 HOH A O 1 HETATM 5467 O O . HOH O 6 . ? 19.216 16.216 7.222 1.00 58.24 ? 1505 HOH A O 1 HETATM 5468 O O . HOH O 6 . ? 21.841 -1.303 22.159 1.00 59.05 ? 1506 HOH A O 1 HETATM 5469 O O . HOH O 6 . ? -17.258 31.069 42.362 1.00 38.91 ? 1507 HOH A O 1 HETATM 5470 O O . HOH O 6 . ? 23.017 31.593 10.564 1.00 38.00 ? 1508 HOH A O 1 HETATM 5471 O O . HOH O 6 . ? 7.277 17.793 65.500 1.00 58.46 ? 1509 HOH A O 1 HETATM 5472 O O . HOH O 6 . ? -14.300 23.004 54.101 1.00 52.36 ? 1510 HOH A O 1 HETATM 5473 O O . HOH O 6 . ? 42.842 3.511 19.956 1.00 54.29 ? 1511 HOH A O 1 HETATM 5474 O O . HOH O 6 . ? 0.519 25.944 14.964 1.00 46.31 ? 1512 HOH A O 1 HETATM 5475 O O . HOH O 6 . ? 43.684 5.388 17.329 1.00 68.24 ? 1513 HOH A O 1 HETATM 5476 O O . HOH O 6 . ? 28.767 1.661 50.772 1.00 57.88 ? 1514 HOH A O 1 HETATM 5477 O O . HOH O 6 . ? 39.775 26.929 12.658 1.00 58.76 ? 1515 HOH A O 1 HETATM 5478 O O . HOH O 6 . ? 13.485 4.181 9.312 1.00 61.14 ? 1516 HOH A O 1 HETATM 5479 O O . HOH O 6 . ? 4.529 43.857 38.748 1.00 50.43 ? 1517 HOH A O 1 HETATM 5480 O O . HOH O 6 . ? -1.486 11.733 50.466 1.00 52.75 ? 1518 HOH A O 1 HETATM 5481 O O . HOH O 6 . ? 16.678 26.166 68.768 1.00 46.80 ? 1519 HOH A O 1 HETATM 5482 O O . HOH O 6 . ? 25.538 27.835 7.472 1.00 42.63 ? 1520 HOH A O 1 HETATM 5483 O O . HOH O 6 . ? 31.867 3.839 54.234 1.00 44.07 ? 1521 HOH A O 1 HETATM 5484 O O . HOH O 6 . ? 31.677 31.013 52.594 1.00 45.18 ? 1522 HOH A O 1 HETATM 5485 O O . HOH O 6 . ? 31.086 32.700 33.039 1.00 42.88 ? 1523 HOH A O 1 HETATM 5486 O O . HOH O 6 . ? -4.712 22.995 21.202 1.00 46.46 ? 1524 HOH A O 1 HETATM 5487 O O . HOH O 6 . ? -9.951 23.022 59.380 1.00 38.37 ? 1525 HOH A O 1 HETATM 5488 O O . HOH O 6 . ? 9.209 40.858 65.891 1.00 41.00 ? 1526 HOH A O 1 HETATM 5489 O O . HOH O 6 . ? -8.956 24.486 38.772 1.00 59.25 ? 1527 HOH A O 1 HETATM 5490 O O . HOH O 6 . ? -9.150 18.019 56.010 1.00 43.02 ? 1528 HOH A O 1 HETATM 5491 O O . HOH O 6 . ? 8.624 5.174 22.105 1.00 45.39 ? 1529 HOH A O 1 HETATM 5492 O O . HOH O 6 . ? 45.510 37.603 52.530 1.00 55.47 ? 1530 HOH A O 1 HETATM 5493 O O . HOH O 6 . ? 2.809 48.993 45.299 1.00 38.63 ? 1531 HOH A O 1 HETATM 5494 O O . HOH O 6 . ? 18.686 41.685 53.168 1.00 57.23 ? 1532 HOH A O 1 HETATM 5495 O O . HOH O 6 . ? 18.266 41.426 35.423 1.00 51.74 ? 1533 HOH A O 1 HETATM 5496 O O . HOH O 6 . ? -5.193 31.883 34.091 1.00 40.09 ? 1534 HOH A O 1 HETATM 5497 O O . HOH O 6 . ? 25.759 -5.490 34.511 1.00 50.93 ? 1535 HOH A O 1 HETATM 5498 O O . HOH O 6 . ? -8.463 26.335 65.336 1.00 47.01 ? 1536 HOH A O 1 HETATM 5499 O O . HOH O 6 . ? 24.225 3.958 -1.302 1.00 68.51 ? 1537 HOH A O 1 HETATM 5500 O O . HOH O 6 . ? 25.555 37.628 19.908 1.00 47.33 ? 1538 HOH A O 1 HETATM 5501 O O . HOH O 6 . ? 23.236 1.716 49.564 1.00 46.04 ? 1539 HOH A O 1 HETATM 5502 O O . HOH O 6 . ? 3.870 51.044 57.033 1.00 61.54 ? 1540 HOH A O 1 HETATM 5503 O O . HOH O 6 . ? 41.938 15.127 42.641 1.00 51.16 ? 1541 HOH A O 1 HETATM 5504 O O . HOH O 6 . ? -8.346 27.671 73.265 1.00 46.07 ? 1542 HOH A O 1 HETATM 5505 O O . HOH O 6 . ? 0.099 23.345 10.500 1.00 64.24 ? 1543 HOH A O 1 HETATM 5506 O O . HOH O 6 . ? 14.841 43.444 30.776 1.00 65.70 ? 1544 HOH A O 1 HETATM 5507 O O . HOH O 6 . ? 42.306 38.095 52.981 1.00 77.63 ? 1545 HOH A O 1 HETATM 5508 O O . HOH O 6 . ? 37.963 25.124 44.878 1.00 53.14 ? 1546 HOH A O 1 HETATM 5509 O O . HOH O 6 . ? 24.490 12.196 57.266 1.00 48.94 ? 1547 HOH A O 1 HETATM 5510 O O . HOH O 6 . ? 0.651 49.580 47.121 1.00 35.40 ? 1548 HOH A O 1 HETATM 5511 O O . HOH O 6 . ? 1.686 50.700 50.338 1.00 37.68 ? 1549 HOH A O 1 HETATM 5512 O O . HOH O 6 . ? 22.755 36.171 31.784 1.00 51.52 ? 1550 HOH A O 1 HETATM 5513 O O . HOH O 6 . ? -14.609 27.424 40.985 1.00 46.42 ? 1551 HOH A O 1 HETATM 5514 O O . HOH O 6 . ? 19.575 9.224 23.848 1.00 37.97 ? 1552 HOH A O 1 HETATM 5515 O O . HOH O 6 . ? 27.989 34.380 29.107 1.00 37.10 ? 1553 HOH A O 1 HETATM 5516 O O . HOH O 6 . ? 6.785 32.599 68.722 1.00 45.96 ? 1554 HOH A O 1 HETATM 5517 O O . HOH O 6 . ? 2.886 37.611 69.459 1.00 56.34 ? 1555 HOH A O 1 HETATM 5518 O O . HOH O 6 . ? 13.627 3.033 44.127 1.00 52.98 ? 1556 HOH A O 1 HETATM 5519 O O . HOH O 6 . ? 39.120 1.907 22.051 1.00 46.43 ? 1557 HOH A O 1 HETATM 5520 O O . HOH O 6 . ? -4.140 40.229 66.734 1.00 53.84 ? 1558 HOH A O 1 HETATM 5521 O O . HOH O 6 . ? 19.962 30.485 65.353 1.00 55.68 ? 1559 HOH A O 1 HETATM 5522 O O . HOH O 6 . ? 38.629 35.621 50.259 1.00 60.20 ? 1560 HOH A O 1 HETATM 5523 O O . HOH O 6 . ? 44.998 14.706 13.152 1.00 42.25 ? 1561 HOH A O 1 HETATM 5524 O O . HOH O 6 . ? 20.958 10.729 7.285 1.00 48.09 ? 1562 HOH A O 1 HETATM 5525 O O . HOH O 6 . ? 27.932 34.992 44.283 1.00 41.13 ? 1563 HOH A O 1 HETATM 5526 O O . HOH O 6 . ? 32.570 29.611 41.973 1.00 43.32 ? 1564 HOH A O 1 HETATM 5527 O O . HOH O 6 . ? 6.128 45.425 63.539 1.00 47.29 ? 1565 HOH A O 1 HETATM 5528 O O . HOH O 6 . ? 14.939 5.762 20.986 1.00 62.69 ? 1566 HOH A O 1 HETATM 5529 O O . HOH O 6 . ? 34.565 25.912 54.958 1.00 53.31 ? 1567 HOH A O 1 HETATM 5530 O O . HOH O 6 . ? 9.698 38.563 66.670 1.00 55.52 ? 1568 HOH A O 1 HETATM 5531 O O . HOH O 6 . ? 29.838 0.743 46.580 1.00 58.61 ? 1569 HOH A O 1 HETATM 5532 O O . HOH O 6 . ? -21.475 31.514 42.130 1.00 55.76 ? 1570 HOH A O 1 HETATM 5533 O O . HOH O 6 . ? 31.941 -0.230 42.340 1.00 56.50 ? 1571 HOH A O 1 HETATM 5534 O O . HOH O 6 . ? -8.507 50.418 46.415 1.00 56.96 ? 1572 HOH A O 1 HETATM 5535 O O . HOH O 6 . ? 16.758 35.003 63.263 1.00 53.63 ? 1573 HOH A O 1 HETATM 5536 O O . HOH O 6 . ? -3.873 15.869 46.271 1.00 43.43 ? 1574 HOH A O 1 HETATM 5537 O O . HOH O 6 . ? -10.571 48.734 45.329 1.00 52.03 ? 1575 HOH A O 1 HETATM 5538 O O . HOH O 6 . ? -10.165 20.241 58.073 1.00 51.54 ? 1576 HOH A O 1 HETATM 5539 O O . HOH O 6 . ? 17.581 6.394 53.439 1.00 58.76 ? 1577 HOH A O 1 HETATM 5540 O O . HOH O 6 . ? 3.400 11.734 56.850 1.00 55.07 ? 1578 HOH A O 1 HETATM 5541 O O . HOH O 6 . ? 28.413 -1.287 21.249 1.00 52.15 ? 1579 HOH A O 1 HETATM 5542 O O . HOH O 6 . ? -7.980 31.189 73.607 1.00 54.14 ? 1580 HOH A O 1 HETATM 5543 O O . HOH O 6 . ? 13.616 6.747 10.974 1.00 52.66 ? 1581 HOH A O 1 HETATM 5544 O O . HOH O 6 . ? 2.912 21.993 65.879 1.00 56.77 ? 1582 HOH A O 1 HETATM 5545 O O . HOH O 6 . ? 30.397 0.324 26.098 1.00 45.25 ? 1583 HOH A O 1 HETATM 5546 O O . HOH O 6 . ? -13.413 23.724 41.194 1.00 60.66 ? 1584 HOH A O 1 HETATM 5547 O O . HOH O 6 . ? 51.753 8.722 21.772 1.00 61.17 ? 1585 HOH A O 1 HETATM 5548 O O . HOH O 6 . ? 17.047 34.044 11.444 1.00 40.21 ? 1586 HOH A O 1 HETATM 5549 O O . HOH O 6 . ? 30.048 35.822 11.394 1.00 51.32 ? 1587 HOH A O 1 HETATM 5550 O O . HOH O 6 . ? 6.792 1.403 26.849 1.00 55.98 ? 1588 HOH A O 1 HETATM 5551 O O . HOH O 6 . ? 33.293 0.585 28.832 1.00 60.90 ? 1589 HOH A O 1 HETATM 5552 O O . HOH O 6 . ? 28.544 -0.401 5.268 1.00 45.96 ? 1590 HOH A O 1 HETATM 5553 O O . HOH O 6 . ? 21.637 37.238 61.728 1.00 60.98 ? 1591 HOH A O 1 HETATM 5554 O O . HOH O 6 . ? 41.235 35.691 52.230 1.00 74.01 ? 1592 HOH A O 1 HETATM 5555 O O . HOH O 6 . ? 9.304 48.386 50.105 1.00 57.67 ? 1593 HOH A O 1 HETATM 5556 O O . HOH O 6 . ? 5.826 3.935 35.189 1.00 58.24 ? 1594 HOH A O 1 HETATM 5557 O O . HOH O 6 . ? -3.392 25.733 67.840 1.00 45.58 ? 1595 HOH A O 1 HETATM 5558 O O . HOH O 6 . ? -8.127 25.029 63.088 1.00 44.78 ? 1596 HOH A O 1 HETATM 5559 O O . HOH O 6 . ? 12.493 27.517 70.341 1.00 60.44 ? 1597 HOH A O 1 HETATM 5560 O O . HOH O 6 . ? 25.297 -2.894 5.520 1.00 66.89 ? 1598 HOH A O 1 HETATM 5561 O O . HOH O 6 . ? 31.326 4.137 3.233 1.00 50.84 ? 1599 HOH A O 1 HETATM 5562 O O . HOH O 6 . ? 33.134 21.330 4.635 1.00 51.86 ? 1600 HOH A O 1 HETATM 5563 O O . HOH O 6 . ? 50.434 14.708 31.979 1.00 47.47 ? 1601 HOH A O 1 HETATM 5564 O O . HOH O 6 . ? -0.482 25.180 12.678 1.00 71.94 ? 1602 HOH A O 1 HETATM 5565 O O . HOH O 6 . ? 27.726 39.103 26.449 1.00 65.88 ? 1603 HOH A O 1 HETATM 5566 O O . HOH O 6 . ? 38.687 30.622 29.405 1.00 68.62 ? 1604 HOH A O 1 HETATM 5567 O O . HOH O 6 . ? 33.645 27.954 7.443 1.00 42.04 ? 1605 HOH A O 1 HETATM 5568 O O . HOH O 6 . ? -9.431 32.010 62.365 1.00 35.43 ? 1606 HOH A O 1 HETATM 5569 O O . HOH O 6 . ? -11.710 33.257 61.424 1.00 32.61 ? 1607 HOH A O 1 HETATM 5570 O O . HOH O 6 . ? -3.564 12.835 54.845 1.00 48.86 ? 1608 HOH A O 1 HETATM 5571 O O . HOH O 6 . ? 20.169 42.501 55.268 1.00 49.60 ? 1609 HOH A O 1 HETATM 5572 O O . HOH O 6 . ? -21.056 46.246 51.328 1.00 63.82 ? 1610 HOH A O 1 HETATM 5573 O O . HOH O 6 . ? 11.978 39.110 64.420 1.00 53.45 ? 1611 HOH A O 1 HETATM 5574 O O . HOH O 6 . ? -6.138 33.496 72.691 1.00 58.39 ? 1612 HOH A O 1 HETATM 5575 O O . HOH O 6 . ? 15.961 3.304 21.827 1.00 56.34 ? 1613 HOH A O 1 HETATM 5576 O O . HOH O 6 . ? 28.520 28.029 61.358 1.00 61.42 ? 1614 HOH A O 1 HETATM 5577 O O . HOH O 6 . ? -1.286 24.972 64.649 1.00 37.09 ? 1615 HOH A O 1 HETATM 5578 O O . HOH O 6 . ? 17.876 38.857 52.512 1.00 53.46 ? 1616 HOH A O 1 HETATM 5579 O O . HOH O 6 . ? 37.571 3.356 17.989 1.00 31.47 ? 1617 HOH A O 1 HETATM 5580 O O . HOH O 6 . ? -15.042 45.725 43.019 1.00 35.78 ? 1618 HOH A O 1 HETATM 5581 O O . HOH O 6 . ? 16.190 41.583 39.926 1.00 34.53 ? 1619 HOH A O 1 HETATM 5582 O O . HOH O 6 . ? -3.566 47.214 41.931 1.00 42.70 ? 1620 HOH A O 1 HETATM 5583 O O . HOH O 6 . ? 9.756 14.545 64.866 1.00 50.19 ? 1621 HOH A O 1 HETATM 5584 O O . HOH O 6 . ? 15.928 43.073 54.822 1.00 38.66 ? 1622 HOH A O 1 HETATM 5585 O O . HOH O 6 . ? 23.323 40.250 45.152 1.00 56.25 ? 1623 HOH A O 1 HETATM 5586 O O . HOH O 6 . ? 10.128 8.851 16.609 1.00 43.39 ? 1624 HOH A O 1 HETATM 5587 O O . HOH O 6 . ? -13.931 46.881 61.094 1.00 51.70 ? 1625 HOH A O 1 HETATM 5588 O O . HOH O 6 . ? 27.329 13.271 57.581 1.00 46.00 ? 1626 HOH A O 1 HETATM 5589 O O . HOH O 6 . ? 26.237 4.134 -3.654 1.00 52.77 ? 1627 HOH A O 1 HETATM 5590 O O . HOH O 6 . ? 26.483 40.975 45.960 1.00 57.87 ? 1628 HOH A O 1 HETATM 5591 O O . HOH O 6 . ? 34.645 11.672 55.196 1.00 55.81 ? 1629 HOH A O 1 HETATM 5592 O O . HOH O 6 . ? 10.711 46.360 58.358 1.00 49.68 ? 1630 HOH A O 1 HETATM 5593 O O . HOH O 6 . ? 36.044 32.797 9.487 1.00 53.72 ? 1631 HOH A O 1 HETATM 5594 O O . HOH O 6 . ? 23.213 -0.801 0.741 1.00 48.24 ? 1632 HOH A O 1 HETATM 5595 O O . HOH O 6 . ? 8.659 17.837 11.392 1.00 52.28 ? 1633 HOH A O 1 HETATM 5596 O O . HOH O 6 . ? -16.638 21.688 53.371 1.00 47.52 ? 1634 HOH A O 1 HETATM 5597 O O . HOH O 6 . ? 41.859 14.158 49.105 1.00 47.47 ? 1635 HOH A O 1 HETATM 5598 O O . HOH O 6 . ? -19.948 23.576 48.674 1.00 51.83 ? 1636 HOH A O 1 HETATM 5599 O O . HOH O 6 . ? 16.495 -6.593 35.694 1.00 52.47 ? 1637 HOH A O 1 HETATM 5600 O O . HOH O 6 . ? 35.191 31.297 38.667 1.00 49.00 ? 1638 HOH A O 1 HETATM 5601 O O . HOH O 6 . ? 35.627 32.598 12.525 1.00 47.50 ? 1639 HOH A O 1 HETATM 5602 O O . HOH O 6 . ? 38.142 5.808 30.881 1.00 48.84 ? 1640 HOH A O 1 HETATM 5603 O O . HOH O 6 . ? 5.069 8.976 46.220 1.00 50.63 ? 1641 HOH A O 1 HETATM 5604 O O . HOH O 6 . ? -3.629 13.465 50.337 1.00 44.87 ? 1642 HOH A O 1 HETATM 5605 O O . HOH O 6 . ? -3.633 54.366 65.792 1.00 59.67 ? 1643 HOH A O 1 HETATM 5606 O O . HOH O 6 . ? 35.770 2.137 19.631 1.00 43.22 ? 1644 HOH A O 1 HETATM 5607 O O . HOH O 6 . ? 4.560 48.625 59.849 1.00 52.33 ? 1645 HOH A O 1 HETATM 5608 O O . HOH O 6 . ? 2.842 31.121 67.780 1.00 49.98 ? 1646 HOH A O 1 HETATM 5609 O O . HOH O 6 . ? 31.200 36.395 18.300 1.00 43.90 ? 1647 HOH A O 1 HETATM 5610 O O . HOH O 6 . ? 12.195 8.991 12.443 1.00 43.09 ? 1648 HOH A O 1 HETATM 5611 O O . HOH O 6 . ? 13.204 1.750 10.383 1.00 53.61 ? 1649 HOH A O 1 HETATM 5612 O O . HOH O 6 . ? 13.673 12.025 8.078 1.00 52.21 ? 1650 HOH A O 1 HETATM 5613 O O . HOH O 6 . ? 4.467 23.318 9.954 1.00 48.29 ? 1651 HOH A O 1 HETATM 5614 O O . HOH O 6 . ? 25.885 35.559 56.941 1.00 48.61 ? 1652 HOH A O 1 HETATM 5615 O O . HOH O 6 . ? -3.272 14.528 56.912 1.00 45.20 ? 1653 HOH A O 1 HETATM 5616 O O . HOH O 6 . ? 34.825 3.474 22.027 1.00 46.49 ? 1654 HOH A O 1 HETATM 5617 O O . HOH O 6 . ? 16.539 11.723 7.411 1.00 56.36 ? 1655 HOH A O 1 HETATM 5618 O O . HOH O 6 . ? 5.175 42.387 67.702 1.00 55.08 ? 1656 HOH A O 1 HETATM 5619 O O . HOH O 6 . ? 30.915 1.575 52.439 1.00 59.47 ? 1657 HOH A O 1 HETATM 5620 O O . HOH O 6 . ? 24.237 37.636 39.607 1.00 54.64 ? 1658 HOH A O 1 HETATM 5621 O O . HOH O 6 . ? 24.851 9.032 56.571 1.00 51.97 ? 1659 HOH A O 1 HETATM 5622 O O . HOH O 6 . ? 0.659 38.997 31.252 1.00 56.35 ? 1660 HOH A O 1 HETATM 5623 O O . HOH O 6 . ? 33.056 34.821 7.694 1.00 65.20 ? 1661 HOH A O 1 HETATM 5624 O O . HOH O 6 . ? 29.846 0.722 1.985 1.00 47.14 ? 1662 HOH A O 1 HETATM 5625 O O . HOH O 6 . ? 28.466 34.950 39.263 1.00 47.74 ? 1663 HOH A O 1 HETATM 5626 O O . HOH O 6 . ? 7.321 23.745 68.431 1.00 55.26 ? 1664 HOH A O 1 HETATM 5627 O O . HOH O 6 . ? -13.767 24.732 57.821 1.00 51.30 ? 1665 HOH A O 1 HETATM 5628 O O . HOH O 6 . ? 27.070 30.064 60.406 1.00 44.22 ? 1666 HOH A O 1 HETATM 5629 O O . HOH O 6 . ? 29.662 -6.663 35.542 1.00 57.97 ? 1667 HOH A O 1 HETATM 5630 O O . HOH O 6 . ? 26.136 -3.827 19.791 1.00 58.34 ? 1668 HOH A O 1 HETATM 5631 O O . HOH O 6 . ? 8.962 12.745 10.973 1.00 61.16 ? 1669 HOH A O 1 HETATM 5632 O O . HOH O 6 . ? 29.135 34.483 54.256 1.00 49.37 ? 1670 HOH A O 1 HETATM 5633 O O . HOH O 6 . ? 20.532 -5.068 32.807 1.00 61.72 ? 1671 HOH A O 1 HETATM 5634 O O . HOH O 6 . ? 30.869 24.465 60.198 1.00 56.62 ? 1672 HOH A O 1 HETATM 5635 O O . HOH O 6 . ? 30.071 33.762 43.568 1.00 53.95 ? 1673 HOH A O 1 HETATM 5636 O O . HOH O 6 . ? -2.404 6.420 54.846 1.00 58.44 ? 1674 HOH A O 1 HETATM 5637 O O . HOH O 6 . ? 53.261 11.342 20.457 1.00 54.08 ? 1675 HOH A O 1 HETATM 5638 O O . HOH O 6 . ? 22.829 41.963 43.146 1.00 61.00 ? 1676 HOH A O 1 HETATM 5639 O O . HOH O 6 . ? 35.105 29.864 40.931 1.00 50.48 ? 1677 HOH A O 1 HETATM 5640 O O . HOH O 6 . ? -0.011 21.465 64.247 1.00 58.21 ? 1678 HOH A O 1 HETATM 5641 O O . HOH O 6 . ? 16.650 17.282 7.126 1.00 54.41 ? 1679 HOH A O 1 HETATM 5642 O O . HOH O 6 . ? 41.653 25.858 47.534 1.00 57.98 ? 1680 HOH A O 1 HETATM 5643 O O . HOH O 6 . ? -0.919 39.571 68.300 1.00 57.15 ? 1681 HOH A O 1 HETATM 5644 O O . HOH O 6 . ? 12.421 5.172 20.339 1.00 50.59 ? 1682 HOH A O 1 HETATM 5645 O O . HOH O 6 . ? 37.795 37.104 48.229 1.00 54.70 ? 1683 HOH A O 1 HETATM 5646 O O . HOH O 6 . ? 17.701 43.837 36.453 1.00 54.83 ? 1684 HOH A O 1 HETATM 5647 O O . HOH O 6 . ? 0.533 49.649 65.958 1.00 58.60 ? 1685 HOH A O 1 HETATM 5648 O O . HOH O 6 . ? 28.035 -3.702 37.503 1.00 62.20 ? 1686 HOH A O 1 HETATM 5649 O O . HOH O 6 . ? 2.651 52.693 61.428 1.00 64.39 ? 1687 HOH A O 1 HETATM 5650 O O . HOH O 6 . ? 44.933 10.293 35.681 1.00 57.49 ? 1688 HOH A O 1 HETATM 5651 O O . HOH O 6 . ? -0.147 11.613 55.403 1.00 57.73 ? 1689 HOH A O 1 HETATM 5652 O O . HOH O 6 . ? -3.916 8.399 44.782 1.00 61.58 ? 1690 HOH A O 1 HETATM 5653 O O . HOH O 6 . ? 27.913 -2.854 10.965 1.00 59.51 ? 1691 HOH A O 1 HETATM 5654 O O . HOH O 6 . ? 35.586 5.287 48.293 1.00 60.68 ? 1692 HOH A O 1 HETATM 5655 O O . HOH O 6 . ? 15.432 5.573 12.610 1.00 49.73 ? 1693 HOH A O 1 HETATM 5656 O O . HOH O 6 . ? -1.637 36.293 69.607 1.00 50.30 ? 1694 HOH A O 1 HETATM 5657 O O . HOH O 6 . ? 2.483 41.137 66.222 1.00 44.33 ? 1695 HOH A O 1 HETATM 5658 O O . HOH O 6 . ? 26.249 35.834 40.765 1.00 54.08 ? 1696 HOH A O 1 HETATM 5659 O O . HOH O 6 . ? 39.358 24.441 47.571 1.00 61.88 ? 1697 HOH A O 1 HETATM 5660 O O . HOH O 6 . ? 54.146 14.028 20.643 1.00 61.20 ? 1698 HOH A O 1 HETATM 5661 O O . HOH O 6 . ? 30.330 29.268 45.673 1.00 49.71 ? 1699 HOH A O 1 HETATM 5662 O O . HOH O 6 . ? 29.818 38.665 48.140 1.00 59.89 ? 1700 HOH A O 1 HETATM 5663 O O . HOH O 6 . ? 29.010 37.051 32.852 1.00 60.31 ? 1701 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 ? 0.5401 0.7864 0.4156 0.0186 0.0677 -0.1880 1 ASP A N 2 C CA . ASP A 1 ? 0.5466 0.7650 0.4350 0.0160 0.0711 -0.1941 1 ASP A CA 3 C C . ASP A 1 ? 0.5356 0.7449 0.4274 0.0089 0.0662 -0.1927 1 ASP A C 4 O O . ASP A 1 ? 0.5251 0.7428 0.4115 0.0077 0.0602 -0.1800 1 ASP A O 5 C CB . ASP A 1 ? 0.5457 0.7467 0.4405 0.0208 0.0741 -0.1793 1 ASP A CB 6 C CG . ASP A 1 ? 0.5740 0.7561 0.4780 0.0245 0.0817 -0.1889 1 ASP A CG 7 O OD1 . ASP A 1 ? 0.6026 0.7694 0.5129 0.0290 0.0841 -0.1784 1 ASP A OD1 8 O OD2 . ASP A 1 ? 0.6332 0.8164 0.5378 0.0236 0.0855 -0.2076 1 ASP A OD2 9 N N . TYR A 2 ? 0.5373 0.7286 0.4386 0.0043 0.0693 -0.2056 2 TYR A N 10 C CA . TYR A 2 ? 0.5217 0.6983 0.4294 -0.0022 0.0664 -0.2020 2 TYR A CA 11 C C . TYR A 2 ? 0.5004 0.6583 0.4118 0.0010 0.0663 -0.1821 2 TYR A C 12 O O . TYR A 2 ? 0.5058 0.6519 0.4208 0.0068 0.0713 -0.1778 2 TYR A O 13 C CB . TYR A 2 ? 0.5325 0.6926 0.4501 -0.0083 0.0718 -0.2204 2 TYR A CB 14 C CG . TYR A 2 ? 0.5249 0.6623 0.4516 -0.0140 0.0720 -0.2157 2 TYR A CG 15 C CD1 . TYR A 2 ? 0.4943 0.6411 0.4210 -0.0211 0.0660 -0.2163 2 TYR A CD1 16 C CD2 . TYR A 2 ? 0.5254 0.6331 0.4604 -0.0116 0.0786 -0.2106 2 TYR A CD2 17 C CE1 . TYR A 2 ? 0.4937 0.6208 0.4287 -0.0264 0.0668 -0.2121 2 TYR A CE1 18 C CE2 . TYR A 2 ? 0.5227 0.6101 0.4652 -0.0165 0.0796 -0.2057 2 TYR A CE2 19 C CZ . TYR A 2 ? 0.5109 0.6081 0.4536 -0.0243 0.0738 -0.2067 2 TYR A CZ 20 O OH . TYR A 2 ? 0.5222 0.6001 0.4723 -0.0292 0.0753 -0.2020 2 TYR A OH 21 N N . VAL A 3 ? 0.4783 0.6355 0.3888 -0.0023 0.0605 -0.1705 3 VAL A N 22 C CA . VAL A 3 ? 0.4542 0.5969 0.3674 0.0001 0.0594 -0.1523 3 VAL A CA 23 C C . VAL A 3 ? 0.4520 0.5744 0.3733 -0.0051 0.0596 -0.1518 3 VAL A C 24 O O . VAL A 3 ? 0.4433 0.5712 0.3633 -0.0101 0.0545 -0.1501 3 VAL A O 25 C CB . VAL A 3 ? 0.4407 0.5993 0.3452 0.0016 0.0532 -0.1368 3 VAL A CB 26 C CG1 . VAL A 3 ? 0.4248 0.5694 0.3328 0.0034 0.0521 -0.1198 3 VAL A CG1 27 C CG2 . VAL A 3 ? 0.4418 0.6202 0.3382 0.0064 0.0542 -0.1365 3 VAL A CG2 28 N N . LEU A 4 ? 0.4557 0.5551 0.3850 -0.0032 0.0658 -0.1527 4 LEU A N 29 C CA . LEU A 4 ? 0.4582 0.5363 0.3954 -0.0081 0.0684 -0.1543 4 LEU A CA 30 C C . LEU A 4 ? 0.4401 0.5162 0.3766 -0.0104 0.0627 -0.1400 4 LEU A C 31 O O . LEU A 4 ? 0.4403 0.5135 0.3801 -0.0172 0.0614 -0.1443 4 LEU A O 32 C CB . LEU A 4 ? 0.4714 0.5243 0.4157 -0.0032 0.0769 -0.1543 4 LEU A CB 33 C CG . LEU A 4 ? 0.4820 0.5098 0.4350 -0.0083 0.0831 -0.1600 4 LEU A CG 34 C CD1 . LEU A 4 ? 0.5116 0.5193 0.4699 -0.0032 0.0932 -0.1673 4 LEU A CD1 35 C CD2 . LEU A 4 ? 0.4518 0.4666 0.4067 -0.0084 0.0812 -0.1445 4 LEU A CD2 36 N N . TYR A 5 ? 0.4228 0.5018 0.3556 -0.0052 0.0593 -0.1242 5 TYR A N 37 C CA . TYR A 5 ? 0.4112 0.4859 0.3436 -0.0067 0.0546 -0.1108 5 TYR A CA 38 C C . TYR A 5 ? 0.4079 0.4985 0.3356 -0.0119 0.0481 -0.1113 5 TYR A C 39 O O . TYR A 5 ? 0.3977 0.4837 0.3264 -0.0145 0.0449 -0.1040 5 TYR A O 40 C CB . TYR A 5 ? 0.3938 0.4687 0.3241 -0.0004 0.0529 -0.0955 5 TYR A CB 41 C CG . TYR A 5 ? 0.3732 0.4684 0.2957 0.0006 0.0480 -0.0891 5 TYR A CG 42 C CD1 . TYR A 5 ? 0.3427 0.4446 0.2609 -0.0024 0.0421 -0.0808 5 TYR A CD1 43 C CD2 . TYR A 5 ? 0.3652 0.4719 0.2849 0.0050 0.0501 -0.0906 5 TYR A CD2 44 C CE1 . TYR A 5 ? 0.3299 0.4476 0.2408 -0.0012 0.0389 -0.0739 5 TYR A CE1 45 C CE2 . TYR A 5 ? 0.3543 0.4783 0.2670 0.0056 0.0470 -0.0838 5 TYR A CE2 46 C CZ . TYR A 5 ? 0.3562 0.4847 0.2644 0.0025 0.0417 -0.0752 5 TYR A CZ 47 O OH . TYR A 5 ? 0.3412 0.4842 0.2423 0.0033 0.0399 -0.0678 5 TYR A OH 48 N N . LYS A 6 ? 0.4214 0.5315 0.3436 -0.0126 0.0462 -0.1196 6 LYS A N 49 C CA . LYS A 6 ? 0.4255 0.5534 0.3422 -0.0158 0.0401 -0.1204 6 LYS A CA 50 C C . LYS A 6 ? 0.4370 0.5666 0.3591 -0.0228 0.0405 -0.1353 6 LYS A C 51 O O . LYS A 6 ? 0.4371 0.5819 0.3564 -0.0255 0.0353 -0.1370 6 LYS A O 52 C CB . LYS A 6 ? 0.4282 0.5787 0.3350 -0.0120 0.0377 -0.1203 6 LYS A CB 53 C CG . LYS A 6 ? 0.4272 0.5792 0.3283 -0.0075 0.0357 -0.1031 6 LYS A CG 54 C CD . LYS A 6 ? 0.4507 0.6231 0.3419 -0.0037 0.0350 -0.1015 6 LYS A CD 55 C CE . LYS A 6 ? 0.4488 0.6211 0.3354 -0.0011 0.0334 -0.0840 6 LYS A CE 56 N NZ . LYS A 6 ? 0.4673 0.6566 0.3451 0.0027 0.0349 -0.0810 6 LYS A NZ 57 N N . ASP A 7 ? 0.4471 0.5612 0.3775 -0.0255 0.0471 -0.1461 7 ASP A N 58 C CA . ASP A 7 ? 0.4546 0.5692 0.3919 -0.0335 0.0492 -0.1627 7 ASP A CA 59 C C . ASP A 7 ? 0.4531 0.5509 0.3981 -0.0385 0.0502 -0.1580 7 ASP A C 60 O O . ASP A 7 ? 0.4603 0.5338 0.4110 -0.0377 0.0562 -0.1535 7 ASP A O 61 C CB . ASP A 7 ? 0.4696 0.5744 0.4119 -0.0343 0.0571 -0.1777 7 ASP A CB 62 C CG . ASP A 7 ? 0.4812 0.5879 0.4315 -0.0439 0.0600 -0.1977 7 ASP A CG 63 O OD1 . ASP A 7 ? 0.4841 0.5985 0.4373 -0.0502 0.0563 -0.1996 7 ASP A OD1 64 O OD2 . ASP A 7 ? 0.5084 0.6087 0.4626 -0.0453 0.0665 -0.2122 7 ASP A OD2 65 N N . ALA A 8 ? 0.4403 0.5524 0.3850 -0.0428 0.0447 -0.1586 8 ALA A N 66 C CA . ALA A 8 ? 0.4420 0.5426 0.3932 -0.0475 0.0449 -0.1537 8 ALA A CA 67 C C . ALA A 8 ? 0.4557 0.5372 0.4188 -0.0552 0.0534 -0.1651 8 ALA A C 68 O O . ALA A 8 ? 0.4632 0.5281 0.4317 -0.0576 0.0562 -0.1581 8 ALA A O 69 C CB . ALA A 8 ? 0.4306 0.5541 0.3793 -0.0500 0.0373 -0.1542 8 ALA A CB 70 N N . THR A 9 ? 0.4750 0.5584 0.4420 -0.0591 0.0580 -0.1825 9 THR A N 71 C CA . THR A 9 ? 0.4895 0.5550 0.4685 -0.0678 0.0671 -0.1960 9 THR A CA 72 C C . THR A 9 ? 0.5006 0.5337 0.4828 -0.0637 0.0768 -0.1905 9 THR A C 73 O O . THR A 9 ? 0.5226 0.5354 0.5143 -0.0700 0.0861 -0.1995 9 THR A O 74 C CB . THR A 9 ? 0.5026 0.5843 0.4852 -0.0746 0.0685 -0.2194 9 THR A CB 75 O OG1 . THR A 9 ? 0.5075 0.5881 0.4849 -0.0682 0.0709 -0.2235 9 THR A OG1 76 C CG2 . THR A 9 ? 0.4972 0.6145 0.4754 -0.0767 0.0586 -0.2248 9 THR A CG2 77 N N . LYS A 10 ? 0.4870 0.5156 0.4614 -0.0531 0.0750 -0.1760 10 LYS A N 78 C CA . LYS A 10 ? 0.4874 0.4898 0.4634 -0.0465 0.0830 -0.1700 10 LYS A CA 79 C C . LYS A 10 ? 0.4738 0.4569 0.4510 -0.0434 0.0846 -0.1524 10 LYS A C 80 O O . LYS A 10 ? 0.4544 0.4479 0.4279 -0.0433 0.0775 -0.1417 10 LYS A O 81 C CB . LYS A 10 ? 0.4851 0.4970 0.4530 -0.0365 0.0802 -0.1651 10 LYS A CB 82 C CG . LYS A 10 ? 0.4963 0.5231 0.4628 -0.0378 0.0810 -0.1825 10 LYS A CG 83 C CD . LYS A 10 ? 0.5187 0.5233 0.4926 -0.0388 0.0922 -0.1953 10 LYS A CD 84 C CE . LYS A 10 ? 0.5510 0.5717 0.5257 -0.0441 0.0930 -0.2173 10 LYS A CE 85 N NZ . LYS A 10 ? 0.5832 0.5805 0.5653 -0.0450 0.1047 -0.2306 10 LYS A NZ 86 N N . PRO A 11 ? 0.4821 0.4371 0.4639 -0.0405 0.0945 -0.1496 11 PRO A N 87 C CA . PRO A 11 ? 0.4763 0.4142 0.4579 -0.0360 0.0963 -0.1323 11 PRO A CA 88 C C . PRO A 11 ? 0.4570 0.4059 0.4300 -0.0262 0.0882 -0.1157 11 PRO A C 89 O O . PRO A 11 ? 0.4504 0.4103 0.4186 -0.0201 0.0852 -0.1158 11 PRO A O 90 C CB . PRO A 11 ? 0.5007 0.4089 0.4868 -0.0315 0.1085 -0.1328 11 PRO A CB 91 C CG . PRO A 11 ? 0.5109 0.4171 0.5034 -0.0396 0.1145 -0.1538 11 PRO A CG 92 C CD . PRO A 11 ? 0.5030 0.4402 0.4905 -0.0408 0.1049 -0.1623 11 PRO A CD 93 N N . VAL A 12 ? 0.4393 0.3856 0.4106 -0.0255 0.0851 -0.1025 12 VAL A N 94 C CA . VAL A 12 ? 0.4149 0.3715 0.3791 -0.0178 0.0776 -0.0875 12 VAL A CA 95 C C . VAL A 12 ? 0.4172 0.3674 0.3791 -0.0068 0.0803 -0.0813 12 VAL A C 96 O O . VAL A 12 ? 0.4012 0.3674 0.3584 -0.0023 0.0747 -0.0784 12 VAL A O 97 C CB . VAL A 12 ? 0.4044 0.3552 0.3680 -0.0184 0.0758 -0.0753 12 VAL A CB 98 C CG1 . VAL A 12 ? 0.3744 0.3300 0.3318 -0.0094 0.0705 -0.0602 12 VAL A CG1 99 C CG2 . VAL A 12 ? 0.4055 0.3708 0.3697 -0.0275 0.0701 -0.0799 12 VAL A CG2 100 N N . GLU A 13 ? 0.4334 0.3606 0.3989 -0.0023 0.0895 -0.0793 13 GLU A N 101 C CA . GLU A 13 ? 0.4420 0.3631 0.4058 0.0098 0.0926 -0.0726 13 GLU A CA 102 C C . GLU A 13 ? 0.4423 0.3755 0.4052 0.0124 0.0920 -0.0821 13 GLU A C 103 O O . GLU A 13 ? 0.4366 0.3797 0.3964 0.0209 0.0891 -0.0757 13 GLU A O 104 C CB . GLU A 13 ? 0.4620 0.3542 0.4294 0.0148 0.1038 -0.0694 13 GLU A CB 105 C CG . GLU A 13 ? 0.4678 0.3487 0.4346 0.0146 0.1049 -0.0571 13 GLU A CG 106 C CD . GLU A 13 ? 0.4810 0.3771 0.4417 0.0211 0.0960 -0.0428 13 GLU A CD 107 O OE1 . GLU A 13 ? 0.4759 0.3792 0.4339 0.0313 0.0940 -0.0372 13 GLU A OE1 108 O OE2 . GLU A 13 ? 0.4948 0.3965 0.4539 0.0158 0.0912 -0.0379 13 GLU A OE2 109 N N . ASP A 14 ? 0.4538 0.3876 0.4198 0.0047 0.0948 -0.0980 14 ASP A N 110 C CA . ASP A 14 ? 0.4535 0.4010 0.4182 0.0058 0.0943 -0.1092 14 ASP A CA 111 C C . ASP A 14 ? 0.4233 0.3989 0.3815 0.0052 0.0840 -0.1059 14 ASP A C 112 O O . ASP A 14 ? 0.4178 0.4053 0.3730 0.0113 0.0827 -0.1054 14 ASP A O 113 C CB . ASP A 14 ? 0.4691 0.4136 0.4384 -0.0039 0.0988 -0.1280 14 ASP A CB 114 C CG . ASP A 14 ? 0.5275 0.4425 0.5038 -0.0037 0.1110 -0.1340 14 ASP A CG 115 O OD1 . ASP A 14 ? 0.5853 0.4944 0.5672 -0.0139 0.1153 -0.1482 14 ASP A OD1 116 O OD2 . ASP A 14 ? 0.5650 0.4631 0.5415 0.0068 0.1167 -0.1251 14 ASP A OD2 117 N N . ARG A 15 ? 0.4072 0.3932 0.3635 -0.0021 0.0774 -0.1037 15 ARG A N 118 C CA . ARG A 15 ? 0.3815 0.3915 0.3313 -0.0026 0.0684 -0.0991 15 ARG A CA 119 C C . ARG A 15 ? 0.3712 0.3841 0.3180 0.0050 0.0652 -0.0838 15 ARG A C 120 O O . ARG A 15 ? 0.3599 0.3892 0.3026 0.0080 0.0617 -0.0813 15 ARG A O 121 C CB . ARG A 15 ? 0.3678 0.3861 0.3166 -0.0109 0.0629 -0.0997 15 ARG A CB 122 C CG . ARG A 15 ? 0.3717 0.3929 0.3240 -0.0192 0.0651 -0.1164 15 ARG A CG 123 C CD . ARG A 15 ? 0.3767 0.4079 0.3287 -0.0263 0.0595 -0.1165 15 ARG A CD 124 N NE . ARG A 15 ? 0.3738 0.4288 0.3179 -0.0252 0.0514 -0.1133 15 ARG A NE 125 C CZ . ARG A 15 ? 0.3578 0.4247 0.2993 -0.0284 0.0452 -0.1099 15 ARG A CZ 126 N NH1 . ARG A 15 ? 0.3181 0.3772 0.2649 -0.0336 0.0458 -0.1099 15 ARG A NH1 127 N NH2 . ARG A 15 ? 0.3167 0.4032 0.2502 -0.0260 0.0390 -0.1059 15 ARG A NH2 128 N N . VAL A 16 ? 0.3624 0.3605 0.3115 0.0080 0.0668 -0.0740 16 VAL A N 129 C CA . VAL A 16 ? 0.3529 0.3546 0.3000 0.0154 0.0639 -0.0606 16 VAL A CA 130 C C . VAL A 16 ? 0.3621 0.3680 0.3099 0.0239 0.0670 -0.0615 16 VAL A C 131 O O . VAL A 16 ? 0.3463 0.3688 0.2916 0.0265 0.0627 -0.0566 16 VAL A O 132 C CB . VAL A 16 ? 0.3575 0.3430 0.3063 0.0187 0.0658 -0.0505 16 VAL A CB 133 C CG1 . VAL A 16 ? 0.3417 0.3335 0.2891 0.0276 0.0632 -0.0389 16 VAL A CG1 134 C CG2 . VAL A 16 ? 0.3306 0.3161 0.2782 0.0110 0.0616 -0.0479 16 VAL A CG2 135 N N . ALA A 17 ? 0.3787 0.3694 0.3301 0.0279 0.0750 -0.0680 17 ALA A N 136 C CA . ALA A 17 ? 0.3932 0.3858 0.3460 0.0375 0.0790 -0.0690 17 ALA A CA 137 C C . ALA A 17 ? 0.3973 0.4099 0.3476 0.0356 0.0769 -0.0772 17 ALA A C 138 O O . ALA A 17 ? 0.3932 0.4191 0.3430 0.0420 0.0760 -0.0736 17 ALA A O 139 C CB . ALA A 17 ? 0.4181 0.3869 0.3752 0.0420 0.0891 -0.0749 17 ALA A CB 140 N N . ASP A 18 ? 0.3942 0.4105 0.3429 0.0270 0.0762 -0.0882 18 ASP A N 141 C CA . ASP A 18 ? 0.3991 0.4355 0.3441 0.0251 0.0742 -0.0960 18 ASP A CA 142 C C . ASP A 18 ? 0.3794 0.4363 0.3195 0.0246 0.0670 -0.0861 18 ASP A C 143 O O . ASP A 18 ? 0.3835 0.4553 0.3217 0.0283 0.0672 -0.0863 18 ASP A O 144 C CB . ASP A 18 ? 0.4002 0.4391 0.3440 0.0162 0.0740 -0.1096 18 ASP A CB 145 C CG . ASP A 18 ? 0.4227 0.4830 0.3615 0.0156 0.0726 -0.1182 18 ASP A CG 146 O OD1 . ASP A 18 ? 0.4332 0.5113 0.3661 0.0117 0.0663 -0.1150 18 ASP A OD1 147 O OD2 . ASP A 18 ? 0.4320 0.4913 0.3722 0.0198 0.0782 -0.1275 18 ASP A OD2 148 N N . LEU A 19 ? 0.3694 0.4265 0.3077 0.0199 0.0615 -0.0778 19 LEU A N 149 C CA . LEU A 19 ? 0.3553 0.4288 0.2894 0.0185 0.0555 -0.0685 19 LEU A CA 150 C C . LEU A 19 ? 0.3530 0.4298 0.2898 0.0252 0.0556 -0.0588 19 LEU A C 151 O O . LEU A 19 ? 0.3523 0.4452 0.2875 0.0263 0.0545 -0.0563 19 LEU A O 152 C CB . LEU A 19 ? 0.3450 0.4160 0.2769 0.0123 0.0502 -0.0629 19 LEU A CB 153 C CG . LEU A 19 ? 0.3278 0.4111 0.2557 0.0105 0.0446 -0.0527 19 LEU A CG 154 C CD1 . LEU A 19 ? 0.3397 0.4413 0.2624 0.0100 0.0442 -0.0545 19 LEU A CD1 155 C CD2 . LEU A 19 ? 0.3223 0.4020 0.2479 0.0049 0.0401 -0.0492 19 LEU A CD2 156 N N . LEU A 20 ? 0.3561 0.4190 0.2969 0.0294 0.0569 -0.0533 20 LEU A N 157 C CA . LEU A 20 ? 0.3572 0.4250 0.3012 0.0368 0.0568 -0.0450 20 LEU A CA 158 C C . LEU A 20 ? 0.3673 0.4471 0.3131 0.0429 0.0605 -0.0492 20 LEU A C 159 O O . LEU A 20 ? 0.3666 0.4626 0.3136 0.0448 0.0585 -0.0441 20 LEU A O 160 C CB . LEU A 20 ? 0.3637 0.4137 0.3110 0.0431 0.0597 -0.0406 20 LEU A CB 161 C CG . LEU A 20 ? 0.3561 0.4124 0.3066 0.0522 0.0592 -0.0318 20 LEU A CG 162 C CD1 . LEU A 20 ? 0.3465 0.4156 0.2958 0.0479 0.0521 -0.0237 20 LEU A CD1 163 C CD2 . LEU A 20 ? 0.3723 0.4095 0.3247 0.0604 0.0637 -0.0280 20 LEU A CD2 164 N N . GLY A 21 ? 0.3813 0.4532 0.3278 0.0455 0.0661 -0.0591 21 GLY A N 165 C CA . GLY A 21 ? 0.3950 0.4766 0.3433 0.0523 0.0705 -0.0642 21 GLY A CA 166 C C . GLY A 21 ? 0.3870 0.4912 0.3317 0.0482 0.0684 -0.0664 21 GLY A C 167 O O . GLY A 21 ? 0.3948 0.5111 0.3411 0.0536 0.0715 -0.0689 21 GLY A O 168 N N . ARG A 22 ? 0.3795 0.4894 0.3189 0.0393 0.0636 -0.0648 22 ARG A N 169 C CA . ARG A 22 ? 0.3740 0.5039 0.3085 0.0355 0.0622 -0.0652 22 ARG A CA 170 C C . ARG A 22 ? 0.3608 0.5023 0.2956 0.0329 0.0583 -0.0537 22 ARG A C 171 O O . ARG A 22 ? 0.3618 0.5195 0.2935 0.0304 0.0585 -0.0520 22 ARG A O 172 C CB . ARG A 22 ? 0.3747 0.5047 0.3022 0.0283 0.0599 -0.0707 22 ARG A CB 173 C CG . ARG A 22 ? 0.3899 0.5126 0.3171 0.0287 0.0637 -0.0847 22 ARG A CG 174 C CD . ARG A 22 ? 0.3915 0.5154 0.3132 0.0212 0.0601 -0.0894 22 ARG A CD 175 N NE . ARG A 22 ? 0.4079 0.5229 0.3312 0.0197 0.0634 -0.1038 22 ARG A NE 176 C CZ . ARG A 22 ? 0.4187 0.5432 0.3394 0.0204 0.0665 -0.1164 22 ARG A CZ 177 N NH1 . ARG A 22 ? 0.4427 0.5577 0.3662 0.0179 0.0697 -0.1305 22 ARG A NH1 178 N NH2 . ARG A 22 ? 0.4182 0.5618 0.3337 0.0233 0.0669 -0.1155 22 ARG A NH2 179 N N . MET A 23 ? 0.3435 0.4767 0.2821 0.0333 0.0555 -0.0461 23 MET A N 180 C CA . MET A 23 ? 0.3310 0.4720 0.2697 0.0286 0.0513 -0.0366 23 MET A CA 181 C C . MET A 23 ? 0.3272 0.4838 0.2720 0.0320 0.0523 -0.0324 23 MET A C 182 O O . MET A 23 ? 0.3393 0.4962 0.2897 0.0399 0.0545 -0.0334 23 MET A O 183 C CB . MET A 23 ? 0.3254 0.4522 0.2650 0.0269 0.0473 -0.0314 23 MET A CB 184 C CG . MET A 23 ? 0.3055 0.4196 0.2401 0.0221 0.0457 -0.0347 23 MET A CG 185 S SD . MET A 23 ? 0.3180 0.4154 0.2541 0.0211 0.0424 -0.0290 23 MET A SD 186 C CE . MET A 23 ? 0.2696 0.3770 0.2043 0.0155 0.0373 -0.0199 23 MET A CE 187 N N . THR A 24 ? 0.3161 0.4859 0.2600 0.0260 0.0511 -0.0276 24 THR A N 188 C CA . THR A 24 ? 0.3052 0.4915 0.2562 0.0267 0.0518 -0.0237 24 THR A CA 189 C C . THR A 24 ? 0.3008 0.4831 0.2566 0.0264 0.0475 -0.0182 24 THR A C 190 O O . THR A 24 ? 0.2949 0.4620 0.2472 0.0241 0.0442 -0.0163 24 THR A O 191 C CB . THR A 24 ? 0.3034 0.5032 0.2522 0.0188 0.0531 -0.0203 24 THR A CB 192 O OG1 . THR A 24 ? 0.2975 0.4885 0.2422 0.0112 0.0495 -0.0148 24 THR A OG1 193 C CG2 . THR A 24 ? 0.2977 0.5027 0.2395 0.0191 0.0571 -0.0250 24 THR A CG2 194 N N . LEU A 25 ? 0.2915 0.4893 0.2553 0.0286 0.0476 -0.0163 25 LEU A N 195 C CA . LEU A 25 ? 0.2868 0.4856 0.2552 0.0280 0.0432 -0.0119 25 LEU A CA 196 C C . LEU A 25 ? 0.2763 0.4689 0.2410 0.0174 0.0400 -0.0080 25 LEU A C 197 O O . LEU A 25 ? 0.2735 0.4548 0.2366 0.0168 0.0361 -0.0056 25 LEU A O 198 C CB . LEU A 25 ? 0.2854 0.5073 0.2638 0.0309 0.0438 -0.0117 25 LEU A CB 199 C CG . LEU A 25 ? 0.2843 0.5115 0.2677 0.0300 0.0388 -0.0085 25 LEU A CG 200 C CD1 . LEU A 25 ? 0.3065 0.5172 0.2866 0.0382 0.0360 -0.0065 25 LEU A CD1 201 C CD2 . LEU A 25 ? 0.2756 0.5300 0.2700 0.0325 0.0392 -0.0097 25 LEU A CD2 202 N N . ALA A 26 ? 0.2718 0.4711 0.2345 0.0096 0.0423 -0.0071 26 ALA A N 203 C CA . ALA A 26 ? 0.2693 0.4611 0.2276 0.0002 0.0406 -0.0030 26 ALA A CA 204 C C . ALA A 26 ? 0.2700 0.4418 0.2199 0.0003 0.0378 -0.0024 26 ALA A C 205 O O . ALA A 26 ? 0.2733 0.4358 0.2215 -0.0039 0.0345 0.0007 26 ALA A O 206 C CB . ALA A 26 ? 0.2731 0.4733 0.2290 -0.0061 0.0452 -0.0014 26 ALA A CB 207 N N . GLU A 27 ? 0.2723 0.4385 0.2173 0.0047 0.0395 -0.0063 27 GLU A N 208 C CA . GLU A 27 ? 0.2685 0.4186 0.2065 0.0045 0.0374 -0.0073 27 GLU A CA 209 C C . GLU A 27 ? 0.2704 0.4087 0.2109 0.0084 0.0344 -0.0072 27 GLU A C 210 O O . GLU A 27 ? 0.2591 0.3855 0.1961 0.0058 0.0315 -0.0055 27 GLU A O 211 C CB . GLU A 27 ? 0.2690 0.4192 0.2023 0.0075 0.0404 -0.0134 27 GLU A CB 212 C CG . GLU A 27 ? 0.2680 0.4278 0.1952 0.0034 0.0427 -0.0121 27 GLU A CG 213 C CD . GLU A 27 ? 0.2827 0.4485 0.2059 0.0070 0.0461 -0.0191 27 GLU A CD 214 O OE1 . GLU A 27 ? 0.2868 0.4527 0.2143 0.0127 0.0481 -0.0251 27 GLU A OE1 215 O OE2 . GLU A 27 ? 0.3042 0.4751 0.2196 0.0046 0.0471 -0.0187 27 GLU A OE2 216 N N . LYS A 28 ? 0.2725 0.4153 0.2191 0.0152 0.0356 -0.0085 28 LYS A N 217 C CA . LYS A 28 ? 0.2786 0.4120 0.2275 0.0204 0.0337 -0.0069 28 LYS A CA 218 C C . LYS A 28 ? 0.2762 0.4111 0.2265 0.0167 0.0293 -0.0020 28 LYS A C 219 O O . LYS A 28 ? 0.2684 0.3908 0.2157 0.0159 0.0268 -0.0001 28 LYS A O 220 C CB . LYS A 28 ? 0.2794 0.4191 0.2338 0.0302 0.0363 -0.0084 28 LYS A CB 221 C CG . LYS A 28 ? 0.2816 0.4130 0.2342 0.0351 0.0409 -0.0140 28 LYS A CG 222 C CD . LYS A 28 ? 0.2735 0.4095 0.2314 0.0459 0.0442 -0.0150 28 LYS A CD 223 C CE . LYS A 28 ? 0.2865 0.4152 0.2430 0.0497 0.0495 -0.0222 28 LYS A CE 224 N NZ . LYS A 28 ? 0.3081 0.4392 0.2695 0.0616 0.0534 -0.0228 28 LYS A NZ 225 N N . ILE A 29 ? 0.2724 0.4234 0.2277 0.0139 0.0288 -0.0007 29 ILE A N 226 C CA . ILE A 29 ? 0.2664 0.4206 0.2239 0.0093 0.0249 0.0022 29 ILE A CA 227 C C . ILE A 29 ? 0.2683 0.4106 0.2198 0.0012 0.0234 0.0041 29 ILE A C 228 O O . ILE A 29 ? 0.2718 0.4074 0.2221 -0.0006 0.0200 0.0060 29 ILE A O 229 C CB . ILE A 29 ? 0.2613 0.4370 0.2270 0.0070 0.0253 0.0015 29 ILE A CB 230 C CG1 . ILE A 29 ? 0.2617 0.4491 0.2334 0.0175 0.0252 0.0005 29 ILE A CG1 231 C CG2 . ILE A 29 ? 0.2577 0.4362 0.2256 -0.0012 0.0222 0.0028 29 ILE A CG2 232 C CD1 . ILE A 29 ? 0.2649 0.4775 0.2460 0.0171 0.0265 -0.0016 29 ILE A CD1 233 N N . GLY A 30 ? 0.2758 0.4159 0.2228 -0.0028 0.0259 0.0038 30 GLY A N 234 C CA . GLY A 30 ? 0.2712 0.3999 0.2114 -0.0083 0.0248 0.0060 30 GLY A CA 235 C C . GLY A 30 ? 0.2678 0.3818 0.2041 -0.0059 0.0220 0.0060 30 GLY A C 236 O O . GLY A 30 ? 0.2747 0.3814 0.2085 -0.0094 0.0195 0.0084 30 GLY A O 237 N N . GLN A 31 ? 0.2679 0.3771 0.2038 -0.0002 0.0231 0.0029 31 GLN A N 238 C CA . GLN A 31 ? 0.2756 0.3710 0.2088 0.0016 0.0216 0.0025 31 GLN A CA 239 C C . GLN A 31 ? 0.2807 0.3727 0.2158 0.0029 0.0188 0.0057 31 GLN A C 240 O O . GLN A 31 ? 0.2797 0.3618 0.2119 0.0014 0.0169 0.0070 31 GLN A O 241 C CB . GLN A 31 ? 0.2817 0.3719 0.2157 0.0070 0.0247 -0.0019 31 GLN A CB 242 C CG . GLN A 31 ? 0.2800 0.3702 0.2102 0.0052 0.0269 -0.0071 31 GLN A CG 243 C CD . GLN A 31 ? 0.2818 0.3670 0.2066 0.0001 0.0245 -0.0068 31 GLN A CD 244 O OE1 . GLN A 31 ? 0.2934 0.3686 0.2179 -0.0003 0.0232 -0.0068 31 GLN A OE1 245 N NE2 . GLN A 31 ? 0.2456 0.3384 0.1661 -0.0031 0.0243 -0.0061 31 GLN A NE2 246 N N . MET A 32 ? 0.2795 0.3820 0.2197 0.0058 0.0184 0.0068 32 MET A N 247 C CA . MET A 32 ? 0.2698 0.3734 0.2119 0.0084 0.0155 0.0094 32 MET A CA 248 C C . MET A 32 ? 0.2681 0.3745 0.2099 0.0013 0.0123 0.0106 32 MET A C 249 O O . MET A 32 ? 0.2660 0.3745 0.2087 0.0023 0.0094 0.0118 32 MET A O 250 C CB . MET A 32 ? 0.2745 0.3918 0.2223 0.0150 0.0161 0.0093 32 MET A CB 251 C CG . MET A 32 ? 0.2720 0.3852 0.2204 0.0236 0.0200 0.0082 32 MET A CG 252 S SD . MET A 32 ? 0.2859 0.4185 0.2414 0.0329 0.0207 0.0086 32 MET A SD 253 C CE . MET A 32 ? 0.2765 0.4131 0.2319 0.0369 0.0161 0.0129 32 MET A CE 254 N N . THR A 33 ? 0.2637 0.3700 0.2039 -0.0054 0.0133 0.0103 33 THR A N 255 C CA . THR A 33 ? 0.2623 0.3688 0.2024 -0.0125 0.0117 0.0113 33 THR A CA 256 C C . THR A 33 ? 0.2714 0.3636 0.2051 -0.0152 0.0107 0.0130 33 THR A C 257 O O . THR A 33 ? 0.2730 0.3599 0.2023 -0.0158 0.0123 0.0135 33 THR A O 258 C CB . THR A 33 ? 0.2647 0.3807 0.2079 -0.0182 0.0147 0.0110 33 THR A CB 259 O OG1 . THR A 33 ? 0.2463 0.3777 0.1961 -0.0150 0.0159 0.0089 33 THR A OG1 260 C CG2 . THR A 33 ? 0.2525 0.3686 0.1975 -0.0260 0.0142 0.0113 33 THR A CG2 261 N N . GLN A 34 ? 0.2684 0.3561 0.2015 -0.0163 0.0079 0.0136 34 GLN A N 262 C CA . GLN A 34 ? 0.2678 0.3438 0.1957 -0.0190 0.0069 0.0151 34 GLN A CA 263 C C . GLN A 34 ? 0.2725 0.3482 0.2015 -0.0254 0.0070 0.0152 34 GLN A C 264 O O . GLN A 34 ? 0.2751 0.3578 0.2086 -0.0271 0.0055 0.0130 34 GLN A O 265 C CB . GLN A 34 ? 0.2656 0.3348 0.1913 -0.0152 0.0045 0.0153 34 GLN A CB 266 C CG . GLN A 34 ? 0.2591 0.3175 0.1799 -0.0172 0.0035 0.0165 34 GLN A CG 267 C CD . GLN A 34 ? 0.2704 0.3239 0.1897 -0.0137 0.0018 0.0167 34 GLN A CD 268 O OE1 . GLN A 34 ? 0.2856 0.3412 0.2056 -0.0133 -0.0001 0.0164 34 GLN A OE1 269 N NE2 . GLN A 34 ? 0.2848 0.3327 0.2020 -0.0114 0.0027 0.0169 34 GLN A NE2 270 N N . ILE A 35 ? 0.2751 0.3431 0.2000 -0.0286 0.0090 0.0176 35 ILE A N 271 C CA . ILE A 35 ? 0.2814 0.3456 0.2070 -0.0349 0.0106 0.0182 35 ILE A CA 272 C C . ILE A 35 ? 0.2871 0.3374 0.2067 -0.0346 0.0101 0.0205 35 ILE A C 273 O O . ILE A 35 ? 0.2803 0.3258 0.1947 -0.0304 0.0092 0.0224 35 ILE A O 274 C CB . ILE A 35 ? 0.2827 0.3507 0.2095 -0.0394 0.0155 0.0203 35 ILE A CB 275 C CG1 . ILE A 35 ? 0.3002 0.3616 0.2192 -0.0369 0.0177 0.0250 35 ILE A CG1 276 C CG2 . ILE A 35 ? 0.2789 0.3625 0.2123 -0.0389 0.0161 0.0175 35 ILE A CG2 277 C CD1 . ILE A 35 ? 0.2891 0.3541 0.2075 -0.0404 0.0232 0.0282 35 ILE A CD1 278 N N . GLU A 36 ? 0.2976 0.3424 0.2187 -0.0393 0.0107 0.0195 36 GLU A N 279 C CA . GLU A 36 ? 0.3081 0.3390 0.2239 -0.0390 0.0111 0.0216 36 GLU A CA 280 C C . GLU A 36 ? 0.3177 0.3413 0.2278 -0.0384 0.0150 0.0276 36 GLU A C 281 O O . GLU A 36 ? 0.3225 0.3486 0.2339 -0.0421 0.0192 0.0296 36 GLU A O 282 C CB . GLU A 36 ? 0.3117 0.3381 0.2313 -0.0451 0.0122 0.0181 36 GLU A CB 283 C CG . GLU A 36 ? 0.3168 0.3386 0.2349 -0.0429 0.0087 0.0149 36 GLU A CG 284 C CD . GLU A 36 ? 0.3398 0.3469 0.2510 -0.0392 0.0095 0.0187 36 GLU A CD 285 O OE1 . GLU A 36 ? 0.3453 0.3446 0.2528 -0.0391 0.0132 0.0238 36 GLU A OE1 286 O OE2 . GLU A 36 ? 0.3791 0.3836 0.2883 -0.0359 0.0066 0.0168 36 GLU A OE2 287 N N . ARG A 37 ? 0.3139 0.3298 0.2175 -0.0333 0.0139 0.0306 37 ARG A N 288 C CA . ARG A 37 ? 0.3250 0.3338 0.2219 -0.0314 0.0176 0.0371 37 ARG A CA 289 C C . ARG A 37 ? 0.3400 0.3388 0.2376 -0.0370 0.0233 0.0398 37 ARG A C 290 O O . ARG A 37 ? 0.3547 0.3506 0.2482 -0.0370 0.0281 0.0458 37 ARG A O 291 C CB . ARG A 37 ? 0.3152 0.3182 0.2060 -0.0248 0.0153 0.0393 37 ARG A CB 292 C CG . ARG A 37 ? 0.2982 0.2921 0.1900 -0.0250 0.0138 0.0368 37 ARG A CG 293 C CD . ARG A 37 ? 0.2820 0.2683 0.1674 -0.0187 0.0137 0.0407 37 ARG A CD 294 N NE . ARG A 37 ? 0.2777 0.2541 0.1577 -0.0174 0.0188 0.0478 37 ARG A NE 295 C CZ . ARG A 37 ? 0.3112 0.2724 0.1906 -0.0195 0.0230 0.0494 37 ARG A CZ 296 N NH1 . ARG A 37 ? 0.3173 0.2679 0.1911 -0.0175 0.0286 0.0571 37 ARG A NH1 297 N NH2 . ARG A 37 ? 0.2999 0.2563 0.1843 -0.0235 0.0219 0.0432 37 ARG A NH2 298 N N . LEU A 38 ? 0.3478 0.3417 0.2506 -0.0422 0.0235 0.0352 38 LEU A N 299 C CA . LEU A 38 ? 0.3636 0.3460 0.2684 -0.0489 0.0297 0.0363 38 LEU A CA 300 C C . LEU A 38 ? 0.3629 0.3527 0.2728 -0.0557 0.0344 0.0369 38 LEU A C 301 O O . LEU A 38 ? 0.3706 0.3499 0.2804 -0.0607 0.0416 0.0405 38 LEU A O 302 C CB . LEU A 38 ? 0.3699 0.3470 0.2798 -0.0533 0.0284 0.0291 38 LEU A CB 303 C CG . LEU A 38 ? 0.4082 0.3723 0.3126 -0.0479 0.0268 0.0296 38 LEU A CG 304 C CD1 . LEU A 38 ? 0.3930 0.3567 0.3024 -0.0515 0.0242 0.0207 38 LEU A CD1 305 C CD2 . LEU A 38 ? 0.4397 0.3848 0.3383 -0.0467 0.0336 0.0368 38 LEU A CD2 306 N N . VAL A 39 ? 0.3471 0.3541 0.2612 -0.0556 0.0313 0.0336 39 VAL A N 307 C CA . VAL A 39 ? 0.3535 0.3703 0.2728 -0.0613 0.0358 0.0340 39 VAL A CA 308 C C . VAL A 39 ? 0.3548 0.3787 0.2684 -0.0561 0.0370 0.0395 39 VAL A C 309 O O . VAL A 39 ? 0.3557 0.3884 0.2724 -0.0598 0.0410 0.0405 39 VAL A O 310 C CB . VAL A 39 ? 0.3476 0.3811 0.2777 -0.0659 0.0327 0.0255 39 VAL A CB 311 C CG1 . VAL A 39 ? 0.3460 0.3748 0.2820 -0.0725 0.0325 0.0190 39 VAL A CG1 312 C CG2 . VAL A 39 ? 0.3082 0.3531 0.2377 -0.0584 0.0259 0.0229 39 VAL A CG2 313 N N . ALA A 40 ? 0.3552 0.3764 0.2607 -0.0479 0.0335 0.0425 40 ALA A N 314 C CA . ALA A 40 ? 0.3528 0.3828 0.2529 -0.0424 0.0333 0.0454 40 ALA A CA 315 C C . ALA A 40 ? 0.3740 0.3971 0.2653 -0.0404 0.0389 0.0542 40 ALA A C 316 O O . ALA A 40 ? 0.3842 0.3930 0.2704 -0.0390 0.0411 0.0592 40 ALA A O 317 C CB . ALA A 40 ? 0.3389 0.3718 0.2357 -0.0352 0.0268 0.0427 40 ALA A CB 318 N N . THR A 41 ? 0.3789 0.4128 0.2676 -0.0391 0.0414 0.0563 41 THR A N 319 C CA . THR A 41 ? 0.3899 0.4215 0.2701 -0.0371 0.0476 0.0651 41 THR A CA 320 C C . THR A 41 ? 0.3861 0.4344 0.2623 -0.0316 0.0452 0.0634 41 THR A C 321 O O . THR A 41 ? 0.3647 0.4241 0.2477 -0.0328 0.0418 0.0558 41 THR A O 322 C CB . THR A 41 ? 0.4079 0.4379 0.2942 -0.0463 0.0553 0.0669 41 THR A CB 323 O OG1 . THR A 41 ? 0.4510 0.4624 0.3347 -0.0492 0.0614 0.0736 41 THR A OG1 324 C CG2 . THR A 41 ? 0.3701 0.4126 0.2543 -0.0463 0.0597 0.0697 41 THR A CG2 325 N N . PRO A 42 ? 0.3896 0.4401 0.2544 -0.0252 0.0472 0.0700 42 PRO A N 326 C CA . PRO A 42 ? 0.3840 0.4516 0.2451 -0.0208 0.0456 0.0670 42 PRO A CA 327 C C . PRO A 42 ? 0.3728 0.4517 0.2406 -0.0258 0.0490 0.0634 42 PRO A C 328 O O . PRO A 42 ? 0.3525 0.4429 0.2242 -0.0244 0.0453 0.0555 42 PRO A O 329 C CB . PRO A 42 ? 0.4029 0.4708 0.2503 -0.0142 0.0493 0.0767 42 PRO A CB 330 C CG . PRO A 42 ? 0.4022 0.4539 0.2461 -0.0116 0.0487 0.0822 42 PRO A CG 331 C CD . PRO A 42 ? 0.4081 0.4467 0.2628 -0.0206 0.0508 0.0800 42 PRO A CD 332 N N . ASP A 43 ? 0.3849 0.4602 0.2546 -0.0316 0.0564 0.0690 43 ASP A N 333 C CA . ASP A 43 ? 0.3845 0.4718 0.2621 -0.0371 0.0603 0.0658 43 ASP A CA 334 C C . ASP A 43 ? 0.3622 0.4543 0.2529 -0.0410 0.0557 0.0562 43 ASP A C 335 O O . ASP A 43 ? 0.3477 0.4539 0.2431 -0.0402 0.0548 0.0504 43 ASP A O 336 C CB . ASP A 43 ? 0.4101 0.4911 0.2887 -0.0442 0.0699 0.0735 43 ASP A CB 337 C CG . ASP A 43 ? 0.4550 0.5377 0.3211 -0.0400 0.0766 0.0836 43 ASP A CG 338 O OD1 . ASP A 43 ? 0.5301 0.6007 0.3935 -0.0438 0.0847 0.0926 43 ASP A OD1 339 O OD2 . ASP A 43 ? 0.4884 0.5844 0.3471 -0.0329 0.0743 0.0824 43 ASP A OD2 340 N N . VAL A 44 ? 0.3544 0.4351 0.2503 -0.0446 0.0530 0.0545 44 VAL A N 341 C CA . VAL A 44 ? 0.3358 0.4217 0.2430 -0.0473 0.0485 0.0462 44 VAL A CA 342 C C . VAL A 44 ? 0.3280 0.4212 0.2347 -0.0403 0.0420 0.0402 44 VAL A C 343 O O . VAL A 44 ? 0.3152 0.4200 0.2290 -0.0399 0.0408 0.0346 44 VAL A O 344 C CB . VAL A 44 ? 0.3358 0.4084 0.2470 -0.0515 0.0464 0.0451 44 VAL A CB 345 C CG1 . VAL A 44 ? 0.3114 0.3903 0.2310 -0.0511 0.0400 0.0370 44 VAL A CG1 346 C CG2 . VAL A 44 ? 0.3431 0.4104 0.2591 -0.0608 0.0537 0.0480 44 VAL A CG2 347 N N . LEU A 45 ? 0.3283 0.4149 0.2269 -0.0347 0.0386 0.0414 45 LEU A N 348 C CA . LEU A 45 ? 0.3233 0.4139 0.2216 -0.0290 0.0332 0.0354 45 LEU A CA 349 C C . LEU A 45 ? 0.3278 0.4316 0.2248 -0.0260 0.0349 0.0323 45 LEU A C 350 O O . LEU A 45 ? 0.3109 0.4202 0.2126 -0.0235 0.0326 0.0258 45 LEU A O 351 C CB . LEU A 45 ? 0.3186 0.4012 0.2091 -0.0247 0.0299 0.0372 45 LEU A CB 352 C CG . LEU A 45 ? 0.3305 0.3999 0.2219 -0.0261 0.0274 0.0388 45 LEU A CG 353 C CD1 . LEU A 45 ? 0.3073 0.3714 0.1903 -0.0211 0.0253 0.0418 45 LEU A CD1 354 C CD2 . LEU A 45 ? 0.3009 0.3696 0.2001 -0.0268 0.0231 0.0327 45 LEU A CD2 355 N N . ARG A 46 ? 0.3450 0.4534 0.2350 -0.0255 0.0395 0.0372 46 ARG A N 356 C CA . ARG A 46 ? 0.3629 0.4850 0.2503 -0.0226 0.0419 0.0345 46 ARG A CA 357 C C . ARG A 46 ? 0.3449 0.4766 0.2418 -0.0259 0.0450 0.0316 46 ARG A C 358 O O . ARG A 46 ? 0.3358 0.4757 0.2369 -0.0228 0.0438 0.0247 46 ARG A O 359 C CB . ARG A 46 ? 0.3757 0.5003 0.2521 -0.0211 0.0465 0.0420 46 ARG A CB 360 C CG . ARG A 46 ? 0.4132 0.5520 0.2828 -0.0160 0.0475 0.0388 46 ARG A CG 361 C CD . ARG A 46 ? 0.4446 0.5868 0.3025 -0.0141 0.0527 0.0482 46 ARG A CD 362 N NE . ARG A 46 ? 0.5594 0.6941 0.4083 -0.0098 0.0496 0.0528 46 ARG A NE 363 C CZ . ARG A 46 ? 0.5999 0.7223 0.4442 -0.0104 0.0523 0.0630 46 ARG A CZ 364 N NH1 . ARG A 46 ? 0.5976 0.7123 0.4454 -0.0165 0.0588 0.0697 46 ARG A NH1 365 N NH2 . ARG A 46 ? 0.6218 0.7398 0.4580 -0.0048 0.0489 0.0662 46 ARG A NH2 366 N N . ASP A 47 ? 0.3454 0.4760 0.2464 -0.0321 0.0494 0.0364 47 ASP A N 367 C CA . ASP A 47 ? 0.3348 0.4780 0.2453 -0.0359 0.0532 0.0341 47 ASP A CA 368 C C . ASP A 47 ? 0.3161 0.4633 0.2372 -0.0350 0.0487 0.0270 47 ASP A C 369 O O . ASP A 47 ? 0.3126 0.4733 0.2403 -0.0337 0.0501 0.0228 47 ASP A O 370 C CB . ASP A 47 ? 0.3463 0.4867 0.2601 -0.0443 0.0593 0.0401 47 ASP A CB 371 C CG . ASP A 47 ? 0.3705 0.5080 0.2735 -0.0446 0.0659 0.0489 47 ASP A CG 372 O OD1 . ASP A 47 ? 0.3620 0.5053 0.2557 -0.0382 0.0660 0.0496 47 ASP A OD1 373 O OD2 . ASP A 47 ? 0.3750 0.5048 0.2791 -0.0514 0.0717 0.0552 47 ASP A OD2 374 N N . ASN A 48 ? 0.3022 0.4382 0.2244 -0.0348 0.0435 0.0260 48 ASN A N 375 C CA . ASN A 48 ? 0.2901 0.4295 0.2210 -0.0331 0.0393 0.0205 48 ASN A CA 376 C C . ASN A 48 ? 0.2860 0.4212 0.2142 -0.0256 0.0349 0.0163 48 ASN A C 377 O O . ASN A 48 ? 0.2883 0.4243 0.2223 -0.0228 0.0318 0.0130 48 ASN A O 378 C CB . ASN A 48 ? 0.2826 0.4152 0.2182 -0.0385 0.0372 0.0213 48 ASN A CB 379 C CG . ASN A 48 ? 0.2935 0.4313 0.2346 -0.0471 0.0424 0.0234 48 ASN A CG 380 O OD1 . ASN A 48 ? 0.2864 0.4393 0.2370 -0.0494 0.0439 0.0200 48 ASN A OD1 381 N ND2 . ASN A 48 ? 0.2676 0.3935 0.2032 -0.0517 0.0458 0.0291 48 ASN A ND2 382 N N . PHE A 49 ? 0.2880 0.4198 0.2078 -0.0224 0.0352 0.0164 49 PHE A N 383 C CA . PHE A 49 ? 0.2792 0.4072 0.1969 -0.0166 0.0323 0.0113 49 PHE A CA 384 C C . PHE A 49 ? 0.2799 0.3965 0.1996 -0.0160 0.0277 0.0109 49 PHE A C 385 O O . PHE A 49 ? 0.2759 0.3907 0.1992 -0.0120 0.0262 0.0070 49 PHE A O 386 C CB . PHE A 49 ? 0.2801 0.4178 0.2028 -0.0121 0.0342 0.0058 49 PHE A CB 387 C CG . PHE A 49 ? 0.2843 0.4355 0.2060 -0.0126 0.0392 0.0059 49 PHE A CG 388 C CD1 . PHE A 49 ? 0.2759 0.4385 0.2048 -0.0151 0.0421 0.0072 49 PHE A CD1 389 C CD2 . PHE A 49 ? 0.2796 0.4339 0.1931 -0.0107 0.0411 0.0042 49 PHE A CD2 390 C CE1 . PHE A 49 ? 0.2617 0.4379 0.1900 -0.0158 0.0476 0.0075 49 PHE A CE1 391 C CE2 . PHE A 49 ? 0.3052 0.4729 0.2168 -0.0107 0.0461 0.0045 49 PHE A CE2 392 C CZ . PHE A 49 ? 0.2940 0.4721 0.2130 -0.0133 0.0497 0.0065 49 PHE A CZ 393 N N . ILE A 50 ? 0.2834 0.3919 0.2004 -0.0197 0.0261 0.0152 50 ILE A N 394 C CA . ILE A 50 ? 0.2769 0.3762 0.1962 -0.0199 0.0222 0.0153 50 ILE A CA 395 C C . ILE A 50 ? 0.2820 0.3742 0.1988 -0.0158 0.0196 0.0122 50 ILE A C 396 O O . ILE A 50 ? 0.2930 0.3841 0.2042 -0.0147 0.0197 0.0112 50 ILE A O 397 C CB . ILE A 50 ? 0.2815 0.3731 0.1983 -0.0247 0.0219 0.0201 50 ILE A CB 398 C CG1 . ILE A 50 ? 0.2598 0.3574 0.1817 -0.0303 0.0251 0.0220 50 ILE A CG1 399 C CG2 . ILE A 50 ? 0.2574 0.3393 0.1747 -0.0241 0.0178 0.0197 50 ILE A CG2 400 C CD1 . ILE A 50 ? 0.2370 0.3437 0.1683 -0.0308 0.0238 0.0182 50 ILE A CD1 401 N N . GLY A 51 ? 0.2749 0.3636 0.1960 -0.0134 0.0177 0.0105 51 GLY A N 402 C CA . GLY A 51 ? 0.2708 0.3521 0.1910 -0.0101 0.0166 0.0075 51 GLY A CA 403 C C . GLY A 51 ? 0.2716 0.3436 0.1889 -0.0115 0.0138 0.0092 51 GLY A C 404 O O . GLY A 51 ? 0.2676 0.3349 0.1833 -0.0103 0.0135 0.0064 51 GLY A O 405 N N . SER A 52 ? 0.2732 0.3431 0.1903 -0.0141 0.0121 0.0128 52 SER A N 406 C CA . SER A 52 ? 0.2715 0.3331 0.1864 -0.0146 0.0096 0.0142 52 SER A CA 407 C C . SER A 52 ? 0.2760 0.3353 0.1892 -0.0182 0.0090 0.0177 52 SER A C 408 O O . SER A 52 ? 0.2719 0.3356 0.1879 -0.0210 0.0102 0.0186 52 SER A O 409 C CB . SER A 52 ? 0.2631 0.3214 0.1813 -0.0120 0.0084 0.0135 52 SER A CB 410 O OG . SER A 52 ? 0.2782 0.3294 0.1943 -0.0122 0.0065 0.0145 52 SER A OG 411 N N . LEU A 53 ? 0.2786 0.3311 0.1877 -0.0182 0.0076 0.0192 53 LEU A N 412 C CA . LEU A 53 ? 0.2801 0.3267 0.1876 -0.0208 0.0072 0.0221 53 LEU A CA 413 C C . LEU A 53 ? 0.2724 0.3131 0.1799 -0.0194 0.0046 0.0213 53 LEU A C 414 O O . LEU A 53 ? 0.2684 0.3089 0.1760 -0.0167 0.0035 0.0196 53 LEU A O 415 C CB . LEU A 53 ? 0.2886 0.3321 0.1901 -0.0207 0.0087 0.0259 53 LEU A CB 416 C CG . LEU A 53 ? 0.3265 0.3744 0.2267 -0.0227 0.0124 0.0286 53 LEU A CG 417 C CD1 . LEU A 53 ? 0.2840 0.3403 0.1820 -0.0198 0.0128 0.0267 53 LEU A CD1 418 C CD2 . LEU A 53 ? 0.3519 0.3922 0.2463 -0.0230 0.0145 0.0342 53 LEU A CD2 419 N N . LEU A 54 ? 0.2690 0.3049 0.1766 -0.0216 0.0041 0.0222 54 LEU A N 420 C CA . LEU A 54 ? 0.2631 0.2933 0.1694 -0.0200 0.0020 0.0216 54 LEU A CA 421 C C . LEU A 54 ? 0.2699 0.2918 0.1735 -0.0219 0.0028 0.0233 54 LEU A C 422 O O . LEU A 54 ? 0.2622 0.2822 0.1662 -0.0254 0.0052 0.0247 54 LEU A O 423 C CB . LEU A 54 ? 0.2542 0.2880 0.1642 -0.0196 0.0002 0.0191 54 LEU A CB 424 C CG . LEU A 54 ? 0.2585 0.2939 0.1711 -0.0231 -0.0003 0.0171 54 LEU A CG 425 C CD1 . LEU A 54 ? 0.2330 0.2711 0.1461 -0.0207 -0.0028 0.0150 54 LEU A CD1 426 C CD2 . LEU A 54 ? 0.2243 0.2681 0.1416 -0.0265 0.0012 0.0161 54 LEU A CD2 427 N N . SER A 55 ? 0.2744 0.2911 0.1757 -0.0194 0.0013 0.0232 55 SER A N 428 C CA . SER A 55 ? 0.2883 0.2963 0.1880 -0.0205 0.0018 0.0233 55 SER A CA 429 C C . SER A 55 ? 0.2860 0.2964 0.1884 -0.0211 -0.0004 0.0192 55 SER A C 430 O O . SER A 55 ? 0.2853 0.2992 0.1875 -0.0179 -0.0022 0.0185 55 SER A O 431 C CB . SER A 55 ? 0.2924 0.2950 0.1874 -0.0158 0.0014 0.0255 55 SER A CB 432 O OG . SER A 55 ? 0.3139 0.3142 0.2051 -0.0142 0.0036 0.0300 55 SER A OG 433 N N . GLY A 56 ? 0.2953 0.3049 0.2002 -0.0254 0.0002 0.0162 56 GLY A N 434 C CA . GLY A 56 ? 0.3001 0.3116 0.2060 -0.0255 -0.0019 0.0118 56 GLY A CA 435 C C . GLY A 56 ? 0.3103 0.3119 0.2122 -0.0231 -0.0017 0.0116 56 GLY A C 436 O O . GLY A 56 ? 0.3080 0.3014 0.2067 -0.0212 0.0001 0.0152 56 GLY A O 437 N N . GLY A 57 ? 0.3093 0.3130 0.2109 -0.0222 -0.0036 0.0075 57 GLY A N 438 C CA . GLY A 57 ? 0.3178 0.3129 0.2160 -0.0198 -0.0031 0.0063 57 GLY A CA 439 C C . GLY A 57 ? 0.3268 0.3084 0.2240 -0.0221 0.0004 0.0068 57 GLY A C 440 O O . GLY A 57 ? 0.3335 0.3124 0.2338 -0.0282 0.0023 0.0037 57 GLY A O 441 N N . GLY A 58 ? 0.3280 0.3017 0.2213 -0.0172 0.0016 0.0110 58 GLY A N 442 C CA . GLY A 58 ? 0.3362 0.2951 0.2271 -0.0170 0.0057 0.0135 58 GLY A CA 443 C C . GLY A 58 ? 0.3428 0.2981 0.2338 -0.0196 0.0089 0.0187 58 GLY A C 444 O O . GLY A 58 ? 0.3511 0.2925 0.2400 -0.0201 0.0134 0.0214 58 GLY A O 445 N N . SER A 59 ? 0.3321 0.2987 0.2249 -0.0209 0.0072 0.0203 59 SER A N 446 C CA . SER A 59 ? 0.3341 0.2996 0.2265 -0.0230 0.0103 0.0253 59 SER A CA 447 C C . SER A 59 ? 0.3353 0.3014 0.2222 -0.0158 0.0101 0.0317 59 SER A C 448 O O . SER A 59 ? 0.3344 0.3119 0.2215 -0.0133 0.0071 0.0318 59 SER A O 449 C CB . SER A 59 ? 0.3279 0.3066 0.2251 -0.0271 0.0087 0.0233 59 SER A CB 450 O OG . SER A 59 ? 0.3355 0.3138 0.2326 -0.0297 0.0123 0.0274 59 SER A OG 451 N N . VAL A 60 ? 0.3441 0.2981 0.2262 -0.0123 0.0136 0.0365 60 VAL A N 452 C CA . VAL A 60 ? 0.3430 0.2989 0.2193 -0.0038 0.0130 0.0421 60 VAL A CA 453 C C . VAL A 60 ? 0.3633 0.3108 0.2342 -0.0020 0.0182 0.0502 60 VAL A C 454 O O . VAL A 60 ? 0.3716 0.3064 0.2433 -0.0068 0.0233 0.0514 60 VAL A O 455 C CB . VAL A 60 ? 0.3397 0.2907 0.2141 0.0024 0.0117 0.0409 60 VAL A CB 456 C CG1 . VAL A 60 ? 0.3173 0.2774 0.1962 0.0007 0.0073 0.0339 60 VAL A CG1 457 C CG2 . VAL A 60 ? 0.3411 0.2731 0.2138 0.0022 0.0165 0.0416 60 VAL A CG2 458 N N . PRO A 61 ? 0.3745 0.3303 0.2403 0.0047 0.0173 0.0556 61 PRO A N 459 C CA . PRO A 61 ? 0.3927 0.3416 0.2518 0.0078 0.0226 0.0646 61 PRO A CA 460 C C . PRO A 61 ? 0.4294 0.3588 0.2836 0.0128 0.0277 0.0703 61 PRO A C 461 O O . PRO A 61 ? 0.4380 0.3539 0.2891 0.0112 0.0346 0.0765 61 PRO A O 462 C CB . PRO A 61 ? 0.3921 0.3577 0.2464 0.0151 0.0192 0.0676 61 PRO A CB 463 C CG . PRO A 61 ? 0.3653 0.3429 0.2237 0.0168 0.0129 0.0605 61 PRO A CG 464 C CD . PRO A 61 ? 0.3573 0.3301 0.2232 0.0091 0.0118 0.0533 61 PRO A CD 465 N N . ARG A 62 ? 0.4384 0.3657 0.2920 0.0188 0.0252 0.0683 62 ARG A N 466 C CA . ARG A 62 ? 0.4813 0.3893 0.3307 0.0246 0.0301 0.0727 62 ARG A CA 467 C C . ARG A 62 ? 0.4729 0.3831 0.3260 0.0266 0.0259 0.0654 62 ARG A C 468 O O . ARG A 62 ? 0.4553 0.3833 0.3111 0.0276 0.0197 0.0609 62 ARG A O 469 C CB . ARG A 62 ? 0.4897 0.3992 0.3298 0.0377 0.0314 0.0829 62 ARG A CB 470 C CG . ARG A 62 ? 0.5511 0.4524 0.3838 0.0400 0.0380 0.0937 62 ARG A CG 471 C CD . ARG A 62 ? 0.5444 0.4416 0.3670 0.0555 0.0403 0.1044 62 ARG A CD 472 N NE . ARG A 62 ? 0.5540 0.4715 0.3763 0.0647 0.0327 0.1015 62 ARG A NE 473 C CZ . ARG A 62 ? 0.5652 0.4808 0.3822 0.0778 0.0329 0.1065 62 ARG A CZ 474 N NH1 . ARG A 62 ? 0.6046 0.4965 0.4155 0.0843 0.0408 0.1152 62 ARG A NH1 475 N NH2 . ARG A 62 ? 0.5502 0.4876 0.3686 0.0846 0.0259 0.1026 62 ARG A NH2 476 N N . LYS A 63 ? 0.4945 0.3862 0.3474 0.0276 0.0299 0.0642 63 LYS A N 477 C CA . LYS A 63 ? 0.4981 0.3916 0.3521 0.0331 0.0268 0.0593 63 LYS A CA 478 C C . LYS A 63 ? 0.4837 0.3883 0.3324 0.0460 0.0243 0.0653 63 LYS A C 479 O O . LYS A 63 ? 0.4999 0.3987 0.3418 0.0536 0.0279 0.0748 63 LYS A O 480 C CB . LYS A 63 ? 0.5297 0.3996 0.3831 0.0334 0.0327 0.0576 63 LYS A CB 481 C CG . LYS A 63 ? 0.5859 0.4467 0.4455 0.0201 0.0350 0.0493 63 LYS A CG 482 C CD . LYS A 63 ? 0.6433 0.5093 0.5078 0.0169 0.0310 0.0381 63 LYS A CD 483 C CE . LYS A 63 ? 0.6283 0.5178 0.4967 0.0135 0.0236 0.0339 63 LYS A CE 484 N NZ . LYS A 63 ? 0.6569 0.5496 0.5290 0.0100 0.0211 0.0238 63 LYS A NZ 485 N N . GLY A 64 ? 0.4585 0.3804 0.3106 0.0483 0.0183 0.0599 64 GLY A N 486 C CA . GLY A 64 ? 0.4397 0.3764 0.2888 0.0597 0.0153 0.0635 64 GLY A CA 487 C C . GLY A 64 ? 0.4292 0.3833 0.2759 0.0616 0.0126 0.0677 64 GLY A C 488 O O . GLY A 64 ? 0.4394 0.4062 0.2826 0.0719 0.0107 0.0717 64 GLY A O 489 N N . ALA A 65 ? 0.4094 0.3660 0.2582 0.0520 0.0123 0.0662 65 ALA A N 490 C CA . ALA A 65 ? 0.3962 0.3696 0.2429 0.0527 0.0100 0.0687 65 ALA A CA 491 C C . ALA A 65 ? 0.3841 0.3814 0.2345 0.0558 0.0039 0.0634 65 ALA A C 492 O O . ALA A 65 ? 0.3760 0.3781 0.2332 0.0513 0.0013 0.0559 65 ALA A O 493 C CB . ALA A 65 ? 0.3782 0.3512 0.2285 0.0412 0.0105 0.0657 65 ALA A CB 494 N N . THR A 66 ? 0.3890 0.4019 0.2348 0.0636 0.0021 0.0673 66 THR A N 495 C CA . THR A 66 ? 0.3726 0.4109 0.2225 0.0657 -0.0035 0.0613 66 THR A CA 496 C C . THR A 66 ? 0.3586 0.4075 0.2145 0.0549 -0.0058 0.0539 66 THR A C 497 O O . THR A 66 ? 0.3550 0.3948 0.2100 0.0484 -0.0036 0.0550 66 THR A O 498 C CB . THR A 66 ? 0.3847 0.4387 0.2274 0.0776 -0.0048 0.0672 66 THR A CB 499 O OG1 . THR A 66 ? 0.3941 0.4498 0.2312 0.0760 -0.0035 0.0713 66 THR A OG1 500 C CG2 . THR A 66 ? 0.3972 0.4383 0.2325 0.0901 -0.0014 0.0766 66 THR A CG2 501 N N . ALA A 67 ? 0.3447 0.4127 0.2071 0.0532 -0.0098 0.0461 67 ALA A N 502 C CA . ALA A 67 ? 0.3301 0.4083 0.1981 0.0442 -0.0114 0.0388 67 ALA A CA 503 C C . ALA A 67 ? 0.3345 0.4186 0.1966 0.0449 -0.0110 0.0417 67 ALA A C 504 O O . ALA A 67 ? 0.3297 0.4096 0.1937 0.0373 -0.0098 0.0394 67 ALA A O 505 C CB . ALA A 67 ? 0.3201 0.4187 0.1955 0.0432 -0.0147 0.0304 67 ALA A CB 506 N N . LYS A 68 ? 0.3388 0.4331 0.1935 0.0548 -0.0118 0.0472 68 LYS A N 507 C CA . LYS A 68 ? 0.3415 0.4422 0.1888 0.0570 -0.0110 0.0511 68 LYS A CA 508 C C . LYS A 68 ? 0.3472 0.4266 0.1897 0.0536 -0.0059 0.0584 68 LYS A C 509 O O . LYS A 68 ? 0.3476 0.4300 0.1893 0.0487 -0.0049 0.0572 68 LYS A O 510 C CB A LYS A 68 ? 0.3593 0.4764 0.1982 0.0700 -0.0128 0.0566 68 LYS A CB 511 C CB B LYS A 68 ? 0.3545 0.4702 0.1933 0.0703 -0.0126 0.0571 68 LYS A CB 512 C CG A LYS A 68 ? 0.3591 0.5069 0.2019 0.0709 -0.0182 0.0471 68 LYS A CG 513 C CG B LYS A 68 ? 0.3479 0.4739 0.1776 0.0743 -0.0119 0.0616 68 LYS A CG 514 C CD A LYS A 68 ? 0.3755 0.5321 0.2203 0.0624 -0.0186 0.0399 68 LYS A CD 515 C CD B LYS A 68 ? 0.3501 0.4863 0.1694 0.0896 -0.0124 0.0708 68 LYS A CD 516 C CE A LYS A 68 ? 0.4027 0.5675 0.2358 0.0692 -0.0177 0.0466 68 LYS A CE 517 C CE B LYS A 68 ? 0.3398 0.4887 0.1485 0.0948 -0.0117 0.0759 68 LYS A CE 518 N NZ A LYS A 68 ? 0.4132 0.5776 0.2480 0.0600 -0.0163 0.0412 68 LYS A NZ 519 N NZ B LYS A 68 ? 0.3273 0.4549 0.1311 0.0899 -0.0055 0.0833 68 LYS A NZ 520 N N . GLU A 69 ? 0.3474 0.4063 0.1874 0.0559 -0.0022 0.0652 69 GLU A N 521 C CA . GLU A 69 ? 0.3546 0.3924 0.1929 0.0503 0.0031 0.0702 69 GLU A CA 522 C C . GLU A 69 ? 0.3412 0.3769 0.1876 0.0381 0.0027 0.0626 69 GLU A C 523 O O . GLU A 69 ? 0.3442 0.3766 0.1894 0.0334 0.0056 0.0644 69 GLU A O 524 C CB . GLU A 69 ? 0.3606 0.3764 0.1977 0.0526 0.0069 0.0752 69 GLU A CB 525 C CG . GLU A 69 ? 0.3963 0.4073 0.2235 0.0653 0.0099 0.0859 69 GLU A CG 526 C CD . GLU A 69 ? 0.4387 0.4248 0.2653 0.0667 0.0147 0.0898 69 GLU A CD 527 O OE1 . GLU A 69 ? 0.4510 0.4178 0.2782 0.0595 0.0201 0.0919 69 GLU A OE1 528 O OE2 . GLU A 69 ? 0.4414 0.4278 0.2676 0.0749 0.0134 0.0901 69 GLU A OE2 529 N N . TRP A 70 ? 0.3257 0.3642 0.1803 0.0337 -0.0004 0.0545 70 TRP A N 530 C CA . TRP A 70 ? 0.3097 0.3479 0.1716 0.0240 -0.0009 0.0477 70 TRP A CA 531 C C . TRP A 70 ? 0.3099 0.3633 0.1723 0.0218 -0.0023 0.0438 70 TRP A C 532 O O . TRP A 70 ? 0.2960 0.3465 0.1601 0.0161 -0.0005 0.0427 70 TRP A O 533 C CB . TRP A 70 ? 0.2979 0.3369 0.1672 0.0211 -0.0034 0.0410 70 TRP A CB 534 C CG . TRP A 70 ? 0.2971 0.3201 0.1675 0.0199 -0.0017 0.0423 70 TRP A CG 535 C CD1 . TRP A 70 ? 0.3040 0.3204 0.1718 0.0259 -0.0013 0.0451 70 TRP A CD1 536 C CD2 . TRP A 70 ? 0.2984 0.3112 0.1727 0.0127 -0.0004 0.0399 70 TRP A CD2 537 N NE1 . TRP A 70 ? 0.2915 0.2935 0.1614 0.0222 0.0005 0.0439 70 TRP A NE1 538 C CE2 . TRP A 70 ? 0.3094 0.3102 0.1834 0.0141 0.0007 0.0407 70 TRP A CE2 539 C CE3 . TRP A 70 ? 0.2757 0.2897 0.1539 0.0059 -0.0001 0.0369 70 TRP A CE3 540 C CZ2 . TRP A 70 ? 0.2941 0.2855 0.1713 0.0082 0.0018 0.0378 70 TRP A CZ2 541 C CZ3 . TRP A 70 ? 0.2854 0.2908 0.1670 0.0009 0.0008 0.0350 70 TRP A CZ3 542 C CH2 . TRP A 70 ? 0.2952 0.2900 0.1762 0.0018 0.0016 0.0351 70 TRP A CH2 543 N N . GLN A 71 ? 0.3121 0.3828 0.1732 0.0266 -0.0053 0.0410 71 GLN A N 544 C CA . GLN A 71 ? 0.3102 0.3967 0.1715 0.0247 -0.0066 0.0358 71 GLN A CA 545 C C . GLN A 71 ? 0.3167 0.4025 0.1704 0.0263 -0.0036 0.0419 71 GLN A C 546 O O . GLN A 71 ? 0.3149 0.4039 0.1705 0.0212 -0.0026 0.0381 71 GLN A O 547 C CB . GLN A 71 ? 0.3091 0.4166 0.1704 0.0297 -0.0104 0.0310 71 GLN A CB 548 C CG . GLN A 71 ? 0.3103 0.4221 0.1810 0.0262 -0.0127 0.0229 71 GLN A CG 549 C CD . GLN A 71 ? 0.3174 0.4535 0.1906 0.0280 -0.0162 0.0150 71 GLN A CD 550 O OE1 . GLN A 71 ? 0.3128 0.4631 0.1806 0.0316 -0.0173 0.0146 71 GLN A OE1 551 N NE2 . GLN A 71 ? 0.3089 0.4510 0.1904 0.0252 -0.0176 0.0082 71 GLN A NE2 552 N N . ASP A 72 ? 0.3297 0.4108 0.1748 0.0336 -0.0016 0.0517 72 ASP A N 553 C CA . ASP A 72 ? 0.3500 0.4290 0.1866 0.0359 0.0025 0.0596 72 ASP A CA 554 C C . ASP A 72 ? 0.3465 0.4098 0.1868 0.0274 0.0068 0.0608 72 ASP A C 555 O O . ASP A 72 ? 0.3486 0.4156 0.1868 0.0248 0.0093 0.0616 72 ASP A O 556 C CB . ASP A 72 ? 0.3679 0.4408 0.1946 0.0460 0.0050 0.0713 72 ASP A CB 557 C CG . ASP A 72 ? 0.3968 0.4901 0.2183 0.0564 0.0007 0.0711 72 ASP A CG 558 O OD1 . ASP A 72 ? 0.4073 0.5217 0.2319 0.0551 -0.0037 0.0619 72 ASP A OD1 559 O OD2 . ASP A 72 ? 0.4050 0.4939 0.2196 0.0662 0.0019 0.0799 72 ASP A OD2 560 N N . MET A 73 ? 0.3441 0.3916 0.1900 0.0232 0.0076 0.0604 73 MET A N 561 C CA . MET A 73 ? 0.3397 0.3751 0.1906 0.0148 0.0109 0.0598 73 MET A CA 562 C C . MET A 73 ? 0.3241 0.3693 0.1816 0.0087 0.0090 0.0515 73 MET A C 563 O O . MET A 73 ? 0.3205 0.3669 0.1782 0.0052 0.0119 0.0523 73 MET A O 564 C CB . MET A 73 ? 0.3414 0.3615 0.1973 0.0118 0.0111 0.0589 73 MET A CB 565 C CG . MET A 73 ? 0.3413 0.3519 0.2025 0.0033 0.0143 0.0577 73 MET A CG 566 S SD . MET A 73 ? 0.3362 0.3357 0.2048 -0.0014 0.0128 0.0525 73 MET A SD 567 C CE . MET A 73 ? 0.3260 0.3386 0.2001 -0.0012 0.0068 0.0441 73 MET A CE 568 N N . VAL A 74 ? 0.3147 0.3664 0.1778 0.0079 0.0048 0.0438 74 VAL A N 569 C CA . VAL A 74 ? 0.2994 0.3581 0.1689 0.0030 0.0036 0.0360 74 VAL A CA 570 C C . VAL A 74 ? 0.3031 0.3755 0.1689 0.0044 0.0042 0.0343 74 VAL A C 571 O O . VAL A 74 ? 0.3081 0.3819 0.1763 0.0007 0.0062 0.0321 74 VAL A O 572 C CB . VAL A 74 ? 0.2921 0.3535 0.1679 0.0021 0.0003 0.0290 74 VAL A CB 573 C CG1 . VAL A 74 ? 0.2826 0.3481 0.1645 -0.0024 0.0004 0.0218 74 VAL A CG1 574 C CG2 . VAL A 74 ? 0.2692 0.3180 0.1479 0.0009 0.0000 0.0306 74 VAL A CG2 575 N N . ASP A 75 ? 0.3081 0.3919 0.1678 0.0103 0.0025 0.0350 75 ASP A N 576 C CA . ASP A 75 ? 0.3100 0.4090 0.1646 0.0125 0.0028 0.0331 75 ASP A CA 577 C C . ASP A 75 ? 0.3245 0.4199 0.1734 0.0124 0.0076 0.0406 75 ASP A C 578 O O . ASP A 75 ? 0.3164 0.4207 0.1648 0.0109 0.0090 0.0371 75 ASP A O 579 C CB . ASP A 75 ? 0.3171 0.4309 0.1650 0.0201 -0.0001 0.0336 75 ASP A CB 580 C CG . ASP A 75 ? 0.3207 0.4460 0.1753 0.0189 -0.0045 0.0230 75 ASP A CG 581 O OD1 . ASP A 75 ? 0.3146 0.4360 0.1781 0.0122 -0.0046 0.0151 75 ASP A OD1 582 O OD2 . ASP A 75 ? 0.3482 0.4867 0.1992 0.0249 -0.0075 0.0227 75 ASP A OD2 583 N N . GLY A 76 ? 0.3305 0.4126 0.1755 0.0138 0.0108 0.0504 76 GLY A N 584 C CA . GLY A 76 ? 0.3423 0.4189 0.1831 0.0124 0.0167 0.0581 76 GLY A CA 585 C C . GLY A 76 ? 0.3374 0.4116 0.1863 0.0044 0.0187 0.0534 76 GLY A C 586 O O . GLY A 76 ? 0.3444 0.4252 0.1912 0.0032 0.0220 0.0544 76 GLY A O 587 N N . PHE A 77 ? 0.3280 0.3941 0.1859 -0.0004 0.0166 0.0486 77 PHE A N 588 C CA . PHE A 77 ? 0.3256 0.3919 0.1919 -0.0065 0.0173 0.0431 77 PHE A CA 589 C C . PHE A 77 ? 0.3206 0.4001 0.1890 -0.0060 0.0157 0.0351 77 PHE A C 590 O O . PHE A 77 ? 0.3180 0.4024 0.1889 -0.0084 0.0182 0.0334 77 PHE A O 591 C CB . PHE A 77 ? 0.3194 0.3761 0.1934 -0.0097 0.0148 0.0399 77 PHE A CB 592 C CG . PHE A 77 ? 0.3306 0.3736 0.2044 -0.0117 0.0169 0.0455 77 PHE A CG 593 C CD1 . PHE A 77 ? 0.3300 0.3648 0.2058 -0.0111 0.0142 0.0443 77 PHE A CD1 594 C CD2 . PHE A 77 ? 0.3481 0.3861 0.2199 -0.0144 0.0224 0.0515 77 PHE A CD2 595 C CE1 . PHE A 77 ? 0.3396 0.3611 0.2155 -0.0132 0.0164 0.0480 77 PHE A CE1 596 C CE2 . PHE A 77 ? 0.3522 0.3759 0.2247 -0.0172 0.0251 0.0554 77 PHE A CE2 597 C CZ . PHE A 77 ? 0.3333 0.3487 0.2077 -0.0164 0.0220 0.0532 77 PHE A CZ 598 N N . GLN A 78 ? 0.3205 0.4060 0.1887 -0.0032 0.0118 0.0296 78 GLN A N 599 C CA . GLN A 78 ? 0.3196 0.4166 0.1898 -0.0031 0.0107 0.0207 78 GLN A CA 600 C C . GLN A 78 ? 0.3320 0.4415 0.1954 -0.0007 0.0131 0.0213 78 GLN A C 601 O O . GLN A 78 ? 0.3203 0.4358 0.1864 -0.0022 0.0147 0.0155 78 GLN A O 602 C CB . GLN A 78 ? 0.3145 0.4168 0.1857 -0.0014 0.0067 0.0145 78 GLN A CB 603 C CG . GLN A 78 ? 0.3112 0.4208 0.1876 -0.0033 0.0063 0.0033 78 GLN A CG 604 C CD . GLN A 78 ? 0.3122 0.4111 0.1972 -0.0071 0.0078 0.0004 78 GLN A CD 605 O OE1 . GLN A 78 ? 0.3074 0.4034 0.1937 -0.0081 0.0103 0.0030 78 GLN A OE1 606 N NE2 . GLN A 78 ? 0.3094 0.4035 0.2003 -0.0089 0.0065 -0.0045 78 GLN A NE2 607 N N . LYS A 79 ? 0.3489 0.4624 0.2028 0.0038 0.0137 0.0285 79 LYS A N 608 C CA . LYS A 79 ? 0.3658 0.4922 0.2113 0.0071 0.0163 0.0305 79 LYS A CA 609 C C . LYS A 79 ? 0.3597 0.4839 0.2076 0.0033 0.0213 0.0325 79 LYS A C 610 O O . LYS A 79 ? 0.3556 0.4916 0.2022 0.0037 0.0229 0.0278 79 LYS A O 611 C CB . LYS A 79 ? 0.3917 0.5186 0.2262 0.0132 0.0176 0.0416 79 LYS A CB 612 C CG . LYS A 79 ? 0.4421 0.5818 0.2706 0.0199 0.0131 0.0395 79 LYS A CG 613 C CD . LYS A 79 ? 0.5180 0.6619 0.3329 0.0280 0.0157 0.0516 79 LYS A CD 614 C CE . LYS A 79 ? 0.5609 0.7116 0.3688 0.0286 0.0211 0.0560 79 LYS A CE 615 N NZ . LYS A 79 ? 0.6033 0.7672 0.3961 0.0387 0.0224 0.0646 79 LYS A NZ 616 N N . ALA A 80 ? 0.3548 0.4652 0.2069 -0.0007 0.0239 0.0387 80 ALA A N 617 C CA . ALA A 80 ? 0.3606 0.4702 0.2168 -0.0052 0.0287 0.0404 80 ALA A CA 618 C C . ALA A 80 ? 0.3511 0.4660 0.2160 -0.0075 0.0275 0.0303 80 ALA A C 619 O O . ALA A 80 ? 0.3565 0.4809 0.2215 -0.0076 0.0306 0.0281 80 ALA A O 620 C CB . ALA A 80 ? 0.3600 0.4546 0.2205 -0.0099 0.0312 0.0469 80 ALA A CB 621 N N . CYS A 81 ? 0.3425 0.4512 0.2143 -0.0085 0.0234 0.0246 81 CYS A N 622 C CA . CYS A 81 ? 0.3360 0.4471 0.2157 -0.0095 0.0228 0.0160 81 CYS A CA 623 C C . CYS A 81 ? 0.3422 0.4651 0.2189 -0.0066 0.0228 0.0081 81 CYS A C 624 O O . CYS A 81 ? 0.3501 0.4782 0.2305 -0.0065 0.0250 0.0027 81 CYS A O 625 C CB . CYS A 81 ? 0.3254 0.4263 0.2116 -0.0106 0.0193 0.0130 81 CYS A CB 626 S SG . CYS A 81 ? 0.3211 0.4101 0.2111 -0.0142 0.0191 0.0200 81 CYS A SG 627 N N . MET A 82 ? 0.3416 0.4700 0.2117 -0.0039 0.0204 0.0068 82 MET A N 628 C CA . MET A 82 ? 0.3430 0.4844 0.2102 -0.0017 0.0200 -0.0022 82 MET A CA 629 C C . MET A 82 ? 0.3456 0.4995 0.2062 0.0004 0.0239 -0.0004 82 MET A C 630 O O . MET A 82 ? 0.3500 0.5150 0.2094 0.0018 0.0246 -0.0092 82 MET A O 631 C CB . MET A 82 ? 0.3444 0.4924 0.2068 0.0007 0.0160 -0.0049 82 MET A CB 632 C CG . MET A 82 ? 0.3581 0.4972 0.2276 -0.0015 0.0126 -0.0093 82 MET A CG 633 S SD . MET A 82 ? 0.4238 0.5564 0.3044 -0.0052 0.0140 -0.0208 82 MET A SD 634 C CE . MET A 82 ? 0.4153 0.5652 0.2932 -0.0044 0.0139 -0.0341 82 MET A CE 635 N N . SER A 83 ? 0.3447 0.4963 0.2011 0.0002 0.0271 0.0106 83 SER A N 636 C CA . SER A 83 ? 0.3529 0.5159 0.2025 0.0019 0.0319 0.0143 83 SER A CA 637 C C . SER A 83 ? 0.3422 0.5069 0.1992 -0.0008 0.0360 0.0115 83 SER A C 638 O O . SER A 83 ? 0.3506 0.5261 0.2032 0.0004 0.0404 0.0130 83 SER A O 639 C CB . SER A 83 ? 0.3635 0.5226 0.2051 0.0028 0.0349 0.0281 83 SER A CB 640 O OG . SER A 83 ? 0.3846 0.5305 0.2333 -0.0024 0.0376 0.0341 83 SER A OG 641 N N . THR A 84 ? 0.3177 0.4730 0.1855 -0.0037 0.0347 0.0076 84 THR A N 642 C CA . THR A 84 ? 0.3114 0.4701 0.1868 -0.0047 0.0379 0.0042 84 THR A CA 643 C C . THR A 84 ? 0.3157 0.4857 0.1898 -0.0013 0.0391 -0.0063 84 THR A C 644 O O . THR A 84 ? 0.3047 0.4780 0.1743 0.0008 0.0365 -0.0128 84 THR A O 645 C CB . THR A 84 ? 0.2988 0.4462 0.1852 -0.0067 0.0358 0.0021 84 THR A CB 646 O OG1 . THR A 84 ? 0.3001 0.4413 0.1882 -0.0052 0.0320 -0.0051 84 THR A OG1 647 C CG2 . THR A 84 ? 0.2950 0.4323 0.1832 -0.0106 0.0348 0.0109 84 THR A CG2 648 N N . ARG A 85 ? 0.3162 0.4928 0.1949 -0.0008 0.0431 -0.0086 85 ARG A N 649 C CA . ARG A 85 ? 0.3245 0.5105 0.2032 0.0027 0.0451 -0.0192 85 ARG A CA 650 C C . ARG A 85 ? 0.3221 0.5004 0.2044 0.0039 0.0419 -0.0300 85 ARG A C 651 O O . ARG A 85 ? 0.3262 0.5118 0.2043 0.0058 0.0420 -0.0392 85 ARG A O 652 C CB . ARG A 85 ? 0.3231 0.5137 0.2098 0.0035 0.0493 -0.0200 85 ARG A CB 653 C CG . ARG A 85 ? 0.3221 0.5227 0.2085 0.0077 0.0524 -0.0304 85 ARG A CG 654 C CD . ARG A 85 ? 0.3228 0.5282 0.2177 0.0094 0.0563 -0.0307 85 ARG A CD 655 N NE . ARG A 85 ? 0.3173 0.5106 0.2224 0.0108 0.0545 -0.0326 85 ARG A NE 656 C CZ . ARG A 85 ? 0.3071 0.4971 0.2175 0.0157 0.0560 -0.0413 85 ARG A CZ 657 N NH1 . ARG A 85 ? 0.3071 0.5045 0.2141 0.0192 0.0592 -0.0507 85 ARG A NH1 658 N NH2 . ARG A 85 ? 0.3167 0.4957 0.2352 0.0177 0.0547 -0.0405 85 ARG A NH2 659 N N . LEU A 86 ? 0.3163 0.4803 0.2064 0.0025 0.0397 -0.0290 86 LEU A N 660 C CA . LEU A 86 ? 0.3200 0.4742 0.2146 0.0030 0.0380 -0.0379 86 LEU A CA 661 C C . LEU A 86 ? 0.3219 0.4704 0.2135 0.0005 0.0336 -0.0377 86 LEU A C 662 O O . LEU A 86 ? 0.3321 0.4755 0.2264 -0.0001 0.0328 -0.0465 86 LEU A O 663 C CB . LEU A 86 ? 0.3081 0.4506 0.2125 0.0043 0.0390 -0.0373 86 LEU A CB 664 C CG . LEU A 86 ? 0.3130 0.4617 0.2220 0.0082 0.0434 -0.0391 86 LEU A CG 665 C CD1 . LEU A 86 ? 0.2838 0.4220 0.2015 0.0107 0.0436 -0.0368 86 LEU A CD1 666 C CD2 . LEU A 86 ? 0.3183 0.4722 0.2260 0.0113 0.0469 -0.0508 86 LEU A CD2 667 N N . GLY A 87 ? 0.3168 0.4659 0.2036 -0.0010 0.0313 -0.0279 87 GLY A N 668 C CA . GLY A 87 ? 0.3183 0.4635 0.2021 -0.0024 0.0270 -0.0265 87 GLY A CA 669 C C . GLY A 87 ? 0.3144 0.4450 0.2060 -0.0042 0.0251 -0.0288 87 GLY A C 670 O O . GLY A 87 ? 0.3197 0.4491 0.2119 -0.0053 0.0232 -0.0352 87 GLY A O 671 N N . ILE A 88 ? 0.3037 0.4247 0.2013 -0.0046 0.0260 -0.0238 88 ILE A N 672 C CA . ILE A 88 ? 0.2979 0.4054 0.2017 -0.0055 0.0246 -0.0243 88 ILE A CA 673 C C . ILE A 88 ? 0.2982 0.4015 0.1993 -0.0075 0.0209 -0.0171 88 ILE A C 674 O O . ILE A 88 ? 0.2950 0.3985 0.1943 -0.0081 0.0205 -0.0090 88 ILE A O 675 C CB . ILE A 88 ? 0.2974 0.3984 0.2080 -0.0037 0.0266 -0.0219 88 ILE A CB 676 C CG1 . ILE A 88 ? 0.2930 0.3991 0.2059 -0.0005 0.0308 -0.0284 88 ILE A CG1 677 C CG2 . ILE A 88 ? 0.2789 0.3660 0.1944 -0.0038 0.0256 -0.0218 88 ILE A CG2 678 C CD1 . ILE A 88 ? 0.2933 0.3975 0.2125 0.0030 0.0328 -0.0253 88 ILE A CD1 679 N N . PRO A 89 ? 0.2989 0.3987 0.2002 -0.0087 0.0186 -0.0206 89 PRO A N 680 C CA . PRO A 89 ? 0.2936 0.3899 0.1924 -0.0096 0.0153 -0.0141 89 PRO A CA 681 C C . PRO A 89 ? 0.2917 0.3768 0.1947 -0.0103 0.0149 -0.0079 89 PRO A C 682 O O . PRO A 89 ? 0.2929 0.3715 0.2016 -0.0099 0.0163 -0.0102 89 PRO A O 683 C CB . PRO A 89 ? 0.2946 0.3910 0.1949 -0.0109 0.0136 -0.0209 89 PRO A CB 684 C CG . PRO A 89 ? 0.3008 0.3940 0.2069 -0.0117 0.0167 -0.0299 89 PRO A CG 685 C CD . PRO A 89 ? 0.2989 0.3982 0.2033 -0.0097 0.0194 -0.0311 89 PRO A CD 686 N N . MET A 90 ? 0.2891 0.3722 0.1891 -0.0109 0.0132 -0.0005 90 MET A N 687 C CA . MET A 90 ? 0.2891 0.3631 0.1926 -0.0118 0.0122 0.0039 90 MET A CA 688 C C . MET A 90 ? 0.2895 0.3569 0.1946 -0.0120 0.0102 0.0021 90 MET A C 689 O O . MET A 90 ? 0.2977 0.3686 0.2007 -0.0120 0.0090 -0.0011 90 MET A O 690 C CB . MET A 90 ? 0.2876 0.3606 0.1881 -0.0132 0.0120 0.0112 90 MET A CB 691 C CG . MET A 90 ? 0.2959 0.3682 0.1899 -0.0125 0.0106 0.0149 90 MET A CG 692 S SD . MET A 90 ? 0.3057 0.3683 0.2011 -0.0125 0.0074 0.0161 90 MET A SD 693 C CE . MET A 90 ? 0.2832 0.3520 0.1728 -0.0094 0.0055 0.0151 90 MET A CE 694 N N . ILE A 91 ? 0.2850 0.3449 0.1940 -0.0121 0.0099 0.0039 91 ILE A N 695 C CA . ILE A 91 ? 0.2800 0.3335 0.1902 -0.0123 0.0084 0.0039 91 ILE A CA 696 C C . ILE A 91 ? 0.2804 0.3304 0.1886 -0.0128 0.0063 0.0097 91 ILE A C 697 O O . ILE A 91 ? 0.2872 0.3369 0.1965 -0.0132 0.0065 0.0124 91 ILE A O 698 C CB . ILE A 91 ? 0.2833 0.3304 0.1985 -0.0113 0.0104 0.0018 91 ILE A CB 699 C CG1 . ILE A 91 ? 0.2890 0.3301 0.2053 -0.0120 0.0099 0.0016 91 ILE A CG1 700 C CG2 . ILE A 91 ? 0.2555 0.3016 0.1729 -0.0092 0.0110 0.0053 91 ILE A CG2 701 C CD1 . ILE A 91 ? 0.2752 0.3086 0.1957 -0.0110 0.0134 0.0001 91 ILE A CD1 702 N N . TYR A 92 ? 0.2763 0.3248 0.1819 -0.0128 0.0045 0.0107 92 TYR A N 703 C CA . TYR A 92 ? 0.2750 0.3187 0.1784 -0.0129 0.0030 0.0154 92 TYR A CA 704 C C . TYR A 92 ? 0.2686 0.3070 0.1743 -0.0126 0.0020 0.0150 92 TYR A C 705 O O . TYR A 92 ? 0.2636 0.3023 0.1703 -0.0121 0.0019 0.0126 92 TYR A O 706 C CB . TYR A 92 ? 0.2747 0.3201 0.1728 -0.0116 0.0021 0.0177 92 TYR A CB 707 C CG . TYR A 92 ? 0.2790 0.3177 0.1742 -0.0117 0.0021 0.0229 92 TYR A CG 708 C CD1 . TYR A 92 ? 0.2753 0.3136 0.1669 -0.0123 0.0041 0.0269 92 TYR A CD1 709 C CD2 . TYR A 92 ? 0.2679 0.3001 0.1639 -0.0115 0.0009 0.0234 92 TYR A CD2 710 C CE1 . TYR A 92 ? 0.2786 0.3083 0.1682 -0.0131 0.0054 0.0312 92 TYR A CE1 711 C CE2 . TYR A 92 ? 0.2796 0.3043 0.1734 -0.0120 0.0015 0.0268 92 TYR A CE2 712 C CZ . TYR A 92 ? 0.2961 0.3188 0.1870 -0.0131 0.0040 0.0306 92 TYR A CZ 713 O OH . TYR A 92 ? 0.3099 0.3230 0.1991 -0.0142 0.0057 0.0336 92 TYR A OH 714 N N . GLY A 93 ? 0.2654 0.3005 0.1721 -0.0130 0.0016 0.0170 93 GLY A N 715 C CA . GLY A 93 ? 0.2623 0.2936 0.1700 -0.0120 0.0008 0.0171 93 GLY A CA 716 C C . GLY A 93 ? 0.2644 0.2918 0.1696 -0.0122 -0.0008 0.0187 93 GLY A C 717 O O . GLY A 93 ? 0.2674 0.2932 0.1709 -0.0136 -0.0009 0.0202 93 GLY A O 718 N N . ILE A 94 ? 0.2724 0.2976 0.1775 -0.0108 -0.0013 0.0184 94 ILE A N 719 C CA . ILE A 94 ? 0.2742 0.2957 0.1770 -0.0104 -0.0026 0.0191 94 ILE A CA 720 C C . ILE A 94 ? 0.2733 0.2944 0.1764 -0.0087 -0.0027 0.0186 94 ILE A C 721 O O . ILE A 94 ? 0.2718 0.2940 0.1767 -0.0078 -0.0013 0.0184 94 ILE A O 722 C CB . ILE A 94 ? 0.2760 0.2962 0.1761 -0.0090 -0.0029 0.0198 94 ILE A CB 723 C CG1 . ILE A 94 ? 0.2807 0.2947 0.1780 -0.0082 -0.0033 0.0209 94 ILE A CG1 724 C CG2 . ILE A 94 ? 0.2740 0.2980 0.1757 -0.0075 -0.0027 0.0182 94 ILE A CG2 725 C CD1 . ILE A 94 ? 0.2731 0.2848 0.1668 -0.0056 -0.0030 0.0234 94 ILE A CD1 726 N N . ASP A 95 ? 0.2814 0.3005 0.1828 -0.0085 -0.0039 0.0181 95 ASP A N 727 C CA . ASP A 95 ? 0.2850 0.3046 0.1853 -0.0063 -0.0039 0.0178 95 ASP A CA 728 C C . ASP A 95 ? 0.2826 0.3006 0.1820 -0.0048 -0.0034 0.0177 95 ASP A C 729 O O . ASP A 95 ? 0.2869 0.3022 0.1841 -0.0038 -0.0042 0.0169 95 ASP A O 730 C CB . ASP A 95 ? 0.2823 0.3022 0.1809 -0.0065 -0.0054 0.0159 95 ASP A CB 731 C CG . ASP A 95 ? 0.3089 0.3341 0.2092 -0.0076 -0.0062 0.0153 95 ASP A CG 732 O OD1 . ASP A 95 ? 0.3129 0.3381 0.2148 -0.0109 -0.0067 0.0138 95 ASP A OD1 733 O OD2 . ASP A 95 ? 0.3129 0.3428 0.2133 -0.0048 -0.0059 0.0168 95 ASP A OD2 734 N N . ALA A 96 ? 0.2841 0.3044 0.1858 -0.0047 -0.0018 0.0180 96 ALA A N 735 C CA . ALA A 96 ? 0.2814 0.3037 0.1838 -0.0035 -0.0010 0.0173 96 ALA A CA 736 C C . ALA A 96 ? 0.2858 0.3085 0.1886 -0.0028 0.0012 0.0181 96 ALA A C 737 O O . ALA A 96 ? 0.2847 0.3078 0.1906 -0.0040 0.0042 0.0186 96 ALA A O 738 C CB . ALA A 96 ? 0.2670 0.2934 0.1727 -0.0049 -0.0002 0.0158 96 ALA A CB 739 N N . VAL A 97 ? 0.2901 0.3124 0.1897 -0.0007 0.0005 0.0183 97 VAL A N 740 C CA . VAL A 97 ? 0.2862 0.3097 0.1842 0.0011 0.0025 0.0200 97 VAL A CA 741 C C . VAL A 97 ? 0.2860 0.3120 0.1834 0.0027 0.0042 0.0197 97 VAL A C 742 O O . VAL A 97 ? 0.2791 0.3063 0.1752 0.0040 0.0071 0.0220 97 VAL A O 743 C CB . VAL A 97 ? 0.2857 0.3102 0.1799 0.0027 0.0004 0.0202 97 VAL A CB 744 C CG1 . VAL A 97 ? 0.2909 0.3153 0.1868 0.0014 -0.0005 0.0209 97 VAL A CG1 745 C CG2 . VAL A 97 ? 0.2894 0.3132 0.1809 0.0028 -0.0024 0.0166 97 VAL A CG2 746 N N . HIS A 98 ? 0.2713 0.2984 0.1694 0.0031 0.0029 0.0174 98 HIS A N 747 C CA . HIS A 98 ? 0.2722 0.3038 0.1715 0.0046 0.0049 0.0166 98 HIS A CA 748 C C . HIS A 98 ? 0.2687 0.3033 0.1708 0.0050 0.0034 0.0146 98 HIS A C 749 O O . HIS A 98 ? 0.2751 0.3101 0.1753 0.0084 0.0020 0.0134 98 HIS A O 750 C CB . HIS A 98 ? 0.2713 0.3036 0.1656 0.0081 0.0048 0.0160 98 HIS A CB 751 C CG . HIS A 98 ? 0.2831 0.3112 0.1740 0.0099 0.0015 0.0132 98 HIS A CG 752 N ND1 . HIS A 98 ? 0.2921 0.3208 0.1802 0.0133 0.0014 0.0106 98 HIS A ND1 753 C CD2 . HIS A 98 ? 0.2749 0.2974 0.1650 0.0085 -0.0010 0.0124 98 HIS A CD2 754 C CE1 . HIS A 98 ? 0.2970 0.3191 0.1828 0.0138 -0.0007 0.0080 98 HIS A CE1 755 N NE2 . HIS A 98 ? 0.2896 0.3080 0.1768 0.0105 -0.0021 0.0093 98 HIS A NE2 756 N N . GLY A 99 ? 0.2708 0.3078 0.1772 0.0020 0.0039 0.0142 99 GLY A N 757 C CA . GLY A 99 ? 0.2676 0.3086 0.1755 0.0028 0.0017 0.0127 99 GLY A CA 758 C C . GLY A 99 ? 0.2715 0.3065 0.1764 0.0025 -0.0006 0.0140 99 GLY A C 759 O O . GLY A 99 ? 0.2676 0.2965 0.1704 0.0010 -0.0006 0.0152 99 GLY A O 760 N N . GLN A 100 ? 0.2746 0.3126 0.1791 0.0042 -0.0025 0.0138 100 GLN A N 761 C CA . GLN A 100 ? 0.2812 0.3142 0.1825 0.0041 -0.0039 0.0157 100 GLN A CA 762 C C . GLN A 100 ? 0.2852 0.3094 0.1816 0.0073 -0.0045 0.0175 100 GLN A C 763 O O . GLN A 100 ? 0.2892 0.3116 0.1828 0.0111 -0.0051 0.0194 100 GLN A O 764 C CB . GLN A 100 ? 0.2792 0.3207 0.1814 0.0052 -0.0050 0.0150 100 GLN A CB 765 C CG . GLN A 100 ? 0.2840 0.3221 0.1820 0.0063 -0.0059 0.0179 100 GLN A CG 766 C CD . GLN A 100 ? 0.2875 0.3194 0.1853 0.0019 -0.0051 0.0185 100 GLN A CD 767 O OE1 . GLN A 100 ? 0.2803 0.3064 0.1788 -0.0002 -0.0044 0.0184 100 GLN A OE1 768 N NE2 . GLN A 100 ? 0.2590 0.2938 0.1558 0.0011 -0.0052 0.0191 100 GLN A NE2 769 N N . ASN A 101 ? 0.2867 0.3056 0.1822 0.0060 -0.0040 0.0168 101 ASN A N 770 C CA . ASN A 101 ? 0.2859 0.2979 0.1781 0.0084 -0.0040 0.0161 101 ASN A CA 771 C C . ASN A 101 ? 0.2998 0.3016 0.1889 0.0084 -0.0039 0.0172 101 ASN A C 772 O O . ASN A 101 ? 0.3079 0.3023 0.1944 0.0109 -0.0031 0.0162 101 ASN A O 773 C CB . ASN A 101 ? 0.2803 0.2926 0.1722 0.0069 -0.0037 0.0140 101 ASN A CB 774 C CG . ASN A 101 ? 0.2876 0.3003 0.1805 0.0029 -0.0040 0.0144 101 ASN A CG 775 O OD1 . ASN A 101 ? 0.3213 0.3298 0.2134 0.0006 -0.0047 0.0139 101 ASN A OD1 776 N ND2 . ASN A 101 ? 0.2420 0.2600 0.1370 0.0021 -0.0029 0.0153 101 ASN A ND2 777 N N . ASN A 102 ? 0.2960 0.2967 0.1853 0.0055 -0.0039 0.0192 102 ASN A N 778 C CA . ASN A 102 ? 0.3000 0.2907 0.1868 0.0048 -0.0025 0.0211 102 ASN A CA 779 C C . ASN A 102 ? 0.3032 0.2912 0.1867 0.0105 -0.0016 0.0251 102 ASN A C 780 O O . ASN A 102 ? 0.3169 0.2937 0.1973 0.0117 0.0007 0.0275 102 ASN A O 781 C CB . ASN A 102 ? 0.2915 0.2832 0.1798 -0.0002 -0.0022 0.0221 102 ASN A CB 782 C CG . ASN A 102 ? 0.2983 0.2908 0.1891 -0.0051 -0.0027 0.0186 102 ASN A CG 783 O OD1 . ASN A 102 ? 0.3333 0.3330 0.2267 -0.0071 -0.0036 0.0182 102 ASN A OD1 784 N ND2 . ASN A 102 ? 0.2592 0.2452 0.1494 -0.0065 -0.0021 0.0156 102 ASN A ND2 785 N N . VAL A 103 ? 0.2974 0.2961 0.1818 0.0143 -0.0030 0.0256 103 VAL A N 786 C CA . VAL A 103 ? 0.3047 0.3066 0.1860 0.0204 -0.0030 0.0296 103 VAL A CA 787 C C . VAL A 103 ? 0.3093 0.3104 0.1890 0.0277 -0.0028 0.0300 103 VAL A C 788 O O . VAL A 103 ? 0.3009 0.3083 0.1838 0.0281 -0.0037 0.0263 103 VAL A O 789 C CB . VAL A 103 ? 0.2976 0.3151 0.1817 0.0196 -0.0050 0.0285 103 VAL A CB 790 C CG1 . VAL A 103 ? 0.3021 0.3281 0.1829 0.0270 -0.0059 0.0318 103 VAL A CG1 791 C CG2 . VAL A 103 ? 0.2825 0.2994 0.1675 0.0135 -0.0047 0.0284 103 VAL A CG2 792 N N . TYR A 104 ? 0.3251 0.3182 0.1998 0.0340 -0.0010 0.0349 104 TYR A N 793 C CA . TYR A 104 ? 0.3458 0.3372 0.2185 0.0427 -0.0003 0.0360 104 TYR A CA 794 C C . TYR A 104 ? 0.3425 0.3545 0.2178 0.0476 -0.0033 0.0349 104 TYR A C 795 O O . TYR A 104 ? 0.3420 0.3655 0.2170 0.0482 -0.0050 0.0366 104 TYR A O 796 C CB . TYR A 104 ? 0.3790 0.3558 0.2450 0.0493 0.0031 0.0429 104 TYR A CB 797 C CG . TYR A 104 ? 0.4071 0.3821 0.2706 0.0603 0.0042 0.0447 104 TYR A CG 798 C CD1 . TYR A 104 ? 0.4158 0.3766 0.2792 0.0613 0.0068 0.0416 104 TYR A CD1 799 C CD2 . TYR A 104 ? 0.4262 0.4156 0.2877 0.0702 0.0024 0.0486 104 TYR A CD2 800 C CE1 . TYR A 104 ? 0.4295 0.3885 0.2907 0.0721 0.0080 0.0429 104 TYR A CE1 801 C CE2 . TYR A 104 ? 0.4449 0.4345 0.3046 0.0814 0.0032 0.0503 104 TYR A CE2 802 C CZ . TYR A 104 ? 0.4531 0.4265 0.3126 0.0824 0.0063 0.0476 104 TYR A CZ 803 O OH . TYR A 104 ? 0.4773 0.4505 0.3350 0.0944 0.0076 0.0491 104 TYR A OH 804 N N . GLY A 105 ? 0.3356 0.3534 0.2138 0.0506 -0.0038 0.0315 105 GLY A N 805 C CA . GLY A 105 ? 0.3253 0.3644 0.2077 0.0545 -0.0063 0.0294 105 GLY A CA 806 C C . GLY A 105 ? 0.3051 0.3575 0.1946 0.0459 -0.0077 0.0239 105 GLY A C 807 O O . GLY A 105 ? 0.3096 0.3803 0.2042 0.0471 -0.0092 0.0208 105 GLY A O 808 N N . ALA A 106 ? 0.2914 0.3349 0.1815 0.0374 -0.0070 0.0226 106 ALA A N 809 C CA . ALA A 106 ? 0.2767 0.3285 0.1730 0.0297 -0.0070 0.0182 106 ALA A CA 810 C C . ALA A 106 ? 0.2700 0.3250 0.1698 0.0295 -0.0057 0.0151 106 ALA A C 811 O O . ALA A 106 ? 0.2731 0.3187 0.1697 0.0323 -0.0047 0.0155 106 ALA A O 812 C CB . ALA A 106 ? 0.2676 0.3087 0.1630 0.0226 -0.0063 0.0186 106 ALA A CB 813 N N . THR A 107 ? 0.2649 0.3332 0.1713 0.0258 -0.0052 0.0115 107 THR A N 814 C CA . THR A 107 ? 0.2635 0.3353 0.1734 0.0243 -0.0029 0.0091 107 THR A CA 815 C C . THR A 107 ? 0.2671 0.3255 0.1738 0.0203 -0.0013 0.0101 107 THR A C 816 O O . THR A 107 ? 0.2684 0.3221 0.1752 0.0151 -0.0011 0.0107 107 THR A O 817 C CB . THR A 107 ? 0.2577 0.3439 0.1760 0.0187 -0.0013 0.0052 107 THR A CB 818 O OG1 . THR A 107 ? 0.2536 0.3560 0.1755 0.0219 -0.0034 0.0029 107 THR A OG1 819 C CG2 . THR A 107 ? 0.2420 0.3318 0.1636 0.0173 0.0022 0.0037 107 THR A CG2 820 N N . ILE A 108 ? 0.2702 0.3239 0.1739 0.0234 -0.0003 0.0099 108 ILE A N 821 C CA . ILE A 108 ? 0.2666 0.3113 0.1669 0.0205 0.0008 0.0101 108 ILE A CA 822 C C . ILE A 108 ? 0.2706 0.3223 0.1735 0.0187 0.0040 0.0092 108 ILE A C 823 O O . ILE A 108 ? 0.2793 0.3368 0.1827 0.0225 0.0053 0.0078 108 ILE A O 824 C CB . ILE A 108 ? 0.2749 0.3084 0.1692 0.0242 0.0000 0.0095 108 ILE A CB 825 C CG1 . ILE A 108 ? 0.2752 0.2995 0.1668 0.0256 -0.0016 0.0114 108 ILE A CG1 826 C CG2 . ILE A 108 ? 0.2584 0.2868 0.1496 0.0210 0.0005 0.0086 108 ILE A CG2 827 C CD1 . ILE A 108 ? 0.2560 0.2775 0.1482 0.0200 -0.0026 0.0132 108 ILE A CD1 828 N N . PHE A 109 ? 0.2597 0.3106 0.1642 0.0135 0.0057 0.0106 109 PHE A N 829 C CA . PHE A 109 ? 0.2651 0.3208 0.1717 0.0114 0.0100 0.0113 109 PHE A CA 830 C C . PHE A 109 ? 0.2723 0.3231 0.1721 0.0136 0.0106 0.0124 109 PHE A C 831 O O . PHE A 109 ? 0.2764 0.3201 0.1714 0.0147 0.0076 0.0121 109 PHE A O 832 C CB . PHE A 109 ? 0.2638 0.3189 0.1749 0.0055 0.0126 0.0126 109 PHE A CB 833 C CG . PHE A 109 ? 0.2769 0.3396 0.1953 0.0025 0.0124 0.0097 109 PHE A CG 834 C CD1 . PHE A 109 ? 0.2679 0.3287 0.1862 0.0020 0.0089 0.0089 109 PHE A CD1 835 C CD2 . PHE A 109 ? 0.2750 0.3489 0.2006 0.0002 0.0159 0.0072 109 PHE A CD2 836 C CE1 . PHE A 109 ? 0.2904 0.3610 0.2148 -0.0001 0.0082 0.0054 109 PHE A CE1 837 C CE2 . PHE A 109 ? 0.2774 0.3614 0.2102 -0.0028 0.0153 0.0030 109 PHE A CE2 838 C CZ . PHE A 109 ? 0.2650 0.3478 0.1968 -0.0026 0.0112 0.0019 109 PHE A CZ 839 N N . PRO A 110 ? 0.2742 0.3303 0.1738 0.0140 0.0147 0.0135 110 PRO A N 840 C CA . PRO A 110 ? 0.2783 0.3322 0.1706 0.0165 0.0153 0.0149 110 PRO A CA 841 C C . PRO A 110 ? 0.2774 0.3249 0.1669 0.0146 0.0143 0.0178 110 PRO A C 842 O O . PRO A 110 ? 0.2895 0.3347 0.1831 0.0110 0.0161 0.0204 110 PRO A O 843 C CB . PRO A 110 ? 0.2792 0.3402 0.1726 0.0164 0.0213 0.0173 110 PRO A CB 844 C CG . PRO A 110 ? 0.2692 0.3379 0.1705 0.0151 0.0228 0.0147 110 PRO A CG 845 C CD . PRO A 110 ? 0.2710 0.3365 0.1771 0.0121 0.0194 0.0134 110 PRO A CD 846 N N . HIS A 111 ? 0.2731 0.3188 0.1561 0.0171 0.0115 0.0166 111 HIS A N 847 C CA . HIS A 111 ? 0.2658 0.3092 0.1459 0.0167 0.0104 0.0192 111 HIS A CA 848 C C . HIS A 111 ? 0.2764 0.3220 0.1547 0.0176 0.0155 0.0253 111 HIS A C 849 O O . HIS A 111 ? 0.2803 0.3300 0.1581 0.0188 0.0199 0.0271 111 HIS A O 850 C CB . HIS A 111 ? 0.2644 0.3089 0.1386 0.0189 0.0065 0.0151 111 HIS A CB 851 C CG . HIS A 111 ? 0.2667 0.3052 0.1430 0.0164 0.0024 0.0112 111 HIS A CG 852 N ND1 . HIS A 111 ? 0.2728 0.3076 0.1524 0.0133 0.0012 0.0132 111 HIS A ND1 853 C CD2 . HIS A 111 ? 0.2769 0.3117 0.1522 0.0165 0.0000 0.0057 111 HIS A CD2 854 C CE1 . HIS A 111 ? 0.2927 0.3226 0.1733 0.0114 -0.0016 0.0095 111 HIS A CE1 855 N NE2 . HIS A 111 ? 0.2673 0.2961 0.1454 0.0132 -0.0022 0.0051 111 HIS A NE2 856 N N . ASN A 112 ? 0.2723 0.3150 0.1497 0.0175 0.0154 0.0289 112 ASN A N 857 C CA . ASN A 112 ? 0.2876 0.3292 0.1637 0.0190 0.0211 0.0359 112 ASN A CA 858 C C . ASN A 112 ? 0.2897 0.3371 0.1591 0.0236 0.0250 0.0398 112 ASN A C 859 O O . ASN A 112 ? 0.2973 0.3425 0.1679 0.0231 0.0319 0.0451 112 ASN A O 860 C CB . ASN A 112 ? 0.2885 0.3272 0.1633 0.0204 0.0198 0.0392 112 ASN A CB 861 C CG . ASN A 112 ? 0.2822 0.3141 0.1643 0.0156 0.0193 0.0377 112 ASN A CG 862 O OD1 . ASN A 112 ? 0.2927 0.3227 0.1807 0.0112 0.0199 0.0346 112 ASN A OD1 863 N ND2 . ASN A 112 ? 0.2825 0.3124 0.1642 0.0170 0.0180 0.0397 112 ASN A ND2 864 N N . VAL A 113 ? 0.2939 0.3487 0.1560 0.0279 0.0212 0.0370 113 VAL A N 865 C CA . VAL A 113 ? 0.2956 0.3579 0.1500 0.0332 0.0248 0.0405 113 VAL A CA 866 C C . VAL A 113 ? 0.3024 0.3654 0.1599 0.0313 0.0304 0.0411 113 VAL A C 867 O O . VAL A 113 ? 0.3082 0.3729 0.1625 0.0334 0.0372 0.0477 113 VAL A O 868 C CB . VAL A 113 ? 0.3063 0.3786 0.1527 0.0376 0.0193 0.0349 113 VAL A CB 869 C CG1 . VAL A 113 ? 0.3009 0.3728 0.1504 0.0348 0.0151 0.0251 113 VAL A CG1 870 C CG2 . VAL A 113 ? 0.2935 0.3754 0.1304 0.0440 0.0234 0.0393 113 VAL A CG2 871 N N . GLY A 114 ? 0.2973 0.3596 0.1610 0.0278 0.0279 0.0344 114 GLY A N 872 C CA . GLY A 114 ? 0.2979 0.3636 0.1659 0.0262 0.0326 0.0338 114 GLY A CA 873 C C . GLY A 114 ? 0.2975 0.3585 0.1734 0.0210 0.0388 0.0384 114 GLY A C 874 O O . GLY A 114 ? 0.3197 0.3841 0.1977 0.0198 0.0457 0.0413 114 GLY A O 875 N N . LEU A 115 ? 0.2910 0.3444 0.1717 0.0174 0.0369 0.0384 115 LEU A N 876 C CA . LEU A 115 ? 0.2927 0.3402 0.1808 0.0120 0.0431 0.0418 115 LEU A CA 877 C C . LEU A 115 ? 0.3021 0.3455 0.1855 0.0142 0.0511 0.0509 115 LEU A C 878 O O . LEU A 115 ? 0.3008 0.3421 0.1893 0.0101 0.0593 0.0538 115 LEU A O 879 C CB . LEU A 115 ? 0.2847 0.3250 0.1774 0.0087 0.0393 0.0396 115 LEU A CB 880 C CG . LEU A 115 ? 0.2750 0.3190 0.1725 0.0066 0.0329 0.0321 115 LEU A CG 881 C CD1 . LEU A 115 ? 0.2617 0.2997 0.1634 0.0033 0.0301 0.0304 115 LEU A CD1 882 C CD2 . LEU A 115 ? 0.2619 0.3140 0.1666 0.0036 0.0356 0.0284 115 LEU A CD2 883 N N . GLY A 116 ? 0.3058 0.3489 0.1794 0.0207 0.0492 0.0554 116 GLY A N 884 C CA . GLY A 116 ? 0.3138 0.3545 0.1804 0.0253 0.0567 0.0653 116 GLY A CA 885 C C . GLY A 116 ? 0.3345 0.3820 0.1986 0.0263 0.0631 0.0679 116 GLY A C 886 O O . GLY A 116 ? 0.3525 0.3950 0.2159 0.0261 0.0729 0.0762 116 GLY A O 887 N N . ALA A 117 ? 0.3265 0.3846 0.1894 0.0272 0.0585 0.0611 117 ALA A N 888 C CA . ALA A 117 ? 0.3347 0.4014 0.1954 0.0284 0.0643 0.0625 117 ALA A CA 889 C C . ALA A 117 ? 0.3386 0.4036 0.2108 0.0206 0.0724 0.0627 117 ALA A C 890 O O . ALA A 117 ? 0.3410 0.4109 0.2124 0.0206 0.0803 0.0666 117 ALA A O 891 C CB . ALA A 117 ? 0.3246 0.4024 0.1821 0.0317 0.0575 0.0540 117 ALA A CB 892 N N . THR A 118 ? 0.3373 0.3966 0.2203 0.0137 0.0705 0.0580 118 THR A N 893 C CA . THR A 118 ? 0.3452 0.4058 0.2407 0.0053 0.0769 0.0555 118 THR A CA 894 C C . THR A 118 ? 0.3590 0.4086 0.2569 0.0013 0.0884 0.0638 118 THR A C 895 O O . THR A 118 ? 0.3686 0.4203 0.2757 -0.0058 0.0967 0.0632 118 THR A O 896 C CB . THR A 118 ? 0.3333 0.3935 0.2395 -0.0006 0.0710 0.0470 118 THR A CB 897 O OG1 . THR A 118 ? 0.3412 0.3884 0.2484 -0.0028 0.0711 0.0493 118 THR A OG1 898 C CG2 . THR A 118 ? 0.3257 0.3927 0.2290 0.0038 0.0602 0.0400 118 THR A CG2 899 N N . ARG A 119 ? 0.3692 0.4073 0.2594 0.0057 0.0893 0.0712 119 ARG A N 900 C CA . ARG A 119 ? 0.3899 0.4130 0.2824 0.0026 0.1002 0.0793 119 ARG A CA 901 C C . ARG A 119 ? 0.3897 0.4072 0.2980 -0.0092 0.1047 0.0729 119 ARG A C 902 O O . ARG A 119 ? 0.4081 0.4170 0.3221 -0.0151 0.1166 0.0771 119 ARG A O 903 C CB . ARG A 119 ? 0.4012 0.4241 0.2877 0.0052 0.1117 0.0895 119 ARG A CB 904 C CG . ARG A 119 ? 0.4108 0.4414 0.2812 0.0170 0.1087 0.0959 119 ARG A CG 905 C CD . ARG A 119 ? 0.4089 0.4317 0.2691 0.0256 0.1050 0.1025 119 ARG A CD 906 N NE . ARG A 119 ? 0.4176 0.4479 0.2624 0.0366 0.1063 0.1112 119 ARG A NE 907 C CZ . ARG A 119 ? 0.4178 0.4636 0.2542 0.0428 0.0974 0.1065 119 ARG A CZ 908 N NH1 . ARG A 119 ? 0.3832 0.4364 0.2252 0.0393 0.0871 0.0940 119 ARG A NH1 909 N NH2 . ARG A 119 ? 0.4043 0.4584 0.2264 0.0528 0.0993 0.1142 119 ARG A NH2 910 N N . ASP A 120 ? 0.3769 0.3997 0.2921 -0.0127 0.0956 0.0627 120 ASP A N 911 C CA . ASP A 120 ? 0.3774 0.4002 0.3074 -0.0235 0.0982 0.0544 120 ASP A CA 912 C C . ASP A 120 ? 0.3696 0.3844 0.3016 -0.0245 0.0920 0.0503 120 ASP A C 913 O O . ASP A 120 ? 0.3580 0.3810 0.2908 -0.0234 0.0817 0.0432 120 ASP A O 914 C CB . ASP A 120 ? 0.3747 0.4167 0.3117 -0.0264 0.0935 0.0454 120 ASP A CB 915 C CG . ASP A 120 ? 0.3908 0.4383 0.3439 -0.0377 0.0971 0.0364 120 ASP A CG 916 O OD1 . ASP A 120 ? 0.4440 0.4800 0.4032 -0.0442 0.1018 0.0351 120 ASP A OD1 917 O OD2 . ASP A 120 ? 0.3924 0.4571 0.3520 -0.0399 0.0951 0.0300 120 ASP A OD2 918 N N . PRO A 121 ? 0.3741 0.3719 0.3061 -0.0256 0.0988 0.0553 121 PRO A N 919 C CA . PRO A 121 ? 0.3651 0.3551 0.2987 -0.0259 0.0938 0.0516 121 PRO A CA 920 C C . PRO A 121 ? 0.3552 0.3522 0.3014 -0.0352 0.0907 0.0392 121 PRO A C 921 O O . PRO A 121 ? 0.3403 0.3388 0.2861 -0.0339 0.0826 0.0344 121 PRO A O 922 C CB . PRO A 121 ? 0.3783 0.3482 0.3108 -0.0257 0.1046 0.0597 121 PRO A CB 923 C CG . PRO A 121 ? 0.4012 0.3690 0.3257 -0.0207 0.1124 0.0709 121 PRO A CG 924 C CD . PRO A 121 ? 0.3964 0.3806 0.3263 -0.0257 0.1120 0.0654 121 PRO A CD 925 N N . TYR A 122 ? 0.3620 0.3647 0.3191 -0.0443 0.0974 0.0341 122 TYR A N 926 C CA . TYR A 122 ? 0.3554 0.3696 0.3250 -0.0529 0.0943 0.0214 122 TYR A CA 927 C C . TYR A 122 ? 0.3350 0.3682 0.3030 -0.0488 0.0822 0.0157 122 TYR A C 928 O O . TYR A 122 ? 0.3232 0.3632 0.2950 -0.0506 0.0754 0.0078 122 TYR A O 929 C CB . TYR A 122 ? 0.3786 0.3964 0.3615 -0.0642 0.1049 0.0165 122 TYR A CB 930 C CG . TYR A 122 ? 0.3953 0.4275 0.3914 -0.0730 0.1014 0.0022 122 TYR A CG 931 C CD1 . TYR A 122 ? 0.4097 0.4359 0.4084 -0.0756 0.0983 -0.0041 122 TYR A CD1 932 C CD2 . TYR A 122 ? 0.3983 0.4525 0.4038 -0.0779 0.1006 -0.0053 122 TYR A CD2 933 C CE1 . TYR A 122 ? 0.4260 0.4682 0.4358 -0.0830 0.0945 -0.0178 122 TYR A CE1 934 C CE2 . TYR A 122 ? 0.4035 0.4745 0.4207 -0.0851 0.0966 -0.0187 122 TYR A CE2 935 C CZ . TYR A 122 ? 0.4117 0.4769 0.4307 -0.0876 0.0935 -0.0250 122 TYR A CZ 936 O OH . TYR A 122 ? 0.4095 0.4936 0.4392 -0.0940 0.0892 -0.0386 122 TYR A OH 937 N N . LEU A 123 ? 0.3281 0.3696 0.2899 -0.0428 0.0800 0.0199 123 LEU A N 938 C CA . LEU A 123 ? 0.3101 0.3650 0.2678 -0.0367 0.0690 0.0165 123 LEU A CA 939 C C . LEU A 123 ? 0.2987 0.3460 0.2484 -0.0310 0.0608 0.0178 123 LEU A C 940 O O . LEU A 123 ? 0.2952 0.3500 0.2461 -0.0302 0.0530 0.0121 123 LEU A O 941 C CB . LEU A 123 ? 0.3133 0.3743 0.2639 -0.0303 0.0691 0.0215 123 LEU A CB 942 C CG . LEU A 123 ? 0.3122 0.3835 0.2571 -0.0228 0.0592 0.0190 123 LEU A CG 943 C CD1 . LEU A 123 ? 0.2994 0.3886 0.2541 -0.0255 0.0567 0.0106 123 LEU A CD1 944 C CD2 . LEU A 123 ? 0.2966 0.3686 0.2316 -0.0156 0.0601 0.0248 123 LEU A CD2 945 N N . VAL A 124 ? 0.2989 0.3322 0.2403 -0.0268 0.0628 0.0255 124 VAL A N 946 C CA . VAL A 124 ? 0.2940 0.3210 0.2285 -0.0219 0.0558 0.0268 124 VAL A CA 947 C C . VAL A 124 ? 0.2944 0.3180 0.2354 -0.0270 0.0547 0.0210 124 VAL A C 948 O O . VAL A 124 ? 0.2772 0.3035 0.2160 -0.0248 0.0470 0.0180 124 VAL A O 949 C CB . VAL A 124 ? 0.2985 0.3148 0.2230 -0.0154 0.0580 0.0363 124 VAL A CB 950 C CG1 . VAL A 124 ? 0.2921 0.3032 0.2117 -0.0114 0.0518 0.0368 124 VAL A CG1 951 C CG2 . VAL A 124 ? 0.2853 0.3088 0.2019 -0.0093 0.0563 0.0399 124 VAL A CG2 952 N N . LYS A 125 ? 0.3112 0.3291 0.2605 -0.0342 0.0629 0.0189 125 LYS A N 953 C CA . LYS A 125 ? 0.3079 0.3243 0.2643 -0.0399 0.0624 0.0114 125 LYS A CA 954 C C . LYS A 125 ? 0.3050 0.3391 0.2660 -0.0418 0.0549 0.0025 125 LYS A C 955 O O . LYS A 125 ? 0.2963 0.3327 0.2564 -0.0409 0.0489 -0.0014 125 LYS A O 956 C CB . LYS A 125 ? 0.3182 0.3261 0.2841 -0.0485 0.0735 0.0089 125 LYS A CB 957 C CG . LYS A 125 ? 0.3200 0.3235 0.2920 -0.0538 0.0739 0.0011 125 LYS A CG 958 C CD . LYS A 125 ? 0.3287 0.3253 0.3120 -0.0641 0.0850 -0.0043 125 LYS A CD 959 C CE . LYS A 125 ? 0.3305 0.3237 0.3195 -0.0691 0.0848 -0.0137 125 LYS A CE 960 N NZ . LYS A 125 ? 0.3536 0.3354 0.3537 -0.0795 0.0974 -0.0187 125 LYS A NZ 961 N N . ARG A 126 ? 0.3049 0.3524 0.2707 -0.0438 0.0555 -0.0003 126 ARG A N 962 C CA . ARG A 126 ? 0.2934 0.3598 0.2635 -0.0441 0.0487 -0.0081 126 ARG A CA 963 C C . ARG A 126 ? 0.2774 0.3463 0.2379 -0.0353 0.0390 -0.0054 126 ARG A C 964 O O . ARG A 126 ? 0.2608 0.3389 0.2221 -0.0343 0.0329 -0.0102 126 ARG A O 965 C CB . ARG A 126 ? 0.2970 0.3778 0.2742 -0.0470 0.0520 -0.0108 126 ARG A CB 966 C CG . ARG A 126 ? 0.3120 0.3953 0.3023 -0.0582 0.0611 -0.0172 126 ARG A CG 967 C CD . ARG A 126 ? 0.3169 0.4187 0.3154 -0.0612 0.0637 -0.0209 126 ARG A CD 968 N NE . ARG A 126 ? 0.4001 0.4953 0.3939 -0.0583 0.0694 -0.0122 126 ARG A NE 969 C CZ . ARG A 126 ? 0.4054 0.5138 0.3981 -0.0539 0.0679 -0.0110 126 ARG A CZ 970 N NH1 . ARG A 126 ? 0.4036 0.5055 0.3911 -0.0513 0.0737 -0.0030 126 ARG A NH1 971 N NH2 . ARG A 126 ? 0.3893 0.5179 0.3856 -0.0509 0.0607 -0.0173 126 ARG A NH2 972 N N . ILE A 127 ? 0.2689 0.3298 0.2202 -0.0289 0.0381 0.0023 127 ILE A N 973 C CA . ILE A 127 ? 0.2637 0.3234 0.2061 -0.0216 0.0303 0.0049 127 ILE A CA 974 C C . ILE A 127 ? 0.2633 0.3158 0.2035 -0.0218 0.0272 0.0044 127 ILE A C 975 O O . ILE A 127 ? 0.2586 0.3158 0.1965 -0.0192 0.0212 0.0025 127 ILE A O 976 C CB . ILE A 127 ? 0.2590 0.3119 0.1928 -0.0160 0.0306 0.0117 127 ILE A CB 977 C CG1 . ILE A 127 ? 0.2611 0.3238 0.1961 -0.0144 0.0321 0.0112 127 ILE A CG1 978 C CG2 . ILE A 127 ? 0.2451 0.2938 0.1706 -0.0103 0.0237 0.0135 127 ILE A CG2 979 C CD1 . ILE A 127 ? 0.2515 0.3098 0.1790 -0.0099 0.0344 0.0169 127 ILE A CD1 980 N N . GLY A 128 ? 0.2749 0.3161 0.2157 -0.0246 0.0321 0.0065 128 GLY A N 981 C CA . GLY A 128 ? 0.2663 0.3012 0.2063 -0.0251 0.0304 0.0055 128 GLY A CA 982 C C . GLY A 128 ? 0.2651 0.3100 0.2113 -0.0293 0.0283 -0.0027 128 GLY A C 983 O O . GLY A 128 ? 0.2448 0.2918 0.1880 -0.0273 0.0233 -0.0041 128 GLY A O 984 N N . GLU A 129 ? 0.2754 0.3282 0.2303 -0.0352 0.0322 -0.0084 129 GLU A N 985 C CA . GLU A 129 ? 0.2793 0.3458 0.2407 -0.0392 0.0298 -0.0176 129 GLU A CA 986 C C . GLU A 129 ? 0.2768 0.3569 0.2340 -0.0334 0.0217 -0.0181 129 GLU A C 987 O O . GLU A 129 ? 0.2697 0.3552 0.2251 -0.0322 0.0174 -0.0212 129 GLU A O 988 C CB . GLU A 129 ? 0.2893 0.3639 0.2620 -0.0473 0.0359 -0.0246 129 GLU A CB 989 C CG . GLU A 129 ? 0.3142 0.3731 0.2915 -0.0537 0.0449 -0.0249 129 GLU A CG 990 C CD . GLU A 129 ? 0.3650 0.4293 0.3543 -0.0630 0.0526 -0.0315 129 GLU A CD 991 O OE1 . GLU A 129 ? 0.3641 0.4461 0.3582 -0.0641 0.0508 -0.0351 129 GLU A OE1 992 O OE2 . GLU A 129 ? 0.3694 0.4200 0.3637 -0.0693 0.0611 -0.0330 129 GLU A OE2 993 N N . ALA A 130 ? 0.2739 0.3587 0.2289 -0.0291 0.0202 -0.0146 130 ALA A N 994 C CA . ALA A 130 ? 0.2650 0.3603 0.2157 -0.0223 0.0136 -0.0140 130 ALA A CA 995 C C . ALA A 130 ? 0.2666 0.3516 0.2077 -0.0169 0.0093 -0.0087 130 ALA A C 996 O O . ALA A 130 ? 0.2720 0.3637 0.2100 -0.0131 0.0047 -0.0092 130 ALA A O 997 C CB . ALA A 130 ? 0.2680 0.3678 0.2182 -0.0184 0.0140 -0.0114 130 ALA A CB 998 N N . THR A 131 ? 0.2690 0.3388 0.2055 -0.0165 0.0112 -0.0034 131 THR A N 999 C CA . THR A 131 ? 0.2657 0.3261 0.1945 -0.0128 0.0079 0.0011 131 THR A CA 1000 C C . THR A 131 ? 0.2682 0.3290 0.1972 -0.0147 0.0067 -0.0014 131 THR A C 1001 O O . THR A 131 ? 0.2752 0.3364 0.1992 -0.0113 0.0029 0.0004 131 THR A O 1002 C CB . THR A 131 ? 0.2699 0.3176 0.1947 -0.0120 0.0102 0.0062 131 THR A CB 1003 O OG1 . THR A 131 ? 0.2735 0.3219 0.1970 -0.0097 0.0114 0.0083 131 THR A OG1 1004 C CG2 . THR A 131 ? 0.2461 0.2870 0.1645 -0.0090 0.0067 0.0095 131 THR A CG2 1005 N N . ALA A 132 ? 0.2674 0.3278 0.2021 -0.0201 0.0104 -0.0056 132 ALA A N 1006 C CA . ALA A 132 ? 0.2749 0.3375 0.2102 -0.0220 0.0095 -0.0095 132 ALA A CA 1007 C C . ALA A 132 ? 0.2765 0.3543 0.2111 -0.0199 0.0049 -0.0131 132 ALA A C 1008 O O . ALA A 132 ? 0.2837 0.3628 0.2136 -0.0175 0.0021 -0.0122 132 ALA A O 1009 C CB . ALA A 132 ? 0.2734 0.3331 0.2161 -0.0286 0.0151 -0.0152 132 ALA A CB 1010 N N . LEU A 133 ? 0.2798 0.3704 0.2189 -0.0203 0.0045 -0.0168 133 LEU A N 1011 C CA . LEU A 133 ? 0.2783 0.3864 0.2168 -0.0169 0.0000 -0.0200 133 LEU A CA 1012 C C . LEU A 133 ? 0.2791 0.3847 0.2083 -0.0085 -0.0041 -0.0124 133 LEU A C 1013 O O . LEU A 133 ? 0.2830 0.3955 0.2076 -0.0049 -0.0072 -0.0120 133 LEU A O 1014 C CB . LEU A 133 ? 0.2781 0.4024 0.2246 -0.0188 0.0006 -0.0258 133 LEU A CB 1015 C CG . LEU A 133 ? 0.2833 0.4137 0.2407 -0.0283 0.0051 -0.0354 133 LEU A CG 1016 C CD1 . LEU A 133 ? 0.2766 0.4217 0.2428 -0.0310 0.0068 -0.0403 133 LEU A CD1 1017 C CD2 . LEU A 133 ? 0.2744 0.4161 0.2333 -0.0308 0.0033 -0.0433 133 LEU A CD2 1018 N N . GLU A 134 ? 0.2814 0.3766 0.2075 -0.0055 -0.0037 -0.0066 134 GLU A N 1019 C CA . GLU A 134 ? 0.2806 0.3699 0.1985 0.0016 -0.0064 0.0001 134 GLU A CA 1020 C C . GLU A 134 ? 0.2735 0.3504 0.1855 0.0015 -0.0066 0.0043 134 GLU A C 1021 O O . GLU A 134 ? 0.2665 0.3416 0.1722 0.0064 -0.0083 0.0086 134 GLU A O 1022 C CB . GLU A 134 ? 0.2838 0.3668 0.2007 0.0045 -0.0056 0.0032 134 GLU A CB 1023 C CG . GLU A 134 ? 0.2871 0.3845 0.2100 0.0053 -0.0052 -0.0008 134 GLU A CG 1024 C CD . GLU A 134 ? 0.3025 0.3987 0.2225 0.0120 -0.0058 0.0024 134 GLU A CD 1025 O OE1 . GLU A 134 ? 0.2845 0.3686 0.1973 0.0166 -0.0068 0.0074 134 GLU A OE1 1026 O OE2 . GLU A 134 ? 0.2810 0.3887 0.2065 0.0124 -0.0049 -0.0007 134 GLU A OE2 1027 N N . VAL A 135 ? 0.2652 0.3339 0.1793 -0.0036 -0.0042 0.0034 135 VAL A N 1028 C CA . VAL A 135 ? 0.2640 0.3245 0.1742 -0.0043 -0.0042 0.0061 135 VAL A CA 1029 C C . VAL A 135 ? 0.2630 0.3331 0.1723 -0.0043 -0.0053 0.0035 135 VAL A C 1030 O O . VAL A 135 ? 0.2680 0.3362 0.1715 -0.0016 -0.0064 0.0074 135 VAL A O 1031 C CB . VAL A 135 ? 0.2632 0.3142 0.1761 -0.0085 -0.0013 0.0060 135 VAL A CB 1032 C CG1 . VAL A 135 ? 0.2632 0.3089 0.1733 -0.0090 -0.0013 0.0080 135 VAL A CG1 1033 C CG2 . VAL A 135 ? 0.2555 0.2991 0.1676 -0.0074 -0.0005 0.0090 135 VAL A CG2 1034 N N . ARG A 136 ? 0.2511 0.3319 0.1659 -0.0075 -0.0047 -0.0034 136 ARG A N 1035 C CA . ARG A 136 ? 0.2612 0.3542 0.1750 -0.0073 -0.0061 -0.0076 136 ARG A CA 1036 C C . ARG A 136 ? 0.2635 0.3683 0.1719 -0.0005 -0.0097 -0.0050 136 ARG A C 1037 O O . ARG A 136 ? 0.2534 0.3656 0.1570 0.0020 -0.0110 -0.0047 136 ARG A O 1038 C CB . ARG A 136 ? 0.2663 0.3685 0.1884 -0.0133 -0.0043 -0.0175 136 ARG A CB 1039 C CG . ARG A 136 ? 0.2497 0.3400 0.1754 -0.0187 -0.0001 -0.0200 136 ARG A CG 1040 C CD . ARG A 136 ? 0.2747 0.3639 0.1956 -0.0176 -0.0005 -0.0193 136 ARG A CD 1041 N NE . ARG A 136 ? 0.2777 0.3585 0.2028 -0.0219 0.0036 -0.0233 136 ARG A NE 1042 C CZ . ARG A 136 ? 0.3106 0.3929 0.2341 -0.0222 0.0043 -0.0262 136 ARG A CZ 1043 N NH1 . ARG A 136 ? 0.3017 0.3941 0.2190 -0.0188 0.0013 -0.0251 136 ARG A NH1 1044 N NH2 . ARG A 136 ? 0.3117 0.3851 0.2395 -0.0252 0.0086 -0.0298 136 ARG A NH2 1045 N N . ALA A 137 ? 0.2592 0.3658 0.1678 0.0032 -0.0108 -0.0027 137 ALA A N 1046 C CA . ALA A 137 ? 0.2694 0.3852 0.1723 0.0116 -0.0136 0.0014 137 ALA A CA 1047 C C . ALA A 137 ? 0.2695 0.3737 0.1631 0.0161 -0.0133 0.0101 137 ALA A C 1048 O O . ALA A 137 ? 0.2776 0.3891 0.1647 0.0230 -0.0148 0.0141 137 ALA A O 1049 C CB . ALA A 137 ? 0.2581 0.3747 0.1632 0.0152 -0.0140 0.0028 137 ALA A CB 1050 N N . THR A 138 ? 0.2786 0.3655 0.1718 0.0122 -0.0110 0.0130 138 THR A N 1051 C CA . THR A 138 ? 0.2815 0.3557 0.1679 0.0142 -0.0097 0.0203 138 THR A CA 1052 C C . THR A 138 ? 0.2796 0.3537 0.1650 0.0102 -0.0085 0.0195 138 THR A C 1053 O O . THR A 138 ? 0.2754 0.3394 0.1568 0.0099 -0.0066 0.0246 138 THR A O 1054 C CB . THR A 138 ? 0.2777 0.3349 0.1646 0.0127 -0.0081 0.0234 138 THR A CB 1055 O OG1 . THR A 138 ? 0.2794 0.3321 0.1717 0.0061 -0.0071 0.0196 138 THR A OG1 1056 C CG2 . THR A 138 ? 0.2618 0.3196 0.1492 0.0171 -0.0089 0.0237 138 THR A CG2 1057 N N . GLY A 139 ? 0.2794 0.3649 0.1691 0.0069 -0.0090 0.0123 139 GLY A N 1058 C CA . GLY A 139 ? 0.2908 0.3777 0.1797 0.0038 -0.0077 0.0103 139 GLY A CA 1059 C C . GLY A 139 ? 0.2928 0.3676 0.1859 -0.0016 -0.0053 0.0096 139 GLY A C 1060 O O . GLY A 139 ? 0.3065 0.3811 0.1991 -0.0036 -0.0038 0.0087 139 GLY A O 1061 N N . ILE A 140 ? 0.2827 0.3486 0.1797 -0.0034 -0.0049 0.0099 140 ILE A N 1062 C CA . ILE A 140 ? 0.2720 0.3278 0.1720 -0.0069 -0.0029 0.0102 140 ILE A CA 1063 C C . ILE A 140 ? 0.2737 0.3308 0.1802 -0.0104 -0.0012 0.0041 140 ILE A C 1064 O O . ILE A 140 ? 0.2705 0.3323 0.1804 -0.0112 -0.0014 0.0002 140 ILE A O 1065 C CB . ILE A 140 ? 0.2710 0.3163 0.1700 -0.0062 -0.0030 0.0149 140 ILE A CB 1066 C CG1 . ILE A 140 ? 0.2613 0.3025 0.1545 -0.0040 -0.0031 0.0205 140 ILE A CG1 1067 C CG2 . ILE A 140 ? 0.2598 0.2985 0.1622 -0.0089 -0.0016 0.0145 140 ILE A CG2 1068 C CD1 . ILE A 140 ? 0.2515 0.2830 0.1436 -0.0033 -0.0030 0.0235 140 ILE A CD1 1069 N N . GLN A 141 ? 0.2738 0.3265 0.1823 -0.0123 0.0009 0.0031 141 GLN A N 1070 C CA . GLN A 141 ? 0.2813 0.3332 0.1954 -0.0152 0.0037 -0.0027 141 GLN A CA 1071 C C . GLN A 141 ? 0.2838 0.3252 0.2009 -0.0156 0.0062 -0.0004 141 GLN A C 1072 O O . GLN A 141 ? 0.2852 0.3228 0.2067 -0.0173 0.0097 -0.0039 141 GLN A O 1073 C CB . GLN A 141 ? 0.2810 0.3371 0.1952 -0.0159 0.0051 -0.0067 141 GLN A CB 1074 C CG . GLN A 141 ? 0.2866 0.3543 0.1962 -0.0145 0.0029 -0.0079 141 GLN A CG 1075 C CD . GLN A 141 ? 0.2896 0.3563 0.1934 -0.0121 0.0022 -0.0013 141 GLN A CD 1076 O OE1 . GLN A 141 ? 0.2677 0.3261 0.1712 -0.0119 0.0024 0.0040 141 GLN A OE1 1077 N NE2 . GLN A 141 ? 0.2845 0.3607 0.1838 -0.0106 0.0017 -0.0020 141 GLN A NE2 1078 N N . TYR A 142 ? 0.2860 0.3226 0.2005 -0.0137 0.0048 0.0052 142 TYR A N 1079 C CA . TYR A 142 ? 0.2879 0.3174 0.2036 -0.0126 0.0066 0.0080 142 TYR A CA 1080 C C . TYR A 142 ? 0.2915 0.3187 0.2048 -0.0112 0.0047 0.0119 142 TYR A C 1081 O O . TYR A 142 ? 0.2961 0.3243 0.2062 -0.0107 0.0021 0.0138 142 TYR A O 1082 C CB . TYR A 142 ? 0.2862 0.3162 0.2014 -0.0115 0.0068 0.0091 142 TYR A CB 1083 C CG . TYR A 142 ? 0.2803 0.3067 0.1964 -0.0090 0.0080 0.0122 142 TYR A CG 1084 C CD1 . TYR A 142 ? 0.2798 0.3100 0.1956 -0.0080 0.0070 0.0136 142 TYR A CD1 1085 C CD2 . TYR A 142 ? 0.2901 0.3109 0.2074 -0.0072 0.0104 0.0138 142 TYR A CD2 1086 C CE1 . TYR A 142 ? 0.2814 0.3118 0.1983 -0.0047 0.0076 0.0160 142 TYR A CE1 1087 C CE2 . TYR A 142 ? 0.3027 0.3222 0.2198 -0.0033 0.0112 0.0173 142 TYR A CE2 1088 C CZ . TYR A 142 ? 0.2963 0.3216 0.2134 -0.0017 0.0095 0.0181 142 TYR A CZ 1089 O OH . TYR A 142 ? 0.2915 0.3186 0.2087 0.0031 0.0098 0.0212 142 TYR A OH 1090 N N . ALA A 143 ? 0.2934 0.3169 0.2081 -0.0107 0.0066 0.0127 143 ALA A N 1091 C CA . ALA A 143 ? 0.2849 0.3069 0.1969 -0.0089 0.0052 0.0157 143 ALA A CA 1092 C C . ALA A 143 ? 0.2872 0.3065 0.1984 -0.0063 0.0064 0.0189 143 ALA A C 1093 O O . ALA A 143 ? 0.2914 0.3071 0.2045 -0.0053 0.0100 0.0197 143 ALA A O 1094 C CB . ALA A 143 ? 0.2875 0.3099 0.2010 -0.0096 0.0067 0.0147 143 ALA A CB 1095 N N . PHE A 144 ? 0.2813 0.3025 0.1896 -0.0049 0.0035 0.0204 144 PHE A N 1096 C CA . PHE A 144 ? 0.2824 0.3047 0.1892 -0.0015 0.0037 0.0231 144 PHE A CA 1097 C C . PHE A 144 ? 0.2846 0.3053 0.1891 0.0008 0.0053 0.0253 144 PHE A C 1098 O O . PHE A 144 ? 0.2902 0.3139 0.1915 0.0021 0.0031 0.0253 144 PHE A O 1099 C CB . PHE A 144 ? 0.2766 0.3039 0.1820 -0.0018 0.0001 0.0222 144 PHE A CB 1100 C CG . PHE A 144 ? 0.2832 0.3126 0.1908 -0.0044 -0.0008 0.0206 144 PHE A CG 1101 C CD1 . PHE A 144 ? 0.2841 0.3138 0.1910 -0.0076 -0.0027 0.0190 144 PHE A CD1 1102 C CD2 . PHE A 144 ? 0.2774 0.3079 0.1875 -0.0034 0.0011 0.0210 144 PHE A CD2 1103 C CE1 . PHE A 144 ? 0.3062 0.3378 0.2148 -0.0102 -0.0026 0.0184 144 PHE A CE1 1104 C CE2 . PHE A 144 ? 0.3033 0.3371 0.2153 -0.0057 0.0007 0.0196 144 PHE A CE2 1105 C CZ . PHE A 144 ? 0.2690 0.3036 0.1800 -0.0093 -0.0010 0.0186 144 PHE A CZ 1106 N N . ALA A 145 ? 0.2898 0.3058 0.1962 0.0007 0.0097 0.0265 145 ALA A N 1107 C CA . ALA A 145 ? 0.2939 0.3080 0.1986 0.0022 0.0127 0.0290 145 ALA A CA 1108 C C . ALA A 145 ? 0.3013 0.3082 0.2090 0.0022 0.0191 0.0312 145 ALA A C 1109 O O . ALA A 145 ? 0.3061 0.3101 0.2181 -0.0007 0.0207 0.0282 145 ALA A O 1110 C CB . ALA A 145 ? 0.2811 0.2971 0.1866 -0.0007 0.0116 0.0260 145 ALA A CB 1111 N N . PRO A 146 ? 0.3040 0.3076 0.2093 0.0053 0.0235 0.0362 146 PRO A N 1112 C CA . PRO A 146 ? 0.3043 0.3124 0.2039 0.0091 0.0226 0.0395 146 PRO A CA 1113 C C . PRO A 146 ? 0.3087 0.3223 0.2026 0.0156 0.0197 0.0430 146 PRO A C 1114 O O . PRO A 146 ? 0.3152 0.3267 0.2089 0.0194 0.0215 0.0464 146 PRO A O 1115 C CB . PRO A 146 ? 0.3054 0.3069 0.2053 0.0095 0.0303 0.0440 146 PRO A CB 1116 C CG . PRO A 146 ? 0.3205 0.3123 0.2241 0.0092 0.0355 0.0455 146 PRO A CG 1117 C CD . PRO A 146 ? 0.3172 0.3110 0.2252 0.0053 0.0311 0.0390 146 PRO A CD 1118 N N . CYS A 147 ? 0.3033 0.3248 0.1929 0.0170 0.0154 0.0415 147 CYS A N 1119 C CA . CYS A 147 ? 0.3108 0.3402 0.1943 0.0235 0.0136 0.0447 147 CYS A CA 1120 C C . CYS A 147 ? 0.3236 0.3497 0.2028 0.0286 0.0199 0.0522 147 CYS A C 1121 O O . CYS A 147 ? 0.3182 0.3432 0.1957 0.0274 0.0225 0.0528 147 CYS A O 1122 C CB . CYS A 147 ? 0.3027 0.3413 0.1831 0.0229 0.0081 0.0397 147 CYS A CB 1123 S SG . CYS A 147 ? 0.3260 0.3784 0.1990 0.0308 0.0053 0.0418 147 CYS A SG 1124 N N . ILE A 148 ? 0.3331 0.3569 0.2104 0.0347 0.0231 0.0585 148 ILE A N 1125 C CA . ILE A 148 ? 0.3385 0.3578 0.2103 0.0411 0.0300 0.0676 148 ILE A CA 1126 C C . ILE A 148 ? 0.3508 0.3829 0.2138 0.0510 0.0274 0.0724 148 ILE A C 1127 O O . ILE A 148 ? 0.3672 0.3966 0.2247 0.0593 0.0329 0.0817 148 ILE A O 1128 C CB . ILE A 148 ? 0.3522 0.3559 0.2281 0.0412 0.0382 0.0725 148 ILE A CB 1129 C CG1 . ILE A 148 ? 0.3561 0.3597 0.2348 0.0440 0.0360 0.0717 148 ILE A CG1 1130 C CG2 . ILE A 148 ? 0.3337 0.3278 0.2174 0.0311 0.0417 0.0674 148 ILE A CG2 1131 C CD1 . ILE A 148 ? 0.3346 0.3234 0.2145 0.0482 0.0447 0.0785 148 ILE A CD1 1132 N N . ALA A 149 ? 0.3384 0.3850 0.1999 0.0504 0.0194 0.0657 149 ALA A N 1133 C CA . ALA A 149 ? 0.3408 0.4033 0.1938 0.0585 0.0161 0.0677 149 ALA A CA 1134 C C . ALA A 149 ? 0.3491 0.4103 0.1944 0.0627 0.0215 0.0742 149 ALA A C 1135 O O . ALA A 149 ? 0.3455 0.3988 0.1930 0.0567 0.0247 0.0726 149 ALA A O 1136 C CB . ALA A 149 ? 0.3339 0.4098 0.1878 0.0542 0.0077 0.0570 149 ALA A CB 1137 N N . VAL A 150 ? 0.3541 0.4246 0.1904 0.0735 0.0227 0.0817 150 VAL A N 1138 C CA . VAL A 150 ? 0.3644 0.4384 0.1913 0.0791 0.0271 0.0880 150 VAL A CA 1139 C C . VAL A 150 ? 0.3666 0.4633 0.1872 0.0826 0.0188 0.0813 150 VAL A C 1140 O O . VAL A 150 ? 0.3718 0.4836 0.1867 0.0916 0.0155 0.0838 150 VAL A O 1141 C CB . VAL A 150 ? 0.3813 0.4494 0.2012 0.0901 0.0353 0.1026 150 VAL A CB 1142 C CG1 . VAL A 150 ? 0.3812 0.4520 0.1909 0.0956 0.0411 0.1103 150 VAL A CG1 1143 C CG2 . VAL A 150 ? 0.3651 0.4103 0.1929 0.0859 0.0432 0.1071 150 VAL A CG2 1144 N N . CYS A 151 ? 0.3630 0.4625 0.1851 0.0754 0.0155 0.0720 151 CYS A N 1145 C CA . CYS A 151 ? 0.3635 0.4828 0.1807 0.0770 0.0082 0.0632 151 CYS A CA 1146 C C . CYS A 151 ? 0.3766 0.5090 0.1808 0.0876 0.0106 0.0700 151 CYS A C 1147 O O . CYS A 151 ? 0.3847 0.5116 0.1842 0.0884 0.0167 0.0748 151 CYS A O 1148 C CB . CYS A 151 ? 0.3594 0.4752 0.1816 0.0671 0.0052 0.0517 151 CYS A CB 1149 S SG . CYS A 151 ? 0.3612 0.4986 0.1774 0.0682 -0.0022 0.0393 151 CYS A SG 1150 N N . ARG A 152 ? 0.3772 0.5288 0.1755 0.0962 0.0059 0.0704 152 ARG A N 1151 C CA . ARG A 152 ? 0.3954 0.5630 0.1799 0.1087 0.0075 0.0780 152 ARG A CA 1152 C C . ARG A 152 ? 0.3899 0.5806 0.1690 0.1091 0.0001 0.0659 152 ARG A C 1153 O O . ARG A 152 ? 0.4041 0.6122 0.1709 0.1194 0.0003 0.0701 152 ARG A O 1154 C CB . ARG A 152 ? 0.4087 0.5845 0.1893 0.1202 0.0074 0.0874 152 ARG A CB 1155 C CG . ARG A 152 ? 0.4241 0.5763 0.2082 0.1219 0.0163 0.1004 152 ARG A CG 1156 C CD . ARG A 152 ? 0.5152 0.6673 0.2866 0.1356 0.0242 0.1167 152 ARG A CD 1157 N NE . ARG A 152 ? 0.5298 0.6633 0.2992 0.1323 0.0343 0.1239 152 ARG A NE 1158 C CZ . ARG A 152 ? 0.5217 0.6553 0.2791 0.1420 0.0423 0.1369 152 ARG A CZ 1159 N NH1 . ARG A 152 ? 0.5683 0.7205 0.3126 0.1573 0.0412 0.1450 152 ARG A NH1 1160 N NH2 . ARG A 152 ? 0.5303 0.6464 0.2887 0.1363 0.0517 0.1417 152 ARG A NH2 1161 N N . ASP A 153 ? 0.3728 0.5631 0.1606 0.0979 -0.0057 0.0510 153 ASP A N 1162 C CA . ASP A 153 ? 0.3676 0.5774 0.1523 0.0962 -0.0125 0.0369 153 ASP A CA 1163 C C . ASP A 153 ? 0.3514 0.5476 0.1459 0.0829 -0.0141 0.0244 153 ASP A C 1164 O O . ASP A 153 ? 0.3457 0.5345 0.1509 0.0749 -0.0172 0.0184 153 ASP A O 1165 C CB . ASP A 153 ? 0.3727 0.6065 0.1579 0.0997 -0.0204 0.0303 153 ASP A CB 1166 C CG . ASP A 153 ? 0.3825 0.6413 0.1621 0.1004 -0.0267 0.0166 153 ASP A CG 1167 O OD1 . ASP A 153 ? 0.4033 0.6884 0.1773 0.1088 -0.0316 0.0152 153 ASP A OD1 1168 O OD2 . ASP A 153 ? 0.3826 0.6356 0.1635 0.0931 -0.0269 0.0065 153 ASP A OD2 1169 N N . PRO A 154 ? 0.3458 0.5391 0.1364 0.0813 -0.0117 0.0207 154 PRO A N 1170 C CA . PRO A 154 ? 0.3393 0.5171 0.1385 0.0706 -0.0118 0.0112 154 PRO A CA 1171 C C . PRO A 154 ? 0.3347 0.5191 0.1397 0.0633 -0.0188 -0.0052 154 PRO A C 1172 O O . PRO A 154 ? 0.3250 0.4953 0.1372 0.0551 -0.0188 -0.0124 154 PRO A O 1173 C CB . PRO A 154 ? 0.3368 0.5146 0.1287 0.0733 -0.0074 0.0117 154 PRO A CB 1174 C CG . PRO A 154 ? 0.3558 0.5562 0.1345 0.0842 -0.0081 0.0150 154 PRO A CG 1175 C CD . PRO A 154 ? 0.3553 0.5603 0.1329 0.0903 -0.0084 0.0255 154 PRO A CD 1176 N N . ARG A 155 ? 0.3388 0.5451 0.1410 0.0665 -0.0245 -0.0111 155 ARG A N 1177 C CA . ARG A 155 ? 0.3330 0.5459 0.1424 0.0583 -0.0304 -0.0269 155 ARG A CA 1178 C C . ARG A 155 ? 0.3343 0.5332 0.1561 0.0503 -0.0310 -0.0264 155 ARG A C 1179 O O . ARG A 155 ? 0.3368 0.5350 0.1666 0.0414 -0.0341 -0.0384 155 ARG A O 1180 C CB . ARG A 155 ? 0.3363 0.5799 0.1401 0.0638 -0.0363 -0.0340 155 ARG A CB 1181 C CG . ARG A 155 ? 0.3308 0.5898 0.1222 0.0705 -0.0363 -0.0379 155 ARG A CG 1182 C CD . ARG A 155 ? 0.3643 0.6577 0.1490 0.0773 -0.0425 -0.0446 155 ARG A CD 1183 N NE . ARG A 155 ? 0.3583 0.6630 0.1365 0.0892 -0.0420 -0.0291 155 ARG A NE 1184 C CZ . ARG A 155 ? 0.3676 0.7032 0.1383 0.0988 -0.0467 -0.0300 155 ARG A CZ 1185 N NH1 . ARG A 155 ? 0.3886 0.7490 0.1575 0.0969 -0.0529 -0.0470 155 ARG A NH1 1186 N NH2 . ARG A 155 ? 0.3823 0.7241 0.1470 0.1106 -0.0450 -0.0139 155 ARG A NH2 1187 N N . TRP A 156 ? 0.3309 0.5186 0.1541 0.0533 -0.0273 -0.0126 156 TRP A N 1188 C CA . TRP A 156 ? 0.3303 0.5043 0.1639 0.0467 -0.0271 -0.0108 156 TRP A CA 1189 C C . TRP A 156 ? 0.3292 0.4809 0.1693 0.0378 -0.0246 -0.0143 156 TRP A C 1190 O O . TRP A 156 ? 0.3334 0.4737 0.1704 0.0392 -0.0204 -0.0098 156 TRP A O 1191 C CB . TRP A 156 ? 0.3244 0.4927 0.1567 0.0533 -0.0233 0.0043 156 TRP A CB 1192 C CG . TRP A 156 ? 0.3217 0.4803 0.1637 0.0485 -0.0233 0.0065 156 TRP A CG 1193 C CD1 . TRP A 156 ? 0.3156 0.4809 0.1655 0.0425 -0.0276 -0.0018 156 TRP A CD1 1194 C CD2 . TRP A 156 ? 0.3136 0.4557 0.1582 0.0495 -0.0182 0.0175 156 TRP A CD2 1195 N NE1 . TRP A 156 ? 0.3029 0.4570 0.1595 0.0403 -0.0256 0.0039 156 TRP A NE1 1196 C CE2 . TRP A 156 ? 0.3171 0.4569 0.1706 0.0446 -0.0201 0.0152 156 TRP A CE2 1197 C CE3 . TRP A 156 ? 0.3248 0.4538 0.1657 0.0534 -0.0118 0.0281 156 TRP A CE3 1198 C CZ2 . TRP A 156 ? 0.3039 0.4289 0.1618 0.0440 -0.0162 0.0229 156 TRP A CZ2 1199 C CZ3 . TRP A 156 ? 0.3136 0.4275 0.1599 0.0519 -0.0078 0.0352 156 TRP A CZ3 1200 C CH2 . TRP A 156 ? 0.3092 0.4215 0.1635 0.0476 -0.0103 0.0322 156 TRP A CH2 1201 N N . GLY A 157 ? 0.3314 0.4777 0.1803 0.0292 -0.0267 -0.0220 157 GLY A N 1202 C CA . GLY A 157 ? 0.3318 0.4574 0.1863 0.0217 -0.0244 -0.0249 157 GLY A CA 1203 C C . GLY A 157 ? 0.3259 0.4345 0.1829 0.0218 -0.0202 -0.0141 157 GLY A C 1204 O O . GLY A 157 ? 0.3366 0.4299 0.1969 0.0177 -0.0181 -0.0150 157 GLY A O 1205 N N . ARG A 158 ? 0.3255 0.4372 0.1813 0.0270 -0.0189 -0.0042 158 ARG A N 1206 C CA . ARG A 158 ? 0.3185 0.4153 0.1771 0.0267 -0.0146 0.0050 158 ARG A CA 1207 C C . ARG A 158 ? 0.3301 0.4260 0.1825 0.0333 -0.0101 0.0138 158 ARG A C 1208 O O . ARG A 158 ? 0.3363 0.4224 0.1908 0.0338 -0.0059 0.0216 158 ARG A O 1209 C CB . ARG A 158 ? 0.3197 0.4162 0.1835 0.0260 -0.0151 0.0089 158 ARG A CB 1210 C CG . ARG A 158 ? 0.2993 0.4013 0.1691 0.0201 -0.0191 0.0008 158 ARG A CG 1211 C CD . ARG A 158 ? 0.3081 0.4072 0.1837 0.0190 -0.0186 0.0052 158 ARG A CD 1212 N NE . ARG A 158 ? 0.2871 0.3689 0.1667 0.0144 -0.0155 0.0078 158 ARG A NE 1213 C CZ . ARG A 158 ? 0.3005 0.3775 0.1858 0.0113 -0.0149 0.0095 158 ARG A CZ 1214 N NH1 . ARG A 158 ? 0.2688 0.3321 0.1565 0.0078 -0.0124 0.0113 158 ARG A NH1 1215 N NH2 . ARG A 158 ? 0.2891 0.3765 0.1773 0.0121 -0.0168 0.0089 158 ARG A NH2 1216 N N . CYS A 159 ? 0.3416 0.4481 0.1863 0.0382 -0.0103 0.0123 159 CYS A N 1217 C CA . CYS A 159 ? 0.3423 0.4481 0.1806 0.0442 -0.0051 0.0211 159 CYS A CA 1218 C C . CYS A 159 ? 0.3389 0.4293 0.1814 0.0402 -0.0002 0.0239 159 CYS A C 1219 O O . CYS A 159 ? 0.3349 0.4195 0.1769 0.0424 0.0055 0.0328 159 CYS A O 1220 C CB . CYS A 159 ? 0.3513 0.4720 0.1802 0.0497 -0.0062 0.0177 159 CYS A CB 1221 S SG . CYS A 159 ? 0.3794 0.5054 0.1982 0.0599 0.0000 0.0313 159 CYS A SG 1222 N N . TYR A 160 ? 0.3308 0.4146 0.1781 0.0345 -0.0020 0.0162 160 TYR A N 1223 C CA . TYR A 160 ? 0.3253 0.3977 0.1772 0.0313 0.0018 0.0181 160 TYR A CA 1224 C C . TYR A 160 ? 0.3197 0.3822 0.1783 0.0281 0.0040 0.0237 160 TYR A C 1225 O O . TYR A 160 ? 0.3221 0.3784 0.1842 0.0264 0.0081 0.0267 160 TYR A O 1226 C CB . TYR A 160 ? 0.3169 0.3848 0.1714 0.0277 -0.0005 0.0094 160 TYR A CB 1227 C CG . TYR A 160 ? 0.3116 0.3729 0.1718 0.0224 -0.0042 0.0044 160 TYR A CG 1228 C CD1 . TYR A 160 ? 0.3058 0.3574 0.1724 0.0188 -0.0032 0.0073 160 TYR A CD1 1229 C CD2 . TYR A 160 ? 0.3082 0.3735 0.1674 0.0207 -0.0081 -0.0038 160 TYR A CD2 1230 C CE1 . TYR A 160 ? 0.2970 0.3425 0.1678 0.0143 -0.0058 0.0036 160 TYR A CE1 1231 C CE2 . TYR A 160 ? 0.3012 0.3595 0.1658 0.0153 -0.0102 -0.0079 160 TYR A CE2 1232 C CZ . TYR A 160 ? 0.3036 0.3517 0.1735 0.0125 -0.0088 -0.0035 160 TYR A CZ 1233 O OH . TYR A 160 ? 0.2924 0.3336 0.1668 0.0074 -0.0102 -0.0067 160 TYR A OH 1234 N N . GLU A 161 ? 0.3108 0.3735 0.1717 0.0272 0.0015 0.0242 161 GLU A N 1235 C CA . GLU A 161 ? 0.3111 0.3654 0.1777 0.0246 0.0036 0.0286 161 GLU A CA 1236 C C . GLU A 161 ? 0.3188 0.3722 0.1831 0.0291 0.0087 0.0375 161 GLU A C 1237 O O . GLU A 161 ? 0.3189 0.3647 0.1878 0.0275 0.0114 0.0411 161 GLU A O 1238 C CB . GLU A 161 ? 0.3151 0.3701 0.1856 0.0219 -0.0007 0.0252 161 GLU A CB 1239 C CG . GLU A 161 ? 0.3044 0.3578 0.1773 0.0171 -0.0045 0.0172 161 GLU A CG 1240 C CD . GLU A 161 ? 0.3423 0.3933 0.2203 0.0130 -0.0068 0.0152 161 GLU A CD 1241 O OE1 . GLU A 161 ? 0.3384 0.3827 0.2205 0.0111 -0.0049 0.0185 161 GLU A OE1 1242 O OE2 . GLU A 161 ? 0.3424 0.3993 0.2207 0.0113 -0.0102 0.0098 161 GLU A OE2 1243 N N . SER A 162 ? 0.3197 0.3803 0.1765 0.0350 0.0106 0.0412 162 SER A N 1244 C CA . SER A 162 ? 0.3299 0.3882 0.1832 0.0403 0.0168 0.0512 162 SER A CA 1245 C C . SER A 162 ? 0.3325 0.3865 0.1849 0.0395 0.0234 0.0546 162 SER A C 1246 O O . SER A 162 ? 0.3369 0.3976 0.1857 0.0402 0.0224 0.0512 162 SER A O 1247 C CB . SER A 162 ? 0.3325 0.4036 0.1769 0.0489 0.0148 0.0544 162 SER A CB 1248 O OG . SER A 162 ? 0.3416 0.4106 0.1800 0.0557 0.0219 0.0654 162 SER A OG 1249 N N . TYR A 163 ? 0.3356 0.3787 0.1921 0.0376 0.0304 0.0606 163 TYR A N 1250 C CA . TYR A 163 ? 0.3401 0.3797 0.1975 0.0356 0.0378 0.0639 163 TYR A CA 1251 C C . TYR A 163 ? 0.3537 0.4004 0.2009 0.0430 0.0418 0.0707 163 TYR A C 1252 O O . TYR A 163 ? 0.3591 0.4086 0.2053 0.0420 0.0456 0.0708 163 TYR A O 1253 C CB . TYR A 163 ? 0.3400 0.3662 0.2043 0.0315 0.0456 0.0686 163 TYR A CB 1254 C CG . TYR A 163 ? 0.3332 0.3535 0.2074 0.0243 0.0427 0.0620 163 TYR A CG 1255 C CD1 . TYR A 163 ? 0.3228 0.3363 0.1991 0.0249 0.0423 0.0635 163 TYR A CD1 1256 C CD2 . TYR A 163 ? 0.2958 0.3182 0.1768 0.0177 0.0408 0.0547 163 TYR A CD2 1257 C CE1 . TYR A 163 ? 0.3262 0.3354 0.2107 0.0186 0.0400 0.0574 163 TYR A CE1 1258 C CE2 . TYR A 163 ? 0.3133 0.3320 0.2023 0.0120 0.0384 0.0492 163 TYR A CE2 1259 C CZ . TYR A 163 ? 0.3218 0.3339 0.2122 0.0122 0.0379 0.0504 163 TYR A CZ 1260 O OH . TYR A 163 ? 0.3041 0.3139 0.2016 0.0069 0.0354 0.0447 163 TYR A OH 1261 N N . SER A 164 ? 0.3697 0.4204 0.2090 0.0511 0.0413 0.0768 164 SER A N 1262 C CA . SER A 164 ? 0.3790 0.4372 0.2070 0.0597 0.0457 0.0850 164 SER A CA 1263 C C . SER A 164 ? 0.3940 0.4617 0.2131 0.0696 0.0420 0.0893 164 SER A C 1264 O O . SER A 164 ? 0.4022 0.4671 0.2249 0.0701 0.0387 0.0888 164 SER A O 1265 C CB . SER A 164 ? 0.3897 0.4351 0.2183 0.0595 0.0577 0.0956 164 SER A CB 1266 O OG . SER A 164 ? 0.3949 0.4472 0.2123 0.0673 0.0630 0.1039 164 SER A OG 1267 N N . GLU A 165 ? 0.4002 0.4810 0.2077 0.0780 0.0426 0.0934 165 GLU A N 1268 C CA . GLU A 165 ? 0.4133 0.5051 0.2107 0.0898 0.0412 0.1004 165 GLU A CA 1269 C C . GLU A 165 ? 0.4289 0.5071 0.2230 0.0961 0.0519 0.1160 165 GLU A C 1270 O O . GLU A 165 ? 0.4459 0.5298 0.2324 0.1070 0.0520 0.1241 165 GLU A O 1271 C CB . GLU A 165 ? 0.4167 0.5290 0.2018 0.0971 0.0384 0.0991 165 GLU A CB 1272 C CG . GLU A 165 ? 0.4268 0.5364 0.2041 0.1008 0.0484 0.1090 165 GLU A CG 1273 C CD . GLU A 165 ? 0.4507 0.5812 0.2163 0.1070 0.0454 0.1057 165 GLU A CD 1274 O OE1 . GLU A 165 ? 0.4709 0.6053 0.2255 0.1152 0.0529 0.1169 165 GLU A OE1 1275 O OE2 . GLU A 165 ? 0.4719 0.6147 0.2391 0.1036 0.0362 0.0919 165 GLU A OE2 1276 N N . ASP A 166 ? 0.4292 0.4898 0.2292 0.0893 0.0612 0.1199 166 ASP A N 1277 C CA . ASP A 166 ? 0.4457 0.4893 0.2444 0.0929 0.0732 0.1337 166 ASP A CA 1278 C C . ASP A 166 ? 0.4363 0.4619 0.2474 0.0857 0.0748 0.1313 166 ASP A C 1279 O O . ASP A 166 ? 0.4156 0.4332 0.2379 0.0738 0.0751 0.1232 166 ASP A O 1280 C CB . ASP A 166 ? 0.4565 0.4934 0.2546 0.0889 0.0836 0.1386 166 ASP A CB 1281 C CG . ASP A 166 ? 0.4887 0.5069 0.2845 0.0924 0.0980 0.1537 166 ASP A CG 1282 O OD1 . ASP A 166 ? 0.4843 0.4892 0.2823 0.0954 0.1009 0.1591 166 ASP A OD1 1283 O OD2 . ASP A 166 ? 0.5384 0.5546 0.3305 0.0920 0.1073 0.1603 166 ASP A OD2 1284 N N . ARG A 167 ? 0.4453 0.4661 0.2538 0.0937 0.0758 0.1382 167 ARG A N 1285 C CA . ARG A 167 ? 0.4473 0.4516 0.2663 0.0889 0.0777 0.1364 167 ARG A CA 1286 C C . ARG A 167 ? 0.4511 0.4336 0.2792 0.0787 0.0887 0.1375 167 ARG A C 1287 O O . ARG A 167 ? 0.4462 0.4194 0.2857 0.0695 0.0877 0.1296 167 ARG A O 1288 C CB . ARG A 167 ? 0.4601 0.4619 0.2730 0.1018 0.0796 0.1465 167 ARG A CB 1289 C CG . ARG A 167 ? 0.5142 0.5065 0.3167 0.1126 0.0917 0.1633 167 ARG A CG 1290 C CD . ARG A 167 ? 0.5558 0.5191 0.3649 0.1093 0.1049 0.1701 167 ARG A CD 1291 N NE . ARG A 167 ? 0.6297 0.5825 0.4278 0.1206 0.1175 0.1876 167 ARG A NE 1292 C CZ . ARG A 167 ? 0.6669 0.5928 0.4682 0.1193 0.1321 0.1965 167 ARG A CZ 1293 N NH1 . ARG A 167 ? 0.6654 0.5732 0.4809 0.1067 0.1355 0.1881 167 ARG A NH1 1294 N NH2 . ARG A 167 ? 0.6949 0.6116 0.4848 0.1306 0.1438 0.2136 167 ARG A NH2 1295 N N . ARG A 168 ? 0.4711 0.4469 0.2945 0.0802 0.0994 0.1469 168 ARG A N 1296 C CA . ARG A 168 ? 0.4828 0.4393 0.3157 0.0696 0.1110 0.1475 168 ARG A CA 1297 C C . ARG A 168 ? 0.4566 0.4187 0.3011 0.0555 0.1060 0.1332 168 ARG A C 1298 O O . ARG A 168 ? 0.4527 0.4022 0.3092 0.0448 0.1108 0.1278 168 ARG A O 1299 C CB . ARG A 168 ? 0.5035 0.4541 0.3286 0.0738 0.1237 0.1605 168 ARG A CB 1300 C CG . ARG A 168 ? 0.5735 0.5105 0.3895 0.0863 0.1332 0.1765 168 ARG A CG 1301 C CD . ARG A 168 ? 0.6612 0.5908 0.4699 0.0891 0.1472 0.1898 168 ARG A CD 1302 N NE . ARG A 168 ? 0.7661 0.6789 0.5659 0.1015 0.1584 0.2069 168 ARG A NE 1303 C CZ . ARG A 168 ? 0.8263 0.7496 0.6093 0.1185 0.1579 0.2196 168 ARG A CZ 1304 N NH1 . ARG A 168 ? 0.8308 0.7821 0.6049 0.1241 0.1462 0.2155 168 ARG A NH1 1305 N NH2 . ARG A 168 ? 0.8637 0.7699 0.6388 0.1305 0.1693 0.2362 168 ARG A NH2 1306 N N . ILE A 169 ? 0.4350 0.4163 0.2758 0.0559 0.0968 0.1268 169 ILE A N 1307 C CA . ILE A 169 ? 0.4142 0.4021 0.2647 0.0448 0.0913 0.1139 169 ILE A CA 1308 C C . ILE A 169 ? 0.3960 0.3838 0.2541 0.0405 0.0820 0.1039 169 ILE A C 1309 O O . ILE A 169 ? 0.3897 0.3731 0.2591 0.0305 0.0818 0.0958 169 ILE A O 1310 C CB . ILE A 169 ? 0.4109 0.4172 0.2550 0.0470 0.0856 0.1102 169 ILE A CB 1311 C CG1 . ILE A 169 ? 0.4190 0.4251 0.2569 0.0497 0.0963 0.1198 169 ILE A CG1 1312 C CG2 . ILE A 169 ? 0.3739 0.3867 0.2281 0.0372 0.0789 0.0968 169 ILE A CG2 1313 C CD1 . ILE A 169 ? 0.4274 0.4522 0.2549 0.0559 0.0919 0.1190 169 ILE A CD1 1314 N N . VAL A 170 ? 0.3901 0.3843 0.2424 0.0482 0.0745 0.1045 170 VAL A N 1315 C CA . VAL A 170 ? 0.3803 0.3740 0.2392 0.0448 0.0668 0.0964 170 VAL A CA 1316 C C . VAL A 170 ? 0.3869 0.3628 0.2544 0.0398 0.0740 0.0972 170 VAL A C 1317 O O . VAL A 170 ? 0.3794 0.3531 0.2564 0.0312 0.0711 0.0881 170 VAL A O 1318 C CB . VAL A 170 ? 0.3821 0.3866 0.2340 0.0540 0.0588 0.0975 170 VAL A CB 1319 C CG1 . VAL A 170 ? 0.3544 0.3578 0.2139 0.0499 0.0523 0.0897 170 VAL A CG1 1320 C CG2 . VAL A 170 ? 0.3724 0.3953 0.2169 0.0572 0.0514 0.0938 170 VAL A CG2 1321 N N . GLN A 171 ? 0.4084 0.3716 0.2722 0.0457 0.0836 0.1080 171 GLN A N 1322 C CA . GLN A 171 ? 0.4201 0.3635 0.2920 0.0408 0.0927 0.1089 171 GLN A CA 1323 C C . GLN A 171 ? 0.4210 0.3592 0.3046 0.0270 0.0970 0.1006 171 GLN A C 1324 O O . GLN A 171 ? 0.4193 0.3513 0.3124 0.0197 0.0966 0.0926 171 GLN A O 1325 C CB . GLN A 171 ? 0.4387 0.3674 0.3039 0.0493 0.1049 0.1233 171 GLN A CB 1326 C CG . GLN A 171 ? 0.4413 0.3703 0.2984 0.0628 0.1026 0.1309 171 GLN A CG 1327 C CD . GLN A 171 ? 0.4759 0.3890 0.3257 0.0725 0.1155 0.1464 171 GLN A CD 1328 O OE1 . GLN A 171 ? 0.5044 0.3994 0.3572 0.0749 0.1227 0.1501 171 GLN A OE1 1329 N NE2 . GLN A 171 ? 0.4554 0.3744 0.2952 0.0786 0.1192 0.1557 171 GLN A NE2 1330 N N . SER A 172 ? 0.4251 0.3679 0.3081 0.0238 0.1010 0.1021 172 SER A N 1331 C CA . SER A 172 ? 0.4226 0.3642 0.3171 0.0111 0.1051 0.0941 172 SER A CA 1332 C C . SER A 172 ? 0.4007 0.3546 0.3024 0.0045 0.0941 0.0807 172 SER A C 1333 O O . SER A 172 ? 0.3898 0.3416 0.3028 -0.0055 0.0960 0.0723 172 SER A O 1334 C CB . SER A 172 ? 0.4304 0.3781 0.3222 0.0102 0.1108 0.0984 172 SER A CB 1335 O OG . SER A 172 ? 0.4179 0.3840 0.3028 0.0148 0.1008 0.0960 172 SER A OG 1336 N N . MET A 173 ? 0.3830 0.3503 0.2782 0.0102 0.0829 0.0787 173 MET A N 1337 C CA . MET A 173 ? 0.3724 0.3509 0.2725 0.0054 0.0728 0.0677 173 MET A CA 1338 C C . MET A 173 ? 0.3592 0.3336 0.2637 0.0037 0.0681 0.0624 173 MET A C 1339 O O . MET A 173 ? 0.3396 0.3220 0.2480 -0.0001 0.0606 0.0540 173 MET A O 1340 C CB . MET A 173 ? 0.3609 0.3536 0.2529 0.0111 0.0640 0.0669 173 MET A CB 1341 C CG . MET A 173 ? 0.4022 0.4018 0.2900 0.0127 0.0676 0.0702 173 MET A CG 1342 S SD . MET A 173 ? 0.4599 0.4616 0.3594 0.0021 0.0731 0.0641 173 MET A SD 1343 C CE . MET A 173 ? 0.4188 0.4283 0.3117 0.0058 0.0787 0.0701 173 MET A CE 1344 N N . THR A 174 ? 0.3690 0.3310 0.2725 0.0071 0.0731 0.0676 174 THR A N 1345 C CA . THR A 174 ? 0.3579 0.3150 0.2665 0.0049 0.0707 0.0622 174 THR A CA 1346 C C . THR A 174 ? 0.3610 0.3160 0.2811 -0.0062 0.0731 0.0525 174 THR A C 1347 O O . THR A 174 ? 0.3405 0.2935 0.2652 -0.0090 0.0708 0.0463 174 THR A O 1348 C CB . THR A 174 ? 0.3723 0.3153 0.2779 0.0116 0.0768 0.0698 174 THR A CB 1349 O OG1 . THR A 174 ? 0.3802 0.3082 0.2878 0.0100 0.0894 0.0756 174 THR A OG1 1350 C CG2 . THR A 174 ? 0.3710 0.3211 0.2659 0.0233 0.0722 0.0776 174 THR A CG2 1351 N N . GLU A 175 ? 0.3654 0.3229 0.2901 -0.0124 0.0777 0.0507 175 GLU A N 1352 C CA . GLU A 175 ? 0.3627 0.3241 0.2988 -0.0230 0.0789 0.0401 175 GLU A CA 1353 C C . GLU A 175 ? 0.3444 0.3206 0.2817 -0.0243 0.0675 0.0316 175 GLU A C 1354 O O . GLU A 175 ? 0.3441 0.3256 0.2898 -0.0315 0.0668 0.0225 175 GLU A O 1355 C CB . GLU A 175 ? 0.3671 0.3317 0.3080 -0.0287 0.0857 0.0401 175 GLU A CB 1356 C CG . GLU A 175 ? 0.4002 0.3482 0.3444 -0.0319 0.0995 0.0455 175 GLU A CG 1357 C CD . GLU A 175 ? 0.4304 0.3670 0.3842 -0.0395 0.1050 0.0382 175 GLU A CD 1358 O OE1 . GLU A 175 ? 0.4488 0.3707 0.3991 -0.0347 0.1078 0.0426 175 GLU A OE1 1359 O OE2 . GLU A 175 ? 0.4264 0.3701 0.3914 -0.0499 0.1062 0.0275 175 GLU A OE2 1360 N N . LEU A 176 ? 0.3299 0.3131 0.2590 -0.0174 0.0593 0.0346 176 LEU A N 1361 C CA . LEU A 176 ? 0.3134 0.3072 0.2426 -0.0176 0.0496 0.0282 176 LEU A CA 1362 C C . LEU A 176 ? 0.3138 0.3034 0.2465 -0.0197 0.0485 0.0236 176 LEU A C 1363 O O . LEU A 176 ? 0.3055 0.3033 0.2418 -0.0232 0.0437 0.0163 176 LEU A O 1364 C CB . LEU A 176 ? 0.3072 0.3059 0.2273 -0.0102 0.0424 0.0322 176 LEU A CB 1365 C CG . LEU A 176 ? 0.2905 0.2988 0.2106 -0.0108 0.0338 0.0265 176 LEU A CG 1366 C CD1 . LEU A 176 ? 0.2694 0.2871 0.1908 -0.0120 0.0322 0.0237 176 LEU A CD1 1367 C CD2 . LEU A 176 ? 0.2993 0.3086 0.2124 -0.0054 0.0277 0.0289 176 LEU A CD2 1368 N N . ILE A 177 ? 0.3222 0.2996 0.2533 -0.0169 0.0533 0.0281 177 ILE A N 1369 C CA . ILE A 177 ? 0.3152 0.2877 0.2488 -0.0176 0.0530 0.0243 177 ILE A CA 1370 C C . ILE A 177 ? 0.3206 0.2936 0.2638 -0.0265 0.0562 0.0145 177 ILE A C 1371 O O . ILE A 177 ? 0.3217 0.3036 0.2666 -0.0285 0.0504 0.0077 177 ILE A O 1372 C CB . ILE A 177 ? 0.3321 0.2917 0.2617 -0.0109 0.0579 0.0319 177 ILE A CB 1373 C CG1 . ILE A 177 ? 0.3144 0.2806 0.2351 -0.0023 0.0514 0.0384 177 ILE A CG1 1374 C CG2 . ILE A 177 ? 0.3138 0.2666 0.2476 -0.0122 0.0598 0.0271 177 ILE A CG2 1375 C CD1 . ILE A 177 ? 0.3256 0.2836 0.2405 0.0065 0.0559 0.0482 177 ILE A CD1 1376 N N . PRO A 178 ? 0.3286 0.2931 0.2782 -0.0320 0.0656 0.0133 178 PRO A N 1377 C CA . PRO A 178 ? 0.3322 0.3004 0.2920 -0.0416 0.0681 0.0018 178 PRO A CA 1378 C C . PRO A 178 ? 0.3226 0.3104 0.2858 -0.0458 0.0617 -0.0051 178 PRO A C 1379 O O . PRO A 178 ? 0.3434 0.3399 0.3137 -0.0521 0.0608 -0.0155 178 PRO A O 1380 C CB . PRO A 178 ? 0.3514 0.3051 0.3173 -0.0470 0.0807 0.0029 178 PRO A CB 1381 C CG . PRO A 178 ? 0.3449 0.2939 0.3038 -0.0409 0.0833 0.0149 178 PRO A CG 1382 C CD . PRO A 178 ? 0.3465 0.2982 0.2946 -0.0303 0.0749 0.0219 178 PRO A CD 1383 N N . GLY A 179 ? 0.3145 0.3101 0.2726 -0.0416 0.0574 0.0002 179 GLY A N 1384 C CA . GLY A 179 ? 0.2872 0.3011 0.2467 -0.0426 0.0502 -0.0049 179 GLY A CA 1385 C C . GLY A 179 ? 0.2811 0.3021 0.2366 -0.0393 0.0416 -0.0078 179 GLY A C 1386 O O . GLY A 179 ? 0.2729 0.3063 0.2328 -0.0427 0.0383 -0.0159 179 GLY A O 1387 N N . LEU A 180 ? 0.2709 0.2853 0.2181 -0.0326 0.0382 -0.0011 180 LEU A N 1388 C CA . LEU A 180 ? 0.2662 0.2856 0.2093 -0.0296 0.0312 -0.0024 180 LEU A CA 1389 C C . LEU A 180 ? 0.2734 0.2917 0.2205 -0.0331 0.0327 -0.0091 180 LEU A C 1390 O O . LEU A 180 ? 0.2665 0.2953 0.2134 -0.0336 0.0279 -0.0141 180 LEU A O 1391 C CB . LEU A 180 ? 0.2613 0.2742 0.1963 -0.0229 0.0285 0.0054 180 LEU A CB 1392 C CG . LEU A 180 ? 0.2509 0.2672 0.1803 -0.0187 0.0248 0.0104 180 LEU A CG 1393 C CD1 . LEU A 180 ? 0.2636 0.2734 0.1869 -0.0134 0.0242 0.0169 180 LEU A CD1 1394 C CD2 . LEU A 180 ? 0.2369 0.2633 0.1644 -0.0177 0.0181 0.0078 180 LEU A CD2 1395 N N . GLN A 181 ? 0.2832 0.2887 0.2332 -0.0349 0.0398 -0.0089 181 GLN A N 1396 C CA . GLN A 181 ? 0.2932 0.2949 0.2462 -0.0370 0.0419 -0.0148 181 GLN A CA 1397 C C . GLN A 181 ? 0.3116 0.3146 0.2741 -0.0456 0.0473 -0.0253 181 GLN A C 1398 O O . GLN A 181 ? 0.3150 0.3199 0.2802 -0.0481 0.0475 -0.0331 181 GLN A O 1399 C CB . GLN A 181 ? 0.3025 0.2878 0.2527 -0.0325 0.0468 -0.0085 181 GLN A CB 1400 C CG . GLN A 181 ? 0.2997 0.2852 0.2415 -0.0243 0.0416 0.0004 181 GLN A CG 1401 C CD . GLN A 181 ? 0.2983 0.2716 0.2382 -0.0190 0.0458 0.0052 181 GLN A CD 1402 O OE1 . GLN A 181 ? 0.3476 0.3076 0.2900 -0.0191 0.0539 0.0072 181 GLN A OE1 1403 N NE2 . GLN A 181 ? 0.2662 0.2437 0.2018 -0.0141 0.0410 0.0074 181 GLN A NE2 1404 N N . GLY A 182 ? 0.3216 0.3243 0.2897 -0.0504 0.0521 -0.0262 182 GLY A N 1405 C CA . GLY A 182 ? 0.3447 0.3459 0.3235 -0.0599 0.0594 -0.0362 182 GLY A CA 1406 C C . GLY A 182 ? 0.3685 0.3469 0.3494 -0.0610 0.0704 -0.0315 182 GLY A C 1407 O O . GLY A 182 ? 0.3625 0.3276 0.3365 -0.0535 0.0715 -0.0224 182 GLY A O 1408 N N . ASP A 183 ? 0.3943 0.3689 0.3850 -0.0701 0.0789 -0.0374 183 ASP A N 1409 C CA . ASP A 183 ? 0.4334 0.3844 0.4270 -0.0719 0.0914 -0.0331 183 ASP A CA 1410 C C . ASP A 183 ? 0.4498 0.3865 0.4445 -0.0716 0.0955 -0.0377 183 ASP A C 1411 O O . ASP A 183 ? 0.4492 0.3955 0.4487 -0.0766 0.0926 -0.0503 183 ASP A O 1412 C CB . ASP A 183 ? 0.4472 0.3984 0.4526 -0.0836 0.1003 -0.0400 183 ASP A CB 1413 C CG . ASP A 183 ? 0.4658 0.4259 0.4699 -0.0829 0.0995 -0.0329 183 ASP A CG 1414 O OD1 . ASP A 183 ? 0.4970 0.4496 0.4912 -0.0738 0.0988 -0.0194 183 ASP A OD1 1415 O OD2 . ASP A 183 ? 0.5003 0.4763 0.5135 -0.0913 0.0996 -0.0416 183 ASP A OD2 1416 N N . VAL A 184 ? 0.4747 0.3897 0.4644 -0.0649 0.1022 -0.0275 184 VAL A N 1417 C CA . VAL A 184 ? 0.5001 0.3990 0.4910 -0.0634 0.1077 -0.0309 184 VAL A CA 1418 C C . VAL A 184 ? 0.5395 0.4254 0.5427 -0.0752 0.1198 -0.0419 184 VAL A C 1419 O O . VAL A 184 ? 0.5457 0.4295 0.5553 -0.0829 0.1265 -0.0422 184 VAL A O 1420 C CB . VAL A 184 ? 0.5078 0.3884 0.4894 -0.0508 0.1112 -0.0160 184 VAL A CB 1421 C CG1 . VAL A 184 ? 0.4760 0.3713 0.4472 -0.0406 0.0989 -0.0083 184 VAL A CG1 1422 C CG2 . VAL A 184 ? 0.5160 0.3797 0.4968 -0.0497 0.1217 -0.0046 184 VAL A CG2 1423 N N . PRO A 185 ? 0.5654 0.4437 0.5725 -0.0774 0.1230 -0.0521 185 PRO A N 1424 C CA . PRO A 185 ? 0.6001 0.4620 0.6188 -0.0883 0.1358 -0.0632 185 PRO A CA 1425 C C . PRO A 185 ? 0.6407 0.4728 0.6603 -0.0873 0.1507 -0.0523 185 PRO A C 1426 O O . PRO A 185 ? 0.6424 0.4646 0.6518 -0.0753 0.1510 -0.0353 185 PRO A O 1427 C CB . PRO A 185 ? 0.6042 0.4613 0.6225 -0.0856 0.1352 -0.0720 185 PRO A CB 1428 C CG . PRO A 185 ? 0.5733 0.4552 0.5840 -0.0795 0.1203 -0.0720 185 PRO A CG 1429 C CD . PRO A 185 ? 0.5587 0.4450 0.5600 -0.0705 0.1146 -0.0550 185 PRO A CD 1430 N N . LYS A 186 ? 0.6794 0.4984 0.7112 -0.1000 0.1631 -0.0623 186 LYS A N 1431 C CA . LYS A 186 ? 0.7294 0.5166 0.7635 -0.1007 0.1800 -0.0533 186 LYS A CA 1432 C C . LYS A 186 ? 0.7467 0.5083 0.7723 -0.0871 0.1854 -0.0429 186 LYS A C 1433 O O . LYS A 186 ? 0.7666 0.5092 0.7848 -0.0776 0.1926 -0.0256 186 LYS A O 1434 C CB . LYS A 186 ? 0.7559 0.5328 0.8066 -0.1185 0.1930 -0.0696 186 LYS A CB 1435 C CG . LYS A 186 ? 0.7715 0.5793 0.8334 -0.1331 0.1863 -0.0864 186 LYS A CG 1436 C CD . LYS A 186 ? 0.7902 0.6199 0.8546 -0.1357 0.1753 -0.1042 186 LYS A CD 1437 C CE . LYS A 186 ? 0.7657 0.6338 0.8277 -0.1354 0.1588 -0.1073 186 LYS A CE 1438 N NZ . LYS A 186 ? 0.7590 0.6451 0.8157 -0.1301 0.1464 -0.1154 186 LYS A NZ 1439 N N . ASP A 187 ? 0.7452 0.5084 0.7717 -0.0857 0.1817 -0.0537 187 ASP A N 1440 C CA . ASP A 187 ? 0.7640 0.5058 0.7842 -0.0731 0.1863 -0.0472 187 ASP A CA 1441 C C . ASP A 187 ? 0.7327 0.4817 0.7380 -0.0549 0.1766 -0.0299 187 ASP A C 1442 O O . ASP A 187 ? 0.7490 0.4816 0.7488 -0.0428 0.1807 -0.0225 187 ASP A O 1443 C CB . ASP A 187 ? 0.7787 0.5256 0.8046 -0.0779 0.1839 -0.0661 187 ASP A CB 1444 C CG . ASP A 187 ? 0.7825 0.5663 0.8099 -0.0843 0.1683 -0.0787 187 ASP A CG 1445 O OD1 . ASP A 187 ? 0.8164 0.6127 0.8535 -0.0985 0.1686 -0.0907 187 ASP A OD1 1446 O OD2 . ASP A 187 ? 0.7955 0.5962 0.8145 -0.0750 0.1562 -0.0763 187 ASP A OD2 1447 N N . PHE A 188 ? 0.6814 0.4552 0.6810 -0.0529 0.1642 -0.0241 188 PHE A N 1448 C CA . PHE A 188 ? 0.6347 0.4243 0.6227 -0.0394 0.1515 -0.0144 188 PHE A CA 1449 C C . PHE A 188 ? 0.6311 0.4046 0.6092 -0.0229 0.1556 0.0030 188 PHE A C 1450 O O . PHE A 188 ? 0.6436 0.4018 0.6187 -0.0192 0.1641 0.0154 188 PHE A O 1451 C CB . PHE A 188 ? 0.6051 0.4202 0.5895 -0.0411 0.1398 -0.0111 188 PHE A CB 1452 C CG . PHE A 188 ? 0.5811 0.4162 0.5564 -0.0315 0.1257 -0.0067 188 PHE A CG 1453 C CD1 . PHE A 188 ? 0.5615 0.4131 0.5385 -0.0341 0.1170 -0.0183 188 PHE A CD1 1454 C CD2 . PHE A 188 ? 0.5645 0.4026 0.5298 -0.0201 0.1217 0.0086 188 PHE A CD2 1455 C CE1 . PHE A 188 ? 0.5345 0.4033 0.5037 -0.0261 0.1053 -0.0141 188 PHE A CE1 1456 C CE2 . PHE A 188 ? 0.5332 0.3896 0.4916 -0.0126 0.1095 0.0114 188 PHE A CE2 1457 C CZ . PHE A 188 ? 0.5262 0.3971 0.4869 -0.0160 0.1017 0.0002 188 PHE A CZ 1458 N N . THR A 189 ? 0.6003 0.3795 0.5733 -0.0127 0.1493 0.0039 189 THR A N 1459 C CA . THR A 189 ? 0.5919 0.3626 0.5555 0.0042 0.1507 0.0197 189 THR A CA 1460 C C . THR A 189 ? 0.5568 0.3498 0.5110 0.0120 0.1387 0.0307 189 THR A C 1461 O O . THR A 189 ? 0.5271 0.3432 0.4797 0.0116 0.1261 0.0257 189 THR A O 1462 C CB . THR A 189 ? 0.5979 0.3640 0.5614 0.0123 0.1511 0.0155 189 THR A CB 1463 O OG1 . THR A 189 ? 0.6381 0.3799 0.6098 0.0060 0.1641 0.0060 189 THR A OG1 1464 C CG2 . THR A 189 ? 0.6026 0.3637 0.5567 0.0309 0.1519 0.0318 189 THR A CG2 1465 N N . SER A 190 ? 0.5465 0.3318 0.4942 0.0191 0.1432 0.0454 190 SER A N 1466 C CA . SER A 190 ? 0.5199 0.3247 0.4582 0.0274 0.1331 0.0559 190 SER A CA 1467 C C . SER A 190 ? 0.5014 0.3232 0.4353 0.0371 0.1224 0.0562 190 SER A C 1468 O O . SER A 190 ? 0.5098 0.3223 0.4430 0.0463 0.1264 0.0583 190 SER A O 1469 C CB . SER A 190 ? 0.5368 0.3282 0.4674 0.0377 0.1414 0.0729 190 SER A CB 1470 O OG . SER A 190 ? 0.5046 0.3163 0.4262 0.0447 0.1317 0.0814 190 SER A OG 1471 N N . GLY A 191 ? 0.4732 0.3197 0.4047 0.0347 0.1096 0.0537 191 GLY A N 1472 C CA . GLY A 191 ? 0.4479 0.3128 0.3763 0.0419 0.0994 0.0533 191 GLY A CA 1473 C C . GLY A 191 ? 0.4322 0.3073 0.3664 0.0340 0.0936 0.0396 191 GLY A C 1474 O O . GLY A 191 ? 0.4081 0.3013 0.3403 0.0369 0.0844 0.0382 191 GLY A O 1475 N N . MET A 192 ? 0.4343 0.2988 0.3757 0.0238 0.0992 0.0292 192 MET A N 1476 C CA . MET A 192 ? 0.4262 0.3023 0.3724 0.0158 0.0937 0.0157 192 MET A CA 1477 C C . MET A 192 ? 0.3988 0.2949 0.3443 0.0080 0.0837 0.0122 192 MET A C 1478 O O . MET A 192 ? 0.3940 0.2898 0.3388 0.0043 0.0841 0.0157 192 MET A O 1479 C CB . MET A 192 ? 0.4444 0.3048 0.3987 0.0071 0.1029 0.0045 192 MET A CB 1480 C CG . MET A 192 ? 0.4713 0.3133 0.4270 0.0145 0.1119 0.0044 192 MET A CG 1481 S SD . MET A 192 ? 0.5224 0.3803 0.4762 0.0216 0.1043 -0.0001 192 MET A SD 1482 C CE . MET A 192 ? 0.4902 0.3567 0.4509 0.0076 0.1023 -0.0194 192 MET A CE 1483 N N . PRO A 193 ? 0.3803 0.2936 0.3254 0.0063 0.0751 0.0059 193 PRO A N 1484 C CA . PRO A 193 ? 0.3599 0.2900 0.3042 -0.0004 0.0666 0.0030 193 PRO A CA 1485 C C . PRO A 193 ? 0.3624 0.2922 0.3130 -0.0116 0.0690 -0.0080 193 PRO A C 1486 O O . PRO A 193 ? 0.3703 0.2903 0.3263 -0.0150 0.0756 -0.0159 193 PRO A O 1487 C CB . PRO A 193 ? 0.3435 0.2896 0.2853 0.0020 0.0586 0.0008 193 PRO A CB 1488 C CG . PRO A 193 ? 0.3522 0.2912 0.2965 0.0052 0.0635 -0.0038 193 PRO A CG 1489 C CD . PRO A 193 ? 0.3789 0.2973 0.3241 0.0107 0.0732 0.0020 193 PRO A CD 1490 N N . PHE A 194 ? 0.3507 0.2917 0.3013 -0.0171 0.0639 -0.0091 194 PHE A N 1491 C CA . PHE A 194 ? 0.3583 0.3043 0.3152 -0.0273 0.0648 -0.0198 194 PHE A CA 1492 C C . PHE A 194 ? 0.3428 0.3075 0.2975 -0.0300 0.0559 -0.0209 194 PHE A C 1493 O O . PHE A 194 ? 0.3432 0.3110 0.2935 -0.0268 0.0524 -0.0127 194 PHE A O 1494 C CB . PHE A 194 ? 0.3713 0.3030 0.3338 -0.0325 0.0743 -0.0200 194 PHE A CB 1495 C CG . PHE A 194 ? 0.3767 0.3158 0.3475 -0.0437 0.0756 -0.0325 194 PHE A CG 1496 C CD1 . PHE A 194 ? 0.3790 0.3140 0.3566 -0.0496 0.0805 -0.0449 194 PHE A CD1 1497 C CD2 . PHE A 194 ? 0.3595 0.3117 0.3316 -0.0482 0.0716 -0.0330 194 PHE A CD2 1498 C CE1 . PHE A 194 ? 0.4048 0.3501 0.3907 -0.0604 0.0812 -0.0581 194 PHE A CE1 1499 C CE2 . PHE A 194 ? 0.3632 0.3259 0.3435 -0.0580 0.0722 -0.0451 194 PHE A CE2 1500 C CZ . PHE A 194 ? 0.3755 0.3356 0.3630 -0.0645 0.0769 -0.0581 194 PHE A CZ 1501 N N . VAL A 195 ? 0.3366 0.3141 0.2941 -0.0353 0.0525 -0.0312 195 VAL A N 1502 C CA . VAL A 195 ? 0.3258 0.3204 0.2827 -0.0385 0.0457 -0.0337 195 VAL A CA 1503 C C . VAL A 195 ? 0.3360 0.3390 0.3001 -0.0465 0.0474 -0.0474 195 VAL A C 1504 O O . VAL A 195 ? 0.3418 0.3439 0.3076 -0.0477 0.0493 -0.0549 195 VAL A O 1505 C CB . VAL A 195 ? 0.3091 0.3163 0.2586 -0.0334 0.0370 -0.0300 195 VAL A CB 1506 C CG1 . VAL A 195 ? 0.2864 0.3093 0.2348 -0.0353 0.0310 -0.0318 195 VAL A CG1 1507 C CG2 . VAL A 195 ? 0.2926 0.2933 0.2361 -0.0262 0.0354 -0.0186 195 VAL A CG2 1508 N N . ALA A 196 ? 0.3420 0.3541 0.3108 -0.0520 0.0469 -0.0513 196 ALA A N 1509 C CA . ALA A 196 ? 0.3534 0.3750 0.3309 -0.0609 0.0492 -0.0655 196 ALA A CA 1510 C C . ALA A 196 ? 0.3564 0.3980 0.3316 -0.0606 0.0423 -0.0739 196 ALA A C 1511 O O . ALA A 196 ? 0.3844 0.4317 0.3654 -0.0664 0.0447 -0.0868 196 ALA A O 1512 C CB . ALA A 196 ? 0.3455 0.3744 0.3293 -0.0665 0.0505 -0.0673 196 ALA A CB 1513 N N . GLY A 197 ? 0.3458 0.3983 0.3126 -0.0539 0.0343 -0.0668 197 GLY A N 1514 C CA . GLY A 197 ? 0.3466 0.4184 0.3095 -0.0523 0.0280 -0.0725 197 GLY A CA 1515 C C . GLY A 197 ? 0.3408 0.4229 0.2955 -0.0457 0.0205 -0.0633 197 GLY A C 1516 O O . GLY A 197 ? 0.3330 0.4051 0.2840 -0.0417 0.0199 -0.0524 197 GLY A O 1517 N N . LYS A 198 ? 0.3426 0.4450 0.2944 -0.0443 0.0151 -0.0680 198 LYS A N 1518 C CA . LYS A 198 ? 0.3400 0.4512 0.2827 -0.0368 0.0086 -0.0591 198 LYS A CA 1519 C C . LYS A 198 ? 0.3336 0.4469 0.2765 -0.0349 0.0064 -0.0530 198 LYS A C 1520 O O . LYS A 198 ? 0.3387 0.4525 0.2741 -0.0285 0.0025 -0.0439 198 LYS A O 1521 C CB . LYS A 198 ? 0.3401 0.4728 0.2785 -0.0346 0.0042 -0.0651 198 LYS A CB 1522 C CG . LYS A 198 ? 0.3488 0.5024 0.2938 -0.0385 0.0026 -0.0764 198 LYS A CG 1523 C CD . LYS A 198 ? 0.3669 0.5439 0.3058 -0.0344 -0.0025 -0.0811 198 LYS A CD 1524 C CE . LYS A 198 ? 0.3910 0.5926 0.3356 -0.0362 -0.0056 -0.0903 198 LYS A CE 1525 N NZ . LYS A 198 ? 0.4172 0.6444 0.3562 -0.0323 -0.0103 -0.0968 198 LYS A NZ 1526 N N . ASN A 199 ? 0.3313 0.4451 0.2829 -0.0405 0.0095 -0.0581 199 ASN A N 1527 C CA . ASN A 199 ? 0.3252 0.4414 0.2777 -0.0386 0.0081 -0.0529 199 ASN A CA 1528 C C . ASN A 199 ? 0.3175 0.4132 0.2698 -0.0384 0.0120 -0.0442 199 ASN A C 1529 O O . ASN A 199 ? 0.3120 0.4080 0.2649 -0.0370 0.0116 -0.0399 199 ASN A O 1530 C CB . ASN A 199 ? 0.3298 0.4633 0.2919 -0.0442 0.0087 -0.0633 199 ASN A CB 1531 C CG . ASN A 199 ? 0.3570 0.5157 0.3179 -0.0424 0.0033 -0.0712 199 ASN A CG 1532 O OD1 . ASN A 199 ? 0.3816 0.5534 0.3506 -0.0491 0.0048 -0.0840 199 ASN A OD1 1533 N ND2 . ASN A 199 ? 0.3695 0.5351 0.3203 -0.0333 -0.0024 -0.0636 199 ASN A ND2 1534 N N . LYS A 200 ? 0.3120 0.3914 0.2629 -0.0389 0.0155 -0.0417 200 LYS A N 1535 C CA . LYS A 200 ? 0.2975 0.3588 0.2471 -0.0375 0.0191 -0.0333 200 LYS A CA 1536 C C . LYS A 200 ? 0.2920 0.3457 0.2334 -0.0317 0.0165 -0.0256 200 LYS A C 1537 O O . LYS A 200 ? 0.2882 0.3483 0.2259 -0.0298 0.0134 -0.0271 200 LYS A O 1538 C CB . LYS A 200 ? 0.3018 0.3504 0.2584 -0.0431 0.0272 -0.0371 200 LYS A CB 1539 C CG . LYS A 200 ? 0.3071 0.3615 0.2735 -0.0507 0.0315 -0.0449 200 LYS A CG 1540 C CD . LYS A 200 ? 0.2914 0.3458 0.2576 -0.0493 0.0317 -0.0384 200 LYS A CD 1541 C CE . LYS A 200 ? 0.3052 0.3660 0.2820 -0.0573 0.0368 -0.0456 200 LYS A CE 1542 N NZ . LYS A 200 ? 0.2850 0.3433 0.2609 -0.0554 0.0383 -0.0381 200 LYS A NZ 1543 N N . VAL A 201 ? 0.2808 0.3227 0.2193 -0.0288 0.0177 -0.0175 201 VAL A N 1544 C CA . VAL A 201 ? 0.2713 0.3075 0.2035 -0.0240 0.0155 -0.0109 201 VAL A CA 1545 C C . VAL A 201 ? 0.2810 0.3039 0.2143 -0.0230 0.0202 -0.0077 201 VAL A C 1546 O O . VAL A 201 ? 0.2882 0.3038 0.2253 -0.0250 0.0253 -0.0077 201 VAL A O 1547 C CB . VAL A 201 ? 0.2643 0.3017 0.1912 -0.0201 0.0113 -0.0042 201 VAL A CB 1548 C CG1 . VAL A 201 ? 0.2517 0.3007 0.1764 -0.0190 0.0069 -0.0058 201 VAL A CG1 1549 C CG2 . VAL A 201 ? 0.2416 0.2737 0.1698 -0.0201 0.0136 -0.0010 201 VAL A CG2 1550 N N . ALA A 202 ? 0.2820 0.3023 0.2119 -0.0196 0.0191 -0.0045 202 ALA A N 1551 C CA . ALA A 202 ? 0.2849 0.2951 0.2142 -0.0162 0.0224 0.0005 202 ALA A CA 1552 C C . ALA A 202 ? 0.2845 0.2928 0.2105 -0.0133 0.0209 0.0073 202 ALA A C 1553 O O . ALA A 202 ? 0.2778 0.2920 0.2004 -0.0126 0.0161 0.0090 202 ALA A O 1554 C CB . ALA A 202 ? 0.2807 0.2927 0.2079 -0.0130 0.0208 0.0015 202 ALA A CB 1555 N N . ALA A 203 ? 0.2928 0.2925 0.2193 -0.0112 0.0255 0.0112 203 ALA A N 1556 C CA . ALA A 203 ? 0.2935 0.2924 0.2160 -0.0076 0.0246 0.0176 203 ALA A CA 1557 C C . ALA A 203 ? 0.2984 0.2964 0.2176 -0.0015 0.0238 0.0226 203 ALA A C 1558 O O . ALA A 203 ? 0.2979 0.2949 0.2185 0.0000 0.0247 0.0215 203 ALA A O 1559 C CB . ALA A 203 ? 0.2928 0.2846 0.2172 -0.0087 0.0306 0.0195 203 ALA A CB 1560 N N . CYS A 204 ? 0.3068 0.3069 0.2218 0.0023 0.0222 0.0276 204 CYS A N 1561 C CA . CYS A 204 ? 0.3097 0.3135 0.2214 0.0082 0.0203 0.0317 204 CYS A CA 1562 C C . CYS A 204 ? 0.3154 0.3188 0.2227 0.0131 0.0218 0.0376 204 CYS A C 1563 O O . CYS A 204 ? 0.3096 0.3181 0.2139 0.0123 0.0186 0.0374 204 CYS A O 1564 C CB . CYS A 204 ? 0.2968 0.3105 0.2075 0.0067 0.0138 0.0291 204 CYS A CB 1565 S SG . CYS A 204 ? 0.3209 0.3439 0.2295 0.0125 0.0107 0.0319 204 CYS A SG 1566 N N . ALA A 205 ? 0.3263 0.3234 0.2324 0.0189 0.0270 0.0431 205 ALA A N 1567 C CA . ALA A 205 ? 0.3351 0.3337 0.2353 0.0254 0.0283 0.0500 205 ALA A CA 1568 C C . ALA A 205 ? 0.3333 0.3460 0.2301 0.0302 0.0218 0.0504 205 ALA A C 1569 O O . ALA A 205 ? 0.3333 0.3502 0.2316 0.0336 0.0205 0.0503 205 ALA A O 1570 C CB . ALA A 205 ? 0.3503 0.3372 0.2497 0.0312 0.0366 0.0569 205 ALA A CB 1571 N N . LYS A 206 ? 0.3277 0.3487 0.2204 0.0302 0.0179 0.0499 206 LYS A N 1572 C CA . LYS A 206 ? 0.3242 0.3600 0.2145 0.0332 0.0116 0.0482 206 LYS A CA 1573 C C . LYS A 206 ? 0.3306 0.3743 0.2137 0.0385 0.0105 0.0515 206 LYS A C 1574 O O . LYS A 206 ? 0.3404 0.3778 0.2205 0.0385 0.0142 0.0544 206 LYS A O 1575 C CB . LYS A 206 ? 0.3098 0.3499 0.2038 0.0253 0.0063 0.0404 206 LYS A CB 1576 C CG . LYS A 206 ? 0.3185 0.3557 0.2114 0.0202 0.0053 0.0373 206 LYS A CG 1577 C CD . LYS A 206 ? 0.2966 0.3355 0.1926 0.0136 0.0012 0.0310 206 LYS A CD 1578 C CE . LYS A 206 ? 0.2932 0.3305 0.1870 0.0108 0.0000 0.0283 206 LYS A CE 1579 N NZ . LYS A 206 ? 0.3003 0.3365 0.1964 0.0053 -0.0029 0.0233 206 LYS A NZ 1580 N N . HIS A 207 ? 0.3331 0.3923 0.2135 0.0433 0.0058 0.0507 207 HIS A N 1581 C CA . HIS A 207 ? 0.3345 0.4042 0.2187 0.0450 0.0023 0.0483 207 HIS A CA 1582 C C . HIS A 207 ? 0.3404 0.4163 0.2204 0.0569 0.0044 0.0561 207 HIS A C 1583 O O . HIS A 207 ? 0.3536 0.4389 0.2266 0.0637 0.0035 0.0596 207 HIS A O 1584 C CB . HIS A 207 ? 0.3274 0.4125 0.2127 0.0409 -0.0047 0.0403 207 HIS A CB 1585 C CG . HIS A 207 ? 0.3426 0.4214 0.2293 0.0317 -0.0062 0.0342 207 HIS A CG 1586 N ND1 . HIS A 207 ? 0.3401 0.4175 0.2217 0.0316 -0.0061 0.0338 207 HIS A ND1 1587 C CD2 . HIS A 207 ? 0.3257 0.3993 0.2177 0.0233 -0.0074 0.0288 207 HIS A CD2 1588 C CE1 . HIS A 207 ? 0.3290 0.4002 0.2132 0.0239 -0.0073 0.0282 207 HIS A CE1 1589 N NE2 . HIS A 207 ? 0.3076 0.3761 0.1976 0.0190 -0.0081 0.0255 207 HIS A NE2 1590 N N . PHE A 208 ? 0.3388 0.4095 0.2225 0.0601 0.0074 0.0588 208 PHE A N 1591 C CA . PHE A 208 ? 0.3457 0.4173 0.2256 0.0725 0.0112 0.0676 208 PHE A CA 1592 C C . PHE A 208 ? 0.3403 0.4367 0.2189 0.0802 0.0052 0.0668 208 PHE A C 1593 O O . PHE A 208 ? 0.3323 0.4400 0.2173 0.0762 0.0006 0.0600 208 PHE A O 1594 C CB . PHE A 208 ? 0.3406 0.3978 0.2260 0.0724 0.0165 0.0689 208 PHE A CB 1595 C CG . PHE A 208 ? 0.3749 0.4279 0.2571 0.0854 0.0221 0.0783 208 PHE A CG 1596 C CD1 . PHE A 208 ? 0.3573 0.3910 0.2354 0.0894 0.0309 0.0867 208 PHE A CD1 1597 C CD2 . PHE A 208 ? 0.3619 0.4298 0.2459 0.0939 0.0194 0.0790 208 PHE A CD2 1598 C CE1 . PHE A 208 ? 0.4172 0.4441 0.2919 0.1022 0.0373 0.0963 208 PHE A CE1 1599 C CE2 . PHE A 208 ? 0.4018 0.4652 0.2824 0.1077 0.0251 0.0885 208 PHE A CE2 1600 C CZ . PHE A 208 ? 0.3966 0.4381 0.2722 0.1122 0.0343 0.0976 208 PHE A CZ 1601 N N . VAL A 209 ? 0.3477 0.4544 0.2181 0.0910 0.0051 0.0734 209 VAL A N 1602 C CA . VAL A 209 ? 0.3552 0.4512 0.2170 0.0954 0.0104 0.0816 209 VAL A CA 1603 C C . VAL A 209 ? 0.3643 0.4825 0.2182 0.1013 0.0051 0.0813 209 VAL A C 1604 O O . VAL A 209 ? 0.3575 0.4988 0.2118 0.1066 -0.0010 0.0782 209 VAL A O 1605 C CB . VAL A 209 ? 0.3731 0.4530 0.2313 0.1063 0.0197 0.0941 209 VAL A CB 1606 C CG1 . VAL A 209 ? 0.3770 0.4731 0.2322 0.1211 0.0183 0.0999 209 VAL A CG1 1607 C CG2 . VAL A 209 ? 0.3878 0.4542 0.2376 0.1093 0.0270 0.1031 209 VAL A CG2 1608 N N . GLY A 210 ? 0.3729 0.4857 0.2202 0.1002 0.0075 0.0838 210 GLY A N 1609 C CA . GLY A 210 ? 0.3808 0.5135 0.2190 0.1065 0.0035 0.0839 210 GLY A CA 1610 C C . GLY A 210 ? 0.3738 0.5203 0.2156 0.0962 -0.0046 0.0701 210 GLY A C 1611 O O . GLY A 210 ? 0.3758 0.5446 0.2125 0.1003 -0.0101 0.0661 210 GLY A O 1612 N N . ASP A 211 ? 0.3606 0.4937 0.2109 0.0833 -0.0050 0.0626 211 ASP A N 1613 C CA . ASP A 211 ? 0.3557 0.4950 0.2097 0.0726 -0.0106 0.0503 211 ASP A CA 1614 C C . ASP A 211 ? 0.3594 0.5034 0.2056 0.0732 -0.0112 0.0486 211 ASP A C 1615 O O . ASP A 211 ? 0.3552 0.5129 0.2017 0.0690 -0.0169 0.0383 211 ASP A O 1616 C CB . ASP A 211 ? 0.3424 0.4633 0.2053 0.0605 -0.0093 0.0454 211 ASP A CB 1617 C CG . ASP A 211 ? 0.3433 0.4418 0.2057 0.0592 -0.0020 0.0523 211 ASP A CG 1618 O OD1 . ASP A 211 ? 0.3830 0.4758 0.2404 0.0671 0.0035 0.0621 211 ASP A OD1 1619 O OD2 . ASP A 211 ? 0.3658 0.4522 0.2332 0.0499 -0.0014 0.0478 211 ASP A OD2 1620 N N . GLY A 212 ? 0.3688 0.5014 0.2083 0.0782 -0.0047 0.0582 212 GLY A N 1621 C CA . GLY A 212 ? 0.3723 0.5094 0.2033 0.0801 -0.0040 0.0582 212 GLY A CA 1622 C C . GLY A 212 ? 0.3891 0.5478 0.2093 0.0925 -0.0058 0.0624 212 GLY A C 1623 O O . GLY A 212 ? 0.3895 0.5536 0.2015 0.0953 -0.0048 0.0630 212 GLY A O 1624 N N . GLY A 213 ? 0.3896 0.5624 0.2095 0.1005 -0.0086 0.0651 213 GLY A N 1625 C CA . GLY A 213 ? 0.4100 0.6053 0.2187 0.1143 -0.0103 0.0705 213 GLY A CA 1626 C C . GLY A 213 ? 0.4169 0.6428 0.2267 0.1154 -0.0200 0.0591 213 GLY A C 1627 O O . GLY A 213 ? 0.4295 0.6778 0.2315 0.1282 -0.0223 0.0635 213 GLY A O 1628 N N . THR A 214 ? 0.4013 0.6291 0.2207 0.1023 -0.0253 0.0444 214 THR A N 1629 C CA . THR A 214 ? 0.4052 0.6612 0.2286 0.1007 -0.0338 0.0317 214 THR A CA 1630 C C . THR A 214 ? 0.4195 0.7000 0.2333 0.1054 -0.0382 0.0254 214 THR A C 1631 O O . THR A 214 ? 0.4263 0.6982 0.2331 0.1045 -0.0353 0.0260 214 THR A O 1632 C CB . THR A 214 ? 0.3871 0.6365 0.2238 0.0846 -0.0370 0.0180 214 THR A CB 1633 O OG1 . THR A 214 ? 0.3942 0.6302 0.2304 0.0754 -0.0359 0.0113 214 THR A OG1 1634 C CG2 . THR A 214 ? 0.3765 0.6052 0.2220 0.0805 -0.0331 0.0236 214 THR A CG2 1635 N N . VAL A 215 ? 0.4238 0.7360 0.2374 0.1106 -0.0450 0.0188 215 VAL A N 1636 C CA . VAL A 215 ? 0.4414 0.7813 0.2460 0.1155 -0.0500 0.0111 215 VAL A CA 1637 C C . VAL A 215 ? 0.4330 0.7667 0.2414 0.1013 -0.0517 -0.0047 215 VAL A C 1638 O O . VAL A 215 ? 0.4149 0.7403 0.2358 0.0875 -0.0534 -0.0158 215 VAL A O 1639 C CB . VAL A 215 ? 0.4483 0.8276 0.2533 0.1234 -0.0578 0.0051 215 VAL A CB 1640 C CG1 . VAL A 215 ? 0.4508 0.8348 0.2721 0.1125 -0.0617 -0.0057 215 VAL A CG1 1641 C CG2 . VAL A 215 ? 0.4650 0.8750 0.2622 0.1257 -0.0638 -0.0071 215 VAL A CG2 1642 N N . ASP A 216 ? 0.4427 0.7789 0.2397 0.1053 -0.0503 -0.0045 216 ASP A N 1643 C CA . ASP A 216 ? 0.4384 0.7690 0.2367 0.0944 -0.0512 -0.0186 216 ASP A CA 1644 C C . ASP A 216 ? 0.4212 0.7166 0.2287 0.0819 -0.0463 -0.0188 216 ASP A C 1645 O O . ASP A 216 ? 0.4207 0.7093 0.2328 0.0713 -0.0473 -0.0318 216 ASP A O 1646 C CB . ASP A 216 ? 0.4432 0.8002 0.2477 0.0873 -0.0592 -0.0390 216 ASP A CB 1647 C CG . ASP A 216 ? 0.4760 0.8718 0.2702 0.0996 -0.0647 -0.0416 216 ASP A CG 1648 O OD1 . ASP A 216 ? 0.4908 0.8911 0.2705 0.1132 -0.0618 -0.0289 216 ASP A OD1 1649 O OD2 . ASP A 216 ? 0.4899 0.9126 0.2904 0.0955 -0.0717 -0.0568 216 ASP A OD2 1650 N N . GLY A 217 ? 0.4087 0.6824 0.2184 0.0838 -0.0408 -0.0045 217 GLY A N 1651 C CA . GLY A 217 ? 0.3900 0.6334 0.2086 0.0731 -0.0366 -0.0037 217 GLY A CA 1652 C C . GLY A 217 ? 0.3806 0.6219 0.2123 0.0606 -0.0404 -0.0162 217 GLY A C 1653 O O . GLY A 217 ? 0.3802 0.6007 0.2181 0.0507 -0.0382 -0.0203 217 GLY A O 1654 N N . ILE A 218 ? 0.3745 0.6381 0.2105 0.0612 -0.0457 -0.0221 218 ILE A N 1655 C CA . ILE A 218 ? 0.3585 0.6219 0.2076 0.0488 -0.0484 -0.0341 218 ILE A CA 1656 C C . ILE A 218 ? 0.3531 0.5948 0.2098 0.0453 -0.0446 -0.0253 218 ILE A C 1657 O O . ILE A 218 ? 0.3554 0.5997 0.2112 0.0534 -0.0434 -0.0145 218 ILE A O 1658 C CB . ILE A 218 ? 0.3649 0.6622 0.2179 0.0496 -0.0552 -0.0446 218 ILE A CB 1659 C CG1 . ILE A 218 ? 0.3510 0.6709 0.1966 0.0518 -0.0593 -0.0559 218 ILE A CG1 1660 C CG2 . ILE A 218 ? 0.3529 0.6477 0.2207 0.0357 -0.0565 -0.0555 218 ILE A CG2 1661 C CD1 . ILE A 218 ? 0.3727 0.7326 0.2182 0.0578 -0.0663 -0.0632 218 ILE A CD1 1662 N N . ASN A 219 ? 0.3438 0.5638 0.2074 0.0340 -0.0422 -0.0297 219 ASN A N 1663 C CA . ASN A 219 ? 0.3338 0.5332 0.2039 0.0303 -0.0384 -0.0223 219 ASN A CA 1664 C C . ASN A 219 ? 0.3295 0.5422 0.2077 0.0294 -0.0408 -0.0233 219 ASN A C 1665 O O . ASN A 219 ? 0.3322 0.5630 0.2162 0.0241 -0.0449 -0.0348 219 ASN A O 1666 C CB . ASN A 219 ? 0.3259 0.5032 0.2011 0.0190 -0.0360 -0.0278 219 ASN A CB 1667 C CG . ASN A 219 ? 0.3152 0.4713 0.1950 0.0162 -0.0319 -0.0195 219 ASN A CG 1668 O OD1 . ASN A 219 ? 0.3524 0.4980 0.2394 0.0072 -0.0310 -0.0241 219 ASN A OD1 1669 N ND2 . ASN A 219 ? 0.2712 0.4207 0.1469 0.0238 -0.0289 -0.0076 219 ASN A ND2 1670 N N . GLU A 220 ? 0.3255 0.5301 0.2043 0.0347 -0.0379 -0.0120 220 GLU A N 1671 C CA . GLU A 220 ? 0.3270 0.5419 0.2135 0.0350 -0.0391 -0.0114 220 GLU A CA 1672 C C . GLU A 220 ? 0.3405 0.5864 0.2250 0.0446 -0.0437 -0.0123 220 GLU A C 1673 O O . GLU A 220 ? 0.3414 0.6021 0.2334 0.0445 -0.0458 -0.0147 220 GLU A O 1674 C CB . GLU A 220 ? 0.3199 0.5322 0.2175 0.0213 -0.0398 -0.0219 220 GLU A CB 1675 C CG . GLU A 220 ? 0.3145 0.4977 0.2136 0.0128 -0.0354 -0.0207 220 GLU A CG 1676 C CD . GLU A 220 ? 0.3242 0.5028 0.2335 0.0006 -0.0348 -0.0281 220 GLU A CD 1677 O OE1 . GLU A 220 ? 0.3361 0.5327 0.2527 -0.0019 -0.0370 -0.0332 220 GLU A OE1 1678 O OE2 . GLU A 220 ? 0.3549 0.5122 0.2647 -0.0060 -0.0316 -0.0284 220 GLU A OE2 1679 N N . ASN A 221 ? 0.3476 0.6046 0.2218 0.0536 -0.0451 -0.0101 221 ASN A N 1680 C CA . ASN A 221 ? 0.3588 0.6493 0.2301 0.0630 -0.0504 -0.0126 221 ASN A CA 1681 C C . ASN A 221 ? 0.3633 0.6591 0.2278 0.0795 -0.0485 0.0024 221 ASN A C 1682 O O . ASN A 221 ? 0.3595 0.6344 0.2253 0.0816 -0.0432 0.0127 221 ASN A O 1683 C CB . ASN A 221 ? 0.3616 0.6667 0.2253 0.0637 -0.0538 -0.0208 221 ASN A CB 1684 C CG . ASN A 221 ? 0.3904 0.7336 0.2569 0.0653 -0.0611 -0.0326 221 ASN A CG 1685 O OD1 . ASN A 221 ? 0.3930 0.7594 0.2503 0.0784 -0.0640 -0.0289 221 ASN A OD1 1686 N ND2 . ASN A 221 ? 0.4114 0.7620 0.2908 0.0520 -0.0638 -0.0468 221 ASN A ND2 1687 N N . ASN A 222 ? 0.3776 0.7011 0.2345 0.0915 -0.0523 0.0035 222 ASN A N 1688 C CA . ASN A 222 ? 0.3938 0.7242 0.2437 0.1088 -0.0504 0.0181 222 ASN A CA 1689 C C . ASN A 222 ? 0.4117 0.7252 0.2475 0.1184 -0.0445 0.0317 222 ASN A C 1690 O O . ASN A 222 ? 0.4129 0.7325 0.2406 0.1186 -0.0458 0.0283 222 ASN A O 1691 C CB . ASN A 222 ? 0.4048 0.7770 0.2536 0.1185 -0.0576 0.0130 222 ASN A CB 1692 C CG . ASN A 222 ? 0.4107 0.7921 0.2560 0.1361 -0.0560 0.0269 222 ASN A CG 1693 O OD1 . ASN A 222 ? 0.4129 0.7695 0.2599 0.1386 -0.0497 0.0378 222 ASN A OD1 1694 N ND2 . ASN A 222 ? 0.4268 0.8448 0.2671 0.1488 -0.0617 0.0260 222 ASN A ND2 1695 N N . THR A 223 ? 0.4175 0.7092 0.2510 0.1255 -0.0374 0.0464 223 THR A N 1696 C CA . THR A 223 ? 0.4390 0.7163 0.2596 0.1361 -0.0306 0.0611 223 THR A CA 1697 C C . THR A 223 ? 0.4601 0.7579 0.2721 0.1558 -0.0307 0.0723 223 THR A C 1698 O O . THR A 223 ? 0.4578 0.7537 0.2738 0.1626 -0.0288 0.0788 223 THR A O 1699 C CB . THR A 223 ? 0.4355 0.6750 0.2592 0.1313 -0.0216 0.0700 223 THR A CB 1700 O OG1 . THR A 223 ? 0.4396 0.6635 0.2706 0.1146 -0.0221 0.0598 223 THR A OG1 1701 C CG2 . THR A 223 ? 0.4585 0.6823 0.2701 0.1413 -0.0132 0.0853 223 THR A CG2 1702 N N . ILE A 224 ? 0.4756 0.7942 0.2753 0.1655 -0.0331 0.0742 224 ILE A N 1703 C CA . ILE A 224 ? 0.4992 0.8414 0.2885 0.1859 -0.0339 0.0849 224 ILE A CA 1704 C C . ILE A 224 ? 0.5165 0.8384 0.2915 0.1980 -0.0239 0.1040 224 ILE A C 1705 O O . ILE A 224 ? 0.5226 0.8473 0.2870 0.1994 -0.0228 0.1053 224 ILE A O 1706 C CB . ILE A 224 ? 0.5042 0.8898 0.2891 0.1900 -0.0440 0.0734 224 ILE A CB 1707 C CG1 . ILE A 224 ? 0.4852 0.8891 0.2858 0.1753 -0.0527 0.0531 224 ILE A CG1 1708 C CG2 . ILE A 224 ? 0.5185 0.9316 0.2917 0.2132 -0.0451 0.0855 224 ILE A CG2 1709 C CD1 . ILE A 224 ? 0.4953 0.9404 0.2937 0.1753 -0.0624 0.0379 224 ILE A CD1 1710 N N . ILE A 225 ? 0.5249 0.8255 0.3001 0.2061 -0.0160 0.1183 225 ILE A N 1711 C CA . ILE A 225 ? 0.5369 0.8116 0.3009 0.2159 -0.0043 0.1371 225 ILE A CA 1712 C C . ILE A 225 ? 0.5524 0.8171 0.3169 0.2295 0.0016 0.1506 225 ILE A C 1713 O O . ILE A 225 ? 0.5326 0.7941 0.3097 0.2241 -0.0007 0.1443 225 ILE A O 1714 C CB . ILE A 225 ? 0.5304 0.7686 0.2992 0.1994 0.0030 0.1358 225 ILE A CB 1715 C CG1 . ILE A 225 ? 0.5413 0.7579 0.2977 0.2077 0.0150 0.1532 225 ILE A CG1 1716 C CG2 . ILE A 225 ? 0.5205 0.7349 0.3047 0.1871 0.0050 0.1308 225 ILE A CG2 1717 C CD1 . ILE A 225 ? 0.5300 0.7199 0.2902 0.1919 0.0208 0.1500 225 ILE A CD1 1718 N N . ASN A 226 ? 0.5732 0.8327 0.3238 0.2477 0.0095 0.1692 226 ASN A N 1719 C CA . ASN A 226 ? 0.5905 0.8361 0.3407 0.2619 0.0169 0.1835 226 ASN A CA 1720 C C . ASN A 226 ? 0.5895 0.7917 0.3496 0.2501 0.0268 0.1854 226 ASN A C 1721 O O . ASN A 226 ? 0.5710 0.7542 0.3363 0.2328 0.0289 0.1784 226 ASN A O 1722 C CB . ASN A 226 ? 0.6154 0.8652 0.3471 0.2856 0.0240 0.2042 226 ASN A CB 1723 C CG . ASN A 226 ? 0.6330 0.8560 0.3542 0.2838 0.0354 0.2156 226 ASN A CG 1724 O OD1 . ASN A 226 ? 0.6193 0.8182 0.3478 0.2654 0.0389 0.2089 226 ASN A OD1 1725 N ND2 . ASN A 226 ? 0.6452 0.8736 0.3491 0.3037 0.0415 0.2335 226 ASN A ND2 1726 N N . ARG A 227 ? 0.6097 0.7980 0.3728 0.2597 0.0327 0.1941 227 ARG A N 1727 C CA . ARG A 227 ? 0.6200 0.7692 0.3931 0.2492 0.0420 0.1946 227 ARG A CA 1728 C C . ARG A 227 ? 0.6273 0.7438 0.3946 0.2440 0.0542 0.2039 227 ARG A C 1729 O O . ARG A 227 ? 0.6151 0.7079 0.3918 0.2266 0.0577 0.1966 227 ARG A O 1730 C CB . ARG A 227 ? 0.6347 0.7742 0.4097 0.2635 0.0477 0.2040 227 ARG A CB 1731 C CG . ARG A 227 ? 0.6473 0.7498 0.4340 0.2515 0.0561 0.2012 227 ARG A CG 1732 C CD . ARG A 227 ? 0.6791 0.7673 0.4660 0.2673 0.0641 0.2120 227 ARG A CD 1733 N NE . ARG A 227 ? 0.7314 0.7865 0.5300 0.2549 0.0715 0.2068 227 ARG A NE 1734 C CZ . ARG A 227 ? 0.7524 0.8126 0.5644 0.2442 0.0653 0.1925 227 ARG A CZ 1735 N NH1 . ARG A 227 ? 0.7737 0.8037 0.5947 0.2339 0.0727 0.1884 227 ARG A NH1 1736 N NH2 . ARG A 227 ? 0.7458 0.8417 0.5624 0.2430 0.0521 0.1819 227 ARG A NH2 1737 N N . GLU A 228 ? 0.6456 0.7626 0.3975 0.2595 0.0609 0.2200 228 GLU A N 1738 C CA . GLU A 228 ? 0.6629 0.7514 0.4085 0.2557 0.0734 0.2301 228 GLU A CA 1739 C C . GLU A 228 ? 0.6354 0.7242 0.3860 0.2353 0.0692 0.2167 228 GLU A C 1740 O O . GLU A 228 ? 0.6318 0.6919 0.3887 0.2220 0.0774 0.2157 228 GLU A O 1741 C CB . GLU A 228 ? 0.6888 0.7857 0.4154 0.2765 0.0793 0.2490 228 GLU A CB 1742 C CG . GLU A 228 ? 0.7190 0.7846 0.4388 0.2743 0.0946 0.2620 228 GLU A CG 1743 C CD . GLU A 228 ? 0.7635 0.8384 0.4632 0.2955 0.1009 0.2817 228 GLU A CD 1744 O OE1 . GLU A 228 ? 0.8157 0.8945 0.5069 0.2922 0.1032 0.2842 228 GLU A OE1 1745 O OE2 . GLU A 228 ? 0.7963 0.8757 0.4880 0.3162 0.1035 0.2949 228 GLU A OE2 1746 N N . GLY A 229 ? 0.6183 0.7405 0.3667 0.2332 0.0566 0.2059 229 GLY A N 1747 C CA . GLY A 229 ? 0.5994 0.7250 0.3515 0.2161 0.0518 0.1929 229 GLY A CA 1748 C C . GLY A 229 ? 0.5743 0.6888 0.3435 0.1964 0.0474 0.1768 229 GLY A C 1749 O O . GLY A 229 ? 0.5654 0.6653 0.3396 0.1817 0.0497 0.1706 229 GLY A O 1750 N N . LEU A 230 ? 0.5640 0.6872 0.3418 0.1969 0.0411 0.1701 230 LEU A N 1751 C CA . LEU A 230 ? 0.5463 0.6575 0.3395 0.1805 0.0383 0.1571 230 LEU A CA 1752 C C . LEU A 230 ? 0.5521 0.6259 0.3500 0.1739 0.0506 0.1630 230 LEU A C 1753 O O . LEU A 230 ? 0.5368 0.5971 0.3425 0.1580 0.0513 0.1544 230 LEU A O 1754 C CB . LEU A 230 ? 0.5384 0.6648 0.3385 0.1855 0.0318 0.1524 230 LEU A CB 1755 C CG . LEU A 230 ? 0.5172 0.6464 0.3319 0.1708 0.0246 0.1367 230 LEU A CG 1756 C CD1 . LEU A 230 ? 0.5265 0.6321 0.3501 0.1688 0.0310 0.1383 230 LEU A CD1 1757 C CD2 . LEU A 230 ? 0.4792 0.6081 0.2991 0.1529 0.0196 0.1235 230 LEU A CD2 1758 N N . MET A 231 ? 0.5757 0.6336 0.3684 0.1868 0.0607 0.1776 231 MET A N 1759 C CA . MET A 231 ? 0.5882 0.6102 0.3862 0.1813 0.0734 0.1827 231 MET A CA 1760 C C . MET A 231 ? 0.5992 0.6030 0.3942 0.1735 0.0824 0.1870 231 MET A C 1761 O O . MET A 231 ? 0.6020 0.5806 0.4057 0.1617 0.0900 0.1842 231 MET A O 1762 C CB . MET A 231 ? 0.6107 0.6191 0.4044 0.1980 0.0825 0.1969 231 MET A CB 1763 C CG . MET A 231 ? 0.5949 0.6154 0.3951 0.2037 0.0758 0.1916 231 MET A CG 1764 S SD . MET A 231 ? 0.5873 0.5973 0.4056 0.1834 0.0719 0.1735 231 MET A SD 1765 C CE . MET A 231 ? 0.5695 0.6089 0.3921 0.1922 0.0607 0.1674 231 MET A CE 1766 N N . ASN A 232 ? 0.6072 0.6248 0.3904 0.1798 0.0820 0.1933 232 ASN A N 1767 C CA . ASN A 232 ? 0.6219 0.6235 0.4023 0.1728 0.0914 0.1980 232 ASN A CA 1768 C C . ASN A 232 ? 0.5861 0.6005 0.3702 0.1584 0.0837 0.1847 232 ASN A C 1769 O O . ASN A 232 ? 0.5829 0.5838 0.3686 0.1493 0.0909 0.1853 232 ASN A O 1770 C CB . ASN A 232 ? 0.6661 0.6648 0.4308 0.1891 0.1015 0.2173 232 ASN A CB 1771 C CG . ASN A 232 ? 0.7119 0.7415 0.4639 0.1969 0.0936 0.2180 232 ASN A CG 1772 O OD1 . ASN A 232 ? 0.7619 0.8194 0.5148 0.1973 0.0798 0.2070 232 ASN A OD1 1773 N ND2 . ASN A 232 ? 0.7577 0.7832 0.4980 0.2026 0.1028 0.2305 232 ASN A ND2 1774 N N . ILE A 233 ? 0.5524 0.5924 0.3386 0.1562 0.0698 0.1724 233 ILE A N 1775 C CA . ILE A 233 ? 0.5168 0.5670 0.3076 0.1426 0.0622 0.1584 233 ILE A CA 1776 C C . ILE A 233 ? 0.4915 0.5366 0.2970 0.1284 0.0562 0.1441 233 ILE A C 1777 O O . ILE A 233 ? 0.4832 0.5149 0.2964 0.1153 0.0588 0.1381 233 ILE A O 1778 C CB . ILE A 233 ? 0.5135 0.5956 0.2954 0.1485 0.0517 0.1536 233 ILE A CB 1779 C CG1 . ILE A 233 ? 0.5309 0.6198 0.2969 0.1620 0.0579 0.1675 233 ILE A CG1 1780 C CG2 . ILE A 233 ? 0.4804 0.5701 0.2685 0.1340 0.0443 0.1380 233 ILE A CG2 1781 C CD1 . ILE A 233 ? 0.5277 0.6508 0.2835 0.1717 0.0477 0.1640 233 ILE A CD1 1782 N N . HIS A 234 ? 0.4777 0.5342 0.2871 0.1314 0.0487 0.1391 234 HIS A N 1783 C CA . HIS A 234 ? 0.4449 0.5039 0.2661 0.1188 0.0409 0.1246 234 HIS A CA 1784 C C . HIS A 234 ? 0.4452 0.4831 0.2768 0.1128 0.0457 0.1233 234 HIS A C 1785 O O . HIS A 234 ? 0.4204 0.4543 0.2615 0.1003 0.0421 0.1125 234 HIS A O 1786 C CB . HIS A 234 ? 0.4391 0.5253 0.2597 0.1233 0.0297 0.1178 234 HIS A CB 1787 C CG . HIS A 234 ? 0.4342 0.5424 0.2474 0.1248 0.0233 0.1135 234 HIS A CG 1788 N ND1 . HIS A 234 ? 0.4522 0.5809 0.2544 0.1388 0.0213 0.1198 234 HIS A ND1 1789 C CD2 . HIS A 234 ? 0.4025 0.5151 0.2173 0.1145 0.0190 0.1035 234 HIS A CD2 1790 C CE1 . HIS A 234 ? 0.4361 0.5816 0.2335 0.1364 0.0158 0.1128 234 HIS A CE1 1791 N NE2 . HIS A 234 ? 0.4468 0.5820 0.2520 0.1217 0.0145 0.1028 234 HIS A NE2 1792 N N . MET A 235 ? 0.4564 0.4805 0.2853 0.1224 0.0544 0.1345 235 MET A N 1793 C CA . MET A 235 ? 0.4547 0.4586 0.2923 0.1188 0.0600 0.1338 235 MET A CA 1794 C C . MET A 235 ? 0.4549 0.4324 0.2974 0.1090 0.0705 0.1348 235 MET A C 1795 O O . MET A 235 ? 0.4523 0.4188 0.3049 0.0988 0.0712 0.1266 235 MET A O 1796 C CB . MET A 235 ? 0.4653 0.4671 0.2985 0.1347 0.0643 0.1445 235 MET A CB 1797 C CG . MET A 235 ? 0.4664 0.4515 0.3086 0.1326 0.0684 0.1419 235 MET A CG 1798 S SD . MET A 235 ? 0.4438 0.4450 0.2972 0.1225 0.0563 0.1255 235 MET A SD 1799 C CE . MET A 235 ? 0.4278 0.4581 0.2759 0.1386 0.0484 0.1290 235 MET A CE 1800 N N . PRO A 236 ? 0.4653 0.4335 0.3009 0.1120 0.0793 0.1446 236 PRO A N 1801 C CA . PRO A 236 ? 0.4666 0.4088 0.3079 0.1033 0.0911 0.1462 236 PRO A CA 1802 C C . PRO A 236 ? 0.4458 0.3823 0.2999 0.0861 0.0889 0.1322 236 PRO A C 1803 O O . PRO A 236 ? 0.4481 0.3653 0.3099 0.0805 0.0965 0.1304 236 PRO A O 1804 C CB . PRO A 236 ? 0.4798 0.4219 0.3123 0.1060 0.0973 0.1554 236 PRO A CB 1805 C CG . PRO A 236 ? 0.4894 0.4472 0.3088 0.1234 0.0943 0.1657 236 PRO A CG 1806 C CD . PRO A 236 ? 0.4741 0.4547 0.2964 0.1235 0.0798 0.1549 236 PRO A CD 1807 N N . ALA A 237 ? 0.4244 0.3776 0.2806 0.0784 0.0790 0.1223 237 ALA A N 1808 C CA . ALA A 237 ? 0.4112 0.3610 0.2782 0.0637 0.0768 0.1101 237 ALA A CA 1809 C C . ALA A 237 ? 0.4064 0.3533 0.2815 0.0600 0.0732 0.1021 237 ALA A C 1810 O O . ALA A 237 ? 0.3911 0.3311 0.2752 0.0490 0.0741 0.0935 237 ALA A O 1811 C CB . ALA A 237 ? 0.3951 0.3624 0.2612 0.0582 0.0677 0.1027 237 ALA A CB 1812 N N . TYR A 238 ? 0.4039 0.3581 0.2759 0.0694 0.0690 0.1046 238 TYR A N 1813 C CA . TYR A 238 ? 0.4107 0.3621 0.2898 0.0674 0.0668 0.0981 238 TYR A CA 1814 C C . TYR A 238 ? 0.4268 0.3545 0.3108 0.0662 0.0782 0.1003 238 TYR A C 1815 O O . TYR A 238 ? 0.4194 0.3411 0.3116 0.0581 0.0783 0.0914 238 TYR A O 1816 C CB . TYR A 238 ? 0.4065 0.3739 0.2820 0.0777 0.0597 0.0998 238 TYR A CB 1817 C CG . TYR A 238 ? 0.4020 0.3910 0.2776 0.0732 0.0480 0.0918 238 TYR A CG 1818 C CD1 . TYR A 238 ? 0.4158 0.4202 0.2837 0.0779 0.0433 0.0946 238 TYR A CD1 1819 C CD2 . TYR A 238 ? 0.3898 0.3828 0.2730 0.0636 0.0422 0.0810 238 TYR A CD2 1820 C CE1 . TYR A 238 ? 0.3923 0.4145 0.2610 0.0728 0.0335 0.0862 238 TYR A CE1 1821 C CE2 . TYR A 238 ? 0.3765 0.3864 0.2600 0.0590 0.0329 0.0741 238 TYR A CE2 1822 C CZ . TYR A 238 ? 0.3747 0.3981 0.2514 0.0633 0.0288 0.0764 238 TYR A CZ 1823 O OH . TYR A 238 ? 0.3604 0.3984 0.2377 0.0583 0.0205 0.0688 238 TYR A OH 1824 N N . LYS A 239 ? 0.4509 0.3648 0.3295 0.0740 0.0883 0.1119 239 LYS A N 1825 C CA . LYS A 239 ? 0.4762 0.3644 0.3594 0.0723 0.1011 0.1143 239 LYS A CA 1826 C C . LYS A 239 ? 0.4679 0.3464 0.3599 0.0564 0.1056 0.1058 239 LYS A C 1827 O O . LYS A 239 ? 0.4742 0.3393 0.3748 0.0491 0.1106 0.0986 239 LYS A O 1828 C CB . LYS A 239 ? 0.5054 0.3803 0.3798 0.0852 0.1117 0.1303 239 LYS A CB 1829 C CG . LYS A 239 ? 0.5649 0.4093 0.4438 0.0842 0.1268 0.1339 239 LYS A CG 1830 C CD . LYS A 239 ? 0.6103 0.4470 0.4958 0.0854 0.1270 0.1273 239 LYS A CD 1831 C CE . LYS A 239 ? 0.6849 0.4902 0.5720 0.0893 0.1431 0.1338 239 LYS A CE 1832 N NZ . LYS A 239 ? 0.7060 0.4919 0.6005 0.0749 0.1540 0.1299 239 LYS A NZ 1833 N N . ASN A 240 ? 0.4563 0.3437 0.3465 0.0511 0.1036 0.1057 240 ASN A N 1834 C CA . ASN A 240 ? 0.4476 0.3324 0.3469 0.0361 0.1055 0.0959 240 ASN A CA 1835 C C . ASN A 240 ? 0.4233 0.3179 0.3307 0.0273 0.0966 0.0818 240 ASN A C 1836 O O . ASN A 240 ? 0.4308 0.3176 0.3475 0.0170 0.1006 0.0731 240 ASN A O 1837 C CB . ASN A 240 ? 0.4434 0.3394 0.3390 0.0334 0.1037 0.0980 240 ASN A CB 1838 C CG . ASN A 240 ? 0.4709 0.3580 0.3582 0.0415 0.1134 0.1122 240 ASN A CG 1839 O OD1 . ASN A 240 ? 0.4867 0.3822 0.3632 0.0538 0.1101 0.1212 240 ASN A OD1 1840 N ND2 . ASN A 240 ? 0.5000 0.3711 0.3921 0.0347 0.1257 0.1143 240 ASN A ND2 1841 N N . ALA A 241 ? 0.4024 0.3144 0.3062 0.0314 0.0849 0.0794 241 ALA A N 1842 C CA . ALA A 241 ? 0.3845 0.3057 0.2941 0.0250 0.0767 0.0679 241 ALA A CA 1843 C C . ALA A 241 ? 0.3885 0.2973 0.3038 0.0244 0.0815 0.0639 241 ALA A C 1844 O O . ALA A 241 ? 0.3913 0.3003 0.3140 0.0154 0.0805 0.0534 241 ALA A O 1845 C CB . ALA A 241 ? 0.3588 0.2990 0.2631 0.0304 0.0651 0.0676 241 ALA A CB 1846 N N . MET A 242 ? 0.4070 0.3057 0.3185 0.0348 0.0868 0.0721 242 MET A N 1847 C CA . MET A 242 ? 0.4188 0.3035 0.3353 0.0356 0.0927 0.0687 242 MET A CA 1848 C C . MET A 242 ? 0.4344 0.3012 0.3590 0.0252 0.1030 0.0629 242 MET A C 1849 O O . MET A 242 ? 0.4285 0.2922 0.3605 0.0181 0.1036 0.0520 242 MET A O 1850 C CB . MET A 242 ? 0.4354 0.3105 0.3457 0.0503 0.0983 0.0803 242 MET A CB 1851 C CG . MET A 242 ? 0.4236 0.3179 0.3269 0.0615 0.0890 0.0856 242 MET A CG 1852 S SD . MET A 242 ? 0.4290 0.3401 0.3372 0.0591 0.0784 0.0745 242 MET A SD 1853 C CE . MET A 242 ? 0.3894 0.3228 0.2961 0.0512 0.0665 0.0695 242 MET A CE 1854 N N . ASP A 243 ? 0.4504 0.3064 0.3736 0.0241 0.1114 0.0699 243 ASP A N 1855 C CA . ASP A 243 ? 0.4675 0.3067 0.3993 0.0131 0.1224 0.0647 243 ASP A CA 1856 C C . ASP A 243 ? 0.4468 0.2988 0.3875 -0.0013 0.1170 0.0501 243 ASP A C 1857 O O . ASP A 243 ? 0.4588 0.3010 0.4088 -0.0113 0.1237 0.0407 243 ASP A O 1858 C CB . ASP A 243 ? 0.4855 0.3142 0.4136 0.0145 0.1320 0.0758 243 ASP A CB 1859 C CG . ASP A 243 ? 0.5209 0.3337 0.4405 0.0290 0.1401 0.0910 243 ASP A CG 1860 O OD1 . ASP A 243 ? 0.5331 0.3394 0.4516 0.0370 0.1404 0.0917 243 ASP A OD1 1861 O OD2 . ASP A 243 ? 0.5575 0.3648 0.4710 0.0330 0.1466 0.1025 243 ASP A OD2 1862 N N . LYS A 244 ? 0.4223 0.2961 0.3599 -0.0019 0.1051 0.0481 244 LYS A N 1863 C CA . LYS A 244 ? 0.4049 0.2933 0.3493 -0.0132 0.0989 0.0358 244 LYS A CA 1864 C C . LYS A 244 ? 0.3930 0.2932 0.3389 -0.0142 0.0897 0.0265 244 LYS A C 1865 O O . LYS A 244 ? 0.3864 0.3009 0.3363 -0.0214 0.0834 0.0174 244 LYS A O 1866 C CB . LYS A 244 ? 0.3942 0.2972 0.3345 -0.0134 0.0933 0.0395 244 LYS A CB 1867 C CG . LYS A 244 ? 0.3957 0.2885 0.3366 -0.0156 0.1037 0.0461 244 LYS A CG 1868 C CD . LYS A 244 ? 0.3864 0.2922 0.3207 -0.0124 0.0990 0.0523 244 LYS A CD 1869 C CE . LYS A 244 ? 0.4086 0.3021 0.3416 -0.0121 0.1110 0.0616 244 LYS A CE 1870 N NZ . LYS A 244 ? 0.4146 0.3221 0.3431 -0.0112 0.1076 0.0651 244 LYS A NZ 1871 N N . GLY A 245 ? 0.3927 0.2875 0.3354 -0.0063 0.0895 0.0292 245 GLY A N 1872 C CA . GLY A 245 ? 0.3801 0.2842 0.3244 -0.0069 0.0827 0.0210 245 GLY A CA 1873 C C . GLY A 245 ? 0.3590 0.2836 0.2986 -0.0048 0.0704 0.0210 245 GLY A C 1874 O O . GLY A 245 ? 0.3525 0.2876 0.2944 -0.0092 0.0648 0.0125 245 GLY A O 1875 N N . VAL A 246 ? 0.3598 0.2899 0.2925 0.0018 0.0666 0.0302 246 VAL A N 1876 C CA . VAL A 246 ? 0.3424 0.2897 0.2708 0.0036 0.0559 0.0300 246 VAL A CA 1877 C C . VAL A 246 ? 0.3412 0.2933 0.2702 0.0062 0.0523 0.0263 246 VAL A C 1878 O O . VAL A 246 ? 0.3515 0.2958 0.2802 0.0125 0.0565 0.0293 246 VAL A O 1879 C CB . VAL A 246 ? 0.3439 0.2964 0.2649 0.0110 0.0529 0.0393 246 VAL A CB 1880 C CG1 . VAL A 246 ? 0.3566 0.3065 0.2736 0.0218 0.0543 0.0466 246 VAL A CG1 1881 C CG2 . VAL A 246 ? 0.3090 0.2777 0.2277 0.0090 0.0431 0.0366 246 VAL A CG2 1882 N N . SER A 247 ? 0.3292 0.2939 0.2589 0.0018 0.0452 0.0202 247 SER A N 1883 C CA . SER A 247 ? 0.3327 0.3028 0.2635 0.0024 0.0426 0.0155 247 SER A CA 1884 C C . SER A 247 ? 0.3269 0.3049 0.2538 0.0096 0.0382 0.0207 247 SER A C 1885 O O . SER A 247 ? 0.3300 0.3089 0.2581 0.0131 0.0390 0.0194 247 SER A O 1886 C CB . SER A 247 ? 0.3139 0.2945 0.2463 -0.0046 0.0377 0.0077 247 SER A CB 1887 O OG . SER A 247 ? 0.3367 0.3125 0.2744 -0.0109 0.0422 0.0001 247 SER A OG 1888 N N . THR A 248 ? 0.3242 0.3092 0.2471 0.0114 0.0336 0.0256 248 THR A N 1889 C CA . THR A 248 ? 0.3215 0.3170 0.2415 0.0167 0.0288 0.0291 248 THR A CA 1890 C C . THR A 248 ? 0.3244 0.3214 0.2399 0.0222 0.0282 0.0363 248 THR A C 1891 O O . THR A 248 ? 0.3246 0.3161 0.2384 0.0206 0.0303 0.0383 248 THR A O 1892 C CB . THR A 248 ? 0.3076 0.3152 0.2275 0.0118 0.0220 0.0251 248 THR A CB 1893 O OG1 . THR A 248 ? 0.3161 0.3260 0.2335 0.0085 0.0188 0.0257 248 THR A OG1 1894 C CG2 . THR A 248 ? 0.3106 0.3181 0.2334 0.0063 0.0224 0.0184 248 THR A CG2 1895 N N . VAL A 249 ? 0.3180 0.3243 0.2316 0.0288 0.0254 0.0396 249 VAL A N 1896 C CA . VAL A 249 ? 0.3154 0.3286 0.2241 0.0344 0.0232 0.0451 249 VAL A CA 1897 C C . VAL A 249 ? 0.3094 0.3397 0.2183 0.0337 0.0159 0.0422 249 VAL A C 1898 O O . VAL A 249 ? 0.3099 0.3474 0.2220 0.0351 0.0146 0.0402 249 VAL A O 1899 C CB . VAL A 249 ? 0.3254 0.3339 0.2313 0.0454 0.0284 0.0530 249 VAL A CB 1900 C CG1 . VAL A 249 ? 0.3196 0.3401 0.2196 0.0524 0.0250 0.0583 249 VAL A CG1 1901 C CG2 . VAL A 249 ? 0.3278 0.3173 0.2336 0.0451 0.0369 0.0563 249 VAL A CG2 1902 N N . MET A 250 ? 0.3076 0.3444 0.2137 0.0310 0.0117 0.0413 250 MET A N 1903 C CA . MET A 250 ? 0.3027 0.3552 0.2095 0.0299 0.0056 0.0379 250 MET A CA 1904 C C . MET A 250 ? 0.3074 0.3717 0.2104 0.0385 0.0039 0.0418 250 MET A C 1905 O O . MET A 250 ? 0.3145 0.3760 0.2123 0.0428 0.0055 0.0464 250 MET A O 1906 C CB . MET A 250 ? 0.2933 0.3461 0.1996 0.0220 0.0021 0.0334 250 MET A CB 1907 C CG . MET A 250 ? 0.2838 0.3500 0.1916 0.0189 -0.0030 0.0288 250 MET A CG 1908 S SD . MET A 250 ? 0.2970 0.3591 0.2033 0.0110 -0.0055 0.0242 250 MET A SD 1909 C CE . MET A 250 ? 0.2921 0.3417 0.2006 0.0056 -0.0029 0.0235 250 MET A CE 1910 N N . ILE A 251 ? 0.3093 0.3890 0.2154 0.0409 0.0006 0.0397 251 ILE A N 1911 C CA . ILE A 251 ? 0.3108 0.4072 0.2140 0.0493 -0.0023 0.0421 251 ILE A CA 1912 C C . ILE A 251 ? 0.3121 0.4196 0.2131 0.0450 -0.0075 0.0372 251 ILE A C 1913 O O . ILE A 251 ? 0.3079 0.4145 0.2122 0.0353 -0.0098 0.0306 251 ILE A O 1914 C CB . ILE A 251 ? 0.3182 0.4297 0.2266 0.0538 -0.0038 0.0409 251 ILE A CB 1915 C CG1 . ILE A 251 ? 0.3128 0.4111 0.2232 0.0579 0.0020 0.0448 251 ILE A CG1 1916 C CG2 . ILE A 251 ? 0.3024 0.4345 0.2080 0.0638 -0.0071 0.0433 251 ILE A CG2 1917 C CD1 . ILE A 251 ? 0.3200 0.4030 0.2246 0.0668 0.0083 0.0536 251 ILE A CD1 1918 N N . SER A 252 ? 0.3178 0.4353 0.2128 0.0529 -0.0089 0.0406 252 SER A N 1919 C CA . SER A 252 ? 0.3198 0.4498 0.2120 0.0504 -0.0137 0.0353 252 SER A CA 1920 C C . SER A 252 ? 0.3178 0.4714 0.2153 0.0483 -0.0196 0.0273 252 SER A C 1921 O O . SER A 252 ? 0.3282 0.4958 0.2284 0.0548 -0.0205 0.0288 252 SER A O 1922 C CB . SER A 252 ? 0.3137 0.4471 0.1965 0.0604 -0.0125 0.0421 252 SER A CB 1923 O OG . SER A 252 ? 0.3348 0.4794 0.2143 0.0577 -0.0169 0.0361 252 SER A OG 1924 N N . TYR A 253 ? 0.3176 0.4756 0.2168 0.0393 -0.0230 0.0185 253 TYR A N 1925 C CA . TYR A 253 ? 0.3220 0.5036 0.2258 0.0363 -0.0284 0.0094 253 TYR A CA 1926 C C . TYR A 253 ? 0.3340 0.5383 0.2323 0.0475 -0.0317 0.0109 253 TYR A C 1927 O O . TYR A 253 ? 0.3376 0.5667 0.2408 0.0485 -0.0360 0.0051 253 TYR A O 1928 C CB . TYR A 253 ? 0.3213 0.5000 0.2259 0.0257 -0.0303 0.0001 253 TYR A CB 1929 C CG . TYR A 253 ? 0.3209 0.4824 0.2312 0.0141 -0.0280 -0.0034 253 TYR A CG 1930 C CD1 . TYR A 253 ? 0.3233 0.4656 0.2299 0.0098 -0.0259 -0.0033 253 TYR A CD1 1931 C CD2 . TYR A 253 ? 0.3219 0.4875 0.2409 0.0080 -0.0276 -0.0068 253 TYR A CD2 1932 C CE1 . TYR A 253 ? 0.3332 0.4604 0.2438 0.0006 -0.0237 -0.0057 253 TYR A CE1 1933 C CE2 . TYR A 253 ? 0.3076 0.4573 0.2305 -0.0019 -0.0249 -0.0090 253 TYR A CE2 1934 C CZ . TYR A 253 ? 0.3097 0.4403 0.2280 -0.0050 -0.0231 -0.0082 253 TYR A CZ 1935 O OH . TYR A 253 ? 0.3148 0.4302 0.2357 -0.0131 -0.0204 -0.0092 253 TYR A OH 1936 N N . SER A 254 ? 0.3393 0.5369 0.2278 0.0557 -0.0297 0.0186 254 SER A N 1937 C CA . SER A 254 ? 0.3536 0.5721 0.2345 0.0672 -0.0325 0.0211 254 SER A CA 1938 C C . SER A 254 ? 0.3612 0.5950 0.2426 0.0794 -0.0328 0.0275 254 SER A C 1939 O O . SER A 254 ? 0.3591 0.5828 0.2457 0.0799 -0.0295 0.0317 254 SER A O 1940 C CB . SER A 254 ? 0.3616 0.5671 0.2313 0.0731 -0.0288 0.0293 254 SER A CB 1941 O OG . SER A 254 ? 0.3743 0.5562 0.2422 0.0766 -0.0218 0.0403 254 SER A OG 1942 N N . SER A 255 ? 0.3709 0.6306 0.2468 0.0897 -0.0368 0.0278 255 SER A N 1943 C CA . SER A 255 ? 0.3803 0.6567 0.2548 0.1045 -0.0371 0.0354 255 SER A CA 1944 C C . SER A 255 ? 0.3955 0.6656 0.2564 0.1196 -0.0329 0.0495 255 SER A C 1945 O O . SER A 255 ? 0.3985 0.6618 0.2512 0.1187 -0.0318 0.0507 255 SER A O 1946 C CB . SER A 255 ? 0.3816 0.6969 0.2604 0.1063 -0.0451 0.0253 255 SER A CB 1947 O OG . SER A 255 ? 0.3738 0.6943 0.2658 0.0916 -0.0479 0.0124 255 SER A OG 1948 N N . TRP A 256 ? 0.4065 0.6779 0.2650 0.1338 -0.0296 0.0606 256 TRP A N 1949 C CA . TRP A 256 ? 0.4202 0.6892 0.2654 0.1505 -0.0252 0.0751 256 TRP A CA 1950 C C . TRP A 256 ? 0.4299 0.7330 0.2714 0.1671 -0.0299 0.0782 256 TRP A C 1951 O O . TRP A 256 ? 0.4278 0.7379 0.2750 0.1740 -0.0297 0.0807 256 TRP A O 1952 C CB . TRP A 256 ? 0.4265 0.6616 0.2700 0.1546 -0.0150 0.0881 256 TRP A CB 1953 C CG . TRP A 256 ? 0.4540 0.6846 0.2841 0.1720 -0.0090 0.1041 256 TRP A CG 1954 C CD1 . TRP A 256 ? 0.4701 0.7039 0.2882 0.1769 -0.0080 0.1092 256 TRP A CD1 1955 C CD2 . TRP A 256 ? 0.4723 0.6937 0.2992 0.1875 -0.0022 0.1178 256 TRP A CD2 1956 N NE1 . TRP A 256 ? 0.4858 0.7127 0.2930 0.1944 -0.0007 0.1261 256 TRP A NE1 1957 C CE2 . TRP A 256 ? 0.4969 0.7151 0.3093 0.2013 0.0031 0.1317 256 TRP A CE2 1958 C CE3 . TRP A 256 ? 0.4680 0.6827 0.3024 0.1915 0.0006 0.1198 256 TRP A CE3 1959 C CZ2 . TRP A 256 ? 0.5080 0.7150 0.3133 0.2190 0.0115 0.1482 256 TRP A CZ2 1960 C CZ3 . TRP A 256 ? 0.4946 0.6984 0.3225 0.2091 0.0085 0.1351 256 TRP A CZ3 1961 C CH2 . TRP A 256 ? 0.5173 0.7165 0.3307 0.2228 0.0141 0.1495 256 TRP A CH2 1962 N N . ASN A 257 ? 0.4390 0.7647 0.2708 0.1741 -0.0341 0.0777 257 ASN A N 1963 C CA . ASN A 257 ? 0.4492 0.8129 0.2766 0.1900 -0.0399 0.0792 257 ASN A CA 1964 C C . ASN A 257 ? 0.4433 0.8342 0.2854 0.1835 -0.0475 0.0651 257 ASN A C 1965 O O . ASN A 257 ? 0.4461 0.8585 0.2904 0.1964 -0.0495 0.0687 257 ASN A O 1966 C CB . ASN A 257 ? 0.4672 0.8231 0.2849 0.2114 -0.0329 0.0989 257 ASN A CB 1967 C CG . ASN A 257 ? 0.4873 0.8246 0.2892 0.2195 -0.0257 0.1127 257 ASN A CG 1968 O OD1 . ASN A 257 ? 0.4936 0.8393 0.2888 0.2152 -0.0286 0.1078 257 ASN A OD1 1969 N ND2 . ASN A 257 ? 0.4850 0.7966 0.2809 0.2313 -0.0156 0.1299 257 ASN A ND2 1970 N N . GLY A 258 ? 0.4232 0.8121 0.2755 0.1635 -0.0511 0.0494 258 GLY A N 1971 C CA . GLY A 258 ? 0.4101 0.8237 0.2771 0.1539 -0.0576 0.0344 258 GLY A CA 1972 C C . GLY A 258 ? 0.3976 0.7949 0.2767 0.1474 -0.0539 0.0346 258 GLY A C 1973 O O . GLY A 258 ? 0.3906 0.8072 0.2826 0.1387 -0.0582 0.0227 258 GLY A O 1974 N N . VAL A 259 ? 0.3950 0.7581 0.2705 0.1512 -0.0457 0.0473 259 VAL A N 1975 C CA . VAL A 259 ? 0.3794 0.7265 0.2657 0.1452 -0.0419 0.0470 259 VAL A CA 1976 C C . VAL A 259 ? 0.3701 0.6842 0.2597 0.1273 -0.0381 0.0429 259 VAL A C 1977 O O . VAL A 259 ? 0.3730 0.6605 0.2543 0.1272 -0.0331 0.0501 259 VAL A O 1978 C CB . VAL A 259 ? 0.3917 0.7257 0.2740 0.1619 -0.0352 0.0621 259 VAL A CB 1979 C CG1 . VAL A 259 ? 0.3700 0.6891 0.2636 0.1548 -0.0315 0.0599 259 VAL A CG1 1980 C CG2 . VAL A 259 ? 0.4110 0.7794 0.2894 0.1819 -0.0390 0.0673 259 VAL A CG2 1981 N N . LYS A 260 ? 0.3521 0.6699 0.2539 0.1127 -0.0404 0.0313 260 LYS A N 1982 C CA . LYS A 260 ? 0.3452 0.6358 0.2512 0.0963 -0.0373 0.0268 260 LYS A CA 1983 C C . LYS A 260 ? 0.3470 0.6055 0.2497 0.1001 -0.0295 0.0378 260 LYS A C 1984 O O . LYS A 260 ? 0.3535 0.6122 0.2590 0.1083 -0.0267 0.0431 260 LYS A O 1985 C CB . LYS A 260 ? 0.3343 0.6361 0.2540 0.0833 -0.0397 0.0151 260 LYS A CB 1986 C CG . LYS A 260 ? 0.3366 0.6663 0.2616 0.0751 -0.0465 0.0015 260 LYS A CG 1987 C CD . LYS A 260 ? 0.3104 0.6229 0.2337 0.0610 -0.0464 -0.0053 260 LYS A CD 1988 C CE . LYS A 260 ? 0.3238 0.6632 0.2504 0.0548 -0.0526 -0.0188 260 LYS A CE 1989 N NZ . LYS A 260 ? 0.2952 0.6158 0.2196 0.0424 -0.0517 -0.0252 260 LYS A NZ 1990 N N . MET A 261 ? 0.3443 0.5764 0.2415 0.0944 -0.0258 0.0407 261 MET A N 1991 C CA . MET A 261 ? 0.3414 0.5429 0.2372 0.0947 -0.0182 0.0485 261 MET A CA 1992 C C . MET A 261 ? 0.3302 0.5256 0.2359 0.0877 -0.0166 0.0445 261 MET A C 1993 O O . MET A 261 ? 0.3303 0.5126 0.2364 0.0938 -0.0113 0.0507 261 MET A O 1994 C CB . MET A 261 ? 0.3391 0.5172 0.2298 0.0870 -0.0153 0.0494 261 MET A CB 1995 C CG . MET A 261 ? 0.3513 0.5268 0.2305 0.0967 -0.0132 0.0580 261 MET A CG 1996 S SD . MET A 261 ? 0.3912 0.5596 0.2634 0.1154 -0.0063 0.0735 261 MET A SD 1997 C CE . MET A 261 ? 0.3467 0.4869 0.2263 0.1100 0.0009 0.0748 261 MET A CE 1998 N N . HIS A 262 ? 0.3189 0.5236 0.2323 0.0751 -0.0205 0.0340 262 HIS A N 1999 C CA . HIS A 262 ? 0.3093 0.5098 0.2316 0.0677 -0.0188 0.0299 262 HIS A CA 2000 C C . HIS A 262 ? 0.3141 0.5334 0.2421 0.0767 -0.0191 0.0309 262 HIS A C 2001 O O . HIS A 262 ? 0.3041 0.5199 0.2387 0.0726 -0.0167 0.0288 262 HIS A O 2002 C CB . HIS A 262 ? 0.3042 0.5083 0.2329 0.0521 -0.0217 0.0196 262 HIS A CB 2003 C CG . HIS A 262 ? 0.3036 0.4844 0.2283 0.0431 -0.0199 0.0191 262 HIS A CG 2004 N ND1 . HIS A 262 ? 0.3177 0.4812 0.2453 0.0341 -0.0168 0.0178 262 HIS A ND1 2005 C CD2 . HIS A 262 ? 0.2894 0.4629 0.2071 0.0425 -0.0208 0.0199 262 HIS A CD2 2006 C CE1 . HIS A 262 ? 0.2908 0.4378 0.2138 0.0289 -0.0160 0.0180 262 HIS A CE1 2007 N NE2 . HIS A 262 ? 0.3066 0.4591 0.2239 0.0335 -0.0183 0.0190 262 HIS A NE2 2008 N N . ALA A 263 ? 0.3201 0.5606 0.2452 0.0894 -0.0219 0.0341 263 ALA A N 2009 C CA . ALA A 263 ? 0.3283 0.5891 0.2580 0.1009 -0.0223 0.0361 263 ALA A CA 2010 C C . ALA A 263 ? 0.3474 0.6009 0.2685 0.1196 -0.0181 0.0488 263 ALA A C 2011 O O . ALA A 263 ? 0.3587 0.6279 0.2821 0.1321 -0.0180 0.0521 263 ALA A O 2012 C CB . ALA A 263 ? 0.3274 0.6262 0.2629 0.1008 -0.0297 0.0278 263 ALA A CB 2013 N N . ASN A 264 ? 0.3551 0.5852 0.2665 0.1217 -0.0143 0.0561 264 ASN A N 2014 C CA . ASN A 264 ? 0.3684 0.5894 0.2708 0.1389 -0.0093 0.0690 264 ASN A CA 2015 C C . ASN A 264 ? 0.3746 0.5682 0.2778 0.1427 -0.0006 0.0752 264 ASN A C 2016 O O . ASN A 264 ? 0.3754 0.5400 0.2757 0.1366 0.0050 0.0776 264 ASN A O 2017 C CB . ASN A 264 ? 0.3719 0.5826 0.2634 0.1400 -0.0084 0.0745 264 ASN A CB 2018 C CG . ASN A 264 ? 0.3950 0.6065 0.2761 0.1596 -0.0046 0.0880 264 ASN A CG 2019 O OD1 . ASN A 264 ? 0.4125 0.6160 0.2935 0.1714 0.0009 0.0958 264 ASN A OD1 2020 N ND2 . ASN A 264 ? 0.4121 0.6332 0.2841 0.1639 -0.0071 0.0911 264 ASN A ND2 2021 N N . GLN A 265 ? 0.3784 0.5826 0.2862 0.1530 0.0006 0.0768 265 GLN A N 2022 C CA . GLN A 265 ? 0.3930 0.5732 0.3023 0.1576 0.0090 0.0813 265 GLN A CA 2023 C C . GLN A 265 ? 0.4176 0.5735 0.3169 0.1699 0.0171 0.0942 265 GLN A C 2024 O O . GLN A 265 ? 0.4241 0.5495 0.3232 0.1667 0.0251 0.0964 265 GLN A O 2025 C CB . GLN A 265 ? 0.3936 0.5943 0.3100 0.1674 0.0081 0.0799 265 GLN A CB 2026 C CG . GLN A 265 ? 0.4093 0.5883 0.3294 0.1697 0.0160 0.0809 265 GLN A CG 2027 C CD . GLN A 265 ? 0.4422 0.6432 0.3683 0.1825 0.0154 0.0808 265 GLN A CD 2028 O OE1 . GLN A 265 ? 0.4734 0.6832 0.4087 0.1755 0.0144 0.0725 265 GLN A OE1 2029 N NE2 . GLN A 265 ? 0.4795 0.6911 0.4003 0.2018 0.0162 0.0904 265 GLN A NE2 2030 N N . ASP A 266 ? 0.4319 0.6020 0.3231 0.1836 0.0155 0.1026 266 ASP A N 2031 C CA . ASP A 266 ? 0.4656 0.6137 0.3460 0.1961 0.0238 0.1165 266 ASP A CA 2032 C C . ASP A 266 ? 0.4536 0.5715 0.3304 0.1835 0.0289 0.1171 266 ASP A C 2033 O O . ASP A 266 ? 0.4665 0.5544 0.3406 0.1864 0.0390 0.1241 266 ASP A O 2034 C CB . ASP A 266 ? 0.4823 0.6545 0.3532 0.2117 0.0199 0.1248 266 ASP A CB 2035 C CG . ASP A 266 ? 0.5373 0.7361 0.4101 0.2293 0.0173 0.1280 266 ASP A CG 2036 O OD1 . ASP A 266 ? 0.5823 0.7775 0.4631 0.2311 0.0199 0.1253 266 ASP A OD1 2037 O OD2 . ASP A 266 ? 0.6064 0.8320 0.4724 0.2421 0.0124 0.1330 266 ASP A OD2 2038 N N . LEU A 267 ? 0.4317 0.5581 0.3089 0.1698 0.0225 0.1094 267 LEU A N 2039 C CA . LEU A 267 ? 0.4310 0.5328 0.3055 0.1578 0.0266 0.1091 267 LEU A CA 2040 C C . LEU A 267 ? 0.4170 0.4986 0.3001 0.1424 0.0293 0.1005 267 LEU A C 2041 O O . LEU A 267 ? 0.4254 0.4798 0.3075 0.1383 0.0371 0.1033 267 LEU A O 2042 C CB . LEU A 267 ? 0.4213 0.5392 0.2918 0.1509 0.0192 0.1049 267 LEU A CB 2043 C CG . LEU A 267 ? 0.4337 0.5656 0.2928 0.1647 0.0184 0.1143 267 LEU A CG 2044 C CD1 . LEU A 267 ? 0.4240 0.5710 0.2804 0.1556 0.0111 0.1073 267 LEU A CD1 2045 C CD2 . LEU A 267 ? 0.4712 0.5766 0.3214 0.1739 0.0295 0.1286 267 LEU A CD2 2046 N N . VAL A 268 ? 0.3982 0.4942 0.2898 0.1339 0.0231 0.0899 268 VAL A N 2047 C CA . VAL A 268 ? 0.3910 0.4715 0.2896 0.1196 0.0248 0.0816 268 VAL A CA 2048 C C . VAL A 268 ? 0.3957 0.4573 0.2974 0.1247 0.0331 0.0838 268 VAL A C 2049 O O . VAL A 268 ? 0.3975 0.4352 0.3002 0.1177 0.0392 0.0825 268 VAL A O 2050 C CB . VAL A 268 ? 0.3726 0.4732 0.2788 0.1087 0.0167 0.0704 268 VAL A CB 2051 C CG1 . VAL A 268 ? 0.3776 0.4629 0.2895 0.0963 0.0190 0.0633 268 VAL A CG1 2052 C CG2 . VAL A 268 ? 0.3685 0.4834 0.2722 0.1018 0.0096 0.0667 268 VAL A CG2 2053 N N . THR A 269 ? 0.3967 0.4699 0.3000 0.1373 0.0334 0.0867 269 THR A N 2054 C CA . THR A 269 ? 0.4090 0.4653 0.3152 0.1436 0.0414 0.0884 269 THR A CA 2055 C C . THR A 269 ? 0.4361 0.4732 0.3349 0.1579 0.0505 0.1010 269 THR A C 2056 O O . THR A 269 ? 0.4475 0.4556 0.3462 0.1554 0.0597 0.1025 269 THR A O 2057 C CB . THR A 269 ? 0.4046 0.4827 0.3173 0.1499 0.0380 0.0844 269 THR A CB 2058 O OG1 . THR A 269 ? 0.3666 0.4586 0.2861 0.1352 0.0313 0.0731 269 THR A OG1 2059 C CG2 . THR A 269 ? 0.4212 0.4811 0.3365 0.1579 0.0468 0.0858 269 THR A CG2 2060 N N . GLY A 270 ? 0.4449 0.4986 0.3375 0.1725 0.0482 0.1100 270 GLY A N 2061 C CA . GLY A 270 ? 0.4728 0.5105 0.3570 0.1888 0.0570 0.1241 270 GLY A CA 2062 C C . GLY A 270 ? 0.4841 0.4940 0.3629 0.1823 0.0644 0.1290 270 GLY A C 2063 O O . GLY A 270 ? 0.5095 0.4908 0.3863 0.1876 0.0759 0.1359 270 GLY A O 2064 N N . TYR A 271 ? 0.4665 0.4843 0.3434 0.1707 0.0585 0.1251 271 TYR A N 2065 C CA . TYR A 271 ? 0.4744 0.4697 0.3467 0.1642 0.0651 0.1295 271 TYR A CA 2066 C C . TYR A 271 ? 0.4606 0.4382 0.3403 0.1450 0.0669 0.1188 271 TYR A C 2067 O O . TYR A 271 ? 0.4748 0.4247 0.3562 0.1422 0.0772 0.1204 271 TYR A O 2068 C CB . TYR A 271 ? 0.4730 0.4850 0.3368 0.1658 0.0596 0.1339 271 TYR A CB 2069 C CG . TYR A 271 ? 0.4951 0.4839 0.3520 0.1659 0.0692 0.1433 271 TYR A CG 2070 C CD1 . TYR A 271 ? 0.5220 0.4965 0.3708 0.1820 0.0792 0.1583 271 TYR A CD1 2071 C CD2 . TYR A 271 ? 0.4810 0.4613 0.3396 0.1502 0.0691 0.1375 271 TYR A CD2 2072 C CE1 . TYR A 271 ? 0.5456 0.4978 0.3883 0.1815 0.0893 0.1674 271 TYR A CE1 2073 C CE2 . TYR A 271 ? 0.4891 0.4491 0.3424 0.1495 0.0786 0.1458 271 TYR A CE2 2074 C CZ . TYR A 271 ? 0.5346 0.4803 0.3802 0.1646 0.0889 0.1606 271 TYR A CZ 2075 O OH . TYR A 271 ? 0.5701 0.4950 0.4106 0.1634 0.0995 0.1693 271 TYR A OH 2076 N N . LEU A 272 ? 0.4294 0.4233 0.3137 0.1320 0.0575 0.1078 272 LEU A N 2077 C CA . LEU A 272 ? 0.4216 0.4023 0.3116 0.1151 0.0583 0.0985 272 LEU A CA 2078 C C . LEU A 272 ? 0.4315 0.3943 0.3284 0.1120 0.0648 0.0934 272 LEU A C 2079 O O . LEU A 272 ? 0.4411 0.3809 0.3398 0.1056 0.0728 0.0925 272 LEU A O 2080 C CB . LEU A 272 ? 0.3950 0.3961 0.2882 0.1038 0.0474 0.0886 272 LEU A CB 2081 C CG . LEU A 272 ? 0.3781 0.3702 0.2769 0.0875 0.0468 0.0788 272 LEU A CG 2082 C CD1 . LEU A 272 ? 0.3850 0.3611 0.2812 0.0818 0.0520 0.0814 272 LEU A CD1 2083 C CD2 . LEU A 272 ? 0.3604 0.3734 0.2616 0.0796 0.0365 0.0708 272 LEU A CD2 2084 N N . LYS A 273 ? 0.4316 0.4057 0.3326 0.1167 0.0618 0.0897 273 LYS A N 2085 C CA . LYS A 273 ? 0.4391 0.3989 0.3465 0.1144 0.0675 0.0836 273 LYS A CA 2086 C C . LYS A 273 ? 0.4741 0.4105 0.3798 0.1262 0.0793 0.0914 273 LYS A C 2087 O O . LYS A 273 ? 0.4859 0.3982 0.3948 0.1199 0.0878 0.0879 273 LYS A O 2088 C CB . LYS A 273 ? 0.4293 0.4099 0.3420 0.1145 0.0606 0.0762 273 LYS A CB 2089 C CG . LYS A 273 ? 0.3943 0.3919 0.3101 0.1008 0.0512 0.0672 273 LYS A CG 2090 C CD . LYS A 273 ? 0.3790 0.3942 0.3004 0.1002 0.0466 0.0604 273 LYS A CD 2091 C CE . LYS A 273 ? 0.3481 0.3738 0.2725 0.0856 0.0397 0.0517 273 LYS A CE 2092 N NZ . LYS A 273 ? 0.3519 0.3915 0.2820 0.0837 0.0372 0.0449 273 LYS A NZ 2093 N N . ASP A 274 ? 0.4917 0.4353 0.3923 0.1433 0.0802 0.1018 274 ASP A N 2094 C CA . ASP A 274 ? 0.5263 0.4488 0.4253 0.1573 0.0916 0.1099 274 ASP A CA 2095 C C . ASP A 274 ? 0.5487 0.4460 0.4410 0.1617 0.1022 0.1215 274 ASP A C 2096 O O . ASP A 274 ? 0.5803 0.4512 0.4728 0.1683 0.1142 0.1260 274 ASP A O 2097 C CB . ASP A 274 ? 0.5299 0.4721 0.4264 0.1760 0.0885 0.1168 274 ASP A CB 2098 C CG . ASP A 274 ? 0.5289 0.4927 0.4331 0.1737 0.0811 0.1061 274 ASP A CG 2099 O OD1 . ASP A 274 ? 0.5294 0.4910 0.4401 0.1586 0.0791 0.0940 274 ASP A OD1 2100 O OD2 . ASP A 274 ? 0.5521 0.5367 0.4556 0.1877 0.0775 0.1103 274 ASP A OD2 2101 N N . THR A 275 ? 0.5398 0.4452 0.4261 0.1589 0.0985 0.1265 275 THR A N 2102 C CA . THR A 275 ? 0.5618 0.4460 0.4410 0.1631 0.1086 0.1386 275 THR A CA 2103 C C . THR A 275 ? 0.5540 0.4218 0.4373 0.1443 0.1123 0.1317 275 THR A C 2104 O O . THR A 275 ? 0.5693 0.4078 0.4539 0.1417 0.1250 0.1345 275 THR A O 2105 C CB . THR A 275 ? 0.5644 0.4688 0.4325 0.1758 0.1037 0.1509 275 THR A CB 2106 O OG1 . THR A 275 ? 0.5756 0.4960 0.4405 0.1942 0.1010 0.1571 275 THR A OG1 2107 C CG2 . THR A 275 ? 0.5834 0.4655 0.4431 0.1808 0.1152 0.1646 275 THR A CG2 2108 N N . LEU A 276 ? 0.5242 0.4110 0.4100 0.1314 0.1017 0.1225 276 LEU A N 2109 C CA . LEU A 276 ? 0.5147 0.3911 0.4053 0.1139 0.1036 0.1147 276 LEU A CA 2110 C C . LEU A 276 ? 0.5120 0.3777 0.4129 0.1019 0.1056 0.1011 276 LEU A C 2111 O O . LEU A 276 ? 0.5094 0.3650 0.4154 0.0880 0.1086 0.0938 276 LEU A O 2112 C CB . LEU A 276 ? 0.4915 0.3914 0.3804 0.1059 0.0920 0.1104 276 LEU A CB 2113 C CG . LEU A 276 ? 0.4926 0.4036 0.3715 0.1137 0.0898 0.1211 276 LEU A CG 2114 C CD1 . LEU A 276 ? 0.4479 0.3789 0.3273 0.1031 0.0790 0.1134 276 LEU A CD1 2115 C CD2 . LEU A 276 ? 0.4903 0.3780 0.3646 0.1162 0.1026 0.1318 276 LEU A CD2 2116 N N . LYS A 277 ? 0.5084 0.3786 0.4123 0.1078 0.1038 0.0973 277 LYS A N 2117 C CA . LYS A 277 ? 0.5054 0.3668 0.4181 0.0988 0.1060 0.0845 277 LYS A CA 2118 C C . LYS A 277 ? 0.4744 0.3504 0.3920 0.0826 0.0970 0.0717 277 LYS A C 2119 O O . LYS A 277 ? 0.4699 0.3359 0.3940 0.0713 0.1004 0.0613 277 LYS A O 2120 C CB . LYS A 277 ? 0.5263 0.3549 0.4423 0.0965 0.1208 0.0845 277 LYS A CB 2121 C CG . LYS A 277 ? 0.5783 0.3882 0.4891 0.1134 0.1316 0.0982 277 LYS A CG 2122 C CD . LYS A 277 ? 0.6192 0.4358 0.5306 0.1261 0.1299 0.0977 277 LYS A CD 2123 C CE . LYS A 277 ? 0.6808 0.4800 0.5862 0.1452 0.1404 0.1123 277 LYS A CE 2124 N NZ . LYS A 277 ? 0.7130 0.5243 0.6194 0.1582 0.1371 0.1115 277 LYS A NZ 2125 N N . PHE A 278 ? 0.4503 0.3505 0.3648 0.0819 0.0858 0.0723 278 PHE A N 2126 C CA . PHE A 278 ? 0.4259 0.3408 0.3440 0.0688 0.0770 0.0618 278 PHE A CA 2127 C C . PHE A 278 ? 0.4191 0.3400 0.3427 0.0661 0.0745 0.0520 278 PHE A C 2128 O O . PHE A 278 ? 0.4174 0.3486 0.3405 0.0751 0.0720 0.0538 278 PHE A O 2129 C CB . PHE A 278 ? 0.4038 0.3412 0.3172 0.0698 0.0667 0.0649 278 PHE A CB 2130 C CG . PHE A 278 ? 0.3767 0.3271 0.2932 0.0575 0.0586 0.0555 278 PHE A CG 2131 C CD1 . PHE A 278 ? 0.3602 0.3024 0.2795 0.0460 0.0604 0.0498 278 PHE A CD1 2132 C CD2 . PHE A 278 ? 0.3559 0.3270 0.2724 0.0575 0.0495 0.0526 278 PHE A CD2 2133 C CE1 . PHE A 278 ? 0.3425 0.2968 0.2636 0.0364 0.0530 0.0423 278 PHE A CE1 2134 C CE2 . PHE A 278 ? 0.3335 0.3144 0.2521 0.0470 0.0430 0.0452 278 PHE A CE2 2135 C CZ . PHE A 278 ? 0.3413 0.3136 0.2616 0.0372 0.0446 0.0406 278 PHE A CZ 2136 N N . LYS A 279 ? 0.4166 0.3326 0.3452 0.0540 0.0753 0.0415 279 LYS A N 2137 C CA . LYS A 279 ? 0.4142 0.3346 0.3476 0.0503 0.0741 0.0311 279 LYS A CA 2138 C C . LYS A 279 ? 0.3919 0.3304 0.3263 0.0403 0.0649 0.0236 279 LYS A C 2139 O O . LYS A 279 ? 0.3952 0.3403 0.3325 0.0368 0.0630 0.0153 279 LYS A O 2140 C CB . LYS A 279 ? 0.4279 0.3274 0.3664 0.0456 0.0839 0.0240 279 LYS A CB 2141 C CG . LYS A 279 ? 0.4669 0.3444 0.4049 0.0556 0.0949 0.0308 279 LYS A CG 2142 C CD . LYS A 279 ? 0.5092 0.3903 0.4466 0.0680 0.0954 0.0328 279 LYS A CD 2143 C CE . LYS A 279 ? 0.5536 0.4125 0.4890 0.0804 0.1065 0.0426 279 LYS A CE 2144 N NZ . LYS A 279 ? 0.5772 0.4458 0.5096 0.0964 0.1048 0.0497 279 LYS A NZ 2145 N N . GLY A 280 ? 0.3745 0.3205 0.3060 0.0362 0.0596 0.0268 280 GLY A N 2146 C CA . GLY A 280 ? 0.3551 0.3174 0.2865 0.0285 0.0511 0.0217 280 GLY A CA 2147 C C . GLY A 280 ? 0.3435 0.3228 0.2729 0.0338 0.0445 0.0247 280 GLY A C 2148 O O . GLY A 280 ? 0.3509 0.3311 0.2804 0.0428 0.0465 0.0283 280 GLY A O 2149 N N . PHE A 281 ? 0.3275 0.3204 0.2558 0.0284 0.0373 0.0230 281 PHE A N 2150 C CA . PHE A 281 ? 0.3253 0.3346 0.2529 0.0317 0.0316 0.0250 281 PHE A CA 2151 C C . PHE A 281 ? 0.3220 0.3388 0.2461 0.0335 0.0271 0.0305 281 PHE A C 2152 O O . PHE A 281 ? 0.3217 0.3343 0.2434 0.0294 0.0262 0.0313 281 PHE A O 2153 C CB . PHE A 281 ? 0.3116 0.3321 0.2410 0.0257 0.0278 0.0189 281 PHE A CB 2154 C CG . PHE A 281 ? 0.2955 0.3191 0.2233 0.0170 0.0236 0.0165 281 PHE A CG 2155 C CD1 . PHE A 281 ? 0.2859 0.3182 0.2117 0.0154 0.0184 0.0190 281 PHE A CD1 2156 C CD2 . PHE A 281 ? 0.2838 0.3030 0.2121 0.0110 0.0248 0.0109 281 PHE A CD2 2157 C CE1 . PHE A 281 ? 0.2844 0.3180 0.2085 0.0085 0.0152 0.0172 281 PHE A CE1 2158 C CE2 . PHE A 281 ? 0.2763 0.2995 0.2027 0.0047 0.0210 0.0092 281 PHE A CE2 2159 C CZ . PHE A 281 ? 0.2707 0.2999 0.1948 0.0037 0.0165 0.0128 281 PHE A CZ 2160 N N . VAL A 282 ? 0.3153 0.3449 0.2394 0.0399 0.0244 0.0333 282 VAL A N 2161 C CA . VAL A 282 ? 0.3098 0.3502 0.2310 0.0423 0.0198 0.0370 282 VAL A CA 2162 C C . VAL A 282 ? 0.2967 0.3517 0.2200 0.0353 0.0137 0.0323 282 VAL A C 2163 O O . VAL A 282 ? 0.2906 0.3554 0.2177 0.0348 0.0127 0.0294 282 VAL A O 2164 C CB . VAL A 282 ? 0.3201 0.3679 0.2404 0.0545 0.0207 0.0427 282 VAL A CB 2165 C CG1 . VAL A 282 ? 0.2990 0.3634 0.2168 0.0568 0.0149 0.0446 282 VAL A CG1 2166 C CG2 . VAL A 282 ? 0.3262 0.3564 0.2436 0.0620 0.0281 0.0489 282 VAL A CG2 2167 N N . ILE A 283 ? 0.2911 0.3469 0.2119 0.0300 0.0103 0.0316 283 ILE A N 2168 C CA . ILE A 283 ? 0.2761 0.3418 0.1985 0.0228 0.0057 0.0274 283 ILE A CA 2169 C C . ILE A 283 ? 0.2889 0.3676 0.2103 0.0245 0.0013 0.0278 283 ILE A C 2170 O O . ILE A 283 ? 0.2927 0.3700 0.2100 0.0292 0.0012 0.0313 283 ILE A O 2171 C CB . ILE A 283 ? 0.2757 0.3317 0.1967 0.0143 0.0055 0.0248 283 ILE A CB 2172 C CG1 . ILE A 283 ? 0.2541 0.3174 0.1769 0.0074 0.0024 0.0212 283 ILE A CG1 2173 C CG2 . ILE A 283 ? 0.2495 0.2973 0.1663 0.0143 0.0055 0.0269 283 ILE A CG2 2174 C CD1 . ILE A 283 ? 0.2571 0.3117 0.1779 0.0010 0.0026 0.0196 283 ILE A CD1 2175 N N . SER A 284 ? 0.2886 0.3809 0.2140 0.0204 -0.0018 0.0238 284 SER A N 2176 C CA . SER A 284 ? 0.2886 0.3940 0.2140 0.0194 -0.0061 0.0215 284 SER A CA 2177 C C . SER A 284 ? 0.2934 0.3900 0.2153 0.0127 -0.0076 0.0195 284 SER A C 2178 O O . SER A 284 ? 0.2899 0.3729 0.2105 0.0081 -0.0057 0.0196 284 SER A O 2179 C CB . SER A 284 ? 0.2793 0.4013 0.2114 0.0151 -0.0082 0.0165 284 SER A CB 2180 O OG . SER A 284 ? 0.2798 0.3958 0.2136 0.0047 -0.0080 0.0129 284 SER A OG 2181 N N . ASP A 285 ? 0.2907 0.3969 0.2114 0.0128 -0.0110 0.0172 285 ASP A N 2182 C CA . ASP A 285 ? 0.2976 0.3983 0.2166 0.0059 -0.0125 0.0135 285 ASP A CA 2183 C C . ASP A 285 ? 0.2975 0.4041 0.2223 -0.0029 -0.0134 0.0076 285 ASP A C 2184 O O . ASP A 285 ? 0.3030 0.4202 0.2334 -0.0035 -0.0131 0.0063 285 ASP A O 2185 C CB . ASP A 285 ? 0.2936 0.4013 0.2080 0.0098 -0.0152 0.0128 285 ASP A CB 2186 C CG . ASP A 285 ? 0.3094 0.4049 0.2196 0.0060 -0.0150 0.0116 285 ASP A CG 2187 O OD1 . ASP A 285 ? 0.3134 0.3985 0.2253 -0.0009 -0.0138 0.0096 285 ASP A OD1 2188 O OD2 . ASP A 285 ? 0.3027 0.3996 0.2075 0.0107 -0.0156 0.0133 285 ASP A OD2 2189 N N . TRP A 286 ? 0.2954 0.3946 0.2191 -0.0094 -0.0138 0.0041 286 TRP A N 2190 C CA . TRP A 286 ? 0.2988 0.3973 0.2272 -0.0186 -0.0130 -0.0006 286 TRP A CA 2191 C C . TRP A 286 ? 0.3032 0.4209 0.2377 -0.0215 -0.0153 -0.0070 286 TRP A C 2192 O O . TRP A 286 ? 0.3064 0.4321 0.2401 -0.0212 -0.0182 -0.0116 286 TRP A O 2193 C CB . TRP A 286 ? 0.3012 0.3857 0.2257 -0.0226 -0.0125 -0.0022 286 TRP A CB 2194 C CG . TRP A 286 ? 0.3052 0.3844 0.2331 -0.0317 -0.0107 -0.0067 286 TRP A CG 2195 C CD1 . TRP A 286 ? 0.3067 0.3946 0.2395 -0.0379 -0.0115 -0.0144 286 TRP A CD1 2196 C CD2 . TRP A 286 ? 0.2983 0.3610 0.2243 -0.0353 -0.0072 -0.0038 286 TRP A CD2 2197 N NE1 . TRP A 286 ? 0.3218 0.3970 0.2564 -0.0458 -0.0078 -0.0161 286 TRP A NE1 2198 C CE2 . TRP A 286 ? 0.3175 0.3772 0.2473 -0.0435 -0.0052 -0.0089 286 TRP A CE2 2199 C CE3 . TRP A 286 ? 0.3031 0.3542 0.2247 -0.0321 -0.0054 0.0024 286 TRP A CE3 2200 C CZ2 . TRP A 286 ? 0.3287 0.3723 0.2571 -0.0476 -0.0008 -0.0064 286 TRP A CZ2 2201 C CZ3 . TRP A 286 ? 0.3080 0.3463 0.2280 -0.0357 -0.0021 0.0044 286 TRP A CZ3 2202 C CH2 . TRP A 286 ? 0.3167 0.3504 0.2396 -0.0428 0.0004 0.0008 286 TRP A CH2 2203 N N . GLU A 287 ? 0.2977 0.4246 0.2388 -0.0243 -0.0140 -0.0080 287 GLU A N 2204 C CA . GLU A 287 ? 0.2975 0.4471 0.2463 -0.0267 -0.0161 -0.0145 287 GLU A CA 2205 C C . GLU A 287 ? 0.2896 0.4564 0.2366 -0.0165 -0.0202 -0.0139 287 GLU A C 2206 O O . GLU A 287 ? 0.2840 0.4716 0.2354 -0.0174 -0.0235 -0.0204 287 GLU A O 2207 C CB . GLU A 287 ? 0.2931 0.4443 0.2459 -0.0370 -0.0164 -0.0232 287 GLU A CB 2208 C CG . GLU A 287 ? 0.3067 0.4418 0.2618 -0.0469 -0.0114 -0.0235 287 GLU A CG 2209 C CD . GLU A 287 ? 0.3267 0.4574 0.2843 -0.0562 -0.0106 -0.0317 287 GLU A CD 2210 O OE1 . GLU A 287 ? 0.3554 0.4927 0.3111 -0.0546 -0.0144 -0.0371 287 GLU A OE1 2211 O OE2 . GLU A 287 ? 0.3577 0.4777 0.3188 -0.0651 -0.0058 -0.0327 287 GLU A OE2 2212 N N . GLY A 288 ? 0.2846 0.4432 0.2250 -0.0069 -0.0197 -0.0061 288 GLY A N 2213 C CA . GLY A 288 ? 0.2897 0.4612 0.2265 0.0044 -0.0223 -0.0031 288 GLY A CA 2214 C C . GLY A 288 ? 0.2948 0.4901 0.2380 0.0092 -0.0240 -0.0046 288 GLY A C 2215 O O . GLY A 288 ? 0.2928 0.5084 0.2358 0.0150 -0.0279 -0.0067 288 GLY A O 2216 N N . ILE A 289 ? 0.2914 0.4859 0.2401 0.0074 -0.0211 -0.0034 289 ILE A N 2217 C CA . ILE A 289 ? 0.2920 0.5104 0.2480 0.0115 -0.0223 -0.0053 289 ILE A CA 2218 C C . ILE A 289 ? 0.2997 0.5414 0.2644 0.0031 -0.0255 -0.0157 289 ILE A C 2219 O O . ILE A 289 ? 0.3006 0.5688 0.2695 0.0089 -0.0290 -0.0185 289 ILE A O 2220 C CB . ILE A 289 ? 0.2918 0.5044 0.2515 0.0122 -0.0179 -0.0019 289 ILE A CB 2221 C CG1 . ILE A 289 ? 0.2891 0.4996 0.2555 -0.0011 -0.0154 -0.0069 289 ILE A CG1 2222 C CG2 . ILE A 289 ? 0.2780 0.4658 0.2296 0.0181 -0.0144 0.0061 289 ILE A CG2 2223 C CD1 . ILE A 289 ? 0.2757 0.4877 0.2465 -0.0001 -0.0114 -0.0048 289 ILE A CD1 2224 N N . ASP A 290 ? 0.3040 0.5361 0.2714 -0.0102 -0.0242 -0.0214 290 ASP A N 2225 C CA . ASP A 290 ? 0.3127 0.5631 0.2887 -0.0206 -0.0262 -0.0326 290 ASP A CA 2226 C C . ASP A 290 ? 0.3235 0.5926 0.2972 -0.0155 -0.0320 -0.0375 290 ASP A C 2227 O O . ASP A 290 ? 0.3284 0.6256 0.3102 -0.0180 -0.0353 -0.0463 290 ASP A O 2228 C CB . ASP A 290 ? 0.3152 0.5454 0.2919 -0.0343 -0.0228 -0.0366 290 ASP A CB 2229 C CG . ASP A 290 ? 0.3077 0.5164 0.2837 -0.0382 -0.0171 -0.0303 290 ASP A CG 2230 O OD1 . ASP A 290 ? 0.2758 0.4719 0.2450 -0.0301 -0.0160 -0.0218 290 ASP A OD1 2231 O OD2 . ASP A 290 ? 0.3297 0.5343 0.3117 -0.0498 -0.0132 -0.0342 290 ASP A OD2 2232 N N . ARG A 291 ? 0.3297 0.5846 0.2923 -0.0085 -0.0330 -0.0322 291 ARG A N 2233 C CA . ARG A 291 ? 0.3380 0.6067 0.2957 -0.0038 -0.0379 -0.0361 291 ARG A CA 2234 C C . ARG A 291 ? 0.3427 0.6339 0.2972 0.0116 -0.0415 -0.0314 291 ARG A C 2235 O O . ARG A 291 ? 0.3565 0.6622 0.3058 0.0175 -0.0456 -0.0336 291 ARG A O 2236 C CB . ARG A 291 ? 0.3389 0.5829 0.2863 -0.0038 -0.0367 -0.0327 291 ARG A CB 2237 C CG . ARG A 291 ? 0.3308 0.5562 0.2813 -0.0179 -0.0338 -0.0386 291 ARG A CG 2238 C CD . ARG A 291 ? 0.3226 0.5241 0.2637 -0.0172 -0.0323 -0.0351 291 ARG A CD 2239 N NE . ARG A 291 ? 0.3268 0.5064 0.2705 -0.0280 -0.0280 -0.0367 291 ARG A NE 2240 C CZ . ARG A 291 ? 0.3306 0.4889 0.2684 -0.0300 -0.0261 -0.0355 291 ARG A CZ 2241 N NH1 . ARG A 291 ? 0.3470 0.5033 0.2764 -0.0230 -0.0281 -0.0335 291 ARG A NH1 2242 N NH2 . ARG A 291 ? 0.3105 0.4502 0.2507 -0.0385 -0.0219 -0.0358 291 ARG A NH2 2243 N N . ILE A 292 ? 0.3410 0.6358 0.2984 0.0186 -0.0396 -0.0248 292 ILE A N 2244 C CA . ILE A 292 ? 0.3354 0.6535 0.2912 0.0340 -0.0424 -0.0202 292 ILE A CA 2245 C C . ILE A 292 ? 0.3414 0.6973 0.3053 0.0321 -0.0482 -0.0316 292 ILE A C 2246 O O . ILE A 292 ? 0.3434 0.7217 0.3027 0.0437 -0.0527 -0.0309 292 ILE A O 2247 C CB . ILE A 292 ? 0.3333 0.6479 0.2923 0.0409 -0.0387 -0.0127 292 ILE A CB 2248 C CG1 . ILE A 292 ? 0.3176 0.5988 0.2676 0.0459 -0.0334 -0.0015 292 ILE A CG1 2249 C CG2 . ILE A 292 ? 0.3282 0.6721 0.2882 0.0563 -0.0417 -0.0099 292 ILE A CG2 2250 C CD1 . ILE A 292 ? 0.3311 0.6032 0.2854 0.0480 -0.0286 0.0030 292 ILE A CD1 2251 N N . THR A 293 ? 0.3353 0.6988 0.3113 0.0173 -0.0477 -0.0422 293 THR A N 2252 C CA . THR A 293 ? 0.3400 0.7399 0.3264 0.0119 -0.0525 -0.0556 293 THR A CA 2253 C C . THR A 293 ? 0.3520 0.7534 0.3380 0.0011 -0.0550 -0.0672 293 THR A C 2254 O O . THR A 293 ? 0.3460 0.7176 0.3259 -0.0055 -0.0521 -0.0658 293 THR A O 2255 C CB . THR A 293 ? 0.3349 0.7448 0.3365 0.0002 -0.0496 -0.0622 293 THR A CB 2256 O OG1 . THR A 293 ? 0.3252 0.7067 0.3290 -0.0157 -0.0443 -0.0649 293 THR A OG1 2257 C CG2 . THR A 293 ? 0.3183 0.7293 0.3214 0.0109 -0.0469 -0.0523 293 THR A CG2 2258 N N . THR A 294 ? 0.3636 0.8015 0.3566 -0.0006 -0.0605 -0.0794 294 THR A N 2259 C CA . THR A 294 ? 0.3832 0.8290 0.3790 -0.0125 -0.0631 -0.0942 294 THR A CA 2260 C C . THR A 294 ? 0.3840 0.8562 0.3979 -0.0271 -0.0634 -0.1098 294 THR A C 2261 O O . THR A 294 ? 0.3880 0.8959 0.4095 -0.0212 -0.0672 -0.1128 294 THR A O 2262 C CB . THR A 294 ? 0.3916 0.8601 0.3774 0.0000 -0.0699 -0.0959 294 THR A CB 2263 O OG1 . THR A 294 ? 0.4014 0.8427 0.3712 0.0115 -0.0682 -0.0815 294 THR A OG1 2264 C CG2 . THR A 294 ? 0.4085 0.8892 0.3979 -0.0125 -0.0729 -0.1137 294 THR A CG2 2265 N N . PRO A 295 ? 0.3856 0.8397 0.4068 -0.0460 -0.0587 -0.1190 295 PRO A N 2266 C CA . PRO A 295 ? 0.3892 0.7993 0.4025 -0.0525 -0.0531 -0.1137 295 PRO A CA 2267 C C . PRO A 295 ? 0.3826 0.7624 0.3906 -0.0475 -0.0476 -0.0973 295 PRO A C 2268 O O . PRO A 295 ? 0.3816 0.7722 0.3948 -0.0429 -0.0467 -0.0920 295 PRO A O 2269 C CB . PRO A 295 ? 0.3928 0.7984 0.4188 -0.0736 -0.0488 -0.1283 295 PRO A CB 2270 C CG . PRO A 295 ? 0.3983 0.8410 0.4404 -0.0794 -0.0503 -0.1385 295 PRO A CG 2271 C CD . PRO A 295 ? 0.3908 0.8691 0.4295 -0.0623 -0.0583 -0.1361 295 PRO A CD 2272 N N . ALA A 296 ? 0.3827 0.7266 0.3807 -0.0480 -0.0441 -0.0901 296 ALA A N 2273 C CA . ALA A 296 ? 0.3739 0.6892 0.3664 -0.0441 -0.0391 -0.0760 296 ALA A CA 2274 C C . ALA A 296 ? 0.3720 0.6839 0.3758 -0.0554 -0.0335 -0.0774 296 ALA A C 2275 O O . ALA A 296 ? 0.3773 0.6904 0.3903 -0.0701 -0.0309 -0.0878 296 ALA A O 2276 C CB . ALA A 296 ? 0.3714 0.6523 0.3532 -0.0450 -0.0364 -0.0707 296 ALA A CB 2277 N N . GLY A 297 ? 0.3659 0.6738 0.3690 -0.0485 -0.0313 -0.0672 297 GLY A N 2278 C CA . GLY A 297 ? 0.3619 0.6671 0.3741 -0.0572 -0.0256 -0.0668 297 GLY A CA 2279 C C . GLY A 297 ? 0.3610 0.6995 0.3885 -0.0643 -0.0261 -0.0771 297 GLY A C 2280 O O . GLY A 297 ? 0.3623 0.6988 0.3984 -0.0740 -0.0205 -0.0781 297 GLY A O 2281 N N . SER A 298 ? 0.3587 0.7293 0.3898 -0.0593 -0.0326 -0.0847 298 SER A N 2282 C CA . SER A 298 ? 0.3540 0.7610 0.4011 -0.0665 -0.0339 -0.0965 298 SER A CA 2283 C C . SER A 298 ? 0.3431 0.7714 0.3957 -0.0570 -0.0340 -0.0911 298 SER A C 2284 O O . SER A 298 ? 0.3451 0.8021 0.4122 -0.0637 -0.0335 -0.0997 298 SER A O 2285 C CB . SER A 298 ? 0.3626 0.7994 0.4125 -0.0662 -0.0410 -0.1091 298 SER A CB 2286 O OG . SER A 298 ? 0.3628 0.8126 0.4023 -0.0471 -0.0476 -0.1023 298 SER A OG 2287 N N . ASP A 299 ? 0.3294 0.7440 0.3710 -0.0416 -0.0342 -0.0775 299 ASP A N 2288 C CA . ASP A 299 ? 0.3209 0.7484 0.3663 -0.0321 -0.0328 -0.0713 299 ASP A CA 2289 C C . ASP A 299 ? 0.3145 0.7076 0.3483 -0.0247 -0.0285 -0.0576 299 ASP A C 2290 O O . ASP A 299 ? 0.3142 0.7021 0.3383 -0.0089 -0.0307 -0.0486 299 ASP A O 2291 C CB . ASP A 299 ? 0.3225 0.7844 0.3684 -0.0158 -0.0396 -0.0714 299 ASP A CB 2292 C CG . ASP A 299 ? 0.3326 0.8140 0.3859 -0.0074 -0.0379 -0.0679 299 ASP A CG 2293 O OD1 . ASP A 299 ? 0.3543 0.8196 0.4101 -0.0125 -0.0316 -0.0639 299 ASP A OD1 2294 O OD2 . ASP A 299 ? 0.3544 0.8682 0.4106 0.0053 -0.0429 -0.0689 299 ASP A OD2 2295 N N . TYR A 300 ? 0.3038 0.6734 0.3387 -0.0363 -0.0221 -0.0561 300 TYR A N 2296 C CA . TYR A 300 ? 0.2971 0.6333 0.3207 -0.0316 -0.0183 -0.0449 300 TYR A CA 2297 C C . TYR A 300 ? 0.2885 0.6296 0.3115 -0.0192 -0.0167 -0.0376 300 TYR A C 2298 O O . TYR A 300 ? 0.2832 0.6027 0.2960 -0.0101 -0.0155 -0.0288 300 TYR A O 2299 C CB . TYR A 300 ? 0.2996 0.6114 0.3236 -0.0462 -0.0120 -0.0450 300 TYR A CB 2300 C CG . TYR A 300 ? 0.3008 0.5785 0.3118 -0.0420 -0.0095 -0.0352 300 TYR A CG 2301 C CD1 . TYR A 300 ? 0.3119 0.5720 0.3128 -0.0388 -0.0124 -0.0329 300 TYR A CD1 2302 C CD2 . TYR A 300 ? 0.3145 0.5795 0.3235 -0.0414 -0.0044 -0.0288 300 TYR A CD2 2303 C CE1 . TYR A 300 ? 0.3114 0.5427 0.3015 -0.0355 -0.0102 -0.0248 300 TYR A CE1 2304 C CE2 . TYR A 300 ? 0.3088 0.5454 0.3065 -0.0379 -0.0025 -0.0211 300 TYR A CE2 2305 C CZ . TYR A 300 ? 0.3104 0.5307 0.2993 -0.0352 -0.0054 -0.0192 300 TYR A CZ 2306 O OH . TYR A 300 ? 0.2907 0.4857 0.2696 -0.0322 -0.0036 -0.0124 300 TYR A OH 2307 N N . SER A 301 ? 0.2888 0.6588 0.3236 -0.0192 -0.0164 -0.0422 301 SER A N 2308 C CA . SER A 301 ? 0.2872 0.6667 0.3227 -0.0061 -0.0152 -0.0367 301 SER A CA 2309 C C . SER A 301 ? 0.2891 0.6712 0.3161 0.0125 -0.0197 -0.0305 301 SER A C 2310 O O . SER A 301 ? 0.2793 0.6449 0.2989 0.0235 -0.0172 -0.0221 301 SER A O 2311 C CB . SER A 301 ? 0.2861 0.7009 0.3370 -0.0095 -0.0146 -0.0440 301 SER A CB 2312 O OG . SER A 301 ? 0.2971 0.7248 0.3487 0.0058 -0.0144 -0.0393 301 SER A OG 2313 N N . TYR A 302 ? 0.2936 0.6961 0.3214 0.0158 -0.0258 -0.0349 302 TYR A N 2314 C CA . TYR A 302 ? 0.3021 0.7051 0.3199 0.0330 -0.0297 -0.0281 302 TYR A CA 2315 C C . TYR A 302 ? 0.2927 0.6577 0.2963 0.0344 -0.0279 -0.0201 302 TYR A C 2316 O O . TYR A 302 ? 0.2888 0.6400 0.2839 0.0479 -0.0264 -0.0108 302 TYR A O 2317 C CB . TYR A 302 ? 0.3205 0.7552 0.3414 0.0352 -0.0369 -0.0353 302 TYR A CB 2318 C CG . TYR A 302 ? 0.3541 0.7889 0.3630 0.0531 -0.0404 -0.0272 302 TYR A CG 2319 C CD1 . TYR A 302 ? 0.3770 0.8227 0.3837 0.0721 -0.0403 -0.0191 302 TYR A CD1 2320 C CD2 . TYR A 302 ? 0.3631 0.7862 0.3624 0.0518 -0.0432 -0.0270 302 TYR A CD2 2321 C CE1 . TYR A 302 ? 0.3956 0.8394 0.3905 0.0892 -0.0423 -0.0102 302 TYR A CE1 2322 C CE2 . TYR A 302 ? 0.3834 0.8063 0.3709 0.0684 -0.0456 -0.0185 302 TYR A CE2 2323 C CZ . TYR A 302 ? 0.3871 0.8198 0.3723 0.0870 -0.0449 -0.0097 302 TYR A CZ 2324 O OH . TYR A 302 ? 0.4147 0.8457 0.3877 0.1039 -0.0461 0.0000 302 TYR A OH 2325 N N . SER A 303 ? 0.2834 0.6315 0.2853 0.0204 -0.0274 -0.0240 303 SER A N 2326 C CA . SER A 303 ? 0.2762 0.5898 0.2660 0.0202 -0.0255 -0.0176 303 SER A CA 2327 C C . SER A 303 ? 0.2723 0.5623 0.2573 0.0256 -0.0202 -0.0091 303 SER A C 2328 O O . SER A 303 ? 0.2788 0.5507 0.2542 0.0346 -0.0193 -0.0016 303 SER A O 2329 C CB . SER A 303 ? 0.2696 0.5687 0.2602 0.0037 -0.0245 -0.0233 303 SER A CB 2330 O OG . SER A 303 ? 0.2713 0.5854 0.2633 -0.0001 -0.0292 -0.0309 303 SER A OG 2331 N N . VAL A 304 ? 0.2653 0.5565 0.2572 0.0196 -0.0163 -0.0109 304 VAL A N 2332 C CA . VAL A 304 ? 0.2615 0.5333 0.2498 0.0235 -0.0112 -0.0049 304 VAL A CA 2333 C C . VAL A 304 ? 0.2717 0.5502 0.2584 0.0404 -0.0107 0.0005 304 VAL A C 2334 O O . VAL A 304 ? 0.2715 0.5286 0.2502 0.0479 -0.0081 0.0070 304 VAL A O 2335 C CB . VAL A 304 ? 0.2610 0.5353 0.2567 0.0130 -0.0069 -0.0085 304 VAL A CB 2336 C CG1 . VAL A 304 ? 0.2471 0.5066 0.2392 0.0188 -0.0019 -0.0035 304 VAL A CG1 2337 C CG2 . VAL A 304 ? 0.2556 0.5162 0.2506 -0.0022 -0.0058 -0.0115 304 VAL A CG2 2338 N N . LYS A 305 ? 0.2705 0.5791 0.2652 0.0462 -0.0129 -0.0024 305 LYS A N 2339 C CA . LYS A 305 ? 0.2875 0.6053 0.2812 0.0639 -0.0124 0.0029 305 LYS A CA 2340 C C . LYS A 305 ? 0.2874 0.5921 0.2699 0.0758 -0.0138 0.0106 305 LYS A C 2341 O O . LYS A 305 ? 0.2911 0.5766 0.2675 0.0860 -0.0096 0.0179 305 LYS A O 2342 C CB . LYS A 305 ? 0.2817 0.6390 0.2861 0.0681 -0.0160 -0.0022 305 LYS A CB 2343 C CG . LYS A 305 ? 0.3308 0.6999 0.3345 0.0880 -0.0154 0.0037 305 LYS A CG 2344 C CD . LYS A 305 ? 0.3812 0.7932 0.3947 0.0932 -0.0205 -0.0017 305 LYS A CD 2345 C CE . LYS A 305 ? 0.4193 0.8429 0.4282 0.1160 -0.0217 0.0062 305 LYS A CE 2346 N NZ . LYS A 305 ? 0.3954 0.8645 0.4133 0.1222 -0.0277 0.0008 305 LYS A NZ 2347 N N . ALA A 306 ? 0.2792 0.5936 0.2593 0.0739 -0.0189 0.0086 306 ALA A N 2348 C CA . ALA A 306 ? 0.2837 0.5906 0.2532 0.0854 -0.0204 0.0159 306 ALA A CA 2349 C C . ALA A 306 ? 0.2847 0.5542 0.2444 0.0835 -0.0160 0.0221 306 ALA A C 2350 O O . ALA A 306 ? 0.2932 0.5492 0.2451 0.0957 -0.0131 0.0307 306 ALA A O 2351 C CB . ALA A 306 ? 0.2785 0.6066 0.2479 0.0823 -0.0270 0.0105 306 ALA A CB 2352 N N . SER A 307 ? 0.2771 0.5305 0.2374 0.0683 -0.0151 0.0177 307 SER A N 2353 C CA . SER A 307 ? 0.2825 0.5040 0.2347 0.0653 -0.0115 0.0222 307 SER A CA 2354 C C . SER A 307 ? 0.2847 0.4874 0.2360 0.0700 -0.0052 0.0265 307 SER A C 2355 O O . SER A 307 ? 0.2857 0.4675 0.2301 0.0761 -0.0015 0.0328 307 SER A O 2356 C CB . SER A 307 ? 0.2759 0.4878 0.2292 0.0490 -0.0124 0.0163 307 SER A CB 2357 O OG . SER A 307 ? 0.2950 0.5132 0.2564 0.0401 -0.0111 0.0110 307 SER A OG 2358 N N . ILE A 308 ? 0.2818 0.4925 0.2406 0.0666 -0.0036 0.0224 308 ILE A N 2359 C CA . ILE A 308 ? 0.2832 0.4779 0.2417 0.0699 0.0023 0.0244 308 ILE A CA 2360 C C . ILE A 308 ? 0.2976 0.4935 0.2543 0.0870 0.0050 0.0306 308 ILE A C 2361 O O . ILE A 308 ? 0.3043 0.4774 0.2563 0.0920 0.0104 0.0348 308 ILE A O 2362 C CB . ILE A 308 ? 0.2826 0.4861 0.2487 0.0617 0.0037 0.0184 308 ILE A CB 2363 C CG1 . ILE A 308 ? 0.2605 0.4572 0.2266 0.0457 0.0025 0.0141 308 ILE A CG1 2364 C CG2 . ILE A 308 ? 0.2780 0.4675 0.2435 0.0669 0.0098 0.0196 308 ILE A CG2 2365 C CD1 . ILE A 308 ? 0.2612 0.4304 0.2192 0.0414 0.0042 0.0165 308 ILE A CD1 2366 N N . LEU A 309 ? 0.2947 0.5171 0.2552 0.0960 0.0017 0.0310 309 LEU A N 2367 C CA . LEU A 309 ? 0.3088 0.5334 0.2663 0.1145 0.0041 0.0385 309 LEU A CA 2368 C C . LEU A 309 ? 0.3214 0.5282 0.2685 0.1217 0.0054 0.0469 309 LEU A C 2369 O O . LEU A 309 ? 0.3453 0.5379 0.2877 0.1348 0.0109 0.0546 309 LEU A O 2370 C CB . LEU A 309 ? 0.3026 0.5636 0.2666 0.1235 -0.0004 0.0370 309 LEU A CB 2371 C CG . LEU A 309 ? 0.2923 0.5699 0.2669 0.1206 0.0007 0.0306 309 LEU A CG 2372 C CD1 . LEU A 309 ? 0.2623 0.5784 0.2441 0.1300 -0.0038 0.0289 309 LEU A CD1 2373 C CD2 . LEU A 309 ? 0.2662 0.5227 0.2401 0.1267 0.0084 0.0331 309 LEU A CD2 2374 N N . ALA A 310 ? 0.3175 0.5240 0.2609 0.1132 0.0012 0.0455 310 ALA A N 2375 C CA . ALA A 310 ? 0.3253 0.5149 0.2586 0.1184 0.0029 0.0532 310 ALA A CA 2376 C C . ALA A 310 ? 0.3372 0.4920 0.2666 0.1150 0.0102 0.0563 310 ALA A C 2377 O O . ALA A 310 ? 0.3514 0.4890 0.2734 0.1228 0.0147 0.0644 310 ALA A O 2378 C CB . ALA A 310 ? 0.3194 0.5176 0.2502 0.1092 -0.0031 0.0495 310 ALA A CB 2379 N N . GLY A 311 ? 0.3272 0.4724 0.2614 0.1032 0.0117 0.0496 311 GLY A N 2380 C CA . GLY A 311 ? 0.3380 0.4538 0.2699 0.0996 0.0184 0.0504 311 GLY A CA 2381 C C . GLY A 311 ? 0.3284 0.4325 0.2599 0.0839 0.0171 0.0451 311 GLY A C 2382 O O . GLY A 311 ? 0.3324 0.4143 0.2619 0.0803 0.0220 0.0453 311 GLY A O 2383 N N . LEU A 312 ? 0.3184 0.4376 0.2521 0.0748 0.0109 0.0402 312 LEU A N 2384 C CA . LEU A 312 ? 0.3119 0.4209 0.2450 0.0611 0.0098 0.0357 312 LEU A CA 2385 C C . LEU A 312 ? 0.3108 0.4144 0.2481 0.0551 0.0125 0.0308 312 LEU A C 2386 O O . LEU A 312 ? 0.3075 0.4233 0.2497 0.0581 0.0130 0.0287 312 LEU A O 2387 C CB . LEU A 312 ? 0.3013 0.4258 0.2356 0.0536 0.0034 0.0318 312 LEU A CB 2388 C CG . LEU A 312 ? 0.3012 0.4275 0.2298 0.0564 0.0006 0.0350 312 LEU A CG 2389 C CD1 . LEU A 312 ? 0.2768 0.4196 0.2039 0.0697 -0.0008 0.0396 312 LEU A CD1 2390 C CD2 . LEU A 312 ? 0.2856 0.4199 0.2154 0.0457 -0.0043 0.0292 312 LEU A CD2 2391 N N . ASP A 313 ? 0.3073 0.3942 0.2424 0.0473 0.0145 0.0289 313 ASP A N 2392 C CA . ASP A 313 ? 0.2994 0.3805 0.2367 0.0425 0.0174 0.0243 313 ASP A CA 2393 C C . ASP A 313 ? 0.2910 0.3780 0.2294 0.0314 0.0143 0.0199 313 ASP A C 2394 O O . ASP A 313 ? 0.2823 0.3765 0.2239 0.0288 0.0152 0.0166 313 ASP A O 2395 C CB . ASP A 313 ? 0.3037 0.3635 0.2384 0.0422 0.0225 0.0242 313 ASP A CB 2396 C CG . ASP A 313 ? 0.3124 0.3622 0.2456 0.0527 0.0272 0.0294 313 ASP A CG 2397 O OD1 . ASP A 313 ? 0.2928 0.3277 0.2228 0.0524 0.0298 0.0322 313 ASP A OD1 2398 O OD2 . ASP A 313 ? 0.2938 0.3512 0.2293 0.0618 0.0286 0.0312 313 ASP A OD2 2399 N N . MET A 314 ? 0.2887 0.3716 0.2240 0.0255 0.0114 0.0204 314 MET A N 2400 C CA . MET A 314 ? 0.2856 0.3710 0.2209 0.0159 0.0090 0.0176 314 MET A CA 2401 C C . MET A 314 ? 0.2802 0.3748 0.2160 0.0130 0.0047 0.0177 314 MET A C 2402 O O . MET A 314 ? 0.2802 0.3725 0.2131 0.0160 0.0030 0.0199 314 MET A O 2403 C CB . MET A 314 ? 0.2813 0.3519 0.2125 0.0111 0.0100 0.0170 314 MET A CB 2404 C CG . MET A 314 ? 0.2732 0.3448 0.2032 0.0028 0.0083 0.0152 314 MET A CG 2405 S SD . MET A 314 ? 0.2877 0.3461 0.2131 -0.0010 0.0089 0.0144 314 MET A SD 2406 C CE . MET A 314 ? 0.2776 0.3341 0.2038 0.0005 0.0128 0.0109 314 MET A CE 2407 N N . ILE A 315 ? 0.2731 0.3783 0.2125 0.0070 0.0035 0.0150 315 ILE A N 2408 C CA . ILE A 315 ? 0.2655 0.3795 0.2066 0.0025 0.0001 0.0131 315 ILE A CA 2409 C C . ILE A 315 ? 0.2682 0.3723 0.2067 -0.0062 -0.0001 0.0121 315 ILE A C 2410 O O . ILE A 315 ? 0.2657 0.3672 0.2047 -0.0114 0.0021 0.0116 315 ILE A O 2411 C CB . ILE A 315 ? 0.2641 0.3986 0.2128 0.0016 -0.0006 0.0101 315 ILE A CB 2412 C CG1 . ILE A 315 ? 0.2624 0.4073 0.2132 0.0123 -0.0004 0.0118 315 ILE A CG1 2413 C CG2 . ILE A 315 ? 0.2548 0.3997 0.2065 -0.0045 -0.0039 0.0062 315 ILE A CG2 2414 C CD1 . ILE A 315 ? 0.2667 0.4106 0.2134 0.0208 -0.0024 0.0151 315 ILE A CD1 2415 N N . MET A 316 ? 0.2659 0.3644 0.2010 -0.0068 -0.0024 0.0123 316 MET A N 2416 C CA . MET A 316 ? 0.2688 0.3592 0.2018 -0.0138 -0.0029 0.0111 316 MET A CA 2417 C C . MET A 316 ? 0.2653 0.3670 0.2038 -0.0201 -0.0036 0.0069 316 MET A C 2418 O O . MET A 316 ? 0.2658 0.3748 0.2057 -0.0206 -0.0064 0.0037 316 MET A O 2419 C CB . MET A 316 ? 0.2605 0.3428 0.1884 -0.0114 -0.0048 0.0121 316 MET A CB 2420 C CG . MET A 316 ? 0.2602 0.3329 0.1855 -0.0173 -0.0050 0.0108 316 MET A CG 2421 S SD . MET A 316 ? 0.2900 0.3556 0.2098 -0.0137 -0.0070 0.0115 316 MET A SD 2422 C CE . MET A 316 ? 0.2199 0.2791 0.1370 -0.0072 -0.0050 0.0161 316 MET A CE 2423 N N . VAL A 317 ? 0.2674 0.3713 0.2094 -0.0254 -0.0008 0.0063 317 VAL A N 2424 C CA . VAL A 317 ? 0.2742 0.3915 0.2237 -0.0320 -0.0003 0.0018 317 VAL A CA 2425 C C . VAL A 317 ? 0.2835 0.3984 0.2339 -0.0384 -0.0017 -0.0026 317 VAL A C 2426 O O . VAL A 317 ? 0.2841 0.4138 0.2392 -0.0390 -0.0045 -0.0077 317 VAL A O 2427 C CB . VAL A 317 ? 0.2759 0.3955 0.2288 -0.0369 0.0042 0.0027 317 VAL A CB 2428 C CG1 . VAL A 317 ? 0.2803 0.4150 0.2424 -0.0445 0.0053 -0.0024 317 VAL A CG1 2429 C CG2 . VAL A 317 ? 0.2670 0.3921 0.2198 -0.0298 0.0051 0.0051 317 VAL A CG2 2430 N N . PRO A 318 ? 0.2902 0.3875 0.2358 -0.0425 0.0001 -0.0010 318 PRO A N 2431 C CA . PRO A 318 ? 0.2964 0.3786 0.2364 -0.0420 0.0033 0.0046 318 PRO A CA 2432 C C . PRO A 318 ? 0.3090 0.3872 0.2513 -0.0498 0.0084 0.0055 318 PRO A C 2433 O O . PRO A 318 ? 0.3166 0.3852 0.2538 -0.0489 0.0113 0.0106 318 PRO A O 2434 C CB . PRO A 318 ? 0.2884 0.3561 0.2220 -0.0404 0.0018 0.0055 318 PRO A CB 2435 C CG . PRO A 318 ? 0.2895 0.3607 0.2269 -0.0456 0.0006 -0.0006 318 PRO A CG 2436 C CD . PRO A 318 ? 0.2863 0.3783 0.2313 -0.0465 -0.0012 -0.0053 318 PRO A CD 2437 N N . ASN A 319 ? 0.3178 0.4039 0.2674 -0.0574 0.0099 0.0005 319 ASN A N 2438 C CA . ASN A 319 ? 0.3359 0.4150 0.2878 -0.0661 0.0160 0.0013 319 ASN A CA 2439 C C . ASN A 319 ? 0.3364 0.4302 0.2956 -0.0700 0.0193 0.0007 319 ASN A C 2440 O O . ASN A 319 ? 0.3490 0.4376 0.3057 -0.0713 0.0244 0.0061 319 ASN A O 2441 C CB . ASN A 319 ? 0.3362 0.4095 0.2919 -0.0741 0.0171 -0.0046 319 ASN A CB 2442 C CG . ASN A 319 ? 0.3567 0.4137 0.3048 -0.0703 0.0149 -0.0037 319 ASN A CG 2443 O OD1 . ASN A 319 ? 0.3817 0.4407 0.3317 -0.0719 0.0120 -0.0102 319 ASN A OD1 2444 N ND2 . ASN A 319 ? 0.3306 0.3734 0.2701 -0.0648 0.0160 0.0039 319 ASN A ND2 2445 N N . LYS A 320 ? 0.3301 0.4441 0.2980 -0.0713 0.0166 -0.0057 320 LYS A N 2446 C CA . LYS A 320 ? 0.3310 0.4621 0.3079 -0.0762 0.0200 -0.0078 320 LYS A CA 2447 C C . LYS A 320 ? 0.3205 0.4624 0.2961 -0.0672 0.0187 -0.0044 320 LYS A C 2448 O O . LYS A 320 ? 0.3113 0.4733 0.2934 -0.0638 0.0159 -0.0082 320 LYS A O 2449 C CB . LYS A 320 ? 0.3326 0.4822 0.3208 -0.0830 0.0182 -0.0176 320 LYS A CB 2450 C CG A LYS A 320 ? 0.3564 0.5257 0.3563 -0.0903 0.0223 -0.0213 320 LYS A CG 2451 C CG B LYS A 320 ? 0.3378 0.4778 0.3306 -0.0959 0.0232 -0.0219 320 LYS A CG 2452 C CD A LYS A 320 ? 0.3727 0.5293 0.3712 -0.0968 0.0309 -0.0154 320 LYS A CD 2453 C CD B LYS A 320 ? 0.3450 0.4652 0.3306 -0.0951 0.0212 -0.0224 320 LYS A CD 2454 C CE A LYS A 320 ? 0.3834 0.5592 0.3887 -0.0972 0.0342 -0.0149 320 LYS A CE 2455 C CE B LYS A 320 ? 0.3584 0.4628 0.3470 -0.1071 0.0279 -0.0253 320 LYS A CE 2456 N NZ A LYS A 320 ? 0.4092 0.6065 0.4297 -0.1082 0.0371 -0.0233 320 LYS A NZ 2457 N NZ B LYS A 320 ? 0.3616 0.4461 0.3424 -0.1047 0.0262 -0.0254 320 LYS A NZ 2458 N N . TYR A 321 ? 0.3173 0.4458 0.2843 -0.0629 0.0209 0.0024 321 TYR A N 2459 C CA . TYR A 321 ? 0.3118 0.4467 0.2764 -0.0547 0.0205 0.0051 321 TYR A CA 2460 C C . TYR A 321 ? 0.3137 0.4666 0.2863 -0.0576 0.0243 0.0034 321 TYR A C 2461 O O . TYR A 321 ? 0.3110 0.4760 0.2855 -0.0505 0.0230 0.0027 321 TYR A O 2462 C CB . TYR A 321 ? 0.3180 0.4366 0.2721 -0.0511 0.0224 0.0112 321 TYR A CB 2463 C CG . TYR A 321 ? 0.3191 0.4289 0.2706 -0.0581 0.0286 0.0153 321 TYR A CG 2464 C CD1 . TYR A 321 ? 0.3099 0.4281 0.2631 -0.0604 0.0340 0.0173 321 TYR A CD1 2465 C CD2 . TYR A 321 ? 0.3122 0.4052 0.2594 -0.0619 0.0297 0.0176 321 TYR A CD2 2466 C CE1 . TYR A 321 ? 0.3374 0.4472 0.2877 -0.0665 0.0407 0.0223 321 TYR A CE1 2467 C CE2 . TYR A 321 ? 0.3308 0.4140 0.2751 -0.0673 0.0362 0.0225 321 TYR A CE2 2468 C CZ . TYR A 321 ? 0.3531 0.4446 0.2987 -0.0697 0.0419 0.0253 321 TYR A CZ 2469 O OH . TYR A 321 ? 0.3723 0.4531 0.3142 -0.0747 0.0493 0.0314 321 TYR A OH 2470 N N . GLN A 322 ? 0.3215 0.4757 0.2990 -0.0678 0.0297 0.0029 322 GLN A N 2471 C CA . GLN A 322 ? 0.3477 0.5196 0.3332 -0.0714 0.0344 0.0017 322 GLN A CA 2472 C C . GLN A 322 ? 0.3293 0.5259 0.3257 -0.0693 0.0304 -0.0053 322 GLN A C 2473 O O . GLN A 322 ? 0.3224 0.5347 0.3221 -0.0634 0.0306 -0.0057 322 GLN A O 2474 C CB . GLN A 322 ? 0.3548 0.5219 0.3439 -0.0839 0.0421 0.0028 322 GLN A CB 2475 C CG . GLN A 322 ? 0.4107 0.5955 0.4075 -0.0882 0.0484 0.0025 322 GLN A CG 2476 C CD . GLN A 322 ? 0.4223 0.6032 0.4247 -0.1021 0.0571 0.0032 322 GLN A CD 2477 O OE1 . GLN A 322 ? 0.5002 0.6999 0.5156 -0.1102 0.0602 -0.0026 322 GLN A OE1 2478 N NE2 . GLN A 322 ? 0.4894 0.6459 0.4822 -0.1046 0.0617 0.0103 322 GLN A NE2 2479 N N . GLN A 323 ? 0.3262 0.5267 0.3276 -0.0733 0.0268 -0.0108 323 GLN A N 2480 C CA . GLN A 323 ? 0.3270 0.5526 0.3377 -0.0703 0.0219 -0.0177 323 GLN A CA 2481 C C . GLN A 323 ? 0.3011 0.5304 0.3067 -0.0553 0.0165 -0.0152 323 GLN A C 2482 O O . GLN A 323 ? 0.2983 0.5485 0.3100 -0.0492 0.0155 -0.0170 323 GLN A O 2483 C CB . GLN A 323 ? 0.3285 0.5554 0.3431 -0.0769 0.0186 -0.0243 323 GLN A CB 2484 C CG . GLN A 323 ? 0.3623 0.6163 0.3848 -0.0725 0.0124 -0.0314 323 GLN A CG 2485 C CD . GLN A 323 ? 0.3642 0.6197 0.3892 -0.0785 0.0087 -0.0388 323 GLN A CD 2486 O OE1 . GLN A 323 ? 0.4330 0.6693 0.4485 -0.0758 0.0061 -0.0367 323 GLN A OE1 2487 N NE2 . GLN A 323 ? 0.3908 0.6708 0.4288 -0.0867 0.0085 -0.0485 323 GLN A NE2 2488 N N . PHE A 324 ? 0.2844 0.4932 0.2791 -0.0495 0.0138 -0.0109 324 PHE A N 2489 C CA . PHE A 324 ? 0.2653 0.4730 0.2546 -0.0361 0.0103 -0.0079 324 PHE A CA 2490 C C . PHE A 324 ? 0.2573 0.4690 0.2465 -0.0302 0.0137 -0.0053 324 PHE A C 2491 O O . PHE A 324 ? 0.2467 0.4723 0.2391 -0.0210 0.0122 -0.0060 324 PHE A O 2492 C CB . PHE A 324 ? 0.2594 0.4431 0.2375 -0.0326 0.0083 -0.0037 324 PHE A CB 2493 C CG . PHE A 324 ? 0.2667 0.4465 0.2396 -0.0202 0.0064 -0.0004 324 PHE A CG 2494 C CD1 . PHE A 324 ? 0.2447 0.4361 0.2193 -0.0118 0.0024 -0.0012 324 PHE A CD1 2495 C CD2 . PHE A 324 ? 0.2443 0.4099 0.2109 -0.0168 0.0091 0.0032 324 PHE A CD2 2496 C CE1 . PHE A 324 ? 0.2504 0.4358 0.2203 -0.0003 0.0022 0.0026 324 PHE A CE1 2497 C CE2 . PHE A 324 ? 0.2420 0.4025 0.2049 -0.0065 0.0085 0.0054 324 PHE A CE2 2498 C CZ . PHE A 324 ? 0.2426 0.4115 0.2072 0.0017 0.0056 0.0056 324 PHE A CZ 2499 N N . ILE A 325 ? 0.2519 0.4516 0.2367 -0.0347 0.0184 -0.0022 325 ILE A N 2500 C CA . ILE A 325 ? 0.2504 0.4534 0.2340 -0.0294 0.0220 -0.0006 325 ILE A CA 2501 C C . ILE A 325 ? 0.2446 0.4730 0.2391 -0.0298 0.0241 -0.0041 325 ILE A C 2502 O O . ILE A 325 ? 0.2450 0.4832 0.2414 -0.0205 0.0241 -0.0047 325 ILE A O 2503 C CB . ILE A 325 ? 0.2578 0.4455 0.2336 -0.0337 0.0265 0.0033 325 ILE A CB 2504 C CG1 . ILE A 325 ? 0.2652 0.4313 0.2307 -0.0304 0.0239 0.0063 325 ILE A CG1 2505 C CG2 . ILE A 325 ? 0.2506 0.4463 0.2262 -0.0291 0.0305 0.0035 325 ILE A CG2 2506 C CD1 . ILE A 325 ? 0.2558 0.4080 0.2132 -0.0349 0.0273 0.0102 325 ILE A CD1 2507 N N . SER A 326 ? 0.2477 0.4869 0.2502 -0.0405 0.0261 -0.0070 326 SER A N 2508 C CA . SER A 326 ? 0.2520 0.5176 0.2663 -0.0426 0.0287 -0.0110 326 SER A CA 2509 C C . SER A 326 ? 0.2497 0.5358 0.2705 -0.0328 0.0233 -0.0147 326 SER A C 2510 O O . SER A 326 ? 0.2450 0.5481 0.2706 -0.0254 0.0245 -0.0157 326 SER A O 2511 C CB . SER A 326 ? 0.2524 0.5245 0.2750 -0.0576 0.0323 -0.0142 326 SER A CB 2512 O OG . SER A 326 ? 0.2847 0.5844 0.3200 -0.0606 0.0353 -0.0187 326 SER A OG 2513 N N . ILE A 327 ? 0.2513 0.5357 0.2712 -0.0318 0.0176 -0.0164 327 ILE A N 2514 C CA . ILE A 327 ? 0.2490 0.5539 0.2738 -0.0219 0.0121 -0.0192 327 ILE A CA 2515 C C . ILE A 327 ? 0.2501 0.5487 0.2682 -0.0059 0.0112 -0.0143 327 ILE A C 2516 O O . ILE A 327 ? 0.2517 0.5704 0.2755 0.0036 0.0107 -0.0153 327 ILE A O 2517 C CB . ILE A 327 ? 0.2542 0.5596 0.2786 -0.0248 0.0065 -0.0223 327 ILE A CB 2518 C CG1 . ILE A 327 ? 0.2688 0.5914 0.3048 -0.0392 0.0076 -0.0301 327 ILE A CG1 2519 C CG2 . ILE A 327 ? 0.2385 0.5592 0.2628 -0.0108 0.0007 -0.0223 327 ILE A CG2 2520 C CD1 . ILE A 327 ? 0.3106 0.6310 0.3462 -0.0450 0.0034 -0.0347 327 ILE A CD1 2521 N N . LEU A 328 ? 0.2445 0.5157 0.2512 -0.0031 0.0116 -0.0094 328 LEU A N 2522 C CA . LEU A 328 ? 0.2522 0.5134 0.2527 0.0104 0.0121 -0.0054 328 LEU A CA 2523 C C . LEU A 328 ? 0.2553 0.5244 0.2592 0.0143 0.0171 -0.0060 328 LEU A C 2524 O O . LEU A 328 ? 0.2682 0.5459 0.2739 0.0266 0.0173 -0.0054 328 LEU A O 2525 C CB . LEU A 328 ? 0.2505 0.4817 0.2396 0.0100 0.0123 -0.0014 328 LEU A CB 2526 C CG . LEU A 328 ? 0.2523 0.4696 0.2351 0.0223 0.0133 0.0021 328 LEU A CG 2527 C CD1 . LEU A 328 ? 0.2553 0.4860 0.2410 0.0351 0.0109 0.0034 328 LEU A CD1 2528 C CD2 . LEU A 328 ? 0.2558 0.4470 0.2290 0.0204 0.0127 0.0050 328 LEU A CD2 2529 N N . THR A 329 ? 0.2569 0.5231 0.2610 0.0045 0.0214 -0.0068 329 THR A N 2530 C CA . THR A 329 ? 0.2589 0.5354 0.2664 0.0069 0.0264 -0.0080 329 THR A CA 2531 C C . THR A 329 ? 0.2632 0.5706 0.2827 0.0121 0.0260 -0.0115 329 THR A C 2532 O O . THR A 329 ? 0.2750 0.5901 0.2961 0.0232 0.0279 -0.0118 329 THR A O 2533 C CB . THR A 329 ? 0.2616 0.5339 0.2678 -0.0055 0.0314 -0.0078 329 THR A CB 2534 O OG1 . THR A 329 ? 0.2562 0.5021 0.2510 -0.0081 0.0313 -0.0044 329 THR A OG1 2535 C CG2 . THR A 329 ? 0.2529 0.5365 0.2615 -0.0025 0.0369 -0.0090 329 THR A CG2 2536 N N . GLY A 330 ? 0.2641 0.5898 0.2923 0.0044 0.0236 -0.0148 330 GLY A N 2537 C CA . GLY A 330 ? 0.2628 0.6220 0.3037 0.0084 0.0226 -0.0192 330 GLY A CA 2538 C C . GLY A 330 ? 0.2709 0.6371 0.3108 0.0258 0.0185 -0.0175 330 GLY A C 2539 O O . GLY A 330 ? 0.2723 0.6575 0.3181 0.0358 0.0200 -0.0185 330 GLY A O 2540 N N . HIS A 331 ? 0.2688 0.6194 0.3009 0.0300 0.0140 -0.0144 331 HIS A N 2541 C CA . HIS A 331 ? 0.2752 0.6290 0.3044 0.0471 0.0108 -0.0110 331 HIS A CA 2542 C C . HIS A 331 ? 0.2804 0.6202 0.3046 0.0596 0.0154 -0.0072 331 HIS A C 2543 O O . HIS A 331 ? 0.2855 0.6382 0.3124 0.0744 0.0155 -0.0058 331 HIS A O 2544 C CB . HIS A 331 ? 0.2729 0.6097 0.2934 0.0479 0.0062 -0.0077 331 HIS A CB 2545 C CG . HIS A 331 ? 0.2689 0.6261 0.2951 0.0413 0.0007 -0.0122 331 HIS A CG 2546 N ND1 . HIS A 331 ? 0.2833 0.6260 0.3033 0.0345 -0.0026 -0.0120 331 HIS A ND1 2547 C CD2 . HIS A 331 ? 0.2723 0.6643 0.3102 0.0403 -0.0021 -0.0182 331 HIS A CD2 2548 C CE1 . HIS A 331 ? 0.2747 0.6414 0.3020 0.0294 -0.0070 -0.0179 331 HIS A CE1 2549 N NE2 . HIS A 331 ? 0.2819 0.6794 0.3204 0.0324 -0.0070 -0.0221 331 HIS A NE2 2550 N N . VAL A 332 ? 0.2823 0.5961 0.2990 0.0542 0.0194 -0.0060 332 VAL A N 2551 C CA . VAL A 332 ? 0.2838 0.5843 0.2964 0.0639 0.0244 -0.0046 332 VAL A CA 2552 C C . VAL A 332 ? 0.2917 0.6150 0.3131 0.0664 0.0284 -0.0084 332 VAL A C 2553 O O . VAL A 332 ? 0.2989 0.6264 0.3216 0.0805 0.0309 -0.0079 332 VAL A O 2554 C CB . VAL A 332 ? 0.2862 0.5560 0.2889 0.0569 0.0271 -0.0037 332 VAL A CB 2555 C CG1 . VAL A 332 ? 0.2745 0.5328 0.2740 0.0654 0.0327 -0.0045 332 VAL A CG1 2556 C CG2 . VAL A 332 ? 0.2713 0.5198 0.2660 0.0566 0.0236 0.0003 332 VAL A CG2 2557 N N . ASN A 333 ? 0.2911 0.6287 0.3185 0.0532 0.0296 -0.0120 333 ASN A N 2558 C CA . ASN A 333 ? 0.3017 0.6634 0.3382 0.0539 0.0339 -0.0158 333 ASN A CA 2559 C C . ASN A 333 ? 0.3068 0.6994 0.3538 0.0652 0.0317 -0.0174 333 ASN A C 2560 O O . ASN A 333 ? 0.3122 0.7199 0.3645 0.0740 0.0353 -0.0192 333 ASN A O 2561 C CB . ASN A 333 ? 0.2935 0.6645 0.3348 0.0365 0.0364 -0.0186 333 ASN A CB 2562 C CG . ASN A 333 ? 0.3066 0.6541 0.3382 0.0291 0.0410 -0.0171 333 ASN A CG 2563 O OD1 . ASN A 333 ? 0.3023 0.6325 0.3259 0.0370 0.0431 -0.0161 333 ASN A OD1 2564 N ND2 . ASN A 333 ? 0.2780 0.6253 0.3104 0.0140 0.0429 -0.0170 333 ASN A ND2 2565 N N . GLY A 334 ? 0.3086 0.7119 0.3584 0.0657 0.0255 -0.0170 334 GLY A N 2566 C CA . GLY A 334 ? 0.3190 0.7544 0.3782 0.0774 0.0223 -0.0184 334 GLY A CA 2567 C C . GLY A 334 ? 0.3293 0.7559 0.3819 0.0976 0.0206 -0.0127 334 GLY A C 2568 O O . GLY A 334 ? 0.3359 0.7884 0.3945 0.1096 0.0173 -0.0125 334 GLY A O 2569 N N . GLY A 335 ? 0.3329 0.7238 0.3735 0.1015 0.0231 -0.0079 335 GLY A N 2570 C CA . GLY A 335 ? 0.3420 0.7193 0.3758 0.1203 0.0236 -0.0017 335 GLY A CA 2571 C C . GLY A 335 ? 0.3479 0.7236 0.3767 0.1256 0.0178 0.0033 335 GLY A C 2572 O O . GLY A 335 ? 0.3606 0.7273 0.3838 0.1422 0.0185 0.0097 335 GLY A O 2573 N N . VAL A 336 ? 0.3323 0.7149 0.3624 0.1116 0.0126 0.0006 336 VAL A N 2574 C CA . VAL A 336 ? 0.3292 0.7140 0.3548 0.1150 0.0067 0.0039 336 VAL A CA 2575 C C . VAL A 336 ? 0.3287 0.6746 0.3408 0.1161 0.0082 0.0104 336 VAL A C 2576 O O . VAL A 336 ? 0.3288 0.6700 0.3344 0.1269 0.0060 0.0164 336 VAL A O 2577 C CB . VAL A 336 ? 0.3206 0.7262 0.3531 0.0988 0.0012 -0.0029 336 VAL A CB 2578 C CG1 . VAL A 336 ? 0.3318 0.7370 0.3583 0.1011 -0.0047 -0.0004 336 VAL A CG1 2579 C CG2 . VAL A 336 ? 0.3283 0.7762 0.3756 0.0986 -0.0003 -0.0097 336 VAL A CG2 2580 N N . ILE A 337 ? 0.3207 0.6406 0.3289 0.1050 0.0122 0.0090 337 ILE A N 2581 C CA . ILE A 337 ? 0.3171 0.6005 0.3141 0.1057 0.0151 0.0138 337 ILE A CA 2582 C C . ILE A 337 ? 0.3214 0.5879 0.3171 0.1105 0.0222 0.0134 337 ILE A C 2583 O O . ILE A 337 ? 0.3183 0.5893 0.3182 0.1021 0.0246 0.0081 337 ILE A O 2584 C CB . ILE A 337 ? 0.3047 0.5727 0.2977 0.0883 0.0131 0.0117 337 ILE A CB 2585 C CG1 . ILE A 337 ? 0.3053 0.5868 0.2986 0.0845 0.0065 0.0115 337 ILE A CG1 2586 C CG2 . ILE A 337 ? 0.2962 0.5287 0.2793 0.0879 0.0167 0.0152 337 ILE A CG2 2587 C CD1 . ILE A 337 ? 0.2926 0.5653 0.2846 0.0669 0.0045 0.0080 337 ILE A CD1 2588 N N . PRO A 338 ? 0.3282 0.5750 0.3180 0.1241 0.0263 0.0188 338 PRO A N 2589 C CA . PRO A 338 ? 0.3330 0.5652 0.3224 0.1292 0.0334 0.0169 338 PRO A CA 2590 C C . PRO A 338 ? 0.3393 0.5445 0.3233 0.1164 0.0364 0.0135 338 PRO A C 2591 O O . PRO A 338 ? 0.3240 0.5149 0.3026 0.1076 0.0338 0.0151 338 PRO A O 2592 C CB . PRO A 338 ? 0.3469 0.5654 0.3319 0.1474 0.0372 0.0242 338 PRO A CB 2593 C CG . PRO A 338 ? 0.3443 0.5545 0.3228 0.1464 0.0332 0.0303 338 PRO A CG 2594 C CD . PRO A 338 ? 0.3333 0.5694 0.3162 0.1349 0.0253 0.0268 338 PRO A CD 2595 N N . MET A 339 ? 0.3425 0.5431 0.3280 0.1158 0.0416 0.0083 339 MET A N 2596 C CA . MET A 339 ? 0.3529 0.5308 0.3333 0.1057 0.0446 0.0041 339 MET A CA 2597 C C . MET A 339 ? 0.3545 0.5024 0.3279 0.1079 0.0471 0.0074 339 MET A C 2598 O O . MET A 339 ? 0.3478 0.4807 0.3167 0.0967 0.0464 0.0055 339 MET A O 2599 C CB . MET A 339 ? 0.3674 0.5462 0.3501 0.1079 0.0504 -0.0023 339 MET A CB 2600 C CG . MET A 339 ? 0.3926 0.5874 0.3777 0.0954 0.0491 -0.0074 339 MET A CG 2601 S SD . MET A 339 ? 0.4529 0.6330 0.4310 0.0779 0.0460 -0.0084 339 MET A SD 2602 C CE . MET A 339 ? 0.3983 0.6074 0.3825 0.0682 0.0426 -0.0088 339 MET A CE 2603 N N . SER A 340 ? 0.3642 0.5035 0.3366 0.1225 0.0505 0.0125 340 SER A N 2604 C CA . SER A 340 ? 0.3737 0.4834 0.3399 0.1248 0.0542 0.0165 340 SER A CA 2605 C C . SER A 340 ? 0.3648 0.4709 0.3267 0.1155 0.0487 0.0203 340 SER A C 2606 O O . SER A 340 ? 0.3677 0.4512 0.3251 0.1092 0.0509 0.0200 340 SER A O 2607 C CB . SER A 340 ? 0.3914 0.4939 0.3568 0.1434 0.0591 0.0236 340 SER A CB 2608 O OG . SER A 340 ? 0.3822 0.5040 0.3478 0.1510 0.0537 0.0311 340 SER A OG 2609 N N . ARG A 341 ? 0.3522 0.4817 0.3162 0.1141 0.0418 0.0228 341 ARG A N 2610 C CA . ARG A 341 ? 0.3405 0.4685 0.3007 0.1058 0.0364 0.0257 341 ARG A CA 2611 C C . ARG A 341 ? 0.3267 0.4495 0.2860 0.0891 0.0345 0.0197 341 ARG A C 2612 O O . ARG A 341 ? 0.3282 0.4337 0.2827 0.0826 0.0345 0.0205 341 ARG A O 2613 C CB . ARG A 341 ? 0.3326 0.4881 0.2957 0.1092 0.0299 0.0285 341 ARG A CB 2614 C CG . ARG A 341 ? 0.3190 0.4748 0.2782 0.1016 0.0243 0.0307 341 ARG A CG 2615 C CD . ARG A 341 ? 0.3348 0.4714 0.2864 0.1090 0.0264 0.0384 341 ARG A CD 2616 N NE . ARG A 341 ? 0.3244 0.4331 0.2715 0.1007 0.0302 0.0374 341 ARG A NE 2617 C CZ . ARG A 341 ? 0.2968 0.4006 0.2419 0.0876 0.0269 0.0347 341 ARG A CZ 2618 N NH1 . ARG A 341 ? 0.2882 0.3690 0.2300 0.0815 0.0306 0.0335 341 ARG A NH1 2619 N NH2 . ARG A 341 ? 0.2840 0.4059 0.2308 0.0806 0.0204 0.0325 341 ARG A NH2 2620 N N . ILE A 342 ? 0.3189 0.4572 0.2829 0.0829 0.0336 0.0142 342 ILE A N 2621 C CA . ILE A 342 ? 0.3054 0.4393 0.2678 0.0689 0.0328 0.0093 342 ILE A CA 2622 C C . ILE A 342 ? 0.3116 0.4214 0.2695 0.0667 0.0374 0.0064 342 ILE A C 2623 O O . ILE A 342 ? 0.3125 0.4121 0.2665 0.0573 0.0358 0.0054 342 ILE A O 2624 C CB . ILE A 342 ? 0.2949 0.4489 0.2626 0.0644 0.0328 0.0046 342 ILE A CB 2625 C CG1 . ILE A 342 ? 0.2879 0.4674 0.2616 0.0640 0.0283 0.0059 342 ILE A CG1 2626 C CG2 . ILE A 342 ? 0.2839 0.4323 0.2483 0.0517 0.0328 0.0009 342 ILE A CG2 2627 C CD1 . ILE A 342 ? 0.2736 0.4533 0.2454 0.0551 0.0229 0.0078 342 ILE A CD1 2628 N N . ASP A 343 ? 0.3255 0.4272 0.2844 0.0753 0.0433 0.0044 343 ASP A N 2629 C CA . ASP A 343 ? 0.3302 0.4103 0.2863 0.0732 0.0486 -0.0005 343 ASP A CA 2630 C C . ASP A 343 ? 0.3406 0.3991 0.2927 0.0724 0.0497 0.0032 343 ASP A C 2631 O O . ASP A 343 ? 0.3391 0.3836 0.2890 0.0647 0.0514 -0.0013 343 ASP A O 2632 C CB . ASP A 343 ? 0.3402 0.4158 0.2989 0.0834 0.0553 -0.0039 343 ASP A CB 2633 C CG . ASP A 343 ? 0.3436 0.4371 0.3054 0.0818 0.0558 -0.0102 343 ASP A CG 2634 O OD1 . ASP A 343 ? 0.3268 0.4346 0.2884 0.0723 0.0514 -0.0114 343 ASP A OD1 2635 O OD2 . ASP A 343 ? 0.3530 0.4455 0.3172 0.0905 0.0612 -0.0136 343 ASP A OD2 2636 N N . ASP A 344 ? 0.3415 0.3991 0.2929 0.0805 0.0490 0.0112 344 ASP A N 2637 C CA . ASP A 344 ? 0.3500 0.3891 0.2974 0.0800 0.0503 0.0159 344 ASP A CA 2638 C C . ASP A 344 ? 0.3357 0.3774 0.2805 0.0676 0.0445 0.0153 344 ASP A C 2639 O O . ASP A 344 ? 0.3420 0.3680 0.2846 0.0611 0.0463 0.0135 344 ASP A O 2640 C CB . ASP A 344 ? 0.3547 0.3949 0.3007 0.0929 0.0509 0.0255 344 ASP A CB 2641 C CG . ASP A 344 ? 0.3591 0.3833 0.3002 0.0920 0.0519 0.0316 344 ASP A CG 2642 O OD1 . ASP A 344 ? 0.3798 0.3805 0.3197 0.0919 0.0589 0.0313 344 ASP A OD1 2643 O OD2 . ASP A 344 ? 0.3404 0.3760 0.2792 0.0912 0.0461 0.0362 344 ASP A OD2 2644 N N . ALA A 345 ? 0.3246 0.3863 0.2704 0.0643 0.0380 0.0163 345 ALA A N 2645 C CA . ALA A 345 ? 0.3071 0.3715 0.2507 0.0536 0.0327 0.0160 345 ALA A CA 2646 C C . ALA A 345 ? 0.3048 0.3624 0.2473 0.0437 0.0335 0.0095 345 ALA A C 2647 O O . ALA A 345 ? 0.2968 0.3445 0.2364 0.0375 0.0327 0.0092 345 ALA A O 2648 C CB . ALA A 345 ? 0.2951 0.3816 0.2411 0.0513 0.0269 0.0167 345 ALA A CB 2649 N N . VAL A 346 ? 0.3023 0.3672 0.2470 0.0431 0.0352 0.0044 346 VAL A N 2650 C CA . VAL A 346 ? 0.2994 0.3615 0.2425 0.0352 0.0361 -0.0021 346 VAL A CA 2651 C C . VAL A 346 ? 0.3101 0.3535 0.2523 0.0350 0.0410 -0.0063 346 VAL A C 2652 O O . VAL A 346 ? 0.3122 0.3510 0.2522 0.0275 0.0401 -0.0101 346 VAL A O 2653 C CB . VAL A 346 ? 0.2961 0.3726 0.2412 0.0351 0.0372 -0.0065 346 VAL A CB 2654 C CG1 . VAL A 346 ? 0.2952 0.3703 0.2371 0.0279 0.0379 -0.0129 346 VAL A CG1 2655 C CG2 . VAL A 346 ? 0.2708 0.3657 0.2179 0.0330 0.0331 -0.0030 346 VAL A CG2 2656 N N . THR A 347 ? 0.3179 0.3505 0.2620 0.0433 0.0464 -0.0057 347 THR A N 2657 C CA . THR A 347 ? 0.3296 0.3420 0.2739 0.0422 0.0522 -0.0098 347 THR A CA 2658 C C . THR A 347 ? 0.3238 0.3269 0.2659 0.0361 0.0505 -0.0069 347 THR A C 2659 O O . THR A 347 ? 0.3288 0.3245 0.2710 0.0289 0.0519 -0.0129 347 THR A O 2660 C CB . THR A 347 ? 0.3414 0.3406 0.2877 0.0532 0.0593 -0.0073 347 THR A CB 2661 O OG1 . THR A 347 ? 0.3458 0.3524 0.2946 0.0582 0.0618 -0.0123 347 THR A OG1 2662 C CG2 . THR A 347 ? 0.3615 0.3370 0.3085 0.0510 0.0664 -0.0108 347 THR A CG2 2663 N N . ARG A 348 ? 0.3224 0.3284 0.2628 0.0392 0.0472 0.0017 348 ARG A N 2664 C CA . ARG A 348 ? 0.3194 0.3171 0.2576 0.0350 0.0461 0.0054 348 ARG A CA 2665 C C . ARG A 348 ? 0.3151 0.3208 0.2516 0.0250 0.0405 0.0021 348 ARG A C 2666 O O . ARG A 348 ? 0.3159 0.3135 0.2520 0.0193 0.0413 0.0003 348 ARG A O 2667 C CB . ARG A 348 ? 0.3206 0.3215 0.2566 0.0421 0.0440 0.0150 348 ARG A CB 2668 C CG . ARG A 348 ? 0.3202 0.3107 0.2566 0.0535 0.0503 0.0200 348 ARG A CG 2669 C CD . ARG A 348 ? 0.3425 0.3436 0.2765 0.0622 0.0470 0.0289 348 ARG A CD 2670 N NE . ARG A 348 ? 0.3529 0.3424 0.2860 0.0744 0.0537 0.0352 348 ARG A NE 2671 C CZ . ARG A 348 ? 0.3480 0.3204 0.2780 0.0772 0.0589 0.0413 348 ARG A CZ 2672 N NH1 . ARG A 348 ? 0.3348 0.3020 0.2629 0.0684 0.0576 0.0411 348 ARG A NH1 2673 N NH2 . ARG A 348 ? 0.3721 0.3326 0.3008 0.0893 0.0660 0.0480 348 ARG A NH2 2674 N N . ILE A 349 ? 0.3003 0.3217 0.2361 0.0231 0.0356 0.0015 349 ILE A N 2675 C CA . ILE A 349 ? 0.2948 0.3236 0.2284 0.0151 0.0308 -0.0005 349 ILE A CA 2676 C C . ILE A 349 ? 0.3023 0.3287 0.2359 0.0099 0.0328 -0.0086 349 ILE A C 2677 O O . ILE A 349 ? 0.3036 0.3281 0.2359 0.0043 0.0312 -0.0105 349 ILE A O 2678 C CB . ILE A 349 ? 0.2907 0.3355 0.2240 0.0144 0.0266 0.0015 349 ILE A CB 2679 C CG1 . ILE A 349 ? 0.2801 0.3297 0.2138 0.0183 0.0239 0.0079 349 ILE A CG1 2680 C CG2 . ILE A 349 ? 0.2727 0.3228 0.2028 0.0070 0.0231 0.0000 349 ILE A CG2 2681 C CD1 . ILE A 349 ? 0.2746 0.3405 0.2101 0.0174 0.0209 0.0088 349 ILE A CD1 2682 N N . LEU A 350 ? 0.3057 0.3340 0.2410 0.0120 0.0361 -0.0139 350 LEU A N 2683 C CA . LEU A 350 ? 0.3089 0.3361 0.2445 0.0078 0.0385 -0.0232 350 LEU A CA 2684 C C . LEU A 350 ? 0.3155 0.3275 0.2537 0.0054 0.0427 -0.0271 350 LEU A C 2685 O O . LEU A 350 ? 0.3204 0.3339 0.2586 -0.0010 0.0420 -0.0335 350 LEU A O 2686 C CB . LEU A 350 ? 0.3146 0.3460 0.2516 0.0117 0.0420 -0.0285 350 LEU A CB 2687 C CG . LEU A 350 ? 0.3054 0.3536 0.2405 0.0129 0.0390 -0.0263 350 LEU A CG 2688 C CD1 . LEU A 350 ? 0.2773 0.3286 0.2143 0.0172 0.0437 -0.0326 350 LEU A CD1 2689 C CD2 . LEU A 350 ? 0.2691 0.3280 0.1996 0.0065 0.0346 -0.0269 350 LEU A CD2 2690 N N . ARG A 351 ? 0.3205 0.3186 0.2611 0.0105 0.0475 -0.0234 351 ARG A N 2691 C CA . ARG A 351 ? 0.3343 0.3161 0.2778 0.0075 0.0528 -0.0259 351 ARG A CA 2692 C C . ARG A 351 ? 0.3277 0.3125 0.2702 0.0005 0.0488 -0.0250 351 ARG A C 2693 O O . ARG A 351 ? 0.3405 0.3232 0.2855 -0.0063 0.0505 -0.0328 351 ARG A O 2694 C CB . ARG A 351 ? 0.3397 0.3060 0.2842 0.0151 0.0584 -0.0183 351 ARG A CB 2695 C CG . ARG A 351 ? 0.3635 0.3107 0.3115 0.0116 0.0659 -0.0210 351 ARG A CG 2696 C CD . ARG A 351 ? 0.3822 0.3126 0.3300 0.0204 0.0726 -0.0121 351 ARG A CD 2697 N NE . ARG A 351 ? 0.3903 0.3146 0.3395 0.0282 0.0778 -0.0138 351 ARG A NE 2698 C CZ . ARG A 351 ? 0.4043 0.3324 0.3512 0.0395 0.0771 -0.0057 351 ARG A CZ 2699 N NH1 . ARG A 351 ? 0.3950 0.3331 0.3380 0.0437 0.0714 0.0044 351 ARG A NH1 2700 N NH2 . ARG A 351 ? 0.4101 0.3328 0.3588 0.0469 0.0822 -0.0082 351 ARG A NH2 2701 N N . VAL A 352 ? 0.3150 0.3061 0.2540 0.0022 0.0435 -0.0164 352 VAL A N 2702 C CA . VAL A 352 ? 0.3100 0.3041 0.2477 -0.0031 0.0398 -0.0149 352 VAL A CA 2703 C C . VAL A 352 ? 0.3065 0.3128 0.2433 -0.0091 0.0358 -0.0221 352 VAL A C 2704 O O . VAL A 352 ? 0.3099 0.3163 0.2486 -0.0146 0.0361 -0.0269 352 VAL A O 2705 C CB . VAL A 352 ? 0.3008 0.2990 0.2347 0.0004 0.0351 -0.0052 352 VAL A CB 2706 C CG1 . VAL A 352 ? 0.2871 0.2897 0.2193 -0.0046 0.0309 -0.0044 352 VAL A CG1 2707 C CG2 . VAL A 352 ? 0.2918 0.2791 0.2260 0.0066 0.0392 0.0018 352 VAL A CG2 2708 N N . LYS A 353 ? 0.3090 0.3268 0.2430 -0.0078 0.0326 -0.0227 353 LYS A N 2709 C CA . LYS A 353 ? 0.3022 0.3330 0.2334 -0.0117 0.0289 -0.0278 353 LYS A CA 2710 C C . LYS A 353 ? 0.3116 0.3436 0.2459 -0.0158 0.0319 -0.0393 353 LYS A C 2711 O O . LYS A 353 ? 0.3091 0.3491 0.2429 -0.0201 0.0293 -0.0438 353 LYS A O 2712 C CB . LYS A 353 ? 0.2945 0.3360 0.2220 -0.0090 0.0266 -0.0254 353 LYS A CB 2713 C CG . LYS A 353 ? 0.2739 0.3182 0.1987 -0.0073 0.0227 -0.0160 353 LYS A CG 2714 C CD . LYS A 353 ? 0.2551 0.3103 0.1770 -0.0063 0.0215 -0.0145 353 LYS A CD 2715 C CE . LYS A 353 ? 0.2593 0.3172 0.1793 -0.0064 0.0183 -0.0067 353 LYS A CE 2716 N NZ . LYS A 353 ? 0.2498 0.3180 0.1674 -0.0068 0.0181 -0.0050 353 LYS A NZ 2717 N N . PHE A 354 ? 0.3139 0.3388 0.2515 -0.0142 0.0373 -0.0446 354 PHE A N 2718 C CA . PHE A 354 ? 0.3236 0.3479 0.2651 -0.0188 0.0412 -0.0574 354 PHE A CA 2719 C C . PHE A 354 ? 0.3260 0.3411 0.2729 -0.0244 0.0441 -0.0606 354 PHE A C 2720 O O . PHE A 354 ? 0.3311 0.3538 0.2805 -0.0305 0.0437 -0.0704 354 PHE A O 2721 C CB . PHE A 354 ? 0.3261 0.3412 0.2705 -0.0154 0.0476 -0.0624 354 PHE A CB 2722 C CG . PHE A 354 ? 0.3279 0.3557 0.2683 -0.0120 0.0460 -0.0650 354 PHE A CG 2723 C CD1 . PHE A 354 ? 0.3083 0.3342 0.2477 -0.0049 0.0471 -0.0584 354 PHE A CD1 2724 C CD2 . PHE A 354 ? 0.3197 0.3633 0.2576 -0.0155 0.0435 -0.0740 354 PHE A CD2 2725 C CE1 . PHE A 354 ? 0.3047 0.3433 0.2411 -0.0021 0.0463 -0.0606 354 PHE A CE1 2726 C CE2 . PHE A 354 ? 0.3201 0.3761 0.2536 -0.0121 0.0426 -0.0757 354 PHE A CE2 2727 C CZ . PHE A 354 ? 0.3031 0.3560 0.2363 -0.0058 0.0444 -0.0690 354 PHE A CZ 2728 N N . THR A 355 ? 0.3274 0.3275 0.2759 -0.0221 0.0472 -0.0525 355 THR A N 2729 C CA . THR A 355 ? 0.3302 0.3194 0.2842 -0.0273 0.0518 -0.0543 355 THR A CA 2730 C C . THR A 355 ? 0.3238 0.3262 0.2775 -0.0325 0.0463 -0.0555 355 THR A C 2731 O O . THR A 355 ? 0.3266 0.3304 0.2860 -0.0396 0.0487 -0.0640 355 THR A O 2732 C CB . THR A 355 ? 0.3329 0.3052 0.2866 -0.0221 0.0559 -0.0428 355 THR A CB 2733 O OG1 . THR A 355 ? 0.3380 0.2975 0.2927 -0.0165 0.0620 -0.0424 355 THR A OG1 2734 C CG2 . THR A 355 ? 0.3253 0.2871 0.2838 -0.0276 0.0609 -0.0431 355 THR A CG2 2735 N N . MET A 356 ? 0.3150 0.3276 0.2626 -0.0290 0.0393 -0.0473 356 MET A N 2736 C CA . MET A 356 ? 0.3113 0.3345 0.2579 -0.0319 0.0343 -0.0462 356 MET A CA 2737 C C . MET A 356 ? 0.2940 0.3358 0.2397 -0.0349 0.0300 -0.0550 356 MET A C 2738 O O . MET A 356 ? 0.3032 0.3559 0.2483 -0.0365 0.0260 -0.0550 356 MET A O 2739 C CB . MET A 356 ? 0.3034 0.3278 0.2438 -0.0269 0.0294 -0.0344 356 MET A CB 2740 C CG . MET A 356 ? 0.3151 0.3486 0.2496 -0.0230 0.0249 -0.0315 356 MET A CG 2741 S SD . MET A 356 ? 0.3167 0.3489 0.2459 -0.0184 0.0207 -0.0192 356 MET A SD 2742 C CE . MET A 356 ? 0.4186 0.4352 0.3508 -0.0158 0.0256 -0.0142 356 MET A CE 2743 N N . GLY A 357 ? 0.2843 0.3309 0.2294 -0.0347 0.0310 -0.0621 357 GLY A N 2744 C CA . GLY A 357 ? 0.2552 0.3214 0.1980 -0.0365 0.0270 -0.0705 357 GLY A CA 2745 C C . GLY A 357 ? 0.2281 0.3065 0.1617 -0.0310 0.0211 -0.0636 357 GLY A C 2746 O O . GLY A 357 ? 0.2267 0.3230 0.1569 -0.0310 0.0174 -0.0684 357 GLY A O 2875 N N . LYS A 374 ? 0.2808 0.4596 0.1369 0.0384 -0.0087 -0.0562 374 LYS A N 2876 C CA . LYS A 374 ? 0.3128 0.5114 0.1734 0.0376 -0.0132 -0.0707 374 LYS A CA 2877 C C . LYS A 374 ? 0.3054 0.4952 0.1775 0.0317 -0.0139 -0.0720 374 LYS A C 2878 O O . LYS A 374 ? 0.2970 0.4665 0.1765 0.0251 -0.0100 -0.0697 374 LYS A O 2879 C CB . LYS A 374 ? 0.3203 0.5246 0.1866 0.0321 -0.0115 -0.0870 374 LYS A CB 2880 C CG . LYS A 374 ? 0.3690 0.6009 0.2352 0.0337 -0.0159 -0.1029 374 LYS A CG 2881 C CD . LYS A 374 ? 0.4157 0.6460 0.2929 0.0250 -0.0128 -0.1209 374 LYS A CD 2882 C CE . LYS A 374 ? 0.5010 0.7602 0.3758 0.0272 -0.0165 -0.1382 374 LYS A CE 2883 N NZ . LYS A 374 ? 0.5584 0.8455 0.4268 0.0349 -0.0241 -0.1387 374 LYS A NZ 2884 N N . GLN A 375 ? 0.3162 0.5227 0.1896 0.0347 -0.0187 -0.0756 375 GLN A N 2885 C CA . GLN A 375 ? 0.3162 0.5171 0.2004 0.0298 -0.0191 -0.0767 375 GLN A CA 2886 C C . GLN A 375 ? 0.3133 0.5036 0.2118 0.0179 -0.0150 -0.0877 375 GLN A C 2887 O O . GLN A 375 ? 0.3142 0.4882 0.2188 0.0134 -0.0122 -0.0828 375 GLN A O 2888 C CB . GLN A 375 ? 0.3229 0.5480 0.2073 0.0355 -0.0251 -0.0810 375 GLN A CB 2889 C CG . GLN A 375 ? 0.3220 0.5417 0.2154 0.0329 -0.0253 -0.0787 375 GLN A CG 2890 C CD . GLN A 375 ? 0.3479 0.5434 0.2364 0.0351 -0.0226 -0.0619 375 GLN A CD 2891 O OE1 . GLN A 375 ? 0.3660 0.5581 0.2431 0.0435 -0.0232 -0.0499 375 GLN A OE1 2892 N NE2 . GLN A 375 ? 0.3344 0.5139 0.2319 0.0275 -0.0192 -0.0614 375 GLN A NE2 2893 N N . GLU A 376 ? 0.3193 0.5183 0.2227 0.0134 -0.0140 -0.1023 376 GLU A N 2894 C CA . GLU A 376 ? 0.3197 0.5048 0.2362 0.0025 -0.0083 -0.1117 376 GLU A CA 2895 C C . GLU A 376 ? 0.3112 0.4674 0.2262 0.0007 -0.0028 -0.0999 376 GLU A C 2896 O O . GLU A 376 ? 0.3119 0.4517 0.2353 -0.0057 0.0016 -0.0990 376 GLU A O 2897 C CB . GLU A 376 ? 0.3263 0.5230 0.2467 -0.0010 -0.0074 -0.1289 376 GLU A CB 2898 C CG . GLU A 376 ? 0.3657 0.5925 0.2921 -0.0021 -0.0123 -0.1455 376 GLU A CG 2899 C CD . GLU A 376 ? 0.3913 0.6446 0.3039 0.0096 -0.0198 -0.1437 376 GLU A CD 2900 O OE1 . GLU A 376 ? 0.3782 0.6253 0.2763 0.0185 -0.0206 -0.1280 376 GLU A OE1 2901 O OE2 . GLU A 376 ? 0.4266 0.7081 0.3431 0.0101 -0.0246 -0.1583 376 GLU A OE2 2902 N N . HIS A 377 ? 0.3108 0.4623 0.2152 0.0068 -0.0029 -0.0908 377 HIS A N 2903 C CA . HIS A 377 ? 0.3026 0.4310 0.2059 0.0061 0.0014 -0.0801 377 HIS A CA 2904 C C . HIS A 377 ? 0.2960 0.4132 0.1984 0.0070 0.0008 -0.0674 377 HIS A C 2905 O O . HIS A 377 ? 0.2973 0.3966 0.2031 0.0041 0.0042 -0.0621 377 HIS A O 2906 C CB . HIS A 377 ? 0.2973 0.4264 0.1908 0.0120 0.0017 -0.0739 377 HIS A CB 2907 C CG . HIS A 377 ? 0.3114 0.4518 0.2040 0.0123 0.0025 -0.0860 377 HIS A CG 2908 N ND1 . HIS A 377 ? 0.3366 0.4828 0.2383 0.0066 0.0036 -0.1024 377 HIS A ND1 2909 C CD2 . HIS A 377 ? 0.2928 0.4403 0.1768 0.0175 0.0030 -0.0847 377 HIS A CD2 2910 C CE1 . HIS A 377 ? 0.3115 0.4680 0.2098 0.0085 0.0041 -0.1114 377 HIS A CE1 2911 N NE2 . HIS A 377 ? 0.3362 0.4943 0.2233 0.0155 0.0038 -0.1006 377 HIS A NE2 2912 N N . ARG A 378 ? 0.2954 0.4237 0.1926 0.0120 -0.0036 -0.0625 378 ARG A N 2913 C CA . ARG A 378 ? 0.2927 0.4123 0.1895 0.0131 -0.0043 -0.0526 378 ARG A CA 2914 C C . ARG A 378 ? 0.2958 0.4120 0.2029 0.0066 -0.0027 -0.0582 378 ARG A C 2915 O O . ARG A 378 ? 0.2914 0.3929 0.2002 0.0046 -0.0005 -0.0515 378 ARG A O 2916 C CB . ARG A 378 ? 0.2979 0.4303 0.1873 0.0209 -0.0088 -0.0471 378 ARG A CB 2917 C CG . ARG A 378 ? 0.2978 0.4290 0.1764 0.0273 -0.0087 -0.0376 378 ARG A CG 2918 C CD . ARG A 378 ? 0.3053 0.4423 0.1763 0.0356 -0.0115 -0.0286 378 ARG A CD 2919 N NE . ARG A 378 ? 0.3067 0.4447 0.1672 0.0415 -0.0102 -0.0205 378 ARG A NE 2920 C CZ . ARG A 378 ? 0.2949 0.4173 0.1530 0.0410 -0.0064 -0.0106 378 ARG A CZ 2921 N NH1 . ARG A 378 ? 0.2964 0.4024 0.1611 0.0356 -0.0046 -0.0079 378 ARG A NH1 2922 N NH2 . ARG A 378 ? 0.2801 0.4050 0.1291 0.0459 -0.0042 -0.0036 378 ARG A NH2 2923 N N . ASP A 379 ? 0.2935 0.4246 0.2076 0.0032 -0.0035 -0.0708 379 ASP A N 2924 C CA . ASP A 379 ? 0.2925 0.4204 0.2182 -0.0046 -0.0002 -0.0774 379 ASP A CA 2925 C C . ASP A 379 ? 0.2914 0.3967 0.2211 -0.0105 0.0065 -0.0755 379 ASP A C 2926 O O . ASP A 379 ? 0.2961 0.3903 0.2298 -0.0140 0.0100 -0.0716 379 ASP A O 2927 C CB . ASP A 379 ? 0.2900 0.4382 0.2246 -0.0088 -0.0013 -0.0936 379 ASP A CB 2928 C CG . ASP A 379 ? 0.3277 0.5010 0.2591 -0.0019 -0.0083 -0.0954 379 ASP A CG 2929 O OD1 . ASP A 379 ? 0.3407 0.5127 0.2648 0.0052 -0.0112 -0.0838 379 ASP A OD1 2930 O OD2 . ASP A 379 ? 0.3630 0.5580 0.2995 -0.0032 -0.0110 -0.1091 379 ASP A OD2 2931 N N . LEU A 380 ? 0.2972 0.3966 0.2252 -0.0105 0.0086 -0.0779 380 LEU A N 2932 C CA . LEU A 380 ? 0.2947 0.3730 0.2253 -0.0136 0.0147 -0.0752 380 LEU A CA 2933 C C . LEU A 380 ? 0.2914 0.3555 0.2155 -0.0096 0.0147 -0.0606 380 LEU A C 2934 O O . LEU A 380 ? 0.2973 0.3470 0.2242 -0.0122 0.0190 -0.0563 380 LEU A O 2935 C CB . LEU A 380 ? 0.3043 0.3818 0.2338 -0.0127 0.0162 -0.0813 380 LEU A CB 2936 C CG . LEU A 380 ? 0.3088 0.3653 0.2407 -0.0138 0.0226 -0.0789 380 LEU A CG 2937 C CD1 . LEU A 380 ? 0.3109 0.3557 0.2536 -0.0215 0.0295 -0.0853 380 LEU A CD1 2938 C CD2 . LEU A 380 ? 0.3061 0.3664 0.2361 -0.0113 0.0229 -0.0854 380 LEU A CD2 2939 N N . ALA A 381 ? 0.2773 0.3461 0.1929 -0.0035 0.0104 -0.0533 381 ALA A N 2940 C CA . ALA A 381 ? 0.2793 0.3374 0.1899 -0.0002 0.0098 -0.0412 381 ALA A CA 2941 C C . ALA A 381 ? 0.2785 0.3342 0.1906 -0.0016 0.0095 -0.0376 381 ALA A C 2942 O O . ALA A 381 ? 0.2819 0.3260 0.1931 -0.0016 0.0113 -0.0311 381 ALA A O 2943 C CB . ALA A 381 ? 0.2684 0.3331 0.1713 0.0054 0.0061 -0.0352 381 ALA A CB 2944 N N . ARG A 382 ? 0.2816 0.3501 0.1959 -0.0021 0.0071 -0.0423 382 ARG A N 2945 C CA . ARG A 382 ? 0.2869 0.3557 0.2038 -0.0035 0.0073 -0.0406 382 ARG A CA 2946 C C . ARG A 382 ? 0.2955 0.3542 0.2191 -0.0098 0.0134 -0.0430 382 ARG A C 2947 O O . ARG A 382 ? 0.2970 0.3475 0.2194 -0.0099 0.0153 -0.0369 382 ARG A O 2948 C CB . ARG A 382 ? 0.2817 0.3691 0.2011 -0.0022 0.0036 -0.0467 382 ARG A CB 2949 C CG . ARG A 382 ? 0.2738 0.3645 0.1965 -0.0027 0.0035 -0.0457 382 ARG A CG 2950 C CD . ARG A 382 ? 0.2763 0.3881 0.2015 0.0003 -0.0008 -0.0519 382 ARG A CD 2951 N NE . ARG A 382 ? 0.2854 0.4035 0.2160 -0.0004 -0.0004 -0.0532 382 ARG A NE 2952 C CZ . ARG A 382 ? 0.3005 0.4373 0.2334 0.0041 -0.0045 -0.0570 382 ARG A CZ 2953 N NH1 . ARG A 382 ? 0.3078 0.4586 0.2365 0.0101 -0.0096 -0.0589 382 ARG A NH1 2954 N NH2 . ARG A 382 ? 0.2921 0.4348 0.2307 0.0034 -0.0036 -0.0584 382 ARG A NH2 2955 N N . GLU A 383 ? 0.3089 0.3685 0.2395 -0.0150 0.0170 -0.0521 383 GLU A N 2956 C CA . GLU A 383 ? 0.3199 0.3660 0.2569 -0.0211 0.0248 -0.0535 383 GLU A CA 2957 C C . GLU A 383 ? 0.3182 0.3453 0.2492 -0.0179 0.0278 -0.0429 383 GLU A C 2958 O O . GLU A 383 ? 0.3198 0.3367 0.2504 -0.0190 0.0321 -0.0372 383 GLU A O 2959 C CB . GLU A 383 ? 0.3326 0.3808 0.2785 -0.0270 0.0285 -0.0658 383 GLU A CB 2960 C CG . GLU A 383 ? 0.3513 0.3823 0.3047 -0.0337 0.0383 -0.0671 383 GLU A CG 2961 C CD . GLU A 383 ? 0.3728 0.4016 0.3350 -0.0392 0.0428 -0.0795 383 GLU A CD 2962 O OE1 . GLU A 383 ? 0.4238 0.4699 0.3881 -0.0395 0.0380 -0.0902 383 GLU A OE1 2963 O OE2 . GLU A 383 ? 0.3957 0.4053 0.3623 -0.0428 0.0514 -0.0787 383 GLU A OE2 2964 N N . ALA A 384 ? 0.3106 0.3348 0.2367 -0.0135 0.0255 -0.0406 384 ALA A N 2965 C CA . ALA A 384 ? 0.3149 0.3251 0.2360 -0.0094 0.0272 -0.0316 384 ALA A CA 2966 C C . ALA A 384 ? 0.3068 0.3159 0.2216 -0.0056 0.0244 -0.0220 384 ALA A C 2967 O O . ALA A 384 ? 0.3123 0.3108 0.2245 -0.0040 0.0274 -0.0155 384 ALA A O 2968 C CB . ALA A 384 ? 0.3066 0.3184 0.2249 -0.0053 0.0248 -0.0321 384 ALA A CB 2969 N N . ALA A 385 ? 0.2996 0.3196 0.2116 -0.0038 0.0187 -0.0216 385 ALA A N 2970 C CA . ALA A 385 ? 0.2948 0.3147 0.2018 -0.0008 0.0157 -0.0147 385 ALA A CA 2971 C C . ALA A 385 ? 0.3052 0.3217 0.2131 -0.0031 0.0193 -0.0133 385 ALA A C 2972 O O . ALA A 385 ? 0.3063 0.3165 0.2097 -0.0007 0.0201 -0.0071 385 ALA A O 2973 C CB . ALA A 385 ? 0.2768 0.3074 0.1819 0.0013 0.0104 -0.0153 385 ALA A CB 2974 N N . ARG A 386 ? 0.3010 0.3234 0.2149 -0.0076 0.0214 -0.0196 386 ARG A N 2975 C CA . ARG A 386 ? 0.3083 0.3287 0.2245 -0.0108 0.0261 -0.0190 386 ARG A CA 2976 C C . ARG A 386 ? 0.3176 0.3229 0.2329 -0.0119 0.0334 -0.0142 386 ARG A C 2977 O O . ARG A 386 ? 0.3171 0.3172 0.2279 -0.0104 0.0362 -0.0079 386 ARG A O 2978 C CB . ARG A 386 ? 0.3116 0.3434 0.2369 -0.0162 0.0275 -0.0283 386 ARG A CB 2979 C CG . ARG A 386 ? 0.3360 0.3682 0.2660 -0.0207 0.0335 -0.0289 386 ARG A CG 2980 C CD . ARG A 386 ? 0.3751 0.3996 0.3135 -0.0281 0.0421 -0.0334 386 ARG A CD 2981 N NE . ARG A 386 ? 0.4140 0.4486 0.3611 -0.0322 0.0405 -0.0448 386 ARG A NE 2982 C CZ . ARG A 386 ? 0.4331 0.4634 0.3900 -0.0397 0.0473 -0.0525 386 ARG A CZ 2983 N NH1 . ARG A 386 ? 0.4763 0.4899 0.4354 -0.0438 0.0571 -0.0483 386 ARG A NH1 2984 N NH2 . ARG A 386 ? 0.4258 0.4685 0.3901 -0.0429 0.0447 -0.0645 386 ARG A NH2 2985 N N . LYS A 387 ? 0.3220 0.3201 0.2409 -0.0137 0.0366 -0.0171 387 LYS A N 2986 C CA . LYS A 387 ? 0.3370 0.3186 0.2557 -0.0140 0.0445 -0.0124 387 LYS A CA 2987 C C . LYS A 387 ? 0.3325 0.3065 0.2415 -0.0060 0.0429 -0.0020 387 LYS A C 2988 O O . LYS A 387 ? 0.3427 0.3043 0.2482 -0.0039 0.0491 0.0052 387 LYS A O 2989 C CB . LYS A 387 ? 0.3427 0.3181 0.2689 -0.0178 0.0487 -0.0197 387 LYS A CB 2990 C CG . LYS A 387 ? 0.3422 0.3224 0.2796 -0.0269 0.0535 -0.0301 387 LYS A CG 2991 C CD . LYS A 387 ? 0.3525 0.3287 0.2981 -0.0311 0.0569 -0.0399 387 LYS A CD 2992 C CE . LYS A 387 ? 0.3462 0.3273 0.3048 -0.0413 0.0625 -0.0515 387 LYS A CE 2993 N NZ . LYS A 387 ? 0.3912 0.3629 0.3585 -0.0461 0.0685 -0.0609 387 LYS A NZ 2994 N N . SER A 388 ? 0.3187 0.3009 0.2235 -0.0016 0.0350 -0.0012 388 SER A N 2995 C CA . SER A 388 ? 0.3244 0.3042 0.2219 0.0055 0.0320 0.0063 388 SER A CA 2996 C C . SER A 388 ? 0.3208 0.3039 0.2116 0.0083 0.0302 0.0117 388 SER A C 2997 O O . SER A 388 ? 0.3334 0.3144 0.2179 0.0143 0.0292 0.0181 388 SER A O 2998 C CB . SER A 388 ? 0.3060 0.2938 0.2036 0.0080 0.0253 0.0041 388 SER A CB 2999 O OG . SER A 388 ? 0.3077 0.3059 0.2040 0.0075 0.0196 0.0027 388 SER A OG 3000 N N . LEU A 389 ? 0.3130 0.3028 0.2052 0.0046 0.0297 0.0086 389 LEU A N 3001 C CA . LEU A 389 ? 0.3124 0.3070 0.1983 0.0074 0.0274 0.0120 389 LEU A CA 3002 C C . LEU A 389 ? 0.3200 0.3070 0.1998 0.0100 0.0336 0.0193 389 LEU A C 3003 O O . LEU A 389 ? 0.3309 0.3099 0.2136 0.0064 0.0414 0.0202 389 LEU A O 3004 C CB . LEU A 389 ? 0.3111 0.3145 0.2006 0.0036 0.0264 0.0068 389 LEU A CB 3005 C CG . LEU A 389 ? 0.3119 0.3233 0.2070 0.0016 0.0216 0.0003 389 LEU A CG 3006 C CD1 . LEU A 389 ? 0.2804 0.3003 0.1790 -0.0008 0.0219 -0.0038 389 LEU A CD1 3007 C CD2 . LEU A 389 ? 0.2783 0.2928 0.1704 0.0055 0.0149 0.0012 389 LEU A CD2 3008 N N . VAL A 390 ? 0.3208 0.3106 0.1921 0.0162 0.0304 0.0242 390 VAL A N 3009 C CA . VAL A 390 ? 0.3312 0.3159 0.1941 0.0203 0.0359 0.0321 390 VAL A CA 3010 C C . VAL A 390 ? 0.3319 0.3260 0.1893 0.0211 0.0342 0.0315 390 VAL A C 3011 O O . VAL A 390 ? 0.3231 0.3267 0.1776 0.0240 0.0270 0.0287 390 VAL A O 3012 C CB . VAL A 390 ? 0.3417 0.3230 0.1973 0.0289 0.0348 0.0394 390 VAL A CB 3013 C CG1 . VAL A 390 ? 0.3381 0.3135 0.1833 0.0342 0.0417 0.0492 390 VAL A CG1 3014 C CG2 . VAL A 390 ? 0.3188 0.2906 0.1803 0.0289 0.0368 0.0395 390 VAL A CG2 3015 N N . LEU A 391 ? 0.3412 0.3327 0.1982 0.0179 0.0417 0.0332 391 LEU A N 3016 C CA . LEU A 391 ? 0.3397 0.3401 0.1913 0.0188 0.0415 0.0324 391 LEU A CA 3017 C C . LEU A 391 ? 0.3591 0.3595 0.1970 0.0270 0.0430 0.0410 391 LEU A C 3018 O O . LEU A 391 ? 0.3765 0.3669 0.2094 0.0291 0.0512 0.0498 391 LEU A O 3019 C CB . LEU A 391 ? 0.3418 0.3414 0.1994 0.0120 0.0496 0.0306 391 LEU A CB 3020 C CG . LEU A 391 ? 0.3419 0.3513 0.1961 0.0121 0.0513 0.0290 391 LEU A CG 3021 C CD1 . LEU A 391 ? 0.3228 0.3436 0.1804 0.0124 0.0421 0.0202 391 LEU A CD1 3022 C CD2 . LEU A 391 ? 0.3365 0.3440 0.1985 0.0047 0.0612 0.0282 391 LEU A CD2 3023 N N . LEU A 392 ? 0.3568 0.3685 0.1886 0.0319 0.0352 0.0383 392 LEU A N 3024 C CA . LEU A 392 ? 0.3720 0.3884 0.1903 0.0410 0.0344 0.0448 392 LEU A CA 3025 C C . LEU A 392 ? 0.3830 0.4069 0.1921 0.0429 0.0379 0.0458 392 LEU A C 3026 O O . LEU A 392 ? 0.3868 0.4127 0.1829 0.0503 0.0408 0.0537 392 LEU A O 3027 C CB . LEU A 392 ? 0.3664 0.3931 0.1841 0.0452 0.0238 0.0398 392 LEU A CB 3028 C CG . LEU A 392 ? 0.3605 0.3825 0.1851 0.0454 0.0203 0.0399 392 LEU A CG 3029 C CD1 . LEU A 392 ? 0.3750 0.4102 0.2003 0.0484 0.0105 0.0337 392 LEU A CD1 3030 C CD2 . LEU A 392 ? 0.3635 0.3754 0.1824 0.0515 0.0260 0.0508 392 LEU A CD2 3031 N N . LYS A 393 ? 0.3752 0.4040 0.1907 0.0370 0.0376 0.0379 393 LYS A N 3032 C CA . LYS A 393 ? 0.3915 0.4292 0.1999 0.0385 0.0406 0.0367 393 LYS A CA 3033 C C . LYS A 393 ? 0.3817 0.4197 0.2018 0.0305 0.0438 0.0302 393 LYS A C 3034 O O . LYS A 393 ? 0.3579 0.3957 0.1889 0.0264 0.0384 0.0230 393 LYS A O 3035 C CB . LYS A 393 ? 0.3857 0.4371 0.1888 0.0432 0.0314 0.0291 393 LYS A CB 3036 C CG . LYS A 393 ? 0.4010 0.4631 0.1949 0.0462 0.0341 0.0271 393 LYS A CG 3037 C CD . LYS A 393 ? 0.3749 0.4501 0.1649 0.0503 0.0249 0.0176 393 LYS A CD 3038 C CE . LYS A 393 ? 0.4047 0.4911 0.1844 0.0539 0.0279 0.0151 393 LYS A CE 3039 N NZ . LYS A 393 ? 0.3972 0.4968 0.1738 0.0574 0.0192 0.0039 393 LYS A NZ 3040 N N . ASN A 394 ? 0.3908 0.4305 0.2085 0.0289 0.0525 0.0328 394 ASN A N 3041 C CA . ASN A 394 ? 0.3909 0.4352 0.2198 0.0224 0.0553 0.0258 394 ASN A CA 3042 C C . ASN A 394 ? 0.4097 0.4636 0.2315 0.0244 0.0610 0.0258 394 ASN A C 3043 O O . ASN A 394 ? 0.4255 0.4783 0.2498 0.0203 0.0712 0.0294 394 ASN A O 3044 C CB . ASN A 394 ? 0.3893 0.4244 0.2293 0.0147 0.0627 0.0280 394 ASN A CB 3045 C CG . ASN A 394 ? 0.3805 0.4232 0.2350 0.0083 0.0626 0.0187 394 ASN A CG 3046 O OD1 . ASN A 394 ? 0.3716 0.4231 0.2289 0.0101 0.0553 0.0109 394 ASN A OD1 3047 N ND2 . ASN A 394 ? 0.3845 0.4239 0.2489 0.0009 0.0710 0.0190 394 ASN A ND2 3048 N N . GLY A 395 ? 0.4166 0.4805 0.2303 0.0302 0.0548 0.0209 395 GLY A N 3049 C CA . GLY A 395 ? 0.4346 0.5093 0.2392 0.0337 0.0593 0.0201 395 GLY A CA 3050 C C . GLY A 395 ? 0.4580 0.5390 0.2457 0.0426 0.0554 0.0225 395 GLY A C 3051 O O . GLY A 395 ? 0.4649 0.5402 0.2439 0.0465 0.0560 0.0318 395 GLY A O 3052 N N . LYS A 396 ? 0.4711 0.5646 0.2540 0.0463 0.0513 0.0137 396 LYS A N 3053 C CA . LYS A 396 ? 0.4883 0.5919 0.2557 0.0547 0.0464 0.0128 396 LYS A CA 3054 C C . LYS A 396 ? 0.5194 0.6272 0.2689 0.0610 0.0547 0.0243 396 LYS A C 3055 O O . LYS A 396 ? 0.5326 0.6457 0.2687 0.0688 0.0510 0.0285 396 LYS A O 3056 C CB . LYS A 396 ? 0.4887 0.6042 0.2569 0.0565 0.0402 -0.0017 396 LYS A CB 3057 C CG . LYS A 396 ? 0.4800 0.5905 0.2633 0.0522 0.0315 -0.0121 396 LYS A CG 3058 C CD . LYS A 396 ? 0.4682 0.5886 0.2502 0.0552 0.0250 -0.0262 396 LYS A CD 3059 C CE . LYS A 396 ? 0.4546 0.5674 0.2505 0.0511 0.0172 -0.0344 396 LYS A CE 3060 N NZ . LYS A 396 ? 0.4624 0.5802 0.2617 0.0521 0.0132 -0.0490 396 LYS A NZ 3061 N N . THR A 397 ? 0.5298 0.6368 0.2791 0.0582 0.0662 0.0294 397 THR A N 3062 C CA . THR A 397 ? 0.5551 0.6645 0.2873 0.0638 0.0765 0.0422 397 THR A CA 3063 C C . THR A 397 ? 0.5657 0.6605 0.3052 0.0567 0.0895 0.0532 397 THR A C 3064 O O . THR A 397 ? 0.5576 0.6456 0.3154 0.0475 0.0901 0.0481 397 THR A O 3065 C CB . THR A 397 ? 0.5637 0.6903 0.2854 0.0680 0.0803 0.0370 397 THR A CB 3066 O OG1 . THR A 397 ? 0.5444 0.6709 0.2787 0.0603 0.0885 0.0336 397 THR A OG1 3067 C CG2 . THR A 397 ? 0.5643 0.7049 0.2840 0.0723 0.0678 0.0215 397 THR A CG2 3068 N N . SER A 398 ? 0.5890 0.6793 0.3143 0.0611 0.1003 0.0681 398 SER A N 3069 C CA . SER A 398 ? 0.5980 0.6728 0.3304 0.0538 0.1146 0.0788 398 SER A CA 3070 C C . SER A 398 ? 0.5897 0.6704 0.3355 0.0445 0.1230 0.0722 398 SER A C 3071 O O . SER A 398 ? 0.6039 0.6739 0.3636 0.0349 0.1324 0.0750 398 SER A O 3072 C CB . SER A 398 ? 0.6249 0.6938 0.3375 0.0617 0.1259 0.0970 398 SER A CB 3073 O OG . SER A 398 ? 0.6604 0.7456 0.3571 0.0680 0.1304 0.0981 398 SER A OG 3074 N N . THR A 399 ? 0.5687 0.6674 0.3111 0.0473 0.1196 0.0624 399 THR A N 3075 C CA . THR A 399 ? 0.5490 0.6566 0.3023 0.0405 0.1276 0.0561 399 THR A CA 3076 C C . THR A 399 ? 0.4999 0.6137 0.2731 0.0350 0.1180 0.0396 399 THR A C 3077 O O . THR A 399 ? 0.4841 0.6065 0.2694 0.0296 0.1234 0.0332 399 THR A O 3078 C CB . THR A 399 ? 0.5698 0.6940 0.3063 0.0478 0.1329 0.0568 399 THR A CB 3079 O OG1 . THR A 399 ? 0.5795 0.7158 0.3078 0.0559 0.1192 0.0458 399 THR A OG1 3080 C CG2 . THR A 399 ? 0.6142 0.7327 0.3301 0.0539 0.1446 0.0752 399 THR A CG2 3081 N N . ASP A 400 ? 0.4657 0.5757 0.2421 0.0370 0.1042 0.0332 400 ASP A N 3082 C CA . ASP A 400 ? 0.4253 0.5382 0.2192 0.0328 0.0955 0.0198 400 ASP A CA 3083 C C . ASP A 400 ? 0.4157 0.5211 0.2286 0.0227 0.1003 0.0203 400 ASP A C 3084 O O . ASP A 400 ? 0.4172 0.5097 0.2306 0.0189 0.1060 0.0297 400 ASP A O 3085 C CB . ASP A 400 ? 0.4169 0.5258 0.2095 0.0368 0.0811 0.0145 400 ASP A CB 3086 C CG . ASP A 400 ? 0.4102 0.5308 0.1906 0.0450 0.0742 0.0071 400 ASP A CG 3087 O OD1 . ASP A 400 ? 0.4154 0.5463 0.1838 0.0494 0.0803 0.0085 400 ASP A OD1 3088 O OD2 . ASP A 400 ? 0.4174 0.5372 0.2005 0.0469 0.0631 -0.0009 400 ASP A OD2 3089 N N . ALA A 401 ? 0.3981 0.5124 0.2266 0.0189 0.0980 0.0095 401 ALA A N 3090 C CA . ALA A 401 ? 0.3910 0.5014 0.2385 0.0107 0.0977 0.0062 401 ALA A CA 3091 C C . ALA A 401 ? 0.3856 0.4833 0.2333 0.0115 0.0874 0.0068 401 ALA A C 3092 O O . ALA A 401 ? 0.3838 0.4817 0.2254 0.0176 0.0772 0.0030 401 ALA A O 3093 C CB . ALA A 401 ? 0.3710 0.4958 0.2326 0.0100 0.0943 -0.0060 401 ALA A CB 3094 N N . PRO A 402 ? 0.3877 0.4745 0.2432 0.0050 0.0906 0.0112 402 PRO A N 3095 C CA . PRO A 402 ? 0.3813 0.4573 0.2384 0.0054 0.0816 0.0113 402 PRO A CA 3096 C C . PRO A 402 ? 0.3650 0.4481 0.2323 0.0061 0.0713 0.0007 402 PRO A C 3097 O O . PRO A 402 ? 0.3639 0.4567 0.2439 0.0024 0.0731 -0.0059 402 PRO A O 3098 C CB . PRO A 402 ? 0.3826 0.4487 0.2495 -0.0030 0.0892 0.0152 402 PRO A CB 3099 C CG . PRO A 402 ? 0.4105 0.4775 0.2758 -0.0066 0.1033 0.0210 402 PRO A CG 3100 C CD . PRO A 402 ? 0.3986 0.4827 0.2626 -0.0035 0.1036 0.0154 402 PRO A CD 3101 N N . LEU A 403 ? 0.3603 0.4396 0.2221 0.0113 0.0611 -0.0011 403 LEU A N 3102 C CA . LEU A 403 ? 0.3574 0.4404 0.2280 0.0125 0.0523 -0.0094 403 LEU A CA 3103 C C . LEU A 403 ? 0.3409 0.4213 0.2242 0.0070 0.0510 -0.0110 403 LEU A C 3104 O O . LEU A 403 ? 0.3311 0.4202 0.2249 0.0064 0.0487 -0.0176 403 LEU A O 3105 C CB . LEU A 403 ? 0.3583 0.4367 0.2212 0.0182 0.0430 -0.0109 403 LEU A CB 3106 C CG . LEU A 403 ? 0.3733 0.4531 0.2446 0.0199 0.0354 -0.0181 403 LEU A CG 3107 C CD1 . LEU A 403 ? 0.3826 0.4733 0.2586 0.0226 0.0367 -0.0250 403 LEU A CD1 3108 C CD2 . LEU A 403 ? 0.3695 0.4432 0.2356 0.0236 0.0278 -0.0196 403 LEU A CD2 3109 N N . LEU A 404 ? 0.3419 0.4113 0.2238 0.0039 0.0525 -0.0053 404 LEU A N 3110 C CA . LEU A 404 ? 0.3374 0.4043 0.2301 -0.0012 0.0512 -0.0076 404 LEU A CA 3111 C C . LEU A 404 ? 0.3470 0.4144 0.2479 -0.0090 0.0616 -0.0069 404 LEU A C 3112 O O . LEU A 404 ? 0.3629 0.4238 0.2575 -0.0102 0.0699 0.0000 404 LEU A O 3113 C CB . LEU A 404 ? 0.3326 0.3870 0.2204 0.0001 0.0466 -0.0032 404 LEU A CB 3114 C CG . LEU A 404 ? 0.3172 0.3702 0.1982 0.0064 0.0375 -0.0039 404 LEU A CG 3115 C CD1 . LEU A 404 ? 0.3013 0.3440 0.1790 0.0070 0.0340 0.0003 404 LEU A CD1 3116 C CD2 . LEU A 404 ? 0.2875 0.3481 0.1754 0.0081 0.0314 -0.0110 404 LEU A CD2 3117 N N . PRO A 405 ? 0.3380 0.4137 0.2531 -0.0143 0.0615 -0.0142 405 PRO A N 3118 C CA . PRO A 405 ? 0.3238 0.4076 0.2449 -0.0115 0.0518 -0.0211 405 PRO A CA 3119 C C . PRO A 405 ? 0.3166 0.4143 0.2396 -0.0061 0.0481 -0.0262 405 PRO A C 3120 O O . PRO A 405 ? 0.3106 0.4176 0.2364 -0.0071 0.0539 -0.0279 405 PRO A O 3121 C CB . PRO A 405 ? 0.3219 0.4117 0.2572 -0.0191 0.0543 -0.0272 405 PRO A CB 3122 C CG . PRO A 405 ? 0.3407 0.4299 0.2814 -0.0269 0.0664 -0.0262 405 PRO A CG 3123 C CD . PRO A 405 ? 0.3466 0.4252 0.2732 -0.0234 0.0715 -0.0165 405 PRO A CD 3124 N N . LEU A 406 ? 0.3075 0.4055 0.2287 -0.0001 0.0390 -0.0280 406 LEU A N 3125 C CA . LEU A 406 ? 0.3094 0.4171 0.2320 0.0066 0.0349 -0.0323 406 LEU A CA 3126 C C . LEU A 406 ? 0.3062 0.4312 0.2424 0.0057 0.0343 -0.0394 406 LEU A C 3127 O O . LEU A 406 ? 0.3027 0.4305 0.2455 0.0013 0.0334 -0.0415 406 LEU A O 3128 C CB . LEU A 406 ? 0.3054 0.4041 0.2214 0.0130 0.0268 -0.0306 406 LEU A CB 3129 C CG . LEU A 406 ? 0.3160 0.4017 0.2201 0.0148 0.0259 -0.0259 406 LEU A CG 3130 C CD1 . LEU A 406 ? 0.3448 0.4209 0.2457 0.0176 0.0191 -0.0242 406 LEU A CD1 3131 C CD2 . LEU A 406 ? 0.3007 0.3900 0.2002 0.0192 0.0273 -0.0282 406 LEU A CD2 3132 N N . PRO A 407 ? 0.3039 0.4421 0.2444 0.0104 0.0344 -0.0439 407 PRO A N 3133 C CA . PRO A 407 ? 0.2977 0.4554 0.2511 0.0117 0.0324 -0.0510 407 PRO A CA 3134 C C . PRO A 407 ? 0.2902 0.4477 0.2425 0.0195 0.0232 -0.0510 407 PRO A C 3135 O O . PRO A 407 ? 0.2934 0.4393 0.2369 0.0266 0.0193 -0.0472 407 PRO A O 3136 C CB . PRO A 407 ? 0.2980 0.4682 0.2548 0.0159 0.0357 -0.0547 407 PRO A CB 3137 C CG . PRO A 407 ? 0.3126 0.4674 0.2557 0.0209 0.0352 -0.0500 407 PRO A CG 3138 C CD . PRO A 407 ? 0.3063 0.4434 0.2401 0.0154 0.0364 -0.0433 407 PRO A CD 3139 N N . LYS A 408 ? 0.2846 0.4550 0.2455 0.0182 0.0204 -0.0554 408 LYS A N 3140 C CA . LYS A 408 ? 0.2803 0.4540 0.2398 0.0269 0.0123 -0.0549 408 LYS A CA 3141 C C . LYS A 408 ? 0.2824 0.4676 0.2444 0.0382 0.0092 -0.0569 408 LYS A C 3142 O O . LYS A 408 ? 0.2755 0.4569 0.2327 0.0476 0.0036 -0.0535 408 LYS A O 3143 C CB . LYS A 408 ? 0.2801 0.4679 0.2475 0.0231 0.0098 -0.0601 408 LYS A CB 3144 C CG . LYS A 408 ? 0.2840 0.4582 0.2480 0.0143 0.0117 -0.0579 408 LYS A CG 3145 C CD . LYS A 408 ? 0.3026 0.4941 0.2773 0.0090 0.0107 -0.0664 408 LYS A CD 3146 C CE . LYS A 408 ? 0.3130 0.4903 0.2860 -0.0004 0.0141 -0.0654 408 LYS A CE 3147 N NZ . LYS A 408 ? 0.3230 0.5141 0.3022 -0.0023 0.0104 -0.0730 408 LYS A NZ 3148 N N . LYS A 409 ? 0.2909 0.4897 0.2606 0.0376 0.0137 -0.0620 409 LYS A N 3149 C CA . LYS A 409 ? 0.2911 0.5015 0.2642 0.0488 0.0117 -0.0646 409 LYS A CA 3150 C C . LYS A 409 ? 0.2989 0.4978 0.2658 0.0512 0.0158 -0.0629 409 LYS A C 3151 O O . LYS A 409 ? 0.2948 0.4971 0.2639 0.0443 0.0226 -0.0651 409 LYS A O 3152 C CB . LYS A 409 ? 0.3018 0.5427 0.2906 0.0482 0.0128 -0.0736 409 LYS A CB 3153 C CG . LYS A 409 ? 0.3069 0.5627 0.3002 0.0621 0.0097 -0.0764 409 LYS A CG 3154 C CD . LYS A 409 ? 0.3354 0.6248 0.3454 0.0620 0.0096 -0.0861 409 LYS A CD 3155 C CE . LYS A 409 ? 0.3524 0.6567 0.3661 0.0781 0.0058 -0.0880 409 LYS A CE 3156 N NZ . LYS A 409 ? 0.3896 0.7306 0.4211 0.0786 0.0054 -0.0984 409 LYS A NZ 3157 N N . ALA A 410 ? 0.3013 0.4867 0.2605 0.0610 0.0122 -0.0593 410 ALA A N 3158 C CA . ALA A 410 ? 0.3065 0.4812 0.2600 0.0647 0.0150 -0.0594 410 ALA A CA 3159 C C . ALA A 410 ? 0.3124 0.4809 0.2642 0.0782 0.0107 -0.0582 410 ALA A C 3160 O O . ALA A 410 ? 0.3189 0.4822 0.2687 0.0826 0.0059 -0.0537 410 ALA A O 3161 C CB . ALA A 410 ? 0.3017 0.4546 0.2439 0.0578 0.0166 -0.0549 410 ALA A CB 3162 N N . PRO A 411 ? 0.3220 0.4907 0.2744 0.0853 0.0130 -0.0619 411 PRO A N 3163 C CA . PRO A 411 ? 0.3297 0.4908 0.2814 0.0989 0.0099 -0.0605 411 PRO A CA 3164 C C . PRO A 411 ? 0.3376 0.4727 0.2803 0.0998 0.0072 -0.0536 411 PRO A C 3165 O O . PRO A 411 ? 0.3403 0.4717 0.2826 0.1082 0.0038 -0.0487 411 PRO A O 3166 C CB . PRO A 411 ? 0.3392 0.5013 0.2922 0.1040 0.0142 -0.0667 411 PRO A CB 3167 C CG . PRO A 411 ? 0.3335 0.5169 0.2925 0.0960 0.0188 -0.0719 411 PRO A CG 3168 C CD . PRO A 411 ? 0.3223 0.4988 0.2762 0.0825 0.0191 -0.0676 411 PRO A CD 3169 N N . LYS A 412 ? 0.3394 0.4581 0.2748 0.0913 0.0089 -0.0529 412 LYS A N 3170 C CA . LYS A 412 ? 0.3474 0.4423 0.2759 0.0914 0.0072 -0.0479 412 LYS A CA 3171 C C . LYS A 412 ? 0.3414 0.4284 0.2640 0.0794 0.0080 -0.0471 412 LYS A C 3172 O O . LYS A 412 ? 0.3406 0.4322 0.2616 0.0745 0.0110 -0.0515 412 LYS A O 3173 C CB . LYS A 412 ? 0.3678 0.4489 0.2957 0.0993 0.0092 -0.0513 412 LYS A CB 3174 C CG . LYS A 412 ? 0.3819 0.4384 0.3059 0.1014 0.0086 -0.0467 412 LYS A CG 3175 C CD . LYS A 412 ? 0.4035 0.4485 0.3293 0.1101 0.0116 -0.0521 412 LYS A CD 3176 C CE . LYS A 412 ? 0.4340 0.4522 0.3574 0.1102 0.0127 -0.0493 412 LYS A CE 3177 N NZ . LYS A 412 ? 0.4424 0.4476 0.3686 0.1177 0.0164 -0.0559 412 LYS A NZ 3178 N N . ILE A 413 ? 0.3294 0.4056 0.2483 0.0754 0.0056 -0.0412 413 ILE A N 3179 C CA . ILE A 413 ? 0.3233 0.3924 0.2369 0.0653 0.0059 -0.0400 413 ILE A CA 3180 C C . ILE A 413 ? 0.3321 0.3815 0.2418 0.0646 0.0044 -0.0366 413 ILE A C 3181 O O . ILE A 413 ? 0.3369 0.3782 0.2478 0.0709 0.0035 -0.0329 413 ILE A O 3182 C CB . ILE A 413 ? 0.3121 0.3919 0.2267 0.0582 0.0053 -0.0371 413 ILE A CB 3183 C CG1 . ILE A 413 ? 0.3091 0.3873 0.2244 0.0603 0.0019 -0.0317 413 ILE A CG1 3184 C CG2 . ILE A 413 ? 0.3020 0.4016 0.2227 0.0575 0.0079 -0.0413 413 ILE A CG2 3185 C CD1 . ILE A 413 ? 0.2899 0.3736 0.2052 0.0523 0.0014 -0.0297 413 ILE A CD1 3186 N N . LEU A 414 ? 0.3274 0.3701 0.2328 0.0574 0.0047 -0.0377 414 LEU A N 3187 C CA . LEU A 414 ? 0.3283 0.3548 0.2318 0.0549 0.0037 -0.0360 414 LEU A CA 3188 C C . LEU A 414 ? 0.3210 0.3468 0.2219 0.0478 0.0021 -0.0310 414 LEU A C 3189 O O . LEU A 414 ? 0.3156 0.3489 0.2138 0.0427 0.0022 -0.0315 414 LEU A O 3190 C CB . LEU A 414 ? 0.3353 0.3555 0.2371 0.0534 0.0048 -0.0435 414 LEU A CB 3191 C CG . LEU A 414 ? 0.3352 0.3411 0.2371 0.0491 0.0042 -0.0446 414 LEU A CG 3192 C CD1 . LEU A 414 ? 0.3373 0.3278 0.2434 0.0534 0.0056 -0.0414 414 LEU A CD1 3193 C CD2 . LEU A 414 ? 0.3441 0.3498 0.2445 0.0471 0.0047 -0.0545 414 LEU A CD2 3194 N N . VAL A 415 ? 0.3249 0.3413 0.2264 0.0480 0.0012 -0.0259 415 VAL A N 3195 C CA . VAL A 415 ? 0.3235 0.3376 0.2230 0.0417 0.0000 -0.0219 415 VAL A CA 3196 C C . VAL A 415 ? 0.3339 0.3344 0.2343 0.0391 0.0006 -0.0234 415 VAL A C 3197 O O . VAL A 415 ? 0.3422 0.3315 0.2452 0.0429 0.0023 -0.0229 415 VAL A O 3198 C CB . VAL A 415 ? 0.3231 0.3403 0.2227 0.0435 -0.0010 -0.0152 415 VAL A CB 3199 C CG1 . VAL A 415 ? 0.3080 0.3226 0.2060 0.0375 -0.0018 -0.0116 415 VAL A CG1 3200 C CG2 . VAL A 415 ? 0.3180 0.3509 0.2189 0.0450 -0.0016 -0.0161 415 VAL A CG2 3201 N N . ALA A 416 ? 0.3223 0.3239 0.2213 0.0328 -0.0005 -0.0256 416 ALA A N 3202 C CA . ALA A 416 ? 0.3213 0.3141 0.2229 0.0292 -0.0002 -0.0299 416 ALA A CA 3203 C C . ALA A 416 ? 0.3157 0.3114 0.2169 0.0231 -0.0019 -0.0284 416 ALA A C 3204 O O . ALA A 416 ? 0.3027 0.3068 0.2003 0.0221 -0.0033 -0.0250 416 ALA A O 3205 C CB . ALA A 416 ? 0.3251 0.3202 0.2262 0.0297 -0.0002 -0.0394 416 ALA A CB 3206 N N . GLY A 417 ? 0.3240 0.3129 0.2297 0.0191 -0.0015 -0.0318 417 GLY A N 3207 C CA . GLY A 417 ? 0.3179 0.3117 0.2247 0.0138 -0.0033 -0.0320 417 GLY A CA 3208 C C . GLY A 417 ? 0.3274 0.3140 0.2383 0.0113 -0.0013 -0.0260 417 GLY A C 3209 O O . GLY A 417 ? 0.3305 0.3110 0.2405 0.0146 0.0009 -0.0191 417 GLY A O 3210 N N . SER A 418 ? 0.3198 0.3090 0.2352 0.0059 -0.0020 -0.0288 418 SER A N 3211 C CA . SER A 418 ? 0.3269 0.3115 0.2470 0.0024 0.0005 -0.0240 418 SER A CA 3212 C C . SER A 418 ? 0.3189 0.3081 0.2340 0.0047 0.0000 -0.0152 418 SER A C 3213 O O . SER A 418 ? 0.3239 0.3089 0.2407 0.0037 0.0028 -0.0095 418 SER A O 3214 C CB . SER A 418 ? 0.3207 0.3127 0.2473 -0.0037 -0.0010 -0.0306 418 SER A CB 3215 O OG . SER A 418 ? 0.3137 0.3198 0.2351 -0.0021 -0.0057 -0.0319 418 SER A OG 3216 N N . HIS A 419 ? 0.3141 0.3120 0.2231 0.0075 -0.0029 -0.0145 419 HIS A N 3217 C CA . HIS A 419 ? 0.3133 0.3159 0.2186 0.0089 -0.0032 -0.0084 419 HIS A CA 3218 C C . HIS A 419 ? 0.3150 0.3177 0.2159 0.0134 -0.0028 -0.0051 419 HIS A C 3219 O O . HIS A 419 ? 0.3176 0.3251 0.2160 0.0142 -0.0031 -0.0018 419 HIS A O 3220 C CB . HIS A 419 ? 0.2968 0.3087 0.1999 0.0080 -0.0058 -0.0097 419 HIS A CB 3221 C CG . HIS A 419 ? 0.3148 0.3309 0.2229 0.0046 -0.0067 -0.0122 419 HIS A CG 3222 N ND1 . HIS A 419 ? 0.3051 0.3210 0.2188 0.0014 -0.0072 -0.0187 419 HIS A ND1 3223 C CD2 . HIS A 419 ? 0.3053 0.3269 0.2147 0.0037 -0.0072 -0.0101 419 HIS A CD2 3224 C CE1 . HIS A 419 ? 0.2981 0.3210 0.2168 -0.0015 -0.0082 -0.0206 419 HIS A CE1 3225 N NE2 . HIS A 419 ? 0.3022 0.3286 0.2181 0.0004 -0.0083 -0.0150 419 HIS A NE2 3226 N N . ALA A 420 ? 0.3207 0.3192 0.2216 0.0164 -0.0021 -0.0069 420 ALA A N 3227 C CA . ALA A 420 ? 0.3221 0.3236 0.2201 0.0213 -0.0021 -0.0049 420 ALA A CA 3228 C C . ALA A 420 ? 0.3237 0.3230 0.2208 0.0247 -0.0009 0.0012 420 ALA A C 3229 O O . ALA A 420 ? 0.3151 0.3222 0.2100 0.0278 -0.0019 0.0028 420 ALA A O 3230 C CB . ALA A 420 ? 0.3277 0.3268 0.2264 0.0245 -0.0018 -0.0091 420 ALA A CB 3231 N N . ASP A 421 ? 0.3270 0.3166 0.2260 0.0242 0.0016 0.0044 421 ASP A N 3232 C CA . ASP A 421 ? 0.3298 0.3167 0.2263 0.0285 0.0037 0.0117 421 ASP A CA 3233 C C . ASP A 421 ? 0.3349 0.3170 0.2330 0.0241 0.0064 0.0153 421 ASP A C 3234 O O . ASP A 421 ? 0.3548 0.3260 0.2541 0.0248 0.0107 0.0198 421 ASP A O 3235 C CB . ASP A 421 ? 0.3349 0.3121 0.2313 0.0349 0.0060 0.0141 421 ASP A CB 3236 C CG . ASP A 421 ? 0.3504 0.3277 0.2417 0.0422 0.0075 0.0228 421 ASP A CG 3237 O OD1 . ASP A 421 ? 0.3362 0.3266 0.2236 0.0442 0.0048 0.0240 421 ASP A OD1 3238 O OD2 . ASP A 421 ? 0.3917 0.3561 0.2827 0.0462 0.0116 0.0283 421 ASP A OD2 3239 N N . ASN A 422 ? 0.3250 0.3150 0.2235 0.0197 0.0047 0.0135 422 ASN A N 3240 C CA . ASN A 422 ? 0.3228 0.3113 0.2240 0.0153 0.0073 0.0159 422 ASN A CA 3241 C C . ASN A 422 ? 0.3153 0.3144 0.2139 0.0147 0.0056 0.0165 422 ASN A C 3242 O O . ASN A 422 ? 0.2939 0.2988 0.1940 0.0120 0.0031 0.0121 422 ASN A O 3243 C CB . ASN A 422 ? 0.3143 0.2999 0.2228 0.0090 0.0076 0.0103 422 ASN A CB 3244 C CG . ASN A 422 ? 0.3161 0.2998 0.2298 0.0042 0.0115 0.0125 422 ASN A CG 3245 O OD1 . ASN A 422 ? 0.3271 0.3165 0.2385 0.0045 0.0122 0.0163 422 ASN A OD1 3246 N ND2 . ASN A 422 ? 0.3031 0.2793 0.2245 -0.0007 0.0144 0.0092 422 ASN A ND2 3247 N N . LEU A 423 ? 0.3192 0.3206 0.2131 0.0182 0.0072 0.0219 423 LEU A N 3248 C CA . LEU A 423 ? 0.3228 0.3342 0.2138 0.0185 0.0059 0.0214 423 LEU A CA 3249 C C . LEU A 423 ? 0.3139 0.3274 0.2090 0.0136 0.0070 0.0201 423 LEU A C 3250 O O . LEU A 423 ? 0.3120 0.3317 0.2074 0.0126 0.0050 0.0166 423 LEU A O 3251 C CB . LEU A 423 ? 0.3198 0.3350 0.2042 0.0239 0.0074 0.0270 423 LEU A CB 3252 C CG . LEU A 423 ? 0.3378 0.3650 0.2187 0.0250 0.0058 0.0247 423 LEU A CG 3253 C CD1 . LEU A 423 ? 0.3167 0.3506 0.1988 0.0246 0.0019 0.0177 423 LEU A CD1 3254 C CD2 . LEU A 423 ? 0.3334 0.3659 0.2067 0.0312 0.0072 0.0300 423 LEU A CD2 3255 N N . GLY A 424 ? 0.3266 0.3348 0.2256 0.0108 0.0108 0.0229 424 GLY A N 3256 C CA . GLY A 424 ? 0.3238 0.3361 0.2286 0.0061 0.0121 0.0211 424 GLY A CA 3257 C C . GLY A 424 ? 0.3128 0.3287 0.2221 0.0037 0.0081 0.0146 424 GLY A C 3258 O O . GLY A 424 ? 0.3047 0.3278 0.2154 0.0033 0.0068 0.0126 424 GLY A O 3259 N N . TYR A 425 ? 0.3134 0.3246 0.2244 0.0029 0.0064 0.0115 425 TYR A N 3260 C CA . TYR A 425 ? 0.3101 0.3260 0.2232 0.0018 0.0025 0.0058 425 TYR A CA 3261 C C . TYR A 425 ? 0.3106 0.3310 0.2183 0.0051 -0.0001 0.0056 425 TYR A C 3262 O O . TYR A 425 ? 0.3102 0.3359 0.2188 0.0052 -0.0020 0.0035 425 TYR A O 3263 C CB . TYR A 425 ? 0.3026 0.3133 0.2169 0.0011 0.0014 0.0020 425 TYR A CB 3264 C CG . TYR A 425 ? 0.3082 0.3153 0.2307 -0.0038 0.0035 -0.0012 425 TYR A CG 3265 C CD1 . TYR A 425 ? 0.3045 0.3077 0.2293 -0.0049 0.0025 -0.0069 425 TYR A CD1 3266 C CD2 . TYR A 425 ? 0.3026 0.3106 0.2315 -0.0078 0.0072 0.0004 425 TYR A CD2 3267 C CE1 . TYR A 425 ? 0.3197 0.3192 0.2536 -0.0104 0.0049 -0.0118 425 TYR A CE1 3268 C CE2 . TYR A 425 ? 0.3206 0.3252 0.2591 -0.0137 0.0101 -0.0038 425 TYR A CE2 3269 C CZ . TYR A 425 ? 0.3244 0.3243 0.2657 -0.0153 0.0089 -0.0103 425 TYR A CZ 3270 O OH . TYR A 425 ? 0.3503 0.3464 0.3027 -0.0221 0.0122 -0.0161 425 TYR A OH 3271 N N . GLN A 426 ? 0.3110 0.3296 0.2135 0.0079 0.0001 0.0075 426 GLN A N 3272 C CA . GLN A 426 ? 0.3109 0.3329 0.2101 0.0096 -0.0012 0.0062 426 GLN A CA 3273 C C . GLN A 426 ? 0.2984 0.3243 0.1975 0.0099 -0.0002 0.0069 426 GLN A C 3274 O O . GLN A 426 ? 0.2909 0.3178 0.1889 0.0106 -0.0003 0.0054 426 GLN A O 3275 C CB . GLN A 426 ? 0.3110 0.3325 0.2069 0.0118 -0.0016 0.0060 426 GLN A CB 3276 C CG . GLN A 426 ? 0.3177 0.3421 0.2112 0.0139 -0.0007 0.0079 426 GLN A CG 3277 C CD . GLN A 426 ? 0.3346 0.3618 0.2262 0.0168 -0.0017 0.0067 426 GLN A CD 3278 O OE1 . GLN A 426 ? 0.3542 0.3782 0.2462 0.0181 -0.0022 0.0067 426 GLN A OE1 3279 N NE2 . GLN A 426 ? 0.3221 0.3567 0.2124 0.0178 -0.0021 0.0048 426 GLN A NE2 3280 N N . CYS A 427 ? 0.2933 0.3207 0.1938 0.0094 0.0017 0.0090 427 CYS A N 3281 C CA . CYS A 427 ? 0.2888 0.3206 0.1895 0.0100 0.0032 0.0089 427 CYS A CA 3282 C C . CYS A 427 ? 0.2906 0.3255 0.1964 0.0090 0.0031 0.0080 427 CYS A C 3283 O O . CYS A 427 ? 0.2982 0.3358 0.2045 0.0107 0.0035 0.0068 427 CYS A O 3284 C CB . CYS A 427 ? 0.2913 0.3254 0.1899 0.0107 0.0058 0.0119 427 CYS A CB 3285 S SG . CYS A 427 ? 0.2999 0.3357 0.1916 0.0141 0.0051 0.0123 427 CYS A SG 3286 N N . GLY A 428 ? 0.2886 0.3237 0.1989 0.0066 0.0026 0.0078 428 GLY A N 3287 C CA . GLY A 428 ? 0.2763 0.3179 0.1928 0.0059 0.0018 0.0058 428 GLY A CA 3288 C C . GLY A 428 ? 0.2817 0.3288 0.2023 0.0049 0.0050 0.0070 428 GLY A C 3289 O O . GLY A 428 ? 0.2797 0.3246 0.1980 0.0042 0.0084 0.0099 428 GLY A O 3290 N N . GLY A 429 ? 0.2714 0.3268 0.1975 0.0059 0.0042 0.0049 429 GLY A N 3291 C CA . GLY A 429 ? 0.2655 0.3286 0.1972 0.0050 0.0075 0.0051 429 GLY A CA 3292 C C . GLY A 429 ? 0.2666 0.3289 0.1931 0.0080 0.0102 0.0068 429 GLY A C 3293 O O . GLY A 429 ? 0.2619 0.3183 0.1815 0.0107 0.0091 0.0067 429 GLY A O 3294 N N . TRP A 430 ? 0.2674 0.3366 0.1977 0.0072 0.0142 0.0074 430 TRP A N 3295 C CA . TRP A 430 ? 0.2647 0.3353 0.1898 0.0099 0.0173 0.0081 430 TRP A CA 3296 C C . TRP A 430 ? 0.2738 0.3372 0.1895 0.0102 0.0175 0.0103 430 TRP A C 3297 O O . TRP A 430 ? 0.2710 0.3329 0.1811 0.0132 0.0165 0.0081 430 TRP A O 3298 C CB . TRP A 430 ? 0.2671 0.3387 0.1915 0.0149 0.0158 0.0047 430 TRP A CB 3299 C CG . TRP A 430 ? 0.2646 0.3454 0.1973 0.0174 0.0158 0.0026 430 TRP A CG 3300 C CD1 . TRP A 430 ? 0.2658 0.3475 0.2016 0.0207 0.0122 0.0015 430 TRP A CD1 3301 C CD2 . TRP A 430 ? 0.2741 0.3659 0.2127 0.0178 0.0197 0.0017 430 TRP A CD2 3302 N NE1 . TRP A 430 ? 0.2721 0.3654 0.2158 0.0238 0.0129 -0.0003 430 TRP A NE1 3303 C CE2 . TRP A 430 ? 0.2753 0.3751 0.2216 0.0216 0.0176 -0.0006 430 TRP A CE2 3304 C CE3 . TRP A 430 ? 0.2740 0.3708 0.2117 0.0159 0.0250 0.0030 430 TRP A CE3 3305 C CZ2 . TRP A 430 ? 0.2712 0.3846 0.2258 0.0234 0.0205 -0.0025 430 TRP A CZ2 3306 C CZ3 . TRP A 430 ? 0.2736 0.3831 0.2190 0.0170 0.0285 0.0013 430 TRP A CZ3 3307 C CH2 . TRP A 430 ? 0.2700 0.3881 0.2246 0.0205 0.0262 -0.0018 430 TRP A CH2 3308 N N . THR A 431 ? 0.2678 0.3269 0.1824 0.0073 0.0189 0.0142 431 THR A N 3309 C CA . THR A 431 ? 0.2732 0.3277 0.1789 0.0091 0.0192 0.0173 431 THR A CA 3310 C C . THR A 431 ? 0.2814 0.3345 0.1862 0.0074 0.0244 0.0236 431 THR A C 3311 O O . THR A 431 ? 0.2815 0.3287 0.1914 0.0037 0.0257 0.0256 431 THR A O 3312 C CB . THR A 431 ? 0.2704 0.3173 0.1737 0.0093 0.0150 0.0165 431 THR A CB 3313 O OG1 . THR A 431 ? 0.2647 0.3115 0.1702 0.0099 0.0114 0.0119 431 THR A OG1 3314 C CG2 . THR A 431 ? 0.2536 0.3001 0.1481 0.0127 0.0144 0.0178 431 THR A CG2 3315 N N . ILE A 432 ? 0.2845 0.3430 0.1829 0.0102 0.0280 0.0264 432 ILE A N 3316 C CA . ILE A 432 ? 0.2994 0.3569 0.1950 0.0098 0.0346 0.0341 432 ILE A CA 3317 C C . ILE A 432 ? 0.3082 0.3686 0.2144 0.0043 0.0398 0.0347 432 ILE A C 3318 O O . ILE A 432 ? 0.3113 0.3794 0.2167 0.0047 0.0452 0.0369 432 ILE A O 3319 C CB . ILE A 432 ? 0.3117 0.3580 0.2023 0.0110 0.0350 0.0403 432 ILE A CB 3320 C CG1 . ILE A 432 ? 0.2953 0.3430 0.1765 0.0169 0.0296 0.0386 432 ILE A CG1 3321 C CG2 . ILE A 432 ? 0.3107 0.3534 0.1979 0.0112 0.0435 0.0502 432 ILE A CG2 3322 C CD1 . ILE A 432 ? 0.3166 0.3753 0.1878 0.0225 0.0301 0.0388 432 ILE A CD1 3323 N N . GLU A 433 ? 0.3089 0.3651 0.2256 -0.0008 0.0383 0.0319 433 GLU A N 3324 C CA . GLU A 433 ? 0.3182 0.3809 0.2478 -0.0065 0.0418 0.0296 433 GLU A CA 3325 C C . GLU A 433 ? 0.3075 0.3799 0.2430 -0.0052 0.0361 0.0218 433 GLU A C 3326 O O . GLU A 433 ? 0.3079 0.3777 0.2385 -0.0013 0.0300 0.0188 433 GLU A O 3327 C CB . GLU A 433 ? 0.3304 0.3847 0.2691 -0.0133 0.0437 0.0298 433 GLU A CB 3328 C CG . GLU A 433 ? 0.3623 0.4030 0.2953 -0.0138 0.0499 0.0385 433 GLU A CG 3329 C CD . GLU A 433 ? 0.4151 0.4575 0.3469 -0.0150 0.0599 0.0461 433 GLU A CD 3330 O OE1 . GLU A 433 ? 0.4244 0.4795 0.3628 -0.0174 0.0630 0.0437 433 GLU A OE1 3331 O OE2 . GLU A 433 ? 0.4478 0.4791 0.3715 -0.0128 0.0653 0.0552 433 GLU A OE2 3332 N N . TRP A 434 ? 0.3034 0.3870 0.2495 -0.0079 0.0388 0.0190 434 TRP A N 3333 C CA . TRP A 434 ? 0.2926 0.3862 0.2457 -0.0057 0.0337 0.0123 434 TRP A CA 3334 C C . TRP A 434 ? 0.2946 0.3838 0.2498 -0.0061 0.0268 0.0086 434 TRP A C 3335 O O . TRP A 434 ? 0.2807 0.3694 0.2317 -0.0009 0.0214 0.0062 434 TRP A O 3336 C CB . TRP A 434 ? 0.2935 0.4015 0.2604 -0.0096 0.0380 0.0098 434 TRP A CB 3337 C CG . TRP A 434 ? 0.2817 0.4029 0.2573 -0.0064 0.0330 0.0032 434 TRP A CG 3338 C CD1 . TRP A 434 ? 0.2702 0.3931 0.2409 0.0016 0.0286 0.0012 434 TRP A CD1 3339 C CD2 . TRP A 434 ? 0.2799 0.4152 0.2711 -0.0106 0.0324 -0.0022 434 TRP A CD2 3340 N NE1 . TRP A 434 ? 0.2633 0.3997 0.2442 0.0040 0.0251 -0.0037 434 TRP A NE1 3341 C CE2 . TRP A 434 ? 0.2729 0.4190 0.2667 -0.0033 0.0268 -0.0065 434 TRP A CE2 3342 C CE3 . TRP A 434 ? 0.2826 0.4227 0.2868 -0.0200 0.0363 -0.0044 434 TRP A CE3 3343 C CZ2 . TRP A 434 ? 0.2758 0.4401 0.2838 -0.0038 0.0239 -0.0127 434 TRP A CZ2 3344 C CZ3 . TRP A 434 ? 0.2768 0.4353 0.2966 -0.0222 0.0337 -0.0122 434 TRP A CZ3 3345 C CH2 . TRP A 434 ? 0.2799 0.4518 0.3012 -0.0136 0.0270 -0.0162 434 TRP A CH2 3346 N N . GLN A 435 ? 0.2982 0.3834 0.2596 -0.0124 0.0278 0.0081 435 GLN A N 3347 C CA . GLN A 435 ? 0.2998 0.3833 0.2640 -0.0133 0.0218 0.0034 435 GLN A CA 3348 C C . GLN A 435 ? 0.3043 0.3736 0.2573 -0.0109 0.0189 0.0059 435 GLN A C 3349 O O . GLN A 435 ? 0.3128 0.3801 0.2662 -0.0110 0.0142 0.0024 435 GLN A O 3350 C CB . GLN A 435 ? 0.3046 0.3916 0.2823 -0.0218 0.0243 -0.0007 435 GLN A CB 3351 C CG . GLN A 435 ? 0.2855 0.3918 0.2777 -0.0244 0.0247 -0.0066 435 GLN A CG 3352 C CD . GLN A 435 ? 0.2928 0.4115 0.2859 -0.0182 0.0163 -0.0121 435 GLN A CD 3353 O OE1 . GLN A 435 ? 0.2745 0.3892 0.2629 -0.0160 0.0104 -0.0144 435 GLN A OE1 3354 N NE2 . GLN A 435 ? 0.2675 0.4016 0.2662 -0.0145 0.0162 -0.0138 435 GLN A NE2 3355 N N . GLY A 436 ? 0.3104 0.3720 0.2533 -0.0080 0.0214 0.0115 436 GLY A N 3356 C CA . GLY A 436 ? 0.3093 0.3588 0.2435 -0.0064 0.0200 0.0143 436 GLY A CA 3357 C C . GLY A 436 ? 0.3198 0.3606 0.2580 -0.0114 0.0243 0.0165 436 GLY A C 3358 O O . GLY A 436 ? 0.3248 0.3683 0.2720 -0.0167 0.0293 0.0166 436 GLY A O 3359 N N . ASP A 437 ? 0.3248 0.3549 0.2575 -0.0099 0.0228 0.0181 437 ASP A N 3360 C CA . ASP A 437 ? 0.3414 0.3600 0.2767 -0.0133 0.0279 0.0212 437 ASP A CA 3361 C C . ASP A 437 ? 0.3387 0.3478 0.2689 -0.0104 0.0244 0.0204 437 ASP A C 3362 O O . ASP A 437 ? 0.3304 0.3430 0.2552 -0.0064 0.0186 0.0178 437 ASP A O 3363 C CB . ASP A 437 ? 0.3522 0.3667 0.2816 -0.0114 0.0349 0.0304 437 ASP A CB 3364 C CG . ASP A 437 ? 0.3956 0.3982 0.3310 -0.0164 0.0432 0.0348 437 ASP A CG 3365 O OD1 . ASP A 437 ? 0.4378 0.4343 0.3824 -0.0218 0.0433 0.0295 437 ASP A OD1 3366 O OD2 . ASP A 437 ? 0.4354 0.4345 0.3659 -0.0148 0.0501 0.0434 437 ASP A OD2 3367 N N . THR A 438 ? 0.3423 0.3388 0.2748 -0.0124 0.0287 0.0227 438 THR A N 3368 C CA . THR A 438 ? 0.3365 0.3237 0.2658 -0.0096 0.0262 0.0213 438 THR A CA 3369 C C . THR A 438 ? 0.3486 0.3269 0.2678 -0.0027 0.0291 0.0305 438 THR A C 3370 O O . THR A 438 ? 0.3614 0.3354 0.2783 -0.0020 0.0354 0.0383 438 THR A O 3371 C CB . THR A 438 ? 0.3393 0.3183 0.2794 -0.0162 0.0288 0.0155 438 THR A CB 3372 O OG1 . THR A 438 ? 0.3439 0.3140 0.2804 -0.0126 0.0265 0.0136 438 THR A OG1 3373 C CG2 . THR A 438 ? 0.3504 0.3184 0.2968 -0.0211 0.0386 0.0209 438 THR A CG2 3374 N N . GLY A 439 ? 0.3438 0.3209 0.2567 0.0029 0.0246 0.0296 439 GLY A N 3375 C CA . GLY A 439 ? 0.3612 0.3307 0.2660 0.0104 0.0267 0.0371 439 GLY A CA 3376 C C . GLY A 439 ? 0.3666 0.3466 0.2615 0.0166 0.0247 0.0417 439 GLY A C 3377 O O . GLY A 439 ? 0.3541 0.3460 0.2483 0.0156 0.0205 0.0372 439 GLY A O 3378 N N . ARG A 440 ? 0.3828 0.3584 0.2701 0.0235 0.0281 0.0505 440 ARG A N 3379 C CA . ARG A 440 ? 0.4004 0.3879 0.2775 0.0308 0.0255 0.0538 440 ARG A CA 3380 C C . ARG A 440 ? 0.3986 0.3923 0.2722 0.0299 0.0295 0.0584 440 ARG A C 3381 O O . ARG A 440 ? 0.4182 0.4086 0.2850 0.0347 0.0350 0.0680 440 ARG A O 3382 C CB . ARG A 440 ? 0.4150 0.3979 0.2846 0.0408 0.0260 0.0605 440 ARG A CB 3383 C CG . ARG A 440 ? 0.4721 0.4705 0.3314 0.0493 0.0224 0.0626 440 ARG A CG 3384 C CD . ARG A 440 ? 0.5675 0.5685 0.4235 0.0580 0.0184 0.0626 440 ARG A CD 3385 N NE . ARG A 440 ? 0.6286 0.6449 0.4869 0.0563 0.0112 0.0522 440 ARG A NE 3386 C CZ . ARG A 440 ? 0.6251 0.6399 0.4912 0.0508 0.0082 0.0439 440 ARG A CZ 3387 N NH1 . ARG A 440 ? 0.6184 0.6186 0.4906 0.0468 0.0106 0.0433 440 ARG A NH1 3388 N NH2 . ARG A 440 ? 0.6004 0.6289 0.4680 0.0493 0.0032 0.0358 440 ARG A NH2 3389 N N . THR A 441 ? 0.3855 0.3883 0.2636 0.0243 0.0273 0.0518 441 THR A N 3390 C CA . THR A 441 ? 0.3803 0.3895 0.2576 0.0222 0.0315 0.0543 441 THR A CA 3391 C C . THR A 441 ? 0.3684 0.3920 0.2361 0.0282 0.0289 0.0539 441 THR A C 3392 O O . THR A 441 ? 0.3650 0.3952 0.2296 0.0283 0.0326 0.0565 441 THR A O 3393 C CB . THR A 441 ? 0.3729 0.3857 0.2609 0.0142 0.0305 0.0468 441 THR A CB 3394 O OG1 . THR A 441 ? 0.3751 0.3948 0.2637 0.0145 0.0234 0.0386 441 THR A OG1 3395 C CG2 . THR A 441 ? 0.3800 0.3817 0.2786 0.0076 0.0331 0.0455 441 THR A CG2 3396 N N . THR A 442 ? 0.3517 0.3814 0.2154 0.0326 0.0227 0.0496 442 THR A N 3397 C CA . THR A 442 ? 0.3422 0.3873 0.1988 0.0370 0.0195 0.0460 442 THR A CA 3398 C C . THR A 442 ? 0.3439 0.3948 0.1964 0.0429 0.0140 0.0435 442 THR A C 3399 O O . THR A 442 ? 0.3432 0.3856 0.1970 0.0449 0.0135 0.0463 442 THR A O 3400 C CB . THR A 442 ? 0.3251 0.3771 0.1873 0.0316 0.0177 0.0371 442 THR A CB 3401 O OG1 . THR A 442 ? 0.3307 0.3966 0.1860 0.0354 0.0166 0.0338 442 THR A OG1 3402 C CG2 . THR A 442 ? 0.2900 0.3393 0.1594 0.0277 0.0130 0.0293 442 THR A CG2 3403 N N . VAL A 443 ? 0.3406 0.4070 0.1887 0.0459 0.0103 0.0375 443 VAL A N 3404 C CA . VAL A 443 ? 0.3391 0.4152 0.1857 0.0505 0.0049 0.0328 443 VAL A CA 3405 C C . VAL A 443 ? 0.3268 0.4010 0.1832 0.0437 0.0015 0.0231 443 VAL A C 3406 O O . VAL A 443 ? 0.3240 0.3992 0.1848 0.0380 0.0017 0.0168 443 VAL A O 3407 C CB . VAL A 443 ? 0.3391 0.4352 0.1775 0.0565 0.0022 0.0290 443 VAL A CB 3408 C CG1 . VAL A 443 ? 0.3313 0.4401 0.1710 0.0600 -0.0038 0.0219 443 VAL A CG1 3409 C CG2 . VAL A 443 ? 0.3595 0.4582 0.1857 0.0651 0.0059 0.0403 443 VAL A CG2 3410 N N . GLY A 444 ? 0.3244 0.3955 0.1838 0.0450 -0.0008 0.0226 444 GLY A N 3411 C CA . GLY A 444 ? 0.3170 0.3850 0.1847 0.0390 -0.0027 0.0154 444 GLY A CA 3412 C C . GLY A 444 ? 0.3231 0.3895 0.1928 0.0420 -0.0047 0.0156 444 GLY A C 3413 O O . GLY A 444 ? 0.3317 0.3998 0.1965 0.0496 -0.0050 0.0210 444 GLY A O 3414 N N . THR A 445 ? 0.3158 0.3793 0.1922 0.0368 -0.0056 0.0099 445 THR A N 3415 C CA . THR A 445 ? 0.3151 0.3784 0.1946 0.0386 -0.0071 0.0083 445 THR A CA 3416 C C . THR A 445 ? 0.3121 0.3622 0.1958 0.0332 -0.0055 0.0081 445 THR A C 3417 O O . THR A 445 ? 0.3065 0.3554 0.1934 0.0273 -0.0050 0.0042 445 THR A O 3418 C CB . THR A 445 ? 0.3062 0.3849 0.1897 0.0378 -0.0097 -0.0004 445 THR A CB 3419 O OG1 . THR A 445 ? 0.3136 0.4076 0.1932 0.0432 -0.0120 -0.0015 445 THR A OG1 3420 C CG2 . THR A 445 ? 0.3041 0.3845 0.1914 0.0400 -0.0108 -0.0020 445 THR A CG2 3421 N N . THR A 446 ? 0.3125 0.3528 0.1960 0.0356 -0.0044 0.0123 446 THR A N 3422 C CA . THR A 446 ? 0.3136 0.3440 0.2008 0.0311 -0.0034 0.0107 446 THR A CA 3423 C C . THR A 446 ? 0.3045 0.3400 0.1947 0.0302 -0.0048 0.0050 446 THR A C 3424 O O . THR A 446 ? 0.3060 0.3522 0.1968 0.0330 -0.0062 0.0024 446 THR A O 3425 C CB . THR A 446 ? 0.3245 0.3421 0.2117 0.0331 -0.0012 0.0150 446 THR A CB 3426 O OG1 . THR A 446 ? 0.3436 0.3617 0.2297 0.0401 -0.0017 0.0164 446 THR A OG1 3427 C CG2 . THR A 446 ? 0.3138 0.3255 0.1988 0.0330 0.0018 0.0214 446 THR A CG2 3428 N N . ILE A 447 ? 0.2997 0.3294 0.1919 0.0264 -0.0042 0.0028 447 ILE A N 3429 C CA . ILE A 447 ? 0.2981 0.3319 0.1922 0.0258 -0.0043 -0.0016 447 ILE A CA 3430 C C . ILE A 447 ? 0.3064 0.3427 0.2012 0.0318 -0.0048 -0.0020 447 ILE A C 3431 O O . ILE A 447 ? 0.3067 0.3534 0.2039 0.0331 -0.0053 -0.0055 447 ILE A O 3432 C CB . ILE A 447 ? 0.2954 0.3233 0.1895 0.0219 -0.0036 -0.0032 447 ILE A CB 3433 C CG1 . ILE A 447 ? 0.2766 0.3047 0.1702 0.0177 -0.0031 -0.0026 447 ILE A CG1 3434 C CG2 . ILE A 447 ? 0.2905 0.3223 0.1853 0.0222 -0.0029 -0.0069 447 ILE A CG2 3435 C CD1 . ILE A 447 ? 0.2813 0.3048 0.1739 0.0155 -0.0032 -0.0028 447 ILE A CD1 3436 N N . LEU A 448 ? 0.3152 0.3422 0.2090 0.0355 -0.0042 0.0012 448 LEU A N 3437 C CA . LEU A 448 ? 0.3187 0.3461 0.2129 0.0430 -0.0043 0.0018 448 LEU A CA 3438 C C . LEU A 448 ? 0.3253 0.3660 0.2186 0.0488 -0.0062 0.0031 448 LEU A C 3439 O O . LEU A 448 ? 0.3243 0.3755 0.2202 0.0530 -0.0074 -0.0002 448 LEU A O 3440 C CB . LEU A 448 ? 0.3243 0.3362 0.2177 0.0460 -0.0020 0.0061 448 LEU A CB 3441 C CG . LEU A 448 ? 0.3340 0.3430 0.2271 0.0556 -0.0013 0.0086 448 LEU A CG 3442 C CD1 . LEU A 448 ? 0.3289 0.3424 0.2254 0.0574 -0.0018 0.0021 448 LEU A CD1 3443 C CD2 . LEU A 448 ? 0.3558 0.3463 0.2484 0.0577 0.0026 0.0140 448 LEU A CD2 3444 N N . GLU A 449 ? 0.3259 0.3681 0.2157 0.0493 -0.0066 0.0072 449 GLU A N 3445 C CA . GLU A 449 ? 0.3371 0.3944 0.2250 0.0552 -0.0090 0.0078 449 GLU A CA 3446 C C . GLU A 449 ? 0.3168 0.3905 0.2097 0.0510 -0.0109 -0.0004 449 GLU A C 3447 O O . GLU A 449 ? 0.3165 0.4061 0.2115 0.0560 -0.0133 -0.0036 449 GLU A O 3448 C CB . GLU A 449 ? 0.3431 0.3992 0.2254 0.0556 -0.0086 0.0131 449 GLU A CB 3449 C CG . GLU A 449 ? 0.3768 0.4186 0.2542 0.0610 -0.0056 0.0225 449 GLU A CG 3450 C CD . GLU A 449 ? 0.3891 0.4292 0.2611 0.0599 -0.0038 0.0279 449 GLU A CD 3451 O OE1 . GLU A 449 ? 0.3825 0.4236 0.2562 0.0521 -0.0035 0.0247 449 GLU A OE1 3452 O OE2 . GLU A 449 ? 0.4861 0.5243 0.3518 0.0677 -0.0021 0.0361 449 GLU A OE2 3453 N N . ALA A 450 ? 0.3014 0.3716 0.1966 0.0420 -0.0095 -0.0039 450 ALA A N 3454 C CA . ALA A 450 ? 0.2936 0.3752 0.1944 0.0366 -0.0094 -0.0112 450 ALA A CA 3455 C C . ALA A 450 ? 0.2880 0.3756 0.1937 0.0378 -0.0088 -0.0152 450 ALA A C 3456 O O . ALA A 450 ? 0.2874 0.3909 0.1989 0.0374 -0.0094 -0.0211 450 ALA A O 3457 C CB . ALA A 450 ? 0.2869 0.3595 0.1880 0.0282 -0.0069 -0.0120 450 ALA A CB 3458 N N . VAL A 451 ? 0.2831 0.3594 0.1873 0.0393 -0.0075 -0.0127 451 VAL A N 3459 C CA . VAL A 451 ? 0.2863 0.3678 0.1945 0.0413 -0.0066 -0.0164 451 VAL A CA 3460 C C . VAL A 451 ? 0.2946 0.3895 0.2052 0.0504 -0.0091 -0.0172 451 VAL A C 3461 O O . VAL A 451 ? 0.2890 0.3998 0.2060 0.0506 -0.0091 -0.0230 451 VAL A O 3462 C CB . VAL A 451 ? 0.2924 0.3593 0.1978 0.0418 -0.0049 -0.0146 451 VAL A CB 3463 C CG1 . VAL A 451 ? 0.2984 0.3719 0.2074 0.0460 -0.0039 -0.0186 451 VAL A CG1 3464 C CG2 . VAL A 451 ? 0.2853 0.3443 0.1888 0.0338 -0.0029 -0.0149 451 VAL A CG2 3465 N N . LYS A 452 ? 0.3054 0.3945 0.2109 0.0582 -0.0107 -0.0112 452 LYS A N 3466 C CA . LYS A 452 ? 0.3183 0.4195 0.2241 0.0693 -0.0134 -0.0099 452 LYS A CA 3467 C C . LYS A 452 ? 0.3130 0.4377 0.2223 0.0697 -0.0166 -0.0150 452 LYS A C 3468 O O . LYS A 452 ? 0.3143 0.4572 0.2283 0.0765 -0.0189 -0.0188 452 LYS A O 3469 C CB . LYS A 452 ? 0.3246 0.4119 0.2228 0.0772 -0.0132 -0.0005 452 LYS A CB 3470 C CG . LYS A 452 ? 0.3682 0.4347 0.2657 0.0781 -0.0099 0.0022 452 LYS A CG 3471 C CD . LYS A 452 ? 0.4216 0.4692 0.3130 0.0799 -0.0076 0.0109 452 LYS A CD 3472 C CE . LYS A 452 ? 0.4966 0.5405 0.3846 0.0933 -0.0069 0.0181 452 LYS A CE 3473 N NZ . LYS A 452 ? 0.5390 0.5573 0.4245 0.0933 -0.0019 0.0248 452 LYS A NZ 3474 N N . ALA A 453 ? 0.3051 0.4306 0.2131 0.0625 -0.0168 -0.0163 453 ALA A N 3475 C CA . ALA A 453 ? 0.3012 0.4484 0.2134 0.0606 -0.0194 -0.0235 453 ALA A CA 3476 C C . ALA A 453 ? 0.2929 0.4523 0.2162 0.0520 -0.0176 -0.0336 453 ALA A C 3477 O O . ALA A 453 ? 0.2956 0.4763 0.2255 0.0507 -0.0197 -0.0418 453 ALA A O 3478 C CB . ALA A 453 ? 0.2884 0.4311 0.1955 0.0561 -0.0195 -0.0220 453 ALA A CB 3479 N N . ALA A 454 ? 0.2869 0.4341 0.2125 0.0462 -0.0134 -0.0335 454 ALA A N 3480 C CA . ALA A 454 ? 0.2826 0.4372 0.2176 0.0370 -0.0096 -0.0411 454 ALA A CA 3481 C C . ALA A 454 ? 0.2912 0.4584 0.2333 0.0403 -0.0087 -0.0452 454 ALA A C 3482 O O . ALA A 454 ? 0.2938 0.4783 0.2465 0.0353 -0.0070 -0.0535 454 ALA A O 3483 C CB . ALA A 454 ? 0.2804 0.4146 0.2121 0.0284 -0.0048 -0.0379 454 ALA A CB 3484 N N . VAL A 455 ? 0.2911 0.4498 0.2285 0.0485 -0.0094 -0.0400 455 VAL A N 3485 C CA . VAL A 455 ? 0.2921 0.4595 0.2355 0.0515 -0.0074 -0.0436 455 VAL A CA 3486 C C . VAL A 455 ? 0.2920 0.4848 0.2428 0.0600 -0.0112 -0.0486 455 VAL A C 3487 O O . VAL A 455 ? 0.2892 0.4896 0.2370 0.0675 -0.0162 -0.0467 455 VAL A O 3488 C CB . VAL A 455 ? 0.2973 0.4461 0.2337 0.0571 -0.0062 -0.0379 455 VAL A CB 3489 C CG1 . VAL A 455 ? 0.2908 0.4196 0.2214 0.0484 -0.0026 -0.0350 455 VAL A CG1 3490 C CG2 . VAL A 455 ? 0.3089 0.4497 0.2385 0.0683 -0.0101 -0.0311 455 VAL A CG2 3491 N N . ASP A 456 ? 0.2831 0.4905 0.2434 0.0594 -0.0086 -0.0549 456 ASP A N 3492 C CA . ASP A 456 ? 0.2876 0.5204 0.2562 0.0688 -0.0118 -0.0602 456 ASP A CA 3493 C C . ASP A 456 ? 0.2922 0.5187 0.2526 0.0848 -0.0162 -0.0526 456 ASP A C 3494 O O . ASP A 456 ? 0.2991 0.5011 0.2507 0.0875 -0.0145 -0.0454 456 ASP A O 3495 C CB . ASP A 456 ? 0.2840 0.5269 0.2623 0.0657 -0.0066 -0.0663 456 ASP A CB 3496 C CG . ASP A 456 ? 0.2986 0.5735 0.2894 0.0727 -0.0092 -0.0743 456 ASP A CG 3497 O OD1 . ASP A 456 ? 0.3224 0.6190 0.3253 0.0645 -0.0083 -0.0835 456 ASP A OD1 3498 O OD2 . ASP A 456 ? 0.3026 0.5818 0.2923 0.0866 -0.0119 -0.0721 456 ASP A OD2 3499 N N . PRO A 457 ? 0.2926 0.5414 0.2559 0.0957 -0.0218 -0.0543 457 PRO A N 3500 C CA . PRO A 457 ? 0.3062 0.5498 0.2618 0.1128 -0.0252 -0.0460 457 PRO A CA 3501 C C . PRO A 457 ? 0.3123 0.5440 0.2680 0.1202 -0.0220 -0.0437 457 PRO A C 3502 O O . PRO A 457 ? 0.3243 0.5373 0.2714 0.1307 -0.0221 -0.0349 457 PRO A O 3503 C CB . PRO A 457 ? 0.3044 0.5824 0.2663 0.1227 -0.0313 -0.0512 457 PRO A CB 3504 C CG . PRO A 457 ? 0.2947 0.5970 0.2714 0.1099 -0.0301 -0.0645 457 PRO A CG 3505 C CD . PRO A 457 ? 0.2789 0.5596 0.2528 0.0930 -0.0251 -0.0642 457 PRO A CD 3506 N N . SER A 458 ? 0.3056 0.5478 0.2713 0.1147 -0.0183 -0.0519 458 SER A N 3507 C CA . SER A 458 ? 0.3095 0.5425 0.2758 0.1214 -0.0149 -0.0516 458 SER A CA 3508 C C . SER A 458 ? 0.3075 0.5092 0.2656 0.1137 -0.0100 -0.0478 458 SER A C 3509 O O . SER A 458 ? 0.3258 0.5159 0.2826 0.1195 -0.0072 -0.0476 458 SER A O 3510 C CB . SER A 458 ? 0.3060 0.5660 0.2864 0.1199 -0.0127 -0.0620 458 SER A CB 3511 O OG . SER A 458 ? 0.2978 0.5567 0.2820 0.1033 -0.0073 -0.0670 458 SER A OG 3512 N N . THR A 459 ? 0.2939 0.4834 0.2470 0.1012 -0.0091 -0.0458 459 THR A N 3513 C CA . THR A 459 ? 0.2921 0.4553 0.2376 0.0940 -0.0054 -0.0426 459 THR A CA 3514 C C . THR A 459 ? 0.3034 0.4427 0.2396 0.1011 -0.0067 -0.0343 459 THR A C 3515 O O . THR A 459 ? 0.3081 0.4433 0.2395 0.1022 -0.0095 -0.0285 459 THR A O 3516 C CB . THR A 459 ? 0.2789 0.4385 0.2229 0.0791 -0.0038 -0.0431 459 THR A CB 3517 O OG1 . THR A 459 ? 0.2749 0.4535 0.2281 0.0716 -0.0007 -0.0504 459 THR A OG1 3518 C CG2 . THR A 459 ? 0.2707 0.4058 0.2064 0.0730 -0.0010 -0.0397 459 THR A CG2 3519 N N . VAL A 460 ? 0.3169 0.4408 0.2511 0.1059 -0.0040 -0.0342 460 VAL A N 3520 C CA . VAL A 460 ? 0.3269 0.4254 0.2539 0.1106 -0.0036 -0.0272 460 VAL A CA 3521 C C . VAL A 460 ? 0.3256 0.4073 0.2474 0.0980 -0.0021 -0.0260 460 VAL A C 3522 O O . VAL A 460 ? 0.3217 0.4022 0.2438 0.0901 0.0002 -0.0312 460 VAL A O 3523 C CB . VAL A 460 ? 0.3422 0.4291 0.2703 0.1202 -0.0008 -0.0288 460 VAL A CB 3524 C CG1 . VAL A 460 ? 0.3540 0.4125 0.2761 0.1238 0.0009 -0.0216 460 VAL A CG1 3525 C CG2 . VAL A 460 ? 0.3428 0.4484 0.2768 0.1343 -0.0023 -0.0301 460 VAL A CG2 3526 N N . VAL A 461 ? 0.3316 0.4022 0.2481 0.0969 -0.0034 -0.0188 461 VAL A N 3527 C CA . VAL A 461 ? 0.3298 0.3853 0.2421 0.0862 -0.0023 -0.0173 461 VAL A CA 3528 C C . VAL A 461 ? 0.3472 0.3784 0.2564 0.0888 0.0001 -0.0136 461 VAL A C 3529 O O . VAL A 461 ? 0.3549 0.3780 0.2621 0.0969 0.0005 -0.0066 461 VAL A O 3530 C CB . VAL A 461 ? 0.3272 0.3883 0.2368 0.0810 -0.0047 -0.0132 461 VAL A CB 3531 C CG1 . VAL A 461 ? 0.2985 0.3455 0.2046 0.0707 -0.0035 -0.0120 461 VAL A CG1 3532 C CG2 . VAL A 461 ? 0.3007 0.3849 0.2150 0.0775 -0.0064 -0.0182 461 VAL A CG2 3533 N N . VAL A 462 ? 0.3529 0.3731 0.2622 0.0823 0.0023 -0.0185 462 VAL A N 3534 C CA . VAL A 462 ? 0.3648 0.3622 0.2733 0.0822 0.0051 -0.0174 462 VAL A CA 3535 C C . VAL A 462 ? 0.3652 0.3556 0.2716 0.0712 0.0049 -0.0162 462 VAL A C 3536 O O . VAL A 462 ? 0.3575 0.3566 0.2630 0.0634 0.0034 -0.0203 462 VAL A O 3537 C CB . VAL A 462 ? 0.3775 0.3685 0.2890 0.0840 0.0077 -0.0260 462 VAL A CB 3538 C CG1 . VAL A 462 ? 0.3812 0.3487 0.2939 0.0817 0.0111 -0.0271 462 VAL A CG1 3539 C CG2 . VAL A 462 ? 0.3695 0.3672 0.2839 0.0962 0.0083 -0.0269 462 VAL A CG2 3540 N N . PHE A 463 ? 0.3720 0.3472 0.2776 0.0711 0.0068 -0.0101 463 PHE A N 3541 C CA . PHE A 463 ? 0.3759 0.3445 0.2811 0.0610 0.0071 -0.0101 463 PHE A CA 3542 C C . PHE A 463 ? 0.3883 0.3392 0.2975 0.0578 0.0107 -0.0150 463 PHE A C 3543 O O . PHE A 463 ? 0.4022 0.3378 0.3136 0.0635 0.0146 -0.0125 463 PHE A O 3544 C CB . PHE A 463 ? 0.3729 0.3400 0.2753 0.0605 0.0072 -0.0007 463 PHE A CB 3545 C CG . PHE A 463 ? 0.3789 0.3393 0.2823 0.0507 0.0081 -0.0008 463 PHE A CG 3546 C CD1 . PHE A 463 ? 0.3657 0.3366 0.2688 0.0430 0.0052 -0.0055 463 PHE A CD1 3547 C CD2 . PHE A 463 ? 0.4193 0.3633 0.3245 0.0495 0.0125 0.0040 463 PHE A CD2 3548 C CE1 . PHE A 463 ? 0.3826 0.3498 0.2874 0.0351 0.0057 -0.0060 463 PHE A CE1 3549 C CE2 . PHE A 463 ? 0.4009 0.3413 0.3088 0.0401 0.0136 0.0030 463 PHE A CE2 3550 C CZ . PHE A 463 ? 0.3737 0.3269 0.2816 0.0333 0.0097 -0.0024 463 PHE A CZ 3551 N N . ALA A 464 ? 0.3876 0.3412 0.2981 0.0490 0.0095 -0.0223 464 ALA A N 3552 C CA . ALA A 464 ? 0.4041 0.3438 0.3198 0.0436 0.0123 -0.0287 464 ALA A CA 3553 C C . ALA A 464 ? 0.4012 0.3478 0.3171 0.0339 0.0098 -0.0311 464 ALA A C 3554 O O . ALA A 464 ? 0.3951 0.3564 0.3074 0.0317 0.0061 -0.0344 464 ALA A O 3555 C CB . ALA A 464 ? 0.4081 0.3471 0.3258 0.0455 0.0128 -0.0398 464 ALA A CB 3556 N N . GLU A 465 ? 0.4062 0.3426 0.3264 0.0285 0.0125 -0.0287 465 GLU A N 3557 C CA . GLU A 465 ? 0.4073 0.3520 0.3285 0.0203 0.0101 -0.0302 465 GLU A CA 3558 C C . GLU A 465 ? 0.4026 0.3553 0.3261 0.0152 0.0073 -0.0425 465 GLU A C 3559 O O . GLU A 465 ? 0.3958 0.3631 0.3154 0.0131 0.0031 -0.0439 465 GLU A O 3560 C CB . GLU A 465 ? 0.4159 0.3494 0.3425 0.0156 0.0143 -0.0252 465 GLU A CB 3561 C CG . GLU A 465 ? 0.4324 0.3769 0.3609 0.0080 0.0117 -0.0268 465 GLU A CG 3562 C CD . GLU A 465 ? 0.4811 0.4175 0.4146 0.0034 0.0163 -0.0209 465 GLU A CD 3563 O OE1 . GLU A 465 ? 0.5118 0.4358 0.4440 0.0074 0.0212 -0.0120 465 GLU A OE1 3564 O OE2 . GLU A 465 ? 0.5188 0.4627 0.4575 -0.0038 0.0153 -0.0249 465 GLU A OE2 3565 N N . ASN A 466 ? 0.4192 0.3623 0.3487 0.0138 0.0099 -0.0517 466 ASN A N 3566 C CA . ASN A 466 ? 0.4181 0.3702 0.3496 0.0094 0.0071 -0.0651 466 ASN A CA 3567 C C . ASN A 466 ? 0.4289 0.3750 0.3614 0.0135 0.0089 -0.0743 466 ASN A C 3568 O O . ASN A 466 ? 0.4347 0.3705 0.3755 0.0096 0.0120 -0.0842 466 ASN A O 3569 C CB A ASN A 466 ? 0.4282 0.3789 0.3693 0.0000 0.0080 -0.0715 466 ASN A CB 3570 C CB B ASN A 466 ? 0.4195 0.3685 0.3609 0.0002 0.0085 -0.0712 466 ASN A CB 3571 C CG A ASN A 466 ? 0.4422 0.3997 0.3830 -0.0035 0.0066 -0.0628 466 ASN A CG 3572 C CG B ASN A 466 ? 0.4072 0.3727 0.3497 -0.0043 0.0036 -0.0843 466 ASN A CG 3573 O OD1 A ASN A 466 ? 0.4762 0.4231 0.4234 -0.0074 0.0110 -0.0581 466 ASN A OD1 3574 O OD1 B ASN A 466 ? 0.3902 0.3713 0.3238 -0.0005 -0.0011 -0.0851 466 ASN A OD1 3575 N ND2 A ASN A 466 ? 0.4437 0.4182 0.3768 -0.0017 0.0013 -0.0603 466 ASN A ND2 3576 N ND2 B ASN A 466 ? 0.4119 0.3748 0.3656 -0.0122 0.0052 -0.0948 466 ASN A ND2 3577 N N . PRO A 467 ? 0.4225 0.3754 0.3476 0.0211 0.0076 -0.0719 467 PRO A N 3578 C CA . PRO A 467 ? 0.4442 0.3915 0.3705 0.0260 0.0099 -0.0804 467 PRO A CA 3579 C C . PRO A 467 ? 0.4523 0.4109 0.3781 0.0227 0.0073 -0.0953 467 PRO A C 3580 O O . PRO A 467 ? 0.4516 0.4274 0.3717 0.0200 0.0028 -0.0962 467 PRO A O 3581 C CB . PRO A 467 ? 0.4328 0.3883 0.3520 0.0344 0.0090 -0.0732 467 PRO A CB 3582 C CG . PRO A 467 ? 0.4173 0.3885 0.3301 0.0317 0.0050 -0.0664 467 PRO A CG 3583 C CD . PRO A 467 ? 0.4116 0.3777 0.3282 0.0248 0.0047 -0.0628 467 PRO A CD 3584 N N . ASP A 468 ? 0.4701 0.4195 0.4012 0.0235 0.0102 -0.1071 468 ASP A N 3585 C CA . ASP A 468 ? 0.4755 0.4380 0.4047 0.0217 0.0076 -0.1224 468 ASP A CA 3586 C C . ASP A 468 ? 0.4678 0.4444 0.3868 0.0293 0.0062 -0.1224 468 ASP A C 3587 O O . ASP A 468 ? 0.4571 0.4320 0.3730 0.0357 0.0077 -0.1120 468 ASP A O 3588 C CB . ASP A 468 ? 0.5025 0.4518 0.4423 0.0180 0.0111 -0.1382 468 ASP A CB 3589 C CG . ASP A 468 ? 0.5326 0.4620 0.4764 0.0251 0.0173 -0.1387 468 ASP A CG 3590 O OD1 . ASP A 468 ? 0.5780 0.4896 0.5325 0.0215 0.0221 -0.1479 468 ASP A OD1 3591 O OD2 . ASP A 468 ? 0.5560 0.4873 0.4936 0.0342 0.0178 -0.1307 468 ASP A OD2 3592 N N . ALA A 469 ? 0.4588 0.4514 0.3728 0.0286 0.0033 -0.1342 469 ALA A N 3593 C CA . ALA A 469 ? 0.4525 0.4608 0.3560 0.0349 0.0026 -0.1348 469 ALA A CA 3594 C C . ALA A 469 ? 0.4583 0.4578 0.3640 0.0424 0.0073 -0.1365 469 ALA A C 3595 O O . ALA A 469 ? 0.4501 0.4580 0.3500 0.0481 0.0082 -0.1294 469 ALA A O 3596 C CB . ALA A 469 ? 0.4549 0.4807 0.3526 0.0333 -0.0007 -0.1488 469 ALA A CB 3597 N N . GLU A 470 ? 0.4729 0.4555 0.3880 0.0424 0.0106 -0.1461 470 GLU A N 3598 C CA . GLU A 470 ? 0.4844 0.4575 0.4024 0.0509 0.0153 -0.1491 470 GLU A CA 3599 C C . GLU A 470 ? 0.4734 0.4379 0.3927 0.0570 0.0174 -0.1329 470 GLU A C 3600 O O . GLU A 470 ? 0.4742 0.4446 0.3913 0.0653 0.0191 -0.1306 470 GLU A O 3601 C CB . GLU A 470 ? 0.5046 0.4582 0.4332 0.0493 0.0193 -0.1629 470 GLU A CB 3602 C CG . GLU A 470 ? 0.5403 0.4854 0.4714 0.0590 0.0241 -0.1681 470 GLU A CG 3603 C CD . GLU A 470 ? 0.6017 0.5202 0.5450 0.0585 0.0298 -0.1778 470 GLU A CD 3604 O OE1 . GLU A 470 ? 0.6098 0.5120 0.5572 0.0676 0.0348 -0.1722 470 GLU A OE1 3605 O OE2 . GLU A 470 ? 0.6067 0.5212 0.5559 0.0495 0.0297 -0.1911 470 GLU A OE2 3606 N N . PHE A 471 ? 0.4650 0.4178 0.3883 0.0531 0.0173 -0.1226 471 PHE A N 3607 C CA . PHE A 471 ? 0.4658 0.4126 0.3893 0.0586 0.0184 -0.1071 471 PHE A CA 3608 C C . PHE A 471 ? 0.4427 0.4106 0.3585 0.0616 0.0155 -0.0996 471 PHE A C 3609 O O . PHE A 471 ? 0.4447 0.4152 0.3608 0.0697 0.0169 -0.0940 471 PHE A O 3610 C CB . PHE A 471 ? 0.4637 0.3993 0.3904 0.0523 0.0182 -0.0978 471 PHE A CB 3611 C CG . PHE A 471 ? 0.4746 0.4069 0.4001 0.0579 0.0187 -0.0821 471 PHE A CG 3612 C CD1 . PHE A 471 ? 0.5067 0.4192 0.4369 0.0643 0.0233 -0.0763 471 PHE A CD1 3613 C CD2 . PHE A 471 ? 0.4570 0.4061 0.3763 0.0571 0.0148 -0.0733 471 PHE A CD2 3614 C CE1 . PHE A 471 ? 0.4914 0.4038 0.4191 0.0706 0.0232 -0.0620 471 PHE A CE1 3615 C CE2 . PHE A 471 ? 0.4576 0.4061 0.3759 0.0622 0.0148 -0.0608 471 PHE A CE2 3616 C CZ . PHE A 471 ? 0.4706 0.4021 0.3926 0.0692 0.0185 -0.0552 471 PHE A CZ 3617 N N . VAL A 472 ? 0.4203 0.4033 0.3299 0.0552 0.0119 -0.0997 472 VAL A N 3618 C CA . VAL A 472 ? 0.3996 0.4012 0.3022 0.0564 0.0104 -0.0932 472 VAL A CA 3619 C C . VAL A 472 ? 0.4023 0.4159 0.3020 0.0624 0.0126 -0.1001 472 VAL A C 3620 O O . VAL A 472 ? 0.3923 0.4139 0.2923 0.0673 0.0140 -0.0945 472 VAL A O 3621 C CB . VAL A 472 ? 0.3890 0.4012 0.2851 0.0490 0.0070 -0.0914 472 VAL A CB 3622 C CG1 . VAL A 472 ? 0.3748 0.4026 0.2645 0.0496 0.0069 -0.0836 472 VAL A CG1 3623 C CG2 . VAL A 472 ? 0.3952 0.3968 0.2953 0.0434 0.0052 -0.0852 472 VAL A CG2 3624 N N . LYS A 473 ? 0.4065 0.4227 0.3042 0.0620 0.0131 -0.1129 473 LYS A N 3625 C CA . LYS A 473 ? 0.4184 0.4474 0.3123 0.0677 0.0157 -0.1203 473 LYS A CA 3626 C C . LYS A 473 ? 0.4165 0.4389 0.3176 0.0767 0.0193 -0.1207 473 LYS A C 3627 O O . LYS A 473 ? 0.4083 0.4445 0.3081 0.0821 0.0216 -0.1206 473 LYS A O 3628 C CB . LYS A 473 ? 0.4361 0.4688 0.3265 0.0663 0.0154 -0.1359 473 LYS A CB 3629 C CG . LYS A 473 ? 0.4463 0.4948 0.3263 0.0609 0.0121 -0.1368 473 LYS A CG 3630 C CD . LYS A 473 ? 0.4716 0.5267 0.3481 0.0610 0.0114 -0.1542 473 LYS A CD 3631 C CE . LYS A 473 ? 0.5236 0.5973 0.3881 0.0577 0.0076 -0.1556 473 LYS A CE 3632 N NZ . LYS A 473 ? 0.5749 0.6453 0.4407 0.0510 0.0031 -0.1481 473 LYS A NZ 3633 N N . SER A 474 ? 0.4160 0.4176 0.3249 0.0787 0.0202 -0.1208 474 SER A N 3634 C CA . SER A 474 ? 0.4312 0.4234 0.3470 0.0889 0.0237 -0.1205 474 SER A CA 3635 C C . SER A 474 ? 0.4169 0.4108 0.3350 0.0937 0.0230 -0.1061 474 SER A C 3636 O O . SER A 474 ? 0.4234 0.4146 0.3463 0.1038 0.0252 -0.1046 474 SER A O 3637 C CB . SER A 474 ? 0.4465 0.4134 0.3694 0.0897 0.0264 -0.1272 474 SER A CB 3638 O OG . SER A 474 ? 0.4715 0.4391 0.3939 0.0875 0.0276 -0.1438 474 SER A OG 3639 N N . GLY A 475 ? 0.3993 0.3996 0.3140 0.0870 0.0198 -0.0964 475 GLY A N 3640 C CA . GLY A 475 ? 0.3892 0.3904 0.3060 0.0901 0.0184 -0.0839 475 GLY A CA 3641 C C . GLY A 475 ? 0.3883 0.4097 0.3060 0.0953 0.0182 -0.0799 475 GLY A C 3642 O O . GLY A 475 ? 0.3800 0.4028 0.3006 0.1000 0.0170 -0.0715 475 GLY A O 3643 N N . GLY A 476 ? 0.3860 0.4246 0.3016 0.0944 0.0197 -0.0861 476 GLY A N 3644 C CA . GLY A 476 ? 0.3825 0.4424 0.3009 0.0977 0.0205 -0.0836 476 GLY A CA 3645 C C . GLY A 476 ? 0.3703 0.4393 0.2876 0.0905 0.0181 -0.0748 476 GLY A C 3646 O O . GLY A 476 ? 0.3627 0.4448 0.2852 0.0936 0.0176 -0.0708 476 GLY A O 3647 N N . PHE A 477 ? 0.3661 0.4294 0.2772 0.0812 0.0168 -0.0726 477 PHE A N 3648 C CA . PHE A 477 ? 0.3568 0.4256 0.2664 0.0740 0.0150 -0.0648 477 PHE A CA 3649 C C . PHE A 477 ? 0.3514 0.4374 0.2590 0.0689 0.0179 -0.0653 477 PHE A C 3650 O O . PHE A 477 ? 0.3587 0.4495 0.2617 0.0682 0.0208 -0.0705 477 PHE A O 3651 C CB . PHE A 477 ? 0.3523 0.4069 0.2568 0.0672 0.0124 -0.0618 477 PHE A CB 3652 C CG . PHE A 477 ? 0.3637 0.4004 0.2709 0.0703 0.0108 -0.0599 477 PHE A CG 3653 C CD1 . PHE A 477 ? 0.3463 0.3687 0.2524 0.0689 0.0111 -0.0655 477 PHE A CD1 3654 C CD2 . PHE A 477 ? 0.3438 0.3784 0.2547 0.0747 0.0095 -0.0527 477 PHE A CD2 3655 C CE1 . PHE A 477 ? 0.3827 0.3868 0.2922 0.0708 0.0112 -0.0632 477 PHE A CE1 3656 C CE2 . PHE A 477 ? 0.3449 0.3618 0.2572 0.0781 0.0093 -0.0492 477 PHE A CE2 3657 C CZ . PHE A 477 ? 0.3703 0.3707 0.2823 0.0757 0.0107 -0.0541 477 PHE A CZ 3658 N N . SER A 478 ? 0.3392 0.4347 0.2504 0.0656 0.0178 -0.0600 478 SER A N 3659 C CA . SER A 478 ? 0.3376 0.4470 0.2484 0.0594 0.0219 -0.0592 478 SER A CA 3660 C C . SER A 478 ? 0.3333 0.4348 0.2355 0.0515 0.0219 -0.0547 478 SER A C 3661 O O . SER A 478 ? 0.3302 0.4375 0.2271 0.0478 0.0261 -0.0544 478 SER A O 3662 C CB . SER A 478 ? 0.3239 0.4465 0.2439 0.0582 0.0220 -0.0570 478 SER A CB 3663 O OG . SER A 478 ? 0.3347 0.4682 0.2627 0.0667 0.0219 -0.0615 478 SER A OG 3664 N N . TYR A 479 ? 0.3280 0.4170 0.2287 0.0497 0.0175 -0.0506 479 TYR A N 3665 C CA . TYR A 479 ? 0.3274 0.4088 0.2210 0.0436 0.0165 -0.0464 479 TYR A CA 3666 C C . TYR A 479 ? 0.3271 0.3950 0.2212 0.0438 0.0116 -0.0440 479 TYR A C 3667 O O . TYR A 479 ? 0.3438 0.4080 0.2430 0.0484 0.0098 -0.0442 479 TYR A O 3668 C CB . TYR A 479 ? 0.3204 0.4079 0.2148 0.0374 0.0194 -0.0411 479 TYR A CB 3669 C CG . TYR A 479 ? 0.3181 0.4100 0.2213 0.0365 0.0182 -0.0393 479 TYR A CG 3670 C CD1 . TYR A 479 ? 0.2935 0.3769 0.1971 0.0352 0.0139 -0.0355 479 TYR A CD1 3671 C CD2 . TYR A 479 ? 0.2993 0.4061 0.2108 0.0370 0.0212 -0.0422 479 TYR A CD2 3672 C CE1 . TYR A 479 ? 0.2997 0.3894 0.2102 0.0350 0.0125 -0.0347 479 TYR A CE1 3673 C CE2 . TYR A 479 ? 0.2962 0.4104 0.2159 0.0364 0.0193 -0.0422 479 TYR A CE2 3674 C CZ . TYR A 479 ? 0.2950 0.4006 0.2135 0.0356 0.0148 -0.0384 479 TYR A CZ 3675 O OH . TYR A 479 ? 0.3016 0.4165 0.2272 0.0357 0.0126 -0.0391 479 TYR A OH 3676 N N . ALA A 480 ? 0.3238 0.3848 0.2124 0.0395 0.0100 -0.0414 480 ALA A N 3677 C CA . ALA A 480 ? 0.3200 0.3696 0.2095 0.0382 0.0063 -0.0387 480 ALA A CA 3678 C C . ALA A 480 ? 0.3135 0.3625 0.2008 0.0329 0.0057 -0.0327 480 ALA A C 3679 O O . ALA A 480 ? 0.3100 0.3633 0.1924 0.0302 0.0077 -0.0310 480 ALA A O 3680 C CB . ALA A 480 ? 0.3223 0.3642 0.2095 0.0387 0.0047 -0.0440 480 ALA A CB 3681 N N . ILE A 481 ? 0.3072 0.3501 0.1976 0.0321 0.0034 -0.0290 481 ILE A N 3682 C CA . ILE A 481 ? 0.3058 0.3458 0.1944 0.0277 0.0023 -0.0243 481 ILE A CA 3683 C C . ILE A 481 ? 0.3116 0.3423 0.2001 0.0271 -0.0004 -0.0249 481 ILE A C 3684 O O . ILE A 481 ? 0.3209 0.3449 0.2130 0.0292 -0.0011 -0.0251 481 ILE A O 3685 C CB . ILE A 481 ? 0.3041 0.3466 0.1967 0.0268 0.0022 -0.0205 481 ILE A CB 3686 C CG1 . ILE A 481 ? 0.2935 0.3465 0.1885 0.0257 0.0054 -0.0215 481 ILE A CG1 3687 C CG2 . ILE A 481 ? 0.2847 0.3225 0.1758 0.0230 0.0011 -0.0163 481 ILE A CG2 3688 C CD1 . ILE A 481 ? 0.2988 0.3593 0.2001 0.0267 0.0047 -0.0216 481 ILE A CD1 3689 N N . VAL A 482 ? 0.3085 0.3394 0.1932 0.0245 -0.0014 -0.0252 482 VAL A N 3690 C CA . VAL A 482 ? 0.3155 0.3405 0.2018 0.0228 -0.0037 -0.0275 482 VAL A CA 3691 C C . VAL A 482 ? 0.3100 0.3355 0.1955 0.0198 -0.0050 -0.0230 482 VAL A C 3692 O O . VAL A 482 ? 0.3100 0.3409 0.1908 0.0196 -0.0048 -0.0208 482 VAL A O 3693 C CB . VAL A 482 ? 0.3217 0.3489 0.2060 0.0235 -0.0046 -0.0355 482 VAL A CB 3694 C CG1 . VAL A 482 ? 0.3513 0.3885 0.2279 0.0247 -0.0040 -0.0358 482 VAL A CG1 3695 C CG2 . VAL A 482 ? 0.3197 0.3430 0.2079 0.0203 -0.0069 -0.0397 482 VAL A CG2 3696 N N . ALA A 483 ? 0.3079 0.3276 0.1979 0.0181 -0.0056 -0.0209 483 ALA A N 3697 C CA . ALA A 483 ? 0.3005 0.3209 0.1908 0.0157 -0.0065 -0.0168 483 ALA A CA 3698 C C . ALA A 483 ? 0.3034 0.3224 0.1977 0.0130 -0.0081 -0.0200 483 ALA A C 3699 O O . ALA A 483 ? 0.3092 0.3213 0.2084 0.0117 -0.0072 -0.0220 483 ALA A O 3700 C CB . ALA A 483 ? 0.2955 0.3132 0.1876 0.0159 -0.0053 -0.0116 483 ALA A CB 3701 N N . VAL A 484 ? 0.2980 0.3238 0.1905 0.0123 -0.0101 -0.0204 484 VAL A N 3702 C CA . VAL A 484 ? 0.2994 0.3286 0.1968 0.0095 -0.0122 -0.0248 484 VAL A CA 3703 C C . VAL A 484 ? 0.2944 0.3299 0.1911 0.0098 -0.0135 -0.0209 484 VAL A C 3704 O O . VAL A 484 ? 0.2941 0.3295 0.1859 0.0122 -0.0124 -0.0152 484 VAL A O 3705 C CB . VAL A 484 ? 0.3052 0.3414 0.2012 0.0100 -0.0146 -0.0334 484 VAL A CB 3706 C CG1 . VAL A 484 ? 0.2976 0.3264 0.1957 0.0097 -0.0128 -0.0387 484 VAL A CG1 3707 C CG2 . VAL A 484 ? 0.3002 0.3455 0.1864 0.0145 -0.0159 -0.0314 484 VAL A CG2 3708 N N . GLY A 485 ? 0.2929 0.3338 0.1956 0.0073 -0.0153 -0.0245 485 GLY A N 3709 C CA . GLY A 485 ? 0.2852 0.3340 0.1877 0.0089 -0.0169 -0.0215 485 GLY A CA 3710 C C . GLY A 485 ? 0.2853 0.3386 0.1976 0.0049 -0.0173 -0.0241 485 GLY A C 3711 O O . GLY A 485 ? 0.2817 0.3348 0.2018 0.0001 -0.0171 -0.0306 485 GLY A O 3712 N N . GLU A 486 ? 0.2817 0.3388 0.1942 0.0068 -0.0173 -0.0194 486 GLU A N 3713 C CA . GLU A 486 ? 0.2739 0.3381 0.1958 0.0039 -0.0174 -0.0214 486 GLU A CA 3714 C C . GLU A 486 ? 0.2890 0.3434 0.2164 -0.0010 -0.0128 -0.0188 486 GLU A C 3715 O O . GLU A 486 ? 0.2891 0.3330 0.2113 0.0001 -0.0101 -0.0134 486 GLU A O 3716 C CB . GLU A 486 ? 0.2728 0.3440 0.1926 0.0090 -0.0184 -0.0168 486 GLU A CB 3717 C CG . GLU A 486 ? 0.2686 0.3508 0.1825 0.0155 -0.0226 -0.0175 486 GLU A CG 3718 C CD . GLU A 486 ? 0.2753 0.3653 0.1900 0.0209 -0.0234 -0.0137 486 GLU A CD 3719 O OE1 . GLU A 486 ? 0.2861 0.3672 0.1971 0.0234 -0.0201 -0.0071 486 GLU A OE1 3720 O OE2 . GLU A 486 ? 0.2941 0.4001 0.2140 0.0227 -0.0272 -0.0183 486 GLU A OE2 3721 N N . HIS A 487 ? 0.2880 0.3474 0.2260 -0.0061 -0.0116 -0.0226 487 HIS A N 3722 C CA . HIS A 487 ? 0.2970 0.3485 0.2398 -0.0102 -0.0062 -0.0188 487 HIS A CA 3723 C C . HIS A 487 ? 0.2900 0.3468 0.2322 -0.0075 -0.0051 -0.0136 487 HIS A C 3724 O O . HIS A 487 ? 0.2886 0.3557 0.2297 -0.0034 -0.0085 -0.0144 487 HIS A O 3725 C CB . HIS A 487 ? 0.3067 0.3592 0.2619 -0.0179 -0.0036 -0.0251 487 HIS A CB 3726 C CG . HIS A 487 ? 0.3308 0.3751 0.2869 -0.0204 -0.0035 -0.0306 487 HIS A CG 3727 N ND1 . HIS A 487 ? 0.3514 0.3957 0.3194 -0.0278 -0.0014 -0.0388 487 HIS A ND1 3728 C CD2 . HIS A 487 ? 0.3431 0.3792 0.2904 -0.0166 -0.0049 -0.0299 487 HIS A CD2 3729 C CE1 . HIS A 487 ? 0.3609 0.3962 0.3270 -0.0280 -0.0015 -0.0431 487 HIS A CE1 3730 N NE2 . HIS A 487 ? 0.3539 0.3848 0.3073 -0.0209 -0.0037 -0.0375 487 HIS A NE2 3731 N N . PRO A 488 ? 0.2898 0.3393 0.2313 -0.0087 -0.0003 -0.0081 488 PRO A N 3732 C CA . PRO A 488 ? 0.2841 0.3392 0.2251 -0.0062 0.0010 -0.0044 488 PRO A CA 3733 C C . PRO A 488 ? 0.2829 0.3522 0.2345 -0.0083 0.0009 -0.0084 488 PRO A C 3734 O O . PRO A 488 ? 0.2936 0.3663 0.2553 -0.0146 0.0028 -0.0125 488 PRO A O 3735 C CB . PRO A 488 ? 0.2793 0.3253 0.2176 -0.0076 0.0065 0.0014 488 PRO A CB 3736 C CG . PRO A 488 ? 0.2917 0.3259 0.2248 -0.0074 0.0064 0.0025 488 PRO A CG 3737 C CD . PRO A 488 ? 0.2861 0.3223 0.2258 -0.0109 0.0041 -0.0044 488 PRO A CD 3738 N N . TYR A 489 ? 0.2793 0.3570 0.2297 -0.0032 -0.0010 -0.0075 489 TYR A N 3739 C CA . TYR A 489 ? 0.2721 0.3656 0.2328 -0.0035 -0.0013 -0.0111 489 TYR A CA 3740 C C . TYR A 489 ? 0.2680 0.3648 0.2255 0.0028 -0.0005 -0.0075 489 TYR A C 3741 O O . TYR A 489 ? 0.2737 0.3615 0.2212 0.0077 -0.0010 -0.0039 489 TYR A O 3742 C CB . TYR A 489 ? 0.2761 0.3824 0.2408 -0.0018 -0.0074 -0.0175 489 TYR A CB 3743 C CG . TYR A 489 ? 0.2783 0.3817 0.2314 0.0064 -0.0119 -0.0150 489 TYR A CG 3744 C CD1 . TYR A 489 ? 0.2726 0.3795 0.2218 0.0144 -0.0128 -0.0114 489 TYR A CD1 3745 C CD2 . TYR A 489 ? 0.2756 0.3719 0.2221 0.0061 -0.0142 -0.0161 489 TYR A CD2 3746 C CE1 . TYR A 489 ? 0.2720 0.3740 0.2108 0.0216 -0.0152 -0.0079 489 TYR A CE1 3747 C CE2 . TYR A 489 ? 0.2784 0.3718 0.2142 0.0131 -0.0169 -0.0129 489 TYR A CE2 3748 C CZ . TYR A 489 ? 0.2825 0.3781 0.2146 0.0206 -0.0171 -0.0084 489 TYR A CZ 3749 O OH . TYR A 489 ? 0.2952 0.3858 0.2169 0.0273 -0.0182 -0.0042 489 TYR A OH 3750 N N . THR A 490 ? 0.2660 0.3760 0.2330 0.0023 0.0012 -0.0096 490 THR A N 3751 C CA . THR A 490 ? 0.2715 0.3861 0.2375 0.0085 0.0025 -0.0076 490 THR A CA 3752 C C . THR A 490 ? 0.2790 0.4139 0.2565 0.0109 0.0003 -0.0122 490 THR A C 3753 O O . THR A 490 ? 0.2841 0.4304 0.2736 0.0044 0.0012 -0.0169 490 THR A O 3754 C CB . THR A 490 ? 0.2733 0.3831 0.2383 0.0056 0.0091 -0.0042 490 THR A CB 3755 O OG1 . THR A 490 ? 0.2561 0.3502 0.2110 0.0039 0.0104 -0.0004 490 THR A OG1 3756 C CG2 . THR A 490 ? 0.2690 0.3825 0.2321 0.0122 0.0108 -0.0033 490 THR A CG2 3757 N N . GLU A 491 ? 0.2801 0.4195 0.2550 0.0203 -0.0020 -0.0111 491 GLU A N 3758 C CA . GLU A 491 ? 0.2824 0.4424 0.2677 0.0251 -0.0039 -0.0148 491 GLU A CA 3759 C C . GLU A 491 ? 0.2830 0.4592 0.2766 0.0228 -0.0094 -0.0211 491 GLU A C 3760 O O . GLU A 491 ? 0.2797 0.4505 0.2661 0.0240 -0.0138 -0.0210 491 GLU A O 3761 C CB . GLU A 491 ? 0.2786 0.4467 0.2729 0.0222 0.0021 -0.0157 491 GLU A CB 3762 C CG . GLU A 491 ? 0.2747 0.4301 0.2599 0.0270 0.0063 -0.0111 491 GLU A CG 3763 C CD . GLU A 491 ? 0.2882 0.4510 0.2796 0.0246 0.0129 -0.0118 491 GLU A CD 3764 O OE1 . GLU A 491 ? 0.2870 0.4675 0.2889 0.0282 0.0131 -0.0151 491 GLU A OE1 3765 O OE2 . GLU A 491 ? 0.2858 0.4376 0.2708 0.0204 0.0178 -0.0089 491 GLU A OE2 3766 N N . THR A 492 ? 0.2876 0.4844 0.2967 0.0191 -0.0090 -0.0273 492 THR A N 3767 C CA . THR A 492 ? 0.2894 0.5065 0.3082 0.0178 -0.0151 -0.0356 492 THR A CA 3768 C C . THR A 492 ? 0.2970 0.5059 0.3156 0.0080 -0.0157 -0.0394 492 THR A C 3769 O O . THR A 492 ? 0.2980 0.5176 0.3176 0.0091 -0.0220 -0.0453 492 THR A O 3770 C CB . THR A 492 ? 0.2885 0.5318 0.3263 0.0151 -0.0140 -0.0427 492 THR A CB 3771 O OG1 . THR A 492 ? 0.2895 0.5391 0.3264 0.0258 -0.0133 -0.0389 492 THR A OG1 3772 C CG2 . THR A 492 ? 0.2827 0.5517 0.3312 0.0153 -0.0215 -0.0530 492 THR A CG2 3773 N N . LYS A 493 ? 0.3017 0.4918 0.3181 -0.0006 -0.0093 -0.0361 493 LYS A N 3774 C CA . LYS A 493 ? 0.3150 0.4934 0.3303 -0.0089 -0.0089 -0.0389 493 LYS A CA 3775 C C . LYS A 493 ? 0.3094 0.4782 0.3102 -0.0027 -0.0146 -0.0369 493 LYS A C 3776 O O . LYS A 493 ? 0.3229 0.4891 0.3241 -0.0074 -0.0166 -0.0420 493 LYS A O 3777 C CB . LYS A 493 ? 0.3224 0.4811 0.3358 -0.0165 -0.0005 -0.0334 493 LYS A CB 3778 C CG . LYS A 493 ? 0.3730 0.5396 0.4028 -0.0266 0.0065 -0.0369 493 LYS A CG 3779 C CD . LYS A 493 ? 0.4556 0.6194 0.4951 -0.0373 0.0079 -0.0444 493 LYS A CD 3780 C CE . LYS A 493 ? 0.5037 0.6817 0.5641 -0.0480 0.0140 -0.0513 493 LYS A CE 3781 N NZ . LYS A 493 ? 0.5414 0.7062 0.6026 -0.0536 0.0252 -0.0430 493 LYS A NZ 3782 N N . GLY A 494 ? 0.3008 0.4638 0.2894 0.0074 -0.0163 -0.0298 494 GLY A N 3783 C CA . GLY A 494 ? 0.2959 0.4500 0.2705 0.0137 -0.0205 -0.0268 494 GLY A CA 3784 C C . GLY A 494 ? 0.2946 0.4657 0.2673 0.0226 -0.0275 -0.0294 494 GLY A C 3785 O O . GLY A 494 ? 0.2979 0.4631 0.2588 0.0277 -0.0305 -0.0268 494 GLY A O 3786 N N . ASP A 495 ? 0.2886 0.4821 0.2723 0.0255 -0.0300 -0.0340 495 ASP A N 3787 C CA . ASP A 495 ? 0.2924 0.5065 0.2749 0.0352 -0.0374 -0.0370 495 ASP A CA 3788 C C . ASP A 495 ? 0.3010 0.5220 0.2842 0.0301 -0.0418 -0.0455 495 ASP A C 3789 O O . ASP A 495 ? 0.2986 0.5219 0.2935 0.0182 -0.0400 -0.0539 495 ASP A O 3790 C CB . ASP A 495 ? 0.2886 0.5292 0.2862 0.0378 -0.0394 -0.0426 495 ASP A CB 3791 C CG . ASP A 495 ? 0.2765 0.5138 0.2723 0.0466 -0.0362 -0.0348 495 ASP A CG 3792 O OD1 . ASP A 495 ? 0.2773 0.4914 0.2607 0.0501 -0.0323 -0.0256 495 ASP A OD1 3793 O OD2 . ASP A 495 ? 0.2602 0.5194 0.2682 0.0500 -0.0374 -0.0388 495 ASP A OD2 3794 N N . ASN A 496 ? 0.3077 0.5307 0.2777 0.0391 -0.0468 -0.0432 496 ASN A N 3795 C CA . ASN A 496 ? 0.3132 0.5378 0.2794 0.0352 -0.0501 -0.0499 496 ASN A CA 3796 C C . ASN A 496 ? 0.3283 0.5687 0.2831 0.0482 -0.0572 -0.0490 496 ASN A C 3797 O O . ASN A 496 ? 0.3276 0.5561 0.2671 0.0582 -0.0560 -0.0377 496 ASN A O 3798 C CB . ASN A 496 ? 0.3071 0.5028 0.2633 0.0302 -0.0448 -0.0440 496 ASN A CB 3799 C CG . ASN A 496 ? 0.3176 0.5126 0.2720 0.0246 -0.0469 -0.0519 496 ASN A CG 3800 O OD1 . ASN A 496 ? 0.3054 0.5198 0.2594 0.0279 -0.0531 -0.0598 496 ASN A OD1 3801 N ND2 . ASN A 496 ? 0.3256 0.4988 0.2785 0.0168 -0.0417 -0.0503 496 ASN A ND2 3802 N N . LEU A 497 ? 0.3426 0.6099 0.3047 0.0479 -0.0639 -0.0613 497 LEU A N 3803 C CA . LEU A 497 ? 0.3630 0.6509 0.3143 0.0615 -0.0715 -0.0613 497 LEU A CA 3804 C C . LEU A 497 ? 0.3796 0.6613 0.3160 0.0626 -0.0732 -0.0621 497 LEU A C 3805 O O . LEU A 497 ? 0.3931 0.6845 0.3148 0.0757 -0.0773 -0.0571 497 LEU A O 3806 C CB . LEU A 497 ? 0.3606 0.6858 0.3267 0.0622 -0.0790 -0.0753 497 LEU A CB 3807 C CG . LEU A 497 ? 0.3537 0.6938 0.3346 0.0643 -0.0788 -0.0754 497 LEU A CG 3808 C CD1 . LEU A 497 ? 0.3429 0.7233 0.3394 0.0641 -0.0869 -0.0916 497 LEU A CD1 3809 C CD2 . LEU A 497 ? 0.3444 0.6779 0.3125 0.0807 -0.0779 -0.0596 497 LEU A CD2 3810 N N A ASN A 498 ? 0.3786 0.6448 0.3185 0.0500 -0.0696 -0.0679 498 ASN A N 3811 N N B ASN A 498 ? 0.3807 0.6462 0.3208 0.0498 -0.0694 -0.0677 498 ASN A N 3812 C CA A ASN A 498 ? 0.3907 0.6519 0.3177 0.0507 -0.0708 -0.0699 498 ASN A CA 3813 C CA B ASN A 498 ? 0.3943 0.6540 0.3235 0.0485 -0.0702 -0.0712 498 ASN A CA 3814 C C . ASN A 498 ? 0.3848 0.6151 0.2981 0.0511 -0.0640 -0.0571 498 ASN A C 3815 O O . ASN A 498 ? 0.3889 0.6167 0.2876 0.0564 -0.0646 -0.0545 498 ASN A O 3816 C CB A ASN A 498 ? 0.3990 0.6669 0.3383 0.0382 -0.0722 -0.0870 498 ASN A CB 3817 C CB B ASN A 498 ? 0.4040 0.6614 0.3478 0.0331 -0.0689 -0.0859 498 ASN A CB 3818 C CG A ASN A 498 ? 0.4320 0.6784 0.3846 0.0241 -0.0650 -0.0884 498 ASN A CG 3819 C CG B ASN A 498 ? 0.4556 0.7341 0.4217 0.0252 -0.0711 -0.0990 498 ASN A CG 3820 O OD1 A ASN A 498 ? 0.4304 0.6507 0.3765 0.0206 -0.0592 -0.0816 498 ASN A OD1 3821 O OD1 B ASN A 498 ? 0.4765 0.7827 0.4462 0.0324 -0.0774 -0.1029 498 ASN A OD1 3822 N ND2 A ASN A 498 ? 0.5090 0.7677 0.4808 0.0164 -0.0649 -0.0969 498 ASN A ND2 3823 N ND2 B ASN A 498 ? 0.5265 0.7928 0.5078 0.0103 -0.0657 -0.1064 498 ASN A ND2 3824 N N . LEU A 499 ? 0.3628 0.5718 0.2804 0.0462 -0.0575 -0.0493 499 LEU A N 3825 C CA . LEU A 499 ? 0.3510 0.5327 0.2576 0.0460 -0.0510 -0.0382 499 LEU A CA 3826 C C . LEU A 499 ? 0.3584 0.5307 0.2582 0.0419 -0.0499 -0.0418 499 LEU A C 3827 O O . LEU A 499 ? 0.3565 0.5180 0.2425 0.0470 -0.0474 -0.0337 499 LEU A O 3828 C CB . LEU A 499 ? 0.3483 0.5250 0.2414 0.0584 -0.0496 -0.0246 499 LEU A CB 3829 C CG . LEU A 499 ? 0.3338 0.5155 0.2331 0.0634 -0.0494 -0.0199 499 LEU A CG 3830 C CD1 . LEU A 499 ? 0.3181 0.4919 0.2038 0.0760 -0.0470 -0.0066 499 LEU A CD1 3831 C CD2 . LEU A 499 ? 0.3101 0.4772 0.2207 0.0535 -0.0441 -0.0199 499 LEU A CD2 3832 N N . THR A 500 ? 0.3674 0.5440 0.2777 0.0326 -0.0511 -0.0543 500 THR A N 3833 C CA . THR A 500 ? 0.3875 0.5530 0.2933 0.0282 -0.0492 -0.0583 500 THR A CA 3834 C C . THR A 500 ? 0.3846 0.5297 0.2999 0.0181 -0.0434 -0.0581 500 THR A C 3835 O O . THR A 500 ? 0.3809 0.5274 0.3098 0.0116 -0.0423 -0.0617 500 THR A O 3836 C CB . THR A 500 ? 0.4019 0.5863 0.3098 0.0269 -0.0547 -0.0734 500 THR A CB 3837 O OG1 . THR A 500 ? 0.4466 0.6357 0.3729 0.0163 -0.0550 -0.0856 500 THR A OG1 3838 C CG2 . THR A 500 ? 0.3838 0.5938 0.2840 0.0377 -0.0615 -0.0743 500 THR A CG2 3839 N N . ILE A 501 ? 0.3883 0.5153 0.2964 0.0172 -0.0392 -0.0533 501 ILE A N 3840 C CA . ILE A 501 ? 0.3900 0.4984 0.3054 0.0097 -0.0338 -0.0516 501 ILE A CA 3841 C C . ILE A 501 ? 0.4023 0.5109 0.3303 0.0010 -0.0335 -0.0638 501 ILE A C 3842 O O . ILE A 501 ? 0.4014 0.5205 0.3297 0.0007 -0.0369 -0.0744 501 ILE A O 3843 C CB . ILE A 501 ? 0.3913 0.4824 0.2971 0.0116 -0.0297 -0.0437 501 ILE A CB 3844 C CG1 . ILE A 501 ? 0.4001 0.4919 0.2999 0.0127 -0.0305 -0.0498 501 ILE A CG1 3845 C CG2 . ILE A 501 ? 0.3833 0.4723 0.2796 0.0183 -0.0286 -0.0324 501 ILE A CG2 3846 C CD1 . ILE A 501 ? 0.4079 0.4833 0.3035 0.0123 -0.0260 -0.0450 501 ILE A CD1 3847 N N . PRO A 502 ? 0.4089 0.5059 0.3473 -0.0059 -0.0288 -0.0624 502 PRO A N 3848 C CA . PRO A 502 ? 0.4248 0.5172 0.3756 -0.0147 -0.0264 -0.0727 502 PRO A CA 3849 C C . PRO A 502 ? 0.4377 0.5182 0.3839 -0.0147 -0.0249 -0.0766 502 PRO A C 3850 O O . PRO A 502 ? 0.4335 0.5045 0.3685 -0.0094 -0.0237 -0.0687 502 PRO A O 3851 C CB . PRO A 502 ? 0.4201 0.4984 0.3783 -0.0198 -0.0200 -0.0655 502 PRO A CB 3852 C CG . PRO A 502 ? 0.4095 0.4817 0.3567 -0.0133 -0.0193 -0.0524 502 PRO A CG 3853 C CD . PRO A 502 ? 0.4030 0.4905 0.3418 -0.0059 -0.0249 -0.0516 502 PRO A CD 3854 N N . GLU A 503 ? 0.4564 0.5382 0.4124 -0.0209 -0.0245 -0.0896 503 GLU A N 3855 C CA . GLU A 503 ? 0.4772 0.5462 0.4313 -0.0214 -0.0222 -0.0947 503 GLU A CA 3856 C C . GLU A 503 ? 0.4865 0.5325 0.4491 -0.0270 -0.0144 -0.0913 503 GLU A C 3857 O O . GLU A 503 ? 0.4927 0.5360 0.4658 -0.0330 -0.0110 -0.0897 503 GLU A O 3858 C CB . GLU A 503 ? 0.4869 0.5702 0.4457 -0.0239 -0.0261 -0.1122 503 GLU A CB 3859 C CG . GLU A 503 ? 0.5019 0.6051 0.4470 -0.0154 -0.0330 -0.1136 503 GLU A CG 3860 C CD . GLU A 503 ? 0.5186 0.6117 0.4479 -0.0075 -0.0315 -0.1025 503 GLU A CD 3861 O OE1 . GLU A 503 ? 0.4992 0.5814 0.4273 -0.0076 -0.0288 -0.1068 503 GLU A OE1 3862 O OE2 . GLU A 503 ? 0.5225 0.6181 0.4422 -0.0015 -0.0324 -0.0900 503 GLU A OE2 3863 N N . PRO A 504 ? 0.4922 0.5217 0.4497 -0.0241 -0.0111 -0.0891 504 PRO A N 3864 C CA . PRO A 504 ? 0.4828 0.5157 0.4279 -0.0167 -0.0141 -0.0895 504 PRO A CA 3865 C C . PRO A 504 ? 0.4608 0.4952 0.3935 -0.0097 -0.0152 -0.0755 504 PRO A C 3866 O O . PRO A 504 ? 0.4596 0.4838 0.3922 -0.0093 -0.0120 -0.0647 504 PRO A O 3867 C CB . PRO A 504 ? 0.4977 0.5112 0.4455 -0.0169 -0.0088 -0.0921 504 PRO A CB 3868 C CG . PRO A 504 ? 0.5079 0.5042 0.4633 -0.0207 -0.0026 -0.0839 504 PRO A CG 3869 C CD . PRO A 504 ? 0.5033 0.5099 0.4676 -0.0274 -0.0035 -0.0857 504 PRO A CD 3870 N N . GLY A 505 ? 0.4369 0.4844 0.3592 -0.0042 -0.0194 -0.0761 505 GLY A N 3871 C CA . GLY A 505 ? 0.4063 0.4552 0.3177 0.0017 -0.0198 -0.0644 505 GLY A CA 3872 C C . GLY A 505 ? 0.3959 0.4536 0.2966 0.0071 -0.0218 -0.0672 505 GLY A C 3873 O O . GLY A 505 ? 0.3925 0.4434 0.2878 0.0103 -0.0192 -0.0639 505 GLY A O 3874 N N . LEU A 506 ? 0.3887 0.4633 0.2865 0.0086 -0.0263 -0.0736 506 LEU A N 3875 C CA . LEU A 506 ? 0.3786 0.4642 0.2654 0.0141 -0.0283 -0.0774 506 LEU A CA 3876 C C . LEU A 506 ? 0.3802 0.4601 0.2690 0.0129 -0.0264 -0.0875 506 LEU A C 3877 O O . LEU A 506 ? 0.3780 0.4568 0.2582 0.0173 -0.0243 -0.0853 506 LEU A O 3878 C CB . LEU A 506 ? 0.3831 0.4902 0.2673 0.0163 -0.0342 -0.0838 506 LEU A CB 3879 C CG . LEU A 506 ? 0.3763 0.4974 0.2468 0.0232 -0.0363 -0.0875 506 LEU A CG 3880 C CD1 . LEU A 506 ? 0.3391 0.4551 0.1964 0.0295 -0.0325 -0.0732 506 LEU A CD1 3881 C CD2 . LEU A 506 ? 0.3904 0.5351 0.2583 0.0264 -0.0429 -0.0944 506 LEU A CD2 3882 N N . SER A 507 ? 0.3815 0.4571 0.2825 0.0067 -0.0263 -0.0986 507 SER A N 3883 C CA . SER A 507 ? 0.3885 0.4563 0.2928 0.0057 -0.0238 -0.1093 507 SER A CA 3884 C C . SER A 507 ? 0.3826 0.4329 0.2850 0.0085 -0.0185 -0.1006 507 SER A C 3885 O O . SER A 507 ? 0.3824 0.4316 0.2804 0.0122 -0.0169 -0.1050 507 SER A O 3886 C CB . SER A 507 ? 0.3990 0.4614 0.3189 -0.0025 -0.0230 -0.1219 507 SER A CB 3887 O OG . SER A 507 ? 0.4165 0.4636 0.3455 -0.0071 -0.0192 -0.1135 507 SER A OG 3888 N N . THR A 508 ? 0.3643 0.4031 0.2698 0.0074 -0.0160 -0.0887 508 THR A N 3889 C CA . THR A 508 ? 0.3594 0.3852 0.2629 0.0110 -0.0119 -0.0804 508 THR A CA 3890 C C . THR A 508 ? 0.3463 0.3811 0.2381 0.0169 -0.0122 -0.0745 508 THR A C 3891 O O . THR A 508 ? 0.3446 0.3767 0.2340 0.0207 -0.0097 -0.0756 508 THR A O 3892 C CB . THR A 508 ? 0.3625 0.3767 0.2711 0.0089 -0.0096 -0.0697 508 THR A CB 3893 O OG1 . THR A 508 ? 0.3963 0.4015 0.3159 0.0031 -0.0078 -0.0749 508 THR A OG1 3894 C CG2 . THR A 508 ? 0.3485 0.3521 0.2555 0.0136 -0.0060 -0.0622 508 THR A CG2 3895 N N . VAL A 509 ? 0.3287 0.3740 0.2139 0.0177 -0.0144 -0.0684 509 VAL A N 3896 C CA . VAL A 509 ? 0.3168 0.3700 0.1913 0.0225 -0.0134 -0.0625 509 VAL A CA 3897 C C . VAL A 509 ? 0.3379 0.4000 0.2060 0.0258 -0.0135 -0.0714 509 VAL A C 3898 O O . VAL A 509 ? 0.3356 0.3981 0.1992 0.0291 -0.0102 -0.0695 509 VAL A O 3899 C CB . VAL A 509 ? 0.3163 0.3776 0.1848 0.0234 -0.0153 -0.0547 509 VAL A CB 3900 C CG1 . VAL A 509 ? 0.2861 0.3548 0.1427 0.0282 -0.0131 -0.0491 509 VAL A CG1 3901 C CG2 . VAL A 509 ? 0.2818 0.3339 0.1555 0.0208 -0.0141 -0.0456 509 VAL A CG2 3902 N N . GLN A 510 ? 0.3524 0.4234 0.2208 0.0249 -0.0171 -0.0821 510 GLN A N 3903 C CA . GLN A 510 ? 0.3750 0.4560 0.2374 0.0281 -0.0176 -0.0927 510 GLN A CA 3904 C C . GLN A 510 ? 0.3862 0.4566 0.2541 0.0284 -0.0140 -0.0997 510 GLN A C 3905 O O . GLN A 510 ? 0.3970 0.4727 0.2581 0.0329 -0.0116 -0.1019 510 GLN A O 3906 C CB . GLN A 510 ? 0.3779 0.4723 0.2412 0.0265 -0.0229 -0.1047 510 GLN A CB 3907 C CG . GLN A 510 ? 0.3800 0.4902 0.2336 0.0299 -0.0267 -0.0984 510 GLN A CG 3908 C CD . GLN A 510 ? 0.4026 0.5281 0.2603 0.0279 -0.0330 -0.1102 510 GLN A CD 3909 O OE1 . GLN A 510 ? 0.4331 0.5545 0.3037 0.0216 -0.0339 -0.1221 510 GLN A OE1 3910 N NE2 . GLN A 510 ? 0.4134 0.5568 0.2606 0.0335 -0.0369 -0.1067 510 GLN A NE2 3911 N N . ALA A 511 ? 0.3923 0.4477 0.2725 0.0243 -0.0129 -0.1027 511 ALA A N 3912 C CA . ALA A 511 ? 0.4053 0.4484 0.2913 0.0258 -0.0091 -0.1085 511 ALA A CA 3913 C C . ALA A 511 ? 0.4025 0.4418 0.2851 0.0307 -0.0054 -0.0982 511 ALA A C 3914 O O . ALA A 511 ? 0.4129 0.4533 0.2937 0.0352 -0.0028 -0.1027 511 ALA A O 3915 C CB . ALA A 511 ? 0.4109 0.4366 0.3102 0.0208 -0.0076 -0.1116 511 ALA A CB 3916 N N . VAL A 512 ? 0.3827 0.4195 0.2650 0.0299 -0.0053 -0.0853 512 VAL A N 3917 C CA . VAL A 512 ? 0.3759 0.4117 0.2566 0.0335 -0.0023 -0.0764 512 VAL A CA 3918 C C . VAL A 512 ? 0.3813 0.4313 0.2524 0.0367 -0.0007 -0.0749 512 VAL A C 3919 O O . VAL A 512 ? 0.3829 0.4355 0.2537 0.0407 0.0024 -0.0769 512 VAL A O 3920 C CB . VAL A 512 ? 0.3653 0.3955 0.2489 0.0311 -0.0027 -0.0647 512 VAL A CB 3921 C CG1 . VAL A 512 ? 0.3559 0.3898 0.2378 0.0339 -0.0001 -0.0569 512 VAL A CG1 3922 C CG2 . VAL A 512 ? 0.3616 0.3768 0.2542 0.0294 -0.0023 -0.0648 512 VAL A CG2 3923 N N . CYS A 513 ? 0.3798 0.4390 0.2432 0.0354 -0.0024 -0.0712 513 CYS A N 3924 C CA . CYS A 513 ? 0.3829 0.4537 0.2361 0.0381 0.0003 -0.0672 513 CYS A CA 3925 C C . CYS A 513 ? 0.3942 0.4748 0.2414 0.0420 0.0014 -0.0772 513 CYS A C 3926 O O . CYS A 513 ? 0.3987 0.4874 0.2395 0.0450 0.0057 -0.0748 513 CYS A O 3927 C CB . CYS A 513 ? 0.3817 0.4580 0.2277 0.0371 -0.0015 -0.0601 513 CYS A CB 3928 S SG . CYS A 513 ? 0.3923 0.4583 0.2451 0.0330 -0.0021 -0.0494 513 CYS A SG 3929 N N . GLY A 514 ? 0.3961 0.4761 0.2458 0.0415 -0.0019 -0.0890 514 GLY A N 3930 C CA . GLY A 514 ? 0.4077 0.4964 0.2530 0.0451 -0.0011 -0.1011 514 GLY A CA 3931 C C . GLY A 514 ? 0.4079 0.4916 0.2583 0.0484 0.0034 -0.1043 514 GLY A C 3932 O O . GLY A 514 ? 0.4156 0.5086 0.2606 0.0525 0.0058 -0.1118 514 GLY A O 3933 N N . GLY A 515 ? 0.4010 0.4717 0.2613 0.0475 0.0047 -0.0986 515 GLY A N 3934 C CA . GLY A 515 ? 0.4054 0.4717 0.2716 0.0520 0.0084 -0.1016 515 GLY A CA 3935 C C . GLY A 515 ? 0.4005 0.4713 0.2677 0.0539 0.0120 -0.0917 515 GLY A C 3936 O O . GLY A 515 ? 0.4032 0.4770 0.2737 0.0587 0.0154 -0.0947 515 GLY A O 3937 N N . VAL A 516 ? 0.3891 0.4611 0.2545 0.0501 0.0115 -0.0807 516 VAL A N 3938 C CA . VAL A 516 ? 0.3890 0.4658 0.2572 0.0503 0.0148 -0.0724 516 VAL A CA 3939 C C . VAL A 516 ? 0.3895 0.4692 0.2520 0.0456 0.0150 -0.0630 516 VAL A C 3940 O O . VAL A 516 ? 0.3813 0.4567 0.2402 0.0430 0.0114 -0.0617 516 VAL A O 3941 C CB . VAL A 516 ? 0.3842 0.4517 0.2631 0.0517 0.0137 -0.0696 516 VAL A CB 3942 C CG1 . VAL A 516 ? 0.3783 0.4359 0.2591 0.0472 0.0101 -0.0627 516 VAL A CG1 3943 C CG2 . VAL A 516 ? 0.3788 0.4561 0.2624 0.0536 0.0172 -0.0659 516 VAL A CG2 3944 N N . ARG A 517 ? 0.3989 0.4860 0.2612 0.0444 0.0196 -0.0568 517 ARG A N 3945 C CA . ARG A 517 ? 0.4164 0.5035 0.2736 0.0402 0.0208 -0.0478 517 ARG A CA 3946 C C . ARG A 517 ? 0.3957 0.4729 0.2595 0.0368 0.0171 -0.0429 517 ARG A C 3947 O O . ARG A 517 ? 0.3834 0.4570 0.2559 0.0375 0.0156 -0.0441 517 ARG A O 3948 C CB . ARG A 517 ? 0.4284 0.5245 0.2837 0.0388 0.0282 -0.0429 517 ARG A CB 3949 C CG . ARG A 517 ? 0.4784 0.5771 0.3450 0.0368 0.0308 -0.0419 517 ARG A CG 3950 C CD . ARG A 517 ? 0.5425 0.6537 0.4094 0.0368 0.0386 -0.0424 517 ARG A CD 3951 N NE . ARG A 517 ? 0.5748 0.6922 0.4543 0.0380 0.0388 -0.0467 517 ARG A NE 3952 C CZ . ARG A 517 ? 0.5885 0.7103 0.4779 0.0338 0.0409 -0.0443 517 ARG A CZ 3953 N NH1 . ARG A 517 ? 0.6005 0.7191 0.4893 0.0273 0.0443 -0.0377 517 ARG A NH1 3954 N NH2 . ARG A 517 ? 0.6276 0.7578 0.5279 0.0367 0.0399 -0.0492 517 ARG A NH2 3955 N N . CYS A 518 ? 0.3926 0.4660 0.2513 0.0343 0.0155 -0.0375 518 CYS A N 3956 C CA . CYS A 518 ? 0.3802 0.4444 0.2437 0.0317 0.0112 -0.0346 518 CYS A CA 3957 C C . CYS A 518 ? 0.3775 0.4398 0.2389 0.0285 0.0128 -0.0262 518 CYS A C 3958 O O . CYS A 518 ? 0.3822 0.4476 0.2353 0.0290 0.0154 -0.0224 518 CYS A O 3959 C CB . CYS A 518 ? 0.3776 0.4379 0.2394 0.0324 0.0061 -0.0395 518 CYS A CB 3960 S SG . CYS A 518 ? 0.3991 0.4666 0.2489 0.0335 0.0050 -0.0385 518 CYS A SG 3961 N N . ALA A 519 ? 0.3591 0.4159 0.2274 0.0258 0.0115 -0.0233 519 ALA A N 3962 C CA . ALA A 519 ? 0.3512 0.4037 0.2189 0.0229 0.0119 -0.0169 519 ALA A CA 3963 C C . ALA A 519 ? 0.3429 0.3895 0.2116 0.0228 0.0064 -0.0172 519 ALA A C 3964 O O . ALA A 519 ? 0.3317 0.3745 0.2065 0.0225 0.0038 -0.0193 519 ALA A O 3965 C CB . ALA A 519 ? 0.3419 0.3945 0.2172 0.0197 0.0146 -0.0149 519 ALA A CB 3966 N N . THR A 520 ? 0.3386 0.3853 0.2013 0.0235 0.0050 -0.0150 520 THR A N 3967 C CA . THR A 520 ? 0.3273 0.3709 0.1922 0.0229 0.0003 -0.0157 520 THR A CA 3968 C C . THR A 520 ? 0.3172 0.3561 0.1845 0.0208 0.0010 -0.0097 520 THR A C 3969 O O . THR A 520 ? 0.3190 0.3574 0.1823 0.0212 0.0041 -0.0045 520 THR A O 3970 C CB . THR A 520 ? 0.3379 0.3874 0.1962 0.0254 -0.0026 -0.0182 520 THR A CB 3971 O OG1 . THR A 520 ? 0.3543 0.4080 0.2118 0.0268 -0.0035 -0.0261 520 THR A OG1 3972 C CG2 . THR A 520 ? 0.3181 0.3670 0.1804 0.0241 -0.0070 -0.0191 520 THR A CG2 3973 N N . VAL A 521 ? 0.3021 0.3368 0.1758 0.0189 -0.0013 -0.0104 521 VAL A N 3974 C CA . VAL A 521 ? 0.3021 0.3334 0.1782 0.0173 -0.0009 -0.0061 521 VAL A CA 3975 C C . VAL A 521 ? 0.3055 0.3371 0.1825 0.0174 -0.0045 -0.0067 521 VAL A C 3976 O O . VAL A 521 ? 0.3005 0.3309 0.1820 0.0161 -0.0067 -0.0101 521 VAL A O 3977 C CB . VAL A 521 ? 0.2971 0.3259 0.1791 0.0156 -0.0004 -0.0062 521 VAL A CB 3978 C CG1 . VAL A 521 ? 0.2884 0.3147 0.1725 0.0141 -0.0003 -0.0031 521 VAL A CG1 3979 C CG2 . VAL A 521 ? 0.2892 0.3212 0.1722 0.0152 0.0029 -0.0069 521 VAL A CG2 3980 N N . LEU A 522 ? 0.3042 0.3376 0.1776 0.0191 -0.0045 -0.0031 522 LEU A N 3981 C CA . LEU A 522 ? 0.3013 0.3383 0.1764 0.0198 -0.0079 -0.0039 522 LEU A CA 3982 C C . LEU A 522 ? 0.2895 0.3230 0.1694 0.0183 -0.0074 -0.0010 522 LEU A C 3983 O O . LEU A 522 ? 0.2849 0.3150 0.1632 0.0192 -0.0046 0.0034 522 LEU A O 3984 C CB . LEU A 522 ? 0.3058 0.3494 0.1737 0.0245 -0.0089 -0.0019 522 LEU A CB 3985 C CG . LEU A 522 ? 0.3064 0.3581 0.1759 0.0266 -0.0130 -0.0032 522 LEU A CG 3986 C CD1 . LEU A 522 ? 0.3034 0.3613 0.1791 0.0235 -0.0171 -0.0119 522 LEU A CD1 3987 C CD2 . LEU A 522 ? 0.3268 0.3853 0.1868 0.0334 -0.0135 0.0006 522 LEU A CD2 3988 N N . ILE A 523 ? 0.2846 0.3185 0.1707 0.0158 -0.0093 -0.0037 523 ILE A N 3989 C CA . ILE A 523 ? 0.2909 0.3230 0.1814 0.0144 -0.0085 -0.0014 523 ILE A CA 3990 C C . ILE A 523 ? 0.2895 0.3289 0.1824 0.0157 -0.0110 -0.0022 523 ILE A C 3991 O O . ILE A 523 ? 0.2953 0.3401 0.1919 0.0141 -0.0135 -0.0069 523 ILE A O 3992 C CB . ILE A 523 ? 0.2856 0.3138 0.1811 0.0112 -0.0079 -0.0027 523 ILE A CB 3993 C CG1 . ILE A 523 ? 0.2850 0.3088 0.1783 0.0115 -0.0062 -0.0022 523 ILE A CG1 3994 C CG2 . ILE A 523 ? 0.2911 0.3193 0.1904 0.0100 -0.0068 -0.0005 523 ILE A CG2 3995 C CD1 . ILE A 523 ? 0.2601 0.2830 0.1521 0.0119 -0.0041 0.0005 523 ILE A CD1 3996 N N . SER A 524 ? 0.2884 0.3285 0.1800 0.0187 -0.0101 0.0016 524 SER A N 3997 C CA . SER A 524 ? 0.2898 0.3391 0.1838 0.0215 -0.0127 0.0010 524 SER A CA 3998 C C . SER A 524 ? 0.2888 0.3358 0.1837 0.0242 -0.0104 0.0052 524 SER A C 3999 O O . SER A 524 ? 0.2810 0.3190 0.1729 0.0244 -0.0069 0.0083 524 SER A O 4000 C CB . SER A 524 ? 0.2965 0.3531 0.1843 0.0266 -0.0153 0.0009 524 SER A CB 4001 O OG . SER A 524 ? 0.3123 0.3627 0.1920 0.0312 -0.0123 0.0072 524 SER A OG 4002 N N . GLY A 525 ? 0.2881 0.3439 0.1879 0.0261 -0.0123 0.0042 525 GLY A N 4003 C CA . GLY A 525 ? 0.2909 0.3453 0.1918 0.0300 -0.0102 0.0075 525 GLY A CA 4004 C C . GLY A 525 ? 0.2967 0.3527 0.1918 0.0384 -0.0106 0.0119 525 GLY A C 4005 O O . GLY A 525 ? 0.2954 0.3496 0.1912 0.0431 -0.0087 0.0149 525 GLY A O 4006 N N . ARG A 526 ? 0.3054 0.3641 0.1939 0.0409 -0.0126 0.0126 526 ARG A N 4007 C CA . ARG A 526 ? 0.3180 0.3821 0.1999 0.0503 -0.0139 0.0171 526 ARG A CA 4008 C C . ARG A 526 ? 0.3258 0.3930 0.1993 0.0515 -0.0156 0.0170 526 ARG A C 4009 O O . ARG A 526 ? 0.3179 0.3858 0.1933 0.0450 -0.0168 0.0116 526 ARG A O 4010 C CB . ARG A 526 ? 0.3159 0.3977 0.2041 0.0542 -0.0190 0.0137 526 ARG A CB 4011 C CG . ARG A 526 ? 0.3157 0.4092 0.2120 0.0468 -0.0232 0.0046 526 ARG A CG 4012 C CD . ARG A 526 ? 0.3212 0.4345 0.2258 0.0492 -0.0279 -0.0004 526 ARG A CD 4013 N NE . ARG A 526 ? 0.3187 0.4383 0.2344 0.0394 -0.0292 -0.0091 526 ARG A NE 4014 C CZ . ARG A 526 ? 0.2930 0.4267 0.2207 0.0371 -0.0308 -0.0145 526 ARG A CZ 4015 N NH1 . ARG A 526 ? 0.2986 0.4440 0.2290 0.0447 -0.0323 -0.0126 526 ARG A NH1 4016 N NH2 . ARG A 526 ? 0.2985 0.4347 0.2363 0.0272 -0.0303 -0.0217 526 ARG A NH2 4017 N N . PRO A 527 ? 0.3406 0.4097 0.2044 0.0607 -0.0152 0.0233 527 PRO A N 4018 C CA . PRO A 527 ? 0.3505 0.4283 0.2057 0.0635 -0.0179 0.0224 527 PRO A CA 4019 C C . PRO A 527 ? 0.3447 0.4420 0.2060 0.0614 -0.0254 0.0122 527 PRO A C 4020 O O . PRO A 527 ? 0.3415 0.4508 0.2105 0.0632 -0.0292 0.0089 527 PRO A O 4021 C CB . PRO A 527 ? 0.3635 0.4430 0.2077 0.0760 -0.0167 0.0319 527 PRO A CB 4022 C CG . PRO A 527 ? 0.3870 0.4502 0.2333 0.0776 -0.0105 0.0389 527 PRO A CG 4023 C CD . PRO A 527 ? 0.3513 0.4143 0.2111 0.0697 -0.0118 0.0320 527 PRO A CD 4024 N N . VAL A 528 ? 0.3380 0.4383 0.1971 0.0572 -0.0270 0.0064 528 VAL A N 4025 C CA . VAL A 528 ? 0.3295 0.4468 0.1943 0.0543 -0.0333 -0.0049 528 VAL A CA 4026 C C . VAL A 528 ? 0.3418 0.4670 0.1946 0.0591 -0.0350 -0.0061 528 VAL A C 4027 O O . VAL A 528 ? 0.3480 0.4629 0.1899 0.0625 -0.0302 0.0020 528 VAL A O 4028 C CB . VAL A 528 ? 0.3249 0.4352 0.2015 0.0426 -0.0324 -0.0128 528 VAL A CB 4029 C CG1 . VAL A 528 ? 0.3090 0.4147 0.1964 0.0387 -0.0307 -0.0115 528 VAL A CG1 4030 C CG2 . VAL A 528 ? 0.3048 0.3990 0.1765 0.0386 -0.0276 -0.0105 528 VAL A CG2 4031 N N . VAL A 529 ? 0.3423 0.4865 0.1975 0.0590 -0.0413 -0.0168 529 VAL A N 4032 C CA . VAL A 529 ? 0.3540 0.5085 0.1977 0.0636 -0.0434 -0.0199 529 VAL A CA 4033 C C . VAL A 529 ? 0.3523 0.4900 0.1931 0.0577 -0.0379 -0.0194 529 VAL A C 4034 O O . VAL A 529 ? 0.3477 0.4769 0.1989 0.0483 -0.0369 -0.0261 529 VAL A O 4035 C CB . VAL A 529 ? 0.3505 0.5291 0.2001 0.0625 -0.0513 -0.0350 529 VAL A CB 4036 C CG1 . VAL A 529 ? 0.3808 0.5713 0.2165 0.0681 -0.0534 -0.0389 529 VAL A CG1 4037 C CG2 . VAL A 529 ? 0.3562 0.5544 0.2100 0.0689 -0.0569 -0.0357 529 VAL A CG2 4038 N N . VAL A 530 ? 0.3558 0.4885 0.1824 0.0637 -0.0338 -0.0107 530 VAL A N 4039 C CA . VAL A 530 ? 0.3487 0.4655 0.1730 0.0588 -0.0275 -0.0083 530 VAL A CA 4040 C C . VAL A 530 ? 0.3640 0.4876 0.1755 0.0629 -0.0263 -0.0095 530 VAL A C 4041 O O . VAL A 530 ? 0.3614 0.4756 0.1729 0.0585 -0.0218 -0.0104 530 VAL A O 4042 C CB . VAL A 530 ? 0.3473 0.4455 0.1708 0.0587 -0.0202 0.0043 530 VAL A CB 4043 C CG1 . VAL A 530 ? 0.3647 0.4625 0.1737 0.0682 -0.0162 0.0160 530 VAL A CG1 4044 C CG2 . VAL A 530 ? 0.3327 0.4165 0.1610 0.0508 -0.0151 0.0034 530 VAL A CG2 4045 N N . GLN A 531 ? 0.3746 0.5163 0.1753 0.0718 -0.0303 -0.0102 531 GLN A N 4046 C CA . GLN A 531 ? 0.3883 0.5381 0.1752 0.0764 -0.0288 -0.0113 531 GLN A CA 4047 C C . GLN A 531 ? 0.3904 0.5403 0.1835 0.0687 -0.0295 -0.0247 531 GLN A C 4048 O O . GLN A 531 ? 0.3978 0.5415 0.1848 0.0682 -0.0239 -0.0226 531 GLN A O 4049 C CB . GLN A 531 ? 0.4007 0.5742 0.1747 0.0877 -0.0346 -0.0122 531 GLN A CB 4050 C CG . GLN A 531 ? 0.4025 0.5748 0.1649 0.0987 -0.0318 0.0040 531 GLN A CG 4051 C CD . GLN A 531 ? 0.4005 0.5791 0.1716 0.1013 -0.0374 0.0042 531 GLN A CD 4052 O OE1 . GLN A 531 ? 0.3919 0.5653 0.1799 0.0921 -0.0397 -0.0030 531 GLN A OE1 4053 N NE2 . GLN A 531 ? 0.3953 0.5853 0.1545 0.1146 -0.0392 0.0132 531 GLN A NE2 4054 N N . PRO A 532 ? 0.3890 0.5462 0.1945 0.0630 -0.0357 -0.0388 532 PRO A N 4055 C CA . PRO A 532 ? 0.3868 0.5412 0.1991 0.0562 -0.0355 -0.0515 532 PRO A CA 4056 C C . PRO A 532 ? 0.3817 0.5142 0.2008 0.0496 -0.0289 -0.0472 532 PRO A C 4057 O O . PRO A 532 ? 0.3862 0.5159 0.2037 0.0484 -0.0261 -0.0519 532 PRO A O 4058 C CB . PRO A 532 ? 0.3807 0.5438 0.2071 0.0506 -0.0420 -0.0653 532 PRO A CB 4059 C CG . PRO A 532 ? 0.3867 0.5689 0.2081 0.0580 -0.0477 -0.0630 532 PRO A CG 4060 C CD . PRO A 532 ? 0.3832 0.5532 0.1974 0.0630 -0.0427 -0.0447 532 PRO A CD 4061 N N . LEU A 533 ? 0.3758 0.4950 0.2025 0.0462 -0.0267 -0.0390 533 LEU A N 4062 C CA . LEU A 533 ? 0.3669 0.4682 0.1992 0.0412 -0.0211 -0.0344 533 LEU A CA 4063 C C . LEU A 533 ? 0.3786 0.4763 0.2003 0.0447 -0.0147 -0.0257 533 LEU A C 4064 O O . LEU A 533 ? 0.3859 0.4774 0.2096 0.0421 -0.0109 -0.0274 533 LEU A O 4065 C CB . LEU A 533 ? 0.3547 0.4456 0.1956 0.0378 -0.0204 -0.0277 533 LEU A CB 4066 C CG . LEU A 533 ? 0.3499 0.4399 0.2041 0.0321 -0.0241 -0.0349 533 LEU A CG 4067 C CD1 . LEU A 533 ? 0.3231 0.4058 0.1824 0.0308 -0.0230 -0.0268 533 LEU A CD1 4068 C CD2 . LEU A 533 ? 0.3343 0.4149 0.1967 0.0264 -0.0225 -0.0420 533 LEU A CD2 4069 N N . LEU A 534 ? 0.3837 0.4852 0.1948 0.0509 -0.0131 -0.0160 534 LEU A N 4070 C CA . LEU A 534 ? 0.4015 0.5002 0.2016 0.0546 -0.0058 -0.0068 534 LEU A CA 4071 C C . LEU A 534 ? 0.4078 0.5163 0.1997 0.0569 -0.0047 -0.0131 534 LEU A C 4072 O O . LEU A 534 ? 0.4123 0.5154 0.2036 0.0549 0.0017 -0.0111 534 LEU A O 4073 C CB . LEU A 534 ? 0.4124 0.5140 0.2014 0.0624 -0.0047 0.0045 534 LEU A CB 4074 C CG . LEU A 534 ? 0.4252 0.5116 0.2141 0.0625 0.0023 0.0180 534 LEU A CG 4075 C CD1 . LEU A 534 ? 0.3712 0.4425 0.1733 0.0536 0.0059 0.0178 534 LEU A CD1 4076 C CD2 . LEU A 534 ? 0.4183 0.5073 0.2039 0.0692 -0.0008 0.0244 534 LEU A CD2 4077 N N . ALA A 535 ? 0.4078 0.5323 0.1942 0.0611 -0.0108 -0.0217 535 ALA A N 4078 C CA . ALA A 535 ? 0.4123 0.5484 0.1898 0.0642 -0.0102 -0.0291 535 ALA A CA 4079 C C . ALA A 535 ? 0.4044 0.5331 0.1920 0.0579 -0.0081 -0.0382 535 ALA A C 4080 O O . ALA A 535 ? 0.4133 0.5445 0.1948 0.0595 -0.0030 -0.0387 535 ALA A O 4081 C CB . ALA A 535 ? 0.4158 0.5722 0.1882 0.0689 -0.0185 -0.0400 535 ALA A CB 4082 N N . ALA A 536 ? 0.3820 0.5017 0.1847 0.0513 -0.0113 -0.0444 536 ALA A N 4083 C CA . ALA A 536 ? 0.3799 0.4915 0.1925 0.0467 -0.0096 -0.0523 536 ALA A CA 4084 C C . ALA A 536 ? 0.3704 0.4699 0.1868 0.0443 -0.0028 -0.0436 536 ALA A C 4085 O O . ALA A 536 ? 0.3802 0.4776 0.2001 0.0435 0.0002 -0.0482 536 ALA A O 4086 C CB . ALA A 536 ? 0.3712 0.4767 0.1979 0.0412 -0.0146 -0.0612 536 ALA A CB 4087 N N . SER A 537 ? 0.3662 0.4591 0.1826 0.0433 -0.0004 -0.0320 537 SER A N 4088 C CA . SER A 537 ? 0.3609 0.4429 0.1847 0.0394 0.0046 -0.0260 537 SER A CA 4089 C C . SER A 537 ? 0.3653 0.4488 0.1824 0.0407 0.0127 -0.0185 537 SER A C 4090 O O . SER A 537 ? 0.3750 0.4630 0.1806 0.0447 0.0153 -0.0119 537 SER A O 4091 C CB . SER A 537 ? 0.3507 0.4237 0.1806 0.0364 0.0032 -0.0195 537 SER A CB 4092 O OG . SER A 537 ? 0.3563 0.4288 0.1926 0.0348 -0.0032 -0.0257 537 SER A OG 4093 N N . ASP A 538 ? 0.3563 0.4365 0.1810 0.0375 0.0169 -0.0194 538 ASP A N 4094 C CA . ASP A 538 ? 0.3579 0.4388 0.1803 0.0365 0.0256 -0.0125 538 ASP A CA 4095 C C . ASP A 538 ? 0.3561 0.4276 0.1813 0.0332 0.0287 -0.0030 538 ASP A C 4096 O O . ASP A 538 ? 0.3690 0.4390 0.1869 0.0341 0.0351 0.0055 538 ASP A O 4097 C CB . ASP A 538 ? 0.3494 0.4326 0.1813 0.0342 0.0285 -0.0180 538 ASP A CB 4098 C CG . ASP A 538 ? 0.3581 0.4498 0.1872 0.0381 0.0270 -0.0273 538 ASP A CG 4099 O OD1 . ASP A 538 ? 0.3887 0.4779 0.2234 0.0388 0.0211 -0.0352 538 ASP A OD1 4100 O OD2 . ASP A 538 ? 0.3145 0.4148 0.1356 0.0406 0.0325 -0.0268 538 ASP A OD2 4101 N N . ALA A 539 ? 0.3350 0.3995 0.1703 0.0297 0.0246 -0.0044 539 ALA A N 4102 C CA . ALA A 539 ? 0.3356 0.3912 0.1740 0.0268 0.0265 0.0026 539 ALA A CA 4103 C C . ALA A 539 ? 0.3292 0.3813 0.1699 0.0275 0.0190 0.0012 539 ALA A C 4104 O O . ALA A 539 ? 0.3208 0.3752 0.1652 0.0277 0.0132 -0.0059 539 ALA A O 4105 C CB . ALA A 539 ? 0.3228 0.3756 0.1726 0.0211 0.0304 0.0017 539 ALA A CB 4106 N N . LEU A 540 ? 0.3341 0.3801 0.1730 0.0278 0.0197 0.0078 540 LEU A N 4107 C CA . LEU A 540 ? 0.3362 0.3798 0.1785 0.0281 0.0134 0.0067 540 LEU A CA 4108 C C . LEU A 540 ? 0.3342 0.3689 0.1805 0.0259 0.0163 0.0125 540 LEU A C 4109 O O . LEU A 540 ? 0.3469 0.3767 0.1880 0.0274 0.0221 0.0198 540 LEU A O 4110 C CB . LEU A 540 ? 0.3378 0.3886 0.1718 0.0337 0.0086 0.0063 540 LEU A CB 4111 C CG . LEU A 540 ? 0.3500 0.4021 0.1892 0.0335 0.0017 0.0028 540 LEU A CG 4112 C CD1 . LEU A 540 ? 0.3684 0.4321 0.2037 0.0367 -0.0041 -0.0041 540 LEU A CD1 4113 C CD2 . LEU A 540 ? 0.3684 0.4162 0.2071 0.0355 0.0021 0.0100 540 LEU A CD2 4114 N N . VAL A 541 ? 0.3162 0.3480 0.1711 0.0227 0.0128 0.0091 541 VAL A N 4115 C CA . VAL A 541 ? 0.3070 0.3314 0.1670 0.0203 0.0147 0.0122 541 VAL A CA 4116 C C . VAL A 541 ? 0.3059 0.3302 0.1670 0.0223 0.0095 0.0122 541 VAL A C 4117 O O . VAL A 541 ? 0.3006 0.3290 0.1652 0.0216 0.0043 0.0074 541 VAL A O 4118 C CB . VAL A 541 ? 0.2961 0.3199 0.1653 0.0152 0.0156 0.0078 541 VAL A CB 4119 C CG1 . VAL A 541 ? 0.2787 0.2964 0.1533 0.0126 0.0170 0.0089 541 VAL A CG1 4120 C CG2 . VAL A 541 ? 0.2733 0.2997 0.1435 0.0129 0.0210 0.0068 541 VAL A CG2 4121 N N . ALA A 542 ? 0.3092 0.3286 0.1681 0.0248 0.0116 0.0178 542 ALA A N 4122 C CA . ALA A 542 ? 0.3102 0.3300 0.1724 0.0262 0.0077 0.0177 542 ALA A CA 4123 C C . ALA A 542 ? 0.3013 0.3156 0.1715 0.0215 0.0093 0.0157 542 ALA A C 4124 O O . ALA A 542 ? 0.2937 0.3003 0.1650 0.0204 0.0146 0.0183 542 ALA A O 4125 C CB . ALA A 542 ? 0.3177 0.3355 0.1739 0.0326 0.0092 0.0245 542 ALA A CB 4126 N N . ALA A 543 ? 0.2975 0.3155 0.1729 0.0188 0.0053 0.0108 543 ALA A N 4127 C CA . ALA A 543 ? 0.2955 0.3113 0.1770 0.0152 0.0060 0.0084 543 ALA A CA 4128 C C . ALA A 543 ? 0.2953 0.3110 0.1798 0.0161 0.0044 0.0088 543 ALA A C 4129 O O . ALA A 543 ? 0.2929 0.3078 0.1812 0.0138 0.0051 0.0069 543 ALA A O 4130 C CB . ALA A 543 ? 0.2934 0.3131 0.1779 0.0130 0.0036 0.0043 543 ALA A CB 4131 N N . TRP A 544 ? 0.2932 0.3116 0.1758 0.0198 0.0022 0.0108 544 TRP A N 4132 C CA . TRP A 544 ? 0.2888 0.3093 0.1749 0.0212 0.0008 0.0111 544 TRP A CA 4133 C C . TRP A 544 ? 0.2831 0.3066 0.1743 0.0176 -0.0010 0.0077 544 TRP A C 4134 O O . TRP A 544 ? 0.2759 0.3018 0.1677 0.0157 -0.0032 0.0056 544 TRP A O 4135 C CB . TRP A 544 ? 0.2974 0.3110 0.1839 0.0229 0.0050 0.0135 544 TRP A CB 4136 C CG . TRP A 544 ? 0.3097 0.3168 0.1908 0.0261 0.0089 0.0182 544 TRP A CG 4137 C CD1 . TRP A 544 ? 0.3156 0.3142 0.1961 0.0235 0.0144 0.0190 544 TRP A CD1 4138 C CD2 . TRP A 544 ? 0.3276 0.3369 0.2028 0.0328 0.0079 0.0231 544 TRP A CD2 4139 N NE1 . TRP A 544 ? 0.3269 0.3202 0.2013 0.0278 0.0180 0.0251 544 TRP A NE1 4140 C CE2 . TRP A 544 ? 0.3380 0.3380 0.2081 0.0344 0.0138 0.0282 544 TRP A CE2 4141 C CE3 . TRP A 544 ? 0.3203 0.3402 0.1946 0.0377 0.0028 0.0234 544 TRP A CE3 4142 C CZ2 . TRP A 544 ? 0.3481 0.3478 0.2099 0.0419 0.0149 0.0351 544 TRP A CZ2 4143 C CZ3 . TRP A 544 ? 0.3388 0.3610 0.2056 0.0453 0.0027 0.0288 544 TRP A CZ3 4144 C CH2 . TRP A 544 ? 0.3513 0.3629 0.2109 0.0480 0.0088 0.0354 544 TRP A CH2 4145 N N . LEU A 545 ? 0.2811 0.3039 0.1753 0.0170 0.0004 0.0074 545 LEU A N 4146 C CA . LEU A 545 ? 0.2812 0.3067 0.1786 0.0143 -0.0002 0.0057 545 LEU A CA 4147 C C . LEU A 545 ? 0.2786 0.3020 0.1757 0.0129 0.0021 0.0041 545 LEU A C 4148 O O . LEU A 545 ? 0.2844 0.3083 0.1828 0.0133 0.0037 0.0032 545 LEU A O 4149 C CB . LEU A 545 ? 0.2671 0.2977 0.1685 0.0151 -0.0007 0.0059 545 LEU A CB 4150 C CG . LEU A 545 ? 0.2828 0.3192 0.1863 0.0162 -0.0036 0.0055 545 LEU A CG 4151 C CD1 . LEU A 545 ? 0.2534 0.2968 0.1622 0.0177 -0.0036 0.0053 545 LEU A CD1 4152 C CD2 . LEU A 545 ? 0.2510 0.2883 0.1562 0.0127 -0.0052 0.0034 545 LEU A CD2 4153 N N . PRO A 546 ? 0.2860 0.3085 0.1816 0.0115 0.0021 0.0029 546 PRO A N 4154 C CA . PRO A 546 ? 0.2819 0.3047 0.1781 0.0100 0.0041 -0.0001 546 PRO A CA 4155 C C . PRO A 546 ? 0.2803 0.3084 0.1769 0.0100 0.0037 -0.0021 546 PRO A C 4156 O O . PRO A 546 ? 0.2782 0.3089 0.1761 0.0088 0.0050 -0.0063 546 PRO A O 4157 C CB . PRO A 546 ? 0.2837 0.3074 0.1792 0.0091 0.0036 -0.0010 546 PRO A CB 4158 C CG . PRO A 546 ? 0.2834 0.3075 0.1775 0.0104 0.0009 0.0011 546 PRO A CG 4159 C CD . PRO A 546 ? 0.2810 0.3037 0.1753 0.0113 0.0003 0.0031 546 PRO A CD 4160 N N . GLY A 547 ? 0.2771 0.3075 0.1729 0.0111 0.0023 0.0005 547 GLY A N 4161 C CA . GLY A 547 ? 0.2754 0.3112 0.1699 0.0121 0.0027 0.0001 547 GLY A CA 4162 C C . GLY A 547 ? 0.2785 0.3183 0.1702 0.0137 0.0013 0.0010 547 GLY A C 4163 O O . GLY A 547 ? 0.2873 0.3242 0.1789 0.0141 0.0002 0.0027 547 GLY A O 4164 N N . SER A 548 ? 0.2795 0.3266 0.1685 0.0156 0.0014 -0.0003 548 SER A N 4165 C CA . SER A 548 ? 0.2913 0.3435 0.1763 0.0193 0.0001 0.0021 548 SER A CA 4166 C C . SER A 548 ? 0.2936 0.3504 0.1798 0.0200 -0.0021 -0.0018 548 SER A C 4167 O O . SER A 548 ? 0.3016 0.3609 0.1853 0.0240 -0.0034 0.0010 548 SER A O 4168 C CB . SER A 548 ? 0.2862 0.3473 0.1662 0.0225 0.0007 0.0023 548 SER A CB 4169 O OG . SER A 548 ? 0.2774 0.3460 0.1588 0.0210 0.0005 -0.0056 548 SER A OG 4170 N N . GLU A 549 ? 0.2980 0.3557 0.1885 0.0163 -0.0017 -0.0079 549 GLU A N 4171 C CA . GLU A 549 ? 0.3019 0.3675 0.1953 0.0159 -0.0029 -0.0132 549 GLU A CA 4172 C C . GLU A 549 ? 0.3008 0.3603 0.1972 0.0141 -0.0023 -0.0125 549 GLU A C 4173 O O . GLU A 549 ? 0.3003 0.3573 0.2008 0.0098 -0.0001 -0.0160 549 GLU A O 4174 C CB . GLU A 549 ? 0.3004 0.3731 0.1979 0.0124 -0.0018 -0.0219 549 GLU A CB 4175 C CG . GLU A 549 ? 0.3098 0.3917 0.2036 0.0148 -0.0027 -0.0246 549 GLU A CG 4176 C CD . GLU A 549 ? 0.3286 0.4198 0.2155 0.0218 -0.0056 -0.0200 549 GLU A CD 4177 O OE1 . GLU A 549 ? 0.3385 0.4382 0.2258 0.0247 -0.0082 -0.0210 549 GLU A OE1 4178 O OE2 . GLU A 549 ? 0.3289 0.4190 0.2099 0.0247 -0.0048 -0.0150 549 GLU A OE2 4179 N N . GLY A 550 ? 0.3051 0.3620 0.1992 0.0175 -0.0037 -0.0078 550 GLY A N 4180 C CA . GLY A 550 ? 0.2952 0.3463 0.1909 0.0166 -0.0032 -0.0070 550 GLY A CA 4181 C C . GLY A 550 ? 0.2978 0.3564 0.1977 0.0154 -0.0028 -0.0120 550 GLY A C 4182 O O . GLY A 550 ? 0.2833 0.3381 0.1844 0.0139 -0.0014 -0.0121 550 GLY A O 4183 N N . GLN A 551 ? 0.2979 0.3688 0.2002 0.0160 -0.0039 -0.0169 551 GLN A N 4184 C CA . GLN A 551 ? 0.2995 0.3805 0.2083 0.0135 -0.0030 -0.0234 551 GLN A CA 4185 C C . GLN A 551 ? 0.2950 0.3705 0.2084 0.0062 0.0016 -0.0267 551 GLN A C 4186 O O . GLN A 551 ? 0.2917 0.3717 0.2106 0.0030 0.0041 -0.0305 551 GLN A O 4187 C CB . GLN A 551 ? 0.2993 0.3981 0.2106 0.0160 -0.0058 -0.0293 551 GLN A CB 4188 C CG . GLN A 551 ? 0.3255 0.4312 0.2329 0.0248 -0.0096 -0.0256 551 GLN A CG 4189 C CD . GLN A 551 ? 0.3703 0.4947 0.2772 0.0297 -0.0133 -0.0296 551 GLN A CD 4190 O OE1 . GLN A 551 ? 0.3984 0.5391 0.3098 0.0328 -0.0156 -0.0346 551 GLN A OE1 4191 N NE2 . GLN A 551 ? 0.3463 0.4704 0.2476 0.0309 -0.0141 -0.0280 551 GLN A NE2 4192 N N . GLY A 552 ? 0.2972 0.3629 0.2085 0.0038 0.0034 -0.0248 552 GLY A N 4193 C CA . GLY A 552 ? 0.2958 0.3520 0.2097 -0.0014 0.0085 -0.0251 552 GLY A CA 4194 C C . GLY A 552 ? 0.3029 0.3519 0.2144 -0.0012 0.0106 -0.0203 552 GLY A C 4195 O O . GLY A 552 ? 0.3055 0.3516 0.2203 -0.0051 0.0156 -0.0213 552 GLY A O 4196 N N . VAL A 553 ? 0.2945 0.3408 0.2006 0.0033 0.0073 -0.0154 553 VAL A N 4197 C CA . VAL A 553 ? 0.2859 0.3282 0.1890 0.0045 0.0081 -0.0123 553 VAL A CA 4198 C C . VAL A 553 ? 0.2836 0.3344 0.1906 0.0040 0.0095 -0.0158 553 VAL A C 4199 O O . VAL A 553 ? 0.2804 0.3296 0.1877 0.0017 0.0137 -0.0154 553 VAL A O 4200 C CB . VAL A 553 ? 0.2853 0.3239 0.1836 0.0087 0.0043 -0.0086 553 VAL A CB 4201 C CG1 . VAL A 553 ? 0.2668 0.3031 0.1622 0.0099 0.0049 -0.0075 553 VAL A CG1 4202 C CG2 . VAL A 553 ? 0.2800 0.3125 0.1760 0.0089 0.0033 -0.0056 553 VAL A CG2 4203 N N . THR A 554 ? 0.2822 0.3429 0.1919 0.0067 0.0063 -0.0189 554 THR A N 4204 C CA . THR A 554 ? 0.2810 0.3525 0.1955 0.0074 0.0071 -0.0229 554 THR A CA 4205 C C . THR A 554 ? 0.2843 0.3642 0.2072 0.0011 0.0114 -0.0289 554 THR A C 4206 O O . THR A 554 ? 0.2857 0.3729 0.2133 -0.0003 0.0144 -0.0317 554 THR A O 4207 C CB . THR A 554 ? 0.2795 0.3596 0.1942 0.0140 0.0023 -0.0237 554 THR A CB 4208 O OG1 . THR A 554 ? 0.2877 0.3734 0.2029 0.0147 -0.0003 -0.0251 554 THR A OG1 4209 C CG2 . THR A 554 ? 0.2622 0.3316 0.1702 0.0189 0.0002 -0.0183 554 THR A CG2 4210 N N . ASP A 555 ? 0.2828 0.3614 0.2082 -0.0029 0.0124 -0.0314 555 ASP A N 4211 C CA . ASP A 555 ? 0.2896 0.3733 0.2244 -0.0104 0.0177 -0.0381 555 ASP A CA 4212 C C . ASP A 555 ? 0.3006 0.3746 0.2357 -0.0149 0.0252 -0.0348 555 ASP A C 4213 O O . ASP A 555 ? 0.3097 0.3900 0.2533 -0.0206 0.0307 -0.0396 555 ASP A O 4214 C CB . ASP A 555 ? 0.2838 0.3638 0.2202 -0.0136 0.0180 -0.0411 555 ASP A CB 4215 C CG . ASP A 555 ? 0.2947 0.3904 0.2336 -0.0111 0.0124 -0.0477 555 ASP A CG 4216 O OD1 . ASP A 555 ? 0.2999 0.4098 0.2397 -0.0064 0.0081 -0.0495 555 ASP A OD1 4217 O OD2 . ASP A 555 ? 0.2965 0.3910 0.2359 -0.0130 0.0122 -0.0511 555 ASP A OD2 4218 N N . ALA A 556 ? 0.3029 0.3625 0.2287 -0.0121 0.0257 -0.0266 556 ALA A N 4219 C CA . ALA A 556 ? 0.3104 0.3609 0.2330 -0.0141 0.0325 -0.0215 556 ALA A CA 4220 C C . ALA A 556 ? 0.3076 0.3637 0.2265 -0.0104 0.0319 -0.0197 556 ALA A C 4221 O O . ALA A 556 ? 0.3104 0.3689 0.2318 -0.0134 0.0382 -0.0198 556 ALA A O 4222 C CB . ALA A 556 ? 0.3127 0.3477 0.2270 -0.0119 0.0334 -0.0140 556 ALA A CB 4223 N N . LEU A 557 ? 0.2986 0.3565 0.2122 -0.0041 0.0250 -0.0185 557 LEU A N 4224 C CA . LEU A 557 ? 0.3009 0.3635 0.2114 -0.0001 0.0242 -0.0183 557 LEU A CA 4225 C C . LEU A 557 ? 0.3006 0.3772 0.2196 -0.0018 0.0269 -0.0241 557 LEU A C 4226 O O . LEU A 557 ? 0.2981 0.3777 0.2156 -0.0012 0.0306 -0.0236 557 LEU A O 4227 C CB . LEU A 557 ? 0.2938 0.3554 0.2000 0.0062 0.0170 -0.0177 557 LEU A CB 4228 C CG . LEU A 557 ? 0.3094 0.3598 0.2081 0.0081 0.0141 -0.0130 557 LEU A CG 4229 C CD1 . LEU A 557 ? 0.2982 0.3480 0.1955 0.0129 0.0085 -0.0136 557 LEU A CD1 4230 C CD2 . LEU A 557 ? 0.3070 0.3524 0.1984 0.0086 0.0171 -0.0094 557 LEU A CD2 4231 N N . PHE A 558 ? 0.2986 0.3860 0.2265 -0.0033 0.0249 -0.0299 558 PHE A N 4232 C CA . PHE A 558 ? 0.2915 0.3962 0.2292 -0.0041 0.0263 -0.0367 558 PHE A CA 4233 C C . PHE A 558 ? 0.3009 0.4113 0.2491 -0.0134 0.0338 -0.0414 558 PHE A C 4234 O O . PHE A 558 ? 0.2904 0.4179 0.2495 -0.0156 0.0355 -0.0485 558 PHE A O 4235 C CB . PHE A 558 ? 0.2920 0.4089 0.2330 0.0018 0.0188 -0.0407 558 PHE A CB 4236 C CG . PHE A 558 ? 0.3002 0.4122 0.2334 0.0108 0.0137 -0.0367 558 PHE A CG 4237 C CD1 . PHE A 558 ? 0.3210 0.4236 0.2476 0.0147 0.0087 -0.0325 558 PHE A CD1 4238 C CD2 . PHE A 558 ? 0.2922 0.4082 0.2252 0.0150 0.0148 -0.0374 558 PHE A CD2 4239 C CE1 . PHE A 558 ? 0.3303 0.4263 0.2510 0.0219 0.0053 -0.0290 558 PHE A CE1 4240 C CE2 . PHE A 558 ? 0.3036 0.4131 0.2304 0.0227 0.0109 -0.0347 558 PHE A CE2 4241 C CZ . PHE A 558 ? 0.3070 0.4055 0.2280 0.0259 0.0064 -0.0304 558 PHE A CZ 4242 N N . GLY A 559 ? 0.3013 0.3974 0.2472 -0.0188 0.0388 -0.0378 559 GLY A N 4243 C CA . GLY A 559 ? 0.3208 0.4170 0.2762 -0.0284 0.0482 -0.0410 559 GLY A CA 4244 C C . GLY A 559 ? 0.3264 0.4327 0.2950 -0.0348 0.0480 -0.0511 559 GLY A C 4245 O O . GLY A 559 ? 0.3321 0.4417 0.3119 -0.0438 0.0561 -0.0564 559 GLY A O 4246 N N . ASP A 560 ? 0.3297 0.4413 0.2971 -0.0306 0.0394 -0.0543 560 ASP A N 4247 C CA . ASP A 560 ? 0.3443 0.4649 0.3223 -0.0363 0.0389 -0.0644 560 ASP A CA 4248 C C . ASP A 560 ? 0.3512 0.4537 0.3309 -0.0441 0.0467 -0.0634 560 ASP A C 4249 O O . ASP A 560 ? 0.3585 0.4661 0.3508 -0.0529 0.0514 -0.0731 560 ASP A O 4250 C CB . ASP A 560 ? 0.3464 0.4749 0.3196 -0.0290 0.0286 -0.0661 560 ASP A CB 4251 C CG . ASP A 560 ? 0.3779 0.5267 0.3525 -0.0214 0.0219 -0.0689 560 ASP A CG 4252 O OD1 . ASP A 560 ? 0.4068 0.5696 0.3907 -0.0237 0.0248 -0.0738 560 ASP A OD1 4253 O OD2 . ASP A 560 ? 0.4317 0.5825 0.3984 -0.0128 0.0142 -0.0658 560 ASP A OD2 4254 N N . PHE A 561 ? 0.3488 0.4304 0.3162 -0.0407 0.0484 -0.0522 561 PHE A N 4255 C CA . PHE A 561 ? 0.3597 0.4213 0.3267 -0.0458 0.0567 -0.0485 561 PHE A CA 4256 C C . PHE A 561 ? 0.3627 0.4099 0.3190 -0.0425 0.0615 -0.0362 561 PHE A C 4257 O O . PHE A 561 ? 0.3624 0.4129 0.3093 -0.0351 0.0559 -0.0309 561 PHE A O 4258 C CB . PHE A 561 ? 0.3521 0.4049 0.3137 -0.0425 0.0518 -0.0478 561 PHE A CB 4259 C CG . PHE A 561 ? 0.3605 0.4278 0.3312 -0.0454 0.0475 -0.0602 561 PHE A CG 4260 C CD1 . PHE A 561 ? 0.3451 0.4294 0.3129 -0.0389 0.0373 -0.0632 561 PHE A CD1 4261 C CD2 . PHE A 561 ? 0.3549 0.4193 0.3372 -0.0545 0.0542 -0.0694 561 PHE A CD2 4262 C CE1 . PHE A 561 ? 0.3357 0.4363 0.3106 -0.0405 0.0331 -0.0746 561 PHE A CE1 4263 C CE2 . PHE A 561 ? 0.3748 0.4556 0.3655 -0.0571 0.0498 -0.0826 561 PHE A CE2 4264 C CZ . PHE A 561 ? 0.3517 0.4518 0.3378 -0.0496 0.0388 -0.0850 561 PHE A CZ 4265 N N . GLY A 562 ? 0.3705 0.4018 0.3280 -0.0476 0.0723 -0.0318 562 GLY A N 4266 C CA . GLY A 562 ? 0.3729 0.3896 0.3176 -0.0427 0.0769 -0.0186 562 GLY A CA 4267 C C . GLY A 562 ? 0.3604 0.3646 0.2927 -0.0347 0.0714 -0.0110 562 GLY A C 4268 O O . GLY A 562 ? 0.3608 0.3612 0.2960 -0.0351 0.0683 -0.0148 562 GLY A O 4269 N N . PHE A 563 ? 0.3602 0.3597 0.2792 -0.0273 0.0701 -0.0010 563 PHE A N 4270 C CA . PHE A 563 ? 0.3528 0.3420 0.2606 -0.0194 0.0657 0.0066 563 PHE A CA 4271 C C . PHE A 563 ? 0.3625 0.3329 0.2695 -0.0202 0.0747 0.0129 563 PHE A C 4272 O O . PHE A 563 ? 0.3743 0.3364 0.2808 -0.0229 0.0851 0.0181 563 PHE A O 4273 C CB . PHE A 563 ? 0.3535 0.3455 0.2481 -0.0117 0.0625 0.0142 563 PHE A CB 4274 C CG . PHE A 563 ? 0.3339 0.3394 0.2270 -0.0082 0.0520 0.0094 563 PHE A CG 4275 C CD1 . PHE A 563 ? 0.3371 0.3551 0.2335 -0.0097 0.0513 0.0046 563 PHE A CD1 4276 C CD2 . PHE A 563 ? 0.3087 0.3139 0.1978 -0.0032 0.0436 0.0097 563 PHE A CD2 4277 C CE1 . PHE A 563 ? 0.3170 0.3448 0.2120 -0.0057 0.0425 0.0007 563 PHE A CE1 4278 C CE2 . PHE A 563 ? 0.2965 0.3115 0.1847 -0.0004 0.0354 0.0059 563 PHE A CE2 4279 C CZ . PHE A 563 ? 0.3027 0.3280 0.1937 -0.0014 0.0349 0.0016 563 PHE A CZ 4280 N N . THR A 564 ? 0.3584 0.3212 0.2651 -0.0176 0.0716 0.0127 564 THR A N 4281 C CA . THR A 564 ? 0.3733 0.3164 0.2799 -0.0172 0.0805 0.0184 564 THR A CA 4282 C C . THR A 564 ? 0.3759 0.3116 0.2726 -0.0072 0.0760 0.0260 564 THR A C 4283 O O . THR A 564 ? 0.3819 0.3009 0.2756 -0.0039 0.0833 0.0335 564 THR A O 4284 C CB . THR A 564 ? 0.3786 0.3163 0.2997 -0.0263 0.0857 0.0082 564 THR A CB 4285 O OG1 . THR A 564 ? 0.3733 0.3231 0.2985 -0.0263 0.0757 -0.0014 564 THR A OG1 4286 C CG2 . THR A 564 ? 0.3933 0.3354 0.3260 -0.0370 0.0936 0.0015 564 THR A CG2 4287 N N . GLY A 565 ? 0.3635 0.3115 0.2561 -0.0023 0.0647 0.0241 565 GLY A N 4288 C CA . GLY A 565 ? 0.3648 0.3098 0.2502 0.0066 0.0598 0.0295 565 GLY A CA 4289 C C . GLY A 565 ? 0.3870 0.3252 0.2604 0.0150 0.0632 0.0418 565 GLY A C 4290 O O . GLY A 565 ? 0.3905 0.3327 0.2579 0.0155 0.0651 0.0457 565 GLY A O 4291 N N . ARG A 566 ? 0.3917 0.3206 0.2613 0.0224 0.0640 0.0478 566 ARG A N 4292 C CA . ARG A 566 ? 0.4083 0.3330 0.2654 0.0331 0.0658 0.0600 566 ARG A CA 4293 C C . ARG A 566 ? 0.4024 0.3355 0.2560 0.0421 0.0566 0.0609 566 ARG A C 4294 O O . ARG A 566 ? 0.3839 0.3162 0.2450 0.0409 0.0539 0.0553 566 ARG A O 4295 C CB . ARG A 566 ? 0.4345 0.3373 0.2909 0.0345 0.0787 0.0684 566 ARG A CB 4296 C CG . ARG A 566 ? 0.4679 0.3633 0.3292 0.0245 0.0891 0.0674 566 ARG A CG 4297 C CD . ARG A 566 ? 0.5374 0.4095 0.3972 0.0258 0.1037 0.0774 566 ARG A CD 4298 N NE . ARG A 566 ? 0.5816 0.4374 0.4495 0.0255 0.1080 0.0751 566 ARG A NE 4299 C CZ . ARG A 566 ? 0.6155 0.4619 0.4980 0.0141 0.1146 0.0653 566 ARG A CZ 4300 N NH1 . ARG A 566 ? 0.6162 0.4476 0.5051 0.0152 0.1185 0.0630 566 ARG A NH1 4301 N NH2 . ARG A 566 ? 0.6191 0.4722 0.5104 0.0019 0.1176 0.0571 566 ARG A NH2 4302 N N . LEU A 567 ? 0.3971 0.3399 0.2397 0.0510 0.0519 0.0671 567 LEU A N 4303 C CA . LEU A 567 ? 0.3907 0.3453 0.2314 0.0589 0.0427 0.0665 567 LEU A CA 4304 C C . LEU A 567 ? 0.3992 0.3430 0.2430 0.0648 0.0456 0.0699 567 LEU A C 4305 O O . LEU A 567 ? 0.4204 0.3489 0.2592 0.0709 0.0539 0.0794 567 LEU A O 4306 C CB . LEU A 567 ? 0.3981 0.3649 0.2261 0.0686 0.0385 0.0728 567 LEU A CB 4307 C CG . LEU A 567 ? 0.3893 0.3708 0.2138 0.0648 0.0335 0.0678 567 LEU A CG 4308 C CD1 . LEU A 567 ? 0.4122 0.4076 0.2243 0.0756 0.0285 0.0726 567 LEU A CD1 4309 C CD2 . LEU A 567 ? 0.3636 0.3555 0.1983 0.0569 0.0256 0.0558 567 LEU A CD2 4310 N N . PRO A 568 ? 0.3887 0.3396 0.2409 0.0633 0.0396 0.0623 568 PRO A N 4311 C CA . PRO A 568 ? 0.3992 0.3430 0.2545 0.0701 0.0413 0.0645 568 PRO A CA 4312 C C . PRO A 568 ? 0.4097 0.3674 0.2593 0.0826 0.0345 0.0693 568 PRO A C 4313 O O . PRO A 568 ? 0.4089 0.3644 0.2611 0.0901 0.0348 0.0711 568 PRO A O 4314 C CB . PRO A 568 ? 0.3751 0.3236 0.2418 0.0618 0.0379 0.0531 568 PRO A CB 4315 C CG . PRO A 568 ? 0.3576 0.3231 0.2247 0.0560 0.0299 0.0471 568 PRO A CG 4316 C CD . PRO A 568 ? 0.3625 0.3276 0.2216 0.0554 0.0318 0.0517 568 PRO A CD 4317 N N . ARG A 569 ? 0.4084 0.3817 0.2510 0.0846 0.0284 0.0700 569 ARG A N 4318 C CA . ARG A 569 ? 0.4080 0.4006 0.2461 0.0949 0.0202 0.0716 569 ARG A CA 4319 C C . ARG A 569 ? 0.4116 0.4095 0.2363 0.1005 0.0201 0.0783 569 ARG A C 4320 O O . ARG A 569 ? 0.4120 0.4045 0.2337 0.0933 0.0236 0.0779 569 ARG A O 4321 C CB . ARG A 569 ? 0.3891 0.4014 0.2350 0.0882 0.0107 0.0602 569 ARG A CB 4322 C CG . ARG A 569 ? 0.3889 0.4026 0.2469 0.0830 0.0090 0.0529 569 ARG A CG 4323 C CD . ARG A 569 ? 0.3767 0.4131 0.2402 0.0823 -0.0002 0.0456 569 ARG A CD 4324 N NE . ARG A 569 ? 0.4101 0.4603 0.2705 0.0949 -0.0043 0.0494 569 ARG A NE 4325 C CZ . ARG A 569 ? 0.4026 0.4526 0.2665 0.1031 -0.0032 0.0524 569 ARG A CZ 4326 N NH1 . ARG A 569 ? 0.4093 0.4744 0.2700 0.1157 -0.0076 0.0559 569 ARG A NH1 4327 N NH2 . ARG A 569 ? 0.3918 0.4277 0.2622 0.0995 0.0022 0.0512 569 ARG A NH2 4328 N N . THR A 570 ? 0.4169 0.4284 0.2338 0.1135 0.0154 0.0835 570 THR A N 4329 C CA . THR A 570 ? 0.4165 0.4403 0.2198 0.1202 0.0128 0.0880 570 THR A CA 4330 C C . THR A 570 ? 0.4027 0.4462 0.2102 0.1117 0.0039 0.0754 570 THR A C 4331 O O . THR A 570 ? 0.3805 0.4369 0.1989 0.1077 -0.0032 0.0657 570 THR A O 4332 C CB . THR A 570 ? 0.4273 0.4647 0.2222 0.1378 0.0086 0.0955 570 THR A CB 4333 O OG1 . THR A 570 ? 0.4506 0.4666 0.2397 0.1472 0.0182 0.1090 570 THR A OG1 4334 C CG2 . THR A 570 ? 0.4317 0.4884 0.2123 0.1454 0.0037 0.0977 570 THR A CG2 4335 N N . TRP A 571 ? 0.4065 0.4517 0.2059 0.1087 0.0052 0.0754 571 TRP A N 4336 C CA . TRP A 571 ? 0.4002 0.4647 0.2017 0.1032 -0.0030 0.0639 571 TRP A CA 4337 C C . TRP A 571 ? 0.4166 0.5025 0.2059 0.1153 -0.0090 0.0656 571 TRP A C 4338 O O . TRP A 571 ? 0.4339 0.5175 0.2082 0.1231 -0.0046 0.0752 571 TRP A O 4339 C CB . TRP A 571 ? 0.3979 0.4544 0.1990 0.0928 0.0011 0.0604 571 TRP A CB 4340 C CG . TRP A 571 ? 0.3830 0.4507 0.1936 0.0833 -0.0058 0.0467 571 TRP A CG 4341 C CD1 . TRP A 571 ? 0.3747 0.4630 0.1844 0.0848 -0.0140 0.0381 571 TRP A CD1 4342 C CD2 . TRP A 571 ? 0.3730 0.4316 0.1958 0.0713 -0.0046 0.0398 571 TRP A CD2 4343 N NE1 . TRP A 571 ? 0.3573 0.4472 0.1786 0.0739 -0.0171 0.0268 571 TRP A NE1 4344 C CE2 . TRP A 571 ? 0.3550 0.4270 0.1835 0.0663 -0.0116 0.0284 571 TRP A CE2 4345 C CE3 . TRP A 571 ? 0.3709 0.4120 0.2003 0.0646 0.0017 0.0417 571 TRP A CE3 4346 C CZ2 . TRP A 571 ? 0.3413 0.4081 0.1805 0.0559 -0.0119 0.0210 571 TRP A CZ2 4347 C CZ3 . TRP A 571 ? 0.3449 0.3841 0.1847 0.0546 0.0002 0.0334 571 TRP A CZ3 4348 C CH2 . TRP A 571 ? 0.3381 0.3892 0.1821 0.0509 -0.0062 0.0241 571 TRP A CH2 4349 N N . PHE A 572 ? 0.4076 0.5155 0.2038 0.1165 -0.0189 0.0560 572 PHE A N 4350 C CA . PHE A 572 ? 0.4193 0.5528 0.2062 0.1282 -0.0264 0.0549 572 PHE A CA 4351 C C . PHE A 572 ? 0.4193 0.5664 0.1998 0.1247 -0.0301 0.0465 572 PHE A C 4352 O O . PHE A 572 ? 0.4037 0.5451 0.1921 0.1120 -0.0296 0.0374 572 PHE A O 4353 C CB . PHE A 572 ? 0.4079 0.5618 0.2075 0.1296 -0.0354 0.0458 572 PHE A CB 4354 C CG . PHE A 572 ? 0.3919 0.5483 0.2087 0.1142 -0.0387 0.0311 572 PHE A CG 4355 C CD1 . PHE A 572 ? 0.3871 0.5588 0.2062 0.1077 -0.0444 0.0183 572 PHE A CD1 4356 C CD2 . PHE A 572 ? 0.3629 0.5051 0.1931 0.1064 -0.0354 0.0304 572 PHE A CD2 4357 C CE1 . PHE A 572 ? 0.3497 0.5205 0.1845 0.0938 -0.0460 0.0061 572 PHE A CE1 4358 C CE2 . PHE A 572 ? 0.3341 0.4773 0.1787 0.0929 -0.0374 0.0187 572 PHE A CE2 4359 C CZ . PHE A 572 ? 0.3334 0.4897 0.1804 0.0867 -0.0424 0.0072 572 PHE A CZ 4360 N N . LYS A 573 ? 0.4410 0.6066 0.2067 0.1372 -0.0337 0.0495 573 LYS A N 4361 C CA . LYS A 573 ? 0.4438 0.6282 0.2036 0.1356 -0.0389 0.0390 573 LYS A CA 4362 C C . LYS A 573 ? 0.4350 0.6434 0.2094 0.1298 -0.0497 0.0205 573 LYS A C 4363 O O . LYS A 573 ? 0.4264 0.6393 0.2067 0.1196 -0.0521 0.0072 573 LYS A O 4364 C CB . LYS A 573 ? 0.4698 0.6683 0.2076 0.1517 -0.0392 0.0483 573 LYS A CB 4365 C CG . LYS A 573 ? 0.4826 0.6574 0.2055 0.1557 -0.0269 0.0657 573 LYS A CG 4366 C CD . LYS A 573 ? 0.5005 0.6890 0.1999 0.1729 -0.0262 0.0767 573 LYS A CD 4367 C CE . LYS A 573 ? 0.5149 0.6788 0.2012 0.1735 -0.0123 0.0925 573 LYS A CE 4368 N NZ . LYS A 573 ? 0.5710 0.7454 0.2325 0.1908 -0.0095 0.1061 573 LYS A NZ 4369 N N . SER A 574 ? 0.4338 0.6575 0.2148 0.1362 -0.0557 0.0192 574 SER A N 4370 C CA . SER A 574 ? 0.4235 0.6693 0.2213 0.1293 -0.0647 0.0015 574 SER A CA 4371 C C . SER A 574 ? 0.4176 0.6677 0.2282 0.1316 -0.0669 0.0028 574 SER A C 4372 O O . SER A 574 ? 0.4173 0.6610 0.2206 0.1434 -0.0639 0.0168 574 SER A O 4373 C CB . SER A 574 ? 0.4405 0.7201 0.2308 0.1369 -0.0739 -0.0088 574 SER A CB 4374 O OG . SER A 574 ? 0.4689 0.7643 0.2464 0.1551 -0.0770 0.0015 574 SER A OG 4375 N N . VAL A 575 ? 0.4036 0.6643 0.2337 0.1207 -0.0714 -0.0118 575 VAL A N 4376 C CA . VAL A 575 ? 0.4019 0.6679 0.2460 0.1216 -0.0729 -0.0118 575 VAL A CA 4377 C C . VAL A 575 ? 0.4180 0.7127 0.2581 0.1381 -0.0801 -0.0099 575 VAL A C 4378 O O . VAL A 575 ? 0.4203 0.7148 0.2659 0.1443 -0.0793 -0.0037 575 VAL A O 4379 C CB . VAL A 575 ? 0.3819 0.6520 0.2486 0.1053 -0.0746 -0.0271 575 VAL A CB 4380 C CG1 . VAL A 575 ? 0.3685 0.6081 0.2385 0.0915 -0.0668 -0.0258 575 VAL A CG1 4381 C CG2 . VAL A 575 ? 0.3816 0.6815 0.2558 0.1014 -0.0830 -0.0453 575 VAL A CG2 4382 N N . ASP A 576 ? 0.4381 0.7585 0.2682 0.1462 -0.0871 -0.0154 576 ASP A N 4383 C CA . ASP A 576 ? 0.4603 0.8107 0.2855 0.1638 -0.0946 -0.0133 576 ASP A CA 4384 C C . ASP A 576 ? 0.4706 0.8069 0.2763 0.1821 -0.0893 0.0090 576 ASP A C 4385 O O . ASP A 576 ? 0.4763 0.8327 0.2775 0.1987 -0.0941 0.0142 576 ASP A O 4386 C CB . ASP A 576 ? 0.4766 0.8655 0.2998 0.1671 -0.1053 -0.0288 576 ASP A CB 4387 C CG . ASP A 576 ? 0.5283 0.9125 0.3333 0.1677 -0.1038 -0.0281 576 ASP A CG 4388 O OD1 . ASP A 576 ? 0.5959 0.9514 0.3853 0.1711 -0.0949 -0.0116 576 ASP A OD1 4389 O OD2 . ASP A 576 ? 0.5846 0.9951 0.3914 0.1646 -0.1113 -0.0449 576 ASP A OD2 4390 N N . GLN A 577 ? 0.4660 0.7668 0.2616 0.1788 -0.0788 0.0219 577 GLN A N 4391 C CA . GLN A 577 ? 0.4788 0.7580 0.2606 0.1926 -0.0710 0.0430 577 GLN A CA 4392 C C . GLN A 577 ? 0.4707 0.7365 0.2662 0.1924 -0.0674 0.0475 577 GLN A C 4393 O O . GLN A 577 ? 0.4869 0.7414 0.2738 0.2065 -0.0627 0.0627 577 GLN A O 4394 C CB . GLN A 577 ? 0.4793 0.7248 0.2497 0.1862 -0.0600 0.0532 577 GLN A CB 4395 C CG . GLN A 577 ? 0.4776 0.7317 0.2311 0.1887 -0.0608 0.0527 577 GLN A CG 4396 C CD . GLN A 577 ? 0.4646 0.6855 0.2085 0.1830 -0.0488 0.0639 577 GLN A CD 4397 O OE1 . GLN A 577 ? 0.4707 0.6718 0.2264 0.1669 -0.0442 0.0587 577 GLN A OE1 4398 N NE2 . GLN A 577 ? 0.4662 0.6813 0.1890 0.1965 -0.0431 0.0798 577 GLN A NE2 4399 N N . LEU A 578 ? 0.4462 0.7117 0.2624 0.1768 -0.0687 0.0346 578 LEU A N 4400 C CA . LEU A 578 ? 0.4402 0.6881 0.2688 0.1737 -0.0633 0.0384 578 LEU A CA 4401 C C . LEU A 578 ? 0.4493 0.7210 0.2861 0.1864 -0.0691 0.0376 578 LEU A C 4402 O O . LEU A 578 ? 0.4425 0.7493 0.2852 0.1896 -0.0790 0.0265 578 LEU A O 4403 C CB . LEU A 578 ? 0.4129 0.6492 0.2583 0.1527 -0.0610 0.0270 578 LEU A CB 4404 C CG . LEU A 578 ? 0.4050 0.6162 0.2446 0.1403 -0.0547 0.0280 578 LEU A CG 4405 C CD1 . LEU A 578 ? 0.3562 0.5627 0.2125 0.1217 -0.0544 0.0155 578 LEU A CD1 4406 C CD2 . LEU A 578 ? 0.3893 0.5678 0.2178 0.1439 -0.0441 0.0437 578 LEU A CD2 4407 N N . PRO A 579 ? 0.4608 0.7146 0.2989 0.1936 -0.0629 0.0484 579 PRO A N 4408 C CA . PRO A 579 ? 0.4700 0.6839 0.3033 0.1897 -0.0511 0.0598 579 PRO A CA 4409 C C . PRO A 579 ? 0.4984 0.6945 0.3097 0.2016 -0.0450 0.0762 579 PRO A C 4410 O O . PRO A 579 ? 0.5195 0.7321 0.3187 0.2192 -0.0488 0.0835 579 PRO A O 4411 C CB . PRO A 579 ? 0.4673 0.6773 0.3111 0.1963 -0.0486 0.0628 579 PRO A CB 4412 C CG . PRO A 579 ? 0.4786 0.7229 0.3215 0.2142 -0.0575 0.0627 579 PRO A CG 4413 C CD . PRO A 579 ? 0.4675 0.7430 0.3139 0.2070 -0.0676 0.0483 579 PRO A CD 4414 N N . MET A 580 ? 0.5110 0.6750 0.3173 0.1921 -0.0353 0.0820 580 MET A N 4415 C CA . MET A 580 ? 0.5465 0.6908 0.3335 0.2006 -0.0273 0.0975 580 MET A CA 4416 C C . MET A 580 ? 0.5623 0.6681 0.3515 0.1908 -0.0147 0.1036 580 MET A C 4417 O O . MET A 580 ? 0.5418 0.6381 0.3379 0.1738 -0.0128 0.0955 580 MET A O 4418 C CB . MET A 580 ? 0.5512 0.7084 0.3271 0.1971 -0.0310 0.0938 580 MET A CB 4419 C CG . MET A 580 ? 0.5698 0.7110 0.3242 0.2064 -0.0228 0.1101 580 MET A CG 4420 S SD . MET A 580 ? 0.5502 0.7092 0.2921 0.2023 -0.0272 0.1039 580 MET A SD 4421 C CE . MET A 580 ? 0.5079 0.6464 0.2637 0.1770 -0.0225 0.0925 580 MET A CE 4422 N N . ASN A 581 ? 0.6051 0.6895 0.3892 0.2019 -0.0062 0.1172 581 ASN A N 4423 C CA . ASN A 581 ? 0.6272 0.6758 0.4156 0.1926 0.0061 0.1214 581 ASN A CA 4424 C C . ASN A 581 ? 0.6738 0.6962 0.4467 0.2015 0.0182 0.1390 581 ASN A C 4425 O O . ASN A 581 ? 0.6911 0.7199 0.4499 0.2197 0.0180 0.1512 581 ASN A O 4426 C CB . ASN A 581 ? 0.6203 0.6617 0.4233 0.1928 0.0075 0.1177 581 ASN A CB 4427 C CG . ASN A 581 ? 0.5713 0.6364 0.3903 0.1833 -0.0023 0.1014 581 ASN A CG 4428 O OD1 . ASN A 581 ? 0.5538 0.6456 0.3765 0.1923 -0.0110 0.0978 581 ASN A OD1 4429 N ND2 . ASN A 581 ? 0.5522 0.6087 0.3811 0.1652 -0.0007 0.0916 581 ASN A ND2 4430 N N . VAL A 582 ? 0.7005 0.6942 0.4761 0.1888 0.0290 0.1402 582 VAL A N 4431 C CA . VAL A 582 ? 0.7515 0.7160 0.5154 0.1944 0.0431 0.1563 582 VAL A CA 4432 C C . VAL A 582 ? 0.7861 0.7399 0.5451 0.2134 0.0477 0.1694 582 VAL A C 4433 O O . VAL A 582 ? 0.7899 0.7368 0.5613 0.2138 0.0482 0.1650 582 VAL A O 4434 C CB . VAL A 582 ? 0.7489 0.6829 0.5222 0.1773 0.0549 0.1533 582 VAL A CB 4435 C CG1 . VAL A 582 ? 0.7600 0.6917 0.5272 0.1664 0.0587 0.1533 582 VAL A CG1 4436 C CG2 . VAL A 582 ? 0.7314 0.6668 0.5241 0.1640 0.0508 0.1374 582 VAL A CG2 4437 N N . GLY A 583 ? 0.8248 0.7779 0.5653 0.2301 0.0512 0.1857 583 GLY A N 4438 C CA . GLY A 583 ? 0.8647 0.8086 0.5984 0.2513 0.0555 0.2002 583 GLY A CA 4439 C C . GLY A 583 ? 0.8801 0.8596 0.6047 0.2705 0.0425 0.2026 583 GLY A C 4440 O O . GLY A 583 ? 0.9096 0.8855 0.6235 0.2918 0.0454 0.2176 583 GLY A O 4441 N N . ASP A 584 ? 0.8613 0.8756 0.5906 0.2634 0.0283 0.1875 584 ASP A N 4442 C CA . ASP A 584 ? 0.8688 0.9225 0.5923 0.2793 0.0144 0.1857 584 ASP A CA 4443 C C . ASP A 584 ? 0.8958 0.9571 0.5946 0.2973 0.0156 0.2018 584 ASP A C 4444 O O . ASP A 584 ? 0.9119 0.9537 0.5986 0.2929 0.0254 0.2108 584 ASP A O 4445 C CB . ASP A 584 ? 0.8437 0.9301 0.5787 0.2647 0.0007 0.1648 584 ASP A CB 4446 C CG . ASP A 584 ? 0.8291 0.9250 0.5866 0.2566 -0.0055 0.1499 584 ASP A CG 4447 O OD1 . ASP A 584 ? 0.8427 0.9171 0.6081 0.2589 0.0015 0.1539 584 ASP A OD1 4448 O OD2 . ASP A 584 ? 0.8106 0.9355 0.5779 0.2477 -0.0167 0.1339 584 ASP A OD2 4449 N N . ALA A 585 ? 0.9004 0.9926 0.5920 0.3175 0.0056 0.2047 585 ALA A N 4450 C CA . ALA A 585 ? 0.9220 1.0281 0.5885 0.3370 0.0047 0.2193 585 ALA A CA 4451 C C . ALA A 585 ? 0.9041 1.0305 0.5622 0.3267 -0.0009 0.2106 585 ALA A C 4452 O O . ALA A 585 ? 0.9290 1.0493 0.5656 0.3345 0.0056 0.2244 585 ALA A O 4453 C CB . ALA A 585 ? 0.9362 1.0762 0.5984 0.3614 -0.0065 0.2222 585 ALA A CB 4454 N N . HIS A 586 ? 0.8530 1.0028 0.5275 0.3097 -0.0122 0.1882 586 HIS A N 4455 C CA . HIS A 586 ? 0.8308 1.0028 0.4983 0.3012 -0.0187 0.1778 586 HIS A CA 4456 C C . HIS A 586 ? 0.7824 0.9385 0.4635 0.2745 -0.0154 0.1644 586 HIS A C 4457 O O . HIS A 586 ? 0.7627 0.9415 0.4494 0.2630 -0.0244 0.1475 586 HIS A O 4458 C CB . HIS A 586 ? 0.8314 1.0530 0.4999 0.3099 -0.0361 0.1644 586 HIS A CB 4459 C CG . HIS A 586 ? 0.8924 1.1347 0.5376 0.3371 -0.0392 0.1791 586 HIS A CG 4460 N ND1 . HIS A 586 ? 0.9377 1.1918 0.5602 0.3442 -0.0391 0.1849 586 HIS A ND1 4461 C CD2 . HIS A 586 ? 0.9343 1.1876 0.5743 0.3601 -0.0420 0.1900 586 HIS A CD2 4462 C CE1 . HIS A 586 ? 0.9756 1.2478 0.5791 0.3705 -0.0420 0.1990 586 HIS A CE1 4463 N NE2 . HIS A 586 ? 0.9833 1.2553 0.5972 0.3810 -0.0440 0.2025 586 HIS A NE2 4464 N N . TYR A 587 ? 0.7537 0.8704 0.4399 0.2657 -0.0019 0.1722 587 TYR A N 4465 C CA . TYR A 587 ? 0.6996 0.7951 0.3955 0.2431 0.0046 0.1645 587 TYR A CA 4466 C C . TYR A 587 ? 0.6851 0.7877 0.3683 0.2375 0.0055 0.1630 587 TYR A C 4467 O O . TYR A 587 ? 0.7124 0.8036 0.3770 0.2463 0.0146 0.1787 587 TYR A O 4468 C CB . TYR A 587 ? 0.7073 0.7605 0.4053 0.2401 0.0206 0.1772 587 TYR A CB 4469 C CG . TYR A 587 ? 0.6697 0.7038 0.3853 0.2168 0.0251 0.1656 587 TYR A CG 4470 C CD1 . TYR A 587 ? 0.6286 0.6744 0.3636 0.2051 0.0162 0.1483 587 TYR A CD1 4471 C CD2 . TYR A 587 ? 0.6620 0.6677 0.3749 0.2070 0.0385 0.1721 587 TYR A CD2 4472 C CE1 . TYR A 587 ? 0.6140 0.6440 0.3635 0.1854 0.0199 0.1384 587 TYR A CE1 4473 C CE2 . TYR A 587 ? 0.6482 0.6396 0.3774 0.1865 0.0417 0.1607 587 TYR A CE2 4474 C CZ . TYR A 587 ? 0.6247 0.6285 0.3714 0.1765 0.0321 0.1442 587 TYR A CZ 4475 O OH . TYR A 587 ? 0.6009 0.5924 0.3624 0.1580 0.0348 0.1335 587 TYR A OH 4476 N N . ASP A 588 ? 0.6350 0.7556 0.3286 0.2230 -0.0033 0.1443 588 ASP A N 4477 C CA . ASP A 588 ? 0.6118 0.7401 0.2962 0.2163 -0.0032 0.1397 588 ASP A CA 4478 C C . ASP A 588 ? 0.5674 0.6916 0.2706 0.1940 -0.0053 0.1222 588 ASP A C 4479 O O . ASP A 588 ? 0.5387 0.6870 0.2489 0.1881 -0.0160 0.1059 588 ASP A O 4480 C CB . ASP A 588 ? 0.6209 0.7873 0.2922 0.2293 -0.0148 0.1352 588 ASP A CB 4481 C CG . ASP A 588 ? 0.6227 0.7989 0.2829 0.2241 -0.0145 0.1300 588 ASP A CG 4482 O OD1 . ASP A 588 ? 0.6235 0.7758 0.2786 0.2169 -0.0028 0.1376 588 ASP A OD1 4483 O OD2 . ASP A 588 ? 0.6216 0.8306 0.2790 0.2270 -0.0261 0.1172 588 ASP A OD2 4484 N N . PRO A 589 ? 0.5542 0.6476 0.2659 0.1819 0.0053 0.1254 589 PRO A N 4485 C CA . PRO A 589 ? 0.5213 0.6093 0.2510 0.1624 0.0037 0.1104 589 PRO A CA 4486 C C . PRO A 589 ? 0.5112 0.6027 0.2367 0.1531 0.0050 0.1041 589 PRO A C 4487 O O . PRO A 589 ? 0.5294 0.6181 0.2388 0.1591 0.0115 0.1140 589 PRO A O 4488 C CB . PRO A 589 ? 0.5201 0.5758 0.2580 0.1559 0.0152 0.1176 589 PRO A CB 4489 C CG . PRO A 589 ? 0.5542 0.5938 0.2752 0.1667 0.0266 0.1362 589 PRO A CG 4490 C CD . PRO A 589 ? 0.5743 0.6365 0.2794 0.1861 0.0198 0.1430 589 PRO A CD 4491 N N . LEU A 590 ? 0.4806 0.5780 0.2204 0.1392 -0.0007 0.0882 590 LEU A N 4492 C CA . LEU A 590 ? 0.4716 0.5657 0.2112 0.1285 0.0025 0.0822 590 LEU A CA 4493 C C . LEU A 590 ? 0.4803 0.5459 0.2233 0.1208 0.0152 0.0904 590 LEU A C 4494 O O . LEU A 590 ? 0.4913 0.5501 0.2254 0.1198 0.0233 0.0962 590 LEU A O 4495 C CB . LEU A 590 ? 0.4443 0.5491 0.1991 0.1165 -0.0059 0.0641 590 LEU A CB 4496 C CG . LEU A 590 ? 0.4437 0.5494 0.1987 0.1073 -0.0045 0.0559 590 LEU A CG 4497 C CD1 . LEU A 590 ? 0.4538 0.5775 0.1919 0.1159 -0.0063 0.0560 590 LEU A CD1 4498 C CD2 . LEU A 590 ? 0.4209 0.5326 0.1922 0.0963 -0.0118 0.0399 590 LEU A CD2 4499 N N . PHE A 591 ? 0.4678 0.5184 0.2244 0.1152 0.0171 0.0899 591 PHE A N 4500 C CA . PHE A 591 ? 0.4744 0.4988 0.2360 0.1085 0.0289 0.0967 591 PHE A CA 4501 C C . PHE A 591 ? 0.4903 0.5017 0.2552 0.1149 0.0317 0.1043 591 PHE A C 4502 O O . PHE A 591 ? 0.4741 0.4930 0.2484 0.1151 0.0241 0.0976 591 PHE A O 4503 C CB . PHE A 591 ? 0.4500 0.4687 0.2274 0.0926 0.0286 0.0848 591 PHE A CB 4504 C CG . PHE A 591 ? 0.4395 0.4703 0.2161 0.0864 0.0254 0.0758 591 PHE A CG 4505 C CD1 . PHE A 591 ? 0.4078 0.4538 0.1920 0.0821 0.0151 0.0627 591 PHE A CD1 4506 C CD2 . PHE A 591 ? 0.4472 0.4735 0.2160 0.0848 0.0335 0.0805 591 PHE A CD2 4507 C CE1 . PHE A 591 ? 0.4052 0.4605 0.1890 0.0771 0.0127 0.0541 591 PHE A CE1 4508 C CE2 . PHE A 591 ? 0.4420 0.4799 0.2103 0.0800 0.0308 0.0718 591 PHE A CE2 4509 C CZ . PHE A 591 ? 0.4200 0.4716 0.1959 0.0764 0.0203 0.0584 591 PHE A CZ 4510 N N . ARG A 592 ? 0.5214 0.5129 0.2789 0.1200 0.0434 0.1182 592 ARG A N 4511 C CA . ARG A 592 ? 0.5478 0.5236 0.3082 0.1268 0.0478 0.1261 592 ARG A CA 4512 C C . ARG A 592 ? 0.5194 0.4809 0.2981 0.1139 0.0500 0.1173 592 ARG A C 4513 O O . ARG A 592 ? 0.4890 0.4473 0.2761 0.1002 0.0519 0.1090 592 ARG A O 4514 C CB . ARG A 592 ? 0.5778 0.5331 0.3253 0.1357 0.0614 0.1440 592 ARG A CB 4515 C CG . ARG A 592 ? 0.6222 0.5620 0.3697 0.1247 0.0732 0.1464 592 ARG A CG 4516 C CD . ARG A 592 ? 0.6637 0.5742 0.4060 0.1288 0.0899 0.1625 592 ARG A CD 4517 N NE . ARG A 592 ? 0.7741 0.6629 0.5343 0.1168 0.0967 0.1566 592 ARG A NE 4518 C CZ . ARG A 592 ? 0.7848 0.6651 0.5569 0.1004 0.1030 0.1486 592 ARG A CZ 4519 N NH1 . ARG A 592 ? 0.7788 0.6688 0.5474 0.0937 0.1042 0.1462 592 ARG A NH1 4520 N NH2 . ARG A 592 ? 0.7708 0.6339 0.5586 0.0910 0.1082 0.1423 592 ARG A NH2 4521 N N . LEU A 593 ? 0.5180 0.4726 0.3026 0.1192 0.0497 0.1187 593 LEU A N 4522 C CA . LEU A 593 ? 0.5053 0.4442 0.3053 0.1088 0.0538 0.1119 593 LEU A CA 4523 C C . LEU A 593 ? 0.5146 0.4300 0.3158 0.1005 0.0675 0.1162 593 LEU A C 4524 O O . LEU A 593 ? 0.5349 0.4365 0.3255 0.1077 0.0772 0.1296 593 LEU A O 4525 C CB . LEU A 593 ? 0.5154 0.4474 0.3190 0.1184 0.0542 0.1154 593 LEU A CB 4526 C CG . LEU A 593 ? 0.5219 0.4417 0.3414 0.1087 0.0567 0.1061 593 LEU A CG 4527 C CD1 . LEU A 593 ? 0.5251 0.4557 0.3504 0.1158 0.0493 0.1022 593 LEU A CD1 4528 C CD2 . LEU A 593 ? 0.5514 0.4409 0.3734 0.1065 0.0712 0.1121 593 LEU A CD2 4529 N N . GLY A 594 ? 0.4912 0.4033 0.3053 0.0855 0.0685 0.1049 594 GLY A N 4530 C CA . GLY A 594 ? 0.4980 0.3911 0.3167 0.0756 0.0810 0.1060 594 GLY A CA 4531 C C . GLY A 594 ? 0.4944 0.3959 0.3098 0.0684 0.0821 0.1042 594 GLY A C 4532 O O . GLY A 594 ? 0.4942 0.3848 0.3162 0.0581 0.0913 0.1023 594 GLY A O 4533 N N . TYR A 595 ? 0.4881 0.4101 0.2944 0.0734 0.0729 0.1036 595 TYR A N 4534 C CA . TYR A 595 ? 0.4862 0.4183 0.2893 0.0674 0.0732 0.1007 595 TYR A CA 4535 C C . TYR A 595 ? 0.4626 0.4007 0.2801 0.0537 0.0694 0.0863 595 TYR A C 4536 O O . TYR A 595 ? 0.4448 0.3906 0.2703 0.0514 0.0606 0.0773 595 TYR A O 4537 C CB . TYR A 595 ? 0.4898 0.4431 0.2802 0.0766 0.0637 0.1017 595 TYR A CB 4538 C CG . TYR A 595 ? 0.4882 0.4533 0.2751 0.0713 0.0630 0.0972 595 TYR A CG 4539 C CD1 . TYR A 595 ? 0.5245 0.4874 0.2988 0.0752 0.0717 0.1070 595 TYR A CD1 4540 C CD2 . TYR A 595 ? 0.4805 0.4590 0.2766 0.0632 0.0544 0.0835 595 TYR A CD2 4541 C CE1 . TYR A 595 ? 0.5140 0.4889 0.2855 0.0706 0.0714 0.1020 595 TYR A CE1 4542 C CE2 . TYR A 595 ? 0.4702 0.4591 0.2639 0.0593 0.0541 0.0788 595 TYR A CE2 4543 C CZ . TYR A 595 ? 0.4963 0.4840 0.2780 0.0629 0.0624 0.0874 595 TYR A CZ 4544 O OH . TYR A 595 ? 0.5178 0.5171 0.2974 0.0594 0.0621 0.0819 595 TYR A OH 4545 N N . GLY A 596 ? 0.4655 0.4013 0.2861 0.0452 0.0764 0.0846 596 GLY A N 4546 C CA . GLY A 596 ? 0.4450 0.3900 0.2778 0.0340 0.0721 0.0714 596 GLY A CA 4547 C C . GLY A 596 ? 0.4497 0.3940 0.2837 0.0272 0.0809 0.0716 596 GLY A C 4548 O O . GLY A 596 ? 0.4708 0.4002 0.3063 0.0242 0.0931 0.0778 596 GLY A O 4549 N N . LEU A 597 ? 0.4369 0.3972 0.2708 0.0248 0.0756 0.0650 597 LEU A N 4550 C CA . LEU A 597 ? 0.4380 0.4009 0.2756 0.0176 0.0833 0.0632 597 LEU A CA 4551 C C . LEU A 597 ? 0.4366 0.3979 0.2919 0.0061 0.0853 0.0529 597 LEU A C 4552 O O . LEU A 597 ? 0.4066 0.3701 0.2695 0.0044 0.0776 0.0455 597 LEU A O 4553 C CB . LEU A 597 ? 0.4264 0.4073 0.2581 0.0199 0.0768 0.0587 597 LEU A CB 4554 C CG . LEU A 597 ? 0.4294 0.4162 0.2433 0.0310 0.0745 0.0666 597 LEU A CG 4555 C CD1 . LEU A 597 ? 0.4156 0.4200 0.2261 0.0320 0.0682 0.0592 597 LEU A CD1 4556 C CD2 . LEU A 597 ? 0.4527 0.4290 0.2558 0.0350 0.0872 0.0804 597 LEU A CD2 4557 N N . THR A 598 ? 0.4488 0.4075 0.3110 -0.0018 0.0959 0.0523 598 THR A N 4558 C CA . THR A 598 ? 0.4587 0.4193 0.3387 -0.0129 0.0977 0.0411 598 THR A CA 4559 C C . THR A 598 ? 0.4546 0.4328 0.3414 -0.0181 0.0969 0.0330 598 THR A C 4560 O O . THR A 598 ? 0.4536 0.4379 0.3322 -0.0151 0.0997 0.0374 598 THR A O 4561 C CB . THR A 598 ? 0.4744 0.4169 0.3627 -0.0200 0.1115 0.0439 598 THR A CB 4562 O OG1 . THR A 598 ? 0.4960 0.4347 0.3812 -0.0224 0.1241 0.0512 598 THR A OG1 4563 C CG2 . THR A 598 ? 0.4884 0.4123 0.3699 -0.0133 0.1129 0.0525 598 THR A CG2 4564 N N . THR A 599 ? 0.4518 0.4395 0.3527 -0.0248 0.0926 0.0210 599 THR A N 4565 C CA . THR A 599 ? 0.4603 0.4639 0.3713 -0.0308 0.0943 0.0127 599 THR A CA 4566 C C . THR A 599 ? 0.4755 0.4790 0.4044 -0.0420 0.1005 0.0039 599 THR A C 4567 O O . THR A 599 ? 0.4789 0.4700 0.4115 -0.0444 0.1019 0.0031 599 THR A O 4568 C CB . THR A 599 ? 0.4409 0.4622 0.3524 -0.0267 0.0816 0.0050 599 THR A CB 4569 O OG1 . THR A 599 ? 0.4285 0.4505 0.3454 -0.0268 0.0732 -0.0011 599 THR A OG1 4570 C CG2 . THR A 599 ? 0.4276 0.4506 0.3235 -0.0169 0.0757 0.0112 599 THR A CG2 4571 N N . ASN A 600 ? 0.4924 0.5107 0.4329 -0.0487 0.1042 -0.0038 600 ASN A N 4572 C CA . ASN A 600 ? 0.5142 0.5391 0.4740 -0.0596 0.1078 -0.0159 600 ASN A CA 4573 C C . ASN A 600 ? 0.5020 0.5512 0.4702 -0.0588 0.0966 -0.0281 600 ASN A C 4574 O O . ASN A 600 ? 0.4888 0.5503 0.4513 -0.0522 0.0905 -0.0274 600 ASN A O 4575 C CB . ASN A 600 ? 0.5311 0.5541 0.5011 -0.0697 0.1235 -0.0158 600 ASN A CB 4576 C CG . ASN A 600 ? 0.5804 0.5762 0.5450 -0.0716 0.1363 -0.0043 600 ASN A CG 4577 O OD1 . ASN A 600 ? 0.6057 0.5937 0.5620 -0.0703 0.1462 0.0066 600 ASN A OD1 4578 N ND2 . ASN A 600 ? 0.6272 0.6085 0.5958 -0.0739 0.1364 -0.0066 600 ASN A ND2 4579 N N . ALA A 601 ? 0.5070 0.5627 0.4882 -0.0646 0.0940 -0.0394 601 ALA A N 4580 C CA . ALA A 601 ? 0.5054 0.5853 0.4951 -0.0634 0.0839 -0.0511 601 ALA A CA 4581 C C . ALA A 601 ? 0.5114 0.6125 0.5109 -0.0661 0.0867 -0.0568 601 ALA A C 4582 O O . ALA A 601 ? 0.5246 0.6262 0.5347 -0.0755 0.0984 -0.0590 601 ALA A O 4583 C CB . ALA A 601 ? 0.4982 0.5824 0.5006 -0.0702 0.0826 -0.0629 601 ALA A CB 4584 N N . THR A 602 ? 0.5113 0.6289 0.5074 -0.0576 0.0768 -0.0587 602 THR A N 4585 C CA . THR A 602 ? 0.5204 0.6614 0.5269 -0.0584 0.0778 -0.0656 602 THR A CA 4586 C C . THR A 602 ? 0.5146 0.6802 0.5360 -0.0600 0.0711 -0.0796 602 THR A C 4587 O O . THR A 602 ? 0.5284 0.6947 0.5592 -0.0673 0.0721 -0.0872 602 THR A O 4588 C CB . THR A 602 ? 0.5176 0.6629 0.5124 -0.0472 0.0722 -0.0597 602 THR A CB 4589 O OG1 . THR A 602 ? 0.5113 0.6488 0.4934 -0.0376 0.0612 -0.0553 602 THR A OG1 4590 C CG2 . THR A 602 ? 0.5481 0.6798 0.5326 -0.0472 0.0814 -0.0493 602 THR A CG2 # _database_PDB_caveat.id 1 _database_PDB_caveat.text 'THE LIGABD NAG 705 HAS LOW CORRELATION AND HIGH REAL SPACE R VALUE.' # 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 # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 498 A ASN 498 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 221 A ASN 221 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 600 A ASN 600 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O # _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 23.5700 16.4030 30.3870 -0.2152 -0.1911 -0.3000 0.0088 0.0115 0.0261 1.4944 0.5490 1.4162 -0.3465 -0.6045 0.2889 -0.1220 -0.0706 -0.1685 0.0575 0.0438 -0.0170 0.1424 0.1536 0.0782 'X-RAY DIFFRACTION' 2 ? refined 2.0020 31.9610 51.2890 -0.1977 -0.1697 -0.3203 0.0161 0.0003 -0.0014 1.7753 0.8133 1.4155 -0.4516 -0.5989 0.4287 -0.0726 -0.1762 0.0051 0.1160 0.0174 0.0110 0.0371 -0.0033 0.0553 # 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 5.2.0005 ? 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 3WLN # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O A HOH 1072 ? ? O A HOH 1462 ? ? 1.84 2 1 O A HOH 1202 ? ? O A HOH 1374 ? ? 2.07 3 1 O A HOH 943 ? ? O A HOH 1176 ? ? 2.07 4 1 SD A MET 356 ? ? O A HOH 1148 ? ? 2.10 5 1 O A HOH 1324 ? ? O A HOH 1447 ? ? 2.12 6 1 O A HOH 1235 ? ? O A HOH 1250 ? ? 2.13 7 1 S1 A SOG 713 ? ? O A HOH 801 ? ? 2.15 8 1 O A HOH 955 ? ? O A HOH 1324 ? ? 2.17 9 1 O A HOH 906 ? ? O A HOH 913 ? ? 2.17 10 1 O A HOH 1286 ? ? O A HOH 1311 ? ? 2.19 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 O _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 HOH _pdbx_validate_symm_contact.auth_seq_id_1 1008 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 ? _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O _pdbx_validate_symm_contact.auth_asym_id_2 A _pdbx_validate_symm_contact.auth_comp_id_2 HOH _pdbx_validate_symm_contact.auth_seq_id_2 1284 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 6_455 _pdbx_validate_symm_contact.dist 2.18 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 HIS A 98 ? ? -152.88 64.88 2 1 ASP A 216 ? ? 58.98 19.56 3 1 ASN A 221 ? ? -94.62 -157.62 4 1 TYR A 271 ? ? -96.75 -64.12 5 1 ILE A 432 ? ? 70.47 -61.64 6 1 GLU A 491 ? ? 57.63 -134.35 7 1 TRP A 544 ? ? 55.15 -134.43 8 1 LEU A 545 ? ? -118.43 79.93 9 1 GLU A 549 ? ? -101.97 76.59 # 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 BETA-D-MANNOSE BMA 4 ALPHA-L-FUCOSE FUC 5 2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL SOG 6 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 2211 NAG NAG A . C 2 NAG 2 702 2212 NAG NAG A . D 3 BMA 3 703 2213 BMA MAN A . E 2 NAG 1 704 4981 NAG NAG A . F 2 NAG 2 705 4982 NAG NAG A . G 3 BMA 3 706 4983 BMA MAN A . H 3 BMA 4 707 4985 BMA MAN A . I 2 NAG 5 708 4986 NAG NAG A . J 2 NAG 1 709 6001 NAG NAG A . K 2 NAG 2 710 6002 NAG NAG A . L 3 BMA 3 711 6003 BMA MAN A . M 4 FUC 4 712 6004 FUC FCU A . N 5 SOG 1 713 1 SOG BSG A . O 6 HOH 1 801 1 HOH HOH A . O 6 HOH 2 802 2 HOH HOH A . O 6 HOH 3 803 3 HOH HOH A . O 6 HOH 4 804 4 HOH HOH A . O 6 HOH 5 805 5 HOH HOH A . O 6 HOH 6 806 6 HOH HOH A . O 6 HOH 7 807 7 HOH HOH A . O 6 HOH 8 808 8 HOH HOH A . O 6 HOH 9 809 9 HOH HOH A . O 6 HOH 10 810 10 HOH HOH A . O 6 HOH 11 811 11 HOH HOH A . O 6 HOH 12 812 12 HOH HOH A . O 6 HOH 13 813 13 HOH HOH A . O 6 HOH 14 814 14 HOH HOH A . O 6 HOH 15 815 15 HOH HOH A . O 6 HOH 16 816 16 HOH HOH A . O 6 HOH 17 817 17 HOH HOH A . O 6 HOH 18 818 18 HOH HOH A . O 6 HOH 19 819 19 HOH HOH A . O 6 HOH 20 820 20 HOH HOH A . O 6 HOH 21 821 21 HOH HOH A . O 6 HOH 22 822 22 HOH HOH A . O 6 HOH 23 823 23 HOH HOH A . O 6 HOH 24 824 24 HOH HOH A . O 6 HOH 25 825 25 HOH HOH A . O 6 HOH 26 826 26 HOH HOH A . O 6 HOH 27 827 27 HOH HOH A . O 6 HOH 28 828 28 HOH HOH A . O 6 HOH 29 829 29 HOH HOH A . O 6 HOH 30 830 30 HOH HOH A . O 6 HOH 31 831 31 HOH HOH A . O 6 HOH 32 832 32 HOH HOH A . O 6 HOH 33 833 33 HOH HOH A . O 6 HOH 34 834 34 HOH HOH A . O 6 HOH 35 835 35 HOH HOH A . O 6 HOH 36 836 36 HOH HOH A . O 6 HOH 37 837 37 HOH HOH A . O 6 HOH 38 838 38 HOH HOH A . O 6 HOH 39 839 39 HOH HOH A . O 6 HOH 40 840 40 HOH HOH A . O 6 HOH 41 841 41 HOH HOH A . O 6 HOH 42 842 42 HOH HOH A . O 6 HOH 43 843 43 HOH HOH A . O 6 HOH 44 844 44 HOH HOH A . O 6 HOH 45 845 45 HOH HOH A . O 6 HOH 46 846 46 HOH HOH A . O 6 HOH 47 847 47 HOH HOH A . O 6 HOH 48 848 48 HOH HOH A . O 6 HOH 49 849 49 HOH HOH A . O 6 HOH 50 850 50 HOH HOH A . O 6 HOH 51 851 51 HOH HOH A . O 6 HOH 52 852 52 HOH HOH A . O 6 HOH 53 853 53 HOH HOH A . O 6 HOH 54 854 54 HOH HOH A . O 6 HOH 55 855 55 HOH HOH A . O 6 HOH 56 856 56 HOH HOH A . O 6 HOH 57 857 57 HOH HOH A . O 6 HOH 58 858 58 HOH HOH A . O 6 HOH 59 859 59 HOH HOH A . O 6 HOH 60 860 60 HOH HOH A . O 6 HOH 61 861 61 HOH HOH A . O 6 HOH 62 862 62 HOH HOH A . O 6 HOH 63 863 63 HOH HOH A . O 6 HOH 64 864 64 HOH HOH A . O 6 HOH 65 865 65 HOH HOH A . O 6 HOH 66 866 66 HOH HOH A . O 6 HOH 67 867 67 HOH HOH A . O 6 HOH 68 868 68 HOH HOH A . O 6 HOH 69 869 69 HOH HOH A . O 6 HOH 70 870 70 HOH HOH A . O 6 HOH 71 871 71 HOH HOH A . O 6 HOH 72 872 72 HOH HOH A . O 6 HOH 73 873 73 HOH HOH A . O 6 HOH 74 874 74 HOH HOH A . O 6 HOH 75 875 75 HOH HOH A . O 6 HOH 76 876 76 HOH HOH A . O 6 HOH 77 877 77 HOH HOH A . O 6 HOH 78 878 78 HOH HOH A . O 6 HOH 79 879 79 HOH HOH A . O 6 HOH 80 880 80 HOH HOH A . O 6 HOH 81 881 81 HOH HOH A . O 6 HOH 82 882 82 HOH HOH A . O 6 HOH 83 883 83 HOH HOH A . O 6 HOH 84 884 84 HOH HOH A . O 6 HOH 85 885 85 HOH HOH A . O 6 HOH 86 886 86 HOH HOH A . O 6 HOH 87 887 87 HOH HOH A . O 6 HOH 88 888 88 HOH HOH A . O 6 HOH 89 889 89 HOH HOH A . O 6 HOH 90 890 90 HOH HOH A . O 6 HOH 91 891 91 HOH HOH A . O 6 HOH 92 892 92 HOH HOH A . O 6 HOH 93 893 93 HOH HOH A . O 6 HOH 94 894 94 HOH HOH A . O 6 HOH 95 895 95 HOH HOH A . O 6 HOH 96 896 96 HOH HOH A . O 6 HOH 97 897 97 HOH HOH A . O 6 HOH 98 898 98 HOH HOH A . O 6 HOH 99 899 99 HOH HOH A . O 6 HOH 100 900 100 HOH HOH A . O 6 HOH 101 901 101 HOH HOH A . O 6 HOH 102 902 102 HOH HOH A . O 6 HOH 103 903 103 HOH HOH A . O 6 HOH 104 904 104 HOH HOH A . O 6 HOH 105 905 105 HOH HOH A . O 6 HOH 106 906 106 HOH HOH A . O 6 HOH 107 907 107 HOH HOH A . O 6 HOH 108 908 108 HOH HOH A . O 6 HOH 109 909 109 HOH HOH A . O 6 HOH 110 910 110 HOH HOH A . O 6 HOH 111 911 111 HOH HOH A . O 6 HOH 112 912 112 HOH HOH A . O 6 HOH 113 913 113 HOH HOH A . O 6 HOH 114 914 114 HOH HOH A . O 6 HOH 115 915 115 HOH HOH A . O 6 HOH 116 916 116 HOH HOH A . O 6 HOH 117 917 117 HOH HOH A . O 6 HOH 118 918 118 HOH HOH A . O 6 HOH 119 919 119 HOH HOH A . O 6 HOH 120 920 120 HOH HOH A . O 6 HOH 121 921 121 HOH HOH A . O 6 HOH 122 922 122 HOH HOH A . O 6 HOH 123 923 123 HOH HOH A . O 6 HOH 124 924 124 HOH HOH A . O 6 HOH 125 925 125 HOH HOH A . O 6 HOH 126 926 126 HOH HOH A . O 6 HOH 127 927 127 HOH HOH A . O 6 HOH 128 928 128 HOH HOH A . O 6 HOH 129 929 129 HOH HOH A . O 6 HOH 130 930 130 HOH HOH A . O 6 HOH 131 931 131 HOH HOH A . O 6 HOH 132 932 132 HOH HOH A . O 6 HOH 133 933 133 HOH HOH A . O 6 HOH 134 934 134 HOH HOH A . O 6 HOH 135 935 135 HOH HOH A . O 6 HOH 136 936 136 HOH HOH A . O 6 HOH 137 937 137 HOH HOH A . O 6 HOH 138 938 138 HOH HOH A . O 6 HOH 139 939 139 HOH HOH A . O 6 HOH 140 940 140 HOH HOH A . O 6 HOH 141 941 141 HOH HOH A . O 6 HOH 142 942 142 HOH HOH A . O 6 HOH 143 943 143 HOH HOH A . O 6 HOH 144 944 144 HOH HOH A . O 6 HOH 145 945 145 HOH HOH A . O 6 HOH 146 946 146 HOH HOH A . O 6 HOH 147 947 147 HOH HOH A . O 6 HOH 148 948 148 HOH HOH A . O 6 HOH 149 949 149 HOH HOH A . O 6 HOH 150 950 150 HOH HOH A . O 6 HOH 151 951 151 HOH HOH A . O 6 HOH 152 952 152 HOH HOH A . O 6 HOH 153 953 153 HOH HOH A . O 6 HOH 154 954 154 HOH HOH A . O 6 HOH 155 955 155 HOH HOH A . O 6 HOH 156 956 156 HOH HOH A . O 6 HOH 157 957 157 HOH HOH A . O 6 HOH 158 958 158 HOH HOH A . O 6 HOH 159 959 159 HOH HOH A . O 6 HOH 160 960 160 HOH HOH A . O 6 HOH 161 961 161 HOH HOH A . O 6 HOH 162 962 162 HOH HOH A . O 6 HOH 163 963 163 HOH HOH A . O 6 HOH 164 964 164 HOH HOH A . O 6 HOH 165 965 165 HOH HOH A . O 6 HOH 166 966 166 HOH HOH A . O 6 HOH 167 967 167 HOH HOH A . O 6 HOH 168 968 168 HOH HOH A . O 6 HOH 169 969 169 HOH HOH A . O 6 HOH 170 970 170 HOH HOH A . O 6 HOH 171 971 171 HOH HOH A . O 6 HOH 172 972 172 HOH HOH A . O 6 HOH 173 973 173 HOH HOH A . O 6 HOH 174 974 174 HOH HOH A . O 6 HOH 175 975 175 HOH HOH A . O 6 HOH 176 976 176 HOH HOH A . O 6 HOH 177 977 177 HOH HOH A . O 6 HOH 178 978 178 HOH HOH A . O 6 HOH 179 979 179 HOH HOH A . O 6 HOH 180 980 180 HOH HOH A . O 6 HOH 181 981 181 HOH HOH A . O 6 HOH 182 982 182 HOH HOH A . O 6 HOH 183 983 183 HOH HOH A . O 6 HOH 184 984 184 HOH HOH A . O 6 HOH 185 985 185 HOH HOH A . O 6 HOH 186 986 186 HOH HOH A . O 6 HOH 187 987 187 HOH HOH A . O 6 HOH 188 988 188 HOH HOH A . O 6 HOH 189 989 189 HOH HOH A . O 6 HOH 190 990 190 HOH HOH A . O 6 HOH 191 991 191 HOH HOH A . O 6 HOH 192 992 192 HOH HOH A . O 6 HOH 193 993 193 HOH HOH A . O 6 HOH 194 994 194 HOH HOH A . O 6 HOH 195 995 195 HOH HOH A . O 6 HOH 196 996 196 HOH HOH A . O 6 HOH 197 997 197 HOH HOH A . O 6 HOH 198 998 198 HOH HOH A . O 6 HOH 199 999 199 HOH HOH A . O 6 HOH 200 1000 200 HOH HOH A . O 6 HOH 201 1001 201 HOH HOH A . O 6 HOH 202 1002 202 HOH HOH A . O 6 HOH 203 1003 203 HOH HOH A . O 6 HOH 204 1004 204 HOH HOH A . O 6 HOH 205 1005 205 HOH HOH A . O 6 HOH 206 1006 206 HOH HOH A . O 6 HOH 207 1007 207 HOH HOH A . O 6 HOH 208 1008 208 HOH HOH A . O 6 HOH 209 1009 209 HOH HOH A . O 6 HOH 210 1010 210 HOH HOH A . O 6 HOH 211 1011 211 HOH HOH A . O 6 HOH 212 1012 212 HOH HOH A . O 6 HOH 213 1013 213 HOH HOH A . O 6 HOH 214 1014 214 HOH HOH A . O 6 HOH 215 1015 215 HOH HOH A . O 6 HOH 216 1016 216 HOH HOH A . O 6 HOH 217 1017 217 HOH HOH A . O 6 HOH 218 1018 218 HOH HOH A . O 6 HOH 219 1019 219 HOH HOH A . O 6 HOH 220 1020 220 HOH HOH A . O 6 HOH 221 1021 221 HOH HOH A . O 6 HOH 222 1022 222 HOH HOH A . O 6 HOH 223 1023 223 HOH HOH A . O 6 HOH 224 1024 224 HOH HOH A . O 6 HOH 225 1025 225 HOH HOH A . O 6 HOH 226 1026 226 HOH HOH A . O 6 HOH 227 1027 227 HOH HOH A . O 6 HOH 228 1028 228 HOH HOH A . O 6 HOH 229 1029 229 HOH HOH A . O 6 HOH 230 1030 230 HOH HOH A . O 6 HOH 231 1031 231 HOH HOH A . O 6 HOH 232 1032 232 HOH HOH A . O 6 HOH 233 1033 233 HOH HOH A . O 6 HOH 234 1034 234 HOH HOH A . O 6 HOH 235 1035 235 HOH HOH A . O 6 HOH 236 1036 236 HOH HOH A . O 6 HOH 237 1037 237 HOH HOH A . O 6 HOH 238 1038 238 HOH HOH A . O 6 HOH 239 1039 239 HOH HOH A . O 6 HOH 240 1040 240 HOH HOH A . O 6 HOH 241 1041 241 HOH HOH A . O 6 HOH 242 1042 242 HOH HOH A . O 6 HOH 243 1043 243 HOH HOH A . O 6 HOH 244 1044 244 HOH HOH A . O 6 HOH 245 1045 245 HOH HOH A . O 6 HOH 246 1046 246 HOH HOH A . O 6 HOH 247 1047 247 HOH HOH A . O 6 HOH 248 1048 248 HOH HOH A . O 6 HOH 249 1049 249 HOH HOH A . O 6 HOH 250 1050 250 HOH HOH A . O 6 HOH 251 1051 251 HOH HOH A . O 6 HOH 252 1052 252 HOH HOH A . O 6 HOH 253 1053 253 HOH HOH A . O 6 HOH 254 1054 254 HOH HOH A . O 6 HOH 255 1055 255 HOH HOH A . O 6 HOH 256 1056 256 HOH HOH A . O 6 HOH 257 1057 257 HOH HOH A . O 6 HOH 258 1058 258 HOH HOH A . O 6 HOH 259 1059 259 HOH HOH A . O 6 HOH 260 1060 260 HOH HOH A . O 6 HOH 261 1061 261 HOH HOH A . O 6 HOH 262 1062 262 HOH HOH A . O 6 HOH 263 1063 263 HOH HOH A . O 6 HOH 264 1064 264 HOH HOH A . O 6 HOH 265 1065 265 HOH HOH A . O 6 HOH 266 1066 266 HOH HOH A . O 6 HOH 267 1067 267 HOH HOH A . O 6 HOH 268 1068 268 HOH HOH A . O 6 HOH 269 1069 269 HOH HOH A . O 6 HOH 270 1070 270 HOH HOH A . O 6 HOH 271 1071 271 HOH HOH A . O 6 HOH 272 1072 272 HOH HOH A . O 6 HOH 273 1073 273 HOH HOH A . O 6 HOH 274 1074 274 HOH HOH A . O 6 HOH 275 1075 275 HOH HOH A . O 6 HOH 276 1076 276 HOH HOH A . O 6 HOH 277 1077 277 HOH HOH A . O 6 HOH 278 1078 278 HOH HOH A . O 6 HOH 279 1079 279 HOH HOH A . O 6 HOH 280 1080 280 HOH HOH A . O 6 HOH 281 1081 281 HOH HOH A . O 6 HOH 282 1082 282 HOH HOH A . O 6 HOH 283 1083 283 HOH HOH A . O 6 HOH 284 1084 284 HOH HOH A . O 6 HOH 285 1085 285 HOH HOH A . O 6 HOH 286 1086 286 HOH HOH A . O 6 HOH 287 1087 287 HOH HOH A . O 6 HOH 288 1088 288 HOH HOH A . O 6 HOH 289 1089 289 HOH HOH A . O 6 HOH 290 1090 290 HOH HOH A . O 6 HOH 291 1091 291 HOH HOH A . O 6 HOH 292 1092 292 HOH HOH A . O 6 HOH 293 1093 293 HOH HOH A . O 6 HOH 294 1094 294 HOH HOH A . O 6 HOH 295 1095 295 HOH HOH A . O 6 HOH 296 1096 296 HOH HOH A . O 6 HOH 297 1097 297 HOH HOH A . O 6 HOH 298 1098 298 HOH HOH A . O 6 HOH 299 1099 299 HOH HOH A . O 6 HOH 300 1100 300 HOH HOH A . O 6 HOH 301 1101 301 HOH HOH A . O 6 HOH 302 1102 302 HOH HOH A . O 6 HOH 303 1103 303 HOH HOH A . O 6 HOH 304 1104 304 HOH HOH A . O 6 HOH 305 1105 305 HOH HOH A . O 6 HOH 306 1106 306 HOH HOH A . O 6 HOH 307 1107 307 HOH HOH A . O 6 HOH 308 1108 308 HOH HOH A . O 6 HOH 309 1109 309 HOH HOH A . O 6 HOH 310 1110 310 HOH HOH A . O 6 HOH 311 1111 311 HOH HOH A . O 6 HOH 312 1112 312 HOH HOH A . O 6 HOH 313 1113 313 HOH HOH A . O 6 HOH 314 1114 314 HOH HOH A . O 6 HOH 315 1115 315 HOH HOH A . O 6 HOH 316 1116 316 HOH HOH A . O 6 HOH 317 1117 317 HOH HOH A . O 6 HOH 318 1118 318 HOH HOH A . O 6 HOH 319 1119 319 HOH HOH A . O 6 HOH 320 1120 320 HOH HOH A . O 6 HOH 321 1121 321 HOH HOH A . O 6 HOH 322 1122 322 HOH HOH A . O 6 HOH 323 1123 323 HOH HOH A . O 6 HOH 324 1124 324 HOH HOH A . O 6 HOH 325 1125 325 HOH HOH A . O 6 HOH 326 1126 326 HOH HOH A . O 6 HOH 327 1127 327 HOH HOH A . O 6 HOH 328 1128 328 HOH HOH A . O 6 HOH 329 1129 329 HOH HOH A . O 6 HOH 330 1130 330 HOH HOH A . O 6 HOH 331 1131 331 HOH HOH A . O 6 HOH 332 1132 332 HOH HOH A . O 6 HOH 333 1133 333 HOH HOH A . O 6 HOH 334 1134 334 HOH HOH A . O 6 HOH 335 1135 335 HOH HOH A . O 6 HOH 336 1136 336 HOH HOH A . O 6 HOH 337 1137 337 HOH HOH A . O 6 HOH 338 1138 338 HOH HOH A . O 6 HOH 339 1139 339 HOH HOH A . O 6 HOH 340 1140 340 HOH HOH A . O 6 HOH 341 1141 341 HOH HOH A . O 6 HOH 342 1142 342 HOH HOH A . O 6 HOH 343 1143 343 HOH HOH A . O 6 HOH 344 1144 344 HOH HOH A . O 6 HOH 345 1145 345 HOH HOH A . O 6 HOH 346 1146 346 HOH HOH A . O 6 HOH 347 1147 347 HOH HOH A . O 6 HOH 348 1148 348 HOH HOH A . O 6 HOH 349 1149 349 HOH HOH A . O 6 HOH 350 1150 350 HOH HOH A . O 6 HOH 351 1151 351 HOH HOH A . O 6 HOH 352 1152 352 HOH HOH A . O 6 HOH 353 1153 353 HOH HOH A . O 6 HOH 354 1154 354 HOH HOH A . O 6 HOH 355 1155 355 HOH HOH A . O 6 HOH 356 1156 356 HOH HOH A . O 6 HOH 357 1157 357 HOH HOH A . O 6 HOH 358 1158 358 HOH HOH A . O 6 HOH 359 1159 359 HOH HOH A . O 6 HOH 360 1160 360 HOH HOH A . O 6 HOH 361 1161 361 HOH HOH A . O 6 HOH 362 1162 362 HOH HOH A . O 6 HOH 363 1163 363 HOH HOH A . O 6 HOH 364 1164 364 HOH HOH A . O 6 HOH 365 1165 365 HOH HOH A . O 6 HOH 366 1166 366 HOH HOH A . O 6 HOH 367 1167 367 HOH HOH A . O 6 HOH 368 1168 368 HOH HOH A . O 6 HOH 369 1169 369 HOH HOH A . O 6 HOH 370 1170 370 HOH HOH A . O 6 HOH 371 1171 371 HOH HOH A . O 6 HOH 372 1172 372 HOH HOH A . O 6 HOH 373 1173 373 HOH HOH A . O 6 HOH 374 1174 374 HOH HOH A . O 6 HOH 375 1175 375 HOH HOH A . O 6 HOH 376 1176 376 HOH HOH A . O 6 HOH 377 1177 377 HOH HOH A . O 6 HOH 378 1178 378 HOH HOH A . O 6 HOH 379 1179 379 HOH HOH A . O 6 HOH 380 1180 380 HOH HOH A . O 6 HOH 381 1181 381 HOH HOH A . O 6 HOH 382 1182 382 HOH HOH A . O 6 HOH 383 1183 383 HOH HOH A . O 6 HOH 384 1184 384 HOH HOH A . O 6 HOH 385 1185 385 HOH HOH A . O 6 HOH 386 1186 386 HOH HOH A . O 6 HOH 387 1187 387 HOH HOH A . O 6 HOH 388 1188 388 HOH HOH A . O 6 HOH 389 1189 389 HOH HOH A . O 6 HOH 390 1190 390 HOH HOH A . O 6 HOH 391 1191 391 HOH HOH A . O 6 HOH 392 1192 392 HOH HOH A . O 6 HOH 393 1193 393 HOH HOH A . O 6 HOH 394 1194 394 HOH HOH A . O 6 HOH 395 1195 395 HOH HOH A . O 6 HOH 396 1196 396 HOH HOH A . O 6 HOH 397 1197 397 HOH HOH A . O 6 HOH 398 1198 398 HOH HOH A . O 6 HOH 399 1199 399 HOH HOH A . O 6 HOH 400 1200 400 HOH HOH A . O 6 HOH 401 1201 401 HOH HOH A . O 6 HOH 402 1202 402 HOH HOH A . O 6 HOH 403 1203 403 HOH HOH A . O 6 HOH 404 1204 404 HOH HOH A . O 6 HOH 405 1205 405 HOH HOH A . O 6 HOH 406 1206 406 HOH HOH A . O 6 HOH 407 1207 407 HOH HOH A . O 6 HOH 408 1208 408 HOH HOH A . O 6 HOH 409 1209 409 HOH HOH A . O 6 HOH 410 1210 410 HOH HOH A . O 6 HOH 411 1211 411 HOH HOH A . O 6 HOH 412 1212 412 HOH HOH A . O 6 HOH 413 1213 413 HOH HOH A . O 6 HOH 414 1214 414 HOH HOH A . O 6 HOH 415 1215 415 HOH HOH A . O 6 HOH 416 1216 416 HOH HOH A . O 6 HOH 417 1217 417 HOH HOH A . O 6 HOH 418 1218 418 HOH HOH A . O 6 HOH 419 1219 419 HOH HOH A . O 6 HOH 420 1220 420 HOH HOH A . O 6 HOH 421 1221 421 HOH HOH A . O 6 HOH 422 1222 422 HOH HOH A . O 6 HOH 423 1223 423 HOH HOH A . O 6 HOH 424 1224 424 HOH HOH A . O 6 HOH 425 1225 425 HOH HOH A . O 6 HOH 426 1226 426 HOH HOH A . O 6 HOH 427 1227 427 HOH HOH A . O 6 HOH 428 1228 428 HOH HOH A . O 6 HOH 429 1229 429 HOH HOH A . O 6 HOH 430 1230 430 HOH HOH A . O 6 HOH 431 1231 431 HOH HOH A . O 6 HOH 432 1232 432 HOH HOH A . O 6 HOH 433 1233 433 HOH HOH A . O 6 HOH 434 1234 434 HOH HOH A . O 6 HOH 435 1235 435 HOH HOH A . O 6 HOH 436 1236 436 HOH HOH A . O 6 HOH 437 1237 437 HOH HOH A . O 6 HOH 438 1238 438 HOH HOH A . O 6 HOH 439 1239 439 HOH HOH A . O 6 HOH 440 1240 440 HOH HOH A . O 6 HOH 441 1241 441 HOH HOH A . O 6 HOH 442 1242 442 HOH HOH A . O 6 HOH 443 1243 443 HOH HOH A . O 6 HOH 444 1244 444 HOH HOH A . O 6 HOH 445 1245 445 HOH HOH A . O 6 HOH 446 1246 446 HOH HOH A . O 6 HOH 447 1247 447 HOH HOH A . O 6 HOH 448 1248 448 HOH HOH A . O 6 HOH 449 1249 449 HOH HOH A . O 6 HOH 450 1250 450 HOH HOH A . O 6 HOH 451 1251 451 HOH HOH A . O 6 HOH 452 1252 452 HOH HOH A . O 6 HOH 453 1253 453 HOH HOH A . O 6 HOH 454 1254 454 HOH HOH A . O 6 HOH 455 1255 455 HOH HOH A . O 6 HOH 456 1256 456 HOH HOH A . O 6 HOH 457 1257 457 HOH HOH A . O 6 HOH 458 1258 458 HOH HOH A . O 6 HOH 459 1259 459 HOH HOH A . O 6 HOH 460 1260 460 HOH HOH A . O 6 HOH 461 1261 461 HOH HOH A . O 6 HOH 462 1262 462 HOH HOH A . O 6 HOH 463 1263 463 HOH HOH A . O 6 HOH 464 1264 464 HOH HOH A . O 6 HOH 465 1265 465 HOH HOH A . O 6 HOH 466 1266 466 HOH HOH A . O 6 HOH 467 1267 467 HOH HOH A . O 6 HOH 468 1268 468 HOH HOH A . O 6 HOH 469 1269 469 HOH HOH A . O 6 HOH 470 1270 470 HOH HOH A . O 6 HOH 471 1271 471 HOH HOH A . O 6 HOH 472 1272 472 HOH HOH A . O 6 HOH 473 1273 473 HOH HOH A . O 6 HOH 474 1274 474 HOH HOH A . O 6 HOH 475 1275 475 HOH HOH A . O 6 HOH 476 1276 476 HOH HOH A . O 6 HOH 477 1277 477 HOH HOH A . O 6 HOH 478 1278 478 HOH HOH A . O 6 HOH 479 1279 479 HOH HOH A . O 6 HOH 480 1280 480 HOH HOH A . O 6 HOH 481 1281 481 HOH HOH A . O 6 HOH 482 1282 482 HOH HOH A . O 6 HOH 483 1283 483 HOH HOH A . O 6 HOH 484 1284 484 HOH HOH A . O 6 HOH 485 1285 485 HOH HOH A . O 6 HOH 486 1286 486 HOH HOH A . O 6 HOH 487 1287 487 HOH HOH A . O 6 HOH 488 1288 488 HOH HOH A . O 6 HOH 489 1289 489 HOH HOH A . O 6 HOH 490 1290 490 HOH HOH A . O 6 HOH 491 1291 491 HOH HOH A . O 6 HOH 492 1292 492 HOH HOH A . O 6 HOH 493 1293 493 HOH HOH A . O 6 HOH 494 1294 494 HOH HOH A . O 6 HOH 495 1295 495 HOH HOH A . O 6 HOH 496 1296 496 HOH HOH A . O 6 HOH 497 1297 497 HOH HOH A . O 6 HOH 498 1298 498 HOH HOH A . O 6 HOH 499 1299 499 HOH HOH A . O 6 HOH 500 1300 500 HOH HOH A . O 6 HOH 501 1301 501 HOH HOH A . O 6 HOH 502 1302 502 HOH HOH A . O 6 HOH 503 1303 503 HOH HOH A . O 6 HOH 504 1304 504 HOH HOH A . O 6 HOH 505 1305 505 HOH HOH A . O 6 HOH 506 1306 506 HOH HOH A . O 6 HOH 507 1307 507 HOH HOH A . O 6 HOH 508 1308 508 HOH HOH A . O 6 HOH 509 1309 509 HOH HOH A . O 6 HOH 510 1310 510 HOH HOH A . O 6 HOH 511 1311 511 HOH HOH A . O 6 HOH 512 1312 512 HOH HOH A . O 6 HOH 513 1313 513 HOH HOH A . O 6 HOH 514 1314 514 HOH HOH A . O 6 HOH 515 1315 515 HOH HOH A . O 6 HOH 516 1316 516 HOH HOH A . O 6 HOH 517 1317 517 HOH HOH A . O 6 HOH 518 1318 518 HOH HOH A . O 6 HOH 519 1319 519 HOH HOH A . O 6 HOH 520 1320 520 HOH HOH A . O 6 HOH 521 1321 521 HOH HOH A . O 6 HOH 522 1322 522 HOH HOH A . O 6 HOH 523 1323 523 HOH HOH A . O 6 HOH 524 1324 524 HOH HOH A . O 6 HOH 525 1325 525 HOH HOH A . O 6 HOH 526 1326 526 HOH HOH A . O 6 HOH 527 1327 527 HOH HOH A . O 6 HOH 528 1328 528 HOH HOH A . O 6 HOH 529 1329 529 HOH HOH A . O 6 HOH 530 1330 530 HOH HOH A . O 6 HOH 531 1331 531 HOH HOH A . O 6 HOH 532 1332 532 HOH HOH A . O 6 HOH 533 1333 533 HOH HOH A . O 6 HOH 534 1334 534 HOH HOH A . O 6 HOH 535 1335 535 HOH HOH A . O 6 HOH 536 1336 536 HOH HOH A . O 6 HOH 537 1337 537 HOH HOH A . O 6 HOH 538 1338 538 HOH HOH A . O 6 HOH 539 1339 539 HOH HOH A . O 6 HOH 540 1340 540 HOH HOH A . O 6 HOH 541 1341 541 HOH HOH A . O 6 HOH 542 1342 542 HOH HOH A . O 6 HOH 543 1343 543 HOH HOH A . O 6 HOH 544 1344 544 HOH HOH A . O 6 HOH 545 1345 545 HOH HOH A . O 6 HOH 546 1346 546 HOH HOH A . O 6 HOH 547 1347 547 HOH HOH A . O 6 HOH 548 1348 548 HOH HOH A . O 6 HOH 549 1349 549 HOH HOH A . O 6 HOH 550 1350 550 HOH HOH A . O 6 HOH 551 1351 551 HOH HOH A . O 6 HOH 552 1352 552 HOH HOH A . O 6 HOH 553 1353 553 HOH HOH A . O 6 HOH 554 1354 554 HOH HOH A . O 6 HOH 555 1355 555 HOH HOH A . O 6 HOH 556 1356 556 HOH HOH A . O 6 HOH 557 1357 557 HOH HOH A . O 6 HOH 558 1358 558 HOH HOH A . O 6 HOH 559 1359 559 HOH HOH A . O 6 HOH 560 1360 560 HOH HOH A . O 6 HOH 561 1361 561 HOH HOH A . O 6 HOH 562 1362 562 HOH HOH A . O 6 HOH 563 1363 563 HOH HOH A . O 6 HOH 564 1364 564 HOH HOH A . O 6 HOH 565 1365 565 HOH HOH A . O 6 HOH 566 1366 566 HOH HOH A . O 6 HOH 567 1367 567 HOH HOH A . O 6 HOH 568 1368 568 HOH HOH A . O 6 HOH 569 1369 569 HOH HOH A . O 6 HOH 570 1370 570 HOH HOH A . O 6 HOH 571 1371 571 HOH HOH A . O 6 HOH 572 1372 572 HOH HOH A . O 6 HOH 573 1373 573 HOH HOH A . O 6 HOH 574 1374 574 HOH HOH A . O 6 HOH 575 1375 575 HOH HOH A . O 6 HOH 576 1376 576 HOH HOH A . O 6 HOH 577 1377 577 HOH HOH A . O 6 HOH 578 1378 578 HOH HOH A . O 6 HOH 579 1379 579 HOH HOH A . O 6 HOH 580 1380 580 HOH HOH A . O 6 HOH 581 1381 581 HOH HOH A . O 6 HOH 582 1382 582 HOH HOH A . O 6 HOH 583 1383 583 HOH HOH A . O 6 HOH 584 1384 584 HOH HOH A . O 6 HOH 585 1385 585 HOH HOH A . O 6 HOH 586 1386 586 HOH HOH A . O 6 HOH 587 1387 587 HOH HOH A . O 6 HOH 588 1388 588 HOH HOH A . O 6 HOH 589 1389 589 HOH HOH A . O 6 HOH 590 1390 590 HOH HOH A . O 6 HOH 591 1391 591 HOH HOH A . O 6 HOH 592 1392 592 HOH HOH A . O 6 HOH 593 1393 593 HOH HOH A . O 6 HOH 594 1394 594 HOH HOH A . O 6 HOH 595 1395 595 HOH HOH A . O 6 HOH 596 1396 596 HOH HOH A . O 6 HOH 597 1397 597 HOH HOH A . O 6 HOH 598 1398 598 HOH HOH A . O 6 HOH 599 1399 599 HOH HOH A . O 6 HOH 600 1400 600 HOH HOH A . O 6 HOH 601 1401 601 HOH HOH A . O 6 HOH 602 1402 602 HOH HOH A . O 6 HOH 603 1403 603 HOH HOH A . O 6 HOH 604 1404 604 HOH HOH A . O 6 HOH 605 1405 605 HOH HOH A . O 6 HOH 606 1406 606 HOH HOH A . O 6 HOH 607 1407 607 HOH HOH A . O 6 HOH 608 1408 608 HOH HOH A . O 6 HOH 609 1409 609 HOH HOH A . O 6 HOH 610 1410 610 HOH HOH A . O 6 HOH 611 1411 611 HOH HOH A . O 6 HOH 612 1412 612 HOH HOH A . O 6 HOH 613 1413 613 HOH HOH A . O 6 HOH 614 1414 614 HOH HOH A . O 6 HOH 615 1415 615 HOH HOH A . O 6 HOH 616 1416 616 HOH HOH A . O 6 HOH 617 1417 617 HOH HOH A . O 6 HOH 618 1418 618 HOH HOH A . O 6 HOH 619 1419 619 HOH HOH A . O 6 HOH 620 1420 620 HOH HOH A . O 6 HOH 621 1421 621 HOH HOH A . O 6 HOH 622 1422 622 HOH HOH A . O 6 HOH 623 1423 623 HOH HOH A . O 6 HOH 624 1424 624 HOH HOH A . O 6 HOH 625 1425 625 HOH HOH A . O 6 HOH 626 1426 626 HOH HOH A . O 6 HOH 627 1427 627 HOH HOH A . O 6 HOH 628 1428 628 HOH HOH A . O 6 HOH 629 1429 629 HOH HOH A . O 6 HOH 630 1430 630 HOH HOH A . O 6 HOH 631 1431 631 HOH HOH A . O 6 HOH 632 1432 632 HOH HOH A . O 6 HOH 633 1433 633 HOH HOH A . O 6 HOH 634 1434 634 HOH HOH A . O 6 HOH 635 1435 635 HOH HOH A . O 6 HOH 636 1436 636 HOH HOH A . O 6 HOH 637 1437 637 HOH HOH A . O 6 HOH 638 1438 638 HOH HOH A . O 6 HOH 639 1439 639 HOH HOH A . O 6 HOH 640 1440 640 HOH HOH A . O 6 HOH 641 1441 641 HOH HOH A . O 6 HOH 642 1442 642 HOH HOH A . O 6 HOH 643 1443 643 HOH HOH A . O 6 HOH 644 1444 644 HOH HOH A . O 6 HOH 645 1445 645 HOH HOH A . O 6 HOH 646 1446 646 HOH HOH A . O 6 HOH 647 1447 647 HOH HOH A . O 6 HOH 648 1448 648 HOH HOH A . O 6 HOH 649 1449 649 HOH HOH A . O 6 HOH 650 1450 650 HOH HOH A . O 6 HOH 651 1451 651 HOH HOH A . O 6 HOH 652 1452 652 HOH HOH A . O 6 HOH 653 1453 653 HOH HOH A . O 6 HOH 654 1454 654 HOH HOH A . O 6 HOH 655 1455 655 HOH HOH A . O 6 HOH 656 1456 656 HOH HOH A . O 6 HOH 657 1457 657 HOH HOH A . O 6 HOH 658 1458 658 HOH HOH A . O 6 HOH 659 1459 659 HOH HOH A . O 6 HOH 660 1460 660 HOH HOH A . O 6 HOH 661 1461 661 HOH HOH A . O 6 HOH 662 1462 662 HOH HOH A . O 6 HOH 663 1463 663 HOH HOH A . O 6 HOH 664 1464 664 HOH HOH A . O 6 HOH 665 1465 665 HOH HOH A . O 6 HOH 666 1466 666 HOH HOH A . O 6 HOH 667 1467 667 HOH HOH A . O 6 HOH 668 1468 668 HOH HOH A . O 6 HOH 669 1469 669 HOH HOH A . O 6 HOH 670 1470 670 HOH HOH A . O 6 HOH 671 1471 671 HOH HOH A . O 6 HOH 672 1472 672 HOH HOH A . O 6 HOH 673 1473 673 HOH HOH A . O 6 HOH 674 1474 674 HOH HOH A . O 6 HOH 675 1475 675 HOH HOH A . O 6 HOH 676 1476 676 HOH HOH A . O 6 HOH 677 1477 677 HOH HOH A . O 6 HOH 678 1478 678 HOH HOH A . O 6 HOH 679 1479 679 HOH HOH A . O 6 HOH 680 1480 680 HOH HOH A . O 6 HOH 681 1481 681 HOH HOH A . O 6 HOH 682 1482 682 HOH HOH A . O 6 HOH 683 1483 683 HOH HOH A . O 6 HOH 684 1484 684 HOH HOH A . O 6 HOH 685 1485 685 HOH HOH A . O 6 HOH 686 1486 686 HOH HOH A . O 6 HOH 687 1487 687 HOH HOH A . O 6 HOH 688 1488 688 HOH HOH A . O 6 HOH 689 1489 689 HOH HOH A . O 6 HOH 690 1490 690 HOH HOH A . O 6 HOH 691 1491 691 HOH HOH A . O 6 HOH 692 1492 692 HOH HOH A . O 6 HOH 693 1493 693 HOH HOH A . O 6 HOH 694 1494 694 HOH HOH A . O 6 HOH 695 1495 695 HOH HOH A . O 6 HOH 696 1496 696 HOH HOH A . O 6 HOH 697 1497 697 HOH HOH A . O 6 HOH 698 1498 698 HOH HOH A . O 6 HOH 699 1499 699 HOH HOH A . O 6 HOH 700 1500 700 HOH HOH A . O 6 HOH 701 1501 701 HOH HOH A . O 6 HOH 702 1502 702 HOH HOH A . O 6 HOH 703 1503 703 HOH HOH A . O 6 HOH 704 1504 704 HOH HOH A . O 6 HOH 705 1505 705 HOH HOH A . O 6 HOH 706 1506 706 HOH HOH A . O 6 HOH 707 1507 707 HOH HOH A . O 6 HOH 708 1508 708 HOH HOH A . O 6 HOH 709 1509 709 HOH HOH A . O 6 HOH 710 1510 710 HOH HOH A . O 6 HOH 711 1511 711 HOH HOH A . O 6 HOH 712 1512 712 HOH HOH A . O 6 HOH 713 1513 713 HOH HOH A . O 6 HOH 714 1514 714 HOH HOH A . O 6 HOH 715 1515 715 HOH HOH A . O 6 HOH 716 1516 716 HOH HOH A . O 6 HOH 717 1517 717 HOH HOH A . O 6 HOH 718 1518 718 HOH HOH A . O 6 HOH 719 1519 719 HOH HOH A . O 6 HOH 720 1520 720 HOH HOH A . O 6 HOH 721 1521 721 HOH HOH A . O 6 HOH 722 1522 722 HOH HOH A . O 6 HOH 723 1523 723 HOH HOH A . O 6 HOH 724 1524 724 HOH HOH A . O 6 HOH 725 1525 725 HOH HOH A . O 6 HOH 726 1526 726 HOH HOH A . O 6 HOH 727 1527 727 HOH HOH A . O 6 HOH 728 1528 728 HOH HOH A . O 6 HOH 729 1529 729 HOH HOH A . O 6 HOH 730 1530 730 HOH HOH A . O 6 HOH 731 1531 731 HOH HOH A . O 6 HOH 732 1532 732 HOH HOH A . O 6 HOH 733 1533 733 HOH HOH A . O 6 HOH 734 1534 734 HOH HOH A . O 6 HOH 735 1535 735 HOH HOH A . O 6 HOH 736 1536 736 HOH HOH A . O 6 HOH 737 1537 737 HOH HOH A . O 6 HOH 738 1538 738 HOH HOH A . O 6 HOH 739 1539 739 HOH HOH A . O 6 HOH 740 1540 740 HOH HOH A . O 6 HOH 741 1541 741 HOH HOH A . O 6 HOH 742 1542 742 HOH HOH A . O 6 HOH 743 1543 743 HOH HOH A . O 6 HOH 744 1544 744 HOH HOH A . O 6 HOH 745 1545 745 HOH HOH A . O 6 HOH 746 1546 746 HOH HOH A . O 6 HOH 747 1547 747 HOH HOH A . O 6 HOH 748 1548 748 HOH HOH A . O 6 HOH 749 1549 749 HOH HOH A . O 6 HOH 750 1550 750 HOH HOH A . O 6 HOH 751 1551 751 HOH HOH A . O 6 HOH 752 1552 752 HOH HOH A . O 6 HOH 753 1553 753 HOH HOH A . O 6 HOH 754 1554 754 HOH HOH A . O 6 HOH 755 1555 755 HOH HOH A . O 6 HOH 756 1556 756 HOH HOH A . O 6 HOH 757 1557 757 HOH HOH A . O 6 HOH 758 1558 758 HOH HOH A . O 6 HOH 759 1559 759 HOH HOH A . O 6 HOH 760 1560 760 HOH HOH A . O 6 HOH 761 1561 761 HOH HOH A . O 6 HOH 762 1562 762 HOH HOH A . O 6 HOH 763 1563 763 HOH HOH A . O 6 HOH 764 1564 764 HOH HOH A . O 6 HOH 765 1565 765 HOH HOH A . O 6 HOH 766 1566 766 HOH HOH A . O 6 HOH 767 1567 767 HOH HOH A . O 6 HOH 768 1568 768 HOH HOH A . O 6 HOH 769 1569 769 HOH HOH A . O 6 HOH 770 1570 770 HOH HOH A . O 6 HOH 771 1571 771 HOH HOH A . O 6 HOH 772 1572 772 HOH HOH A . O 6 HOH 773 1573 773 HOH HOH A . O 6 HOH 774 1574 774 HOH HOH A . O 6 HOH 775 1575 775 HOH HOH A . O 6 HOH 776 1576 776 HOH HOH A . O 6 HOH 777 1577 777 HOH HOH A . O 6 HOH 778 1578 778 HOH HOH A . O 6 HOH 779 1579 779 HOH HOH A . O 6 HOH 780 1580 780 HOH HOH A . O 6 HOH 781 1581 781 HOH HOH A . O 6 HOH 782 1582 782 HOH HOH A . O 6 HOH 783 1583 783 HOH HOH A . O 6 HOH 784 1584 784 HOH HOH A . O 6 HOH 785 1585 785 HOH HOH A . O 6 HOH 786 1586 786 HOH HOH A . O 6 HOH 787 1587 787 HOH HOH A . O 6 HOH 788 1588 788 HOH HOH A . O 6 HOH 789 1589 789 HOH HOH A . O 6 HOH 790 1590 790 HOH HOH A . O 6 HOH 791 1591 791 HOH HOH A . O 6 HOH 792 1592 792 HOH HOH A . O 6 HOH 793 1593 793 HOH HOH A . O 6 HOH 794 1594 794 HOH HOH A . O 6 HOH 795 1595 795 HOH HOH A . O 6 HOH 796 1596 796 HOH HOH A . O 6 HOH 797 1597 797 HOH HOH A . O 6 HOH 798 1598 798 HOH HOH A . O 6 HOH 799 1599 799 HOH HOH A . O 6 HOH 800 1600 800 HOH HOH A . O 6 HOH 801 1601 801 HOH HOH A . O 6 HOH 802 1602 802 HOH HOH A . O 6 HOH 803 1603 803 HOH HOH A . O 6 HOH 804 1604 804 HOH HOH A . O 6 HOH 805 1605 805 HOH HOH A . O 6 HOH 806 1606 806 HOH HOH A . O 6 HOH 807 1607 807 HOH HOH A . O 6 HOH 808 1608 808 HOH HOH A . O 6 HOH 809 1609 809 HOH HOH A . O 6 HOH 810 1610 810 HOH HOH A . O 6 HOH 811 1611 811 HOH HOH A . O 6 HOH 812 1612 812 HOH HOH A . O 6 HOH 813 1613 813 HOH HOH A . O 6 HOH 814 1614 814 HOH HOH A . O 6 HOH 815 1615 815 HOH HOH A . O 6 HOH 816 1616 816 HOH HOH A . O 6 HOH 817 1617 817 HOH HOH A . O 6 HOH 818 1618 818 HOH HOH A . O 6 HOH 819 1619 819 HOH HOH A . O 6 HOH 820 1620 820 HOH HOH A . O 6 HOH 821 1621 821 HOH HOH A . O 6 HOH 822 1622 822 HOH HOH A . O 6 HOH 823 1623 823 HOH HOH A . O 6 HOH 824 1624 824 HOH HOH A . O 6 HOH 825 1625 825 HOH HOH A . O 6 HOH 826 1626 826 HOH HOH A . O 6 HOH 827 1627 827 HOH HOH A . O 6 HOH 828 1628 828 HOH HOH A . O 6 HOH 829 1629 829 HOH HOH A . O 6 HOH 830 1630 830 HOH HOH A . O 6 HOH 831 1631 831 HOH HOH A . O 6 HOH 832 1632 832 HOH HOH A . O 6 HOH 833 1633 833 HOH HOH A . O 6 HOH 834 1634 834 HOH HOH A . O 6 HOH 835 1635 835 HOH HOH A . O 6 HOH 836 1636 836 HOH HOH A . O 6 HOH 837 1637 837 HOH HOH A . O 6 HOH 838 1638 838 HOH HOH A . O 6 HOH 839 1639 839 HOH HOH A . O 6 HOH 840 1640 840 HOH HOH A . O 6 HOH 841 1641 841 HOH HOH A . O 6 HOH 842 1642 842 HOH HOH A . O 6 HOH 843 1643 843 HOH HOH A . O 6 HOH 844 1644 844 HOH HOH A . O 6 HOH 845 1645 845 HOH HOH A . O 6 HOH 846 1646 846 HOH HOH A . O 6 HOH 847 1647 847 HOH HOH A . O 6 HOH 848 1648 848 HOH HOH A . O 6 HOH 849 1649 849 HOH HOH A . O 6 HOH 850 1650 850 HOH HOH A . O 6 HOH 851 1651 851 HOH HOH A . O 6 HOH 852 1652 852 HOH HOH A . O 6 HOH 853 1653 853 HOH HOH A . O 6 HOH 854 1654 854 HOH HOH A . O 6 HOH 855 1655 855 HOH HOH A . O 6 HOH 856 1656 856 HOH HOH A . O 6 HOH 857 1657 857 HOH HOH A . O 6 HOH 858 1658 858 HOH HOH A . O 6 HOH 859 1659 859 HOH HOH A . O 6 HOH 860 1660 860 HOH HOH A . O 6 HOH 861 1661 861 HOH HOH A . O 6 HOH 862 1662 862 HOH HOH A . O 6 HOH 863 1663 863 HOH HOH A . O 6 HOH 864 1664 864 HOH HOH A . O 6 HOH 865 1665 865 HOH HOH A . O 6 HOH 866 1666 866 HOH HOH A . O 6 HOH 867 1667 867 HOH HOH A . O 6 HOH 868 1668 868 HOH HOH A . O 6 HOH 869 1669 869 HOH HOH A . O 6 HOH 870 1670 870 HOH HOH A . O 6 HOH 871 1671 871 HOH HOH A . O 6 HOH 872 1672 872 HOH HOH A . O 6 HOH 873 1673 873 HOH HOH A . O 6 HOH 874 1674 874 HOH HOH A . O 6 HOH 875 1675 875 HOH HOH A . O 6 HOH 876 1676 876 HOH HOH A . O 6 HOH 877 1677 877 HOH HOH A . O 6 HOH 878 1678 878 HOH HOH A . O 6 HOH 879 1679 879 HOH HOH A . O 6 HOH 880 1680 880 HOH HOH A . O 6 HOH 881 1681 881 HOH HOH A . O 6 HOH 882 1682 882 HOH HOH A . O 6 HOH 883 1683 883 HOH HOH A . O 6 HOH 884 1684 884 HOH HOH A . O 6 HOH 885 1685 885 HOH HOH A . O 6 HOH 886 1686 886 HOH HOH A . O 6 HOH 887 1687 887 HOH HOH A . O 6 HOH 888 1688 888 HOH HOH A . O 6 HOH 889 1689 889 HOH HOH A . O 6 HOH 890 1690 890 HOH HOH A . O 6 HOH 891 1691 891 HOH HOH A . O 6 HOH 892 1692 892 HOH HOH A . O 6 HOH 893 1693 893 HOH HOH A . O 6 HOH 894 1694 894 HOH HOH A . O 6 HOH 895 1695 895 HOH HOH A . O 6 HOH 896 1696 896 HOH HOH A . O 6 HOH 897 1697 897 HOH HOH A . O 6 HOH 898 1698 898 HOH HOH A . O 6 HOH 899 1699 899 HOH HOH A . O 6 HOH 900 1700 900 HOH HOH A . O 6 HOH 901 1701 901 HOH HOH A . #