data_5DLP # _entry.id 5DLP # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 5DLP WWPDB D_1000213396 # loop_ _pdbx_database_related.db_name _pdbx_database_related.details _pdbx_database_related.db_id _pdbx_database_related.content_type PDB . 2W9I unspecified PDB . 1W6R unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.entry_id 5DLP _pdbx_database_status.recvd_initial_deposition_date 2015-09-07 _pdbx_database_status.SG_entry N _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBE _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # _audit_author.name 'Dym, O.' _audit_author.pdbx_ordinal 1 # _citation.abstract ? _citation.abstract_id_CAS ? _citation.book_id_ISBN ? _citation.book_publisher ? _citation.book_publisher_city ? _citation.book_title ? _citation.coordinate_linkage ? _citation.country US _citation.database_id_Medline ? _citation.details ? _citation.id primary _citation.journal_abbrev 'Protein Sci.' _citation.journal_id_ASTM PRCIEI _citation.journal_id_CSD 0795 _citation.journal_id_ISSN 1469-896X _citation.journal_full ? _citation.journal_issue ? _citation.journal_volume 25 _citation.language ? _citation.page_first 1096 _citation.page_last 1114 _citation.title ;The impact of crystallization conditions on structure-based drug design: A case study on the methylene blue/acetylcholinesterase complex. ; _citation.year 2016 _citation.database_id_CSD ? _citation.pdbx_database_id_DOI 10.1002/pro.2923 _citation.pdbx_database_id_PubMed 26990888 _citation.unpublished_flag ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Dym, O.' 1 primary 'Song, W.' 2 primary 'Felder, C.' 3 primary 'Roth, E.' 4 primary 'Shnyrov, V.' 5 primary 'Ashani, Y.' 6 primary 'Xu, Y.' 7 primary 'Joosten, R.P.' 8 primary 'Weiner, L.' 9 primary 'Sussman, J.L.' 10 primary 'Silman, I.' 11 # _cell.entry_id 5DLP _cell.length_a 111.059 _cell.length_b 111.059 _cell.length_c 137.172 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 6 _cell.pdbx_unique_axis ? # _symmetry.entry_id 5DLP _symmetry.space_group_name_H-M 'P 31 2 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 152 # 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 Acetylcholinesterase 61325.090 1 3.1.1.7 ? ? ? 2 non-polymer syn '3,7-BIS(DIMETHYLAMINO)PHENOTHIAZIN-5-IUM' 284.399 1 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 4 non-polymer man ALPHA-L-FUCOSE 164.156 1 ? ? ? ? 5 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 6 non-polymer man ALPHA-D-MANNOSE 180.156 2 ? ? ? ? 7 non-polymer syn 'SULFATE ION' 96.063 15 ? ? ? ? 8 water nat water 18.015 15 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name AChE # _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 ;DDHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSG SEMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHG SQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAE GRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQIL LGVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNV ICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTG NPNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFLPKLLNATACDGELSS ; _entity_poly.pdbx_seq_one_letter_code_can ;DDHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSG SEMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHG SQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAE GRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQIL LGVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNV ICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTG NPNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFLPKLLNATACDGELSS ; _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 ASP n 1 3 HIS n 1 4 SER n 1 5 GLU n 1 6 LEU n 1 7 LEU n 1 8 VAL n 1 9 ASN n 1 10 THR n 1 11 LYS n 1 12 SER n 1 13 GLY n 1 14 LYS n 1 15 VAL n 1 16 MET n 1 17 GLY n 1 18 THR n 1 19 ARG n 1 20 VAL n 1 21 PRO n 1 22 VAL n 1 23 LEU n 1 24 SER n 1 25 SER n 1 26 HIS n 1 27 ILE n 1 28 SER n 1 29 ALA n 1 30 PHE n 1 31 LEU n 1 32 GLY n 1 33 ILE n 1 34 PRO n 1 35 PHE n 1 36 ALA n 1 37 GLU n 1 38 PRO n 1 39 PRO n 1 40 VAL n 1 41 GLY n 1 42 ASN n 1 43 MET n 1 44 ARG n 1 45 PHE n 1 46 ARG n 1 47 ARG n 1 48 PRO n 1 49 GLU n 1 50 PRO n 1 51 LYS n 1 52 LYS n 1 53 PRO n 1 54 TRP n 1 55 SER n 1 56 GLY n 1 57 VAL n 1 58 TRP n 1 59 ASN n 1 60 ALA n 1 61 SER n 1 62 THR n 1 63 TYR n 1 64 PRO n 1 65 ASN n 1 66 ASN n 1 67 CYS n 1 68 GLN n 1 69 GLN n 1 70 TYR n 1 71 VAL n 1 72 ASP n 1 73 GLU n 1 74 GLN n 1 75 PHE n 1 76 PRO n 1 77 GLY n 1 78 PHE n 1 79 SER n 1 80 GLY n 1 81 SER n 1 82 GLU n 1 83 MET n 1 84 TRP n 1 85 ASN n 1 86 PRO n 1 87 ASN n 1 88 ARG n 1 89 GLU n 1 90 MET n 1 91 SER n 1 92 GLU n 1 93 ASP n 1 94 CYS n 1 95 LEU n 1 96 TYR n 1 97 LEU n 1 98 ASN n 1 99 ILE n 1 100 TRP n 1 101 VAL n 1 102 PRO n 1 103 SER n 1 104 PRO n 1 105 ARG n 1 106 PRO n 1 107 LYS n 1 108 SER n 1 109 THR n 1 110 THR n 1 111 VAL n 1 112 MET n 1 113 VAL n 1 114 TRP n 1 115 ILE n 1 116 TYR n 1 117 GLY n 1 118 GLY n 1 119 GLY n 1 120 PHE n 1 121 TYR n 1 122 SER n 1 123 GLY n 1 124 SER n 1 125 SER n 1 126 THR n 1 127 LEU n 1 128 ASP n 1 129 VAL n 1 130 TYR n 1 131 ASN n 1 132 GLY n 1 133 LYS n 1 134 TYR n 1 135 LEU n 1 136 ALA n 1 137 TYR n 1 138 THR n 1 139 GLU n 1 140 GLU n 1 141 VAL n 1 142 VAL n 1 143 LEU n 1 144 VAL n 1 145 SER n 1 146 LEU n 1 147 SER n 1 148 TYR n 1 149 ARG n 1 150 VAL n 1 151 GLY n 1 152 ALA n 1 153 PHE n 1 154 GLY n 1 155 PHE n 1 156 LEU n 1 157 ALA n 1 158 LEU n 1 159 HIS n 1 160 GLY n 1 161 SER n 1 162 GLN n 1 163 GLU n 1 164 ALA n 1 165 PRO n 1 166 GLY n 1 167 ASN n 1 168 VAL n 1 169 GLY n 1 170 LEU n 1 171 LEU n 1 172 ASP n 1 173 GLN n 1 174 ARG n 1 175 MET n 1 176 ALA n 1 177 LEU n 1 178 GLN n 1 179 TRP n 1 180 VAL n 1 181 HIS n 1 182 ASP n 1 183 ASN n 1 184 ILE n 1 185 GLN n 1 186 PHE n 1 187 PHE n 1 188 GLY n 1 189 GLY n 1 190 ASP n 1 191 PRO n 1 192 LYS n 1 193 THR n 1 194 VAL n 1 195 THR n 1 196 ILE n 1 197 PHE n 1 198 GLY n 1 199 GLU n 1 200 SER n 1 201 ALA n 1 202 GLY n 1 203 GLY n 1 204 ALA n 1 205 SER n 1 206 VAL n 1 207 GLY n 1 208 MET n 1 209 HIS n 1 210 ILE n 1 211 LEU n 1 212 SER n 1 213 PRO n 1 214 GLY n 1 215 SER n 1 216 ARG n 1 217 ASP n 1 218 LEU n 1 219 PHE n 1 220 ARG n 1 221 ARG n 1 222 ALA n 1 223 ILE n 1 224 LEU n 1 225 GLN n 1 226 SER n 1 227 GLY n 1 228 SER n 1 229 PRO n 1 230 ASN n 1 231 CYS n 1 232 PRO n 1 233 TRP n 1 234 ALA n 1 235 SER n 1 236 VAL n 1 237 SER n 1 238 VAL n 1 239 ALA n 1 240 GLU n 1 241 GLY n 1 242 ARG n 1 243 ARG n 1 244 ARG n 1 245 ALA n 1 246 VAL n 1 247 GLU n 1 248 LEU n 1 249 GLY n 1 250 ARG n 1 251 ASN n 1 252 LEU n 1 253 ASN n 1 254 CYS n 1 255 ASN n 1 256 LEU n 1 257 ASN n 1 258 SER n 1 259 ASP n 1 260 GLU n 1 261 GLU n 1 262 LEU n 1 263 ILE n 1 264 HIS n 1 265 CYS n 1 266 LEU n 1 267 ARG n 1 268 GLU n 1 269 LYS n 1 270 LYS n 1 271 PRO n 1 272 GLN n 1 273 GLU n 1 274 LEU n 1 275 ILE n 1 276 ASP n 1 277 VAL n 1 278 GLU n 1 279 TRP n 1 280 ASN n 1 281 VAL n 1 282 LEU n 1 283 PRO n 1 284 PHE n 1 285 ASP n 1 286 SER n 1 287 ILE n 1 288 PHE n 1 289 ARG n 1 290 PHE n 1 291 SER n 1 292 PHE n 1 293 VAL n 1 294 PRO n 1 295 VAL n 1 296 ILE n 1 297 ASP n 1 298 GLY n 1 299 GLU n 1 300 PHE n 1 301 PHE n 1 302 PRO n 1 303 THR n 1 304 SER n 1 305 LEU n 1 306 GLU n 1 307 SER n 1 308 MET n 1 309 LEU n 1 310 ASN n 1 311 SER n 1 312 GLY n 1 313 ASN n 1 314 PHE n 1 315 LYS n 1 316 LYS n 1 317 THR n 1 318 GLN n 1 319 ILE n 1 320 LEU n 1 321 LEU n 1 322 GLY n 1 323 VAL n 1 324 ASN n 1 325 LYS n 1 326 ASP n 1 327 GLU n 1 328 GLY n 1 329 SER n 1 330 PHE n 1 331 PHE n 1 332 LEU n 1 333 LEU n 1 334 TYR n 1 335 GLY n 1 336 ALA n 1 337 PRO n 1 338 GLY n 1 339 PHE n 1 340 SER n 1 341 LYS n 1 342 ASP n 1 343 SER n 1 344 GLU n 1 345 SER n 1 346 LYS n 1 347 ILE n 1 348 SER n 1 349 ARG n 1 350 GLU n 1 351 ASP n 1 352 PHE n 1 353 MET n 1 354 SER n 1 355 GLY n 1 356 VAL n 1 357 LYS n 1 358 LEU n 1 359 SER n 1 360 VAL n 1 361 PRO n 1 362 HIS n 1 363 ALA n 1 364 ASN n 1 365 ASP n 1 366 LEU n 1 367 GLY n 1 368 LEU n 1 369 ASP n 1 370 ALA n 1 371 VAL n 1 372 THR n 1 373 LEU n 1 374 GLN n 1 375 TYR n 1 376 THR n 1 377 ASP n 1 378 TRP n 1 379 MET n 1 380 ASP n 1 381 ASP n 1 382 ASN n 1 383 ASN n 1 384 GLY n 1 385 ILE n 1 386 LYS n 1 387 ASN n 1 388 ARG n 1 389 ASP n 1 390 GLY n 1 391 LEU n 1 392 ASP n 1 393 ASP n 1 394 ILE n 1 395 VAL n 1 396 GLY n 1 397 ASP n 1 398 HIS n 1 399 ASN n 1 400 VAL n 1 401 ILE n 1 402 CYS n 1 403 PRO n 1 404 LEU n 1 405 MET n 1 406 HIS n 1 407 PHE n 1 408 VAL n 1 409 ASN n 1 410 LYS n 1 411 TYR n 1 412 THR n 1 413 LYS n 1 414 PHE n 1 415 GLY n 1 416 ASN n 1 417 GLY n 1 418 THR n 1 419 TYR n 1 420 LEU n 1 421 TYR n 1 422 PHE n 1 423 PHE n 1 424 ASN n 1 425 HIS n 1 426 ARG n 1 427 ALA n 1 428 SER n 1 429 ASN n 1 430 LEU n 1 431 VAL n 1 432 TRP n 1 433 PRO n 1 434 GLU n 1 435 TRP n 1 436 MET n 1 437 GLY n 1 438 VAL n 1 439 ILE n 1 440 HIS n 1 441 GLY n 1 442 TYR n 1 443 GLU n 1 444 ILE n 1 445 GLU n 1 446 PHE n 1 447 VAL n 1 448 PHE n 1 449 GLY n 1 450 LEU n 1 451 PRO n 1 452 LEU n 1 453 VAL n 1 454 LYS n 1 455 GLU n 1 456 LEU n 1 457 ASN n 1 458 TYR n 1 459 THR n 1 460 ALA n 1 461 GLU n 1 462 GLU n 1 463 GLU n 1 464 ALA n 1 465 LEU n 1 466 SER n 1 467 ARG n 1 468 ARG n 1 469 ILE n 1 470 MET n 1 471 HIS n 1 472 TYR n 1 473 TRP n 1 474 ALA n 1 475 THR n 1 476 PHE n 1 477 ALA n 1 478 LYS n 1 479 THR n 1 480 GLY n 1 481 ASN n 1 482 PRO n 1 483 ASN n 1 484 GLU n 1 485 PRO n 1 486 HIS n 1 487 SER n 1 488 GLN n 1 489 GLU n 1 490 SER n 1 491 LYS n 1 492 TRP n 1 493 PRO n 1 494 LEU n 1 495 PHE n 1 496 THR n 1 497 THR n 1 498 LYS n 1 499 GLU n 1 500 GLN n 1 501 LYS n 1 502 PHE n 1 503 ILE n 1 504 ASP n 1 505 LEU n 1 506 ASN n 1 507 THR n 1 508 GLU n 1 509 PRO n 1 510 MET n 1 511 LYS n 1 512 VAL n 1 513 HIS n 1 514 GLN n 1 515 ARG n 1 516 LEU n 1 517 ARG n 1 518 VAL n 1 519 GLN n 1 520 MET n 1 521 CYS n 1 522 VAL n 1 523 PHE n 1 524 TRP n 1 525 ASN n 1 526 GLN n 1 527 PHE n 1 528 LEU n 1 529 PRO n 1 530 LYS n 1 531 LEU n 1 532 LEU n 1 533 ASN n 1 534 ALA n 1 535 THR n 1 536 ALA n 1 537 CYS n 1 538 ASP n 1 539 GLY n 1 540 GLU n 1 541 LEU n 1 542 SER n 1 543 SER 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 1 _entity_src_nat.pdbx_end_seq_num 543 _entity_src_nat.common_name 'Pacific electric ray' _entity_src_nat.pdbx_organism_scientific 'Torpedo californica' _entity_src_nat.pdbx_ncbi_taxonomy_id 7787 _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 ACES_TORCA _struct_ref.pdbx_db_accession P04058 _struct_ref.pdbx_db_isoform ? _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;DDHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSG SEMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHG SQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAE GRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQIL LGVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNV ICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTG NPNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFLPKLLNATACDGELSS ; _struct_ref.pdbx_align_begin 22 # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 5DLP _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 543 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P04058 _struct_ref_seq.db_align_beg 22 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 564 _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 543 # 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 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MBT non-polymer . '3,7-BIS(DIMETHYLAMINO)PHENOTHIAZIN-5-IUM' 'METHYLENE BLUE' 'C16 H18 N3 S 1' 284.399 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 SO4 non-polymer . 'SULFATE ION' ? 'O4 S -2' 96.063 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.absorpt_coefficient_mu ? _exptl.absorpt_correction_T_max ? _exptl.absorpt_correction_T_min ? _exptl.absorpt_correction_type ? _exptl.absorpt_process_details ? _exptl.entry_id 5DLP _exptl.crystals_number 1 _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 3.98 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 69.11 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.id 1 _exptl_crystal.preparation ? _exptl_crystal.size_max ? _exptl_crystal.size_mid ? _exptl_crystal.size_min ? _exptl_crystal.size_rad ? _exptl_crystal.colour_lustre ? _exptl_crystal.colour_modifier ? _exptl_crystal.colour_primary ? _exptl_crystal.density_meas ? _exptl_crystal.density_meas_esd ? _exptl_crystal.density_meas_gt ? _exptl_crystal.density_meas_lt ? _exptl_crystal.density_meas_temp ? _exptl_crystal.density_meas_temp_esd ? _exptl_crystal.density_meas_temp_gt ? _exptl_crystal.density_meas_temp_lt ? _exptl_crystal.pdbx_crystal_image_url ? _exptl_crystal.pdbx_crystal_image_format ? _exptl_crystal.pdbx_mosaicity ? _exptl_crystal.pdbx_mosaicity_esd ? # _exptl_crystal_grow.apparatus ? _exptl_crystal_grow.atmosphere ? _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.details ? _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.method_ref ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pressure ? _exptl_crystal_grow.pressure_esd ? _exptl_crystal_grow.seeding ? _exptl_crystal_grow.seeding_ref ? _exptl_crystal_grow.temp 277 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details '46% PEG200 (v/v) in 100 mM NaCl/1 mM MES, pH 6.5' _exptl_crystal_grow.pdbx_pH_range 6.5 # _diffrn.ambient_environment ? _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.ambient_temp_esd ? _diffrn.crystal_id 1 _diffrn.crystal_support ? _diffrn.crystal_treatment ? _diffrn.details ? _diffrn.id 1 _diffrn.ambient_pressure ? _diffrn.ambient_pressure_esd ? _diffrn.ambient_pressure_gt ? _diffrn.ambient_pressure_lt ? _diffrn.ambient_temp_gt ? _diffrn.ambient_temp_lt ? # _diffrn_detector.details ? _diffrn_detector.detector PIXEL _diffrn_detector.diffrn_id 1 _diffrn_detector.type 'PSI PILATUS 6M' _diffrn_detector.area_resol_mean ? _diffrn_detector.dtime ? _diffrn_detector.pdbx_frames_total ? _diffrn_detector.pdbx_collection_time_total ? _diffrn_detector.pdbx_collection_date 2012-11-07 # _diffrn_radiation.collimation ? _diffrn_radiation.diffrn_id 1 _diffrn_radiation.filter_edge ? _diffrn_radiation.inhomogeneity ? _diffrn_radiation.monochromator ? _diffrn_radiation.polarisn_norm ? _diffrn_radiation.polarisn_ratio ? _diffrn_radiation.probe ? _diffrn_radiation.type ? _diffrn_radiation.xray_symbol ? _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_wavelength_list ? _diffrn_radiation.pdbx_wavelength ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_analyzer ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.0000 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.current ? _diffrn_source.details ? _diffrn_source.diffrn_id 1 _diffrn_source.power ? _diffrn_source.size ? _diffrn_source.source SYNCHROTRON _diffrn_source.target ? _diffrn_source.type 'SLS BEAMLINE X10SA' _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 1.0000 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline X10SA _diffrn_source.pdbx_synchrotron_site SLS # _reflns.B_iso_Wilson_estimate ? _reflns.entry_id 5DLP _reflns.data_reduction_details ? _reflns.data_reduction_method ? _reflns.d_resolution_high 2.7 _reflns.d_resolution_low 96.18 _reflns.details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.number_all ? _reflns.number_obs 27016 _reflns.observed_criterion ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.observed_criterion_I_max ? _reflns.observed_criterion_I_min ? _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.percent_possible_obs 98.9 _reflns.R_free_details ? _reflns.Rmerge_F_all ? _reflns.Rmerge_F_obs ? _reflns.Friedel_coverage ? _reflns.number_gt ? _reflns.threshold_expression ? _reflns.pdbx_redundancy 6.4 _reflns.pdbx_Rmerge_I_obs 0.104 _reflns.pdbx_Rmerge_I_all ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_av_sigmaI ? _reflns.pdbx_netI_over_sigmaI 6.4 _reflns.pdbx_res_netI_over_av_sigmaI_2 ? _reflns.pdbx_res_netI_over_sigmaI_2 ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_d_res_high_opt ? _reflns.pdbx_d_res_low_opt ? _reflns.pdbx_d_res_opt_method ? _reflns.phase_calculation_details ? _reflns.pdbx_Rrim_I_all ? _reflns.pdbx_Rpim_I_all ? _reflns.pdbx_d_opt ? _reflns.pdbx_number_measured_all ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.pdbx_CC_half ? _reflns.pdbx_R_split ? # _reflns_shell.d_res_high 2.7 _reflns_shell.d_res_low 2.85 _reflns_shell.meanI_over_sigI_all ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_possible ? _reflns_shell.number_unique_all ? _reflns_shell.number_unique_obs ? _reflns_shell.percent_possible_all ? _reflns_shell.percent_possible_obs ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.Rmerge_I_obs 0.643 _reflns_shell.meanI_over_sigI_gt ? _reflns_shell.meanI_over_uI_all ? _reflns_shell.meanI_over_uI_gt ? _reflns_shell.number_measured_gt ? _reflns_shell.number_unique_gt ? _reflns_shell.percent_possible_gt ? _reflns_shell.Rmerge_F_gt ? _reflns_shell.Rmerge_I_gt ? _reflns_shell.pdbx_redundancy ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_netI_over_sigmaI_all ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_CC_half ? _reflns_shell.pdbx_R_split ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 5DLP _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 25658 _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 96.18 _refine.ls_d_res_high 2.70 _refine.ls_percent_reflns_obs 98.54 _refine.ls_R_factor_obs 0.19409 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.19254 _refine.ls_R_factor_R_free 0.22378 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 1356 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.944 _refine.correlation_coeff_Fo_to_Fc_free 0.924 _refine.B_iso_mean 52.018 _refine.aniso_B[1][1] -0.33 _refine.aniso_B[2][2] -0.33 _refine.aniso_B[3][3] 1.06 _refine.aniso_B[1][2] -0.16 _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 2W9I _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 0.391 _refine.pdbx_overall_ESU_R_Free 0.255 _refine.overall_SU_ML 0.203 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 22.738 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 4179 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 194 _refine_hist.number_atoms_solvent 15 _refine_hist.number_atoms_total 4388 _refine_hist.d_res_high 2.70 _refine_hist.d_res_low 96.18 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.007 0.019 ? 4493 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 4035 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.201 1.987 ? 6134 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.731 3.000 ? 9250 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.890 5.000 ? 531 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 32.203 23.950 ? 200 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 13.322 15.000 ? 667 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 14.873 15.000 ? 22 'X-RAY DIFFRACTION' ? r_chiral_restr 0.065 0.200 ? 672 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.005 0.021 ? 4996 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 1062 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 1.162 3.383 ? 2127 'X-RAY DIFFRACTION' ? r_mcbond_other 1.157 3.381 ? 2126 'X-RAY DIFFRACTION' ? r_mcangle_it 1.934 5.075 ? 2657 'X-RAY DIFFRACTION' ? r_mcangle_other 1.935 5.076 ? 2658 'X-RAY DIFFRACTION' ? r_scbond_it 1.460 3.775 ? 2366 'X-RAY DIFFRACTION' ? r_scbond_other 1.400 3.680 ? 2306 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other 2.346 5.481 ? 3388 'X-RAY DIFFRACTION' ? r_long_range_B_refined 4.690 28.993 ? 5152 'X-RAY DIFFRACTION' ? r_long_range_B_other 4.692 28.992 ? 5151 '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 2.700 _refine_ls_shell.d_res_low 2.770 _refine_ls_shell.number_reflns_R_work 1889 _refine_ls_shell.R_factor_R_work 0.270 _refine_ls_shell.percent_reflns_obs 98.50 _refine_ls_shell.R_factor_R_free 0.337 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 84 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 5DLP _struct.title 'Acetycholinesterase Methylene Blue no PEG' _struct.pdbx_descriptor 'Acetylcholinesterase (E.C.3.1.1.7)' _struct.pdbx_model_details ? _struct.pdbx_formula_weight ? _struct.pdbx_formula_weight_method ? _struct.pdbx_model_type_details ? _struct.pdbx_CASP_flag ? # _struct_keywords.entry_id 5DLP _struct_keywords.text 'Inhibitor, hydrolase' _struct_keywords.pdbx_keywords HYDROLASE # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 3 ? F N N 3 ? G N N 3 ? H N N 5 ? I N N 6 ? J N N 6 ? K N N 7 ? L N N 7 ? M N N 7 ? N N N 7 ? O N N 7 ? P N N 7 ? Q N N 7 ? R N N 7 ? S N N 7 ? T N N 7 ? U N N 7 ? V N N 7 ? W N N 7 ? X N N 7 ? Y N N 7 ? Z N N 8 ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 AA1 VAL A 40 ? ARG A 44 ? VAL A 40 ARG A 44 5 ? 5 HELX_P HELX_P2 AA2 PHE A 78 ? MET A 83 ? PHE A 78 MET A 83 1 ? 6 HELX_P HELX_P3 AA3 LEU A 127 ? ASN A 131 ? LEU A 127 ASN A 131 5 ? 5 HELX_P HELX_P4 AA4 GLY A 132 ? GLU A 140 ? GLY A 132 GLU A 140 1 ? 9 HELX_P HELX_P5 AA5 VAL A 150 ? LEU A 156 ? VAL A 150 LEU A 156 1 ? 7 HELX_P HELX_P6 AA6 ASN A 167 ? ILE A 184 ? ASN A 167 ILE A 184 1 ? 18 HELX_P HELX_P7 AA7 GLN A 185 ? PHE A 187 ? GLN A 185 PHE A 187 5 ? 3 HELX_P HELX_P8 AA8 SER A 200 ? SER A 212 ? SER A 200 SER A 212 1 ? 13 HELX_P HELX_P9 AA9 SER A 212 ? ASP A 217 ? SER A 212 ASP A 217 1 ? 6 HELX_P HELX_P10 AB1 SER A 237 ? LEU A 252 ? SER A 237 LEU A 252 1 ? 16 HELX_P HELX_P11 AB2 SER A 258 ? LYS A 269 ? SER A 258 LYS A 269 1 ? 12 HELX_P HELX_P12 AB3 LYS A 270 ? ASP A 276 ? LYS A 270 ASP A 276 1 ? 7 HELX_P HELX_P13 AB4 VAL A 277 ? LEU A 282 ? VAL A 277 LEU A 282 5 ? 6 HELX_P HELX_P14 AB5 SER A 304 ? GLY A 312 ? SER A 304 GLY A 312 1 ? 9 HELX_P HELX_P15 AB6 GLY A 328 ? ALA A 336 ? GLY A 328 ALA A 336 1 ? 9 HELX_P HELX_P16 AB7 SER A 348 ? VAL A 360 ? SER A 348 VAL A 360 1 ? 13 HELX_P HELX_P17 AB8 ASN A 364 ? THR A 376 ? ASN A 364 THR A 376 1 ? 13 HELX_P HELX_P18 AB9 ASP A 377 ? ASP A 381 ? ASP A 377 ASP A 381 5 ? 5 HELX_P HELX_P19 AC1 ASN A 383 ? VAL A 400 ? ASN A 383 VAL A 400 1 ? 18 HELX_P HELX_P20 AC2 VAL A 400 ? LYS A 413 ? VAL A 400 LYS A 413 1 ? 14 HELX_P HELX_P21 AC3 PRO A 433 ? GLY A 437 ? PRO A 433 GLY A 437 5 ? 5 HELX_P HELX_P22 AC4 GLU A 443 ? PHE A 448 ? GLU A 443 PHE A 448 1 ? 6 HELX_P HELX_P23 AC5 GLY A 449 ? ASN A 457 ? GLY A 449 ASN A 457 5 ? 9 HELX_P HELX_P24 AC6 THR A 459 ? GLY A 480 ? THR A 459 GLY A 480 1 ? 22 HELX_P HELX_P25 AC7 ARG A 517 ? GLN A 526 ? ARG A 517 GLN A 526 1 ? 10 HELX_P HELX_P26 AC8 GLN A 526 ? THR A 535 ? GLN A 526 THR A 535 1 ? 10 # _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 67 SG ? ? ? 1_555 A CYS 94 SG ? ? A CYS 67 A CYS 94 1_555 ? ? ? ? ? ? ? 2.042 ? disulf2 disulf ? ? A CYS 254 SG ? ? ? 1_555 A CYS 265 SG ? ? A CYS 254 A CYS 265 1_555 ? ? ? ? ? ? ? 2.034 ? disulf3 disulf ? ? A CYS 402 SG ? ? ? 1_555 A CYS 521 SG ? ? A CYS 402 A CYS 521 1_555 ? ? ? ? ? ? ? 2.037 ? covale1 covale one ? A ASN 59 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 59 A NAG 602 1_555 ? ? ? ? ? ? ? 1.458 ? covale2 covale one ? A ASN 416 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 416 A NAG 604 1_555 ? ? ? ? ? ? ? 1.454 ? covale3 covale one ? A ASN 457 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 457 A NAG 605 1_555 ? ? ? ? ? ? ? 1.463 ? covale4 covale one ? C NAG . O6 ? ? ? 1_555 D FUC . C1 ? ? A NAG 602 A FUC 603 1_555 ? ? ? ? ? ? ? 1.446 ? covale5 covale both ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 605 A NAG 606 1_555 ? ? ? ? ? ? ? 1.454 ? covale6 covale both ? G NAG . O4 ? ? ? 1_555 H BMA . C1 ? ? A NAG 606 A BMA 607 1_555 ? ? ? ? ? ? ? 1.449 ? covale7 covale one ? H BMA . O3 ? ? ? 1_555 I MAN . C1 ? ? A BMA 607 A MAN 608 1_555 ? ? ? ? ? ? ? 1.463 ? covale8 covale one ? I MAN . O2 ? ? ? 1_555 J MAN . C1 ? ? A MAN 608 A MAN 609 1_555 ? ? ? ? ? ? ? 1.452 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # _struct_mon_prot_cis.pdbx_id 1 _struct_mon_prot_cis.label_comp_id SER _struct_mon_prot_cis.label_seq_id 103 _struct_mon_prot_cis.label_asym_id A _struct_mon_prot_cis.label_alt_id . _struct_mon_prot_cis.pdbx_PDB_ins_code ? _struct_mon_prot_cis.auth_comp_id SER _struct_mon_prot_cis.auth_seq_id 103 _struct_mon_prot_cis.auth_asym_id A _struct_mon_prot_cis.pdbx_label_comp_id_2 PRO _struct_mon_prot_cis.pdbx_label_seq_id_2 104 _struct_mon_prot_cis.pdbx_label_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_ins_code_2 ? _struct_mon_prot_cis.pdbx_auth_comp_id_2 PRO _struct_mon_prot_cis.pdbx_auth_seq_id_2 104 _struct_mon_prot_cis.pdbx_auth_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_model_num 1 _struct_mon_prot_cis.pdbx_omega_angle -1.33 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 3 ? AA2 ? 11 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA1 1 2 ? anti-parallel AA1 2 3 ? parallel AA2 1 2 ? anti-parallel AA2 2 3 ? anti-parallel AA2 3 4 ? anti-parallel AA2 4 5 ? parallel AA2 5 6 ? parallel AA2 6 7 ? parallel AA2 7 8 ? parallel AA2 8 9 ? parallel AA2 9 10 ? parallel AA2 10 11 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA1 1 LEU A 7 ? THR A 10 ? LEU A 7 THR A 10 AA1 2 GLY A 13 ? MET A 16 ? GLY A 13 MET A 16 AA1 3 VAL A 57 ? ASN A 59 ? VAL A 57 ASN A 59 AA2 1 THR A 18 ? VAL A 22 ? THR A 18 VAL A 22 AA2 2 SER A 25 ? PRO A 34 ? SER A 25 PRO A 34 AA2 3 TYR A 96 ? VAL A 101 ? TYR A 96 VAL A 101 AA2 4 VAL A 142 ? SER A 145 ? VAL A 142 SER A 145 AA2 5 THR A 109 ? ILE A 115 ? THR A 109 ILE A 115 AA2 6 GLY A 189 ? GLU A 199 ? GLY A 189 GLU A 199 AA2 7 ARG A 221 ? GLN A 225 ? ARG A 221 GLN A 225 AA2 8 GLN A 318 ? ASN A 324 ? GLN A 318 ASN A 324 AA2 9 GLY A 417 ? PHE A 423 ? GLY A 417 PHE A 423 AA2 10 LYS A 501 ? LEU A 505 ? LYS A 501 LEU A 505 AA2 11 VAL A 512 ? GLN A 514 ? VAL A 512 GLN A 514 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id AA1 1 2 N VAL A 8 ? N VAL A 8 O VAL A 15 ? O VAL A 15 AA1 2 3 N MET A 16 ? N MET A 16 O TRP A 58 ? O TRP A 58 AA2 1 2 N THR A 18 ? N THR A 18 O ALA A 29 ? O ALA A 29 AA2 2 3 N PHE A 30 ? N PHE A 30 O ILE A 99 ? O ILE A 99 AA2 3 4 N TRP A 100 ? N TRP A 100 O LEU A 143 ? O LEU A 143 AA2 4 5 O VAL A 144 ? O VAL A 144 N TRP A 114 ? N TRP A 114 AA2 5 6 N VAL A 113 ? N VAL A 113 O THR A 195 ? O THR A 195 AA2 6 7 N GLY A 198 ? N GLY A 198 O GLN A 225 ? O GLN A 225 AA2 7 8 N LEU A 224 ? N LEU A 224 O LEU A 320 ? O LEU A 320 AA2 8 9 N VAL A 323 ? N VAL A 323 O PHE A 423 ? O PHE A 423 AA2 9 10 N PHE A 422 ? N PHE A 422 O ILE A 503 ? O ILE A 503 AA2 10 11 N PHE A 502 ? N PHE A 502 O HIS A 513 ? O HIS A 513 # 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 A MBT 601 ? 7 'binding site for residue MBT A 601' AC2 Software A SO4 610 ? 2 'binding site for residue SO4 A 610' AC3 Software A SO4 611 ? 2 'binding site for residue SO4 A 611' AC4 Software A SO4 612 ? 3 'binding site for residue SO4 A 612' AC5 Software A SO4 613 ? 4 'binding site for residue SO4 A 613' AC6 Software A SO4 614 ? 3 'binding site for residue SO4 A 614' AC7 Software A SO4 615 ? 5 'binding site for residue SO4 A 615' AC8 Software A SO4 616 ? 3 'binding site for residue SO4 A 616' AC9 Software A SO4 617 ? 4 'binding site for residue SO4 A 617' AD1 Software A SO4 618 ? 5 'binding site for residue SO4 A 618' AD2 Software A SO4 619 ? 2 'binding site for residue SO4 A 619' AD3 Software A SO4 620 ? 3 'binding site for residue SO4 A 620' AD4 Software A SO4 621 ? 3 'binding site for residue SO4 A 621' AD5 Software A SO4 622 ? 2 'binding site for residue SO4 A 622' AD6 Software A SO4 623 ? 5 'binding site for residue SO4 A 623' AD7 Software A SO4 624 ? 3 'binding site for residue SO4 A 624' AD8 Software A ASN 59 ? 2 'binding site for Poly-Saccharide residues NAG A 602 through FUC A 603 bound to ASN A 59' AD9 Software A NAG 604 ? 2 'binding site for Mono-Saccharide NAG A 604 bound to ASN A 416' AE1 Software A ASN 457 ? 5 'binding site for Poly-Saccharide residues NAG A 605 through MAN A 609 bound to ASN A 457' # 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 7 TYR A 70 ? TYR A 70 . ? 1_555 ? 2 AC1 7 TYR A 121 ? TYR A 121 . ? 1_555 ? 3 AC1 7 TRP A 279 ? TRP A 279 . ? 1_555 ? 4 AC1 7 PHE A 330 ? PHE A 330 . ? 1_555 ? 5 AC1 7 PHE A 331 ? PHE A 331 . ? 1_555 ? 6 AC1 7 TYR A 334 ? TYR A 334 . ? 1_555 ? 7 AC1 7 HOH Z . ? HOH A 702 . ? 1_555 ? 8 AC2 2 SER A 237 ? SER A 237 . ? 1_555 ? 9 AC2 2 ARG A 243 ? ARG A 243 . ? 1_555 ? 10 AC3 2 LYS A 346 ? LYS A 346 . ? 1_555 ? 11 AC3 2 GLY A 384 ? GLY A 384 . ? 1_555 ? 12 AC4 3 MET A 379 ? MET A 379 . ? 6_555 ? 13 AC4 3 HIS A 513 ? HIS A 513 . ? 1_555 ? 14 AC4 3 GLN A 514 ? GLN A 514 . ? 1_555 ? 15 AC5 4 PRO A 106 ? PRO A 106 . ? 1_555 ? 16 AC5 4 LYS A 107 ? LYS A 107 . ? 1_555 ? 17 AC5 4 SER A 108 ? SER A 108 . ? 1_555 ? 18 AC5 4 THR A 109 ? THR A 109 . ? 1_555 ? 19 AC6 3 HIS A 406 ? HIS A 406 . ? 1_555 ? 20 AC6 3 ASN A 525 ? ASN A 525 . ? 1_555 ? 21 AC6 3 GLN A 526 ? GLN A 526 . ? 1_555 ? 22 AC7 5 ASN A 424 ? ASN A 424 . ? 1_555 ? 23 AC7 5 HIS A 425 ? HIS A 425 . ? 1_555 ? 24 AC7 5 ASN A 506 ? ASN A 506 . ? 1_555 ? 25 AC7 5 THR A 507 ? THR A 507 . ? 1_555 ? 26 AC7 5 GLU A 508 ? GLU A 508 . ? 1_555 ? 27 AC8 3 THR A 459 ? THR A 459 . ? 1_555 ? 28 AC8 3 ALA A 460 ? ALA A 460 . ? 1_555 ? 29 AC8 3 GLU A 461 ? GLU A 461 . ? 1_555 ? 30 AC9 4 VAL A 22 ? VAL A 22 . ? 1_555 ? 31 AC9 4 LEU A 23 ? LEU A 23 . ? 1_555 ? 32 AC9 4 LYS A 133 ? LYS A 133 . ? 1_555 ? 33 AC9 4 TYR A 134 ? TYR A 134 . ? 1_555 ? 34 AD1 5 ARG A 289 ? ARG A 289 . ? 1_555 ? 35 AD1 5 VAL A 360 ? VAL A 360 . ? 1_555 ? 36 AD1 5 PRO A 361 ? PRO A 361 . ? 1_555 ? 37 AD1 5 HIS A 362 ? HIS A 362 . ? 1_555 ? 38 AD1 5 HIS A 398 ? HIS A 398 . ? 1_555 ? 39 AD2 2 PRO A 433 ? PRO A 433 . ? 1_555 ? 40 AD2 2 GLU A 434 ? GLU A 434 . ? 1_555 ? 41 AD3 3 GLN A 68 ? GLN A 68 . ? 1_555 ? 42 AD3 3 SER A 91 ? SER A 91 . ? 1_555 ? 43 AD3 3 GLU A 92 ? GLU A 92 . ? 1_555 ? 44 AD4 3 PRO A 213 ? PRO A 213 . ? 2_565 ? 45 AD4 3 SER A 343 ? SER A 343 . ? 1_555 ? 46 AD4 3 GLU A 344 ? GLU A 344 . ? 1_555 ? 47 AD5 2 SER A 490 ? SER A 490 . ? 1_555 ? 48 AD5 2 LYS A 491 ? LYS A 491 . ? 1_555 ? 49 AD6 5 PRO A 76 ? PRO A 76 . ? 3_454 ? 50 AD6 5 ARG A 220 ? ARG A 220 . ? 1_555 ? 51 AD6 5 ARG A 221 ? ARG A 221 . ? 1_555 ? 52 AD6 5 GLN A 318 ? GLN A 318 . ? 1_555 ? 53 AD6 5 ASN A 416 ? ASN A 416 . ? 1_555 ? 54 AD7 3 ARG A 46 ? ARG A 46 . ? 2_565 ? 55 AD7 3 GLN A 162 ? GLN A 162 . ? 2_565 ? 56 AD7 3 ASN A 382 ? ASN A 382 . ? 1_555 ? 57 AD8 2 ASN A 59 ? ASN A 59 . ? 1_555 ? 58 AD8 2 SER A 61 ? SER A 61 . ? 1_555 ? 59 AD9 2 ASN A 416 ? ASN A 416 . ? 1_555 ? 60 AD9 2 MAN J . ? MAN A 609 . ? 3_454 ? 61 AE1 5 LYS A 413 ? LYS A 413 . ? 2_565 ? 62 AE1 5 PHE A 414 ? PHE A 414 . ? 2_565 ? 63 AE1 5 GLU A 455 ? GLU A 455 . ? 1_555 ? 64 AE1 5 ASN A 457 ? ASN A 457 . ? 1_555 ? 65 AE1 5 NAG E . ? NAG A 604 . ? 2_565 ? # _atom_sites.entry_id 5DLP _atom_sites.fract_transf_matrix[1][1] 0.009004 _atom_sites.fract_transf_matrix[1][2] 0.005199 _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] 0.010397 _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] 0.007290 _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 . SER A 1 4 ? -82.872 32.756 -10.726 1.00 92.21 ? 4 SER A N 1 ATOM 2 C CA . SER A 1 4 ? -82.785 33.363 -9.373 1.00 92.07 ? 4 SER A CA 1 ATOM 3 C C . SER A 1 4 ? -81.340 33.736 -9.044 1.00 88.81 ? 4 SER A C 1 ATOM 4 O O . SER A 1 4 ? -80.413 32.948 -9.241 1.00 86.94 ? 4 SER A O 1 ATOM 5 C CB . SER A 1 4 ? -83.338 32.406 -8.308 1.00 93.07 ? 4 SER A CB 1 ATOM 6 O OG . SER A 1 4 ? -83.003 32.841 -6.995 1.00 90.73 ? 4 SER A OG 1 ATOM 7 N N . GLU A 1 5 ? -81.178 34.939 -8.503 1.00 86.36 ? 5 GLU A N 1 ATOM 8 C CA . GLU A 1 5 ? -79.877 35.528 -8.206 1.00 81.16 ? 5 GLU A CA 1 ATOM 9 C C . GLU A 1 5 ? -79.103 34.734 -7.156 1.00 77.11 ? 5 GLU A C 1 ATOM 10 O O . GLU A 1 5 ? -77.875 34.825 -7.073 1.00 73.81 ? 5 GLU A O 1 ATOM 11 C CB . GLU A 1 5 ? -80.101 36.950 -7.701 1.00 82.51 ? 5 GLU A CB 1 ATOM 12 C CG . GLU A 1 5 ? -78.944 37.896 -7.915 1.00 82.98 ? 5 GLU A CG 1 ATOM 13 C CD . GLU A 1 5 ? -79.252 39.292 -7.412 1.00 85.24 ? 5 GLU A CD 1 ATOM 14 O OE1 . GLU A 1 5 ? -80.440 39.681 -7.398 1.00 88.61 ? 5 GLU A OE1 1 ATOM 15 O OE2 . GLU A 1 5 ? -78.302 40.003 -7.031 1.00 87.04 ? 5 GLU A OE2 1 ATOM 16 N N . LEU A 1 6 ? -79.833 33.968 -6.346 1.00 76.12 ? 6 LEU A N 1 ATOM 17 C CA . LEU A 1 6 ? -79.246 33.188 -5.260 1.00 72.42 ? 6 LEU A CA 1 ATOM 18 C C . LEU A 1 6 ? -78.935 31.746 -5.663 1.00 70.64 ? 6 LEU A C 1 ATOM 19 O O . LEU A 1 6 ? -78.575 30.942 -4.810 1.00 69.37 ? 6 LEU A O 1 ATOM 20 C CB . LEU A 1 6 ? -80.192 33.187 -4.049 1.00 73.43 ? 6 LEU A CB 1 ATOM 21 C CG . LEU A 1 6 ? -80.747 34.537 -3.569 1.00 73.39 ? 6 LEU A CG 1 ATOM 22 C CD1 . LEU A 1 6 ? -81.728 34.332 -2.423 1.00 72.67 ? 6 LEU A CD1 1 ATOM 23 C CD2 . LEU A 1 6 ? -79.622 35.485 -3.163 1.00 71.36 ? 6 LEU A CD2 1 ATOM 24 N N . LEU A 1 7 ? -79.073 31.416 -6.948 1.00 70.83 ? 7 LEU A N 1 ATOM 25 C CA . LEU A 1 7 ? -78.738 30.080 -7.446 1.00 69.74 ? 7 LEU A CA 1 ATOM 26 C C . LEU A 1 7 ? -77.538 30.161 -8.386 1.00 66.88 ? 7 LEU A C 1 ATOM 27 O O . LEU A 1 7 ? -77.571 30.907 -9.351 1.00 67.74 ? 7 LEU A O 1 ATOM 28 C CB . LEU A 1 7 ? -79.941 29.481 -8.165 1.00 73.10 ? 7 LEU A CB 1 ATOM 29 C CG . LEU A 1 7 ? -79.735 28.148 -8.881 1.00 74.03 ? 7 LEU A CG 1 ATOM 30 C CD1 . LEU A 1 7 ? -79.101 27.121 -7.957 1.00 72.77 ? 7 LEU A CD1 1 ATOM 31 C CD2 . LEU A 1 7 ? -81.072 27.654 -9.416 1.00 77.11 ? 7 LEU A CD2 1 ATOM 32 N N . VAL A 1 8 ? -76.480 29.406 -8.091 1.00 64.25 ? 8 VAL A N 1 ATOM 33 C CA . VAL A 1 8 ? -75.232 29.467 -8.863 1.00 62.56 ? 8 VAL A CA 1 ATOM 34 C C . VAL A 1 8 ? -74.700 28.076 -9.199 1.00 62.06 ? 8 VAL A C 1 ATOM 35 O O . VAL A 1 8 ? -74.484 27.258 -8.305 1.00 60.70 ? 8 VAL A O 1 ATOM 36 C CB . VAL A 1 8 ? -74.127 30.204 -8.083 1.00 60.29 ? 8 VAL A CB 1 ATOM 37 C CG1 . VAL A 1 8 ? -72.821 30.212 -8.870 1.00 59.24 ? 8 VAL A CG1 1 ATOM 38 C CG2 . VAL A 1 8 ? -74.546 31.626 -7.754 1.00 60.59 ? 8 VAL A CG2 1 ATOM 39 N N . ASN A 1 9 ? -74.470 27.816 -10.482 1.00 63.38 ? 9 ASN A N 1 ATOM 40 C CA . ASN A 1 9 ? -73.844 26.562 -10.908 1.00 64.12 ? 9 ASN A CA 1 ATOM 41 C C . ASN A 1 9 ? -72.330 26.676 -10.887 1.00 62.04 ? 9 ASN A C 1 ATOM 42 O O . ASN A 1 9 ? -71.748 27.468 -11.627 1.00 62.44 ? 9 ASN A O 1 ATOM 43 C CB . ASN A 1 9 ? -74.297 26.165 -12.310 1.00 66.14 ? 9 ASN A CB 1 ATOM 44 C CG . ASN A 1 9 ? -75.734 25.706 -12.345 1.00 69.27 ? 9 ASN A CG 1 ATOM 45 O OD1 . ASN A 1 9 ? -76.166 24.921 -11.504 1.00 70.47 ? 9 ASN A OD1 1 ATOM 46 N ND2 . ASN A 1 9 ? -76.485 26.190 -13.323 1.00 72.21 ? 9 ASN A ND2 1 ATOM 47 N N . THR A 1 10 ? -71.697 25.890 -10.030 1.00 60.20 ? 10 THR A N 1 ATOM 48 C CA . THR A 1 10 ? -70.257 25.824 -9.989 1.00 59.37 ? 10 THR A CA 1 ATOM 49 C C . THR A 1 10 ? -69.865 24.477 -10.555 1.00 60.07 ? 10 THR A C 1 ATOM 50 O O . THR A 1 10 ? -70.696 23.574 -10.636 1.00 61.56 ? 10 THR A O 1 ATOM 51 C CB . THR A 1 10 ? -69.724 25.955 -8.548 1.00 58.00 ? 10 THR A CB 1 ATOM 52 O OG1 . THR A 1 10 ? -69.939 24.730 -7.836 1.00 59.37 ? 10 THR A OG1 1 ATOM 53 C CG2 . THR A 1 10 ? -70.417 27.100 -7.810 1.00 57.52 ? 10 THR A CG2 1 ATOM 54 N N . LYS A 1 11 ? -68.593 24.336 -10.914 1.00 59.09 ? 11 LYS A N 1 ATOM 55 C CA . LYS A 1 11 ? -68.042 23.048 -11.340 1.00 58.55 ? 11 LYS A CA 1 ATOM 56 C C . LYS A 1 11 ? -68.261 21.914 -10.310 1.00 57.26 ? 11 LYS A C 1 ATOM 57 O O . LYS A 1 11 ? -68.164 20.751 -10.663 1.00 56.99 ? 11 LYS A O 1 ATOM 58 C CB . LYS A 1 11 ? -66.544 23.191 -11.642 1.00 58.52 ? 11 LYS A CB 1 ATOM 59 C CG . LYS A 1 11 ? -66.193 24.116 -12.811 1.00 60.03 ? 11 LYS A CG 1 ATOM 60 C CD . LYS A 1 11 ? -64.746 24.589 -12.697 1.00 60.25 ? 11 LYS A CD 1 ATOM 61 C CE . LYS A 1 11 ? -64.193 25.188 -13.984 1.00 61.63 ? 11 LYS A CE 1 ATOM 62 N NZ . LYS A 1 11 ? -64.338 26.667 -14.040 1.00 61.84 ? 11 LYS A NZ 1 ATOM 63 N N . SER A 1 12 ? -68.540 22.246 -9.047 1.00 56.14 ? 12 SER A N 1 ATOM 64 C CA . SER A 1 12 ? -68.830 21.230 -8.022 1.00 56.12 ? 12 SER A CA 1 ATOM 65 C C . SER A 1 12 ? -70.320 20.875 -7.903 1.00 56.88 ? 12 SER A C 1 ATOM 66 O O . SER A 1 12 ? -70.674 19.895 -7.243 1.00 54.94 ? 12 SER A O 1 ATOM 67 C CB . SER A 1 12 ? -68.331 21.698 -6.656 1.00 54.99 ? 12 SER A CB 1 ATOM 68 O OG . SER A 1 12 ? -66.968 22.067 -6.688 1.00 54.68 ? 12 SER A OG 1 ATOM 69 N N . GLY A 1 13 ? -71.175 21.677 -8.537 1.00 58.12 ? 13 GLY A N 1 ATOM 70 C CA . GLY A 1 13 ? -72.628 21.548 -8.422 1.00 60.23 ? 13 GLY A CA 1 ATOM 71 C C . GLY A 1 13 ? -73.304 22.890 -8.155 1.00 60.50 ? 13 GLY A C 1 ATOM 72 O O . GLY A 1 13 ? -72.637 23.916 -7.980 1.00 58.09 ? 13 GLY A O 1 ATOM 73 N N . LYS A 1 14 ? -74.638 22.881 -8.134 1.00 61.95 ? 14 LYS A N 1 ATOM 74 C CA . LYS A 1 14 ? -75.421 24.081 -7.841 1.00 61.50 ? 14 LYS A CA 1 ATOM 75 C C . LYS A 1 14 ? -75.353 24.407 -6.341 1.00 60.09 ? 14 LYS A C 1 ATOM 76 O O . LYS A 1 14 ? -75.306 23.497 -5.512 1.00 59.70 ? 14 LYS A O 1 ATOM 77 C CB . LYS A 1 14 ? -76.881 23.879 -8.280 1.00 62.97 ? 14 LYS A CB 1 ATOM 78 N N . VAL A 1 15 ? -75.334 25.697 -5.998 1.00 58.97 ? 15 VAL A N 1 ATOM 79 C CA . VAL A 1 15 ? -75.478 26.132 -4.603 1.00 58.75 ? 15 VAL A CA 1 ATOM 80 C C . VAL A 1 15 ? -76.577 27.175 -4.475 1.00 61.10 ? 15 VAL A C 1 ATOM 81 O O . VAL A 1 15 ? -76.739 28.014 -5.361 1.00 62.24 ? 15 VAL A O 1 ATOM 82 C CB . VAL A 1 15 ? -74.181 26.730 -4.012 1.00 56.35 ? 15 VAL A CB 1 ATOM 83 C CG1 . VAL A 1 15 ? -73.051 25.723 -4.055 1.00 55.25 ? 15 VAL A CG1 1 ATOM 84 C CG2 . VAL A 1 15 ? -73.777 28.011 -4.723 1.00 56.29 ? 15 VAL A CG2 1 ATOM 85 N N . MET A 1 16 ? -77.319 27.125 -3.366 1.00 62.72 ? 16 MET A N 1 ATOM 86 C CA . MET A 1 16 ? -78.366 28.108 -3.080 1.00 64.79 ? 16 MET A CA 1 ATOM 87 C C . MET A 1 16 ? -77.977 28.939 -1.874 1.00 62.29 ? 16 MET A C 1 ATOM 88 O O . MET A 1 16 ? -77.866 28.419 -0.762 1.00 60.90 ? 16 MET A O 1 ATOM 89 C CB . MET A 1 16 ? -79.713 27.427 -2.816 1.00 68.79 ? 16 MET A CB 1 ATOM 90 C CG . MET A 1 16 ? -80.880 28.377 -2.549 1.00 71.86 ? 16 MET A CG 1 ATOM 91 S SD . MET A 1 16 ? -81.429 29.245 -4.033 1.00 76.29 ? 16 MET A SD 1 ATOM 92 C CE . MET A 1 16 ? -82.574 28.043 -4.732 1.00 77.76 ? 16 MET A CE 1 ATOM 93 N N . GLY A 1 17 ? -77.789 30.235 -2.107 1.00 61.61 ? 17 GLY A N 1 ATOM 94 C CA . GLY A 1 17 ? -77.478 31.192 -1.049 1.00 60.60 ? 17 GLY A CA 1 ATOM 95 C C . GLY A 1 17 ? -78.704 31.905 -0.515 1.00 61.56 ? 17 GLY A C 1 ATOM 96 O O . GLY A 1 17 ? -79.834 31.464 -0.738 1.00 62.89 ? 17 GLY A O 1 ATOM 97 N N . THR A 1 18 ? -78.465 33.016 0.182 1.00 61.07 ? 18 THR A N 1 ATOM 98 C CA . THR A 1 18 ? -79.512 33.765 0.878 1.00 63.07 ? 18 THR A CA 1 ATOM 99 C C . THR A 1 18 ? -79.321 35.268 0.709 1.00 64.47 ? 18 THR A C 1 ATOM 100 O O . THR A 1 18 ? -78.189 35.754 0.644 1.00 63.76 ? 18 THR A O 1 ATOM 101 C CB . THR A 1 18 ? -79.562 33.413 2.389 1.00 62.47 ? 18 THR A CB 1 ATOM 102 O OG1 . THR A 1 18 ? -80.613 34.151 3.027 1.00 64.62 ? 18 THR A OG1 1 ATOM 103 C CG2 . THR A 1 18 ? -78.236 33.722 3.096 1.00 59.92 ? 18 THR A CG2 1 ATOM 104 N N . ARG A 1 19 ? -80.439 35.991 0.636 1.00 68.32 ? 19 ARG A N 1 ATOM 105 C CA . ARG A 1 19 ? -80.435 37.450 0.598 1.00 70.28 ? 19 ARG A CA 1 ATOM 106 C C . ARG A 1 19 ? -80.256 37.936 2.029 1.00 70.34 ? 19 ARG A C 1 ATOM 107 O O . ARG A 1 19 ? -81.059 37.588 2.900 1.00 71.58 ? 19 ARG A O 1 ATOM 108 C CB . ARG A 1 19 ? -81.761 37.973 0.035 1.00 74.42 ? 19 ARG A CB 1 ATOM 109 C CG . ARG A 1 19 ? -81.681 39.331 -0.652 1.00 76.65 ? 19 ARG A CG 1 ATOM 110 C CD . ARG A 1 19 ? -83.025 40.054 -0.597 1.00 79.91 ? 19 ARG A CD 1 ATOM 111 N NE . ARG A 1 19 ? -83.180 41.068 -1.645 1.00 82.41 ? 19 ARG A NE 1 ATOM 112 C CZ . ARG A 1 19 ? -84.089 42.048 -1.631 1.00 85.10 ? 19 ARG A CZ 1 ATOM 113 N NH1 . ARG A 1 19 ? -84.929 42.180 -0.610 1.00 86.31 ? 19 ARG A NH1 1 ATOM 114 N NH2 . ARG A 1 19 ? -84.151 42.916 -2.637 1.00 85.46 ? 19 ARG A NH2 1 ATOM 115 N N . VAL A 1 20 ? -79.198 38.706 2.281 1.00 68.80 ? 20 VAL A N 1 ATOM 116 C CA . VAL A 1 20 ? -78.952 39.260 3.621 1.00 68.68 ? 20 VAL A CA 1 ATOM 117 C C . VAL A 1 20 ? -79.035 40.783 3.595 1.00 69.62 ? 20 VAL A C 1 ATOM 118 O O . VAL A 1 20 ? -78.609 41.407 2.625 1.00 70.47 ? 20 VAL A O 1 ATOM 119 C CB . VAL A 1 20 ? -77.582 38.842 4.206 1.00 65.68 ? 20 VAL A CB 1 ATOM 120 C CG1 . VAL A 1 20 ? -77.455 37.329 4.232 1.00 65.05 ? 20 VAL A CG1 1 ATOM 121 C CG2 . VAL A 1 20 ? -76.430 39.466 3.431 1.00 64.94 ? 20 VAL A CG2 1 ATOM 122 N N . PRO A 1 21 ? -79.591 41.385 4.662 1.00 69.69 ? 21 PRO A N 1 ATOM 123 C CA . PRO A 1 21 ? -79.636 42.838 4.726 1.00 70.22 ? 21 PRO A CA 1 ATOM 124 C C . PRO A 1 21 ? -78.276 43.437 5.088 1.00 68.75 ? 21 PRO A C 1 ATOM 125 O O . PRO A 1 21 ? -77.438 42.772 5.702 1.00 65.97 ? 21 PRO A O 1 ATOM 126 C CB . PRO A 1 21 ? -80.667 43.105 5.820 1.00 71.27 ? 21 PRO A CB 1 ATOM 127 C CG . PRO A 1 21 ? -80.549 41.932 6.726 1.00 70.21 ? 21 PRO A CG 1 ATOM 128 C CD . PRO A 1 21 ? -80.216 40.763 5.845 1.00 69.50 ? 21 PRO A CD 1 ATOM 129 N N . VAL A 1 22 ? -78.071 44.688 4.693 1.00 69.98 ? 22 VAL A N 1 ATOM 130 C CA . VAL A 1 22 ? -76.840 45.403 4.983 1.00 69.48 ? 22 VAL A CA 1 ATOM 131 C C . VAL A 1 22 ? -77.079 46.900 4.790 1.00 71.98 ? 22 VAL A C 1 ATOM 132 O O . VAL A 1 22 ? -77.571 47.323 3.741 1.00 72.68 ? 22 VAL A O 1 ATOM 133 C CB . VAL A 1 22 ? -75.669 44.896 4.101 1.00 68.40 ? 22 VAL A CB 1 ATOM 134 C CG1 . VAL A 1 22 ? -76.010 44.961 2.617 1.00 69.51 ? 22 VAL A CG1 1 ATOM 135 C CG2 . VAL A 1 22 ? -74.392 45.672 4.396 1.00 68.00 ? 22 VAL A CG2 1 ATOM 136 N N . LEU A 1 23 ? -76.756 47.686 5.817 1.00 72.86 ? 23 LEU A N 1 ATOM 137 C CA . LEU A 1 23 ? -76.949 49.142 5.800 1.00 75.50 ? 23 LEU A CA 1 ATOM 138 C C . LEU A 1 23 ? -78.223 49.555 5.047 1.00 78.68 ? 23 LEU A C 1 ATOM 139 O O . LEU A 1 23 ? -78.189 50.417 4.158 1.00 78.13 ? 23 LEU A O 1 ATOM 140 C CB . LEU A 1 23 ? -75.712 49.828 5.206 1.00 75.31 ? 23 LEU A CB 1 ATOM 141 C CG . LEU A 1 23 ? -74.382 49.496 5.904 1.00 73.42 ? 23 LEU A CG 1 ATOM 142 C CD1 . LEU A 1 23 ? -73.186 49.966 5.085 1.00 72.19 ? 23 LEU A CD1 1 ATOM 143 C CD2 . LEU A 1 23 ? -74.338 50.095 7.304 1.00 73.34 ? 23 LEU A CD2 1 ATOM 144 N N . SER A 1 24 ? -79.338 48.925 5.426 1.00 81.29 ? 24 SER A N 1 ATOM 145 C CA . SER A 1 24 ? -80.660 49.139 4.799 1.00 84.91 ? 24 SER A CA 1 ATOM 146 C C . SER A 1 24 ? -80.623 48.981 3.272 1.00 83.50 ? 24 SER A C 1 ATOM 147 O O . SER A 1 24 ? -81.073 49.833 2.513 1.00 84.18 ? 24 SER A O 1 ATOM 148 C CB . SER A 1 24 ? -81.261 50.487 5.217 1.00 88.38 ? 24 SER A CB 1 ATOM 149 O OG . SER A 1 24 ? -80.345 51.544 5.000 1.00 89.58 ? 24 SER A OG 1 ATOM 150 N N . SER A 1 25 ? -80.056 47.862 2.853 1.00 81.12 ? 25 SER A N 1 ATOM 151 C CA . SER A 1 25 ? -80.050 47.430 1.469 1.00 79.59 ? 25 SER A CA 1 ATOM 152 C C . SER A 1 25 ? -79.834 45.931 1.570 1.00 78.05 ? 25 SER A C 1 ATOM 153 O O . SER A 1 25 ? -79.882 45.382 2.672 1.00 76.72 ? 25 SER A O 1 ATOM 154 C CB . SER A 1 25 ? -78.928 48.109 0.687 1.00 78.03 ? 25 SER A CB 1 ATOM 155 O OG . SER A 1 25 ? -78.888 47.659 -0.657 1.00 77.60 ? 25 SER A OG 1 ATOM 156 N N . HIS A 1 26 ? -79.607 45.258 0.450 1.00 77.78 ? 26 HIS A N 1 ATOM 157 C CA . HIS A 1 26 ? -79.448 43.812 0.478 1.00 77.53 ? 26 HIS A CA 1 ATOM 158 C C . HIS A 1 26 ? -78.388 43.362 -0.518 1.00 74.28 ? 26 HIS A C 1 ATOM 159 O O . HIS A 1 26 ? -78.137 44.037 -1.520 1.00 76.01 ? 26 HIS A O 1 ATOM 160 C CB . HIS A 1 26 ? -80.780 43.112 0.173 1.00 82.73 ? 26 HIS A CB 1 ATOM 161 C CG . HIS A 1 26 ? -81.950 43.657 0.943 1.00 89.23 ? 26 HIS A CG 1 ATOM 162 N ND1 . HIS A 1 26 ? -82.223 43.292 2.247 1.00 90.67 ? 26 HIS A ND1 1 ATOM 163 C CD2 . HIS A 1 26 ? -82.919 44.537 0.590 1.00 92.99 ? 26 HIS A CD2 1 ATOM 164 C CE1 . HIS A 1 26 ? -83.306 43.925 2.663 1.00 92.61 ? 26 HIS A CE1 1 ATOM 165 N NE2 . HIS A 1 26 ? -83.747 44.686 1.677 1.00 95.93 ? 26 HIS A NE2 1 ATOM 166 N N . ILE A 1 27 ? -77.762 42.228 -0.213 1.00 68.97 ? 27 ILE A N 1 ATOM 167 C CA . ILE A 1 27 ? -76.876 41.537 -1.137 1.00 66.33 ? 27 ILE A CA 1 ATOM 168 C C . ILE A 1 27 ? -77.014 40.020 -0.966 1.00 64.91 ? 27 ILE A C 1 ATOM 169 O O . ILE A 1 27 ? -77.700 39.538 -0.063 1.00 64.98 ? 27 ILE A O 1 ATOM 170 C CB . ILE A 1 27 ? -75.405 41.971 -0.968 1.00 64.73 ? 27 ILE A CB 1 ATOM 171 C CG1 . ILE A 1 27 ? -74.931 41.758 0.469 1.00 63.61 ? 27 ILE A CG1 1 ATOM 172 C CG2 . ILE A 1 27 ? -75.227 43.429 -1.377 1.00 65.72 ? 27 ILE A CG2 1 ATOM 173 C CD1 . ILE A 1 27 ? -73.480 42.126 0.673 1.00 62.33 ? 27 ILE A CD1 1 ATOM 174 N N . SER A 1 28 ? -76.375 39.274 -1.858 1.00 63.63 ? 28 SER A N 1 ATOM 175 C CA . SER A 1 28 ? -76.450 37.824 -1.841 1.00 62.43 ? 28 SER A CA 1 ATOM 176 C C . SER A 1 28 ? -75.350 37.311 -0.928 1.00 59.50 ? 28 SER A C 1 ATOM 177 O O . SER A 1 28 ? -74.306 37.947 -0.796 1.00 58.52 ? 28 SER A O 1 ATOM 178 C CB . SER A 1 28 ? -76.283 37.261 -3.259 1.00 63.37 ? 28 SER A CB 1 ATOM 179 O OG . SER A 1 28 ? -77.030 38.003 -4.223 1.00 66.10 ? 28 SER A OG 1 ATOM 180 N N . ALA A 1 29 ? -75.588 36.175 -0.282 1.00 58.37 ? 29 ALA A N 1 ATOM 181 C CA . ALA A 1 29 ? -74.567 35.537 0.550 1.00 55.84 ? 29 ALA A CA 1 ATOM 182 C C . ALA A 1 29 ? -74.628 34.037 0.367 1.00 54.85 ? 29 ALA A C 1 ATOM 183 O O . ALA A 1 29 ? -75.709 33.451 0.359 1.00 57.00 ? 29 ALA A O 1 ATOM 184 C CB . ALA A 1 29 ? -74.767 35.887 2.015 1.00 56.09 ? 29 ALA A CB 1 ATOM 185 N N . PHE A 1 30 ? -73.463 33.422 0.218 1.00 51.71 ? 30 PHE A N 1 ATOM 186 C CA . PHE A 1 30 ? -73.362 31.976 0.080 1.00 50.80 ? 30 PHE A CA 1 ATOM 187 C C . PHE A 1 30 ? -72.439 31.510 1.175 1.00 49.34 ? 30 PHE A C 1 ATOM 188 O O . PHE A 1 30 ? -71.241 31.736 1.118 1.00 48.67 ? 30 PHE A O 1 ATOM 189 C CB . PHE A 1 30 ? -72.805 31.592 -1.295 1.00 49.60 ? 30 PHE A CB 1 ATOM 190 C CG . PHE A 1 30 ? -73.600 32.142 -2.436 1.00 49.32 ? 30 PHE A CG 1 ATOM 191 C CD1 . PHE A 1 30 ? -73.437 33.461 -2.831 1.00 48.69 ? 30 PHE A CD1 1 ATOM 192 C CD2 . PHE A 1 30 ? -74.514 31.351 -3.102 1.00 50.11 ? 30 PHE A CD2 1 ATOM 193 C CE1 . PHE A 1 30 ? -74.173 33.984 -3.868 1.00 50.03 ? 30 PHE A CE1 1 ATOM 194 C CE2 . PHE A 1 30 ? -75.249 31.862 -4.150 1.00 51.95 ? 30 PHE A CE2 1 ATOM 195 C CZ . PHE A 1 30 ? -75.081 33.182 -4.532 1.00 51.87 ? 30 PHE A CZ 1 ATOM 196 N N . LEU A 1 31 ? -73.017 30.871 2.177 1.00 50.69 ? 31 LEU A N 1 ATOM 197 C CA . LEU A 1 31 ? -72.312 30.532 3.392 1.00 49.50 ? 31 LEU A CA 1 ATOM 198 C C . LEU A 1 31 ? -72.179 29.021 3.498 1.00 50.00 ? 31 LEU A C 1 ATOM 199 O O . LEU A 1 31 ? -73.144 28.291 3.286 1.00 51.52 ? 31 LEU A O 1 ATOM 200 C CB . LEU A 1 31 ? -73.107 31.053 4.589 1.00 50.40 ? 31 LEU A CB 1 ATOM 201 C CG . LEU A 1 31 ? -73.599 32.500 4.537 1.00 50.61 ? 31 LEU A CG 1 ATOM 202 C CD1 . LEU A 1 31 ? -74.542 32.765 5.698 1.00 51.52 ? 31 LEU A CD1 1 ATOM 203 C CD2 . LEU A 1 31 ? -72.424 33.457 4.563 1.00 48.94 ? 31 LEU A CD2 1 ATOM 204 N N . GLY A 1 32 ? -70.982 28.558 3.838 1.00 49.41 ? 32 GLY A N 1 ATOM 205 C CA . GLY A 1 32 ? -70.761 27.145 4.157 1.00 49.13 ? 32 GLY A CA 1 ATOM 206 C C . GLY A 1 32 ? -70.675 26.250 2.945 1.00 48.97 ? 32 GLY A C 1 ATOM 207 O O . GLY A 1 32 ? -71.213 25.148 2.961 1.00 49.70 ? 32 GLY A O 1 ATOM 208 N N . ILE A 1 33 ? -69.995 26.734 1.903 1.00 48.89 ? 33 ILE A N 1 ATOM 209 C CA . ILE A 1 33 ? -69.744 25.971 0.674 1.00 49.33 ? 33 ILE A CA 1 ATOM 210 C C . ILE A 1 33 ? -68.513 25.110 0.888 1.00 48.72 ? 33 ILE A C 1 ATOM 211 O O . ILE A 1 33 ? -67.490 25.625 1.332 1.00 49.27 ? 33 ILE A O 1 ATOM 212 C CB . ILE A 1 33 ? -69.417 26.884 -0.515 1.00 48.59 ? 33 ILE A CB 1 ATOM 213 C CG1 . ILE A 1 33 ? -70.558 27.861 -0.788 1.00 49.77 ? 33 ILE A CG1 1 ATOM 214 C CG2 . ILE A 1 33 ? -69.132 26.047 -1.754 1.00 49.59 ? 33 ILE A CG2 1 ATOM 215 C CD1 . ILE A 1 33 ? -70.216 28.910 -1.828 1.00 50.23 ? 33 ILE A CD1 1 ATOM 216 N N . PRO A 1 34 ? -68.590 23.807 0.569 1.00 48.84 ? 34 PRO A N 1 ATOM 217 C CA . PRO A 1 34 ? -67.448 22.929 0.819 1.00 48.56 ? 34 PRO A CA 1 ATOM 218 C C . PRO A 1 34 ? -66.416 22.961 -0.309 1.00 47.77 ? 34 PRO A C 1 ATOM 219 O O . PRO A 1 34 ? -66.783 22.824 -1.467 1.00 48.11 ? 34 PRO A O 1 ATOM 220 C CB . PRO A 1 34 ? -68.094 21.546 0.923 1.00 49.98 ? 34 PRO A CB 1 ATOM 221 C CG . PRO A 1 34 ? -69.291 21.633 0.044 1.00 51.44 ? 34 PRO A CG 1 ATOM 222 C CD . PRO A 1 34 ? -69.771 23.055 0.119 1.00 50.67 ? 34 PRO A CD 1 ATOM 223 N N . PHE A 1 35 ? -65.141 23.150 0.031 1.00 46.67 ? 35 PHE A N 1 ATOM 224 C CA . PHE A 1 35 ? -64.071 23.158 -0.966 1.00 46.52 ? 35 PHE A CA 1 ATOM 225 C C . PHE A 1 35 ? -63.180 21.931 -0.874 1.00 45.98 ? 35 PHE A C 1 ATOM 226 O O . PHE A 1 35 ? -62.292 21.741 -1.709 1.00 46.38 ? 35 PHE A O 1 ATOM 227 C CB . PHE A 1 35 ? -63.241 24.441 -0.877 1.00 46.55 ? 35 PHE A CB 1 ATOM 228 C CG . PHE A 1 35 ? -62.495 24.618 0.421 1.00 46.72 ? 35 PHE A CG 1 ATOM 229 C CD1 . PHE A 1 35 ? -61.250 24.041 0.606 1.00 46.89 ? 35 PHE A CD1 1 ATOM 230 C CD2 . PHE A 1 35 ? -63.017 25.411 1.443 1.00 47.59 ? 35 PHE A CD2 1 ATOM 231 C CE1 . PHE A 1 35 ? -60.550 24.225 1.790 1.00 46.43 ? 35 PHE A CE1 1 ATOM 232 C CE2 . PHE A 1 35 ? -62.324 25.592 2.637 1.00 46.06 ? 35 PHE A CE2 1 ATOM 233 C CZ . PHE A 1 35 ? -61.089 25.003 2.807 1.00 45.92 ? 35 PHE A CZ 1 ATOM 234 N N . ALA A 1 36 ? -63.433 21.090 0.123 1.00 45.67 ? 36 ALA A N 1 ATOM 235 C CA . ALA A 1 36 ? -62.681 19.861 0.302 1.00 46.20 ? 36 ALA A CA 1 ATOM 236 C C . ALA A 1 36 ? -63.538 18.789 0.928 1.00 48.60 ? 36 ALA A C 1 ATOM 237 O O . ALA A 1 36 ? -64.606 19.063 1.469 1.00 51.70 ? 36 ALA A O 1 ATOM 238 C CB . ALA A 1 36 ? -61.474 20.118 1.176 1.00 44.78 ? 36 ALA A CB 1 ATOM 239 N N . GLU A 1 37 ? -63.060 17.557 0.862 1.00 50.55 ? 37 GLU A N 1 ATOM 240 C CA . GLU A 1 37 ? -63.671 16.481 1.618 1.00 51.88 ? 37 GLU A CA 1 ATOM 241 C C . GLU A 1 37 ? -63.454 16.736 3.108 1.00 50.72 ? 37 GLU A C 1 ATOM 242 O O . GLU A 1 37 ? -62.444 17.317 3.488 1.00 49.76 ? 37 GLU A O 1 ATOM 243 C CB . GLU A 1 37 ? -63.071 15.139 1.212 1.00 53.13 ? 37 GLU A CB 1 ATOM 244 C CG . GLU A 1 37 ? -63.516 14.681 -0.166 1.00 55.30 ? 37 GLU A CG 1 ATOM 245 C CD . GLU A 1 37 ? -65.002 14.375 -0.237 1.00 56.83 ? 37 GLU A CD 1 ATOM 246 O OE1 . GLU A 1 37 ? -65.477 13.558 0.577 1.00 57.24 ? 37 GLU A OE1 1 ATOM 247 O OE2 . GLU A 1 37 ? -65.691 14.953 -1.107 1.00 57.08 ? 37 GLU A OE2 1 ATOM 248 N N . PRO A 1 38 ? -64.414 16.326 3.956 1.00 51.94 ? 38 PRO A N 1 ATOM 249 C CA . PRO A 1 38 ? -64.181 16.442 5.391 1.00 51.37 ? 38 PRO A CA 1 ATOM 250 C C . PRO A 1 38 ? -62.981 15.594 5.804 1.00 51.68 ? 38 PRO A C 1 ATOM 251 O O . PRO A 1 38 ? -62.987 14.388 5.563 1.00 55.85 ? 38 PRO A O 1 ATOM 252 C CB . PRO A 1 38 ? -65.468 15.880 6.014 1.00 52.71 ? 38 PRO A CB 1 ATOM 253 C CG . PRO A 1 38 ? -66.494 15.947 4.938 1.00 53.66 ? 38 PRO A CG 1 ATOM 254 C CD . PRO A 1 38 ? -65.746 15.771 3.654 1.00 53.39 ? 38 PRO A CD 1 ATOM 255 N N . PRO A 1 39 ? -61.957 16.215 6.413 1.00 49.76 ? 39 PRO A N 1 ATOM 256 C CA . PRO A 1 39 ? -60.754 15.487 6.784 1.00 49.31 ? 39 PRO A CA 1 ATOM 257 C C . PRO A 1 39 ? -60.941 14.737 8.100 1.00 49.08 ? 39 PRO A C 1 ATOM 258 O O . PRO A 1 39 ? -60.406 15.135 9.132 1.00 47.19 ? 39 PRO A O 1 ATOM 259 C CB . PRO A 1 39 ? -59.717 16.602 6.910 1.00 48.40 ? 39 PRO A CB 1 ATOM 260 C CG . PRO A 1 39 ? -60.506 17.772 7.396 1.00 48.06 ? 39 PRO A CG 1 ATOM 261 C CD . PRO A 1 39 ? -61.892 17.627 6.836 1.00 48.64 ? 39 PRO A CD 1 ATOM 262 N N . VAL A 1 40 ? -61.686 13.641 8.038 1.00 50.36 ? 40 VAL A N 1 ATOM 263 C CA . VAL A 1 40 ? -62.086 12.903 9.229 1.00 51.85 ? 40 VAL A CA 1 ATOM 264 C C . VAL A 1 40 ? -61.544 11.485 9.233 1.00 53.10 ? 40 VAL A C 1 ATOM 265 O O . VAL A 1 40 ? -61.127 10.968 8.204 1.00 53.98 ? 40 VAL A O 1 ATOM 266 C CB . VAL A 1 40 ? -63.620 12.853 9.359 1.00 53.06 ? 40 VAL A CB 1 ATOM 267 C CG1 . VAL A 1 40 ? -64.160 14.243 9.665 1.00 52.15 ? 40 VAL A CG1 1 ATOM 268 C CG2 . VAL A 1 40 ? -64.259 12.281 8.098 1.00 53.55 ? 40 VAL A CG2 1 ATOM 269 N N . GLY A 1 41 ? -61.571 10.871 10.410 1.00 55.19 ? 41 GLY A N 1 ATOM 270 C CA . GLY A 1 41 ? -61.108 9.509 10.614 1.00 58.25 ? 41 GLY A CA 1 ATOM 271 C C . GLY A 1 41 ? -59.657 9.340 10.222 1.00 60.34 ? 41 GLY A C 1 ATOM 272 O O . GLY A 1 41 ? -58.779 10.064 10.702 1.00 61.43 ? 41 GLY A O 1 ATOM 273 N N . ASN A 1 42 ? -59.416 8.395 9.319 1.00 63.85 ? 42 ASN A N 1 ATOM 274 C CA . ASN A 1 42 ? -58.077 8.129 8.798 1.00 65.05 ? 42 ASN A CA 1 ATOM 275 C C . ASN A 1 42 ? -57.509 9.268 7.939 1.00 62.10 ? 42 ASN A C 1 ATOM 276 O O . ASN A 1 42 ? -56.376 9.176 7.465 1.00 61.59 ? 42 ASN A O 1 ATOM 277 C CB . ASN A 1 42 ? -58.065 6.805 8.016 1.00 69.07 ? 42 ASN A CB 1 ATOM 278 C CG . ASN A 1 42 ? -59.088 6.778 6.884 1.00 72.42 ? 42 ASN A CG 1 ATOM 279 O OD1 . ASN A 1 42 ? -60.300 6.762 7.123 1.00 75.50 ? 42 ASN A OD1 1 ATOM 280 N ND2 . ASN A 1 42 ? -58.604 6.760 5.646 1.00 73.02 ? 42 ASN A ND2 1 ATOM 281 N N . MET A 1 43 ? -58.287 10.329 7.731 1.00 60.71 ? 43 MET A N 1 ATOM 282 C CA . MET A 1 43 ? -57.806 11.506 7.017 1.00 60.00 ? 43 MET A CA 1 ATOM 283 C C . MET A 1 43 ? -57.367 12.634 7.938 1.00 57.32 ? 43 MET A C 1 ATOM 284 O O . MET A 1 43 ? -56.868 13.660 7.465 1.00 55.56 ? 43 MET A O 1 ATOM 285 C CB . MET A 1 43 ? -58.870 12.010 6.053 1.00 62.43 ? 43 MET A CB 1 ATOM 286 C CG . MET A 1 43 ? -59.179 11.009 4.956 1.00 66.62 ? 43 MET A CG 1 ATOM 287 S SD . MET A 1 43 ? -59.586 11.834 3.412 1.00 72.36 ? 43 MET A SD 1 ATOM 288 C CE . MET A 1 43 ? -61.114 12.668 3.838 1.00 70.88 ? 43 MET A CE 1 ATOM 289 N N . ARG A 1 44 ? -57.541 12.460 9.246 1.00 56.05 ? 44 ARG A N 1 ATOM 290 C CA . ARG A 1 44 ? -57.021 13.438 10.192 1.00 52.73 ? 44 ARG A CA 1 ATOM 291 C C . ARG A 1 44 ? -55.512 13.503 9.994 1.00 50.31 ? 44 ARG A C 1 ATOM 292 O O . ARG A 1 44 ? -54.863 12.474 9.847 1.00 49.20 ? 44 ARG A O 1 ATOM 293 C CB . ARG A 1 44 ? -57.370 13.080 11.648 1.00 52.52 ? 44 ARG A CB 1 ATOM 294 C CG . ARG A 1 44 ? -56.964 14.163 12.644 1.00 49.70 ? 44 ARG A CG 1 ATOM 295 C CD . ARG A 1 44 ? -57.047 13.707 14.088 1.00 49.64 ? 44 ARG A CD 1 ATOM 296 N NE . ARG A 1 44 ? -58.419 13.661 14.583 1.00 49.62 ? 44 ARG A NE 1 ATOM 297 C CZ . ARG A 1 44 ? -58.784 13.131 15.751 1.00 49.66 ? 44 ARG A CZ 1 ATOM 298 N NH1 . ARG A 1 44 ? -57.890 12.588 16.569 1.00 49.70 ? 44 ARG A NH1 1 ATOM 299 N NH2 . ARG A 1 44 ? -60.059 13.134 16.102 1.00 50.37 ? 44 ARG A NH2 1 ATOM 300 N N . PHE A 1 45 ? -54.990 14.727 9.969 1.00 49.31 ? 45 PHE A N 1 ATOM 301 C CA . PHE A 1 45 ? -53.571 15.036 9.730 1.00 48.84 ? 45 PHE A CA 1 ATOM 302 C C . PHE A 1 45 ? -53.134 14.986 8.270 1.00 49.63 ? 45 PHE A C 1 ATOM 303 O O . PHE A 1 45 ? -52.088 15.549 7.929 1.00 51.62 ? 45 PHE A O 1 ATOM 304 C CB . PHE A 1 45 ? -52.623 14.184 10.578 1.00 49.26 ? 45 PHE A CB 1 ATOM 305 C CG . PHE A 1 45 ? -52.978 14.146 12.036 1.00 50.43 ? 45 PHE A CG 1 ATOM 306 C CD1 . PHE A 1 45 ? -53.139 15.319 12.753 1.00 50.16 ? 45 PHE A CD1 1 ATOM 307 C CD2 . PHE A 1 45 ? -53.132 12.931 12.697 1.00 52.16 ? 45 PHE A CD2 1 ATOM 308 C CE1 . PHE A 1 45 ? -53.466 15.283 14.098 1.00 50.97 ? 45 PHE A CE1 1 ATOM 309 C CE2 . PHE A 1 45 ? -53.448 12.887 14.041 1.00 52.82 ? 45 PHE A CE2 1 ATOM 310 C CZ . PHE A 1 45 ? -53.620 14.066 14.744 1.00 52.27 ? 45 PHE A CZ 1 ATOM 311 N N . ARG A 1 46 ? -53.918 14.342 7.411 1.00 52.01 ? 46 ARG A N 1 ATOM 312 C CA . ARG A 1 46 ? -53.561 14.213 5.996 1.00 53.20 ? 46 ARG A CA 1 ATOM 313 C C . ARG A 1 46 ? -53.802 15.504 5.205 1.00 50.23 ? 46 ARG A C 1 ATOM 314 O O . ARG A 1 46 ? -54.515 16.397 5.654 1.00 49.30 ? 46 ARG A O 1 ATOM 315 C CB . ARG A 1 46 ? -54.344 13.077 5.340 1.00 56.48 ? 46 ARG A CB 1 ATOM 316 C CG . ARG A 1 46 ? -53.976 11.686 5.829 1.00 60.02 ? 46 ARG A CG 1 ATOM 317 C CD . ARG A 1 46 ? -54.474 10.623 4.857 1.00 63.93 ? 46 ARG A CD 1 ATOM 318 N NE . ARG A 1 46 ? -53.943 10.868 3.514 1.00 66.46 ? 46 ARG A NE 1 ATOM 319 C CZ . ARG A 1 46 ? -52.932 10.210 2.938 1.00 69.19 ? 46 ARG A CZ 1 ATOM 320 N NH1 . ARG A 1 46 ? -52.307 9.200 3.543 1.00 71.04 ? 46 ARG A NH1 1 ATOM 321 N NH2 . ARG A 1 46 ? -52.553 10.559 1.716 1.00 68.91 ? 46 ARG A NH2 1 ATOM 322 N N . ARG A 1 47 ? -53.186 15.587 4.028 1.00 49.79 ? 47 ARG A N 1 ATOM 323 C CA . ARG A 1 47 ? -53.457 16.661 3.076 1.00 48.07 ? 47 ARG A CA 1 ATOM 324 C C . ARG A 1 47 ? -54.946 16.632 2.715 1.00 46.71 ? 47 ARG A C 1 ATOM 325 O O . ARG A 1 47 ? -55.566 15.581 2.723 1.00 46.36 ? 47 ARG A O 1 ATOM 326 C CB . ARG A 1 47 ? -52.584 16.496 1.814 1.00 47.16 ? 47 ARG A CB 1 ATOM 327 N N . PRO A 1 48 ? -55.534 17.790 2.420 1.00 45.56 ? 48 PRO A N 1 ATOM 328 C CA . PRO A 1 48 ? -56.937 17.773 2.040 1.00 46.60 ? 48 PRO A CA 1 ATOM 329 C C . PRO A 1 48 ? -57.152 17.217 0.628 1.00 48.52 ? 48 PRO A C 1 ATOM 330 O O . PRO A 1 48 ? -56.282 17.346 -0.224 1.00 48.54 ? 48 PRO A O 1 ATOM 331 C CB . PRO A 1 48 ? -57.319 19.251 2.089 1.00 44.89 ? 48 PRO A CB 1 ATOM 332 C CG . PRO A 1 48 ? -56.054 19.962 1.756 1.00 44.17 ? 48 PRO A CG 1 ATOM 333 C CD . PRO A 1 48 ? -54.975 19.153 2.416 1.00 44.66 ? 48 PRO A CD 1 ATOM 334 N N . GLU A 1 49 ? -58.306 16.607 0.399 1.00 51.20 ? 49 GLU A N 1 ATOM 335 C CA . GLU A 1 49 ? -58.714 16.186 -0.932 1.00 54.66 ? 49 GLU A CA 1 ATOM 336 C C . GLU A 1 49 ? -59.790 17.128 -1.458 1.00 53.19 ? 49 GLU A C 1 ATOM 337 O O . GLU A 1 49 ? -60.539 17.692 -0.672 1.00 52.49 ? 49 GLU A O 1 ATOM 338 C CB . GLU A 1 49 ? -59.287 14.777 -0.889 1.00 60.01 ? 49 GLU A CB 1 ATOM 339 C CG . GLU A 1 49 ? -58.322 13.709 -0.397 1.00 64.54 ? 49 GLU A CG 1 ATOM 340 C CD . GLU A 1 49 ? -58.968 12.331 -0.346 1.00 69.98 ? 49 GLU A CD 1 ATOM 341 O OE1 . GLU A 1 49 ? -60.150 12.198 -0.753 1.00 72.65 ? 49 GLU A OE1 1 ATOM 342 O OE2 . GLU A 1 49 ? -58.296 11.377 0.101 1.00 72.80 ? 49 GLU A OE2 1 ATOM 343 N N . PRO A 1 50 ? -59.892 17.283 -2.793 1.00 52.87 ? 50 PRO A N 1 ATOM 344 C CA . PRO A 1 50 ? -60.942 18.158 -3.315 1.00 52.03 ? 50 PRO A CA 1 ATOM 345 C C . PRO A 1 50 ? -62.322 17.583 -3.065 1.00 53.07 ? 50 PRO A C 1 ATOM 346 O O . PRO A 1 50 ? -62.502 16.359 -3.075 1.00 51.76 ? 50 PRO A O 1 ATOM 347 C CB . PRO A 1 50 ? -60.663 18.221 -4.824 1.00 52.15 ? 50 PRO A CB 1 ATOM 348 C CG . PRO A 1 50 ? -59.478 17.355 -5.077 1.00 52.93 ? 50 PRO A CG 1 ATOM 349 C CD . PRO A 1 50 ? -59.228 16.521 -3.861 1.00 52.97 ? 50 PRO A CD 1 ATOM 350 N N . LYS A 1 51 ? -63.285 18.471 -2.849 1.00 53.73 ? 51 LYS A N 1 ATOM 351 C CA . LYS A 1 51 ? -64.664 18.067 -2.664 1.00 56.00 ? 51 LYS A CA 1 ATOM 352 C C . LYS A 1 51 ? -65.190 17.297 -3.876 1.00 58.05 ? 51 LYS A C 1 ATOM 353 O O . LYS A 1 51 ? -65.071 17.747 -5.017 1.00 56.65 ? 51 LYS A O 1 ATOM 354 C CB . LYS A 1 51 ? -65.546 19.291 -2.422 1.00 56.12 ? 51 LYS A CB 1 ATOM 355 C CG . LYS A 1 51 ? -66.991 18.961 -2.081 1.00 57.99 ? 51 LYS A CG 1 ATOM 356 C CD . LYS A 1 51 ? -67.088 18.023 -0.888 1.00 59.02 ? 51 LYS A CD 1 ATOM 357 C CE . LYS A 1 51 ? -68.516 17.884 -0.390 1.00 60.67 ? 51 LYS A CE 1 ATOM 358 N NZ . LYS A 1 51 ? -68.634 16.683 0.484 1.00 61.88 ? 51 LYS A NZ 1 ATOM 359 N N . LYS A 1 52 ? -65.765 16.130 -3.617 1.00 60.48 ? 52 LYS A N 1 ATOM 360 C CA . LYS A 1 52 ? -66.445 15.382 -4.652 1.00 63.65 ? 52 LYS A CA 1 ATOM 361 C C . LYS A 1 52 ? -67.691 16.151 -5.062 1.00 63.49 ? 52 LYS A C 1 ATOM 362 O O . LYS A 1 52 ? -68.518 16.482 -4.221 1.00 61.59 ? 52 LYS A O 1 ATOM 363 C CB . LYS A 1 52 ? -66.834 13.991 -4.153 1.00 68.04 ? 52 LYS A CB 1 ATOM 364 C CG . LYS A 1 52 ? -65.646 13.062 -3.978 1.00 70.47 ? 52 LYS A CG 1 ATOM 365 C CD . LYS A 1 52 ? -65.987 11.834 -3.148 1.00 74.14 ? 52 LYS A CD 1 ATOM 366 C CE . LYS A 1 52 ? -64.718 11.069 -2.786 1.00 76.29 ? 52 LYS A CE 1 ATOM 367 N NZ . LYS A 1 52 ? -64.971 9.874 -1.929 1.00 78.41 ? 52 LYS A NZ 1 ATOM 368 N N . PRO A 1 53 ? -67.830 16.442 -6.359 1.00 65.24 ? 53 PRO A N 1 ATOM 369 C CA . PRO A 1 53 ? -69.031 17.129 -6.831 1.00 66.78 ? 53 PRO A CA 1 ATOM 370 C C . PRO A 1 53 ? -70.322 16.480 -6.339 1.00 68.01 ? 53 PRO A C 1 ATOM 371 O O . PRO A 1 53 ? -70.344 15.293 -6.015 1.00 67.91 ? 53 PRO A O 1 ATOM 372 C CB . PRO A 1 53 ? -68.933 17.008 -8.357 1.00 67.72 ? 53 PRO A CB 1 ATOM 373 C CG . PRO A 1 53 ? -67.481 16.828 -8.647 1.00 66.90 ? 53 PRO A CG 1 ATOM 374 C CD . PRO A 1 53 ? -66.880 16.150 -7.450 1.00 66.04 ? 53 PRO A CD 1 ATOM 375 N N . TRP A 1 54 ? -71.386 17.268 -6.296 1.00 68.96 ? 54 TRP A N 1 ATOM 376 C CA . TRP A 1 54 ? -72.685 16.798 -5.824 1.00 70.67 ? 54 TRP A CA 1 ATOM 377 C C . TRP A 1 54 ? -73.755 17.191 -6.844 1.00 72.54 ? 54 TRP A C 1 ATOM 378 O O . TRP A 1 54 ? -73.643 18.220 -7.527 1.00 71.92 ? 54 TRP A O 1 ATOM 379 C CB . TRP A 1 54 ? -73.007 17.402 -4.445 1.00 68.77 ? 54 TRP A CB 1 ATOM 380 C CG . TRP A 1 54 ? -73.074 18.881 -4.500 1.00 66.70 ? 54 TRP A CG 1 ATOM 381 C CD1 . TRP A 1 54 ? -74.153 19.642 -4.837 1.00 67.96 ? 54 TRP A CD1 1 ATOM 382 C CD2 . TRP A 1 54 ? -71.998 19.787 -4.279 1.00 63.46 ? 54 TRP A CD2 1 ATOM 383 N NE1 . TRP A 1 54 ? -73.817 20.973 -4.825 1.00 66.32 ? 54 TRP A NE1 1 ATOM 384 C CE2 . TRP A 1 54 ? -72.497 21.088 -4.486 1.00 63.54 ? 54 TRP A CE2 1 ATOM 385 C CE3 . TRP A 1 54 ? -70.661 19.629 -3.921 1.00 62.03 ? 54 TRP A CE3 1 ATOM 386 C CZ2 . TRP A 1 54 ? -71.707 22.223 -4.342 1.00 61.75 ? 54 TRP A CZ2 1 ATOM 387 C CZ3 . TRP A 1 54 ? -69.876 20.762 -3.765 1.00 60.41 ? 54 TRP A CZ3 1 ATOM 388 C CH2 . TRP A 1 54 ? -70.401 22.040 -3.979 1.00 60.47 ? 54 TRP A CH2 1 ATOM 389 N N . SER A 1 55 ? -74.783 16.363 -6.962 1.00 74.82 ? 55 SER A N 1 ATOM 390 C CA . SER A 1 55 ? -75.966 16.752 -7.714 1.00 77.85 ? 55 SER A CA 1 ATOM 391 C C . SER A 1 55 ? -76.905 17.443 -6.736 1.00 78.26 ? 55 SER A C 1 ATOM 392 O O . SER A 1 55 ? -76.648 17.475 -5.526 1.00 78.07 ? 55 SER A O 1 ATOM 393 C CB . SER A 1 55 ? -76.642 15.547 -8.381 1.00 79.95 ? 55 SER A CB 1 ATOM 394 O OG . SER A 1 55 ? -77.076 14.601 -7.421 1.00 80.66 ? 55 SER A OG 1 ATOM 395 N N . GLY A 1 56 ? -77.986 18.007 -7.263 1.00 79.06 ? 56 GLY A N 1 ATOM 396 C CA . GLY A 1 56 ? -78.929 18.756 -6.443 1.00 77.28 ? 56 GLY A CA 1 ATOM 397 C C . GLY A 1 56 ? -78.332 20.060 -5.958 1.00 73.01 ? 56 GLY A C 1 ATOM 398 O O . GLY A 1 56 ? -77.268 20.485 -6.420 1.00 71.45 ? 56 GLY A O 1 ATOM 399 N N . VAL A 1 57 ? -79.021 20.684 -5.010 1.00 71.08 ? 57 VAL A N 1 ATOM 400 C CA . VAL A 1 57 ? -78.666 22.013 -4.529 1.00 67.45 ? 57 VAL A CA 1 ATOM 401 C C . VAL A 1 57 ? -78.041 21.960 -3.144 1.00 63.73 ? 57 VAL A C 1 ATOM 402 O O . VAL A 1 57 ? -78.582 21.336 -2.235 1.00 61.87 ? 57 VAL A O 1 ATOM 403 C CB . VAL A 1 57 ? -79.906 22.923 -4.488 1.00 68.35 ? 57 VAL A CB 1 ATOM 404 C CG1 . VAL A 1 57 ? -79.492 24.371 -4.293 1.00 67.18 ? 57 VAL A CG1 1 ATOM 405 C CG2 . VAL A 1 57 ? -80.705 22.771 -5.772 1.00 70.51 ? 57 VAL A CG2 1 ATOM 406 N N . TRP A 1 58 ? -76.891 22.613 -3.001 1.00 62.21 ? 58 TRP A N 1 ATOM 407 C CA . TRP A 1 58 ? -76.266 22.789 -1.699 1.00 61.10 ? 58 TRP A CA 1 ATOM 408 C C . TRP A 1 58 ? -76.909 23.989 -1.005 1.00 62.62 ? 58 TRP A C 1 ATOM 409 O O . TRP A 1 58 ? -76.892 25.101 -1.542 1.00 62.44 ? 58 TRP A O 1 ATOM 410 C CB . TRP A 1 58 ? -74.759 23.008 -1.831 1.00 58.27 ? 58 TRP A CB 1 ATOM 411 C CG . TRP A 1 58 ? -74.068 23.005 -0.494 1.00 56.62 ? 58 TRP A CG 1 ATOM 412 C CD1 . TRP A 1 58 ? -73.871 24.073 0.328 1.00 55.22 ? 58 TRP A CD1 1 ATOM 413 C CD2 . TRP A 1 58 ? -73.515 21.872 0.186 1.00 56.22 ? 58 TRP A CD2 1 ATOM 414 N NE1 . TRP A 1 58 ? -73.225 23.683 1.473 1.00 53.56 ? 58 TRP A NE1 1 ATOM 415 C CE2 . TRP A 1 58 ? -72.998 22.335 1.416 1.00 54.09 ? 58 TRP A CE2 1 ATOM 416 C CE3 . TRP A 1 58 ? -73.404 20.510 -0.126 1.00 57.65 ? 58 TRP A CE3 1 ATOM 417 C CZ2 . TRP A 1 58 ? -72.369 21.490 2.333 1.00 53.64 ? 58 TRP A CZ2 1 ATOM 418 C CZ3 . TRP A 1 58 ? -72.786 19.664 0.792 1.00 57.23 ? 58 TRP A CZ3 1 ATOM 419 C CH2 . TRP A 1 58 ? -72.273 20.163 2.008 1.00 55.42 ? 58 TRP A CH2 1 ATOM 420 N N . ASN A 1 59 ? -77.494 23.756 0.172 1.00 64.09 ? 59 ASN A N 1 ATOM 421 C CA . ASN A 1 59 ? -78.053 24.835 0.973 1.00 65.72 ? 59 ASN A CA 1 ATOM 422 C C . ASN A 1 59 ? -76.867 25.568 1.572 1.00 61.49 ? 59 ASN A C 1 ATOM 423 O O . ASN A 1 59 ? -76.166 25.034 2.427 1.00 59.78 ? 59 ASN A O 1 ATOM 424 C CB . ASN A 1 59 ? -79.017 24.305 2.060 1.00 70.13 ? 59 ASN A CB 1 ATOM 425 C CG . ASN A 1 59 ? -79.813 25.419 2.753 1.00 74.65 ? 59 ASN A CG 1 ATOM 426 O OD1 . ASN A 1 59 ? -79.272 26.490 3.032 1.00 72.51 ? 59 ASN A OD1 1 ATOM 427 N ND2 . ASN A 1 59 ? -81.109 25.161 3.038 1.00 80.22 ? 59 ASN A ND2 1 ATOM 428 N N . ALA A 1 60 ? -76.623 26.773 1.072 1.00 59.46 ? 60 ALA A N 1 ATOM 429 C CA . ALA A 1 60 ? -75.569 27.626 1.583 1.00 57.53 ? 60 ALA A CA 1 ATOM 430 C C . ALA A 1 60 ? -76.185 28.859 2.226 1.00 58.54 ? 60 ALA A C 1 ATOM 431 O O . ALA A 1 60 ? -75.777 29.988 1.941 1.00 58.94 ? 60 ALA A O 1 ATOM 432 C CB . ALA A 1 60 ? -74.628 28.028 0.458 1.00 56.39 ? 60 ALA A CB 1 ATOM 433 N N . SER A 1 61 ? -77.171 28.643 3.091 1.00 59.94 ? 61 SER A N 1 ATOM 434 C CA . SER A 1 61 ? -77.871 29.745 3.745 1.00 60.88 ? 61 SER A CA 1 ATOM 435 C C . SER A 1 61 ? -77.422 29.985 5.191 1.00 58.90 ? 61 SER A C 1 ATOM 436 O O . SER A 1 61 ? -77.775 31.006 5.773 1.00 58.37 ? 61 SER A O 1 ATOM 437 C CB . SER A 1 61 ? -79.379 29.514 3.686 1.00 63.61 ? 61 SER A CB 1 ATOM 438 O OG . SER A 1 61 ? -79.745 28.382 4.449 1.00 65.02 ? 61 SER A OG 1 ATOM 439 N N . THR A 1 62 ? -76.653 29.061 5.767 1.00 58.24 ? 62 THR A N 1 ATOM 440 C CA . THR A 1 62 ? -76.126 29.238 7.127 1.00 59.01 ? 62 THR A CA 1 ATOM 441 C C . THR A 1 62 ? -74.617 29.067 7.181 1.00 57.19 ? 62 THR A C 1 ATOM 442 O O . THR A 1 62 ? -74.028 28.381 6.351 1.00 57.49 ? 62 THR A O 1 ATOM 443 C CB . THR A 1 62 ? -76.742 28.236 8.119 1.00 60.71 ? 62 THR A CB 1 ATOM 444 O OG1 . THR A 1 62 ? -76.622 26.909 7.594 1.00 60.83 ? 62 THR A OG1 1 ATOM 445 C CG2 . THR A 1 62 ? -78.220 28.564 8.383 1.00 63.29 ? 62 THR A CG2 1 ATOM 446 N N . TYR A 1 63 ? -73.996 29.697 8.170 1.00 56.90 ? 63 TYR A N 1 ATOM 447 C CA . TYR A 1 63 ? -72.556 29.558 8.388 1.00 54.70 ? 63 TYR A CA 1 ATOM 448 C C . TYR A 1 63 ? -72.194 28.109 8.682 1.00 53.65 ? 63 TYR A C 1 ATOM 449 O O . TYR A 1 63 ? -72.962 27.384 9.299 1.00 54.73 ? 63 TYR A O 1 ATOM 450 C CB . TYR A 1 63 ? -72.092 30.399 9.576 1.00 53.65 ? 63 TYR A CB 1 ATOM 451 C CG . TYR A 1 63 ? -71.732 31.835 9.287 1.00 54.33 ? 63 TYR A CG 1 ATOM 452 C CD1 . TYR A 1 63 ? -70.874 32.171 8.245 1.00 54.08 ? 63 TYR A CD1 1 ATOM 453 C CD2 . TYR A 1 63 ? -72.197 32.864 10.108 1.00 55.88 ? 63 TYR A CD2 1 ATOM 454 C CE1 . TYR A 1 63 ? -70.512 33.493 8.011 1.00 54.45 ? 63 TYR A CE1 1 ATOM 455 C CE2 . TYR A 1 63 ? -71.844 34.185 9.880 1.00 56.14 ? 63 TYR A CE2 1 ATOM 456 C CZ . TYR A 1 63 ? -70.999 34.497 8.834 1.00 55.44 ? 63 TYR A CZ 1 ATOM 457 O OH . TYR A 1 63 ? -70.642 35.810 8.615 1.00 56.32 ? 63 TYR A OH 1 ATOM 458 N N . PRO A 1 64 ? -70.999 27.693 8.275 1.00 52.17 ? 64 PRO A N 1 ATOM 459 C CA . PRO A 1 64 ? -70.561 26.333 8.516 1.00 52.15 ? 64 PRO A CA 1 ATOM 460 C C . PRO A 1 64 ? -70.047 26.168 9.932 1.00 51.69 ? 64 PRO A C 1 ATOM 461 O O . PRO A 1 64 ? -69.882 27.153 10.641 1.00 51.97 ? 64 PRO A O 1 ATOM 462 C CB . PRO A 1 64 ? -69.403 26.186 7.541 1.00 51.32 ? 64 PRO A CB 1 ATOM 463 C CG . PRO A 1 64 ? -68.802 27.552 7.518 1.00 49.93 ? 64 PRO A CG 1 ATOM 464 C CD . PRO A 1 64 ? -69.954 28.500 7.621 1.00 50.56 ? 64 PRO A CD 1 ATOM 465 N N . ASN A 1 65 ? -69.780 24.929 10.329 1.00 51.83 ? 65 ASN A N 1 ATOM 466 C CA . ASN A 1 65 ? -69.088 24.662 11.586 1.00 52.21 ? 65 ASN A CA 1 ATOM 467 C C . ASN A 1 65 ? -67.695 25.300 11.598 1.00 49.44 ? 65 ASN A C 1 ATOM 468 O O . ASN A 1 65 ? -67.105 25.533 10.549 1.00 49.25 ? 65 ASN A O 1 ATOM 469 C CB . ASN A 1 65 ? -68.945 23.151 11.819 1.00 54.05 ? 65 ASN A CB 1 ATOM 470 C CG . ASN A 1 65 ? -70.270 22.458 12.138 1.00 55.97 ? 65 ASN A CG 1 ATOM 471 O OD1 . ASN A 1 65 ? -70.406 21.266 11.899 1.00 57.85 ? 65 ASN A OD1 1 ATOM 472 N ND2 . ASN A 1 65 ? -71.233 23.189 12.687 1.00 55.94 ? 65 ASN A ND2 1 ATOM 473 N N . ASN A 1 66 ? -67.181 25.584 12.790 1.00 48.08 ? 66 ASN A N 1 ATOM 474 C CA . ASN A 1 66 ? -65.812 26.056 12.946 1.00 45.48 ? 66 ASN A CA 1 ATOM 475 C C . ASN A 1 66 ? -64.920 24.850 13.180 1.00 45.38 ? 66 ASN A C 1 ATOM 476 O O . ASN A 1 66 ? -65.392 23.819 13.657 1.00 47.87 ? 66 ASN A O 1 ATOM 477 C CB . ASN A 1 66 ? -65.704 27.014 14.129 1.00 44.48 ? 66 ASN A CB 1 ATOM 478 C CG . ASN A 1 66 ? -66.658 28.187 14.030 1.00 45.20 ? 66 ASN A CG 1 ATOM 479 O OD1 . ASN A 1 66 ? -67.275 28.576 15.019 1.00 47.30 ? 66 ASN A OD1 1 ATOM 480 N ND2 . ASN A 1 66 ? -66.790 28.755 12.840 1.00 45.20 ? 66 ASN A ND2 1 ATOM 481 N N . CYS A 1 67 ? -63.640 24.967 12.847 1.00 43.34 ? 67 CYS A N 1 ATOM 482 C CA . CYS A 1 67 ? -62.699 23.872 13.079 1.00 43.66 ? 67 CYS A CA 1 ATOM 483 C C . CYS A 1 67 ? -62.420 23.701 14.579 1.00 43.77 ? 67 CYS A C 1 ATOM 484 O O . CYS A 1 67 ? -62.523 24.658 15.334 1.00 42.85 ? 67 CYS A O 1 ATOM 485 C CB . CYS A 1 67 ? -61.390 24.110 12.316 1.00 42.45 ? 67 CYS A CB 1 ATOM 486 S SG . CYS A 1 67 ? -61.535 24.122 10.503 1.00 42.91 ? 67 CYS A SG 1 ATOM 487 N N . GLN A 1 68 ? -62.064 22.479 14.983 1.00 44.57 ? 68 GLN A N 1 ATOM 488 C CA . GLN A 1 68 ? -61.743 22.147 16.375 1.00 44.51 ? 68 GLN A CA 1 ATOM 489 C C . GLN A 1 68 ? -60.532 22.917 16.870 1.00 43.76 ? 68 GLN A C 1 ATOM 490 O O . GLN A 1 68 ? -59.495 22.948 16.205 1.00 43.78 ? 68 GLN A O 1 ATOM 491 C CB . GLN A 1 68 ? -61.432 20.661 16.524 1.00 45.30 ? 68 GLN A CB 1 ATOM 492 C CG . GLN A 1 68 ? -62.625 19.751 16.322 1.00 47.16 ? 68 GLN A CG 1 ATOM 493 C CD . GLN A 1 68 ? -63.527 19.674 17.529 1.00 47.77 ? 68 GLN A CD 1 ATOM 494 O OE1 . GLN A 1 68 ? -63.470 20.512 18.423 1.00 48.49 ? 68 GLN A OE1 1 ATOM 495 N NE2 . GLN A 1 68 ? -64.369 18.656 17.561 1.00 48.89 ? 68 GLN A NE2 1 ATOM 496 N N . GLN A 1 69 ? -60.641 23.456 18.078 1.00 43.24 ? 69 GLN A N 1 ATOM 497 C CA . GLN A 1 69 ? -59.684 24.428 18.566 1.00 42.92 ? 69 GLN A CA 1 ATOM 498 C C . GLN A 1 69 ? -59.844 24.738 20.048 1.00 44.07 ? 69 GLN A C 1 ATOM 499 O O . GLN A 1 69 ? -60.846 24.415 20.695 1.00 42.46 ? 69 GLN A O 1 ATOM 500 C CB . GLN A 1 69 ? -59.761 25.731 17.755 1.00 41.96 ? 69 GLN A CB 1 ATOM 501 C CG . GLN A 1 69 ? -61.117 26.400 17.795 1.00 42.69 ? 69 GLN A CG 1 ATOM 502 C CD . GLN A 1 69 ? -61.207 27.719 17.063 1.00 43.16 ? 69 GLN A CD 1 ATOM 503 O OE1 . GLN A 1 69 ? -60.774 28.768 17.559 1.00 42.81 ? 69 GLN A OE1 1 ATOM 504 N NE2 . GLN A 1 69 ? -61.817 27.682 15.890 1.00 44.00 ? 69 GLN A NE2 1 ATOM 505 N N . TYR A 1 70 ? -58.804 25.371 20.572 1.00 46.07 ? 70 TYR A N 1 ATOM 506 C CA . TYR A 1 70 ? -58.803 25.850 21.933 1.00 45.54 ? 70 TYR A CA 1 ATOM 507 C C . TYR A 1 70 ? -59.850 26.939 22.033 1.00 44.78 ? 70 TYR A C 1 ATOM 508 O O . TYR A 1 70 ? -60.059 27.702 21.097 1.00 44.57 ? 70 TYR A O 1 ATOM 509 C CB . TYR A 1 70 ? -57.429 26.381 22.308 1.00 44.90 ? 70 TYR A CB 1 ATOM 510 C CG . TYR A 1 70 ? -57.362 26.942 23.704 1.00 48.45 ? 70 TYR A CG 1 ATOM 511 C CD1 . TYR A 1 70 ? -57.234 26.103 24.807 1.00 50.01 ? 70 TYR A CD1 1 ATOM 512 C CD2 . TYR A 1 70 ? -57.432 28.314 23.922 1.00 49.26 ? 70 TYR A CD2 1 ATOM 513 C CE1 . TYR A 1 70 ? -57.171 26.615 26.080 1.00 52.53 ? 70 TYR A CE1 1 ATOM 514 C CE2 . TYR A 1 70 ? -57.371 28.839 25.195 1.00 51.55 ? 70 TYR A CE2 1 ATOM 515 C CZ . TYR A 1 70 ? -57.238 27.989 26.270 1.00 54.20 ? 70 TYR A CZ 1 ATOM 516 O OH . TYR A 1 70 ? -57.183 28.516 27.544 1.00 58.38 ? 70 TYR A OH 1 ATOM 517 N N . VAL A 1 71 ? -60.532 26.969 23.169 1.00 45.17 ? 71 VAL A N 1 ATOM 518 C CA . VAL A 1 71 ? -61.543 27.966 23.453 1.00 43.46 ? 71 VAL A CA 1 ATOM 519 C C . VAL A 1 71 ? -61.067 28.742 24.675 1.00 44.10 ? 71 VAL A C 1 ATOM 520 O O . VAL A 1 71 ? -60.856 28.176 25.758 1.00 43.78 ? 71 VAL A O 1 ATOM 521 C CB . VAL A 1 71 ? -62.899 27.302 23.721 1.00 44.27 ? 71 VAL A CB 1 ATOM 522 C CG1 . VAL A 1 71 ? -63.943 28.340 24.101 1.00 44.76 ? 71 VAL A CG1 1 ATOM 523 C CG2 . VAL A 1 71 ? -63.332 26.497 22.505 1.00 43.77 ? 71 VAL A CG2 1 ATOM 524 N N . ASP A 1 72 ? -60.868 30.039 24.469 1.00 44.24 ? 72 ASP A N 1 ATOM 525 C CA . ASP A 1 72 ? -60.449 30.960 25.511 1.00 45.30 ? 72 ASP A CA 1 ATOM 526 C C . ASP A 1 72 ? -61.607 31.125 26.476 1.00 47.34 ? 72 ASP A C 1 ATOM 527 O O . ASP A 1 72 ? -62.698 31.463 26.058 1.00 48.02 ? 72 ASP A O 1 ATOM 528 C CB . ASP A 1 72 ? -60.074 32.293 24.855 1.00 44.95 ? 72 ASP A CB 1 ATOM 529 C CG . ASP A 1 72 ? -59.806 33.400 25.841 1.00 45.90 ? 72 ASP A CG 1 ATOM 530 O OD1 . ASP A 1 72 ? -59.647 33.141 27.057 1.00 49.31 ? 72 ASP A OD1 1 ATOM 531 O OD2 . ASP A 1 72 ? -59.760 34.553 25.375 1.00 45.22 ? 72 ASP A OD2 1 ATOM 532 N N . GLU A 1 73 ? -61.380 30.848 27.757 1.00 50.33 ? 73 GLU A N 1 ATOM 533 C CA . GLU A 1 73 ? -62.396 31.076 28.795 1.00 53.15 ? 73 GLU A CA 1 ATOM 534 C C . GLU A 1 73 ? -61.786 31.856 29.955 1.00 52.81 ? 73 GLU A C 1 ATOM 535 O O . GLU A 1 73 ? -62.212 31.731 31.106 1.00 51.94 ? 73 GLU A O 1 ATOM 536 C CB . GLU A 1 73 ? -62.960 29.751 29.297 1.00 56.72 ? 73 GLU A CB 1 ATOM 537 C CG . GLU A 1 73 ? -63.546 28.873 28.203 1.00 59.34 ? 73 GLU A CG 1 ATOM 538 C CD . GLU A 1 73 ? -64.060 27.538 28.725 1.00 63.33 ? 73 GLU A CD 1 ATOM 539 O OE1 . GLU A 1 73 ? -63.530 27.026 29.748 1.00 62.98 ? 73 GLU A OE1 1 ATOM 540 O OE2 . GLU A 1 73 ? -65.000 27.002 28.095 1.00 64.77 ? 73 GLU A OE2 1 ATOM 541 N N . GLN A 1 74 ? -60.781 32.663 29.628 1.00 51.59 ? 74 GLN A N 1 ATOM 542 C CA . GLN A 1 74 ? -60.126 33.515 30.593 1.00 52.59 ? 74 GLN A CA 1 ATOM 543 C C . GLN A 1 74 ? -61.121 34.543 31.153 1.00 52.62 ? 74 GLN A C 1 ATOM 544 O O . GLN A 1 74 ? -61.102 34.846 32.331 1.00 54.56 ? 74 GLN A O 1 ATOM 545 C CB . GLN A 1 74 ? -58.948 34.208 29.910 1.00 53.83 ? 74 GLN A CB 1 ATOM 546 C CG . GLN A 1 74 ? -58.050 35.017 30.831 1.00 57.38 ? 74 GLN A CG 1 ATOM 547 C CD . GLN A 1 74 ? -57.358 34.163 31.875 1.00 60.17 ? 74 GLN A CD 1 ATOM 548 O OE1 . GLN A 1 74 ? -57.045 32.994 31.629 1.00 62.86 ? 74 GLN A OE1 1 ATOM 549 N NE2 . GLN A 1 74 ? -57.118 34.740 33.051 1.00 60.14 ? 74 GLN A NE2 1 ATOM 550 N N . PHE A 1 75 ? -62.011 35.051 30.303 1.00 52.71 ? 75 PHE A N 1 ATOM 551 C CA . PHE A 1 75 ? -62.982 36.076 30.696 1.00 51.31 ? 75 PHE A CA 1 ATOM 552 C C . PHE A 1 75 ? -64.403 35.706 30.248 1.00 52.26 ? 75 PHE A C 1 ATOM 553 O O . PHE A 1 75 ? -64.961 36.322 29.347 1.00 52.40 ? 75 PHE A O 1 ATOM 554 C CB . PHE A 1 75 ? -62.551 37.415 30.093 1.00 48.98 ? 75 PHE A CB 1 ATOM 555 C CG . PHE A 1 75 ? -61.150 37.812 30.460 1.00 46.43 ? 75 PHE A CG 1 ATOM 556 C CD1 . PHE A 1 75 ? -60.845 38.187 31.759 1.00 46.36 ? 75 PHE A CD1 1 ATOM 557 C CD2 . PHE A 1 75 ? -60.137 37.795 29.517 1.00 44.09 ? 75 PHE A CD2 1 ATOM 558 C CE1 . PHE A 1 75 ? -59.556 38.544 32.106 1.00 45.72 ? 75 PHE A CE1 1 ATOM 559 C CE2 . PHE A 1 75 ? -58.842 38.149 29.858 1.00 43.34 ? 75 PHE A CE2 1 ATOM 560 C CZ . PHE A 1 75 ? -58.548 38.522 31.154 1.00 43.60 ? 75 PHE A CZ 1 ATOM 561 N N . PRO A 1 76 ? -64.999 34.687 30.879 1.00 53.36 ? 76 PRO A N 1 ATOM 562 C CA . PRO A 1 76 ? -66.304 34.216 30.437 1.00 53.82 ? 76 PRO A CA 1 ATOM 563 C C . PRO A 1 76 ? -67.327 35.334 30.272 1.00 55.41 ? 76 PRO A C 1 ATOM 564 O O . PRO A 1 76 ? -67.514 36.145 31.182 1.00 54.31 ? 76 PRO A O 1 ATOM 565 C CB . PRO A 1 76 ? -66.717 33.267 31.551 1.00 54.67 ? 76 PRO A CB 1 ATOM 566 C CG . PRO A 1 76 ? -65.432 32.736 32.058 1.00 54.32 ? 76 PRO A CG 1 ATOM 567 C CD . PRO A 1 76 ? -64.513 33.919 32.035 1.00 54.18 ? 76 PRO A CD 1 ATOM 568 N N . GLY A 1 77 ? -67.958 35.377 29.099 1.00 56.43 ? 77 GLY A N 1 ATOM 569 C CA . GLY A 1 77 ? -68.953 36.405 28.776 1.00 57.79 ? 77 GLY A CA 1 ATOM 570 C C . GLY A 1 77 ? -68.403 37.793 28.445 1.00 56.41 ? 77 GLY A C 1 ATOM 571 O O . GLY A 1 77 ? -69.175 38.729 28.224 1.00 59.97 ? 77 GLY A O 1 ATOM 572 N N . PHE A 1 78 ? -67.082 37.947 28.409 1.00 51.95 ? 78 PHE A N 1 ATOM 573 C CA . PHE A 1 78 ? -66.483 39.232 28.086 1.00 49.53 ? 78 PHE A CA 1 ATOM 574 C C . PHE A 1 78 ? -66.373 39.337 26.570 1.00 47.19 ? 78 PHE A C 1 ATOM 575 O O . PHE A 1 78 ? -65.655 38.576 25.948 1.00 45.39 ? 78 PHE A O 1 ATOM 576 C CB . PHE A 1 78 ? -65.114 39.369 28.761 1.00 48.18 ? 78 PHE A CB 1 ATOM 577 C CG . PHE A 1 78 ? -64.415 40.669 28.475 1.00 47.29 ? 78 PHE A CG 1 ATOM 578 C CD1 . PHE A 1 78 ? -64.955 41.866 28.901 1.00 47.85 ? 78 PHE A CD1 1 ATOM 579 C CD2 . PHE A 1 78 ? -63.215 40.691 27.772 1.00 46.12 ? 78 PHE A CD2 1 ATOM 580 C CE1 . PHE A 1 78 ? -64.317 43.065 28.640 1.00 47.79 ? 78 PHE A CE1 1 ATOM 581 C CE2 . PHE A 1 78 ? -62.572 41.887 27.507 1.00 45.81 ? 78 PHE A CE2 1 ATOM 582 C CZ . PHE A 1 78 ? -63.124 43.078 27.946 1.00 46.88 ? 78 PHE A CZ 1 ATOM 583 N N . SER A 1 79 ? -67.088 40.289 25.987 1.00 48.12 ? 79 SER A N 1 ATOM 584 C CA . SER A 1 79 ? -67.140 40.442 24.535 1.00 47.95 ? 79 SER A CA 1 ATOM 585 C C . SER A 1 79 ? -65.760 40.556 23.898 1.00 45.92 ? 79 SER A C 1 ATOM 586 O O . SER A 1 79 ? -65.542 40.013 22.828 1.00 46.22 ? 79 SER A O 1 ATOM 587 C CB . SER A 1 79 ? -67.965 41.670 24.156 1.00 49.52 ? 79 SER A CB 1 ATOM 588 O OG . SER A 1 79 ? -67.228 42.856 24.400 1.00 50.41 ? 79 SER A OG 1 ATOM 589 N N . GLY A 1 80 ? -64.829 41.250 24.547 1.00 44.93 ? 80 GLY A N 1 ATOM 590 C CA . GLY A 1 80 ? -63.476 41.412 23.991 1.00 43.88 ? 80 GLY A CA 1 ATOM 591 C C . GLY A 1 80 ? -62.737 40.100 23.776 1.00 42.55 ? 80 GLY A C 1 ATOM 592 O O . GLY A 1 80 ? -61.891 39.983 22.901 1.00 39.41 ? 80 GLY A O 1 ATOM 593 N N . SER A 1 81 ? -63.064 39.130 24.622 1.00 44.93 ? 81 SER A N 1 ATOM 594 C CA . SER A 1 81 ? -62.474 37.798 24.638 1.00 45.05 ? 81 SER A CA 1 ATOM 595 C C . SER A 1 81 ? -63.290 36.869 23.739 1.00 44.76 ? 81 SER A C 1 ATOM 596 O O . SER A 1 81 ? -62.742 36.183 22.874 1.00 43.13 ? 81 SER A O 1 ATOM 597 C CB . SER A 1 81 ? -62.459 37.298 26.100 1.00 47.37 ? 81 SER A CB 1 ATOM 598 O OG . SER A 1 81 ? -62.389 35.886 26.233 1.00 49.65 ? 81 SER A OG 1 ATOM 599 N N . GLU A 1 82 ? -64.607 36.879 23.943 1.00 46.45 ? 82 GLU A N 1 ATOM 600 C CA . GLU A 1 82 ? -65.531 35.973 23.264 1.00 47.19 ? 82 GLU A CA 1 ATOM 601 C C . GLU A 1 82 ? -65.659 36.287 21.777 1.00 45.78 ? 82 GLU A C 1 ATOM 602 O O . GLU A 1 82 ? -65.939 35.399 20.980 1.00 45.25 ? 82 GLU A O 1 ATOM 603 C CB . GLU A 1 82 ? -66.921 36.040 23.900 1.00 50.56 ? 82 GLU A CB 1 ATOM 604 C CG . GLU A 1 82 ? -66.987 35.693 25.389 1.00 53.16 ? 82 GLU A CG 1 ATOM 605 C CD . GLU A 1 82 ? -67.051 34.201 25.675 1.00 54.52 ? 82 GLU A CD 1 ATOM 606 O OE1 . GLU A 1 82 ? -66.813 33.396 24.736 1.00 53.23 ? 82 GLU A OE1 1 ATOM 607 O OE2 . GLU A 1 82 ? -67.345 33.845 26.851 1.00 55.52 ? 82 GLU A OE2 1 ATOM 608 N N . MET A 1 83 ? -65.437 37.537 21.386 1.00 45.13 ? 83 MET A N 1 ATOM 609 C CA . MET A 1 83 ? -65.571 37.893 19.986 1.00 44.68 ? 83 MET A CA 1 ATOM 610 C C . MET A 1 83 ? -64.646 37.072 19.086 1.00 43.12 ? 83 MET A C 1 ATOM 611 O O . MET A 1 83 ? -64.894 36.997 17.891 1.00 43.18 ? 83 MET A O 1 ATOM 612 C CB . MET A 1 83 ? -65.335 39.385 19.764 1.00 46.44 ? 83 MET A CB 1 ATOM 613 C CG . MET A 1 83 ? -63.911 39.841 20.011 1.00 48.24 ? 83 MET A CG 1 ATOM 614 S SD . MET A 1 83 ? -63.608 41.449 19.264 1.00 51.33 ? 83 MET A SD 1 ATOM 615 C CE . MET A 1 83 ? -64.342 42.537 20.490 1.00 55.79 ? 83 MET A CE 1 ATOM 616 N N . TRP A 1 84 ? -63.592 36.473 19.651 1.00 41.78 ? 84 TRP A N 1 ATOM 617 C CA . TRP A 1 84 ? -62.639 35.660 18.871 1.00 40.37 ? 84 TRP A CA 1 ATOM 618 C C . TRP A 1 84 ? -62.903 34.154 18.920 1.00 39.46 ? 84 TRP A C 1 ATOM 619 O O . TRP A 1 84 ? -62.355 33.414 18.106 1.00 35.87 ? 84 TRP A O 1 ATOM 620 C CB . TRP A 1 84 ? -61.204 35.929 19.326 1.00 39.89 ? 84 TRP A CB 1 ATOM 621 C CG . TRP A 1 84 ? -60.858 37.374 19.339 1.00 41.28 ? 84 TRP A CG 1 ATOM 622 C CD1 . TRP A 1 84 ? -60.750 38.185 20.431 1.00 43.01 ? 84 TRP A CD1 1 ATOM 623 C CD2 . TRP A 1 84 ? -60.594 38.193 18.206 1.00 41.66 ? 84 TRP A CD2 1 ATOM 624 N NE1 . TRP A 1 84 ? -60.423 39.464 20.045 1.00 42.36 ? 84 TRP A NE1 1 ATOM 625 C CE2 . TRP A 1 84 ? -60.324 39.495 18.682 1.00 41.96 ? 84 TRP A CE2 1 ATOM 626 C CE3 . TRP A 1 84 ? -60.566 37.958 16.826 1.00 42.18 ? 84 TRP A CE3 1 ATOM 627 C CZ2 . TRP A 1 84 ? -60.026 40.553 17.830 1.00 42.50 ? 84 TRP A CZ2 1 ATOM 628 C CZ3 . TRP A 1 84 ? -60.271 39.015 15.976 1.00 41.53 ? 84 TRP A CZ3 1 ATOM 629 C CH2 . TRP A 1 84 ? -60.005 40.297 16.484 1.00 42.37 ? 84 TRP A CH2 1 ATOM 630 N N . ASN A 1 85 ? -63.708 33.700 19.882 1.00 40.25 ? 85 ASN A N 1 ATOM 631 C CA . ASN A 1 85 ? -64.024 32.279 20.005 1.00 41.30 ? 85 ASN A CA 1 ATOM 632 C C . ASN A 1 85 ? -65.015 31.834 18.925 1.00 43.05 ? 85 ASN A C 1 ATOM 633 O O . ASN A 1 85 ? -65.714 32.661 18.331 1.00 43.58 ? 85 ASN A O 1 ATOM 634 C CB . ASN A 1 85 ? -64.646 31.957 21.380 1.00 43.24 ? 85 ASN A CB 1 ATOM 635 C CG . ASN A 1 85 ? -63.648 32.004 22.532 1.00 42.25 ? 85 ASN A CG 1 ATOM 636 O OD1 . ASN A 1 85 ? -62.502 31.589 22.421 1.00 40.77 ? 85 ASN A OD1 1 ATOM 637 N ND2 . ASN A 1 85 ? -64.111 32.494 23.665 1.00 43.61 ? 85 ASN A ND2 1 ATOM 638 N N . PRO A 1 86 ? -65.097 30.514 18.682 1.00 44.84 ? 86 PRO A N 1 ATOM 639 C CA . PRO A 1 86 ? -66.119 29.959 17.799 1.00 45.52 ? 86 PRO A CA 1 ATOM 640 C C . PRO A 1 86 ? -67.538 30.342 18.209 1.00 48.32 ? 86 PRO A C 1 ATOM 641 O O . PRO A 1 86 ? -67.918 30.171 19.371 1.00 49.71 ? 86 PRO A O 1 ATOM 642 C CB . PRO A 1 86 ? -65.921 28.451 17.938 1.00 45.22 ? 86 PRO A CB 1 ATOM 643 C CG . PRO A 1 86 ? -64.485 28.294 18.254 1.00 44.39 ? 86 PRO A CG 1 ATOM 644 C CD . PRO A 1 86 ? -64.074 29.511 19.034 1.00 44.34 ? 86 PRO A CD 1 ATOM 645 N N . ASN A 1 87 ? -68.287 30.869 17.240 1.00 48.62 ? 87 ASN A N 1 ATOM 646 C CA . ASN A 1 87 ? -69.702 31.189 17.382 1.00 49.23 ? 87 ASN A CA 1 ATOM 647 C C . ASN A 1 87 ? -70.596 30.101 16.802 1.00 52.37 ? 87 ASN A C 1 ATOM 648 O O . ASN A 1 87 ? -71.811 30.167 16.933 1.00 54.33 ? 87 ASN A O 1 ATOM 649 C CB . ASN A 1 87 ? -70.020 32.515 16.689 1.00 48.93 ? 87 ASN A CB 1 ATOM 650 C CG . ASN A 1 87 ? -69.519 32.567 15.249 1.00 47.99 ? 87 ASN A CG 1 ATOM 651 O OD1 . ASN A 1 87 ? -68.878 31.638 14.758 1.00 47.22 ? 87 ASN A OD1 1 ATOM 652 N ND2 . ASN A 1 87 ? -69.799 33.667 14.577 1.00 47.57 ? 87 ASN A ND2 1 ATOM 653 N N . ARG A 1 88 ? -69.998 29.122 16.131 1.00 54.42 ? 88 ARG A N 1 ATOM 654 C CA . ARG A 1 88 ? -70.725 27.958 15.648 1.00 56.59 ? 88 ARG A CA 1 ATOM 655 C C . ARG A 1 88 ? -70.192 26.733 16.370 1.00 56.30 ? 88 ARG A C 1 ATOM 656 O O . ARG A 1 88 ? -69.216 26.820 17.116 1.00 56.71 ? 88 ARG A O 1 ATOM 657 C CB . ARG A 1 88 ? -70.557 27.814 14.131 1.00 58.07 ? 88 ARG A CB 1 ATOM 658 C CG . ARG A 1 88 ? -71.355 28.818 13.312 1.00 60.50 ? 88 ARG A CG 1 ATOM 659 C CD . ARG A 1 88 ? -72.848 28.488 13.327 1.00 64.66 ? 88 ARG A CD 1 ATOM 660 N NE . ARG A 1 88 ? -73.684 29.570 12.798 1.00 66.87 ? 88 ARG A NE 1 ATOM 661 C CZ . ARG A 1 88 ? -73.929 30.728 13.422 1.00 68.21 ? 88 ARG A CZ 1 ATOM 662 N NH1 . ARG A 1 88 ? -73.401 31.006 14.612 1.00 67.76 ? 88 ARG A NH1 1 ATOM 663 N NH2 . ARG A 1 88 ? -74.704 31.633 12.843 1.00 70.36 ? 88 ARG A NH2 1 ATOM 664 N N . GLU A 1 89 ? -70.836 25.594 16.155 1.00 57.73 ? 89 GLU A N 1 ATOM 665 C CA . GLU A 1 89 ? -70.378 24.350 16.748 1.00 59.49 ? 89 GLU A CA 1 ATOM 666 C C . GLU A 1 89 ? -69.091 23.901 16.076 1.00 55.71 ? 89 GLU A C 1 ATOM 667 O O . GLU A 1 89 ? -68.875 24.148 14.889 1.00 55.19 ? 89 GLU A O 1 ATOM 668 C CB . GLU A 1 89 ? -71.436 23.253 16.633 1.00 65.73 ? 89 GLU A CB 1 ATOM 669 C CG . GLU A 1 89 ? -71.473 22.358 17.866 1.00 71.85 ? 89 GLU A CG 1 ATOM 670 C CD . GLU A 1 89 ? -72.286 21.094 17.669 1.00 76.68 ? 89 GLU A CD 1 ATOM 671 O OE1 . GLU A 1 89 ? -72.277 20.533 16.539 1.00 75.44 ? 89 GLU A OE1 1 ATOM 672 O OE2 . GLU A 1 89 ? -72.922 20.662 18.660 1.00 80.00 ? 89 GLU A OE2 1 ATOM 673 N N . MET A 1 90 ? -68.228 23.249 16.839 1.00 52.69 ? 90 MET A N 1 ATOM 674 C CA . MET A 1 90 ? -66.950 22.825 16.309 1.00 49.87 ? 90 MET A CA 1 ATOM 675 C C . MET A 1 90 ? -67.027 21.428 15.758 1.00 48.27 ? 90 MET A C 1 ATOM 676 O O . MET A 1 90 ? -67.730 20.570 16.291 1.00 48.58 ? 90 MET A O 1 ATOM 677 C CB . MET A 1 90 ? -65.886 22.832 17.380 1.00 50.16 ? 90 MET A CB 1 ATOM 678 C CG . MET A 1 90 ? -65.731 24.152 18.072 1.00 49.77 ? 90 MET A CG 1 ATOM 679 S SD . MET A 1 90 ? -64.546 23.881 19.380 1.00 51.04 ? 90 MET A SD 1 ATOM 680 C CE . MET A 1 90 ? -63.248 24.789 18.650 1.00 47.62 ? 90 MET A CE 1 ATOM 681 N N . SER A 1 91 ? -66.264 21.211 14.698 1.00 45.86 ? 91 SER A N 1 ATOM 682 C CA . SER A 1 91 ? -66.238 19.936 14.014 1.00 45.77 ? 91 SER A CA 1 ATOM 683 C C . SER A 1 91 ? -64.933 19.800 13.254 1.00 43.78 ? 91 SER A C 1 ATOM 684 O O . SER A 1 91 ? -64.359 20.795 12.819 1.00 40.51 ? 91 SER A O 1 ATOM 685 C CB . SER A 1 91 ? -67.417 19.847 13.052 1.00 45.87 ? 91 SER A CB 1 ATOM 686 O OG . SER A 1 91 ? -67.505 18.565 12.486 1.00 46.51 ? 91 SER A OG 1 ATOM 687 N N . GLU A 1 92 ? -64.457 18.568 13.125 1.00 45.29 ? 92 GLU A N 1 ATOM 688 C CA . GLU A 1 92 ? -63.383 18.264 12.185 1.00 45.47 ? 92 GLU A CA 1 ATOM 689 C C . GLU A 1 92 ? -63.880 18.470 10.761 1.00 47.37 ? 92 GLU A C 1 ATOM 690 O O . GLU A 1 92 ? -63.097 18.793 9.864 1.00 47.94 ? 92 GLU A O 1 ATOM 691 C CB . GLU A 1 92 ? -62.886 16.838 12.356 1.00 45.54 ? 92 GLU A CB 1 ATOM 692 C CG . GLU A 1 92 ? -62.081 16.628 13.620 1.00 45.24 ? 92 GLU A CG 1 ATOM 693 C CD . GLU A 1 92 ? -61.228 15.385 13.534 1.00 46.33 ? 92 GLU A CD 1 ATOM 694 O OE1 . GLU A 1 92 ? -60.128 15.466 12.925 1.00 45.81 ? 92 GLU A OE1 1 ATOM 695 O OE2 . GLU A 1 92 ? -61.657 14.334 14.068 1.00 46.86 ? 92 GLU A OE2 1 ATOM 696 N N . ASP A 1 93 ? -65.184 18.273 10.560 1.00 49.32 ? 93 ASP A N 1 ATOM 697 C CA . ASP A 1 93 ? -65.830 18.626 9.304 1.00 48.81 ? 93 ASP A CA 1 ATOM 698 C C . ASP A 1 93 ? -65.983 20.146 9.254 1.00 48.05 ? 93 ASP A C 1 ATOM 699 O O . ASP A 1 93 ? -66.989 20.694 9.710 1.00 49.64 ? 93 ASP A O 1 ATOM 700 C CB . ASP A 1 93 ? -67.189 17.931 9.192 1.00 49.45 ? 93 ASP A CB 1 ATOM 701 C CG . ASP A 1 93 ? -67.799 18.048 7.808 1.00 50.23 ? 93 ASP A CG 1 ATOM 702 O OD1 . ASP A 1 93 ? -67.475 19.009 7.063 1.00 48.05 ? 93 ASP A OD1 1 ATOM 703 O OD2 . ASP A 1 93 ? -68.600 17.155 7.460 1.00 52.29 ? 93 ASP A OD2 1 ATOM 704 N N . CYS A 1 94 ? -64.981 20.824 8.708 1.00 46.95 ? 94 CYS A N 1 ATOM 705 C CA . CYS A 1 94 ? -64.952 22.289 8.767 1.00 46.89 ? 94 CYS A CA 1 ATOM 706 C C . CYS A 1 94 ? -64.351 23.012 7.569 1.00 45.87 ? 94 CYS A C 1 ATOM 707 O O . CYS A 1 94 ? -64.180 24.231 7.620 1.00 46.14 ? 94 CYS A O 1 ATOM 708 C CB . CYS A 1 94 ? -64.203 22.738 10.033 1.00 46.30 ? 94 CYS A CB 1 ATOM 709 S SG . CYS A 1 94 ? -62.438 22.341 10.078 1.00 45.36 ? 94 CYS A SG 1 ATOM 710 N N . LEU A 1 95 ? -64.047 22.302 6.489 1.00 45.80 ? 95 LEU A N 1 ATOM 711 C CA . LEU A 1 95 ? -63.425 22.953 5.340 1.00 44.88 ? 95 LEU A CA 1 ATOM 712 C C . LEU A 1 95 ? -64.501 23.516 4.427 1.00 44.18 ? 95 LEU A C 1 ATOM 713 O O . LEU A 1 95 ? -64.995 22.850 3.519 1.00 44.36 ? 95 LEU A O 1 ATOM 714 C CB . LEU A 1 95 ? -62.488 21.999 4.625 1.00 45.26 ? 95 LEU A CB 1 ATOM 715 C CG . LEU A 1 95 ? -61.386 21.534 5.576 1.00 46.38 ? 95 LEU A CG 1 ATOM 716 C CD1 . LEU A 1 95 ? -60.500 20.517 4.873 1.00 48.03 ? 95 LEU A CD1 1 ATOM 717 C CD2 . LEU A 1 95 ? -60.568 22.721 6.074 1.00 45.24 ? 95 LEU A CD2 1 ATOM 718 N N . TYR A 1 96 ? -64.886 24.750 4.735 1.00 42.88 ? 96 TYR A N 1 ATOM 719 C CA . TYR A 1 96 ? -65.890 25.474 3.990 1.00 42.44 ? 96 TYR A CA 1 ATOM 720 C C . TYR A 1 96 ? -65.430 26.891 3.776 1.00 41.36 ? 96 TYR A C 1 ATOM 721 O O . TYR A 1 96 ? -64.580 27.392 4.510 1.00 40.96 ? 96 TYR A O 1 ATOM 722 C CB . TYR A 1 96 ? -67.195 25.487 4.767 1.00 43.33 ? 96 TYR A CB 1 ATOM 723 C CG . TYR A 1 96 ? -67.726 24.111 5.020 1.00 44.28 ? 96 TYR A CG 1 ATOM 724 C CD1 . TYR A 1 96 ? -67.324 23.385 6.125 1.00 44.22 ? 96 TYR A CD1 1 ATOM 725 C CD2 . TYR A 1 96 ? -68.620 23.530 4.144 1.00 45.36 ? 96 TYR A CD2 1 ATOM 726 C CE1 . TYR A 1 96 ? -67.807 22.109 6.354 1.00 45.80 ? 96 TYR A CE1 1 ATOM 727 C CE2 . TYR A 1 96 ? -69.109 22.260 4.364 1.00 46.75 ? 96 TYR A CE2 1 ATOM 728 C CZ . TYR A 1 96 ? -68.700 21.555 5.463 1.00 46.36 ? 96 TYR A CZ 1 ATOM 729 O OH . TYR A 1 96 ? -69.196 20.296 5.653 1.00 48.51 ? 96 TYR A OH 1 ATOM 730 N N . LEU A 1 97 ? -66.002 27.540 2.773 1.00 42.00 ? 97 LEU A N 1 ATOM 731 C CA . LEU A 1 97 ? -65.772 28.953 2.569 1.00 42.47 ? 97 LEU A CA 1 ATOM 732 C C . LEU A 1 97 ? -67.091 29.674 2.381 1.00 43.68 ? 97 LEU A C 1 ATOM 733 O O . LEU A 1 97 ? -68.098 29.056 2.065 1.00 43.93 ? 97 LEU A O 1 ATOM 734 C CB . LEU A 1 97 ? -64.854 29.168 1.375 1.00 43.28 ? 97 LEU A CB 1 ATOM 735 C CG . LEU A 1 97 ? -65.275 28.569 0.030 1.00 45.10 ? 97 LEU A CG 1 ATOM 736 C CD1 . LEU A 1 97 ? -66.280 29.459 -0.690 1.00 47.28 ? 97 LEU A CD1 1 ATOM 737 C CD2 . LEU A 1 97 ? -64.054 28.343 -0.850 1.00 44.61 ? 97 LEU A CD2 1 ATOM 738 N N . ASN A 1 98 ? -67.068 30.987 2.590 1.00 44.46 ? 98 ASN A N 1 ATOM 739 C CA . ASN A 1 98 ? -68.249 31.833 2.467 1.00 45.51 ? 98 ASN A CA 1 ATOM 740 C C . ASN A 1 98 ? -68.012 32.919 1.450 1.00 45.15 ? 98 ASN A C 1 ATOM 741 O O . ASN A 1 98 ? -66.908 33.437 1.353 1.00 46.35 ? 98 ASN A O 1 ATOM 742 C CB . ASN A 1 98 ? -68.569 32.496 3.803 1.00 46.20 ? 98 ASN A CB 1 ATOM 743 C CG . ASN A 1 98 ? -68.480 31.533 4.963 1.00 46.15 ? 98 ASN A CG 1 ATOM 744 O OD1 . ASN A 1 98 ? -69.272 30.591 5.077 1.00 47.01 ? 98 ASN A OD1 1 ATOM 745 N ND2 . ASN A 1 98 ? -67.503 31.758 5.831 1.00 45.47 ? 98 ASN A ND2 1 ATOM 746 N N . ILE A 1 99 ? -69.052 33.281 0.707 1.00 46.62 ? 99 ILE A N 1 ATOM 747 C CA . ILE A 1 99 ? -68.935 34.292 -0.344 1.00 46.75 ? 99 ILE A CA 1 ATOM 748 C C . ILE A 1 99 ? -70.033 35.329 -0.216 1.00 47.83 ? 99 ILE A C 1 ATOM 749 O O . ILE A 1 99 ? -71.195 34.974 -0.087 1.00 49.94 ? 99 ILE A O 1 ATOM 750 C CB . ILE A 1 99 ? -69.025 33.667 -1.745 1.00 46.17 ? 99 ILE A CB 1 ATOM 751 C CG1 . ILE A 1 99 ? -68.112 32.438 -1.834 1.00 45.23 ? 99 ILE A CG1 1 ATOM 752 C CG2 . ILE A 1 99 ? -68.661 34.707 -2.793 1.00 45.89 ? 99 ILE A CG2 1 ATOM 753 C CD1 . ILE A 1 99 ? -68.358 31.561 -3.040 1.00 46.38 ? 99 ILE A CD1 1 ATOM 754 N N . TRP A 1 100 ? -69.655 36.602 -0.246 1.00 47.72 ? 100 TRP A N 1 ATOM 755 C CA . TRP A 1 100 ? -70.611 37.695 -0.250 1.00 49.31 ? 100 TRP A CA 1 ATOM 756 C C . TRP A 1 100 ? -70.583 38.377 -1.599 1.00 50.65 ? 100 TRP A C 1 ATOM 757 O O . TRP A 1 100 ? -69.550 38.893 -2.015 1.00 52.44 ? 100 TRP A O 1 ATOM 758 C CB . TRP A 1 100 ? -70.270 38.698 0.834 1.00 49.14 ? 100 TRP A CB 1 ATOM 759 C CG . TRP A 1 100 ? -70.746 38.271 2.147 1.00 49.56 ? 100 TRP A CG 1 ATOM 760 C CD1 . TRP A 1 100 ? -71.992 38.450 2.657 1.00 51.14 ? 100 TRP A CD1 1 ATOM 761 C CD2 . TRP A 1 100 ? -70.000 37.571 3.138 1.00 48.73 ? 100 TRP A CD2 1 ATOM 762 N NE1 . TRP A 1 100 ? -72.072 37.909 3.912 1.00 50.64 ? 100 TRP A NE1 1 ATOM 763 C CE2 . TRP A 1 100 ? -70.860 37.366 4.236 1.00 49.02 ? 100 TRP A CE2 1 ATOM 764 C CE3 . TRP A 1 100 ? -68.684 37.106 3.211 1.00 47.71 ? 100 TRP A CE3 1 ATOM 765 C CZ2 . TRP A 1 100 ? -70.450 36.716 5.396 1.00 47.97 ? 100 TRP A CZ2 1 ATOM 766 C CZ3 . TRP A 1 100 ? -68.278 36.452 4.365 1.00 47.39 ? 100 TRP A CZ3 1 ATOM 767 C CH2 . TRP A 1 100 ? -69.162 36.268 5.444 1.00 47.38 ? 100 TRP A CH2 1 ATOM 768 N N . VAL A 1 101 ? -71.722 38.382 -2.277 1.00 51.73 ? 101 VAL A N 1 ATOM 769 C CA . VAL A 1 101 ? -71.811 38.880 -3.643 1.00 53.36 ? 101 VAL A CA 1 ATOM 770 C C . VAL A 1 101 ? -72.765 40.065 -3.687 1.00 54.72 ? 101 VAL A C 1 ATOM 771 O O . VAL A 1 101 ? -73.837 40.012 -3.079 1.00 55.24 ? 101 VAL A O 1 ATOM 772 C CB . VAL A 1 101 ? -72.337 37.792 -4.601 1.00 54.40 ? 101 VAL A CB 1 ATOM 773 C CG1 . VAL A 1 101 ? -72.279 38.277 -6.040 1.00 56.40 ? 101 VAL A CG1 1 ATOM 774 C CG2 . VAL A 1 101 ? -71.546 36.505 -4.437 1.00 52.45 ? 101 VAL A CG2 1 ATOM 775 N N . PRO A 1 102 ? -72.382 41.137 -4.395 1.00 55.11 ? 102 PRO A N 1 ATOM 776 C CA . PRO A 1 102 ? -73.295 42.265 -4.537 1.00 58.30 ? 102 PRO A CA 1 ATOM 777 C C . PRO A 1 102 ? -74.569 41.935 -5.326 1.00 61.81 ? 102 PRO A C 1 ATOM 778 O O . PRO A 1 102 ? -74.669 40.876 -5.976 1.00 61.90 ? 102 PRO A O 1 ATOM 779 C CB . PRO A 1 102 ? -72.461 43.307 -5.287 1.00 58.00 ? 102 PRO A CB 1 ATOM 780 C CG . PRO A 1 102 ? -71.050 42.953 -4.998 1.00 55.66 ? 102 PRO A CG 1 ATOM 781 C CD . PRO A 1 102 ? -71.023 41.465 -4.856 1.00 54.30 ? 102 PRO A CD 1 ATOM 782 N N . SER A 1 103 ? -75.531 42.852 -5.253 1.00 64.46 ? 103 SER A N 1 ATOM 783 C CA . SER A 1 103 ? -76.793 42.709 -5.965 1.00 67.96 ? 103 SER A CA 1 ATOM 784 C C . SER A 1 103 ? -77.142 44.016 -6.697 1.00 69.52 ? 103 SER A C 1 ATOM 785 O O . SER A 1 103 ? -77.161 45.074 -6.082 1.00 70.59 ? 103 SER A O 1 ATOM 786 C CB . SER A 1 103 ? -77.906 42.314 -4.992 1.00 69.08 ? 103 SER A CB 1 ATOM 787 O OG . SER A 1 103 ? -79.105 42.042 -5.699 1.00 72.55 ? 103 SER A OG 1 ATOM 788 N N . PRO A 1 104 ? -77.401 43.967 -8.002 1.00 71.29 ? 104 PRO A N 1 ATOM 789 C CA . PRO A 1 104 ? -77.350 42.742 -8.810 1.00 70.85 ? 104 PRO A CA 1 ATOM 790 C C . PRO A 1 104 ? -75.946 42.148 -8.942 1.00 67.73 ? 104 PRO A C 1 ATOM 791 O O . PRO A 1 104 ? -74.945 42.858 -8.787 1.00 64.74 ? 104 PRO A O 1 ATOM 792 C CB . PRO A 1 104 ? -77.856 43.205 -10.181 1.00 73.11 ? 104 PRO A CB 1 ATOM 793 C CG . PRO A 1 104 ? -77.599 44.676 -10.208 1.00 74.29 ? 104 PRO A CG 1 ATOM 794 C CD . PRO A 1 104 ? -77.809 45.138 -8.795 1.00 73.59 ? 104 PRO A CD 1 ATOM 795 N N . ARG A 1 105 ? -75.905 40.846 -9.221 1.00 67.00 ? 105 ARG A N 1 ATOM 796 C CA . ARG A 1 105 ? -74.660 40.113 -9.448 1.00 64.43 ? 105 ARG A CA 1 ATOM 797 C C . ARG A 1 105 ? -73.771 40.814 -10.474 1.00 64.07 ? 105 ARG A C 1 ATOM 798 O O . ARG A 1 105 ? -74.233 41.172 -11.562 1.00 66.98 ? 105 ARG A O 1 ATOM 799 C CB . ARG A 1 105 ? -74.961 38.692 -9.939 1.00 64.73 ? 105 ARG A CB 1 ATOM 800 C CG . ARG A 1 105 ? -73.746 37.780 -9.965 1.00 63.97 ? 105 ARG A CG 1 ATOM 801 C CD . ARG A 1 105 ? -74.063 36.414 -10.535 1.00 65.01 ? 105 ARG A CD 1 ATOM 802 N NE . ARG A 1 105 ? -74.992 35.657 -9.699 1.00 66.68 ? 105 ARG A NE 1 ATOM 803 C CZ . ARG A 1 105 ? -75.518 34.475 -10.034 1.00 69.42 ? 105 ARG A CZ 1 ATOM 804 N NH1 . ARG A 1 105 ? -75.209 33.898 -11.192 1.00 71.18 ? 105 ARG A NH1 1 ATOM 805 N NH2 . ARG A 1 105 ? -76.361 33.858 -9.213 1.00 70.31 ? 105 ARG A NH2 1 ATOM 806 N N . PRO A 1 106 ? -72.491 41.011 -10.137 1.00 62.07 ? 106 PRO A N 1 ATOM 807 C CA . PRO A 1 106 ? -71.564 41.547 -11.133 1.00 62.69 ? 106 PRO A CA 1 ATOM 808 C C . PRO A 1 106 ? -71.174 40.487 -12.173 1.00 62.97 ? 106 PRO A C 1 ATOM 809 O O . PRO A 1 106 ? -71.512 39.316 -12.018 1.00 62.85 ? 106 PRO A O 1 ATOM 810 C CB . PRO A 1 106 ? -70.353 41.986 -10.293 1.00 60.64 ? 106 PRO A CB 1 ATOM 811 C CG . PRO A 1 106 ? -70.417 41.177 -9.047 1.00 58.52 ? 106 PRO A CG 1 ATOM 812 C CD . PRO A 1 106 ? -71.852 40.797 -8.824 1.00 59.92 ? 106 PRO A CD 1 ATOM 813 N N . LYS A 1 107 ? -70.476 40.899 -13.224 1.00 63.91 ? 107 LYS A N 1 ATOM 814 C CA . LYS A 1 107 ? -70.021 39.974 -14.257 1.00 64.72 ? 107 LYS A CA 1 ATOM 815 C C . LYS A 1 107 ? -68.592 39.496 -14.004 1.00 63.75 ? 107 LYS A C 1 ATOM 816 O O . LYS A 1 107 ? -68.317 38.301 -14.099 1.00 63.69 ? 107 LYS A O 1 ATOM 817 C CB . LYS A 1 107 ? -70.107 40.633 -15.632 1.00 67.46 ? 107 LYS A CB 1 ATOM 818 C CG . LYS A 1 107 ? -71.492 41.150 -16.002 1.00 70.69 ? 107 LYS A CG 1 ATOM 819 C CD . LYS A 1 107 ? -72.582 40.131 -15.690 1.00 72.02 ? 107 LYS A CD 1 ATOM 820 C CE . LYS A 1 107 ? -73.881 40.445 -16.413 1.00 75.47 ? 107 LYS A CE 1 ATOM 821 N NZ . LYS A 1 107 ? -74.401 41.808 -16.105 1.00 76.84 ? 107 LYS A NZ 1 ATOM 822 N N . SER A 1 108 ? -67.693 40.428 -13.684 1.00 63.21 ? 108 SER A N 1 ATOM 823 C CA . SER A 1 108 ? -66.267 40.135 -13.505 1.00 61.48 ? 108 SER A CA 1 ATOM 824 C C . SER A 1 108 ? -65.626 41.272 -12.708 1.00 60.77 ? 108 SER A C 1 ATOM 825 O O . SER A 1 108 ? -65.099 42.236 -13.277 1.00 61.79 ? 108 SER A O 1 ATOM 826 C CB . SER A 1 108 ? -65.576 39.968 -14.871 1.00 62.21 ? 108 SER A CB 1 ATOM 827 O OG . SER A 1 108 ? -64.315 39.324 -14.765 1.00 60.31 ? 108 SER A OG 1 ATOM 828 N N . THR A 1 109 ? -65.698 41.163 -11.387 1.00 58.53 ? 109 THR A N 1 ATOM 829 C CA . THR A 1 109 ? -65.237 42.229 -10.500 1.00 57.69 ? 109 THR A CA 1 ATOM 830 C C . THR A 1 109 ? -64.137 41.736 -9.553 1.00 54.45 ? 109 THR A C 1 ATOM 831 O O . THR A 1 109 ? -63.844 40.536 -9.473 1.00 53.60 ? 109 THR A O 1 ATOM 832 C CB . THR A 1 109 ? -66.415 42.843 -9.696 1.00 58.73 ? 109 THR A CB 1 ATOM 833 O OG1 . THR A 1 109 ? -66.044 44.125 -9.180 1.00 58.71 ? 109 THR A OG1 1 ATOM 834 C CG2 . THR A 1 109 ? -66.832 41.948 -8.532 1.00 57.90 ? 109 THR A CG2 1 ATOM 835 N N . THR A 1 110 ? -63.539 42.681 -8.837 1.00 51.81 ? 110 THR A N 1 ATOM 836 C CA . THR A 1 110 ? -62.437 42.395 -7.930 1.00 48.43 ? 110 THR A CA 1 ATOM 837 C C . THR A 1 110 ? -62.838 41.440 -6.800 1.00 46.25 ? 110 THR A C 1 ATOM 838 O O . THR A 1 110 ? -63.904 41.584 -6.203 1.00 45.97 ? 110 THR A O 1 ATOM 839 C CB . THR A 1 110 ? -61.921 43.697 -7.314 1.00 48.48 ? 110 THR A CB 1 ATOM 840 O OG1 . THR A 1 110 ? -61.546 44.604 -8.357 1.00 49.07 ? 110 THR A OG1 1 ATOM 841 C CG2 . THR A 1 110 ? -60.733 43.431 -6.422 1.00 48.12 ? 110 THR A CG2 1 ATOM 842 N N . VAL A 1 111 ? -61.970 40.472 -6.512 1.00 44.18 ? 111 VAL A N 1 ATOM 843 C CA . VAL A 1 111 ? -62.217 39.475 -5.476 1.00 42.59 ? 111 VAL A CA 1 ATOM 844 C C . VAL A 1 111 ? -61.229 39.656 -4.327 1.00 41.82 ? 111 VAL A C 1 ATOM 845 O O . VAL A 1 111 ? -60.037 39.867 -4.566 1.00 42.82 ? 111 VAL A O 1 ATOM 846 C CB . VAL A 1 111 ? -62.064 38.058 -6.048 1.00 41.70 ? 111 VAL A CB 1 ATOM 847 C CG1 . VAL A 1 111 ? -62.233 37.001 -4.954 1.00 40.25 ? 111 VAL A CG1 1 ATOM 848 C CG2 . VAL A 1 111 ? -63.063 37.850 -7.170 1.00 43.12 ? 111 VAL A CG2 1 ATOM 849 N N . MET A 1 112 ? -61.722 39.570 -3.090 1.00 40.59 ? 112 MET A N 1 ATOM 850 C CA . MET A 1 112 ? -60.864 39.602 -1.902 1.00 39.43 ? 112 MET A CA 1 ATOM 851 C C . MET A 1 112 ? -61.147 38.378 -1.057 1.00 39.76 ? 112 MET A C 1 ATOM 852 O O . MET A 1 112 ? -62.303 38.024 -0.835 1.00 41.99 ? 112 MET A O 1 ATOM 853 C CB . MET A 1 112 ? -61.103 40.860 -1.080 1.00 39.37 ? 112 MET A CB 1 ATOM 854 C CG . MET A 1 112 ? -60.777 42.142 -1.820 1.00 40.65 ? 112 MET A CG 1 ATOM 855 S SD . MET A 1 112 ? -61.107 43.616 -0.836 1.00 40.73 ? 112 MET A SD 1 ATOM 856 C CE . MET A 1 112 ? -59.825 43.476 0.402 1.00 40.13 ? 112 MET A CE 1 ATOM 857 N N . VAL A 1 113 ? -60.090 37.727 -0.591 1.00 39.83 ? 113 VAL A N 1 ATOM 858 C CA . VAL A 1 113 ? -60.222 36.459 0.101 1.00 40.43 ? 113 VAL A CA 1 ATOM 859 C C . VAL A 1 113 ? -59.562 36.553 1.462 1.00 41.09 ? 113 VAL A C 1 ATOM 860 O O . VAL A 1 113 ? -58.344 36.698 1.557 1.00 41.71 ? 113 VAL A O 1 ATOM 861 C CB . VAL A 1 113 ? -59.600 35.314 -0.707 1.00 39.95 ? 113 VAL A CB 1 ATOM 862 C CG1 . VAL A 1 113 ? -59.884 33.965 -0.041 1.00 39.11 ? 113 VAL A CG1 1 ATOM 863 C CG2 . VAL A 1 113 ? -60.138 35.354 -2.128 1.00 40.47 ? 113 VAL A CG2 1 ATOM 864 N N . TRP A 1 114 ? -60.390 36.456 2.500 1.00 41.24 ? 114 TRP A N 1 ATOM 865 C CA . TRP A 1 114 ? -59.969 36.647 3.875 1.00 40.35 ? 114 TRP A CA 1 ATOM 866 C C . TRP A 1 114 ? -59.445 35.354 4.465 1.00 40.11 ? 114 TRP A C 1 ATOM 867 O O . TRP A 1 114 ? -60.128 34.329 4.420 1.00 40.15 ? 114 TRP A O 1 ATOM 868 C CB . TRP A 1 114 ? -61.145 37.144 4.723 1.00 40.48 ? 114 TRP A CB 1 ATOM 869 C CG . TRP A 1 114 ? -60.834 37.266 6.172 1.00 38.83 ? 114 TRP A CG 1 ATOM 870 C CD1 . TRP A 1 114 ? -61.348 36.520 7.183 1.00 39.56 ? 114 TRP A CD1 1 ATOM 871 C CD2 . TRP A 1 114 ? -59.924 38.179 6.770 1.00 38.53 ? 114 TRP A CD2 1 ATOM 872 N NE1 . TRP A 1 114 ? -60.818 36.913 8.391 1.00 39.21 ? 114 TRP A NE1 1 ATOM 873 C CE2 . TRP A 1 114 ? -59.938 37.935 8.163 1.00 38.40 ? 114 TRP A CE2 1 ATOM 874 C CE3 . TRP A 1 114 ? -59.102 39.186 6.270 1.00 38.76 ? 114 TRP A CE3 1 ATOM 875 C CZ2 . TRP A 1 114 ? -59.169 38.662 9.056 1.00 37.27 ? 114 TRP A CZ2 1 ATOM 876 C CZ3 . TRP A 1 114 ? -58.332 39.910 7.158 1.00 39.77 ? 114 TRP A CZ3 1 ATOM 877 C CH2 . TRP A 1 114 ? -58.367 39.639 8.541 1.00 38.89 ? 114 TRP A CH2 1 ATOM 878 N N . ILE A 1 115 ? -58.240 35.422 5.036 1.00 41.19 ? 115 ILE A N 1 ATOM 879 C CA . ILE A 1 115 ? -57.664 34.316 5.817 1.00 41.45 ? 115 ILE A CA 1 ATOM 880 C C . ILE A 1 115 ? -57.524 34.714 7.292 1.00 40.85 ? 115 ILE A C 1 ATOM 881 O O . ILE A 1 115 ? -56.708 35.558 7.653 1.00 40.54 ? 115 ILE A O 1 ATOM 882 C CB . ILE A 1 115 ? -56.303 33.879 5.267 1.00 41.45 ? 115 ILE A CB 1 ATOM 883 C CG1 . ILE A 1 115 ? -56.386 33.687 3.751 1.00 42.75 ? 115 ILE A CG1 1 ATOM 884 C CG2 . ILE A 1 115 ? -55.869 32.587 5.940 1.00 42.21 ? 115 ILE A CG2 1 ATOM 885 C CD1 . ILE A 1 115 ? -55.082 33.266 3.114 1.00 42.98 ? 115 ILE A CD1 1 ATOM 886 N N . TYR A 1 116 ? -58.333 34.094 8.140 1.00 41.52 ? 116 TYR A N 1 ATOM 887 C CA . TYR A 1 116 ? -58.411 34.491 9.524 1.00 41.54 ? 116 TYR A CA 1 ATOM 888 C C . TYR A 1 116 ? -57.135 34.195 10.300 1.00 41.34 ? 116 TYR A C 1 ATOM 889 O O . TYR A 1 116 ? -56.336 33.338 9.907 1.00 39.70 ? 116 TYR A O 1 ATOM 890 C CB . TYR A 1 116 ? -59.615 33.841 10.206 1.00 42.89 ? 116 TYR A CB 1 ATOM 891 C CG . TYR A 1 116 ? -59.655 32.321 10.223 1.00 42.41 ? 116 TYR A CG 1 ATOM 892 C CD1 . TYR A 1 116 ? -58.725 31.571 10.935 1.00 42.54 ? 116 TYR A CD1 1 ATOM 893 C CD2 . TYR A 1 116 ? -60.672 31.638 9.573 1.00 43.70 ? 116 TYR A CD2 1 ATOM 894 C CE1 . TYR A 1 116 ? -58.796 30.184 10.972 1.00 42.55 ? 116 TYR A CE1 1 ATOM 895 C CE2 . TYR A 1 116 ? -60.750 30.258 9.606 1.00 42.83 ? 116 TYR A CE2 1 ATOM 896 C CZ . TYR A 1 116 ? -59.813 29.536 10.300 1.00 42.10 ? 116 TYR A CZ 1 ATOM 897 O OH . TYR A 1 116 ? -59.904 28.168 10.308 1.00 41.77 ? 116 TYR A OH 1 ATOM 898 N N . GLY A 1 117 ? -56.963 34.916 11.408 1.00 41.61 ? 117 GLY A N 1 ATOM 899 C CA . GLY A 1 117 ? -55.851 34.684 12.320 1.00 40.86 ? 117 GLY A CA 1 ATOM 900 C C . GLY A 1 117 ? -56.252 33.754 13.448 1.00 41.02 ? 117 GLY A C 1 ATOM 901 O O . GLY A 1 117 ? -57.230 33.003 13.344 1.00 39.87 ? 117 GLY A O 1 ATOM 902 N N . GLY A 1 118 ? -55.493 33.828 14.536 1.00 40.92 ? 118 GLY A N 1 ATOM 903 C CA . GLY A 1 118 ? -55.666 32.947 15.690 1.00 39.29 ? 118 GLY A CA 1 ATOM 904 C C . GLY A 1 118 ? -54.433 32.127 16.036 1.00 39.01 ? 118 GLY A C 1 ATOM 905 O O . GLY A 1 118 ? -54.554 31.052 16.619 1.00 39.69 ? 118 GLY A O 1 ATOM 906 N N . GLY A 1 119 ? -53.247 32.618 15.672 1.00 38.15 ? 119 GLY A N 1 ATOM 907 C CA . GLY A 1 119 ? -51.986 31.969 16.051 1.00 37.04 ? 119 GLY A CA 1 ATOM 908 C C . GLY A 1 119 ? -51.792 30.550 15.551 1.00 35.97 ? 119 GLY A C 1 ATOM 909 O O . GLY A 1 119 ? -50.973 29.796 16.095 1.00 36.73 ? 119 GLY A O 1 ATOM 910 N N . PHE A 1 120 ? -52.546 30.188 14.517 1.00 35.87 ? 120 PHE A N 1 ATOM 911 C CA . PHE A 1 120 ? -52.570 28.823 13.959 1.00 36.03 ? 120 PHE A CA 1 ATOM 912 C C . PHE A 1 120 ? -53.183 27.770 14.893 1.00 36.17 ? 120 PHE A C 1 ATOM 913 O O . PHE A 1 120 ? -53.257 26.605 14.505 1.00 36.56 ? 120 PHE A O 1 ATOM 914 C CB . PHE A 1 120 ? -51.171 28.348 13.502 1.00 35.55 ? 120 PHE A CB 1 ATOM 915 C CG . PHE A 1 120 ? -50.595 29.128 12.352 1.00 35.56 ? 120 PHE A CG 1 ATOM 916 C CD1 . PHE A 1 120 ? -51.095 28.978 11.071 1.00 36.06 ? 120 PHE A CD1 1 ATOM 917 C CD2 . PHE A 1 120 ? -49.529 29.983 12.541 1.00 35.67 ? 120 PHE A CD2 1 ATOM 918 C CE1 . PHE A 1 120 ? -50.556 29.685 10.006 1.00 35.59 ? 120 PHE A CE1 1 ATOM 919 C CE2 . PHE A 1 120 ? -48.986 30.689 11.479 1.00 35.17 ? 120 PHE A CE2 1 ATOM 920 C CZ . PHE A 1 120 ? -49.502 30.540 10.212 1.00 35.19 ? 120 PHE A CZ 1 ATOM 921 N N . TYR A 1 121 ? -53.623 28.159 16.097 1.00 36.40 ? 121 TYR A N 1 ATOM 922 C CA . TYR A 1 121 ? -54.267 27.219 17.051 1.00 36.74 ? 121 TYR A CA 1 ATOM 923 C C . TYR A 1 121 ? -55.784 27.413 17.167 1.00 37.03 ? 121 TYR A C 1 ATOM 924 O O . TYR A 1 121 ? -56.460 26.623 17.838 1.00 41.38 ? 121 TYR A O 1 ATOM 925 C CB . TYR A 1 121 ? -53.637 27.331 18.446 1.00 36.53 ? 121 TYR A CB 1 ATOM 926 C CG . TYR A 1 121 ? -53.979 28.610 19.186 1.00 36.67 ? 121 TYR A CG 1 ATOM 927 C CD1 . TYR A 1 121 ? -55.153 28.703 19.947 1.00 37.82 ? 121 TYR A CD1 1 ATOM 928 C CD2 . TYR A 1 121 ? -53.140 29.721 19.128 1.00 35.56 ? 121 TYR A CD2 1 ATOM 929 C CE1 . TYR A 1 121 ? -55.487 29.862 20.620 1.00 38.15 ? 121 TYR A CE1 1 ATOM 930 C CE2 . TYR A 1 121 ? -53.464 30.886 19.796 1.00 37.12 ? 121 TYR A CE2 1 ATOM 931 C CZ . TYR A 1 121 ? -54.638 30.945 20.545 1.00 38.63 ? 121 TYR A CZ 1 ATOM 932 O OH . TYR A 1 121 ? -54.982 32.086 21.218 1.00 39.70 ? 121 TYR A OH 1 ATOM 933 N N . SER A 1 122 ? -56.300 28.452 16.513 1.00 35.61 ? 122 SER A N 1 ATOM 934 C CA . SER A 1 122 ? -57.670 28.908 16.685 1.00 36.27 ? 122 SER A CA 1 ATOM 935 C C . SER A 1 122 ? -58.061 29.732 15.484 1.00 36.19 ? 122 SER A C 1 ATOM 936 O O . SER A 1 122 ? -57.223 30.023 14.637 1.00 35.33 ? 122 SER A O 1 ATOM 937 C CB . SER A 1 122 ? -57.795 29.780 17.942 1.00 36.56 ? 122 SER A CB 1 ATOM 938 O OG . SER A 1 122 ? -56.934 30.910 17.890 1.00 34.40 ? 122 SER A OG 1 ATOM 939 N N . GLY A 1 123 ? -59.329 30.125 15.425 1.00 37.92 ? 123 GLY A N 1 ATOM 940 C CA . GLY A 1 123 ? -59.829 30.985 14.349 1.00 38.76 ? 123 GLY A CA 1 ATOM 941 C C . GLY A 1 123 ? -61.097 30.446 13.715 1.00 39.35 ? 123 GLY A C 1 ATOM 942 O O . GLY A 1 123 ? -61.348 29.242 13.730 1.00 38.77 ? 123 GLY A O 1 ATOM 943 N N . SER A 1 124 ? -61.897 31.351 13.163 1.00 39.82 ? 124 SER A N 1 ATOM 944 C CA . SER A 1 124 ? -63.137 30.984 12.499 1.00 41.44 ? 124 SER A CA 1 ATOM 945 C C . SER A 1 124 ? -63.414 31.911 11.321 1.00 42.11 ? 124 SER A C 1 ATOM 946 O O . SER A 1 124 ? -63.133 33.097 11.369 1.00 43.02 ? 124 SER A O 1 ATOM 947 C CB . SER A 1 124 ? -64.293 31.040 13.491 1.00 43.65 ? 124 SER A CB 1 ATOM 948 O OG . SER A 1 124 ? -64.243 29.957 14.412 1.00 44.39 ? 124 SER A OG 1 ATOM 949 N N . SER A 1 125 ? -63.962 31.359 10.250 1.00 43.74 ? 125 SER A N 1 ATOM 950 C CA . SER A 1 125 ? -64.366 32.173 9.113 1.00 44.74 ? 125 SER A CA 1 ATOM 951 C C . SER A 1 125 ? -65.644 32.961 9.411 1.00 46.09 ? 125 SER A C 1 ATOM 952 O O . SER A 1 125 ? -65.972 33.902 8.695 1.00 49.85 ? 125 SER A O 1 ATOM 953 C CB . SER A 1 125 ? -64.596 31.279 7.893 1.00 45.47 ? 125 SER A CB 1 ATOM 954 O OG . SER A 1 125 ? -65.807 30.547 7.999 1.00 46.03 ? 125 SER A OG 1 ATOM 955 N N . THR A 1 126 ? -66.329 32.582 10.487 1.00 45.26 ? 126 THR A N 1 ATOM 956 C CA . THR A 1 126 ? -67.716 32.936 10.734 1.00 45.22 ? 126 THR A CA 1 ATOM 957 C C . THR A 1 126 ? -67.930 33.991 11.827 1.00 45.36 ? 126 THR A C 1 ATOM 958 O O . THR A 1 126 ? -69.050 34.211 12.246 1.00 46.18 ? 126 THR A O 1 ATOM 959 C CB . THR A 1 126 ? -68.470 31.671 11.180 1.00 44.90 ? 126 THR A CB 1 ATOM 960 O OG1 . THR A 1 126 ? -67.918 31.202 12.412 1.00 43.60 ? 126 THR A OG1 1 ATOM 961 C CG2 . THR A 1 126 ? -68.323 30.582 10.158 1.00 44.42 ? 126 THR A CG2 1 ATOM 962 N N . LEU A 1 127 ? -66.870 34.643 12.292 1.00 45.35 ? 127 LEU A N 1 ATOM 963 C CA . LEU A 1 127 ? -66.993 35.584 13.405 1.00 44.40 ? 127 LEU A CA 1 ATOM 964 C C . LEU A 1 127 ? -67.730 36.832 12.961 1.00 45.59 ? 127 LEU A C 1 ATOM 965 O O . LEU A 1 127 ? -67.594 37.250 11.820 1.00 45.46 ? 127 LEU A O 1 ATOM 966 C CB . LEU A 1 127 ? -65.615 35.984 13.929 1.00 42.30 ? 127 LEU A CB 1 ATOM 967 C CG . LEU A 1 127 ? -64.704 34.868 14.446 1.00 41.82 ? 127 LEU A CG 1 ATOM 968 C CD1 . LEU A 1 127 ? -63.433 35.469 15.029 1.00 41.58 ? 127 LEU A CD1 1 ATOM 969 C CD2 . LEU A 1 127 ? -65.394 34.005 15.484 1.00 42.29 ? 127 LEU A CD2 1 ATOM 970 N N . ASP A 1 128 ? -68.498 37.435 13.866 1.00 48.75 ? 128 ASP A N 1 ATOM 971 C CA . ASP A 1 128 ? -69.165 38.708 13.577 1.00 51.36 ? 128 ASP A CA 1 ATOM 972 C C . ASP A 1 128 ? -68.179 39.674 12.911 1.00 51.73 ? 128 ASP A C 1 ATOM 973 O O . ASP A 1 128 ? -68.439 40.212 11.827 1.00 53.30 ? 128 ASP A O 1 ATOM 974 C CB . ASP A 1 128 ? -69.740 39.337 14.854 1.00 52.12 ? 128 ASP A CB 1 ATOM 975 C CG . ASP A 1 128 ? -70.998 38.619 15.357 1.00 54.53 ? 128 ASP A CG 1 ATOM 976 O OD1 . ASP A 1 128 ? -71.525 37.745 14.643 1.00 55.45 ? 128 ASP A OD1 1 ATOM 977 O OD2 . ASP A 1 128 ? -71.466 38.930 16.476 1.00 55.11 ? 128 ASP A OD2 1 ATOM 978 N N . VAL A 1 129 ? -67.024 39.840 13.544 1.00 49.59 ? 129 VAL A N 1 ATOM 979 C CA . VAL A 1 129 ? -66.028 40.794 13.085 1.00 48.19 ? 129 VAL A CA 1 ATOM 980 C C . VAL A 1 129 ? -65.501 40.544 11.655 1.00 47.28 ? 129 VAL A C 1 ATOM 981 O O . VAL A 1 129 ? -64.942 41.456 11.050 1.00 47.77 ? 129 VAL A O 1 ATOM 982 C CB . VAL A 1 129 ? -64.861 40.864 14.097 1.00 47.12 ? 129 VAL A CB 1 ATOM 983 C CG1 . VAL A 1 129 ? -63.982 39.620 14.006 1.00 45.82 ? 129 VAL A CG1 1 ATOM 984 C CG2 . VAL A 1 129 ? -64.052 42.134 13.904 1.00 46.75 ? 129 VAL A CG2 1 ATOM 985 N N . TYR A 1 130 ? -65.660 39.327 11.120 1.00 46.39 ? 130 TYR A N 1 ATOM 986 C CA . TYR A 1 130 ? -65.297 39.043 9.717 1.00 44.92 ? 130 TYR A CA 1 ATOM 987 C C . TYR A 1 130 ? -66.520 38.933 8.799 1.00 45.12 ? 130 TYR A C 1 ATOM 988 O O . TYR A 1 130 ? -66.458 38.275 7.765 1.00 46.84 ? 130 TYR A O 1 ATOM 989 C CB . TYR A 1 130 ? -64.500 37.735 9.576 1.00 43.92 ? 130 TYR A CB 1 ATOM 990 C CG . TYR A 1 130 ? -63.326 37.523 10.512 1.00 43.09 ? 130 TYR A CG 1 ATOM 991 C CD1 . TYR A 1 130 ? -62.458 38.558 10.847 1.00 41.55 ? 130 TYR A CD1 1 ATOM 992 C CD2 . TYR A 1 130 ? -63.062 36.250 11.026 1.00 42.65 ? 130 TYR A CD2 1 ATOM 993 C CE1 . TYR A 1 130 ? -61.390 38.336 11.701 1.00 40.48 ? 130 TYR A CE1 1 ATOM 994 C CE2 . TYR A 1 130 ? -62.000 36.020 11.869 1.00 40.95 ? 130 TYR A CE2 1 ATOM 995 C CZ . TYR A 1 130 ? -61.167 37.060 12.209 1.00 41.27 ? 130 TYR A CZ 1 ATOM 996 O OH . TYR A 1 130 ? -60.100 36.807 13.055 1.00 40.76 ? 130 TYR A OH 1 ATOM 997 N N . ASN A 1 131 ? -67.636 39.551 9.160 1.00 45.58 ? 131 ASN A N 1 ATOM 998 C CA . ASN A 1 131 ? -68.795 39.542 8.278 1.00 46.38 ? 131 ASN A CA 1 ATOM 999 C C . ASN A 1 131 ? -68.502 40.402 7.059 1.00 46.84 ? 131 ASN A C 1 ATOM 1000 O O . ASN A 1 131 ? -68.409 41.623 7.157 1.00 46.89 ? 131 ASN A O 1 ATOM 1001 C CB . ASN A 1 131 ? -70.023 40.065 9.002 1.00 47.46 ? 131 ASN A CB 1 ATOM 1002 C CG . ASN A 1 131 ? -71.314 39.683 8.319 1.00 48.16 ? 131 ASN A CG 1 ATOM 1003 O OD1 . ASN A 1 131 ? -71.374 39.462 7.101 1.00 47.93 ? 131 ASN A OD1 1 ATOM 1004 N ND2 . ASN A 1 131 ? -72.369 39.610 9.113 1.00 49.14 ? 131 ASN A ND2 1 ATOM 1005 N N . GLY A 1 132 ? -68.356 39.756 5.909 1.00 47.21 ? 132 GLY A N 1 ATOM 1006 C CA . GLY A 1 132 ? -67.927 40.440 4.689 1.00 47.84 ? 132 GLY A CA 1 ATOM 1007 C C . GLY A 1 132 ? -68.997 41.200 3.924 1.00 49.14 ? 132 GLY A C 1 ATOM 1008 O O . GLY A 1 132 ? -68.736 41.686 2.828 1.00 48.74 ? 132 GLY A O 1 ATOM 1009 N N . LYS A 1 133 ? -70.196 41.323 4.483 1.00 51.13 ? 133 LYS A N 1 ATOM 1010 C CA . LYS A 1 133 ? -71.274 41.985 3.756 1.00 54.26 ? 133 LYS A CA 1 ATOM 1011 C C . LYS A 1 133 ? -71.057 43.486 3.623 1.00 55.39 ? 133 LYS A C 1 ATOM 1012 O O . LYS A 1 133 ? -71.362 44.055 2.577 1.00 57.61 ? 133 LYS A O 1 ATOM 1013 C CB . LYS A 1 133 ? -72.636 41.682 4.377 1.00 55.15 ? 133 LYS A CB 1 ATOM 1014 C CG . LYS A 1 133 ? -72.925 42.372 5.694 1.00 55.84 ? 133 LYS A CG 1 ATOM 1015 C CD . LYS A 1 133 ? -74.012 41.601 6.427 1.00 57.07 ? 133 LYS A CD 1 ATOM 1016 C CE . LYS A 1 133 ? -74.781 42.449 7.424 1.00 58.12 ? 133 LYS A CE 1 ATOM 1017 N NZ . LYS A 1 133 ? -76.010 41.730 7.867 1.00 58.99 ? 133 LYS A NZ 1 ATOM 1018 N N . TYR A 1 134 ? -70.506 44.122 4.652 1.00 54.30 ? 134 TYR A N 1 ATOM 1019 C CA . TYR A 1 134 ? -70.328 45.578 4.618 1.00 54.97 ? 134 TYR A CA 1 ATOM 1020 C C . TYR A 1 134 ? -69.329 45.931 3.536 1.00 54.19 ? 134 TYR A C 1 ATOM 1021 O O . TYR A 1 134 ? -69.540 46.859 2.751 1.00 56.64 ? 134 TYR A O 1 ATOM 1022 C CB . TYR A 1 134 ? -69.861 46.126 5.968 1.00 54.28 ? 134 TYR A CB 1 ATOM 1023 C CG . TYR A 1 134 ? -70.770 45.730 7.104 1.00 54.86 ? 134 TYR A CG 1 ATOM 1024 C CD1 . TYR A 1 134 ? -72.014 46.318 7.255 1.00 57.42 ? 134 TYR A CD1 1 ATOM 1025 C CD2 . TYR A 1 134 ? -70.399 44.741 8.008 1.00 53.49 ? 134 TYR A CD2 1 ATOM 1026 C CE1 . TYR A 1 134 ? -72.863 45.947 8.286 1.00 58.47 ? 134 TYR A CE1 1 ATOM 1027 C CE2 . TYR A 1 134 ? -71.240 44.359 9.038 1.00 53.93 ? 134 TYR A CE2 1 ATOM 1028 C CZ . TYR A 1 134 ? -72.471 44.966 9.173 1.00 56.23 ? 134 TYR A CZ 1 ATOM 1029 O OH . TYR A 1 134 ? -73.314 44.604 10.197 1.00 55.94 ? 134 TYR A OH 1 ATOM 1030 N N . LEU A 1 135 ? -68.255 45.157 3.479 1.00 51.16 ? 135 LEU A N 1 ATOM 1031 C CA . LEU A 1 135 ? -67.199 45.382 2.508 1.00 49.88 ? 135 LEU A CA 1 ATOM 1032 C C . LEU A 1 135 ? -67.723 45.078 1.104 1.00 51.21 ? 135 LEU A C 1 ATOM 1033 O O . LEU A 1 135 ? -67.619 45.911 0.197 1.00 51.82 ? 135 LEU A O 1 ATOM 1034 C CB . LEU A 1 135 ? -65.991 44.509 2.869 1.00 47.77 ? 135 LEU A CB 1 ATOM 1035 C CG . LEU A 1 135 ? -64.607 44.850 2.329 1.00 46.53 ? 135 LEU A CG 1 ATOM 1036 C CD1 . LEU A 1 135 ? -64.301 46.334 2.392 1.00 47.45 ? 135 LEU A CD1 1 ATOM 1037 C CD2 . LEU A 1 135 ? -63.582 44.065 3.122 1.00 44.76 ? 135 LEU A CD2 1 ATOM 1038 N N . ALA A 1 136 ? -68.319 43.898 0.936 1.00 51.13 ? 136 ALA A N 1 ATOM 1039 C CA . ALA A 1 136 ? -68.892 43.505 -0.350 1.00 51.78 ? 136 ALA A CA 1 ATOM 1040 C C . ALA A 1 136 ? -69.815 44.598 -0.875 1.00 54.49 ? 136 ALA A C 1 ATOM 1041 O O . ALA A 1 136 ? -69.700 45.032 -2.023 1.00 56.18 ? 136 ALA A O 1 ATOM 1042 C CB . ALA A 1 136 ? -69.652 42.190 -0.219 1.00 51.37 ? 136 ALA A CB 1 ATOM 1043 N N . TYR A 1 137 ? -70.721 45.054 -0.017 1.00 54.99 ? 137 TYR A N 1 ATOM 1044 C CA . TYR A 1 137 ? -71.695 46.066 -0.407 1.00 55.78 ? 137 TYR A CA 1 ATOM 1045 C C . TYR A 1 137 ? -71.025 47.416 -0.675 1.00 56.26 ? 137 TYR A C 1 ATOM 1046 O O . TYR A 1 137 ? -71.248 48.017 -1.716 1.00 57.91 ? 137 TYR A O 1 ATOM 1047 C CB . TYR A 1 137 ? -72.785 46.187 0.662 1.00 55.93 ? 137 TYR A CB 1 ATOM 1048 C CG . TYR A 1 137 ? -73.707 47.361 0.489 1.00 58.12 ? 137 TYR A CG 1 ATOM 1049 C CD1 . TYR A 1 137 ? -74.718 47.348 -0.474 1.00 60.32 ? 137 TYR A CD1 1 ATOM 1050 C CD2 . TYR A 1 137 ? -73.577 48.493 1.290 1.00 58.86 ? 137 TYR A CD2 1 ATOM 1051 C CE1 . TYR A 1 137 ? -75.566 48.433 -0.637 1.00 62.01 ? 137 TYR A CE1 1 ATOM 1052 C CE2 . TYR A 1 137 ? -74.423 49.581 1.137 1.00 61.08 ? 137 TYR A CE2 1 ATOM 1053 C CZ . TYR A 1 137 ? -75.413 49.543 0.177 1.00 62.52 ? 137 TYR A CZ 1 ATOM 1054 O OH . TYR A 1 137 ? -76.247 50.616 0.040 1.00 65.09 ? 137 TYR A OH 1 ATOM 1055 N N . THR A 1 138 ? -70.181 47.883 0.238 1.00 55.44 ? 138 THR A N 1 ATOM 1056 C CA . THR A 1 138 ? -69.668 49.246 0.125 1.00 56.05 ? 138 THR A CA 1 ATOM 1057 C C . THR A 1 138 ? -68.700 49.407 -1.040 1.00 55.68 ? 138 THR A C 1 ATOM 1058 O O . THR A 1 138 ? -68.824 50.351 -1.813 1.00 55.88 ? 138 THR A O 1 ATOM 1059 C CB . THR A 1 138 ? -69.000 49.720 1.428 1.00 55.14 ? 138 THR A CB 1 ATOM 1060 O OG1 . THR A 1 138 ? -69.901 49.520 2.522 1.00 55.31 ? 138 THR A OG1 1 ATOM 1061 C CG2 . THR A 1 138 ? -68.650 51.203 1.342 1.00 56.51 ? 138 THR A CG2 1 ATOM 1062 N N . GLU A 1 139 ? -67.749 48.486 -1.168 1.00 54.31 ? 139 GLU A N 1 ATOM 1063 C CA . GLU A 1 139 ? -66.722 48.584 -2.209 1.00 55.43 ? 139 GLU A CA 1 ATOM 1064 C C . GLU A 1 139 ? -67.053 47.809 -3.482 1.00 56.47 ? 139 GLU A C 1 ATOM 1065 O O . GLU A 1 139 ? -66.271 47.836 -4.430 1.00 56.04 ? 139 GLU A O 1 ATOM 1066 C CB . GLU A 1 139 ? -65.378 48.110 -1.663 1.00 54.84 ? 139 GLU A CB 1 ATOM 1067 C CG . GLU A 1 139 ? -64.879 48.924 -0.471 1.00 55.03 ? 139 GLU A CG 1 ATOM 1068 C CD . GLU A 1 139 ? -64.633 50.369 -0.828 1.00 55.84 ? 139 GLU A CD 1 ATOM 1069 O OE1 . GLU A 1 139 ? -64.227 50.626 -1.984 1.00 56.79 ? 139 GLU A OE1 1 ATOM 1070 O OE2 . GLU A 1 139 ? -64.845 51.241 0.039 1.00 55.85 ? 139 GLU A OE2 1 ATOM 1071 N N . GLU A 1 140 ? -68.199 47.123 -3.497 1.00 57.11 ? 140 GLU A N 1 ATOM 1072 C CA . GLU A 1 140 ? -68.669 46.387 -4.671 1.00 58.39 ? 140 GLU A CA 1 ATOM 1073 C C . GLU A 1 140 ? -67.633 45.379 -5.142 1.00 55.73 ? 140 GLU A C 1 ATOM 1074 O O . GLU A 1 140 ? -67.160 45.403 -6.280 1.00 54.59 ? 140 GLU A O 1 ATOM 1075 C CB . GLU A 1 140 ? -69.080 47.351 -5.775 1.00 62.34 ? 140 GLU A CB 1 ATOM 1076 C CG . GLU A 1 140 ? -69.948 48.468 -5.227 1.00 65.94 ? 140 GLU A CG 1 ATOM 1077 C CD . GLU A 1 140 ? -70.897 49.025 -6.251 1.00 69.79 ? 140 GLU A CD 1 ATOM 1078 O OE1 . GLU A 1 140 ? -70.417 49.527 -7.290 1.00 71.65 ? 140 GLU A OE1 1 ATOM 1079 O OE2 . GLU A 1 140 ? -72.119 48.959 -6.003 1.00 71.77 ? 140 GLU A OE2 1 ATOM 1080 N N . VAL A 1 141 ? -67.307 44.489 -4.215 1.00 53.78 ? 141 VAL A N 1 ATOM 1081 C CA . VAL A 1 141 ? -66.342 43.426 -4.422 1.00 51.75 ? 141 VAL A CA 1 ATOM 1082 C C . VAL A 1 141 ? -66.980 42.110 -4.023 1.00 51.05 ? 141 VAL A C 1 ATOM 1083 O O . VAL A 1 141 ? -67.936 42.076 -3.242 1.00 50.33 ? 141 VAL A O 1 ATOM 1084 C CB . VAL A 1 141 ? -65.070 43.646 -3.578 1.00 50.73 ? 141 VAL A CB 1 ATOM 1085 C CG1 . VAL A 1 141 ? -64.338 44.901 -4.043 1.00 51.88 ? 141 VAL A CG1 1 ATOM 1086 C CG2 . VAL A 1 141 ? -65.391 43.734 -2.087 1.00 49.19 ? 141 VAL A CG2 1 ATOM 1087 N N . VAL A 1 142 ? -66.463 41.026 -4.579 1.00 50.27 ? 142 VAL A N 1 ATOM 1088 C CA . VAL A 1 142 ? -66.857 39.704 -4.134 1.00 49.92 ? 142 VAL A CA 1 ATOM 1089 C C . VAL A 1 142 ? -65.909 39.339 -3.008 1.00 48.97 ? 142 VAL A C 1 ATOM 1090 O O . VAL A 1 142 ? -64.712 39.225 -3.227 1.00 48.84 ? 142 VAL A O 1 ATOM 1091 C CB . VAL A 1 142 ? -66.782 38.685 -5.275 1.00 49.11 ? 142 VAL A CB 1 ATOM 1092 C CG1 . VAL A 1 142 ? -67.064 37.283 -4.766 1.00 48.12 ? 142 VAL A CG1 1 ATOM 1093 C CG2 . VAL A 1 142 ? -67.767 39.076 -6.367 1.00 51.00 ? 142 VAL A CG2 1 ATOM 1094 N N . LEU A 1 143 ? -66.452 39.184 -1.805 1.00 50.01 ? 143 LEU A N 1 ATOM 1095 C CA . LEU A 1 143 ? -65.658 38.913 -0.608 1.00 49.46 ? 143 LEU A CA 1 ATOM 1096 C C . LEU A 1 143 ? -65.761 37.433 -0.231 1.00 48.19 ? 143 LEU A C 1 ATOM 1097 O O . LEU A 1 143 ? -66.861 36.911 -0.002 1.00 49.05 ? 143 LEU A O 1 ATOM 1098 C CB . LEU A 1 143 ? -66.149 39.795 0.548 1.00 50.50 ? 143 LEU A CB 1 ATOM 1099 C CG . LEU A 1 143 ? -65.200 40.017 1.729 1.00 50.63 ? 143 LEU A CG 1 ATOM 1100 C CD1 . LEU A 1 143 ? -64.919 38.726 2.488 1.00 50.32 ? 143 LEU A CD1 1 ATOM 1101 C CD2 . LEU A 1 143 ? -63.893 40.658 1.282 1.00 50.40 ? 143 LEU A CD2 1 ATOM 1102 N N . VAL A 1 144 ? -64.617 36.761 -0.164 1.00 44.64 ? 144 VAL A N 1 ATOM 1103 C CA . VAL A 1 144 ? -64.587 35.357 0.217 1.00 43.26 ? 144 VAL A CA 1 ATOM 1104 C C . VAL A 1 144 ? -63.865 35.255 1.534 1.00 41.67 ? 144 VAL A C 1 ATOM 1105 O O . VAL A 1 144 ? -62.858 35.930 1.733 1.00 40.27 ? 144 VAL A O 1 ATOM 1106 C CB . VAL A 1 144 ? -63.822 34.491 -0.807 1.00 42.80 ? 144 VAL A CB 1 ATOM 1107 C CG1 . VAL A 1 144 ? -63.870 33.023 -0.411 1.00 42.51 ? 144 VAL A CG1 1 ATOM 1108 C CG2 . VAL A 1 144 ? -64.394 34.679 -2.196 1.00 44.01 ? 144 VAL A CG2 1 ATOM 1109 N N . SER A 1 145 ? -64.375 34.420 2.437 1.00 41.72 ? 145 SER A N 1 ATOM 1110 C CA . SER A 1 145 ? -63.610 34.037 3.617 1.00 41.07 ? 145 SER A CA 1 ATOM 1111 C C . SER A 1 145 ? -63.472 32.526 3.584 1.00 41.94 ? 145 SER A C 1 ATOM 1112 O O . SER A 1 145 ? -64.458 31.800 3.447 1.00 43.81 ? 145 SER A O 1 ATOM 1113 C CB . SER A 1 145 ? -64.264 34.521 4.908 1.00 41.49 ? 145 SER A CB 1 ATOM 1114 O OG . SER A 1 145 ? -65.336 33.688 5.304 1.00 43.32 ? 145 SER A OG 1 ATOM 1115 N N . LEU A 1 146 ? -62.230 32.061 3.654 1.00 41.33 ? 146 LEU A N 1 ATOM 1116 C CA . LEU A 1 146 ? -61.943 30.636 3.677 1.00 41.14 ? 146 LEU A CA 1 ATOM 1117 C C . LEU A 1 146 ? -61.767 30.147 5.118 1.00 41.03 ? 146 LEU A C 1 ATOM 1118 O O . LEU A 1 146 ? -61.807 30.929 6.086 1.00 39.92 ? 146 LEU A O 1 ATOM 1119 C CB . LEU A 1 146 ? -60.712 30.310 2.811 1.00 40.46 ? 146 LEU A CB 1 ATOM 1120 C CG . LEU A 1 146 ? -59.374 31.033 3.032 1.00 39.82 ? 146 LEU A CG 1 ATOM 1121 C CD1 . LEU A 1 146 ? -58.684 30.588 4.309 1.00 39.30 ? 146 LEU A CD1 1 ATOM 1122 C CD2 . LEU A 1 146 ? -58.440 30.831 1.849 1.00 39.71 ? 146 LEU A CD2 1 ATOM 1123 N N . SER A 1 147 ? -61.602 28.839 5.247 1.00 41.00 ? 147 SER A N 1 ATOM 1124 C CA . SER A 1 147 ? -61.303 28.223 6.523 1.00 40.31 ? 147 SER A CA 1 ATOM 1125 C C . SER A 1 147 ? -60.179 27.232 6.321 1.00 38.93 ? 147 SER A C 1 ATOM 1126 O O . SER A 1 147 ? -59.830 26.888 5.186 1.00 37.08 ? 147 SER A O 1 ATOM 1127 C CB . SER A 1 147 ? -62.530 27.520 7.085 1.00 41.06 ? 147 SER A CB 1 ATOM 1128 O OG . SER A 1 147 ? -62.685 26.249 6.479 1.00 42.89 ? 147 SER A OG 1 ATOM 1129 N N . TYR A 1 148 ? -59.605 26.797 7.434 1.00 38.78 ? 148 TYR A N 1 ATOM 1130 C CA . TYR A 1 148 ? -58.486 25.865 7.411 1.00 38.92 ? 148 TYR A CA 1 ATOM 1131 C C . TYR A 1 148 ? -58.283 25.267 8.783 1.00 39.01 ? 148 TYR A C 1 ATOM 1132 O O . TYR A 1 148 ? -58.612 25.896 9.797 1.00 39.04 ? 148 TYR A O 1 ATOM 1133 C CB . TYR A 1 148 ? -57.199 26.553 6.940 1.00 38.05 ? 148 TYR A CB 1 ATOM 1134 C CG . TYR A 1 148 ? -56.710 27.690 7.811 1.00 36.65 ? 148 TYR A CG 1 ATOM 1135 C CD1 . TYR A 1 148 ? -57.214 28.983 7.665 1.00 36.85 ? 148 TYR A CD1 1 ATOM 1136 C CD2 . TYR A 1 148 ? -55.716 27.484 8.751 1.00 35.90 ? 148 TYR A CD2 1 ATOM 1137 C CE1 . TYR A 1 148 ? -56.748 30.029 8.452 1.00 35.87 ? 148 TYR A CE1 1 ATOM 1138 C CE2 . TYR A 1 148 ? -55.250 28.521 9.541 1.00 35.46 ? 148 TYR A CE2 1 ATOM 1139 C CZ . TYR A 1 148 ? -55.765 29.787 9.390 1.00 34.86 ? 148 TYR A CZ 1 ATOM 1140 O OH . TYR A 1 148 ? -55.287 30.796 10.186 1.00 33.53 ? 148 TYR A OH 1 ATOM 1141 N N . ARG A 1 149 ? -57.761 24.044 8.809 1.00 39.08 ? 149 ARG A N 1 ATOM 1142 C CA . ARG A 1 149 ? -57.514 23.351 10.064 1.00 38.86 ? 149 ARG A CA 1 ATOM 1143 C C . ARG A 1 149 ? -56.437 24.055 10.866 1.00 38.18 ? 149 ARG A C 1 ATOM 1144 O O . ARG A 1 149 ? -55.432 24.490 10.308 1.00 37.64 ? 149 ARG A O 1 ATOM 1145 C CB . ARG A 1 149 ? -57.110 21.910 9.817 1.00 39.16 ? 149 ARG A CB 1 ATOM 1146 C CG . ARG A 1 149 ? -58.269 21.037 9.394 1.00 40.86 ? 149 ARG A CG 1 ATOM 1147 C CD . ARG A 1 149 ? -57.788 19.673 8.926 1.00 41.80 ? 149 ARG A CD 1 ATOM 1148 N NE . ARG A 1 149 ? -57.188 19.750 7.600 1.00 40.76 ? 149 ARG A NE 1 ATOM 1149 C CZ . ARG A 1 149 ? -56.575 18.743 6.992 1.00 40.86 ? 149 ARG A CZ 1 ATOM 1150 N NH1 . ARG A 1 149 ? -56.468 17.559 7.580 1.00 41.95 ? 149 ARG A NH1 1 ATOM 1151 N NH2 . ARG A 1 149 ? -56.073 18.926 5.781 1.00 40.60 ? 149 ARG A NH2 1 ATOM 1152 N N . VAL A 1 150 ? -56.678 24.170 12.172 1.00 38.74 ? 150 VAL A N 1 ATOM 1153 C CA . VAL A 1 150 ? -55.735 24.768 13.114 1.00 37.99 ? 150 VAL A CA 1 ATOM 1154 C C . VAL A 1 150 ? -55.314 23.714 14.122 1.00 38.87 ? 150 VAL A C 1 ATOM 1155 O O . VAL A 1 150 ? -55.879 22.619 14.169 1.00 41.04 ? 150 VAL A O 1 ATOM 1156 C CB . VAL A 1 150 ? -56.363 25.955 13.874 1.00 38.26 ? 150 VAL A CB 1 ATOM 1157 C CG1 . VAL A 1 150 ? -56.637 27.107 12.913 1.00 37.90 ? 150 VAL A CG1 1 ATOM 1158 C CG2 . VAL A 1 150 ? -57.641 25.534 14.604 1.00 39.17 ? 150 VAL A CG2 1 ATOM 1159 N N . GLY A 1 151 ? -54.327 24.047 14.939 1.00 38.56 ? 151 GLY A N 1 ATOM 1160 C CA . GLY A 1 151 ? -53.879 23.144 15.995 1.00 39.67 ? 151 GLY A CA 1 ATOM 1161 C C . GLY A 1 151 ? -53.173 21.931 15.429 1.00 40.05 ? 151 GLY A C 1 ATOM 1162 O O . GLY A 1 151 ? -52.698 21.955 14.299 1.00 40.65 ? 151 GLY A O 1 ATOM 1163 N N . ALA A 1 152 ? -53.112 20.868 16.218 1.00 40.49 ? 152 ALA A N 1 ATOM 1164 C CA . ALA A 1 152 ? -52.535 19.616 15.770 1.00 41.01 ? 152 ALA A CA 1 ATOM 1165 C C . ALA A 1 152 ? -53.230 19.137 14.504 1.00 41.52 ? 152 ALA A C 1 ATOM 1166 O O . ALA A 1 152 ? -52.598 18.555 13.631 1.00 41.34 ? 152 ALA A O 1 ATOM 1167 C CB . ALA A 1 152 ? -52.657 18.556 16.859 1.00 41.98 ? 152 ALA A CB 1 ATOM 1168 N N . PHE A 1 153 ? -54.532 19.405 14.415 1.00 42.24 ? 153 PHE A N 1 ATOM 1169 C CA . PHE A 1 153 ? -55.377 18.917 13.321 1.00 41.47 ? 153 PHE A CA 1 ATOM 1170 C C . PHE A 1 153 ? -54.905 19.430 11.972 1.00 41.29 ? 153 PHE A C 1 ATOM 1171 O O . PHE A 1 153 ? -55.011 18.721 10.963 1.00 43.56 ? 153 PHE A O 1 ATOM 1172 C CB . PHE A 1 153 ? -56.824 19.330 13.571 1.00 42.17 ? 153 PHE A CB 1 ATOM 1173 C CG . PHE A 1 153 ? -57.354 18.855 14.891 1.00 43.63 ? 153 PHE A CG 1 ATOM 1174 C CD1 . PHE A 1 153 ? -57.845 17.571 15.034 1.00 44.62 ? 153 PHE A CD1 1 ATOM 1175 C CD2 . PHE A 1 153 ? -57.313 19.676 16.002 1.00 45.40 ? 153 PHE A CD2 1 ATOM 1176 C CE1 . PHE A 1 153 ? -58.304 17.120 16.255 1.00 45.98 ? 153 PHE A CE1 1 ATOM 1177 C CE2 . PHE A 1 153 ? -57.767 19.234 17.232 1.00 46.36 ? 153 PHE A CE2 1 ATOM 1178 C CZ . PHE A 1 153 ? -58.262 17.952 17.356 1.00 46.88 ? 153 PHE A CZ 1 ATOM 1179 N N . GLY A 1 154 ? -54.361 20.649 11.969 1.00 39.46 ? 154 GLY A N 1 ATOM 1180 C CA . GLY A 1 154 ? -53.872 21.291 10.750 1.00 38.63 ? 154 GLY A CA 1 ATOM 1181 C C . GLY A 1 154 ? -52.362 21.364 10.602 1.00 37.68 ? 154 GLY A C 1 ATOM 1182 O O . GLY A 1 154 ? -51.860 21.565 9.495 1.00 36.85 ? 154 GLY A O 1 ATOM 1183 N N . PHE A 1 155 ? -51.623 21.206 11.700 1.00 36.53 ? 155 PHE A N 1 ATOM 1184 C CA . PHE A 1 155 ? -50.182 21.427 11.658 1.00 35.37 ? 155 PHE A CA 1 ATOM 1185 C C . PHE A 1 155 ? -49.280 20.393 12.343 1.00 36.67 ? 155 PHE A C 1 ATOM 1186 O O . PHE A 1 155 ? -48.063 20.568 12.395 1.00 36.67 ? 155 PHE A O 1 ATOM 1187 C CB . PHE A 1 155 ? -49.899 22.852 12.126 1.00 33.72 ? 155 PHE A CB 1 ATOM 1188 C CG . PHE A 1 155 ? -50.464 23.887 11.196 1.00 33.45 ? 155 PHE A CG 1 ATOM 1189 C CD1 . PHE A 1 155 ? -49.837 24.159 9.984 1.00 33.38 ? 155 PHE A CD1 1 ATOM 1190 C CD2 . PHE A 1 155 ? -51.649 24.533 11.488 1.00 32.91 ? 155 PHE A CD2 1 ATOM 1191 C CE1 . PHE A 1 155 ? -50.353 25.085 9.108 1.00 32.48 ? 155 PHE A CE1 1 ATOM 1192 C CE2 . PHE A 1 155 ? -52.178 25.463 10.610 1.00 33.17 ? 155 PHE A CE2 1 ATOM 1193 C CZ . PHE A 1 155 ? -51.531 25.742 9.419 1.00 33.11 ? 155 PHE A CZ 1 ATOM 1194 N N . LEU A 1 156 ? -49.837 19.283 12.799 1.00 39.15 ? 156 LEU A N 1 ATOM 1195 C CA . LEU A 1 156 ? -48.984 18.217 13.298 1.00 42.16 ? 156 LEU A CA 1 ATOM 1196 C C . LEU A 1 156 ? -48.038 17.822 12.172 1.00 43.27 ? 156 LEU A C 1 ATOM 1197 O O . LEU A 1 156 ? -48.480 17.561 11.057 1.00 46.79 ? 156 LEU A O 1 ATOM 1198 C CB . LEU A 1 156 ? -49.803 17.014 13.733 1.00 43.61 ? 156 LEU A CB 1 ATOM 1199 C CG . LEU A 1 156 ? -48.999 16.009 14.548 1.00 45.30 ? 156 LEU A CG 1 ATOM 1200 C CD1 . LEU A 1 156 ? -49.059 16.398 16.015 1.00 46.05 ? 156 LEU A CD1 1 ATOM 1201 C CD2 . LEU A 1 156 ? -49.524 14.597 14.336 1.00 46.77 ? 156 LEU A CD2 1 ATOM 1202 N N . ALA A 1 157 ? -46.744 17.779 12.464 1.00 44.89 ? 157 ALA A N 1 ATOM 1203 C CA . ALA A 1 157 ? -45.718 17.573 11.439 1.00 46.05 ? 157 ALA A CA 1 ATOM 1204 C C . ALA A 1 157 ? -44.721 16.454 11.757 1.00 47.68 ? 157 ALA A C 1 ATOM 1205 O O . ALA A 1 157 ? -43.730 16.685 12.450 1.00 48.59 ? 157 ALA A O 1 ATOM 1206 C CB . ALA A 1 157 ? -44.967 18.877 11.207 1.00 44.32 ? 157 ALA A CB 1 ATOM 1207 N N . LEU A 1 158 ? -44.977 15.259 11.226 1.00 50.24 ? 158 LEU A N 1 ATOM 1208 C CA . LEU A 1 158 ? -44.013 14.151 11.270 1.00 52.71 ? 158 LEU A CA 1 ATOM 1209 C C . LEU A 1 158 ? -43.372 13.957 9.896 1.00 56.90 ? 158 LEU A C 1 ATOM 1210 O O . LEU A 1 158 ? -43.753 13.062 9.137 1.00 58.40 ? 158 LEU A O 1 ATOM 1211 C CB . LEU A 1 158 ? -44.706 12.871 11.714 1.00 52.95 ? 158 LEU A CB 1 ATOM 1212 C CG . LEU A 1 158 ? -45.186 12.852 13.163 1.00 53.46 ? 158 LEU A CG 1 ATOM 1213 C CD1 . LEU A 1 158 ? -46.215 11.747 13.382 1.00 54.29 ? 158 LEU A CD1 1 ATOM 1214 C CD2 . LEU A 1 158 ? -44.007 12.706 14.119 1.00 53.82 ? 158 LEU A CD2 1 ATOM 1215 N N . HIS A 1 159 ? -42.389 14.804 9.593 1.00 61.83 ? 159 HIS A N 1 ATOM 1216 C CA . HIS A 1 159 ? -41.803 14.917 8.245 1.00 65.93 ? 159 HIS A CA 1 ATOM 1217 C C . HIS A 1 159 ? -41.326 13.571 7.709 1.00 67.62 ? 159 HIS A C 1 ATOM 1218 O O . HIS A 1 159 ? -40.881 12.718 8.471 1.00 67.26 ? 159 HIS A O 1 ATOM 1219 C CB . HIS A 1 159 ? -40.644 15.930 8.254 1.00 68.42 ? 159 HIS A CB 1 ATOM 1220 C CG . HIS A 1 159 ? -40.109 16.258 6.894 1.00 72.69 ? 159 HIS A CG 1 ATOM 1221 N ND1 . HIS A 1 159 ? -38.920 15.745 6.417 1.00 75.61 ? 159 HIS A ND1 1 ATOM 1222 C CD2 . HIS A 1 159 ? -40.597 17.052 5.912 1.00 73.35 ? 159 HIS A CD2 1 ATOM 1223 C CE1 . HIS A 1 159 ? -38.700 16.205 5.198 1.00 75.48 ? 159 HIS A CE1 1 ATOM 1224 N NE2 . HIS A 1 159 ? -39.702 17.001 4.869 1.00 76.37 ? 159 HIS A NE2 1 ATOM 1225 N N . GLY A 1 160 ? -41.447 13.379 6.397 1.00 69.48 ? 160 GLY A N 1 ATOM 1226 C CA . GLY A 1 160 ? -41.068 12.114 5.767 1.00 71.24 ? 160 GLY A CA 1 ATOM 1227 C C . GLY A 1 160 ? -42.176 11.075 5.750 1.00 70.43 ? 160 GLY A C 1 ATOM 1228 O O . GLY A 1 160 ? -42.032 10.032 5.118 1.00 70.43 ? 160 GLY A O 1 ATOM 1229 N N . SER A 1 161 ? -43.273 11.350 6.450 1.00 69.97 ? 161 SER A N 1 ATOM 1230 C CA . SER A 1 161 ? -44.443 10.492 6.430 1.00 72.70 ? 161 SER A CA 1 ATOM 1231 C C . SER A 1 161 ? -45.539 11.211 5.672 1.00 72.00 ? 161 SER A C 1 ATOM 1232 O O . SER A 1 161 ? -45.558 12.445 5.629 1.00 70.66 ? 161 SER A O 1 ATOM 1233 C CB . SER A 1 161 ? -44.912 10.191 7.847 1.00 75.70 ? 161 SER A CB 1 ATOM 1234 O OG . SER A 1 161 ? -46.065 9.365 7.821 1.00 81.59 ? 161 SER A OG 1 ATOM 1235 N N . GLN A 1 162 ? -46.447 10.441 5.073 1.00 72.39 ? 162 GLN A N 1 ATOM 1236 C CA . GLN A 1 162 ? -47.529 11.010 4.252 1.00 70.93 ? 162 GLN A CA 1 ATOM 1237 C C . GLN A 1 162 ? -48.873 11.070 4.973 1.00 65.78 ? 162 GLN A C 1 ATOM 1238 O O . GLN A 1 162 ? -49.832 11.681 4.485 1.00 60.86 ? 162 GLN A O 1 ATOM 1239 C CB . GLN A 1 162 ? -47.650 10.234 2.933 1.00 75.57 ? 162 GLN A CB 1 ATOM 1240 C CG . GLN A 1 162 ? -46.442 10.403 2.010 1.00 78.73 ? 162 GLN A CG 1 ATOM 1241 C CD . GLN A 1 162 ? -46.067 11.870 1.782 1.00 79.28 ? 162 GLN A CD 1 ATOM 1242 O OE1 . GLN A 1 162 ? -46.937 12.752 1.707 1.00 75.16 ? 162 GLN A OE1 1 ATOM 1243 N NE2 . GLN A 1 162 ? -44.763 12.138 1.683 1.00 80.85 ? 162 GLN A NE2 1 ATOM 1244 N N . GLU A 1 163 ? -48.922 10.455 6.148 1.00 63.81 ? 163 GLU A N 1 ATOM 1245 C CA . GLU A 1 163 ? -50.110 10.456 6.976 1.00 62.70 ? 163 GLU A CA 1 ATOM 1246 C C . GLU A 1 163 ? -50.209 11.746 7.802 1.00 59.67 ? 163 GLU A C 1 ATOM 1247 O O . GLU A 1 163 ? -51.310 12.221 8.077 1.00 59.13 ? 163 GLU A O 1 ATOM 1248 C CB . GLU A 1 163 ? -50.096 9.225 7.887 1.00 65.56 ? 163 GLU A CB 1 ATOM 1249 C CG . GLU A 1 163 ? -50.005 7.888 7.156 1.00 67.21 ? 163 GLU A CG 1 ATOM 1250 C CD . GLU A 1 163 ? -51.134 7.673 6.157 1.00 67.63 ? 163 GLU A CD 1 ATOM 1251 O OE1 . GLU A 1 163 ? -52.235 8.248 6.351 1.00 63.98 ? 163 GLU A OE1 1 ATOM 1252 O OE2 . GLU A 1 163 ? -50.919 6.927 5.170 1.00 68.72 ? 163 GLU A OE2 1 ATOM 1253 N N . ALA A 1 164 ? -49.063 12.301 8.195 1.00 57.04 ? 164 ALA A N 1 ATOM 1254 C CA . ALA A 1 164 ? -49.017 13.577 8.907 1.00 54.41 ? 164 ALA A CA 1 ATOM 1255 C C . ALA A 1 164 ? -47.801 14.396 8.458 1.00 53.66 ? 164 ALA A C 1 ATOM 1256 O O . ALA A 1 164 ? -46.863 14.617 9.228 1.00 55.09 ? 164 ALA A O 1 ATOM 1257 C CB . ALA A 1 164 ? -48.988 13.346 10.408 1.00 54.10 ? 164 ALA A CB 1 ATOM 1258 N N . PRO A 1 165 ? -47.826 14.872 7.207 1.00 51.18 ? 165 PRO A N 1 ATOM 1259 C CA . PRO A 1 165 ? -46.685 15.586 6.653 1.00 49.91 ? 165 PRO A CA 1 ATOM 1260 C C . PRO A 1 165 ? -46.388 16.937 7.293 1.00 48.05 ? 165 PRO A C 1 ATOM 1261 O O . PRO A 1 165 ? -45.272 17.424 7.169 1.00 47.09 ? 165 PRO A O 1 ATOM 1262 C CB . PRO A 1 165 ? -47.089 15.798 5.188 1.00 50.38 ? 165 PRO A CB 1 ATOM 1263 C CG . PRO A 1 165 ? -48.574 15.823 5.206 1.00 49.98 ? 165 PRO A CG 1 ATOM 1264 C CD . PRO A 1 165 ? -48.975 14.856 6.282 1.00 51.05 ? 165 PRO A CD 1 ATOM 1265 N N . GLY A 1 166 ? -47.374 17.550 7.946 1.00 48.20 ? 166 GLY A N 1 ATOM 1266 C CA . GLY A 1 166 ? -47.259 18.953 8.359 1.00 46.53 ? 166 GLY A CA 1 ATOM 1267 C C . GLY A 1 166 ? -47.760 19.906 7.278 1.00 44.26 ? 166 GLY A C 1 ATOM 1268 O O . GLY A 1 166 ? -47.876 19.529 6.116 1.00 44.35 ? 166 GLY A O 1 ATOM 1269 N N . ASN A 1 167 ? -48.088 21.130 7.682 1.00 42.12 ? 167 ASN A N 1 ATOM 1270 C CA . ASN A 1 167 ? -48.570 22.181 6.784 1.00 40.23 ? 167 ASN A CA 1 ATOM 1271 C C . ASN A 1 167 ? -49.939 21.980 6.153 1.00 40.16 ? 167 ASN A C 1 ATOM 1272 O O . ASN A 1 167 ? -50.351 22.779 5.317 1.00 39.00 ? 167 ASN A O 1 ATOM 1273 C CB . ASN A 1 167 ? -47.546 22.453 5.683 1.00 40.05 ? 167 ASN A CB 1 ATOM 1274 C CG . ASN A 1 167 ? -46.297 23.082 6.218 1.00 39.29 ? 167 ASN A CG 1 ATOM 1275 O OD1 . ASN A 1 167 ? -46.312 23.642 7.302 1.00 37.73 ? 167 ASN A OD1 1 ATOM 1276 N ND2 . ASN A 1 167 ? -45.215 23.018 5.455 1.00 39.61 ? 167 ASN A ND2 1 ATOM 1277 N N . VAL A 1 168 ? -50.675 20.956 6.564 1.00 42.18 ? 168 VAL A N 1 ATOM 1278 C CA . VAL A 1 168 ? -51.909 20.623 5.842 1.00 43.47 ? 168 VAL A CA 1 ATOM 1279 C C . VAL A 1 168 ? -52.949 21.747 5.975 1.00 42.57 ? 168 VAL A C 1 ATOM 1280 O O . VAL A 1 168 ? -53.795 21.935 5.093 1.00 43.65 ? 168 VAL A O 1 ATOM 1281 C CB . VAL A 1 168 ? -52.473 19.240 6.237 1.00 44.24 ? 168 VAL A CB 1 ATOM 1282 C CG1 . VAL A 1 168 ? -51.388 18.181 6.100 1.00 44.62 ? 168 VAL A CG1 1 ATOM 1283 C CG2 . VAL A 1 168 ? -53.056 19.247 7.644 1.00 44.80 ? 168 VAL A CG2 1 ATOM 1284 N N . GLY A 1 169 ? -52.848 22.511 7.057 1.00 41.70 ? 169 GLY A N 1 ATOM 1285 C CA . GLY A 1 169 ? -53.652 23.717 7.238 1.00 40.79 ? 169 GLY A CA 1 ATOM 1286 C C . GLY A 1 169 ? -53.412 24.718 6.124 1.00 39.30 ? 169 GLY A C 1 ATOM 1287 O O . GLY A 1 169 ? -54.336 25.372 5.654 1.00 38.30 ? 169 GLY A O 1 ATOM 1288 N N . LEU A 1 170 ? -52.160 24.850 5.713 1.00 38.52 ? 170 LEU A N 1 ATOM 1289 C CA . LEU A 1 170 ? -51.823 25.731 4.608 1.00 37.86 ? 170 LEU A CA 1 ATOM 1290 C C . LEU A 1 170 ? -52.325 25.161 3.293 1.00 38.25 ? 170 LEU A C 1 ATOM 1291 O O . LEU A 1 170 ? -52.700 25.914 2.397 1.00 39.49 ? 170 LEU A O 1 ATOM 1292 C CB . LEU A 1 170 ? -50.320 25.945 4.533 1.00 37.57 ? 170 LEU A CB 1 ATOM 1293 C CG . LEU A 1 170 ? -49.759 26.850 5.613 1.00 37.05 ? 170 LEU A CG 1 ATOM 1294 C CD1 . LEU A 1 170 ? -48.242 26.810 5.556 1.00 37.64 ? 170 LEU A CD1 1 ATOM 1295 C CD2 . LEU A 1 170 ? -50.275 28.268 5.428 1.00 37.06 ? 170 LEU A CD2 1 ATOM 1296 N N . LEU A 1 171 ? -52.333 23.837 3.172 1.00 37.71 ? 171 LEU A N 1 ATOM 1297 C CA . LEU A 1 171 ? -52.915 23.198 1.992 1.00 38.20 ? 171 LEU A CA 1 ATOM 1298 C C . LEU A 1 171 ? -54.431 23.384 1.933 1.00 37.43 ? 171 LEU A C 1 ATOM 1299 O O . LEU A 1 171 ? -54.988 23.491 0.847 1.00 37.86 ? 171 LEU A O 1 ATOM 1300 C CB . LEU A 1 171 ? -52.534 21.717 1.920 1.00 38.43 ? 171 LEU A CB 1 ATOM 1301 C CG . LEU A 1 171 ? -51.025 21.512 1.725 1.00 37.91 ? 171 LEU A CG 1 ATOM 1302 C CD1 . LEU A 1 171 ? -50.644 20.047 1.866 1.00 38.59 ? 171 LEU A CD1 1 ATOM 1303 C CD2 . LEU A 1 171 ? -50.558 22.065 0.385 1.00 37.24 ? 171 LEU A CD2 1 ATOM 1304 N N . ASP A 1 172 ? -55.089 23.427 3.088 1.00 36.31 ? 172 ASP A N 1 ATOM 1305 C CA . ASP A 1 172 ? -56.503 23.779 3.131 1.00 36.80 ? 172 ASP A CA 1 ATOM 1306 C C . ASP A 1 172 ? -56.706 25.148 2.503 1.00 36.74 ? 172 ASP A C 1 ATOM 1307 O O . ASP A 1 172 ? -57.585 25.347 1.671 1.00 39.22 ? 172 ASP A O 1 ATOM 1308 C CB . ASP A 1 172 ? -57.033 23.801 4.569 1.00 36.84 ? 172 ASP A CB 1 ATOM 1309 C CG . ASP A 1 172 ? -57.022 22.429 5.224 1.00 38.49 ? 172 ASP A CG 1 ATOM 1310 O OD1 . ASP A 1 172 ? -56.896 21.407 4.517 1.00 38.31 ? 172 ASP A OD1 1 ATOM 1311 O OD2 . ASP A 1 172 ? -57.145 22.368 6.468 1.00 40.02 ? 172 ASP A OD2 1 ATOM 1312 N N . GLN A 1 173 ? -55.875 26.092 2.901 1.00 36.81 ? 173 GLN A N 1 ATOM 1313 C CA . GLN A 1 173 ? -55.980 27.455 2.431 1.00 37.23 ? 173 GLN A CA 1 ATOM 1314 C C . GLN A 1 173 ? -55.835 27.494 0.923 1.00 38.46 ? 173 GLN A C 1 ATOM 1315 O O . GLN A 1 173 ? -56.635 28.119 0.245 1.00 39.89 ? 173 GLN A O 1 ATOM 1316 C CB . GLN A 1 173 ? -54.909 28.327 3.098 1.00 37.60 ? 173 GLN A CB 1 ATOM 1317 C CG . GLN A 1 173 ? -55.113 28.564 4.596 1.00 37.09 ? 173 GLN A CG 1 ATOM 1318 C CD . GLN A 1 173 ? -54.049 29.476 5.196 1.00 37.37 ? 173 GLN A CD 1 ATOM 1319 O OE1 . GLN A 1 173 ? -53.336 30.187 4.478 1.00 35.46 ? 173 GLN A OE1 1 ATOM 1320 N NE2 . GLN A 1 173 ? -53.935 29.457 6.525 1.00 37.17 ? 173 GLN A NE2 1 ATOM 1321 N N . ARG A 1 174 ? -54.827 26.794 0.407 1.00 39.39 ? 174 ARG A N 1 ATOM 1322 C CA . ARG A 1 174 ? -54.529 26.763 -1.035 1.00 39.69 ? 174 ARG A CA 1 ATOM 1323 C C . ARG A 1 174 ? -55.645 26.145 -1.860 1.00 42.44 ? 174 ARG A C 1 ATOM 1324 O O . ARG A 1 174 ? -55.949 26.621 -2.960 1.00 42.77 ? 174 ARG A O 1 ATOM 1325 C CB . ARG A 1 174 ? -53.240 25.983 -1.293 1.00 38.38 ? 174 ARG A CB 1 ATOM 1326 C CG . ARG A 1 174 ? -52.827 25.911 -2.752 1.00 38.47 ? 174 ARG A CG 1 ATOM 1327 C CD . ARG A 1 174 ? -51.700 24.907 -2.941 1.00 38.62 ? 174 ARG A CD 1 ATOM 1328 N NE . ARG A 1 174 ? -50.408 25.467 -2.563 1.00 38.40 ? 174 ARG A NE 1 ATOM 1329 C CZ . ARG A 1 174 ? -49.295 24.764 -2.376 1.00 38.08 ? 174 ARG A CZ 1 ATOM 1330 N NH1 . ARG A 1 174 ? -49.286 23.448 -2.493 1.00 39.15 ? 174 ARG A NH1 1 ATOM 1331 N NH2 . ARG A 1 174 ? -48.182 25.388 -2.053 1.00 38.21 ? 174 ARG A NH2 1 ATOM 1332 N N . MET A 1 175 ? -56.235 25.071 -1.342 1.00 44.42 ? 175 MET A N 1 ATOM 1333 C CA . MET A 1 175 ? -57.342 24.417 -2.024 1.00 46.16 ? 175 MET A CA 1 ATOM 1334 C C . MET A 1 175 ? -58.541 25.347 -2.103 1.00 45.83 ? 175 MET A C 1 ATOM 1335 O O . MET A 1 175 ? -59.260 25.350 -3.087 1.00 48.02 ? 175 MET A O 1 ATOM 1336 C CB . MET A 1 175 ? -57.741 23.122 -1.323 1.00 47.58 ? 175 MET A CB 1 ATOM 1337 C CG . MET A 1 175 ? -58.790 22.346 -2.099 1.00 50.34 ? 175 MET A CG 1 ATOM 1338 S SD . MET A 1 175 ? -58.888 20.618 -1.619 1.00 56.19 ? 175 MET A SD 1 ATOM 1339 C CE . MET A 1 175 ? -57.336 19.984 -2.239 1.00 53.94 ? 175 MET A CE 1 ATOM 1340 N N . ALA A 1 176 ? -58.760 26.138 -1.066 1.00 44.93 ? 176 ALA A N 1 ATOM 1341 C CA . ALA A 1 176 ? -59.826 27.117 -1.111 1.00 45.21 ? 176 ALA A CA 1 ATOM 1342 C C . ALA A 1 176 ? -59.530 28.149 -2.191 1.00 45.13 ? 176 ALA A C 1 ATOM 1343 O O . ALA A 1 176 ? -60.445 28.622 -2.856 1.00 46.31 ? 176 ALA A O 1 ATOM 1344 C CB . ALA A 1 176 ? -59.998 27.792 0.243 1.00 45.65 ? 176 ALA A CB 1 ATOM 1345 N N . LEU A 1 177 ? -58.254 28.497 -2.361 1.00 44.25 ? 177 LEU A N 1 ATOM 1346 C CA . LEU A 1 177 ? -57.851 29.447 -3.402 1.00 43.56 ? 177 LEU A CA 1 ATOM 1347 C C . LEU A 1 177 ? -57.955 28.834 -4.788 1.00 44.12 ? 177 LEU A C 1 ATOM 1348 O O . LEU A 1 177 ? -58.266 29.525 -5.751 1.00 45.18 ? 177 LEU A O 1 ATOM 1349 C CB . LEU A 1 177 ? -56.425 29.940 -3.173 1.00 43.01 ? 177 LEU A CB 1 ATOM 1350 C CG . LEU A 1 177 ? -56.165 30.698 -1.872 1.00 42.79 ? 177 LEU A CG 1 ATOM 1351 C CD1 . LEU A 1 177 ? -54.673 30.970 -1.715 1.00 42.12 ? 177 LEU A CD1 1 ATOM 1352 C CD2 . LEU A 1 177 ? -56.965 31.993 -1.801 1.00 42.99 ? 177 LEU A CD2 1 ATOM 1353 N N . GLN A 1 178 ? -57.668 27.542 -4.890 1.00 44.83 ? 178 GLN A N 1 ATOM 1354 C CA . GLN A 1 178 ? -57.892 26.797 -6.134 1.00 46.11 ? 178 GLN A CA 1 ATOM 1355 C C . GLN A 1 178 ? -59.354 26.870 -6.527 1.00 45.86 ? 178 GLN A C 1 ATOM 1356 O O . GLN A 1 178 ? -59.682 27.137 -7.681 1.00 48.35 ? 178 GLN A O 1 ATOM 1357 C CB . GLN A 1 178 ? -57.496 25.318 -5.973 1.00 46.58 ? 178 GLN A CB 1 ATOM 1358 C CG . GLN A 1 178 ? -57.427 24.526 -7.266 1.00 48.05 ? 178 GLN A CG 1 ATOM 1359 C CD . GLN A 1 178 ? -56.429 25.112 -8.248 1.00 49.01 ? 178 GLN A CD 1 ATOM 1360 O OE1 . GLN A 1 178 ? -56.810 25.723 -9.254 1.00 49.04 ? 178 GLN A OE1 1 ATOM 1361 N NE2 . GLN A 1 178 ? -55.140 24.947 -7.951 1.00 48.19 ? 178 GLN A NE2 1 ATOM 1362 N N . TRP A 1 179 ? -60.222 26.642 -5.550 1.00 44.08 ? 179 TRP A N 1 ATOM 1363 C CA . TRP A 1 179 ? -61.649 26.630 -5.783 1.00 45.09 ? 179 TRP A CA 1 ATOM 1364 C C . TRP A 1 179 ? -62.127 27.999 -6.244 1.00 44.73 ? 179 TRP A C 1 ATOM 1365 O O . TRP A 1 179 ? -62.931 28.107 -7.162 1.00 47.90 ? 179 TRP A O 1 ATOM 1366 C CB . TRP A 1 179 ? -62.392 26.195 -4.525 1.00 44.80 ? 179 TRP A CB 1 ATOM 1367 C CG . TRP A 1 179 ? -63.779 25.775 -4.811 1.00 47.15 ? 179 TRP A CG 1 ATOM 1368 C CD1 . TRP A 1 179 ? -64.212 24.513 -5.100 1.00 48.28 ? 179 TRP A CD1 1 ATOM 1369 C CD2 . TRP A 1 179 ? -64.933 26.621 -4.862 1.00 48.58 ? 179 TRP A CD2 1 ATOM 1370 N NE1 . TRP A 1 179 ? -65.571 24.524 -5.324 1.00 50.21 ? 179 TRP A NE1 1 ATOM 1371 C CE2 . TRP A 1 179 ? -66.034 25.807 -5.180 1.00 49.83 ? 179 TRP A CE2 1 ATOM 1372 C CE3 . TRP A 1 179 ? -65.142 27.993 -4.666 1.00 48.28 ? 179 TRP A CE3 1 ATOM 1373 C CZ2 . TRP A 1 179 ? -67.321 26.317 -5.303 1.00 51.07 ? 179 TRP A CZ2 1 ATOM 1374 C CZ3 . TRP A 1 179 ? -66.421 28.496 -4.794 1.00 48.82 ? 179 TRP A CZ3 1 ATOM 1375 C CH2 . TRP A 1 179 ? -67.492 27.663 -5.106 1.00 50.19 ? 179 TRP A CH2 1 ATOM 1376 N N . VAL A 1 180 ? -61.613 29.038 -5.613 1.00 43.06 ? 180 VAL A N 1 ATOM 1377 C CA . VAL A 1 180 ? -61.913 30.411 -6.007 1.00 43.45 ? 180 VAL A CA 1 ATOM 1378 C C . VAL A 1 180 ? -61.431 30.664 -7.436 1.00 44.02 ? 180 VAL A C 1 ATOM 1379 O O . VAL A 1 180 ? -62.156 31.217 -8.247 1.00 45.45 ? 180 VAL A O 1 ATOM 1380 C CB . VAL A 1 180 ? -61.253 31.415 -5.026 1.00 42.25 ? 180 VAL A CB 1 ATOM 1381 C CG1 . VAL A 1 180 ? -61.282 32.838 -5.557 1.00 42.80 ? 180 VAL A CG1 1 ATOM 1382 C CG2 . VAL A 1 180 ? -61.927 31.353 -3.667 1.00 41.92 ? 180 VAL A CG2 1 ATOM 1383 N N . HIS A 1 181 ? -60.207 30.255 -7.738 1.00 43.85 ? 181 HIS A N 1 ATOM 1384 C CA . HIS A 1 181 ? -59.657 30.449 -9.064 1.00 45.17 ? 181 HIS A CA 1 ATOM 1385 C C . HIS A 1 181 ? -60.573 29.781 -10.062 1.00 45.92 ? 181 HIS A C 1 ATOM 1386 O O . HIS A 1 181 ? -60.916 30.380 -11.075 1.00 46.67 ? 181 HIS A O 1 ATOM 1387 C CB . HIS A 1 181 ? -58.246 29.860 -9.159 1.00 46.50 ? 181 HIS A CB 1 ATOM 1388 C CG . HIS A 1 181 ? -57.670 29.867 -10.544 1.00 49.81 ? 181 HIS A CG 1 ATOM 1389 N ND1 . HIS A 1 181 ? -57.883 28.844 -11.448 1.00 52.67 ? 181 HIS A ND1 1 ATOM 1390 C CD2 . HIS A 1 181 ? -56.881 30.767 -11.178 1.00 51.26 ? 181 HIS A CD2 1 ATOM 1391 C CE1 . HIS A 1 181 ? -57.248 29.113 -12.577 1.00 53.52 ? 181 HIS A CE1 1 ATOM 1392 N NE2 . HIS A 1 181 ? -56.634 30.276 -12.440 1.00 52.99 ? 181 HIS A NE2 1 ATOM 1393 N N . ASP A 1 182 ? -60.986 28.554 -9.751 1.00 44.96 ? 182 ASP A N 1 ATOM 1394 C CA . ASP A 1 182 ? -61.808 27.758 -10.655 1.00 46.61 ? 182 ASP A CA 1 ATOM 1395 C C . ASP A 1 182 ? -63.285 28.213 -10.745 1.00 47.07 ? 182 ASP A C 1 ATOM 1396 O O . ASP A 1 182 ? -63.886 28.130 -11.809 1.00 48.95 ? 182 ASP A O 1 ATOM 1397 C CB . ASP A 1 182 ? -61.747 26.268 -10.255 1.00 47.29 ? 182 ASP A CB 1 ATOM 1398 C CG . ASP A 1 182 ? -60.350 25.647 -10.425 1.00 47.27 ? 182 ASP A CG 1 ATOM 1399 O OD1 . ASP A 1 182 ? -59.562 26.113 -11.282 1.00 49.29 ? 182 ASP A OD1 1 ATOM 1400 O OD2 . ASP A 1 182 ? -60.039 24.677 -9.700 1.00 45.37 ? 182 ASP A OD2 1 ATOM 1401 N N . ASN A 1 183 ? -63.870 28.683 -9.648 1.00 45.50 ? 183 ASN A N 1 ATOM 1402 C CA . ASN A 1 183 ? -65.323 28.843 -9.578 1.00 46.50 ? 183 ASN A CA 1 ATOM 1403 C C . ASN A 1 183 ? -65.878 30.241 -9.295 1.00 47.26 ? 183 ASN A C 1 ATOM 1404 O O . ASN A 1 183 ? -67.084 30.465 -9.459 1.00 48.14 ? 183 ASN A O 1 ATOM 1405 C CB . ASN A 1 183 ? -65.874 27.882 -8.534 1.00 46.42 ? 183 ASN A CB 1 ATOM 1406 C CG . ASN A 1 183 ? -65.706 26.439 -8.942 1.00 47.86 ? 183 ASN A CG 1 ATOM 1407 O OD1 . ASN A 1 183 ? -66.469 25.921 -9.760 1.00 49.70 ? 183 ASN A OD1 1 ATOM 1408 N ND2 . ASN A 1 183 ? -64.703 25.778 -8.379 1.00 47.18 ? 183 ASN A ND2 1 ATOM 1409 N N . ILE A 1 184 ? -65.032 31.185 -8.892 1.00 45.91 ? 184 ILE A N 1 ATOM 1410 C CA . ILE A 1 184 ? -65.533 32.498 -8.497 1.00 46.06 ? 184 ILE A CA 1 ATOM 1411 C C . ILE A 1 184 ? -66.159 33.286 -9.654 1.00 48.14 ? 184 ILE A C 1 ATOM 1412 O O . ILE A 1 184 ? -67.007 34.148 -9.422 1.00 49.80 ? 184 ILE A O 1 ATOM 1413 C CB . ILE A 1 184 ? -64.439 33.339 -7.814 1.00 44.71 ? 184 ILE A CB 1 ATOM 1414 C CG1 . ILE A 1 184 ? -65.068 34.428 -6.918 1.00 44.80 ? 184 ILE A CG1 1 ATOM 1415 C CG2 . ILE A 1 184 ? -63.476 33.916 -8.847 1.00 44.74 ? 184 ILE A CG2 1 ATOM 1416 C CD1 . ILE A 1 184 ? -65.757 33.902 -5.670 1.00 44.06 ? 184 ILE A CD1 1 ATOM 1417 N N . GLN A 1 185 ? -65.762 32.981 -10.888 1.00 49.17 ? 185 GLN A N 1 ATOM 1418 C CA . GLN A 1 185 ? -66.359 33.615 -12.074 1.00 51.70 ? 185 GLN A CA 1 ATOM 1419 C C . GLN A 1 185 ? -67.878 33.446 -12.133 1.00 52.51 ? 185 GLN A C 1 ATOM 1420 O O . GLN A 1 185 ? -68.580 34.279 -12.706 1.00 52.75 ? 185 GLN A O 1 ATOM 1421 C CB . GLN A 1 185 ? -65.742 33.051 -13.364 1.00 53.36 ? 185 GLN A CB 1 ATOM 1422 C CG . GLN A 1 185 ? -66.174 31.620 -13.683 1.00 54.60 ? 185 GLN A CG 1 ATOM 1423 C CD . GLN A 1 185 ? -65.270 30.935 -14.683 1.00 55.00 ? 185 GLN A CD 1 ATOM 1424 O OE1 . GLN A 1 185 ? -64.151 30.541 -14.358 1.00 52.96 ? 185 GLN A OE1 1 ATOM 1425 N NE2 . GLN A 1 185 ? -65.759 30.778 -15.907 1.00 56.97 ? 185 GLN A NE2 1 ATOM 1426 N N . PHE A 1 186 ? -68.374 32.359 -11.555 1.00 51.92 ? 186 PHE A N 1 ATOM 1427 C CA . PHE A 1 186 ? -69.798 32.083 -11.561 1.00 54.72 ? 186 PHE A CA 1 ATOM 1428 C C . PHE A 1 186 ? -70.544 32.969 -10.566 1.00 56.54 ? 186 PHE A C 1 ATOM 1429 O O . PHE A 1 186 ? -71.761 33.155 -10.671 1.00 60.06 ? 186 PHE A O 1 ATOM 1430 C CB . PHE A 1 186 ? -70.034 30.601 -11.284 1.00 54.55 ? 186 PHE A CB 1 ATOM 1431 C CG . PHE A 1 186 ? -69.310 29.705 -12.244 1.00 54.67 ? 186 PHE A CG 1 ATOM 1432 C CD1 . PHE A 1 186 ? -69.552 29.801 -13.604 1.00 55.10 ? 186 PHE A CD1 1 ATOM 1433 C CD2 . PHE A 1 186 ? -68.353 28.804 -11.798 1.00 53.94 ? 186 PHE A CD2 1 ATOM 1434 C CE1 . PHE A 1 186 ? -68.872 29.004 -14.499 1.00 55.32 ? 186 PHE A CE1 1 ATOM 1435 C CE2 . PHE A 1 186 ? -67.669 27.997 -12.693 1.00 54.11 ? 186 PHE A CE2 1 ATOM 1436 C CZ . PHE A 1 186 ? -67.934 28.097 -14.044 1.00 54.78 ? 186 PHE A CZ 1 ATOM 1437 N N . PHE A 1 187 ? -69.802 33.536 -9.620 1.00 55.66 ? 187 PHE A N 1 ATOM 1438 C CA . PHE A 1 187 ? -70.355 34.456 -8.646 1.00 55.18 ? 187 PHE A CA 1 ATOM 1439 C C . PHE A 1 187 ? -70.140 35.909 -9.050 1.00 56.29 ? 187 PHE A C 1 ATOM 1440 O O . PHE A 1 187 ? -70.423 36.814 -8.262 1.00 56.70 ? 187 PHE A O 1 ATOM 1441 C CB . PHE A 1 187 ? -69.712 34.190 -7.298 1.00 52.54 ? 187 PHE A CB 1 ATOM 1442 C CG . PHE A 1 187 ? -70.027 32.835 -6.748 1.00 51.69 ? 187 PHE A CG 1 ATOM 1443 C CD1 . PHE A 1 187 ? -69.241 31.747 -7.064 1.00 50.73 ? 187 PHE A CD1 1 ATOM 1444 C CD2 . PHE A 1 187 ? -71.121 32.649 -5.915 1.00 52.46 ? 187 PHE A CD2 1 ATOM 1445 C CE1 . PHE A 1 187 ? -69.535 30.495 -6.555 1.00 51.12 ? 187 PHE A CE1 1 ATOM 1446 C CE2 . PHE A 1 187 ? -71.423 31.400 -5.403 1.00 52.10 ? 187 PHE A CE2 1 ATOM 1447 C CZ . PHE A 1 187 ? -70.632 30.319 -5.727 1.00 51.59 ? 187 PHE A CZ 1 ATOM 1448 N N . GLY A 1 188 ? -69.664 36.130 -10.277 1.00 56.01 ? 188 GLY A N 1 ATOM 1449 C CA . GLY A 1 188 ? -69.336 37.468 -10.750 1.00 56.22 ? 188 GLY A CA 1 ATOM 1450 C C . GLY A 1 188 ? -67.911 37.890 -10.443 1.00 54.63 ? 188 GLY A C 1 ATOM 1451 O O . GLY A 1 188 ? -67.502 38.997 -10.796 1.00 56.25 ? 188 GLY A O 1 ATOM 1452 N N . GLY A 1 189 ? -67.146 37.020 -9.790 1.00 52.57 ? 189 GLY A N 1 ATOM 1453 C CA . GLY A 1 189 ? -65.772 37.348 -9.417 1.00 51.10 ? 189 GLY A CA 1 ATOM 1454 C C . GLY A 1 189 ? -64.865 37.238 -10.615 1.00 50.81 ? 189 GLY A C 1 ATOM 1455 O O . GLY A 1 189 ? -65.139 36.472 -11.525 1.00 53.12 ? 189 GLY A O 1 ATOM 1456 N N . ASP A 1 190 ? -63.803 38.032 -10.632 1.00 49.90 ? 190 ASP A N 1 ATOM 1457 C CA . ASP A 1 190 ? -62.785 37.933 -11.672 1.00 49.99 ? 190 ASP A CA 1 ATOM 1458 C C . ASP A 1 190 ? -61.598 37.151 -11.135 1.00 48.56 ? 190 ASP A C 1 ATOM 1459 O O . ASP A 1 190 ? -60.882 37.635 -10.259 1.00 48.67 ? 190 ASP A O 1 ATOM 1460 C CB . ASP A 1 190 ? -62.317 39.319 -12.107 1.00 50.23 ? 190 ASP A CB 1 ATOM 1461 C CG . ASP A 1 190 ? -61.147 39.263 -13.059 1.00 49.51 ? 190 ASP A CG 1 ATOM 1462 O OD1 . ASP A 1 190 ? -60.930 38.204 -13.672 1.00 49.40 ? 190 ASP A OD1 1 ATOM 1463 O OD2 . ASP A 1 190 ? -60.438 40.273 -13.203 1.00 49.46 ? 190 ASP A OD2 1 ATOM 1464 N N . PRO A 1 191 ? -61.356 35.951 -11.674 1.00 48.49 ? 191 PRO A N 1 ATOM 1465 C CA . PRO A 1 191 ? -60.234 35.169 -11.154 1.00 47.57 ? 191 PRO A CA 1 ATOM 1466 C C . PRO A 1 191 ? -58.850 35.791 -11.411 1.00 47.72 ? 191 PRO A C 1 ATOM 1467 O O . PRO A 1 191 ? -57.924 35.521 -10.674 1.00 46.11 ? 191 PRO A O 1 ATOM 1468 C CB . PRO A 1 191 ? -60.391 33.821 -11.861 1.00 48.09 ? 191 PRO A CB 1 ATOM 1469 C CG . PRO A 1 191 ? -61.148 34.125 -13.110 1.00 49.18 ? 191 PRO A CG 1 ATOM 1470 C CD . PRO A 1 191 ? -62.031 35.289 -12.801 1.00 49.25 ? 191 PRO A CD 1 ATOM 1471 N N . LYS A 1 192 ? -58.734 36.636 -12.429 1.00 52.20 ? 192 LYS A N 1 ATOM 1472 C CA . LYS A 1 192 ? -57.490 37.357 -12.722 1.00 54.50 ? 192 LYS A CA 1 ATOM 1473 C C . LYS A 1 192 ? -57.119 38.398 -11.669 1.00 53.27 ? 192 LYS A C 1 ATOM 1474 O O . LYS A 1 192 ? -55.962 38.821 -11.610 1.00 52.53 ? 192 LYS A O 1 ATOM 1475 C CB . LYS A 1 192 ? -57.602 38.108 -14.058 1.00 58.28 ? 192 LYS A CB 1 ATOM 1476 C CG . LYS A 1 192 ? -57.860 37.241 -15.286 1.00 61.85 ? 192 LYS A CG 1 ATOM 1477 C CD . LYS A 1 192 ? -57.759 38.046 -16.588 1.00 64.67 ? 192 LYS A CD 1 ATOM 1478 C CE . LYS A 1 192 ? -58.744 39.214 -16.650 1.00 65.46 ? 192 LYS A CE 1 ATOM 1479 N NZ . LYS A 1 192 ? -60.137 38.810 -16.314 1.00 64.80 ? 192 LYS A NZ 1 ATOM 1480 N N . THR A 1 193 ? -58.099 38.836 -10.875 1.00 52.64 ? 193 THR A N 1 ATOM 1481 C CA . THR A 1 193 ? -57.912 39.958 -9.941 1.00 51.04 ? 193 THR A CA 1 ATOM 1482 C C . THR A 1 193 ? -58.319 39.554 -8.515 1.00 48.79 ? 193 THR A C 1 ATOM 1483 O O . THR A 1 193 ? -59.177 40.170 -7.896 1.00 49.23 ? 193 THR A O 1 ATOM 1484 C CB . THR A 1 193 ? -58.690 41.212 -10.426 1.00 50.89 ? 193 THR A CB 1 ATOM 1485 O OG1 . THR A 1 193 ? -58.324 41.509 -11.781 1.00 52.15 ? 193 THR A OG1 1 ATOM 1486 C CG2 . THR A 1 193 ? -58.392 42.428 -9.570 1.00 50.19 ? 193 THR A CG2 1 ATOM 1487 N N . VAL A 1 194 ? -57.673 38.517 -7.997 1.00 46.86 ? 194 VAL A N 1 ATOM 1488 C CA . VAL A 1 194 ? -57.962 38.034 -6.657 1.00 44.89 ? 194 VAL A CA 1 ATOM 1489 C C . VAL A 1 194 ? -56.886 38.511 -5.696 1.00 44.29 ? 194 VAL A C 1 ATOM 1490 O O . VAL A 1 194 ? -55.691 38.347 -5.949 1.00 43.34 ? 194 VAL A O 1 ATOM 1491 C CB . VAL A 1 194 ? -58.033 36.501 -6.628 1.00 44.44 ? 194 VAL A CB 1 ATOM 1492 C CG1 . VAL A 1 194 ? -58.082 35.979 -5.200 1.00 43.71 ? 194 VAL A CG1 1 ATOM 1493 C CG2 . VAL A 1 194 ? -59.230 36.011 -7.427 1.00 45.47 ? 194 VAL A CG2 1 ATOM 1494 N N . THR A 1 195 ? -57.321 39.087 -4.582 1.00 44.91 ? 195 THR A N 1 ATOM 1495 C CA . THR A 1 195 ? -56.415 39.606 -3.559 1.00 44.23 ? 195 THR A CA 1 ATOM 1496 C C . THR A 1 195 ? -56.577 38.813 -2.274 1.00 43.45 ? 195 THR A C 1 ATOM 1497 O O . THR A 1 195 ? -57.673 38.730 -1.733 1.00 46.04 ? 195 THR A O 1 ATOM 1498 C CB . THR A 1 195 ? -56.718 41.090 -3.269 1.00 43.80 ? 195 THR A CB 1 ATOM 1499 O OG1 . THR A 1 195 ? -56.358 41.873 -4.410 1.00 45.42 ? 195 THR A OG1 1 ATOM 1500 C CG2 . THR A 1 195 ? -55.950 41.584 -2.058 1.00 42.97 ? 195 THR A CG2 1 ATOM 1501 N N . ILE A 1 196 ? -55.499 38.238 -1.768 1.00 41.72 ? 196 ILE A N 1 ATOM 1502 C CA . ILE A 1 196 ? -55.584 37.573 -0.467 1.00 40.86 ? 196 ILE A CA 1 ATOM 1503 C C . ILE A 1 196 ? -55.202 38.537 0.655 1.00 40.14 ? 196 ILE A C 1 ATOM 1504 O O . ILE A 1 196 ? -54.232 39.279 0.541 1.00 39.88 ? 196 ILE A O 1 ATOM 1505 C CB . ILE A 1 196 ? -54.747 36.269 -0.394 1.00 40.12 ? 196 ILE A CB 1 ATOM 1506 C CG1 . ILE A 1 196 ? -53.257 36.518 -0.654 1.00 39.49 ? 196 ILE A CG1 1 ATOM 1507 C CG2 . ILE A 1 196 ? -55.290 35.240 -1.379 1.00 40.72 ? 196 ILE A CG2 1 ATOM 1508 C CD1 . ILE A 1 196 ? -52.428 35.250 -0.640 1.00 39.08 ? 196 ILE A CD1 1 ATOM 1509 N N . PHE A 1 197 ? -55.976 38.536 1.737 1.00 39.51 ? 197 PHE A N 1 ATOM 1510 C CA . PHE A 1 197 ? -55.643 39.361 2.887 1.00 38.63 ? 197 PHE A CA 1 ATOM 1511 C C . PHE A 1 197 ? -55.907 38.632 4.174 1.00 38.51 ? 197 PHE A C 1 ATOM 1512 O O . PHE A 1 197 ? -56.747 37.740 4.216 1.00 39.64 ? 197 PHE A O 1 ATOM 1513 C CB . PHE A 1 197 ? -56.323 40.743 2.830 1.00 39.82 ? 197 PHE A CB 1 ATOM 1514 C CG . PHE A 1 197 ? -57.819 40.749 3.013 1.00 39.76 ? 197 PHE A CG 1 ATOM 1515 C CD1 . PHE A 1 197 ? -58.660 39.964 2.226 1.00 40.70 ? 197 PHE A CD1 1 ATOM 1516 C CD2 . PHE A 1 197 ? -58.400 41.631 3.928 1.00 39.34 ? 197 PHE A CD2 1 ATOM 1517 C CE1 . PHE A 1 197 ? -60.043 40.015 2.392 1.00 41.26 ? 197 PHE A CE1 1 ATOM 1518 C CE2 . PHE A 1 197 ? -59.780 41.691 4.093 1.00 40.01 ? 197 PHE A CE2 1 ATOM 1519 C CZ . PHE A 1 197 ? -60.604 40.885 3.321 1.00 40.90 ? 197 PHE A CZ 1 ATOM 1520 N N . GLY A 1 198 ? -55.140 38.971 5.205 1.00 37.85 ? 198 GLY A N 1 ATOM 1521 C CA . GLY A 1 198 ? -55.236 38.288 6.496 1.00 36.85 ? 198 GLY A CA 1 ATOM 1522 C C . GLY A 1 198 ? -54.543 39.043 7.609 1.00 36.30 ? 198 GLY A C 1 ATOM 1523 O O . GLY A 1 198 ? -53.779 39.982 7.357 1.00 35.61 ? 198 GLY A O 1 ATOM 1524 N N . GLU A 1 199 ? -54.821 38.628 8.841 1.00 35.91 ? 199 GLU A N 1 ATOM 1525 C CA . GLU A 1 199 ? -54.282 39.278 10.033 1.00 35.83 ? 199 GLU A CA 1 ATOM 1526 C C . GLU A 1 199 ? -53.652 38.255 10.957 1.00 35.78 ? 199 GLU A C 1 ATOM 1527 O O . GLU A 1 199 ? -54.151 37.144 11.068 1.00 36.04 ? 199 GLU A O 1 ATOM 1528 C CB . GLU A 1 199 ? -55.398 40.029 10.762 1.00 36.56 ? 199 GLU A CB 1 ATOM 1529 C CG . GLU A 1 199 ? -54.951 40.874 11.956 1.00 36.82 ? 199 GLU A CG 1 ATOM 1530 C CD . GLU A 1 199 ? -54.918 40.118 13.278 1.00 36.65 ? 199 GLU A CD 1 ATOM 1531 O OE1 . GLU A 1 199 ? -55.410 38.978 13.358 1.00 36.82 ? 199 GLU A OE1 1 ATOM 1532 O OE2 . GLU A 1 199 ? -54.400 40.677 14.254 1.00 37.58 ? 199 GLU A OE2 1 ATOM 1533 N N . SER A 1 200 ? -52.561 38.635 11.623 1.00 37.25 ? 200 SER A N 1 ATOM 1534 C CA . SER A 1 200 ? -51.835 37.738 12.531 1.00 37.60 ? 200 SER A CA 1 ATOM 1535 C C . SER A 1 200 ? -51.366 36.521 11.734 1.00 36.59 ? 200 SER A C 1 ATOM 1536 O O . SER A 1 200 ? -50.695 36.684 10.719 1.00 38.53 ? 200 SER A O 1 ATOM 1537 C CB . SER A 1 200 ? -52.703 37.367 13.741 1.00 38.92 ? 200 SER A CB 1 ATOM 1538 O OG . SER A 1 200 ? -52.068 36.428 14.602 1.00 40.71 ? 200 SER A OG 1 ATOM 1539 N N . ALA A 1 201 ? -51.726 35.315 12.159 1.00 36.19 ? 201 ALA A N 1 ATOM 1540 C CA . ALA A 1 201 ? -51.375 34.099 11.415 1.00 36.60 ? 201 ALA A CA 1 ATOM 1541 C C . ALA A 1 201 ? -51.906 34.107 9.977 1.00 36.35 ? 201 ALA A C 1 ATOM 1542 O O . ALA A 1 201 ? -51.331 33.463 9.101 1.00 35.86 ? 201 ALA A O 1 ATOM 1543 C CB . ALA A 1 201 ? -51.869 32.860 12.150 1.00 36.66 ? 201 ALA A CB 1 ATOM 1544 N N . GLY A 1 202 ? -53.002 34.825 9.744 1.00 36.32 ? 202 GLY A N 1 ATOM 1545 C CA . GLY A 1 202 ? -53.531 35.016 8.388 1.00 37.36 ? 202 GLY A CA 1 ATOM 1546 C C . GLY A 1 202 ? -52.633 35.885 7.531 1.00 37.37 ? 202 GLY A C 1 ATOM 1547 O O . GLY A 1 202 ? -52.449 35.624 6.343 1.00 38.71 ? 202 GLY A O 1 ATOM 1548 N N . GLY A 1 203 ? -52.078 36.930 8.137 1.00 36.68 ? 203 GLY A N 1 ATOM 1549 C CA . GLY A 1 203 ? -51.070 37.743 7.488 1.00 36.73 ? 203 GLY A CA 1 ATOM 1550 C C . GLY A 1 203 ? -49.823 36.930 7.212 1.00 34.56 ? 203 GLY A C 1 ATOM 1551 O O . GLY A 1 203 ? -49.235 37.044 6.154 1.00 33.34 ? 203 GLY A O 1 ATOM 1552 N N . ALA A 1 204 ? -49.425 36.099 8.163 1.00 34.52 ? 204 ALA A N 1 ATOM 1553 C CA . ALA A 1 204 ? -48.247 35.246 7.963 1.00 36.35 ? 204 ALA A CA 1 ATOM 1554 C C . ALA A 1 204 ? -48.514 34.224 6.865 1.00 35.69 ? 204 ALA A C 1 ATOM 1555 O O . ALA A 1 204 ? -47.629 33.896 6.071 1.00 37.00 ? 204 ALA A O 1 ATOM 1556 C CB . ALA A 1 204 ? -47.846 34.547 9.259 1.00 35.52 ? 204 ALA A CB 1 ATOM 1557 N N . SER A 1 205 ? -49.743 33.729 6.840 1.00 35.07 ? 205 SER A N 1 ATOM 1558 C CA . SER A 1 205 ? -50.189 32.808 5.822 1.00 35.31 ? 205 SER A CA 1 ATOM 1559 C C . SER A 1 205 ? -50.117 33.471 4.440 1.00 36.00 ? 205 SER A C 1 ATOM 1560 O O . SER A 1 205 ? -49.605 32.876 3.501 1.00 35.87 ? 205 SER A O 1 ATOM 1561 C CB . SER A 1 205 ? -51.620 32.336 6.129 1.00 35.77 ? 205 SER A CB 1 ATOM 1562 O OG . SER A 1 205 ? -51.673 31.510 7.285 1.00 34.61 ? 205 SER A OG 1 ATOM 1563 N N . VAL A 1 206 ? -50.600 34.709 4.330 1.00 36.17 ? 206 VAL A N 1 ATOM 1564 C CA . VAL A 1 206 ? -50.560 35.444 3.064 1.00 36.56 ? 206 VAL A CA 1 ATOM 1565 C C . VAL A 1 206 ? -49.131 35.508 2.530 1.00 38.43 ? 206 VAL A C 1 ATOM 1566 O O . VAL A 1 206 ? -48.882 35.229 1.343 1.00 41.81 ? 206 VAL A O 1 ATOM 1567 C CB . VAL A 1 206 ? -51.121 36.878 3.211 1.00 35.80 ? 206 VAL A CB 1 ATOM 1568 C CG1 . VAL A 1 206 ? -50.792 37.722 1.987 1.00 35.31 ? 206 VAL A CG1 1 ATOM 1569 C CG2 . VAL A 1 206 ? -52.630 36.859 3.458 1.00 35.70 ? 206 VAL A CG2 1 ATOM 1570 N N . GLY A 1 207 ? -48.194 35.875 3.400 1.00 37.21 ? 207 GLY A N 1 ATOM 1571 C CA . GLY A 1 207 ? -46.788 35.909 3.029 1.00 38.13 ? 207 GLY A CA 1 ATOM 1572 C C . GLY A 1 207 ? -46.241 34.535 2.683 1.00 39.56 ? 207 GLY A C 1 ATOM 1573 O O . GLY A 1 207 ? -45.337 34.407 1.865 1.00 40.44 ? 207 GLY A O 1 ATOM 1574 N N . MET A 1 208 ? -46.772 33.496 3.315 1.00 39.96 ? 208 MET A N 1 ATOM 1575 C CA . MET A 1 208 ? -46.338 32.142 3.003 1.00 40.95 ? 208 MET A CA 1 ATOM 1576 C C . MET A 1 208 ? -46.816 31.701 1.608 1.00 41.35 ? 208 MET A C 1 ATOM 1577 O O . MET A 1 208 ? -46.142 30.916 0.947 1.00 42.32 ? 208 MET A O 1 ATOM 1578 C CB . MET A 1 208 ? -46.786 31.164 4.096 1.00 40.61 ? 208 MET A CB 1 ATOM 1579 C CG . MET A 1 208 ? -45.982 31.286 5.384 1.00 41.89 ? 208 MET A CG 1 ATOM 1580 S SD . MET A 1 208 ? -46.640 30.330 6.768 1.00 42.69 ? 208 MET A SD 1 ATOM 1581 C CE . MET A 1 208 ? -45.426 30.620 8.044 1.00 43.20 ? 208 MET A CE 1 ATOM 1582 N N . HIS A 1 209 ? -47.961 32.204 1.153 1.00 39.86 ? 209 HIS A N 1 ATOM 1583 C CA . HIS A 1 209 ? -48.448 31.865 -0.182 1.00 39.73 ? 209 HIS A CA 1 ATOM 1584 C C . HIS A 1 209 ? -47.702 32.647 -1.251 1.00 40.32 ? 209 HIS A C 1 ATOM 1585 O O . HIS A 1 209 ? -47.589 32.206 -2.398 1.00 40.61 ? 209 HIS A O 1 ATOM 1586 C CB . HIS A 1 209 ? -49.944 32.096 -0.301 1.00 40.04 ? 209 HIS A CB 1 ATOM 1587 C CG . HIS A 1 209 ? -50.764 31.148 0.515 1.00 40.54 ? 209 HIS A CG 1 ATOM 1588 N ND1 . HIS A 1 209 ? -50.794 29.790 0.278 1.00 41.02 ? 209 HIS A ND1 1 ATOM 1589 C CD2 . HIS A 1 209 ? -51.594 31.365 1.562 1.00 40.72 ? 209 HIS A CD2 1 ATOM 1590 C CE1 . HIS A 1 209 ? -51.597 29.209 1.150 1.00 40.79 ? 209 HIS A CE1 1 ATOM 1591 N NE2 . HIS A 1 209 ? -52.098 30.143 1.939 1.00 41.77 ? 209 HIS A NE2 1 ATOM 1592 N N . ILE A 1 210 ? -47.185 33.808 -0.871 1.00 39.30 ? 210 ILE A N 1 ATOM 1593 C CA . ILE A 1 210 ? -46.275 34.538 -1.739 1.00 38.74 ? 210 ILE A CA 1 ATOM 1594 C C . ILE A 1 210 ? -44.985 33.755 -1.963 1.00 38.92 ? 210 ILE A C 1 ATOM 1595 O O . ILE A 1 210 ? -44.488 33.706 -3.086 1.00 39.22 ? 210 ILE A O 1 ATOM 1596 C CB . ILE A 1 210 ? -45.975 35.933 -1.175 1.00 38.33 ? 210 ILE A CB 1 ATOM 1597 C CG1 . ILE A 1 210 ? -47.182 36.830 -1.397 1.00 38.55 ? 210 ILE A CG1 1 ATOM 1598 C CG2 . ILE A 1 210 ? -44.759 36.558 -1.847 1.00 40.11 ? 210 ILE A CG2 1 ATOM 1599 C CD1 . ILE A 1 210 ? -47.235 38.018 -0.470 1.00 38.76 ? 210 ILE A CD1 1 ATOM 1600 N N . LEU A 1 211 ? -44.453 33.154 -0.898 1.00 39.05 ? 211 LEU A N 1 ATOM 1601 C CA . LEU A 1 211 ? -43.184 32.432 -0.969 1.00 39.73 ? 211 LEU A CA 1 ATOM 1602 C C . LEU A 1 211 ? -43.353 31.093 -1.665 1.00 41.01 ? 211 LEU A C 1 ATOM 1603 O O . LEU A 1 211 ? -42.590 30.767 -2.580 1.00 42.89 ? 211 LEU A O 1 ATOM 1604 C CB . LEU A 1 211 ? -42.585 32.226 0.427 1.00 40.16 ? 211 LEU A CB 1 ATOM 1605 C CG . LEU A 1 211 ? -42.107 33.479 1.190 1.00 40.35 ? 211 LEU A CG 1 ATOM 1606 C CD1 . LEU A 1 211 ? -41.788 33.163 2.641 1.00 40.32 ? 211 LEU A CD1 1 ATOM 1607 C CD2 . LEU A 1 211 ? -40.898 34.123 0.543 1.00 41.43 ? 211 LEU A CD2 1 ATOM 1608 N N . SER A 1 212 ? -44.367 30.336 -1.252 1.00 41.03 ? 212 SER A N 1 ATOM 1609 C CA . SER A 1 212 ? -44.587 28.963 -1.747 1.00 42.05 ? 212 SER A CA 1 ATOM 1610 C C . SER A 1 212 ? -44.945 28.903 -3.233 1.00 43.06 ? 212 SER A C 1 ATOM 1611 O O . SER A 1 212 ? -45.995 29.412 -3.636 1.00 44.18 ? 212 SER A O 1 ATOM 1612 C CB . SER A 1 212 ? -45.707 28.281 -0.956 1.00 41.64 ? 212 SER A CB 1 ATOM 1613 O OG . SER A 1 212 ? -45.805 26.913 -1.295 1.00 41.05 ? 212 SER A OG 1 ATOM 1614 N N . PRO A 1 213 ? -44.081 28.271 -4.047 1.00 42.71 ? 213 PRO A N 1 ATOM 1615 C CA . PRO A 1 213 ? -44.345 28.093 -5.470 1.00 43.30 ? 213 PRO A CA 1 ATOM 1616 C C . PRO A 1 213 ? -45.718 27.506 -5.811 1.00 43.49 ? 213 PRO A C 1 ATOM 1617 O O . PRO A 1 213 ? -46.350 27.954 -6.769 1.00 46.89 ? 213 PRO A O 1 ATOM 1618 C CB . PRO A 1 213 ? -43.241 27.131 -5.897 1.00 43.99 ? 213 PRO A CB 1 ATOM 1619 C CG . PRO A 1 213 ? -42.106 27.475 -5.013 1.00 43.18 ? 213 PRO A CG 1 ATOM 1620 C CD . PRO A 1 213 ? -42.727 27.807 -3.691 1.00 42.46 ? 213 PRO A CD 1 ATOM 1621 N N . GLY A 1 214 ? -46.172 26.511 -5.053 1.00 41.90 ? 214 GLY A N 1 ATOM 1622 C CA . GLY A 1 214 ? -47.480 25.897 -5.297 1.00 40.51 ? 214 GLY A CA 1 ATOM 1623 C C . GLY A 1 214 ? -48.671 26.827 -5.146 1.00 40.20 ? 214 GLY A C 1 ATOM 1624 O O . GLY A 1 214 ? -49.732 26.551 -5.685 1.00 40.93 ? 214 GLY A O 1 ATOM 1625 N N . SER A 1 215 ? -48.503 27.921 -4.400 1.00 39.70 ? 215 SER A N 1 ATOM 1626 C CA . SER A 1 215 ? -49.586 28.871 -4.124 1.00 39.26 ? 215 SER A CA 1 ATOM 1627 C C . SER A 1 215 ? -49.544 30.143 -4.978 1.00 39.26 ? 215 SER A C 1 ATOM 1628 O O . SER A 1 215 ? -50.571 30.785 -5.185 1.00 39.46 ? 215 SER A O 1 ATOM 1629 C CB . SER A 1 215 ? -49.545 29.280 -2.645 1.00 38.69 ? 215 SER A CB 1 ATOM 1630 O OG . SER A 1 215 ? -49.595 28.148 -1.788 1.00 37.96 ? 215 SER A OG 1 ATOM 1631 N N . ARG A 1 216 ? -48.362 30.507 -5.465 1.00 39.82 ? 216 ARG A N 1 ATOM 1632 C CA . ARG A 1 216 ? -48.156 31.783 -6.173 1.00 40.00 ? 216 ARG A CA 1 ATOM 1633 C C . ARG A 1 216 ? -49.127 32.063 -7.301 1.00 39.77 ? 216 ARG A C 1 ATOM 1634 O O . ARG A 1 216 ? -49.518 33.205 -7.492 1.00 39.61 ? 216 ARG A O 1 ATOM 1635 C CB . ARG A 1 216 ? -46.748 31.864 -6.760 1.00 40.38 ? 216 ARG A CB 1 ATOM 1636 C CG . ARG A 1 216 ? -45.655 31.943 -5.728 1.00 39.90 ? 216 ARG A CG 1 ATOM 1637 C CD . ARG A 1 216 ? -44.297 32.136 -6.364 1.00 41.51 ? 216 ARG A CD 1 ATOM 1638 N NE . ARG A 1 216 ? -43.257 31.784 -5.404 1.00 42.55 ? 216 ARG A NE 1 ATOM 1639 C CZ . ARG A 1 216 ? -41.988 31.535 -5.705 1.00 43.64 ? 216 ARG A CZ 1 ATOM 1640 N NH1 . ARG A 1 216 ? -41.557 31.600 -6.963 1.00 44.74 ? 216 ARG A NH1 1 ATOM 1641 N NH2 . ARG A 1 216 ? -41.145 31.223 -4.728 1.00 43.64 ? 216 ARG A NH2 1 ATOM 1642 N N . ASP A 1 217 ? -49.510 31.043 -8.058 1.00 40.40 ? 217 ASP A N 1 ATOM 1643 C CA . ASP A 1 217 ? -50.294 31.301 -9.266 1.00 42.81 ? 217 ASP A CA 1 ATOM 1644 C C . ASP A 1 217 ? -51.778 31.579 -9.013 1.00 43.82 ? 217 ASP A C 1 ATOM 1645 O O . ASP A 1 217 ? -52.479 31.993 -9.927 1.00 48.01 ? 217 ASP A O 1 ATOM 1646 C CB . ASP A 1 217 ? -50.141 30.155 -10.259 1.00 43.37 ? 217 ASP A CB 1 ATOM 1647 C CG . ASP A 1 217 ? -48.718 29.993 -10.748 1.00 43.33 ? 217 ASP A CG 1 ATOM 1648 O OD1 . ASP A 1 217 ? -47.824 30.711 -10.255 1.00 45.00 ? 217 ASP A OD1 1 ATOM 1649 O OD2 . ASP A 1 217 ? -48.484 29.130 -11.616 1.00 43.36 ? 217 ASP A OD2 1 ATOM 1650 N N . LEU A 1 218 ? -52.250 31.376 -7.783 1.00 42.85 ? 218 LEU A N 1 ATOM 1651 C CA . LEU A 1 218 ? -53.679 31.413 -7.476 1.00 41.13 ? 218 LEU A CA 1 ATOM 1652 C C . LEU A 1 218 ? -54.189 32.770 -6.943 1.00 41.33 ? 218 LEU A C 1 ATOM 1653 O O . LEU A 1 218 ? -55.340 32.869 -6.482 1.00 41.74 ? 218 LEU A O 1 ATOM 1654 C CB . LEU A 1 218 ? -54.000 30.323 -6.458 1.00 40.35 ? 218 LEU A CB 1 ATOM 1655 C CG . LEU A 1 218 ? -53.603 28.884 -6.796 1.00 40.69 ? 218 LEU A CG 1 ATOM 1656 C CD1 . LEU A 1 218 ? -53.680 27.992 -5.565 1.00 40.14 ? 218 LEU A CD1 1 ATOM 1657 C CD2 . LEU A 1 218 ? -54.499 28.316 -7.876 1.00 42.38 ? 218 LEU A CD2 1 ATOM 1658 N N . PHE A 1 219 ? -53.367 33.818 -7.008 1.00 39.60 ? 219 PHE A N 1 ATOM 1659 C CA . PHE A 1 219 ? -53.828 35.157 -6.602 1.00 38.51 ? 219 PHE A CA 1 ATOM 1660 C C . PHE A 1 219 ? -52.975 36.233 -7.262 1.00 39.20 ? 219 PHE A C 1 ATOM 1661 O O . PHE A 1 219 ? -51.880 35.952 -7.726 1.00 39.07 ? 219 PHE A O 1 ATOM 1662 C CB . PHE A 1 219 ? -53.815 35.312 -5.072 1.00 36.49 ? 219 PHE A CB 1 ATOM 1663 C CG . PHE A 1 219 ? -52.440 35.221 -4.458 1.00 35.22 ? 219 PHE A CG 1 ATOM 1664 C CD1 . PHE A 1 219 ? -51.849 33.987 -4.218 1.00 34.90 ? 219 PHE A CD1 1 ATOM 1665 C CD2 . PHE A 1 219 ? -51.745 36.362 -4.110 1.00 34.60 ? 219 PHE A CD2 1 ATOM 1666 C CE1 . PHE A 1 219 ? -50.587 33.896 -3.653 1.00 34.64 ? 219 PHE A CE1 1 ATOM 1667 C CE2 . PHE A 1 219 ? -50.477 36.281 -3.554 1.00 34.91 ? 219 PHE A CE2 1 ATOM 1668 C CZ . PHE A 1 219 ? -49.893 35.046 -3.327 1.00 34.49 ? 219 PHE A CZ 1 ATOM 1669 N N . ARG A 1 220 ? -53.484 37.458 -7.293 1.00 40.00 ? 220 ARG A N 1 ATOM 1670 C CA . ARG A 1 220 ? -52.831 38.557 -7.988 1.00 41.78 ? 220 ARG A CA 1 ATOM 1671 C C . ARG A 1 220 ? -52.024 39.414 -7.017 1.00 41.66 ? 220 ARG A C 1 ATOM 1672 O O . ARG A 1 220 ? -50.869 39.753 -7.309 1.00 41.87 ? 220 ARG A O 1 ATOM 1673 C CB . ARG A 1 220 ? -53.887 39.405 -8.694 1.00 43.80 ? 220 ARG A CB 1 ATOM 1674 C CG . ARG A 1 220 ? -53.379 40.630 -9.441 1.00 45.76 ? 220 ARG A CG 1 ATOM 1675 C CD . ARG A 1 220 ? -52.740 40.280 -10.767 1.00 47.53 ? 220 ARG A CD 1 ATOM 1676 N NE . ARG A 1 220 ? -52.678 41.427 -11.683 1.00 49.95 ? 220 ARG A NE 1 ATOM 1677 C CZ . ARG A 1 220 ? -53.578 41.727 -12.625 1.00 51.69 ? 220 ARG A CZ 1 ATOM 1678 N NH1 . ARG A 1 220 ? -54.673 40.998 -12.815 1.00 53.15 ? 220 ARG A NH1 1 ATOM 1679 N NH2 . ARG A 1 220 ? -53.380 42.778 -13.396 1.00 53.52 ? 220 ARG A NH2 1 ATOM 1680 N N . ARG A 1 221 ? -52.640 39.766 -5.883 1.00 40.44 ? 221 ARG A N 1 ATOM 1681 C CA . ARG A 1 221 ? -52.040 40.670 -4.887 1.00 40.49 ? 221 ARG A CA 1 ATOM 1682 C C . ARG A 1 221 ? -52.283 40.177 -3.488 1.00 38.46 ? 221 ARG A C 1 ATOM 1683 O O . ARG A 1 221 ? -53.034 39.232 -3.283 1.00 38.92 ? 221 ARG A O 1 ATOM 1684 C CB . ARG A 1 221 ? -52.662 42.060 -4.957 1.00 42.39 ? 221 ARG A CB 1 ATOM 1685 C CG . ARG A 1 221 ? -52.816 42.603 -6.342 1.00 44.63 ? 221 ARG A CG 1 ATOM 1686 C CD . ARG A 1 221 ? -53.172 44.075 -6.334 1.00 46.00 ? 221 ARG A CD 1 ATOM 1687 N NE . ARG A 1 221 ? -52.829 44.610 -7.646 1.00 47.97 ? 221 ARG A NE 1 ATOM 1688 C CZ . ARG A 1 221 ? -53.609 44.567 -8.712 1.00 48.37 ? 221 ARG A CZ 1 ATOM 1689 N NH1 . ARG A 1 221 ? -54.830 44.061 -8.644 1.00 49.16 ? 221 ARG A NH1 1 ATOM 1690 N NH2 . ARG A 1 221 ? -53.166 45.067 -9.849 1.00 51.60 ? 221 ARG A NH2 1 ATOM 1691 N N . ALA A 1 222 ? -51.707 40.878 -2.516 1.00 38.36 ? 222 ALA A N 1 ATOM 1692 C CA . ALA A 1 222 ? -51.725 40.430 -1.125 1.00 37.03 ? 222 ALA A CA 1 ATOM 1693 C C . ALA A 1 222 ? -51.772 41.594 -0.155 1.00 37.57 ? 222 ALA A C 1 ATOM 1694 O O . ALA A 1 222 ? -51.183 42.644 -0.407 1.00 39.17 ? 222 ALA A O 1 ATOM 1695 C CB . ALA A 1 222 ? -50.508 39.558 -0.841 1.00 35.36 ? 222 ALA A CB 1 ATOM 1696 N N . ILE A 1 223 ? -52.487 41.395 0.950 1.00 37.49 ? 223 ILE A N 1 ATOM 1697 C CA . ILE A 1 223 ? -52.463 42.312 2.086 1.00 37.61 ? 223 ILE A CA 1 ATOM 1698 C C . ILE A 1 223 ? -52.110 41.524 3.358 1.00 35.94 ? 223 ILE A C 1 ATOM 1699 O O . ILE A 1 223 ? -52.703 40.487 3.640 1.00 35.39 ? 223 ILE A O 1 ATOM 1700 C CB . ILE A 1 223 ? -53.819 43.028 2.249 1.00 37.83 ? 223 ILE A CB 1 ATOM 1701 C CG1 . ILE A 1 223 ? -54.113 43.892 1.020 1.00 39.20 ? 223 ILE A CG1 1 ATOM 1702 C CG2 . ILE A 1 223 ? -53.860 43.859 3.532 1.00 37.40 ? 223 ILE A CG2 1 ATOM 1703 C CD1 . ILE A 1 223 ? -55.527 44.431 0.962 1.00 39.76 ? 223 ILE A CD1 1 ATOM 1704 N N . LEU A 1 224 ? -51.140 42.021 4.115 1.00 35.55 ? 224 LEU A N 1 ATOM 1705 C CA . LEU A 1 224 ? -50.699 41.366 5.351 1.00 35.16 ? 224 LEU A CA 1 ATOM 1706 C C . LEU A 1 224 ? -50.917 42.320 6.523 1.00 35.74 ? 224 LEU A C 1 ATOM 1707 O O . LEU A 1 224 ? -50.354 43.407 6.538 1.00 36.06 ? 224 LEU A O 1 ATOM 1708 C CB . LEU A 1 224 ? -49.212 41.009 5.269 1.00 34.32 ? 224 LEU A CB 1 ATOM 1709 C CG . LEU A 1 224 ? -48.764 40.011 4.192 1.00 34.07 ? 224 LEU A CG 1 ATOM 1710 C CD1 . LEU A 1 224 ? -48.600 40.675 2.831 1.00 34.91 ? 224 LEU A CD1 1 ATOM 1711 C CD2 . LEU A 1 224 ? -47.473 39.313 4.586 1.00 33.06 ? 224 LEU A CD2 1 ATOM 1712 N N . GLN A 1 225 ? -51.732 41.916 7.495 1.00 36.12 ? 225 GLN A N 1 ATOM 1713 C CA . GLN A 1 225 ? -52.026 42.749 8.664 1.00 36.99 ? 225 GLN A CA 1 ATOM 1714 C C . GLN A 1 225 ? -51.427 42.153 9.926 1.00 35.45 ? 225 GLN A C 1 ATOM 1715 O O . GLN A 1 225 ? -51.824 41.087 10.358 1.00 35.85 ? 225 GLN A O 1 ATOM 1716 C CB . GLN A 1 225 ? -53.535 42.894 8.822 1.00 38.98 ? 225 GLN A CB 1 ATOM 1717 C CG . GLN A 1 225 ? -54.170 43.674 7.684 1.00 41.88 ? 225 GLN A CG 1 ATOM 1718 C CD . GLN A 1 225 ? -55.669 43.494 7.586 1.00 44.44 ? 225 GLN A CD 1 ATOM 1719 O OE1 . GLN A 1 225 ? -56.223 43.485 6.488 1.00 46.70 ? 225 GLN A OE1 1 ATOM 1720 N NE2 . GLN A 1 225 ? -56.336 43.360 8.729 1.00 44.92 ? 225 GLN A NE2 1 ATOM 1721 N N . SER A 1 226 ? -50.458 42.836 10.511 1.00 35.89 ? 226 SER A N 1 ATOM 1722 C CA . SER A 1 226 ? -49.833 42.381 11.763 1.00 36.13 ? 226 SER A CA 1 ATOM 1723 C C . SER A 1 226 ? -49.403 40.916 11.700 1.00 35.16 ? 226 SER A C 1 ATOM 1724 O O . SER A 1 226 ? -49.659 40.135 12.597 1.00 35.21 ? 226 SER A O 1 ATOM 1725 C CB . SER A 1 226 ? -50.773 42.609 12.949 1.00 35.84 ? 226 SER A CB 1 ATOM 1726 O OG . SER A 1 226 ? -51.193 43.967 13.017 1.00 37.21 ? 226 SER A OG 1 ATOM 1727 N N . GLY A 1 227 ? -48.738 40.551 10.622 1.00 35.52 ? 227 GLY A N 1 ATOM 1728 C CA . GLY A 1 227 ? -48.235 39.197 10.474 1.00 35.35 ? 227 GLY A CA 1 ATOM 1729 C C . GLY A 1 227 ? -47.370 39.125 9.240 1.00 35.31 ? 227 GLY A C 1 ATOM 1730 O O . GLY A 1 227 ? -47.624 39.826 8.260 1.00 35.73 ? 227 GLY A O 1 ATOM 1731 N N . SER A 1 228 ? -46.325 38.314 9.294 1.00 34.85 ? 228 SER A N 1 ATOM 1732 C CA . SER A 1 228 ? -45.494 38.099 8.119 1.00 35.99 ? 228 SER A CA 1 ATOM 1733 C C . SER A 1 228 ? -44.864 36.732 8.248 1.00 35.54 ? 228 SER A C 1 ATOM 1734 O O . SER A 1 228 ? -44.770 36.214 9.342 1.00 36.90 ? 228 SER A O 1 ATOM 1735 C CB . SER A 1 228 ? -44.467 39.224 7.948 1.00 36.45 ? 228 SER A CB 1 ATOM 1736 O OG . SER A 1 228 ? -43.382 39.092 8.826 1.00 37.05 ? 228 SER A OG 1 ATOM 1737 N N . PRO A 1 229 ? -44.476 36.120 7.124 1.00 36.91 ? 229 PRO A N 1 ATOM 1738 C CA . PRO A 1 229 ? -44.185 34.689 7.185 1.00 36.66 ? 229 PRO A CA 1 ATOM 1739 C C . PRO A 1 229 ? -42.996 34.372 8.073 1.00 35.73 ? 229 PRO A C 1 ATOM 1740 O O . PRO A 1 229 ? -42.976 33.324 8.692 1.00 35.76 ? 229 PRO A O 1 ATOM 1741 C CB . PRO A 1 229 ? -43.917 34.319 5.727 1.00 38.45 ? 229 PRO A CB 1 ATOM 1742 C CG . PRO A 1 229 ? -43.457 35.586 5.088 1.00 39.26 ? 229 PRO A CG 1 ATOM 1743 C CD . PRO A 1 229 ? -44.153 36.705 5.810 1.00 38.08 ? 229 PRO A CD 1 ATOM 1744 N N . ASN A 1 230 ? -42.050 35.304 8.170 1.00 35.91 ? 230 ASN A N 1 ATOM 1745 C CA . ASN A 1 230 ? -40.839 35.138 8.991 1.00 34.84 ? 230 ASN A CA 1 ATOM 1746 C C . ASN A 1 230 ? -40.982 35.448 10.481 1.00 35.36 ? 230 ASN A C 1 ATOM 1747 O O . ASN A 1 230 ? -40.001 35.391 11.207 1.00 36.35 ? 230 ASN A O 1 ATOM 1748 C CB . ASN A 1 230 ? -39.720 36.011 8.437 1.00 34.33 ? 230 ASN A CB 1 ATOM 1749 C CG . ASN A 1 230 ? -40.058 37.478 8.484 1.00 33.90 ? 230 ASN A CG 1 ATOM 1750 O OD1 . ASN A 1 230 ? -41.135 37.876 8.072 1.00 33.50 ? 230 ASN A OD1 1 ATOM 1751 N ND2 . ASN A 1 230 ? -39.136 38.293 8.974 1.00 35.80 ? 230 ASN A ND2 1 ATOM 1752 N N . CYS A 1 231 ? -42.178 35.791 10.948 1.00 35.43 ? 231 CYS A N 1 ATOM 1753 C CA . CYS A 1 231 ? -42.399 35.966 12.382 1.00 35.42 ? 231 CYS A CA 1 ATOM 1754 C C . CYS A 1 231 ? -41.904 34.708 13.136 1.00 35.28 ? 231 CYS A C 1 ATOM 1755 O O . CYS A 1 231 ? -42.102 33.588 12.667 1.00 34.86 ? 231 CYS A O 1 ATOM 1756 C CB . CYS A 1 231 ? -43.888 36.241 12.679 1.00 35.56 ? 231 CYS A CB 1 ATOM 1757 S SG . CYS A 1 231 ? -44.508 37.867 12.128 1.00 36.89 ? 231 CYS A SG 1 ATOM 1758 N N . PRO A 1 232 ? -41.256 34.889 14.308 1.00 35.91 ? 232 PRO A N 1 ATOM 1759 C CA . PRO A 1 232 ? -40.661 33.740 15.001 1.00 35.74 ? 232 PRO A CA 1 ATOM 1760 C C . PRO A 1 232 ? -41.679 32.699 15.494 1.00 36.00 ? 232 PRO A C 1 ATOM 1761 O O . PRO A 1 232 ? -41.340 31.521 15.648 1.00 36.58 ? 232 PRO A O 1 ATOM 1762 C CB . PRO A 1 232 ? -39.916 34.383 16.176 1.00 35.90 ? 232 PRO A CB 1 ATOM 1763 C CG . PRO A 1 232 ? -40.564 35.698 16.395 1.00 35.00 ? 232 PRO A CG 1 ATOM 1764 C CD . PRO A 1 232 ? -41.096 36.144 15.074 1.00 35.18 ? 232 PRO A CD 1 ATOM 1765 N N . TRP A 1 233 ? -42.913 33.135 15.730 1.00 35.87 ? 233 TRP A N 1 ATOM 1766 C CA . TRP A 1 233 ? -43.980 32.247 16.207 1.00 35.33 ? 233 TRP A CA 1 ATOM 1767 C C . TRP A 1 233 ? -44.647 31.511 15.076 1.00 34.99 ? 233 TRP A C 1 ATOM 1768 O O . TRP A 1 233 ? -45.408 30.600 15.323 1.00 36.70 ? 233 TRP A O 1 ATOM 1769 C CB . TRP A 1 233 ? -45.041 33.039 16.981 1.00 35.12 ? 233 TRP A CB 1 ATOM 1770 C CG . TRP A 1 233 ? -45.495 34.269 16.278 1.00 35.29 ? 233 TRP A CG 1 ATOM 1771 C CD1 . TRP A 1 233 ? -44.990 35.525 16.429 1.00 36.33 ? 233 TRP A CD1 1 ATOM 1772 C CD2 . TRP A 1 233 ? -46.512 34.365 15.283 1.00 34.56 ? 233 TRP A CD2 1 ATOM 1773 N NE1 . TRP A 1 233 ? -45.639 36.402 15.601 1.00 36.04 ? 233 TRP A NE1 1 ATOM 1774 C CE2 . TRP A 1 233 ? -46.581 35.718 14.887 1.00 34.33 ? 233 TRP A CE2 1 ATOM 1775 C CE3 . TRP A 1 233 ? -47.380 33.443 14.692 1.00 34.72 ? 233 TRP A CE3 1 ATOM 1776 C CZ2 . TRP A 1 233 ? -47.478 36.173 13.931 1.00 33.90 ? 233 TRP A CZ2 1 ATOM 1777 C CZ3 . TRP A 1 233 ? -48.285 33.900 13.744 1.00 34.76 ? 233 TRP A CZ3 1 ATOM 1778 C CH2 . TRP A 1 233 ? -48.322 35.255 13.369 1.00 34.42 ? 233 TRP A CH2 1 ATOM 1779 N N . ALA A 1 234 ? -44.355 31.896 13.837 1.00 35.72 ? 234 ALA A N 1 ATOM 1780 C CA . ALA A 1 234 ? -45.116 31.448 12.673 1.00 34.68 ? 234 ALA A CA 1 ATOM 1781 C C . ALA A 1 234 ? -44.624 30.156 12.036 1.00 35.54 ? 234 ALA A C 1 ATOM 1782 O O . ALA A 1 234 ? -45.324 29.592 11.205 1.00 36.95 ? 234 ALA A O 1 ATOM 1783 C CB . ALA A 1 234 ? -45.141 32.549 11.628 1.00 35.13 ? 234 ALA A CB 1 ATOM 1784 N N . SER A 1 235 ? -43.431 29.683 12.386 1.00 36.78 ? 235 SER A N 1 ATOM 1785 C CA . SER A 1 235 ? -42.949 28.406 11.838 1.00 37.17 ? 235 SER A CA 1 ATOM 1786 C C . SER A 1 235 ? -41.928 27.723 12.734 1.00 38.38 ? 235 SER A C 1 ATOM 1787 O O . SER A 1 235 ? -41.445 28.309 13.692 1.00 39.44 ? 235 SER A O 1 ATOM 1788 C CB . SER A 1 235 ? -42.360 28.601 10.440 1.00 37.19 ? 235 SER A CB 1 ATOM 1789 O OG . SER A 1 235 ? -41.209 29.419 10.473 1.00 36.43 ? 235 SER A OG 1 ATOM 1790 N N . VAL A 1 236 ? -41.629 26.466 12.422 1.00 39.31 ? 236 VAL A N 1 ATOM 1791 C CA . VAL A 1 236 ? -40.633 25.679 13.151 1.00 40.03 ? 236 VAL A CA 1 ATOM 1792 C C . VAL A 1 236 ? -39.914 24.728 12.202 1.00 40.54 ? 236 VAL A C 1 ATOM 1793 O O . VAL A 1 236 ? -40.441 24.379 11.151 1.00 40.38 ? 236 VAL A O 1 ATOM 1794 C CB . VAL A 1 236 ? -41.263 24.832 14.277 1.00 40.19 ? 236 VAL A CB 1 ATOM 1795 C CG1 . VAL A 1 236 ? -41.968 25.716 15.287 1.00 39.57 ? 236 VAL A CG1 1 ATOM 1796 C CG2 . VAL A 1 236 ? -42.217 23.782 13.719 1.00 40.04 ? 236 VAL A CG2 1 ATOM 1797 N N . SER A 1 237 ? -38.718 24.304 12.583 1.00 41.07 ? 237 SER A N 1 ATOM 1798 C CA . SER A 1 237 ? -37.963 23.355 11.787 1.00 42.77 ? 237 SER A CA 1 ATOM 1799 C C . SER A 1 237 ? -38.665 22.010 11.849 1.00 44.58 ? 237 SER A C 1 ATOM 1800 O O . SER A 1 237 ? -39.504 21.790 12.726 1.00 45.97 ? 237 SER A O 1 ATOM 1801 C CB . SER A 1 237 ? -36.555 23.204 12.348 1.00 43.84 ? 237 SER A CB 1 ATOM 1802 O OG . SER A 1 237 ? -36.606 22.553 13.603 1.00 44.77 ? 237 SER A OG 1 ATOM 1803 N N . VAL A 1 238 ? -38.309 21.098 10.950 1.00 45.15 ? 238 VAL A N 1 ATOM 1804 C CA . VAL A 1 238 ? -38.965 19.793 10.925 1.00 45.07 ? 238 VAL A CA 1 ATOM 1805 C C . VAL A 1 238 ? -38.588 18.986 12.154 1.00 44.55 ? 238 VAL A C 1 ATOM 1806 O O . VAL A 1 238 ? -39.392 18.219 12.661 1.00 46.59 ? 238 VAL A O 1 ATOM 1807 C CB . VAL A 1 238 ? -38.697 18.995 9.620 1.00 45.90 ? 238 VAL A CB 1 ATOM 1808 C CG1 . VAL A 1 238 ? -38.979 19.863 8.401 1.00 46.22 ? 238 VAL A CG1 1 ATOM 1809 C CG2 . VAL A 1 238 ? -37.285 18.456 9.564 1.00 46.84 ? 238 VAL A CG2 1 ATOM 1810 N N . ALA A 1 239 ? -37.374 19.169 12.648 1.00 45.22 ? 239 ALA A N 1 ATOM 1811 C CA . ALA A 1 239 ? -36.965 18.494 13.878 1.00 45.84 ? 239 ALA A CA 1 ATOM 1812 C C . ALA A 1 239 ? -37.805 18.994 15.043 1.00 44.73 ? 239 ALA A C 1 ATOM 1813 O O . ALA A 1 239 ? -38.193 18.210 15.900 1.00 46.60 ? 239 ALA A O 1 ATOM 1814 C CB . ALA A 1 239 ? -35.490 18.717 14.151 1.00 46.32 ? 239 ALA A CB 1 ATOM 1815 N N . GLU A 1 240 ? -38.102 20.291 15.067 1.00 42.71 ? 240 GLU A N 1 ATOM 1816 C CA . GLU A 1 240 ? -38.949 20.845 16.117 1.00 42.15 ? 240 GLU A CA 1 ATOM 1817 C C . GLU A 1 240 ? -40.401 20.367 15.996 1.00 41.87 ? 240 GLU A C 1 ATOM 1818 O O . GLU A 1 240 ? -41.027 20.020 16.992 1.00 41.41 ? 240 GLU A O 1 ATOM 1819 C CB . GLU A 1 240 ? -38.866 22.367 16.125 1.00 41.16 ? 240 GLU A CB 1 ATOM 1820 C CG . GLU A 1 240 ? -39.646 23.036 17.251 1.00 40.93 ? 240 GLU A CG 1 ATOM 1821 C CD . GLU A 1 240 ? -39.234 22.571 18.629 1.00 42.83 ? 240 GLU A CD 1 ATOM 1822 O OE1 . GLU A 1 240 ? -38.070 22.141 18.805 1.00 43.99 ? 240 GLU A OE1 1 ATOM 1823 O OE2 . GLU A 1 240 ? -40.078 22.651 19.547 1.00 44.37 ? 240 GLU A OE2 1 ATOM 1824 N N . GLY A 1 241 ? -40.925 20.329 14.776 1.00 42.73 ? 241 GLY A N 1 ATOM 1825 C CA . GLY A 1 241 ? -42.244 19.742 14.522 1.00 43.35 ? 241 GLY A CA 1 ATOM 1826 C C . GLY A 1 241 ? -42.331 18.304 15.003 1.00 45.02 ? 241 GLY A C 1 ATOM 1827 O O . GLY A 1 241 ? -43.341 17.865 15.551 1.00 45.30 ? 241 GLY A O 1 ATOM 1828 N N . ARG A 1 242 ? -41.247 17.577 14.800 1.00 47.49 ? 242 ARG A N 1 ATOM 1829 C CA . ARG A 1 242 ? -41.172 16.190 15.195 1.00 49.93 ? 242 ARG A CA 1 ATOM 1830 C C . ARG A 1 242 ? -41.163 16.079 16.712 1.00 50.20 ? 242 ARG A C 1 ATOM 1831 O O . ARG A 1 242 ? -41.943 15.322 17.277 1.00 52.88 ? 242 ARG A O 1 ATOM 1832 C CB . ARG A 1 242 ? -39.925 15.552 14.590 1.00 51.53 ? 242 ARG A CB 1 ATOM 1833 C CG . ARG A 1 242 ? -39.864 14.044 14.718 1.00 54.25 ? 242 ARG A CG 1 ATOM 1834 C CD . ARG A 1 242 ? -38.898 13.450 13.700 1.00 55.32 ? 242 ARG A CD 1 ATOM 1835 N NE . ARG A 1 242 ? -39.542 13.208 12.406 1.00 54.72 ? 242 ARG A NE 1 ATOM 1836 C CZ . ARG A 1 242 ? -40.358 12.182 12.149 1.00 55.86 ? 242 ARG A CZ 1 ATOM 1837 N NH1 . ARG A 1 242 ? -40.657 11.296 13.099 1.00 56.26 ? 242 ARG A NH1 1 ATOM 1838 N NH2 . ARG A 1 242 ? -40.890 12.041 10.938 1.00 56.08 ? 242 ARG A NH2 1 ATOM 1839 N N . ARG A 1 243 ? -40.303 16.845 17.374 1.00 49.09 ? 243 ARG A N 1 ATOM 1840 C CA . ARG A 1 243 ? -40.214 16.778 18.833 1.00 49.32 ? 243 ARG A CA 1 ATOM 1841 C C . ARG A 1 243 ? -41.564 17.011 19.496 1.00 46.48 ? 243 ARG A C 1 ATOM 1842 O O . ARG A 1 243 ? -41.936 16.278 20.408 1.00 45.95 ? 243 ARG A O 1 ATOM 1843 C CB . ARG A 1 243 ? -39.178 17.765 19.373 1.00 50.75 ? 243 ARG A CB 1 ATOM 1844 C CG . ARG A 1 243 ? -37.745 17.244 19.301 1.00 53.48 ? 243 ARG A CG 1 ATOM 1845 C CD . ARG A 1 243 ? -36.745 18.232 19.900 1.00 54.49 ? 243 ARG A CD 1 ATOM 1846 N NE . ARG A 1 243 ? -36.671 19.469 19.114 1.00 53.53 ? 243 ARG A NE 1 ATOM 1847 C CZ . ARG A 1 243 ? -35.787 19.723 18.146 1.00 52.95 ? 243 ARG A CZ 1 ATOM 1848 N NH1 . ARG A 1 243 ? -34.846 18.841 17.812 1.00 53.69 ? 243 ARG A NH1 1 ATOM 1849 N NH2 . ARG A 1 243 ? -35.843 20.888 17.508 1.00 51.66 ? 243 ARG A NH2 1 ATOM 1850 N N . ARG A 1 244 ? -42.295 18.013 19.009 1.00 44.35 ? 244 ARG A N 1 ATOM 1851 C CA . ARG A 1 244 ? -43.591 18.409 19.588 1.00 43.05 ? 244 ARG A CA 1 ATOM 1852 C C . ARG A 1 244 ? -44.684 17.391 19.304 1.00 43.25 ? 244 ARG A C 1 ATOM 1853 O O . ARG A 1 244 ? -45.486 17.067 20.187 1.00 44.78 ? 244 ARG A O 1 ATOM 1854 C CB . ARG A 1 244 ? -44.040 19.767 19.047 1.00 40.55 ? 244 ARG A CB 1 ATOM 1855 C CG . ARG A 1 244 ? -43.123 20.909 19.423 1.00 39.08 ? 244 ARG A CG 1 ATOM 1856 C CD . ARG A 1 244 ? -43.643 22.210 18.859 1.00 37.47 ? 244 ARG A CD 1 ATOM 1857 N NE . ARG A 1 244 ? -42.719 23.309 19.119 1.00 37.04 ? 244 ARG A NE 1 ATOM 1858 C CZ . ARG A 1 244 ? -43.015 24.597 18.971 1.00 35.84 ? 244 ARG A CZ 1 ATOM 1859 N NH1 . ARG A 1 244 ? -44.216 24.992 18.578 1.00 35.20 ? 244 ARG A NH1 1 ATOM 1860 N NH2 . ARG A 1 244 ? -42.102 25.504 19.233 1.00 36.89 ? 244 ARG A NH2 1 ATOM 1861 N N . ALA A 1 245 ? -44.722 16.905 18.068 1.00 41.60 ? 245 ALA A N 1 ATOM 1862 C CA . ALA A 1 245 ? -45.624 15.820 17.704 1.00 41.60 ? 245 ALA A CA 1 ATOM 1863 C C . ALA A 1 245 ? -45.470 14.622 18.638 1.00 41.96 ? 245 ALA A C 1 ATOM 1864 O O . ALA A 1 245 ? -46.449 14.078 19.108 1.00 41.88 ? 245 ALA A O 1 ATOM 1865 C CB . ALA A 1 245 ? -45.372 15.390 16.268 1.00 42.15 ? 245 ALA A CB 1 ATOM 1866 N N . VAL A 1 246 ? -44.234 14.212 18.890 1.00 42.40 ? 246 VAL A N 1 ATOM 1867 C CA . VAL A 1 246 ? -43.961 13.074 19.767 1.00 44.58 ? 246 VAL A CA 1 ATOM 1868 C C . VAL A 1 246 ? -44.333 13.401 21.215 1.00 45.22 ? 246 VAL A C 1 ATOM 1869 O O . VAL A 1 246 ? -44.881 12.550 21.931 1.00 46.47 ? 246 VAL A O 1 ATOM 1870 C CB . VAL A 1 246 ? -42.468 12.650 19.687 1.00 45.34 ? 246 VAL A CB 1 ATOM 1871 C CG1 . VAL A 1 246 ? -42.110 11.632 20.765 1.00 46.39 ? 246 VAL A CG1 1 ATOM 1872 C CG2 . VAL A 1 246 ? -42.150 12.102 18.300 1.00 45.37 ? 246 VAL A CG2 1 ATOM 1873 N N . GLU A 1 247 ? -44.033 14.631 21.635 1.00 44.45 ? 247 GLU A N 1 ATOM 1874 C CA . GLU A 1 247 ? -44.322 15.070 22.984 1.00 44.89 ? 247 GLU A CA 1 ATOM 1875 C C . GLU A 1 247 ? -45.831 15.096 23.231 1.00 45.11 ? 247 GLU A C 1 ATOM 1876 O O . GLU A 1 247 ? -46.292 14.719 24.302 1.00 47.01 ? 247 GLU A O 1 ATOM 1877 C CB . GLU A 1 247 ? -43.665 16.420 23.252 1.00 43.72 ? 247 GLU A CB 1 ATOM 1878 C CG . GLU A 1 247 ? -43.785 16.931 24.680 1.00 45.58 ? 247 GLU A CG 1 ATOM 1879 C CD . GLU A 1 247 ? -43.329 15.934 25.749 1.00 49.04 ? 247 GLU A CD 1 ATOM 1880 O OE1 . GLU A 1 247 ? -42.556 14.992 25.427 1.00 50.56 ? 247 GLU A OE1 1 ATOM 1881 O OE2 . GLU A 1 247 ? -43.757 16.099 26.923 1.00 49.20 ? 247 GLU A OE2 1 ATOM 1882 N N . LEU A 1 248 ? -46.602 15.486 22.227 1.00 44.34 ? 248 LEU A N 1 ATOM 1883 C CA . LEU A 1 248 ? -48.055 15.379 22.299 1.00 44.98 ? 248 LEU A CA 1 ATOM 1884 C C . LEU A 1 248 ? -48.448 13.935 22.555 1.00 48.15 ? 248 LEU A C 1 ATOM 1885 O O . LEU A 1 248 ? -49.161 13.624 23.510 1.00 50.04 ? 248 LEU A O 1 ATOM 1886 C CB . LEU A 1 248 ? -48.670 15.860 20.990 1.00 44.44 ? 248 LEU A CB 1 ATOM 1887 C CG . LEU A 1 248 ? -50.189 15.792 20.821 1.00 45.26 ? 248 LEU A CG 1 ATOM 1888 C CD1 . LEU A 1 248 ? -50.883 16.718 21.813 1.00 45.53 ? 248 LEU A CD1 1 ATOM 1889 C CD2 . LEU A 1 248 ? -50.577 16.151 19.394 1.00 43.88 ? 248 LEU A CD2 1 ATOM 1890 N N . GLY A 1 249 ? -47.959 13.048 21.695 1.00 49.98 ? 249 GLY A N 1 ATOM 1891 C CA . GLY A 1 249 ? -48.177 11.617 21.837 1.00 51.21 ? 249 GLY A CA 1 ATOM 1892 C C . GLY A 1 249 ? -47.830 11.137 23.224 1.00 52.63 ? 249 GLY A C 1 ATOM 1893 O O . GLY A 1 249 ? -48.578 10.369 23.820 1.00 53.43 ? 249 GLY A O 1 ATOM 1894 N N . ARG A 1 250 ? -46.706 11.605 23.750 1.00 53.42 ? 250 ARG A N 1 ATOM 1895 C CA . ARG A 1 250 ? -46.281 11.197 25.085 1.00 57.18 ? 250 ARG A CA 1 ATOM 1896 C C . ARG A 1 250 ? -47.246 11.685 26.168 1.00 56.03 ? 250 ARG A C 1 ATOM 1897 O O . ARG A 1 250 ? -47.497 10.973 27.129 1.00 57.04 ? 250 ARG A O 1 ATOM 1898 C CB . ARG A 1 250 ? -44.869 11.681 25.381 1.00 60.11 ? 250 ARG A CB 1 ATOM 1899 C CG . ARG A 1 250 ? -44.134 10.793 26.368 1.00 64.92 ? 250 ARG A CG 1 ATOM 1900 C CD . ARG A 1 250 ? -42.755 11.351 26.641 1.00 67.75 ? 250 ARG A CD 1 ATOM 1901 N NE . ARG A 1 250 ? -42.870 12.673 27.253 1.00 70.72 ? 250 ARG A NE 1 ATOM 1902 C CZ . ARG A 1 250 ? -43.141 12.902 28.544 1.00 74.45 ? 250 ARG A CZ 1 ATOM 1903 N NH1 . ARG A 1 250 ? -43.317 11.897 29.404 1.00 77.39 ? 250 ARG A NH1 1 ATOM 1904 N NH2 . ARG A 1 250 ? -43.230 14.154 28.985 1.00 73.75 ? 250 ARG A NH2 1 ATOM 1905 N N . ASN A 1 251 ? -47.791 12.887 25.995 1.00 53.77 ? 251 ASN A N 1 ATOM 1906 C CA . ASN A 1 251 ? -48.803 13.432 26.909 1.00 53.70 ? 251 ASN A CA 1 ATOM 1907 C C . ASN A 1 251 ? -50.108 12.659 26.921 1.00 54.59 ? 251 ASN A C 1 ATOM 1908 O O . ASN A 1 251 ? -50.836 12.702 27.907 1.00 54.90 ? 251 ASN A O 1 ATOM 1909 C CB . ASN A 1 251 ? -49.119 14.891 26.568 1.00 52.38 ? 251 ASN A CB 1 ATOM 1910 C CG . ASN A 1 251 ? -48.222 15.863 27.294 1.00 51.97 ? 251 ASN A CG 1 ATOM 1911 O OD1 . ASN A 1 251 ? -48.402 16.106 28.478 1.00 52.42 ? 251 ASN A OD1 1 ATOM 1912 N ND2 . ASN A 1 251 ? -47.258 16.434 26.582 1.00 51.84 ? 251 ASN A ND2 1 ATOM 1913 N N . LEU A 1 252 ? -50.412 11.981 25.817 1.00 55.36 ? 252 LEU A N 1 ATOM 1914 C CA . LEU A 1 252 ? -51.597 11.121 25.729 1.00 56.93 ? 252 LEU A CA 1 ATOM 1915 C C . LEU A 1 252 ? -51.309 9.626 25.881 1.00 58.77 ? 252 LEU A C 1 ATOM 1916 O O . LEU A 1 252 ? -52.150 8.803 25.531 1.00 57.43 ? 252 LEU A O 1 ATOM 1917 C CB . LEU A 1 252 ? -52.306 11.367 24.405 1.00 55.48 ? 252 LEU A CB 1 ATOM 1918 C CG . LEU A 1 252 ? -52.798 12.797 24.247 1.00 53.31 ? 252 LEU A CG 1 ATOM 1919 C CD1 . LEU A 1 252 ? -53.085 13.072 22.788 1.00 52.13 ? 252 LEU A CD1 1 ATOM 1920 C CD2 . LEU A 1 252 ? -54.029 13.047 25.105 1.00 53.84 ? 252 LEU A CD2 1 ATOM 1921 N N . ASN A 1 253 ? -50.140 9.290 26.427 1.00 62.07 ? 253 ASN A N 1 ATOM 1922 C CA . ASN A 1 253 ? -49.734 7.896 26.670 1.00 66.97 ? 253 ASN A CA 1 ATOM 1923 C C . ASN A 1 253 ? -49.762 7.051 25.398 1.00 67.10 ? 253 ASN A C 1 ATOM 1924 O O . ASN A 1 253 ? -50.163 5.888 25.426 1.00 67.44 ? 253 ASN A O 1 ATOM 1925 C CB . ASN A 1 253 ? -50.606 7.250 27.763 1.00 70.80 ? 253 ASN A CB 1 ATOM 1926 C CG . ASN A 1 253 ? -50.814 8.168 28.961 1.00 72.76 ? 253 ASN A CG 1 ATOM 1927 O OD1 . ASN A 1 253 ? -51.905 8.717 29.160 1.00 74.22 ? 253 ASN A OD1 1 ATOM 1928 N ND2 . ASN A 1 253 ? -49.760 8.367 29.746 1.00 73.23 ? 253 ASN A ND2 1 ATOM 1929 N N . CYS A 1 254 ? -49.339 7.650 24.287 1.00 65.53 ? 254 CYS A N 1 ATOM 1930 C CA . CYS A 1 254 ? -49.329 6.961 23.014 1.00 64.97 ? 254 CYS A CA 1 ATOM 1931 C C . CYS A 1 254 ? -48.078 6.126 22.878 1.00 67.02 ? 254 CYS A C 1 ATOM 1932 O O . CYS A 1 254 ? -47.050 6.403 23.509 1.00 66.70 ? 254 CYS A O 1 ATOM 1933 C CB . CYS A 1 254 ? -49.402 7.933 21.844 1.00 63.74 ? 254 CYS A CB 1 ATOM 1934 S SG . CYS A 1 254 ? -51.044 8.616 21.519 1.00 64.40 ? 254 CYS A SG 1 ATOM 1935 N N . ASN A 1 255 ? -48.197 5.093 22.046 1.00 68.53 ? 255 ASN A N 1 ATOM 1936 C CA . ASN A 1 255 ? -47.082 4.265 21.635 1.00 68.88 ? 255 ASN A CA 1 ATOM 1937 C C . ASN A 1 255 ? -46.170 5.071 20.723 1.00 66.16 ? 255 ASN A C 1 ATOM 1938 O O . ASN A 1 255 ? -46.594 5.523 19.661 1.00 63.77 ? 255 ASN A O 1 ATOM 1939 C CB . ASN A 1 255 ? -47.607 3.046 20.887 1.00 70.72 ? 255 ASN A CB 1 ATOM 1940 C CG . ASN A 1 255 ? -46.521 2.050 20.569 1.00 72.83 ? 255 ASN A CG 1 ATOM 1941 O OD1 . ASN A 1 255 ? -45.421 2.414 20.153 1.00 72.72 ? 255 ASN A OD1 1 ATOM 1942 N ND2 . ASN A 1 255 ? -46.825 0.782 20.764 1.00 75.16 ? 255 ASN A ND2 1 ATOM 1943 N N . LEU A 1 256 ? -44.920 5.251 21.133 1.00 65.89 ? 256 LEU A N 1 ATOM 1944 C CA . LEU A 1 256 ? -44.008 6.117 20.396 1.00 64.29 ? 256 LEU A CA 1 ATOM 1945 C C . LEU A 1 256 ? -42.997 5.355 19.546 1.00 65.51 ? 256 LEU A C 1 ATOM 1946 O O . LEU A 1 256 ? -42.099 5.969 18.993 1.00 65.91 ? 256 LEU A O 1 ATOM 1947 C CB . LEU A 1 256 ? -43.274 7.048 21.365 1.00 63.52 ? 256 LEU A CB 1 ATOM 1948 C CG . LEU A 1 256 ? -44.145 7.810 22.371 1.00 63.16 ? 256 LEU A CG 1 ATOM 1949 C CD1 . LEU A 1 256 ? -43.301 8.790 23.173 1.00 62.43 ? 256 LEU A CD1 1 ATOM 1950 C CD2 . LEU A 1 256 ? -45.279 8.549 21.669 1.00 61.87 ? 256 LEU A CD2 1 ATOM 1951 N N . ASN A 1 257 ? -43.146 4.039 19.417 1.00 67.31 ? 257 ASN A N 1 ATOM 1952 C CA . ASN A 1 257 ? -42.155 3.228 18.703 1.00 69.48 ? 257 ASN A CA 1 ATOM 1953 C C . ASN A 1 257 ? -41.987 3.562 17.210 1.00 68.72 ? 257 ASN A C 1 ATOM 1954 O O . ASN A 1 257 ? -40.941 3.279 16.637 1.00 69.97 ? 257 ASN A O 1 ATOM 1955 C CB . ASN A 1 257 ? -42.450 1.730 18.874 1.00 72.72 ? 257 ASN A CB 1 ATOM 1956 C CG . ASN A 1 257 ? -42.222 1.242 20.297 1.00 74.46 ? 257 ASN A CG 1 ATOM 1957 O OD1 . ASN A 1 257 ? -41.938 2.023 21.203 1.00 74.29 ? 257 ASN A OD1 1 ATOM 1958 N ND2 . ASN A 1 257 ? -42.347 -0.057 20.495 1.00 76.82 ? 257 ASN A ND2 1 ATOM 1959 N N . SER A 1 258 ? -43.000 4.150 16.579 1.00 67.47 ? 258 SER A N 1 ATOM 1960 C CA . SER A 1 258 ? -42.870 4.601 15.190 1.00 66.29 ? 258 SER A CA 1 ATOM 1961 C C . SER A 1 258 ? -43.885 5.683 14.824 1.00 63.98 ? 258 SER A C 1 ATOM 1962 O O . SER A 1 258 ? -44.813 5.963 15.580 1.00 63.62 ? 258 SER A O 1 ATOM 1963 C CB . SER A 1 258 ? -43.027 3.423 14.227 1.00 67.91 ? 258 SER A CB 1 ATOM 1964 O OG . SER A 1 258 ? -44.393 3.098 14.047 1.00 68.04 ? 258 SER A OG 1 ATOM 1965 N N . ASP A 1 259 ? -43.699 6.275 13.650 1.00 62.84 ? 259 ASP A N 1 ATOM 1966 C CA . ASP A 1 259 ? -44.631 7.264 13.127 1.00 61.14 ? 259 ASP A CA 1 ATOM 1967 C C . ASP A 1 259 ? -45.996 6.670 12.873 1.00 62.12 ? 259 ASP A C 1 ATOM 1968 O O . ASP A 1 259 ? -47.003 7.325 13.119 1.00 61.22 ? 259 ASP A O 1 ATOM 1969 C CB . ASP A 1 259 ? -44.134 7.839 11.804 1.00 61.31 ? 259 ASP A CB 1 ATOM 1970 C CG . ASP A 1 259 ? -43.019 8.824 11.977 1.00 60.53 ? 259 ASP A CG 1 ATOM 1971 O OD1 . ASP A 1 259 ? -42.471 8.904 13.091 1.00 60.31 ? 259 ASP A OD1 1 ATOM 1972 O OD2 . ASP A 1 259 ? -42.692 9.519 10.990 1.00 61.23 ? 259 ASP A OD2 1 ATOM 1973 N N . GLU A 1 260 ? -46.037 5.451 12.338 1.00 65.26 ? 260 GLU A N 1 ATOM 1974 C CA . GLU A 1 260 ? -47.317 4.817 12.031 1.00 66.25 ? 260 GLU A CA 1 ATOM 1975 C C . GLU A 1 260 ? -48.080 4.596 13.336 1.00 67.13 ? 260 GLU A C 1 ATOM 1976 O O . GLU A 1 260 ? -49.270 4.901 13.426 1.00 65.65 ? 260 GLU A O 1 ATOM 1977 C CB . GLU A 1 260 ? -47.130 3.502 11.262 1.00 66.94 ? 260 GLU A CB 1 ATOM 1978 N N . GLU A 1 261 ? -47.378 4.111 14.356 1.00 69.40 ? 261 GLU A N 1 ATOM 1979 C CA . GLU A 1 261 ? -48.015 3.786 15.633 1.00 71.87 ? 261 GLU A CA 1 ATOM 1980 C C . GLU A 1 261 ? -48.472 5.027 16.394 1.00 68.82 ? 261 GLU A C 1 ATOM 1981 O O . GLU A 1 261 ? -49.524 5.009 17.037 1.00 69.90 ? 261 GLU A O 1 ATOM 1982 C CB . GLU A 1 261 ? -47.085 2.933 16.504 1.00 75.93 ? 261 GLU A CB 1 ATOM 1983 C CG . GLU A 1 261 ? -47.042 1.469 16.086 1.00 79.23 ? 261 GLU A CG 1 ATOM 1984 C CD . GLU A 1 261 ? -45.893 0.714 16.724 1.00 83.05 ? 261 GLU A CD 1 ATOM 1985 O OE1 . GLU A 1 261 ? -44.738 1.182 16.598 1.00 84.37 ? 261 GLU A OE1 1 ATOM 1986 O OE2 . GLU A 1 261 ? -46.140 -0.346 17.343 1.00 84.00 ? 261 GLU A OE2 1 ATOM 1987 N N . LEU A 1 262 ? -47.680 6.095 16.316 1.00 65.06 ? 262 LEU A N 1 ATOM 1988 C CA . LEU A 1 262 ? -48.019 7.372 16.950 1.00 61.19 ? 262 LEU A CA 1 ATOM 1989 C C . LEU A 1 262 ? -49.233 8.021 16.291 1.00 59.22 ? 262 LEU A C 1 ATOM 1990 O O . LEU A 1 262 ? -50.149 8.470 16.965 1.00 57.67 ? 262 LEU A O 1 ATOM 1991 C CB . LEU A 1 262 ? -46.818 8.324 16.886 1.00 59.21 ? 262 LEU A CB 1 ATOM 1992 C CG . LEU A 1 262 ? -47.050 9.800 17.213 1.00 56.08 ? 262 LEU A CG 1 ATOM 1993 C CD1 . LEU A 1 262 ? -47.611 9.967 18.614 1.00 56.31 ? 262 LEU A CD1 1 ATOM 1994 C CD2 . LEU A 1 262 ? -45.742 10.555 17.064 1.00 54.71 ? 262 LEU A CD2 1 ATOM 1995 N N . ILE A 1 263 ? -49.234 8.066 14.967 1.00 59.84 ? 263 ILE A N 1 ATOM 1996 C CA . ILE A 1 263 ? -50.332 8.674 14.234 1.00 59.74 ? 263 ILE A CA 1 ATOM 1997 C C . ILE A 1 263 ? -51.612 7.884 14.458 1.00 63.09 ? 263 ILE A C 1 ATOM 1998 O O . ILE A 1 263 ? -52.666 8.463 14.705 1.00 63.19 ? 263 ILE A O 1 ATOM 1999 C CB . ILE A 1 263 ? -50.004 8.788 12.737 1.00 58.96 ? 263 ILE A CB 1 ATOM 2000 C CG1 . ILE A 1 263 ? -48.913 9.841 12.538 1.00 58.18 ? 263 ILE A CG1 1 ATOM 2001 C CG2 . ILE A 1 263 ? -51.237 9.178 11.932 1.00 58.29 ? 263 ILE A CG2 1 ATOM 2002 C CD1 . ILE A 1 263 ? -48.226 9.773 11.192 1.00 58.68 ? 263 ILE A CD1 1 ATOM 2003 N N . HIS A 1 264 ? -51.522 6.562 14.395 1.00 68.01 ? 264 HIS A N 1 ATOM 2004 C CA . HIS A 1 264 ? -52.687 5.728 14.653 1.00 72.07 ? 264 HIS A CA 1 ATOM 2005 C C . HIS A 1 264 ? -53.276 6.066 16.016 1.00 69.96 ? 264 HIS A C 1 ATOM 2006 O O . HIS A 1 264 ? -54.488 6.183 16.148 1.00 71.14 ? 264 HIS A O 1 ATOM 2007 C CB . HIS A 1 264 ? -52.344 4.239 14.568 1.00 77.17 ? 264 HIS A CB 1 ATOM 2008 C CG . HIS A 1 264 ? -53.526 3.339 14.762 1.00 84.55 ? 264 HIS A CG 1 ATOM 2009 N ND1 . HIS A 1 264 ? -53.950 2.923 16.008 1.00 87.94 ? 264 HIS A ND1 1 ATOM 2010 C CD2 . HIS A 1 264 ? -54.377 2.780 13.868 1.00 89.03 ? 264 HIS A CD2 1 ATOM 2011 C CE1 . HIS A 1 264 ? -55.006 2.139 15.873 1.00 90.81 ? 264 HIS A CE1 1 ATOM 2012 N NE2 . HIS A 1 264 ? -55.284 2.033 14.585 1.00 92.11 ? 264 HIS A NE2 1 ATOM 2013 N N . CYS A 1 265 ? -52.419 6.237 17.021 1.00 68.74 ? 265 CYS A N 1 ATOM 2014 C CA . CYS A 1 265 ? -52.877 6.600 18.367 1.00 67.53 ? 265 CYS A CA 1 ATOM 2015 C C . CYS A 1 265 ? -53.564 7.970 18.387 1.00 63.09 ? 265 CYS A C 1 ATOM 2016 O O . CYS A 1 265 ? -54.666 8.108 18.923 1.00 62.01 ? 265 CYS A O 1 ATOM 2017 C CB . CYS A 1 265 ? -51.713 6.587 19.358 1.00 68.59 ? 265 CYS A CB 1 ATOM 2018 S SG . CYS A 1 265 ? -52.183 6.994 21.061 1.00 71.97 ? 265 CYS A SG 1 ATOM 2019 N N . LEU A 1 266 ? -52.914 8.966 17.785 1.00 58.94 ? 266 LEU A N 1 ATOM 2020 C CA . LEU A 1 266 ? -53.454 10.326 17.720 1.00 55.01 ? 266 LEU A CA 1 ATOM 2021 C C . LEU A 1 266 ? -54.771 10.394 16.950 1.00 54.72 ? 266 LEU A C 1 ATOM 2022 O O . LEU A 1 266 ? -55.624 11.212 17.258 1.00 53.60 ? 266 LEU A O 1 ATOM 2023 C CB . LEU A 1 266 ? -52.427 11.299 17.115 1.00 52.00 ? 266 LEU A CB 1 ATOM 2024 C CG . LEU A 1 266 ? -51.146 11.562 17.926 1.00 50.83 ? 266 LEU A CG 1 ATOM 2025 C CD1 . LEU A 1 266 ? -50.209 12.499 17.192 1.00 48.82 ? 266 LEU A CD1 1 ATOM 2026 C CD2 . LEU A 1 266 ? -51.457 12.137 19.295 1.00 51.19 ? 266 LEU A CD2 1 ATOM 2027 N N . ARG A 1 267 ? -54.939 9.530 15.960 1.00 57.51 ? 267 ARG A N 1 ATOM 2028 C CA . ARG A 1 267 ? -56.193 9.456 15.204 1.00 58.84 ? 267 ARG A CA 1 ATOM 2029 C C . ARG A 1 267 ? -57.349 8.813 15.958 1.00 59.67 ? 267 ARG A C 1 ATOM 2030 O O . ARG A 1 267 ? -58.498 9.140 15.690 1.00 60.35 ? 267 ARG A O 1 ATOM 2031 C CB . ARG A 1 267 ? -55.977 8.720 13.883 1.00 60.52 ? 267 ARG A CB 1 ATOM 2032 C CG . ARG A 1 267 ? -55.271 9.588 12.859 1.00 59.63 ? 267 ARG A CG 1 ATOM 2033 C CD . ARG A 1 267 ? -55.089 8.869 11.542 1.00 60.22 ? 267 ARG A CD 1 ATOM 2034 N NE . ARG A 1 267 ? -54.419 9.736 10.576 1.00 59.14 ? 267 ARG A NE 1 ATOM 2035 C CZ . ARG A 1 267 ? -53.878 9.317 9.437 1.00 58.33 ? 267 ARG A CZ 1 ATOM 2036 N NH1 . ARG A 1 267 ? -53.932 8.035 9.110 1.00 58.72 ? 267 ARG A NH1 1 ATOM 2037 N NH2 . ARG A 1 267 ? -53.279 10.186 8.626 1.00 57.03 ? 267 ARG A NH2 1 ATOM 2038 N N . GLU A 1 268 ? -57.052 7.908 16.888 1.00 60.89 ? 268 GLU A N 1 ATOM 2039 C CA . GLU A 1 268 ? -58.094 7.249 17.684 1.00 62.53 ? 268 GLU A CA 1 ATOM 2040 C C . GLU A 1 268 ? -58.719 8.201 18.720 1.00 61.48 ? 268 GLU A C 1 ATOM 2041 O O . GLU A 1 268 ? -59.834 7.971 19.174 1.00 63.99 ? 268 GLU A O 1 ATOM 2042 C CB . GLU A 1 268 ? -57.549 5.977 18.367 1.00 63.65 ? 268 GLU A CB 1 ATOM 2043 N N . LYS A 1 269 ? -58.016 9.277 19.074 1.00 58.69 ? 269 LYS A N 1 ATOM 2044 C CA . LYS A 1 269 ? -58.475 10.199 20.118 1.00 56.46 ? 269 LYS A CA 1 ATOM 2045 C C . LYS A 1 269 ? -59.646 11.075 19.691 1.00 55.31 ? 269 LYS A C 1 ATOM 2046 O O . LYS A 1 269 ? -59.786 11.415 18.518 1.00 56.36 ? 269 LYS A O 1 ATOM 2047 C CB . LYS A 1 269 ? -57.331 11.117 20.561 1.00 54.13 ? 269 LYS A CB 1 ATOM 2048 C CG . LYS A 1 269 ? -56.116 10.407 21.133 1.00 54.47 ? 269 LYS A CG 1 ATOM 2049 C CD . LYS A 1 269 ? -56.452 9.538 22.343 1.00 56.17 ? 269 LYS A CD 1 ATOM 2050 C CE . LYS A 1 269 ? -55.215 8.838 22.887 1.00 56.30 ? 269 LYS A CE 1 ATOM 2051 N NZ . LYS A 1 269 ? -55.558 7.840 23.928 1.00 58.64 ? 269 LYS A NZ 1 ATOM 2052 N N . LYS A 1 270 ? -60.481 11.447 20.659 1.00 55.09 ? 270 LYS A N 1 ATOM 2053 C CA . LYS A 1 270 ? -61.486 12.478 20.445 1.00 53.31 ? 270 LYS A CA 1 ATOM 2054 C C . LYS A 1 270 ? -60.717 13.797 20.358 1.00 50.62 ? 270 LYS A C 1 ATOM 2055 O O . LYS A 1 270 ? -59.707 13.971 21.041 1.00 52.47 ? 270 LYS A O 1 ATOM 2056 C CB . LYS A 1 270 ? -62.529 12.495 21.573 1.00 53.64 ? 270 LYS A CB 1 ATOM 2057 N N . PRO A 1 271 ? -61.170 14.723 19.511 1.00 47.85 ? 271 PRO A N 1 ATOM 2058 C CA . PRO A 1 271 ? -60.436 15.973 19.298 1.00 46.36 ? 271 PRO A CA 1 ATOM 2059 C C . PRO A 1 271 ? -60.065 16.728 20.580 1.00 47.03 ? 271 PRO A C 1 ATOM 2060 O O . PRO A 1 271 ? -58.980 17.303 20.675 1.00 46.66 ? 271 PRO A O 1 ATOM 2061 C CB . PRO A 1 271 ? -61.411 16.819 18.473 1.00 45.44 ? 271 PRO A CB 1 ATOM 2062 C CG . PRO A 1 271 ? -62.321 15.842 17.827 1.00 46.54 ? 271 PRO A CG 1 ATOM 2063 C CD . PRO A 1 271 ? -62.445 14.697 18.780 1.00 48.15 ? 271 PRO A CD 1 ATOM 2064 N N . GLN A 1 272 ? -60.968 16.732 21.553 1.00 49.13 ? 272 GLN A N 1 ATOM 2065 C CA . GLN A 1 272 ? -60.767 17.495 22.783 1.00 49.15 ? 272 GLN A CA 1 ATOM 2066 C C . GLN A 1 272 ? -59.608 16.955 23.643 1.00 50.06 ? 272 GLN A C 1 ATOM 2067 O O . GLN A 1 272 ? -59.009 17.689 24.422 1.00 49.81 ? 272 GLN A O 1 ATOM 2068 C CB . GLN A 1 272 ? -62.072 17.533 23.589 1.00 50.42 ? 272 GLN A CB 1 ATOM 2069 C CG . GLN A 1 272 ? -62.110 18.583 24.695 1.00 50.81 ? 272 GLN A CG 1 ATOM 2070 C CD . GLN A 1 272 ? -61.850 19.988 24.179 1.00 48.90 ? 272 GLN A CD 1 ATOM 2071 O OE1 . GLN A 1 272 ? -62.233 20.334 23.057 1.00 48.82 ? 272 GLN A OE1 1 ATOM 2072 N NE2 . GLN A 1 272 ? -61.182 20.798 24.987 1.00 47.59 ? 272 GLN A NE2 1 ATOM 2073 N N . GLU A 1 273 ? -59.281 15.678 23.491 1.00 51.47 ? 273 GLU A N 1 ATOM 2074 C CA . GLU A 1 273 ? -58.136 15.106 24.187 1.00 51.47 ? 273 GLU A CA 1 ATOM 2075 C C . GLU A 1 273 ? -56.827 15.675 23.649 1.00 49.75 ? 273 GLU A C 1 ATOM 2076 O O . GLU A 1 273 ? -55.878 15.830 24.394 1.00 50.63 ? 273 GLU A O 1 ATOM 2077 C CB . GLU A 1 273 ? -58.148 13.589 24.062 1.00 53.65 ? 273 GLU A CB 1 ATOM 2078 C CG . GLU A 1 273 ? -59.381 12.954 24.690 1.00 56.01 ? 273 GLU A CG 1 ATOM 2079 C CD . GLU A 1 273 ? -59.554 11.499 24.314 1.00 57.59 ? 273 GLU A CD 1 ATOM 2080 O OE1 . GLU A 1 273 ? -58.969 10.633 24.999 1.00 57.92 ? 273 GLU A OE1 1 ATOM 2081 O OE2 . GLU A 1 273 ? -60.295 11.231 23.344 1.00 57.16 ? 273 GLU A OE2 1 ATOM 2082 N N . LEU A 1 274 ? -56.778 15.991 22.359 1.00 48.55 ? 274 LEU A N 1 ATOM 2083 C CA . LEU A 1 274 ? -55.609 16.661 21.781 1.00 47.33 ? 274 LEU A CA 1 ATOM 2084 C C . LEU A 1 274 ? -55.524 18.135 22.216 1.00 45.68 ? 274 LEU A C 1 ATOM 2085 O O . LEU A 1 274 ? -54.446 18.649 22.524 1.00 44.52 ? 274 LEU A O 1 ATOM 2086 C CB . LEU A 1 274 ? -55.638 16.578 20.250 1.00 46.75 ? 274 LEU A CB 1 ATOM 2087 C CG . LEU A 1 274 ? -55.052 15.326 19.600 1.00 47.90 ? 274 LEU A CG 1 ATOM 2088 C CD1 . LEU A 1 274 ? -55.546 14.053 20.250 1.00 50.08 ? 274 LEU A CD1 1 ATOM 2089 C CD2 . LEU A 1 274 ? -55.400 15.316 18.124 1.00 48.20 ? 274 LEU A CD2 1 ATOM 2090 N N . ILE A 1 275 ? -56.665 18.809 22.221 1.00 45.05 ? 275 ILE A N 1 ATOM 2091 C CA . ILE A 1 275 ? -56.734 20.214 22.629 1.00 43.88 ? 275 ILE A CA 1 ATOM 2092 C C . ILE A 1 275 ? -56.382 20.409 24.112 1.00 43.00 ? 275 ILE A C 1 ATOM 2093 O O . ILE A 1 275 ? -55.716 21.366 24.467 1.00 42.39 ? 275 ILE A O 1 ATOM 2094 C CB . ILE A 1 275 ? -58.130 20.798 22.328 1.00 44.32 ? 275 ILE A CB 1 ATOM 2095 C CG1 . ILE A 1 275 ? -58.343 20.884 20.803 1.00 43.15 ? 275 ILE A CG1 1 ATOM 2096 C CG2 . ILE A 1 275 ? -58.298 22.164 22.982 1.00 43.96 ? 275 ILE A CG2 1 ATOM 2097 C CD1 . ILE A 1 275 ? -59.796 20.881 20.369 1.00 43.37 ? 275 ILE A CD1 1 ATOM 2098 N N . ASP A 1 276 ? -56.798 19.490 24.970 1.00 43.76 ? 276 ASP A N 1 ATOM 2099 C CA . ASP A 1 276 ? -56.527 19.610 26.405 1.00 44.16 ? 276 ASP A CA 1 ATOM 2100 C C . ASP A 1 276 ? -55.045 19.668 26.777 1.00 44.48 ? 276 ASP A C 1 ATOM 2101 O O . ASP A 1 276 ? -54.699 20.227 27.822 1.00 46.10 ? 276 ASP A O 1 ATOM 2102 C CB . ASP A 1 276 ? -57.191 18.465 27.174 1.00 45.32 ? 276 ASP A CB 1 ATOM 2103 C CG . ASP A 1 276 ? -58.679 18.682 27.386 1.00 45.62 ? 276 ASP A CG 1 ATOM 2104 O OD1 . ASP A 1 276 ? -59.173 19.805 27.122 1.00 44.91 ? 276 ASP A OD1 1 ATOM 2105 O OD2 . ASP A 1 276 ? -59.346 17.729 27.831 1.00 45.62 ? 276 ASP A OD2 1 ATOM 2106 N N . VAL A 1 277 ? -54.178 19.099 25.941 1.00 43.67 ? 277 VAL A N 1 ATOM 2107 C CA . VAL A 1 277 ? -52.742 19.062 26.228 1.00 43.18 ? 277 VAL A CA 1 ATOM 2108 C C . VAL A 1 277 ? -51.892 19.800 25.193 1.00 42.40 ? 277 VAL A C 1 ATOM 2109 O O . VAL A 1 277 ? -50.661 19.771 25.270 1.00 42.76 ? 277 VAL A O 1 ATOM 2110 C CB . VAL A 1 277 ? -52.249 17.612 26.373 1.00 44.43 ? 277 VAL A CB 1 ATOM 2111 C CG1 . VAL A 1 277 ? -53.005 16.924 27.505 1.00 46.60 ? 277 VAL A CG1 1 ATOM 2112 C CG2 . VAL A 1 277 ? -52.425 16.830 25.076 1.00 44.23 ? 277 VAL A CG2 1 ATOM 2113 N N . GLU A 1 278 ? -52.548 20.481 24.254 1.00 41.63 ? 278 GLU A N 1 ATOM 2114 C CA . GLU A 1 278 ? -51.873 21.169 23.155 1.00 41.21 ? 278 GLU A CA 1 ATOM 2115 C C . GLU A 1 278 ? -50.721 22.035 23.659 1.00 40.72 ? 278 GLU A C 1 ATOM 2116 O O . GLU A 1 278 ? -49.610 21.953 23.177 1.00 40.72 ? 278 GLU A O 1 ATOM 2117 C CB . GLU A 1 278 ? -52.894 22.006 22.350 1.00 41.77 ? 278 GLU A CB 1 ATOM 2118 C CG . GLU A 1 278 ? -52.270 23.013 21.390 1.00 42.17 ? 278 GLU A CG 1 ATOM 2119 C CD . GLU A 1 278 ? -53.222 23.610 20.360 1.00 43.09 ? 278 GLU A CD 1 ATOM 2120 O OE1 . GLU A 1 278 ? -54.457 23.423 20.433 1.00 44.05 ? 278 GLU A OE1 1 ATOM 2121 O OE2 . GLU A 1 278 ? -52.702 24.287 19.441 1.00 48.66 ? 278 GLU A OE2 1 ATOM 2122 N N . TRP A 1 279 ? -50.993 22.846 24.660 1.00 43.13 ? 279 TRP A N 1 ATOM 2123 C CA . TRP A 1 279 ? -50.023 23.806 25.165 1.00 44.01 ? 279 TRP A CA 1 ATOM 2124 C C . TRP A 1 279 ? -48.885 23.175 25.936 1.00 44.92 ? 279 TRP A C 1 ATOM 2125 O O . TRP A 1 279 ? -47.856 23.815 26.117 1.00 45.86 ? 279 TRP A O 1 ATOM 2126 C CB . TRP A 1 279 ? -50.723 24.796 26.083 1.00 46.00 ? 279 TRP A CB 1 ATOM 2127 C CG . TRP A 1 279 ? -51.752 25.569 25.380 1.00 47.24 ? 279 TRP A CG 1 ATOM 2128 C CD1 . TRP A 1 279 ? -53.090 25.345 25.391 1.00 48.45 ? 279 TRP A CD1 1 ATOM 2129 C CD2 . TRP A 1 279 ? -51.533 26.693 24.535 1.00 47.07 ? 279 TRP A CD2 1 ATOM 2130 N NE1 . TRP A 1 279 ? -53.725 26.275 24.616 1.00 49.30 ? 279 TRP A NE1 1 ATOM 2131 C CE2 . TRP A 1 279 ? -52.792 27.113 24.071 1.00 48.21 ? 279 TRP A CE2 1 ATOM 2132 C CE3 . TRP A 1 279 ? -50.393 27.387 24.127 1.00 48.56 ? 279 TRP A CE3 1 ATOM 2133 C CZ2 . TRP A 1 279 ? -52.953 28.201 23.211 1.00 49.46 ? 279 TRP A CZ2 1 ATOM 2134 C CZ3 . TRP A 1 279 ? -50.548 28.470 23.270 1.00 50.93 ? 279 TRP A CZ3 1 ATOM 2135 C CH2 . TRP A 1 279 ? -51.826 28.868 22.821 1.00 49.59 ? 279 TRP A CH2 1 ATOM 2136 N N . ASN A 1 280 ? -49.067 21.940 26.401 1.00 45.14 ? 280 ASN A N 1 ATOM 2137 C CA . ASN A 1 280 ? -48.020 21.233 27.131 1.00 46.18 ? 280 ASN A CA 1 ATOM 2138 C C . ASN A 1 280 ? -46.763 20.948 26.320 1.00 45.69 ? 280 ASN A C 1 ATOM 2139 O O . ASN A 1 280 ? -45.730 20.664 26.903 1.00 48.23 ? 280 ASN A O 1 ATOM 2140 C CB . ASN A 1 280 ? -48.526 19.888 27.666 1.00 48.28 ? 280 ASN A CB 1 ATOM 2141 C CG . ASN A 1 280 ? -49.625 20.026 28.705 1.00 49.27 ? 280 ASN A CG 1 ATOM 2142 O OD1 . ASN A 1 280 ? -49.974 21.124 29.145 1.00 50.35 ? 280 ASN A OD1 1 ATOM 2143 N ND2 . ASN A 1 280 ? -50.175 18.895 29.105 1.00 50.25 ? 280 ASN A ND2 1 ATOM 2144 N N . VAL A 1 281 ? -46.841 20.993 24.993 1.00 44.59 ? 281 VAL A N 1 ATOM 2145 C CA . VAL A 1 281 ? -45.702 20.604 24.151 1.00 45.07 ? 281 VAL A CA 1 ATOM 2146 C C . VAL A 1 281 ? -44.704 21.729 23.844 1.00 44.43 ? 281 VAL A C 1 ATOM 2147 O O . VAL A 1 281 ? -43.644 21.464 23.275 1.00 43.39 ? 281 VAL A O 1 ATOM 2148 C CB . VAL A 1 281 ? -46.166 19.973 22.817 1.00 45.14 ? 281 VAL A CB 1 ATOM 2149 C CG1 . VAL A 1 281 ? -47.250 18.939 23.067 1.00 47.24 ? 281 VAL A CG1 1 ATOM 2150 C CG2 . VAL A 1 281 ? -46.669 21.025 21.846 1.00 43.89 ? 281 VAL A CG2 1 ATOM 2151 N N . LEU A 1 282 ? -45.031 22.975 24.196 1.00 44.26 ? 282 LEU A N 1 ATOM 2152 C CA . LEU A 1 282 ? -44.106 24.085 23.962 1.00 43.02 ? 282 LEU A CA 1 ATOM 2153 C C . LEU A 1 282 ? -42.809 23.804 24.713 1.00 44.59 ? 282 LEU A C 1 ATOM 2154 O O . LEU A 1 282 ? -42.843 23.400 25.862 1.00 45.57 ? 282 LEU A O 1 ATOM 2155 C CB . LEU A 1 282 ? -44.691 25.415 24.423 1.00 40.97 ? 282 LEU A CB 1 ATOM 2156 C CG . LEU A 1 282 ? -45.816 26.035 23.602 1.00 39.84 ? 282 LEU A CG 1 ATOM 2157 C CD1 . LEU A 1 282 ? -46.389 27.226 24.346 1.00 39.88 ? 282 LEU A CD1 1 ATOM 2158 C CD2 . LEU A 1 282 ? -45.355 26.462 22.222 1.00 38.92 ? 282 LEU A CD2 1 ATOM 2159 N N . PRO A 1 283 ? -41.661 23.989 24.056 1.00 45.83 ? 283 PRO A N 1 ATOM 2160 C CA . PRO A 1 283 ? -40.404 23.653 24.711 1.00 47.14 ? 283 PRO A CA 1 ATOM 2161 C C . PRO A 1 283 ? -39.905 24.714 25.700 1.00 48.52 ? 283 PRO A C 1 ATOM 2162 O O . PRO A 1 283 ? -38.953 24.451 26.429 1.00 47.84 ? 283 PRO A O 1 ATOM 2163 C CB . PRO A 1 283 ? -39.434 23.530 23.536 1.00 47.14 ? 283 PRO A CB 1 ATOM 2164 C CG . PRO A 1 283 ? -39.965 24.486 22.528 1.00 46.29 ? 283 PRO A CG 1 ATOM 2165 C CD . PRO A 1 283 ? -41.461 24.433 22.663 1.00 45.04 ? 283 PRO A CD 1 ATOM 2166 N N . PHE A 1 284 ? -40.520 25.898 25.710 1.00 49.40 ? 284 PHE A N 1 ATOM 2167 C CA . PHE A 1 284 ? -40.085 26.989 26.579 1.00 50.40 ? 284 PHE A CA 1 ATOM 2168 C C . PHE A 1 284 ? -41.230 27.602 27.372 1.00 48.91 ? 284 PHE A C 1 ATOM 2169 O O . PHE A 1 284 ? -42.387 27.528 26.982 1.00 47.54 ? 284 PHE A O 1 ATOM 2170 C CB . PHE A 1 284 ? -39.440 28.104 25.751 1.00 52.34 ? 284 PHE A CB 1 ATOM 2171 C CG . PHE A 1 284 ? -38.192 27.686 25.042 1.00 55.60 ? 284 PHE A CG 1 ATOM 2172 C CD1 . PHE A 1 284 ? -37.060 27.302 25.765 1.00 58.05 ? 284 PHE A CD1 1 ATOM 2173 C CD2 . PHE A 1 284 ? -38.136 27.684 23.650 1.00 58.01 ? 284 PHE A CD2 1 ATOM 2174 C CE1 . PHE A 1 284 ? -35.896 26.913 25.114 1.00 59.86 ? 284 PHE A CE1 1 ATOM 2175 C CE2 . PHE A 1 284 ? -36.977 27.292 22.991 1.00 60.35 ? 284 PHE A CE2 1 ATOM 2176 C CZ . PHE A 1 284 ? -35.855 26.906 23.723 1.00 61.74 ? 284 PHE A CZ 1 ATOM 2177 N N . ASP A 1 285 ? -40.878 28.220 28.491 1.00 49.52 ? 285 ASP A N 1 ATOM 2178 C CA . ASP A 1 285 ? -41.777 29.098 29.220 1.00 47.93 ? 285 ASP A CA 1 ATOM 2179 C C . ASP A 1 285 ? -41.804 30.414 28.422 1.00 45.31 ? 285 ASP A C 1 ATOM 2180 O O . ASP A 1 285 ? -40.836 31.166 28.406 1.00 43.95 ? 285 ASP A O 1 ATOM 2181 C CB . ASP A 1 285 ? -41.244 29.279 30.649 1.00 49.16 ? 285 ASP A CB 1 ATOM 2182 C CG . ASP A 1 285 ? -42.227 29.967 31.576 1.00 50.12 ? 285 ASP A CG 1 ATOM 2183 O OD1 . ASP A 1 285 ? -43.386 30.201 31.156 1.00 49.47 ? 285 ASP A OD1 1 ATOM 2184 O OD2 . ASP A 1 285 ? -41.828 30.268 32.736 1.00 49.42 ? 285 ASP A OD2 1 ATOM 2185 N N . SER A 1 286 ? -42.905 30.674 27.734 1.00 44.52 ? 286 SER A N 1 ATOM 2186 C CA . SER A 1 286 ? -42.926 31.724 26.729 1.00 44.21 ? 286 SER A CA 1 ATOM 2187 C C . SER A 1 286 ? -44.282 32.401 26.565 1.00 43.31 ? 286 SER A C 1 ATOM 2188 O O . SER A 1 286 ? -45.289 31.943 27.096 1.00 43.18 ? 286 SER A O 1 ATOM 2189 C CB . SER A 1 286 ? -42.536 31.117 25.387 1.00 44.94 ? 286 SER A CB 1 ATOM 2190 O OG . SER A 1 286 ? -43.545 30.225 24.932 1.00 45.22 ? 286 SER A OG 1 ATOM 2191 N N . ILE A 1 287 ? -44.292 33.499 25.813 1.00 41.95 ? 287 ILE A N 1 ATOM 2192 C CA . ILE A 1 287 ? -45.540 34.070 25.316 1.00 40.90 ? 287 ILE A CA 1 ATOM 2193 C C . ILE A 1 287 ? -45.417 34.374 23.836 1.00 38.52 ? 287 ILE A C 1 ATOM 2194 O O . ILE A 1 287 ? -44.312 34.542 23.323 1.00 38.58 ? 287 ILE A O 1 ATOM 2195 C CB . ILE A 1 287 ? -45.966 35.345 26.066 1.00 40.53 ? 287 ILE A CB 1 ATOM 2196 C CG1 . ILE A 1 287 ? -44.819 36.351 26.113 1.00 41.42 ? 287 ILE A CG1 1 ATOM 2197 C CG2 . ILE A 1 287 ? -46.425 34.996 27.465 1.00 42.02 ? 287 ILE A CG2 1 ATOM 2198 C CD1 . ILE A 1 287 ? -45.264 37.749 26.466 1.00 41.95 ? 287 ILE A CD1 1 ATOM 2199 N N . PHE A 1 288 ? -46.570 34.472 23.181 1.00 36.51 ? 288 PHE A N 1 ATOM 2200 C CA . PHE A 1 288 ? -46.654 34.653 21.738 1.00 35.89 ? 288 PHE A CA 1 ATOM 2201 C C . PHE A 1 288 ? -45.978 33.491 21.034 1.00 36.13 ? 288 PHE A C 1 ATOM 2202 O O . PHE A 1 288 ? -45.282 33.687 20.049 1.00 36.35 ? 288 PHE A O 1 ATOM 2203 C CB . PHE A 1 288 ? -46.025 35.982 21.303 1.00 36.13 ? 288 PHE A CB 1 ATOM 2204 C CG . PHE A 1 288 ? -46.747 36.661 20.169 1.00 35.78 ? 288 PHE A CG 1 ATOM 2205 C CD1 . PHE A 1 288 ? -47.147 35.954 19.035 1.00 36.52 ? 288 PHE A CD1 1 ATOM 2206 C CD2 . PHE A 1 288 ? -47.021 38.018 20.231 1.00 35.27 ? 288 PHE A CD2 1 ATOM 2207 C CE1 . PHE A 1 288 ? -47.813 36.590 17.995 1.00 35.45 ? 288 PHE A CE1 1 ATOM 2208 C CE2 . PHE A 1 288 ? -47.684 38.653 19.200 1.00 35.42 ? 288 PHE A CE2 1 ATOM 2209 C CZ . PHE A 1 288 ? -48.086 37.936 18.081 1.00 35.12 ? 288 PHE A CZ 1 ATOM 2210 N N . ARG A 1 289 ? -46.168 32.286 21.560 1.00 37.57 ? 289 ARG A N 1 ATOM 2211 C CA . ARG A 1 289 ? -45.712 31.072 20.901 1.00 38.43 ? 289 ARG A CA 1 ATOM 2212 C C . ARG A 1 289 ? -46.822 30.060 20.938 1.00 39.88 ? 289 ARG A C 1 ATOM 2213 O O . ARG A 1 289 ? -47.552 29.950 21.933 1.00 39.30 ? 289 ARG A O 1 ATOM 2214 C CB . ARG A 1 289 ? -44.491 30.493 21.586 1.00 39.72 ? 289 ARG A CB 1 ATOM 2215 C CG . ARG A 1 289 ? -43.283 31.400 21.534 1.00 41.47 ? 289 ARG A CG 1 ATOM 2216 C CD . ARG A 1 289 ? -42.771 31.560 20.112 1.00 41.96 ? 289 ARG A CD 1 ATOM 2217 N NE . ARG A 1 289 ? -41.578 32.404 20.069 1.00 42.25 ? 289 ARG A NE 1 ATOM 2218 C CZ . ARG A 1 289 ? -41.574 33.722 19.920 1.00 41.27 ? 289 ARG A CZ 1 ATOM 2219 N NH1 . ARG A 1 289 ? -42.707 34.394 19.795 1.00 42.15 ? 289 ARG A NH1 1 ATOM 2220 N NH2 . ARG A 1 289 ? -40.422 34.377 19.890 1.00 42.08 ? 289 ARG A NH2 1 ATOM 2221 N N . PHE A 1 290 ? -46.941 29.315 19.841 1.00 40.18 ? 290 PHE A N 1 ATOM 2222 C CA . PHE A 1 290 ? -48.048 28.394 19.658 1.00 38.90 ? 290 PHE A CA 1 ATOM 2223 C C . PHE A 1 290 ? -47.519 27.049 19.218 1.00 37.78 ? 290 PHE A C 1 ATOM 2224 O O . PHE A 1 290 ? -46.462 26.961 18.602 1.00 34.88 ? 290 PHE A O 1 ATOM 2225 C CB . PHE A 1 290 ? -49.016 28.979 18.652 1.00 38.84 ? 290 PHE A CB 1 ATOM 2226 C CG . PHE A 1 290 ? -49.184 30.459 18.795 1.00 38.85 ? 290 PHE A CG 1 ATOM 2227 C CD1 . PHE A 1 290 ? -49.881 30.985 19.869 1.00 39.38 ? 290 PHE A CD1 1 ATOM 2228 C CD2 . PHE A 1 290 ? -48.616 31.330 17.876 1.00 38.29 ? 290 PHE A CD2 1 ATOM 2229 C CE1 . PHE A 1 290 ? -50.036 32.353 20.013 1.00 39.70 ? 290 PHE A CE1 1 ATOM 2230 C CE2 . PHE A 1 290 ? -48.769 32.702 18.013 1.00 38.24 ? 290 PHE A CE2 1 ATOM 2231 C CZ . PHE A 1 290 ? -49.484 33.214 19.079 1.00 39.03 ? 290 PHE A CZ 1 ATOM 2232 N N . SER A 1 291 ? -48.274 26.005 19.547 1.00 38.80 ? 291 SER A N 1 ATOM 2233 C CA . SER A 1 291 ? -47.739 24.654 19.537 1.00 39.01 ? 291 SER A CA 1 ATOM 2234 C C . SER A 1 291 ? -47.509 24.112 18.141 1.00 38.08 ? 291 SER A C 1 ATOM 2235 O O . SER A 1 291 ? -46.388 23.790 17.787 1.00 38.34 ? 291 SER A O 1 ATOM 2236 C CB . SER A 1 291 ? -48.627 23.721 20.347 1.00 40.26 ? 291 SER A CB 1 ATOM 2237 O OG . SER A 1 291 ? -48.449 23.992 21.732 1.00 41.95 ? 291 SER A OG 1 ATOM 2238 N N . PHE A 1 292 ? -48.560 24.029 17.344 1.00 37.34 ? 292 PHE A N 1 ATOM 2239 C CA . PHE A 1 292 ? -48.444 23.472 16.011 1.00 35.67 ? 292 PHE A CA 1 ATOM 2240 C C . PHE A 1 292 ? -48.622 24.560 14.975 1.00 35.02 ? 292 PHE A C 1 ATOM 2241 O O . PHE A 1 292 ? -49.729 25.056 14.764 1.00 35.67 ? 292 PHE A O 1 ATOM 2242 C CB . PHE A 1 292 ? -49.457 22.348 15.836 1.00 36.47 ? 292 PHE A CB 1 ATOM 2243 C CG . PHE A 1 292 ? -49.356 21.312 16.908 1.00 37.93 ? 292 PHE A CG 1 ATOM 2244 C CD1 . PHE A 1 292 ? -48.388 20.334 16.845 1.00 38.50 ? 292 PHE A CD1 1 ATOM 2245 C CD2 . PHE A 1 292 ? -50.185 21.359 18.019 1.00 38.61 ? 292 PHE A CD2 1 ATOM 2246 C CE1 . PHE A 1 292 ? -48.265 19.396 17.856 1.00 40.19 ? 292 PHE A CE1 1 ATOM 2247 C CE2 . PHE A 1 292 ? -50.065 20.429 19.030 1.00 39.52 ? 292 PHE A CE2 1 ATOM 2248 C CZ . PHE A 1 292 ? -49.107 19.441 18.947 1.00 40.51 ? 292 PHE A CZ 1 ATOM 2249 N N . VAL A 1 293 ? -47.508 24.905 14.333 1.00 34.32 ? 293 VAL A N 1 ATOM 2250 C CA . VAL A 1 293 ? -47.438 25.946 13.317 1.00 33.61 ? 293 VAL A CA 1 ATOM 2251 C C . VAL A 1 293 ? -46.786 25.373 12.043 1.00 33.70 ? 293 VAL A C 1 ATOM 2252 O O . VAL A 1 293 ? -46.285 24.255 12.066 1.00 35.45 ? 293 VAL A O 1 ATOM 2253 C CB . VAL A 1 293 ? -46.656 27.161 13.861 1.00 33.53 ? 293 VAL A CB 1 ATOM 2254 C CG1 . VAL A 1 293 ? -47.332 27.708 15.109 1.00 33.52 ? 293 VAL A CG1 1 ATOM 2255 C CG2 . VAL A 1 293 ? -45.215 26.801 14.185 1.00 34.17 ? 293 VAL A CG2 1 ATOM 2256 N N . PRO A 1 294 ? -46.816 26.116 10.922 1.00 33.39 ? 294 PRO A N 1 ATOM 2257 C CA . PRO A 1 294 ? -46.155 25.646 9.707 1.00 34.59 ? 294 PRO A CA 1 ATOM 2258 C C . PRO A 1 294 ? -44.721 25.144 9.911 1.00 36.30 ? 294 PRO A C 1 ATOM 2259 O O . PRO A 1 294 ? -43.943 25.802 10.610 1.00 37.50 ? 294 PRO A O 1 ATOM 2260 C CB . PRO A 1 294 ? -46.143 26.894 8.826 1.00 33.42 ? 294 PRO A CB 1 ATOM 2261 C CG . PRO A 1 294 ? -47.396 27.598 9.196 1.00 33.11 ? 294 PRO A CG 1 ATOM 2262 C CD . PRO A 1 294 ? -47.676 27.279 10.643 1.00 32.73 ? 294 PRO A CD 1 ATOM 2263 N N . VAL A 1 295 ? -44.392 23.989 9.328 1.00 37.12 ? 295 VAL A N 1 ATOM 2264 C CA . VAL A 1 295 ? -43.007 23.497 9.304 1.00 39.91 ? 295 VAL A CA 1 ATOM 2265 C C . VAL A 1 295 ? -42.288 23.907 8.028 1.00 41.27 ? 295 VAL A C 1 ATOM 2266 O O . VAL A 1 295 ? -42.899 23.999 6.953 1.00 42.59 ? 295 VAL A O 1 ATOM 2267 C CB . VAL A 1 295 ? -42.870 21.958 9.427 1.00 41.81 ? 295 VAL A CB 1 ATOM 2268 C CG1 . VAL A 1 295 ? -43.027 21.513 10.863 1.00 43.26 ? 295 VAL A CG1 1 ATOM 2269 C CG2 . VAL A 1 295 ? -43.850 21.215 8.534 1.00 43.31 ? 295 VAL A CG2 1 ATOM 2270 N N . ILE A 1 296 ? -40.986 24.140 8.152 1.00 41.50 ? 296 ILE A N 1 ATOM 2271 C CA . ILE A 1 296 ? -40.157 24.477 7.009 1.00 42.81 ? 296 ILE A CA 1 ATOM 2272 C C . ILE A 1 296 ? -39.681 23.158 6.408 1.00 45.22 ? 296 ILE A C 1 ATOM 2273 O O . ILE A 1 296 ? -38.627 22.645 6.768 1.00 45.99 ? 296 ILE A O 1 ATOM 2274 C CB . ILE A 1 296 ? -38.981 25.376 7.425 1.00 42.77 ? 296 ILE A CB 1 ATOM 2275 C CG1 . ILE A 1 296 ? -39.497 26.657 8.088 1.00 41.99 ? 296 ILE A CG1 1 ATOM 2276 C CG2 . ILE A 1 296 ? -38.129 25.730 6.218 1.00 44.00 ? 296 ILE A CG2 1 ATOM 2277 C CD1 . ILE A 1 296 ? -40.284 27.566 7.159 1.00 42.20 ? 296 ILE A CD1 1 ATOM 2278 N N . ASP A 1 297 ? -40.477 22.622 5.485 1.00 47.29 ? 297 ASP A N 1 ATOM 2279 C CA . ASP A 1 297 ? -40.421 21.203 5.127 1.00 48.82 ? 297 ASP A CA 1 ATOM 2280 C C . ASP A 1 297 ? -39.642 20.911 3.860 1.00 51.43 ? 297 ASP A C 1 ATOM 2281 O O . ASP A 1 297 ? -39.452 19.742 3.505 1.00 53.47 ? 297 ASP A O 1 ATOM 2282 C CB . ASP A 1 297 ? -41.846 20.628 4.998 1.00 48.26 ? 297 ASP A CB 1 ATOM 2283 C CG . ASP A 1 297 ? -42.678 21.329 3.930 1.00 47.47 ? 297 ASP A CG 1 ATOM 2284 O OD1 . ASP A 1 297 ? -42.238 22.382 3.404 1.00 46.02 ? 297 ASP A OD1 1 ATOM 2285 O OD2 . ASP A 1 297 ? -43.781 20.826 3.613 1.00 46.81 ? 297 ASP A OD2 1 ATOM 2286 N N . GLY A 1 298 ? -39.203 21.953 3.163 1.00 52.77 ? 298 GLY A N 1 ATOM 2287 C CA . GLY A 1 298 ? -38.538 21.756 1.876 1.00 55.29 ? 298 GLY A CA 1 ATOM 2288 C C . GLY A 1 298 ? -39.496 21.475 0.721 1.00 56.70 ? 298 GLY A C 1 ATOM 2289 O O . GLY A 1 298 ? -39.062 21.359 -0.417 1.00 59.58 ? 298 GLY A O 1 ATOM 2290 N N . GLU A 1 299 ? -40.795 21.366 1.004 1.00 57.85 ? 299 GLU A N 1 ATOM 2291 C CA . GLU A 1 299 ? -41.802 21.080 -0.013 1.00 57.61 ? 299 GLU A CA 1 ATOM 2292 C C . GLU A 1 299 ? -42.639 22.319 -0.224 1.00 51.60 ? 299 GLU A C 1 ATOM 2293 O O . GLU A 1 299 ? -42.547 22.952 -1.253 1.00 50.73 ? 299 GLU A O 1 ATOM 2294 C CB . GLU A 1 299 ? -42.662 19.891 0.398 1.00 63.58 ? 299 GLU A CB 1 ATOM 2295 C CG . GLU A 1 299 ? -41.847 18.616 0.570 1.00 73.58 ? 299 GLU A CG 1 ATOM 2296 C CD . GLU A 1 299 ? -42.702 17.388 0.832 1.00 81.24 ? 299 GLU A CD 1 ATOM 2297 O OE1 . GLU A 1 299 ? -43.882 17.376 0.400 1.00 84.14 ? 299 GLU A OE1 1 ATOM 2298 O OE2 . GLU A 1 299 ? -42.185 16.433 1.462 1.00 84.27 ? 299 GLU A OE2 1 ATOM 2299 N N . PHE A 1 300 ? -43.423 22.696 0.769 1.00 49.41 ? 300 PHE A N 1 ATOM 2300 C CA . PHE A 1 300 ? -44.182 23.941 0.706 1.00 47.96 ? 300 PHE A CA 1 ATOM 2301 C C . PHE A 1 300 ? -43.241 25.140 0.541 1.00 48.04 ? 300 PHE A C 1 ATOM 2302 O O . PHE A 1 300 ? -43.550 26.090 -0.188 1.00 44.96 ? 300 PHE A O 1 ATOM 2303 C CB . PHE A 1 300 ? -45.013 24.094 1.973 1.00 46.02 ? 300 PHE A CB 1 ATOM 2304 C CG . PHE A 1 300 ? -46.141 25.070 1.848 1.00 43.71 ? 300 PHE A CG 1 ATOM 2305 C CD1 . PHE A 1 300 ? -45.940 26.416 2.092 1.00 42.71 ? 300 PHE A CD1 1 ATOM 2306 C CD2 . PHE A 1 300 ? -47.415 24.634 1.522 1.00 42.33 ? 300 PHE A CD2 1 ATOM 2307 C CE1 . PHE A 1 300 ? -46.985 27.312 2.001 1.00 40.99 ? 300 PHE A CE1 1 ATOM 2308 C CE2 . PHE A 1 300 ? -48.461 25.524 1.424 1.00 40.50 ? 300 PHE A CE2 1 ATOM 2309 C CZ . PHE A 1 300 ? -48.246 26.863 1.660 1.00 40.61 ? 300 PHE A CZ 1 ATOM 2310 N N . PHE A 1 301 ? -42.094 25.073 1.224 1.00 48.70 ? 301 PHE A N 1 ATOM 2311 C CA . PHE A 1 301 ? -41.044 26.076 1.120 1.00 47.26 ? 301 PHE A CA 1 ATOM 2312 C C . PHE A 1 301 ? -39.795 25.428 0.561 1.00 48.11 ? 301 PHE A C 1 ATOM 2313 O O . PHE A 1 301 ? -39.184 24.617 1.236 1.00 48.67 ? 301 PHE A O 1 ATOM 2314 C CB . PHE A 1 301 ? -40.736 26.642 2.496 1.00 46.42 ? 301 PHE A CB 1 ATOM 2315 C CG . PHE A 1 301 ? -41.928 27.225 3.187 1.00 46.06 ? 301 PHE A CG 1 ATOM 2316 C CD1 . PHE A 1 301 ? -42.390 28.485 2.850 1.00 46.50 ? 301 PHE A CD1 1 ATOM 2317 C CD2 . PHE A 1 301 ? -42.585 26.518 4.170 1.00 46.07 ? 301 PHE A CD2 1 ATOM 2318 C CE1 . PHE A 1 301 ? -43.485 29.033 3.492 1.00 47.09 ? 301 PHE A CE1 1 ATOM 2319 C CE2 . PHE A 1 301 ? -43.679 27.057 4.816 1.00 45.94 ? 301 PHE A CE2 1 ATOM 2320 C CZ . PHE A 1 301 ? -44.128 28.320 4.483 1.00 45.72 ? 301 PHE A CZ 1 ATOM 2321 N N . PRO A 1 302 ? -39.410 25.768 -0.678 1.00 49.59 ? 302 PRO A N 1 ATOM 2322 C CA . PRO A 1 302 ? -38.270 25.049 -1.268 1.00 50.94 ? 302 PRO A CA 1 ATOM 2323 C C . PRO A 1 302 ? -37.003 25.124 -0.430 1.00 50.99 ? 302 PRO A C 1 ATOM 2324 O O . PRO A 1 302 ? -36.241 24.158 -0.392 1.00 52.17 ? 302 PRO A O 1 ATOM 2325 C CB . PRO A 1 302 ? -38.064 25.736 -2.628 1.00 51.24 ? 302 PRO A CB 1 ATOM 2326 C CG . PRO A 1 302 ? -38.930 26.956 -2.609 1.00 50.69 ? 302 PRO A CG 1 ATOM 2327 C CD . PRO A 1 302 ? -40.037 26.686 -1.640 1.00 48.82 ? 302 PRO A CD 1 ATOM 2328 N N . THR A 1 303 ? -36.783 26.262 0.224 1.00 50.23 ? 303 THR A N 1 ATOM 2329 C CA . THR A 1 303 ? -35.619 26.452 1.096 1.00 50.57 ? 303 THR A CA 1 ATOM 2330 C C . THR A 1 303 ? -36.041 27.298 2.283 1.00 46.98 ? 303 THR A C 1 ATOM 2331 O O . THR A 1 303 ? -37.214 27.568 2.449 1.00 46.09 ? 303 THR A O 1 ATOM 2332 C CB . THR A 1 303 ? -34.424 27.111 0.347 1.00 52.81 ? 303 THR A CB 1 ATOM 2333 O OG1 . THR A 1 303 ? -34.760 28.442 -0.062 1.00 51.72 ? 303 THR A OG1 1 ATOM 2334 C CG2 . THR A 1 303 ? -34.013 26.287 -0.882 1.00 54.69 ? 303 THR A CG2 1 ATOM 2335 N N . SER A 1 304 ? -35.091 27.711 3.110 1.00 46.61 ? 304 SER A N 1 ATOM 2336 C CA . SER A 1 304 ? -35.408 28.500 4.294 1.00 45.44 ? 304 SER A CA 1 ATOM 2337 C C . SER A 1 304 ? -36.016 29.823 3.896 1.00 44.52 ? 304 SER A C 1 ATOM 2338 O O . SER A 1 304 ? -35.647 30.393 2.874 1.00 46.15 ? 304 SER A O 1 ATOM 2339 C CB . SER A 1 304 ? -34.155 28.800 5.115 1.00 45.81 ? 304 SER A CB 1 ATOM 2340 O OG . SER A 1 304 ? -33.460 29.901 4.551 1.00 46.22 ? 304 SER A OG 1 ATOM 2341 N N . LEU A 1 305 ? -36.911 30.325 4.739 1.00 43.23 ? 305 LEU A N 1 ATOM 2342 C CA . LEU A 1 305 ? -37.557 31.603 4.501 1.00 43.40 ? 305 LEU A CA 1 ATOM 2343 C C . LEU A 1 305 ? -36.541 32.696 4.187 1.00 45.15 ? 305 LEU A C 1 ATOM 2344 O O . LEU A 1 305 ? -36.721 33.451 3.232 1.00 48.02 ? 305 LEU A O 1 ATOM 2345 C CB . LEU A 1 305 ? -38.410 32.022 5.700 1.00 42.23 ? 305 LEU A CB 1 ATOM 2346 C CG . LEU A 1 305 ? -39.585 31.125 6.098 1.00 42.92 ? 305 LEU A CG 1 ATOM 2347 C CD1 . LEU A 1 305 ? -40.489 31.840 7.098 1.00 42.45 ? 305 LEU A CD1 1 ATOM 2348 C CD2 . LEU A 1 305 ? -40.391 30.669 4.886 1.00 42.76 ? 305 LEU A CD2 1 ATOM 2349 N N . GLU A 1 306 ? -35.470 32.777 4.971 1.00 46.26 ? 306 GLU A N 1 ATOM 2350 C CA . GLU A 1 306 ? -34.512 33.868 4.812 1.00 46.11 ? 306 GLU A CA 1 ATOM 2351 C C . GLU A 1 306 ? -33.817 33.810 3.458 1.00 45.84 ? 306 GLU A C 1 ATOM 2352 O O . GLU A 1 306 ? -33.674 34.842 2.809 1.00 45.23 ? 306 GLU A O 1 ATOM 2353 C CB . GLU A 1 306 ? -33.481 33.879 5.947 1.00 47.23 ? 306 GLU A CB 1 ATOM 2354 C CG . GLU A 1 306 ? -32.482 35.032 5.887 1.00 49.60 ? 306 GLU A CG 1 ATOM 2355 C CD . GLU A 1 306 ? -33.142 36.410 5.843 1.00 51.64 ? 306 GLU A CD 1 ATOM 2356 O OE1 . GLU A 1 306 ? -34.314 36.546 6.272 1.00 52.13 ? 306 GLU A OE1 1 ATOM 2357 O OE2 . GLU A 1 306 ? -32.487 37.374 5.390 1.00 52.53 ? 306 GLU A OE2 1 ATOM 2358 N N . SER A 1 307 ? -33.398 32.621 3.023 1.00 45.65 ? 307 SER A N 1 ATOM 2359 C CA . SER A 1 307 ? -32.692 32.511 1.734 1.00 47.81 ? 307 SER A CA 1 ATOM 2360 C C . SER A 1 307 ? -33.614 32.813 0.561 1.00 46.85 ? 307 SER A C 1 ATOM 2361 O O . SER A 1 307 ? -33.183 33.386 -0.434 1.00 49.76 ? 307 SER A O 1 ATOM 2362 C CB . SER A 1 307 ? -32.021 31.146 1.550 1.00 48.37 ? 307 SER A CB 1 ATOM 2363 O OG . SER A 1 307 ? -32.967 30.105 1.536 1.00 49.65 ? 307 SER A OG 1 ATOM 2364 N N . MET A 1 308 ? -34.878 32.428 0.685 1.00 45.36 ? 308 MET A N 1 ATOM 2365 C CA . MET A 1 308 ? -35.875 32.760 -0.322 1.00 45.93 ? 308 MET A CA 1 ATOM 2366 C C . MET A 1 308 ? -36.047 34.279 -0.442 1.00 45.30 ? 308 MET A C 1 ATOM 2367 O O . MET A 1 308 ? -36.154 34.813 -1.543 1.00 46.56 ? 308 MET A O 1 ATOM 2368 C CB . MET A 1 308 ? -37.220 32.097 0.003 1.00 45.40 ? 308 MET A CB 1 ATOM 2369 C CG . MET A 1 308 ? -37.197 30.581 -0.098 1.00 46.17 ? 308 MET A CG 1 ATOM 2370 S SD . MET A 1 308 ? -38.816 29.824 0.101 1.00 45.13 ? 308 MET A SD 1 ATOM 2371 C CE . MET A 1 308 ? -39.582 30.284 -1.445 1.00 46.27 ? 308 MET A CE 1 ATOM 2372 N N . LEU A 1 309 ? -36.065 34.974 0.686 1.00 44.10 ? 309 LEU A N 1 ATOM 2373 C CA . LEU A 1 309 ? -36.232 36.418 0.662 1.00 44.63 ? 309 LEU A CA 1 ATOM 2374 C C . LEU A 1 309 ? -35.005 37.090 0.050 1.00 46.71 ? 309 LEU A C 1 ATOM 2375 O O . LEU A 1 309 ? -35.138 38.021 -0.745 1.00 49.40 ? 309 LEU A O 1 ATOM 2376 C CB . LEU A 1 309 ? -36.526 36.960 2.065 1.00 43.57 ? 309 LEU A CB 1 ATOM 2377 C CG . LEU A 1 309 ? -37.910 36.614 2.642 1.00 42.75 ? 309 LEU A CG 1 ATOM 2378 C CD1 . LEU A 1 309 ? -37.993 37.005 4.107 1.00 43.18 ? 309 LEU A CD1 1 ATOM 2379 C CD2 . LEU A 1 309 ? -39.052 37.279 1.888 1.00 41.83 ? 309 LEU A CD2 1 ATOM 2380 N N . ASN A 1 310 ? -33.818 36.610 0.402 1.00 47.61 ? 310 ASN A N 1 ATOM 2381 C CA . ASN A 1 310 ? -32.586 37.116 -0.199 1.00 50.58 ? 310 ASN A CA 1 ATOM 2382 C C . ASN A 1 310 ? -32.492 36.897 -1.698 1.00 51.31 ? 310 ASN A C 1 ATOM 2383 O O . ASN A 1 310 ? -32.225 37.835 -2.432 1.00 52.88 ? 310 ASN A O 1 ATOM 2384 C CB . ASN A 1 310 ? -31.360 36.501 0.461 1.00 52.87 ? 310 ASN A CB 1 ATOM 2385 C CG . ASN A 1 310 ? -30.791 37.394 1.515 1.00 54.41 ? 310 ASN A CG 1 ATOM 2386 O OD1 . ASN A 1 310 ? -29.968 38.248 1.221 1.00 58.01 ? 310 ASN A OD1 1 ATOM 2387 N ND2 . ASN A 1 310 ? -31.250 37.229 2.746 1.00 54.03 ? 310 ASN A ND2 1 ATOM 2388 N N . SER A 1 311 ? -32.713 35.661 -2.144 1.00 50.35 ? 311 SER A N 1 ATOM 2389 C CA . SER A 1 311 ? -32.620 35.323 -3.562 1.00 51.21 ? 311 SER A CA 1 ATOM 2390 C C . SER A 1 311 ? -33.688 35.978 -4.430 1.00 50.22 ? 311 SER A C 1 ATOM 2391 O O . SER A 1 311 ? -33.558 35.996 -5.643 1.00 51.88 ? 311 SER A O 1 ATOM 2392 C CB . SER A 1 311 ? -32.695 33.806 -3.759 1.00 52.29 ? 311 SER A CB 1 ATOM 2393 O OG . SER A 1 311 ? -33.900 33.270 -3.240 1.00 51.52 ? 311 SER A OG 1 ATOM 2394 N N . GLY A 1 312 ? -34.747 36.499 -3.821 1.00 48.28 ? 312 GLY A N 1 ATOM 2395 C CA . GLY A 1 312 ? -35.891 36.974 -4.579 1.00 47.66 ? 312 GLY A CA 1 ATOM 2396 C C . GLY A 1 312 ? -36.773 35.815 -5.024 1.00 46.59 ? 312 GLY A C 1 ATOM 2397 O O . GLY A 1 312 ? -37.537 35.937 -5.993 1.00 46.13 ? 312 GLY A O 1 ATOM 2398 N N . ASN A 1 313 ? -36.677 34.685 -4.325 1.00 44.17 ? 313 ASN A N 1 ATOM 2399 C CA . ASN A 1 313 ? -37.493 33.536 -4.657 1.00 42.93 ? 313 ASN A CA 1 ATOM 2400 C C . ASN A 1 313 ? -38.867 33.702 -4.027 1.00 41.86 ? 313 ASN A C 1 ATOM 2401 O O . ASN A 1 313 ? -39.149 33.166 -2.960 1.00 42.24 ? 313 ASN A O 1 ATOM 2402 C CB . ASN A 1 313 ? -36.829 32.238 -4.205 1.00 42.53 ? 313 ASN A CB 1 ATOM 2403 C CG . ASN A 1 313 ? -37.546 31.016 -4.727 1.00 42.76 ? 313 ASN A CG 1 ATOM 2404 O OD1 . ASN A 1 313 ? -38.534 31.127 -5.450 1.00 43.57 ? 313 ASN A OD1 1 ATOM 2405 N ND2 . ASN A 1 313 ? -37.055 29.845 -4.371 1.00 43.14 ? 313 ASN A ND2 1 ATOM 2406 N N . PHE A 1 314 ? -39.712 34.477 -4.694 1.00 41.38 ? 314 PHE A N 1 ATOM 2407 C CA . PHE A 1 314 ? -41.078 34.712 -4.244 1.00 39.45 ? 314 PHE A CA 1 ATOM 2408 C C . PHE A 1 314 ? -41.886 35.453 -5.306 1.00 39.07 ? 314 PHE A C 1 ATOM 2409 O O . PHE A 1 314 ? -41.332 36.038 -6.239 1.00 38.06 ? 314 PHE A O 1 ATOM 2410 C CB . PHE A 1 314 ? -41.106 35.482 -2.909 1.00 39.09 ? 314 PHE A CB 1 ATOM 2411 C CG . PHE A 1 314 ? -40.263 36.740 -2.890 1.00 39.54 ? 314 PHE A CG 1 ATOM 2412 C CD1 . PHE A 1 314 ? -40.750 37.934 -3.412 1.00 39.35 ? 314 PHE A CD1 1 ATOM 2413 C CD2 . PHE A 1 314 ? -39.000 36.740 -2.321 1.00 40.04 ? 314 PHE A CD2 1 ATOM 2414 C CE1 . PHE A 1 314 ? -39.989 39.091 -3.389 1.00 39.39 ? 314 PHE A CE1 1 ATOM 2415 C CE2 . PHE A 1 314 ? -38.238 37.900 -2.284 1.00 40.40 ? 314 PHE A CE2 1 ATOM 2416 C CZ . PHE A 1 314 ? -38.731 39.074 -2.827 1.00 40.17 ? 314 PHE A CZ 1 ATOM 2417 N N . LYS A 1 315 ? -43.204 35.433 -5.150 1.00 39.01 ? 315 LYS A N 1 ATOM 2418 C CA . LYS A 1 315 ? -44.070 36.087 -6.114 1.00 39.44 ? 315 LYS A CA 1 ATOM 2419 C C . LYS A 1 315 ? -43.790 37.578 -6.097 1.00 40.18 ? 315 LYS A C 1 ATOM 2420 O O . LYS A 1 315 ? -43.687 38.184 -5.037 1.00 37.67 ? 315 LYS A O 1 ATOM 2421 C CB . LYS A 1 315 ? -45.533 35.822 -5.798 1.00 38.61 ? 315 LYS A CB 1 ATOM 2422 C CG . LYS A 1 315 ? -46.499 36.288 -6.877 1.00 38.99 ? 315 LYS A CG 1 ATOM 2423 C CD . LYS A 1 315 ? -47.931 36.170 -6.382 1.00 38.80 ? 315 LYS A CD 1 ATOM 2424 C CE . LYS A 1 315 ? -48.929 36.794 -7.337 1.00 39.40 ? 315 LYS A CE 1 ATOM 2425 N NZ . LYS A 1 315 ? -49.285 35.834 -8.406 1.00 40.22 ? 315 LYS A NZ 1 ATOM 2426 N N . LYS A 1 316 ? -43.667 38.155 -7.286 1.00 42.60 ? 316 LYS A N 1 ATOM 2427 C CA . LYS A 1 316 ? -43.388 39.570 -7.439 1.00 43.63 ? 316 LYS A CA 1 ATOM 2428 C C . LYS A 1 316 ? -44.644 40.287 -7.916 1.00 42.59 ? 316 LYS A C 1 ATOM 2429 O O . LYS A 1 316 ? -45.099 40.097 -9.026 1.00 43.43 ? 316 LYS A O 1 ATOM 2430 C CB . LYS A 1 316 ? -42.212 39.756 -8.386 1.00 46.12 ? 316 LYS A CB 1 ATOM 2431 C CG . LYS A 1 316 ? -40.929 39.182 -7.795 1.00 48.90 ? 316 LYS A CG 1 ATOM 2432 C CD . LYS A 1 316 ? -39.841 38.960 -8.841 1.00 54.06 ? 316 LYS A CD 1 ATOM 2433 C CE . LYS A 1 316 ? -38.701 38.071 -8.333 1.00 55.87 ? 316 LYS A CE 1 ATOM 2434 N NZ . LYS A 1 316 ? -39.104 36.646 -8.137 1.00 56.12 ? 316 LYS A NZ 1 ATOM 2435 N N . THR A 1 317 ? -45.211 41.095 -7.032 1.00 43.09 ? 317 THR A N 1 ATOM 2436 C CA . THR A 1 317 ? -46.466 41.798 -7.286 1.00 43.68 ? 317 THR A CA 1 ATOM 2437 C C . THR A 1 317 ? -46.577 42.986 -6.319 1.00 44.60 ? 317 THR A C 1 ATOM 2438 O O . THR A 1 317 ? -45.576 43.412 -5.746 1.00 45.71 ? 317 THR A O 1 ATOM 2439 C CB . THR A 1 317 ? -47.668 40.832 -7.159 1.00 41.89 ? 317 THR A CB 1 ATOM 2440 O OG1 . THR A 1 317 ? -48.889 41.517 -7.447 1.00 41.71 ? 317 THR A OG1 1 ATOM 2441 C CG2 . THR A 1 317 ? -47.738 40.209 -5.774 1.00 40.01 ? 317 THR A CG2 1 ATOM 2442 N N . GLN A 1 318 ? -47.775 43.534 -6.152 1.00 45.54 ? 318 GLN A N 1 ATOM 2443 C CA . GLN A 1 318 ? -47.991 44.615 -5.198 1.00 45.26 ? 318 GLN A CA 1 ATOM 2444 C C . GLN A 1 318 ? -48.342 44.016 -3.857 1.00 44.65 ? 318 GLN A C 1 ATOM 2445 O O . GLN A 1 318 ? -49.009 42.985 -3.790 1.00 44.46 ? 318 GLN A O 1 ATOM 2446 C CB . GLN A 1 318 ? -49.135 45.522 -5.636 1.00 46.44 ? 318 GLN A CB 1 ATOM 2447 C CG . GLN A 1 318 ? -48.900 46.250 -6.952 1.00 48.92 ? 318 GLN A CG 1 ATOM 2448 C CD . GLN A 1 318 ? -49.211 45.408 -8.172 1.00 48.42 ? 318 GLN A CD 1 ATOM 2449 O OE1 . GLN A 1 318 ? -49.998 44.470 -8.108 1.00 46.44 ? 318 GLN A OE1 1 ATOM 2450 N NE2 . GLN A 1 318 ? -48.588 45.742 -9.291 1.00 49.72 ? 318 GLN A NE2 1 ATOM 2451 N N . ILE A 1 319 ? -47.891 44.652 -2.784 1.00 45.51 ? 319 ILE A N 1 ATOM 2452 C CA . ILE A 1 319 ? -48.357 44.289 -1.453 1.00 44.35 ? 319 ILE A CA 1 ATOM 2453 C C . ILE A 1 319 ? -48.699 45.528 -0.662 1.00 44.57 ? 319 ILE A C 1 ATOM 2454 O O . ILE A 1 319 ? -48.085 46.592 -0.846 1.00 46.12 ? 319 ILE A O 1 ATOM 2455 C CB . ILE A 1 319 ? -47.328 43.457 -0.665 1.00 44.65 ? 319 ILE A CB 1 ATOM 2456 C CG1 . ILE A 1 319 ? -46.044 44.254 -0.404 1.00 45.43 ? 319 ILE A CG1 1 ATOM 2457 C CG2 . ILE A 1 319 ? -47.023 42.167 -1.416 1.00 44.85 ? 319 ILE A CG2 1 ATOM 2458 C CD1 . ILE A 1 319 ? -45.102 43.575 0.560 1.00 44.25 ? 319 ILE A CD1 1 ATOM 2459 N N . LEU A 1 320 ? -49.703 45.380 0.195 1.00 42.99 ? 320 LEU A N 1 ATOM 2460 C CA . LEU A 1 320 ? -50.101 46.414 1.128 1.00 42.89 ? 320 LEU A CA 1 ATOM 2461 C C . LEU A 1 320 ? -50.118 45.776 2.508 1.00 42.55 ? 320 LEU A C 1 ATOM 2462 O O . LEU A 1 320 ? -50.683 44.690 2.686 1.00 42.82 ? 320 LEU A O 1 ATOM 2463 C CB . LEU A 1 320 ? -51.478 46.946 0.755 1.00 42.65 ? 320 LEU A CB 1 ATOM 2464 C CG . LEU A 1 320 ? -52.003 48.106 1.603 1.00 42.39 ? 320 LEU A CG 1 ATOM 2465 C CD1 . LEU A 1 320 ? -52.973 48.952 0.791 1.00 43.21 ? 320 LEU A CD1 1 ATOM 2466 C CD2 . LEU A 1 320 ? -52.648 47.627 2.898 1.00 41.24 ? 320 LEU A CD2 1 ATOM 2467 N N . LEU A 1 321 ? -49.493 46.439 3.478 1.00 41.53 ? 321 LEU A N 1 ATOM 2468 C CA . LEU A 1 321 ? -49.352 45.866 4.821 1.00 39.19 ? 321 LEU A CA 1 ATOM 2469 C C . LEU A 1 321 ? -49.001 46.876 5.896 1.00 39.38 ? 321 LEU A C 1 ATOM 2470 O O . LEU A 1 321 ? -48.638 48.024 5.616 1.00 40.01 ? 321 LEU A O 1 ATOM 2471 C CB . LEU A 1 321 ? -48.312 44.732 4.843 1.00 37.79 ? 321 LEU A CB 1 ATOM 2472 C CG . LEU A 1 321 ? -46.984 44.789 4.078 1.00 38.20 ? 321 LEU A CG 1 ATOM 2473 C CD1 . LEU A 1 321 ? -46.476 46.190 3.798 1.00 40.55 ? 321 LEU A CD1 1 ATOM 2474 C CD2 . LEU A 1 321 ? -45.925 43.978 4.807 1.00 36.74 ? 321 LEU A CD2 1 ATOM 2475 N N . GLY A 1 322 ? -49.120 46.433 7.139 1.00 38.07 ? 322 GLY A N 1 ATOM 2476 C CA . GLY A 1 322 ? -48.796 47.281 8.254 1.00 38.12 ? 322 GLY A CA 1 ATOM 2477 C C . GLY A 1 322 ? -49.080 46.622 9.567 1.00 36.98 ? 322 GLY A C 1 ATOM 2478 O O . GLY A 1 322 ? -49.385 45.428 9.612 1.00 34.89 ? 322 GLY A O 1 ATOM 2479 N N . VAL A 1 323 ? -49.003 47.429 10.625 1.00 37.77 ? 323 VAL A N 1 ATOM 2480 C CA . VAL A 1 323 ? -49.057 46.944 12.002 1.00 38.81 ? 323 VAL A CA 1 ATOM 2481 C C . VAL A 1 323 ? -49.788 47.923 12.907 1.00 39.18 ? 323 VAL A C 1 ATOM 2482 O O . VAL A 1 323 ? -50.076 49.046 12.512 1.00 40.08 ? 323 VAL A O 1 ATOM 2483 C CB . VAL A 1 323 ? -47.637 46.755 12.575 1.00 39.11 ? 323 VAL A CB 1 ATOM 2484 C CG1 . VAL A 1 323 ? -46.836 45.786 11.717 1.00 38.36 ? 323 VAL A CG1 1 ATOM 2485 C CG2 . VAL A 1 323 ? -46.922 48.095 12.684 1.00 40.67 ? 323 VAL A CG2 1 ATOM 2486 N N . ASN A 1 324 ? -50.074 47.492 14.129 1.00 38.96 ? 324 ASN A N 1 ATOM 2487 C CA . ASN A 1 324 ? -50.727 48.358 15.108 1.00 40.59 ? 324 ASN A CA 1 ATOM 2488 C C . ASN A 1 324 ? -49.779 48.864 16.196 1.00 40.81 ? 324 ASN A C 1 ATOM 2489 O O . ASN A 1 324 ? -48.750 48.267 16.472 1.00 40.38 ? 324 ASN A O 1 ATOM 2490 C CB . ASN A 1 324 ? -51.913 47.645 15.733 1.00 40.44 ? 324 ASN A CB 1 ATOM 2491 C CG . ASN A 1 324 ? -52.937 47.228 14.711 1.00 41.33 ? 324 ASN A CG 1 ATOM 2492 O OD1 . ASN A 1 324 ? -52.800 47.501 13.524 1.00 44.23 ? 324 ASN A OD1 1 ATOM 2493 N ND2 . ASN A 1 324 ? -53.968 46.547 15.165 1.00 42.85 ? 324 ASN A ND2 1 ATOM 2494 N N . LYS A 1 325 ? -50.142 49.977 16.812 1.00 42.83 ? 325 LYS A N 1 ATOM 2495 C CA . LYS A 1 325 ? -49.296 50.619 17.811 1.00 44.30 ? 325 LYS A CA 1 ATOM 2496 C C . LYS A 1 325 ? -48.880 49.680 18.944 1.00 43.51 ? 325 LYS A C 1 ATOM 2497 O O . LYS A 1 325 ? -47.754 49.749 19.405 1.00 44.19 ? 325 LYS A O 1 ATOM 2498 C CB . LYS A 1 325 ? -50.024 51.836 18.370 1.00 46.58 ? 325 LYS A CB 1 ATOM 2499 C CG . LYS A 1 325 ? -49.231 52.746 19.288 1.00 49.59 ? 325 LYS A CG 1 ATOM 2500 C CD . LYS A 1 325 ? -50.022 54.034 19.515 1.00 53.80 ? 325 LYS A CD 1 ATOM 2501 C CE . LYS A 1 325 ? -50.155 54.393 20.984 1.00 56.81 ? 325 LYS A CE 1 ATOM 2502 N NZ . LYS A 1 325 ? -48.924 55.066 21.475 1.00 59.24 ? 325 LYS A NZ 1 ATOM 2503 N N . ASP A 1 326 ? -49.767 48.790 19.379 1.00 43.26 ? 326 ASP A N 1 ATOM 2504 C CA . ASP A 1 326 ? -49.528 48.008 20.596 1.00 43.67 ? 326 ASP A CA 1 ATOM 2505 C C . ASP A 1 326 ? -49.795 46.506 20.406 1.00 43.34 ? 326 ASP A C 1 ATOM 2506 O O . ASP A 1 326 ? -50.661 45.911 21.054 1.00 42.68 ? 326 ASP A O 1 ATOM 2507 C CB . ASP A 1 326 ? -50.365 48.589 21.748 1.00 45.14 ? 326 ASP A CB 1 ATOM 2508 C CG . ASP A 1 326 ? -49.980 50.019 22.084 1.00 46.19 ? 326 ASP A CG 1 ATOM 2509 O OD1 . ASP A 1 326 ? -48.888 50.199 22.648 1.00 49.64 ? 326 ASP A OD1 1 ATOM 2510 O OD2 . ASP A 1 326 ? -50.751 50.965 21.789 1.00 46.90 ? 326 ASP A OD2 1 ATOM 2511 N N . GLU A 1 327 ? -49.003 45.885 19.537 1.00 44.41 ? 327 GLU A N 1 ATOM 2512 C CA . GLU A 1 327 ? -49.216 44.484 19.156 1.00 43.28 ? 327 GLU A CA 1 ATOM 2513 C C . GLU A 1 327 ? -49.006 43.501 20.318 1.00 43.09 ? 327 GLU A C 1 ATOM 2514 O O . GLU A 1 327 ? -49.548 42.398 20.301 1.00 45.35 ? 327 GLU A O 1 ATOM 2515 C CB . GLU A 1 327 ? -48.289 44.102 17.989 1.00 43.84 ? 327 GLU A CB 1 ATOM 2516 C CG . GLU A 1 327 ? -48.502 44.890 16.691 1.00 44.08 ? 327 GLU A CG 1 ATOM 2517 C CD . GLU A 1 327 ? -49.682 44.414 15.843 1.00 43.43 ? 327 GLU A CD 1 ATOM 2518 O OE1 . GLU A 1 327 ? -50.500 43.599 16.318 1.00 43.24 ? 327 GLU A OE1 1 ATOM 2519 O OE2 . GLU A 1 327 ? -49.800 44.876 14.687 1.00 43.45 ? 327 GLU A OE2 1 ATOM 2520 N N . GLY A 1 328 ? -48.224 43.892 21.321 1.00 42.53 ? 328 GLY A N 1 ATOM 2521 C CA . GLY A 1 328 ? -47.844 42.974 22.390 1.00 41.40 ? 328 GLY A CA 1 ATOM 2522 C C . GLY A 1 328 ? -48.832 42.800 23.531 1.00 41.41 ? 328 GLY A C 1 ATOM 2523 O O . GLY A 1 328 ? -48.910 41.723 24.120 1.00 41.03 ? 328 GLY A O 1 ATOM 2524 N N . SER A 1 329 ? -49.588 43.847 23.841 1.00 41.74 ? 329 SER A N 1 ATOM 2525 C CA . SER A 1 329 ? -50.396 43.888 25.059 1.00 43.24 ? 329 SER A CA 1 ATOM 2526 C C . SER A 1 329 ? -51.288 42.667 25.309 1.00 44.08 ? 329 SER A C 1 ATOM 2527 O O . SER A 1 329 ? -51.421 42.232 26.457 1.00 47.23 ? 329 SER A O 1 ATOM 2528 C CB . SER A 1 329 ? -51.253 45.164 25.100 1.00 44.09 ? 329 SER A CB 1 ATOM 2529 O OG . SER A 1 329 ? -52.216 45.199 24.058 1.00 44.55 ? 329 SER A OG 1 ATOM 2530 N N . PHE A 1 330 ? -51.898 42.114 24.262 1.00 43.80 ? 330 PHE A N 1 ATOM 2531 C CA . PHE A 1 330 ? -52.838 40.988 24.430 1.00 43.79 ? 330 PHE A CA 1 ATOM 2532 C C . PHE A 1 330 ? -52.179 39.779 25.086 1.00 42.29 ? 330 PHE A C 1 ATOM 2533 O O . PHE A 1 330 ? -52.766 39.103 25.936 1.00 43.24 ? 330 PHE A O 1 ATOM 2534 C CB . PHE A 1 330 ? -53.423 40.548 23.080 1.00 44.13 ? 330 PHE A CB 1 ATOM 2535 C CG . PHE A 1 330 ? -54.838 40.075 23.173 1.00 45.48 ? 330 PHE A CG 1 ATOM 2536 C CD1 . PHE A 1 330 ? -55.142 38.873 23.772 1.00 48.60 ? 330 PHE A CD1 1 ATOM 2537 C CD2 . PHE A 1 330 ? -55.864 40.839 22.683 1.00 46.41 ? 330 PHE A CD2 1 ATOM 2538 C CE1 . PHE A 1 330 ? -56.453 38.444 23.881 1.00 49.35 ? 330 PHE A CE1 1 ATOM 2539 C CE2 . PHE A 1 330 ? -57.170 40.421 22.782 1.00 48.26 ? 330 PHE A CE2 1 ATOM 2540 C CZ . PHE A 1 330 ? -57.469 39.218 23.381 1.00 48.70 ? 330 PHE A CZ 1 ATOM 2541 N N . PHE A 1 331 ? -50.939 39.537 24.693 1.00 39.80 ? 331 PHE A N 1 ATOM 2542 C CA . PHE A 1 331 ? -50.211 38.354 25.091 1.00 39.17 ? 331 PHE A CA 1 ATOM 2543 C C . PHE A 1 331 ? -49.630 38.529 26.466 1.00 39.68 ? 331 PHE A C 1 ATOM 2544 O O . PHE A 1 331 ? -49.563 37.569 27.222 1.00 42.67 ? 331 PHE A O 1 ATOM 2545 C CB . PHE A 1 331 ? -49.124 38.054 24.067 1.00 38.77 ? 331 PHE A CB 1 ATOM 2546 C CG . PHE A 1 331 ? -49.673 37.868 22.708 1.00 37.18 ? 331 PHE A CG 1 ATOM 2547 C CD1 . PHE A 1 331 ? -50.112 36.622 22.306 1.00 36.54 ? 331 PHE A CD1 1 ATOM 2548 C CD2 . PHE A 1 331 ? -49.853 38.954 21.873 1.00 36.40 ? 331 PHE A CD2 1 ATOM 2549 C CE1 . PHE A 1 331 ? -50.681 36.444 21.063 1.00 36.70 ? 331 PHE A CE1 1 ATOM 2550 C CE2 . PHE A 1 331 ? -50.424 38.787 20.635 1.00 36.91 ? 331 PHE A CE2 1 ATOM 2551 C CZ . PHE A 1 331 ? -50.833 37.527 20.224 1.00 36.58 ? 331 PHE A CZ 1 ATOM 2552 N N . LEU A 1 332 ? -49.228 39.748 26.801 1.00 39.43 ? 332 LEU A N 1 ATOM 2553 C CA . LEU A 1 332 ? -48.771 40.036 28.153 1.00 41.71 ? 332 LEU A CA 1 ATOM 2554 C C . LEU A 1 332 ? -49.888 39.858 29.181 1.00 42.02 ? 332 LEU A C 1 ATOM 2555 O O . LEU A 1 332 ? -49.649 39.355 30.273 1.00 42.34 ? 332 LEU A O 1 ATOM 2556 C CB . LEU A 1 332 ? -48.179 41.444 28.234 1.00 43.45 ? 332 LEU A CB 1 ATOM 2557 C CG . LEU A 1 332 ? -46.832 41.608 27.524 1.00 42.67 ? 332 LEU A CG 1 ATOM 2558 C CD1 . LEU A 1 332 ? -46.596 43.060 27.169 1.00 42.79 ? 332 LEU A CD1 1 ATOM 2559 C CD2 . LEU A 1 332 ? -45.700 41.073 28.389 1.00 43.21 ? 332 LEU A CD2 1 ATOM 2560 N N . LEU A 1 333 ? -51.103 40.263 28.821 1.00 42.58 ? 333 LEU A N 1 ATOM 2561 C CA . LEU A 1 333 ? -52.254 40.128 29.705 1.00 43.26 ? 333 LEU A CA 1 ATOM 2562 C C . LEU A 1 333 ? -52.468 38.675 30.075 1.00 44.18 ? 333 LEU A C 1 ATOM 2563 O O . LEU A 1 333 ? -52.689 38.351 31.230 1.00 46.14 ? 333 LEU A O 1 ATOM 2564 C CB . LEU A 1 333 ? -53.514 40.675 29.033 1.00 42.93 ? 333 LEU A CB 1 ATOM 2565 C CG . LEU A 1 333 ? -54.838 40.368 29.745 1.00 44.45 ? 333 LEU A CG 1 ATOM 2566 C CD1 . LEU A 1 333 ? -54.883 40.971 31.139 1.00 45.60 ? 333 LEU A CD1 1 ATOM 2567 C CD2 . LEU A 1 333 ? -56.014 40.858 28.925 1.00 44.79 ? 333 LEU A CD2 1 ATOM 2568 N N . TYR A 1 334 ? -52.405 37.805 29.077 1.00 45.29 ? 334 TYR A N 1 ATOM 2569 C CA . TYR A 1 334 ? -52.707 36.382 29.253 1.00 46.07 ? 334 TYR A CA 1 ATOM 2570 C C . TYR A 1 334 ? -51.581 35.577 29.918 1.00 46.60 ? 334 TYR A C 1 ATOM 2571 O O . TYR A 1 334 ? -51.854 34.707 30.757 1.00 50.27 ? 334 TYR A O 1 ATOM 2572 C CB . TYR A 1 334 ? -53.067 35.757 27.895 1.00 44.84 ? 334 TYR A CB 1 ATOM 2573 C CG . TYR A 1 334 ? -54.524 35.922 27.525 1.00 45.05 ? 334 TYR A CG 1 ATOM 2574 C CD1 . TYR A 1 334 ? -55.044 37.171 27.207 1.00 46.01 ? 334 TYR A CD1 1 ATOM 2575 C CD2 . TYR A 1 334 ? -55.389 34.829 27.511 1.00 44.87 ? 334 TYR A CD2 1 ATOM 2576 C CE1 . TYR A 1 334 ? -56.382 37.329 26.881 1.00 45.62 ? 334 TYR A CE1 1 ATOM 2577 C CE2 . TYR A 1 334 ? -56.727 34.974 27.185 1.00 45.27 ? 334 TYR A CE2 1 ATOM 2578 C CZ . TYR A 1 334 ? -57.220 36.225 26.865 1.00 45.31 ? 334 TYR A CZ 1 ATOM 2579 O OH . TYR A 1 334 ? -58.550 36.380 26.542 1.00 44.14 ? 334 TYR A OH 1 ATOM 2580 N N . GLY A 1 335 ? -50.333 35.871 29.551 1.00 45.16 ? 335 GLY A N 1 ATOM 2581 C CA . GLY A 1 335 ? -49.183 35.060 29.964 1.00 44.64 ? 335 GLY A CA 1 ATOM 2582 C C . GLY A 1 335 ? -48.160 35.663 30.920 1.00 44.11 ? 335 GLY A C 1 ATOM 2583 O O . GLY A 1 335 ? -47.430 34.933 31.572 1.00 46.67 ? 335 GLY A O 1 ATOM 2584 N N . ALA A 1 336 ? -48.085 36.979 31.021 1.00 41.90 ? 336 ALA A N 1 ATOM 2585 C CA . ALA A 1 336 ? -47.004 37.583 31.773 1.00 41.31 ? 336 ALA A CA 1 ATOM 2586 C C . ALA A 1 336 ? -47.456 37.976 33.170 1.00 42.71 ? 336 ALA A C 1 ATOM 2587 O O . ALA A 1 336 ? -48.505 38.585 33.326 1.00 43.21 ? 336 ALA A O 1 ATOM 2588 C CB . ALA A 1 336 ? -46.474 38.793 31.032 1.00 41.11 ? 336 ALA A CB 1 ATOM 2589 N N . PRO A 1 337 ? -46.648 37.661 34.192 1.00 43.46 ? 337 PRO A N 1 ATOM 2590 C CA . PRO A 1 337 ? -47.020 38.069 35.531 1.00 45.17 ? 337 PRO A CA 1 ATOM 2591 C C . PRO A 1 337 ? -47.004 39.578 35.641 1.00 44.92 ? 337 PRO A C 1 ATOM 2592 O O . PRO A 1 337 ? -46.161 40.219 35.010 1.00 45.68 ? 337 PRO A O 1 ATOM 2593 C CB . PRO A 1 337 ? -45.909 37.481 36.394 1.00 46.63 ? 337 PRO A CB 1 ATOM 2594 C CG . PRO A 1 337 ? -44.722 37.491 35.499 1.00 46.22 ? 337 PRO A CG 1 ATOM 2595 C CD . PRO A 1 337 ? -45.253 37.192 34.129 1.00 44.19 ? 337 PRO A CD 1 ATOM 2596 N N . GLY A 1 338 ? -47.937 40.119 36.426 1.00 45.03 ? 338 GLY A N 1 ATOM 2597 C CA . GLY A 1 338 ? -48.084 41.561 36.640 1.00 45.32 ? 338 GLY A CA 1 ATOM 2598 C C . GLY A 1 338 ? -49.259 42.202 35.897 1.00 45.53 ? 338 GLY A C 1 ATOM 2599 O O . GLY A 1 338 ? -49.785 43.229 36.332 1.00 47.13 ? 338 GLY A O 1 ATOM 2600 N N . PHE A 1 339 ? -49.683 41.590 34.791 1.00 43.82 ? 339 PHE A N 1 ATOM 2601 C CA . PHE A 1 339 ? -50.693 42.163 33.916 1.00 43.60 ? 339 PHE A CA 1 ATOM 2602 C C . PHE A 1 339 ? -52.082 41.637 34.229 1.00 45.53 ? 339 PHE A C 1 ATOM 2603 O O . PHE A 1 339 ? -52.280 40.430 34.352 1.00 45.70 ? 339 PHE A O 1 ATOM 2604 C CB . PHE A 1 339 ? -50.349 41.840 32.464 1.00 41.71 ? 339 PHE A CB 1 ATOM 2605 C CG . PHE A 1 339 ? -49.103 42.515 31.991 1.00 40.62 ? 339 PHE A CG 1 ATOM 2606 C CD1 . PHE A 1 339 ? -47.855 41.989 32.299 1.00 40.22 ? 339 PHE A CD1 1 ATOM 2607 C CD2 . PHE A 1 339 ? -49.173 43.696 31.280 1.00 39.30 ? 339 PHE A CD2 1 ATOM 2608 C CE1 . PHE A 1 339 ? -46.704 42.621 31.883 1.00 39.36 ? 339 PHE A CE1 1 ATOM 2609 C CE2 . PHE A 1 339 ? -48.028 44.329 30.858 1.00 38.98 ? 339 PHE A CE2 1 ATOM 2610 C CZ . PHE A 1 339 ? -46.791 43.790 31.156 1.00 38.95 ? 339 PHE A CZ 1 ATOM 2611 N N . SER A 1 340 ? -53.044 42.551 34.327 1.00 47.63 ? 340 SER A N 1 ATOM 2612 C CA . SER A 1 340 ? -54.430 42.196 34.618 1.00 49.16 ? 340 SER A CA 1 ATOM 2613 C C . SER A 1 340 ? -55.410 43.063 33.837 1.00 48.87 ? 340 SER A C 1 ATOM 2614 O O . SER A 1 340 ? -55.108 44.208 33.502 1.00 50.31 ? 340 SER A O 1 ATOM 2615 C CB . SER A 1 340 ? -54.692 42.339 36.108 1.00 51.94 ? 340 SER A CB 1 ATOM 2616 O OG . SER A 1 340 ? -54.086 41.265 36.797 1.00 55.05 ? 340 SER A OG 1 ATOM 2617 N N . LYS A 1 341 ? -56.591 42.518 33.564 1.00 47.35 ? 341 LYS A N 1 ATOM 2618 C CA . LYS A 1 341 ? -57.569 43.217 32.751 1.00 46.71 ? 341 LYS A CA 1 ATOM 2619 C C . LYS A 1 341 ? -58.134 44.449 33.431 1.00 47.45 ? 341 LYS A C 1 ATOM 2620 O O . LYS A 1 341 ? -58.517 45.398 32.758 1.00 50.44 ? 341 LYS A O 1 ATOM 2621 C CB . LYS A 1 341 ? -58.719 42.292 32.346 1.00 46.85 ? 341 LYS A CB 1 ATOM 2622 C CG . LYS A 1 341 ? -59.577 42.877 31.226 1.00 47.18 ? 341 LYS A CG 1 ATOM 2623 C CD . LYS A 1 341 ? -60.666 41.925 30.740 1.00 47.45 ? 341 LYS A CD 1 ATOM 2624 C CE . LYS A 1 341 ? -61.765 41.715 31.775 1.00 49.59 ? 341 LYS A CE 1 ATOM 2625 N NZ . LYS A 1 341 ? -62.384 42.977 32.271 1.00 50.61 ? 341 LYS A NZ 1 ATOM 2626 N N . ASP A 1 342 ? -58.198 44.445 34.754 1.00 47.16 ? 342 ASP A N 1 ATOM 2627 C CA . ASP A 1 342 ? -58.925 45.486 35.470 1.00 48.13 ? 342 ASP A CA 1 ATOM 2628 C C . ASP A 1 342 ? -58.034 46.434 36.266 1.00 48.63 ? 342 ASP A C 1 ATOM 2629 O O . ASP A 1 342 ? -58.524 47.235 37.046 1.00 48.40 ? 342 ASP A O 1 ATOM 2630 C CB . ASP A 1 342 ? -59.968 44.839 36.383 1.00 49.01 ? 342 ASP A CB 1 ATOM 2631 C CG . ASP A 1 342 ? -60.999 44.026 35.615 1.00 48.02 ? 342 ASP A CG 1 ATOM 2632 O OD1 . ASP A 1 342 ? -61.008 44.071 34.365 1.00 45.58 ? 342 ASP A OD1 1 ATOM 2633 O OD2 . ASP A 1 342 ? -61.812 43.344 36.277 1.00 49.24 ? 342 ASP A OD2 1 ATOM 2634 N N . SER A 1 343 ? -56.730 46.354 36.050 1.00 49.98 ? 343 SER A N 1 ATOM 2635 C CA . SER A 1 343 ? -55.780 47.266 36.682 1.00 52.29 ? 343 SER A CA 1 ATOM 2636 C C . SER A 1 343 ? -55.027 48.019 35.607 1.00 51.53 ? 343 SER A C 1 ATOM 2637 O O . SER A 1 343 ? -55.020 47.611 34.451 1.00 48.87 ? 343 SER A O 1 ATOM 2638 C CB . SER A 1 343 ? -54.779 46.497 37.559 1.00 53.14 ? 343 SER A CB 1 ATOM 2639 O OG . SER A 1 343 ? -54.016 45.572 36.796 1.00 52.73 ? 343 SER A OG 1 ATOM 2640 N N . GLU A 1 344 ? -54.385 49.111 36.007 1.00 54.23 ? 344 GLU A N 1 ATOM 2641 C CA . GLU A 1 344 ? -53.431 49.804 35.147 1.00 55.28 ? 344 GLU A CA 1 ATOM 2642 C C . GLU A 1 344 ? -52.264 48.883 34.768 1.00 52.46 ? 344 GLU A C 1 ATOM 2643 O O . GLU A 1 344 ? -51.602 49.109 33.759 1.00 53.10 ? 344 GLU A O 1 ATOM 2644 C CB . GLU A 1 344 ? -52.884 51.064 35.836 1.00 59.88 ? 344 GLU A CB 1 ATOM 2645 C CG . GLU A 1 344 ? -53.685 52.338 35.580 1.00 63.47 ? 344 GLU A CG 1 ATOM 2646 C CD . GLU A 1 344 ? -53.158 53.535 36.368 1.00 69.06 ? 344 GLU A CD 1 ATOM 2647 O OE1 . GLU A 1 344 ? -52.200 53.390 37.169 1.00 71.27 ? 344 GLU A OE1 1 ATOM 2648 O OE2 . GLU A 1 344 ? -53.710 54.638 36.192 1.00 73.14 ? 344 GLU A OE2 1 ATOM 2649 N N . SER A 1 345 ? -52.006 47.871 35.593 1.00 50.38 ? 345 SER A N 1 ATOM 2650 C CA . SER A 1 345 ? -50.953 46.900 35.352 1.00 48.35 ? 345 SER A CA 1 ATOM 2651 C C . SER A 1 345 ? -49.558 47.543 35.325 1.00 48.47 ? 345 SER A C 1 ATOM 2652 O O . SER A 1 345 ? -48.752 47.273 34.436 1.00 47.27 ? 345 SER A O 1 ATOM 2653 C CB . SER A 1 345 ? -51.223 46.111 34.066 1.00 47.61 ? 345 SER A CB 1 ATOM 2654 O OG . SER A 1 345 ? -52.488 45.478 34.107 1.00 47.90 ? 345 SER A OG 1 ATOM 2655 N N . LYS A 1 346 ? -49.280 48.384 36.318 1.00 50.04 ? 346 LYS A N 1 ATOM 2656 C CA . LYS A 1 346 ? -47.931 48.887 36.553 1.00 50.91 ? 346 LYS A CA 1 ATOM 2657 C C . LYS A 1 346 ? -47.041 47.733 36.997 1.00 50.10 ? 346 LYS A C 1 ATOM 2658 O O . LYS A 1 346 ? -47.408 46.970 37.869 1.00 50.90 ? 346 LYS A O 1 ATOM 2659 C CB . LYS A 1 346 ? -47.957 49.992 37.599 1.00 54.59 ? 346 LYS A CB 1 ATOM 2660 C CG . LYS A 1 346 ? -48.644 51.260 37.097 1.00 57.38 ? 346 LYS A CG 1 ATOM 2661 C CD . LYS A 1 346 ? -48.561 52.412 38.094 1.00 60.81 ? 346 LYS A CD 1 ATOM 2662 C CE . LYS A 1 346 ? -49.412 52.153 39.327 1.00 63.31 ? 346 LYS A CE 1 ATOM 2663 N NZ . LYS A 1 346 ? -49.500 53.347 40.216 1.00 66.94 ? 346 LYS A NZ 1 ATOM 2664 N N . ILE A 1 347 ? -45.879 47.602 36.375 1.00 49.60 ? 347 ILE A N 1 ATOM 2665 C CA . ILE A 1 347 ? -45.064 46.397 36.475 1.00 49.01 ? 347 ILE A CA 1 ATOM 2666 C C . ILE A 1 347 ? -43.799 46.661 37.283 1.00 50.08 ? 347 ILE A C 1 ATOM 2667 O O . ILE A 1 347 ? -43.054 47.594 37.009 1.00 50.37 ? 347 ILE A O 1 ATOM 2668 C CB . ILE A 1 347 ? -44.701 45.918 35.051 1.00 48.16 ? 347 ILE A CB 1 ATOM 2669 C CG1 . ILE A 1 347 ? -45.954 45.414 34.347 1.00 47.09 ? 347 ILE A CG1 1 ATOM 2670 C CG2 . ILE A 1 347 ? -43.624 44.838 35.053 1.00 48.34 ? 347 ILE A CG2 1 ATOM 2671 C CD1 . ILE A 1 347 ? -46.656 44.280 35.056 1.00 46.96 ? 347 ILE A CD1 1 ATOM 2672 N N . SER A 1 348 ? -43.554 45.823 38.278 1.00 50.79 ? 348 SER A N 1 ATOM 2673 C CA . SER A 1 348 ? -42.395 45.992 39.134 1.00 51.56 ? 348 SER A CA 1 ATOM 2674 C C . SER A 1 348 ? -41.101 45.589 38.428 1.00 52.50 ? 348 SER A C 1 ATOM 2675 O O . SER A 1 348 ? -41.120 45.042 37.317 1.00 52.65 ? 348 SER A O 1 ATOM 2676 C CB . SER A 1 348 ? -42.564 45.130 40.371 1.00 52.08 ? 348 SER A CB 1 ATOM 2677 O OG . SER A 1 348 ? -42.626 43.767 40.006 1.00 50.97 ? 348 SER A OG 1 ATOM 2678 N N . ARG A 1 349 ? -39.981 45.862 39.093 1.00 54.61 ? 349 ARG A N 1 ATOM 2679 C CA . ARG A 1 349 ? -38.666 45.365 38.693 1.00 54.17 ? 349 ARG A CA 1 ATOM 2680 C C . ARG A 1 349 ? -38.739 43.869 38.389 1.00 52.77 ? 349 ARG A C 1 ATOM 2681 O O . ARG A 1 349 ? -38.432 43.437 37.285 1.00 50.41 ? 349 ARG A O 1 ATOM 2682 C CB . ARG A 1 349 ? -37.650 45.616 39.822 1.00 56.44 ? 349 ARG A CB 1 ATOM 2683 N N . GLU A 1 350 ? -39.175 43.093 39.379 1.00 54.18 ? 350 GLU A N 1 ATOM 2684 C CA . GLU A 1 350 ? -39.257 41.634 39.257 1.00 53.93 ? 350 GLU A CA 1 ATOM 2685 C C . GLU A 1 350 ? -40.114 41.192 38.054 1.00 51.95 ? 350 GLU A C 1 ATOM 2686 O O . GLU A 1 350 ? -39.638 40.447 37.197 1.00 52.38 ? 350 GLU A O 1 ATOM 2687 C CB . GLU A 1 350 ? -39.747 40.996 40.578 1.00 53.78 ? 350 GLU A CB 1 ATOM 2688 N N . ASP A 1 351 ? -41.354 41.670 37.966 1.00 51.80 ? 351 ASP A N 1 ATOM 2689 C CA . ASP A 1 351 ? -42.266 41.255 36.877 1.00 50.25 ? 351 ASP A CA 1 ATOM 2690 C C . ASP A 1 351 ? -41.783 41.659 35.480 1.00 48.45 ? 351 ASP A C 1 ATOM 2691 O O . ASP A 1 351 ? -42.153 41.035 34.483 1.00 47.75 ? 351 ASP A O 1 ATOM 2692 C CB . ASP A 1 351 ? -43.677 41.827 37.087 1.00 50.90 ? 351 ASP A CB 1 ATOM 2693 C CG . ASP A 1 351 ? -44.427 41.172 38.234 1.00 51.64 ? 351 ASP A CG 1 ATOM 2694 O OD1 . ASP A 1 351 ? -44.225 39.973 38.488 1.00 52.21 ? 351 ASP A OD1 1 ATOM 2695 O OD2 . ASP A 1 351 ? -45.247 41.869 38.872 1.00 53.02 ? 351 ASP A OD2 1 ATOM 2696 N N . PHE A 1 352 ? -40.987 42.719 35.410 1.00 48.92 ? 352 PHE A N 1 ATOM 2697 C CA . PHE A 1 352 ? -40.379 43.131 34.159 1.00 48.46 ? 352 PHE A CA 1 ATOM 2698 C C . PHE A 1 352 ? -39.371 42.103 33.672 1.00 49.40 ? 352 PHE A C 1 ATOM 2699 O O . PHE A 1 352 ? -39.376 41.717 32.500 1.00 47.21 ? 352 PHE A O 1 ATOM 2700 C CB . PHE A 1 352 ? -39.671 44.466 34.338 1.00 49.94 ? 352 PHE A CB 1 ATOM 2701 C CG . PHE A 1 352 ? -39.101 45.010 33.068 1.00 49.82 ? 352 PHE A CG 1 ATOM 2702 C CD1 . PHE A 1 352 ? -39.922 45.641 32.146 1.00 49.13 ? 352 PHE A CD1 1 ATOM 2703 C CD2 . PHE A 1 352 ? -37.755 44.872 32.781 1.00 50.17 ? 352 PHE A CD2 1 ATOM 2704 C CE1 . PHE A 1 352 ? -39.410 46.132 30.962 1.00 48.50 ? 352 PHE A CE1 1 ATOM 2705 C CE2 . PHE A 1 352 ? -37.236 45.365 31.601 1.00 49.90 ? 352 PHE A CE2 1 ATOM 2706 C CZ . PHE A 1 352 ? -38.064 45.997 30.690 1.00 49.18 ? 352 PHE A CZ 1 ATOM 2707 N N . MET A 1 353 ? -38.498 41.671 34.581 1.00 52.22 ? 353 MET A N 1 ATOM 2708 C CA . MET A 1 353 ? -37.458 40.709 34.238 1.00 52.90 ? 353 MET A CA 1 ATOM 2709 C C . MET A 1 353 ? -38.095 39.399 33.825 1.00 50.57 ? 353 MET A C 1 ATOM 2710 O O . MET A 1 353 ? -37.676 38.795 32.842 1.00 49.67 ? 353 MET A O 1 ATOM 2711 C CB . MET A 1 353 ? -36.505 40.488 35.408 1.00 56.64 ? 353 MET A CB 1 ATOM 2712 C CG . MET A 1 353 ? -35.682 41.715 35.792 1.00 60.75 ? 353 MET A CG 1 ATOM 2713 S SD . MET A 1 353 ? -34.435 41.416 37.083 1.00 67.06 ? 353 MET A SD 1 ATOM 2714 C CE . MET A 1 353 ? -35.228 40.216 38.162 1.00 67.06 ? 353 MET A CE 1 ATOM 2715 N N . SER A 1 354 ? -39.112 38.974 34.574 1.00 49.99 ? 354 SER A N 1 ATOM 2716 C CA . SER A 1 354 ? -39.898 37.779 34.230 1.00 50.15 ? 354 SER A CA 1 ATOM 2717 C C . SER A 1 354 ? -40.491 37.856 32.823 1.00 48.30 ? 354 SER A C 1 ATOM 2718 O O . SER A 1 354 ? -40.444 36.888 32.071 1.00 47.84 ? 354 SER A O 1 ATOM 2719 C CB . SER A 1 354 ? -41.054 37.591 35.216 1.00 50.17 ? 354 SER A CB 1 ATOM 2720 O OG . SER A 1 354 ? -40.590 37.268 36.504 1.00 51.53 ? 354 SER A OG 1 ATOM 2721 N N . GLY A 1 355 ? -41.070 39.008 32.497 1.00 47.33 ? 355 GLY A N 1 ATOM 2722 C CA . GLY A 1 355 ? -41.733 39.212 31.223 1.00 45.67 ? 355 GLY A CA 1 ATOM 2723 C C . GLY A 1 355 ? -40.751 39.197 30.080 1.00 45.41 ? 355 GLY A C 1 ATOM 2724 O O . GLY A 1 355 ? -41.079 38.746 28.984 1.00 44.75 ? 355 GLY A O 1 ATOM 2725 N N . VAL A 1 356 ? -39.537 39.680 30.331 1.00 46.25 ? 356 VAL A N 1 ATOM 2726 C CA . VAL A 1 356 ? -38.495 39.660 29.312 1.00 45.49 ? 356 VAL A CA 1 ATOM 2727 C C . VAL A 1 356 ? -38.080 38.227 28.985 1.00 45.65 ? 356 VAL A C 1 ATOM 2728 O O . VAL A 1 356 ? -38.014 37.859 27.813 1.00 44.39 ? 356 VAL A O 1 ATOM 2729 C CB . VAL A 1 356 ? -37.264 40.462 29.744 1.00 47.33 ? 356 VAL A CB 1 ATOM 2730 C CG1 . VAL A 1 356 ? -36.161 40.345 28.701 1.00 47.55 ? 356 VAL A CG1 1 ATOM 2731 C CG2 . VAL A 1 356 ? -37.631 41.922 29.980 1.00 48.69 ? 356 VAL A CG2 1 ATOM 2732 N N . LYS A 1 357 ? -37.805 37.432 30.021 1.00 47.39 ? 357 LYS A N 1 ATOM 2733 C CA . LYS A 1 357 ? -37.525 35.993 29.868 1.00 48.07 ? 357 LYS A CA 1 ATOM 2734 C C . LYS A 1 357 ? -38.623 35.314 29.055 1.00 47.25 ? 357 LYS A C 1 ATOM 2735 O O . LYS A 1 357 ? -38.341 34.530 28.141 1.00 49.22 ? 357 LYS A O 1 ATOM 2736 C CB . LYS A 1 357 ? -37.385 35.303 31.239 1.00 50.18 ? 357 LYS A CB 1 ATOM 2737 C CG . LYS A 1 357 ? -35.960 35.278 31.787 1.00 53.10 ? 357 LYS A CG 1 ATOM 2738 C CD . LYS A 1 357 ? -35.888 35.391 33.316 1.00 54.85 ? 357 LYS A CD 1 ATOM 2739 N N . LEU A 1 358 ? -39.873 35.626 29.385 1.00 45.44 ? 358 LEU A N 1 ATOM 2740 C CA . LEU A 1 358 ? -41.006 35.043 28.697 1.00 43.14 ? 358 LEU A CA 1 ATOM 2741 C C . LEU A 1 358 ? -41.070 35.507 27.249 1.00 43.10 ? 358 LEU A C 1 ATOM 2742 O O . LEU A 1 358 ? -41.449 34.738 26.378 1.00 45.21 ? 358 LEU A O 1 ATOM 2743 C CB . LEU A 1 358 ? -42.317 35.381 29.416 1.00 42.68 ? 358 LEU A CB 1 ATOM 2744 C CG . LEU A 1 358 ? -42.601 34.781 30.804 1.00 43.07 ? 358 LEU A CG 1 ATOM 2745 C CD1 . LEU A 1 358 ? -43.839 35.438 31.389 1.00 43.68 ? 358 LEU A CD1 1 ATOM 2746 C CD2 . LEU A 1 358 ? -42.781 33.270 30.802 1.00 42.11 ? 358 LEU A CD2 1 ATOM 2747 N N . SER A 1 359 ? -40.709 36.757 26.985 1.00 44.38 ? 359 SER A N 1 ATOM 2748 C CA . SER A 1 359 ? -40.822 37.320 25.628 1.00 44.50 ? 359 SER A CA 1 ATOM 2749 C C . SER A 1 359 ? -39.772 36.803 24.655 1.00 45.28 ? 359 SER A C 1 ATOM 2750 O O . SER A 1 359 ? -40.015 36.748 23.452 1.00 47.22 ? 359 SER A O 1 ATOM 2751 C CB . SER A 1 359 ? -40.755 38.845 25.670 1.00 44.62 ? 359 SER A CB 1 ATOM 2752 O OG . SER A 1 359 ? -41.817 39.370 26.449 1.00 44.87 ? 359 SER A OG 1 ATOM 2753 N N . VAL A 1 360 ? -38.615 36.419 25.181 1.00 48.10 ? 360 VAL A N 1 ATOM 2754 C CA . VAL A 1 360 ? -37.468 36.028 24.376 1.00 48.70 ? 360 VAL A CA 1 ATOM 2755 C C . VAL A 1 360 ? -36.940 34.689 24.898 1.00 50.06 ? 360 VAL A C 1 ATOM 2756 O O . VAL A 1 360 ? -35.894 34.635 25.528 1.00 51.45 ? 360 VAL A O 1 ATOM 2757 C CB . VAL A 1 360 ? -36.363 37.105 24.462 1.00 50.54 ? 360 VAL A CB 1 ATOM 2758 C CG1 . VAL A 1 360 ? -35.403 36.972 23.299 1.00 52.54 ? 360 VAL A CG1 1 ATOM 2759 C CG2 . VAL A 1 360 ? -36.958 38.499 24.445 1.00 50.87 ? 360 VAL A CG2 1 ATOM 2760 N N . PRO A 1 361 ? -37.680 33.597 24.652 1.00 51.98 ? 361 PRO A N 1 ATOM 2761 C CA . PRO A 1 361 ? -37.365 32.302 25.287 1.00 53.31 ? 361 PRO A CA 1 ATOM 2762 C C . PRO A 1 361 ? -36.030 31.639 24.914 1.00 54.66 ? 361 PRO A C 1 ATOM 2763 O O . PRO A 1 361 ? -35.538 30.819 25.677 1.00 54.14 ? 361 PRO A O 1 ATOM 2764 C CB . PRO A 1 361 ? -38.544 31.409 24.873 1.00 52.82 ? 361 PRO A CB 1 ATOM 2765 C CG . PRO A 1 361 ? -39.191 32.097 23.717 1.00 50.45 ? 361 PRO A CG 1 ATOM 2766 C CD . PRO A 1 361 ? -38.954 33.557 23.912 1.00 50.24 ? 361 PRO A CD 1 ATOM 2767 N N . HIS A 1 362 ? -35.461 31.973 23.760 1.00 59.43 ? 362 HIS A N 1 ATOM 2768 C CA . HIS A 1 362 ? -34.166 31.412 23.338 1.00 64.48 ? 362 HIS A CA 1 ATOM 2769 C C . HIS A 1 362 ? -32.998 32.264 23.820 1.00 63.73 ? 362 HIS A C 1 ATOM 2770 O O . HIS A 1 362 ? -31.846 31.915 23.589 1.00 64.62 ? 362 HIS A O 1 ATOM 2771 C CB . HIS A 1 362 ? -34.056 31.315 21.808 1.00 68.55 ? 362 HIS A CB 1 ATOM 2772 C CG . HIS A 1 362 ? -34.789 30.157 21.202 1.00 74.44 ? 362 HIS A CG 1 ATOM 2773 N ND1 . HIS A 1 362 ? -34.167 28.962 20.904 1.00 79.56 ? 362 HIS A ND1 1 ATOM 2774 C CD2 . HIS A 1 362 ? -36.074 30.025 20.793 1.00 76.96 ? 362 HIS A CD2 1 ATOM 2775 C CE1 . HIS A 1 362 ? -35.040 28.138 20.353 1.00 80.37 ? 362 HIS A CE1 1 ATOM 2776 N NE2 . HIS A 1 362 ? -36.204 28.759 20.274 1.00 80.85 ? 362 HIS A NE2 1 ATOM 2777 N N . ALA A 1 363 ? -33.280 33.392 24.463 1.00 61.43 ? 363 ALA A N 1 ATOM 2778 C CA . ALA A 1 363 ? -32.217 34.313 24.826 1.00 60.65 ? 363 ALA A CA 1 ATOM 2779 C C . ALA A 1 363 ? -31.451 33.838 26.052 1.00 60.07 ? 363 ALA A C 1 ATOM 2780 O O . ALA A 1 363 ? -32.045 33.603 27.108 1.00 63.75 ? 363 ALA A O 1 ATOM 2781 C CB . ALA A 1 363 ? -32.776 35.706 25.063 1.00 60.79 ? 363 ALA A CB 1 ATOM 2782 N N . ASN A 1 364 ? -30.131 33.705 25.902 1.00 57.02 ? 364 ASN A N 1 ATOM 2783 C CA . ASN A 1 364 ? -29.236 33.461 27.033 1.00 55.04 ? 364 ASN A CA 1 ATOM 2784 C C . ASN A 1 364 ? -29.155 34.700 27.925 1.00 55.76 ? 364 ASN A C 1 ATOM 2785 O O . ASN A 1 364 ? -29.620 35.772 27.551 1.00 55.05 ? 364 ASN A O 1 ATOM 2786 C CB . ASN A 1 364 ? -27.839 33.047 26.553 1.00 54.05 ? 364 ASN A CB 1 ATOM 2787 C CG . ASN A 1 364 ? -27.179 34.084 25.655 1.00 53.22 ? 364 ASN A CG 1 ATOM 2788 O OD1 . ASN A 1 364 ? -27.728 35.141 25.387 1.00 52.76 ? 364 ASN A OD1 1 ATOM 2789 N ND2 . ASN A 1 364 ? -25.995 33.772 25.182 1.00 53.97 ? 364 ASN A ND2 1 ATOM 2790 N N . ASP A 1 365 ? -28.556 34.544 29.099 1.00 57.33 ? 365 ASP A N 1 ATOM 2791 C CA . ASP A 1 365 ? -28.423 35.628 30.067 1.00 57.56 ? 365 ASP A CA 1 ATOM 2792 C C . ASP A 1 365 ? -28.027 36.943 29.387 1.00 55.41 ? 365 ASP A C 1 ATOM 2793 O O . ASP A 1 365 ? -28.667 37.971 29.590 1.00 54.88 ? 365 ASP A O 1 ATOM 2794 C CB . ASP A 1 365 ? -27.398 35.222 31.131 1.00 61.93 ? 365 ASP A CB 1 ATOM 2795 C CG . ASP A 1 365 ? -27.136 36.313 32.160 1.00 66.22 ? 365 ASP A CG 1 ATOM 2796 O OD1 . ASP A 1 365 ? -28.097 37.011 32.567 1.00 68.08 ? 365 ASP A OD1 1 ATOM 2797 O OD2 . ASP A 1 365 ? -25.959 36.459 32.576 1.00 68.09 ? 365 ASP A OD2 1 ATOM 2798 N N . LEU A 1 366 ? -26.994 36.902 28.554 1.00 54.75 ? 366 LEU A N 1 ATOM 2799 C CA . LEU A 1 366 ? -26.516 38.100 27.860 1.00 53.18 ? 366 LEU A CA 1 ATOM 2800 C C . LEU A 1 366 ? -27.568 38.683 26.918 1.00 50.74 ? 366 LEU A C 1 ATOM 2801 O O . LEU A 1 366 ? -27.726 39.892 26.829 1.00 51.34 ? 366 LEU A O 1 ATOM 2802 C CB . LEU A 1 366 ? -25.247 37.789 27.077 1.00 53.51 ? 366 LEU A CB 1 ATOM 2803 C CG . LEU A 1 366 ? -24.611 38.958 26.327 1.00 53.87 ? 366 LEU A CG 1 ATOM 2804 C CD1 . LEU A 1 366 ? -23.976 39.939 27.296 1.00 55.60 ? 366 LEU A CD1 1 ATOM 2805 C CD2 . LEU A 1 366 ? -23.571 38.449 25.344 1.00 55.30 ? 366 LEU A CD2 1 ATOM 2806 N N . GLY A 1 367 ? -28.278 37.824 26.206 1.00 49.07 ? 367 GLY A N 1 ATOM 2807 C CA . GLY A 1 367 ? -29.386 38.274 25.361 1.00 47.41 ? 367 GLY A CA 1 ATOM 2808 C C . GLY A 1 367 ? -30.450 39.038 26.130 1.00 46.56 ? 367 GLY A C 1 ATOM 2809 O O . GLY A 1 367 ? -31.034 39.990 25.617 1.00 45.01 ? 367 GLY A O 1 ATOM 2810 N N . LEU A 1 368 ? -30.688 38.628 27.372 1.00 47.16 ? 368 LEU A N 1 ATOM 2811 C CA . LEU A 1 368 ? -31.673 39.284 28.212 1.00 46.72 ? 368 LEU A CA 1 ATOM 2812 C C . LEU A 1 368 ? -31.177 40.641 28.657 1.00 47.83 ? 368 LEU A C 1 ATOM 2813 O O . LEU A 1 368 ? -31.943 41.603 28.682 1.00 47.51 ? 368 LEU A O 1 ATOM 2814 C CB . LEU A 1 368 ? -32.001 38.433 29.432 1.00 47.21 ? 368 LEU A CB 1 ATOM 2815 C CG . LEU A 1 368 ? -32.557 37.040 29.136 1.00 46.31 ? 368 LEU A CG 1 ATOM 2816 C CD1 . LEU A 1 368 ? -32.686 36.274 30.444 1.00 47.15 ? 368 LEU A CD1 1 ATOM 2817 C CD2 . LEU A 1 368 ? -33.890 37.117 28.405 1.00 44.28 ? 368 LEU A CD2 1 ATOM 2818 N N . ASP A 1 369 ? -29.901 40.728 29.010 1.00 48.61 ? 369 ASP A N 1 ATOM 2819 C CA . ASP A 1 369 ? -29.311 42.033 29.315 1.00 49.87 ? 369 ASP A CA 1 ATOM 2820 C C . ASP A 1 369 ? -29.428 42.995 28.134 1.00 48.75 ? 369 ASP A C 1 ATOM 2821 O O . ASP A 1 369 ? -29.700 44.181 28.317 1.00 49.26 ? 369 ASP A O 1 ATOM 2822 C CB . ASP A 1 369 ? -27.844 41.890 29.706 1.00 51.68 ? 369 ASP A CB 1 ATOM 2823 C CG . ASP A 1 369 ? -27.663 41.368 31.109 1.00 52.84 ? 369 ASP A CG 1 ATOM 2824 O OD1 . ASP A 1 369 ? -28.661 41.023 31.771 1.00 51.58 ? 369 ASP A OD1 1 ATOM 2825 O OD2 . ASP A 1 369 ? -26.502 41.309 31.550 1.00 56.09 ? 369 ASP A OD2 1 ATOM 2826 N N . ALA A 1 370 ? -29.229 42.475 26.929 1.00 47.21 ? 370 ALA A N 1 ATOM 2827 C CA . ALA A 1 370 ? -29.246 43.299 25.731 1.00 46.76 ? 370 ALA A CA 1 ATOM 2828 C C . ALA A 1 370 ? -30.628 43.889 25.469 1.00 45.33 ? 370 ALA A C 1 ATOM 2829 O O . ALA A 1 370 ? -30.747 45.074 25.170 1.00 46.32 ? 370 ALA A O 1 ATOM 2830 C CB . ALA A 1 370 ? -28.777 42.495 24.534 1.00 46.43 ? 370 ALA A CB 1 ATOM 2831 N N . VAL A 1 371 ? -31.658 43.053 25.572 1.00 43.60 ? 371 VAL A N 1 ATOM 2832 C CA . VAL A 1 371 ? -33.041 43.497 25.435 1.00 41.76 ? 371 VAL A CA 1 ATOM 2833 C C . VAL A 1 371 ? -33.346 44.523 26.524 1.00 42.38 ? 371 VAL A C 1 ATOM 2834 O O . VAL A 1 371 ? -33.893 45.593 26.254 1.00 43.35 ? 371 VAL A O 1 ATOM 2835 C CB . VAL A 1 371 ? -34.029 42.319 25.585 1.00 41.45 ? 371 VAL A CB 1 ATOM 2836 C CG1 . VAL A 1 371 ? -35.474 42.811 25.643 1.00 40.98 ? 371 VAL A CG1 1 ATOM 2837 C CG2 . VAL A 1 371 ? -33.863 41.308 24.456 1.00 40.86 ? 371 VAL A CG2 1 ATOM 2838 N N . THR A 1 372 ? -32.986 44.194 27.757 1.00 42.52 ? 372 THR A N 1 ATOM 2839 C CA . THR A 1 372 ? -33.231 45.076 28.887 1.00 42.88 ? 372 THR A CA 1 ATOM 2840 C C . THR A 1 372 ? -32.583 46.442 28.689 1.00 43.94 ? 372 THR A C 1 ATOM 2841 O O . THR A 1 372 ? -33.204 47.468 28.952 1.00 45.21 ? 372 THR A O 1 ATOM 2842 C CB . THR A 1 372 ? -32.708 44.465 30.196 1.00 44.16 ? 372 THR A CB 1 ATOM 2843 O OG1 . THR A 1 372 ? -33.238 43.147 30.359 1.00 42.96 ? 372 THR A OG1 1 ATOM 2844 C CG2 . THR A 1 372 ? -33.115 45.315 31.396 1.00 45.35 ? 372 THR A CG2 1 ATOM 2845 N N . LEU A 1 373 ? -31.341 46.456 28.221 1.00 44.27 ? 373 LEU A N 1 ATOM 2846 C CA . LEU A 1 373 ? -30.642 47.709 27.940 1.00 44.89 ? 373 LEU A CA 1 ATOM 2847 C C . LEU A 1 373 ? -31.381 48.548 26.902 1.00 45.10 ? 373 LEU A C 1 ATOM 2848 O O . LEU A 1 373 ? -31.420 49.772 27.011 1.00 45.75 ? 373 LEU A O 1 ATOM 2849 C CB . LEU A 1 373 ? -29.231 47.418 27.444 1.00 45.19 ? 373 LEU A CB 1 ATOM 2850 C CG . LEU A 1 373 ? -28.335 48.623 27.196 1.00 46.48 ? 373 LEU A CG 1 ATOM 2851 C CD1 . LEU A 1 373 ? -27.888 49.223 28.510 1.00 48.52 ? 373 LEU A CD1 1 ATOM 2852 C CD2 . LEU A 1 373 ? -27.126 48.241 26.370 1.00 47.24 ? 373 LEU A CD2 1 ATOM 2853 N N . GLN A 1 374 ? -31.962 47.889 25.902 1.00 44.63 ? 374 GLN A N 1 ATOM 2854 C CA . GLN A 1 374 ? -32.646 48.584 24.815 1.00 45.91 ? 374 GLN A CA 1 ATOM 2855 C C . GLN A 1 374 ? -33.939 49.237 25.207 1.00 46.29 ? 374 GLN A C 1 ATOM 2856 O O . GLN A 1 374 ? -34.318 50.235 24.615 1.00 47.10 ? 374 GLN A O 1 ATOM 2857 C CB . GLN A 1 374 ? -32.972 47.627 23.669 1.00 45.69 ? 374 GLN A CB 1 ATOM 2858 C CG . GLN A 1 374 ? -31.775 47.284 22.820 1.00 47.33 ? 374 GLN A CG 1 ATOM 2859 C CD . GLN A 1 374 ? -31.184 48.508 22.165 1.00 48.70 ? 374 GLN A CD 1 ATOM 2860 O OE1 . GLN A 1 374 ? -31.816 49.138 21.306 1.00 49.54 ? 374 GLN A OE1 1 ATOM 2861 N NE2 . GLN A 1 374 ? -29.973 48.861 22.572 1.00 49.90 ? 374 GLN A NE2 1 ATOM 2862 N N . TYR A 1 375 ? -34.634 48.659 26.174 1.00 47.25 ? 375 TYR A N 1 ATOM 2863 C CA . TYR A 1 375 ? -36.001 49.057 26.450 1.00 47.34 ? 375 TYR A CA 1 ATOM 2864 C C . TYR A 1 375 ? -36.225 49.673 27.821 1.00 49.46 ? 375 TYR A C 1 ATOM 2865 O O . TYR A 1 375 ? -37.364 49.922 28.201 1.00 50.29 ? 375 TYR A O 1 ATOM 2866 C CB . TYR A 1 375 ? -36.892 47.847 26.258 1.00 46.37 ? 375 TYR A CB 1 ATOM 2867 C CG . TYR A 1 375 ? -37.160 47.577 24.805 1.00 45.96 ? 375 TYR A CG 1 ATOM 2868 C CD1 . TYR A 1 375 ? -38.204 48.235 24.141 1.00 44.91 ? 375 TYR A CD1 1 ATOM 2869 C CD2 . TYR A 1 375 ? -36.372 46.676 24.076 1.00 44.94 ? 375 TYR A CD2 1 ATOM 2870 C CE1 . TYR A 1 375 ? -38.461 47.994 22.804 1.00 43.66 ? 375 TYR A CE1 1 ATOM 2871 C CE2 . TYR A 1 375 ? -36.631 46.430 22.732 1.00 43.62 ? 375 TYR A CE2 1 ATOM 2872 C CZ . TYR A 1 375 ? -37.677 47.092 22.111 1.00 42.84 ? 375 TYR A CZ 1 ATOM 2873 O OH . TYR A 1 375 ? -37.946 46.869 20.795 1.00 43.27 ? 375 TYR A OH 1 ATOM 2874 N N . THR A 1 376 ? -35.145 49.952 28.542 1.00 51.31 ? 376 THR A N 1 ATOM 2875 C CA . THR A 1 376 ? -35.232 50.489 29.887 1.00 53.08 ? 376 THR A CA 1 ATOM 2876 C C . THR A 1 376 ? -34.827 51.947 29.861 1.00 56.09 ? 376 THR A C 1 ATOM 2877 O O . THR A 1 376 ? -33.770 52.283 29.343 1.00 58.36 ? 376 THR A O 1 ATOM 2878 C CB . THR A 1 376 ? -34.300 49.712 30.841 1.00 53.54 ? 376 THR A CB 1 ATOM 2879 O OG1 . THR A 1 376 ? -34.770 48.364 30.964 1.00 52.88 ? 376 THR A OG1 1 ATOM 2880 C CG2 . THR A 1 376 ? -34.247 50.342 32.218 1.00 54.19 ? 376 THR A CG2 1 ATOM 2881 N N . ASP A 1 377 ? -35.675 52.810 30.414 1.00 58.10 ? 377 ASP A N 1 ATOM 2882 C CA . ASP A 1 377 ? -35.314 54.204 30.649 1.00 60.14 ? 377 ASP A CA 1 ATOM 2883 C C . ASP A 1 377 ? -34.501 54.234 31.933 1.00 61.25 ? 377 ASP A C 1 ATOM 2884 O O . ASP A 1 377 ? -35.047 54.033 33.010 1.00 62.24 ? 377 ASP A O 1 ATOM 2885 C CB . ASP A 1 377 ? -36.581 55.055 30.787 1.00 61.22 ? 377 ASP A CB 1 ATOM 2886 C CG . ASP A 1 377 ? -36.294 56.527 31.035 1.00 63.33 ? 377 ASP A CG 1 ATOM 2887 O OD1 . ASP A 1 377 ? -35.142 56.913 31.336 1.00 63.01 ? 377 ASP A OD1 1 ATOM 2888 O OD2 . ASP A 1 377 ? -37.260 57.304 30.936 1.00 65.92 ? 377 ASP A OD2 1 ATOM 2889 N N . TRP A 1 378 ? -33.202 54.487 31.822 1.00 61.49 ? 378 TRP A N 1 ATOM 2890 C CA . TRP A 1 378 ? -32.317 54.409 32.982 1.00 62.70 ? 378 TRP A CA 1 ATOM 2891 C C . TRP A 1 378 ? -32.408 55.611 33.896 1.00 66.65 ? 378 TRP A C 1 ATOM 2892 O O . TRP A 1 378 ? -32.053 55.504 35.067 1.00 69.25 ? 378 TRP A O 1 ATOM 2893 C CB . TRP A 1 378 ? -30.883 54.155 32.536 1.00 62.34 ? 378 TRP A CB 1 ATOM 2894 C CG . TRP A 1 378 ? -30.799 52.844 31.849 1.00 60.24 ? 378 TRP A CG 1 ATOM 2895 C CD1 . TRP A 1 378 ? -30.799 52.611 30.499 1.00 58.00 ? 378 TRP A CD1 1 ATOM 2896 C CD2 . TRP A 1 378 ? -30.770 51.565 32.478 1.00 58.73 ? 378 TRP A CD2 1 ATOM 2897 N NE1 . TRP A 1 378 ? -30.747 51.262 30.253 1.00 55.84 ? 378 TRP A NE1 1 ATOM 2898 C CE2 . TRP A 1 378 ? -30.731 50.596 31.452 1.00 57.02 ? 378 TRP A CE2 1 ATOM 2899 C CE3 . TRP A 1 378 ? -30.764 51.143 33.813 1.00 59.39 ? 378 TRP A CE3 1 ATOM 2900 C CZ2 . TRP A 1 378 ? -30.688 49.224 31.721 1.00 56.81 ? 378 TRP A CZ2 1 ATOM 2901 C CZ3 . TRP A 1 378 ? -30.723 49.783 34.081 1.00 59.16 ? 378 TRP A CZ3 1 ATOM 2902 C CH2 . TRP A 1 378 ? -30.687 48.837 33.038 1.00 57.66 ? 378 TRP A CH2 1 ATOM 2903 N N . MET A 1 379 ? -32.890 56.743 33.374 1.00 70.32 ? 379 MET A N 1 ATOM 2904 C CA . MET A 1 379 ? -33.206 57.923 34.199 1.00 74.93 ? 379 MET A CA 1 ATOM 2905 C C . MET A 1 379 ? -34.240 57.584 35.273 1.00 74.41 ? 379 MET A C 1 ATOM 2906 O O . MET A 1 379 ? -34.179 58.103 36.379 1.00 75.08 ? 379 MET A O 1 ATOM 2907 C CB . MET A 1 379 ? -33.786 59.061 33.343 1.00 78.27 ? 379 MET A CB 1 ATOM 2908 C CG . MET A 1 379 ? -32.825 59.764 32.392 1.00 80.85 ? 379 MET A CG 1 ATOM 2909 S SD . MET A 1 379 ? -31.552 60.773 33.186 1.00 90.23 ? 379 MET A SD 1 ATOM 2910 C CE . MET A 1 379 ? -32.412 61.613 34.528 1.00 89.17 ? 379 MET A CE 1 ATOM 2911 N N . ASP A 1 380 ? -35.178 56.708 34.916 1.00 74.30 ? 380 ASP A N 1 ATOM 2912 C CA . ASP A 1 380 ? -36.367 56.413 35.707 1.00 75.50 ? 380 ASP A CA 1 ATOM 2913 C C . ASP A 1 380 ? -36.692 54.915 35.519 1.00 76.16 ? 380 ASP A C 1 ATOM 2914 O O . ASP A 1 380 ? -37.674 54.545 34.852 1.00 75.82 ? 380 ASP A O 1 ATOM 2915 C CB . ASP A 1 380 ? -37.502 57.320 35.198 1.00 75.03 ? 380 ASP A CB 1 ATOM 2916 C CG . ASP A 1 380 ? -38.753 57.283 36.063 1.00 73.51 ? 380 ASP A CG 1 ATOM 2917 O OD1 . ASP A 1 380 ? -38.677 56.968 37.269 1.00 73.96 ? 380 ASP A OD1 1 ATOM 2918 O OD2 . ASP A 1 380 ? -39.826 57.602 35.512 1.00 70.56 ? 380 ASP A OD2 1 ATOM 2919 N N . ASP A 1 381 ? -35.845 54.059 36.096 1.00 78.45 ? 381 ASP A N 1 ATOM 2920 C CA . ASP A 1 381 ? -35.853 52.611 35.785 1.00 77.51 ? 381 ASP A CA 1 ATOM 2921 C C . ASP A 1 381 ? -36.726 51.749 36.699 1.00 76.50 ? 381 ASP A C 1 ATOM 2922 O O . ASP A 1 381 ? -36.753 50.530 36.552 1.00 74.38 ? 381 ASP A O 1 ATOM 2923 C CB . ASP A 1 381 ? -34.416 52.044 35.737 1.00 79.54 ? 381 ASP A CB 1 ATOM 2924 C CG . ASP A 1 381 ? -33.768 51.903 37.123 1.00 83.10 ? 381 ASP A CG 1 ATOM 2925 O OD1 . ASP A 1 381 ? -33.975 52.769 38.006 1.00 83.87 ? 381 ASP A OD1 1 ATOM 2926 O OD2 . ASP A 1 381 ? -33.025 50.917 37.314 1.00 84.24 ? 381 ASP A OD2 1 ATOM 2927 N N . ASN A 1 382 ? -37.434 52.373 37.636 1.00 78.59 ? 382 ASN A N 1 ATOM 2928 C CA . ASN A 1 382 ? -38.379 51.650 38.481 1.00 76.99 ? 382 ASN A CA 1 ATOM 2929 C C . ASN A 1 382 ? -39.805 52.193 38.399 1.00 72.48 ? 382 ASN A C 1 ATOM 2930 O O . ASN A 1 382 ? -40.639 51.910 39.261 1.00 72.39 ? 382 ASN A O 1 ATOM 2931 C CB . ASN A 1 382 ? -37.898 51.653 39.928 1.00 80.25 ? 382 ASN A CB 1 ATOM 2932 C CG . ASN A 1 382 ? -38.448 50.487 40.716 1.00 80.86 ? 382 ASN A CG 1 ATOM 2933 O OD1 . ASN A 1 382 ? -38.663 49.389 40.175 1.00 76.18 ? 382 ASN A OD1 1 ATOM 2934 N ND2 . ASN A 1 382 ? -38.690 50.717 42.001 1.00 83.01 ? 382 ASN A ND2 1 ATOM 2935 N N . ASN A 1 383 ? -40.074 52.966 37.352 1.00 67.24 ? 383 ASN A N 1 ATOM 2936 C CA . ASN A 1 383 ? -41.417 53.410 37.044 1.00 63.58 ? 383 ASN A CA 1 ATOM 2937 C C . ASN A 1 383 ? -42.209 52.245 36.440 1.00 59.39 ? 383 ASN A C 1 ATOM 2938 O O . ASN A 1 383 ? -41.801 51.644 35.443 1.00 57.32 ? 383 ASN A O 1 ATOM 2939 C CB . ASN A 1 383 ? -41.358 54.610 36.098 1.00 63.47 ? 383 ASN A CB 1 ATOM 2940 C CG . ASN A 1 383 ? -42.711 54.988 35.540 1.00 63.51 ? 383 ASN A CG 1 ATOM 2941 O OD1 . ASN A 1 383 ? -43.475 54.132 35.104 1.00 64.24 ? 383 ASN A OD1 1 ATOM 2942 N ND2 . ASN A 1 383 ? -42.998 56.278 35.511 1.00 65.16 ? 383 ASN A ND2 1 ATOM 2943 N N . GLY A 1 384 ? -43.347 51.939 37.052 1.00 57.08 ? 384 GLY A N 1 ATOM 2944 C CA . GLY A 1 384 ? -44.181 50.827 36.624 1.00 53.94 ? 384 GLY A CA 1 ATOM 2945 C C . GLY A 1 384 ? -44.847 51.009 35.280 1.00 50.94 ? 384 GLY A C 1 ATOM 2946 O O . GLY A 1 384 ? -45.093 50.032 34.576 1.00 49.70 ? 384 GLY A O 1 ATOM 2947 N N . ILE A 1 385 ? -45.146 52.251 34.918 1.00 50.97 ? 385 ILE A N 1 ATOM 2948 C CA . ILE A 1 385 ? -45.774 52.537 33.629 1.00 50.09 ? 385 ILE A CA 1 ATOM 2949 C C . ILE A 1 385 ? -44.783 52.335 32.496 1.00 49.32 ? 385 ILE A C 1 ATOM 2950 O O . ILE A 1 385 ? -45.099 51.694 31.498 1.00 49.17 ? 385 ILE A O 1 ATOM 2951 C CB . ILE A 1 385 ? -46.386 53.953 33.582 1.00 51.00 ? 385 ILE A CB 1 ATOM 2952 C CG1 . ILE A 1 385 ? -47.548 54.031 34.587 1.00 52.30 ? 385 ILE A CG1 1 ATOM 2953 C CG2 . ILE A 1 385 ? -46.862 54.287 32.172 1.00 49.51 ? 385 ILE A CG2 1 ATOM 2954 C CD1 . ILE A 1 385 ? -48.307 55.343 34.610 1.00 53.37 ? 385 ILE A CD1 1 ATOM 2955 N N . LYS A 1 386 ? -43.581 52.867 32.658 1.00 50.21 ? 386 LYS A N 1 ATOM 2956 C CA . LYS A 1 386 ? -42.528 52.673 31.668 1.00 49.22 ? 386 LYS A CA 1 ATOM 2957 C C . LYS A 1 386 ? -42.152 51.201 31.554 1.00 47.18 ? 386 LYS A C 1 ATOM 2958 O O . LYS A 1 386 ? -41.987 50.681 30.450 1.00 47.21 ? 386 LYS A O 1 ATOM 2959 C CB . LYS A 1 386 ? -41.309 53.524 32.009 1.00 50.98 ? 386 LYS A CB 1 ATOM 2960 C CG . LYS A 1 386 ? -41.574 55.002 31.836 1.00 52.80 ? 386 LYS A CG 1 ATOM 2961 C CD . LYS A 1 386 ? -40.386 55.838 32.253 1.00 56.32 ? 386 LYS A CD 1 ATOM 2962 C CE . LYS A 1 386 ? -40.757 57.312 32.289 1.00 58.76 ? 386 LYS A CE 1 ATOM 2963 N NZ . LYS A 1 386 ? -39.602 58.182 32.636 1.00 61.56 ? 386 LYS A NZ 1 ATOM 2964 N N . ASN A 1 387 ? -42.036 50.529 32.689 1.00 46.40 ? 387 ASN A N 1 ATOM 2965 C CA . ASN A 1 387 ? -41.854 49.085 32.693 1.00 45.71 ? 387 ASN A CA 1 ATOM 2966 C C . ASN A 1 387 ? -42.948 48.341 31.948 1.00 43.88 ? 387 ASN A C 1 ATOM 2967 O O . ASN A 1 387 ? -42.682 47.382 31.222 1.00 42.04 ? 387 ASN A O 1 ATOM 2968 C CB . ASN A 1 387 ? -41.816 48.564 34.122 1.00 47.66 ? 387 ASN A CB 1 ATOM 2969 C CG . ASN A 1 387 ? -40.496 48.819 34.787 1.00 50.18 ? 387 ASN A CG 1 ATOM 2970 O OD1 . ASN A 1 387 ? -39.483 49.001 34.116 1.00 52.82 ? 387 ASN A OD1 1 ATOM 2971 N ND2 . ASN A 1 387 ? -40.491 48.831 36.108 1.00 51.92 ? 387 ASN A ND2 1 ATOM 2972 N N . ARG A 1 388 ? -44.187 48.761 32.157 1.00 43.88 ? 388 ARG A N 1 ATOM 2973 C CA . ARG A 1 388 ? -45.304 48.107 31.505 1.00 42.48 ? 388 ARG A CA 1 ATOM 2974 C C . ARG A 1 388 ? -45.218 48.382 30.020 1.00 41.21 ? 388 ARG A C 1 ATOM 2975 O O . ARG A 1 388 ? -45.232 47.450 29.209 1.00 40.07 ? 388 ARG A O 1 ATOM 2976 C CB . ARG A 1 388 ? -46.636 48.614 32.056 1.00 43.09 ? 388 ARG A CB 1 ATOM 2977 C CG . ARG A 1 388 ? -47.845 47.880 31.488 1.00 41.61 ? 388 ARG A CG 1 ATOM 2978 C CD . ARG A 1 388 ? -49.102 48.701 31.669 1.00 42.12 ? 388 ARG A CD 1 ATOM 2979 N NE . ARG A 1 388 ? -48.989 49.978 30.969 1.00 42.63 ? 388 ARG A NE 1 ATOM 2980 C CZ . ARG A 1 388 ? -49.546 51.122 31.364 1.00 42.97 ? 388 ARG A CZ 1 ATOM 2981 N NH1 . ARG A 1 388 ? -50.277 51.189 32.475 1.00 43.79 ? 388 ARG A NH1 1 ATOM 2982 N NH2 . ARG A 1 388 ? -49.356 52.214 30.642 1.00 42.40 ? 388 ARG A NH2 1 ATOM 2983 N N . ASP A 1 389 ? -45.113 49.662 29.668 1.00 41.55 ? 389 ASP A N 1 ATOM 2984 C CA . ASP A 1 389 ? -45.088 50.064 28.265 1.00 41.29 ? 389 ASP A CA 1 ATOM 2985 C C . ASP A 1 389 ? -43.877 49.499 27.527 1.00 41.69 ? 389 ASP A C 1 ATOM 2986 O O . ASP A 1 389 ? -43.972 49.190 26.333 1.00 40.37 ? 389 ASP A O 1 ATOM 2987 C CB . ASP A 1 389 ? -45.135 51.585 28.124 1.00 42.15 ? 389 ASP A CB 1 ATOM 2988 C CG . ASP A 1 389 ? -46.494 52.173 28.490 1.00 42.72 ? 389 ASP A CG 1 ATOM 2989 O OD1 . ASP A 1 389 ? -47.507 51.433 28.434 1.00 41.06 ? 389 ASP A OD1 1 ATOM 2990 O OD2 . ASP A 1 389 ? -46.542 53.383 28.830 1.00 43.76 ? 389 ASP A OD2 1 ATOM 2991 N N . GLY A 1 390 ? -42.756 49.360 28.237 1.00 43.47 ? 390 GLY A N 1 ATOM 2992 C CA . GLY A 1 390 ? -41.548 48.765 27.673 1.00 44.05 ? 390 GLY A CA 1 ATOM 2993 C C . GLY A 1 390 ? -41.740 47.315 27.265 1.00 44.04 ? 390 GLY A C 1 ATOM 2994 O O . GLY A 1 390 ? -41.341 46.918 26.179 1.00 44.44 ? 390 GLY A O 1 ATOM 2995 N N . LEU A 1 391 ? -42.346 46.518 28.140 1.00 45.07 ? 391 LEU A N 1 ATOM 2996 C CA . LEU A 1 391 ? -42.662 45.129 27.810 1.00 44.86 ? 391 LEU A CA 1 ATOM 2997 C C . LEU A 1 391 ? -43.623 45.037 26.633 1.00 43.28 ? 391 LEU A C 1 ATOM 2998 O O . LEU A 1 391 ? -43.470 44.193 25.759 1.00 42.38 ? 391 LEU A O 1 ATOM 2999 C CB . LEU A 1 391 ? -43.263 44.399 29.011 1.00 46.09 ? 391 LEU A CB 1 ATOM 3000 C CG . LEU A 1 391 ? -42.282 43.742 29.973 1.00 47.94 ? 391 LEU A CG 1 ATOM 3001 C CD1 . LEU A 1 391 ? -42.996 43.219 31.211 1.00 48.20 ? 391 LEU A CD1 1 ATOM 3002 C CD2 . LEU A 1 391 ? -41.560 42.609 29.259 1.00 49.11 ? 391 LEU A CD2 1 ATOM 3003 N N . ASP A 1 392 ? -44.625 45.895 26.621 1.00 44.02 ? 392 ASP A N 1 ATOM 3004 C CA . ASP A 1 392 ? -45.540 45.928 25.508 1.00 45.04 ? 392 ASP A CA 1 ATOM 3005 C C . ASP A 1 392 ? -44.731 46.065 24.217 1.00 42.88 ? 392 ASP A C 1 ATOM 3006 O O . ASP A 1 392 ? -44.871 45.261 23.297 1.00 43.61 ? 392 ASP A O 1 ATOM 3007 C CB . ASP A 1 392 ? -46.515 47.092 25.674 1.00 49.99 ? 392 ASP A CB 1 ATOM 3008 C CG . ASP A 1 392 ? -47.748 46.952 24.808 1.00 52.96 ? 392 ASP A CG 1 ATOM 3009 O OD1 . ASP A 1 392 ? -47.638 46.726 23.577 1.00 54.81 ? 392 ASP A OD1 1 ATOM 3010 O OD2 . ASP A 1 392 ? -48.842 47.082 25.376 1.00 56.81 ? 392 ASP A OD2 1 ATOM 3011 N N . ASP A 1 393 ? -43.864 47.066 24.168 1.00 41.21 ? 393 ASP A N 1 ATOM 3012 C CA . ASP A 1 393 ? -43.063 47.330 22.984 1.00 40.62 ? 393 ASP A CA 1 ATOM 3013 C C . ASP A 1 393 ? -42.149 46.161 22.644 1.00 39.20 ? 393 ASP A C 1 ATOM 3014 O O . ASP A 1 393 ? -41.980 45.819 21.482 1.00 37.07 ? 393 ASP A O 1 ATOM 3015 C CB . ASP A 1 393 ? -42.222 48.595 23.180 1.00 42.98 ? 393 ASP A CB 1 ATOM 3016 C CG . ASP A 1 393 ? -43.067 49.858 23.246 1.00 44.89 ? 393 ASP A CG 1 ATOM 3017 O OD1 . ASP A 1 393 ? -44.212 49.818 22.779 1.00 47.39 ? 393 ASP A OD1 1 ATOM 3018 O OD2 . ASP A 1 393 ? -42.597 50.892 23.761 1.00 46.73 ? 393 ASP A OD2 1 ATOM 3019 N N . ILE A 1 394 ? -41.550 45.554 23.661 1.00 39.30 ? 394 ILE A N 1 ATOM 3020 C CA . ILE A 1 394 ? -40.670 44.412 23.445 1.00 38.24 ? 394 ILE A CA 1 ATOM 3021 C C . ILE A 1 394 ? -41.405 43.325 22.687 1.00 36.53 ? 394 ILE A C 1 ATOM 3022 O O . ILE A 1 394 ? -40.916 42.816 21.684 1.00 35.57 ? 394 ILE A O 1 ATOM 3023 C CB . ILE A 1 394 ? -40.133 43.863 24.777 1.00 39.17 ? 394 ILE A CB 1 ATOM 3024 C CG1 . ILE A 1 394 ? -39.060 44.820 25.309 1.00 41.05 ? 394 ILE A CG1 1 ATOM 3025 C CG2 . ILE A 1 394 ? -39.562 42.454 24.609 1.00 38.24 ? 394 ILE A CG2 1 ATOM 3026 C CD1 . ILE A 1 394 ? -38.664 44.593 26.753 1.00 42.69 ? 394 ILE A CD1 1 ATOM 3027 N N . VAL A 1 395 ? -42.602 43.003 23.150 1.00 35.82 ? 395 VAL A N 1 ATOM 3028 C CA . VAL A 1 395 ? -43.341 41.886 22.601 1.00 34.20 ? 395 VAL A CA 1 ATOM 3029 C C . VAL A 1 395 ? -43.809 42.192 21.183 1.00 33.50 ? 395 VAL A C 1 ATOM 3030 O O . VAL A 1 395 ? -43.666 41.354 20.287 1.00 32.72 ? 395 VAL A O 1 ATOM 3031 C CB . VAL A 1 395 ? -44.521 41.511 23.514 1.00 34.11 ? 395 VAL A CB 1 ATOM 3032 C CG1 . VAL A 1 395 ? -45.328 40.372 22.914 1.00 33.24 ? 395 VAL A CG1 1 ATOM 3033 C CG2 . VAL A 1 395 ? -44.016 41.115 24.900 1.00 34.70 ? 395 VAL A CG2 1 ATOM 3034 N N . GLY A 1 396 ? -44.349 43.396 20.981 1.00 33.88 ? 396 GLY A N 1 ATOM 3035 C CA . GLY A 1 396 ? -44.844 43.822 19.673 1.00 32.38 ? 396 GLY A CA 1 ATOM 3036 C C . GLY A 1 396 ? -43.719 43.965 18.666 1.00 33.95 ? 396 GLY A C 1 ATOM 3037 O O . GLY A 1 396 ? -43.838 43.506 17.537 1.00 36.41 ? 396 GLY A O 1 ATOM 3038 N N . ASP A 1 397 ? -42.613 44.583 19.067 1.00 34.89 ? 397 ASP A N 1 ATOM 3039 C CA . ASP A 1 397 ? -41.459 44.733 18.183 1.00 35.65 ? 397 ASP A CA 1 ATOM 3040 C C . ASP A 1 397 ? -40.870 43.389 17.771 1.00 36.06 ? 397 ASP A C 1 ATOM 3041 O O . ASP A 1 397 ? -40.586 43.157 16.592 1.00 37.02 ? 397 ASP A O 1 ATOM 3042 C CB . ASP A 1 397 ? -40.363 45.590 18.834 1.00 36.98 ? 397 ASP A CB 1 ATOM 3043 C CG . ASP A 1 397 ? -40.765 47.052 18.987 1.00 37.57 ? 397 ASP A CG 1 ATOM 3044 O OD1 . ASP A 1 397 ? -41.654 47.520 18.251 1.00 36.31 ? 397 ASP A OD1 1 ATOM 3045 O OD2 . ASP A 1 397 ? -40.193 47.738 19.856 1.00 39.55 ? 397 ASP A OD2 1 ATOM 3046 N N . HIS A 1 398 ? -40.685 42.503 18.739 1.00 36.16 ? 398 HIS A N 1 ATOM 3047 C CA . HIS A 1 398 ? -40.055 41.206 18.471 1.00 35.68 ? 398 HIS A CA 1 ATOM 3048 C C . HIS A 1 398 ? -40.936 40.282 17.649 1.00 34.16 ? 398 HIS A C 1 ATOM 3049 O O . HIS A 1 398 ? -40.445 39.609 16.765 1.00 35.92 ? 398 HIS A O 1 ATOM 3050 C CB . HIS A 1 398 ? -39.676 40.520 19.782 1.00 36.07 ? 398 HIS A CB 1 ATOM 3051 C CG . HIS A 1 398 ? -39.093 39.152 19.615 1.00 36.24 ? 398 HIS A CG 1 ATOM 3052 N ND1 . HIS A 1 398 ? -38.158 38.849 18.650 1.00 36.71 ? 398 HIS A ND1 1 ATOM 3053 C CD2 . HIS A 1 398 ? -39.287 38.013 20.319 1.00 36.24 ? 398 HIS A CD2 1 ATOM 3054 C CE1 . HIS A 1 398 ? -37.806 37.584 18.762 1.00 35.88 ? 398 HIS A CE1 1 ATOM 3055 N NE2 . HIS A 1 398 ? -38.479 37.054 19.765 1.00 36.25 ? 398 HIS A NE2 1 ATOM 3056 N N . ASN A 1 399 ? -42.230 40.258 17.924 1.00 33.33 ? 399 ASN A N 1 ATOM 3057 C CA . ASN A 1 399 ? -43.093 39.259 17.317 1.00 32.78 ? 399 ASN A CA 1 ATOM 3058 C C . ASN A 1 399 ? -43.803 39.692 16.044 1.00 32.73 ? 399 ASN A C 1 ATOM 3059 O O . ASN A 1 399 ? -44.198 38.844 15.246 1.00 31.48 ? 399 ASN A O 1 ATOM 3060 C CB . ASN A 1 399 ? -44.107 38.772 18.342 1.00 33.12 ? 399 ASN A CB 1 ATOM 3061 C CG . ASN A 1 399 ? -43.465 37.919 19.415 1.00 33.41 ? 399 ASN A CG 1 ATOM 3062 O OD1 . ASN A 1 399 ? -43.137 36.756 19.184 1.00 32.34 ? 399 ASN A OD1 1 ATOM 3063 N ND2 . ASN A 1 399 ? -43.265 38.496 20.586 1.00 33.80 ? 399 ASN A ND2 1 ATOM 3064 N N . VAL A 1 400 ? -43.956 40.998 15.848 1.00 32.98 ? 400 VAL A N 1 ATOM 3065 C CA . VAL A 1 400 ? -44.788 41.497 14.768 1.00 33.46 ? 400 VAL A CA 1 ATOM 3066 C C . VAL A 1 400 ? -44.111 42.574 13.950 1.00 35.25 ? 400 VAL A C 1 ATOM 3067 O O . VAL A 1 400 ? -43.880 42.382 12.750 1.00 36.23 ? 400 VAL A O 1 ATOM 3068 C CB . VAL A 1 400 ? -46.130 42.023 15.297 1.00 33.88 ? 400 VAL A CB 1 ATOM 3069 C CG1 . VAL A 1 400 ? -47.003 42.547 14.154 1.00 33.70 ? 400 VAL A CG1 1 ATOM 3070 C CG2 . VAL A 1 400 ? -46.845 40.915 16.063 1.00 33.44 ? 400 VAL A CG2 1 ATOM 3071 N N . ILE A 1 401 ? -43.787 43.703 14.573 1.00 36.03 ? 401 ILE A N 1 ATOM 3072 C CA . ILE A 1 401 ? -43.321 44.847 13.790 1.00 38.05 ? 401 ILE A CA 1 ATOM 3073 C C . ILE A 1 401 ? -41.984 44.579 13.123 1.00 39.39 ? 401 ILE A C 1 ATOM 3074 O O . ILE A 1 401 ? -41.861 44.701 11.911 1.00 42.05 ? 401 ILE A O 1 ATOM 3075 C CB . ILE A 1 401 ? -43.246 46.136 14.609 1.00 39.21 ? 401 ILE A CB 1 ATOM 3076 C CG1 . ILE A 1 401 ? -44.650 46.495 15.104 1.00 39.36 ? 401 ILE A CG1 1 ATOM 3077 C CG2 . ILE A 1 401 ? -42.644 47.259 13.763 1.00 40.15 ? 401 ILE A CG2 1 ATOM 3078 C CD1 . ILE A 1 401 ? -44.730 47.760 15.924 1.00 40.55 ? 401 ILE A CD1 1 ATOM 3079 N N . CYS A 1 402 ? -40.985 44.203 13.900 1.00 39.72 ? 402 CYS A N 1 ATOM 3080 C CA . CYS A 1 402 ? -39.663 44.019 13.334 1.00 39.79 ? 402 CYS A CA 1 ATOM 3081 C C . CYS A 1 402 ? -39.528 42.840 12.360 1.00 39.82 ? 402 CYS A C 1 ATOM 3082 O O . CYS A 1 402 ? -38.714 42.918 11.443 1.00 41.04 ? 402 CYS A O 1 ATOM 3083 C CB . CYS A 1 402 ? -38.613 43.979 14.440 1.00 39.94 ? 402 CYS A CB 1 ATOM 3084 S SG . CYS A 1 402 ? -38.461 45.596 15.239 1.00 41.18 ? 402 CYS A SG 1 ATOM 3085 N N . PRO A 1 403 ? -40.294 41.749 12.556 1.00 38.63 ? 403 PRO A N 1 ATOM 3086 C CA . PRO A 1 403 ? -40.322 40.722 11.516 1.00 38.11 ? 403 PRO A CA 1 ATOM 3087 C C . PRO A 1 403 ? -40.949 41.192 10.209 1.00 37.26 ? 403 PRO A C 1 ATOM 3088 O O . PRO A 1 403 ? -40.466 40.842 9.127 1.00 37.03 ? 403 PRO A O 1 ATOM 3089 C CB . PRO A 1 403 ? -41.158 39.614 12.151 1.00 37.77 ? 403 PRO A CB 1 ATOM 3090 C CG . PRO A 1 403 ? -40.806 39.705 13.590 1.00 38.08 ? 403 PRO A CG 1 ATOM 3091 C CD . PRO A 1 403 ? -40.664 41.183 13.864 1.00 39.13 ? 403 PRO A CD 1 ATOM 3092 N N . LEU A 1 404 ? -42.016 41.975 10.316 1.00 36.23 ? 404 LEU A N 1 ATOM 3093 C CA . LEU A 1 404 ? -42.696 42.511 9.143 1.00 35.26 ? 404 LEU A CA 1 ATOM 3094 C C . LEU A 1 404 ? -41.834 43.561 8.446 1.00 37.45 ? 404 LEU A C 1 ATOM 3095 O O . LEU A 1 404 ? -41.879 43.685 7.225 1.00 39.27 ? 404 LEU A O 1 ATOM 3096 C CB . LEU A 1 404 ? -44.042 43.110 9.535 1.00 34.11 ? 404 LEU A CB 1 ATOM 3097 C CG . LEU A 1 404 ? -44.817 43.786 8.405 1.00 34.39 ? 404 LEU A CG 1 ATOM 3098 C CD1 . LEU A 1 404 ? -46.314 43.653 8.630 1.00 34.28 ? 404 LEU A CD1 1 ATOM 3099 C CD2 . LEU A 1 404 ? -44.436 45.249 8.251 1.00 35.46 ? 404 LEU A CD2 1 ATOM 3100 N N . MET A 1 405 ? -41.045 44.313 9.208 1.00 37.49 ? 405 MET A N 1 ATOM 3101 C CA . MET A 1 405 ? -40.187 45.318 8.604 1.00 38.45 ? 405 MET A CA 1 ATOM 3102 C C . MET A 1 405 ? -39.034 44.678 7.862 1.00 39.29 ? 405 MET A C 1 ATOM 3103 O O . MET A 1 405 ? -38.518 45.245 6.910 1.00 40.88 ? 405 MET A O 1 ATOM 3104 C CB . MET A 1 405 ? -39.677 46.299 9.649 1.00 38.43 ? 405 MET A CB 1 ATOM 3105 C CG . MET A 1 405 ? -40.786 47.203 10.163 1.00 39.31 ? 405 MET A CG 1 ATOM 3106 S SD . MET A 1 405 ? -41.643 48.115 8.864 1.00 39.72 ? 405 MET A SD 1 ATOM 3107 C CE . MET A 1 405 ? -40.239 49.006 8.170 1.00 41.06 ? 405 MET A CE 1 ATOM 3108 N N . HIS A 1 406 ? -38.638 43.492 8.287 1.00 40.03 ? 406 HIS A N 1 ATOM 3109 C CA . HIS A 1 406 ? -37.573 42.767 7.609 1.00 41.65 ? 406 HIS A CA 1 ATOM 3110 C C . HIS A 1 406 ? -38.128 42.235 6.300 1.00 41.70 ? 406 HIS A C 1 ATOM 3111 O O . HIS A 1 406 ? -37.526 42.404 5.239 1.00 41.23 ? 406 HIS A O 1 ATOM 3112 C CB . HIS A 1 406 ? -37.070 41.642 8.500 1.00 41.75 ? 406 HIS A CB 1 ATOM 3113 C CG . HIS A 1 406 ? -36.103 40.720 7.839 1.00 42.99 ? 406 HIS A CG 1 ATOM 3114 N ND1 . HIS A 1 406 ? -34.757 40.996 7.743 1.00 45.19 ? 406 HIS A ND1 1 ATOM 3115 C CD2 . HIS A 1 406 ? -36.278 39.499 7.286 1.00 43.07 ? 406 HIS A CD2 1 ATOM 3116 C CE1 . HIS A 1 406 ? -34.144 39.991 7.142 1.00 45.88 ? 406 HIS A CE1 1 ATOM 3117 N NE2 . HIS A 1 406 ? -35.046 39.070 6.854 1.00 45.18 ? 406 HIS A NE2 1 ATOM 3118 N N . PHE A 1 407 ? -39.305 41.630 6.391 1.00 40.84 ? 407 PHE A N 1 ATOM 3119 C CA . PHE A 1 407 ? -40.020 41.158 5.221 1.00 42.07 ? 407 PHE A CA 1 ATOM 3120 C C . PHE A 1 407 ? -40.208 42.277 4.198 1.00 42.54 ? 407 PHE A C 1 ATOM 3121 O O . PHE A 1 407 ? -39.945 42.095 3.010 1.00 40.89 ? 407 PHE A O 1 ATOM 3122 C CB . PHE A 1 407 ? -41.375 40.598 5.639 1.00 42.48 ? 407 PHE A CB 1 ATOM 3123 C CG . PHE A 1 407 ? -42.190 40.081 4.497 1.00 43.16 ? 407 PHE A CG 1 ATOM 3124 C CD1 . PHE A 1 407 ? -41.902 38.857 3.927 1.00 43.45 ? 407 PHE A CD1 1 ATOM 3125 C CD2 . PHE A 1 407 ? -43.250 40.812 3.999 1.00 44.64 ? 407 PHE A CD2 1 ATOM 3126 C CE1 . PHE A 1 407 ? -42.657 38.366 2.875 1.00 43.81 ? 407 PHE A CE1 1 ATOM 3127 C CE2 . PHE A 1 407 ? -44.012 40.328 2.945 1.00 45.47 ? 407 PHE A CE2 1 ATOM 3128 C CZ . PHE A 1 407 ? -43.711 39.103 2.378 1.00 44.16 ? 407 PHE A CZ 1 ATOM 3129 N N . VAL A 1 408 ? -40.634 43.439 4.679 1.00 42.99 ? 408 VAL A N 1 ATOM 3130 C CA . VAL A 1 408 ? -40.904 44.575 3.815 1.00 44.91 ? 408 VAL A CA 1 ATOM 3131 C C . VAL A 1 408 ? -39.667 45.066 3.082 1.00 46.58 ? 408 VAL A C 1 ATOM 3132 O O . VAL A 1 408 ? -39.720 45.327 1.876 1.00 47.94 ? 408 VAL A O 1 ATOM 3133 C CB . VAL A 1 408 ? -41.540 45.726 4.605 1.00 46.58 ? 408 VAL A CB 1 ATOM 3134 C CG1 . VAL A 1 408 ? -41.320 47.060 3.920 1.00 49.85 ? 408 VAL A CG1 1 ATOM 3135 C CG2 . VAL A 1 408 ? -43.024 45.474 4.739 1.00 46.95 ? 408 VAL A CG2 1 ATOM 3136 N N . ASN A 1 409 ? -38.563 45.210 3.804 1.00 47.21 ? 409 ASN A N 1 ATOM 3137 C CA . ASN A 1 409 ? -37.326 45.703 3.196 1.00 49.12 ? 409 ASN A CA 1 ATOM 3138 C C . ASN A 1 409 ? -36.760 44.706 2.197 1.00 48.85 ? 409 ASN A C 1 ATOM 3139 O O . ASN A 1 409 ? -36.199 45.096 1.166 1.00 49.37 ? 409 ASN A O 1 ATOM 3140 C CB . ASN A 1 409 ? -36.281 46.022 4.265 1.00 50.38 ? 409 ASN A CB 1 ATOM 3141 C CG . ASN A 1 409 ? -36.684 47.194 5.136 1.00 50.87 ? 409 ASN A CG 1 ATOM 3142 O OD1 . ASN A 1 409 ? -37.006 48.278 4.636 1.00 50.96 ? 409 ASN A OD1 1 ATOM 3143 N ND2 . ASN A 1 409 ? -36.671 46.982 6.451 1.00 49.96 ? 409 ASN A ND2 1 ATOM 3144 N N . LYS A 1 410 ? -36.913 43.422 2.511 1.00 46.73 ? 410 LYS A N 1 ATOM 3145 C CA . LYS A 1 410 ? -36.481 42.369 1.616 1.00 46.90 ? 410 LYS A CA 1 ATOM 3146 C C . LYS A 1 410 ? -37.391 42.256 0.395 1.00 47.00 ? 410 LYS A C 1 ATOM 3147 O O . LYS A 1 410 ? -36.900 42.120 -0.736 1.00 48.71 ? 410 LYS A O 1 ATOM 3148 C CB . LYS A 1 410 ? -36.421 41.038 2.348 1.00 46.48 ? 410 LYS A CB 1 ATOM 3149 C CG . LYS A 1 410 ? -35.351 40.978 3.430 1.00 48.55 ? 410 LYS A CG 1 ATOM 3150 C CD . LYS A 1 410 ? -33.961 41.139 2.850 1.00 50.64 ? 410 LYS A CD 1 ATOM 3151 C CE . LYS A 1 410 ? -32.893 40.517 3.727 1.00 51.84 ? 410 LYS A CE 1 ATOM 3152 N NZ . LYS A 1 410 ? -31.659 40.265 2.926 1.00 53.90 ? 410 LYS A NZ 1 ATOM 3153 N N . TYR A 1 411 ? -38.706 42.314 0.610 1.00 43.85 ? 411 TYR A N 1 ATOM 3154 C CA . TYR A 1 411 ? -39.640 42.111 -0.491 1.00 42.35 ? 411 TYR A CA 1 ATOM 3155 C C . TYR A 1 411 ? -39.518 43.235 -1.488 1.00 44.10 ? 411 TYR A C 1 ATOM 3156 O O . TYR A 1 411 ? -39.553 43.012 -2.696 1.00 44.93 ? 411 TYR A O 1 ATOM 3157 C CB . TYR A 1 411 ? -41.097 42.020 -0.015 1.00 40.17 ? 411 TYR A CB 1 ATOM 3158 C CG . TYR A 1 411 ? -42.055 41.664 -1.134 1.00 39.16 ? 411 TYR A CG 1 ATOM 3159 C CD1 . TYR A 1 411 ? -42.298 40.339 -1.465 1.00 38.20 ? 411 TYR A CD1 1 ATOM 3160 C CD2 . TYR A 1 411 ? -42.692 42.651 -1.878 1.00 39.42 ? 411 TYR A CD2 1 ATOM 3161 C CE1 . TYR A 1 411 ? -43.160 40.000 -2.488 1.00 38.12 ? 411 TYR A CE1 1 ATOM 3162 C CE2 . TYR A 1 411 ? -43.553 42.327 -2.908 1.00 39.59 ? 411 TYR A CE2 1 ATOM 3163 C CZ . TYR A 1 411 ? -43.789 40.999 -3.217 1.00 39.39 ? 411 TYR A CZ 1 ATOM 3164 O OH . TYR A 1 411 ? -44.648 40.664 -4.255 1.00 38.50 ? 411 TYR A OH 1 ATOM 3165 N N . THR A 1 412 ? -39.373 44.443 -0.964 1.00 44.65 ? 412 THR A N 1 ATOM 3166 C CA . THR A 1 412 ? -39.442 45.655 -1.773 1.00 46.00 ? 412 THR A CA 1 ATOM 3167 C C . THR A 1 412 ? -38.321 45.770 -2.810 1.00 47.39 ? 412 THR A C 1 ATOM 3168 O O . THR A 1 412 ? -38.497 46.453 -3.812 1.00 48.20 ? 412 THR A O 1 ATOM 3169 C CB . THR A 1 412 ? -39.504 46.898 -0.854 1.00 46.27 ? 412 THR A CB 1 ATOM 3170 O OG1 . THR A 1 412 ? -40.771 46.910 -0.176 1.00 44.81 ? 412 THR A OG1 1 ATOM 3171 C CG2 . THR A 1 412 ? -39.321 48.204 -1.633 1.00 47.59 ? 412 THR A CG2 1 ATOM 3172 N N . LYS A 1 413 ? -37.193 45.100 -2.582 1.00 49.15 ? 413 LYS A N 1 ATOM 3173 C CA . LYS A 1 413 ? -36.092 45.083 -3.557 1.00 53.45 ? 413 LYS A CA 1 ATOM 3174 C C . LYS A 1 413 ? -36.467 44.419 -4.876 1.00 51.39 ? 413 LYS A C 1 ATOM 3175 O O . LYS A 1 413 ? -35.932 44.789 -5.906 1.00 52.18 ? 413 LYS A O 1 ATOM 3176 C CB . LYS A 1 413 ? -34.853 44.379 -2.987 1.00 57.92 ? 413 LYS A CB 1 ATOM 3177 C CG . LYS A 1 413 ? -34.036 45.247 -2.046 1.00 64.21 ? 413 LYS A CG 1 ATOM 3178 C CD . LYS A 1 413 ? -32.950 44.442 -1.342 1.00 69.34 ? 413 LYS A CD 1 ATOM 3179 C CE . LYS A 1 413 ? -32.399 45.170 -0.120 1.00 71.94 ? 413 LYS A CE 1 ATOM 3180 N NZ . LYS A 1 413 ? -31.788 44.211 0.847 1.00 72.84 ? 413 LYS A NZ 1 ATOM 3181 N N . PHE A 1 414 ? -37.362 43.431 -4.822 1.00 49.36 ? 414 PHE A N 1 ATOM 3182 C CA . PHE A 1 414 ? -37.801 42.661 -5.998 1.00 48.84 ? 414 PHE A CA 1 ATOM 3183 C C . PHE A 1 414 ? -39.275 42.853 -6.413 1.00 48.08 ? 414 PHE A C 1 ATOM 3184 O O . PHE A 1 414 ? -39.651 42.487 -7.527 1.00 49.35 ? 414 PHE A O 1 ATOM 3185 C CB . PHE A 1 414 ? -37.605 41.174 -5.739 1.00 47.82 ? 414 PHE A CB 1 ATOM 3186 C CG . PHE A 1 414 ? -36.178 40.757 -5.576 1.00 48.62 ? 414 PHE A CG 1 ATOM 3187 C CD1 . PHE A 1 414 ? -35.358 40.605 -6.682 1.00 50.20 ? 414 PHE A CD1 1 ATOM 3188 C CD2 . PHE A 1 414 ? -35.667 40.461 -4.318 1.00 47.92 ? 414 PHE A CD2 1 ATOM 3189 C CE1 . PHE A 1 414 ? -34.043 40.196 -6.539 1.00 51.63 ? 414 PHE A CE1 1 ATOM 3190 C CE2 . PHE A 1 414 ? -34.352 40.052 -4.168 1.00 48.90 ? 414 PHE A CE2 1 ATOM 3191 C CZ . PHE A 1 414 ? -33.537 39.920 -5.279 1.00 50.69 ? 414 PHE A CZ 1 ATOM 3192 N N . GLY A 1 415 ? -40.103 43.408 -5.533 1.00 47.52 ? 415 GLY A N 1 ATOM 3193 C CA . GLY A 1 415 ? -41.548 43.511 -5.776 1.00 47.84 ? 415 GLY A CA 1 ATOM 3194 C C . GLY A 1 415 ? -41.938 44.627 -6.725 1.00 48.80 ? 415 GLY A C 1 ATOM 3195 O O . GLY A 1 415 ? -41.089 45.393 -7.171 1.00 49.65 ? 415 GLY A O 1 ATOM 3196 N N . ASN A 1 416 ? -43.232 44.711 -7.030 1.00 49.76 ? 416 ASN A N 1 ATOM 3197 C CA . ASN A 1 416 ? -43.744 45.682 -7.999 1.00 54.06 ? 416 ASN A CA 1 ATOM 3198 C C . ASN A 1 416 ? -44.519 46.811 -7.327 1.00 53.03 ? 416 ASN A C 1 ATOM 3199 O O . ASN A 1 416 ? -45.186 47.588 -8.003 1.00 54.58 ? 416 ASN A O 1 ATOM 3200 C CB . ASN A 1 416 ? -44.598 44.963 -9.073 1.00 56.63 ? 416 ASN A CB 1 ATOM 3201 C CG . ASN A 1 416 ? -44.936 45.843 -10.291 1.00 60.27 ? 416 ASN A CG 1 ATOM 3202 O OD1 . ASN A 1 416 ? -46.081 45.843 -10.750 1.00 63.54 ? 416 ASN A OD1 1 ATOM 3203 N ND2 . ASN A 1 416 ? -43.960 46.580 -10.823 1.00 62.82 ? 416 ASN A ND2 1 ATOM 3204 N N . GLY A 1 417 ? -44.415 46.916 -6.001 1.00 52.18 ? 417 GLY A N 1 ATOM 3205 C CA . GLY A 1 417 ? -44.999 48.040 -5.270 1.00 51.43 ? 417 GLY A CA 1 ATOM 3206 C C . GLY A 1 417 ? -45.435 47.699 -3.856 1.00 50.73 ? 417 GLY A C 1 ATOM 3207 O O . GLY A 1 417 ? -46.209 46.764 -3.641 1.00 51.58 ? 417 GLY A O 1 ATOM 3208 N N . THR A 1 418 ? -44.960 48.481 -2.891 1.00 49.35 ? 418 THR A N 1 ATOM 3209 C CA . THR A 1 418 ? -45.269 48.258 -1.492 1.00 47.83 ? 418 THR A CA 1 ATOM 3210 C C . THR A 1 418 ? -45.900 49.504 -0.887 1.00 48.16 ? 418 THR A C 1 ATOM 3211 O O . THR A 1 418 ? -45.452 50.621 -1.147 1.00 47.86 ? 418 THR A O 1 ATOM 3212 C CB . THR A 1 418 ? -43.991 47.932 -0.704 1.00 48.95 ? 418 THR A CB 1 ATOM 3213 O OG1 . THR A 1 418 ? -43.355 46.771 -1.258 1.00 48.12 ? 418 THR A OG1 1 ATOM 3214 C CG2 . THR A 1 418 ? -44.310 47.681 0.766 1.00 49.01 ? 418 THR A CG2 1 ATOM 3215 N N . TYR A 1 419 ? -46.937 49.305 -0.078 1.00 47.01 ? 419 TYR A N 1 ATOM 3216 C CA . TYR A 1 419 ? -47.572 50.387 0.668 1.00 47.48 ? 419 TYR A CA 1 ATOM 3217 C C . TYR A 1 419 ? -47.660 49.961 2.142 1.00 46.29 ? 419 TYR A C 1 ATOM 3218 O O . TYR A 1 419 ? -48.209 48.894 2.452 1.00 45.95 ? 419 TYR A O 1 ATOM 3219 C CB . TYR A 1 419 ? -48.961 50.684 0.098 1.00 48.68 ? 419 TYR A CB 1 ATOM 3220 C CG . TYR A 1 419 ? -48.960 51.158 -1.348 1.00 51.10 ? 419 TYR A CG 1 ATOM 3221 C CD1 . TYR A 1 419 ? -48.940 50.243 -2.406 1.00 50.66 ? 419 TYR A CD1 1 ATOM 3222 C CD2 . TYR A 1 419 ? -48.991 52.517 -1.661 1.00 53.13 ? 419 TYR A CD2 1 ATOM 3223 C CE1 . TYR A 1 419 ? -48.931 50.665 -3.726 1.00 51.91 ? 419 TYR A CE1 1 ATOM 3224 C CE2 . TYR A 1 419 ? -48.983 52.950 -2.981 1.00 54.91 ? 419 TYR A CE2 1 ATOM 3225 C CZ . TYR A 1 419 ? -48.956 52.022 -4.013 1.00 54.93 ? 419 TYR A CZ 1 ATOM 3226 O OH . TYR A 1 419 ? -48.961 52.447 -5.332 1.00 55.99 ? 419 TYR A OH 1 ATOM 3227 N N . LEU A 1 420 ? -47.118 50.786 3.041 1.00 45.04 ? 420 LEU A N 1 ATOM 3228 C CA . LEU A 1 420 ? -46.974 50.422 4.458 1.00 43.02 ? 420 LEU A CA 1 ATOM 3229 C C . LEU A 1 420 ? -47.766 51.349 5.390 1.00 42.10 ? 420 LEU A C 1 ATOM 3230 O O . LEU A 1 420 ? -47.749 52.560 5.210 1.00 41.69 ? 420 LEU A O 1 ATOM 3231 C CB . LEU A 1 420 ? -45.490 50.453 4.828 1.00 43.55 ? 420 LEU A CB 1 ATOM 3232 C CG . LEU A 1 420 ? -45.091 50.088 6.255 1.00 42.72 ? 420 LEU A CG 1 ATOM 3233 C CD1 . LEU A 1 420 ? -45.560 48.682 6.586 1.00 41.47 ? 420 LEU A CD1 1 ATOM 3234 C CD2 . LEU A 1 420 ? -43.587 50.222 6.439 1.00 42.75 ? 420 LEU A CD2 1 ATOM 3235 N N . TYR A 1 421 ? -48.457 50.775 6.380 1.00 41.85 ? 421 TYR A N 1 ATOM 3236 C CA . TYR A 1 421 ? -49.247 51.564 7.349 1.00 41.97 ? 421 TYR A CA 1 ATOM 3237 C C . TYR A 1 421 ? -48.947 51.240 8.810 1.00 40.21 ? 421 TYR A C 1 ATOM 3238 O O . TYR A 1 421 ? -48.551 50.140 9.162 1.00 37.62 ? 421 TYR A O 1 ATOM 3239 C CB . TYR A 1 421 ? -50.758 51.377 7.123 1.00 42.58 ? 421 TYR A CB 1 ATOM 3240 C CG . TYR A 1 421 ? -51.295 50.020 7.560 1.00 41.36 ? 421 TYR A CG 1 ATOM 3241 C CD1 . TYR A 1 421 ? -51.655 49.778 8.885 1.00 40.87 ? 421 TYR A CD1 1 ATOM 3242 C CD2 . TYR A 1 421 ? -51.438 48.979 6.646 1.00 41.23 ? 421 TYR A CD2 1 ATOM 3243 C CE1 . TYR A 1 421 ? -52.133 48.535 9.281 1.00 39.77 ? 421 TYR A CE1 1 ATOM 3244 C CE2 . TYR A 1 421 ? -51.919 47.733 7.037 1.00 39.47 ? 421 TYR A CE2 1 ATOM 3245 C CZ . TYR A 1 421 ? -52.261 47.520 8.350 1.00 38.70 ? 421 TYR A CZ 1 ATOM 3246 O OH . TYR A 1 421 ? -52.722 46.290 8.729 1.00 37.67 ? 421 TYR A OH 1 ATOM 3247 N N . PHE A 1 422 ? -49.200 52.219 9.657 1.00 41.36 ? 422 PHE A N 1 ATOM 3248 C CA . PHE A 1 422 ? -49.104 52.067 11.091 1.00 41.02 ? 422 PHE A CA 1 ATOM 3249 C C . PHE A 1 422 ? -50.454 52.500 11.633 1.00 42.03 ? 422 PHE A C 1 ATOM 3250 O O . PHE A 1 422 ? -50.794 53.685 11.599 1.00 44.70 ? 422 PHE A O 1 ATOM 3251 C CB . PHE A 1 422 ? -47.981 52.967 11.601 1.00 42.06 ? 422 PHE A CB 1 ATOM 3252 C CG . PHE A 1 422 ? -47.737 52.885 13.075 1.00 41.40 ? 422 PHE A CG 1 ATOM 3253 C CD1 . PHE A 1 422 ? -47.063 51.809 13.616 1.00 40.39 ? 422 PHE A CD1 1 ATOM 3254 C CD2 . PHE A 1 422 ? -48.138 53.920 13.915 1.00 43.16 ? 422 PHE A CD2 1 ATOM 3255 C CE1 . PHE A 1 422 ? -46.807 51.751 14.975 1.00 41.51 ? 422 PHE A CE1 1 ATOM 3256 C CE2 . PHE A 1 422 ? -47.892 53.872 15.276 1.00 43.66 ? 422 PHE A CE2 1 ATOM 3257 C CZ . PHE A 1 422 ? -47.224 52.783 15.809 1.00 43.07 ? 422 PHE A CZ 1 ATOM 3258 N N . PHE A 1 423 ? -51.239 51.532 12.088 1.00 42.32 ? 423 PHE A N 1 ATOM 3259 C CA . PHE A 1 423 ? -52.578 51.790 12.610 1.00 43.55 ? 423 PHE A CA 1 ATOM 3260 C C . PHE A 1 423 ? -52.522 52.065 14.108 1.00 44.10 ? 423 PHE A C 1 ATOM 3261 O O . PHE A 1 423 ? -52.185 51.188 14.889 1.00 45.90 ? 423 PHE A O 1 ATOM 3262 C CB . PHE A 1 423 ? -53.473 50.592 12.336 1.00 42.95 ? 423 PHE A CB 1 ATOM 3263 C CG . PHE A 1 423 ? -54.872 50.764 12.832 1.00 44.82 ? 423 PHE A CG 1 ATOM 3264 C CD1 . PHE A 1 423 ? -55.220 50.386 14.118 1.00 45.41 ? 423 PHE A CD1 1 ATOM 3265 C CD2 . PHE A 1 423 ? -55.845 51.302 12.016 1.00 46.09 ? 423 PHE A CD2 1 ATOM 3266 C CE1 . PHE A 1 423 ? -56.517 50.544 14.583 1.00 46.16 ? 423 PHE A CE1 1 ATOM 3267 C CE2 . PHE A 1 423 ? -57.143 51.463 12.477 1.00 47.06 ? 423 PHE A CE2 1 ATOM 3268 C CZ . PHE A 1 423 ? -57.481 51.083 13.760 1.00 46.03 ? 423 PHE A CZ 1 ATOM 3269 N N . ASN A 1 424 ? -52.865 53.276 14.518 1.00 45.12 ? 424 ASN A N 1 ATOM 3270 C CA . ASN A 1 424 ? -52.692 53.667 15.906 1.00 45.15 ? 424 ASN A CA 1 ATOM 3271 C C . ASN A 1 424 ? -53.871 54.473 16.461 1.00 46.64 ? 424 ASN A C 1 ATOM 3272 O O . ASN A 1 424 ? -53.683 55.396 17.254 1.00 46.40 ? 424 ASN A O 1 ATOM 3273 C CB . ASN A 1 424 ? -51.389 54.454 16.036 1.00 45.37 ? 424 ASN A CB 1 ATOM 3274 C CG . ASN A 1 424 ? -51.451 55.799 15.349 1.00 45.89 ? 424 ASN A CG 1 ATOM 3275 O OD1 . ASN A 1 424 ? -52.395 56.094 14.627 1.00 46.85 ? 424 ASN A OD1 1 ATOM 3276 N ND2 . ASN A 1 424 ? -50.446 56.623 15.576 1.00 46.22 ? 424 ASN A ND2 1 ATOM 3277 N N . HIS A 1 425 ? -55.084 54.117 16.042 1.00 47.68 ? 425 HIS A N 1 ATOM 3278 C CA . HIS A 1 425 ? -56.291 54.710 16.603 1.00 49.93 ? 425 HIS A CA 1 ATOM 3279 C C . HIS A 1 425 ? -56.913 53.750 17.605 1.00 51.53 ? 425 HIS A C 1 ATOM 3280 O O . HIS A 1 425 ? -57.167 52.574 17.292 1.00 51.75 ? 425 HIS A O 1 ATOM 3281 C CB . HIS A 1 425 ? -57.316 55.031 15.522 1.00 50.00 ? 425 HIS A CB 1 ATOM 3282 C CG . HIS A 1 425 ? -58.630 55.493 16.071 1.00 51.26 ? 425 HIS A CG 1 ATOM 3283 N ND1 . HIS A 1 425 ? -58.850 56.791 16.483 1.00 53.18 ? 425 HIS A ND1 1 ATOM 3284 C CD2 . HIS A 1 425 ? -59.785 54.825 16.304 1.00 50.53 ? 425 HIS A CD2 1 ATOM 3285 C CE1 . HIS A 1 425 ? -60.089 56.908 16.928 1.00 53.47 ? 425 HIS A CE1 1 ATOM 3286 N NE2 . HIS A 1 425 ? -60.677 55.730 16.833 1.00 52.20 ? 425 HIS A NE2 1 ATOM 3287 N N . ARG A 1 426 ? -57.163 54.256 18.809 1.00 54.19 ? 426 ARG A N 1 ATOM 3288 C CA . ARG A 1 426 ? -57.831 53.473 19.843 1.00 56.08 ? 426 ARG A CA 1 ATOM 3289 C C . ARG A 1 426 ? -59.329 53.739 19.768 1.00 54.40 ? 426 ARG A C 1 ATOM 3290 O O . ARG A 1 426 ? -59.763 54.887 19.878 1.00 54.51 ? 426 ARG A O 1 ATOM 3291 C CB . ARG A 1 426 ? -57.301 53.821 21.246 1.00 59.43 ? 426 ARG A CB 1 ATOM 3292 C CG . ARG A 1 426 ? -57.808 52.858 22.321 1.00 62.08 ? 426 ARG A CG 1 ATOM 3293 C CD . ARG A 1 426 ? -57.672 53.411 23.732 1.00 66.12 ? 426 ARG A CD 1 ATOM 3294 N NE . ARG A 1 426 ? -58.560 52.737 24.684 1.00 67.72 ? 426 ARG A NE 1 ATOM 3295 C CZ . ARG A 1 426 ? -58.412 51.481 25.117 1.00 66.43 ? 426 ARG A CZ 1 ATOM 3296 N NH1 . ARG A 1 426 ? -57.403 50.704 24.699 1.00 61.95 ? 426 ARG A NH1 1 ATOM 3297 N NH2 . ARG A 1 426 ? -59.288 50.997 25.991 1.00 67.16 ? 426 ARG A NH2 1 ATOM 3298 N N . ALA A 1 427 ? -60.113 52.678 19.596 1.00 52.10 ? 427 ALA A N 1 ATOM 3299 C CA . ALA A 1 427 ? -61.547 52.835 19.405 1.00 52.92 ? 427 ALA A CA 1 ATOM 3300 C C . ALA A 1 427 ? -62.185 53.438 20.639 1.00 54.11 ? 427 ALA A C 1 ATOM 3301 O O . ALA A 1 427 ? -61.854 53.082 21.774 1.00 51.77 ? 427 ALA A O 1 ATOM 3302 C CB . ALA A 1 427 ? -62.210 51.511 19.048 1.00 52.50 ? 427 ALA A CB 1 ATOM 3303 N N . SER A 1 428 ? -63.097 54.372 20.389 1.00 56.74 ? 428 SER A N 1 ATOM 3304 C CA . SER A 1 428 ? -63.839 55.054 21.436 1.00 58.47 ? 428 SER A CA 1 ATOM 3305 C C . SER A 1 428 ? -64.691 54.088 22.266 1.00 59.33 ? 428 SER A C 1 ATOM 3306 O O . SER A 1 428 ? -65.011 54.394 23.408 1.00 60.21 ? 428 SER A O 1 ATOM 3307 C CB . SER A 1 428 ? -64.740 56.103 20.802 1.00 59.80 ? 428 SER A CB 1 ATOM 3308 O OG . SER A 1 428 ? -65.519 55.495 19.791 1.00 59.94 ? 428 SER A OG 1 ATOM 3309 N N . ASN A 1 429 ? -65.053 52.934 21.693 1.00 59.29 ? 429 ASN A N 1 ATOM 3310 C CA . ASN A 1 429 ? -65.891 51.927 22.379 1.00 58.91 ? 429 ASN A CA 1 ATOM 3311 C C . ASN A 1 429 ? -65.141 50.668 22.845 1.00 56.30 ? 429 ASN A C 1 ATOM 3312 O O . ASN A 1 429 ? -65.769 49.646 23.129 1.00 54.89 ? 429 ASN A O 1 ATOM 3313 C CB . ASN A 1 429 ? -67.061 51.502 21.470 1.00 59.13 ? 429 ASN A CB 1 ATOM 3314 C CG . ASN A 1 429 ? -66.599 50.906 20.152 1.00 58.54 ? 429 ASN A CG 1 ATOM 3315 O OD1 . ASN A 1 429 ? -65.399 50.775 19.894 1.00 57.63 ? 429 ASN A OD1 1 ATOM 3316 N ND2 . ASN A 1 429 ? -67.556 50.562 19.296 1.00 59.67 ? 429 ASN A ND2 1 ATOM 3317 N N . LEU A 1 430 ? -63.814 50.736 22.931 1.00 53.81 ? 430 LEU A N 1 ATOM 3318 C CA . LEU A 1 430 ? -63.025 49.540 23.218 1.00 52.30 ? 430 LEU A CA 1 ATOM 3319 C C . LEU A 1 430 ? -63.283 49.038 24.633 1.00 51.76 ? 430 LEU A C 1 ATOM 3320 O O . LEU A 1 430 ? -63.231 49.806 25.592 1.00 52.58 ? 430 LEU A O 1 ATOM 3321 C CB . LEU A 1 430 ? -61.527 49.787 23.022 1.00 51.83 ? 430 LEU A CB 1 ATOM 3322 C CG . LEU A 1 430 ? -60.741 48.512 22.691 1.00 50.60 ? 430 LEU A CG 1 ATOM 3323 C CD1 . LEU A 1 430 ? -60.898 48.134 21.227 1.00 49.56 ? 430 LEU A CD1 1 ATOM 3324 C CD2 . LEU A 1 430 ? -59.274 48.685 23.026 1.00 50.73 ? 430 LEU A CD2 1 ATOM 3325 N N . VAL A 1 431 ? -63.572 47.744 24.739 1.00 50.27 ? 431 VAL A N 1 ATOM 3326 C CA . VAL A 1 431 ? -63.934 47.119 26.013 1.00 49.71 ? 431 VAL A CA 1 ATOM 3327 C C . VAL A 1 431 ? -62.702 46.804 26.871 1.00 47.93 ? 431 VAL A C 1 ATOM 3328 O O . VAL A 1 431 ? -62.799 46.721 28.091 1.00 48.88 ? 431 VAL A O 1 ATOM 3329 C CB . VAL A 1 431 ? -64.785 45.837 25.809 1.00 49.04 ? 431 VAL A CB 1 ATOM 3330 C CG1 . VAL A 1 431 ? -66.183 46.199 25.327 1.00 49.52 ? 431 VAL A CG1 1 ATOM 3331 C CG2 . VAL A 1 431 ? -64.113 44.860 24.848 1.00 46.86 ? 431 VAL A CG2 1 ATOM 3332 N N . TRP A 1 432 ? -61.551 46.645 26.226 1.00 45.25 ? 432 TRP A N 1 ATOM 3333 C CA . TRP A 1 432 ? -60.294 46.386 26.920 1.00 43.90 ? 432 TRP A CA 1 ATOM 3334 C C . TRP A 1 432 ? -59.816 47.637 27.663 1.00 43.85 ? 432 TRP A C 1 ATOM 3335 O O . TRP A 1 432 ? -60.253 48.735 27.359 1.00 44.03 ? 432 TRP A O 1 ATOM 3336 C CB . TRP A 1 432 ? -59.235 45.908 25.920 1.00 42.80 ? 432 TRP A CB 1 ATOM 3337 C CG . TRP A 1 432 ? -59.544 44.563 25.293 1.00 42.14 ? 432 TRP A CG 1 ATOM 3338 C CD1 . TRP A 1 432 ? -59.957 44.334 24.023 1.00 41.79 ? 432 TRP A CD1 1 ATOM 3339 C CD2 . TRP A 1 432 ? -59.459 43.282 25.917 1.00 42.54 ? 432 TRP A CD2 1 ATOM 3340 N NE1 . TRP A 1 432 ? -60.141 42.995 23.813 1.00 40.87 ? 432 TRP A NE1 1 ATOM 3341 C CE2 . TRP A 1 432 ? -59.833 42.324 24.959 1.00 41.96 ? 432 TRP A CE2 1 ATOM 3342 C CE3 . TRP A 1 432 ? -59.118 42.851 27.197 1.00 44.57 ? 432 TRP A CE3 1 ATOM 3343 C CZ2 . TRP A 1 432 ? -59.860 40.957 25.233 1.00 43.34 ? 432 TRP A CZ2 1 ATOM 3344 C CZ3 . TRP A 1 432 ? -59.148 41.486 27.474 1.00 45.42 ? 432 TRP A CZ3 1 ATOM 3345 C CH2 . TRP A 1 432 ? -59.513 40.557 26.494 1.00 44.23 ? 432 TRP A CH2 1 ATOM 3346 N N . PRO A 1 433 ? -58.939 47.471 28.671 1.00 43.99 ? 433 PRO A N 1 ATOM 3347 C CA . PRO A 1 433 ? -58.450 48.635 29.398 1.00 44.34 ? 433 PRO A CA 1 ATOM 3348 C C . PRO A 1 433 ? -57.499 49.469 28.554 1.00 45.49 ? 433 PRO A C 1 ATOM 3349 O O . PRO A 1 433 ? -56.934 48.973 27.576 1.00 45.15 ? 433 PRO A O 1 ATOM 3350 C CB . PRO A 1 433 ? -57.720 48.019 30.588 1.00 44.26 ? 433 PRO A CB 1 ATOM 3351 C CG . PRO A 1 433 ? -57.307 46.670 30.125 1.00 42.97 ? 433 PRO A CG 1 ATOM 3352 C CD . PRO A 1 433 ? -58.432 46.213 29.252 1.00 43.03 ? 433 PRO A CD 1 ATOM 3353 N N . GLU A 1 434 ? -57.318 50.723 28.946 1.00 48.90 ? 434 GLU A N 1 ATOM 3354 C CA . GLU A 1 434 ? -56.551 51.691 28.166 1.00 51.55 ? 434 GLU A CA 1 ATOM 3355 C C . GLU A 1 434 ? -55.070 51.327 28.023 1.00 48.62 ? 434 GLU A C 1 ATOM 3356 O O . GLU A 1 434 ? -54.473 51.617 26.991 1.00 48.54 ? 434 GLU A O 1 ATOM 3357 C CB . GLU A 1 434 ? -56.701 53.097 28.762 1.00 57.70 ? 434 GLU A CB 1 ATOM 3358 C CG . GLU A 1 434 ? -56.299 54.236 27.834 1.00 63.56 ? 434 GLU A CG 1 ATOM 3359 C CD . GLU A 1 434 ? -56.265 55.588 28.543 1.00 71.05 ? 434 GLU A CD 1 ATOM 3360 O OE1 . GLU A 1 434 ? -57.009 55.784 29.538 1.00 75.64 ? 434 GLU A OE1 1 ATOM 3361 O OE2 . GLU A 1 434 ? -55.490 56.465 28.103 1.00 74.80 ? 434 GLU A OE2 1 ATOM 3362 N N . TRP A 1 435 ? -54.483 50.688 29.033 1.00 46.72 ? 435 TRP A N 1 ATOM 3363 C CA . TRP A 1 435 ? -53.060 50.323 28.983 1.00 44.96 ? 435 TRP A CA 1 ATOM 3364 C C . TRP A 1 435 ? -52.729 49.375 27.844 1.00 42.31 ? 435 TRP A C 1 ATOM 3365 O O . TRP A 1 435 ? -51.587 49.306 27.415 1.00 39.82 ? 435 TRP A O 1 ATOM 3366 C CB . TRP A 1 435 ? -52.561 49.716 30.320 1.00 45.90 ? 435 TRP A CB 1 ATOM 3367 C CG . TRP A 1 435 ? -53.104 48.329 30.690 1.00 44.76 ? 435 TRP A CG 1 ATOM 3368 C CD1 . TRP A 1 435 ? -54.133 48.059 31.541 1.00 45.58 ? 435 TRP A CD1 1 ATOM 3369 C CD2 . TRP A 1 435 ? -52.619 47.055 30.241 1.00 42.74 ? 435 TRP A CD2 1 ATOM 3370 N NE1 . TRP A 1 435 ? -54.324 46.704 31.645 1.00 44.36 ? 435 TRP A NE1 1 ATOM 3371 C CE2 . TRP A 1 435 ? -53.413 46.067 30.849 1.00 42.92 ? 435 TRP A CE2 1 ATOM 3372 C CE3 . TRP A 1 435 ? -51.592 46.657 29.381 1.00 41.71 ? 435 TRP A CE3 1 ATOM 3373 C CZ2 . TRP A 1 435 ? -53.219 44.707 30.620 1.00 42.26 ? 435 TRP A CZ2 1 ATOM 3374 C CZ3 . TRP A 1 435 ? -51.396 45.302 29.159 1.00 40.67 ? 435 TRP A CZ3 1 ATOM 3375 C CH2 . TRP A 1 435 ? -52.207 44.345 29.773 1.00 40.84 ? 435 TRP A CH2 1 ATOM 3376 N N . MET A 1 436 ? -53.725 48.631 27.377 1.00 42.33 ? 436 MET A N 1 ATOM 3377 C CA . MET A 1 436 ? -53.540 47.696 26.274 1.00 41.18 ? 436 MET A CA 1 ATOM 3378 C C . MET A 1 436 ? -53.389 48.390 24.914 1.00 41.02 ? 436 MET A C 1 ATOM 3379 O O . MET A 1 436 ? -52.905 47.785 23.944 1.00 39.45 ? 436 MET A O 1 ATOM 3380 C CB . MET A 1 436 ? -54.693 46.694 26.249 1.00 41.29 ? 436 MET A CB 1 ATOM 3381 C CG . MET A 1 436 ? -54.679 45.757 27.448 1.00 42.15 ? 436 MET A CG 1 ATOM 3382 S SD . MET A 1 436 ? -55.931 44.464 27.364 1.00 42.25 ? 436 MET A SD 1 ATOM 3383 C CE . MET A 1 436 ? -55.239 43.446 26.064 1.00 40.78 ? 436 MET A CE 1 ATOM 3384 N N . GLY A 1 437 ? -53.823 49.645 24.846 1.00 42.14 ? 437 GLY A N 1 ATOM 3385 C CA . GLY A 1 437 ? -53.563 50.505 23.692 1.00 42.71 ? 437 GLY A CA 1 ATOM 3386 C C . GLY A 1 437 ? -54.336 50.149 22.433 1.00 42.16 ? 437 GLY A C 1 ATOM 3387 O O . GLY A 1 437 ? -55.520 49.809 22.499 1.00 43.24 ? 437 GLY A O 1 ATOM 3388 N N . VAL A 1 438 ? -53.654 50.250 21.288 1.00 40.99 ? 438 VAL A N 1 ATOM 3389 C CA . VAL A 1 438 ? -54.198 49.849 19.993 1.00 39.77 ? 438 VAL A CA 1 ATOM 3390 C C . VAL A 1 438 ? -53.822 48.385 19.802 1.00 39.18 ? 438 VAL A C 1 ATOM 3391 O O . VAL A 1 438 ? -52.681 48.043 19.482 1.00 38.19 ? 438 VAL A O 1 ATOM 3392 C CB . VAL A 1 438 ? -53.642 50.725 18.859 1.00 39.29 ? 438 VAL A CB 1 ATOM 3393 C CG1 . VAL A 1 438 ? -54.375 50.446 17.553 1.00 38.41 ? 438 VAL A CG1 1 ATOM 3394 C CG2 . VAL A 1 438 ? -53.747 52.196 19.243 1.00 40.40 ? 438 VAL A CG2 1 ATOM 3395 N N . ILE A 1 439 ? -54.797 47.520 20.023 1.00 40.01 ? 439 ILE A N 1 ATOM 3396 C CA . ILE A 1 439 ? -54.522 46.119 20.293 1.00 39.00 ? 439 ILE A CA 1 ATOM 3397 C C . ILE A 1 439 ? -54.416 45.285 19.024 1.00 39.46 ? 439 ILE A C 1 ATOM 3398 O O . ILE A 1 439 ? -55.110 45.524 18.036 1.00 40.64 ? 439 ILE A O 1 ATOM 3399 C CB . ILE A 1 439 ? -55.621 45.535 21.203 1.00 39.96 ? 439 ILE A CB 1 ATOM 3400 C CG1 . ILE A 1 439 ? -55.655 46.280 22.545 1.00 40.93 ? 439 ILE A CG1 1 ATOM 3401 C CG2 . ILE A 1 439 ? -55.406 44.050 21.429 1.00 39.58 ? 439 ILE A CG2 1 ATOM 3402 C CD1 . ILE A 1 439 ? -56.739 45.803 23.486 1.00 41.61 ? 439 ILE A CD1 1 ATOM 3403 N N . HIS A 1 440 ? -53.517 44.310 19.069 1.00 40.31 ? 440 HIS A N 1 ATOM 3404 C CA . HIS A 1 440 ? -53.427 43.257 18.068 1.00 39.91 ? 440 HIS A CA 1 ATOM 3405 C C . HIS A 1 440 ? -54.826 42.751 17.749 1.00 40.18 ? 440 HIS A C 1 ATOM 3406 O O . HIS A 1 440 ? -55.501 42.201 18.613 1.00 40.79 ? 440 HIS A O 1 ATOM 3407 C CB . HIS A 1 440 ? -52.565 42.130 18.635 1.00 39.80 ? 440 HIS A CB 1 ATOM 3408 C CG . HIS A 1 440 ? -52.211 41.053 17.659 1.00 40.30 ? 440 HIS A CG 1 ATOM 3409 N ND1 . HIS A 1 440 ? -51.315 41.244 16.627 1.00 40.22 ? 440 HIS A ND1 1 ATOM 3410 C CD2 . HIS A 1 440 ? -52.568 39.747 17.610 1.00 40.75 ? 440 HIS A CD2 1 ATOM 3411 C CE1 . HIS A 1 440 ? -51.159 40.109 15.967 1.00 41.09 ? 440 HIS A CE1 1 ATOM 3412 N NE2 . HIS A 1 440 ? -51.904 39.183 16.547 1.00 41.83 ? 440 HIS A NE2 1 ATOM 3413 N N . GLY A 1 441 ? -55.273 42.993 16.521 1.00 40.61 ? 441 GLY A N 1 ATOM 3414 C CA . GLY A 1 441 ? -56.543 42.463 16.043 1.00 40.66 ? 441 GLY A CA 1 ATOM 3415 C C . GLY A 1 441 ? -57.619 43.502 15.845 1.00 41.55 ? 441 GLY A C 1 ATOM 3416 O O . GLY A 1 441 ? -58.602 43.247 15.156 1.00 44.11 ? 441 GLY A O 1 ATOM 3417 N N . TYR A 1 442 ? -57.428 44.688 16.405 1.00 42.41 ? 442 TYR A N 1 ATOM 3418 C CA . TYR A 1 442 ? -58.507 45.665 16.484 1.00 43.77 ? 442 TYR A CA 1 ATOM 3419 C C . TYR A 1 442 ? -58.524 46.702 15.364 1.00 43.61 ? 442 TYR A C 1 ATOM 3420 O O . TYR A 1 442 ? -59.254 47.691 15.431 1.00 46.35 ? 442 TYR A O 1 ATOM 3421 C CB . TYR A 1 442 ? -58.529 46.273 17.895 1.00 45.29 ? 442 TYR A CB 1 ATOM 3422 C CG . TYR A 1 442 ? -59.125 45.258 18.837 1.00 46.22 ? 442 TYR A CG 1 ATOM 3423 C CD1 . TYR A 1 442 ? -58.367 44.198 19.316 1.00 45.81 ? 442 TYR A CD1 1 ATOM 3424 C CD2 . TYR A 1 442 ? -60.472 45.294 19.160 1.00 47.36 ? 442 TYR A CD2 1 ATOM 3425 C CE1 . TYR A 1 442 ? -58.925 43.236 20.141 1.00 46.59 ? 442 TYR A CE1 1 ATOM 3426 C CE2 . TYR A 1 442 ? -61.033 44.334 19.978 1.00 48.08 ? 442 TYR A CE2 1 ATOM 3427 C CZ . TYR A 1 442 ? -60.258 43.309 20.462 1.00 47.08 ? 442 TYR A CZ 1 ATOM 3428 O OH . TYR A 1 442 ? -60.824 42.360 21.274 1.00 49.56 ? 442 TYR A OH 1 ATOM 3429 N N . GLU A 1 443 ? -57.734 46.454 14.328 1.00 42.44 ? 443 GLU A N 1 ATOM 3430 C CA . GLU A 1 443 ? -57.864 47.170 13.064 1.00 43.01 ? 443 GLU A CA 1 ATOM 3431 C C . GLU A 1 443 ? -58.868 46.453 12.146 1.00 42.60 ? 443 GLU A C 1 ATOM 3432 O O . GLU A 1 443 ? -59.389 47.045 11.198 1.00 43.43 ? 443 GLU A O 1 ATOM 3433 C CB . GLU A 1 443 ? -56.491 47.320 12.379 1.00 43.25 ? 443 GLU A CB 1 ATOM 3434 C CG . GLU A 1 443 ? -56.080 46.214 11.399 1.00 42.22 ? 443 GLU A CG 1 ATOM 3435 C CD . GLU A 1 443 ? -55.804 44.868 12.044 1.00 40.93 ? 443 GLU A CD 1 ATOM 3436 O OE1 . GLU A 1 443 ? -55.805 44.761 13.282 1.00 42.08 ? 443 GLU A OE1 1 ATOM 3437 O OE2 . GLU A 1 443 ? -55.591 43.902 11.302 1.00 40.34 ? 443 GLU A OE2 1 ATOM 3438 N N . ILE A 1 444 ? -59.148 45.187 12.451 1.00 42.47 ? 444 ILE A N 1 ATOM 3439 C CA . ILE A 1 444 ? -59.984 44.340 11.602 1.00 42.83 ? 444 ILE A CA 1 ATOM 3440 C C . ILE A 1 444 ? -61.388 44.916 11.471 1.00 44.42 ? 444 ILE A C 1 ATOM 3441 O O . ILE A 1 444 ? -61.920 45.049 10.368 1.00 44.90 ? 444 ILE A O 1 ATOM 3442 C CB . ILE A 1 444 ? -60.089 42.908 12.166 1.00 42.36 ? 444 ILE A CB 1 ATOM 3443 C CG1 . ILE A 1 444 ? -58.726 42.212 12.119 1.00 40.75 ? 444 ILE A CG1 1 ATOM 3444 C CG2 . ILE A 1 444 ? -61.097 42.102 11.360 1.00 43.55 ? 444 ILE A CG2 1 ATOM 3445 C CD1 . ILE A 1 444 ? -58.705 40.852 12.769 1.00 39.84 ? 444 ILE A CD1 1 ATOM 3446 N N . GLU A 1 445 ? -61.981 45.255 12.608 1.00 44.89 ? 445 GLU A N 1 ATOM 3447 C CA . GLU A 1 445 ? -63.312 45.826 12.617 1.00 46.36 ? 445 GLU A CA 1 ATOM 3448 C C . GLU A 1 445 ? -63.416 47.059 11.714 1.00 47.25 ? 445 GLU A C 1 ATOM 3449 O O . GLU A 1 445 ? -64.477 47.304 11.132 1.00 49.01 ? 445 GLU A O 1 ATOM 3450 C CB . GLU A 1 445 ? -63.781 46.117 14.057 1.00 47.88 ? 445 GLU A CB 1 ATOM 3451 C CG . GLU A 1 445 ? -62.901 47.063 14.869 1.00 48.01 ? 445 GLU A CG 1 ATOM 3452 C CD . GLU A 1 445 ? -63.115 46.928 16.366 1.00 46.42 ? 445 GLU A CD 1 ATOM 3453 O OE1 . GLU A 1 445 ? -62.948 45.821 16.904 1.00 44.91 ? 445 GLU A OE1 1 ATOM 3454 O OE2 . GLU A 1 445 ? -63.436 47.936 17.010 1.00 48.03 ? 445 GLU A OE2 1 ATOM 3455 N N . PHE A 1 446 ? -62.326 47.813 11.563 1.00 46.37 ? 446 PHE A N 1 ATOM 3456 C CA . PHE A 1 446 ? -62.321 48.947 10.622 1.00 46.93 ? 446 PHE A CA 1 ATOM 3457 C C . PHE A 1 446 ? -62.240 48.498 9.178 1.00 46.67 ? 446 PHE A C 1 ATOM 3458 O O . PHE A 1 446 ? -62.902 49.056 8.293 1.00 46.66 ? 446 PHE A O 1 ATOM 3459 C CB . PHE A 1 446 ? -61.194 49.914 10.943 1.00 46.21 ? 446 PHE A CB 1 ATOM 3460 C CG . PHE A 1 446 ? -61.477 50.736 12.153 1.00 47.12 ? 446 PHE A CG 1 ATOM 3461 C CD1 . PHE A 1 446 ? -61.223 50.233 13.415 1.00 45.49 ? 446 PHE A CD1 1 ATOM 3462 C CD2 . PHE A 1 446 ? -62.060 51.990 12.030 1.00 48.55 ? 446 PHE A CD2 1 ATOM 3463 C CE1 . PHE A 1 446 ? -61.516 50.983 14.532 1.00 47.13 ? 446 PHE A CE1 1 ATOM 3464 C CE2 . PHE A 1 446 ? -62.359 52.746 13.145 1.00 49.16 ? 446 PHE A CE2 1 ATOM 3465 C CZ . PHE A 1 446 ? -62.088 52.243 14.399 1.00 48.67 ? 446 PHE A CZ 1 ATOM 3466 N N . VAL A 1 447 ? -61.436 47.472 8.951 1.00 45.82 ? 447 VAL A N 1 ATOM 3467 C CA . VAL A 1 447 ? -61.287 46.903 7.619 1.00 47.25 ? 447 VAL A CA 1 ATOM 3468 C C . VAL A 1 447 ? -62.584 46.256 7.114 1.00 48.29 ? 447 VAL A C 1 ATOM 3469 O O . VAL A 1 447 ? -62.799 46.205 5.905 1.00 49.63 ? 447 VAL A O 1 ATOM 3470 C CB . VAL A 1 447 ? -60.111 45.901 7.590 1.00 45.69 ? 447 VAL A CB 1 ATOM 3471 C CG1 . VAL A 1 447 ? -60.153 45.015 6.348 1.00 45.35 ? 447 VAL A CG1 1 ATOM 3472 C CG2 . VAL A 1 447 ? -58.794 46.659 7.683 1.00 44.65 ? 447 VAL A CG2 1 ATOM 3473 N N . PHE A 1 448 ? -63.435 45.775 8.027 1.00 48.21 ? 448 PHE A N 1 ATOM 3474 C CA . PHE A 1 448 ? -64.703 45.128 7.654 1.00 48.84 ? 448 PHE A CA 1 ATOM 3475 C C . PHE A 1 448 ? -65.933 46.048 7.790 1.00 51.84 ? 448 PHE A C 1 ATOM 3476 O O . PHE A 1 448 ? -67.062 45.618 7.545 1.00 53.19 ? 448 PHE A O 1 ATOM 3477 C CB . PHE A 1 448 ? -64.896 43.830 8.451 1.00 47.92 ? 448 PHE A CB 1 ATOM 3478 C CG . PHE A 1 448 ? -64.197 42.639 7.850 1.00 46.88 ? 448 PHE A CG 1 ATOM 3479 C CD1 . PHE A 1 448 ? -62.846 42.434 8.056 1.00 45.85 ? 448 PHE A CD1 1 ATOM 3480 C CD2 . PHE A 1 448 ? -64.899 41.717 7.074 1.00 48.11 ? 448 PHE A CD2 1 ATOM 3481 C CE1 . PHE A 1 448 ? -62.203 41.341 7.492 1.00 46.14 ? 448 PHE A CE1 1 ATOM 3482 C CE2 . PHE A 1 448 ? -64.263 40.621 6.505 1.00 46.42 ? 448 PHE A CE2 1 ATOM 3483 C CZ . PHE A 1 448 ? -62.913 40.437 6.710 1.00 45.88 ? 448 PHE A CZ 1 ATOM 3484 N N . GLY A 1 449 ? -65.725 47.308 8.169 1.00 52.59 ? 449 GLY A N 1 ATOM 3485 C CA . GLY A 1 449 ? -66.794 48.300 8.122 1.00 53.55 ? 449 GLY A CA 1 ATOM 3486 C C . GLY A 1 449 ? -67.730 48.346 9.316 1.00 55.32 ? 449 GLY A C 1 ATOM 3487 O O . GLY A 1 449 ? -68.775 48.994 9.256 1.00 58.41 ? 449 GLY A O 1 ATOM 3488 N N . LEU A 1 450 ? -67.370 47.700 10.417 1.00 54.15 ? 450 LEU A N 1 ATOM 3489 C CA . LEU A 1 450 ? -68.242 47.705 11.595 1.00 55.15 ? 450 LEU A CA 1 ATOM 3490 C C . LEU A 1 450 ? -68.559 49.100 12.115 1.00 55.48 ? 450 LEU A C 1 ATOM 3491 O O . LEU A 1 450 ? -69.618 49.302 12.696 1.00 57.62 ? 450 LEU A O 1 ATOM 3492 C CB . LEU A 1 450 ? -67.678 46.834 12.727 1.00 54.83 ? 450 LEU A CB 1 ATOM 3493 C CG . LEU A 1 450 ? -68.167 45.385 12.672 1.00 55.21 ? 450 LEU A CG 1 ATOM 3494 C CD1 . LEU A 1 450 ? -67.744 44.716 11.371 1.00 54.91 ? 450 LEU A CD1 1 ATOM 3495 C CD2 . LEU A 1 450 ? -67.671 44.605 13.878 1.00 54.88 ? 450 LEU A CD2 1 ATOM 3496 N N . PRO A 1 451 ? -67.651 50.067 11.920 1.00 54.44 ? 451 PRO A N 1 ATOM 3497 C CA . PRO A 1 451 ? -68.016 51.432 12.287 1.00 56.85 ? 451 PRO A CA 1 ATOM 3498 C C . PRO A 1 451 ? -69.168 52.045 11.499 1.00 58.85 ? 451 PRO A C 1 ATOM 3499 O O . PRO A 1 451 ? -69.672 53.088 11.894 1.00 59.81 ? 451 PRO A O 1 ATOM 3500 C CB . PRO A 1 451 ? -66.718 52.205 12.058 1.00 56.04 ? 451 PRO A CB 1 ATOM 3501 C CG . PRO A 1 451 ? -65.680 51.211 12.428 1.00 53.76 ? 451 PRO A CG 1 ATOM 3502 C CD . PRO A 1 451 ? -66.189 49.923 11.827 1.00 53.05 ? 451 PRO A CD 1 ATOM 3503 N N . LEU A 1 452 ? -69.584 51.407 10.409 1.00 60.61 ? 452 LEU A N 1 ATOM 3504 C CA . LEU A 1 452 ? -70.760 51.863 9.660 1.00 64.38 ? 452 LEU A CA 1 ATOM 3505 C C . LEU A 1 452 ? -72.080 51.512 10.353 1.00 65.86 ? 452 LEU A C 1 ATOM 3506 O O . LEU A 1 452 ? -73.065 52.245 10.236 1.00 69.83 ? 452 LEU A O 1 ATOM 3507 C CB . LEU A 1 452 ? -70.746 51.311 8.232 1.00 63.86 ? 452 LEU A CB 1 ATOM 3508 C CG . LEU A 1 452 ? -69.861 52.095 7.265 1.00 63.49 ? 452 LEU A CG 1 ATOM 3509 C CD1 . LEU A 1 452 ? -68.396 52.057 7.685 1.00 61.09 ? 452 LEU A CD1 1 ATOM 3510 C CD2 . LEU A 1 452 ? -70.058 51.552 5.856 1.00 63.95 ? 452 LEU A CD2 1 ATOM 3511 N N . VAL A 1 453 ? -72.087 50.399 11.077 1.00 65.37 ? 453 VAL A N 1 ATOM 3512 C CA . VAL A 1 453 ? -73.263 49.959 11.823 1.00 67.39 ? 453 VAL A CA 1 ATOM 3513 C C . VAL A 1 453 ? -73.463 50.869 13.040 1.00 69.33 ? 453 VAL A C 1 ATOM 3514 O O . VAL A 1 453 ? -72.618 50.939 13.934 1.00 66.44 ? 453 VAL A O 1 ATOM 3515 C CB . VAL A 1 453 ? -73.134 48.483 12.266 1.00 65.48 ? 453 VAL A CB 1 ATOM 3516 C CG1 . VAL A 1 453 ? -74.341 48.053 13.094 1.00 66.86 ? 453 VAL A CG1 1 ATOM 3517 C CG2 . VAL A 1 453 ? -72.963 47.571 11.055 1.00 63.59 ? 453 VAL A CG2 1 ATOM 3518 N N . LYS A 1 454 ? -74.602 51.543 13.073 1.00 73.84 ? 454 LYS A N 1 ATOM 3519 C CA . LYS A 1 454 ? -74.815 52.630 14.021 1.00 78.92 ? 454 LYS A CA 1 ATOM 3520 C C . LYS A 1 454 ? -75.104 52.136 15.443 1.00 79.04 ? 454 LYS A C 1 ATOM 3521 O O . LYS A 1 454 ? -74.699 52.780 16.417 1.00 77.62 ? 454 LYS A O 1 ATOM 3522 C CB . LYS A 1 454 ? -75.911 53.564 13.498 1.00 83.61 ? 454 LYS A CB 1 ATOM 3523 C CG . LYS A 1 454 ? -75.694 53.914 12.027 1.00 86.52 ? 454 LYS A CG 1 ATOM 3524 C CD . LYS A 1 454 ? -76.215 55.288 11.631 1.00 91.16 ? 454 LYS A CD 1 ATOM 3525 C CE . LYS A 1 454 ? -75.607 55.718 10.301 1.00 91.14 ? 454 LYS A CE 1 ATOM 3526 N NZ . LYS A 1 454 ? -76.163 57.010 9.815 1.00 94.13 ? 454 LYS A NZ 1 ATOM 3527 N N . GLU A 1 455 ? -75.757 50.978 15.561 1.00 79.13 ? 455 GLU A N 1 ATOM 3528 C CA . GLU A 1 455 ? -76.020 50.368 16.874 1.00 79.45 ? 455 GLU A CA 1 ATOM 3529 C C . GLU A 1 455 ? -74.755 49.824 17.592 1.00 77.29 ? 455 GLU A C 1 ATOM 3530 O O . GLU A 1 455 ? -74.832 49.449 18.766 1.00 77.70 ? 455 GLU A O 1 ATOM 3531 C CB . GLU A 1 455 ? -77.103 49.275 16.764 1.00 79.70 ? 455 GLU A CB 1 ATOM 3532 C CG . GLU A 1 455 ? -76.692 48.021 16.007 1.00 78.34 ? 455 GLU A CG 1 ATOM 3533 N N . LEU A 1 456 ? -73.604 49.795 16.911 1.00 73.70 ? 456 LEU A N 1 ATOM 3534 C CA . LEU A 1 456 ? -72.347 49.365 17.537 1.00 71.37 ? 456 LEU A CA 1 ATOM 3535 C C . LEU A 1 456 ? -71.598 50.470 18.304 1.00 73.72 ? 456 LEU A C 1 ATOM 3536 O O . LEU A 1 456 ? -70.623 50.177 19.006 1.00 71.88 ? 456 LEU A O 1 ATOM 3537 C CB . LEU A 1 456 ? -71.412 48.723 16.504 1.00 69.22 ? 456 LEU A CB 1 ATOM 3538 C CG . LEU A 1 456 ? -71.830 47.359 15.937 1.00 68.20 ? 456 LEU A CG 1 ATOM 3539 C CD1 . LEU A 1 456 ? -70.790 46.883 14.933 1.00 66.16 ? 456 LEU A CD1 1 ATOM 3540 C CD2 . LEU A 1 456 ? -72.040 46.311 17.025 1.00 67.21 ? 456 LEU A CD2 1 ATOM 3541 N N . ASN A 1 457 ? -72.043 51.723 18.167 1.00 77.88 ? 457 ASN A N 1 ATOM 3542 C CA . ASN A 1 457 ? -71.579 52.849 19.013 1.00 79.33 ? 457 ASN A CA 1 ATOM 3543 C C . ASN A 1 457 ? -70.197 53.449 18.665 1.00 73.53 ? 457 ASN A C 1 ATOM 3544 O O . ASN A 1 457 ? -69.530 54.004 19.547 1.00 72.48 ? 457 ASN A O 1 ATOM 3545 C CB . ASN A 1 457 ? -71.592 52.474 20.519 1.00 84.17 ? 457 ASN A CB 1 ATOM 3546 C CG . ASN A 1 457 ? -72.987 52.167 21.064 1.00 91.26 ? 457 ASN A CG 1 ATOM 3547 O OD1 . ASN A 1 457 ? -74.007 52.455 20.429 1.00 93.47 ? 457 ASN A OD1 1 ATOM 3548 N ND2 . ASN A 1 457 ? -73.023 51.576 22.283 1.00 97.58 ? 457 ASN A ND2 1 ATOM 3549 N N . TYR A 1 458 ? -69.765 53.358 17.406 1.00 67.26 ? 458 TYR A N 1 ATOM 3550 C CA . TYR A 1 458 ? -68.546 54.061 16.974 1.00 63.02 ? 458 TYR A CA 1 ATOM 3551 C C . TYR A 1 458 ? -68.868 55.528 16.712 1.00 63.38 ? 458 TYR A C 1 ATOM 3552 O O . TYR A 1 458 ? -70.031 55.887 16.553 1.00 64.86 ? 458 TYR A O 1 ATOM 3553 C CB . TYR A 1 458 ? -67.959 53.438 15.707 1.00 60.58 ? 458 TYR A CB 1 ATOM 3554 C CG . TYR A 1 458 ? -67.414 52.040 15.885 1.00 56.97 ? 458 TYR A CG 1 ATOM 3555 C CD1 . TYR A 1 458 ? -66.092 51.830 16.259 1.00 55.05 ? 458 TYR A CD1 1 ATOM 3556 C CD2 . TYR A 1 458 ? -68.218 50.928 15.666 1.00 55.97 ? 458 TYR A CD2 1 ATOM 3557 C CE1 . TYR A 1 458 ? -65.584 50.552 16.421 1.00 52.69 ? 458 TYR A CE1 1 ATOM 3558 C CE2 . TYR A 1 458 ? -67.723 49.648 15.815 1.00 54.30 ? 458 TYR A CE2 1 ATOM 3559 C CZ . TYR A 1 458 ? -66.402 49.465 16.199 1.00 52.81 ? 458 TYR A CZ 1 ATOM 3560 O OH . TYR A 1 458 ? -65.906 48.192 16.347 1.00 51.22 ? 458 TYR A OH 1 ATOM 3561 N N . THR A 1 459 ? -67.844 56.375 16.668 1.00 62.10 ? 459 THR A N 1 ATOM 3562 C CA . THR A 1 459 ? -68.034 57.800 16.370 1.00 63.77 ? 459 THR A CA 1 ATOM 3563 C C . THR A 1 459 ? -68.207 58.011 14.870 1.00 64.27 ? 459 THR A C 1 ATOM 3564 O O . THR A 1 459 ? -68.023 57.083 14.089 1.00 64.15 ? 459 THR A O 1 ATOM 3565 C CB . THR A 1 459 ? -66.841 58.648 16.849 1.00 62.90 ? 459 THR A CB 1 ATOM 3566 O OG1 . THR A 1 459 ? -65.635 58.175 16.240 1.00 60.51 ? 459 THR A OG1 1 ATOM 3567 C CG2 . THR A 1 459 ? -66.705 58.566 18.349 1.00 62.65 ? 459 THR A CG2 1 ATOM 3568 N N . ALA A 1 460 ? -68.560 59.231 14.475 1.00 66.28 ? 460 ALA A N 1 ATOM 3569 C CA . ALA A 1 460 ? -68.618 59.608 13.060 1.00 66.01 ? 460 ALA A CA 1 ATOM 3570 C C . ALA A 1 460 ? -67.222 59.573 12.431 1.00 64.28 ? 460 ALA A C 1 ATOM 3571 O O . ALA A 1 460 ? -67.039 59.020 11.347 1.00 62.15 ? 460 ALA A O 1 ATOM 3572 C CB . ALA A 1 460 ? -69.225 60.990 12.907 1.00 68.03 ? 460 ALA A CB 1 ATOM 3573 N N . GLU A 1 461 ? -66.244 60.150 13.129 1.00 64.59 ? 461 GLU A N 1 ATOM 3574 C CA . GLU A 1 461 ? -64.844 60.141 12.691 1.00 64.12 ? 461 GLU A CA 1 ATOM 3575 C C . GLU A 1 461 ? -64.346 58.709 12.446 1.00 61.17 ? 461 GLU A C 1 ATOM 3576 O O . GLU A 1 461 ? -63.512 58.470 11.568 1.00 60.05 ? 461 GLU A O 1 ATOM 3577 C CB . GLU A 1 461 ? -63.938 60.825 13.731 1.00 65.88 ? 461 GLU A CB 1 ATOM 3578 C CG . GLU A 1 461 ? -64.031 62.350 13.808 1.00 70.34 ? 461 GLU A CG 1 ATOM 3579 C CD . GLU A 1 461 ? -65.213 62.878 14.632 1.00 75.30 ? 461 GLU A CD 1 ATOM 3580 O OE1 . GLU A 1 461 ? -65.864 62.092 15.367 1.00 76.02 ? 461 GLU A OE1 1 ATOM 3581 O OE2 . GLU A 1 461 ? -65.502 64.100 14.542 1.00 79.54 ? 461 GLU A OE2 1 ATOM 3582 N N . GLU A 1 462 ? -64.858 57.769 13.238 1.00 59.60 ? 462 GLU A N 1 ATOM 3583 C CA . GLU A 1 462 ? -64.524 56.358 13.101 1.00 57.22 ? 462 GLU A CA 1 ATOM 3584 C C . GLU A 1 462 ? -65.193 55.704 11.887 1.00 57.36 ? 462 GLU A C 1 ATOM 3585 O O . GLU A 1 462 ? -64.575 54.881 11.200 1.00 56.31 ? 462 GLU A O 1 ATOM 3586 C CB . GLU A 1 462 ? -64.860 55.610 14.399 1.00 57.18 ? 462 GLU A CB 1 ATOM 3587 C CG . GLU A 1 462 ? -63.777 55.795 15.463 1.00 56.99 ? 462 GLU A CG 1 ATOM 3588 C CD . GLU A 1 462 ? -64.172 55.343 16.860 1.00 57.22 ? 462 GLU A CD 1 ATOM 3589 O OE1 . GLU A 1 462 ? -65.366 55.073 17.109 1.00 59.46 ? 462 GLU A OE1 1 ATOM 3590 O OE2 . GLU A 1 462 ? -63.272 55.270 17.726 1.00 56.05 ? 462 GLU A OE2 1 ATOM 3591 N N . GLU A 1 463 ? -66.446 56.062 11.617 1.00 58.63 ? 463 GLU A N 1 ATOM 3592 C CA . GLU A 1 463 ? -67.106 55.611 10.398 1.00 58.25 ? 463 GLU A CA 1 ATOM 3593 C C . GLU A 1 463 ? -66.284 56.061 9.202 1.00 57.05 ? 463 GLU A C 1 ATOM 3594 O O . GLU A 1 463 ? -66.049 55.287 8.276 1.00 55.78 ? 463 GLU A O 1 ATOM 3595 C CB . GLU A 1 463 ? -68.536 56.168 10.274 1.00 61.72 ? 463 GLU A CB 1 ATOM 3596 C CG . GLU A 1 463 ? -69.321 55.527 9.123 1.00 62.85 ? 463 GLU A CG 1 ATOM 3597 C CD . GLU A 1 463 ? -70.698 56.128 8.871 1.00 65.04 ? 463 GLU A CD 1 ATOM 3598 O OE1 . GLU A 1 463 ? -71.312 56.689 9.804 1.00 66.11 ? 463 GLU A OE1 1 ATOM 3599 O OE2 . GLU A 1 463 ? -71.176 56.014 7.720 1.00 65.36 ? 463 GLU A OE2 1 ATOM 3600 N N . ALA A 1 464 ? -65.852 57.317 9.235 1.00 57.57 ? 464 ALA A N 1 ATOM 3601 C CA . ALA A 1 464 ? -65.079 57.897 8.145 1.00 57.83 ? 464 ALA A CA 1 ATOM 3602 C C . ALA A 1 464 ? -63.766 57.146 7.934 1.00 56.66 ? 464 ALA A C 1 ATOM 3603 O O . ALA A 1 464 ? -63.380 56.865 6.795 1.00 56.34 ? 464 ALA A O 1 ATOM 3604 C CB . ALA A 1 464 ? -64.811 59.367 8.419 1.00 58.77 ? 464 ALA A CB 1 ATOM 3605 N N . LEU A 1 465 ? -63.092 56.828 9.038 1.00 55.42 ? 465 LEU A N 1 ATOM 3606 C CA . LEU A 1 465 ? -61.836 56.087 8.991 1.00 54.62 ? 465 LEU A CA 1 ATOM 3607 C C . LEU A 1 465 ? -62.038 54.701 8.401 1.00 53.52 ? 465 LEU A C 1 ATOM 3608 O O . LEU A 1 465 ? -61.225 54.231 7.599 1.00 54.58 ? 465 LEU A O 1 ATOM 3609 C CB . LEU A 1 465 ? -61.241 55.946 10.393 1.00 53.99 ? 465 LEU A CB 1 ATOM 3610 C CG . LEU A 1 465 ? -59.938 55.154 10.498 1.00 51.70 ? 465 LEU A CG 1 ATOM 3611 C CD1 . LEU A 1 465 ? -58.839 55.846 9.713 1.00 51.71 ? 465 LEU A CD1 1 ATOM 3612 C CD2 . LEU A 1 465 ? -59.538 54.973 11.956 1.00 51.78 ? 465 LEU A CD2 1 ATOM 3613 N N . SER A 1 466 ? -63.112 54.038 8.805 1.00 52.56 ? 466 SER A N 1 ATOM 3614 C CA . SER A 1 466 ? -63.406 52.729 8.260 1.00 51.08 ? 466 SER A CA 1 ATOM 3615 C C . SER A 1 466 ? -63.627 52.825 6.756 1.00 52.20 ? 466 SER A C 1 ATOM 3616 O O . SER A 1 466 ? -63.157 51.967 6.019 1.00 52.58 ? 466 SER A O 1 ATOM 3617 C CB . SER A 1 466 ? -64.625 52.111 8.938 1.00 50.84 ? 466 SER A CB 1 ATOM 3618 O OG . SER A 1 466 ? -64.772 50.763 8.531 1.00 50.06 ? 466 SER A OG 1 ATOM 3619 N N . ARG A 1 467 ? -64.325 53.867 6.302 1.00 53.04 ? 467 ARG A N 1 ATOM 3620 C CA . ARG A 1 467 ? -64.619 54.020 4.877 1.00 54.05 ? 467 ARG A CA 1 ATOM 3621 C C . ARG A 1 467 ? -63.342 54.262 4.073 1.00 53.33 ? 467 ARG A C 1 ATOM 3622 O O . ARG A 1 467 ? -63.186 53.714 2.989 1.00 53.00 ? 467 ARG A O 1 ATOM 3623 C CB . ARG A 1 467 ? -65.632 55.146 4.637 1.00 56.76 ? 467 ARG A CB 1 ATOM 3624 C CG . ARG A 1 467 ? -67.041 54.853 5.153 1.00 57.72 ? 467 ARG A CG 1 ATOM 3625 C CD . ARG A 1 467 ? -68.054 55.916 4.717 1.00 60.18 ? 467 ARG A CD 1 ATOM 3626 N NE . ARG A 1 467 ? -69.432 55.594 5.116 1.00 61.15 ? 467 ARG A NE 1 ATOM 3627 C CZ . ARG A 1 467 ? -70.224 54.702 4.513 1.00 60.79 ? 467 ARG A CZ 1 ATOM 3628 N NH1 . ARG A 1 467 ? -69.803 53.996 3.462 1.00 59.95 ? 467 ARG A NH1 1 ATOM 3629 N NH2 . ARG A 1 467 ? -71.453 54.500 4.971 1.00 61.21 ? 467 ARG A NH2 1 ATOM 3630 N N . ARG A 1 468 ? -62.443 55.084 4.615 1.00 53.55 ? 468 ARG A N 1 ATOM 3631 C CA . ARG A 1 468 ? -61.122 55.323 4.021 1.00 53.69 ? 468 ARG A CA 1 ATOM 3632 C C . ARG A 1 468 ? -60.357 54.040 3.867 1.00 51.07 ? 468 ARG A C 1 ATOM 3633 O O . ARG A 1 468 ? -59.728 53.809 2.845 1.00 51.57 ? 468 ARG A O 1 ATOM 3634 C CB . ARG A 1 468 ? -60.265 56.224 4.913 1.00 55.79 ? 468 ARG A CB 1 ATOM 3635 C CG . ARG A 1 468 ? -60.246 57.694 4.550 1.00 59.46 ? 468 ARG A CG 1 ATOM 3636 C CD . ARG A 1 468 ? -59.386 58.458 5.546 1.00 62.13 ? 468 ARG A CD 1 ATOM 3637 N NE . ARG A 1 468 ? -57.952 58.247 5.315 1.00 63.02 ? 468 ARG A NE 1 ATOM 3638 C CZ . ARG A 1 468 ? -57.002 58.252 6.258 1.00 63.80 ? 468 ARG A CZ 1 ATOM 3639 N NH1 . ARG A 1 468 ? -57.300 58.433 7.546 1.00 63.42 ? 468 ARG A NH1 1 ATOM 3640 N NH2 . ARG A 1 468 ? -55.731 58.057 5.906 1.00 64.07 ? 468 ARG A NH2 1 ATOM 3641 N N . ILE A 1 469 ? -60.381 53.232 4.921 1.00 48.59 ? 469 ILE A N 1 ATOM 3642 C CA . ILE A 1 469 ? -59.620 52.000 4.962 1.00 46.19 ? 469 ILE A CA 1 ATOM 3643 C C . ILE A 1 469 ? -60.187 50.971 4.007 1.00 46.75 ? 469 ILE A C 1 ATOM 3644 O O . ILE A 1 469 ? -59.449 50.371 3.232 1.00 45.79 ? 469 ILE A O 1 ATOM 3645 C CB . ILE A 1 469 ? -59.565 51.435 6.387 1.00 44.17 ? 469 ILE A CB 1 ATOM 3646 C CG1 . ILE A 1 469 ? -58.563 52.262 7.200 1.00 44.21 ? 469 ILE A CG1 1 ATOM 3647 C CG2 . ILE A 1 469 ? -59.188 49.956 6.376 1.00 42.10 ? 469 ILE A CG2 1 ATOM 3648 C CD1 . ILE A 1 469 ? -58.431 51.868 8.656 1.00 43.20 ? 469 ILE A CD1 1 ATOM 3649 N N . MET A 1 470 ? -61.495 50.767 4.060 1.00 48.73 ? 470 MET A N 1 ATOM 3650 C CA . MET A 1 470 ? -62.140 49.832 3.144 1.00 49.95 ? 470 MET A CA 1 ATOM 3651 C C . MET A 1 470 ? -61.864 50.233 1.715 1.00 50.36 ? 470 MET A C 1 ATOM 3652 O O . MET A 1 470 ? -61.636 49.379 0.866 1.00 50.51 ? 470 MET A O 1 ATOM 3653 C CB . MET A 1 470 ? -63.648 49.803 3.349 1.00 51.80 ? 470 MET A CB 1 ATOM 3654 C CG . MET A 1 470 ? -64.078 49.168 4.651 1.00 51.70 ? 470 MET A CG 1 ATOM 3655 S SD . MET A 1 470 ? -65.742 49.705 5.026 1.00 55.44 ? 470 MET A SD 1 ATOM 3656 C CE . MET A 1 470 ? -66.644 48.428 4.164 1.00 55.69 ? 470 MET A CE 1 ATOM 3657 N N . HIS A 1 471 ? -61.880 51.532 1.447 1.00 51.88 ? 471 HIS A N 1 ATOM 3658 C CA . HIS A 1 471 ? -61.696 51.980 0.086 1.00 53.57 ? 471 HIS A CA 1 ATOM 3659 C C . HIS A 1 471 ? -60.258 51.777 -0.350 1.00 52.67 ? 471 HIS A C 1 ATOM 3660 O O . HIS A 1 471 ? -60.019 51.338 -1.463 1.00 54.03 ? 471 HIS A O 1 ATOM 3661 C CB . HIS A 1 471 ? -62.149 53.420 -0.127 1.00 56.05 ? 471 HIS A CB 1 ATOM 3662 C CG . HIS A 1 471 ? -62.366 53.746 -1.567 1.00 58.32 ? 471 HIS A CG 1 ATOM 3663 N ND1 . HIS A 1 471 ? -63.286 53.074 -2.346 1.00 59.35 ? 471 HIS A ND1 1 ATOM 3664 C CD2 . HIS A 1 471 ? -61.746 54.621 -2.391 1.00 59.49 ? 471 HIS A CD2 1 ATOM 3665 C CE1 . HIS A 1 471 ? -63.243 53.540 -3.580 1.00 59.99 ? 471 HIS A CE1 1 ATOM 3666 N NE2 . HIS A 1 471 ? -62.317 54.479 -3.634 1.00 61.38 ? 471 HIS A NE2 1 ATOM 3667 N N . TYR A 1 472 ? -59.310 52.090 0.527 1.00 52.30 ? 472 TYR A N 1 ATOM 3668 C CA . TYR A 1 472 ? -57.911 51.747 0.294 1.00 50.75 ? 472 TYR A CA 1 ATOM 3669 C C . TYR A 1 472 ? -57.780 50.266 -0.042 1.00 49.39 ? 472 TYR A C 1 ATOM 3670 O O . TYR A 1 472 ? -57.219 49.892 -1.070 1.00 51.58 ? 472 TYR A O 1 ATOM 3671 C CB . TYR A 1 472 ? -57.065 51.997 1.541 1.00 49.64 ? 472 TYR A CB 1 ATOM 3672 C CG . TYR A 1 472 ? -56.717 53.423 1.868 1.00 51.76 ? 472 TYR A CG 1 ATOM 3673 C CD1 . TYR A 1 472 ? -56.508 54.378 0.869 1.00 53.42 ? 472 TYR A CD1 1 ATOM 3674 C CD2 . TYR A 1 472 ? -56.532 53.810 3.197 1.00 52.11 ? 472 TYR A CD2 1 ATOM 3675 C CE1 . TYR A 1 472 ? -56.155 55.678 1.188 1.00 53.50 ? 472 TYR A CE1 1 ATOM 3676 C CE2 . TYR A 1 472 ? -56.184 55.108 3.521 1.00 52.56 ? 472 TYR A CE2 1 ATOM 3677 C CZ . TYR A 1 472 ? -55.998 56.031 2.513 1.00 53.98 ? 472 TYR A CZ 1 ATOM 3678 O OH . TYR A 1 472 ? -55.648 57.309 2.838 1.00 56.71 ? 472 TYR A OH 1 ATOM 3679 N N . TRP A 1 473 ? -58.292 49.422 0.842 1.00 47.34 ? 473 TRP A N 1 ATOM 3680 C CA . TRP A 1 473 ? -58.099 47.982 0.708 1.00 45.57 ? 473 TRP A CA 1 ATOM 3681 C C . TRP A 1 473 ? -58.667 47.531 -0.645 1.00 45.90 ? 473 TRP A C 1 ATOM 3682 O O . TRP A 1 473 ? -57.980 46.876 -1.430 1.00 45.54 ? 473 TRP A O 1 ATOM 3683 C CB . TRP A 1 473 ? -58.766 47.227 1.866 1.00 43.93 ? 473 TRP A CB 1 ATOM 3684 C CG . TRP A 1 473 ? -57.886 46.890 3.038 1.00 42.61 ? 473 TRP A CG 1 ATOM 3685 C CD1 . TRP A 1 473 ? -57.779 45.668 3.636 1.00 41.95 ? 473 TRP A CD1 1 ATOM 3686 C CD2 . TRP A 1 473 ? -57.012 47.765 3.772 1.00 42.80 ? 473 TRP A CD2 1 ATOM 3687 N NE1 . TRP A 1 473 ? -56.893 45.720 4.683 1.00 40.94 ? 473 TRP A NE1 1 ATOM 3688 C CE2 . TRP A 1 473 ? -56.408 46.996 4.790 1.00 41.69 ? 473 TRP A CE2 1 ATOM 3689 C CE3 . TRP A 1 473 ? -56.665 49.115 3.659 1.00 44.00 ? 473 TRP A CE3 1 ATOM 3690 C CZ2 . TRP A 1 473 ? -55.477 47.534 5.689 1.00 41.61 ? 473 TRP A CZ2 1 ATOM 3691 C CZ3 . TRP A 1 473 ? -55.738 49.648 4.552 1.00 43.58 ? 473 TRP A CZ3 1 ATOM 3692 C CH2 . TRP A 1 473 ? -55.157 48.859 5.553 1.00 42.33 ? 473 TRP A CH2 1 ATOM 3693 N N . ALA A 1 474 ? -59.906 47.926 -0.920 1.00 45.81 ? 474 ALA A N 1 ATOM 3694 C CA . ALA A 1 474 ? -60.586 47.547 -2.161 1.00 46.53 ? 474 ALA A CA 1 ATOM 3695 C C . ALA A 1 474 ? -59.898 48.104 -3.403 1.00 46.81 ? 474 ALA A C 1 ATOM 3696 O O . ALA A 1 474 ? -59.613 47.376 -4.345 1.00 45.60 ? 474 ALA A O 1 ATOM 3697 C CB . ALA A 1 474 ? -62.032 48.011 -2.121 1.00 47.81 ? 474 ALA A CB 1 ATOM 3698 N N . THR A 1 475 ? -59.642 49.405 -3.390 1.00 48.06 ? 475 THR A N 1 ATOM 3699 C CA . THR A 1 475 ? -59.009 50.077 -4.510 1.00 49.66 ? 475 THR A CA 1 ATOM 3700 C C . THR A 1 475 ? -57.638 49.471 -4.808 1.00 49.59 ? 475 THR A C 1 ATOM 3701 O O . THR A 1 475 ? -57.248 49.356 -5.976 1.00 50.46 ? 475 THR A O 1 ATOM 3702 C CB . THR A 1 475 ? -58.871 51.584 -4.227 1.00 50.87 ? 475 THR A CB 1 ATOM 3703 O OG1 . THR A 1 475 ? -60.171 52.143 -3.992 1.00 51.02 ? 475 THR A OG1 1 ATOM 3704 C CG2 . THR A 1 475 ? -58.208 52.309 -5.394 1.00 52.28 ? 475 THR A CG2 1 ATOM 3705 N N . PHE A 1 476 ? -56.913 49.084 -3.761 1.00 48.23 ? 476 PHE A N 1 ATOM 3706 C CA . PHE A 1 476 ? -55.639 48.395 -3.935 1.00 47.99 ? 476 PHE A CA 1 ATOM 3707 C C . PHE A 1 476 ? -55.846 46.993 -4.517 1.00 47.46 ? 476 PHE A C 1 ATOM 3708 O O . PHE A 1 476 ? -55.122 46.587 -5.422 1.00 48.57 ? 476 PHE A O 1 ATOM 3709 C CB . PHE A 1 476 ? -54.872 48.310 -2.612 1.00 47.72 ? 476 PHE A CB 1 ATOM 3710 C CG . PHE A 1 476 ? -53.670 47.397 -2.666 1.00 47.42 ? 476 PHE A CG 1 ATOM 3711 C CD1 . PHE A 1 476 ? -52.449 47.858 -3.148 1.00 47.80 ? 476 PHE A CD1 1 ATOM 3712 C CD2 . PHE A 1 476 ? -53.762 46.073 -2.249 1.00 45.83 ? 476 PHE A CD2 1 ATOM 3713 C CE1 . PHE A 1 476 ? -51.347 47.020 -3.207 1.00 46.60 ? 476 PHE A CE1 1 ATOM 3714 C CE2 . PHE A 1 476 ? -52.664 45.234 -2.312 1.00 44.82 ? 476 PHE A CE2 1 ATOM 3715 C CZ . PHE A 1 476 ? -51.456 45.706 -2.792 1.00 45.16 ? 476 PHE A CZ 1 ATOM 3716 N N . ALA A 1 477 ? -56.825 46.254 -4.003 1.00 46.72 ? 477 ALA A N 1 ATOM 3717 C CA . ALA A 1 477 ? -57.151 44.932 -4.548 1.00 46.80 ? 477 ALA A CA 1 ATOM 3718 C C . ALA A 1 477 ? -57.409 44.986 -6.050 1.00 48.92 ? 477 ALA A C 1 ATOM 3719 O O . ALA A 1 477 ? -57.040 44.071 -6.798 1.00 48.08 ? 477 ALA A O 1 ATOM 3720 C CB . ALA A 1 477 ? -58.373 44.357 -3.853 1.00 46.54 ? 477 ALA A CB 1 ATOM 3721 N N . LYS A 1 478 ? -58.068 46.064 -6.457 1.00 51.13 ? 478 LYS A N 1 ATOM 3722 C CA . LYS A 1 478 ? -58.500 46.267 -7.816 1.00 53.93 ? 478 LYS A CA 1 ATOM 3723 C C . LYS A 1 478 ? -57.383 46.727 -8.760 1.00 54.15 ? 478 LYS A C 1 ATOM 3724 O O . LYS A 1 478 ? -57.369 46.336 -9.925 1.00 55.04 ? 478 LYS A O 1 ATOM 3725 C CB . LYS A 1 478 ? -59.631 47.299 -7.826 1.00 57.94 ? 478 LYS A CB 1 ATOM 3726 C CG . LYS A 1 478 ? -60.189 47.551 -9.214 1.00 63.00 ? 478 LYS A CG 1 ATOM 3727 C CD . LYS A 1 478 ? -61.410 48.451 -9.223 1.00 66.22 ? 478 LYS A CD 1 ATOM 3728 C CE . LYS A 1 478 ? -61.990 48.503 -10.632 1.00 69.43 ? 478 LYS A CE 1 ATOM 3729 N NZ . LYS A 1 478 ? -62.556 49.837 -10.955 1.00 72.20 ? 478 LYS A NZ 1 ATOM 3730 N N . THR A 1 479 ? -56.472 47.564 -8.266 1.00 52.67 ? 479 THR A N 1 ATOM 3731 C CA . THR A 1 479 ? -55.498 48.251 -9.121 1.00 52.58 ? 479 THR A CA 1 ATOM 3732 C C . THR A 1 479 ? -54.028 48.092 -8.743 1.00 51.18 ? 479 THR A C 1 ATOM 3733 O O . THR A 1 479 ? -53.155 48.448 -9.528 1.00 52.22 ? 479 THR A O 1 ATOM 3734 C CB . THR A 1 479 ? -55.748 49.769 -9.098 1.00 54.12 ? 479 THR A CB 1 ATOM 3735 O OG1 . THR A 1 479 ? -55.453 50.278 -7.788 1.00 53.26 ? 479 THR A OG1 1 ATOM 3736 C CG2 . THR A 1 479 ? -57.188 50.091 -9.463 1.00 54.82 ? 479 THR A CG2 1 ATOM 3737 N N . GLY A 1 480 ? -53.739 47.609 -7.542 1.00 49.24 ? 480 GLY A N 1 ATOM 3738 C CA . GLY A 1 480 ? -52.360 47.585 -7.046 1.00 48.45 ? 480 GLY A CA 1 ATOM 3739 C C . GLY A 1 480 ? -51.938 48.893 -6.408 1.00 48.76 ? 480 GLY A C 1 ATOM 3740 O O . GLY A 1 480 ? -50.779 49.056 -6.018 1.00 46.97 ? 480 GLY A O 1 ATOM 3741 N N . ASN A 1 481 ? -52.889 49.821 -6.297 1.00 50.15 ? 481 ASN A N 1 ATOM 3742 C CA . ASN A 1 481 ? -52.667 51.115 -5.664 1.00 51.20 ? 481 ASN A CA 1 ATOM 3743 C C . ASN A 1 481 ? -53.904 51.500 -4.829 1.00 51.68 ? 481 ASN A C 1 ATOM 3744 O O . ASN A 1 481 ? -55.012 51.550 -5.361 1.00 52.87 ? 481 ASN A O 1 ATOM 3745 C CB . ASN A 1 481 ? -52.386 52.169 -6.737 1.00 52.62 ? 481 ASN A CB 1 ATOM 3746 C CG . ASN A 1 481 ? -51.976 53.503 -6.152 1.00 53.64 ? 481 ASN A CG 1 ATOM 3747 O OD1 . ASN A 1 481 ? -52.338 53.841 -5.031 1.00 53.84 ? 481 ASN A OD1 1 ATOM 3748 N ND2 . ASN A 1 481 ? -51.223 54.273 -6.915 1.00 54.93 ? 481 ASN A ND2 1 ATOM 3749 N N . PRO A 1 482 ? -53.724 51.767 -3.519 1.00 51.21 ? 482 PRO A N 1 ATOM 3750 C CA . PRO A 1 482 ? -54.870 52.134 -2.676 1.00 51.53 ? 482 PRO A CA 1 ATOM 3751 C C . PRO A 1 482 ? -55.442 53.532 -2.954 1.00 53.44 ? 482 PRO A C 1 ATOM 3752 O O . PRO A 1 482 ? -56.562 53.828 -2.537 1.00 53.27 ? 482 PRO A O 1 ATOM 3753 C CB . PRO A 1 482 ? -54.287 52.083 -1.265 1.00 50.10 ? 482 PRO A CB 1 ATOM 3754 C CG . PRO A 1 482 ? -52.847 52.416 -1.449 1.00 50.63 ? 482 PRO A CG 1 ATOM 3755 C CD . PRO A 1 482 ? -52.459 51.791 -2.758 1.00 50.71 ? 482 PRO A CD 1 ATOM 3756 N N . ASN A 1 483 ? -54.679 54.377 -3.646 1.00 55.23 ? 483 ASN A N 1 ATOM 3757 C CA . ASN A 1 483 ? -55.114 55.731 -3.973 1.00 57.31 ? 483 ASN A CA 1 ATOM 3758 C C . ASN A 1 483 ? -56.001 55.786 -5.196 1.00 61.03 ? 483 ASN A C 1 ATOM 3759 O O . ASN A 1 483 ? -55.731 55.146 -6.211 1.00 60.09 ? 483 ASN A O 1 ATOM 3760 C CB . ASN A 1 483 ? -53.916 56.631 -4.207 1.00 56.74 ? 483 ASN A CB 1 ATOM 3761 C CG . ASN A 1 483 ? -53.049 56.742 -2.987 1.00 55.11 ? 483 ASN A CG 1 ATOM 3762 O OD1 . ASN A 1 483 ? -53.460 57.301 -1.973 1.00 54.16 ? 483 ASN A OD1 1 ATOM 3763 N ND2 . ASN A 1 483 ? -51.845 56.199 -3.067 1.00 54.09 ? 483 ASN A ND2 1 ATOM 3764 N N . GLU A 1 484 ? -57.067 56.564 -5.083 1.00 66.14 ? 484 GLU A N 1 ATOM 3765 C CA . GLU A 1 484 ? -57.903 56.860 -6.218 1.00 71.80 ? 484 GLU A CA 1 ATOM 3766 C C . GLU A 1 484 ? -57.212 57.979 -7.019 1.00 75.64 ? 484 GLU A C 1 ATOM 3767 O O . GLU A 1 484 ? -56.779 58.983 -6.440 1.00 74.11 ? 484 GLU A O 1 ATOM 3768 C CB . GLU A 1 484 ? -59.299 57.261 -5.751 1.00 73.48 ? 484 GLU A CB 1 ATOM 3769 C CG . GLU A 1 484 ? -60.358 57.149 -6.832 1.00 76.74 ? 484 GLU A CG 1 ATOM 3770 C CD . GLU A 1 484 ? -61.604 56.466 -6.333 1.00 77.31 ? 484 GLU A CD 1 ATOM 3771 O OE1 . GLU A 1 484 ? -62.651 57.135 -6.194 1.00 82.94 ? 484 GLU A OE1 1 ATOM 3772 O OE2 . GLU A 1 484 ? -61.523 55.254 -6.060 1.00 75.00 ? 484 GLU A OE2 1 ATOM 3773 N N . PRO A 1 485 ? -57.074 57.789 -8.347 1.00 79.79 ? 485 PRO A N 1 ATOM 3774 C CA . PRO A 1 485 ? -56.333 58.724 -9.213 1.00 83.45 ? 485 PRO A CA 1 ATOM 3775 C C . PRO A 1 485 ? -56.595 60.237 -9.046 1.00 87.38 ? 485 PRO A C 1 ATOM 3776 O O . PRO A 1 485 ? -55.657 61.025 -9.193 1.00 89.14 ? 485 PRO A O 1 ATOM 3777 C CB . PRO A 1 485 ? -56.722 58.261 -10.618 1.00 83.08 ? 485 PRO A CB 1 ATOM 3778 C CG . PRO A 1 485 ? -56.919 56.785 -10.470 1.00 80.36 ? 485 PRO A CG 1 ATOM 3779 C CD . PRO A 1 485 ? -57.448 56.557 -9.077 1.00 78.05 ? 485 PRO A CD 1 ATOM 3780 N N . HIS A 1 486 ? -57.829 60.641 -8.739 1.00 90.51 ? 486 HIS A N 1 ATOM 3781 C CA . HIS A 1 486 ? -58.182 62.079 -8.695 1.00 94.82 ? 486 HIS A CA 1 ATOM 3782 C C . HIS A 1 486 ? -58.179 62.705 -7.288 1.00 93.58 ? 486 HIS A C 1 ATOM 3783 O O . HIS A 1 486 ? -57.738 63.841 -7.121 1.00 95.75 ? 486 HIS A O 1 ATOM 3784 C CB . HIS A 1 486 ? -59.529 62.312 -9.367 1.00 96.70 ? 486 HIS A CB 1 ATOM 3785 N N . SER A 1 487 ? -58.679 61.965 -6.300 1.00 89.85 ? 487 SER A N 1 ATOM 3786 C CA . SER A 1 487 ? -58.831 62.440 -4.912 1.00 89.00 ? 487 SER A CA 1 ATOM 3787 C C . SER A 1 487 ? -58.025 63.694 -4.521 1.00 89.98 ? 487 SER A C 1 ATOM 3788 O O . SER A 1 487 ? -56.815 63.779 -4.742 1.00 88.07 ? 487 SER A O 1 ATOM 3789 C CB . SER A 1 487 ? -58.521 61.303 -3.935 1.00 84.15 ? 487 SER A CB 1 ATOM 3790 N N . GLN A 1 488 ? -58.720 64.663 -3.928 1.00 92.82 ? 488 GLN A N 1 ATOM 3791 C CA . GLN A 1 488 ? -58.077 65.805 -3.272 1.00 93.89 ? 488 GLN A CA 1 ATOM 3792 C C . GLN A 1 488 ? -57.291 65.331 -2.054 1.00 89.07 ? 488 GLN A C 1 ATOM 3793 O O . GLN A 1 488 ? -56.341 65.981 -1.627 1.00 87.89 ? 488 GLN A O 1 ATOM 3794 C CB . GLN A 1 488 ? -59.121 66.841 -2.856 1.00 95.97 ? 488 GLN A CB 1 ATOM 3795 N N . GLU A 1 489 ? -57.710 64.200 -1.492 1.00 86.88 ? 489 GLU A N 1 ATOM 3796 C CA . GLU A 1 489 ? -57.020 63.586 -0.370 1.00 83.36 ? 489 GLU A CA 1 ATOM 3797 C C . GLU A 1 489 ? -55.560 63.297 -0.732 1.00 81.68 ? 489 GLU A C 1 ATOM 3798 O O . GLU A 1 489 ? -55.254 62.903 -1.862 1.00 78.81 ? 489 GLU A O 1 ATOM 3799 C CB . GLU A 1 489 ? -57.739 62.310 0.050 1.00 79.77 ? 489 GLU A CB 1 ATOM 3800 N N . SER A 1 490 ? -54.670 63.509 0.237 1.00 80.81 ? 490 SER A N 1 ATOM 3801 C CA . SER A 1 490 ? -53.236 63.282 0.058 1.00 79.08 ? 490 SER A CA 1 ATOM 3802 C C . SER A 1 490 ? -52.913 61.821 -0.290 1.00 74.81 ? 490 SER A C 1 ATOM 3803 O O . SER A 1 490 ? -53.562 60.892 0.195 1.00 71.24 ? 490 SER A O 1 ATOM 3804 C CB . SER A 1 490 ? -52.463 63.708 1.316 1.00 79.27 ? 490 SER A CB 1 ATOM 3805 O OG . SER A 1 490 ? -52.480 65.120 1.477 1.00 82.07 ? 490 SER A OG 1 ATOM 3806 N N . LYS A 1 491 ? -51.906 61.642 -1.141 1.00 72.17 ? 491 LYS A N 1 ATOM 3807 C CA . LYS A 1 491 ? -51.515 60.329 -1.623 1.00 68.01 ? 491 LYS A CA 1 ATOM 3808 C C . LYS A 1 491 ? -50.803 59.564 -0.507 1.00 64.87 ? 491 LYS A C 1 ATOM 3809 O O . LYS A 1 491 ? -49.946 60.116 0.182 1.00 67.21 ? 491 LYS A O 1 ATOM 3810 C CB . LYS A 1 491 ? -50.593 60.454 -2.850 1.00 68.29 ? 491 LYS A CB 1 ATOM 3811 C CG . LYS A 1 491 ? -51.227 61.083 -4.086 1.00 70.07 ? 491 LYS A CG 1 ATOM 3812 N N . TRP A 1 492 ? -51.201 58.310 -0.314 1.00 59.67 ? 492 TRP A N 1 ATOM 3813 C CA . TRP A 1 492 ? -50.448 57.339 0.468 1.00 56.00 ? 492 TRP A CA 1 ATOM 3814 C C . TRP A 1 492 ? -49.260 56.939 -0.398 1.00 56.72 ? 492 TRP A C 1 ATOM 3815 O O . TRP A 1 492 ? -49.434 56.259 -1.405 1.00 57.39 ? 492 TRP A O 1 ATOM 3816 C CB . TRP A 1 492 ? -51.343 56.123 0.744 1.00 53.64 ? 492 TRP A CB 1 ATOM 3817 C CG . TRP A 1 492 ? -50.743 54.973 1.546 1.00 49.41 ? 492 TRP A CG 1 ATOM 3818 C CD1 . TRP A 1 492 ? -49.433 54.753 1.836 1.00 48.82 ? 492 TRP A CD1 1 ATOM 3819 C CD2 . TRP A 1 492 ? -51.461 53.874 2.104 1.00 45.75 ? 492 TRP A CD2 1 ATOM 3820 N NE1 . TRP A 1 492 ? -49.293 53.601 2.558 1.00 45.98 ? 492 TRP A NE1 1 ATOM 3821 C CE2 . TRP A 1 492 ? -50.525 53.039 2.734 1.00 44.08 ? 492 TRP A CE2 1 ATOM 3822 C CE3 . TRP A 1 492 ? -52.812 53.527 2.148 1.00 45.75 ? 492 TRP A CE3 1 ATOM 3823 C CZ2 . TRP A 1 492 ? -50.888 51.875 3.394 1.00 42.41 ? 492 TRP A CZ2 1 ATOM 3824 C CZ3 . TRP A 1 492 ? -53.177 52.371 2.803 1.00 44.20 ? 492 TRP A CZ3 1 ATOM 3825 C CH2 . TRP A 1 492 ? -52.215 51.554 3.422 1.00 42.54 ? 492 TRP A CH2 1 ATOM 3826 N N . PRO A 1 493 ? -48.045 57.355 -0.022 1.00 57.29 ? 493 PRO A N 1 ATOM 3827 C CA . PRO A 1 493 ? -46.922 57.129 -0.927 1.00 57.57 ? 493 PRO A CA 1 ATOM 3828 C C . PRO A 1 493 ? -46.452 55.685 -0.956 1.00 55.27 ? 493 PRO A C 1 ATOM 3829 O O . PRO A 1 493 ? -46.705 54.934 -0.019 1.00 55.42 ? 493 PRO A O 1 ATOM 3830 C CB . PRO A 1 493 ? -45.827 58.025 -0.349 1.00 58.57 ? 493 PRO A CB 1 ATOM 3831 C CG . PRO A 1 493 ? -46.112 58.050 1.105 1.00 58.26 ? 493 PRO A CG 1 ATOM 3832 C CD . PRO A 1 493 ? -47.608 57.930 1.260 1.00 57.52 ? 493 PRO A CD 1 ATOM 3833 N N . LEU A 1 494 ? -45.779 55.312 -2.039 1.00 55.99 ? 494 LEU A N 1 ATOM 3834 C CA . LEU A 1 494 ? -45.090 54.030 -2.127 1.00 54.77 ? 494 LEU A CA 1 ATOM 3835 C C . LEU A 1 494 ? -43.995 53.954 -1.085 1.00 54.39 ? 494 LEU A C 1 ATOM 3836 O O . LEU A 1 494 ? -43.346 54.957 -0.777 1.00 55.33 ? 494 LEU A O 1 ATOM 3837 C CB . LEU A 1 494 ? -44.435 53.831 -3.502 1.00 55.40 ? 494 LEU A CB 1 ATOM 3838 C CG . LEU A 1 494 ? -45.248 53.199 -4.628 1.00 55.85 ? 494 LEU A CG 1 ATOM 3839 C CD1 . LEU A 1 494 ? -44.555 53.436 -5.959 1.00 58.57 ? 494 LEU A CD1 1 ATOM 3840 C CD2 . LEU A 1 494 ? -45.457 51.712 -4.407 1.00 53.97 ? 494 LEU A CD2 1 ATOM 3841 N N . PHE A 1 495 ? -43.797 52.750 -0.561 1.00 53.73 ? 495 PHE A N 1 ATOM 3842 C CA . PHE A 1 495 ? -42.652 52.442 0.276 1.00 55.05 ? 495 PHE A CA 1 ATOM 3843 C C . PHE A 1 495 ? -41.507 52.069 -0.657 1.00 56.28 ? 495 PHE A C 1 ATOM 3844 O O . PHE A 1 495 ? -41.616 51.104 -1.416 1.00 54.31 ? 495 PHE A O 1 ATOM 3845 C CB . PHE A 1 495 ? -42.976 51.284 1.224 1.00 53.03 ? 495 PHE A CB 1 ATOM 3846 C CG . PHE A 1 495 ? -41.819 50.845 2.074 1.00 52.54 ? 495 PHE A CG 1 ATOM 3847 C CD1 . PHE A 1 495 ? -40.882 49.946 1.585 1.00 52.58 ? 495 PHE A CD1 1 ATOM 3848 C CD2 . PHE A 1 495 ? -41.679 51.311 3.370 1.00 53.58 ? 495 PHE A CD2 1 ATOM 3849 C CE1 . PHE A 1 495 ? -39.812 49.538 2.364 1.00 53.08 ? 495 PHE A CE1 1 ATOM 3850 C CE2 . PHE A 1 495 ? -40.621 50.895 4.164 1.00 54.10 ? 495 PHE A CE2 1 ATOM 3851 C CZ . PHE A 1 495 ? -39.681 50.015 3.657 1.00 54.17 ? 495 PHE A CZ 1 ATOM 3852 N N . THR A 1 496 ? -40.427 52.844 -0.602 1.00 58.82 ? 496 THR A N 1 ATOM 3853 C CA . THR A 1 496 ? -39.222 52.566 -1.374 1.00 60.83 ? 496 THR A CA 1 ATOM 3854 C C . THR A 1 496 ? -38.124 52.166 -0.416 1.00 60.40 ? 496 THR A C 1 ATOM 3855 O O . THR A 1 496 ? -38.148 52.552 0.745 1.00 60.20 ? 496 THR A O 1 ATOM 3856 C CB . THR A 1 496 ? -38.738 53.806 -2.150 1.00 63.23 ? 496 THR A CB 1 ATOM 3857 O OG1 . THR A 1 496 ? -38.236 54.788 -1.233 1.00 65.77 ? 496 THR A OG1 1 ATOM 3858 C CG2 . THR A 1 496 ? -39.861 54.407 -2.958 1.00 63.39 ? 496 THR A CG2 1 ATOM 3859 N N . THR A 1 497 ? -37.154 51.403 -0.911 1.00 62.04 ? 497 THR A N 1 ATOM 3860 C CA . THR A 1 497 ? -35.971 51.045 -0.131 1.00 61.60 ? 497 THR A CA 1 ATOM 3861 C C . THR A 1 497 ? -35.293 52.305 0.384 1.00 62.55 ? 497 THR A C 1 ATOM 3862 O O . THR A 1 497 ? -34.870 52.373 1.534 1.00 59.58 ? 497 THR A O 1 ATOM 3863 C CB . THR A 1 497 ? -34.938 50.279 -0.986 1.00 62.61 ? 497 THR A CB 1 ATOM 3864 O OG1 . THR A 1 497 ? -35.593 49.255 -1.744 1.00 63.96 ? 497 THR A OG1 1 ATOM 3865 C CG2 . THR A 1 497 ? -33.864 49.656 -0.108 1.00 62.79 ? 497 THR A CG2 1 ATOM 3866 N N . LYS A 1 498 ? -35.215 53.300 -0.493 1.00 65.38 ? 498 LYS A N 1 ATOM 3867 C CA . LYS A 1 498 ? -34.439 54.497 -0.253 1.00 67.85 ? 498 LYS A CA 1 ATOM 3868 C C . LYS A 1 498 ? -35.048 55.401 0.817 1.00 66.95 ? 498 LYS A C 1 ATOM 3869 O O . LYS A 1 498 ? -34.343 55.839 1.724 1.00 65.29 ? 498 LYS A O 1 ATOM 3870 C CB . LYS A 1 498 ? -34.297 55.262 -1.566 1.00 71.45 ? 498 LYS A CB 1 ATOM 3871 C CG . LYS A 1 498 ? -33.377 56.464 -1.484 1.00 76.00 ? 498 LYS A CG 1 ATOM 3872 C CD . LYS A 1 498 ? -33.538 57.343 -2.708 1.00 80.15 ? 498 LYS A CD 1 ATOM 3873 C CE . LYS A 1 498 ? -33.427 58.814 -2.349 1.00 82.57 ? 498 LYS A CE 1 ATOM 3874 N NZ . LYS A 1 498 ? -33.557 59.644 -3.575 1.00 85.24 ? 498 LYS A NZ 1 ATOM 3875 N N . GLU A 1 499 ? -36.346 55.679 0.698 1.00 66.62 ? 499 GLU A N 1 ATOM 3876 C CA . GLU A 1 499 ? -37.028 56.649 1.564 1.00 66.65 ? 499 GLU A CA 1 ATOM 3877 C C . GLU A 1 499 ? -37.905 56.011 2.644 1.00 62.50 ? 499 GLU A C 1 ATOM 3878 O O . GLU A 1 499 ? -38.134 56.610 3.687 1.00 63.30 ? 499 GLU A O 1 ATOM 3879 C CB . GLU A 1 499 ? -37.860 57.603 0.713 1.00 70.47 ? 499 GLU A CB 1 ATOM 3880 C CG . GLU A 1 499 ? -37.036 58.488 -0.215 1.00 75.41 ? 499 GLU A CG 1 ATOM 3881 C CD . GLU A 1 499 ? -37.701 58.688 -1.570 1.00 80.85 ? 499 GLU A CD 1 ATOM 3882 O OE1 . GLU A 1 499 ? -38.050 57.680 -2.243 1.00 80.46 ? 499 GLU A OE1 1 ATOM 3883 O OE2 . GLU A 1 499 ? -37.868 59.860 -1.968 1.00 85.39 ? 499 GLU A OE2 1 ATOM 3884 N N . GLN A 1 500 ? -38.410 54.811 2.385 1.00 59.33 ? 500 GLN A N 1 ATOM 3885 C CA . GLN A 1 500 ? -39.060 53.980 3.414 1.00 57.09 ? 500 GLN A CA 1 ATOM 3886 C C . GLN A 1 500 ? -40.274 54.612 4.082 1.00 55.38 ? 500 GLN A C 1 ATOM 3887 O O . GLN A 1 500 ? -40.462 54.519 5.293 1.00 55.39 ? 500 GLN A O 1 ATOM 3888 C CB . GLN A 1 500 ? -38.037 53.549 4.463 1.00 57.91 ? 500 GLN A CB 1 ATOM 3889 C CG . GLN A 1 500 ? -36.867 52.801 3.850 1.00 58.92 ? 500 GLN A CG 1 ATOM 3890 C CD . GLN A 1 500 ? -36.089 52.011 4.864 1.00 58.00 ? 500 GLN A CD 1 ATOM 3891 O OE1 . GLN A 1 500 ? -36.639 51.150 5.551 1.00 60.42 ? 500 GLN A OE1 1 ATOM 3892 N NE2 . GLN A 1 500 ? -34.806 52.293 4.964 1.00 58.47 ? 500 GLN A NE2 1 ATOM 3893 N N . LYS A 1 501 ? -41.119 55.212 3.260 1.00 55.71 ? 501 LYS A N 1 ATOM 3894 C CA . LYS A 1 501 ? -42.260 55.971 3.732 1.00 54.83 ? 501 LYS A CA 1 ATOM 3895 C C . LYS A 1 501 ? -43.434 55.083 4.129 1.00 51.81 ? 501 LYS A C 1 ATOM 3896 O O . LYS A 1 501 ? -43.706 54.063 3.497 1.00 51.85 ? 501 LYS A O 1 ATOM 3897 C CB . LYS A 1 501 ? -42.695 56.956 2.645 1.00 57.80 ? 501 LYS A CB 1 ATOM 3898 C CG . LYS A 1 501 ? -41.614 57.967 2.280 1.00 60.20 ? 501 LYS A CG 1 ATOM 3899 C CD . LYS A 1 501 ? -42.062 58.951 1.205 1.00 61.86 ? 501 LYS A CD 1 ATOM 3900 C CE . LYS A 1 501 ? -41.270 60.250 1.296 1.00 63.96 ? 501 LYS A CE 1 ATOM 3901 N NZ . LYS A 1 501 ? -40.950 60.822 -0.034 1.00 65.86 ? 501 LYS A NZ 1 ATOM 3902 N N . PHE A 1 502 ? -44.130 55.485 5.183 1.00 50.88 ? 502 PHE A N 1 ATOM 3903 C CA . PHE A 1 502 ? -45.386 54.855 5.563 1.00 49.43 ? 502 PHE A CA 1 ATOM 3904 C C . PHE A 1 502 ? -46.341 55.907 6.077 1.00 49.72 ? 502 PHE A C 1 ATOM 3905 O O . PHE A 1 502 ? -45.960 57.061 6.216 1.00 51.54 ? 502 PHE A O 1 ATOM 3906 C CB . PHE A 1 502 ? -45.154 53.792 6.623 1.00 48.52 ? 502 PHE A CB 1 ATOM 3907 C CG . PHE A 1 502 ? -44.701 54.334 7.948 1.00 48.40 ? 502 PHE A CG 1 ATOM 3908 C CD1 . PHE A 1 502 ? -43.367 54.658 8.164 1.00 49.81 ? 502 PHE A CD1 1 ATOM 3909 C CD2 . PHE A 1 502 ? -45.595 54.486 8.988 1.00 48.12 ? 502 PHE A CD2 1 ATOM 3910 C CE1 . PHE A 1 502 ? -42.939 55.137 9.394 1.00 49.85 ? 502 PHE A CE1 1 ATOM 3911 C CE2 . PHE A 1 502 ? -45.176 54.965 10.215 1.00 49.11 ? 502 PHE A CE2 1 ATOM 3912 C CZ . PHE A 1 502 ? -43.845 55.292 10.421 1.00 49.25 ? 502 PHE A CZ 1 ATOM 3913 N N . ILE A 1 503 ? -47.581 55.512 6.347 1.00 49.97 ? 503 ILE A N 1 ATOM 3914 C CA . ILE A 1 503 ? -48.595 56.444 6.859 1.00 51.83 ? 503 ILE A CA 1 ATOM 3915 C C . ILE A 1 503 ? -49.192 55.970 8.170 1.00 50.34 ? 503 ILE A C 1 ATOM 3916 O O . ILE A 1 503 ? -49.286 54.771 8.427 1.00 49.74 ? 503 ILE A O 1 ATOM 3917 C CB . ILE A 1 503 ? -49.747 56.693 5.845 1.00 53.67 ? 503 ILE A CB 1 ATOM 3918 C CG1 . ILE A 1 503 ? -50.535 55.416 5.532 1.00 53.12 ? 503 ILE A CG1 1 ATOM 3919 C CG2 . ILE A 1 503 ? -49.215 57.273 4.545 1.00 55.23 ? 503 ILE A CG2 1 ATOM 3920 C CD1 . ILE A 1 503 ? -51.849 55.699 4.832 1.00 54.23 ? 503 ILE A CD1 1 ATOM 3921 N N . ASP A 1 504 ? -49.587 56.919 9.006 1.00 52.19 ? 504 ASP A N 1 ATOM 3922 C CA . ASP A 1 504 ? -50.420 56.598 10.153 1.00 52.35 ? 504 ASP A CA 1 ATOM 3923 C C . ASP A 1 504 ? -51.839 56.392 9.618 1.00 52.16 ? 504 ASP A C 1 ATOM 3924 O O . ASP A 1 504 ? -52.282 57.133 8.738 1.00 52.15 ? 504 ASP A O 1 ATOM 3925 C CB . ASP A 1 504 ? -50.403 57.730 11.195 1.00 53.99 ? 504 ASP A CB 1 ATOM 3926 C CG . ASP A 1 504 ? -49.041 57.893 11.898 1.00 54.24 ? 504 ASP A CG 1 ATOM 3927 O OD1 . ASP A 1 504 ? -48.257 56.918 11.976 1.00 54.05 ? 504 ASP A OD1 1 ATOM 3928 O OD2 . ASP A 1 504 ? -48.761 59.008 12.397 1.00 54.30 ? 504 ASP A OD2 1 ATOM 3929 N N . LEU A 1 505 ? -52.534 55.376 10.125 1.00 50.88 ? 505 LEU A N 1 ATOM 3930 C CA . LEU A 1 505 ? -53.974 55.230 9.891 1.00 51.01 ? 505 LEU A CA 1 ATOM 3931 C C . LEU A 1 505 ? -54.749 55.589 11.155 1.00 51.84 ? 505 LEU A C 1 ATOM 3932 O O . LEU A 1 505 ? -54.768 54.827 12.120 1.00 50.72 ? 505 LEU A O 1 ATOM 3933 C CB . LEU A 1 505 ? -54.319 53.804 9.473 1.00 50.36 ? 505 LEU A CB 1 ATOM 3934 C CG . LEU A 1 505 ? -54.043 53.444 8.016 1.00 51.05 ? 505 LEU A CG 1 ATOM 3935 C CD1 . LEU A 1 505 ? -54.488 52.018 7.747 1.00 49.80 ? 505 LEU A CD1 1 ATOM 3936 C CD2 . LEU A 1 505 ? -54.743 54.402 7.062 1.00 53.16 ? 505 LEU A CD2 1 ATOM 3937 N N . ASN A 1 506 ? -55.384 56.756 11.145 1.00 53.98 ? 506 ASN A N 1 ATOM 3938 C CA . ASN A 1 506 ? -56.173 57.217 12.279 1.00 54.84 ? 506 ASN A CA 1 ATOM 3939 C C . ASN A 1 506 ? -57.152 58.291 11.849 1.00 56.32 ? 506 ASN A C 1 ATOM 3940 O O . ASN A 1 506 ? -57.272 58.562 10.669 1.00 57.69 ? 506 ASN A O 1 ATOM 3941 C CB . ASN A 1 506 ? -55.244 57.719 13.388 1.00 56.41 ? 506 ASN A CB 1 ATOM 3942 C CG . ASN A 1 506 ? -54.335 58.847 12.938 1.00 58.19 ? 506 ASN A CG 1 ATOM 3943 O OD1 . ASN A 1 506 ? -54.746 59.752 12.205 1.00 59.85 ? 506 ASN A OD1 1 ATOM 3944 N ND2 . ASN A 1 506 ? -53.085 58.806 13.398 1.00 57.59 ? 506 ASN A ND2 1 ATOM 3945 N N . THR A 1 507 ? -57.850 58.905 12.797 1.00 58.44 ? 507 THR A N 1 ATOM 3946 C CA . THR A 1 507 ? -58.840 59.934 12.471 1.00 60.84 ? 507 THR A CA 1 ATOM 3947 C C . THR A 1 507 ? -58.230 61.313 12.168 1.00 63.43 ? 507 THR A C 1 ATOM 3948 O O . THR A 1 507 ? -58.925 62.186 11.664 1.00 64.74 ? 507 THR A O 1 ATOM 3949 C CB . THR A 1 507 ? -59.883 60.080 13.599 1.00 61.59 ? 507 THR A CB 1 ATOM 3950 O OG1 . THR A 1 507 ? -59.250 60.563 14.791 1.00 61.19 ? 507 THR A OG1 1 ATOM 3951 C CG2 . THR A 1 507 ? -60.564 58.739 13.882 1.00 59.97 ? 507 THR A CG2 1 ATOM 3952 N N . GLU A 1 508 ? -56.950 61.516 12.484 1.00 65.09 ? 508 GLU A N 1 ATOM 3953 C CA . GLU A 1 508 ? -56.259 62.774 12.164 1.00 67.81 ? 508 GLU A CA 1 ATOM 3954 C C . GLU A 1 508 ? -55.905 62.855 10.660 1.00 69.48 ? 508 GLU A C 1 ATOM 3955 O O . GLU A 1 508 ? -55.748 61.827 9.995 1.00 65.55 ? 508 GLU A O 1 ATOM 3956 C CB . GLU A 1 508 ? -55.003 62.924 13.035 1.00 66.60 ? 508 GLU A CB 1 ATOM 3957 N N . PRO A 1 509 ? -55.795 64.081 10.110 1.00 75.57 ? 509 PRO A N 1 ATOM 3958 C CA . PRO A 1 509 ? -55.477 64.169 8.681 1.00 76.92 ? 509 PRO A CA 1 ATOM 3959 C C . PRO A 1 509 ? -54.131 63.519 8.390 1.00 76.43 ? 509 PRO A C 1 ATOM 3960 O O . PRO A 1 509 ? -53.167 63.735 9.123 1.00 75.27 ? 509 PRO A O 1 ATOM 3961 C CB . PRO A 1 509 ? -55.447 65.678 8.400 1.00 79.06 ? 509 PRO A CB 1 ATOM 3962 C CG . PRO A 1 509 ? -55.275 66.331 9.730 1.00 79.92 ? 509 PRO A CG 1 ATOM 3963 C CD . PRO A 1 509 ? -55.896 65.411 10.742 1.00 78.45 ? 509 PRO A CD 1 ATOM 3964 N N . MET A 1 510 ? -54.091 62.725 7.327 1.00 78.96 ? 510 MET A N 1 ATOM 3965 C CA . MET A 1 510 ? -52.955 61.854 7.020 1.00 78.43 ? 510 MET A CA 1 ATOM 3966 C C . MET A 1 510 ? -51.603 62.550 7.171 1.00 77.18 ? 510 MET A C 1 ATOM 3967 O O . MET A 1 510 ? -51.357 63.575 6.538 1.00 77.87 ? 510 MET A O 1 ATOM 3968 C CB . MET A 1 510 ? -53.087 61.305 5.595 1.00 79.89 ? 510 MET A CB 1 ATOM 3969 C CG . MET A 1 510 ? -52.217 60.091 5.319 1.00 79.84 ? 510 MET A CG 1 ATOM 3970 S SD . MET A 1 510 ? -52.208 59.648 3.571 1.00 81.48 ? 510 MET A SD 1 ATOM 3971 C CE . MET A 1 510 ? -51.162 60.942 2.909 1.00 85.45 ? 510 MET A CE 1 ATOM 3972 N N . LYS A 1 511 ? -50.755 61.990 8.039 1.00 75.12 ? 511 LYS A N 1 ATOM 3973 C CA . LYS A 1 511 ? -49.336 62.356 8.134 1.00 72.21 ? 511 LYS A CA 1 ATOM 3974 C C . LYS A 1 511 ? -48.493 61.176 7.628 1.00 68.63 ? 511 LYS A C 1 ATOM 3975 O O . LYS A 1 511 ? -48.802 60.010 7.898 1.00 66.59 ? 511 LYS A O 1 ATOM 3976 C CB . LYS A 1 511 ? -48.946 62.726 9.573 1.00 69.43 ? 511 LYS A CB 1 ATOM 3977 N N . VAL A 1 512 ? -47.445 61.496 6.874 1.00 66.98 ? 512 VAL A N 1 ATOM 3978 C CA . VAL A 1 512 ? -46.523 60.513 6.322 1.00 63.44 ? 512 VAL A CA 1 ATOM 3979 C C . VAL A 1 512 ? -45.258 60.509 7.160 1.00 61.73 ? 512 VAL A C 1 ATOM 3980 O O . VAL A 1 512 ? -44.776 61.561 7.569 1.00 63.61 ? 512 VAL A O 1 ATOM 3981 C CB . VAL A 1 512 ? -46.147 60.875 4.871 1.00 65.41 ? 512 VAL A CB 1 ATOM 3982 C CG1 . VAL A 1 512 ? -45.043 59.963 4.339 1.00 64.64 ? 512 VAL A CG1 1 ATOM 3983 C CG2 . VAL A 1 512 ? -47.381 60.838 3.972 1.00 65.49 ? 512 VAL A CG2 1 ATOM 3984 N N . HIS A 1 513 ? -44.711 59.324 7.390 1.00 59.08 ? 513 HIS A N 1 ATOM 3985 C CA . HIS A 1 513 ? -43.508 59.156 8.194 1.00 57.65 ? 513 HIS A CA 1 ATOM 3986 C C . HIS A 1 513 ? -42.500 58.317 7.424 1.00 55.61 ? 513 HIS A C 1 ATOM 3987 O O . HIS A 1 513 ? -42.776 57.898 6.314 1.00 55.57 ? 513 HIS A O 1 ATOM 3988 C CB . HIS A 1 513 ? -43.875 58.469 9.509 1.00 57.40 ? 513 HIS A CB 1 ATOM 3989 C CG . HIS A 1 513 ? -44.766 59.285 10.399 1.00 58.51 ? 513 HIS A CG 1 ATOM 3990 N ND1 . HIS A 1 513 ? -44.367 60.475 10.971 1.00 60.48 ? 513 HIS A ND1 1 ATOM 3991 C CD2 . HIS A 1 513 ? -46.027 59.063 10.835 1.00 57.80 ? 513 HIS A CD2 1 ATOM 3992 C CE1 . HIS A 1 513 ? -45.351 60.957 11.709 1.00 61.09 ? 513 HIS A CE1 1 ATOM 3993 N NE2 . HIS A 1 513 ? -46.369 60.119 11.643 1.00 59.29 ? 513 HIS A NE2 1 ATOM 3994 N N . GLN A 1 514 ? -41.331 58.079 8.009 1.00 56.20 ? 514 GLN A N 1 ATOM 3995 C CA . GLN A 1 514 ? -40.297 57.249 7.381 1.00 55.70 ? 514 GLN A CA 1 ATOM 3996 C C . GLN A 1 514 ? -39.672 56.310 8.394 1.00 54.01 ? 514 GLN A C 1 ATOM 3997 O O . GLN A 1 514 ? -39.679 56.572 9.591 1.00 54.22 ? 514 GLN A O 1 ATOM 3998 C CB . GLN A 1 514 ? -39.192 58.114 6.771 1.00 57.41 ? 514 GLN A CB 1 ATOM 3999 C CG . GLN A 1 514 ? -39.644 58.946 5.591 1.00 59.69 ? 514 GLN A CG 1 ATOM 4000 C CD . GLN A 1 514 ? -38.567 59.897 5.095 1.00 62.49 ? 514 GLN A CD 1 ATOM 4001 O OE1 . GLN A 1 514 ? -38.633 61.100 5.333 1.00 63.23 ? 514 GLN A OE1 1 ATOM 4002 N NE2 . GLN A 1 514 ? -37.570 59.360 4.400 1.00 62.55 ? 514 GLN A NE2 1 ATOM 4003 N N . ARG A 1 515 ? -39.133 55.210 7.892 1.00 54.21 ? 515 ARG A N 1 ATOM 4004 C CA . ARG A 1 515 ? -38.355 54.277 8.690 1.00 53.59 ? 515 ARG A CA 1 ATOM 4005 C C . ARG A 1 515 ? -39.038 53.856 9.987 1.00 52.09 ? 515 ARG A C 1 ATOM 4006 O O . ARG A 1 515 ? -38.568 54.167 11.074 1.00 51.71 ? 515 ARG A O 1 ATOM 4007 C CB . ARG A 1 515 ? -36.996 54.881 8.974 1.00 56.06 ? 515 ARG A CB 1 ATOM 4008 C CG . ARG A 1 515 ? -36.252 55.224 7.705 1.00 59.56 ? 515 ARG A CG 1 ATOM 4009 C CD . ARG A 1 515 ? -34.796 55.571 7.955 1.00 62.26 ? 515 ARG A CD 1 ATOM 4010 N NE . ARG A 1 515 ? -34.035 55.348 6.728 1.00 65.62 ? 515 ARG A NE 1 ATOM 4011 C CZ . ARG A 1 515 ? -34.008 56.175 5.680 1.00 67.89 ? 515 ARG A CZ 1 ATOM 4012 N NH1 . ARG A 1 515 ? -34.691 57.320 5.687 1.00 68.27 ? 515 ARG A NH1 1 ATOM 4013 N NH2 . ARG A 1 515 ? -33.281 55.854 4.614 1.00 69.56 ? 515 ARG A NH2 1 ATOM 4014 N N . LEU A 1 516 ? -40.149 53.141 9.849 1.00 50.73 ? 516 LEU A N 1 ATOM 4015 C CA . LEU A 1 516 ? -40.905 52.653 10.988 1.00 49.72 ? 516 LEU A CA 1 ATOM 4016 C C . LEU A 1 516 ? -40.026 51.792 11.886 1.00 50.12 ? 516 LEU A C 1 ATOM 4017 O O . LEU A 1 516 ? -39.646 50.679 11.507 1.00 50.94 ? 516 LEU A O 1 ATOM 4018 C CB . LEU A 1 516 ? -42.120 51.850 10.509 1.00 49.51 ? 516 LEU A CB 1 ATOM 4019 C CG . LEU A 1 516 ? -42.967 51.101 11.544 1.00 48.80 ? 516 LEU A CG 1 ATOM 4020 C CD1 . LEU A 1 516 ? -43.518 52.052 12.580 1.00 50.46 ? 516 LEU A CD1 1 ATOM 4021 C CD2 . LEU A 1 516 ? -44.107 50.361 10.872 1.00 48.17 ? 516 LEU A CD2 1 ATOM 4022 N N . ARG A 1 517 ? -39.706 52.333 13.064 1.00 51.09 ? 517 ARG A N 1 ATOM 4023 C CA . ARG A 1 517 ? -38.916 51.663 14.106 1.00 50.69 ? 517 ARG A CA 1 ATOM 4024 C C . ARG A 1 517 ? -37.605 51.070 13.651 1.00 49.49 ? 517 ARG A C 1 ATOM 4025 O O . ARG A 1 517 ? -37.300 49.938 13.993 1.00 47.12 ? 517 ARG A O 1 ATOM 4026 C CB . ARG A 1 517 ? -39.713 50.541 14.730 1.00 52.57 ? 517 ARG A CB 1 ATOM 4027 C CG . ARG A 1 517 ? -41.128 50.908 15.071 1.00 55.67 ? 517 ARG A CG 1 ATOM 4028 C CD . ARG A 1 517 ? -41.690 49.820 15.947 1.00 57.38 ? 517 ARG A CD 1 ATOM 4029 N NE . ARG A 1 517 ? -41.256 50.017 17.315 1.00 58.47 ? 517 ARG A NE 1 ATOM 4030 C CZ . ARG A 1 517 ? -41.847 50.847 18.158 1.00 60.93 ? 517 ARG A CZ 1 ATOM 4031 N NH1 . ARG A 1 517 ? -42.900 51.553 17.753 1.00 60.82 ? 517 ARG A NH1 1 ATOM 4032 N NH2 . ARG A 1 517 ? -41.383 50.966 19.404 1.00 62.46 ? 517 ARG A NH2 1 ATOM 4033 N N . VAL A 1 518 ? -36.843 51.818 12.869 1.00 51.10 ? 518 VAL A N 1 ATOM 4034 C CA . VAL A 1 518 ? -35.516 51.368 12.466 1.00 52.03 ? 518 VAL A CA 1 ATOM 4035 C C . VAL A 1 518 ? -34.649 50.942 13.640 1.00 52.55 ? 518 VAL A C 1 ATOM 4036 O O . VAL A 1 518 ? -34.110 49.848 13.628 1.00 53.88 ? 518 VAL A O 1 ATOM 4037 C CB . VAL A 1 518 ? -34.717 52.435 11.691 1.00 53.24 ? 518 VAL A CB 1 ATOM 4038 C CG1 . VAL A 1 518 ? -34.762 52.150 10.204 1.00 53.46 ? 518 VAL A CG1 1 ATOM 4039 C CG2 . VAL A 1 518 ? -35.179 53.849 12.031 1.00 54.03 ? 518 VAL A CG2 1 ATOM 4040 N N . GLN A 1 519 ? -34.501 51.803 14.639 1.00 54.45 ? 519 GLN A N 1 ATOM 4041 C CA . GLN A 1 519 ? -33.515 51.559 15.689 1.00 58.70 ? 519 GLN A CA 1 ATOM 4042 C C . GLN A 1 519 ? -33.798 50.252 16.406 1.00 55.14 ? 519 GLN A C 1 ATOM 4043 O O . GLN A 1 519 ? -32.928 49.396 16.513 1.00 55.96 ? 519 GLN A O 1 ATOM 4044 C CB . GLN A 1 519 ? -33.459 52.713 16.696 1.00 64.69 ? 519 GLN A CB 1 ATOM 4045 C CG . GLN A 1 519 ? -32.547 52.429 17.884 1.00 69.97 ? 519 GLN A CG 1 ATOM 4046 C CD . GLN A 1 519 ? -32.130 53.681 18.639 1.00 77.01 ? 519 GLN A CD 1 ATOM 4047 O OE1 . GLN A 1 519 ? -32.463 53.855 19.816 1.00 79.53 ? 519 GLN A OE1 1 ATOM 4048 N NE2 . GLN A 1 519 ? -31.391 54.561 17.965 1.00 81.27 ? 519 GLN A NE2 1 ATOM 4049 N N . MET A 1 520 ? -35.023 50.099 16.884 1.00 51.64 ? 520 MET A N 1 ATOM 4050 C CA . MET A 1 520 ? -35.399 48.881 17.572 1.00 49.90 ? 520 MET A CA 1 ATOM 4051 C C . MET A 1 520 ? -35.309 47.667 16.659 1.00 46.77 ? 520 MET A C 1 ATOM 4052 O O . MET A 1 520 ? -34.862 46.616 17.091 1.00 46.65 ? 520 MET A O 1 ATOM 4053 C CB . MET A 1 520 ? -36.802 49.010 18.169 1.00 50.88 ? 520 MET A CB 1 ATOM 4054 C CG . MET A 1 520 ? -36.883 49.988 19.334 1.00 53.81 ? 520 MET A CG 1 ATOM 4055 S SD . MET A 1 520 ? -35.809 49.564 20.734 1.00 56.41 ? 520 MET A SD 1 ATOM 4056 C CE . MET A 1 520 ? -34.387 50.617 20.486 1.00 58.24 ? 520 MET A CE 1 ATOM 4057 N N . CYS A 1 521 ? -35.729 47.804 15.404 1.00 44.20 ? 521 CYS A N 1 ATOM 4058 C CA . CYS A 1 521 ? -35.677 46.686 14.461 1.00 41.48 ? 521 CYS A CA 1 ATOM 4059 C C . CYS A 1 521 ? -34.278 46.341 13.978 1.00 40.57 ? 521 CYS A C 1 ATOM 4060 O O . CYS A 1 521 ? -34.055 45.220 13.559 1.00 39.21 ? 521 CYS A O 1 ATOM 4061 C CB . CYS A 1 521 ? -36.582 46.929 13.261 1.00 41.22 ? 521 CYS A CB 1 ATOM 4062 S SG . CYS A 1 521 ? -38.334 46.872 13.656 1.00 41.42 ? 521 CYS A SG 1 ATOM 4063 N N . VAL A 1 522 ? -33.339 47.279 14.025 1.00 41.23 ? 522 VAL A N 1 ATOM 4064 C CA . VAL A 1 522 ? -31.934 46.928 13.793 1.00 42.99 ? 522 VAL A CA 1 ATOM 4065 C C . VAL A 1 522 ? -31.480 45.999 14.914 1.00 43.31 ? 522 VAL A C 1 ATOM 4066 O O . VAL A 1 522 ? -30.709 45.063 14.687 1.00 43.94 ? 522 VAL A O 1 ATOM 4067 C CB . VAL A 1 522 ? -30.997 48.158 13.758 1.00 44.40 ? 522 VAL A CB 1 ATOM 4068 C CG1 . VAL A 1 522 ? -29.536 47.733 13.827 1.00 44.68 ? 522 VAL A CG1 1 ATOM 4069 C CG2 . VAL A 1 522 ? -31.247 48.989 12.507 1.00 45.32 ? 522 VAL A CG2 1 ATOM 4070 N N . PHE A 1 523 ? -31.955 46.275 16.124 1.00 42.03 ? 523 PHE A N 1 ATOM 4071 C CA . PHE A 1 523 ? -31.643 45.435 17.267 1.00 41.65 ? 523 PHE A CA 1 ATOM 4072 C C . PHE A 1 523 ? -32.206 44.029 17.109 1.00 40.95 ? 523 PHE A C 1 ATOM 4073 O O . PHE A 1 523 ? -31.524 43.041 17.379 1.00 42.68 ? 523 PHE A O 1 ATOM 4074 C CB . PHE A 1 523 ? -32.161 46.075 18.566 1.00 40.44 ? 523 PHE A CB 1 ATOM 4075 C CG . PHE A 1 523 ? -32.109 45.167 19.743 1.00 38.43 ? 523 PHE A CG 1 ATOM 4076 C CD1 . PHE A 1 523 ? -30.912 44.939 20.396 1.00 39.84 ? 523 PHE A CD1 1 ATOM 4077 C CD2 . PHE A 1 523 ? -33.247 44.535 20.191 1.00 37.32 ? 523 PHE A CD2 1 ATOM 4078 C CE1 . PHE A 1 523 ? -30.848 44.093 21.484 1.00 39.90 ? 523 PHE A CE1 1 ATOM 4079 C CE2 . PHE A 1 523 ? -33.200 43.678 21.279 1.00 37.78 ? 523 PHE A CE2 1 ATOM 4080 C CZ . PHE A 1 523 ? -31.994 43.458 21.927 1.00 39.11 ? 523 PHE A CZ 1 ATOM 4081 N N . TRP A 1 524 ? -33.452 43.930 16.682 1.00 40.26 ? 524 TRP A N 1 ATOM 4082 C CA . TRP A 1 524 ? -34.110 42.629 16.648 1.00 40.42 ? 524 TRP A CA 1 ATOM 4083 C C . TRP A 1 524 ? -33.697 41.797 15.442 1.00 39.93 ? 524 TRP A C 1 ATOM 4084 O O . TRP A 1 524 ? -33.544 40.577 15.549 1.00 39.20 ? 524 TRP A O 1 ATOM 4085 C CB . TRP A 1 524 ? -35.623 42.802 16.680 1.00 39.57 ? 524 TRP A CB 1 ATOM 4086 C CG . TRP A 1 524 ? -36.119 43.249 18.008 1.00 39.42 ? 524 TRP A CG 1 ATOM 4087 C CD1 . TRP A 1 524 ? -36.578 44.480 18.328 1.00 39.79 ? 524 TRP A CD1 1 ATOM 4088 C CD2 . TRP A 1 524 ? -36.191 42.466 19.204 1.00 39.15 ? 524 TRP A CD2 1 ATOM 4089 N NE1 . TRP A 1 524 ? -36.945 44.520 19.648 1.00 40.31 ? 524 TRP A NE1 1 ATOM 4090 C CE2 . TRP A 1 524 ? -36.725 43.290 20.207 1.00 40.03 ? 524 TRP A CE2 1 ATOM 4091 C CE3 . TRP A 1 524 ? -35.873 41.144 19.519 1.00 39.11 ? 524 TRP A CE3 1 ATOM 4092 C CZ2 . TRP A 1 524 ? -36.950 42.837 21.508 1.00 40.12 ? 524 TRP A CZ2 1 ATOM 4093 C CZ3 . TRP A 1 524 ? -36.103 40.693 20.806 1.00 39.61 ? 524 TRP A CZ3 1 ATOM 4094 C CH2 . TRP A 1 524 ? -36.628 41.540 21.788 1.00 39.58 ? 524 TRP A CH2 1 ATOM 4095 N N . ASN A 1 525 ? -33.511 42.469 14.313 1.00 40.85 ? 525 ASN A N 1 ATOM 4096 C CA . ASN A 1 525 ? -33.178 41.814 13.050 1.00 42.16 ? 525 ASN A CA 1 ATOM 4097 C C . ASN A 1 525 ? -31.669 41.572 12.829 1.00 43.29 ? 525 ASN A C 1 ATOM 4098 O O . ASN A 1 525 ? -31.288 40.546 12.280 1.00 42.99 ? 525 ASN A O 1 ATOM 4099 C CB . ASN A 1 525 ? -33.767 42.608 11.875 1.00 42.81 ? 525 ASN A CB 1 ATOM 4100 C CG . ASN A 1 525 ? -35.289 42.690 11.927 1.00 42.69 ? 525 ASN A CG 1 ATOM 4101 O OD1 . ASN A 1 525 ? -35.952 41.779 12.416 1.00 43.13 ? 525 ASN A OD1 1 ATOM 4102 N ND2 . ASN A 1 525 ? -35.847 43.782 11.413 1.00 42.81 ? 525 ASN A ND2 1 ATOM 4103 N N . GLN A 1 526 ? -30.813 42.493 13.258 1.00 44.35 ? 526 GLN A N 1 ATOM 4104 C CA . GLN A 1 526 ? -29.376 42.346 13.023 1.00 45.57 ? 526 GLN A CA 1 ATOM 4105 C C . GLN A 1 526 ? -28.609 41.998 14.300 1.00 45.87 ? 526 GLN A C 1 ATOM 4106 O O . GLN A 1 526 ? -27.987 40.943 14.378 1.00 48.56 ? 526 GLN A O 1 ATOM 4107 C CB . GLN A 1 526 ? -28.799 43.601 12.347 1.00 47.11 ? 526 GLN A CB 1 ATOM 4108 C CG . GLN A 1 526 ? -29.437 43.926 10.991 1.00 47.21 ? 526 GLN A CG 1 ATOM 4109 N N . PHE A 1 527 ? -28.666 42.851 15.312 1.00 44.67 ? 527 PHE A N 1 ATOM 4110 C CA . PHE A 1 527 ? -27.732 42.716 16.424 1.00 44.86 ? 527 PHE A CA 1 ATOM 4111 C C . PHE A 1 527 ? -27.994 41.481 17.271 1.00 44.28 ? 527 PHE A C 1 ATOM 4112 O O . PHE A 1 527 ? -27.120 40.634 17.407 1.00 46.15 ? 527 PHE A O 1 ATOM 4113 C CB . PHE A 1 527 ? -27.716 43.978 17.295 1.00 44.74 ? 527 PHE A CB 1 ATOM 4114 C CG . PHE A 1 527 ? -26.791 43.886 18.482 1.00 44.92 ? 527 PHE A CG 1 ATOM 4115 C CD1 . PHE A 1 527 ? -25.426 44.039 18.326 1.00 46.64 ? 527 PHE A CD1 1 ATOM 4116 C CD2 . PHE A 1 527 ? -27.292 43.653 19.755 1.00 44.19 ? 527 PHE A CD2 1 ATOM 4117 C CE1 . PHE A 1 527 ? -24.574 43.958 19.415 1.00 48.04 ? 527 PHE A CE1 1 ATOM 4118 C CE2 . PHE A 1 527 ? -26.448 43.567 20.845 1.00 45.77 ? 527 PHE A CE2 1 ATOM 4119 C CZ . PHE A 1 527 ? -25.085 43.715 20.677 1.00 47.31 ? 527 PHE A CZ 1 ATOM 4120 N N . LEU A 1 528 ? -29.188 41.376 17.834 1.00 43.42 ? 528 LEU A N 1 ATOM 4121 C CA . LEU A 1 528 ? -29.490 40.305 18.781 1.00 44.19 ? 528 LEU A CA 1 ATOM 4122 C C . LEU A 1 528 ? -29.236 38.887 18.235 1.00 46.37 ? 528 LEU A C 1 ATOM 4123 O O . LEU A 1 528 ? -28.632 38.066 18.934 1.00 49.40 ? 528 LEU A O 1 ATOM 4124 C CB . LEU A 1 528 ? -30.930 40.421 19.298 1.00 41.77 ? 528 LEU A CB 1 ATOM 4125 C CG . LEU A 1 528 ? -31.305 39.309 20.278 1.00 40.94 ? 528 LEU A CG 1 ATOM 4126 C CD1 . LEU A 1 528 ? -30.450 39.436 21.531 1.00 42.25 ? 528 LEU A CD1 1 ATOM 4127 C CD2 . LEU A 1 528 ? -32.787 39.338 20.615 1.00 39.38 ? 528 LEU A CD2 1 ATOM 4128 N N . PRO A 1 529 ? -29.701 38.586 17.007 1.00 46.39 ? 529 PRO A N 1 ATOM 4129 C CA . PRO A 1 529 ? -29.431 37.281 16.424 1.00 47.63 ? 529 PRO A CA 1 ATOM 4130 C C . PRO A 1 529 ? -27.961 36.973 16.374 1.00 50.78 ? 529 PRO A C 1 ATOM 4131 O O . PRO A 1 529 ? -27.542 35.908 16.829 1.00 53.92 ? 529 PRO A O 1 ATOM 4132 C CB . PRO A 1 529 ? -29.985 37.420 15.013 1.00 47.23 ? 529 PRO A CB 1 ATOM 4133 C CG . PRO A 1 529 ? -31.148 38.333 15.198 1.00 46.28 ? 529 PRO A CG 1 ATOM 4134 C CD . PRO A 1 529 ? -30.645 39.351 16.175 1.00 46.66 ? 529 PRO A CD 1 ATOM 4135 N N . LYS A 1 530 ? -27.189 37.920 15.846 1.00 51.97 ? 530 LYS A N 1 ATOM 4136 C CA . LYS A 1 530 ? -25.735 37.831 15.825 1.00 52.64 ? 530 LYS A CA 1 ATOM 4137 C C . LYS A 1 530 ? -25.125 37.684 17.216 1.00 53.04 ? 530 LYS A C 1 ATOM 4138 O O . LYS A 1 530 ? -24.081 37.056 17.362 1.00 56.24 ? 530 LYS A O 1 ATOM 4139 C CB . LYS A 1 530 ? -25.157 39.067 15.141 1.00 54.59 ? 530 LYS A CB 1 ATOM 4140 C CG . LYS A 1 530 ? -23.639 39.100 15.083 1.00 57.79 ? 530 LYS A CG 1 ATOM 4141 C CD . LYS A 1 530 ? -23.162 40.203 14.161 1.00 59.55 ? 530 LYS A CD 1 ATOM 4142 C CE . LYS A 1 530 ? -21.668 40.115 13.928 1.00 62.53 ? 530 LYS A CE 1 ATOM 4143 N NZ . LYS A 1 530 ? -21.199 41.216 13.043 1.00 64.43 ? 530 LYS A NZ 1 ATOM 4144 N N . LEU A 1 531 ? -25.751 38.278 18.226 1.00 51.33 ? 531 LEU A N 1 ATOM 4145 C CA . LEU A 1 531 ? -25.296 38.120 19.600 1.00 53.03 ? 531 LEU A CA 1 ATOM 4146 C C . LEU A 1 531 ? -25.480 36.694 20.047 1.00 52.42 ? 531 LEU A C 1 ATOM 4147 O O . LEU A 1 531 ? -24.571 36.098 20.613 1.00 53.12 ? 531 LEU A O 1 ATOM 4148 C CB . LEU A 1 531 ? -26.064 39.048 20.546 1.00 53.85 ? 531 LEU A CB 1 ATOM 4149 C CG . LEU A 1 531 ? -25.537 39.126 21.989 1.00 55.20 ? 531 LEU A CG 1 ATOM 4150 C CD1 . LEU A 1 531 ? -25.891 40.462 22.624 1.00 54.83 ? 531 LEU A CD1 1 ATOM 4151 C CD2 . LEU A 1 531 ? -26.046 37.978 22.854 1.00 55.47 ? 531 LEU A CD2 1 ATOM 4152 N N . LEU A 1 532 ? -26.666 36.153 19.803 1.00 52.08 ? 532 LEU A N 1 ATOM 4153 C CA . LEU A 1 532 ? -26.987 34.786 20.224 1.00 54.48 ? 532 LEU A CA 1 ATOM 4154 C C . LEU A 1 532 ? -26.201 33.738 19.442 1.00 58.51 ? 532 LEU A C 1 ATOM 4155 O O . LEU A 1 532 ? -25.906 32.669 19.975 1.00 60.92 ? 532 LEU A O 1 ATOM 4156 C CB . LEU A 1 532 ? -28.481 34.505 20.094 1.00 51.78 ? 532 LEU A CB 1 ATOM 4157 C CG . LEU A 1 532 ? -29.387 35.373 20.965 1.00 50.70 ? 532 LEU A CG 1 ATOM 4158 C CD1 . LEU A 1 532 ? -30.797 35.351 20.404 1.00 49.10 ? 532 LEU A CD1 1 ATOM 4159 C CD2 . LEU A 1 532 ? -29.360 34.947 22.429 1.00 50.52 ? 532 LEU A CD2 1 ATOM 4160 N N . ASN A 1 533 ? -25.858 34.044 18.192 1.00 62.08 ? 533 ASN A N 1 ATOM 4161 C CA . ASN A 1 533 ? -25.018 33.155 17.382 1.00 65.94 ? 533 ASN A CA 1 ATOM 4162 C C . ASN A 1 533 ? -23.587 33.078 17.904 1.00 69.15 ? 533 ASN A C 1 ATOM 4163 O O . ASN A 1 533 ? -22.996 32.006 17.921 1.00 72.30 ? 533 ASN A O 1 ATOM 4164 C CB . ASN A 1 533 ? -25.000 33.587 15.912 1.00 66.90 ? 533 ASN A CB 1 ATOM 4165 C CG . ASN A 1 533 ? -24.656 32.445 14.979 1.00 69.86 ? 533 ASN A CG 1 ATOM 4166 O OD1 . ASN A 1 533 ? -23.581 32.410 14.378 1.00 71.22 ? 533 ASN A OD1 1 ATOM 4167 N ND2 . ASN A 1 533 ? -25.569 31.491 14.863 1.00 70.93 ? 533 ASN A ND2 1 ATOM 4168 N N . ALA A 1 534 ? -23.037 34.213 18.332 1.00 71.15 ? 534 ALA A N 1 ATOM 4169 C CA . ALA A 1 534 ? -21.676 34.255 18.870 1.00 74.64 ? 534 ALA A CA 1 ATOM 4170 C C . ALA A 1 534 ? -21.578 33.596 20.244 1.00 77.65 ? 534 ALA A C 1 ATOM 4171 O O . ALA A 1 534 ? -20.487 33.261 20.694 1.00 77.41 ? 534 ALA A O 1 ATOM 4172 C CB . ALA A 1 534 ? -21.183 35.686 18.942 1.00 76.41 ? 534 ALA A CB 1 ATOM 4173 N N . THR A 1 535 ? -22.719 33.439 20.912 1.00 82.16 ? 535 THR A N 1 ATOM 4174 C CA . THR A 1 535 ? -22.826 32.598 22.106 1.00 85.07 ? 535 THR A CA 1 ATOM 4175 C C . THR A 1 535 ? -23.719 31.383 21.794 1.00 87.94 ? 535 THR A C 1 ATOM 4176 O O . THR A 1 535 ? -23.369 30.235 22.074 1.00 92.35 ? 535 THR A O 1 ATOM 4177 C CB . THR A 1 535 ? -23.449 33.364 23.287 1.00 82.87 ? 535 THR A CB 1 ATOM 4178 O OG1 . THR A 1 535 ? -23.145 34.765 23.192 1.00 78.77 ? 535 THR A OG1 1 ATOM 4179 C CG2 . THR A 1 535 ? -22.941 32.796 24.613 1.00 84.17 ? 535 THR A CG2 1 HETATM 4180 C C1 . MBT B 2 . ? -53.562 34.096 23.751 1.00 73.89 ? 601 MBT A C1 1 HETATM 4181 C C2 . MBT B 2 . ? -54.992 33.718 23.898 1.00 76.65 ? 601 MBT A C2 1 HETATM 4182 S S3 . MBT B 2 . ? -55.396 32.416 24.727 1.00 84.79 ? 601 MBT A S3 1 HETATM 4183 C C4 . MBT B 2 . ? -54.107 31.688 25.333 1.00 75.87 ? 601 MBT A C4 1 HETATM 4184 C C5 . MBT B 2 . ? -52.761 32.240 25.067 1.00 75.01 ? 601 MBT A C5 1 HETATM 4185 N N6 . MBT B 2 . ? -52.568 33.366 24.322 1.00 75.33 ? 601 MBT A N6 1 HETATM 4186 C C7 . MBT B 2 . ? -54.223 30.522 26.098 1.00 76.41 ? 601 MBT A C7 1 HETATM 4187 C C8 . MBT B 2 . ? -53.117 29.844 26.650 1.00 74.00 ? 601 MBT A C8 1 HETATM 4188 C C9 . MBT B 2 . ? -51.849 30.391 26.385 1.00 74.30 ? 601 MBT A C9 1 HETATM 4189 C C10 . MBT B 2 . ? -51.688 31.548 25.616 1.00 75.88 ? 601 MBT A C10 1 HETATM 4190 C C11 . MBT B 2 . ? -55.979 34.495 23.291 1.00 73.51 ? 601 MBT A C11 1 HETATM 4191 C C12 . MBT B 2 . ? -55.651 35.648 22.546 1.00 72.06 ? 601 MBT A C12 1 HETATM 4192 C C13 . MBT B 2 . ? -54.288 35.990 22.421 1.00 71.16 ? 601 MBT A C13 1 HETATM 4193 C C14 . MBT B 2 . ? -53.270 35.231 23.009 1.00 74.30 ? 601 MBT A C14 1 HETATM 4194 N N15 . MBT B 2 . ? -53.256 28.653 27.439 1.00 74.58 ? 601 MBT A N15 1 HETATM 4195 C C16 . MBT B 2 . ? -54.551 28.038 27.747 1.00 72.72 ? 601 MBT A C16 1 HETATM 4196 C C17 . MBT B 2 . ? -52.080 27.972 27.990 1.00 74.23 ? 601 MBT A C17 1 HETATM 4197 N N18 . MBT B 2 . ? -56.672 36.441 21.937 1.00 70.10 ? 601 MBT A N18 1 HETATM 4198 C C19 . MBT B 2 . ? -58.089 36.089 22.060 1.00 70.62 ? 601 MBT A C19 1 HETATM 4199 C C20 . MBT B 2 . ? -56.337 37.641 21.173 1.00 71.12 ? 601 MBT A C20 1 HETATM 4200 C C1 . NAG C 3 . ? -82.020 26.083 3.705 1.00 51.98 ? 602 NAG A C1 1 HETATM 4201 C C2 . NAG C 3 . ? -83.537 25.881 3.547 1.00 55.14 ? 602 NAG A C2 1 HETATM 4202 C C3 . NAG C 3 . ? -84.362 26.822 4.446 1.00 55.91 ? 602 NAG A C3 1 HETATM 4203 C C4 . NAG C 3 . ? -83.888 26.758 5.895 1.00 56.38 ? 602 NAG A C4 1 HETATM 4204 C C5 . NAG C 3 . ? -82.389 27.066 5.888 1.00 57.29 ? 602 NAG A C5 1 HETATM 4205 C C6 . NAG C 3 . ? -81.780 27.040 7.289 1.00 61.33 ? 602 NAG A C6 1 HETATM 4206 C C7 . NAG C 3 . ? -83.855 25.085 1.235 1.00 57.61 ? 602 NAG A C7 1 HETATM 4207 C C8 . NAG C 3 . ? -84.342 25.434 -0.144 1.00 57.26 ? 602 NAG A C8 1 HETATM 4208 N N2 . NAG C 3 . ? -83.950 26.048 2.160 1.00 56.52 ? 602 NAG A N2 1 HETATM 4209 O O3 . NAG C 3 . ? -85.747 26.544 4.396 1.00 53.92 ? 602 NAG A O3 1 HETATM 4210 O O4 . NAG C 3 . ? -84.649 27.638 6.714 1.00 53.42 ? 602 NAG A O4 1 HETATM 4211 O O5 . NAG C 3 . ? -81.716 26.104 5.089 1.00 53.52 ? 602 NAG A O5 1 HETATM 4212 O O6 . NAG C 3 . ? -81.135 25.793 7.465 1.00 68.56 ? 602 NAG A O6 1 HETATM 4213 O O7 . NAG C 3 . ? -83.400 23.962 1.452 1.00 57.88 ? 602 NAG A O7 1 HETATM 4214 C C1 . FUC D 4 . ? -81.059 25.384 8.850 1.00 75.22 ? 603 FUC A C1 1 HETATM 4215 C C2 . FUC D 4 . ? -82.212 24.434 9.202 1.00 78.98 ? 603 FUC A C2 1 HETATM 4216 C C3 . FUC D 4 . ? -82.095 23.141 8.394 1.00 79.67 ? 603 FUC A C3 1 HETATM 4217 C C4 . FUC D 4 . ? -80.713 22.518 8.596 1.00 78.99 ? 603 FUC A C4 1 HETATM 4218 C C5 . FUC D 4 . ? -79.607 23.549 8.354 1.00 78.97 ? 603 FUC A C5 1 HETATM 4219 C C6 . FUC D 4 . ? -78.239 22.964 8.700 1.00 78.94 ? 603 FUC A C6 1 HETATM 4220 O O2 . FUC D 4 . ? -83.478 25.032 8.988 1.00 80.14 ? 603 FUC A O2 1 HETATM 4221 O O3 . FUC D 4 . ? -83.115 22.237 8.764 1.00 77.47 ? 603 FUC A O3 1 HETATM 4222 O O4 . FUC D 4 . ? -80.604 21.993 9.902 1.00 76.57 ? 603 FUC A O4 1 HETATM 4223 O O5 . FUC D 4 . ? -79.836 24.721 9.126 1.00 76.66 ? 603 FUC A O5 1 HETATM 4224 C C1 . NAG E 3 . ? -44.217 47.425 -11.978 0.78 43.49 ? 604 NAG A C1 1 HETATM 4225 C C2 . NAG E 3 . ? -43.388 48.714 -11.925 0.78 43.76 ? 604 NAG A C2 1 HETATM 4226 C C3 . NAG E 3 . ? -43.655 49.534 -13.178 0.78 44.88 ? 604 NAG A C3 1 HETATM 4227 C C4 . NAG E 3 . ? -43.263 48.687 -14.381 0.78 45.44 ? 604 NAG A C4 1 HETATM 4228 C C5 . NAG E 3 . ? -44.164 47.450 -14.398 0.78 45.63 ? 604 NAG A C5 1 HETATM 4229 C C6 . NAG E 3 . ? -43.900 46.586 -15.641 0.78 46.59 ? 604 NAG A C6 1 HETATM 4230 C C7 . NAG E 3 . ? -42.986 49.365 -9.591 0.78 42.99 ? 604 NAG A C7 1 HETATM 4231 C C8 . NAG E 3 . ? -43.388 50.253 -8.449 0.78 41.83 ? 604 NAG A C8 1 HETATM 4232 N N2 . NAG E 3 . ? -43.664 49.512 -10.737 0.78 42.98 ? 604 NAG A N2 1 HETATM 4233 O O3 . NAG E 3 . ? -42.919 50.734 -13.148 0.78 46.10 ? 604 NAG A O3 1 HETATM 4234 O O4 . NAG E 3 . ? -43.311 49.439 -15.579 0.78 45.07 ? 604 NAG A O4 1 HETATM 4235 O O5 . NAG E 3 . ? -43.961 46.718 -13.191 0.78 44.50 ? 604 NAG A O5 1 HETATM 4236 O O6 . NAG E 3 . ? -43.796 45.205 -15.350 0.78 48.57 ? 604 NAG A O6 1 HETATM 4237 O O7 . NAG E 3 . ? -42.075 48.549 -9.430 0.78 42.87 ? 604 NAG A O7 1 HETATM 4238 C C1 . NAG F 3 . ? -74.219 51.193 23.034 1.00 71.42 ? 605 NAG A C1 1 HETATM 4239 C C2 . NAG F 3 . ? -74.011 49.739 23.486 1.00 72.50 ? 605 NAG A C2 1 HETATM 4240 C C3 . NAG F 3 . ? -74.996 49.288 24.560 1.00 75.82 ? 605 NAG A C3 1 HETATM 4241 C C4 . NAG F 3 . ? -74.988 50.309 25.693 1.00 80.49 ? 605 NAG A C4 1 HETATM 4242 C C5 . NAG F 3 . ? -75.438 51.633 25.059 1.00 79.93 ? 605 NAG A C5 1 HETATM 4243 C C6 . NAG F 3 . ? -75.841 52.742 26.050 1.00 78.09 ? 605 NAG A C6 1 HETATM 4244 C C7 . NAG F 3 . ? -73.170 47.858 22.185 1.00 66.53 ? 605 NAG A C7 1 HETATM 4245 C C8 . NAG F 3 . ? -73.349 46.950 21.005 1.00 65.61 ? 605 NAG A C8 1 HETATM 4246 N N2 . NAG F 3 . ? -74.082 48.810 22.370 1.00 69.81 ? 605 NAG A N2 1 HETATM 4247 O O3 . NAG F 3 . ? -74.646 48.004 25.021 1.00 75.01 ? 605 NAG A O3 1 HETATM 4248 O O4 . NAG F 3 . ? -75.815 49.898 26.776 1.00 87.88 ? 605 NAG A O4 1 HETATM 4249 O O5 . NAG F 3 . ? -74.420 52.048 24.156 1.00 74.24 ? 605 NAG A O5 1 HETATM 4250 O O6 . NAG F 3 . ? -74.731 53.472 26.523 1.00 78.47 ? 605 NAG A O6 1 HETATM 4251 O O7 . NAG F 3 . ? -72.207 47.705 22.928 1.00 65.44 ? 605 NAG A O7 1 HETATM 4252 C C1 . NAG G 3 . ? -75.161 49.024 27.737 1.00 90.85 ? 606 NAG A C1 1 HETATM 4253 C C2 . NAG G 3 . ? -75.240 49.677 29.129 1.00 91.65 ? 606 NAG A C2 1 HETATM 4254 C C3 . NAG G 3 . ? -76.606 49.404 29.794 1.00 86.95 ? 606 NAG A C3 1 HETATM 4255 C C4 . NAG G 3 . ? -77.017 47.919 29.775 1.00 85.36 ? 606 NAG A C4 1 HETATM 4256 C C5 . NAG G 3 . ? -76.009 47.097 28.950 1.00 83.95 ? 606 NAG A C5 1 HETATM 4257 C C6 . NAG G 3 . ? -76.486 45.690 28.615 1.00 80.58 ? 606 NAG A C6 1 HETATM 4258 C C7 . NAG G 3 . ? -72.822 49.638 29.789 1.00 91.92 ? 606 NAG A C7 1 HETATM 4259 C C8 . NAG G 3 . ? -71.835 49.192 30.831 1.00 90.03 ? 606 NAG A C8 1 HETATM 4260 N N2 . NAG G 3 . ? -74.113 49.334 30.016 1.00 93.74 ? 606 NAG A N2 1 HETATM 4261 O O3 . NAG G 3 . ? -77.596 50.177 29.150 1.00 82.46 ? 606 NAG A O3 1 HETATM 4262 O O4 . NAG G 3 . ? -77.086 47.479 31.127 1.00 83.43 ? 606 NAG A O4 1 HETATM 4263 O O5 . NAG G 3 . ? -75.746 47.730 27.708 1.00 87.80 ? 606 NAG A O5 1 HETATM 4264 O O6 . NAG G 3 . ? -75.654 45.161 27.612 1.00 74.80 ? 606 NAG A O6 1 HETATM 4265 O O7 . NAG G 3 . ? -72.406 50.242 28.799 1.00 90.43 ? 606 NAG A O7 1 HETATM 4266 C C1 . BMA H 5 . ? -77.992 46.392 31.439 1.00 80.57 ? 607 BMA A C1 1 HETATM 4267 C C2 . BMA H 5 . ? -77.212 45.360 32.267 1.00 79.15 ? 607 BMA A C2 1 HETATM 4268 C C3 . BMA H 5 . ? -78.084 44.239 32.846 1.00 79.82 ? 607 BMA A C3 1 HETATM 4269 C C4 . BMA H 5 . ? -79.369 44.818 33.460 1.00 79.02 ? 607 BMA A C4 1 HETATM 4270 C C5 . BMA H 5 . ? -80.065 45.801 32.506 1.00 78.53 ? 607 BMA A C5 1 HETATM 4271 C C6 . BMA H 5 . ? -81.369 46.383 33.085 1.00 76.14 ? 607 BMA A C6 1 HETATM 4272 O O2 . BMA H 5 . ? -76.532 46.027 33.339 1.00 73.82 ? 607 BMA A O2 1 HETATM 4273 O O3 . BMA H 5 . ? -77.318 43.489 33.830 1.00 79.81 ? 607 BMA A O3 1 HETATM 4274 O O4 . BMA H 5 . ? -80.269 43.752 33.792 1.00 77.70 ? 607 BMA A O4 1 HETATM 4275 O O5 . BMA H 5 . ? -79.148 46.844 32.155 1.00 80.77 ? 607 BMA A O5 1 HETATM 4276 O O6 . BMA H 5 . ? -81.197 47.704 33.617 1.00 71.84 ? 607 BMA A O6 1 HETATM 4277 C C1 . MAN I 6 . ? -77.085 42.077 33.528 1.00 78.70 ? 608 MAN A C1 1 HETATM 4278 C C2 . MAN I 6 . ? -77.165 41.225 34.798 1.00 77.72 ? 608 MAN A C2 1 HETATM 4279 C C3 . MAN I 6 . ? -76.062 41.680 35.750 1.00 74.71 ? 608 MAN A C3 1 HETATM 4280 C C4 . MAN I 6 . ? -74.698 41.437 35.101 1.00 74.63 ? 608 MAN A C4 1 HETATM 4281 C C5 . MAN I 6 . ? -74.623 41.895 33.634 1.00 73.73 ? 608 MAN A C5 1 HETATM 4282 C C6 . MAN I 6 . ? -73.563 41.062 32.914 1.00 73.91 ? 608 MAN A C6 1 HETATM 4283 O O2 . MAN I 6 . ? -76.987 39.846 34.480 1.00 81.97 ? 608 MAN A O2 1 HETATM 4284 O O3 . MAN I 6 . ? -76.137 40.977 36.970 1.00 68.78 ? 608 MAN A O3 1 HETATM 4285 O O4 . MAN I 6 . ? -73.689 42.081 35.856 1.00 70.37 ? 608 MAN A O4 1 HETATM 4286 O O5 . MAN I 6 . ? -75.840 41.797 32.891 1.00 76.73 ? 608 MAN A O5 1 HETATM 4287 O O6 . MAN I 6 . ? -73.044 41.754 31.800 1.00 75.73 ? 608 MAN A O6 1 HETATM 4288 C C1 . MAN J 6 . ? -78.186 39.028 34.492 1.00 84.14 ? 609 MAN A C1 1 HETATM 4289 C C2 . MAN J 6 . ? -78.313 38.295 35.829 1.00 83.27 ? 609 MAN A C2 1 HETATM 4290 C C3 . MAN J 6 . ? -79.662 37.569 35.920 1.00 80.38 ? 609 MAN A C3 1 HETATM 4291 C C4 . MAN J 6 . ? -80.123 37.071 34.553 1.00 81.67 ? 609 MAN A C4 1 HETATM 4292 C C5 . MAN J 6 . ? -78.909 36.860 33.640 1.00 87.34 ? 609 MAN A C5 1 HETATM 4293 C C6 . MAN J 6 . ? -79.296 36.273 32.282 1.00 89.80 ? 609 MAN A C6 1 HETATM 4294 O O2 . MAN J 6 . ? -78.143 39.178 36.916 1.00 83.80 ? 609 MAN A O2 1 HETATM 4295 O O3 . MAN J 6 . ? -80.650 38.420 36.448 1.00 76.55 ? 609 MAN A O3 1 HETATM 4296 O O4 . MAN J 6 . ? -80.851 35.872 34.722 1.00 76.38 ? 609 MAN A O4 1 HETATM 4297 O O5 . MAN J 6 . ? -78.177 38.071 33.437 1.00 87.44 ? 609 MAN A O5 1 HETATM 4298 O O6 . MAN J 6 . ? -80.112 37.169 31.567 1.00 97.20 ? 609 MAN A O6 1 HETATM 4299 S S . SO4 K 7 . ? -33.451 22.222 14.972 1.00 72.43 ? 610 SO4 A S 1 HETATM 4300 O O1 . SO4 K 7 . ? -33.563 21.840 13.534 1.00 67.94 ? 610 SO4 A O1 1 HETATM 4301 O O2 . SO4 K 7 . ? -32.556 23.394 15.082 1.00 73.57 ? 610 SO4 A O2 1 HETATM 4302 O O3 . SO4 K 7 . ? -32.914 21.070 15.752 1.00 66.01 ? 610 SO4 A O3 1 HETATM 4303 O O4 . SO4 K 7 . ? -34.755 22.658 15.537 1.00 68.21 ? 610 SO4 A O4 1 HETATM 4304 S S . SO4 L 7 . ? -44.850 53.127 40.462 1.00 64.98 ? 611 SO4 A S 1 HETATM 4305 O O1 . SO4 L 7 . ? -43.684 53.925 40.014 1.00 63.27 ? 611 SO4 A O1 1 HETATM 4306 O O2 . SO4 L 7 . ? -44.827 51.776 39.837 1.00 61.45 ? 611 SO4 A O2 1 HETATM 4307 O O3 . SO4 L 7 . ? -46.092 53.809 40.038 1.00 63.30 ? 611 SO4 A O3 1 HETATM 4308 O O4 . SO4 L 7 . ? -44.801 53.025 41.950 1.00 61.32 ? 611 SO4 A O4 1 HETATM 4309 S S . SO4 M 7 . ? -40.802 61.046 10.551 1.00 74.04 ? 612 SO4 A S 1 HETATM 4310 O O1 . SO4 M 7 . ? -40.699 61.793 9.271 1.00 71.95 ? 612 SO4 A O1 1 HETATM 4311 O O2 . SO4 M 7 . ? -40.947 59.604 10.258 1.00 72.90 ? 612 SO4 A O2 1 HETATM 4312 O O3 . SO4 M 7 . ? -41.962 61.544 11.334 1.00 70.76 ? 612 SO4 A O3 1 HETATM 4313 O O4 . SO4 M 7 . ? -39.561 61.225 11.338 1.00 74.93 ? 612 SO4 A O4 1 HETATM 4314 S S . SO4 N 7 . ? -68.813 44.194 -13.366 1.00 62.27 ? 613 SO4 A S 1 HETATM 4315 O O1 . SO4 N 7 . ? -67.990 43.068 -13.863 1.00 61.25 ? 613 SO4 A O1 1 HETATM 4316 O O2 . SO4 N 7 . ? -69.119 45.122 -14.482 1.00 62.24 ? 613 SO4 A O2 1 HETATM 4317 O O3 . SO4 N 7 . ? -70.098 43.684 -12.837 1.00 59.41 ? 613 SO4 A O3 1 HETATM 4318 O O4 . SO4 N 7 . ? -68.043 44.893 -12.299 1.00 61.06 ? 613 SO4 A O4 1 HETATM 4319 S S . SO4 O 7 . ? -33.100 44.132 7.828 1.00 67.09 ? 614 SO4 A S 1 HETATM 4320 O O1 . SO4 O 7 . ? -32.891 44.750 6.500 1.00 66.31 ? 614 SO4 A O1 1 HETATM 4321 O O2 . SO4 O 7 . ? -33.336 42.690 7.660 1.00 67.46 ? 614 SO4 A O2 1 HETATM 4322 O O3 . SO4 O 7 . ? -34.283 44.758 8.472 1.00 63.17 ? 614 SO4 A O3 1 HETATM 4323 O O4 . SO4 O 7 . ? -31.870 44.261 8.651 1.00 68.59 ? 614 SO4 A O4 1 HETATM 4324 S S . SO4 P 7 . ? -56.462 59.527 16.504 1.00 52.94 ? 615 SO4 A S 1 HETATM 4325 O O1 . SO4 P 7 . ? -57.549 58.820 15.791 1.00 52.34 ? 615 SO4 A O1 1 HETATM 4326 O O2 . SO4 P 7 . ? -56.000 60.678 15.680 1.00 52.83 ? 615 SO4 A O2 1 HETATM 4327 O O3 . SO4 P 7 . ? -55.328 58.596 16.751 1.00 51.81 ? 615 SO4 A O3 1 HETATM 4328 O O4 . SO4 P 7 . ? -57.012 60.004 17.798 1.00 52.80 ? 615 SO4 A O4 1 HETATM 4329 S S . SO4 Q 7 . ? -70.490 60.862 17.175 1.00 74.71 ? 616 SO4 A S 1 HETATM 4330 O O1 . SO4 Q 7 . ? -69.215 60.942 16.422 1.00 74.39 ? 616 SO4 A O1 1 HETATM 4331 O O2 . SO4 Q 7 . ? -71.581 60.487 16.242 1.00 73.28 ? 616 SO4 A O2 1 HETATM 4332 O O3 . SO4 Q 7 . ? -70.362 59.865 18.264 1.00 71.55 ? 616 SO4 A O3 1 HETATM 4333 O O4 . SO4 Q 7 . ? -70.808 62.182 17.765 1.00 76.38 ? 616 SO4 A O4 1 HETATM 4334 S S . SO4 R 7 . ? -76.822 45.795 9.375 1.00 51.50 ? 617 SO4 A S 1 HETATM 4335 O O1 . SO4 R 7 . ? -76.364 46.695 8.289 1.00 53.91 ? 617 SO4 A O1 1 HETATM 4336 O O2 . SO4 R 7 . ? -77.949 44.972 8.869 1.00 50.66 ? 617 SO4 A O2 1 HETATM 4337 O O3 . SO4 R 7 . ? -75.699 44.916 9.773 1.00 52.46 ? 617 SO4 A O3 1 HETATM 4338 O O4 . SO4 R 7 . ? -77.235 46.600 10.552 1.00 50.34 ? 617 SO4 A O4 1 HETATM 4339 S S . SO4 S 7 . ? -36.687 33.739 20.680 1.00 78.78 ? 618 SO4 A S 1 HETATM 4340 O O1 . SO4 S 7 . ? -35.319 34.307 20.564 1.00 75.16 ? 618 SO4 A O1 1 HETATM 4341 O O2 . SO4 S 7 . ? -37.042 32.922 19.486 1.00 76.51 ? 618 SO4 A O2 1 HETATM 4342 O O3 . SO4 S 7 . ? -36.729 32.893 21.887 1.00 81.59 ? 618 SO4 A O3 1 HETATM 4343 O O4 . SO4 S 7 . ? -37.678 34.820 20.866 1.00 75.20 ? 618 SO4 A O4 1 HETATM 4344 S S . SO4 T 7 . ? -59.633 51.554 31.743 1.00 80.86 ? 619 SO4 A S 1 HETATM 4345 O O1 . SO4 T 7 . ? -58.991 51.972 30.481 1.00 78.68 ? 619 SO4 A O1 1 HETATM 4346 O O2 . SO4 T 7 . ? -61.101 51.592 31.551 1.00 85.67 ? 619 SO4 A O2 1 HETATM 4347 O O3 . SO4 T 7 . ? -59.221 50.176 32.114 1.00 76.29 ? 619 SO4 A O3 1 HETATM 4348 O O4 . SO4 T 7 . ? -59.254 52.509 32.818 1.00 83.42 ? 619 SO4 A O4 1 HETATM 4349 S S . SO4 U 7 . ? -66.188 16.167 14.961 1.00 104.71 ? 620 SO4 A S 1 HETATM 4350 O O1 . SO4 U 7 . ? -66.256 16.072 13.484 1.00 109.97 ? 620 SO4 A O1 1 HETATM 4351 O O2 . SO4 U 7 . ? -65.063 17.054 15.334 1.00 99.21 ? 620 SO4 A O2 1 HETATM 4352 O O3 . SO4 U 7 . ? -65.948 14.816 15.520 1.00 101.26 ? 620 SO4 A O3 1 HETATM 4353 O O4 . SO4 U 7 . ? -67.465 16.726 15.471 1.00 97.88 ? 620 SO4 A O4 1 HETATM 4354 S S . SO4 V 7 . ? -55.475 49.200 40.007 1.00 87.15 ? 621 SO4 A S 1 HETATM 4355 O O1 . SO4 V 7 . ? -54.467 49.511 38.960 1.00 86.55 ? 621 SO4 A O1 1 HETATM 4356 O O2 . SO4 V 7 . ? -56.842 49.567 39.556 1.00 83.89 ? 621 SO4 A O2 1 HETATM 4357 O O3 . SO4 V 7 . ? -55.414 47.754 40.316 1.00 87.66 ? 621 SO4 A O3 1 HETATM 4358 O O4 . SO4 V 7 . ? -55.169 49.952 41.243 1.00 89.60 ? 621 SO4 A O4 1 HETATM 4359 S S . SO4 W 7 . ? -50.224 64.719 -1.945 1.00 86.32 ? 622 SO4 A S 1 HETATM 4360 O O1 . SO4 W 7 . ? -50.630 64.184 -3.267 1.00 83.86 ? 622 SO4 A O1 1 HETATM 4361 O O2 . SO4 W 7 . ? -48.948 65.456 -2.098 1.00 86.81 ? 622 SO4 A O2 1 HETATM 4362 O O3 . SO4 W 7 . ? -50.038 63.599 -0.993 1.00 88.31 ? 622 SO4 A O3 1 HETATM 4363 O O4 . SO4 W 7 . ? -51.258 65.639 -1.411 1.00 85.64 ? 622 SO4 A O4 1 HETATM 4364 S S . SO4 X 7 . ? -50.277 44.182 -12.183 1.00 80.16 ? 623 SO4 A S 1 HETATM 4365 O O1 . SO4 X 7 . ? -48.883 44.629 -12.460 1.00 78.47 ? 623 SO4 A O1 1 HETATM 4366 O O2 . SO4 X 7 . ? -50.856 43.586 -13.407 1.00 76.12 ? 623 SO4 A O2 1 HETATM 4367 O O3 . SO4 X 7 . ? -50.289 43.179 -11.081 1.00 78.23 ? 623 SO4 A O3 1 HETATM 4368 O O4 . SO4 X 7 . ? -51.102 45.350 -11.801 1.00 77.26 ? 623 SO4 A O4 1 HETATM 4369 S S . SO4 Y 7 . ? -39.101 48.226 44.914 1.00 81.74 ? 624 SO4 A S 1 HETATM 4370 O O1 . SO4 Y 7 . ? -38.134 48.374 43.802 1.00 83.77 ? 624 SO4 A O1 1 HETATM 4371 O O2 . SO4 Y 7 . ? -39.736 46.890 44.802 1.00 80.64 ? 624 SO4 A O2 1 HETATM 4372 O O3 . SO4 Y 7 . ? -40.150 49.269 44.823 1.00 81.31 ? 624 SO4 A O3 1 HETATM 4373 O O4 . SO4 Y 7 . ? -38.382 48.375 46.209 1.00 79.15 ? 624 SO4 A O4 1 HETATM 4374 O O . HOH Z 8 . ? -50.948 38.153 33.201 1.00 22.62 ? 701 HOH A O 1 HETATM 4375 O O . HOH Z 8 . ? -60.580 34.848 22.655 1.00 30.78 ? 702 HOH A O 1 HETATM 4376 O O . HOH Z 8 . ? -53.515 43.140 13.777 1.00 34.43 ? 703 HOH A O 1 HETATM 4377 O O . HOH Z 8 . ? -59.637 34.281 13.628 1.00 33.35 ? 704 HOH A O 1 HETATM 4378 O O . HOH Z 8 . ? -67.533 43.636 5.697 1.00 27.16 ? 705 HOH A O 1 HETATM 4379 O O . HOH Z 8 . ? -41.295 32.143 10.372 1.00 23.41 ? 706 HOH A O 1 HETATM 4380 O O . HOH Z 8 . ? -55.092 30.805 13.250 1.00 29.74 ? 707 HOH A O 1 HETATM 4381 O O . HOH Z 8 . ? -45.176 29.317 17.674 1.00 23.03 ? 708 HOH A O 1 HETATM 4382 O O . HOH Z 8 . ? -58.529 22.155 13.721 1.00 27.47 ? 709 HOH A O 1 HETATM 4383 O O . HOH Z 8 . ? -42.834 28.172 18.452 1.00 25.08 ? 710 HOH A O 1 HETATM 4384 O O . HOH Z 8 . ? -48.148 56.607 17.324 1.00 15.44 ? 711 HOH A O 1 HETATM 4385 O O . HOH Z 8 . ? -58.453 16.678 10.850 1.00 28.80 ? 712 HOH A O 1 HETATM 4386 O O . HOH Z 8 . ? -62.043 23.285 23.172 1.00 27.00 ? 713 HOH A O 1 HETATM 4387 O O . HOH Z 8 . ? -56.821 22.410 17.854 1.00 33.25 ? 714 HOH A O 1 HETATM 4388 O O . HOH Z 8 . ? -39.141 32.971 -8.939 1.00 15.08 ? 715 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 . SER A 4 ? 0.7837 1.6601 1.0596 0.0436 -0.2588 -0.0945 4 SER A N 2 C CA . SER A 4 ? 0.7786 1.6472 1.0724 0.0543 -0.2420 -0.0902 4 SER A CA 3 C C . SER A 4 ? 0.7690 1.5771 1.0281 0.0585 -0.2282 -0.0795 4 SER A C 4 O O . SER A 4 ? 0.7650 1.5402 0.9983 0.0416 -0.2207 -0.0811 4 SER A O 5 C CB . SER A 4 ? 0.7725 1.6655 1.0983 0.0336 -0.2271 -0.1021 4 SER A CB 6 O OG . SER A 4 ? 0.7460 1.6216 1.0799 0.0402 -0.2084 -0.0980 4 SER A OG 7 N N . GLU A 5 ? 0.7420 1.5369 1.0024 0.0813 -0.2250 -0.0696 5 GLU A N 8 C CA . GLU A 5 ? 0.7044 1.4451 0.9342 0.0884 -0.2140 -0.0586 5 GLU A CA 9 C C . GLU A 5 ? 0.6627 1.3773 0.8897 0.0703 -0.1923 -0.0626 5 GLU A C 10 O O . GLU A 5 ? 0.6456 1.3151 0.8439 0.0687 -0.1833 -0.0561 5 GLU A O 11 C CB . GLU A 5 ? 0.7191 1.4576 0.9581 0.1158 -0.2153 -0.0496 5 GLU A CB 12 C CG . GLU A 5 ? 0.7540 1.4412 0.9575 0.1287 -0.2136 -0.0356 5 GLU A CG 13 C CD . GLU A 5 ? 0.7803 1.4644 0.9939 0.1556 -0.2157 -0.0278 5 GLU A CD 14 O OE1 . GLU A 5 ? 0.7998 1.5246 1.0426 0.1696 -0.2261 -0.0314 5 GLU A OE1 15 O OE2 . GLU A 5 ? 0.8244 1.4655 1.0170 0.1630 -0.2072 -0.0188 5 GLU A OE2 16 N N . LEU A 6 ? 0.6304 1.3745 0.8875 0.0566 -0.1840 -0.0732 6 LEU A N 17 C CA . LEU A 6 ? 0.5909 1.3133 0.8474 0.0395 -0.1640 -0.0768 6 LEU A CA 18 C C . LEU A 6 ? 0.5748 1.2892 0.8200 0.0130 -0.1619 -0.0850 6 LEU A C 19 O O . LEU A 6 ? 0.5634 1.2626 0.8096 -0.0031 -0.1470 -0.0888 6 LEU A O 20 C CB . LEU A 6 ? 0.5802 1.3362 0.8737 0.0389 -0.1541 -0.0828 6 LEU A CB 21 C CG . LEU A 6 ? 0.5681 1.3406 0.8799 0.0654 -0.1559 -0.0782 6 LEU A CG 22 C CD1 . LEU A 6 ? 0.5338 1.3446 0.8829 0.0611 -0.1448 -0.0867 6 LEU A CD1 23 C CD2 . LEU A 6 ? 0.5671 1.2910 0.8532 0.0806 -0.1486 -0.0671 6 LEU A CD2 24 N N . LEU A 7 ? 0.5784 1.3013 0.8116 0.0086 -0.1772 -0.0878 7 LEU A N 25 C CA . LEU A 7 ? 0.5729 1.2848 0.7921 -0.0153 -0.1764 -0.0965 7 LEU A CA 26 C C . LEU A 7 ? 0.5634 1.2352 0.7423 -0.0124 -0.1797 -0.0909 7 LEU A C 27 O O . LEU A 7 ? 0.5776 1.2531 0.7431 0.0016 -0.1935 -0.0851 7 LEU A O 28 C CB . LEU A 7 ? 0.5935 1.3515 0.8326 -0.0261 -0.1910 -0.1073 7 LEU A CB 29 C CG . LEU A 7 ? 0.6131 1.3626 0.8372 -0.0500 -0.1939 -0.1178 7 LEU A CG 30 C CD1 . LEU A 7 ? 0.6086 1.3278 0.8287 -0.0693 -0.1753 -0.1219 7 LEU A CD1 31 C CD2 . LEU A 7 ? 0.6263 1.4272 0.8762 -0.0609 -0.2081 -0.1290 7 LEU A CD2 32 N N . VAL A 8 ? 0.5492 1.1832 0.7088 -0.0251 -0.1670 -0.0925 8 VAL A N 33 C CA . VAL A 8 ? 0.5529 1.1487 0.6756 -0.0226 -0.1670 -0.0878 8 VAL A CA 34 C C . VAL A 8 ? 0.5576 1.1349 0.6653 -0.0437 -0.1627 -0.0983 8 VAL A C 35 O O . VAL A 8 ? 0.5422 1.1065 0.6574 -0.0568 -0.1502 -0.1030 8 VAL A O 36 C CB . VAL A 8 ? 0.5403 1.0996 0.6507 -0.0112 -0.1537 -0.0769 8 VAL A CB 37 C CG1 . VAL A 8 ? 0.5511 1.0742 0.6255 -0.0104 -0.1524 -0.0729 8 VAL A CG1 38 C CG2 . VAL A 8 ? 0.5366 1.1072 0.6583 0.0106 -0.1574 -0.0667 8 VAL A CG2 39 N N . ASN A 9 ? 0.5831 1.1573 0.6678 -0.0465 -0.1732 -0.1018 9 ASN A N 40 C CA . ASN A 9 ? 0.6059 1.1581 0.6722 -0.0641 -0.1693 -0.1124 9 ASN A CA 41 C C . ASN A 9 ? 0.6033 1.1121 0.6419 -0.0591 -0.1581 -0.1068 9 ASN A C 42 O O . ASN A 9 ? 0.6191 1.1178 0.6356 -0.0469 -0.1621 -0.0989 9 ASN A O 43 C CB . ASN A 9 ? 0.6300 1.1997 0.6832 -0.0703 -0.1854 -0.1209 9 ASN A CB 44 C CG . ASN A 9 ? 0.6460 1.2584 0.7275 -0.0810 -0.1960 -0.1303 9 ASN A CG 45 O OD1 . ASN A 9 ? 0.6520 1.2705 0.7552 -0.0956 -0.1885 -0.1373 9 ASN A OD1 46 N ND2 . ASN A 9 ? 0.6731 1.3161 0.7544 -0.0742 -0.2139 -0.1303 9 ASN A ND2 47 N N . THR A 10 ? 0.5880 1.0717 0.6278 -0.0688 -0.1442 -0.1104 10 THR A N 48 C CA . THR A 10 ? 0.5980 1.0432 0.6145 -0.0658 -0.1336 -0.1073 10 THR A CA 49 C C . THR A 10 ? 0.6170 1.0465 0.6188 -0.0813 -0.1326 -0.1208 10 THR A C 50 O O . THR A 10 ? 0.6272 1.0713 0.6403 -0.0959 -0.1375 -0.1316 10 THR A O 51 C CB . THR A 10 ? 0.5836 1.0093 0.6110 -0.0631 -0.1189 -0.1010 10 THR A CB 52 O OG1 . THR A 10 ? 0.5992 1.0187 0.6378 -0.0796 -0.1124 -0.1099 10 THR A OG1 53 C CG2 . THR A 10 ? 0.5639 1.0097 0.6119 -0.0507 -0.1197 -0.0911 10 THR A CG2 54 N N . LYS A 11 ? 0.6226 1.0223 0.6002 -0.0783 -0.1260 -0.1209 11 LYS A N 55 C CA . LYS A 11 ? 0.6276 1.0067 0.5904 -0.0908 -0.1229 -0.1343 11 LYS A CA 56 C C . LYS A 11 ? 0.6098 0.9771 0.5887 -0.1050 -0.1157 -0.1414 11 LYS A C 57 O O . LYS A 11 ? 0.6134 0.9676 0.5842 -0.1176 -0.1160 -0.1542 11 LYS A O 58 C CB . LYS A 11 ? 0.6450 0.9947 0.5838 -0.0828 -0.1140 -0.1319 11 LYS A CB 59 C CG . LYS A 11 ? 0.6693 1.0256 0.5858 -0.0723 -0.1199 -0.1261 11 LYS A CG 60 C CD . LYS A 11 ? 0.6855 1.0168 0.5868 -0.0628 -0.1083 -0.1191 11 LYS A CD 61 C CE . LYS A 11 ? 0.7120 1.0442 0.5854 -0.0566 -0.1115 -0.1164 11 LYS A CE 62 N NZ . LYS A 11 ? 0.7120 1.0537 0.5839 -0.0441 -0.1154 -0.0998 11 LYS A NZ 63 N N . SER A 12 ? 0.5878 0.9577 0.5874 -0.1030 -0.1091 -0.1333 12 SER A N 64 C CA . SER A 12 ? 0.5863 0.9460 0.6002 -0.1172 -0.1023 -0.1382 12 SER A CA 65 C C . SER A 12 ? 0.5776 0.9693 0.6141 -0.1307 -0.1093 -0.1437 12 SER A C 66 O O . SER A 12 ? 0.5524 0.9367 0.5984 -0.1464 -0.1048 -0.1493 12 SER A O 67 C CB . SER A 12 ? 0.5738 0.9190 0.5964 -0.1097 -0.0905 -0.1271 12 SER A CB 68 O OG . SER A 12 ? 0.5845 0.9033 0.5895 -0.0979 -0.0841 -0.1219 12 SER A OG 69 N N . GLY A 13 ? 0.5788 1.0060 0.6236 -0.1246 -0.1204 -0.1417 13 GLY A N 70 C CA . GLY A 13 ? 0.5842 1.0496 0.6547 -0.1347 -0.1277 -0.1460 13 GLY A CA 71 C C . GLY A 13 ? 0.5707 1.0684 0.6596 -0.1190 -0.1317 -0.1354 13 GLY A C 72 O O . GLY A 13 ? 0.5465 1.0333 0.6274 -0.1012 -0.1282 -0.1243 13 GLY A O 73 N N . LYS A 14 ? 0.5671 1.1052 0.6815 -0.1256 -0.1393 -0.1396 14 LYS A N 74 C CA . LYS A 14 ? 0.5428 1.1151 0.6787 -0.1104 -0.1436 -0.1313 14 LYS A CA 75 C C . LYS A 14 ? 0.5217 1.0878 0.6736 -0.1068 -0.1288 -0.1239 14 LYS A C 76 O O . LYS A 14 ? 0.5195 1.0723 0.6766 -0.1226 -0.1182 -0.1278 14 LYS A O 77 C CB . LYS A 14 ? 0.5369 1.1579 0.6977 -0.1193 -0.1564 -0.1397 14 LYS A CB 78 N N . VAL A 15 ? 0.5031 1.0767 0.6607 -0.0864 -0.1281 -0.1133 15 VAL A N 79 C CA . VAL A 15 ? 0.4939 1.0692 0.6691 -0.0817 -0.1156 -0.1075 15 VAL A CA 80 C C . VAL A 15 ? 0.5009 1.1184 0.7022 -0.0676 -0.1220 -0.1046 15 VAL A C 81 O O . VAL A 15 ? 0.5126 1.1426 0.7096 -0.0523 -0.1347 -0.1010 15 VAL A O 82 C CB . VAL A 15 ? 0.4834 1.0185 0.6391 -0.0690 -0.1051 -0.0974 15 VAL A CB 83 C CG1 . VAL A 15 ? 0.4908 0.9853 0.6230 -0.0807 -0.0983 -0.1003 15 VAL A CG1 84 C CG2 . VAL A 15 ? 0.4881 1.0198 0.6307 -0.0474 -0.1130 -0.0886 15 VAL A CG2 85 N N . MET A 16 ? 0.5055 1.1444 0.7331 -0.0722 -0.1131 -0.1061 16 MET A N 86 C CA . MET A 16 ? 0.5088 1.1889 0.7643 -0.0576 -0.1170 -0.1045 16 MET A CA 87 C C . MET A 16 ? 0.4814 1.1465 0.7390 -0.0440 -0.1038 -0.0966 16 MET A C 88 O O . MET A 16 ? 0.4655 1.1209 0.7275 -0.0553 -0.0892 -0.0976 16 MET A O 89 C CB . MET A 16 ? 0.5329 1.2594 0.8214 -0.0740 -0.1175 -0.1145 16 MET A CB 90 C CG . MET A 16 ? 0.5444 1.3199 0.8661 -0.0587 -0.1218 -0.1148 16 MET A CG 91 S SD . MET A 16 ? 0.5901 1.3946 0.9141 -0.0391 -0.1462 -0.1139 16 MET A SD 92 C CE . MET A 16 ? 0.5865 1.4360 0.9322 -0.0642 -0.1570 -0.1282 16 MET A CE 93 N N . GLY A 17 ? 0.4752 1.1376 0.7281 -0.0199 -0.1095 -0.0887 17 GLY A N 94 C CA . GLY A 17 ? 0.4661 1.1156 0.7209 -0.0045 -0.0990 -0.0819 17 GLY A CA 95 C C . GLY A 17 ? 0.4527 1.1457 0.7406 0.0073 -0.0995 -0.0844 17 GLY A C 96 O O . GLY A 17 ? 0.4466 1.1830 0.7601 -0.0007 -0.1048 -0.0924 17 GLY A O 97 N N . THR A 18 ? 0.4504 1.1321 0.7379 0.0266 -0.0939 -0.0784 18 THR A N 98 C CA . THR A 18 ? 0.4534 1.1719 0.7712 0.0402 -0.0914 -0.0813 18 THR A CA 99 C C . THR A 18 ? 0.4770 1.1839 0.7888 0.0691 -0.0981 -0.0736 18 THR A C 100 O O . THR A 18 ? 0.4922 1.1547 0.7756 0.0759 -0.0967 -0.0653 18 THR A O 101 C CB . THR A 18 ? 0.4428 1.1607 0.7702 0.0303 -0.0715 -0.0846 18 THR A CB 102 O OG1 . THR A 18 ? 0.4470 1.2037 0.8046 0.0442 -0.0684 -0.0888 18 THR A OG1 103 C CG2 . THR A 18 ? 0.4374 1.1030 0.7361 0.0336 -0.0608 -0.0771 18 THR A CG2 104 N N . ARG A 19 ? 0.5030 1.2504 0.8423 0.0858 -0.1056 -0.0767 19 ARG A N 105 C CA . ARG A 19 ? 0.5314 1.2700 0.8688 0.1148 -0.1118 -0.0704 19 ARG A CA 106 C C . ARG A 19 ? 0.5347 1.2614 0.8767 0.1210 -0.0945 -0.0715 19 ARG A C 107 O O . ARG A 19 ? 0.5303 1.2906 0.8988 0.1149 -0.0840 -0.0801 19 ARG A O 108 C CB . ARG A 19 ? 0.5569 1.3460 0.9247 0.1312 -0.1265 -0.0745 19 ARG A CB 109 C CG . ARG A 19 ? 0.5934 1.3681 0.9507 0.1600 -0.1415 -0.0655 19 ARG A CG 110 C CD . ARG A 19 ? 0.6063 1.4301 1.0000 0.1817 -0.1500 -0.0709 19 ARG A CD 111 N NE . ARG A 19 ? 0.6421 1.4614 1.0275 0.2062 -0.1706 -0.0626 19 ARG A NE 112 C CZ . ARG A 19 ? 0.6593 1.5058 1.0684 0.2331 -0.1799 -0.0639 19 ARG A CZ 113 N NH1 . ARG A 19 ? 0.6509 1.5335 1.0949 0.2396 -0.1694 -0.0742 19 ARG A NH1 114 N NH2 . ARG A 19 ? 0.6712 1.5079 1.0680 0.2543 -0.1997 -0.0547 19 ARG A NH2 115 N N . VAL A 20 ? 0.5397 1.2191 0.8552 0.1315 -0.0910 -0.0633 20 VAL A N 116 C CA . VAL A 20 ? 0.5430 1.2072 0.8592 0.1385 -0.0757 -0.0645 20 VAL A CA 117 C C . VAL A 20 ? 0.5589 1.2120 0.8743 0.1680 -0.0823 -0.0602 20 VAL A C 118 O O . VAL A 20 ? 0.5832 1.2140 0.8805 0.1792 -0.0957 -0.0515 20 VAL A O 119 C CB . VAL A 20 ? 0.5311 1.1469 0.8174 0.1241 -0.0636 -0.0599 20 VAL A CB 120 C CG1 . VAL A 20 ? 0.5217 1.1432 0.8067 0.0961 -0.0577 -0.0637 20 VAL A CG1 121 C CG2 . VAL A 20 ? 0.5474 1.1180 0.8020 0.1318 -0.0720 -0.0492 20 VAL A CG2 122 N N . PRO A 21 ? 0.5488 1.2164 0.8825 0.1805 -0.0726 -0.0663 21 PRO A N 123 C CA . PRO A 21 ? 0.5614 1.2137 0.8931 0.2091 -0.0781 -0.0632 21 PRO A CA 124 C C . PRO A 21 ? 0.5741 1.1665 0.8714 0.2110 -0.0727 -0.0551 21 PRO A C 125 O O . PRO A 21 ? 0.5518 1.1216 0.8332 0.1922 -0.0605 -0.0549 21 PRO A O 126 C CB . PRO A 21 ? 0.5515 1.2415 0.9148 0.2187 -0.0671 -0.0747 21 PRO A CB 127 C CG . PRO A 21 ? 0.5343 1.2333 0.9001 0.1923 -0.0498 -0.0805 21 PRO A CG 128 C CD . PRO A 21 ? 0.5288 1.2270 0.8848 0.1690 -0.0560 -0.0767 21 PRO A CD 129 N N . VAL A 22 ? 0.6020 1.1690 0.8880 0.2335 -0.0824 -0.0485 22 VAL A N 130 C CA . VAL A 22 ? 0.6246 1.1359 0.8795 0.2366 -0.0787 -0.0411 22 VAL A CA 131 C C . VAL A 22 ? 0.6624 1.1570 0.9155 0.2656 -0.0883 -0.0373 22 VAL A C 132 O O . VAL A 22 ? 0.6671 1.1711 0.9234 0.2792 -0.1046 -0.0320 22 VAL A O 133 C CB . VAL A 22 ? 0.6319 1.1103 0.8566 0.2198 -0.0835 -0.0308 22 VAL A CB 134 C CG1 . VAL A 22 ? 0.6432 1.1323 0.8655 0.2254 -0.1018 -0.0240 22 VAL A CG1 135 C CG2 . VAL A 22 ? 0.6551 1.0788 0.8499 0.2222 -0.0796 -0.0233 22 VAL A CG2 136 N N . LEU A 23 ? 0.6840 1.1533 0.9312 0.2753 -0.0786 -0.0403 23 LEU A N 137 C CA . LEU A 23 ? 0.7255 1.1733 0.9699 0.3032 -0.0861 -0.0380 23 LEU A CA 138 C C . LEU A 23 ? 0.7451 1.2301 1.0144 0.3250 -0.1012 -0.0392 23 LEU A C 139 O O . LEU A 23 ? 0.7491 1.2130 1.0066 0.3419 -0.1168 -0.0296 23 LEU A O 140 C CB . LEU A 23 ? 0.7548 1.1444 0.9624 0.3030 -0.0928 -0.0245 23 LEU A CB 141 C CG . LEU A 23 ? 0.7511 1.1038 0.9345 0.2827 -0.0795 -0.0230 23 LEU A CG 142 C CD1 . LEU A 23 ? 0.7630 1.0671 0.9129 0.2782 -0.0869 -0.0091 23 LEU A CD1 143 C CD2 . LEU A 23 ? 0.7536 1.0934 0.9395 0.2904 -0.0666 -0.0322 23 LEU A CD2 144 N N . SER A 24 ? 0.7479 1.2889 1.0517 0.3240 -0.0965 -0.0508 24 SER A N 145 C CA . SER A 24 ? 0.7678 1.3560 1.1024 0.3427 -0.1101 -0.0544 24 SER A CA 146 C C . SER A 24 ? 0.7537 1.3415 1.0774 0.3415 -0.1301 -0.0429 24 SER A C 147 O O . SER A 24 ? 0.7623 1.3488 1.0874 0.3647 -0.1470 -0.0373 24 SER A O 148 C CB . SER A 24 ? 0.8090 1.3935 1.1556 0.3760 -0.1133 -0.0588 24 SER A CB 149 O OG . SER A 24 ? 0.8558 1.3784 1.1692 0.3873 -0.1191 -0.0480 24 SER A OG 150 N N . SER A 25 ? 0.7280 1.3152 1.0390 0.3142 -0.1278 -0.0397 25 SER A N 151 C CA . SER A 25 ? 0.7095 1.3033 1.0111 0.3076 -0.1441 -0.0315 25 SER A CA 152 C C . SER A 25 ? 0.6828 1.2956 0.9870 0.2762 -0.1343 -0.0366 25 SER A C 153 O O . SER A 25 ? 0.6579 1.2825 0.9745 0.2642 -0.1173 -0.0457 25 SER A O 154 C CB . SER A 25 ? 0.7224 1.2589 0.9834 0.3105 -0.1527 -0.0161 25 SER A CB 155 O OG . SER A 25 ? 0.7191 1.2616 0.9679 0.3031 -0.1675 -0.0084 25 SER A OG 156 N N . HIS A 26 ? 0.6830 1.2977 0.9744 0.2627 -0.1448 -0.0311 26 HIS A N 157 C CA . HIS A 26 ? 0.6735 1.3049 0.9674 0.2336 -0.1368 -0.0366 26 HIS A CA 158 C C . HIS A 26 ? 0.6548 1.2530 0.9144 0.2187 -0.1425 -0.0272 26 HIS A C 159 O O . HIS A 26 ? 0.6898 1.2685 0.9299 0.2303 -0.1567 -0.0170 26 HIS A O 160 C CB . HIS A 26 ? 0.7069 1.4006 1.0359 0.2300 -0.1435 -0.0463 26 HIS A CB 161 C CG . HIS A 26 ? 0.7635 1.4974 1.1295 0.2482 -0.1407 -0.0556 26 HIS A CG 162 N ND1 . HIS A 26 ? 0.7696 1.5206 1.1548 0.2401 -0.1217 -0.0658 26 HIS A ND1 163 C CD2 . HIS A 26 ? 0.7950 1.5562 1.1822 0.2747 -0.1544 -0.0565 26 HIS A CD2 164 C CE1 . HIS A 26 ? 0.7710 1.5596 1.1883 0.2605 -0.1227 -0.0734 26 HIS A CE1 165 N NE2 . HIS A 26 ? 0.8097 1.6053 1.2299 0.2824 -0.1427 -0.0682 26 HIS A NE2 166 N N . ILE A 27 ? 0.5927 1.1835 0.8443 0.1933 -0.1307 -0.0306 27 ILE A N 167 C CA . ILE A 27 ? 0.5759 1.1444 0.8001 0.1765 -0.1346 -0.0252 27 ILE A CA 168 C C . ILE A 27 ? 0.5472 1.1377 0.7815 0.1505 -0.1270 -0.0344 27 ILE A C 169 O O . ILE A 27 ? 0.5301 1.1489 0.7900 0.1442 -0.1175 -0.0436 27 ILE A O 170 C CB . ILE A 27 ? 0.5852 1.0982 0.7760 0.1744 -0.1273 -0.0161 27 ILE A CB 171 C CG1 . ILE A 27 ? 0.5745 1.0735 0.7688 0.1666 -0.1085 -0.0211 27 ILE A CG1 172 C CG2 . ILE A 27 ? 0.6113 1.0984 0.7875 0.1975 -0.1369 -0.0056 27 ILE A CG2 173 C CD1 . ILE A 27 ? 0.5854 1.0335 0.7493 0.1632 -0.1016 -0.0133 27 ILE A CD1 174 N N . SER A 28 ? 0.5426 1.1192 0.7558 0.1354 -0.1313 -0.0320 28 SER A N 175 C CA . SER A 28 ? 0.5204 1.1122 0.7394 0.1109 -0.1260 -0.0405 28 SER A CA 176 C C . SER A 28 ? 0.4998 1.0569 0.7039 0.0971 -0.1090 -0.0403 28 SER A C 177 O O . SER A 28 ? 0.5077 1.0262 0.6895 0.1034 -0.1052 -0.0326 28 SER A O 178 C CB . SER A 28 ? 0.5376 1.1302 0.7398 0.1022 -0.1390 -0.0393 28 SER A CB 179 O OG . SER A 28 ? 0.5638 1.1775 0.7703 0.1189 -0.1570 -0.0357 28 SER A OG 180 N N . ALA A 29 ? 0.4768 1.0476 0.6935 0.0782 -0.0991 -0.0486 29 ALA A N 181 C CA . ALA A 29 ? 0.4602 0.9990 0.6623 0.0641 -0.0844 -0.0485 29 ALA A CA 182 C C . ALA A 29 ? 0.4448 0.9911 0.6480 0.0403 -0.0819 -0.0555 29 ALA A C 183 O O . ALA A 29 ? 0.4521 1.0353 0.6783 0.0319 -0.0839 -0.0631 29 ALA A O 184 C CB . ALA A 29 ? 0.4585 0.9989 0.6737 0.0682 -0.0708 -0.0504 29 ALA A CB 185 N N . PHE A 30 ? 0.4248 0.9361 0.6038 0.0296 -0.0777 -0.0534 30 PHE A N 186 C CA . PHE A 30 ? 0.4147 0.9246 0.5910 0.0076 -0.0748 -0.0600 30 PHE A CA 187 C C . PHE A 30 ? 0.4103 0.8887 0.5758 -0.0008 -0.0605 -0.0586 30 PHE A C 188 O O . PHE A 30 ? 0.4205 0.8647 0.5642 0.0030 -0.0582 -0.0532 30 PHE A O 189 C CB . PHE A 30 ? 0.4104 0.9080 0.5662 0.0036 -0.0850 -0.0599 30 PHE A CB 190 C CG . PHE A 30 ? 0.3959 0.9208 0.5573 0.0133 -0.1007 -0.0598 30 PHE A CG 191 C CD1 . PHE A 30 ? 0.3925 0.9115 0.5461 0.0337 -0.1075 -0.0510 30 PHE A CD1 192 C CD2 . PHE A 30 ? 0.3915 0.9473 0.5654 0.0019 -0.1092 -0.0682 30 PHE A CD2 193 C CE1 . PHE A 30 ? 0.4003 0.9431 0.5575 0.0438 -0.1231 -0.0497 30 PHE A CE1 194 C CE2 . PHE A 30 ? 0.4043 0.9866 0.5829 0.0114 -0.1251 -0.0679 30 PHE A CE2 195 C CZ . PHE A 30 ? 0.4084 0.9841 0.5783 0.0331 -0.1323 -0.0582 30 PHE A CZ 196 N N . LEU A 31 ? 0.4179 0.9092 0.5987 -0.0123 -0.0511 -0.0632 31 LEU A N 197 C CA . LEU A 31 ? 0.4145 0.8796 0.5867 -0.0186 -0.0377 -0.0612 31 LEU A CA 198 C C . LEU A 31 ? 0.4256 0.8809 0.5932 -0.0409 -0.0335 -0.0660 31 LEU A C 199 O O . LEU A 31 ? 0.4309 0.9125 0.6139 -0.0539 -0.0355 -0.0725 31 LEU A O 200 C CB . LEU A 31 ? 0.4125 0.8985 0.6038 -0.0138 -0.0288 -0.0620 31 LEU A CB 201 C CG . LEU A 31 ? 0.4057 0.9091 0.6082 0.0085 -0.0333 -0.0597 31 LEU A CG 202 C CD1 . LEU A 31 ? 0.4010 0.9311 0.6254 0.0103 -0.0235 -0.0636 31 LEU A CD1 203 C CD2 . LEU A 31 ? 0.4039 0.8708 0.5846 0.0230 -0.0336 -0.0519 31 LEU A CD2 204 N N . GLY A 32 ? 0.4378 0.8550 0.5844 -0.0453 -0.0280 -0.0629 32 GLY A N 205 C CA . GLY A 32 ? 0.4419 0.8428 0.5820 -0.0649 -0.0228 -0.0664 32 GLY A CA 206 C C . GLY A 32 ? 0.4433 0.8410 0.5765 -0.0748 -0.0314 -0.0721 32 GLY A C 207 O O . GLY A 32 ? 0.4489 0.8519 0.5874 -0.0926 -0.0304 -0.0780 32 GLY A O 208 N N . ILE A 33 ? 0.4500 0.8378 0.5699 -0.0641 -0.0393 -0.0705 33 ILE A N 209 C CA . ILE A 33 ? 0.4613 0.8429 0.5701 -0.0714 -0.0473 -0.0764 33 ILE A CA 210 C C . ILE A 33 ? 0.4733 0.8155 0.5625 -0.0775 -0.0418 -0.0767 33 ILE A C 211 O O . ILE A 33 ? 0.4915 0.8111 0.5695 -0.0675 -0.0371 -0.0704 33 ILE A O 212 C CB . ILE A 33 ? 0.4539 0.8392 0.5531 -0.0569 -0.0570 -0.0737 33 ILE A CB 213 C CG1 . ILE A 33 ? 0.4505 0.8726 0.5678 -0.0470 -0.0644 -0.0723 33 ILE A CG1 214 C CG2 . ILE A 33 ? 0.4735 0.8520 0.5589 -0.0651 -0.0642 -0.0808 33 ILE A CG2 215 C CD1 . ILE A 33 ? 0.4604 0.8823 0.5658 -0.0311 -0.0737 -0.0670 33 ILE A CD1 216 N N . PRO A 34 ? 0.4792 0.8124 0.5642 -0.0934 -0.0428 -0.0843 34 PRO A N 217 C CA . PRO A 34 ? 0.4944 0.7890 0.5617 -0.0980 -0.0379 -0.0851 34 PRO A CA 218 C C . PRO A 34 ? 0.4957 0.7743 0.5450 -0.0903 -0.0428 -0.0875 34 PRO A C 219 O O . PRO A 34 ? 0.4963 0.7883 0.5433 -0.0926 -0.0509 -0.0938 34 PRO A O 220 C CB . PRO A 34 ? 0.5119 0.8039 0.5830 -0.1185 -0.0374 -0.0929 34 PRO A CB 221 C CG . PRO A 34 ? 0.5137 0.8419 0.5987 -0.1240 -0.0461 -0.0992 34 PRO A CG 222 C CD . PRO A 34 ? 0.4900 0.8474 0.5879 -0.1087 -0.0480 -0.0928 34 PRO A CD 223 N N . PHE A 35 ? 0.4950 0.7469 0.5314 -0.0815 -0.0378 -0.0829 35 PHE A N 224 C CA . PHE A 35 ? 0.5035 0.7407 0.5232 -0.0746 -0.0405 -0.0854 35 PHE A CA 225 C C . PHE A 35 ? 0.5110 0.7171 0.5189 -0.0806 -0.0371 -0.0913 35 PHE A C 226 O O . PHE A 35 ? 0.5244 0.7186 0.5191 -0.0761 -0.0384 -0.0956 35 PHE A O 227 C CB . PHE A 35 ? 0.5064 0.7410 0.5213 -0.0588 -0.0384 -0.0765 35 PHE A CB 228 C CG . PHE A 35 ? 0.5149 0.7304 0.5300 -0.0546 -0.0304 -0.0699 35 PHE A CG 229 C CD1 . PHE A 35 ? 0.5297 0.7183 0.5337 -0.0533 -0.0266 -0.0711 35 PHE A CD1 230 C CD2 . PHE A 35 ? 0.5189 0.7444 0.5450 -0.0508 -0.0271 -0.0629 35 PHE A CD2 231 C CE1 . PHE A 35 ? 0.5294 0.7017 0.5331 -0.0490 -0.0207 -0.0650 35 PHE A CE1 232 C CE2 . PHE A 35 ? 0.5059 0.7139 0.5301 -0.0472 -0.0204 -0.0573 35 PHE A CE2 233 C CZ . PHE A 35 ? 0.5169 0.6984 0.5297 -0.0465 -0.0177 -0.0580 35 PHE A CZ 234 N N . ALA A 36 ? 0.5101 0.7029 0.5222 -0.0907 -0.0328 -0.0915 36 ALA A N 235 C CA . ALA A 36 ? 0.5313 0.6918 0.5325 -0.0961 -0.0304 -0.0965 36 ALA A CA 236 C C . ALA A 36 ? 0.5622 0.7160 0.5684 -0.1132 -0.0292 -0.0993 36 ALA A C 237 O O . ALA A 36 ? 0.5900 0.7647 0.6096 -0.1203 -0.0279 -0.0960 36 ALA A O 238 C CB . ALA A 36 ? 0.5226 0.6609 0.5178 -0.0856 -0.0247 -0.0893 36 ALA A CB 239 N N . GLU A 37 ? 0.6005 0.7244 0.5959 -0.1200 -0.0291 -0.1057 37 GLU A N 240 C CA . GLU A 37 ? 0.6221 0.7306 0.6187 -0.1366 -0.0268 -0.1065 37 GLU A CA 241 C C . GLU A 37 ? 0.6104 0.7084 0.6085 -0.1342 -0.0197 -0.0948 37 GLU A C 242 O O . GLU A 37 ? 0.6031 0.6915 0.5961 -0.1197 -0.0174 -0.0889 37 GLU A O 243 C CB . GLU A 37 ? 0.6545 0.7275 0.6367 -0.1420 -0.0288 -0.1156 37 GLU A CB 244 C CG . GLU A 37 ? 0.6797 0.7621 0.6595 -0.1491 -0.0357 -0.1289 37 GLU A CG 245 C CD . GLU A 37 ? 0.6877 0.7922 0.6795 -0.1682 -0.0384 -0.1325 37 GLU A CD 246 O OE1 . GLU A 37 ? 0.6975 0.7864 0.6907 -0.1833 -0.0352 -0.1309 37 GLU A OE1 247 O OE2 . GLU A 37 ? 0.6770 0.8151 0.6768 -0.1686 -0.0440 -0.1366 37 GLU A OE2 248 N N . PRO A 38 ? 0.6225 0.7238 0.6272 -0.1493 -0.0160 -0.0916 38 PRO A N 249 C CA . PRO A 38 ? 0.6206 0.7085 0.6227 -0.1483 -0.0090 -0.0809 38 PRO A CA 250 C C . PRO A 38 ? 0.6452 0.6889 0.6296 -0.1442 -0.0087 -0.0793 38 PRO A C 251 O O . PRO A 38 ? 0.7093 0.7276 0.6852 -0.1548 -0.0109 -0.0849 38 PRO A O 252 C CB . PRO A 38 ? 0.6318 0.7292 0.6419 -0.1690 -0.0050 -0.0800 38 PRO A CB 253 C CG . PRO A 38 ? 0.6285 0.7582 0.6523 -0.1770 -0.0102 -0.0891 38 PRO A CG 254 C CD . PRO A 38 ? 0.6315 0.7509 0.6464 -0.1684 -0.0177 -0.0977 38 PRO A CD 255 N N . PRO A 39 ? 0.6258 0.6600 0.6049 -0.1288 -0.0068 -0.0721 39 PRO A N 256 C CA . PRO A 39 ? 0.6379 0.6335 0.6022 -0.1222 -0.0078 -0.0706 39 PRO A CA 257 C C . PRO A 39 ? 0.6466 0.6166 0.6019 -0.1325 -0.0040 -0.0625 39 PRO A C 258 O O . PRO A 39 ? 0.6270 0.5890 0.5772 -0.1251 -0.0013 -0.0533 39 PRO A O 259 C CB . PRO A 39 ? 0.6235 0.6268 0.5887 -0.1029 -0.0075 -0.0661 39 PRO A CB 260 C CG . PRO A 39 ? 0.6050 0.6397 0.5815 -0.1030 -0.0036 -0.0599 39 PRO A CG 261 C CD . PRO A 39 ? 0.6008 0.6594 0.5879 -0.1169 -0.0040 -0.0651 39 PRO A CD 262 N N . VAL A 40 ? 0.6685 0.6246 0.6203 -0.1504 -0.0041 -0.0659 40 VAL A N 263 C CA . VAL A 40 ? 0.6980 0.6315 0.6406 -0.1644 0.0003 -0.0577 40 VAL A CA 264 C C . VAL A 40 ? 0.7354 0.6212 0.6609 -0.1692 -0.0035 -0.0597 40 VAL A C 265 O O . VAL A 40 ? 0.7512 0.6253 0.6746 -0.1653 -0.0090 -0.0701 40 VAL A O 266 C CB . VAL A 40 ? 0.7010 0.6603 0.6548 -0.1853 0.0050 -0.0581 40 VAL A CB 267 C CG1 . VAL A 40 ? 0.6698 0.6724 0.6394 -0.1792 0.0096 -0.0542 40 VAL A CG1 268 C CG2 . VAL A 40 ? 0.7020 0.6699 0.6629 -0.1963 0.0002 -0.0707 40 VAL A CG2 269 N N . GLY A 41 ? 0.7758 0.6334 0.6878 -0.1776 -0.0005 -0.0497 41 GLY A N 270 C CA . GLY A 41 ? 0.8375 0.6447 0.7309 -0.1825 -0.0041 -0.0491 41 GLY A CA 271 C C . GLY A 41 ? 0.8743 0.6578 0.7605 -0.1605 -0.0109 -0.0529 41 GLY A C 272 O O . GLY A 41 ? 0.8865 0.6750 0.7726 -0.1431 -0.0114 -0.0471 41 GLY A O 273 N N . ASN A 42 ? 0.9284 0.6880 0.8097 -0.1614 -0.0161 -0.0639 42 ASN A N 274 C CA . ASN A 42 ? 0.9521 0.6910 0.8285 -0.1406 -0.0221 -0.0704 42 ASN A CA 275 C C . ASN A 42 ? 0.8973 0.6739 0.7882 -0.1233 -0.0224 -0.0770 42 ASN A C 276 O O . ASN A 42 ? 0.8948 0.6614 0.7842 -0.1057 -0.0261 -0.0830 42 ASN A O 277 C CB . ASN A 42 ? 1.0180 0.7216 0.8849 -0.1470 -0.0268 -0.0821 42 ASN A CB 278 C CG . ASN A 42 ? 1.0491 0.7770 0.9257 -0.1620 -0.0263 -0.0945 42 ASN A CG 279 O OD1 . ASN A 42 ? 1.0819 0.8238 0.9629 -0.1829 -0.0228 -0.0916 42 ASN A OD1 280 N ND2 . ASN A 42 ? 1.0535 0.7877 0.9332 -0.1516 -0.0299 -0.1089 42 ASN A ND2 281 N N . MET A 43 ? 0.8607 0.6804 0.7656 -0.1281 -0.0185 -0.0761 43 MET A N 282 C CA . MET A 43 ? 0.8362 0.6904 0.7530 -0.1130 -0.0185 -0.0799 43 MET A CA 283 C C . MET A 43 ? 0.7955 0.6660 0.7164 -0.1021 -0.0155 -0.0685 43 MET A C 284 O O . MET A 43 ? 0.7619 0.6576 0.6914 -0.0893 -0.0154 -0.0701 43 MET A O 285 C CB . MET A 43 ? 0.8511 0.7413 0.7798 -0.1227 -0.0177 -0.0870 43 MET A CB 286 C CG . MET A 43 ? 0.9097 0.7874 0.8343 -0.1317 -0.0216 -0.1007 43 MET A CG 287 S SD . MET A 43 ? 0.9646 0.8847 0.9003 -0.1293 -0.0238 -0.1117 43 MET A SD 288 C CE . MET A 43 ? 0.9273 0.8873 0.8784 -0.1435 -0.0207 -0.1045 43 MET A CE 289 N N . ARG A 44 ? 0.7870 0.6423 0.7004 -0.1076 -0.0132 -0.0571 44 ARG A N 290 C CA . ARG A 44 ? 0.7410 0.6069 0.6554 -0.0968 -0.0112 -0.0471 44 ARG A CA 291 C C . ARG A 44 ? 0.7151 0.5692 0.6274 -0.0768 -0.0159 -0.0494 44 ARG A C 292 O O . ARG A 44 ? 0.7143 0.5371 0.6179 -0.0726 -0.0203 -0.0531 44 ARG A O 293 C CB . ARG A 44 ? 0.7488 0.5955 0.6512 -0.1062 -0.0083 -0.0349 44 ARG A CB 294 C CG . ARG A 44 ? 0.7083 0.5689 0.6110 -0.0966 -0.0060 -0.0256 44 ARG A CG 295 C CD . ARG A 44 ? 0.7213 0.5574 0.6073 -0.1033 -0.0042 -0.0135 44 ARG A CD 296 N NE . ARG A 44 ? 0.7173 0.5648 0.6034 -0.1227 0.0033 -0.0095 44 ARG A NE 297 C CZ . ARG A 44 ? 0.7299 0.5571 0.6000 -0.1342 0.0068 0.0006 44 ARG A CZ 298 N NH1 . ARG A 44 ? 0.7483 0.5405 0.5997 -0.1275 0.0021 0.0086 44 ARG A NH1 299 N NH2 . ARG A 44 ? 0.7326 0.5756 0.6055 -0.1525 0.0149 0.0030 44 ARG A NH2 300 N N . PHE A 45 ? 0.6908 0.5708 0.6121 -0.0649 -0.0149 -0.0477 45 PHE A N 301 C CA . PHE A 45 ? 0.6845 0.5633 0.6081 -0.0465 -0.0183 -0.0502 45 PHE A CA 302 C C . PHE A 45 ? 0.6889 0.5777 0.6192 -0.0398 -0.0196 -0.0627 45 PHE A C 303 O O . PHE A 45 ? 0.7087 0.6081 0.6447 -0.0260 -0.0204 -0.0652 45 PHE A O 304 C CB . PHE A 45 ? 0.7051 0.5491 0.6173 -0.0387 -0.0232 -0.0457 45 PHE A CB 305 C CG . PHE A 45 ? 0.7280 0.5588 0.6295 -0.0452 -0.0223 -0.0329 45 PHE A CG 306 C CD1 . PHE A 45 ? 0.7157 0.5694 0.6209 -0.0445 -0.0189 -0.0257 45 PHE A CD1 307 C CD2 . PHE A 45 ? 0.7675 0.5610 0.6534 -0.0522 -0.0249 -0.0281 45 PHE A CD2 308 C CE1 . PHE A 45 ? 0.7338 0.5759 0.6271 -0.0507 -0.0175 -0.0147 45 PHE A CE1 309 C CE2 . PHE A 45 ? 0.7843 0.5651 0.6574 -0.0589 -0.0236 -0.0157 45 PHE A CE2 310 C CZ . PHE A 45 ? 0.7676 0.5740 0.6444 -0.0582 -0.0196 -0.0093 45 PHE A CZ 311 N N . ARG A 46 ? 0.7200 0.6069 0.6494 -0.0503 -0.0196 -0.0708 46 ARG A N 312 C CA . ARG A 46 ? 0.7312 0.6263 0.6638 -0.0451 -0.0207 -0.0835 46 ARG A CA 313 C C . ARG A 46 ? 0.6774 0.6111 0.6201 -0.0431 -0.0181 -0.0849 46 ARG A C 314 O O . ARG A 46 ? 0.6572 0.6109 0.6052 -0.0480 -0.0157 -0.0773 46 ARG A O 315 C CB . ARG A 46 ? 0.7801 0.6591 0.7067 -0.0579 -0.0224 -0.0926 46 ARG A CB 316 C CG . ARG A 46 ? 0.8435 0.6788 0.7581 -0.0585 -0.0258 -0.0937 46 ARG A CG 317 C CD . ARG A 46 ? 0.9003 0.7198 0.8091 -0.0680 -0.0279 -0.1066 46 ARG A CD 318 N NE . ARG A 46 ? 0.9254 0.7619 0.8380 -0.0585 -0.0280 -0.1196 46 ARG A NE 319 C CZ . ARG A 46 ? 0.9674 0.7857 0.8757 -0.0459 -0.0300 -0.1301 46 ARG A CZ 320 N NH1 . ARG A 46 ? 1.0064 0.7861 0.9067 -0.0397 -0.0332 -0.1298 46 ARG A NH1 321 N NH2 . ARG A 46 ? 0.9559 0.7950 0.8673 -0.0390 -0.0286 -0.1414 46 ARG A NH2 322 N N . ARG A 47 ? 0.6683 0.6110 0.6123 -0.0353 -0.0184 -0.0946 47 ARG A N 323 C CA . ARG A 47 ? 0.6337 0.6092 0.5836 -0.0347 -0.0167 -0.0966 47 ARG A CA 324 C C . ARG A 47 ? 0.6119 0.6000 0.5630 -0.0495 -0.0175 -0.0978 47 ARG A C 325 O O . ARG A 47 ? 0.6145 0.5858 0.5610 -0.0601 -0.0193 -0.1023 47 ARG A O 326 C CB . ARG A 47 ? 0.6218 0.6009 0.5693 -0.0260 -0.0165 -0.1081 47 ARG A CB 327 N N . PRO A 48 ? 0.5852 0.6028 0.5429 -0.0504 -0.0166 -0.0937 48 PRO A N 328 C CA . PRO A 48 ? 0.5920 0.6254 0.5531 -0.0632 -0.0183 -0.0955 48 PRO A CA 329 C C . PRO A 48 ? 0.6169 0.6540 0.5728 -0.0672 -0.0217 -0.1082 48 PRO A C 330 O O . PRO A 48 ? 0.6184 0.6568 0.5692 -0.0581 -0.0216 -0.1139 48 PRO A O 331 C CB . PRO A 48 ? 0.5578 0.6207 0.5271 -0.0589 -0.0172 -0.0876 48 PRO A CB 332 C CG . PRO A 48 ? 0.5489 0.6135 0.5158 -0.0451 -0.0157 -0.0865 48 PRO A CG 333 C CD . PRO A 48 ? 0.5658 0.6030 0.5282 -0.0400 -0.0145 -0.0873 48 PRO A CD 334 N N . GLU A 49 ? 0.6495 0.6895 0.6066 -0.0814 -0.0245 -0.1128 49 GLU A N 335 C CA . GLU A 49 ? 0.6923 0.7400 0.6446 -0.0871 -0.0288 -0.1249 49 GLU A CA 336 C C . GLU A 49 ? 0.6590 0.7426 0.6194 -0.0911 -0.0318 -0.1225 49 GLU A C 337 O O . GLU A 49 ? 0.6417 0.7397 0.6129 -0.0945 -0.0306 -0.1138 49 GLU A O 338 C CB . GLU A 49 ? 0.7690 0.7943 0.7168 -0.1017 -0.0311 -0.1331 49 GLU A CB 339 C CG . GLU A 49 ? 0.8428 0.8283 0.7813 -0.0978 -0.0296 -0.1360 49 GLU A CG 340 C CD . GLU A 49 ? 0.9222 0.8820 0.8549 -0.1138 -0.0322 -0.1434 49 GLU A CD 341 O OE1 . GLU A 49 ? 0.9493 0.9250 0.8862 -0.1289 -0.0351 -0.1475 49 GLU A OE1 342 O OE2 . GLU A 49 ? 0.9729 0.8962 0.8970 -0.1114 -0.0318 -0.1453 49 GLU A OE2 343 N N . PRO A 50 ? 0.6519 0.7505 0.6066 -0.0903 -0.0360 -0.1307 50 PRO A N 344 C CA . PRO A 50 ? 0.6276 0.7599 0.5895 -0.0931 -0.0406 -0.1280 50 PRO A CA 345 C C . PRO A 50 ? 0.6343 0.7761 0.6060 -0.1095 -0.0442 -0.1309 50 PRO A C 346 O O . PRO A 50 ? 0.6256 0.7481 0.5931 -0.1211 -0.0451 -0.1395 50 PRO A O 347 C CB . PRO A 50 ? 0.6304 0.7714 0.5797 -0.0898 -0.0449 -0.1372 50 PRO A CB 348 C CG . PRO A 50 ? 0.6538 0.7665 0.5906 -0.0855 -0.0413 -0.1458 50 PRO A CG 349 C CD . PRO A 50 ? 0.6623 0.7471 0.6032 -0.0887 -0.0375 -0.1438 50 PRO A CD 350 N N . LYS A 51 ? 0.6283 0.7998 0.6134 -0.1103 -0.0461 -0.1240 51 LYS A N 351 C CA . LYS A 51 ? 0.6470 0.8358 0.6449 -0.1257 -0.0494 -0.1268 51 LYS A CA 352 C C . LYS A 51 ? 0.6730 0.8676 0.6652 -0.1367 -0.0574 -0.1404 51 LYS A C 353 O O . LYS A 51 ? 0.6532 0.8615 0.6377 -0.1302 -0.0631 -0.1443 51 LYS A O 354 C CB . LYS A 51 ? 0.6312 0.8557 0.6453 -0.1210 -0.0510 -0.1184 51 LYS A CB 355 C CG . LYS A 51 ? 0.6412 0.8891 0.6730 -0.1363 -0.0530 -0.1207 51 LYS A CG 356 C CD . LYS A 51 ? 0.6606 0.8867 0.6950 -0.1492 -0.0456 -0.1193 51 LYS A CD 357 C CE . LYS A 51 ? 0.6657 0.9195 0.7200 -0.1641 -0.0452 -0.1196 51 LYS A CE 358 N NZ . LYS A 51 ? 0.6903 0.9186 0.7422 -0.1815 -0.0392 -0.1205 51 LYS A NZ 359 N N . LYS A 52 ? 0.7069 0.8896 0.7014 -0.1540 -0.0578 -0.1474 52 LYS A N 360 C CA . LYS A 52 ? 0.7457 0.9358 0.7370 -0.1674 -0.0659 -0.1609 52 LYS A CA 361 C C . LYS A 52 ? 0.7231 0.9587 0.7306 -0.1705 -0.0731 -0.1598 52 LYS A C 362 O O . LYS A 52 ? 0.6864 0.9415 0.7124 -0.1754 -0.0707 -0.1530 52 LYS A O 363 C CB . LYS A 52 ? 0.8094 0.9750 0.8006 -0.1870 -0.0643 -0.1676 52 LYS A CB 364 C CG . LYS A 52 ? 0.8620 0.9803 0.8352 -0.1837 -0.0599 -0.1715 52 LYS A CG 365 C CD . LYS A 52 ? 0.9183 1.0074 0.8914 -0.2016 -0.0569 -0.1732 52 LYS A CD 366 C CE . LYS A 52 ? 0.9671 1.0082 0.9234 -0.1937 -0.0525 -0.1741 52 LYS A CE 367 N NZ . LYS A 52 ? 1.0066 1.0131 0.9595 -0.2100 -0.0499 -0.1738 52 LYS A NZ 368 N N . PRO A 53 ? 0.7418 0.9952 0.7418 -0.1671 -0.0820 -0.1666 53 PRO A N 369 C CA . PRO A 53 ? 0.7417 1.0390 0.7567 -0.1691 -0.0910 -0.1661 53 PRO A CA 370 C C . PRO A 53 ? 0.7447 1.0596 0.7799 -0.1893 -0.0929 -0.1705 53 PRO A C 371 O O . PRO A 53 ? 0.7526 1.0432 0.7846 -0.2054 -0.0898 -0.1775 53 PRO A O 372 C CB . PRO A 53 ? 0.7572 1.0605 0.7551 -0.1683 -0.1011 -0.1768 53 PRO A CB 373 C CG . PRO A 53 ? 0.7661 1.0348 0.7409 -0.1577 -0.0951 -0.1782 53 PRO A CG 374 C CD . PRO A 53 ? 0.7658 1.0007 0.7426 -0.1606 -0.0843 -0.1753 53 PRO A CD 375 N N . TRP A 54 ? 0.7358 1.0927 0.7917 -0.1883 -0.0979 -0.1664 54 TRP A N 376 C CA . TRP A 54 ? 0.7412 1.1235 0.8205 -0.2070 -0.0991 -0.1701 54 TRP A CA 377 C C . TRP A 54 ? 0.7459 1.1733 0.8369 -0.2089 -0.1133 -0.1764 54 TRP A C 378 O O . TRP A 54 ? 0.7335 1.1786 0.8205 -0.1915 -0.1202 -0.1719 54 TRP A O 379 C CB . TRP A 54 ? 0.7069 1.1004 0.8057 -0.2033 -0.0891 -0.1580 54 TRP A CB 380 C CG . TRP A 54 ? 0.6691 1.0894 0.7760 -0.1818 -0.0914 -0.1484 54 TRP A CG 381 C CD1 . TRP A 54 ? 0.6629 1.1293 0.7901 -0.1778 -0.0998 -0.1482 54 TRP A CD1 382 C CD2 . TRP A 54 ? 0.6386 1.0399 0.7326 -0.1609 -0.0865 -0.1381 54 TRP A CD2 383 N NE1 . TRP A 54 ? 0.6398 1.1140 0.7662 -0.1550 -0.1003 -0.1378 54 TRP A NE1 384 C CE2 . TRP A 54 ? 0.6246 1.0591 0.7305 -0.1454 -0.0919 -0.1315 54 TRP A CE2 385 C CE3 . TRP A 54 ? 0.6409 1.0009 0.7151 -0.1539 -0.0783 -0.1339 54 TRP A CE3 386 C CZ2 . TRP A 54 ? 0.6079 1.0328 0.7053 -0.1247 -0.0890 -0.1209 54 TRP A CZ2 387 C CZ3 . TRP A 54 ? 0.6245 0.9788 0.6922 -0.1337 -0.0754 -0.1236 54 TRP A CZ3 388 C CH2 . TRP A 54 ? 0.6113 0.9965 0.6898 -0.1201 -0.0805 -0.1172 54 TRP A CH2 389 N N . SER A 55 ? 0.7643 1.2096 0.8690 -0.2306 -0.1182 -0.1865 55 SER A N 390 C CA . SER A 55 ? 0.7802 1.2752 0.9027 -0.2336 -0.1317 -0.1918 55 SER A CA 391 C C . SER A 55 ? 0.7620 1.2947 0.9167 -0.2319 -0.1273 -0.1837 55 SER A C 392 O O . SER A 55 ? 0.7630 1.2803 0.9231 -0.2315 -0.1137 -0.1754 55 SER A O 393 C CB . SER A 55 ? 0.8051 1.3047 0.9280 -0.2587 -0.1402 -0.2081 55 SER A CB 394 O OG . SER A 55 ? 0.8131 1.3029 0.9488 -0.2809 -0.1311 -0.2106 55 SER A OG 395 N N . GLY A 56 ? 0.7486 1.3312 0.9240 -0.2299 -0.1391 -0.1863 56 GLY A N 396 C CA . GLY A 56 ? 0.7013 1.3254 0.9094 -0.2254 -0.1359 -0.1799 56 GLY A CA 397 C C . GLY A 56 ? 0.6500 1.2688 0.8551 -0.1983 -0.1302 -0.1656 56 GLY A C 398 O O . GLY A 56 ? 0.6488 1.2379 0.8280 -0.1827 -0.1311 -0.1605 56 GLY A O 399 N N . VAL A 57 ? 0.6070 1.2546 0.8389 -0.1934 -0.1238 -0.1598 57 VAL A N 400 C CA . VAL A 57 ? 0.5602 1.2089 0.7936 -0.1677 -0.1196 -0.1475 57 VAL A CA 401 C C . VAL A 57 ? 0.5243 1.1431 0.7541 -0.1679 -0.1014 -0.1399 57 VAL A C 402 O O . VAL A 57 ? 0.4930 1.1194 0.7384 -0.1847 -0.0917 -0.1421 57 VAL A O 403 C CB . VAL A 57 ? 0.5419 1.2470 0.8081 -0.1575 -0.1265 -0.1470 57 VAL A CB 404 C CG1 . VAL A 57 ? 0.5291 1.2315 0.7920 -0.1284 -0.1261 -0.1352 57 VAL A CG1 405 C CG2 . VAL A 57 ? 0.5552 1.2951 0.8286 -0.1619 -0.1455 -0.1561 57 VAL A CG2 406 N N . TRP A 58 ? 0.5234 1.1084 0.7318 -0.1500 -0.0970 -0.1307 58 TRP A N 407 C CA . TRP A 58 ? 0.5192 1.0784 0.7237 -0.1461 -0.0815 -0.1224 58 TRP A CA 408 C C . TRP A 58 ? 0.5205 1.1113 0.7474 -0.1303 -0.0784 -0.1163 58 TRP A C 409 O O . TRP A 58 ? 0.5143 1.1170 0.7412 -0.1096 -0.0866 -0.1119 58 TRP A O 410 C CB . TRP A 58 ? 0.5093 1.0216 0.6833 -0.1339 -0.0786 -0.1160 58 TRP A CB 411 C CG . TRP A 58 ? 0.4997 0.9834 0.6681 -0.1326 -0.0637 -0.1086 58 TRP A CG 412 C CD1 . TRP A 58 ? 0.4803 0.9651 0.6529 -0.1164 -0.0571 -0.0998 58 TRP A CD1 413 C CD2 . TRP A 58 ? 0.5102 0.9594 0.6666 -0.1483 -0.0543 -0.1097 58 TRP A CD2 414 N NE1 . TRP A 58 ? 0.4720 0.9271 0.6359 -0.1213 -0.0445 -0.0954 58 TRP A NE1 415 C CE2 . TRP A 58 ? 0.4896 0.9223 0.6434 -0.1404 -0.0428 -0.1007 58 TRP A CE2 416 C CE3 . TRP A 58 ? 0.5382 0.9672 0.6849 -0.1678 -0.0552 -0.1174 58 TRP A CE3 417 C CZ2 . TRP A 58 ? 0.4997 0.8974 0.6411 -0.1509 -0.0328 -0.0983 58 TRP A CZ2 418 C CZ3 . TRP A 58 ? 0.5491 0.9413 0.6839 -0.1779 -0.0449 -0.1149 58 TRP A CZ3 419 C CH2 . TRP A 58 ? 0.5321 0.9095 0.6642 -0.1691 -0.0341 -0.1050 58 TRP A CH2 420 N N . ASN A 59 ? 0.5288 1.1327 0.7737 -0.1400 -0.0667 -0.1162 59 ASN A N 421 C CA . ASN A 59 ? 0.5335 1.1647 0.7988 -0.1251 -0.0613 -0.1116 59 ASN A CA 422 C C . ASN A 59 ? 0.4998 1.0925 0.7440 -0.1081 -0.0538 -0.1017 59 ASN A C 423 O O . ASN A 59 ? 0.4939 1.0536 0.7241 -0.1163 -0.0423 -0.0985 59 ASN A O 424 C CB . ASN A 59 ? 0.5725 1.2301 0.8619 -0.1424 -0.0494 -0.1153 59 ASN A CB 425 C CG . ASN A 59 ? 0.6083 1.3043 0.9236 -0.1266 -0.0449 -0.1135 59 ASN A CG 426 O OD1 . ASN A 59 ? 0.5883 1.2711 0.8956 -0.1044 -0.0433 -0.1065 59 ASN A OD1 427 N ND2 . ASN A 59 ? 0.6522 1.3965 0.9992 -0.1385 -0.0425 -0.1205 59 ASN A ND2 428 N N . ALA A 60 ? 0.4744 1.0697 0.7151 -0.0849 -0.0613 -0.0966 60 ALA A N 429 C CA . ALA A 60 ? 0.4668 1.0295 0.6898 -0.0681 -0.0554 -0.0876 60 ALA A CA 430 C C . ALA A 60 ? 0.4650 1.0525 0.7066 -0.0500 -0.0528 -0.0845 60 ALA A C 431 O O . ALA A 60 ? 0.4756 1.0544 0.7095 -0.0294 -0.0577 -0.0785 60 ALA A O 432 C CB . ALA A 60 ? 0.4684 1.0066 0.6675 -0.0567 -0.0655 -0.0837 60 ALA A CB 433 N N . SER A 61 ? 0.4644 1.0825 0.7303 -0.0580 -0.0446 -0.0888 61 SER A N 434 C CA . SER A 61 ? 0.4602 1.1062 0.7468 -0.0411 -0.0411 -0.0881 61 SER A CA 435 C C . SER A 61 ? 0.4440 1.0698 0.7243 -0.0394 -0.0247 -0.0843 61 SER A C 436 O O . SER A 61 ? 0.4286 1.0687 0.7204 -0.0227 -0.0209 -0.0835 61 SER A O 437 C CB . SER A 61 ? 0.4644 1.1666 0.7859 -0.0482 -0.0434 -0.0967 61 SER A CB 438 O OG . SER A 61 ? 0.4776 1.1862 0.8065 -0.0731 -0.0315 -0.1012 61 SER A OG 439 N N . THR A 62 ? 0.4531 1.0454 0.7146 -0.0558 -0.0155 -0.0823 62 THR A N 440 C CA . THR A 62 ? 0.4737 1.0434 0.7250 -0.0548 -0.0010 -0.0781 62 THR A CA 441 C C . THR A 62 ? 0.4788 0.9961 0.6981 -0.0540 -0.0002 -0.0715 62 THR A C 442 O O . THR A 62 ? 0.4938 0.9913 0.6992 -0.0615 -0.0071 -0.0713 62 THR A O 443 C CB . THR A 62 ? 0.4881 1.0702 0.7486 -0.0771 0.0120 -0.0815 62 THR A CB 444 O OG1 . THR A 62 ? 0.4960 1.0661 0.7490 -0.0989 0.0089 -0.0837 62 THR A OG1 445 C CG2 . THR A 62 ? 0.4908 1.1283 0.7855 -0.0765 0.0152 -0.0883 62 THR A CG2 446 N N . TYR A 63 ? 0.4857 0.9820 0.6941 -0.0446 0.0082 -0.0667 63 TYR A N 447 C CA . TYR A 63 ? 0.4829 0.9324 0.6633 -0.0438 0.0099 -0.0606 63 TYR A CA 448 C C . TYR A 63 ? 0.4803 0.9090 0.6490 -0.0654 0.0146 -0.0608 63 TYR A C 449 O O . TYR A 63 ? 0.4855 0.9297 0.6641 -0.0809 0.0221 -0.0637 63 TYR A O 450 C CB . TYR A 63 ? 0.4771 0.9116 0.6496 -0.0327 0.0189 -0.0567 63 TYR A CB 451 C CG . TYR A 63 ? 0.4882 0.9176 0.6583 -0.0100 0.0134 -0.0539 63 TYR A CG 452 C CD1 . TYR A 63 ? 0.4964 0.9053 0.6530 -0.0022 0.0032 -0.0500 63 TYR A CD1 453 C CD2 . TYR A 63 ? 0.5006 0.9429 0.6799 0.0032 0.0192 -0.0550 63 TYR A CD2 454 C CE1 . TYR A 63 ? 0.5054 0.9059 0.6576 0.0170 -0.0014 -0.0464 63 TYR A CE1 455 C CE2 . TYR A 63 ? 0.5084 0.9411 0.6836 0.0236 0.0141 -0.0522 63 TYR A CE2 456 C CZ . TYR A 63 ? 0.5114 0.9223 0.6727 0.0299 0.0036 -0.0474 63 TYR A CZ 457 O OH . TYR A 63 ? 0.5285 0.9272 0.6843 0.0486 -0.0012 -0.0438 63 TYR A OH 458 N N . PRO A 64 ? 0.4809 0.8734 0.6280 -0.0664 0.0108 -0.0576 64 PRO A N 459 C CA . PRO A 64 ? 0.4932 0.8610 0.6274 -0.0844 0.0141 -0.0577 64 PRO A CA 460 C C . PRO A 64 ? 0.4991 0.8440 0.6207 -0.0877 0.0250 -0.0526 64 PRO A C 461 O O . PRO A 64 ? 0.5026 0.8483 0.6235 -0.0751 0.0293 -0.0496 64 PRO A O 462 C CB . PRO A 64 ? 0.4977 0.8375 0.6146 -0.0791 0.0057 -0.0566 64 PRO A CB 463 C CG . PRO A 64 ? 0.4830 0.8184 0.5956 -0.0588 0.0037 -0.0521 64 PRO A CG 464 C CD . PRO A 64 ? 0.4721 0.8438 0.6053 -0.0503 0.0038 -0.0537 64 PRO A CD 465 N N . ASN A 65 ? 0.5122 0.8348 0.6224 -0.1043 0.0287 -0.0517 65 ASN A N 466 C CA . ASN A 65 ? 0.5323 0.8263 0.6251 -0.1071 0.0369 -0.0456 65 ASN A CA 467 C C . ASN A 65 ? 0.5123 0.7777 0.5885 -0.0910 0.0332 -0.0411 65 ASN A C 468 O O . ASN A 65 ? 0.5127 0.7721 0.5866 -0.0826 0.0248 -0.0425 65 ASN A O 469 C CB . ASN A 65 ? 0.5677 0.8372 0.6486 -0.1268 0.0390 -0.0447 65 ASN A CB 470 C CG . ASN A 65 ? 0.5793 0.8732 0.6741 -0.1466 0.0455 -0.0478 65 ASN A CG 471 O OD1 . ASN A 65 ? 0.6090 0.8897 0.6993 -0.1638 0.0445 -0.0493 65 ASN A OD1 472 N ND2 . ASN A 65 ? 0.5617 0.8906 0.6733 -0.1446 0.0525 -0.0490 65 ASN A ND2 473 N N . ASN A 66 ? 0.5045 0.7537 0.5688 -0.0875 0.0398 -0.0360 66 ASN A N 474 C CA . ASN A 66 ? 0.4862 0.7074 0.5345 -0.0751 0.0366 -0.0318 66 ASN A CA 475 C C . ASN A 66 ? 0.5024 0.6890 0.5328 -0.0839 0.0355 -0.0288 66 ASN A C 476 O O . ASN A 66 ? 0.5369 0.7179 0.5639 -0.0993 0.0398 -0.0280 66 ASN A O 477 C CB . ASN A 66 ? 0.4749 0.6964 0.5189 -0.0664 0.0431 -0.0287 66 ASN A CB 478 C CG . ASN A 66 ? 0.4671 0.7215 0.5289 -0.0567 0.0450 -0.0323 66 ASN A CG 479 O OD1 . ASN A 66 ? 0.4883 0.7557 0.5534 -0.0568 0.0534 -0.0328 66 ASN A OD1 480 N ND2 . ASN A 66 ? 0.4590 0.7268 0.5315 -0.0477 0.0371 -0.0350 66 ASN A ND2 481 N N . CYS A 67 ? 0.4879 0.6515 0.5073 -0.0744 0.0298 -0.0271 67 CYS A N 482 C CA . CYS A 67 ? 0.5084 0.6387 0.5116 -0.0796 0.0278 -0.0245 67 CYS A CA 483 C C . CYS A 67 ? 0.5204 0.6333 0.5094 -0.0825 0.0336 -0.0181 67 CYS A C 484 O O . CYS A 67 ? 0.5054 0.6279 0.4947 -0.0760 0.0378 -0.0161 67 CYS A O 485 C CB . CYS A 67 ? 0.5001 0.6152 0.4978 -0.0675 0.0206 -0.0253 67 CYS A CB 486 S SG . CYS A 67 ? 0.4976 0.6273 0.5055 -0.0652 0.0136 -0.0326 67 CYS A SG 487 N N . GLN A 68 ? 0.5440 0.6299 0.5194 -0.0920 0.0333 -0.0150 68 GLN A N 488 C CA . GLN A 68 ? 0.5560 0.6210 0.5140 -0.0958 0.0374 -0.0077 68 GLN A CA 489 C C . GLN A 68 ? 0.5538 0.6065 0.5025 -0.0809 0.0340 -0.0046 68 GLN A C 490 O O . GLN A 68 ? 0.5578 0.5995 0.5061 -0.0713 0.0268 -0.0062 68 GLN A O 491 C CB . GLN A 68 ? 0.5815 0.6146 0.5251 -0.1067 0.0351 -0.0045 68 GLN A CB 492 C CG . GLN A 68 ? 0.6012 0.6407 0.5498 -0.1255 0.0395 -0.0063 68 GLN A CG 493 C CD . GLN A 68 ? 0.6083 0.6550 0.5517 -0.1383 0.0497 -0.0010 68 GLN A CD 494 O OE1 . GLN A 68 ? 0.6161 0.6710 0.5554 -0.1318 0.0544 0.0022 68 GLN A OE1 495 N NE2 . GLN A 68 ? 0.6238 0.6674 0.5665 -0.1574 0.0537 -0.0006 68 GLN A NE2 496 N N . GLN A 69 ? 0.5495 0.6036 0.4899 -0.0801 0.0394 -0.0004 69 GLN A N 497 C CA . GLN A 69 ? 0.5491 0.5982 0.4835 -0.0666 0.0367 0.0011 69 GLN A CA 498 C C . GLN A 69 ? 0.5696 0.6152 0.4896 -0.0687 0.0429 0.0057 69 GLN A C 499 O O . GLN A 69 ? 0.5476 0.6009 0.4647 -0.0800 0.0513 0.0073 69 GLN A O 500 C CB . GLN A 69 ? 0.5237 0.5961 0.4745 -0.0551 0.0353 -0.0044 69 GLN A CB 501 C CG . GLN A 69 ? 0.5187 0.6208 0.4827 -0.0575 0.0426 -0.0077 69 GLN A CG 502 C CD . GLN A 69 ? 0.5135 0.6349 0.4915 -0.0449 0.0404 -0.0121 69 GLN A CD 503 O OE1 . GLN A 69 ? 0.5107 0.6308 0.4851 -0.0352 0.0407 -0.0119 69 GLN A OE1 504 N NE2 . GLN A 69 ? 0.5133 0.6521 0.5065 -0.0456 0.0380 -0.0160 69 GLN A NE2 505 N N . TYR A 70 ? 0.6018 0.6362 0.5124 -0.0582 0.0387 0.0074 70 TYR A N 506 C CA . TYR A 70 ? 0.6011 0.6324 0.4967 -0.0579 0.0432 0.0105 70 TYR A CA 507 C C . TYR A 70 ? 0.5781 0.6379 0.4856 -0.0560 0.0516 0.0052 70 TYR A C 508 O O . TYR A 70 ? 0.5635 0.6409 0.4890 -0.0486 0.0500 -0.0002 70 TYR A O 509 C CB . TYR A 70 ? 0.6013 0.6173 0.4873 -0.0467 0.0353 0.0117 70 TYR A CB 510 C CG . TYR A 70 ? 0.6533 0.6655 0.5221 -0.0459 0.0389 0.0139 70 TYR A CG 511 C CD1 . TYR A 70 ? 0.6872 0.6798 0.5331 -0.0534 0.0396 0.0211 70 TYR A CD1 512 C CD2 . TYR A 70 ? 0.6572 0.6837 0.5307 -0.0376 0.0413 0.0087 70 TYR A CD2 513 C CE1 . TYR A 70 ? 0.7262 0.7157 0.5540 -0.0529 0.0427 0.0228 70 TYR A CE1 514 C CE2 . TYR A 70 ? 0.6932 0.7159 0.5497 -0.0369 0.0446 0.0093 70 TYR A CE2 515 C CZ . TYR A 70 ? 0.7402 0.7454 0.5736 -0.0447 0.0453 0.0161 70 TYR A CZ 516 O OH . TYR A 70 ? 0.8008 0.8024 0.6148 -0.0442 0.0486 0.0164 70 TYR A OH 517 N N . VAL A 71 ? 0.5850 0.6493 0.4819 -0.0626 0.0606 0.0069 71 VAL A N 518 C CA . VAL A 71 ? 0.5511 0.6425 0.4579 -0.0600 0.0696 0.0013 71 VAL A CA 519 C C . VAL A 71 ? 0.5679 0.6509 0.4568 -0.0540 0.0716 0.0015 71 VAL A C 520 O O . VAL A 71 ? 0.5766 0.6437 0.4433 -0.0612 0.0741 0.0070 71 VAL A O 521 C CB . VAL A 71 ? 0.5539 0.6628 0.4653 -0.0745 0.0806 0.0015 71 VAL A CB 522 C CG1 . VAL A 71 ? 0.5461 0.6856 0.4689 -0.0703 0.0906 -0.0053 71 VAL A CG1 523 C CG2 . VAL A 71 ? 0.5397 0.6555 0.4678 -0.0816 0.0773 0.0005 71 VAL A CG2 524 N N . ASP A 72 ? 0.5638 0.6558 0.4612 -0.0409 0.0698 -0.0045 72 ASP A N 525 C CA . ASP A 72 ? 0.5843 0.6700 0.4669 -0.0341 0.0712 -0.0066 72 ASP A CA 526 C C . ASP A 72 ? 0.6061 0.7086 0.4839 -0.0394 0.0846 -0.0095 72 ASP A C 527 O O . ASP A 72 ? 0.5998 0.7282 0.4966 -0.0385 0.0916 -0.0148 72 ASP A O 528 C CB . ASP A 72 ? 0.5738 0.6647 0.4695 -0.0199 0.0661 -0.0128 72 ASP A CB 529 C CG . ASP A 72 ? 0.5916 0.6779 0.4746 -0.0125 0.0681 -0.0174 72 ASP A CG 530 O OD1 . ASP A 72 ? 0.6452 0.7215 0.5066 -0.0175 0.0714 -0.0154 72 ASP A OD1 531 O OD2 . ASP A 72 ? 0.5776 0.6691 0.4714 -0.0018 0.0660 -0.0230 72 ASP A OD2 532 N N . GLU A 73 ? 0.6568 0.7460 0.5093 -0.0450 0.0883 -0.0060 73 GLU A N 533 C CA . GLU A 73 ? 0.6900 0.7951 0.5345 -0.0499 0.1024 -0.0094 73 GLU A CA 534 C C . GLU A 73 ? 0.6976 0.7900 0.5188 -0.0438 0.1024 -0.0120 73 GLU A C 535 O O . GLU A 73 ? 0.6926 0.7866 0.4943 -0.0504 0.1120 -0.0116 73 GLU A O 536 C CB . GLU A 73 ? 0.7399 0.8427 0.5724 -0.0677 0.1097 -0.0016 73 GLU A CB 537 C CG . GLU A 73 ? 0.7628 0.8758 0.6162 -0.0761 0.1093 0.0006 73 GLU A CG 538 C CD . GLU A 73 ? 0.8202 0.9265 0.6597 -0.0954 0.1163 0.0087 73 GLU A CD 539 O OE1 . GLU A 73 ? 0.8336 0.9157 0.6436 -0.1016 0.1161 0.0163 73 GLU A OE1 540 O OE2 . GLU A 73 ? 0.8259 0.9509 0.6840 -0.1050 0.1214 0.0077 73 GLU A OE2 541 N N . GLN A 74 ? 0.6858 0.7659 0.5086 -0.0320 0.0916 -0.0148 74 GLN A N 542 C CA . GLN A 74 ? 0.7090 0.7769 0.5122 -0.0256 0.0896 -0.0188 74 GLN A CA 543 C C . GLN A 74 ? 0.7021 0.7897 0.5076 -0.0201 0.1020 -0.0293 74 GLN A C 544 O O . GLN A 74 ? 0.7358 0.8185 0.5188 -0.0210 0.1071 -0.0323 74 GLN A O 545 C CB . GLN A 74 ? 0.7266 0.7813 0.5372 -0.0152 0.0760 -0.0205 74 GLN A CB 546 C CG . GLN A 74 ? 0.7837 0.8226 0.5741 -0.0100 0.0708 -0.0243 74 GLN A CG 547 C CD . GLN A 74 ? 0.8347 0.8549 0.5964 -0.0179 0.0667 -0.0168 74 GLN A CD 548 O OE1 . GLN A 74 ? 0.8726 0.8838 0.6320 -0.0246 0.0619 -0.0074 74 GLN A OE1 549 N NE2 . GLN A 74 ? 0.8445 0.8574 0.5830 -0.0167 0.0678 -0.0211 74 GLN A NE2 550 N N . PHE A 75 ? 0.6865 0.7971 0.5192 -0.0139 0.1066 -0.0353 75 PHE A N 551 C CA . PHE A 75 ? 0.6596 0.7907 0.4992 -0.0057 0.1176 -0.0464 75 PHE A CA 552 C C . PHE A 75 ? 0.6531 0.8167 0.5157 -0.0096 0.1286 -0.0484 75 PHE A C 553 O O . PHE A 75 ? 0.6404 0.8216 0.5288 0.0001 0.1279 -0.0537 75 PHE A O 554 C CB . PHE A 75 ? 0.6280 0.7536 0.4793 0.0103 0.1099 -0.0537 75 PHE A CB 555 C CG . PHE A 75 ? 0.6120 0.7083 0.4439 0.0128 0.0988 -0.0525 75 PHE A CG 556 C CD1 . PHE A 75 ? 0.6235 0.7086 0.4292 0.0124 0.1018 -0.0569 75 PHE A CD1 557 C CD2 . PHE A 75 ? 0.5845 0.6663 0.4243 0.0150 0.0855 -0.0476 75 PHE A CD2 558 C CE1 . PHE A 75 ? 0.6293 0.6896 0.4182 0.0139 0.0906 -0.0563 75 PHE A CE1 559 C CE2 . PHE A 75 ? 0.5879 0.6464 0.4124 0.0164 0.0753 -0.0469 75 PHE A CE2 560 C CZ . PHE A 75 ? 0.6031 0.6510 0.4026 0.0158 0.0773 -0.0513 75 PHE A CZ 561 N N . PRO A 76 ? 0.6674 0.8395 0.5205 -0.0245 0.1385 -0.0437 76 PRO A N 562 C CA . PRO A 76 ? 0.6549 0.8592 0.5310 -0.0311 0.1485 -0.0451 76 PRO A CA 563 C C . PRO A 76 ? 0.6570 0.8922 0.5561 -0.0176 0.1564 -0.0577 76 PRO A C 564 O O . PRO A 76 ? 0.6456 0.8841 0.5339 -0.0104 0.1642 -0.0660 76 PRO A O 565 C CB . PRO A 76 ? 0.6724 0.8780 0.5267 -0.0485 0.1605 -0.0400 76 PRO A CB 566 C CG . PRO A 76 ? 0.6907 0.8586 0.5146 -0.0535 0.1506 -0.0305 76 PRO A CG 567 C CD . PRO A 76 ? 0.6954 0.8478 0.5153 -0.0368 0.1408 -0.0365 76 PRO A CD 568 N N . GLY A 77 ? 0.6525 0.9092 0.5825 -0.0134 0.1535 -0.0594 77 GLY A N 569 C CA . GLY A 77 ? 0.6510 0.9381 0.6066 0.0013 0.1587 -0.0707 77 GLY A CA 570 C C . GLY A 77 ? 0.6376 0.9103 0.5956 0.0220 0.1498 -0.0770 77 GLY A C 571 O O . GLY A 77 ? 0.6694 0.9629 0.6464 0.0366 0.1532 -0.0864 77 GLY A O 572 N N . PHE A 78 ? 0.5992 0.8362 0.5383 0.0235 0.1384 -0.0719 78 PHE A N 573 C CA . PHE A 78 ? 0.5741 0.7940 0.5137 0.0404 0.1297 -0.0769 78 PHE A CA 574 C C . PHE A 78 ? 0.5367 0.7581 0.4982 0.0462 0.1181 -0.0728 78 PHE A C 575 O O . PHE A 78 ? 0.5192 0.7272 0.4782 0.0377 0.1095 -0.0639 78 PHE A O 576 C CB . PHE A 78 ? 0.5788 0.7627 0.4891 0.0380 0.1230 -0.0739 78 PHE A CB 577 C CG . PHE A 78 ? 0.5747 0.7384 0.4837 0.0526 0.1141 -0.0788 78 PHE A CG 578 C CD1 . PHE A 78 ? 0.5795 0.7481 0.4906 0.0666 0.1197 -0.0905 78 PHE A CD1 579 C CD2 . PHE A 78 ? 0.5691 0.7085 0.4748 0.0519 0.1004 -0.0720 78 PHE A CD2 580 C CE1 . PHE A 78 ? 0.5870 0.7333 0.4955 0.0790 0.1113 -0.0947 78 PHE A CE1 581 C CE2 . PHE A 78 ? 0.5722 0.6923 0.4762 0.0632 0.0927 -0.0761 78 PHE A CE2 582 C CZ . PHE A 78 ? 0.5850 0.7068 0.4896 0.0763 0.0979 -0.0871 78 PHE A CZ 583 N N . SER A 79 ? 0.5362 0.7736 0.5184 0.0615 0.1177 -0.0797 79 SER A N 584 C CA . SER A 79 ? 0.5258 0.7677 0.5284 0.0677 0.1070 -0.0760 79 SER A CA 585 C C . SER A 79 ? 0.5150 0.7237 0.5059 0.0671 0.0938 -0.0686 79 SER A C 586 O O . SER A 79 ? 0.5155 0.7250 0.5155 0.0628 0.0861 -0.0619 79 SER A O 587 C CB . SER A 79 ? 0.5344 0.7913 0.5556 0.0874 0.1071 -0.0844 79 SER A CB 588 O OG . SER A 79 ? 0.5599 0.7880 0.5675 0.0995 0.1023 -0.0879 79 SER A OG 589 N N . GLY A 80 ? 0.5182 0.6994 0.4894 0.0708 0.0913 -0.0704 80 GLY A N 590 C CA . GLY A 80 ? 0.5179 0.6699 0.4793 0.0696 0.0794 -0.0641 80 GLY A CA 591 C C . GLY A 80 ? 0.5057 0.6508 0.4604 0.0545 0.0753 -0.0549 80 GLY A C 592 O O . GLY A 80 ? 0.4697 0.6018 0.4257 0.0531 0.0658 -0.0492 80 GLY A O 593 N N . SER A 81 ? 0.5359 0.6890 0.4824 0.0434 0.0831 -0.0539 81 SER A N 594 C CA . SER A 81 ? 0.5431 0.6879 0.4807 0.0291 0.0804 -0.0455 81 SER A CA 595 C C . SER A 81 ? 0.5261 0.6921 0.4823 0.0224 0.0816 -0.0423 81 SER A C 596 O O . SER A 81 ? 0.5068 0.6655 0.4662 0.0174 0.0740 -0.0364 81 SER A O 597 C CB . SER A 81 ? 0.5816 0.7211 0.4973 0.0204 0.0883 -0.0456 81 SER A CB 598 O OG . SER A 81 ? 0.6133 0.7509 0.5223 0.0060 0.0892 -0.0379 81 SER A OG 599 N N . GLU A 82 ? 0.5341 0.7277 0.5030 0.0226 0.0913 -0.0472 82 GLU A N 600 C CA . GLU A 82 ? 0.5295 0.7473 0.5164 0.0142 0.0937 -0.0454 82 GLU A CA 601 C C . GLU A 82 ? 0.5021 0.7283 0.5092 0.0219 0.0845 -0.0451 82 GLU A C 602 O O . GLU A 82 ? 0.4887 0.7246 0.5060 0.0134 0.0817 -0.0418 82 GLU A O 603 C CB . GLU A 82 ? 0.5579 0.8073 0.5557 0.0131 0.1069 -0.0520 82 GLU A CB 604 C CG . GLU A 82 ? 0.5992 0.8446 0.5762 0.0041 0.1183 -0.0525 82 GLU A CG 605 C CD . GLU A 82 ? 0.6202 0.8633 0.5881 -0.0160 0.1221 -0.0449 82 GLU A CD 606 O OE1 . GLU A 82 ? 0.6031 0.8413 0.5780 -0.0228 0.1144 -0.0392 82 GLU A OE1 607 O OE2 . GLU A 82 ? 0.6376 0.8823 0.5897 -0.0251 0.1330 -0.0448 82 GLU A OE2 608 N N . MET A 83 ? 0.4943 0.7149 0.5053 0.0373 0.0793 -0.0482 83 MET A N 609 C CA . MET A 83 ? 0.4809 0.7084 0.5081 0.0449 0.0703 -0.0470 83 MET A CA 610 C C . MET A 83 ? 0.4680 0.6798 0.4905 0.0364 0.0614 -0.0397 83 MET A C 611 O O . MET A 83 ? 0.4612 0.6829 0.4965 0.0383 0.0551 -0.0382 83 MET A O 612 C CB . MET A 83 ? 0.5068 0.7236 0.5343 0.0620 0.0656 -0.0500 83 MET A CB 613 C CG . MET A 83 ? 0.5476 0.7300 0.5552 0.0628 0.0602 -0.0470 83 MET A CG 614 S SD . MET A 83 ? 0.5909 0.7585 0.6009 0.0800 0.0520 -0.0480 83 MET A SD 615 C CE . MET A 83 ? 0.6469 0.8180 0.6550 0.0922 0.0608 -0.0584 83 MET A CE 616 N N . TRP A 84 ? 0.4650 0.6534 0.4690 0.0279 0.0607 -0.0356 84 TRP A N 617 C CA . TRP A 84 ? 0.4537 0.6269 0.4532 0.0210 0.0528 -0.0297 84 TRP A CA 618 C C . TRP A 84 ? 0.4410 0.6184 0.4398 0.0061 0.0554 -0.0269 84 TRP A C 619 O O . TRP A 84 ? 0.3984 0.5675 0.3971 0.0012 0.0492 -0.0236 84 TRP A O 620 C CB . TRP A 84 ? 0.4631 0.6077 0.4447 0.0222 0.0484 -0.0271 84 TRP A CB 621 C CG . TRP A 84 ? 0.4840 0.6203 0.4641 0.0344 0.0458 -0.0298 84 TRP A CG 622 C CD1 . TRP A 84 ? 0.5123 0.6401 0.4819 0.0393 0.0496 -0.0337 84 TRP A CD1 623 C CD2 . TRP A 84 ? 0.4872 0.6208 0.4747 0.0427 0.0389 -0.0288 84 TRP A CD2 624 N NE1 . TRP A 84 ? 0.5068 0.6252 0.4776 0.0501 0.0452 -0.0356 84 TRP A NE1 625 C CE2 . TRP A 84 ? 0.4971 0.6186 0.4785 0.0521 0.0387 -0.0319 84 TRP A CE2 626 C CE3 . TRP A 84 ? 0.4888 0.6280 0.4858 0.0427 0.0329 -0.0257 84 TRP A CE3 627 C CZ2 . TRP A 84 ? 0.5058 0.6189 0.4902 0.0609 0.0327 -0.0309 84 TRP A CZ2 628 C CZ3 . TRP A 84 ? 0.4820 0.6147 0.4813 0.0517 0.0272 -0.0244 84 TRP A CZ3 629 C CH2 . TRP A 84 ? 0.4993 0.6182 0.4922 0.0605 0.0271 -0.0266 84 TRP A CH2 630 N N . ASN A 85 ? 0.4479 0.6364 0.4449 -0.0013 0.0648 -0.0283 85 ASN A N 631 C CA . ASN A 85 ? 0.4614 0.6515 0.4562 -0.0171 0.0680 -0.0252 85 ASN A CA 632 C C . ASN A 85 ? 0.4684 0.6833 0.4841 -0.0213 0.0669 -0.0273 85 ASN A C 633 O O . ASN A 85 ? 0.4622 0.6988 0.4950 -0.0118 0.0659 -0.0317 85 ASN A O 634 C CB . ASN A 85 ? 0.4873 0.6830 0.4727 -0.0255 0.0795 -0.0255 85 ASN A CB 635 C CG . ASN A 85 ? 0.4922 0.6610 0.4522 -0.0256 0.0799 -0.0222 85 ASN A CG 636 O OD1 . ASN A 85 ? 0.4857 0.6297 0.4335 -0.0265 0.0720 -0.0173 85 ASN A OD1 637 N ND2 . ASN A 85 ? 0.5097 0.6854 0.4618 -0.0246 0.0891 -0.0253 85 ASN A ND2 638 N N . PRO A 86 ? 0.4929 0.7039 0.5070 -0.0357 0.0666 -0.0245 86 PRO A N 639 C CA . PRO A 86 ? 0.4871 0.7225 0.5200 -0.0430 0.0663 -0.0273 86 PRO A CA 640 C C . PRO A 86 ? 0.5052 0.7758 0.5551 -0.0439 0.0754 -0.0325 86 PRO A C 641 O O . PRO A 86 ? 0.5239 0.7978 0.5669 -0.0506 0.0857 -0.0323 86 PRO A O 642 C CB . PRO A 86 ? 0.4923 0.7111 0.5147 -0.0604 0.0669 -0.0232 86 PRO A CB 643 C CG . PRO A 86 ? 0.5005 0.6840 0.5020 -0.0568 0.0618 -0.0182 86 PRO A CG 644 C CD . PRO A 86 ? 0.5032 0.6835 0.4978 -0.0441 0.0638 -0.0186 86 PRO A CD 645 N N . ASN A 87 ? 0.4927 0.7901 0.5643 -0.0366 0.0713 -0.0371 87 ASN A N 646 C CA . ASN A 87 ? 0.4800 0.8169 0.5735 -0.0362 0.0781 -0.0432 87 ASN A CA 647 C C . ASN A 87 ? 0.5075 0.8664 0.6159 -0.0525 0.0783 -0.0449 87 ASN A C 648 O O . ASN A 87 ? 0.5135 0.9086 0.6421 -0.0556 0.0844 -0.0501 87 ASN A O 649 C CB . ASN A 87 ? 0.4654 0.8193 0.5744 -0.0162 0.0720 -0.0473 87 ASN A CB 650 C CG . ASN A 87 ? 0.4555 0.8011 0.5667 -0.0109 0.0585 -0.0452 87 ASN A CG 651 O OD1 . ASN A 87 ? 0.4553 0.7824 0.5566 -0.0213 0.0539 -0.0417 87 ASN A OD1 652 N ND2 . ASN A 87 ? 0.4423 0.8002 0.5649 0.0057 0.0522 -0.0473 87 ASN A ND2 653 N N . ARG A 88 ? 0.5433 0.8815 0.6430 -0.0626 0.0714 -0.0415 88 ARG A N 654 C CA . ARG A 88 ? 0.5627 0.9149 0.6725 -0.0808 0.0715 -0.0432 88 ARG A CA 655 C C . ARG A 88 ? 0.5762 0.8980 0.6649 -0.0982 0.0762 -0.0377 88 ARG A C 656 O O . ARG A 88 ? 0.5988 0.8902 0.6660 -0.0942 0.0776 -0.0325 88 ARG A O 657 C CB . ARG A 88 ? 0.5786 0.9319 0.6957 -0.0778 0.0585 -0.0451 88 ARG A CB 658 C CG . ARG A 88 ? 0.5901 0.9783 0.7301 -0.0639 0.0528 -0.0503 88 ARG A CG 659 C CD . ARG A 88 ? 0.6201 1.0515 0.7852 -0.0743 0.0576 -0.0563 88 ARG A CD 660 N NE . ARG A 88 ? 0.6282 1.0958 0.8166 -0.0582 0.0531 -0.0612 88 ARG A NE 661 C CZ . ARG A 88 ? 0.6393 1.1185 0.8338 -0.0417 0.0579 -0.0627 88 ARG A CZ 662 N NH1 . ARG A 88 ? 0.6458 1.1046 0.8243 -0.0395 0.0675 -0.0600 88 ARG A NH1 663 N NH2 . ARG A 88 ? 0.6488 1.1596 0.8649 -0.0264 0.0522 -0.0671 88 ARG A NH2 664 N N . GLU A 89 ? 0.5900 0.9190 0.6843 -0.1175 0.0781 -0.0387 89 GLU A N 665 C CA . GLU A 89 ? 0.6300 0.9269 0.7034 -0.1347 0.0815 -0.0329 89 GLU A CA 666 C C . GLU A 89 ? 0.6004 0.8590 0.6572 -0.1301 0.0705 -0.0298 89 GLU A C 667 O O . GLU A 89 ? 0.5895 0.8525 0.6548 -0.1217 0.0608 -0.0336 89 GLU A O 668 C CB . GLU A 89 ? 0.7000 1.0134 0.7841 -0.1579 0.0861 -0.0352 89 GLU A CB 669 C CG . GLU A 89 ? 0.7905 1.0839 0.8557 -0.1761 0.0969 -0.0285 89 GLU A CG 670 C CD . GLU A 89 ? 0.8481 1.1464 0.9188 -0.2018 0.0999 -0.0294 89 GLU A CD 671 O OE1 . GLU A 89 ? 0.8312 1.1262 0.9090 -0.2062 0.0903 -0.0335 89 GLU A OE1 672 O OE2 . GLU A 89 ? 0.8895 1.1942 0.9561 -0.2182 0.1124 -0.0263 89 GLU A OE2 673 N N . MET A 90 ? 0.5824 0.8041 0.6152 -0.1350 0.0720 -0.0230 90 MET A N 674 C CA . MET A 90 ? 0.5635 0.7499 0.5814 -0.1291 0.0623 -0.0206 90 MET A CA 675 C C . MET A 90 ? 0.5502 0.7196 0.5642 -0.1452 0.0589 -0.0212 90 MET A C 676 O O . MET A 90 ? 0.5554 0.7238 0.5668 -0.1637 0.0655 -0.0194 90 MET A O 677 C CB . MET A 90 ? 0.5858 0.7400 0.5800 -0.1241 0.0636 -0.0132 90 MET A CB 678 C CG . MET A 90 ? 0.5772 0.7427 0.5713 -0.1096 0.0672 -0.0128 90 MET A CG 679 S SD . MET A 90 ? 0.6162 0.7429 0.5802 -0.1081 0.0679 -0.0042 90 MET A SD 680 C CE . MET A 90 ? 0.5759 0.6927 0.5408 -0.0875 0.0570 -0.0060 90 MET A CE 681 N N . SER A 91 ? 0.5251 0.6797 0.5375 -0.1383 0.0489 -0.0241 91 SER A N 682 C CA . SER A 91 ? 0.5315 0.6678 0.5399 -0.1511 0.0442 -0.0266 91 SER A CA 683 C C . SER A 91 ? 0.5183 0.6282 0.5169 -0.1386 0.0348 -0.0278 91 SER A C 684 O O . SER A 91 ? 0.4727 0.5911 0.4753 -0.1219 0.0309 -0.0290 91 SER A O 685 C CB . SER A 91 ? 0.5146 0.6842 0.5443 -0.1602 0.0428 -0.0347 91 SER A CB 686 O OG . SER A 91 ? 0.5303 0.6817 0.5553 -0.1752 0.0391 -0.0380 91 SER A OG 687 N N . GLU A 92 ? 0.5528 0.6300 0.5381 -0.1468 0.0315 -0.0275 92 GLU A N 688 C CA . GLU A 92 ? 0.5639 0.6205 0.5433 -0.1368 0.0228 -0.0315 92 GLU A CA 689 C C . GLU A 92 ? 0.5746 0.6560 0.5691 -0.1363 0.0178 -0.0410 92 GLU A C 690 O O . GLU A 92 ? 0.5827 0.6619 0.5769 -0.1238 0.0118 -0.0449 92 GLU A O 691 C CB . GLU A 92 ? 0.5840 0.5999 0.5465 -0.1456 0.0205 -0.0302 92 GLU A CB 692 C CG . GLU A 92 ? 0.5963 0.5823 0.5404 -0.1418 0.0222 -0.0204 92 GLU A CG 693 C CD . GLU A 92 ? 0.6299 0.5729 0.5576 -0.1425 0.0165 -0.0200 92 GLU A CD 694 O OE1 . GLU A 92 ? 0.6272 0.5597 0.5536 -0.1273 0.0100 -0.0237 92 GLU A OE1 695 O OE2 . GLU A 92 ? 0.6481 0.5679 0.5645 -0.1582 0.0188 -0.0161 92 GLU A OE2 696 N N . ASP A 93 ? 0.5868 0.6929 0.5944 -0.1507 0.0203 -0.0447 93 ASP A N 697 C CA . ASP A 93 ? 0.5650 0.7012 0.5884 -0.1501 0.0151 -0.0531 93 ASP A CA 698 C C . ASP A 93 ? 0.5410 0.7083 0.5765 -0.1344 0.0155 -0.0515 93 ASP A C 699 O O . ASP A 93 ? 0.5467 0.7433 0.5961 -0.1375 0.0204 -0.0506 93 ASP A O 700 C CB . ASP A 93 ? 0.5630 0.7179 0.5981 -0.1710 0.0172 -0.0576 93 ASP A CB 701 C CG . ASP A 93 ? 0.5592 0.7411 0.6081 -0.1721 0.0095 -0.0673 93 ASP A CG 702 O OD1 . ASP A 93 ? 0.5250 0.7223 0.5784 -0.1557 0.0043 -0.0689 93 ASP A OD1 703 O OD2 . ASP A 93 ? 0.5819 0.7686 0.6361 -0.1904 0.0083 -0.0732 93 ASP A OD2 704 N N . CYS A 94 ? 0.5310 0.6915 0.5614 -0.1176 0.0107 -0.0512 94 CYS A N 705 C CA . CYS A 94 ? 0.5207 0.7023 0.5587 -0.1021 0.0111 -0.0483 94 CYS A CA 706 C C . CYS A 94 ? 0.5060 0.6929 0.5441 -0.0883 0.0039 -0.0509 94 CYS A C 707 O O . CYS A 94 ? 0.5046 0.7027 0.5461 -0.0752 0.0038 -0.0476 94 CYS A O 708 C CB . CYS A 94 ? 0.5224 0.6866 0.5503 -0.0947 0.0166 -0.0406 94 CYS A CB 709 S SG . CYS A 94 ? 0.5301 0.6547 0.5387 -0.0860 0.0131 -0.0380 94 CYS A SG 710 N N . LEU A 95 ? 0.5096 0.6880 0.5428 -0.0916 -0.0019 -0.0569 95 LEU A N 711 C CA . LEU A 95 ? 0.4974 0.6800 0.5278 -0.0795 -0.0078 -0.0590 95 LEU A CA 712 C C . LEU A 95 ? 0.4732 0.6892 0.5163 -0.0794 -0.0129 -0.0625 95 LEU A C 713 O O . LEU A 95 ? 0.4724 0.6961 0.5172 -0.0878 -0.0180 -0.0696 95 LEU A O 714 C CB . LEU A 95 ? 0.5147 0.6726 0.5322 -0.0810 -0.0110 -0.0642 95 LEU A CB 715 C CG . LEU A 95 ? 0.5432 0.6696 0.5496 -0.0784 -0.0071 -0.0601 95 LEU A CG 716 C CD1 . LEU A 95 ? 0.5757 0.6781 0.5710 -0.0788 -0.0102 -0.0666 95 LEU A CD1 717 C CD2 . LEU A 95 ? 0.5292 0.6556 0.5342 -0.0641 -0.0051 -0.0531 95 LEU A CD2 718 N N . TYR A 96 ? 0.4472 0.6827 0.4993 -0.0694 -0.0119 -0.0577 96 TYR A N 719 C CA . TYR A 96 ? 0.4266 0.6945 0.4916 -0.0656 -0.0175 -0.0595 96 TYR A CA 720 C C . TYR A 96 ? 0.4126 0.6835 0.4754 -0.0484 -0.0194 -0.0538 96 TYR A C 721 O O . TYR A 96 ? 0.4160 0.6689 0.4715 -0.0411 -0.0147 -0.0485 96 TYR A O 722 C CB . TYR A 96 ? 0.4234 0.7165 0.5062 -0.0726 -0.0135 -0.0601 96 TYR A CB 723 C CG . TYR A 96 ? 0.4357 0.7259 0.5209 -0.0921 -0.0109 -0.0650 96 TYR A CG 724 C CD1 . TYR A 96 ? 0.4459 0.7116 0.5226 -0.1004 -0.0030 -0.0620 96 TYR A CD1 725 C CD2 . TYR A 96 ? 0.4394 0.7501 0.5339 -0.1027 -0.0170 -0.0724 96 TYR A CD2 726 C CE1 . TYR A 96 ? 0.4680 0.7273 0.5449 -0.1193 -0.0007 -0.0657 96 TYR A CE1 727 C CE2 . TYR A 96 ? 0.4580 0.7640 0.5542 -0.1223 -0.0147 -0.0771 96 TYR A CE2 728 C CZ . TYR A 96 ? 0.4651 0.7443 0.5521 -0.1307 -0.0063 -0.0734 96 TYR A CZ 729 O OH . TYR A 96 ? 0.4949 0.7664 0.5819 -0.1511 -0.0042 -0.0774 96 TYR A OH 730 N N . LEU A 97 ? 0.4116 0.7042 0.4798 -0.0422 -0.0270 -0.0548 97 LEU A N 731 C CA . LEU A 97 ? 0.4168 0.7131 0.4836 -0.0262 -0.0295 -0.0486 97 LEU A CA 732 C C . LEU A 97 ? 0.4155 0.7447 0.4995 -0.0206 -0.0343 -0.0489 97 LEU A C 733 O O . LEU A 97 ? 0.4070 0.7590 0.5032 -0.0295 -0.0377 -0.0547 97 LEU A O 734 C CB . LEU A 97 ? 0.4366 0.7205 0.4873 -0.0211 -0.0349 -0.0476 97 LEU A CB 735 C CG . LEU A 97 ? 0.4563 0.7529 0.5043 -0.0270 -0.0433 -0.0538 97 LEU A CG 736 C CD1 . LEU A 97 ? 0.4719 0.7962 0.5283 -0.0191 -0.0522 -0.0521 97 LEU A CD1 737 C CD2 . LEU A 97 ? 0.4635 0.7396 0.4919 -0.0261 -0.0442 -0.0545 97 LEU A CD2 738 N N . ASN A 98 ? 0.4242 0.7554 0.5097 -0.0058 -0.0348 -0.0431 98 ASN A N 739 C CA . ASN A 98 ? 0.4220 0.7828 0.5242 0.0036 -0.0398 -0.0428 98 ASN A CA 740 C C . ASN A 98 ? 0.4212 0.7800 0.5145 0.0178 -0.0488 -0.0374 98 ASN A C 741 O O . ASN A 98 ? 0.4506 0.7834 0.5272 0.0232 -0.0474 -0.0318 98 ASN A O 742 C CB . ASN A 98 ? 0.4263 0.7902 0.5389 0.0102 -0.0316 -0.0410 98 ASN A CB 743 C CG . ASN A 98 ? 0.4278 0.7841 0.5418 -0.0033 -0.0210 -0.0438 98 ASN A CG 744 O OD1 . ASN A 98 ? 0.4290 0.8030 0.5543 -0.0164 -0.0193 -0.0492 98 ASN A OD1 745 N ND2 . ASN A 98 ? 0.4323 0.7616 0.5339 -0.0009 -0.0140 -0.0399 98 ASN A ND2 746 N N . ILE A 99 ? 0.4267 0.8133 0.5312 0.0235 -0.0584 -0.0385 99 ILE A N 747 C CA . ILE A 99 ? 0.4324 0.8172 0.5267 0.0369 -0.0686 -0.0324 99 ILE A CA 748 C C . ILE A 99 ? 0.4323 0.8411 0.5438 0.0521 -0.0743 -0.0306 99 ILE A C 749 O O . ILE A 99 ? 0.4410 0.8824 0.5742 0.0495 -0.0766 -0.0367 99 ILE A O 750 C CB . ILE A 99 ? 0.4253 0.8186 0.5105 0.0301 -0.0785 -0.0352 99 ILE A CB 751 C CG1 . ILE A 99 ? 0.4244 0.7979 0.4964 0.0144 -0.0725 -0.0399 99 ILE A CG1 752 C CG2 . ILE A 99 ? 0.4304 0.8147 0.4986 0.0428 -0.0876 -0.0269 99 ILE A CG2 753 C CD1 . ILE A 99 ? 0.4373 0.8217 0.5032 0.0047 -0.0807 -0.0463 99 ILE A CD1 754 N N . TRP A 100 ? 0.4394 0.8319 0.5419 0.0678 -0.0765 -0.0226 100 TRP A N 755 C CA . TRP A 100 ? 0.4489 0.8596 0.5650 0.0854 -0.0835 -0.0202 100 TRP A CA 756 C C . TRP A 100 ? 0.4718 0.8792 0.5735 0.0953 -0.0973 -0.0130 100 TRP A C 757 O O . TRP A 100 ? 0.5126 0.8892 0.5907 0.0977 -0.0975 -0.0052 100 TRP A O 758 C CB . TRP A 100 ? 0.4533 0.8446 0.5692 0.0968 -0.0757 -0.0167 100 TRP A CB 759 C CG . TRP A 100 ? 0.4479 0.8528 0.5823 0.0918 -0.0646 -0.0239 100 TRP A CG 760 C CD1 . TRP A 100 ? 0.4484 0.8863 0.6083 0.0986 -0.0642 -0.0295 100 TRP A CD1 761 C CD2 . TRP A 100 ? 0.4452 0.8324 0.5738 0.0788 -0.0518 -0.0263 100 TRP A CD2 762 N NE1 . TRP A 100 ? 0.4378 0.8794 0.6069 0.0894 -0.0510 -0.0351 100 TRP A NE1 763 C CE2 . TRP A 100 ? 0.4347 0.8441 0.5838 0.0774 -0.0438 -0.0327 100 TRP A CE2 764 C CE3 . TRP A 100 ? 0.4496 0.8054 0.5578 0.0687 -0.0466 -0.0235 100 TRP A CE3 765 C CZ2 . TRP A 100 ? 0.4257 0.8243 0.5726 0.0658 -0.0312 -0.0355 100 TRP A CZ2 766 C CZ3 . TRP A 100 ? 0.4488 0.7947 0.5569 0.0584 -0.0351 -0.0267 100 TRP A CZ3 767 C CH2 . TRP A 100 ? 0.4361 0.8021 0.5620 0.0569 -0.0277 -0.0321 100 TRP A CH2 768 N N . VAL A 101 ? 0.4699 0.9100 0.5855 0.1006 -0.1091 -0.0154 101 VAL A N 769 C CA . VAL A 101 ? 0.4953 0.9359 0.5962 0.1087 -0.1240 -0.0088 101 VAL A CA 770 C C . VAL A 101 ? 0.5030 0.9590 0.6171 0.1307 -0.1341 -0.0047 101 VAL A C 771 O O . VAL A 101 ? 0.4893 0.9774 0.6321 0.1354 -0.1340 -0.0117 101 VAL A O 772 C CB . VAL A 101 ? 0.4988 0.9659 0.6023 0.0959 -0.1324 -0.0156 101 VAL A CB 773 C CG1 . VAL A 101 ? 0.5323 0.9961 0.6147 0.1031 -0.1474 -0.0082 101 VAL A CG1 774 C CG2 . VAL A 101 ? 0.4813 0.9354 0.5761 0.0747 -0.1220 -0.0220 101 VAL A CG2 775 N N . PRO A 102 ? 0.5225 0.9556 0.6157 0.1442 -0.1428 0.0066 102 PRO A N 776 C CA . PRO A 102 ? 0.5554 1.0005 0.6593 0.1669 -0.1544 0.0111 102 PRO A CA 777 C C . PRO A 102 ? 0.5791 1.0685 0.7009 0.1709 -0.1698 0.0066 102 PRO A C 778 O O . PRO A 102 ? 0.5748 1.0818 0.6951 0.1551 -0.1730 0.0012 102 PRO A O 779 C CB . PRO A 102 ? 0.5756 0.9813 0.6470 0.1762 -0.1606 0.0255 102 PRO A CB 780 C CG . PRO A 102 ? 0.5643 0.9358 0.6148 0.1605 -0.1468 0.0272 102 PRO A CG 781 C CD . PRO A 102 ? 0.5373 0.9287 0.5973 0.1402 -0.1397 0.0160 102 PRO A CD 782 N N . SER A 103 ? 0.6010 1.1081 0.7401 0.1925 -0.1795 0.0083 103 SER A N 783 C CA . SER A 103 ? 0.6239 1.1756 0.7827 0.1998 -0.1958 0.0045 103 SER A CA 784 C C . SER A 103 ? 0.6499 1.1929 0.7988 0.2254 -0.2132 0.0161 103 SER A C 785 O O . SER A 103 ? 0.6682 1.1937 0.8203 0.2436 -0.2111 0.0204 103 SER A O 786 C CB . SER A 103 ? 0.6093 1.2054 0.8102 0.2004 -0.1900 -0.0087 103 SER A CB 787 O OG . SER A 103 ? 0.6301 1.2739 0.8526 0.2045 -0.2057 -0.0137 103 SER A OG 788 N N . PRO A 104 ? 0.6737 1.2263 0.8085 0.2271 -0.2306 0.0213 104 PRO A N 789 C CA . PRO A 104 ? 0.6645 1.2352 0.7922 0.2056 -0.2340 0.0156 104 PRO A CA 790 C C . PRO A 104 ? 0.6482 1.1807 0.7444 0.1850 -0.2210 0.0180 104 PRO A C 791 O O . PRO A 104 ? 0.6327 1.1222 0.7050 0.1887 -0.2141 0.0279 104 PRO A O 792 C CB . PRO A 104 ? 0.6946 1.2756 0.8079 0.2180 -0.2572 0.0238 104 PRO A CB 793 C CG . PRO A 104 ? 0.7265 1.2729 0.8232 0.2414 -0.2626 0.0385 104 PRO A CG 794 C CD . PRO A 104 ? 0.7088 1.2547 0.8326 0.2513 -0.2496 0.0333 104 PRO A CD 795 N N . ARG A 105 ? 0.6328 1.1824 0.7307 0.1634 -0.2179 0.0081 105 ARG A N 796 C CA . ARG A 105 ? 0.6193 1.1388 0.6901 0.1437 -0.2069 0.0080 105 ARG A CA 797 C C . ARG A 105 ? 0.6398 1.1242 0.6704 0.1486 -0.2129 0.0218 105 ARG A C 798 O O . ARG A 105 ? 0.6775 1.1716 0.6956 0.1568 -0.2300 0.0276 105 ARG A O 799 C CB . ARG A 105 ? 0.6125 1.1584 0.6886 0.1233 -0.2087 -0.0044 105 ARG A CB 800 C CG . ARG A 105 ? 0.6194 1.1373 0.6739 0.1032 -0.1952 -0.0077 105 ARG A CG 801 C CD . ARG A 105 ? 0.6243 1.1646 0.6814 0.0840 -0.1985 -0.0202 105 ARG A CD 802 N NE . ARG A 105 ? 0.6226 1.1956 0.7155 0.0756 -0.1946 -0.0323 105 ARG A NE 803 C CZ . ARG A 105 ? 0.6458 1.2434 0.7483 0.0586 -0.1980 -0.0446 105 ARG A CZ 804 N NH1 . ARG A 105 ? 0.6775 1.2708 0.7562 0.0490 -0.2057 -0.0474 105 ARG A NH1 805 N NH2 . ARG A 105 ? 0.6366 1.2630 0.7719 0.0501 -0.1933 -0.0544 105 ARG A NH2 806 N N . PRO A 106 ? 0.6349 1.0790 0.6446 0.1428 -0.1991 0.0274 106 PRO A N 807 C CA . PRO A 106 ? 0.6665 1.0784 0.6371 0.1432 -0.2025 0.0397 106 PRO A CA 808 C C . PRO A 106 ? 0.6748 1.0923 0.6254 0.1257 -0.2042 0.0344 106 PRO A C 809 O O . PRO A 106 ? 0.6600 1.1012 0.6269 0.1124 -0.2013 0.0209 106 PRO A O 810 C CB . PRO A 106 ? 0.6568 1.0296 0.6176 0.1406 -0.1856 0.0447 106 PRO A CB 811 C CG . PRO A 106 ? 0.6168 1.0013 0.6054 0.1314 -0.1719 0.0321 106 PRO A CG 812 C CD . PRO A 106 ? 0.6095 1.0371 0.6303 0.1360 -0.1802 0.0228 106 PRO A CD 813 N N . LYS A 107 ? 0.7062 1.1013 0.6208 0.1253 -0.2084 0.0448 107 LYS A N 814 C CA . LYS A 107 ? 0.7232 1.1210 0.6149 0.1097 -0.2092 0.0396 107 LYS A CA 815 C C . LYS A 107 ? 0.7255 1.0951 0.6018 0.0950 -0.1904 0.0375 107 LYS A C 816 O O . LYS A 107 ? 0.7214 1.0992 0.5992 0.0797 -0.1841 0.0251 107 LYS A O 817 C CB . LYS A 107 ? 0.7705 1.1632 0.6295 0.1169 -0.2247 0.0516 107 LYS A CB 818 C CG . LYS A 107 ? 0.7977 1.2185 0.6696 0.1333 -0.2457 0.0548 107 LYS A CG 819 C CD . LYS A 107 ? 0.7883 1.2529 0.6953 0.1277 -0.2505 0.0381 107 LYS A CD 820 C CE . LYS A 107 ? 0.8183 1.3162 0.7330 0.1407 -0.2738 0.0398 107 LYS A CE 821 N NZ . LYS A 107 ? 0.8348 1.3272 0.7575 0.1651 -0.2828 0.0526 107 LYS A NZ 822 N N . SER A 108 ? 0.7342 1.0709 0.5966 0.0999 -0.1822 0.0491 108 SER A N 823 C CA . SER A 108 ? 0.7261 1.0367 0.5733 0.0874 -0.1653 0.0485 108 SER A CA 824 C C . SER A 108 ? 0.7274 1.0081 0.5735 0.0952 -0.1573 0.0596 108 SER A C 825 O O . SER A 108 ? 0.7568 1.0138 0.5769 0.0995 -0.1593 0.0734 108 SER A O 826 C CB . SER A 108 ? 0.7504 1.0524 0.5609 0.0792 -0.1669 0.0523 108 SER A CB 827 O OG . SER A 108 ? 0.7343 1.0216 0.5356 0.0653 -0.1506 0.0466 108 SER A OG 828 N N . THR A 109 ? 0.6898 0.9711 0.5630 0.0964 -0.1486 0.0536 109 THR A N 829 C CA . THR A 109 ? 0.6870 0.9423 0.5626 0.1044 -0.1421 0.0620 109 THR A CA 830 C C . THR A 109 ? 0.6488 0.8895 0.5305 0.0929 -0.1246 0.0559 109 THR A C 831 O O . THR A 109 ? 0.6324 0.8842 0.5201 0.0805 -0.1179 0.0448 109 THR A O 832 C CB . THR A 109 ? 0.6872 0.9551 0.5890 0.1207 -0.1492 0.0619 109 THR A CB 833 O OG1 . THR A 109 ? 0.6989 0.9372 0.5947 0.1313 -0.1469 0.0724 109 THR A OG1 834 C CG2 . THR A 109 ? 0.6592 0.9477 0.5931 0.1156 -0.1410 0.0478 109 THR A CG2 835 N N . THR A 110 ? 0.6247 0.8395 0.5045 0.0976 -0.1183 0.0632 110 THR A N 836 C CA . THR A 110 ? 0.5857 0.7849 0.4697 0.0881 -0.1032 0.0590 110 THR A CA 837 C C . THR A 110 ? 0.5426 0.7596 0.4549 0.0846 -0.0971 0.0458 110 THR A C 838 O O . THR A 110 ? 0.5273 0.7594 0.4598 0.0936 -0.1018 0.0428 110 THR A O 839 C CB . THR A 110 ? 0.5979 0.7675 0.4764 0.0950 -0.0998 0.0688 110 THR A CB 840 O OG1 . THR A 110 ? 0.6212 0.7715 0.4717 0.0970 -0.1051 0.0824 110 THR A OG1 841 C CG2 . THR A 110 ? 0.5971 0.7521 0.4792 0.0847 -0.0854 0.0646 110 THR A CG2 842 N N . VAL A 111 ? 0.5168 0.7317 0.4300 0.0716 -0.0866 0.0382 111 VAL A N 843 C CA . VAL A 111 ? 0.4850 0.7124 0.4207 0.0663 -0.0803 0.0267 111 VAL A CA 844 C C . VAL A 111 ? 0.4808 0.6879 0.4201 0.0634 -0.0687 0.0266 111 VAL A C 845 O O . VAL A 111 ? 0.5046 0.6935 0.4289 0.0582 -0.0630 0.0305 111 VAL A O 846 C CB . VAL A 111 ? 0.4700 0.7106 0.4039 0.0539 -0.0787 0.0169 111 VAL A CB 847 C CG1 . VAL A 111 ? 0.4422 0.6907 0.3966 0.0471 -0.0718 0.0063 111 VAL A CG1 848 C CG2 . VAL A 111 ? 0.4821 0.7440 0.4121 0.0557 -0.0911 0.0159 111 VAL A CG2 849 N N . MET A 112 ? 0.4571 0.6692 0.4161 0.0663 -0.0653 0.0219 112 MET A N 850 C CA . MET A 112 ? 0.4466 0.6419 0.4096 0.0630 -0.0551 0.0204 112 MET A CA 851 C C . MET A 112 ? 0.4410 0.6493 0.4203 0.0558 -0.0499 0.0102 112 MET A C 852 O O . MET A 112 ? 0.4576 0.6862 0.4517 0.0577 -0.0532 0.0057 112 MET A O 853 C CB . MET A 112 ? 0.4486 0.6317 0.4157 0.0742 -0.0552 0.0256 112 MET A CB 854 C CG . MET A 112 ? 0.4770 0.6413 0.4265 0.0810 -0.0602 0.0367 112 MET A CG 855 S SD . MET A 112 ? 0.4825 0.6288 0.4364 0.0950 -0.0610 0.0414 112 MET A SD 856 C CE . MET A 112 ? 0.4810 0.6084 0.4355 0.0856 -0.0487 0.0376 112 MET A CE 857 N N . VAL A 113 ? 0.4468 0.6434 0.4232 0.0472 -0.0419 0.0069 113 VAL A N 858 C CA . VAL A 113 ? 0.4481 0.6523 0.4357 0.0391 -0.0373 -0.0017 113 VAL A CA 859 C C . VAL A 113 ? 0.4601 0.6495 0.4516 0.0384 -0.0296 -0.0021 113 VAL A C 860 O O . VAL A 113 ? 0.4764 0.6493 0.4591 0.0359 -0.0255 -0.0001 113 VAL A O 861 C CB . VAL A 113 ? 0.4446 0.6492 0.4242 0.0295 -0.0363 -0.0069 113 VAL A CB 862 C CG1 . VAL A 113 ? 0.4285 0.6388 0.4188 0.0212 -0.0329 -0.0155 113 VAL A CG1 863 C CG2 . VAL A 113 ? 0.4496 0.6670 0.4211 0.0303 -0.0444 -0.0062 113 VAL A CG2 864 N N . TRP A 114 ? 0.4549 0.6524 0.4596 0.0401 -0.0277 -0.0050 114 TRP A N 865 C CA . TRP A 114 ? 0.4467 0.6320 0.4543 0.0404 -0.0211 -0.0054 114 TRP A CA 866 C C . TRP A 114 ? 0.4448 0.6258 0.4533 0.0303 -0.0161 -0.0104 114 TRP A C 867 O O . TRP A 114 ? 0.4389 0.6323 0.4541 0.0241 -0.0162 -0.0153 114 TRP A O 868 C CB . TRP A 114 ? 0.4403 0.6374 0.4605 0.0471 -0.0206 -0.0066 114 TRP A CB 869 C CG . TRP A 114 ? 0.4225 0.6088 0.4441 0.0468 -0.0136 -0.0079 114 TRP A CG 870 C CD1 . TRP A 114 ? 0.4264 0.6206 0.4561 0.0417 -0.0084 -0.0125 114 TRP A CD1 871 C CD2 . TRP A 114 ? 0.4285 0.5937 0.4417 0.0509 -0.0113 -0.0047 114 TRP A CD2 872 N NE1 . TRP A 114 ? 0.4283 0.6078 0.4538 0.0431 -0.0031 -0.0123 114 TRP A NE1 873 C CE2 . TRP A 114 ? 0.4271 0.5890 0.4431 0.0487 -0.0052 -0.0080 114 TRP A CE2 874 C CE3 . TRP A 114 ? 0.4406 0.5890 0.4431 0.0550 -0.0138 0.0008 114 TRP A CE3 875 C CZ2 . TRP A 114 ? 0.4213 0.5646 0.4302 0.0512 -0.0023 -0.0069 114 TRP A CZ2 876 C CZ3 . TRP A 114 ? 0.4616 0.5912 0.4584 0.0566 -0.0106 0.0019 114 TRP A CZ3 877 C CH2 . TRP A 114 ? 0.4500 0.5776 0.4502 0.0549 -0.0053 -0.0024 114 TRP A CH2 878 N N . ILE A 115 ? 0.4668 0.6297 0.4685 0.0288 -0.0121 -0.0092 115 ILE A N 879 C CA . ILE A 115 ? 0.4726 0.6279 0.4744 0.0215 -0.0078 -0.0129 115 ILE A CA 880 C C . ILE A 115 ? 0.4678 0.6139 0.4706 0.0234 -0.0037 -0.0120 115 ILE A C 881 O O . ILE A 115 ? 0.4698 0.6033 0.4674 0.0270 -0.0029 -0.0091 115 ILE A O 882 C CB . ILE A 115 ? 0.4790 0.6231 0.4727 0.0182 -0.0074 -0.0134 115 ILE A CB 883 C CG1 . ILE A 115 ? 0.4939 0.6466 0.4836 0.0171 -0.0110 -0.0144 115 ILE A CG1 884 C CG2 . ILE A 115 ? 0.4908 0.6278 0.4853 0.0121 -0.0048 -0.0177 115 ILE A CG2 885 C CD1 . ILE A 115 ? 0.5019 0.6469 0.4841 0.0144 -0.0094 -0.0161 115 ILE A CD1 886 N N . TYR A 116 ? 0.4720 0.6247 0.4809 0.0200 -0.0008 -0.0147 116 TYR A N 887 C CA . TYR A 116 ? 0.4743 0.6211 0.4829 0.0218 0.0035 -0.0143 116 TYR A CA 888 C C . TYR A 116 ? 0.4809 0.6089 0.4808 0.0191 0.0051 -0.0135 116 TYR A C 889 O O . TYR A 116 ? 0.4635 0.5849 0.4601 0.0147 0.0038 -0.0143 116 TYR A O 890 C CB . TYR A 116 ? 0.4843 0.6448 0.5007 0.0173 0.0072 -0.0172 116 TYR A CB 891 C CG . TYR A 116 ? 0.4786 0.6383 0.4945 0.0062 0.0083 -0.0195 116 TYR A CG 892 C CD1 . TYR A 116 ? 0.4894 0.6306 0.4962 0.0014 0.0099 -0.0187 116 TYR A CD1 893 C CD2 . TYR A 116 ? 0.4864 0.6631 0.5108 0.0006 0.0071 -0.0226 116 TYR A CD2 894 C CE1 . TYR A 116 ? 0.4916 0.6283 0.4967 -0.0081 0.0105 -0.0205 116 TYR A CE1 895 C CE2 . TYR A 116 ? 0.4770 0.6501 0.5001 -0.0105 0.0080 -0.0249 116 TYR A CE2 896 C CZ . TYR A 116 ? 0.4785 0.6300 0.4914 -0.0145 0.0098 -0.0236 116 TYR A CZ 897 O OH . TYR A 116 ? 0.4775 0.6218 0.4879 -0.0249 0.0102 -0.0257 116 TYR A OH 898 N N . GLY A 117 ? 0.4882 0.6083 0.4846 0.0225 0.0076 -0.0127 117 GLY A N 899 C CA . GLY A 117 ? 0.4868 0.5908 0.4750 0.0202 0.0083 -0.0121 117 GLY A CA 900 C C . GLY A 117 ? 0.4903 0.5927 0.4757 0.0147 0.0119 -0.0131 117 GLY A C 901 O O . GLY A 117 ? 0.4705 0.5836 0.4608 0.0100 0.0140 -0.0144 117 GLY A O 902 N N . GLY A 118 ? 0.4963 0.5854 0.4730 0.0145 0.0124 -0.0123 118 GLY A N 903 C CA . GLY A 118 ? 0.4800 0.5632 0.4495 0.0089 0.0152 -0.0118 118 GLY A CA 904 C C . GLY A 118 ? 0.4845 0.5519 0.4460 0.0064 0.0113 -0.0101 118 GLY A C 905 O O . GLY A 118 ? 0.4974 0.5579 0.4528 0.0009 0.0122 -0.0087 118 GLY A O 906 N N . GLY A 119 ? 0.4753 0.5370 0.4371 0.0105 0.0070 -0.0101 119 GLY A N 907 C CA . GLY A 119 ? 0.4670 0.5165 0.4237 0.0101 0.0025 -0.0092 119 GLY A CA 908 C C . GLY A 119 ? 0.4545 0.4999 0.4123 0.0071 0.0006 -0.0093 119 GLY A C 909 O O . GLY A 119 ? 0.4700 0.5035 0.4221 0.0073 -0.0031 -0.0081 119 GLY A O 910 N N . PHE A 120 ? 0.4480 0.5023 0.4126 0.0048 0.0024 -0.0110 120 PHE A N 911 C CA . PHE A 120 ? 0.4514 0.5009 0.4165 0.0010 0.0011 -0.0124 120 PHE A CA 912 C C . PHE A 120 ? 0.4595 0.4983 0.4163 -0.0056 0.0027 -0.0101 120 PHE A C 913 O O . PHE A 120 ? 0.4674 0.4986 0.4232 -0.0096 0.0015 -0.0112 120 PHE A O 914 C CB . PHE A 120 ? 0.4475 0.4895 0.4138 0.0053 -0.0036 -0.0142 120 PHE A CB 915 C CG . PHE A 120 ? 0.4412 0.4945 0.4154 0.0092 -0.0040 -0.0167 120 PHE A CG 916 C CD1 . PHE A 120 ? 0.4427 0.5055 0.4216 0.0078 -0.0028 -0.0197 120 PHE A CD1 917 C CD2 . PHE A 120 ? 0.4418 0.4959 0.4175 0.0134 -0.0057 -0.0161 120 PHE A CD2 918 C CE1 . PHE A 120 ? 0.4323 0.5045 0.4156 0.0107 -0.0028 -0.0211 120 PHE A CE1 919 C CE2 . PHE A 120 ? 0.4303 0.4941 0.4120 0.0154 -0.0053 -0.0177 120 PHE A CE2 920 C CZ . PHE A 120 ? 0.4268 0.4990 0.4112 0.0141 -0.0035 -0.0198 120 PHE A CZ 921 N N . TYR A 121 ? 0.4655 0.5026 0.4151 -0.0073 0.0057 -0.0070 121 TYR A N 922 C CA . TYR A 121 ? 0.4765 0.5037 0.4158 -0.0152 0.0086 -0.0037 121 TYR A CA 923 C C . TYR A 121 ? 0.4736 0.5163 0.4171 -0.0218 0.0159 -0.0044 121 TYR A C 924 O O . TYR A 121 ? 0.5328 0.5703 0.4690 -0.0306 0.0197 -0.0018 121 TYR A O 925 C CB . TYR A 121 ? 0.4833 0.4966 0.4082 -0.0136 0.0070 0.0004 121 TYR A CB 926 C CG . TYR A 121 ? 0.4825 0.5054 0.4053 -0.0110 0.0109 -0.0001 121 TYR A CG 927 C CD1 . TYR A 121 ? 0.4965 0.5260 0.4145 -0.0168 0.0185 0.0008 121 TYR A CD1 928 C CD2 . TYR A 121 ? 0.4667 0.4921 0.3925 -0.0033 0.0075 -0.0020 121 TYR A CD2 929 C CE1 . TYR A 121 ? 0.4986 0.5364 0.4144 -0.0133 0.0225 -0.0011 121 TYR A CE1 930 C CE2 . TYR A 121 ? 0.4855 0.5166 0.4083 -0.0008 0.0109 -0.0034 121 TYR A CE2 931 C CZ . TYR A 121 ? 0.5044 0.5413 0.4220 -0.0050 0.0183 -0.0033 121 TYR A CZ 932 O OH . TYR A 121 ? 0.5174 0.5595 0.4317 -0.0014 0.0221 -0.0060 121 TYR A OH 933 N N . SER A 122 ? 0.4454 0.5071 0.4005 -0.0175 0.0176 -0.0076 122 SER A N 934 C CA . SER A 122 ? 0.4453 0.5258 0.4070 -0.0205 0.0241 -0.0091 122 SER A CA 935 C C . SER A 122 ? 0.4336 0.5321 0.4095 -0.0147 0.0225 -0.0126 122 SER A C 936 O O . SER A 122 ? 0.4232 0.5180 0.4012 -0.0092 0.0174 -0.0132 122 SER A O 937 C CB . SER A 122 ? 0.4513 0.5321 0.4056 -0.0173 0.0284 -0.0081 122 SER A CB 938 O OG . SER A 122 ? 0.4254 0.5025 0.3791 -0.0076 0.0247 -0.0090 122 SER A OG 939 N N . GLY A 123 ? 0.4455 0.5643 0.4311 -0.0157 0.0269 -0.0147 123 GLY A N 940 C CA . GLY A 123 ? 0.4458 0.5825 0.4443 -0.0089 0.0245 -0.0173 123 GLY A CA 941 C C . GLY A 123 ? 0.4421 0.5999 0.4530 -0.0152 0.0258 -0.0201 123 GLY A C 942 O O . GLY A 123 ? 0.4362 0.5912 0.4458 -0.0261 0.0268 -0.0204 123 GLY A O 943 N N . SER A 124 ? 0.4372 0.6155 0.4602 -0.0083 0.0250 -0.0223 124 SER A N 944 C CA . SER A 124 ? 0.4447 0.6477 0.4822 -0.0131 0.0248 -0.0256 124 SER A CA 945 C C . SER A 124 ? 0.4454 0.6626 0.4921 -0.0027 0.0184 -0.0266 124 SER A C 946 O O . SER A 124 ? 0.4585 0.6723 0.5037 0.0088 0.0172 -0.0250 124 SER A O 947 C CB . SER A 124 ? 0.4639 0.6854 0.5093 -0.0166 0.0329 -0.0276 124 SER A CB 948 O OG . SER A 124 ? 0.4798 0.6905 0.5163 -0.0295 0.0387 -0.0261 124 SER A OG 949 N N . SER A 125 ? 0.4586 0.6900 0.5132 -0.0074 0.0138 -0.0290 125 SER A N 950 C CA . SER A 125 ? 0.4637 0.7103 0.5260 0.0019 0.0069 -0.0294 125 SER A CA 951 C C . SER A 125 ? 0.4665 0.7400 0.5449 0.0090 0.0085 -0.0315 125 SER A C 952 O O . SER A 125 ? 0.5088 0.7926 0.5927 0.0204 0.0027 -0.0308 125 SER A O 953 C CB . SER A 125 ? 0.4693 0.7242 0.5341 -0.0059 0.0009 -0.0323 125 SER A CB 954 O OG . SER A 125 ? 0.4643 0.7421 0.5427 -0.0157 0.0026 -0.0367 125 SER A OG 955 N N . THR A 126 ? 0.4502 0.7342 0.5352 0.0026 0.0166 -0.0340 126 THR A N 956 C CA . THR A 126 ? 0.4325 0.7490 0.5366 0.0055 0.0195 -0.0381 126 THR A CA 957 C C . THR A 126 ? 0.4330 0.7515 0.5389 0.0165 0.0262 -0.0387 126 THR A C 958 O O . THR A 126 ? 0.4289 0.7749 0.5509 0.0185 0.0308 -0.0430 126 THR A O 959 C CB . THR A 126 ? 0.4211 0.7523 0.5328 -0.0121 0.0256 -0.0414 126 THR A CB 960 O OG1 . THR A 126 ? 0.4161 0.7266 0.5140 -0.0198 0.0343 -0.0391 126 THR A OG1 961 C CG2 . THR A 126 ? 0.4167 0.7447 0.5265 -0.0238 0.0193 -0.0422 126 THR A CG2 962 N N . LEU A 127 ? 0.4475 0.7381 0.5373 0.0235 0.0268 -0.0353 127 LEU A N 963 C CA . LEU A 127 ? 0.4367 0.7253 0.5251 0.0328 0.0334 -0.0369 127 LEU A CA 964 C C . LEU A 127 ? 0.4419 0.7470 0.5435 0.0499 0.0294 -0.0392 127 LEU A C 965 O O . LEU A 127 ? 0.4402 0.7439 0.5432 0.0569 0.0199 -0.0365 127 LEU A O 966 C CB . LEU A 127 ? 0.4286 0.6824 0.4962 0.0353 0.0334 -0.0332 127 LEU A CB 967 C CG . LEU A 127 ? 0.4344 0.6677 0.4870 0.0216 0.0359 -0.0303 127 LEU A CG 968 C CD1 . LEU A 127 ? 0.4467 0.6510 0.4821 0.0264 0.0352 -0.0277 127 LEU A CD1 969 C CD2 . LEU A 127 ? 0.4364 0.6804 0.4902 0.0101 0.0453 -0.0324 127 LEU A CD2 970 N N . ASP A 128 ? 0.4740 0.7940 0.5842 0.0573 0.0366 -0.0442 128 ASP A N 971 C CA . ASP A 128 ? 0.4990 0.8315 0.6212 0.0763 0.0330 -0.0469 128 ASP A CA 972 C C . ASP A 128 ? 0.5184 0.8207 0.6265 0.0871 0.0239 -0.0414 128 ASP A C 973 O O . ASP A 128 ? 0.5346 0.8421 0.6487 0.0968 0.0144 -0.0389 128 ASP A O 974 C CB . ASP A 128 ? 0.5041 0.8456 0.6307 0.0839 0.0434 -0.0535 128 ASP A CB 975 C CG . ASP A 128 ? 0.5152 0.8956 0.6612 0.0760 0.0525 -0.0597 128 ASP A CG 976 O OD1 . ASP A 128 ? 0.5155 0.9172 0.6740 0.0659 0.0493 -0.0592 128 ASP A OD1 977 O OD2 . ASP A 128 ? 0.5184 0.9086 0.6668 0.0791 0.0632 -0.0656 128 ASP A OD2 978 N N . VAL A 129 ? 0.5083 0.7791 0.5968 0.0842 0.0266 -0.0389 129 VAL A N 979 C CA . VAL A 129 ? 0.5050 0.7462 0.5796 0.0923 0.0198 -0.0340 129 VAL A CA 980 C C . VAL A 129 ? 0.4969 0.7319 0.5677 0.0892 0.0100 -0.0275 129 VAL A C 981 O O . VAL A 129 ? 0.5122 0.7284 0.5744 0.0973 0.0037 -0.0230 129 VAL A O 982 C CB . VAL A 129 ? 0.5075 0.7197 0.5631 0.0869 0.0246 -0.0335 129 VAL A CB 983 C CG1 . VAL A 129 ? 0.4972 0.7003 0.5436 0.0708 0.0247 -0.0298 129 VAL A CG1 984 C CG2 . VAL A 129 ? 0.5160 0.7003 0.5600 0.0969 0.0195 -0.0307 129 VAL A CG2 985 N N . TYR A 130 ? 0.4794 0.7284 0.5549 0.0770 0.0090 -0.0272 130 TYR A N 986 C CA . TYR A 130 ? 0.4626 0.7094 0.5346 0.0743 0.0002 -0.0225 130 TYR A CA 987 C C . TYR A 130 ? 0.4495 0.7269 0.5381 0.0783 -0.0060 -0.0242 130 TYR A C 988 O O . TYR A 130 ? 0.4697 0.7527 0.5574 0.0716 -0.0118 -0.0226 130 TYR A O 989 C CB . TYR A 130 ? 0.4556 0.6939 0.5193 0.0583 0.0017 -0.0216 130 TYR A CB 990 C CG . TYR A 130 ? 0.4583 0.6712 0.5077 0.0523 0.0071 -0.0205 130 TYR A CG 991 C CD1 . TYR A 130 ? 0.4500 0.6401 0.4884 0.0594 0.0068 -0.0179 130 TYR A CD1 992 C CD2 . TYR A 130 ? 0.4544 0.6653 0.5009 0.0392 0.0116 -0.0220 130 TYR A CD2 993 C CE1 . TYR A 130 ? 0.4472 0.6170 0.4737 0.0536 0.0105 -0.0174 130 TYR A CE1 994 C CE2 . TYR A 130 ? 0.4444 0.6333 0.4780 0.0347 0.0150 -0.0206 130 TYR A CE2 995 C CZ . TYR A 130 ? 0.4579 0.6280 0.4822 0.0419 0.0143 -0.0186 130 TYR A CZ 996 O OH . TYR A 130 ? 0.4620 0.6125 0.4743 0.0372 0.0166 -0.0178 130 TYR A OH 997 N N . ASN A 131 ? 0.4430 0.7415 0.5472 0.0892 -0.0050 -0.0281 131 ASN A N 998 C CA . ASN A 131 ? 0.4369 0.7667 0.5586 0.0946 -0.0124 -0.0298 131 ASN A CA 999 C C . ASN A 131 ? 0.4497 0.7674 0.5627 0.1058 -0.0242 -0.0231 131 ASN A C 1000 O O . ASN A 131 ? 0.4566 0.7598 0.5652 0.1207 -0.0267 -0.0204 131 ASN A O 1001 C CB . ASN A 131 ? 0.4348 0.7916 0.5769 0.1055 -0.0083 -0.0362 131 ASN A CB 1002 C CG . ASN A 131 ? 0.4224 0.8201 0.5874 0.1063 -0.0140 -0.0401 131 ASN A CG 1003 O OD1 . ASN A 131 ? 0.4178 0.8213 0.5822 0.1052 -0.0246 -0.0369 131 ASN A OD1 1004 N ND2 . ASN A 131 ? 0.4177 0.8459 0.6034 0.1080 -0.0067 -0.0475 131 ASN A ND2 1005 N N . GLY A 132 ? 0.4543 0.7764 0.5631 0.0982 -0.0314 -0.0205 132 GLY A N 1006 C CA . GLY A 132 ? 0.4713 0.7793 0.5669 0.1058 -0.0420 -0.0130 132 GLY A CA 1007 C C . GLY A 132 ? 0.4774 0.8057 0.5840 0.1213 -0.0530 -0.0115 132 GLY A C 1008 O O . GLY A 132 ? 0.4800 0.7981 0.5740 0.1267 -0.0627 -0.0045 132 GLY A O 1009 N N . LYS A 133 ? 0.4852 0.8428 0.6146 0.1289 -0.0516 -0.0179 133 LYS A N 1010 C CA . LYS A 133 ? 0.5126 0.8937 0.6555 0.1449 -0.0632 -0.0172 133 LYS A CA 1011 C C . LYS A 133 ? 0.5387 0.8947 0.6712 0.1648 -0.0690 -0.0104 133 LYS A C 1012 O O . LYS A 133 ? 0.5676 0.9250 0.6963 0.1758 -0.0818 -0.0045 133 LYS A O 1013 C CB . LYS A 133 ? 0.4994 0.9232 0.6728 0.1476 -0.0599 -0.0269 133 LYS A CB 1014 C CG . LYS A 133 ? 0.5052 0.9283 0.6882 0.1582 -0.0498 -0.0319 133 LYS A CG 1015 C CD . LYS A 133 ? 0.4977 0.9629 0.7078 0.1512 -0.0416 -0.0422 133 LYS A CD 1016 C CE . LYS A 133 ? 0.5003 0.9803 0.7277 0.1677 -0.0351 -0.0489 133 LYS A CE 1017 N NZ . LYS A 133 ? 0.4848 1.0143 0.7421 0.1615 -0.0291 -0.0586 133 LYS A NZ 1018 N N . TYR A 134 ? 0.5357 0.8664 0.6612 0.1690 -0.0602 -0.0110 134 TYR A N 1019 C CA . TYR A 134 ? 0.5565 0.8602 0.6721 0.1876 -0.0651 -0.0054 134 TYR A CA 1020 C C . TYR A 134 ? 0.5659 0.8379 0.6552 0.1847 -0.0729 0.0061 134 TYR A C 1021 O O . TYR A 134 ? 0.6028 0.8643 0.6849 0.1989 -0.0840 0.0135 134 TYR A O 1022 C CB . TYR A 134 ? 0.5566 0.8378 0.6681 0.1902 -0.0538 -0.0096 134 TYR A CB 1023 C CG . TYR A 134 ? 0.5460 0.8580 0.6805 0.1911 -0.0439 -0.0212 134 TYR A CG 1024 C CD1 . TYR A 134 ? 0.5623 0.9007 0.7186 0.2095 -0.0469 -0.0267 134 TYR A CD1 1025 C CD2 . TYR A 134 ? 0.5273 0.8432 0.6619 0.1735 -0.0316 -0.0264 134 TYR A CD2 1026 C CE1 . TYR A 134 ? 0.5579 0.9278 0.7360 0.2095 -0.0365 -0.0378 134 TYR A CE1 1027 C CE2 . TYR A 134 ? 0.5170 0.8612 0.6707 0.1727 -0.0217 -0.0362 134 TYR A CE2 1028 C CZ . TYR A 134 ? 0.5295 0.9018 0.7052 0.1902 -0.0235 -0.0422 134 TYR A CZ 1029 O OH . TYR A 134 ? 0.5091 0.9121 0.7042 0.1888 -0.0123 -0.0524 134 TYR A OH 1030 N N . LEU A 135 ? 0.5372 0.7947 0.6121 0.1662 -0.0671 0.0078 135 LEU A N 1031 C CA . LEU A 135 ? 0.5385 0.7682 0.5886 0.1606 -0.0718 0.0178 135 LEU A CA 1032 C C . LEU A 135 ? 0.5496 0.7979 0.5982 0.1614 -0.0839 0.0221 135 LEU A C 1033 O O . LEU A 135 ? 0.5676 0.8001 0.6013 0.1703 -0.0935 0.0316 135 LEU A O 1034 C CB . LEU A 135 ? 0.5199 0.7359 0.5594 0.1412 -0.0619 0.0163 135 LEU A CB 1035 C CG . LEU A 135 ? 0.5235 0.7063 0.5382 0.1340 -0.0616 0.0247 135 LEU A CG 1036 C CD1 . LEU A 135 ? 0.5495 0.7015 0.5519 0.1461 -0.0646 0.0319 135 LEU A CD1 1037 C CD2 . LEU A 135 ? 0.5051 0.6788 0.5168 0.1188 -0.0507 0.0203 135 LEU A CD2 1038 N N . ALA A 136 ? 0.5328 0.8139 0.5960 0.1520 -0.0837 0.0151 136 ALA A N 1039 C CA . ALA A 136 ? 0.5340 0.8365 0.5970 0.1516 -0.0955 0.0171 136 ALA A CA 1040 C C . ALA A 136 ? 0.5644 0.8740 0.6320 0.1727 -0.1086 0.0222 136 ALA A C 1041 O O . ALA A 136 ? 0.5945 0.8948 0.6451 0.1774 -0.1197 0.0312 136 ALA A O 1042 C CB . ALA A 136 ? 0.5095 0.8493 0.5931 0.1401 -0.0935 0.0068 136 ALA A CB 1043 N N . TYR A 137 ? 0.5580 0.8837 0.6479 0.1860 -0.1071 0.0164 137 TYR A N 1044 C CA . TYR A 137 ? 0.5618 0.8974 0.6603 0.2085 -0.1196 0.0197 137 TYR A CA 1045 C C . TYR A 137 ? 0.5906 0.8821 0.6648 0.2212 -0.1243 0.0314 137 TYR A C 1046 O O . TYR A 137 ? 0.6174 0.9029 0.6800 0.2318 -0.1381 0.0407 137 TYR A O 1047 C CB . TYR A 137 ? 0.5434 0.9085 0.6733 0.2196 -0.1148 0.0090 137 TYR A CB 1048 C CG . TYR A 137 ? 0.5654 0.9369 0.7059 0.2462 -0.1261 0.0111 137 TYR A CG 1049 C CD1 . TYR A 137 ? 0.5786 0.9820 0.7314 0.2563 -0.1416 0.0123 137 TYR A CD1 1050 C CD2 . TYR A 137 ? 0.5844 0.9295 0.7225 0.2620 -0.1220 0.0114 137 TYR A CD2 1051 C CE1 . TYR A 137 ? 0.5946 1.0037 0.7577 0.2828 -0.1531 0.0144 137 TYR A CE1 1052 C CE2 . TYR A 137 ? 0.6081 0.9566 0.7559 0.2883 -0.1327 0.0130 137 TYR A CE2 1053 C CZ . TYR A 137 ? 0.6113 0.9922 0.7720 0.2991 -0.1484 0.0147 137 TYR A CZ 1054 O OH . TYR A 137 ? 0.6392 1.0235 0.8103 0.3268 -0.1598 0.0162 137 TYR A OH 1055 N N . THR A 138 ? 0.5940 0.8534 0.6589 0.2191 -0.1134 0.0315 138 THR A N 1056 C CA . THR A 138 ? 0.6226 0.8400 0.6672 0.2316 -0.1175 0.0413 138 THR A CA 1057 C C . THR A 138 ? 0.6376 0.8268 0.6513 0.2228 -0.1231 0.0545 138 THR A C 1058 O O . THR A 138 ? 0.6513 0.8216 0.6501 0.2355 -0.1346 0.0652 138 THR A O 1059 C CB . THR A 138 ? 0.6209 0.8111 0.6631 0.2304 -0.1047 0.0370 138 THR A CB 1060 O OG1 . THR A 138 ? 0.6046 0.8228 0.6741 0.2376 -0.0981 0.0243 138 THR A OG1 1061 C CG2 . THR A 138 ? 0.6587 0.8059 0.6825 0.2449 -0.1100 0.0460 138 THR A CG2 1062 N N . GLU A 139 ? 0.6246 0.8109 0.6280 0.2014 -0.1150 0.0537 139 GLU A N 1063 C CA . GLU A 139 ? 0.6570 0.8182 0.6311 0.1910 -0.1175 0.0649 139 GLU A CA 1064 C C . GLU A 139 ? 0.6637 0.8489 0.6329 0.1852 -0.1263 0.0671 139 GLU A C 1065 O O . GLU A 139 ? 0.6724 0.8405 0.6165 0.1766 -0.1283 0.0758 139 GLU A O 1066 C CB . GLU A 139 ? 0.6588 0.8014 0.6234 0.1722 -0.1035 0.0626 139 GLU A CB 1067 C CG . GLU A 139 ? 0.6705 0.7853 0.6352 0.1759 -0.0954 0.0611 139 GLU A CG 1068 C CD . GLU A 139 ? 0.6996 0.7772 0.6449 0.1870 -0.1020 0.0727 139 GLU A CD 1069 O OE1 . GLU A 139 ? 0.7234 0.7873 0.6470 0.1836 -0.1084 0.0840 139 GLU A OE1 1070 O OE2 . GLU A 139 ? 0.7036 0.7645 0.6539 0.1988 -0.1006 0.0703 139 GLU A OE2 1071 N N . GLU A 140 ? 0.6506 0.8760 0.6432 0.1890 -0.1313 0.0586 140 GLU A N 1072 C CA . GLU A 140 ? 0.6590 0.9106 0.6491 0.1842 -0.1413 0.0589 140 GLU A CA 1073 C C . GLU A 140 ? 0.6324 0.8788 0.6064 0.1624 -0.1338 0.0577 140 GLU A C 1074 O O . GLU A 140 ? 0.6294 0.8656 0.5791 0.1576 -0.1393 0.0655 140 GLU A O 1075 C CB . GLU A 140 ? 0.7175 0.9601 0.6911 0.1993 -0.1577 0.0714 140 GLU A CB 1076 C CG . GLU A 140 ? 0.7590 0.9995 0.7470 0.2229 -0.1642 0.0729 140 GLU A CG 1077 C CD . GLU A 140 ? 0.8046 1.0572 0.7898 0.2403 -0.1836 0.0804 140 GLU A CD 1078 O OE1 . GLU A 140 ? 0.8467 1.0743 0.8013 0.2406 -0.1918 0.0939 140 GLU A OE1 1079 O OE2 . GLU A 140 ? 0.8086 1.0964 0.8221 0.2535 -0.1905 0.0730 140 GLU A OE2 1080 N N . VAL A 141 ? 0.6007 0.8544 0.5884 0.1501 -0.1211 0.0474 141 VAL A N 1081 C CA . VAL A 141 ? 0.5796 0.8296 0.5572 0.1306 -0.1125 0.0437 141 VAL A CA 1082 C C . VAL A 141 ? 0.5524 0.8348 0.5524 0.1212 -0.1092 0.0308 141 VAL A C 1083 O O . VAL A 141 ? 0.5283 0.8316 0.5525 0.1275 -0.1090 0.0245 141 VAL A O 1084 C CB . VAL A 141 ? 0.5796 0.7990 0.5488 0.1235 -0.0993 0.0449 141 VAL A CB 1085 C CG1 . VAL A 141 ? 0.6135 0.7990 0.5587 0.1292 -0.1018 0.0579 141 VAL A CG1 1086 C CG2 . VAL A 141 ? 0.5521 0.7743 0.5427 0.1277 -0.0914 0.0378 141 VAL A CG2 1087 N N . VAL A 142 ? 0.5441 0.8304 0.5355 0.1058 -0.1066 0.0265 142 VAL A N 1088 C CA . VAL A 142 ? 0.5261 0.8353 0.5354 0.0940 -0.1017 0.0145 142 VAL A CA 1089 C C . VAL A 142 ? 0.5200 0.8102 0.5306 0.0855 -0.0873 0.0113 142 VAL A C 1090 O O . VAL A 142 ? 0.5317 0.7996 0.5246 0.0783 -0.0818 0.0140 142 VAL A O 1091 C CB . VAL A 142 ? 0.5156 0.8361 0.5144 0.0822 -0.1065 0.0104 142 VAL A CB 1092 C CG1 . VAL A 142 ? 0.4918 0.8294 0.5069 0.0682 -0.1005 -0.0019 142 VAL A CG1 1093 C CG2 . VAL A 142 ? 0.5332 0.8741 0.5303 0.0911 -0.1223 0.0137 142 VAL A CG2 1094 N N . LEU A 143 ? 0.5228 0.8232 0.5541 0.0866 -0.0813 0.0055 143 LEU A N 1095 C CA . LEU A 143 ? 0.5212 0.8043 0.5538 0.0801 -0.0687 0.0029 143 LEU A CA 1096 C C . LEU A 143 ? 0.4977 0.7936 0.5398 0.0650 -0.0629 -0.0065 143 LEU A C 1097 O O . LEU A 143 ? 0.4935 0.8161 0.5541 0.0629 -0.0644 -0.0127 143 LEU A O 1098 C CB . LEU A 143 ? 0.5302 0.8127 0.5759 0.0916 -0.0652 0.0031 143 LEU A CB 1099 C CG . LEU A 143 ? 0.5418 0.7994 0.5827 0.0891 -0.0542 0.0033 143 LEU A CG 1100 C CD1 . LEU A 143 ? 0.5346 0.7960 0.5812 0.0746 -0.0452 -0.0039 143 LEU A CD1 1101 C CD2 . LEU A 143 ? 0.5567 0.7831 0.5753 0.0888 -0.0539 0.0111 143 LEU A CD2 1102 N N . VAL A 144 ? 0.4630 0.7400 0.4930 0.0545 -0.0563 -0.0075 144 VAL A N 1103 C CA . VAL A 144 ? 0.4417 0.7241 0.4778 0.0406 -0.0509 -0.0156 144 VAL A CA 1104 C C . VAL A 144 ? 0.4274 0.6917 0.4640 0.0379 -0.0406 -0.0159 144 VAL A C 1105 O O . VAL A 144 ? 0.4208 0.6632 0.4461 0.0419 -0.0376 -0.0108 144 VAL A O 1106 C CB . VAL A 144 ? 0.4435 0.7183 0.4646 0.0311 -0.0524 -0.0181 144 VAL A CB 1107 C CG1 . VAL A 144 ? 0.4368 0.7145 0.4641 0.0175 -0.0477 -0.0268 144 VAL A CG1 1108 C CG2 . VAL A 144 ? 0.4556 0.7455 0.4710 0.0339 -0.0632 -0.0171 144 VAL A CG2 1109 N N . SER A 145 ? 0.4210 0.6943 0.4699 0.0304 -0.0353 -0.0216 145 SER A N 1110 C CA . SER A 145 ? 0.4198 0.6748 0.4658 0.0253 -0.0261 -0.0222 145 SER A CA 1111 C C . SER A 145 ? 0.4314 0.6853 0.4768 0.0111 -0.0239 -0.0280 145 SER A C 1112 O O . SER A 145 ? 0.4453 0.7182 0.5013 0.0040 -0.0255 -0.0330 145 SER A O 1113 C CB . SER A 145 ? 0.4191 0.6807 0.4767 0.0297 -0.0207 -0.0225 145 SER A CB 1114 O OG . SER A 145 ? 0.4303 0.7135 0.5024 0.0217 -0.0184 -0.0281 145 SER A OG 1115 N N . LEU A 146 ? 0.4353 0.6666 0.4683 0.0072 -0.0207 -0.0276 146 LEU A N 1116 C CA . LEU A 146 ? 0.4363 0.6603 0.4666 -0.0045 -0.0186 -0.0329 146 LEU A CA 1117 C C . LEU A 146 ? 0.4381 0.6505 0.4702 -0.0092 -0.0113 -0.0327 146 LEU A C 1118 O O . LEU A 146 ? 0.4238 0.6345 0.4584 -0.0035 -0.0075 -0.0291 146 LEU A O 1119 C CB . LEU A 146 ? 0.4375 0.6457 0.4540 -0.0051 -0.0199 -0.0337 146 LEU A CB 1120 C CG . LEU A 146 ? 0.4387 0.6284 0.4457 0.0015 -0.0170 -0.0287 146 LEU A CG 1121 C CD1 . LEU A 146 ? 0.4378 0.6109 0.4444 -0.0009 -0.0112 -0.0285 146 LEU A CD1 1122 C CD2 . LEU A 146 ? 0.4431 0.6268 0.4388 0.0012 -0.0188 -0.0303 146 LEU A CD2 1123 N N . SER A 147 ? 0.4416 0.6450 0.4710 -0.0198 -0.0097 -0.0368 147 SER A N 1124 C CA . SER A 147 ? 0.4388 0.6269 0.4657 -0.0250 -0.0037 -0.0358 147 SER A CA 1125 C C . SER A 147 ? 0.4327 0.5978 0.4487 -0.0287 -0.0041 -0.0378 147 SER A C 1126 O O . SER A 147 ? 0.4108 0.5751 0.4228 -0.0289 -0.0080 -0.0417 147 SER A O 1127 C CB . SER A 147 ? 0.4409 0.6419 0.4773 -0.0357 -0.0008 -0.0383 147 SER A CB 1128 O OG . SER A 147 ? 0.4659 0.6630 0.5006 -0.0469 -0.0031 -0.0436 147 SER A OG 1129 N N . TYR A 148 ? 0.4388 0.5855 0.4492 -0.0306 -0.0002 -0.0354 148 TYR A N 1130 C CA . TYR A 148 ? 0.4514 0.5751 0.4523 -0.0319 -0.0009 -0.0371 148 TYR A CA 1131 C C . TYR A 148 ? 0.4602 0.5663 0.4558 -0.0360 0.0027 -0.0337 148 TYR A C 1132 O O . TYR A 148 ? 0.4589 0.5689 0.4557 -0.0347 0.0062 -0.0292 148 TYR A O 1133 C CB . TYR A 148 ? 0.4440 0.5616 0.4403 -0.0217 -0.0025 -0.0359 148 TYR A CB 1134 C CG . TYR A 148 ? 0.4271 0.5427 0.4228 -0.0143 -0.0004 -0.0300 148 TYR A CG 1135 C CD1 . TYR A 148 ? 0.4232 0.5534 0.4236 -0.0088 -0.0004 -0.0272 148 TYR A CD1 1136 C CD2 . TYR A 148 ? 0.4253 0.5235 0.4153 -0.0122 0.0007 -0.0277 148 TYR A CD2 1137 C CE1 . TYR A 148 ? 0.4129 0.5385 0.4116 -0.0024 0.0013 -0.0228 148 TYR A CE1 1138 C CE2 . TYR A 148 ? 0.4208 0.5170 0.4095 -0.0063 0.0019 -0.0233 148 TYR A CE2 1139 C CZ . TYR A 148 ? 0.4075 0.5166 0.4004 -0.0019 0.0025 -0.0213 148 TYR A CZ 1140 O OH . TYR A 148 ? 0.3930 0.4973 0.3835 0.0034 0.0036 -0.0179 148 TYR A OH 1141 N N . ARG A 149 ? 0.4702 0.5560 0.4587 -0.0406 0.0015 -0.0359 149 ARG A N 1142 C CA . ARG A 149 ? 0.4770 0.5422 0.4573 -0.0445 0.0036 -0.0318 149 ARG A CA 1143 C C . ARG A 149 ? 0.4730 0.5294 0.4483 -0.0347 0.0036 -0.0269 149 ARG A C 1144 O O . ARG A 149 ? 0.4661 0.5220 0.4421 -0.0259 0.0009 -0.0283 149 ARG A O 1145 C CB . ARG A 149 ? 0.4909 0.5331 0.4638 -0.0497 0.0010 -0.0353 149 ARG A CB 1146 C CG . ARG A 149 ? 0.5104 0.5562 0.4860 -0.0633 0.0015 -0.0395 149 ARG A CG 1147 C CD . ARG A 149 ? 0.5333 0.5541 0.5010 -0.0671 -0.0019 -0.0447 149 ARG A CD 1148 N NE . ARG A 149 ? 0.5178 0.5435 0.4875 -0.0598 -0.0056 -0.0523 149 ARG A NE 1149 C CZ . ARG A 149 ? 0.5275 0.5339 0.4911 -0.0591 -0.0087 -0.0590 149 ARG A CZ 1150 N NH1 . ARG A 149 ? 0.5538 0.5314 0.5086 -0.0647 -0.0094 -0.0585 149 ARG A NH1 1151 N NH2 . ARG A 149 ? 0.5210 0.5357 0.4861 -0.0525 -0.0108 -0.0663 149 ARG A NH2 1152 N N . VAL A 150 ? 0.4836 0.5346 0.4538 -0.0371 0.0069 -0.0214 150 VAL A N 1153 C CA . VAL A 150 ? 0.4793 0.5210 0.4430 -0.0294 0.0063 -0.0169 150 VAL A CA 1154 C C . VAL A 150 ? 0.5031 0.5198 0.4539 -0.0331 0.0053 -0.0129 150 VAL A C 1155 O O . VAL A 150 ? 0.5355 0.5418 0.4821 -0.0426 0.0062 -0.0129 150 VAL A O 1156 C CB . VAL A 150 ? 0.4771 0.5335 0.4431 -0.0278 0.0108 -0.0141 150 VAL A CB 1157 C CG1 . VAL A 150 ? 0.4619 0.5391 0.4390 -0.0217 0.0104 -0.0169 150 VAL A CG1 1158 C CG2 . VAL A 150 ? 0.4873 0.5489 0.4521 -0.0384 0.0166 -0.0124 150 VAL A CG2 1159 N N . GLY A 151 ? 0.5050 0.5113 0.4488 -0.0261 0.0029 -0.0093 151 GLY A N 1160 C CA . GLY A 151 ? 0.5320 0.5138 0.4614 -0.0281 0.0006 -0.0042 151 GLY A CA 1161 C C . GLY A 151 ? 0.5441 0.5065 0.4712 -0.0263 -0.0048 -0.0065 151 GLY A C 1162 O O . GLY A 151 ? 0.5464 0.5153 0.4828 -0.0210 -0.0071 -0.0127 151 GLY A O 1163 N N . ALA A 152 ? 0.5625 0.4999 0.4758 -0.0306 -0.0067 -0.0017 152 ALA A N 1164 C CA . ALA A 152 ? 0.5781 0.4926 0.4876 -0.0288 -0.0121 -0.0039 152 ALA A CA 1165 C C . ALA A 152 ? 0.5795 0.5004 0.4976 -0.0352 -0.0100 -0.0115 152 ALA A C 1166 O O . ALA A 152 ? 0.5787 0.4918 0.5002 -0.0296 -0.0139 -0.0177 152 ALA A O 1167 C CB . ALA A 152 ? 0.6065 0.4909 0.4974 -0.0351 -0.0138 0.0039 152 ALA A CB 1168 N N . PHE A 153 ? 0.5820 0.5189 0.5041 -0.0466 -0.0039 -0.0115 153 PHE A N 1169 C CA . PHE A 153 ? 0.5672 0.5117 0.4966 -0.0552 -0.0024 -0.0184 153 PHE A CA 1170 C C . PHE A 153 ? 0.5553 0.5168 0.4966 -0.0464 -0.0047 -0.0266 153 PHE A C 1171 O O . PHE A 153 ? 0.5847 0.5423 0.5280 -0.0492 -0.0065 -0.0339 153 PHE A O 1172 C CB . PHE A 153 ? 0.5674 0.5328 0.5020 -0.0674 0.0043 -0.0168 153 PHE A CB 1173 C CG . PHE A 153 ? 0.5948 0.5462 0.5169 -0.0778 0.0084 -0.0087 153 PHE A CG 1174 C CD1 . PHE A 153 ? 0.6176 0.5472 0.5307 -0.0912 0.0088 -0.0074 153 PHE A CD1 1175 C CD2 . PHE A 153 ? 0.6167 0.5744 0.5340 -0.0746 0.0117 -0.0023 153 PHE A CD2 1176 C CE1 . PHE A 153 ? 0.6443 0.5595 0.5434 -0.1019 0.0131 0.0012 153 PHE A CE1 1177 C CE2 . PHE A 153 ? 0.6379 0.5825 0.5409 -0.0845 0.0160 0.0054 153 PHE A CE2 1178 C CZ . PHE A 153 ? 0.6546 0.5781 0.5483 -0.0984 0.0170 0.0077 153 PHE A CZ 1179 N N . GLY A 154 ? 0.5244 0.5030 0.4718 -0.0365 -0.0045 -0.0256 154 GLY A N 1180 C CA . GLY A 154 ? 0.5051 0.5005 0.4620 -0.0286 -0.0058 -0.0317 154 GLY A CA 1181 C C . GLY A 154 ? 0.4955 0.4838 0.4525 -0.0163 -0.0094 -0.0334 154 GLY A C 1182 O O . GLY A 154 ? 0.4798 0.4778 0.4426 -0.0111 -0.0101 -0.0395 154 GLY A O 1183 N N . PHE A 155 ? 0.4882 0.4611 0.4389 -0.0117 -0.0118 -0.0281 155 PHE A N 1184 C CA . PHE A 155 ? 0.4729 0.4444 0.4267 0.0003 -0.0156 -0.0296 155 PHE A CA 1185 C C . PHE A 155 ? 0.5002 0.4465 0.4468 0.0062 -0.0213 -0.0281 155 PHE A C 1186 O O . PHE A 155 ? 0.4981 0.4460 0.4493 0.0168 -0.0250 -0.0295 155 PHE A O 1187 C CB . PHE A 155 ? 0.4450 0.4334 0.4030 0.0040 -0.0142 -0.0255 155 PHE A CB 1188 C CG . PHE A 155 ? 0.4312 0.4426 0.3971 0.0021 -0.0102 -0.0279 155 PHE A CG 1189 C CD1 . PHE A 155 ? 0.4242 0.4471 0.3972 0.0068 -0.0101 -0.0336 155 PHE A CD1 1190 C CD2 . PHE A 155 ? 0.4211 0.4426 0.3869 -0.0042 -0.0065 -0.0246 155 PHE A CD2 1191 C CE1 . PHE A 155 ? 0.4049 0.4465 0.3826 0.0051 -0.0073 -0.0346 155 PHE A CE1 1192 C CE2 . PHE A 155 ? 0.4154 0.4567 0.3882 -0.0044 -0.0042 -0.0263 155 PHE A CE2 1193 C CZ . PHE A 155 ? 0.4102 0.4601 0.3877 0.0001 -0.0050 -0.0307 155 PHE A CZ 1194 N N . LEU A 156 ? 0.5428 0.4661 0.4787 -0.0003 -0.0224 -0.0257 156 LEU A N 1195 C CA . LEU A 156 ? 0.5926 0.4886 0.5207 0.0066 -0.0288 -0.0245 156 LEU A CA 1196 C C . LEU A 156 ? 0.6028 0.5009 0.5404 0.0170 -0.0313 -0.0346 156 LEU A C 1197 O O . LEU A 156 ? 0.6442 0.5478 0.5858 0.0132 -0.0283 -0.0423 156 LEU A O 1198 C CB . LEU A 156 ? 0.6249 0.4929 0.5390 -0.0037 -0.0292 -0.0209 156 LEU A CB 1199 C CG . LEU A 156 ? 0.6613 0.4968 0.5633 0.0035 -0.0368 -0.0162 156 LEU A CG 1200 C CD1 . LEU A 156 ? 0.6766 0.5067 0.5666 0.0013 -0.0379 -0.0046 156 LEU A CD1 1201 C CD2 . LEU A 156 ? 0.6938 0.4982 0.5851 -0.0039 -0.0380 -0.0176 156 LEU A CD2 1202 N N . ALA A 157 ? 0.6230 0.5183 0.5643 0.0302 -0.0367 -0.0351 157 ALA A N 1203 C CA . ALA A 157 ? 0.6311 0.5345 0.5840 0.0416 -0.0378 -0.0454 157 ALA A CA 1204 C C . ALA A 157 ? 0.6604 0.5401 0.6112 0.0542 -0.0456 -0.0475 157 ALA A C 1205 O O . ALA A 157 ? 0.6696 0.5520 0.6244 0.0644 -0.0510 -0.0444 157 ALA A O 1206 C CB . ALA A 157 ? 0.5944 0.5287 0.5608 0.0469 -0.0358 -0.0465 157 ALA A CB 1207 N N . LEU A 158 ? 0.7024 0.5593 0.6473 0.0539 -0.0465 -0.0533 158 LEU A N 1208 C CA . LEU A 158 ? 0.7416 0.5754 0.6859 0.0681 -0.0537 -0.0579 158 LEU A CA 1209 C C . LEU A 158 ? 0.7857 0.6333 0.7429 0.0771 -0.0507 -0.0728 158 LEU A C 1210 O O . LEU A 158 ? 0.8119 0.6429 0.7641 0.0750 -0.0495 -0.0811 158 LEU A O 1211 C CB . LEU A 158 ? 0.7643 0.5568 0.6906 0.0619 -0.0573 -0.0540 158 LEU A CB 1212 C CG . LEU A 158 ? 0.7822 0.5562 0.6927 0.0545 -0.0607 -0.0389 158 LEU A CG 1213 C CD1 . LEU A 158 ? 0.8108 0.5487 0.7030 0.0415 -0.0607 -0.0352 158 LEU A CD1 1214 C CD2 . LEU A 158 ? 0.7905 0.5546 0.6999 0.0702 -0.0705 -0.0333 158 LEU A CD2 1215 N N . HIS A 159 ? 0.8326 0.7109 0.8058 0.0863 -0.0492 -0.0766 159 HIS A N 1216 C CA . HIS A 159 ? 0.8729 0.7732 0.8590 0.0926 -0.0438 -0.0902 159 HIS A CA 1217 C C . HIS A 159 ? 0.9021 0.7800 0.8872 0.1040 -0.0468 -0.1016 159 HIS A C 1218 O O . HIS A 159 ? 0.9078 0.7591 0.8887 0.1138 -0.0550 -0.0990 159 HIS A O 1219 C CB . HIS A 159 ? 0.8875 0.8213 0.8911 0.1012 -0.0427 -0.0911 159 HIS A CB 1220 C CG . HIS A 159 ? 0.9283 0.8894 0.9440 0.1046 -0.0350 -0.1033 159 HIS A CG 1221 N ND1 . HIS A 159 ? 0.9586 0.9273 0.9870 0.1201 -0.0356 -0.1145 159 HIS A ND1 1222 C CD2 . HIS A 159 ? 0.9292 0.9123 0.9453 0.0948 -0.0265 -0.1061 159 HIS A CD2 1223 C CE1 . HIS A 159 ? 0.9459 0.9407 0.9814 0.1185 -0.0266 -0.1238 159 HIS A CE1 1224 N NE2 . HIS A 159 ? 0.9573 0.9600 0.9844 0.1031 -0.0215 -0.1183 159 HIS A NE2 1225 N N . GLY A 160 ? 0.9219 0.8087 0.9092 0.1030 -0.0404 -0.1143 160 GLY A N 1226 C CA . GLY A 160 ? 0.9521 0.8172 0.9374 0.1134 -0.0422 -0.1274 160 GLY A CA 1227 C C . GLY A 160 ? 0.9605 0.7879 0.9275 0.1030 -0.0445 -0.1277 160 GLY A C 1228 O O . GLY A 160 ? 0.9689 0.7754 0.9318 0.1092 -0.0454 -0.1397 160 GLY A O 1229 N N . SER A 161 ? 0.9611 0.7798 0.9174 0.0870 -0.0450 -0.1152 161 SER A N 1230 C CA . SER A 161 ? 1.0114 0.7993 0.9515 0.0731 -0.0459 -0.1147 161 SER A CA 1231 C C . SER A 161 ? 0.9948 0.8066 0.9344 0.0562 -0.0388 -0.1159 161 SER A C 1232 O O . SER A 161 ? 0.9639 0.8091 0.9119 0.0535 -0.0346 -0.1111 161 SER A O 1233 C CB . SER A 161 ? 1.0626 0.8231 0.9906 0.0667 -0.0516 -0.0992 161 SER A CB 1234 O OG . SER A 161 ? 1.1517 0.8836 1.0647 0.0510 -0.0516 -0.0986 161 SER A OG 1235 N N . GLN A 162 ? 1.0090 0.8031 0.9385 0.0449 -0.0382 -0.1226 162 GLN A N 1236 C CA . GLN A 162 ? 0.9831 0.7998 0.9122 0.0294 -0.0329 -0.1253 162 GLN A CA 1237 C C . GLN A 162 ? 0.9227 0.7323 0.8444 0.0106 -0.0331 -0.1141 162 GLN A C 1238 O O . GLN A 162 ? 0.8522 0.6844 0.7758 -0.0019 -0.0295 -0.1140 162 GLN A O 1239 C CB . GLN A 162 ? 1.0457 0.8553 0.9701 0.0285 -0.0317 -0.1424 162 GLN A CB 1240 C CG . GLN A 162 ? 1.0770 0.9045 1.0098 0.0452 -0.0286 -0.1549 162 GLN A CG 1241 C CD . GLN A 162 ? 1.0657 0.9363 1.0102 0.0476 -0.0233 -0.1499 162 GLN A CD 1242 O OE1 . GLN A 162 ? 1.0067 0.8977 0.9512 0.0353 -0.0209 -0.1428 162 GLN A OE1 1243 N NE2 . GLN A 162 ? 1.0774 0.9619 1.0326 0.0637 -0.0217 -0.1537 162 GLN A NE2 1244 N N . GLU A 163 ? 0.9105 0.6899 0.8240 0.0092 -0.0373 -0.1046 163 GLU A N 1245 C CA . GLU A 163 ? 0.9014 0.6733 0.8074 -0.0084 -0.0366 -0.0933 163 GLU A CA 1246 C C . GLU A 163 ? 0.8517 0.6511 0.7643 -0.0091 -0.0338 -0.0807 163 GLU A C 1247 O O . GLU A 163 ? 0.8405 0.6531 0.7529 -0.0235 -0.0303 -0.0746 163 GLU A O 1248 C CB . GLU A 163 ? 0.9582 0.6835 0.8494 -0.0103 -0.0418 -0.0877 163 GLU A CB 1249 C CG . GLU A 163 ? 0.9931 0.6847 0.8760 -0.0095 -0.0452 -0.1002 163 GLU A CG 1250 C CD . GLU A 163 ? 0.9962 0.6952 0.8781 -0.0269 -0.0418 -0.1098 163 GLU A CD 1251 O OE1 . GLU A 163 ? 0.9424 0.6618 0.8266 -0.0435 -0.0380 -0.1034 163 GLU A OE1 1252 O OE2 . GLU A 163 ? 1.0155 0.7010 0.8946 -0.0236 -0.0433 -0.1246 163 GLU A OE2 1253 N N . ALA A 164 ? 0.8134 0.6217 0.7323 0.0065 -0.0356 -0.0777 164 ALA A N 1254 C CA . ALA A 164 ? 0.7694 0.6034 0.6945 0.0071 -0.0334 -0.0676 164 ALA A CA 1255 C C . ALA A 164 ? 0.7473 0.6060 0.6854 0.0225 -0.0330 -0.0720 164 ALA A C 1256 O O . ALA A 164 ? 0.7651 0.6223 0.7058 0.0332 -0.0366 -0.0670 164 ALA A O 1257 C CB . ALA A 164 ? 0.7762 0.5885 0.6910 0.0062 -0.0369 -0.0546 164 ALA A CB 1258 N N . PRO A 165 ? 0.7053 0.5881 0.6513 0.0225 -0.0287 -0.0812 165 PRO A N 1259 C CA . PRO A 165 ? 0.6774 0.5839 0.6351 0.0350 -0.0271 -0.0861 165 PRO A CA 1260 C C . PRO A 165 ? 0.6437 0.5734 0.6086 0.0365 -0.0257 -0.0769 165 PRO A C 1261 O O . PRO A 165 ? 0.6234 0.5680 0.5980 0.0470 -0.0256 -0.0791 165 PRO A O 1262 C CB . PRO A 165 ? 0.6764 0.6015 0.6362 0.0304 -0.0222 -0.0963 165 PRO A CB 1263 C CG . PRO A 165 ? 0.6740 0.5979 0.6271 0.0144 -0.0211 -0.0924 165 PRO A CG 1264 C CD . PRO A 165 ? 0.7014 0.5931 0.6453 0.0095 -0.0252 -0.0865 165 PRO A CD 1265 N N . GLY A 166 ? 0.6456 0.5794 0.6065 0.0258 -0.0243 -0.0675 166 GLY A N 1266 C CA . GLY A 166 ? 0.6146 0.5716 0.5816 0.0259 -0.0221 -0.0605 166 GLY A CA 1267 C C . GLY A 166 ? 0.5755 0.5587 0.5476 0.0210 -0.0168 -0.0636 166 GLY A C 1268 O O . GLY A 166 ? 0.5752 0.5625 0.5474 0.0202 -0.0151 -0.0722 166 GLY A O 1269 N N . ASN A 167 ? 0.5422 0.5413 0.5168 0.0180 -0.0148 -0.0564 167 ASN A N 1270 C CA . ASN A 167 ? 0.5094 0.5316 0.4876 0.0143 -0.0108 -0.0570 167 ASN A CA 1271 C C . ASN A 167 ? 0.5084 0.5343 0.4830 0.0047 -0.0096 -0.0588 167 ASN A C 1272 O O . ASN A 167 ? 0.4870 0.5313 0.4635 0.0027 -0.0076 -0.0594 167 ASN A O 1273 C CB . ASN A 167 ? 0.5008 0.5367 0.4844 0.0210 -0.0088 -0.0638 167 ASN A CB 1274 C CG . ASN A 167 ? 0.4867 0.5288 0.4774 0.0286 -0.0092 -0.0612 167 ASN A CG 1275 O OD1 . ASN A 167 ? 0.4677 0.5075 0.4585 0.0282 -0.0109 -0.0536 167 ASN A OD1 1276 N ND2 . ASN A 167 ? 0.4854 0.5372 0.4823 0.0351 -0.0074 -0.0680 167 ASN A ND2 1277 N N . VAL A 168 ? 0.5414 0.5505 0.5106 -0.0019 -0.0112 -0.0592 168 VAL A N 1278 C CA . VAL A 168 ? 0.5566 0.5709 0.5242 -0.0119 -0.0106 -0.0630 168 VAL A CA 1279 C C . VAL A 168 ? 0.5369 0.5719 0.5086 -0.0170 -0.0086 -0.0570 168 VAL A C 1280 O O . VAL A 168 ? 0.5451 0.5949 0.5185 -0.0221 -0.0087 -0.0602 168 VAL A O 1281 C CB . VAL A 168 ? 0.5765 0.5670 0.5374 -0.0199 -0.0125 -0.0650 168 VAL A CB 1282 C CG1 . VAL A 168 ? 0.5902 0.5581 0.5470 -0.0122 -0.0151 -0.0711 168 VAL A CG1 1283 C CG2 . VAL A 168 ? 0.5875 0.5691 0.5455 -0.0258 -0.0118 -0.0554 168 VAL A CG2 1284 N N . GLY A 169 ? 0.5249 0.5614 0.4981 -0.0146 -0.0075 -0.0489 169 GLY A N 1285 C CA . GLY A 169 ? 0.5056 0.5609 0.4832 -0.0162 -0.0055 -0.0437 169 GLY A CA 1286 C C . GLY A 169 ? 0.4796 0.5530 0.4606 -0.0113 -0.0054 -0.0452 169 GLY A C 1287 O O . GLY A 169 ? 0.4606 0.5502 0.4446 -0.0136 -0.0053 -0.0442 169 GLY A O 1288 N N . LEU A 170 ? 0.4707 0.5419 0.4511 -0.0043 -0.0054 -0.0473 170 LEU A N 1289 C CA . LEU A 170 ? 0.4570 0.5434 0.4382 -0.0009 -0.0046 -0.0484 170 LEU A CA 1290 C C . LEU A 170 ? 0.4608 0.5537 0.4388 -0.0047 -0.0056 -0.0555 170 LEU A C 1291 O O . LEU A 170 ? 0.4721 0.5797 0.4487 -0.0048 -0.0058 -0.0548 170 LEU A O 1292 C CB . LEU A 170 ? 0.4536 0.5379 0.4359 0.0060 -0.0033 -0.0494 170 LEU A CB 1293 C CG . LEU A 170 ? 0.4465 0.5294 0.4319 0.0094 -0.0029 -0.0426 170 LEU A CG 1294 C CD1 . LEU A 170 ? 0.4530 0.5352 0.4418 0.0153 -0.0024 -0.0452 170 LEU A CD1 1295 C CD2 . LEU A 170 ? 0.4426 0.5373 0.4281 0.0088 -0.0019 -0.0368 170 LEU A CD2 1296 N N . LEU A 171 ? 0.4590 0.5393 0.4344 -0.0076 -0.0067 -0.0624 171 LEU A N 1297 C CA . LEU A 171 ? 0.4651 0.5499 0.4363 -0.0126 -0.0083 -0.0705 171 LEU A CA 1298 C C . LEU A 171 ? 0.4507 0.5471 0.4242 -0.0207 -0.0105 -0.0685 171 LEU A C 1299 O O . LEU A 171 ? 0.4527 0.5623 0.4237 -0.0234 -0.0127 -0.0725 171 LEU A O 1300 C CB . LEU A 171 ? 0.4759 0.5410 0.4433 -0.0137 -0.0092 -0.0793 171 LEU A CB 1301 C CG . LEU A 171 ? 0.4716 0.5302 0.4386 -0.0039 -0.0072 -0.0835 171 LEU A CG 1302 C CD1 . LEU A 171 ? 0.4892 0.5243 0.4529 -0.0028 -0.0088 -0.0914 171 LEU A CD1 1303 C CD2 . LEU A 171 ? 0.4583 0.5341 0.4225 -0.0008 -0.0048 -0.0883 171 LEU A CD2 1304 N N . ASP A 172 ? 0.4361 0.5293 0.4142 -0.0244 -0.0100 -0.0627 172 ASP A N 1305 C CA . ASP A 172 ? 0.4352 0.5444 0.4188 -0.0308 -0.0113 -0.0605 172 ASP A CA 1306 C C . ASP A 172 ? 0.4270 0.5565 0.4127 -0.0250 -0.0123 -0.0564 172 ASP A C 1307 O O . ASP A 172 ? 0.4523 0.5983 0.4395 -0.0278 -0.0157 -0.0585 172 ASP A O 1308 C CB . ASP A 172 ? 0.4357 0.5404 0.4238 -0.0343 -0.0088 -0.0542 172 ASP A CB 1309 C CG . ASP A 172 ? 0.4652 0.5482 0.4491 -0.0419 -0.0082 -0.0565 172 ASP A CG 1310 O OD1 . ASP A 172 ? 0.4678 0.5407 0.4473 -0.0459 -0.0103 -0.0641 172 ASP A OD1 1311 O OD2 . ASP A 172 ? 0.4876 0.5619 0.4712 -0.0440 -0.0056 -0.0507 172 ASP A OD2 1312 N N . GLN A 173 ? 0.4288 0.5560 0.4140 -0.0171 -0.0101 -0.0505 173 GLN A N 1313 C CA . GLN A 173 ? 0.4294 0.5704 0.4149 -0.0114 -0.0110 -0.0453 173 GLN A CA 1314 C C . GLN A 173 ? 0.4444 0.5939 0.4230 -0.0110 -0.0135 -0.0493 173 GLN A C 1315 O O . GLN A 173 ? 0.4577 0.6219 0.4360 -0.0104 -0.0170 -0.0474 173 GLN A O 1316 C CB . GLN A 173 ? 0.4370 0.5700 0.4217 -0.0046 -0.0080 -0.0395 173 GLN A CB 1317 C CG . GLN A 173 ? 0.4311 0.5575 0.4204 -0.0042 -0.0060 -0.0348 173 GLN A CG 1318 C CD . GLN A 173 ? 0.4375 0.5567 0.4255 0.0018 -0.0041 -0.0300 173 GLN A CD 1319 O OE1 . GLN A 173 ? 0.4135 0.5353 0.3985 0.0053 -0.0040 -0.0287 173 GLN A OE1 1320 N NE2 . GLN A 173 ? 0.4377 0.5478 0.4268 0.0020 -0.0025 -0.0274 173 GLN A NE2 1321 N N . ARG A 174 ? 0.4612 0.6016 0.4337 -0.0107 -0.0118 -0.0552 174 ARG A N 1322 C CA . ARG A 174 ? 0.4657 0.6134 0.4290 -0.0105 -0.0128 -0.0600 174 ARG A CA 1323 C C . ARG A 174 ? 0.4982 0.6554 0.4591 -0.0168 -0.0177 -0.0662 174 ARG A C 1324 O O . ARG A 174 ? 0.5005 0.6703 0.4541 -0.0164 -0.0209 -0.0663 174 ARG A O 1325 C CB . ARG A 174 ? 0.4542 0.5908 0.4134 -0.0085 -0.0090 -0.0670 174 ARG A CB 1326 C CG . ARG A 174 ? 0.4564 0.6006 0.4047 -0.0082 -0.0083 -0.0732 174 ARG A CG 1327 C CD . ARG A 174 ? 0.4624 0.5962 0.4089 -0.0059 -0.0044 -0.0828 174 ARG A CD 1328 N NE . ARG A 174 ? 0.4586 0.5915 0.4089 0.0002 0.0007 -0.0791 174 ARG A NE 1329 C CZ . ARG A 174 ? 0.4560 0.5811 0.4097 0.0047 0.0041 -0.0856 174 ARG A CZ 1330 N NH1 . ARG A 174 ? 0.4738 0.5874 0.4262 0.0047 0.0031 -0.0959 174 ARG A NH1 1331 N NH2 . ARG A 174 ? 0.4548 0.5834 0.4138 0.0095 0.0081 -0.0819 174 ARG A NH2 1332 N N . MET A 175 ? 0.5239 0.6743 0.4897 -0.0234 -0.0188 -0.0713 175 MET A N 1333 C CA . MET A 175 ? 0.5430 0.7027 0.5082 -0.0315 -0.0239 -0.0780 175 MET A CA 1334 C C . MET A 175 ? 0.5294 0.7106 0.5013 -0.0316 -0.0284 -0.0720 175 MET A C 1335 O O . MET A 175 ? 0.5532 0.7493 0.5221 -0.0345 -0.0341 -0.0756 175 MET A O 1336 C CB . MET A 175 ? 0.5641 0.7101 0.5336 -0.0402 -0.0236 -0.0835 175 MET A CB 1337 C CG . MET A 175 ? 0.5965 0.7511 0.5652 -0.0505 -0.0290 -0.0921 175 MET A CG 1338 S SD . MET A 175 ? 0.6790 0.8091 0.6467 -0.0616 -0.0283 -0.1011 175 MET A SD 1339 C CE . MET A 175 ? 0.6621 0.7705 0.6167 -0.0539 -0.0256 -0.1092 175 MET A CE 1340 N N . ALA A 176 ? 0.5144 0.6975 0.4951 -0.0277 -0.0263 -0.0634 176 ALA A N 1341 C CA . ALA A 176 ? 0.5088 0.7121 0.4969 -0.0249 -0.0303 -0.0579 176 ALA A CA 1342 C C . ALA A 176 ? 0.5084 0.7194 0.4869 -0.0175 -0.0337 -0.0538 176 ALA A C 1343 O O . ALA A 176 ? 0.5170 0.7458 0.4966 -0.0163 -0.0402 -0.0526 176 ALA A O 1344 C CB . ALA A 176 ? 0.5117 0.7133 0.5096 -0.0210 -0.0263 -0.0506 176 ALA A CB 1345 N N . LEU A 177 ? 0.5048 0.7028 0.4736 -0.0128 -0.0294 -0.0513 177 LEU A N 1346 C CA . LEU A 177 ? 0.4987 0.7011 0.4554 -0.0075 -0.0313 -0.0466 177 LEU A CA 1347 C C . LEU A 177 ? 0.5073 0.7170 0.4521 -0.0117 -0.0353 -0.0540 177 LEU A C 1348 O O . LEU A 177 ? 0.5205 0.7404 0.4558 -0.0091 -0.0403 -0.0503 177 LEU A O 1349 C CB . LEU A 177 ? 0.4982 0.6866 0.4492 -0.0034 -0.0246 -0.0425 177 LEU A CB 1350 C CG . LEU A 177 ? 0.4953 0.6754 0.4551 0.0010 -0.0211 -0.0352 177 LEU A CG 1351 C CD1 . LEU A 177 ? 0.4923 0.6604 0.4475 0.0030 -0.0150 -0.0335 177 LEU A CD1 1352 C CD2 . LEU A 177 ? 0.4947 0.6823 0.4566 0.0068 -0.0252 -0.0265 177 LEU A CD2 1353 N N . GLN A 178 ? 0.5191 0.7216 0.4626 -0.0179 -0.0332 -0.0644 178 GLN A N 1354 C CA . GLN A 178 ? 0.5371 0.7457 0.4693 -0.0231 -0.0373 -0.0740 178 GLN A CA 1355 C C . GLN A 178 ? 0.5261 0.7538 0.4627 -0.0267 -0.0466 -0.0745 178 GLN A C 1356 O O . GLN A 178 ? 0.5575 0.7971 0.4825 -0.0265 -0.0527 -0.0755 178 GLN A O 1357 C CB . GLN A 178 ? 0.5476 0.7421 0.4801 -0.0292 -0.0341 -0.0860 178 GLN A CB 1358 C CG . GLN A 178 ? 0.5704 0.7667 0.4885 -0.0337 -0.0366 -0.0978 178 GLN A CG 1359 C CD . GLN A 178 ? 0.5874 0.7856 0.4893 -0.0283 -0.0330 -0.0967 178 GLN A CD 1360 O OE1 . GLN A 178 ? 0.5872 0.7989 0.4773 -0.0280 -0.0377 -0.0942 178 GLN A OE1 1361 N NE2 . GLN A 178 ? 0.5814 0.7669 0.4827 -0.0241 -0.0246 -0.0982 178 GLN A NE2 1362 N N . TRP A 179 ? 0.4965 0.7283 0.4498 -0.0300 -0.0477 -0.0739 179 TRP A N 1363 C CA . TRP A 179 ? 0.4991 0.7525 0.4614 -0.0340 -0.0561 -0.0755 179 TRP A CA 1364 C C . TRP A 179 ? 0.4897 0.7591 0.4506 -0.0247 -0.0622 -0.0658 179 TRP A C 1365 O O . TRP A 179 ? 0.5250 0.8125 0.4827 -0.0255 -0.0714 -0.0677 179 TRP A O 1366 C CB . TRP A 179 ? 0.4886 0.7439 0.4699 -0.0395 -0.0538 -0.0758 179 TRP A CB 1367 C CG . TRP A 179 ? 0.5072 0.7850 0.4992 -0.0476 -0.0613 -0.0813 179 TRP A CG 1368 C CD1 . TRP A 179 ? 0.5213 0.7991 0.5140 -0.0606 -0.0636 -0.0924 179 TRP A CD1 1369 C CD2 . TRP A 179 ? 0.5121 0.8170 0.5167 -0.0433 -0.0681 -0.0766 179 TRP A CD2 1370 N NE1 . TRP A 179 ? 0.5323 0.8376 0.5380 -0.0661 -0.0714 -0.0949 179 TRP A NE1 1371 C CE2 . TRP A 179 ? 0.5186 0.8422 0.5327 -0.0547 -0.0743 -0.0854 179 TRP A CE2 1372 C CE3 . TRP A 179 ? 0.5036 0.8182 0.5127 -0.0305 -0.0698 -0.0663 179 TRP A CE3 1373 C CZ2 . TRP A 179 ? 0.5185 0.8737 0.5483 -0.0533 -0.0822 -0.0842 179 TRP A CZ2 1374 C CZ3 . TRP A 179 ? 0.4960 0.8392 0.5196 -0.0276 -0.0778 -0.0651 179 TRP A CZ3 1375 C CH2 . TRP A 179 ? 0.5024 0.8673 0.5371 -0.0387 -0.0839 -0.0740 179 TRP A CH2 1376 N N . VAL A 180 ? 0.4708 0.7322 0.4330 -0.0158 -0.0577 -0.0557 180 VAL A N 1377 C CA . VAL A 180 ? 0.4741 0.7442 0.4326 -0.0057 -0.0630 -0.0454 180 VAL A CA 1378 C C . VAL A 180 ? 0.4888 0.7586 0.4250 -0.0045 -0.0669 -0.0445 180 VAL A C 1379 O O . VAL A 180 ? 0.5040 0.7881 0.4348 -0.0008 -0.0763 -0.0410 180 VAL A O 1380 C CB . VAL A 180 ? 0.4626 0.7184 0.4244 0.0024 -0.0563 -0.0358 180 VAL A CB 1381 C CG1 . VAL A 180 ? 0.4724 0.7290 0.4250 0.0125 -0.0610 -0.0248 180 VAL A CG1 1382 C CG2 . VAL A 180 ? 0.4503 0.7100 0.4324 0.0025 -0.0536 -0.0358 180 VAL A CG2 1383 N N . HIS A 181 ? 0.4962 0.7504 0.4193 -0.0074 -0.0596 -0.0477 181 HIS A N 1384 C CA . HIS A 181 ? 0.5206 0.7745 0.4210 -0.0074 -0.0611 -0.0474 181 HIS A CA 1385 C C . HIS A 181 ? 0.5266 0.7969 0.4212 -0.0127 -0.0707 -0.0557 181 HIS A C 1386 O O . HIS A 181 ? 0.5378 0.8176 0.4179 -0.0098 -0.0784 -0.0512 181 HIS A O 1387 C CB . HIS A 181 ? 0.5458 0.7841 0.4371 -0.0106 -0.0507 -0.0530 181 HIS A CB 1388 C CG . HIS A 181 ? 0.5950 0.8349 0.4625 -0.0122 -0.0504 -0.0553 181 HIS A CG 1389 N ND1 . HIS A 181 ? 0.6327 0.8785 0.4900 -0.0184 -0.0534 -0.0677 181 HIS A ND1 1390 C CD2 . HIS A 181 ? 0.6205 0.8563 0.4709 -0.0092 -0.0469 -0.0471 181 HIS A CD2 1391 C CE1 . HIS A 181 ? 0.6508 0.8973 0.4854 -0.0185 -0.0515 -0.0673 181 HIS A CE1 1392 N NE2 . HIS A 181 ? 0.6476 0.8883 0.4776 -0.0134 -0.0473 -0.0543 181 HIS A NE2 1393 N N . ASP A 182 ? 0.5101 0.7828 0.4154 -0.0210 -0.0708 -0.0675 182 ASP A N 1394 C CA . ASP A 182 ? 0.5279 0.8149 0.4283 -0.0285 -0.0796 -0.0778 182 ASP A CA 1395 C C . ASP A 182 ? 0.5215 0.8332 0.4337 -0.0269 -0.0919 -0.0745 182 ASP A C 1396 O O . ASP A 182 ? 0.5436 0.8706 0.4457 -0.0291 -0.1020 -0.0781 182 ASP A O 1397 C CB . ASP A 182 ? 0.5370 0.8151 0.4447 -0.0390 -0.0756 -0.0917 182 ASP A CB 1398 C CG . ASP A 182 ? 0.5484 0.8048 0.4430 -0.0397 -0.0656 -0.0980 182 ASP A CG 1399 O OD1 . ASP A 182 ? 0.5808 0.8351 0.4567 -0.0355 -0.0632 -0.0960 182 ASP A OD1 1400 O OD2 . ASP A 182 ? 0.5263 0.7683 0.4294 -0.0443 -0.0600 -0.1052 182 ASP A OD2 1401 N N . ASN A 183 ? 0.4926 0.8099 0.4264 -0.0229 -0.0912 -0.0683 183 ASN A N 1402 C CA . ASN A 183 ? 0.4905 0.8345 0.4416 -0.0228 -0.1015 -0.0686 183 ASN A CA 1403 C C . ASN A 183 ? 0.4937 0.8487 0.4533 -0.0093 -0.1065 -0.0559 183 ASN A C 1404 O O . ASN A 183 ? 0.4919 0.8727 0.4645 -0.0070 -0.1168 -0.0562 183 ASN A O 1405 C CB . ASN A 183 ? 0.4810 0.8285 0.4544 -0.0328 -0.0973 -0.0763 183 ASN A CB 1406 C CG . ASN A 183 ? 0.5039 0.8441 0.4706 -0.0469 -0.0963 -0.0901 183 ASN A CG 1407 O OD1 . ASN A 183 ? 0.5220 0.8791 0.4873 -0.0542 -0.1057 -0.0984 183 ASN A OD1 1408 N ND2 . ASN A 183 ? 0.5053 0.8196 0.4678 -0.0504 -0.0856 -0.0932 183 ASN A ND2 1409 N N . ILE A 184 ? 0.4850 0.8215 0.4378 -0.0001 -0.0998 -0.0454 184 ILE A N 1410 C CA . ILE A 184 ? 0.4822 0.8245 0.4434 0.0132 -0.1038 -0.0342 184 ILE A CA 1411 C C . ILE A 184 ? 0.5076 0.8642 0.4574 0.0215 -0.1177 -0.0280 184 ILE A C 1412 O O . ILE A 184 ? 0.5202 0.8899 0.4822 0.0325 -0.1248 -0.0217 184 ILE A O 1413 C CB . ILE A 184 ? 0.4758 0.7922 0.4308 0.0199 -0.0938 -0.0248 184 ILE A CB 1414 C CG1 . ILE A 184 ? 0.4701 0.7907 0.4413 0.0319 -0.0951 -0.0170 184 ILE A CG1 1415 C CG2 . ILE A 184 ? 0.4905 0.7915 0.4179 0.0224 -0.0940 -0.0179 184 ILE A CG2 1416 C CD1 . ILE A 184 ? 0.4482 0.7802 0.4455 0.0285 -0.0903 -0.0233 184 ILE A CD1 1417 N N . GLN A 185 ? 0.5294 0.8835 0.4554 0.0170 -0.1218 -0.0300 185 GLN A N 1418 C CA . GLN A 185 ? 0.5618 0.9293 0.4732 0.0237 -0.1363 -0.0243 185 GLN A CA 1419 C C . GLN A 185 ? 0.5539 0.9547 0.4864 0.0254 -0.1496 -0.0291 185 GLN A C 1420 O O . GLN A 185 ? 0.5535 0.9677 0.4830 0.0362 -0.1626 -0.0216 185 GLN A O 1421 C CB . GLN A 185 ? 0.5943 0.9566 0.4766 0.0156 -0.1377 -0.0290 185 GLN A CB 1422 C CG . GLN A 185 ? 0.6034 0.9803 0.4908 0.0020 -0.1402 -0.0456 185 GLN A CG 1423 C CD . GLN A 185 ? 0.6217 0.9867 0.4813 -0.0066 -0.1364 -0.0528 185 GLN A CD 1424 O OE1 . GLN A 185 ? 0.6046 0.9488 0.4586 -0.0107 -0.1229 -0.0557 185 GLN A OE1 1425 N NE2 . GLN A 185 ? 0.6477 1.0271 0.4897 -0.0089 -0.1484 -0.0563 185 GLN A NE2 1426 N N . PHE A 186 ? 0.5351 0.9493 0.4885 0.0144 -0.1466 -0.0415 186 PHE A N 1427 C CA . PHE A 186 ? 0.5512 1.0001 0.5277 0.0131 -0.1578 -0.0477 186 PHE A CA 1428 C C . PHE A 186 ? 0.5612 1.0230 0.5639 0.0257 -0.1582 -0.0411 186 PHE A C 1429 O O . PHE A 186 ? 0.5888 1.0825 0.6106 0.0304 -0.1696 -0.0429 186 PHE A O 1430 C CB . PHE A 186 ? 0.5426 0.9989 0.5312 -0.0050 -0.1535 -0.0629 186 PHE A CB 1431 C CG . PHE A 186 ? 0.5573 0.9997 0.5203 -0.0163 -0.1528 -0.0711 186 PHE A CG 1432 C CD1 . PHE A 186 ? 0.5656 1.0192 0.5086 -0.0156 -0.1659 -0.0721 186 PHE A CD1 1433 C CD2 . PHE A 186 ? 0.5580 0.9756 0.5157 -0.0264 -0.1394 -0.0778 186 PHE A CD2 1434 C CE1 . PHE A 186 ? 0.5810 1.0218 0.4989 -0.0253 -0.1645 -0.0807 186 PHE A CE1 1435 C CE2 . PHE A 186 ? 0.5723 0.9770 0.5067 -0.0351 -0.1384 -0.0864 186 PHE A CE2 1436 C CZ . PHE A 186 ? 0.5835 1.0001 0.4979 -0.0348 -0.1504 -0.0884 186 PHE A CZ 1437 N N . PHE A 187 ? 0.5579 0.9958 0.5614 0.0316 -0.1462 -0.0341 187 PHE A N 1438 C CA . PHE A 187 ? 0.5423 0.9872 0.5669 0.0446 -0.1449 -0.0282 187 PHE A CA 1439 C C . PHE A 187 ? 0.5658 0.9975 0.5755 0.0625 -0.1512 -0.0141 187 PHE A C 1440 O O . PHE A 187 ? 0.5670 0.9974 0.5900 0.0753 -0.1495 -0.0085 187 PHE A O 1441 C CB . PHE A 187 ? 0.5122 0.9382 0.5460 0.0397 -0.1283 -0.0297 187 PHE A CB 1442 C CG . PHE A 187 ? 0.4925 0.9295 0.5420 0.0230 -0.1221 -0.0419 187 PHE A CG 1443 C CD1 . PHE A 187 ? 0.4908 0.9112 0.5256 0.0087 -0.1169 -0.0486 187 PHE A CD1 1444 C CD2 . PHE A 187 ? 0.4837 0.9472 0.5624 0.0215 -0.1213 -0.0469 187 PHE A CD2 1445 C CE1 . PHE A 187 ? 0.4895 0.9159 0.5371 -0.0069 -0.1117 -0.0592 187 PHE A CE1 1446 C CE2 . PHE A 187 ? 0.4720 0.9438 0.5637 0.0044 -0.1153 -0.0572 187 PHE A CE2 1447 C CZ . PHE A 187 ? 0.4778 0.9291 0.5531 -0.0099 -0.1109 -0.0630 187 PHE A CZ 1448 N N . GLY A 188 ? 0.5752 0.9964 0.5565 0.0632 -0.1584 -0.0088 188 GLY A N 1449 C CA . GLY A 188 ? 0.5904 0.9934 0.5521 0.0779 -0.1639 0.0059 188 GLY A CA 1450 C C . GLY A 188 ? 0.5894 0.9545 0.5317 0.0762 -0.1506 0.0131 188 GLY A C 1451 O O . GLY A 188 ? 0.6228 0.9679 0.5466 0.0861 -0.1534 0.0258 188 GLY A O 1452 N N . GLY A 189 ? 0.5656 0.9202 0.5118 0.0636 -0.1367 0.0053 189 GLY A N 1453 C CA . GLY A 189 ? 0.5626 0.8849 0.4940 0.0613 -0.1239 0.0108 189 GLY A CA 1454 C C . GLY A 189 ? 0.5737 0.8828 0.4742 0.0551 -0.1238 0.0137 189 GLY A C 1455 O O . GLY A 189 ? 0.6009 0.9243 0.4930 0.0482 -0.1298 0.0070 189 GLY A O 1456 N N . ASP A 190 ? 0.5769 0.8595 0.4598 0.0571 -0.1170 0.0235 190 ASP A N 1457 C CA . ASP A 190 ? 0.5920 0.8617 0.4456 0.0498 -0.1136 0.0261 190 ASP A CA 1458 C C . ASP A 190 ? 0.5772 0.8348 0.4329 0.0390 -0.0982 0.0184 190 ASP A C 1459 O O . ASP A 190 ? 0.5826 0.8229 0.4438 0.0404 -0.0891 0.0226 190 ASP A O 1460 C CB . ASP A 190 ? 0.6096 0.8578 0.4412 0.0573 -0.1155 0.0424 190 ASP A CB 1461 C CG . ASP A 190 ? 0.6148 0.8495 0.4168 0.0483 -0.1088 0.0456 190 ASP A CG 1462 O OD1 . ASP A 190 ? 0.6121 0.8578 0.4073 0.0388 -0.1067 0.0352 190 ASP A OD1 1463 O OD2 . ASP A 190 ? 0.6271 0.8400 0.4122 0.0501 -0.1053 0.0580 190 ASP A OD2 1464 N N . PRO A 191 ? 0.5752 0.8412 0.4258 0.0287 -0.0957 0.0068 191 PRO A N 1465 C CA . PRO A 191 ? 0.5664 0.8210 0.4202 0.0203 -0.0819 -0.0010 191 PRO A CA 1466 C C . PRO A 191 ? 0.5809 0.8159 0.4163 0.0187 -0.0723 0.0064 191 PRO A C 1467 O O . PRO A 191 ? 0.5615 0.7859 0.4047 0.0153 -0.0613 0.0032 191 PRO A O 1468 C CB . PRO A 191 ? 0.5702 0.8373 0.4197 0.0111 -0.0835 -0.0151 191 PRO A CB 1469 C CG . PRO A 191 ? 0.5854 0.8658 0.4175 0.0133 -0.0963 -0.0119 191 PRO A CG 1470 C CD . PRO A 191 ? 0.5822 0.8666 0.4224 0.0248 -0.1057 0.0001 191 PRO A CD 1471 N N . LYS A 192 ? 0.6471 0.8778 0.4584 0.0210 -0.0766 0.0167 192 LYS A N 1472 C CA . LYS A 192 ? 0.6883 0.9013 0.4812 0.0183 -0.0675 0.0254 192 LYS A CA 1473 C C . LYS A 192 ? 0.6751 0.8705 0.4784 0.0232 -0.0631 0.0351 192 LYS A C 1474 O O . LYS A 192 ? 0.6731 0.8545 0.4681 0.0186 -0.0533 0.0396 192 LYS A O 1475 C CB . LYS A 192 ? 0.7471 0.9581 0.5094 0.0193 -0.0744 0.0363 192 LYS A CB 1476 C CG . LYS A 192 ? 0.7929 1.0195 0.5375 0.0140 -0.0790 0.0278 192 LYS A CG 1477 C CD . LYS A 192 ? 0.8420 1.0635 0.5517 0.0139 -0.0840 0.0401 192 LYS A CD 1478 C CE . LYS A 192 ? 0.8548 1.0717 0.5606 0.0253 -0.0984 0.0551 192 LYS A CE 1479 N NZ . LYS A 192 ? 0.8326 1.0690 0.5604 0.0326 -0.1117 0.0487 192 LYS A NZ 1480 N N . THR A 193 ? 0.6606 0.8578 0.4814 0.0321 -0.0704 0.0380 193 THR A N 1481 C CA . THR A 193 ? 0.6440 0.8233 0.4720 0.0384 -0.0682 0.0473 193 THR A CA 1482 C C . THR A 193 ? 0.6043 0.7882 0.4613 0.0413 -0.0656 0.0395 193 THR A C 1483 O O . THR A 193 ? 0.6057 0.7901 0.4748 0.0508 -0.0715 0.0430 193 THR A O 1484 C CB . THR A 193 ? 0.6485 0.8207 0.4644 0.0491 -0.0798 0.0610 193 THR A CB 1485 O OG1 . THR A 193 ? 0.6760 0.8437 0.4619 0.0452 -0.0823 0.0687 193 THR A OG1 1486 C CG2 . THR A 193 ? 0.6462 0.7953 0.4655 0.0550 -0.0772 0.0705 193 THR A CG2 1487 N N . VAL A 194 ? 0.5755 0.7623 0.4427 0.0334 -0.0567 0.0290 194 VAL A N 1488 C CA . VAL A 194 ? 0.5415 0.7312 0.4328 0.0344 -0.0534 0.0220 194 VAL A CA 1489 C C . VAL A 194 ? 0.5388 0.7102 0.4337 0.0331 -0.0441 0.0248 194 VAL A C 1490 O O . VAL A 194 ? 0.5321 0.6960 0.4184 0.0263 -0.0366 0.0241 194 VAL A O 1491 C CB . VAL A 194 ? 0.5286 0.7314 0.4287 0.0267 -0.0509 0.0086 194 VAL A CB 1492 C CG1 . VAL A 194 ? 0.5128 0.7140 0.4339 0.0259 -0.0457 0.0027 194 VAL A CG1 1493 C CG2 . VAL A 194 ? 0.5350 0.7576 0.4349 0.0272 -0.0611 0.0045 194 VAL A CG2 1494 N N . THR A 195 ? 0.5440 0.7099 0.4524 0.0395 -0.0446 0.0269 195 THR A N 1495 C CA . THR A 195 ? 0.5398 0.6886 0.4522 0.0386 -0.0372 0.0290 195 THR A CA 1496 C C . THR A 195 ? 0.5220 0.6755 0.4535 0.0375 -0.0332 0.0203 195 THR A C 1497 O O . THR A 195 ? 0.5476 0.7106 0.4913 0.0426 -0.0369 0.0179 195 THR A O 1498 C CB . THR A 195 ? 0.5406 0.6743 0.4493 0.0474 -0.0410 0.0390 195 THR A CB 1499 O OG1 . THR A 195 ? 0.5714 0.6953 0.4590 0.0468 -0.0437 0.0488 195 THR A OG1 1500 C CG2 . THR A 195 ? 0.5336 0.6507 0.4483 0.0464 -0.0343 0.0392 195 THR A CG2 1501 N N . ILE A 196 ? 0.5012 0.6486 0.4351 0.0309 -0.0257 0.0159 196 ILE A N 1502 C CA . ILE A 196 ? 0.4851 0.6332 0.4341 0.0300 -0.0223 0.0094 196 ILE A CA 1503 C C . ILE A 196 ? 0.4799 0.6131 0.4320 0.0335 -0.0195 0.0134 196 ILE A C 1504 O O . ILE A 196 ? 0.4836 0.6040 0.4276 0.0318 -0.0170 0.0182 196 ILE A O 1505 C CB . ILE A 196 ? 0.4745 0.6242 0.4258 0.0225 -0.0171 0.0014 196 ILE A CB 1506 C CG1 . ILE A 196 ? 0.4721 0.6125 0.4158 0.0187 -0.0117 0.0030 196 ILE A CG1 1507 C CG2 . ILE A 196 ? 0.4783 0.6416 0.4273 0.0191 -0.0202 -0.0046 196 ILE A CG2 1508 C CD1 . ILE A 196 ? 0.4649 0.6079 0.4120 0.0138 -0.0073 -0.0055 196 ILE A CD1 1509 N N . PHE A 197 ? 0.4675 0.6029 0.4309 0.0375 -0.0198 0.0110 197 PHE A N 1510 C CA . PHE A 197 ? 0.4603 0.5816 0.4258 0.0406 -0.0171 0.0130 197 PHE A CA 1511 C C . PHE A 197 ? 0.4540 0.5786 0.4304 0.0393 -0.0137 0.0068 197 PHE A C 1512 O O . PHE A 197 ? 0.4612 0.5999 0.4451 0.0379 -0.0144 0.0024 197 PHE A O 1513 C CB . PHE A 197 ? 0.4787 0.5931 0.4412 0.0500 -0.0213 0.0192 197 PHE A CB 1514 C CG . PHE A 197 ? 0.4695 0.5987 0.4423 0.0580 -0.0253 0.0172 197 PHE A CG 1515 C CD1 . PHE A 197 ? 0.4732 0.6227 0.4505 0.0571 -0.0294 0.0147 197 PHE A CD1 1516 C CD2 . PHE A 197 ? 0.4643 0.5880 0.4425 0.0668 -0.0253 0.0175 197 PHE A CD2 1517 C CE1 . PHE A 197 ? 0.4706 0.6373 0.4598 0.0642 -0.0333 0.0125 197 PHE A CE1 1518 C CE2 . PHE A 197 ? 0.4634 0.6039 0.4531 0.0750 -0.0285 0.0150 197 PHE A CE2 1519 C CZ . PHE A 197 ? 0.4648 0.6281 0.4611 0.0735 -0.0326 0.0127 197 PHE A CZ 1520 N N . GLY A 198 ? 0.4503 0.5617 0.4262 0.0384 -0.0102 0.0066 198 GLY A N 1521 C CA . GLY A 198 ? 0.4352 0.5470 0.4178 0.0364 -0.0068 0.0017 198 GLY A CA 1522 C C . GLY A 198 ? 0.4343 0.5308 0.4141 0.0375 -0.0046 0.0023 198 GLY A C 1523 O O . GLY A 198 ? 0.4316 0.5162 0.4051 0.0377 -0.0052 0.0060 198 GLY A O 1524 N N . GLU A 199 ? 0.4282 0.5247 0.4116 0.0370 -0.0020 -0.0014 199 GLU A N 1525 C CA . GLU A 199 ? 0.4328 0.5158 0.4126 0.0380 -0.0003 -0.0021 199 GLU A CA 1526 C C . GLU A 199 ? 0.4331 0.5139 0.4125 0.0323 0.0016 -0.0052 199 GLU A C 1527 O O . GLU A 199 ? 0.4324 0.5216 0.4152 0.0295 0.0028 -0.0072 199 GLU A O 1528 C CB . GLU A 199 ? 0.4411 0.5251 0.4229 0.0453 0.0009 -0.0034 199 GLU A CB 1529 C CG . GLU A 199 ? 0.4516 0.5201 0.4275 0.0472 0.0024 -0.0051 199 GLU A CG 1530 C CD . GLU A 199 ? 0.4495 0.5188 0.4242 0.0435 0.0059 -0.0092 199 GLU A CD 1531 O OE1 . GLU A 199 ? 0.4464 0.5274 0.4253 0.0399 0.0077 -0.0104 199 GLU A OE1 1532 O OE2 . GLU A 199 ? 0.4677 0.5244 0.4357 0.0437 0.0065 -0.0111 199 GLU A OE2 1533 N N . SER A 200 ? 0.4572 0.5260 0.4320 0.0305 0.0014 -0.0053 200 SER A N 1534 C CA . SER A 200 ? 0.4634 0.5287 0.4367 0.0263 0.0015 -0.0075 200 SER A CA 1535 C C . SER A 200 ? 0.4473 0.5190 0.4242 0.0226 0.0007 -0.0080 200 SER A C 1536 O O . SER A 200 ? 0.4706 0.5445 0.4490 0.0216 -0.0002 -0.0070 200 SER A O 1537 C CB . SER A 200 ? 0.4806 0.5464 0.4517 0.0270 0.0041 -0.0096 200 SER A CB 1538 O OG . SER A 200 ? 0.5063 0.5671 0.4734 0.0231 0.0035 -0.0105 200 SER A OG 1539 N N . ALA A 201 ? 0.4412 0.5151 0.4187 0.0203 0.0013 -0.0097 201 ALA A N 1540 C CA . ALA A 201 ? 0.4444 0.5218 0.4246 0.0175 0.0004 -0.0113 201 ALA A CA 1541 C C . ALA A 201 ? 0.4365 0.5244 0.4202 0.0176 0.0004 -0.0114 201 ALA A C 1542 O O . ALA A 201 ? 0.4291 0.5195 0.4139 0.0160 -0.0003 -0.0133 201 ALA A O 1543 C CB . ALA A 201 ? 0.4466 0.5212 0.4250 0.0144 0.0011 -0.0124 201 ALA A CB 1544 N N . GLY A 202 ? 0.4336 0.5279 0.4185 0.0200 0.0010 -0.0099 202 GLY A N 1545 C CA . GLY A 202 ? 0.4429 0.5472 0.4294 0.0209 -0.0004 -0.0092 202 GLY A CA 1546 C C . GLY A 202 ? 0.4454 0.5464 0.4280 0.0221 -0.0014 -0.0063 202 GLY A C 1547 O O . GLY A 202 ? 0.4610 0.5678 0.4420 0.0206 -0.0021 -0.0066 202 GLY A O 1548 N N . GLY A 203 ? 0.4408 0.5320 0.4207 0.0239 -0.0010 -0.0038 203 GLY A N 1549 C CA . GLY A 203 ? 0.4445 0.5307 0.4205 0.0226 -0.0011 -0.0008 203 GLY A CA 1550 C C . GLY A 203 ? 0.4155 0.5041 0.3935 0.0182 0.0001 -0.0037 203 GLY A C 1551 O O . GLY A 203 ? 0.3993 0.4920 0.3753 0.0159 0.0011 -0.0027 203 GLY A O 1552 N N . ALA A 204 ? 0.4146 0.5010 0.3960 0.0175 0.0000 -0.0072 204 ALA A N 1553 C CA . ALA A 204 ? 0.4356 0.5248 0.4206 0.0154 0.0004 -0.0107 204 ALA A CA 1554 C C . ALA A 204 ? 0.4244 0.5218 0.4100 0.0148 0.0011 -0.0139 204 ALA A C 1555 O O . ALA A 204 ? 0.4386 0.5416 0.4256 0.0137 0.0026 -0.0166 204 ALA A O 1556 C CB . ALA A 204 ? 0.4265 0.5096 0.4136 0.0161 -0.0014 -0.0131 204 ALA A CB 1557 N N . SER A 205 ? 0.4163 0.5154 0.4009 0.0152 0.0002 -0.0145 205 SER A N 1558 C CA . SER A 205 ? 0.4172 0.5232 0.4012 0.0138 0.0001 -0.0182 205 SER A CA 1559 C C . SER A 205 ? 0.4249 0.5386 0.4044 0.0134 0.0008 -0.0164 205 SER A C 1560 O O . SER A 205 ? 0.4220 0.5409 0.3999 0.0120 0.0021 -0.0203 205 SER A O 1561 C CB . SER A 205 ? 0.4220 0.5301 0.4070 0.0129 -0.0011 -0.0187 205 SER A CB 1562 O OG . SER A 205 ? 0.4095 0.5096 0.3961 0.0116 -0.0010 -0.0202 205 SER A OG 1563 N N . VAL A 206 ? 0.4283 0.5415 0.4045 0.0150 -0.0001 -0.0105 206 VAL A N 1564 C CA . VAL A 206 ? 0.4342 0.5518 0.4031 0.0145 -0.0001 -0.0068 206 VAL A CA 1565 C C . VAL A 206 ? 0.4583 0.5767 0.4252 0.0112 0.0037 -0.0077 206 VAL A C 1566 O O . VAL A 206 ? 0.5004 0.6264 0.4618 0.0092 0.0053 -0.0093 206 VAL A O 1567 C CB . VAL A 206 ? 0.4279 0.5396 0.3929 0.0178 -0.0020 0.0006 206 VAL A CB 1568 C CG1 . VAL A 206 ? 0.4252 0.5366 0.3798 0.0164 -0.0019 0.0061 206 VAL A CG1 1569 C CG2 . VAL A 206 ? 0.4241 0.5404 0.3921 0.0221 -0.0056 0.0008 206 VAL A CG2 1570 N N . GLY A 207 ? 0.4432 0.5557 0.4148 0.0104 0.0053 -0.0071 207 GLY A N 1571 C CA . GLY A 207 ? 0.4528 0.5696 0.4263 0.0069 0.0091 -0.0088 207 GLY A CA 1572 C C . GLY A 207 ? 0.4665 0.5917 0.4450 0.0075 0.0109 -0.0171 207 GLY A C 1573 O O . GLY A 207 ? 0.4747 0.6087 0.4532 0.0052 0.0150 -0.0198 207 GLY A O 1574 N N . MET A 208 ? 0.4714 0.5932 0.4538 0.0104 0.0082 -0.0213 208 MET A N 1575 C CA . MET A 208 ? 0.4814 0.6069 0.4674 0.0119 0.0090 -0.0295 208 MET A CA 1576 C C . MET A 208 ? 0.4866 0.6195 0.4651 0.0105 0.0104 -0.0330 208 MET A C 1577 O O . MET A 208 ? 0.4967 0.6352 0.4760 0.0112 0.0131 -0.0401 208 MET A O 1578 C CB . MET A 208 ? 0.4791 0.5950 0.4690 0.0144 0.0054 -0.0320 208 MET A CB 1579 C CG . MET A 208 ? 0.4952 0.6051 0.4914 0.0164 0.0038 -0.0307 208 MET A CG 1580 S SD . MET A 208 ? 0.5101 0.6059 0.5060 0.0181 -0.0003 -0.0308 208 MET A SD 1581 C CE . MET A 208 ? 0.5162 0.6079 0.5174 0.0208 -0.0030 -0.0294 208 MET A CE 1582 N N . HIS A 209 ? 0.4700 0.6035 0.4411 0.0092 0.0082 -0.0286 209 HIS A N 1583 C CA . HIS A 209 ? 0.4686 0.6099 0.4310 0.0076 0.0082 -0.0316 209 HIS A CA 1584 C C . HIS A 209 ? 0.4764 0.6249 0.4306 0.0052 0.0125 -0.0288 209 HIS A C 1585 O O . HIS A 209 ? 0.4802 0.6364 0.4265 0.0036 0.0146 -0.0335 209 HIS A O 1586 C CB . HIS A 209 ? 0.4736 0.6156 0.4322 0.0074 0.0031 -0.0281 209 HIS A CB 1587 C CG . HIS A 209 ? 0.4790 0.6169 0.4444 0.0075 0.0002 -0.0320 209 HIS A CG 1588 N ND1 . HIS A 209 ? 0.4853 0.6220 0.4513 0.0058 -0.0001 -0.0407 209 HIS A ND1 1589 C CD2 . HIS A 209 ? 0.4807 0.6147 0.4516 0.0083 -0.0022 -0.0284 209 HIS A CD2 1590 C CE1 . HIS A 209 ? 0.4824 0.6137 0.4537 0.0044 -0.0025 -0.0414 209 HIS A CE1 1591 N NE2 . HIS A 209 ? 0.4938 0.6249 0.4683 0.0058 -0.0034 -0.0342 209 HIS A NE2 1592 N N . ILE A 210 ? 0.4644 0.6097 0.4192 0.0040 0.0140 -0.0214 210 ILE A N 1593 C CA . ILE A 210 ? 0.4576 0.6087 0.4056 -0.0002 0.0194 -0.0183 210 ILE A CA 1594 C C . ILE A 210 ? 0.4542 0.6152 0.4093 -0.0008 0.0255 -0.0270 210 ILE A C 1595 O O . ILE A 210 ? 0.4573 0.6282 0.4047 -0.0038 0.0308 -0.0294 210 ILE A O 1596 C CB . ILE A 210 ? 0.4552 0.5981 0.4031 -0.0025 0.0196 -0.0088 210 ILE A CB 1597 C CG1 . ILE A 210 ? 0.4642 0.5989 0.4016 -0.0010 0.0144 -0.0002 210 ILE A CG1 1598 C CG2 . ILE A 210 ? 0.4769 0.6260 0.4211 -0.0090 0.0265 -0.0066 210 ILE A CG2 1599 C CD1 . ILE A 210 ? 0.4706 0.5921 0.4099 -0.0005 0.0125 0.0072 210 ILE A CD1 1600 N N . LEU A 211 ? 0.4521 0.6107 0.4211 0.0025 0.0246 -0.0318 211 LEU A N 1601 C CA . LEU A 211 ? 0.4540 0.6227 0.4329 0.0041 0.0293 -0.0403 211 LEU A CA 1602 C C . LEU A 211 ? 0.4698 0.6420 0.4465 0.0077 0.0301 -0.0508 211 LEU A C 1603 O O . LEU A 211 ? 0.4899 0.6744 0.4654 0.0073 0.0362 -0.0574 211 LEU A O 1604 C CB . LEU A 211 ? 0.4560 0.6201 0.4496 0.0076 0.0263 -0.0414 211 LEU A CB 1605 C CG . LEU A 211 ? 0.4579 0.6198 0.4556 0.0036 0.0260 -0.0338 211 LEU A CG 1606 C CD1 . LEU A 211 ? 0.4558 0.6112 0.4648 0.0077 0.0209 -0.0351 211 LEU A CD1 1607 C CD2 . LEU A 211 ? 0.4656 0.6420 0.4666 -0.0022 0.0329 -0.0337 211 LEU A CD2 1608 N N . SER A 212 ? 0.4741 0.6354 0.4496 0.0105 0.0242 -0.0527 212 SER A N 1609 C CA . SER A 212 ? 0.4881 0.6480 0.4617 0.0134 0.0238 -0.0633 212 SER A CA 1610 C C . SER A 212 ? 0.5027 0.6712 0.4622 0.0102 0.0266 -0.0669 212 SER A C 1611 O O . SER A 212 ? 0.5207 0.6881 0.4699 0.0067 0.0232 -0.0611 212 SER A O 1612 C CB . SER A 212 ? 0.4874 0.6331 0.4617 0.0144 0.0170 -0.0631 212 SER A CB 1613 O OG . SER A 212 ? 0.4820 0.6225 0.4552 0.0166 0.0162 -0.0736 212 SER A OG 1614 N N . PRO A 213 ? 0.4955 0.6732 0.4543 0.0121 0.0324 -0.0769 213 PRO A N 1615 C CA . PRO A 213 ? 0.5053 0.6911 0.4486 0.0091 0.0355 -0.0821 213 PRO A CA 1616 C C . PRO A 213 ? 0.5137 0.6915 0.4470 0.0074 0.0287 -0.0845 213 PRO A C 1617 O O . PRO A 213 ? 0.5598 0.7434 0.4782 0.0030 0.0277 -0.0817 213 PRO A O 1618 C CB . PRO A 213 ? 0.5099 0.7030 0.4585 0.0141 0.0419 -0.0958 213 PRO A CB 1619 C CG . PRO A 213 ? 0.4923 0.6902 0.4581 0.0173 0.0448 -0.0934 213 PRO A CG 1620 C CD . PRO A 213 ? 0.4857 0.6692 0.4583 0.0174 0.0369 -0.0839 213 PRO A CD 1621 N N . GLY A 214 ? 0.4954 0.6603 0.4361 0.0100 0.0237 -0.0894 214 GLY A N 1622 C CA . GLY A 214 ? 0.4825 0.6408 0.4160 0.0067 0.0172 -0.0923 214 GLY A CA 1623 C C . GLY A 214 ? 0.4790 0.6394 0.4089 0.0024 0.0116 -0.0810 214 GLY A C 1624 O O . GLY A 214 ? 0.4902 0.6523 0.4127 -0.0012 0.0066 -0.0831 214 GLY A O 1625 N N . SER A 215 ? 0.4706 0.6312 0.4066 0.0033 0.0120 -0.0697 215 SER A N 1626 C CA . SER A 215 ? 0.4653 0.6267 0.3998 0.0015 0.0068 -0.0591 215 SER A CA 1627 C C . SER A 215 ? 0.4664 0.6360 0.3894 0.0002 0.0078 -0.0505 215 SER A C 1628 O O . SER A 215 ? 0.4698 0.6417 0.3876 -0.0004 0.0023 -0.0438 215 SER A O 1629 C CB . SER A 215 ? 0.4568 0.6095 0.4038 0.0038 0.0058 -0.0524 215 SER A CB 1630 O OG . SER A 215 ? 0.4480 0.5909 0.4035 0.0047 0.0046 -0.0584 215 SER A OG 1631 N N . ARG A 216 ? 0.4733 0.6474 0.3922 -0.0003 0.0147 -0.0505 216 ARG A N 1632 C CA . ARG A 216 ? 0.4781 0.6567 0.3850 -0.0029 0.0168 -0.0407 216 ARG A CA 1633 C C . ARG A 216 ? 0.4794 0.6629 0.3689 -0.0048 0.0119 -0.0377 216 ARG A C 1634 O O . ARG A 216 ? 0.4807 0.6622 0.3621 -0.0051 0.0090 -0.0263 216 ARG A O 1635 C CB . ARG A 216 ? 0.4814 0.6676 0.3851 -0.0052 0.0264 -0.0438 216 ARG A CB 1636 C CG . ARG A 216 ? 0.4703 0.6548 0.3908 -0.0037 0.0309 -0.0443 216 ARG A CG 1637 C CD . ARG A 216 ? 0.4871 0.6836 0.4064 -0.0068 0.0407 -0.0471 216 ARG A CD 1638 N NE . ARG A 216 ? 0.4932 0.6916 0.4319 -0.0037 0.0437 -0.0519 216 ARG A NE 1639 C CZ . ARG A 216 ? 0.5001 0.7121 0.4458 -0.0039 0.0519 -0.0588 216 ARG A CZ 1640 N NH1 . ARG A 216 ? 0.5138 0.7388 0.4474 -0.0079 0.0597 -0.0619 216 ARG A NH1 1641 N NH2 . ARG A 216 ? 0.4931 0.7070 0.4579 0.0002 0.0523 -0.0627 216 ARG A NH2 1642 N N . ASP A 217 ? 0.4877 0.6767 0.3706 -0.0058 0.0102 -0.0479 217 ASP A N 1643 C CA . ASP A 217 ? 0.5222 0.7180 0.3862 -0.0080 0.0053 -0.0457 217 ASP A CA 1644 C C . ASP A 217 ? 0.5342 0.7301 0.4006 -0.0063 -0.0056 -0.0403 217 ASP A C 1645 O O . ASP A 217 ? 0.5901 0.7922 0.4418 -0.0069 -0.0116 -0.0362 217 ASP A O 1646 C CB . ASP A 217 ? 0.5305 0.7330 0.3844 -0.0103 0.0073 -0.0597 217 ASP A CB 1647 C CG . ASP A 217 ? 0.5300 0.7369 0.3794 -0.0113 0.0187 -0.0653 217 ASP A CG 1648 O OD1 . ASP A 217 ? 0.5493 0.7550 0.4056 -0.0111 0.0248 -0.0586 217 ASP A OD1 1649 O OD2 . ASP A 217 ? 0.5319 0.7443 0.3714 -0.0124 0.0217 -0.0775 217 ASP A OD2 1650 N N . LEU A 218 ? 0.5176 0.7081 0.4023 -0.0040 -0.0083 -0.0401 218 LEU A N 1651 C CA . LEU A 218 ? 0.4926 0.6868 0.3834 -0.0027 -0.0176 -0.0379 218 LEU A CA 1652 C C . LEU A 218 ? 0.4949 0.6866 0.3890 0.0021 -0.0213 -0.0246 218 LEU A C 1653 O O . LEU A 218 ? 0.4953 0.6917 0.3988 0.0045 -0.0280 -0.0229 218 LEU A O 1654 C CB . LEU A 218 ? 0.4784 0.6688 0.3860 -0.0040 -0.0177 -0.0461 218 LEU A CB 1655 C CG . LEU A 218 ? 0.4839 0.6720 0.3901 -0.0078 -0.0150 -0.0599 218 LEU A CG 1656 C CD1 . LEU A 218 ? 0.4751 0.6532 0.3969 -0.0085 -0.0140 -0.0646 218 LEU A CD1 1657 C CD2 . LEU A 218 ? 0.5054 0.7034 0.4015 -0.0119 -0.0215 -0.0669 218 LEU A CD2 1658 N N . PHE A 219 ? 0.4777 0.6622 0.3647 0.0033 -0.0170 -0.0157 219 PHE A N 1659 C CA . PHE A 219 ? 0.4658 0.6443 0.3532 0.0083 -0.0209 -0.0034 219 PHE A CA 1660 C C . PHE A 219 ? 0.4825 0.6535 0.3534 0.0068 -0.0172 0.0062 219 PHE A C 1661 O O . PHE A 219 ? 0.4829 0.6544 0.3471 0.0017 -0.0095 0.0030 219 PHE A O 1662 C CB . PHE A 219 ? 0.4367 0.6072 0.3426 0.0111 -0.0190 -0.0027 219 PHE A CB 1663 C CG . PHE A 219 ? 0.4219 0.5839 0.3323 0.0083 -0.0102 -0.0045 219 PHE A CG 1664 C CD1 . PHE A 219 ? 0.4148 0.5788 0.3323 0.0054 -0.0059 -0.0149 219 PHE A CD1 1665 C CD2 . PHE A 219 ? 0.4184 0.5698 0.3265 0.0087 -0.0071 0.0039 219 PHE A CD2 1666 C CE1 . PHE A 219 ? 0.4114 0.5701 0.3348 0.0041 0.0009 -0.0168 219 PHE A CE1 1667 C CE2 . PHE A 219 ? 0.4219 0.5686 0.3359 0.0056 0.0000 0.0017 219 PHE A CE2 1668 C CZ . PHE A 219 ? 0.4122 0.5640 0.3345 0.0039 0.0039 -0.0087 219 PHE A CZ 1669 N N . ARG A 220 ? 0.4971 0.6609 0.3619 0.0114 -0.0225 0.0179 220 ARG A N 1670 C CA . ARG A 220 ? 0.5292 0.6829 0.3753 0.0092 -0.0201 0.0289 220 ARG A CA 1671 C C . ARG A 220 ? 0.5304 0.6687 0.3836 0.0084 -0.0145 0.0345 220 ARG A C 1672 O O . ARG A 220 ? 0.5375 0.6707 0.3828 0.0016 -0.0067 0.0373 220 ARG A O 1673 C CB . ARG A 220 ? 0.5600 0.7118 0.3923 0.0151 -0.0307 0.0390 220 ARG A CB 1674 C CG . ARG A 220 ? 0.5973 0.7345 0.4068 0.0131 -0.0299 0.0528 220 ARG A CG 1675 C CD . ARG A 220 ? 0.6247 0.7688 0.4123 0.0050 -0.0255 0.0521 220 ARG A CD 1676 N NE . ARG A 220 ? 0.6685 0.7998 0.4295 0.0040 -0.0282 0.0671 220 ARG A NE 1677 C CZ . ARG A 220 ? 0.6961 0.8292 0.4388 0.0086 -0.0389 0.0739 220 ARG A CZ 1678 N NH1 . ARG A 220 ? 0.7069 0.8565 0.4562 0.0144 -0.0485 0.0666 220 ARG A NH1 1679 N NH2 . ARG A 220 ? 0.7330 0.8509 0.4498 0.0069 -0.0405 0.0886 220 ARG A NH2 1680 N N . ARG A 221 ? 0.5123 0.6442 0.3801 0.0148 -0.0183 0.0356 221 ARG A N 1681 C CA . ARG A 221 ? 0.5163 0.6320 0.3900 0.0149 -0.0147 0.0405 221 ARG A CA 1682 C C . ARG A 221 ? 0.4832 0.6002 0.3778 0.0182 -0.0142 0.0332 221 ARG A C 1683 O O . ARG A 221 ? 0.4818 0.6110 0.3861 0.0206 -0.0169 0.0258 221 ARG A O 1684 C CB . ARG A 221 ? 0.5488 0.6488 0.4130 0.0212 -0.0211 0.0525 221 ARG A CB 1685 C CG . ARG A 221 ? 0.5857 0.6830 0.4269 0.0203 -0.0250 0.0618 221 ARG A CG 1686 C CD . ARG A 221 ? 0.6140 0.6896 0.4442 0.0262 -0.0306 0.0749 221 ARG A CD 1687 N NE . ARG A 221 ? 0.6500 0.7186 0.4542 0.0212 -0.0310 0.0852 221 ARG A NE 1688 C CZ . ARG A 221 ? 0.6577 0.7330 0.4471 0.0253 -0.0391 0.0895 221 ARG A CZ 1689 N NH1 . ARG A 221 ? 0.6591 0.7496 0.4591 0.0348 -0.0481 0.0844 221 ARG A NH1 1690 N NH2 . ARG A 221 ? 0.7101 0.7772 0.4732 0.0194 -0.0383 0.0995 221 ARG A NH2 1691 N N . ALA A 222 ? 0.4847 0.5880 0.3846 0.0178 -0.0111 0.0357 222 ALA A N 1692 C CA . ALA A 222 ? 0.4622 0.5654 0.3792 0.0197 -0.0096 0.0290 222 ALA A CA 1693 C C . ALA A 222 ? 0.4741 0.5604 0.3931 0.0234 -0.0106 0.0339 222 ALA A C 1694 O O . ALA A 222 ? 0.5025 0.5744 0.4115 0.0207 -0.0095 0.0412 222 ALA A O 1695 C CB . ALA A 222 ? 0.4372 0.5454 0.3609 0.0128 -0.0028 0.0218 222 ALA A CB 1696 N N . ILE A 223 ? 0.4687 0.5561 0.3996 0.0290 -0.0123 0.0296 223 ILE A N 1697 C CA . ILE A 223 ? 0.4742 0.5464 0.4084 0.0324 -0.0121 0.0311 223 ILE A CA 1698 C C . ILE A 223 ? 0.4480 0.5235 0.3942 0.0302 -0.0086 0.0232 223 ILE A C 1699 O O . ILE A 223 ? 0.4341 0.5223 0.3884 0.0314 -0.0088 0.0175 223 ILE A O 1700 C CB . ILE A 223 ? 0.4777 0.5472 0.4127 0.0434 -0.0179 0.0340 223 ILE A CB 1701 C CG1 . ILE A 223 ? 0.5020 0.5647 0.4229 0.0465 -0.0228 0.0434 223 ILE A CG1 1702 C CG2 . ILE A 223 ? 0.4760 0.5303 0.4147 0.0478 -0.0171 0.0331 223 ILE A CG2 1703 C CD1 . ILE A 223 ? 0.5075 0.5725 0.4307 0.0592 -0.0300 0.0458 223 ILE A CD1 1704 N N . LEU A 224 ? 0.4471 0.5105 0.3933 0.0265 -0.0059 0.0231 224 LEU A N 1705 C CA . LEU A 224 ? 0.4386 0.5035 0.3938 0.0246 -0.0036 0.0165 224 LEU A CA 1706 C C . LEU A 224 ? 0.4509 0.5013 0.4059 0.0284 -0.0045 0.0166 224 LEU A C 1707 O O . LEU A 224 ? 0.4620 0.4974 0.4107 0.0264 -0.0046 0.0204 224 LEU A O 1708 C CB . LEU A 224 ? 0.4270 0.4935 0.3837 0.0164 -0.0002 0.0146 224 LEU A CB 1709 C CG . LEU A 224 ? 0.4188 0.4995 0.3760 0.0126 0.0019 0.0125 224 LEU A CG 1710 C CD1 . LEU A 224 ? 0.4332 0.5134 0.3796 0.0097 0.0027 0.0187 224 LEU A CD1 1711 C CD2 . LEU A 224 ? 0.4018 0.4878 0.3664 0.0078 0.0049 0.0072 224 LEU A CD2 1712 N N . GLN A 225 ? 0.4525 0.5066 0.4132 0.0332 -0.0046 0.0122 225 GLN A N 1713 C CA . GLN A 225 ? 0.4680 0.5098 0.4277 0.0376 -0.0047 0.0106 225 GLN A CA 1714 C C . GLN A 225 ? 0.4477 0.4889 0.4103 0.0338 -0.0028 0.0052 225 GLN A C 1715 O O . GLN A 225 ? 0.4476 0.4994 0.4151 0.0337 -0.0016 0.0017 225 GLN A O 1716 C CB . GLN A 225 ? 0.4899 0.5379 0.4531 0.0470 -0.0058 0.0097 225 GLN A CB 1717 C CG . GLN A 225 ? 0.5285 0.5749 0.4880 0.0530 -0.0096 0.0156 225 GLN A CG 1718 C CD . GLN A 225 ? 0.5534 0.6148 0.5204 0.0619 -0.0115 0.0140 225 GLN A CD 1719 O OE1 . GLN A 225 ? 0.5793 0.6492 0.5458 0.0649 -0.0154 0.0177 225 GLN A OE1 1720 N NE2 . GLN A 225 ? 0.5557 0.6218 0.5294 0.0659 -0.0089 0.0083 225 GLN A NE2 1721 N N . SER A 226 ? 0.4589 0.4870 0.4177 0.0301 -0.0029 0.0047 226 SER A N 1722 C CA . SER A 226 ? 0.4621 0.4887 0.4219 0.0269 -0.0026 -0.0002 226 SER A CA 1723 C C . SER A 226 ? 0.4434 0.4835 0.4090 0.0233 -0.0022 -0.0021 226 SER A C 1724 O O . SER A 226 ? 0.4429 0.4858 0.4092 0.0240 -0.0019 -0.0052 226 SER A O 1725 C CB . SER A 226 ? 0.4607 0.4830 0.4180 0.0328 -0.0017 -0.0039 226 SER A CB 1726 O OG . SER A 226 ? 0.4846 0.4928 0.4367 0.0378 -0.0023 -0.0032 226 SER A OG 1727 N N . GLY A 227 ? 0.4446 0.4918 0.4132 0.0195 -0.0020 -0.0003 227 GLY A N 1728 C CA . GLY A 227 ? 0.4370 0.4949 0.4111 0.0172 -0.0018 -0.0030 227 GLY A CA 1729 C C . GLY A 227 ? 0.4334 0.4983 0.4098 0.0132 -0.0006 -0.0017 227 GLY A C 1730 O O . GLY A 227 ? 0.4403 0.5045 0.4127 0.0128 0.0004 0.0024 227 GLY A O 1731 N N . SER A 228 ? 0.4233 0.4951 0.4057 0.0106 -0.0006 -0.0050 228 SER A N 1732 C CA . SER A 228 ? 0.4333 0.5152 0.4190 0.0071 0.0018 -0.0052 228 SER A CA 1733 C C . SER A 228 ? 0.4223 0.5128 0.4154 0.0084 0.0013 -0.0107 228 SER A C 1734 O O . SER A 228 ? 0.4401 0.5267 0.4353 0.0107 -0.0016 -0.0128 228 SER A O 1735 C CB . SER A 228 ? 0.4399 0.5196 0.4256 0.0010 0.0031 -0.0029 228 SER A CB 1736 O OG . SER A 228 ? 0.4442 0.5263 0.4373 -0.0012 0.0012 -0.0065 228 SER A OG 1737 N N . PRO A 229 ? 0.4351 0.5365 0.4309 0.0077 0.0041 -0.0130 229 PRO A N 1738 C CA . PRO A 229 ? 0.4283 0.5347 0.4298 0.0111 0.0032 -0.0188 229 PRO A CA 1739 C C . PRO A 229 ? 0.4129 0.5214 0.4232 0.0123 0.0006 -0.0220 229 PRO A C 1740 O O . PRO A 229 ? 0.4138 0.5188 0.4262 0.0166 -0.0026 -0.0250 229 PRO A O 1741 C CB . PRO A 229 ? 0.4472 0.5650 0.4488 0.0100 0.0074 -0.0214 229 PRO A CB 1742 C CG . PRO A 229 ? 0.4572 0.5786 0.4560 0.0044 0.0108 -0.0170 229 PRO A CG 1743 C CD . PRO A 229 ? 0.4485 0.5568 0.4414 0.0036 0.0083 -0.0108 229 PRO A CD 1744 N N . ASN A 230 ? 0.4122 0.5254 0.4268 0.0082 0.0013 -0.0210 230 ASN A N 1745 C CA . ASN A 230 ? 0.3933 0.5121 0.4181 0.0088 -0.0022 -0.0244 230 ASN A CA 1746 C C . ASN A 230 ? 0.4051 0.5121 0.4264 0.0095 -0.0081 -0.0227 230 ASN A C 1747 O O . ASN A 230 ? 0.4136 0.5254 0.4423 0.0098 -0.0123 -0.0252 230 ASN A O 1748 C CB . ASN A 230 ? 0.3801 0.5117 0.4124 0.0020 0.0013 -0.0247 230 ASN A CB 1749 C CG . ASN A 230 ? 0.3809 0.5024 0.4049 -0.0051 0.0025 -0.0188 230 ASN A CG 1750 O OD1 . ASN A 230 ? 0.3828 0.4941 0.3958 -0.0049 0.0041 -0.0144 230 ASN A OD1 1751 N ND2 . ASN A 230 ? 0.4021 0.5263 0.4317 -0.0112 0.0011 -0.0190 230 ASN A ND2 1752 N N . CYS A 231 ? 0.4141 0.5075 0.4244 0.0100 -0.0085 -0.0191 231 CYS A N 1753 C CA . CYS A 231 ? 0.4196 0.5018 0.4242 0.0112 -0.0132 -0.0184 231 CYS A CA 1754 C C . CYS A 231 ? 0.4166 0.4994 0.4244 0.0162 -0.0183 -0.0211 231 CYS A C 1755 O O . CYS A 231 ? 0.4102 0.4945 0.4197 0.0199 -0.0176 -0.0226 231 CYS A O 1756 C CB . CYS A 231 ? 0.4289 0.4996 0.4225 0.0124 -0.0115 -0.0153 231 CYS A CB 1757 S SG . CYS A 231 ? 0.4496 0.5146 0.4376 0.0092 -0.0079 -0.0116 231 CYS A SG 1758 N N . PRO A 232 ? 0.4257 0.5057 0.4331 0.0163 -0.0242 -0.0219 232 PRO A N 1759 C CA . PRO A 232 ? 0.4228 0.5027 0.4326 0.0219 -0.0306 -0.0236 232 PRO A CA 1760 C C . PRO A 232 ? 0.4343 0.5004 0.4329 0.0256 -0.0312 -0.0212 232 PRO A C 1761 O O . PRO A 232 ? 0.4421 0.5058 0.4422 0.0308 -0.0351 -0.0220 232 PRO A O 1762 C CB . PRO A 232 ? 0.4254 0.5045 0.4340 0.0201 -0.0372 -0.0242 232 PRO A CB 1763 C CG . PRO A 232 ? 0.4196 0.4908 0.4195 0.0142 -0.0339 -0.0225 232 PRO A CG 1764 C CD . PRO A 232 ? 0.4197 0.4944 0.4225 0.0116 -0.0261 -0.0212 232 PRO A CD 1765 N N . TRP A 233 ? 0.4393 0.4964 0.4270 0.0228 -0.0273 -0.0182 233 TRP A N 1766 C CA . TRP A 233 ? 0.4398 0.4855 0.4170 0.0239 -0.0265 -0.0157 233 TRP A CA 1767 C C . TRP A 233 ? 0.4336 0.4818 0.4142 0.0240 -0.0220 -0.0164 233 TRP A C 1768 O O . TRP A 233 ? 0.4603 0.5000 0.4344 0.0239 -0.0214 -0.0149 233 TRP A O 1769 C CB . TRP A 233 ? 0.4434 0.4819 0.4092 0.0209 -0.0235 -0.0134 233 TRP A CB 1770 C CG . TRP A 233 ? 0.4428 0.4865 0.4116 0.0187 -0.0186 -0.0138 233 TRP A CG 1771 C CD1 . TRP A 233 ? 0.4555 0.4998 0.4252 0.0169 -0.0194 -0.0147 233 TRP A CD1 1772 C CD2 . TRP A 233 ? 0.4313 0.4794 0.4024 0.0182 -0.0132 -0.0130 233 TRP A CD2 1773 N NE1 . TRP A 233 ? 0.4507 0.4968 0.4218 0.0158 -0.0146 -0.0139 233 TRP A NE1 1774 C CE2 . TRP A 233 ? 0.4275 0.4771 0.3997 0.0171 -0.0111 -0.0127 233 TRP A CE2 1775 C CE3 . TRP A 233 ? 0.4325 0.4825 0.4042 0.0182 -0.0105 -0.0127 233 TRP A CE3 1776 C CZ2 . TRP A 233 ? 0.4203 0.4738 0.3939 0.0175 -0.0072 -0.0114 233 TRP A CZ2 1777 C CZ3 . TRP A 233 ? 0.4300 0.4864 0.4042 0.0177 -0.0065 -0.0122 233 TRP A CZ3 1778 C CH2 . TRP A 233 ? 0.4249 0.4832 0.3999 0.0180 -0.0052 -0.0113 233 TRP A CH2 1779 N N . ALA A 234 ? 0.4359 0.4955 0.4257 0.0234 -0.0187 -0.0186 234 ALA A N 1780 C CA . ALA A 234 ? 0.4211 0.4843 0.4122 0.0226 -0.0142 -0.0196 234 ALA A CA 1781 C C . ALA A 234 ? 0.4301 0.4943 0.4262 0.0259 -0.0153 -0.0236 234 ALA A C 1782 O O . ALA A 234 ? 0.4481 0.5127 0.4432 0.0248 -0.0125 -0.0252 234 ALA A O 1783 C CB . ALA A 234 ? 0.4223 0.4955 0.4171 0.0201 -0.0102 -0.0194 234 ALA A CB 1784 N N . SER A 235 ? 0.4435 0.5085 0.4453 0.0304 -0.0198 -0.0260 235 SER A N 1785 C CA . SER A 235 ? 0.4472 0.5112 0.4539 0.0356 -0.0212 -0.0307 235 SER A CA 1786 C C . SER A 235 ? 0.4634 0.5221 0.4729 0.0423 -0.0285 -0.0315 235 SER A C 1787 O O . SER A 235 ? 0.4768 0.5361 0.4859 0.0424 -0.0327 -0.0289 235 SER A O 1788 C CB . SER A 235 ? 0.4386 0.5191 0.4552 0.0360 -0.0165 -0.0360 235 SER A CB 1789 O OG . SER A 235 ? 0.4211 0.5156 0.4475 0.0362 -0.0169 -0.0370 235 SER A OG 1790 N N . VAL A 236 ? 0.4765 0.5289 0.4883 0.0484 -0.0307 -0.0354 236 VAL A N 1791 C CA . VAL A 236 ? 0.4864 0.5329 0.5016 0.0573 -0.0388 -0.0364 236 VAL A CA 1792 C C . VAL A 236 ? 0.4878 0.5390 0.5136 0.0655 -0.0386 -0.0445 236 VAL A C 1793 O O . VAL A 236 ? 0.4860 0.5373 0.5110 0.0634 -0.0328 -0.0486 236 VAL A O 1794 C CB . VAL A 236 ? 0.5021 0.5233 0.5016 0.0578 -0.0442 -0.0304 236 VAL A CB 1795 C CG1 . VAL A 236 ? 0.4993 0.5166 0.4874 0.0504 -0.0438 -0.0235 236 VAL A CG1 1796 C CG2 . VAL A 236 ? 0.5080 0.5134 0.4997 0.0556 -0.0411 -0.0315 236 VAL A CG2 1797 N N . SER A 237 ? 0.4897 0.5453 0.5255 0.0753 -0.0453 -0.0475 237 SER A N 1798 C CA . SER A 237 ? 0.5060 0.5660 0.5529 0.0855 -0.0454 -0.0562 237 SER A CA 1799 C C . SER A 237 ? 0.5428 0.5742 0.5769 0.0887 -0.0480 -0.0560 237 SER A C 1800 O O . SER A 237 ? 0.5728 0.5827 0.5911 0.0839 -0.0511 -0.0481 237 SER A O 1801 C CB . SER A 237 ? 0.5109 0.5825 0.5724 0.0966 -0.0535 -0.0590 237 SER A CB 1802 O OG . SER A 237 ? 0.5338 0.5828 0.5845 0.1019 -0.0640 -0.0527 237 SER A OG 1803 N N . VAL A 238 ? 0.5483 0.5786 0.5886 0.0964 -0.0464 -0.0650 238 VAL A N 1804 C CA . VAL A 238 ? 0.5613 0.5619 0.5890 0.0987 -0.0488 -0.0657 238 VAL A CA 1805 C C . VAL A 238 ? 0.5648 0.5420 0.5860 0.1075 -0.0601 -0.0602 238 VAL A C 1806 O O . VAL A 238 ? 0.6061 0.5538 0.6105 0.1041 -0.0629 -0.0548 238 VAL A O 1807 C CB . VAL A 238 ? 0.5690 0.5717 0.6032 0.1050 -0.0443 -0.0782 238 VAL A CB 1808 C CG1 . VAL A 238 ? 0.5633 0.5908 0.6021 0.0964 -0.0336 -0.0829 238 VAL A CG1 1809 C CG2 . VAL A 238 ? 0.5727 0.5841 0.6230 0.1218 -0.0490 -0.0862 238 VAL A CG2 1810 N N . ALA A 239 ? 0.5644 0.5553 0.5986 0.1181 -0.0667 -0.0612 239 ALA A N 1811 C CA . ALA A 239 ? 0.5816 0.5515 0.6085 0.1272 -0.0791 -0.0548 239 ALA A CA 1812 C C . ALA A 239 ? 0.5784 0.5347 0.5865 0.1159 -0.0813 -0.0423 239 ALA A C 1813 O O . ALA A 239 ? 0.6178 0.5442 0.6084 0.1169 -0.0879 -0.0348 239 ALA A O 1814 C CB . ALA A 239 ? 0.5733 0.5663 0.6202 0.1405 -0.0864 -0.0589 239 ALA A CB 1815 N N . GLU A 240 ? 0.5452 0.5221 0.5556 0.1051 -0.0754 -0.0400 240 GLU A N 1816 C CA . GLU A 240 ? 0.5474 0.5136 0.5403 0.0945 -0.0758 -0.0297 240 GLU A CA 1817 C C . GLU A 240 ? 0.5569 0.5013 0.5326 0.0839 -0.0697 -0.0257 240 GLU A C 1818 O O . GLU A 240 ? 0.5645 0.4869 0.5218 0.0793 -0.0728 -0.0171 240 GLU A O 1819 C CB . GLU A 240 ? 0.5235 0.5161 0.5241 0.0868 -0.0711 -0.0296 240 GLU A CB 1820 C CG . GLU A 240 ? 0.5293 0.5130 0.5128 0.0774 -0.0715 -0.0207 240 GLU A CG 1821 C CD . GLU A 240 ? 0.5630 0.5302 0.5340 0.0828 -0.0829 -0.0140 240 GLU A CD 1822 O OE1 . GLU A 240 ? 0.5731 0.5444 0.5538 0.0947 -0.0922 -0.0165 240 GLU A OE1 1823 O OE2 . GLU A 240 ? 0.5944 0.5458 0.5457 0.0754 -0.0826 -0.0063 240 GLU A OE2 1824 N N . GLY A 241 ? 0.5636 0.5149 0.5449 0.0794 -0.0611 -0.0321 241 GLY A N 1825 C CA . GLY A 241 ? 0.5822 0.5149 0.5502 0.0696 -0.0561 -0.0301 241 GLY A CA 1826 C C . GLY A 241 ? 0.6188 0.5178 0.5738 0.0736 -0.0625 -0.0273 241 GLY A C 1827 O O . GLY A 241 ? 0.6349 0.5129 0.5732 0.0641 -0.0615 -0.0205 241 GLY A O 1828 N N . ARG A 242 ? 0.6492 0.5431 0.6121 0.0878 -0.0691 -0.0326 242 ARG A N 1829 C CA . ARG A 242 ? 0.6956 0.5548 0.6466 0.0942 -0.0765 -0.0305 242 ARG A CA 1830 C C . ARG A 242 ? 0.7111 0.5512 0.6452 0.0941 -0.0847 -0.0179 242 ARG A C 1831 O O . ARG A 242 ? 0.7618 0.5713 0.6760 0.0871 -0.0859 -0.0104 242 ARG A O 1832 C CB . ARG A 242 ? 0.7099 0.5720 0.6760 0.1120 -0.0817 -0.0404 242 ARG A CB 1833 C CG . ARG A 242 ? 0.7610 0.5846 0.7159 0.1203 -0.0888 -0.0407 242 ARG A CG 1834 C CD . ARG A 242 ? 0.7666 0.5968 0.7387 0.1363 -0.0898 -0.0547 242 ARG A CD 1835 N NE . ARG A 242 ? 0.7578 0.5897 0.7316 0.1292 -0.0800 -0.0649 242 ARG A NE 1836 C CZ . ARG A 242 ? 0.7883 0.5872 0.7471 0.1234 -0.0794 -0.0660 242 ARG A CZ 1837 N NH1 . ARG A 242 ? 0.8127 0.5722 0.7527 0.1230 -0.0871 -0.0565 242 ARG A NH1 1838 N NH2 . ARG A 242 ? 0.7885 0.5927 0.7495 0.1169 -0.0711 -0.0764 242 ARG A NH2 1839 N N . ARG A 243 ? 0.6886 0.5468 0.6296 0.1005 -0.0903 -0.0155 243 ARG A N 1840 C CA . ARG A 243 ? 0.7031 0.5444 0.6265 0.1011 -0.0991 -0.0040 243 ARG A CA 1841 C C . ARG A 243 ? 0.6784 0.5070 0.5807 0.0839 -0.0927 0.0053 243 ARG A C 1842 O O . ARG A 243 ? 0.6890 0.4877 0.5693 0.0812 -0.0974 0.0149 243 ARG A O 1843 C CB . ARG A 243 ? 0.7084 0.5764 0.6435 0.1078 -0.1051 -0.0043 243 ARG A CB 1844 C CG . ARG A 243 ? 0.7362 0.6092 0.6866 0.1270 -0.1163 -0.0095 243 ARG A CG 1845 C CD . ARG A 243 ? 0.7356 0.6367 0.6980 0.1317 -0.1229 -0.0098 243 ARG A CD 1846 N NE . ARG A 243 ? 0.7053 0.6420 0.6866 0.1243 -0.1129 -0.0173 243 ARG A NE 1847 C CZ . ARG A 243 ? 0.6801 0.6447 0.6872 0.1313 -0.1104 -0.0280 243 ARG A CZ 1848 N NH1 . ARG A 243 ? 0.6849 0.6499 0.7052 0.1474 -0.1170 -0.0342 243 ARG A NH1 1849 N NH2 . ARG A 243 ? 0.6504 0.6429 0.6697 0.1221 -0.1008 -0.0325 243 ARG A NH2 1850 N N . ARG A 244 ? 0.6416 0.4931 0.5506 0.0726 -0.0819 0.0024 244 ARG A N 1851 C CA . ARG A 244 ? 0.6319 0.4788 0.5249 0.0570 -0.0745 0.0095 244 ARG A CA 1852 C C . ARG A 244 ? 0.6465 0.4694 0.5277 0.0472 -0.0696 0.0115 244 ARG A C 1853 O O . ARG A 244 ? 0.6787 0.4828 0.5399 0.0373 -0.0682 0.0206 244 ARG A O 1854 C CB . ARG A 244 ? 0.5855 0.4638 0.4912 0.0498 -0.0650 0.0049 244 ARG A CB 1855 C CG . ARG A 244 ? 0.5564 0.4570 0.4715 0.0556 -0.0686 0.0036 244 ARG A CG 1856 C CD . ARG A 244 ? 0.5242 0.4503 0.4494 0.0482 -0.0593 -0.0003 244 ARG A CD 1857 N NE . ARG A 244 ? 0.5088 0.4548 0.4437 0.0525 -0.0626 -0.0024 244 ARG A NE 1858 C CZ . ARG A 244 ? 0.4859 0.4501 0.4259 0.0468 -0.0567 -0.0041 244 ARG A CZ 1859 N NH1 . ARG A 244 ? 0.4777 0.4449 0.4150 0.0381 -0.0476 -0.0038 244 ARG A NH1 1860 N NH2 . ARG A 244 ? 0.4915 0.4707 0.4396 0.0499 -0.0605 -0.0061 244 ARG A NH2 1861 N N . ALA A 245 ? 0.6210 0.4455 0.5141 0.0489 -0.0666 0.0026 245 ALA A N 1862 C CA . ALA A 245 ? 0.6325 0.4324 0.5157 0.0402 -0.0635 0.0028 245 ALA A CA 1863 C C . ALA A 245 ? 0.6573 0.4174 0.5196 0.0424 -0.0718 0.0116 245 ALA A C 1864 O O . ALA A 245 ? 0.6691 0.4080 0.5141 0.0293 -0.0686 0.0187 245 ALA A O 1865 C CB . ALA A 245 ? 0.6328 0.4380 0.5309 0.0454 -0.0617 -0.0095 245 ALA A CB 1866 N N . VAL A 246 ? 0.6655 0.4159 0.5298 0.0590 -0.0826 0.0113 246 VAL A N 1867 C CA . VAL A 246 ? 0.7132 0.4236 0.5571 0.0640 -0.0925 0.0204 246 VAL A CA 1868 C C . VAL A 246 ? 0.7314 0.4332 0.5534 0.0560 -0.0941 0.0343 246 VAL A C 1869 O O . VAL A 246 ? 0.7668 0.4342 0.5646 0.0483 -0.0959 0.0445 246 VAL A O 1870 C CB . VAL A 246 ? 0.7204 0.4273 0.5748 0.0865 -0.1048 0.0160 246 VAL A CB 1871 C CG1 . VAL A 246 ? 0.7550 0.4212 0.5865 0.0936 -0.1172 0.0274 246 VAL A CG1 1872 C CG2 . VAL A 246 ? 0.7142 0.4235 0.5861 0.0944 -0.1026 0.0020 246 VAL A CG2 1873 N N . GLU A 247 ? 0.7093 0.4413 0.5384 0.0572 -0.0933 0.0345 247 GLU A N 1874 C CA . GLU A 247 ? 0.7231 0.4508 0.5318 0.0505 -0.0944 0.0457 247 GLU A CA 1875 C C . GLU A 247 ? 0.7325 0.4547 0.5267 0.0301 -0.0823 0.0510 247 GLU A C 1876 O O . GLU A 247 ? 0.7725 0.4725 0.5412 0.0220 -0.0830 0.0623 247 GLU A O 1877 C CB . GLU A 247 ? 0.6926 0.4545 0.5140 0.0560 -0.0958 0.0423 247 GLU A CB 1878 C CG . GLU A 247 ? 0.7243 0.4831 0.5243 0.0513 -0.0985 0.0522 247 GLU A CG 1879 C CD . GLU A 247 ? 0.7883 0.5121 0.5630 0.0572 -0.1111 0.0637 247 GLU A CD 1880 O OE1 . GLU A 247 ? 0.8121 0.5182 0.5908 0.0703 -0.1210 0.0629 247 GLU A OE1 1881 O OE2 . GLU A 247 ? 0.8020 0.5157 0.5517 0.0492 -0.1110 0.0737 247 GLU A OE2 1882 N N . LEU A 248 ? 0.7108 0.4531 0.5207 0.0216 -0.0714 0.0428 248 LEU A N 1883 C CA . LEU A 248 ? 0.7230 0.4625 0.5236 0.0026 -0.0601 0.0461 248 LEU A CA 1884 C C . LEU A 248 ? 0.7835 0.4820 0.5640 -0.0043 -0.0625 0.0532 248 LEU A C 1885 O O . LEU A 248 ? 0.8207 0.5018 0.5787 -0.0168 -0.0593 0.0637 248 LEU A O 1886 C CB . LEU A 248 ? 0.6999 0.4660 0.5228 -0.0024 -0.0510 0.0350 248 LEU A CB 1887 C CG . LEU A 248 ? 0.7097 0.4802 0.5297 -0.0212 -0.0396 0.0357 248 LEU A CG 1888 C CD1 . LEU A 248 ? 0.7105 0.4970 0.5223 -0.0298 -0.0326 0.0416 248 LEU A CD1 1889 C CD2 . LEU A 248 ? 0.6765 0.4717 0.5192 -0.0225 -0.0341 0.0240 248 LEU A CD2 1890 N N . GLY A 249 ? 0.8096 0.4916 0.5976 0.0037 -0.0678 0.0472 249 GLY A N 1891 C CA . GLY A 249 ? 0.8460 0.4842 0.6155 -0.0007 -0.0718 0.0528 249 GLY A CA 1892 C C . GLY A 249 ? 0.8836 0.4908 0.6253 0.0013 -0.0800 0.0675 249 GLY A C 1893 O O . GLY A 249 ? 0.9116 0.4885 0.6299 -0.0127 -0.0777 0.0775 249 GLY A O 1894 N N . ARG A 250 ? 0.8904 0.5056 0.6339 0.0179 -0.0898 0.0691 250 ARG A N 1895 C CA . ARG A 250 ? 0.9565 0.5436 0.6726 0.0216 -0.0997 0.0832 250 ARG A CA 1896 C C . ARG A 250 ? 0.9481 0.5383 0.6424 0.0038 -0.0912 0.0938 250 ARG A C 1897 O O . ARG A 250 ? 0.9822 0.5387 0.6465 -0.0030 -0.0942 0.1072 250 ARG A O 1898 C CB . ARG A 250 ? 0.9857 0.5868 0.7113 0.0429 -0.1126 0.0813 250 ARG A CB 1899 C CG . ARG A 250 ? 1.0675 0.6305 0.7686 0.0538 -0.1280 0.0934 250 ARG A CG 1900 C CD . ARG A 250 ? 1.0922 0.6755 0.8064 0.0743 -0.1410 0.0902 250 ARG A CD 1901 N NE . ARG A 250 ? 1.1185 0.7352 0.8335 0.0681 -0.1365 0.0906 250 ARG A NE 1902 C CZ . ARG A 250 ? 1.1781 0.7854 0.8651 0.0608 -0.1383 0.1025 250 ARG A CZ 1903 N NH1 . ARG A 250 ? 1.2404 0.8055 0.8946 0.0580 -0.1448 0.1169 250 ARG A NH1 1904 N NH2 . ARG A 250 ? 1.1576 0.7966 0.8478 0.0559 -0.1336 0.1001 250 ARG A NH2 1905 N N . ASN A 251 ? 0.9015 0.5311 0.6103 -0.0035 -0.0803 0.0875 251 ASN A N 1906 C CA . ASN A 251 ? 0.9036 0.5415 0.5954 -0.0203 -0.0699 0.0948 251 ASN A CA 1907 C C . ASN A 251 ? 0.9256 0.5449 0.6037 -0.0412 -0.0592 0.1001 251 ASN A C 1908 O O . ASN A 251 ? 0.9389 0.5524 0.5946 -0.0551 -0.0526 0.1097 251 ASN A O 1909 C CB . ASN A 251 ? 0.8642 0.5482 0.5778 -0.0217 -0.0606 0.0850 251 ASN A CB 1910 C CG . ASN A 251 ? 0.8540 0.5543 0.5665 -0.0101 -0.0676 0.0852 251 ASN A CG 1911 O OD1 . ASN A 251 ? 0.8692 0.5640 0.5585 -0.0152 -0.0673 0.0936 251 ASN A OD1 1912 N ND2 . ASN A 251 ? 0.8372 0.5583 0.5742 0.0045 -0.0737 0.0755 251 ASN A ND2 1913 N N . LEU A 252 ? 0.9331 0.5451 0.6251 -0.0443 -0.0571 0.0932 252 LEU A N 1914 C CA . LEU A 252 ? 0.9634 0.5557 0.6441 -0.0651 -0.0483 0.0973 252 LEU A CA 1915 C C . LEU A 252 ? 1.0114 0.5508 0.6707 -0.0653 -0.0571 0.1056 252 LEU A C 1916 O O . LEU A 252 ? 1.0025 0.5229 0.6567 -0.0814 -0.0514 0.1063 252 LEU A O 1917 C CB . LEU A 252 ? 0.9267 0.5459 0.6353 -0.0717 -0.0395 0.0838 252 LEU A CB 1918 C CG . LEU A 252 ? 0.8764 0.5446 0.6044 -0.0736 -0.0299 0.0768 252 LEU A CG 1919 C CD1 . LEU A 252 ? 0.8434 0.5370 0.6004 -0.0728 -0.0261 0.0627 252 LEU A CD1 1920 C CD2 . LEU A 252 ? 0.8847 0.5616 0.5992 -0.0933 -0.0174 0.0838 252 LEU A CD2 1921 N N . ASN A 253 ? 1.0654 0.5810 0.7120 -0.0478 -0.0715 0.1117 253 ASN A N 1922 C CA . ASN A 253 ? 1.1530 0.6146 0.7771 -0.0442 -0.0822 0.1207 253 ASN A CA 1923 C C . ASN A 253 ? 1.1546 0.6006 0.7942 -0.0426 -0.0832 0.1099 253 ASN A C 1924 O O . ASN A 253 ? 1.1793 0.5825 0.8005 -0.0526 -0.0843 0.1159 253 ASN A O 1925 C CB . ASN A 253 ? 1.2245 0.6531 0.8123 -0.0653 -0.0772 0.1376 253 ASN A CB 1926 C CG . ASN A 253 ? 1.2476 0.6969 0.8199 -0.0706 -0.0725 0.1462 253 ASN A CG 1927 O OD1 . ASN A 253 ? 1.2578 0.7315 0.8307 -0.0894 -0.0574 0.1460 253 ASN A OD1 1928 N ND2 . ASN A 253 ? 1.2602 0.7022 0.8199 -0.0536 -0.0855 0.1527 253 ASN A ND2 1929 N N . CYS A 254 ? 1.1126 0.5926 0.7846 -0.0306 -0.0827 0.0940 254 CYS A N 1930 C CA . CYS A 254 ? 1.1037 0.5739 0.7911 -0.0280 -0.0832 0.0816 254 CYS A CA 1931 C C . CYS A 254 ? 1.1412 0.5793 0.8261 -0.0053 -0.0984 0.0804 254 CYS A C 1932 O O . CYS A 254 ? 1.1374 0.5772 0.8199 0.0126 -0.1087 0.0850 254 CYS A O 1933 C CB . CYS A 254 ? 1.0605 0.5800 0.7814 -0.0249 -0.0760 0.0652 254 CYS A CB 1934 S SG . CYS A 254 ? 1.0545 0.6081 0.7842 -0.0513 -0.0585 0.0621 254 CYS A SG 1935 N N . ASN A 255 ? 1.1696 0.5787 0.8554 -0.0062 -0.0998 0.0735 255 ASN A N 1936 C CA . ASN A 255 ? 1.1826 0.5635 0.8710 0.0165 -0.1127 0.0679 255 ASN A CA 1937 C C . ASN A 255 ? 1.1223 0.5473 0.8440 0.0362 -0.1138 0.0520 255 ASN A C 1938 O O . ASN A 255 ? 1.0750 0.5305 0.8174 0.0302 -0.1045 0.0388 255 ASN A O 1939 C CB . ASN A 255 ? 1.2213 0.5628 0.9029 0.0075 -0.1116 0.0623 255 ASN A CB 1940 C CG . ASN A 255 ? 1.2609 0.5652 0.9411 0.0311 -0.1252 0.0573 255 ASN A CG 1941 O OD1 . ASN A 255 ? 1.2450 0.5720 0.9461 0.0549 -0.1314 0.0477 255 ASN A OD1 1942 N ND2 . ASN A 255 ? 1.3177 0.5643 0.9736 0.0244 -0.1297 0.0637 255 ASN A ND2 1943 N N . LEU A 256 ? 1.1160 0.5451 0.8424 0.0593 -0.1254 0.0534 256 LEU A N 1944 C CA . LEU A 256 ? 1.0700 0.5447 0.8280 0.0765 -0.1258 0.0396 256 LEU A CA 1945 C C . LEU A 256 ? 1.0851 0.5470 0.8570 0.0988 -0.1339 0.0270 256 LEU A C 1946 O O . LEU A 256 ? 1.0697 0.5674 0.8671 0.1147 -0.1351 0.0160 256 LEU A O 1947 C CB . LEU A 256 ? 1.0514 0.5511 0.8110 0.0861 -0.1319 0.0473 256 LEU A CB 1948 C CG . LEU A 256 ? 1.0488 0.5592 0.7919 0.0670 -0.1251 0.0599 256 LEU A CG 1949 C CD1 . LEU A 256 ? 1.0288 0.5670 0.7765 0.0782 -0.1317 0.0639 256 LEU A CD1 1950 C CD2 . LEU A 256 ? 1.0180 0.5597 0.7733 0.0474 -0.1088 0.0529 256 LEU A CD2 1951 N N . ASN A 257 ? 1.1300 0.5418 0.8859 0.0997 -0.1388 0.0277 257 ASN A N 1952 C CA . ASN A 257 ? 1.1594 0.5542 0.9264 0.1231 -0.1474 0.0155 257 ASN A CA 1953 C C . ASN A 257 ? 1.1284 0.5583 0.9243 0.1277 -0.1388 -0.0058 257 ASN A C 1954 O O . ASN A 257 ? 1.1372 0.5717 0.9496 0.1504 -0.1445 -0.0177 257 ASN A O 1955 C CB . ASN A 257 ? 1.2312 0.5597 0.9722 0.1215 -0.1541 0.0207 257 ASN A CB 1956 C CG . ASN A 257 ? 1.2761 0.5648 0.9884 0.1253 -0.1664 0.0411 257 ASN A CG 1957 O OD1 . ASN A 257 ? 1.2671 0.5784 0.9773 0.1271 -0.1696 0.0516 257 ASN A OD1 1958 N ND2 . ASN A 257 ? 1.3341 0.5619 1.0227 0.1262 -0.1739 0.0468 257 ASN A ND2 1959 N N . SER A 258 ? 1.1023 0.5574 0.9039 0.1068 -0.1253 -0.0107 258 SER A N 1960 C CA . SER A 258 ? 1.0668 0.5585 0.8934 0.1098 -0.1169 -0.0295 258 SER A CA 1961 C C . SER A 258 ? 1.0220 0.5532 0.8559 0.0884 -0.1038 -0.0301 258 SER A C 1962 O O . SER A 258 ? 1.0232 0.5510 0.8430 0.0699 -0.1000 -0.0176 258 SER A O 1963 C CB . SER A 258 ? 1.0998 0.5580 0.9226 0.1115 -0.1170 -0.0424 258 SER A CB 1964 O OG . SER A 258 ? 1.1122 0.5528 0.9202 0.0857 -0.1096 -0.0402 258 SER A OG 1965 N N . ASP A 259 ? 0.9879 0.5565 0.8434 0.0916 -0.0968 -0.0450 259 ASP A N 1966 C CA . ASP A 259 ? 0.9514 0.5567 0.8149 0.0736 -0.0852 -0.0472 259 ASP A CA 1967 C C . ASP A 259 ? 0.9758 0.5593 0.8251 0.0513 -0.0799 -0.0467 259 ASP A C 1968 O O . ASP A 259 ? 0.9593 0.5605 0.8064 0.0331 -0.0729 -0.0402 259 ASP A O 1969 C CB . ASP A 259 ? 0.9334 0.5767 0.8195 0.0819 -0.0796 -0.0636 259 ASP A CB 1970 C CG . ASP A 259 ? 0.9054 0.5849 0.8094 0.0972 -0.0811 -0.0638 259 ASP A CG 1971 O OD1 . ASP A 259 ? 0.9066 0.5786 0.8063 0.1049 -0.0887 -0.0530 259 ASP A OD1 1972 O OD2 . ASP A 259 ? 0.8964 0.6119 0.8180 0.1006 -0.0749 -0.0746 259 ASP A OD2 1973 N N . GLU A 260 ? 1.0306 0.5773 0.8716 0.0527 -0.0829 -0.0547 260 GLU A N 1974 C CA . GLU A 260 ? 1.0546 0.5798 0.8829 0.0302 -0.0783 -0.0557 260 GLU A CA 1975 C C . GLU A 260 ? 1.0809 0.5812 0.8887 0.0141 -0.0791 -0.0372 260 GLU A C 1976 O O . GLU A 260 ? 1.0593 0.5711 0.8638 -0.0082 -0.0716 -0.0328 260 GLU A O 1977 C CB . GLU A 260 ? 1.0788 0.5644 0.9003 0.0355 -0.0825 -0.0684 260 GLU A CB 1978 N N . GLU A 261 ? 1.1246 0.5935 0.9189 0.0257 -0.0882 -0.0261 261 GLU A N 1979 C CA . GLU A 261 ? 1.1734 0.6133 0.9439 0.0111 -0.0895 -0.0077 261 GLU A CA 1980 C C . GLU A 261 ? 1.1210 0.5993 0.8946 0.0013 -0.0830 0.0028 261 GLU A C 1981 O O . GLU A 261 ? 1.1416 0.6131 0.9012 -0.0199 -0.0774 0.0133 261 GLU A O 1982 C CB . GLU A 261 ? 1.2456 0.6404 0.9989 0.0279 -0.1024 0.0017 261 GLU A CB 1983 C CG . GLU A 261 ? 1.3102 0.6501 1.0499 0.0301 -0.1083 -0.0037 261 GLU A CG 1984 C CD . GLU A 261 ? 1.3755 0.6761 1.1040 0.0539 -0.1227 0.0023 261 GLU A CD 1985 O OE1 . GLU A 261 ? 1.3779 0.7036 1.1243 0.0783 -0.1282 -0.0035 261 GLU A OE1 1986 O OE2 . GLU A 261 ? 1.4149 0.6598 1.1168 0.0482 -0.1288 0.0128 261 GLU A OE2 1987 N N . LEU A 262 ? 1.0539 0.5722 0.8458 0.0164 -0.0835 -0.0005 262 LEU A N 1988 C CA . LEU A 262 ? 0.9907 0.5469 0.7873 0.0095 -0.0777 0.0072 262 LEU A CA 1989 C C . LEU A 262 ? 0.9518 0.5398 0.7587 -0.0098 -0.0656 0.0018 262 LEU A C 1990 O O . LEU A 262 ? 0.9312 0.5289 0.7310 -0.0259 -0.0592 0.0108 262 LEU A O 1991 C CB . LEU A 262 ? 0.9483 0.5380 0.7633 0.0301 -0.0816 0.0030 262 LEU A CB 1992 C CG . LEU A 262 ? 0.8905 0.5246 0.7158 0.0252 -0.0751 0.0062 262 LEU A CG 1993 C CD1 . LEU A 262 ? 0.9040 0.5269 0.7086 0.0138 -0.0745 0.0222 262 LEU A CD1 1994 C CD2 . LEU A 262 ? 0.8581 0.5194 0.7013 0.0454 -0.0801 0.0009 262 LEU A CD2 1995 N N . ILE A 263 ? 0.9484 0.5534 0.7718 -0.0073 -0.0626 -0.0132 263 ILE A N 1996 C CA . ILE A 263 ? 0.9331 0.5696 0.7673 -0.0235 -0.0529 -0.0191 263 ILE A CA 1997 C C . ILE A 263 ? 0.9881 0.6010 0.8079 -0.0467 -0.0490 -0.0146 263 ILE A C 1998 O O . ILE A 263 ? 0.9813 0.6165 0.8031 -0.0631 -0.0413 -0.0103 263 ILE A O 1999 C CB . ILE A 263 ? 0.9108 0.5672 0.7625 -0.0155 -0.0517 -0.0361 263 ILE A CB 2000 C CG1 . ILE A 263 ? 0.8843 0.5740 0.7525 0.0029 -0.0528 -0.0394 263 ILE A CG1 2001 C CG2 . ILE A 263 ? 0.8910 0.5731 0.7505 -0.0333 -0.0437 -0.0421 263 ILE A CG2 2002 C CD1 . ILE A 263 ? 0.8816 0.5841 0.7637 0.0151 -0.0529 -0.0553 263 ILE A CD1 2003 N N . HIS A 264 ? 1.0703 0.6379 0.8760 -0.0482 -0.0542 -0.0157 264 HIS A N 2004 C CA . HIS A 264 ? 1.1356 0.6766 0.9261 -0.0719 -0.0507 -0.0109 264 HIS A CA 2005 C C . HIS A 264 ? 1.1133 0.6545 0.8904 -0.0846 -0.0466 0.0062 264 HIS A C 2006 O O . HIS A 264 ? 1.1243 0.6778 0.9008 -0.1065 -0.0383 0.0090 264 HIS A O 2007 C CB . HIS A 264 ? 1.2248 0.7091 0.9982 -0.0698 -0.0583 -0.0125 264 HIS A CB 2008 C CG . HIS A 264 ? 1.3333 0.7880 1.0910 -0.0962 -0.0547 -0.0082 264 HIS A CG 2009 N ND1 . HIS A 264 ? 1.3933 0.8193 1.1287 -0.1094 -0.0540 0.0089 264 HIS A ND1 2010 C CD2 . HIS A 264 ? 1.3907 0.8407 1.1512 -0.1130 -0.0514 -0.0189 264 HIS A CD2 2011 C CE1 . HIS A 264 ? 1.4399 0.8447 1.1659 -0.1340 -0.0499 0.0088 264 HIS A CE1 2012 N NE2 . HIS A 264 ? 1.4464 0.8654 1.1880 -0.1366 -0.0487 -0.0082 264 HIS A NE2 2013 N N . CYS A 265 ? 1.1051 0.6349 0.8719 -0.0709 -0.0523 0.0169 265 CYS A N 2014 C CA . CYS A 265 ? 1.0947 0.6249 0.8463 -0.0814 -0.0486 0.0329 265 CYS A CA 2015 C C . CYS A 265 ? 1.0154 0.5987 0.7831 -0.0885 -0.0386 0.0317 265 CYS A C 2016 O O . CYS A 265 ? 1.0011 0.5925 0.7627 -0.1084 -0.0299 0.0382 265 CYS A O 2017 C CB . CYS A 265 ? 1.1191 0.6298 0.8572 -0.0629 -0.0583 0.0432 265 CYS A CB 2018 S SG . CYS A 265 ? 1.1706 0.6788 0.8852 -0.0747 -0.0545 0.0627 265 CYS A SG 2019 N N . LEU A 266 ? 0.9439 0.5629 0.7325 -0.0724 -0.0395 0.0230 266 LEU A N 2020 C CA . LEU A 266 ? 0.8727 0.5400 0.6773 -0.0760 -0.0313 0.0210 266 LEU A CA 2021 C C . LEU A 266 ? 0.8582 0.5469 0.6741 -0.0945 -0.0226 0.0141 266 LEU A C 2022 O O . LEU A 266 ? 0.8319 0.5507 0.6539 -0.1043 -0.0145 0.0166 266 LEU A O 2023 C CB . LEU A 266 ? 0.8185 0.5151 0.6421 -0.0556 -0.0348 0.0129 266 LEU A CB 2024 C CG . LEU A 266 ? 0.8083 0.4970 0.6261 -0.0374 -0.0429 0.0190 266 LEU A CG 2025 C CD1 . LEU A 266 ? 0.7653 0.4854 0.6043 -0.0205 -0.0450 0.0097 266 LEU A CD1 2026 C CD2 . LEU A 266 ? 0.8162 0.5087 0.6203 -0.0435 -0.0402 0.0316 266 LEU A CD2 2027 N N . ARG A 267 ? 0.8976 0.5713 0.7164 -0.0987 -0.0246 0.0049 267 ARG A N 2028 C CA . ARG A 267 ? 0.9050 0.5969 0.7338 -0.1172 -0.0180 -0.0022 267 ARG A CA 2029 C C . ARG A 267 ? 0.9251 0.6015 0.7405 -0.1416 -0.0120 0.0064 267 ARG A C 2030 O O . ARG A 267 ? 0.9206 0.6254 0.7470 -0.1575 -0.0046 0.0033 267 ARG A O 2031 C CB . ARG A 267 ? 0.9282 0.6082 0.7629 -0.1145 -0.0226 -0.0161 267 ARG A CB 2032 C CG . ARG A 267 ? 0.9003 0.6120 0.7535 -0.0968 -0.0244 -0.0270 267 ARG A CG 2033 C CD . ARG A 267 ? 0.9097 0.6113 0.7670 -0.0945 -0.0280 -0.0416 267 ARG A CD 2034 N NE . ARG A 267 ? 0.8803 0.6135 0.7534 -0.0786 -0.0286 -0.0512 267 ARG A NE 2035 C CZ . ARG A 267 ? 0.8702 0.5988 0.7471 -0.0700 -0.0318 -0.0645 267 ARG A CZ 2036 N NH1 . ARG A 267 ? 0.8909 0.5830 0.7572 -0.0749 -0.0353 -0.0708 267 ARG A NH1 2037 N NH2 . ARG A 267 ? 0.8392 0.5985 0.7292 -0.0569 -0.0311 -0.0717 267 ARG A NH2 2038 N N . GLU A 268 ? 0.9632 0.5956 0.7549 -0.1447 -0.0153 0.0172 268 GLU A N 2039 C CA . GLU A 268 ? 0.9953 0.6094 0.7710 -0.1693 -0.0089 0.0271 268 GLU A CA 2040 C C . GLU A 268 ? 0.9720 0.6167 0.7473 -0.1767 0.0004 0.0366 268 GLU A C 2041 O O . GLU A 268 ? 1.0040 0.6528 0.7746 -0.1991 0.0091 0.0416 268 GLU A O 2042 C CB . GLU A 268 ? 1.0392 0.5927 0.7866 -0.1699 -0.0159 0.0371 268 GLU A CB 2043 N N . LYS A 269 ? 0.9272 0.5945 0.7080 -0.1585 -0.0010 0.0382 269 LYS A N 2044 C CA . LYS A 269 ? 0.8915 0.5843 0.6695 -0.1629 0.0071 0.0464 269 LYS A CA 2045 C C . LYS A 269 ? 0.8531 0.5951 0.6535 -0.1733 0.0174 0.0394 269 LYS A C 2046 O O . LYS A 269 ? 0.8511 0.6172 0.6732 -0.1691 0.0161 0.0275 269 LYS A O 2047 C CB . LYS A 269 ? 0.8591 0.5607 0.6369 -0.1400 0.0015 0.0486 269 LYS A CB 2048 C CG . LYS A 269 ? 0.8847 0.5433 0.6416 -0.1269 -0.0096 0.0563 269 LYS A CG 2049 C CD . LYS A 269 ? 0.9288 0.5502 0.6551 -0.1412 -0.0082 0.0714 269 LYS A CD 2050 C CE . LYS A 269 ? 0.9519 0.5298 0.6573 -0.1260 -0.0212 0.0794 269 LYS A CE 2051 N NZ . LYS A 269 ? 1.0067 0.5416 0.6795 -0.1408 -0.0208 0.0946 269 LYS A NZ 2052 N N . LYS A 270 ? 0.8471 0.6045 0.6417 -0.1863 0.0274 0.0467 270 LYS A N 2053 C CA . LYS A 270 ? 0.8004 0.6082 0.6170 -0.1916 0.0369 0.0406 270 LYS A CA 2054 C C . LYS A 270 ? 0.7543 0.5868 0.5820 -0.1688 0.0336 0.0369 270 LYS A C 2055 O O . LYS A 270 ? 0.7887 0.6030 0.6018 -0.1557 0.0283 0.0431 270 LYS A O 2056 C CB . LYS A 270 ? 0.8047 0.6221 0.6114 -0.2107 0.0494 0.0490 270 LYS A CB 2057 N N . PRO A 271 ? 0.6974 0.5703 0.5503 -0.1642 0.0359 0.0270 271 PRO A N 2058 C CA . PRO A 271 ? 0.6680 0.5619 0.5316 -0.1436 0.0325 0.0232 271 PRO A CA 2059 C C . PRO A 271 ? 0.6804 0.5754 0.5310 -0.1367 0.0353 0.0308 271 PRO A C 2060 O O . PRO A 271 ? 0.6779 0.5686 0.5264 -0.1198 0.0288 0.0310 271 PRO A O 2061 C CB . PRO A 271 ? 0.6331 0.5711 0.5224 -0.1456 0.0375 0.0141 271 PRO A CB 2062 C CG . PRO A 271 ? 0.6455 0.5823 0.5405 -0.1634 0.0392 0.0102 271 PRO A CG 2063 C CD . PRO A 271 ? 0.6851 0.5872 0.5573 -0.1788 0.0419 0.0196 271 PRO A CD 2064 N N . GLN A 272 ? 0.7075 0.6095 0.5495 -0.1505 0.0452 0.0365 272 GLN A N 2065 C CA . GLN A 272 ? 0.7109 0.6170 0.5397 -0.1455 0.0493 0.0425 272 GLN A CA 2066 C C . GLN A 272 ? 0.7447 0.6111 0.5463 -0.1390 0.0413 0.0521 272 GLN A C 2067 O O . GLN A 272 ? 0.7442 0.6119 0.5364 -0.1286 0.0397 0.0550 272 GLN A O 2068 C CB . GLN A 272 ? 0.7220 0.6461 0.5475 -0.1631 0.0632 0.0455 272 GLN A CB 2069 C CG . GLN A 272 ? 0.7244 0.6643 0.5417 -0.1574 0.0697 0.0477 272 GLN A CG 2070 C CD . GLN A 272 ? 0.6837 0.6528 0.5214 -0.1393 0.0675 0.0386 272 GLN A CD 2071 O OE1 . GLN A 272 ? 0.6668 0.6589 0.5292 -0.1361 0.0665 0.0302 272 GLN A OE1 2072 N NE2 . GLN A 272 ? 0.6718 0.6385 0.4978 -0.1278 0.0661 0.0405 272 GLN A NE2 2073 N N . GLU A 273 ? 0.7787 0.6093 0.5677 -0.1445 0.0353 0.0567 273 GLU A N 2074 C CA . GLU A 273 ? 0.7995 0.5916 0.5645 -0.1361 0.0256 0.0656 273 GLU A CA 2075 C C . GLU A 273 ? 0.7734 0.5678 0.5490 -0.1133 0.0144 0.0600 273 GLU A C 2076 O O . GLU A 273 ? 0.7941 0.5742 0.5555 -0.1024 0.0074 0.0655 273 GLU A O 2077 C CB . GLU A 273 ? 0.8457 0.5971 0.5958 -0.1466 0.0216 0.0711 273 GLU A CB 2078 C CG . GLU A 273 ? 0.8820 0.6275 0.6187 -0.1715 0.0329 0.0783 273 GLU A CG 2079 C CD . GLU A 273 ? 0.9179 0.6256 0.6445 -0.1844 0.0297 0.0814 273 GLU A CD 2080 O OE1 . GLU A 273 ? 0.9458 0.6098 0.6452 -0.1844 0.0232 0.0924 273 GLU A OE1 2081 O OE2 . GLU A 273 ? 0.9018 0.6230 0.6472 -0.1947 0.0332 0.0727 273 GLU A OE2 2082 N N . LEU A 274 ? 0.7435 0.5574 0.5439 -0.1069 0.0126 0.0490 274 LEU A N 2083 C CA . LEU A 274 ? 0.7210 0.5433 0.5340 -0.0870 0.0041 0.0428 274 LEU A CA 2084 C C . LEU A 274 ? 0.6881 0.5399 0.5077 -0.0792 0.0074 0.0411 274 LEU A C 2085 O O . LEU A 274 ? 0.6748 0.5244 0.4921 -0.0655 0.0004 0.0417 274 LEU A O 2086 C CB . LEU A 274 ? 0.7022 0.5369 0.5373 -0.0839 0.0024 0.0318 274 LEU A CB 2087 C CG . LEU A 274 ? 0.7282 0.5321 0.5596 -0.0815 -0.0054 0.0298 274 LEU A CG 2088 C CD1 . LEU A 274 ? 0.7745 0.5437 0.5848 -0.0961 -0.0046 0.0382 274 LEU A CD1 2089 C CD2 . LEU A 274 ? 0.7195 0.5407 0.5712 -0.0824 -0.0045 0.0182 274 LEU A CD2 2090 N N . ILE A 275 ? 0.6676 0.5473 0.4965 -0.0880 0.0178 0.0383 275 ILE A N 2091 C CA . ILE A 275 ? 0.6420 0.5483 0.4769 -0.0812 0.0218 0.0358 275 ILE A CA 2092 C C . ILE A 275 ? 0.6430 0.5364 0.4543 -0.0805 0.0219 0.0438 275 ILE A C 2093 O O . ILE A 275 ? 0.6327 0.5340 0.4439 -0.0694 0.0188 0.0422 275 ILE A O 2094 C CB . ILE A 275 ? 0.6317 0.5702 0.4820 -0.0901 0.0329 0.0307 275 ILE A CB 2095 C CG1 . ILE A 275 ? 0.6033 0.5586 0.4775 -0.0875 0.0307 0.0219 275 ILE A CG1 2096 C CG2 . ILE A 275 ? 0.6191 0.5798 0.4712 -0.0838 0.0380 0.0289 275 ILE A CG2 2097 C CD1 . ILE A 275 ? 0.5931 0.5735 0.4814 -0.0999 0.0394 0.0179 275 ILE A CD1 2098 N N . ASP A 276 ? 0.6668 0.5391 0.4566 -0.0929 0.0251 0.0526 276 ASP A N 2099 C CA . ASP A 276 ? 0.6849 0.5442 0.4486 -0.0935 0.0254 0.0610 276 ASP A CA 2100 C C . ASP A 276 ? 0.6990 0.5391 0.4521 -0.0784 0.0119 0.0640 276 ASP A C 2101 O O . ASP A 276 ? 0.7252 0.5644 0.4621 -0.0748 0.0109 0.0674 276 ASP A O 2102 C CB . ASP A 276 ? 0.7154 0.5510 0.4554 -0.1108 0.0307 0.0713 276 ASP A CB 2103 C CG . ASP A 276 ? 0.7095 0.5697 0.4542 -0.1271 0.0465 0.0697 276 ASP A CG 2104 O OD1 . ASP A 276 ? 0.6825 0.5775 0.4464 -0.1229 0.0529 0.0610 276 ASP A OD1 2105 O OD2 . ASP A 276 ? 0.7199 0.5644 0.4491 -0.1440 0.0524 0.0772 276 ASP A OD2 2106 N N . VAL A 277 ? 0.6903 0.5166 0.4523 -0.0694 0.0016 0.0620 277 VAL A N 2107 C CA . VAL A 277 ? 0.6915 0.5021 0.4469 -0.0545 -0.0119 0.0642 277 VAL A CA 2108 C C . VAL A 277 ? 0.6666 0.4965 0.4477 -0.0401 -0.0176 0.0541 277 VAL A C 2109 O O . VAL A 277 ? 0.6740 0.4956 0.4549 -0.0274 -0.0287 0.0543 277 VAL A O 2110 C CB . VAL A 277 ? 0.7256 0.4978 0.4646 -0.0545 -0.0207 0.0722 277 VAL A CB 2111 C CG1 . VAL A 277 ? 0.7704 0.5206 0.4797 -0.0697 -0.0153 0.0841 277 VAL A CG1 2112 C CG2 . VAL A 277 ? 0.7193 0.4861 0.4750 -0.0560 -0.0210 0.0665 277 VAL A CG2 2113 N N . GLU A 278 ? 0.6406 0.4974 0.4436 -0.0422 -0.0101 0.0457 278 GLU A N 2114 C CA . GLU A 278 ? 0.6214 0.4966 0.4479 -0.0309 -0.0138 0.0366 278 GLU A CA 2115 C C . GLU A 278 ? 0.6137 0.4939 0.4396 -0.0190 -0.0212 0.0359 278 GLU A C 2116 O O . GLU A 278 ? 0.6112 0.4896 0.4462 -0.0084 -0.0297 0.0329 278 GLU A O 2117 C CB . GLU A 278 ? 0.6126 0.5168 0.4575 -0.0357 -0.0041 0.0295 278 GLU A CB 2118 C CG . GLU A 278 ? 0.6040 0.5288 0.4694 -0.0250 -0.0067 0.0216 278 GLU A CG 2119 C CD . GLU A 278 ? 0.6016 0.5508 0.4849 -0.0285 0.0005 0.0152 278 GLU A CD 2120 O OE1 . GLU A 278 ? 0.6115 0.5676 0.4946 -0.0388 0.0082 0.0158 278 GLU A OE1 2121 O OE2 . GLU A 278 ? 0.6627 0.6252 0.5609 -0.0207 -0.0019 0.0097 278 GLU A OE2 2122 N N . TRP A 279 ? 0.6456 0.5328 0.4605 -0.0213 -0.0176 0.0380 279 TRP A N 2123 C CA . TRP A 279 ? 0.6546 0.5488 0.4690 -0.0121 -0.0239 0.0361 279 TRP A CA 2124 C C . TRP A 279 ? 0.6780 0.5513 0.4774 -0.0054 -0.0362 0.0419 279 TRP A C 2125 O O . TRP A 279 ? 0.6861 0.5662 0.4900 0.0035 -0.0440 0.0392 279 TRP A O 2126 C CB . TRP A 279 ? 0.6795 0.5846 0.4836 -0.0170 -0.0163 0.0358 279 TRP A CB 2127 C CG . TRP A 279 ? 0.6822 0.6098 0.5027 -0.0207 -0.0057 0.0295 279 TRP A CG 2128 C CD1 . TRP A 279 ? 0.6957 0.6298 0.5153 -0.0309 0.0051 0.0302 279 TRP A CD1 2129 C CD2 . TRP A 279 ? 0.6667 0.6141 0.5075 -0.0142 -0.0053 0.0217 279 TRP A CD2 2130 N NE1 . TRP A 279 ? 0.6922 0.6499 0.5310 -0.0295 0.0114 0.0230 279 TRP A NE1 2131 C CE2 . TRP A 279 ? 0.6723 0.6365 0.5231 -0.0193 0.0051 0.0182 279 TRP A CE2 2132 C CE3 . TRP A 279 ? 0.6803 0.6329 0.5318 -0.0050 -0.0127 0.0176 279 TRP A CE3 2133 C CZ2 . TRP A 279 ? 0.6757 0.6589 0.5448 -0.0145 0.0074 0.0116 279 TRP A CZ2 2134 C CZ3 . TRP A 279 ? 0.6984 0.6693 0.5675 -0.0020 -0.0093 0.0112 279 TRP A CZ3 2135 C CH2 . TRP A 279 ? 0.6743 0.6589 0.5510 -0.0062 0.0003 0.0086 279 TRP A CH2 2136 N N . ASN A 280 ? 0.6953 0.5431 0.4767 -0.0097 -0.0385 0.0502 280 ASN A N 2137 C CA . ASN A 280 ? 0.7213 0.5464 0.4869 -0.0021 -0.0516 0.0569 280 ASN A CA 2138 C C . ASN A 280 ? 0.7087 0.5345 0.4928 0.0117 -0.0626 0.0522 280 ASN A C 2139 O O . ASN A 280 ? 0.7470 0.5621 0.5235 0.0211 -0.0748 0.0557 280 ASN A O 2140 C CB . ASN A 280 ? 0.7662 0.5598 0.5082 -0.0100 -0.0517 0.0675 280 ASN A CB 2141 C CG . ASN A 280 ? 0.7876 0.5780 0.5064 -0.0240 -0.0416 0.0740 280 ASN A CG 2142 O OD1 . ASN A 280 ? 0.7946 0.6053 0.5130 -0.0264 -0.0353 0.0704 280 ASN A OD1 2143 N ND2 . ASN A 280 ? 0.8157 0.5795 0.5141 -0.0337 -0.0398 0.0835 280 ASN A ND2 2144 N N . VAL A 281 ? 0.6824 0.5216 0.4904 0.0134 -0.0585 0.0441 281 VAL A N 2145 C CA . VAL A 281 ? 0.6822 0.5226 0.5078 0.0261 -0.0672 0.0388 281 VAL A CA 2146 C C . VAL A 281 ? 0.6588 0.5256 0.5036 0.0348 -0.0709 0.0314 281 VAL A C 2147 O O . VAL A 281 ? 0.6393 0.5104 0.4990 0.0457 -0.0782 0.0269 281 VAL A O 2148 C CB . VAL A 281 ? 0.6783 0.5184 0.5183 0.0239 -0.0616 0.0332 281 VAL A CB 2149 C CG1 . VAL A 281 ? 0.7189 0.5345 0.5414 0.0123 -0.0568 0.0398 281 VAL A CG1 2150 C CG2 . VAL A 281 ? 0.6462 0.5156 0.5058 0.0200 -0.0520 0.0250 281 VAL A CG2 2151 N N . LEU A 282 ? 0.6507 0.5352 0.4957 0.0299 -0.0656 0.0296 282 LEU A N 2152 C CA . LEU A 282 ? 0.6220 0.5291 0.4835 0.0360 -0.0690 0.0230 282 LEU A CA 2153 C C . LEU A 282 ? 0.6451 0.5465 0.5026 0.0459 -0.0832 0.0252 282 LEU A C 2154 O O . LEU A 282 ? 0.6708 0.5548 0.5059 0.0452 -0.0888 0.0327 282 LEU A O 2155 C CB . LEU A 282 ? 0.5928 0.5133 0.4504 0.0292 -0.0622 0.0213 282 LEU A CB 2156 C CG . LEU A 282 ? 0.5711 0.5046 0.4382 0.0221 -0.0495 0.0174 282 LEU A CG 2157 C CD1 . LEU A 282 ? 0.5717 0.5129 0.4304 0.0171 -0.0441 0.0165 282 LEU A CD1 2158 C CD2 . LEU A 282 ? 0.5454 0.4964 0.4369 0.0260 -0.0481 0.0102 282 LEU A CD2 2159 N N . PRO A 283 ? 0.6484 0.5655 0.5274 0.0550 -0.0891 0.0188 283 PRO A N 2160 C CA . PRO A 283 ? 0.6660 0.5808 0.5445 0.0655 -0.1036 0.0202 283 PRO A CA 2161 C C . PRO A 283 ? 0.6816 0.6076 0.5544 0.0641 -0.1093 0.0200 283 PRO A C 2162 O O . PRO A 283 ? 0.6750 0.5987 0.5439 0.0719 -0.1225 0.0220 283 PRO A O 2163 C CB . PRO A 283 ? 0.6505 0.5831 0.5574 0.0747 -0.1056 0.0118 283 PRO A CB 2164 C CG . PRO A 283 ? 0.6285 0.5804 0.5497 0.0668 -0.0930 0.0055 283 PRO A CG 2165 C CD . PRO A 283 ? 0.6230 0.5610 0.5274 0.0561 -0.0829 0.0102 283 PRO A CD 2166 N N . PHE A 284 ? 0.6890 0.6266 0.5614 0.0549 -0.1002 0.0169 284 PHE A N 2167 C CA . PHE A 284 ? 0.7002 0.6474 0.5672 0.0526 -0.1048 0.0149 284 PHE A CA 2168 C C . PHE A 284 ? 0.6915 0.6305 0.5363 0.0428 -0.0966 0.0175 284 PHE A C 2169 O O . PHE A 284 ? 0.6767 0.6112 0.5183 0.0367 -0.0848 0.0187 284 PHE A O 2170 C CB . PHE A 284 ? 0.7077 0.6806 0.6001 0.0520 -0.1026 0.0058 284 PHE A CB 2171 C CG . PHE A 284 ? 0.7365 0.7236 0.6526 0.0612 -0.1101 0.0016 284 PHE A CG 2172 C CD1 . PHE A 284 ? 0.7665 0.7558 0.6831 0.0695 -0.1250 0.0024 284 PHE A CD1 2173 C CD2 . PHE A 284 ? 0.7552 0.7554 0.6934 0.0619 -0.1024 -0.0036 284 PHE A CD2 2174 C CE1 . PHE A 284 ? 0.7759 0.7817 0.7170 0.0791 -0.1316 -0.0025 284 PHE A CE1 2175 C CE2 . PHE A 284 ? 0.7722 0.7878 0.7328 0.0706 -0.1081 -0.0085 284 PHE A CE2 2176 C CZ . PHE A 284 ? 0.7877 0.8071 0.7511 0.0795 -0.1224 -0.0082 284 PHE A CZ 2177 N N . ASP A 285 ? 0.7042 0.6430 0.5345 0.0415 -0.1031 0.0176 285 ASP A N 2178 C CA . ASP A 285 ? 0.6908 0.6270 0.5032 0.0331 -0.0952 0.0168 285 ASP A CA 2179 C C . ASP A 285 ? 0.6448 0.5995 0.4774 0.0300 -0.0880 0.0078 285 ASP A C 2180 O O . ASP A 285 ? 0.6197 0.5866 0.4635 0.0314 -0.0947 0.0022 285 ASP A O 2181 C CB . ASP A 285 ? 0.7164 0.6457 0.5058 0.0336 -0.1061 0.0188 285 ASP A CB 2182 C CG . ASP A 285 ? 0.7387 0.6617 0.5039 0.0256 -0.0977 0.0185 285 ASP A CG 2183 O OD1 . ASP A 285 ? 0.7299 0.6535 0.4964 0.0203 -0.0834 0.0175 285 ASP A OD1 2184 O OD2 . ASP A 285 ? 0.7383 0.6567 0.4830 0.0251 -0.1059 0.0187 285 ASP A OD2 2185 N N . SER A 286 ? 0.6325 0.5889 0.4700 0.0256 -0.0748 0.0067 286 SER A N 2186 C CA . SER A 286 ? 0.6168 0.5882 0.4747 0.0241 -0.0685 -0.0001 286 SER A CA 2187 C C . SER A 286 ? 0.6068 0.5782 0.4605 0.0190 -0.0554 -0.0018 286 SER A C 2188 O O . SER A 286 ? 0.6132 0.5759 0.4514 0.0161 -0.0495 0.0021 286 SER A O 2189 C CB . SER A 286 ? 0.6159 0.5955 0.4963 0.0279 -0.0681 -0.0006 286 SER A CB 2190 O OG . SER A 286 ? 0.6229 0.5948 0.5005 0.0267 -0.0608 0.0034 286 SER A OG 2191 N N . ILE A 287 ? 0.5812 0.5630 0.4495 0.0180 -0.0511 -0.0073 287 ILE A N 2192 C CA . ILE A 287 ? 0.5665 0.5507 0.4370 0.0156 -0.0394 -0.0089 287 ILE A CA 2193 C C . ILE A 287 ? 0.5254 0.5205 0.4179 0.0166 -0.0364 -0.0108 287 ILE A C 2194 O O . ILE A 287 ? 0.5197 0.5213 0.4248 0.0179 -0.0421 -0.0127 287 ILE A O 2195 C CB . ILE A 287 ? 0.5662 0.5480 0.4259 0.0137 -0.0359 -0.0138 287 ILE A CB 2196 C CG1 . ILE A 287 ? 0.5747 0.5590 0.4402 0.0134 -0.0432 -0.0190 287 ILE A CG1 2197 C CG2 . ILE A 287 ? 0.5965 0.5684 0.4316 0.0119 -0.0355 -0.0119 287 ILE A CG2 2198 C CD1 . ILE A 287 ? 0.5847 0.5651 0.4440 0.0118 -0.0388 -0.0252 287 ILE A CD1 2199 N N . PHE A 288 ? 0.4976 0.4958 0.3940 0.0158 -0.0273 -0.0105 288 PHE A N 2200 C CA . PHE A 288 ? 0.4807 0.4883 0.3946 0.0166 -0.0240 -0.0114 288 PHE A CA 2201 C C . PHE A 288 ? 0.4797 0.4901 0.4030 0.0183 -0.0280 -0.0094 288 PHE A C 2202 O O . PHE A 288 ? 0.4751 0.4939 0.4123 0.0193 -0.0292 -0.0113 288 PHE A O 2203 C CB . PHE A 288 ? 0.4798 0.4914 0.4018 0.0163 -0.0251 -0.0152 288 PHE A CB 2204 C CG . PHE A 288 ? 0.4704 0.4875 0.4016 0.0167 -0.0187 -0.0156 288 PHE A CG 2205 C CD1 . PHE A 288 ? 0.4743 0.4986 0.4148 0.0173 -0.0157 -0.0136 288 PHE A CD1 2206 C CD2 . PHE A 288 ? 0.4658 0.4793 0.3949 0.0167 -0.0164 -0.0182 288 PHE A CD2 2207 C CE1 . PHE A 288 ? 0.4566 0.4862 0.4039 0.0180 -0.0110 -0.0135 288 PHE A CE1 2208 C CE2 . PHE A 288 ? 0.4643 0.4811 0.4004 0.0181 -0.0117 -0.0177 288 PHE A CE2 2209 C CZ . PHE A 288 ? 0.4545 0.4803 0.3996 0.0188 -0.0093 -0.0150 288 PHE A CZ 2210 N N . ARG A 289 ? 0.5035 0.5058 0.4180 0.0184 -0.0298 -0.0058 289 ARG A N 2211 C CA . ARG A 289 ? 0.5124 0.5138 0.4341 0.0209 -0.0330 -0.0044 289 ARG A CA 2212 C C . ARG A 289 ? 0.5360 0.5294 0.4500 0.0179 -0.0283 -0.0009 289 ARG A C 2213 O O . ARG A 289 ? 0.5363 0.5217 0.4351 0.0144 -0.0257 0.0021 289 ARG A O 2214 C CB . ARG A 289 ? 0.5315 0.5274 0.4502 0.0251 -0.0432 -0.0033 289 ARG A CB 2215 C CG . ARG A 289 ? 0.5466 0.5533 0.4756 0.0269 -0.0486 -0.0074 289 ARG A CG 2216 C CD . ARG A 289 ? 0.5414 0.5622 0.4906 0.0282 -0.0462 -0.0111 289 ARG A CD 2217 N NE . ARG A 289 ? 0.5377 0.5702 0.4976 0.0282 -0.0508 -0.0149 289 ARG A NE 2218 C CZ . ARG A 289 ? 0.5227 0.5604 0.4852 0.0234 -0.0477 -0.0171 289 ARG A CZ 2219 N NH1 . ARG A 289 ? 0.5378 0.5703 0.4933 0.0202 -0.0404 -0.0162 289 ARG A NH1 2220 N NH2 . ARG A 289 ? 0.5260 0.5742 0.4988 0.0219 -0.0522 -0.0205 289 ARG A NH2 2221 N N . PHE A 290 ? 0.5355 0.5314 0.4596 0.0184 -0.0267 -0.0018 290 PHE A N 2222 C CA . PHE A 290 ? 0.5230 0.5128 0.4424 0.0138 -0.0218 0.0004 290 PHE A CA 2223 C C . PHE A 290 ? 0.5115 0.4913 0.4328 0.0163 -0.0265 0.0009 290 PHE A C 2224 O O . PHE A 290 ? 0.4697 0.4539 0.4016 0.0224 -0.0311 -0.0024 290 PHE A O 2225 C CB . PHE A 290 ? 0.5142 0.5178 0.4436 0.0110 -0.0145 -0.0025 290 PHE A CB 2226 C CG . PHE A 290 ? 0.5104 0.5238 0.4421 0.0119 -0.0117 -0.0043 290 PHE A CG 2227 C CD1 . PHE A 290 ? 0.5214 0.5326 0.4423 0.0097 -0.0082 -0.0031 290 PHE A CD1 2228 C CD2 . PHE A 290 ? 0.4961 0.5194 0.4394 0.0149 -0.0124 -0.0073 290 PHE A CD2 2229 C CE1 . PHE A 290 ? 0.5230 0.5403 0.4451 0.0115 -0.0060 -0.0057 290 PHE A CE1 2230 C CE2 . PHE A 290 ? 0.4937 0.5217 0.4375 0.0156 -0.0103 -0.0086 290 PHE A CE2 2231 C CZ . PHE A 290 ? 0.5083 0.5327 0.4418 0.0145 -0.0074 -0.0082 290 PHE A CZ 2232 N N . SER A 291 ? 0.5324 0.4985 0.4432 0.0114 -0.0248 0.0046 291 SER A N 2233 C CA . SER A 291 ? 0.5424 0.4908 0.4490 0.0142 -0.0307 0.0064 291 SER A CA 2234 C C . SER A 291 ? 0.5245 0.4772 0.4452 0.0171 -0.0306 0.0006 291 SER A C 2235 O O . SER A 291 ? 0.5257 0.4775 0.4536 0.0254 -0.0365 -0.0024 291 SER A O 2236 C CB . SER A 291 ? 0.5705 0.4999 0.4593 0.0064 -0.0287 0.0128 291 SER A CB 2237 O OG . SER A 291 ? 0.6000 0.5214 0.4724 0.0061 -0.0314 0.0185 291 SER A OG 2238 N N . PHE A 292 ? 0.5116 0.4705 0.4365 0.0104 -0.0239 -0.0017 292 PHE A N 2239 C CA . PHE A 292 ? 0.4859 0.4480 0.4214 0.0121 -0.0235 -0.0078 292 PHE A CA 2240 C C . PHE A 292 ? 0.4655 0.4512 0.4140 0.0123 -0.0190 -0.0125 292 PHE A C 2241 O O . PHE A 292 ? 0.4702 0.4657 0.4195 0.0060 -0.0136 -0.0121 292 PHE A O 2242 C CB . PHE A 292 ? 0.5028 0.4512 0.4315 0.0037 -0.0210 -0.0072 292 PHE A CB 2243 C CG . PHE A 292 ? 0.5355 0.4573 0.4484 0.0022 -0.0251 -0.0009 292 PHE A CG 2244 C CD1 . PHE A 292 ? 0.5496 0.4530 0.4603 0.0101 -0.0324 -0.0018 292 PHE A CD1 2245 C CD2 . PHE A 292 ? 0.5509 0.4661 0.4501 -0.0063 -0.0218 0.0062 292 PHE A CD2 2246 C CE1 . PHE A 292 ? 0.5857 0.4616 0.4797 0.0096 -0.0373 0.0053 292 PHE A CE1 2247 C CE2 . PHE A 292 ? 0.5770 0.4660 0.4586 -0.0083 -0.0257 0.0134 292 PHE A CE2 2248 C CZ . PHE A 292 ? 0.5977 0.4656 0.4760 -0.0002 -0.0340 0.0135 292 PHE A CZ 2249 N N . VAL A 293 ? 0.4503 0.4450 0.4087 0.0196 -0.0215 -0.0167 293 VAL A N 2250 C CA . VAL A 293 ? 0.4311 0.4459 0.3999 0.0201 -0.0179 -0.0202 293 VAL A CA 2251 C C . VAL A 293 ? 0.4279 0.4474 0.4050 0.0242 -0.0182 -0.0270 293 VAL A C 2252 O O . VAL A 293 ? 0.4546 0.4617 0.4306 0.0282 -0.0217 -0.0295 293 VAL A O 2253 C CB . VAL A 293 ? 0.4263 0.4497 0.3981 0.0233 -0.0194 -0.0184 293 VAL A CB 2254 C CG1 . VAL A 293 ? 0.4312 0.4492 0.3931 0.0196 -0.0187 -0.0132 293 VAL A CG1 2255 C CG2 . VAL A 293 ? 0.4339 0.4547 0.4099 0.0304 -0.0256 -0.0200 293 VAL A CG2 2256 N N . PRO A 294 ? 0.4161 0.4523 0.4001 0.0235 -0.0144 -0.0302 294 PRO A N 2257 C CA . PRO A 294 ? 0.4270 0.4698 0.4175 0.0271 -0.0135 -0.0372 294 PRO A CA 2258 C C . PRO A 294 ? 0.4472 0.4880 0.4440 0.0356 -0.0174 -0.0406 294 PRO A C 2259 O O . PRO A 294 ? 0.4595 0.5052 0.4602 0.0383 -0.0198 -0.0380 294 PRO A O 2260 C CB . PRO A 294 ? 0.4046 0.4659 0.3995 0.0252 -0.0094 -0.0372 294 PRO A CB 2261 C CG . PRO A 294 ? 0.4021 0.4638 0.3919 0.0196 -0.0078 -0.0318 294 PRO A CG 2262 C CD . PRO A 294 ? 0.4038 0.4518 0.3879 0.0189 -0.0104 -0.0275 294 PRO A CD 2263 N N . VAL A 295 ? 0.4594 0.4934 0.4576 0.0399 -0.0184 -0.0471 295 VAL A N 2264 C CA . VAL A 295 ? 0.4911 0.5272 0.4982 0.0500 -0.0216 -0.0523 295 VAL A CA 2265 C C . VAL A 295 ? 0.4977 0.5554 0.5150 0.0522 -0.0164 -0.0596 295 VAL A C 2266 O O . VAL A 295 ? 0.5134 0.5772 0.5275 0.0474 -0.0113 -0.0627 295 VAL A O 2267 C CB . VAL A 295 ? 0.5235 0.5381 0.5268 0.0562 -0.0260 -0.0564 295 VAL A CB 2268 C CG1 . VAL A 295 ? 0.5520 0.5454 0.5462 0.0569 -0.0327 -0.0486 295 VAL A CG1 2269 C CG2 . VAL A 295 ? 0.5479 0.5535 0.5442 0.0507 -0.0227 -0.0610 295 VAL A CG2 2270 N N . ILE A 296 ? 0.4924 0.5629 0.5216 0.0590 -0.0177 -0.0622 296 ILE A N 2271 C CA . ILE A 296 ? 0.4981 0.5909 0.5378 0.0609 -0.0119 -0.0694 296 ILE A CA 2272 C C . ILE A 296 ? 0.5289 0.6168 0.5723 0.0702 -0.0122 -0.0797 296 ILE A C 2273 O O . ILE A 296 ? 0.5344 0.6248 0.5884 0.0805 -0.0162 -0.0839 296 ILE A O 2274 C CB . ILE A 296 ? 0.4868 0.5985 0.5397 0.0625 -0.0126 -0.0682 296 ILE A CB 2275 C CG1 . ILE A 296 ? 0.4787 0.5905 0.5261 0.0535 -0.0129 -0.0587 296 ILE A CG1 2276 C CG2 . ILE A 296 ? 0.4905 0.6272 0.5542 0.0628 -0.0051 -0.0754 296 ILE A CG2 2277 C CD1 . ILE A 296 ? 0.4816 0.5999 0.5221 0.0444 -0.0058 -0.0562 296 ILE A CD1 2278 N N . ASP A 297 ? 0.5604 0.6415 0.5949 0.0669 -0.0085 -0.0843 297 ASP A N 2279 C CA . ASP A 297 ? 0.5858 0.6512 0.6181 0.0743 -0.0104 -0.0932 297 ASP A CA 2280 C C . ASP A 297 ? 0.6109 0.6928 0.6504 0.0801 -0.0042 -0.1057 297 ASP A C 2281 O O . ASP A 297 ? 0.6412 0.7107 0.6798 0.0880 -0.0053 -0.1152 297 ASP A O 2282 C CB . ASP A 297 ? 0.5908 0.6352 0.6077 0.0661 -0.0111 -0.0916 297 ASP A CB 2283 C CG . ASP A 297 ? 0.5783 0.6364 0.5891 0.0560 -0.0049 -0.0920 297 ASP A CG 2284 O OD1 . ASP A 297 ? 0.5507 0.6315 0.5666 0.0543 0.0001 -0.0910 297 ASP A OD1 2285 O OD2 . ASP A 297 ? 0.5773 0.6233 0.5778 0.0495 -0.0053 -0.0930 297 ASP A OD2 2286 N N . GLY A 298 ? 0.6170 0.7256 0.6623 0.0761 0.0028 -0.1061 298 GLY A N 2287 C CA . GLY A 298 ? 0.6413 0.7681 0.6912 0.0797 0.0105 -0.1178 298 GLY A CA 2288 C C . GLY A 298 ? 0.6658 0.7879 0.7005 0.0731 0.0149 -0.1227 298 GLY A C 2289 O O . GLY A 298 ? 0.6974 0.8343 0.7321 0.0748 0.0220 -0.1324 298 GLY A O 2290 N N . GLU A 299 ? 0.6910 0.7942 0.7128 0.0654 0.0108 -0.1164 299 GLU A N 2291 C CA . GLU A 299 ? 0.6940 0.7930 0.7018 0.0584 0.0131 -0.1208 299 GLU A CA 2292 C C . GLU A 299 ? 0.6167 0.7264 0.6176 0.0472 0.0147 -0.1105 299 GLU A C 2293 O O . GLU A 299 ? 0.6014 0.7284 0.5979 0.0435 0.0205 -0.1120 299 GLU A O 2294 C CB . GLU A 299 ? 0.7819 0.8522 0.7816 0.0579 0.0068 -0.1230 299 GLU A CB 2295 C CG . GLU A 299 ? 0.9120 0.9670 0.9168 0.0702 0.0044 -0.1333 299 GLU A CG 2296 C CD . GLU A 299 ? 1.0232 1.0463 1.0174 0.0682 -0.0013 -0.1361 299 GLU A CD 2297 O OE1 . GLU A 299 ? 1.0651 1.0836 1.0482 0.0568 -0.0013 -0.1353 299 GLU A OE1 2298 O OE2 . GLU A 299 ? 1.0674 1.0699 1.0645 0.0778 -0.0062 -0.1391 299 GLU A OE2 2299 N N . PHE A 300 ? 0.5929 0.6922 0.5922 0.0424 0.0098 -0.0999 300 PHE A N 2300 C CA . PHE A 300 ? 0.5730 0.6816 0.5675 0.0340 0.0107 -0.0898 300 PHE A CA 2301 C C . PHE A 300 ? 0.5656 0.6934 0.5664 0.0342 0.0154 -0.0857 300 PHE A C 2302 O O . PHE A 300 ? 0.5248 0.6641 0.5193 0.0283 0.0187 -0.0815 300 PHE A O 2303 C CB . PHE A 300 ? 0.5532 0.6480 0.5472 0.0308 0.0053 -0.0804 300 PHE A CB 2304 C CG . PHE A 300 ? 0.5241 0.6246 0.5121 0.0230 0.0052 -0.0724 300 PHE A CG 2305 C CD1 . PHE A 300 ? 0.5073 0.6179 0.4976 0.0216 0.0067 -0.0642 300 PHE A CD1 2306 C CD2 . PHE A 300 ? 0.5106 0.6061 0.4914 0.0173 0.0030 -0.0735 300 PHE A CD2 2307 C CE1 . PHE A 300 ? 0.4861 0.6003 0.4712 0.0165 0.0059 -0.0571 300 PHE A CE1 2308 C CE2 . PHE A 300 ? 0.4862 0.5891 0.4636 0.0119 0.0021 -0.0665 300 PHE A CE2 2309 C CZ . PHE A 300 ? 0.4840 0.5956 0.4633 0.0124 0.0035 -0.0583 300 PHE A CZ 2310 N N . PHE A 301 ? 0.5689 0.6996 0.5819 0.0406 0.0151 -0.0868 301 PHE A N 2311 C CA . PHE A 301 ? 0.5413 0.6912 0.5630 0.0401 0.0196 -0.0845 301 PHE A CA 2312 C C . PHE A 301 ? 0.5443 0.7075 0.5761 0.0476 0.0240 -0.0958 301 PHE A C 2313 O O . PHE A 301 ? 0.5501 0.7075 0.5918 0.0565 0.0200 -0.1004 301 PHE A O 2314 C CB . PHE A 301 ? 0.5294 0.6752 0.5590 0.0407 0.0147 -0.0766 301 PHE A CB 2315 C CG . PHE A 301 ? 0.5322 0.6650 0.5529 0.0348 0.0107 -0.0667 301 PHE A CG 2316 C CD1 . PHE A 301 ? 0.5376 0.6766 0.5525 0.0276 0.0133 -0.0594 301 PHE A CD1 2317 C CD2 . PHE A 301 ? 0.5394 0.6536 0.5573 0.0367 0.0047 -0.0647 301 PHE A CD2 2318 C CE1 . PHE A 301 ? 0.5507 0.6793 0.5591 0.0239 0.0099 -0.0515 301 PHE A CE1 2319 C CE2 . PHE A 301 ? 0.5431 0.6485 0.5540 0.0314 0.0023 -0.0566 301 PHE A CE2 2320 C CZ . PHE A 301 ? 0.5389 0.6523 0.5460 0.0258 0.0049 -0.0505 301 PHE A CZ 2321 N N . PRO A 302 ? 0.5579 0.7392 0.5870 0.0446 0.0323 -0.1004 302 PRO A N 2322 C CA . PRO A 302 ? 0.5670 0.7626 0.6060 0.0527 0.0376 -0.1132 302 PRO A CA 2323 C C . PRO A 302 ? 0.5568 0.7641 0.6165 0.0594 0.0364 -0.1143 302 PRO A C 2324 O O . PRO A 302 ? 0.5671 0.7773 0.6379 0.0707 0.0359 -0.1248 302 PRO A O 2325 C CB . PRO A 302 ? 0.5665 0.7825 0.5978 0.0455 0.0478 -0.1149 302 PRO A CB 2326 C CG . PRO A 302 ? 0.5650 0.7769 0.5842 0.0343 0.0466 -0.1012 302 PRO A CG 2327 C CD . PRO A 302 ? 0.5505 0.7388 0.5656 0.0348 0.0369 -0.0951 302 PRO A CD 2328 N N . THR A 303 ? 0.5432 0.7571 0.6080 0.0530 0.0352 -0.1042 303 THR A N 2329 C CA . THR A 303 ? 0.5368 0.7633 0.6213 0.0577 0.0326 -0.1045 303 THR A CA 2330 C C . THR A 303 ? 0.4959 0.7106 0.5784 0.0520 0.0255 -0.0922 303 THR A C 2331 O O . THR A 303 ? 0.4958 0.6925 0.5632 0.0466 0.0229 -0.0848 303 THR A O 2332 C CB . THR A 303 ? 0.5501 0.8090 0.6472 0.0540 0.0425 -0.1088 303 THR A CB 2333 O OG1 . THR A 303 ? 0.5382 0.8016 0.6251 0.0398 0.0476 -0.0991 303 THR A OG1 2334 C CG2 . THR A 303 ? 0.5693 0.8416 0.6670 0.0599 0.0511 -0.1223 303 THR A CG2 2335 N N . SER A 304 ? 0.4823 0.7083 0.5802 0.0534 0.0223 -0.0909 304 SER A N 2336 C CA . SER A 304 ? 0.4721 0.6869 0.5675 0.0484 0.0154 -0.0807 304 SER A CA 2337 C C . SER A 304 ? 0.4645 0.6786 0.5483 0.0352 0.0202 -0.0720 304 SER A C 2338 O O . SER A 304 ? 0.4797 0.7100 0.5637 0.0287 0.0288 -0.0731 304 SER A O 2339 C CB . SER A 304 ? 0.4649 0.6962 0.5796 0.0508 0.0113 -0.0821 304 SER A CB 2340 O OG . SER A 304 ? 0.4600 0.7141 0.5821 0.0407 0.0189 -0.0813 304 SER A OG 2341 N N . LEU A 305 ? 0.4580 0.6530 0.5314 0.0316 0.0146 -0.0634 305 LEU A N 2342 C CA . LEU A 305 ? 0.4656 0.6560 0.5276 0.0211 0.0175 -0.0548 305 LEU A CA 2343 C C . LEU A 305 ? 0.4788 0.6875 0.5492 0.0127 0.0228 -0.0535 305 LEU A C 2344 O O . LEU A 305 ? 0.5166 0.7292 0.5786 0.0047 0.0296 -0.0499 305 LEU A O 2345 C CB . LEU A 305 ? 0.4600 0.6304 0.5140 0.0201 0.0105 -0.0473 305 LEU A CB 2346 C CG . LEU A 305 ? 0.4784 0.6299 0.5225 0.0252 0.0060 -0.0466 305 LEU A CG 2347 C CD1 . LEU A 305 ? 0.4807 0.6165 0.5157 0.0220 0.0019 -0.0389 305 LEU A CD1 2348 C CD2 . LEU A 305 ? 0.4798 0.6304 0.5147 0.0246 0.0105 -0.0488 305 LEU A CD2 2349 N N . GLU A 306 ? 0.4838 0.7037 0.5701 0.0139 0.0194 -0.0562 306 GLU A N 2350 C CA . GLU A 306 ? 0.4732 0.7102 0.5686 0.0038 0.0238 -0.0548 306 GLU A CA 2351 C C . GLU A 306 ? 0.4602 0.7204 0.5610 0.0002 0.0347 -0.0599 306 GLU A C 2352 O O . GLU A 306 ? 0.4526 0.7180 0.5481 -0.0116 0.0416 -0.0550 306 GLU A O 2353 C CB . GLU A 306 ? 0.4779 0.7254 0.5911 0.0060 0.0168 -0.0579 306 GLU A CB 2354 C CG . GLU A 306 ? 0.4984 0.7639 0.6224 -0.0065 0.0205 -0.0569 306 GLU A CG 2355 C CD . GLU A 306 ? 0.5355 0.7834 0.6430 -0.0192 0.0225 -0.0471 306 GLU A CD 2356 O OE1 . GLU A 306 ? 0.5558 0.7781 0.6467 -0.0168 0.0182 -0.0414 306 GLU A OE1 2357 O OE2 . GLU A 306 ? 0.5416 0.8011 0.6530 -0.0317 0.0285 -0.0452 306 GLU A OE2 2358 N N . SER A 307 ? 0.4506 0.7233 0.5606 0.0103 0.0366 -0.0696 307 SER A N 2359 C CA . SER A 307 ? 0.4680 0.7652 0.5833 0.0076 0.0481 -0.0761 307 SER A CA 2360 C C . SER A 307 ? 0.4665 0.7542 0.5593 0.0013 0.0551 -0.0716 307 SER A C 2361 O O . SER A 307 ? 0.4993 0.8024 0.5891 -0.0078 0.0651 -0.0711 307 SER A O 2362 C CB . SER A 307 ? 0.4652 0.7772 0.5956 0.0216 0.0485 -0.0891 307 SER A CB 2363 O OG . SER A 307 ? 0.4926 0.7828 0.6110 0.0314 0.0440 -0.0913 307 SER A OG 2364 N N . MET A 308 ? 0.4612 0.7244 0.5380 0.0057 0.0495 -0.0682 308 MET A N 2365 C CA . MET A 308 ? 0.4789 0.7322 0.5341 0.0003 0.0535 -0.0631 308 MET A CA 2366 C C . MET A 308 ? 0.4759 0.7241 0.5210 -0.0126 0.0558 -0.0513 308 MET A C 2367 O O . MET A 308 ? 0.4948 0.7472 0.5269 -0.0202 0.0630 -0.0477 308 MET A O 2368 C CB . MET A 308 ? 0.4840 0.7138 0.5272 0.0069 0.0459 -0.0616 308 MET A CB 2369 C CG . MET A 308 ? 0.4922 0.7219 0.5402 0.0181 0.0442 -0.0728 308 MET A CG 2370 S SD . MET A 308 ? 0.4928 0.6964 0.5256 0.0221 0.0368 -0.0711 308 MET A SD 2371 C CE . MET A 308 ? 0.5127 0.7196 0.5256 0.0146 0.0429 -0.0688 308 MET A CE 2372 N N . LEU A 309 ? 0.4627 0.7004 0.5123 -0.0150 0.0494 -0.0454 309 LEU A N 2373 C CA . LEU A 309 ? 0.4758 0.7043 0.5156 -0.0265 0.0506 -0.0347 309 LEU A CA 2374 C C . LEU A 309 ? 0.4927 0.7423 0.5399 -0.0378 0.0598 -0.0350 309 LEU A C 2375 O O . LEU A 309 ? 0.5328 0.7785 0.5657 -0.0482 0.0655 -0.0272 309 LEU A O 2376 C CB . LEU A 309 ? 0.4672 0.6787 0.5097 -0.0260 0.0416 -0.0301 309 LEU A CB 2377 C CG . LEU A 309 ? 0.4678 0.6570 0.4994 -0.0180 0.0340 -0.0272 309 LEU A CG 2378 C CD1 . LEU A 309 ? 0.4761 0.6526 0.5120 -0.0168 0.0262 -0.0251 309 LEU A CD1 2379 C CD2 . LEU A 309 ? 0.4675 0.6424 0.4794 -0.0210 0.0351 -0.0191 309 LEU A CD2 2380 N N . ASN A 310 ? 0.4892 0.7613 0.5584 -0.0358 0.0613 -0.0437 310 ASN A N 2381 C CA . ASN A 310 ? 0.5146 0.8127 0.5946 -0.0467 0.0712 -0.0458 310 ASN A CA 2382 C C . ASN A 310 ? 0.5226 0.8345 0.5925 -0.0501 0.0830 -0.0479 310 ASN A C 2383 O O . ASN A 310 ? 0.5443 0.8602 0.6047 -0.0638 0.0912 -0.0413 310 ASN A O 2384 C CB . ASN A 310 ? 0.5255 0.8492 0.6340 -0.0414 0.0698 -0.0563 310 ASN A CB 2385 C CG . ASN A 310 ? 0.5413 0.8649 0.6612 -0.0496 0.0643 -0.0528 310 ASN A CG 2386 O OD1 . ASN A 310 ? 0.5795 0.9186 0.7060 -0.0636 0.0710 -0.0510 310 ASN A OD1 2387 N ND2 . ASN A 310 ? 0.5423 0.8478 0.6629 -0.0421 0.0523 -0.0516 310 ASN A ND2 2388 N N . SER A 311 ? 0.5084 0.8260 0.5786 -0.0380 0.0838 -0.0571 311 SER A N 2389 C CA . SER A 311 ? 0.5182 0.8497 0.5778 -0.0398 0.0949 -0.0613 311 SER A CA 2390 C C . SER A 311 ? 0.5222 0.8342 0.5518 -0.0469 0.0964 -0.0505 311 SER A C 2391 O O . SER A 311 ? 0.5438 0.8668 0.5607 -0.0521 0.1061 -0.0514 311 SER A O 2392 C CB . SER A 311 ? 0.5278 0.8655 0.5935 -0.0242 0.0938 -0.0747 311 SER A CB 2393 O OG . SER A 311 ? 0.5305 0.8410 0.5860 -0.0153 0.0830 -0.0726 311 SER A OG 2394 N N . GLY A 312 ? 0.5108 0.7948 0.5287 -0.0464 0.0867 -0.0407 312 GLY A N 2395 C CA . GLY A 312 ? 0.5182 0.7833 0.5092 -0.0494 0.0855 -0.0313 312 GLY A CA 2396 C C . GLY A 312 ? 0.5089 0.7699 0.4915 -0.0383 0.0822 -0.0382 312 GLY A C 2397 O O . GLY A 312 ? 0.5124 0.7668 0.4733 -0.0403 0.0832 -0.0341 312 GLY A O 2398 N N . ASN A 313 ? 0.4720 0.7356 0.4708 -0.0270 0.0775 -0.0486 313 ASN A N 2399 C CA . ASN A 313 ? 0.4607 0.7180 0.4525 -0.0175 0.0739 -0.0558 313 ASN A CA 2400 C C . ASN A 313 ? 0.4584 0.6910 0.4411 -0.0146 0.0631 -0.0481 313 ASN A C 2401 O O . ASN A 313 ? 0.4630 0.6859 0.4561 -0.0076 0.0557 -0.0504 313 ASN A O 2402 C CB . ASN A 313 ? 0.4458 0.7130 0.4571 -0.0066 0.0733 -0.0697 313 ASN A CB 2403 C CG . ASN A 313 ? 0.4538 0.7144 0.4565 0.0016 0.0712 -0.0786 313 ASN A CG 2404 O OD1 . ASN A 313 ? 0.4736 0.7251 0.4566 -0.0014 0.0701 -0.0750 313 ASN A OD1 2405 N ND2 . ASN A 313 ? 0.4526 0.7170 0.4697 0.0120 0.0700 -0.0905 313 ASN A ND2 2406 N N . PHE A 314 ? 0.4621 0.6854 0.4248 -0.0201 0.0624 -0.0387 314 PHE A N 2407 C CA . PHE A 314 ? 0.4470 0.6506 0.4013 -0.0173 0.0528 -0.0317 314 PHE A CA 2408 C C . PHE A 314 ? 0.4517 0.6498 0.3831 -0.0221 0.0527 -0.0228 314 PHE A C 2409 O O . PHE A 314 ? 0.4400 0.6459 0.3604 -0.0296 0.0599 -0.0192 314 PHE A O 2410 C CB . PHE A 314 ? 0.4434 0.6345 0.4072 -0.0176 0.0475 -0.0246 314 PHE A CB 2411 C CG . PHE A 314 ? 0.4484 0.6414 0.4125 -0.0269 0.0522 -0.0171 314 PHE A CG 2412 C CD1 . PHE A 314 ? 0.4555 0.6372 0.4023 -0.0334 0.0521 -0.0054 314 PHE A CD1 2413 C CD2 . PHE A 314 ? 0.4448 0.6500 0.4265 -0.0294 0.0558 -0.0216 314 PHE A CD2 2414 C CE1 . PHE A 314 ? 0.4571 0.6369 0.4027 -0.0434 0.0564 0.0018 314 PHE A CE1 2415 C CE2 . PHE A 314 ? 0.4486 0.6554 0.4311 -0.0400 0.0600 -0.0150 314 PHE A CE2 2416 C CZ . PHE A 314 ? 0.4566 0.6495 0.4204 -0.0476 0.0607 -0.0032 314 PHE A CZ 2417 N N . LYS A 315 ? 0.4576 0.6430 0.3816 -0.0179 0.0442 -0.0191 315 LYS A N 2418 C CA . LYS A 315 ? 0.4717 0.6522 0.3747 -0.0205 0.0417 -0.0107 315 LYS A CA 2419 C C . LYS A 315 ? 0.4867 0.6580 0.3820 -0.0270 0.0432 0.0024 315 LYS A C 2420 O O . LYS A 315 ? 0.4549 0.6161 0.3604 -0.0266 0.0406 0.0066 315 LYS A O 2421 C CB . LYS A 315 ? 0.4649 0.6362 0.3661 -0.0142 0.0316 -0.0095 315 LYS A CB 2422 C CG . LYS A 315 ? 0.4772 0.6466 0.3577 -0.0149 0.0273 -0.0027 315 LYS A CG 2423 C CD . LYS A 315 ? 0.4758 0.6388 0.3595 -0.0086 0.0170 -0.0012 315 LYS A CD 2424 C CE . LYS A 315 ? 0.4900 0.6516 0.3552 -0.0078 0.0106 0.0069 315 LYS A CE 2425 N NZ . LYS A 315 ? 0.4999 0.6733 0.3549 -0.0086 0.0095 -0.0012 315 LYS A NZ 2426 N N . LYS A 316 ? 0.5233 0.6966 0.3988 -0.0333 0.0472 0.0088 316 LYS A N 2427 C CA . LYS A 316 ? 0.5439 0.7056 0.4081 -0.0409 0.0490 0.0222 316 LYS A CA 2428 C C . LYS A 316 ? 0.5425 0.6887 0.3871 -0.0377 0.0403 0.0334 316 LYS A C 2429 O O . LYS A 316 ? 0.5577 0.7084 0.3841 -0.0378 0.0393 0.0347 316 LYS A O 2430 C CB . LYS A 316 ? 0.5740 0.7488 0.4297 -0.0516 0.0609 0.0224 316 LYS A CB 2431 C CG . LYS A 316 ? 0.5956 0.7875 0.4747 -0.0537 0.0688 0.0116 316 LYS A CG 2432 C CD . LYS A 316 ? 0.6557 0.8687 0.5296 -0.0621 0.0818 0.0069 316 LYS A CD 2433 C CE . LYS A 316 ? 0.6628 0.8974 0.5628 -0.0599 0.0883 -0.0072 316 LYS A CE 2434 N NZ . LYS A 316 ? 0.6608 0.9009 0.5706 -0.0475 0.0840 -0.0207 316 LYS A NZ 2435 N N . THR A 317 ? 0.5533 0.6818 0.4021 -0.0338 0.0334 0.0406 317 THR A N 2436 C CA . THR A 317 ? 0.5704 0.6841 0.4051 -0.0279 0.0236 0.0505 317 THR A CA 2437 C C . THR A 317 ? 0.5880 0.6800 0.4266 -0.0267 0.0200 0.0590 317 THR A C 2438 O O . THR A 317 ? 0.6009 0.6887 0.4472 -0.0337 0.0258 0.0592 317 THR A O 2439 C CB . THR A 317 ? 0.5428 0.6647 0.3843 -0.0178 0.0156 0.0430 317 THR A CB 2440 O OG1 . THR A 317 ? 0.5478 0.6594 0.3778 -0.0112 0.0057 0.0521 317 THR A OG1 2441 C CG2 . THR A 317 ? 0.5103 0.6337 0.3761 -0.0128 0.0144 0.0342 317 THR A CG2 2442 N N . GLN A 318 ? 0.6059 0.6848 0.4395 -0.0177 0.0103 0.0652 318 GLN A N 2443 C CA . GLN A 318 ? 0.6083 0.6656 0.4457 -0.0145 0.0064 0.0715 318 GLN A CA 2444 C C . GLN A 318 ? 0.5915 0.6535 0.4516 -0.0075 0.0042 0.0616 318 GLN A C 2445 O O . GLN A 318 ? 0.5812 0.6582 0.4500 -0.0016 0.0014 0.0537 318 GLN A O 2446 C CB . GLN A 318 ? 0.6339 0.6748 0.4557 -0.0062 -0.0031 0.0825 318 GLN A CB 2447 C CG . GLN A 318 ? 0.6777 0.7087 0.4724 -0.0125 -0.0025 0.0949 318 GLN A CG 2448 C CD . GLN A 318 ? 0.6688 0.7192 0.4519 -0.0127 -0.0033 0.0928 318 GLN A CD 2449 O OE1 . GLN A 318 ? 0.6347 0.7016 0.4280 -0.0052 -0.0080 0.0841 318 GLN A OE1 2450 N NE2 . GLN A 318 ? 0.6935 0.7416 0.4541 -0.0224 0.0017 0.1005 318 GLN A NE2 2451 N N . ILE A 319 ? 0.6040 0.6527 0.4725 -0.0090 0.0054 0.0619 319 ILE A N 2452 C CA . ILE A 319 ? 0.5832 0.6327 0.4692 -0.0017 0.0024 0.0544 319 ILE A CA 2453 C C . ILE A 319 ? 0.5946 0.6206 0.4785 0.0024 -0.0015 0.0598 319 ILE A C 2454 O O . ILE A 319 ? 0.6236 0.6317 0.4969 -0.0041 0.0002 0.0674 319 ILE A O 2455 C CB . ILE A 319 ? 0.5778 0.6389 0.4799 -0.0070 0.0081 0.0446 319 ILE A CB 2456 C CG1 . ILE A 319 ? 0.5907 0.6429 0.4925 -0.0174 0.0132 0.0473 319 ILE A CG1 2457 C CG2 . ILE A 319 ? 0.5721 0.6550 0.4771 -0.0092 0.0118 0.0376 319 ILE A CG2 2458 C CD1 . ILE A 319 ? 0.5663 0.6293 0.4856 -0.0206 0.0165 0.0380 319 ILE A CD1 2459 N N . LEU A 320 ? 0.5714 0.5973 0.4648 0.0128 -0.0063 0.0557 320 LEU A N 2460 C CA . LEU A 320 ? 0.5768 0.5823 0.4706 0.0187 -0.0096 0.0577 320 LEU A CA 2461 C C . LEU A 320 ? 0.5646 0.5774 0.4749 0.0209 -0.0082 0.0476 320 LEU A C 2462 O O . LEU A 320 ? 0.5586 0.5895 0.4787 0.0248 -0.0086 0.0412 320 LEU A O 2463 C CB . LEU A 320 ? 0.5775 0.5773 0.4654 0.0312 -0.0171 0.0630 320 LEU A CB 2464 C CG . LEU A 320 ? 0.5821 0.5592 0.4692 0.0398 -0.0209 0.0649 320 LEU A CG 2465 C CD1 . LEU A 320 ? 0.6005 0.5660 0.4754 0.0502 -0.0285 0.0742 320 LEU A CD1 2466 C CD2 . LEU A 320 ? 0.5590 0.5453 0.4625 0.0473 -0.0208 0.0548 320 LEU A CD2 2467 N N . LEU A 321 ? 0.5560 0.5538 0.4681 0.0177 -0.0067 0.0462 321 LEU A N 2468 C CA . LEU A 321 ? 0.5203 0.5236 0.4450 0.0185 -0.0054 0.0370 321 LEU A CA 2469 C C . LEU A 321 ? 0.5302 0.5128 0.4532 0.0176 -0.0059 0.0359 321 LEU A C 2470 O O . LEU A 321 ? 0.5483 0.5107 0.4612 0.0140 -0.0066 0.0419 321 LEU A O 2471 C CB . LEU A 321 ? 0.4938 0.5148 0.4271 0.0103 -0.0012 0.0315 321 LEU A CB 2472 C CG . LEU A 321 ? 0.4986 0.5233 0.4294 -0.0012 0.0031 0.0339 321 LEU A CG 2473 C CD1 . LEU A 321 ? 0.5389 0.5431 0.4586 -0.0077 0.0036 0.0415 321 LEU A CD1 2474 C CD2 . LEU A 321 ? 0.4720 0.5088 0.4153 -0.0064 0.0058 0.0262 321 LEU A CD2 2475 N N . GLY A 322 ? 0.5095 0.4961 0.4411 0.0204 -0.0057 0.0281 322 GLY A N 2476 C CA . GLY A 322 ? 0.5168 0.4854 0.4463 0.0195 -0.0064 0.0251 322 GLY A CA 2477 C C . GLY A 322 ? 0.4975 0.4735 0.4343 0.0234 -0.0061 0.0167 322 GLY A C 2478 O O . GLY A 322 ? 0.4621 0.4571 0.4064 0.0250 -0.0050 0.0137 322 GLY A O 2479 N N . VAL A 323 ? 0.5143 0.4735 0.4473 0.0244 -0.0071 0.0131 323 VAL A N 2480 C CA . VAL A 323 ? 0.5249 0.4882 0.4614 0.0260 -0.0066 0.0051 323 VAL A CA 2481 C C . VAL A 323 ? 0.5376 0.4832 0.4676 0.0338 -0.0074 0.0012 323 VAL A C 2482 O O . VAL A 323 ? 0.5575 0.4846 0.4807 0.0375 -0.0089 0.0045 323 VAL A O 2483 C CB . VAL A 323 ? 0.5280 0.4918 0.4663 0.0151 -0.0072 0.0019 323 VAL A CB 2484 C CG1 . VAL A 323 ? 0.5096 0.4921 0.4557 0.0085 -0.0059 0.0043 323 VAL A CG1 2485 C CG2 . VAL A 323 ? 0.5576 0.4992 0.4885 0.0087 -0.0087 0.0028 323 VAL A CG2 2486 N N . ASN A 324 ? 0.5331 0.4833 0.4640 0.0366 -0.0063 -0.0058 324 ASN A N 2487 C CA . ASN A 324 ? 0.5610 0.4960 0.4853 0.0441 -0.0060 -0.0115 324 ASN A CA 2488 C C . ASN A 324 ? 0.5712 0.4913 0.4880 0.0372 -0.0075 -0.0174 324 ASN A C 2489 O O . ASN A 324 ? 0.5625 0.4901 0.4816 0.0278 -0.0088 -0.0182 324 ASN A O 2490 C CB . ASN A 324 ? 0.5524 0.5032 0.4809 0.0527 -0.0026 -0.0159 324 ASN A CB 2491 C CG . ASN A 324 ? 0.5558 0.5221 0.4925 0.0594 -0.0020 -0.0113 324 ASN A CG 2492 O OD1 . ASN A 324 ? 0.5931 0.5571 0.5304 0.0588 -0.0044 -0.0046 324 ASN A OD1 2493 N ND2 . ASN A 324 ? 0.5675 0.5506 0.5099 0.0651 0.0013 -0.0148 324 ASN A ND2 2494 N N . LYS A 325 ? 0.6066 0.5059 0.5148 0.0425 -0.0079 -0.0222 325 LYS A N 2495 C CA . LYS A 325 ? 0.6339 0.5160 0.5332 0.0358 -0.0101 -0.0287 325 LYS A CA 2496 C C . LYS A 325 ? 0.6194 0.5155 0.5183 0.0314 -0.0100 -0.0344 325 LYS A C 2497 O O . LYS A 325 ? 0.6301 0.5223 0.5265 0.0214 -0.0135 -0.0369 325 LYS A O 2498 C CB . LYS A 325 ? 0.6740 0.5323 0.5634 0.0452 -0.0097 -0.0347 325 LYS A CB 2499 C CG . LYS A 325 ? 0.7239 0.5584 0.6017 0.0384 -0.0126 -0.0422 325 LYS A CG 2500 C CD . LYS A 325 ? 0.7896 0.5968 0.6579 0.0494 -0.0123 -0.0471 325 LYS A CD 2501 C CE . LYS A 325 ? 0.8347 0.6317 0.6920 0.0522 -0.0113 -0.0601 325 LYS A CE 2502 N NZ . LYS A 325 ? 0.8756 0.6519 0.7234 0.0386 -0.0162 -0.0645 325 LYS A NZ 2503 N N . ASP A 326 ? 0.6098 0.5226 0.5112 0.0382 -0.0064 -0.0362 326 ASP A N 2504 C CA . ASP A 326 ? 0.6138 0.5352 0.5104 0.0352 -0.0062 -0.0414 326 ASP A CA 2505 C C . ASP A 326 ? 0.5990 0.5440 0.5035 0.0348 -0.0042 -0.0371 326 ASP A C 2506 O O . ASP A 326 ? 0.5885 0.5426 0.4906 0.0394 -0.0001 -0.0395 326 ASP A O 2507 C CB . ASP A 326 ? 0.6394 0.5512 0.5247 0.0428 -0.0029 -0.0502 326 ASP A CB 2508 C CG . ASP A 326 ? 0.6649 0.5500 0.5402 0.0423 -0.0057 -0.0560 326 ASP A CG 2509 O OD1 . ASP A 326 ? 0.7133 0.5904 0.5823 0.0328 -0.0104 -0.0592 326 ASP A OD1 2510 O OD2 . ASP A 326 ? 0.6789 0.5503 0.5527 0.0515 -0.0037 -0.0577 326 ASP A OD2 2511 N N . GLU A 327 ? 0.6066 0.5607 0.5200 0.0286 -0.0068 -0.0313 327 GLU A N 2512 C CA . GLU A 327 ? 0.5833 0.5567 0.5045 0.0283 -0.0054 -0.0272 327 GLU A CA 2513 C C . GLU A 327 ? 0.5810 0.5599 0.4963 0.0260 -0.0062 -0.0297 327 GLU A C 2514 O O . GLU A 327 ? 0.6047 0.5955 0.5228 0.0271 -0.0037 -0.0275 327 GLU A O 2515 C CB . GLU A 327 ? 0.5847 0.5653 0.5157 0.0225 -0.0079 -0.0219 327 GLU A CB 2516 C CG . GLU A 327 ? 0.5878 0.5642 0.5227 0.0238 -0.0070 -0.0174 327 GLU A CG 2517 C CD . GLU A 327 ? 0.5741 0.5617 0.5145 0.0304 -0.0039 -0.0139 327 GLU A CD 2518 O OE1 . GLU A 327 ? 0.5678 0.5657 0.5095 0.0340 -0.0014 -0.0157 327 GLU A OE1 2519 O OE2 . GLU A 327 ? 0.5740 0.5602 0.5167 0.0313 -0.0041 -0.0091 327 GLU A OE2 2520 N N . GLY A 328 ? 0.5800 0.5495 0.4862 0.0222 -0.0101 -0.0342 328 GLY A N 2521 C CA . GLY A 328 ? 0.5670 0.5404 0.4657 0.0196 -0.0127 -0.0354 328 GLY A CA 2522 C C . GLY A 328 ? 0.5721 0.5438 0.4576 0.0233 -0.0081 -0.0389 328 GLY A C 2523 O O . GLY A 328 ? 0.5670 0.5446 0.4472 0.0219 -0.0080 -0.0368 328 GLY A O 2524 N N . SER A 329 ? 0.5811 0.5442 0.4607 0.0281 -0.0039 -0.0441 329 SER A N 2525 C CA . SER A 329 ? 0.6054 0.5666 0.4708 0.0313 0.0011 -0.0496 329 SER A CA 2526 C C . SER A 329 ? 0.6115 0.5869 0.4764 0.0318 0.0070 -0.0461 329 SER A C 2527 O O . SER A 329 ? 0.6566 0.6313 0.5066 0.0298 0.0087 -0.0480 329 SER A O 2528 C CB . SER A 329 ? 0.6199 0.5722 0.4833 0.0389 0.0061 -0.0561 329 SER A CB 2529 O OG . SER A 329 ? 0.6180 0.5795 0.4954 0.0452 0.0107 -0.0528 329 SER A OG 2530 N N . PHE A 330 ? 0.5990 0.5866 0.4785 0.0334 0.0100 -0.0410 330 PHE A N 2531 C CA . PHE A 330 ? 0.5942 0.5952 0.4744 0.0324 0.0161 -0.0380 330 PHE A CA 2532 C C . PHE A 330 ? 0.5790 0.5785 0.4494 0.0256 0.0125 -0.0337 330 PHE A C 2533 O O . PHE A 330 ? 0.5936 0.5960 0.4532 0.0231 0.0173 -0.0331 330 PHE A O 2534 C CB . PHE A 330 ? 0.5883 0.6022 0.4864 0.0339 0.0178 -0.0334 330 PHE A CB 2535 C CG . PHE A 330 ? 0.5990 0.6279 0.5011 0.0355 0.0262 -0.0339 330 PHE A CG 2536 C CD1 . PHE A 330 ? 0.6387 0.6732 0.5346 0.0292 0.0295 -0.0311 330 PHE A CD1 2537 C CD2 . PHE A 330 ? 0.6046 0.6420 0.5168 0.0431 0.0306 -0.0371 330 PHE A CD2 2538 C CE1 . PHE A 330 ? 0.6414 0.6917 0.5420 0.0286 0.0380 -0.0318 330 PHE A CE1 2539 C CE2 . PHE A 330 ? 0.6199 0.6752 0.5385 0.0442 0.0383 -0.0383 330 PHE A CE2 2540 C CZ . PHE A 330 ? 0.6249 0.6875 0.5381 0.0361 0.0426 -0.0359 330 PHE A CZ 2541 N N . PHE A 331 ? 0.5477 0.5426 0.4218 0.0227 0.0040 -0.0307 331 PHE A N 2542 C CA . PHE A 331 ? 0.5423 0.5356 0.4105 0.0183 -0.0013 -0.0260 331 PHE A CA 2543 C C . PHE A 331 ? 0.5585 0.5419 0.4074 0.0164 -0.0055 -0.0287 331 PHE A C 2544 O O . PHE A 331 ? 0.6013 0.5821 0.4378 0.0136 -0.0070 -0.0249 331 PHE A O 2545 C CB . PHE A 331 ? 0.5318 0.5273 0.4140 0.0174 -0.0084 -0.0230 331 PHE A CB 2546 C CG . PHE A 331 ? 0.5032 0.5080 0.4016 0.0189 -0.0046 -0.0207 331 PHE A CG 2547 C CD1 . PHE A 331 ? 0.4918 0.5024 0.3941 0.0174 -0.0027 -0.0164 331 PHE A CD1 2548 C CD2 . PHE A 331 ? 0.4897 0.4960 0.3972 0.0217 -0.0029 -0.0227 331 PHE A CD2 2549 C CE1 . PHE A 331 ? 0.4862 0.5061 0.4021 0.0183 0.0005 -0.0151 331 PHE A CE1 2550 C CE2 . PHE A 331 ? 0.4890 0.5042 0.4091 0.0233 0.0000 -0.0203 331 PHE A CE2 2551 C CZ . PHE A 331 ? 0.4807 0.5038 0.4053 0.0215 0.0016 -0.0170 331 PHE A CZ 2552 N N . LEU A 332 ? 0.5589 0.5354 0.4037 0.0176 -0.0078 -0.0350 332 LEU A N 2553 C CA . LEU A 332 ? 0.5977 0.5648 0.4222 0.0156 -0.0118 -0.0391 332 LEU A CA 2554 C C . LEU A 332 ? 0.6076 0.5744 0.4145 0.0160 -0.0031 -0.0410 332 LEU A C 2555 O O . LEU A 332 ? 0.6198 0.5816 0.4072 0.0130 -0.0057 -0.0400 332 LEU A O 2556 C CB . LEU A 332 ? 0.6228 0.5813 0.4470 0.0159 -0.0156 -0.0467 332 LEU A CB 2557 C CG . LEU A 332 ? 0.6080 0.5673 0.4459 0.0127 -0.0251 -0.0453 332 LEU A CG 2558 C CD1 . LEU A 332 ? 0.6110 0.5616 0.4532 0.0122 -0.0255 -0.0515 332 LEU A CD1 2559 C CD2 . LEU A 332 ? 0.6184 0.5766 0.4467 0.0089 -0.0357 -0.0448 332 LEU A CD2 2560 N N . LEU A 333 ? 0.6103 0.5836 0.4239 0.0199 0.0072 -0.0437 333 LEU A N 2561 C CA . LEU A 333 ? 0.6220 0.5994 0.4222 0.0203 0.0174 -0.0463 333 LEU A CA 2562 C C . LEU A 333 ? 0.6351 0.6165 0.4272 0.0143 0.0190 -0.0381 333 LEU A C 2563 O O . LEU A 333 ? 0.6682 0.6461 0.4388 0.0110 0.0220 -0.0382 333 LEU A O 2564 C CB . LEU A 333 ? 0.6091 0.5977 0.4243 0.0263 0.0274 -0.0499 333 LEU A CB 2565 C CG . LEU A 333 ? 0.6271 0.6271 0.4347 0.0263 0.0398 -0.0522 333 LEU A CG 2566 C CD1 . LEU A 333 ? 0.6523 0.6444 0.4361 0.0268 0.0432 -0.0602 333 LEU A CD1 2567 C CD2 . LEU A 333 ? 0.6199 0.6346 0.4474 0.0333 0.0477 -0.0554 333 LEU A CD2 2568 N N . TYR A 334 ? 0.6420 0.6290 0.4499 0.0128 0.0170 -0.0310 334 TYR A N 2569 C CA . TYR A 334 ? 0.6534 0.6418 0.4555 0.0069 0.0189 -0.0228 334 TYR A CA 2570 C C . TYR A 334 ? 0.6696 0.6449 0.4560 0.0035 0.0084 -0.0170 334 TYR A C 2571 O O . TYR A 334 ? 0.7241 0.6940 0.4920 -0.0016 0.0105 -0.0118 334 TYR A O 2572 C CB . TYR A 334 ? 0.6271 0.6251 0.4516 0.0067 0.0201 -0.0186 334 TYR A CB 2573 C CG . TYR A 334 ? 0.6211 0.6346 0.4561 0.0072 0.0317 -0.0212 334 TYR A CG 2574 C CD1 . TYR A 334 ? 0.6274 0.6483 0.4724 0.0143 0.0358 -0.0285 334 TYR A CD1 2575 C CD2 . TYR A 334 ? 0.6162 0.6371 0.4516 0.0006 0.0382 -0.0164 334 TYR A CD2 2576 C CE1 . TYR A 334 ? 0.6130 0.6509 0.4696 0.0162 0.0455 -0.0313 334 TYR A CE1 2577 C CE2 . TYR A 334 ? 0.6112 0.6502 0.4586 0.0006 0.0485 -0.0194 334 TYR A CE2 2578 C CZ . TYR A 334 ? 0.6047 0.6535 0.4635 0.0092 0.0518 -0.0270 334 TYR A CZ 2579 O OH . TYR A 334 ? 0.5783 0.6477 0.4510 0.0107 0.0611 -0.0304 334 TYR A OH 2580 N N . GLY A 335 ? 0.6506 0.6212 0.4441 0.0062 -0.0027 -0.0177 335 GLY A N 2581 C CA . GLY A 335 ? 0.6501 0.6114 0.4346 0.0050 -0.0144 -0.0122 335 GLY A CA 2582 C C . GLY A 335 ? 0.6508 0.6046 0.4207 0.0056 -0.0241 -0.0160 335 GLY A C 2583 O O . GLY A 335 ? 0.6900 0.6363 0.4468 0.0048 -0.0332 -0.0111 335 GLY A O 2584 N N . ALA A 336 ? 0.6219 0.5767 0.3933 0.0071 -0.0231 -0.0247 336 ALA A N 2585 C CA . ALA A 336 ? 0.6200 0.5688 0.3809 0.0066 -0.0337 -0.0293 336 ALA A CA 2586 C C . ALA A 336 ? 0.6498 0.5910 0.3821 0.0047 -0.0305 -0.0338 336 ALA A C 2587 O O . ALA A 336 ? 0.6569 0.5996 0.3852 0.0055 -0.0190 -0.0391 336 ALA A O 2588 C CB . ALA A 336 ? 0.6106 0.5621 0.3893 0.0078 -0.0361 -0.0364 336 ALA A CB 2589 N N . PRO A 337 ? 0.6683 0.6024 0.3805 0.0028 -0.0410 -0.0323 337 PRO A N 2590 C CA . PRO A 337 ? 0.7024 0.6292 0.3847 0.0006 -0.0383 -0.0373 337 PRO A CA 2591 C C . PRO A 337 ? 0.6994 0.6245 0.3829 0.0016 -0.0365 -0.0502 337 PRO A C 2592 O O . PRO A 337 ? 0.7028 0.6290 0.4040 0.0021 -0.0440 -0.0540 337 PRO A O 2593 C CB . PRO A 337 ? 0.7290 0.6492 0.3934 -0.0009 -0.0536 -0.0329 337 PRO A CB 2594 C CG . PRO A 337 ? 0.7131 0.6395 0.4036 0.0013 -0.0654 -0.0322 337 PRO A CG 2595 C CD . PRO A 337 ? 0.6758 0.6098 0.3935 0.0034 -0.0568 -0.0286 337 PRO A CD 2596 N N . GLY A 338 ? 0.7082 0.6301 0.3728 0.0017 -0.0261 -0.0571 338 GLY A N 2597 C CA . GLY A 338 ? 0.7144 0.6312 0.3765 0.0036 -0.0229 -0.0706 338 GLY A CA 2598 C C . GLY A 338 ? 0.7099 0.6318 0.3884 0.0088 -0.0087 -0.0753 338 GLY A C 2599 O O . GLY A 338 ? 0.7348 0.6515 0.4046 0.0119 -0.0022 -0.0865 338 GLY A O 2600 N N . PHE A 339 ? 0.6771 0.6091 0.3788 0.0105 -0.0044 -0.0672 339 PHE A N 2601 C CA . PHE A 339 ? 0.6657 0.6043 0.3866 0.0161 0.0064 -0.0705 339 PHE A CA 2602 C C . PHE A 339 ? 0.6883 0.6378 0.4039 0.0172 0.0207 -0.0693 339 PHE A C 2603 O O . PHE A 339 ? 0.6900 0.6451 0.4013 0.0125 0.0223 -0.0600 339 PHE A O 2604 C CB . PHE A 339 ? 0.6302 0.5751 0.3794 0.0169 0.0024 -0.0631 339 PHE A CB 2605 C CG . PHE A 339 ? 0.6157 0.5532 0.3744 0.0156 -0.0091 -0.0652 339 PHE A CG 2606 C CD1 . PHE A 339 ? 0.6129 0.5482 0.3670 0.0107 -0.0214 -0.0615 339 PHE A CD1 2607 C CD2 . PHE A 339 ? 0.5964 0.5289 0.3679 0.0191 -0.0077 -0.0710 339 PHE A CD2 2608 C CE1 . PHE A 339 ? 0.5997 0.5315 0.3642 0.0083 -0.0313 -0.0641 339 PHE A CE1 2609 C CE2 . PHE A 339 ? 0.5921 0.5176 0.3715 0.0158 -0.0173 -0.0727 339 PHE A CE2 2610 C CZ . PHE A 339 ? 0.5920 0.5188 0.3690 0.0099 -0.0287 -0.0696 339 PHE A CZ 2611 N N . SER A 340 ? 0.7134 0.6659 0.4305 0.0233 0.0311 -0.0788 340 SER A N 2612 C CA . SER A 340 ? 0.7286 0.6956 0.4438 0.0247 0.0460 -0.0797 340 SER A CA 2613 C C . SER A 340 ? 0.7146 0.6908 0.4515 0.0343 0.0544 -0.0864 340 SER A C 2614 O O . SER A 340 ? 0.7344 0.6999 0.4773 0.0407 0.0504 -0.0937 340 SER A O 2615 C CB . SER A 340 ? 0.7753 0.7386 0.4595 0.0225 0.0520 -0.0866 340 SER A CB 2616 O OG . SER A 340 ? 0.8231 0.7814 0.4870 0.0135 0.0461 -0.0775 340 SER A OG 2617 N N . LYS A 341 ? 0.6851 0.6807 0.4332 0.0351 0.0656 -0.0839 341 LYS A N 2618 C CA . LYS A 341 ? 0.6654 0.6730 0.4365 0.0452 0.0724 -0.0892 341 LYS A CA 2619 C C . LYS A 341 ? 0.6785 0.6830 0.4415 0.0549 0.0797 -0.1037 341 LYS A C 2620 O O . LYS A 341 ? 0.7111 0.7150 0.4904 0.0656 0.0801 -0.1094 341 LYS A O 2621 C CB . LYS A 341 ? 0.6538 0.6863 0.4399 0.0428 0.0824 -0.0837 341 LYS A CB 2622 C CG . LYS A 341 ? 0.6438 0.6904 0.4584 0.0531 0.0854 -0.0866 341 LYS A CG 2623 C CD . LYS A 341 ? 0.6326 0.7059 0.4644 0.0494 0.0936 -0.0814 341 LYS A CD 2624 C CE . LYS A 341 ? 0.6563 0.7483 0.4796 0.0476 0.1089 -0.0874 341 LYS A CE 2625 N NZ . LYS A 341 ? 0.6682 0.7637 0.4910 0.0608 0.1162 -0.1016 341 LYS A NZ 2626 N N . ASP A 342 ? 0.6845 0.6860 0.4214 0.0517 0.0853 -0.1099 342 ASP A N 2627 C CA . ASP A 342 ? 0.6993 0.7015 0.4279 0.0613 0.0950 -0.1250 342 ASP A CA 2628 C C . ASP A 342 ? 0.7220 0.6985 0.4273 0.0625 0.0880 -0.1349 342 ASP A C 2629 O O . ASP A 342 ? 0.7242 0.6981 0.4167 0.0694 0.0958 -0.1486 342 ASP A O 2630 C CB . ASP A 342 ? 0.7071 0.7305 0.4245 0.0576 0.1107 -0.1271 342 ASP A CB 2631 C CG . ASP A 342 ? 0.6769 0.7280 0.4195 0.0563 0.1188 -0.1198 342 ASP A CG 2632 O OD1 . ASP A 342 ? 0.6361 0.6905 0.4050 0.0605 0.1127 -0.1146 342 ASP A OD1 2633 O OD2 . ASP A 342 ? 0.6887 0.7586 0.4237 0.0502 0.1316 -0.1193 342 ASP A OD2 2634 N N . SER A 343 ? 0.7466 0.7053 0.4473 0.0558 0.0733 -0.1289 343 SER A N 2635 C CA . SER A 343 ? 0.7903 0.7248 0.4718 0.0553 0.0645 -0.1380 343 SER A CA 2636 C C . SER A 343 ? 0.7796 0.6989 0.4795 0.0579 0.0532 -0.1367 343 SER A C 2637 O O . SER A 343 ? 0.7353 0.6627 0.4588 0.0579 0.0504 -0.1264 343 SER A O 2638 C CB . SER A 343 ? 0.8115 0.7393 0.4682 0.0432 0.0560 -0.1325 343 SER A CB 2639 O OG . SER A 343 ? 0.8009 0.7315 0.4709 0.0362 0.0460 -0.1179 343 SER A OG 2640 N N . GLU A 344 ? 0.8254 0.7222 0.5129 0.0591 0.0469 -0.1472 344 GLU A N 2641 C CA . GLU A 344 ? 0.8404 0.7197 0.5404 0.0576 0.0350 -0.1454 344 GLU A CA 2642 C C . GLU A 344 ? 0.8018 0.6847 0.5067 0.0459 0.0233 -0.1325 344 GLU A C 2643 O O . GLU A 344 ? 0.8059 0.6834 0.5281 0.0438 0.0155 -0.1268 344 GLU A O 2644 C CB . GLU A 344 ? 0.9134 0.7665 0.5952 0.0580 0.0299 -0.1599 344 GLU A CB 2645 C CG . GLU A 344 ? 0.9616 0.8012 0.6487 0.0713 0.0363 -0.1714 344 GLU A CG 2646 C CD . GLU A 344 ? 1.0491 0.8600 0.7149 0.0709 0.0316 -0.1870 344 GLU A CD 2647 O OE1 . GLU A 344 ? 1.0860 0.8897 0.7323 0.0598 0.0235 -0.1896 344 GLU A OE1 2648 O OE2 . GLU A 344 ? 1.1054 0.9000 0.7736 0.0821 0.0355 -0.1972 344 GLU A OE2 2649 N N . SER A 345 ? 0.7780 0.6695 0.4668 0.0387 0.0221 -0.1280 345 SER A N 2650 C CA . SER A 345 ? 0.7496 0.6456 0.4420 0.0295 0.0111 -0.1163 345 SER A CA 2651 C C . SER A 345 ? 0.7565 0.6373 0.4477 0.0234 -0.0032 -0.1194 345 SER A C 2652 O O . SER A 345 ? 0.7343 0.6180 0.4437 0.0194 -0.0114 -0.1113 345 SER A O 2653 C CB . SER A 345 ? 0.7264 0.6370 0.4457 0.0306 0.0128 -0.1037 345 SER A CB 2654 O OG . SER A 345 ? 0.7241 0.6504 0.4456 0.0343 0.0254 -0.1010 345 SER A OG 2655 N N . LYS A 346 ? 0.7886 0.6545 0.4580 0.0221 -0.0059 -0.1318 346 LYS A N 2656 C CA . LYS A 346 ? 0.8054 0.6590 0.4697 0.0140 -0.0202 -0.1358 346 LYS A CA 2657 C C . LYS A 346 ? 0.7939 0.6583 0.4513 0.0064 -0.0305 -0.1268 346 LYS A C 2658 O O . LYS A 346 ? 0.8086 0.6789 0.4465 0.0063 -0.0275 -0.1247 346 LYS A O 2659 C CB . LYS A 346 ? 0.8665 0.7015 0.5063 0.0143 -0.0203 -0.1523 346 LYS A CB 2660 C CG . LYS A 346 ? 0.9043 0.7238 0.5520 0.0224 -0.0128 -0.1618 346 LYS A CG 2661 C CD . LYS A 346 ? 0.9632 0.7605 0.5867 0.0225 -0.0140 -0.1797 346 LYS A CD 2662 C CE . LYS A 346 ? 1.0021 0.8044 0.5989 0.0272 -0.0042 -0.1877 346 LYS A CE 2663 N NZ . LYS A 346 ? 1.0634 0.8433 0.6369 0.0296 -0.0032 -0.2070 346 LYS A NZ 2664 N N . ILE A 347 ? 0.7812 0.6483 0.4549 0.0004 -0.0424 -0.1214 347 ILE A N 2665 C CA . ILE A 347 ? 0.7689 0.6488 0.4443 -0.0040 -0.0521 -0.1109 347 ILE A CA 2666 C C . ILE A 347 ? 0.7881 0.6638 0.4508 -0.0116 -0.0675 -0.1165 347 ILE A C 2667 O O . ILE A 347 ? 0.7912 0.6600 0.4626 -0.0167 -0.0743 -0.1234 347 ILE A O 2668 C CB . ILE A 347 ? 0.7437 0.6350 0.4511 -0.0039 -0.0536 -0.1002 347 ILE A CB 2669 C CG1 . ILE A 347 ? 0.7244 0.6228 0.4422 0.0031 -0.0399 -0.0936 347 ILE A CG1 2670 C CG2 . ILE A 347 ? 0.7401 0.6435 0.4532 -0.0077 -0.0657 -0.0914 347 ILE A CG2 2671 C CD1 . ILE A 347 ? 0.7257 0.6311 0.4275 0.0048 -0.0345 -0.0877 347 ILE A CD1 2672 N N . SER A 348 ? 0.8027 0.6826 0.4444 -0.0130 -0.0736 -0.1132 348 SER A N 2673 C CA . SER A 348 ? 0.8177 0.6958 0.4454 -0.0196 -0.0896 -0.1184 348 SER A CA 2674 C C . SER A 348 ? 0.8168 0.7079 0.4701 -0.0236 -0.1032 -0.1119 348 SER A C 2675 O O . SER A 348 ? 0.8067 0.7079 0.4859 -0.0208 -0.0998 -0.1025 348 SER A O 2676 C CB . SER A 348 ? 0.8347 0.7134 0.4308 -0.0190 -0.0923 -0.1150 348 SER A CB 2677 O OG . SER A 348 ? 0.8142 0.7039 0.4184 -0.0159 -0.0925 -0.0998 348 SER A OG 2678 N N . ARG A 349 ? 0.8456 0.7379 0.4914 -0.0300 -0.1187 -0.1177 349 ARG A N 2679 C CA . ARG A 349 ? 0.8274 0.7363 0.4947 -0.0334 -0.1336 -0.1123 349 ARG A CA 2680 C C . ARG A 349 ? 0.8032 0.7242 0.4775 -0.0264 -0.1340 -0.0974 349 ARG A C 2681 O O . ARG A 349 ? 0.7598 0.6925 0.4630 -0.0246 -0.1331 -0.0904 349 ARG A O 2682 C CB . ARG A 349 ? 0.8617 0.7717 0.5112 -0.0397 -0.1510 -0.1201 349 ARG A CB 2683 N N . GLU A 350 ? 0.8321 0.7485 0.4779 -0.0229 -0.1347 -0.0927 350 GLU A N 2684 C CA . GLU A 350 ? 0.8265 0.7493 0.4733 -0.0169 -0.1361 -0.0784 350 GLU A CA 2685 C C . GLU A 350 ? 0.7933 0.7187 0.4618 -0.0125 -0.1211 -0.0707 350 GLU A C 2686 O O . GLU A 350 ? 0.7873 0.7234 0.4795 -0.0095 -0.1246 -0.0628 350 GLU A O 2687 C CB . GLU A 350 ? 0.8410 0.7540 0.4483 -0.0156 -0.1372 -0.0745 350 GLU A CB 2688 N N . ASP A 351 ? 0.7968 0.7135 0.4580 -0.0116 -0.1049 -0.0740 351 ASP A N 2689 C CA . ASP A 351 ? 0.7697 0.6898 0.4498 -0.0076 -0.0910 -0.0673 351 ASP A CA 2690 C C . ASP A 351 ? 0.7322 0.6610 0.4475 -0.0078 -0.0910 -0.0676 351 ASP A C 2691 O O . ASP A 351 ? 0.7151 0.6502 0.4489 -0.0045 -0.0846 -0.0600 351 ASP A O 2692 C CB . ASP A 351 ? 0.7849 0.6968 0.4522 -0.0061 -0.0743 -0.0725 351 ASP A CB 2693 C CG . ASP A 351 ? 0.8067 0.7133 0.4419 -0.0059 -0.0693 -0.0694 351 ASP A CG 2694 O OD1 . ASP A 351 ? 0.8159 0.7243 0.4436 -0.0057 -0.0744 -0.0585 351 ASP A OD1 2695 O OD2 . ASP A 351 ? 0.8324 0.7325 0.4495 -0.0058 -0.0595 -0.0779 351 ASP A OD2 2696 N N . PHE A 352 ? 0.7358 0.6640 0.4588 -0.0127 -0.0977 -0.0765 352 PHE A N 2697 C CA . PHE A 352 ? 0.7169 0.6535 0.4709 -0.0149 -0.0985 -0.0765 352 PHE A CA 2698 C C . PHE A 352 ? 0.7170 0.6701 0.4900 -0.0137 -0.1084 -0.0686 352 PHE A C 2699 O O . PHE A 352 ? 0.6785 0.6404 0.4747 -0.0114 -0.1037 -0.0630 352 PHE A O 2700 C CB . PHE A 352 ? 0.7371 0.6681 0.4923 -0.0226 -0.1044 -0.0877 352 PHE A CB 2701 C CG . PHE A 352 ? 0.7236 0.6613 0.5081 -0.0267 -0.1037 -0.0876 352 PHE A CG 2702 C CD1 . PHE A 352 ? 0.7145 0.6440 0.5080 -0.0251 -0.0912 -0.0874 352 PHE A CD1 2703 C CD2 . PHE A 352 ? 0.7167 0.6700 0.5197 -0.0321 -0.1153 -0.0873 352 PHE A CD2 2704 C CE1 . PHE A 352 ? 0.6970 0.6313 0.5145 -0.0297 -0.0902 -0.0862 352 PHE A CE1 2705 C CE2 . PHE A 352 ? 0.7021 0.6628 0.5312 -0.0372 -0.1131 -0.0869 352 PHE A CE2 2706 C CZ . PHE A 352 ? 0.6946 0.6445 0.5294 -0.0364 -0.1005 -0.0859 352 PHE A CZ 2707 N N . MET A 353 ? 0.7547 0.7122 0.5172 -0.0144 -0.1225 -0.0687 353 MET A N 2708 C CA . MET A 353 ? 0.7519 0.7257 0.5322 -0.0115 -0.1337 -0.0624 353 MET A CA 2709 C C . MET A 353 ? 0.7222 0.6956 0.5037 -0.0037 -0.1277 -0.0512 353 MET A C 2710 O O . MET A 353 ? 0.6988 0.6840 0.5046 -0.0004 -0.1282 -0.0466 353 MET A O 2711 C CB . MET A 353 ? 0.8029 0.7805 0.5687 -0.0124 -0.1511 -0.0645 353 MET A CB 2712 C CG . MET A 353 ? 0.8534 0.8341 0.6208 -0.0216 -0.1597 -0.0764 353 MET A CG 2713 S SD . MET A 353 ? 0.9345 0.9247 0.6886 -0.0226 -0.1829 -0.0792 353 MET A SD 2714 C CE . MET A 353 ? 0.9518 0.9274 0.6688 -0.0140 -0.1837 -0.0691 353 MET A CE 2715 N N . SER A 354 ? 0.7283 0.6880 0.4831 -0.0015 -0.1216 -0.0475 354 SER A N 2716 C CA . SER A 354 ? 0.7320 0.6883 0.4852 0.0037 -0.1141 -0.0371 354 SER A CA 2717 C C . SER A 354 ? 0.6987 0.6600 0.4765 0.0047 -0.1015 -0.0358 354 SER A C 2718 O O . SER A 354 ? 0.6865 0.6528 0.4784 0.0088 -0.1008 -0.0289 354 SER A O 2719 C CB . SER A 354 ? 0.7478 0.6895 0.4688 0.0030 -0.1060 -0.0350 354 SER A CB 2720 O OG . SER A 354 ? 0.7760 0.7115 0.4703 0.0027 -0.1174 -0.0336 354 SER A OG 2721 N N . GLY A 355 ? 0.6863 0.6449 0.4673 0.0014 -0.0920 -0.0427 355 GLY A N 2722 C CA . GLY A 355 ? 0.6575 0.6196 0.4582 0.0025 -0.0804 -0.0416 355 GLY A CA 2723 C C . GLY A 355 ? 0.6403 0.6156 0.4695 0.0021 -0.0849 -0.0410 355 GLY A C 2724 O O . GLY A 355 ? 0.6246 0.6056 0.4701 0.0046 -0.0784 -0.0367 355 GLY A O 2725 N N . VAL A 356 ? 0.6467 0.6286 0.4821 -0.0015 -0.0960 -0.0458 356 VAL A N 2726 C CA . VAL A 356 ? 0.6224 0.6204 0.4856 -0.0028 -0.1002 -0.0459 356 VAL A CA 2727 C C . VAL A 356 ? 0.6179 0.6256 0.4910 0.0041 -0.1049 -0.0388 356 VAL A C 2728 O O . VAL A 356 ? 0.5921 0.6090 0.4854 0.0061 -0.1000 -0.0363 356 VAL A O 2729 C CB . VAL A 356 ? 0.6414 0.6469 0.5099 -0.0094 -0.1114 -0.0532 356 VAL A CB 2730 C CG1 . VAL A 356 ? 0.6273 0.6534 0.5261 -0.0110 -0.1149 -0.0532 356 VAL A CG1 2731 C CG2 . VAL A 356 ? 0.6661 0.6587 0.5252 -0.0166 -0.1068 -0.0610 356 VAL A CG2 2732 N N . LYS A 357 ? 0.6464 0.6505 0.5039 0.0080 -0.1147 -0.0358 357 LYS A N 2733 C CA . LYS A 357 ? 0.6524 0.6598 0.5144 0.0160 -0.1199 -0.0283 357 LYS A CA 2734 C C . LYS A 357 ? 0.6437 0.6442 0.5074 0.0188 -0.1072 -0.0226 357 LYS A C 2735 O O . LYS A 357 ? 0.6602 0.6683 0.5417 0.0234 -0.1068 -0.0198 357 LYS A O 2736 C CB . LYS A 357 ? 0.6909 0.6882 0.5274 0.0194 -0.1308 -0.0242 357 LYS A CB 2737 C CG . LYS A 357 ? 0.7215 0.7316 0.5644 0.0213 -0.1484 -0.0271 357 LYS A CG 2738 C CD . LYS A 357 ? 0.7574 0.7570 0.5696 0.0199 -0.1586 -0.0273 357 LYS A CD 2739 N N . LEU A 358 ? 0.6310 0.6185 0.4769 0.0159 -0.0969 -0.0218 358 LEU A N 2740 C CA . LEU A 358 ? 0.6031 0.5857 0.4502 0.0173 -0.0851 -0.0171 358 LEU A CA 2741 C C . LEU A 358 ? 0.5909 0.5842 0.4626 0.0164 -0.0776 -0.0197 358 LEU A C 2742 O O . LEU A 358 ? 0.6137 0.6090 0.4951 0.0190 -0.0726 -0.0159 358 LEU A O 2743 C CB . LEU A 358 ? 0.6087 0.5793 0.4335 0.0142 -0.0756 -0.0170 358 LEU A CB 2744 C CG . LEU A 358 ? 0.6278 0.5857 0.4231 0.0139 -0.0791 -0.0127 358 LEU A CG 2745 C CD1 . LEU A 358 ? 0.6436 0.5949 0.4212 0.0101 -0.0676 -0.0157 358 LEU A CD1 2746 C CD2 . LEU A 358 ? 0.6199 0.5706 0.4097 0.0169 -0.0807 -0.0032 358 LEU A CD2 2747 N N . SER A 359 ? 0.6025 0.6011 0.4826 0.0122 -0.0769 -0.0259 359 SER A N 2748 C CA . SER A 359 ? 0.5949 0.6013 0.4946 0.0105 -0.0693 -0.0274 359 SER A CA 2749 C C . SER A 359 ? 0.5920 0.6139 0.5145 0.0122 -0.0733 -0.0269 359 SER A C 2750 O O . SER A 359 ? 0.6100 0.6379 0.5461 0.0124 -0.0663 -0.0259 359 SER A O 2751 C CB . SER A 359 ? 0.5974 0.6010 0.4968 0.0047 -0.0674 -0.0335 359 SER A CB 2752 O OG . SER A 359 ? 0.6117 0.6017 0.4915 0.0045 -0.0620 -0.0353 359 SER A OG 2753 N N . VAL A 360 ? 0.6239 0.6534 0.5504 0.0139 -0.0846 -0.0280 360 VAL A N 2754 C CA . VAL A 360 ? 0.6175 0.6653 0.5676 0.0160 -0.0891 -0.0294 360 VAL A CA 2755 C C . VAL A 360 ? 0.6349 0.6837 0.5835 0.0245 -0.0989 -0.0261 360 VAL A C 2756 O O . VAL A 360 ? 0.6483 0.7058 0.6006 0.0262 -0.1106 -0.0284 360 VAL A O 2757 C CB . VAL A 360 ? 0.6327 0.6934 0.5944 0.0091 -0.0946 -0.0357 360 VAL A CB 2758 C CG1 . VAL A 360 ? 0.6416 0.7241 0.6306 0.0088 -0.0937 -0.0377 360 VAL A CG1 2759 C CG2 . VAL A 360 ? 0.6429 0.6933 0.5967 0.0007 -0.0876 -0.0385 360 VAL A CG2 2760 N N . PRO A 361 ? 0.6646 0.7034 0.6070 0.0300 -0.0949 -0.0208 361 PRO A N 2761 C CA . PRO A 361 ? 0.6863 0.7181 0.6211 0.0383 -0.1043 -0.0163 361 PRO A CA 2762 C C . PRO A 361 ? 0.6909 0.7391 0.6469 0.0462 -0.1139 -0.0185 361 PRO A C 2763 O O . PRO A 361 ? 0.6883 0.7315 0.6374 0.0536 -0.1253 -0.0155 361 PRO A O 2764 C CB . PRO A 361 ? 0.6881 0.7050 0.6139 0.0399 -0.0955 -0.0109 361 PRO A CB 2765 C CG . PRO A 361 ? 0.6522 0.6757 0.5892 0.0348 -0.0829 -0.0137 361 PRO A CG 2766 C CD . PRO A 361 ? 0.6465 0.6771 0.5854 0.0281 -0.0820 -0.0184 361 PRO A CD 2767 N N . HIS A 362 ? 0.7366 0.8042 0.7173 0.0453 -0.1094 -0.0236 362 HIS A N 2768 C CA . HIS A 362 ? 0.7860 0.8738 0.7900 0.0530 -0.1170 -0.0274 362 HIS A CA 2769 C C . HIS A 362 ? 0.7657 0.8737 0.7819 0.0493 -0.1260 -0.0329 362 HIS A C 2770 O O . HIS A 362 ? 0.7628 0.8921 0.8005 0.0552 -0.1333 -0.0369 362 HIS A O 2771 C CB . HIS A 362 ? 0.8257 0.9279 0.8511 0.0533 -0.1067 -0.0311 362 HIS A CB 2772 C CG . HIS A 362 ? 0.9064 0.9948 0.9271 0.0599 -0.1013 -0.0279 362 HIS A CG 2773 N ND1 . HIS A 362 ? 0.9667 1.0584 0.9980 0.0717 -0.1067 -0.0292 362 HIS A ND1 2774 C CD2 . HIS A 362 ? 0.9482 1.0201 0.9558 0.0561 -0.0912 -0.0243 362 HIS A CD2 2775 C CE1 . HIS A 362 ? 0.9849 1.0604 1.0084 0.0740 -0.1001 -0.0266 362 HIS A CE1 2776 N NE2 . HIS A 362 ? 0.9992 1.0639 1.0089 0.0642 -0.0908 -0.0236 362 HIS A NE2 2777 N N . ALA A 363 ? 0.7426 0.8451 0.7463 0.0392 -0.1256 -0.0339 363 ALA A N 2778 C CA . ALA A 363 ? 0.7224 0.8438 0.7382 0.0329 -0.1332 -0.0401 363 ALA A CA 2779 C C . ALA A 363 ? 0.7162 0.8403 0.7260 0.0394 -0.1505 -0.0399 363 ALA A C 2780 O O . ALA A 363 ? 0.7787 0.8819 0.7617 0.0410 -0.1553 -0.0353 363 ALA A O 2781 C CB . ALA A 363 ? 0.7314 0.8431 0.7350 0.0201 -0.1270 -0.0422 363 ALA A CB 2782 N N . ASN A 364 ? 0.6600 0.8114 0.6951 0.0429 -0.1598 -0.0450 364 ASN A N 2783 C CA . ASN A 364 ? 0.6327 0.7925 0.6661 0.0481 -0.1782 -0.0461 364 ASN A CA 2784 C C . ASN A 364 ? 0.6466 0.8047 0.6674 0.0353 -0.1828 -0.0501 364 ASN A C 2785 O O . ASN A 364 ? 0.6398 0.7932 0.6585 0.0230 -0.1719 -0.0530 364 ASN A O 2786 C CB . ASN A 364 ? 0.5972 0.7914 0.6652 0.0555 -0.1864 -0.0517 364 ASN A CB 2787 C CG . ASN A 364 ? 0.5681 0.7903 0.6639 0.0432 -0.1786 -0.0598 364 ASN A CG 2788 O OD1 . ASN A 364 ? 0.5675 0.7811 0.6559 0.0294 -0.1680 -0.0608 364 ASN A OD1 2789 N ND2 . ASN A 364 ? 0.5558 0.8114 0.6836 0.0485 -0.1836 -0.0656 364 ASN A ND2 2790 N N . ASP A 365 ? 0.6686 0.8295 0.6803 0.0388 -0.1998 -0.0506 365 ASP A N 2791 C CA . ASP A 365 ? 0.6771 0.8355 0.6743 0.0274 -0.2064 -0.0554 365 ASP A CA 2792 C C . ASP A 365 ? 0.6378 0.8125 0.6552 0.0121 -0.1988 -0.0639 365 ASP A C 2793 O O . ASP A 365 ? 0.6420 0.8001 0.6432 0.0006 -0.1917 -0.0662 365 ASP A O 2794 C CB . ASP A 365 ? 0.7280 0.9000 0.7249 0.0340 -0.2282 -0.0568 365 ASP A CB 2795 C CG . ASP A 365 ? 0.7872 0.9590 0.7697 0.0219 -0.2371 -0.0633 365 ASP A CG 2796 O OD1 . ASP A 365 ? 0.8282 0.9750 0.7836 0.0134 -0.2288 -0.0632 365 ASP A OD1 2797 O OD2 . ASP A 365 ? 0.7970 0.9945 0.7955 0.0213 -0.2529 -0.0691 365 ASP A OD2 2798 N N . LEU A 366 ? 0.6072 0.8134 0.6596 0.0119 -0.1996 -0.0685 366 LEU A N 2799 C CA . LEU A 366 ? 0.5750 0.7980 0.6477 -0.0040 -0.1923 -0.0757 366 LEU A CA 2800 C C . LEU A 366 ? 0.5531 0.7565 0.6184 -0.0113 -0.1727 -0.0729 366 LEU A C 2801 O O . LEU A 366 ? 0.5643 0.7607 0.6257 -0.0256 -0.1669 -0.0766 366 LEU A O 2802 C CB . LEU A 366 ? 0.5526 0.8156 0.6649 -0.0019 -0.1951 -0.0806 366 LEU A CB 2803 C CG . LEU A 366 ? 0.5424 0.8265 0.6780 -0.0198 -0.1876 -0.0876 366 LEU A CG 2804 C CD1 . LEU A 366 ? 0.5629 0.8537 0.6961 -0.0331 -0.1998 -0.0947 366 LEU A CD1 2805 C CD2 . LEU A 366 ? 0.5345 0.8578 0.7088 -0.0157 -0.1856 -0.0912 366 LEU A CD2 2806 N N . GLY A 367 ? 0.5357 0.7296 0.5991 -0.0013 -0.1632 -0.0666 367 GLY A N 2807 C CA . GLY A 367 ? 0.5242 0.6989 0.5784 -0.0063 -0.1460 -0.0632 367 GLY A CA 2808 C C . GLY A 367 ? 0.5338 0.6781 0.5572 -0.0121 -0.1431 -0.0619 367 GLY A C 2809 O O . GLY A 367 ? 0.5196 0.6522 0.5386 -0.0212 -0.1322 -0.0625 367 GLY A O 2810 N N . LEU A 368 ? 0.5531 0.6844 0.5543 -0.0065 -0.1531 -0.0604 368 LEU A N 2811 C CA . LEU A 368 ? 0.5666 0.6709 0.5376 -0.0109 -0.1504 -0.0603 368 LEU A CA 2812 C C . LEU A 368 ? 0.5807 0.6861 0.5506 -0.0244 -0.1544 -0.0687 368 LEU A C 2813 O O . LEU A 368 ? 0.5879 0.6738 0.5434 -0.0314 -0.1461 -0.0707 368 LEU A O 2814 C CB . LEU A 368 ? 0.5855 0.6768 0.5314 -0.0020 -0.1597 -0.0561 368 LEU A CB 2815 C CG . LEU A 368 ? 0.5775 0.6622 0.5200 0.0105 -0.1565 -0.0473 368 LEU A CG 2816 C CD1 . LEU A 368 ? 0.6011 0.6728 0.5176 0.0175 -0.1678 -0.0428 368 LEU A CD1 2817 C CD2 . LEU A 368 ? 0.5598 0.6278 0.4949 0.0097 -0.1394 -0.0435 368 LEU A CD2 2818 N N . ASP A 369 ? 0.5778 0.7059 0.5633 -0.0279 -0.1676 -0.0741 369 ASP A N 2819 C CA . ASP A 369 ? 0.5918 0.7232 0.5801 -0.0430 -0.1717 -0.0829 369 ASP A CA 2820 C C . ASP A 369 ? 0.5732 0.7035 0.5757 -0.0542 -0.1578 -0.0843 369 ASP A C 2821 O O . ASP A 369 ? 0.5890 0.7023 0.5802 -0.0656 -0.1545 -0.0889 369 ASP A O 2822 C CB . ASP A 369 ? 0.5973 0.7597 0.6065 -0.0454 -0.1879 -0.0886 369 ASP A CB 2823 C CG . ASP A 369 ? 0.6197 0.7790 0.6088 -0.0384 -0.2045 -0.0890 369 ASP A CG 2824 O OD1 . ASP A 369 ? 0.6226 0.7560 0.5811 -0.0315 -0.2025 -0.0843 369 ASP A OD1 2825 O OD2 . ASP A 369 ? 0.6475 0.8319 0.6516 -0.0400 -0.2197 -0.0941 369 ASP A OD2 2826 N N . ALA A 370 ? 0.5406 0.6873 0.5660 -0.0508 -0.1499 -0.0802 370 ALA A N 2827 C CA . ALA A 370 ? 0.5301 0.6778 0.5689 -0.0615 -0.1371 -0.0802 370 ALA A CA 2828 C C . ALA A 370 ? 0.5304 0.6452 0.5467 -0.0619 -0.1246 -0.0764 370 ALA A C 2829 O O . ALA A 370 ? 0.5481 0.6503 0.5614 -0.0737 -0.1191 -0.0789 370 ALA A O 2830 C CB . ALA A 370 ? 0.5087 0.6816 0.5740 -0.0562 -0.1312 -0.0769 370 ALA A CB 2831 N N . VAL A 371 ? 0.5180 0.6193 0.5194 -0.0490 -0.1206 -0.0705 371 VAL A N 2832 C CA . VAL A 371 ? 0.5109 0.5841 0.4918 -0.0472 -0.1098 -0.0673 371 VAL A CA 2833 C C . VAL A 371 ? 0.5333 0.5851 0.4920 -0.0534 -0.1136 -0.0734 371 VAL A C 2834 O O . VAL A 371 ? 0.5544 0.5873 0.5052 -0.0595 -0.1064 -0.0750 371 VAL A O 2835 C CB . VAL A 371 ? 0.5137 0.5790 0.4823 -0.0332 -0.1066 -0.0608 371 VAL A CB 2836 C CG1 . VAL A 371 ? 0.5233 0.5627 0.4709 -0.0313 -0.0966 -0.0589 371 VAL A CG1 2837 C CG2 . VAL A 371 ? 0.4941 0.5763 0.4822 -0.0267 -0.1019 -0.0556 371 VAL A CG2 2838 N N . THR A 372 ? 0.5381 0.5919 0.4857 -0.0512 -0.1255 -0.0769 372 THR A N 2839 C CA . THR A 372 ? 0.5568 0.5913 0.4811 -0.0564 -0.1301 -0.0840 372 THR A CA 2840 C C . THR A 372 ? 0.5687 0.6003 0.5004 -0.0718 -0.1312 -0.0915 372 THR A C 2841 O O . THR A 372 ? 0.5988 0.6055 0.5136 -0.0765 -0.1267 -0.0959 372 THR A O 2842 C CB . THR A 372 ? 0.5747 0.6161 0.4872 -0.0528 -0.1449 -0.0866 372 THR A CB 2843 O OG1 . THR A 372 ? 0.5615 0.6039 0.4668 -0.0395 -0.1443 -0.0785 372 THR A OG1 2844 C CG2 . THR A 372 ? 0.6066 0.6260 0.4904 -0.0573 -0.1483 -0.0943 372 THR A CG2 2845 N N . LEU A 373 ? 0.5560 0.6128 0.5133 -0.0799 -0.1368 -0.0932 373 LEU A N 2846 C CA . LEU A 373 ? 0.5610 0.6170 0.5277 -0.0970 -0.1373 -0.0997 373 LEU A CA 2847 C C . LEU A 373 ? 0.5713 0.6063 0.5362 -0.1014 -0.1228 -0.0960 373 LEU A C 2848 O O . LEU A 373 ? 0.5893 0.6037 0.5453 -0.1127 -0.1216 -0.1013 373 LEU A O 2849 C CB . LEU A 373 ? 0.5421 0.6343 0.5406 -0.1042 -0.1435 -0.1009 373 LEU A CB 2850 C CG . LEU A 373 ? 0.5527 0.6493 0.5640 -0.1245 -0.1450 -0.1077 373 LEU A CG 2851 C CD1 . LEU A 373 ? 0.5849 0.6755 0.5829 -0.1327 -0.1588 -0.1181 373 LEU A CD1 2852 C CD2 . LEU A 373 ? 0.5376 0.6734 0.5840 -0.1305 -0.1459 -0.1071 373 LEU A CD2 2853 N N . GLN A 374 ? 0.5616 0.6005 0.5337 -0.0923 -0.1126 -0.0872 374 GLN A N 2854 C CA . GLN A 374 ? 0.5839 0.6054 0.5549 -0.0952 -0.0997 -0.0824 374 GLN A CA 2855 C C . GLN A 374 ? 0.6087 0.5960 0.5541 -0.0899 -0.0944 -0.0831 374 GLN A C 2856 O O . GLN A 374 ? 0.6272 0.5943 0.5683 -0.0955 -0.0875 -0.0822 374 GLN A O 2857 C CB . GLN A 374 ? 0.5720 0.6079 0.5561 -0.0860 -0.0911 -0.0734 374 GLN A CB 2858 C CG . GLN A 374 ? 0.5730 0.6403 0.5850 -0.0928 -0.0914 -0.0724 374 GLN A CG 2859 C CD . GLN A 374 ? 0.5889 0.6527 0.6086 -0.1105 -0.0874 -0.0737 374 GLN A CD 2860 O OE1 . GLN A 374 ? 0.6080 0.6533 0.6212 -0.1132 -0.0775 -0.0686 374 GLN A OE1 2861 N NE2 . GLN A 374 ? 0.5939 0.6751 0.6271 -0.1232 -0.0956 -0.0805 374 GLN A NE2 2862 N N . TYR A 375 ? 0.6287 0.6096 0.5569 -0.0787 -0.0971 -0.0844 375 TYR A N 2863 C CA . TYR A 375 ? 0.6461 0.6000 0.5526 -0.0707 -0.0898 -0.0845 375 TYR A CA 2864 C C . TYR A 375 ? 0.6870 0.6220 0.5701 -0.0717 -0.0955 -0.0942 375 TYR A C 2865 O O . TYR A 375 ? 0.7103 0.6257 0.5750 -0.0636 -0.0895 -0.0956 375 TYR A O 2866 C CB . TYR A 375 ? 0.6318 0.5932 0.5368 -0.0564 -0.0844 -0.0771 375 TYR A CB 2867 C CG . TYR A 375 ? 0.6188 0.5876 0.5397 -0.0541 -0.0754 -0.0687 375 TYR A CG 2868 C CD1 . TYR A 375 ? 0.6140 0.5640 0.5285 -0.0509 -0.0658 -0.0658 375 TYR A CD1 2869 C CD2 . TYR A 375 ? 0.5904 0.5850 0.5321 -0.0545 -0.0767 -0.0641 375 TYR A CD2 2870 C CE1 . TYR A 375 ? 0.5918 0.5485 0.5186 -0.0490 -0.0585 -0.0580 375 TYR A CE1 2871 C CE2 . TYR A 375 ? 0.5675 0.5686 0.5214 -0.0527 -0.0681 -0.0572 375 TYR A CE2 2872 C CZ . TYR A 375 ? 0.5668 0.5487 0.5123 -0.0504 -0.0594 -0.0539 375 TYR A CZ 2873 O OH . TYR A 375 ? 0.5669 0.5550 0.5222 -0.0487 -0.0519 -0.0470 375 TYR A OH 2874 N N . THR A 376 ? 0.7078 0.6498 0.5919 -0.0817 -0.1068 -0.1015 376 THR A N 2875 C CA . THR A 376 ? 0.7434 0.6693 0.6041 -0.0837 -0.1135 -0.1118 376 THR A CA 2876 C C . THR A 376 ? 0.7891 0.6951 0.6471 -0.0977 -0.1150 -0.1201 376 THR A C 2877 O O . THR A 376 ? 0.8076 0.7256 0.6843 -0.1107 -0.1192 -0.1206 376 THR A O 2878 C CB . THR A 376 ? 0.7418 0.6895 0.6028 -0.0848 -0.1275 -0.1146 376 THR A CB 2879 O OG1 . THR A 376 ? 0.7301 0.6901 0.5890 -0.0713 -0.1262 -0.1066 376 THR A OG1 2880 C CG2 . THR A 376 ? 0.7637 0.6959 0.5995 -0.0890 -0.1359 -0.1262 376 THR A CG2 2881 N N . ASP A 377 ? 0.8323 0.7078 0.6673 -0.0951 -0.1112 -0.1271 377 ASP A N 2882 C CA . ASP A 377 ? 0.8689 0.7201 0.6959 -0.1080 -0.1143 -0.1372 377 ASP A CA 2883 C C . ASP A 377 ? 0.8845 0.7420 0.7009 -0.1157 -0.1281 -0.1482 377 ASP A C 2884 O O . ASP A 377 ? 0.9072 0.7570 0.7005 -0.1077 -0.1301 -0.1540 377 ASP A O 2885 C CB . ASP A 377 ? 0.9016 0.7172 0.7074 -0.0996 -0.1052 -0.1415 377 ASP A CB 2886 C CG . ASP A 377 ? 0.9424 0.7266 0.7372 -0.1118 -0.1081 -0.1525 377 ASP A CG 2887 O OD1 . ASP A 377 ? 0.9351 0.7243 0.7349 -0.1281 -0.1182 -0.1588 377 ASP A OD1 2888 O OD2 . ASP A 377 ? 0.9898 0.7437 0.7710 -0.1046 -0.1005 -0.1552 377 ASP A OD2 2889 N N . TRP A 378 ? 0.8770 0.7496 0.7098 -0.1315 -0.1375 -0.1513 378 TRP A N 2890 C CA . TRP A 378 ? 0.8904 0.7751 0.7167 -0.1390 -0.1527 -0.1611 378 TRP A CA 2891 C C . TRP A 378 ? 0.9590 0.8127 0.7605 -0.1475 -0.1570 -0.1759 378 TRP A C 2892 O O . TRP A 378 ? 0.9958 0.8536 0.7819 -0.1494 -0.1684 -0.1850 378 TRP A O 2893 C CB . TRP A 378 ? 0.8649 0.7828 0.7210 -0.1522 -0.1618 -0.1595 378 TRP A CB 2894 C CG . TRP A 378 ? 0.8211 0.7699 0.6980 -0.1413 -0.1589 -0.1470 378 TRP A CG 2895 C CD1 . TRP A 378 ? 0.7815 0.7408 0.6812 -0.1407 -0.1488 -0.1368 378 TRP A CD1 2896 C CD2 . TRP A 378 ? 0.7957 0.7658 0.6700 -0.1284 -0.1658 -0.1433 378 TRP A CD2 2897 N NE1 . TRP A 378 ? 0.7410 0.7273 0.6533 -0.1283 -0.1491 -0.1283 378 TRP A NE1 2898 C CE2 . TRP A 378 ? 0.7590 0.7512 0.6562 -0.1205 -0.1596 -0.1316 378 TRP A CE2 2899 C CE3 . TRP A 378 ? 0.8109 0.7819 0.6638 -0.1231 -0.1769 -0.1485 378 TRP A CE3 2900 C CZ2 . TRP A 378 ? 0.7483 0.7615 0.6485 -0.1072 -0.1644 -0.1252 378 TRP A CZ2 2901 C CZ3 . TRP A 378 ? 0.8004 0.7923 0.6552 -0.1102 -0.1817 -0.1409 378 TRP A CZ3 2902 C CH2 . TRP A 378 ? 0.7667 0.7785 0.6454 -0.1022 -0.1756 -0.1294 378 TRP A CH2 2903 N N . MET A 379 ? 1.0182 0.8394 0.8144 -0.1519 -0.1485 -0.1785 379 MET A N 2904 C CA . MET A 379 ? 1.0976 0.8821 0.8671 -0.1568 -0.1504 -0.1932 379 MET A CA 2905 C C . MET A 379 ? 1.1044 0.8782 0.8446 -0.1404 -0.1480 -0.1987 379 MET A C 2906 O O . MET A 379 ? 1.1258 0.8843 0.8425 -0.1442 -0.1549 -0.2127 379 MET A O 2907 C CB . MET A 379 ? 1.1527 0.9009 0.9204 -0.1591 -0.1397 -0.1924 379 MET A CB 2908 C CG . MET A 379 ? 1.1787 0.9256 0.9675 -0.1791 -0.1411 -0.1894 379 MET A CG 2909 S SD . MET A 379 ? 1.3017 1.0401 1.0864 -0.2049 -0.1559 -0.2059 379 MET A SD 2910 C CE . MET A 379 ? 1.3164 1.0116 1.0601 -0.1978 -0.1577 -0.2238 379 MET A CE 2911 N N . ASP A 380 ? 1.0996 0.8823 0.8413 -0.1233 -0.1380 -0.1878 380 ASP A N 2912 C CA . ASP A 380 ? 1.1267 0.8988 0.8431 -0.1072 -0.1313 -0.1910 380 ASP A CA 2913 C C . ASP A 380 ? 1.1222 0.9241 0.8476 -0.0949 -0.1282 -0.1774 380 ASP A C 2914 O O . ASP A 380 ? 1.1164 0.9175 0.8468 -0.0828 -0.1159 -0.1686 380 ASP A O 2915 C CB . ASP A 380 ? 1.1341 0.8736 0.8432 -0.0991 -0.1181 -0.1928 380 ASP A CB 2916 C CG . ASP A 380 ? 1.1281 0.8542 0.8108 -0.0836 -0.1101 -0.1997 380 ASP A CG 2917 O OD1 . ASP A 380 ? 1.1392 0.8701 0.8007 -0.0830 -0.1158 -0.2077 380 ASP A OD1 2918 O OD2 . ASP A 380 ? 1.0957 0.8066 0.7786 -0.0720 -0.0980 -0.1971 380 ASP A OD2 2919 N N . ASP A 381 ? 1.1419 0.9695 0.8695 -0.0983 -0.1400 -0.1759 381 ASP A N 2920 C CA . ASP A 381 ? 1.1161 0.9723 0.8568 -0.0893 -0.1396 -0.1621 381 ASP A CA 2921 C C . ASP A 381 ? 1.1109 0.9681 0.8274 -0.0764 -0.1365 -0.1602 381 ASP A C 2922 O O . ASP A 381 ? 1.0751 0.9522 0.7988 -0.0693 -0.1368 -0.1491 381 ASP A O 2923 C CB . ASP A 381 ? 1.1252 1.0109 0.8861 -0.0983 -0.1541 -0.1594 381 ASP A CB 2924 C CG . ASP A 381 ? 1.1748 1.0665 0.9162 -0.1024 -0.1697 -0.1682 381 ASP A CG 2925 O OD1 . ASP A 381 ? 1.2003 1.0700 0.9164 -0.1067 -0.1719 -0.1810 381 ASP A OD1 2926 O OD2 . ASP A 381 ? 1.1771 1.0954 0.9282 -0.1007 -0.1803 -0.1625 381 ASP A OD2 2927 N N . ASN A 382 ? 1.1545 0.9897 0.8418 -0.0738 -0.1331 -0.1711 382 ASN A N 2928 C CA . ASN A 382 ? 1.1426 0.9775 0.8051 -0.0626 -0.1274 -0.1695 382 ASN A CA 2929 C C . ASN A 382 ? 1.0961 0.9108 0.7469 -0.0529 -0.1107 -0.1734 382 ASN A C 2930 O O . ASN A 382 ? 1.1044 0.9152 0.7306 -0.0455 -0.1047 -0.1764 382 ASN A O 2931 C CB . ASN A 382 ? 1.1939 1.0275 0.8277 -0.0672 -0.1395 -0.1792 382 ASN A CB 2932 C CG . ASN A 382 ? 1.2054 1.0485 0.8183 -0.0582 -0.1379 -0.1722 382 ASN A CG 2933 O OD1 . ASN A 382 ? 1.1364 0.9950 0.7629 -0.0517 -0.1342 -0.1580 382 ASN A OD1 2934 N ND2 . ASN A 382 ? 1.2479 1.0802 0.8259 -0.0584 -0.1403 -0.1823 382 ASN A ND2 2935 N N . ASN A 383 ? 1.0279 0.8307 0.6964 -0.0528 -0.1034 -0.1730 383 ASN A N 2936 C CA . ASN A 383 ? 0.9880 0.7754 0.6522 -0.0416 -0.0882 -0.1746 383 ASN A CA 2937 C C . ASN A 383 ? 0.9245 0.7312 0.6009 -0.0312 -0.0787 -0.1603 383 ASN A C 2938 O O . ASN A 383 ? 0.8849 0.7073 0.5858 -0.0328 -0.0802 -0.1484 383 ASN A O 2939 C CB . ASN A 383 ? 0.9888 0.7557 0.6671 -0.0450 -0.0856 -0.1776 383 ASN A CB 2940 C CG . ASN A 383 ? 0.9931 0.7472 0.6730 -0.0316 -0.0710 -0.1766 383 ASN A CG 2941 O OD1 . ASN A 383 ? 0.9938 0.7643 0.6826 -0.0220 -0.0627 -0.1665 383 ASN A OD1 2942 N ND2 . ASN A 383 ? 1.0262 0.7510 0.6987 -0.0308 -0.0684 -0.1871 383 ASN A ND2 2943 N N . GLY A 384 ? 0.9013 0.7071 0.5603 -0.0212 -0.0686 -0.1622 384 GLY A N 2944 C CA . GLY A 384 ? 0.8527 0.6762 0.5205 -0.0128 -0.0593 -0.1500 384 GLY A CA 2945 C C . GLY A 384 ? 0.8065 0.6304 0.4985 -0.0064 -0.0501 -0.1432 384 GLY A C 2946 O O . GLY A 384 ? 0.7797 0.6211 0.4875 -0.0034 -0.0467 -0.1309 384 GLY A O 2947 N N . ILE A 385 ? 0.8130 0.6166 0.5070 -0.0042 -0.0465 -0.1510 385 ILE A N 2948 C CA . ILE A 385 ? 0.7955 0.5972 0.5105 0.0023 -0.0390 -0.1445 385 ILE A CA 2949 C C . ILE A 385 ? 0.7754 0.5848 0.5137 -0.0062 -0.0460 -0.1342 385 ILE A C 2950 O O . ILE A 385 ? 0.7627 0.5863 0.5193 -0.0024 -0.0417 -0.1229 385 ILE A O 2951 C CB . ILE A 385 ? 0.8183 0.5927 0.5268 0.0084 -0.0340 -0.1555 385 ILE A CB 2952 C CG1 . ILE A 385 ? 0.8421 0.6142 0.5308 0.0194 -0.0242 -0.1655 385 ILE A CG1 2953 C CG2 . ILE A 385 ? 0.7934 0.5644 0.5235 0.0142 -0.0291 -0.1472 385 ILE A CG2 2954 C CD1 . ILE A 385 ? 0.8664 0.6129 0.5487 0.0291 -0.0181 -0.1775 385 ILE A CD1 2955 N N . LYS A 386 ? 0.7894 0.5912 0.5272 -0.0182 -0.0565 -0.1385 386 LYS A N 2956 C CA . LYS A 386 ? 0.7658 0.5783 0.5260 -0.0277 -0.0629 -0.1299 386 LYS A CA 2957 C C . LYS A 386 ? 0.7268 0.5683 0.4975 -0.0276 -0.0659 -0.1195 386 LYS A C 2958 O O . LYS A 386 ? 0.7157 0.5708 0.5073 -0.0276 -0.0641 -0.1092 386 LYS A O 2959 C CB . LYS A 386 ? 0.7929 0.5941 0.5502 -0.0419 -0.0737 -0.1381 386 LYS A CB 2960 C CG . LYS A 386 ? 0.8290 0.5980 0.5793 -0.0435 -0.0711 -0.1465 386 LYS A CG 2961 C CD . LYS A 386 ? 0.8790 0.6358 0.6251 -0.0595 -0.0819 -0.1556 386 LYS A CD 2962 C CE . LYS A 386 ? 0.9267 0.6456 0.6602 -0.0602 -0.0794 -0.1657 386 LYS A CE 2963 N NZ . LYS A 386 ? 0.9682 0.6728 0.6979 -0.0779 -0.0898 -0.1749 386 LYS A NZ 2964 N N . ASN A 387 ? 0.7196 0.5689 0.4744 -0.0271 -0.0704 -0.1222 387 ASN A N 2965 C CA . ASN A 387 ? 0.7012 0.5735 0.4620 -0.0247 -0.0727 -0.1123 387 ASN A CA 2966 C C . ASN A 387 ? 0.6722 0.5528 0.4421 -0.0151 -0.0614 -0.1029 387 ASN A C 2967 O O . ASN A 387 ? 0.6379 0.5350 0.4243 -0.0145 -0.0622 -0.0929 387 ASN A O 2968 C CB . ASN A 387 ? 0.7336 0.6076 0.4697 -0.0242 -0.0779 -0.1163 387 ASN A CB 2969 C CG . ASN A 387 ? 0.7665 0.6421 0.4979 -0.0342 -0.0928 -0.1224 387 ASN A CG 2970 O OD1 . ASN A 387 ? 0.7905 0.6740 0.5424 -0.0416 -0.0998 -0.1207 387 ASN A OD1 2971 N ND2 . ASN A 387 ? 0.7994 0.6693 0.5040 -0.0349 -0.0977 -0.1296 387 ASN A ND2 2972 N N . ARG A 388 ? 0.6794 0.5494 0.4385 -0.0073 -0.0509 -0.1069 388 ARG A N 2973 C CA . ARG A 388 ? 0.6555 0.5350 0.4235 0.0013 -0.0402 -0.0992 388 ARG A CA 2974 C C . ARG A 388 ? 0.6309 0.5122 0.4227 0.0014 -0.0384 -0.0929 388 ARG A C 2975 O O . ARG A 388 ? 0.6061 0.5030 0.4132 0.0025 -0.0371 -0.0831 388 ARG A O 2976 C CB . ARG A 388 ? 0.6711 0.5415 0.4248 0.0100 -0.0294 -0.1064 388 ARG A CB 2977 C CG . ARG A 388 ? 0.6446 0.5285 0.4079 0.0181 -0.0186 -0.0992 388 ARG A CG 2978 C CD . ARG A 388 ? 0.6557 0.5315 0.4133 0.0277 -0.0080 -0.1073 388 ARG A CD 2979 N NE . ARG A 388 ? 0.6652 0.5236 0.4309 0.0298 -0.0093 -0.1115 388 ARG A NE 2980 C CZ . ARG A 388 ? 0.6788 0.5193 0.4345 0.0363 -0.0053 -0.1227 388 ARG A CZ 2981 N NH1 . ARG A 388 ? 0.6953 0.5355 0.4330 0.0416 0.0014 -0.1320 388 ARG A NH1 2982 N NH2 . ARG A 388 ? 0.6754 0.4972 0.4382 0.0375 -0.0077 -0.1246 388 ARG A NH2 2983 N N . ASP A 389 ? 0.6407 0.5042 0.4339 -0.0002 -0.0385 -0.0984 389 ASP A N 2984 C CA . ASP A 389 ? 0.6317 0.4934 0.4437 -0.0004 -0.0364 -0.0921 389 ASP A CA 2985 C C . ASP A 389 ? 0.6262 0.5026 0.4552 -0.0095 -0.0432 -0.0846 389 ASP A C 2986 O O . ASP A 389 ? 0.6012 0.4864 0.4464 -0.0083 -0.0400 -0.0762 389 ASP A O 2987 C CB . ASP A 389 ? 0.6531 0.4884 0.4600 -0.0013 -0.0362 -0.0992 389 ASP A CB 2988 C CG . ASP A 389 ? 0.6684 0.4906 0.4642 0.0113 -0.0278 -0.1056 389 ASP A CG 2989 O OD1 . ASP A 389 ? 0.6415 0.4784 0.4401 0.0205 -0.0205 -0.1020 389 ASP A OD1 2990 O OD2 . ASP A 389 ? 0.6935 0.4907 0.4784 0.0118 -0.0284 -0.1149 389 ASP A OD2 2991 N N . GLY A 390 ? 0.6486 0.5292 0.4740 -0.0181 -0.0526 -0.0883 390 GLY A N 2992 C CA . GLY A 390 ? 0.6441 0.5426 0.4869 -0.0258 -0.0594 -0.0827 390 GLY A CA 2993 C C . GLY A 390 ? 0.6337 0.5533 0.4864 -0.0200 -0.0575 -0.0736 390 GLY A C 2994 O O . GLY A 390 ? 0.6285 0.5606 0.4995 -0.0217 -0.0567 -0.0670 390 GLY A O 2995 N N . LEU A 391 ? 0.6502 0.5728 0.4895 -0.0139 -0.0564 -0.0735 391 LEU A N 2996 C CA . LEU A 391 ? 0.6402 0.5783 0.4862 -0.0086 -0.0541 -0.0650 391 LEU A CA 2997 C C . LEU A 391 ? 0.6155 0.5558 0.4729 -0.0032 -0.0442 -0.0593 391 LEU A C 2998 O O . LEU A 391 ? 0.5950 0.5485 0.4669 -0.0022 -0.0434 -0.0524 391 LEU A O 2999 C CB . LEU A 391 ? 0.6628 0.5998 0.4888 -0.0043 -0.0535 -0.0655 391 LEU A CB 3000 C CG . LEU A 391 ? 0.6872 0.6297 0.5045 -0.0075 -0.0649 -0.0657 391 LEU A CG 3001 C CD1 . LEU A 391 ? 0.7007 0.6378 0.4929 -0.0042 -0.0631 -0.0662 391 LEU A CD1 3002 C CD2 . LEU A 391 ? 0.6905 0.6493 0.5260 -0.0068 -0.0697 -0.0576 391 LEU A CD2 3003 N N . ASP A 392 ? 0.6314 0.5590 0.4820 0.0010 -0.0370 -0.0628 392 ASP A N 3004 C CA . ASP A 392 ? 0.6399 0.5699 0.5013 0.0066 -0.0291 -0.0579 392 ASP A CA 3005 C C . ASP A 392 ? 0.6050 0.5403 0.4841 0.0016 -0.0315 -0.0528 392 ASP A C 3006 O O . ASP A 392 ? 0.6058 0.5541 0.4970 0.0034 -0.0290 -0.0461 392 ASP A O 3007 C CB . ASP A 392 ? 0.7109 0.6247 0.5638 0.0122 -0.0233 -0.0637 392 ASP A CB 3008 C CG . ASP A 392 ? 0.7439 0.6632 0.6052 0.0207 -0.0152 -0.0593 392 ASP A CG 3009 O OD1 . ASP A 392 ? 0.7600 0.6866 0.6358 0.0201 -0.0149 -0.0523 392 ASP A OD1 3010 O OD2 . ASP A 392 ? 0.7958 0.7136 0.6493 0.0280 -0.0090 -0.0634 392 ASP A OD2 3011 N N . ASP A 393 ? 0.5870 0.5122 0.4667 -0.0057 -0.0360 -0.0564 393 ASP A N 3012 C CA . ASP A 393 ? 0.5730 0.5026 0.4678 -0.0123 -0.0371 -0.0519 393 ASP A CA 3013 C C . ASP A 393 ? 0.5430 0.4950 0.4514 -0.0155 -0.0409 -0.0477 393 ASP A C 3014 O O . ASP A 393 ? 0.5081 0.4705 0.4298 -0.0162 -0.0382 -0.0420 393 ASP A O 3015 C CB . ASP A 393 ? 0.6091 0.5234 0.5007 -0.0220 -0.0416 -0.0572 393 ASP A CB 3016 C CG . ASP A 393 ? 0.6458 0.5343 0.5256 -0.0183 -0.0377 -0.0608 393 ASP A CG 3017 O OD1 . ASP A 393 ? 0.6785 0.5645 0.5576 -0.0085 -0.0313 -0.0575 393 ASP A OD1 3018 O OD2 . ASP A 393 ? 0.6778 0.5485 0.5493 -0.0249 -0.0415 -0.0675 393 ASP A OD2 3019 N N . ILE A 394 ? 0.5434 0.5023 0.4477 -0.0167 -0.0476 -0.0508 394 ILE A N 3020 C CA . ILE A 394 ? 0.5189 0.4980 0.4359 -0.0176 -0.0524 -0.0475 394 ILE A CA 3021 C C . ILE A 394 ? 0.4922 0.4804 0.4153 -0.0102 -0.0465 -0.0409 394 ILE A C 3022 O O . ILE A 394 ? 0.4705 0.4721 0.4088 -0.0111 -0.0457 -0.0373 394 ILE A O 3023 C CB . ILE A 394 ? 0.5328 0.5151 0.4405 -0.0174 -0.0613 -0.0511 394 ILE A CB 3024 C CG1 . ILE A 394 ? 0.5576 0.5373 0.4650 -0.0269 -0.0692 -0.0579 394 ILE A CG1 3025 C CG2 . ILE A 394 ? 0.5114 0.5117 0.4297 -0.0137 -0.0656 -0.0466 394 ILE A CG2 3026 C CD1 . ILE A 394 ? 0.5836 0.5621 0.4765 -0.0272 -0.0787 -0.0629 394 ILE A CD1 3027 N N . VAL A 395 ? 0.4896 0.4708 0.4006 -0.0036 -0.0419 -0.0401 395 VAL A N 3028 C CA . VAL A 395 ? 0.4649 0.4543 0.3802 0.0021 -0.0372 -0.0346 395 VAL A CA 3029 C C . VAL A 395 ? 0.4516 0.4436 0.3778 0.0029 -0.0308 -0.0311 395 VAL A C 3030 O O . VAL A 395 ? 0.4341 0.4378 0.3714 0.0039 -0.0296 -0.0272 395 VAL A O 3031 C CB . VAL A 395 ? 0.4711 0.4540 0.3709 0.0070 -0.0332 -0.0350 395 VAL A CB 3032 C CG1 . VAL A 395 ? 0.4557 0.4467 0.3605 0.0111 -0.0281 -0.0295 395 VAL A CG1 3033 C CG2 . VAL A 395 ? 0.4843 0.4641 0.3701 0.0059 -0.0400 -0.0373 395 VAL A CG2 3034 N N . GLY A 396 ? 0.4617 0.4418 0.3837 0.0030 -0.0272 -0.0327 396 GLY A N 3035 C CA . GLY A 396 ? 0.4403 0.4203 0.3696 0.0043 -0.0221 -0.0287 396 GLY A CA 3036 C C . GLY A 396 ? 0.4537 0.4411 0.3951 -0.0026 -0.0239 -0.0262 396 GLY A C 3037 O O . GLY A 396 ? 0.4789 0.4759 0.4287 -0.0017 -0.0207 -0.0217 396 GLY A O 3038 N N . ASP A 397 ? 0.4663 0.4507 0.4085 -0.0102 -0.0286 -0.0295 397 ASP A N 3039 C CA . ASP A 397 ? 0.4684 0.4629 0.4233 -0.0183 -0.0295 -0.0278 397 ASP A CA 3040 C C . ASP A 397 ? 0.4621 0.4784 0.4298 -0.0168 -0.0305 -0.0263 397 ASP A C 3041 O O . ASP A 397 ? 0.4673 0.4943 0.4449 -0.0185 -0.0269 -0.0231 397 ASP A O 3042 C CB . ASP A 397 ? 0.4869 0.4766 0.4417 -0.0280 -0.0351 -0.0327 397 ASP A CB 3043 C CG . ASP A 397 ? 0.5064 0.4716 0.4495 -0.0313 -0.0338 -0.0344 397 ASP A CG 3044 O OD1 . ASP A 397 ? 0.4955 0.4497 0.4343 -0.0272 -0.0285 -0.0301 397 ASP A OD1 3045 O OD2 . ASP A 397 ? 0.5363 0.4924 0.4742 -0.0376 -0.0389 -0.0402 397 ASP A OD2 3046 N N . HIS A 398 ? 0.4621 0.4836 0.4281 -0.0130 -0.0355 -0.0288 398 HIS A N 3047 C CA . HIS A 398 ? 0.4463 0.4857 0.4238 -0.0101 -0.0378 -0.0281 398 HIS A CA 3048 C C . HIS A 398 ? 0.4254 0.4682 0.4042 -0.0037 -0.0323 -0.0241 398 HIS A C 3049 O O . HIS A 398 ? 0.4393 0.4956 0.4298 -0.0031 -0.0309 -0.0233 398 HIS A O 3050 C CB . HIS A 398 ? 0.4526 0.4929 0.4251 -0.0071 -0.0458 -0.0307 398 HIS A CB 3051 C CG . HIS A 398 ? 0.4465 0.5012 0.4292 -0.0020 -0.0493 -0.0298 398 HIS A CG 3052 N ND1 . HIS A 398 ? 0.4405 0.5129 0.4413 -0.0034 -0.0488 -0.0306 398 HIS A ND1 3053 C CD2 . HIS A 398 ? 0.4492 0.5020 0.4257 0.0046 -0.0535 -0.0285 398 HIS A CD2 3054 C CE1 . HIS A 398 ? 0.4254 0.5060 0.4317 0.0036 -0.0529 -0.0305 398 HIS A CE1 3055 N NE2 . HIS A 398 ? 0.4397 0.5071 0.4308 0.0083 -0.0562 -0.0287 398 HIS A NE2 3056 N N . ASN A 399 ? 0.4223 0.4541 0.3898 0.0008 -0.0288 -0.0225 399 ASN A N 3057 C CA . ASN A 399 ? 0.4136 0.4495 0.3822 0.0060 -0.0247 -0.0195 399 ASN A CA 3058 C C . ASN A 399 ? 0.4119 0.4486 0.3830 0.0061 -0.0186 -0.0166 399 ASN A C 3059 O O . ASN A 399 ? 0.3922 0.4363 0.3676 0.0087 -0.0159 -0.0149 399 ASN A O 3060 C CB . ASN A 399 ? 0.4248 0.4524 0.3812 0.0102 -0.0244 -0.0193 399 ASN A CB 3061 C CG . ASN A 399 ? 0.4299 0.4574 0.3823 0.0112 -0.0309 -0.0203 399 ASN A CG 3062 O OD1 . ASN A 399 ? 0.4125 0.4460 0.3702 0.0137 -0.0330 -0.0190 399 ASN A OD1 3063 N ND2 . ASN A 399 ? 0.4408 0.4605 0.3828 0.0097 -0.0348 -0.0228 399 ASN A ND2 3064 N N . VAL A 400 ? 0.4193 0.4471 0.3867 0.0034 -0.0169 -0.0160 400 VAL A N 3065 C CA . VAL A 400 ? 0.4264 0.4520 0.3930 0.0050 -0.0123 -0.0123 400 VAL A CA 3066 C C . VAL A 400 ? 0.4496 0.4717 0.4180 -0.0012 -0.0114 -0.0101 400 VAL A C 3067 O O . VAL A 400 ? 0.4574 0.4882 0.4308 -0.0033 -0.0087 -0.0071 400 VAL A O 3068 C CB . VAL A 400 ? 0.4384 0.4529 0.3958 0.0107 -0.0104 -0.0125 400 VAL A CB 3069 C CG1 . VAL A 400 ? 0.4367 0.4499 0.3939 0.0138 -0.0072 -0.0083 400 VAL A CG1 3070 C CG2 . VAL A 400 ? 0.4320 0.4513 0.3872 0.0150 -0.0100 -0.0140 400 VAL A CG2 3071 N N . ILE A 401 ? 0.4659 0.4743 0.4287 -0.0051 -0.0133 -0.0117 401 ILE A N 3072 C CA . ILE A 401 ? 0.4946 0.4948 0.4564 -0.0120 -0.0119 -0.0085 401 ILE A CA 3073 C C . ILE A 401 ? 0.5029 0.5183 0.4755 -0.0208 -0.0114 -0.0082 401 ILE A C 3074 O O . ILE A 401 ? 0.5344 0.5546 0.5088 -0.0239 -0.0075 -0.0036 401 ILE A O 3075 C CB . ILE A 401 ? 0.5193 0.4986 0.4721 -0.0151 -0.0143 -0.0111 401 ILE A CB 3076 C CG1 . ILE A 401 ? 0.5291 0.4944 0.4719 -0.0050 -0.0135 -0.0118 401 ILE A CG1 3077 C CG2 . ILE A 401 ? 0.5352 0.5041 0.4864 -0.0244 -0.0130 -0.0069 401 ILE A CG2 3078 C CD1 . ILE A 401 ? 0.5554 0.4976 0.4877 -0.0059 -0.0155 -0.0157 401 ILE A CD1 3079 N N . CYS A 402 ? 0.5015 0.5262 0.4814 -0.0244 -0.0153 -0.0131 402 CYS A N 3080 C CA . CYS A 402 ? 0.4922 0.5344 0.4851 -0.0326 -0.0147 -0.0139 402 CYS A CA 3081 C C . CYS A 402 ? 0.4829 0.5451 0.4852 -0.0288 -0.0111 -0.0130 402 CYS A C 3082 O O . CYS A 402 ? 0.4912 0.5665 0.5017 -0.0355 -0.0073 -0.0122 402 CYS A O 3083 C CB . CYS A 402 ? 0.4897 0.5385 0.4894 -0.0369 -0.0211 -0.0199 402 CYS A CB 3084 S SG . CYS A 402 ? 0.5165 0.5423 0.5059 -0.0459 -0.0243 -0.0219 402 CYS A SG 3085 N N . PRO A 403 ? 0.4674 0.5321 0.4683 -0.0190 -0.0119 -0.0137 403 PRO A N 3086 C CA . PRO A 403 ? 0.4539 0.5331 0.4610 -0.0155 -0.0081 -0.0132 403 PRO A CA 3087 C C . PRO A 403 ? 0.4463 0.5224 0.4470 -0.0171 -0.0023 -0.0080 403 PRO A C 3088 O O . PRO A 403 ? 0.4371 0.5268 0.4430 -0.0196 0.0019 -0.0078 403 PRO A O 3089 C CB . PRO A 403 ? 0.4516 0.5282 0.4554 -0.0063 -0.0107 -0.0147 403 PRO A CB 3090 C CG . PRO A 403 ? 0.4579 0.5287 0.4601 -0.0060 -0.0169 -0.0176 403 PRO A CG 3091 C CD . PRO A 403 ? 0.4769 0.5362 0.4738 -0.0128 -0.0171 -0.0167 403 PRO A CD 3092 N N . LEU A 404 ? 0.4430 0.5018 0.4320 -0.0150 -0.0024 -0.0041 404 LEU A N 3093 C CA . LEU A 404 ? 0.4350 0.4887 0.4161 -0.0152 0.0013 0.0018 404 LEU A CA 3094 C C . LEU A 404 ? 0.4643 0.5152 0.4437 -0.0257 0.0042 0.0056 404 LEU A C 3095 O O . LEU A 404 ? 0.4874 0.5419 0.4627 -0.0284 0.0082 0.0102 404 LEU A O 3096 C CB . LEU A 404 ? 0.4295 0.4661 0.4002 -0.0086 -0.0005 0.0044 404 LEU A CB 3097 C CG . LEU A 404 ? 0.4386 0.4679 0.4002 -0.0072 0.0013 0.0111 404 LEU A CG 3098 C CD1 . LEU A 404 ? 0.4400 0.4648 0.3976 0.0030 -0.0005 0.0115 404 LEU A CD1 3099 C CD2 . LEU A 404 ? 0.4608 0.4720 0.4145 -0.0136 0.0014 0.0159 404 LEU A CD2 3100 N N . MET A 405 ? 0.4661 0.5105 0.4477 -0.0327 0.0022 0.0038 405 MET A N 3101 C CA . MET A 405 ? 0.4798 0.5209 0.4601 -0.0449 0.0053 0.0075 405 MET A CA 3102 C C . MET A 405 ? 0.4778 0.5444 0.4707 -0.0515 0.0098 0.0053 405 MET A C 3103 O O . MET A 405 ? 0.4980 0.5669 0.4884 -0.0611 0.0151 0.0098 405 MET A O 3104 C CB . MET A 405 ? 0.4846 0.5114 0.4640 -0.0517 0.0014 0.0051 405 MET A CB 3105 C CG . MET A 405 ? 0.5101 0.5087 0.4748 -0.0461 -0.0015 0.0075 405 MET A CG 3106 S SD . MET A 405 ? 0.5267 0.5065 0.4759 -0.0453 0.0018 0.0180 405 MET A SD 3107 C CE . MET A 405 ? 0.5440 0.5224 0.4935 -0.0645 0.0058 0.0222 405 MET A CE 3108 N N . HIS A 406 ? 0.4766 0.5620 0.4823 -0.0460 0.0081 -0.0014 406 HIS A N 3109 C CA . HIS A 406 ? 0.4838 0.5954 0.5034 -0.0495 0.0124 -0.0051 406 HIS A CA 3110 C C . HIS A 406 ? 0.4845 0.6019 0.4979 -0.0459 0.0181 -0.0022 406 HIS A C 3111 O O . HIS A 406 ? 0.4744 0.6036 0.4887 -0.0533 0.0249 -0.0006 406 HIS A O 3112 C CB . HIS A 406 ? 0.4754 0.6018 0.5092 -0.0423 0.0074 -0.0130 406 HIS A CB 3113 C CG . HIS A 406 ? 0.4769 0.6305 0.5261 -0.0418 0.0112 -0.0182 406 HIS A CG 3114 N ND1 . HIS A 406 ? 0.4930 0.6666 0.5574 -0.0507 0.0134 -0.0217 406 HIS A ND1 3115 C CD2 . HIS A 406 ? 0.4729 0.6377 0.5258 -0.0329 0.0132 -0.0217 406 HIS A CD2 3116 C CE1 . HIS A 406 ? 0.4895 0.6869 0.5670 -0.0462 0.0170 -0.0273 406 HIS A CE1 3117 N NE2 . HIS A 406 ? 0.4854 0.6761 0.5551 -0.0352 0.0168 -0.0274 406 HIS A NE2 3118 N N . PHE A 407 ? 0.4789 0.5878 0.4850 -0.0353 0.0154 -0.0018 407 PHE A N 3119 C CA . PHE A 407 ? 0.4960 0.6081 0.4942 -0.0316 0.0191 0.0006 407 PHE A CA 3120 C C . PHE A 407 ? 0.5097 0.6124 0.4942 -0.0391 0.0232 0.0091 407 PHE A C 3121 O O . PHE A 407 ? 0.4863 0.6001 0.4674 -0.0427 0.0289 0.0105 407 PHE A O 3122 C CB . PHE A 407 ? 0.5066 0.6085 0.4988 -0.0211 0.0145 0.0005 407 PHE A CB 3123 C CG . PHE A 407 ? 0.5166 0.6223 0.5011 -0.0174 0.0168 0.0021 407 PHE A CG 3124 C CD1 . PHE A 407 ? 0.5129 0.6345 0.5034 -0.0146 0.0193 -0.0038 407 PHE A CD1 3125 C CD2 . PHE A 407 ? 0.5440 0.6370 0.5152 -0.0160 0.0158 0.0090 407 PHE A CD2 3126 C CE1 . PHE A 407 ? 0.5191 0.6440 0.5014 -0.0119 0.0208 -0.0034 407 PHE A CE1 3127 C CE2 . PHE A 407 ? 0.5552 0.6533 0.5191 -0.0128 0.0167 0.0102 407 PHE A CE2 3128 C CZ . PHE A 407 ? 0.5316 0.6457 0.5005 -0.0114 0.0193 0.0038 407 PHE A CZ 3129 N N . VAL A 408 ? 0.5257 0.6067 0.5012 -0.0413 0.0201 0.0146 408 VAL A N 3130 C CA . VAL A 408 ? 0.5601 0.6261 0.5202 -0.0473 0.0224 0.0240 408 VAL A CA 3131 C C . VAL A 408 ? 0.5778 0.6529 0.5390 -0.0615 0.0293 0.0264 408 VAL A C 3132 O O . VAL A 408 ? 0.5988 0.6743 0.5483 -0.0661 0.0341 0.0328 408 VAL A O 3133 C CB . VAL A 408 ? 0.5933 0.6319 0.5445 -0.0457 0.0173 0.0282 408 VAL A CB 3134 C CG1 . VAL A 408 ? 0.6456 0.6658 0.5828 -0.0556 0.0196 0.0376 408 VAL A CG1 3135 C CG2 . VAL A 408 ? 0.6030 0.6331 0.5478 -0.0324 0.0128 0.0292 408 VAL A CG2 3136 N N . ASN A 409 ? 0.5786 0.6617 0.5533 -0.0690 0.0297 0.0215 409 ASN A N 3137 C CA . ASN A 409 ? 0.5976 0.6925 0.5764 -0.0843 0.0368 0.0230 409 ASN A CA 3138 C C . ASN A 409 ? 0.5819 0.7060 0.5681 -0.0846 0.0443 0.0190 409 ASN A C 3139 O O . ASN A 409 ? 0.5878 0.7194 0.5685 -0.0956 0.0524 0.0232 409 ASN A O 3140 C CB . ASN A 409 ? 0.6065 0.7069 0.6009 -0.0921 0.0344 0.0173 409 ASN A CB 3141 C CG . ASN A 409 ? 0.6261 0.6960 0.6107 -0.0950 0.0284 0.0209 409 ASN A CG 3142 O OD1 . ASN A 409 ? 0.6405 0.6872 0.6086 -0.1016 0.0299 0.0297 409 ASN A OD1 3143 N ND2 . ASN A 409 ? 0.6123 0.6803 0.6055 -0.0895 0.0213 0.0139 409 ASN A ND2 3144 N N . LYS A 410 ? 0.5463 0.6854 0.5439 -0.0726 0.0418 0.0105 410 LYS A N 3145 C CA . LYS A 410 ? 0.5377 0.7022 0.5419 -0.0702 0.0481 0.0049 410 LYS A CA 3146 C C . LYS A 410 ? 0.5475 0.7060 0.5324 -0.0674 0.0512 0.0103 410 LYS A C 3147 O O . LYS A 410 ? 0.5653 0.7390 0.5464 -0.0732 0.0596 0.0104 410 LYS A O 3148 C CB . LYS A 410 ? 0.5229 0.7001 0.5429 -0.0577 0.0435 -0.0054 410 LYS A CB 3149 C CG . LYS A 410 ? 0.5385 0.7277 0.5787 -0.0597 0.0401 -0.0117 410 LYS A CG 3150 C CD . LYS A 410 ? 0.5514 0.7673 0.6055 -0.0705 0.0483 -0.0152 410 LYS A CD 3151 C CE . LYS A 410 ? 0.5510 0.7888 0.6299 -0.0671 0.0445 -0.0248 410 LYS A CE 3152 N NZ . LYS A 410 ? 0.5605 0.8317 0.6556 -0.0733 0.0539 -0.0308 410 LYS A NZ 3153 N N . TYR A 411 ? 0.5183 0.6565 0.4912 -0.0586 0.0445 0.0145 411 TYR A N 3154 C CA . TYR A 411 ? 0.5061 0.6407 0.4621 -0.0546 0.0454 0.0187 411 TYR A CA 3155 C C . TYR A 411 ? 0.5374 0.6629 0.4754 -0.0655 0.0502 0.0294 411 TYR A C 3156 O O . TYR A 411 ? 0.5490 0.6830 0.4753 -0.0678 0.0554 0.0314 411 TYR A O 3157 C CB . TYR A 411 ? 0.4866 0.6039 0.4358 -0.0434 0.0368 0.0209 411 TYR A CB 3158 C CG . TYR A 411 ? 0.4786 0.5965 0.4130 -0.0388 0.0364 0.0237 411 TYR A CG 3159 C CD1 . TYR A 411 ? 0.4598 0.5926 0.3989 -0.0324 0.0367 0.0152 411 TYR A CD1 3160 C CD2 . TYR A 411 ? 0.4933 0.5960 0.4083 -0.0411 0.0351 0.0346 411 TYR A CD2 3161 C CE1 . TYR A 411 ? 0.4628 0.5972 0.3883 -0.0291 0.0356 0.0167 411 TYR A CE1 3162 C CE2 . TYR A 411 ? 0.4994 0.6043 0.4006 -0.0368 0.0335 0.0370 411 TYR A CE2 3163 C CZ . TYR A 411 ? 0.4894 0.6111 0.3960 -0.0313 0.0337 0.0276 411 TYR A CZ 3164 O OH . TYR A 411 ? 0.4819 0.6067 0.3744 -0.0279 0.0314 0.0291 411 TYR A OH 3165 N N . THR A 412 ? 0.5519 0.6584 0.4861 -0.0724 0.0483 0.0363 412 THR A N 3166 C CA . THR A 412 ? 0.5818 0.6705 0.4954 -0.0821 0.0509 0.0488 412 THR A CA 3167 C C . THR A 412 ? 0.5948 0.7007 0.5053 -0.0965 0.0622 0.0505 412 THR A C 3168 O O . THR A 412 ? 0.6158 0.7107 0.5049 -0.1034 0.0654 0.0610 412 THR A O 3169 C CB . THR A 412 ? 0.5953 0.6567 0.5063 -0.0861 0.0459 0.0544 412 THR A CB 3170 O OG1 . THR A 412 ? 0.5834 0.6275 0.4915 -0.0719 0.0366 0.0546 412 THR A OG1 3171 C CG2 . THR A 412 ? 0.6258 0.6663 0.5162 -0.0988 0.0492 0.0674 412 THR A CG2 3172 N N . LYS A 413 ? 0.6010 0.7343 0.5323 -0.1007 0.0681 0.0404 413 LYS A N 3173 C CA . LYS A 413 ? 0.6478 0.8037 0.5795 -0.1138 0.0802 0.0398 413 LYS A CA 3174 C C . LYS A 413 ? 0.6228 0.7900 0.5396 -0.1102 0.0855 0.0399 413 LYS A C 3175 O O . LYS A 413 ? 0.6344 0.8092 0.5389 -0.1222 0.0951 0.0449 413 LYS A O 3176 C CB . LYS A 413 ? 0.6842 0.8712 0.6451 -0.1157 0.0845 0.0270 413 LYS A CB 3177 C CG . LYS A 413 ? 0.7608 0.9440 0.7348 -0.1270 0.0832 0.0277 413 LYS A CG 3178 C CD . LYS A 413 ? 0.8050 1.0197 0.8098 -0.1252 0.0842 0.0143 413 LYS A CD 3179 C CE . LYS A 413 ? 0.8357 1.0437 0.8540 -0.1324 0.0783 0.0134 413 LYS A CE 3180 N NZ . LYS A 413 ? 0.8302 1.0615 0.8757 -0.1232 0.0733 0.0006 413 LYS A NZ 3181 N N . PHE A 414 ? 0.5965 0.7650 0.5138 -0.0949 0.0793 0.0340 414 PHE A N 3182 C CA . PHE A 414 ? 0.5908 0.7701 0.4946 -0.0902 0.0827 0.0317 414 PHE A CA 3183 C C . PHE A 414 ? 0.5959 0.7535 0.4775 -0.0821 0.0739 0.0398 414 PHE A C 3184 O O . PHE A 414 ? 0.6157 0.7790 0.4805 -0.0810 0.0762 0.0405 414 PHE A O 3185 C CB . PHE A 414 ? 0.5641 0.7656 0.4871 -0.0792 0.0829 0.0161 414 PHE A CB 3186 C CG . PHE A 414 ? 0.5577 0.7868 0.5028 -0.0842 0.0916 0.0062 414 PHE A CG 3187 C CD1 . PHE A 414 ? 0.5715 0.8232 0.5127 -0.0924 0.1041 0.0032 414 PHE A CD1 3188 C CD2 . PHE A 414 ? 0.5388 0.7731 0.5089 -0.0799 0.0871 -0.0008 414 PHE A CD2 3189 C CE1 . PHE A 414 ? 0.5721 0.8530 0.5365 -0.0959 0.1125 -0.0071 414 PHE A CE1 3190 C CE2 . PHE A 414 ? 0.5343 0.7966 0.5269 -0.0831 0.0940 -0.0104 414 PHE A CE2 3191 C CZ . PHE A 414 ? 0.5494 0.8360 0.5405 -0.0908 0.1069 -0.0139 414 PHE A CZ 3192 N N . GLY A 415 ? 0.5964 0.7308 0.4782 -0.0759 0.0639 0.0451 415 GLY A N 3193 C CA . GLY A 415 ? 0.6112 0.7289 0.4775 -0.0660 0.0545 0.0510 415 GLY A CA 3194 C C . GLY A 415 ? 0.6388 0.7379 0.4776 -0.0718 0.0539 0.0659 415 GLY A C 3195 O O . GLY A 415 ? 0.6537 0.7496 0.4834 -0.0851 0.0613 0.0728 415 GLY A O 3196 N N . ASN A 416 ? 0.6595 0.7464 0.4849 -0.0619 0.0447 0.0711 416 ASN A N 3197 C CA . ASN A 416 ? 0.7295 0.7980 0.5266 -0.0645 0.0418 0.0858 416 ASN A CA 3198 C C . ASN A 416 ? 0.7280 0.7663 0.5206 -0.0586 0.0323 0.0956 416 ASN A C 3199 O O . ASN A 416 ? 0.7613 0.7811 0.5315 -0.0565 0.0267 0.1079 416 ASN A O 3200 C CB . ASN A 416 ? 0.7633 0.8428 0.5457 -0.0577 0.0380 0.0847 416 ASN A CB 3201 C CG . ASN A 416 ? 0.8252 0.8898 0.5748 -0.0619 0.0361 0.1000 416 ASN A CG 3202 O OD1 . ASN A 416 ? 0.8727 0.9320 0.6097 -0.0522 0.0260 0.1043 416 ASN A OD1 3203 N ND2 . ASN A 416 ? 0.8644 0.9228 0.5997 -0.0765 0.0453 0.1085 416 ASN A ND2 3204 N N . GLY A 417 ? 0.7123 0.7450 0.5252 -0.0554 0.0302 0.0900 417 GLY A N 3205 C CA . GLY A 417 ? 0.7137 0.7170 0.5234 -0.0504 0.0226 0.0975 417 GLY A CA 3206 C C . GLY A 417 ? 0.6972 0.7012 0.5291 -0.0403 0.0177 0.0879 417 GLY A C 3207 O O . GLY A 417 ? 0.6999 0.7184 0.5417 -0.0297 0.0136 0.0802 417 GLY A O 3208 N N . THR A 418 ? 0.6832 0.6705 0.5213 -0.0445 0.0179 0.0883 418 THR A N 3209 C CA . THR A 418 ? 0.6582 0.6444 0.5147 -0.0364 0.0140 0.0794 418 THR A CA 3210 C C . THR A 418 ? 0.6754 0.6301 0.5243 -0.0308 0.0075 0.0856 418 THR A C 3211 O O . THR A 418 ? 0.6839 0.6155 0.5192 -0.0392 0.0085 0.0945 418 THR A O 3212 C CB . THR A 418 ? 0.6627 0.6608 0.5363 -0.0463 0.0201 0.0709 418 THR A CB 3213 O OG1 . THR A 418 ? 0.6398 0.6670 0.5216 -0.0501 0.0263 0.0642 418 THR A OG1 3214 C CG2 . THR A 418 ? 0.6587 0.6551 0.5483 -0.0382 0.0156 0.0621 418 THR A CG2 3215 N N . TYR A 419 ? 0.6584 0.6118 0.5160 -0.0167 0.0012 0.0804 419 TYR A N 3216 C CA . TYR A 419 ? 0.6749 0.6007 0.5284 -0.0089 -0.0046 0.0832 419 TYR A CA 3217 C C . TYR A 419 ? 0.6517 0.5836 0.5234 -0.0040 -0.0050 0.0713 419 TYR A C 3218 O O . TYR A 419 ? 0.6361 0.5896 0.5201 0.0033 -0.0056 0.0639 419 TYR A O 3219 C CB . TYR A 419 ? 0.6958 0.6143 0.5396 0.0057 -0.0123 0.0895 419 TYR A CB 3220 C CG . TYR A 419 ? 0.7364 0.6463 0.5587 0.0019 -0.0135 0.1024 419 TYR A CG 3221 C CD1 . TYR A 419 ? 0.7240 0.6579 0.5428 -0.0009 -0.0114 0.1029 419 TYR A CD1 3222 C CD2 . TYR A 419 ? 0.7798 0.6556 0.5831 0.0012 -0.0169 0.1143 419 TYR A CD2 3223 C CE1 . TYR A 419 ? 0.7499 0.6762 0.5463 -0.0048 -0.0124 0.1148 419 TYR A CE1 3224 C CE2 . TYR A 419 ? 0.8132 0.6793 0.5938 -0.0028 -0.0182 0.1274 419 TYR A CE2 3225 C CZ . TYR A 419 ? 0.8060 0.6984 0.5828 -0.0059 -0.0159 0.1277 419 TYR A CZ 3226 O OH . TYR A 419 ? 0.8309 0.7140 0.5824 -0.0100 -0.0172 0.1409 419 TYR A OH 3227 N N . LEU A 420 ? 0.6424 0.5547 0.5144 -0.0088 -0.0047 0.0697 420 LEU A N 3228 C CA . LEU A 420 ? 0.6102 0.5278 0.4967 -0.0068 -0.0046 0.0586 420 LEU A CA 3229 C C . LEU A 420 ? 0.6078 0.5009 0.4908 0.0035 -0.0094 0.0568 420 LEU A C 3230 O O . LEU A 420 ? 0.6166 0.4809 0.4865 0.0022 -0.0115 0.0632 420 LEU A O 3231 C CB . LEU A 420 ? 0.6140 0.5346 0.5060 -0.0226 0.0000 0.0553 420 LEU A CB 3232 C CG . LEU A 420 ? 0.5972 0.5238 0.5024 -0.0229 -0.0005 0.0444 420 LEU A CG 3233 C CD1 . LEU A 420 ? 0.5685 0.5212 0.4862 -0.0145 -0.0005 0.0373 420 LEU A CD1 3234 C CD2 . LEU A 420 ? 0.5941 0.5252 0.5048 -0.0391 0.0029 0.0421 420 LEU A CD2 3235 N N . TYR A 421 ? 0.5975 0.5012 0.4912 0.0135 -0.0106 0.0479 421 TYR A N 3236 C CA . TYR A 421 ? 0.6063 0.4904 0.4978 0.0243 -0.0140 0.0440 421 TYR A CA 3237 C C . TYR A 421 ? 0.5798 0.4681 0.4799 0.0232 -0.0125 0.0329 421 TYR A C 3238 O O . TYR A 421 ? 0.5360 0.4471 0.4464 0.0191 -0.0102 0.0277 421 TYR A O 3239 C CB . TYR A 421 ? 0.6108 0.5025 0.5047 0.0412 -0.0174 0.0445 421 TYR A CB 3240 C CG . TYR A 421 ? 0.5802 0.5028 0.4886 0.0455 -0.0155 0.0370 421 TYR A CG 3241 C CD1 . TYR A 421 ? 0.5702 0.4965 0.4860 0.0505 -0.0142 0.0275 421 TYR A CD1 3242 C CD2 . TYR A 421 ? 0.5691 0.5155 0.4820 0.0438 -0.0148 0.0393 421 TYR A CD2 3243 C CE1 . TYR A 421 ? 0.5439 0.4960 0.4711 0.0528 -0.0121 0.0218 421 TYR A CE1 3244 C CE2 . TYR A 421 ? 0.5344 0.5058 0.4596 0.0465 -0.0132 0.0326 421 TYR A CE2 3245 C CZ . TYR A 421 ? 0.5215 0.4951 0.4537 0.0505 -0.0118 0.0245 421 TYR A CZ 3246 O OH . TYR A 421 ? 0.4976 0.4935 0.4400 0.0516 -0.0099 0.0190 421 TYR A OH 3247 N N . PHE A 422 ? 0.6043 0.4688 0.4986 0.0279 -0.0145 0.0293 422 PHE A N 3248 C CA . PHE A 422 ? 0.5982 0.4635 0.4970 0.0287 -0.0138 0.0186 422 PHE A CA 3249 C C . PHE A 422 ? 0.6142 0.4714 0.5115 0.0455 -0.0152 0.0145 422 PHE A C 3250 O O . PHE A 422 ? 0.6603 0.4901 0.5480 0.0515 -0.0178 0.0162 422 PHE A O 3251 C CB . PHE A 422 ? 0.6212 0.4638 0.5130 0.0165 -0.0145 0.0166 422 PHE A CB 3252 C CG . PHE A 422 ? 0.6126 0.4544 0.5062 0.0157 -0.0147 0.0054 422 PHE A CG 3253 C CD1 . PHE A 422 ? 0.5887 0.4542 0.4916 0.0091 -0.0136 0.0006 422 PHE A CD1 3254 C CD2 . PHE A 422 ? 0.6467 0.4621 0.5311 0.0217 -0.0165 -0.0004 422 PHE A CD2 3255 C CE1 . PHE A 422 ? 0.6037 0.4677 0.5057 0.0080 -0.0147 -0.0089 422 PHE A CE1 3256 C CE2 . PHE A 422 ? 0.6537 0.4679 0.5371 0.0203 -0.0168 -0.0112 422 PHE A CE2 3257 C CZ . PHE A 422 ? 0.6353 0.4741 0.5269 0.0132 -0.0161 -0.0150 422 PHE A CZ 3258 N N . PHE A 423 ? 0.6067 0.4878 0.5137 0.0531 -0.0133 0.0093 423 PHE A N 3259 C CA . PHE A 423 ? 0.6216 0.5028 0.5305 0.0691 -0.0133 0.0045 423 PHE A CA 3260 C C . PHE A 423 ? 0.6324 0.5048 0.5385 0.0703 -0.0113 -0.0064 423 PHE A C 3261 O O . PHE A 423 ? 0.6485 0.5367 0.5586 0.0646 -0.0087 -0.0117 423 PHE A O 3262 C CB . PHE A 423 ? 0.5992 0.5124 0.5203 0.0747 -0.0115 0.0042 423 PHE A CB 3263 C CG . PHE A 423 ? 0.6189 0.5387 0.5453 0.0902 -0.0107 -0.0012 423 PHE A CG 3264 C CD1 . PHE A 423 ? 0.6223 0.5510 0.5520 0.0925 -0.0063 -0.0108 423 PHE A CD1 3265 C CD2 . PHE A 423 ? 0.6349 0.5534 0.5629 0.1027 -0.0143 0.0034 423 PHE A CD2 3266 C CE1 . PHE A 423 ? 0.6266 0.5647 0.5625 0.1065 -0.0041 -0.0166 423 PHE A CE1 3267 C CE2 . PHE A 423 ? 0.6412 0.5697 0.5771 0.1179 -0.0134 -0.0025 423 PHE A CE2 3268 C CZ . PHE A 423 ? 0.6230 0.5622 0.5635 0.1195 -0.0076 -0.0129 423 PHE A CZ 3269 N N . ASN A 424 ? 0.6569 0.5030 0.5545 0.0783 -0.0128 -0.0098 424 ASN A N 3270 C CA . ASN A 424 ? 0.6632 0.4973 0.5549 0.0783 -0.0112 -0.0208 424 ASN A CA 3271 C C . ASN A 424 ? 0.6868 0.5091 0.5760 0.0958 -0.0103 -0.0280 424 ASN A C 3272 O O . ASN A 424 ? 0.6958 0.4926 0.5746 0.0974 -0.0108 -0.0354 424 ASN A O 3273 C CB . ASN A 424 ? 0.6785 0.4860 0.5595 0.0647 -0.0140 -0.0205 424 ASN A CB 3274 C CG . ASN A 424 ? 0.6995 0.4733 0.5706 0.0682 -0.0177 -0.0151 424 ASN A CG 3275 O OD1 . ASN A 424 ? 0.7121 0.4835 0.5844 0.0811 -0.0191 -0.0099 424 ASN A OD1 3276 N ND2 . ASN A 424 ? 0.7160 0.4631 0.5769 0.0564 -0.0199 -0.0161 424 ASN A ND2 3277 N N . HIS A 425 ? 0.6901 0.5321 0.5894 0.1090 -0.0091 -0.0265 425 HIS A N 3278 C CA . HIS A 425 ? 0.7189 0.5582 0.6202 0.1271 -0.0073 -0.0346 425 HIS A CA 3279 C C . HIS A 425 ? 0.7265 0.5956 0.6359 0.1292 -0.0003 -0.0435 425 HIS A C 3280 O O . HIS A 425 ? 0.7155 0.6149 0.6357 0.1250 0.0018 -0.0399 425 HIS A O 3281 C CB . HIS A 425 ? 0.7159 0.5594 0.6246 0.1418 -0.0111 -0.0278 425 HIS A CB 3282 C CG . HIS A 425 ? 0.7280 0.5765 0.6432 0.1619 -0.0088 -0.0368 425 HIS A CG 3283 N ND1 . HIS A 425 ? 0.7659 0.5827 0.6720 0.1740 -0.0106 -0.0428 425 HIS A ND1 3284 C CD2 . HIS A 425 ? 0.7022 0.5848 0.6329 0.1718 -0.0045 -0.0418 425 HIS A CD2 3285 C CE1 . HIS A 425 ? 0.7609 0.5932 0.6774 0.1920 -0.0074 -0.0513 425 HIS A CE1 3286 N NE2 . HIS A 425 ? 0.7260 0.5996 0.6580 0.1904 -0.0034 -0.0508 425 HIS A NE2 3287 N N . ARG A 426 ? 0.7656 0.6249 0.6684 0.1350 0.0035 -0.0553 426 ARG A N 3288 C CA . ARG A 426 ? 0.7792 0.6647 0.6869 0.1374 0.0112 -0.0641 426 ARG A CA 3289 C C . ARG A 426 ? 0.7488 0.6496 0.6685 0.1566 0.0145 -0.0687 426 ARG A C 3290 O O . ARG A 426 ? 0.7582 0.6384 0.6743 0.1706 0.0131 -0.0740 426 ARG A O 3291 C CB . ARG A 426 ? 0.8320 0.7016 0.7246 0.1330 0.0143 -0.0753 426 ARG A CB 3292 C CG . ARG A 426 ? 0.8561 0.7528 0.7501 0.1315 0.0226 -0.0824 426 ARG A CG 3293 C CD . ARG A 426 ? 0.9176 0.7992 0.7955 0.1327 0.0265 -0.0957 426 ARG A CD 3294 N NE . ARG A 426 ? 0.9286 0.8364 0.8082 0.1364 0.0362 -0.1033 426 ARG A NE 3295 C CZ . ARG A 426 ? 0.9049 0.8350 0.7842 0.1251 0.0398 -0.1003 426 ARG A CZ 3296 N NH1 . ARG A 426 ? 0.8480 0.7790 0.7268 0.1107 0.0342 -0.0906 426 ARG A NH1 3297 N NH2 . ARG A 426 ? 0.9071 0.8586 0.7861 0.1284 0.0495 -0.1072 426 ARG A NH2 3298 N N . ALA A 427 ? 0.7027 0.6398 0.6373 0.1571 0.0186 -0.0671 427 ALA A N 3299 C CA . ALA A 427 ? 0.7007 0.6591 0.6508 0.1743 0.0211 -0.0709 427 ALA A CA 3300 C C . ALA A 427 ? 0.7176 0.6739 0.6644 0.1859 0.0285 -0.0853 427 ALA A C 3301 O O . ALA A 427 ? 0.6909 0.6485 0.6278 0.1776 0.0350 -0.0924 427 ALA A O 3302 C CB . ALA A 427 ? 0.6763 0.6752 0.6430 0.1695 0.0245 -0.0672 427 ALA A CB 3303 N N . SER A 428 ? 0.7497 0.7022 0.7041 0.2058 0.0271 -0.0896 428 SER A N 3304 C CA . SER A 428 ? 0.7722 0.7237 0.7257 0.2206 0.0342 -0.1046 428 SER A CA 3305 C C . SER A 428 ? 0.7656 0.7587 0.7302 0.2191 0.0461 -0.1123 428 SER A C 3306 O O . SER A 428 ? 0.7786 0.7722 0.7370 0.2245 0.0546 -0.1254 428 SER A O 3307 C CB . SER A 428 ? 0.7879 0.7323 0.7517 0.2440 0.0292 -0.1061 428 SER A CB 3308 O OG . SER A 428 ? 0.7719 0.7488 0.7566 0.2483 0.0260 -0.0981 428 SER A OG 3309 N N . ASN A 429 ? 0.7486 0.7756 0.7284 0.2110 0.0469 -0.1046 429 ASN A N 3310 C CA . ASN A 429 ? 0.7266 0.7941 0.7177 0.2069 0.0582 -0.1102 429 ASN A CA 3311 C C . ASN A 429 ? 0.6946 0.7689 0.6756 0.1841 0.0620 -0.1052 429 ASN A C 3312 O O . ASN A 429 ? 0.6627 0.7697 0.6533 0.1772 0.0696 -0.1057 429 ASN A O 3313 C CB . ASN A 429 ? 0.7079 0.8129 0.7260 0.2150 0.0571 -0.1068 429 ASN A CB 3314 C CG . ASN A 429 ? 0.6988 0.8042 0.7213 0.2053 0.0469 -0.0922 429 ASN A CG 3315 O OD1 . ASN A 429 ? 0.7010 0.7806 0.7079 0.1925 0.0415 -0.0845 429 ASN A OD1 3316 N ND2 . ASN A 429 ? 0.6955 0.8318 0.7400 0.2117 0.0442 -0.0892 429 ASN A ND2 3317 N N . LEU A 430 ? 0.6797 0.7233 0.6415 0.1724 0.0564 -0.1004 430 LEU A N 3318 C CA . LEU A 430 ? 0.6619 0.7102 0.6152 0.1524 0.0575 -0.0942 430 LEU A CA 3319 C C . LEU A 430 ? 0.6543 0.7145 0.5977 0.1469 0.0686 -0.1027 430 LEU A C 3320 O O . LEU A 430 ? 0.6741 0.7196 0.6041 0.1527 0.0726 -0.1129 430 LEU A O 3321 C CB . LEU A 430 ? 0.6725 0.6876 0.6094 0.1422 0.0487 -0.0882 430 LEU A CB 3322 C CG . LEU A 430 ? 0.6546 0.6774 0.5905 0.1247 0.0460 -0.0782 430 LEU A CG 3323 C CD1 . LEU A 430 ? 0.6326 0.6664 0.5841 0.1246 0.0399 -0.0682 430 LEU A CD1 3324 C CD2 . LEU A 430 ? 0.6713 0.6666 0.5895 0.1140 0.0403 -0.0763 430 LEU A CD2 3325 N N . VAL A 431 ? 0.6250 0.7110 0.5740 0.1353 0.0737 -0.0982 431 VAL A N 3326 C CA . VAL A 431 ? 0.6163 0.7168 0.5557 0.1285 0.0851 -0.1042 431 VAL A CA 3327 C C . VAL A 431 ? 0.6101 0.6873 0.5238 0.1152 0.0830 -0.1025 431 VAL A C 3328 O O . VAL A 431 ? 0.6271 0.7051 0.5251 0.1123 0.0910 -0.1094 431 VAL A O 3329 C CB . VAL A 431 ? 0.5909 0.7269 0.5455 0.1200 0.0916 -0.0996 431 VAL A CB 3330 C CG1 . VAL A 431 ? 0.5787 0.7442 0.5585 0.1338 0.0962 -0.1050 431 VAL A CG1 3331 C CG2 . VAL A 431 ? 0.5628 0.6965 0.5212 0.1074 0.0831 -0.0867 431 VAL A CG2 3332 N N . TRP A 432 ? 0.5839 0.6418 0.4935 0.1077 0.0722 -0.0936 432 TRP A N 3333 C CA . TRP A 432 ? 0.5809 0.6179 0.4690 0.0962 0.0678 -0.0916 432 TRP A CA 3334 C C . TRP A 432 ? 0.5944 0.6055 0.4660 0.1023 0.0662 -0.1015 432 TRP A C 3335 O O . TRP A 432 ? 0.5974 0.6006 0.4751 0.1154 0.0660 -0.1076 432 TRP A O 3336 C CB . TRP A 432 ? 0.5688 0.5962 0.4611 0.0876 0.0571 -0.0804 432 TRP A CB 3337 C CG . TRP A 432 ? 0.5492 0.5980 0.4537 0.0797 0.0580 -0.0715 432 TRP A CG 3338 C CD1 . TRP A 432 ? 0.5344 0.5957 0.4579 0.0821 0.0551 -0.0658 432 TRP A CD1 3339 C CD2 . TRP A 432 ? 0.5541 0.6118 0.4506 0.0678 0.0615 -0.0675 432 TRP A CD2 3340 N NE1 . TRP A 432 ? 0.5156 0.5931 0.4442 0.0722 0.0569 -0.0596 432 TRP A NE1 3341 C CE2 . TRP A 432 ? 0.5359 0.6103 0.4482 0.0633 0.0608 -0.0601 432 TRP A CE2 3342 C CE3 . TRP A 432 ? 0.5885 0.6403 0.4645 0.0604 0.0649 -0.0693 432 TRP A CE3 3343 C CZ2 . TRP A 432 ? 0.5516 0.6347 0.4604 0.0515 0.0634 -0.0545 432 TRP A CZ2 3344 C CZ3 . TRP A 432 ? 0.5978 0.6586 0.4694 0.0491 0.0673 -0.0625 432 TRP A CZ3 3345 C CH2 . TRP A 432 ? 0.5724 0.6475 0.4606 0.0447 0.0666 -0.0553 432 TRP A CH2 3346 N N . PRO A 433 ? 0.6082 0.6051 0.4579 0.0932 0.0647 -0.1036 433 PRO A N 3347 C CA . PRO A 433 ? 0.6267 0.5984 0.4595 0.0975 0.0625 -0.1139 433 PRO A CA 3348 C C . PRO A 433 ? 0.6487 0.5954 0.4845 0.0979 0.0511 -0.1108 433 PRO A C 3349 O O . PRO A 433 ? 0.6401 0.5888 0.4867 0.0916 0.0444 -0.0999 433 PRO A O 3350 C CB . PRO A 433 ? 0.6351 0.6020 0.4446 0.0856 0.0622 -0.1147 433 PRO A CB 3351 C CG . PRO A 433 ? 0.6125 0.5917 0.4282 0.0742 0.0586 -0.1015 433 PRO A CG 3352 C CD . PRO A 433 ? 0.5978 0.6010 0.4361 0.0792 0.0647 -0.0972 433 PRO A CD 3353 N N . GLU A 434 ? 0.7033 0.6261 0.5288 0.1045 0.0494 -0.1207 434 GLU A N 3354 C CA . GLU A 434 ? 0.7449 0.6413 0.5724 0.1051 0.0399 -0.1187 434 GLU A CA 3355 C C . GLU A 434 ? 0.7133 0.5992 0.5349 0.0895 0.0301 -0.1115 434 GLU A C 3356 O O . GLU A 434 ? 0.7126 0.5887 0.5431 0.0866 0.0231 -0.1041 434 GLU A O 3357 C CB . GLU A 434 ? 0.8356 0.7058 0.6507 0.1149 0.0406 -0.1323 434 GLU A CB 3358 C CG . GLU A 434 ? 0.9179 0.7599 0.7371 0.1190 0.0327 -0.1302 434 GLU A CG 3359 C CD . GLU A 434 ? 1.0286 0.8389 0.8318 0.1262 0.0323 -0.1443 434 GLU A CD 3360 O OE1 . GLU A 434 ? 1.0882 0.9029 0.8827 0.1351 0.0405 -0.1571 434 GLU A OE1 3361 O OE2 . GLU A 434 ? 1.0877 0.8679 0.8864 0.1225 0.0242 -0.1431 434 GLU A OE2 3362 N N . TRP A 435 ? 0.6931 0.5822 0.4998 0.0797 0.0295 -0.1134 435 TRP A N 3363 C CA . TRP A 435 ? 0.6745 0.5566 0.4771 0.0660 0.0196 -0.1076 435 TRP A CA 3364 C C . TRP A 435 ? 0.6299 0.5274 0.4502 0.0606 0.0162 -0.0940 435 TRP A C 3365 O O . TRP A 435 ? 0.5995 0.4910 0.4226 0.0518 0.0080 -0.0889 435 TRP A O 3366 C CB . TRP A 435 ? 0.6922 0.5769 0.4748 0.0579 0.0187 -0.1115 435 TRP A CB 3367 C CG . TRP A 435 ? 0.6700 0.5788 0.4519 0.0557 0.0247 -0.1056 435 TRP A CG 3368 C CD1 . TRP A 435 ? 0.6799 0.5998 0.4522 0.0601 0.0351 -0.1110 435 TRP A CD1 3369 C CD2 . TRP A 435 ? 0.6371 0.5598 0.4271 0.0478 0.0207 -0.0936 435 TRP A CD2 3370 N NE1 . TRP A 435 ? 0.6580 0.5964 0.4311 0.0542 0.0378 -0.1022 435 TRP A NE1 3371 C CE2 . TRP A 435 ? 0.6359 0.5750 0.4198 0.0473 0.0287 -0.0917 435 TRP A CE2 3372 C CE3 . TRP A 435 ? 0.6201 0.5428 0.4219 0.0412 0.0117 -0.0849 435 TRP A CE3 3373 C CZ2 . TRP A 435 ? 0.6219 0.5738 0.4101 0.0406 0.0271 -0.0809 435 TRP A CZ2 3374 C CZ3 . TRP A 435 ? 0.6003 0.5377 0.4074 0.0360 0.0103 -0.0752 435 TRP A CZ3 3375 C CH2 . TRP A 435 ? 0.6006 0.5507 0.4004 0.0358 0.0176 -0.0732 435 TRP A CH2 3376 N N . MET A 436 ? 0.6191 0.5377 0.4517 0.0656 0.0227 -0.0890 436 MET A N 3377 C CA . MET A 436 ? 0.5942 0.5275 0.4429 0.0613 0.0202 -0.0773 436 MET A CA 3378 C C . MET A 436 ? 0.5902 0.5157 0.4525 0.0644 0.0161 -0.0724 436 MET A C 3379 O O . MET A 436 ? 0.5642 0.4973 0.4374 0.0591 0.0123 -0.0634 436 MET A O 3380 C CB . MET A 436 ? 0.5848 0.5426 0.4413 0.0643 0.0284 -0.0745 436 MET A CB 3381 C CG . MET A 436 ? 0.5980 0.5634 0.4401 0.0579 0.0318 -0.0756 436 MET A CG 3382 S SD . MET A 436 ? 0.5870 0.5801 0.4382 0.0574 0.0413 -0.0708 436 MET A SD 3383 C CE . MET A 436 ? 0.5614 0.5603 0.4278 0.0505 0.0338 -0.0585 436 MET A CE 3384 N N . GLY A 437 ? 0.6106 0.5199 0.4709 0.0734 0.0170 -0.0783 437 GLY A N 3385 C CA . GLY A 437 ? 0.6203 0.5147 0.4878 0.0756 0.0121 -0.0736 437 GLY A CA 3386 C C . GLY A 437 ? 0.6025 0.5127 0.4867 0.0817 0.0134 -0.0653 437 GLY A C 3387 O O . GLY A 437 ? 0.6079 0.5359 0.4993 0.0905 0.0192 -0.0671 437 GLY A O 3388 N N . VAL A 438 ? 0.5876 0.4922 0.4777 0.0765 0.0078 -0.0566 438 VAL A N 3389 C CA . VAL A 438 ? 0.5627 0.4819 0.4665 0.0802 0.0076 -0.0479 438 VAL A CA 3390 C C . VAL A 438 ? 0.5456 0.4872 0.4558 0.0707 0.0080 -0.0427 438 VAL A C 3391 O O . VAL A 438 ? 0.5340 0.4733 0.4438 0.0603 0.0040 -0.0384 438 VAL A O 3392 C CB . VAL A 438 ? 0.5631 0.4633 0.4666 0.0788 0.0020 -0.0411 438 VAL A CB 3393 C CG1 . VAL A 438 ? 0.5435 0.4575 0.4584 0.0848 0.0013 -0.0330 438 VAL A CG1 3394 C CG2 . VAL A 438 ? 0.5905 0.4609 0.4837 0.0858 0.0005 -0.0469 438 VAL A CG2 3395 N N . ILE A 439 ? 0.5467 0.5101 0.4634 0.0745 0.0130 -0.0437 439 ILE A N 3396 C CA . ILE A 439 ? 0.5278 0.5079 0.4463 0.0658 0.0143 -0.0413 439 ILE A CA 3397 C C . ILE A 439 ? 0.5252 0.5188 0.4552 0.0620 0.0121 -0.0331 439 ILE A C 3398 O O . ILE A 439 ? 0.5351 0.5350 0.4738 0.0680 0.0117 -0.0299 439 ILE A O 3399 C CB . ILE A 439 ? 0.5347 0.5308 0.4529 0.0693 0.0218 -0.0462 439 ILE A CB 3400 C CG1 . ILE A 439 ? 0.5560 0.5393 0.4600 0.0723 0.0247 -0.0554 439 ILE A CG1 3401 C CG2 . ILE A 439 ? 0.5250 0.5352 0.4436 0.0600 0.0229 -0.0424 439 ILE A CG2 3402 C CD1 . ILE A 439 ? 0.5598 0.5592 0.4619 0.0754 0.0336 -0.0608 439 ILE A CD1 3403 N N . HIS A 440 ? 0.5350 0.5326 0.4642 0.0525 0.0100 -0.0301 440 HIS A N 3404 C CA . HIS A 440 ? 0.5220 0.5337 0.4607 0.0484 0.0088 -0.0242 440 HIS A CA 3405 C C . HIS A 440 ? 0.5166 0.5462 0.4639 0.0534 0.0131 -0.0241 440 HIS A C 3406 O O . HIS A 440 ? 0.5219 0.5602 0.4677 0.0532 0.0178 -0.0273 440 HIS A O 3407 C CB . HIS A 440 ? 0.5210 0.5351 0.4560 0.0401 0.0074 -0.0235 440 HIS A CB 3408 C CG . HIS A 440 ? 0.5211 0.5456 0.4644 0.0356 0.0056 -0.0187 440 HIS A CG 3409 N ND1 . HIS A 440 ? 0.5193 0.5418 0.4671 0.0329 0.0020 -0.0155 440 HIS A ND1 3410 C CD2 . HIS A 440 ? 0.5220 0.5577 0.4685 0.0328 0.0072 -0.0173 440 HIS A CD2 3411 C CE1 . HIS A 440 ? 0.5247 0.5578 0.4786 0.0298 0.0015 -0.0131 440 HIS A CE1 3412 N NE2 . HIS A 440 ? 0.5322 0.5719 0.4852 0.0297 0.0042 -0.0141 440 HIS A NE2 3413 N N . GLY A 441 ? 0.5172 0.5528 0.4729 0.0574 0.0113 -0.0205 441 GLY A N 3414 C CA . GLY A 441 ? 0.5076 0.5634 0.4739 0.0611 0.0138 -0.0203 441 GLY A CA 3415 C C . GLY A 441 ? 0.5163 0.5748 0.4877 0.0730 0.0144 -0.0224 441 GLY A C 3416 O O . GLY A 441 ? 0.5392 0.6154 0.5214 0.0772 0.0143 -0.0214 441 GLY A O 3417 N N . TYR A 442 ? 0.5357 0.5763 0.4995 0.0790 0.0142 -0.0255 442 TYR A N 3418 C CA . TYR A 442 ? 0.5511 0.5929 0.5192 0.0924 0.0154 -0.0293 442 TYR A CA 3419 C C . TYR A 442 ? 0.5529 0.5824 0.5215 0.1003 0.0091 -0.0243 442 TYR A C 3420 O O . TYR A 442 ? 0.5888 0.6130 0.5591 0.1130 0.0086 -0.0272 442 TYR A O 3421 C CB . TYR A 442 ? 0.5771 0.6076 0.5361 0.0958 0.0201 -0.0375 442 TYR A CB 3422 C CG . TYR A 442 ? 0.5815 0.6320 0.5427 0.0916 0.0274 -0.0419 442 TYR A CG 3423 C CD1 . TYR A 442 ? 0.5783 0.6293 0.5328 0.0790 0.0282 -0.0399 442 TYR A CD1 3424 C CD2 . TYR A 442 ? 0.5859 0.6565 0.5570 0.1000 0.0334 -0.0473 442 TYR A CD2 3425 C CE1 . TYR A 442 ? 0.5831 0.6498 0.5374 0.0740 0.0349 -0.0423 442 TYR A CE1 3426 C CE2 . TYR A 442 ? 0.5882 0.6778 0.5608 0.0941 0.0411 -0.0504 442 TYR A CE2 3427 C CZ . TYR A 442 ? 0.5800 0.6660 0.5430 0.0807 0.0418 -0.0474 442 TYR A CZ 3428 O OH . TYR A 442 ? 0.6064 0.7083 0.5685 0.0740 0.0494 -0.0493 442 TYR A OH 3429 N N . GLU A 443 ? 0.5402 0.5654 0.5070 0.0931 0.0045 -0.0169 443 GLU A N 3430 C CA . GLU A 443 ? 0.5497 0.5679 0.5164 0.0989 -0.0015 -0.0101 443 GLU A CA 3431 C C . GLU A 443 ? 0.5316 0.5763 0.5106 0.1023 -0.0032 -0.0076 443 GLU A C 3432 O O . GLU A 443 ? 0.5418 0.5860 0.5224 0.1107 -0.0085 -0.0030 443 GLU A O 3433 C CB . GLU A 443 ? 0.5617 0.5628 0.5188 0.0884 -0.0048 -0.0035 443 GLU A CB 3434 C CG . GLU A 443 ? 0.5423 0.5590 0.5029 0.0792 -0.0058 0.0014 443 GLU A CG 3435 C CD . GLU A 443 ? 0.5193 0.5512 0.4846 0.0706 -0.0018 -0.0027 443 GLU A CD 3436 O OE1 . GLU A 443 ? 0.5350 0.5649 0.4989 0.0700 0.0017 -0.0084 443 GLU A OE1 3437 O OE2 . GLU A 443 ? 0.5064 0.5510 0.4753 0.0644 -0.0024 -0.0002 443 GLU A OE2 3438 N N . ILE A 444 ? 0.5202 0.5868 0.5069 0.0954 0.0008 -0.0106 444 ILE A N 3439 C CA . ILE A 444 ? 0.5123 0.6045 0.5105 0.0952 -0.0009 -0.0091 444 ILE A CA 3440 C C . ILE A 444 ? 0.5237 0.6308 0.5332 0.1093 -0.0024 -0.0115 444 ILE A C 3441 O O . ILE A 444 ? 0.5250 0.6416 0.5395 0.1146 -0.0086 -0.0074 444 ILE A O 3442 C CB . ILE A 444 ? 0.4988 0.6084 0.5024 0.0847 0.0043 -0.0128 444 ILE A CB 3443 C CG1 . ILE A 444 ? 0.4854 0.5830 0.4799 0.0724 0.0043 -0.0101 444 ILE A CG1 3444 C CG2 . ILE A 444 ? 0.5006 0.6370 0.5170 0.0841 0.0026 -0.0127 444 ILE A CG2 3445 C CD1 . ILE A 444 ? 0.4697 0.5777 0.4664 0.0628 0.0087 -0.0130 444 ILE A CD1 3446 N N . GLU A 445 ? 0.5271 0.6376 0.5407 0.1157 0.0031 -0.0186 445 GLU A N 3447 C CA . GLU A 445 ? 0.5360 0.6630 0.5626 0.1305 0.0026 -0.0226 445 GLU A CA 3448 C C . GLU A 445 ? 0.5537 0.6648 0.5769 0.1439 -0.0060 -0.0173 445 GLU A C 3449 O O . GLU A 445 ? 0.5659 0.6949 0.6014 0.1556 -0.0105 -0.0173 445 GLU A O 3450 C CB . GLU A 445 ? 0.5535 0.6833 0.5823 0.1356 0.0112 -0.0320 445 GLU A CB 3451 C CG . GLU A 445 ? 0.5717 0.6685 0.5840 0.1375 0.0127 -0.0342 445 GLU A CG 3452 C CD . GLU A 445 ? 0.5509 0.6518 0.5611 0.1363 0.0223 -0.0436 445 GLU A CD 3453 O OE1 . GLU A 445 ? 0.5281 0.6409 0.5374 0.1237 0.0277 -0.0444 445 GLU A OE1 3454 O OE2 . GLU A 445 ? 0.5756 0.6661 0.5831 0.1482 0.0245 -0.0501 445 GLU A OE2 3455 N N . PHE A 446 ? 0.5590 0.6371 0.5656 0.1418 -0.0089 -0.0125 446 PHE A N 3456 C CA . PHE A 446 ? 0.5750 0.6333 0.5746 0.1523 -0.0174 -0.0054 446 PHE A CA 3457 C C . PHE A 446 ? 0.5693 0.6362 0.5679 0.1478 -0.0244 0.0037 446 PHE A C 3458 O O . PHE A 446 ? 0.5679 0.6368 0.5684 0.1593 -0.0322 0.0086 446 PHE A O 3459 C CB . PHE A 446 ? 0.5849 0.6045 0.5665 0.1495 -0.0177 -0.0031 446 PHE A CB 3460 C CG . PHE A 446 ? 0.6012 0.6076 0.5816 0.1591 -0.0135 -0.0120 446 PHE A CG 3461 C CD1 . PHE A 446 ? 0.5789 0.5903 0.5593 0.1519 -0.0053 -0.0205 446 PHE A CD1 3462 C CD2 . PHE A 446 ? 0.6255 0.6148 0.6043 0.1764 -0.0181 -0.0122 446 PHE A CD2 3463 C CE1 . PHE A 446 ? 0.6042 0.6044 0.5820 0.1609 -0.0011 -0.0297 446 PHE A CE1 3464 C CE2 . PHE A 446 ? 0.6377 0.6147 0.6153 0.1864 -0.0140 -0.0220 446 PHE A CE2 3465 C CZ . PHE A 446 ? 0.6297 0.6129 0.6065 0.1783 -0.0051 -0.0312 446 PHE A CZ 3466 N N . VAL A 447 ? 0.5578 0.6299 0.5530 0.1317 -0.0219 0.0055 447 VAL A N 3467 C CA . VAL A 447 ? 0.5736 0.6550 0.5666 0.1257 -0.0272 0.0125 447 VAL A CA 3468 C C . VAL A 447 ? 0.5702 0.6854 0.5792 0.1311 -0.0305 0.0102 447 VAL A C 3469 O O . VAL A 447 ? 0.5858 0.7074 0.5924 0.1325 -0.0378 0.0161 447 VAL A O 3470 C CB . VAL A 447 ? 0.5565 0.6363 0.5433 0.1082 -0.0228 0.0130 447 VAL A CB 3471 C CG1 . VAL A 447 ? 0.5463 0.6429 0.5337 0.1018 -0.0266 0.0167 447 VAL A CG1 3472 C CG2 . VAL A 447 ? 0.5587 0.6076 0.5300 0.1028 -0.0221 0.0172 447 VAL A CG2 3473 N N . PHE A 448 ? 0.5566 0.6938 0.5812 0.1334 -0.0252 0.0016 448 PHE A N 3474 C CA . PHE A 448 ? 0.5468 0.7196 0.5895 0.1368 -0.0276 -0.0018 448 PHE A CA 3475 C C . PHE A 448 ? 0.5765 0.7611 0.6322 0.1561 -0.0312 -0.0047 448 PHE A C 3476 O O . PHE A 448 ? 0.5766 0.7941 0.6504 0.1602 -0.0335 -0.0084 448 PHE A O 3477 C CB . PHE A 448 ? 0.5248 0.7185 0.5775 0.1243 -0.0191 -0.0090 448 PHE A CB 3478 C CG . PHE A 448 ? 0.5130 0.7083 0.5598 0.1081 -0.0192 -0.0066 448 PHE A CG 3479 C CD1 . PHE A 448 ? 0.5130 0.6844 0.5449 0.0982 -0.0160 -0.0041 448 PHE A CD1 3480 C CD2 . PHE A 448 ? 0.5165 0.7381 0.5735 0.1031 -0.0228 -0.0078 448 PHE A CD2 3481 C CE1 . PHE A 448 ? 0.5176 0.6907 0.5450 0.0852 -0.0161 -0.0029 448 PHE A CE1 3482 C CE2 . PHE A 448 ? 0.4973 0.7184 0.5480 0.0891 -0.0229 -0.0069 448 PHE A CE2 3483 C CZ . PHE A 448 ? 0.5036 0.7002 0.5396 0.0809 -0.0194 -0.0044 448 PHE A CZ 3484 N N . GLY A 449 ? 0.5974 0.7559 0.6449 0.1680 -0.0321 -0.0036 449 GLY A N 3485 C CA . GLY A 449 ? 0.6040 0.7687 0.6619 0.1890 -0.0374 -0.0054 449 GLY A CA 3486 C C . GLY A 449 ? 0.6135 0.7991 0.6892 0.1975 -0.0294 -0.0171 449 GLY A C 3487 O O . GLY A 449 ? 0.6433 0.8430 0.7328 0.2157 -0.0334 -0.0203 449 GLY A O 3488 N N . LEU A 450 ? 0.5981 0.7860 0.6732 0.1855 -0.0181 -0.0235 450 LEU A N 3489 C CA . LEU A 450 ? 0.5988 0.8077 0.6888 0.1920 -0.0089 -0.0347 450 LEU A CA 3490 C C . LEU A 450 ? 0.6093 0.8008 0.6981 0.2123 -0.0092 -0.0393 450 LEU A C 3491 O O . LEU A 450 ? 0.6225 0.8383 0.7287 0.2244 -0.0048 -0.0484 450 LEU A O 3492 C CB . LEU A 450 ? 0.5970 0.8053 0.6809 0.1750 0.0030 -0.0395 450 LEU A CB 3493 C CG . LEU A 450 ? 0.5861 0.8285 0.6830 0.1605 0.0072 -0.0411 450 LEU A CG 3494 C CD1 . LEU A 450 ? 0.5835 0.8261 0.6769 0.1508 -0.0015 -0.0326 450 LEU A CD1 3495 C CD2 . LEU A 450 ? 0.5858 0.8247 0.6748 0.1456 0.0186 -0.0451 450 LEU A CD2 3496 N N . PRO A 451 ? 0.6167 0.7662 0.6854 0.2159 -0.0141 -0.0337 451 PRO A N 3497 C CA . PRO A 451 ? 0.6543 0.7843 0.7214 0.2365 -0.0161 -0.0379 451 PRO A CA 3498 C C . PRO A 451 ? 0.6691 0.8151 0.7519 0.2580 -0.0257 -0.0368 451 PRO A C 3499 O O . PRO A 451 ? 0.6838 0.8192 0.7696 0.2777 -0.0265 -0.0424 451 PRO A O 3500 C CB . PRO A 451 ? 0.6690 0.7499 0.7102 0.2316 -0.0204 -0.0301 451 PRO A CB 3501 C CG . PRO A 451 ? 0.6440 0.7231 0.6757 0.2084 -0.0138 -0.0289 451 PRO A CG 3502 C CD . PRO A 451 ? 0.6173 0.7348 0.6638 0.1995 -0.0141 -0.0268 451 PRO A CD 3503 N N . LEU A 452 ? 0.6798 0.8508 0.7722 0.2551 -0.0333 -0.0302 452 LEU A N 3504 C CA . LEU A 452 ? 0.7145 0.9075 0.8243 0.2754 -0.0435 -0.0295 452 LEU A CA 3505 C C . LEU A 452 ? 0.7076 0.9477 0.8472 0.2845 -0.0368 -0.0424 452 LEU A C 3506 O O . LEU A 452 ? 0.7480 1.0017 0.9035 0.3073 -0.0423 -0.0464 452 LEU A O 3507 C CB . LEU A 452 ? 0.7046 0.9088 0.8129 0.2687 -0.0549 -0.0184 452 LEU A CB 3508 C CG . LEU A 452 ? 0.7231 0.8840 0.8053 0.2699 -0.0653 -0.0047 452 LEU A CG 3509 C CD1 . LEU A 452 ? 0.7130 0.8367 0.7714 0.2518 -0.0580 -0.0015 452 LEU A CD1 3510 C CD2 . LEU A 452 ? 0.7233 0.9013 0.8053 0.2655 -0.0766 0.0047 452 LEU A CD2 3511 N N . VAL A 453 ? 0.6906 0.9554 0.8378 0.2669 -0.0248 -0.0488 453 VAL A N 3512 C CA . VAL A 453 ? 0.6918 1.0027 0.8662 0.2710 -0.0158 -0.0611 453 VAL A CA 3513 C C . VAL A 453 ? 0.7202 1.0196 0.8945 0.2858 -0.0066 -0.0721 453 VAL A C 3514 O O . VAL A 453 ? 0.6991 0.9707 0.8545 0.2766 0.0022 -0.0745 453 VAL A O 3515 C CB . VAL A 453 ? 0.6583 0.9934 0.8365 0.2456 -0.0052 -0.0635 453 VAL A CB 3516 C CG1 . VAL A 453 ? 0.6510 1.0333 0.8562 0.2478 0.0057 -0.0759 453 VAL A CG1 3517 C CG2 . VAL A 453 ? 0.6308 0.9765 0.8090 0.2316 -0.0143 -0.0543 453 VAL A CG2 3518 N N . LYS A 454 ? 0.7624 1.0850 0.9583 0.3090 -0.0089 -0.0796 454 LYS A N 3519 C CA . LYS A 454 ? 0.8325 1.1391 1.0271 0.3282 -0.0030 -0.0900 454 LYS A CA 3520 C C . LYS A 454 ? 0.8241 1.1534 1.0256 0.3203 0.0157 -0.1036 454 LYS A C 3521 O O . LYS A 454 ? 0.8201 1.1222 1.0068 0.3249 0.0235 -0.1108 454 LYS A O 3522 C CB . LYS A 454 ? 0.8799 1.2017 1.0952 0.3583 -0.0131 -0.0932 454 LYS A CB 3523 C CG . LYS A 454 ? 0.9256 1.2287 1.1330 0.3643 -0.0322 -0.0782 454 LYS A CG 3524 C CD . LYS A 454 ? 0.9893 1.2744 1.1998 0.3959 -0.0442 -0.0780 454 LYS A CD 3525 C CE . LYS A 454 ? 1.0081 1.2573 1.1977 0.3970 -0.0616 -0.0605 454 LYS A CE 3526 N NZ . LYS A 454 ? 1.0515 1.2821 1.2430 0.4282 -0.0752 -0.0583 454 LYS A NZ 3527 N N . GLU A 455 ? 0.8027 1.1798 1.0242 0.3067 0.0229 -0.1068 455 GLU A N 3528 C CA . GLU A 455 ? 0.7977 1.1975 1.0235 0.2954 0.0414 -0.1179 455 GLU A CA 3529 C C . GLU A 455 ? 0.7917 1.1578 0.9872 0.2721 0.0492 -0.1141 455 GLU A C 3530 O O . GLU A 455 ? 0.7945 1.1708 0.9869 0.2635 0.0640 -0.1224 455 GLU A O 3531 C CB . GLU A 455 ? 0.7708 1.2309 1.0267 0.2858 0.0467 -0.1216 455 GLU A CB 3532 C CG . GLU A 455 ? 0.7527 1.2189 1.0050 0.2609 0.0420 -0.1107 455 GLU A CG 3533 N N . LEU A 456 ? 0.7664 1.0940 0.9397 0.2624 0.0394 -0.1017 456 LEU A N 3534 C CA . LEU A 456 ? 0.7569 1.0521 0.9027 0.2425 0.0448 -0.0981 456 LEU A CA 3535 C C . LEU A 456 ? 0.8088 1.0602 0.9319 0.2511 0.0466 -0.1024 456 LEU A C 3536 O O . LEU A 456 ? 0.8005 1.0284 0.9021 0.2360 0.0518 -0.1016 456 LEU A O 3537 C CB . LEU A 456 ? 0.7395 1.0172 0.8733 0.2264 0.0348 -0.0841 456 LEU A CB 3538 C CG . LEU A 456 ? 0.7098 1.0232 0.8583 0.2103 0.0348 -0.0800 456 LEU A CG 3539 C CD1 . LEU A 456 ? 0.6968 0.9869 0.8301 0.1969 0.0250 -0.0675 456 LEU A CD1 3540 C CD2 . LEU A 456 ? 0.6893 1.0245 0.8400 0.1935 0.0494 -0.0860 456 LEU A CD2 3541 N N . ASN A 457 ? 0.8638 1.1038 0.9916 0.2752 0.0417 -0.1072 457 ASN A N 3542 C CA . ASN A 457 ? 0.9010 1.1029 1.0102 0.2859 0.0447 -0.1149 457 ASN A CA 3543 C C . ASN A 457 ? 0.8552 1.0022 0.9364 0.2799 0.0356 -0.1057 457 ASN A C 3544 O O . ASN A 457 ? 0.8588 0.9747 0.9203 0.2785 0.0400 -0.1116 457 ASN A O 3545 C CB . ASN A 457 ? 0.9614 1.1730 1.0637 0.2772 0.0612 -0.1269 457 ASN A CB 3546 C CG . ASN A 457 ? 1.0254 1.2882 1.1539 0.2859 0.0727 -0.1388 457 ASN A CG 3547 O OD1 . ASN A 457 ? 1.0359 1.3260 1.1897 0.3029 0.0682 -0.1409 457 ASN A OD1 3548 N ND2 . ASN A 457 ? 1.1029 1.3797 1.2248 0.2736 0.0880 -0.1469 457 ASN A ND2 3549 N N . TYR A 458 ? 0.7803 0.9162 0.8592 0.2757 0.0233 -0.0919 458 TYR A N 3550 C CA . TYR A 458 ? 0.7515 0.8371 0.8059 0.2715 0.0146 -0.0830 458 TYR A CA 3551 C C . TYR A 458 ? 0.7665 0.8236 0.8182 0.2955 0.0070 -0.0850 458 TYR A C 3552 O O . TYR A 458 ? 0.7712 0.8508 0.8425 0.3159 0.0055 -0.0904 458 TYR A O 3553 C CB . TYR A 458 ? 0.7221 0.8063 0.7734 0.2579 0.0053 -0.0677 458 TYR A CB 3554 C CG . TYR A 458 ? 0.6708 0.7731 0.7206 0.2338 0.0112 -0.0647 458 TYR A CG 3555 C CD1 . TYR A 458 ? 0.6626 0.7375 0.6917 0.2165 0.0130 -0.0614 458 TYR A CD1 3556 C CD2 . TYR A 458 ? 0.6370 0.7833 0.7064 0.2284 0.0143 -0.0652 458 TYR A CD2 3557 C CE1 . TYR A 458 ? 0.6283 0.7178 0.6558 0.1963 0.0175 -0.0586 458 TYR A CE1 3558 C CE2 . TYR A 458 ? 0.6126 0.7713 0.6793 0.2069 0.0191 -0.0622 458 TYR A CE2 3559 C CZ . TYR A 458 ? 0.6106 0.7401 0.6560 0.1918 0.0205 -0.0588 458 TYR A CZ 3560 O OH . TYR A 458 ? 0.5877 0.7280 0.6304 0.1723 0.0245 -0.0558 458 TYR A OH 3561 N N . THR A 459 ? 0.7746 0.7822 0.8027 0.2930 0.0020 -0.0808 459 THR A N 3562 C CA . THR A 459 ? 0.8098 0.7819 0.8314 0.3143 -0.0063 -0.0811 459 THR A CA 3563 C C . THR A 459 ? 0.8165 0.7845 0.8411 0.3209 -0.0203 -0.0662 459 THR A C 3564 O O . THR A 459 ? 0.8065 0.7955 0.8354 0.3069 -0.0231 -0.0562 459 THR A O 3565 C CB . THR A 459 ? 0.8260 0.7439 0.8199 0.3070 -0.0069 -0.0817 459 THR A CB 3566 O OG1 . THR A 459 ? 0.8057 0.7083 0.7852 0.2839 -0.0109 -0.0685 459 THR A OG1 3567 C CG2 . THR A 459 ? 0.8243 0.7436 0.8126 0.3026 0.0056 -0.0972 459 THR A CG2 3568 N N . ALA A 460 ? 0.8527 0.7921 0.8735 0.3425 -0.0292 -0.0648 460 ALA A N 3569 C CA . ALA A 460 ? 0.8549 0.7811 0.8723 0.3493 -0.0438 -0.0492 460 ALA A CA 3570 C C . ALA A 460 ? 0.8532 0.7439 0.8452 0.3268 -0.0479 -0.0349 460 ALA A C 3571 O O . ALA A 460 ? 0.8228 0.7247 0.8142 0.3175 -0.0543 -0.0220 460 ALA A O 3572 C CB . ALA A 460 ? 0.8911 0.7875 0.9065 0.3777 -0.0524 -0.0511 460 ALA A CB 3573 N N . GLU A 461 ? 0.8774 0.7276 0.8491 0.3176 -0.0438 -0.0382 461 GLU A N 3574 C CA . GLU A 461 ? 0.8896 0.7080 0.8387 0.2946 -0.0460 -0.0268 461 GLU A CA 3575 C C . GLU A 461 ? 0.8386 0.6919 0.7937 0.2716 -0.0412 -0.0221 461 GLU A C 3576 O O . GLU A 461 ? 0.8318 0.6745 0.7755 0.2563 -0.0455 -0.0093 461 GLU A O 3577 C CB . GLU A 461 ? 0.9312 0.7099 0.8621 0.2867 -0.0406 -0.0349 461 GLU A CB 3578 C CG . GLU A 461 ? 1.0092 0.7376 0.9259 0.3039 -0.0468 -0.0367 461 GLU A CG 3579 C CD . GLU A 461 ? 1.0649 0.8015 0.9948 0.3304 -0.0437 -0.0528 461 GLU A CD 3580 O OE1 . GLU A 461 ? 1.0531 0.8337 1.0016 0.3329 -0.0345 -0.0644 461 GLU A OE1 3581 O OE2 . GLU A 461 ? 1.1343 0.8323 1.0555 0.3493 -0.0503 -0.0539 461 GLU A OE2 3582 N N . GLU A 462 ? 0.7996 0.6932 0.7717 0.2694 -0.0320 -0.0328 462 GLU A N 3583 C CA . GLU A 462 ? 0.7561 0.6831 0.7350 0.2496 -0.0273 -0.0299 462 GLU A CA 3584 C C . GLU A 462 ? 0.7429 0.7012 0.7354 0.2522 -0.0340 -0.0209 462 GLU A C 3585 O O . GLU A 462 ? 0.7279 0.6947 0.7167 0.2353 -0.0352 -0.0124 462 GLU A O 3586 C CB . GLU A 462 ? 0.7424 0.6980 0.7321 0.2457 -0.0151 -0.0437 462 GLU A CB 3587 C CG . GLU A 462 ? 0.7548 0.6834 0.7270 0.2326 -0.0089 -0.0495 462 GLU A CG 3588 C CD . GLU A 462 ? 0.7489 0.6983 0.7268 0.2322 0.0027 -0.0639 462 GLU A CD 3589 O OE1 . GLU A 462 ? 0.7602 0.7427 0.7564 0.2444 0.0072 -0.0709 462 GLU A OE1 3590 O OE2 . GLU A 462 ? 0.7443 0.6775 0.7079 0.2193 0.0074 -0.0681 462 GLU A OE2 3591 N N . GLU A 463 ? 0.7477 0.7241 0.7560 0.2736 -0.0386 -0.0236 463 GLU A N 3592 C CA . GLU A 463 ? 0.7301 0.7332 0.7498 0.2779 -0.0474 -0.0149 463 GLU A CA 3593 C C . GLU A 463 ? 0.7331 0.7031 0.7316 0.2720 -0.0575 0.0010 463 GLU A C 3594 O O . GLU A 463 ? 0.7122 0.6976 0.7096 0.2600 -0.0610 0.0096 463 GLU A O 3595 C CB . GLU A 463 ? 0.7610 0.7839 0.8001 0.3049 -0.0530 -0.0199 463 GLU A CB 3596 C CG . GLU A 463 ? 0.7580 0.8178 0.8124 0.3080 -0.0620 -0.0131 463 GLU A CG 3597 C CD . GLU A 463 ? 0.7722 0.8525 0.8467 0.3358 -0.0700 -0.0168 463 GLU A CD 3598 O OE1 . GLU A 463 ? 0.7809 0.8643 0.8667 0.3521 -0.0647 -0.0291 463 GLU A OE1 3599 O OE2 . GLU A 463 ? 0.7696 0.8648 0.8489 0.3416 -0.0821 -0.0079 463 GLU A OE2 3600 N N . ALA A 464 ? 0.7610 0.6847 0.7416 0.2798 -0.0617 0.0044 464 ALA A N 3601 C CA . ALA A 464 ? 0.7839 0.6716 0.7418 0.2741 -0.0706 0.0200 464 ALA A CA 3602 C C . ALA A 464 ? 0.7745 0.6583 0.7199 0.2464 -0.0653 0.0258 464 ALA A C 3603 O O . ALA A 464 ? 0.7736 0.6572 0.7097 0.2375 -0.0708 0.0381 464 ALA A O 3604 C CB . ALA A 464 ? 0.8190 0.6547 0.7595 0.2854 -0.0743 0.0210 464 ALA A CB 3605 N N . LEU A 465 ? 0.7598 0.6413 0.7046 0.2338 -0.0550 0.0165 465 LEU A N 3606 C CA . LEU A 465 ? 0.7531 0.6335 0.6889 0.2089 -0.0497 0.0201 465 LEU A CA 3607 C C . LEU A 465 ? 0.7212 0.6431 0.6692 0.1996 -0.0486 0.0222 465 LEU A C 3608 O O . LEU A 465 ? 0.7380 0.6587 0.6770 0.1845 -0.0496 0.0308 465 LEU A O 3609 C CB . LEU A 465 ? 0.7471 0.6221 0.6823 0.1999 -0.0400 0.0084 465 LEU A CB 3610 C CG . LEU A 465 ? 0.7198 0.5962 0.6483 0.1758 -0.0348 0.0104 465 LEU A CG 3611 C CD1 . LEU A 465 ? 0.7380 0.5797 0.6471 0.1652 -0.0392 0.0218 465 LEU A CD1 3612 C CD2 . LEU A 465 ? 0.7210 0.5964 0.6501 0.1696 -0.0265 -0.0019 465 LEU A CD2 3613 N N . SER A 466 ? 0.6898 0.6487 0.6585 0.2079 -0.0460 0.0137 466 SER A N 3614 C CA . SER A 466 ? 0.6543 0.6515 0.6350 0.1992 -0.0454 0.0148 466 SER A CA 3615 C C . SER A 466 ? 0.6696 0.6686 0.6452 0.2025 -0.0561 0.0268 466 SER A C 3616 O O . SER A 466 ? 0.6715 0.6826 0.6437 0.1885 -0.0564 0.0319 466 SER A O 3617 C CB . SER A 466 ? 0.6304 0.6667 0.6347 0.2076 -0.0410 0.0037 466 SER A CB 3618 O OG . SER A 466 ? 0.6059 0.6757 0.6203 0.1954 -0.0393 0.0040 466 SER A OG 3619 N N . ARG A 467 ? 0.6853 0.6711 0.6589 0.2215 -0.0651 0.0311 467 ARG A N 3620 C CA . ARG A 467 ? 0.7000 0.6869 0.6667 0.2264 -0.0766 0.0431 467 ARG A CA 3621 C C . ARG A 467 ? 0.7100 0.6653 0.6510 0.2111 -0.0781 0.0556 467 ARG A C 3622 O O . ARG A 467 ? 0.7040 0.6709 0.6389 0.2032 -0.0823 0.0634 467 ARG A O 3623 C CB . ARG A 467 ? 0.7368 0.7137 0.7062 0.2520 -0.0869 0.0454 467 ARG A CB 3624 C CG . ARG A 467 ? 0.7260 0.7430 0.7241 0.2686 -0.0869 0.0339 467 ARG A CG 3625 C CD . ARG A 467 ? 0.7581 0.7684 0.7601 0.2956 -0.0992 0.0371 467 ARG A CD 3626 N NE . ARG A 467 ? 0.7451 0.8003 0.7779 0.3115 -0.0995 0.0258 467 ARG A NE 3627 C CZ . ARG A 467 ? 0.7194 0.8200 0.7703 0.3108 -0.1039 0.0250 467 ARG A CZ 3628 N NH1 . ARG A 467 ? 0.7100 0.8173 0.7504 0.2957 -0.1088 0.0344 467 ARG A NH1 3629 N NH2 . ARG A 467 ? 0.7015 0.8427 0.7816 0.3248 -0.1032 0.0139 467 ARG A NH2 3630 N N . ARG A 468 ? 0.7306 0.6474 0.6567 0.2064 -0.0743 0.0566 468 ARG A N 3631 C CA . ARG A 468 ? 0.7495 0.6375 0.6529 0.1891 -0.0733 0.0670 468 ARG A CA 3632 C C . ARG A 468 ? 0.7073 0.6193 0.6137 0.1686 -0.0662 0.0653 468 ARG A C 3633 O O . ARG A 468 ? 0.7189 0.6282 0.6124 0.1574 -0.0678 0.0747 468 ARG A O 3634 C CB . ARG A 468 ? 0.7928 0.6420 0.6849 0.1843 -0.0684 0.0644 468 ARG A CB 3635 C CG . ARG A 468 ? 0.8608 0.6646 0.7340 0.1944 -0.0760 0.0736 468 ARG A CG 3636 C CD . ARG A 468 ? 0.9096 0.6778 0.7734 0.1872 -0.0703 0.0684 468 ARG A CD 3637 N NE . ARG A 468 ? 0.9289 0.6855 0.7799 0.1625 -0.0650 0.0737 468 ARG A NE 3638 C CZ . ARG A 468 ? 0.9425 0.6889 0.7926 0.1487 -0.0575 0.0662 468 ARG A CZ 3639 N NH1 . ARG A 468 ? 0.9353 0.6800 0.7943 0.1561 -0.0539 0.0528 468 ARG A NH1 3640 N NH2 . ARG A 468 ? 0.9514 0.6913 0.7917 0.1271 -0.0535 0.0718 468 ARG A NH2 3641 N N . ILE A 469 ? 0.6634 0.5970 0.5858 0.1639 -0.0580 0.0531 469 ILE A N 3642 C CA . ILE A 469 ? 0.6251 0.5786 0.5511 0.1456 -0.0510 0.0502 469 ILE A CA 3643 C C . ILE A 469 ? 0.6188 0.6053 0.5523 0.1443 -0.0544 0.0521 469 ILE A C 3644 O O . ILE A 469 ? 0.6080 0.5984 0.5334 0.1310 -0.0534 0.0568 469 ILE A O 3645 C CB . ILE A 469 ? 0.5912 0.5566 0.5303 0.1421 -0.0423 0.0375 469 ILE A CB 3646 C CG1 . ILE A 469 ? 0.6068 0.5387 0.5342 0.1364 -0.0385 0.0360 469 ILE A CG1 3647 C CG2 . ILE A 469 ? 0.5532 0.5463 0.5003 0.1278 -0.0370 0.0338 469 ILE A CG2 3648 C CD1 . ILE A 469 ? 0.5890 0.5276 0.5248 0.1333 -0.0308 0.0240 469 ILE A CD1 3649 N N . MET A 470 ? 0.6303 0.6414 0.5796 0.1578 -0.0583 0.0476 470 MET A N 3650 C CA . MET A 470 ? 0.6325 0.6756 0.5895 0.1567 -0.0629 0.0486 470 MET A CA 3651 C C . MET A 470 ? 0.6482 0.6787 0.5865 0.1559 -0.0712 0.0613 470 MET A C 3652 O O . MET A 470 ? 0.6461 0.6924 0.5808 0.1458 -0.0719 0.0634 470 MET A O 3653 C CB . MET A 470 ? 0.6402 0.7106 0.6173 0.1730 -0.0674 0.0427 470 MET A CB 3654 C CG . MET A 470 ? 0.6254 0.7168 0.6220 0.1720 -0.0584 0.0299 470 MET A CG 3655 S SD . MET A 470 ? 0.6579 0.7720 0.6763 0.1950 -0.0630 0.0235 470 MET A SD 3656 C CE . MET A 470 ? 0.6402 0.8008 0.6751 0.1902 -0.0677 0.0218 470 MET A CE 3657 N N . HIS A 471 ? 0.6821 0.6823 0.6067 0.1665 -0.0773 0.0697 471 HIS A N 3658 C CA . HIS A 471 ? 0.7149 0.7013 0.6191 0.1664 -0.0857 0.0832 471 HIS A CA 3659 C C . HIS A 471 ? 0.7151 0.6853 0.6009 0.1462 -0.0793 0.0888 471 HIS A C 3660 O O . HIS A 471 ? 0.7334 0.7117 0.6079 0.1387 -0.0818 0.0952 471 HIS A O 3661 C CB . HIS A 471 ? 0.7603 0.7162 0.6532 0.1837 -0.0950 0.0918 471 HIS A CB 3662 C CG . HIS A 471 ? 0.7971 0.7473 0.6717 0.1875 -0.1063 0.1056 471 HIS A CG 3663 N ND1 . HIS A 471 ? 0.7961 0.7801 0.6789 0.1935 -0.1145 0.1054 471 HIS A ND1 3664 C CD2 . HIS A 471 ? 0.8329 0.7478 0.6796 0.1845 -0.1107 0.1202 471 HIS A CD2 3665 C CE1 . HIS A 471 ? 0.8165 0.7864 0.6765 0.1953 -0.1241 0.1192 471 HIS A CE1 3666 N NE2 . HIS A 471 ? 0.8559 0.7833 0.6931 0.1898 -0.1216 0.1288 471 HIS A NE2 3667 N N . TYR A 472 ? 0.7182 0.6674 0.6015 0.1376 -0.0709 0.0858 472 TYR A N 3668 C CA . TYR A 472 ? 0.7050 0.6462 0.5770 0.1176 -0.0632 0.0883 472 TYR A CA 3669 C C . TYR A 472 ? 0.6732 0.6488 0.5546 0.1074 -0.0591 0.0824 472 TYR A C 3670 O O . TYR A 472 ? 0.7038 0.6831 0.5729 0.0974 -0.0587 0.0880 472 TYR A O 3671 C CB . TYR A 472 ? 0.6951 0.6201 0.5710 0.1102 -0.0548 0.0816 472 TYR A CB 3672 C CG . TYR A 472 ? 0.7398 0.6244 0.6023 0.1134 -0.0564 0.0870 472 TYR A CG 3673 C CD1 . TYR A 472 ? 0.7775 0.6342 0.6181 0.1134 -0.0620 0.1009 472 TYR A CD1 3674 C CD2 . TYR A 472 ? 0.7462 0.6180 0.6158 0.1148 -0.0521 0.0782 472 TYR A CD2 3675 C CE1 . TYR A 472 ? 0.7967 0.6125 0.6238 0.1149 -0.0634 0.1059 472 TYR A CE1 3676 C CE2 . TYR A 472 ? 0.7693 0.6018 0.6259 0.1167 -0.0536 0.0819 472 TYR A CE2 3677 C CZ . TYR A 472 ? 0.8038 0.6077 0.6396 0.1165 -0.0593 0.0957 472 TYR A CZ 3678 O OH . TYR A 472 ? 0.8570 0.6188 0.6790 0.1173 -0.0609 0.0994 472 TYR A OH 3679 N N . TRP A 473 ? 0.6324 0.6318 0.5345 0.1096 -0.0557 0.0707 473 TRP A N 3680 C CA . TRP A 473 ? 0.5976 0.6251 0.5088 0.0991 -0.0512 0.0639 473 TRP A CA 3681 C C . TRP A 473 ? 0.5977 0.6428 0.5034 0.1004 -0.0582 0.0684 473 TRP A C 3682 O O . TRP A 473 ? 0.5941 0.6453 0.4910 0.0890 -0.0557 0.0698 473 TRP A O 3683 C CB . TRP A 473 ? 0.5626 0.6110 0.4956 0.1024 -0.0475 0.0520 473 TRP A CB 3684 C CG . TRP A 473 ? 0.5463 0.5885 0.4841 0.0933 -0.0385 0.0453 473 TRP A CG 3685 C CD1 . TRP A 473 ? 0.5278 0.5888 0.4772 0.0860 -0.0330 0.0368 473 TRP A CD1 3686 C CD2 . TRP A 473 ? 0.5603 0.5753 0.4907 0.0907 -0.0349 0.0463 473 TRP A CD2 3687 N NE1 . TRP A 473 ? 0.5193 0.5676 0.4687 0.0798 -0.0268 0.0331 473 TRP A NE1 3688 C CE2 . TRP A 473 ? 0.5414 0.5627 0.4799 0.0822 -0.0278 0.0382 473 TRP A CE2 3689 C CE3 . TRP A 473 ? 0.5901 0.5748 0.5070 0.0939 -0.0375 0.0534 473 TRP A CE3 3690 C CZ2 . TRP A 473 ? 0.5485 0.5496 0.4828 0.0770 -0.0238 0.0364 473 TRP A CZ2 3691 C CZ3 . TRP A 473 ? 0.5932 0.5566 0.5061 0.0877 -0.0328 0.0512 473 TRP A CZ3 3692 C CH2 . TRP A 473 ? 0.5710 0.5442 0.4931 0.0794 -0.0262 0.0424 473 TRP A CH2 3693 N N . ALA A 474 ? 0.5923 0.6456 0.5026 0.1151 -0.0674 0.0703 474 ALA A N 3694 C CA . ALA A 474 ? 0.5968 0.6687 0.5025 0.1178 -0.0761 0.0741 474 ALA A CA 3695 C C . ALA A 474 ? 0.6159 0.6683 0.4945 0.1129 -0.0795 0.0867 474 ALA A C 3696 O O . ALA A 474 ? 0.5994 0.6644 0.4689 0.1038 -0.0796 0.0875 474 ALA A O 3697 C CB . ALA A 474 ? 0.6049 0.6891 0.5225 0.1362 -0.0861 0.0739 474 ALA A CB 3698 N N . THR A 475 ? 0.6470 0.6675 0.5115 0.1185 -0.0820 0.0965 475 THR A N 3699 C CA . THR A 475 ? 0.6841 0.6820 0.5206 0.1134 -0.0849 0.1102 475 THR A CA 3700 C C . THR A 475 ? 0.6866 0.6840 0.5136 0.0934 -0.0740 0.1094 475 THR A C 3701 O O . THR A 475 ? 0.7041 0.7015 0.5115 0.0859 -0.0750 0.1166 475 THR A O 3702 C CB . THR A 475 ? 0.7167 0.6754 0.5406 0.1212 -0.0879 0.1199 475 THR A CB 3703 O OG1 . THR A 475 ? 0.7148 0.6753 0.5485 0.1420 -0.0983 0.1199 475 THR A OG1 3704 C CG2 . THR A 475 ? 0.7538 0.6864 0.5462 0.1142 -0.0904 0.1357 475 THR A CG2 3705 N N . PHE A 476 ? 0.6648 0.6627 0.5052 0.0853 -0.0638 0.1005 476 PHE A N 3706 C CA . PHE A 476 ? 0.6615 0.6639 0.4981 0.0679 -0.0536 0.0976 476 PHE A CA 3707 C C . PHE A 476 ? 0.6422 0.6764 0.4849 0.0635 -0.0529 0.0898 476 PHE A C 3708 O O . PHE A 476 ? 0.6591 0.6977 0.4886 0.0529 -0.0491 0.0918 476 PHE A O 3709 C CB . PHE A 476 ? 0.6553 0.6517 0.5060 0.0620 -0.0448 0.0895 476 PHE A CB 3710 C CG . PHE A 476 ? 0.6468 0.6549 0.4999 0.0467 -0.0351 0.0839 476 PHE A CG 3711 C CD1 . PHE A 476 ? 0.6612 0.6553 0.4997 0.0343 -0.0292 0.0903 476 PHE A CD1 3712 C CD2 . PHE A 476 ? 0.6128 0.6459 0.4828 0.0448 -0.0318 0.0722 476 PHE A CD2 3713 C CE1 . PHE A 476 ? 0.6400 0.6477 0.4829 0.0217 -0.0203 0.0842 476 PHE A CE1 3714 C CE2 . PHE A 476 ? 0.5958 0.6386 0.4684 0.0329 -0.0237 0.0667 476 PHE A CE2 3715 C CZ . PHE A 476 ? 0.6080 0.6397 0.4681 0.0220 -0.0179 0.0722 476 PHE A CZ 3716 N N . ALA A 477 ? 0.6190 0.6750 0.4812 0.0708 -0.0560 0.0805 477 ALA A N 3717 C CA . ALA A 477 ? 0.6086 0.6928 0.4766 0.0666 -0.0565 0.0727 477 ALA A CA 3718 C C . ALA A 477 ? 0.6407 0.7295 0.4886 0.0665 -0.0636 0.0800 477 ALA A C 3719 O O . ALA A 477 ? 0.6274 0.7302 0.4692 0.0576 -0.0609 0.0757 477 ALA A O 3720 C CB . ALA A 477 ? 0.5909 0.6960 0.4812 0.0750 -0.0606 0.0639 477 ALA A CB 3721 N N . LYS A 478 ? 0.6764 0.7528 0.5137 0.0772 -0.0731 0.0906 478 LYS A N 3722 C CA . LYS A 478 ? 0.7177 0.7969 0.5346 0.0799 -0.0824 0.0990 478 LYS A CA 3723 C C . LYS A 478 ? 0.7364 0.7966 0.5245 0.0690 -0.0778 0.1095 478 LYS A C 3724 O O . LYS A 478 ? 0.7502 0.8202 0.5210 0.0644 -0.0806 0.1119 478 LYS A O 3725 C CB . LYS A 478 ? 0.7711 0.8424 0.5879 0.0975 -0.0952 0.1071 478 LYS A CB 3726 C CG . LYS A 478 ? 0.8414 0.9159 0.6366 0.1023 -0.1075 0.1168 478 LYS A CG 3727 C CD . LYS A 478 ? 0.8822 0.9533 0.6807 0.1220 -0.1219 0.1235 478 LYS A CD 3728 C CE . LYS A 478 ? 0.9270 1.0063 0.7046 0.1263 -0.1354 0.1320 478 LYS A CE 3729 N NZ . LYS A 478 ? 0.9747 1.0306 0.7381 0.1426 -0.1482 0.1466 478 LYS A NZ 3730 N N . THR A 479 ? 0.7284 0.7622 0.5108 0.0642 -0.0707 0.1154 479 THR A N 3731 C CA . THR A 479 ? 0.7437 0.7563 0.4980 0.0540 -0.0667 0.1276 479 THR A CA 3732 C C . THR A 479 ? 0.7275 0.7342 0.4830 0.0380 -0.0520 0.1243 479 THR A C 3733 O O . THR A 479 ? 0.7514 0.7474 0.4853 0.0267 -0.0466 0.1325 479 THR A O 3734 C CB . THR A 479 ? 0.7794 0.7579 0.5189 0.0623 -0.0737 0.1423 479 THR A CB 3735 O OG1 . THR A 479 ? 0.7685 0.7309 0.5242 0.0639 -0.0689 0.1385 479 THR A OG1 3736 C CG2 . THR A 479 ? 0.7873 0.7699 0.5258 0.0805 -0.0895 0.1468 479 THR A CG2 3737 N N . GLY A 480 ? 0.6924 0.7060 0.4725 0.0368 -0.0457 0.1128 480 GLY A N 3738 C CA . GLY A 480 ? 0.6832 0.6907 0.4671 0.0233 -0.0334 0.1098 480 GLY A CA 3739 C C . GLY A 480 ? 0.6990 0.6752 0.4784 0.0223 -0.0325 0.1179 480 GLY A C 3740 O O . GLY A 480 ? 0.6779 0.6473 0.4594 0.0103 -0.0233 0.1167 480 GLY A O 3741 N N . ASN A 481 ? 0.7246 0.6822 0.4987 0.0353 -0.0425 0.1254 481 ASN A N 3742 C CA . ASN A 481 ? 0.7509 0.6747 0.5199 0.0367 -0.0433 0.1324 481 ASN A CA 3743 C C . ASN A 481 ? 0.7541 0.6727 0.5366 0.0556 -0.0524 0.1292 481 ASN A C 3744 O O . ASN A 481 ? 0.7683 0.6929 0.5476 0.0687 -0.0624 0.1328 481 ASN A O 3745 C CB . ASN A 481 ? 0.7882 0.6847 0.5263 0.0319 -0.0459 0.1496 481 ASN A CB 3746 C CG . ASN A 481 ? 0.8168 0.6743 0.5470 0.0299 -0.0456 0.1570 481 ASN A CG 3747 O OD1 . ASN A 481 ? 0.8173 0.6655 0.5629 0.0389 -0.0478 0.1508 481 ASN A OD1 3748 N ND2 . ASN A 481 ? 0.8493 0.6833 0.5544 0.0175 -0.0426 0.1703 481 ASN A ND2 3749 N N . PRO A 482 ? 0.7461 0.6556 0.5442 0.0572 -0.0489 0.1218 482 PRO A N 3750 C CA . PRO A 482 ? 0.7468 0.6529 0.5581 0.0751 -0.0559 0.1174 482 PRO A CA 3751 C C . PRO A 482 ? 0.7876 0.6603 0.5827 0.0872 -0.0651 0.1291 482 PRO A C 3752 O O . PRO A 482 ? 0.7818 0.6554 0.5868 0.1051 -0.0726 0.1264 482 PRO A O 3753 C CB . PRO A 482 ? 0.7247 0.6270 0.5518 0.0704 -0.0483 0.1069 482 PRO A CB 3754 C CG . PRO A 482 ? 0.7410 0.6270 0.5559 0.0522 -0.0408 0.1115 482 PRO A CG 3755 C CD . PRO A 482 ? 0.7404 0.6425 0.5438 0.0428 -0.0388 0.1170 482 PRO A CD 3756 N N . ASN A 483 ? 0.8280 0.6715 0.5988 0.0777 -0.0645 0.1420 483 ASN A N 3757 C CA . ASN A 483 ? 0.8733 0.6792 0.6249 0.0881 -0.0735 0.1548 483 ASN A CA 3758 C C . ASN A 483 ? 0.9237 0.7345 0.6608 0.0989 -0.0847 0.1654 483 ASN A C 3759 O O . ASN A 483 ? 0.9095 0.7379 0.6359 0.0896 -0.0834 0.1695 483 ASN A O 3760 C CB . ASN A 483 ? 0.8855 0.6555 0.6151 0.0714 -0.0680 0.1652 483 ASN A CB 3761 C CG . ASN A 483 ? 0.8630 0.6251 0.6057 0.0611 -0.0589 0.1552 483 ASN A CG 3762 O OD1 . ASN A 483 ? 0.8533 0.5994 0.6053 0.0718 -0.0615 0.1492 483 ASN A OD1 3763 N ND2 . ASN A 483 ? 0.8455 0.6202 0.5896 0.0408 -0.0483 0.1527 483 ASN A ND2 3764 N N . GLU A 484 ? 0.9936 0.7891 0.7303 0.1195 -0.0961 0.1692 484 GLU A N 3765 C CA . GLU A 484 ? 1.0715 0.8649 0.7916 0.1317 -0.1092 0.1812 484 GLU A CA 3766 C C . GLU A 484 ? 1.1470 0.8954 0.8316 0.1235 -0.1110 0.2000 484 GLU A C 3767 O O . GLU A 484 ? 1.1429 0.8527 0.8204 0.1221 -0.1090 0.2035 484 GLU A O 3768 C CB . GLU A 484 ? 1.0867 0.8829 0.8225 0.1582 -0.1209 0.1774 484 GLU A CB 3769 C CG . GLU A 484 ? 1.1248 0.9372 0.8538 0.1726 -0.1354 0.1850 484 GLU A CG 3770 C CD . GLU A 484 ? 1.1079 0.9608 0.8688 0.1893 -0.1407 0.1713 484 GLU A CD 3771 O OE1 . GLU A 484 ? 1.1788 1.0263 0.9463 0.2120 -0.1522 0.1728 484 GLU A OE1 3772 O OE2 . GLU A 484 ? 1.0598 0.9500 0.8397 0.1795 -0.1329 0.1589 484 GLU A OE2 3773 N N . PRO A 485 ? 1.2062 0.9588 0.8669 0.1165 -0.1142 0.2120 485 PRO A N 3774 C CA . PRO A 485 ? 1.2780 0.9907 0.9019 0.1049 -0.1141 0.2309 485 PRO A CA 3775 C C . PRO A 485 ? 1.3515 1.0109 0.9578 0.1164 -0.1230 0.2436 485 PRO A C 3776 O O . PRO A 485 ? 1.3937 1.0155 0.9776 0.1010 -0.1174 0.2543 485 PRO A O 3777 C CB . PRO A 485 ? 1.2738 1.0049 0.8778 0.1055 -0.1215 0.2403 485 PRO A CB 3778 C CG . PRO A 485 ? 1.2129 0.9969 0.8433 0.1032 -0.1166 0.2232 485 PRO A CG 3779 C CD . PRO A 485 ? 1.1673 0.9644 0.8339 0.1151 -0.1155 0.2068 485 PRO A CD 3780 N N . HIS A 486 ? 1.3889 1.0445 1.0056 0.1426 -0.1364 0.2421 486 HIS A N 3781 C CA . HIS A 486 ? 1.4672 1.0703 1.0654 0.1569 -0.1469 0.2546 486 HIS A CA 3782 C C . HIS A 486 ? 1.4528 1.0334 1.0696 0.1643 -0.1434 0.2434 486 HIS A C 3783 O O . HIS A 486 ? 1.5035 1.0333 1.1011 0.1616 -0.1439 0.2523 486 HIS A O 3784 C CB . HIS A 486 ? 1.4911 1.0986 1.0847 0.1832 -0.1658 0.2622 486 HIS A CB 3785 N N . SER A 487 ? 1.3813 0.9989 1.0337 0.1731 -0.1398 0.2240 487 SER A N 3786 C CA . SER A 487 ? 1.3688 0.9721 1.0408 0.1825 -0.1367 0.2108 487 SER A CA 3787 C C . SER A 487 ? 1.4076 0.9520 1.0592 0.1743 -0.1338 0.2176 487 SER A C 3788 O O . SER A 487 ? 1.3941 0.9226 1.0296 0.1492 -0.1245 0.2236 487 SER A O 3789 C CB . SER A 487 ? 1.2830 0.9285 0.9858 0.1724 -0.1238 0.1911 487 SER A CB 3790 N N . GLN A 488 ? 1.4534 0.9665 1.1067 0.1958 -0.1419 0.2157 488 GLN A N 3791 C CA . GLN A 488 ? 1.4897 0.9484 1.1295 0.1902 -0.1390 0.2170 488 GLN A CA 3792 C C . GLN A 488 ? 1.4168 0.8907 1.0770 0.1740 -0.1244 0.1992 488 GLN A C 3793 O O . GLN A 488 ? 1.4177 0.8557 1.0660 0.1579 -0.1183 0.1999 488 GLN A O 3794 C CB . GLN A 488 ? 1.5267 0.9529 1.1670 0.2203 -0.1512 0.2160 488 GLN A CB 3795 N N . GLU A 489 ? 1.3612 0.8880 1.0518 0.1784 -0.1196 0.1834 489 GLU A N 3796 C CA . GLU A 489 ? 1.3035 0.8503 1.0136 0.1640 -0.1067 0.1668 489 GLU A CA 3797 C C . GLU A 489 ? 1.2870 0.8316 0.9848 0.1327 -0.0965 0.1725 489 GLU A C 3798 O O . GLU A 489 ? 1.2512 0.8073 0.9361 0.1221 -0.0965 0.1843 489 GLU A O 3799 C CB . GLU A 489 ? 1.2283 0.8334 0.9692 0.1724 -0.1040 0.1524 489 GLU A CB 3800 N N . SER A 490 ? 1.2791 0.8103 0.9811 0.1183 -0.0879 0.1634 490 SER A N 3801 C CA . SER A 490 ? 1.2596 0.7908 0.9542 0.0887 -0.0777 0.1664 490 SER A CA 3802 C C . SER A 490 ? 1.1823 0.7679 0.8923 0.0778 -0.0705 0.1619 490 SER A C 3803 O O . SER A 490 ? 1.1166 0.7406 0.8497 0.0888 -0.0700 0.1498 490 SER A O 3804 C CB . SER A 490 ? 1.2662 0.7785 0.9671 0.0778 -0.0713 0.1545 490 SER A CB 3805 O OG . SER A 490 ? 1.3273 0.7825 1.0086 0.0816 -0.0768 0.1604 490 SER A OG 3806 N N . LYS A 491 ? 1.1527 0.7402 0.8491 0.0561 -0.0647 0.1716 491 LYS A N 3807 C CA . LYS A 491 ? 1.0807 0.7152 0.7880 0.0454 -0.0578 0.1683 491 LYS A CA 3808 C C . LYS A 491 ? 1.0243 0.6848 0.7558 0.0351 -0.0485 0.1517 491 LYS A C 3809 O O . LYS A 491 ? 1.0610 0.7009 0.7917 0.0224 -0.0439 0.1484 491 LYS A O 3810 C CB . LYS A 491 ? 1.0943 0.7218 0.7787 0.0250 -0.0532 0.1831 491 LYS A CB 3811 C CG . LYS A 491 ? 1.1337 0.7382 0.7905 0.0333 -0.0625 0.2013 491 LYS A CG 3812 N N . TRP A 492 ? 0.9369 0.6412 0.6892 0.0410 -0.0466 0.1414 492 TRP A N 3813 C CA . TRP A 492 ? 0.8736 0.6079 0.6463 0.0297 -0.0378 0.1280 492 TRP A CA 3814 C C . TRP A 492 ? 0.8811 0.6274 0.6465 0.0083 -0.0300 0.1339 492 TRP A C 3815 O O . TRP A 492 ? 0.8836 0.6519 0.6450 0.0081 -0.0297 0.1386 492 TRP A O 3816 C CB . TRP A 492 ? 0.8235 0.5976 0.6169 0.0430 -0.0390 0.1177 492 TRP A CB 3817 C CG . TRP A 492 ? 0.7524 0.5584 0.5668 0.0346 -0.0314 0.1042 492 TRP A CG 3818 C CD1 . TRP A 492 ? 0.7423 0.5525 0.5602 0.0165 -0.0238 0.1008 492 TRP A CD1 3819 C CD2 . TRP A 492 ? 0.6886 0.5268 0.5228 0.0444 -0.0314 0.0932 492 TRP A CD2 3820 N NE1 . TRP A 492 ? 0.6895 0.5305 0.5272 0.0160 -0.0200 0.0886 492 TRP A NE1 3821 C CE2 . TRP A 492 ? 0.6569 0.5142 0.5039 0.0323 -0.0242 0.0841 492 TRP A CE2 3822 C CE3 . TRP A 492 ? 0.6809 0.5338 0.5235 0.0621 -0.0369 0.0901 492 TRP A CE3 3823 C CZ2 . TRP A 492 ? 0.6199 0.5064 0.4851 0.0368 -0.0224 0.0732 492 TRP A CZ2 3824 C CZ3 . TRP A 492 ? 0.6444 0.5286 0.5065 0.0651 -0.0342 0.0787 492 TRP A CZ3 3825 C CH2 . TRP A 492 ? 0.6152 0.5140 0.4871 0.0524 -0.0270 0.0708 492 TRP A CH2 3826 N N . PRO A 493 ? 0.8931 0.6268 0.6570 -0.0101 -0.0235 0.1331 493 PRO A N 3827 C CA . PRO A 493 ? 0.8959 0.6398 0.6517 -0.0306 -0.0156 0.1397 493 PRO A CA 3828 C C . PRO A 493 ? 0.8449 0.6353 0.6200 -0.0357 -0.0087 0.1297 493 PRO A C 3829 O O . PRO A 493 ? 0.8332 0.6438 0.6289 -0.0278 -0.0091 0.1168 493 PRO A O 3830 C CB . PRO A 493 ? 0.9181 0.6365 0.6707 -0.0482 -0.0113 0.1398 493 PRO A CB 3831 C CG . PRO A 493 ? 0.9096 0.6250 0.6791 -0.0389 -0.0143 0.1261 493 PRO A CG 3832 C CD . PRO A 493 ? 0.8996 0.6147 0.6712 -0.0139 -0.0226 0.1244 493 PRO A CD 3833 N N . LEU A 494 ? 0.8517 0.6573 0.6185 -0.0486 -0.0024 0.1357 494 LEU A N 3834 C CA . LEU A 494 ? 0.8169 0.6634 0.6007 -0.0557 0.0054 0.1261 494 LEU A CA 3835 C C . LEU A 494 ? 0.8038 0.6572 0.6056 -0.0675 0.0109 0.1161 494 LEU A C 3836 O O . LEU A 494 ? 0.8259 0.6547 0.6216 -0.0792 0.0123 0.1199 494 LEU A O 3837 C CB . LEU A 494 ? 0.8259 0.6842 0.5949 -0.0692 0.0126 0.1345 494 LEU A CB 3838 C CG . LEU A 494 ? 0.8303 0.7035 0.5881 -0.0598 0.0096 0.1388 494 LEU A CG 3839 C CD1 . LEU A 494 ? 0.8723 0.7453 0.6077 -0.0752 0.0167 0.1501 494 LEU A CD1 3840 C CD2 . LEU A 494 ? 0.7866 0.6983 0.5656 -0.0523 0.0110 0.1248 494 LEU A CD2 3841 N N . PHE A 495 ? 0.7770 0.6635 0.6007 -0.0644 0.0134 0.1033 495 PHE A N 3842 C CA . PHE A 495 ? 0.7828 0.6840 0.6249 -0.0754 0.0186 0.0935 495 PHE A CA 3843 C C . PHE A 495 ? 0.7909 0.7143 0.6333 -0.0916 0.0283 0.0954 495 PHE A C 3844 O O . PHE A 495 ? 0.7571 0.7056 0.6010 -0.0882 0.0314 0.0936 495 PHE A O 3845 C CB . PHE A 495 ? 0.7420 0.6673 0.6056 -0.0638 0.0163 0.0801 495 PHE A CB 3846 C CG . PHE A 495 ? 0.7235 0.6666 0.6062 -0.0732 0.0200 0.0699 495 PHE A CG 3847 C CD1 . PHE A 495 ? 0.7100 0.6841 0.6038 -0.0811 0.0270 0.0656 495 PHE A CD1 3848 C CD2 . PHE A 495 ? 0.7388 0.6685 0.6285 -0.0730 0.0161 0.0640 495 PHE A CD2 3849 C CE1 . PHE A 495 ? 0.7039 0.6961 0.6169 -0.0881 0.0292 0.0562 495 PHE A CE1 3850 C CE2 . PHE A 495 ? 0.7337 0.6811 0.6409 -0.0810 0.0181 0.0547 495 PHE A CE2 3851 C CZ . PHE A 495 ? 0.7198 0.6989 0.6394 -0.0883 0.0242 0.0512 495 PHE A CZ 3852 N N . THR A 496 ? 0.8266 0.7410 0.6674 -0.1095 0.0333 0.0983 496 THR A N 3853 C CA . THR A 496 ? 0.8431 0.7812 0.6871 -0.1266 0.0440 0.0989 496 THR A CA 3854 C C . THR A 496 ? 0.8216 0.7820 0.6914 -0.1346 0.0470 0.0866 496 THR A C 3855 O O . THR A 496 ? 0.8209 0.7677 0.6987 -0.1326 0.0411 0.0815 496 THR A O 3856 C CB . THR A 496 ? 0.8893 0.8019 0.7113 -0.1444 0.0486 0.1129 496 THR A CB 3857 O OG1 . THR A 496 ? 0.9281 0.8174 0.7533 -0.1546 0.0465 0.1123 496 THR A OG1 3858 C CG2 . THR A 496 ? 0.9105 0.7936 0.7045 -0.1354 0.0430 0.1266 496 THR A CG2 3859 N N . THR A 497 ? 0.8264 0.8218 0.7089 -0.1431 0.0558 0.0814 497 THR A N 3860 C CA . THR A 497 ? 0.8039 0.8243 0.7121 -0.1516 0.0587 0.0703 497 THR A CA 3861 C C . THR A 497 ? 0.8238 0.8227 0.7300 -0.1688 0.0586 0.0738 497 THR A C 3862 O O . THR A 497 ? 0.7802 0.7811 0.7026 -0.1701 0.0540 0.0653 497 THR A O 3863 C CB . THR A 497 ? 0.7999 0.8595 0.7194 -0.1607 0.0700 0.0661 497 THR A CB 3864 O OG1 . THR A 497 ? 0.8138 0.8880 0.7286 -0.1472 0.0712 0.0646 497 THR A OG1 3865 C CG2 . THR A 497 ? 0.7816 0.8722 0.7318 -0.1635 0.0708 0.0526 497 THR A CG2 3866 N N . LYS A 498 ? 0.8743 0.8511 0.7588 -0.1822 0.0632 0.0868 498 LYS A N 3867 C CA . LYS A 498 ? 0.9134 0.8704 0.7941 -0.2028 0.0653 0.0914 498 LYS A CA 3868 C C . LYS A 498 ? 0.9177 0.8345 0.7914 -0.1976 0.0546 0.0915 498 LYS A C 3869 O O . LYS A 498 ? 0.8936 0.8078 0.7794 -0.2082 0.0526 0.0850 498 LYS A O 3870 C CB . LYS A 498 ? 0.9729 0.9139 0.8282 -0.2179 0.0733 0.1068 498 LYS A CB 3871 C CG . LYS A 498 ? 1.0384 0.9604 0.8888 -0.2433 0.0775 0.1125 498 LYS A CG 3872 C CD . LYS A 498 ? 1.1112 1.0048 0.9291 -0.2554 0.0830 0.1307 498 LYS A CD 3873 C CE . LYS A 498 ? 1.1634 1.0091 0.9650 -0.2703 0.0795 0.1395 498 LYS A CE 3874 N NZ . LYS A 498 ? 1.2183 1.0346 0.9860 -0.2825 0.0847 0.1586 498 LYS A NZ 3875 N N . GLU A 499 ? 0.9300 0.8169 0.7844 -0.1812 0.0475 0.0983 499 GLU A N 3876 C CA . GLU A 499 ? 0.9479 0.7927 0.7919 -0.1750 0.0381 0.0994 499 GLU A CA 3877 C C . GLU A 499 ? 0.8899 0.7391 0.7456 -0.1529 0.0296 0.0884 499 GLU A C 3878 O O . GLU A 499 ? 0.9079 0.7337 0.7635 -0.1497 0.0231 0.0836 499 GLU A O 3879 C CB . GLU A 499 ? 1.0200 0.8242 0.8335 -0.1723 0.0358 0.1152 499 GLU A CB 3880 C CG . GLU A 499 ? 1.0933 0.8822 0.8899 -0.1962 0.0436 0.1279 499 GLU A CG 3881 C CD . GLU A 499 ? 1.1761 0.9504 0.9455 -0.1923 0.0449 0.1437 499 GLU A CD 3882 O OE1 . GLU A 499 ? 1.1603 0.9644 0.9324 -0.1821 0.0472 0.1429 499 GLU A OE1 3883 O OE2 . GLU A 499 ? 1.2563 0.9878 1.0004 -0.1997 0.0430 0.1572 499 GLU A OE2 3884 N N . GLN A 500 ? 0.8374 0.7152 0.7017 -0.1383 0.0299 0.0845 500 GLN A N 3885 C CA . GLN A 500 ? 0.8003 0.6902 0.6788 -0.1204 0.0237 0.0732 500 GLN A CA 3886 C C . GLN A 500 ? 0.7932 0.6503 0.6606 -0.1052 0.0152 0.0739 500 GLN A C 3887 O O . GLN A 500 ? 0.7910 0.6459 0.6675 -0.0983 0.0104 0.0643 500 GLN A O 3888 C CB . GLN A 500 ? 0.7958 0.7077 0.6967 -0.1277 0.0238 0.0608 500 GLN A CB 3889 C CG . GLN A 500 ? 0.7910 0.7408 0.7071 -0.1396 0.0320 0.0582 500 GLN A CG 3890 C CD . GLN A 500 ? 0.7615 0.7397 0.7023 -0.1396 0.0302 0.0450 500 GLN A CD 3891 O OE1 . GLN A 500 ? 0.7865 0.7741 0.7352 -0.1241 0.0252 0.0379 500 GLN A OE1 3892 N NE2 . GLN A 500 ? 0.7587 0.7512 0.7117 -0.1572 0.0339 0.0420 500 GLN A NE2 3893 N N . LYS A 501 ? 0.8120 0.6452 0.6595 -0.0990 0.0133 0.0852 501 LYS A N 3894 C CA . LYS A 501 ? 0.8158 0.6158 0.6517 -0.0843 0.0056 0.0870 501 LYS A CA 3895 C C . LYS A 501 ? 0.7693 0.5854 0.6139 -0.0629 0.0013 0.0805 501 LYS A C 3896 O O . LYS A 501 ? 0.7587 0.6025 0.6089 -0.0576 0.0033 0.0807 501 LYS A O 3897 C CB . LYS A 501 ? 0.8723 0.6406 0.6833 -0.0852 0.0043 0.1025 501 LYS A CB 3898 C CG . LYS A 501 ? 0.9140 0.6600 0.7132 -0.1079 0.0087 0.1102 501 LYS A CG 3899 C CD . LYS A 501 ? 0.9562 0.6668 0.7274 -0.1087 0.0068 0.1271 501 LYS A CD 3900 C CE . LYS A 501 ? 0.9998 0.6728 0.7574 -0.1282 0.0082 0.1333 501 LYS A CE 3901 N NZ . LYS A 501 ? 1.0373 0.6939 0.7713 -0.1420 0.0126 0.1505 501 LYS A NZ 3902 N N . PHE A 502 ? 0.7631 0.5617 0.6086 -0.0512 -0.0042 0.0744 502 PHE A N 3903 C CA . PHE A 502 ? 0.7389 0.5485 0.5906 -0.0310 -0.0081 0.0693 502 PHE A CA 3904 C C . PHE A 502 ? 0.7573 0.5331 0.5987 -0.0181 -0.0140 0.0698 502 PHE A C 3905 O O . PHE A 502 ? 0.7953 0.5380 0.6248 -0.0251 -0.0154 0.0730 502 PHE A O 3906 C CB . PHE A 502 ? 0.7119 0.5492 0.5826 -0.0293 -0.0068 0.0564 502 PHE A CB 3907 C CG . PHE A 502 ? 0.7143 0.5369 0.5876 -0.0334 -0.0085 0.0476 502 PHE A CG 3908 C CD1 . PHE A 502 ? 0.7320 0.5529 0.6078 -0.0516 -0.0063 0.0459 502 PHE A CD1 3909 C CD2 . PHE A 502 ? 0.7138 0.5269 0.5876 -0.0196 -0.0122 0.0402 502 PHE A CD2 3910 C CE1 . PHE A 502 ? 0.7360 0.5443 0.6137 -0.0559 -0.0088 0.0370 502 PHE A CE1 3911 C CE2 . PHE A 502 ? 0.7307 0.5305 0.6049 -0.0234 -0.0138 0.0312 502 PHE A CE2 3912 C CZ . PHE A 502 ? 0.7330 0.5297 0.6086 -0.0417 -0.0127 0.0296 502 PHE A CZ 3913 N N . ILE A 503 ? 0.7560 0.5403 0.6023 0.0007 -0.0174 0.0661 503 ILE A N 3914 C CA . ILE A 503 ? 0.7913 0.5476 0.6304 0.0162 -0.0228 0.0648 503 ILE A CA 3915 C C . ILE A 503 ? 0.7638 0.5329 0.6158 0.0273 -0.0229 0.0513 503 ILE A C 3916 O O . ILE A 503 ? 0.7406 0.5428 0.6065 0.0285 -0.0202 0.0455 503 ILE A O 3917 C CB . ILE A 503 ? 0.8194 0.5700 0.6500 0.0312 -0.0277 0.0746 503 ILE A CB 3918 C CG1 . ILE A 503 ? 0.7949 0.5845 0.6390 0.0408 -0.0275 0.0719 503 ILE A CG1 3919 C CG2 . ILE A 503 ? 0.8508 0.5840 0.6639 0.0205 -0.0281 0.0894 503 ILE A CG2 3920 C CD1 . ILE A 503 ? 0.8118 0.5979 0.6509 0.0587 -0.0341 0.0783 503 ILE A CD1 3921 N N . ASP A 504 ? 0.7985 0.5399 0.6446 0.0353 -0.0256 0.0461 504 ASP A N 3922 C CA . ASP A 504 ? 0.7940 0.5458 0.6495 0.0490 -0.0255 0.0340 504 ASP A CA 3923 C C . ASP A 504 ? 0.7863 0.5496 0.6458 0.0682 -0.0282 0.0371 504 ASP A C 3924 O O . ASP A 504 ? 0.7959 0.5401 0.6454 0.0752 -0.0327 0.0466 504 ASP A O 3925 C CB . ASP A 504 ? 0.8290 0.5468 0.6757 0.0520 -0.0272 0.0262 504 ASP A CB 3926 C CG . ASP A 504 ? 0.8356 0.5452 0.6801 0.0328 -0.0253 0.0208 504 ASP A CG 3927 O OD1 . ASP A 504 ? 0.8205 0.5582 0.6750 0.0210 -0.0223 0.0192 504 ASP A OD1 3928 O OD2 . ASP A 504 ? 0.8517 0.5265 0.6849 0.0300 -0.0275 0.0175 504 ASP A OD2 3929 N N . LEU A 505 ? 0.7548 0.5498 0.6286 0.0761 -0.0259 0.0296 505 LEU A N 3930 C CA . LEU A 505 ? 0.7497 0.5580 0.6304 0.0950 -0.0283 0.0293 505 LEU A CA 3931 C C . LEU A 505 ? 0.7602 0.5642 0.6453 0.1083 -0.0270 0.0173 505 LEU A C 3932 O O . LEU A 505 ? 0.7365 0.5605 0.6302 0.1061 -0.0222 0.0078 505 LEU A O 3933 C CB . LEU A 505 ? 0.7235 0.5722 0.6178 0.0938 -0.0262 0.0295 505 LEU A CB 3934 C CG . LEU A 505 ? 0.7307 0.5879 0.6211 0.0873 -0.0283 0.0410 505 LEU A CG 3935 C CD1 . LEU A 505 ? 0.6975 0.5932 0.6016 0.0871 -0.0264 0.0385 505 LEU A CD1 3936 C CD2 . LEU A 505 ? 0.7671 0.6053 0.6473 0.0988 -0.0352 0.0507 505 LEU A CD2 3937 N N . ASN A 506 ? 0.7988 0.5755 0.6765 0.1223 -0.0311 0.0177 506 ASN A N 3938 C CA . ASN A 506 ? 0.8105 0.5816 0.6916 0.1370 -0.0295 0.0055 506 ASN A CA 3939 C C . ASN A 506 ? 0.8378 0.5874 0.7149 0.1572 -0.0356 0.0084 506 ASN A C 3940 O O . ASN A 506 ? 0.8594 0.6014 0.7314 0.1596 -0.0415 0.0206 506 ASN A O 3941 C CB . ASN A 506 ? 0.8416 0.5889 0.7130 0.1267 -0.0267 -0.0031 506 ASN A CB 3942 C CG . ASN A 506 ? 0.8839 0.5890 0.7380 0.1174 -0.0309 0.0040 506 ASN A CG 3943 O OD1 . ASN A 506 ? 0.9163 0.5959 0.7619 0.1269 -0.0363 0.0116 506 ASN A OD1 3944 N ND2 . ASN A 506 ? 0.8808 0.5781 0.7295 0.0984 -0.0289 0.0016 506 ASN A ND2 3945 N N . THR A 507 ? 0.8674 0.6070 0.7461 0.1723 -0.0343 -0.0030 507 THR A N 3946 C CA . THR A 507 ? 0.9052 0.6246 0.7819 0.1947 -0.0404 -0.0018 507 THR A CA 3947 C C . THR A 507 ? 0.9633 0.6282 0.8187 0.1934 -0.0463 0.0044 507 THR A C 3948 O O . THR A 507 ? 0.9888 0.6317 0.8396 0.2110 -0.0531 0.0089 507 THR A O 3949 C CB . THR A 507 ? 0.9072 0.6382 0.7949 0.2132 -0.0360 -0.0177 507 THR A CB 3950 O OG1 . THR A 507 ? 0.9135 0.6207 0.7906 0.2069 -0.0314 -0.0292 507 THR A OG1 3951 C CG2 . THR A 507 ? 0.8620 0.6464 0.7704 0.2136 -0.0299 -0.0231 507 THR A CG2 3952 N N . GLU A 508 ? 0.9960 0.6386 0.8387 0.1729 -0.0440 0.0045 508 GLU A N 3953 C CA . GLU A 508 ? 1.0548 0.6450 0.8765 0.1672 -0.0490 0.0111 508 GLU A CA 3954 C C . GLU A 508 ? 1.0819 0.6635 0.8944 0.1594 -0.0544 0.0304 508 GLU A C 3955 O O . GLU A 508 ? 1.0177 0.6342 0.8387 0.1507 -0.0526 0.0371 508 GLU A O 3956 C CB . GLU A 508 ? 1.0479 0.6216 0.8611 0.1462 -0.0447 0.0038 508 GLU A CB 3957 N N . PRO A 509 ? 1.1813 0.7152 0.9750 0.1625 -0.0609 0.0395 509 PRO A N 3958 C CA . PRO A 509 ? 1.2052 0.7303 0.9871 0.1546 -0.0657 0.0586 509 PRO A CA 3959 C C . PRO A 509 ? 1.1951 0.7338 0.9750 0.1256 -0.0598 0.0636 509 PRO A C 3960 O O . PRO A 509 ? 1.1863 0.7112 0.9624 0.1093 -0.0556 0.0569 509 PRO A O 3961 C CB . PRO A 509 ? 1.2600 0.7245 1.0192 0.1603 -0.0728 0.0660 509 PRO A CB 3962 C CG . PRO A 509 ? 1.2802 0.7190 1.0375 0.1620 -0.0701 0.0499 509 PRO A CG 3963 C CD . PRO A 509 ? 1.2390 0.7229 1.0190 0.1719 -0.0641 0.0332 509 PRO A CD 3964 N N . MET A 510 ? 1.2168 0.7838 0.9997 0.1201 -0.0598 0.0744 510 MET A N 3965 C CA . MET A 510 ? 1.2009 0.7922 0.9869 0.0958 -0.0534 0.0773 510 MET A CA 3966 C C . MET A 510 ? 1.2003 0.7598 0.9724 0.0731 -0.0506 0.0798 510 MET A C 3967 O O . MET A 510 ? 1.2291 0.7483 0.9814 0.0689 -0.0544 0.0912 510 MET A O 3968 C CB . MET A 510 ? 1.2140 0.8248 0.9967 0.0938 -0.0554 0.0916 510 MET A CB 3969 C CG . MET A 510 ? 1.1975 0.8463 0.9897 0.0749 -0.0482 0.0911 510 MET A CG 3970 S SD . MET A 510 ? 1.2169 0.8802 0.9989 0.0699 -0.0501 0.1079 510 MET A SD 3971 C CE . MET A 510 ? 1.2929 0.9067 1.0472 0.0523 -0.0503 0.1225 510 MET A CE 3972 N N . LYS A 511 ? 1.1646 0.7423 0.9473 0.0584 -0.0443 0.0690 511 LYS A N 3973 C CA . LYS A 511 ? 1.1357 0.6971 0.9108 0.0332 -0.0408 0.0704 511 LYS A CA 3974 C C . LYS A 511 ? 1.0728 0.6759 0.8591 0.0165 -0.0348 0.0731 511 LYS A C 3975 O O . LYS A 511 ? 1.0279 0.6712 0.8311 0.0223 -0.0324 0.0663 511 LYS A O 3976 C CB . LYS A 511 ? 1.1040 0.6521 0.8820 0.0294 -0.0397 0.0550 511 LYS A CB 3977 N N . VAL A 512 ? 1.0587 0.6510 0.8351 -0.0040 -0.0323 0.0831 512 VAL A N 3978 C CA . VAL A 512 ? 0.9986 0.6273 0.7845 -0.0208 -0.0260 0.0856 512 VAL A CA 3979 C C . VAL A 512 ? 0.9729 0.6057 0.7667 -0.0404 -0.0220 0.0766 512 VAL A C 3980 O O . VAL A 512 ? 1.0118 0.6097 0.7953 -0.0500 -0.0235 0.0758 512 VAL A O 3981 C CB . VAL A 512 ? 1.0328 0.6502 0.8023 -0.0319 -0.0247 0.1027 512 VAL A CB 3982 C CG1 . VAL A 512 ? 1.0077 0.6615 0.7868 -0.0509 -0.0168 0.1038 512 VAL A CG1 3983 C CG2 . VAL A 512 ? 1.0373 0.6530 0.7981 -0.0125 -0.0300 0.1123 512 VAL A CG2 3984 N N . HIS A 513 ? 0.9193 0.5943 0.7313 -0.0464 -0.0176 0.0698 513 HIS A N 3985 C CA . HIS A 513 ? 0.8937 0.5801 0.7165 -0.0634 -0.0149 0.0606 513 HIS A CA 3986 C C . HIS A 513 ? 0.8530 0.5740 0.6860 -0.0789 -0.0087 0.0644 513 HIS A C 3987 O O . HIS A 513 ? 0.8493 0.5829 0.6791 -0.0762 -0.0062 0.0735 513 HIS A O 3988 C CB . HIS A 513 ? 0.8798 0.5847 0.7163 -0.0521 -0.0168 0.0458 513 HIS A CB 3989 C CG . HIS A 513 ? 0.9072 0.5809 0.7348 -0.0378 -0.0216 0.0394 513 HIS A CG 3990 N ND1 . HIS A 513 ? 0.9485 0.5846 0.7647 -0.0457 -0.0242 0.0360 513 HIS A ND1 3991 C CD2 . HIS A 513 ? 0.8969 0.5730 0.7261 -0.0163 -0.0238 0.0346 513 HIS A CD2 3992 C CE1 . HIS A 513 ? 0.9652 0.5806 0.7755 -0.0283 -0.0278 0.0290 513 HIS A CE1 3993 N NE2 . HIS A 513 ? 0.9311 0.5718 0.7499 -0.0103 -0.0272 0.0282 513 HIS A NE2 3994 N N . GLN A 514 ? 0.8508 0.5882 0.6962 -0.0946 -0.0063 0.0568 514 GLN A N 3995 C CA . GLN A 514 ? 0.8280 0.6018 0.6865 -0.1084 0.0000 0.0581 514 GLN A CA 3996 C C . GLN A 514 ? 0.7887 0.5951 0.6683 -0.1096 -0.0005 0.0449 514 GLN A C 3997 O O . GLN A 514 ? 0.7940 0.5903 0.6757 -0.1074 -0.0053 0.0354 514 GLN A O 3998 C CB . GLN A 514 ? 0.8564 0.6167 0.7080 -0.1321 0.0042 0.0654 514 GLN A CB 3999 C CG . GLN A 514 ? 0.9031 0.6331 0.7317 -0.1336 0.0055 0.0809 514 GLN A CG 4000 C CD . GLN A 514 ? 0.9477 0.6596 0.7672 -0.1591 0.0100 0.0885 514 GLN A CD 4001 O OE1 . GLN A 514 ? 0.9766 0.6454 0.7803 -0.1648 0.0066 0.0920 514 GLN A OE1 4002 N NE2 . GLN A 514 ? 0.9343 0.6787 0.7636 -0.1750 0.0182 0.0906 514 GLN A NE2 4003 N N . ARG A 515 ? 0.7737 0.6183 0.6677 -0.1124 0.0041 0.0442 515 ARG A N 4004 C CA . ARG A 515 ? 0.7480 0.6253 0.6627 -0.1149 0.0035 0.0331 515 ARG A CA 4005 C C . ARG A 515 ? 0.7283 0.6047 0.6463 -0.0998 -0.0028 0.0234 515 ARG A C 4006 O O . ARG A 515 ? 0.7240 0.5951 0.6454 -0.1048 -0.0069 0.0151 515 ARG A O 4007 C CB . ARG A 515 ? 0.7766 0.6553 0.6982 -0.1362 0.0044 0.0301 515 ARG A CB 4008 C CG . ARG A 515 ? 0.8200 0.7037 0.7392 -0.1529 0.0123 0.0395 515 ARG A CG 4009 C CD . ARG A 515 ? 0.8453 0.7424 0.7777 -0.1752 0.0143 0.0350 515 ARG A CD 4010 N NE . ARG A 515 ? 0.8786 0.7989 0.8160 -0.1883 0.0239 0.0416 515 ARG A NE 4011 C CZ . ARG A 515 ? 0.9197 0.8198 0.8401 -0.2002 0.0298 0.0538 515 ARG A CZ 4012 N NH1 . ARG A 515 ? 0.9479 0.8012 0.8451 -0.2003 0.0263 0.0613 515 ARG A NH1 4013 N NH2 . ARG A 515 ? 0.9305 0.8566 0.8560 -0.2120 0.0396 0.0585 515 ARG A NH2 4014 N N . LEU A 516 ? 0.7095 0.5921 0.6260 -0.0824 -0.0032 0.0243 516 LEU A N 4015 C CA . LEU A 516 ? 0.6955 0.5794 0.6142 -0.0682 -0.0076 0.0161 516 LEU A CA 4016 C C . LEU A 516 ? 0.6869 0.5965 0.6210 -0.0721 -0.0095 0.0068 516 LEU A C 4017 O O . LEU A 516 ? 0.6833 0.6223 0.6299 -0.0713 -0.0073 0.0063 516 LEU A O 4018 C CB . LEU A 516 ? 0.6898 0.5835 0.6077 -0.0518 -0.0065 0.0192 516 LEU A CB 4019 C CG . LEU A 516 ? 0.6771 0.5786 0.5986 -0.0376 -0.0092 0.0116 516 LEU A CG 4020 C CD1 . LEU A 516 ? 0.7105 0.5849 0.6219 -0.0325 -0.0127 0.0068 516 LEU A CD1 4021 C CD2 . LEU A 516 ? 0.6653 0.5779 0.5872 -0.0247 -0.0077 0.0155 516 LEU A CD2 4022 N N . ARG A 517 ? 0.7041 0.6011 0.6361 -0.0759 -0.0143 -0.0008 517 ARG A N 4023 C CA . ARG A 517 ? 0.6884 0.6056 0.6321 -0.0788 -0.0184 -0.0099 517 ARG A CA 4024 C C . ARG A 517 ? 0.6572 0.6046 0.6184 -0.0903 -0.0168 -0.0103 517 ARG A C 4025 O O . ARG A 517 ? 0.6146 0.5877 0.5879 -0.0852 -0.0186 -0.0145 517 ARG A O 4026 C CB . ARG A 517 ? 0.7072 0.6374 0.6528 -0.0632 -0.0199 -0.0136 517 ARG A CB 4027 C CG . ARG A 517 ? 0.7584 0.6668 0.6900 -0.0498 -0.0199 -0.0134 517 ARG A CG 4028 C CD . ARG A 517 ? 0.7745 0.6971 0.7084 -0.0385 -0.0215 -0.0184 517 ARG A CD 4029 N NE . ARG A 517 ? 0.7913 0.7088 0.7215 -0.0414 -0.0267 -0.0271 517 ARG A NE 4030 C CZ . ARG A 517 ? 0.8347 0.7289 0.7515 -0.0376 -0.0283 -0.0322 517 ARG A CZ 4031 N NH1 . ARG A 517 ? 0.8430 0.7174 0.7507 -0.0297 -0.0251 -0.0292 517 ARG A NH1 4032 N NH2 . ARG A 517 ? 0.8567 0.7479 0.7688 -0.0410 -0.0335 -0.0407 517 ARG A NH2 4033 N N . VAL A 518 ? 0.6784 0.6226 0.6408 -0.1054 -0.0133 -0.0059 518 VAL A N 4034 C CA . VAL A 518 ? 0.6736 0.6489 0.6545 -0.1177 -0.0110 -0.0074 518 VAL A CA 4035 C C . VAL A 518 ? 0.6694 0.6633 0.6640 -0.1204 -0.0181 -0.0177 518 VAL A C 4036 O O . VAL A 518 ? 0.6704 0.6957 0.6813 -0.1166 -0.0186 -0.0208 518 VAL A O 4037 C CB . VAL A 518 ? 0.6920 0.6591 0.6715 -0.1376 -0.0063 -0.0023 518 VAL A CB 4038 C CG1 . VAL A 518 ? 0.6913 0.6695 0.6705 -0.1391 0.0027 0.0069 518 VAL A CG1 4039 C CG2 . VAL A 518 ? 0.7228 0.6470 0.6829 -0.1427 -0.0089 -0.0002 518 VAL A CG2 4040 N N . GLN A 519 ? 0.7024 0.6765 0.6899 -0.1266 -0.0242 -0.0231 519 GLN A N 4041 C CA . GLN A 519 ? 0.7459 0.7383 0.7459 -0.1324 -0.0319 -0.0327 519 GLN A CA 4042 C C . GLN A 519 ? 0.6930 0.7040 0.6982 -0.1162 -0.0367 -0.0369 519 GLN A C 4043 O O . GLN A 519 ? 0.6868 0.7292 0.7102 -0.1165 -0.0395 -0.0404 519 GLN A O 4044 C CB . GLN A 519 ? 0.8354 0.7996 0.8229 -0.1407 -0.0383 -0.0388 519 GLN A CB 4045 C CG . GLN A 519 ? 0.8926 0.8752 0.8906 -0.1453 -0.0481 -0.0492 519 GLN A CG 4046 C CD . GLN A 519 ? 0.9925 0.9519 0.9816 -0.1600 -0.0538 -0.0559 519 GLN A CD 4047 O OE1 . GLN A 519 ? 1.0335 0.9781 1.0103 -0.1549 -0.0611 -0.0634 519 GLN A OE1 4048 N NE2 . GLN A 519 ? 1.0460 1.0015 1.0403 -0.1793 -0.0502 -0.0535 519 GLN A NE2 4049 N N . MET A 520 ? 0.6604 0.6519 0.6497 -0.1020 -0.0375 -0.0363 520 MET A N 4050 C CA . MET A 520 ? 0.6334 0.6384 0.6243 -0.0877 -0.0414 -0.0390 520 MET A CA 4051 C C . MET A 520 ? 0.5805 0.6114 0.5851 -0.0809 -0.0369 -0.0348 520 MET A C 4052 O O . MET A 520 ? 0.5684 0.6205 0.5834 -0.0752 -0.0413 -0.0381 520 MET A O 4053 C CB . MET A 520 ? 0.6605 0.6406 0.6319 -0.0752 -0.0411 -0.0389 520 MET A CB 4054 C CG . MET A 520 ? 0.7103 0.6669 0.6674 -0.0789 -0.0467 -0.0459 520 MET A CG 4055 S SD . MET A 520 ? 0.7360 0.7092 0.6983 -0.0834 -0.0581 -0.0555 520 MET A SD 4056 C CE . MET A 520 ? 0.7541 0.7309 0.7278 -0.1049 -0.0611 -0.0590 520 MET A CE 4057 N N . CYS A 521 ? 0.5493 0.5774 0.5527 -0.0811 -0.0286 -0.0277 521 CYS A N 4058 C CA . CYS A 521 ? 0.5035 0.5546 0.5179 -0.0751 -0.0238 -0.0246 521 CYS A CA 4059 C C . CYS A 521 ? 0.4749 0.5563 0.5102 -0.0840 -0.0227 -0.0272 521 CYS A C 4060 O O . CYS A 521 ? 0.4465 0.5500 0.4932 -0.0769 -0.0211 -0.0280 521 CYS A O 4061 C CB . CYS A 521 ? 0.5072 0.5468 0.5121 -0.0724 -0.0159 -0.0167 521 CYS A CB 4062 S SG . CYS A 521 ? 0.5238 0.5395 0.5105 -0.0573 -0.0165 -0.0143 521 CYS A SG 4063 N N . VAL A 522 ? 0.4808 0.5640 0.5218 -0.0995 -0.0233 -0.0291 522 VAL A N 4064 C CA . VAL A 522 ? 0.4841 0.6010 0.5484 -0.1080 -0.0233 -0.0334 522 VAL A CA 4065 C C . VAL A 522 ? 0.4787 0.6129 0.5538 -0.0991 -0.0334 -0.0409 522 VAL A C 4066 O O . VAL A 522 ? 0.4701 0.6348 0.5645 -0.0952 -0.0340 -0.0442 522 VAL A O 4067 C CB . VAL A 522 ? 0.5005 0.6166 0.5697 -0.1286 -0.0227 -0.0347 522 VAL A CB 4068 C CG1 . VAL A 522 ? 0.4820 0.6374 0.5784 -0.1362 -0.0250 -0.0415 522 VAL A CG1 4069 C CG2 . VAL A 522 ? 0.5201 0.6220 0.5797 -0.1389 -0.0122 -0.0261 522 VAL A CG2 4070 N N . PHE A 523 ? 0.4737 0.5879 0.5354 -0.0955 -0.0415 -0.0435 523 PHE A N 4071 C CA . PHE A 523 ? 0.4634 0.5891 0.5298 -0.0866 -0.0520 -0.0492 523 PHE A CA 4072 C C . PHE A 523 ? 0.4521 0.5849 0.5190 -0.0697 -0.0513 -0.0469 523 PHE A C 4073 O O . PHE A 523 ? 0.4618 0.6171 0.5428 -0.0630 -0.0568 -0.0503 523 PHE A O 4074 C CB . PHE A 523 ? 0.4632 0.5629 0.5103 -0.0866 -0.0595 -0.0522 523 PHE A CB 4075 C CG . PHE A 523 ? 0.4364 0.5424 0.4815 -0.0759 -0.0698 -0.0561 523 PHE A CG 4076 C CD1 . PHE A 523 ? 0.4417 0.5704 0.5015 -0.0796 -0.0799 -0.0622 523 PHE A CD1 4077 C CD2 . PHE A 523 ? 0.4333 0.5232 0.4615 -0.0626 -0.0695 -0.0532 523 PHE A CD2 4078 C CE1 . PHE A 523 ? 0.4424 0.5754 0.4981 -0.0692 -0.0904 -0.0647 523 PHE A CE1 4079 C CE2 . PHE A 523 ? 0.4394 0.5330 0.4629 -0.0535 -0.0788 -0.0555 523 PHE A CE2 4080 C CZ . PHE A 523 ? 0.4453 0.5593 0.4815 -0.0564 -0.0896 -0.0609 523 PHE A CZ 4081 N N . TRP A 524 ? 0.4549 0.5682 0.5064 -0.0625 -0.0450 -0.0414 524 TRP A N 4082 C CA . TRP A 524 ? 0.4570 0.5727 0.5062 -0.0478 -0.0448 -0.0395 524 TRP A CA 4083 C C . TRP A 524 ? 0.4382 0.5761 0.5031 -0.0448 -0.0387 -0.0386 524 TRP A C 4084 O O . TRP A 524 ? 0.4225 0.5724 0.4945 -0.0344 -0.0417 -0.0403 524 TRP A O 4085 C CB . TRP A 524 ? 0.4618 0.5513 0.4905 -0.0416 -0.0407 -0.0349 524 TRP A CB 4086 C CG . TRP A 524 ? 0.4715 0.5418 0.4844 -0.0403 -0.0467 -0.0372 524 TRP A CG 4087 C CD1 . TRP A 524 ? 0.4879 0.5364 0.4876 -0.0459 -0.0458 -0.0377 524 TRP A CD1 4088 C CD2 . TRP A 524 ? 0.4703 0.5402 0.4772 -0.0326 -0.0545 -0.0397 524 TRP A CD2 4089 N NE1 . TRP A 524 ? 0.5030 0.5392 0.4892 -0.0421 -0.0518 -0.0413 524 TRP A NE1 4090 C CE2 . TRP A 524 ? 0.4941 0.5433 0.4836 -0.0345 -0.0571 -0.0420 524 TRP A CE2 4091 C CE3 . TRP A 524 ? 0.4632 0.5465 0.4763 -0.0241 -0.0595 -0.0400 524 TRP A CE3 4092 C CZ2 . TRP A 524 ? 0.5013 0.5445 0.4785 -0.0290 -0.0639 -0.0444 524 TRP A CZ2 4093 C CZ3 . TRP A 524 ? 0.4765 0.5517 0.4769 -0.0186 -0.0670 -0.0412 524 TRP A CZ3 4094 C CH2 . TRP A 524 ? 0.4885 0.5448 0.4707 -0.0216 -0.0689 -0.0433 524 TRP A CH2 4095 N N . ASN A 525 ? 0.4473 0.5890 0.5159 -0.0540 -0.0301 -0.0360 525 ASN A N 4096 C CA . ASN A 525 ? 0.4532 0.6151 0.5337 -0.0525 -0.0225 -0.0355 525 ASN A CA 4097 C C . ASN A 525 ? 0.4481 0.6433 0.5533 -0.0577 -0.0230 -0.0414 525 ASN A C 4098 O O . ASN A 525 ? 0.4333 0.6489 0.5513 -0.0501 -0.0207 -0.0442 525 ASN A O 4099 C CB . ASN A 525 ? 0.4689 0.6190 0.5387 -0.0595 -0.0126 -0.0290 525 ASN A CB 4100 C CG . ASN A 525 ? 0.4833 0.6062 0.5324 -0.0518 -0.0119 -0.0238 525 ASN A CG 4101 O OD1 . ASN A 525 ? 0.4915 0.6106 0.5367 -0.0403 -0.0153 -0.0247 525 ASN A OD1 4102 N ND2 . ASN A 525 ? 0.4954 0.5996 0.5316 -0.0584 -0.0075 -0.0181 525 ASN A ND2 4103 N N . GLN A 526 ? 0.4569 0.6583 0.5697 -0.0705 -0.0260 -0.0439 526 GLN A N 4104 C CA . GLN A 526 ? 0.4519 0.6887 0.5907 -0.0769 -0.0259 -0.0500 526 GLN A CA 4105 C C . GLN A 526 ? 0.4472 0.6973 0.5982 -0.0730 -0.0392 -0.0567 526 GLN A C 4106 O O . GLN A 526 ? 0.4676 0.7418 0.6357 -0.0626 -0.0432 -0.0614 526 GLN A O 4107 C CB . GLN A 526 ? 0.4689 0.7098 0.6112 -0.0970 -0.0183 -0.0482 526 GLN A CB 4108 C CG . GLN A 526 ? 0.4780 0.7080 0.6078 -0.1010 -0.0055 -0.0407 526 GLN A CG 4109 N N . PHE A 527 ? 0.4408 0.6744 0.5820 -0.0804 -0.0467 -0.0573 527 PHE A N 4110 C CA . PHE A 527 ? 0.4332 0.6838 0.5875 -0.0806 -0.0596 -0.0642 527 PHE A CA 4111 C C . PHE A 527 ? 0.4273 0.6768 0.5782 -0.0619 -0.0696 -0.0653 527 PHE A C 4112 O O . PHE A 527 ? 0.4352 0.7121 0.6062 -0.0542 -0.0756 -0.0700 527 PHE A O 4113 C CB . PHE A 527 ? 0.4418 0.6737 0.5844 -0.0942 -0.0654 -0.0657 527 PHE A CB 4114 C CG . PHE A 527 ? 0.4348 0.6836 0.5886 -0.0951 -0.0799 -0.0731 527 PHE A CG 4115 C CD1 . PHE A 527 ? 0.4352 0.7201 0.6169 -0.1051 -0.0825 -0.0793 527 PHE A CD1 4116 C CD2 . PHE A 527 ? 0.4376 0.6676 0.5736 -0.0863 -0.0911 -0.0740 527 PHE A CD2 4117 C CE1 . PHE A 527 ? 0.4433 0.7458 0.6361 -0.1057 -0.0973 -0.0864 527 PHE A CE1 4118 C CE2 . PHE A 527 ? 0.4499 0.6952 0.5939 -0.0870 -0.1056 -0.0806 527 PHE A CE2 4119 C CZ . PHE A 527 ? 0.4476 0.7295 0.6206 -0.0963 -0.1094 -0.0869 527 PHE A CZ 4120 N N . LEU A 528 ? 0.4354 0.6533 0.5611 -0.0545 -0.0712 -0.0609 528 LEU A N 4121 C CA . LEU A 528 ? 0.4497 0.6617 0.5677 -0.0392 -0.0810 -0.0609 528 LEU A CA 4122 C C . LEU A 528 ? 0.4668 0.6964 0.5987 -0.0249 -0.0804 -0.0612 528 LEU A C 4123 O O . LEU A 528 ? 0.4984 0.7402 0.6385 -0.0151 -0.0914 -0.0640 528 LEU A O 4124 C CB . LEU A 528 ? 0.4406 0.6171 0.5292 -0.0349 -0.0794 -0.0557 528 LEU A CB 4125 C CG . LEU A 528 ? 0.4366 0.6048 0.5142 -0.0209 -0.0883 -0.0544 528 LEU A CG 4126 C CD1 . LEU A 528 ? 0.4500 0.6262 0.5292 -0.0222 -0.1027 -0.0591 528 LEU A CD1 4127 C CD2 . LEU A 528 ? 0.4360 0.5733 0.4870 -0.0171 -0.0840 -0.0493 528 LEU A CD2 4128 N N . PRO A 529 ? 0.4666 0.6961 0.5998 -0.0229 -0.0684 -0.0584 529 PRO A N 4129 C CA . PRO A 529 ? 0.4728 0.7178 0.6190 -0.0098 -0.0672 -0.0602 529 PRO A CA 4130 C C . PRO A 529 ? 0.4910 0.7724 0.6662 -0.0083 -0.0723 -0.0675 529 PRO A C 4131 O O . PRO A 529 ? 0.5250 0.8153 0.7086 0.0056 -0.0812 -0.0701 529 PRO A O 4132 C CB . PRO A 529 ? 0.4694 0.7121 0.6132 -0.0134 -0.0526 -0.0575 529 PRO A CB 4133 C CG . PRO A 529 ? 0.4754 0.6878 0.5952 -0.0205 -0.0492 -0.0514 529 PRO A CG 4134 C CD . PRO A 529 ? 0.4810 0.6918 0.6001 -0.0306 -0.0565 -0.0533 529 PRO A CD 4135 N N . LYS A 530 ? 0.4941 0.7960 0.6846 -0.0228 -0.0668 -0.0705 530 LYS A N 4136 C CA . LYS A 530 ? 0.4792 0.8206 0.7002 -0.0245 -0.0710 -0.0783 530 LYS A CA 4137 C C . LYS A 530 ? 0.4805 0.8283 0.7065 -0.0200 -0.0884 -0.0817 530 LYS A C 4138 O O . LYS A 530 ? 0.5026 0.8813 0.7531 -0.0121 -0.0957 -0.0879 530 LYS A O 4139 C CB . LYS A 530 ? 0.4950 0.8522 0.7269 -0.0451 -0.0617 -0.0797 530 LYS A CB 4140 C CG . LYS A 530 ? 0.5092 0.9114 0.7752 -0.0500 -0.0646 -0.0883 530 LYS A CG 4141 C CD . LYS A 530 ? 0.5234 0.9404 0.7987 -0.0714 -0.0518 -0.0885 530 LYS A CD 4142 C CE . LYS A 530 ? 0.5319 0.9993 0.8444 -0.0761 -0.0520 -0.0977 530 LYS A CE 4143 N NZ . LYS A 530 ? 0.5489 1.0301 0.8691 -0.0995 -0.0386 -0.0972 530 LYS A NZ 4144 N N . LEU A 531 ? 0.4758 0.7958 0.6787 -0.0247 -0.0952 -0.0782 531 LEU A N 4145 C CA . LEU A 531 ? 0.4970 0.8192 0.6988 -0.0202 -0.1124 -0.0808 531 LEU A CA 4146 C C . LEU A 531 ? 0.4923 0.8093 0.6901 0.0007 -0.1209 -0.0789 531 LEU A C 4147 O O . LEU A 531 ? 0.4889 0.8271 0.7025 0.0098 -0.1337 -0.0831 531 LEU A O 4148 C CB . LEU A 531 ? 0.5275 0.8176 0.7011 -0.0293 -0.1161 -0.0777 531 LEU A CB 4149 C CG . LEU A 531 ? 0.5449 0.8376 0.7148 -0.0284 -0.1339 -0.0812 531 LEU A CG 4150 C CD1 . LEU A 531 ? 0.5534 0.8251 0.7046 -0.0443 -0.1347 -0.0821 531 LEU A CD1 4151 C CD2 . LEU A 531 ? 0.5597 0.8357 0.7121 -0.0105 -0.1438 -0.0770 531 LEU A CD2 4152 N N . LEU A 532 ? 0.5049 0.7928 0.6811 0.0082 -0.1143 -0.0725 532 LEU A N 4153 C CA . LEU A 532 ? 0.5421 0.8180 0.7100 0.0266 -0.1215 -0.0696 532 LEU A CA 4154 C C . LEU A 532 ? 0.5759 0.8776 0.7696 0.0394 -0.1208 -0.0742 532 LEU A C 4155 O O . LEU A 532 ? 0.6057 0.9075 0.8015 0.0552 -0.1319 -0.0742 532 LEU A O 4156 C CB . LEU A 532 ? 0.5293 0.7692 0.6691 0.0290 -0.1135 -0.0621 532 LEU A CB 4157 C CG . LEU A 532 ? 0.5339 0.7463 0.6463 0.0200 -0.1143 -0.0579 532 LEU A CG 4158 C CD1 . LEU A 532 ? 0.5286 0.7152 0.6218 0.0192 -0.1020 -0.0521 532 LEU A CD1 4159 C CD2 . LEU A 532 ? 0.5408 0.7414 0.6375 0.0268 -0.1294 -0.0559 532 LEU A CD2 4160 N N . ASN A 533 ? 0.6081 0.9307 0.8201 0.0331 -0.1079 -0.0782 533 ASN A N 4161 C CA . ASN A 533 ? 0.6383 0.9900 0.8772 0.0446 -0.1056 -0.0847 533 ASN A CA 4162 C C . ASN A 533 ? 0.6571 1.0456 0.9248 0.0486 -0.1178 -0.0921 533 ASN A C 4163 O O . ASN A 533 ? 0.6869 1.0898 0.9703 0.0660 -0.1248 -0.0962 533 ASN A O 4164 C CB . ASN A 533 ? 0.6420 1.0084 0.8914 0.0350 -0.0876 -0.0872 533 ASN A CB 4165 C CG . ASN A 533 ? 0.6688 1.0512 0.9344 0.0496 -0.0821 -0.0928 533 ASN A CG 4166 O OD1 . ASN A 533 ? 0.6638 1.0839 0.9581 0.0500 -0.0784 -0.1009 533 ASN A OD1 4167 N ND2 . ASN A 533 ? 0.6979 1.0521 0.9452 0.0614 -0.0814 -0.0891 533 ASN A ND2 4168 N N . ALA A 534 ? 0.6749 1.0784 0.9500 0.0329 -0.1211 -0.0943 534 ALA A N 4169 C CA . ALA A 534 ? 0.6969 1.1385 1.0007 0.0344 -0.1336 -0.1019 534 ALA A CA 4170 C C . ALA A 534 ? 0.7419 1.1725 1.0359 0.0485 -0.1541 -0.0999 534 ALA A C 4171 O O . ALA A 534 ? 0.7207 1.1821 1.0386 0.0566 -0.1672 -0.1058 534 ALA A O 4172 C CB . ALA A 534 ? 0.7111 1.1688 1.0232 0.0113 -0.1313 -0.1048 534 ALA A CB 4173 N N . THR A 535 ? 0.8251 1.2129 1.0837 0.0510 -0.1569 -0.0913 535 THR A N 4174 C CA . THR A 535 ? 0.8732 1.2433 1.1159 0.0661 -0.1743 -0.0871 535 THR A CA 4175 C C . THR A 535 ? 0.9252 1.2655 1.1505 0.0817 -0.1701 -0.0810 535 THR A C 4176 O O . THR A 535 ? 0.9794 1.3201 1.2095 0.1003 -0.1806 -0.0807 535 THR A O 4177 C CB . THR A 535 ? 0.8646 1.2075 1.0767 0.0556 -0.1815 -0.0821 535 THR A CB 4178 O OG1 . THR A 535 ? 0.8057 1.1622 1.0251 0.0349 -0.1767 -0.0866 535 THR A OG1 4179 C CG2 . THR A 535 ? 0.8829 1.2261 1.0891 0.0674 -0.2033 -0.0810 535 THR A CG2 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ASP 1 1 ? ? ? A . n A 1 2 ASP 2 2 ? ? ? A . n A 1 3 HIS 3 3 ? ? ? A . n A 1 4 SER 4 4 4 SER SER A . n A 1 5 GLU 5 5 5 GLU GLU A . n A 1 6 LEU 6 6 6 LEU LEU A . n A 1 7 LEU 7 7 7 LEU LEU A . n A 1 8 VAL 8 8 8 VAL VAL A . n A 1 9 ASN 9 9 9 ASN ASN A . n A 1 10 THR 10 10 10 THR THR A . n A 1 11 LYS 11 11 11 LYS LYS A . n A 1 12 SER 12 12 12 SER SER A . n A 1 13 GLY 13 13 13 GLY GLY A . n A 1 14 LYS 14 14 14 LYS LYS A . n A 1 15 VAL 15 15 15 VAL VAL A . n A 1 16 MET 16 16 16 MET MET A . n A 1 17 GLY 17 17 17 GLY GLY A . n A 1 18 THR 18 18 18 THR THR A . n A 1 19 ARG 19 19 19 ARG ARG A . n A 1 20 VAL 20 20 20 VAL VAL A . n A 1 21 PRO 21 21 21 PRO PRO A . n A 1 22 VAL 22 22 22 VAL VAL A . n A 1 23 LEU 23 23 23 LEU LEU A . n A 1 24 SER 24 24 24 SER SER A . n A 1 25 SER 25 25 25 SER SER A . n A 1 26 HIS 26 26 26 HIS HIS A . n A 1 27 ILE 27 27 27 ILE ILE A . n A 1 28 SER 28 28 28 SER SER A . n A 1 29 ALA 29 29 29 ALA ALA A . n A 1 30 PHE 30 30 30 PHE PHE A . n A 1 31 LEU 31 31 31 LEU LEU A . n A 1 32 GLY 32 32 32 GLY GLY A . n A 1 33 ILE 33 33 33 ILE ILE A . n A 1 34 PRO 34 34 34 PRO PRO A . n A 1 35 PHE 35 35 35 PHE PHE A . n A 1 36 ALA 36 36 36 ALA ALA A . n A 1 37 GLU 37 37 37 GLU GLU A . n A 1 38 PRO 38 38 38 PRO PRO A . n A 1 39 PRO 39 39 39 PRO PRO A . n A 1 40 VAL 40 40 40 VAL VAL A . n A 1 41 GLY 41 41 41 GLY GLY A . n A 1 42 ASN 42 42 42 ASN ASN A . n A 1 43 MET 43 43 43 MET MET A . n A 1 44 ARG 44 44 44 ARG ARG A . n A 1 45 PHE 45 45 45 PHE PHE A . n A 1 46 ARG 46 46 46 ARG ARG A . n A 1 47 ARG 47 47 47 ARG ARG A . n A 1 48 PRO 48 48 48 PRO PRO A . n A 1 49 GLU 49 49 49 GLU GLU A . n A 1 50 PRO 50 50 50 PRO PRO A . n A 1 51 LYS 51 51 51 LYS LYS A . n A 1 52 LYS 52 52 52 LYS LYS A . n A 1 53 PRO 53 53 53 PRO PRO A . n A 1 54 TRP 54 54 54 TRP TRP 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 VAL 57 57 57 VAL VAL A . n A 1 58 TRP 58 58 58 TRP TRP A . n A 1 59 ASN 59 59 59 ASN ASN A . n A 1 60 ALA 60 60 60 ALA ALA A . n A 1 61 SER 61 61 61 SER SER A . n A 1 62 THR 62 62 62 THR THR A . n A 1 63 TYR 63 63 63 TYR TYR A . n A 1 64 PRO 64 64 64 PRO PRO A . n A 1 65 ASN 65 65 65 ASN ASN A . n A 1 66 ASN 66 66 66 ASN ASN A . n A 1 67 CYS 67 67 67 CYS CYS A . n A 1 68 GLN 68 68 68 GLN GLN A . n A 1 69 GLN 69 69 69 GLN GLN A . n A 1 70 TYR 70 70 70 TYR TYR A . n A 1 71 VAL 71 71 71 VAL VAL A . n A 1 72 ASP 72 72 72 ASP ASP A . n A 1 73 GLU 73 73 73 GLU GLU A . n A 1 74 GLN 74 74 74 GLN GLN A . n A 1 75 PHE 75 75 75 PHE PHE A . n A 1 76 PRO 76 76 76 PRO PRO A . n A 1 77 GLY 77 77 77 GLY GLY A . n A 1 78 PHE 78 78 78 PHE PHE A . n A 1 79 SER 79 79 79 SER SER A . n A 1 80 GLY 80 80 80 GLY GLY A . n A 1 81 SER 81 81 81 SER SER A . n A 1 82 GLU 82 82 82 GLU GLU A . n A 1 83 MET 83 83 83 MET MET A . n A 1 84 TRP 84 84 84 TRP TRP A . n A 1 85 ASN 85 85 85 ASN ASN A . n A 1 86 PRO 86 86 86 PRO PRO A . n A 1 87 ASN 87 87 87 ASN ASN A . n A 1 88 ARG 88 88 88 ARG ARG A . n A 1 89 GLU 89 89 89 GLU GLU A . n A 1 90 MET 90 90 90 MET MET A . n A 1 91 SER 91 91 91 SER SER A . n A 1 92 GLU 92 92 92 GLU GLU A . n A 1 93 ASP 93 93 93 ASP ASP A . n A 1 94 CYS 94 94 94 CYS CYS A . n A 1 95 LEU 95 95 95 LEU LEU A . n A 1 96 TYR 96 96 96 TYR TYR A . n A 1 97 LEU 97 97 97 LEU LEU A . n A 1 98 ASN 98 98 98 ASN ASN A . n A 1 99 ILE 99 99 99 ILE ILE A . n A 1 100 TRP 100 100 100 TRP TRP A . n A 1 101 VAL 101 101 101 VAL VAL A . n A 1 102 PRO 102 102 102 PRO PRO A . n A 1 103 SER 103 103 103 SER SER A . n A 1 104 PRO 104 104 104 PRO PRO A . n A 1 105 ARG 105 105 105 ARG ARG A . n A 1 106 PRO 106 106 106 PRO PRO A . n A 1 107 LYS 107 107 107 LYS LYS A . n A 1 108 SER 108 108 108 SER SER A . n A 1 109 THR 109 109 109 THR THR A . n A 1 110 THR 110 110 110 THR THR A . n A 1 111 VAL 111 111 111 VAL VAL A . n A 1 112 MET 112 112 112 MET MET A . n A 1 113 VAL 113 113 113 VAL VAL A . n A 1 114 TRP 114 114 114 TRP TRP A . n A 1 115 ILE 115 115 115 ILE ILE A . n A 1 116 TYR 116 116 116 TYR TYR A . n A 1 117 GLY 117 117 117 GLY GLY A . n A 1 118 GLY 118 118 118 GLY GLY A . n A 1 119 GLY 119 119 119 GLY GLY A . n A 1 120 PHE 120 120 120 PHE PHE A . n A 1 121 TYR 121 121 121 TYR TYR A . n A 1 122 SER 122 122 122 SER SER A . n A 1 123 GLY 123 123 123 GLY GLY A . n A 1 124 SER 124 124 124 SER SER A . n A 1 125 SER 125 125 125 SER SER A . n A 1 126 THR 126 126 126 THR THR A . n A 1 127 LEU 127 127 127 LEU LEU A . n A 1 128 ASP 128 128 128 ASP ASP A . n A 1 129 VAL 129 129 129 VAL VAL A . n A 1 130 TYR 130 130 130 TYR TYR A . n A 1 131 ASN 131 131 131 ASN ASN A . n A 1 132 GLY 132 132 132 GLY GLY A . n A 1 133 LYS 133 133 133 LYS LYS A . n A 1 134 TYR 134 134 134 TYR TYR A . n A 1 135 LEU 135 135 135 LEU LEU A . n A 1 136 ALA 136 136 136 ALA ALA A . n A 1 137 TYR 137 137 137 TYR TYR A . n A 1 138 THR 138 138 138 THR THR A . n A 1 139 GLU 139 139 139 GLU GLU A . n A 1 140 GLU 140 140 140 GLU GLU A . n A 1 141 VAL 141 141 141 VAL VAL A . n A 1 142 VAL 142 142 142 VAL VAL A . n A 1 143 LEU 143 143 143 LEU LEU A . n A 1 144 VAL 144 144 144 VAL VAL A . n A 1 145 SER 145 145 145 SER SER A . n A 1 146 LEU 146 146 146 LEU LEU A . n A 1 147 SER 147 147 147 SER SER A . n A 1 148 TYR 148 148 148 TYR TYR A . n A 1 149 ARG 149 149 149 ARG ARG A . n A 1 150 VAL 150 150 150 VAL VAL A . n A 1 151 GLY 151 151 151 GLY GLY A . n A 1 152 ALA 152 152 152 ALA ALA A . n A 1 153 PHE 153 153 153 PHE PHE A . n A 1 154 GLY 154 154 154 GLY GLY A . n A 1 155 PHE 155 155 155 PHE PHE A . n A 1 156 LEU 156 156 156 LEU LEU A . n A 1 157 ALA 157 157 157 ALA ALA A . n A 1 158 LEU 158 158 158 LEU LEU A . n A 1 159 HIS 159 159 159 HIS HIS A . n A 1 160 GLY 160 160 160 GLY GLY A . n A 1 161 SER 161 161 161 SER SER A . n A 1 162 GLN 162 162 162 GLN GLN A . n A 1 163 GLU 163 163 163 GLU GLU A . n A 1 164 ALA 164 164 164 ALA ALA A . n A 1 165 PRO 165 165 165 PRO PRO A . n A 1 166 GLY 166 166 166 GLY GLY A . n A 1 167 ASN 167 167 167 ASN ASN A . n A 1 168 VAL 168 168 168 VAL VAL A . n A 1 169 GLY 169 169 169 GLY GLY A . n A 1 170 LEU 170 170 170 LEU LEU A . n A 1 171 LEU 171 171 171 LEU LEU A . n A 1 172 ASP 172 172 172 ASP ASP A . n A 1 173 GLN 173 173 173 GLN GLN A . n A 1 174 ARG 174 174 174 ARG ARG A . n A 1 175 MET 175 175 175 MET MET A . n A 1 176 ALA 176 176 176 ALA ALA A . n A 1 177 LEU 177 177 177 LEU LEU A . n A 1 178 GLN 178 178 178 GLN GLN A . n A 1 179 TRP 179 179 179 TRP TRP A . n A 1 180 VAL 180 180 180 VAL VAL A . n A 1 181 HIS 181 181 181 HIS HIS A . n A 1 182 ASP 182 182 182 ASP ASP A . n A 1 183 ASN 183 183 183 ASN ASN A . n A 1 184 ILE 184 184 184 ILE ILE A . n A 1 185 GLN 185 185 185 GLN GLN A . n A 1 186 PHE 186 186 186 PHE PHE A . n A 1 187 PHE 187 187 187 PHE PHE A . n A 1 188 GLY 188 188 188 GLY GLY A . n A 1 189 GLY 189 189 189 GLY GLY A . n A 1 190 ASP 190 190 190 ASP ASP A . n A 1 191 PRO 191 191 191 PRO PRO A . n A 1 192 LYS 192 192 192 LYS LYS A . n A 1 193 THR 193 193 193 THR THR A . n A 1 194 VAL 194 194 194 VAL VAL A . n A 1 195 THR 195 195 195 THR THR A . n A 1 196 ILE 196 196 196 ILE ILE A . n A 1 197 PHE 197 197 197 PHE PHE A . n A 1 198 GLY 198 198 198 GLY GLY A . n A 1 199 GLU 199 199 199 GLU GLU A . n A 1 200 SER 200 200 200 SER SER A . n A 1 201 ALA 201 201 201 ALA ALA A . n A 1 202 GLY 202 202 202 GLY GLY A . n A 1 203 GLY 203 203 203 GLY GLY A . n A 1 204 ALA 204 204 204 ALA ALA A . n A 1 205 SER 205 205 205 SER SER A . n A 1 206 VAL 206 206 206 VAL VAL A . n A 1 207 GLY 207 207 207 GLY GLY A . n A 1 208 MET 208 208 208 MET MET A . n A 1 209 HIS 209 209 209 HIS HIS A . n A 1 210 ILE 210 210 210 ILE ILE A . n A 1 211 LEU 211 211 211 LEU LEU A . n A 1 212 SER 212 212 212 SER SER A . n A 1 213 PRO 213 213 213 PRO PRO A . n A 1 214 GLY 214 214 214 GLY GLY A . n A 1 215 SER 215 215 215 SER SER A . n A 1 216 ARG 216 216 216 ARG ARG A . n A 1 217 ASP 217 217 217 ASP ASP A . n A 1 218 LEU 218 218 218 LEU LEU A . n A 1 219 PHE 219 219 219 PHE PHE A . n A 1 220 ARG 220 220 220 ARG ARG A . n A 1 221 ARG 221 221 221 ARG ARG A . n A 1 222 ALA 222 222 222 ALA ALA A . n A 1 223 ILE 223 223 223 ILE ILE A . n A 1 224 LEU 224 224 224 LEU LEU A . n A 1 225 GLN 225 225 225 GLN GLN A . n A 1 226 SER 226 226 226 SER SER A . n A 1 227 GLY 227 227 227 GLY GLY A . n A 1 228 SER 228 228 228 SER SER A . n A 1 229 PRO 229 229 229 PRO PRO A . n A 1 230 ASN 230 230 230 ASN ASN A . n A 1 231 CYS 231 231 231 CYS CYS A . n A 1 232 PRO 232 232 232 PRO PRO A . n A 1 233 TRP 233 233 233 TRP TRP A . n A 1 234 ALA 234 234 234 ALA ALA A . n A 1 235 SER 235 235 235 SER SER A . n A 1 236 VAL 236 236 236 VAL VAL A . n A 1 237 SER 237 237 237 SER SER A . n A 1 238 VAL 238 238 238 VAL VAL A . n A 1 239 ALA 239 239 239 ALA ALA A . n A 1 240 GLU 240 240 240 GLU GLU A . n A 1 241 GLY 241 241 241 GLY GLY A . n A 1 242 ARG 242 242 242 ARG ARG A . n A 1 243 ARG 243 243 243 ARG ARG A . n A 1 244 ARG 244 244 244 ARG ARG A . n A 1 245 ALA 245 245 245 ALA ALA A . n A 1 246 VAL 246 246 246 VAL VAL A . n A 1 247 GLU 247 247 247 GLU GLU A . n A 1 248 LEU 248 248 248 LEU LEU A . n A 1 249 GLY 249 249 249 GLY GLY A . n A 1 250 ARG 250 250 250 ARG ARG A . n A 1 251 ASN 251 251 251 ASN ASN A . n A 1 252 LEU 252 252 252 LEU LEU A . n A 1 253 ASN 253 253 253 ASN ASN A . n A 1 254 CYS 254 254 254 CYS CYS A . n A 1 255 ASN 255 255 255 ASN ASN A . n A 1 256 LEU 256 256 256 LEU LEU A . n A 1 257 ASN 257 257 257 ASN ASN A . n A 1 258 SER 258 258 258 SER SER A . n A 1 259 ASP 259 259 259 ASP ASP A . n A 1 260 GLU 260 260 260 GLU GLU A . n A 1 261 GLU 261 261 261 GLU GLU A . n A 1 262 LEU 262 262 262 LEU LEU A . n A 1 263 ILE 263 263 263 ILE ILE A . n A 1 264 HIS 264 264 264 HIS HIS A . n A 1 265 CYS 265 265 265 CYS CYS A . n A 1 266 LEU 266 266 266 LEU LEU A . n A 1 267 ARG 267 267 267 ARG ARG A . n A 1 268 GLU 268 268 268 GLU GLU A . n A 1 269 LYS 269 269 269 LYS LYS A . n A 1 270 LYS 270 270 270 LYS LYS A . n A 1 271 PRO 271 271 271 PRO PRO A . n A 1 272 GLN 272 272 272 GLN GLN A . n A 1 273 GLU 273 273 273 GLU GLU A . n A 1 274 LEU 274 274 274 LEU LEU A . n A 1 275 ILE 275 275 275 ILE ILE A . n A 1 276 ASP 276 276 276 ASP ASP A . n A 1 277 VAL 277 277 277 VAL VAL A . n A 1 278 GLU 278 278 278 GLU GLU A . n A 1 279 TRP 279 279 279 TRP TRP A . n A 1 280 ASN 280 280 280 ASN ASN A . n A 1 281 VAL 281 281 281 VAL VAL A . n A 1 282 LEU 282 282 282 LEU LEU A . n A 1 283 PRO 283 283 283 PRO PRO A . n A 1 284 PHE 284 284 284 PHE PHE A . n A 1 285 ASP 285 285 285 ASP ASP A . n A 1 286 SER 286 286 286 SER SER A . n A 1 287 ILE 287 287 287 ILE ILE A . n A 1 288 PHE 288 288 288 PHE PHE A . n A 1 289 ARG 289 289 289 ARG ARG A . n A 1 290 PHE 290 290 290 PHE PHE A . n A 1 291 SER 291 291 291 SER SER A . n A 1 292 PHE 292 292 292 PHE PHE A . n A 1 293 VAL 293 293 293 VAL VAL A . n A 1 294 PRO 294 294 294 PRO PRO A . n A 1 295 VAL 295 295 295 VAL VAL A . n A 1 296 ILE 296 296 296 ILE ILE A . n A 1 297 ASP 297 297 297 ASP ASP A . n A 1 298 GLY 298 298 298 GLY GLY A . n A 1 299 GLU 299 299 299 GLU GLU A . n A 1 300 PHE 300 300 300 PHE PHE A . n A 1 301 PHE 301 301 301 PHE PHE A . n A 1 302 PRO 302 302 302 PRO PRO A . n A 1 303 THR 303 303 303 THR THR A . n A 1 304 SER 304 304 304 SER SER A . n A 1 305 LEU 305 305 305 LEU LEU A . n A 1 306 GLU 306 306 306 GLU GLU A . n A 1 307 SER 307 307 307 SER SER A . n A 1 308 MET 308 308 308 MET MET A . n A 1 309 LEU 309 309 309 LEU LEU A . n A 1 310 ASN 310 310 310 ASN ASN A . n A 1 311 SER 311 311 311 SER SER A . n A 1 312 GLY 312 312 312 GLY GLY A . n A 1 313 ASN 313 313 313 ASN ASN A . n A 1 314 PHE 314 314 314 PHE PHE A . n A 1 315 LYS 315 315 315 LYS LYS A . n A 1 316 LYS 316 316 316 LYS LYS A . n A 1 317 THR 317 317 317 THR THR A . n A 1 318 GLN 318 318 318 GLN GLN A . n A 1 319 ILE 319 319 319 ILE ILE A . n A 1 320 LEU 320 320 320 LEU LEU A . n A 1 321 LEU 321 321 321 LEU LEU A . n A 1 322 GLY 322 322 322 GLY GLY A . n A 1 323 VAL 323 323 323 VAL VAL A . n A 1 324 ASN 324 324 324 ASN ASN A . n A 1 325 LYS 325 325 325 LYS LYS A . n A 1 326 ASP 326 326 326 ASP ASP A . n A 1 327 GLU 327 327 327 GLU GLU A . n A 1 328 GLY 328 328 328 GLY GLY A . n A 1 329 SER 329 329 329 SER SER A . n A 1 330 PHE 330 330 330 PHE PHE A . n A 1 331 PHE 331 331 331 PHE PHE A . n A 1 332 LEU 332 332 332 LEU LEU A . n A 1 333 LEU 333 333 333 LEU LEU A . n A 1 334 TYR 334 334 334 TYR TYR A . n A 1 335 GLY 335 335 335 GLY GLY A . n A 1 336 ALA 336 336 336 ALA ALA A . n A 1 337 PRO 337 337 337 PRO PRO A . n A 1 338 GLY 338 338 338 GLY GLY A . n A 1 339 PHE 339 339 339 PHE PHE A . n A 1 340 SER 340 340 340 SER SER A . n A 1 341 LYS 341 341 341 LYS LYS A . n A 1 342 ASP 342 342 342 ASP ASP A . n A 1 343 SER 343 343 343 SER SER A . n A 1 344 GLU 344 344 344 GLU GLU A . n A 1 345 SER 345 345 345 SER SER A . n A 1 346 LYS 346 346 346 LYS LYS A . n A 1 347 ILE 347 347 347 ILE ILE A . n A 1 348 SER 348 348 348 SER SER A . n A 1 349 ARG 349 349 349 ARG ARG A . n A 1 350 GLU 350 350 350 GLU GLU A . n A 1 351 ASP 351 351 351 ASP ASP A . n A 1 352 PHE 352 352 352 PHE PHE A . n A 1 353 MET 353 353 353 MET MET A . n A 1 354 SER 354 354 354 SER SER A . n A 1 355 GLY 355 355 355 GLY GLY A . n A 1 356 VAL 356 356 356 VAL VAL A . n A 1 357 LYS 357 357 357 LYS LYS A . n A 1 358 LEU 358 358 358 LEU LEU A . n A 1 359 SER 359 359 359 SER SER A . n A 1 360 VAL 360 360 360 VAL VAL A . n A 1 361 PRO 361 361 361 PRO PRO A . n A 1 362 HIS 362 362 362 HIS HIS A . n A 1 363 ALA 363 363 363 ALA ALA A . n A 1 364 ASN 364 364 364 ASN ASN A . n A 1 365 ASP 365 365 365 ASP ASP A . n A 1 366 LEU 366 366 366 LEU LEU A . n A 1 367 GLY 367 367 367 GLY GLY A . n A 1 368 LEU 368 368 368 LEU LEU A . n A 1 369 ASP 369 369 369 ASP ASP A . n A 1 370 ALA 370 370 370 ALA ALA A . n A 1 371 VAL 371 371 371 VAL VAL A . n A 1 372 THR 372 372 372 THR THR A . n A 1 373 LEU 373 373 373 LEU LEU A . n A 1 374 GLN 374 374 374 GLN GLN A . n A 1 375 TYR 375 375 375 TYR TYR A . n A 1 376 THR 376 376 376 THR THR A . n A 1 377 ASP 377 377 377 ASP ASP A . n A 1 378 TRP 378 378 378 TRP TRP A . n A 1 379 MET 379 379 379 MET MET A . n A 1 380 ASP 380 380 380 ASP ASP A . n A 1 381 ASP 381 381 381 ASP ASP A . n A 1 382 ASN 382 382 382 ASN ASN A . n A 1 383 ASN 383 383 383 ASN ASN A . n A 1 384 GLY 384 384 384 GLY GLY A . n A 1 385 ILE 385 385 385 ILE ILE A . n A 1 386 LYS 386 386 386 LYS LYS A . n A 1 387 ASN 387 387 387 ASN ASN A . n A 1 388 ARG 388 388 388 ARG ARG A . n A 1 389 ASP 389 389 389 ASP ASP A . n A 1 390 GLY 390 390 390 GLY GLY A . n A 1 391 LEU 391 391 391 LEU LEU A . n A 1 392 ASP 392 392 392 ASP ASP A . n A 1 393 ASP 393 393 393 ASP ASP A . n A 1 394 ILE 394 394 394 ILE ILE A . n A 1 395 VAL 395 395 395 VAL VAL A . n A 1 396 GLY 396 396 396 GLY GLY A . n A 1 397 ASP 397 397 397 ASP ASP A . n A 1 398 HIS 398 398 398 HIS HIS A . n A 1 399 ASN 399 399 399 ASN ASN A . n A 1 400 VAL 400 400 400 VAL VAL A . n A 1 401 ILE 401 401 401 ILE ILE A . n A 1 402 CYS 402 402 402 CYS CYS A . n A 1 403 PRO 403 403 403 PRO PRO A . n A 1 404 LEU 404 404 404 LEU LEU A . n A 1 405 MET 405 405 405 MET MET A . n A 1 406 HIS 406 406 406 HIS HIS A . n A 1 407 PHE 407 407 407 PHE PHE A . n A 1 408 VAL 408 408 408 VAL VAL A . n A 1 409 ASN 409 409 409 ASN ASN A . n A 1 410 LYS 410 410 410 LYS LYS A . n A 1 411 TYR 411 411 411 TYR TYR A . n A 1 412 THR 412 412 412 THR THR A . n A 1 413 LYS 413 413 413 LYS LYS A . n A 1 414 PHE 414 414 414 PHE PHE A . n A 1 415 GLY 415 415 415 GLY GLY A . n A 1 416 ASN 416 416 416 ASN ASN A . n A 1 417 GLY 417 417 417 GLY GLY A . n A 1 418 THR 418 418 418 THR THR A . n A 1 419 TYR 419 419 419 TYR TYR A . n A 1 420 LEU 420 420 420 LEU LEU A . n A 1 421 TYR 421 421 421 TYR TYR A . n A 1 422 PHE 422 422 422 PHE PHE A . n A 1 423 PHE 423 423 423 PHE PHE A . n A 1 424 ASN 424 424 424 ASN ASN A . n A 1 425 HIS 425 425 425 HIS HIS A . n A 1 426 ARG 426 426 426 ARG ARG A . n A 1 427 ALA 427 427 427 ALA ALA A . n A 1 428 SER 428 428 428 SER SER A . n A 1 429 ASN 429 429 429 ASN ASN A . n A 1 430 LEU 430 430 430 LEU LEU A . n A 1 431 VAL 431 431 431 VAL VAL A . n A 1 432 TRP 432 432 432 TRP TRP A . n A 1 433 PRO 433 433 433 PRO PRO A . n A 1 434 GLU 434 434 434 GLU GLU A . n A 1 435 TRP 435 435 435 TRP TRP A . n A 1 436 MET 436 436 436 MET MET A . n A 1 437 GLY 437 437 437 GLY GLY A . n A 1 438 VAL 438 438 438 VAL VAL A . n A 1 439 ILE 439 439 439 ILE ILE A . n A 1 440 HIS 440 440 440 HIS HIS A . n A 1 441 GLY 441 441 441 GLY GLY A . n A 1 442 TYR 442 442 442 TYR TYR A . n A 1 443 GLU 443 443 443 GLU GLU A . n A 1 444 ILE 444 444 444 ILE ILE A . n A 1 445 GLU 445 445 445 GLU GLU A . n A 1 446 PHE 446 446 446 PHE PHE A . n A 1 447 VAL 447 447 447 VAL VAL A . n A 1 448 PHE 448 448 448 PHE PHE A . n A 1 449 GLY 449 449 449 GLY GLY A . n A 1 450 LEU 450 450 450 LEU LEU A . n A 1 451 PRO 451 451 451 PRO PRO A . n A 1 452 LEU 452 452 452 LEU LEU A . n A 1 453 VAL 453 453 453 VAL VAL A . n A 1 454 LYS 454 454 454 LYS LYS A . n A 1 455 GLU 455 455 455 GLU GLU A . n A 1 456 LEU 456 456 456 LEU LEU A . n A 1 457 ASN 457 457 457 ASN ASN A . n A 1 458 TYR 458 458 458 TYR TYR A . n A 1 459 THR 459 459 459 THR THR A . n A 1 460 ALA 460 460 460 ALA ALA A . n A 1 461 GLU 461 461 461 GLU GLU A . n A 1 462 GLU 462 462 462 GLU GLU A . n A 1 463 GLU 463 463 463 GLU GLU A . n A 1 464 ALA 464 464 464 ALA ALA A . n A 1 465 LEU 465 465 465 LEU LEU A . n A 1 466 SER 466 466 466 SER SER A . n A 1 467 ARG 467 467 467 ARG ARG A . n A 1 468 ARG 468 468 468 ARG ARG A . n A 1 469 ILE 469 469 469 ILE ILE A . n A 1 470 MET 470 470 470 MET MET A . n A 1 471 HIS 471 471 471 HIS HIS A . n A 1 472 TYR 472 472 472 TYR TYR A . n A 1 473 TRP 473 473 473 TRP TRP A . n A 1 474 ALA 474 474 474 ALA ALA A . n A 1 475 THR 475 475 475 THR THR A . n A 1 476 PHE 476 476 476 PHE PHE A . n A 1 477 ALA 477 477 477 ALA ALA A . n A 1 478 LYS 478 478 478 LYS LYS A . n A 1 479 THR 479 479 479 THR THR A . n A 1 480 GLY 480 480 480 GLY GLY A . n A 1 481 ASN 481 481 481 ASN ASN A . n A 1 482 PRO 482 482 482 PRO PRO A . n A 1 483 ASN 483 483 483 ASN ASN A . n A 1 484 GLU 484 484 484 GLU GLU A . n A 1 485 PRO 485 485 485 PRO PRO A . n A 1 486 HIS 486 486 486 HIS ALA A . n A 1 487 SER 487 487 487 SER ALA A . n A 1 488 GLN 488 488 488 GLN ALA A . n A 1 489 GLU 489 489 489 GLU ALA A . n A 1 490 SER 490 490 490 SER SER A . n A 1 491 LYS 491 491 491 LYS LYS A . n A 1 492 TRP 492 492 492 TRP TRP A . n A 1 493 PRO 493 493 493 PRO PRO A . n A 1 494 LEU 494 494 494 LEU LEU A . n A 1 495 PHE 495 495 495 PHE PHE A . n A 1 496 THR 496 496 496 THR THR A . n A 1 497 THR 497 497 497 THR THR A . n A 1 498 LYS 498 498 498 LYS LYS A . n A 1 499 GLU 499 499 499 GLU GLU A . n A 1 500 GLN 500 500 500 GLN GLN A . n A 1 501 LYS 501 501 501 LYS LYS A . n A 1 502 PHE 502 502 502 PHE PHE A . n A 1 503 ILE 503 503 503 ILE ILE A . n A 1 504 ASP 504 504 504 ASP ASP A . n A 1 505 LEU 505 505 505 LEU LEU A . n A 1 506 ASN 506 506 506 ASN ASN A . n A 1 507 THR 507 507 507 THR THR A . n A 1 508 GLU 508 508 508 GLU GLU A . n A 1 509 PRO 509 509 509 PRO PRO A . n A 1 510 MET 510 510 510 MET MET A . n A 1 511 LYS 511 511 511 LYS LYS A . n A 1 512 VAL 512 512 512 VAL VAL A . n A 1 513 HIS 513 513 513 HIS HIS A . n A 1 514 GLN 514 514 514 GLN GLN A . n A 1 515 ARG 515 515 515 ARG ARG A . n A 1 516 LEU 516 516 516 LEU LEU A . n A 1 517 ARG 517 517 517 ARG ARG A . n A 1 518 VAL 518 518 518 VAL VAL A . n A 1 519 GLN 519 519 519 GLN GLN A . n A 1 520 MET 520 520 520 MET MET A . n A 1 521 CYS 521 521 521 CYS CYS A . n A 1 522 VAL 522 522 522 VAL VAL A . n A 1 523 PHE 523 523 523 PHE PHE A . n A 1 524 TRP 524 524 524 TRP TRP A . n A 1 525 ASN 525 525 525 ASN ASN A . n A 1 526 GLN 526 526 526 GLN GLN A . n A 1 527 PHE 527 527 527 PHE PHE A . n A 1 528 LEU 528 528 528 LEU LEU A . n A 1 529 PRO 529 529 529 PRO PRO A . n A 1 530 LYS 530 530 530 LYS LYS A . n A 1 531 LEU 531 531 531 LEU LEU A . n A 1 532 LEU 532 532 532 LEU LEU A . n A 1 533 ASN 533 533 533 ASN ASN A . n A 1 534 ALA 534 534 534 ALA ALA A . n A 1 535 THR 535 535 535 THR THR A . n A 1 536 ALA 536 536 ? ? ? A . n A 1 537 CYS 537 537 ? ? ? A . n A 1 538 ASP 538 538 ? ? ? A . n A 1 539 GLY 539 539 ? ? ? A . n A 1 540 GLU 540 540 ? ? ? A . n A 1 541 LEU 541 541 ? ? ? A . n A 1 542 SER 542 542 ? ? ? A . n A 1 543 SER 543 543 ? ? ? A . n # 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 MBT 1 601 1540 MBT MBT A . C 3 NAG 1 602 1536 NAG NAG A . D 4 FUC 2 603 2106 FUC FUC A . E 3 NAG 1 604 1537 NAG NAG A . F 3 NAG 1 605 1539 NAG NAG A . G 3 NAG 2 606 2107 NAG NAG A . H 5 BMA 3 607 2108 BMA BMA A . I 6 MAN 4 608 2109 MAN MAN A . J 6 MAN 5 609 2110 MAN MAN A . K 7 SO4 1 610 701 SO4 SO4 A . L 7 SO4 1 611 702 SO4 SO4 A . M 7 SO4 1 612 703 SO4 SO4 A . N 7 SO4 1 613 704 SO4 SO4 A . O 7 SO4 1 614 705 SO4 SO4 A . P 7 SO4 1 615 706 SO4 SO4 A . Q 7 SO4 1 616 707 SO4 SO4 A . R 7 SO4 1 617 708 SO4 SO4 A . S 7 SO4 1 618 709 SO4 SO4 A . T 7 SO4 1 619 710 SO4 SO4 A . U 7 SO4 1 620 711 SO4 SO4 A . V 7 SO4 1 621 712 SO4 SO4 A . W 7 SO4 1 622 713 SO4 SO4 A . X 7 SO4 1 623 714 SO4 SO4 A . Y 7 SO4 1 624 715 SO4 SO4 A . Z 8 HOH 1 701 611 HOH HOH A . Z 8 HOH 2 702 603 HOH HOH A . Z 8 HOH 3 703 606 HOH HOH A . Z 8 HOH 4 704 614 HOH HOH A . Z 8 HOH 5 705 605 HOH HOH A . Z 8 HOH 6 706 607 HOH HOH A . Z 8 HOH 7 707 604 HOH HOH A . Z 8 HOH 8 708 608 HOH HOH A . Z 8 HOH 9 709 613 HOH HOH A . Z 8 HOH 10 710 609 HOH HOH A . Z 8 HOH 11 711 615 HOH HOH A . Z 8 HOH 12 712 602 HOH HOH A . Z 8 HOH 13 713 610 HOH HOH A . Z 8 HOH 14 714 612 HOH HOH A . Z 8 HOH 15 715 601 HOH HOH A . # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 4260 ? 1 MORE -150 ? 1 'SSA (A^2)' 21930 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2016-03-30 2 'Structure model' 1 1 2016-06-01 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls.id 1 _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x -53.8059 _pdbx_refine_tls.origin_y 36.5123 _pdbx_refine_tls.origin_z 10.6917 _pdbx_refine_tls.T[1][1] 0.0244 _pdbx_refine_tls.T[2][2] 0.1152 _pdbx_refine_tls.T[3][3] 0.0078 _pdbx_refine_tls.T[1][2] 0.0265 _pdbx_refine_tls.T[1][3] 0.0022 _pdbx_refine_tls.T[2][3] -0.0076 _pdbx_refine_tls.L[1][1] 1.3853 _pdbx_refine_tls.L[2][2] 1.4242 _pdbx_refine_tls.L[3][3] 2.0750 _pdbx_refine_tls.L[1][2] 0.1751 _pdbx_refine_tls.L[1][3] 0.1981 _pdbx_refine_tls.L[2][3] 0.3648 _pdbx_refine_tls.S[1][1] -0.0061 _pdbx_refine_tls.S[1][2] 0.0922 _pdbx_refine_tls.S[1][3] 0.0539 _pdbx_refine_tls.S[2][1] 0.0446 _pdbx_refine_tls.S[2][2] -0.0097 _pdbx_refine_tls.S[2][3] 0.0817 _pdbx_refine_tls.S[3][1] -0.0960 _pdbx_refine_tls.S[3][2] -0.2054 _pdbx_refine_tls.S[3][3] 0.0158 # _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.refine_tls_id 1 _pdbx_refine_tls_group.beg_auth_asym_id A _pdbx_refine_tls_group.beg_auth_seq_id 4 _pdbx_refine_tls_group.beg_label_asym_id ? _pdbx_refine_tls_group.beg_label_seq_id ? _pdbx_refine_tls_group.end_auth_asym_id A _pdbx_refine_tls_group.end_auth_seq_id 535 _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 ? # loop_ _software.citation_id _software.classification _software.compiler_name _software.compiler_version _software.contact_author _software.contact_author_email _software.date _software.description _software.dependencies _software.hardware _software.language _software.location _software.mods _software.name _software.os _software.os_version _software.type _software.version _software.pdbx_ordinal ? refinement ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0073 1 ? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM ? ? ? . 2 ? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? SCALA ? ? ? . 3 ? phasing ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? . 4 # 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 LEU A 23 ? ? 36.06 51.23 2 1 PHE A 45 ? ? 78.81 -17.71 3 1 PRO A 53 ? ? -49.88 156.30 4 1 SER A 108 ? ? -161.17 86.29 5 1 PHE A 120 ? ? 67.65 -0.37 6 1 LEU A 158 ? ? -105.11 79.72 7 1 SER A 200 ? ? 59.42 -124.14 8 1 GLU A 299 ? ? -109.85 -67.92 9 1 THR A 317 ? ? -160.10 -162.96 10 1 VAL A 400 ? ? -131.87 -62.59 11 1 SER A 487 ? ? -17.10 129.58 12 1 LEU A 516 ? ? -57.23 109.35 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A LYS 14 ? CG ? A LYS 14 CG 2 1 Y 1 A LYS 14 ? CD ? A LYS 14 CD 3 1 Y 1 A LYS 14 ? CE ? A LYS 14 CE 4 1 Y 1 A LYS 14 ? NZ ? A LYS 14 NZ 5 1 Y 1 A ARG 47 ? CG ? A ARG 47 CG 6 1 Y 1 A ARG 47 ? CD ? A ARG 47 CD 7 1 Y 1 A ARG 47 ? NE ? A ARG 47 NE 8 1 Y 1 A ARG 47 ? CZ ? A ARG 47 CZ 9 1 Y 1 A ARG 47 ? NH1 ? A ARG 47 NH1 10 1 Y 1 A ARG 47 ? NH2 ? A ARG 47 NH2 11 1 Y 1 A GLU 260 ? CG ? A GLU 260 CG 12 1 Y 1 A GLU 260 ? CD ? A GLU 260 CD 13 1 Y 1 A GLU 260 ? OE1 ? A GLU 260 OE1 14 1 Y 1 A GLU 260 ? OE2 ? A GLU 260 OE2 15 1 Y 1 A GLU 268 ? CG ? A GLU 268 CG 16 1 Y 1 A GLU 268 ? CD ? A GLU 268 CD 17 1 Y 1 A GLU 268 ? OE1 ? A GLU 268 OE1 18 1 Y 1 A GLU 268 ? OE2 ? A GLU 268 OE2 19 1 Y 1 A LYS 270 ? CG ? A LYS 270 CG 20 1 Y 1 A LYS 270 ? CD ? A LYS 270 CD 21 1 Y 1 A LYS 270 ? CE ? A LYS 270 CE 22 1 Y 1 A LYS 270 ? NZ ? A LYS 270 NZ 23 1 Y 1 A ARG 349 ? CG ? A ARG 349 CG 24 1 Y 1 A ARG 349 ? CD ? A ARG 349 CD 25 1 Y 1 A ARG 349 ? NE ? A ARG 349 NE 26 1 Y 1 A ARG 349 ? CZ ? A ARG 349 CZ 27 1 Y 1 A ARG 349 ? NH1 ? A ARG 349 NH1 28 1 Y 1 A ARG 349 ? NH2 ? A ARG 349 NH2 29 1 Y 1 A GLU 350 ? CG ? A GLU 350 CG 30 1 Y 1 A GLU 350 ? CD ? A GLU 350 CD 31 1 Y 1 A GLU 350 ? OE1 ? A GLU 350 OE1 32 1 Y 1 A GLU 350 ? OE2 ? A GLU 350 OE2 33 1 Y 1 A LYS 357 ? CE ? A LYS 357 CE 34 1 Y 1 A LYS 357 ? NZ ? A LYS 357 NZ 35 1 Y 1 A GLU 455 ? CD ? A GLU 455 CD 36 1 Y 1 A GLU 455 ? OE1 ? A GLU 455 OE1 37 1 Y 1 A GLU 455 ? OE2 ? A GLU 455 OE2 38 1 Y 1 A HIS 486 ? CG ? A HIS 486 CG 39 1 Y 1 A HIS 486 ? ND1 ? A HIS 486 ND1 40 1 Y 1 A HIS 486 ? CD2 ? A HIS 486 CD2 41 1 Y 1 A HIS 486 ? CE1 ? A HIS 486 CE1 42 1 Y 1 A HIS 486 ? NE2 ? A HIS 486 NE2 43 1 Y 1 A SER 487 ? OG ? A SER 487 OG 44 1 Y 1 A GLN 488 ? CG ? A GLN 488 CG 45 1 Y 1 A GLN 488 ? CD ? A GLN 488 CD 46 1 Y 1 A GLN 488 ? OE1 ? A GLN 488 OE1 47 1 Y 1 A GLN 488 ? NE2 ? A GLN 488 NE2 48 1 Y 1 A GLU 489 ? CG ? A GLU 489 CG 49 1 Y 1 A GLU 489 ? CD ? A GLU 489 CD 50 1 Y 1 A GLU 489 ? OE1 ? A GLU 489 OE1 51 1 Y 1 A GLU 489 ? OE2 ? A GLU 489 OE2 52 1 Y 1 A LYS 491 ? CD ? A LYS 491 CD 53 1 Y 1 A LYS 491 ? CE ? A LYS 491 CE 54 1 Y 1 A LYS 491 ? NZ ? A LYS 491 NZ 55 1 Y 1 A GLU 508 ? CG ? A GLU 508 CG 56 1 Y 1 A GLU 508 ? CD ? A GLU 508 CD 57 1 Y 1 A GLU 508 ? OE1 ? A GLU 508 OE1 58 1 Y 1 A GLU 508 ? OE2 ? A GLU 508 OE2 59 1 Y 1 A LYS 511 ? CG ? A LYS 511 CG 60 1 Y 1 A LYS 511 ? CD ? A LYS 511 CD 61 1 Y 1 A LYS 511 ? CE ? A LYS 511 CE 62 1 Y 1 A LYS 511 ? NZ ? A LYS 511 NZ 63 1 Y 1 A GLN 526 ? CD ? A GLN 526 CD 64 1 Y 1 A GLN 526 ? OE1 ? A GLN 526 OE1 65 1 Y 1 A GLN 526 ? NE2 ? A GLN 526 NE2 # 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 ASP 1 ? A ASP 1 2 1 Y 1 A ASP 2 ? A ASP 2 3 1 Y 1 A HIS 3 ? A HIS 3 4 1 Y 1 A ALA 536 ? A ALA 536 5 1 Y 1 A CYS 537 ? A CYS 537 6 1 Y 1 A ASP 538 ? A ASP 538 7 1 Y 1 A GLY 539 ? A GLY 539 8 1 Y 1 A GLU 540 ? A GLU 540 9 1 Y 1 A LEU 541 ? A LEU 541 10 1 Y 1 A SER 542 ? A SER 542 11 1 Y 1 A SER 543 ? A SER 543 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 '3,7-BIS(DIMETHYLAMINO)PHENOTHIAZIN-5-IUM' MBT 3 N-ACETYL-D-GLUCOSAMINE NAG 4 ALPHA-L-FUCOSE FUC 5 BETA-D-MANNOSE BMA 6 ALPHA-D-MANNOSE MAN 7 'SULFATE ION' SO4 8 water HOH #