data_4KKI # _entry.id 4KKI # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.287 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4KKI RCSB RCSB079452 WWPDB D_1000079452 # _pdbx_database_related.db_name PDB _pdbx_database_related.db_id 4KKJ _pdbx_database_related.details . _pdbx_database_related.content_type unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4KKI _pdbx_database_status.recvd_initial_deposition_date 2013-05-06 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Furger, E.' 1 'Frei, D.C.' 2 'Schibli, R.' 3 'Fischer, E.' 4 'Prota, A.E.' 5 # _citation.id primary _citation.title 'Structural basis for universal corrinoid recognition by the cobalamin transport protein haptocorrin.' _citation.journal_abbrev J.Biol.Chem. _citation.journal_volume 288 _citation.page_first 25466 _citation.page_last 25476 _citation.year 2013 _citation.journal_id_ASTM JBCHA3 _citation.country US _citation.journal_id_ISSN 0021-9258 _citation.journal_id_CSD 0071 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 23846701 _citation.pdbx_database_id_DOI 10.1074/jbc.M113.483271 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Furger, E.' 1 primary 'Frei, D.C.' 2 primary 'Schibli, R.' 3 primary 'Fischer, E.' 4 primary 'Prota, A.E.' 5 # _cell.entry_id 4KKI _cell.length_a 149.890 _cell.length_b 149.890 _cell.length_c 57.490 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 6 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 4KKI _symmetry.space_group_name_H-M 'P 64' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 172 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man Transcobalamin-1 52196.758 1 ? ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 7 ? ? ? ? 3 non-polymer syn CO-CYANOCOBALAMIN 1355.365 1 ? ? ? ? 4 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 5 non-polymer syn 'DI(HYDROXYETHYL)ETHER' 106.120 11 ? ? ? ? 6 water nat water 18.015 134 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'TC-1, Transcobalamin I, TC I, TCI' # _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 ;MRQSHQLPLVGLLLFSFIPSQLCEICEVSEENYIRLKPLLNTMIQSNYNRGTSAVNVVLSLKLVGIQIQTLMQKMIQQIK YNVKSRLSDVSSGELALIILALGVCRNAEENLIYDYHLIDKLENKFQAEIENMEAHNGTPLTNYYQLSLDVLALCLFNGN YSTAEVVNHFTPENKNYYFGSQFSVDTGAMAVLALTCVKKSLINGQIKADEGSLKNISIYTKSLVEKILSEKKENGLIGN TFSTGEAMQALFVSSDYYNENDWNCQQTLNTVLTEISQGAFSNPNAAAQVLPALMGKTFLDINKDSSCVSASGNFNISAD EPITVTPPDSQSYISVNYSVRINETYFTNVTVLNGSVFLSVMEKAQKMNDTIFGFTMEERSWGPYITCIQGLCANNNDRT YWELLSGGEPLSQGAGSYVVRNGENLEVRWSKYLVPRGSLESRGPFEQKLISEEDLNMHTGHHHHHH ; _entity_poly.pdbx_seq_one_letter_code_can ;MRQSHQLPLVGLLLFSFIPSQLCEICEVSEENYIRLKPLLNTMIQSNYNRGTSAVNVVLSLKLVGIQIQTLMQKMIQQIK YNVKSRLSDVSSGELALIILALGVCRNAEENLIYDYHLIDKLENKFQAEIENMEAHNGTPLTNYYQLSLDVLALCLFNGN YSTAEVVNHFTPENKNYYFGSQFSVDTGAMAVLALTCVKKSLINGQIKADEGSLKNISIYTKSLVEKILSEKKENGLIGN TFSTGEAMQALFVSSDYYNENDWNCQQTLNTVLTEISQGAFSNPNAAAQVLPALMGKTFLDINKDSSCVSASGNFNISAD EPITVTPPDSQSYISVNYSVRINETYFTNVTVLNGSVFLSVMEKAQKMNDTIFGFTMEERSWGPYITCIQGLCANNNDRT YWELLSGGEPLSQGAGSYVVRNGENLEVRWSKYLVPRGSLESRGPFEQKLISEEDLNMHTGHHHHHH ; _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 MET n 1 2 ARG n 1 3 GLN n 1 4 SER n 1 5 HIS n 1 6 GLN n 1 7 LEU n 1 8 PRO n 1 9 LEU n 1 10 VAL n 1 11 GLY n 1 12 LEU n 1 13 LEU n 1 14 LEU n 1 15 PHE n 1 16 SER n 1 17 PHE n 1 18 ILE n 1 19 PRO n 1 20 SER n 1 21 GLN n 1 22 LEU n 1 23 CYS n 1 24 GLU n 1 25 ILE n 1 26 CYS n 1 27 GLU n 1 28 VAL n 1 29 SER n 1 30 GLU n 1 31 GLU n 1 32 ASN n 1 33 TYR n 1 34 ILE n 1 35 ARG n 1 36 LEU n 1 37 LYS n 1 38 PRO n 1 39 LEU n 1 40 LEU n 1 41 ASN n 1 42 THR n 1 43 MET n 1 44 ILE n 1 45 GLN n 1 46 SER n 1 47 ASN n 1 48 TYR n 1 49 ASN n 1 50 ARG n 1 51 GLY n 1 52 THR n 1 53 SER n 1 54 ALA n 1 55 VAL n 1 56 ASN n 1 57 VAL n 1 58 VAL n 1 59 LEU n 1 60 SER n 1 61 LEU n 1 62 LYS n 1 63 LEU n 1 64 VAL n 1 65 GLY n 1 66 ILE n 1 67 GLN n 1 68 ILE n 1 69 GLN n 1 70 THR n 1 71 LEU n 1 72 MET n 1 73 GLN n 1 74 LYS n 1 75 MET n 1 76 ILE n 1 77 GLN n 1 78 GLN n 1 79 ILE n 1 80 LYS n 1 81 TYR n 1 82 ASN n 1 83 VAL n 1 84 LYS n 1 85 SER n 1 86 ARG n 1 87 LEU n 1 88 SER n 1 89 ASP n 1 90 VAL n 1 91 SER n 1 92 SER n 1 93 GLY n 1 94 GLU n 1 95 LEU n 1 96 ALA n 1 97 LEU n 1 98 ILE n 1 99 ILE n 1 100 LEU n 1 101 ALA n 1 102 LEU n 1 103 GLY n 1 104 VAL n 1 105 CYS n 1 106 ARG n 1 107 ASN n 1 108 ALA n 1 109 GLU n 1 110 GLU n 1 111 ASN n 1 112 LEU n 1 113 ILE n 1 114 TYR n 1 115 ASP n 1 116 TYR n 1 117 HIS n 1 118 LEU n 1 119 ILE n 1 120 ASP n 1 121 LYS n 1 122 LEU n 1 123 GLU n 1 124 ASN n 1 125 LYS n 1 126 PHE n 1 127 GLN n 1 128 ALA n 1 129 GLU n 1 130 ILE n 1 131 GLU n 1 132 ASN n 1 133 MET n 1 134 GLU n 1 135 ALA n 1 136 HIS n 1 137 ASN n 1 138 GLY n 1 139 THR n 1 140 PRO n 1 141 LEU n 1 142 THR n 1 143 ASN n 1 144 TYR n 1 145 TYR n 1 146 GLN n 1 147 LEU n 1 148 SER n 1 149 LEU n 1 150 ASP n 1 151 VAL n 1 152 LEU n 1 153 ALA n 1 154 LEU n 1 155 CYS n 1 156 LEU n 1 157 PHE n 1 158 ASN n 1 159 GLY n 1 160 ASN n 1 161 TYR n 1 162 SER n 1 163 THR n 1 164 ALA n 1 165 GLU n 1 166 VAL n 1 167 VAL n 1 168 ASN n 1 169 HIS n 1 170 PHE n 1 171 THR n 1 172 PRO n 1 173 GLU n 1 174 ASN n 1 175 LYS n 1 176 ASN n 1 177 TYR n 1 178 TYR n 1 179 PHE n 1 180 GLY n 1 181 SER n 1 182 GLN n 1 183 PHE n 1 184 SER n 1 185 VAL n 1 186 ASP n 1 187 THR n 1 188 GLY n 1 189 ALA n 1 190 MET n 1 191 ALA n 1 192 VAL n 1 193 LEU n 1 194 ALA n 1 195 LEU n 1 196 THR n 1 197 CYS n 1 198 VAL n 1 199 LYS n 1 200 LYS n 1 201 SER n 1 202 LEU n 1 203 ILE n 1 204 ASN n 1 205 GLY n 1 206 GLN n 1 207 ILE n 1 208 LYS n 1 209 ALA n 1 210 ASP n 1 211 GLU n 1 212 GLY n 1 213 SER n 1 214 LEU n 1 215 LYS n 1 216 ASN n 1 217 ILE n 1 218 SER n 1 219 ILE n 1 220 TYR n 1 221 THR n 1 222 LYS n 1 223 SER n 1 224 LEU n 1 225 VAL n 1 226 GLU n 1 227 LYS n 1 228 ILE n 1 229 LEU n 1 230 SER n 1 231 GLU n 1 232 LYS n 1 233 LYS n 1 234 GLU n 1 235 ASN n 1 236 GLY n 1 237 LEU n 1 238 ILE n 1 239 GLY n 1 240 ASN n 1 241 THR n 1 242 PHE n 1 243 SER n 1 244 THR n 1 245 GLY n 1 246 GLU n 1 247 ALA n 1 248 MET n 1 249 GLN n 1 250 ALA n 1 251 LEU n 1 252 PHE n 1 253 VAL n 1 254 SER n 1 255 SER n 1 256 ASP n 1 257 TYR n 1 258 TYR n 1 259 ASN n 1 260 GLU n 1 261 ASN n 1 262 ASP n 1 263 TRP n 1 264 ASN n 1 265 CYS n 1 266 GLN n 1 267 GLN n 1 268 THR n 1 269 LEU n 1 270 ASN n 1 271 THR n 1 272 VAL n 1 273 LEU n 1 274 THR n 1 275 GLU n 1 276 ILE n 1 277 SER n 1 278 GLN n 1 279 GLY n 1 280 ALA n 1 281 PHE n 1 282 SER n 1 283 ASN n 1 284 PRO n 1 285 ASN n 1 286 ALA n 1 287 ALA n 1 288 ALA n 1 289 GLN n 1 290 VAL n 1 291 LEU n 1 292 PRO n 1 293 ALA n 1 294 LEU n 1 295 MET n 1 296 GLY n 1 297 LYS n 1 298 THR n 1 299 PHE n 1 300 LEU n 1 301 ASP n 1 302 ILE n 1 303 ASN n 1 304 LYS n 1 305 ASP n 1 306 SER n 1 307 SER n 1 308 CYS n 1 309 VAL n 1 310 SER n 1 311 ALA n 1 312 SER n 1 313 GLY n 1 314 ASN n 1 315 PHE n 1 316 ASN n 1 317 ILE n 1 318 SER n 1 319 ALA n 1 320 ASP n 1 321 GLU n 1 322 PRO n 1 323 ILE n 1 324 THR n 1 325 VAL n 1 326 THR n 1 327 PRO n 1 328 PRO n 1 329 ASP n 1 330 SER n 1 331 GLN n 1 332 SER n 1 333 TYR n 1 334 ILE n 1 335 SER n 1 336 VAL n 1 337 ASN n 1 338 TYR n 1 339 SER n 1 340 VAL n 1 341 ARG n 1 342 ILE n 1 343 ASN n 1 344 GLU n 1 345 THR n 1 346 TYR n 1 347 PHE n 1 348 THR n 1 349 ASN n 1 350 VAL n 1 351 THR n 1 352 VAL n 1 353 LEU n 1 354 ASN n 1 355 GLY n 1 356 SER n 1 357 VAL n 1 358 PHE n 1 359 LEU n 1 360 SER n 1 361 VAL n 1 362 MET n 1 363 GLU n 1 364 LYS n 1 365 ALA n 1 366 GLN n 1 367 LYS n 1 368 MET n 1 369 ASN n 1 370 ASP n 1 371 THR n 1 372 ILE n 1 373 PHE n 1 374 GLY n 1 375 PHE n 1 376 THR n 1 377 MET n 1 378 GLU n 1 379 GLU n 1 380 ARG n 1 381 SER n 1 382 TRP n 1 383 GLY n 1 384 PRO n 1 385 TYR n 1 386 ILE n 1 387 THR n 1 388 CYS n 1 389 ILE n 1 390 GLN n 1 391 GLY n 1 392 LEU n 1 393 CYS n 1 394 ALA n 1 395 ASN n 1 396 ASN n 1 397 ASN n 1 398 ASP n 1 399 ARG n 1 400 THR n 1 401 TYR n 1 402 TRP n 1 403 GLU n 1 404 LEU n 1 405 LEU n 1 406 SER n 1 407 GLY n 1 408 GLY n 1 409 GLU n 1 410 PRO n 1 411 LEU n 1 412 SER n 1 413 GLN n 1 414 GLY n 1 415 ALA n 1 416 GLY n 1 417 SER n 1 418 TYR n 1 419 VAL n 1 420 VAL n 1 421 ARG n 1 422 ASN n 1 423 GLY n 1 424 GLU n 1 425 ASN n 1 426 LEU n 1 427 GLU n 1 428 VAL n 1 429 ARG n 1 430 TRP n 1 431 SER n 1 432 LYS n 1 433 TYR n 1 434 LEU n 1 435 VAL n 1 436 PRO n 1 437 ARG n 1 438 GLY n 1 439 SER n 1 440 LEU n 1 441 GLU n 1 442 SER n 1 443 ARG n 1 444 GLY n 1 445 PRO n 1 446 PHE n 1 447 GLU n 1 448 GLN n 1 449 LYS n 1 450 LEU n 1 451 ILE n 1 452 SER n 1 453 GLU n 1 454 GLU n 1 455 ASP n 1 456 LEU n 1 457 ASN n 1 458 MET n 1 459 HIS n 1 460 THR n 1 461 GLY n 1 462 HIS n 1 463 HIS n 1 464 HIS n 1 465 HIS n 1 466 HIS n 1 467 HIS n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name human _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'TC1, TCN1' _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Homo sapiens' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line 'HEK293 GnTI-' _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Homo Sapiens' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 9606 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type plasmid _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name 'pcDNA4/myc-His A' _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code TCO1_HUMAN _struct_ref.pdbx_db_accession P20061 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;MRQSHQLPLVGLLLFSFIPSQLCEICEVSEENYIRLKPLLNTMIQSNYNRGTSAVNVVLSLKLVGIQIQTLMQKMIQQIK YNVKSRLSDVSSGELALIILALGVCRNAEENLIYDYHLIDKLENKFQAEIENMEAHNGTPLTNYYQLSLDVLALCLFNGN YSTAEVVNHFTPENKNYYFGSQFSVDTGAMAVLALTCVKKSLINGQIKADEGSLKNISIYTKSLVEKILSEKKENGLIGN TFSTGEAMQALFVSSDYYNENDWNCQQTLNTVLTEISQGAFSNPNAAAQVLPALMGKTFLDINKDSSCVSASGNFNISAD EPITVTPPDSQSYISVNYSVRINETYFTNVTVLNGSVFLSVMEKAQKMNDTIFGFTMEERSWGPYITCIQGLCANNNDRT YWELLSGGEPLSQGAGSYVVRNGENLEVRWSKY ; _struct_ref.pdbx_align_begin 1 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4KKI _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 433 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P20061 _struct_ref_seq.db_align_beg 1 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 433 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg -22 _struct_ref_seq.pdbx_auth_seq_align_end 410 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 4KKI LEU A 434 ? UNP P20061 ? ? 'EXPRESSION TAG' 411 1 1 4KKI VAL A 435 ? UNP P20061 ? ? 'EXPRESSION TAG' 412 2 1 4KKI PRO A 436 ? UNP P20061 ? ? 'EXPRESSION TAG' 413 3 1 4KKI ARG A 437 ? UNP P20061 ? ? 'EXPRESSION TAG' 414 4 1 4KKI GLY A 438 ? UNP P20061 ? ? 'EXPRESSION TAG' 415 5 1 4KKI SER A 439 ? UNP P20061 ? ? 'EXPRESSION TAG' 416 6 1 4KKI LEU A 440 ? UNP P20061 ? ? 'EXPRESSION TAG' 417 7 1 4KKI GLU A 441 ? UNP P20061 ? ? 'EXPRESSION TAG' 418 8 1 4KKI SER A 442 ? UNP P20061 ? ? 'EXPRESSION TAG' 419 9 1 4KKI ARG A 443 ? UNP P20061 ? ? 'EXPRESSION TAG' 420 10 1 4KKI GLY A 444 ? UNP P20061 ? ? 'EXPRESSION TAG' 421 11 1 4KKI PRO A 445 ? UNP P20061 ? ? 'EXPRESSION TAG' 422 12 1 4KKI PHE A 446 ? UNP P20061 ? ? 'EXPRESSION TAG' 423 13 1 4KKI GLU A 447 ? UNP P20061 ? ? 'EXPRESSION TAG' 424 14 1 4KKI GLN A 448 ? UNP P20061 ? ? 'EXPRESSION TAG' 425 15 1 4KKI LYS A 449 ? UNP P20061 ? ? 'EXPRESSION TAG' 426 16 1 4KKI LEU A 450 ? UNP P20061 ? ? 'EXPRESSION TAG' 427 17 1 4KKI ILE A 451 ? UNP P20061 ? ? 'EXPRESSION TAG' 428 18 1 4KKI SER A 452 ? UNP P20061 ? ? 'EXPRESSION TAG' 429 19 1 4KKI GLU A 453 ? UNP P20061 ? ? 'EXPRESSION TAG' 430 20 1 4KKI GLU A 454 ? UNP P20061 ? ? 'EXPRESSION TAG' 431 21 1 4KKI ASP A 455 ? UNP P20061 ? ? 'EXPRESSION TAG' 432 22 1 4KKI LEU A 456 ? UNP P20061 ? ? 'EXPRESSION TAG' 433 23 1 4KKI ASN A 457 ? UNP P20061 ? ? 'EXPRESSION TAG' 434 24 1 4KKI MET A 458 ? UNP P20061 ? ? 'EXPRESSION TAG' 435 25 1 4KKI HIS A 459 ? UNP P20061 ? ? 'EXPRESSION TAG' 436 26 1 4KKI THR A 460 ? UNP P20061 ? ? 'EXPRESSION TAG' 437 27 1 4KKI GLY A 461 ? UNP P20061 ? ? 'EXPRESSION TAG' 438 28 1 4KKI HIS A 462 ? UNP P20061 ? ? 'EXPRESSION TAG' 439 29 1 4KKI HIS A 463 ? UNP P20061 ? ? 'EXPRESSION TAG' 440 30 1 4KKI HIS A 464 ? UNP P20061 ? ? 'EXPRESSION TAG' 441 31 1 4KKI HIS A 465 ? UNP P20061 ? ? 'EXPRESSION TAG' 442 32 1 4KKI HIS A 466 ? UNP P20061 ? ? 'EXPRESSION TAG' 443 33 1 4KKI HIS A 467 ? UNP P20061 ? ? 'EXPRESSION TAG' 444 34 # 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 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CNC non-polymer . CO-CYANOCOBALAMIN ? 'C63 H88 Co N14 O14 P 1' 1355.365 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PEG non-polymer . 'DI(HYDROXYETHYL)ETHER' ? 'C4 H10 O3' 106.120 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 4KKI _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.57 _exptl_crystal.density_percent_sol 65.56 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp 277 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 6.5 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '50% PEG 400, 0.2M magnesium chloride, 0.1M sodium cacodylate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K' # _diffrn.id 1 _diffrn.ambient_temp 100.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector PIXEL _diffrn_detector.type 'PSI PILATUS 6M' _diffrn_detector.pdbx_collection_date 2011-03-25 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'LN2 COOLED FIXED-EXIT SI(111) MONOCHROMATOR, SAGITTALLY - HORIZONTALLY FOCUSSED' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.0015 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'SLS BEAMLINE X06SA' _diffrn_source.pdbx_synchrotron_site SLS _diffrn_source.pdbx_synchrotron_beamline X06SA _diffrn_source.pdbx_wavelength 1.0015 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4KKI _reflns.observed_criterion_sigma_I 0.000 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 49.000 _reflns.d_resolution_high 2.350 _reflns.number_obs 31018 _reflns.number_all ? _reflns.percent_possible_obs 100.0 _reflns.pdbx_Rmerge_I_obs 0.096 _reflns.pdbx_Rsym_value 0.096 _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 10.2 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.35 _reflns_shell.d_res_low 2.40 _reflns_shell.percent_possible_all 100.0 _reflns_shell.Rmerge_I_obs 1.485 _reflns_shell.pdbx_Rsym_value 1.485 _reflns_shell.meanI_over_sigI_obs 1.890 _reflns_shell.pdbx_redundancy 10.60 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4KKI _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 31015 _refine.ls_number_reflns_all 31018 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 2.000 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 49.00 _refine.ls_d_res_high 2.35 _refine.ls_percent_reflns_obs 100.0 _refine.ls_R_factor_obs 0.197 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.196 _refine.ls_R_factor_R_free 0.226 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.050 _refine.ls_number_reflns_R_free 1565 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model 'pdb entries 2PMV, 2BB6' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.280 _refine.pdbx_overall_phase_error 24.940 _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3116 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 269 _refine_hist.number_atoms_solvent 134 _refine_hist.number_atoms_total 3519 _refine_hist.d_res_high 2.35 _refine_hist.d_res_low 49.00 # 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 f_bond_d 0.002 ? ? 3444 'X-RAY DIFFRACTION' ? f_angle_d 0.683 ? ? 4661 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 14.037 ? ? 1303 'X-RAY DIFFRACTION' ? f_chiral_restr 0.046 ? ? 534 'X-RAY DIFFRACTION' ? f_plane_restr 0.002 ? ? 571 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all _refine_ls_shell.redundancy_reflns_obs _refine_ls_shell.number_reflns_obs 'X-RAY DIFFRACTION' . 2.3500 2.4258 2652 0.2687 100.00 0.3022 . . 157 . . . . 'X-RAY DIFFRACTION' . 2.4258 2.5125 2670 0.2526 100.00 0.2812 . . 135 . . . . 'X-RAY DIFFRACTION' . 2.5125 2.6131 2651 0.2280 100.00 0.2916 . . 128 . . . . 'X-RAY DIFFRACTION' . 2.6131 2.7320 2672 0.2208 100.00 0.2922 . . 134 . . . . 'X-RAY DIFFRACTION' . 2.7320 2.8760 2660 0.2218 100.00 0.2890 . . 137 . . . . 'X-RAY DIFFRACTION' . 2.8760 3.0562 2680 0.2176 100.00 0.2581 . . 136 . . . . 'X-RAY DIFFRACTION' . 3.0562 3.2921 2622 0.2214 100.00 0.2460 . . 151 . . . . 'X-RAY DIFFRACTION' . 3.2921 3.6233 2688 0.1961 100.00 0.2386 . . 150 . . . . 'X-RAY DIFFRACTION' . 3.6233 4.1474 2703 0.1752 100.00 0.2243 . . 122 . . . . 'X-RAY DIFFRACTION' . 4.1474 5.2244 2684 0.1645 100.00 0.1956 . . 168 . . . . 'X-RAY DIFFRACTION' . 5.2244 49.0737 2768 0.1942 100.00 0.1937 . . 147 . . . . # _struct.entry_id 4KKI _struct.title 'Crystal Structure of Haptocorrin in Complex with CNCbl' _struct.pdbx_descriptor Transcobalamin-1 _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4KKI _struct_keywords.pdbx_keywords 'TRANSPORT PROTEIN' _struct_keywords.text 'Cobalamin transport protein, alpha6-alpha6 helical barrel, transport protein' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 2 ? E N N 2 ? F N N 2 ? G N N 2 ? H N N 2 ? I N N 3 ? J N N 4 ? K N N 5 ? L N N 5 ? M N N 5 ? N N N 5 ? O N N 5 ? P N N 5 ? Q N N 5 ? R N N 5 ? S N N 5 ? T N N 5 ? U N N 5 ? V N N 6 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 SER A 29 ? ARG A 35 ? SER A 6 ARG A 12 5 ? 7 HELX_P HELX_P2 2 LEU A 36 ? SER A 46 ? LEU A 13 SER A 23 1 ? 11 HELX_P HELX_P3 3 ASN A 47 ? ASN A 49 ? ASN A 24 ASN A 26 5 ? 3 HELX_P HELX_P4 4 ALA A 54 ? VAL A 64 ? ALA A 31 VAL A 41 1 ? 11 HELX_P HELX_P5 5 ILE A 68 ? ARG A 86 ? ILE A 45 ARG A 63 1 ? 19 HELX_P HELX_P6 6 SER A 91 ? GLY A 103 ? SER A 68 GLY A 80 1 ? 13 HELX_P HELX_P7 7 ASN A 107 ? GLU A 109 ? ASN A 84 GLU A 86 5 ? 3 HELX_P HELX_P8 8 GLU A 110 ? TYR A 116 ? GLU A 87 TYR A 93 1 ? 7 HELX_P HELX_P9 9 HIS A 117 ? HIS A 136 ? HIS A 94 HIS A 113 1 ? 20 HELX_P HELX_P10 10 ASN A 143 ? PHE A 157 ? ASN A 120 PHE A 134 1 ? 15 HELX_P HELX_P11 11 SER A 162 ? PHE A 170 ? SER A 139 PHE A 147 1 ? 9 HELX_P HELX_P12 12 ASN A 174 ? ASN A 176 ? ASN A 151 ASN A 153 5 ? 3 HELX_P HELX_P13 13 SER A 184 ? ASN A 204 ? SER A 161 ASN A 181 1 ? 21 HELX_P HELX_P14 14 GLY A 212 ? SER A 230 ? GLY A 189 SER A 207 1 ? 19 HELX_P HELX_P15 15 SER A 243 ? VAL A 253 ? SER A 220 VAL A 230 1 ? 11 HELX_P HELX_P16 16 SER A 254 ? TYR A 258 ? SER A 231 TYR A 235 5 ? 5 HELX_P HELX_P17 17 ASN A 264 ? GLN A 278 ? ASN A 241 GLN A 255 1 ? 15 HELX_P HELX_P18 18 ASN A 283 ? MET A 295 ? ASN A 260 MET A 272 1 ? 13 HELX_P HELX_P19 19 THR A 298 ? ILE A 302 ? THR A 275 ILE A 279 5 ? 5 HELX_P HELX_P20 20 VAL A 357 ? ASN A 369 ? VAL A 334 ASN A 346 1 ? 13 HELX_P HELX_P21 21 ASN A 369 ? GLY A 374 ? ASN A 346 GLY A 351 1 ? 6 # _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 26 SG ? ? ? 1_555 A CYS 265 SG ? ? A CYS 3 A CYS 242 1_555 ? ? ? ? ? ? ? 2.034 ? disulf2 disulf ? ? A CYS 105 SG ? ? ? 1_555 A CYS 308 SG ? ? A CYS 82 A CYS 285 1_555 ? ? ? ? ? ? ? 2.032 ? disulf3 disulf ? ? A CYS 155 SG ? ? ? 1_555 A CYS 197 SG ? ? A CYS 132 A CYS 174 1_555 ? ? ? ? ? ? ? 2.036 ? disulf4 disulf ? ? A CYS 388 SG ? ? ? 1_555 A CYS 393 SG ? ? A CYS 365 A CYS 370 1_555 ? ? ? ? ? ? ? 2.032 ? covale1 covale ? ? A ASN 343 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 320 A NAG 501 1_555 ? ? ? ? ? ? ? 1.439 ? covale2 covale ? ? A ASN 354 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 331 A NAG 506 1_555 ? ? ? ? ? ? ? 1.447 ? covale3 covale ? ? A ASN 316 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 293 A NAG 505 1_555 ? ? ? ? ? ? ? 1.440 ? covale4 covale ? ? A ASN 337 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 314 A NAG 507 1_555 ? ? ? ? ? ? ? 1.441 ? covale5 covale ? ? A ASN 369 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 346 A NAG 503 1_555 ? ? ? ? ? ? ? 1.454 ? covale6 covale ? ? A ASN 216 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 193 A NAG 504 1_555 ? ? ? ? ? ? ? 1.442 ? covale7 covale ? ? A ASN 349 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 326 A NAG 502 1_555 ? ? ? ? ? ? ? 1.451 ? metalc1 metalc ? ? J CA . CA ? ? ? 1_555 V HOH . O ? ? A CA 509 A HOH 725 1_555 ? ? ? ? ? ? ? 2.441 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 2 ? B ? 5 ? C ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? parallel B 3 4 ? anti-parallel B 4 5 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 TYR A 178 ? PHE A 179 ? TYR A 155 PHE A 156 A 2 GLN A 182 ? PHE A 183 ? GLN A 159 PHE A 160 B 1 THR A 345 ? LEU A 353 ? THR A 322 LEU A 330 B 2 TYR A 333 ? ARG A 341 ? TYR A 310 ARG A 318 B 3 LEU A 426 ? LYS A 432 ? LEU A 403 LYS A 409 B 4 THR A 400 ? SER A 406 ? THR A 377 SER A 383 B 5 GLU A 409 ? PRO A 410 ? GLU A 386 PRO A 387 C 1 PHE A 375 ? GLU A 379 ? PHE A 352 GLU A 356 C 2 PRO A 384 ? ILE A 389 ? PRO A 361 ILE A 366 C 3 LEU A 392 ? CYS A 393 ? LEU A 369 CYS A 370 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N PHE A 179 ? N PHE A 156 O GLN A 182 ? O GLN A 159 B 1 2 O VAL A 352 ? O VAL A 329 N ILE A 334 ? N ILE A 311 B 2 3 N ARG A 341 ? N ARG A 318 O TRP A 430 ? O TRP A 407 B 3 4 O ARG A 429 ? O ARG A 406 N GLU A 403 ? N GLU A 380 B 4 5 N SER A 406 ? N SER A 383 O GLU A 409 ? O GLU A 386 C 1 2 N THR A 376 ? N THR A 353 O CYS A 388 ? O CYS A 365 C 2 3 N ILE A 389 ? N ILE A 366 O LEU A 392 ? O LEU A 369 # 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 ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG A 501' AC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 502' AC3 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 503' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 504' AC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 505' AC6 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 506' AC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 507' AC8 Software ? ? ? ? 36 'BINDING SITE FOR RESIDUE CNC A 508' AC9 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE CA A 509' BC1 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE PEG A 510' BC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE PEG A 511' BC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE PEG A 512' BC4 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE PEG A 513' BC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE PEG A 514' BC6 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE PEG A 515' BC7 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE PEG A 516' BC8 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE PEG A 517' BC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE PEG A 518' CC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE PEG A 519' CC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE PEG A 520' # 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 8 GLN A 67 ? GLN A 44 . ? 5_555 ? 2 AC1 8 GLN A 69 ? GLN A 46 . ? 5_555 ? 3 AC1 8 ASN A 107 ? ASN A 84 . ? 5_555 ? 4 AC1 8 GLU A 109 ? GLU A 86 . ? 5_555 ? 5 AC1 8 SER A 310 ? SER A 287 . ? 5_555 ? 6 AC1 8 ILE A 342 ? ILE A 319 . ? 1_555 ? 7 AC1 8 ASN A 343 ? ASN A 320 . ? 1_555 ? 8 AC1 8 TRP A 430 ? TRP A 407 . ? 1_555 ? 9 AC2 6 ASP A 120 ? ASP A 97 . ? 5_554 ? 10 AC2 6 GLU A 123 ? GLU A 100 . ? 5_554 ? 11 AC2 6 ASN A 124 ? ASN A 101 . ? 5_554 ? 12 AC2 6 ASN A 349 ? ASN A 326 . ? 1_555 ? 13 AC2 6 THR A 351 ? THR A 328 . ? 1_555 ? 14 AC2 6 NAG F . ? NAG A 505 . ? 5_555 ? 15 AC3 6 LYS A 37 ? LYS A 14 . ? 5_555 ? 16 AC3 6 ASN A 41 ? ASN A 18 . ? 5_555 ? 17 AC3 6 GLN A 45 ? GLN A 22 . ? 5_555 ? 18 AC3 6 ILE A 317 ? ILE A 294 . ? 5_555 ? 19 AC3 6 ASN A 369 ? ASN A 346 . ? 1_555 ? 20 AC3 6 THR A 371 ? THR A 348 . ? 1_555 ? 21 AC4 5 ASP A 210 ? ASP A 187 . ? 1_555 ? 22 AC4 5 GLU A 211 ? GLU A 188 . ? 4_565 ? 23 AC4 5 GLU A 211 ? GLU A 188 . ? 1_555 ? 24 AC4 5 SER A 213 ? SER A 190 . ? 1_555 ? 25 AC4 5 ASN A 216 ? ASN A 193 . ? 1_555 ? 26 AC5 3 ASN A 316 ? ASN A 293 . ? 1_555 ? 27 AC5 3 NAG C . ? NAG A 502 . ? 6_554 ? 28 AC5 3 HOH V . ? HOH A 669 . ? 1_555 ? 29 AC6 2 ILE A 334 ? ILE A 311 . ? 1_555 ? 30 AC6 2 ASN A 354 ? ASN A 331 . ? 1_555 ? 31 AC7 5 ASN A 337 ? ASN A 314 . ? 1_555 ? 32 AC7 5 SER A 339 ? SER A 316 . ? 1_555 ? 33 AC7 5 THR A 345 ? THR A 322 . ? 1_555 ? 34 AC7 5 PHE A 347 ? PHE A 324 . ? 1_555 ? 35 AC7 5 ASN A 425 ? ASN A 402 . ? 1_555 ? 36 AC8 36 GLY A 93 ? GLY A 70 . ? 1_555 ? 37 AC8 36 GLU A 94 ? GLU A 71 . ? 1_555 ? 38 AC8 36 THR A 142 ? THR A 119 . ? 1_555 ? 39 AC8 36 ASN A 143 ? ASN A 120 . ? 1_555 ? 40 AC8 36 TYR A 145 ? TYR A 122 . ? 1_555 ? 41 AC8 36 GLN A 146 ? GLN A 123 . ? 1_555 ? 42 AC8 36 PHE A 179 ? PHE A 156 . ? 1_555 ? 43 AC8 36 ASP A 186 ? ASP A 163 . ? 1_555 ? 44 AC8 36 ASN A 240 ? ASN A 217 . ? 1_555 ? 45 AC8 36 PHE A 242 ? PHE A 219 . ? 1_555 ? 46 AC8 36 SER A 243 ? SER A 220 . ? 1_555 ? 47 AC8 36 GLN A 289 ? GLN A 266 . ? 1_555 ? 48 AC8 36 TRP A 382 ? TRP A 359 . ? 1_555 ? 49 AC8 36 GLY A 383 ? GLY A 360 . ? 1_555 ? 50 AC8 36 PRO A 384 ? PRO A 361 . ? 1_555 ? 51 AC8 36 TYR A 385 ? TYR A 362 . ? 1_555 ? 52 AC8 36 ILE A 386 ? ILE A 363 . ? 1_555 ? 53 AC8 36 ASN A 396 ? ASN A 373 . ? 1_555 ? 54 AC8 36 TYR A 401 ? TYR A 378 . ? 1_555 ? 55 AC8 36 TRP A 402 ? TRP A 379 . ? 1_555 ? 56 AC8 36 GLU A 403 ? GLU A 380 . ? 1_555 ? 57 AC8 36 LEU A 404 ? LEU A 381 . ? 1_555 ? 58 AC8 36 LEU A 411 ? LEU A 388 . ? 1_555 ? 59 AC8 36 SER A 412 ? SER A 389 . ? 1_555 ? 60 AC8 36 GLN A 413 ? GLN A 390 . ? 1_555 ? 61 AC8 36 GLY A 414 ? GLY A 391 . ? 1_555 ? 62 AC8 36 TYR A 433 ? TYR A 410 . ? 1_555 ? 63 AC8 36 PEG T . ? PEG A 519 . ? 1_555 ? 64 AC8 36 HOH V . ? HOH A 602 . ? 1_555 ? 65 AC8 36 HOH V . ? HOH A 603 . ? 1_555 ? 66 AC8 36 HOH V . ? HOH A 631 . ? 1_555 ? 67 AC8 36 HOH V . ? HOH A 668 . ? 1_555 ? 68 AC8 36 HOH V . ? HOH A 720 . ? 1_555 ? 69 AC8 36 HOH V . ? HOH A 721 . ? 1_555 ? 70 AC8 36 HOH V . ? HOH A 723 . ? 1_555 ? 71 AC8 36 HOH V . ? HOH A 734 . ? 1_555 ? 72 AC9 1 HOH V . ? HOH A 725 . ? 1_555 ? 73 BC1 7 THR A 196 ? THR A 173 . ? 1_555 ? 74 BC1 7 LYS A 200 ? LYS A 177 . ? 1_555 ? 75 BC1 7 ILE A 203 ? ILE A 180 . ? 1_555 ? 76 BC1 7 VAL A 253 ? VAL A 230 . ? 1_555 ? 77 BC1 7 ASP A 256 ? ASP A 233 . ? 4_565 ? 78 BC1 7 TYR A 257 ? TYR A 234 . ? 4_565 ? 79 BC1 7 PEG L . ? PEG A 511 . ? 1_555 ? 80 BC2 4 LYS A 200 ? LYS A 177 . ? 1_555 ? 81 BC2 4 ASP A 256 ? ASP A 233 . ? 4_565 ? 82 BC2 4 TYR A 258 ? TYR A 235 . ? 4_565 ? 83 BC2 4 PEG K . ? PEG A 510 . ? 1_555 ? 84 BC3 5 LEU A 63 ? LEU A 40 . ? 1_555 ? 85 BC3 5 GLY A 65 ? GLY A 42 . ? 1_555 ? 86 BC3 5 VAL A 104 ? VAL A 81 . ? 1_555 ? 87 BC3 5 LYS A 297 ? LYS A 274 . ? 1_555 ? 88 BC3 5 ASP A 301 ? ASP A 278 . ? 1_555 ? 89 BC4 2 GLY A 65 ? GLY A 42 . ? 1_555 ? 90 BC4 2 ILE A 66 ? ILE A 43 . ? 1_555 ? 91 BC5 4 CYS A 155 ? CYS A 132 . ? 1_555 ? 92 BC5 4 LEU A 156 ? LEU A 133 . ? 1_555 ? 93 BC5 4 ASN A 158 ? ASN A 135 . ? 1_555 ? 94 BC5 4 GLN A 206 ? GLN A 183 . ? 1_555 ? 95 BC6 2 LYS A 222 ? LYS A 199 . ? 1_555 ? 96 BC6 2 GLU A 226 ? GLU A 203 . ? 1_555 ? 97 BC7 1 GLN A 278 ? GLN A 255 . ? 1_555 ? 98 BC8 6 ASN A 49 ? ASN A 26 . ? 1_555 ? 99 BC8 6 PRO A 284 ? PRO A 261 . ? 1_555 ? 100 BC8 6 GLU A 379 ? GLU A 356 . ? 1_555 ? 101 BC8 6 ARG A 380 ? ARG A 357 . ? 1_555 ? 102 BC8 6 SER A 381 ? SER A 358 . ? 1_555 ? 103 BC8 6 GLY A 383 ? GLY A 360 . ? 1_555 ? 104 BC9 3 ASN A 395 ? ASN A 372 . ? 1_555 ? 105 BC9 3 ASN A 397 ? ASN A 374 . ? 1_555 ? 106 BC9 3 ASP A 398 ? ASP A 375 . ? 1_555 ? 107 CC1 4 ASN A 240 ? ASN A 217 . ? 1_555 ? 108 CC1 4 LEU A 411 ? LEU A 388 . ? 1_555 ? 109 CC1 4 SER A 412 ? SER A 389 . ? 1_555 ? 110 CC1 4 CNC I . ? CNC A 508 . ? 1_555 ? 111 CC2 6 SER A 53 ? SER A 30 . ? 1_555 ? 112 CC2 6 VAL A 55 ? VAL A 32 . ? 1_555 ? 113 CC2 6 ASN A 82 ? ASN A 59 . ? 1_555 ? 114 CC2 6 GLU A 94 ? GLU A 71 . ? 1_555 ? 115 CC2 6 LEU A 97 ? LEU A 74 . ? 1_555 ? 116 CC2 6 HOH V . ? HOH A 733 . ? 1_555 ? # _database_PDB_matrix.entry_id 4KKI _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 4KKI _atom_sites.fract_transf_matrix[1][1] 0.006672 _atom_sites.fract_transf_matrix[1][2] 0.003852 _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] 0.007704 _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] 0.017394 _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 CA CO N O P 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 . GLU A 1 24 ? -33.626 64.900 11.732 1.00 39.46 ? 1 GLU A N 1 ATOM 2 C CA . GLU A 1 24 ? -34.050 64.601 10.370 1.00 44.68 ? 1 GLU A CA 1 ATOM 3 C C . GLU A 1 24 ? -33.909 63.115 10.059 1.00 45.70 ? 1 GLU A C 1 ATOM 4 O O . GLU A 1 24 ? -32.953 62.470 10.489 1.00 47.88 ? 1 GLU A O 1 ATOM 5 C CB . GLU A 1 24 ? -33.236 65.418 9.366 1.00 39.59 ? 1 GLU A CB 1 ATOM 6 C CG . GLU A 1 24 ? -33.634 65.193 7.914 1.00 55.60 ? 1 GLU A CG 1 ATOM 7 C CD . GLU A 1 24 ? -32.734 65.924 6.938 1.00 71.06 ? 1 GLU A CD 1 ATOM 8 O OE1 . GLU A 1 24 ? -31.832 66.657 7.395 1.00 71.10 ? 1 GLU A OE1 1 ATOM 9 O OE2 . GLU A 1 24 ? -32.929 65.760 5.713 1.00 76.50 ? 1 GLU A OE2 1 ATOM 10 N N . ILE A 1 25 ? -34.870 62.572 9.318 1.00 47.96 ? 2 ILE A N 1 ATOM 11 C CA . ILE A 1 25 ? -34.773 61.200 8.837 1.00 47.04 ? 2 ILE A CA 1 ATOM 12 C C . ILE A 1 25 ? -34.834 61.165 7.315 1.00 54.40 ? 2 ILE A C 1 ATOM 13 O O . ILE A 1 25 ? -35.818 61.595 6.712 1.00 51.54 ? 2 ILE A O 1 ATOM 14 C CB . ILE A 1 25 ? -35.890 60.303 9.414 1.00 51.48 ? 2 ILE A CB 1 ATOM 15 C CG1 . ILE A 1 25 ? -35.896 60.375 10.943 1.00 54.98 ? 2 ILE A CG1 1 ATOM 16 C CG2 . ILE A 1 25 ? -35.714 58.861 8.943 1.00 37.72 ? 2 ILE A CG2 1 ATOM 17 C CD1 . ILE A 1 25 ? -36.956 59.514 11.595 1.00 46.89 ? 2 ILE A CD1 1 ATOM 18 N N . CYS A 1 26 ? -33.768 60.669 6.695 1.00 49.11 ? 3 CYS A N 1 ATOM 19 C CA . CYS A 1 26 ? -33.770 60.437 5.257 1.00 46.30 ? 3 CYS A CA 1 ATOM 20 C C . CYS A 1 26 ? -33.478 58.967 4.982 1.00 46.66 ? 3 CYS A C 1 ATOM 21 O O . CYS A 1 26 ? -33.017 58.240 5.863 1.00 47.77 ? 3 CYS A O 1 ATOM 22 C CB . CYS A 1 26 ? -32.763 61.342 4.539 1.00 43.29 ? 3 CYS A CB 1 ATOM 23 S SG . CYS A 1 26 ? -31.029 60.902 4.770 1.00 55.11 ? 3 CYS A SG 1 ATOM 24 N N . GLU A 1 27 ? -33.760 58.529 3.762 1.00 44.00 ? 4 GLU A N 1 ATOM 25 C CA . GLU A 1 27 ? -33.580 57.130 3.405 1.00 47.44 ? 4 GLU A CA 1 ATOM 26 C C . GLU A 1 27 ? -33.494 56.958 1.898 1.00 45.67 ? 4 GLU A C 1 ATOM 27 O O . GLU A 1 27 ? -33.850 57.857 1.137 1.00 53.01 ? 4 GLU A O 1 ATOM 28 C CB . GLU A 1 27 ? -34.725 56.281 3.967 1.00 52.55 ? 4 GLU A CB 1 ATOM 29 C CG . GLU A 1 27 ? -36.103 56.670 3.452 1.00 60.20 ? 4 GLU A CG 1 ATOM 30 C CD . GLU A 1 27 ? -37.224 56.051 4.266 1.00 68.78 ? 4 GLU A CD 1 ATOM 31 O OE1 . GLU A 1 27 ? -37.664 54.933 3.927 1.00 70.04 ? 4 GLU A OE1 1 ATOM 32 O OE2 . GLU A 1 27 ? -37.664 56.685 5.249 1.00 74.70 ? 4 GLU A OE2 1 ATOM 33 N N . VAL A 1 28 ? -33.011 55.795 1.478 1.00 37.97 ? 5 VAL A N 1 ATOM 34 C CA . VAL A 1 28 ? -32.906 55.471 0.065 1.00 43.11 ? 5 VAL A CA 1 ATOM 35 C C . VAL A 1 28 ? -34.292 55.357 -0.560 1.00 53.23 ? 5 VAL A C 1 ATOM 36 O O . VAL A 1 28 ? -35.149 54.628 -0.059 1.00 56.07 ? 5 VAL A O 1 ATOM 37 C CB . VAL A 1 28 ? -32.144 54.146 -0.138 1.00 45.42 ? 5 VAL A CB 1 ATOM 38 C CG1 . VAL A 1 28 ? -32.146 53.747 -1.598 1.00 44.04 ? 5 VAL A CG1 1 ATOM 39 C CG2 . VAL A 1 28 ? -30.718 54.268 0.385 1.00 52.03 ? 5 VAL A CG2 1 ATOM 40 N N . SER A 1 29 ? -34.512 56.089 -1.648 1.00 58.06 ? 6 SER A N 1 ATOM 41 C CA . SER A 1 29 ? -35.767 55.994 -2.386 1.00 69.44 ? 6 SER A CA 1 ATOM 42 C C . SER A 1 29 ? -35.931 54.594 -2.972 1.00 73.95 ? 6 SER A C 1 ATOM 43 O O . SER A 1 29 ? -34.949 53.877 -3.170 1.00 70.43 ? 6 SER A O 1 ATOM 44 C CB . SER A 1 29 ? -35.824 57.048 -3.493 1.00 69.79 ? 6 SER A CB 1 ATOM 45 O OG . SER A 1 29 ? -34.706 56.942 -4.358 1.00 80.34 ? 6 SER A OG 1 ATOM 46 N N . GLU A 1 30 ? -37.173 54.208 -3.248 1.00 84.10 ? 7 GLU A N 1 ATOM 47 C CA . GLU A 1 30 ? -37.462 52.875 -3.772 1.00 93.61 ? 7 GLU A CA 1 ATOM 48 C C . GLU A 1 30 ? -36.862 52.658 -5.159 1.00 91.34 ? 7 GLU A C 1 ATOM 49 O O . GLU A 1 30 ? -36.654 51.521 -5.583 1.00 91.85 ? 7 GLU A O 1 ATOM 50 C CB . GLU A 1 30 ? -38.969 52.608 -3.791 1.00 108.44 ? 7 GLU A CB 1 ATOM 51 C CG . GLU A 1 30 ? -39.610 52.570 -2.412 1.00 119.79 ? 7 GLU A CG 1 ATOM 52 C CD . GLU A 1 30 ? -40.955 51.867 -2.410 1.00 131.17 ? 7 GLU A CD 1 ATOM 53 O OE1 . GLU A 1 30 ? -41.165 50.979 -3.264 1.00 133.23 ? 7 GLU A OE1 1 ATOM 54 O OE2 . GLU A 1 30 ? -41.803 52.201 -1.556 1.00 135.89 ? 7 GLU A OE2 1 ATOM 55 N N . GLU A 1 31 ? -36.586 53.752 -5.860 1.00 93.07 ? 8 GLU A N 1 ATOM 56 C CA . GLU A 1 31 ? -35.934 53.681 -7.161 1.00 97.88 ? 8 GLU A CA 1 ATOM 57 C C . GLU A 1 31 ? -34.462 53.307 -7.001 1.00 90.49 ? 8 GLU A C 1 ATOM 58 O O . GLU A 1 31 ? -33.884 52.633 -7.853 1.00 89.30 ? 8 GLU A O 1 ATOM 59 C CB . GLU A 1 31 ? -36.064 55.017 -7.898 1.00 108.04 ? 8 GLU A CB 1 ATOM 60 C CG . GLU A 1 31 ? -35.367 55.058 -9.250 1.00 122.82 ? 8 GLU A CG 1 ATOM 61 C CD . GLU A 1 31 ? -35.583 56.369 -9.982 1.00 132.91 ? 8 GLU A CD 1 ATOM 62 O OE1 . GLU A 1 31 ? -36.564 57.074 -9.667 1.00 139.23 ? 8 GLU A OE1 1 ATOM 63 O OE2 . GLU A 1 31 ? -34.768 56.695 -10.872 1.00 132.55 ? 8 GLU A OE2 1 ATOM 64 N N . ASN A 1 32 ? -33.864 53.738 -5.895 1.00 81.48 ? 9 ASN A N 1 ATOM 65 C CA . ASN A 1 32 ? -32.442 53.516 -5.663 1.00 83.17 ? 9 ASN A CA 1 ATOM 66 C C . ASN A 1 32 ? -32.141 52.316 -4.767 1.00 71.68 ? 9 ASN A C 1 ATOM 67 O O . ASN A 1 32 ? -31.024 52.176 -4.270 1.00 67.30 ? 9 ASN A O 1 ATOM 68 C CB . ASN A 1 32 ? -31.794 54.777 -5.087 1.00 87.78 ? 9 ASN A CB 1 ATOM 69 C CG . ASN A 1 32 ? -31.938 55.974 -6.005 1.00 89.71 ? 9 ASN A CG 1 ATOM 70 O OD1 . ASN A 1 32 ? -32.735 55.958 -6.942 1.00 87.02 ? 9 ASN A OD1 1 ATOM 71 N ND2 . ASN A 1 32 ? -31.166 57.021 -5.738 1.00 90.94 ? 9 ASN A ND2 1 ATOM 72 N N . TYR A 1 33 ? -33.134 51.453 -4.566 1.00 64.08 ? 10 TYR A N 1 ATOM 73 C CA . TYR A 1 33 ? -32.950 50.249 -3.759 1.00 64.93 ? 10 TYR A CA 1 ATOM 74 C C . TYR A 1 33 ? -31.860 49.349 -4.330 1.00 64.21 ? 10 TYR A C 1 ATOM 75 O O . TYR A 1 33 ? -31.214 48.600 -3.597 1.00 59.27 ? 10 TYR A O 1 ATOM 76 C CB . TYR A 1 33 ? -34.256 49.462 -3.642 1.00 67.98 ? 10 TYR A CB 1 ATOM 77 C CG . TYR A 1 33 ? -35.136 49.892 -2.492 1.00 84.25 ? 10 TYR A CG 1 ATOM 78 C CD1 . TYR A 1 33 ? -34.764 50.939 -1.659 1.00 84.83 ? 10 TYR A CD1 1 ATOM 79 C CD2 . TYR A 1 33 ? -36.334 49.239 -2.230 1.00 93.47 ? 10 TYR A CD2 1 ATOM 80 C CE1 . TYR A 1 33 ? -35.567 51.331 -0.604 1.00 84.31 ? 10 TYR A CE1 1 ATOM 81 C CE2 . TYR A 1 33 ? -37.142 49.623 -1.178 1.00 94.18 ? 10 TYR A CE2 1 ATOM 82 C CZ . TYR A 1 33 ? -36.754 50.669 -0.368 1.00 91.43 ? 10 TYR A CZ 1 ATOM 83 O OH . TYR A 1 33 ? -37.557 51.054 0.681 1.00 95.27 ? 10 TYR A OH 1 ATOM 84 N N . ILE A 1 34 ? -31.662 49.434 -5.642 1.00 59.60 ? 11 ILE A N 1 ATOM 85 C CA . ILE A 1 34 ? -30.650 48.642 -6.330 1.00 49.76 ? 11 ILE A CA 1 ATOM 86 C C . ILE A 1 34 ? -29.245 48.965 -5.809 1.00 51.67 ? 11 ILE A C 1 ATOM 87 O O . ILE A 1 34 ? -28.355 48.115 -5.828 1.00 61.13 ? 11 ILE A O 1 ATOM 88 C CB . ILE A 1 34 ? -30.729 48.844 -7.869 1.00 58.39 ? 11 ILE A CB 1 ATOM 89 C CG1 . ILE A 1 34 ? -29.777 47.892 -8.599 1.00 64.16 ? 11 ILE A CG1 1 ATOM 90 C CG2 . ILE A 1 34 ? -30.462 50.300 -8.245 1.00 50.74 ? 11 ILE A CG2 1 ATOM 91 C CD1 . ILE A 1 34 ? -30.061 46.426 -8.343 1.00 69.78 ? 11 ILE A CD1 1 ATOM 92 N N . ARG A 1 35 ? -29.061 50.187 -5.320 1.00 54.70 ? 12 ARG A N 1 ATOM 93 C CA . ARG A 1 35 ? -27.773 50.608 -4.778 1.00 53.82 ? 12 ARG A CA 1 ATOM 94 C C . ARG A 1 35 ? -27.432 49.892 -3.473 1.00 51.21 ? 12 ARG A C 1 ATOM 95 O O . ARG A 1 35 ? -26.275 49.872 -3.056 1.00 57.18 ? 12 ARG A O 1 ATOM 96 C CB . ARG A 1 35 ? -27.747 52.124 -4.568 1.00 52.63 ? 12 ARG A CB 1 ATOM 97 C CG . ARG A 1 35 ? -27.602 52.927 -5.848 1.00 59.13 ? 12 ARG A CG 1 ATOM 98 C CD . ARG A 1 35 ? -27.590 54.416 -5.553 1.00 77.43 ? 12 ARG A CD 1 ATOM 99 N NE . ARG A 1 35 ? -27.147 55.201 -6.700 1.00 93.36 ? 12 ARG A NE 1 ATOM 100 C CZ . ARG A 1 35 ? -25.888 55.574 -6.907 1.00 101.41 ? 12 ARG A CZ 1 ATOM 101 N NH1 . ARG A 1 35 ? -24.943 55.234 -6.042 1.00 95.17 ? 12 ARG A NH1 1 ATOM 102 N NH2 . ARG A 1 35 ? -25.574 56.289 -7.979 1.00 108.15 ? 12 ARG A NH2 1 ATOM 103 N N . LEU A 1 36 ? -28.438 49.304 -2.835 1.00 51.42 ? 13 LEU A N 1 ATOM 104 C CA . LEU A 1 36 ? -28.224 48.577 -1.587 1.00 50.04 ? 13 LEU A CA 1 ATOM 105 C C . LEU A 1 36 ? -27.878 47.110 -1.825 1.00 43.04 ? 13 LEU A C 1 ATOM 106 O O . LEU A 1 36 ? -27.554 46.386 -0.885 1.00 46.28 ? 13 LEU A O 1 ATOM 107 C CB . LEU A 1 36 ? -29.453 48.685 -0.684 1.00 47.92 ? 13 LEU A CB 1 ATOM 108 C CG . LEU A 1 36 ? -29.827 50.106 -0.262 1.00 51.70 ? 13 LEU A CG 1 ATOM 109 C CD1 . LEU A 1 36 ? -30.980 50.086 0.726 1.00 52.26 ? 13 LEU A CD1 1 ATOM 110 C CD2 . LEU A 1 36 ? -28.624 50.818 0.326 1.00 47.97 ? 13 LEU A CD2 1 ATOM 111 N N . LYS A 1 37 ? -27.951 46.682 -3.082 1.00 50.84 ? 14 LYS A N 1 ATOM 112 C CA . LYS A 1 37 ? -27.656 45.294 -3.454 1.00 55.28 ? 14 LYS A CA 1 ATOM 113 C C . LYS A 1 37 ? -26.291 44.763 -2.982 1.00 51.50 ? 14 LYS A C 1 ATOM 114 O O . LYS A 1 37 ? -26.217 43.630 -2.503 1.00 52.68 ? 14 LYS A O 1 ATOM 115 C CB . LYS A 1 37 ? -27.818 45.082 -4.967 1.00 62.31 ? 14 LYS A CB 1 ATOM 116 C CG . LYS A 1 37 ? -28.739 43.927 -5.354 1.00 73.80 ? 14 LYS A CG 1 ATOM 117 C CD . LYS A 1 37 ? -28.258 42.601 -4.779 1.00 80.12 ? 14 LYS A CD 1 ATOM 118 C CE . LYS A 1 37 ? -29.100 41.427 -5.266 1.00 84.50 ? 14 LYS A CE 1 ATOM 119 N NZ . LYS A 1 37 ? -28.934 41.170 -6.726 1.00 81.44 ? 14 LYS A NZ 1 ATOM 120 N N . PRO A 1 38 ? -25.209 45.559 -3.127 1.00 51.57 ? 15 PRO A N 1 ATOM 121 C CA . PRO A 1 38 ? -23.919 45.047 -2.643 1.00 45.03 ? 15 PRO A CA 1 ATOM 122 C C . PRO A 1 38 ? -23.946 44.687 -1.163 1.00 45.56 ? 15 PRO A C 1 ATOM 123 O O . PRO A 1 38 ? -23.301 43.718 -0.758 1.00 38.54 ? 15 PRO A O 1 ATOM 124 C CB . PRO A 1 38 ? -22.971 46.223 -2.885 1.00 36.59 ? 15 PRO A CB 1 ATOM 125 C CG . PRO A 1 38 ? -23.555 46.914 -4.062 1.00 42.46 ? 15 PRO A CG 1 ATOM 126 C CD . PRO A 1 38 ? -25.040 46.836 -3.847 1.00 48.11 ? 15 PRO A CD 1 ATOM 127 N N . LEU A 1 39 ? -24.693 45.451 -0.372 1.00 38.09 ? 16 LEU A N 1 ATOM 128 C CA . LEU A 1 39 ? -24.841 45.154 1.046 1.00 41.34 ? 16 LEU A CA 1 ATOM 129 C C . LEU A 1 39 ? -25.531 43.810 1.210 1.00 49.51 ? 16 LEU A C 1 ATOM 130 O O . LEU A 1 39 ? -25.104 42.974 2.007 1.00 48.28 ? 16 LEU A O 1 ATOM 131 C CB . LEU A 1 39 ? -25.658 46.238 1.749 1.00 35.62 ? 16 LEU A CB 1 ATOM 132 C CG . LEU A 1 39 ? -25.140 47.675 1.690 1.00 37.73 ? 16 LEU A CG 1 ATOM 133 C CD1 . LEU A 1 39 ? -26.020 48.582 2.536 1.00 36.65 ? 16 LEU A CD1 1 ATOM 134 C CD2 . LEU A 1 39 ? -23.696 47.746 2.147 1.00 36.84 ? 16 LEU A CD2 1 ATOM 135 N N . LEU A 1 40 ? -26.600 43.615 0.444 1.00 47.28 ? 17 LEU A N 1 ATOM 136 C CA . LEU A 1 40 ? -27.367 42.378 0.485 1.00 46.64 ? 17 LEU A CA 1 ATOM 137 C C . LEU A 1 40 ? -26.487 41.203 0.075 1.00 45.47 ? 17 LEU A C 1 ATOM 138 O O . LEU A 1 40 ? -26.436 40.187 0.766 1.00 40.57 ? 17 LEU A O 1 ATOM 139 C CB . LEU A 1 40 ? -28.599 42.476 -0.425 1.00 54.18 ? 17 LEU A CB 1 ATOM 140 C CG . LEU A 1 40 ? -29.569 43.632 -0.146 1.00 69.85 ? 17 LEU A CG 1 ATOM 141 C CD1 . LEU A 1 40 ? -30.693 43.686 -1.177 1.00 77.20 ? 17 LEU A CD1 1 ATOM 142 C CD2 . LEU A 1 40 ? -30.139 43.532 1.261 1.00 67.77 ? 17 LEU A CD2 1 ATOM 143 N N . ASN A 1 41 ? -25.781 41.357 -1.042 1.00 36.06 ? 18 ASN A N 1 ATOM 144 C CA . ASN A 1 41 ? -24.877 40.321 -1.527 1.00 42.78 ? 18 ASN A CA 1 ATOM 145 C C . ASN A 1 41 ? -23.824 39.935 -0.498 1.00 46.08 ? 18 ASN A C 1 ATOM 146 O O . ASN A 1 41 ? -23.650 38.757 -0.202 1.00 48.15 ? 18 ASN A O 1 ATOM 147 C CB . ASN A 1 41 ? -24.207 40.749 -2.835 1.00 47.10 ? 18 ASN A CB 1 ATOM 148 C CG . ASN A 1 41 ? -25.194 40.872 -3.977 1.00 57.70 ? 18 ASN A CG 1 ATOM 149 O OD1 . ASN A 1 41 ? -26.228 40.204 -3.992 1.00 54.29 ? 18 ASN A OD1 1 ATOM 150 N ND2 . ASN A 1 41 ? -24.879 41.727 -4.943 1.00 60.77 ? 18 ASN A ND2 1 ATOM 151 N N . THR A 1 42 ? -23.143 40.936 0.052 1.00 48.13 ? 19 THR A N 1 ATOM 152 C CA . THR A 1 42 ? -22.132 40.727 1.086 1.00 49.06 ? 19 THR A CA 1 ATOM 153 C C . THR A 1 42 ? -22.648 39.885 2.258 1.00 47.72 ? 19 THR A C 1 ATOM 154 O O . THR A 1 42 ? -21.995 38.933 2.684 1.00 48.21 ? 19 THR A O 1 ATOM 155 C CB . THR A 1 42 ? -21.601 42.076 1.620 1.00 48.59 ? 19 THR A CB 1 ATOM 156 O OG1 . THR A 1 42 ? -20.829 42.726 0.602 1.00 51.05 ? 19 THR A OG1 1 ATOM 157 C CG2 . THR A 1 42 ? -20.732 41.868 2.847 1.00 35.51 ? 19 THR A CG2 1 ATOM 158 N N . MET A 1 43 ? -23.828 40.229 2.763 1.00 46.26 ? 20 MET A N 1 ATOM 159 C CA . MET A 1 43 ? -24.407 39.512 3.896 1.00 43.89 ? 20 MET A CA 1 ATOM 160 C C . MET A 1 43 ? -24.781 38.075 3.537 1.00 46.31 ? 20 MET A C 1 ATOM 161 O O . MET A 1 43 ? -24.716 37.182 4.382 1.00 46.91 ? 20 MET A O 1 ATOM 162 C CB . MET A 1 43 ? -25.610 40.278 4.455 1.00 37.67 ? 20 MET A CB 1 ATOM 163 C CG . MET A 1 43 ? -25.263 41.710 4.856 1.00 55.54 ? 20 MET A CG 1 ATOM 164 S SD . MET A 1 43 ? -26.673 42.775 5.222 1.00 62.95 ? 20 MET A SD 1 ATOM 165 C CE . MET A 1 43 ? -26.961 42.376 6.937 1.00 54.13 ? 20 MET A CE 1 ATOM 166 N N . ILE A 1 44 ? -25.153 37.849 2.281 1.00 48.37 ? 21 ILE A N 1 ATOM 167 C CA . ILE A 1 44 ? -25.461 36.498 1.818 1.00 48.68 ? 21 ILE A CA 1 ATOM 168 C C . ILE A 1 44 ? -24.206 35.621 1.763 1.00 51.83 ? 21 ILE A C 1 ATOM 169 O O . ILE A 1 44 ? -24.252 34.445 2.127 1.00 52.17 ? 21 ILE A O 1 ATOM 170 C CB . ILE A 1 44 ? -26.163 36.500 0.440 1.00 57.41 ? 21 ILE A CB 1 ATOM 171 C CG1 . ILE A 1 44 ? -27.469 37.289 0.501 1.00 58.98 ? 21 ILE A CG1 1 ATOM 172 C CG2 . ILE A 1 44 ? -26.457 35.081 -0.016 1.00 50.22 ? 21 ILE A CG2 1 ATOM 173 C CD1 . ILE A 1 44 ? -28.467 36.736 1.485 1.00 57.65 ? 21 ILE A CD1 1 ATOM 174 N N . GLN A 1 45 ? -23.087 36.194 1.321 1.00 47.73 ? 22 GLN A N 1 ATOM 175 C CA . GLN A 1 45 ? -21.842 35.431 1.207 1.00 54.14 ? 22 GLN A CA 1 ATOM 176 C C . GLN A 1 45 ? -21.310 35.020 2.574 1.00 50.49 ? 22 GLN A C 1 ATOM 177 O O . GLN A 1 45 ? -20.524 34.078 2.682 1.00 52.39 ? 22 GLN A O 1 ATOM 178 C CB . GLN A 1 45 ? -20.751 36.216 0.466 1.00 71.43 ? 22 GLN A CB 1 ATOM 179 C CG . GLN A 1 45 ? -21.217 37.112 -0.672 1.00 89.31 ? 22 GLN A CG 1 ATOM 180 C CD . GLN A 1 45 ? -21.683 36.360 -1.907 1.00 102.54 ? 22 GLN A CD 1 ATOM 181 O OE1 . GLN A 1 45 ? -21.883 35.145 -1.882 1.00 106.72 ? 22 GLN A OE1 1 ATOM 182 N NE2 . GLN A 1 45 ? -21.856 37.089 -3.004 1.00 105.51 ? 22 GLN A NE2 1 ATOM 183 N N . SER A 1 46 ? -21.738 35.731 3.614 1.00 41.34 ? 23 SER A N 1 ATOM 184 C CA . SER A 1 46 ? -21.277 35.453 4.971 1.00 45.50 ? 23 SER A CA 1 ATOM 185 C C . SER A 1 46 ? -21.751 34.087 5.471 1.00 52.96 ? 23 SER A C 1 ATOM 186 O O . SER A 1 46 ? -21.265 33.591 6.487 1.00 50.75 ? 23 SER A O 1 ATOM 187 C CB . SER A 1 46 ? -21.703 36.565 5.937 1.00 42.53 ? 23 SER A CB 1 ATOM 188 O OG . SER A 1 46 ? -23.107 36.593 6.113 1.00 47.76 ? 23 SER A OG 1 ATOM 189 N N . ASN A 1 47 ? -22.699 33.487 4.752 1.00 51.84 ? 24 ASN A N 1 ATOM 190 C CA . ASN A 1 47 ? -23.127 32.115 5.018 1.00 54.04 ? 24 ASN A CA 1 ATOM 191 C C . ASN A 1 47 ? -21.967 31.124 4.987 1.00 61.37 ? 24 ASN A C 1 ATOM 192 O O . ASN A 1 47 ? -21.944 30.158 5.748 1.00 65.44 ? 24 ASN A O 1 ATOM 193 C CB . ASN A 1 47 ? -24.183 31.675 4.002 1.00 51.93 ? 24 ASN A CB 1 ATOM 194 C CG . ASN A 1 47 ? -25.597 31.839 4.519 1.00 58.01 ? 24 ASN A CG 1 ATOM 195 O OD1 . ASN A 1 47 ? -26.393 32.589 3.954 1.00 67.51 ? 24 ASN A OD1 1 ATOM 196 N ND2 . ASN A 1 47 ? -25.922 31.128 5.593 1.00 59.16 ? 24 ASN A ND2 1 ATOM 197 N N . TYR A 1 48 ? -21.009 31.374 4.098 1.00 58.84 ? 25 TYR A N 1 ATOM 198 C CA . TYR A 1 48 ? -19.878 30.472 3.904 1.00 63.98 ? 25 TYR A CA 1 ATOM 199 C C . TYR A 1 48 ? -18.699 30.795 4.818 1.00 72.17 ? 25 TYR A C 1 ATOM 200 O O . TYR A 1 48 ? -17.632 30.191 4.702 1.00 84.97 ? 25 TYR A O 1 ATOM 201 C CB . TYR A 1 48 ? -19.429 30.491 2.440 1.00 60.26 ? 25 TYR A CB 1 ATOM 202 C CG . TYR A 1 48 ? -20.500 30.034 1.477 1.00 61.13 ? 25 TYR A CG 1 ATOM 203 C CD1 . TYR A 1 48 ? -20.694 28.684 1.216 1.00 63.85 ? 25 TYR A CD1 1 ATOM 204 C CD2 . TYR A 1 48 ? -21.322 30.951 0.833 1.00 56.13 ? 25 TYR A CD2 1 ATOM 205 C CE1 . TYR A 1 48 ? -21.672 28.258 0.340 1.00 68.96 ? 25 TYR A CE1 1 ATOM 206 C CE2 . TYR A 1 48 ? -22.304 30.535 -0.045 1.00 65.62 ? 25 TYR A CE2 1 ATOM 207 C CZ . TYR A 1 48 ? -22.474 29.187 -0.288 1.00 70.14 ? 25 TYR A CZ 1 ATOM 208 O OH . TYR A 1 48 ? -23.449 28.762 -1.161 1.00 76.37 ? 25 TYR A OH 1 ATOM 209 N N . ASN A 1 49 ? -18.893 31.746 5.725 1.00 71.17 ? 26 ASN A N 1 ATOM 210 C CA . ASN A 1 49 ? -17.850 32.133 6.667 1.00 64.65 ? 26 ASN A CA 1 ATOM 211 C C . ASN A 1 49 ? -18.246 31.748 8.088 1.00 64.72 ? 26 ASN A C 1 ATOM 212 O O . ASN A 1 49 ? -19.017 32.449 8.738 1.00 65.13 ? 26 ASN A O 1 ATOM 213 C CB . ASN A 1 49 ? -17.588 33.640 6.581 1.00 57.31 ? 26 ASN A CB 1 ATOM 214 C CG . ASN A 1 49 ? -16.291 34.052 7.254 1.00 62.54 ? 26 ASN A CG 1 ATOM 215 O OD1 . ASN A 1 49 ? -15.936 35.231 7.261 1.00 66.69 ? 26 ASN A OD1 1 ATOM 216 N ND2 . ASN A 1 49 ? -15.569 33.086 7.804 1.00 63.78 ? 26 ASN A ND2 1 ATOM 217 N N . ARG A 1 50 ? -17.710 30.630 8.562 1.00 67.48 ? 27 ARG A N 1 ATOM 218 C CA . ARG A 1 50 ? -18.050 30.112 9.881 1.00 61.98 ? 27 ARG A CA 1 ATOM 219 C C . ARG A 1 50 ? -17.469 30.985 10.991 1.00 60.73 ? 27 ARG A C 1 ATOM 220 O O . ARG A 1 50 ? -17.887 30.899 12.146 1.00 62.33 ? 27 ARG A O 1 ATOM 221 C CB . ARG A 1 50 ? -17.553 28.673 10.024 1.00 75.51 ? 27 ARG A CB 1 ATOM 222 C CG . ARG A 1 50 ? -18.454 27.779 10.856 1.00 91.81 ? 27 ARG A CG 1 ATOM 223 C CD . ARG A 1 50 ? -18.041 26.321 10.735 1.00 104.74 ? 27 ARG A CD 1 ATOM 224 N NE . ARG A 1 50 ? -19.014 25.423 11.352 1.00 115.94 ? 27 ARG A NE 1 ATOM 225 C CZ . ARG A 1 50 ? -20.073 24.923 10.722 1.00 123.53 ? 27 ARG A CZ 1 ATOM 226 N NH1 . ARG A 1 50 ? -20.905 24.112 11.361 1.00 128.55 ? 27 ARG A NH1 1 ATOM 227 N NH2 . ARG A 1 50 ? -20.302 25.234 9.454 1.00 124.50 ? 27 ARG A NH2 1 ATOM 228 N N . GLY A 1 51 ? -16.506 31.828 10.631 1.00 56.03 ? 28 GLY A N 1 ATOM 229 C CA . GLY A 1 51 ? -15.854 32.699 11.591 1.00 57.14 ? 28 GLY A CA 1 ATOM 230 C C . GLY A 1 51 ? -16.610 33.990 11.844 1.00 66.02 ? 28 GLY A C 1 ATOM 231 O O . GLY A 1 51 ? -16.381 34.664 12.848 1.00 68.97 ? 28 GLY A O 1 ATOM 232 N N . THR A 1 52 ? -17.514 34.339 10.934 1.00 58.00 ? 29 THR A N 1 ATOM 233 C CA . THR A 1 52 ? -18.272 35.575 11.075 1.00 61.99 ? 29 THR A CA 1 ATOM 234 C C . THR A 1 52 ? -19.652 35.321 11.681 1.00 57.28 ? 29 THR A C 1 ATOM 235 O O . THR A 1 52 ? -20.215 34.233 11.551 1.00 53.15 ? 29 THR A O 1 ATOM 236 C CB . THR A 1 52 ? -18.408 36.329 9.734 1.00 57.22 ? 29 THR A CB 1 ATOM 237 O OG1 . THR A 1 52 ? -18.761 37.695 9.986 1.00 60.14 ? 29 THR A OG1 1 ATOM 238 C CG2 . THR A 1 52 ? -19.471 35.687 8.853 1.00 53.18 ? 29 THR A CG2 1 ATOM 239 N N . SER A 1 53 ? -20.185 36.335 12.352 1.00 58.41 ? 30 SER A N 1 ATOM 240 C CA . SER A 1 53 ? -21.461 36.213 13.037 1.00 60.25 ? 30 SER A CA 1 ATOM 241 C C . SER A 1 53 ? -22.633 36.335 12.070 1.00 54.98 ? 30 SER A C 1 ATOM 242 O O . SER A 1 53 ? -22.541 37.017 11.049 1.00 49.70 ? 30 SER A O 1 ATOM 243 C CB . SER A 1 53 ? -21.576 37.275 14.133 1.00 56.86 ? 30 SER A CB 1 ATOM 244 O OG . SER A 1 53 ? -22.845 37.230 14.759 1.00 67.61 ? 30 SER A OG 1 ATOM 245 N N . ALA A 1 54 ? -23.730 35.661 12.396 1.00 47.38 ? 31 ALA A N 1 ATOM 246 C CA . ALA A 1 54 ? -24.971 35.806 11.644 1.00 43.05 ? 31 ALA A CA 1 ATOM 247 C C . ALA A 1 54 ? -25.975 36.609 12.460 1.00 42.14 ? 31 ALA A C 1 ATOM 248 O O . ALA A 1 54 ? -27.032 36.991 11.961 1.00 46.96 ? 31 ALA A O 1 ATOM 249 C CB . ALA A 1 54 ? -25.542 34.443 11.288 1.00 39.61 ? 31 ALA A CB 1 ATOM 250 N N . VAL A 1 55 ? -25.635 36.862 13.720 1.00 42.88 ? 32 VAL A N 1 ATOM 251 C CA . VAL A 1 55 ? -26.515 37.592 14.625 1.00 43.11 ? 32 VAL A CA 1 ATOM 252 C C . VAL A 1 55 ? -26.721 39.035 14.174 1.00 42.30 ? 32 VAL A C 1 ATOM 253 O O . VAL A 1 55 ? -27.854 39.491 14.015 1.00 38.20 ? 32 VAL A O 1 ATOM 254 C CB . VAL A 1 55 ? -25.962 37.585 16.059 1.00 41.49 ? 32 VAL A CB 1 ATOM 255 C CG1 . VAL A 1 55 ? -26.829 38.447 16.966 1.00 39.80 ? 32 VAL A CG1 1 ATOM 256 C CG2 . VAL A 1 55 ? -25.873 36.156 16.582 1.00 36.86 ? 32 VAL A CG2 1 ATOM 257 N N . ASN A 1 56 ? -25.617 39.749 13.975 1.00 39.92 ? 33 ASN A N 1 ATOM 258 C CA . ASN A 1 56 ? -25.668 41.130 13.508 1.00 40.30 ? 33 ASN A CA 1 ATOM 259 C C . ASN A 1 56 ? -26.317 41.245 12.130 1.00 38.93 ? 33 ASN A C 1 ATOM 260 O O . ASN A 1 56 ? -27.071 42.180 11.859 1.00 45.40 ? 33 ASN A O 1 ATOM 261 C CB . ASN A 1 56 ? -24.261 41.730 13.475 1.00 38.91 ? 33 ASN A CB 1 ATOM 262 C CG . ASN A 1 56 ? -23.267 40.849 12.739 1.00 52.97 ? 33 ASN A CG 1 ATOM 263 O OD1 . ASN A 1 56 ? -23.623 39.792 12.212 1.00 52.21 ? 33 ASN A OD1 1 ATOM 264 N ND2 . ASN A 1 56 ? -22.012 41.285 12.694 1.00 49.19 ? 33 ASN A ND2 1 ATOM 265 N N . VAL A 1 57 ? -26.017 40.280 11.270 1.00 33.11 ? 34 VAL A N 1 ATOM 266 C CA . VAL A 1 57 ? -26.527 40.261 9.908 1.00 32.67 ? 34 VAL A CA 1 ATOM 267 C C . VAL A 1 57 ? -28.047 40.103 9.887 1.00 43.39 ? 34 VAL A C 1 ATOM 268 O O . VAL A 1 57 ? -28.753 40.872 9.230 1.00 45.56 ? 34 VAL A O 1 ATOM 269 C CB . VAL A 1 57 ? -25.870 39.123 9.101 1.00 44.21 ? 34 VAL A CB 1 ATOM 270 C CG1 . VAL A 1 57 ? -26.570 38.928 7.769 1.00 44.22 ? 34 VAL A CG1 1 ATOM 271 C CG2 . VAL A 1 57 ? -24.385 39.405 8.907 1.00 41.03 ? 34 VAL A CG2 1 ATOM 272 N N . VAL A 1 58 ? -28.544 39.109 10.617 1.00 33.51 ? 35 VAL A N 1 ATOM 273 C CA . VAL A 1 58 ? -29.976 38.836 10.672 1.00 36.16 ? 35 VAL A CA 1 ATOM 274 C C . VAL A 1 58 ? -30.730 39.982 11.350 1.00 38.82 ? 35 VAL A C 1 ATOM 275 O O . VAL A 1 58 ? -31.804 40.377 10.896 1.00 36.87 ? 35 VAL A O 1 ATOM 276 C CB . VAL A 1 58 ? -30.274 37.483 11.370 1.00 40.09 ? 35 VAL A CB 1 ATOM 277 C CG1 . VAL A 1 58 ? -31.756 37.344 11.685 1.00 35.01 ? 35 VAL A CG1 1 ATOM 278 C CG2 . VAL A 1 58 ? -29.800 36.323 10.502 1.00 37.27 ? 35 VAL A CG2 1 ATOM 279 N N . LEU A 1 59 ? -30.158 40.520 12.424 1.00 35.91 ? 36 LEU A N 1 ATOM 280 C CA . LEU A 1 59 ? -30.724 41.690 13.093 1.00 41.49 ? 36 LEU A CA 1 ATOM 281 C C . LEU A 1 59 ? -30.904 42.843 12.111 1.00 39.50 ? 36 LEU A C 1 ATOM 282 O O . LEU A 1 59 ? -31.960 43.469 12.059 1.00 40.32 ? 36 LEU A O 1 ATOM 283 C CB . LEU A 1 59 ? -29.828 42.137 14.251 1.00 37.67 ? 36 LEU A CB 1 ATOM 284 C CG . LEU A 1 59 ? -30.125 43.508 14.871 1.00 38.59 ? 36 LEU A CG 1 ATOM 285 C CD1 . LEU A 1 59 ? -31.563 43.601 15.359 1.00 33.57 ? 36 LEU A CD1 1 ATOM 286 C CD2 . LEU A 1 59 ? -29.160 43.806 16.010 1.00 35.06 ? 36 LEU A CD2 1 ATOM 287 N N . SER A 1 60 ? -29.859 43.106 11.335 1.00 35.98 ? 37 SER A N 1 ATOM 288 C CA . SER A 1 60 ? -29.865 44.177 10.350 1.00 36.27 ? 37 SER A CA 1 ATOM 289 C C . SER A 1 60 ? -30.976 43.987 9.320 1.00 34.50 ? 37 SER A C 1 ATOM 290 O O . SER A 1 60 ? -31.711 44.922 9.001 1.00 37.34 ? 37 SER A O 1 ATOM 291 C CB . SER A 1 60 ? -28.505 44.233 9.649 1.00 33.93 ? 37 SER A CB 1 ATOM 292 O OG . SER A 1 60 ? -28.515 45.149 8.572 1.00 47.20 ? 37 SER A OG 1 ATOM 293 N N . LEU A 1 61 ? -31.094 42.767 8.809 1.00 39.80 ? 38 LEU A N 1 ATOM 294 C CA . LEU A 1 61 ? -32.079 42.445 7.782 1.00 46.82 ? 38 LEU A CA 1 ATOM 295 C C . LEU A 1 61 ? -33.517 42.514 8.291 1.00 45.02 ? 38 LEU A C 1 ATOM 296 O O . LEU A 1 61 ? -34.386 43.095 7.638 1.00 43.55 ? 38 LEU A O 1 ATOM 297 C CB . LEU A 1 61 ? -31.791 41.061 7.196 1.00 47.25 ? 38 LEU A CB 1 ATOM 298 C CG . LEU A 1 61 ? -30.492 40.985 6.391 1.00 44.31 ? 38 LEU A CG 1 ATOM 299 C CD1 . LEU A 1 61 ? -30.113 39.546 6.091 1.00 41.86 ? 38 LEU A CD1 1 ATOM 300 C CD2 . LEU A 1 61 ? -30.628 41.785 5.105 1.00 35.55 ? 38 LEU A CD2 1 ATOM 301 N N . LYS A 1 62 ? -33.767 41.919 9.453 1.00 42.37 ? 39 LYS A N 1 ATOM 302 C CA . LYS A 1 62 ? -35.114 41.896 10.018 1.00 52.13 ? 39 LYS A CA 1 ATOM 303 C C . LYS A 1 62 ? -35.588 43.310 10.340 1.00 51.72 ? 39 LYS A C 1 ATOM 304 O O . LYS A 1 62 ? -36.779 43.615 10.259 1.00 52.06 ? 39 LYS A O 1 ATOM 305 C CB . LYS A 1 62 ? -35.166 41.003 11.263 1.00 50.43 ? 39 LYS A CB 1 ATOM 306 C CG . LYS A 1 62 ? -34.851 39.538 10.980 1.00 58.07 ? 39 LYS A CG 1 ATOM 307 C CD . LYS A 1 62 ? -35.945 38.610 11.484 1.00 65.29 ? 39 LYS A CD 1 ATOM 308 C CE . LYS A 1 62 ? -36.041 38.624 13.000 1.00 68.22 ? 39 LYS A CE 1 ATOM 309 N NZ . LYS A 1 62 ? -37.105 37.699 13.483 1.00 78.05 ? 39 LYS A NZ 1 ATOM 310 N N . LEU A 1 63 ? -34.638 44.173 10.680 1.00 50.85 ? 40 LEU A N 1 ATOM 311 C CA . LEU A 1 63 ? -34.930 45.556 11.025 1.00 49.87 ? 40 LEU A CA 1 ATOM 312 C C . LEU A 1 63 ? -35.485 46.345 9.837 1.00 46.91 ? 40 LEU A C 1 ATOM 313 O O . LEU A 1 63 ? -36.262 47.284 10.014 1.00 45.12 ? 40 LEU A O 1 ATOM 314 C CB . LEU A 1 63 ? -33.668 46.226 11.563 1.00 56.99 ? 40 LEU A CB 1 ATOM 315 C CG . LEU A 1 63 ? -33.869 47.430 12.476 1.00 59.44 ? 40 LEU A CG 1 ATOM 316 C CD1 . LEU A 1 63 ? -34.864 47.105 13.579 1.00 58.74 ? 40 LEU A CD1 1 ATOM 317 C CD2 . LEU A 1 63 ? -32.532 47.830 13.061 1.00 52.11 ? 40 LEU A CD2 1 ATOM 318 N N . VAL A 1 64 ? -35.087 45.960 8.629 1.00 43.25 ? 41 VAL A N 1 ATOM 319 C CA . VAL A 1 64 ? -35.588 46.611 7.422 1.00 38.60 ? 41 VAL A CA 1 ATOM 320 C C . VAL A 1 64 ? -36.621 45.742 6.698 1.00 38.78 ? 41 VAL A C 1 ATOM 321 O O . VAL A 1 64 ? -36.898 45.939 5.515 1.00 49.95 ? 41 VAL A O 1 ATOM 322 C CB . VAL A 1 64 ? -34.440 47.005 6.466 1.00 38.46 ? 41 VAL A CB 1 ATOM 323 C CG1 . VAL A 1 64 ? -33.469 47.938 7.174 1.00 40.12 ? 41 VAL A CG1 1 ATOM 324 C CG2 . VAL A 1 64 ? -33.711 45.773 5.960 1.00 29.91 ? 41 VAL A CG2 1 ATOM 325 N N . GLY A 1 65 ? -37.191 44.784 7.421 1.00 43.26 ? 42 GLY A N 1 ATOM 326 C CA . GLY A 1 65 ? -38.250 43.950 6.882 1.00 45.40 ? 42 GLY A CA 1 ATOM 327 C C . GLY A 1 65 ? -37.749 42.962 5.851 1.00 52.46 ? 42 GLY A C 1 ATOM 328 O O . GLY A 1 65 ? -38.407 42.704 4.846 1.00 60.02 ? 42 GLY A O 1 ATOM 329 N N . ILE A 1 66 ? -36.567 42.412 6.095 1.00 50.03 ? 43 ILE A N 1 ATOM 330 C CA . ILE A 1 66 ? -36.005 41.413 5.201 1.00 44.57 ? 43 ILE A CA 1 ATOM 331 C C . ILE A 1 66 ? -35.693 40.127 5.955 1.00 50.38 ? 43 ILE A C 1 ATOM 332 O O . ILE A 1 66 ? -35.002 40.141 6.974 1.00 51.81 ? 43 ILE A O 1 ATOM 333 C CB . ILE A 1 66 ? -34.726 41.915 4.520 1.00 47.48 ? 43 ILE A CB 1 ATOM 334 C CG1 . ILE A 1 66 ? -35.031 43.111 3.618 1.00 47.65 ? 43 ILE A CG1 1 ATOM 335 C CG2 . ILE A 1 66 ? -34.091 40.801 3.708 1.00 46.81 ? 43 ILE A CG2 1 ATOM 336 C CD1 . ILE A 1 66 ? -33.809 43.654 2.906 1.00 49.25 ? 43 ILE A CD1 1 ATOM 337 N N . GLN A 1 67 ? -36.216 39.014 5.456 1.00 41.47 ? 44 GLN A N 1 ATOM 338 C CA . GLN A 1 67 ? -35.927 37.717 6.046 1.00 49.26 ? 44 GLN A CA 1 ATOM 339 C C . GLN A 1 67 ? -35.108 36.876 5.079 1.00 37.90 ? 44 GLN A C 1 ATOM 340 O O . GLN A 1 67 ? -35.470 36.731 3.917 1.00 44.46 ? 44 GLN A O 1 ATOM 341 C CB . GLN A 1 67 ? -37.222 37.001 6.424 1.00 52.20 ? 44 GLN A CB 1 ATOM 342 C CG . GLN A 1 67 ? -38.099 37.799 7.374 1.00 60.24 ? 44 GLN A CG 1 ATOM 343 C CD . GLN A 1 67 ? -39.357 37.056 7.772 1.00 69.20 ? 44 GLN A CD 1 ATOM 344 O OE1 . GLN A 1 67 ? -40.421 37.256 7.186 1.00 75.55 ? 44 GLN A OE1 1 ATOM 345 N NE2 . GLN A 1 67 ? -39.241 36.191 8.774 1.00 65.74 ? 44 GLN A NE2 1 ATOM 346 N N . ILE A 1 68 ? -33.986 36.352 5.556 1.00 45.65 ? 45 ILE A N 1 ATOM 347 C CA . ILE A 1 68 ? -33.148 35.474 4.751 1.00 43.95 ? 45 ILE A CA 1 ATOM 348 C C . ILE A 1 68 ? -32.988 34.149 5.477 1.00 44.95 ? 45 ILE A C 1 ATOM 349 O O . ILE A 1 68 ? -32.318 34.073 6.507 1.00 51.30 ? 45 ILE A O 1 ATOM 350 C CB . ILE A 1 68 ? -31.761 36.087 4.489 1.00 48.55 ? 45 ILE A CB 1 ATOM 351 C CG1 . ILE A 1 68 ? -31.900 37.416 3.744 1.00 52.06 ? 45 ILE A CG1 1 ATOM 352 C CG2 . ILE A 1 68 ? -30.895 35.120 3.694 1.00 40.12 ? 45 ILE A CG2 1 ATOM 353 C CD1 . ILE A 1 68 ? -32.583 37.292 2.399 1.00 55.56 ? 45 ILE A CD1 1 ATOM 354 N N . GLN A 1 69 ? -33.611 33.113 4.929 1.00 43.75 ? 46 GLN A N 1 ATOM 355 C CA . GLN A 1 69 ? -33.689 31.811 5.584 1.00 48.65 ? 46 GLN A CA 1 ATOM 356 C C . GLN A 1 69 ? -32.333 31.213 5.951 1.00 53.90 ? 46 GLN A C 1 ATOM 357 O O . GLN A 1 69 ? -32.130 30.788 7.088 1.00 50.03 ? 46 GLN A O 1 ATOM 358 C CB . GLN A 1 69 ? -34.473 30.825 4.719 1.00 46.76 ? 46 GLN A CB 1 ATOM 359 C CG . GLN A 1 69 ? -34.693 29.478 5.381 1.00 58.88 ? 46 GLN A CG 1 ATOM 360 C CD . GLN A 1 69 ? -35.510 29.590 6.655 1.00 63.96 ? 46 GLN A CD 1 ATOM 361 O OE1 . GLN A 1 69 ? -36.324 30.502 6.806 1.00 59.02 ? 46 GLN A OE1 1 ATOM 362 N NE2 . GLN A 1 69 ? -35.289 28.666 7.583 1.00 60.65 ? 46 GLN A NE2 1 ATOM 363 N N . THR A 1 70 ? -31.416 31.175 4.986 1.00 43.52 ? 47 THR A N 1 ATOM 364 C CA . THR A 1 70 ? -30.099 30.580 5.202 1.00 43.68 ? 47 THR A CA 1 ATOM 365 C C . THR A 1 70 ? -29.356 31.250 6.354 1.00 45.46 ? 47 THR A C 1 ATOM 366 O O . THR A 1 70 ? -28.784 30.576 7.210 1.00 55.85 ? 47 THR A O 1 ATOM 367 C CB . THR A 1 70 ? -29.227 30.653 3.936 1.00 43.23 ? 47 THR A CB 1 ATOM 368 O OG1 . THR A 1 70 ? -29.228 31.994 3.432 1.00 39.48 ? 47 THR A OG1 1 ATOM 369 C CG2 . THR A 1 70 ? -29.760 29.715 2.867 1.00 43.70 ? 47 THR A CG2 1 ATOM 370 N N . LEU A 1 71 ? -29.375 32.578 6.369 1.00 45.38 ? 48 LEU A N 1 ATOM 371 C CA . LEU A 1 71 ? -28.735 33.342 7.432 1.00 47.13 ? 48 LEU A CA 1 ATOM 372 C C . LEU A 1 71 ? -29.471 33.156 8.754 1.00 41.18 ? 48 LEU A C 1 ATOM 373 O O . LEU A 1 71 ? -28.854 33.099 9.818 1.00 41.79 ? 48 LEU A O 1 ATOM 374 C CB . LEU A 1 71 ? -28.668 34.825 7.057 1.00 42.61 ? 48 LEU A CB 1 ATOM 375 C CG . LEU A 1 71 ? -27.730 35.155 5.894 1.00 48.07 ? 48 LEU A CG 1 ATOM 376 C CD1 . LEU A 1 71 ? -27.930 36.584 5.414 1.00 39.36 ? 48 LEU A CD1 1 ATOM 377 C CD2 . LEU A 1 71 ? -26.278 34.923 6.302 1.00 40.98 ? 48 LEU A CD2 1 ATOM 378 N N . MET A 1 72 ? -30.793 33.060 8.679 1.00 42.73 ? 49 MET A N 1 ATOM 379 C CA . MET A 1 72 ? -31.611 32.821 9.860 1.00 49.63 ? 49 MET A CA 1 ATOM 380 C C . MET A 1 72 ? -31.253 31.482 10.507 1.00 52.31 ? 49 MET A C 1 ATOM 381 O O . MET A 1 72 ? -31.106 31.391 11.727 1.00 41.00 ? 49 MET A O 1 ATOM 382 C CB . MET A 1 72 ? -33.094 32.853 9.491 1.00 50.83 ? 49 MET A CB 1 ATOM 383 C CG . MET A 1 72 ? -34.019 32.471 10.629 1.00 67.53 ? 49 MET A CG 1 ATOM 384 S SD . MET A 1 72 ? -34.003 33.699 11.944 1.00 78.42 ? 49 MET A SD 1 ATOM 385 C CE . MET A 1 72 ? -34.623 35.125 11.055 1.00 89.76 ? 49 MET A CE 1 ATOM 386 N N . GLN A 1 73 ? -31.106 30.451 9.680 1.00 50.60 ? 50 GLN A N 1 ATOM 387 C CA . GLN A 1 73 ? -30.723 29.123 10.153 1.00 53.76 ? 50 GLN A CA 1 ATOM 388 C C . GLN A 1 73 ? -29.325 29.138 10.756 1.00 52.97 ? 50 GLN A C 1 ATOM 389 O O . GLN A 1 73 ? -29.068 28.487 11.769 1.00 50.22 ? 50 GLN A O 1 ATOM 390 C CB . GLN A 1 73 ? -30.781 28.106 9.011 1.00 44.83 ? 50 GLN A CB 1 ATOM 391 C CG . GLN A 1 73 ? -32.182 27.834 8.502 1.00 52.49 ? 50 GLN A CG 1 ATOM 392 C CD . GLN A 1 73 ? -32.196 27.069 7.192 1.00 65.72 ? 50 GLN A CD 1 ATOM 393 O OE1 . GLN A 1 73 ? -33.259 26.790 6.639 1.00 79.51 ? 50 GLN A OE1 1 ATOM 394 N NE2 . GLN A 1 73 ? -31.015 26.729 6.686 1.00 61.52 ? 50 GLN A NE2 1 ATOM 395 N N . LYS A 1 74 ? -28.422 29.880 10.124 1.00 47.32 ? 51 LYS A N 1 ATOM 396 C CA . LYS A 1 74 ? -27.062 29.995 10.627 1.00 55.71 ? 51 LYS A CA 1 ATOM 397 C C . LYS A 1 74 ? -27.052 30.647 12.003 1.00 55.49 ? 51 LYS A C 1 ATOM 398 O O . LYS A 1 74 ? -26.326 30.214 12.896 1.00 55.54 ? 51 LYS A O 1 ATOM 399 C CB . LYS A 1 74 ? -26.186 30.799 9.663 1.00 53.42 ? 51 LYS A CB 1 ATOM 400 C CG . LYS A 1 74 ? -24.743 30.937 10.133 1.00 53.91 ? 51 LYS A CG 1 ATOM 401 C CD . LYS A 1 74 ? -23.921 31.809 9.201 1.00 50.90 ? 51 LYS A CD 1 ATOM 402 C CE . LYS A 1 74 ? -22.504 31.985 9.730 1.00 55.97 ? 51 LYS A CE 1 ATOM 403 N NZ . LYS A 1 74 ? -21.731 32.988 8.946 1.00 61.00 ? 51 LYS A NZ 1 ATOM 404 N N . MET A 1 75 ? -27.866 31.686 12.171 1.00 47.11 ? 52 MET A N 1 ATOM 405 C CA . MET A 1 75 ? -27.886 32.427 13.426 1.00 48.92 ? 52 MET A CA 1 ATOM 406 C C . MET A 1 75 ? -28.408 31.571 14.570 1.00 47.79 ? 52 MET A C 1 ATOM 407 O O . MET A 1 75 ? -27.849 31.582 15.666 1.00 54.15 ? 52 MET A O 1 ATOM 408 C CB . MET A 1 75 ? -28.723 33.700 13.310 1.00 46.06 ? 52 MET A CB 1 ATOM 409 C CG . MET A 1 75 ? -28.720 34.529 14.587 1.00 44.13 ? 52 MET A CG 1 ATOM 410 S SD . MET A 1 75 ? -29.985 35.811 14.645 1.00 48.69 ? 52 MET A SD 1 ATOM 411 C CE . MET A 1 75 ? -31.481 34.828 14.591 1.00 44.74 ? 52 MET A CE 1 ATOM 412 N N . ILE A 1 76 ? -29.483 30.834 14.308 1.00 47.04 ? 53 ILE A N 1 ATOM 413 C CA . ILE A 1 76 ? -30.081 29.962 15.312 1.00 48.68 ? 53 ILE A CA 1 ATOM 414 C C . ILE A 1 76 ? -29.076 28.909 15.760 1.00 53.36 ? 53 ILE A C 1 ATOM 415 O O . ILE A 1 76 ? -28.946 28.625 16.952 1.00 55.23 ? 53 ILE A O 1 ATOM 416 C CB . ILE A 1 76 ? -31.355 29.276 14.780 1.00 48.86 ? 53 ILE A CB 1 ATOM 417 C CG1 . ILE A 1 76 ? -32.419 30.320 14.442 1.00 46.78 ? 53 ILE A CG1 1 ATOM 418 C CG2 . ILE A 1 76 ? -31.899 28.282 15.800 1.00 47.17 ? 53 ILE A CG2 1 ATOM 419 C CD1 . ILE A 1 76 ? -32.827 31.181 15.620 1.00 49.34 ? 53 ILE A CD1 1 ATOM 420 N N . GLN A 1 77 ? -28.357 28.345 14.795 1.00 56.06 ? 54 GLN A N 1 ATOM 421 C CA . GLN A 1 77 ? -27.321 27.361 15.075 1.00 57.79 ? 54 GLN A CA 1 ATOM 422 C C . GLN A 1 77 ? -26.231 27.958 15.965 1.00 54.17 ? 54 GLN A C 1 ATOM 423 O O . GLN A 1 77 ? -25.779 27.320 16.914 1.00 60.72 ? 54 GLN A O 1 ATOM 424 C CB . GLN A 1 77 ? -26.717 26.837 13.771 1.00 73.56 ? 54 GLN A CB 1 ATOM 425 C CG . GLN A 1 77 ? -25.622 25.801 13.961 1.00 95.06 ? 54 GLN A CG 1 ATOM 426 C CD . GLN A 1 77 ? -24.998 25.367 12.650 1.00 110.40 ? 54 GLN A CD 1 ATOM 427 O OE1 . GLN A 1 77 ? -25.380 25.842 11.580 1.00 114.98 ? 54 GLN A OE1 1 ATOM 428 N NE2 . GLN A 1 77 ? -24.030 24.460 12.726 1.00 115.01 ? 54 GLN A NE2 1 ATOM 429 N N . GLN A 1 78 ? -25.816 29.183 15.659 1.00 48.35 ? 55 GLN A N 1 ATOM 430 C CA . GLN A 1 78 ? -24.821 29.871 16.476 1.00 56.77 ? 55 GLN A CA 1 ATOM 431 C C . GLN A 1 78 ? -25.352 30.140 17.880 1.00 54.23 ? 55 GLN A C 1 ATOM 432 O O . GLN A 1 78 ? -24.642 29.951 18.867 1.00 53.46 ? 55 GLN A O 1 ATOM 433 C CB . GLN A 1 78 ? -24.390 31.187 15.824 1.00 53.29 ? 55 GLN A CB 1 ATOM 434 C CG . GLN A 1 78 ? -23.550 31.022 14.569 1.00 62.76 ? 55 GLN A CG 1 ATOM 435 C CD . GLN A 1 78 ? -23.105 32.353 13.989 1.00 68.74 ? 55 GLN A CD 1 ATOM 436 O OE1 . GLN A 1 78 ? -23.647 33.406 14.330 1.00 60.62 ? 55 GLN A OE1 1 ATOM 437 N NE2 . GLN A 1 78 ? -22.111 32.311 13.110 1.00 72.65 ? 55 GLN A NE2 1 ATOM 438 N N . ILE A 1 79 ? -26.602 30.584 17.961 1.00 55.50 ? 56 ILE A N 1 ATOM 439 C CA . ILE A 1 79 ? -27.218 30.903 19.243 1.00 54.85 ? 56 ILE A CA 1 ATOM 440 C C . ILE A 1 79 ? -27.359 29.655 20.110 1.00 55.87 ? 56 ILE A C 1 ATOM 441 O O . ILE A 1 79 ? -26.991 29.663 21.284 1.00 53.08 ? 56 ILE A O 1 ATOM 442 C CB . ILE A 1 79 ? -28.589 31.589 19.061 1.00 53.27 ? 56 ILE A CB 1 ATOM 443 C CG1 . ILE A 1 79 ? -28.403 32.986 18.461 1.00 51.04 ? 56 ILE A CG1 1 ATOM 444 C CG2 . ILE A 1 79 ? -29.325 31.679 20.391 1.00 42.91 ? 56 ILE A CG2 1 ATOM 445 C CD1 . ILE A 1 79 ? -29.701 33.704 18.146 1.00 41.34 ? 56 ILE A CD1 1 ATOM 446 N N . LYS A 1 80 ? -27.877 28.581 19.522 1.00 53.89 ? 57 LYS A N 1 ATOM 447 C CA . LYS A 1 80 ? -28.042 27.328 20.249 1.00 61.14 ? 57 LYS A CA 1 ATOM 448 C C . LYS A 1 80 ? -26.698 26.764 20.699 1.00 62.25 ? 57 LYS A C 1 ATOM 449 O O . LYS A 1 80 ? -26.590 26.187 21.779 1.00 68.97 ? 57 LYS A O 1 ATOM 450 C CB . LYS A 1 80 ? -28.803 26.300 19.407 1.00 58.43 ? 57 LYS A CB 1 ATOM 451 C CG . LYS A 1 80 ? -30.293 26.588 19.277 1.00 59.17 ? 57 LYS A CG 1 ATOM 452 C CD . LYS A 1 80 ? -31.005 25.499 18.490 1.00 59.99 ? 57 LYS A CD 1 ATOM 453 C CE . LYS A 1 80 ? -32.509 25.735 18.452 1.00 63.81 ? 57 LYS A CE 1 ATOM 454 N NZ . LYS A 1 80 ? -33.208 24.715 17.620 1.00 67.82 ? 57 LYS A NZ 1 ATOM 455 N N . TYR A 1 81 ? -25.673 26.945 19.873 1.00 60.13 ? 58 TYR A N 1 ATOM 456 C CA . TYR A 1 81 ? -24.339 26.463 20.204 1.00 63.90 ? 58 TYR A CA 1 ATOM 457 C C . TYR A 1 81 ? -23.745 27.218 21.388 1.00 65.78 ? 58 TYR A C 1 ATOM 458 O O . TYR A 1 81 ? -23.274 26.609 22.348 1.00 69.51 ? 58 TYR A O 1 ATOM 459 C CB . TYR A 1 81 ? -23.409 26.569 18.995 1.00 69.60 ? 58 TYR A CB 1 ATOM 460 C CG . TYR A 1 81 ? -21.953 26.356 19.335 1.00 80.06 ? 58 TYR A CG 1 ATOM 461 C CD1 . TYR A 1 81 ? -21.469 25.091 19.644 1.00 85.15 ? 58 TYR A CD1 1 ATOM 462 C CD2 . TYR A 1 81 ? -21.061 27.420 19.347 1.00 81.64 ? 58 TYR A CD2 1 ATOM 463 C CE1 . TYR A 1 81 ? -20.137 24.893 19.957 1.00 90.28 ? 58 TYR A CE1 1 ATOM 464 C CE2 . TYR A 1 81 ? -19.729 27.232 19.659 1.00 89.01 ? 58 TYR A CE2 1 ATOM 465 C CZ . TYR A 1 81 ? -19.272 25.967 19.962 1.00 95.41 ? 58 TYR A CZ 1 ATOM 466 O OH . TYR A 1 81 ? -17.945 25.778 20.271 1.00 100.02 ? 58 TYR A OH 1 ATOM 467 N N . ASN A 1 82 ? -23.771 28.544 21.315 1.00 58.53 ? 59 ASN A N 1 ATOM 468 C CA . ASN A 1 82 ? -23.225 29.375 22.381 1.00 65.04 ? 59 ASN A CA 1 ATOM 469 C C . ASN A 1 82 ? -23.979 29.218 23.699 1.00 72.90 ? 59 ASN A C 1 ATOM 470 O O . ASN A 1 82 ? -23.372 29.189 24.767 1.00 78.06 ? 59 ASN A O 1 ATOM 471 C CB . ASN A 1 82 ? -23.186 30.846 21.960 1.00 64.97 ? 59 ASN A CB 1 ATOM 472 C CG . ASN A 1 82 ? -22.085 31.135 20.956 1.00 72.01 ? 59 ASN A CG 1 ATOM 473 O OD1 . ASN A 1 82 ? -20.928 31.328 21.328 1.00 75.29 ? 59 ASN A OD1 1 ATOM 474 N ND2 . ASN A 1 82 ? -22.441 31.169 19.676 1.00 72.48 ? 59 ASN A ND2 1 ATOM 475 N N . VAL A 1 83 ? -25.300 29.109 23.619 1.00 69.63 ? 60 VAL A N 1 ATOM 476 C CA . VAL A 1 83 ? -26.120 28.968 24.816 1.00 66.22 ? 60 VAL A CA 1 ATOM 477 C C . VAL A 1 83 ? -25.872 27.635 25.521 1.00 71.12 ? 60 VAL A C 1 ATOM 478 O O . VAL A 1 83 ? -25.773 27.580 26.748 1.00 74.93 ? 60 VAL A O 1 ATOM 479 C CB . VAL A 1 83 ? -27.625 29.128 24.493 1.00 65.35 ? 60 VAL A CB 1 ATOM 480 C CG1 . VAL A 1 83 ? -28.487 28.593 25.627 1.00 70.06 ? 60 VAL A CG1 1 ATOM 481 C CG2 . VAL A 1 83 ? -27.953 30.590 24.211 1.00 61.20 ? 60 VAL A CG2 1 ATOM 482 N N . LYS A 1 84 ? -25.741 26.568 24.740 1.00 71.38 ? 61 LYS A N 1 ATOM 483 C CA . LYS A 1 84 ? -25.666 25.226 25.303 1.00 83.66 ? 61 LYS A CA 1 ATOM 484 C C . LYS A 1 84 ? -24.273 24.825 25.787 1.00 86.88 ? 61 LYS A C 1 ATOM 485 O O . LYS A 1 84 ? -24.128 23.820 26.483 1.00 91.91 ? 61 LYS A O 1 ATOM 486 C CB . LYS A 1 84 ? -26.181 24.189 24.299 1.00 93.88 ? 61 LYS A CB 1 ATOM 487 C CG . LYS A 1 84 ? -25.141 23.723 23.290 1.00 103.14 ? 61 LYS A CG 1 ATOM 488 C CD . LYS A 1 84 ? -25.706 22.652 22.368 1.00 109.55 ? 61 LYS A CD 1 ATOM 489 C CE . LYS A 1 84 ? -24.616 22.017 21.518 1.00 111.61 ? 61 LYS A CE 1 ATOM 490 N NZ . LYS A 1 84 ? -23.606 21.302 22.348 1.00 111.20 ? 61 LYS A NZ 1 ATOM 491 N N . SER A 1 85 ? -23.250 25.596 25.432 1.00 85.43 ? 62 SER A N 1 ATOM 492 C CA . SER A 1 85 ? -21.888 25.182 25.761 1.00 83.36 ? 62 SER A CA 1 ATOM 493 C C . SER A 1 85 ? -20.847 26.298 25.848 1.00 77.22 ? 62 SER A C 1 ATOM 494 O O . SER A 1 85 ? -19.649 26.019 25.891 1.00 80.22 ? 62 SER A O 1 ATOM 495 C CB . SER A 1 85 ? -21.412 24.117 24.768 1.00 84.72 ? 62 SER A CB 1 ATOM 496 O OG . SER A 1 85 ? -21.426 24.617 23.442 1.00 77.85 ? 62 SER A OG 1 ATOM 497 N N . ARG A 1 86 ? -21.286 27.552 25.883 1.00 75.63 ? 63 ARG A N 1 ATOM 498 C CA . ARG A 1 86 ? -20.342 28.666 25.955 1.00 74.44 ? 63 ARG A CA 1 ATOM 499 C C . ARG A 1 86 ? -20.992 29.941 26.480 1.00 65.02 ? 63 ARG A C 1 ATOM 500 O O . ARG A 1 86 ? -20.428 31.030 26.355 1.00 69.77 ? 63 ARG A O 1 ATOM 501 C CB . ARG A 1 86 ? -19.725 28.933 24.579 1.00 81.84 ? 63 ARG A CB 1 ATOM 502 C CG . ARG A 1 86 ? -18.287 29.424 24.631 1.00 95.20 ? 63 ARG A CG 1 ATOM 503 C CD . ARG A 1 86 ? -17.866 30.054 23.314 1.00 100.10 ? 63 ARG A CD 1 ATOM 504 N NE . ARG A 1 86 ? -18.412 31.399 23.151 1.00 103.04 ? 63 ARG A NE 1 ATOM 505 C CZ . ARG A 1 86 ? -17.775 32.511 23.503 1.00 105.13 ? 63 ARG A CZ 1 ATOM 506 N NH1 . ARG A 1 86 ? -16.564 32.440 24.039 1.00 103.73 ? 63 ARG A NH1 1 ATOM 507 N NH2 . ARG A 1 86 ? -18.346 33.694 23.319 1.00 101.10 ? 63 ARG A NH2 1 ATOM 508 N N . LEU A 1 87 ? -22.175 29.798 27.068 1.00 59.05 ? 64 LEU A N 1 ATOM 509 C CA . LEU A 1 87 ? -22.970 30.939 27.513 1.00 62.06 ? 64 LEU A CA 1 ATOM 510 C C . LEU A 1 87 ? -22.232 31.806 28.530 1.00 67.62 ? 64 LEU A C 1 ATOM 511 O O . LEU A 1 87 ? -22.412 33.023 28.569 1.00 67.83 ? 64 LEU A O 1 ATOM 512 C CB . LEU A 1 87 ? -24.302 30.459 28.094 1.00 58.67 ? 64 LEU A CB 1 ATOM 513 C CG . LEU A 1 87 ? -25.318 31.530 28.498 1.00 63.93 ? 64 LEU A CG 1 ATOM 514 C CD1 . LEU A 1 87 ? -25.580 32.491 27.347 1.00 52.58 ? 64 LEU A CD1 1 ATOM 515 C CD2 . LEU A 1 87 ? -26.615 30.883 28.966 1.00 62.35 ? 64 LEU A CD2 1 ATOM 516 N N . SER A 1 88 ? -21.394 31.172 29.342 1.00 73.78 ? 65 SER A N 1 ATOM 517 C CA . SER A 1 88 ? -20.666 31.874 30.392 1.00 77.28 ? 65 SER A CA 1 ATOM 518 C C . SER A 1 88 ? -19.576 32.784 29.828 1.00 70.13 ? 65 SER A C 1 ATOM 519 O O . SER A 1 88 ? -19.229 33.798 30.435 1.00 71.54 ? 65 SER A O 1 ATOM 520 C CB . SER A 1 88 ? -20.063 30.872 31.379 1.00 84.13 ? 65 SER A CB 1 ATOM 521 O OG . SER A 1 88 ? -19.389 31.535 32.433 1.00 93.78 ? 65 SER A OG 1 ATOM 522 N N . ASP A 1 89 ? -19.043 32.421 28.665 1.00 62.49 ? 66 ASP A N 1 ATOM 523 C CA . ASP A 1 89 ? -17.970 33.189 28.039 1.00 69.72 ? 66 ASP A CA 1 ATOM 524 C C . ASP A 1 89 ? -18.485 34.264 27.079 1.00 70.67 ? 66 ASP A C 1 ATOM 525 O O . ASP A 1 89 ? -17.728 35.137 26.652 1.00 72.77 ? 66 ASP A O 1 ATOM 526 C CB . ASP A 1 89 ? -16.996 32.257 27.315 1.00 82.88 ? 66 ASP A CB 1 ATOM 527 C CG . ASP A 1 89 ? -16.251 31.342 28.267 1.00 95.65 ? 66 ASP A CG 1 ATOM 528 O OD1 . ASP A 1 89 ? -16.018 31.752 29.423 1.00 97.46 ? 66 ASP A OD1 1 ATOM 529 O OD2 . ASP A 1 89 ? -15.899 30.214 27.860 1.00 98.60 ? 66 ASP A OD2 1 ATOM 530 N N . VAL A 1 90 ? -19.769 34.198 26.741 1.00 62.71 ? 67 VAL A N 1 ATOM 531 C CA . VAL A 1 90 ? -20.376 35.173 25.841 1.00 55.61 ? 67 VAL A CA 1 ATOM 532 C C . VAL A 1 90 ? -20.408 36.556 26.485 1.00 48.34 ? 67 VAL A C 1 ATOM 533 O O . VAL A 1 90 ? -20.887 36.712 27.606 1.00 49.62 ? 67 VAL A O 1 ATOM 534 C CB . VAL A 1 90 ? -21.806 34.754 25.445 1.00 57.83 ? 67 VAL A CB 1 ATOM 535 C CG1 . VAL A 1 90 ? -22.511 35.878 24.707 1.00 57.38 ? 67 VAL A CG1 1 ATOM 536 C CG2 . VAL A 1 90 ? -21.771 33.492 24.597 1.00 56.60 ? 67 VAL A CG2 1 ATOM 537 N N . SER A 1 91 ? -19.889 37.559 25.781 1.00 40.17 ? 68 SER A N 1 ATOM 538 C CA . SER A 1 91 ? -19.841 38.909 26.334 1.00 42.97 ? 68 SER A CA 1 ATOM 539 C C . SER A 1 91 ? -21.244 39.487 26.440 1.00 48.59 ? 68 SER A C 1 ATOM 540 O O . SER A 1 91 ? -22.159 39.051 25.739 1.00 39.88 ? 68 SER A O 1 ATOM 541 C CB . SER A 1 91 ? -18.968 39.823 25.477 1.00 38.79 ? 68 SER A CB 1 ATOM 542 O OG . SER A 1 91 ? -19.690 40.305 24.356 1.00 49.62 ? 68 SER A OG 1 ATOM 543 N N . SER A 1 92 ? -21.408 40.469 27.321 1.00 48.17 ? 69 SER A N 1 ATOM 544 C CA . SER A 1 92 ? -22.699 41.118 27.512 1.00 43.04 ? 69 SER A CA 1 ATOM 545 C C . SER A 1 92 ? -23.235 41.680 26.194 1.00 40.10 ? 69 SER A C 1 ATOM 546 O O . SER A 1 92 ? -24.405 41.492 25.864 1.00 38.74 ? 69 SER A O 1 ATOM 547 C CB . SER A 1 92 ? -22.599 42.221 28.569 1.00 42.06 ? 69 SER A CB 1 ATOM 548 O OG . SER A 1 92 ? -21.648 43.205 28.200 1.00 42.82 ? 69 SER A OG 1 ATOM 549 N N . GLY A 1 93 ? -22.367 42.348 25.440 1.00 38.98 ? 70 GLY A N 1 ATOM 550 C CA . GLY A 1 93 ? -22.744 42.913 24.156 1.00 40.62 ? 70 GLY A CA 1 ATOM 551 C C . GLY A 1 93 ? -23.176 41.869 23.142 1.00 41.72 ? 70 GLY A C 1 ATOM 552 O O . GLY A 1 93 ? -24.087 42.106 22.349 1.00 43.15 ? 70 GLY A O 1 ATOM 553 N N . GLU A 1 94 ? -22.519 40.713 23.162 1.00 40.36 ? 71 GLU A N 1 ATOM 554 C CA . GLU A 1 94 ? -22.859 39.626 22.249 1.00 44.68 ? 71 GLU A CA 1 ATOM 555 C C . GLU A 1 94 ? -24.243 39.075 22.559 1.00 36.48 ? 71 GLU A C 1 ATOM 556 O O . GLU A 1 94 ? -25.021 38.779 21.654 1.00 41.50 ? 71 GLU A O 1 ATOM 557 C CB . GLU A 1 94 ? -21.824 38.501 22.330 1.00 51.16 ? 71 GLU A CB 1 ATOM 558 C CG . GLU A 1 94 ? -20.507 38.807 21.640 1.00 59.71 ? 71 GLU A CG 1 ATOM 559 C CD . GLU A 1 94 ? -19.480 37.708 21.837 1.00 60.59 ? 71 GLU A CD 1 ATOM 560 O OE1 . GLU A 1 94 ? -19.630 36.911 22.789 1.00 53.61 ? 71 GLU A OE1 1 ATOM 561 O OE2 . GLU A 1 94 ? -18.525 37.639 21.038 1.00 66.87 ? 71 GLU A OE2 1 ATOM 562 N N . LEU A 1 95 ? -24.540 38.940 23.846 1.00 34.24 ? 72 LEU A N 1 ATOM 563 C CA . LEU A 1 95 ? -25.842 38.462 24.283 1.00 34.69 ? 72 LEU A CA 1 ATOM 564 C C . LEU A 1 95 ? -26.919 39.498 23.979 1.00 38.80 ? 72 LEU A C 1 ATOM 565 O O . LEU A 1 95 ? -28.045 39.149 23.614 1.00 39.75 ? 72 LEU A O 1 ATOM 566 C CB . LEU A 1 95 ? -25.822 38.138 25.779 1.00 38.97 ? 72 LEU A CB 1 ATOM 567 C CG . LEU A 1 95 ? -27.141 37.637 26.365 1.00 48.67 ? 72 LEU A CG 1 ATOM 568 C CD1 . LEU A 1 95 ? -27.640 36.437 25.578 1.00 51.25 ? 72 LEU A CD1 1 ATOM 569 C CD2 . LEU A 1 95 ? -26.985 37.287 27.838 1.00 55.56 ? 72 LEU A CD2 1 ATOM 570 N N . ALA A 1 96 ? -26.567 40.772 24.134 1.00 39.16 ? 73 ALA A N 1 ATOM 571 C CA . ALA A 1 96 ? -27.480 41.865 23.816 1.00 43.21 ? 73 ALA A CA 1 ATOM 572 C C . ALA A 1 96 ? -27.916 41.801 22.353 1.00 39.65 ? 73 ALA A C 1 ATOM 573 O O . ALA A 1 96 ? -29.100 41.921 22.050 1.00 39.06 ? 73 ALA A O 1 ATOM 574 C CB . ALA A 1 96 ? -26.835 43.209 24.125 1.00 36.58 ? 73 ALA A CB 1 ATOM 575 N N . LEU A 1 97 ? -26.956 41.604 21.453 1.00 37.44 ? 74 LEU A N 1 ATOM 576 C CA . LEU A 1 97 ? -27.262 41.493 20.028 1.00 42.52 ? 74 LEU A CA 1 ATOM 577 C C . LEU A 1 97 ? -28.124 40.272 19.733 1.00 42.90 ? 74 LEU A C 1 ATOM 578 O O . LEU A 1 97 ? -28.992 40.314 18.863 1.00 42.43 ? 74 LEU A O 1 ATOM 579 C CB . LEU A 1 97 ? -25.981 41.440 19.194 1.00 36.45 ? 74 LEU A CB 1 ATOM 580 C CG . LEU A 1 97 ? -25.237 42.762 18.996 1.00 44.27 ? 74 LEU A CG 1 ATOM 581 C CD1 . LEU A 1 97 ? -23.934 42.529 18.251 1.00 42.67 ? 74 LEU A CD1 1 ATOM 582 C CD2 . LEU A 1 97 ? -26.106 43.767 18.252 1.00 37.40 ? 74 LEU A CD2 1 ATOM 583 N N . ILE A 1 98 ? -27.875 39.184 20.456 1.00 49.19 ? 75 ILE A N 1 ATOM 584 C CA . ILE A 1 98 ? -28.659 37.967 20.288 1.00 42.14 ? 75 ILE A CA 1 ATOM 585 C C . ILE A 1 98 ? -30.118 38.235 20.621 1.00 38.93 ? 75 ILE A C 1 ATOM 586 O O . ILE A 1 98 ? -31.017 37.880 19.859 1.00 42.49 ? 75 ILE A O 1 ATOM 587 C CB . ILE A 1 98 ? -28.123 36.822 21.163 1.00 40.74 ? 75 ILE A CB 1 ATOM 588 C CG1 . ILE A 1 98 ? -26.797 36.313 20.599 1.00 38.25 ? 75 ILE A CG1 1 ATOM 589 C CG2 . ILE A 1 98 ? -29.128 35.679 21.237 1.00 34.14 ? 75 ILE A CG2 1 ATOM 590 C CD1 . ILE A 1 98 ? -26.172 35.211 21.414 1.00 38.45 ? 75 ILE A CD1 1 ATOM 591 N N . ILE A 1 99 ? -30.342 38.886 21.757 1.00 40.10 ? 76 ILE A N 1 ATOM 592 C CA . ILE A 1 99 ? -31.687 39.223 22.196 1.00 45.48 ? 76 ILE A CA 1 ATOM 593 C C . ILE A 1 99 ? -32.366 40.161 21.198 1.00 48.02 ? 76 ILE A C 1 ATOM 594 O O . ILE A 1 99 ? -33.536 39.975 20.861 1.00 42.46 ? 76 ILE A O 1 ATOM 595 C CB . ILE A 1 99 ? -31.674 39.855 23.604 1.00 47.96 ? 76 ILE A CB 1 ATOM 596 C CG1 . ILE A 1 99 ? -31.114 38.854 24.621 1.00 51.52 ? 76 ILE A CG1 1 ATOM 597 C CG2 . ILE A 1 99 ? -33.071 40.312 24.003 1.00 46.18 ? 76 ILE A CG2 1 ATOM 598 C CD1 . ILE A 1 99 ? -30.987 39.394 26.031 1.00 45.48 ? 76 ILE A CD1 1 ATOM 599 N N . LEU A 1 100 ? -31.623 41.154 20.717 1.00 41.94 ? 77 LEU A N 1 ATOM 600 C CA . LEU A 1 100 ? -32.162 42.106 19.752 1.00 44.55 ? 77 LEU A CA 1 ATOM 601 C C . LEU A 1 100 ? -32.542 41.408 18.452 1.00 47.36 ? 77 LEU A C 1 ATOM 602 O O . LEU A 1 100 ? -33.631 41.621 17.924 1.00 52.84 ? 77 LEU A O 1 ATOM 603 C CB . LEU A 1 100 ? -31.166 43.233 19.472 1.00 31.69 ? 77 LEU A CB 1 ATOM 604 C CG . LEU A 1 100 ? -30.844 44.179 20.632 1.00 44.15 ? 77 LEU A CG 1 ATOM 605 C CD1 . LEU A 1 100 ? -29.739 45.146 20.231 1.00 42.21 ? 77 LEU A CD1 1 ATOM 606 C CD2 . LEU A 1 100 ? -32.085 44.933 21.090 1.00 40.00 ? 77 LEU A CD2 1 ATOM 607 N N . ALA A 1 101 ? -31.641 40.570 17.949 1.00 39.82 ? 78 ALA A N 1 ATOM 608 C CA . ALA A 1 101 ? -31.888 39.829 16.716 1.00 44.25 ? 78 ALA A CA 1 ATOM 609 C C . ALA A 1 101 ? -33.083 38.880 16.835 1.00 48.56 ? 78 ALA A C 1 ATOM 610 O O . ALA A 1 101 ? -33.848 38.718 15.888 1.00 52.41 ? 78 ALA A O 1 ATOM 611 C CB . ALA A 1 101 ? -30.643 39.061 16.300 1.00 34.39 ? 78 ALA A CB 1 ATOM 612 N N . LEU A 1 102 ? -33.241 38.259 18.000 1.00 46.49 ? 79 LEU A N 1 ATOM 613 C CA . LEU A 1 102 ? -34.322 37.300 18.204 1.00 47.70 ? 79 LEU A CA 1 ATOM 614 C C . LEU A 1 102 ? -35.669 37.982 18.428 1.00 41.48 ? 79 LEU A C 1 ATOM 615 O O . LEU A 1 102 ? -36.719 37.361 18.270 1.00 50.13 ? 79 LEU A O 1 ATOM 616 C CB . LEU A 1 102 ? -34.011 36.369 19.382 1.00 47.78 ? 79 LEU A CB 1 ATOM 617 C CG . LEU A 1 102 ? -32.957 35.280 19.166 1.00 50.95 ? 79 LEU A CG 1 ATOM 618 C CD1 . LEU A 1 102 ? -32.621 34.590 20.481 1.00 40.56 ? 79 LEU A CD1 1 ATOM 619 C CD2 . LEU A 1 102 ? -33.432 34.264 18.134 1.00 45.94 ? 79 LEU A CD2 1 ATOM 620 N N . GLY A 1 103 ? -35.639 39.258 18.793 1.00 43.39 ? 80 GLY A N 1 ATOM 621 C CA . GLY A 1 103 ? -36.857 39.951 19.165 1.00 50.24 ? 80 GLY A CA 1 ATOM 622 C C . GLY A 1 103 ? -37.153 41.229 18.407 1.00 58.61 ? 80 GLY A C 1 ATOM 623 O O . GLY A 1 103 ? -37.820 42.116 18.942 1.00 68.86 ? 80 GLY A O 1 ATOM 624 N N . VAL A 1 104 ? -36.662 41.330 17.173 1.00 54.53 ? 81 VAL A N 1 ATOM 625 C CA . VAL A 1 104 ? -36.955 42.482 16.320 1.00 57.72 ? 81 VAL A CA 1 ATOM 626 C C . VAL A 1 104 ? -38.465 42.612 16.174 1.00 63.35 ? 81 VAL A C 1 ATOM 627 O O . VAL A 1 104 ? -39.024 43.710 16.218 1.00 65.05 ? 81 VAL A O 1 ATOM 628 C CB . VAL A 1 104 ? -36.326 42.335 14.919 1.00 53.97 ? 81 VAL A CB 1 ATOM 629 C CG1 . VAL A 1 104 ? -36.648 43.546 14.056 1.00 48.56 ? 81 VAL A CG1 1 ATOM 630 C CG2 . VAL A 1 104 ? -34.828 42.146 15.024 1.00 57.21 ? 81 VAL A CG2 1 ATOM 631 N N . CYS A 1 105 ? -39.115 41.465 16.013 1.00 57.06 ? 82 CYS A N 1 ATOM 632 C CA . CYS A 1 105 ? -40.566 41.382 15.960 1.00 62.87 ? 82 CYS A CA 1 ATOM 633 C C . CYS A 1 105 ? -41.010 40.037 16.527 1.00 65.71 ? 82 CYS A C 1 ATOM 634 O O . CYS A 1 105 ? -40.198 39.124 16.685 1.00 66.75 ? 82 CYS A O 1 ATOM 635 C CB . CYS A 1 105 ? -41.052 41.549 14.521 1.00 61.49 ? 82 CYS A CB 1 ATOM 636 S SG . CYS A 1 105 ? -40.086 40.625 13.304 1.00 82.53 ? 82 CYS A SG 1 ATOM 637 N N . ARG A 1 106 ? -42.295 39.914 16.836 1.00 71.71 ? 83 ARG A N 1 ATOM 638 C CA . ARG A 1 106 ? -42.805 38.685 17.434 1.00 78.40 ? 83 ARG A CA 1 ATOM 639 C C . ARG A 1 106 ? -42.826 37.528 16.442 1.00 79.27 ? 83 ARG A C 1 ATOM 640 O O . ARG A 1 106 ? -43.470 37.601 15.395 1.00 84.43 ? 83 ARG A O 1 ATOM 641 C CB . ARG A 1 106 ? -44.201 38.900 18.019 1.00 85.12 ? 83 ARG A CB 1 ATOM 642 C CG . ARG A 1 106 ? -44.831 37.651 18.607 1.00 93.69 ? 83 ARG A CG 1 ATOM 643 C CD . ARG A 1 106 ? -44.978 37.760 20.114 1.00 100.74 ? 83 ARG A CD 1 ATOM 644 N NE . ARG A 1 106 ? -45.683 36.610 20.670 1.00 113.00 ? 83 ARG A NE 1 ATOM 645 C CZ . ARG A 1 106 ? -47.007 36.508 20.737 1.00 119.95 ? 83 ARG A CZ 1 ATOM 646 N NH1 . ARG A 1 106 ? -47.773 37.491 20.282 1.00 122.72 ? 83 ARG A NH1 1 ATOM 647 N NH2 . ARG A 1 106 ? -47.566 35.424 21.258 1.00 120.81 ? 83 ARG A NH2 1 ATOM 648 N N . ASN A 1 107 ? -42.109 36.462 16.781 1.00 74.21 ? 84 ASN A N 1 ATOM 649 C CA . ASN A 1 107 ? -42.142 35.232 16.002 1.00 76.46 ? 84 ASN A CA 1 ATOM 650 C C . ASN A 1 107 ? -41.826 34.032 16.884 1.00 80.49 ? 84 ASN A C 1 ATOM 651 O O . ASN A 1 107 ? -41.664 34.173 18.097 1.00 83.81 ? 84 ASN A O 1 ATOM 652 C CB . ASN A 1 107 ? -41.172 35.303 14.822 1.00 74.06 ? 84 ASN A CB 1 ATOM 653 C CG . ASN A 1 107 ? -39.722 35.346 15.256 1.00 75.65 ? 84 ASN A CG 1 ATOM 654 O OD1 . ASN A 1 107 ? -39.405 35.786 16.360 1.00 93.70 ? 84 ASN A OD1 1 ATOM 655 N ND2 . ASN A 1 107 ? -38.831 34.892 14.383 1.00 72.71 ? 84 ASN A ND2 1 ATOM 656 N N . ALA A 1 108 ? -41.741 32.854 16.277 1.00 82.17 ? 85 ALA A N 1 ATOM 657 C CA . ALA A 1 108 ? -41.478 31.633 17.030 1.00 82.82 ? 85 ALA A CA 1 ATOM 658 C C . ALA A 1 108 ? -40.082 31.640 17.650 1.00 81.41 ? 85 ALA A C 1 ATOM 659 O O . ALA A 1 108 ? -39.878 31.117 18.745 1.00 82.83 ? 85 ALA A O 1 ATOM 660 C CB . ALA A 1 108 ? -41.667 30.408 16.145 1.00 73.07 ? 85 ALA A CB 1 ATOM 661 N N . GLU A 1 109 ? -39.127 32.242 16.948 1.00 75.67 ? 86 GLU A N 1 ATOM 662 C CA . GLU A 1 109 ? -37.742 32.275 17.409 1.00 78.34 ? 86 GLU A CA 1 ATOM 663 C C . GLU A 1 109 ? -37.559 33.204 18.609 1.00 68.77 ? 86 GLU A C 1 ATOM 664 O O . GLU A 1 109 ? -36.582 33.089 19.349 1.00 59.48 ? 86 GLU A O 1 ATOM 665 C CB . GLU A 1 109 ? -36.797 32.676 16.271 1.00 85.03 ? 86 GLU A CB 1 ATOM 666 C CG . GLU A 1 109 ? -36.579 31.594 15.214 1.00 93.71 ? 86 GLU A CG 1 ATOM 667 C CD . GLU A 1 109 ? -37.776 31.401 14.298 1.00 93.65 ? 86 GLU A CD 1 ATOM 668 O OE1 . GLU A 1 109 ? -37.877 30.326 13.669 1.00 81.99 ? 86 GLU A OE1 1 ATOM 669 O OE2 . GLU A 1 109 ? -38.611 32.325 14.202 1.00 97.76 ? 86 GLU A OE2 1 ATOM 670 N N . GLU A 1 110 ? -38.507 34.116 18.799 1.00 67.05 ? 87 GLU A N 1 ATOM 671 C CA . GLU A 1 110 ? -38.463 35.051 19.917 1.00 60.26 ? 87 GLU A CA 1 ATOM 672 C C . GLU A 1 110 ? -38.624 34.327 21.252 1.00 62.72 ? 87 GLU A C 1 ATOM 673 O O . GLU A 1 110 ? -38.180 34.816 22.291 1.00 57.72 ? 87 GLU A O 1 ATOM 674 C CB . GLU A 1 110 ? -39.545 36.120 19.764 1.00 53.94 ? 87 GLU A CB 1 ATOM 675 C CG . GLU A 1 110 ? -39.382 37.302 20.704 1.00 63.93 ? 87 GLU A CG 1 ATOM 676 C CD . GLU A 1 110 ? -40.552 38.261 20.641 1.00 65.38 ? 87 GLU A CD 1 ATOM 677 O OE1 . GLU A 1 110 ? -40.348 39.465 20.897 1.00 63.39 ? 87 GLU A OE1 1 ATOM 678 O OE2 . GLU A 1 110 ? -41.676 37.809 20.340 1.00 68.55 ? 87 GLU A OE2 1 ATOM 679 N N . ASN A 1 111 ? -39.259 33.159 21.216 1.00 56.37 ? 88 ASN A N 1 ATOM 680 C CA . ASN A 1 111 ? -39.418 32.331 22.405 1.00 59.81 ? 88 ASN A CA 1 ATOM 681 C C . ASN A 1 111 ? -38.087 31.907 23.019 1.00 63.72 ? 88 ASN A C 1 ATOM 682 O O . ASN A 1 111 ? -38.008 31.655 24.221 1.00 69.77 ? 88 ASN A O 1 ATOM 683 C CB . ASN A 1 111 ? -40.263 31.092 22.094 1.00 67.45 ? 88 ASN A CB 1 ATOM 684 C CG . ASN A 1 111 ? -41.753 31.370 22.159 1.00 75.02 ? 88 ASN A CG 1 ATOM 685 O OD1 . ASN A 1 111 ? -42.343 31.881 21.208 1.00 78.69 ? 88 ASN A OD1 1 ATOM 686 N ND2 . ASN A 1 111 ? -42.369 31.027 23.284 1.00 84.77 ? 88 ASN A ND2 1 ATOM 687 N N . LEU A 1 112 ? -37.047 31.833 22.192 1.00 53.97 ? 89 LEU A N 1 ATOM 688 C CA . LEU A 1 112 ? -35.721 31.428 22.653 1.00 49.76 ? 89 LEU A CA 1 ATOM 689 C C . LEU A 1 112 ? -35.195 32.381 23.719 1.00 53.80 ? 89 LEU A C 1 ATOM 690 O O . LEU A 1 112 ? -34.428 31.985 24.595 1.00 55.70 ? 89 LEU A O 1 ATOM 691 C CB . LEU A 1 112 ? -34.730 31.352 21.487 1.00 57.05 ? 89 LEU A CB 1 ATOM 692 C CG . LEU A 1 112 ? -34.685 30.083 20.630 1.00 70.39 ? 89 LEU A CG 1 ATOM 693 C CD1 . LEU A 1 112 ? -35.970 29.889 19.838 1.00 76.92 ? 89 LEU A CD1 1 ATOM 694 C CD2 . LEU A 1 112 ? -33.480 30.116 19.699 1.00 64.31 ? 89 LEU A CD2 1 ATOM 695 N N . ILE A 1 113 ? -35.611 33.639 23.634 1.00 51.34 ? 90 ILE A N 1 ATOM 696 C CA . ILE A 1 113 ? -35.223 34.640 24.616 1.00 54.50 ? 90 ILE A CA 1 ATOM 697 C C . ILE A 1 113 ? -35.750 34.267 25.993 1.00 52.94 ? 90 ILE A C 1 ATOM 698 O O . ILE A 1 113 ? -35.029 34.337 26.988 1.00 64.95 ? 90 ILE A O 1 ATOM 699 C CB . ILE A 1 113 ? -35.769 36.027 24.249 1.00 52.37 ? 90 ILE A CB 1 ATOM 700 C CG1 . ILE A 1 113 ? -35.269 36.447 22.865 1.00 51.60 ? 90 ILE A CG1 1 ATOM 701 C CG2 . ILE A 1 113 ? -35.374 37.047 25.307 1.00 49.97 ? 90 ILE A CG2 1 ATOM 702 C CD1 . ILE A 1 113 ? -35.858 37.752 22.369 1.00 36.73 ? 90 ILE A CD1 1 ATOM 703 N N . TYR A 1 114 ? -37.012 33.860 26.042 1.00 56.18 ? 91 TYR A N 1 ATOM 704 C CA . TYR A 1 114 ? -37.663 33.576 27.313 1.00 58.35 ? 91 TYR A CA 1 ATOM 705 C C . TYR A 1 114 ? -37.492 32.122 27.741 1.00 49.03 ? 91 TYR A C 1 ATOM 706 O O . TYR A 1 114 ? -37.562 31.808 28.929 1.00 65.59 ? 91 TYR A O 1 ATOM 707 C CB . TYR A 1 114 ? -39.139 33.970 27.245 1.00 58.24 ? 91 TYR A CB 1 ATOM 708 C CG . TYR A 1 114 ? -39.335 35.389 26.763 1.00 62.61 ? 91 TYR A CG 1 ATOM 709 C CD1 . TYR A 1 114 ? -39.095 36.467 27.607 1.00 66.21 ? 91 TYR A CD1 1 ATOM 710 C CD2 . TYR A 1 114 ? -39.740 35.654 25.461 1.00 58.40 ? 91 TYR A CD2 1 ATOM 711 C CE1 . TYR A 1 114 ? -39.264 37.768 27.172 1.00 61.87 ? 91 TYR A CE1 1 ATOM 712 C CE2 . TYR A 1 114 ? -39.912 36.952 25.017 1.00 63.83 ? 91 TYR A CE2 1 ATOM 713 C CZ . TYR A 1 114 ? -39.672 38.004 25.877 1.00 65.54 ? 91 TYR A CZ 1 ATOM 714 O OH . TYR A 1 114 ? -39.841 39.298 25.441 1.00 70.00 ? 91 TYR A OH 1 ATOM 715 N N . ASP A 1 115 ? -37.255 31.240 26.776 1.00 47.34 ? 92 ASP A N 1 ATOM 716 C CA . ASP A 1 115 ? -37.024 29.831 27.079 1.00 62.58 ? 92 ASP A CA 1 ATOM 717 C C . ASP A 1 115 ? -35.617 29.602 27.623 1.00 60.92 ? 92 ASP A C 1 ATOM 718 O O . ASP A 1 115 ? -35.377 28.647 28.361 1.00 59.21 ? 92 ASP A O 1 ATOM 719 C CB . ASP A 1 115 ? -37.267 28.958 25.844 1.00 74.39 ? 92 ASP A CB 1 ATOM 720 C CG . ASP A 1 115 ? -38.733 28.886 25.458 1.00 83.42 ? 92 ASP A CG 1 ATOM 721 O OD1 . ASP A 1 115 ? -39.594 29.093 26.341 1.00 87.26 ? 92 ASP A OD1 1 ATOM 722 O OD2 . ASP A 1 115 ? -39.026 28.618 24.273 1.00 87.55 ? 92 ASP A OD2 1 ATOM 723 N N . TYR A 1 116 ? -34.691 30.485 27.259 1.00 57.21 ? 93 TYR A N 1 ATOM 724 C CA . TYR A 1 116 ? -33.311 30.378 27.721 1.00 58.60 ? 93 TYR A CA 1 ATOM 725 C C . TYR A 1 116 ? -33.006 31.406 28.806 1.00 55.77 ? 93 TYR A C 1 ATOM 726 O O . TYR A 1 116 ? -31.901 31.432 29.352 1.00 60.06 ? 93 TYR A O 1 ATOM 727 C CB . TYR A 1 116 ? -32.336 30.560 26.555 1.00 60.36 ? 93 TYR A CB 1 ATOM 728 C CG . TYR A 1 116 ? -32.404 29.477 25.501 1.00 71.61 ? 93 TYR A CG 1 ATOM 729 C CD1 . TYR A 1 116 ? -32.749 28.173 25.835 1.00 71.07 ? 93 TYR A CD1 1 ATOM 730 C CD2 . TYR A 1 116 ? -32.122 29.760 24.170 1.00 73.36 ? 93 TYR A CD2 1 ATOM 731 C CE1 . TYR A 1 116 ? -32.810 27.181 24.872 1.00 72.54 ? 93 TYR A CE1 1 ATOM 732 C CE2 . TYR A 1 116 ? -32.181 28.776 23.201 1.00 79.50 ? 93 TYR A CE2 1 ATOM 733 C CZ . TYR A 1 116 ? -32.526 27.489 23.557 1.00 83.22 ? 93 TYR A CZ 1 ATOM 734 O OH . TYR A 1 116 ? -32.585 26.508 22.593 1.00 91.47 ? 93 TYR A OH 1 ATOM 735 N N . HIS A 1 117 ? -33.993 32.247 29.108 1.00 52.84 ? 94 HIS A N 1 ATOM 736 C CA . HIS A 1 117 ? -33.845 33.325 30.086 1.00 58.10 ? 94 HIS A CA 1 ATOM 737 C C . HIS A 1 117 ? -32.675 34.251 29.757 1.00 57.75 ? 94 HIS A C 1 ATOM 738 O O . HIS A 1 117 ? -31.878 34.602 30.629 1.00 60.99 ? 94 HIS A O 1 ATOM 739 C CB . HIS A 1 117 ? -33.719 32.762 31.506 1.00 55.13 ? 94 HIS A CB 1 ATOM 740 C CG . HIS A 1 117 ? -34.992 32.176 32.032 1.00 53.28 ? 94 HIS A CG 1 ATOM 741 N ND1 . HIS A 1 117 ? -35.795 32.835 32.938 1.00 64.81 ? 94 HIS A ND1 1 ATOM 742 C CD2 . HIS A 1 117 ? -35.611 31.003 31.764 1.00 57.88 ? 94 HIS A CD2 1 ATOM 743 C CE1 . HIS A 1 117 ? -36.849 32.088 33.213 1.00 64.88 ? 94 HIS A CE1 1 ATOM 744 N NE2 . HIS A 1 117 ? -36.762 30.971 32.514 1.00 60.14 ? 94 HIS A NE2 1 ATOM 745 N N . LEU A 1 118 ? -32.589 34.649 28.493 1.00 50.96 ? 95 LEU A N 1 ATOM 746 C CA . LEU A 1 118 ? -31.482 35.468 28.013 1.00 55.22 ? 95 LEU A CA 1 ATOM 747 C C . LEU A 1 118 ? -31.501 36.871 28.608 1.00 52.66 ? 95 LEU A C 1 ATOM 748 O O . LEU A 1 118 ? -30.449 37.479 28.815 1.00 44.46 ? 95 LEU A O 1 ATOM 749 C CB . LEU A 1 118 ? -31.494 35.539 26.484 1.00 43.99 ? 95 LEU A CB 1 ATOM 750 C CG . LEU A 1 118 ? -31.365 34.191 25.772 1.00 52.20 ? 95 LEU A CG 1 ATOM 751 C CD1 . LEU A 1 118 ? -31.255 34.378 24.264 1.00 47.85 ? 95 LEU A CD1 1 ATOM 752 C CD2 . LEU A 1 118 ? -30.172 33.414 26.310 1.00 49.81 ? 95 LEU A CD2 1 ATOM 753 N N . ILE A 1 119 ? -32.698 37.382 28.875 1.00 43.92 ? 96 ILE A N 1 ATOM 754 C CA . ILE A 1 119 ? -32.845 38.700 29.479 1.00 44.88 ? 96 ILE A CA 1 ATOM 755 C C . ILE A 1 119 ? -32.263 38.687 30.888 1.00 52.53 ? 96 ILE A C 1 ATOM 756 O O . ILE A 1 119 ? -31.514 39.587 31.269 1.00 49.64 ? 96 ILE A O 1 ATOM 757 C CB . ILE A 1 119 ? -34.322 39.143 29.525 1.00 51.48 ? 96 ILE A CB 1 ATOM 758 C CG1 . ILE A 1 119 ? -34.858 39.363 28.109 1.00 52.85 ? 96 ILE A CG1 1 ATOM 759 C CG2 . ILE A 1 119 ? -34.479 40.416 30.340 1.00 46.53 ? 96 ILE A CG2 1 ATOM 760 C CD1 . ILE A 1 119 ? -36.307 39.810 28.073 1.00 55.14 ? 96 ILE A CD1 1 ATOM 761 N N . ASP A 1 120 ? -32.604 37.652 31.652 1.00 49.02 ? 97 ASP A N 1 ATOM 762 C CA . ASP A 1 120 ? -32.056 37.479 32.991 1.00 56.67 ? 97 ASP A CA 1 ATOM 763 C C . ASP A 1 120 ? -30.536 37.365 32.936 1.00 50.13 ? 97 ASP A C 1 ATOM 764 O O . ASP A 1 120 ? -29.832 37.945 33.763 1.00 50.13 ? 97 ASP A O 1 ATOM 765 C CB . ASP A 1 120 ? -32.661 36.248 33.674 1.00 64.38 ? 97 ASP A CB 1 ATOM 766 C CG . ASP A 1 120 ? -34.130 36.428 34.011 1.00 72.25 ? 97 ASP A CG 1 ATOM 767 O OD1 . ASP A 1 120 ? -34.793 37.264 33.362 1.00 74.66 ? 97 ASP A OD1 1 ATOM 768 O OD2 . ASP A 1 120 ? -34.625 35.733 34.923 1.00 86.76 ? 97 ASP A OD2 1 ATOM 769 N N . LYS A 1 121 ? -30.035 36.628 31.949 1.00 42.21 ? 98 LYS A N 1 ATOM 770 C CA . LYS A 1 121 ? -28.595 36.439 31.796 1.00 49.27 ? 98 LYS A CA 1 ATOM 771 C C . LYS A 1 121 ? -27.906 37.747 31.426 1.00 48.57 ? 98 LYS A C 1 ATOM 772 O O . LYS A 1 121 ? -26.789 38.019 31.867 1.00 52.30 ? 98 LYS A O 1 ATOM 773 C CB . LYS A 1 121 ? -28.294 35.358 30.754 1.00 56.23 ? 98 LYS A CB 1 ATOM 774 C CG . LYS A 1 121 ? -28.561 33.940 31.238 1.00 71.78 ? 98 LYS A CG 1 ATOM 775 C CD . LYS A 1 121 ? -27.607 33.551 32.357 1.00 86.30 ? 98 LYS A CD 1 ATOM 776 C CE . LYS A 1 121 ? -27.992 32.218 32.985 1.00 96.95 ? 98 LYS A CE 1 ATOM 777 N NZ . LYS A 1 121 ? -28.061 31.115 31.988 1.00 100.50 ? 98 LYS A NZ 1 ATOM 778 N N . LEU A 1 122 ? -28.584 38.555 30.618 1.00 47.96 ? 99 LEU A N 1 ATOM 779 C CA . LEU A 1 122 ? -28.052 39.849 30.213 1.00 46.01 ? 99 LEU A CA 1 ATOM 780 C C . LEU A 1 122 ? -27.950 40.794 31.406 1.00 51.22 ? 99 LEU A C 1 ATOM 781 O O . LEU A 1 122 ? -27.011 41.582 31.501 1.00 48.79 ? 99 LEU A O 1 ATOM 782 C CB . LEU A 1 122 ? -28.916 40.469 29.113 1.00 34.77 ? 99 LEU A CB 1 ATOM 783 C CG . LEU A 1 122 ? -28.418 41.810 28.573 1.00 42.90 ? 99 LEU A CG 1 ATOM 784 C CD1 . LEU A 1 122 ? -27.011 41.671 28.010 1.00 40.37 ? 99 LEU A CD1 1 ATOM 785 C CD2 . LEU A 1 122 ? -29.366 42.357 27.521 1.00 42.46 ? 99 LEU A CD2 1 ATOM 786 N N . GLU A 1 123 ? -28.916 40.707 32.316 1.00 50.34 ? 100 GLU A N 1 ATOM 787 C CA . GLU A 1 123 ? -28.898 41.519 33.529 1.00 48.62 ? 100 GLU A CA 1 ATOM 788 C C . GLU A 1 123 ? -27.666 41.215 34.376 1.00 51.42 ? 100 GLU A C 1 ATOM 789 O O . GLU A 1 123 ? -27.045 42.120 34.933 1.00 53.05 ? 100 GLU A O 1 ATOM 790 C CB . GLU A 1 123 ? -30.167 41.290 34.350 1.00 42.94 ? 100 GLU A CB 1 ATOM 791 C CG . GLU A 1 123 ? -31.435 41.762 33.665 1.00 48.11 ? 100 GLU A CG 1 ATOM 792 C CD . GLU A 1 123 ? -32.691 41.349 34.409 1.00 52.99 ? 100 GLU A CD 1 ATOM 793 O OE1 . GLU A 1 123 ? -32.571 40.765 35.505 1.00 58.66 ? 100 GLU A OE1 1 ATOM 794 O OE2 . GLU A 1 123 ? -33.798 41.606 33.893 1.00 54.97 ? 100 GLU A OE2 1 ATOM 795 N N . ASN A 1 124 ? -27.315 39.936 34.463 1.00 48.59 ? 101 ASN A N 1 ATOM 796 C CA . ASN A 1 124 ? -26.138 39.520 35.212 1.00 51.99 ? 101 ASN A CA 1 ATOM 797 C C . ASN A 1 124 ? -24.846 39.953 34.524 1.00 52.32 ? 101 ASN A C 1 ATOM 798 O O . ASN A 1 124 ? -23.934 40.471 35.168 1.00 52.21 ? 101 ASN A O 1 ATOM 799 C CB . ASN A 1 124 ? -26.143 38.005 35.437 1.00 53.45 ? 101 ASN A CB 1 ATOM 800 C CG . ASN A 1 124 ? -27.345 37.540 36.237 1.00 72.30 ? 101 ASN A CG 1 ATOM 801 O OD1 . ASN A 1 124 ? -27.913 38.298 37.023 1.00 66.98 ? 101 ASN A OD1 1 ATOM 802 N ND2 . ASN A 1 124 ? -27.739 36.286 36.039 1.00 83.00 ? 101 ASN A ND2 1 ATOM 803 N N . LYS A 1 125 ? -24.774 39.743 33.213 1.00 47.86 ? 102 LYS A N 1 ATOM 804 C CA . LYS A 1 125 ? -23.591 40.129 32.450 1.00 51.30 ? 102 LYS A CA 1 ATOM 805 C C . LYS A 1 125 ? -23.394 41.640 32.475 1.00 52.05 ? 102 LYS A C 1 ATOM 806 O O . LYS A 1 125 ? -22.267 42.124 32.568 1.00 48.40 ? 102 LYS A O 1 ATOM 807 C CB . LYS A 1 125 ? -23.677 39.620 31.009 1.00 46.01 ? 102 LYS A CB 1 ATOM 808 C CG . LYS A 1 125 ? -23.551 38.109 30.882 1.00 48.49 ? 102 LYS A CG 1 ATOM 809 C CD . LYS A 1 125 ? -23.548 37.671 29.427 1.00 47.68 ? 102 LYS A CD 1 ATOM 810 C CE . LYS A 1 125 ? -23.485 36.156 29.307 1.00 42.62 ? 102 LYS A CE 1 ATOM 811 N NZ . LYS A 1 125 ? -22.242 35.607 29.912 1.00 45.17 ? 102 LYS A NZ 1 ATOM 812 N N . PHE A 1 126 ? -24.496 42.379 32.402 1.00 48.79 ? 103 PHE A N 1 ATOM 813 C CA . PHE A 1 126 ? -24.438 43.834 32.469 1.00 51.32 ? 103 PHE A CA 1 ATOM 814 C C . PHE A 1 126 ? -23.966 44.292 33.845 1.00 54.95 ? 103 PHE A C 1 ATOM 815 O O . PHE A 1 126 ? -23.200 45.248 33.961 1.00 56.33 ? 103 PHE A O 1 ATOM 816 C CB . PHE A 1 126 ? -25.799 44.447 32.133 1.00 48.75 ? 103 PHE A CB 1 ATOM 817 C CG . PHE A 1 126 ? -25.874 45.927 32.377 1.00 53.35 ? 103 PHE A CG 1 ATOM 818 C CD1 . PHE A 1 126 ? -25.187 46.814 31.564 1.00 50.68 ? 103 PHE A CD1 1 ATOM 819 C CD2 . PHE A 1 126 ? -26.638 46.433 33.415 1.00 52.44 ? 103 PHE A CD2 1 ATOM 820 C CE1 . PHE A 1 126 ? -25.257 48.177 31.786 1.00 48.67 ? 103 PHE A CE1 1 ATOM 821 C CE2 . PHE A 1 126 ? -26.712 47.794 33.642 1.00 54.13 ? 103 PHE A CE2 1 ATOM 822 C CZ . PHE A 1 126 ? -26.020 48.667 32.827 1.00 46.77 ? 103 PHE A CZ 1 ATOM 823 N N . GLN A 1 127 ? -24.419 43.600 34.886 1.00 58.85 ? 104 GLN A N 1 ATOM 824 C CA . GLN A 1 127 ? -24.009 43.922 36.246 1.00 59.87 ? 104 GLN A CA 1 ATOM 825 C C . GLN A 1 127 ? -22.540 43.571 36.469 1.00 55.10 ? 104 GLN A C 1 ATOM 826 O O . GLN A 1 127 ? -21.855 44.209 37.268 1.00 58.94 ? 104 GLN A O 1 ATOM 827 C CB . GLN A 1 127 ? -24.894 43.201 37.265 1.00 66.73 ? 104 GLN A CB 1 ATOM 828 C CG . GLN A 1 127 ? -24.737 43.709 38.690 1.00 81.58 ? 104 GLN A CG 1 ATOM 829 C CD . GLN A 1 127 ? -25.147 45.164 38.842 1.00 95.31 ? 104 GLN A CD 1 ATOM 830 O OE1 . GLN A 1 127 ? -26.008 45.661 38.113 1.00 93.12 ? 104 GLN A OE1 1 ATOM 831 N NE2 . GLN A 1 127 ? -24.527 45.856 39.791 1.00 98.53 ? 104 GLN A NE2 1 ATOM 832 N N . ALA A 1 128 ? -22.058 42.556 35.759 1.00 45.60 ? 105 ALA A N 1 ATOM 833 C CA . ALA A 1 128 ? -20.654 42.175 35.840 1.00 50.87 ? 105 ALA A CA 1 ATOM 834 C C . ALA A 1 128 ? -19.775 43.267 35.236 1.00 59.46 ? 105 ALA A C 1 ATOM 835 O O . ALA A 1 128 ? -18.674 43.528 35.722 1.00 68.72 ? 105 ALA A O 1 ATOM 836 C CB . ALA A 1 128 ? -20.414 40.844 35.144 1.00 43.44 ? 105 ALA A CB 1 ATOM 837 N N . GLU A 1 129 ? -20.272 43.902 34.177 1.00 50.55 ? 106 GLU A N 1 ATOM 838 C CA . GLU A 1 129 ? -19.586 45.035 33.568 1.00 50.83 ? 106 GLU A CA 1 ATOM 839 C C . GLU A 1 129 ? -19.454 46.161 34.585 1.00 49.49 ? 106 GLU A C 1 ATOM 840 O O . GLU A 1 129 ? -18.391 46.768 34.723 1.00 47.11 ? 106 GLU A O 1 ATOM 841 C CB . GLU A 1 129 ? -20.357 45.538 32.344 1.00 43.31 ? 106 GLU A CB 1 ATOM 842 C CG . GLU A 1 129 ? -20.505 44.525 31.218 1.00 50.86 ? 106 GLU A CG 1 ATOM 843 C CD . GLU A 1 129 ? -19.324 44.525 30.264 1.00 55.73 ? 106 GLU A CD 1 ATOM 844 O OE1 . GLU A 1 129 ? -18.350 45.267 30.516 1.00 49.72 ? 106 GLU A OE1 1 ATOM 845 O OE2 . GLU A 1 129 ? -19.372 43.784 29.258 1.00 46.09 ? 106 GLU A OE2 1 ATOM 846 N N . ILE A 1 130 ? -20.545 46.426 35.298 1.00 56.67 ? 107 ILE A N 1 ATOM 847 C CA . ILE A 1 130 ? -20.582 47.475 36.311 1.00 62.05 ? 107 ILE A CA 1 ATOM 848 C C . ILE A 1 130 ? -19.611 47.183 37.450 1.00 64.87 ? 107 ILE A C 1 ATOM 849 O O . ILE A 1 130 ? -18.852 48.056 37.875 1.00 65.12 ? 107 ILE A O 1 ATOM 850 C CB . ILE A 1 130 ? -22.000 47.639 36.896 1.00 67.80 ? 107 ILE A CB 1 ATOM 851 C CG1 . ILE A 1 130 ? -23.002 47.979 35.791 1.00 64.98 ? 107 ILE A CG1 1 ATOM 852 C CG2 . ILE A 1 130 ? -22.015 48.710 37.976 1.00 76.20 ? 107 ILE A CG2 1 ATOM 853 C CD1 . ILE A 1 130 ? -22.727 49.297 35.101 1.00 63.94 ? 107 ILE A CD1 1 ATOM 854 N N . GLU A 1 131 ? -19.633 45.947 37.937 1.00 65.64 ? 108 GLU A N 1 ATOM 855 C CA . GLU A 1 131 ? -18.786 45.554 39.057 1.00 72.20 ? 108 GLU A CA 1 ATOM 856 C C . GLU A 1 131 ? -17.315 45.521 38.659 1.00 64.25 ? 108 GLU A C 1 ATOM 857 O O . GLU A 1 131 ? -16.431 45.620 39.509 1.00 63.19 ? 108 GLU A O 1 ATOM 858 C CB . GLU A 1 131 ? -19.231 44.202 39.619 1.00 81.40 ? 108 GLU A CB 1 ATOM 859 C CG . GLU A 1 131 ? -20.613 44.241 40.259 1.00 93.70 ? 108 GLU A CG 1 ATOM 860 C CD . GLU A 1 131 ? -21.155 42.862 40.578 1.00 103.13 ? 108 GLU A CD 1 ATOM 861 O OE1 . GLU A 1 131 ? -20.438 41.868 40.342 1.00 107.34 ? 108 GLU A OE1 1 ATOM 862 O OE2 . GLU A 1 131 ? -22.303 42.774 41.063 1.00 106.86 ? 108 GLU A OE2 1 ATOM 863 N N . ASN A 1 132 ? -17.054 45.390 37.364 1.00 63.54 ? 109 ASN A N 1 ATOM 864 C CA . ASN A 1 132 ? -15.683 45.447 36.880 1.00 62.09 ? 109 ASN A CA 1 ATOM 865 C C . ASN A 1 132 ? -15.165 46.881 36.864 1.00 63.04 ? 109 ASN A C 1 ATOM 866 O O . ASN A 1 132 ? -13.981 47.123 37.094 1.00 63.21 ? 109 ASN A O 1 ATOM 867 C CB . ASN A 1 132 ? -15.559 44.817 35.494 1.00 57.10 ? 109 ASN A CB 1 ATOM 868 C CG . ASN A 1 132 ? -14.118 44.680 35.050 1.00 58.73 ? 109 ASN A CG 1 ATOM 869 O OD1 . ASN A 1 132 ? -13.445 43.706 35.382 1.00 63.19 ? 109 ASN A OD1 1 ATOM 870 N ND2 . ASN A 1 132 ? -13.634 45.663 34.302 1.00 62.32 ? 109 ASN A ND2 1 ATOM 871 N N . MET A 1 133 ? -16.059 47.828 36.596 1.00 57.91 ? 110 MET A N 1 ATOM 872 C CA . MET A 1 133 ? -15.697 49.241 36.600 1.00 56.79 ? 110 MET A CA 1 ATOM 873 C C . MET A 1 133 ? -15.404 49.718 38.017 1.00 69.84 ? 110 MET A C 1 ATOM 874 O O . MET A 1 133 ? -14.524 50.551 38.233 1.00 72.11 ? 110 MET A O 1 ATOM 875 C CB . MET A 1 133 ? -16.811 50.089 35.986 1.00 47.69 ? 110 MET A CB 1 ATOM 876 C CG . MET A 1 133 ? -17.030 49.847 34.504 1.00 50.17 ? 110 MET A CG 1 ATOM 877 S SD . MET A 1 133 ? -18.328 50.887 33.814 1.00 57.14 ? 110 MET A SD 1 ATOM 878 C CE . MET A 1 133 ? -17.729 52.515 34.258 1.00 96.19 ? 110 MET A CE 1 ATOM 879 N N . GLU A 1 134 ? -16.150 49.188 38.980 1.00 76.81 ? 111 GLU A N 1 ATOM 880 C CA . GLU A 1 134 ? -15.936 49.526 40.379 1.00 82.98 ? 111 GLU A CA 1 ATOM 881 C C . GLU A 1 134 ? -14.608 48.950 40.852 1.00 76.01 ? 111 GLU A C 1 ATOM 882 O O . GLU A 1 134 ? -13.900 49.567 41.648 1.00 78.43 ? 111 GLU A O 1 ATOM 883 C CB . GLU A 1 134 ? -17.080 48.985 41.235 1.00 91.27 ? 111 GLU A CB 1 ATOM 884 C CG . GLU A 1 134 ? -18.446 49.523 40.839 1.00 101.80 ? 111 GLU A CG 1 ATOM 885 C CD . GLU A 1 134 ? -19.589 48.800 41.526 1.00 109.65 ? 111 GLU A CD 1 ATOM 886 O OE1 . GLU A 1 134 ? -19.336 47.775 42.194 1.00 114.89 ? 111 GLU A OE1 1 ATOM 887 O OE2 . GLU A 1 134 ? -20.745 49.257 41.396 1.00 111.27 ? 111 GLU A OE2 1 ATOM 888 N N . ALA A 1 135 ? -14.267 47.769 40.348 1.00 72.42 ? 112 ALA A N 1 ATOM 889 C CA . ALA A 1 135 ? -13.044 47.097 40.764 1.00 74.16 ? 112 ALA A CA 1 ATOM 890 C C . ALA A 1 135 ? -11.814 47.597 40.007 1.00 74.10 ? 112 ALA A C 1 ATOM 891 O O . ALA A 1 135 ? -10.712 47.616 40.548 1.00 73.34 ? 112 ALA A O 1 ATOM 892 C CB . ALA A 1 135 ? -13.194 45.587 40.610 1.00 74.37 ? 112 ALA A CB 1 ATOM 893 N N . HIS A 1 136 ? -12.013 48.007 38.758 1.00 73.20 ? 113 HIS A N 1 ATOM 894 C CA . HIS A 1 136 ? -10.901 48.358 37.875 1.00 71.26 ? 113 HIS A CA 1 ATOM 895 C C . HIS A 1 136 ? -10.905 49.792 37.347 1.00 69.27 ? 113 HIS A C 1 ATOM 896 O O . HIS A 1 136 ? -10.753 50.014 36.142 1.00 72.34 ? 113 HIS A O 1 ATOM 897 C CB . HIS A 1 136 ? -10.824 47.387 36.696 1.00 73.26 ? 113 HIS A CB 1 ATOM 898 C CG . HIS A 1 136 ? -10.199 46.069 37.035 1.00 82.51 ? 113 HIS A CG 1 ATOM 899 N ND1 . HIS A 1 136 ? -10.915 45.021 37.574 1.00 84.84 ? 113 HIS A ND1 1 ATOM 900 C CD2 . HIS A 1 136 ? -8.926 45.630 36.904 1.00 86.16 ? 113 HIS A CD2 1 ATOM 901 C CE1 . HIS A 1 136 ? -10.106 43.992 37.760 1.00 88.07 ? 113 HIS A CE1 1 ATOM 902 N NE2 . HIS A 1 136 ? -8.896 44.333 37.364 1.00 88.06 ? 113 HIS A NE2 1 ATOM 903 N N . ASN A 1 137 ? -11.082 50.754 38.247 1.00 66.74 ? 114 ASN A N 1 ATOM 904 C CA . ASN A 1 137 ? -10.865 52.166 37.922 1.00 77.59 ? 114 ASN A CA 1 ATOM 905 C C . ASN A 1 137 ? -11.760 52.706 36.799 1.00 80.15 ? 114 ASN A C 1 ATOM 906 O O . ASN A 1 137 ? -11.395 53.653 36.101 1.00 82.65 ? 114 ASN A O 1 ATOM 907 C CB . ASN A 1 137 ? -9.379 52.404 37.603 1.00 86.34 ? 114 ASN A CB 1 ATOM 908 C CG . ASN A 1 137 ? -8.959 53.855 37.772 1.00 90.88 ? 114 ASN A CG 1 ATOM 909 O OD1 . ASN A 1 137 ? -9.496 54.582 38.608 1.00 97.74 ? 114 ASN A OD1 1 ATOM 910 N ND2 . ASN A 1 137 ? -7.987 54.280 36.971 1.00 82.37 ? 114 ASN A ND2 1 ATOM 911 N N . GLY A 1 138 ? -12.930 52.096 36.633 1.00 72.21 ? 115 GLY A N 1 ATOM 912 C CA . GLY A 1 138 ? -13.914 52.572 35.680 1.00 58.83 ? 115 GLY A CA 1 ATOM 913 C C . GLY A 1 138 ? -13.900 51.868 34.335 1.00 58.25 ? 115 GLY A C 1 ATOM 914 O O . GLY A 1 138 ? -14.664 52.224 33.443 1.00 54.64 ? 115 GLY A O 1 ATOM 915 N N . THR A 1 139 ? -13.032 50.874 34.179 1.00 57.13 ? 116 THR A N 1 ATOM 916 C CA . THR A 1 139 ? -12.969 50.109 32.935 1.00 56.10 ? 116 THR A CA 1 ATOM 917 C C . THR A 1 139 ? -13.892 48.894 32.998 1.00 57.43 ? 116 THR A C 1 ATOM 918 O O . THR A 1 139 ? -13.760 48.054 33.887 1.00 55.36 ? 116 THR A O 1 ATOM 919 C CB . THR A 1 139 ? -11.532 49.639 32.621 1.00 51.11 ? 116 THR A CB 1 ATOM 920 O OG1 . THR A 1 139 ? -10.647 50.763 32.642 1.00 57.64 ? 116 THR A OG1 1 ATOM 921 C CG2 . THR A 1 139 ? -11.470 48.987 31.255 1.00 49.31 ? 116 THR A CG2 1 ATOM 922 N N . PRO A 1 140 ? -14.839 48.799 32.054 1.00 51.53 ? 117 PRO A N 1 ATOM 923 C CA . PRO A 1 140 ? -15.741 47.645 32.006 1.00 47.62 ? 117 PRO A CA 1 ATOM 924 C C . PRO A 1 140 ? -15.015 46.396 31.523 1.00 51.91 ? 117 PRO A C 1 ATOM 925 O O . PRO A 1 140 ? -13.836 46.467 31.174 1.00 52.26 ? 117 PRO A O 1 ATOM 926 C CB . PRO A 1 140 ? -16.799 48.075 30.989 1.00 44.35 ? 117 PRO A CB 1 ATOM 927 C CG . PRO A 1 140 ? -16.093 49.042 30.108 1.00 41.84 ? 117 PRO A CG 1 ATOM 928 C CD . PRO A 1 140 ? -15.135 49.778 30.995 1.00 45.51 ? 117 PRO A CD 1 ATOM 929 N N . LEU A 1 141 ? -15.712 45.264 31.521 1.00 53.90 ? 118 LEU A N 1 ATOM 930 C CA . LEU A 1 141 ? -15.148 44.021 31.012 1.00 52.82 ? 118 LEU A CA 1 ATOM 931 C C . LEU A 1 141 ? -14.876 44.152 29.522 1.00 48.42 ? 118 LEU A C 1 ATOM 932 O O . LEU A 1 141 ? -13.875 43.647 29.015 1.00 51.95 ? 118 LEU A O 1 ATOM 933 C CB . LEU A 1 141 ? -16.099 42.852 31.278 1.00 50.67 ? 118 LEU A CB 1 ATOM 934 C CG . LEU A 1 141 ? -16.162 42.350 32.721 1.00 51.98 ? 118 LEU A CG 1 ATOM 935 C CD1 . LEU A 1 141 ? -17.262 41.312 32.890 1.00 43.03 ? 118 LEU A CD1 1 ATOM 936 C CD2 . LEU A 1 141 ? -14.814 41.776 33.133 1.00 48.12 ? 118 LEU A CD2 1 ATOM 937 N N . THR A 1 142 ? -15.774 44.844 28.827 1.00 47.38 ? 119 THR A N 1 ATOM 938 C CA . THR A 1 142 ? -15.625 45.080 27.398 1.00 42.21 ? 119 THR A CA 1 ATOM 939 C C . THR A 1 142 ? -15.441 46.567 27.091 1.00 44.39 ? 119 THR A C 1 ATOM 940 O O . THR A 1 142 ? -14.321 47.074 27.095 1.00 44.92 ? 119 THR A O 1 ATOM 941 C CB . THR A 1 142 ? -16.827 44.533 26.607 1.00 45.52 ? 119 THR A CB 1 ATOM 942 O OG1 . THR A 1 142 ? -18.027 45.185 27.041 1.00 43.61 ? 119 THR A OG1 1 ATOM 943 C CG2 . THR A 1 142 ? -16.965 43.032 26.822 1.00 37.65 ? 119 THR A CG2 1 ATOM 944 N N . ASN A 1 143 ? -16.544 47.261 26.830 1.00 41.02 ? 120 ASN A N 1 ATOM 945 C CA . ASN A 1 143 ? -16.487 48.665 26.441 1.00 34.41 ? 120 ASN A CA 1 ATOM 946 C C . ASN A 1 143 ? -17.857 49.327 26.567 1.00 41.52 ? 120 ASN A C 1 ATOM 947 O O . ASN A 1 143 ? -18.838 48.668 26.909 1.00 44.62 ? 120 ASN A O 1 ATOM 948 C CB . ASN A 1 143 ? -15.976 48.785 25.007 1.00 39.35 ? 120 ASN A CB 1 ATOM 949 C CG . ASN A 1 143 ? -16.746 47.907 24.046 1.00 40.06 ? 120 ASN A CG 1 ATOM 950 O OD1 . ASN A 1 143 ? -17.904 48.180 23.738 1.00 42.16 ? 120 ASN A OD1 1 ATOM 951 N ND2 . ASN A 1 143 ? -16.112 46.842 23.573 1.00 40.96 ? 120 ASN A ND2 1 ATOM 952 N N . TYR A 1 144 ? -17.927 50.625 26.285 1.00 36.97 ? 121 TYR A N 1 ATOM 953 C CA . TYR A 1 144 ? -19.185 51.355 26.419 1.00 47.07 ? 121 TYR A CA 1 ATOM 954 C C . TYR A 1 144 ? -20.136 51.127 25.248 1.00 42.98 ? 121 TYR A C 1 ATOM 955 O O . TYR A 1 144 ? -21.342 51.333 25.372 1.00 43.18 ? 121 TYR A O 1 ATOM 956 C CB . TYR A 1 144 ? -18.941 52.852 26.620 1.00 42.07 ? 121 TYR A CB 1 ATOM 957 C CG . TYR A 1 144 ? -18.939 53.285 28.067 1.00 48.88 ? 121 TYR A CG 1 ATOM 958 C CD1 . TYR A 1 144 ? -18.536 52.417 29.076 1.00 45.37 ? 121 TYR A CD1 1 ATOM 959 C CD2 . TYR A 1 144 ? -19.356 54.559 28.425 1.00 40.80 ? 121 TYR A CD2 1 ATOM 960 C CE1 . TYR A 1 144 ? -18.535 52.815 30.402 1.00 45.78 ? 121 TYR A CE1 1 ATOM 961 C CE2 . TYR A 1 144 ? -19.364 54.964 29.744 1.00 40.98 ? 121 TYR A CE2 1 ATOM 962 C CZ . TYR A 1 144 ? -18.954 54.090 30.729 1.00 50.81 ? 121 TYR A CZ 1 ATOM 963 O OH . TYR A 1 144 ? -18.965 54.497 32.044 1.00 51.33 ? 121 TYR A OH 1 ATOM 964 N N . TYR A 1 145 ? -19.590 50.712 24.111 1.00 38.43 ? 122 TYR A N 1 ATOM 965 C CA . TYR A 1 145 ? -20.412 50.338 22.972 1.00 37.16 ? 122 TYR A CA 1 ATOM 966 C C . TYR A 1 145 ? -21.298 49.152 23.353 1.00 40.93 ? 122 TYR A C 1 ATOM 967 O O . TYR A 1 145 ? -22.504 49.158 23.100 1.00 45.96 ? 122 TYR A O 1 ATOM 968 C CB . TYR A 1 145 ? -19.526 49.997 21.775 1.00 33.05 ? 122 TYR A CB 1 ATOM 969 C CG . TYR A 1 145 ? -20.270 49.681 20.501 1.00 37.70 ? 122 TYR A CG 1 ATOM 970 C CD1 . TYR A 1 145 ? -20.636 50.691 19.618 1.00 34.46 ? 122 TYR A CD1 1 ATOM 971 C CD2 . TYR A 1 145 ? -20.590 48.371 20.170 1.00 34.78 ? 122 TYR A CD2 1 ATOM 972 C CE1 . TYR A 1 145 ? -21.310 50.405 18.446 1.00 27.11 ? 122 TYR A CE1 1 ATOM 973 C CE2 . TYR A 1 145 ? -21.262 48.075 19.001 1.00 37.24 ? 122 TYR A CE2 1 ATOM 974 C CZ . TYR A 1 145 ? -21.621 49.094 18.143 1.00 37.67 ? 122 TYR A CZ 1 ATOM 975 O OH . TYR A 1 145 ? -22.289 48.797 16.979 1.00 42.23 ? 122 TYR A OH 1 ATOM 976 N N . GLN A 1 146 ? -20.698 48.145 23.982 1.00 44.14 ? 123 GLN A N 1 ATOM 977 C CA . GLN A 1 146 ? -21.447 46.982 24.447 1.00 48.13 ? 123 GLN A CA 1 ATOM 978 C C . GLN A 1 146 ? -22.334 47.343 25.632 1.00 42.16 ? 123 GLN A C 1 ATOM 979 O O . GLN A 1 146 ? -23.460 46.857 25.747 1.00 39.81 ? 123 GLN A O 1 ATOM 980 C CB . GLN A 1 146 ? -20.506 45.834 24.820 1.00 39.25 ? 123 GLN A CB 1 ATOM 981 C CG . GLN A 1 146 ? -19.694 45.306 23.650 1.00 37.38 ? 123 GLN A CG 1 ATOM 982 C CD . GLN A 1 146 ? -19.093 43.941 23.918 1.00 44.00 ? 123 GLN A CD 1 ATOM 983 O OE1 . GLN A 1 146 ? -19.582 43.188 24.760 1.00 49.80 ? 123 GLN A OE1 1 ATOM 984 N NE2 . GLN A 1 146 ? -18.027 43.614 23.198 1.00 45.66 ? 123 GLN A NE2 1 ATOM 985 N N . LEU A 1 147 ? -21.824 48.204 26.506 1.00 38.21 ? 124 LEU A N 1 ATOM 986 C CA . LEU A 1 147 ? -22.590 48.671 27.653 1.00 45.54 ? 124 LEU A CA 1 ATOM 987 C C . LEU A 1 147 ? -23.863 49.364 27.184 1.00 49.79 ? 124 LEU A C 1 ATOM 988 O O . LEU A 1 147 ? -24.918 49.242 27.810 1.00 44.20 ? 124 LEU A O 1 ATOM 989 C CB . LEU A 1 147 ? -21.757 49.632 28.499 1.00 54.45 ? 124 LEU A CB 1 ATOM 990 C CG . LEU A 1 147 ? -22.200 49.795 29.952 1.00 59.07 ? 124 LEU A CG 1 ATOM 991 C CD1 . LEU A 1 147 ? -21.885 48.534 30.743 1.00 57.47 ? 124 LEU A CD1 1 ATOM 992 C CD2 . LEU A 1 147 ? -21.542 51.006 30.583 1.00 59.05 ? 124 LEU A CD2 1 ATOM 993 N N . SER A 1 148 ? -23.756 50.086 26.072 1.00 42.83 ? 125 SER A N 1 ATOM 994 C CA . SER A 1 148 ? -24.905 50.762 25.483 1.00 45.85 ? 125 SER A CA 1 ATOM 995 C C . SER A 1 148 ? -25.842 49.739 24.861 1.00 39.86 ? 125 SER A C 1 ATOM 996 O O . SER A 1 148 ? -27.062 49.853 24.971 1.00 47.22 ? 125 SER A O 1 ATOM 997 C CB . SER A 1 148 ? -24.453 51.768 24.424 1.00 36.71 ? 125 SER A CB 1 ATOM 998 O OG . SER A 1 148 ? -23.574 52.730 24.974 1.00 38.68 ? 125 SER A OG 1 ATOM 999 N N . LEU A 1 149 ? -25.260 48.744 24.199 1.00 35.30 ? 126 LEU A N 1 ATOM 1000 C CA . LEU A 1 149 ? -26.035 47.632 23.662 1.00 35.19 ? 126 LEU A CA 1 ATOM 1001 C C . LEU A 1 149 ? -26.810 46.941 24.781 1.00 32.84 ? 126 LEU A C 1 ATOM 1002 O O . LEU A 1 149 ? -27.964 46.556 24.599 1.00 35.62 ? 126 LEU A O 1 ATOM 1003 C CB . LEU A 1 149 ? -25.124 46.627 22.950 1.00 33.87 ? 126 LEU A CB 1 ATOM 1004 C CG . LEU A 1 149 ? -24.659 46.963 21.532 1.00 40.25 ? 126 LEU A CG 1 ATOM 1005 C CD1 . LEU A 1 149 ? -23.636 45.946 21.042 1.00 28.79 ? 126 LEU A CD1 1 ATOM 1006 C CD2 . LEU A 1 149 ? -25.847 47.016 20.590 1.00 34.02 ? 126 LEU A CD2 1 ATOM 1007 N N . ASP A 1 150 ? -26.171 46.799 25.940 1.00 33.03 ? 127 ASP A N 1 ATOM 1008 C CA . ASP A 1 150 ? -26.797 46.148 27.089 1.00 44.05 ? 127 ASP A CA 1 ATOM 1009 C C . ASP A 1 150 ? -28.029 46.903 27.569 1.00 42.37 ? 127 ASP A C 1 ATOM 1010 O O . ASP A 1 150 ? -29.105 46.323 27.716 1.00 46.68 ? 127 ASP A O 1 ATOM 1011 C CB . ASP A 1 150 ? -25.799 46.007 28.238 1.00 41.33 ? 127 ASP A CB 1 ATOM 1012 C CG . ASP A 1 150 ? -24.627 45.118 27.886 1.00 46.46 ? 127 ASP A CG 1 ATOM 1013 O OD1 . ASP A 1 150 ? -24.783 44.248 27.004 1.00 42.51 ? 127 ASP A OD1 1 ATOM 1014 O OD2 . ASP A 1 150 ? -23.547 45.296 28.487 1.00 46.05 ? 127 ASP A OD2 1 ATOM 1015 N N . VAL A 1 151 ? -27.861 48.197 27.817 1.00 39.41 ? 128 VAL A N 1 ATOM 1016 C CA . VAL A 1 151 ? -28.961 49.036 28.271 1.00 34.96 ? 128 VAL A CA 1 ATOM 1017 C C . VAL A 1 151 ? -30.082 49.067 27.236 1.00 43.53 ? 128 VAL A C 1 ATOM 1018 O O . VAL A 1 151 ? -31.259 48.984 27.584 1.00 44.40 ? 128 VAL A O 1 ATOM 1019 C CB . VAL A 1 151 ? -28.485 50.471 28.575 1.00 38.55 ? 128 VAL A CB 1 ATOM 1020 C CG1 . VAL A 1 151 ? -29.662 51.360 28.952 1.00 42.19 ? 128 VAL A CG1 1 ATOM 1021 C CG2 . VAL A 1 151 ? -27.448 50.454 29.687 1.00 37.89 ? 128 VAL A CG2 1 ATOM 1022 N N . LEU A 1 152 ? -29.708 49.167 25.963 1.00 40.60 ? 129 LEU A N 1 ATOM 1023 C CA . LEU A 1 152 ? -30.680 49.212 24.875 1.00 38.88 ? 129 LEU A CA 1 ATOM 1024 C C . LEU A 1 152 ? -31.557 47.964 24.857 1.00 43.54 ? 129 LEU A C 1 ATOM 1025 O O . LEU A 1 152 ? -32.784 48.057 24.797 1.00 43.84 ? 129 LEU A O 1 ATOM 1026 C CB . LEU A 1 152 ? -29.970 49.379 23.528 1.00 39.96 ? 129 LEU A CB 1 ATOM 1027 C CG . LEU A 1 152 ? -30.836 49.368 22.265 1.00 41.54 ? 129 LEU A CG 1 ATOM 1028 C CD1 . LEU A 1 152 ? -31.892 50.463 22.317 1.00 34.68 ? 129 LEU A CD1 1 ATOM 1029 C CD2 . LEU A 1 152 ? -29.969 49.516 21.018 1.00 40.24 ? 129 LEU A CD2 1 ATOM 1030 N N . ALA A 1 153 ? -30.918 46.800 24.921 1.00 44.45 ? 130 ALA A N 1 ATOM 1031 C CA . ALA A 1 153 ? -31.628 45.526 24.891 1.00 46.25 ? 130 ALA A CA 1 ATOM 1032 C C . ALA A 1 153 ? -32.515 45.334 26.121 1.00 44.52 ? 130 ALA A C 1 ATOM 1033 O O . ALA A 1 153 ? -33.670 44.925 26.000 1.00 45.61 ? 130 ALA A O 1 ATOM 1034 C CB . ALA A 1 153 ? -30.643 44.374 24.757 1.00 40.47 ? 130 ALA A CB 1 ATOM 1035 N N . LEU A 1 154 ? -31.972 45.630 27.299 1.00 38.20 ? 131 LEU A N 1 ATOM 1036 C CA . LEU A 1 154 ? -32.727 45.523 28.544 1.00 42.27 ? 131 LEU A CA 1 ATOM 1037 C C . LEU A 1 154 ? -33.920 46.473 28.557 1.00 47.49 ? 131 LEU A C 1 ATOM 1038 O O . LEU A 1 154 ? -34.987 46.141 29.076 1.00 47.84 ? 131 LEU A O 1 ATOM 1039 C CB . LEU A 1 154 ? -31.825 45.804 29.748 1.00 32.89 ? 131 LEU A CB 1 ATOM 1040 C CG . LEU A 1 154 ? -30.738 44.769 30.037 1.00 39.82 ? 131 LEU A CG 1 ATOM 1041 C CD1 . LEU A 1 154 ? -29.802 45.264 31.130 1.00 32.57 ? 131 LEU A CD1 1 ATOM 1042 C CD2 . LEU A 1 154 ? -31.363 43.439 30.422 1.00 46.32 ? 131 LEU A CD2 1 ATOM 1043 N N . CYS A 1 155 ? -33.730 47.655 27.980 1.00 46.04 ? 132 CYS A N 1 ATOM 1044 C CA . CYS A 1 155 ? -34.787 48.656 27.895 1.00 40.38 ? 132 CYS A CA 1 ATOM 1045 C C . CYS A 1 155 ? -35.903 48.244 26.936 1.00 41.58 ? 132 CYS A C 1 ATOM 1046 O O . CYS A 1 155 ? -37.085 48.339 27.268 1.00 45.07 ? 132 CYS A O 1 ATOM 1047 C CB . CYS A 1 155 ? -34.204 50.004 27.467 1.00 39.50 ? 132 CYS A CB 1 ATOM 1048 S SG . CYS A 1 155 ? -35.439 51.247 27.075 1.00 39.96 ? 132 CYS A SG 1 ATOM 1049 N N . LEU A 1 156 ? -35.522 47.786 25.746 1.00 39.78 ? 133 LEU A N 1 ATOM 1050 C CA . LEU A 1 156 ? -36.488 47.390 24.722 1.00 41.57 ? 133 LEU A CA 1 ATOM 1051 C C . LEU A 1 156 ? -37.312 46.162 25.108 1.00 48.04 ? 133 LEU A C 1 ATOM 1052 O O . LEU A 1 156 ? -38.427 45.981 24.620 1.00 47.06 ? 133 LEU A O 1 ATOM 1053 C CB . LEU A 1 156 ? -35.778 47.125 23.394 1.00 38.96 ? 133 LEU A CB 1 ATOM 1054 C CG . LEU A 1 156 ? -35.280 48.342 22.616 1.00 44.18 ? 133 LEU A CG 1 ATOM 1055 C CD1 . LEU A 1 156 ? -34.421 47.906 21.436 1.00 38.62 ? 133 LEU A CD1 1 ATOM 1056 C CD2 . LEU A 1 156 ? -36.461 49.172 22.141 1.00 30.16 ? 133 LEU A CD2 1 ATOM 1057 N N . PHE A 1 157 ? -36.762 45.318 25.975 1.00 42.79 ? 134 PHE A N 1 ATOM 1058 C CA . PHE A 1 157 ? -37.428 44.064 26.322 1.00 56.14 ? 134 PHE A CA 1 ATOM 1059 C C . PHE A 1 157 ? -37.821 43.984 27.795 1.00 55.22 ? 134 PHE A C 1 ATOM 1060 O O . PHE A 1 157 ? -37.975 42.895 28.348 1.00 59.42 ? 134 PHE A O 1 ATOM 1061 C CB . PHE A 1 157 ? -36.568 42.865 25.905 1.00 46.92 ? 134 PHE A CB 1 ATOM 1062 C CG . PHE A 1 157 ? -36.377 42.757 24.421 1.00 41.33 ? 134 PHE A CG 1 ATOM 1063 C CD1 . PHE A 1 157 ? -35.370 43.464 23.786 1.00 41.02 ? 134 PHE A CD1 1 ATOM 1064 C CD2 . PHE A 1 157 ? -37.217 41.965 23.656 1.00 51.33 ? 134 PHE A CD2 1 ATOM 1065 C CE1 . PHE A 1 157 ? -35.198 43.378 22.417 1.00 47.06 ? 134 PHE A CE1 1 ATOM 1066 C CE2 . PHE A 1 157 ? -37.048 41.873 22.286 1.00 55.25 ? 134 PHE A CE2 1 ATOM 1067 C CZ . PHE A 1 157 ? -36.039 42.583 21.666 1.00 38.28 ? 134 PHE A CZ 1 ATOM 1068 N N . ASN A 1 158 ? -37.987 45.151 28.412 1.00 50.93 ? 135 ASN A N 1 ATOM 1069 C CA . ASN A 1 158 ? -38.472 45.255 29.785 1.00 57.20 ? 135 ASN A CA 1 ATOM 1070 C C . ASN A 1 158 ? -37.646 44.466 30.794 1.00 58.90 ? 135 ASN A C 1 ATOM 1071 O O . ASN A 1 158 ? -38.190 43.869 31.721 1.00 59.02 ? 135 ASN A O 1 ATOM 1072 C CB . ASN A 1 158 ? -39.942 44.834 29.870 1.00 66.25 ? 135 ASN A CB 1 ATOM 1073 C CG . ASN A 1 158 ? -40.851 45.730 29.055 1.00 77.57 ? 135 ASN A CG 1 ATOM 1074 O OD1 . ASN A 1 158 ? -41.449 45.295 28.071 1.00 84.87 ? 135 ASN A OD1 1 ATOM 1075 N ND2 . ASN A 1 158 ? -40.961 46.989 29.462 1.00 79.11 ? 135 ASN A ND2 1 ATOM 1076 N N . GLY A 1 159 ? -36.332 44.460 30.602 1.00 56.64 ? 136 GLY A N 1 ATOM 1077 C CA . GLY A 1 159 ? -35.436 43.820 31.544 1.00 48.35 ? 136 GLY A CA 1 ATOM 1078 C C . GLY A 1 159 ? -35.206 44.722 32.738 1.00 54.76 ? 136 GLY A C 1 ATOM 1079 O O . GLY A 1 159 ? -35.496 45.917 32.683 1.00 62.19 ? 136 GLY A O 1 ATOM 1080 N N . ASN A 1 160 ? -34.686 44.156 33.820 1.00 56.59 ? 137 ASN A N 1 ATOM 1081 C CA . ASN A 1 160 ? -34.448 44.927 35.032 1.00 60.95 ? 137 ASN A CA 1 ATOM 1082 C C . ASN A 1 160 ? -33.075 45.592 35.022 1.00 62.31 ? 137 ASN A C 1 ATOM 1083 O O . ASN A 1 160 ? -32.046 44.918 34.989 1.00 62.74 ? 137 ASN A O 1 ATOM 1084 C CB . ASN A 1 160 ? -34.615 44.046 36.273 1.00 75.98 ? 137 ASN A CB 1 ATOM 1085 C CG . ASN A 1 160 ? -34.839 44.854 37.539 1.00 93.32 ? 137 ASN A CG 1 ATOM 1086 O OD1 . ASN A 1 160 ? -34.150 45.842 37.794 1.00 93.24 ? 137 ASN A OD1 1 ATOM 1087 N ND2 . ASN A 1 160 ? -35.816 44.438 38.338 1.00 101.67 ? 137 ASN A ND2 1 ATOM 1088 N N . TYR A 1 161 ? -33.071 46.920 35.042 1.00 58.08 ? 138 TYR A N 1 ATOM 1089 C CA . TYR A 1 161 ? -31.836 47.690 35.080 1.00 58.74 ? 138 TYR A CA 1 ATOM 1090 C C . TYR A 1 161 ? -32.044 48.956 35.902 1.00 62.11 ? 138 TYR A C 1 ATOM 1091 O O . TYR A 1 161 ? -33.152 49.487 35.967 1.00 61.21 ? 138 TYR A O 1 ATOM 1092 C CB . TYR A 1 161 ? -31.372 48.048 33.663 1.00 55.14 ? 138 TYR A CB 1 ATOM 1093 C CG . TYR A 1 161 ? -32.343 48.918 32.894 1.00 61.39 ? 138 TYR A CG 1 ATOM 1094 C CD1 . TYR A 1 161 ? -33.414 48.357 32.211 1.00 65.46 ? 138 TYR A CD1 1 ATOM 1095 C CD2 . TYR A 1 161 ? -32.187 50.300 32.847 1.00 52.41 ? 138 TYR A CD2 1 ATOM 1096 C CE1 . TYR A 1 161 ? -34.304 49.142 31.508 1.00 68.20 ? 138 TYR A CE1 1 ATOM 1097 C CE2 . TYR A 1 161 ? -33.075 51.096 32.144 1.00 50.55 ? 138 TYR A CE2 1 ATOM 1098 C CZ . TYR A 1 161 ? -34.132 50.509 31.476 1.00 61.77 ? 138 TYR A CZ 1 ATOM 1099 O OH . TYR A 1 161 ? -35.026 51.281 30.773 1.00 57.22 ? 138 TYR A OH 1 ATOM 1100 N N . SER A 1 162 ? -30.977 49.435 36.531 1.00 64.04 ? 139 SER A N 1 ATOM 1101 C CA . SER A 1 162 ? -31.055 50.648 37.333 1.00 61.57 ? 139 SER A CA 1 ATOM 1102 C C . SER A 1 162 ? -30.808 51.882 36.476 1.00 60.91 ? 139 SER A C 1 ATOM 1103 O O . SER A 1 162 ? -29.751 52.017 35.861 1.00 65.75 ? 139 SER A O 1 ATOM 1104 C CB . SER A 1 162 ? -30.044 50.601 38.478 1.00 66.54 ? 139 SER A CB 1 ATOM 1105 O OG . SER A 1 162 ? -30.054 51.814 39.210 1.00 71.70 ? 139 SER A OG 1 ATOM 1106 N N . THR A 1 163 ? -31.787 52.781 36.435 1.00 48.74 ? 140 THR A N 1 ATOM 1107 C CA . THR A 1 163 ? -31.637 54.026 35.696 1.00 45.89 ? 140 THR A CA 1 ATOM 1108 C C . THR A 1 163 ? -30.580 54.900 36.359 1.00 53.98 ? 140 THR A C 1 ATOM 1109 O O . THR A 1 163 ? -29.871 55.649 35.689 1.00 57.48 ? 140 THR A O 1 ATOM 1110 C CB . THR A 1 163 ? -32.958 54.807 35.615 1.00 57.42 ? 140 THR A CB 1 ATOM 1111 O OG1 . THR A 1 163 ? -33.400 55.131 36.938 1.00 79.17 ? 140 THR A OG1 1 ATOM 1112 C CG2 . THR A 1 163 ? -34.024 53.980 34.914 1.00 51.73 ? 140 THR A CG2 1 ATOM 1113 N N . ALA A 1 164 ? -30.484 54.796 37.681 1.00 55.15 ? 141 ALA A N 1 ATOM 1114 C CA . ALA A 1 164 ? -29.466 55.515 38.436 1.00 52.97 ? 141 ALA A CA 1 ATOM 1115 C C . ALA A 1 164 ? -28.080 55.063 37.998 1.00 56.36 ? 141 ALA A C 1 ATOM 1116 O O . ALA A 1 164 ? -27.158 55.871 37.889 1.00 51.85 ? 141 ALA A O 1 ATOM 1117 C CB . ALA A 1 164 ? -29.653 55.287 39.926 1.00 46.97 ? 141 ALA A CB 1 ATOM 1118 N N . GLU A 1 165 ? -27.947 53.766 37.742 1.00 60.42 ? 142 GLU A N 1 ATOM 1119 C CA . GLU A 1 165 ? -26.698 53.197 37.255 1.00 69.20 ? 142 GLU A CA 1 ATOM 1120 C C . GLU A 1 165 ? -26.345 53.801 35.899 1.00 59.59 ? 142 GLU A C 1 ATOM 1121 O O . GLU A 1 165 ? -25.182 54.086 35.617 1.00 57.89 ? 142 GLU A O 1 ATOM 1122 C CB . GLU A 1 165 ? -26.823 51.679 37.129 1.00 80.40 ? 142 GLU A CB 1 ATOM 1123 C CG . GLU A 1 165 ? -25.541 50.919 37.415 1.00 88.50 ? 142 GLU A CG 1 ATOM 1124 C CD . GLU A 1 165 ? -25.287 50.751 38.899 1.00 88.85 ? 142 GLU A CD 1 ATOM 1125 O OE1 . GLU A 1 165 ? -25.983 49.927 39.530 1.00 91.89 ? 142 GLU A OE1 1 ATOM 1126 O OE2 . GLU A 1 165 ? -24.397 51.444 39.435 1.00 83.09 ? 142 GLU A OE2 1 ATOM 1127 N N . VAL A 1 166 ? -27.364 53.995 35.067 1.00 51.13 ? 143 VAL A N 1 ATOM 1128 C CA . VAL A 1 166 ? -27.186 54.588 33.746 1.00 50.67 ? 143 VAL A CA 1 ATOM 1129 C C . VAL A 1 166 ? -26.741 56.044 33.848 1.00 48.03 ? 143 VAL A C 1 ATOM 1130 O O . VAL A 1 166 ? -25.770 56.453 33.209 1.00 46.97 ? 143 VAL A O 1 ATOM 1131 C CB . VAL A 1 166 ? -28.484 54.501 32.922 1.00 49.12 ? 143 VAL A CB 1 ATOM 1132 C CG1 . VAL A 1 166 ? -28.352 55.292 31.634 1.00 50.34 ? 143 VAL A CG1 1 ATOM 1133 C CG2 . VAL A 1 166 ? -28.830 53.049 32.635 1.00 49.78 ? 143 VAL A CG2 1 ATOM 1134 N N . VAL A 1 167 ? -27.455 56.818 34.660 1.00 52.64 ? 144 VAL A N 1 ATOM 1135 C CA . VAL A 1 167 ? -27.108 58.213 34.913 1.00 57.36 ? 144 VAL A CA 1 ATOM 1136 C C . VAL A 1 167 ? -25.690 58.327 35.468 1.00 58.14 ? 144 VAL A C 1 ATOM 1137 O O . VAL A 1 167 ? -24.950 59.258 35.142 1.00 54.80 ? 144 VAL A O 1 ATOM 1138 C CB . VAL A 1 167 ? -28.105 58.862 35.901 1.00 54.01 ? 144 VAL A CB 1 ATOM 1139 C CG1 . VAL A 1 167 ? -27.689 60.288 36.238 1.00 50.65 ? 144 VAL A CG1 1 ATOM 1140 C CG2 . VAL A 1 167 ? -29.511 58.839 35.325 1.00 57.34 ? 144 VAL A CG2 1 ATOM 1141 N N . ASN A 1 168 ? -25.309 57.359 36.294 1.00 54.86 ? 145 ASN A N 1 ATOM 1142 C CA . ASN A 1 168 ? -24.000 57.368 36.932 1.00 60.97 ? 145 ASN A CA 1 ATOM 1143 C C . ASN A 1 168 ? -22.847 57.127 35.955 1.00 63.59 ? 145 ASN A C 1 ATOM 1144 O O . ASN A 1 168 ? -21.804 57.771 36.052 1.00 65.71 ? 145 ASN A O 1 ATOM 1145 C CB . ASN A 1 168 ? -23.957 56.335 38.062 1.00 67.99 ? 145 ASN A CB 1 ATOM 1146 C CG . ASN A 1 168 ? -22.999 56.722 39.172 1.00 88.28 ? 145 ASN A CG 1 ATOM 1147 O OD1 . ASN A 1 168 ? -23.394 56.841 40.332 1.00 100.93 ? 145 ASN A OD1 1 ATOM 1148 N ND2 . ASN A 1 168 ? -21.732 56.919 38.823 1.00 89.47 ? 145 ASN A ND2 1 ATOM 1149 N N . HIS A 1 169 ? -23.040 56.213 35.009 1.00 49.37 ? 146 HIS A N 1 ATOM 1150 C CA . HIS A 1 169 ? -21.936 55.765 34.161 1.00 49.49 ? 146 HIS A CA 1 ATOM 1151 C C . HIS A 1 169 ? -21.900 56.354 32.749 1.00 48.69 ? 146 HIS A C 1 ATOM 1152 O O . HIS A 1 169 ? -20.839 56.407 32.127 1.00 50.05 ? 146 HIS A O 1 ATOM 1153 C CB . HIS A 1 169 ? -21.909 54.235 34.084 1.00 53.70 ? 146 HIS A CB 1 ATOM 1154 C CG . HIS A 1 169 ? -21.631 53.571 35.396 1.00 55.96 ? 146 HIS A CG 1 ATOM 1155 N ND1 . HIS A 1 169 ? -20.382 53.566 35.978 1.00 55.07 ? 146 HIS A ND1 1 ATOM 1156 C CD2 . HIS A 1 169 ? -22.442 52.890 36.241 1.00 46.73 ? 146 HIS A CD2 1 ATOM 1157 C CE1 . HIS A 1 169 ? -20.434 52.911 37.124 1.00 55.88 ? 146 HIS A CE1 1 ATOM 1158 N NE2 . HIS A 1 169 ? -21.673 52.490 37.306 1.00 59.32 ? 146 HIS A NE2 1 ATOM 1159 N N . PHE A 1 170 ? -23.046 56.797 32.242 1.00 48.45 ? 147 PHE A N 1 ATOM 1160 C CA . PHE A 1 170 ? -23.129 57.230 30.847 1.00 45.32 ? 147 PHE A CA 1 ATOM 1161 C C . PHE A 1 170 ? -22.857 58.717 30.617 1.00 42.02 ? 147 PHE A C 1 ATOM 1162 O O . PHE A 1 170 ? -23.151 59.243 29.544 1.00 43.12 ? 147 PHE A O 1 ATOM 1163 C CB . PHE A 1 170 ? -24.474 56.829 30.234 1.00 47.62 ? 147 PHE A CB 1 ATOM 1164 C CG . PHE A 1 170 ? -24.533 55.394 29.791 1.00 51.05 ? 147 PHE A CG 1 ATOM 1165 C CD1 . PHE A 1 170 ? -24.715 54.376 30.714 1.00 50.64 ? 147 PHE A CD1 1 ATOM 1166 C CD2 . PHE A 1 170 ? -24.404 55.063 28.450 1.00 44.77 ? 147 PHE A CD2 1 ATOM 1167 C CE1 . PHE A 1 170 ? -24.767 53.053 30.309 1.00 46.27 ? 147 PHE A CE1 1 ATOM 1168 C CE2 . PHE A 1 170 ? -24.455 53.743 28.040 1.00 47.58 ? 147 PHE A CE2 1 ATOM 1169 C CZ . PHE A 1 170 ? -24.637 52.736 28.971 1.00 42.33 ? 147 PHE A CZ 1 ATOM 1170 N N . THR A 1 171 ? -22.295 59.384 31.621 1.00 42.44 ? 148 THR A N 1 ATOM 1171 C CA . THR A 1 171 ? -21.906 60.787 31.498 1.00 49.36 ? 148 THR A CA 1 ATOM 1172 C C . THR A 1 171 ? -20.973 60.993 30.307 1.00 49.21 ? 148 THR A C 1 ATOM 1173 O O . THR A 1 171 ? -19.966 60.300 30.178 1.00 51.84 ? 148 THR A O 1 ATOM 1174 C CB . THR A 1 171 ? -21.185 61.275 32.763 1.00 55.92 ? 148 THR A CB 1 ATOM 1175 O OG1 . THR A 1 171 ? -21.739 60.626 33.914 1.00 75.64 ? 148 THR A OG1 1 ATOM 1176 C CG2 . THR A 1 171 ? -21.323 62.785 32.910 1.00 51.25 ? 148 THR A CG2 1 ATOM 1177 N N . PRO A 1 172 ? -21.305 61.956 29.435 1.00 55.85 ? 149 PRO A N 1 ATOM 1178 C CA . PRO A 1 172 ? -20.565 62.225 28.195 1.00 60.92 ? 149 PRO A CA 1 ATOM 1179 C C . PRO A 1 172 ? -19.076 62.505 28.404 1.00 53.57 ? 149 PRO A C 1 ATOM 1180 O O . PRO A 1 172 ? -18.299 62.391 27.456 1.00 58.01 ? 149 PRO A O 1 ATOM 1181 C CB . PRO A 1 172 ? -21.257 63.474 27.645 1.00 62.93 ? 149 PRO A CB 1 ATOM 1182 C CG . PRO A 1 172 ? -22.633 63.405 28.196 1.00 65.53 ? 149 PRO A CG 1 ATOM 1183 C CD . PRO A 1 172 ? -22.480 62.832 29.569 1.00 59.42 ? 149 PRO A CD 1 ATOM 1184 N N . GLU A 1 173 ? -18.685 62.865 29.620 1.00 53.57 ? 150 GLU A N 1 ATOM 1185 C CA . GLU A 1 173 ? -17.286 63.168 29.896 1.00 64.27 ? 150 GLU A CA 1 ATOM 1186 C C . GLU A 1 173 ? -16.508 61.928 30.334 1.00 56.50 ? 150 GLU A C 1 ATOM 1187 O O . GLU A 1 173 ? -15.294 61.988 30.528 1.00 60.96 ? 150 GLU A O 1 ATOM 1188 C CB . GLU A 1 173 ? -17.166 64.284 30.939 1.00 76.37 ? 150 GLU A CB 1 ATOM 1189 C CG . GLU A 1 173 ? -17.813 65.600 30.515 1.00 87.86 ? 150 GLU A CG 1 ATOM 1190 C CD . GLU A 1 173 ? -17.219 66.168 29.234 1.00 94.79 ? 150 GLU A CD 1 ATOM 1191 O OE1 . GLU A 1 173 ? -16.002 65.999 29.011 1.00 98.05 ? 150 GLU A OE1 1 ATOM 1192 O OE2 . GLU A 1 173 ? -17.974 66.781 28.449 1.00 91.60 ? 150 GLU A OE2 1 ATOM 1193 N N . ASN A 1 174 ? -17.211 60.808 30.482 1.00 46.12 ? 151 ASN A N 1 ATOM 1194 C CA . ASN A 1 174 ? -16.576 59.547 30.853 1.00 47.04 ? 151 ASN A CA 1 ATOM 1195 C C . ASN A 1 174 ? -15.530 59.134 29.826 1.00 51.59 ? 151 ASN A C 1 ATOM 1196 O O . ASN A 1 174 ? -15.755 59.243 28.621 1.00 52.53 ? 151 ASN A O 1 ATOM 1197 C CB . ASN A 1 174 ? -17.616 58.437 31.011 1.00 45.27 ? 151 ASN A CB 1 ATOM 1198 C CG . ASN A 1 174 ? -17.031 57.169 31.604 1.00 49.48 ? 151 ASN A CG 1 ATOM 1199 O OD1 . ASN A 1 174 ? -16.368 56.392 30.915 1.00 52.60 ? 151 ASN A OD1 1 ATOM 1200 N ND2 . ASN A 1 174 ? -17.281 56.950 32.889 1.00 43.05 ? 151 ASN A ND2 1 ATOM 1201 N N . LYS A 1 175 ? -14.392 58.654 30.315 1.00 47.73 ? 152 LYS A N 1 ATOM 1202 C CA . LYS A 1 175 ? -13.251 58.339 29.461 1.00 54.20 ? 152 LYS A CA 1 ATOM 1203 C C . LYS A 1 175 ? -13.551 57.253 28.430 1.00 49.18 ? 152 LYS A C 1 ATOM 1204 O O . LYS A 1 175 ? -12.925 57.206 27.371 1.00 55.22 ? 152 LYS A O 1 ATOM 1205 C CB . LYS A 1 175 ? -12.049 57.926 30.315 1.00 67.86 ? 152 LYS A CB 1 ATOM 1206 C CG . LYS A 1 175 ? -12.306 56.721 31.207 1.00 75.58 ? 152 LYS A CG 1 ATOM 1207 C CD . LYS A 1 175 ? -11.059 56.324 31.982 1.00 84.21 ? 152 LYS A CD 1 ATOM 1208 C CE . LYS A 1 175 ? -11.313 55.093 32.839 1.00 86.49 ? 152 LYS A CE 1 ATOM 1209 N NZ . LYS A 1 175 ? -10.094 54.666 33.582 1.00 94.83 ? 152 LYS A NZ 1 ATOM 1210 N N . ASN A 1 176 ? -14.514 56.390 28.736 1.00 46.21 ? 153 ASN A N 1 ATOM 1211 C CA . ASN A 1 176 ? -14.815 55.250 27.877 1.00 46.80 ? 153 ASN A CA 1 ATOM 1212 C C . ASN A 1 176 ? -15.473 55.620 26.553 1.00 44.75 ? 153 ASN A C 1 ATOM 1213 O O . ASN A 1 176 ? -15.689 54.760 25.699 1.00 46.07 ? 153 ASN A O 1 ATOM 1214 C CB . ASN A 1 176 ? -15.670 54.225 28.621 1.00 45.26 ? 153 ASN A CB 1 ATOM 1215 C CG . ASN A 1 176 ? -14.909 53.535 29.731 1.00 55.14 ? 153 ASN A CG 1 ATOM 1216 O OD1 . ASN A 1 176 ? -14.114 52.631 29.481 1.00 51.17 ? 153 ASN A OD1 1 ATOM 1217 N ND2 . ASN A 1 176 ? -15.150 53.957 30.968 1.00 49.53 ? 153 ASN A ND2 1 ATOM 1218 N N . TYR A 1 177 ? -15.793 56.899 26.389 1.00 39.47 ? 154 TYR A N 1 ATOM 1219 C CA . TYR A 1 177 ? -16.333 57.392 25.131 1.00 45.41 ? 154 TYR A CA 1 ATOM 1220 C C . TYR A 1 177 ? -15.203 57.728 24.167 1.00 43.52 ? 154 TYR A C 1 ATOM 1221 O O . TYR A 1 177 ? -15.442 58.032 22.999 1.00 43.98 ? 154 TYR A O 1 ATOM 1222 C CB . TYR A 1 177 ? -17.190 58.637 25.364 1.00 40.59 ? 154 TYR A CB 1 ATOM 1223 C CG . TYR A 1 177 ? -18.583 58.359 25.882 1.00 37.82 ? 154 TYR A CG 1 ATOM 1224 C CD1 . TYR A 1 177 ? -19.553 57.800 25.060 1.00 35.34 ? 154 TYR A CD1 1 ATOM 1225 C CD2 . TYR A 1 177 ? -18.936 58.681 27.186 1.00 37.14 ? 154 TYR A CD2 1 ATOM 1226 C CE1 . TYR A 1 177 ? -20.834 57.556 25.527 1.00 37.23 ? 154 TYR A CE1 1 ATOM 1227 C CE2 . TYR A 1 177 ? -20.212 58.441 27.661 1.00 43.18 ? 154 TYR A CE2 1 ATOM 1228 C CZ . TYR A 1 177 ? -21.156 57.880 26.828 1.00 45.39 ? 154 TYR A CZ 1 ATOM 1229 O OH . TYR A 1 177 ? -22.426 57.643 27.304 1.00 44.00 ? 154 TYR A OH 1 ATOM 1230 N N . TYR A 1 178 ? -13.971 57.669 24.665 1.00 45.96 ? 155 TYR A N 1 ATOM 1231 C CA . TYR A 1 178 ? -12.811 58.100 23.892 1.00 49.13 ? 155 TYR A CA 1 ATOM 1232 C C . TYR A 1 178 ? -11.746 57.013 23.778 1.00 51.31 ? 155 TYR A C 1 ATOM 1233 O O . TYR A 1 178 ? -11.430 56.330 24.751 1.00 59.37 ? 155 TYR A O 1 ATOM 1234 C CB . TYR A 1 178 ? -12.199 59.359 24.515 1.00 46.85 ? 155 TYR A CB 1 ATOM 1235 C CG . TYR A 1 178 ? -13.194 60.477 24.733 1.00 51.43 ? 155 TYR A CG 1 ATOM 1236 C CD1 . TYR A 1 178 ? -13.930 60.558 25.908 1.00 44.60 ? 155 TYR A CD1 1 ATOM 1237 C CD2 . TYR A 1 178 ? -13.400 61.449 23.763 1.00 50.43 ? 155 TYR A CD2 1 ATOM 1238 C CE1 . TYR A 1 178 ? -14.843 61.575 26.111 1.00 50.77 ? 155 TYR A CE1 1 ATOM 1239 C CE2 . TYR A 1 178 ? -14.312 62.471 23.957 1.00 50.16 ? 155 TYR A CE2 1 ATOM 1240 C CZ . TYR A 1 178 ? -15.030 62.527 25.133 1.00 56.65 ? 155 TYR A CZ 1 ATOM 1241 O OH . TYR A 1 178 ? -15.939 63.539 25.336 1.00 66.49 ? 155 TYR A OH 1 ATOM 1242 N N . PHE A 1 179 ? -11.203 56.855 22.576 1.00 56.91 ? 156 PHE A N 1 ATOM 1243 C CA . PHE A 1 179 ? -10.055 55.987 22.362 1.00 56.26 ? 156 PHE A CA 1 ATOM 1244 C C . PHE A 1 179 ? -8.850 56.868 22.073 1.00 62.60 ? 156 PHE A C 1 ATOM 1245 O O . PHE A 1 179 ? -8.593 57.226 20.925 1.00 63.24 ? 156 PHE A O 1 ATOM 1246 C CB . PHE A 1 179 ? -10.308 55.027 21.202 1.00 50.67 ? 156 PHE A CB 1 ATOM 1247 C CG . PHE A 1 179 ? -11.402 54.035 21.467 1.00 53.33 ? 156 PHE A CG 1 ATOM 1248 C CD1 . PHE A 1 179 ? -11.607 53.536 22.742 1.00 61.72 ? 156 PHE A CD1 1 ATOM 1249 C CD2 . PHE A 1 179 ? -12.230 53.607 20.443 1.00 55.70 ? 156 PHE A CD2 1 ATOM 1250 C CE1 . PHE A 1 179 ? -12.615 52.624 22.992 1.00 61.40 ? 156 PHE A CE1 1 ATOM 1251 C CE2 . PHE A 1 179 ? -13.241 52.696 20.686 1.00 54.86 ? 156 PHE A CE2 1 ATOM 1252 C CZ . PHE A 1 179 ? -13.433 52.204 21.962 1.00 54.76 ? 156 PHE A CZ 1 ATOM 1253 N N . GLY A 1 180 ? -8.122 57.221 23.126 1.00 62.54 ? 157 GLY A N 1 ATOM 1254 C CA . GLY A 1 180 ? -7.046 58.185 23.014 1.00 71.57 ? 157 GLY A CA 1 ATOM 1255 C C . GLY A 1 180 ? -7.607 59.590 23.094 1.00 70.86 ? 157 GLY A C 1 ATOM 1256 O O . GLY A 1 180 ? -8.245 59.957 24.082 1.00 64.52 ? 157 GLY A O 1 ATOM 1257 N N . SER A 1 181 ? -7.378 60.376 22.048 1.00 77.40 ? 158 SER A N 1 ATOM 1258 C CA . SER A 1 181 ? -7.918 61.727 21.974 1.00 82.72 ? 158 SER A CA 1 ATOM 1259 C C . SER A 1 181 ? -9.176 61.745 21.113 1.00 78.65 ? 158 SER A C 1 ATOM 1260 O O . SER A 1 181 ? -9.881 62.751 21.045 1.00 83.95 ? 158 SER A O 1 ATOM 1261 C CB . SER A 1 181 ? -6.876 62.687 21.398 1.00 86.24 ? 158 SER A CB 1 ATOM 1262 O OG . SER A 1 181 ? -6.517 62.316 20.077 1.00 85.08 ? 158 SER A OG 1 ATOM 1263 N N . GLN A 1 182 ? -9.454 60.620 20.462 1.00 60.40 ? 159 GLN A N 1 ATOM 1264 C CA . GLN A 1 182 ? -10.563 60.530 19.522 1.00 48.54 ? 159 GLN A CA 1 ATOM 1265 C C . GLN A 1 182 ? -11.868 60.088 20.181 1.00 38.59 ? 159 GLN A C 1 ATOM 1266 O O . GLN A 1 182 ? -11.938 59.021 20.792 1.00 42.70 ? 159 GLN A O 1 ATOM 1267 C CB . GLN A 1 182 ? -10.210 59.576 18.378 1.00 52.45 ? 159 GLN A CB 1 ATOM 1268 C CG . GLN A 1 182 ? -11.340 59.347 17.387 1.00 66.59 ? 159 GLN A CG 1 ATOM 1269 C CD . GLN A 1 182 ? -11.740 60.613 16.655 1.00 81.11 ? 159 GLN A CD 1 ATOM 1270 O OE1 . GLN A 1 182 ? -10.894 61.440 16.311 1.00 93.32 ? 159 GLN A OE1 1 ATOM 1271 N NE2 . GLN A 1 182 ? -13.037 60.774 16.418 1.00 74.23 ? 159 GLN A NE2 1 ATOM 1272 N N . PHE A 1 183 ? -12.905 60.895 20.044 1.00 42.97 ? 160 PHE A N 1 ATOM 1273 C CA . PHE A 1 183 ? -14.221 60.508 20.508 1.00 39.98 ? 160 PHE A CA 1 ATOM 1274 C C . PHE A 1 183 ? -14.732 59.378 19.627 1.00 42.66 ? 160 PHE A C 1 ATOM 1275 O O . PHE A 1 183 ? -14.712 59.478 18.414 1.00 45.82 ? 160 PHE A O 1 ATOM 1276 C CB . PHE A 1 183 ? -15.162 61.704 20.457 1.00 44.50 ? 160 PHE A CB 1 ATOM 1277 C CG . PHE A 1 183 ? -16.609 61.359 20.655 1.00 47.64 ? 160 PHE A CG 1 ATOM 1278 C CD1 . PHE A 1 183 ? -17.114 61.124 21.916 1.00 40.20 ? 160 PHE A CD1 1 ATOM 1279 C CD2 . PHE A 1 183 ? -17.468 61.295 19.579 1.00 38.75 ? 160 PHE A CD2 1 ATOM 1280 C CE1 . PHE A 1 183 ? -18.442 60.824 22.099 1.00 41.89 ? 160 PHE A CE1 1 ATOM 1281 C CE2 . PHE A 1 183 ? -18.797 60.994 19.755 1.00 38.70 ? 160 PHE A CE2 1 ATOM 1282 C CZ . PHE A 1 183 ? -19.287 60.760 21.016 1.00 40.98 ? 160 PHE A CZ 1 ATOM 1283 N N . SER A 1 184 ? -15.165 58.294 20.249 1.00 45.92 ? 161 SER A N 1 ATOM 1284 C CA . SER A 1 184 ? -15.706 57.153 19.517 1.00 43.09 ? 161 SER A CA 1 ATOM 1285 C C . SER A 1 184 ? -17.148 57.417 19.098 1.00 44.48 ? 161 SER A C 1 ATOM 1286 O O . SER A 1 184 ? -18.070 57.336 19.915 1.00 39.50 ? 161 SER A O 1 ATOM 1287 C CB . SER A 1 184 ? -15.623 55.876 20.358 1.00 43.82 ? 161 SER A CB 1 ATOM 1288 O OG . SER A 1 184 ? -16.200 54.775 19.673 1.00 45.60 ? 161 SER A OG 1 ATOM 1289 N N . VAL A 1 185 ? -17.332 57.724 17.824 1.00 38.62 ? 162 VAL A N 1 ATOM 1290 C CA . VAL A 1 185 ? -18.643 58.002 17.270 1.00 37.16 ? 162 VAL A CA 1 ATOM 1291 C C . VAL A 1 185 ? -19.570 56.808 17.432 1.00 39.53 ? 162 VAL A C 1 ATOM 1292 O O . VAL A 1 185 ? -20.719 56.958 17.803 1.00 43.23 ? 162 VAL A O 1 ATOM 1293 C CB . VAL A 1 185 ? -18.532 58.376 15.784 1.00 41.73 ? 162 VAL A CB 1 ATOM 1294 C CG1 . VAL A 1 185 ? -19.903 58.541 15.155 1.00 34.10 ? 162 VAL A CG1 1 ATOM 1295 C CG2 . VAL A 1 185 ? -17.713 59.640 15.629 1.00 41.99 ? 162 VAL A CG2 1 ATOM 1296 N N . ASP A 1 186 ? -19.049 55.622 17.160 1.00 36.17 ? 163 ASP A N 1 ATOM 1297 C CA . ASP A 1 186 ? -19.822 54.387 17.272 1.00 37.75 ? 163 ASP A CA 1 ATOM 1298 C C . ASP A 1 186 ? -20.374 54.233 18.684 1.00 31.67 ? 163 ASP A C 1 ATOM 1299 O O . ASP A 1 186 ? -21.558 53.955 18.879 1.00 37.36 ? 163 ASP A O 1 ATOM 1300 C CB . ASP A 1 186 ? -18.945 53.177 16.941 1.00 41.32 ? 163 ASP A CB 1 ATOM 1301 C CG . ASP A 1 186 ? -18.107 53.379 15.692 1.00 48.12 ? 163 ASP A CG 1 ATOM 1302 O OD1 . ASP A 1 186 ? -17.139 54.167 15.750 1.00 43.65 ? 163 ASP A OD1 1 ATOM 1303 O OD2 . ASP A 1 186 ? -18.405 52.742 14.659 1.00 45.77 ? 163 ASP A OD2 1 ATOM 1304 N N . THR A 1 187 ? -19.498 54.419 19.662 1.00 38.29 ? 164 THR A N 1 ATOM 1305 C CA . THR A 1 187 ? -19.863 54.323 21.066 1.00 34.40 ? 164 THR A CA 1 ATOM 1306 C C . THR A 1 187 ? -20.887 55.390 21.441 1.00 39.39 ? 164 THR A C 1 ATOM 1307 O O . THR A 1 187 ? -21.907 55.091 22.063 1.00 36.11 ? 164 THR A O 1 ATOM 1308 C CB . THR A 1 187 ? -18.618 54.466 21.954 1.00 35.95 ? 164 THR A CB 1 ATOM 1309 O OG1 . THR A 1 187 ? -17.655 53.473 21.582 1.00 42.14 ? 164 THR A OG1 1 ATOM 1310 C CG2 . THR A 1 187 ? -18.981 54.295 23.414 1.00 31.90 ? 164 THR A CG2 1 ATOM 1311 N N . GLY A 1 188 ? -20.609 56.632 21.055 1.00 36.44 ? 165 GLY A N 1 ATOM 1312 C CA . GLY A 1 188 ? -21.522 57.733 21.305 1.00 29.99 ? 165 GLY A CA 1 ATOM 1313 C C . GLY A 1 188 ? -22.885 57.514 20.671 1.00 40.83 ? 165 GLY A C 1 ATOM 1314 O O . GLY A 1 188 ? -23.914 57.817 21.273 1.00 37.53 ? 165 GLY A O 1 ATOM 1315 N N . ALA A 1 189 ? -22.890 56.974 19.456 1.00 32.46 ? 166 ALA A N 1 ATOM 1316 C CA . ALA A 1 189 ? -24.132 56.731 18.734 1.00 34.48 ? 166 ALA A CA 1 ATOM 1317 C C . ALA A 1 189 ? -24.968 55.660 19.420 1.00 36.30 ? 166 ALA A C 1 ATOM 1318 O O . ALA A 1 189 ? -26.174 55.830 19.609 1.00 34.15 ? 166 ALA A O 1 ATOM 1319 C CB . ALA A 1 189 ? -23.846 56.339 17.287 1.00 32.34 ? 166 ALA A CB 1 ATOM 1320 N N . MET A 1 190 ? -24.328 54.557 19.797 1.00 29.04 ? 167 MET A N 1 ATOM 1321 C CA . MET A 1 190 ? -25.043 53.474 20.460 1.00 36.52 ? 167 MET A CA 1 ATOM 1322 C C . MET A 1 190 ? -25.544 53.920 21.832 1.00 35.52 ? 167 MET A C 1 ATOM 1323 O O . MET A 1 190 ? -26.624 53.517 22.269 1.00 39.27 ? 167 MET A O 1 ATOM 1324 C CB . MET A 1 190 ? -24.172 52.220 20.578 1.00 32.32 ? 167 MET A CB 1 ATOM 1325 C CG . MET A 1 190 ? -24.965 50.955 20.921 1.00 34.17 ? 167 MET A CG 1 ATOM 1326 S SD . MET A 1 190 ? -26.228 50.559 19.687 1.00 38.78 ? 167 MET A SD 1 ATOM 1327 C CE . MET A 1 190 ? -25.209 50.223 18.251 1.00 30.97 ? 167 MET A CE 1 ATOM 1328 N N . ALA A 1 191 ? -24.762 54.764 22.501 1.00 34.78 ? 168 ALA A N 1 ATOM 1329 C CA . ALA A 1 191 ? -25.169 55.325 23.787 1.00 39.27 ? 168 ALA A CA 1 ATOM 1330 C C . ALA A 1 191 ? -26.416 56.187 23.622 1.00 41.04 ? 168 ALA A C 1 ATOM 1331 O O . ALA A 1 191 ? -27.351 56.099 24.416 1.00 39.21 ? 168 ALA A O 1 ATOM 1332 C CB . ALA A 1 191 ? -24.036 56.134 24.402 1.00 39.22 ? 168 ALA A CB 1 ATOM 1333 N N . VAL A 1 192 ? -26.426 57.014 22.581 1.00 36.85 ? 169 VAL A N 1 ATOM 1334 C CA . VAL A 1 192 ? -27.587 57.840 22.270 1.00 37.61 ? 169 VAL A CA 1 ATOM 1335 C C . VAL A 1 192 ? -28.835 56.992 22.040 1.00 34.05 ? 169 VAL A C 1 ATOM 1336 O O . VAL A 1 192 ? -29.916 57.325 22.527 1.00 37.93 ? 169 VAL A O 1 ATOM 1337 C CB . VAL A 1 192 ? -27.330 58.735 21.041 1.00 38.58 ? 169 VAL A CB 1 ATOM 1338 C CG1 . VAL A 1 192 ? -28.635 59.301 20.502 1.00 36.18 ? 169 VAL A CG1 1 ATOM 1339 C CG2 . VAL A 1 192 ? -26.365 59.855 21.402 1.00 29.06 ? 169 VAL A CG2 1 ATOM 1340 N N . LEU A 1 193 ? -28.683 55.891 21.311 1.00 29.54 ? 170 LEU A N 1 ATOM 1341 C CA . LEU A 1 193 ? -29.812 55.003 21.043 1.00 34.12 ? 170 LEU A CA 1 ATOM 1342 C C . LEU A 1 193 ? -30.316 54.380 22.339 1.00 42.83 ? 170 LEU A C 1 ATOM 1343 O O . LEU A 1 193 ? -31.523 54.245 22.548 1.00 39.35 ? 170 LEU A O 1 ATOM 1344 C CB . LEU A 1 193 ? -29.419 53.907 20.049 1.00 31.69 ? 170 LEU A CB 1 ATOM 1345 C CG . LEU A 1 193 ? -29.141 54.355 18.613 1.00 39.57 ? 170 LEU A CG 1 ATOM 1346 C CD1 . LEU A 1 193 ? -28.557 53.212 17.805 1.00 41.12 ? 170 LEU A CD1 1 ATOM 1347 C CD2 . LEU A 1 193 ? -30.413 54.875 17.961 1.00 33.83 ? 170 LEU A CD2 1 ATOM 1348 N N . ALA A 1 194 ? -29.379 54.011 23.207 1.00 39.78 ? 171 ALA A N 1 ATOM 1349 C CA . ALA A 1 194 ? -29.713 53.408 24.492 1.00 39.13 ? 171 ALA A CA 1 ATOM 1350 C C . ALA A 1 194 ? -30.386 54.414 25.418 1.00 38.83 ? 171 ALA A C 1 ATOM 1351 O O . ALA A 1 194 ? -31.436 54.132 25.995 1.00 39.72 ? 171 ALA A O 1 ATOM 1352 C CB . ALA A 1 194 ? -28.464 52.834 25.147 1.00 33.18 ? 171 ALA A CB 1 ATOM 1353 N N . LEU A 1 195 ? -29.776 55.588 25.556 1.00 42.70 ? 172 LEU A N 1 ATOM 1354 C CA . LEU A 1 195 ? -30.311 56.636 26.418 1.00 41.18 ? 172 LEU A CA 1 ATOM 1355 C C . LEU A 1 195 ? -31.691 57.089 25.953 1.00 45.43 ? 172 LEU A C 1 ATOM 1356 O O . LEU A 1 195 ? -32.554 57.423 26.766 1.00 40.09 ? 172 LEU A O 1 ATOM 1357 C CB . LEU A 1 195 ? -29.351 57.829 26.475 1.00 35.70 ? 172 LEU A CB 1 ATOM 1358 C CG . LEU A 1 195 ? -27.989 57.578 27.131 1.00 35.22 ? 172 LEU A CG 1 ATOM 1359 C CD1 . LEU A 1 195 ? -27.070 58.784 26.976 1.00 34.39 ? 172 LEU A CD1 1 ATOM 1360 C CD2 . LEU A 1 195 ? -28.155 57.215 28.599 1.00 34.87 ? 172 LEU A CD2 1 ATOM 1361 N N . THR A 1 196 ? -31.894 57.090 24.640 1.00 35.23 ? 173 THR A N 1 ATOM 1362 C CA . THR A 1 196 ? -33.165 57.513 24.066 1.00 37.23 ? 173 THR A CA 1 ATOM 1363 C C . THR A 1 196 ? -34.260 56.505 24.389 1.00 47.41 ? 173 THR A C 1 ATOM 1364 O O . THR A 1 196 ? -35.416 56.873 24.605 1.00 41.00 ? 173 THR A O 1 ATOM 1365 C CB . THR A 1 196 ? -33.054 57.694 22.543 1.00 42.31 ? 173 THR A CB 1 ATOM 1366 O OG1 . THR A 1 196 ? -31.986 58.605 22.249 1.00 38.05 ? 173 THR A OG1 1 ATOM 1367 C CG2 . THR A 1 196 ? -34.349 58.240 21.971 1.00 32.76 ? 173 THR A CG2 1 ATOM 1368 N N . CYS A 1 197 ? -33.890 55.229 24.427 1.00 42.79 ? 174 CYS A N 1 ATOM 1369 C CA . CYS A 1 197 ? -34.838 54.184 24.788 1.00 40.84 ? 174 CYS A CA 1 ATOM 1370 C C . CYS A 1 197 ? -35.300 54.360 26.230 1.00 41.15 ? 174 CYS A C 1 ATOM 1371 O O . CYS A 1 197 ? -36.488 54.242 26.525 1.00 46.68 ? 174 CYS A O 1 ATOM 1372 C CB . CYS A 1 197 ? -34.226 52.795 24.590 1.00 43.40 ? 174 CYS A CB 1 ATOM 1373 S SG . CYS A 1 197 ? -35.335 51.436 25.050 1.00 47.30 ? 174 CYS A SG 1 ATOM 1374 N N . VAL A 1 198 ? -34.355 54.638 27.124 1.00 40.11 ? 175 VAL A N 1 ATOM 1375 C CA . VAL A 1 198 ? -34.673 54.872 28.530 1.00 44.68 ? 175 VAL A CA 1 ATOM 1376 C C . VAL A 1 198 ? -35.588 56.085 28.680 1.00 49.79 ? 175 VAL A C 1 ATOM 1377 O O . VAL A 1 198 ? -36.514 56.078 29.491 1.00 46.94 ? 175 VAL A O 1 ATOM 1378 C CB . VAL A 1 198 ? -33.400 55.079 29.369 1.00 38.52 ? 175 VAL A CB 1 ATOM 1379 C CG1 . VAL A 1 198 ? -33.753 55.277 30.837 1.00 44.51 ? 175 VAL A CG1 1 ATOM 1380 C CG2 . VAL A 1 198 ? -32.461 53.898 29.201 1.00 31.19 ? 175 VAL A CG2 1 ATOM 1381 N N . LYS A 1 199 ? -35.324 57.120 27.886 1.00 51.82 ? 176 LYS A N 1 ATOM 1382 C CA . LYS A 1 199 ? -36.165 58.312 27.867 1.00 49.99 ? 176 LYS A CA 1 ATOM 1383 C C . LYS A 1 199 ? -37.610 57.965 27.513 1.00 44.49 ? 176 LYS A C 1 ATOM 1384 O O . LYS A 1 199 ? -38.538 58.353 28.222 1.00 42.85 ? 176 LYS A O 1 ATOM 1385 C CB . LYS A 1 199 ? -35.607 59.352 26.889 1.00 57.58 ? 176 LYS A CB 1 ATOM 1386 C CG . LYS A 1 199 ? -34.389 60.108 27.412 1.00 63.77 ? 176 LYS A CG 1 ATOM 1387 C CD . LYS A 1 199 ? -33.487 60.599 26.284 1.00 68.70 ? 176 LYS A CD 1 ATOM 1388 C CE . LYS A 1 199 ? -34.222 61.522 25.325 1.00 71.93 ? 176 LYS A CE 1 ATOM 1389 N NZ . LYS A 1 199 ? -33.344 61.983 24.209 1.00 60.01 ? 176 LYS A NZ 1 ATOM 1390 N N . LYS A 1 200 ? -37.796 57.228 26.423 1.00 36.06 ? 177 LYS A N 1 ATOM 1391 C CA . LYS A 1 200 ? -39.133 56.840 25.988 1.00 40.06 ? 177 LYS A CA 1 ATOM 1392 C C . LYS A 1 200 ? -39.789 55.953 27.037 1.00 50.17 ? 177 LYS A C 1 ATOM 1393 O O . LYS A 1 200 ? -40.980 56.083 27.319 1.00 47.41 ? 177 LYS A O 1 ATOM 1394 C CB . LYS A 1 200 ? -39.078 56.114 24.642 1.00 42.93 ? 177 LYS A CB 1 ATOM 1395 C CG . LYS A 1 200 ? -38.405 56.913 23.543 1.00 42.18 ? 177 LYS A CG 1 ATOM 1396 C CD . LYS A 1 200 ? -38.246 56.101 22.272 1.00 51.16 ? 177 LYS A CD 1 ATOM 1397 C CE . LYS A 1 200 ? -39.508 56.129 21.441 1.00 62.12 ? 177 LYS A CE 1 ATOM 1398 N NZ . LYS A 1 200 ? -39.821 57.516 21.001 1.00 62.13 ? 177 LYS A NZ 1 ATOM 1399 N N . SER A 1 201 ? -38.993 55.065 27.623 1.00 47.77 ? 178 SER A N 1 ATOM 1400 C CA . SER A 1 201 ? -39.469 54.160 28.660 1.00 49.70 ? 178 SER A CA 1 ATOM 1401 C C . SER A 1 201 ? -39.922 54.920 29.907 1.00 52.07 ? 178 SER A C 1 ATOM 1402 O O . SER A 1 201 ? -40.888 54.529 30.561 1.00 55.20 ? 178 SER A O 1 ATOM 1403 C CB . SER A 1 201 ? -38.380 53.148 29.020 1.00 50.88 ? 178 SER A CB 1 ATOM 1404 O OG . SER A 1 201 ? -38.818 52.269 30.039 1.00 60.00 ? 178 SER A OG 1 ATOM 1405 N N . LEU A 1 202 ? -39.222 56.005 30.226 1.00 58.07 ? 179 LEU A N 1 ATOM 1406 C CA . LEU A 1 202 ? -39.581 56.858 31.358 1.00 56.40 ? 179 LEU A CA 1 ATOM 1407 C C . LEU A 1 202 ? -40.873 57.632 31.112 1.00 61.42 ? 179 LEU A C 1 ATOM 1408 O O . LEU A 1 202 ? -41.736 57.712 31.987 1.00 64.43 ? 179 LEU A O 1 ATOM 1409 C CB . LEU A 1 202 ? -38.450 57.840 31.669 1.00 52.35 ? 179 LEU A CB 1 ATOM 1410 C CG . LEU A 1 202 ? -37.300 57.304 32.519 1.00 62.39 ? 179 LEU A CG 1 ATOM 1411 C CD1 . LEU A 1 202 ? -36.185 58.332 32.627 1.00 58.60 ? 179 LEU A CD1 1 ATOM 1412 C CD2 . LEU A 1 202 ? -37.811 56.913 33.896 1.00 63.31 ? 179 LEU A CD2 1 ATOM 1413 N N . ILE A 1 203 ? -40.991 58.211 29.921 1.00 59.38 ? 180 ILE A N 1 ATOM 1414 C CA . ILE A 1 203 ? -42.172 58.979 29.545 1.00 55.49 ? 180 ILE A CA 1 ATOM 1415 C C . ILE A 1 203 ? -43.402 58.072 29.467 1.00 55.81 ? 180 ILE A C 1 ATOM 1416 O O . ILE A 1 203 ? -44.514 58.483 29.804 1.00 54.64 ? 180 ILE A O 1 ATOM 1417 C CB . ILE A 1 203 ? -41.945 59.736 28.217 1.00 55.37 ? 180 ILE A CB 1 ATOM 1418 C CG1 . ILE A 1 203 ? -40.768 60.707 28.367 1.00 54.22 ? 180 ILE A CG1 1 ATOM 1419 C CG2 . ILE A 1 203 ? -43.202 60.481 27.788 1.00 53.00 ? 180 ILE A CG2 1 ATOM 1420 C CD1 . ILE A 1 203 ? -40.443 61.492 27.113 1.00 49.61 ? 180 ILE A CD1 1 ATOM 1421 N N . ASN A 1 204 ? -43.194 56.831 29.036 1.00 52.12 ? 181 ASN A N 1 ATOM 1422 C CA . ASN A 1 204 ? -44.243 55.818 29.100 1.00 60.51 ? 181 ASN A CA 1 ATOM 1423 C C . ASN A 1 204 ? -44.387 55.308 30.531 1.00 71.13 ? 181 ASN A C 1 ATOM 1424 O O . ASN A 1 204 ? -43.874 55.917 31.469 1.00 78.90 ? 181 ASN A O 1 ATOM 1425 C CB . ASN A 1 204 ? -43.938 54.653 28.155 1.00 58.60 ? 181 ASN A CB 1 ATOM 1426 C CG . ASN A 1 204 ? -43.832 55.085 26.704 1.00 63.10 ? 181 ASN A CG 1 ATOM 1427 O OD1 . ASN A 1 204 ? -44.380 56.112 26.306 1.00 67.17 ? 181 ASN A OD1 1 ATOM 1428 N ND2 . ASN A 1 204 ? -43.124 54.297 25.904 1.00 66.40 ? 181 ASN A ND2 1 ATOM 1429 N N . GLY A 1 205 ? -45.075 54.187 30.703 1.00 77.78 ? 182 GLY A N 1 ATOM 1430 C CA . GLY A 1 205 ? -45.262 53.627 32.029 1.00 91.71 ? 182 GLY A CA 1 ATOM 1431 C C . GLY A 1 205 ? -44.365 52.436 32.307 1.00 92.46 ? 182 GLY A C 1 ATOM 1432 O O . GLY A 1 205 ? -44.546 51.734 33.301 1.00 104.09 ? 182 GLY A O 1 ATOM 1433 N N . GLN A 1 206 ? -43.389 52.213 31.432 1.00 76.63 ? 183 GLN A N 1 ATOM 1434 C CA . GLN A 1 206 ? -42.536 51.032 31.521 1.00 74.32 ? 183 GLN A CA 1 ATOM 1435 C C . GLN A 1 206 ? -41.599 51.030 32.726 1.00 73.51 ? 183 GLN A C 1 ATOM 1436 O O . GLN A 1 206 ? -41.451 50.012 33.400 1.00 82.72 ? 183 GLN A O 1 ATOM 1437 C CB . GLN A 1 206 ? -41.724 50.851 30.236 1.00 80.31 ? 183 GLN A CB 1 ATOM 1438 C CG . GLN A 1 206 ? -42.383 49.963 29.193 1.00 92.81 ? 183 GLN A CG 1 ATOM 1439 C CD . GLN A 1 206 ? -43.592 50.608 28.549 1.00 101.68 ? 183 GLN A CD 1 ATOM 1440 O OE1 . GLN A 1 206 ? -43.471 51.314 27.547 1.00 103.29 ? 183 GLN A OE1 1 ATOM 1441 N NE2 . GLN A 1 206 ? -44.767 50.365 29.118 1.00 105.74 ? 183 GLN A NE2 1 ATOM 1442 N N . ILE A 1 207 ? -40.965 52.165 32.995 1.00 69.28 ? 184 ILE A N 1 ATOM 1443 C CA . ILE A 1 207 ? -39.926 52.219 34.018 1.00 79.61 ? 184 ILE A CA 1 ATOM 1444 C C . ILE A 1 207 ? -40.046 53.436 34.934 1.00 85.08 ? 184 ILE A C 1 ATOM 1445 O O . ILE A 1 207 ? -40.236 54.559 34.469 1.00 100.34 ? 184 ILE A O 1 ATOM 1446 C CB . ILE A 1 207 ? -38.517 52.177 33.377 1.00 88.06 ? 184 ILE A CB 1 ATOM 1447 C CG1 . ILE A 1 207 ? -38.189 50.757 32.915 1.00 95.03 ? 184 ILE A CG1 1 ATOM 1448 C CG2 . ILE A 1 207 ? -37.456 52.656 34.352 1.00 93.77 ? 184 ILE A CG2 1 ATOM 1449 C CD1 . ILE A 1 207 ? -38.207 49.737 34.034 1.00 101.09 ? 184 ILE A CD1 1 ATOM 1450 N N . LYS A 1 208 ? -39.941 53.199 36.238 1.00 74.60 ? 185 LYS A N 1 ATOM 1451 C CA . LYS A 1 208 ? -39.925 54.277 37.218 1.00 81.98 ? 185 LYS A CA 1 ATOM 1452 C C . LYS A 1 208 ? -38.488 54.647 37.578 1.00 78.62 ? 185 LYS A C 1 ATOM 1453 O O . LYS A 1 208 ? -37.585 53.814 37.495 1.00 80.91 ? 185 LYS A O 1 ATOM 1454 C CB . LYS A 1 208 ? -40.689 53.865 38.478 1.00 90.94 ? 185 LYS A CB 1 ATOM 1455 C CG . LYS A 1 208 ? -42.141 53.492 38.232 1.00 102.31 ? 185 LYS A CG 1 ATOM 1456 C CD . LYS A 1 208 ? -42.813 53.031 39.516 1.00 111.58 ? 185 LYS A CD 1 ATOM 1457 C CE . LYS A 1 208 ? -44.259 52.630 39.273 1.00 115.54 ? 185 LYS A CE 1 ATOM 1458 N NZ . LYS A 1 208 ? -44.915 52.137 40.515 1.00 118.41 ? 185 LYS A NZ 1 ATOM 1459 N N . ALA A 1 209 ? -38.282 55.898 37.979 1.00 74.09 ? 186 ALA A N 1 ATOM 1460 C CA . ALA A 1 209 ? -36.954 56.372 38.358 1.00 62.65 ? 186 ALA A CA 1 ATOM 1461 C C . ALA A 1 209 ? -37.040 57.576 39.285 1.00 63.75 ? 186 ALA A C 1 ATOM 1462 O O . ALA A 1 209 ? -38.106 58.172 39.444 1.00 69.53 ? 186 ALA A O 1 ATOM 1463 C CB . ALA A 1 209 ? -36.146 56.723 37.122 1.00 52.58 ? 186 ALA A CB 1 ATOM 1464 N N . ASP A 1 210 ? -35.914 57.929 39.897 1.00 65.98 ? 187 ASP A N 1 ATOM 1465 C CA . ASP A 1 210 ? -35.839 59.141 40.700 1.00 74.27 ? 187 ASP A CA 1 ATOM 1466 C C . ASP A 1 210 ? -36.125 60.337 39.805 1.00 72.51 ? 187 ASP A C 1 ATOM 1467 O O . ASP A 1 210 ? -35.516 60.482 38.746 1.00 75.72 ? 187 ASP A O 1 ATOM 1468 C CB . ASP A 1 210 ? -34.458 59.286 41.343 1.00 85.62 ? 187 ASP A CB 1 ATOM 1469 C CG . ASP A 1 210 ? -34.195 58.236 42.404 1.00 99.24 ? 187 ASP A CG 1 ATOM 1470 O OD1 . ASP A 1 210 ? -35.167 57.765 43.031 1.00 100.26 ? 187 ASP A OD1 1 ATOM 1471 O OD2 . ASP A 1 210 ? -33.014 57.885 42.613 1.00 107.29 ? 187 ASP A OD2 1 ATOM 1472 N N . GLU A 1 211 ? -37.063 61.178 40.228 1.00 67.79 ? 188 GLU A N 1 ATOM 1473 C CA . GLU A 1 211 ? -37.446 62.353 39.454 1.00 72.79 ? 188 GLU A CA 1 ATOM 1474 C C . GLU A 1 211 ? -36.235 63.231 39.149 1.00 77.17 ? 188 GLU A C 1 ATOM 1475 O O . GLU A 1 211 ? -35.415 63.507 40.026 1.00 71.43 ? 188 GLU A O 1 ATOM 1476 C CB . GLU A 1 211 ? -38.528 63.153 40.185 1.00 74.77 ? 188 GLU A CB 1 ATOM 1477 C CG . GLU A 1 211 ? -39.803 62.365 40.451 1.00 78.85 ? 188 GLU A CG 1 ATOM 1478 C CD . GLU A 1 211 ? -40.860 63.184 41.167 1.00 94.80 ? 188 GLU A CD 1 ATOM 1479 O OE1 . GLU A 1 211 ? -41.148 62.886 42.345 1.00 105.67 ? 188 GLU A OE1 1 ATOM 1480 O OE2 . GLU A 1 211 ? -41.407 64.123 40.549 1.00 97.95 ? 188 GLU A OE2 1 ATOM 1481 N N . GLY A 1 212 ? -36.124 63.648 37.892 1.00 78.69 ? 189 GLY A N 1 ATOM 1482 C CA . GLY A 1 212 ? -34.982 64.417 37.436 1.00 74.55 ? 189 GLY A CA 1 ATOM 1483 C C . GLY A 1 212 ? -34.042 63.577 36.594 1.00 69.63 ? 189 GLY A C 1 ATOM 1484 O O . GLY A 1 212 ? -33.093 64.095 36.003 1.00 67.07 ? 189 GLY A O 1 ATOM 1485 N N . SER A 1 213 ? -34.305 62.274 36.541 1.00 62.81 ? 190 SER A N 1 ATOM 1486 C CA . SER A 1 213 ? -33.481 61.361 35.757 1.00 60.01 ? 190 SER A CA 1 ATOM 1487 C C . SER A 1 213 ? -33.625 61.654 34.271 1.00 59.35 ? 190 SER A C 1 ATOM 1488 O O . SER A 1 213 ? -32.644 61.633 33.527 1.00 55.87 ? 190 SER A O 1 ATOM 1489 C CB . SER A 1 213 ? -33.860 59.905 36.040 1.00 58.83 ? 190 SER A CB 1 ATOM 1490 O OG . SER A 1 213 ? -33.647 59.574 37.400 1.00 68.19 ? 190 SER A OG 1 ATOM 1491 N N . LEU A 1 214 ? -34.856 61.929 33.847 1.00 54.44 ? 191 LEU A N 1 ATOM 1492 C CA . LEU A 1 214 ? -35.137 62.239 32.451 1.00 55.30 ? 191 LEU A CA 1 ATOM 1493 C C . LEU A 1 214 ? -34.352 63.468 32.014 1.00 56.78 ? 191 LEU A C 1 ATOM 1494 O O . LEU A 1 214 ? -33.857 63.535 30.889 1.00 48.27 ? 191 LEU A O 1 ATOM 1495 C CB . LEU A 1 214 ? -36.635 62.467 32.239 1.00 53.15 ? 191 LEU A CB 1 ATOM 1496 C CG . LEU A 1 214 ? -37.061 62.775 30.800 1.00 54.51 ? 191 LEU A CG 1 ATOM 1497 C CD1 . LEU A 1 214 ? -36.753 61.600 29.881 1.00 49.01 ? 191 LEU A CD1 1 ATOM 1498 C CD2 . LEU A 1 214 ? -38.534 63.135 30.733 1.00 57.28 ? 191 LEU A CD2 1 ATOM 1499 N N . LYS A 1 215 ? -34.238 64.433 32.921 1.00 54.56 ? 192 LYS A N 1 ATOM 1500 C CA . LYS A 1 215 ? -33.500 65.662 32.662 1.00 55.30 ? 192 LYS A CA 1 ATOM 1501 C C . LYS A 1 215 ? -32.023 65.374 32.404 1.00 55.20 ? 192 LYS A C 1 ATOM 1502 O O . LYS A 1 215 ? -31.469 65.797 31.391 1.00 46.37 ? 192 LYS A O 1 ATOM 1503 C CB . LYS A 1 215 ? -33.660 66.627 33.839 1.00 54.16 ? 192 LYS A CB 1 ATOM 1504 C CG . LYS A 1 215 ? -33.018 67.992 33.648 1.00 53.38 ? 192 LYS A CG 1 ATOM 1505 C CD . LYS A 1 215 ? -33.385 68.916 34.804 1.00 66.21 ? 192 LYS A CD 1 ATOM 1506 C CE . LYS A 1 215 ? -32.678 70.255 34.708 1.00 79.86 ? 192 LYS A CE 1 ATOM 1507 N NZ . LYS A 1 215 ? -31.203 70.122 34.857 1.00 89.27 ? 192 LYS A NZ 1 ATOM 1508 N N . ASN A 1 216 ? -31.393 64.644 33.319 1.00 53.07 ? 193 ASN A N 1 ATOM 1509 C CA . ASN A 1 216 ? -29.973 64.331 33.199 1.00 52.41 ? 193 ASN A CA 1 ATOM 1510 C C . ASN A 1 216 ? -29.647 63.480 31.975 1.00 47.72 ? 193 ASN A C 1 ATOM 1511 O O . ASN A 1 216 ? -28.643 63.711 31.302 1.00 51.15 ? 193 ASN A O 1 ATOM 1512 C CB . ASN A 1 216 ? -29.457 63.661 34.474 1.00 57.58 ? 193 ASN A CB 1 ATOM 1513 C CG . ASN A 1 216 ? -29.563 64.565 35.686 1.00 71.50 ? 193 ASN A CG 1 ATOM 1514 O OD1 . ASN A 1 216 ? -29.752 65.775 35.553 1.00 69.63 ? 193 ASN A OD1 1 ATOM 1515 N ND2 . ASN A 1 216 ? -29.438 63.984 36.876 1.00 83.88 ? 193 ASN A ND2 1 ATOM 1516 N N . ILE A 1 217 ? -30.500 62.503 31.688 1.00 43.56 ? 194 ILE A N 1 ATOM 1517 C CA . ILE A 1 217 ? -30.315 61.651 30.518 1.00 44.52 ? 194 ILE A CA 1 ATOM 1518 C C . ILE A 1 217 ? -30.428 62.473 29.235 1.00 44.49 ? 194 ILE A C 1 ATOM 1519 O O . ILE A 1 217 ? -29.647 62.290 28.300 1.00 42.72 ? 194 ILE A O 1 ATOM 1520 C CB . ILE A 1 217 ? -31.325 60.485 30.506 1.00 49.93 ? 194 ILE A CB 1 ATOM 1521 C CG1 . ILE A 1 217 ? -31.074 59.559 31.697 1.00 52.45 ? 194 ILE A CG1 1 ATOM 1522 C CG2 . ILE A 1 217 ? -31.224 59.695 29.214 1.00 49.35 ? 194 ILE A CG2 1 ATOM 1523 C CD1 . ILE A 1 217 ? -32.056 58.418 31.796 1.00 52.12 ? 194 ILE A CD1 1 ATOM 1524 N N . SER A 1 218 ? -31.392 63.391 29.210 1.00 43.20 ? 195 SER A N 1 ATOM 1525 C CA . SER A 1 218 ? -31.586 64.284 28.071 1.00 47.11 ? 195 SER A CA 1 ATOM 1526 C C . SER A 1 218 ? -30.361 65.161 27.842 1.00 45.48 ? 195 SER A C 1 ATOM 1527 O O . SER A 1 218 ? -29.963 65.403 26.702 1.00 42.43 ? 195 SER A O 1 ATOM 1528 C CB . SER A 1 218 ? -32.823 65.165 28.280 1.00 39.69 ? 195 SER A CB 1 ATOM 1529 O OG . SER A 1 218 ? -34.002 64.382 28.340 1.00 55.99 ? 195 SER A OG 1 ATOM 1530 N N . ILE A 1 219 ? -29.773 65.639 28.935 1.00 40.87 ? 196 ILE A N 1 ATOM 1531 C CA . ILE A 1 219 ? -28.562 66.449 28.866 1.00 43.86 ? 196 ILE A CA 1 ATOM 1532 C C . ILE A 1 219 ? -27.391 65.620 28.339 1.00 49.20 ? 196 ILE A C 1 ATOM 1533 O O . ILE A 1 219 ? -26.611 66.095 27.510 1.00 43.47 ? 196 ILE A O 1 ATOM 1534 C CB . ILE A 1 219 ? -28.219 67.071 30.239 1.00 46.69 ? 196 ILE A CB 1 ATOM 1535 C CG1 . ILE A 1 219 ? -29.303 68.074 30.647 1.00 50.17 ? 196 ILE A CG1 1 ATOM 1536 C CG2 . ILE A 1 219 ? -26.858 67.751 30.201 1.00 38.66 ? 196 ILE A CG2 1 ATOM 1537 C CD1 . ILE A 1 219 ? -29.101 68.685 32.018 1.00 44.93 ? 196 ILE A CD1 1 ATOM 1538 N N . TYR A 1 220 ? -27.282 64.380 28.815 1.00 39.18 ? 197 TYR A N 1 ATOM 1539 C CA . TYR A 1 220 ? -26.277 63.447 28.312 1.00 41.34 ? 197 TYR A CA 1 ATOM 1540 C C . TYR A 1 220 ? -26.425 63.276 26.804 1.00 42.94 ? 197 TYR A C 1 ATOM 1541 O O . TYR A 1 220 ? -25.444 63.332 26.064 1.00 41.23 ? 197 TYR A O 1 ATOM 1542 C CB . TYR A 1 220 ? -26.408 62.072 28.978 1.00 37.63 ? 197 TYR A CB 1 ATOM 1543 C CG . TYR A 1 220 ? -25.999 62.012 30.431 1.00 44.48 ? 197 TYR A CG 1 ATOM 1544 C CD1 . TYR A 1 220 ? -25.565 63.146 31.106 1.00 45.42 ? 197 TYR A CD1 1 ATOM 1545 C CD2 . TYR A 1 220 ? -26.038 60.810 31.127 1.00 46.92 ? 197 TYR A CD2 1 ATOM 1546 C CE1 . TYR A 1 220 ? -25.191 63.086 32.434 1.00 42.15 ? 197 TYR A CE1 1 ATOM 1547 C CE2 . TYR A 1 220 ? -25.666 60.739 32.453 1.00 48.24 ? 197 TYR A CE2 1 ATOM 1548 C CZ . TYR A 1 220 ? -25.243 61.879 33.102 1.00 49.56 ? 197 TYR A CZ 1 ATOM 1549 O OH . TYR A 1 220 ? -24.871 61.809 34.425 1.00 48.63 ? 197 TYR A OH 1 ATOM 1550 N N . THR A 1 221 ? -27.662 63.062 26.363 1.00 43.42 ? 198 THR A N 1 ATOM 1551 C CA . THR A 1 221 ? -27.958 62.876 24.948 1.00 49.22 ? 198 THR A CA 1 ATOM 1552 C C . THR A 1 221 ? -27.600 64.120 24.143 1.00 44.85 ? 198 THR A C 1 ATOM 1553 O O . THR A 1 221 ? -27.008 64.024 23.069 1.00 41.04 ? 198 THR A O 1 ATOM 1554 C CB . THR A 1 221 ? -29.445 62.535 24.714 1.00 47.45 ? 198 THR A CB 1 ATOM 1555 O OG1 . THR A 1 221 ? -29.800 61.378 25.478 1.00 55.38 ? 198 THR A OG1 1 ATOM 1556 C CG2 . THR A 1 221 ? -29.698 62.260 23.243 1.00 57.90 ? 198 THR A CG2 1 ATOM 1557 N N . LYS A 1 222 ? -27.964 65.284 24.673 1.00 44.05 ? 199 LYS A N 1 ATOM 1558 C CA . LYS A 1 222 ? -27.640 66.560 24.042 1.00 52.44 ? 199 LYS A CA 1 ATOM 1559 C C . LYS A 1 222 ? -26.138 66.711 23.806 1.00 49.87 ? 199 LYS A C 1 ATOM 1560 O O . LYS A 1 222 ? -25.707 67.086 22.716 1.00 45.15 ? 199 LYS A O 1 ATOM 1561 C CB . LYS A 1 222 ? -28.154 67.719 24.899 1.00 51.68 ? 199 LYS A CB 1 ATOM 1562 C CG . LYS A 1 222 ? -27.871 69.095 24.320 1.00 48.87 ? 199 LYS A CG 1 ATOM 1563 C CD . LYS A 1 222 ? -28.525 70.185 25.153 1.00 51.10 ? 199 LYS A CD 1 ATOM 1564 C CE . LYS A 1 222 ? -28.195 71.571 24.617 1.00 55.47 ? 199 LYS A CE 1 ATOM 1565 N NZ . LYS A 1 222 ? -26.739 71.874 24.691 1.00 60.35 ? 199 LYS A NZ 1 ATOM 1566 N N . SER A 1 223 ? -25.349 66.410 24.833 1.00 41.70 ? 200 SER A N 1 ATOM 1567 C CA . SER A 1 223 ? -23.895 66.498 24.746 1.00 46.43 ? 200 SER A CA 1 ATOM 1568 C C . SER A 1 223 ? -23.320 65.492 23.746 1.00 49.18 ? 200 SER A C 1 ATOM 1569 O O . SER A 1 223 ? -22.427 65.823 22.964 1.00 42.58 ? 200 SER A O 1 ATOM 1570 C CB . SER A 1 223 ? -23.267 66.292 26.128 1.00 36.54 ? 200 SER A CB 1 ATOM 1571 O OG . SER A 1 223 ? -21.851 66.275 26.054 1.00 56.94 ? 200 SER A OG 1 ATOM 1572 N N . LEU A 1 224 ? -23.837 64.268 23.775 1.00 44.10 ? 201 LEU A N 1 ATOM 1573 C CA . LEU A 1 224 ? -23.380 63.220 22.865 1.00 44.16 ? 201 LEU A CA 1 ATOM 1574 C C . LEU A 1 224 ? -23.678 63.541 21.400 1.00 40.70 ? 201 LEU A C 1 ATOM 1575 O O . LEU A 1 224 ? -22.866 63.254 20.522 1.00 41.76 ? 201 LEU A O 1 ATOM 1576 C CB . LEU A 1 224 ? -23.982 61.867 23.250 1.00 41.65 ? 201 LEU A CB 1 ATOM 1577 C CG . LEU A 1 224 ? -23.439 61.251 24.540 1.00 45.08 ? 201 LEU A CG 1 ATOM 1578 C CD1 . LEU A 1 224 ? -24.167 59.958 24.880 1.00 36.34 ? 201 LEU A CD1 1 ATOM 1579 C CD2 . LEU A 1 224 ? -21.940 61.015 24.423 1.00 40.08 ? 201 LEU A CD2 1 ATOM 1580 N N . VAL A 1 225 ? -24.839 64.139 21.143 1.00 37.66 ? 202 VAL A N 1 ATOM 1581 C CA . VAL A 1 225 ? -25.213 64.544 19.790 1.00 38.73 ? 202 VAL A CA 1 ATOM 1582 C C . VAL A 1 225 ? -24.254 65.604 19.253 1.00 45.47 ? 202 VAL A C 1 ATOM 1583 O O . VAL A 1 225 ? -23.810 65.535 18.106 1.00 47.03 ? 202 VAL A O 1 ATOM 1584 C CB . VAL A 1 225 ? -26.662 65.076 19.739 1.00 40.76 ? 202 VAL A CB 1 ATOM 1585 C CG1 . VAL A 1 225 ? -26.936 65.787 18.416 1.00 26.91 ? 202 VAL A CG1 1 ATOM 1586 C CG2 . VAL A 1 225 ? -27.646 63.939 19.952 1.00 38.81 ? 202 VAL A CG2 1 ATOM 1587 N N . GLU A 1 226 ? -23.927 66.577 20.096 1.00 43.91 ? 203 GLU A N 1 ATOM 1588 C CA . GLU A 1 226 ? -22.967 67.610 19.734 1.00 38.14 ? 203 GLU A CA 1 ATOM 1589 C C . GLU A 1 226 ? -21.596 67.019 19.406 1.00 47.30 ? 203 GLU A C 1 ATOM 1590 O O . GLU A 1 226 ? -20.972 67.403 18.417 1.00 40.59 ? 203 GLU A O 1 ATOM 1591 C CB . GLU A 1 226 ? -22.857 68.642 20.856 1.00 45.18 ? 203 GLU A CB 1 ATOM 1592 C CG . GLU A 1 226 ? -24.149 69.403 21.097 1.00 55.38 ? 203 GLU A CG 1 ATOM 1593 C CD . GLU A 1 226 ? -24.153 70.146 22.415 1.00 57.63 ? 203 GLU A CD 1 ATOM 1594 O OE1 . GLU A 1 226 ? -23.229 69.927 23.225 1.00 67.60 ? 203 GLU A OE1 1 ATOM 1595 O OE2 . GLU A 1 226 ? -25.084 70.947 22.641 1.00 57.50 ? 203 GLU A OE2 1 ATOM 1596 N N . LYS A 1 227 ? -21.138 66.081 20.232 1.00 40.58 ? 204 LYS A N 1 ATOM 1597 C CA . LYS A 1 227 ? -19.858 65.412 20.005 1.00 47.54 ? 204 LYS A CA 1 ATOM 1598 C C . LYS A 1 227 ? -19.885 64.552 18.744 1.00 49.95 ? 204 LYS A C 1 ATOM 1599 O O . LYS A 1 227 ? -18.882 64.439 18.039 1.00 46.14 ? 204 LYS A O 1 ATOM 1600 C CB . LYS A 1 227 ? -19.469 64.549 21.208 1.00 43.02 ? 204 LYS A CB 1 ATOM 1601 C CG . LYS A 1 227 ? -19.199 65.326 22.482 1.00 43.00 ? 204 LYS A CG 1 ATOM 1602 C CD . LYS A 1 227 ? -18.988 64.385 23.660 1.00 53.17 ? 204 LYS A CD 1 ATOM 1603 C CE . LYS A 1 227 ? -18.700 65.153 24.938 1.00 51.77 ? 204 LYS A CE 1 ATOM 1604 N NZ . LYS A 1 227 ? -17.402 65.875 24.857 1.00 58.04 ? 204 LYS A NZ 1 ATOM 1605 N N . ILE A 1 228 ? -21.032 63.939 18.468 1.00 44.44 ? 205 ILE A N 1 ATOM 1606 C CA . ILE A 1 228 ? -21.193 63.155 17.250 1.00 40.95 ? 205 ILE A CA 1 ATOM 1607 C C . ILE A 1 228 ? -21.097 64.056 16.019 1.00 44.17 ? 205 ILE A C 1 ATOM 1608 O O . ILE A 1 228 ? -20.337 63.776 15.093 1.00 40.69 ? 205 ILE A O 1 ATOM 1609 C CB . ILE A 1 228 ? -22.525 62.375 17.241 1.00 36.99 ? 205 ILE A CB 1 ATOM 1610 C CG1 . ILE A 1 228 ? -22.452 61.190 18.203 1.00 36.41 ? 205 ILE A CG1 1 ATOM 1611 C CG2 . ILE A 1 228 ? -22.845 61.870 15.842 1.00 28.77 ? 205 ILE A CG2 1 ATOM 1612 C CD1 . ILE A 1 228 ? -23.761 60.443 18.348 1.00 33.30 ? 205 ILE A CD1 1 ATOM 1613 N N . LEU A 1 229 ? -21.855 65.149 16.025 1.00 41.38 ? 206 LEU A N 1 ATOM 1614 C CA . LEU A 1 229 ? -21.858 66.093 14.911 1.00 44.86 ? 206 LEU A CA 1 ATOM 1615 C C . LEU A 1 229 ? -20.513 66.796 14.730 1.00 49.12 ? 206 LEU A C 1 ATOM 1616 O O . LEU A 1 229 ? -20.172 67.220 13.627 1.00 54.49 ? 206 LEU A O 1 ATOM 1617 C CB . LEU A 1 229 ? -22.975 67.125 15.083 1.00 34.53 ? 206 LEU A CB 1 ATOM 1618 C CG . LEU A 1 229 ? -24.387 66.625 14.778 1.00 37.89 ? 206 LEU A CG 1 ATOM 1619 C CD1 . LEU A 1 229 ? -25.425 67.649 15.195 1.00 47.26 ? 206 LEU A CD1 1 ATOM 1620 C CD2 . LEU A 1 229 ? -24.515 66.304 13.299 1.00 42.62 ? 206 LEU A CD2 1 ATOM 1621 N N . SER A 1 230 ? -19.752 66.914 15.814 1.00 52.07 ? 207 SER A N 1 ATOM 1622 C CA . SER A 1 230 ? -18.429 67.530 15.756 1.00 53.04 ? 207 SER A CA 1 ATOM 1623 C C . SER A 1 230 ? -17.450 66.673 14.965 1.00 54.15 ? 207 SER A C 1 ATOM 1624 O O . SER A 1 230 ? -16.381 67.140 14.576 1.00 57.89 ? 207 SER A O 1 ATOM 1625 C CB . SER A 1 230 ? -17.878 67.766 17.164 1.00 47.45 ? 207 SER A CB 1 ATOM 1626 O OG . SER A 1 230 ? -18.653 68.724 17.862 1.00 58.93 ? 207 SER A OG 1 ATOM 1627 N N . GLU A 1 231 ? -17.815 65.415 14.739 1.00 38.42 ? 208 GLU A N 1 ATOM 1628 C CA . GLU A 1 231 ? -16.959 64.499 13.998 1.00 37.27 ? 208 GLU A CA 1 ATOM 1629 C C . GLU A 1 231 ? -17.441 64.339 12.562 1.00 37.85 ? 208 GLU A C 1 ATOM 1630 O O . GLU A 1 231 ? -16.973 63.461 11.838 1.00 46.75 ? 208 GLU A O 1 ATOM 1631 C CB . GLU A 1 231 ? -16.903 63.132 14.686 1.00 35.63 ? 208 GLU A CB 1 ATOM 1632 C CG . GLU A 1 231 ? -16.430 63.166 16.134 1.00 41.34 ? 208 GLU A CG 1 ATOM 1633 C CD . GLU A 1 231 ? -14.958 63.519 16.277 1.00 54.06 ? 208 GLU A CD 1 ATOM 1634 O OE1 . GLU A 1 231 ? -14.204 63.392 15.288 1.00 55.19 ? 208 GLU A OE1 1 ATOM 1635 O OE2 . GLU A 1 231 ? -14.555 63.923 17.387 1.00 55.64 ? 208 GLU A OE2 1 ATOM 1636 N N . LYS A 1 232 ? -18.381 65.186 12.154 1.00 42.71 ? 209 LYS A N 1 ATOM 1637 C CA . LYS A 1 232 ? -18.887 65.153 10.786 1.00 45.92 ? 209 LYS A CA 1 ATOM 1638 C C . LYS A 1 232 ? -17.840 65.695 9.821 1.00 48.38 ? 209 LYS A C 1 ATOM 1639 O O . LYS A 1 232 ? -17.345 66.809 9.986 1.00 47.24 ? 209 LYS A O 1 ATOM 1640 C CB . LYS A 1 232 ? -20.187 65.951 10.665 1.00 43.78 ? 209 LYS A CB 1 ATOM 1641 C CG . LYS A 1 232 ? -20.819 65.917 9.278 1.00 46.80 ? 209 LYS A CG 1 ATOM 1642 C CD . LYS A 1 232 ? -22.214 66.540 9.282 1.00 45.32 ? 209 LYS A CD 1 ATOM 1643 C CE . LYS A 1 232 ? -22.163 68.050 9.463 1.00 50.65 ? 209 LYS A CE 1 ATOM 1644 N NZ . LYS A 1 232 ? -21.566 68.733 8.279 1.00 56.35 ? 209 LYS A NZ 1 ATOM 1645 N N . LYS A 1 233 ? -17.498 64.894 8.820 1.00 50.01 ? 210 LYS A N 1 ATOM 1646 C CA . LYS A 1 233 ? -16.523 65.307 7.823 1.00 53.07 ? 210 LYS A CA 1 ATOM 1647 C C . LYS A 1 233 ? -17.179 66.195 6.774 1.00 56.42 ? 210 LYS A C 1 ATOM 1648 O O . LYS A 1 233 ? -18.399 66.371 6.772 1.00 51.61 ? 210 LYS A O 1 ATOM 1649 C CB . LYS A 1 233 ? -15.863 64.091 7.167 1.00 54.85 ? 210 LYS A CB 1 ATOM 1650 C CG . LYS A 1 233 ? -14.573 63.640 7.845 1.00 66.63 ? 210 LYS A CG 1 ATOM 1651 C CD . LYS A 1 233 ? -14.788 63.297 9.310 1.00 68.65 ? 210 LYS A CD 1 ATOM 1652 C CE . LYS A 1 233 ? -13.476 62.968 10.001 1.00 72.95 ? 210 LYS A CE 1 ATOM 1653 N NZ . LYS A 1 233 ? -13.673 62.659 11.445 1.00 72.32 ? 210 LYS A NZ 1 ATOM 1654 N N . GLU A 1 234 ? -16.361 66.752 5.888 1.00 57.07 ? 211 GLU A N 1 ATOM 1655 C CA . GLU A 1 234 ? -16.835 67.673 4.863 1.00 57.33 ? 211 GLU A CA 1 ATOM 1656 C C . GLU A 1 234 ? -17.754 66.980 3.861 1.00 55.46 ? 211 GLU A C 1 ATOM 1657 O O . GLU A 1 234 ? -18.676 67.594 3.320 1.00 54.89 ? 211 GLU A O 1 ATOM 1658 C CB . GLU A 1 234 ? -15.644 68.307 4.139 1.00 66.35 ? 211 GLU A CB 1 ATOM 1659 C CG . GLU A 1 234 ? -15.999 69.504 3.274 1.00 85.76 ? 211 GLU A CG 1 ATOM 1660 C CD . GLU A 1 234 ? -14.781 70.147 2.637 1.00 103.71 ? 211 GLU A CD 1 ATOM 1661 O OE1 . GLU A 1 234 ? -13.755 69.453 2.473 1.00 109.84 ? 211 GLU A OE1 1 ATOM 1662 O OE2 . GLU A 1 234 ? -14.849 71.349 2.305 1.00 110.93 ? 211 GLU A OE2 1 ATOM 1663 N N . ASN A 1 235 ? -17.502 65.696 3.624 1.00 54.35 ? 212 ASN A N 1 ATOM 1664 C CA . ASN A 1 235 ? -18.279 64.921 2.659 1.00 54.52 ? 212 ASN A CA 1 ATOM 1665 C C . ASN A 1 235 ? -19.574 64.334 3.229 1.00 54.81 ? 212 ASN A C 1 ATOM 1666 O O . ASN A 1 235 ? -20.300 63.627 2.531 1.00 56.11 ? 212 ASN A O 1 ATOM 1667 C CB . ASN A 1 235 ? -17.421 63.810 2.045 1.00 49.57 ? 212 ASN A CB 1 ATOM 1668 C CG . ASN A 1 235 ? -16.839 62.872 3.089 1.00 54.00 ? 212 ASN A CG 1 ATOM 1669 O OD1 . ASN A 1 235 ? -17.180 62.946 4.271 1.00 57.15 ? 212 ASN A OD1 1 ATOM 1670 N ND2 . ASN A 1 235 ? -15.958 61.979 2.654 1.00 50.98 ? 212 ASN A ND2 1 ATOM 1671 N N . GLY A 1 236 ? -19.855 64.620 4.496 1.00 46.51 ? 213 GLY A N 1 ATOM 1672 C CA . GLY A 1 236 ? -21.097 64.183 5.107 1.00 48.48 ? 213 GLY A CA 1 ATOM 1673 C C . GLY A 1 236 ? -20.940 62.982 6.021 1.00 48.50 ? 213 GLY A C 1 ATOM 1674 O O . GLY A 1 236 ? -21.839 62.665 6.801 1.00 51.50 ? 213 GLY A O 1 ATOM 1675 N N . LEU A 1 237 ? -19.801 62.306 5.916 1.00 40.76 ? 214 LEU A N 1 ATOM 1676 C CA . LEU A 1 237 ? -19.498 61.188 6.799 1.00 40.47 ? 214 LEU A CA 1 ATOM 1677 C C . LEU A 1 237 ? -19.385 61.679 8.235 1.00 46.54 ? 214 LEU A C 1 ATOM 1678 O O . LEU A 1 237 ? -18.920 62.792 8.489 1.00 40.73 ? 214 LEU A O 1 ATOM 1679 C CB . LEU A 1 237 ? -18.205 60.488 6.373 1.00 42.85 ? 214 LEU A CB 1 ATOM 1680 C CG . LEU A 1 237 ? -18.243 59.730 5.044 1.00 49.17 ? 214 LEU A CG 1 ATOM 1681 C CD1 . LEU A 1 237 ? -16.941 58.971 4.818 1.00 38.07 ? 214 LEU A CD1 1 ATOM 1682 C CD2 . LEU A 1 237 ? -19.434 58.782 5.000 1.00 52.81 ? 214 LEU A CD2 1 ATOM 1683 N N . ILE A 1 238 ? -19.828 60.849 9.172 1.00 41.71 ? 215 ILE A N 1 ATOM 1684 C CA . ILE A 1 238 ? -19.798 61.205 10.583 1.00 42.76 ? 215 ILE A CA 1 ATOM 1685 C C . ILE A 1 238 ? -18.889 60.236 11.324 1.00 44.71 ? 215 ILE A C 1 ATOM 1686 O O . ILE A 1 238 ? -19.253 59.082 11.564 1.00 40.00 ? 215 ILE A O 1 ATOM 1687 C CB . ILE A 1 238 ? -21.207 61.182 11.192 1.00 36.27 ? 215 ILE A CB 1 ATOM 1688 C CG1 . ILE A 1 238 ? -22.178 61.966 10.306 1.00 37.66 ? 215 ILE A CG1 1 ATOM 1689 C CG2 . ILE A 1 238 ? -21.183 61.751 12.597 1.00 37.56 ? 215 ILE A CG2 1 ATOM 1690 C CD1 . ILE A 1 238 ? -23.629 61.796 10.693 1.00 47.14 ? 215 ILE A CD1 1 ATOM 1691 N N . GLY A 1 239 ? -17.704 60.715 11.685 1.00 41.23 ? 216 GLY A N 1 ATOM 1692 C CA . GLY A 1 239 ? -16.635 59.847 12.144 1.00 36.21 ? 216 GLY A CA 1 ATOM 1693 C C . GLY A 1 239 ? -15.894 59.348 10.919 1.00 38.67 ? 216 GLY A C 1 ATOM 1694 O O . GLY A 1 239 ? -15.266 60.129 10.207 1.00 48.73 ? 216 GLY A O 1 ATOM 1695 N N . ASN A 1 240 ? -15.970 58.047 10.668 1.00 39.78 ? 217 ASN A N 1 ATOM 1696 C CA . ASN A 1 240 ? -15.480 57.496 9.411 1.00 34.70 ? 217 ASN A CA 1 ATOM 1697 C C . ASN A 1 240 ? -16.603 56.788 8.661 1.00 38.35 ? 217 ASN A C 1 ATOM 1698 O O . ASN A 1 240 ? -17.771 56.899 9.033 1.00 36.96 ? 217 ASN A O 1 ATOM 1699 C CB . ASN A 1 240 ? -14.283 56.563 9.629 1.00 36.92 ? 217 ASN A CB 1 ATOM 1700 C CG . ASN A 1 240 ? -14.603 55.390 10.542 1.00 44.34 ? 217 ASN A CG 1 ATOM 1701 O OD1 . ASN A 1 240 ? -15.764 55.028 10.736 1.00 45.36 ? 217 ASN A OD1 1 ATOM 1702 N ND2 . ASN A 1 240 ? -13.563 54.789 11.107 1.00 44.01 ? 217 ASN A ND2 1 ATOM 1703 N N . THR A 1 241 ? -16.239 56.056 7.615 1.00 38.15 ? 218 THR A N 1 ATOM 1704 C CA . THR A 1 241 ? -17.206 55.352 6.783 1.00 34.81 ? 218 THR A CA 1 ATOM 1705 C C . THR A 1 241 ? -18.018 54.337 7.582 1.00 40.51 ? 218 THR A C 1 ATOM 1706 O O . THR A 1 241 ? -19.208 54.140 7.337 1.00 40.26 ? 218 THR A O 1 ATOM 1707 C CB . THR A 1 241 ? -16.495 54.611 5.634 1.00 32.98 ? 218 THR A CB 1 ATOM 1708 O OG1 . THR A 1 241 ? -15.799 55.557 4.816 1.00 40.34 ? 218 THR A OG1 1 ATOM 1709 C CG2 . THR A 1 241 ? -17.493 53.843 4.777 1.00 33.68 ? 218 THR A CG2 1 ATOM 1710 N N . PHE A 1 242 ? -17.368 53.706 8.551 1.00 40.91 ? 219 PHE A N 1 ATOM 1711 C CA . PHE A 1 242 ? -17.963 52.576 9.249 1.00 37.67 ? 219 PHE A CA 1 ATOM 1712 C C . PHE A 1 242 ? -18.635 52.956 10.568 1.00 38.22 ? 219 PHE A C 1 ATOM 1713 O O . PHE A 1 242 ? -19.144 52.092 11.279 1.00 40.21 ? 219 PHE A O 1 ATOM 1714 C CB . PHE A 1 242 ? -16.913 51.485 9.460 1.00 38.81 ? 219 PHE A CB 1 ATOM 1715 C CG . PHE A 1 242 ? -16.204 51.086 8.197 1.00 40.94 ? 219 PHE A CG 1 ATOM 1716 C CD1 . PHE A 1 242 ? -16.858 50.344 7.226 1.00 32.67 ? 219 PHE A CD1 1 ATOM 1717 C CD2 . PHE A 1 242 ? -14.888 51.462 7.975 1.00 36.77 ? 219 PHE A CD2 1 ATOM 1718 C CE1 . PHE A 1 242 ? -16.213 49.978 6.058 1.00 33.54 ? 219 PHE A CE1 1 ATOM 1719 C CE2 . PHE A 1 242 ? -14.235 51.098 6.810 1.00 41.99 ? 219 PHE A CE2 1 ATOM 1720 C CZ . PHE A 1 242 ? -14.898 50.354 5.850 1.00 33.73 ? 219 PHE A CZ 1 ATOM 1721 N N . SER A 1 243 ? -18.643 54.247 10.886 1.00 36.65 ? 220 SER A N 1 ATOM 1722 C CA . SER A 1 243 ? -19.361 54.733 12.061 1.00 37.36 ? 220 SER A CA 1 ATOM 1723 C C . SER A 1 243 ? -20.566 55.569 11.645 1.00 35.20 ? 220 SER A C 1 ATOM 1724 O O . SER A 1 243 ? -21.390 55.943 12.475 1.00 36.78 ? 220 SER A O 1 ATOM 1725 C CB . SER A 1 243 ? -18.441 55.563 12.958 1.00 33.33 ? 220 SER A CB 1 ATOM 1726 O OG . SER A 1 243 ? -18.012 56.745 12.301 1.00 42.05 ? 220 SER A OG 1 ATOM 1727 N N . THR A 1 244 ? -20.664 55.854 10.352 1.00 35.11 ? 221 THR A N 1 ATOM 1728 C CA . THR A 1 244 ? -21.696 56.751 9.843 1.00 33.58 ? 221 THR A CA 1 ATOM 1729 C C . THR A 1 244 ? -23.106 56.173 9.953 1.00 38.14 ? 221 THR A C 1 ATOM 1730 O O . THR A 1 244 ? -24.050 56.881 10.312 1.00 40.94 ? 221 THR A O 1 ATOM 1731 C CB . THR A 1 244 ? -21.415 57.138 8.385 1.00 37.25 ? 221 THR A CB 1 ATOM 1732 O OG1 . THR A 1 244 ? -20.176 57.857 8.315 1.00 39.79 ? 221 THR A OG1 1 ATOM 1733 C CG2 . THR A 1 244 ? -22.525 58.013 7.843 1.00 37.81 ? 221 THR A CG2 1 ATOM 1734 N N . GLY A 1 245 ? -23.241 54.886 9.652 1.00 31.88 ? 222 GLY A N 1 ATOM 1735 C CA . GLY A 1 245 ? -24.536 54.226 9.643 1.00 32.39 ? 222 GLY A CA 1 ATOM 1736 C C . GLY A 1 245 ? -25.262 54.310 10.971 1.00 37.33 ? 222 GLY A C 1 ATOM 1737 O O . GLY A 1 245 ? -26.432 54.686 11.028 1.00 39.88 ? 222 GLY A O 1 ATOM 1738 N N . GLU A 1 246 ? -24.565 53.968 12.047 1.00 31.62 ? 223 GLU A N 1 ATOM 1739 C CA . GLU A 1 246 ? -25.167 54.012 13.370 1.00 39.51 ? 223 GLU A CA 1 ATOM 1740 C C . GLU A 1 246 ? -25.208 55.435 13.922 1.00 40.96 ? 223 GLU A C 1 ATOM 1741 O O . GLU A 1 246 ? -26.035 55.751 14.775 1.00 35.73 ? 223 GLU A O 1 ATOM 1742 C CB . GLU A 1 246 ? -24.464 53.038 14.319 1.00 29.95 ? 223 GLU A CB 1 ATOM 1743 C CG . GLU A 1 246 ? -24.578 51.586 13.854 1.00 31.16 ? 223 GLU A CG 1 ATOM 1744 C CD . GLU A 1 246 ? -24.079 50.578 14.874 1.00 39.98 ? 223 GLU A CD 1 ATOM 1745 O OE1 . GLU A 1 246 ? -23.131 50.893 15.623 1.00 38.90 ? 223 GLU A OE1 1 ATOM 1746 O OE2 . GLU A 1 246 ? -24.644 49.463 14.925 1.00 41.60 ? 223 GLU A OE2 1 ATOM 1747 N N . ALA A 1 247 ? -24.334 56.301 13.416 1.00 38.92 ? 224 ALA A N 1 ATOM 1748 C CA . ALA A 1 247 ? -24.408 57.715 13.766 1.00 43.63 ? 224 ALA A CA 1 ATOM 1749 C C . ALA A 1 247 ? -25.705 58.310 13.222 1.00 40.04 ? 224 ALA A C 1 ATOM 1750 O O . ALA A 1 247 ? -26.364 59.098 13.900 1.00 33.14 ? 224 ALA A O 1 ATOM 1751 C CB . ALA A 1 247 ? -23.199 58.472 13.239 1.00 35.66 ? 224 ALA A CB 1 ATOM 1752 N N . MET A 1 248 ? -26.069 57.918 12.002 1.00 35.37 ? 225 MET A N 1 ATOM 1753 C CA . MET A 1 248 ? -27.331 58.340 11.399 1.00 36.17 ? 225 MET A CA 1 ATOM 1754 C C . MET A 1 248 ? -28.526 57.907 12.250 1.00 38.57 ? 225 MET A C 1 ATOM 1755 O O . MET A 1 248 ? -29.453 58.688 12.462 1.00 40.62 ? 225 MET A O 1 ATOM 1756 C CB . MET A 1 248 ? -27.474 57.796 9.971 1.00 41.23 ? 225 MET A CB 1 ATOM 1757 C CG . MET A 1 248 ? -26.466 58.353 8.967 1.00 29.08 ? 225 MET A CG 1 ATOM 1758 S SD . MET A 1 248 ? -26.584 57.583 7.334 1.00 38.13 ? 225 MET A SD 1 ATOM 1759 C CE . MET A 1 248 ? -28.212 58.120 6.816 1.00 29.63 ? 225 MET A CE 1 ATOM 1760 N N . GLN A 1 249 ? -28.496 56.667 12.738 1.00 35.08 ? 226 GLN A N 1 ATOM 1761 C CA . GLN A 1 249 ? -29.545 56.167 13.625 1.00 37.12 ? 226 GLN A CA 1 ATOM 1762 C C . GLN A 1 249 ? -29.693 57.065 14.844 1.00 37.43 ? 226 GLN A C 1 ATOM 1763 O O . GLN A 1 249 ? -30.802 57.463 15.205 1.00 39.66 ? 226 GLN A O 1 ATOM 1764 C CB . GLN A 1 249 ? -29.242 54.744 14.100 1.00 32.78 ? 226 GLN A CB 1 ATOM 1765 C CG . GLN A 1 249 ? -29.357 53.670 13.040 1.00 38.39 ? 226 GLN A CG 1 ATOM 1766 C CD . GLN A 1 249 ? -29.311 52.277 13.638 1.00 40.99 ? 226 GLN A CD 1 ATOM 1767 O OE1 . GLN A 1 249 ? -29.892 52.026 14.695 1.00 31.73 ? 226 GLN A OE1 1 ATOM 1768 N NE2 . GLN A 1 249 ? -28.609 51.367 12.972 1.00 32.54 ? 226 GLN A NE2 1 ATOM 1769 N N . ALA A 1 250 ? -28.565 57.373 15.476 1.00 34.19 ? 227 ALA A N 1 ATOM 1770 C CA . ALA A 1 250 ? -28.551 58.225 16.660 1.00 38.02 ? 227 ALA A CA 1 ATOM 1771 C C . ALA A 1 250 ? -29.143 59.602 16.366 1.00 43.41 ? 227 ALA A C 1 ATOM 1772 O O . ALA A 1 250 ? -29.908 60.138 17.166 1.00 38.93 ? 227 ALA A O 1 ATOM 1773 C CB . ALA A 1 250 ? -27.137 58.354 17.201 1.00 37.43 ? 227 ALA A CB 1 ATOM 1774 N N . LEU A 1 251 ? -28.793 60.166 15.213 1.00 37.45 ? 228 LEU A N 1 ATOM 1775 C CA . LEU A 1 251 ? -29.309 61.473 14.820 1.00 34.89 ? 228 LEU A CA 1 ATOM 1776 C C . LEU A 1 251 ? -30.776 61.401 14.394 1.00 45.89 ? 228 LEU A C 1 ATOM 1777 O O . LEU A 1 251 ? -31.519 62.373 14.547 1.00 41.58 ? 228 LEU A O 1 ATOM 1778 C CB . LEU A 1 251 ? -28.455 62.086 13.704 1.00 33.83 ? 228 LEU A CB 1 ATOM 1779 C CG . LEU A 1 251 ? -27.002 62.420 14.060 1.00 44.80 ? 228 LEU A CG 1 ATOM 1780 C CD1 . LEU A 1 251 ? -26.284 63.024 12.866 1.00 48.45 ? 228 LEU A CD1 1 ATOM 1781 C CD2 . LEU A 1 251 ? -26.932 63.359 15.259 1.00 43.06 ? 228 LEU A CD2 1 ATOM 1782 N N . PHE A 1 252 ? -31.183 60.251 13.859 1.00 39.53 ? 229 PHE A N 1 ATOM 1783 C CA . PHE A 1 252 ? -32.579 60.018 13.489 1.00 41.18 ? 229 PHE A CA 1 ATOM 1784 C C . PHE A 1 252 ? -33.514 60.213 14.678 1.00 41.30 ? 229 PHE A C 1 ATOM 1785 O O . PHE A 1 252 ? -34.584 60.802 14.546 1.00 39.74 ? 229 PHE A O 1 ATOM 1786 C CB . PHE A 1 252 ? -32.776 58.596 12.945 1.00 38.40 ? 229 PHE A CB 1 ATOM 1787 C CG . PHE A 1 252 ? -32.364 58.421 11.510 1.00 32.81 ? 229 PHE A CG 1 ATOM 1788 C CD1 . PHE A 1 252 ? -31.868 59.487 10.776 1.00 29.71 ? 229 PHE A CD1 1 ATOM 1789 C CD2 . PHE A 1 252 ? -32.488 57.188 10.892 1.00 31.85 ? 229 PHE A CD2 1 ATOM 1790 C CE1 . PHE A 1 252 ? -31.495 59.321 9.456 1.00 36.03 ? 229 PHE A CE1 1 ATOM 1791 C CE2 . PHE A 1 252 ? -32.121 57.016 9.571 1.00 38.40 ? 229 PHE A CE2 1 ATOM 1792 C CZ . PHE A 1 252 ? -31.622 58.085 8.851 1.00 35.14 ? 229 PHE A CZ 1 ATOM 1793 N N . VAL A 1 253 ? -33.101 59.713 15.840 1.00 38.69 ? 230 VAL A N 1 ATOM 1794 C CA . VAL A 1 253 ? -33.966 59.703 17.013 1.00 39.98 ? 230 VAL A CA 1 ATOM 1795 C C . VAL A 1 253 ? -33.709 60.875 17.958 1.00 45.87 ? 230 VAL A C 1 ATOM 1796 O O . VAL A 1 253 ? -34.342 60.978 19.009 1.00 35.51 ? 230 VAL A O 1 ATOM 1797 C CB . VAL A 1 253 ? -33.820 58.385 17.804 1.00 38.80 ? 230 VAL A CB 1 ATOM 1798 C CG1 . VAL A 1 253 ? -34.035 57.191 16.883 1.00 36.87 ? 230 VAL A CG1 1 ATOM 1799 C CG2 . VAL A 1 253 ? -32.455 58.310 18.473 1.00 31.83 ? 230 VAL A CG2 1 ATOM 1800 N N . SER A 1 254 ? -32.787 61.757 17.584 1.00 38.04 ? 231 SER A N 1 ATOM 1801 C CA . SER A 1 254 ? -32.410 62.863 18.460 1.00 45.54 ? 231 SER A CA 1 ATOM 1802 C C . SER A 1 254 ? -32.483 64.232 17.777 1.00 47.02 ? 231 SER A C 1 ATOM 1803 O O . SER A 1 254 ? -31.595 65.069 17.945 1.00 46.21 ? 231 SER A O 1 ATOM 1804 C CB . SER A 1 254 ? -31.018 62.623 19.057 1.00 44.20 ? 231 SER A CB 1 ATOM 1805 O OG . SER A 1 254 ? -30.038 62.467 18.046 1.00 57.20 ? 231 SER A OG 1 ATOM 1806 N N . SER A 1 255 ? -33.556 64.462 17.031 1.00 43.26 ? 232 SER A N 1 ATOM 1807 C CA . SER A 1 255 ? -33.761 65.726 16.332 1.00 50.03 ? 232 SER A CA 1 ATOM 1808 C C . SER A 1 255 ? -34.020 66.886 17.285 1.00 57.69 ? 232 SER A C 1 ATOM 1809 O O . SER A 1 255 ? -34.066 68.034 16.875 1.00 62.62 ? 232 SER A O 1 ATOM 1810 C CB . SER A 1 255 ? -34.919 65.609 15.349 1.00 47.36 ? 232 SER A CB 1 ATOM 1811 O OG . SER A 1 255 ? -35.301 64.262 15.174 1.00 68.64 ? 232 SER A OG 1 ATOM 1812 N N . ASP A 1 256 ? -34.180 66.575 18.559 1.00 46.42 ? 233 ASP A N 1 ATOM 1813 C CA . ASP A 1 256 ? -34.404 67.580 19.585 1.00 54.36 ? 233 ASP A CA 1 ATOM 1814 C C . ASP A 1 256 ? -33.176 68.448 19.801 1.00 63.65 ? 233 ASP A C 1 ATOM 1815 O O . ASP A 1 256 ? -33.275 69.559 20.321 1.00 66.09 ? 233 ASP A O 1 ATOM 1816 C CB . ASP A 1 256 ? -34.749 66.896 20.907 1.00 60.00 ? 233 ASP A CB 1 ATOM 1817 C CG . ASP A 1 256 ? -36.158 66.350 20.933 1.00 54.38 ? 233 ASP A CG 1 ATOM 1818 O OD1 . ASP A 1 256 ? -36.861 66.440 19.902 1.00 62.96 ? 233 ASP A OD1 1 ATOM 1819 O OD2 . ASP A 1 256 ? -36.557 65.828 21.991 1.00 54.33 ? 233 ASP A OD2 1 ATOM 1820 N N . TYR A 1 257 ? -32.016 67.938 19.404 1.00 57.40 ? 234 TYR A N 1 ATOM 1821 C CA . TYR A 1 257 ? -30.759 68.548 19.808 1.00 57.67 ? 234 TYR A CA 1 ATOM 1822 C C . TYR A 1 257 ? -29.945 69.110 18.650 1.00 53.38 ? 234 TYR A C 1 ATOM 1823 O O . TYR A 1 257 ? -28.763 69.410 18.808 1.00 64.26 ? 234 TYR A O 1 ATOM 1824 C CB . TYR A 1 257 ? -29.931 67.540 20.606 1.00 59.93 ? 234 TYR A CB 1 ATOM 1825 C CG . TYR A 1 257 ? -30.732 66.815 21.664 1.00 52.39 ? 234 TYR A CG 1 ATOM 1826 C CD1 . TYR A 1 257 ? -30.968 67.394 22.904 1.00 47.24 ? 234 TYR A CD1 1 ATOM 1827 C CD2 . TYR A 1 257 ? -31.258 65.551 21.422 1.00 61.25 ? 234 TYR A CD2 1 ATOM 1828 C CE1 . TYR A 1 257 ? -31.699 66.735 23.875 1.00 44.85 ? 234 TYR A CE1 1 ATOM 1829 C CE2 . TYR A 1 257 ? -31.994 64.886 22.386 1.00 57.98 ? 234 TYR A CE2 1 ATOM 1830 C CZ . TYR A 1 257 ? -32.210 65.481 23.610 1.00 55.07 ? 234 TYR A CZ 1 ATOM 1831 O OH . TYR A 1 257 ? -32.940 64.824 24.573 1.00 60.49 ? 234 TYR A OH 1 ATOM 1832 N N . TYR A 1 258 ? -30.590 69.292 17.509 1.00 58.02 ? 235 TYR A N 1 ATOM 1833 C CA . TYR A 1 258 ? -29.926 69.913 16.379 1.00 59.00 ? 235 TYR A CA 1 ATOM 1834 C C . TYR A 1 258 ? -30.912 70.480 15.366 1.00 61.79 ? 235 TYR A C 1 ATOM 1835 O O . TYR A 1 258 ? -32.048 70.036 15.276 1.00 58.39 ? 235 TYR A O 1 ATOM 1836 C CB . TYR A 1 258 ? -28.941 68.941 15.726 1.00 52.30 ? 235 TYR A CB 1 ATOM 1837 C CG . TYR A 1 258 ? -29.573 67.776 15.013 1.00 50.25 ? 235 TYR A CG 1 ATOM 1838 C CD1 . TYR A 1 258 ? -29.813 66.580 15.670 1.00 45.06 ? 235 TYR A CD1 1 ATOM 1839 C CD2 . TYR A 1 258 ? -29.916 67.866 13.679 1.00 44.48 ? 235 TYR A CD2 1 ATOM 1840 C CE1 . TYR A 1 258 ? -30.388 65.514 15.015 1.00 38.24 ? 235 TYR A CE1 1 ATOM 1841 C CE2 . TYR A 1 258 ? -30.487 66.808 13.018 1.00 43.27 ? 235 TYR A CE2 1 ATOM 1842 C CZ . TYR A 1 258 ? -30.720 65.636 13.691 1.00 48.06 ? 235 TYR A CZ 1 ATOM 1843 O OH . TYR A 1 258 ? -31.292 64.591 13.024 1.00 48.13 ? 235 TYR A OH 1 ATOM 1844 N N . ASN A 1 259 ? -30.463 71.477 14.616 1.00 60.29 ? 236 ASN A N 1 ATOM 1845 C CA . ASN A 1 259 ? -31.287 72.123 13.604 1.00 65.63 ? 236 ASN A CA 1 ATOM 1846 C C . ASN A 1 259 ? -31.052 71.481 12.246 1.00 57.57 ? 236 ASN A C 1 ATOM 1847 O O . ASN A 1 259 ? -30.171 70.635 12.102 1.00 51.34 ? 236 ASN A O 1 ATOM 1848 C CB . ASN A 1 259 ? -30.969 73.618 13.533 1.00 76.59 ? 236 ASN A CB 1 ATOM 1849 C CG . ASN A 1 259 ? -30.817 74.249 14.907 1.00 90.87 ? 236 ASN A CG 1 ATOM 1850 O OD1 . ASN A 1 259 ? -31.801 74.629 15.541 1.00 96.45 ? 236 ASN A OD1 1 ATOM 1851 N ND2 . ASN A 1 259 ? -29.577 74.363 15.372 1.00 89.36 ? 236 ASN A ND2 1 ATOM 1852 N N . GLU A 1 260 ? -31.832 71.891 11.250 1.00 65.40 ? 237 GLU A N 1 ATOM 1853 C CA . GLU A 1 260 ? -31.691 71.356 9.900 1.00 66.49 ? 237 GLU A CA 1 ATOM 1854 C C . GLU A 1 260 ? -30.340 71.713 9.284 1.00 70.23 ? 237 GLU A C 1 ATOM 1855 O O . GLU A 1 260 ? -29.825 70.988 8.432 1.00 74.63 ? 237 GLU A O 1 ATOM 1856 C CB . GLU A 1 260 ? -32.821 71.855 8.994 1.00 82.62 ? 237 GLU A CB 1 ATOM 1857 C CG . GLU A 1 260 ? -32.826 73.361 8.762 1.00 97.93 ? 237 GLU A CG 1 ATOM 1858 C CD . GLU A 1 260 ? -33.509 73.750 7.464 1.00 106.71 ? 237 GLU A CD 1 ATOM 1859 O OE1 . GLU A 1 260 ? -33.724 74.961 7.240 1.00 107.59 ? 237 GLU A OE1 1 ATOM 1860 O OE2 . GLU A 1 260 ? -33.826 72.844 6.664 1.00 111.29 ? 237 GLU A OE2 1 ATOM 1861 N N . ASN A 1 261 ? -29.771 72.833 9.717 1.00 61.03 ? 238 ASN A N 1 ATOM 1862 C CA . ASN A 1 261 ? -28.506 73.306 9.166 1.00 66.34 ? 238 ASN A CA 1 ATOM 1863 C C . ASN A 1 261 ? -27.286 72.810 9.940 1.00 66.85 ? 238 ASN A C 1 ATOM 1864 O O . ASN A 1 261 ? -26.158 73.221 9.669 1.00 70.32 ? 238 ASN A O 1 ATOM 1865 C CB . ASN A 1 261 ? -28.501 74.835 9.047 1.00 76.89 ? 238 ASN A CB 1 ATOM 1866 C CG . ASN A 1 261 ? -28.988 75.522 10.309 1.00 81.38 ? 238 ASN A CG 1 ATOM 1867 O OD1 . ASN A 1 261 ? -28.764 75.043 11.420 1.00 92.01 ? 238 ASN A OD1 1 ATOM 1868 N ND2 . ASN A 1 261 ? -29.666 76.651 10.141 1.00 79.30 ? 238 ASN A ND2 1 ATOM 1869 N N . ASP A 1 262 ? -27.517 71.926 10.905 1.00 62.86 ? 239 ASP A N 1 ATOM 1870 C CA . ASP A 1 262 ? -26.422 71.282 11.618 1.00 48.66 ? 239 ASP A CA 1 ATOM 1871 C C . ASP A 1 262 ? -26.031 69.993 10.906 1.00 51.14 ? 239 ASP A C 1 ATOM 1872 O O . ASP A 1 262 ? -24.921 69.487 11.077 1.00 53.43 ? 239 ASP A O 1 ATOM 1873 C CB . ASP A 1 262 ? -26.810 70.986 13.069 1.00 57.47 ? 239 ASP A CB 1 ATOM 1874 C CG . ASP A 1 262 ? -26.995 72.247 13.895 1.00 61.91 ? 239 ASP A CG 1 ATOM 1875 O OD1 . ASP A 1 262 ? -26.361 73.273 13.572 1.00 69.62 ? 239 ASP A OD1 1 ATOM 1876 O OD2 . ASP A 1 262 ? -27.772 72.209 14.872 1.00 53.69 ? 239 ASP A OD2 1 ATOM 1877 N N . TRP A 1 263 ? -26.948 69.470 10.099 1.00 42.46 ? 240 TRP A N 1 ATOM 1878 C CA . TRP A 1 263 ? -26.721 68.209 9.405 1.00 47.13 ? 240 TRP A CA 1 ATOM 1879 C C . TRP A 1 263 ? -27.573 68.080 8.150 1.00 50.46 ? 240 TRP A C 1 ATOM 1880 O O . TRP A 1 263 ? -28.789 68.254 8.192 1.00 53.88 ? 240 TRP A O 1 ATOM 1881 C CB . TRP A 1 263 ? -27.013 67.029 10.334 1.00 35.32 ? 240 TRP A CB 1 ATOM 1882 C CG . TRP A 1 263 ? -26.784 65.694 9.695 1.00 46.82 ? 240 TRP A CG 1 ATOM 1883 C CD1 . TRP A 1 263 ? -25.745 65.339 8.882 1.00 46.65 ? 240 TRP A CD1 1 ATOM 1884 C CD2 . TRP A 1 263 ? -27.621 64.536 9.805 1.00 45.28 ? 240 TRP A CD2 1 ATOM 1885 N NE1 . TRP A 1 263 ? -25.880 64.029 8.487 1.00 44.42 ? 240 TRP A NE1 1 ATOM 1886 C CE2 . TRP A 1 263 ? -27.023 63.514 9.039 1.00 41.83 ? 240 TRP A CE2 1 ATOM 1887 C CE3 . TRP A 1 263 ? -28.815 64.263 10.479 1.00 38.71 ? 240 TRP A CE3 1 ATOM 1888 C CZ2 . TRP A 1 263 ? -27.579 62.241 8.930 1.00 43.99 ? 240 TRP A CZ2 1 ATOM 1889 C CZ3 . TRP A 1 263 ? -29.365 62.998 10.369 1.00 40.79 ? 240 TRP A CZ3 1 ATOM 1890 C CH2 . TRP A 1 263 ? -28.748 62.003 9.603 1.00 42.03 ? 240 TRP A CH2 1 ATOM 1891 N N . ASN A 1 264 ? -26.923 67.769 7.036 1.00 59.36 ? 241 ASN A N 1 ATOM 1892 C CA . ASN A 1 264 ? -27.625 67.450 5.804 1.00 53.41 ? 241 ASN A CA 1 ATOM 1893 C C . ASN A 1 264 ? -27.653 65.937 5.644 1.00 52.64 ? 241 ASN A C 1 ATOM 1894 O O . ASN A 1 264 ? -26.670 65.334 5.209 1.00 56.75 ? 241 ASN A O 1 ATOM 1895 C CB . ASN A 1 264 ? -26.922 68.103 4.612 1.00 51.63 ? 241 ASN A CB 1 ATOM 1896 C CG . ASN A 1 264 ? -27.723 68.000 3.324 1.00 58.08 ? 241 ASN A CG 1 ATOM 1897 O OD1 . ASN A 1 264 ? -28.585 67.135 3.176 1.00 66.63 ? 241 ASN A OD1 1 ATOM 1898 N ND2 . ASN A 1 264 ? -27.432 68.886 2.380 1.00 64.06 ? 241 ASN A ND2 1 ATOM 1899 N N . CYS A 1 265 ? -28.779 65.327 6.005 1.00 51.06 ? 242 CYS A N 1 ATOM 1900 C CA . CYS A 1 265 ? -28.909 63.872 5.980 1.00 44.57 ? 242 CYS A CA 1 ATOM 1901 C C . CYS A 1 265 ? -28.742 63.315 4.573 1.00 43.28 ? 242 CYS A C 1 ATOM 1902 O O . CYS A 1 265 ? -28.177 62.239 4.387 1.00 39.02 ? 242 CYS A O 1 ATOM 1903 C CB . CYS A 1 265 ? -30.260 63.439 6.557 1.00 49.03 ? 242 CYS A CB 1 ATOM 1904 S SG . CYS A 1 265 ? -30.522 61.643 6.595 1.00 53.61 ? 242 CYS A SG 1 ATOM 1905 N N . GLN A 1 266 ? -29.234 64.054 3.585 1.00 46.11 ? 243 GLN A N 1 ATOM 1906 C CA . GLN A 1 266 ? -29.177 63.599 2.204 1.00 47.60 ? 243 GLN A CA 1 ATOM 1907 C C . GLN A 1 266 ? -27.738 63.502 1.699 1.00 48.07 ? 243 GLN A C 1 ATOM 1908 O O . GLN A 1 266 ? -27.384 62.551 1.003 1.00 52.97 ? 243 GLN A O 1 ATOM 1909 C CB . GLN A 1 266 ? -30.002 64.515 1.298 1.00 44.79 ? 243 GLN A CB 1 ATOM 1910 C CG . GLN A 1 266 ? -30.261 63.935 -0.079 1.00 46.28 ? 243 GLN A CG 1 ATOM 1911 C CD . GLN A 1 266 ? -31.081 62.658 -0.026 1.00 64.23 ? 243 GLN A CD 1 ATOM 1912 O OE1 . GLN A 1 266 ? -30.730 61.655 -0.648 1.00 66.99 ? 243 GLN A OE1 1 ATOM 1913 N NE2 . GLN A 1 266 ? -32.183 62.691 0.717 1.00 65.24 ? 243 GLN A NE2 1 ATOM 1914 N N . GLN A 1 267 ? -26.912 64.483 2.052 1.00 53.91 ? 244 GLN A N 1 ATOM 1915 C CA . GLN A 1 267 ? -25.506 64.463 1.657 1.00 51.75 ? 244 GLN A CA 1 ATOM 1916 C C . GLN A 1 267 ? -24.801 63.261 2.275 1.00 48.12 ? 244 GLN A C 1 ATOM 1917 O O . GLN A 1 267 ? -24.067 62.544 1.595 1.00 44.20 ? 244 GLN A O 1 ATOM 1918 C CB . GLN A 1 267 ? -24.799 65.753 2.076 1.00 51.19 ? 244 GLN A CB 1 ATOM 1919 C CG . GLN A 1 267 ? -23.342 65.816 1.636 1.00 53.10 ? 244 GLN A CG 1 ATOM 1920 C CD . GLN A 1 267 ? -22.499 66.718 2.516 1.00 58.39 ? 244 GLN A CD 1 ATOM 1921 O OE1 . GLN A 1 267 ? -22.916 67.108 3.607 1.00 59.48 ? 244 GLN A OE1 1 ATOM 1922 N NE2 . GLN A 1 267 ? -21.302 67.051 2.046 1.00 54.39 ? 244 GLN A NE2 1 ATOM 1923 N N . THR A 1 268 ? -25.035 63.050 3.567 1.00 39.89 ? 245 THR A N 1 ATOM 1924 C CA . THR A 1 268 ? -24.490 61.898 4.278 1.00 43.53 ? 245 THR A CA 1 ATOM 1925 C C . THR A 1 268 ? -24.916 60.597 3.603 1.00 50.27 ? 245 THR A C 1 ATOM 1926 O O . THR A 1 268 ? -24.091 59.719 3.349 1.00 49.73 ? 245 THR A O 1 ATOM 1927 C CB . THR A 1 268 ? -24.948 61.879 5.750 1.00 39.64 ? 245 THR A CB 1 ATOM 1928 O OG1 . THR A 1 268 ? -24.387 63.000 6.445 1.00 38.66 ? 245 THR A OG1 1 ATOM 1929 C CG2 . THR A 1 268 ? -24.503 60.599 6.432 1.00 31.96 ? 245 THR A CG2 1 ATOM 1930 N N . LEU A 1 269 ? -26.207 60.490 3.306 1.00 48.16 ? 246 LEU A N 1 ATOM 1931 C CA . LEU A 1 269 ? -26.756 59.325 2.620 1.00 51.15 ? 246 LEU A CA 1 ATOM 1932 C C . LEU A 1 269 ? -26.098 59.101 1.258 1.00 48.65 ? 246 LEU A C 1 ATOM 1933 O O . LEU A 1 269 ? -25.700 57.981 0.932 1.00 55.41 ? 246 LEU A O 1 ATOM 1934 C CB . LEU A 1 269 ? -28.272 59.480 2.455 1.00 55.79 ? 246 LEU A CB 1 ATOM 1935 C CG . LEU A 1 269 ? -29.009 58.423 1.632 1.00 51.95 ? 246 LEU A CG 1 ATOM 1936 C CD1 . LEU A 1 269 ? -28.880 57.052 2.272 1.00 46.91 ? 246 LEU A CD1 1 ATOM 1937 C CD2 . LEU A 1 269 ? -30.471 58.805 1.472 1.00 60.30 ? 246 LEU A CD2 1 ATOM 1938 N N . ASN A 1 270 ? -25.981 60.169 0.472 1.00 46.02 ? 247 ASN A N 1 ATOM 1939 C CA . ASN A 1 270 ? -25.380 60.090 -0.858 1.00 50.05 ? 247 ASN A CA 1 ATOM 1940 C C . ASN A 1 270 ? -23.928 59.622 -0.834 1.00 50.36 ? 247 ASN A C 1 ATOM 1941 O O . ASN A 1 270 ? -23.522 58.783 -1.639 1.00 58.06 ? 247 ASN A O 1 ATOM 1942 C CB . ASN A 1 270 ? -25.483 61.437 -1.583 1.00 51.35 ? 247 ASN A CB 1 ATOM 1943 C CG . ASN A 1 270 ? -26.910 61.794 -1.953 1.00 57.98 ? 247 ASN A CG 1 ATOM 1944 O OD1 . ASN A 1 270 ? -27.777 60.925 -2.041 1.00 62.80 ? 247 ASN A OD1 1 ATOM 1945 N ND2 . ASN A 1 270 ? -27.159 63.079 -2.177 1.00 58.98 ? 247 ASN A ND2 1 ATOM 1946 N N . THR A 1 271 ? -23.152 60.171 0.093 1.00 45.04 ? 248 THR A N 1 ATOM 1947 C CA . THR A 1 271 ? -21.757 59.782 0.253 1.00 46.04 ? 248 THR A CA 1 ATOM 1948 C C . THR A 1 271 ? -21.637 58.304 0.621 1.00 49.18 ? 248 THR A C 1 ATOM 1949 O O . THR A 1 271 ? -20.786 57.590 0.089 1.00 41.96 ? 248 THR A O 1 ATOM 1950 C CB . THR A 1 271 ? -21.059 60.646 1.317 1.00 45.03 ? 248 THR A CB 1 ATOM 1951 O OG1 . THR A 1 271 ? -21.062 62.015 0.891 1.00 53.02 ? 248 THR A OG1 1 ATOM 1952 C CG2 . THR A 1 271 ? -19.625 60.191 1.526 1.00 43.86 ? 248 THR A CG2 1 ATOM 1953 N N . VAL A 1 272 ? -22.501 57.846 1.522 1.00 44.63 ? 249 VAL A N 1 ATOM 1954 C CA . VAL A 1 272 ? -22.515 56.439 1.909 1.00 46.73 ? 249 VAL A CA 1 ATOM 1955 C C . VAL A 1 272 ? -22.839 55.542 0.712 1.00 46.44 ? 249 VAL A C 1 ATOM 1956 O O . VAL A 1 272 ? -22.173 54.529 0.492 1.00 45.97 ? 249 VAL A O 1 ATOM 1957 C CB . VAL A 1 272 ? -23.504 56.175 3.064 1.00 44.17 ? 249 VAL A CB 1 ATOM 1958 C CG1 . VAL A 1 272 ? -23.650 54.678 3.319 1.00 41.34 ? 249 VAL A CG1 1 ATOM 1959 C CG2 . VAL A 1 272 ? -23.041 56.890 4.324 1.00 39.03 ? 249 VAL A CG2 1 ATOM 1960 N N . LEU A 1 273 ? -23.847 55.927 -0.068 1.00 38.40 ? 250 LEU A N 1 ATOM 1961 C CA . LEU A 1 273 ? -24.230 55.162 -1.254 1.00 45.71 ? 250 LEU A CA 1 ATOM 1962 C C . LEU A 1 273 ? -23.072 55.065 -2.245 1.00 43.18 ? 250 LEU A C 1 ATOM 1963 O O . LEU A 1 273 ? -22.881 54.037 -2.896 1.00 46.59 ? 250 LEU A O 1 ATOM 1964 C CB . LEU A 1 273 ? -25.458 55.780 -1.932 1.00 48.69 ? 250 LEU A CB 1 ATOM 1965 C CG . LEU A 1 273 ? -26.781 55.700 -1.165 1.00 56.24 ? 250 LEU A CG 1 ATOM 1966 C CD1 . LEU A 1 273 ? -27.879 56.458 -1.900 1.00 58.88 ? 250 LEU A CD1 1 ATOM 1967 C CD2 . LEU A 1 273 ? -27.189 54.251 -0.935 1.00 48.91 ? 250 LEU A CD2 1 ATOM 1968 N N . THR A 1 274 ? -22.300 56.140 -2.350 1.00 49.44 ? 251 THR A N 1 ATOM 1969 C CA . THR A 1 274 ? -21.122 56.152 -3.206 1.00 50.93 ? 251 THR A CA 1 ATOM 1970 C C . THR A 1 274 ? -20.095 55.146 -2.703 1.00 45.67 ? 251 THR A C 1 ATOM 1971 O O . THR A 1 274 ? -19.488 54.420 -3.490 1.00 56.23 ? 251 THR A O 1 ATOM 1972 C CB . THR A 1 274 ? -20.480 57.544 -3.254 1.00 49.43 ? 251 THR A CB 1 ATOM 1973 O OG1 . THR A 1 274 ? -21.425 58.487 -3.770 1.00 53.42 ? 251 THR A OG1 1 ATOM 1974 C CG2 . THR A 1 274 ? -19.246 57.530 -4.142 1.00 47.43 ? 251 THR A CG2 1 ATOM 1975 N N . GLU A 1 275 ? -19.912 55.107 -1.386 1.00 42.19 ? 252 GLU A N 1 ATOM 1976 C CA . GLU A 1 275 ? -18.982 54.170 -0.765 1.00 43.60 ? 252 GLU A CA 1 ATOM 1977 C C . GLU A 1 275 ? -19.374 52.724 -1.052 1.00 45.67 ? 252 GLU A C 1 ATOM 1978 O O . GLU A 1 275 ? -18.518 51.891 -1.345 1.00 53.47 ? 252 GLU A O 1 ATOM 1979 C CB . GLU A 1 275 ? -18.919 54.397 0.748 1.00 48.08 ? 252 GLU A CB 1 ATOM 1980 C CG . GLU A 1 275 ? -18.428 55.775 1.165 1.00 55.54 ? 252 GLU A CG 1 ATOM 1981 C CD . GLU A 1 275 ? -16.923 55.924 1.062 1.00 72.65 ? 252 GLU A CD 1 ATOM 1982 O OE1 . GLU A 1 275 ? -16.388 55.878 -0.066 1.00 80.82 ? 252 GLU A OE1 1 ATOM 1983 O OE2 . GLU A 1 275 ? -16.274 56.088 2.116 1.00 74.18 ? 252 GLU A OE2 1 ATOM 1984 N N . ILE A 1 276 ? -20.670 52.434 -0.960 1.00 48.10 ? 253 ILE A N 1 ATOM 1985 C CA . ILE A 1 276 ? -21.185 51.092 -1.219 1.00 45.54 ? 253 ILE A CA 1 ATOM 1986 C C . ILE A 1 276 ? -20.839 50.622 -2.628 1.00 46.66 ? 253 ILE A C 1 ATOM 1987 O O . ILE A 1 276 ? -20.375 49.497 -2.821 1.00 51.52 ? 253 ILE A O 1 ATOM 1988 C CB . ILE A 1 276 ? -22.714 51.027 -1.036 1.00 47.49 ? 253 ILE A CB 1 ATOM 1989 C CG1 . ILE A 1 276 ? -23.097 51.382 0.401 1.00 43.06 ? 253 ILE A CG1 1 ATOM 1990 C CG2 . ILE A 1 276 ? -23.239 49.643 -1.396 1.00 42.97 ? 253 ILE A CG2 1 ATOM 1991 C CD1 . ILE A 1 276 ? -24.590 51.419 0.639 1.00 42.71 ? 253 ILE A CD1 1 ATOM 1992 N N . SER A 1 277 ? -21.057 51.494 -3.606 1.00 40.52 ? 254 SER A N 1 ATOM 1993 C CA . SER A 1 277 ? -20.796 51.160 -5.000 1.00 50.61 ? 254 SER A CA 1 ATOM 1994 C C . SER A 1 277 ? -19.310 50.916 -5.237 1.00 53.48 ? 254 SER A C 1 ATOM 1995 O O . SER A 1 277 ? -18.928 50.190 -6.153 1.00 56.05 ? 254 SER A O 1 ATOM 1996 C CB . SER A 1 277 ? -21.303 52.271 -5.921 1.00 51.51 ? 254 SER A CB 1 ATOM 1997 O OG . SER A 1 277 ? -20.630 53.489 -5.661 1.00 65.13 ? 254 SER A OG 1 ATOM 1998 N N . GLN A 1 278 ? -18.475 51.522 -4.400 1.00 48.46 ? 255 GLN A N 1 ATOM 1999 C CA . GLN A 1 278 ? -17.031 51.350 -4.507 1.00 51.84 ? 255 GLN A CA 1 ATOM 2000 C C . GLN A 1 278 ? -16.543 50.136 -3.721 1.00 52.32 ? 255 GLN A C 1 ATOM 2001 O O . GLN A 1 278 ? -15.348 49.850 -3.689 1.00 60.19 ? 255 GLN A O 1 ATOM 2002 C CB . GLN A 1 278 ? -16.310 52.614 -4.045 1.00 55.75 ? 255 GLN A CB 1 ATOM 2003 C CG . GLN A 1 278 ? -16.590 53.822 -4.919 1.00 61.71 ? 255 GLN A CG 1 ATOM 2004 C CD . GLN A 1 278 ? -16.064 55.108 -4.321 1.00 74.59 ? 255 GLN A CD 1 ATOM 2005 O OE1 . GLN A 1 278 ? -15.735 55.165 -3.136 1.00 80.25 ? 255 GLN A OE1 1 ATOM 2006 N NE2 . GLN A 1 278 ? -15.982 56.151 -5.139 1.00 78.02 ? 255 GLN A NE2 1 ATOM 2007 N N . GLY A 1 279 ? -17.475 49.425 -3.094 1.00 53.36 ? 256 GLY A N 1 ATOM 2008 C CA . GLY A 1 279 ? -17.152 48.206 -2.372 1.00 49.40 ? 256 GLY A CA 1 ATOM 2009 C C . GLY A 1 279 ? -16.570 48.441 -0.990 1.00 51.16 ? 256 GLY A C 1 ATOM 2010 O O . GLY A 1 279 ? -15.845 47.597 -0.467 1.00 50.33 ? 256 GLY A O 1 ATOM 2011 N N . ALA A 1 280 ? -16.892 49.584 -0.393 1.00 46.42 ? 257 ALA A N 1 ATOM 2012 C CA . ALA A 1 280 ? -16.362 49.928 0.924 1.00 46.51 ? 257 ALA A CA 1 ATOM 2013 C C . ALA A 1 280 ? -16.941 49.042 2.023 1.00 49.05 ? 257 ALA A C 1 ATOM 2014 O O . ALA A 1 280 ? -16.344 48.892 3.088 1.00 49.35 ? 257 ALA A O 1 ATOM 2015 C CB . ALA A 1 280 ? -16.621 51.392 1.234 1.00 38.33 ? 257 ALA A CB 1 ATOM 2016 N N . PHE A 1 281 ? -18.102 48.454 1.759 1.00 46.77 ? 258 PHE A N 1 ATOM 2017 C CA . PHE A 1 281 ? -18.789 47.646 2.759 1.00 47.27 ? 258 PHE A CA 1 ATOM 2018 C C . PHE A 1 281 ? -18.746 46.154 2.443 1.00 52.31 ? 258 PHE A C 1 ATOM 2019 O O . PHE A 1 281 ? -19.747 45.451 2.580 1.00 51.53 ? 258 PHE A O 1 ATOM 2020 C CB . PHE A 1 281 ? -20.234 48.119 2.919 1.00 34.91 ? 258 PHE A CB 1 ATOM 2021 C CG . PHE A 1 281 ? -20.355 49.492 3.510 1.00 33.38 ? 258 PHE A CG 1 ATOM 2022 C CD1 . PHE A 1 281 ? -20.431 49.664 4.881 1.00 36.15 ? 258 PHE A CD1 1 ATOM 2023 C CD2 . PHE A 1 281 ? -20.382 50.612 2.696 1.00 34.61 ? 258 PHE A CD2 1 ATOM 2024 C CE1 . PHE A 1 281 ? -20.536 50.926 5.431 1.00 30.30 ? 258 PHE A CE1 1 ATOM 2025 C CE2 . PHE A 1 281 ? -20.489 51.878 3.241 1.00 40.71 ? 258 PHE A CE2 1 ATOM 2026 C CZ . PHE A 1 281 ? -20.565 52.035 4.610 1.00 36.34 ? 258 PHE A CZ 1 ATOM 2027 N N . SER A 1 282 ? -17.576 45.676 2.031 1.00 52.57 ? 259 SER A N 1 ATOM 2028 C CA . SER A 1 282 ? -17.389 44.265 1.713 1.00 52.37 ? 259 SER A CA 1 ATOM 2029 C C . SER A 1 282 ? -17.370 43.392 2.969 1.00 43.62 ? 259 SER A C 1 ATOM 2030 O O . SER A 1 282 ? -17.602 42.187 2.900 1.00 47.88 ? 259 SER A O 1 ATOM 2031 C CB . SER A 1 282 ? -16.099 44.067 0.915 1.00 45.77 ? 259 SER A CB 1 ATOM 2032 O OG . SER A 1 282 ? -14.984 44.566 1.632 1.00 59.62 ? 259 SER A OG 1 ATOM 2033 N N . ASN A 1 283 ? -17.085 44.002 4.114 1.00 41.44 ? 260 ASN A N 1 ATOM 2034 C CA . ASN A 1 283 ? -17.138 43.290 5.386 1.00 36.12 ? 260 ASN A CA 1 ATOM 2035 C C . ASN A 1 283 ? -18.589 43.186 5.873 1.00 40.50 ? 260 ASN A C 1 ATOM 2036 O O . ASN A 1 283 ? -19.252 44.205 6.063 1.00 40.71 ? 260 ASN A O 1 ATOM 2037 C CB . ASN A 1 283 ? -16.262 44.007 6.420 1.00 31.22 ? 260 ASN A CB 1 ATOM 2038 C CG . ASN A 1 283 ? -16.010 43.172 7.663 1.00 43.77 ? 260 ASN A CG 1 ATOM 2039 O OD1 . ASN A 1 283 ? -16.922 42.549 8.209 1.00 43.24 ? 260 ASN A OD1 1 ATOM 2040 N ND2 . ASN A 1 283 ? -14.761 43.160 8.120 1.00 47.50 ? 260 ASN A ND2 1 ATOM 2041 N N . PRO A 1 284 ? -19.080 41.949 6.072 1.00 43.06 ? 261 PRO A N 1 ATOM 2042 C CA . PRO A 1 284 ? -20.464 41.678 6.489 1.00 44.38 ? 261 PRO A CA 1 ATOM 2043 C C . PRO A 1 284 ? -20.874 42.397 7.773 1.00 42.92 ? 261 PRO A C 1 ATOM 2044 O O . PRO A 1 284 ? -22.048 42.737 7.929 1.00 47.32 ? 261 PRO A O 1 ATOM 2045 C CB . PRO A 1 284 ? -20.478 40.154 6.704 1.00 42.26 ? 261 PRO A CB 1 ATOM 2046 C CG . PRO A 1 284 ? -19.042 39.759 6.824 1.00 47.05 ? 261 PRO A CG 1 ATOM 2047 C CD . PRO A 1 284 ? -18.300 40.708 5.939 1.00 37.15 ? 261 PRO A CD 1 ATOM 2048 N N . ASN A 1 285 ? -19.927 42.625 8.677 1.00 39.21 ? 262 ASN A N 1 ATOM 2049 C CA . ASN A 1 285 ? -20.222 43.371 9.896 1.00 38.55 ? 262 ASN A CA 1 ATOM 2050 C C . ASN A 1 285 ? -20.515 44.832 9.587 1.00 38.41 ? 262 ASN A C 1 ATOM 2051 O O . ASN A 1 285 ? -21.404 45.437 10.185 1.00 36.34 ? 262 ASN A O 1 ATOM 2052 C CB . ASN A 1 285 ? -19.070 43.268 10.899 1.00 34.29 ? 262 ASN A CB 1 ATOM 2053 C CG . ASN A 1 285 ? -18.803 41.841 11.335 1.00 48.73 ? 262 ASN A CG 1 ATOM 2054 O OD1 . ASN A 1 285 ? -19.407 41.346 12.286 1.00 55.61 ? 262 ASN A OD1 1 ATOM 2055 N ND2 . ASN A 1 285 ? -17.890 41.171 10.639 1.00 47.11 ? 262 ASN A ND2 1 ATOM 2056 N N . ALA A 1 286 ? -19.766 45.395 8.644 1.00 33.47 ? 263 ALA A N 1 ATOM 2057 C CA . ALA A 1 286 ? -19.949 46.790 8.269 1.00 36.44 ? 263 ALA A CA 1 ATOM 2058 C C . ALA A 1 286 ? -21.227 46.969 7.459 1.00 44.21 ? 263 ALA A C 1 ATOM 2059 O O . ALA A 1 286 ? -21.940 47.960 7.620 1.00 43.28 ? 263 ALA A O 1 ATOM 2060 C CB . ALA A 1 286 ? -18.743 47.301 7.493 1.00 23.56 ? 263 ALA A CB 1 ATOM 2061 N N . ALA A 1 287 ? -21.511 46.005 6.588 1.00 40.71 ? 264 ALA A N 1 ATOM 2062 C CA . ALA A 1 287 ? -22.727 46.044 5.786 1.00 45.96 ? 264 ALA A CA 1 ATOM 2063 C C . ALA A 1 287 ? -23.958 45.968 6.683 1.00 40.57 ? 264 ALA A C 1 ATOM 2064 O O . ALA A 1 287 ? -24.938 46.682 6.470 1.00 34.50 ? 264 ALA A O 1 ATOM 2065 C CB . ALA A 1 287 ? -22.733 44.913 4.768 1.00 37.71 ? 264 ALA A CB 1 ATOM 2066 N N . ALA A 1 288 ? -23.894 45.109 7.695 1.00 33.62 ? 265 ALA A N 1 ATOM 2067 C CA . ALA A 1 288 ? -24.998 44.950 8.633 1.00 37.44 ? 265 ALA A CA 1 ATOM 2068 C C . ALA A 1 288 ? -25.278 46.222 9.427 1.00 37.83 ? 265 ALA A C 1 ATOM 2069 O O . ALA A 1 288 ? -26.434 46.585 9.643 1.00 34.39 ? 265 ALA A O 1 ATOM 2070 C CB . ALA A 1 288 ? -24.732 43.784 9.578 1.00 37.43 ? 265 ALA A CB 1 ATOM 2071 N N . GLN A 1 289 ? -24.225 46.905 9.860 1.00 35.94 ? 266 GLN A N 1 ATOM 2072 C CA . GLN A 1 289 ? -24.403 48.074 10.718 1.00 42.79 ? 266 GLN A CA 1 ATOM 2073 C C . GLN A 1 289 ? -24.905 49.306 9.971 1.00 38.93 ? 266 GLN A C 1 ATOM 2074 O O . GLN A 1 289 ? -25.554 50.169 10.561 1.00 37.02 ? 266 GLN A O 1 ATOM 2075 C CB . GLN A 1 289 ? -23.114 48.397 11.473 1.00 42.31 ? 266 GLN A CB 1 ATOM 2076 C CG . GLN A 1 289 ? -22.738 47.349 12.496 1.00 35.19 ? 266 GLN A CG 1 ATOM 2077 C CD . GLN A 1 289 ? -21.524 47.740 13.312 1.00 37.09 ? 266 GLN A CD 1 ATOM 2078 O OE1 . GLN A 1 289 ? -21.326 47.247 14.423 1.00 38.53 ? 266 GLN A OE1 1 ATOM 2079 N NE2 . GLN A 1 289 ? -20.704 48.629 12.766 1.00 31.19 ? 266 GLN A NE2 1 ATOM 2080 N N . VAL A 1 290 ? -24.613 49.385 8.676 1.00 36.90 ? 267 VAL A N 1 ATOM 2081 C CA . VAL A 1 290 ? -24.973 50.568 7.898 1.00 35.20 ? 267 VAL A CA 1 ATOM 2082 C C . VAL A 1 290 ? -26.388 50.484 7.314 1.00 39.49 ? 267 VAL A C 1 ATOM 2083 O O . VAL A 1 290 ? -27.044 51.506 7.113 1.00 38.50 ? 267 VAL A O 1 ATOM 2084 C CB . VAL A 1 290 ? -23.946 50.852 6.771 1.00 36.46 ? 267 VAL A CB 1 ATOM 2085 C CG1 . VAL A 1 290 ? -24.122 49.880 5.608 1.00 36.47 ? 267 VAL A CG1 1 ATOM 2086 C CG2 . VAL A 1 290 ? -24.070 52.287 6.286 1.00 34.25 ? 267 VAL A CG2 1 ATOM 2087 N N . LEU A 1 291 ? -26.860 49.264 7.076 1.00 33.38 ? 268 LEU A N 1 ATOM 2088 C CA . LEU A 1 291 ? -28.125 49.038 6.373 1.00 31.51 ? 268 LEU A CA 1 ATOM 2089 C C . LEU A 1 291 ? -29.398 49.681 6.962 1.00 28.76 ? 268 LEU A C 1 ATOM 2090 O O . LEU A 1 291 ? -30.148 50.319 6.223 1.00 41.64 ? 268 LEU A O 1 ATOM 2091 C CB . LEU A 1 291 ? -28.347 47.538 6.121 1.00 32.64 ? 268 LEU A CB 1 ATOM 2092 C CG . LEU A 1 291 ? -29.647 47.166 5.405 1.00 37.58 ? 268 LEU A CG 1 ATOM 2093 C CD1 . LEU A 1 291 ? -29.667 47.746 3.996 1.00 25.90 ? 268 LEU A CD1 1 ATOM 2094 C CD2 . LEU A 1 291 ? -29.846 45.651 5.376 1.00 38.10 ? 268 LEU A CD2 1 ATOM 2095 N N . PRO A 1 292 ? -29.658 49.506 8.277 1.00 34.60 ? 269 PRO A N 1 ATOM 2096 C CA . PRO A 1 292 ? -30.928 50.016 8.820 1.00 37.25 ? 269 PRO A CA 1 ATOM 2097 C C . PRO A 1 292 ? -31.168 51.506 8.570 1.00 43.34 ? 269 PRO A C 1 ATOM 2098 O O . PRO A 1 292 ? -32.258 51.885 8.135 1.00 38.83 ? 269 PRO A O 1 ATOM 2099 C CB . PRO A 1 292 ? -30.794 49.751 10.321 1.00 34.59 ? 269 PRO A CB 1 ATOM 2100 C CG . PRO A 1 292 ? -29.892 48.573 10.404 1.00 36.76 ? 269 PRO A CG 1 ATOM 2101 C CD . PRO A 1 292 ? -28.891 48.771 9.302 1.00 30.85 ? 269 PRO A CD 1 ATOM 2102 N N . ALA A 1 293 ? -30.158 52.329 8.833 1.00 35.88 ? 270 ALA A N 1 ATOM 2103 C CA . ALA A 1 293 ? -30.278 53.772 8.661 1.00 40.77 ? 270 ALA A CA 1 ATOM 2104 C C . ALA A 1 293 ? -30.586 54.151 7.217 1.00 34.06 ? 270 ALA A C 1 ATOM 2105 O O . ALA A 1 293 ? -31.363 55.068 6.964 1.00 38.62 ? 270 ALA A O 1 ATOM 2106 C CB . ALA A 1 293 ? -29.015 54.473 9.139 1.00 38.63 ? 270 ALA A CB 1 ATOM 2107 N N . LEU A 1 294 ? -29.988 53.433 6.269 1.00 36.11 ? 271 LEU A N 1 ATOM 2108 C CA . LEU A 1 294 ? -30.196 53.723 4.851 1.00 40.39 ? 271 LEU A CA 1 ATOM 2109 C C . LEU A 1 294 ? -31.643 53.469 4.435 1.00 44.51 ? 271 LEU A C 1 ATOM 2110 O O . LEU A 1 294 ? -32.091 53.931 3.385 1.00 41.81 ? 271 LEU A O 1 ATOM 2111 C CB . LEU A 1 294 ? -29.249 52.890 3.988 1.00 37.20 ? 271 LEU A CB 1 ATOM 2112 C CG . LEU A 1 294 ? -27.764 53.004 4.336 1.00 41.43 ? 271 LEU A CG 1 ATOM 2113 C CD1 . LEU A 1 294 ? -26.934 52.105 3.436 1.00 35.41 ? 271 LEU A CD1 1 ATOM 2114 C CD2 . LEU A 1 294 ? -27.297 54.446 4.240 1.00 46.05 ? 271 LEU A CD2 1 ATOM 2115 N N . MET A 1 295 ? -32.364 52.728 5.269 1.00 41.86 ? 272 MET A N 1 ATOM 2116 C CA . MET A 1 295 ? -33.758 52.411 5.011 1.00 40.74 ? 272 MET A CA 1 ATOM 2117 C C . MET A 1 295 ? -34.644 53.178 5.979 1.00 37.88 ? 272 MET A C 1 ATOM 2118 O O . MET A 1 295 ? -35.835 52.898 6.100 1.00 40.99 ? 272 MET A O 1 ATOM 2119 C CB . MET A 1 295 ? -33.998 50.912 5.178 1.00 42.08 ? 272 MET A CB 1 ATOM 2120 C CG . MET A 1 295 ? -34.953 50.333 4.165 1.00 68.92 ? 272 MET A CG 1 ATOM 2121 S SD . MET A 1 295 ? -34.086 49.884 2.658 1.00 84.26 ? 272 MET A SD 1 ATOM 2122 C CE . MET A 1 295 ? -33.131 48.492 3.252 1.00 50.39 ? 272 MET A CE 1 ATOM 2123 N N . GLY A 1 296 ? -34.048 54.139 6.678 1.00 37.04 ? 273 GLY A N 1 ATOM 2124 C CA . GLY A 1 296 ? -34.786 54.994 7.591 1.00 33.85 ? 273 GLY A CA 1 ATOM 2125 C C . GLY A 1 296 ? -35.169 54.296 8.881 1.00 43.73 ? 273 GLY A C 1 ATOM 2126 O O . GLY A 1 296 ? -36.150 54.659 9.529 1.00 41.99 ? 273 GLY A O 1 ATOM 2127 N N . LYS A 1 297 ? -34.384 53.292 9.259 1.00 44.20 ? 274 LYS A N 1 ATOM 2128 C CA . LYS A 1 297 ? -34.668 52.503 10.449 1.00 35.03 ? 274 LYS A CA 1 ATOM 2129 C C . LYS A 1 297 ? -33.570 52.660 11.491 1.00 38.50 ? 274 LYS A C 1 ATOM 2130 O O . LYS A 1 297 ? -32.412 52.907 11.153 1.00 41.57 ? 274 LYS A O 1 ATOM 2131 C CB . LYS A 1 297 ? -34.818 51.025 10.078 1.00 38.98 ? 274 LYS A CB 1 ATOM 2132 C CG . LYS A 1 297 ? -36.005 50.722 9.174 1.00 41.17 ? 274 LYS A CG 1 ATOM 2133 C CD . LYS A 1 297 ? -37.317 50.866 9.926 1.00 51.89 ? 274 LYS A CD 1 ATOM 2134 C CE . LYS A 1 297 ? -38.504 50.543 9.037 1.00 64.61 ? 274 LYS A CE 1 ATOM 2135 N NZ . LYS A 1 297 ? -39.795 50.710 9.762 1.00 79.23 ? 274 LYS A NZ 1 ATOM 2136 N N . THR A 1 298 ? -33.943 52.527 12.760 1.00 33.03 ? 275 THR A N 1 ATOM 2137 C CA . THR A 1 298 ? -32.973 52.505 13.850 1.00 36.53 ? 275 THR A CA 1 ATOM 2138 C C . THR A 1 298 ? -33.262 51.312 14.752 1.00 42.78 ? 275 THR A C 1 ATOM 2139 O O . THR A 1 298 ? -34.270 50.627 14.581 1.00 38.68 ? 275 THR A O 1 ATOM 2140 C CB . THR A 1 298 ? -33.032 53.782 14.713 1.00 35.30 ? 275 THR A CB 1 ATOM 2141 O OG1 . THR A 1 298 ? -34.129 53.695 15.632 1.00 36.77 ? 275 THR A OG1 1 ATOM 2142 C CG2 . THR A 1 298 ? -33.186 55.025 13.846 1.00 33.22 ? 275 THR A CG2 1 ATOM 2143 N N . PHE A 1 299 ? -32.386 51.074 15.721 1.00 41.12 ? 276 PHE A N 1 ATOM 2144 C CA . PHE A 1 299 ? -32.597 49.998 16.684 1.00 32.44 ? 276 PHE A CA 1 ATOM 2145 C C . PHE A 1 299 ? -33.855 50.207 17.530 1.00 45.94 ? 276 PHE A C 1 ATOM 2146 O O . PHE A 1 299 ? -34.354 49.267 18.145 1.00 44.65 ? 276 PHE A O 1 ATOM 2147 C CB . PHE A 1 299 ? -31.376 49.826 17.591 1.00 37.52 ? 276 PHE A CB 1 ATOM 2148 C CG . PHE A 1 299 ? -30.225 49.108 16.938 1.00 32.95 ? 276 PHE A CG 1 ATOM 2149 C CD1 . PHE A 1 299 ? -30.353 48.572 15.668 1.00 41.79 ? 276 PHE A CD1 1 ATOM 2150 C CD2 . PHE A 1 299 ? -29.020 48.961 17.602 1.00 49.94 ? 276 PHE A CD2 1 ATOM 2151 C CE1 . PHE A 1 299 ? -29.297 47.910 15.069 1.00 50.54 ? 276 PHE A CE1 1 ATOM 2152 C CE2 . PHE A 1 299 ? -27.961 48.295 17.011 1.00 50.48 ? 276 PHE A CE2 1 ATOM 2153 C CZ . PHE A 1 299 ? -28.100 47.769 15.743 1.00 46.58 ? 276 PHE A CZ 1 ATOM 2154 N N . LEU A 1 300 ? -34.369 51.433 17.558 1.00 41.15 ? 277 LEU A N 1 ATOM 2155 C CA . LEU A 1 300 ? -35.560 51.735 18.349 1.00 44.22 ? 277 LEU A CA 1 ATOM 2156 C C . LEU A 1 300 ? -36.852 51.299 17.663 1.00 43.90 ? 277 LEU A C 1 ATOM 2157 O O . LEU A 1 300 ? -37.929 51.365 18.255 1.00 45.60 ? 277 LEU A O 1 ATOM 2158 C CB . LEU A 1 300 ? -35.624 53.223 18.688 1.00 42.25 ? 277 LEU A CB 1 ATOM 2159 C CG . LEU A 1 300 ? -34.477 53.749 19.550 1.00 50.81 ? 277 LEU A CG 1 ATOM 2160 C CD1 . LEU A 1 300 ? -34.715 55.204 19.901 1.00 51.94 ? 277 LEU A CD1 1 ATOM 2161 C CD2 . LEU A 1 300 ? -34.316 52.907 20.806 1.00 48.26 ? 277 LEU A CD2 1 ATOM 2162 N N . ASP A 1 301 ? -36.742 50.852 16.415 1.00 44.60 ? 278 ASP A N 1 ATOM 2163 C CA . ASP A 1 301 ? -37.902 50.358 15.679 1.00 48.57 ? 278 ASP A CA 1 ATOM 2164 C C . ASP A 1 301 ? -38.194 48.900 16.017 1.00 50.99 ? 278 ASP A C 1 ATOM 2165 O O . ASP A 1 301 ? -39.102 48.289 15.455 1.00 53.41 ? 278 ASP A O 1 ATOM 2166 C CB . ASP A 1 301 ? -37.693 50.526 14.175 1.00 47.87 ? 278 ASP A CB 1 ATOM 2167 C CG . ASP A 1 301 ? -37.655 51.977 13.761 1.00 52.21 ? 278 ASP A CG 1 ATOM 2168 O OD1 . ASP A 1 301 ? -38.348 52.790 14.405 1.00 48.88 ? 278 ASP A OD1 1 ATOM 2169 O OD2 . ASP A 1 301 ? -36.929 52.307 12.801 1.00 56.71 ? 278 ASP A OD2 1 ATOM 2170 N N . ILE A 1 302 ? -37.412 48.350 16.940 1.00 49.15 ? 279 ILE A N 1 ATOM 2171 C CA . ILE A 1 302 ? -37.631 46.996 17.424 1.00 61.13 ? 279 ILE A CA 1 ATOM 2172 C C . ILE A 1 302 ? -38.863 46.933 18.326 1.00 67.81 ? 279 ILE A C 1 ATOM 2173 O O . ILE A 1 302 ? -38.852 47.428 19.455 1.00 68.66 ? 279 ILE A O 1 ATOM 2174 C CB . ILE A 1 302 ? -36.397 46.470 18.180 1.00 59.15 ? 279 ILE A CB 1 ATOM 2175 C CG1 . ILE A 1 302 ? -35.218 46.314 17.217 1.00 55.25 ? 279 ILE A CG1 1 ATOM 2176 C CG2 . ILE A 1 302 ? -36.707 45.146 18.855 1.00 70.72 ? 279 ILE A CG2 1 ATOM 2177 C CD1 . ILE A 1 302 ? -33.922 45.908 17.885 1.00 52.42 ? 279 ILE A CD1 1 ATOM 2178 N N . ASN A 1 303 ? -39.932 46.338 17.808 1.00 64.98 ? 280 ASN A N 1 ATOM 2179 C CA . ASN A 1 303 ? -41.157 46.151 18.573 1.00 71.72 ? 280 ASN A CA 1 ATOM 2180 C C . ASN A 1 303 ? -41.324 44.671 18.901 1.00 84.68 ? 280 ASN A C 1 ATOM 2181 O O . ASN A 1 303 ? -41.719 43.877 18.045 1.00 89.81 ? 280 ASN A O 1 ATOM 2182 C CB . ASN A 1 303 ? -42.361 46.672 17.783 1.00 79.00 ? 280 ASN A CB 1 ATOM 2183 C CG . ASN A 1 303 ? -43.602 46.854 18.645 1.00 90.74 ? 280 ASN A CG 1 ATOM 2184 O OD1 . ASN A 1 303 ? -43.735 46.243 19.705 1.00 92.65 ? 280 ASN A OD1 1 ATOM 2185 N ND2 . ASN A 1 303 ? -44.520 47.698 18.185 1.00 94.04 ? 280 ASN A ND2 1 ATOM 2186 N N . LYS A 1 304 ? -41.013 44.303 20.140 1.00 81.23 ? 281 LYS A N 1 ATOM 2187 C CA . LYS A 1 304 ? -41.034 42.902 20.554 1.00 82.78 ? 281 LYS A CA 1 ATOM 2188 C C . LYS A 1 304 ? -42.440 42.307 20.515 1.00 92.73 ? 281 LYS A C 1 ATOM 2189 O O . LYS A 1 304 ? -42.603 41.093 20.389 1.00 89.74 ? 281 LYS A O 1 ATOM 2190 C CB . LYS A 1 304 ? -40.424 42.739 21.950 1.00 79.40 ? 281 LYS A CB 1 ATOM 2191 C CG . LYS A 1 304 ? -41.301 43.235 23.087 1.00 76.62 ? 281 LYS A CG 1 ATOM 2192 C CD . LYS A 1 304 ? -40.585 43.112 24.422 1.00 79.95 ? 281 LYS A CD 1 ATOM 2193 C CE . LYS A 1 304 ? -41.562 43.196 25.581 1.00 83.15 ? 281 LYS A CE 1 ATOM 2194 N NZ . LYS A 1 304 ? -42.516 42.051 25.573 1.00 84.51 ? 281 LYS A NZ 1 ATOM 2195 N N . ASP A 1 305 ? -43.451 43.164 20.618 1.00 109.04 ? 282 ASP A N 1 ATOM 2196 C CA . ASP A 1 305 ? -44.838 42.717 20.564 1.00 117.69 ? 282 ASP A CA 1 ATOM 2197 C C . ASP A 1 305 ? -45.428 42.864 19.163 1.00 121.75 ? 282 ASP A C 1 ATOM 2198 O O . ASP A 1 305 ? -46.403 43.589 18.957 1.00 123.19 ? 282 ASP A O 1 ATOM 2199 C CB . ASP A 1 305 ? -45.691 43.453 21.601 1.00 119.49 ? 282 ASP A CB 1 ATOM 2200 C CG . ASP A 1 305 ? -45.318 43.087 23.027 1.00 116.77 ? 282 ASP A CG 1 ATOM 2201 O OD1 . ASP A 1 305 ? -45.778 42.031 23.511 1.00 121.07 ? 282 ASP A OD1 1 ATOM 2202 O OD2 . ASP A 1 305 ? -44.566 43.854 23.664 1.00 110.52 ? 282 ASP A OD2 1 ATOM 2203 N N . SER A 1 306 ? -44.796 42.181 18.211 1.00 127.25 ? 283 SER A N 1 ATOM 2204 C CA . SER A 1 306 ? -45.292 42.007 16.841 1.00 131.31 ? 283 SER A CA 1 ATOM 2205 C C . SER A 1 306 ? -45.120 43.192 15.889 1.00 133.25 ? 283 SER A C 1 ATOM 2206 O O . SER A 1 306 ? -45.583 44.303 16.147 1.00 132.73 ? 283 SER A O 1 ATOM 2207 C CB . SER A 1 306 ? -46.739 41.496 16.822 1.00 134.79 ? 283 SER A CB 1 ATOM 2208 O OG . SER A 1 306 ? -47.142 41.167 15.505 1.00 135.81 ? 283 SER A OG 1 ATOM 2209 N N . SER A 1 307 ? -44.436 42.914 14.784 1.00 134.17 ? 284 SER A N 1 ATOM 2210 C CA . SER A 1 307 ? -44.313 43.820 13.651 1.00 130.75 ? 284 SER A CA 1 ATOM 2211 C C . SER A 1 307 ? -43.937 42.953 12.459 1.00 137.20 ? 284 SER A C 1 ATOM 2212 O O . SER A 1 307 ? -43.798 43.434 11.334 1.00 135.18 ? 284 SER A O 1 ATOM 2213 C CB . SER A 1 307 ? -43.231 44.871 13.898 1.00 122.25 ? 284 SER A CB 1 ATOM 2214 O OG . SER A 1 307 ? -43.598 45.752 14.944 1.00 119.37 ? 284 SER A OG 1 ATOM 2215 N N . CYS A 1 308 ? -43.782 41.659 12.733 1.00 147.76 ? 285 CYS A N 1 ATOM 2216 C CA . CYS A 1 308 ? -43.314 40.687 11.750 1.00 155.09 ? 285 CYS A CA 1 ATOM 2217 C C . CYS A 1 308 ? -44.265 40.516 10.574 1.00 158.29 ? 285 CYS A C 1 ATOM 2218 O O . CYS A 1 308 ? -45.273 39.817 10.672 1.00 160.87 ? 285 CYS A O 1 ATOM 2219 C CB . CYS A 1 308 ? -43.071 39.324 12.412 1.00 156.85 ? 285 CYS A CB 1 ATOM 2220 S SG . CYS A 1 308 ? -41.478 39.145 13.254 1.00 111.33 ? 285 CYS A SG 1 ATOM 2221 N N . VAL A 1 309 ? -43.933 41.161 9.461 1.00 154.05 ? 286 VAL A N 1 ATOM 2222 C CA . VAL A 1 309 ? -44.643 40.935 8.214 1.00 148.36 ? 286 VAL A CA 1 ATOM 2223 C C . VAL A 1 309 ? -44.054 39.691 7.559 1.00 153.86 ? 286 VAL A C 1 ATOM 2224 O O . VAL A 1 309 ? -42.946 39.732 7.024 1.00 158.01 ? 286 VAL A O 1 ATOM 2225 C CB . VAL A 1 309 ? -44.507 42.136 7.263 1.00 136.18 ? 286 VAL A CB 1 ATOM 2226 C CG1 . VAL A 1 309 ? -45.355 41.925 6.018 1.00 134.71 ? 286 VAL A CG1 1 ATOM 2227 C CG2 . VAL A 1 309 ? -44.904 43.422 7.971 1.00 129.94 ? 286 VAL A CG2 1 ATOM 2228 N N . SER A 1 310 ? -44.793 38.586 7.621 1.00 153.79 ? 287 SER A N 1 ATOM 2229 C CA . SER A 1 310 ? -44.315 37.296 7.126 1.00 151.54 ? 287 SER A CA 1 ATOM 2230 C C . SER A 1 310 ? -43.932 37.333 5.647 1.00 156.18 ? 287 SER A C 1 ATOM 2231 O O . SER A 1 310 ? -42.997 36.653 5.222 1.00 157.61 ? 287 SER A O 1 ATOM 2232 C CB . SER A 1 310 ? -45.359 36.204 7.376 1.00 145.31 ? 287 SER A CB 1 ATOM 2233 O OG . SER A 1 310 ? -45.590 36.025 8.763 1.00 137.48 ? 287 SER A OG 1 ATOM 2234 N N . ALA A 1 311 ? -44.659 38.128 4.868 1.00 155.42 ? 288 ALA A N 1 ATOM 2235 C CA . ALA A 1 311 ? -44.351 38.303 3.453 1.00 149.31 ? 288 ALA A CA 1 ATOM 2236 C C . ALA A 1 311 ? -43.529 39.571 3.245 1.00 139.31 ? 288 ALA A C 1 ATOM 2237 O O . ALA A 1 311 ? -44.081 40.664 3.120 1.00 142.46 ? 288 ALA A O 1 ATOM 2238 C CB . ALA A 1 311 ? -45.630 38.355 2.633 1.00 150.67 ? 288 ALA A CB 1 ATOM 2239 N N . SER A 1 312 ? -42.209 39.421 3.211 1.00 123.63 ? 289 SER A N 1 ATOM 2240 C CA . SER A 1 312 ? -41.320 40.570 3.090 1.00 113.63 ? 289 SER A CA 1 ATOM 2241 C C . SER A 1 312 ? -39.986 40.227 2.434 1.00 96.30 ? 289 SER A C 1 ATOM 2242 O O . SER A 1 312 ? -39.073 39.715 3.083 1.00 78.15 ? 289 SER A O 1 ATOM 2243 C CB . SER A 1 312 ? -41.075 41.198 4.463 1.00 118.46 ? 289 SER A CB 1 ATOM 2244 O OG . SER A 1 312 ? -42.247 41.817 4.961 1.00 119.47 ? 289 SER A OG 1 ATOM 2245 N N . GLY A 1 313 ? -39.878 40.525 1.143 1.00 87.37 ? 290 GLY A N 1 ATOM 2246 C CA . GLY A 1 313 ? -38.633 40.340 0.426 1.00 70.46 ? 290 GLY A CA 1 ATOM 2247 C C . GLY A 1 313 ? -38.779 39.547 -0.856 1.00 71.21 ? 290 GLY A C 1 ATOM 2248 O O . GLY A 1 313 ? -38.976 38.333 -0.826 1.00 70.98 ? 290 GLY A O 1 ATOM 2249 N N . ASN A 1 314 ? -38.692 40.243 -1.985 1.00 72.69 ? 291 ASN A N 1 ATOM 2250 C CA . ASN A 1 314 ? -38.640 39.605 -3.296 1.00 68.09 ? 291 ASN A CA 1 ATOM 2251 C C . ASN A 1 314 ? -37.295 39.904 -3.948 1.00 74.36 ? 291 ASN A C 1 ATOM 2252 O O . ASN A 1 314 ? -37.005 41.054 -4.277 1.00 79.37 ? 291 ASN A O 1 ATOM 2253 C CB . ASN A 1 314 ? -39.776 40.104 -4.188 1.00 69.61 ? 291 ASN A CB 1 ATOM 2254 C CG . ASN A 1 314 ? -41.146 39.738 -3.651 1.00 82.72 ? 291 ASN A CG 1 ATOM 2255 O OD1 . ASN A 1 314 ? -41.316 38.706 -3.001 1.00 93.27 ? 291 ASN A OD1 1 ATOM 2256 N ND2 . ASN A 1 314 ? -42.135 40.583 -3.925 1.00 76.64 ? 291 ASN A ND2 1 ATOM 2257 N N . PHE A 1 315 ? -36.477 38.871 -4.133 1.00 70.32 ? 292 PHE A N 1 ATOM 2258 C CA . PHE A 1 315 ? -35.103 39.065 -4.595 1.00 69.66 ? 292 PHE A CA 1 ATOM 2259 C C . PHE A 1 315 ? -34.809 38.471 -5.972 1.00 79.36 ? 292 PHE A C 1 ATOM 2260 O O . PHE A 1 315 ? -34.726 37.252 -6.132 1.00 73.28 ? 292 PHE A O 1 ATOM 2261 C CB . PHE A 1 315 ? -34.114 38.515 -3.564 1.00 63.15 ? 292 PHE A CB 1 ATOM 2262 C CG . PHE A 1 315 ? -34.289 39.099 -2.195 1.00 68.31 ? 292 PHE A CG 1 ATOM 2263 C CD1 . PHE A 1 315 ? -33.769 40.345 -1.889 1.00 77.35 ? 292 PHE A CD1 1 ATOM 2264 C CD2 . PHE A 1 315 ? -34.983 38.408 -1.216 1.00 70.81 ? 292 PHE A CD2 1 ATOM 2265 C CE1 . PHE A 1 315 ? -33.934 40.890 -0.631 1.00 76.01 ? 292 PHE A CE1 1 ATOM 2266 C CE2 . PHE A 1 315 ? -35.151 38.947 0.044 1.00 74.15 ? 292 PHE A CE2 1 ATOM 2267 C CZ . PHE A 1 315 ? -34.625 40.190 0.336 1.00 78.53 ? 292 PHE A CZ 1 ATOM 2268 N N . ASN A 1 316 ? -34.646 39.346 -6.960 1.00 87.95 ? 293 ASN A N 1 ATOM 2269 C CA . ASN A 1 316 ? -34.198 38.933 -8.283 1.00 96.06 ? 293 ASN A CA 1 ATOM 2270 C C . ASN A 1 316 ? -32.717 38.584 -8.237 1.00 94.23 ? 293 ASN A C 1 ATOM 2271 O O . ASN A 1 316 ? -31.941 39.219 -7.523 1.00 96.00 ? 293 ASN A O 1 ATOM 2272 C CB . ASN A 1 316 ? -34.453 40.033 -9.314 1.00 114.30 ? 293 ASN A CB 1 ATOM 2273 C CG . ASN A 1 316 ? -34.069 39.615 -10.723 1.00 135.17 ? 293 ASN A CG 1 ATOM 2274 O OD1 . ASN A 1 316 ? -33.905 38.428 -11.009 1.00 136.20 ? 293 ASN A OD1 1 ATOM 2275 N ND2 . ASN A 1 316 ? -33.928 40.593 -11.613 1.00 153.12 ? 293 ASN A ND2 1 ATOM 2276 N N . ILE A 1 317 ? -32.327 37.568 -8.998 1.00 98.54 ? 294 ILE A N 1 ATOM 2277 C CA . ILE A 1 317 ? -30.963 37.063 -8.935 1.00 97.09 ? 294 ILE A CA 1 ATOM 2278 C C . ILE A 1 317 ? -30.519 36.444 -10.257 1.00 98.78 ? 294 ILE A C 1 ATOM 2279 O O . ILE A 1 317 ? -29.478 36.808 -10.805 1.00 103.27 ? 294 ILE A O 1 ATOM 2280 C CB . ILE A 1 317 ? -30.813 36.040 -7.792 1.00 89.58 ? 294 ILE A CB 1 ATOM 2281 C CG1 . ILE A 1 317 ? -29.796 34.963 -8.157 1.00 88.85 ? 294 ILE A CG1 1 ATOM 2282 C CG2 . ILE A 1 317 ? -32.150 35.387 -7.470 1.00 81.60 ? 294 ILE A CG2 1 ATOM 2283 C CD1 . ILE A 1 317 ? -29.852 33.777 -7.238 1.00 89.92 ? 294 ILE A CD1 1 ATOM 2284 N N . GLN A 1 331 ? 2.088 41.213 -13.032 1.00 118.11 ? 308 GLN A N 1 ATOM 2285 C CA . GLN A 1 331 ? 1.789 40.848 -11.653 1.00 117.13 ? 308 GLN A CA 1 ATOM 2286 C C . GLN A 1 331 ? 2.086 42.013 -10.710 1.00 113.77 ? 308 GLN A C 1 ATOM 2287 O O . GLN A 1 331 ? 1.241 42.392 -9.897 1.00 120.37 ? 308 GLN A O 1 ATOM 2288 C CB . GLN A 1 331 ? 2.590 39.611 -11.243 1.00 116.82 ? 308 GLN A CB 1 ATOM 2289 C CG . GLN A 1 331 ? 2.122 38.965 -9.951 1.00 117.85 ? 308 GLN A CG 1 ATOM 2290 C CD . GLN A 1 331 ? 2.897 37.706 -9.617 1.00 119.02 ? 308 GLN A CD 1 ATOM 2291 O OE1 . GLN A 1 331 ? 4.025 37.517 -10.074 1.00 116.53 ? 308 GLN A OE1 1 ATOM 2292 N NE2 . GLN A 1 331 ? 2.292 36.832 -8.820 1.00 120.73 ? 308 GLN A NE2 1 ATOM 2293 N N . SER A 1 332 ? 3.289 42.569 -10.814 1.00 98.46 ? 309 SER A N 1 ATOM 2294 C CA . SER A 1 332 ? 3.674 43.764 -10.063 1.00 88.47 ? 309 SER A CA 1 ATOM 2295 C C . SER A 1 332 ? 3.872 43.564 -8.560 1.00 84.65 ? 309 SER A C 1 ATOM 2296 O O . SER A 1 332 ? 3.147 42.807 -7.920 1.00 78.93 ? 309 SER A O 1 ATOM 2297 C CB . SER A 1 332 ? 2.669 44.889 -10.302 1.00 89.28 ? 309 SER A CB 1 ATOM 2298 O OG . SER A 1 332 ? 3.125 46.103 -9.737 1.00 90.64 ? 309 SER A OG 1 ATOM 2299 N N . TYR A 1 333 ? 4.859 44.265 -8.007 1.00 72.01 ? 310 TYR A N 1 ATOM 2300 C CA . TYR A 1 333 ? 5.118 44.232 -6.572 1.00 58.58 ? 310 TYR A CA 1 ATOM 2301 C C . TYR A 1 333 ? 5.162 45.643 -5.998 1.00 63.45 ? 310 TYR A C 1 ATOM 2302 O O . TYR A 1 333 ? 5.421 46.610 -6.715 1.00 60.44 ? 310 TYR A O 1 ATOM 2303 C CB . TYR A 1 333 ? 6.433 43.508 -6.272 1.00 63.22 ? 310 TYR A CB 1 ATOM 2304 C CG . TYR A 1 333 ? 6.352 42.003 -6.389 1.00 63.62 ? 310 TYR A CG 1 ATOM 2305 C CD1 . TYR A 1 333 ? 6.420 41.377 -7.627 1.00 69.47 ? 310 TYR A CD1 1 ATOM 2306 C CD2 . TYR A 1 333 ? 6.215 41.207 -5.258 1.00 63.74 ? 310 TYR A CD2 1 ATOM 2307 C CE1 . TYR A 1 333 ? 6.349 40.000 -7.737 1.00 76.21 ? 310 TYR A CE1 1 ATOM 2308 C CE2 . TYR A 1 333 ? 6.143 39.829 -5.358 1.00 70.67 ? 310 TYR A CE2 1 ATOM 2309 C CZ . TYR A 1 333 ? 6.211 39.232 -6.600 1.00 77.84 ? 310 TYR A CZ 1 ATOM 2310 O OH . TYR A 1 333 ? 6.139 37.863 -6.706 1.00 86.88 ? 310 TYR A OH 1 ATOM 2311 N N . ILE A 1 334 ? 4.941 45.752 -4.701 1.00 69.23 ? 311 ILE A N 1 ATOM 2312 C CA . ILE A 1 334 ? 4.905 47.053 -4.069 1.00 60.14 ? 311 ILE A CA 1 ATOM 2313 C C . ILE A 1 334 ? 5.747 47.058 -2.796 1.00 51.84 ? 311 ILE A C 1 ATOM 2314 O O . ILE A 1 334 ? 5.970 46.020 -2.192 1.00 50.85 ? 311 ILE A O 1 ATOM 2315 C CB . ILE A 1 334 ? 3.437 47.511 -3.873 1.00 71.55 ? 311 ILE A CB 1 ATOM 2316 C CG1 . ILE A 1 334 ? 3.258 48.930 -4.391 1.00 72.67 ? 311 ILE A CG1 1 ATOM 2317 C CG2 . ILE A 1 334 ? 2.934 47.348 -2.441 1.00 64.97 ? 311 ILE A CG2 1 ATOM 2318 C CD1 . ILE A 1 334 ? 2.485 48.986 -5.684 1.00 68.88 ? 311 ILE A CD1 1 ATOM 2319 N N . SER A 1 335 ? 6.221 48.231 -2.407 1.00 50.87 ? 312 SER A N 1 ATOM 2320 C CA . SER A 1 335 ? 7.077 48.346 -1.228 1.00 60.45 ? 312 SER A CA 1 ATOM 2321 C C . SER A 1 335 ? 6.587 49.408 -0.248 1.00 61.95 ? 312 SER A C 1 ATOM 2322 O O . SER A 1 335 ? 6.104 50.467 -0.652 1.00 51.88 ? 312 SER A O 1 ATOM 2323 C CB . SER A 1 335 ? 8.526 48.632 -1.631 1.00 69.53 ? 312 SER A CB 1 ATOM 2324 O OG . SER A 1 335 ? 9.143 47.473 -2.163 1.00 76.29 ? 312 SER A OG 1 ATOM 2325 N N . VAL A 1 336 ? 6.721 49.115 1.044 1.00 56.37 ? 313 VAL A N 1 ATOM 2326 C CA . VAL A 1 336 ? 6.257 50.017 2.094 1.00 55.12 ? 313 VAL A CA 1 ATOM 2327 C C . VAL A 1 336 ? 7.247 50.107 3.254 1.00 51.33 ? 313 VAL A C 1 ATOM 2328 O O . VAL A 1 336 ? 8.130 49.263 3.400 1.00 51.36 ? 313 VAL A O 1 ATOM 2329 C CB . VAL A 1 336 ? 4.901 49.558 2.668 1.00 54.70 ? 313 VAL A CB 1 ATOM 2330 C CG1 . VAL A 1 336 ? 3.798 49.696 1.629 1.00 48.73 ? 313 VAL A CG1 1 ATOM 2331 C CG2 . VAL A 1 336 ? 5.001 48.124 3.168 1.00 46.50 ? 313 VAL A CG2 1 ATOM 2332 N N . ASN A 1 337 ? 7.083 51.133 4.080 1.00 59.70 ? 314 ASN A N 1 ATOM 2333 C CA . ASN A 1 337 ? 7.876 51.281 5.294 1.00 63.87 ? 314 ASN A CA 1 ATOM 2334 C C . ASN A 1 337 ? 7.115 50.738 6.503 1.00 68.10 ? 314 ASN A C 1 ATOM 2335 O O . ASN A 1 337 ? 6.381 51.469 7.168 1.00 77.08 ? 314 ASN A O 1 ATOM 2336 C CB . ASN A 1 337 ? 8.250 52.751 5.511 1.00 75.33 ? 314 ASN A CB 1 ATOM 2337 C CG . ASN A 1 337 ? 9.069 52.972 6.772 1.00 90.60 ? 314 ASN A CG 1 ATOM 2338 O OD1 . ASN A 1 337 ? 9.828 52.100 7.198 1.00 92.71 ? 314 ASN A OD1 1 ATOM 2339 N ND2 . ASN A 1 337 ? 8.908 54.145 7.381 1.00 99.00 ? 314 ASN A ND2 1 ATOM 2340 N N . TYR A 1 338 ? 7.292 49.449 6.778 1.00 57.03 ? 315 TYR A N 1 ATOM 2341 C CA . TYR A 1 338 ? 6.607 48.795 7.889 1.00 59.65 ? 315 TYR A CA 1 ATOM 2342 C C . TYR A 1 338 ? 7.370 48.939 9.199 1.00 63.99 ? 315 TYR A C 1 ATOM 2343 O O . TYR A 1 338 ? 8.532 48.544 9.300 1.00 63.12 ? 315 TYR A O 1 ATOM 2344 C CB . TYR A 1 338 ? 6.389 47.314 7.583 1.00 59.43 ? 315 TYR A CB 1 ATOM 2345 C CG . TYR A 1 338 ? 5.726 46.539 8.700 1.00 59.45 ? 315 TYR A CG 1 ATOM 2346 C CD1 . TYR A 1 338 ? 4.388 46.742 9.013 1.00 58.38 ? 315 TYR A CD1 1 ATOM 2347 C CD2 . TYR A 1 338 ? 6.434 45.593 9.432 1.00 54.65 ? 315 TYR A CD2 1 ATOM 2348 C CE1 . TYR A 1 338 ? 3.775 46.032 10.026 1.00 58.28 ? 315 TYR A CE1 1 ATOM 2349 C CE2 . TYR A 1 338 ? 5.829 44.878 10.448 1.00 61.85 ? 315 TYR A CE2 1 ATOM 2350 C CZ . TYR A 1 338 ? 4.498 45.101 10.740 1.00 60.89 ? 315 TYR A CZ 1 ATOM 2351 O OH . TYR A 1 338 ? 3.887 44.392 11.748 1.00 47.06 ? 315 TYR A OH 1 ATOM 2352 N N . SER A 1 339 ? 6.706 49.496 10.205 1.00 57.79 ? 316 SER A N 1 ATOM 2353 C CA . SER A 1 339 ? 7.337 49.699 11.501 1.00 60.58 ? 316 SER A CA 1 ATOM 2354 C C . SER A 1 339 ? 6.471 49.195 12.651 1.00 64.00 ? 316 SER A C 1 ATOM 2355 O O . SER A 1 339 ? 5.242 49.238 12.586 1.00 64.62 ? 316 SER A O 1 ATOM 2356 C CB . SER A 1 339 ? 7.686 51.176 11.705 1.00 52.22 ? 316 SER A CB 1 ATOM 2357 O OG . SER A 1 339 ? 6.522 51.981 11.719 1.00 64.86 ? 316 SER A OG 1 ATOM 2358 N N . VAL A 1 340 ? 7.127 48.707 13.698 1.00 53.65 ? 317 VAL A N 1 ATOM 2359 C CA . VAL A 1 340 ? 6.443 48.304 14.919 1.00 45.63 ? 317 VAL A CA 1 ATOM 2360 C C . VAL A 1 340 ? 6.922 49.175 16.071 1.00 47.83 ? 317 VAL A C 1 ATOM 2361 O O . VAL A 1 340 ? 8.071 49.069 16.500 1.00 55.08 ? 317 VAL A O 1 ATOM 2362 C CB . VAL A 1 340 ? 6.709 46.828 15.262 1.00 50.72 ? 317 VAL A CB 1 ATOM 2363 C CG1 . VAL A 1 340 ? 6.112 46.484 16.620 1.00 48.63 ? 317 VAL A CG1 1 ATOM 2364 C CG2 . VAL A 1 340 ? 6.147 45.917 14.177 1.00 50.02 ? 317 VAL A CG2 1 ATOM 2365 N N . ARG A 1 341 ? 6.044 50.045 16.561 1.00 47.81 ? 318 ARG A N 1 ATOM 2366 C CA . ARG A 1 341 ? 6.400 50.962 17.639 1.00 49.06 ? 318 ARG A CA 1 ATOM 2367 C C . ARG A 1 341 ? 5.825 50.538 18.990 1.00 56.53 ? 318 ARG A C 1 ATOM 2368 O O . ARG A 1 341 ? 4.618 50.346 19.136 1.00 65.68 ? 318 ARG A O 1 ATOM 2369 C CB . ARG A 1 341 ? 5.970 52.393 17.301 1.00 45.40 ? 318 ARG A CB 1 ATOM 2370 C CG . ARG A 1 341 ? 5.968 53.342 18.494 1.00 50.03 ? 318 ARG A CG 1 ATOM 2371 C CD . ARG A 1 341 ? 5.768 54.793 18.071 1.00 42.14 ? 318 ARG A CD 1 ATOM 2372 N NE . ARG A 1 341 ? 7.014 55.397 17.604 1.00 76.31 ? 318 ARG A NE 1 ATOM 2373 C CZ . ARG A 1 341 ? 7.307 55.623 16.327 1.00 83.93 ? 318 ARG A CZ 1 ATOM 2374 N NH1 . ARG A 1 341 ? 6.437 55.308 15.378 1.00 84.31 ? 318 ARG A NH1 1 ATOM 2375 N NH2 . ARG A 1 341 ? 8.469 56.172 16.001 1.00 87.44 ? 318 ARG A NH2 1 ATOM 2376 N N . ILE A 1 342 ? 6.712 50.390 19.968 1.00 50.69 ? 319 ILE A N 1 ATOM 2377 C CA . ILE A 1 342 ? 6.328 50.117 21.347 1.00 47.00 ? 319 ILE A CA 1 ATOM 2378 C C . ILE A 1 342 ? 6.805 51.297 22.186 1.00 45.66 ? 319 ILE A C 1 ATOM 2379 O O . ILE A 1 342 ? 6.043 52.221 22.473 1.00 51.51 ? 319 ILE A O 1 ATOM 2380 C CB . ILE A 1 342 ? 6.967 48.810 21.842 1.00 44.06 ? 319 ILE A CB 1 ATOM 2381 C CG1 . ILE A 1 342 ? 6.695 47.689 20.836 1.00 46.07 ? 319 ILE A CG1 1 ATOM 2382 C CG2 . ILE A 1 342 ? 6.452 48.443 23.227 1.00 40.87 ? 319 ILE A CG2 1 ATOM 2383 C CD1 . ILE A 1 342 ? 7.191 46.333 21.268 1.00 49.17 ? 319 ILE A CD1 1 ATOM 2384 N N . ASN A 1 343 ? 8.074 51.258 22.572 1.00 55.69 ? 320 ASN A N 1 ATOM 2385 C CA . ASN A 1 343 ? 8.774 52.444 23.042 1.00 53.66 ? 320 ASN A CA 1 ATOM 2386 C C . ASN A 1 343 ? 9.785 52.790 21.969 1.00 49.16 ? 320 ASN A C 1 ATOM 2387 O O . ASN A 1 343 ? 9.746 53.865 21.368 1.00 44.81 ? 320 ASN A O 1 ATOM 2388 C CB . ASN A 1 343 ? 9.478 52.170 24.367 1.00 57.35 ? 320 ASN A CB 1 ATOM 2389 C CG . ASN A 1 343 ? 8.559 52.332 25.556 1.00 69.02 ? 320 ASN A CG 1 ATOM 2390 O OD1 . ASN A 1 343 ? 7.844 53.331 25.669 1.00 64.55 ? 320 ASN A OD1 1 ATOM 2391 N ND2 . ASN A 1 343 ? 8.561 51.347 26.448 1.00 73.83 ? 320 ASN A ND2 1 ATOM 2392 N N . GLU A 1 344 ? 10.683 51.844 21.727 1.00 57.33 ? 321 GLU A N 1 ATOM 2393 C CA . GLU A 1 344 ? 11.580 51.890 20.590 1.00 52.71 ? 321 GLU A CA 1 ATOM 2394 C C . GLU A 1 344 ? 10.781 51.521 19.348 1.00 56.67 ? 321 GLU A C 1 ATOM 2395 O O . GLU A 1 344 ? 9.633 51.086 19.447 1.00 50.89 ? 321 GLU A O 1 ATOM 2396 C CB . GLU A 1 344 ? 12.705 50.875 20.784 1.00 51.33 ? 321 GLU A CB 1 ATOM 2397 C CG . GLU A 1 344 ? 12.271 49.418 20.599 1.00 45.55 ? 321 GLU A CG 1 ATOM 2398 C CD . GLU A 1 344 ? 11.483 48.852 21.779 1.00 47.67 ? 321 GLU A CD 1 ATOM 2399 O OE1 . GLU A 1 344 ? 11.051 49.628 22.660 1.00 42.40 ? 321 GLU A OE1 1 ATOM 2400 O OE2 . GLU A 1 344 ? 11.305 47.617 21.832 1.00 47.26 ? 321 GLU A OE2 1 ATOM 2401 N N . THR A 1 345 ? 11.393 51.677 18.180 1.00 58.15 ? 322 THR A N 1 ATOM 2402 C CA . THR A 1 345 ? 10.727 51.340 16.929 1.00 52.55 ? 322 THR A CA 1 ATOM 2403 C C . THR A 1 345 ? 11.597 50.436 16.059 1.00 55.50 ? 322 THR A C 1 ATOM 2404 O O . THR A 1 345 ? 12.774 50.718 15.836 1.00 55.93 ? 322 THR A O 1 ATOM 2405 C CB . THR A 1 345 ? 10.346 52.606 16.137 1.00 53.92 ? 322 THR A CB 1 ATOM 2406 O OG1 . THR A 1 345 ? 9.564 53.475 16.967 1.00 53.90 ? 322 THR A OG1 1 ATOM 2407 C CG2 . THR A 1 345 ? 9.544 52.240 14.899 1.00 56.39 ? 322 THR A CG2 1 ATOM 2408 N N . TYR A 1 346 ? 11.009 49.342 15.585 1.00 56.63 ? 323 TYR A N 1 ATOM 2409 C CA . TYR A 1 346 ? 11.675 48.452 14.642 1.00 58.28 ? 323 TYR A CA 1 ATOM 2410 C C . TYR A 1 346 ? 11.039 48.639 13.270 1.00 62.16 ? 323 TYR A C 1 ATOM 2411 O O . TYR A 1 346 ? 9.815 48.659 13.154 1.00 62.25 ? 323 TYR A O 1 ATOM 2412 C CB . TYR A 1 346 ? 11.532 46.994 15.083 1.00 50.37 ? 323 TYR A CB 1 ATOM 2413 C CG . TYR A 1 346 ? 11.884 46.734 16.533 1.00 53.35 ? 323 TYR A CG 1 ATOM 2414 C CD1 . TYR A 1 346 ? 10.921 46.841 17.530 1.00 43.06 ? 323 TYR A CD1 1 ATOM 2415 C CD2 . TYR A 1 346 ? 13.175 46.372 16.906 1.00 53.84 ? 323 TYR A CD2 1 ATOM 2416 C CE1 . TYR A 1 346 ? 11.230 46.601 18.854 1.00 47.50 ? 323 TYR A CE1 1 ATOM 2417 C CE2 . TYR A 1 346 ? 13.496 46.131 18.234 1.00 53.48 ? 323 TYR A CE2 1 ATOM 2418 C CZ . TYR A 1 346 ? 12.517 46.248 19.204 1.00 56.38 ? 323 TYR A CZ 1 ATOM 2419 O OH . TYR A 1 346 ? 12.817 46.013 20.527 1.00 51.34 ? 323 TYR A OH 1 ATOM 2420 N N . PHE A 1 347 ? 11.860 48.777 12.234 1.00 65.59 ? 324 PHE A N 1 ATOM 2421 C CA . PHE A 1 347 ? 11.335 49.013 10.891 1.00 62.06 ? 324 PHE A CA 1 ATOM 2422 C C . PHE A 1 347 ? 12.125 48.306 9.792 1.00 67.40 ? 324 PHE A C 1 ATOM 2423 O O . PHE A 1 347 ? 13.331 48.094 9.912 1.00 77.76 ? 324 PHE A O 1 ATOM 2424 C CB . PHE A 1 347 ? 11.260 50.513 10.596 1.00 60.78 ? 324 PHE A CB 1 ATOM 2425 C CG . PHE A 1 347 ? 12.599 51.188 10.544 1.00 73.83 ? 324 PHE A CG 1 ATOM 2426 C CD1 . PHE A 1 347 ? 13.208 51.640 11.703 1.00 82.20 ? 324 PHE A CD1 1 ATOM 2427 C CD2 . PHE A 1 347 ? 13.249 51.375 9.335 1.00 76.63 ? 324 PHE A CD2 1 ATOM 2428 C CE1 . PHE A 1 347 ? 14.441 52.261 11.659 1.00 82.93 ? 324 PHE A CE1 1 ATOM 2429 C CE2 . PHE A 1 347 ? 14.482 51.995 9.283 1.00 79.53 ? 324 PHE A CE2 1 ATOM 2430 C CZ . PHE A 1 347 ? 15.078 52.440 10.447 1.00 83.21 ? 324 PHE A CZ 1 ATOM 2431 N N . THR A 1 348 ? 11.421 47.946 8.723 1.00 64.82 ? 325 THR A N 1 ATOM 2432 C CA . THR A 1 348 ? 12.025 47.362 7.532 1.00 69.14 ? 325 THR A CA 1 ATOM 2433 C C . THR A 1 348 ? 11.272 47.857 6.309 1.00 72.48 ? 325 THR A C 1 ATOM 2434 O O . THR A 1 348 ? 10.215 48.476 6.431 1.00 78.72 ? 325 THR A O 1 ATOM 2435 C CB . THR A 1 348 ? 11.948 45.818 7.533 1.00 72.82 ? 325 THR A CB 1 ATOM 2436 O OG1 . THR A 1 348 ? 10.641 45.399 7.948 1.00 82.25 ? 325 THR A OG1 1 ATOM 2437 C CG2 . THR A 1 348 ? 12.982 45.220 8.464 1.00 74.92 ? 325 THR A CG2 1 ATOM 2438 N N . ASN A 1 349 ? 11.806 47.570 5.139 1.00 65.77 ? 326 ASN A N 1 ATOM 2439 C CA . ASN A 1 349 ? 11.063 47.787 3.929 1.00 60.72 ? 326 ASN A CA 1 ATOM 2440 C C . ASN A 1 349 ? 10.637 46.421 3.447 1.00 67.57 ? 326 ASN A C 1 ATOM 2441 O O . ASN A 1 349 ? 11.464 45.558 3.204 1.00 75.91 ? 326 ASN A O 1 ATOM 2442 C CB . ASN A 1 349 ? 11.893 48.534 2.889 1.00 58.94 ? 326 ASN A CB 1 ATOM 2443 C CG . ASN A 1 349 ? 13.180 47.819 2.533 1.00 71.16 ? 326 ASN A CG 1 ATOM 2444 O OD1 . ASN A 1 349 ? 13.909 47.346 3.398 1.00 57.83 ? 326 ASN A OD1 1 ATOM 2445 N ND2 . ASN A 1 349 ? 13.464 47.746 1.245 1.00 85.76 ? 326 ASN A ND2 1 ATOM 2446 N N . VAL A 1 350 ? 9.336 46.206 3.360 1.00 71.28 ? 327 VAL A N 1 ATOM 2447 C CA . VAL A 1 350 ? 8.821 44.930 2.878 1.00 69.44 ? 327 VAL A CA 1 ATOM 2448 C C . VAL A 1 350 ? 8.285 45.064 1.458 1.00 59.80 ? 327 VAL A C 1 ATOM 2449 O O . VAL A 1 350 ? 7.823 46.132 1.051 1.00 58.86 ? 327 VAL A O 1 ATOM 2450 C CB . VAL A 1 350 ? 7.731 44.347 3.810 1.00 68.08 ? 327 VAL A CB 1 ATOM 2451 C CG1 . VAL A 1 350 ? 7.958 44.804 5.243 1.00 63.65 ? 327 VAL A CG1 1 ATOM 2452 C CG2 . VAL A 1 350 ? 6.344 44.745 3.340 1.00 74.78 ? 327 VAL A CG2 1 ATOM 2453 N N . THR A 1 351 ? 8.359 43.983 0.704 1.00 67.31 ? 328 THR A N 1 ATOM 2454 C CA . THR A 1 351 ? 7.845 43.991 -0.648 1.00 71.94 ? 328 THR A CA 1 ATOM 2455 C C . THR A 1 351 ? 6.785 42.912 -0.791 1.00 68.94 ? 328 THR A C 1 ATOM 2456 O O . THR A 1 351 ? 7.031 41.745 -0.518 1.00 68.40 ? 328 THR A O 1 ATOM 2457 C CB . THR A 1 351 ? 8.967 43.801 -1.680 1.00 65.02 ? 328 THR A CB 1 ATOM 2458 O OG1 . THR A 1 351 ? 9.949 44.821 -1.497 1.00 69.38 ? 328 THR A OG1 1 ATOM 2459 C CG2 . THR A 1 351 ? 8.418 43.904 -3.081 1.00 65.26 ? 328 THR A CG2 1 ATOM 2460 N N . VAL A 1 352 ? 5.599 43.326 -1.209 1.00 66.35 ? 329 VAL A N 1 ATOM 2461 C CA . VAL A 1 352 ? 4.467 42.421 -1.371 1.00 68.74 ? 329 VAL A CA 1 ATOM 2462 C C . VAL A 1 352 ? 3.818 42.583 -2.741 1.00 70.75 ? 329 VAL A C 1 ATOM 2463 O O . VAL A 1 352 ? 4.015 43.595 -3.416 1.00 65.40 ? 329 VAL A O 1 ATOM 2464 C CB . VAL A 1 352 ? 3.397 42.660 -0.284 1.00 56.97 ? 329 VAL A CB 1 ATOM 2465 C CG1 . VAL A 1 352 ? 3.906 42.212 1.078 1.00 57.41 ? 329 VAL A CG1 1 ATOM 2466 C CG2 . VAL A 1 352 ? 2.990 44.127 -0.254 1.00 54.39 ? 329 VAL A CG2 1 ATOM 2467 N N . LEU A 1 353 ? 3.055 41.576 -3.150 1.00 77.13 ? 330 LEU A N 1 ATOM 2468 C CA . LEU A 1 353 ? 2.310 41.643 -4.397 1.00 81.07 ? 330 LEU A CA 1 ATOM 2469 C C . LEU A 1 353 ? 1.316 42.783 -4.326 1.00 74.27 ? 330 LEU A C 1 ATOM 2470 O O . LEU A 1 353 ? 0.752 43.051 -3.275 1.00 84.47 ? 330 LEU A O 1 ATOM 2471 C CB . LEU A 1 353 ? 1.568 40.333 -4.653 1.00 85.04 ? 330 LEU A CB 1 ATOM 2472 C CG . LEU A 1 353 ? 2.431 39.078 -4.768 1.00 94.03 ? 330 LEU A CG 1 ATOM 2473 C CD1 . LEU A 1 353 ? 1.636 37.831 -4.425 1.00 97.74 ? 330 LEU A CD1 1 ATOM 2474 C CD2 . LEU A 1 353 ? 3.026 38.966 -6.160 1.00 94.67 ? 330 LEU A CD2 1 ATOM 2475 N N . ASN A 1 354 ? 1.083 43.436 -5.453 1.00 104.80 ? 331 ASN A N 1 ATOM 2476 C CA . ASN A 1 354 ? 0.160 44.552 -5.503 1.00 97.73 ? 331 ASN A CA 1 ATOM 2477 C C . ASN A 1 354 ? -1.217 44.053 -5.110 1.00 87.65 ? 331 ASN A C 1 ATOM 2478 O O . ASN A 1 354 ? -1.607 42.953 -5.475 1.00 88.83 ? 331 ASN A O 1 ATOM 2479 C CB . ASN A 1 354 ? 0.125 45.109 -6.921 1.00 100.75 ? 331 ASN A CB 1 ATOM 2480 C CG . ASN A 1 354 ? -0.405 46.525 -6.993 1.00 103.44 ? 331 ASN A CG 1 ATOM 2481 O OD1 . ASN A 1 354 ? -0.371 47.276 -6.024 1.00 83.96 ? 331 ASN A OD1 1 ATOM 2482 N ND2 . ASN A 1 354 ? -0.897 46.892 -8.163 1.00 131.90 ? 331 ASN A ND2 1 ATOM 2483 N N . GLY A 1 355 ? -1.948 44.860 -4.354 1.00 78.72 ? 332 GLY A N 1 ATOM 2484 C CA . GLY A 1 355 ? -3.248 44.450 -3.866 1.00 72.73 ? 332 GLY A CA 1 ATOM 2485 C C . GLY A 1 355 ? -3.193 43.596 -2.617 1.00 66.02 ? 332 GLY A C 1 ATOM 2486 O O . GLY A 1 355 ? -4.194 43.024 -2.207 1.00 57.10 ? 332 GLY A O 1 ATOM 2487 N N . SER A 1 356 ? -2.015 43.500 -2.016 1.00 63.51 ? 333 SER A N 1 ATOM 2488 C CA . SER A 1 356 ? -1.862 42.771 -0.769 1.00 58.43 ? 333 SER A CA 1 ATOM 2489 C C . SER A 1 356 ? -2.471 43.580 0.362 1.00 57.82 ? 333 SER A C 1 ATOM 2490 O O . SER A 1 356 ? -2.589 44.794 0.268 1.00 48.95 ? 333 SER A O 1 ATOM 2491 C CB . SER A 1 356 ? -0.387 42.506 -0.485 1.00 62.00 ? 333 SER A CB 1 ATOM 2492 O OG . SER A 1 356 ? 0.070 41.358 -1.167 1.00 64.61 ? 333 SER A OG 1 ATOM 2493 N N . VAL A 1 357 ? -2.862 42.909 1.433 1.00 56.21 ? 334 VAL A N 1 ATOM 2494 C CA . VAL A 1 357 ? -3.421 43.619 2.573 1.00 53.41 ? 334 VAL A CA 1 ATOM 2495 C C . VAL A 1 357 ? -2.367 43.881 3.642 1.00 54.82 ? 334 VAL A C 1 ATOM 2496 O O . VAL A 1 357 ? -1.260 43.345 3.583 1.00 54.37 ? 334 VAL A O 1 ATOM 2497 C CB . VAL A 1 357 ? -4.622 42.871 3.191 1.00 48.90 ? 334 VAL A CB 1 ATOM 2498 C CG1 . VAL A 1 357 ? -5.762 42.785 2.187 1.00 43.37 ? 334 VAL A CG1 1 ATOM 2499 C CG2 . VAL A 1 357 ? -4.209 41.484 3.668 1.00 38.85 ? 334 VAL A CG2 1 ATOM 2500 N N . PHE A 1 358 ? -2.729 44.718 4.609 1.00 54.43 ? 335 PHE A N 1 ATOM 2501 C CA . PHE A 1 358 ? -1.855 45.082 5.716 1.00 49.40 ? 335 PHE A CA 1 ATOM 2502 C C . PHE A 1 358 ? -1.323 43.841 6.440 1.00 54.81 ? 335 PHE A C 1 ATOM 2503 O O . PHE A 1 358 ? -0.177 43.820 6.886 1.00 51.41 ? 335 PHE A O 1 ATOM 2504 C CB . PHE A 1 358 ? -2.626 45.984 6.687 1.00 45.83 ? 335 PHE A CB 1 ATOM 2505 C CG . PHE A 1 358 ? -1.763 46.688 7.700 1.00 41.41 ? 335 PHE A CG 1 ATOM 2506 C CD1 . PHE A 1 358 ? -1.281 46.017 8.812 1.00 41.04 ? 335 PHE A CD1 1 ATOM 2507 C CD2 . PHE A 1 358 ? -1.467 48.034 7.559 1.00 46.05 ? 335 PHE A CD2 1 ATOM 2508 C CE1 . PHE A 1 358 ? -0.500 46.666 9.749 1.00 44.55 ? 335 PHE A CE1 1 ATOM 2509 C CE2 . PHE A 1 358 ? -0.687 48.690 8.496 1.00 48.87 ? 335 PHE A CE2 1 ATOM 2510 C CZ . PHE A 1 358 ? -0.206 48.004 9.593 1.00 48.28 ? 335 PHE A CZ 1 ATOM 2511 N N . LEU A 1 359 ? -2.158 42.811 6.547 1.00 50.01 ? 336 LEU A N 1 ATOM 2512 C CA . LEU A 1 359 ? -1.771 41.573 7.221 1.00 52.46 ? 336 LEU A CA 1 ATOM 2513 C C . LEU A 1 359 ? -0.645 40.847 6.484 1.00 59.22 ? 336 LEU A C 1 ATOM 2514 O O . LEU A 1 359 ? 0.234 40.252 7.108 1.00 55.53 ? 336 LEU A O 1 ATOM 2515 C CB . LEU A 1 359 ? -2.976 40.644 7.375 1.00 45.72 ? 336 LEU A CB 1 ATOM 2516 C CG . LEU A 1 359 ? -2.752 39.341 8.146 1.00 46.94 ? 336 LEU A CG 1 ATOM 2517 C CD1 . LEU A 1 359 ? -2.310 39.633 9.569 1.00 42.80 ? 336 LEU A CD1 1 ATOM 2518 C CD2 . LEU A 1 359 ? -4.015 38.490 8.139 1.00 49.94 ? 336 LEU A CD2 1 ATOM 2519 N N . SER A 1 360 ? -0.681 40.894 5.156 1.00 52.54 ? 337 SER A N 1 ATOM 2520 C CA . SER A 1 360 ? 0.344 40.253 4.342 1.00 55.37 ? 337 SER A CA 1 ATOM 2521 C C . SER A 1 360 ? 1.711 40.876 4.614 1.00 56.62 ? 337 SER A C 1 ATOM 2522 O O . SER A 1 360 ? 2.727 40.180 4.646 1.00 50.19 ? 337 SER A O 1 ATOM 2523 C CB . SER A 1 360 ? -0.006 40.355 2.855 1.00 54.11 ? 337 SER A CB 1 ATOM 2524 O OG . SER A 1 360 ? -1.245 39.723 2.581 1.00 60.51 ? 337 SER A OG 1 ATOM 2525 N N . VAL A 1 361 ? 1.723 42.190 4.815 1.00 55.53 ? 338 VAL A N 1 ATOM 2526 C CA . VAL A 1 361 ? 2.942 42.910 5.161 1.00 55.41 ? 338 VAL A CA 1 ATOM 2527 C C . VAL A 1 361 ? 3.504 42.394 6.479 1.00 62.90 ? 338 VAL A C 1 ATOM 2528 O O . VAL A 1 361 ? 4.701 42.118 6.591 1.00 63.87 ? 338 VAL A O 1 ATOM 2529 C CB . VAL A 1 361 ? 2.683 44.428 5.267 1.00 55.07 ? 338 VAL A CB 1 ATOM 2530 C CG1 . VAL A 1 361 ? 3.876 45.139 5.890 1.00 51.85 ? 338 VAL A CG1 1 ATOM 2531 C CG2 . VAL A 1 361 ? 2.361 45.008 3.897 1.00 59.55 ? 338 VAL A CG2 1 ATOM 2532 N N . MET A 1 362 ? 2.628 42.255 7.469 1.00 65.33 ? 339 MET A N 1 ATOM 2533 C CA . MET A 1 362 ? 3.020 41.769 8.789 1.00 56.73 ? 339 MET A CA 1 ATOM 2534 C C . MET A 1 362 ? 3.615 40.367 8.712 1.00 50.65 ? 339 MET A C 1 ATOM 2535 O O . MET A 1 362 ? 4.607 40.068 9.375 1.00 53.08 ? 339 MET A O 1 ATOM 2536 C CB . MET A 1 362 ? 1.820 41.777 9.740 1.00 49.54 ? 339 MET A CB 1 ATOM 2537 C CG . MET A 1 362 ? 1.224 43.156 9.981 1.00 53.11 ? 339 MET A CG 1 ATOM 2538 S SD . MET A 1 362 ? -0.140 43.133 11.161 1.00 49.62 ? 339 MET A SD 1 ATOM 2539 C CE . MET A 1 362 ? 0.679 42.461 12.607 1.00 47.51 ? 339 MET A CE 1 ATOM 2540 N N . GLU A 1 363 ? 3.004 39.516 7.894 1.00 56.84 ? 340 GLU A N 1 ATOM 2541 C CA . GLU A 1 363 ? 3.443 38.132 7.754 1.00 65.49 ? 340 GLU A CA 1 ATOM 2542 C C . GLU A 1 363 ? 4.805 38.016 7.071 1.00 66.17 ? 340 GLU A C 1 ATOM 2543 O O . GLU A 1 363 ? 5.605 37.145 7.415 1.00 61.62 ? 340 GLU A O 1 ATOM 2544 C CB . GLU A 1 363 ? 2.392 37.309 7.007 1.00 66.11 ? 340 GLU A CB 1 ATOM 2545 C CG . GLU A 1 363 ? 1.102 37.119 7.791 1.00 73.65 ? 340 GLU A CG 1 ATOM 2546 C CD . GLU A 1 363 ? 0.056 36.340 7.019 1.00 79.53 ? 340 GLU A CD 1 ATOM 2547 O OE1 . GLU A 1 363 ? 0.195 36.219 5.785 1.00 80.75 ? 340 GLU A OE1 1 ATOM 2548 O OE2 . GLU A 1 363 ? -0.904 35.847 7.649 1.00 84.91 ? 340 GLU A OE2 1 ATOM 2549 N N . LYS A 1 364 ? 5.065 38.891 6.104 1.00 70.47 ? 341 LYS A N 1 ATOM 2550 C CA . LYS A 1 364 ? 6.366 38.921 5.445 1.00 77.12 ? 341 LYS A CA 1 ATOM 2551 C C . LYS A 1 364 ? 7.453 39.359 6.417 1.00 73.12 ? 341 LYS A C 1 ATOM 2552 O O . LYS A 1 364 ? 8.548 38.798 6.430 1.00 69.57 ? 341 LYS A O 1 ATOM 2553 C CB . LYS A 1 364 ? 6.347 39.844 4.224 1.00 84.73 ? 341 LYS A CB 1 ATOM 2554 C CG . LYS A 1 364 ? 6.093 39.125 2.910 1.00 95.09 ? 341 LYS A CG 1 ATOM 2555 C CD . LYS A 1 364 ? 7.141 38.047 2.663 1.00 106.39 ? 341 LYS A CD 1 ATOM 2556 C CE . LYS A 1 364 ? 8.541 38.639 2.572 1.00 107.96 ? 341 LYS A CE 1 ATOM 2557 N NZ . LYS A 1 364 ? 9.589 37.585 2.473 1.00 105.61 ? 341 LYS A NZ 1 ATOM 2558 N N . ALA A 1 365 ? 7.141 40.361 7.232 1.00 62.30 ? 342 ALA A N 1 ATOM 2559 C CA . ALA A 1 365 ? 8.082 40.850 8.229 1.00 58.62 ? 342 ALA A CA 1 ATOM 2560 C C . ALA A 1 365 ? 8.351 39.781 9.285 1.00 63.64 ? 342 ALA A C 1 ATOM 2561 O O . ALA A 1 365 ? 9.471 39.659 9.784 1.00 53.65 ? 342 ALA A O 1 ATOM 2562 C CB . ALA A 1 365 ? 7.561 42.125 8.873 1.00 48.39 ? 342 ALA A CB 1 ATOM 2563 N N . GLN A 1 366 ? 7.321 39.007 9.617 1.00 57.15 ? 343 GLN A N 1 ATOM 2564 C CA . GLN A 1 366 ? 7.460 37.928 10.591 1.00 60.31 ? 343 GLN A CA 1 ATOM 2565 C C . GLN A 1 366 ? 8.435 36.868 10.086 1.00 62.44 ? 343 GLN A C 1 ATOM 2566 O O . GLN A 1 366 ? 9.205 36.301 10.860 1.00 57.93 ? 343 GLN A O 1 ATOM 2567 C CB . GLN A 1 366 ? 6.100 37.294 10.900 1.00 52.24 ? 343 GLN A CB 1 ATOM 2568 C CG . GLN A 1 366 ? 6.149 36.213 11.972 1.00 51.37 ? 343 GLN A CG 1 ATOM 2569 C CD . GLN A 1 366 ? 4.770 35.709 12.360 1.00 60.25 ? 343 GLN A CD 1 ATOM 2570 O OE1 . GLN A 1 366 ? 4.494 35.462 13.535 1.00 69.49 ? 343 GLN A OE1 1 ATOM 2571 N NE2 . GLN A 1 366 ? 3.899 35.548 11.372 1.00 51.02 ? 343 GLN A NE2 1 ATOM 2572 N N . LYS A 1 367 ? 8.397 36.610 8.782 1.00 68.13 ? 344 LYS A N 1 ATOM 2573 C CA . LYS A 1 367 ? 9.309 35.652 8.167 1.00 75.79 ? 344 LYS A CA 1 ATOM 2574 C C . LYS A 1 367 ? 10.745 36.168 8.161 1.00 70.49 ? 344 LYS A C 1 ATOM 2575 O O . LYS A 1 367 ? 11.685 35.405 8.381 1.00 69.11 ? 344 LYS A O 1 ATOM 2576 C CB . LYS A 1 367 ? 8.859 35.304 6.744 1.00 85.02 ? 344 LYS A CB 1 ATOM 2577 C CG . LYS A 1 367 ? 7.663 34.358 6.673 1.00 91.84 ? 344 LYS A CG 1 ATOM 2578 C CD . LYS A 1 367 ? 8.076 32.937 6.282 1.00 105.93 ? 344 LYS A CD 1 ATOM 2579 C CE . LYS A 1 367 ? 8.883 32.245 7.376 1.00 113.45 ? 344 LYS A CE 1 ATOM 2580 N NZ . LYS A 1 367 ? 9.330 30.880 6.974 1.00 113.95 ? 344 LYS A NZ 1 ATOM 2581 N N . MET A 1 368 ? 10.907 37.466 7.913 1.00 69.29 ? 345 MET A N 1 ATOM 2582 C CA . MET A 1 368 ? 12.226 38.091 7.907 1.00 69.29 ? 345 MET A CA 1 ATOM 2583 C C . MET A 1 368 ? 12.866 38.026 9.289 1.00 70.11 ? 345 MET A C 1 ATOM 2584 O O . MET A 1 368 ? 14.081 37.867 9.415 1.00 73.54 ? 345 MET A O 1 ATOM 2585 C CB . MET A 1 368 ? 12.134 39.549 7.449 1.00 68.83 ? 345 MET A CB 1 ATOM 2586 C CG . MET A 1 368 ? 11.610 39.736 6.034 1.00 72.09 ? 345 MET A CG 1 ATOM 2587 S SD . MET A 1 368 ? 11.422 41.476 5.590 1.00 162.77 ? 345 MET A SD 1 ATOM 2588 C CE . MET A 1 368 ? 10.662 41.339 3.974 1.00 79.75 ? 345 MET A CE 1 ATOM 2589 N N . ASN A 1 369 ? 12.029 38.147 10.314 1.00 65.13 ? 346 ASN A N 1 ATOM 2590 C CA . ASN A 1 369 ? 12.474 38.189 11.697 1.00 64.77 ? 346 ASN A CA 1 ATOM 2591 C C . ASN A 1 369 ? 11.356 37.888 12.686 1.00 70.40 ? 346 ASN A C 1 ATOM 2592 O O . ASN A 1 369 ? 10.561 38.767 13.002 1.00 74.38 ? 346 ASN A O 1 ATOM 2593 C CB . ASN A 1 369 ? 13.034 39.567 12.008 1.00 62.48 ? 346 ASN A CB 1 ATOM 2594 C CG . ASN A 1 369 ? 14.040 39.536 13.121 1.00 69.20 ? 346 ASN A CG 1 ATOM 2595 O OD1 . ASN A 1 369 ? 13.813 38.932 14.162 1.00 58.97 ? 346 ASN A OD1 1 ATOM 2596 N ND2 . ASN A 1 369 ? 15.164 40.187 12.903 1.00 97.37 ? 346 ASN A ND2 1 ATOM 2597 N N . ASP A 1 370 ? 11.297 36.658 13.182 1.00 66.74 ? 347 ASP A N 1 ATOM 2598 C CA . ASP A 1 370 ? 10.212 36.261 14.074 1.00 69.27 ? 347 ASP A CA 1 ATOM 2599 C C . ASP A 1 370 ? 10.391 36.850 15.469 1.00 60.22 ? 347 ASP A C 1 ATOM 2600 O O . ASP A 1 370 ? 9.431 36.979 16.228 1.00 59.37 ? 347 ASP A O 1 ATOM 2601 C CB . ASP A 1 370 ? 10.107 34.734 14.150 1.00 65.54 ? 347 ASP A CB 1 ATOM 2602 C CG . ASP A 1 370 ? 8.866 34.267 14.892 1.00 63.47 ? 347 ASP A CG 1 ATOM 2603 O OD1 . ASP A 1 370 ? 7.770 34.286 14.292 1.00 77.17 ? 347 ASP A OD1 1 ATOM 2604 O OD2 . ASP A 1 370 ? 8.985 33.873 16.070 1.00 60.05 ? 347 ASP A OD2 1 ATOM 2605 N N . THR A 1 371 ? 11.626 37.208 15.802 1.00 61.89 ? 348 THR A N 1 ATOM 2606 C CA . THR A 1 371 ? 11.925 37.767 17.113 1.00 64.81 ? 348 THR A CA 1 ATOM 2607 C C . THR A 1 371 ? 11.310 39.153 17.260 1.00 57.41 ? 348 THR A C 1 ATOM 2608 O O . THR A 1 371 ? 10.738 39.486 18.297 1.00 55.08 ? 348 THR A O 1 ATOM 2609 C CB . THR A 1 371 ? 13.444 37.870 17.345 1.00 62.94 ? 348 THR A CB 1 ATOM 2610 O OG1 . THR A 1 371 ? 14.066 36.619 17.024 1.00 69.70 ? 348 THR A OG1 1 ATOM 2611 C CG2 . THR A 1 371 ? 13.743 38.228 18.795 1.00 58.85 ? 348 THR A CG2 1 ATOM 2612 N N . ILE A 1 372 ? 11.422 39.951 16.203 1.00 55.14 ? 349 ILE A N 1 ATOM 2613 C CA . ILE A 1 372 ? 11.023 41.352 16.248 1.00 55.86 ? 349 ILE A CA 1 ATOM 2614 C C . ILE A 1 372 ? 9.638 41.573 15.642 1.00 62.01 ? 349 ILE A C 1 ATOM 2615 O O . ILE A 1 372 ? 8.837 42.353 16.161 1.00 66.77 ? 349 ILE A O 1 ATOM 2616 C CB . ILE A 1 372 ? 12.075 42.250 15.546 1.00 56.53 ? 349 ILE A CB 1 ATOM 2617 C CG1 . ILE A 1 372 ? 13.133 42.727 16.543 1.00 57.01 ? 349 ILE A CG1 1 ATOM 2618 C CG2 . ILE A 1 372 ? 11.429 43.461 14.917 1.00 46.81 ? 349 ILE A CG2 1 ATOM 2619 C CD1 . ILE A 1 372 ? 14.027 41.637 17.075 1.00 64.15 ? 349 ILE A CD1 1 ATOM 2620 N N . PHE A 1 373 ? 9.348 40.873 14.552 1.00 64.96 ? 350 PHE A N 1 ATOM 2621 C CA . PHE A 1 373 ? 8.091 41.077 13.844 1.00 59.17 ? 350 PHE A CA 1 ATOM 2622 C C . PHE A 1 373 ? 7.117 39.910 14.003 1.00 55.83 ? 350 PHE A C 1 ATOM 2623 O O . PHE A 1 373 ? 6.099 39.845 13.316 1.00 59.43 ? 350 PHE A O 1 ATOM 2624 C CB . PHE A 1 373 ? 8.359 41.365 12.366 1.00 55.56 ? 350 PHE A CB 1 ATOM 2625 C CG . PHE A 1 373 ? 9.098 42.651 12.128 1.00 58.75 ? 350 PHE A CG 1 ATOM 2626 C CD1 . PHE A 1 373 ? 8.660 43.833 12.706 1.00 61.40 ? 350 PHE A CD1 1 ATOM 2627 C CD2 . PHE A 1 373 ? 10.237 42.679 11.339 1.00 54.81 ? 350 PHE A CD2 1 ATOM 2628 C CE1 . PHE A 1 373 ? 9.337 45.022 12.491 1.00 58.31 ? 350 PHE A CE1 1 ATOM 2629 C CE2 . PHE A 1 373 ? 10.921 43.864 11.123 1.00 56.24 ? 350 PHE A CE2 1 ATOM 2630 C CZ . PHE A 1 373 ? 10.470 45.037 11.700 1.00 56.80 ? 350 PHE A CZ 1 ATOM 2631 N N . GLY A 1 374 ? 7.431 38.993 14.912 1.00 54.97 ? 351 GLY A N 1 ATOM 2632 C CA . GLY A 1 374 ? 6.533 37.893 15.214 1.00 56.89 ? 351 GLY A CA 1 ATOM 2633 C C . GLY A 1 374 ? 5.310 38.393 15.957 1.00 58.85 ? 351 GLY A C 1 ATOM 2634 O O . GLY A 1 374 ? 5.428 39.126 16.940 1.00 55.54 ? 351 GLY A O 1 ATOM 2635 N N . PHE A 1 375 ? 4.130 38.002 15.492 1.00 57.04 ? 352 PHE A N 1 ATOM 2636 C CA . PHE A 1 375 ? 2.897 38.492 16.095 1.00 62.69 ? 352 PHE A CA 1 ATOM 2637 C C . PHE A 1 375 ? 1.877 37.390 16.346 1.00 64.56 ? 352 PHE A C 1 ATOM 2638 O O . PHE A 1 375 ? 1.974 36.292 15.797 1.00 59.19 ? 352 PHE A O 1 ATOM 2639 C CB . PHE A 1 375 ? 2.275 39.600 15.235 1.00 57.94 ? 352 PHE A CB 1 ATOM 2640 C CG . PHE A 1 375 ? 1.715 39.116 13.925 1.00 49.79 ? 352 PHE A CG 1 ATOM 2641 C CD1 . PHE A 1 375 ? 2.539 38.946 12.823 1.00 60.41 ? 352 PHE A CD1 1 ATOM 2642 C CD2 . PHE A 1 375 ? 0.362 38.844 13.792 1.00 50.93 ? 352 PHE A CD2 1 ATOM 2643 C CE1 . PHE A 1 375 ? 2.025 38.505 11.615 1.00 50.00 ? 352 PHE A CE1 1 ATOM 2644 C CE2 . PHE A 1 375 ? -0.158 38.403 12.588 1.00 53.22 ? 352 PHE A CE2 1 ATOM 2645 C CZ . PHE A 1 375 ? 0.675 38.233 11.498 1.00 56.27 ? 352 PHE A CZ 1 ATOM 2646 N N . THR A 1 376 ? 0.897 37.702 17.187 1.00 67.67 ? 353 THR A N 1 ATOM 2647 C CA . THR A 1 376 ? -0.200 36.792 17.469 1.00 61.67 ? 353 THR A CA 1 ATOM 2648 C C . THR A 1 376 ? -1.521 37.445 17.083 1.00 62.18 ? 353 THR A C 1 ATOM 2649 O O . THR A 1 376 ? -1.832 38.552 17.523 1.00 60.83 ? 353 THR A O 1 ATOM 2650 C CB . THR A 1 376 ? -0.250 36.404 18.958 1.00 59.49 ? 353 THR A CB 1 ATOM 2651 O OG1 . THR A 1 376 ? 0.986 35.786 19.338 1.00 66.74 ? 353 THR A OG1 1 ATOM 2652 C CG2 . THR A 1 376 ? -1.398 35.442 19.222 1.00 57.69 ? 353 THR A CG2 1 ATOM 2653 N N . MET A 1 377 ? -2.291 36.758 16.248 1.00 52.96 ? 354 MET A N 1 ATOM 2654 C CA . MET A 1 377 ? -3.598 37.250 15.849 1.00 55.39 ? 354 MET A CA 1 ATOM 2655 C C . MET A 1 377 ? -4.692 36.258 16.209 1.00 56.68 ? 354 MET A C 1 ATOM 2656 O O . MET A 1 377 ? -4.465 35.049 16.244 1.00 66.69 ? 354 MET A O 1 ATOM 2657 C CB . MET A 1 377 ? -3.633 37.527 14.347 1.00 61.13 ? 354 MET A CB 1 ATOM 2658 C CG . MET A 1 377 ? -3.240 36.337 13.497 1.00 66.38 ? 354 MET A CG 1 ATOM 2659 S SD . MET A 1 377 ? -4.011 36.395 11.873 1.00 86.95 ? 354 MET A SD 1 ATOM 2660 C CE . MET A 1 377 ? -5.713 36.046 12.315 1.00 71.48 ? 354 MET A CE 1 ATOM 2661 N N . GLU A 1 378 ? -5.883 36.778 16.474 1.00 58.42 ? 355 GLU A N 1 ATOM 2662 C CA . GLU A 1 378 ? -7.041 35.937 16.729 1.00 55.09 ? 355 GLU A CA 1 ATOM 2663 C C . GLU A 1 378 ? -8.132 36.236 15.709 1.00 58.18 ? 355 GLU A C 1 ATOM 2664 O O . GLU A 1 378 ? -8.293 37.376 15.272 1.00 51.98 ? 355 GLU A O 1 ATOM 2665 C CB . GLU A 1 378 ? -7.562 36.151 18.151 1.00 56.04 ? 355 GLU A CB 1 ATOM 2666 C CG . GLU A 1 378 ? -6.558 35.796 19.239 1.00 68.84 ? 355 GLU A CG 1 ATOM 2667 C CD . GLU A 1 378 ? -7.129 35.959 20.635 1.00 80.32 ? 355 GLU A CD 1 ATOM 2668 O OE1 . GLU A 1 378 ? -8.369 35.997 20.769 1.00 79.75 ? 355 GLU A OE1 1 ATOM 2669 O OE2 . GLU A 1 378 ? -6.337 36.052 21.597 1.00 88.45 ? 355 GLU A OE2 1 ATOM 2670 N N . GLU A 1 379 ? -8.876 35.207 15.323 1.00 68.62 ? 356 GLU A N 1 ATOM 2671 C CA . GLU A 1 379 ? -9.960 35.381 14.369 1.00 72.90 ? 356 GLU A CA 1 ATOM 2672 C C . GLU A 1 379 ? -11.205 35.912 15.071 1.00 63.02 ? 356 GLU A C 1 ATOM 2673 O O . GLU A 1 379 ? -11.727 35.283 15.992 1.00 66.22 ? 356 GLU A O 1 ATOM 2674 C CB . GLU A 1 379 ? -10.270 34.062 13.661 1.00 89.22 ? 356 GLU A CB 1 ATOM 2675 C CG . GLU A 1 379 ? -11.030 34.228 12.357 1.00 103.07 ? 356 GLU A CG 1 ATOM 2676 C CD . GLU A 1 379 ? -10.206 34.923 11.290 1.00 104.83 ? 356 GLU A CD 1 ATOM 2677 O OE1 . GLU A 1 379 ? -9.004 34.604 11.163 1.00 105.71 ? 356 GLU A OE1 1 ATOM 2678 O OE2 . GLU A 1 379 ? -10.758 35.792 10.584 1.00 100.33 ? 356 GLU A OE2 1 ATOM 2679 N N . ARG A 1 380 ? -11.669 37.080 14.642 1.00 56.76 ? 357 ARG A N 1 ATOM 2680 C CA . ARG A 1 380 ? -12.888 37.666 15.183 1.00 61.51 ? 357 ARG A CA 1 ATOM 2681 C C . ARG A 1 380 ? -13.959 37.678 14.105 1.00 63.53 ? 357 ARG A C 1 ATOM 2682 O O . ARG A 1 380 ? -13.703 37.290 12.965 1.00 59.22 ? 357 ARG A O 1 ATOM 2683 C CB . ARG A 1 380 ? -12.629 39.091 15.668 1.00 59.01 ? 357 ARG A CB 1 ATOM 2684 C CG . ARG A 1 380 ? -11.678 39.196 16.846 1.00 60.66 ? 357 ARG A CG 1 ATOM 2685 C CD . ARG A 1 380 ? -12.345 38.768 18.141 1.00 64.29 ? 357 ARG A CD 1 ATOM 2686 N NE . ARG A 1 380 ? -11.560 39.171 19.305 1.00 74.17 ? 357 ARG A NE 1 ATOM 2687 C CZ . ARG A 1 380 ? -10.659 38.399 19.904 1.00 74.40 ? 357 ARG A CZ 1 ATOM 2688 N NH1 . ARG A 1 380 ? -10.429 37.173 19.455 1.00 72.50 ? 357 ARG A NH1 1 ATOM 2689 N NH2 . ARG A 1 380 ? -9.990 38.853 20.955 1.00 77.05 ? 357 ARG A NH2 1 ATOM 2690 N N . SER A 1 381 ? -15.156 38.126 14.464 1.00 62.82 ? 358 SER A N 1 ATOM 2691 C CA . SER A 1 381 ? -16.241 38.239 13.498 1.00 55.01 ? 358 SER A CA 1 ATOM 2692 C C . SER A 1 381 ? -15.888 39.280 12.445 1.00 51.52 ? 358 SER A C 1 ATOM 2693 O O . SER A 1 381 ? -16.194 39.112 11.264 1.00 54.42 ? 358 SER A O 1 ATOM 2694 C CB . SER A 1 381 ? -17.549 38.612 14.197 1.00 51.01 ? 358 SER A CB 1 ATOM 2695 O OG . SER A 1 381 ? -18.605 38.748 13.262 1.00 56.40 ? 358 SER A OG 1 ATOM 2696 N N . TRP A 1 382 ? -15.232 40.352 12.880 1.00 54.23 ? 359 TRP A N 1 ATOM 2697 C CA . TRP A 1 382 ? -14.803 41.410 11.974 1.00 50.47 ? 359 TRP A CA 1 ATOM 2698 C C . TRP A 1 382 ? -13.650 40.946 11.092 1.00 50.51 ? 359 TRP A C 1 ATOM 2699 O O . TRP A 1 382 ? -13.435 41.480 10.004 1.00 48.41 ? 359 TRP A O 1 ATOM 2700 C CB . TRP A 1 382 ? -14.391 42.659 12.756 1.00 44.19 ? 359 TRP A CB 1 ATOM 2701 C CG . TRP A 1 382 ? -15.524 43.564 13.126 1.00 38.92 ? 359 TRP A CG 1 ATOM 2702 C CD1 . TRP A 1 382 ? -16.211 43.581 14.305 1.00 41.57 ? 359 TRP A CD1 1 ATOM 2703 C CD2 . TRP A 1 382 ? -16.096 44.597 12.314 1.00 39.75 ? 359 TRP A CD2 1 ATOM 2704 N NE1 . TRP A 1 382 ? -17.178 44.559 14.276 1.00 44.01 ? 359 TRP A NE1 1 ATOM 2705 C CE2 . TRP A 1 382 ? -17.129 45.197 13.064 1.00 43.95 ? 359 TRP A CE2 1 ATOM 2706 C CE3 . TRP A 1 382 ? -15.837 45.072 11.024 1.00 40.68 ? 359 TRP A CE3 1 ATOM 2707 C CZ2 . TRP A 1 382 ? -17.902 46.244 12.568 1.00 48.30 ? 359 TRP A CZ2 1 ATOM 2708 C CZ3 . TRP A 1 382 ? -16.607 46.113 10.532 1.00 41.90 ? 359 TRP A CZ3 1 ATOM 2709 C CH2 . TRP A 1 382 ? -17.626 46.687 11.302 1.00 43.02 ? 359 TRP A CH2 1 ATOM 2710 N N . GLY A 1 383 ? -12.911 39.949 11.567 1.00 53.78 ? 360 GLY A N 1 ATOM 2711 C CA . GLY A 1 383 ? -11.771 39.430 10.836 1.00 47.25 ? 360 GLY A CA 1 ATOM 2712 C C . GLY A 1 383 ? -10.559 39.263 11.731 1.00 48.35 ? 360 GLY A C 1 ATOM 2713 O O . GLY A 1 383 ? -10.699 39.169 12.950 1.00 44.94 ? 360 GLY A O 1 ATOM 2714 N N . PRO A 1 384 ? -9.362 39.219 11.127 1.00 48.99 ? 361 PRO A N 1 ATOM 2715 C CA . PRO A 1 384 ? -8.092 39.078 11.851 1.00 49.76 ? 361 PRO A CA 1 ATOM 2716 C C . PRO A 1 384 ? -7.831 40.254 12.785 1.00 40.53 ? 361 PRO A C 1 ATOM 2717 O O . PRO A 1 384 ? -7.764 41.398 12.338 1.00 39.94 ? 361 PRO A O 1 ATOM 2718 C CB . PRO A 1 384 ? -7.048 39.060 10.728 1.00 40.50 ? 361 PRO A CB 1 ATOM 2719 C CG . PRO A 1 384 ? -7.798 38.620 9.518 1.00 44.02 ? 361 PRO A CG 1 ATOM 2720 C CD . PRO A 1 384 ? -9.168 39.206 9.668 1.00 38.58 ? 361 PRO A CD 1 ATOM 2721 N N . TYR A 1 385 ? -7.684 39.966 14.073 1.00 45.19 ? 362 TYR A N 1 ATOM 2722 C CA . TYR A 1 385 ? -7.427 40.994 15.070 1.00 39.87 ? 362 TYR A CA 1 ATOM 2723 C C . TYR A 1 385 ? -6.053 40.769 15.690 1.00 48.51 ? 362 TYR A C 1 ATOM 2724 O O . TYR A 1 385 ? -5.738 39.663 16.128 1.00 48.82 ? 362 TYR A O 1 ATOM 2725 C CB . TYR A 1 385 ? -8.512 40.967 16.152 1.00 43.27 ? 362 TYR A CB 1 ATOM 2726 C CG . TYR A 1 385 ? -8.338 42.003 17.242 1.00 48.45 ? 362 TYR A CG 1 ATOM 2727 C CD1 . TYR A 1 385 ? -8.767 43.313 17.057 1.00 41.45 ? 362 TYR A CD1 1 ATOM 2728 C CD2 . TYR A 1 385 ? -7.754 41.670 18.458 1.00 47.28 ? 362 TYR A CD2 1 ATOM 2729 C CE1 . TYR A 1 385 ? -8.611 44.264 18.050 1.00 38.63 ? 362 TYR A CE1 1 ATOM 2730 C CE2 . TYR A 1 385 ? -7.593 42.615 19.458 1.00 50.45 ? 362 TYR A CE2 1 ATOM 2731 C CZ . TYR A 1 385 ? -8.025 43.911 19.249 1.00 50.17 ? 362 TYR A CZ 1 ATOM 2732 O OH . TYR A 1 385 ? -7.869 44.855 20.238 1.00 50.68 ? 362 TYR A OH 1 ATOM 2733 N N . ILE A 1 386 ? -5.235 41.819 15.720 1.00 45.42 ? 363 ILE A N 1 ATOM 2734 C CA . ILE A 1 386 ? -3.885 41.722 16.268 1.00 39.96 ? 363 ILE A CA 1 ATOM 2735 C C . ILE A 1 386 ? -3.892 41.870 17.786 1.00 45.01 ? 363 ILE A C 1 ATOM 2736 O O . ILE A 1 386 ? -4.185 42.944 18.316 1.00 46.33 ? 363 ILE A O 1 ATOM 2737 C CB . ILE A 1 386 ? -2.943 42.781 15.661 1.00 44.50 ? 363 ILE A CB 1 ATOM 2738 C CG1 . ILE A 1 386 ? -3.006 42.744 14.132 1.00 42.52 ? 363 ILE A CG1 1 ATOM 2739 C CG2 . ILE A 1 386 ? -1.516 42.571 16.154 1.00 39.20 ? 363 ILE A CG2 1 ATOM 2740 C CD1 . ILE A 1 386 ? -2.723 41.378 13.540 1.00 44.35 ? 363 ILE A CD1 1 ATOM 2741 N N . THR A 1 387 ? -3.566 40.785 18.480 1.00 44.65 ? 364 THR A N 1 ATOM 2742 C CA . THR A 1 387 ? -3.587 40.773 19.939 1.00 44.75 ? 364 THR A CA 1 ATOM 2743 C C . THR A 1 387 ? -2.198 40.966 20.531 1.00 49.41 ? 364 THR A C 1 ATOM 2744 O O . THR A 1 387 ? -2.021 41.726 21.484 1.00 51.60 ? 364 THR A O 1 ATOM 2745 C CB . THR A 1 387 ? -4.180 39.459 20.487 1.00 45.11 ? 364 THR A CB 1 ATOM 2746 O OG1 . THR A 1 387 ? -3.389 38.351 20.041 1.00 47.79 ? 364 THR A OG1 1 ATOM 2747 C CG2 . THR A 1 387 ? -5.615 39.275 20.009 1.00 40.66 ? 364 THR A CG2 1 ATOM 2748 N N . CYS A 1 388 ? -1.213 40.273 19.968 1.00 47.18 ? 365 CYS A N 1 ATOM 2749 C CA . CYS A 1 388 ? 0.138 40.311 20.514 1.00 55.59 ? 365 CYS A CA 1 ATOM 2750 C C . CYS A 1 388 ? 1.196 40.497 19.436 1.00 53.92 ? 365 CYS A C 1 ATOM 2751 O O . CYS A 1 388 ? 1.066 39.983 18.325 1.00 51.24 ? 365 CYS A O 1 ATOM 2752 C CB . CYS A 1 388 ? 0.444 39.029 21.294 1.00 51.35 ? 365 CYS A CB 1 ATOM 2753 S SG . CYS A 1 388 ? -0.843 38.480 22.438 1.00 60.45 ? 365 CYS A SG 1 ATOM 2754 N N . ILE A 1 389 ? 2.240 41.243 19.779 1.00 53.46 ? 366 ILE A N 1 ATOM 2755 C CA . ILE A 1 389 ? 3.456 41.318 18.978 1.00 53.49 ? 366 ILE A CA 1 ATOM 2756 C C . ILE A 1 389 ? 4.645 41.219 19.927 1.00 48.85 ? 366 ILE A C 1 ATOM 2757 O O . ILE A 1 389 ? 4.658 41.874 20.971 1.00 51.27 ? 366 ILE A O 1 ATOM 2758 C CB . ILE A 1 389 ? 3.538 42.631 18.177 1.00 53.79 ? 366 ILE A CB 1 ATOM 2759 C CG1 . ILE A 1 389 ? 2.368 42.736 17.200 1.00 54.52 ? 366 ILE A CG1 1 ATOM 2760 C CG2 . ILE A 1 389 ? 4.857 42.720 17.424 1.00 44.83 ? 366 ILE A CG2 1 ATOM 2761 C CD1 . ILE A 1 389 ? 2.428 43.945 16.307 1.00 49.84 ? 366 ILE A CD1 1 ATOM 2762 N N . GLN A 1 390 ? 5.623 40.386 19.575 1.00 54.72 ? 367 GLN A N 1 ATOM 2763 C CA . GLN A 1 390 ? 6.808 40.157 20.406 1.00 53.36 ? 367 GLN A CA 1 ATOM 2764 C C . GLN A 1 390 ? 6.457 39.646 21.802 1.00 51.28 ? 367 GLN A C 1 ATOM 2765 O O . GLN A 1 390 ? 7.173 39.915 22.767 1.00 48.73 ? 367 GLN A O 1 ATOM 2766 C CB . GLN A 1 390 ? 7.652 41.430 20.533 1.00 62.42 ? 367 GLN A CB 1 ATOM 2767 C CG . GLN A 1 390 ? 8.233 41.951 19.234 1.00 63.55 ? 367 GLN A CG 1 ATOM 2768 C CD . GLN A 1 390 ? 9.080 43.193 19.440 1.00 56.45 ? 367 GLN A CD 1 ATOM 2769 O OE1 . GLN A 1 390 ? 9.361 43.584 20.573 1.00 58.00 ? 367 GLN A OE1 1 ATOM 2770 N NE2 . GLN A 1 390 ? 9.488 43.821 18.345 1.00 57.03 ? 367 GLN A NE2 1 ATOM 2771 N N . GLY A 1 391 ? 5.350 38.918 21.909 1.00 53.99 ? 368 GLY A N 1 ATOM 2772 C CA . GLY A 1 391 ? 4.899 38.415 23.194 1.00 49.69 ? 368 GLY A CA 1 ATOM 2773 C C . GLY A 1 391 ? 4.183 39.468 24.020 1.00 57.28 ? 368 GLY A C 1 ATOM 2774 O O . GLY A 1 391 ? 3.672 39.177 25.101 1.00 59.61 ? 368 GLY A O 1 ATOM 2775 N N . LEU A 1 392 ? 4.150 40.698 23.515 1.00 58.37 ? 369 LEU A N 1 ATOM 2776 C CA . LEU A 1 392 ? 3.442 41.783 24.184 1.00 59.59 ? 369 LEU A CA 1 ATOM 2777 C C . LEU A 1 392 ? 1.986 41.819 23.731 1.00 57.84 ? 369 LEU A C 1 ATOM 2778 O O . LEU A 1 392 ? 1.685 42.200 22.599 1.00 51.81 ? 369 LEU A O 1 ATOM 2779 C CB . LEU A 1 392 ? 4.123 43.127 23.910 1.00 48.49 ? 369 LEU A CB 1 ATOM 2780 C CG . LEU A 1 392 ? 3.407 44.372 24.443 1.00 55.57 ? 369 LEU A CG 1 ATOM 2781 C CD1 . LEU A 1 392 ? 3.262 44.317 25.960 1.00 47.96 ? 369 LEU A CD1 1 ATOM 2782 C CD2 . LEU A 1 392 ? 4.139 45.635 24.015 1.00 55.84 ? 369 LEU A CD2 1 ATOM 2783 N N . CYS A 1 393 ? 1.086 41.421 24.624 1.00 53.38 ? 370 CYS A N 1 ATOM 2784 C CA . CYS A 1 393 ? -0.325 41.287 24.281 1.00 47.92 ? 370 CYS A CA 1 ATOM 2785 C C . CYS A 1 393 ? -1.174 42.442 24.798 1.00 52.25 ? 370 CYS A C 1 ATOM 2786 O O . CYS A 1 393 ? -0.941 42.959 25.892 1.00 54.72 ? 370 CYS A O 1 ATOM 2787 C CB . CYS A 1 393 ? -0.872 39.962 24.813 1.00 44.74 ? 370 CYS A CB 1 ATOM 2788 S SG . CYS A 1 393 ? 0.061 38.517 24.258 1.00 61.98 ? 370 CYS A SG 1 ATOM 2789 N N . ALA A 1 394 ? -2.159 42.835 23.996 1.00 46.90 ? 371 ALA A N 1 ATOM 2790 C CA . ALA A 1 394 ? -3.115 43.866 24.378 1.00 50.04 ? 371 ALA A CA 1 ATOM 2791 C C . ALA A 1 394 ? -3.870 43.461 25.641 1.00 57.46 ? 371 ALA A C 1 ATOM 2792 O O . ALA A 1 394 ? -4.205 42.290 25.820 1.00 54.13 ? 371 ALA A O 1 ATOM 2793 C CB . ALA A 1 394 ? -4.092 44.123 23.236 1.00 42.17 ? 371 ALA A CB 1 ATOM 2794 N N . ASN A 1 395 ? -4.131 44.429 26.516 1.00 51.60 ? 372 ASN A N 1 ATOM 2795 C CA . ASN A 1 395 ? -4.854 44.162 27.756 1.00 50.12 ? 372 ASN A CA 1 ATOM 2796 C C . ASN A 1 395 ? -6.027 45.115 27.956 1.00 53.78 ? 372 ASN A C 1 ATOM 2797 O O . ASN A 1 395 ? -5.881 46.332 27.841 1.00 61.36 ? 372 ASN A O 1 ATOM 2798 C CB . ASN A 1 395 ? -3.912 44.222 28.963 1.00 47.53 ? 372 ASN A CB 1 ATOM 2799 C CG . ASN A 1 395 ? -4.587 43.779 30.252 1.00 60.14 ? 372 ASN A CG 1 ATOM 2800 O OD1 . ASN A 1 395 ? -5.105 44.599 31.012 1.00 55.22 ? 372 ASN A OD1 1 ATOM 2801 N ND2 . ASN A 1 395 ? -4.584 42.474 30.502 1.00 64.18 ? 372 ASN A ND2 1 ATOM 2802 N N . ASN A 1 396 ? -7.189 44.549 28.258 1.00 48.61 ? 373 ASN A N 1 ATOM 2803 C CA . ASN A 1 396 ? -8.405 45.336 28.412 1.00 58.20 ? 373 ASN A CA 1 ATOM 2804 C C . ASN A 1 396 ? -8.389 46.208 29.665 1.00 54.18 ? 373 ASN A C 1 ATOM 2805 O O . ASN A 1 396 ? -8.677 47.402 29.600 1.00 51.57 ? 373 ASN A O 1 ATOM 2806 C CB . ASN A 1 396 ? -9.632 44.422 28.410 1.00 68.08 ? 373 ASN A CB 1 ATOM 2807 C CG . ASN A 1 396 ? -10.836 45.067 27.752 1.00 90.59 ? 373 ASN A CG 1 ATOM 2808 O OD1 . ASN A 1 396 ? -11.143 46.235 27.995 1.00 89.61 ? 373 ASN A OD1 1 ATOM 2809 N ND2 . ASN A 1 396 ? -11.518 44.308 26.900 1.00 97.86 ? 373 ASN A ND2 1 ATOM 2810 N N . ASN A 1 397 ? -8.048 45.609 30.802 1.00 57.32 ? 374 ASN A N 1 ATOM 2811 C CA . ASN A 1 397 ? -7.984 46.349 32.059 1.00 56.12 ? 374 ASN A CA 1 ATOM 2812 C C . ASN A 1 397 ? -6.904 47.421 32.036 1.00 55.19 ? 374 ASN A C 1 ATOM 2813 O O . ASN A 1 397 ? -7.069 48.494 32.617 1.00 54.84 ? 374 ASN A O 1 ATOM 2814 C CB . ASN A 1 397 ? -7.774 45.402 33.242 1.00 65.63 ? 374 ASN A CB 1 ATOM 2815 C CG . ASN A 1 397 ? -9.037 44.644 33.614 1.00 71.86 ? 374 ASN A CG 1 ATOM 2816 O OD1 . ASN A 1 397 ? -10.137 45.198 33.591 1.00 69.82 ? 374 ASN A OD1 1 ATOM 2817 N ND2 . ASN A 1 397 ? -8.883 43.371 33.959 1.00 75.34 ? 374 ASN A ND2 1 ATOM 2818 N N . ASP A 1 398 ? -5.801 47.131 31.351 1.00 44.89 ? 375 ASP A N 1 ATOM 2819 C CA . ASP A 1 398 ? -4.728 48.105 31.191 1.00 51.54 ? 375 ASP A CA 1 ATOM 2820 C C . ASP A 1 398 ? -5.088 49.144 30.133 1.00 55.28 ? 375 ASP A C 1 ATOM 2821 O O . ASP A 1 398 ? -4.384 50.139 29.967 1.00 61.15 ? 375 ASP A O 1 ATOM 2822 C CB . ASP A 1 398 ? -3.414 47.412 30.818 1.00 58.64 ? 375 ASP A CB 1 ATOM 2823 C CG . ASP A 1 398 ? -2.899 46.505 31.919 1.00 63.42 ? 375 ASP A CG 1 ATOM 2824 O OD1 . ASP A 1 398 ? -3.212 46.762 33.101 1.00 66.82 ? 375 ASP A OD1 1 ATOM 2825 O OD2 . ASP A 1 398 ? -2.181 45.533 31.601 1.00 60.10 ? 375 ASP A OD2 1 ATOM 2826 N N . ARG A 1 399 ? -6.188 48.898 29.422 1.00 59.77 ? 376 ARG A N 1 ATOM 2827 C CA . ARG A 1 399 ? -6.668 49.799 28.377 1.00 65.52 ? 376 ARG A CA 1 ATOM 2828 C C . ARG A 1 399 ? -5.611 49.989 27.290 1.00 62.68 ? 376 ARG A C 1 ATOM 2829 O O . ARG A 1 399 ? -5.435 51.085 26.759 1.00 59.95 ? 376 ARG A O 1 ATOM 2830 C CB . ARG A 1 399 ? -7.099 51.145 28.976 1.00 70.86 ? 376 ARG A CB 1 ATOM 2831 C CG . ARG A 1 399 ? -7.973 51.006 30.218 1.00 72.93 ? 376 ARG A CG 1 ATOM 2832 C CD . ARG A 1 399 ? -8.380 52.351 30.807 1.00 75.64 ? 376 ARG A CD 1 ATOM 2833 N NE . ARG A 1 399 ? -9.525 52.937 30.114 1.00 83.67 ? 376 ARG A NE 1 ATOM 2834 C CZ . ARG A 1 399 ? -9.459 54.014 29.340 1.00 78.02 ? 376 ARG A CZ 1 ATOM 2835 N NH1 . ARG A 1 399 ? -8.300 54.632 29.161 1.00 88.49 ? 376 ARG A NH1 1 ATOM 2836 N NH2 . ARG A 1 399 ? -10.552 54.476 28.749 1.00 58.28 ? 376 ARG A NH2 1 ATOM 2837 N N . THR A 1 400 ? -4.910 48.907 26.966 1.00 57.44 ? 377 THR A N 1 ATOM 2838 C CA . THR A 1 400 ? -3.848 48.941 25.970 1.00 49.94 ? 377 THR A CA 1 ATOM 2839 C C . THR A 1 400 ? -4.217 48.101 24.755 1.00 47.37 ? 377 THR A C 1 ATOM 2840 O O . THR A 1 400 ? -4.942 47.114 24.875 1.00 46.49 ? 377 THR A O 1 ATOM 2841 C CB . THR A 1 400 ? -2.530 48.397 26.542 1.00 49.33 ? 377 THR A CB 1 ATOM 2842 O OG1 . THR A 1 400 ? -2.696 47.017 26.893 1.00 47.47 ? 377 THR A OG1 1 ATOM 2843 C CG2 . THR A 1 400 ? -2.114 49.183 27.773 1.00 47.34 ? 377 THR A CG2 1 ATOM 2844 N N . TYR A 1 401 ? -3.710 48.487 23.587 1.00 47.08 ? 378 TYR A N 1 ATOM 2845 C CA . TYR A 1 401 ? -3.972 47.737 22.363 1.00 46.55 ? 378 TYR A CA 1 ATOM 2846 C C . TYR A 1 401 ? -2.979 48.078 21.258 1.00 47.33 ? 378 TYR A C 1 ATOM 2847 O O . TYR A 1 401 ? -2.233 49.051 21.356 1.00 42.81 ? 378 TYR A O 1 ATOM 2848 C CB . TYR A 1 401 ? -5.394 47.996 21.868 1.00 41.36 ? 378 TYR A CB 1 ATOM 2849 C CG . TYR A 1 401 ? -5.588 49.346 21.212 1.00 49.07 ? 378 TYR A CG 1 ATOM 2850 C CD1 . TYR A 1 401 ? -5.600 50.513 21.966 1.00 49.66 ? 378 TYR A CD1 1 ATOM 2851 C CD2 . TYR A 1 401 ? -5.770 49.452 19.838 1.00 47.17 ? 378 TYR A CD2 1 ATOM 2852 C CE1 . TYR A 1 401 ? -5.781 51.748 21.370 1.00 54.00 ? 378 TYR A CE1 1 ATOM 2853 C CE2 . TYR A 1 401 ? -5.953 50.682 19.233 1.00 52.59 ? 378 TYR A CE2 1 ATOM 2854 C CZ . TYR A 1 401 ? -5.958 51.827 20.004 1.00 59.41 ? 378 TYR A CZ 1 ATOM 2855 O OH . TYR A 1 401 ? -6.140 53.053 19.407 1.00 51.98 ? 378 TYR A OH 1 ATOM 2856 N N . TRP A 1 402 ? -2.978 47.266 20.206 1.00 41.97 ? 379 TRP A N 1 ATOM 2857 C CA . TRP A 1 402 ? -2.151 47.533 19.037 1.00 44.26 ? 379 TRP A CA 1 ATOM 2858 C C . TRP A 1 402 ? -2.948 48.325 18.006 1.00 51.43 ? 379 TRP A C 1 ATOM 2859 O O . TRP A 1 402 ? -4.032 47.912 17.592 1.00 39.34 ? 379 TRP A O 1 ATOM 2860 C CB . TRP A 1 402 ? -1.625 46.230 18.429 1.00 39.18 ? 379 TRP A CB 1 ATOM 2861 C CG . TRP A 1 402 ? -0.644 45.510 19.308 1.00 48.84 ? 379 TRP A CG 1 ATOM 2862 C CD1 . TRP A 1 402 ? -0.894 44.431 20.107 1.00 46.93 ? 379 TRP A CD1 1 ATOM 2863 C CD2 . TRP A 1 402 ? 0.744 45.820 19.480 1.00 51.38 ? 379 TRP A CD2 1 ATOM 2864 N NE1 . TRP A 1 402 ? 0.250 44.050 20.764 1.00 53.86 ? 379 TRP A NE1 1 ATOM 2865 C CE2 . TRP A 1 402 ? 1.274 44.889 20.395 1.00 52.68 ? 379 TRP A CE2 1 ATOM 2866 C CE3 . TRP A 1 402 ? 1.594 46.798 18.948 1.00 47.26 ? 379 TRP A CE3 1 ATOM 2867 C CZ2 . TRP A 1 402 ? 2.609 44.901 20.792 1.00 57.17 ? 379 TRP A CZ2 1 ATOM 2868 C CZ3 . TRP A 1 402 ? 2.922 46.810 19.343 1.00 46.41 ? 379 TRP A CZ3 1 ATOM 2869 C CH2 . TRP A 1 402 ? 3.416 45.869 20.256 1.00 49.14 ? 379 TRP A CH2 1 ATOM 2870 N N . GLU A 1 403 ? -2.404 49.468 17.602 1.00 50.06 ? 380 GLU A N 1 ATOM 2871 C CA . GLU A 1 403 ? -3.082 50.360 16.668 1.00 42.68 ? 380 GLU A CA 1 ATOM 2872 C C . GLU A 1 403 ? -2.432 50.302 15.290 1.00 49.49 ? 380 GLU A C 1 ATOM 2873 O O . GLU A 1 403 ? -1.207 50.295 15.170 1.00 47.89 ? 380 GLU A O 1 ATOM 2874 C CB . GLU A 1 403 ? -3.058 51.792 17.204 1.00 48.99 ? 380 GLU A CB 1 ATOM 2875 C CG . GLU A 1 403 ? -3.821 52.798 16.364 1.00 49.40 ? 380 GLU A CG 1 ATOM 2876 C CD . GLU A 1 403 ? -3.640 54.220 16.862 1.00 55.83 ? 380 GLU A CD 1 ATOM 2877 O OE1 . GLU A 1 403 ? -4.457 55.090 16.496 1.00 53.87 ? 380 GLU A OE1 1 ATOM 2878 O OE2 . GLU A 1 403 ? -2.676 54.468 17.619 1.00 59.67 ? 380 GLU A OE2 1 ATOM 2879 N N . LEU A 1 404 ? -3.259 50.257 14.251 1.00 44.62 ? 381 LEU A N 1 ATOM 2880 C CA . LEU A 1 404 ? -2.761 50.206 12.882 1.00 45.03 ? 381 LEU A CA 1 ATOM 2881 C C . LEU A 1 404 ? -2.786 51.597 12.258 1.00 46.86 ? 381 LEU A C 1 ATOM 2882 O O . LEU A 1 404 ? -3.810 52.281 12.291 1.00 46.81 ? 381 LEU A O 1 ATOM 2883 C CB . LEU A 1 404 ? -3.599 49.239 12.047 1.00 41.68 ? 381 LEU A CB 1 ATOM 2884 C CG . LEU A 1 404 ? -3.854 47.859 12.657 1.00 48.79 ? 381 LEU A CG 1 ATOM 2885 C CD1 . LEU A 1 404 ? -4.637 46.997 11.685 1.00 41.60 ? 381 LEU A CD1 1 ATOM 2886 C CD2 . LEU A 1 404 ? -2.549 47.176 13.063 1.00 47.65 ? 381 LEU A CD2 1 ATOM 2887 N N . LEU A 1 405 ? -1.655 52.019 11.697 1.00 46.57 ? 382 LEU A N 1 ATOM 2888 C CA . LEU A 1 405 ? -1.554 53.358 11.123 1.00 46.28 ? 382 LEU A CA 1 ATOM 2889 C C . LEU A 1 405 ? -0.874 53.377 9.760 1.00 51.68 ? 382 LEU A C 1 ATOM 2890 O O . LEU A 1 405 ? -0.066 52.506 9.437 1.00 60.91 ? 382 LEU A O 1 ATOM 2891 C CB . LEU A 1 405 ? -0.813 54.309 12.071 1.00 43.21 ? 382 LEU A CB 1 ATOM 2892 C CG . LEU A 1 405 ? -1.382 54.516 13.476 1.00 51.58 ? 382 LEU A CG 1 ATOM 2893 C CD1 . LEU A 1 405 ? -0.725 53.555 14.451 1.00 54.12 ? 382 LEU A CD1 1 ATOM 2894 C CD2 . LEU A 1 405 ? -1.212 55.956 13.934 1.00 55.21 ? 382 LEU A CD2 1 ATOM 2895 N N . SER A 1 406 ? -1.212 54.384 8.965 1.00 61.21 ? 383 SER A N 1 ATOM 2896 C CA . SER A 1 406 ? -0.530 54.630 7.704 1.00 69.56 ? 383 SER A CA 1 ATOM 2897 C C . SER A 1 406 ? -0.236 56.117 7.586 1.00 66.18 ? 383 SER A C 1 ATOM 2898 O O . SER A 1 406 ? -1.152 56.932 7.490 1.00 64.30 ? 383 SER A O 1 ATOM 2899 C CB . SER A 1 406 ? -1.382 54.167 6.523 1.00 69.84 ? 383 SER A CB 1 ATOM 2900 O OG . SER A 1 406 ? -0.747 54.470 5.292 1.00 76.02 ? 383 SER A OG 1 ATOM 2901 N N . GLY A 1 407 ? 1.046 56.467 7.603 1.00 66.00 ? 384 GLY A N 1 ATOM 2902 C CA . GLY A 1 407 ? 1.445 57.859 7.541 1.00 63.82 ? 384 GLY A CA 1 ATOM 2903 C C . GLY A 1 407 ? 1.035 58.606 8.794 1.00 64.59 ? 384 GLY A C 1 ATOM 2904 O O . GLY A 1 407 ? 0.715 59.795 8.749 1.00 65.01 ? 384 GLY A O 1 ATOM 2905 N N . GLY A 1 408 ? 1.035 57.898 9.919 1.00 53.92 ? 385 GLY A N 1 ATOM 2906 C CA . GLY A 1 408 ? 0.716 58.498 11.202 1.00 47.22 ? 385 GLY A CA 1 ATOM 2907 C C . GLY A 1 408 ? -0.771 58.625 11.472 1.00 55.35 ? 385 GLY A C 1 ATOM 2908 O O . GLY A 1 408 ? -1.172 59.155 12.506 1.00 61.14 ? 385 GLY A O 1 ATOM 2909 N N . GLU A 1 409 ? -1.590 58.138 10.542 1.00 56.42 ? 386 GLU A N 1 ATOM 2910 C CA . GLU A 1 409 ? -3.043 58.196 10.688 1.00 67.65 ? 386 GLU A CA 1 ATOM 2911 C C . GLU A 1 409 ? -3.628 56.802 10.917 1.00 59.05 ? 386 GLU A C 1 ATOM 2912 O O . GLU A 1 409 ? -3.273 55.856 10.215 1.00 58.45 ? 386 GLU A O 1 ATOM 2913 C CB . GLU A 1 409 ? -3.676 58.820 9.440 1.00 83.08 ? 386 GLU A CB 1 ATOM 2914 C CG . GLU A 1 409 ? -3.167 60.214 9.094 1.00 92.38 ? 386 GLU A CG 1 ATOM 2915 C CD . GLU A 1 409 ? -3.947 61.317 9.787 1.00 103.66 ? 386 GLU A CD 1 ATOM 2916 O OE1 . GLU A 1 409 ? -4.871 60.998 10.565 1.00 105.41 ? 386 GLU A OE1 1 ATOM 2917 O OE2 . GLU A 1 409 ? -3.641 62.505 9.547 1.00 110.23 ? 386 GLU A OE2 1 ATOM 2918 N N . PRO A 1 410 ? -4.538 56.673 11.896 1.00 51.85 ? 387 PRO A N 1 ATOM 2919 C CA . PRO A 1 410 ? -5.167 55.379 12.200 1.00 45.40 ? 387 PRO A CA 1 ATOM 2920 C C . PRO A 1 410 ? -6.025 54.858 11.051 1.00 47.82 ? 387 PRO A C 1 ATOM 2921 O O . PRO A 1 410 ? -6.794 55.618 10.460 1.00 52.09 ? 387 PRO A O 1 ATOM 2922 C CB . PRO A 1 410 ? -6.044 55.691 13.418 1.00 48.10 ? 387 PRO A CB 1 ATOM 2923 C CG . PRO A 1 410 ? -6.296 57.157 13.343 1.00 55.00 ? 387 PRO A CG 1 ATOM 2924 C CD . PRO A 1 410 ? -5.049 57.753 12.759 1.00 45.89 ? 387 PRO A CD 1 ATOM 2925 N N . LEU A 1 411 ? -5.891 53.572 10.741 1.00 50.76 ? 388 LEU A N 1 ATOM 2926 C CA . LEU A 1 411 ? -6.663 52.954 9.668 1.00 47.90 ? 388 LEU A CA 1 ATOM 2927 C C . LEU A 1 411 ? -8.129 52.796 10.054 1.00 48.95 ? 388 LEU A C 1 ATOM 2928 O O . LEU A 1 411 ? -8.461 52.677 11.234 1.00 42.39 ? 388 LEU A O 1 ATOM 2929 C CB . LEU A 1 411 ? -6.085 51.586 9.304 1.00 42.54 ? 388 LEU A CB 1 ATOM 2930 C CG . LEU A 1 411 ? -4.610 51.539 8.908 1.00 54.13 ? 388 LEU A CG 1 ATOM 2931 C CD1 . LEU A 1 411 ? -4.223 50.127 8.501 1.00 57.74 ? 388 LEU A CD1 1 ATOM 2932 C CD2 . LEU A 1 411 ? -4.329 52.521 7.787 1.00 50.74 ? 388 LEU A CD2 1 ATOM 2933 N N . SER A 1 412 ? -8.995 52.793 9.045 1.00 48.10 ? 389 SER A N 1 ATOM 2934 C CA . SER A 1 412 ? -10.423 52.567 9.239 1.00 48.85 ? 389 SER A CA 1 ATOM 2935 C C . SER A 1 412 ? -10.769 51.110 8.967 1.00 45.66 ? 389 SER A C 1 ATOM 2936 O O . SER A 1 412 ? -11.931 50.716 9.034 1.00 45.43 ? 389 SER A O 1 ATOM 2937 C CB . SER A 1 412 ? -11.244 53.465 8.308 1.00 42.53 ? 389 SER A CB 1 ATOM 2938 O OG . SER A 1 412 ? -11.054 54.834 8.612 1.00 64.69 ? 389 SER A OG 1 ATOM 2939 N N . GLN A 1 413 ? -9.755 50.316 8.642 1.00 47.17 ? 390 GLN A N 1 ATOM 2940 C CA . GLN A 1 413 ? -9.950 48.903 8.350 1.00 47.44 ? 390 GLN A CA 1 ATOM 2941 C C . GLN A 1 413 ? -8.969 48.052 9.141 1.00 46.69 ? 390 GLN A C 1 ATOM 2942 O O . GLN A 1 413 ? -7.973 48.556 9.661 1.00 36.80 ? 390 GLN A O 1 ATOM 2943 C CB . GLN A 1 413 ? -9.759 48.631 6.857 1.00 54.00 ? 390 GLN A CB 1 ATOM 2944 C CG . GLN A 1 413 ? -10.712 49.380 5.946 1.00 48.64 ? 390 GLN A CG 1 ATOM 2945 C CD . GLN A 1 413 ? -10.419 49.127 4.481 1.00 49.53 ? 390 GLN A CD 1 ATOM 2946 O OE1 . GLN A 1 413 ? -10.948 48.188 3.884 1.00 60.15 ? 390 GLN A OE1 1 ATOM 2947 N NE2 . GLN A 1 413 ? -9.569 49.960 3.895 1.00 48.27 ? 390 GLN A NE2 1 ATOM 2948 N N . GLY A 1 414 ? -9.252 46.756 9.221 1.00 44.37 ? 391 GLY A N 1 ATOM 2949 C CA . GLY A 1 414 ? -8.348 45.822 9.864 1.00 44.48 ? 391 GLY A CA 1 ATOM 2950 C C . GLY A 1 414 ? -7.198 45.407 8.971 1.00 48.65 ? 391 GLY A C 1 ATOM 2951 O O . GLY A 1 414 ? -7.208 45.668 7.766 1.00 45.98 ? 391 GLY A O 1 ATOM 2952 N N . ALA A 1 415 ? -6.208 44.752 9.572 1.00 38.92 ? 392 ALA A N 1 ATOM 2953 C CA . ALA A 1 415 ? -5.023 44.287 8.855 1.00 37.33 ? 392 ALA A CA 1 ATOM 2954 C C . ALA A 1 415 ? -5.374 43.352 7.699 1.00 44.58 ? 392 ALA A C 1 ATOM 2955 O O . ALA A 1 415 ? -4.695 43.340 6.671 1.00 54.76 ? 392 ALA A O 1 ATOM 2956 C CB . ALA A 1 415 ? -4.062 43.602 9.819 1.00 37.83 ? 392 ALA A CB 1 ATOM 2957 N N . GLY A 1 416 ? -6.442 42.579 7.870 1.00 48.67 ? 393 GLY A N 1 ATOM 2958 C CA . GLY A 1 416 ? -6.866 41.626 6.860 1.00 45.34 ? 393 GLY A CA 1 ATOM 2959 C C . GLY A 1 416 ? -7.587 42.234 5.671 1.00 43.84 ? 393 GLY A C 1 ATOM 2960 O O . GLY A 1 416 ? -7.823 41.552 4.674 1.00 50.91 ? 393 GLY A O 1 ATOM 2961 N N . SER A 1 417 ? -7.933 43.515 5.760 1.00 41.63 ? 394 SER A N 1 ATOM 2962 C CA . SER A 1 417 ? -8.732 44.147 4.710 1.00 47.96 ? 394 SER A CA 1 ATOM 2963 C C . SER A 1 417 ? -8.086 45.381 4.078 1.00 47.18 ? 394 SER A C 1 ATOM 2964 O O . SER A 1 417 ? -8.377 45.715 2.930 1.00 53.62 ? 394 SER A O 1 ATOM 2965 C CB . SER A 1 417 ? -10.124 44.497 5.240 1.00 45.92 ? 394 SER A CB 1 ATOM 2966 O OG . SER A 1 417 ? -10.815 43.332 5.656 1.00 62.63 ? 394 SER A OG 1 ATOM 2967 N N . TYR A 1 418 ? -7.216 46.058 4.820 1.00 42.88 ? 395 TYR A N 1 ATOM 2968 C CA . TYR A 1 418 ? -6.616 47.291 4.325 1.00 42.64 ? 395 TYR A CA 1 ATOM 2969 C C . TYR A 1 418 ? -5.618 47.040 3.196 1.00 42.59 ? 395 TYR A C 1 ATOM 2970 O O . TYR A 1 418 ? -4.537 46.496 3.420 1.00 47.58 ? 395 TYR A O 1 ATOM 2971 C CB . TYR A 1 418 ? -5.942 48.069 5.457 1.00 40.81 ? 395 TYR A CB 1 ATOM 2972 C CG . TYR A 1 418 ? -5.399 49.410 5.017 1.00 48.13 ? 395 TYR A CG 1 ATOM 2973 C CD1 . TYR A 1 418 ? -6.227 50.523 4.939 1.00 45.62 ? 395 TYR A CD1 1 ATOM 2974 C CD2 . TYR A 1 418 ? -4.061 49.563 4.672 1.00 46.24 ? 395 TYR A CD2 1 ATOM 2975 C CE1 . TYR A 1 418 ? -5.738 51.752 4.533 1.00 44.72 ? 395 TYR A CE1 1 ATOM 2976 C CE2 . TYR A 1 418 ? -3.563 50.788 4.265 1.00 47.83 ? 395 TYR A CE2 1 ATOM 2977 C CZ . TYR A 1 418 ? -4.407 51.878 4.199 1.00 49.50 ? 395 TYR A CZ 1 ATOM 2978 O OH . TYR A 1 418 ? -3.918 53.099 3.796 1.00 53.93 ? 395 TYR A OH 1 ATOM 2979 N N . VAL A 1 419 ? -5.986 47.443 1.984 1.00 43.77 ? 396 VAL A N 1 ATOM 2980 C CA . VAL A 1 419 ? -5.112 47.292 0.826 1.00 55.17 ? 396 VAL A CA 1 ATOM 2981 C C . VAL A 1 419 ? -4.030 48.368 0.834 1.00 60.93 ? 396 VAL A C 1 ATOM 2982 O O . VAL A 1 419 ? -4.328 49.561 0.803 1.00 62.28 ? 396 VAL A O 1 ATOM 2983 C CB . VAL A 1 419 ? -5.905 47.365 -0.492 1.00 51.34 ? 396 VAL A CB 1 ATOM 2984 C CG1 . VAL A 1 419 ? -4.968 47.236 -1.682 1.00 49.91 ? 396 VAL A CG1 1 ATOM 2985 C CG2 . VAL A 1 419 ? -6.972 46.282 -0.525 1.00 37.76 ? 396 VAL A CG2 1 ATOM 2986 N N . VAL A 1 420 ? -2.774 47.937 0.877 1.00 62.35 ? 397 VAL A N 1 ATOM 2987 C CA . VAL A 1 420 ? -1.654 48.861 1.012 1.00 62.01 ? 397 VAL A CA 1 ATOM 2988 C C . VAL A 1 420 ? -1.190 49.406 -0.338 1.00 64.75 ? 397 VAL A C 1 ATOM 2989 O O . VAL A 1 420 ? -1.365 48.763 -1.373 1.00 64.72 ? 397 VAL A O 1 ATOM 2990 C CB . VAL A 1 420 ? -0.471 48.198 1.743 1.00 58.74 ? 397 VAL A CB 1 ATOM 2991 C CG1 . VAL A 1 420 ? -0.938 47.630 3.073 1.00 48.96 ? 397 VAL A CG1 1 ATOM 2992 C CG2 . VAL A 1 420 ? 0.137 47.101 0.887 1.00 55.59 ? 397 VAL A CG2 1 ATOM 2993 N N . ARG A 1 421 ? -0.604 50.599 -0.318 1.00 63.84 ? 398 ARG A N 1 ATOM 2994 C CA . ARG A 1 421 ? -0.127 51.237 -1.540 1.00 68.05 ? 398 ARG A CA 1 ATOM 2995 C C . ARG A 1 421 ? 1.368 51.525 -1.468 1.00 70.07 ? 398 ARG A C 1 ATOM 2996 O O . ARG A 1 421 ? 1.968 51.485 -0.394 1.00 68.82 ? 398 ARG A O 1 ATOM 2997 C CB . ARG A 1 421 ? -0.909 52.525 -1.824 1.00 76.66 ? 398 ARG A CB 1 ATOM 2998 C CG . ARG A 1 421 ? -2.400 52.309 -2.083 1.00 83.43 ? 398 ARG A CG 1 ATOM 2999 C CD . ARG A 1 421 ? -3.067 53.566 -2.630 1.00 92.65 ? 398 ARG A CD 1 ATOM 3000 N NE . ARG A 1 421 ? -2.973 54.695 -1.707 1.00 107.81 ? 398 ARG A NE 1 ATOM 3001 C CZ . ARG A 1 421 ? -3.940 55.064 -0.873 1.00 112.30 ? 398 ARG A CZ 1 ATOM 3002 N NH1 . ARG A 1 421 ? -5.086 54.398 -0.845 1.00 106.66 ? 398 ARG A NH1 1 ATOM 3003 N NH2 . ARG A 1 421 ? -3.764 56.105 -0.070 1.00 118.62 ? 398 ARG A NH2 1 ATOM 3004 N N . ASN A 1 422 ? 1.961 51.819 -2.621 1.00 68.16 ? 399 ASN A N 1 ATOM 3005 C CA . ASN A 1 422 ? 3.399 52.036 -2.721 1.00 67.87 ? 399 ASN A CA 1 ATOM 3006 C C . ASN A 1 422 ? 3.884 53.244 -1.925 1.00 66.75 ? 399 ASN A C 1 ATOM 3007 O O . ASN A 1 422 ? 3.301 54.325 -2.002 1.00 69.11 ? 399 ASN A O 1 ATOM 3008 C CB . ASN A 1 422 ? 3.806 52.190 -4.187 1.00 82.06 ? 399 ASN A CB 1 ATOM 3009 C CG . ASN A 1 422 ? 5.282 51.935 -4.411 1.00 77.26 ? 399 ASN A CG 1 ATOM 3010 O OD1 . ASN A 1 422 ? 5.877 51.068 -3.772 1.00 69.67 ? 399 ASN A OD1 1 ATOM 3011 N ND2 . ASN A 1 422 ? 5.881 52.693 -5.321 1.00 84.04 ? 399 ASN A ND2 1 ATOM 3012 N N . GLY A 1 423 ? 4.956 53.051 -1.162 1.00 58.99 ? 400 GLY A N 1 ATOM 3013 C CA . GLY A 1 423 ? 5.567 54.131 -0.410 1.00 58.86 ? 400 GLY A CA 1 ATOM 3014 C C . GLY A 1 423 ? 4.809 54.516 0.845 1.00 71.16 ? 400 GLY A C 1 ATOM 3015 O O . GLY A 1 423 ? 4.988 55.612 1.375 1.00 76.47 ? 400 GLY A O 1 ATOM 3016 N N . GLU A 1 424 ? 3.962 53.612 1.327 1.00 69.69 ? 401 GLU A N 1 ATOM 3017 C CA . GLU A 1 424 ? 3.180 53.873 2.529 1.00 68.70 ? 401 GLU A CA 1 ATOM 3018 C C . GLU A 1 424 ? 3.981 53.614 3.802 1.00 62.90 ? 401 GLU A C 1 ATOM 3019 O O . GLU A 1 424 ? 4.673 52.603 3.918 1.00 63.54 ? 401 GLU A O 1 ATOM 3020 C CB . GLU A 1 424 ? 1.906 53.026 2.536 1.00 68.35 ? 401 GLU A CB 1 ATOM 3021 C CG . GLU A 1 424 ? 0.630 53.826 2.354 1.00 70.02 ? 401 GLU A CG 1 ATOM 3022 C CD . GLU A 1 424 ? -0.616 52.990 2.569 1.00 62.96 ? 401 GLU A CD 1 ATOM 3023 O OE1 . GLU A 1 424 ? -1.600 53.523 3.121 1.00 60.29 ? 401 GLU A OE1 1 ATOM 3024 O OE2 . GLU A 1 424 ? -0.612 51.802 2.186 1.00 64.81 ? 401 GLU A OE2 1 ATOM 3025 N N . ASN A 1 425 ? 3.885 54.538 4.754 1.00 57.07 ? 402 ASN A N 1 ATOM 3026 C CA . ASN A 1 425 ? 4.480 54.344 6.071 1.00 62.54 ? 402 ASN A CA 1 ATOM 3027 C C . ASN A 1 425 ? 3.544 53.560 6.989 1.00 56.05 ? 402 ASN A C 1 ATOM 3028 O O . ASN A 1 425 ? 2.837 54.141 7.811 1.00 54.91 ? 402 ASN A O 1 ATOM 3029 C CB . ASN A 1 425 ? 4.832 55.689 6.713 1.00 73.12 ? 402 ASN A CB 1 ATOM 3030 C CG . ASN A 1 425 ? 5.927 56.422 5.967 1.00 89.28 ? 402 ASN A CG 1 ATOM 3031 O OD1 . ASN A 1 425 ? 6.844 55.807 5.424 1.00 97.04 ? 402 ASN A OD1 1 ATOM 3032 N ND2 . ASN A 1 425 ? 5.836 57.747 5.936 1.00 93.68 ? 402 ASN A ND2 1 ATOM 3033 N N . LEU A 1 426 ? 3.541 52.240 6.837 1.00 59.87 ? 403 LEU A N 1 ATOM 3034 C CA . LEU A 1 426 ? 2.692 51.376 7.650 1.00 62.53 ? 403 LEU A CA 1 ATOM 3035 C C . LEU A 1 426 ? 3.275 51.199 9.044 1.00 60.77 ? 403 LEU A C 1 ATOM 3036 O O . LEU A 1 426 ? 4.481 51.016 9.205 1.00 56.10 ? 403 LEU A O 1 ATOM 3037 C CB . LEU A 1 426 ? 2.531 50.013 6.985 1.00 55.54 ? 403 LEU A CB 1 ATOM 3038 C CG . LEU A 1 426 ? 2.023 50.049 5.547 1.00 55.73 ? 403 LEU A CG 1 ATOM 3039 C CD1 . LEU A 1 426 ? 1.900 48.639 5.005 1.00 61.39 ? 403 LEU A CD1 1 ATOM 3040 C CD2 . LEU A 1 426 ? 0.692 50.780 5.472 1.00 60.28 ? 403 LEU A CD2 1 ATOM 3041 N N . GLU A 1 427 ? 2.415 51.242 10.054 1.00 56.86 ? 404 GLU A N 1 ATOM 3042 C CA . GLU A 1 427 ? 2.881 51.144 11.428 1.00 56.26 ? 404 GLU A CA 1 ATOM 3043 C C . GLU A 1 427 ? 1.883 50.428 12.324 1.00 52.35 ? 404 GLU A C 1 ATOM 3044 O O . GLU A 1 427 ? 0.679 50.672 12.251 1.00 52.47 ? 404 GLU A O 1 ATOM 3045 C CB . GLU A 1 427 ? 3.173 52.538 11.984 1.00 60.23 ? 404 GLU A CB 1 ATOM 3046 C CG . GLU A 1 427 ? 3.635 52.555 13.430 1.00 71.64 ? 404 GLU A CG 1 ATOM 3047 C CD . GLU A 1 427 ? 3.888 53.959 13.938 1.00 81.15 ? 404 GLU A CD 1 ATOM 3048 O OE1 . GLU A 1 427 ? 3.933 54.892 13.108 1.00 93.73 ? 404 GLU A OE1 1 ATOM 3049 O OE2 . GLU A 1 427 ? 4.037 54.133 15.165 1.00 73.70 ? 404 GLU A OE2 1 ATOM 3050 N N . VAL A 1 428 ? 2.391 49.533 13.163 1.00 55.57 ? 405 VAL A N 1 ATOM 3051 C CA . VAL A 1 428 ? 1.590 48.946 14.224 1.00 45.33 ? 405 VAL A CA 1 ATOM 3052 C C . VAL A 1 428 ? 2.108 49.479 15.555 1.00 51.51 ? 405 VAL A C 1 ATOM 3053 O O . VAL A 1 428 ? 3.256 49.236 15.924 1.00 47.34 ? 405 VAL A O 1 ATOM 3054 C CB . VAL A 1 428 ? 1.653 47.415 14.214 1.00 48.58 ? 405 VAL A CB 1 ATOM 3055 C CG1 . VAL A 1 428 ? 0.637 46.850 15.192 1.00 54.34 ? 405 VAL A CG1 1 ATOM 3056 C CG2 . VAL A 1 428 ? 1.392 46.887 12.812 1.00 48.87 ? 405 VAL A CG2 1 ATOM 3057 N N . ARG A 1 429 ? 1.255 50.207 16.269 1.00 50.98 ? 406 ARG A N 1 ATOM 3058 C CA . ARG A 1 429 ? 1.680 50.975 17.434 1.00 50.19 ? 406 ARG A CA 1 ATOM 3059 C C . ARG A 1 429 ? 1.031 50.507 18.738 1.00 45.04 ? 406 ARG A C 1 ATOM 3060 O O . ARG A 1 429 ? -0.181 50.311 18.807 1.00 46.68 ? 406 ARG A O 1 ATOM 3061 C CB . ARG A 1 429 ? 1.378 52.459 17.202 1.00 55.26 ? 406 ARG A CB 1 ATOM 3062 C CG . ARG A 1 429 ? 1.677 53.376 18.378 1.00 58.08 ? 406 ARG A CG 1 ATOM 3063 C CD . ARG A 1 429 ? 1.306 54.817 18.046 1.00 57.30 ? 406 ARG A CD 1 ATOM 3064 N NE . ARG A 1 429 ? 1.954 55.278 16.819 1.00 67.86 ? 406 ARG A NE 1 ATOM 3065 C CZ . ARG A 1 429 ? 1.742 56.464 16.256 1.00 62.93 ? 406 ARG A CZ 1 ATOM 3066 N NH1 . ARG A 1 429 ? 0.895 57.322 16.806 1.00 56.91 ? 406 ARG A NH1 1 ATOM 3067 N NH2 . ARG A 1 429 ? 2.378 56.793 15.139 1.00 56.02 ? 406 ARG A NH2 1 ATOM 3068 N N . TRP A 1 430 ? 1.852 50.335 19.768 1.00 45.29 ? 407 TRP A N 1 ATOM 3069 C CA . TRP A 1 430 ? 1.362 50.016 21.103 1.00 51.70 ? 407 TRP A CA 1 ATOM 3070 C C . TRP A 1 430 ? 0.724 51.261 21.719 1.00 44.79 ? 407 TRP A C 1 ATOM 3071 O O . TRP A 1 430 ? 1.404 52.258 21.948 1.00 44.51 ? 407 TRP A O 1 ATOM 3072 C CB . TRP A 1 430 ? 2.520 49.520 21.969 1.00 46.68 ? 407 TRP A CB 1 ATOM 3073 C CG . TRP A 1 430 ? 2.134 49.146 23.360 1.00 54.87 ? 407 TRP A CG 1 ATOM 3074 C CD1 . TRP A 1 430 ? 2.430 49.830 24.503 1.00 53.43 ? 407 TRP A CD1 1 ATOM 3075 C CD2 . TRP A 1 430 ? 1.382 47.996 23.762 1.00 53.62 ? 407 TRP A CD2 1 ATOM 3076 N NE1 . TRP A 1 430 ? 1.910 49.176 25.592 1.00 55.94 ? 407 TRP A NE1 1 ATOM 3077 C CE2 . TRP A 1 430 ? 1.261 48.048 25.165 1.00 57.99 ? 407 TRP A CE2 1 ATOM 3078 C CE3 . TRP A 1 430 ? 0.801 46.927 23.072 1.00 54.36 ? 407 TRP A CE3 1 ATOM 3079 C CZ2 . TRP A 1 430 ? 0.583 47.071 25.892 1.00 52.78 ? 407 TRP A CZ2 1 ATOM 3080 C CZ3 . TRP A 1 430 ? 0.127 45.958 23.796 1.00 59.12 ? 407 TRP A CZ3 1 ATOM 3081 C CH2 . TRP A 1 430 ? 0.022 46.038 25.192 1.00 55.90 ? 407 TRP A CH2 1 ATOM 3082 N N . SER A 1 431 ? -0.580 51.206 21.981 1.00 48.53 ? 408 SER A N 1 ATOM 3083 C CA . SER A 1 431 ? -1.316 52.405 22.380 1.00 53.83 ? 408 SER A CA 1 ATOM 3084 C C . SER A 1 431 ? -2.261 52.198 23.564 1.00 58.53 ? 408 SER A C 1 ATOM 3085 O O . SER A 1 431 ? -2.582 51.068 23.931 1.00 51.43 ? 408 SER A O 1 ATOM 3086 C CB . SER A 1 431 ? -2.103 52.956 21.189 1.00 54.80 ? 408 SER A CB 1 ATOM 3087 O OG . SER A 1 431 ? -1.268 53.115 20.056 1.00 58.24 ? 408 SER A OG 1 ATOM 3088 N N . LYS A 1 432 ? -2.705 53.307 24.148 1.00 65.06 ? 409 LYS A N 1 ATOM 3089 C CA . LYS A 1 432 ? -3.636 53.279 25.270 1.00 72.82 ? 409 LYS A CA 1 ATOM 3090 C C . LYS A 1 432 ? -4.977 53.864 24.840 1.00 75.24 ? 409 LYS A C 1 ATOM 3091 O O . LYS A 1 432 ? -5.075 54.491 23.785 1.00 61.21 ? 409 LYS A O 1 ATOM 3092 C CB . LYS A 1 432 ? -3.088 54.100 26.440 1.00 75.23 ? 409 LYS A CB 1 ATOM 3093 C CG . LYS A 1 432 ? -1.585 53.995 26.656 1.00 89.32 ? 409 LYS A CG 1 ATOM 3094 C CD . LYS A 1 432 ? -1.180 52.633 27.191 1.00 97.82 ? 409 LYS A CD 1 ATOM 3095 C CE . LYS A 1 432 ? 0.272 52.631 27.649 1.00 96.64 ? 409 LYS A CE 1 ATOM 3096 N NZ . LYS A 1 432 ? 1.201 53.042 26.560 1.00 99.54 ? 409 LYS A NZ 1 ATOM 3097 N N . TYR A 1 433 ? -6.009 53.665 25.657 1.00 87.83 ? 410 TYR A N 1 ATOM 3098 C CA . TYR A 1 433 ? -7.294 54.315 25.415 1.00 94.29 ? 410 TYR A CA 1 ATOM 3099 C C . TYR A 1 433 ? -7.251 55.731 25.983 1.00 104.01 ? 410 TYR A C 1 ATOM 3100 O O . TYR A 1 433 ? -8.067 56.578 25.620 1.00 108.70 ? 410 TYR A O 1 ATOM 3101 C CB . TYR A 1 433 ? -8.450 53.556 26.077 1.00 90.08 ? 410 TYR A CB 1 ATOM 3102 C CG . TYR A 1 433 ? -8.620 52.103 25.682 1.00 90.30 ? 410 TYR A CG 1 ATOM 3103 C CD1 . TYR A 1 433 ? -7.988 51.572 24.564 1.00 85.12 ? 410 TYR A CD1 1 ATOM 3104 C CD2 . TYR A 1 433 ? -9.434 51.262 26.433 1.00 85.05 ? 410 TYR A CD2 1 ATOM 3105 C CE1 . TYR A 1 433 ? -8.153 50.241 24.217 1.00 78.08 ? 410 TYR A CE1 1 ATOM 3106 C CE2 . TYR A 1 433 ? -9.605 49.937 26.094 1.00 78.79 ? 410 TYR A CE2 1 ATOM 3107 C CZ . TYR A 1 433 ? -8.964 49.430 24.987 1.00 76.56 ? 410 TYR A CZ 1 ATOM 3108 O OH . TYR A 1 433 ? -9.139 48.107 24.656 1.00 76.21 ? 410 TYR A OH 1 ATOM 3109 N N . LEU A 1 434 ? -6.295 55.967 26.880 1.00 105.08 ? 411 LEU A N 1 ATOM 3110 C CA . LEU A 1 434 ? -6.163 57.236 27.600 1.00 100.92 ? 411 LEU A CA 1 ATOM 3111 C C . LEU A 1 434 ? -7.428 57.594 28.377 1.00 93.95 ? 411 LEU A C 1 ATOM 3112 O O . LEU A 1 434 ? -7.386 57.795 29.591 1.00 89.02 ? 411 LEU A O 1 ATOM 3113 C CB . LEU A 1 434 ? -5.773 58.381 26.657 1.00 99.73 ? 411 LEU A CB 1 ATOM 3114 C CG . LEU A 1 434 ? -5.641 59.759 27.313 1.00 101.37 ? 411 LEU A CG 1 ATOM 3115 C CD1 . LEU A 1 434 ? -4.516 59.766 28.340 1.00 100.25 ? 411 LEU A CD1 1 ATOM 3116 C CD2 . LEU A 1 434 ? -5.432 60.851 26.272 1.00 98.71 ? 411 LEU A CD2 1 HETATM 3117 C C1 . NAG B 2 . ? 8.070 51.855 27.702 1.00 76.79 ? 501 NAG A C1 1 HETATM 3118 C C2 . NAG B 2 . ? 7.688 50.499 28.291 1.00 79.19 ? 501 NAG A C2 1 HETATM 3119 C C3 . NAG B 2 . ? 7.528 50.522 29.809 1.00 78.67 ? 501 NAG A C3 1 HETATM 3120 C C4 . NAG B 2 . ? 8.601 51.360 30.491 1.00 81.54 ? 501 NAG A C4 1 HETATM 3121 C C5 . NAG B 2 . ? 8.748 52.707 29.798 1.00 82.54 ? 501 NAG A C5 1 HETATM 3122 C C6 . NAG B 2 . ? 9.833 53.551 30.456 1.00 82.69 ? 501 NAG A C6 1 HETATM 3123 C C7 . NAG B 2 . ? 6.208 48.752 27.506 1.00 79.28 ? 501 NAG A C7 1 HETATM 3124 C C8 . NAG B 2 . ? 5.058 48.392 26.613 1.00 67.92 ? 501 NAG A C8 1 HETATM 3125 N N2 . NAG B 2 . ? 6.448 50.046 27.686 1.00 75.04 ? 501 NAG A N2 1 HETATM 3126 O O3 . NAG B 2 . ? 7.586 49.197 30.292 1.00 70.71 ? 501 NAG A O3 1 HETATM 3127 O O4 . NAG B 2 . ? 8.235 51.574 31.836 1.00 79.87 ? 501 NAG A O4 1 HETATM 3128 O O5 . NAG B 2 . ? 9.083 52.497 28.445 1.00 75.71 ? 501 NAG A O5 1 HETATM 3129 O O6 . NAG B 2 . ? 9.601 54.915 30.180 1.00 90.77 ? 501 NAG A O6 1 HETATM 3130 O O7 . NAG B 2 . ? 6.880 47.874 28.043 1.00 97.57 ? 501 NAG A O7 1 HETATM 3131 C C1 . NAG C 2 . ? 14.667 47.096 0.760 1.00 87.41 ? 502 NAG A C1 1 HETATM 3132 C C2 . NAG C 2 . ? 14.837 45.829 -0.111 1.00 89.80 ? 502 NAG A C2 1 HETATM 3133 C C3 . NAG C 2 . ? 16.238 45.560 -0.651 1.00 91.17 ? 502 NAG A C3 1 HETATM 3134 C C4 . NAG C 2 . ? 16.950 46.847 -0.979 1.00 86.78 ? 502 NAG A C4 1 HETATM 3135 C C5 . NAG C 2 . ? 16.955 47.707 0.261 1.00 86.75 ? 502 NAG A C5 1 HETATM 3136 C C6 . NAG C 2 . ? 17.812 48.943 0.044 1.00 91.52 ? 502 NAG A C6 1 HETATM 3137 C C7 . NAG C 2 . ? 13.140 44.273 0.615 1.00 85.96 ? 502 NAG A C7 1 HETATM 3138 C C8 . NAG C 2 . ? 12.871 42.960 1.284 1.00 76.43 ? 502 NAG A C8 1 HETATM 3139 N N2 . NAG C 2 . ? 14.396 44.694 0.668 1.00 85.53 ? 502 NAG A N2 1 HETATM 3140 O O3 . NAG C 2 . ? 16.152 44.785 -1.847 1.00 88.49 ? 502 NAG A O3 1 HETATM 3141 O O4 . NAG C 2 . ? 18.284 46.549 -1.373 1.00 76.64 ? 502 NAG A O4 1 HETATM 3142 O O5 . NAG C 2 . ? 15.621 48.121 0.488 1.00 83.81 ? 502 NAG A O5 1 HETATM 3143 O O6 . NAG C 2 . ? 17.188 49.797 -0.918 1.00 83.14 ? 502 NAG A O6 1 HETATM 3144 O O7 . NAG C 2 . ? 12.269 44.914 0.057 1.00 86.58 ? 502 NAG A O7 1 HETATM 3145 C C1 . NAG D 2 . ? 16.247 40.238 13.872 1.00 67.90 ? 503 NAG A C1 1 HETATM 3146 C C2 . NAG D 2 . ? 17.397 39.233 14.121 1.00 72.42 ? 503 NAG A C2 1 HETATM 3147 C C3 . NAG D 2 . ? 18.478 39.688 15.088 1.00 78.04 ? 503 NAG A C3 1 HETATM 3148 C C4 . NAG D 2 . ? 18.712 41.180 15.023 1.00 69.47 ? 503 NAG A C4 1 HETATM 3149 C C5 . NAG D 2 . ? 17.392 41.887 15.168 1.00 63.11 ? 503 NAG A C5 1 HETATM 3150 C C6 . NAG D 2 . ? 17.604 43.383 15.241 1.00 65.63 ? 503 NAG A C6 1 HETATM 3151 C C7 . NAG D 2 . ? 16.558 37.021 13.736 1.00 74.41 ? 503 NAG A C7 1 HETATM 3152 C C8 . NAG D 2 . ? 15.747 35.884 14.268 1.00 71.68 ? 503 NAG A C8 1 HETATM 3153 N N2 . NAG D 2 . ? 16.820 37.997 14.590 1.00 70.18 ? 503 NAG A N2 1 HETATM 3154 O O3 . NAG D 2 . ? 19.688 39.025 14.732 1.00 82.56 ? 503 NAG A O3 1 HETATM 3155 O O4 . NAG D 2 . ? 19.575 41.561 16.085 1.00 68.89 ? 503 NAG A O4 1 HETATM 3156 O O5 . NAG D 2 . ? 16.668 41.593 13.991 1.00 69.94 ? 503 NAG A O5 1 HETATM 3157 O O6 . NAG D 2 . ? 18.379 43.780 14.116 1.00 72.17 ? 503 NAG A O6 1 HETATM 3158 O O7 . NAG D 2 . ? 16.953 37.049 12.589 1.00 80.62 ? 503 NAG A O7 1 HETATM 3159 C C1 . NAG E 2 . ? -29.290 64.993 37.895 1.00 69.79 ? 504 NAG A C1 1 HETATM 3160 C C2 . NAG E 2 . ? -29.426 64.322 39.260 1.00 76.04 ? 504 NAG A C2 1 HETATM 3161 C C3 . NAG E 2 . ? -29.121 65.282 40.408 1.00 84.31 ? 504 NAG A C3 1 HETATM 3162 C C4 . NAG E 2 . ? -27.859 66.090 40.137 1.00 86.44 ? 504 NAG A C4 1 HETATM 3163 C C5 . NAG E 2 . ? -27.927 66.722 38.753 1.00 82.43 ? 504 NAG A C5 1 HETATM 3164 C C6 . NAG E 2 . ? -26.676 67.537 38.445 1.00 82.73 ? 504 NAG A C6 1 HETATM 3165 C C7 . NAG E 2 . ? -31.029 62.500 39.232 1.00 67.23 ? 504 NAG A C7 1 HETATM 3166 C C8 . NAG E 2 . ? -32.404 62.037 39.612 1.00 63.62 ? 504 NAG A C8 1 HETATM 3167 N N2 . NAG E 2 . ? -30.770 63.794 39.399 1.00 71.19 ? 504 NAG A N2 1 HETATM 3168 O O3 . NAG E 2 . ? -28.960 64.554 41.607 1.00 87.68 ? 504 NAG A O3 1 HETATM 3169 O O4 . NAG E 2 . ? -27.721 67.095 41.117 1.00 88.87 ? 504 NAG A O4 1 HETATM 3170 O O5 . NAG E 2 . ? -28.075 65.707 37.784 1.00 78.30 ? 504 NAG A O5 1 HETATM 3171 O O6 . NAG E 2 . ? -25.552 66.686 38.418 1.00 92.75 ? 504 NAG A O6 1 HETATM 3172 O O7 . NAG E 2 . ? -30.202 61.704 38.790 1.00 74.03 ? 504 NAG A O7 1 HETATM 3173 C C1 . NAG F 2 . ? -33.760 40.028 -12.927 1.00 120.53 ? 505 NAG A C1 1 HETATM 3174 C C2 . NAG F 2 . ? -34.413 41.159 -13.722 1.00 122.15 ? 505 NAG A C2 1 HETATM 3175 C C3 . NAG F 2 . ? -34.095 41.081 -15.212 1.00 132.24 ? 505 NAG A C3 1 HETATM 3176 C C4 . NAG F 2 . ? -32.608 40.833 -15.434 1.00 139.48 ? 505 NAG A C4 1 HETATM 3177 C C5 . NAG F 2 . ? -32.165 39.616 -14.632 1.00 134.61 ? 505 NAG A C5 1 HETATM 3178 C C6 . NAG F 2 . ? -30.690 39.298 -14.859 1.00 132.07 ? 505 NAG A C6 1 HETATM 3179 C C7 . NAG F 2 . ? -36.493 42.113 -12.901 1.00 109.01 ? 505 NAG A C7 1 HETATM 3180 C C8 . NAG F 2 . ? -36.920 43.277 -13.745 1.00 105.40 ? 505 NAG A C8 1 HETATM 3181 N N2 . NAG F 2 . ? -35.850 41.129 -13.525 1.00 115.05 ? 505 NAG A N2 1 HETATM 3182 O O3 . NAG F 2 . ? -34.481 42.284 -15.841 1.00 132.21 ? 505 NAG A O3 1 HETATM 3183 O O4 . NAG F 2 . ? -32.351 40.625 -16.804 1.00 146.06 ? 505 NAG A O4 1 HETATM 3184 O O5 . NAG F 2 . ? -32.396 39.851 -13.260 1.00 129.94 ? 505 NAG A O5 1 HETATM 3185 O O6 . NAG F 2 . ? -30.509 38.760 -16.151 1.00 129.68 ? 505 NAG A O6 1 HETATM 3186 O O7 . NAG F 2 . ? -36.738 42.093 -11.695 1.00 108.22 ? 505 NAG A O7 1 HETATM 3187 C C1 . NAG G 2 . ? -1.445 48.206 -8.423 1.00 111.64 ? 506 NAG A C1 1 HETATM 3188 C C2 . NAG G 2 . ? -0.913 49.394 -9.234 1.00 123.56 ? 506 NAG A C2 1 HETATM 3189 C C3 . NAG G 2 . ? -1.667 50.670 -8.895 1.00 128.64 ? 506 NAG A C3 1 HETATM 3190 C C4 . NAG G 2 . ? -3.157 50.435 -9.063 1.00 128.34 ? 506 NAG A C4 1 HETATM 3191 C C5 . NAG G 2 . ? -3.574 49.253 -8.206 1.00 125.52 ? 506 NAG A C5 1 HETATM 3192 C C6 . NAG G 2 . ? -5.063 48.983 -8.346 1.00 120.24 ? 506 NAG A C6 1 HETATM 3193 C C7 . NAG G 2 . ? 1.169 50.646 -9.225 1.00 128.16 ? 506 NAG A C7 1 HETATM 3194 C C8 . NAG G 2 . ? 1.209 51.057 -10.665 1.00 124.83 ? 506 NAG A C8 1 HETATM 3195 N N2 . NAG G 2 . ? 0.502 49.530 -8.967 1.00 127.16 ? 506 NAG A N2 1 HETATM 3196 O O3 . NAG G 2 . ? -1.251 51.725 -9.764 1.00 131.22 ? 506 NAG A O3 1 HETATM 3197 O O4 . NAG G 2 . ? -3.885 51.605 -8.677 1.00 127.03 ? 506 NAG A O4 1 HETATM 3198 O O5 . NAG G 2 . ? -2.850 48.103 -8.633 1.00 122.92 ? 506 NAG A O5 1 HETATM 3199 O O6 . NAG G 2 . ? -5.261 47.570 -8.476 1.00 115.94 ? 506 NAG A O6 1 HETATM 3200 O O7 . NAG G 2 . ? 1.716 51.289 -8.346 1.00 131.78 ? 506 NAG A O7 1 HETATM 3201 C C1 . NAG H 2 . ? 10.114 54.512 8.079 1.00 105.77 ? 507 NAG A C1 1 HETATM 3202 C C2 . NAG H 2 . ? 10.559 55.929 7.725 1.00 111.68 ? 507 NAG A C2 1 HETATM 3203 C C3 . NAG H 2 . ? 11.847 56.288 8.451 1.00 111.53 ? 507 NAG A C3 1 HETATM 3204 C C4 . NAG H 2 . ? 11.687 56.045 9.944 1.00 116.09 ? 507 NAG A C4 1 HETATM 3205 C C5 . NAG H 2 . ? 11.159 54.642 10.219 1.00 116.47 ? 507 NAG A C5 1 HETATM 3206 C C6 . NAG H 2 . ? 10.867 54.485 11.706 1.00 121.70 ? 507 NAG A C6 1 HETATM 3207 C C7 . NAG H 2 . ? 10.181 57.105 5.640 1.00 115.44 ? 507 NAG A C7 1 HETATM 3208 C C8 . NAG H 2 . ? 10.869 57.542 4.380 1.00 114.99 ? 507 NAG A C8 1 HETATM 3209 N N2 . NAG H 2 . ? 10.727 56.081 6.291 1.00 114.18 ? 507 NAG A N2 1 HETATM 3210 O O3 . NAG H 2 . ? 12.158 57.644 8.226 1.00 108.06 ? 507 NAG A O3 1 HETATM 3211 O O4 . NAG H 2 . ? 12.932 56.208 10.587 1.00 118.17 ? 507 NAG A O4 1 HETATM 3212 O O5 . NAG H 2 . ? 9.981 54.376 9.481 1.00 110.29 ? 507 NAG A O5 1 HETATM 3213 O O6 . NAG H 2 . ? 10.266 53.232 11.933 1.00 125.99 ? 507 NAG A O6 1 HETATM 3214 O O7 . NAG H 2 . ? 9.167 57.684 6.030 1.00 115.22 ? 507 NAG A O7 1 HETATM 3215 CO CO . CNC I 3 . ? -12.333 48.966 16.900 1.00 40.17 ? 508 CNC A CO 1 HETATM 3216 N N21 . CNC I 3 . ? -13.161 49.151 15.202 1.00 47.72 ? 508 CNC A N21 1 HETATM 3217 N N22 . CNC I 3 . ? -10.583 48.948 16.033 1.00 48.62 ? 508 CNC A N22 1 HETATM 3218 N N23 . CNC I 3 . ? -11.687 48.765 18.723 1.00 47.63 ? 508 CNC A N23 1 HETATM 3219 N N24 . CNC I 3 . ? -14.099 49.128 17.592 1.00 44.41 ? 508 CNC A N24 1 HETATM 3220 C C1 . CNC I 3 . ? -14.664 49.058 15.170 1.00 42.64 ? 508 CNC A C1 1 HETATM 3221 C C20 . CNC I 3 . ? -15.052 47.521 15.100 1.00 28.39 ? 508 CNC A C20 1 HETATM 3222 C C2 . CNC I 3 . ? -14.984 49.909 13.868 1.00 42.19 ? 508 CNC A C2 1 HETATM 3223 C C25 . CNC I 3 . ? -16.369 49.567 13.246 1.00 23.70 ? 508 CNC A C25 1 HETATM 3224 C C26 . CNC I 3 . ? -14.981 51.458 14.223 1.00 26.40 ? 508 CNC A C26 1 HETATM 3225 C C27 . CNC I 3 . ? -14.948 52.410 13.006 1.00 30.19 ? 508 CNC A C27 1 HETATM 3226 O O28 . CNC I 3 . ? -13.885 52.633 12.411 1.00 40.02 ? 508 CNC A O28 1 HETATM 3227 N N29 . CNC I 3 . ? -16.063 52.984 12.600 1.00 35.50 ? 508 CNC A N29 1 HETATM 3228 C C3 . CNC I 3 . ? -13.769 49.610 12.923 1.00 36.13 ? 508 CNC A C3 1 HETATM 3229 C C30 . CNC I 3 . ? -14.110 48.501 11.841 1.00 35.16 ? 508 CNC A C30 1 HETATM 3230 C C31 . CNC I 3 . ? -14.093 48.926 10.412 1.00 39.03 ? 508 CNC A C31 1 HETATM 3231 C C32 . CNC I 3 . ? -13.788 47.892 9.374 1.00 44.17 ? 508 CNC A C32 1 HETATM 3232 O O34 . CNC I 3 . ? -12.990 47.098 9.778 1.00 38.27 ? 508 CNC A O34 1 HETATM 3233 N N33 . CNC I 3 . ? -14.321 47.873 8.190 1.00 46.91 ? 508 CNC A N33 1 HETATM 3234 C C4 . CNC I 3 . ? -12.668 49.366 13.995 1.00 37.03 ? 508 CNC A C4 1 HETATM 3235 C C5 . CNC I 3 . ? -11.230 49.631 13.754 1.00 44.54 ? 508 CNC A C5 1 HETATM 3236 C C35 . CNC I 3 . ? -10.943 50.192 12.342 1.00 39.89 ? 508 CNC A C35 1 HETATM 3237 C C6 . CNC I 3 . ? -10.282 49.235 14.669 1.00 46.16 ? 508 CNC A C6 1 HETATM 3238 C C7 . CNC I 3 . ? -8.737 49.199 14.479 1.00 46.52 ? 508 CNC A C7 1 HETATM 3239 C C36 . CNC I 3 . ? -8.037 48.547 13.226 1.00 26.75 ? 508 CNC A C36 1 HETATM 3240 C C37 . CNC I 3 . ? -8.236 50.694 14.552 1.00 36.76 ? 508 CNC A C37 1 HETATM 3241 C C38 . CNC I 3 . ? -6.783 50.997 14.303 1.00 41.06 ? 508 CNC A C38 1 HETATM 3242 O O39 . CNC I 3 . ? -5.896 50.539 15.042 1.00 52.16 ? 508 CNC A O39 1 HETATM 3243 N N40 . CNC I 3 . ? -6.468 51.752 13.296 1.00 46.23 ? 508 CNC A N40 1 HETATM 3244 C C8 . CNC I 3 . ? -8.245 48.536 15.821 1.00 39.61 ? 508 CNC A C8 1 HETATM 3245 C C41 . CNC I 3 . ? -7.755 47.035 15.612 1.00 35.78 ? 508 CNC A C41 1 HETATM 3246 C C42 . CNC I 3 . ? -6.222 46.805 15.592 1.00 39.03 ? 508 CNC A C42 1 HETATM 3247 C C43 . CNC I 3 . ? -5.875 45.353 15.850 1.00 35.44 ? 508 CNC A C43 1 HETATM 3248 O O44 . CNC I 3 . ? -6.185 44.463 15.054 1.00 39.84 ? 508 CNC A O44 1 HETATM 3249 N N45 . CNC I 3 . ? -5.244 45.114 16.960 1.00 39.87 ? 508 CNC A N45 1 HETATM 3250 C C9 . CNC I 3 . ? -9.481 48.646 16.709 1.00 46.89 ? 508 CNC A C9 1 HETATM 3251 C C10 . CNC I 3 . ? -9.362 48.670 18.091 1.00 46.09 ? 508 CNC A C10 1 HETATM 3252 C C11 . CNC I 3 . ? -10.369 48.704 19.011 1.00 46.21 ? 508 CNC A C11 1 HETATM 3253 C C12 . CNC I 3 . ? -10.143 48.719 20.523 1.00 53.89 ? 508 CNC A C12 1 HETATM 3254 C C46 . CNC I 3 . ? -9.987 50.217 20.924 1.00 49.34 ? 508 CNC A C46 1 HETATM 3255 C C47 . CNC I 3 . ? -8.820 48.041 21.007 1.00 40.84 ? 508 CNC A C47 1 HETATM 3256 C C13 . CNC I 3 . ? -11.522 48.281 21.058 1.00 44.92 ? 508 CNC A C13 1 HETATM 3257 C C48 . CNC I 3 . ? -11.468 46.724 21.257 1.00 39.54 ? 508 CNC A C48 1 HETATM 3258 C C49 . CNC I 3 . ? -11.194 46.208 22.698 1.00 57.51 ? 508 CNC A C49 1 HETATM 3259 C C50 . CNC I 3 . ? -12.365 46.383 23.604 1.00 64.23 ? 508 CNC A C50 1 HETATM 3260 O O51 . CNC I 3 . ? -13.424 45.906 23.265 1.00 60.52 ? 508 CNC A O51 1 HETATM 3261 N N52 . CNC I 3 . ? -12.223 47.024 24.723 1.00 68.20 ? 508 CNC A N52 1 HETATM 3262 C C14 . CNC I 3 . ? -12.455 48.654 19.887 1.00 43.47 ? 508 CNC A C14 1 HETATM 3263 C C15 . CNC I 3 . ? -13.832 48.873 20.016 1.00 45.87 ? 508 CNC A C15 1 HETATM 3264 C C53 . CNC I 3 . ? -14.387 48.748 21.441 1.00 33.87 ? 508 CNC A C53 1 HETATM 3265 C C16 . CNC I 3 . ? -14.647 48.950 18.788 1.00 44.04 ? 508 CNC A C16 1 HETATM 3266 C C17 . CNC I 3 . ? -16.176 49.232 18.699 1.00 35.54 ? 508 CNC A C17 1 HETATM 3267 C C54 . CNC I 3 . ? -16.422 50.658 19.242 1.00 24.59 ? 508 CNC A C54 1 HETATM 3268 C C55 . CNC I 3 . ? -17.156 48.271 19.447 1.00 34.76 ? 508 CNC A C55 1 HETATM 3269 C C56 . CNC I 3 . ? -16.830 46.772 19.256 1.00 38.15 ? 508 CNC A C56 1 HETATM 3270 C C57 . CNC I 3 . ? -17.801 45.932 20.065 1.00 45.98 ? 508 CNC A C57 1 HETATM 3271 O O58 . CNC I 3 . ? -17.598 45.713 21.246 1.00 42.48 ? 508 CNC A O58 1 HETATM 3272 N N59 . CNC I 3 . ? -18.869 45.481 19.392 1.00 45.61 ? 508 CNC A N59 1 HETATM 3273 C C18 . CNC I 3 . ? -16.439 49.136 17.150 1.00 41.45 ? 508 CNC A C18 1 HETATM 3274 C C60 . CNC I 3 . ? -17.665 49.917 16.578 1.00 31.15 ? 508 CNC A C60 1 HETATM 3275 C C61 . CNC I 3 . ? -18.648 49.193 15.717 1.00 33.44 ? 508 CNC A C61 1 HETATM 3276 O O63 . CNC I 3 . ? -19.290 49.701 14.768 1.00 41.10 ? 508 CNC A O63 1 HETATM 3277 N N62 . CNC I 3 . ? -18.795 47.947 16.027 1.00 33.06 ? 508 CNC A N62 1 HETATM 3278 C C19 . CNC I 3 . ? -15.082 49.574 16.558 1.00 35.05 ? 508 CNC A C19 1 HETATM 3279 C C1P . CNC I 3 . ? -19.949 44.640 19.986 1.00 47.24 ? 508 CNC A C1P 1 HETATM 3280 C C2P . CNC I 3 . ? -19.508 43.175 20.201 1.00 51.47 ? 508 CNC A C2P 1 HETATM 3281 C C3P . CNC I 3 . ? -20.687 42.395 20.737 1.00 48.87 ? 508 CNC A C3P 1 HETATM 3282 O O3 . CNC I 3 . ? -19.030 42.501 18.988 1.00 47.00 ? 508 CNC A O3 1 HETATM 3283 O O4 . CNC I 3 . ? -17.513 41.862 17.188 1.00 49.52 1 508 CNC A O4 1 HETATM 3284 O O5 . CNC I 3 . ? -17.400 40.788 19.450 1.00 57.45 ? 508 CNC A O5 1 HETATM 3285 P P . CNC I 3 . ? -17.566 41.979 18.636 1.00 44.17 ? 508 CNC A P 1 HETATM 3286 O O2 . CNC I 3 . ? -16.635 43.203 19.173 1.00 60.21 ? 508 CNC A O2 1 HETATM 3287 C C3R . CNC I 3 . ? -15.309 42.759 19.456 1.00 49.13 ? 508 CNC A C3R 1 HETATM 3288 C C2R . CNC I 3 . ? -14.477 42.792 18.213 1.00 48.79 ? 508 CNC A C2R 1 HETATM 3289 O O7R . CNC I 3 . ? -15.046 43.694 17.347 1.00 49.42 ? 508 CNC A O7R 1 HETATM 3290 C C1R . CNC I 3 . ? -13.106 43.298 18.603 1.00 43.55 ? 508 CNC A C1R 1 HETATM 3291 O O6R . CNC I 3 . ? -13.295 43.876 19.879 1.00 45.33 ? 508 CNC A O6R 1 HETATM 3292 C C4R . CNC I 3 . ? -14.627 43.706 20.424 1.00 48.14 ? 508 CNC A C4R 1 HETATM 3293 C C5R . CNC I 3 . ? -14.510 43.096 21.794 1.00 40.24 ? 508 CNC A C5R 1 HETATM 3294 O O8R . CNC I 3 . ? -13.725 41.882 21.756 1.00 49.84 ? 508 CNC A O8R 1 HETATM 3295 N N1B . CNC I 3 . ? -12.714 44.380 17.662 1.00 43.70 ? 508 CNC A N1B 1 HETATM 3296 C C8B . CNC I 3 . ? -12.184 44.287 16.349 1.00 36.06 ? 508 CNC A C8B 1 HETATM 3297 C C2B . CNC I 3 . ? -12.808 45.693 17.895 1.00 41.93 ? 508 CNC A C2B 1 HETATM 3298 N N3B . CNC I 3 . ? -12.407 46.466 16.900 1.00 29.71 ? 508 CNC A N3B 1 HETATM 3299 C C9B . CNC I 3 . ? -12.003 45.616 15.898 1.00 35.64 ? 508 CNC A C9B 1 HETATM 3300 C C4B . CNC I 3 . ? -11.479 45.900 14.601 1.00 33.85 ? 508 CNC A C4B 1 HETATM 3301 C C5B . CNC I 3 . ? -11.144 44.834 13.784 1.00 41.41 ? 508 CNC A C5B 1 HETATM 3302 C C5M . CNC I 3 . ? -10.586 45.151 12.395 1.00 29.61 ? 508 CNC A C5M 1 HETATM 3303 C C6B . CNC I 3 . ? -11.328 43.461 14.242 1.00 44.85 ? 508 CNC A C6B 1 HETATM 3304 C C6M . CNC I 3 . ? -10.955 42.302 13.323 1.00 38.27 ? 508 CNC A C6M 1 HETATM 3305 C C7B . CNC I 3 . ? -11.845 43.166 15.510 1.00 46.15 ? 508 CNC A C7B 1 HETATM 3306 N N1A . CNC I 3 . ? -12.113 52.006 17.148 1.00 72.66 ? 508 CNC A N1A 1 HETATM 3307 C C1A . CNC I 3 . ? -12.204 50.863 17.030 1.00 69.56 ? 508 CNC A C1A 1 HETATM 3308 CA CA . CA J 4 . ? 5.197 33.694 17.075 1.00 101.69 ? 509 CA A CA 1 HETATM 3309 C C1 . PEG K 5 . ? -39.765 60.132 23.712 1.00 70.41 ? 510 PEG A C1 1 HETATM 3310 O O1 . PEG K 5 . ? -40.825 61.066 23.925 1.00 79.95 ? 510 PEG A O1 1 HETATM 3311 C C2 . PEG K 5 . ? -38.508 60.858 23.244 1.00 68.50 ? 510 PEG A C2 1 HETATM 3312 O O2 . PEG K 5 . ? -37.696 59.931 22.530 1.00 71.91 ? 510 PEG A O2 1 HETATM 3313 C C3 . PEG K 5 . ? -37.201 60.471 21.308 1.00 61.42 ? 510 PEG A C3 1 HETATM 3314 C C4 . PEG K 5 . ? -37.270 59.382 20.242 1.00 57.00 ? 510 PEG A C4 1 HETATM 3315 O O4 . PEG K 5 . ? -36.914 59.919 18.964 1.00 55.48 ? 510 PEG A O4 1 HETATM 3316 C C1 . PEG L 5 . ? -42.886 57.094 22.323 1.00 81.10 ? 511 PEG A C1 1 HETATM 3317 O O1 . PEG L 5 . ? -42.411 58.399 22.677 1.00 78.65 ? 511 PEG A O1 1 HETATM 3318 C C2 . PEG L 5 . ? -43.306 57.057 20.856 1.00 77.96 ? 511 PEG A C2 1 HETATM 3319 O O2 . PEG L 5 . ? -42.213 57.428 20.014 1.00 74.40 ? 511 PEG A O2 1 HETATM 3320 C C3 . PEG L 5 . ? -42.534 57.312 18.627 1.00 68.98 ? 511 PEG A C3 1 HETATM 3321 C C4 . PEG L 5 . ? -41.594 58.182 17.795 1.00 73.13 ? 511 PEG A C4 1 HETATM 3322 O O4 . PEG L 5 . ? -40.235 57.770 17.979 1.00 76.04 ? 511 PEG A O4 1 HETATM 3323 C C1 . PEG M 5 . ? -39.040 46.081 11.967 1.00 77.62 ? 512 PEG A C1 1 HETATM 3324 O O1 . PEG M 5 . ? -39.425 45.999 13.344 1.00 76.90 ? 512 PEG A O1 1 HETATM 3325 C C2 . PEG M 5 . ? -40.034 46.956 11.213 1.00 81.24 ? 512 PEG A C2 1 HETATM 3326 O O2 . PEG M 5 . ? -39.767 46.897 9.812 1.00 80.58 ? 512 PEG A O2 1 HETATM 3327 C C3 . PEG M 5 . ? -40.745 47.622 9.067 1.00 81.40 ? 512 PEG A C3 1 HETATM 3328 C C4 . PEG M 5 . ? -40.330 47.711 7.604 1.00 79.72 ? 512 PEG A C4 1 HETATM 3329 O O4 . PEG M 5 . ? -40.381 46.409 7.011 1.00 87.65 ? 512 PEG A O4 1 HETATM 3330 C C1 . PEG N 5 . ? -38.212 44.555 2.141 1.00 90.69 ? 513 PEG A C1 1 HETATM 3331 O O1 . PEG N 5 . ? -39.574 44.913 2.401 1.00 86.22 ? 513 PEG A O1 1 HETATM 3332 C C2 . PEG N 5 . ? -37.596 45.523 1.135 1.00 92.73 ? 513 PEG A C2 1 HETATM 3333 O O2 . PEG N 5 . ? -36.213 45.212 0.959 1.00 90.90 ? 513 PEG A O2 1 HETATM 3334 C C3 . PEG N 5 . ? -35.578 46.024 -0.030 1.00 84.83 ? 513 PEG A C3 1 HETATM 3335 C C4 . PEG N 5 . ? -34.075 45.762 -0.003 1.00 79.82 ? 513 PEG A C4 1 HETATM 3336 O O4 . PEG N 5 . ? -33.445 46.326 -1.159 1.00 81.24 ? 513 PEG A O4 1 HETATM 3337 C C1 . PEG O 5 . ? -40.356 48.552 26.285 1.00 71.92 ? 514 PEG A C1 1 HETATM 3338 O O1 . PEG O 5 . ? -41.179 48.103 25.203 1.00 74.07 ? 514 PEG A O1 1 HETATM 3339 C C2 . PEG O 5 . ? -40.201 50.070 26.238 1.00 66.92 ? 514 PEG A C2 1 HETATM 3340 O O2 . PEG O 5 . ? -39.577 50.458 25.014 1.00 66.35 ? 514 PEG A O2 1 HETATM 3341 C C3 . PEG O 5 . ? -39.426 51.874 24.903 1.00 53.01 ? 514 PEG A C3 1 HETATM 3342 C C4 . PEG O 5 . ? -38.742 52.215 23.582 1.00 59.44 ? 514 PEG A C4 1 HETATM 3343 O O4 . PEG O 5 . ? -39.600 51.891 22.482 1.00 60.21 ? 514 PEG A O4 1 HETATM 3344 C C1 . PEG P 5 . ? -25.097 70.089 27.569 1.00 59.94 ? 515 PEG A C1 1 HETATM 3345 O O1 . PEG P 5 . ? -24.485 70.479 26.332 1.00 65.37 ? 515 PEG A O1 1 HETATM 3346 C C2 . PEG P 5 . ? -26.307 70.972 27.868 1.00 66.01 ? 515 PEG A C2 1 HETATM 3347 O O2 . PEG P 5 . ? -26.040 72.311 27.448 1.00 79.90 ? 515 PEG A O2 1 HETATM 3348 C C3 . PEG P 5 . ? -27.048 73.242 27.843 1.00 68.56 ? 515 PEG A C3 1 HETATM 3349 C C4 . PEG P 5 . ? -26.715 74.627 27.290 1.00 68.62 ? 515 PEG A C4 1 HETATM 3350 O O4 . PEG P 5 . ? -26.911 74.667 25.870 1.00 64.74 ? 515 PEG A O4 1 HETATM 3351 C C1 . PEG Q 5 . ? -13.162 51.063 -1.750 1.00 91.61 ? 516 PEG A C1 1 HETATM 3352 O O1 . PEG Q 5 . ? -11.949 51.719 -2.135 1.00 94.75 ? 516 PEG A O1 1 HETATM 3353 C C2 . PEG Q 5 . ? -12.942 50.310 -0.444 1.00 93.89 ? 516 PEG A C2 1 HETATM 3354 O O2 . PEG Q 5 . ? -12.173 51.142 0.420 1.00 98.97 ? 516 PEG A O2 1 HETATM 3355 C C3 . PEG Q 5 . ? -12.642 51.115 1.765 1.00 89.76 ? 516 PEG A C3 1 HETATM 3356 C C4 . PEG Q 5 . ? -12.058 52.318 2.496 1.00 80.65 ? 516 PEG A C4 1 HETATM 3357 O O4 . PEG Q 5 . ? -12.840 52.606 3.660 1.00 73.67 ? 516 PEG A O4 1 HETATM 3358 C C1 . PEG R 5 . ? -14.929 39.581 5.603 1.00 84.69 ? 517 PEG A C1 1 HETATM 3359 O O1 . PEG R 5 . ? -14.234 40.267 4.557 1.00 85.85 ? 517 PEG A O1 1 HETATM 3360 C C2 . PEG R 5 . ? -13.946 39.197 6.703 1.00 80.68 ? 517 PEG A C2 1 HETATM 3361 O O2 . PEG R 5 . ? -14.632 38.486 7.732 1.00 76.39 ? 517 PEG A O2 1 HETATM 3362 C C3 . PEG R 5 . ? -13.745 37.607 8.423 1.00 78.47 ? 517 PEG A C3 1 HETATM 3363 C C4 . PEG R 5 . ? -14.483 36.904 9.555 1.00 77.25 ? 517 PEG A C4 1 HETATM 3364 O O4 . PEG R 5 . ? -13.677 35.825 10.044 1.00 77.57 ? 517 PEG A O4 1 HETATM 3365 C C1 . PEG S 5 . ? -5.357 42.611 33.821 1.00 96.93 ? 518 PEG A C1 1 HETATM 3366 O O1 . PEG S 5 . ? -6.002 41.334 33.877 1.00 97.29 ? 518 PEG A O1 1 HETATM 3367 C C2 . PEG S 5 . ? -4.068 42.579 34.636 1.00 96.54 ? 518 PEG A C2 1 HETATM 3368 O O2 . PEG S 5 . ? -3.576 43.910 34.778 1.00 95.35 ? 518 PEG A O2 1 HETATM 3369 C C3 . PEG S 5 . ? -2.460 43.988 35.662 1.00 93.15 ? 518 PEG A C3 1 HETATM 3370 C C4 . PEG S 5 . ? -2.142 45.455 35.935 1.00 87.70 ? 518 PEG A C4 1 HETATM 3371 O O4 . PEG S 5 . ? -0.881 45.561 36.604 1.00 83.86 ? 518 PEG A O4 1 HETATM 3372 C C1 . PEG T 5 . ? -10.323 55.838 11.606 1.00 55.29 ? 519 PEG A C1 1 HETATM 3373 O O1 . PEG T 5 . ? -10.622 57.121 11.049 1.00 59.81 ? 519 PEG A O1 1 HETATM 3374 C C2 . PEG T 5 . ? -10.667 55.843 13.088 1.00 65.34 ? 519 PEG A C2 1 HETATM 3375 O O2 . PEG T 5 . ? -10.256 54.620 13.688 1.00 70.08 ? 519 PEG A O2 1 HETATM 3376 C C3 . PEG T 5 . ? -10.657 54.556 15.055 1.00 81.89 ? 519 PEG A C3 1 HETATM 3377 C C4 . PEG T 5 . ? -9.679 53.702 15.853 1.00 79.12 ? 519 PEG A C4 1 HETATM 3378 O O4 . PEG T 5 . ? -8.734 54.542 16.522 1.00 78.56 ? 519 PEG A O4 1 HETATM 3379 C C1 . PEG U 5 . ? -23.014 39.040 18.396 1.00 77.62 ? 520 PEG A C1 1 HETATM 3380 O O1 . PEG U 5 . ? -22.963 38.928 16.968 1.00 61.69 ? 520 PEG A O1 1 HETATM 3381 C C2 . PEG U 5 . ? -23.375 37.696 19.017 1.00 84.90 ? 520 PEG A C2 1 HETATM 3382 O O2 . PEG U 5 . ? -22.438 36.718 18.574 1.00 95.68 ? 520 PEG A O2 1 HETATM 3383 C C3 . PEG U 5 . ? -22.748 35.395 19.004 1.00 89.43 ? 520 PEG A C3 1 HETATM 3384 C C4 . PEG U 5 . ? -22.052 34.399 18.083 1.00 89.97 ? 520 PEG A C4 1 HETATM 3385 O O4 . PEG U 5 . ? -20.675 34.759 17.927 1.00 90.62 ? 520 PEG A O4 1 HETATM 3386 O O . HOH V 6 . ? -4.769 45.044 20.124 1.00 43.68 ? 601 HOH A O 1 HETATM 3387 O O . HOH V 6 . ? -6.770 43.923 12.426 1.00 37.22 ? 602 HOH A O 1 HETATM 3388 O O . HOH V 6 . ? -18.436 45.432 16.631 1.00 43.30 ? 603 HOH A O 1 HETATM 3389 O O . HOH V 6 . ? -27.647 51.911 10.554 1.00 30.71 ? 604 HOH A O 1 HETATM 3390 O O . HOH V 6 . ? 3.334 37.478 19.574 1.00 29.31 ? 605 HOH A O 1 HETATM 3391 O O . HOH V 6 . ? -19.376 49.515 10.814 1.00 33.07 ? 606 HOH A O 1 HETATM 3392 O O . HOH V 6 . ? -37.807 62.373 35.742 1.00 33.91 ? 607 HOH A O 1 HETATM 3393 O O . HOH V 6 . ? -16.096 46.744 4.733 1.00 47.33 ? 608 HOH A O 1 HETATM 3394 O O . HOH V 6 . ? -22.148 52.680 11.742 1.00 32.05 ? 609 HOH A O 1 HETATM 3395 O O . HOH V 6 . ? 1.858 56.295 4.479 1.00 65.73 ? 610 HOH A O 1 HETATM 3396 O O . HOH V 6 . ? -19.783 48.050 -0.475 1.00 40.13 ? 611 HOH A O 1 HETATM 3397 O O . HOH V 6 . ? -15.336 53.852 17.674 1.00 51.41 ? 612 HOH A O 1 HETATM 3398 O O . HOH V 6 . ? -36.410 54.603 14.961 1.00 46.74 ? 613 HOH A O 1 HETATM 3399 O O . HOH V 6 . ? -30.146 29.092 32.401 1.00 63.47 ? 614 HOH A O 1 HETATM 3400 O O . HOH V 6 . ? -30.705 32.734 34.625 1.00 59.73 ? 615 HOH A O 1 HETATM 3401 O O . HOH V 6 . ? -16.687 51.483 23.212 1.00 32.75 ? 616 HOH A O 1 HETATM 3402 O O . HOH V 6 . ? -11.959 53.800 26.397 1.00 50.72 ? 617 HOH A O 1 HETATM 3403 O O . HOH V 6 . ? 2.177 55.341 10.001 1.00 68.38 ? 618 HOH A O 1 HETATM 3404 O O . HOH V 6 . ? 3.870 59.277 5.033 1.00 69.44 ? 619 HOH A O 1 HETATM 3405 O O . HOH V 6 . ? -8.519 42.438 9.927 1.00 41.90 ? 620 HOH A O 1 HETATM 3406 O O . HOH V 6 . ? -20.729 50.333 8.753 1.00 38.21 ? 621 HOH A O 1 HETATM 3407 O O . HOH V 6 . ? -13.166 67.524 17.291 1.00 69.53 ? 622 HOH A O 1 HETATM 3408 O O . HOH V 6 . ? -13.354 56.045 6.141 1.00 34.57 ? 623 HOH A O 1 HETATM 3409 O O . HOH V 6 . ? -24.502 47.074 16.176 1.00 42.92 ? 624 HOH A O 1 HETATM 3410 O O . HOH V 6 . ? -23.852 66.238 5.898 1.00 54.41 ? 625 HOH A O 1 HETATM 3411 O O . HOH V 6 . ? -8.286 49.269 1.508 1.00 54.46 ? 626 HOH A O 1 HETATM 3412 O O . HOH V 6 . ? -37.662 49.559 29.552 1.00 50.96 ? 627 HOH A O 1 HETATM 3413 O O . HOH V 6 . ? -1.204 56.467 1.245 1.00 72.17 ? 628 HOH A O 1 HETATM 3414 O O . HOH V 6 . ? -19.153 41.295 28.888 1.00 46.94 ? 629 HOH A O 1 HETATM 3415 O O . HOH V 6 . ? -34.414 60.901 1.778 1.00 71.74 ? 630 HOH A O 1 HETATM 3416 O O . HOH V 6 . ? -18.980 38.404 18.317 1.00 51.74 ? 631 HOH A O 1 HETATM 3417 O O . HOH V 6 . ? -7.701 41.745 28.696 1.00 65.47 ? 632 HOH A O 1 HETATM 3418 O O . HOH V 6 . ? -20.965 67.702 5.601 1.00 59.49 ? 633 HOH A O 1 HETATM 3419 O O . HOH V 6 . ? -31.051 30.817 33.536 1.00 55.77 ? 634 HOH A O 1 HETATM 3420 O O . HOH V 6 . ? -13.504 66.812 6.395 1.00 50.81 ? 635 HOH A O 1 HETATM 3421 O O . HOH V 6 . ? -1.397 46.325 -1.955 1.00 65.52 ? 636 HOH A O 1 HETATM 3422 O O . HOH V 6 . ? -20.949 39.334 10.422 1.00 56.89 ? 637 HOH A O 1 HETATM 3423 O O . HOH V 6 . ? -16.143 64.782 19.041 1.00 54.59 ? 638 HOH A O 1 HETATM 3424 O O . HOH V 6 . ? -34.344 52.575 37.990 1.00 67.97 ? 639 HOH A O 1 HETATM 3425 O O . HOH V 6 . ? -38.795 28.199 21.140 1.00 86.35 ? 640 HOH A O 1 HETATM 3426 O O . HOH V 6 . ? -10.472 64.037 16.725 1.00 71.67 ? 641 HOH A O 1 HETATM 3427 O O . HOH V 6 . ? 2.384 54.958 24.599 1.00 79.29 ? 642 HOH A O 1 HETATM 3428 O O . HOH V 6 . ? 0.697 59.511 15.126 1.00 76.13 ? 643 HOH A O 1 HETATM 3429 O O . HOH V 6 . ? -42.274 56.339 34.292 1.00 76.82 ? 644 HOH A O 1 HETATM 3430 O O . HOH V 6 . ? -21.141 52.432 14.086 1.00 40.32 ? 645 HOH A O 1 HETATM 3431 O O . HOH V 6 . ? -21.511 52.859 8.994 1.00 41.78 ? 646 HOH A O 1 HETATM 3432 O O . HOH V 6 . ? -12.758 63.368 28.886 1.00 73.03 ? 647 HOH A O 1 HETATM 3433 O O . HOH V 6 . ? -26.561 28.781 33.053 1.00 70.28 ? 648 HOH A O 1 HETATM 3434 O O . HOH V 6 . ? -12.159 48.812 28.041 1.00 71.37 ? 649 HOH A O 1 HETATM 3435 O O . HOH V 6 . ? -23.107 35.444 8.743 1.00 52.36 ? 650 HOH A O 1 HETATM 3436 O O . HOH V 6 . ? -36.450 63.643 26.107 1.00 56.10 ? 651 HOH A O 1 HETATM 3437 O O . HOH V 6 . ? -37.348 47.588 31.845 1.00 71.98 ? 652 HOH A O 1 HETATM 3438 O O . HOH V 6 . ? -15.506 51.937 25.572 1.00 44.61 ? 653 HOH A O 1 HETATM 3439 O O . HOH V 6 . ? -32.720 53.794 39.459 1.00 61.90 ? 654 HOH A O 1 HETATM 3440 O O . HOH V 6 . ? -7.849 42.838 30.978 1.00 65.62 ? 655 HOH A O 1 HETATM 3441 O O . HOH V 6 . ? -12.017 64.120 26.876 1.00 65.00 ? 656 HOH A O 1 HETATM 3442 O O . HOH V 6 . ? -41.421 51.759 11.247 1.00 79.02 ? 657 HOH A O 1 HETATM 3443 O O . HOH V 6 . ? 1.180 56.788 -0.201 1.00 73.80 ? 658 HOH A O 1 HETATM 3444 O O . HOH V 6 . ? -0.433 45.406 -11.408 1.00 86.98 ? 659 HOH A O 1 HETATM 3445 O O . HOH V 6 . ? 3.981 53.581 25.620 1.00 73.73 ? 660 HOH A O 1 HETATM 3446 O O . HOH V 6 . ? -32.413 61.288 21.660 1.00 46.52 ? 661 HOH A O 1 HETATM 3447 O O . HOH V 6 . ? -22.635 27.314 14.005 1.00 64.09 ? 662 HOH A O 1 HETATM 3448 O O . HOH V 6 . ? -39.875 53.322 10.149 1.00 67.27 ? 663 HOH A O 1 HETATM 3449 O O . HOH V 6 . ? -13.256 51.729 27.129 1.00 48.73 ? 664 HOH A O 1 HETATM 3450 O O . HOH V 6 . ? -3.952 36.322 21.636 1.00 54.44 ? 665 HOH A O 1 HETATM 3451 O O . HOH V 6 . ? -10.743 66.831 17.830 1.00 75.34 ? 666 HOH A O 1 HETATM 3452 O O . HOH V 6 . ? -31.876 57.789 -2.709 1.00 56.26 ? 667 HOH A O 1 HETATM 3453 O O . HOH V 6 . ? -15.504 40.459 15.931 1.00 68.35 ? 668 HOH A O 1 HETATM 3454 O O . HOH V 6 . ? -34.015 44.504 -16.805 1.00 80.53 ? 669 HOH A O 1 HETATM 3455 O O . HOH V 6 . ? -35.525 36.086 30.643 1.00 43.33 ? 670 HOH A O 1 HETATM 3456 O O . HOH V 6 . ? -31.666 32.354 2.155 1.00 48.58 ? 671 HOH A O 1 HETATM 3457 O O . HOH V 6 . ? -36.495 38.316 34.871 1.00 76.52 ? 672 HOH A O 1 HETATM 3458 O O . HOH V 6 . ? -14.918 66.773 26.113 1.00 79.96 ? 673 HOH A O 1 HETATM 3459 O O . HOH V 6 . ? -20.848 27.726 15.448 1.00 72.39 ? 674 HOH A O 1 HETATM 3460 O O . HOH V 6 . ? -14.816 59.918 0.429 1.00 68.46 ? 675 HOH A O 1 HETATM 3461 O O . HOH V 6 . ? -39.287 53.684 6.810 1.00 95.12 ? 676 HOH A O 1 HETATM 3462 O O . HOH V 6 . ? -37.291 37.849 32.425 1.00 73.15 ? 677 HOH A O 1 HETATM 3463 O O . HOH V 6 . ? -31.636 45.771 38.809 1.00 74.80 ? 678 HOH A O 1 HETATM 3464 O O . HOH V 6 . ? 10.165 48.945 25.250 1.00 39.40 ? 679 HOH A O 1 HETATM 3465 O O . HOH V 6 . ? -38.021 63.036 6.254 1.00 60.27 ? 680 HOH A O 1 HETATM 3466 O O . HOH V 6 . ? -33.656 56.191 39.408 1.00 56.24 ? 681 HOH A O 1 HETATM 3467 O O . HOH V 6 . ? -3.385 40.983 28.237 1.00 65.32 ? 682 HOH A O 1 HETATM 3468 O O . HOH V 6 . ? -18.701 57.074 39.218 1.00 73.95 ? 683 HOH A O 1 HETATM 3469 O O . HOH V 6 . ? 10.718 55.087 18.811 1.00 57.90 ? 684 HOH A O 1 HETATM 3470 O O . HOH V 6 . ? -7.769 44.086 22.690 1.00 59.36 ? 685 HOH A O 1 HETATM 3471 O O . HOH V 6 . ? -3.982 65.081 9.091 1.00 91.79 ? 686 HOH A O 1 HETATM 3472 O O . HOH V 6 . ? -20.153 36.560 31.668 1.00 82.46 ? 687 HOH A O 1 HETATM 3473 O O . HOH V 6 . ? -0.486 34.859 9.842 1.00 69.74 ? 688 HOH A O 1 HETATM 3474 O O . HOH V 6 . ? -22.888 70.731 16.905 1.00 56.66 ? 689 HOH A O 1 HETATM 3475 O O . HOH V 6 . ? -34.209 69.306 14.133 1.00 74.63 ? 690 HOH A O 1 HETATM 3476 O O . HOH V 6 . ? -13.575 60.778 4.235 1.00 59.33 ? 691 HOH A O 1 HETATM 3477 O O . HOH V 6 . ? -25.311 70.997 17.661 1.00 59.00 ? 692 HOH A O 1 HETATM 3478 O O . HOH V 6 . ? -38.737 41.558 10.046 1.00 54.91 ? 693 HOH A O 1 HETATM 3479 O O . HOH V 6 . ? 4.690 41.717 11.702 1.00 49.79 ? 694 HOH A O 1 HETATM 3480 O O . HOH V 6 . ? -1.125 41.373 29.654 1.00 65.92 ? 695 HOH A O 1 HETATM 3481 O O . HOH V 6 . ? -43.567 47.618 31.457 1.00 86.07 ? 696 HOH A O 1 HETATM 3482 O O . HOH V 6 . ? -14.010 58.903 2.919 1.00 71.99 ? 697 HOH A O 1 HETATM 3483 O O . HOH V 6 . ? -38.573 39.491 31.181 1.00 72.83 ? 698 HOH A O 1 HETATM 3484 O O . HOH V 6 . ? -15.730 38.427 17.587 1.00 58.42 ? 699 HOH A O 1 HETATM 3485 O O . HOH V 6 . ? -7.352 45.693 24.817 1.00 47.59 ? 700 HOH A O 1 HETATM 3486 O O . HOH V 6 . ? -32.667 22.335 20.028 1.00 58.15 ? 701 HOH A O 1 HETATM 3487 O O . HOH V 6 . ? -0.796 39.781 -13.898 1.00 74.77 ? 702 HOH A O 1 HETATM 3488 O O . HOH V 6 . ? -18.166 36.929 30.157 1.00 74.77 ? 703 HOH A O 1 HETATM 3489 O O . HOH V 6 . ? -39.213 60.168 6.092 1.00 74.45 ? 704 HOH A O 1 HETATM 3490 O O . HOH V 6 . ? -11.853 67.533 15.237 1.00 102.18 ? 705 HOH A O 1 HETATM 3491 O O . HOH V 6 . ? -37.359 35.883 34.936 1.00 70.33 ? 706 HOH A O 1 HETATM 3492 O O . HOH V 6 . ? -32.780 59.804 -5.789 1.00 72.46 ? 707 HOH A O 1 HETATM 3493 O O . HOH V 6 . ? 7.219 36.284 18.097 1.00 69.90 ? 708 HOH A O 1 HETATM 3494 O O . HOH V 6 . ? -14.862 38.350 21.451 1.00 81.63 ? 709 HOH A O 1 HETATM 3495 O O . HOH V 6 . ? -13.018 38.571 22.735 1.00 76.56 ? 710 HOH A O 1 HETATM 3496 O O . HOH V 6 . ? -24.321 44.898 14.595 1.00 51.18 ? 711 HOH A O 1 HETATM 3497 O O . HOH V 6 . ? -26.696 49.085 12.936 1.00 34.27 ? 712 HOH A O 1 HETATM 3498 O O . HOH V 6 . ? -17.028 40.990 22.963 1.00 60.32 ? 713 HOH A O 1 HETATM 3499 O O . HOH V 6 . ? -14.258 56.235 14.059 1.00 61.49 ? 714 HOH A O 1 HETATM 3500 O O . HOH V 6 . ? -28.913 33.507 35.914 1.00 71.03 ? 715 HOH A O 1 HETATM 3501 O O . HOH V 6 . ? -13.904 58.949 33.110 1.00 47.56 ? 716 HOH A O 1 HETATM 3502 O O . HOH V 6 . ? -15.354 57.771 15.773 1.00 55.35 ? 717 HOH A O 1 HETATM 3503 O O . HOH V 6 . ? -28.235 67.896 -0.403 1.00 61.30 ? 718 HOH A O 1 HETATM 3504 O O . HOH V 6 . ? -27.570 46.871 12.252 1.00 36.80 ? 719 HOH A O 1 HETATM 3505 O O . HOH V 6 . ? -11.794 45.257 8.248 1.00 47.95 ? 720 HOH A O 1 HETATM 3506 O O . HOH V 6 . ? -13.321 46.341 5.890 1.00 22.29 ? 721 HOH A O 1 HETATM 3507 O O . HOH V 6 . ? -10.756 42.462 22.465 1.00 49.59 ? 722 HOH A O 1 HETATM 3508 O O . HOH V 6 . ? -11.224 41.608 20.443 1.00 57.33 ? 723 HOH A O 1 HETATM 3509 O O . HOH V 6 . ? 1.087 34.601 13.114 1.00 78.46 ? 724 HOH A O 1 HETATM 3510 O O . HOH V 6 . ? 4.910 33.422 19.484 1.00 63.67 ? 725 HOH A O 1 HETATM 3511 O O . HOH V 6 . ? 1.735 35.508 23.688 1.00 68.57 ? 726 HOH A O 1 HETATM 3512 O O . HOH V 6 . ? -11.227 42.828 9.059 1.00 42.04 ? 727 HOH A O 1 HETATM 3513 O O . HOH V 6 . ? -17.974 36.638 5.061 1.00 50.76 ? 728 HOH A O 1 HETATM 3514 O O . HOH V 6 . ? -23.347 71.505 8.513 1.00 56.78 ? 729 HOH A O 1 HETATM 3515 O O . HOH V 6 . ? -23.922 69.963 6.892 1.00 64.82 ? 730 HOH A O 1 HETATM 3516 O O . HOH V 6 . ? -11.146 44.972 31.279 1.00 57.75 ? 731 HOH A O 1 HETATM 3517 O O . HOH V 6 . ? -4.534 38.307 35.426 1.00 70.87 ? 732 HOH A O 1 HETATM 3518 O O . HOH V 6 . ? -18.835 34.154 15.741 1.00 66.51 ? 733 HOH A O 1 HETATM 3519 O O . HOH V 6 . ? -16.842 39.527 21.243 1.00 82.52 ? 734 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 . GLU A 24 ? 0.5601 0.4837 0.4554 0.0801 -0.0599 0.0517 1 GLU A N 2 C CA . GLU A 24 ? 0.6266 0.5563 0.5147 0.0865 -0.0675 0.0545 1 GLU A CA 3 C C . GLU A 24 ? 0.6264 0.5809 0.5289 0.0772 -0.0697 0.0499 1 GLU A C 4 O O . GLU A 24 ? 0.6515 0.6077 0.5601 0.0639 -0.0637 0.0482 1 GLU A O 5 C CB . GLU A 24 ? 0.5815 0.4814 0.4414 0.0865 -0.0648 0.0625 1 GLU A CB 6 C CG . GLU A 24 ? 0.7879 0.6908 0.6340 0.0942 -0.0727 0.0660 1 GLU A CG 7 C CD . GLU A 24 ? 1.0040 0.8759 0.8199 0.0926 -0.0676 0.0747 1 GLU A CD 8 O OE1 . GLU A 24 ? 1.0148 0.8632 0.8232 0.0851 -0.0579 0.0778 1 GLU A OE1 9 O OE2 . GLU A 24 ? 1.0788 0.9498 0.8781 0.0983 -0.0731 0.0783 1 GLU A OE2 10 N N . ILE A 25 ? 0.6466 0.6204 0.5553 0.0844 -0.0788 0.0475 2 ILE A N 11 C CA . ILE A 25 ? 0.6247 0.6184 0.5441 0.0759 -0.0814 0.0425 2 ILE A CA 12 C C . ILE A 25 ? 0.7257 0.7156 0.6258 0.0808 -0.0886 0.0447 2 ILE A C 13 O O . ILE A 25 ? 0.6895 0.6843 0.5846 0.0940 -0.0984 0.0455 2 ILE A O 14 C CB . ILE A 25 ? 0.6611 0.6858 0.6093 0.0765 -0.0856 0.0348 2 ILE A CB 15 C CG1 . ILE A 25 ? 0.6994 0.7266 0.6629 0.0728 -0.0777 0.0333 2 ILE A CG1 16 C CG2 . ILE A 25 ? 0.4777 0.5190 0.4364 0.0662 -0.0871 0.0291 2 ILE A CG2 17 C CD1 . ILE A 25 ? 0.5780 0.6339 0.5696 0.0723 -0.0789 0.0266 2 ILE A CD1 18 N N . CYS A 26 ? 0.6653 0.6466 0.5540 0.0710 -0.0838 0.0457 3 CYS A N 19 C CA . CYS A 26 ? 0.6372 0.6159 0.5062 0.0741 -0.0895 0.0464 3 CYS A CA 20 C C . CYS A 26 ? 0.6320 0.6278 0.5132 0.0632 -0.0890 0.0385 3 CYS A C 21 O O . CYS A 26 ? 0.6368 0.6405 0.5378 0.0529 -0.0823 0.0349 3 CYS A O 22 C CB . CYS A 26 ? 0.6197 0.5674 0.4575 0.0740 -0.0826 0.0555 3 CYS A CB 23 S SG . CYS A 26 ? 0.7730 0.7097 0.6113 0.0564 -0.0674 0.0561 3 CYS A SG 24 N N . GLU A 27 ? 0.6013 0.6015 0.4691 0.0662 -0.0964 0.0357 4 GLU A N 25 C CA . GLU A 27 ? 0.6367 0.6513 0.5145 0.0567 -0.0965 0.0268 4 GLU A CA 26 C C . GLU A 27 ? 0.6255 0.6339 0.4759 0.0598 -0.1016 0.0257 4 GLU A C 27 O O . GLU A 27 ? 0.7302 0.7278 0.5561 0.0711 -0.1082 0.0315 4 GLU A O 28 C CB . GLU A 27 ? 0.6817 0.7249 0.5902 0.0559 -0.1041 0.0175 4 GLU A CB 29 C CG . GLU A 27 ? 0.7736 0.8314 0.6822 0.0685 -0.1190 0.0152 4 GLU A CG 30 C CD . GLU A 27 ? 0.8609 0.9474 0.8050 0.0672 -0.1237 0.0071 4 GLU A CD 31 O OE1 . GLU A 27 ? 0.8660 0.9710 0.8242 0.0608 -0.1287 -0.0028 4 GLU A OE1 32 O OE2 . GLU A 27 ? 0.9302 1.0200 0.8880 0.0720 -0.1214 0.0104 4 GLU A OE2 33 N N . VAL A 28 ? 0.5253 0.5390 0.3784 0.0504 -0.0984 0.0183 5 VAL A N 34 C CA . VAL A 28 ? 0.6009 0.6094 0.4275 0.0522 -0.1025 0.0151 5 VAL A CA 35 C C . VAL A 28 ? 0.7235 0.7499 0.5491 0.0614 -0.1206 0.0086 5 VAL A C 36 O O . VAL A 28 ? 0.7418 0.7921 0.5964 0.0586 -0.1274 -0.0004 5 VAL A O 37 C CB . VAL A 28 ? 0.6269 0.6384 0.4606 0.0401 -0.0946 0.0065 5 VAL A CB 38 C CG1 . VAL A 28 ? 0.6202 0.6273 0.4256 0.0421 -0.0994 0.0011 5 VAL A CG1 39 C CG2 . VAL A 28 ? 0.7152 0.7114 0.5504 0.0322 -0.0777 0.0128 5 VAL A CG2 40 N N . SER A 29 ? 0.7994 0.8146 0.5918 0.0723 -0.1282 0.0135 6 SER A N 41 C CA . SER A 29 ? 0.9391 0.9720 0.7272 0.0822 -0.1474 0.0072 6 SER A CA 42 C C . SER A 29 ? 0.9889 1.0378 0.7833 0.0732 -0.1524 -0.0079 6 SER A C 43 O O . SER A 29 ? 0.9496 0.9881 0.7382 0.0626 -0.1406 -0.0111 6 SER A O 44 C CB . SER A 29 ? 0.9643 0.9779 0.7096 0.0964 -0.1539 0.0169 6 SER A CB 45 O OG . SER A 29 ? 1.1167 1.1070 0.8287 0.0915 -0.1432 0.0200 6 SER A OG 46 N N . GLU A 30 ? 1.1045 1.1789 0.9120 0.0774 -0.1698 -0.0177 7 GLU A N 47 C CA . GLU A 30 ? 1.2167 1.3072 1.0328 0.0680 -0.1759 -0.0340 7 GLU A CA 48 C C . GLU A 30 ? 1.2077 1.2811 0.9815 0.0687 -0.1767 -0.0366 7 GLU A C 49 O O . GLU A 30 ? 1.2127 1.2895 0.9877 0.0586 -0.1753 -0.0493 7 GLU A O 50 C CB . GLU A 30 ? 1.3852 1.5088 1.2260 0.0722 -0.1955 -0.0445 7 GLU A CB 51 C CG . GLU A 30 ? 1.5072 1.6509 1.3935 0.0691 -0.1928 -0.0448 7 GLU A CG 52 C CD . GLU A 30 ? 1.6286 1.8080 1.5473 0.0667 -0.2081 -0.0594 7 GLU A CD 53 O OE1 . GLU A 30 ? 1.6536 1.8415 1.5671 0.0606 -0.2168 -0.0727 7 GLU A OE1 54 O OE2 . GLU A 30 ? 1.6713 1.8707 1.6212 0.0706 -0.2109 -0.0583 7 GLU A OE2 55 N N . GLU A 31 ? 1.2493 1.3024 0.9845 0.0808 -0.1778 -0.0244 8 GLU A N 56 C CA . GLU A 31 ? 1.3319 1.3650 1.0219 0.0823 -0.1757 -0.0245 8 GLU A CA 57 C C . GLU A 31 ? 1.2472 1.2590 0.9319 0.0705 -0.1525 -0.0218 8 GLU A C 58 O O . GLU A 31 ? 1.2426 1.2453 0.9052 0.0655 -0.1474 -0.0288 8 GLU A O 59 C CB . GLU A 31 ? 1.4803 1.4952 1.1293 0.0991 -0.1821 -0.0101 8 GLU A CB 60 C CG . GLU A 31 ? 1.6929 1.6839 1.2898 0.1016 -0.1782 -0.0080 8 GLU A CG 61 C CD . GLU A 31 ? 1.8386 1.8113 1.4002 0.1165 -0.1823 0.0076 8 GLU A CD 62 O OE1 . GLU A 31 ? 1.9084 1.8933 1.4883 0.1257 -0.1933 0.0126 8 GLU A OE1 63 O OE2 . GLU A 31 ? 1.8561 1.8024 1.3779 0.1169 -0.1710 0.0150 8 GLU A OE2 64 N N . ASN A 32 ? 1.1283 1.1333 0.8342 0.0664 -0.1386 -0.0124 9 ASN A N 65 C CA . ASN A 32 ? 1.1563 1.1434 0.8605 0.0564 -0.1172 -0.0086 9 ASN A CA 66 C C . ASN A 32 ? 0.9933 0.9937 0.7364 0.0431 -0.1095 -0.0184 9 ASN A C 67 O O . ASN A 32 ? 0.9386 0.9287 0.6899 0.0357 -0.0928 -0.0144 9 ASN A O 68 C CB . ASN A 32 ? 1.2226 1.1909 0.9218 0.0595 -0.1061 0.0079 9 ASN A CB 69 C CG . ASN A 32 ? 1.2676 1.2162 0.9247 0.0724 -0.1105 0.0194 9 ASN A CG 70 O OD1 . ASN A 32 ? 1.2396 1.1927 0.8740 0.0815 -0.1256 0.0158 9 ASN A OD1 71 N ND2 . ASN A 32 ? 1.2944 1.2204 0.9404 0.0731 -0.0976 0.0334 9 ASN A ND2 72 N N . TYR A 33 ? 0.8814 0.9046 0.6486 0.0403 -0.1216 -0.0309 10 TYR A N 73 C CA . TYR A 33 ? 0.8770 0.9108 0.6792 0.0280 -0.1147 -0.0401 10 TYR A CA 74 C C . TYR A 33 ? 0.8763 0.8967 0.6667 0.0203 -0.1017 -0.0462 10 TYR A C 75 O O . TYR A 33 ? 0.8061 0.8260 0.6200 0.0117 -0.0900 -0.0483 10 TYR A O 76 C CB . TYR A 33 ? 0.8990 0.9581 0.7259 0.0255 -0.1298 -0.0535 10 TYR A CB 77 C CG . TYR A 33 ? 1.0885 1.1652 0.9476 0.0278 -0.1353 -0.0494 10 TYR A CG 78 C CD1 . TYR A 33 ? 1.0978 1.1658 0.9595 0.0326 -0.1280 -0.0351 10 TYR A CD1 79 C CD2 . TYR A 33 ? 1.1873 1.2893 1.0748 0.0244 -0.1469 -0.0606 10 TYR A CD2 80 C CE1 . TYR A 33 ? 1.0770 1.1602 0.9662 0.0352 -0.1319 -0.0321 10 TYR A CE1 81 C CE2 . TYR A 33 ? 1.1807 1.2996 1.0980 0.0266 -0.1500 -0.0571 10 TYR A CE2 82 C CZ . TYR A 33 ? 1.1494 1.2584 1.0663 0.0325 -0.1424 -0.0428 10 TYR A CZ 83 O OH . TYR A 33 ? 1.1835 1.3083 1.1282 0.0353 -0.1445 -0.0400 10 TYR A OH 84 N N . ILE A 34 ? 0.8343 0.8433 0.5868 0.0244 -0.1036 -0.0490 11 ILE A N 85 C CA . ILE A 34 ? 0.7195 0.7148 0.4563 0.0187 -0.0906 -0.0555 11 ILE A CA 86 C C . ILE A 34 ? 0.7472 0.7278 0.4881 0.0154 -0.0699 -0.0445 11 ILE A C 87 O O . ILE A 34 ? 0.8666 0.8419 0.6143 0.0088 -0.0567 -0.0499 11 ILE A O 88 C CB . ILE A 34 ? 0.8482 0.8326 0.5377 0.0252 -0.0963 -0.0592 11 ILE A CB 89 C CG1 . ILE A 34 ? 0.9307 0.9023 0.6048 0.0191 -0.0826 -0.0688 11 ILE A CG1 90 C CG2 . ILE A 34 ? 0.7671 0.7359 0.4249 0.0352 -0.0944 -0.0424 11 ILE A CG2 91 C CD1 . ILE A 34 ? 0.9890 0.9717 0.6906 0.0097 -0.0844 -0.0861 11 ILE A CD1 92 N N . ARG A 35 ? 0.7882 0.7631 0.5271 0.0200 -0.0675 -0.0297 12 ARG A N 93 C CA . ARG A 35 ? 0.7788 0.7421 0.5240 0.0162 -0.0495 -0.0195 12 ARG A CA 94 C C . ARG A 35 ? 0.7281 0.7023 0.5152 0.0084 -0.0436 -0.0216 12 ARG A C 95 O O . ARG A 35 ? 0.8024 0.7708 0.5993 0.0039 -0.0290 -0.0169 12 ARG A O 96 C CB . ARG A 35 ? 0.7715 0.7244 0.5038 0.0224 -0.0494 -0.0043 12 ARG A CB 97 C CG . ARG A 35 ? 0.8754 0.8095 0.5619 0.0294 -0.0483 0.0020 12 ARG A CG 98 C CD . ARG A 35 ? 1.1151 1.0360 0.7909 0.0352 -0.0473 0.0175 12 ARG A CD 99 N NE . ARG A 35 ? 1.3395 1.2369 0.9708 0.0402 -0.0406 0.0260 12 ARG A NE 100 C CZ . ARG A 35 ? 1.4507 1.3311 1.0713 0.0346 -0.0211 0.0332 12 ARG A CZ 101 N NH1 . ARG A 35 ? 1.3590 1.2453 1.0117 0.0245 -0.0081 0.0322 12 ARG A NH1 102 N NH2 . ARG A 35 ? 1.5577 1.4156 1.1357 0.0392 -0.0145 0.0415 12 ARG A NH2 103 N N . LEU A 36 ? 0.7170 0.7077 0.5289 0.0069 -0.0548 -0.0284 13 LEU A N 104 C CA . LEU A 36 ? 0.6843 0.6840 0.5331 0.0002 -0.0498 -0.0297 13 LEU A CA 105 C C . LEU A 36 ? 0.5923 0.5924 0.4508 -0.0062 -0.0441 -0.0418 13 LEU A C 106 O O . LEU A 36 ? 0.6227 0.6268 0.5088 -0.0112 -0.0382 -0.0425 13 LEU A O 107 C CB . LEU A 36 ? 0.6445 0.6603 0.5162 0.0012 -0.0620 -0.0300 13 LEU A CB 108 C CG . LEU A 36 ? 0.6943 0.7094 0.5607 0.0083 -0.0669 -0.0185 13 LEU A CG 109 C CD1 . LEU A 36 ? 0.6867 0.7192 0.5796 0.0089 -0.0763 -0.0198 13 LEU A CD1 110 C CD2 . LEU A 36 ? 0.6512 0.6540 0.5176 0.0068 -0.0539 -0.0074 13 LEU A CD2 111 N N . LYS A 37 ? 0.7011 0.6954 0.5351 -0.0054 -0.0458 -0.0511 14 LYS A N 112 C CA . LYS A 37 ? 0.7565 0.7480 0.5958 -0.0109 -0.0402 -0.0643 14 LYS A CA 113 C C . LYS A 37 ? 0.7063 0.6902 0.5602 -0.0142 -0.0225 -0.0615 14 LYS A C 114 O O . LYS A 37 ? 0.7132 0.6987 0.5896 -0.0189 -0.0190 -0.0685 14 LYS A O 115 C CB . LYS A 37 ? 0.8599 0.8437 0.6638 -0.0087 -0.0437 -0.0745 14 LYS A CB 116 C CG . LYS A 37 ? 1.0014 0.9920 0.8107 -0.0134 -0.0541 -0.0920 14 LYS A CG 117 C CD . LYS A 37 ? 1.0733 1.0610 0.9098 -0.0209 -0.0435 -0.0997 14 LYS A CD 118 C CE . LYS A 37 ? 1.1267 1.1173 0.9665 -0.0271 -0.0521 -0.1185 14 LYS A CE 119 N NZ . LYS A 37 ? 1.1039 1.0836 0.9068 -0.0253 -0.0525 -0.1303 14 LYS A NZ 120 N N . PRO A 38 ? 0.7140 0.6895 0.5561 -0.0117 -0.0110 -0.0515 15 PRO A N 121 C CA . PRO A 38 ? 0.6260 0.5985 0.4865 -0.0142 0.0047 -0.0493 15 PRO A CA 122 C C . PRO A 38 ? 0.6174 0.5994 0.5144 -0.0169 0.0035 -0.0451 15 PRO A C 123 O O . PRO A 38 ? 0.5223 0.5035 0.4384 -0.0188 0.0117 -0.0483 15 PRO A O 124 C CB . PRO A 38 ? 0.5261 0.4921 0.3719 -0.0120 0.0144 -0.0378 15 PRO A CB 125 C CG . PRO A 38 ? 0.6157 0.5737 0.4236 -0.0080 0.0083 -0.0383 15 PRO A CG 126 C CD . PRO A 38 ? 0.6831 0.6504 0.4943 -0.0067 -0.0105 -0.0428 15 PRO A CD 127 N N . LEU A 39 ? 0.5175 0.5074 0.4225 -0.0162 -0.0064 -0.0378 16 LEU A N 128 C CA . LEU A 39 ? 0.5456 0.5439 0.4811 -0.0185 -0.0081 -0.0337 16 LEU A CA 129 C C . LEU A 39 ? 0.6433 0.6443 0.5938 -0.0223 -0.0115 -0.0441 16 LEU A C 130 O O . LEU A 39 ? 0.6206 0.6212 0.5927 -0.0244 -0.0057 -0.0437 16 LEU A O 131 C CB . LEU A 39 ? 0.4701 0.4755 0.4077 -0.0166 -0.0179 -0.0257 16 LEU A CB 132 C CG . LEU A 39 ? 0.5034 0.5037 0.4263 -0.0135 -0.0156 -0.0151 16 LEU A CG 133 C CD1 . LEU A 39 ? 0.4857 0.4923 0.4145 -0.0111 -0.0250 -0.0087 16 LEU A CD1 134 C CD2 . LEU A 39 ? 0.4897 0.4871 0.4230 -0.0156 -0.0030 -0.0092 16 LEU A CD2 135 N N . LEU A 40 ? 0.6182 0.6215 0.5569 -0.0230 -0.0213 -0.0535 17 LEU A N 136 C CA . LEU A 40 ? 0.6047 0.6103 0.5571 -0.0283 -0.0252 -0.0652 17 LEU A CA 137 C C . LEU A 40 ? 0.5936 0.5869 0.5471 -0.0303 -0.0137 -0.0730 17 LEU A C 138 O O . LEU A 40 ? 0.5252 0.5158 0.5004 -0.0339 -0.0093 -0.0754 17 LEU A O 139 C CB . LEU A 40 ? 0.7028 0.7150 0.6406 -0.0288 -0.0389 -0.0752 17 LEU A CB 140 C CG . LEU A 40 ? 0.8975 0.9226 0.8339 -0.0248 -0.0513 -0.0685 17 LEU A CG 141 C CD1 . LEU A 40 ? 0.9930 1.0261 0.9142 -0.0238 -0.0659 -0.0790 17 LEU A CD1 142 C CD2 . LEU A 40 ? 0.8573 0.8932 0.8245 -0.0279 -0.0526 -0.0634 17 LEU A CD2 143 N N . ASN A 41 ? 0.4855 0.4700 0.4148 -0.0273 -0.0078 -0.0765 18 ASN A N 144 C CA . ASN A 41 ? 0.5750 0.5473 0.5033 -0.0277 0.0047 -0.0844 18 ASN A CA 145 C C . ASN A 41 ? 0.6089 0.5796 0.5623 -0.0264 0.0161 -0.0762 18 ASN A C 146 O O . ASN A 41 ? 0.6322 0.5961 0.6012 -0.0280 0.0214 -0.0819 18 ASN A O 147 C CB . ASN A 41 ? 0.6431 0.6070 0.5396 -0.0239 0.0112 -0.0873 18 ASN A CB 148 C CG . ASN A 41 ? 0.7871 0.7501 0.6552 -0.0244 -0.0003 -0.0978 18 ASN A CG 149 O OD1 . ASN A 41 ? 0.7404 0.7073 0.6152 -0.0289 -0.0108 -0.1083 18 ASN A OD1 150 N ND2 . ASN A 41 ? 0.8383 0.7964 0.6744 -0.0200 0.0014 -0.0950 18 ASN A ND2 151 N N . THR A 42 ? 0.6317 0.6082 0.5887 -0.0232 0.0191 -0.0629 19 THR A N 152 C CA . THR A 42 ? 0.6348 0.6134 0.6158 -0.0213 0.0274 -0.0543 19 THR A CA 153 C C . THR A 42 ? 0.6091 0.5891 0.6149 -0.0235 0.0237 -0.0531 19 THR A C 154 O O . THR A 42 ? 0.6118 0.5862 0.6336 -0.0218 0.0313 -0.0535 19 THR A O 155 C CB . THR A 42 ? 0.6260 0.6127 0.6076 -0.0195 0.0273 -0.0409 19 THR A CB 156 O OG1 . THR A 42 ? 0.6650 0.6480 0.6268 -0.0178 0.0354 -0.0407 19 THR A OG1 157 C CG2 . THR A 42 ? 0.4496 0.4418 0.4578 -0.0179 0.0320 -0.0325 19 THR A CG2 158 N N . MET A 43 ? 0.5875 0.5743 0.5959 -0.0268 0.0126 -0.0515 20 MET A N 159 C CA . MET A 43 ? 0.5499 0.5378 0.5800 -0.0297 0.0101 -0.0495 20 MET A CA 160 C C . MET A 43 ? 0.5825 0.5593 0.6180 -0.0337 0.0130 -0.0615 20 MET A C 161 O O . MET A 43 ? 0.5860 0.5567 0.6395 -0.0347 0.0171 -0.0592 20 MET A O 162 C CB . MET A 43 ? 0.4667 0.4660 0.4986 -0.0323 -0.0010 -0.0456 20 MET A CB 163 C CG . MET A 43 ? 0.6924 0.6995 0.7184 -0.0284 -0.0035 -0.0342 20 MET A CG 164 S SD . MET A 43 ? 0.7831 0.8023 0.8064 -0.0290 -0.0160 -0.0312 20 MET A SD 165 C CE . MET A 43 ? 0.6619 0.6852 0.7096 -0.0310 -0.0150 -0.0237 20 MET A CE 166 N N . ILE A 44 ? 0.6156 0.5881 0.6340 -0.0360 0.0110 -0.0744 21 ILE A N 167 C CA . ILE A 44 ? 0.6228 0.5827 0.6442 -0.0406 0.0141 -0.0882 21 ILE A CA 168 C C . ILE A 44 ? 0.6659 0.6112 0.6924 -0.0359 0.0280 -0.0891 21 ILE A C 169 O O . ILE A 44 ? 0.6696 0.6025 0.7100 -0.0380 0.0330 -0.0933 21 ILE A O 170 C CB . ILE A 44 ? 0.7410 0.7003 0.7400 -0.0440 0.0072 -0.1032 21 ILE A CB 171 C CG1 . ILE A 44 ? 0.7560 0.7317 0.7533 -0.0474 -0.0078 -0.1029 21 ILE A CG1 172 C CG2 . ILE A 44 ? 0.6536 0.5985 0.6561 -0.0499 0.0105 -0.1192 21 ILE A CG2 173 C CD1 . ILE A 44 ? 0.7290 0.7101 0.7515 -0.0545 -0.0119 -0.1031 21 ILE A CD1 174 N N . GLN A 45 ? 0.6168 0.5633 0.6334 -0.0293 0.0349 -0.0848 22 GLN A N 175 C CA . GLN A 45 ? 0.6993 0.6351 0.7226 -0.0233 0.0486 -0.0860 22 GLN A CA 176 C C . GLN A 45 ? 0.6443 0.5803 0.6937 -0.0195 0.0521 -0.0742 22 GLN A C 177 O O . GLN A 45 ? 0.6684 0.5935 0.7287 -0.0144 0.0618 -0.0757 22 GLN A O 178 C CB . GLN A 45 ? 0.9214 0.8617 0.9310 -0.0177 0.0562 -0.0836 22 GLN A CB 179 C CG . GLN A 45 ? 1.1567 1.1001 1.1367 -0.0201 0.0512 -0.0886 22 GLN A CG 180 C CD . GLN A 45 ? 1.3353 1.2660 1.2945 -0.0227 0.0518 -0.1061 22 GLN A CD 181 O OE1 . GLN A 45 ? 1.3892 1.3082 1.3574 -0.0248 0.0544 -0.1160 22 GLN A OE1 182 N NE2 . GLN A 45 ? 1.3826 1.3141 1.3121 -0.0226 0.0492 -0.1101 22 GLN A NE2 183 N N . SER A 46 ? 0.5216 0.4694 0.5798 -0.0210 0.0440 -0.0626 23 SER A N 184 C CA . SER A 46 ? 0.5670 0.5158 0.6460 -0.0170 0.0456 -0.0504 23 SER A CA 185 C C . SER A 46 ? 0.6628 0.5956 0.7539 -0.0191 0.0483 -0.0535 23 SER A C 186 O O . SER A 46 ? 0.6312 0.5596 0.7373 -0.0142 0.0516 -0.0441 23 SER A O 187 C CB . SER A 46 ? 0.5234 0.4872 0.6052 -0.0186 0.0365 -0.0386 23 SER A CB 188 O OG . SER A 46 ? 0.5899 0.5551 0.6696 -0.0259 0.0284 -0.0416 23 SER A OG 189 N N . ASN A 47 ? 0.6542 0.5776 0.7380 -0.0266 0.0468 -0.0668 24 ASN A N 190 C CA . ASN A 47 ? 0.6850 0.5894 0.7790 -0.0303 0.0514 -0.0724 24 ASN A CA 191 C C . ASN A 47 ? 0.7810 0.6685 0.8822 -0.0215 0.0634 -0.0727 24 ASN A C 192 O O . ASN A 47 ? 0.8334 0.7055 0.9474 -0.0200 0.0682 -0.0684 24 ASN A O 193 C CB . ASN A 47 ? 0.6637 0.5618 0.7475 -0.0403 0.0479 -0.0899 24 ASN A CB 194 C CG . ASN A 47 ? 0.7357 0.6422 0.8262 -0.0506 0.0386 -0.0899 24 ASN A CG 195 O OD1 . ASN A 47 ? 0.8544 0.7755 0.9351 -0.0553 0.0288 -0.0956 24 ASN A OD1 196 N ND2 . ASN A 47 ? 0.7478 0.6452 0.8549 -0.0535 0.0421 -0.0833 24 ASN A ND2 197 N N . TYR A 48 ? 0.7511 0.6409 0.8436 -0.0151 0.0690 -0.0773 25 TYR A N 198 C CA . TYR A 48 ? 0.8185 0.6942 0.9182 -0.0055 0.0813 -0.0795 25 TYR A CA 199 C C . TYR A 48 ? 0.9133 0.8000 1.0290 0.0058 0.0839 -0.0638 25 TYR A C 200 O O . TYR A 48 ? 1.0745 0.9547 1.1993 0.0159 0.0936 -0.0641 25 TYR A O 201 C CB . TYR A 48 ? 0.7781 0.6508 0.8608 -0.0042 0.0880 -0.0938 25 TYR A CB 202 C CG . TYR A 48 ? 0.7988 0.6594 0.8645 -0.0144 0.0850 -0.1113 25 TYR A CG 203 C CD1 . TYR A 48 ? 0.8407 0.6764 0.9089 -0.0163 0.0918 -0.1234 25 TYR A CD1 204 C CD2 . TYR A 48 ? 0.7372 0.6108 0.7846 -0.0220 0.0748 -0.1162 25 TYR A CD2 205 C CE1 . TYR A 48 ? 0.9137 0.7394 0.9673 -0.0267 0.0880 -0.1410 25 TYR A CE1 206 C CE2 . TYR A 48 ? 0.8651 0.7303 0.8977 -0.0310 0.0701 -0.1329 25 TYR A CE2 207 C CZ . TYR A 48 ? 0.9290 0.7710 0.9652 -0.0340 0.0764 -0.1459 25 TYR A CZ 208 O OH . TYR A 48 ? 1.0150 0.8494 1.0372 -0.0442 0.0707 -0.1642 25 TYR A OH 209 N N . ASN A 49 ? 0.8935 0.7975 1.0132 0.0043 0.0749 -0.0510 26 ASN A N 210 C CA . ASN A 49 ? 0.8017 0.7185 0.9362 0.0138 0.0746 -0.0367 26 ASN A CA 211 C C . ASN A 49 ? 0.8006 0.7125 0.9458 0.0146 0.0697 -0.0245 26 ASN A C 212 O O . ASN A 49 ? 0.8041 0.7250 0.9456 0.0084 0.0610 -0.0183 26 ASN A O 213 C CB . ASN A 49 ? 0.7027 0.6430 0.8316 0.0118 0.0689 -0.0317 26 ASN A CB 214 C CG . ASN A 49 ? 0.7586 0.7142 0.9036 0.0210 0.0699 -0.0209 26 ASN A CG 215 O OD1 . ASN A 49 ? 0.8057 0.7793 0.9489 0.0193 0.0664 -0.0166 26 ASN A OD1 216 N ND2 . ASN A 49 ? 0.7711 0.7198 0.9324 0.0309 0.0746 -0.0167 26 ASN A ND2 217 N N . ARG A 50 ? 0.8369 0.7332 0.9938 0.0232 0.0759 -0.0208 27 ARG A N 218 C CA . ARG A 50 ? 0.7681 0.6548 0.9319 0.0251 0.0730 -0.0086 27 ARG A CA 219 C C . ARG A 50 ? 0.7434 0.6506 0.9135 0.0311 0.0650 0.0065 27 ARG A C 220 O O . ARG A 50 ? 0.7647 0.6685 0.9352 0.0310 0.0603 0.0176 27 ARG A O 221 C CB . ARG A 50 ? 0.9449 0.8066 1.1177 0.0345 0.0822 -0.0082 27 ARG A CB 222 C CG . ARG A 50 ? 1.1592 0.9976 1.3315 0.0302 0.0833 -0.0027 27 ARG A CG 223 C CD . ARG A 50 ? 1.3309 1.1392 1.5094 0.0383 0.0942 -0.0051 27 ARG A CD 224 N NE . ARG A 50 ? 1.4823 1.2642 1.6587 0.0313 0.0974 -0.0019 27 ARG A NE 225 C CZ . ARG A 50 ? 1.5855 1.3515 1.7566 0.0173 0.1012 -0.0152 27 ARG A CZ 226 N NH1 . ARG A 50 ? 1.6567 1.3991 1.8284 0.0103 0.1053 -0.0113 27 ARG A NH1 227 N NH2 . ARG A 50 ? 1.5973 1.3709 1.7621 0.0098 0.1009 -0.0325 27 ARG A NH2 228 N N . GLY A 51 ? 0.6756 0.6035 0.8498 0.0356 0.0638 0.0064 28 GLY A N 229 C CA . GLY A 51 ? 0.6803 0.6291 0.8616 0.0404 0.0559 0.0185 28 GLY A CA 230 C C . GLY A 51 ? 0.7917 0.7548 0.9618 0.0302 0.0469 0.0204 28 GLY A C 231 O O . GLY A 51 ? 0.8240 0.8001 0.9966 0.0320 0.0391 0.0304 28 GLY A O 232 N N . THR A 52 ? 0.6953 0.6559 0.8524 0.0201 0.0476 0.0105 29 THR A N 233 C CA . THR A 52 ? 0.7453 0.7184 0.8917 0.0117 0.0396 0.0118 29 THR A CA 234 C C . THR A 52 ? 0.6906 0.6547 0.8312 0.0046 0.0358 0.0134 29 THR A C 235 O O . THR A 52 ? 0.6437 0.5904 0.7853 0.0025 0.0405 0.0092 29 THR A O 236 C CB . THR A 52 ? 0.6868 0.6658 0.8214 0.0060 0.0410 0.0015 29 THR A CB 237 O OG1 . THR A 52 ? 0.7218 0.7148 0.8485 0.0013 0.0333 0.0055 29 THR A OG1 238 C CG2 . THR A 52 ? 0.6438 0.6087 0.7682 -0.0007 0.0433 -0.0101 29 THR A CG2 239 N N . SER A 53 ? 0.7029 0.6784 0.8382 0.0008 0.0282 0.0191 30 SER A N 240 C CA . SER A 53 ? 0.7290 0.6996 0.8607 -0.0055 0.0255 0.0215 30 SER A CA 241 C C . SER A 53 ? 0.6649 0.6347 0.7894 -0.0148 0.0248 0.0101 30 SER A C 242 O O . SER A 53 ? 0.5980 0.5753 0.7151 -0.0163 0.0231 0.0029 30 SER A O 243 C CB . SER A 53 ? 0.6830 0.6662 0.8111 -0.0051 0.0182 0.0311 30 SER A CB 244 O OG . SER A 53 ? 0.8214 0.8015 0.9462 -0.0111 0.0170 0.0329 30 SER A OG 245 N N . ALA A 54 ? 0.5708 0.5318 0.6978 -0.0209 0.0261 0.0085 31 ALA A N 246 C CA . ALA A 54 ? 0.5160 0.4803 0.6394 -0.0302 0.0234 -0.0022 31 ALA A CA 247 C C . ALA A 54 ? 0.5007 0.4768 0.6236 -0.0341 0.0179 0.0030 31 ALA A C 248 O O . ALA A 54 ? 0.5594 0.5439 0.6809 -0.0404 0.0136 -0.0045 31 ALA A O 249 C CB . ALA A 54 ? 0.4760 0.4233 0.6056 -0.0361 0.0294 -0.0106 31 ALA A CB 250 N N . VAL A 55 ? 0.5093 0.4867 0.6333 -0.0297 0.0178 0.0154 32 VAL A N 251 C CA . VAL A 55 ? 0.5095 0.4965 0.6320 -0.0324 0.0144 0.0208 32 VAL A CA 252 C C . VAL A 55 ? 0.4965 0.4997 0.6111 -0.0321 0.0067 0.0180 32 VAL A C 253 O O . VAL A 55 ? 0.4416 0.4535 0.5565 -0.0367 0.0035 0.0136 32 VAL A O 254 C CB . VAL A 55 ? 0.4906 0.4742 0.6117 -0.0266 0.0156 0.0345 32 VAL A CB 255 C CG1 . VAL A 55 ? 0.4672 0.4607 0.5842 -0.0288 0.0128 0.0392 32 VAL A CG1 256 C CG2 . VAL A 55 ? 0.4364 0.4011 0.5633 -0.0261 0.0235 0.0392 32 VAL A CG2 257 N N . ASN A 56 ? 0.4670 0.4742 0.5757 -0.0264 0.0042 0.0208 33 ASN A N 258 C CA . ASN A 56 ? 0.4711 0.4895 0.5705 -0.0258 -0.0018 0.0191 33 ASN A CA 259 C C . ASN A 56 ? 0.4547 0.4753 0.5492 -0.0293 -0.0041 0.0082 33 ASN A C 260 O O . ASN A 56 ? 0.5359 0.5650 0.6242 -0.0302 -0.0097 0.0061 33 ASN A O 261 C CB . ASN A 56 ? 0.4539 0.4745 0.5500 -0.0206 -0.0022 0.0234 33 ASN A CB 262 C CG . ASN A 56 ? 0.6326 0.6465 0.7334 -0.0182 0.0033 0.0200 33 ASN A CG 263 O OD1 . ASN A 56 ? 0.6247 0.6299 0.7291 -0.0202 0.0074 0.0139 33 ASN A OD1 264 N ND2 . ASN A 56 ? 0.5829 0.6011 0.6850 -0.0140 0.0040 0.0231 33 ASN A ND2 265 N N . VAL A 57 ? 0.3831 0.3954 0.4794 -0.0305 0.0000 0.0011 34 VAL A N 266 C CA . VAL A 57 ? 0.3797 0.3928 0.4686 -0.0336 -0.0024 -0.0103 34 VAL A CA 267 C C . VAL A 57 ? 0.5118 0.5311 0.6057 -0.0397 -0.0070 -0.0163 34 VAL A C 268 O O . VAL A 57 ? 0.5386 0.5673 0.6250 -0.0401 -0.0141 -0.0210 34 VAL A O 269 C CB . VAL A 57 ? 0.5297 0.5305 0.6194 -0.0337 0.0041 -0.0176 34 VAL A CB 270 C CG1 . VAL A 57 ? 0.5330 0.5335 0.6139 -0.0379 0.0010 -0.0310 34 VAL A CG1 271 C CG2 . VAL A 57 ? 0.4912 0.4902 0.5774 -0.0273 0.0087 -0.0132 34 VAL A CG2 272 N N . VAL A 58 ? 0.3840 0.3981 0.4913 -0.0442 -0.0027 -0.0158 35 VAL A N 273 C CA . VAL A 58 ? 0.4118 0.4331 0.5288 -0.0515 -0.0054 -0.0220 35 VAL A CA 274 C C . VAL A 58 ? 0.4402 0.4769 0.5579 -0.0498 -0.0106 -0.0164 35 VAL A C 275 O O . VAL A 58 ? 0.4103 0.4599 0.5308 -0.0524 -0.0171 -0.0231 35 VAL A O 276 C CB . VAL A 58 ? 0.4607 0.4702 0.5922 -0.0577 0.0030 -0.0215 35 VAL A CB 277 C CG1 . VAL A 58 ? 0.3882 0.4084 0.5334 -0.0661 0.0017 -0.0259 35 VAL A CG1 278 C CG2 . VAL A 58 ? 0.4303 0.4240 0.5618 -0.0602 0.0075 -0.0306 35 VAL A CG2 279 N N . LEU A 59 ? 0.4047 0.4402 0.5196 -0.0449 -0.0083 -0.0047 36 LEU A N 280 C CA . LEU A 59 ? 0.4720 0.5194 0.5848 -0.0420 -0.0124 0.0004 36 LEU A CA 281 C C . LEU A 59 ? 0.4476 0.5039 0.5494 -0.0383 -0.0208 -0.0039 36 LEU A C 282 O O . LEU A 59 ? 0.4530 0.5216 0.5575 -0.0380 -0.0260 -0.0066 36 LEU A O 283 C CB . LEU A 59 ? 0.4271 0.4697 0.5344 -0.0368 -0.0096 0.0122 36 LEU A CB 284 C CG . LEU A 59 ? 0.4381 0.4895 0.5386 -0.0327 -0.0137 0.0170 36 LEU A CG 285 C CD1 . LEU A 59 ? 0.3679 0.4297 0.4777 -0.0356 -0.0133 0.0150 36 LEU A CD1 286 C CD2 . LEU A 59 ? 0.3973 0.4431 0.4917 -0.0287 -0.0116 0.0269 36 LEU A CD2 287 N N . SER A 60 ? 0.4094 0.4589 0.4987 -0.0349 -0.0215 -0.0041 37 SER A N 288 C CA . SER A 60 ? 0.4166 0.4701 0.4914 -0.0310 -0.0280 -0.0067 37 SER A CA 289 C C . SER A 60 ? 0.3914 0.4529 0.4664 -0.0334 -0.0347 -0.0173 37 SER A C 290 O O . SER A 60 ? 0.4261 0.4969 0.4956 -0.0298 -0.0422 -0.0182 37 SER A O 291 C CB . SER A 60 ? 0.3942 0.4379 0.4572 -0.0287 -0.0246 -0.0057 37 SER A CB 292 O OG . SER A 60 ? 0.5676 0.6120 0.6137 -0.0256 -0.0294 -0.0081 37 SER A OG 293 N N . LEU A 61 ? 0.4578 0.5154 0.5393 -0.0391 -0.0325 -0.0257 38 LEU A N 294 C CA . LEU A 61 ? 0.5438 0.6092 0.6259 -0.0426 -0.0398 -0.0378 38 LEU A CA 295 C C . LEU A 61 ? 0.5096 0.5919 0.6092 -0.0457 -0.0446 -0.0406 38 LEU A C 296 O O . LEU A 61 ? 0.4873 0.5831 0.5845 -0.0435 -0.0546 -0.0461 38 LEU A O 297 C CB . LEU A 61 ? 0.5518 0.6065 0.6371 -0.0489 -0.0351 -0.0472 38 LEU A CB 298 C CG . LEU A 61 ? 0.5250 0.5658 0.5928 -0.0451 -0.0307 -0.0476 38 LEU A CG 299 C CD1 . LEU A 61 ? 0.4965 0.5239 0.5700 -0.0503 -0.0234 -0.0555 38 LEU A CD1 300 C CD2 . LEU A 61 ? 0.4200 0.4646 0.4662 -0.0411 -0.0388 -0.0527 38 LEU A CD2 301 N N . LYS A 62 ? 0.4703 0.5523 0.5873 -0.0504 -0.0373 -0.0365 39 LYS A N 302 C CA . LYS A 62 ? 0.5818 0.6804 0.7183 -0.0545 -0.0390 -0.0391 39 LYS A CA 303 C C . LYS A 62 ? 0.5737 0.6853 0.7062 -0.0462 -0.0449 -0.0335 39 LYS A C 304 O O . LYS A 62 ? 0.5676 0.6978 0.7125 -0.0463 -0.0509 -0.0386 39 LYS A O 305 C CB . LYS A 62 ? 0.5574 0.6493 0.7095 -0.0609 -0.0274 -0.0338 39 LYS A CB 306 C CG . LYS A 62 ? 0.6570 0.7341 0.8151 -0.0693 -0.0210 -0.0397 39 LYS A CG 307 C CD . LYS A 62 ? 0.7390 0.8213 0.9206 -0.0803 -0.0155 -0.0445 39 LYS A CD 308 C CE . LYS A 62 ? 0.7746 0.8543 0.9631 -0.0803 -0.0055 -0.0321 39 LYS A CE 309 N NZ . LYS A 62 ? 0.8902 0.9738 1.1017 -0.0922 0.0021 -0.0362 39 LYS A NZ 310 N N . LEU A 63 ? 0.5713 0.6731 0.6875 -0.0389 -0.0431 -0.0237 40 LEU A N 311 C CA . LEU A 63 ? 0.5588 0.6677 0.6685 -0.0305 -0.0474 -0.0180 40 LEU A CA 312 C C . LEU A 63 ? 0.5215 0.6394 0.6216 -0.0246 -0.0591 -0.0235 40 LEU A C 313 O O . LEU A 63 ? 0.4943 0.6234 0.5965 -0.0182 -0.0643 -0.0220 40 LEU A O 314 C CB . LEU A 63 ? 0.6590 0.7532 0.7530 -0.0258 -0.0429 -0.0077 40 LEU A CB 315 C CG . LEU A 63 ? 0.6904 0.7872 0.7808 -0.0195 -0.0430 -0.0006 40 LEU A CG 316 C CD1 . LEU A 63 ? 0.6719 0.7794 0.7804 -0.0222 -0.0384 -0.0002 40 LEU A CD1 317 C CD2 . LEU A 63 ? 0.6065 0.6889 0.6844 -0.0178 -0.0384 0.0077 40 LEU A CD2 318 N N . VAL A 64 ? 0.4809 0.5931 0.5694 -0.0259 -0.0630 -0.0296 41 VAL A N 319 C CA . VAL A 64 ? 0.4241 0.5431 0.4995 -0.0199 -0.0748 -0.0347 41 VAL A CA 320 C C . VAL A 64 ? 0.4168 0.5510 0.5056 -0.0256 -0.0825 -0.0481 41 VAL A C 321 O O . VAL A 64 ? 0.5614 0.6995 0.6370 -0.0222 -0.0929 -0.0546 41 VAL A O 322 C CB . VAL A 64 ? 0.4374 0.5392 0.4848 -0.0159 -0.0746 -0.0320 41 VAL A CB 323 C CG1 . VAL A 64 ? 0.4661 0.5552 0.5032 -0.0115 -0.0678 -0.0199 41 VAL A CG1 324 C CG2 . VAL A 64 ? 0.3330 0.4246 0.3788 -0.0235 -0.0689 -0.0383 41 VAL A CG2 325 N N . GLY A 65 ? 0.4624 0.6046 0.5768 -0.0348 -0.0773 -0.0523 42 GLY A N 326 C CA . GLY A 65 ? 0.4781 0.6365 0.6104 -0.0424 -0.0839 -0.0659 42 GLY A CA 327 C C . GLY A 65 ? 0.5748 0.7216 0.6968 -0.0489 -0.0848 -0.0758 42 GLY A C 328 O O . GLY A 65 ? 0.6670 0.8248 0.7888 -0.0510 -0.0958 -0.0881 42 GLY A O 329 N N . ILE A 66 ? 0.5543 0.6792 0.6676 -0.0514 -0.0735 -0.0711 43 ILE A N 330 C CA . ILE A 66 ? 0.4927 0.6039 0.5967 -0.0570 -0.0717 -0.0806 43 ILE A CA 331 C C . ILE A 66 ? 0.5649 0.6635 0.6857 -0.0667 -0.0590 -0.0811 43 ILE A C 332 O O . ILE A 66 ? 0.5857 0.6739 0.7089 -0.0649 -0.0488 -0.0694 43 ILE A O 333 C CB . ILE A 66 ? 0.5453 0.6393 0.6196 -0.0494 -0.0695 -0.0754 43 ILE A CB 334 C CG1 . ILE A 66 ? 0.5517 0.6537 0.6050 -0.0400 -0.0817 -0.0750 43 ILE A CG1 335 C CG2 . ILE A 66 ? 0.5447 0.6233 0.6107 -0.0548 -0.0649 -0.0853 43 ILE A CG2 336 C CD1 . ILE A 66 ? 0.5877 0.6724 0.6111 -0.0335 -0.0779 -0.0695 43 ILE A CD1 337 N N . GLN A 67 ? 0.4484 0.5470 0.5801 -0.0768 -0.0600 -0.0949 44 GLN A N 338 C CA . GLN A 67 ? 0.5478 0.6303 0.6935 -0.0861 -0.0475 -0.0961 44 GLN A CA 339 C C . GLN A 67 ? 0.4156 0.4781 0.5462 -0.0879 -0.0446 -0.1052 44 GLN A C 340 O O . GLN A 67 ? 0.5003 0.5671 0.6219 -0.0903 -0.0537 -0.1191 44 GLN A O 341 C CB . GLN A 67 ? 0.5710 0.6668 0.7456 -0.0984 -0.0478 -0.1047 44 GLN A CB 342 C CG . GLN A 67 ? 0.6601 0.7772 0.8513 -0.0964 -0.0492 -0.0967 44 GLN A CG 343 C CD . GLN A 67 ? 0.7584 0.8899 0.9811 -0.1097 -0.0473 -0.1052 44 GLN A CD 344 O OE1 . GLN A 67 ? 0.8266 0.9822 1.0618 -0.1129 -0.0588 -0.1166 44 GLN A OE1 345 N NE2 . GLN A 67 ? 0.7150 0.8320 0.9508 -0.1174 -0.0325 -0.0995 44 GLN A NE2 346 N N . ILE A 68 ? 0.5222 0.5632 0.6491 -0.0858 -0.0322 -0.0975 45 ILE A N 347 C CA . ILE A 68 ? 0.5115 0.5320 0.6265 -0.0867 -0.0268 -0.1057 45 ILE A CA 348 C C . ILE A 68 ? 0.5248 0.5265 0.6566 -0.0939 -0.0144 -0.1055 45 ILE A C 349 O O . ILE A 68 ? 0.6069 0.5990 0.7432 -0.0895 -0.0052 -0.0915 45 ILE A O 350 C CB . ILE A 68 ? 0.5801 0.5909 0.6737 -0.0752 -0.0227 -0.0968 45 ILE A CB 351 C CG1 . ILE A 68 ? 0.6261 0.6515 0.7004 -0.0682 -0.0337 -0.0959 45 ILE A CG1 352 C CG2 . ILE A 68 ? 0.4836 0.4736 0.5670 -0.0754 -0.0152 -0.1058 45 ILE A CG2 353 C CD1 . ILE A 68 ? 0.6727 0.7038 0.7346 -0.0715 -0.0443 -0.1123 45 ILE A CD1 354 N N . GLN A 69 ? 0.5089 0.5045 0.6488 -0.1049 -0.0146 -0.1212 46 GLN A N 355 C CA . GLN A 69 ? 0.5716 0.5479 0.7289 -0.1137 -0.0028 -0.1223 46 GLN A CA 356 C C . GLN A 69 ? 0.6495 0.5990 0.7997 -0.1061 0.0101 -0.1132 46 GLN A C 357 O O . GLN A 69 ? 0.6004 0.5389 0.7617 -0.1058 0.0197 -0.1010 46 GLN A O 358 C CB . GLN A 69 ? 0.5469 0.5188 0.7112 -0.1272 -0.0057 -0.1434 46 GLN A CB 359 C CG . GLN A 69 ? 0.7012 0.6513 0.8846 -0.1383 0.0070 -0.1452 46 GLN A CG 360 C CD . GLN A 69 ? 0.7543 0.7155 0.9604 -0.1442 0.0111 -0.1341 46 GLN A CD 361 O OE1 . GLN A 69 ? 0.6798 0.6694 0.8932 -0.1446 0.0019 -0.1326 46 GLN A OE1 362 N NE2 . GLN A 69 ? 0.7168 0.6546 0.9331 -0.1480 0.0256 -0.1258 46 GLN A NE2 363 N N . THR A 70 ? 0.5275 0.4671 0.6590 -0.0994 0.0106 -0.1191 47 THR A N 364 C CA . THR A 70 ? 0.5388 0.4552 0.6655 -0.0911 0.0226 -0.1124 47 THR A CA 365 C C . THR A 70 ? 0.5591 0.4800 0.6882 -0.0808 0.0260 -0.0915 47 THR A C 366 O O . THR A 70 ? 0.6935 0.5980 0.8306 -0.0774 0.0356 -0.0819 47 THR A O 367 C CB . THR A 70 ? 0.5422 0.4524 0.6478 -0.0844 0.0227 -0.1218 47 THR A CB 368 O OG1 . THR A 70 ? 0.4927 0.4242 0.5832 -0.0791 0.0128 -0.1193 47 THR A OG1 369 C CG2 . THR A 70 ? 0.5535 0.4520 0.6550 -0.0941 0.0217 -0.1434 47 THR A CG2 370 N N . LEU A 71 ? 0.5536 0.4959 0.6749 -0.0756 0.0177 -0.0848 48 LEU A N 371 C CA . LEU A 71 ? 0.5733 0.5218 0.6957 -0.0669 0.0191 -0.0668 48 LEU A CA 372 C C . LEU A 71 ? 0.4921 0.4424 0.6302 -0.0716 0.0213 -0.0574 48 LEU A C 373 O O . LEU A 71 ? 0.5008 0.4448 0.6422 -0.0658 0.0268 -0.0435 48 LEU A O 374 C CB . LEU A 71 ? 0.5138 0.4821 0.6231 -0.0616 0.0100 -0.0636 48 LEU A CB 375 C CG . LEU A 71 ? 0.5899 0.5555 0.6811 -0.0554 0.0103 -0.0688 48 LEU A CG 376 C CD1 . LEU A 71 ? 0.4786 0.4614 0.5554 -0.0521 0.0010 -0.0668 48 LEU A CD1 377 C CD2 . LEU A 71 ? 0.5031 0.4583 0.5956 -0.0467 0.0198 -0.0596 48 LEU A CD2 378 N N . MET A 72 ? 0.5053 0.4652 0.6530 -0.0821 0.0170 -0.0653 49 MET A N 379 C CA . MET A 72 ? 0.5868 0.5487 0.7503 -0.0882 0.0211 -0.0580 49 MET A CA 380 C C . MET A 72 ? 0.6272 0.5623 0.7982 -0.0907 0.0338 -0.0536 49 MET A C 381 O O . MET A 72 ? 0.4846 0.4138 0.6593 -0.0880 0.0400 -0.0392 49 MET A O 382 C CB . MET A 72 ? 0.5923 0.5709 0.7681 -0.1000 0.0148 -0.0700 49 MET A CB 383 C CG . MET A 72 ? 0.7968 0.7774 0.9915 -0.1084 0.0215 -0.0643 49 MET A CG 384 S SD . MET A 72 ? 0.9307 0.9263 1.1227 -0.0996 0.0211 -0.0458 49 MET A SD 385 C CE . MET A 72 ? 1.0657 1.0917 1.2529 -0.0961 0.0053 -0.0536 49 MET A CE 386 N N . GLN A 73 ? 0.6113 0.5287 0.7827 -0.0953 0.0377 -0.0661 50 GLN A N 387 C CA . GLN A 73 ? 0.6593 0.5469 0.8366 -0.0967 0.0502 -0.0629 50 GLN A CA 388 C C . GLN A 73 ? 0.6559 0.5316 0.8249 -0.0817 0.0552 -0.0478 50 GLN A C 389 O O . GLN A 73 ? 0.6256 0.4837 0.7988 -0.0791 0.0637 -0.0357 50 GLN A O 390 C CB . GLN A 73 ? 0.5519 0.4223 0.7291 -0.1037 0.0527 -0.0815 50 GLN A CB 391 C CG . GLN A 73 ? 0.6419 0.5216 0.8309 -0.1204 0.0483 -0.0977 50 GLN A CG 392 C CD . GLN A 73 ? 0.8154 0.6823 0.9996 -0.1267 0.0473 -0.1187 50 GLN A CD 393 O OE1 . GLN A 73 ? 0.9844 0.8589 1.1777 -0.1405 0.0422 -0.1345 50 GLN A OE1 394 N NE2 . GLN A 73 ? 0.7729 0.6213 0.9433 -0.1164 0.0521 -0.1197 50 GLN A NE2 395 N N . LYS A 74 ? 0.5850 0.4706 0.7423 -0.0718 0.0498 -0.0485 51 LYS A N 396 C CA . LYS A 74 ? 0.6948 0.5747 0.8473 -0.0576 0.0531 -0.0355 51 LYS A CA 397 C C . LYS A 74 ? 0.6882 0.5778 0.8422 -0.0532 0.0513 -0.0179 51 LYS A C 398 O O . LYS A 74 ? 0.6927 0.5698 0.8477 -0.0451 0.0564 -0.0051 51 LYS A O 399 C CB . LYS A 74 ? 0.6654 0.5577 0.8068 -0.0498 0.0482 -0.0401 51 LYS A CB 400 C CG . LYS A 74 ? 0.6725 0.5628 0.8131 -0.0359 0.0514 -0.0281 51 LYS A CG 401 C CD . LYS A 74 ? 0.6328 0.5371 0.7641 -0.0300 0.0481 -0.0324 51 LYS A CD 402 C CE . LYS A 74 ? 0.6949 0.6016 0.8300 -0.0171 0.0509 -0.0209 51 LYS A CE 403 N NZ . LYS A 74 ? 0.7558 0.6785 0.8835 -0.0129 0.0486 -0.0235 51 LYS A NZ 404 N N . MET A 75 ? 0.5751 0.4866 0.7282 -0.0579 0.0437 -0.0175 52 MET A N 405 C CA . MET A 75 ? 0.5951 0.5167 0.7469 -0.0537 0.0418 -0.0025 52 MET A CA 406 C C . MET A 75 ? 0.5837 0.4900 0.7422 -0.0578 0.0502 0.0065 52 MET A C 407 O O . MET A 75 ? 0.6676 0.5682 0.8218 -0.0501 0.0525 0.0211 52 MET A O 408 C CB . MET A 75 ? 0.5513 0.4978 0.7009 -0.0575 0.0329 -0.0052 52 MET A CB 409 C CG . MET A 75 ? 0.5248 0.4808 0.6712 -0.0529 0.0312 0.0088 52 MET A CG 410 S SD . MET A 75 ? 0.5738 0.5550 0.7210 -0.0578 0.0236 0.0056 52 MET A SD 411 C CE . MET A 75 ? 0.5191 0.4980 0.6830 -0.0719 0.0293 -0.0031 52 MET A CE 412 N N . ILE A 76 ? 0.5732 0.4726 0.7414 -0.0703 0.0548 -0.0026 53 ILE A N 413 C CA . ILE A 76 ? 0.5973 0.4800 0.7723 -0.0764 0.0651 0.0052 53 ILE A CA 414 C C . ILE A 76 ? 0.6676 0.5210 0.8386 -0.0681 0.0735 0.0147 53 ILE A C 415 O O . ILE A 76 ? 0.6966 0.5382 0.8638 -0.0640 0.0793 0.0300 53 ILE A O 416 C CB . ILE A 76 ? 0.5956 0.4759 0.7850 -0.0931 0.0690 -0.0088 53 ILE A CB 417 C CG1 . ILE A 76 ? 0.5567 0.4685 0.7523 -0.0999 0.0599 -0.0170 53 ILE A CG1 418 C CG2 . ILE A 76 ? 0.5789 0.4380 0.7754 -0.1004 0.0824 -0.0002 53 ILE A CG2 419 C CD1 . ILE A 76 ? 0.5845 0.5114 0.7789 -0.0973 0.0599 -0.0041 53 ILE A CD1 420 N N . GLN A 77 ? 0.7060 0.5475 0.8766 -0.0645 0.0742 0.0057 54 GLN A N 421 C CA . GLN A 77 ? 0.7377 0.5521 0.9058 -0.0542 0.0817 0.0134 54 GLN A CA 422 C C . GLN A 77 ? 0.6923 0.5138 0.8522 -0.0384 0.0774 0.0302 54 GLN A C 423 O O . GLN A 77 ? 0.7825 0.5853 0.9394 -0.0307 0.0829 0.0442 54 GLN A O 424 C CB . GLN A 77 ? 0.9404 0.7452 1.1093 -0.0521 0.0826 -0.0012 54 GLN A CB 425 C CG . GLN A 77 ? 1.2222 0.9992 1.3905 -0.0399 0.0907 0.0053 54 GLN A CG 426 C CD . GLN A 77 ? 1.4191 1.1883 1.5874 -0.0369 0.0926 -0.0101 54 GLN A CD 427 O OE1 . GLN A 77 ? 1.4728 1.2568 1.6391 -0.0443 0.0874 -0.0255 54 GLN A OE1 428 N NE2 . GLN A 77 ? 1.4851 1.2304 1.6545 -0.0250 0.1002 -0.0058 54 GLN A NE2 429 N N . GLN A 78 ? 0.6111 0.4592 0.7669 -0.0337 0.0673 0.0286 55 GLN A N 430 C CA . GLN A 78 ? 0.7163 0.5750 0.8658 -0.0206 0.0617 0.0424 55 GLN A CA 431 C C . GLN A 78 ? 0.6856 0.5454 0.8294 -0.0214 0.0618 0.0565 55 GLN A C 432 O O . GLN A 78 ? 0.6803 0.5326 0.8182 -0.0109 0.0619 0.0708 55 GLN A O 433 C CB . GLN A 78 ? 0.6640 0.5499 0.8107 -0.0183 0.0518 0.0367 55 GLN A CB 434 C CG . GLN A 78 ? 0.7832 0.6689 0.9324 -0.0141 0.0524 0.0259 55 GLN A CG 435 C CD . GLN A 78 ? 0.8522 0.7626 0.9970 -0.0121 0.0443 0.0221 55 GLN A CD 436 O OE1 . GLN A 78 ? 0.7454 0.6724 0.8855 -0.0160 0.0377 0.0245 55 GLN A OE1 437 N NE2 . GLN A 78 ? 0.9008 0.8127 1.0470 -0.0060 0.0458 0.0163 55 GLN A NE2 438 N N . ILE A 79 ? 0.6978 0.5679 0.8430 -0.0334 0.0618 0.0522 56 ILE A N 439 C CA . ILE A 79 ? 0.6908 0.5632 0.8299 -0.0351 0.0636 0.0640 56 ILE A CA 440 C C . ILE A 79 ? 0.7141 0.5574 0.8512 -0.0351 0.0751 0.0750 56 ILE A C 441 O O . ILE A 79 ? 0.6847 0.5216 0.8104 -0.0270 0.0759 0.0905 56 ILE A O 442 C CB . ILE A 79 ? 0.6630 0.5537 0.8074 -0.0477 0.0625 0.0556 56 ILE A CB 443 C CG1 . ILE A 79 ? 0.6267 0.5443 0.7684 -0.0450 0.0507 0.0490 56 ILE A CG1 444 C CG2 . ILE A 79 ? 0.5339 0.4230 0.6733 -0.0506 0.0683 0.0672 56 ILE A CG2 445 C CD1 . ILE A 79 ? 0.4954 0.4322 0.6433 -0.0550 0.0480 0.0400 56 ILE A CD1 446 N N . LYS A 80 ? 0.6921 0.5164 0.8389 -0.0442 0.0840 0.0670 57 LYS A N 447 C CA . LYS A 80 ? 0.7953 0.5874 0.9403 -0.0453 0.0967 0.0771 57 LYS A CA 448 C C . LYS A 80 ? 0.8187 0.5918 0.9546 -0.0280 0.0966 0.0899 57 LYS A C 449 O O . LYS A 80 ? 0.9140 0.6664 1.0400 -0.0226 0.1031 0.1059 57 LYS A O 450 C CB . LYS A 80 ? 0.7623 0.5369 0.9208 -0.0594 0.1059 0.0634 57 LYS A CB 451 C CG . LYS A 80 ? 0.7628 0.5526 0.9327 -0.0775 0.1085 0.0539 57 LYS A CG 452 C CD . LYS A 80 ? 0.7743 0.5461 0.9587 -0.0924 0.1170 0.0397 57 LYS A CD 453 C CE . LYS A 80 ? 0.8120 0.6013 1.0114 -0.1107 0.1196 0.0306 57 LYS A CE 454 N NZ . LYS A 80 ? 0.8622 0.6370 1.0778 -0.1268 0.1263 0.0143 57 LYS A NZ 455 N N . TYR A 81 ? 0.7882 0.5690 0.9275 -0.0188 0.0894 0.0832 58 TYR A N 456 C CA . TYR A 81 ? 0.8417 0.6096 0.9767 -0.0011 0.0882 0.0938 58 TYR A CA 457 C C . TYR A 81 ? 0.8650 0.6465 0.9877 0.0106 0.0797 0.1098 58 TYR A C 458 O O . TYR A 81 ? 0.9216 0.6845 1.0351 0.0214 0.0822 0.1255 58 TYR A O 459 C CB . TYR A 81 ? 0.9079 0.6851 1.0516 0.0053 0.0835 0.0815 58 TYR A CB 460 C CG . TYR A 81 ? 1.0415 0.8160 1.1846 0.0248 0.0797 0.0917 58 TYR A CG 461 C CD1 . TYR A 81 ? 1.1164 0.8594 1.2595 0.0348 0.0877 0.0999 58 TYR A CD1 462 C CD2 . TYR A 81 ? 1.0516 0.8552 1.1953 0.0335 0.0682 0.0930 58 TYR A CD2 463 C CE1 . TYR A 81 ? 1.1808 0.9238 1.3256 0.0542 0.0833 0.1093 58 TYR A CE1 464 C CE2 . TYR A 81 ? 1.1433 0.9484 1.2902 0.0511 0.0641 0.1015 58 TYR A CE2 465 C CZ . TYR A 81 ? 1.2337 1.0098 1.3817 0.0621 0.0711 0.1096 58 TYR A CZ 466 O OH . TYR A 81 ? 1.2891 1.0691 1.4423 0.0811 0.0660 0.1180 58 TYR A OH 467 N N . ASN A 82 ? 0.7632 0.5761 0.8847 0.0086 0.0695 0.1055 59 ASN A N 468 C CA . ASN A 82 ? 0.8447 0.6724 0.9543 0.0181 0.0603 0.1179 59 ASN A CA 469 C C . ASN A 82 ? 0.9531 0.7689 1.0477 0.0156 0.0656 0.1315 59 ASN A C 470 O O . ASN A 82 ? 1.0247 0.8357 1.1057 0.0272 0.0618 0.1462 59 ASN A O 471 C CB . ASN A 82 ? 0.8322 0.6929 0.9435 0.0147 0.0496 0.1090 59 ASN A CB 472 C CG . ASN A 82 ? 0.9135 0.7874 1.0353 0.0213 0.0435 0.1005 59 ASN A CG 473 O OD1 . ASN A 82 ? 0.9524 0.8340 1.0742 0.0337 0.0366 0.1072 59 ASN A OD1 474 N ND2 . ASN A 82 ? 0.9151 0.7928 1.0459 0.0129 0.0460 0.0854 59 ASN A ND2 475 N N . VAL A 83 ? 0.9123 0.7238 1.0094 0.0006 0.0744 0.1263 60 VAL A N 476 C CA . VAL A 83 ? 0.8772 0.6779 0.9610 -0.0036 0.0823 0.1382 60 VAL A CA 477 C C . VAL A 83 ? 0.9543 0.7190 1.0289 0.0028 0.0924 0.1530 60 VAL A C 478 O O . VAL A 83 ? 1.0123 0.7673 1.0676 0.0099 0.0937 0.1692 60 VAL A O 479 C CB . VAL A 83 ? 0.8608 0.6680 0.9543 -0.0220 0.0905 0.1280 60 VAL A CB 480 C CG1 . VAL A 83 ? 0.9301 0.7188 1.0132 -0.0277 0.1039 0.1403 60 VAL A CG1 481 C CG2 . VAL A 83 ? 0.7960 0.6375 0.8920 -0.0255 0.0803 0.1186 60 VAL A CG2 482 N N . LYS A 84 ? 0.9608 0.7041 1.0472 0.0013 0.0994 0.1476 61 LYS A N 483 C CA . LYS A 84 ? 1.1318 0.8361 1.2107 0.0055 0.1115 0.1606 61 LYS A CA 484 C C . LYS A 84 ? 1.1800 0.8724 1.2488 0.0273 0.1049 0.1744 61 LYS A C 485 O O . LYS A 84 ? 1.2584 0.9179 1.3157 0.0345 0.1133 0.1893 61 LYS A O 486 C CB . LYS A 84 ? 1.2630 0.9455 1.3586 -0.0062 0.1230 0.1482 61 LYS A CB 487 C CG . LYS A 84 ? 1.3786 1.0555 1.4848 0.0037 0.1188 0.1398 61 LYS A CG 488 C CD . LYS A 84 ? 1.4637 1.1154 1.5834 -0.0087 0.1309 0.1268 61 LYS A CD 489 C CE . LYS A 84 ? 1.4916 1.1306 1.6184 0.0036 0.1296 0.1206 61 LYS A CE 490 N NZ . LYS A 84 ? 1.4985 1.1124 1.6144 0.0237 0.1311 0.1397 61 LYS A NZ 491 N N . SER A 85 ? 1.1510 0.8700 1.2247 0.0382 0.0901 0.1700 62 SER A N 492 C CA . SER A 85 ? 1.1286 0.8403 1.1986 0.0592 0.0831 0.1809 62 SER A CA 493 C C . SER A 85 ? 1.0385 0.7855 1.1099 0.0703 0.0655 0.1800 62 SER A C 494 O O . SER A 85 ? 1.0749 0.8228 1.1503 0.0872 0.0585 0.1853 62 SER A O 495 C CB . SER A 85 ? 1.1475 0.8384 1.2332 0.0633 0.0898 0.1736 62 SER A CB 496 O OG . SER A 85 ? 1.0473 0.7596 1.1511 0.0548 0.0871 0.1532 62 SER A OG 497 N N . ARG A 86 ? 1.0094 0.7852 1.0789 0.0610 0.0587 0.1731 63 ARG A N 498 C CA . ARG A 86 ? 0.9829 0.7911 1.0544 0.0691 0.0427 0.1711 63 ARG A CA 499 C C . ARG A 86 ? 0.8600 0.6902 0.9204 0.0601 0.0371 0.1692 63 ARG A C 500 O O . ARG A 86 ? 0.9097 0.7677 0.9736 0.0619 0.0252 0.1636 63 ARG A O 501 C CB . ARG A 86 ? 1.0634 0.8890 1.1572 0.0684 0.0395 0.1552 63 ARG A CB 502 C CG . ARG A 86 ? 1.2226 1.0707 1.3240 0.0829 0.0262 0.1569 63 ARG A CG 503 C CD . ARG A 86 ? 1.2708 1.1414 1.3912 0.0783 0.0239 0.1403 63 ARG A CD 504 N NE . ARG A 86 ? 1.3014 1.1955 1.4184 0.0660 0.0186 0.1320 63 ARG A NE 505 C CZ . ARG A 86 ? 1.3193 1.2393 1.4358 0.0689 0.0067 0.1323 63 ARG A CZ 506 N NH1 . ARG A 86 ? 1.2971 1.2262 1.4179 0.0830 -0.0023 0.1398 63 ARG A NH1 507 N NH2 . ARG A 86 ? 1.2640 1.2009 1.3766 0.0577 0.0034 0.1247 63 ARG A NH2 508 N N . LEU A 87 ? 0.7930 0.6098 0.8408 0.0503 0.0467 0.1736 64 LEU A N 509 C CA . LEU A 87 ? 0.8281 0.6633 0.8665 0.0410 0.0443 0.1706 64 LEU A CA 510 C C . LEU A 87 ? 0.8989 0.7498 0.9205 0.0514 0.0308 0.1785 64 LEU A C 511 O O . LEU A 87 ? 0.8946 0.7684 0.9142 0.0464 0.0238 0.1714 64 LEU A O 512 C CB . LEU A 87 ? 0.7949 0.6110 0.8232 0.0303 0.0591 0.1759 64 LEU A CB 513 C CG . LEU A 87 ? 0.8581 0.6916 0.8793 0.0200 0.0601 0.1717 64 LEU A CG 514 C CD1 . LEU A 87 ? 0.6994 0.5592 0.7391 0.0113 0.0543 0.1536 64 LEU A CD1 515 C CD2 . LEU A 87 ? 0.8460 0.6605 0.8625 0.0089 0.0773 0.1764 64 LEU A CD2 516 N N . SER A 88 ? 0.9854 0.8232 0.9949 0.0661 0.0266 0.1929 65 SER A N 517 C CA . SER A 88 ? 1.0310 0.8824 1.0228 0.0767 0.0126 0.2009 65 SER A CA 518 C C . SER A 88 ? 0.9248 0.8070 0.9328 0.0810 -0.0029 0.1908 65 SER A C 519 O O . SER A 88 ? 0.9395 0.8409 0.9377 0.0828 -0.0148 0.1902 65 SER A O 520 C CB . SER A 88 ? 1.1312 0.9599 1.1053 0.0927 0.0114 0.2197 65 SER A CB 521 O OG . SER A 88 ? 1.2553 1.0978 1.2102 0.1029 -0.0036 0.2269 65 SER A OG 522 N N . ASP A 89 ? 0.8185 0.7045 0.8512 0.0819 -0.0019 0.1824 66 ASP A N 523 C CA . ASP A 89 ? 0.8947 0.8088 0.9454 0.0854 -0.0139 0.1729 66 ASP A CA 524 C C . ASP A 89 ? 0.8970 0.8296 0.9585 0.0708 -0.0129 0.1568 66 ASP A C 525 O O . ASP A 89 ? 0.9119 0.8683 0.9848 0.0710 -0.0220 0.1490 66 ASP A O 526 C CB . ASP A 89 ? 1.0562 0.9657 1.1272 0.0960 -0.0130 0.1728 66 ASP A CB 527 C CG . ASP A 89 ? 1.2256 1.1210 1.2876 0.1139 -0.0176 0.1891 66 ASP A CG 528 O OD1 . ASP A 89 ? 1.2527 1.1543 1.2962 0.1202 -0.0281 0.1984 66 ASP A OD1 529 O OD2 . ASP A 89 ? 1.2656 1.1430 1.3377 0.1224 -0.0110 0.1925 66 ASP A OD2 530 N N . VAL A 90 ? 0.8008 0.7227 0.8592 0.0583 -0.0016 0.1522 67 VAL A N 531 C CA . VAL A 90 ? 0.7030 0.6405 0.7696 0.0456 -0.0007 0.1379 67 VAL A CA 532 C C . VAL A 90 ? 0.6085 0.5647 0.6635 0.0433 -0.0102 0.1365 67 VAL A C 533 O O . VAL A 90 ? 0.6330 0.5836 0.6687 0.0439 -0.0102 0.1443 67 VAL A O 534 C CB . VAL A 90 ? 0.7357 0.6592 0.8024 0.0336 0.0122 0.1336 67 VAL A CB 535 C CG1 . VAL A 90 ? 0.7226 0.6636 0.7942 0.0224 0.0110 0.1207 67 VAL A CG1 536 C CG2 . VAL A 90 ? 0.7217 0.6272 0.8017 0.0336 0.0213 0.1311 67 VAL A CG2 537 N N . SER A 91 ? 0.4946 0.4713 0.5602 0.0405 -0.0172 0.1265 68 SER A N 538 C CA . SER A 91 ? 0.5282 0.5208 0.5837 0.0378 -0.0260 0.1239 68 SER A CA 539 C C . SER A 91 ? 0.6040 0.5934 0.6490 0.0279 -0.0197 0.1201 68 SER A C 540 O O . SER A 91 ? 0.4939 0.4756 0.5456 0.0212 -0.0101 0.1158 68 SER A O 541 C CB . SER A 91 ? 0.4636 0.4763 0.5340 0.0360 -0.0331 0.1141 68 SER A CB 542 O OG . SER A 91 ? 0.5979 0.6127 0.6748 0.0263 -0.0271 0.1037 68 SER A OG 543 N N . SER A 92 ? 0.6016 0.5978 0.6309 0.0272 -0.0253 0.1208 69 SER A N 544 C CA . SER A 92 ? 0.5402 0.5353 0.5600 0.0195 -0.0194 0.1170 69 SER A CA 545 C C . SER A 92 ? 0.4953 0.4983 0.5299 0.0113 -0.0165 0.1051 69 SER A C 546 O O . SER A 92 ? 0.4786 0.4774 0.5159 0.0053 -0.0080 0.1021 69 SER A O 547 C CB . SER A 92 ? 0.5317 0.5336 0.5326 0.0209 -0.0270 0.1176 69 SER A CB 548 O OG . SER A 92 ? 0.5343 0.5511 0.5417 0.0208 -0.0377 0.1106 69 SER A OG 549 N N . GLY A 93 ? 0.4740 0.4888 0.5181 0.0113 -0.0236 0.0986 70 GLY A N 550 C CA . GLY A 93 ? 0.4892 0.5103 0.5440 0.0050 -0.0217 0.0884 70 GLY A CA 551 C C . GLY A 93 ? 0.5013 0.5152 0.5687 0.0023 -0.0138 0.0856 70 GLY A C 552 O O . GLY A 93 ? 0.5176 0.5329 0.5889 -0.0037 -0.0101 0.0784 70 GLY A O 553 N N . GLU A 94 ? 0.4847 0.4905 0.5583 0.0073 -0.0117 0.0906 71 GLU A N 554 C CA . GLU A 94 ? 0.5390 0.5349 0.6237 0.0049 -0.0039 0.0872 71 GLU A CA 555 C C . GLU A 94 ? 0.4397 0.4252 0.5212 -0.0011 0.0045 0.0883 71 GLU A C 556 O O . GLU A 94 ? 0.5009 0.4849 0.5908 -0.0078 0.0095 0.0804 71 GLU A O 557 C CB . GLU A 94 ? 0.6219 0.6090 0.7131 0.0131 -0.0030 0.0931 71 GLU A CB 558 C CG . GLU A 94 ? 0.7226 0.7214 0.8246 0.0178 -0.0083 0.0892 71 GLU A CG 559 C CD . GLU A 94 ? 0.7335 0.7251 0.8434 0.0281 -0.0077 0.0957 71 GLU A CD 560 O OE1 . GLU A 94 ? 0.6521 0.6302 0.7547 0.0332 -0.0061 0.1057 71 GLU A OE1 561 O OE2 . GLU A 94 ? 0.8062 0.8052 0.9293 0.0316 -0.0083 0.0911 71 GLU A OE2 562 N N . LEU A 95 ? 0.4175 0.3967 0.4868 0.0012 0.0062 0.0977 72 LEU A N 563 C CA . LEU A 95 ? 0.4270 0.3973 0.4937 -0.0050 0.0159 0.0998 72 LEU A CA 564 C C . LEU A 95 ? 0.4741 0.4579 0.5422 -0.0121 0.0158 0.0913 72 LEU A C 565 O O . LEU A 95 ? 0.4836 0.4666 0.5602 -0.0196 0.0230 0.0865 72 LEU A O 566 C CB . LEU A 95 ? 0.4905 0.4501 0.5402 0.0000 0.0184 0.1129 72 LEU A CB 567 C CG . LEU A 95 ? 0.6178 0.5675 0.6639 -0.0068 0.0308 0.1165 72 LEU A CG 568 C CD1 . LEU A 95 ? 0.6493 0.5867 0.7113 -0.0134 0.0403 0.1131 72 LEU A CD1 569 C CD2 . LEU A 95 ? 0.7166 0.6531 0.7415 -0.0006 0.0339 0.1309 72 LEU A CD2 570 N N . ALA A 96 ? 0.4770 0.4732 0.5377 -0.0095 0.0076 0.0891 73 ALA A N 571 C CA . ALA A 96 ? 0.5242 0.5323 0.5854 -0.0139 0.0066 0.0813 73 ALA A CA 572 C C . ALA A 96 ? 0.4724 0.4860 0.5483 -0.0191 0.0067 0.0709 73 ALA A C 573 O O . ALA A 96 ? 0.4609 0.4801 0.5432 -0.0243 0.0102 0.0655 73 ALA A O 574 C CB . ALA A 96 ? 0.4408 0.4575 0.4914 -0.0100 -0.0024 0.0804 73 ALA A CB 575 N N . LEU A 97 ? 0.4429 0.4559 0.5240 -0.0172 0.0028 0.0679 74 LEU A N 576 C CA . LEU A 97 ? 0.5027 0.5191 0.5938 -0.0214 0.0026 0.0579 74 LEU A CA 577 C C . LEU A 97 ? 0.5066 0.5155 0.6081 -0.0274 0.0102 0.0550 74 LEU A C 578 O O . LEU A 97 ? 0.4960 0.5111 0.6050 -0.0329 0.0102 0.0460 74 LEU A O 579 C CB . LEU A 97 ? 0.4253 0.4412 0.5185 -0.0179 -0.0009 0.0558 74 LEU A CB 580 C CG . LEU A 97 ? 0.5233 0.5486 0.6102 -0.0152 -0.0079 0.0547 74 LEU A CG 581 C CD1 . LEU A 97 ? 0.5015 0.5266 0.5933 -0.0123 -0.0089 0.0533 74 LEU A CD1 582 C CD2 . LEU A 97 ? 0.4348 0.4676 0.5187 -0.0186 -0.0105 0.0476 74 LEU A CD2 583 N N . ILE A 98 ? 0.5907 0.5858 0.6925 -0.0263 0.0163 0.0626 75 ILE A N 584 C CA . ILE A 98 ? 0.5017 0.4860 0.6134 -0.0331 0.0251 0.0605 75 ILE A CA 585 C C . ILE A 98 ? 0.4567 0.4494 0.5731 -0.0404 0.0292 0.0578 75 ILE A C 586 O O . ILE A 98 ? 0.4961 0.4929 0.6253 -0.0484 0.0314 0.0485 75 ILE A O 587 C CB . ILE A 98 ? 0.4917 0.4563 0.5999 -0.0294 0.0317 0.0715 75 ILE A CB 588 C CG1 . ILE A 98 ? 0.4621 0.4191 0.5719 -0.0224 0.0289 0.0718 75 ILE A CG1 589 C CG2 . ILE A 98 ? 0.4094 0.3610 0.5265 -0.0382 0.0428 0.0707 75 ILE A CG2 590 C CD1 . ILE A 98 ? 0.4725 0.4096 0.5787 -0.0161 0.0341 0.0833 75 ILE A CD1 591 N N . ILE A 99 ? 0.4735 0.4700 0.5800 -0.0376 0.0300 0.0653 76 ILE A N 592 C CA . ILE A 99 ? 0.5368 0.5429 0.6481 -0.0432 0.0352 0.0634 76 ILE A CA 593 C C . ILE A 99 ? 0.5598 0.5850 0.6798 -0.0453 0.0283 0.0517 76 ILE A C 594 O O . ILE A 99 ? 0.4814 0.5159 0.6160 -0.0524 0.0317 0.0448 76 ILE A O 595 C CB . ILE A 99 ? 0.5737 0.5796 0.6689 -0.0381 0.0373 0.0731 76 ILE A CB 596 C CG1 . ILE A 99 ? 0.6290 0.6150 0.7135 -0.0354 0.0441 0.0857 76 ILE A CG1 597 C CG2 . ILE A 99 ? 0.5450 0.5630 0.6464 -0.0430 0.0436 0.0700 76 ILE A CG2 598 C CD1 . ILE A 99 ? 0.5602 0.5438 0.6242 -0.0297 0.0454 0.0955 76 ILE A CD1 599 N N . LEU A 100 ? 0.4836 0.5147 0.5952 -0.0392 0.0186 0.0497 77 LEU A N 600 C CA . LEU A 100 ? 0.5102 0.5564 0.6259 -0.0393 0.0114 0.0403 77 LEU A CA 601 C C . LEU A 100 ? 0.5408 0.5892 0.6694 -0.0451 0.0100 0.0302 77 LEU A C 602 O O . LEU A 100 ? 0.6023 0.6640 0.7416 -0.0489 0.0080 0.0222 77 LEU A O 603 C CB . LEU A 100 ? 0.3514 0.3988 0.4538 -0.0323 0.0028 0.0411 77 LEU A CB 604 C CG . LEU A 100 ? 0.5138 0.5611 0.6026 -0.0269 0.0018 0.0481 77 LEU A CG 605 C CD1 . LEU A 100 ? 0.4928 0.5396 0.5713 -0.0222 -0.0061 0.0479 77 LEU A CD1 606 C CD2 . LEU A 100 ? 0.4573 0.5150 0.5477 -0.0269 0.0038 0.0459 77 LEU A CD2 607 N N . ALA A 101 ? 0.4498 0.4857 0.5775 -0.0454 0.0106 0.0300 78 ALA A N 608 C CA . ALA A 101 ? 0.5031 0.5380 0.6401 -0.0509 0.0097 0.0194 78 ALA A CA 609 C C . ALA A 101 ? 0.5519 0.5877 0.7054 -0.0608 0.0164 0.0147 78 ALA A C 610 O O . ALA A 101 ? 0.5942 0.6392 0.7580 -0.0666 0.0128 0.0033 78 ALA A O 611 C CB . ALA A 101 ? 0.3850 0.4043 0.5175 -0.0483 0.0112 0.0206 78 ALA A CB 612 N N . LEU A 102 ? 0.5282 0.5544 0.6838 -0.0630 0.0260 0.0234 79 LEU A N 613 C CA . LEU A 102 ? 0.5385 0.5632 0.7107 -0.0738 0.0349 0.0199 79 LEU A CA 614 C C . LEU A 102 ? 0.4483 0.4951 0.6325 -0.0778 0.0347 0.0157 79 LEU A C 615 O O . LEU A 102 ? 0.5494 0.6027 0.7526 -0.0881 0.0396 0.0087 79 LEU A O 616 C CB . LEU A 102 ? 0.5479 0.5517 0.7160 -0.0746 0.0469 0.0322 79 LEU A CB 617 C CG . LEU A 102 ? 0.5977 0.5774 0.7609 -0.0726 0.0500 0.0353 79 LEU A CG 618 C CD1 . LEU A 102 ? 0.4756 0.4351 0.6302 -0.0700 0.0603 0.0503 79 LEU A CD1 619 C CD2 . LEU A 102 ? 0.5312 0.5047 0.7095 -0.0828 0.0525 0.0227 79 LEU A CD2 620 N N . GLY A 103 ? 0.4718 0.5305 0.6464 -0.0696 0.0294 0.0194 80 GLY A N 621 C CA . GLY A 103 ? 0.5482 0.6271 0.7337 -0.0710 0.0306 0.0168 80 GLY A CA 622 C C . GLY A 103 ? 0.6484 0.7461 0.8327 -0.0645 0.0184 0.0100 80 GLY A C 623 O O . GLY A 103 ? 0.7729 0.8841 0.9592 -0.0605 0.0188 0.0112 80 GLY A O 624 N N . VAL A 104 ? 0.5983 0.6955 0.7781 -0.0627 0.0084 0.0033 81 VAL A N 625 C CA . VAL A 104 ? 0.6347 0.7472 0.8113 -0.0562 -0.0034 -0.0026 81 VAL A CA 626 C C . VAL A 104 ? 0.6909 0.8268 0.8894 -0.0600 -0.0048 -0.0108 81 VAL A C 627 O O . VAL A 104 ? 0.7073 0.8580 0.9062 -0.0528 -0.0099 -0.0113 81 VAL A O 628 C CB . VAL A 104 ? 0.5915 0.6990 0.7601 -0.0556 -0.0123 -0.0096 81 VAL A CB 629 C CG1 . VAL A 104 ? 0.5208 0.6416 0.6827 -0.0481 -0.0241 -0.0140 81 VAL A CG1 630 C CG2 . VAL A 104 ? 0.6451 0.7321 0.7963 -0.0521 -0.0099 -0.0024 81 VAL A CG2 631 N N . CYS A 105 ? 0.6036 0.7429 0.8217 -0.0713 0.0000 -0.0174 82 CYS A N 632 C CA . CYS A 105 ? 0.6601 0.8238 0.9048 -0.0773 0.0002 -0.0258 82 CYS A CA 633 C C . CYS A 105 ? 0.6919 0.8499 0.9550 -0.0913 0.0137 -0.0266 82 CYS A C 634 O O . CYS A 105 ? 0.7161 0.8501 0.9701 -0.0955 0.0202 -0.0223 82 CYS A O 635 C CB . CYS A 105 ? 0.6347 0.8149 0.8866 -0.0774 -0.0146 -0.0391 82 CYS A CB 636 S SG . CYS A 105 ? 0.9122 1.0727 1.1509 -0.0821 -0.0199 -0.0458 82 CYS A SG 637 N N . ARG A 106 ? 0.7518 0.9314 1.0416 -0.0982 0.0185 -0.0319 83 ARG A N 638 C CA . ARG A 106 ? 0.8321 1.0061 1.1407 -0.1128 0.0334 -0.0322 83 ARG A CA 639 C C . ARG A 106 ? 0.8416 1.0091 1.1612 -0.1249 0.0303 -0.0437 83 ARG A C 640 O O . ARG A 106 ? 0.8951 1.0831 1.2297 -0.1281 0.0183 -0.0578 83 ARG A O 641 C CB . ARG A 106 ? 0.8986 1.1000 1.2356 -0.1177 0.0407 -0.0354 83 ARG A CB 642 C CG . ARG A 106 ? 1.0014 1.1982 1.3604 -0.1346 0.0577 -0.0361 83 ARG A CG 643 C CD . ARG A 106 ? 1.0946 1.2845 1.4486 -0.1335 0.0759 -0.0226 83 ARG A CD 644 N NE . ARG A 106 ? 1.2439 1.4300 1.6198 -0.1503 0.0938 -0.0228 83 ARG A NE 645 C CZ . ARG A 106 ? 1.3105 1.5251 1.7218 -0.1605 0.1002 -0.0314 83 ARG A CZ 646 N NH1 . ARG A 106 ? 1.3279 1.5781 1.7568 -0.1538 0.0889 -0.0405 83 ARG A NH1 647 N NH2 . ARG A 106 ? 1.3174 1.5252 1.7475 -0.1771 0.1183 -0.0308 83 ARG A NH2 648 N N . ASN A 107 ? 0.7903 0.9283 1.1011 -0.1309 0.0407 -0.0380 84 ASN A N 649 C CA . ASN A 107 ? 0.8190 0.9458 1.1404 -0.1436 0.0412 -0.0488 84 ASN A CA 650 C C . ASN A 107 ? 0.8803 0.9773 1.2007 -0.1522 0.0594 -0.0398 84 ASN A C 651 O O . ASN A 107 ? 0.9283 1.0162 1.2400 -0.1483 0.0709 -0.0252 84 ASN A O 652 C CB . ASN A 107 ? 0.7988 0.9149 1.1004 -0.1369 0.0279 -0.0545 84 ASN A CB 653 C CG . ASN A 107 ? 0.8378 0.9259 1.1106 -0.1261 0.0316 -0.0406 84 ASN A CG 654 O OD1 . ASN A 107 ? 1.0716 1.1544 1.3342 -0.1193 0.0384 -0.0266 84 ASN A OD1 655 N ND2 . ASN A 107 ? 0.8106 0.8818 1.0703 -0.1243 0.0268 -0.0452 84 ASN A ND2 656 N N . ALA A 108 ? 0.9047 0.9850 1.2322 -0.1633 0.0620 -0.0484 85 ALA A N 657 C CA . ALA A 108 ? 0.9238 0.9724 1.2507 -0.1716 0.0796 -0.0401 85 ALA A CA 658 C C . ALA A 108 ? 0.9260 0.9455 1.2218 -0.1578 0.0831 -0.0232 85 ALA A C 659 O O . ALA A 108 ? 0.9532 0.9516 1.2423 -0.1584 0.0976 -0.0092 85 ALA A O 660 C CB . ALA A 108 ? 0.8002 0.8354 1.1408 -0.1862 0.0807 -0.0548 85 ALA A CB 661 N N . GLU A 109 ? 0.8596 0.8789 1.1367 -0.1453 0.0698 -0.0244 86 GLU A N 662 C CA . GLU A 109 ? 0.9099 0.9058 1.1610 -0.1320 0.0710 -0.0103 86 GLU A CA 663 C C . GLU A 109 ? 0.7911 0.7930 1.0289 -0.1218 0.0733 0.0051 86 GLU A C 664 O O . GLU A 109 ? 0.6863 0.6686 0.9051 -0.1129 0.0773 0.0188 86 GLU A O 665 C CB . GLU A 109 ? 0.9990 0.9952 1.2364 -0.1228 0.0573 -0.0170 86 GLU A CB 666 C CG . GLU A 109 ? 1.1129 1.0928 1.3548 -0.1300 0.0572 -0.0297 86 GLU A CG 667 C CD . GLU A 109 ? 1.0990 1.0976 1.3619 -0.1435 0.0519 -0.0485 86 GLU A CD 668 O OE1 . GLU A 109 ? 0.9537 0.9371 1.2243 -0.1536 0.0550 -0.0596 86 GLU A OE1 669 O OE2 . GLU A 109 ? 1.1381 1.1665 1.4100 -0.1437 0.0440 -0.0526 86 GLU A OE2 670 N N . GLU A 110 ? 0.7567 0.7861 1.0046 -0.1227 0.0705 0.0021 87 GLU A N 671 C CA . GLU A 110 ? 0.6727 0.7087 0.9082 -0.1137 0.0731 0.0144 87 GLU A CA 672 C C . GLU A 110 ? 0.7111 0.7288 0.9434 -0.1179 0.0906 0.0276 87 GLU A C 673 O O . GLU A 110 ? 0.6560 0.6677 0.8692 -0.1089 0.0939 0.0406 87 GLU A O 674 C CB . GLU A 110 ? 0.5769 0.6459 0.8266 -0.1137 0.0674 0.0068 87 GLU A CB 675 C CG . GLU A 110 ? 0.7064 0.7825 0.9402 -0.1021 0.0671 0.0169 87 GLU A CG 676 C CD . GLU A 110 ? 0.7090 0.8160 0.9591 -0.1017 0.0640 0.0097 87 GLU A CD 677 O OE1 . GLU A 110 ? 0.6854 0.8008 0.9223 -0.0903 0.0578 0.0131 87 GLU A OE1 678 O OE2 . GLU A 110 ? 0.7347 0.8579 1.0120 -0.1127 0.0678 0.0004 87 GLU A OE2 679 N N . ASN A 111 ? 0.6281 0.6357 0.8779 -0.1320 0.1021 0.0239 88 ASN A N 680 C CA . ASN A 111 ? 0.6804 0.6660 0.9261 -0.1371 0.1205 0.0370 88 ASN A CA 681 C C . ASN A 111 ? 0.7500 0.7037 0.9672 -0.1261 0.1226 0.0526 88 ASN A C 682 O O . ASN A 111 ? 0.8368 0.7744 1.0397 -0.1239 0.1345 0.0675 88 ASN A O 683 C CB . ASN A 111 ? 0.7716 0.7490 1.0422 -0.1556 0.1323 0.0290 88 ASN A CB 684 C CG . ASN A 111 ? 0.8478 0.8552 1.1474 -0.1679 0.1379 0.0199 88 ASN A CG 685 O OD1 . ASN A 111 ? 0.8782 0.9145 1.1971 -0.1708 0.1257 0.0043 88 ASN A OD1 686 N ND2 . ASN A 111 ? 0.9723 0.9734 1.2751 -0.1747 0.1566 0.0298 88 ASN A ND2 687 N N . LEU A 112 ? 0.6321 0.5775 0.8410 -0.1186 0.1110 0.0490 89 LEU A N 688 C CA . LEU A 112 ? 0.5954 0.5140 0.7813 -0.1069 0.1110 0.0623 89 LEU A CA 689 C C . LEU A 112 ? 0.6525 0.5759 0.8158 -0.0939 0.1079 0.0756 89 LEU A C 690 O O . LEU A 112 ? 0.6902 0.5920 0.8341 -0.0858 0.1121 0.0903 89 LEU A O 691 C CB . LEU A 112 ? 0.6895 0.6047 0.8735 -0.1007 0.0988 0.0541 89 LEU A CB 692 C CG . LEU A 112 ? 0.8613 0.7563 1.0569 -0.1090 0.1033 0.0452 89 LEU A CG 693 C CD1 . LEU A 112 ? 0.9305 0.8411 1.1510 -0.1255 0.1044 0.0282 89 LEU A CD1 694 C CD2 . LEU A 112 ? 0.7885 0.6787 0.9762 -0.0989 0.0926 0.0404 89 LEU A CD2 695 N N . ILE A 113 ? 0.6115 0.5627 0.7766 -0.0915 0.0998 0.0701 90 ILE A N 696 C CA . ILE A 113 ? 0.6565 0.6134 0.8008 -0.0805 0.0966 0.0801 90 ILE A CA 697 C C . ILE A 113 ? 0.6439 0.5891 0.7787 -0.0830 0.1123 0.0928 90 ILE A C 698 O O . ILE A 113 ? 0.8087 0.7401 0.9190 -0.0735 0.1131 0.1063 90 ILE A O 699 C CB . ILE A 113 ? 0.6175 0.6045 0.7678 -0.0787 0.0873 0.0707 90 ILE A CB 700 C CG1 . ILE A 113 ? 0.6022 0.5996 0.7587 -0.0760 0.0725 0.0590 90 ILE A CG1 701 C CG2 . ILE A 113 ? 0.5936 0.5838 0.7214 -0.0682 0.0849 0.0799 90 ILE A CG2 702 C CD1 . ILE A 113 ? 0.4029 0.4273 0.5654 -0.0740 0.0632 0.0498 90 ILE A CD1 703 N N . TYR A 114 ? 0.6764 0.6275 0.8306 -0.0961 0.1247 0.0882 91 TYR A N 704 C CA . TYR A 114 ? 0.7093 0.6517 0.8559 -0.1000 0.1420 0.0994 91 TYR A CA 705 C C . TYR A 114 ? 0.6043 0.5129 0.7459 -0.1055 0.1562 0.1101 91 TYR A C 706 O O . TYR A 114 ? 0.8259 0.7173 0.9490 -0.1041 0.1693 0.1247 91 TYR A O 707 C CB . TYR A 114 ? 0.6909 0.6596 0.8625 -0.1110 0.1498 0.0896 91 TYR A CB 708 C CG . TYR A 114 ? 0.7340 0.7340 0.9108 -0.1042 0.1356 0.0792 91 TYR A CG 709 C CD1 . TYR A 114 ? 0.7849 0.7908 0.9400 -0.0930 0.1330 0.0856 91 TYR A CD1 710 C CD2 . TYR A 114 ? 0.6655 0.6869 0.8667 -0.1086 0.1244 0.0632 91 TYR A CD2 711 C CE1 . TYR A 114 ? 0.7204 0.7511 0.8793 -0.0865 0.1208 0.0766 91 TYR A CE1 712 C CE2 . TYR A 114 ? 0.7248 0.7719 0.9286 -0.1013 0.1116 0.0551 91 TYR A CE2 713 C CZ . TYR A 114 ? 0.7521 0.8028 0.9353 -0.0903 0.1104 0.0621 91 TYR A CZ 714 O OH . TYR A 114 ? 0.8007 0.8732 0.9857 -0.0827 0.0985 0.0544 91 TYR A OH 715 N N . ASP A 115 ? 0.5819 0.4790 0.7379 -0.1112 0.1540 0.1030 92 ASP A N 716 C CA . ASP A 115 ? 0.7883 0.6495 0.9399 -0.1157 0.1671 0.1125 92 ASP A CA 717 C C . ASP A 115 ? 0.7856 0.6219 0.9072 -0.0991 0.1616 0.1278 92 ASP A C 718 O O . ASP A 115 ? 0.7792 0.5839 0.8865 -0.0979 0.1736 0.1422 92 ASP A O 719 C CB . ASP A 115 ? 0.9311 0.7871 1.1083 -0.1276 0.1669 0.0980 92 ASP A CB 720 C CG . ASP A 115 ? 1.0282 0.9047 1.2367 -0.1463 0.1750 0.0844 92 ASP A CG 721 O OD1 . ASP A 115 ? 1.0734 0.9578 1.2844 -0.1520 0.1878 0.0901 92 ASP A OD1 722 O OD2 . ASP A 115 ? 1.0699 0.9557 1.3011 -0.1552 0.1685 0.0676 92 ASP A OD2 723 N N . TYR A 116 ? 0.7366 0.5876 0.8494 -0.0862 0.1437 0.1248 93 TYR A N 724 C CA . TYR A 116 ? 0.7680 0.6019 0.8564 -0.0698 0.1359 0.1375 93 TYR A CA 725 C C . TYR A 116 ? 0.7369 0.5812 0.8007 -0.0590 0.1307 0.1473 93 TYR A C 726 O O . TYR A 116 ? 0.8019 0.6357 0.8443 -0.0452 0.1231 0.1582 93 TYR A O 727 C CB . TYR A 116 ? 0.7852 0.6267 0.8815 -0.0631 0.1202 0.1275 93 TYR A CB 728 C CG . TYR A 116 ? 0.9264 0.7530 1.0416 -0.0712 0.1244 0.1181 93 TYR A CG 729 C CD1 . TYR A 116 ? 0.9292 0.7251 1.0459 -0.0782 0.1401 0.1248 93 TYR A CD1 730 C CD2 . TYR A 116 ? 0.9388 0.7801 1.0684 -0.0720 0.1132 0.1023 93 TYR A CD2 731 C CE1 . TYR A 116 ? 0.9476 0.7278 1.0809 -0.0861 0.1441 0.1149 93 TYR A CE1 732 C CE2 . TYR A 116 ? 1.0164 0.8434 1.1609 -0.0793 0.1169 0.0923 93 TYR A CE2 733 C CZ . TYR A 116 ? 1.0729 0.8693 1.2198 -0.0866 0.1321 0.0980 93 TYR A CZ 734 O OH . TYR A 116 ? 1.1780 0.9581 1.3393 -0.0944 0.1360 0.0868 93 TYR A OH 735 N N . HIS A 117 ? 0.6914 0.5570 0.7592 -0.0652 0.1344 0.1424 94 HIS A N 736 C CA . HIS A 117 ? 0.7620 0.6386 0.8071 -0.0562 0.1300 0.1486 94 HIS A CA 737 C C . HIS A 117 ? 0.7561 0.6455 0.7925 -0.0437 0.1099 0.1453 94 HIS A C 738 O O . HIS A 117 ? 0.8074 0.6915 0.8185 -0.0324 0.1038 0.1553 94 HIS A O 739 C CB . HIS A 117 ? 0.7424 0.5938 0.7586 -0.0514 0.1416 0.1676 94 HIS A CB 740 C CG . HIS A 117 ? 0.7198 0.5629 0.7418 -0.0642 0.1635 0.1712 94 HIS A CG 741 N ND1 . HIS A 117 ? 0.8659 0.7193 0.8773 -0.0662 0.1731 0.1738 94 HIS A ND1 742 C CD2 . HIS A 117 ? 0.7783 0.6041 0.8168 -0.0766 0.1787 0.1719 94 HIS A CD2 743 C CE1 . HIS A 117 ? 0.8662 0.7105 0.8884 -0.0793 0.1938 0.1765 94 HIS A CE1 744 N NE2 . HIS A 117 ? 0.8063 0.6334 0.8453 -0.0864 0.1974 0.1753 94 HIS A NE2 745 N N . LEU A 118 ? 0.6576 0.5640 0.7145 -0.0463 0.0997 0.1309 95 LEU A N 746 C CA . LEU A 118 ? 0.7092 0.6272 0.7616 -0.0365 0.0824 0.1268 95 LEU A CA 747 C C . LEU A 118 ? 0.6755 0.6111 0.7141 -0.0313 0.0753 0.1259 95 LEU A C 748 O O . LEU A 118 ? 0.5751 0.5138 0.6003 -0.0218 0.0632 0.1283 95 LEU A O 749 C CB . LEU A 118 ? 0.5552 0.4854 0.6309 -0.0414 0.0755 0.1118 95 LEU A CB 750 C CG . LEU A 118 ? 0.6608 0.5729 0.7497 -0.0462 0.0811 0.1101 95 LEU A CG 751 C CD1 . LEU A 118 ? 0.5956 0.5203 0.7023 -0.0495 0.0727 0.0947 95 LEU A CD1 752 C CD2 . LEU A 118 ? 0.6431 0.5323 0.7172 -0.0355 0.0804 0.1232 95 LEU A CD2 753 N N . ILE A 119 ? 0.5594 0.5068 0.6027 -0.0379 0.0831 0.1216 96 ILE A N 754 C CA . ILE A 119 ? 0.5713 0.5329 0.6011 -0.0331 0.0786 0.1200 96 ILE A CA 755 C C . ILE A 119 ? 0.6833 0.6307 0.6819 -0.0248 0.0799 0.1336 96 ILE A C 756 O O . ILE A 119 ? 0.6505 0.6031 0.6326 -0.0167 0.0685 0.1338 96 ILE A O 757 C CB . ILE A 119 ? 0.6453 0.6223 0.6884 -0.0409 0.0888 0.1130 96 ILE A CB 758 C CG1 . ILE A 119 ? 0.6472 0.6421 0.7190 -0.0472 0.0834 0.0985 96 ILE A CG1 759 C CG2 . ILE A 119 ? 0.5852 0.5720 0.6107 -0.0348 0.0867 0.1126 96 ILE A CG2 760 C CD1 . ILE A 119 ? 0.6640 0.6779 0.7532 -0.0538 0.0916 0.0907 96 ILE A CD1 761 N N . ASP A 120 ? 0.6481 0.5764 0.6379 -0.0272 0.0938 0.1449 97 ASP A N 762 C CA . ASP A 120 ? 0.7615 0.6731 0.7184 -0.0186 0.0954 0.1595 97 ASP A CA 763 C C . ASP A 120 ? 0.6845 0.5898 0.6306 -0.0075 0.0793 0.1644 97 ASP A C 764 O O . ASP A 120 ? 0.6925 0.5981 0.6142 0.0016 0.0702 0.1694 97 ASP A O 765 C CB . ASP A 120 ? 0.8693 0.7578 0.8192 -0.0234 0.1143 0.1719 97 ASP A CB 766 C CG . ASP A 120 ? 0.9638 0.8600 0.9213 -0.0338 0.1318 0.1686 97 ASP A CG 767 O OD1 . ASP A 120 ? 0.9794 0.8996 0.9576 -0.0387 0.1293 0.1547 97 ASP A OD1 768 O OD2 . ASP A 120 ? 1.1585 1.0367 1.1014 -0.0365 0.1486 0.1803 97 ASP A OD2 769 N N . LYS A 121 ? 0.5792 0.4801 0.5446 -0.0084 0.0756 0.1620 98 LYS A N 770 C CA . LYS A 121 ? 0.6714 0.5686 0.6322 0.0023 0.0615 0.1659 98 LYS A CA 771 C C . LYS A 121 ? 0.6543 0.5740 0.6170 0.0062 0.0450 0.1561 98 LYS A C 772 O O . LYS A 121 ? 0.7055 0.6267 0.6552 0.0159 0.0327 0.1605 98 LYS A O 773 C CB . LYS A 121 ? 0.7557 0.6428 0.7382 0.0002 0.0635 0.1640 98 LYS A CB 774 C CG . LYS A 121 ? 0.9642 0.8224 0.9407 -0.0006 0.0776 0.1766 98 LYS A CG 775 C CD . LYS A 121 ? 1.1628 1.0045 1.1116 0.0135 0.0729 0.1933 98 LYS A CD 776 C CE . LYS A 121 ? 1.3122 1.1216 1.2498 0.0129 0.0889 0.2081 98 LYS A CE 777 N NZ . LYS A 121 ? 1.3543 1.1488 1.3155 0.0074 0.0962 0.2044 98 LYS A NZ 778 N N . LEU A 122 ? 0.6354 0.5723 0.6147 -0.0014 0.0449 0.1428 99 LEU A N 779 C CA . LEU A 122 ? 0.6039 0.5595 0.5849 0.0010 0.0314 0.1333 99 LEU A CA 780 C C . LEU A 122 ? 0.6773 0.6361 0.6329 0.0059 0.0271 0.1363 99 LEU A C 781 O O . LEU A 122 ? 0.6460 0.6130 0.5949 0.0110 0.0139 0.1337 99 LEU A O 782 C CB . LEU A 122 ? 0.4496 0.4202 0.4514 -0.0073 0.0331 0.1198 99 LEU A CB 783 C CG . LEU A 122 ? 0.5466 0.5333 0.5502 -0.0054 0.0206 0.1104 99 LEU A CG 784 C CD1 . LEU A 122 ? 0.5126 0.5002 0.5212 -0.0005 0.0097 0.1104 99 LEU A CD1 785 C CD2 . LEU A 122 ? 0.5309 0.5301 0.5523 -0.0121 0.0226 0.0987 99 LEU A CD2 786 N N . GLU A 123 ? 0.6731 0.6249 0.6146 0.0037 0.0391 0.1412 100 GLU A N 787 C CA . GLU A 123 ? 0.6607 0.6126 0.5742 0.0084 0.0370 0.1440 100 GLU A CA 788 C C . GLU A 123 ? 0.7068 0.6495 0.5975 0.0185 0.0265 0.1543 100 GLU A C 789 O O . GLU A 123 ? 0.7307 0.6800 0.6048 0.0233 0.0150 0.1518 100 GLU A O 790 C CB . GLU A 123 ? 0.5949 0.5394 0.4973 0.0044 0.0547 0.1486 100 GLU A CB 791 C CG . GLU A 123 ? 0.6481 0.6064 0.5732 -0.0043 0.0638 0.1375 100 GLU A CG 792 C CD . GLU A 123 ? 0.7136 0.6661 0.6337 -0.0093 0.0835 0.1423 100 GLU A CD 793 O OE1 . GLU A 123 ? 0.7995 0.7349 0.6943 -0.0060 0.0907 0.1548 100 GLU A OE1 794 O OE2 . GLU A 123 ? 0.7270 0.6925 0.6689 -0.0164 0.0919 0.1338 100 GLU A OE2 795 N N . ASN A 124 ? 0.6762 0.6034 0.5666 0.0217 0.0301 0.1655 101 ASN A N 796 C CA . ASN A 124 ? 0.7286 0.6474 0.5995 0.0330 0.0193 0.1764 101 ASN A CA 797 C C . ASN A 124 ? 0.7227 0.6567 0.6086 0.0376 0.0012 0.1697 101 ASN A C 798 O O . ASN A 124 ? 0.7243 0.6646 0.5949 0.0449 -0.0129 0.1710 101 ASN A O 799 C CB . ASN A 124 ? 0.7560 0.6515 0.6234 0.0363 0.0290 0.1908 101 ASN A CB 800 C CG . ASN A 124 ? 1.0059 0.8847 0.8564 0.0314 0.0483 0.1991 101 ASN A CG 801 O OD1 . ASN A 124 ? 0.9439 0.8263 0.7747 0.0301 0.0520 0.1978 101 ASN A OD1 802 N ND2 . ASN A 124 ? 1.1453 1.0048 1.0037 0.0283 0.0617 0.2073 101 ASN A ND2 803 N N . LYS A 125 ? 0.6540 0.5946 0.5699 0.0328 0.0018 0.1621 102 LYS A N 804 C CA . LYS A 125 ? 0.6869 0.6425 0.6197 0.0360 -0.0126 0.1553 102 LYS A CA 805 C C . LYS A 125 ? 0.6916 0.6649 0.6211 0.0333 -0.0225 0.1445 102 LYS A C 806 O O . LYS A 125 ? 0.6415 0.6259 0.5715 0.0379 -0.0366 0.1423 102 LYS A O 807 C CB . LYS A 125 ? 0.6096 0.5668 0.5719 0.0307 -0.0077 0.1486 102 LYS A CB 808 C CG . LYS A 125 ? 0.6452 0.5839 0.6131 0.0345 -0.0003 0.1581 102 LYS A CG 809 C CD . LYS A 125 ? 0.6252 0.5659 0.6207 0.0295 0.0034 0.1493 102 LYS A CD 810 C CE . LYS A 125 ? 0.5666 0.4856 0.5671 0.0327 0.0121 0.1576 102 LYS A CE 811 N NZ . LYS A 125 ? 0.6034 0.5165 0.5963 0.0469 0.0036 0.1686 102 LYS A NZ 812 N N . PHE A 126 ? 0.6502 0.6261 0.5776 0.0258 -0.0149 0.1374 103 PHE A N 813 C CA . PHE A 126 ? 0.6797 0.6682 0.6021 0.0233 -0.0224 0.1273 103 PHE A CA 814 C C . PHE A 126 ? 0.7360 0.7227 0.6292 0.0292 -0.0306 0.1313 103 PHE A C 815 O O . PHE A 126 ? 0.7510 0.7480 0.6411 0.0298 -0.0431 0.1246 103 PHE A O 816 C CB . PHE A 126 ? 0.6452 0.6356 0.5716 0.0159 -0.0116 0.1197 103 PHE A CB 817 C CG . PHE A 126 ? 0.7040 0.7024 0.6208 0.0146 -0.0173 0.1104 103 PHE A CG 818 C CD1 . PHE A 126 ? 0.6624 0.6713 0.5917 0.0125 -0.0272 0.1013 103 PHE A CD1 819 C CD2 . PHE A 126 ? 0.7014 0.6950 0.5960 0.0153 -0.0114 0.1107 103 PHE A CD2 820 C CE1 . PHE A 126 ? 0.6388 0.6516 0.5588 0.0110 -0.0316 0.0928 103 PHE A CE1 821 C CE2 . PHE A 126 ? 0.7244 0.7228 0.6095 0.0145 -0.0160 0.1013 103 PHE A CE2 822 C CZ . PHE A 126 ? 0.6240 0.6311 0.5219 0.0122 -0.0263 0.0924 103 PHE A CZ 823 N N . GLN A 127 ? 0.7976 0.7700 0.6684 0.0332 -0.0231 0.1422 104 GLN A N 824 C CA . GLN A 127 ? 0.8226 0.7912 0.6608 0.0397 -0.0307 0.1470 104 GLN A CA 825 C C . GLN A 127 ? 0.7608 0.7344 0.5982 0.0483 -0.0476 0.1520 104 GLN A C 826 O O . GLN A 127 ? 0.8137 0.7931 0.6325 0.0524 -0.0609 0.1501 104 GLN A O 827 C CB . GLN A 127 ? 0.9241 0.8745 0.7367 0.0420 -0.0165 0.1587 104 GLN A CB 828 C CG . GLN A 127 ? 1.1269 1.0722 0.9004 0.0477 -0.0218 0.1618 104 GLN A CG 829 C CD . GLN A 127 ? 1.3002 1.2547 1.0667 0.0429 -0.0233 0.1477 104 GLN A CD 830 O OE1 . GLN A 127 ? 1.2644 1.2242 1.0495 0.0355 -0.0139 0.1389 104 GLN A OE1 831 N NE2 . GLN A 127 ? 1.3495 1.3054 1.0887 0.0474 -0.0358 0.1451 104 GLN A NE2 832 N N . ALA A 128 ? 0.6342 0.6060 0.4925 0.0512 -0.0473 0.1576 105 ALA A N 833 C CA . ALA A 128 ? 0.6966 0.6759 0.5604 0.0603 -0.0628 0.1619 105 ALA A CA 834 C C . ALA A 128 ? 0.7917 0.7935 0.6741 0.0566 -0.0765 0.1484 105 ALA A C 835 O O . ALA A 128 ? 0.9062 0.9196 0.7852 0.0624 -0.0927 0.1482 105 ALA A O 836 C CB . ALA A 128 ? 0.5987 0.5696 0.4823 0.0645 -0.0571 0.1699 105 ALA A CB 837 N N . GLU A 129 ? 0.6701 0.6781 0.5724 0.0467 -0.0701 0.1374 106 GLU A N 838 C CA . GLU A 129 ? 0.6624 0.6883 0.5805 0.0413 -0.0800 0.1247 106 GLU A CA 839 C C . GLU A 129 ? 0.6520 0.6818 0.5465 0.0403 -0.0895 0.1192 106 GLU A C 840 O O . GLU A 129 ? 0.6156 0.6596 0.5148 0.0405 -0.1040 0.1135 106 GLU A O 841 C CB . GLU A 129 ? 0.5606 0.5877 0.4971 0.0316 -0.0697 0.1154 106 GLU A CB 842 C CG . GLU A 129 ? 0.6497 0.6734 0.6092 0.0311 -0.0608 0.1179 106 GLU A CG 843 C CD . GLU A 129 ? 0.6985 0.7359 0.6832 0.0316 -0.0680 0.1134 106 GLU A CD 844 O OE1 . GLU A 129 ? 0.6172 0.6681 0.6038 0.0320 -0.0802 0.1091 106 GLU A OE1 845 O OE2 . GLU A 129 ? 0.5710 0.6059 0.5742 0.0310 -0.0610 0.1136 106 GLU A OE2 846 N N . ILE A 130 ? 0.7552 0.7726 0.6253 0.0389 -0.0806 0.1201 107 ILE A N 847 C CA . ILE A 130 ? 0.8321 0.8496 0.6758 0.0381 -0.0873 0.1141 107 ILE A CA 848 C C . ILE A 130 ? 0.8739 0.8939 0.6968 0.0468 -0.1024 0.1203 107 ILE A C 849 O O . ILE A 130 ? 0.8756 0.9062 0.6923 0.0456 -0.1169 0.1119 107 ILE A O 850 C CB . ILE A 130 ? 0.9174 0.9203 0.7383 0.0364 -0.0722 0.1153 107 ILE A CB 851 C CG1 . ILE A 130 ? 0.8746 0.8777 0.7168 0.0287 -0.0590 0.1086 107 ILE A CG1 852 C CG2 . ILE A 130 ? 1.0344 1.0355 0.8253 0.0364 -0.0785 0.1083 107 ILE A CG2 853 C CD1 . ILE A 130 ? 0.8538 0.8665 0.7090 0.0223 -0.0653 0.0947 107 ILE A CD1 854 N N . GLU A 131 ? 0.8907 0.9005 0.7028 0.0556 -0.0993 0.1349 108 GLU A N 855 C CA . GLU A 131 ? 0.9814 0.9917 0.7704 0.0662 -0.1137 0.1430 108 GLU A CA 856 C C . GLU A 131 ? 0.8653 0.8965 0.6792 0.0698 -0.1320 0.1402 108 GLU A C 857 O O . GLU A 131 ? 0.8537 0.8936 0.6535 0.0767 -0.1493 0.1414 108 GLU A O 858 C CB . GLU A 131 ? 1.1105 1.1010 0.8812 0.0753 -0.1040 0.1609 108 GLU A CB 859 C CG . GLU A 131 ? 1.2822 1.2535 1.0246 0.0721 -0.0862 0.1643 108 GLU A CG 860 C CD . GLU A 131 ? 1.4126 1.3625 1.1433 0.0781 -0.0723 0.1818 108 GLU A CD 861 O OE1 . GLU A 131 ? 1.4628 1.4107 1.2049 0.0859 -0.0774 0.1916 108 GLU A OE1 862 O OE2 . GLU A 131 ? 1.4716 1.4062 1.1824 0.0749 -0.0554 0.1857 108 GLU A OE2 863 N N . ASN A 132 ? 0.8409 0.8813 0.6921 0.0653 -0.1282 0.1360 109 ASN A N 864 C CA . ASN A 132 ? 0.8058 0.8684 0.6849 0.0673 -0.1431 0.1317 109 ASN A CA 865 C C . ASN A 132 ? 0.8104 0.8900 0.6950 0.0580 -0.1543 0.1159 109 ASN A C 866 O O . ASN A 132 ? 0.8026 0.9017 0.6975 0.0603 -0.1715 0.1119 109 ASN A O 867 C CB . ASN A 132 ? 0.7296 0.7953 0.6448 0.0657 -0.1338 0.1321 109 ASN A CB 868 C CG . ASN A 132 ? 0.7328 0.8213 0.6775 0.0700 -0.1472 0.1297 109 ASN A CG 869 O OD1 . ASN A 132 ? 0.7876 0.8783 0.7351 0.0825 -0.1540 0.1399 109 ASN A OD1 870 N ND2 . ASN A 132 ? 0.7649 0.8705 0.7324 0.0600 -0.1505 0.1165 109 ASN A ND2 871 N N . MET A 133 ? 0.7500 0.8218 0.6285 0.0474 -0.1445 0.1067 110 MET A N 872 C CA . MET A 133 ? 0.7317 0.8139 0.6122 0.0377 -0.1529 0.0915 110 MET A CA 873 C C . MET A 133 ? 0.9076 0.9903 0.7557 0.0409 -0.1670 0.0890 110 MET A C 874 O O . MET A 133 ? 0.9296 1.0274 0.7830 0.0361 -0.1818 0.0783 110 MET A O 875 C CB . MET A 133 ? 0.6207 0.6911 0.5003 0.0278 -0.1381 0.0836 110 MET A CB 876 C CG . MET A 133 ? 0.6412 0.7132 0.5520 0.0233 -0.1266 0.0832 110 MET A CG 877 S SD . MET A 133 ? 0.7343 0.7938 0.6428 0.0138 -0.1119 0.0743 110 MET A SD 878 C CE . MET A 133 ? 1.2300 1.2945 1.1303 0.0057 -0.1235 0.0596 110 MET A CE 879 N N . GLU A 134 ? 1.0129 1.0787 0.8269 0.0483 -0.1619 0.0986 111 GLU A N 880 C CA . GLU A 134 ? 1.1039 1.1676 0.8812 0.0528 -0.1745 0.0974 111 GLU A CA 881 C C . GLU A 134 ? 1.0083 1.0895 0.7902 0.0622 -0.1953 0.1026 111 GLU A C 882 O O . GLU A 134 ? 1.0398 1.1321 0.8079 0.0623 -0.2134 0.0949 111 GLU A O 883 C CB . GLU A 134 ? 1.2294 1.2696 0.9688 0.0590 -0.1612 0.1082 111 GLU A CB 884 C CG . GLU A 134 ? 1.3687 1.3943 1.1050 0.0509 -0.1407 0.1032 111 GLU A CG 885 C CD . GLU A 134 ? 1.4849 1.4895 1.1918 0.0565 -0.1244 0.1152 111 GLU A CD 886 O OE1 . GLU A 134 ? 1.5591 1.5575 1.2487 0.0665 -0.1273 0.1294 111 GLU A OE1 887 O OE2 . GLU A 134 ? 1.5106 1.5050 1.2123 0.0510 -0.1081 0.1109 111 GLU A OE2 888 N N . ALA A 135 ? 0.9551 1.0391 0.7574 0.0706 -0.1932 0.1150 112 ALA A N 889 C CA . ALA A 135 ? 0.9695 1.0700 0.7783 0.0824 -0.2121 0.1217 112 ALA A CA 890 C C . ALA A 135 ? 0.9446 1.0752 0.7957 0.0768 -0.2253 0.1102 112 ALA A C 891 O O . ALA A 135 ? 0.9266 1.0779 0.7819 0.0826 -0.2461 0.1084 112 ALA A O 892 C CB . ALA A 135 ? 0.9755 1.0637 0.7866 0.0951 -0.2036 0.1403 112 ALA A CB 893 N N . HIS A 136 ? 0.9220 1.0553 0.8042 0.0655 -0.2129 0.1024 113 HIS A N 894 C CA . HIS A 136 ? 0.8741 1.0340 0.7993 0.0598 -0.2205 0.0932 113 HIS A CA 895 C C . HIS A 136 ? 0.8431 1.0088 0.7801 0.0425 -0.2188 0.0758 113 HIS A C 896 O O . HIS A 136 ? 0.8693 1.0412 0.8380 0.0346 -0.2096 0.0709 113 HIS A O 897 C CB . HIS A 136 ? 0.8888 1.0491 0.8457 0.0638 -0.2081 0.1008 113 HIS A CB 898 C CG . HIS A 136 ? 1.0031 1.1680 0.9641 0.0810 -0.2155 0.1149 113 HIS A CG 899 N ND1 . HIS A 136 ? 1.0495 1.1905 0.9836 0.0923 -0.2081 0.1304 113 HIS A ND1 900 C CD2 . HIS A 136 ? 1.0313 1.2214 1.0210 0.0892 -0.2290 0.1160 113 HIS A CD2 901 C CE1 . HIS A 136 ? 1.0845 1.2333 1.0285 0.1074 -0.2170 0.1410 113 HIS A CE1 902 N NE2 . HIS A 136 ? 1.0626 1.2422 1.0410 0.1066 -0.2301 0.1325 113 HIS A NE2 903 N N . ASN A 137 ? 0.8214 0.9831 0.7313 0.0370 -0.2268 0.0667 114 ASN A N 904 C CA . ASN A 137 ? 0.9533 1.1211 0.8735 0.0210 -0.2288 0.0494 114 ASN A CA 905 C C . ASN A 137 ? 0.9878 1.1397 0.9178 0.0108 -0.2082 0.0455 114 ASN A C 906 O O . ASN A 137 ? 1.0103 1.1690 0.9612 -0.0016 -0.2071 0.0340 114 ASN A O 907 C CB . ASN A 137 ? 1.0410 1.2410 0.9987 0.0167 -0.2445 0.0414 114 ASN A CB 908 C CG . ASN A 137 ? 1.0952 1.3025 1.0555 0.0010 -0.2529 0.0231 114 ASN A CG 909 O OD1 . ASN A 137 ? 1.1983 1.3906 1.1249 -0.0026 -0.2557 0.0162 114 ASN A OD1 910 N ND2 . ASN A 137 ? 0.9665 1.1960 0.9672 -0.0087 -0.2560 0.0146 114 ASN A ND2 911 N N . GLY A 138 ? 0.8993 1.0302 0.8141 0.0162 -0.1921 0.0554 115 GLY A N 912 C CA . GLY A 138 ? 0.7332 0.8489 0.6530 0.0084 -0.1739 0.0523 115 GLY A CA 913 C C . GLY A 138 ? 0.7144 0.8335 0.6652 0.0088 -0.1625 0.0580 115 GLY A C 914 O O . GLY A 138 ? 0.6705 0.7787 0.6269 0.0030 -0.1487 0.0556 115 GLY A O 915 N N . THR A 139 ? 0.6888 0.8227 0.6591 0.0165 -0.1687 0.0652 116 THR A N 916 C CA . THR A 139 ? 0.6657 0.8019 0.6638 0.0180 -0.1578 0.0702 116 THR A CA 917 C C . THR A 139 ? 0.6927 0.8115 0.6779 0.0274 -0.1468 0.0831 116 THR A C 918 O O . THR A 139 ? 0.6720 0.7885 0.6429 0.0381 -0.1528 0.0928 116 THR A O 919 C CB . THR A 139 ? 0.5836 0.7450 0.6134 0.0218 -0.1681 0.0706 116 THR A CB 920 O OG1 . THR A 139 ? 0.6558 0.8350 0.6992 0.0117 -0.1785 0.0581 116 THR A OG1 921 C CG2 . THR A 139 ? 0.5512 0.7138 0.6086 0.0222 -0.1552 0.0734 116 THR A CG2 922 N N . PRO A 140 ? 0.6207 0.7266 0.6106 0.0232 -0.1307 0.0833 117 PRO A N 923 C CA . PRO A 140 ? 0.5793 0.6691 0.5611 0.0298 -0.1191 0.0941 117 PRO A CA 924 C C . PRO A 140 ? 0.6246 0.7202 0.6276 0.0381 -0.1192 0.1018 117 PRO A C 925 O O . PRO A 140 ? 0.6153 0.7295 0.6409 0.0390 -0.1277 0.0984 117 PRO A O 926 C CB . PRO A 140 ? 0.5397 0.6194 0.5261 0.0214 -0.1046 0.0888 117 PRO A CB 927 C CG . PRO A 140 ? 0.4969 0.5894 0.5036 0.0131 -0.1076 0.0784 117 PRO A CG 928 C CD . PRO A 140 ? 0.5407 0.6458 0.5427 0.0119 -0.1229 0.0735 117 PRO A CD 929 N N . LEU A 141 ? 0.6572 0.7368 0.6537 0.0441 -0.1093 0.1116 118 LEU A N 930 C CA . LEU A 141 ? 0.6371 0.7173 0.6524 0.0524 -0.1071 0.1188 118 LEU A CA 931 C C . LEU A 141 ? 0.5690 0.6573 0.6134 0.0461 -0.1003 0.1107 118 LEU A C 932 O O . LEU A 141 ? 0.6022 0.7022 0.6695 0.0513 -0.1032 0.1112 118 LEU A O 933 C CB . LEU A 141 ? 0.6224 0.6795 0.6233 0.0576 -0.0956 0.1299 118 LEU A CB 934 C CG . LEU A 141 ? 0.6519 0.6986 0.6243 0.0672 -0.1011 0.1418 118 LEU A CG 935 C CD1 . LEU A 141 ? 0.5516 0.5730 0.5101 0.0690 -0.0860 0.1519 118 LEU A CD1 936 C CD2 . LEU A 141 ? 0.5965 0.6550 0.5770 0.0800 -0.1154 0.1481 118 LEU A CD2 937 N N . THR A 142 ? 0.5585 0.6407 0.6011 0.0358 -0.0910 0.1035 119 THR A N 938 C CA . THR A 142 ? 0.4838 0.5714 0.5484 0.0294 -0.0841 0.0958 119 THR A CA 939 C C . THR A 142 ? 0.5076 0.6048 0.5741 0.0193 -0.0875 0.0854 119 THR A C 940 O O . THR A 142 ? 0.5043 0.6183 0.5843 0.0180 -0.0960 0.0812 119 THR A O 941 C CB . THR A 142 ? 0.5318 0.6031 0.5945 0.0263 -0.0699 0.0962 119 THR A CB 942 O OG1 . THR A 142 ? 0.5174 0.5793 0.5604 0.0209 -0.0664 0.0946 119 THR A OG1 943 C CG2 . THR A 142 ? 0.4362 0.4954 0.4989 0.0348 -0.0650 0.1058 119 THR A CG2 944 N N . ASN A 143 ? 0.4726 0.5592 0.5268 0.0124 -0.0807 0.0812 120 ASN A N 945 C CA . ASN A 143 ? 0.3874 0.4781 0.4418 0.0032 -0.0820 0.0720 120 ASN A CA 946 C C . ASN A 143 ? 0.4886 0.5653 0.5238 -0.0007 -0.0760 0.0696 120 ASN A C 947 O O . ASN A 143 ? 0.5348 0.6012 0.5592 0.0028 -0.0703 0.0747 120 ASN A O 948 C CB . ASN A 143 ? 0.4409 0.5377 0.5165 -0.0013 -0.0763 0.0672 120 ASN A CB 949 C CG . ASN A 143 ? 0.4520 0.5389 0.5312 0.0004 -0.0652 0.0693 120 ASN A CG 950 O OD1 . ASN A 143 ? 0.4858 0.5618 0.5542 -0.0027 -0.0591 0.0676 120 ASN A OD1 951 N ND2 . ASN A 143 ? 0.4567 0.5479 0.5518 0.0056 -0.0629 0.0722 120 ASN A ND2 952 N N . TYR A 144 ? 0.4321 0.5083 0.4642 -0.0078 -0.0766 0.0620 121 TYR A N 953 C CA . TYR A 144 ? 0.5698 0.6336 0.5849 -0.0100 -0.0715 0.0593 121 TYR A CA 954 C C . TYR A 144 ? 0.5183 0.5758 0.5390 -0.0110 -0.0613 0.0589 121 TYR A C 955 O O . TYR A 144 ? 0.5270 0.5764 0.5371 -0.0104 -0.0561 0.0585 121 TYR A O 956 C CB . TYR A 144 ? 0.5095 0.5718 0.5173 -0.0163 -0.0760 0.0513 121 TYR A CB 957 C CG . TYR A 144 ? 0.6030 0.6631 0.5912 -0.0149 -0.0833 0.0501 121 TYR A CG 958 C CD1 . TYR A 144 ? 0.5586 0.6241 0.5412 -0.0088 -0.0897 0.0560 121 TYR A CD1 959 C CD2 . TYR A 144 ? 0.5086 0.5596 0.4820 -0.0189 -0.0837 0.0429 121 TYR A CD2 960 C CE1 . TYR A 144 ? 0.5719 0.6348 0.5329 -0.0072 -0.0968 0.0547 121 TYR A CE1 961 C CE2 . TYR A 144 ? 0.5186 0.5665 0.4718 -0.0177 -0.0901 0.0405 121 TYR A CE2 962 C CZ . TYR A 144 ? 0.6434 0.6977 0.5895 -0.0120 -0.0968 0.0463 121 TYR A CZ 963 O OH . TYR A 144 ? 0.6592 0.7097 0.5814 -0.0105 -0.1035 0.0436 121 TYR A OH 964 N N . TYR A 145 ? 0.4534 0.5157 0.4910 -0.0123 -0.0585 0.0584 122 TYR A N 965 C CA . TYR A 145 ? 0.4376 0.4948 0.4797 -0.0127 -0.0503 0.0577 122 TYR A CA 966 C C . TYR A 145 ? 0.4876 0.5402 0.5274 -0.0084 -0.0458 0.0628 122 TYR A C 967 O O . TYR A 145 ? 0.5546 0.6018 0.5900 -0.0091 -0.0405 0.0617 122 TYR A O 968 C CB . TYR A 145 ? 0.3780 0.4410 0.4366 -0.0143 -0.0479 0.0561 122 TYR A CB 969 C CG . TYR A 145 ? 0.4380 0.4956 0.4989 -0.0152 -0.0406 0.0540 122 TYR A CG 970 C CD1 . TYR A 145 ? 0.4002 0.4536 0.4556 -0.0189 -0.0384 0.0496 122 TYR A CD1 971 C CD2 . TYR A 145 ? 0.3993 0.4552 0.4668 -0.0121 -0.0362 0.0561 122 TYR A CD2 972 C CE1 . TYR A 145 ? 0.3083 0.3578 0.3638 -0.0189 -0.0334 0.0474 122 TYR A CE1 973 C CE2 . TYR A 145 ? 0.4313 0.4832 0.5003 -0.0135 -0.0307 0.0527 122 TYR A CE2 974 C CZ . TYR A 145 ? 0.4397 0.4894 0.5022 -0.0166 -0.0300 0.0483 122 TYR A CZ 975 O OH . TYR A 145 ? 0.4987 0.5452 0.5606 -0.0172 -0.0262 0.0447 122 TYR A OH 976 N N . GLN A 146 ? 0.5264 0.5810 0.5698 -0.0040 -0.0479 0.0687 123 GLN A N 977 C CA . GLN A 146 ? 0.5804 0.6277 0.6205 -0.0004 -0.0427 0.0748 123 GLN A CA 978 C C . GLN A 146 ? 0.5127 0.5546 0.5345 0.0003 -0.0421 0.0772 123 GLN A C 979 O O . GLN A 146 ? 0.4862 0.5217 0.5048 -0.0001 -0.0346 0.0790 123 GLN A O 980 C CB . GLN A 146 ? 0.4654 0.5136 0.5124 0.0056 -0.0451 0.0816 123 GLN A CB 981 C CG . GLN A 146 ? 0.4337 0.4866 0.4998 0.0061 -0.0434 0.0791 123 GLN A CG 982 C CD . GLN A 146 ? 0.5161 0.5659 0.5897 0.0135 -0.0427 0.0862 123 GLN A CD 983 O OE1 . GLN A 146 ? 0.5962 0.6359 0.6602 0.0174 -0.0408 0.0935 123 GLN A OE1 984 N NE2 . GLN A 146 ? 0.5290 0.5864 0.6195 0.0161 -0.0435 0.0844 123 GLN A NE2 985 N N . LEU A 147 ? 0.4656 0.5103 0.4759 0.0009 -0.0496 0.0763 124 LEU A N 986 C CA . LEU A 147 ? 0.5670 0.6061 0.5572 0.0018 -0.0488 0.0773 124 LEU A CA 987 C C . LEU A 147 ? 0.6225 0.6583 0.6110 -0.0015 -0.0417 0.0718 124 LEU A C 988 O O . LEU A 147 ? 0.5566 0.5875 0.5353 -0.0004 -0.0352 0.0737 124 LEU A O 989 C CB . LEU A 147 ? 0.6824 0.7253 0.6609 0.0019 -0.0591 0.0743 124 LEU A CB 990 C CG . LEU A 147 ? 0.7513 0.7879 0.7050 0.0051 -0.0600 0.0771 124 LEU A CG 991 C CD1 . LEU A 147 ? 0.7340 0.7681 0.6813 0.0116 -0.0610 0.0877 124 LEU A CD1 992 C CD2 . LEU A 147 ? 0.7540 0.7934 0.6960 0.0030 -0.0699 0.0702 124 LEU A CD2 993 N N . SER A 148 ? 0.5301 0.5689 0.5283 -0.0051 -0.0425 0.0654 125 SER A N 994 C CA . SER A 148 ? 0.5692 0.6057 0.5671 -0.0066 -0.0373 0.0605 125 SER A CA 995 C C . SER A 148 ? 0.4894 0.5267 0.4983 -0.0068 -0.0298 0.0622 125 SER A C 996 O O . SER A 148 ? 0.5833 0.6202 0.5908 -0.0065 -0.0242 0.0607 125 SER A O 997 C CB . SER A 148 ? 0.4515 0.4888 0.4544 -0.0097 -0.0405 0.0545 125 SER A CB 998 O OG . SER A 148 ? 0.4795 0.5158 0.4745 -0.0114 -0.0469 0.0519 125 SER A OG 999 N N . LEU A 149 ? 0.4272 0.4658 0.4482 -0.0074 -0.0296 0.0643 126 LEU A N 1000 C CA . LEU A 149 ? 0.4226 0.4603 0.4542 -0.0085 -0.0228 0.0653 126 LEU A CA 1001 C C . LEU A 149 ? 0.3964 0.4296 0.4218 -0.0075 -0.0166 0.0709 126 LEU A C 1002 O O . LEU A 149 ? 0.4294 0.4633 0.4609 -0.0099 -0.0097 0.0695 126 LEU A O 1003 C CB . LEU A 149 ? 0.4022 0.4393 0.4454 -0.0084 -0.0232 0.0668 126 LEU A CB 1004 C CG . LEU A 149 ? 0.4789 0.5195 0.5307 -0.0105 -0.0250 0.0607 126 LEU A CG 1005 C CD1 . LEU A 149 ? 0.3305 0.3705 0.3929 -0.0091 -0.0244 0.0624 126 LEU A CD1 1006 C CD2 . LEU A 149 ? 0.3984 0.4400 0.4541 -0.0133 -0.0216 0.0550 126 LEU A CD2 1007 N N . ASP A 150 ? 0.4042 0.4335 0.4174 -0.0041 -0.0191 0.0772 127 ASP A N 1008 C CA . ASP A 150 ? 0.5495 0.5721 0.5522 -0.0026 -0.0124 0.0842 127 ASP A CA 1009 C C . ASP A 150 ? 0.5302 0.5544 0.5253 -0.0038 -0.0067 0.0809 127 ASP A C 1010 O O . ASP A 150 ? 0.5837 0.6068 0.5832 -0.0061 0.0032 0.0824 127 ASP A O 1011 C CB . ASP A 150 ? 0.5217 0.5400 0.5086 0.0026 -0.0184 0.0913 127 ASP A CB 1012 C CG . ASP A 150 ? 0.5837 0.6013 0.5801 0.0056 -0.0232 0.0957 127 ASP A CG 1013 O OD1 . ASP A 150 ? 0.5294 0.5447 0.5413 0.0038 -0.0182 0.0955 127 ASP A OD1 1014 O OD2 . ASP A 150 ? 0.5802 0.6003 0.5692 0.0100 -0.0324 0.0986 127 ASP A OD2 1015 N N . VAL A 151 ? 0.4953 0.5221 0.4802 -0.0024 -0.0122 0.0760 128 VAL A N 1016 C CA . VAL A 151 ? 0.4409 0.4689 0.4183 -0.0019 -0.0068 0.0720 128 VAL A CA 1017 C C . VAL A 151 ? 0.5410 0.5764 0.5367 -0.0044 -0.0016 0.0666 128 VAL A C 1018 O O . VAL A 151 ? 0.5501 0.5886 0.5483 -0.0047 0.0072 0.0660 128 VAL A O 1019 C CB . VAL A 151 ? 0.4913 0.5182 0.4552 0.0000 -0.0142 0.0664 128 VAL A CB 1020 C CG1 . VAL A 151 ? 0.5395 0.5666 0.4969 0.0019 -0.0079 0.0615 128 VAL A CG1 1021 C CG2 . VAL A 151 ? 0.4908 0.5127 0.4363 0.0022 -0.0206 0.0705 128 VAL A CG2 1022 N N . LEU A 152 ? 0.4984 0.5375 0.5068 -0.0061 -0.0071 0.0625 129 LEU A N 1023 C CA . LEU A 152 ? 0.4686 0.5155 0.4929 -0.0078 -0.0049 0.0569 129 LEU A CA 1024 C C . LEU A 152 ? 0.5222 0.5723 0.5599 -0.0116 0.0036 0.0587 129 LEU A C 1025 O O . LEU A 152 ? 0.5201 0.5784 0.5671 -0.0125 0.0091 0.0552 129 LEU A O 1026 C CB . LEU A 152 ? 0.4796 0.5276 0.5111 -0.0090 -0.0120 0.0533 129 LEU A CB 1027 C CG . LEU A 152 ? 0.4925 0.5481 0.5377 -0.0102 -0.0121 0.0473 129 LEU A CG 1028 C CD1 . LEU A 152 ? 0.4042 0.4654 0.4481 -0.0064 -0.0118 0.0431 129 LEU A CD1 1029 C CD2 . LEU A 152 ? 0.4761 0.5300 0.5229 -0.0110 -0.0183 0.0448 129 LEU A CD2 1030 N N . ALA A 153 ? 0.5352 0.5786 0.5750 -0.0138 0.0050 0.0641 130 ALA A N 1031 C CA . ALA A 153 ? 0.5542 0.5966 0.6064 -0.0186 0.0138 0.0660 130 ALA A CA 1032 C C . ALA A 153 ? 0.5347 0.5757 0.5811 -0.0193 0.0244 0.0706 130 ALA A C 1033 O O . ALA A 153 ? 0.5416 0.5892 0.6023 -0.0240 0.0327 0.0680 130 ALA A O 1034 C CB . ALA A 153 ? 0.4842 0.5161 0.5375 -0.0193 0.0132 0.0714 130 ALA A CB 1035 N N . LEU A 154 ? 0.4642 0.4973 0.4897 -0.0149 0.0244 0.0771 131 LEU A N 1036 C CA . LEU A 154 ? 0.5205 0.5504 0.5351 -0.0146 0.0353 0.0820 131 LEU A CA 1037 C C . LEU A 154 ? 0.5806 0.6229 0.6010 -0.0143 0.0398 0.0747 131 LEU A C 1038 O O . LEU A 154 ? 0.5821 0.6280 0.6078 -0.0170 0.0522 0.0757 131 LEU A O 1039 C CB . LEU A 154 ? 0.4145 0.4338 0.4016 -0.0089 0.0317 0.0890 131 LEU A CB 1040 C CG . LEU A 154 ? 0.5088 0.5159 0.4884 -0.0071 0.0285 0.0984 131 LEU A CG 1041 C CD1 . LEU A 154 ? 0.4279 0.4288 0.3809 -0.0006 0.0211 0.1033 131 LEU A CD1 1042 C CD2 . LEU A 154 ? 0.5933 0.5907 0.5761 -0.0108 0.0418 0.1065 131 LEU A CD2 1043 N N . CYS A 155 ? 0.5602 0.6087 0.5803 -0.0106 0.0305 0.0676 132 CYS A N 1044 C CA . CYS A 155 ? 0.4829 0.5425 0.5089 -0.0080 0.0332 0.0604 132 CYS A CA 1045 C C . CYS A 155 ? 0.4839 0.5584 0.5377 -0.0121 0.0367 0.0549 132 CYS A C 1046 O O . CYS A 155 ? 0.5210 0.6062 0.5851 -0.0124 0.0459 0.0523 132 CYS A O 1047 C CB . CYS A 155 ? 0.4751 0.5335 0.4923 -0.0028 0.0221 0.0551 132 CYS A CB 1048 S SG . CYS A 155 ? 0.4738 0.5441 0.5003 0.0026 0.0234 0.0463 132 CYS A SG 1049 N N . LEU A 156 ? 0.4563 0.5327 0.5225 -0.0153 0.0293 0.0523 133 LEU A N 1050 C CA . LEU A 156 ? 0.4658 0.5567 0.5572 -0.0196 0.0297 0.0456 133 LEU A CA 1051 C C . LEU A 156 ? 0.5413 0.6357 0.6482 -0.0276 0.0420 0.0475 133 LEU A C 1052 O O . LEU A 156 ? 0.5159 0.6266 0.6455 -0.0315 0.0450 0.0410 133 LEU A O 1053 C CB . LEU A 156 ? 0.4315 0.5207 0.5280 -0.0213 0.0192 0.0423 133 LEU A CB 1054 C CG . LEU A 156 ? 0.5004 0.5898 0.5884 -0.0150 0.0079 0.0385 133 LEU A CG 1055 C CD1 . LEU A 156 ? 0.4310 0.5158 0.5205 -0.0173 0.0004 0.0369 133 LEU A CD1 1056 C CD2 . LEU A 156 ? 0.3140 0.4189 0.4132 -0.0109 0.0060 0.0317 133 LEU A CD2 1057 N N . PHE A 157 ? 0.4839 0.5630 0.5788 -0.0303 0.0490 0.0564 134 PHE A N 1058 C CA . PHE A 157 ? 0.6494 0.7266 0.7570 -0.0389 0.0619 0.0595 134 PHE A CA 1059 C C . PHE A 157 ? 0.6444 0.7154 0.7385 -0.0384 0.0759 0.0674 134 PHE A C 1060 O O . PHE A 157 ? 0.7009 0.7614 0.7952 -0.0444 0.0875 0.0743 134 PHE A O 1061 C CB . PHE A 157 ? 0.5378 0.5995 0.6453 -0.0433 0.0602 0.0636 134 PHE A CB 1062 C CG . PHE A 157 ? 0.4600 0.5281 0.5822 -0.0455 0.0496 0.0547 134 PHE A CG 1063 C CD1 . PHE A 157 ? 0.4602 0.5263 0.5718 -0.0390 0.0368 0.0530 134 PHE A CD1 1064 C CD2 . PHE A 157 ? 0.5759 0.6523 0.7223 -0.0545 0.0529 0.0475 134 PHE A CD2 1065 C CE1 . PHE A 157 ? 0.5318 0.6027 0.6536 -0.0407 0.0283 0.0451 134 PHE A CE1 1066 C CE2 . PHE A 157 ? 0.6204 0.7020 0.7770 -0.0561 0.0427 0.0386 134 PHE A CE2 1067 C CZ . PHE A 157 ? 0.4110 0.4894 0.5540 -0.0488 0.0308 0.0378 134 PHE A CZ 1068 N N . ASN A 158 ? 0.5928 0.6686 0.6737 -0.0310 0.0755 0.0662 135 ASN A N 1069 C CA . ASN A 158 ? 0.6785 0.7502 0.7447 -0.0295 0.0893 0.0719 135 ASN A CA 1070 C C . ASN A 158 ? 0.7162 0.7652 0.7567 -0.0295 0.0942 0.0844 135 ASN A C 1071 O O . ASN A 158 ? 0.7217 0.7646 0.7563 -0.0329 0.1097 0.0912 135 ASN A O 1072 C CB . ASN A 158 ? 0.7795 0.8668 0.8711 -0.0366 0.1046 0.0685 135 ASN A CB 1073 C CG . ASN A 158 ? 0.9064 1.0186 1.0223 -0.0340 0.0995 0.0565 135 ASN A CG 1074 O OD1 . ASN A 158 ? 0.9843 1.1113 1.1289 -0.0401 0.0971 0.0497 135 ASN A OD1 1075 N ND2 . ASN A 158 ? 0.9287 1.0449 1.0323 -0.0244 0.0975 0.0535 135 ASN A ND2 1076 N N . GLY A 159 ? 0.6964 0.7336 0.7220 -0.0254 0.0812 0.0878 136 GLY A N 1077 C CA . GLY A 159 ? 0.6067 0.6238 0.6067 -0.0228 0.0825 0.0998 136 GLY A CA 1078 C C . GLY A 159 ? 0.6995 0.7119 0.6693 -0.0154 0.0824 0.1024 136 GLY A C 1079 O O . GLY A 159 ? 0.7905 0.8132 0.7594 -0.0118 0.0787 0.0940 136 GLY A O 1080 N N . ASN A 160 ? 0.7370 0.7324 0.6806 -0.0127 0.0863 0.1137 137 ASN A N 1081 C CA . ASN A 160 ? 0.8052 0.7945 0.7160 -0.0058 0.0861 0.1161 137 ASN A CA 1082 C C . ASN A 160 ? 0.8287 0.8151 0.7236 0.0007 0.0667 0.1145 137 ASN A C 1083 O O . ASN A 160 ? 0.8389 0.8166 0.7283 0.0027 0.0583 0.1215 137 ASN A O 1084 C CB . ASN A 160 ? 1.0095 0.9817 0.8958 -0.0054 0.0998 0.1294 137 ASN A CB 1085 C CG . ASN A 160 ? 1.2413 1.2094 1.0951 0.0001 0.1051 0.1297 137 ASN A CG 1086 O OD1 . ASN A 160 ? 1.2458 1.2149 1.0821 0.0062 0.0920 0.1245 137 ASN A OD1 1087 N ND2 . ASN A 160 ? 1.3514 1.3146 1.1970 -0.0026 0.1253 0.1353 137 ASN A ND2 1088 N N . TYR A 161 ? 0.7746 0.7684 0.6636 0.0039 0.0602 0.1048 138 TYR A N 1089 C CA . TYR A 161 ? 0.7882 0.7804 0.6633 0.0084 0.0428 0.1015 138 TYR A CA 1090 C C . TYR A 161 ? 0.8388 0.8300 0.6913 0.0125 0.0426 0.0947 138 TYR A C 1091 O O . TYR A 161 ? 0.8239 0.8205 0.6813 0.0122 0.0536 0.0890 138 TYR A O 1092 C CB . TYR A 161 ? 0.7306 0.7328 0.6316 0.0061 0.0314 0.0939 138 TYR A CB 1093 C CG . TYR A 161 ? 0.7998 0.8134 0.7191 0.0045 0.0348 0.0835 138 TYR A CG 1094 C CD1 . TYR A 161 ? 0.8402 0.8624 0.7844 0.0001 0.0446 0.0823 138 TYR A CD1 1095 C CD2 . TYR A 161 ? 0.6879 0.7034 0.6000 0.0075 0.0278 0.0746 138 TYR A CD2 1096 C CE1 . TYR A 161 ? 0.8651 0.8996 0.8266 0.0001 0.0461 0.0731 138 TYR A CE1 1097 C CE2 . TYR A 161 ? 0.6561 0.6806 0.5840 0.0079 0.0305 0.0662 138 TYR A CE2 1098 C CZ . TYR A 161 ? 0.7864 0.8216 0.7391 0.0049 0.0391 0.0657 138 TYR A CZ 1099 O OH . TYR A 161 ? 0.7197 0.7657 0.6887 0.0067 0.0404 0.0576 138 TYR A OH 1100 N N . SER A 162 ? 0.8732 0.8582 0.7018 0.0163 0.0301 0.0944 139 SER A N 1101 C CA . SER A 162 ? 0.8511 0.8327 0.6556 0.0197 0.0287 0.0865 139 SER A CA 1102 C C . SER A 162 ? 0.8360 0.8241 0.6543 0.0187 0.0189 0.0741 139 SER A C 1103 O O . SER A 162 ? 0.8936 0.8842 0.7205 0.0170 0.0048 0.0725 139 SER A O 1104 C CB . SER A 162 ? 0.9287 0.9004 0.6990 0.0239 0.0190 0.0910 139 SER A CB 1105 O OG . SER A 162 ? 1.0034 0.9709 0.7497 0.0263 0.0163 0.0813 139 SER A OG 1106 N N . THR A 163 ? 0.6803 0.6704 0.5010 0.0200 0.0272 0.0658 140 THR A N 1107 C CA . THR A 163 ? 0.6405 0.6326 0.4706 0.0200 0.0193 0.0548 140 THR A CA 1108 C C . THR A 163 ? 0.7544 0.7373 0.5594 0.0208 0.0069 0.0491 140 THR A C 1109 O O . THR A 163 ? 0.7961 0.7790 0.6091 0.0185 -0.0042 0.0428 140 THR A O 1110 C CB . THR A 163 ? 0.7834 0.7785 0.6199 0.0234 0.0313 0.0475 140 THR A CB 1111 O OG1 . THR A 163 ? 1.0710 1.0580 0.8793 0.0274 0.0406 0.0459 140 THR A OG1 1112 C CG2 . THR A 163 ? 0.6975 0.7054 0.5627 0.0217 0.0423 0.0515 140 THR A CG2 1113 N N . ALA A 164 ? 0.7822 0.7569 0.5563 0.0236 0.0091 0.0512 141 ALA A N 1114 C CA . ALA A 164 ? 0.7659 0.7327 0.5140 0.0239 -0.0039 0.0454 141 ALA A CA 1115 C C . ALA A 164 ? 0.8038 0.7761 0.5616 0.0205 -0.0205 0.0491 141 ALA A C 1116 O O . ALA A 164 ? 0.7475 0.7192 0.5034 0.0176 -0.0337 0.0412 141 ALA A O 1117 C CB . ALA A 164 ? 0.7054 0.6629 0.4163 0.0281 0.0016 0.0484 141 ALA A CB 1118 N N . GLU A 165 ? 0.8495 0.8270 0.6192 0.0206 -0.0190 0.0609 142 GLU A N 1119 C CA . GLU A 165 ? 0.9541 0.9383 0.7370 0.0188 -0.0329 0.0654 142 GLU A CA 1120 C C . GLU A 165 ? 0.8203 0.8118 0.6321 0.0138 -0.0385 0.0583 142 GLU A C 1121 O O . GLU A 165 ? 0.7951 0.7913 0.6132 0.0111 -0.0518 0.0552 142 GLU A O 1122 C CB . GLU A 165 ? 1.0924 1.0780 0.8845 0.0206 -0.0270 0.0790 142 GLU A CB 1123 C CG . GLU A 165 ? 1.1956 1.1833 0.9837 0.0233 -0.0404 0.0866 142 GLU A CG 1124 C CD . GLU A 165 ? 1.2152 1.1947 0.9661 0.0290 -0.0439 0.0916 142 GLU A CD 1125 O OE1 . GLU A 165 ? 1.2618 1.2321 0.9975 0.0324 -0.0319 0.1017 142 GLU A OE1 1126 O OE2 . GLU A 165 ? 1.1465 1.1282 0.8825 0.0296 -0.0586 0.0853 142 GLU A OE2 1127 N N . VAL A 166 ? 0.7068 0.6997 0.5361 0.0128 -0.0279 0.0560 143 VAL A N 1128 C CA . VAL A 166 ? 0.6915 0.6891 0.5446 0.0090 -0.0315 0.0501 143 VAL A CA 1129 C C . VAL A 166 ? 0.6634 0.6547 0.5067 0.0070 -0.0386 0.0391 143 VAL A C 1130 O O . VAL A 166 ? 0.6456 0.6394 0.4996 0.0025 -0.0482 0.0356 143 VAL A O 1131 C CB . VAL A 166 ? 0.6649 0.6657 0.5358 0.0098 -0.0195 0.0499 143 VAL A CB 1132 C CG1 . VAL A 166 ? 0.6737 0.6764 0.5626 0.0073 -0.0236 0.0437 143 VAL A CG1 1133 C CG2 . VAL A 166 ? 0.6667 0.6732 0.5516 0.0094 -0.0131 0.0594 143 VAL A CG2 1134 N N . VAL A 167 ? 0.7316 0.7139 0.5547 0.0100 -0.0328 0.0332 144 VAL A N 1135 C CA . VAL A 167 ? 0.7990 0.7715 0.6091 0.0082 -0.0384 0.0218 144 VAL A CA 1136 C C . VAL A 167 ? 0.8121 0.7854 0.6116 0.0039 -0.0534 0.0192 144 VAL A C 1137 O O . VAL A 167 ? 0.7698 0.7396 0.5726 -0.0016 -0.0615 0.0110 144 VAL A O 1138 C CB . VAL A 167 ? 0.7680 0.7298 0.5543 0.0135 -0.0286 0.0160 144 VAL A CB 1139 C CG1 . VAL A 167 ? 0.7352 0.6836 0.5056 0.0114 -0.0345 0.0032 144 VAL A CG1 1140 C CG2 . VAL A 167 ? 0.8043 0.7688 0.6055 0.0181 -0.0144 0.0174 144 VAL A CG2 1141 N N . ASN A 168 ? 0.7730 0.7510 0.5605 0.0063 -0.0571 0.0266 145 ASN A N 1142 C CA . ASN A 168 ? 0.8526 0.8343 0.6296 0.0038 -0.0727 0.0247 145 ASN A CA 1143 C C . ASN A 168 ? 0.8723 0.8665 0.6774 -0.0015 -0.0831 0.0261 145 ASN A C 1144 O O . ASN A 168 ? 0.8977 0.8952 0.7039 -0.0069 -0.0954 0.0185 145 ASN A O 1145 C CB . ASN A 168 ? 0.9485 0.9311 0.7036 0.0099 -0.0738 0.0340 145 ASN A CB 1146 C CG . ASN A 168 ? 1.2142 1.1961 0.9439 0.0095 -0.0889 0.0284 145 ASN A CG 1147 O OD1 . ASN A 168 ? 1.3885 1.3611 1.0852 0.0137 -0.0866 0.0271 145 ASN A OD1 1148 N ND2 . ASN A 168 ? 1.2205 1.2133 0.9656 0.0044 -0.1043 0.0244 145 ASN A ND2 1149 N N . HIS A 169 ? 0.6820 0.6834 0.5105 -0.0003 -0.0775 0.0349 146 HIS A N 1150 C CA . HIS A 169 ? 0.6708 0.6848 0.5247 -0.0038 -0.0858 0.0375 146 HIS A CA 1151 C C . HIS A 169 ? 0.6524 0.6673 0.5303 -0.0095 -0.0825 0.0331 146 HIS A C 1152 O O . HIS A 169 ? 0.6605 0.6845 0.5564 -0.0143 -0.0897 0.0316 146 HIS A O 1153 C CB . HIS A 169 ? 0.7192 0.7398 0.5815 0.0016 -0.0834 0.0503 146 HIS A CB 1154 C CG . HIS A 169 ? 0.7556 0.7756 0.5949 0.0076 -0.0891 0.0566 146 HIS A CG 1155 N ND1 . HIS A 169 ? 0.7429 0.7716 0.5780 0.0081 -0.1049 0.0556 146 HIS A ND1 1156 C CD2 . HIS A 169 ? 0.6486 0.6601 0.4671 0.0136 -0.0809 0.0645 146 HIS A CD2 1157 C CE1 . HIS A 169 ? 0.7626 0.7875 0.5730 0.0153 -0.1073 0.0630 146 HIS A CE1 1158 N NE2 . HIS A 169 ? 0.8139 0.8270 0.6129 0.0184 -0.0920 0.0689 146 HIS A NE2 1159 N N . PHE A 170 ? 0.6521 0.6584 0.5303 -0.0085 -0.0715 0.0313 147 PHE A N 1160 C CA . PHE A 170 ? 0.6059 0.6118 0.5041 -0.0121 -0.0678 0.0292 147 PHE A CA 1161 C C . PHE A 170 ? 0.5688 0.5646 0.4630 -0.0175 -0.0702 0.0191 147 PHE A C 1162 O O . PHE A 170 ? 0.5809 0.5717 0.4855 -0.0191 -0.0655 0.0177 147 PHE A O 1163 C CB . PHE A 170 ? 0.6336 0.6377 0.5380 -0.0076 -0.0560 0.0332 147 PHE A CB 1164 C CG . PHE A 170 ? 0.6689 0.6826 0.5881 -0.0057 -0.0532 0.0422 147 PHE A CG 1165 C CD1 . PHE A 170 ? 0.6661 0.6815 0.5764 -0.0018 -0.0514 0.0491 147 PHE A CD1 1166 C CD2 . PHE A 170 ? 0.5809 0.5995 0.5207 -0.0078 -0.0516 0.0437 147 PHE A CD2 1167 C CE1 . PHE A 170 ? 0.6045 0.6254 0.5281 -0.0004 -0.0480 0.0571 147 PHE A CE1 1168 C CE2 . PHE A 170 ? 0.6099 0.6352 0.5626 -0.0064 -0.0487 0.0506 147 PHE A CE2 1169 C CZ . PHE A 170 ? 0.5457 0.5716 0.4911 -0.0028 -0.0468 0.0573 147 PHE A CZ 1170 N N . THR A 171 ? 0.5810 0.5725 0.4590 -0.0204 -0.0777 0.0121 148 THR A N 1171 C CA . THR A 171 ? 0.6739 0.6538 0.5479 -0.0271 -0.0804 0.0017 148 THR A CA 1172 C C . THR A 171 ? 0.6625 0.6476 0.5598 -0.0349 -0.0829 0.0015 148 THR A C 1173 O O . THR A 171 ? 0.6856 0.6865 0.5977 -0.0379 -0.0896 0.0046 148 THR A O 1174 C CB . THR A 171 ? 0.7636 0.7418 0.6193 -0.0308 -0.0909 -0.0066 148 THR A CB 1175 O OG1 . THR A 171 ? 1.0199 0.9991 0.8549 -0.0231 -0.0903 -0.0031 148 THR A OG1 1176 C CG2 . THR A 171 ? 0.7152 0.6740 0.5582 -0.0355 -0.0896 -0.0186 148 THR A CG2 1177 N N . PRO A 172 ? 0.7502 0.7216 0.6502 -0.0375 -0.0767 -0.0018 149 PRO A N 1178 C CA . PRO A 172 ? 0.8076 0.7803 0.7267 -0.0446 -0.0758 -0.0011 149 PRO A CA 1179 C C . PRO A 172 ? 0.7082 0.6896 0.6375 -0.0554 -0.0850 -0.0066 149 PRO A C 1180 O O . PRO A 172 ? 0.7554 0.7444 0.7042 -0.0613 -0.0841 -0.0046 149 PRO A O 1181 C CB . PRO A 172 ? 0.8435 0.7937 0.7538 -0.0446 -0.0685 -0.0051 149 PRO A CB 1182 C CG . PRO A 172 ? 0.8837 0.8273 0.7788 -0.0339 -0.0633 -0.0042 149 PRO A CG 1183 C CD . PRO A 172 ? 0.8071 0.7597 0.6910 -0.0323 -0.0691 -0.0057 149 PRO A CD 1184 N N . GLU A 173 ? 0.7126 0.6938 0.6289 -0.0582 -0.0936 -0.0141 150 GLU A N 1185 C CA . GLU A 173 ? 0.8408 0.8329 0.7684 -0.0691 -0.1039 -0.0209 150 GLU A CA 1186 C C . GLU A 173 ? 0.7297 0.7478 0.6693 -0.0661 -0.1135 -0.0157 150 GLU A C 1187 O O . GLU A 173 ? 0.7763 0.8097 0.7303 -0.0737 -0.1234 -0.0204 150 GLU A O 1188 C CB . GLU A 173 ? 1.0052 0.9836 0.9130 -0.0748 -0.1099 -0.0337 150 GLU A CB 1189 C CG . GLU A 173 ? 1.1638 1.1138 1.0605 -0.0778 -0.1005 -0.0395 150 GLU A CG 1190 C CD . GLU A 173 ? 1.2467 1.1917 1.1632 -0.0874 -0.0948 -0.0390 150 GLU A CD 1191 O OE1 . GLU A 173 ? 1.2754 1.2373 1.2128 -0.0972 -0.1006 -0.0407 150 GLU A OE1 1192 O OE2 . GLU A 173 ? 1.2149 1.1393 1.1259 -0.0847 -0.0841 -0.0366 150 GLU A OE2 1193 N N . ASN A 174 ? 0.5982 0.6212 0.5329 -0.0550 -0.1105 -0.0060 151 ASN A N 1194 C CA . ASN A 174 ? 0.5996 0.6436 0.5441 -0.0500 -0.1182 0.0009 151 ASN A CA 1195 C C . ASN A 174 ? 0.6412 0.7020 0.6171 -0.0546 -0.1188 0.0035 151 ASN A C 1196 O O . ASN A 174 ? 0.6508 0.7066 0.6387 -0.0567 -0.1087 0.0059 151 ASN A O 1197 C CB . ASN A 174 ? 0.5812 0.6229 0.5161 -0.0383 -0.1115 0.0115 151 ASN A CB 1198 C CG . ASN A 174 ? 0.6278 0.6858 0.5666 -0.0317 -0.1195 0.0192 151 ASN A CG 1199 O OD1 . ASN A 174 ? 0.6551 0.7268 0.6169 -0.0309 -0.1202 0.0244 151 ASN A OD1 1200 N ND2 . ASN A 174 ? 0.5553 0.6106 0.4699 -0.0262 -0.1251 0.0202 151 ASN A ND2 1201 N N . LYS A 175 ? 0.5811 0.6627 0.5698 -0.0553 -0.1308 0.0029 152 LYS A N 1202 C CA . LYS A 175 ? 0.6459 0.7467 0.6668 -0.0600 -0.1319 0.0037 152 LYS A CA 1203 C C . LYS A 175 ? 0.5768 0.6804 0.6113 -0.0529 -0.1217 0.0140 152 LYS A C 1204 O O . LYS A 175 ? 0.6427 0.7546 0.7006 -0.0575 -0.1164 0.0141 152 LYS A O 1205 C CB . LYS A 175 ? 0.8070 0.9321 0.8392 -0.0594 -0.1482 0.0015 152 LYS A CB 1206 C CG . LYS A 175 ? 0.9074 1.0378 0.9264 -0.0455 -0.1547 0.0108 152 LYS A CG 1207 C CD . LYS A 175 ? 1.0043 1.1600 1.0353 -0.0433 -0.1723 0.0093 152 LYS A CD 1208 C CE . LYS A 175 ? 1.0378 1.1954 1.0530 -0.0282 -0.1781 0.0204 152 LYS A CE 1209 N NZ . LYS A 175 ? 1.1311 1.3143 1.1577 -0.0238 -0.1967 0.0200 152 LYS A NZ 1210 N N . ASN A 176 ? 0.5468 0.6428 0.5662 -0.0424 -0.1181 0.0221 153 ASN A N 1211 C CA . ASN A 176 ? 0.5496 0.6477 0.5807 -0.0357 -0.1095 0.0310 153 ASN A CA 1212 C C . ASN A 176 ? 0.5264 0.6125 0.5613 -0.0392 -0.0964 0.0307 153 ASN A C 1213 O O . ASN A 176 ? 0.5394 0.6268 0.5843 -0.0352 -0.0891 0.0362 153 ASN A O 1214 C CB . ASN A 176 ? 0.5377 0.6300 0.5520 -0.0249 -0.1088 0.0394 153 ASN A CB 1215 C CG . ASN A 176 ? 0.6593 0.7643 0.6715 -0.0186 -0.1213 0.0430 153 ASN A CG 1216 O OD1 . ASN A 176 ? 0.5980 0.7171 0.6292 -0.0140 -0.1244 0.0479 153 ASN A OD1 1217 N ND2 . ASN A 176 ? 0.5980 0.6978 0.5859 -0.0174 -0.1287 0.0406 153 ASN A ND2 1218 N N . TYR A 177 ? 0.4672 0.5402 0.4925 -0.0463 -0.0936 0.0241 154 TYR A N 1219 C CA . TYR A 177 ? 0.5459 0.6067 0.5727 -0.0493 -0.0826 0.0240 154 TYR A CA 1220 C C . TYR A 177 ? 0.5123 0.5812 0.5602 -0.0578 -0.0801 0.0214 154 TYR A C 1221 O O . TYR A 177 ? 0.5203 0.5805 0.5704 -0.0602 -0.0707 0.0223 154 TYR A O 1222 C CB . TYR A 177 ? 0.4985 0.5390 0.5047 -0.0517 -0.0800 0.0190 154 TYR A CB 1223 C CG . TYR A 177 ? 0.4730 0.5035 0.4605 -0.0430 -0.0769 0.0220 154 TYR A CG 1224 C CD1 . TYR A 177 ? 0.4425 0.4692 0.4310 -0.0373 -0.0687 0.0274 154 TYR A CD1 1225 C CD2 . TYR A 177 ? 0.4723 0.4978 0.4412 -0.0408 -0.0819 0.0188 154 TYR A CD2 1226 C CE1 . TYR A 177 ? 0.4730 0.4933 0.4482 -0.0303 -0.0652 0.0295 154 TYR A CE1 1227 C CE2 . TYR A 177 ? 0.5566 0.5741 0.5098 -0.0332 -0.0771 0.0215 154 TYR A CE2 1228 C CZ . TYR A 177 ? 0.5835 0.5993 0.5417 -0.0282 -0.0686 0.0269 154 TYR A CZ 1229 O OH . TYR A 177 ? 0.5716 0.5822 0.5179 -0.0215 -0.0633 0.0289 154 TYR A OH 1230 N N . TYR A 178 ? 0.5321 0.6188 0.5956 -0.0621 -0.0886 0.0181 155 TYR A N 1231 C CA . TYR A 178 ? 0.5611 0.6581 0.6474 -0.0718 -0.0859 0.0143 155 TYR A CA 1232 C C . TYR A 178 ? 0.5714 0.6941 0.6840 -0.0685 -0.0894 0.0172 155 TYR A C 1233 O O . TYR A 178 ? 0.6683 0.8045 0.7831 -0.0621 -0.1002 0.0187 155 TYR A O 1234 C CB . TYR A 178 ? 0.5330 0.6286 0.6186 -0.0834 -0.0924 0.0048 155 TYR A CB 1235 C CG . TYR A 178 ? 0.6088 0.6774 0.6681 -0.0859 -0.0893 0.0012 155 TYR A CG 1236 C CD1 . TYR A 178 ? 0.5323 0.5930 0.5691 -0.0802 -0.0962 -0.0005 155 TYR A CD1 1237 C CD2 . TYR A 178 ? 0.6034 0.6534 0.6593 -0.0929 -0.0786 -0.0002 155 TYR A CD2 1238 C CE1 . TYR A 178 ? 0.6263 0.6626 0.6402 -0.0812 -0.0925 -0.0043 155 TYR A CE1 1239 C CE2 . TYR A 178 ? 0.6164 0.6406 0.6488 -0.0933 -0.0757 -0.0031 155 TYR A CE2 1240 C CZ . TYR A 178 ? 0.7072 0.7254 0.7198 -0.0873 -0.0826 -0.0057 155 TYR A CZ 1241 O OH . TYR A 178 ? 0.8477 0.8406 0.8381 -0.0866 -0.0790 -0.0092 155 TYR A OH 1242 N N . PHE A 179 ? 0.6343 0.7627 0.7654 -0.0718 -0.0797 0.0182 156 PHE A N 1243 C CA . PHE A 179 ? 0.6079 0.7617 0.7680 -0.0694 -0.0813 0.0193 156 PHE A CA 1244 C C . PHE A 179 ? 0.6762 0.8434 0.8589 -0.0828 -0.0804 0.0120 156 PHE A C 1245 O O . PHE A 179 ? 0.6828 0.8460 0.8739 -0.0895 -0.0676 0.0115 156 PHE A O 1246 C CB . PHE A 179 ? 0.5361 0.6876 0.7015 -0.0627 -0.0694 0.0252 156 PHE A CB 1247 C CG . PHE A 179 ? 0.5791 0.7198 0.7273 -0.0508 -0.0700 0.0317 156 PHE A CG 1248 C CD1 . PHE A 179 ? 0.6870 0.8312 0.8270 -0.0435 -0.0813 0.0344 156 PHE A CD1 1249 C CD2 . PHE A 179 ? 0.6168 0.7435 0.7562 -0.0473 -0.0590 0.0351 156 PHE A CD2 1250 C CE1 . PHE A 179 ? 0.6916 0.8249 0.8165 -0.0339 -0.0800 0.0407 156 PHE A CE1 1251 C CE2 . PHE A 179 ? 0.6134 0.7312 0.7398 -0.0381 -0.0591 0.0401 156 PHE A CE2 1252 C CZ . PHE A 179 ? 0.6135 0.7340 0.7332 -0.0318 -0.0687 0.0432 156 PHE A CZ 1253 N N . GLY A 180 ? 0.6672 0.8502 0.8590 -0.0871 -0.0939 0.0061 157 GLY A N 1254 C CA . GLY A 180 ? 0.7702 0.9657 0.9835 -0.1021 -0.0944 -0.0026 157 GLY A CA 1255 C C . GLY A 180 ? 0.7771 0.9466 0.9687 -0.1135 -0.0914 -0.0081 157 GLY A C 1256 O O . GLY A 180 ? 0.7086 0.8659 0.8769 -0.1116 -0.1006 -0.0106 157 GLY A O 1257 N N . SER A 181 ? 0.8613 1.0205 1.0590 -0.1247 -0.0776 -0.0098 158 SER A N 1258 C CA . SER A 181 ? 0.9454 1.0756 1.1219 -0.1348 -0.0726 -0.0140 158 SER A CA 1259 C C . SER A 181 ? 0.9125 1.0137 1.0622 -0.1273 -0.0605 -0.0061 158 SER A C 1260 O O . SER A 181 ? 0.9962 1.0698 1.1236 -0.1311 -0.0564 -0.0074 158 SER A O 1261 C CB . SER A 181 ? 0.9816 1.1153 1.1797 -0.1528 -0.0646 -0.0204 158 SER A CB 1262 O OG . SER A 181 ? 0.9607 1.0986 1.1732 -0.1534 -0.0490 -0.0147 158 SER A OG 1263 N N . GLN A 182 ? 0.6783 0.7859 0.8307 -0.1162 -0.0555 0.0017 159 GLN A N 1264 C CA . GLN A 182 ? 0.5430 0.6277 0.6737 -0.1093 -0.0448 0.0086 159 GLN A CA 1265 C C . GLN A 182 ? 0.4285 0.5023 0.5353 -0.0969 -0.0513 0.0120 159 GLN A C 1266 O O . GLN A 182 ? 0.4743 0.5626 0.5855 -0.0879 -0.0587 0.0144 159 GLN A O 1267 C CB . GLN A 182 ? 0.5841 0.6798 0.7290 -0.1050 -0.0348 0.0138 159 GLN A CB 1268 C CG . GLN A 182 ? 0.7774 0.8525 0.9001 -0.0973 -0.0256 0.0201 159 GLN A CG 1269 C CD . GLN A 182 ? 0.9765 1.0249 1.0805 -0.1043 -0.0164 0.0205 159 GLN A CD 1270 O OE1 . GLN A 182 ? 1.1286 1.1752 1.2420 -0.1164 -0.0098 0.0177 159 GLN A OE1 1271 N NE2 . GLN A 182 ? 0.9050 0.9324 0.9830 -0.0965 -0.0157 0.0242 159 GLN A NE2 1272 N N . PHE A 183 ? 0.5010 0.5487 0.5831 -0.0963 -0.0478 0.0124 160 PHE A N 1273 C CA . PHE A 183 ? 0.4735 0.5109 0.5348 -0.0846 -0.0509 0.0158 160 PHE A CA 1274 C C . PHE A 183 ? 0.5054 0.5471 0.5685 -0.0754 -0.0453 0.0227 160 PHE A C 1275 O O . PHE A 183 ? 0.5475 0.5826 0.6108 -0.0769 -0.0357 0.0252 160 PHE A O 1276 C CB . PHE A 183 ? 0.5479 0.5575 0.5854 -0.0853 -0.0473 0.0145 160 PHE A CB 1277 C CG . PHE A 183 ? 0.5968 0.5973 0.6159 -0.0732 -0.0483 0.0180 160 PHE A CG 1278 C CD1 . PHE A 183 ? 0.5043 0.5079 0.5151 -0.0683 -0.0564 0.0159 160 PHE A CD1 1279 C CD2 . PHE A 183 ? 0.4909 0.4805 0.5010 -0.0670 -0.0410 0.0232 160 PHE A CD2 1280 C CE1 . PHE A 183 ? 0.5329 0.5296 0.5293 -0.0581 -0.0555 0.0189 160 PHE A CE1 1281 C CE2 . PHE A 183 ? 0.4962 0.4807 0.4934 -0.0566 -0.0420 0.0255 160 PHE A CE2 1282 C CZ . PHE A 183 ? 0.5257 0.5140 0.5173 -0.0525 -0.0485 0.0234 160 PHE A CZ 1283 N N . SER A 184 ? 0.5433 0.5948 0.6065 -0.0663 -0.0510 0.0255 161 SER A N 1284 C CA . SER A 184 ? 0.5061 0.5602 0.5708 -0.0581 -0.0461 0.0308 161 SER A CA 1285 C C . SER A 184 ? 0.5364 0.5727 0.5810 -0.0529 -0.0423 0.0328 161 SER A C 1286 O O . SER A 184 ? 0.4785 0.5105 0.5117 -0.0476 -0.0464 0.0332 161 SER A O 1287 C CB . SER A 184 ? 0.5079 0.5767 0.5805 -0.0508 -0.0527 0.0335 161 SER A CB 1288 O OG . SER A 184 ? 0.5301 0.5987 0.6038 -0.0439 -0.0475 0.0377 161 SER A OG 1289 N N . VAL A 185 ? 0.4668 0.4935 0.5071 -0.0541 -0.0343 0.0340 162 VAL A N 1290 C CA . VAL A 185 ? 0.4592 0.4710 0.4819 -0.0484 -0.0316 0.0358 162 VAL A CA 1291 C C . VAL A 185 ? 0.4867 0.5053 0.5098 -0.0400 -0.0336 0.0379 162 VAL A C 1292 O O . VAL A 185 ? 0.5392 0.5516 0.5516 -0.0348 -0.0354 0.0381 162 VAL A O 1293 C CB . VAL A 185 ? 0.5224 0.5239 0.5393 -0.0505 -0.0233 0.0375 162 VAL A CB 1294 C CG1 . VAL A 185 ? 0.4358 0.4247 0.4352 -0.0428 -0.0227 0.0395 162 VAL A CG1 1295 C CG2 . VAL A 185 ? 0.5297 0.5208 0.5449 -0.0598 -0.0196 0.0360 162 VAL A CG2 1296 N N . ASP A 186 ? 0.4353 0.4667 0.4724 -0.0389 -0.0324 0.0392 163 ASP A N 1297 C CA . ASP A 186 ? 0.4529 0.4893 0.4922 -0.0325 -0.0331 0.0409 163 ASP A CA 1298 C C . ASP A 186 ? 0.3765 0.4146 0.4121 -0.0293 -0.0387 0.0418 163 ASP A C 1299 O O . ASP A 186 ? 0.4518 0.4868 0.4808 -0.0250 -0.0385 0.0425 163 ASP A O 1300 C CB . ASP A 186 ? 0.4888 0.5366 0.5445 -0.0319 -0.0308 0.0418 163 ASP A CB 1301 C CG . ASP A 186 ? 0.5733 0.6213 0.6338 -0.0358 -0.0240 0.0405 163 ASP A CG 1302 O OD1 . ASP A 186 ? 0.5141 0.5645 0.5799 -0.0417 -0.0233 0.0394 163 ASP A OD1 1303 O OD2 . ASP A 186 ? 0.5447 0.5905 0.6038 -0.0335 -0.0190 0.0400 163 ASP A OD2 1304 N N . THR A 187 ? 0.4569 0.5011 0.4969 -0.0318 -0.0436 0.0415 164 THR A N 1305 C CA . THR A 187 ? 0.4096 0.4548 0.4427 -0.0289 -0.0491 0.0423 164 THR A CA 1306 C C . THR A 187 ? 0.4825 0.5154 0.4987 -0.0283 -0.0490 0.0399 164 THR A C 1307 O O . THR A 187 ? 0.4442 0.4750 0.4527 -0.0235 -0.0485 0.0412 164 THR A O 1308 C CB . THR A 187 ? 0.4240 0.4785 0.4635 -0.0320 -0.0561 0.0413 164 THR A CB 1309 O OG1 . THR A 187 ? 0.4920 0.5593 0.5496 -0.0309 -0.0560 0.0436 164 THR A OG1 1310 C CG2 . THR A 187 ? 0.3764 0.4310 0.4047 -0.0281 -0.0620 0.0426 164 THR A CG2 1311 N N . GLY A 188 ? 0.4498 0.4740 0.4609 -0.0330 -0.0484 0.0364 165 GLY A N 1312 C CA . GLY A 188 ? 0.3780 0.3882 0.3733 -0.0314 -0.0476 0.0339 165 GLY A CA 1313 C C . GLY A 188 ? 0.5181 0.5243 0.5089 -0.0248 -0.0435 0.0357 165 GLY A C 1314 O O . GLY A 188 ? 0.4808 0.4825 0.4626 -0.0200 -0.0432 0.0347 165 GLY A O 1315 N N . ALA A 189 ? 0.4088 0.4180 0.4066 -0.0245 -0.0403 0.0376 166 ALA A N 1316 C CA . ALA A 189 ? 0.4357 0.4436 0.4309 -0.0187 -0.0381 0.0384 166 ALA A CA 1317 C C . ALA A 189 ? 0.4538 0.4711 0.4542 -0.0148 -0.0381 0.0395 166 ALA A C 1318 O O . ALA A 189 ? 0.4280 0.4447 0.4248 -0.0101 -0.0373 0.0386 166 ALA A O 1319 C CB . ALA A 189 ? 0.4070 0.4157 0.4062 -0.0198 -0.0353 0.0393 166 ALA A CB 1320 N N . MET A 190 ? 0.3559 0.3818 0.3658 -0.0166 -0.0385 0.0415 167 MET A N 1321 C CA . MET A 190 ? 0.4471 0.4791 0.4614 -0.0138 -0.0371 0.0437 167 MET A CA 1322 C C . MET A 190 ? 0.4385 0.4681 0.4428 -0.0117 -0.0377 0.0438 167 MET A C 1323 O O . MET A 190 ? 0.4854 0.5173 0.4896 -0.0087 -0.0344 0.0445 167 MET A O 1324 C CB . MET A 190 ? 0.3883 0.4265 0.4130 -0.0151 -0.0370 0.0468 167 MET A CB 1325 C CG . MET A 190 ? 0.4090 0.4502 0.4391 -0.0130 -0.0336 0.0495 167 MET A CG 1326 S SD . MET A 190 ? 0.4648 0.5075 0.5011 -0.0128 -0.0298 0.0459 167 MET A SD 1327 C CE . MET A 190 ? 0.3638 0.4064 0.4064 -0.0150 -0.0298 0.0439 167 MET A CE 1328 N N . ALA A 191 ? 0.4333 0.4585 0.4295 -0.0137 -0.0415 0.0424 168 ALA A N 1329 C CA . ALA A 191 ? 0.4960 0.5169 0.4791 -0.0117 -0.0422 0.0411 168 ALA A CA 1330 C C . ALA A 191 ? 0.5228 0.5373 0.4991 -0.0076 -0.0386 0.0380 168 ALA A C 1331 O O . ALA A 191 ? 0.5012 0.5164 0.4722 -0.0037 -0.0352 0.0379 168 ALA A O 1332 C CB . ALA A 191 ? 0.4990 0.5162 0.4750 -0.0157 -0.0481 0.0382 168 ALA A CB 1333 N N . VAL A 192 ? 0.4718 0.4801 0.4481 -0.0079 -0.0389 0.0358 169 VAL A N 1334 C CA . VAL A 192 ? 0.4851 0.4874 0.4563 -0.0022 -0.0364 0.0334 169 VAL A CA 1335 C C . VAL A 192 ? 0.4331 0.4466 0.4140 0.0024 -0.0330 0.0346 169 VAL A C 1336 O O . VAL A 192 ? 0.4826 0.4970 0.4614 0.0077 -0.0299 0.0328 169 VAL A O 1337 C CB . VAL A 192 ? 0.5016 0.4941 0.4701 -0.0025 -0.0374 0.0327 169 VAL A CB 1338 C CG1 . VAL A 192 ? 0.4731 0.4626 0.4391 0.0057 -0.0359 0.0318 169 VAL A CG1 1339 C CG2 . VAL A 192 ? 0.3892 0.3678 0.3473 -0.0073 -0.0391 0.0302 169 VAL A CG2 1340 N N . LEU A 193 ? 0.3691 0.3913 0.3619 -0.0002 -0.0331 0.0369 170 LEU A N 1341 C CA . LEU A 193 ? 0.4196 0.4529 0.4240 0.0020 -0.0301 0.0369 170 LEU A CA 1342 C C . LEU A 193 ? 0.5281 0.5661 0.5333 0.0022 -0.0254 0.0385 170 LEU A C 1343 O O . LEU A 193 ? 0.4795 0.5247 0.4909 0.0053 -0.0211 0.0371 170 LEU A O 1344 C CB . LEU A 193 ? 0.3833 0.4221 0.3985 -0.0018 -0.0309 0.0379 170 LEU A CB 1345 C CG . LEU A 193 ? 0.4850 0.5203 0.4984 -0.0016 -0.0341 0.0363 170 LEU A CG 1346 C CD1 . LEU A 193 ? 0.5004 0.5397 0.5223 -0.0057 -0.0337 0.0367 170 LEU A CD1 1347 C CD2 . LEU A 193 ? 0.4109 0.4496 0.4249 0.0043 -0.0356 0.0336 170 LEU A CD2 1348 N N . ALA A 194 ? 0.4925 0.5272 0.4917 -0.0007 -0.0260 0.0415 171 ALA A N 1349 C CA . ALA A 194 ? 0.4852 0.5214 0.4802 -0.0003 -0.0213 0.0445 171 ALA A CA 1350 C C . ALA A 194 ? 0.4871 0.5190 0.4694 0.0040 -0.0184 0.0416 171 ALA A C 1351 O O . ALA A 194 ? 0.4961 0.5328 0.4803 0.0063 -0.0112 0.0419 171 ALA A O 1352 C CB . ALA A 194 ? 0.4127 0.4459 0.4021 -0.0029 -0.0246 0.0489 171 ALA A CB 1353 N N . LEU A 195 ? 0.5433 0.5658 0.5134 0.0046 -0.0230 0.0383 172 LEU A N 1354 C CA . LEU A 195 ? 0.5312 0.5465 0.4871 0.0089 -0.0203 0.0342 172 LEU A CA 1355 C C . LEU A 195 ? 0.5810 0.6005 0.5447 0.0151 -0.0153 0.0312 172 LEU A C 1356 O O . LEU A 195 ? 0.5151 0.5348 0.4734 0.0198 -0.0090 0.0289 172 LEU A O 1357 C CB . LEU A 195 ? 0.4704 0.4727 0.4134 0.0071 -0.0265 0.0301 172 LEU A CB 1358 C CG . LEU A 195 ? 0.4674 0.4679 0.4029 0.0015 -0.0327 0.0313 172 LEU A CG 1359 C CD1 . LEU A 195 ? 0.4631 0.4524 0.3910 -0.0024 -0.0385 0.0261 172 LEU A CD1 1360 C CD2 . LEU A 195 ? 0.4679 0.4683 0.3889 0.0033 -0.0304 0.0324 172 LEU A CD2 1361 N N . THR A 196 ? 0.4462 0.4699 0.4224 0.0157 -0.0182 0.0310 173 THR A N 1362 C CA . THR A 196 ? 0.4663 0.4964 0.4517 0.0226 -0.0160 0.0282 173 THR A CA 1363 C C . THR A 196 ? 0.5847 0.6313 0.5853 0.0229 -0.0091 0.0289 173 THR A C 1364 O O . THR A 196 ? 0.4990 0.5529 0.5058 0.0291 -0.0042 0.0259 173 THR A O 1365 C CB . THR A 196 ? 0.5283 0.5587 0.5206 0.0232 -0.0221 0.0282 173 THR A CB 1366 O OG1 . THR A 196 ? 0.4844 0.4984 0.4630 0.0214 -0.0265 0.0282 173 THR A OG1 1367 C CG2 . THR A 196 ? 0.4022 0.4397 0.4027 0.0321 -0.0219 0.0254 173 THR A CG2 1368 N N . CYS A 197 ? 0.5220 0.5742 0.5296 0.0161 -0.0080 0.0328 174 CYS A N 1369 C CA . CYS A 197 ? 0.4882 0.5534 0.5100 0.0142 -0.0002 0.0339 174 CYS A CA 1370 C C . CYS A 197 ? 0.4962 0.5594 0.5077 0.0166 0.0090 0.0345 174 CYS A C 1371 O O . CYS A 197 ? 0.5589 0.6333 0.5815 0.0189 0.0172 0.0327 174 CYS A O 1372 C CB . CYS A 197 ? 0.5180 0.5844 0.5465 0.0066 -0.0003 0.0385 174 CYS A CB 1373 S SG . CYS A 197 ? 0.5577 0.6361 0.6035 0.0020 0.0110 0.0404 174 CYS A SG 1374 N N . VAL A 198 ? 0.4947 0.5445 0.4850 0.0158 0.0076 0.0367 175 VAL A N 1375 C CA . VAL A 198 ? 0.5594 0.6045 0.5337 0.0184 0.0156 0.0369 175 VAL A CA 1376 C C . VAL A 198 ? 0.6246 0.6701 0.5971 0.0263 0.0195 0.0303 175 VAL A C 1377 O O . VAL A 198 ? 0.5871 0.6375 0.5591 0.0295 0.0303 0.0292 175 VAL A O 1378 C CB . VAL A 198 ? 0.4941 0.5250 0.4443 0.0166 0.0102 0.0389 175 VAL A CB 1379 C CG1 . VAL A 198 ? 0.5787 0.6039 0.5085 0.0195 0.0184 0.0388 175 VAL A CG1 1380 C CG2 . VAL A 198 ? 0.4001 0.4313 0.3537 0.0108 0.0058 0.0457 175 VAL A CG2 1381 N N . LYS A 199 ? 0.6527 0.6920 0.6242 0.0299 0.0116 0.0262 176 LYS A N 1382 C CA . LYS A 199 ? 0.6303 0.6678 0.6011 0.0390 0.0144 0.0203 176 LYS A CA 1383 C C . LYS A 199 ? 0.5459 0.6037 0.5409 0.0435 0.0211 0.0188 176 LYS A C 1384 O O . LYS A 199 ? 0.5233 0.5857 0.5191 0.0498 0.0305 0.0155 176 LYS A O 1385 C CB . LYS A 199 ? 0.7318 0.7576 0.6985 0.0416 0.0046 0.0179 176 LYS A CB 1386 C CG . LYS A 199 ? 0.8248 0.8300 0.7680 0.0383 -0.0001 0.0163 176 LYS A CG 1387 C CD . LYS A 199 ? 0.8906 0.8862 0.8335 0.0354 -0.0095 0.0170 176 LYS A CD 1388 C CE . LYS A 199 ? 0.9308 0.9230 0.8792 0.0440 -0.0106 0.0150 176 LYS A CE 1389 N NZ . LYS A 199 ? 0.7846 0.7654 0.7299 0.0408 -0.0181 0.0168 176 LYS A NZ 1390 N N . LYS A 200 ? 0.4279 0.4987 0.4433 0.0401 0.0164 0.0206 177 LYS A N 1391 C CA . LYS A 200 ? 0.4624 0.5555 0.5042 0.0430 0.0207 0.0182 177 LYS A CA 1392 C C . LYS A 200 ? 0.5847 0.6881 0.6334 0.0388 0.0343 0.0197 177 LYS A C 1393 O O . LYS A 200 ? 0.5395 0.6583 0.6036 0.0436 0.0429 0.0162 177 LYS A O 1394 C CB . LYS A 200 ? 0.4894 0.5930 0.5487 0.0384 0.0121 0.0189 177 LYS A CB 1395 C CG . LYS A 200 ? 0.4866 0.5790 0.5369 0.0420 0.0001 0.0186 177 LYS A CG 1396 C CD . LYS A 200 ? 0.5933 0.6941 0.6564 0.0367 -0.0076 0.0191 177 LYS A CD 1397 C CE . LYS A 200 ? 0.7179 0.8395 0.8030 0.0425 -0.0108 0.0147 177 LYS A CE 1398 N NZ . LYS A 200 ? 0.7223 0.8382 0.8002 0.0551 -0.0163 0.0130 177 LYS A NZ 1399 N N . SER A 201 ? 0.5610 0.6557 0.5982 0.0304 0.0365 0.0253 178 SER A N 1400 C CA . SER A 201 ? 0.5834 0.6830 0.6221 0.0257 0.0501 0.0289 178 SER A CA 1401 C C . SER A 201 ? 0.6205 0.7151 0.6429 0.0322 0.0609 0.0267 178 SER A C 1402 O O . SER A 201 ? 0.6534 0.7589 0.6850 0.0319 0.0749 0.0267 178 SER A O 1403 C CB . SER A 201 ? 0.6071 0.6942 0.6322 0.0174 0.0486 0.0365 178 SER A CB 1404 O OG . SER A 201 ? 0.7229 0.8110 0.7459 0.0132 0.0624 0.0414 178 SER A OG 1405 N N . LEU A 202 ? 0.7103 0.7877 0.7085 0.0376 0.0550 0.0242 179 LEU A N 1406 C CA . LEU A 202 ? 0.6980 0.7676 0.6773 0.0445 0.0642 0.0203 179 LEU A CA 1407 C C . LEU A 202 ? 0.7509 0.8342 0.7487 0.0543 0.0705 0.0135 179 LEU A C 1408 O O . LEU A 202 ? 0.7869 0.8764 0.7849 0.0582 0.0849 0.0113 179 LEU A O 1409 C CB . LEU A 202 ? 0.6641 0.7109 0.6141 0.0466 0.0548 0.0179 179 LEU A CB 1410 C CG . LEU A 202 ? 0.8042 0.8374 0.7288 0.0399 0.0520 0.0231 179 LEU A CG 1411 C CD1 . LEU A 202 ? 0.7701 0.7844 0.6719 0.0407 0.0406 0.0189 179 LEU A CD1 1412 C CD2 . LEU A 202 ? 0.8216 0.8536 0.7302 0.0406 0.0665 0.0250 179 LEU A CD2 1413 N N . ILE A 203 ? 0.7186 0.8064 0.7312 0.0591 0.0599 0.0104 180 ILE A N 1414 C CA . ILE A 203 ? 0.6583 0.7599 0.6901 0.0704 0.0630 0.0044 180 ILE A CA 1415 C C . ILE A 203 ? 0.6417 0.7726 0.7062 0.0683 0.0727 0.0041 180 ILE A C 1416 O O . ILE A 203 ? 0.6173 0.7625 0.6963 0.0766 0.0828 -0.0007 180 ILE A O 1417 C CB . ILE A 203 ? 0.6561 0.7541 0.6935 0.0763 0.0480 0.0028 180 ILE A CB 1418 C CG1 . ILE A 203 ? 0.6618 0.7300 0.6681 0.0773 0.0408 0.0023 180 ILE A CG1 1419 C CG2 . ILE A 203 ? 0.6140 0.7276 0.6724 0.0898 0.0498 -0.0026 180 ILE A CG2 1420 C CD1 . ILE A 203 ? 0.6061 0.6658 0.6133 0.0822 0.0279 0.0021 180 ILE A CD1 1421 N N . ASN A 204 ? 0.5878 0.7274 0.6652 0.0568 0.0704 0.0088 181 ASN A N 1422 C CA . ASN A 204 ? 0.6758 0.8405 0.7828 0.0511 0.0811 0.0087 181 ASN A CA 1423 C C . ASN A 204 ? 0.8165 0.9761 0.9102 0.0464 0.0992 0.0122 181 ASN A C 1424 O O . ASN A 204 ? 0.9317 1.0716 0.9945 0.0505 0.1030 0.0129 181 ASN A O 1425 C CB . ASN A 204 ? 0.6439 0.8158 0.7670 0.0397 0.0730 0.0118 181 ASN A CB 1426 C CG . ASN A 204 ? 0.6954 0.8727 0.8295 0.0441 0.0557 0.0084 181 ASN A CG 1427 O OD1 . ASN A 204 ? 0.7426 0.9265 0.8830 0.0558 0.0513 0.0036 181 ASN A OD1 1428 N ND2 . ASN A 204 ? 0.7382 0.9115 0.8732 0.0353 0.0464 0.0112 181 ASN A ND2 1429 N N . GLY A 205 ? 0.8879 1.0641 1.0034 0.0375 0.1105 0.0144 182 GLY A N 1430 C CA . GLY A 205 ? 1.0707 1.2411 1.1728 0.0327 0.1293 0.0191 182 GLY A CA 1431 C C . GLY A 205 ? 1.0909 1.2451 1.1771 0.0208 0.1294 0.0287 182 GLY A C 1432 O O . GLY A 205 ? 1.2430 1.3922 1.3196 0.0153 0.1451 0.0345 182 GLY A O 1433 N N . GLN A 206 ? 0.8947 1.0397 0.9772 0.0176 0.1124 0.0307 183 GLN A N 1434 C CA . GLN A 206 ? 0.8735 1.0045 0.9457 0.0075 0.1110 0.0394 183 GLN A CA 1435 C C . GLN A 206 ? 0.8848 0.9912 0.9170 0.0086 0.1140 0.0468 183 GLN A C 1436 O O . GLN A 206 ? 1.0074 1.1051 1.0304 0.0020 0.1235 0.0552 183 GLN A O 1437 C CB . GLN A 206 ? 0.9478 1.0765 1.0272 0.0050 0.0925 0.0387 183 GLN A CB 1438 C CG . GLN A 206 ? 1.0881 1.2354 1.2027 -0.0028 0.0914 0.0357 183 GLN A CG 1439 C CD . GLN A 206 ? 1.1822 1.3553 1.3260 0.0024 0.0906 0.0263 183 GLN A CD 1440 O OE1 . GLN A 206 ? 1.1992 1.3772 1.3482 0.0085 0.0763 0.0212 183 GLN A OE1 1441 N NE2 . GLN A 206 ? 1.2212 1.4117 1.3845 0.0003 0.1064 0.0243 183 GLN A NE2 1442 N N . ILE A 207 ? 0.8433 0.9378 0.8513 0.0168 0.1056 0.0436 184 ILE A N 1443 C CA . ILE A 207 ? 0.9943 1.0665 0.9639 0.0178 0.1039 0.0492 184 ILE A CA 1444 C C . ILE A 207 ? 1.0746 1.1387 1.0193 0.0266 0.1079 0.0435 184 ILE A C 1445 O O . ILE A 207 ? 1.2652 1.3323 1.2151 0.0335 0.1020 0.0351 184 ILE A O 1446 C CB . ILE A 207 ? 1.1082 1.1688 1.0688 0.0160 0.0850 0.0515 184 ILE A CB 1447 C CG1 . ILE A 207 ? 1.1919 1.2530 1.1656 0.0075 0.0842 0.0592 184 ILE A CG1 1448 C CG2 . ILE A 207 ? 1.1994 1.2408 1.1226 0.0192 0.0794 0.0534 184 ILE A CG2 1449 C CD1 . ILE A 207 ? 1.2775 1.3286 1.2350 0.0037 0.0970 0.0692 184 ILE A CD1 1450 N N . LYS A 208 ? 0.9556 1.0076 0.8713 0.0268 0.1184 0.0483 185 LYS A N 1451 C CA . LYS A 208 ? 1.0627 1.1035 0.9486 0.0346 0.1220 0.0426 185 LYS A CA 1452 C C . LYS A 208 ? 1.0378 1.0587 0.8907 0.0352 0.1062 0.0434 185 LYS A C 1453 O O . LYS A 208 ? 1.0706 1.0857 0.9180 0.0299 0.0976 0.0515 185 LYS A O 1454 C CB . LYS A 208 ? 1.1820 1.2212 1.0521 0.0350 0.1436 0.0464 185 LYS A CB 1455 C CG . LYS A 208 ? 1.3071 1.3683 1.2119 0.0334 0.1613 0.0450 185 LYS A CG 1456 C CD . LYS A 208 ? 1.4314 1.4894 1.3186 0.0326 0.1846 0.0499 185 LYS A CD 1457 C CE . LYS A 208 ? 1.4604 1.5431 1.3866 0.0296 0.2033 0.0480 185 LYS A CE 1458 N NZ . LYS A 208 ? 1.5035 1.5826 1.4131 0.0276 0.2284 0.0536 185 LYS A NZ 1459 N N . ALA A 209 ? 0.9905 1.0014 0.8232 0.0416 0.1023 0.0344 186 ALA A N 1460 C CA . ALA A 209 ? 0.8612 0.8549 0.6642 0.0413 0.0869 0.0329 186 ALA A CA 1461 C C . ALA A 209 ? 0.8896 0.8700 0.6628 0.0479 0.0902 0.0228 186 ALA A C 1462 O O . ALA A 209 ? 0.9594 0.9440 0.7385 0.0540 0.1034 0.0164 186 ALA A O 1463 C CB . ALA A 209 ? 0.7272 0.7224 0.5483 0.0388 0.0690 0.0304 186 ALA A CB 1464 N N . ASP A 210 ? 0.9332 0.8982 0.6755 0.0469 0.0781 0.0208 187 ASP A N 1465 C CA . ASP A 210 ? 1.0531 1.0030 0.7659 0.0519 0.0784 0.0092 187 ASP A CA 1466 C C . ASP A 210 ? 1.0246 0.9738 0.7566 0.0556 0.0749 -0.0013 187 ASP A C 1467 O O . ASP A 210 ? 1.0579 1.0096 0.8094 0.0519 0.0615 -0.0009 187 ASP A O 1468 C CB . ASP A 210 ? 1.2120 1.1481 0.8930 0.0485 0.0622 0.0079 187 ASP A CB 1469 C CG . ASP A 210 ? 1.3944 1.3277 1.0484 0.0475 0.0654 0.0181 187 ASP A CG 1470 O OD1 . ASP A 210 ? 1.4093 1.3442 1.0560 0.0506 0.0841 0.0226 187 ASP A OD1 1471 O OD2 . ASP A 210 ? 1.5022 1.4317 1.1425 0.0440 0.0497 0.0220 187 ASP A OD2 1472 N N . GLU A 211 ? 0.9683 0.9133 0.6943 0.0636 0.0878 -0.0101 188 GLU A N 1473 C CA . GLU A 211 ? 1.0272 0.9690 0.7693 0.0695 0.0861 -0.0195 188 GLU A CA 1474 C C . GLU A 211 ? 1.0926 1.0170 0.8225 0.0656 0.0682 -0.0260 188 GLU A C 1475 O O . GLU A 211 ? 1.0355 0.9451 0.7334 0.0624 0.0620 -0.0306 188 GLU A O 1476 C CB . GLU A 211 ? 1.0575 0.9943 0.7890 0.0800 0.1032 -0.0288 188 GLU A CB 1477 C CG . GLU A 211 ? 1.0971 1.0535 0.8453 0.0835 0.1230 -0.0233 188 GLU A CG 1478 C CD . GLU A 211 ? 1.3032 1.2561 1.0426 0.0947 0.1410 -0.0332 188 GLU A CD 1479 O OE1 . GLU A 211 ? 1.4508 1.3998 1.1645 0.0956 0.1552 -0.0331 188 GLU A OE1 1480 O OE2 . GLU A 211 ? 1.3369 1.2902 1.0944 0.1033 0.1416 -0.0407 188 GLU A OE2 1481 N N . GLY A 212 ? 1.1026 1.0293 0.8579 0.0654 0.0600 -0.0263 189 GLY A N 1482 C CA . GLY A 212 ? 1.0573 0.9688 0.8063 0.0601 0.0444 -0.0311 189 GLY A CA 1483 C C . GLY A 212 ? 0.9859 0.9079 0.7518 0.0507 0.0313 -0.0220 189 GLY A C 1484 O O . GLY A 212 ? 0.9557 0.8691 0.7234 0.0452 0.0191 -0.0244 189 GLY A O 1485 N N . SER A 213 ? 0.8893 0.8291 0.6681 0.0487 0.0351 -0.0116 190 SER A N 1486 C CA . SER A 213 ? 0.8450 0.7949 0.6404 0.0409 0.0244 -0.0028 190 SER A CA 1487 C C . SER A 213 ? 0.8254 0.7806 0.6491 0.0412 0.0201 -0.0021 190 SER A C 1488 O O . SER A 213 ? 0.7794 0.7332 0.6102 0.0351 0.0086 -0.0003 190 SER A O 1489 C CB . SER A 213 ? 0.8227 0.7875 0.6253 0.0393 0.0315 0.0078 190 SER A CB 1490 O OG . SER A 213 ? 0.9532 0.9114 0.7261 0.0393 0.0350 0.0091 190 SER A OG 1491 N N . LEU A 214 ? 0.7558 0.7175 0.5952 0.0490 0.0295 -0.0037 191 LEU A N 1492 C CA . LEU A 214 ? 0.7570 0.7237 0.6206 0.0513 0.0253 -0.0030 191 LEU A CA 1493 C C . LEU A 214 ? 0.7856 0.7324 0.6393 0.0506 0.0163 -0.0087 191 LEU A C 1494 O O . LEU A 214 ? 0.6737 0.6204 0.5398 0.0473 0.0083 -0.0059 191 LEU A O 1495 C CB . LEU A 214 ? 0.7204 0.6981 0.6007 0.0616 0.0362 -0.0050 191 LEU A CB 1496 C CG . LEU A 214 ? 0.7274 0.7119 0.6316 0.0661 0.0311 -0.0040 191 LEU A CG 1497 C CD1 . LEU A 214 ? 0.6460 0.6463 0.5699 0.0584 0.0248 0.0037 191 LEU A CD1 1498 C CD2 . LEU A 214 ? 0.7534 0.7496 0.6735 0.0781 0.0409 -0.0074 191 LEU A CD2 1499 N N . LYS A 215 ? 0.7715 0.7001 0.6015 0.0531 0.0187 -0.0172 192 LYS A N 1500 C CA . LYS A 215 ? 0.7923 0.6984 0.6107 0.0512 0.0117 -0.0240 192 LYS A CA 1501 C C . LYS A 215 ? 0.7923 0.6964 0.6087 0.0387 -0.0009 -0.0216 192 LYS A C 1502 O O . LYS A 215 ? 0.6795 0.5774 0.5051 0.0350 -0.0072 -0.0205 192 LYS A O 1503 C CB . LYS A 215 ? 0.7932 0.6799 0.5847 0.0553 0.0172 -0.0348 192 LYS A CB 1504 C CG . LYS A 215 ? 0.7965 0.6563 0.5754 0.0533 0.0118 -0.0435 192 LYS A CG 1505 C CD . LYS A 215 ? 0.9742 0.8145 0.7270 0.0589 0.0192 -0.0554 192 LYS A CD 1506 C CE . LYS A 215 ? 1.1619 0.9722 0.9004 0.0550 0.0141 -0.0652 192 LYS A CE 1507 N NZ . LYS A 215 ? 1.2845 1.0919 1.0155 0.0395 0.0011 -0.0669 192 LYS A NZ 1508 N N . ASN A 216 ? 0.7673 0.6773 0.5719 0.0327 -0.0040 -0.0203 193 ASN A N 1509 C CA . ASN A 216 ? 0.7586 0.6699 0.5628 0.0218 -0.0163 -0.0186 193 ASN A CA 1510 C C . ASN A 216 ? 0.6856 0.6120 0.5156 0.0181 -0.0205 -0.0092 193 ASN A C 1511 O O . ASN A 216 ? 0.7277 0.6513 0.5644 0.0108 -0.0286 -0.0092 193 ASN A O 1512 C CB . ASN A 216 ? 0.8289 0.7448 0.6143 0.0187 -0.0195 -0.0183 193 ASN A CB 1513 C CG . ASN A 216 ? 1.0206 0.9196 0.7764 0.0209 -0.0173 -0.0293 193 ASN A CG 1514 O OD1 . ASN A 216 ? 1.0048 0.8862 0.7545 0.0226 -0.0153 -0.0383 193 ASN A OD1 1515 N ND2 . ASN A 216 ? 1.1833 1.0856 0.9183 0.0211 -0.0174 -0.0286 193 ASN A ND2 1516 N N . ILE A 217 ? 0.6228 0.5650 0.4672 0.0225 -0.0142 -0.0019 194 ILE A N 1517 C CA . ILE A 217 ? 0.6227 0.5784 0.4904 0.0196 -0.0172 0.0059 194 ILE A CA 1518 C C . ILE A 217 ? 0.6210 0.5698 0.4996 0.0211 -0.0188 0.0045 194 ILE A C 1519 O O . ILE A 217 ? 0.5945 0.5453 0.4835 0.0155 -0.0248 0.0077 194 ILE A O 1520 C CB . ILE A 217 ? 0.6811 0.6537 0.5621 0.0234 -0.0094 0.0124 194 ILE A CB 1521 C CG1 . ILE A 217 ? 0.7158 0.6927 0.5844 0.0212 -0.0076 0.0162 194 ILE A CG1 1522 C CG2 . ILE A 217 ? 0.6622 0.6467 0.5664 0.0206 -0.0124 0.0184 194 ILE A CG2 1523 C CD1 . ILE A 217 ? 0.7032 0.6937 0.5835 0.0234 0.0021 0.0227 194 ILE A CD1 1524 N N . SER A 218 ? 0.6089 0.5488 0.4839 0.0295 -0.0130 0.0000 195 SER A N 1525 C CA . SER A 218 ? 0.6597 0.5896 0.5408 0.0332 -0.0143 -0.0007 195 SER A CA 1526 C C . SER A 218 ? 0.6487 0.5597 0.5197 0.0253 -0.0206 -0.0040 195 SER A C 1527 O O . SER A 218 ? 0.6089 0.5156 0.4875 0.0229 -0.0238 -0.0009 195 SER A O 1528 C CB . SER A 218 ? 0.5696 0.4918 0.4468 0.0454 -0.0068 -0.0053 195 SER A CB 1529 O OG . SER A 218 ? 0.7643 0.7071 0.6561 0.0521 -0.0004 -0.0025 195 SER A OG 1530 N N . ILE A 219 ? 0.5999 0.4996 0.4533 0.0209 -0.0221 -0.0108 196 ILE A N 1531 C CA . ILE A 219 ? 0.6459 0.5293 0.4914 0.0112 -0.0282 -0.0156 196 ILE A CA 1532 C C . ILE A 219 ? 0.7044 0.6017 0.5631 0.0008 -0.0355 -0.0102 196 ILE A C 1533 O O . ILE A 219 ? 0.6328 0.5222 0.4968 -0.0059 -0.0383 -0.0099 196 ILE A O 1534 C CB . ILE A 219 ? 0.6933 0.5639 0.5167 0.0083 -0.0294 -0.0257 196 ILE A CB 1535 C CG1 . ILE A 219 ? 0.7478 0.6005 0.5578 0.0190 -0.0210 -0.0323 196 ILE A CG1 1536 C CG2 . ILE A 219 ? 0.5971 0.4554 0.4164 -0.0043 -0.0370 -0.0314 196 ILE A CG2 1537 C CD1 . ILE A 219 ? 0.6944 0.5329 0.4798 0.0172 -0.0208 -0.0435 196 ILE A CD1 1538 N N . TYR A 220 ? 0.5692 0.4863 0.4331 0.0000 -0.0374 -0.0057 197 TYR A N 1539 C CA . TYR A 220 ? 0.5867 0.5187 0.4652 -0.0075 -0.0434 0.0000 197 TYR A CA 1540 C C . TYR A 220 ? 0.6005 0.5355 0.4955 -0.0067 -0.0414 0.0058 197 TYR A C 1541 O O . TYR A 220 ? 0.5760 0.5111 0.4793 -0.0140 -0.0448 0.0071 197 TYR A O 1542 C CB . TYR A 220 ? 0.5328 0.4829 0.4141 -0.0055 -0.0437 0.0055 197 TYR A CB 1543 C CG . TYR A 220 ? 0.6257 0.5751 0.4891 -0.0070 -0.0477 0.0016 197 TYR A CG 1544 C CD1 . TYR A 220 ? 0.6482 0.5827 0.4947 -0.0105 -0.0513 -0.0080 197 TYR A CD1 1545 C CD2 . TYR A 220 ? 0.6530 0.6152 0.5146 -0.0049 -0.0480 0.0077 197 TYR A CD2 1546 C CE1 . TYR A 220 ? 0.6133 0.5475 0.4409 -0.0117 -0.0562 -0.0124 197 TYR A CE1 1547 C CE2 . TYR A 220 ? 0.6768 0.6377 0.5186 -0.0052 -0.0523 0.0050 197 TYR A CE2 1548 C CZ . TYR A 220 ? 0.7037 0.6515 0.5280 -0.0085 -0.0569 -0.0054 197 TYR A CZ 1549 O OH . TYR A 220 ? 0.6997 0.6465 0.5017 -0.0086 -0.0624 -0.0088 197 TYR A OH 1550 N N . THR A 221 ? 0.6038 0.5424 0.5035 0.0023 -0.0357 0.0089 198 THR A N 1551 C CA . THR A 221 ? 0.6719 0.6139 0.5845 0.0045 -0.0347 0.0139 198 THR A CA 1552 C C . THR A 221 ? 0.6250 0.5473 0.5317 0.0030 -0.0349 0.0121 198 THR A C 1553 O O . THR A 221 ? 0.5746 0.4967 0.4881 -0.0013 -0.0362 0.0159 198 THR A O 1554 C CB . THR A 221 ? 0.6444 0.5952 0.5634 0.0148 -0.0298 0.0159 198 THR A CB 1555 O OG1 . THR A 221 ? 0.7376 0.7047 0.6620 0.0150 -0.0277 0.0179 198 THR A OG1 1556 C CG2 . THR A 221 ? 0.7710 0.7271 0.7020 0.0168 -0.0308 0.0204 198 THR A CG2 1557 N N . LYS A 222 ? 0.6258 0.5295 0.5184 0.0067 -0.0326 0.0066 199 LYS A N 1558 C CA . LYS A 222 ? 0.7430 0.6226 0.6271 0.0053 -0.0317 0.0048 199 LYS A CA 1559 C C . LYS A 222 ? 0.7110 0.5864 0.5973 -0.0087 -0.0351 0.0041 199 LYS A C 1560 O O . LYS A 222 ? 0.6536 0.5198 0.5421 -0.0121 -0.0337 0.0077 199 LYS A O 1561 C CB . LYS A 222 ? 0.7457 0.6045 0.6134 0.0105 -0.0284 -0.0026 199 LYS A CB 1562 C CG . LYS A 222 ? 0.7235 0.5527 0.5808 0.0094 -0.0264 -0.0044 199 LYS A CG 1563 C CD . LYS A 222 ? 0.7642 0.5717 0.6055 0.0168 -0.0223 -0.0123 199 LYS A CD 1564 C CE . LYS A 222 ? 0.8348 0.6084 0.6645 0.0151 -0.0195 -0.0140 199 LYS A CE 1565 N NZ . LYS A 222 ? 0.9000 0.6645 0.7284 -0.0026 -0.0223 -0.0178 199 LYS A NZ 1566 N N . SER A 223 ? 0.6053 0.4882 0.4910 -0.0166 -0.0393 -0.0007 200 SER A N 1567 C CA . SER A 223 ? 0.6627 0.5467 0.5545 -0.0302 -0.0435 -0.0027 200 SER A CA 1568 C C . SER A 223 ? 0.6857 0.5877 0.5952 -0.0336 -0.0442 0.0048 200 SER A C 1569 O O . SER A 223 ? 0.6016 0.4990 0.5174 -0.0420 -0.0431 0.0058 200 SER A O 1570 C CB . SER A 223 ? 0.5364 0.4284 0.4238 -0.0358 -0.0499 -0.0094 200 SER A CB 1571 O OG . SER A 223 ? 0.7890 0.6876 0.6868 -0.0486 -0.0552 -0.0117 200 SER A OG 1572 N N . LEU A 224 ? 0.6122 0.5337 0.5297 -0.0275 -0.0448 0.0097 201 LEU A N 1573 C CA . LEU A 224 ? 0.6022 0.5400 0.5356 -0.0295 -0.0450 0.0160 201 LEU A CA 1574 C C . LEU A 224 ? 0.5612 0.4900 0.4953 -0.0272 -0.0402 0.0204 201 LEU A C 1575 O O . LEU A 224 ? 0.5701 0.5033 0.5132 -0.0330 -0.0390 0.0233 201 LEU A O 1576 C CB . LEU A 224 ? 0.5620 0.5185 0.5020 -0.0234 -0.0458 0.0197 201 LEU A CB 1577 C CG . LEU A 224 ? 0.6019 0.5695 0.5416 -0.0259 -0.0510 0.0181 201 LEU A CG 1578 C CD1 . LEU A 224 ? 0.4852 0.4666 0.4292 -0.0195 -0.0496 0.0230 201 LEU A CD1 1579 C CD2 . LEU A 224 ? 0.5317 0.5082 0.4830 -0.0351 -0.0559 0.0177 201 LEU A CD2 1580 N N . VAL A 225 ? 0.5300 0.4468 0.4542 -0.0180 -0.0374 0.0210 202 VAL A N 1581 C CA . VAL A 225 ? 0.5482 0.4546 0.4689 -0.0139 -0.0341 0.0256 202 VAL A CA 1582 C C . VAL A 225 ? 0.6424 0.5285 0.5565 -0.0223 -0.0311 0.0254 202 VAL A C 1583 O O . VAL A 225 ? 0.6625 0.5463 0.5782 -0.0252 -0.0282 0.0300 202 VAL A O 1584 C CB . VAL A 225 ? 0.5796 0.4776 0.4914 -0.0008 -0.0329 0.0259 202 VAL A CB 1585 C CG1 . VAL A 225 ? 0.4125 0.2942 0.3157 0.0041 -0.0308 0.0307 202 VAL A CG1 1586 C CG2 . VAL A 225 ? 0.5440 0.4643 0.4662 0.0063 -0.0344 0.0269 202 VAL A CG2 1587 N N . GLU A 226 ? 0.6306 0.5012 0.5366 -0.0269 -0.0311 0.0195 203 GLU A N 1588 C CA . GLU A 226 ? 0.5658 0.4162 0.4671 -0.0372 -0.0276 0.0181 203 GLU A CA 1589 C C . GLU A 226 ? 0.6716 0.5371 0.5887 -0.0500 -0.0277 0.0187 203 GLU A C 1590 O O . GLU A 226 ? 0.5896 0.4454 0.5071 -0.0563 -0.0220 0.0222 203 GLU A O 1591 C CB . GLU A 226 ? 0.6641 0.4971 0.5553 -0.0410 -0.0285 0.0095 203 GLU A CB 1592 C CG . GLU A 226 ? 0.8048 0.6190 0.6802 -0.0278 -0.0264 0.0086 203 GLU A CG 1593 C CD . GLU A 226 ? 0.8410 0.6426 0.7063 -0.0300 -0.0278 -0.0016 203 GLU A CD 1594 O OE1 . GLU A 226 ? 0.9621 0.7735 0.8326 -0.0411 -0.0323 -0.0079 203 GLU A OE1 1595 O OE2 . GLU A 226 ? 0.8503 0.6325 0.7021 -0.0199 -0.0247 -0.0037 203 GLU A OE2 1596 N N . LYS A 227 ? 0.5742 0.4635 0.5042 -0.0532 -0.0335 0.0157 204 LYS A N 1597 C CA . LYS A 227 ? 0.6501 0.5578 0.5983 -0.0632 -0.0344 0.0160 204 LYS A CA 1598 C C . LYS A 227 ? 0.6749 0.5926 0.6306 -0.0599 -0.0301 0.0234 204 LYS A C 1599 O O . LYS A 227 ? 0.6214 0.5439 0.5877 -0.0680 -0.0260 0.0248 204 LYS A O 1600 C CB . LYS A 227 ? 0.5820 0.5122 0.5403 -0.0643 -0.0427 0.0122 204 LYS A CB 1601 C CG . LYS A 227 ? 0.5866 0.5098 0.5374 -0.0695 -0.0482 0.0035 204 LYS A CG 1602 C CD . LYS A 227 ? 0.7066 0.6512 0.6622 -0.0676 -0.0570 0.0014 204 LYS A CD 1603 C CE . LYS A 227 ? 0.6947 0.6325 0.6399 -0.0727 -0.0635 -0.0082 204 LYS A CE 1604 N NZ . LYS A 227 ? 0.7708 0.7077 0.7267 -0.0874 -0.0656 -0.0146 204 LYS A NZ 1605 N N . ILE A 228 ? 0.6056 0.5270 0.5561 -0.0483 -0.0307 0.0272 205 ILE A N 1606 C CA . ILE A 228 ? 0.5575 0.4863 0.5120 -0.0445 -0.0273 0.0329 205 ILE A CA 1607 C C . ILE A 228 ? 0.6092 0.5173 0.5518 -0.0460 -0.0203 0.0367 205 ILE A C 1608 O O . ILE A 228 ? 0.5624 0.4736 0.5101 -0.0512 -0.0151 0.0394 205 ILE A O 1609 C CB . ILE A 228 ? 0.5054 0.4424 0.4576 -0.0327 -0.0301 0.0349 205 ILE A CB 1610 C CG1 . ILE A 228 ? 0.4868 0.4449 0.4518 -0.0323 -0.0346 0.0333 205 ILE A CG1 1611 C CG2 . ILE A 228 ? 0.4012 0.3399 0.3519 -0.0286 -0.0271 0.0394 205 ILE A CG2 1612 C CD1 . ILE A 228 ? 0.4447 0.4109 0.4095 -0.0227 -0.0362 0.0345 205 ILE A CD1 1613 N N . LEU A 229 ? 0.5870 0.4728 0.5126 -0.0408 -0.0194 0.0372 206 LEU A N 1614 C CA . LEU A 229 ? 0.6442 0.5058 0.5544 -0.0406 -0.0128 0.0422 206 LEU A CA 1615 C C . LEU A 229 ? 0.7009 0.5514 0.6141 -0.0552 -0.0060 0.0413 206 LEU A C 1616 O O . LEU A 229 ? 0.7768 0.6126 0.6810 -0.0580 0.0019 0.0468 206 LEU A O 1617 C CB . LEU A 229 ? 0.5269 0.3661 0.4191 -0.0303 -0.0138 0.0429 206 LEU A CB 1618 C CG . LEU A 229 ? 0.5680 0.4155 0.4561 -0.0148 -0.0186 0.0456 206 LEU A CG 1619 C CD1 . LEU A 229 ? 0.6974 0.5260 0.5722 -0.0041 -0.0198 0.0449 206 LEU A CD1 1620 C CD2 . LEU A 229 ? 0.6307 0.4772 0.5114 -0.0108 -0.0165 0.0524 206 LEU A CD2 1621 N N . SER A 230 ? 0.7317 0.5896 0.6572 -0.0649 -0.0089 0.0344 207 SER A N 1622 C CA . SER A 230 ? 0.7432 0.5952 0.6769 -0.0806 -0.0033 0.0317 207 SER A CA 1623 C C . SER A 230 ? 0.7451 0.6168 0.6955 -0.0871 0.0016 0.0344 207 SER A C 1624 O O . SER A 230 ? 0.7913 0.6590 0.7494 -0.0997 0.0092 0.0339 207 SER A O 1625 C CB . SER A 230 ? 0.6663 0.5259 0.6105 -0.0889 -0.0100 0.0222 207 SER A CB 1626 O OG . SER A 230 ? 0.8249 0.6621 0.7521 -0.0845 -0.0123 0.0185 207 SER A OG 1627 N N . GLU A 231 ? 0.5367 0.4296 0.4937 -0.0787 -0.0019 0.0367 208 GLU A N 1628 C CA . GLU A 231 ? 0.5107 0.4223 0.4831 -0.0828 0.0029 0.0386 208 GLU A CA 1629 C C . GLU A 231 ? 0.5267 0.4280 0.4836 -0.0762 0.0101 0.0456 208 GLU A C 1630 O O . GLU A 231 ? 0.6319 0.5472 0.5973 -0.0767 0.0144 0.0471 208 GLU A O 1631 C CB . GLU A 231 ? 0.4742 0.4149 0.4646 -0.0785 -0.0051 0.0359 208 GLU A CB 1632 C CG . GLU A 231 ? 0.5382 0.4911 0.5415 -0.0833 -0.0138 0.0295 208 GLU A CG 1633 C CD . GLU A 231 ? 0.6898 0.6518 0.7123 -0.0974 -0.0112 0.0253 208 GLU A CD 1634 O OE1 . GLU A 231 ? 0.6999 0.6656 0.7315 -0.1029 -0.0019 0.0276 208 GLU A OE1 1635 O OE2 . GLU A 231 ? 0.7064 0.6726 0.7352 -0.1033 -0.0184 0.0189 208 GLU A OE2 1636 N N . LYS A 232 ? 0.6045 0.4808 0.5375 -0.0693 0.0110 0.0497 209 LYS A N 1637 C CA . LYS A 232 ? 0.6554 0.5198 0.5694 -0.0622 0.0163 0.0567 209 LYS A CA 1638 C C . LYS A 232 ? 0.6924 0.5438 0.6020 -0.0726 0.0297 0.0606 209 LYS A C 1639 O O . LYS A 232 ? 0.6858 0.5177 0.5915 -0.0814 0.0355 0.0610 209 LYS A O 1640 C CB . LYS A 232 ? 0.6436 0.4858 0.5340 -0.0503 0.0123 0.0604 209 LYS A CB 1641 C CG . LYS A 232 ? 0.6929 0.5238 0.5613 -0.0409 0.0149 0.0676 209 LYS A CG 1642 C CD . LYS A 232 ? 0.6855 0.5011 0.5353 -0.0264 0.0079 0.0705 209 LYS A CD 1643 C CE . LYS A 232 ? 0.7690 0.5520 0.6035 -0.0279 0.0126 0.0736 209 LYS A CE 1644 N NZ . LYS A 232 ? 0.8562 0.6141 0.6709 -0.0323 0.0240 0.0818 209 LYS A NZ 1645 N N . LYS A 233 ? 0.7095 0.5708 0.6196 -0.0720 0.0355 0.0631 210 LYS A N 1646 C CA . LYS A 233 ? 0.7538 0.6039 0.6588 -0.0814 0.0503 0.0672 210 LYS A CA 1647 C C . LYS A 233 ? 0.8187 0.6363 0.6887 -0.0750 0.0558 0.0761 210 LYS A C 1648 O O . LYS A 233 ? 0.7669 0.5747 0.6194 -0.0620 0.0468 0.0785 210 LYS A O 1649 C CB . LYS A 233 ? 0.7643 0.6373 0.6825 -0.0827 0.0558 0.0657 210 LYS A CB 1650 C CG . LYS A 233 ? 0.8936 0.7917 0.8465 -0.0943 0.0584 0.0594 210 LYS A CG 1651 C CD . LYS A 233 ? 0.9069 0.8225 0.8790 -0.0928 0.0441 0.0531 210 LYS A CD 1652 C CE . LYS A 233 ? 0.9421 0.8822 0.9475 -0.1036 0.0450 0.0472 210 LYS A CE 1653 N NZ . LYS A 233 ? 0.9241 0.8796 0.9440 -0.1015 0.0305 0.0417 210 LYS A NZ 1654 N N . GLU A 234 ? 0.8355 0.6370 0.6960 -0.0837 0.0709 0.0813 211 GLU A N 1655 C CA . GLU A 234 ? 0.8624 0.6292 0.6868 -0.0784 0.0779 0.0914 211 GLU A CA 1656 C C . GLU A 234 ? 0.8458 0.6141 0.6473 -0.0632 0.0730 0.0954 211 GLU A C 1657 O O . GLU A 234 ? 0.8564 0.6012 0.6280 -0.0519 0.0696 0.1026 211 GLU A O 1658 C CB . GLU A 234 ? 0.9833 0.7340 0.8038 -0.0928 0.0974 0.0961 211 GLU A CB 1659 C CG . GLU A 234 ? 1.2558 0.9642 1.0385 -0.0896 0.1063 0.1077 211 GLU A CG 1660 C CD . GLU A 234 ? 1.4895 1.1811 1.2700 -0.1060 0.1277 0.1125 211 GLU A CD 1661 O OE1 . GLU A 234 ? 1.5512 1.2671 1.3550 -0.1165 0.1366 0.1080 211 GLU A OE1 1662 O OE2 . GLU A 234 ? 1.6015 1.2552 1.3579 -0.1082 0.1364 0.1209 211 GLU A OE2 1663 N N . ASN A 235 ? 0.8177 0.6137 0.6336 -0.0627 0.0719 0.0904 212 ASN A N 1664 C CA . ASN A 235 ? 0.8252 0.6250 0.6214 -0.0503 0.0671 0.0919 212 ASN A CA 1665 C C . ASN A 235 ? 0.8225 0.6368 0.6231 -0.0376 0.0489 0.0874 212 ASN A C 1666 O O . ASN A 235 ? 0.8410 0.6618 0.6291 -0.0278 0.0426 0.0868 212 ASN A O 1667 C CB . ASN A 235 ? 0.7522 0.5718 0.5596 -0.0555 0.0760 0.0879 212 ASN A CB 1668 C CG . ASN A 235 ? 0.7844 0.6356 0.6318 -0.0616 0.0720 0.0785 212 ASN A CG 1669 O OD1 . ASN A 235 ? 0.8157 0.6754 0.6803 -0.0611 0.0612 0.0749 212 ASN A OD1 1670 N ND2 . ASN A 235 ? 0.7359 0.6039 0.5971 -0.0664 0.0809 0.0749 212 ASN A ND2 1671 N N . GLY A 236 ? 0.7096 0.5294 0.5281 -0.0383 0.0407 0.0837 213 GLY A N 1672 C CA . GLY A 236 ? 0.7288 0.5611 0.5521 -0.0270 0.0254 0.0799 213 GLY A CA 1673 C C . GLY A 236 ? 0.7085 0.5716 0.5627 -0.0301 0.0196 0.0713 213 GLY A C 1674 O O . GLY A 236 ? 0.7398 0.6140 0.6028 -0.0235 0.0087 0.0678 213 GLY A O 1675 N N . LEU A 237 ? 0.6006 0.4771 0.4711 -0.0395 0.0275 0.0685 214 LEU A N 1676 C CA . LEU A 237 ? 0.5783 0.4817 0.4778 -0.0423 0.0229 0.0615 214 LEU A CA 1677 C C . LEU A 237 ? 0.6487 0.5554 0.5641 -0.0464 0.0176 0.0589 214 LEU A C 1678 O O . LEU A 237 ? 0.5815 0.4728 0.4933 -0.0529 0.0220 0.0608 214 LEU A O 1679 C CB . LEU A 237 ? 0.5993 0.5152 0.5136 -0.0506 0.0333 0.0595 214 LEU A CB 1680 C CG . LEU A 237 ? 0.6838 0.6001 0.5844 -0.0466 0.0388 0.0597 214 LEU A CG 1681 C CD1 . LEU A 237 ? 0.5315 0.4630 0.4519 -0.0540 0.0495 0.0564 214 LEU A CD1 1682 C CD2 . LEU A 237 ? 0.7277 0.6535 0.6254 -0.0363 0.0273 0.0561 214 LEU A CD2 1683 N N . ILE A 238 ? 0.5760 0.5012 0.5076 -0.0429 0.0085 0.0544 215 ILE A N 1684 C CA . ILE A 238 ? 0.5840 0.5132 0.5277 -0.0456 0.0027 0.0514 215 ILE A CA 1685 C C . ILE A 238 ? 0.5923 0.5446 0.5619 -0.0512 0.0016 0.0473 215 ILE A C 1686 O O . ILE A 238 ? 0.5244 0.4922 0.5033 -0.0462 -0.0030 0.0455 215 ILE A O 1687 C CB . ILE A 238 ? 0.5037 0.4329 0.4415 -0.0354 -0.0069 0.0506 215 ILE A CB 1688 C CG1 . ILE A 238 ? 0.5359 0.4457 0.4495 -0.0270 -0.0071 0.0550 215 ILE A CG1 1689 C CG2 . ILE A 238 ? 0.5181 0.4466 0.4625 -0.0381 -0.0113 0.0475 215 ILE A CG2 1690 C CD1 . ILE A 238 ? 0.6552 0.5698 0.5663 -0.0158 -0.0161 0.0537 215 ILE A CD1 1691 N N . GLY A 239 ? 0.5436 0.4978 0.5251 -0.0614 0.0057 0.0458 216 GLY A N 1692 C CA . GLY A 239 ? 0.4640 0.4409 0.4708 -0.0664 0.0057 0.0426 216 GLY A CA 1693 C C . GLY A 239 ? 0.4924 0.4736 0.5032 -0.0688 0.0164 0.0440 216 GLY A C 1694 O O . GLY A 239 ? 0.6252 0.5955 0.6308 -0.0760 0.0262 0.0458 216 GLY A O 1695 N N . ASN A 240 ? 0.4991 0.4945 0.5181 -0.0630 0.0156 0.0429 217 ASN A N 1696 C CA . ASN A 240 ? 0.4345 0.4315 0.4526 -0.0631 0.0261 0.0434 217 ASN A CA 1697 C C . ASN A 240 ? 0.4884 0.4798 0.4891 -0.0537 0.0238 0.0437 217 ASN A C 1698 O O . ASN A 240 ? 0.4762 0.4619 0.4661 -0.0478 0.0150 0.0442 217 ASN A O 1699 C CB . ASN A 240 ? 0.4456 0.4651 0.4920 -0.0658 0.0295 0.0403 217 ASN A CB 1700 C CG . ASN A 240 ? 0.5300 0.5645 0.5902 -0.0588 0.0196 0.0383 217 ASN A CG 1701 O OD1 . ASN A 240 ? 0.5488 0.5776 0.5971 -0.0521 0.0127 0.0387 217 ASN A OD1 1702 N ND2 . ASN A 240 ? 0.5106 0.5646 0.5968 -0.0603 0.0191 0.0363 217 ASN A ND2 1703 N N . THR A 241 ? 0.4854 0.4796 0.4847 -0.0525 0.0319 0.0425 218 THR A N 1704 C CA . THR A 241 ? 0.4502 0.4395 0.4329 -0.0449 0.0300 0.0412 218 THR A CA 1705 C C . THR A 241 ? 0.5153 0.5153 0.5086 -0.0391 0.0194 0.0380 218 THR A C 1706 O O . THR A 241 ? 0.5181 0.5133 0.4983 -0.0334 0.0129 0.0371 218 THR A O 1707 C CB . THR A 241 ? 0.4264 0.4183 0.4082 -0.0452 0.0414 0.0387 218 THR A CB 1708 O OG1 . THR A 241 ? 0.5277 0.5081 0.4970 -0.0509 0.0532 0.0423 218 THR A OG1 1709 C CG2 . THR A 241 ? 0.4430 0.4299 0.4068 -0.0380 0.0382 0.0355 218 THR A CG2 1710 N N . PHE A 242 ? 0.5073 0.5222 0.5249 -0.0405 0.0175 0.0367 219 PHE A N 1711 C CA . PHE A 242 ? 0.4599 0.4836 0.4879 -0.0354 0.0103 0.0345 219 PHE A CA 1712 C C . PHE A 242 ? 0.4657 0.4906 0.4961 -0.0344 0.0005 0.0364 219 PHE A C 1713 O O . PHE A 242 ? 0.4862 0.5173 0.5245 -0.0309 -0.0047 0.0357 219 PHE A O 1714 C CB . PHE A 242 ? 0.4622 0.4995 0.5128 -0.0352 0.0145 0.0326 219 PHE A CB 1715 C CG . PHE A 242 ? 0.4899 0.5264 0.5391 -0.0357 0.0258 0.0299 219 PHE A CG 1716 C CD1 . PHE A 242 ? 0.3919 0.4215 0.4278 -0.0318 0.0280 0.0260 219 PHE A CD1 1717 C CD2 . PHE A 242 ? 0.4308 0.4741 0.4920 -0.0405 0.0347 0.0304 219 PHE A CD2 1718 C CE1 . PHE A 242 ? 0.4051 0.4327 0.4366 -0.0320 0.0392 0.0228 219 PHE A CE1 1719 C CE2 . PHE A 242 ? 0.4978 0.5404 0.5571 -0.0408 0.0471 0.0277 219 PHE A CE2 1720 C CZ . PHE A 242 ? 0.4016 0.4355 0.4446 -0.0361 0.0496 0.0239 219 PHE A CZ 1721 N N . SER A 243 ? 0.4509 0.4683 0.4732 -0.0376 -0.0010 0.0387 220 SER A N 1722 C CA . SER A 243 ? 0.4610 0.4770 0.4815 -0.0361 -0.0093 0.0396 220 SER A CA 1723 C C . SER A 243 ? 0.4450 0.4472 0.4450 -0.0324 -0.0118 0.0407 220 SER A C 1724 O O . SER A 243 ? 0.4668 0.4671 0.4636 -0.0294 -0.0177 0.0409 220 SER A O 1725 C CB . SER A 243 ? 0.4066 0.4246 0.4351 -0.0422 -0.0103 0.0401 220 SER A CB 1726 O OG . SER A 243 ? 0.5243 0.5301 0.5431 -0.0477 -0.0046 0.0411 220 SER A OG 1727 N N . THR A 244 ? 0.4519 0.4447 0.4375 -0.0316 -0.0071 0.0415 221 THR A N 1728 C CA . THR A 244 ? 0.4441 0.4229 0.4089 -0.0268 -0.0098 0.0435 221 THR A CA 1729 C C . THR A 244 ? 0.5003 0.4849 0.4639 -0.0193 -0.0176 0.0413 221 THR A C 1730 O O . THR A 244 ? 0.5399 0.5194 0.4961 -0.0145 -0.0227 0.0423 221 THR A O 1731 C CB . THR A 244 ? 0.5007 0.4673 0.4474 -0.0270 -0.0030 0.0456 221 THR A CB 1732 O OG1 . THR A 244 ? 0.5345 0.4945 0.4828 -0.0350 0.0055 0.0480 221 THR A OG1 1733 C CG2 . THR A 244 ? 0.5201 0.4723 0.4442 -0.0198 -0.0074 0.0486 221 THR A CG2 1734 N N . GLY A 245 ? 0.4145 0.4099 0.3868 -0.0186 -0.0178 0.0378 222 GLY A N 1735 C CA . GLY A 245 ? 0.4181 0.4205 0.3919 -0.0135 -0.0242 0.0346 222 GLY A CA 1736 C C . GLY A 245 ? 0.4755 0.4839 0.4591 -0.0117 -0.0291 0.0349 222 GLY A C 1737 O O . GLY A 245 ? 0.5090 0.5180 0.4882 -0.0065 -0.0341 0.0343 222 GLY A O 1738 N N . GLU A 246 ? 0.3972 0.4107 0.3937 -0.0154 -0.0274 0.0358 223 GLU A N 1739 C CA . GLU A 246 ? 0.4934 0.5114 0.4963 -0.0139 -0.0308 0.0364 223 GLU A CA 1740 C C . GLU A 246 ? 0.5182 0.5267 0.5112 -0.0130 -0.0321 0.0383 223 GLU A C 1741 O O . GLU A 246 ? 0.4517 0.4613 0.4444 -0.0096 -0.0348 0.0381 223 GLU A O 1742 C CB . GLU A 246 ? 0.3649 0.3908 0.3821 -0.0170 -0.0295 0.0371 223 GLU A CB 1743 C CG . GLU A 246 ? 0.3749 0.4072 0.4019 -0.0172 -0.0276 0.0349 223 GLU A CG 1744 C CD . GLU A 246 ? 0.4805 0.5184 0.5203 -0.0181 -0.0266 0.0370 223 GLU A CD 1745 O OE1 . GLU A 246 ? 0.4655 0.5044 0.5080 -0.0194 -0.0272 0.0397 223 GLU A OE1 1746 O OE2 . GLU A 246 ? 0.4976 0.5383 0.5446 -0.0176 -0.0255 0.0358 223 GLU A OE2 1747 N N . ALA A 247 ? 0.4987 0.4968 0.4834 -0.0162 -0.0292 0.0400 224 ALA A N 1748 C CA . ALA A 247 ? 0.5665 0.5513 0.5398 -0.0156 -0.0298 0.0413 224 ALA A CA 1749 C C . ALA A 247 ? 0.5274 0.5053 0.4884 -0.0072 -0.0327 0.0418 224 ALA A C 1750 O O . ALA A 247 ? 0.4435 0.4157 0.3998 -0.0029 -0.0348 0.0417 224 ALA A O 1751 C CB . ALA A 247 ? 0.4709 0.4449 0.4390 -0.0221 -0.0246 0.0430 224 ALA A CB 1752 N N . MET A 248 ? 0.4697 0.4488 0.4254 -0.0041 -0.0332 0.0420 225 MET A N 1753 C CA . MET A 248 ? 0.4840 0.4605 0.4296 0.0050 -0.0380 0.0422 225 MET A CA 1754 C C . MET A 248 ? 0.5057 0.4961 0.4637 0.0098 -0.0426 0.0391 225 MET A C 1755 O O . MET A 248 ? 0.5342 0.5215 0.4877 0.0174 -0.0457 0.0394 225 MET A O 1756 C CB . MET A 248 ? 0.5501 0.5283 0.4880 0.0068 -0.0391 0.0416 225 MET A CB 1757 C CG . MET A 248 ? 0.4071 0.3694 0.3283 0.0036 -0.0332 0.0455 225 MET A CG 1758 S SD . MET A 248 ? 0.5252 0.4895 0.4342 0.0057 -0.0337 0.0437 225 MET A SD 1759 C CE . MET A 248 ? 0.4218 0.3860 0.3181 0.0185 -0.0448 0.0440 225 MET A CE 1760 N N . GLN A 249 ? 0.4513 0.4564 0.4253 0.0056 -0.0420 0.0363 226 GLN A N 1761 C CA . GLN A 249 ? 0.4684 0.4866 0.4554 0.0082 -0.0438 0.0338 226 GLN A CA 1762 C C . GLN A 249 ? 0.4750 0.4877 0.4596 0.0104 -0.0427 0.0349 226 GLN A C 1763 O O . GLN A 249 ? 0.5014 0.5179 0.4877 0.0170 -0.0443 0.0336 226 GLN A O 1764 C CB . GLN A 249 ? 0.4046 0.4340 0.4068 0.0020 -0.0413 0.0322 226 GLN A CB 1765 C CG . GLN A 249 ? 0.4718 0.5079 0.4789 0.0001 -0.0422 0.0290 226 GLN A CG 1766 C CD . GLN A 249 ? 0.4965 0.5415 0.5194 -0.0048 -0.0392 0.0275 226 GLN A CD 1767 O OE1 . GLN A 249 ? 0.3743 0.4252 0.4059 -0.0048 -0.0380 0.0280 226 GLN A OE1 1768 N NE2 . GLN A 249 ? 0.3889 0.4332 0.4144 -0.0087 -0.0371 0.0259 226 GLN A NE2 1769 N N . ALA A 250 ? 0.4379 0.4423 0.4190 0.0048 -0.0398 0.0366 227 ALA A N 1770 C CA . ALA A 250 ? 0.4903 0.4875 0.4666 0.0056 -0.0390 0.0364 227 ALA A CA 1771 C C . ALA A 250 ? 0.5676 0.5508 0.5308 0.0127 -0.0399 0.0366 227 ALA A C 1772 O O . ALA A 250 ? 0.5119 0.4937 0.4736 0.0182 -0.0397 0.0349 227 ALA A O 1773 C CB . ALA A 250 ? 0.4852 0.4768 0.4601 -0.0024 -0.0375 0.0371 227 ALA A CB 1774 N N . LEU A 251 ? 0.4995 0.4711 0.4522 0.0134 -0.0402 0.0390 228 LEU A N 1775 C CA . LEU A 251 ? 0.4775 0.4323 0.4157 0.0212 -0.0410 0.0407 228 LEU A CA 1776 C C . LEU A 251 ? 0.6127 0.5772 0.5538 0.0327 -0.0456 0.0401 228 LEU A C 1777 O O . LEU A 251 ? 0.5633 0.5189 0.4977 0.0420 -0.0466 0.0404 228 LEU A O 1778 C CB . LEU A 251 ? 0.4747 0.4120 0.3985 0.0181 -0.0388 0.0449 228 LEU A CB 1779 C CG . LEU A 251 ? 0.6177 0.5446 0.5400 0.0066 -0.0338 0.0451 228 LEU A CG 1780 C CD1 . LEU A 251 ? 0.6743 0.5840 0.5826 0.0036 -0.0296 0.0497 228 LEU A CD1 1781 C CD2 . LEU A 251 ? 0.6005 0.5160 0.5195 0.0056 -0.0329 0.0425 228 LEU A CD2 1782 N N . PHE A 252 ? 0.5222 0.5053 0.4746 0.0321 -0.0485 0.0385 229 PHE A N 1783 C CA . PHE A 252 ? 0.5355 0.5334 0.4957 0.0414 -0.0539 0.0363 229 PHE A CA 1784 C C . PHE A 252 ? 0.5304 0.5371 0.5017 0.0465 -0.0524 0.0334 229 PHE A C 1785 O O . PHE A 252 ? 0.5090 0.5191 0.4817 0.0575 -0.0556 0.0327 229 PHE A O 1786 C CB . PHE A 252 ? 0.4894 0.5067 0.4631 0.0366 -0.0563 0.0331 229 PHE A CB 1787 C CG . PHE A 252 ? 0.4242 0.4365 0.3861 0.0360 -0.0594 0.0343 229 PHE A CG 1788 C CD1 . PHE A 252 ? 0.3990 0.3906 0.3393 0.0396 -0.0592 0.0393 229 PHE A CD1 1789 C CD2 . PHE A 252 ? 0.4042 0.4307 0.3752 0.0317 -0.0617 0.0303 229 PHE A CD2 1790 C CE1 . PHE A 252 ? 0.4855 0.4715 0.4120 0.0392 -0.0609 0.0409 229 PHE A CE1 1791 C CE2 . PHE A 252 ? 0.4934 0.5146 0.4509 0.0314 -0.0641 0.0305 229 PHE A CE2 1792 C CZ . PHE A 252 ? 0.4665 0.4678 0.4010 0.0354 -0.0635 0.0361 229 PHE A CZ 1793 N N . VAL A 253 ? 0.4936 0.5042 0.4723 0.0392 -0.0473 0.0320 230 VAL A N 1794 C CA . VAL A 253 ? 0.5035 0.5237 0.4920 0.0428 -0.0440 0.0292 230 VAL A CA 1795 C C . VAL A 253 ? 0.5883 0.5908 0.5639 0.0455 -0.0403 0.0291 230 VAL A C 1796 O O . VAL A 253 ? 0.4539 0.4615 0.4339 0.0488 -0.0363 0.0264 230 VAL A O 1797 C CB . VAL A 253 ? 0.4793 0.5137 0.4814 0.0341 -0.0401 0.0280 230 VAL A CB 1798 C CG1 . VAL A 253 ? 0.4456 0.4948 0.4604 0.0302 -0.0431 0.0270 230 VAL A CG1 1799 C CG2 . VAL A 253 ? 0.3979 0.4206 0.3910 0.0255 -0.0374 0.0301 230 VAL A CG2 1800 N N . SER A 254 ? 0.5017 0.4827 0.4610 0.0437 -0.0409 0.0314 231 SER A N 1801 C CA . SER A 254 ? 0.6074 0.5691 0.5537 0.0441 -0.0375 0.0300 231 SER A CA 1802 C C . SER A 254 ? 0.6391 0.5777 0.5698 0.0517 -0.0385 0.0321 231 SER A C 1803 O O . SER A 254 ? 0.6405 0.5573 0.5578 0.0468 -0.0363 0.0324 231 SER A O 1804 C CB . SER A 254 ? 0.5938 0.5495 0.5361 0.0315 -0.0359 0.0298 231 SER A CB 1805 O OG . SER A 254 ? 0.7610 0.7117 0.7008 0.0248 -0.0374 0.0331 231 SER A OG 1806 N N . SER A 255 ? 0.5890 0.5325 0.5221 0.0637 -0.0419 0.0335 232 SER A N 1807 C CA . SER A 255 ? 0.6875 0.6087 0.6050 0.0738 -0.0433 0.0368 232 SER A CA 1808 C C . SER A 255 ? 0.7940 0.6957 0.7024 0.0797 -0.0387 0.0339 232 SER A C 1809 O O . SER A 255 ? 0.8699 0.7465 0.7629 0.0870 -0.0382 0.0366 232 SER A O 1810 C CB . SER A 255 ? 0.6466 0.5821 0.5708 0.0872 -0.0499 0.0386 232 SER A CB 1811 O OG . SER A 255 ? 0.9072 0.8611 0.8396 0.0814 -0.0544 0.0394 232 SER A OG 1812 N N . ASP A 256 ? 0.6452 0.5570 0.5616 0.0769 -0.0347 0.0282 233 ASP A N 1813 C CA . ASP A 256 ? 0.7545 0.6492 0.6617 0.0820 -0.0296 0.0236 233 ASP A CA 1814 C C . ASP A 256 ? 0.8883 0.7531 0.7771 0.0726 -0.0272 0.0229 233 ASP A C 1815 O O . ASP A 256 ? 0.9311 0.7727 0.8074 0.0774 -0.0235 0.0194 233 ASP A O 1816 C CB . ASP A 256 ? 0.8166 0.7295 0.7337 0.0793 -0.0253 0.0179 233 ASP A CB 1817 C CG . ASP A 256 ? 0.7303 0.6694 0.6663 0.0899 -0.0247 0.0168 233 ASP A CG 1818 O OD1 . ASP A 256 ? 0.8343 0.7804 0.7773 0.0995 -0.0296 0.0199 233 ASP A OD1 1819 O OD2 . ASP A 256 ? 0.7225 0.6757 0.6661 0.0885 -0.0194 0.0129 233 ASP A OD2 1820 N N . TYR A 257 ? 0.8089 0.6746 0.6975 0.0589 -0.0288 0.0254 234 TYR A N 1821 C CA . TYR A 257 ? 0.8231 0.6678 0.7002 0.0466 -0.0266 0.0230 234 TYR A CA 1822 C C . TYR A 257 ? 0.7787 0.6034 0.6461 0.0416 -0.0262 0.0287 234 TYR A C 1823 O O . TYR A 257 ? 0.9220 0.7346 0.7850 0.0284 -0.0243 0.0272 234 TYR A O 1824 C CB . TYR A 257 ? 0.8426 0.7056 0.7287 0.0336 -0.0277 0.0200 234 TYR A CB 1825 C CG . TYR A 257 ? 0.7376 0.6209 0.6320 0.0381 -0.0269 0.0162 234 TYR A CG 1826 C CD1 . TYR A 257 ? 0.6785 0.5528 0.5638 0.0402 -0.0237 0.0095 234 TYR A CD1 1827 C CD2 . TYR A 257 ? 0.8357 0.7458 0.7459 0.0397 -0.0284 0.0192 234 TYR A CD2 1828 C CE1 . TYR A 257 ? 0.6406 0.5324 0.5313 0.0442 -0.0212 0.0067 234 TYR A CE1 1829 C CE2 . TYR A 257 ? 0.7861 0.7132 0.7037 0.0427 -0.0259 0.0165 234 TYR A CE2 1830 C CZ . TYR A 257 ? 0.7557 0.6738 0.6630 0.0452 -0.0218 0.0108 234 TYR A CZ 1831 O OH . TYR A 257 ? 0.8173 0.7513 0.7299 0.0481 -0.0176 0.0087 234 TYR A OH 1832 N N . TYR A 258 ? 0.8395 0.6613 0.7036 0.0518 -0.0280 0.0353 235 TYR A N 1833 C CA . TYR A 258 ? 0.8640 0.6632 0.7145 0.0488 -0.0262 0.0419 235 TYR A CA 1834 C C . TYR A 258 ? 0.9066 0.6946 0.7466 0.0656 -0.0284 0.0485 235 TYR A C 1835 O O . TYR A 258 ? 0.8538 0.6618 0.7029 0.0780 -0.0334 0.0484 235 TYR A O 1836 C CB . TYR A 258 ? 0.7717 0.5859 0.6294 0.0363 -0.0267 0.0449 235 TYR A CB 1837 C CG . TYR A 258 ? 0.7332 0.5746 0.6016 0.0422 -0.0320 0.0475 235 TYR A CG 1838 C CD1 . TYR A 258 ? 0.6516 0.5222 0.5384 0.0396 -0.0346 0.0431 235 TYR A CD1 1839 C CD2 . TYR A 258 ? 0.6650 0.5014 0.5236 0.0497 -0.0342 0.0542 235 TYR A CD2 1840 C CE1 . TYR A 258 ? 0.5540 0.4478 0.4512 0.0435 -0.0390 0.0444 235 TYR A CE1 1841 C CE2 . TYR A 258 ? 0.6383 0.4994 0.5062 0.0541 -0.0398 0.0550 235 TYR A CE2 1842 C CZ . TYR A 258 ? 0.6827 0.5723 0.5710 0.0504 -0.0420 0.0496 235 TYR A CZ 1843 O OH . TYR A 258 ? 0.6727 0.5852 0.5709 0.0535 -0.0472 0.0493 235 TYR A OH 1844 N N . ASN A 259 ? 0.9047 0.6604 0.7255 0.0658 -0.0247 0.0544 236 ASN A N 1845 C CA . ASN A 259 ? 0.9824 0.7227 0.7887 0.0825 -0.0271 0.0623 236 ASN A CA 1846 C C . ASN A 259 ? 0.8789 0.6279 0.6804 0.0813 -0.0302 0.0699 236 ASN A C 1847 O O . ASN A 259 ? 0.7927 0.5561 0.6020 0.0669 -0.0286 0.0687 236 ASN A O 1848 C CB . ASN A 259 ? 1.1432 0.8390 0.9277 0.0843 -0.0204 0.0658 236 ASN A CB 1849 C CG . ASN A 259 ? 1.3276 1.0107 1.1145 0.0798 -0.0157 0.0563 236 ASN A CG 1850 O OD1 . ASN A 259 ? 1.3977 1.0803 1.1866 0.0935 -0.0169 0.0523 236 ASN A OD1 1851 N ND2 . ASN A 259 ? 1.3115 0.9852 1.0984 0.0606 -0.0105 0.0520 236 ASN A ND2 1852 N N . GLU A 260 ? 0.9859 0.7256 0.7735 0.0972 -0.0346 0.0775 237 GLU A N 1853 C CA . GLU A 260 ? 1.0010 0.7465 0.7790 0.0978 -0.0381 0.0845 237 GLU A CA 1854 C C . GLU A 260 ? 1.0625 0.7825 0.8235 0.0834 -0.0286 0.0902 237 GLU A C 1855 O O . GLU A 260 ? 1.1158 0.8457 0.8739 0.0767 -0.0283 0.0930 237 GLU A O 1856 C CB . GLU A 260 ? 1.2124 0.9509 0.9758 0.1194 -0.0460 0.0918 237 GLU A CB 1857 C CG . GLU A 260 ? 1.4296 1.1239 1.1675 0.1289 -0.0410 0.0999 237 GLU A CG 1858 C CD . GLU A 260 ? 1.5522 1.2348 1.2674 0.1472 -0.0482 0.1108 237 GLU A CD 1859 O OE1 . GLU A 260 ? 1.5825 1.2292 1.2764 0.1591 -0.0455 0.1185 237 GLU A OE1 1860 O OE2 . GLU A 260 ? 1.6009 1.3092 1.3183 0.1499 -0.0567 0.1115 237 GLU A OE2 1861 N N . ASN A 261 ? 0.9606 0.6474 0.7108 0.0782 -0.0200 0.0913 238 ASN A N 1862 C CA . ASN A 261 ? 1.0415 0.7021 0.7770 0.0638 -0.0093 0.0967 238 ASN A CA 1863 C C . ASN A 261 ? 1.0372 0.7108 0.7919 0.0419 -0.0035 0.0886 238 ASN A C 1864 O O . ASN A 261 ? 1.0895 0.7445 0.8379 0.0275 0.0063 0.0910 238 ASN A O 1865 C CB . ASN A 261 ? 1.1986 0.8123 0.9104 0.0690 -0.0024 0.1032 238 ASN A CB 1866 C CG . ASN A 261 ? 1.2560 0.8606 0.9754 0.0737 -0.0029 0.0954 238 ASN A CG 1867 O OD1 . ASN A 261 ? 1.3766 1.0023 1.1170 0.0644 -0.0039 0.0845 238 ASN A OD1 1868 N ND2 . ASN A 261 ? 1.2469 0.8188 0.9474 0.0892 -0.0020 0.1010 238 ASN A ND2 1869 N N . ASP A 262 ? 0.9680 0.6739 0.7464 0.0396 -0.0094 0.0793 239 ASP A N 1870 C CA . ASP A 262 ? 0.7760 0.4994 0.5735 0.0213 -0.0064 0.0720 239 ASP A CA 1871 C C . ASP A 262 ? 0.7950 0.5458 0.6023 0.0162 -0.0079 0.0733 239 ASP A C 1872 O O . ASP A 262 ? 0.8163 0.5779 0.6360 0.0013 -0.0038 0.0703 239 ASP A O 1873 C CB . ASP A 262 ? 0.8759 0.6172 0.6907 0.0216 -0.0113 0.0621 239 ASP A CB 1874 C CG . ASP A 262 ? 0.9445 0.6578 0.7500 0.0238 -0.0084 0.0584 239 ASP A CG 1875 O OD1 . ASP A 262 ? 1.0578 0.7387 0.8489 0.0176 -0.0011 0.0615 239 ASP A OD1 1876 O OD2 . ASP A 262 ? 0.8350 0.5576 0.6472 0.0314 -0.0124 0.0521 239 ASP A OD2 1877 N N . TRP A 263 ? 0.6831 0.4452 0.4851 0.0292 -0.0143 0.0772 240 TRP A N 1878 C CA . TRP A 263 ? 0.7312 0.5183 0.5411 0.0258 -0.0163 0.0771 240 TRP A CA 1879 C C . TRP A 263 ? 0.7794 0.5656 0.5724 0.0394 -0.0216 0.0833 240 TRP A C 1880 O O . TRP A 263 ? 0.8221 0.6120 0.6132 0.0543 -0.0299 0.0835 240 TRP A O 1881 C CB . TRP A 263 ? 0.5617 0.3827 0.3975 0.0239 -0.0224 0.0687 240 TRP A CB 1882 C CG . TRP A 263 ? 0.6964 0.5412 0.5414 0.0202 -0.0240 0.0676 240 TRP A CG 1883 C CD1 . TRP A 263 ? 0.6960 0.5391 0.5373 0.0110 -0.0174 0.0700 240 TRP A CD1 1884 C CD2 . TRP A 263 ? 0.6628 0.5354 0.5224 0.0256 -0.0317 0.0632 240 TRP A CD2 1885 N NE1 . TRP A 263 ? 0.6563 0.5234 0.5079 0.0110 -0.0209 0.0669 240 TRP A NE1 1886 C CE2 . TRP A 263 ? 0.6140 0.4987 0.4768 0.0193 -0.0299 0.0627 240 TRP A CE2 1887 C CE3 . TRP A 263 ? 0.5706 0.4587 0.4415 0.0345 -0.0389 0.0593 240 TRP A CE3 1888 C CZ2 . TRP A 263 ? 0.6285 0.5380 0.5048 0.0213 -0.0355 0.0582 240 TRP A CZ2 1889 C CZ3 . TRP A 263 ? 0.5832 0.4977 0.4690 0.0356 -0.0441 0.0552 240 TRP A CZ3 1890 C CH2 . TRP A 263 ? 0.5951 0.5189 0.4830 0.0288 -0.0427 0.0545 240 TRP A CH2 1891 N N . ASN A 264 ? 0.8974 0.6797 0.6784 0.0346 -0.0169 0.0878 241 ASN A N 1892 C CA . ASN A 264 ? 0.8268 0.6116 0.5908 0.0461 -0.0230 0.0924 241 ASN A CA 1893 C C . ASN A 264 ? 0.8001 0.6182 0.5816 0.0422 -0.0276 0.0855 241 ASN A C 1894 O O . ASN A 264 ? 0.8504 0.6726 0.6333 0.0313 -0.0205 0.0848 241 ASN A O 1895 C CB . ASN A 264 ? 0.8238 0.5798 0.5582 0.0440 -0.0137 0.1021 241 ASN A CB 1896 C CG . ASN A 264 ? 0.9147 0.6679 0.6243 0.0584 -0.0211 0.1080 241 ASN A CG 1897 O OD1 . ASN A 264 ? 1.0113 0.7905 0.7299 0.0661 -0.0328 0.1028 241 ASN A OD1 1898 N ND2 . ASN A 264 ? 1.0119 0.7328 0.6891 0.0616 -0.0144 0.1188 241 ASN A ND2 1899 N N . CYS A 265 ? 0.7676 0.6089 0.5634 0.0510 -0.0387 0.0801 242 CYS A N 1900 C CA . CYS A 265 ? 0.6692 0.5408 0.4837 0.0469 -0.0430 0.0727 242 CYS A CA 1901 C C . CYS A 265 ? 0.6583 0.5304 0.4557 0.0476 -0.0436 0.0743 242 CYS A C 1902 O O . CYS A 265 ? 0.5963 0.4828 0.4036 0.0390 -0.0407 0.0694 242 CYS A O 1903 C CB . CYS A 265 ? 0.7121 0.6066 0.5443 0.0562 -0.0540 0.0670 242 CYS A CB 1904 S SG . CYS A 265 ? 0.7504 0.6795 0.6069 0.0502 -0.0587 0.0575 242 CYS A SG 1905 N N . GLN A 266 ? 0.7091 0.5640 0.4789 0.0589 -0.0473 0.0812 243 GLN A N 1906 C CA . GLN A 266 ? 0.7356 0.5892 0.4836 0.0613 -0.0489 0.0828 243 GLN A CA 1907 C C . GLN A 266 ? 0.7496 0.5896 0.4871 0.0484 -0.0340 0.0856 243 GLN A C 1908 O O . GLN A 266 ? 0.8090 0.6594 0.5442 0.0440 -0.0323 0.0815 243 GLN A O 1909 C CB . GLN A 266 ? 0.7161 0.5521 0.4336 0.0776 -0.0566 0.0910 243 GLN A CB 1910 C CG . GLN A 266 ? 0.7412 0.5813 0.4360 0.0829 -0.0629 0.0907 243 GLN A CG 1911 C CD . GLN A 266 ? 0.9494 0.8245 0.6664 0.0837 -0.0753 0.0787 243 GLN A CD 1912 O OE1 . GLN A 266 ? 0.9816 0.8669 0.6966 0.0772 -0.0742 0.0728 243 GLN A OE1 1913 N NE2 . GLN A 266 ? 0.9489 0.8420 0.6879 0.0915 -0.0861 0.0747 243 GLN A NE2 1914 N N . GLN A 267 ? 0.8330 0.6501 0.5654 0.0422 -0.0228 0.0919 244 GLN A N 1915 C CA . GLN A 267 ? 0.8110 0.6172 0.5381 0.0288 -0.0073 0.0943 244 GLN A CA 1916 C C . GLN A 267 ? 0.7458 0.5783 0.5041 0.0169 -0.0041 0.0849 244 GLN A C 1917 O O . GLN A 267 ? 0.6951 0.5329 0.4513 0.0107 0.0032 0.0829 244 GLN A O 1918 C CB . GLN A 267 ? 0.8150 0.5938 0.5363 0.0226 0.0035 0.1012 244 GLN A CB 1919 C CG . GLN A 267 ? 0.8437 0.6122 0.5617 0.0080 0.0207 0.1039 244 GLN A CG 1920 C CD . GLN A 267 ? 0.9112 0.6658 0.6417 -0.0037 0.0302 0.1050 244 GLN A CD 1921 O OE1 . GLN A 267 ? 0.9195 0.6758 0.6644 -0.0022 0.0237 0.1018 244 GLN A OE1 1922 N NE2 . GLN A 267 ? 0.8668 0.6079 0.5920 -0.0161 0.0462 0.1089 244 GLN A NE2 1923 N N . THR A 268 ? 0.6271 0.4751 0.4132 0.0147 -0.0092 0.0793 245 THR A N 1924 C CA . THR A 268 ? 0.6553 0.5279 0.4709 0.0057 -0.0080 0.0712 245 THR A CA 1925 C C . THR A 268 ? 0.7338 0.6249 0.5513 0.0088 -0.0133 0.0654 245 THR A C 1926 O O . THR A 268 ? 0.7211 0.6213 0.5473 0.0014 -0.0066 0.0617 245 THR A O 1927 C CB . THR A 268 ? 0.5939 0.4789 0.4334 0.0058 -0.0146 0.0669 245 THR A CB 1928 O OG1 . THR A 268 ? 0.5872 0.4554 0.4264 0.0006 -0.0091 0.0702 245 THR A OG1 1929 C CG2 . THR A 268 ? 0.4794 0.3888 0.3461 -0.0014 -0.0146 0.0598 245 THR A CG2 1930 N N . LEU A 269 ? 0.7077 0.6043 0.5179 0.0199 -0.0253 0.0641 246 LEU A N 1931 C CA . LEU A 269 ? 0.7399 0.6530 0.5506 0.0228 -0.0319 0.0574 246 LEU A CA 1932 C C . LEU A 269 ? 0.7198 0.6225 0.5062 0.0211 -0.0248 0.0587 246 LEU A C 1933 O O . LEU A 269 ? 0.7991 0.7134 0.5930 0.0160 -0.0218 0.0520 246 LEU A O 1934 C CB . LEU A 269 ? 0.7978 0.7180 0.6037 0.0353 -0.0467 0.0561 246 LEU A CB 1935 C CG . LEU A 269 ? 0.7445 0.6810 0.5482 0.0388 -0.0560 0.0483 246 LEU A CG 1936 C CD1 . LEU A 269 ? 0.6637 0.6216 0.4970 0.0301 -0.0550 0.0388 246 LEU A CD1 1937 C CD2 . LEU A 269 ? 0.8490 0.7931 0.6490 0.0518 -0.0710 0.0479 246 LEU A CD2 1938 N N . ASN A 270 ? 0.7045 0.5836 0.4605 0.0256 -0.0211 0.0676 247 ASN A N 1939 C CA . ASN A 270 ? 0.7695 0.6353 0.4969 0.0247 -0.0129 0.0703 247 ASN A CA 1940 C C . ASN A 270 ? 0.7692 0.6362 0.5081 0.0117 0.0036 0.0685 247 ASN A C 1941 O O . ASN A 270 ? 0.8677 0.7390 0.5993 0.0094 0.0087 0.0638 247 ASN A O 1942 C CB . ASN A 270 ? 0.8077 0.6442 0.4992 0.0319 -0.0104 0.0823 247 ASN A CB 1943 C CG . ASN A 270 ? 0.8974 0.7335 0.5723 0.0476 -0.0274 0.0841 247 ASN A CG 1944 O OD1 . ASN A 270 ? 0.9479 0.8060 0.6322 0.0524 -0.0404 0.0755 247 ASN A OD1 1945 N ND2 . ASN A 270 ? 0.9263 0.7373 0.5773 0.0558 -0.0274 0.0952 247 ASN A ND2 1946 N N . THR A 271 ? 0.6968 0.5605 0.4541 0.0035 0.0116 0.0715 248 THR A N 1947 C CA . THR A 271 ? 0.7021 0.5708 0.4763 -0.0087 0.0261 0.0695 248 THR A CA 1948 C C . THR A 271 ? 0.7246 0.6188 0.5254 -0.0114 0.0233 0.0592 248 THR A C 1949 O O . THR A 271 ? 0.6305 0.5296 0.4341 -0.0162 0.0335 0.0557 248 THR A O 1950 C CB . THR A 271 ? 0.6850 0.5487 0.4773 -0.0170 0.0318 0.0731 248 THR A CB 1951 O OG1 . THR A 271 ? 0.8042 0.6399 0.5705 -0.0156 0.0369 0.0828 248 THR A OG1 1952 C CG2 . THR A 271 ? 0.6593 0.5334 0.4740 -0.0292 0.0451 0.0701 248 THR A CG2 1953 N N . VAL A 272 ? 0.6555 0.5649 0.4754 -0.0078 0.0106 0.0545 249 VAL A N 1954 C CA . VAL A 272 ? 0.6671 0.5976 0.5107 -0.0098 0.0076 0.0455 249 VAL A CA 1955 C C . VAL A 272 ? 0.6682 0.6005 0.4957 -0.0061 0.0065 0.0397 249 VAL A C 1956 O O . VAL A 272 ? 0.6562 0.5964 0.4939 -0.0102 0.0134 0.0338 249 VAL A O 1957 C CB . VAL A 272 ? 0.6234 0.5676 0.4874 -0.0066 -0.0049 0.0425 249 VAL A CB 1958 C CG1 . VAL A 272 ? 0.5747 0.5369 0.4590 -0.0082 -0.0077 0.0339 249 VAL A CG1 1959 C CG2 . VAL A 272 ? 0.5530 0.4966 0.4335 -0.0111 -0.0031 0.0464 249 VAL A CG2 1960 N N . LEU A 273 ? 0.5776 0.5022 0.3793 0.0021 -0.0024 0.0409 250 LEU A N 1961 C CA . LEU A 273 ? 0.6763 0.6018 0.4585 0.0058 -0.0053 0.0344 250 LEU A CA 1962 C C . LEU A 273 ? 0.6542 0.5681 0.4182 0.0017 0.0105 0.0354 250 LEU A C 1963 O O . LEU A 273 ? 0.6970 0.6156 0.4577 0.0006 0.0135 0.0271 250 LEU A O 1964 C CB . LEU A 273 ? 0.7251 0.6442 0.4806 0.0164 -0.0187 0.0369 250 LEU A CB 1965 C CG . LEU A 273 ? 0.8096 0.7442 0.5832 0.0218 -0.0350 0.0335 250 LEU A CG 1966 C CD1 . LEU A 273 ? 0.8539 0.7822 0.6009 0.0338 -0.0478 0.0372 250 LEU A CD1 1967 C CD2 . LEU A 273 ? 0.7023 0.6574 0.4989 0.0181 -0.0404 0.0211 250 LEU A CD2 1968 N N . THR A 274 ? 0.7427 0.6405 0.4953 -0.0011 0.0216 0.0452 251 THR A N 1969 C CA . THR A 274 ? 0.7698 0.6572 0.5080 -0.0062 0.0394 0.0471 251 THR A CA 1970 C C . THR A 274 ? 0.6869 0.5905 0.4577 -0.0141 0.0493 0.0401 251 THR A C 1971 O O . THR A 274 ? 0.8227 0.7268 0.5868 -0.0156 0.0595 0.0349 251 THR A O 1972 C CB . THR A 274 ? 0.7618 0.6293 0.4868 -0.0097 0.0504 0.0591 251 THR A CB 1973 O OG1 . THR A 274 ? 0.8294 0.6788 0.5216 -0.0005 0.0416 0.0667 251 THR A OG1 1974 C CG2 . THR A 274 ? 0.7440 0.6021 0.4561 -0.0160 0.0710 0.0610 251 THR A CG2 1975 N N . GLU A 275 ? 0.6272 0.5437 0.4322 -0.0181 0.0459 0.0400 252 GLU A N 1976 C CA . GLU A 275 ? 0.6285 0.5616 0.4666 -0.0239 0.0529 0.0344 252 GLU A CA 1977 C C . GLU A 275 ? 0.6495 0.5929 0.4929 -0.0206 0.0486 0.0238 252 GLU A C 1978 O O . GLU A 275 ? 0.7431 0.6920 0.5965 -0.0229 0.0592 0.0186 252 GLU A O 1979 C CB . GLU A 275 ? 0.6711 0.6154 0.5404 -0.0271 0.0466 0.0364 252 GLU A CB 1980 C CG . GLU A 275 ? 0.7691 0.7036 0.6375 -0.0321 0.0512 0.0449 252 GLU A CG 1981 C CD . GLU A 275 ? 0.9806 0.9176 0.8623 -0.0409 0.0676 0.0462 252 GLU A CD 1982 O OE1 . GLU A 275 ? 1.0924 1.0216 0.9570 -0.0420 0.0804 0.0466 252 GLU A OE1 1983 O OE2 . GLU A 275 ? 0.9870 0.9351 0.8965 -0.0466 0.0677 0.0464 252 GLU A OE2 1984 N N . ILE A 276 ? 0.6811 0.6273 0.5193 -0.0153 0.0333 0.0202 253 ILE A N 1985 C CA . ILE A 276 ? 0.6443 0.5986 0.4874 -0.0133 0.0281 0.0093 253 ILE A CA 1986 C C . ILE A 276 ? 0.6701 0.6155 0.4873 -0.0121 0.0367 0.0035 253 ILE A C 1987 O O . ILE A 276 ? 0.7266 0.6767 0.5542 -0.0135 0.0431 -0.0050 253 ILE A O 1988 C CB . ILE A 276 ? 0.6686 0.6275 0.5082 -0.0086 0.0103 0.0063 253 ILE A CB 1989 C CG1 . ILE A 276 ? 0.6009 0.5690 0.4662 -0.0095 0.0031 0.0109 253 ILE A CG1 1990 C CG2 . ILE A 276 ? 0.6076 0.5735 0.4517 -0.0084 0.0056 -0.0061 253 ILE A CG2 1991 C CD1 . ILE A 276 ? 0.5943 0.5689 0.4594 -0.0048 -0.0127 0.0085 253 ILE A CD1 1992 N N . SER A 277 ? 0.6089 0.5399 0.3908 -0.0089 0.0374 0.0084 254 SER A N 1993 C CA . SER A 277 ? 0.7507 0.6710 0.5011 -0.0070 0.0454 0.0035 254 SER A CA 1994 C C . SER A 277 ? 0.7851 0.7038 0.5432 -0.0121 0.0666 0.0035 254 SER A C 1995 O O . SER A 277 ? 0.8237 0.7385 0.5674 -0.0114 0.0757 -0.0042 254 SER A O 1996 C CB . SER A 277 ? 0.7818 0.6850 0.4903 -0.0016 0.0419 0.0112 254 SER A CB 1997 O OG . SER A 277 ? 0.9586 0.8514 0.6648 -0.0044 0.0517 0.0241 254 SER A OG 1998 N N . GLN A 278 ? 0.7122 0.6352 0.4940 -0.0172 0.0744 0.0114 255 GLN A N 1999 C CA . GLN A 278 ? 0.7491 0.6753 0.5453 -0.0224 0.0942 0.0116 255 GLN A CA 2000 C C . GLN A 278 ? 0.7363 0.6803 0.5713 -0.0235 0.0952 0.0038 255 GLN A C 2001 O O . GLN A 278 ? 0.8274 0.7784 0.6812 -0.0266 0.1101 0.0028 255 GLN A O 2002 C CB . GLN A 278 ? 0.7972 0.7200 0.6009 -0.0283 0.1021 0.0231 255 GLN A CB 2003 C CG . GLN A 278 ? 0.8936 0.7942 0.6568 -0.0273 0.1054 0.0322 255 GLN A CG 2004 C CD . GLN A 278 ? 1.0558 0.9506 0.8278 -0.0338 0.1109 0.0430 255 GLN A CD 2005 O OE1 . GLN A 278 ? 1.1111 1.0198 0.9184 -0.0383 0.1074 0.0433 255 GLN A OE1 2006 N NE2 . GLN A 278 ? 1.1177 0.9905 0.8561 -0.0344 0.1195 0.0520 255 GLN A NE2 2007 N N . GLY A 279 ? 0.7429 0.6941 0.5903 -0.0207 0.0798 -0.0015 256 GLY A N 2008 C CA . GLY A 279 ? 0.6775 0.6417 0.5577 -0.0206 0.0799 -0.0083 256 GLY A CA 2009 C C . GLY A 279 ? 0.6834 0.6611 0.5993 -0.0236 0.0786 -0.0020 256 GLY A C 2010 O O . GLY A 279 ? 0.6602 0.6484 0.6037 -0.0232 0.0835 -0.0052 256 GLY A O 2011 N N . ALA A 280 ? 0.6242 0.6008 0.5387 -0.0258 0.0716 0.0065 257 ALA A N 2012 C CA . ALA A 280 ? 0.6115 0.5998 0.5560 -0.0291 0.0693 0.0119 257 ALA A CA 2013 C C . ALA A 280 ? 0.6328 0.6312 0.5996 -0.0265 0.0575 0.0091 257 ALA A C 2014 O O . ALA A 280 ? 0.6238 0.6338 0.6176 -0.0278 0.0566 0.0115 257 ALA A O 2015 C CB . ALA A 280 ? 0.5137 0.4949 0.4477 -0.0322 0.0652 0.0206 257 ALA A CB 2016 N N . PHE A 281 ? 0.6094 0.6033 0.5643 -0.0232 0.0484 0.0039 258 PHE A N 2017 C CA . PHE A 281 ? 0.6072 0.6082 0.5806 -0.0216 0.0383 0.0017 258 PHE A CA 2018 C C . PHE A 281 ? 0.6685 0.6695 0.6496 -0.0195 0.0416 -0.0073 258 PHE A C 2019 O O . PHE A 281 ? 0.6589 0.6588 0.6403 -0.0187 0.0335 -0.0123 258 PHE A O 2020 C CB . PHE A 281 ? 0.4560 0.4541 0.4165 -0.0205 0.0249 0.0025 258 PHE A CB 2021 C CG . PHE A 281 ? 0.4380 0.4352 0.3952 -0.0215 0.0207 0.0112 258 PHE A CG 2022 C CD1 . PHE A 281 ? 0.4640 0.4688 0.4407 -0.0225 0.0151 0.0153 258 PHE A CD1 2023 C CD2 . PHE A 281 ? 0.4654 0.4518 0.3979 -0.0213 0.0229 0.0152 258 PHE A CD2 2024 C CE1 . PHE A 281 ? 0.3922 0.3944 0.3649 -0.0235 0.0117 0.0219 258 PHE A CE1 2025 C CE2 . PHE A 281 ? 0.5450 0.5274 0.4742 -0.0222 0.0198 0.0228 258 PHE A CE2 2026 C CZ . PHE A 281 ? 0.4802 0.4706 0.4299 -0.0235 0.0142 0.0254 258 PHE A CZ 2027 N N . SER A 282 ? 0.6687 0.6710 0.6575 -0.0188 0.0543 -0.0097 259 SER A N 2028 C CA . SER A 282 ? 0.6644 0.6644 0.6609 -0.0159 0.0595 -0.0185 259 SER A CA 2029 C C . SER A 282 ? 0.5421 0.5485 0.5667 -0.0140 0.0549 -0.0169 259 SER A C 2030 O O . SER A 282 ? 0.5961 0.5971 0.6262 -0.0119 0.0558 -0.0237 259 SER A O 2031 C CB . SER A 282 ? 0.5805 0.5806 0.5780 -0.0145 0.0759 -0.0213 259 SER A CB 2032 O OG . SER A 282 ? 0.7441 0.7567 0.7645 -0.0152 0.0810 -0.0139 259 SER A OG 2033 N N . ASN A 283 ? 0.5060 0.5221 0.5466 -0.0148 0.0502 -0.0080 260 ASN A N 2034 C CA . ASN A 283 ? 0.4295 0.4505 0.4923 -0.0125 0.0446 -0.0047 260 ASN A CA 2035 C C . ASN A 283 ? 0.4886 0.5053 0.5448 -0.0144 0.0333 -0.0049 260 ASN A C 2036 O O . ASN A 283 ? 0.4943 0.5125 0.5401 -0.0170 0.0263 -0.0012 260 ASN A O 2037 C CB . ASN A 283 ? 0.3574 0.3912 0.4376 -0.0126 0.0431 0.0040 260 ASN A CB 2038 C CG . ASN A 283 ? 0.5072 0.5464 0.6095 -0.0083 0.0390 0.0079 260 ASN A CG 2039 O OD1 . ASN A 283 ? 0.5028 0.5359 0.6044 -0.0076 0.0330 0.0080 260 ASN A OD1 2040 N ND2 . ASN A 283 ? 0.5438 0.5949 0.6661 -0.0054 0.0424 0.0113 260 ASN A ND2 2041 N N . PRO A 284 ? 0.5207 0.5315 0.5840 -0.0131 0.0326 -0.0094 261 PRO A N 2042 C CA . PRO A 284 ? 0.5394 0.5470 0.6000 -0.0159 0.0239 -0.0109 261 PRO A CA 2043 C C . PRO A 284 ? 0.5163 0.5313 0.5833 -0.0168 0.0160 -0.0017 261 PRO A C 2044 O O . PRO A 284 ? 0.5739 0.5897 0.6344 -0.0195 0.0089 -0.0023 261 PRO A O 2045 C CB . PRO A 284 ? 0.5111 0.5103 0.5843 -0.0144 0.0278 -0.0152 261 PRO A CB 2046 C CG . PRO A 284 ? 0.5670 0.5676 0.6533 -0.0086 0.0364 -0.0125 261 PRO A CG 2047 C CD . PRO A 284 ? 0.4431 0.4493 0.5193 -0.0088 0.0411 -0.0133 261 PRO A CD 2048 N N . ASN A 285 ? 0.4629 0.4844 0.5426 -0.0142 0.0170 0.0060 262 ASN A N 2049 C CA . ASN A 285 ? 0.4513 0.4790 0.5342 -0.0148 0.0098 0.0140 262 ASN A CA 2050 C C . ASN A 285 ? 0.4534 0.4839 0.5221 -0.0176 0.0061 0.0153 262 ASN A C 2051 O O . ASN A 285 ? 0.4283 0.4601 0.4924 -0.0188 -0.0005 0.0180 262 ASN A O 2052 C CB . ASN A 285 ? 0.3899 0.4245 0.4885 -0.0112 0.0105 0.0209 262 ASN A CB 2053 C CG . ASN A 285 ? 0.5699 0.5997 0.6817 -0.0066 0.0136 0.0215 262 ASN A CG 2054 O OD1 . ASN A 285 ? 0.6574 0.6835 0.7720 -0.0059 0.0101 0.0257 262 ASN A OD1 2055 N ND2 . ASN A 285 ? 0.5474 0.5760 0.6667 -0.0030 0.0212 0.0178 262 ASN A ND2 2056 N N . ALA A 286 ? 0.3933 0.4236 0.4549 -0.0182 0.0114 0.0137 263 ALA A N 2057 C CA . ALA A 286 ? 0.4364 0.4655 0.4827 -0.0205 0.0093 0.0158 263 ALA A CA 2058 C C . ALA A 286 ? 0.5430 0.5659 0.5709 -0.0206 0.0048 0.0115 263 ALA A C 2059 O O . ALA A 286 ? 0.5348 0.5569 0.5527 -0.0207 -0.0012 0.0143 263 ALA A O 2060 C CB . ALA A 286 ? 0.2740 0.3034 0.3177 -0.0218 0.0181 0.0161 263 ALA A CB 2061 N N . ALA A 287 ? 0.5014 0.5203 0.5253 -0.0201 0.0072 0.0040 264 ALA A N 2062 C CA . ALA A 287 ? 0.5743 0.5898 0.5823 -0.0202 0.0013 -0.0017 264 ALA A CA 2063 C C . ALA A 287 ? 0.5015 0.5223 0.5176 -0.0207 -0.0076 -0.0010 264 ALA A C 2064 O O . ALA A 287 ? 0.4274 0.4500 0.4333 -0.0198 -0.0149 -0.0012 264 ALA A O 2065 C CB . ALA A 287 ? 0.4730 0.4832 0.4765 -0.0205 0.0054 -0.0115 264 ALA A CB 2066 N N . ALA A 288 ? 0.4066 0.4298 0.4412 -0.0216 -0.0064 0.0005 265 ALA A N 2067 C CA . ALA A 288 ? 0.4503 0.4784 0.4939 -0.0227 -0.0122 0.0017 265 ALA A CA 2068 C C . ALA A 288 ? 0.4548 0.4874 0.4953 -0.0212 -0.0169 0.0088 265 ALA A C 2069 O O . ALA A 288 ? 0.4101 0.4472 0.4496 -0.0210 -0.0227 0.0080 265 ALA A O 2070 C CB . ALA A 288 ? 0.4450 0.4714 0.5059 -0.0235 -0.0082 0.0036 265 ALA A CB 2071 N N . GLN A 289 ? 0.4312 0.4630 0.4714 -0.0203 -0.0143 0.0150 266 GLN A N 2072 C CA . GLN A 289 ? 0.5182 0.5520 0.5555 -0.0194 -0.0182 0.0208 266 GLN A CA 2073 C C . GLN A 289 ? 0.4762 0.5065 0.4965 -0.0177 -0.0217 0.0206 266 GLN A C 2074 O O . GLN A 289 ? 0.4528 0.4839 0.4698 -0.0159 -0.0261 0.0234 266 GLN A O 2075 C CB . GLN A 289 ? 0.5097 0.5444 0.5533 -0.0199 -0.0154 0.0262 266 GLN A CB 2076 C CG . GLN A 289 ? 0.4134 0.4515 0.4722 -0.0194 -0.0142 0.0286 266 GLN A CG 2077 C CD . GLN A 289 ? 0.4339 0.4760 0.4995 -0.0192 -0.0141 0.0336 266 GLN A CD 2078 O OE1 . GLN A 289 ? 0.4484 0.4934 0.5223 -0.0176 -0.0158 0.0375 266 GLN A OE1 2079 N NE2 . GLN A 289 ? 0.3604 0.4026 0.4221 -0.0211 -0.0121 0.0336 266 GLN A NE2 2080 N N . VAL A 290 ? 0.4562 0.4815 0.4642 -0.0175 -0.0194 0.0176 267 VAL A N 2081 C CA . VAL A 290 ? 0.4434 0.4624 0.4318 -0.0149 -0.0221 0.0191 267 VAL A CA 2082 C C . VAL A 290 ? 0.4990 0.5213 0.4803 -0.0114 -0.0301 0.0144 267 VAL A C 2083 O O . VAL A 290 ? 0.4913 0.5109 0.4605 -0.0071 -0.0354 0.0168 267 VAL A O 2084 C CB . VAL A 290 ? 0.4669 0.4773 0.4413 -0.0160 -0.0149 0.0195 267 VAL A CB 2085 C CG1 . VAL A 290 ? 0.4696 0.4793 0.4370 -0.0156 -0.0136 0.0121 267 VAL A CG1 2086 C CG2 . VAL A 290 ? 0.4491 0.4492 0.4031 -0.0137 -0.0160 0.0244 267 VAL A CG2 2087 N N . LEU A 291 ? 0.4167 0.4448 0.4066 -0.0133 -0.0313 0.0074 268 LEU A N 2088 C CA . LEU A 291 ? 0.3927 0.4266 0.3781 -0.0113 -0.0395 0.0008 268 LEU A CA 2089 C C . LEU A 291 ? 0.3531 0.3960 0.3438 -0.0076 -0.0477 0.0020 268 LEU A C 2090 O O . LEU A 291 ? 0.5199 0.5643 0.4980 -0.0024 -0.0552 0.0007 268 LEU A O 2091 C CB . LEU A 291 ? 0.4018 0.4396 0.3987 -0.0159 -0.0384 -0.0081 268 LEU A CB 2092 C CG . LEU A 291 ? 0.4620 0.5082 0.4577 -0.0158 -0.0476 -0.0173 268 LEU A CG 2093 C CD1 . LEU A 291 ? 0.3245 0.3656 0.2940 -0.0114 -0.0522 -0.0198 268 LEU A CD1 2094 C CD2 . LEU A 291 ? 0.4629 0.5112 0.4735 -0.0223 -0.0453 -0.0264 268 LEU A CD2 2095 N N . PRO A 292 ? 0.4190 0.4680 0.4276 -0.0093 -0.0462 0.0047 269 PRO A N 2096 C CA . PRO A 292 ? 0.4467 0.5061 0.4625 -0.0057 -0.0524 0.0046 269 PRO A CA 2097 C C . PRO A 292 ? 0.5308 0.5853 0.5306 0.0021 -0.0570 0.0094 269 PRO A C 2098 O O . PRO A 292 ? 0.4716 0.5340 0.4698 0.0077 -0.0650 0.0067 269 PRO A O 2099 C CB . PRO A 292 ? 0.4071 0.4687 0.4384 -0.0086 -0.0470 0.0087 269 PRO A CB 2100 C CG . PRO A 292 ? 0.4338 0.4910 0.4719 -0.0145 -0.0406 0.0078 269 PRO A CG 2101 C CD . PRO A 292 ? 0.3673 0.4149 0.3900 -0.0139 -0.0389 0.0074 269 PRO A CD 2102 N N . ALA A 293 ? 0.4443 0.4858 0.4334 0.0025 -0.0520 0.0162 270 ALA A N 2103 C CA . ALA A 293 ? 0.5147 0.5467 0.4876 0.0092 -0.0546 0.0214 270 ALA A CA 2104 C C . ALA A 293 ? 0.4380 0.4651 0.3910 0.0147 -0.0601 0.0205 270 ALA A C 2105 O O . ALA A 293 ? 0.4994 0.5249 0.4430 0.0231 -0.0664 0.0226 270 ALA A O 2106 C CB . ALA A 293 ? 0.4944 0.5126 0.4608 0.0061 -0.0474 0.0276 270 ALA A CB 2107 N N . LEU A 294 ? 0.4675 0.4917 0.4129 0.0108 -0.0576 0.0172 271 LEU A N 2108 C CA . LEU A 294 ? 0.5316 0.5496 0.4536 0.0158 -0.0623 0.0162 271 LEU A CA 2109 C C . LEU A 294 ? 0.5774 0.6105 0.5032 0.0214 -0.0748 0.0099 271 LEU A C 2110 O O . LEU A 294 ? 0.5510 0.5810 0.4565 0.0286 -0.0823 0.0099 271 LEU A O 2111 C CB . LEU A 294 ? 0.4957 0.5082 0.4094 0.0101 -0.0558 0.0126 271 LEU A CB 2112 C CG . LEU A 294 ? 0.5526 0.5544 0.4672 0.0041 -0.0432 0.0176 271 LEU A CG 2113 C CD1 . LEU A 294 ? 0.4794 0.4780 0.3879 -0.0002 -0.0363 0.0128 271 LEU A CD1 2114 C CD2 . LEU A 294 ? 0.6222 0.6082 0.5191 0.0070 -0.0399 0.0267 271 LEU A CD2 2115 N N . MET A 295 ? 0.5294 0.5795 0.4814 0.0182 -0.0770 0.0046 272 MET A N 2116 C CA . MET A 295 ? 0.5054 0.5743 0.4682 0.0217 -0.0882 -0.0026 272 MET A CA 2117 C C . MET A 295 ? 0.4616 0.5396 0.4382 0.0279 -0.0912 0.0008 272 MET A C 2118 O O . MET A 295 ? 0.4884 0.5862 0.4826 0.0300 -0.0986 -0.0050 272 MET A O 2119 C CB . MET A 295 ? 0.5110 0.5927 0.4953 0.0121 -0.0870 -0.0122 272 MET A CB 2120 C CG . MET A 295 ? 0.8461 0.9416 0.8308 0.0126 -0.0983 -0.0228 272 MET A CG 2121 S SD . MET A 295 ? 1.0551 1.1358 1.0107 0.0108 -0.0978 -0.0273 272 MET A SD 2122 C CE . MET A 295 ? 0.6223 0.6972 0.5949 -0.0017 -0.0842 -0.0310 272 MET A CE 2123 N N . GLY A 296 ? 0.4578 0.5219 0.4276 0.0304 -0.0849 0.0095 273 GLY A N 2124 C CA . GLY A 296 ? 0.4128 0.4815 0.3917 0.0373 -0.0862 0.0127 273 GLY A CA 2125 C C . GLY A 296 ? 0.5243 0.6070 0.5301 0.0313 -0.0812 0.0097 273 GLY A C 2126 O O . GLY A 296 ? 0.4938 0.5884 0.5131 0.0366 -0.0833 0.0089 273 GLY A O 2127 N N . LYS A 297 ? 0.5286 0.6092 0.5417 0.0209 -0.0739 0.0085 274 LYS A N 2128 C CA . LYS A 297 ? 0.4015 0.4924 0.4369 0.0147 -0.0681 0.0067 274 LYS A CA 2129 C C . LYS A 297 ? 0.4511 0.5288 0.4831 0.0108 -0.0592 0.0131 274 LYS A C 2130 O O . LYS A 297 ? 0.4994 0.5627 0.5172 0.0090 -0.0565 0.0166 274 LYS A O 2131 C CB . LYS A 297 ? 0.4439 0.5441 0.4929 0.0060 -0.0678 -0.0006 274 LYS A CB 2132 C CG . LYS A 297 ? 0.4633 0.5807 0.5202 0.0080 -0.0777 -0.0091 274 LYS A CG 2133 C CD . LYS A 297 ? 0.5851 0.7222 0.6642 0.0106 -0.0795 -0.0114 274 LYS A CD 2134 C CE . LYS A 297 ? 0.7352 0.8933 0.8262 0.0120 -0.0906 -0.0210 274 LYS A CE 2135 N NZ . LYS A 297 ? 0.9044 1.0850 1.0209 0.0147 -0.0915 -0.0236 274 LYS A NZ 2136 N N . THR A 298 ? 0.3755 0.4590 0.4204 0.0094 -0.0546 0.0142 275 THR A N 2137 C CA . THR A 298 ? 0.4239 0.4975 0.4665 0.0055 -0.0474 0.0193 275 THR A CA 2138 C C . THR A 298 ? 0.4947 0.5766 0.5541 -0.0007 -0.0418 0.0184 275 THR A C 2139 O O . THR A 298 ? 0.4333 0.5285 0.5077 -0.0025 -0.0426 0.0135 275 THR A O 2140 C CB . THR A 298 ? 0.4133 0.4801 0.4476 0.0112 -0.0463 0.0232 275 THR A CB 2141 O OG1 . THR A 298 ? 0.4237 0.5025 0.4710 0.0133 -0.0440 0.0216 275 THR A OG1 2142 C CG2 . THR A 298 ? 0.3946 0.4535 0.4142 0.0191 -0.0517 0.0241 275 THR A CG2 2143 N N . PHE A 299 ? 0.4771 0.5511 0.5342 -0.0039 -0.0364 0.0231 276 PHE A N 2144 C CA . PHE A 299 ? 0.3619 0.4399 0.4309 -0.0088 -0.0302 0.0243 276 PHE A CA 2145 C C . PHE A 299 ? 0.5263 0.6147 0.6044 -0.0067 -0.0271 0.0234 276 PHE A C 2146 O O . PHE A 299 ? 0.5042 0.5979 0.5943 -0.0113 -0.0211 0.0236 276 PHE A O 2147 C CB . PHE A 299 ? 0.4321 0.4995 0.4939 -0.0106 -0.0266 0.0304 276 PHE A CB 2148 C CG . PHE A 299 ? 0.3766 0.4376 0.4377 -0.0139 -0.0267 0.0309 276 PHE A CG 2149 C CD1 . PHE A 299 ? 0.4865 0.5496 0.5516 -0.0157 -0.0286 0.0257 276 PHE A CD1 2150 C CD2 . PHE A 299 ? 0.5955 0.6496 0.6523 -0.0146 -0.0251 0.0360 276 PHE A CD2 2151 C CE1 . PHE A 299 ? 0.5998 0.6566 0.6641 -0.0180 -0.0272 0.0256 276 PHE A CE1 2152 C CE2 . PHE A 299 ? 0.6030 0.6532 0.6619 -0.0165 -0.0245 0.0362 276 PHE A CE2 2153 C CZ . PHE A 299 ? 0.5521 0.6030 0.6146 -0.0181 -0.0247 0.0310 276 PHE A CZ 2154 N N . LEU A 300 ? 0.4669 0.5573 0.5393 0.0004 -0.0301 0.0227 277 LEU A N 2155 C CA . LEU A 300 ? 0.4991 0.6004 0.5808 0.0038 -0.0263 0.0214 277 LEU A CA 2156 C C . LEU A 300 ? 0.4820 0.6024 0.5836 0.0036 -0.0287 0.0150 277 LEU A C 2157 O O . LEU A 300 ? 0.4945 0.6283 0.6096 0.0054 -0.0245 0.0129 277 LEU A O 2158 C CB . LEU A 300 ? 0.4807 0.5755 0.5493 0.0125 -0.0280 0.0225 277 LEU A CB 2159 C CG . LEU A 300 ? 0.6008 0.6786 0.6512 0.0118 -0.0257 0.0272 277 LEU A CG 2160 C CD1 . LEU A 300 ? 0.6213 0.6918 0.6602 0.0199 -0.0266 0.0266 277 LEU A CD1 2161 C CD2 . LEU A 300 ? 0.5678 0.6457 0.6201 0.0068 -0.0181 0.0303 277 LEU A CD2 2162 N N . ASP A 301 ? 0.4892 0.6122 0.5931 0.0013 -0.0354 0.0111 278 ASP A N 2163 C CA . ASP A 301 ? 0.5266 0.6690 0.6498 0.0000 -0.0398 0.0035 278 ASP A CA 2164 C C . ASP A 301 ? 0.5491 0.6977 0.6905 -0.0111 -0.0328 0.0009 278 ASP A C 2165 O O . ASP A 301 ? 0.5681 0.7329 0.7283 -0.0152 -0.0356 -0.0066 278 ASP A O 2166 C CB . ASP A 301 ? 0.5210 0.6624 0.6355 0.0025 -0.0506 -0.0004 278 ASP A CB 2167 C CG . ASP A 301 ? 0.5834 0.7190 0.6814 0.0140 -0.0572 0.0024 278 ASP A CG 2168 O OD1 . ASP A 301 ? 0.5378 0.6794 0.6400 0.0212 -0.0560 0.0035 278 ASP A OD1 2169 O OD2 . ASP A 301 ? 0.6503 0.7741 0.7304 0.0160 -0.0625 0.0036 278 ASP A OD2 2170 N N . ILE A 302 ? 0.5324 0.6673 0.6678 -0.0159 -0.0241 0.0070 279 ILE A N 2171 C CA . ILE A 302 ? 0.6791 0.8147 0.8288 -0.0257 -0.0155 0.0067 279 ILE A CA 2172 C C . ILE A 302 ? 0.7528 0.9035 0.9203 -0.0274 -0.0074 0.0059 279 ILE A C 2173 O O . ILE A 302 ? 0.7673 0.9141 0.9275 -0.0238 -0.0005 0.0118 279 ILE A O 2174 C CB . ILE A 302 ? 0.6653 0.7808 0.8013 -0.0282 -0.0091 0.0151 279 ILE A CB 2175 C CG1 . ILE A 302 ? 0.6238 0.7274 0.7479 -0.0279 -0.0153 0.0147 279 ILE A CG1 2176 C CG2 . ILE A 302 ? 0.8084 0.9216 0.9569 -0.0370 0.0013 0.0168 279 ILE A CG2 2177 C CD1 . ILE A 302 ? 0.5975 0.6843 0.7100 -0.0284 -0.0110 0.0226 279 ILE A CD1 2178 N N . ASN A 303 ? 0.7030 0.8717 0.8942 -0.0331 -0.0082 -0.0023 280 ASN A N 2179 C CA . ASN A 303 ? 0.7752 0.9614 0.9886 -0.0365 0.0009 -0.0042 280 ASN A CA 2180 C C . ASN A 303 ? 0.9357 1.1181 1.1635 -0.0501 0.0114 -0.0046 280 ASN A C 2181 O O . ASN A 303 ? 0.9926 1.1828 1.2369 -0.0582 0.0076 -0.0130 280 ASN A O 2182 C CB . ASN A 303 ? 0.8513 1.0649 1.0854 -0.0326 -0.0080 -0.0139 280 ASN A CB 2183 C CG . ASN A 303 ? 0.9855 1.2199 1.2422 -0.0325 0.0014 -0.0154 280 ASN A CG 2184 O OD1 . ASN A 303 ? 1.0096 1.2396 1.2711 -0.0394 0.0162 -0.0110 280 ASN A OD1 2185 N ND2 . ASN A 303 ? 1.0151 1.2725 1.2856 -0.0239 -0.0066 -0.0215 280 ASN A ND2 2186 N N . LYS A 304 ? 0.8994 1.0680 1.1191 -0.0525 0.0245 0.0046 281 LYS A N 2187 C CA . LYS A 304 ? 0.9194 1.0779 1.1479 -0.0646 0.0360 0.0069 281 LYS A CA 2188 C C . LYS A 304 ? 1.0274 1.2073 1.2886 -0.0749 0.0430 -0.0011 281 LYS A C 2189 O O . LYS A 304 ? 0.9871 1.1613 1.2614 -0.0870 0.0495 -0.0034 281 LYS A O 2190 C CB . LYS A 304 ? 0.8898 1.0284 1.0988 -0.0631 0.0481 0.0197 281 LYS A CB 2191 C CG . LYS A 304 ? 0.8497 0.9987 1.0627 -0.0612 0.0595 0.0229 281 LYS A CG 2192 C CD . LYS A 304 ? 0.9076 1.0349 1.0951 -0.0585 0.0695 0.0356 281 LYS A CD 2193 C CE . LYS A 304 ? 0.9438 1.0789 1.1367 -0.0602 0.0855 0.0387 281 LYS A CE 2194 N NZ . LYS A 304 ? 0.9495 1.0919 1.1693 -0.0738 0.0981 0.0361 281 LYS A NZ 2195 N N . ASP A 305 ? 1.2209 1.4255 1.4968 -0.0700 0.0420 -0.0056 282 ASP A N 2196 C CA . ASP A 305 ? 1.3097 1.5405 1.6213 -0.0792 0.0480 -0.0142 282 ASP A CA 2197 C C . ASP A 305 ? 1.3468 1.6010 1.6782 -0.0794 0.0316 -0.0279 282 ASP A C 2198 O O . ASP A 305 ? 1.3492 1.6316 1.6998 -0.0739 0.0266 -0.0343 282 ASP A O 2199 C CB . ASP A 305 ? 1.3245 1.5712 1.6445 -0.0739 0.0589 -0.0115 282 ASP A CB 2200 C CG . ASP A 305 ? 1.3030 1.5283 1.6056 -0.0763 0.0772 0.0009 282 ASP A CG 2201 O OD1 . ASP A 305 ? 1.3531 1.5765 1.6705 -0.0892 0.0919 0.0023 282 ASP A OD1 2202 O OD2 . ASP A 305 ? 1.2388 1.4485 1.5121 -0.0656 0.0768 0.0091 282 ASP A OD2 2203 N N . SER A 306 ? 1.4227 1.6645 1.7477 -0.0847 0.0230 -0.0321 283 SER A N 2204 C CA . SER A 306 ? 1.4626 1.7227 1.8040 -0.0880 0.0080 -0.0460 283 SER A CA 2205 C C . SER A 306 ? 1.4889 1.7577 1.8163 -0.0734 -0.0104 -0.0489 283 SER A C 2206 O O . SER A 306 ? 1.4770 1.7605 1.8057 -0.0618 -0.0134 -0.0470 283 SER A O 2207 C CB . SER A 306 ? 1.4827 1.7735 1.8652 -0.0992 0.0119 -0.0569 283 SER A CB 2208 O OG . SER A 306 ? 1.4855 1.7923 1.8824 -0.1041 -0.0035 -0.0712 283 SER A OG 2209 N N . SER A 307 ? 1.5092 1.7666 1.8220 -0.0739 -0.0218 -0.0534 284 SER A N 2210 C CA . SER A 307 ? 1.4681 1.7324 1.7673 -0.0624 -0.0396 -0.0575 284 SER A CA 2211 C C . SER A 307 ? 1.5540 1.8107 1.8484 -0.0701 -0.0480 -0.0668 284 SER A C 2212 O O . SER A 307 ? 1.5317 1.7917 1.8127 -0.0631 -0.0629 -0.0717 284 SER A O 2213 C CB . SER A 307 ? 1.3786 1.6218 1.6445 -0.0491 -0.0405 -0.0457 284 SER A CB 2214 O OG . SER A 307 ? 1.3394 1.5888 1.6075 -0.0411 -0.0338 -0.0386 284 SER A OG 2215 N N . CYS A 308 ? 1.6886 1.9333 1.9923 -0.0844 -0.0375 -0.0690 285 CYS A N 2216 C CA . CYS A 308 ? 1.7878 2.0195 2.0856 -0.0928 -0.0421 -0.0778 285 CYS A CA 2217 C C . CYS A 308 ? 1.8142 2.0710 2.1290 -0.0972 -0.0571 -0.0946 285 CYS A C 2218 O O . CYS A 308 ? 1.8304 2.1055 2.1765 -0.1095 -0.0548 -0.1043 285 CYS A O 2219 C CB . CYS A 308 ? 1.8133 2.0259 2.1203 -0.1071 -0.0261 -0.0764 285 CYS A CB 2220 S SG . CYS A 308 ? 1.2595 1.4338 1.5368 -0.1020 -0.0136 -0.0595 285 CYS A SG 2221 N N . VAL A 309 ? 1.7675 2.0250 2.0609 -0.0873 -0.0725 -0.0980 286 VAL A N 2222 C CA . VAL A 309 ? 1.6860 1.9630 1.9878 -0.0906 -0.0889 -0.1142 286 VAL A CA 2223 C C . VAL A 309 ? 1.7653 2.0215 2.0592 -0.1027 -0.0868 -0.1233 286 VAL A C 2224 O O . VAL A 309 ? 1.8362 2.0682 2.0992 -0.0974 -0.0875 -0.1198 286 VAL A O 2225 C CB . VAL A 309 ? 1.5379 1.8211 1.8151 -0.0740 -0.1059 -0.1131 286 VAL A CB 2226 C CG1 . VAL A 309 ? 1.5087 1.8152 1.7944 -0.0765 -0.1246 -0.1300 286 VAL A CG1 2227 C CG2 . VAL A 309 ? 1.4535 1.7499 1.7339 -0.0603 -0.1061 -0.1024 286 VAL A CG2 2228 N N . SER A 310 ? 1.7520 2.0169 2.0746 -0.1193 -0.0829 -0.1351 287 SER A N 2229 C CA . SER A 310 ? 1.7324 1.9749 2.0508 -0.1322 -0.0785 -0.1446 287 SER A CA 2230 C C . SER A 310 ? 1.8009 2.0391 2.0942 -0.1281 -0.0943 -0.1558 287 SER A C 2231 O O . SER A 310 ? 1.8350 2.0452 2.1082 -0.1310 -0.0894 -0.1578 287 SER A O 2232 C CB . SER A 310 ? 1.6363 1.8921 1.9929 -0.1517 -0.0732 -0.1573 287 SER A CB 2233 O OG . SER A 310 ? 1.5314 1.7851 1.9071 -0.1566 -0.0552 -0.1459 287 SER A OG 2234 N N . ALA A 311 ? 1.7819 2.0477 2.0755 -0.1206 -0.1129 -0.1628 288 ALA A N 2235 C CA . ALA A 311 ? 1.7151 1.9778 1.9803 -0.1147 -0.1289 -0.1722 288 ALA A CA 2236 C C . ALA A 311 ? 1.6037 1.8559 1.8336 -0.0954 -0.1325 -0.1576 288 ALA A C 2237 O O . ALA A 311 ? 1.6368 1.9098 1.8661 -0.0834 -0.1439 -0.1536 288 ALA A O 2238 C CB . ALA A 311 ? 1.7141 2.0124 1.9981 -0.1177 -0.1489 -0.1894 288 ALA A CB 2239 N N . SER A 312 ? 1.4252 1.6451 1.6273 -0.0926 -0.1222 -0.1496 289 SER A N 2240 C CA . SER A 312 ? 1.3133 1.5206 1.4836 -0.0766 -0.1227 -0.1352 289 SER A CA 2241 C C . SER A 312 ? 1.1147 1.2916 1.2527 -0.0752 -0.1168 -0.1344 289 SER A C 2242 O O . SER A 312 ? 0.8923 1.0475 1.0295 -0.0785 -0.1014 -0.1272 289 SER A O 2243 C CB . SER A 312 ? 1.3725 1.5769 1.5515 -0.0714 -0.1105 -0.1180 289 SER A CB 2244 O OG . SER A 312 ? 1.3678 1.6006 1.5708 -0.0684 -0.1164 -0.1174 289 SER A OG 2245 N N . GLY A 313 ? 1.0106 1.1869 1.1220 -0.0694 -0.1290 -0.1415 290 GLY A N 2246 C CA . GLY A 313 ? 0.8163 0.9658 0.8950 -0.0666 -0.1231 -0.1407 290 GLY A CA 2247 C C . GLY A 313 ? 0.8314 0.9780 0.8962 -0.0725 -0.1315 -0.1593 290 GLY A C 2248 O O . GLY A 313 ? 0.8244 0.9668 0.9057 -0.0856 -0.1273 -0.1718 290 GLY A O 2249 N N . ASN A 314 ? 0.8608 1.0079 0.8933 -0.0628 -0.1433 -0.1612 291 ASN A N 2250 C CA . ASN A 314 ? 0.8125 0.9527 0.8219 -0.0662 -0.1508 -0.1780 291 ASN A CA 2251 C C . ASN A 314 ? 0.9142 1.0275 0.8838 -0.0582 -0.1416 -0.1712 291 ASN A C 2252 O O . ASN A 314 ? 0.9865 1.0983 0.9311 -0.0456 -0.1452 -0.1596 291 ASN A O 2253 C CB . ASN A 314 ? 0.8256 0.9911 0.8282 -0.0616 -0.1741 -0.1878 291 ASN A CB 2254 C CG . ASN A 314 ? 0.9672 1.1632 1.0126 -0.0707 -0.1837 -0.1972 291 ASN A CG 2255 O OD1 . ASN A 314 ? 1.0912 1.2859 1.1666 -0.0850 -0.1742 -0.2040 291 ASN A OD1 2256 N ND2 . ASN A 314 ? 0.8798 1.1033 0.9289 -0.0621 -0.2021 -0.1974 291 ASN A ND2 2257 N N . PHE A 315 ? 0.8720 0.9634 0.8364 -0.0653 -0.1287 -0.1783 292 PHE A N 2258 C CA . PHE A 315 ? 0.8824 0.9490 0.8154 -0.0584 -0.1160 -0.1713 292 PHE A CA 2259 C C . PHE A 315 ? 1.0203 1.0736 0.9213 -0.0597 -0.1183 -0.1874 292 PHE A C 2260 O O . PHE A 315 ? 0.9442 0.9870 0.8530 -0.0696 -0.1128 -0.2020 292 PHE A O 2261 C CB . PHE A 315 ? 0.7993 0.8494 0.7508 -0.0618 -0.0958 -0.1622 292 PHE A CB 2262 C CG . PHE A 315 ? 0.8523 0.9128 0.8304 -0.0601 -0.0925 -0.1462 292 PHE A CG 2263 C CD1 . PHE A 315 ? 0.9708 1.0312 0.9371 -0.0496 -0.0903 -0.1292 292 PHE A CD1 2264 C CD2 . PHE A 315 ? 0.8693 0.9384 0.8829 -0.0695 -0.0908 -0.1486 292 PHE A CD2 2265 C CE1 . PHE A 315 ? 0.9435 1.0124 0.9320 -0.0480 -0.0875 -0.1158 292 PHE A CE1 2266 C CE2 . PHE A 315 ? 0.9015 0.9794 0.9364 -0.0676 -0.0871 -0.1343 292 PHE A CE2 2267 C CZ . PHE A 315 ? 0.9613 1.0393 0.9832 -0.0566 -0.0859 -0.1184 292 PHE A CZ 2268 N N . ASN A 316 ? 1.1424 1.1940 1.0055 -0.0494 -0.1256 -0.1846 293 ASN A N 2269 C CA . ASN A 316 ? 1.2629 1.2987 1.0881 -0.0486 -0.1253 -0.1975 293 ASN A CA 2270 C C . ASN A 316 ? 1.2517 1.2618 1.0667 -0.0475 -0.1024 -0.1921 293 ASN A C 2271 O O . ASN A 316 ? 1.2736 1.2790 1.0949 -0.0422 -0.0905 -0.1742 293 ASN A O 2272 C CB . ASN A 316 ? 1.5059 1.5462 1.2909 -0.0369 -0.1391 -0.1938 293 ASN A CB 2273 C CG . ASN A 316 ? 1.7899 1.8142 1.5315 -0.0358 -0.1396 -0.2078 293 ASN A CG 2274 O OD1 . ASN A 316 ? 1.8055 1.8197 1.5499 -0.0450 -0.1342 -0.2248 293 ASN A OD1 2275 N ND2 . ASN A 316 ? 2.0330 2.0529 1.7321 -0.0242 -0.1454 -0.2006 293 ASN A ND2 2276 N N . ILE A 317 ? 1.3166 1.3106 1.1168 -0.0524 -0.0963 -0.2084 294 ILE A N 2277 C CA . ILE A 317 ? 1.3074 1.2784 1.1033 -0.0514 -0.0739 -0.2056 294 ILE A CA 2278 C C . ILE A 317 ? 1.3470 1.3000 1.1063 -0.0513 -0.0696 -0.2224 294 ILE A C 2279 O O . ILE A 317 ? 1.4179 1.3566 1.1493 -0.0439 -0.0566 -0.2165 294 ILE A O 2280 C CB . ILE A 317 ? 1.1998 1.1664 1.0376 -0.0599 -0.0632 -0.2063 294 ILE A CB 2281 C CG1 . ILE A 317 ? 1.2009 1.1430 1.0320 -0.0615 -0.0455 -0.2161 294 ILE A CG1 2282 C CG2 . ILE A 317 ? 1.0850 1.0659 0.9495 -0.0710 -0.0773 -0.2191 294 ILE A CG2 2283 C CD1 . ILE A 317 ? 1.2047 1.1393 1.0725 -0.0703 -0.0377 -0.2207 294 ILE A CD1 2475 N N . ASN A 354 ? 1.0864 1.6564 1.2393 -0.0845 0.0178 -0.0060 331 ASN A N 2476 C CA . ASN A 354 ? 1.0045 1.5567 1.1519 -0.0981 0.0134 0.0037 331 ASN A CA 2477 C C . ASN A 354 ? 0.8901 1.4067 1.0337 -0.0925 0.0129 0.0029 331 ASN A C 2478 O O . ASN A 354 ? 0.9071 1.4188 1.0491 -0.0859 0.0163 -0.0036 331 ASN A O 2479 C CB . ASN A 354 ? 1.0374 1.6097 1.1810 -0.1120 0.0138 0.0069 331 ASN A CB 2480 C CG . ASN A 354 ? 1.0747 1.6397 1.2157 -0.1289 0.0074 0.0189 331 ASN A CG 2481 O OD1 . ASN A 354 ? 0.8358 1.3769 0.9773 -0.1296 0.0026 0.0237 331 ASN A OD1 2482 N ND2 . ASN A 354 ? 1.4288 2.0153 1.5673 -0.1426 0.0067 0.0236 331 ASN A ND2 2483 N N . GLY A 355 ? 0.7852 1.2778 0.9281 -0.0949 0.0083 0.0090 332 GLY A N 2484 C CA . GLY A 355 ? 0.7214 1.1807 0.8613 -0.0900 0.0077 0.0086 332 GLY A CA 2485 C C . GLY A 355 ? 0.6403 1.0850 0.7831 -0.0759 0.0086 0.0052 332 GLY A C 2486 O O . GLY A 355 ? 0.5367 0.9552 0.6776 -0.0701 0.0088 0.0043 332 GLY A O 2487 N N . SER A 356 ? 0.6011 1.0635 0.7486 -0.0707 0.0090 0.0037 333 SER A N 2488 C CA . SER A 356 ? 0.5397 0.9903 0.6899 -0.0580 0.0092 0.0015 333 SER A CA 2489 C C . SER A 356 ? 0.5395 0.9695 0.6879 -0.0621 0.0045 0.0082 333 SER A C 2490 O O . SER A 356 ? 0.4271 0.8585 0.5744 -0.0745 0.0005 0.0143 333 SER A O 2491 C CB . SER A 356 ? 0.5745 1.0507 0.7305 -0.0519 0.0102 -0.0021 333 SER A CB 2492 O OG . SER A 356 ? 0.5999 1.0963 0.7586 -0.0467 0.0144 -0.0099 333 SER A OG 2493 N N . VAL A 357 ? 0.5253 0.9366 0.6737 -0.0516 0.0047 0.0071 334 VAL A N 2494 C CA . VAL A 357 ? 0.4965 0.8895 0.6432 -0.0542 0.0007 0.0123 334 VAL A CA 2495 C C . VAL A 357 ? 0.5093 0.9139 0.6595 -0.0511 -0.0016 0.0137 334 VAL A C 2496 O O . VAL A 357 ? 0.4959 0.9201 0.6498 -0.0451 0.0002 0.0103 334 VAL A O 2497 C CB . VAL A 357 ? 0.4498 0.8145 0.5936 -0.0463 0.0020 0.0113 334 VAL A CB 2498 C CG1 . VAL A 357 ? 0.3852 0.7365 0.5259 -0.0507 0.0035 0.0103 334 VAL A CG1 2499 C CG2 . VAL A 357 ? 0.3216 0.6868 0.4679 -0.0316 0.0052 0.0066 334 VAL A CG2 2500 N N . PHE A 358 ? 0.5087 0.9014 0.6579 -0.0550 -0.0059 0.0183 335 PHE A N 2501 C CA . PHE A 358 ? 0.4412 0.8426 0.5933 -0.0525 -0.0089 0.0199 335 PHE A CA 2502 C C . PHE A 358 ? 0.5088 0.9115 0.6621 -0.0379 -0.0061 0.0160 335 PHE A C 2503 O O . PHE A 358 ? 0.4589 0.8784 0.6159 -0.0343 -0.0070 0.0153 335 PHE A O 2504 C CB . PHE A 358 ? 0.4024 0.7861 0.5528 -0.0569 -0.0138 0.0239 335 PHE A CB 2505 C CG . PHE A 358 ? 0.3419 0.7359 0.4956 -0.0575 -0.0182 0.0260 335 PHE A CG 2506 C CD1 . PHE A 358 ? 0.3371 0.7312 0.4909 -0.0463 -0.0174 0.0245 335 PHE A CD1 2507 C CD2 . PHE A 358 ? 0.3967 0.7992 0.5537 -0.0693 -0.0238 0.0297 335 PHE A CD2 2508 C CE1 . PHE A 358 ? 0.3775 0.7810 0.5344 -0.0466 -0.0217 0.0261 335 PHE A CE1 2509 C CE2 . PHE A 358 ? 0.4281 0.8398 0.5890 -0.0695 -0.0284 0.0313 335 PHE A CE2 2510 C CZ . PHE A 358 ? 0.4205 0.8328 0.5811 -0.0580 -0.0272 0.0292 335 PHE A CZ 2511 N N . LEU A 359 ? 0.4550 0.8395 0.6055 -0.0296 -0.0031 0.0138 336 LEU A N 2512 C CA . LEU A 359 ? 0.4861 0.8690 0.6381 -0.0159 -0.0012 0.0108 336 LEU A CA 2513 C C . LEU A 359 ? 0.5624 0.9679 0.7197 -0.0105 0.0011 0.0052 336 LEU A C 2514 O O . LEU A 359 ? 0.5117 0.9258 0.6725 -0.0015 0.0006 0.0031 336 LEU A O 2515 C CB . LEU A 359 ? 0.4099 0.7684 0.5587 -0.0095 0.0010 0.0102 336 LEU A CB 2516 C CG . LEU A 359 ? 0.4269 0.7795 0.5771 0.0043 0.0019 0.0084 336 LEU A CG 2517 C CD1 . LEU A 359 ? 0.3748 0.7272 0.5240 0.0071 -0.0012 0.0120 336 LEU A CD1 2518 C CD2 . LEU A 359 ? 0.4737 0.8023 0.6214 0.0088 0.0040 0.0084 336 LEU A CD2 2519 N N . SER A 360 ? 0.4743 0.8896 0.6322 -0.0158 0.0034 0.0025 337 SER A N 2520 C CA . SER A 360 ? 0.5005 0.9397 0.6638 -0.0113 0.0059 -0.0038 337 SER A CA 2521 C C . SER A 360 ? 0.5066 0.9707 0.6741 -0.0140 0.0039 -0.0032 337 SER A C 2522 O O . SER A 360 ? 0.4177 0.8985 0.5907 -0.0058 0.0048 -0.0085 337 SER A O 2523 C CB . SER A 360 ? 0.4825 0.9290 0.6446 -0.0183 0.0086 -0.0063 337 SER A CB 2524 O OG . SER A 360 ? 0.5721 0.9958 0.7311 -0.0150 0.0103 -0.0075 337 SER A OG 2525 N N . VAL A 361 ? 0.4926 0.9588 0.6584 -0.0255 0.0008 0.0029 338 VAL A N 2526 C CA . VAL A 361 ? 0.4825 0.9704 0.6526 -0.0292 -0.0017 0.0044 338 VAL A CA 2527 C C . VAL A 361 ? 0.5775 1.0626 0.7499 -0.0180 -0.0035 0.0035 338 VAL A C 2528 O O . VAL A 361 ? 0.5811 1.0866 0.7591 -0.0132 -0.0036 0.0000 338 VAL A O 2529 C CB . VAL A 361 ? 0.4794 0.9653 0.6479 -0.0433 -0.0061 0.0117 338 VAL A CB 2530 C CG1 . VAL A 361 ? 0.4307 0.9351 0.6043 -0.0457 -0.0097 0.0137 338 VAL A CG1 2531 C CG2 . VAL A 361 ? 0.5341 1.0274 0.7011 -0.0555 -0.0052 0.0134 338 VAL A CG2 2532 N N . MET A 362 ? 0.6180 1.0783 0.7860 -0.0140 -0.0050 0.0064 339 MET A N 2533 C CA . MET A 362 ? 0.5105 0.9657 0.6793 -0.0038 -0.0071 0.0066 339 MET A CA 2534 C C . MET A 362 ? 0.4301 0.8914 0.6030 0.0093 -0.0049 0.0004 339 MET A C 2535 O O . MET A 362 ? 0.4559 0.9281 0.6328 0.0162 -0.0068 -0.0013 339 MET A O 2536 C CB . MET A 362 ? 0.4307 0.8583 0.5932 -0.0023 -0.0083 0.0107 339 MET A CB 2537 C CG . MET A 362 ? 0.4792 0.8998 0.6388 -0.0140 -0.0116 0.0159 339 MET A CG 2538 S SD . MET A 362 ? 0.4470 0.8382 0.5999 -0.0115 -0.0128 0.0194 339 MET A SD 2539 C CE . MET A 362 ? 0.4192 0.8133 0.5726 0.0007 -0.0146 0.0195 339 MET A CE 2540 N N . GLU A 363 ? 0.5110 0.9652 0.6835 0.0127 -0.0016 -0.0033 340 GLU A N 2541 C CA . GLU A 363 ? 0.6177 1.0756 0.7952 0.0255 -0.0004 -0.0099 340 GLU A CA 2542 C C . GLU A 363 ? 0.6135 1.1021 0.7987 0.0269 0.0004 -0.0164 340 GLU A C 2543 O O . GLU A 363 ? 0.5511 1.0477 0.7423 0.0378 -0.0008 -0.0214 340 GLU A O 2544 C CB . GLU A 363 ? 0.6312 1.0735 0.8072 0.0284 0.0025 -0.0126 340 GLU A CB 2545 C CG . GLU A 363 ? 0.7388 1.1508 0.9086 0.0298 0.0018 -0.0072 340 GLU A CG 2546 C CD . GLU A 363 ? 0.8187 1.2153 0.9877 0.0322 0.0045 -0.0098 340 GLU A CD 2547 O OE1 . GLU A 363 ? 0.8291 1.2382 1.0008 0.0301 0.0069 -0.0152 340 GLU A OE1 2548 O OE2 . GLU A 363 ? 0.8959 1.2687 1.0617 0.0361 0.0041 -0.0066 340 GLU A OE2 2549 N N . LYS A 364 ? 0.6619 1.1683 0.8473 0.0158 0.0020 -0.0164 341 LYS A N 2550 C CA . LYS A 364 ? 0.7331 1.2714 0.9256 0.0154 0.0030 -0.0220 341 LYS A CA 2551 C C . LYS A 364 ? 0.6771 1.2275 0.8734 0.0168 -0.0004 -0.0203 341 LYS A C 2552 O O . LYS A 364 ? 0.6234 1.1929 0.8270 0.0243 -0.0006 -0.0266 341 LYS A O 2553 C CB . LYS A 364 ? 0.8246 1.3791 1.0156 0.0015 0.0053 -0.0207 341 LYS A CB 2554 C CG . LYS A 364 ? 0.9529 1.5152 1.1450 0.0031 0.0094 -0.0277 341 LYS A CG 2555 C CD . LYS A 364 ? 1.0861 1.6693 1.2870 0.0149 0.0106 -0.0381 341 LYS A CD 2556 C CE . LYS A 364 ? 1.0933 1.7087 1.3000 0.0106 0.0102 -0.0396 341 LYS A CE 2557 N NZ . LYS A 364 ? 1.0537 1.6890 1.2700 0.0230 0.0107 -0.0504 341 LYS A NZ 2558 N N . ALA A 365 ? 0.5453 1.0847 0.7371 0.0099 -0.0034 -0.0125 342 ALA A N 2559 C CA . ALA A 365 ? 0.4945 1.0434 0.6895 0.0110 -0.0071 -0.0104 342 ALA A CA 2560 C C . ALA A 365 ? 0.5606 1.1000 0.7572 0.0256 -0.0091 -0.0130 342 ALA A C 2561 O O . ALA A 365 ? 0.4271 0.9818 0.6295 0.0309 -0.0113 -0.0157 342 ALA A O 2562 C CB . ALA A 365 ? 0.3704 0.9077 0.5605 0.0009 -0.0105 -0.0021 342 ALA A CB 2563 N N . GLN A 366 ? 0.4883 1.0027 0.6803 0.0319 -0.0086 -0.0120 343 GLN A N 2564 C CA . GLN A 366 ? 0.5317 1.0350 0.7249 0.0453 -0.0109 -0.0134 343 GLN A CA 2565 C C . GLN A 366 ? 0.5498 1.0707 0.7521 0.0553 -0.0105 -0.0224 343 GLN A C 2566 O O . GLN A 366 ? 0.4900 1.0145 0.6967 0.0648 -0.0138 -0.0245 343 GLN A O 2567 C CB . GLN A 366 ? 0.4414 0.9151 0.6282 0.0489 -0.0102 -0.0101 343 GLN A CB 2568 C CG . GLN A 366 ? 0.4347 0.8951 0.6220 0.0616 -0.0132 -0.0096 343 GLN A CG 2569 C CD . GLN A 366 ? 0.5590 0.9906 0.7397 0.0634 -0.0126 -0.0049 343 GLN A CD 2570 O OE1 . GLN A 366 ? 0.6823 1.0993 0.8589 0.0679 -0.0153 0.0002 343 GLN A OE1 2571 N NE2 . GLN A 366 ? 0.4450 0.8689 0.6245 0.0599 -0.0091 -0.0065 343 GLN A NE2 2572 N N . LYS A 367 ? 0.6169 1.1492 0.8224 0.0533 -0.0069 -0.0282 344 LYS A N 2573 C CA . LYS A 367 ? 0.7043 1.2560 0.9194 0.0623 -0.0065 -0.0384 344 LYS A CA 2574 C C . LYS A 367 ? 0.6249 1.2066 0.8468 0.0606 -0.0074 -0.0418 344 LYS A C 2575 O O . LYS A 367 ? 0.6006 1.1945 0.8309 0.0709 -0.0096 -0.0486 344 LYS A O 2576 C CB . LYS A 367 ? 0.8187 1.3765 1.0350 0.0600 -0.0022 -0.0442 344 LYS A CB 2577 C CG . LYS A 367 ? 0.9149 1.4461 1.1284 0.0663 -0.0018 -0.0444 344 LYS A CG 2578 C CD . LYS A 367 ? 1.0881 1.6252 1.3115 0.0799 -0.0029 -0.0550 344 LYS A CD 2579 C CE . LYS A 367 ? 1.1817 1.7179 1.4111 0.0916 -0.0081 -0.0565 344 LYS A CE 2580 N NZ . LYS A 367 ? 1.1822 1.7248 1.4227 0.1049 -0.0104 -0.0675 344 LYS A NZ 2581 N N . MET A 368 ? 0.6067 1.2001 0.8258 0.0475 -0.0063 -0.0369 345 MET A N 2582 C CA . MET A 368 ? 0.5952 1.2170 0.8207 0.0440 -0.0072 -0.0388 345 MET A CA 2583 C C . MET A 368 ? 0.6062 1.2239 0.8338 0.0513 -0.0122 -0.0370 345 MET A C 2584 O O . MET A 368 ? 0.6398 1.2789 0.8756 0.0560 -0.0137 -0.0423 345 MET A O 2585 C CB . MET A 368 ? 0.5875 1.2186 0.8093 0.0275 -0.0061 -0.0321 345 MET A CB 2586 C CG . MET A 368 ? 0.6269 1.2654 0.8466 0.0187 -0.0015 -0.0333 345 MET A CG 2587 S SD . MET A 368 ? 1.7745 2.4202 1.9898 -0.0013 -0.0018 -0.0237 345 MET A SD 2588 C CE . MET A 368 ? 0.7230 1.3727 0.9346 -0.0084 0.0033 -0.0259 345 MET A CE 2589 N N . ASN A 369 ? 0.5547 1.1454 0.7747 0.0524 -0.0147 -0.0296 346 ASN A N 2590 C CA . ASN A 369 ? 0.5520 1.1368 0.7722 0.0587 -0.0196 -0.0268 346 ASN A CA 2591 C C . ASN A 369 ? 0.6368 1.1899 0.8480 0.0620 -0.0214 -0.0201 346 ASN A C 2592 O O . ASN A 369 ? 0.6938 1.2345 0.8978 0.0533 -0.0214 -0.0131 346 ASN A O 2593 C CB . ASN A 369 ? 0.5175 1.1176 0.7388 0.0493 -0.0215 -0.0229 346 ASN A CB 2594 C CG . ASN A 369 ? 0.6000 1.2043 0.8249 0.0570 -0.0265 -0.0232 346 ASN A CG 2595 O OD1 . ASN A 369 ? 0.4787 1.0629 0.6989 0.0642 -0.0295 -0.0199 346 ASN A OD1 2596 N ND2 . ASN A 369 ? 0.9451 1.5763 1.1784 0.0553 -0.0273 -0.0270 346 ASN A ND2 2597 N N . ASP A 370 ? 0.5942 1.1350 0.8066 0.0744 -0.0233 -0.0223 347 ASP A N 2598 C CA . ASP A 370 ? 0.6386 1.1503 0.8429 0.0780 -0.0248 -0.0158 347 ASP A CA 2599 C C . ASP A 370 ? 0.5275 1.0334 0.7271 0.0779 -0.0289 -0.0095 347 ASP A C 2600 O O . ASP A 370 ? 0.5266 1.0114 0.7178 0.0767 -0.0295 -0.0029 347 ASP A O 2601 C CB . ASP A 370 ? 0.5938 1.0948 0.8017 0.0909 -0.0263 -0.0196 347 ASP A CB 2602 C CG . ASP A 370 ? 0.5803 1.0514 0.7798 0.0934 -0.0271 -0.0125 347 ASP A CG 2603 O OD1 . ASP A 370 ? 0.7597 1.2177 0.9549 0.0885 -0.0235 -0.0108 347 ASP A OD1 2604 O OD2 . ASP A 370 ? 0.5411 1.0022 0.7384 0.1000 -0.0313 -0.0084 347 ASP A OD2 2605 N N . THR A 371 ? 0.5402 1.0658 0.7456 0.0793 -0.0317 -0.0120 348 THR A N 2606 C CA . THR A 371 ? 0.5793 1.1020 0.7813 0.0799 -0.0361 -0.0070 348 THR A CA 2607 C C . THR A 371 ? 0.4889 1.0077 0.6847 0.0675 -0.0354 -0.0013 348 THR A C 2608 O O . THR A 371 ? 0.4668 0.9707 0.6554 0.0671 -0.0377 0.0044 348 THR A O 2609 C CB . THR A 371 ? 0.5448 1.0911 0.7556 0.0839 -0.0394 -0.0118 348 THR A CB 2610 O OG1 . THR A 371 ? 0.6257 1.1783 0.8443 0.0949 -0.0402 -0.0188 348 THR A OG1 2611 C CG2 . THR A 371 ? 0.4959 1.0371 0.7030 0.0869 -0.0446 -0.0071 348 THR A CG2 2612 N N . ILE A 372 ? 0.4545 0.9872 0.6535 0.0574 -0.0327 -0.0029 349 ILE A N 2613 C CA . ILE A 372 ? 0.4648 0.9971 0.6605 0.0451 -0.0333 0.0019 349 ILE A CA 2614 C C . ILE A 372 ? 0.5507 1.0657 0.7399 0.0377 -0.0300 0.0051 349 ILE A C 2615 O O . ILE A 372 ? 0.6172 1.1190 0.8007 0.0318 -0.0315 0.0100 349 ILE A O 2616 C CB . ILE A 372 ? 0.4616 1.0209 0.6654 0.0369 -0.0336 -0.0004 349 ILE A CB 2617 C CG1 . ILE A 372 ? 0.4623 1.0334 0.6703 0.0395 -0.0387 -0.0002 349 ILE A CG1 2618 C CG2 . ILE A 372 ? 0.3396 0.8978 0.5412 0.0226 -0.0329 0.0037 349 ILE A CG2 2619 C CD1 . ILE A 372 ? 0.5494 1.1263 0.7616 0.0529 -0.0404 -0.0048 349 ILE A CD1 2620 N N . PHE A 373 ? 0.5875 1.1028 0.7780 0.0386 -0.0258 0.0015 350 PHE A N 2621 C CA . PHE A 373 ? 0.5208 1.0214 0.7060 0.0314 -0.0226 0.0039 350 PHE A CA 2622 C C . PHE A 373 ? 0.4876 0.9658 0.6680 0.0396 -0.0206 0.0039 350 PHE A C 2623 O O . PHE A 373 ? 0.5383 1.0044 0.7152 0.0354 -0.0176 0.0047 350 PHE A O 2624 C CB . PHE A 373 ? 0.4678 0.9858 0.6573 0.0237 -0.0192 0.0005 350 PHE A CB 2625 C CG . PHE A 373 ? 0.5003 1.0381 0.6938 0.0129 -0.0212 0.0023 350 PHE A CG 2626 C CD1 . PHE A 373 ? 0.5376 1.0673 0.7280 0.0044 -0.0248 0.0082 350 PHE A CD1 2627 C CD2 . PHE A 373 ? 0.4387 1.0038 0.6399 0.0112 -0.0200 -0.0021 350 PHE A CD2 2628 C CE1 . PHE A 373 ? 0.4911 1.0383 0.6863 -0.0058 -0.0276 0.0102 350 PHE A CE1 2629 C CE2 . PHE A 373 ? 0.4492 1.0329 0.6546 0.0006 -0.0221 0.0003 350 PHE A CE2 2630 C CZ . PHE A 373 ? 0.4606 1.0345 0.6632 -0.0080 -0.0262 0.0068 350 PHE A CZ 2631 N N . GLY A 374 ? 0.4784 0.9509 0.6591 0.0510 -0.0228 0.0036 351 GLY A N 2632 C CA . GLY A 374 ? 0.5115 0.9620 0.6882 0.0586 -0.0220 0.0049 351 GLY A CA 2633 C C . GLY A 374 ? 0.5465 0.9756 0.7140 0.0539 -0.0222 0.0117 351 GLY A C 2634 O O . GLY A 374 ? 0.5057 0.9347 0.6699 0.0517 -0.0252 0.0153 351 GLY A O 2635 N N . PHE A 375 ? 0.5306 0.9424 0.6943 0.0525 -0.0191 0.0128 352 PHE A N 2636 C CA . PHE A 375 ? 0.6112 1.0037 0.7668 0.0474 -0.0189 0.0184 352 PHE A CA 2637 C C . PHE A 375 ? 0.6436 1.0141 0.7953 0.0536 -0.0173 0.0207 352 PHE A C 2638 O O . PHE A 375 ? 0.5749 0.9436 0.7307 0.0605 -0.0163 0.0176 352 PHE A O 2639 C CB . PHE A 375 ? 0.5514 0.9443 0.7058 0.0350 -0.0170 0.0185 352 PHE A CB 2640 C CG . PHE A 375 ? 0.4489 0.8380 0.6049 0.0333 -0.0130 0.0154 352 PHE A CG 2641 C CD1 . PHE A 375 ? 0.5752 0.9828 0.7375 0.0331 -0.0115 0.0101 352 PHE A CD1 2642 C CD2 . PHE A 375 ? 0.4721 0.8399 0.6231 0.0318 -0.0107 0.0175 352 PHE A CD2 2643 C CE1 . PHE A 375 ? 0.4436 0.8488 0.6071 0.0317 -0.0079 0.0068 352 PHE A CE1 2644 C CE2 . PHE A 375 ? 0.5018 0.8659 0.6544 0.0305 -0.0073 0.0143 352 PHE A CE2 2645 C CZ . PHE A 375 ? 0.5322 0.9151 0.6908 0.0305 -0.0060 0.0089 352 PHE A CZ 2646 N N . THR A 376 ? 0.6908 1.0453 0.8351 0.0509 -0.0176 0.0259 353 THR A N 2647 C CA . THR A 376 ? 0.6232 0.9565 0.7633 0.0549 -0.0160 0.0292 353 THR A CA 2648 C C . THR A 376 ? 0.6356 0.9558 0.7713 0.0459 -0.0131 0.0305 353 THR A C 2649 O O . THR A 376 ? 0.6195 0.9402 0.7516 0.0387 -0.0141 0.0322 353 THR A O 2650 C CB . THR A 376 ? 0.5999 0.9254 0.7348 0.0608 -0.0188 0.0347 353 THR A CB 2651 O OG1 . THR A 376 ? 0.6865 1.0234 0.8258 0.0694 -0.0222 0.0335 353 THR A OG1 2652 C CG2 . THR A 376 ? 0.5857 0.8898 0.7166 0.0641 -0.0171 0.0389 353 THR A CG2 2653 N N . MET A 377 ? 0.5223 0.8309 0.6589 0.0466 -0.0101 0.0292 354 MET A N 2654 C CA . MET A 377 ? 0.5590 0.8538 0.6919 0.0388 -0.0075 0.0302 354 MET A CA 2655 C C . MET A 377 ? 0.5834 0.8571 0.7131 0.0432 -0.0058 0.0336 354 MET A C 2656 O O . MET A 377 ? 0.7105 0.9803 0.8431 0.0519 -0.0062 0.0338 354 MET A O 2657 C CB . MET A 377 ? 0.6284 0.9289 0.7653 0.0333 -0.0052 0.0254 354 MET A CB 2658 C CG . MET A 377 ? 0.6920 0.9954 0.8347 0.0408 -0.0038 0.0212 354 MET A CG 2659 S SD . MET A 377 ? 0.9533 1.2529 1.0977 0.0348 -0.0001 0.0170 354 MET A SD 2660 C CE . MET A 377 ? 0.7687 1.0396 0.9076 0.0340 0.0016 0.0213 354 MET A CE 2661 N N . GLU A 378 ? 0.6116 0.8720 0.7362 0.0371 -0.0044 0.0361 355 GLU A N 2662 C CA . GLU A 378 ? 0.5769 0.8175 0.6988 0.0397 -0.0023 0.0394 355 GLU A CA 2663 C C . GLU A 378 ? 0.6195 0.8495 0.7417 0.0329 0.0007 0.0370 355 GLU A C 2664 O O . GLU A 378 ? 0.5396 0.7743 0.6613 0.0244 0.0006 0.0347 355 GLU A O 2665 C CB . GLU A 378 ? 0.5935 0.8273 0.7084 0.0393 -0.0032 0.0449 355 GLU A CB 2666 C CG . GLU A 378 ? 0.7530 0.9959 0.8667 0.0462 -0.0065 0.0481 355 GLU A CG 2667 C CD . GLU A 378 ? 0.9028 1.1399 1.0089 0.0458 -0.0072 0.0537 355 GLU A CD 2668 O OE1 . GLU A 378 ? 0.9013 1.1251 1.0037 0.0419 -0.0047 0.0556 355 GLU A OE1 2669 O OE2 . GLU A 378 ? 1.0034 1.2501 1.1073 0.0492 -0.0102 0.0558 355 GLU A OE2 2670 N N . GLU A 379 ? 0.7560 0.9714 0.8796 0.0367 0.0028 0.0374 356 GLU A N 2671 C CA . GLU A 379 ? 0.8139 1.0180 0.9380 0.0311 0.0055 0.0351 356 GLU A CA 2672 C C . GLU A 379 ? 0.6952 0.8857 0.8137 0.0255 0.0065 0.0384 356 GLU A C 2673 O O . GLU A 379 ? 0.7401 0.9204 0.8556 0.0292 0.0070 0.0431 356 GLU A O 2674 C CB . GLU A 379 ? 1.0225 1.2164 1.1512 0.0378 0.0069 0.0336 356 GLU A CB 2675 C CG . GLU A 379 ? 1.1993 1.3868 1.3301 0.0328 0.0093 0.0292 356 GLU A CG 2676 C CD . GLU A 379 ? 1.2148 1.4199 1.3483 0.0286 0.0091 0.0238 356 GLU A CD 2677 O OE1 . GLU A 379 ? 1.2195 1.4402 1.3567 0.0338 0.0077 0.0215 356 GLU A OE1 2678 O OE2 . GLU A 379 ? 1.1588 1.3625 1.2908 0.0200 0.0100 0.0220 356 GLU A OE2 2679 N N . ARG A 380 ? 0.6160 0.8072 0.7334 0.0164 0.0066 0.0358 357 ARG A N 2680 C CA . ARG A 380 ? 0.6814 0.8607 0.7948 0.0106 0.0073 0.0372 357 ARG A CA 2681 C C . ARG A 380 ? 0.7108 0.8772 0.8261 0.0060 0.0095 0.0344 357 ARG A C 2682 O O . ARG A 380 ? 0.6544 0.8222 0.7734 0.0070 0.0103 0.0314 357 ARG A O 2683 C CB . ARG A 380 ? 0.6469 0.8367 0.7587 0.0037 0.0043 0.0361 357 ARG A CB 2684 C CG . ARG A 380 ? 0.6643 0.8664 0.7739 0.0078 0.0018 0.0387 357 ARG A CG 2685 C CD . ARG A 380 ? 0.7149 0.9086 0.8192 0.0110 0.0027 0.0431 357 ARG A CD 2686 N NE . ARG A 380 ? 0.8368 1.0430 0.9382 0.0131 -0.0002 0.0449 357 ARG A NE 2687 C CZ . ARG A 380 ? 0.8379 1.0505 0.9384 0.0208 -0.0012 0.0483 357 ARG A CZ 2688 N NH1 . ARG A 380 ? 0.8148 1.0222 0.9176 0.0273 0.0002 0.0500 357 ARG A NH1 2689 N NH2 . ARG A 380 ? 0.8687 1.0926 0.9663 0.0222 -0.0041 0.0496 357 ARG A NH2 2690 N N . SER A 381 ? 0.7064 0.8610 0.8193 0.0010 0.0103 0.0347 358 SER A N 2691 C CA . SER A 381 ? 0.6114 0.7530 0.7259 -0.0040 0.0119 0.0318 358 SER A CA 2692 C C . SER A 381 ? 0.5636 0.7136 0.6805 -0.0114 0.0096 0.0277 358 SER A C 2693 O O . SER A 381 ? 0.6011 0.7464 0.7203 -0.0133 0.0107 0.0250 358 SER A O 2694 C CB . SER A 381 ? 0.5657 0.6948 0.6776 -0.0081 0.0127 0.0325 358 SER A CB 2695 O OG . SER A 381 ? 0.6376 0.7538 0.7516 -0.0129 0.0138 0.0293 358 SER A OG 2696 N N . TRP A 382 ? 0.5938 0.7567 0.7101 -0.0156 0.0061 0.0275 359 TRP A N 2697 C CA . TRP A 382 ? 0.5422 0.7145 0.6609 -0.0234 0.0031 0.0248 359 TRP A CA 2698 C C . TRP A 382 ? 0.5374 0.7232 0.6586 -0.0204 0.0038 0.0240 359 TRP A C 2699 O O . TRP A 382 ? 0.5081 0.7000 0.6313 -0.0263 0.0026 0.0220 359 TRP A O 2700 C CB . TRP A 382 ? 0.4593 0.6418 0.5780 -0.0285 -0.0016 0.0250 359 TRP A CB 2701 C CG . TRP A 382 ? 0.3961 0.5682 0.5146 -0.0352 -0.0039 0.0233 359 TRP A CG 2702 C CD1 . TRP A 382 ? 0.4326 0.5984 0.5486 -0.0334 -0.0036 0.0237 359 TRP A CD1 2703 C CD2 . TRP A 382 ? 0.4070 0.5748 0.5284 -0.0448 -0.0074 0.0205 359 TRP A CD2 2704 N NE1 . TRP A 382 ? 0.4654 0.6237 0.5832 -0.0408 -0.0066 0.0204 359 TRP A NE1 2705 C CE2 . TRP A 382 ? 0.4634 0.6219 0.5848 -0.0479 -0.0093 0.0186 359 TRP A CE2 2706 C CE3 . TRP A 382 ? 0.4166 0.5882 0.5407 -0.0512 -0.0094 0.0196 359 TRP A CE3 2707 C CZ2 . TRP A 382 ? 0.5196 0.6713 0.6444 -0.0568 -0.0137 0.0153 359 TRP A CZ2 2708 C CZ3 . TRP A 382 ? 0.4337 0.5980 0.5603 -0.0605 -0.0138 0.0174 359 TRP A CZ3 2709 C CH2 . TRP A 382 ? 0.4511 0.6050 0.5784 -0.0630 -0.0162 0.0151 359 TRP A CH2 2710 N N . GLY A 383 ? 0.5770 0.7681 0.6982 -0.0111 0.0054 0.0256 360 GLY A N 2711 C CA . GLY A 383 ? 0.4885 0.6940 0.6129 -0.0070 0.0059 0.0238 360 GLY A CA 2712 C C . GLY A 383 ? 0.4976 0.7173 0.6223 -0.0012 0.0043 0.0256 360 GLY A C 2713 O O . GLY A 383 ? 0.4568 0.6722 0.5786 0.0020 0.0036 0.0287 360 GLY A O 2714 N N . PRO A 384 ? 0.4986 0.7360 0.6267 0.0002 0.0037 0.0234 361 PRO A N 2715 C CA . PRO A 384 ? 0.5028 0.7556 0.6322 0.0057 0.0019 0.0243 361 PRO A CA 2716 C C . PRO A 384 ? 0.3845 0.6437 0.5119 0.0005 -0.0016 0.0266 361 PRO A C 2717 O O . PRO A 384 ? 0.3745 0.6403 0.5028 -0.0086 -0.0037 0.0258 361 PRO A O 2718 C CB . PRO A 384 ? 0.3778 0.6492 0.5119 0.0052 0.0022 0.0204 361 PRO A CB 2719 C CG . PRO A 384 ? 0.4248 0.6878 0.5599 0.0038 0.0050 0.0174 361 PRO A CG 2720 C CD . PRO A 384 ? 0.3634 0.6079 0.4946 -0.0029 0.0050 0.0196 361 PRO A CD 2721 N N . TYR A 385 ? 0.4451 0.7022 0.5698 0.0062 -0.0026 0.0295 362 TYR A N 2722 C CA . TYR A 385 ? 0.3762 0.6397 0.4991 0.0026 -0.0062 0.0311 362 TYR A CA 2723 C C . TYR A 385 ? 0.4796 0.7593 0.6042 0.0088 -0.0082 0.0316 362 TYR A C 2724 O O . TYR A 385 ? 0.4844 0.7622 0.6084 0.0180 -0.0072 0.0330 362 TYR A O 2725 C CB . TYR A 385 ? 0.4259 0.6744 0.5436 0.0032 -0.0059 0.0337 362 TYR A CB 2726 C CG . TYR A 385 ? 0.4899 0.7451 0.6059 0.0001 -0.0098 0.0343 362 TYR A CG 2727 C CD1 . TYR A 385 ? 0.4007 0.6563 0.5182 -0.0092 -0.0127 0.0322 362 TYR A CD1 2728 C CD2 . TYR A 385 ? 0.4742 0.7349 0.5873 0.0068 -0.0111 0.0369 362 TYR A CD2 2729 C CE1 . TYR A 385 ? 0.3629 0.6249 0.4799 -0.0116 -0.0170 0.0318 362 TYR A CE1 2730 C CE2 . TYR A 385 ? 0.5125 0.7801 0.6242 0.0044 -0.0148 0.0368 362 TYR A CE2 2731 C CZ . TYR A 385 ? 0.5079 0.7763 0.6219 -0.0046 -0.0178 0.0339 362 TYR A CZ 2732 O OH . TYR A 385 ? 0.5121 0.7876 0.6258 -0.0065 -0.0222 0.0328 362 TYR A OH 2733 N N . ILE A 386 ? 0.4345 0.7295 0.5616 0.0038 -0.0117 0.0307 363 ILE A N 2734 C CA . ILE A 386 ? 0.3592 0.6707 0.4886 0.0091 -0.0140 0.0307 363 ILE A CA 2735 C C . ILE A 386 ? 0.4252 0.7347 0.5504 0.0127 -0.0165 0.0335 363 ILE A C 2736 O O . ILE A 386 ? 0.4421 0.7521 0.5662 0.0068 -0.0195 0.0336 363 ILE A O 2737 C CB . ILE A 386 ? 0.4087 0.7389 0.5433 0.0019 -0.0168 0.0288 363 ILE A CB 2738 C CG1 . ILE A 386 ? 0.3814 0.7150 0.5193 -0.0031 -0.0143 0.0264 363 ILE A CG1 2739 C CG2 . ILE A 386 ? 0.3345 0.6824 0.4724 0.0080 -0.0188 0.0283 363 ILE A CG2 2740 C CD1 . ILE A 386 ? 0.4039 0.7381 0.5433 0.0054 -0.0104 0.0242 363 ILE A CD1 2741 N N . THR A 387 ? 0.4219 0.7294 0.5451 0.0224 -0.0159 0.0355 364 THR A N 2742 C CA . THR A 387 ? 0.4254 0.7312 0.5437 0.0264 -0.0180 0.0387 364 THR A CA 2743 C C . THR A 387 ? 0.4779 0.8010 0.5986 0.0305 -0.0218 0.0383 364 THR A C 2744 O O . THR A 387 ? 0.5045 0.8329 0.6231 0.0291 -0.0251 0.0390 364 THR A O 2745 C CB . THR A 387 ? 0.4363 0.7277 0.5500 0.0341 -0.0157 0.0427 364 THR A CB 2746 O OG1 . THR A 387 ? 0.4677 0.7627 0.5855 0.0418 -0.0154 0.0422 364 THR A OG1 2747 C CG2 . THR A 387 ? 0.3867 0.6604 0.4980 0.0301 -0.0121 0.0432 364 THR A CG2 2748 N N . CYS A 388 ? 0.4449 0.7773 0.5706 0.0357 -0.0215 0.0366 365 CYS A N 2749 C CA . CYS A 388 ? 0.5449 0.8936 0.6736 0.0406 -0.0250 0.0359 365 CYS A CA 2750 C C . CYS A 388 ? 0.5154 0.8812 0.6521 0.0390 -0.0251 0.0315 365 CYS A C 2751 O O . CYS A 388 ? 0.4808 0.8455 0.6207 0.0388 -0.0220 0.0291 365 CYS A O 2752 C CB . CYS A 388 ? 0.4936 0.8376 0.6200 0.0516 -0.0258 0.0388 365 CYS A CB 2753 S SG . CYS A 388 ? 0.6188 0.9424 0.7355 0.0540 -0.0249 0.0451 365 CYS A SG 2754 N N . ILE A 389 ? 0.5028 0.8853 0.6430 0.0377 -0.0287 0.0303 366 ILE A N 2755 C CA . ILE A 389 ? 0.4941 0.8962 0.6423 0.0376 -0.0291 0.0264 366 ILE A CA 2756 C C . ILE A 389 ? 0.4303 0.8449 0.5807 0.0444 -0.0331 0.0262 366 ILE A C 2757 O O . ILE A 389 ? 0.4621 0.8766 0.6094 0.0436 -0.0365 0.0283 366 ILE A O 2758 C CB . ILE A 389 ? 0.4932 0.9055 0.6452 0.0258 -0.0297 0.0251 366 ILE A CB 2759 C CG1 . ILE A 389 ? 0.5072 0.9071 0.6571 0.0189 -0.0262 0.0253 366 ILE A CG1 2760 C CG2 . ILE A 389 ? 0.3693 0.8043 0.5295 0.0253 -0.0301 0.0215 366 ILE A CG2 2761 C CD1 . ILE A 389 ? 0.4436 0.8529 0.5974 0.0069 -0.0273 0.0247 366 ILE A CD1 2762 N N . GLN A 390 ? 0.4992 0.9246 0.6552 0.0516 -0.0330 0.0230 367 GLN A N 2763 C CA . GLN A 390 ? 0.4770 0.9143 0.6360 0.0591 -0.0370 0.0222 367 GLN A CA 2764 C C . GLN A 390 ? 0.4576 0.8815 0.6092 0.0661 -0.0396 0.0268 367 GLN A C 2765 O O . GLN A 390 ? 0.4228 0.8544 0.5742 0.0694 -0.0437 0.0276 367 GLN A O 2766 C CB . GLN A 390 ? 0.5844 1.0397 0.7477 0.0527 -0.0402 0.0210 367 GLN A CB 2767 C CG . GLN A 390 ? 0.5904 1.0629 0.7615 0.0456 -0.0384 0.0171 367 GLN A CG 2768 C CD . GLN A 390 ? 0.4930 0.9828 0.6691 0.0391 -0.0422 0.0168 367 GLN A CD 2769 O OE1 . GLN A 390 ? 0.5130 1.0031 0.6876 0.0415 -0.0465 0.0184 367 GLN A OE1 2770 N NE2 . GLN A 390 ? 0.4932 0.9980 0.6756 0.0307 -0.0410 0.0149 367 GLN A NE2 2771 N N . GLY A 391 ? 0.5003 0.9050 0.6460 0.0681 -0.0372 0.0301 368 GLY A N 2772 C CA . GLY A 391 ? 0.4527 0.8446 0.5907 0.0737 -0.0392 0.0355 368 GLY A CA 2773 C C . GLY A 391 ? 0.5526 0.9401 0.6836 0.0672 -0.0400 0.0385 368 GLY A C 2774 O O . GLY A 391 ? 0.5878 0.9656 0.7113 0.0704 -0.0411 0.0431 368 GLY A O 2775 N N . LEU A 392 ? 0.5630 0.9581 0.6968 0.0581 -0.0398 0.0357 369 LEU A N 2776 C CA . LEU A 392 ? 0.5812 0.9727 0.7102 0.0516 -0.0413 0.0371 369 LEU A CA 2777 C C . LEU A 392 ? 0.5660 0.9409 0.6908 0.0460 -0.0373 0.0384 369 LEU A C 2778 O O . LEU A 392 ? 0.4884 0.8630 0.6171 0.0393 -0.0351 0.0361 369 LEU A O 2779 C CB . LEU A 392 ? 0.4332 0.8406 0.5687 0.0444 -0.0445 0.0337 369 LEU A CB 2780 C CG . LEU A 392 ? 0.5246 0.9291 0.6577 0.0369 -0.0470 0.0336 369 LEU A CG 2781 C CD1 . LEU A 392 ? 0.4315 0.8333 0.5576 0.0423 -0.0498 0.0357 369 LEU A CD1 2782 C CD2 . LEU A 392 ? 0.5202 0.9400 0.6616 0.0295 -0.0508 0.0306 369 LEU A CD2 2783 N N . CYS A 393 ? 0.5166 0.8782 0.6333 0.0485 -0.0366 0.0422 370 CYS A N 2784 C CA . CYS A 393 ? 0.4543 0.7993 0.5670 0.0442 -0.0326 0.0436 370 CYS A CA 2785 C C . CYS A 393 ? 0.5112 0.8535 0.6206 0.0370 -0.0338 0.0427 370 CYS A C 2786 O O . CYS A 393 ? 0.5413 0.8900 0.6479 0.0382 -0.0374 0.0429 370 CYS A O 2787 C CB . CYS A 393 ? 0.4207 0.7520 0.5273 0.0514 -0.0305 0.0486 370 CYS A CB 2788 S SG . CYS A 393 ? 0.6367 0.9696 0.7486 0.0609 -0.0304 0.0489 370 CYS A SG 2789 N N . ALA A 394 ? 0.4462 0.7793 0.5565 0.0299 -0.0313 0.0412 371 ALA A N 2790 C CA . ALA A 394 ? 0.4881 0.8168 0.5964 0.0230 -0.0326 0.0395 371 ALA A CA 2791 C C . ALA A 394 ? 0.5874 0.9085 0.6872 0.0269 -0.0318 0.0426 371 ALA A C 2792 O O . ALA A 394 ? 0.5500 0.8617 0.6451 0.0323 -0.0285 0.0469 371 ALA A O 2793 C CB . ALA A 394 ? 0.3912 0.7091 0.5018 0.0156 -0.0298 0.0378 371 ALA A CB 2794 N N . ASN A 395 ? 0.5122 0.8381 0.6104 0.0241 -0.0352 0.0403 372 ASN A N 2795 C CA . ASN A 395 ? 0.4977 0.8194 0.5874 0.0270 -0.0344 0.0427 372 ASN A CA 2796 C C . ASN A 395 ? 0.5456 0.8629 0.6349 0.0202 -0.0349 0.0386 372 ASN A C 2797 O O . ASN A 395 ? 0.6372 0.9617 0.7324 0.0149 -0.0394 0.0333 372 ASN A O 2798 C CB . ASN A 395 ? 0.4614 0.7963 0.5482 0.0329 -0.0385 0.0437 372 ASN A CB 2799 C CG . ASN A 395 ? 0.6255 0.9574 0.7023 0.0364 -0.0373 0.0473 372 ASN A CG 2800 O OD1 . ASN A 395 ? 0.5624 0.8988 0.6370 0.0336 -0.0393 0.0439 372 ASN A OD1 2801 N ND2 . ASN A 395 ? 0.6807 1.0059 0.7520 0.0423 -0.0345 0.0540 372 ASN A ND2 2802 N N . ASN A 396 ? 0.4860 0.7917 0.5692 0.0203 -0.0307 0.0409 373 ASN A N 2803 C CA . ASN A 396 ? 0.6091 0.9100 0.6923 0.0142 -0.0307 0.0365 373 ASN A CA 2804 C C . ASN A 396 ? 0.5549 0.8677 0.6361 0.0144 -0.0351 0.0326 373 ASN A C 2805 O O . ASN A 396 ? 0.5186 0.8352 0.6055 0.0090 -0.0393 0.0259 373 ASN A O 2806 C CB . ASN A 396 ? 0.7411 1.0273 0.8185 0.0144 -0.0247 0.0402 373 ASN A CB 2807 C CG . ASN A 396 ? 1.0280 1.3046 1.1092 0.0069 -0.0237 0.0353 373 ASN A CG 2808 O OD1 . ASN A 396 ? 1.0127 1.2946 1.0974 0.0023 -0.0277 0.0289 373 ASN A OD1 2809 N ND2 . ASN A 396 ? 1.1250 1.3873 1.2062 0.0059 -0.0189 0.0378 373 ASN A ND2 2810 N N . ASN A 397 ? 0.5952 0.9142 0.6687 0.0208 -0.0348 0.0367 374 ASN A N 2811 C CA . ASN A 397 ? 0.5765 0.9084 0.6472 0.0219 -0.0389 0.0330 374 ASN A CA 2812 C C . ASN A 397 ? 0.5577 0.9029 0.6363 0.0211 -0.0459 0.0277 374 ASN A C 2813 O O . ASN A 397 ? 0.5495 0.9033 0.6310 0.0189 -0.0507 0.0210 374 ASN A O 2814 C CB . ASN A 397 ? 0.6992 1.0353 0.7593 0.0289 -0.0372 0.0396 374 ASN A CB 2815 C CG . ASN A 397 ? 0.7840 1.1104 0.8360 0.0282 -0.0314 0.0438 374 ASN A CG 2816 O OD1 . ASN A 397 ? 0.7589 1.0821 0.8119 0.0232 -0.0301 0.0389 374 ASN A OD1 2817 N ND2 . ASN A 397 ? 0.8321 1.1539 0.8768 0.0333 -0.0284 0.0529 374 ASN A ND2 2818 N N . ASP A 398 ? 0.4251 0.7724 0.5080 0.0230 -0.0467 0.0303 375 ASP A N 2819 C CA . ASP A 398 ? 0.5023 0.8621 0.5938 0.0217 -0.0532 0.0260 375 ASP A CA 2820 C C . ASP A 398 ? 0.5476 0.9038 0.6489 0.0129 -0.0557 0.0208 375 ASP A C 2821 O O . ASP A 398 ? 0.6159 0.9818 0.7257 0.0099 -0.0618 0.0168 375 ASP A O 2822 C CB . ASP A 398 ? 0.5901 0.9547 0.6831 0.0266 -0.0530 0.0303 375 ASP A CB 2823 C CG . ASP A 398 ? 0.6520 1.0212 0.7364 0.0353 -0.0525 0.0353 375 ASP A CG 2824 O OD1 . ASP A 398 ? 0.6952 1.0698 0.7738 0.0372 -0.0542 0.0342 375 ASP A OD1 2825 O OD2 . ASP A 398 ? 0.6107 0.9786 0.6944 0.0402 -0.0506 0.0400 375 ASP A OD2 2826 N N . ARG A 399 ? 0.6093 0.9517 0.7099 0.0087 -0.0514 0.0211 376 ARG A N 2827 C CA . ARG A 399 ? 0.6812 1.0181 0.7903 0.0001 -0.0537 0.0169 376 ARG A CA 2828 C C . ARG A 399 ? 0.6411 0.9827 0.7578 -0.0026 -0.0555 0.0182 376 ARG A C 2829 O O . ARG A 399 ? 0.6023 0.9477 0.7279 -0.0094 -0.0611 0.0145 376 ARG A O 2830 C CB . ARG A 399 ? 0.7451 1.0877 0.8595 -0.0041 -0.0606 0.0092 376 ARG A CB 2831 C CG . ARG A 399 ? 0.7737 1.1168 0.8807 -0.0007 -0.0591 0.0070 376 ARG A CG 2832 C CD . ARG A 399 ? 0.8034 1.1535 0.9169 -0.0042 -0.0665 -0.0022 376 ARG A CD 2833 N NE . ARG A 399 ? 0.9070 1.2462 1.0261 -0.0115 -0.0674 -0.0069 376 ARG A NE 2834 C CZ . ARG A 399 ? 0.8320 1.1701 0.9625 -0.0185 -0.0741 -0.0112 376 ARG A CZ 2835 N NH1 . ARG A 399 ? 0.9589 1.3068 1.0966 -0.0195 -0.0803 -0.0112 376 ARG A NH1 2836 N NH2 . ARG A 399 ? 0.5840 0.9112 0.7191 -0.0247 -0.0751 -0.0153 376 ARG A NH2 2837 N N . THR A 400 ? 0.5756 0.9176 0.6891 0.0026 -0.0512 0.0234 377 THR A N 2838 C CA . THR A 400 ? 0.4763 0.8250 0.5963 0.0009 -0.0521 0.0246 377 THR A CA 2839 C C . THR A 400 ? 0.4475 0.7854 0.5668 -0.0003 -0.0461 0.0274 377 THR A C 2840 O O . THR A 400 ? 0.4424 0.7690 0.5551 0.0035 -0.0408 0.0301 377 THR A O 2841 C CB . THR A 400 ? 0.4648 0.8258 0.5836 0.0087 -0.0529 0.0270 377 THR A CB 2842 O OG1 . THR A 400 ? 0.4464 0.8003 0.5569 0.0164 -0.0475 0.0316 377 THR A OG1 2843 C CG2 . THR A 400 ? 0.4356 0.8080 0.5549 0.0107 -0.0590 0.0241 377 THR A CG2 2844 N N . TYR A 401 ? 0.4401 0.7823 0.5664 -0.0058 -0.0472 0.0268 378 TYR A N 2845 C CA . TYR A 401 ? 0.4362 0.7703 0.5623 -0.0070 -0.0419 0.0287 378 TYR A CA 2846 C C . TYR A 401 ? 0.4398 0.7854 0.5732 -0.0113 -0.0433 0.0285 378 TYR A C 2847 O O . TYR A 401 ? 0.3763 0.7345 0.5158 -0.0152 -0.0488 0.0271 378 TYR A O 2848 C CB . TYR A 401 ? 0.3758 0.6945 0.5010 -0.0131 -0.0403 0.0273 378 TYR A CB 2849 C CG . TYR A 401 ? 0.4705 0.7909 0.6031 -0.0236 -0.0456 0.0244 378 TYR A CG 2850 C CD1 . TYR A 401 ? 0.4748 0.8006 0.6113 -0.0269 -0.0525 0.0211 378 TYR A CD1 2851 C CD2 . TYR A 401 ? 0.4466 0.7631 0.5826 -0.0302 -0.0444 0.0248 378 TYR A CD2 2852 C CE1 . TYR A 401 ? 0.5270 0.8534 0.6713 -0.0366 -0.0587 0.0187 378 TYR A CE1 2853 C CE2 . TYR A 401 ? 0.5125 0.8301 0.6554 -0.0403 -0.0501 0.0230 378 TYR A CE2 2854 C CZ . TYR A 401 ? 0.5960 0.9180 0.7434 -0.0435 -0.0575 0.0201 378 TYR A CZ 2855 O OH . TYR A 401 ? 0.4992 0.8213 0.6545 -0.0537 -0.0644 0.0186 378 TYR A OH 2856 N N . TRP A 402 ? 0.3730 0.7152 0.5063 -0.0106 -0.0384 0.0297 379 TRP A N 2857 C CA . TRP A 402 ? 0.3961 0.7499 0.5357 -0.0155 -0.0388 0.0294 379 TRP A CA 2858 C C . TRP A 402 ? 0.4882 0.8352 0.6306 -0.0262 -0.0398 0.0287 379 TRP A C 2859 O O . TRP A 402 ? 0.3413 0.6732 0.4801 -0.0271 -0.0363 0.0287 379 TRP A O 2860 C CB . TRP A 402 ? 0.3313 0.6876 0.4699 -0.0085 -0.0334 0.0301 379 TRP A CB 2861 C CG . TRP A 402 ? 0.4510 0.8161 0.5886 0.0015 -0.0336 0.0307 379 TRP A CG 2862 C CD1 . TRP A 402 ? 0.4317 0.7880 0.5636 0.0108 -0.0313 0.0325 379 TRP A CD1 2863 C CD2 . TRP A 402 ? 0.4751 0.8592 0.6180 0.0029 -0.0369 0.0298 379 TRP A CD2 2864 N NE1 . TRP A 402 ? 0.5150 0.8832 0.6480 0.0181 -0.0332 0.0327 379 TRP A NE1 2865 C CE2 . TRP A 402 ? 0.4921 0.8776 0.6319 0.0137 -0.0364 0.0307 379 TRP A CE2 2866 C CE3 . TRP A 402 ? 0.4150 0.8154 0.5652 -0.0041 -0.0404 0.0287 379 TRP A CE3 2867 C CZ2 . TRP A 402 ? 0.5421 0.9443 0.6860 0.0180 -0.0393 0.0298 379 TRP A CZ2 2868 C CZ3 . TRP A 402 ? 0.3971 0.8146 0.5515 0.0000 -0.0429 0.0279 379 TRP A CZ3 2869 C CH2 . TRP A 402 ? 0.4325 0.8507 0.5839 0.0112 -0.0423 0.0282 379 TRP A CH2 2870 N N . GLU A 403 ? 0.4649 0.8230 0.6141 -0.0346 -0.0452 0.0284 380 GLU A N 2871 C CA . GLU A 403 ? 0.3721 0.7247 0.5249 -0.0458 -0.0479 0.0283 380 GLU A CA 2872 C C . GLU A 403 ? 0.4537 0.8169 0.6099 -0.0510 -0.0461 0.0298 380 GLU A C 2873 O O . GLU A 403 ? 0.4264 0.8071 0.5863 -0.0500 -0.0467 0.0304 380 GLU A O 2874 C CB . GLU A 403 ? 0.4488 0.8050 0.6075 -0.0527 -0.0566 0.0272 380 GLU A CB 2875 C CG . GLU A 403 ? 0.4550 0.8038 0.6182 -0.0644 -0.0611 0.0273 380 GLU A CG 2876 C CD . GLU A 403 ? 0.5320 0.8860 0.7033 -0.0711 -0.0710 0.0260 380 GLU A CD 2877 O OE1 . GLU A 403 ? 0.5090 0.8538 0.6842 -0.0796 -0.0763 0.0252 380 GLU A OE1 2878 O OE2 . GLU A 403 ? 0.5752 0.9423 0.7495 -0.0677 -0.0742 0.0257 380 GLU A OE2 2879 N N . LEU A 404 ? 0.3957 0.7490 0.5506 -0.0566 -0.0440 0.0302 381 LEU A N 2880 C CA . LEU A 404 ? 0.3967 0.7604 0.5540 -0.0623 -0.0421 0.0315 381 LEU A CA 2881 C C . LEU A 404 ? 0.4165 0.7843 0.5798 -0.0758 -0.0490 0.0336 381 LEU A C 2882 O O . LEU A 404 ? 0.4204 0.7741 0.5841 -0.0816 -0.0530 0.0334 381 LEU A O 2883 C CB . LEU A 404 ? 0.3599 0.7113 0.5123 -0.0600 -0.0357 0.0307 381 LEU A CB 2884 C CG . LEU A 404 ? 0.4549 0.7973 0.6018 -0.0473 -0.0297 0.0291 381 LEU A CG 2885 C CD1 . LEU A 404 ? 0.3686 0.6999 0.5123 -0.0461 -0.0242 0.0281 381 LEU A CD1 2886 C CD2 . LEU A 404 ? 0.4346 0.7932 0.5829 -0.0387 -0.0281 0.0286 381 LEU A CD2 2887 N N . LEU A 405 ? 0.4045 0.7921 0.5730 -0.0810 -0.0510 0.0356 382 LEU A N 2888 C CA . LEU A 405 ? 0.3968 0.7900 0.5718 -0.0945 -0.0584 0.0388 382 LEU A CA 2889 C C . LEU A 405 ? 0.4591 0.8685 0.6359 -0.1019 -0.0565 0.0418 382 LEU A C 2890 O O . LEU A 405 ? 0.5719 0.9951 0.7474 -0.0960 -0.0505 0.0406 382 LEU A O 2891 C CB . LEU A 405 ? 0.3523 0.7551 0.5342 -0.0960 -0.0660 0.0393 382 LEU A CB 2892 C CG . LEU A 405 ? 0.4627 0.8532 0.6439 -0.0899 -0.0694 0.0360 382 LEU A CG 2893 C CD1 . LEU A 405 ? 0.4942 0.8906 0.6716 -0.0768 -0.0647 0.0339 382 LEU A CD1 2894 C CD2 . LEU A 405 ? 0.5046 0.8985 0.6947 -0.0978 -0.0802 0.0366 382 LEU A CD2 2895 N N . SER A 406 ? 0.5791 0.9874 0.7594 -0.1150 -0.0621 0.0454 383 SER A N 2896 C CA . SER A 406 ? 0.6781 1.1041 0.8607 -0.1243 -0.0617 0.0493 383 SER A CA 2897 C C . SER A 406 ? 0.6304 1.0627 0.8214 -0.1378 -0.0720 0.0544 383 SER A C 2898 O O . SER A 406 ? 0.6111 1.0282 0.8039 -0.1455 -0.0786 0.0561 383 SER A O 2899 C CB . SER A 406 ? 0.6865 1.1038 0.8634 -0.1277 -0.0572 0.0496 383 SER A CB 2900 O OG . SER A 406 ? 0.7580 1.1938 0.9366 -0.1377 -0.0571 0.0537 383 SER A OG 2901 N N . GLY A 407 ? 0.6187 1.0733 0.8156 -0.1406 -0.0740 0.0568 384 GLY A N 2902 C CA . GLY A 407 ? 0.5855 1.0475 0.7917 -0.1533 -0.0843 0.0621 384 GLY A CA 2903 C C . GLY A 407 ? 0.5982 1.0466 0.8094 -0.1512 -0.0926 0.0600 384 GLY A C 2904 O O . GLY A 407 ? 0.6029 1.0458 0.8213 -0.1616 -0.1028 0.0631 384 GLY A O 2905 N N . GLY A 408 ? 0.4659 0.9092 0.6737 -0.1376 -0.0887 0.0544 385 GLY A N 2906 C CA . GLY A 408 ? 0.3831 0.8162 0.5949 -0.1341 -0.0956 0.0512 385 GLY A CA 2907 C C . GLY A 408 ? 0.4953 0.9039 0.7039 -0.1335 -0.0975 0.0482 385 GLY A C 2908 O O . GLY A 408 ? 0.5704 0.9703 0.7824 -0.1308 -0.1035 0.0447 385 GLY A O 2909 N N . GLU A 409 ? 0.5143 0.9126 0.7167 -0.1358 -0.0926 0.0490 386 GLU A N 2910 C CA . GLU A 409 ? 0.6653 1.0403 0.8646 -0.1355 -0.0938 0.0460 386 GLU A CA 2911 C C . GLU A 409 ? 0.5633 0.9281 0.7522 -0.1234 -0.0830 0.0421 386 GLU A C 2912 O O . GLU A 409 ? 0.5553 0.9268 0.7389 -0.1202 -0.0748 0.0431 386 GLU A O 2913 C CB . GLU A 409 ? 0.8624 1.2307 1.0635 -0.1485 -0.0980 0.0501 386 GLU A CB 2914 C CG . GLU A 409 ? 0.9737 1.3508 1.1856 -0.1620 -0.1096 0.0553 386 GLU A CG 2915 C CD . GLU A 409 ? 1.1188 1.4812 1.3386 -0.1659 -0.1212 0.0526 386 GLU A CD 2916 O OE1 . GLU A 409 ? 1.1472 1.4941 1.3637 -0.1579 -0.1194 0.0463 386 GLU A OE1 2917 O OE2 . GLU A 409 ? 1.1981 1.5631 1.4270 -0.1760 -0.1315 0.0563 386 GLU A OE2 2918 N N . PRO A 410 ? 0.4782 0.8272 0.6647 -0.1169 -0.0832 0.0374 387 PRO A N 2919 C CA . PRO A 410 ? 0.4033 0.7414 0.5805 -0.1059 -0.0738 0.0344 387 PRO A CA 2920 C C . PRO A 410 ? 0.4393 0.7660 0.6116 -0.1089 -0.0689 0.0352 387 PRO A C 2921 O O . PRO A 410 ? 0.4956 0.8126 0.6708 -0.1182 -0.0742 0.0360 387 PRO A O 2922 C CB . PRO A 410 ? 0.4418 0.7665 0.6192 -0.1017 -0.0772 0.0298 387 PRO A CB 2923 C CG . PRO A 410 ? 0.5268 0.8495 0.7135 -0.1125 -0.0886 0.0298 387 PRO A CG 2924 C CD . PRO A 410 ? 0.4032 0.7444 0.5962 -0.1197 -0.0928 0.0346 387 PRO A CD 2925 N N . LEU A 411 ? 0.4783 0.8063 0.6440 -0.1009 -0.0595 0.0348 388 LEU A N 2926 C CA . LEU A 411 ? 0.4470 0.7649 0.6080 -0.1024 -0.0544 0.0349 388 LEU A CA 2927 C C . LEU A 411 ? 0.4690 0.7639 0.6268 -0.1001 -0.0538 0.0318 388 LEU A C 2928 O O . LEU A 411 ? 0.3885 0.6769 0.5453 -0.0936 -0.0539 0.0291 388 LEU A O 2929 C CB . LEU A 411 ? 0.3781 0.7040 0.5341 -0.0934 -0.0452 0.0343 388 LEU A CB 2930 C CG . LEU A 411 ? 0.5158 0.8660 0.6748 -0.0940 -0.0444 0.0362 388 LEU A CG 2931 C CD1 . LEU A 411 ? 0.5611 0.9170 0.7160 -0.0845 -0.0357 0.0341 388 LEU A CD1 2932 C CD2 . LEU A 411 ? 0.4682 0.8284 0.6313 -0.1077 -0.0491 0.0401 388 LEU A CD2 2933 N N . SER A 412 ? 0.4625 0.7463 0.6189 -0.1058 -0.0531 0.0321 389 SER A N 2934 C CA . SER A 412 ? 0.4802 0.7423 0.6337 -0.1040 -0.0519 0.0290 389 SER A CA 2935 C C . SER A 412 ? 0.4441 0.6996 0.5910 -0.0949 -0.0423 0.0277 389 SER A C 2936 O O . SER A 412 ? 0.4480 0.6860 0.5922 -0.0926 -0.0399 0.0254 389 SER A O 2937 C CB . SER A 412 ? 0.4023 0.6545 0.5590 -0.1156 -0.0579 0.0298 389 SER A CB 2938 O OG . SER A 412 ? 0.6793 0.9350 0.8435 -0.1241 -0.0682 0.0307 389 SER A OG 2939 N N . GLN A 413 ? 0.4591 0.7289 0.6042 -0.0897 -0.0372 0.0289 390 GLN A N 2940 C CA . GLN A 413 ? 0.4658 0.7309 0.6060 -0.0806 -0.0289 0.0274 390 GLN A CA 2941 C C . GLN A 413 ? 0.4529 0.7291 0.5920 -0.0699 -0.0251 0.0271 390 GLN A C 2942 O O . GLN A 413 ? 0.3217 0.6126 0.4637 -0.0704 -0.0283 0.0283 390 GLN A O 2943 C CB . GLN A 413 ? 0.5470 0.8184 0.6865 -0.0848 -0.0264 0.0280 390 GLN A CB 2944 C CG . GLN A 413 ? 0.4826 0.7430 0.6226 -0.0955 -0.0301 0.0286 390 GLN A CG 2945 C CD . GLN A 413 ? 0.4912 0.7608 0.6300 -0.0998 -0.0277 0.0295 390 GLN A CD 2946 O OE1 . GLN A 413 ? 0.6293 0.8913 0.7649 -0.0951 -0.0223 0.0270 390 GLN A OE1 2947 N NE2 . GLN A 413 ? 0.4684 0.7553 0.6101 -0.1089 -0.0318 0.0329 390 GLN A NE2 2948 N N . GLY A 414 ? 0.4272 0.6960 0.5627 -0.0602 -0.0188 0.0256 391 GLY A N 2949 C CA . GLY A 414 ? 0.4257 0.7039 0.5605 -0.0497 -0.0156 0.0254 391 GLY A CA 2950 C C . GLY A 414 ? 0.4714 0.7686 0.6085 -0.0484 -0.0135 0.0248 391 GLY A C 2951 O O . GLY A 414 ? 0.4356 0.7377 0.5737 -0.0552 -0.0133 0.0245 391 GLY A O 2952 N N . ALA A 415 ? 0.3441 0.6525 0.4821 -0.0398 -0.0120 0.0243 392 ALA A N 2953 C CA . ALA A 415 ? 0.3163 0.6448 0.4573 -0.0371 -0.0100 0.0226 392 ALA A CA 2954 C C . ALA A 415 ? 0.4092 0.7348 0.5497 -0.0345 -0.0053 0.0195 392 ALA A C 2955 O O . ALA A 415 ? 0.5318 0.8740 0.6747 -0.0372 -0.0041 0.0177 392 ALA A O 2956 C CB . ALA A 415 ? 0.3193 0.6565 0.4615 -0.0267 -0.0095 0.0220 392 ALA A CB 2957 N N . GLY A 416 ? 0.4688 0.7741 0.6064 -0.0293 -0.0028 0.0188 393 GLY A N 2958 C CA . GLY A 416 ? 0.4282 0.7287 0.5660 -0.0257 0.0012 0.0154 393 GLY A CA 2959 C C . GLY A 416 ? 0.4108 0.7074 0.5474 -0.0357 0.0011 0.0151 393 GLY A C 2960 O O . GLY A 416 ? 0.5005 0.7966 0.6373 -0.0337 0.0042 0.0118 393 GLY A O 2961 N N . SER A 417 ? 0.3841 0.6780 0.5197 -0.0464 -0.0030 0.0184 394 SER A N 2962 C CA . SER A 417 ? 0.4668 0.7543 0.6012 -0.0564 -0.0042 0.0188 394 SER A CA 2963 C C . SER A 417 ? 0.4508 0.7549 0.5870 -0.0685 -0.0084 0.0216 394 SER A C 2964 O O . SER A 417 ? 0.5320 0.8380 0.6674 -0.0763 -0.0088 0.0219 394 SER A O 2965 C CB . SER A 417 ? 0.4498 0.7129 0.5821 -0.0589 -0.0059 0.0199 394 SER A CB 2966 O OG . SER A 417 ? 0.6671 0.9147 0.7977 -0.0490 -0.0018 0.0179 394 SER A OG 2967 N N . TYR A 418 ? 0.3913 0.7077 0.5301 -0.0703 -0.0119 0.0239 395 TYR A N 2968 C CA . TYR A 418 ? 0.3825 0.7138 0.5239 -0.0824 -0.0168 0.0274 395 TYR A CA 2969 C C . TYR A 418 ? 0.3735 0.7285 0.5161 -0.0845 -0.0141 0.0267 395 TYR A C 2970 O O . TYR A 418 ? 0.4303 0.8023 0.5751 -0.0778 -0.0116 0.0247 395 TYR A O 2971 C CB . TYR A 418 ? 0.3559 0.6940 0.5006 -0.0834 -0.0216 0.0298 395 TYR A CB 2972 C CG . TYR A 418 ? 0.4428 0.7944 0.5916 -0.0965 -0.0279 0.0340 395 TYR A CG 2973 C CD1 . TYR A 418 ? 0.4147 0.7539 0.5647 -0.1069 -0.0344 0.0368 395 TYR A CD1 2974 C CD2 . TYR A 418 ? 0.4093 0.7862 0.5614 -0.0987 -0.0279 0.0353 395 TYR A CD2 2975 C CE1 . TYR A 418 ? 0.3980 0.7486 0.5525 -0.1193 -0.0413 0.0413 395 TYR A CE1 2976 C CE2 . TYR A 418 ? 0.4239 0.8134 0.5801 -0.1114 -0.0340 0.0400 395 TYR A CE2 2977 C CZ . TYR A 418 ? 0.4493 0.8250 0.6067 -0.1217 -0.0409 0.0434 395 TYR A CZ 2978 O OH . TYR A 418 ? 0.4998 0.8871 0.6622 -0.1347 -0.0480 0.0487 395 TYR A OH 2979 N N . VAL A 419 ? 0.3883 0.7451 0.5295 -0.0940 -0.0147 0.0280 396 VAL A N 2980 C CA . VAL A 419 ? 0.5245 0.9054 0.6662 -0.0975 -0.0122 0.0274 396 VAL A CA 2981 C C . VAL A 419 ? 0.5890 0.9914 0.7348 -0.1070 -0.0167 0.0322 396 VAL A C 2982 O O . VAL A 419 ? 0.6072 1.0051 0.7541 -0.1186 -0.0232 0.0376 396 VAL A O 2983 C CB . VAL A 419 ? 0.4789 0.8549 0.6170 -0.1048 -0.0115 0.0276 396 VAL A CB 2984 C CG1 . VAL A 419 ? 0.4514 0.8552 0.5897 -0.1089 -0.0088 0.0269 396 VAL A CG1 2985 C CG2 . VAL A 419 ? 0.3149 0.6698 0.4500 -0.0953 -0.0072 0.0227 396 VAL A CG2 2986 N N . VAL A 420 ? 0.5982 1.0238 0.7469 -0.1021 -0.0138 0.0301 397 VAL A N 2987 C CA . VAL A 420 ? 0.5853 1.0322 0.7386 -0.1098 -0.0178 0.0343 397 VAL A CA 2988 C C . VAL A 420 ? 0.6128 1.0811 0.7663 -0.1222 -0.0182 0.0376 397 VAL A C 2989 O O . VAL A 420 ? 0.6116 1.0857 0.7618 -0.1214 -0.0134 0.0344 397 VAL A O 2990 C CB . VAL A 420 ? 0.5373 1.0003 0.6945 -0.0990 -0.0150 0.0305 397 VAL A CB 2991 C CG1 . VAL A 420 ? 0.4206 0.8629 0.5768 -0.0871 -0.0148 0.0280 397 VAL A CG1 2992 C CG2 . VAL A 420 ? 0.4912 0.9726 0.6484 -0.0923 -0.0082 0.0244 397 VAL A CG2 2993 N N . ARG A 421 ? 0.5959 1.0763 0.7534 -0.1340 -0.0241 0.0440 398 ARG A N 2994 C CA . ARG A 421 ? 0.6420 1.1437 0.7998 -0.1475 -0.0254 0.0488 398 ARG A CA 2995 C C . ARG A 421 ? 0.6556 1.1876 0.8191 -0.1501 -0.0255 0.0503 398 ARG A C 2996 O O . ARG A 421 ? 0.6378 1.1714 0.8057 -0.1432 -0.0265 0.0488 398 ARG A O 2997 C CB . ARG A 421 ? 0.7557 1.2438 0.9133 -0.1624 -0.0337 0.0568 398 ARG A CB 2998 C CG . ARG A 421 ? 0.8526 1.3126 1.0047 -0.1616 -0.0339 0.0554 398 ARG A CG 2999 C CD . ARG A 421 ? 0.9723 1.4231 1.1248 -0.1776 -0.0424 0.0632 398 ARG A CD 3000 N NE . ARG A 421 ? 1.1644 1.6083 1.3235 -0.1832 -0.0515 0.0678 398 ARG A NE 3001 C CZ . ARG A 421 ? 1.2295 1.6473 1.3900 -0.1813 -0.0566 0.0668 398 ARG A CZ 3002 N NH1 . ARG A 421 ? 1.1671 1.5628 1.3225 -0.1742 -0.0531 0.0620 398 ARG A NH1 3003 N NH2 . ARG A 421 ? 1.3083 1.7229 1.4757 -0.1863 -0.0652 0.0702 398 ARG A NH2 3004 N N . ASN A 422 ? 0.6231 1.1799 0.7866 -0.1604 -0.0244 0.0534 399 ASN A N 3005 C CA . ASN A 422 ? 0.6069 1.1958 0.7760 -0.1636 -0.0237 0.0545 399 ASN A CA 3006 C C . ASN A 422 ? 0.5901 1.1800 0.7660 -0.1716 -0.0320 0.0616 399 ASN A C 3007 O O . ASN A 422 ? 0.6239 1.2015 0.8005 -0.1836 -0.0397 0.0692 399 ASN A O 3008 C CB . ASN A 422 ? 0.7786 1.3938 0.9455 -0.1748 -0.0212 0.0573 399 ASN A CB 3009 C CG . ASN A 422 ? 0.7040 1.3555 0.8759 -0.1738 -0.0170 0.0547 399 ASN A CG 3010 O OD1 . ASN A 422 ? 0.6050 1.2622 0.7800 -0.1599 -0.0127 0.0467 399 ASN A OD1 3011 N ND2 . ASN A 422 ? 0.7811 1.4578 0.9542 -0.1888 -0.0186 0.0615 399 ASN A ND2 3012 N N . GLY A 423 ? 0.4850 1.0896 0.6667 -0.1647 -0.0310 0.0588 400 GLY A N 3013 C CA . GLY A 423 ? 0.4794 1.0884 0.6686 -0.1714 -0.0387 0.0646 400 GLY A CA 3014 C C . GLY A 423 ? 0.6446 1.2243 0.8349 -0.1668 -0.0447 0.0649 400 GLY A C 3015 O O . GLY A 423 ? 0.7104 1.2881 0.9069 -0.1746 -0.0531 0.0704 400 GLY A O 3016 N N . GLU A 424 ? 0.6352 1.1928 0.8200 -0.1542 -0.0407 0.0586 401 GLU A N 3017 C CA . GLU A 424 ? 0.6315 1.1623 0.8166 -0.1491 -0.0454 0.0580 401 GLU A CA 3018 C C . GLU A 424 ? 0.5551 1.0905 0.7444 -0.1383 -0.0456 0.0545 401 GLU A C 3019 O O . GLU A 424 ? 0.5593 1.1068 0.7481 -0.1276 -0.0391 0.0490 401 GLU A O 3020 C CB . GLU A 424 ? 0.6380 1.1435 0.8155 -0.1408 -0.0411 0.0535 401 GLU A CB 3021 C CG . GLU A 424 ? 0.6676 1.1498 0.8432 -0.1497 -0.0471 0.0575 401 GLU A CG 3022 C CD . GLU A 424 ? 0.5889 1.0455 0.7580 -0.1405 -0.0431 0.0526 401 GLU A CD 3023 O OE1 . GLU A 424 ? 0.5625 0.9966 0.7315 -0.1423 -0.0482 0.0535 401 GLU A OE1 3024 O OE2 . GLU A 424 ? 0.6128 1.0720 0.7776 -0.1314 -0.0351 0.0476 401 GLU A OE2 3025 N N . ASN A 425 ? 0.4828 1.0086 0.6768 -0.1412 -0.0535 0.0572 402 ASN A N 3026 C CA . ASN A 425 ? 0.5508 1.0774 0.7480 -0.1307 -0.0544 0.0538 402 ASN A CA 3027 C C . ASN A 425 ? 0.4788 0.9808 0.6700 -0.1179 -0.0517 0.0488 402 ASN A C 3028 O O . ASN A 425 ? 0.4702 0.9542 0.6618 -0.1183 -0.0572 0.0494 402 ASN A O 3029 C CB . ASN A 425 ? 0.6813 1.2100 0.8868 -0.1391 -0.0645 0.0584 402 ASN A CB 3030 C CG . ASN A 425 ? 0.8748 1.4300 1.0874 -0.1510 -0.0674 0.0638 402 ASN A CG 3031 O OD1 . ASN A 425 ? 0.9656 1.5432 1.1784 -0.1488 -0.0612 0.0622 402 ASN A OD1 3032 N ND2 . ASN A 425 ? 0.9289 1.4824 1.1481 -0.1639 -0.0772 0.0702 402 ASN A ND2 3033 N N . LEU A 426 ? 0.5290 1.0309 0.7150 -0.1068 -0.0435 0.0438 403 LEU A N 3034 C CA . LEU A 426 ? 0.5719 1.0517 0.7522 -0.0947 -0.0404 0.0397 403 LEU A CA 3035 C C . LEU A 426 ? 0.5487 1.0294 0.7311 -0.0848 -0.0420 0.0376 403 LEU A C 3036 O O . LEU A 426 ? 0.4815 0.9820 0.6681 -0.0814 -0.0414 0.0363 403 LEU A O 3037 C CB . LEU A 426 ? 0.4850 0.9649 0.6605 -0.0862 -0.0320 0.0352 403 LEU A CB 3038 C CG . LEU A 426 ? 0.4878 0.9691 0.6606 -0.0948 -0.0296 0.0364 403 LEU A CG 3039 C CD1 . LEU A 426 ? 0.5607 1.0421 0.7297 -0.0847 -0.0218 0.0307 403 LEU A CD1 3040 C CD2 . LEU A 426 ? 0.5541 1.0123 0.7240 -0.1027 -0.0338 0.0398 403 LEU A CD2 3041 N N . GLU A 427 ? 0.5072 0.9670 0.6864 -0.0802 -0.0442 0.0369 404 GLU A N 3042 C CA . GLU A 427 ? 0.4992 0.9591 0.6795 -0.0714 -0.0464 0.0352 404 GLU A CA 3043 C C . GLU A 427 ? 0.4592 0.8970 0.6327 -0.0618 -0.0441 0.0330 404 GLU A C 3044 O O . GLU A 427 ? 0.4679 0.8874 0.6381 -0.0654 -0.0448 0.0336 404 GLU A O 3045 C CB . GLU A 427 ? 0.5458 1.0101 0.7327 -0.0796 -0.0552 0.0379 404 GLU A CB 3046 C CG . GLU A 427 ? 0.6897 1.1546 0.8778 -0.0710 -0.0582 0.0360 404 GLU A CG 3047 C CD . GLU A 427 ? 0.8062 1.2753 1.0019 -0.0790 -0.0676 0.0379 404 GLU A CD 3048 O OE1 . GLU A 427 ? 0.9618 1.4365 1.1629 -0.0915 -0.0720 0.0414 404 GLU A OE1 3049 O OE2 . GLU A 427 ? 0.7124 1.1792 0.9088 -0.0730 -0.0712 0.0360 404 GLU A OE2 3050 N N . VAL A 428 ? 0.4998 0.9399 0.6715 -0.0498 -0.0415 0.0307 405 VAL A N 3051 C CA . VAL A 428 ? 0.3784 0.8000 0.5440 -0.0410 -0.0403 0.0297 405 VAL A CA 3052 C C . VAL A 428 ? 0.4545 0.8804 0.6221 -0.0378 -0.0456 0.0297 405 VAL A C 3053 O O . VAL A 428 ? 0.3957 0.8367 0.5663 -0.0326 -0.0460 0.0289 405 VAL A O 3054 C CB . VAL A 428 ? 0.4220 0.8403 0.5835 -0.0293 -0.0338 0.0276 405 VAL A CB 3055 C CG1 . VAL A 428 ? 0.5042 0.9018 0.6589 -0.0222 -0.0326 0.0278 405 VAL A CG1 3056 C CG2 . VAL A 428 ? 0.4255 0.8445 0.5867 -0.0319 -0.0290 0.0265 405 VAL A CG2 3057 N N . ARG A 429 ? 0.4525 0.8657 0.6187 -0.0408 -0.0498 0.0300 406 ARG A N 3058 C CA . ARG A 429 ? 0.4398 0.8582 0.6090 -0.0398 -0.0561 0.0295 406 ARG A CA 3059 C C . ARG A 429 ? 0.3811 0.7867 0.5436 -0.0310 -0.0554 0.0282 406 ARG A C 3060 O O . ARG A 429 ? 0.4092 0.7979 0.5665 -0.0312 -0.0534 0.0280 406 ARG A O 3061 C CB . ARG A 429 ? 0.5018 0.9202 0.6775 -0.0519 -0.0635 0.0302 406 ARG A CB 3062 C CG . ARG A 429 ? 0.5347 0.9572 0.7147 -0.0516 -0.0712 0.0287 406 ARG A CG 3063 C CD . ARG A 429 ? 0.5228 0.9438 0.7106 -0.0638 -0.0795 0.0291 406 ARG A CD 3064 N NE . ARG A 429 ? 0.6504 1.0834 0.8445 -0.0735 -0.0808 0.0326 406 ARG A NE 3065 C CZ . ARG A 429 ? 0.5856 1.0186 0.7871 -0.0856 -0.0880 0.0345 406 ARG A CZ 3066 N NH1 . ARG A 429 ? 0.5122 0.9333 0.7166 -0.0890 -0.0950 0.0324 406 ARG A NH1 3067 N NH2 . ARG A 429 ? 0.4922 0.9377 0.6986 -0.0946 -0.0887 0.0385 406 ARG A NH2 3068 N N . TRP A 430 ? 0.3812 0.7957 0.5437 -0.0236 -0.0573 0.0276 407 TRP A N 3069 C CA . TRP A 430 ? 0.4676 0.8732 0.6237 -0.0160 -0.0576 0.0269 407 TRP A CA 3070 C C . TRP A 430 ? 0.3805 0.7821 0.5392 -0.0219 -0.0641 0.0249 407 TRP A C 3071 O O . TRP A 430 ? 0.3708 0.7839 0.5367 -0.0259 -0.0707 0.0238 407 TRP A O 3072 C CB . TRP A 430 ? 0.3999 0.8179 0.5559 -0.0068 -0.0584 0.0268 407 TRP A CB 3073 C CG . TRP A 430 ? 0.5083 0.9193 0.6571 0.0011 -0.0588 0.0268 407 TRP A CG 3074 C CD1 . TRP A 430 ? 0.4878 0.9051 0.6374 0.0028 -0.0645 0.0252 407 TRP A CD1 3075 C CD2 . TRP A 430 ? 0.5000 0.8975 0.6397 0.0082 -0.0536 0.0287 407 TRP A CD2 3076 N NE1 . TRP A 430 ? 0.5251 0.9345 0.6659 0.0104 -0.0628 0.0260 407 TRP A NE1 3077 C CE2 . TRP A 430 ? 0.5572 0.9542 0.6919 0.0135 -0.0562 0.0286 407 TRP A CE2 3078 C CE3 . TRP A 430 ? 0.5146 0.9007 0.6503 0.0104 -0.0474 0.0305 407 TRP A CE3 3079 C CZ2 . TRP A 430 ? 0.4980 0.8839 0.6234 0.0202 -0.0526 0.0312 407 TRP A CZ2 3080 C CZ3 . TRP A 430 ? 0.5817 0.9557 0.7091 0.0174 -0.0441 0.0328 407 TRP A CZ3 3081 C CH2 . TRP A 430 ? 0.5426 0.9167 0.6647 0.0219 -0.0467 0.0336 407 TRP A CH2 3082 N N . SER A 431 ? 0.4349 0.8206 0.5884 -0.0224 -0.0626 0.0241 408 SER A N 3083 C CA . SER A 431 ? 0.5024 0.8835 0.6594 -0.0288 -0.0690 0.0211 408 SER A CA 3084 C C . SER A 431 ? 0.5674 0.9389 0.7175 -0.0234 -0.0683 0.0189 408 SER A C 3085 O O . SER A 431 ? 0.4826 0.8474 0.6241 -0.0161 -0.0621 0.0208 408 SER A O 3086 C CB . SER A 431 ? 0.5164 0.8885 0.6772 -0.0390 -0.0697 0.0212 408 SER A CB 3087 O OG . SER A 431 ? 0.5549 0.9370 0.7212 -0.0446 -0.0699 0.0237 408 SER A OG 3088 N N . LYS A 432 ? 0.6487 1.0203 0.8031 -0.0274 -0.0751 0.0147 409 LYS A N 3089 C CA . LYS A 432 ? 0.7510 1.1160 0.8997 -0.0233 -0.0750 0.0115 409 LYS A CA 3090 C C . LYS A 432 ? 0.7853 1.1372 0.9363 -0.0305 -0.0764 0.0083 409 LYS A C 3091 O O . LYS A 432 ? 0.6062 0.9552 0.7642 -0.0389 -0.0793 0.0084 409 LYS A O 3092 C CB . LYS A 432 ? 0.7761 1.1535 0.9287 -0.0209 -0.0825 0.0075 409 LYS A CB 3093 C CG . LYS A 432 ? 0.9487 1.3414 1.1038 -0.0168 -0.0844 0.0096 409 LYS A CG 3094 C CD . LYS A 432 ? 1.0593 1.4530 1.2043 -0.0067 -0.0776 0.0135 409 LYS A CD 3095 C CE . LYS A 432 ? 1.0381 1.4477 1.1860 -0.0018 -0.0807 0.0142 409 LYS A CE 3096 N NZ . LYS A 432 ? 1.0689 1.4870 1.2263 -0.0076 -0.0828 0.0155 409 LYS A NZ 3097 N N . TYR A 433 ? 0.9491 1.2936 1.0943 -0.0273 -0.0745 0.0055 410 TYR A N 3098 C CA . TYR A 433 ? 1.0336 1.3670 1.1820 -0.0336 -0.0768 0.0010 410 TYR A CA 3099 C C . TYR A 433 ? 1.1510 1.4919 1.3090 -0.0373 -0.0873 -0.0058 410 TYR A C 3100 O O . TYR A 433 ? 1.2105 1.5444 1.3754 -0.0441 -0.0924 -0.0103 410 TYR A O 3101 C CB . TYR A 433 ? 0.9865 1.3103 1.1256 -0.0290 -0.0706 0.0002 410 TYR A CB 3102 C CG . TYR A 433 ? 0.9953 1.3105 1.1252 -0.0245 -0.0608 0.0066 410 TYR A CG 3103 C CD1 . TYR A 433 ? 0.9299 1.2436 1.0607 -0.0256 -0.0577 0.0114 410 TYR A CD1 3104 C CD2 . TYR A 433 ? 0.9339 1.2429 1.0547 -0.0193 -0.0549 0.0076 410 TYR A CD2 3105 C CE1 . TYR A 433 ? 0.8457 1.1515 0.9694 -0.0209 -0.0496 0.0164 410 TYR A CE1 3106 C CE2 . TYR A 433 ? 0.8600 1.1603 0.9735 -0.0153 -0.0470 0.0136 410 TYR A CE2 3107 C CZ . TYR A 433 ? 0.8318 1.1301 0.9472 -0.0158 -0.0446 0.0176 410 TYR A CZ 3108 O OH . TYR A 433 ? 0.8322 1.1219 0.9417 -0.0112 -0.0375 0.0228 410 TYR A OH 3109 N N . LEU A 434 ? 1.1595 1.5145 1.3186 -0.0326 -0.0911 -0.0069 411 LEU A N 3110 C CA . LEU A 434 ? 1.1007 1.4647 1.2690 -0.0344 -0.1015 -0.0139 411 LEU A CA 3111 C C . LEU A 434 ? 1.0144 1.3735 1.1818 -0.0337 -0.1031 -0.0215 411 LEU A C 3112 O O . LEU A 434 ? 0.9494 1.3178 1.1151 -0.0282 -0.1057 -0.0263 411 LEU A O 3113 C CB . LEU A 434 ? 1.0807 1.4458 1.2626 -0.0440 -0.1103 -0.0145 411 LEU A CB 3114 C CG . LEU A 434 ? 1.0948 1.4681 1.2887 -0.0465 -0.1227 -0.0221 411 LEU A CG 3115 C CD1 . LEU A 434 ? 1.0753 1.4647 1.2688 -0.0393 -0.1250 -0.0228 411 LEU A CD1 3116 C CD2 . LEU A 434 ? 1.0571 1.4286 1.2647 -0.0573 -0.1317 -0.0216 411 LEU A CD2 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 MET 1 -22 ? ? ? A . n A 1 2 ARG 2 -21 ? ? ? A . n A 1 3 GLN 3 -20 ? ? ? A . n A 1 4 SER 4 -19 ? ? ? A . n A 1 5 HIS 5 -18 ? ? ? A . n A 1 6 GLN 6 -17 ? ? ? A . n A 1 7 LEU 7 -16 ? ? ? A . n A 1 8 PRO 8 -15 ? ? ? A . n A 1 9 LEU 9 -14 ? ? ? A . n A 1 10 VAL 10 -13 ? ? ? A . n A 1 11 GLY 11 -12 ? ? ? A . n A 1 12 LEU 12 -11 ? ? ? A . n A 1 13 LEU 13 -10 ? ? ? A . n A 1 14 LEU 14 -9 ? ? ? A . n A 1 15 PHE 15 -8 ? ? ? A . n A 1 16 SER 16 -7 ? ? ? A . n A 1 17 PHE 17 -6 ? ? ? A . n A 1 18 ILE 18 -5 ? ? ? A . n A 1 19 PRO 19 -4 ? ? ? A . n A 1 20 SER 20 -3 ? ? ? A . n A 1 21 GLN 21 -2 ? ? ? A . n A 1 22 LEU 22 -1 ? ? ? A . n A 1 23 CYS 23 0 ? ? ? A . n A 1 24 GLU 24 1 1 GLU GLU A . n A 1 25 ILE 25 2 2 ILE ILE A . n A 1 26 CYS 26 3 3 CYS CYS A . n A 1 27 GLU 27 4 4 GLU GLU A . n A 1 28 VAL 28 5 5 VAL VAL A . n A 1 29 SER 29 6 6 SER SER A . n A 1 30 GLU 30 7 7 GLU GLU A . n A 1 31 GLU 31 8 8 GLU GLU A . n A 1 32 ASN 32 9 9 ASN ASN A . n A 1 33 TYR 33 10 10 TYR TYR A . n A 1 34 ILE 34 11 11 ILE ILE A . n A 1 35 ARG 35 12 12 ARG ARG A . n A 1 36 LEU 36 13 13 LEU LEU A . n A 1 37 LYS 37 14 14 LYS LYS A . n A 1 38 PRO 38 15 15 PRO PRO A . n A 1 39 LEU 39 16 16 LEU LEU A . n A 1 40 LEU 40 17 17 LEU LEU A . n A 1 41 ASN 41 18 18 ASN ASN A . n A 1 42 THR 42 19 19 THR THR A . n A 1 43 MET 43 20 20 MET MET A . n A 1 44 ILE 44 21 21 ILE ILE A . n A 1 45 GLN 45 22 22 GLN GLN A . n A 1 46 SER 46 23 23 SER SER A . n A 1 47 ASN 47 24 24 ASN ASN A . n A 1 48 TYR 48 25 25 TYR TYR A . n A 1 49 ASN 49 26 26 ASN ASN A . n A 1 50 ARG 50 27 27 ARG ARG A . n A 1 51 GLY 51 28 28 GLY GLY A . n A 1 52 THR 52 29 29 THR THR A . n A 1 53 SER 53 30 30 SER SER A . n A 1 54 ALA 54 31 31 ALA ALA A . n A 1 55 VAL 55 32 32 VAL VAL A . n A 1 56 ASN 56 33 33 ASN ASN A . n A 1 57 VAL 57 34 34 VAL VAL A . n A 1 58 VAL 58 35 35 VAL VAL A . n A 1 59 LEU 59 36 36 LEU LEU A . n A 1 60 SER 60 37 37 SER SER A . n A 1 61 LEU 61 38 38 LEU LEU A . n A 1 62 LYS 62 39 39 LYS LYS A . n A 1 63 LEU 63 40 40 LEU LEU A . n A 1 64 VAL 64 41 41 VAL VAL A . n A 1 65 GLY 65 42 42 GLY GLY A . n A 1 66 ILE 66 43 43 ILE ILE A . n A 1 67 GLN 67 44 44 GLN GLN A . n A 1 68 ILE 68 45 45 ILE ILE A . n A 1 69 GLN 69 46 46 GLN GLN A . n A 1 70 THR 70 47 47 THR THR A . n A 1 71 LEU 71 48 48 LEU LEU A . n A 1 72 MET 72 49 49 MET MET A . n A 1 73 GLN 73 50 50 GLN GLN A . n A 1 74 LYS 74 51 51 LYS LYS A . n A 1 75 MET 75 52 52 MET MET A . n A 1 76 ILE 76 53 53 ILE ILE A . n A 1 77 GLN 77 54 54 GLN GLN A . n A 1 78 GLN 78 55 55 GLN GLN A . n A 1 79 ILE 79 56 56 ILE ILE A . n A 1 80 LYS 80 57 57 LYS LYS A . n A 1 81 TYR 81 58 58 TYR TYR A . n A 1 82 ASN 82 59 59 ASN ASN A . n A 1 83 VAL 83 60 60 VAL VAL A . n A 1 84 LYS 84 61 61 LYS LYS A . n A 1 85 SER 85 62 62 SER SER A . n A 1 86 ARG 86 63 63 ARG ARG A . n A 1 87 LEU 87 64 64 LEU LEU A . n A 1 88 SER 88 65 65 SER SER A . n A 1 89 ASP 89 66 66 ASP ASP A . n A 1 90 VAL 90 67 67 VAL VAL A . n A 1 91 SER 91 68 68 SER SER A . n A 1 92 SER 92 69 69 SER SER A . n A 1 93 GLY 93 70 70 GLY GLY A . n A 1 94 GLU 94 71 71 GLU GLU A . n A 1 95 LEU 95 72 72 LEU LEU A . n A 1 96 ALA 96 73 73 ALA ALA A . n A 1 97 LEU 97 74 74 LEU LEU A . n A 1 98 ILE 98 75 75 ILE ILE A . n A 1 99 ILE 99 76 76 ILE ILE A . n A 1 100 LEU 100 77 77 LEU LEU A . n A 1 101 ALA 101 78 78 ALA ALA A . n A 1 102 LEU 102 79 79 LEU LEU A . n A 1 103 GLY 103 80 80 GLY GLY A . n A 1 104 VAL 104 81 81 VAL VAL A . n A 1 105 CYS 105 82 82 CYS CYS A . n A 1 106 ARG 106 83 83 ARG ARG A . n A 1 107 ASN 107 84 84 ASN ASN A . n A 1 108 ALA 108 85 85 ALA ALA A . n A 1 109 GLU 109 86 86 GLU GLU A . n A 1 110 GLU 110 87 87 GLU GLU A . n A 1 111 ASN 111 88 88 ASN ASN A . n A 1 112 LEU 112 89 89 LEU LEU A . n A 1 113 ILE 113 90 90 ILE ILE A . n A 1 114 TYR 114 91 91 TYR TYR A . n A 1 115 ASP 115 92 92 ASP ASP A . n A 1 116 TYR 116 93 93 TYR TYR A . n A 1 117 HIS 117 94 94 HIS HIS A . n A 1 118 LEU 118 95 95 LEU LEU A . n A 1 119 ILE 119 96 96 ILE ILE A . n A 1 120 ASP 120 97 97 ASP ASP A . n A 1 121 LYS 121 98 98 LYS LYS A . n A 1 122 LEU 122 99 99 LEU LEU A . n A 1 123 GLU 123 100 100 GLU GLU A . n A 1 124 ASN 124 101 101 ASN ASN A . n A 1 125 LYS 125 102 102 LYS LYS A . n A 1 126 PHE 126 103 103 PHE PHE A . n A 1 127 GLN 127 104 104 GLN GLN A . n A 1 128 ALA 128 105 105 ALA ALA A . n A 1 129 GLU 129 106 106 GLU GLU A . n A 1 130 ILE 130 107 107 ILE ILE A . n A 1 131 GLU 131 108 108 GLU GLU A . n A 1 132 ASN 132 109 109 ASN ASN A . n A 1 133 MET 133 110 110 MET MET A . n A 1 134 GLU 134 111 111 GLU GLU A . n A 1 135 ALA 135 112 112 ALA ALA A . n A 1 136 HIS 136 113 113 HIS HIS A . n A 1 137 ASN 137 114 114 ASN ASN A . n A 1 138 GLY 138 115 115 GLY GLY A . n A 1 139 THR 139 116 116 THR THR A . n A 1 140 PRO 140 117 117 PRO PRO A . n A 1 141 LEU 141 118 118 LEU LEU A . n A 1 142 THR 142 119 119 THR THR A . n A 1 143 ASN 143 120 120 ASN ASN A . n A 1 144 TYR 144 121 121 TYR TYR A . n A 1 145 TYR 145 122 122 TYR TYR A . n A 1 146 GLN 146 123 123 GLN GLN A . n A 1 147 LEU 147 124 124 LEU LEU A . n A 1 148 SER 148 125 125 SER SER A . n A 1 149 LEU 149 126 126 LEU LEU A . n A 1 150 ASP 150 127 127 ASP ASP A . n A 1 151 VAL 151 128 128 VAL VAL A . n A 1 152 LEU 152 129 129 LEU LEU A . n A 1 153 ALA 153 130 130 ALA ALA A . n A 1 154 LEU 154 131 131 LEU LEU A . n A 1 155 CYS 155 132 132 CYS CYS A . n A 1 156 LEU 156 133 133 LEU LEU A . n A 1 157 PHE 157 134 134 PHE PHE A . n A 1 158 ASN 158 135 135 ASN ASN A . n A 1 159 GLY 159 136 136 GLY GLY A . n A 1 160 ASN 160 137 137 ASN ASN A . n A 1 161 TYR 161 138 138 TYR TYR A . n A 1 162 SER 162 139 139 SER SER A . n A 1 163 THR 163 140 140 THR THR A . n A 1 164 ALA 164 141 141 ALA ALA A . n A 1 165 GLU 165 142 142 GLU GLU A . n A 1 166 VAL 166 143 143 VAL VAL A . n A 1 167 VAL 167 144 144 VAL VAL A . n A 1 168 ASN 168 145 145 ASN ASN A . n A 1 169 HIS 169 146 146 HIS HIS A . n A 1 170 PHE 170 147 147 PHE PHE A . n A 1 171 THR 171 148 148 THR THR A . n A 1 172 PRO 172 149 149 PRO PRO A . n A 1 173 GLU 173 150 150 GLU GLU A . n A 1 174 ASN 174 151 151 ASN ASN A . n A 1 175 LYS 175 152 152 LYS LYS A . n A 1 176 ASN 176 153 153 ASN ASN A . n A 1 177 TYR 177 154 154 TYR TYR A . n A 1 178 TYR 178 155 155 TYR TYR A . n A 1 179 PHE 179 156 156 PHE PHE A . n A 1 180 GLY 180 157 157 GLY GLY A . n A 1 181 SER 181 158 158 SER SER A . n A 1 182 GLN 182 159 159 GLN GLN A . n A 1 183 PHE 183 160 160 PHE PHE A . n A 1 184 SER 184 161 161 SER SER A . n A 1 185 VAL 185 162 162 VAL VAL A . n A 1 186 ASP 186 163 163 ASP ASP A . n A 1 187 THR 187 164 164 THR THR A . n A 1 188 GLY 188 165 165 GLY GLY A . n A 1 189 ALA 189 166 166 ALA ALA A . n A 1 190 MET 190 167 167 MET MET A . n A 1 191 ALA 191 168 168 ALA ALA A . n A 1 192 VAL 192 169 169 VAL VAL A . n A 1 193 LEU 193 170 170 LEU LEU A . n A 1 194 ALA 194 171 171 ALA ALA A . n A 1 195 LEU 195 172 172 LEU LEU A . n A 1 196 THR 196 173 173 THR THR A . n A 1 197 CYS 197 174 174 CYS CYS A . n A 1 198 VAL 198 175 175 VAL VAL A . n A 1 199 LYS 199 176 176 LYS LYS A . n A 1 200 LYS 200 177 177 LYS LYS A . n A 1 201 SER 201 178 178 SER SER A . n A 1 202 LEU 202 179 179 LEU LEU A . n A 1 203 ILE 203 180 180 ILE ILE A . n A 1 204 ASN 204 181 181 ASN ASN A . n A 1 205 GLY 205 182 182 GLY GLY A . n A 1 206 GLN 206 183 183 GLN GLN A . n A 1 207 ILE 207 184 184 ILE ILE A . n A 1 208 LYS 208 185 185 LYS LYS A . n A 1 209 ALA 209 186 186 ALA ALA A . n A 1 210 ASP 210 187 187 ASP ASP A . n A 1 211 GLU 211 188 188 GLU GLU A . n A 1 212 GLY 212 189 189 GLY GLY A . n A 1 213 SER 213 190 190 SER SER A . n A 1 214 LEU 214 191 191 LEU LEU A . n A 1 215 LYS 215 192 192 LYS LYS A . n A 1 216 ASN 216 193 193 ASN ASN A . n A 1 217 ILE 217 194 194 ILE ILE A . n A 1 218 SER 218 195 195 SER SER A . n A 1 219 ILE 219 196 196 ILE ILE A . n A 1 220 TYR 220 197 197 TYR TYR A . n A 1 221 THR 221 198 198 THR THR A . n A 1 222 LYS 222 199 199 LYS LYS A . n A 1 223 SER 223 200 200 SER SER A . n A 1 224 LEU 224 201 201 LEU LEU A . n A 1 225 VAL 225 202 202 VAL VAL A . n A 1 226 GLU 226 203 203 GLU GLU A . n A 1 227 LYS 227 204 204 LYS LYS A . n A 1 228 ILE 228 205 205 ILE ILE A . n A 1 229 LEU 229 206 206 LEU LEU A . n A 1 230 SER 230 207 207 SER SER A . n A 1 231 GLU 231 208 208 GLU GLU A . n A 1 232 LYS 232 209 209 LYS LYS A . n A 1 233 LYS 233 210 210 LYS LYS A . n A 1 234 GLU 234 211 211 GLU GLU A . n A 1 235 ASN 235 212 212 ASN ASN A . n A 1 236 GLY 236 213 213 GLY GLY A . n A 1 237 LEU 237 214 214 LEU LEU A . n A 1 238 ILE 238 215 215 ILE ILE A . n A 1 239 GLY 239 216 216 GLY GLY A . n A 1 240 ASN 240 217 217 ASN ASN A . n A 1 241 THR 241 218 218 THR THR A . n A 1 242 PHE 242 219 219 PHE PHE A . n A 1 243 SER 243 220 220 SER SER A . n A 1 244 THR 244 221 221 THR THR A . n A 1 245 GLY 245 222 222 GLY GLY A . n A 1 246 GLU 246 223 223 GLU GLU A . n A 1 247 ALA 247 224 224 ALA ALA A . n A 1 248 MET 248 225 225 MET MET A . n A 1 249 GLN 249 226 226 GLN GLN A . n A 1 250 ALA 250 227 227 ALA ALA A . n A 1 251 LEU 251 228 228 LEU LEU A . n A 1 252 PHE 252 229 229 PHE PHE A . n A 1 253 VAL 253 230 230 VAL VAL A . n A 1 254 SER 254 231 231 SER SER A . n A 1 255 SER 255 232 232 SER SER A . n A 1 256 ASP 256 233 233 ASP ASP A . n A 1 257 TYR 257 234 234 TYR TYR A . n A 1 258 TYR 258 235 235 TYR TYR A . n A 1 259 ASN 259 236 236 ASN ASN A . n A 1 260 GLU 260 237 237 GLU GLU A . n A 1 261 ASN 261 238 238 ASN ASN A . n A 1 262 ASP 262 239 239 ASP ASP A . n A 1 263 TRP 263 240 240 TRP TRP A . n A 1 264 ASN 264 241 241 ASN ASN A . n A 1 265 CYS 265 242 242 CYS CYS A . n A 1 266 GLN 266 243 243 GLN GLN A . n A 1 267 GLN 267 244 244 GLN GLN A . n A 1 268 THR 268 245 245 THR THR A . n A 1 269 LEU 269 246 246 LEU LEU A . n A 1 270 ASN 270 247 247 ASN ASN A . n A 1 271 THR 271 248 248 THR THR A . n A 1 272 VAL 272 249 249 VAL VAL A . n A 1 273 LEU 273 250 250 LEU LEU A . n A 1 274 THR 274 251 251 THR THR A . n A 1 275 GLU 275 252 252 GLU GLU A . n A 1 276 ILE 276 253 253 ILE ILE A . n A 1 277 SER 277 254 254 SER SER A . n A 1 278 GLN 278 255 255 GLN GLN A . n A 1 279 GLY 279 256 256 GLY GLY A . n A 1 280 ALA 280 257 257 ALA ALA A . n A 1 281 PHE 281 258 258 PHE PHE A . n A 1 282 SER 282 259 259 SER SER A . n A 1 283 ASN 283 260 260 ASN ASN A . n A 1 284 PRO 284 261 261 PRO PRO A . n A 1 285 ASN 285 262 262 ASN ASN A . n A 1 286 ALA 286 263 263 ALA ALA A . n A 1 287 ALA 287 264 264 ALA ALA A . n A 1 288 ALA 288 265 265 ALA ALA A . n A 1 289 GLN 289 266 266 GLN GLN A . n A 1 290 VAL 290 267 267 VAL VAL A . n A 1 291 LEU 291 268 268 LEU LEU A . n A 1 292 PRO 292 269 269 PRO PRO A . n A 1 293 ALA 293 270 270 ALA ALA A . n A 1 294 LEU 294 271 271 LEU LEU A . n A 1 295 MET 295 272 272 MET MET A . n A 1 296 GLY 296 273 273 GLY GLY A . n A 1 297 LYS 297 274 274 LYS LYS A . n A 1 298 THR 298 275 275 THR THR A . n A 1 299 PHE 299 276 276 PHE PHE A . n A 1 300 LEU 300 277 277 LEU LEU A . n A 1 301 ASP 301 278 278 ASP ASP A . n A 1 302 ILE 302 279 279 ILE ILE A . n A 1 303 ASN 303 280 280 ASN ASN A . n A 1 304 LYS 304 281 281 LYS LYS A . n A 1 305 ASP 305 282 282 ASP ASP A . n A 1 306 SER 306 283 283 SER SER A . n A 1 307 SER 307 284 284 SER SER A . n A 1 308 CYS 308 285 285 CYS CYS A . n A 1 309 VAL 309 286 286 VAL VAL A . n A 1 310 SER 310 287 287 SER SER A . n A 1 311 ALA 311 288 288 ALA ALA A . n A 1 312 SER 312 289 289 SER SER A . n A 1 313 GLY 313 290 290 GLY GLY A . n A 1 314 ASN 314 291 291 ASN ASN A . n A 1 315 PHE 315 292 292 PHE PHE A . n A 1 316 ASN 316 293 293 ASN ASN A . n A 1 317 ILE 317 294 294 ILE ILE A . n A 1 318 SER 318 295 ? ? ? A . n A 1 319 ALA 319 296 ? ? ? A . n A 1 320 ASP 320 297 ? ? ? A . n A 1 321 GLU 321 298 ? ? ? A . n A 1 322 PRO 322 299 ? ? ? A . n A 1 323 ILE 323 300 ? ? ? A . n A 1 324 THR 324 301 ? ? ? A . n A 1 325 VAL 325 302 ? ? ? A . n A 1 326 THR 326 303 ? ? ? A . n A 1 327 PRO 327 304 ? ? ? A . n A 1 328 PRO 328 305 ? ? ? A . n A 1 329 ASP 329 306 ? ? ? A . n A 1 330 SER 330 307 ? ? ? A . n A 1 331 GLN 331 308 308 GLN GLN A . n A 1 332 SER 332 309 309 SER SER A . n A 1 333 TYR 333 310 310 TYR TYR A . n A 1 334 ILE 334 311 311 ILE ILE A . n A 1 335 SER 335 312 312 SER SER A . n A 1 336 VAL 336 313 313 VAL VAL A . n A 1 337 ASN 337 314 314 ASN ASN A . n A 1 338 TYR 338 315 315 TYR TYR A . n A 1 339 SER 339 316 316 SER SER A . n A 1 340 VAL 340 317 317 VAL VAL A . n A 1 341 ARG 341 318 318 ARG ARG A . n A 1 342 ILE 342 319 319 ILE ILE A . n A 1 343 ASN 343 320 320 ASN ASN A . n A 1 344 GLU 344 321 321 GLU GLU A . n A 1 345 THR 345 322 322 THR THR A . n A 1 346 TYR 346 323 323 TYR TYR A . n A 1 347 PHE 347 324 324 PHE PHE A . n A 1 348 THR 348 325 325 THR THR A . n A 1 349 ASN 349 326 326 ASN ASN A . n A 1 350 VAL 350 327 327 VAL VAL A . n A 1 351 THR 351 328 328 THR THR A . n A 1 352 VAL 352 329 329 VAL VAL A . n A 1 353 LEU 353 330 330 LEU LEU A . n A 1 354 ASN 354 331 331 ASN ASN A . n A 1 355 GLY 355 332 332 GLY GLY A . n A 1 356 SER 356 333 333 SER SER A . n A 1 357 VAL 357 334 334 VAL VAL A . n A 1 358 PHE 358 335 335 PHE PHE A . n A 1 359 LEU 359 336 336 LEU LEU A . n A 1 360 SER 360 337 337 SER SER A . n A 1 361 VAL 361 338 338 VAL VAL A . n A 1 362 MET 362 339 339 MET MET A . n A 1 363 GLU 363 340 340 GLU GLU A . n A 1 364 LYS 364 341 341 LYS LYS A . n A 1 365 ALA 365 342 342 ALA ALA A . n A 1 366 GLN 366 343 343 GLN GLN A . n A 1 367 LYS 367 344 344 LYS LYS A . n A 1 368 MET 368 345 345 MET MET A . n A 1 369 ASN 369 346 346 ASN ASN A . n A 1 370 ASP 370 347 347 ASP ASP A . n A 1 371 THR 371 348 348 THR THR A . n A 1 372 ILE 372 349 349 ILE ILE A . n A 1 373 PHE 373 350 350 PHE PHE A . n A 1 374 GLY 374 351 351 GLY GLY A . n A 1 375 PHE 375 352 352 PHE PHE A . n A 1 376 THR 376 353 353 THR THR A . n A 1 377 MET 377 354 354 MET MET A . n A 1 378 GLU 378 355 355 GLU GLU A . n A 1 379 GLU 379 356 356 GLU GLU A . n A 1 380 ARG 380 357 357 ARG ARG A . n A 1 381 SER 381 358 358 SER SER A . n A 1 382 TRP 382 359 359 TRP TRP A . n A 1 383 GLY 383 360 360 GLY GLY A . n A 1 384 PRO 384 361 361 PRO PRO A . n A 1 385 TYR 385 362 362 TYR TYR A . n A 1 386 ILE 386 363 363 ILE ILE A . n A 1 387 THR 387 364 364 THR THR A . n A 1 388 CYS 388 365 365 CYS CYS A . n A 1 389 ILE 389 366 366 ILE ILE A . n A 1 390 GLN 390 367 367 GLN GLN A . n A 1 391 GLY 391 368 368 GLY GLY A . n A 1 392 LEU 392 369 369 LEU LEU A . n A 1 393 CYS 393 370 370 CYS CYS A . n A 1 394 ALA 394 371 371 ALA ALA A . n A 1 395 ASN 395 372 372 ASN ASN A . n A 1 396 ASN 396 373 373 ASN ASN A . n A 1 397 ASN 397 374 374 ASN ASN A . n A 1 398 ASP 398 375 375 ASP ASP A . n A 1 399 ARG 399 376 376 ARG ARG A . n A 1 400 THR 400 377 377 THR THR A . n A 1 401 TYR 401 378 378 TYR TYR A . n A 1 402 TRP 402 379 379 TRP TRP A . n A 1 403 GLU 403 380 380 GLU GLU A . n A 1 404 LEU 404 381 381 LEU LEU A . n A 1 405 LEU 405 382 382 LEU LEU A . n A 1 406 SER 406 383 383 SER SER A . n A 1 407 GLY 407 384 384 GLY GLY A . n A 1 408 GLY 408 385 385 GLY GLY A . n A 1 409 GLU 409 386 386 GLU GLU A . n A 1 410 PRO 410 387 387 PRO PRO A . n A 1 411 LEU 411 388 388 LEU LEU A . n A 1 412 SER 412 389 389 SER SER A . n A 1 413 GLN 413 390 390 GLN GLN A . n A 1 414 GLY 414 391 391 GLY GLY A . n A 1 415 ALA 415 392 392 ALA ALA A . n A 1 416 GLY 416 393 393 GLY GLY A . n A 1 417 SER 417 394 394 SER SER A . n A 1 418 TYR 418 395 395 TYR TYR A . n A 1 419 VAL 419 396 396 VAL VAL A . n A 1 420 VAL 420 397 397 VAL VAL A . n A 1 421 ARG 421 398 398 ARG ARG A . n A 1 422 ASN 422 399 399 ASN ASN A . n A 1 423 GLY 423 400 400 GLY GLY A . n A 1 424 GLU 424 401 401 GLU GLU A . n A 1 425 ASN 425 402 402 ASN ASN A . n A 1 426 LEU 426 403 403 LEU LEU A . n A 1 427 GLU 427 404 404 GLU GLU A . n A 1 428 VAL 428 405 405 VAL VAL A . n A 1 429 ARG 429 406 406 ARG ARG A . n A 1 430 TRP 430 407 407 TRP TRP A . n A 1 431 SER 431 408 408 SER SER A . n A 1 432 LYS 432 409 409 LYS LYS A . n A 1 433 TYR 433 410 410 TYR TYR A . n A 1 434 LEU 434 411 411 LEU LEU A . n A 1 435 VAL 435 412 ? ? ? A . n A 1 436 PRO 436 413 ? ? ? A . n A 1 437 ARG 437 414 ? ? ? A . n A 1 438 GLY 438 415 ? ? ? A . n A 1 439 SER 439 416 ? ? ? A . n A 1 440 LEU 440 417 ? ? ? A . n A 1 441 GLU 441 418 ? ? ? A . n A 1 442 SER 442 419 ? ? ? A . n A 1 443 ARG 443 420 ? ? ? A . n A 1 444 GLY 444 421 ? ? ? A . n A 1 445 PRO 445 422 ? ? ? A . n A 1 446 PHE 446 423 ? ? ? A . n A 1 447 GLU 447 424 ? ? ? A . n A 1 448 GLN 448 425 ? ? ? A . n A 1 449 LYS 449 426 ? ? ? A . n A 1 450 LEU 450 427 ? ? ? A . n A 1 451 ILE 451 428 ? ? ? A . n A 1 452 SER 452 429 ? ? ? A . n A 1 453 GLU 453 430 ? ? ? A . n A 1 454 GLU 454 431 ? ? ? A . n A 1 455 ASP 455 432 ? ? ? A . n A 1 456 LEU 456 433 ? ? ? A . n A 1 457 ASN 457 434 ? ? ? A . n A 1 458 MET 458 435 ? ? ? A . n A 1 459 HIS 459 436 ? ? ? A . n A 1 460 THR 460 437 ? ? ? A . n A 1 461 GLY 461 438 ? ? ? A . n A 1 462 HIS 462 439 ? ? ? A . n A 1 463 HIS 463 440 ? ? ? A . n A 1 464 HIS 464 441 ? ? ? A . n A 1 465 HIS 465 442 ? ? ? A . n A 1 466 HIS 466 443 ? ? ? A . n A 1 467 HIS 467 444 ? ? ? 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 NAG 1 501 500 NAG NAG A . C 2 NAG 1 502 502 NAG NAG A . D 2 NAG 1 503 503 NAG NAG A . E 2 NAG 1 504 503 NAG NAG A . F 2 NAG 1 505 504 NAG NAG A . G 2 NAG 1 506 506 NAG NAG A . H 2 NAG 1 507 506 NAG NAG A . I 3 CNC 1 508 507 CNC CNC A . J 4 CA 1 509 1 CA CA A . K 5 PEG 1 510 1 PEG PEG A . L 5 PEG 1 511 2 PEG PEG A . M 5 PEG 1 512 3 PEG PEG A . N 5 PEG 1 513 4 PEG PEG A . O 5 PEG 1 514 5 PEG PEG A . P 5 PEG 1 515 7 PEG PEG A . Q 5 PEG 1 516 8 PEG PEG A . R 5 PEG 1 517 10 PEG PEG A . S 5 PEG 1 518 11 PEG PEG A . T 5 PEG 1 519 12 PEG PEG A . U 5 PEG 1 520 13 PEG PEG A . V 6 HOH 1 601 1 HOH HOH A . V 6 HOH 2 602 2 HOH HOH A . V 6 HOH 3 603 3 HOH HOH A . V 6 HOH 4 604 4 HOH HOH A . V 6 HOH 5 605 8 HOH HOH A . V 6 HOH 6 606 9 HOH HOH A . V 6 HOH 7 607 11 HOH HOH A . V 6 HOH 8 608 12 HOH HOH A . V 6 HOH 9 609 14 HOH HOH A . V 6 HOH 10 610 15 HOH HOH A . V 6 HOH 11 611 16 HOH HOH A . V 6 HOH 12 612 17 HOH HOH A . V 6 HOH 13 613 18 HOH HOH A . V 6 HOH 14 614 19 HOH HOH A . V 6 HOH 15 615 20 HOH HOH A . V 6 HOH 16 616 23 HOH HOH A . V 6 HOH 17 617 24 HOH HOH A . V 6 HOH 18 618 26 HOH HOH A . V 6 HOH 19 619 27 HOH HOH A . V 6 HOH 20 620 29 HOH HOH A . V 6 HOH 21 621 30 HOH HOH A . V 6 HOH 22 622 31 HOH HOH A . V 6 HOH 23 623 32 HOH HOH A . V 6 HOH 24 624 34 HOH HOH A . V 6 HOH 25 625 35 HOH HOH A . V 6 HOH 26 626 36 HOH HOH A . V 6 HOH 27 627 38 HOH HOH A . V 6 HOH 28 628 39 HOH HOH A . V 6 HOH 29 629 40 HOH HOH A . V 6 HOH 30 630 42 HOH HOH A . V 6 HOH 31 631 44 HOH HOH A . V 6 HOH 32 632 45 HOH HOH A . V 6 HOH 33 633 46 HOH HOH A . V 6 HOH 34 634 47 HOH HOH A . V 6 HOH 35 635 48 HOH HOH A . V 6 HOH 36 636 49 HOH HOH A . V 6 HOH 37 637 51 HOH HOH A . V 6 HOH 38 638 53 HOH HOH A . V 6 HOH 39 639 55 HOH HOH A . V 6 HOH 40 640 57 HOH HOH A . V 6 HOH 41 641 58 HOH HOH A . V 6 HOH 42 642 59 HOH HOH A . V 6 HOH 43 643 60 HOH HOH A . V 6 HOH 44 644 61 HOH HOH A . V 6 HOH 45 645 62 HOH HOH A . V 6 HOH 46 646 63 HOH HOH A . V 6 HOH 47 647 64 HOH HOH A . V 6 HOH 48 648 66 HOH HOH A . V 6 HOH 49 649 67 HOH HOH A . V 6 HOH 50 650 68 HOH HOH A . V 6 HOH 51 651 69 HOH HOH A . V 6 HOH 52 652 70 HOH HOH A . V 6 HOH 53 653 71 HOH HOH A . V 6 HOH 54 654 72 HOH HOH A . V 6 HOH 55 655 74 HOH HOH A . V 6 HOH 56 656 75 HOH HOH A . V 6 HOH 57 657 76 HOH HOH A . V 6 HOH 58 658 77 HOH HOH A . V 6 HOH 59 659 659 HOH HOH A . V 6 HOH 60 660 80 HOH HOH A . V 6 HOH 61 661 81 HOH HOH A . V 6 HOH 62 662 82 HOH HOH A . V 6 HOH 63 663 83 HOH HOH A . V 6 HOH 64 664 85 HOH HOH A . V 6 HOH 65 665 86 HOH HOH A . V 6 HOH 66 666 87 HOH HOH A . V 6 HOH 67 667 88 HOH HOH A . V 6 HOH 68 668 89 HOH HOH A . V 6 HOH 69 669 90 HOH HOH A . V 6 HOH 70 670 91 HOH HOH A . V 6 HOH 71 671 97 HOH HOH A . V 6 HOH 72 672 100 HOH HOH A . V 6 HOH 73 673 105 HOH HOH A . V 6 HOH 74 674 106 HOH HOH A . V 6 HOH 75 675 109 HOH HOH A . V 6 HOH 76 676 110 HOH HOH A . V 6 HOH 77 677 111 HOH HOH A . V 6 HOH 78 678 112 HOH HOH A . V 6 HOH 79 679 114 HOH HOH A . V 6 HOH 80 680 115 HOH HOH A . V 6 HOH 81 681 116 HOH HOH A . V 6 HOH 82 682 117 HOH HOH A . V 6 HOH 83 683 118 HOH HOH A . V 6 HOH 84 684 119 HOH HOH A . V 6 HOH 85 685 120 HOH HOH A . V 6 HOH 86 686 122 HOH HOH A . V 6 HOH 87 687 123 HOH HOH A . V 6 HOH 88 688 124 HOH HOH A . V 6 HOH 89 689 689 HOH HOH A . V 6 HOH 90 690 690 HOH HOH A . V 6 HOH 91 691 132 HOH HOH A . V 6 HOH 92 692 692 HOH HOH A . V 6 HOH 93 693 136 HOH HOH A . V 6 HOH 94 694 138 HOH HOH A . V 6 HOH 95 695 139 HOH HOH A . V 6 HOH 96 696 140 HOH HOH A . V 6 HOH 97 697 142 HOH HOH A . V 6 HOH 98 698 146 HOH HOH A . V 6 HOH 99 699 147 HOH HOH A . V 6 HOH 100 700 148 HOH HOH A . V 6 HOH 101 701 701 HOH HOH A . V 6 HOH 102 702 152 HOH HOH A . V 6 HOH 103 703 153 HOH HOH A . V 6 HOH 104 704 154 HOH HOH A . V 6 HOH 105 705 157 HOH HOH A . V 6 HOH 106 706 158 HOH HOH A . V 6 HOH 107 707 159 HOH HOH A . V 6 HOH 108 708 160 HOH HOH A . V 6 HOH 109 709 162 HOH HOH A . V 6 HOH 110 710 163 HOH HOH A . V 6 HOH 111 711 166 HOH HOH A . V 6 HOH 112 712 167 HOH HOH A . V 6 HOH 113 713 169 HOH HOH A . V 6 HOH 114 714 714 HOH HOH A . V 6 HOH 115 715 173 HOH HOH A . V 6 HOH 116 716 174 HOH HOH A . V 6 HOH 117 717 717 HOH HOH A . V 6 HOH 118 718 176 HOH HOH A . V 6 HOH 119 719 178 HOH HOH A . V 6 HOH 120 720 179 HOH HOH A . V 6 HOH 121 721 180 HOH HOH A . V 6 HOH 122 722 181 HOH HOH A . V 6 HOH 123 723 182 HOH HOH A . V 6 HOH 124 724 183 HOH HOH A . V 6 HOH 125 725 185 HOH HOH A . V 6 HOH 126 726 186 HOH HOH A . V 6 HOH 127 727 187 HOH HOH A . V 6 HOH 128 728 188 HOH HOH A . V 6 HOH 129 729 189 HOH HOH A . V 6 HOH 130 730 190 HOH HOH A . V 6 HOH 131 731 191 HOH HOH A . V 6 HOH 132 732 192 HOH HOH A . V 6 HOH 133 733 193 HOH HOH A . V 6 HOH 134 734 194 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 343 A ASN 320 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 354 A ASN 331 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 316 A ASN 293 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 337 A ASN 314 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 369 A ASN 346 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 216 A ASN 193 ? ASN 'GLYCOSYLATION SITE' 7 A ASN 349 A ASN 326 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # 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 2013-07-17 2 'Structure model' 1 1 2013-10-09 3 'Structure model' 1 2 2017-11-15 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Database references' 2 3 'Structure model' 'Refinement description' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 3 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category software # _pdbx_audit_revision_item.ordinal 1 _pdbx_audit_revision_item.revision_ordinal 3 _pdbx_audit_revision_item.data_content_type 'Structure model' _pdbx_audit_revision_item.item '_software.name' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined -27.5530 48.9720 17.5992 0.2079 0.2563 0.2608 -0.0150 -0.0258 0.0390 1.4661 2.0136 1.8127 -0.2342 -0.4233 0.3249 -0.0580 -0.0157 -0.1887 0.0238 -0.0259 0.0503 -0.0191 -0.0897 0.0000 'X-RAY DIFFRACTION' 2 ? refined -1.3877 45.4848 13.6403 0.3184 0.6871 0.4658 -0.0220 -0.0233 0.0268 1.0385 0.3311 0.3384 0.0801 0.5985 0.2290 -0.1437 0.0562 -0.0427 0.0460 0.0877 -0.0933 0.0943 0.4252 0.0000 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '(chain A and resid 1:294)' 'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '(chain A and resid 331:411)' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal RemDAq 'data collection' . ? 1 PHASER phasing . ? 2 PHENIX refinement '(phenix.refine: 1.8.1_1168)' ? 3 XDS 'data reduction' . ? 4 XDS 'data scaling' . ? 5 # 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 SER A 62 ? ? -156.29 12.89 2 1 ARG A 63 ? ? -159.46 14.80 3 1 THR A 119 ? ? -115.16 -91.95 4 1 ASN A 181 ? ? -76.72 -165.25 5 1 ASN A 217 ? ? -120.65 -169.16 6 1 PHE A 258 ? ? -108.37 43.70 7 1 ASP A 282 ? ? -96.55 59.63 8 1 SER A 283 ? ? 77.79 122.84 9 1 SER A 284 ? ? -159.03 -1.80 10 1 SER A 309 ? ? 70.98 143.26 11 1 ILE A 319 ? ? -117.33 -83.37 12 1 ASN A 320 ? ? -109.96 -60.39 13 1 ASN A 346 ? ? -161.75 99.66 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A MET -22 ? A MET 1 2 1 Y 1 A ARG -21 ? A ARG 2 3 1 Y 1 A GLN -20 ? A GLN 3 4 1 Y 1 A SER -19 ? A SER 4 5 1 Y 1 A HIS -18 ? A HIS 5 6 1 Y 1 A GLN -17 ? A GLN 6 7 1 Y 1 A LEU -16 ? A LEU 7 8 1 Y 1 A PRO -15 ? A PRO 8 9 1 Y 1 A LEU -14 ? A LEU 9 10 1 Y 1 A VAL -13 ? A VAL 10 11 1 Y 1 A GLY -12 ? A GLY 11 12 1 Y 1 A LEU -11 ? A LEU 12 13 1 Y 1 A LEU -10 ? A LEU 13 14 1 Y 1 A LEU -9 ? A LEU 14 15 1 Y 1 A PHE -8 ? A PHE 15 16 1 Y 1 A SER -7 ? A SER 16 17 1 Y 1 A PHE -6 ? A PHE 17 18 1 Y 1 A ILE -5 ? A ILE 18 19 1 Y 1 A PRO -4 ? A PRO 19 20 1 Y 1 A SER -3 ? A SER 20 21 1 Y 1 A GLN -2 ? A GLN 21 22 1 Y 1 A LEU -1 ? A LEU 22 23 1 Y 1 A CYS 0 ? A CYS 23 24 1 Y 1 A SER 295 ? A SER 318 25 1 Y 1 A ALA 296 ? A ALA 319 26 1 Y 1 A ASP 297 ? A ASP 320 27 1 Y 1 A GLU 298 ? A GLU 321 28 1 Y 1 A PRO 299 ? A PRO 322 29 1 Y 1 A ILE 300 ? A ILE 323 30 1 Y 1 A THR 301 ? A THR 324 31 1 Y 1 A VAL 302 ? A VAL 325 32 1 Y 1 A THR 303 ? A THR 326 33 1 Y 1 A PRO 304 ? A PRO 327 34 1 Y 1 A PRO 305 ? A PRO 328 35 1 Y 1 A ASP 306 ? A ASP 329 36 1 Y 1 A SER 307 ? A SER 330 37 1 Y 1 A VAL 412 ? A VAL 435 38 1 Y 1 A PRO 413 ? A PRO 436 39 1 Y 1 A ARG 414 ? A ARG 437 40 1 Y 1 A GLY 415 ? A GLY 438 41 1 Y 1 A SER 416 ? A SER 439 42 1 Y 1 A LEU 417 ? A LEU 440 43 1 Y 1 A GLU 418 ? A GLU 441 44 1 Y 1 A SER 419 ? A SER 442 45 1 Y 1 A ARG 420 ? A ARG 443 46 1 Y 1 A GLY 421 ? A GLY 444 47 1 Y 1 A PRO 422 ? A PRO 445 48 1 Y 1 A PHE 423 ? A PHE 446 49 1 Y 1 A GLU 424 ? A GLU 447 50 1 Y 1 A GLN 425 ? A GLN 448 51 1 Y 1 A LYS 426 ? A LYS 449 52 1 Y 1 A LEU 427 ? A LEU 450 53 1 Y 1 A ILE 428 ? A ILE 451 54 1 Y 1 A SER 429 ? A SER 452 55 1 Y 1 A GLU 430 ? A GLU 453 56 1 Y 1 A GLU 431 ? A GLU 454 57 1 Y 1 A ASP 432 ? A ASP 455 58 1 Y 1 A LEU 433 ? A LEU 456 59 1 Y 1 A ASN 434 ? A ASN 457 60 1 Y 1 A MET 435 ? A MET 458 61 1 Y 1 A HIS 436 ? A HIS 459 62 1 Y 1 A THR 437 ? A THR 460 63 1 Y 1 A GLY 438 ? A GLY 461 64 1 Y 1 A HIS 439 ? A HIS 462 65 1 Y 1 A HIS 440 ? A HIS 463 66 1 Y 1 A HIS 441 ? A HIS 464 67 1 Y 1 A HIS 442 ? A HIS 465 68 1 Y 1 A HIS 443 ? A HIS 466 69 1 Y 1 A HIS 444 ? A HIS 467 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 CO-CYANOCOBALAMIN CNC 4 'CALCIUM ION' CA 5 'DI(HYDROXYETHYL)ETHER' PEG 6 water HOH #