data_4FZ1 # _entry.id 4FZ1 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.281 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4FZ1 RCSB RCSB073530 WWPDB D_1000073530 # _pdbx_database_related.db_name PDB _pdbx_database_related.db_id 4FZ0 _pdbx_database_related.details . _pdbx_database_related.content_type unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4FZ1 _pdbx_database_status.recvd_initial_deposition_date 2012-07-05 _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 'Baconguis, I.' 1 'Gouaux, E.' 2 # _citation.id primary _citation.title 'Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes.' _citation.journal_abbrev Nature _citation.journal_volume 489 _citation.page_first 400 _citation.page_last 405 _citation.year 2012 _citation.journal_id_ASTM NATUAS _citation.country UK _citation.journal_id_ISSN 0028-0836 _citation.journal_id_CSD 0006 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 22842900 _citation.pdbx_database_id_DOI 10.1038/nature11375 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Baconguis, I.' 1 primary 'Gouaux, E.' 2 # _cell.entry_id 4FZ1 _cell.length_a 131.520 _cell.length_b 131.520 _cell.length_c 129.920 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 9 _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 4FZ1 _symmetry.space_group_name_H-M 'H 3' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 146 _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 'Acid-sensing ion channel 1' 51327.352 1 ? ? 'UNP residues 14-463' ? 2 polymer syn Pi-theraphotoxin-Pc1a 4705.513 1 ? ? 'UNP residues 1-40' ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 2 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'ASIC1, Amiloride-sensitive cation channel 2, neuronal' 2 'Pi-TRTX-Pc1a, PcTx1, Psalmotoxin-1' # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 'polypeptide(L)' no no ;GQPVSIQAFASSSTLHGISHIFSYERLSLKRVVWALCFMGSLALLALVCTNRIQYYFLYPHVTKLDEVAATRLTFPAVTF CNLNEFRFSRVTKNDLYHAGELLALLNNRYEIPDTQTADEKQLEILQDKANFRNFKPKPFNMLEFYDRAGHDIREMLLSC FFRGEQCSPEDFKVVFTRYGKCYTFNAGQDGKPRLITMKGGTGNGLEIMLDIQQDEYLPVWGETDETSFEAGIKVQIHSQ DEPPLIDQLGFGVAPGFQTFVSCQEQRLIYLPPPWGDCKATTGDSEFYDTYSITACRIDCETRYLVENCNCRMVHMPGDA PYCTPEQYKECADPALDFLVEKDNEYCVCEMPCNVTRYGKELSMVKIPSKASAKYLAKKYNKSEQYIGENILVLDIFFEA LNYETIEQKKAYEVAGLLGDIGGQMGLFIGASILTVLELFDYAYEVIKHR ; ;GQPVSIQAFASSSTLHGISHIFSYERLSLKRVVWALCFMGSLALLALVCTNRIQYYFLYPHVTKLDEVAATRLTFPAVTF CNLNEFRFSRVTKNDLYHAGELLALLNNRYEIPDTQTADEKQLEILQDKANFRNFKPKPFNMLEFYDRAGHDIREMLLSC FFRGEQCSPEDFKVVFTRYGKCYTFNAGQDGKPRLITMKGGTGNGLEIMLDIQQDEYLPVWGETDETSFEAGIKVQIHSQ DEPPLIDQLGFGVAPGFQTFVSCQEQRLIYLPPPWGDCKATTGDSEFYDTYSITACRIDCETRYLVENCNCRMVHMPGDA PYCTPEQYKECADPALDFLVEKDNEYCVCEMPCNVTRYGKELSMVKIPSKASAKYLAKKYNKSEQYIGENILVLDIFFEA LNYETIEQKKAYEVAGLLGDIGGQMGLFIGASILTVLELFDYAYEVIKHR ; A ? 2 'polypeptide(L)' no no EDCIPKWKGCVNRHGDCCEGLECWKRRRSFEVCVPKTPKT EDCIPKWKGCVNRHGDCCEGLECWKRRRSFEVCVPKTPKT D ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 GLY n 1 2 GLN n 1 3 PRO n 1 4 VAL n 1 5 SER n 1 6 ILE n 1 7 GLN n 1 8 ALA n 1 9 PHE n 1 10 ALA n 1 11 SER n 1 12 SER n 1 13 SER n 1 14 THR n 1 15 LEU n 1 16 HIS n 1 17 GLY n 1 18 ILE n 1 19 SER n 1 20 HIS n 1 21 ILE n 1 22 PHE n 1 23 SER n 1 24 TYR n 1 25 GLU n 1 26 ARG n 1 27 LEU n 1 28 SER n 1 29 LEU n 1 30 LYS n 1 31 ARG n 1 32 VAL n 1 33 VAL n 1 34 TRP n 1 35 ALA n 1 36 LEU n 1 37 CYS n 1 38 PHE n 1 39 MET n 1 40 GLY n 1 41 SER n 1 42 LEU n 1 43 ALA n 1 44 LEU n 1 45 LEU n 1 46 ALA n 1 47 LEU n 1 48 VAL n 1 49 CYS n 1 50 THR n 1 51 ASN n 1 52 ARG n 1 53 ILE n 1 54 GLN n 1 55 TYR n 1 56 TYR n 1 57 PHE n 1 58 LEU n 1 59 TYR n 1 60 PRO n 1 61 HIS n 1 62 VAL n 1 63 THR n 1 64 LYS n 1 65 LEU n 1 66 ASP n 1 67 GLU n 1 68 VAL n 1 69 ALA n 1 70 ALA n 1 71 THR n 1 72 ARG n 1 73 LEU n 1 74 THR n 1 75 PHE n 1 76 PRO n 1 77 ALA n 1 78 VAL n 1 79 THR n 1 80 PHE n 1 81 CYS n 1 82 ASN n 1 83 LEU n 1 84 ASN n 1 85 GLU n 1 86 PHE n 1 87 ARG n 1 88 PHE n 1 89 SER n 1 90 ARG n 1 91 VAL n 1 92 THR n 1 93 LYS n 1 94 ASN n 1 95 ASP n 1 96 LEU n 1 97 TYR n 1 98 HIS n 1 99 ALA n 1 100 GLY n 1 101 GLU n 1 102 LEU n 1 103 LEU n 1 104 ALA n 1 105 LEU n 1 106 LEU n 1 107 ASN n 1 108 ASN n 1 109 ARG n 1 110 TYR n 1 111 GLU n 1 112 ILE n 1 113 PRO n 1 114 ASP n 1 115 THR n 1 116 GLN n 1 117 THR n 1 118 ALA n 1 119 ASP n 1 120 GLU n 1 121 LYS n 1 122 GLN n 1 123 LEU n 1 124 GLU n 1 125 ILE n 1 126 LEU n 1 127 GLN n 1 128 ASP n 1 129 LYS n 1 130 ALA n 1 131 ASN n 1 132 PHE n 1 133 ARG n 1 134 ASN n 1 135 PHE n 1 136 LYS n 1 137 PRO n 1 138 LYS n 1 139 PRO n 1 140 PHE n 1 141 ASN n 1 142 MET n 1 143 LEU n 1 144 GLU n 1 145 PHE n 1 146 TYR n 1 147 ASP n 1 148 ARG n 1 149 ALA n 1 150 GLY n 1 151 HIS n 1 152 ASP n 1 153 ILE n 1 154 ARG n 1 155 GLU n 1 156 MET n 1 157 LEU n 1 158 LEU n 1 159 SER n 1 160 CYS n 1 161 PHE n 1 162 PHE n 1 163 ARG n 1 164 GLY n 1 165 GLU n 1 166 GLN n 1 167 CYS n 1 168 SER n 1 169 PRO n 1 170 GLU n 1 171 ASP n 1 172 PHE n 1 173 LYS n 1 174 VAL n 1 175 VAL n 1 176 PHE n 1 177 THR n 1 178 ARG n 1 179 TYR n 1 180 GLY n 1 181 LYS n 1 182 CYS n 1 183 TYR n 1 184 THR n 1 185 PHE n 1 186 ASN n 1 187 ALA n 1 188 GLY n 1 189 GLN n 1 190 ASP n 1 191 GLY n 1 192 LYS n 1 193 PRO n 1 194 ARG n 1 195 LEU n 1 196 ILE n 1 197 THR n 1 198 MET n 1 199 LYS n 1 200 GLY n 1 201 GLY n 1 202 THR n 1 203 GLY n 1 204 ASN n 1 205 GLY n 1 206 LEU n 1 207 GLU n 1 208 ILE n 1 209 MET n 1 210 LEU n 1 211 ASP n 1 212 ILE n 1 213 GLN n 1 214 GLN n 1 215 ASP n 1 216 GLU n 1 217 TYR n 1 218 LEU n 1 219 PRO n 1 220 VAL n 1 221 TRP n 1 222 GLY n 1 223 GLU n 1 224 THR n 1 225 ASP n 1 226 GLU n 1 227 THR n 1 228 SER n 1 229 PHE n 1 230 GLU n 1 231 ALA n 1 232 GLY n 1 233 ILE n 1 234 LYS n 1 235 VAL n 1 236 GLN n 1 237 ILE n 1 238 HIS n 1 239 SER n 1 240 GLN n 1 241 ASP n 1 242 GLU n 1 243 PRO n 1 244 PRO n 1 245 LEU n 1 246 ILE n 1 247 ASP n 1 248 GLN n 1 249 LEU n 1 250 GLY n 1 251 PHE n 1 252 GLY n 1 253 VAL n 1 254 ALA n 1 255 PRO n 1 256 GLY n 1 257 PHE n 1 258 GLN n 1 259 THR n 1 260 PHE n 1 261 VAL n 1 262 SER n 1 263 CYS n 1 264 GLN n 1 265 GLU n 1 266 GLN n 1 267 ARG n 1 268 LEU n 1 269 ILE n 1 270 TYR n 1 271 LEU n 1 272 PRO n 1 273 PRO n 1 274 PRO n 1 275 TRP n 1 276 GLY n 1 277 ASP n 1 278 CYS n 1 279 LYS n 1 280 ALA n 1 281 THR n 1 282 THR n 1 283 GLY n 1 284 ASP n 1 285 SER n 1 286 GLU n 1 287 PHE n 1 288 TYR n 1 289 ASP n 1 290 THR n 1 291 TYR n 1 292 SER n 1 293 ILE n 1 294 THR n 1 295 ALA n 1 296 CYS n 1 297 ARG n 1 298 ILE n 1 299 ASP n 1 300 CYS n 1 301 GLU n 1 302 THR n 1 303 ARG n 1 304 TYR n 1 305 LEU n 1 306 VAL n 1 307 GLU n 1 308 ASN n 1 309 CYS n 1 310 ASN n 1 311 CYS n 1 312 ARG n 1 313 MET n 1 314 VAL n 1 315 HIS n 1 316 MET n 1 317 PRO n 1 318 GLY n 1 319 ASP n 1 320 ALA n 1 321 PRO n 1 322 TYR n 1 323 CYS n 1 324 THR n 1 325 PRO n 1 326 GLU n 1 327 GLN n 1 328 TYR n 1 329 LYS n 1 330 GLU n 1 331 CYS n 1 332 ALA n 1 333 ASP n 1 334 PRO n 1 335 ALA n 1 336 LEU n 1 337 ASP n 1 338 PHE n 1 339 LEU n 1 340 VAL n 1 341 GLU n 1 342 LYS n 1 343 ASP n 1 344 ASN n 1 345 GLU n 1 346 TYR n 1 347 CYS n 1 348 VAL n 1 349 CYS n 1 350 GLU n 1 351 MET n 1 352 PRO n 1 353 CYS n 1 354 ASN n 1 355 VAL n 1 356 THR n 1 357 ARG n 1 358 TYR n 1 359 GLY n 1 360 LYS n 1 361 GLU n 1 362 LEU n 1 363 SER n 1 364 MET n 1 365 VAL n 1 366 LYS n 1 367 ILE n 1 368 PRO n 1 369 SER n 1 370 LYS n 1 371 ALA n 1 372 SER n 1 373 ALA n 1 374 LYS n 1 375 TYR n 1 376 LEU n 1 377 ALA n 1 378 LYS n 1 379 LYS n 1 380 TYR n 1 381 ASN n 1 382 LYS n 1 383 SER n 1 384 GLU n 1 385 GLN n 1 386 TYR n 1 387 ILE n 1 388 GLY n 1 389 GLU n 1 390 ASN n 1 391 ILE n 1 392 LEU n 1 393 VAL n 1 394 LEU n 1 395 ASP n 1 396 ILE n 1 397 PHE n 1 398 PHE n 1 399 GLU n 1 400 ALA n 1 401 LEU n 1 402 ASN n 1 403 TYR n 1 404 GLU n 1 405 THR n 1 406 ILE n 1 407 GLU n 1 408 GLN n 1 409 LYS n 1 410 LYS n 1 411 ALA n 1 412 TYR n 1 413 GLU n 1 414 VAL n 1 415 ALA n 1 416 GLY n 1 417 LEU n 1 418 LEU n 1 419 GLY n 1 420 ASP n 1 421 ILE n 1 422 GLY n 1 423 GLY n 1 424 GLN n 1 425 MET n 1 426 GLY n 1 427 LEU n 1 428 PHE n 1 429 ILE n 1 430 GLY n 1 431 ALA n 1 432 SER n 1 433 ILE n 1 434 LEU n 1 435 THR n 1 436 VAL n 1 437 LEU n 1 438 GLU n 1 439 LEU n 1 440 PHE n 1 441 ASP n 1 442 TYR n 1 443 ALA n 1 444 TYR n 1 445 GLU n 1 446 VAL n 1 447 ILE n 1 448 LYS n 1 449 HIS n 1 450 ARG n 2 1 GLU n 2 2 ASP n 2 3 CYS n 2 4 ILE n 2 5 PRO n 2 6 LYS n 2 7 TRP n 2 8 LYS n 2 9 GLY n 2 10 CYS n 2 11 VAL n 2 12 ASN n 2 13 ARG n 2 14 HIS n 2 15 GLY n 2 16 ASP n 2 17 CYS n 2 18 CYS n 2 19 GLU n 2 20 GLY n 2 21 LEU n 2 22 GLU n 2 23 CYS n 2 24 TRP n 2 25 LYS n 2 26 ARG n 2 27 ARG n 2 28 ARG n 2 29 SER n 2 30 PHE n 2 31 GLU n 2 32 VAL n 2 33 CYS n 2 34 VAL n 2 35 PRO n 2 36 LYS n 2 37 THR n 2 38 PRO n 2 39 LYS n 2 40 THR 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 bantam,chickens _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'ASIC1, ACCN2' _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 'Gallus gallus' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9031 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name 'fall armyworm' _entity_src_gen.pdbx_host_org_scientific_name 'SPODOPTERA FRUGIPERDA' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7108 _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 Sf9 _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 ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _pdbx_entity_src_syn.entity_id 2 _pdbx_entity_src_syn.pdbx_src_id 1 _pdbx_entity_src_syn.pdbx_alt_source_flag sample _pdbx_entity_src_syn.pdbx_beg_seq_num ? _pdbx_entity_src_syn.pdbx_end_seq_num ? _pdbx_entity_src_syn.organism_scientific 'Psalmopoeus cambridgei' _pdbx_entity_src_syn.organism_common_name 'Trinidad chevron tarantula' _pdbx_entity_src_syn.ncbi_taxonomy_id 179874 _pdbx_entity_src_syn.details synthetic # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_isoform 1 UNP ASIC1_CHICK Q1XA76 1 ;GQPVSIQAFASSSTLHGISHIFSYERLSLKRVVWALCFMGSLALLALVCTNRIQYYFLYPHVTKLDEVAATRLTFPAVTF CNLNEFRFSRVTKNDLYHAGELLALLNNRYEIPDTQTADEKQLEILQDKANFRNFKPKPFNMLEFYDRAGHDIREMLLSC FFRGEQCSPEDFKVVFTRYGKCYTFNAGQDGKPRLITMKGGTGNGLEIMLDIQQDEYLPVWGETDETSFEAGIKVQIHSQ DEPPLIDQLGFGVAPGFQTFVSCQEQRLIYLPPPWGDCKATTGDSEFYDTYSITACRIDCETRYLVENCNCRMVHMPGDA PYCTPEQYKECADPALDFLVEKDNEYCVCEMPCNVTRYGKELSMVKIPSKASAKYLAKKYNKSEQYIGENILVLDIFFEA LNYETIEQKKAYEVAGLLGDIGGQMGLFIGASILTVLELFDYAYEVIKHR ; 14 ? 2 UNP TXP1_PSACA P60514 2 EDCIPKWKGCVNRHGDCCEGLECWKRRRSFEVCVPKTPKT 1 ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 4FZ1 A 1 ? 450 ? Q1XA76 14 ? 463 ? 14 463 2 2 4FZ1 D 1 ? 40 ? P60514 1 ? 40 ? 1 40 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 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 4FZ1 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.86 _exptl_crystal.density_percent_sol 68.13 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 277 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.25 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '20 mM Tris, 14-18% PEG 550 MME, pH 7.25, VAPOR DIFFUSION, HANGING DROP, temperature 277K' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC QUANTUM 315' _diffrn_detector.pdbx_collection_date 2011-04-24 _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 'DOUBLE-CRYSTAL, SI(111)' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.000 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ALS BEAMLINE 5.0.2' _diffrn_source.pdbx_synchrotron_site ALS _diffrn_source.pdbx_synchrotron_beamline 5.0.2 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.000 # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4FZ1 _reflns.observed_criterion_sigma_I -3.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 50.00 _reflns.d_resolution_high 3.35 _reflns.number_obs 11369 _reflns.number_all 11371 _reflns.percent_possible_obs 95.4 _reflns.pdbx_Rmerge_I_obs 0.064 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 22.9 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 3.35 _reflns_shell.d_res_low 3.47 _reflns_shell.percent_possible_all 97.0 _reflns_shell.Rmerge_I_obs 0.904 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 1.4 _reflns_shell.pdbx_redundancy 4.0 _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 4FZ1 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 11369 _refine.ls_number_reflns_all 11371 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.97 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 42.823 _refine.ls_d_res_high 3.359 _refine.ls_percent_reflns_obs 95.25 _refine.ls_R_factor_obs 0.2226 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.2159 _refine.ls_R_factor_R_free 0.2808 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 9.96 _refine.ls_number_reflns_R_free 1132 _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] 0.0000 _refine.aniso_B[2][2] 0.0000 _refine.aniso_B[3][3] 0.0000 _refine.aniso_B[1][2] 0.0000 _refine.aniso_B[1][3] 0.0000 _refine.aniso_B[2][3] 0.0000 _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol 0.253 _refine.solvent_model_param_bsol 120.003 _refine.pdbx_solvent_vdw_probe_radii 1.10 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.83 _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model ? _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 0.40 _refine.pdbx_overall_phase_error 27.78 _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 3175 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 28 _refine_hist.number_atoms_solvent 0 _refine_hist.number_atoms_total 3203 _refine_hist.d_res_high 3.359 _refine_hist.d_res_low 42.823 # 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 0.009 ? ? 3288 'X-RAY DIFFRACTION' ? f_angle_d 1.283 ? ? 4501 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 17.561 ? ? 1096 'X-RAY DIFFRACTION' ? f_chiral_restr 0.079 ? ? 509 'X-RAY DIFFRACTION' ? f_plane_restr 0.006 ? ? 595 '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' . 3.3594 3.5122 1263 0.2678 95.00 0.3095 . . 142 . . . . 'X-RAY DIFFRACTION' . 3.5122 3.6973 1304 0.2717 97.00 0.2840 . . 142 . . . . 'X-RAY DIFFRACTION' . 3.6973 3.9288 1296 0.2265 96.00 0.2858 . . 144 . . . . 'X-RAY DIFFRACTION' . 3.9288 4.2319 1281 0.1943 96.00 0.2931 . . 144 . . . . 'X-RAY DIFFRACTION' . 4.2319 4.6573 1302 0.1684 96.00 0.2105 . . 143 . . . . 'X-RAY DIFFRACTION' . 4.6573 5.3302 1272 0.1644 96.00 0.2194 . . 137 . . . . 'X-RAY DIFFRACTION' . 5.3302 6.7113 1281 0.2300 95.00 0.3328 . . 139 . . . . 'X-RAY DIFFRACTION' . 6.7113 42.8267 1238 0.2349 92.00 0.2968 . . 141 . . . . # _pdbx_refine.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine.entry_id 4FZ1 _pdbx_refine.R_factor_all_no_cutoff ? _pdbx_refine.R_factor_obs_no_cutoff ? _pdbx_refine.free_R_factor_no_cutoff ? _pdbx_refine.free_R_error_no_cutoff ? _pdbx_refine.free_R_val_test_set_size_perc_no_cutoff ? _pdbx_refine.free_R_val_test_set_ct_no_cutoff ? _pdbx_refine.R_factor_all_4sig_cutoff ? _pdbx_refine.R_factor_obs_4sig_cutoff ? _pdbx_refine.free_R_factor_4sig_cutoff ? _pdbx_refine.free_R_val_test_set_size_perc_4sig_cutoff ? _pdbx_refine.free_R_val_test_set_ct_4sig_cutoff ? _pdbx_refine.number_reflns_obs_4sig_cutoff ? # _struct.entry_id 4FZ1 _struct.title 'Crystal structure of acid-sensing ion channel in complex with psalmotoxin 1 at high pH' _struct.pdbx_descriptor 'Acid-sensing ion channel 1, Pi-theraphotoxin-Pc1a' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4FZ1 _struct_keywords.pdbx_keywords 'TRANSPORT PROTEIN' _struct_keywords.text 'inhibitor cystine knot, 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 3 ? D N N 3 ? # _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 28 ? TYR A 56 ? SER A 41 TYR A 69 1 ? 29 HELX_P HELX_P2 2 THR A 92 ? ALA A 99 ? THR A 105 ALA A 112 1 ? 8 HELX_P HELX_P3 3 LYS A 121 ? ASP A 128 ? LYS A 134 ASP A 141 1 ? 8 HELX_P HELX_P4 4 ASN A 141 ? GLY A 150 ? ASN A 154 GLY A 163 1 ? 10 HELX_P HELX_P5 5 ASP A 152 ? MET A 156 ? ASP A 165 MET A 169 1 ? 5 HELX_P HELX_P6 6 SER A 168 ? GLU A 170 ? SER A 181 GLU A 183 5 ? 3 HELX_P HELX_P7 7 GLN A 213 ? TYR A 217 ? GLN A 226 TYR A 230 5 ? 5 HELX_P HELX_P8 8 LEU A 245 ? GLY A 250 ? LEU A 258 GLY A 263 1 ? 6 HELX_P HELX_P9 9 SER A 292 ? ASN A 310 ? SER A 305 ASN A 323 1 ? 19 HELX_P HELX_P10 10 THR A 324 ? CYS A 331 ? THR A 337 CYS A 344 1 ? 8 HELX_P HELX_P11 11 CYS A 331 ? GLU A 341 ? CYS A 344 GLU A 354 1 ? 11 HELX_P HELX_P12 12 SER A 372 ? TYR A 380 ? SER A 385 TYR A 393 1 ? 9 HELX_P HELX_P13 13 SER A 383 ? ASN A 390 ? SER A 396 ASN A 403 1 ? 8 HELX_P HELX_P14 14 GLU A 413 ? LEU A 437 ? GLU A 426 LEU A 450 1 ? 25 # _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 81 SG ? ? ? 1_555 A CYS 182 SG ? ? A CYS 94 A CYS 195 1_555 ? ? ? ? ? ? ? 2.047 ? disulf2 disulf ? ? A CYS 160 SG ? ? ? 1_555 A CYS 167 SG ? ? A CYS 173 A CYS 180 1_555 ? ? ? ? ? ? ? 2.033 ? disulf3 disulf ? ? A CYS 278 SG ? ? ? 1_555 A CYS 353 SG ? ? A CYS 291 A CYS 366 1_555 ? ? ? ? ? ? ? 2.047 ? disulf4 disulf ? ? A CYS 296 SG ? ? ? 1_555 A CYS 349 SG ? ? A CYS 309 A CYS 362 1_555 ? ? ? ? ? ? ? 2.046 ? disulf5 disulf ? ? A CYS 300 SG ? ? ? 1_555 A CYS 347 SG ? ? A CYS 313 A CYS 360 1_555 ? ? ? ? ? ? ? 2.051 ? disulf6 disulf ? ? A CYS 309 SG ? ? ? 1_555 A CYS 331 SG ? ? A CYS 322 A CYS 344 1_555 ? ? ? ? ? ? ? 2.036 ? disulf7 disulf ? ? A CYS 311 SG ? ? ? 1_555 A CYS 323 SG ? ? A CYS 324 A CYS 336 1_555 ? ? ? ? ? ? ? 2.045 ? disulf8 disulf ? ? B CYS 3 SG ? ? ? 1_555 B CYS 18 SG ? ? D CYS 3 D CYS 18 1_555 ? ? ? ? ? ? ? 2.056 ? disulf9 disulf ? ? B CYS 10 SG ? ? ? 1_555 B CYS 23 SG ? ? D CYS 10 D CYS 23 1_555 ? ? ? ? ? ? ? 2.048 ? disulf10 disulf ? ? B CYS 17 SG ? ? ? 1_555 B CYS 33 SG ? ? D CYS 17 D CYS 33 1_555 ? ? ? ? ? ? ? 2.050 ? covale1 covale ? ? A ASN 381 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 394 A NAG 502 1_555 ? ? ? ? ? ? ? 1.439 ? covale2 covale ? ? A ASN 354 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 367 A NAG 501 1_555 ? ? ? ? ? ? ? 1.450 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 PRO 273 A . ? PRO 286 A PRO 274 A ? PRO 287 A 1 3.48 2 ILE 367 A . ? ILE 380 A PRO 368 A ? PRO 381 A 1 -2.02 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 7 ? B ? 4 ? C ? 2 ? D ? 5 ? E ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? parallel A 3 4 ? parallel A 4 5 ? anti-parallel A 5 6 ? anti-parallel A 6 7 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? parallel B 3 4 ? anti-parallel C 1 2 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel D 4 5 ? anti-parallel E 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 HIS A 61 ? ALA A 69 ? HIS A 74 ALA A 82 A 2 ASN A 402 ? LYS A 410 ? ASN A 415 LYS A 423 A 3 PHE A 257 ? ILE A 269 ? PHE A 270 ILE A 282 A 4 ILE A 391 ? PHE A 398 ? ILE A 404 PHE A 411 A 5 GLY A 201 ? ASP A 211 ? GLY A 214 ASP A 224 A 6 LEU A 157 ? PHE A 162 ? LEU A 170 PHE A 175 A 7 GLU A 165 ? GLN A 166 ? GLU A 178 GLN A 179 B 1 HIS A 61 ? ALA A 69 ? HIS A 74 ALA A 82 B 2 ASN A 402 ? LYS A 410 ? ASN A 415 LYS A 423 B 3 PHE A 257 ? ILE A 269 ? PHE A 270 ILE A 282 B 4 ASN A 354 ? LYS A 366 ? ASN A 367 LYS A 379 C 1 LEU A 73 ? THR A 74 ? LEU A 86 THR A 87 C 2 ILE A 196 ? THR A 197 ? ILE A 209 THR A 210 D 1 PHE A 172 ? THR A 177 ? PHE A 185 THR A 190 D 2 GLY A 180 ? PHE A 185 ? GLY A 193 PHE A 198 D 3 ALA A 77 ? ASN A 82 ? ALA A 90 ASN A 95 D 4 ILE A 233 ? HIS A 238 ? ILE A 246 HIS A 251 D 5 PHE A 251 ? VAL A 253 ? PHE A 264 VAL A 266 E 1 LEU B 21 ? TRP B 24 ? LEU D 21 TRP D 24 E 2 VAL B 32 ? PRO B 35 ? VAL D 32 PRO D 35 # 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 LYS A 64 ? N LYS A 77 O GLU A 407 ? O GLU A 420 A 2 3 O GLU A 404 ? O GLU A 417 N ARG A 267 ? N ARG A 280 A 3 4 N CYS A 263 ? N CYS A 276 O PHE A 397 ? O PHE A 410 A 4 5 O LEU A 394 ? O LEU A 407 N ILE A 208 ? N ILE A 221 A 5 6 O GLU A 207 ? O GLU A 220 N PHE A 161 ? N PHE A 174 A 6 7 N PHE A 162 ? N PHE A 175 O GLU A 165 ? O GLU A 178 B 1 2 N LYS A 64 ? N LYS A 77 O GLU A 407 ? O GLU A 420 B 2 3 O GLU A 404 ? O GLU A 417 N ARG A 267 ? N ARG A 280 B 3 4 N GLN A 258 ? N GLN A 271 O VAL A 365 ? O VAL A 378 C 1 2 N LEU A 73 ? N LEU A 86 O THR A 197 ? O THR A 210 D 1 2 N LYS A 173 ? N LYS A 186 O THR A 184 ? O THR A 197 D 2 3 O PHE A 185 ? O PHE A 198 N VAL A 78 ? N VAL A 91 D 3 4 N ALA A 77 ? N ALA A 90 O HIS A 238 ? O HIS A 251 D 4 5 N VAL A 235 ? N VAL A 248 O PHE A 251 ? O PHE A 264 E 1 2 N GLU B 22 ? N GLU D 22 O VAL B 34 ? O VAL D 34 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 501' AC2 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 502' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 1 ASN A 354 ? ASN A 367 . ? 1_555 ? 2 AC2 1 ASN A 381 ? ASN A 394 . ? 1_555 ? # _database_PDB_matrix.entry_id 4FZ1 _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 4FZ1 _atom_sites.fract_transf_matrix[1][1] 0.007603 _atom_sites.fract_transf_matrix[1][2] 0.004390 _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] 0.008780 _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] 0.007697 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . SER A 1 28 ? 20.983 -1.874 -26.552 1.00 214.53 ? 41 SER A N 1 ATOM 2 C CA . SER A 1 28 ? 19.598 -2.069 -26.140 1.00 216.52 ? 41 SER A CA 1 ATOM 3 C C . SER A 1 28 ? 19.367 -1.521 -24.736 1.00 219.53 ? 41 SER A C 1 ATOM 4 O O . SER A 1 28 ? 18.774 -2.192 -23.894 1.00 220.74 ? 41 SER A O 1 ATOM 5 C CB . SER A 1 28 ? 19.232 -3.547 -26.203 1.00 216.60 ? 41 SER A CB 1 ATOM 6 N N . LEU A 1 29 ? 19.838 -0.299 -24.498 1.00 219.81 ? 42 LEU A N 1 ATOM 7 C CA . LEU A 1 29 ? 19.771 0.330 -23.178 1.00 217.31 ? 42 LEU A CA 1 ATOM 8 C C . LEU A 1 29 ? 18.348 0.390 -22.624 1.00 215.29 ? 42 LEU A C 1 ATOM 9 O O . LEU A 1 29 ? 18.043 -0.231 -21.605 1.00 212.26 ? 42 LEU A O 1 ATOM 10 C CB . LEU A 1 29 ? 20.392 1.726 -23.219 1.00 214.17 ? 42 LEU A CB 1 ATOM 11 N N . LYS A 1 30 ? 17.487 1.150 -23.295 1.00 217.94 ? 43 LYS A N 1 ATOM 12 C CA . LYS A 1 30 ? 16.080 1.252 -22.913 1.00 223.28 ? 43 LYS A CA 1 ATOM 13 C C . LYS A 1 30 ? 15.374 -0.100 -23.006 1.00 228.74 ? 43 LYS A C 1 ATOM 14 O O . LYS A 1 30 ? 14.435 -0.374 -22.254 1.00 230.63 ? 43 LYS A O 1 ATOM 15 C CB . LYS A 1 30 ? 15.367 2.282 -23.782 1.00 220.89 ? 43 LYS A CB 1 ATOM 16 N N . ARG A 1 31 ? 15.822 -0.937 -23.939 1.00 229.57 ? 44 ARG A N 1 ATOM 17 C CA . ARG A 1 31 ? 15.275 -2.282 -24.089 1.00 228.56 ? 44 ARG A CA 1 ATOM 18 C C . ARG A 1 31 ? 15.603 -3.118 -22.855 1.00 228.51 ? 44 ARG A C 1 ATOM 19 O O . ARG A 1 31 ? 14.789 -3.927 -22.403 1.00 227.37 ? 44 ARG A O 1 ATOM 20 C CB . ARG A 1 31 ? 15.822 -2.940 -25.347 1.00 225.35 ? 44 ARG A CB 1 ATOM 21 N N . VAL A 1 32 ? 16.801 -2.902 -22.316 1.00 228.00 ? 45 VAL A N 1 ATOM 22 C CA . VAL A 1 32 ? 17.253 -3.562 -21.095 1.00 228.53 ? 45 VAL A CA 1 ATOM 23 C C . VAL A 1 32 ? 16.480 -3.069 -19.871 1.00 230.87 ? 45 VAL A C 1 ATOM 24 O O . VAL A 1 32 ? 15.983 -3.867 -19.078 1.00 230.79 ? 45 VAL A O 1 ATOM 25 C CB . VAL A 1 32 ? 18.769 -3.350 -20.870 1.00 225.18 ? 45 VAL A CB 1 ATOM 26 C CG1 . VAL A 1 32 ? 19.139 -3.618 -19.423 1.00 226.09 ? 45 VAL A CG1 1 ATOM 27 C CG2 . VAL A 1 32 ? 19.580 -4.232 -21.811 1.00 221.67 ? 45 VAL A CG2 1 ATOM 28 N N . VAL A 1 33 ? 16.383 -1.751 -19.721 1.00 232.70 ? 46 VAL A N 1 ATOM 29 C CA . VAL A 1 33 ? 15.606 -1.155 -18.637 1.00 234.28 ? 46 VAL A CA 1 ATOM 30 C C . VAL A 1 33 ? 14.180 -1.712 -18.607 1.00 234.05 ? 46 VAL A C 1 ATOM 31 O O . VAL A 1 33 ? 13.667 -2.060 -17.545 1.00 234.69 ? 46 VAL A O 1 ATOM 32 C CB . VAL A 1 33 ? 15.571 0.391 -18.742 1.00 204.64 ? 46 VAL A CB 1 ATOM 33 C CG1 . VAL A 1 33 ? 14.460 0.972 -17.878 1.00 203.35 ? 46 VAL A CG1 1 ATOM 34 C CG2 . VAL A 1 33 ? 16.922 0.982 -18.361 1.00 202.63 ? 46 VAL A CG2 1 ATOM 35 N N . TRP A 1 34 ? 13.553 -1.801 -19.779 1.00 232.26 ? 47 TRP A N 1 ATOM 36 C CA . TRP A 1 34 ? 12.189 -2.315 -19.896 1.00 229.51 ? 47 TRP A CA 1 ATOM 37 C C . TRP A 1 34 ? 12.035 -3.660 -19.196 1.00 226.68 ? 47 TRP A C 1 ATOM 38 O O . TRP A 1 34 ? 11.034 -3.908 -18.521 1.00 225.06 ? 47 TRP A O 1 ATOM 39 C CB . TRP A 1 34 ? 11.782 -2.426 -21.360 1.00 227.83 ? 47 TRP A CB 1 ATOM 40 N N . ALA A 1 35 ? 13.015 -4.537 -19.394 1.00 226.26 ? 48 ALA A N 1 ATOM 41 C CA . ALA A 1 35 ? 13.065 -5.821 -18.695 1.00 227.20 ? 48 ALA A CA 1 ATOM 42 C C . ALA A 1 35 ? 13.716 -5.728 -17.309 1.00 224.05 ? 48 ALA A C 1 ATOM 43 O O . ALA A 1 35 ? 13.516 -6.604 -16.465 1.00 222.39 ? 48 ALA A O 1 ATOM 44 C CB . ALA A 1 35 ? 13.778 -6.867 -19.550 1.00 227.09 ? 48 ALA A CB 1 ATOM 45 N N . LEU A 1 36 ? 14.520 -4.687 -17.097 1.00 220.88 ? 49 LEU A N 1 ATOM 46 C CA . LEU A 1 36 ? 15.156 -4.448 -15.805 1.00 218.33 ? 49 LEU A CA 1 ATOM 47 C C . LEU A 1 36 ? 14.112 -4.262 -14.704 1.00 221.30 ? 49 LEU A C 1 ATOM 48 O O . LEU A 1 36 ? 13.992 -5.091 -13.801 1.00 224.74 ? 49 LEU A O 1 ATOM 49 C CB . LEU A 1 36 ? 16.085 -3.245 -15.880 1.00 211.71 ? 49 LEU A CB 1 ATOM 50 N N . CYS A 1 37 ? 13.356 -3.171 -14.787 1.00 217.36 ? 50 CYS A N 1 ATOM 51 C CA . CYS A 1 37 ? 12.307 -2.881 -13.810 1.00 215.02 ? 50 CYS A CA 1 ATOM 52 C C . CYS A 1 37 ? 11.120 -3.857 -13.907 1.00 215.13 ? 50 CYS A C 1 ATOM 53 O O . CYS A 1 37 ? 10.387 -4.045 -12.939 1.00 215.54 ? 50 CYS A O 1 ATOM 54 C CB . CYS A 1 37 ? 11.839 -1.437 -13.949 1.00 212.39 ? 50 CYS A CB 1 ATOM 55 N N . PHE A 1 38 ? 10.930 -4.469 -15.076 1.00 213.78 ? 51 PHE A N 1 ATOM 56 C CA . PHE A 1 38 ? 9.862 -5.457 -15.247 1.00 211.69 ? 51 PHE A CA 1 ATOM 57 C C . PHE A 1 38 ? 10.166 -6.708 -14.438 1.00 213.97 ? 51 PHE A C 1 ATOM 58 O O . PHE A 1 38 ? 9.274 -7.280 -13.806 1.00 216.15 ? 51 PHE A O 1 ATOM 59 C CB . PHE A 1 38 ? 9.651 -5.807 -16.709 1.00 207.73 ? 51 PHE A CB 1 ATOM 60 N N . MET A 1 39 ? 11.431 -7.124 -14.470 1.00 213.55 ? 52 MET A N 1 ATOM 61 C CA . MET A 1 39 ? 11.905 -8.251 -13.673 1.00 215.07 ? 52 MET A CA 1 ATOM 62 C C . MET A 1 39 ? 12.188 -7.823 -12.233 1.00 214.49 ? 52 MET A C 1 ATOM 63 O O . MET A 1 39 ? 12.359 -8.663 -11.348 1.00 215.54 ? 52 MET A O 1 ATOM 64 C CB . MET A 1 39 ? 13.147 -8.876 -14.301 1.00 213.61 ? 52 MET A CB 1 ATOM 65 N N . GLY A 1 40 ? 12.248 -6.511 -12.011 1.00 209.48 ? 53 GLY A N 1 ATOM 66 C CA . GLY A 1 40 ? 12.380 -5.962 -10.673 1.00 203.83 ? 53 GLY A CA 1 ATOM 67 C C . GLY A 1 40 ? 11.054 -6.002 -9.931 1.00 198.49 ? 53 GLY A C 1 ATOM 68 O O . GLY A 1 40 ? 11.001 -6.334 -8.748 1.00 196.34 ? 53 GLY A O 1 ATOM 69 N N . SER A 1 41 ? 9.980 -5.661 -10.640 1.00 194.00 ? 54 SER A N 1 ATOM 70 C CA . SER A 1 41 ? 8.623 -5.707 -10.096 1.00 188.31 ? 54 SER A CA 1 ATOM 71 C C . SER A 1 41 ? 8.347 -7.030 -9.387 1.00 185.61 ? 54 SER A C 1 ATOM 72 O O . SER A 1 41 ? 8.066 -7.053 -8.189 1.00 181.65 ? 54 SER A O 1 ATOM 73 C CB . SER A 1 41 ? 7.598 -5.465 -11.199 1.00 184.33 ? 54 SER A CB 1 ATOM 74 N N . LEU A 1 42 ? 8.414 -8.123 -10.144 1.00 187.41 ? 55 LEU A N 1 ATOM 75 C CA . LEU A 1 42 ? 8.192 -9.465 -9.608 1.00 187.13 ? 55 LEU A CA 1 ATOM 76 C C . LEU A 1 42 ? 9.234 -9.862 -8.558 1.00 186.26 ? 55 LEU A C 1 ATOM 77 O O . LEU A 1 42 ? 9.015 -10.779 -7.770 1.00 183.86 ? 55 LEU A O 1 ATOM 78 C CB . LEU A 1 42 ? 8.149 -10.495 -10.739 1.00 183.69 ? 55 LEU A CB 1 ATOM 79 N N . ALA A 1 43 ? 10.379 -9.191 -8.564 1.00 185.58 ? 56 ALA A N 1 ATOM 80 C CA . ALA A 1 43 ? 11.360 -9.388 -7.504 1.00 184.70 ? 56 ALA A CA 1 ATOM 81 C C . ALA A 1 43 ? 10.762 -9.029 -6.143 1.00 184.50 ? 56 ALA A C 1 ATOM 82 O O . ALA A 1 43 ? 10.492 -9.903 -5.318 1.00 180.70 ? 56 ALA A O 1 ATOM 83 C CB . ALA A 1 43 ? 12.603 -8.565 -7.775 1.00 182.98 ? 56 ALA A CB 1 ATOM 84 N N . LEU A 1 44 ? 10.536 -7.734 -5.933 1.00 188.38 ? 57 LEU A N 1 ATOM 85 C CA . LEU A 1 44 ? 9.958 -7.233 -4.689 1.00 191.66 ? 57 LEU A CA 1 ATOM 86 C C . LEU A 1 44 ? 8.606 -7.887 -4.404 1.00 188.92 ? 57 LEU A C 1 ATOM 87 O O . LEU A 1 44 ? 8.349 -8.322 -3.286 1.00 190.18 ? 57 LEU A O 1 ATOM 88 C CB . LEU A 1 44 ? 9.793 -5.704 -4.727 1.00 195.20 ? 57 LEU A CB 1 ATOM 89 C CG . LEU A 1 44 ? 10.846 -4.807 -5.392 1.00 194.37 ? 57 LEU A CG 1 ATOM 90 C CD1 . LEU A 1 44 ? 10.407 -3.334 -5.357 1.00 189.90 ? 57 LEU A CD1 1 ATOM 91 C CD2 . LEU A 1 44 ? 12.220 -4.983 -4.758 1.00 193.10 ? 57 LEU A CD2 1 ATOM 92 N N . LEU A 1 45 ? 7.755 -7.956 -5.424 1.00 184.92 ? 58 LEU A N 1 ATOM 93 C CA . LEU A 1 45 ? 6.396 -8.477 -5.282 1.00 184.34 ? 58 LEU A CA 1 ATOM 94 C C . LEU A 1 45 ? 6.376 -9.781 -4.502 1.00 192.67 ? 58 LEU A C 1 ATOM 95 O O . LEU A 1 45 ? 5.755 -9.874 -3.445 1.00 193.61 ? 58 LEU A O 1 ATOM 96 C CB . LEU A 1 45 ? 5.757 -8.670 -6.641 1.00 180.69 ? 58 LEU A CB 1 ATOM 97 N N . ALA A 1 46 ? 7.037 -10.796 -5.046 1.00 199.86 ? 59 ALA A N 1 ATOM 98 C CA . ALA A 1 46 ? 7.196 -12.066 -4.349 1.00 204.62 ? 59 ALA A CA 1 ATOM 99 C C . ALA A 1 46 ? 8.057 -11.909 -3.100 1.00 205.42 ? 59 ALA A C 1 ATOM 100 O O . ALA A 1 46 ? 7.823 -12.582 -2.098 1.00 207.78 ? 59 ALA A O 1 ATOM 101 C CB . ALA A 1 46 ? 7.796 -13.112 -5.271 1.00 205.85 ? 59 ALA A CB 1 ATOM 102 N N . LEU A 1 47 ? 9.056 -11.031 -3.162 1.00 204.15 ? 60 LEU A N 1 ATOM 103 C CA . LEU A 1 47 ? 9.933 -10.807 -2.014 1.00 205.44 ? 60 LEU A CA 1 ATOM 104 C C . LEU A 1 47 ? 9.117 -10.401 -0.791 1.00 209.42 ? 60 LEU A C 1 ATOM 105 O O . LEU A 1 47 ? 8.961 -11.182 0.149 1.00 215.79 ? 60 LEU A O 1 ATOM 106 C CB . LEU A 1 47 ? 10.982 -9.748 -2.329 1.00 199.42 ? 60 LEU A CB 1 ATOM 107 N N . VAL A 1 48 ? 8.579 -9.184 -0.824 1.00 202.48 ? 61 VAL A N 1 ATOM 108 C CA . VAL A 1 48 ? 7.706 -8.692 0.236 1.00 194.54 ? 61 VAL A CA 1 ATOM 109 C C . VAL A 1 48 ? 6.569 -9.668 0.521 1.00 187.84 ? 61 VAL A C 1 ATOM 110 O O . VAL A 1 48 ? 6.320 -10.016 1.671 1.00 186.16 ? 61 VAL A O 1 ATOM 111 C CB . VAL A 1 48 ? 7.150 -7.326 -0.123 1.00 189.22 ? 61 VAL A CB 1 ATOM 112 N N . CYS A 1 49 ? 5.889 -10.111 -0.530 1.00 182.85 ? 62 CYS A N 1 ATOM 113 C CA . CYS A 1 49 ? 4.746 -10.999 -0.372 1.00 184.29 ? 62 CYS A CA 1 ATOM 114 C C . CYS A 1 49 ? 5.071 -12.164 0.562 1.00 194.44 ? 62 CYS A C 1 ATOM 115 O O . CYS A 1 49 ? 4.328 -12.433 1.503 1.00 197.05 ? 62 CYS A O 1 ATOM 116 C CB . CYS A 1 49 ? 4.275 -11.520 -1.731 1.00 179.52 ? 62 CYS A CB 1 ATOM 117 S SG . CYS A 1 49 ? 2.845 -12.621 -1.658 1.00 246.89 ? 62 CYS A SG 1 ATOM 118 N N . THR A 1 50 ? 6.185 -12.845 0.315 1.00 200.73 ? 63 THR A N 1 ATOM 119 C CA . THR A 1 50 ? 6.578 -13.973 1.157 1.00 205.76 ? 63 THR A CA 1 ATOM 120 C C . THR A 1 50 ? 7.039 -13.507 2.535 1.00 208.74 ? 63 THR A C 1 ATOM 121 O O . THR A 1 50 ? 6.892 -14.227 3.520 1.00 213.30 ? 63 THR A O 1 ATOM 122 C CB . THR A 1 50 ? 7.683 -14.830 0.510 1.00 204.62 ? 63 THR A CB 1 ATOM 123 O OG1 . THR A 1 50 ? 8.798 -13.996 0.167 1.00 204.69 ? 63 THR A OG1 1 ATOM 124 C CG2 . THR A 1 50 ? 7.156 -15.544 -0.733 1.00 199.30 ? 63 THR A CG2 1 ATOM 125 N N . ASN A 1 51 ? 7.608 -12.308 2.599 1.00 204.04 ? 64 ASN A N 1 ATOM 126 C CA . ASN A 1 51 ? 7.940 -11.698 3.883 1.00 203.37 ? 64 ASN A CA 1 ATOM 127 C C . ASN A 1 51 ? 6.709 -11.564 4.782 1.00 197.38 ? 64 ASN A C 1 ATOM 128 O O . ASN A 1 51 ? 6.638 -12.169 5.850 1.00 194.84 ? 64 ASN A O 1 ATOM 129 C CB . ASN A 1 51 ? 8.620 -10.347 3.675 1.00 207.50 ? 64 ASN A CB 1 ATOM 130 C CG . ASN A 1 51 ? 9.838 -10.452 2.782 1.00 212.94 ? 64 ASN A CG 1 ATOM 131 O OD1 . ASN A 1 51 ? 10.410 -11.536 2.626 1.00 213.94 ? 64 ASN A OD1 1 ATOM 132 N ND2 . ASN A 1 51 ? 10.238 -9.331 2.182 1.00 213.85 ? 64 ASN A ND2 1 ATOM 133 N N . ARG A 1 52 ? 5.744 -10.761 4.345 1.00 192.43 ? 65 ARG A N 1 ATOM 134 C CA . ARG A 1 52 ? 4.470 -10.638 5.047 1.00 186.29 ? 65 ARG A CA 1 ATOM 135 C C . ARG A 1 52 ? 3.798 -11.997 5.265 1.00 184.64 ? 65 ARG A C 1 ATOM 136 O O . ARG A 1 52 ? 3.053 -12.174 6.227 1.00 187.99 ? 65 ARG A O 1 ATOM 137 C CB . ARG A 1 52 ? 3.533 -9.680 4.313 1.00 179.34 ? 65 ARG A CB 1 ATOM 138 N N . ILE A 1 53 ? 4.044 -12.953 4.373 1.00 181.78 ? 66 ILE A N 1 ATOM 139 C CA . ILE A 1 53 ? 3.526 -14.303 4.584 1.00 185.51 ? 66 ILE A CA 1 ATOM 140 C C . ILE A 1 53 ? 4.279 -14.975 5.724 1.00 191.47 ? 66 ILE A C 1 ATOM 141 O O . ILE A 1 53 ? 3.702 -15.740 6.495 1.00 189.55 ? 66 ILE A O 1 ATOM 142 C CB . ILE A 1 53 ? 3.633 -15.189 3.327 1.00 182.01 ? 66 ILE A CB 1 ATOM 143 C CG1 . ILE A 1 53 ? 2.685 -14.700 2.234 1.00 179.20 ? 66 ILE A CG1 1 ATOM 144 C CG2 . ILE A 1 53 ? 3.293 -16.626 3.676 1.00 180.16 ? 66 ILE A CG2 1 ATOM 145 C CD1 . ILE A 1 53 ? 3.003 -15.248 0.861 1.00 174.66 ? 66 ILE A CD1 1 ATOM 146 N N . GLN A 1 54 ? 5.575 -14.685 5.823 1.00 196.94 ? 67 GLN A N 1 ATOM 147 C CA . GLN A 1 54 ? 6.410 -15.245 6.881 1.00 201.58 ? 67 GLN A CA 1 ATOM 148 C C . GLN A 1 54 ? 6.031 -14.650 8.230 1.00 206.46 ? 67 GLN A C 1 ATOM 149 O O . GLN A 1 54 ? 5.989 -15.353 9.241 1.00 208.75 ? 67 GLN A O 1 ATOM 150 C CB . GLN A 1 54 ? 7.890 -15.005 6.584 1.00 197.64 ? 67 GLN A CB 1 ATOM 151 N N . TYR A 1 55 ? 5.753 -13.349 8.238 1.00 205.37 ? 68 TYR A N 1 ATOM 152 C CA . TYR A 1 55 ? 5.377 -12.650 9.462 1.00 202.54 ? 68 TYR A CA 1 ATOM 153 C C . TYR A 1 55 ? 4.110 -13.238 10.089 1.00 203.71 ? 68 TYR A C 1 ATOM 154 O O . TYR A 1 55 ? 3.966 -13.244 11.306 1.00 210.76 ? 68 TYR A O 1 ATOM 155 C CB . TYR A 1 55 ? 5.220 -11.153 9.206 1.00 196.24 ? 68 TYR A CB 1 ATOM 156 N N . TYR A 1 56 ? 3.198 -13.738 9.263 1.00 197.61 ? 69 TYR A N 1 ATOM 157 C CA . TYR A 1 56 ? 2.007 -14.405 9.779 1.00 200.52 ? 69 TYR A CA 1 ATOM 158 C C . TYR A 1 56 ? 2.329 -15.794 10.338 1.00 208.55 ? 69 TYR A C 1 ATOM 159 O O . TYR A 1 56 ? 1.553 -16.357 11.109 1.00 212.73 ? 69 TYR A O 1 ATOM 160 C CB . TYR A 1 56 ? 0.923 -14.507 8.695 1.00 198.67 ? 69 TYR A CB 1 ATOM 161 C CG . TYR A 1 56 ? -0.288 -15.330 9.103 1.00 199.99 ? 69 TYR A CG 1 ATOM 162 C CD1 . TYR A 1 56 ? -0.977 -15.054 10.274 1.00 205.96 ? 69 TYR A CD1 1 ATOM 163 C CD2 . TYR A 1 56 ? -0.739 -16.383 8.318 1.00 167.38 ? 69 TYR A CD2 1 ATOM 164 C CE1 . TYR A 1 56 ? -2.083 -15.807 10.653 1.00 209.64 ? 69 TYR A CE1 1 ATOM 165 C CE2 . TYR A 1 56 ? -1.843 -17.138 8.686 1.00 198.58 ? 69 TYR A CE2 1 ATOM 166 C CZ . TYR A 1 56 ? -2.513 -16.847 9.854 1.00 203.66 ? 69 TYR A CZ 1 ATOM 167 O OH . TYR A 1 56 ? -3.613 -17.595 10.232 1.00 200.40 ? 69 TYR A OH 1 ATOM 168 N N . PHE A 1 57 ? 3.470 -16.347 9.943 1.00 210.04 ? 70 PHE A N 1 ATOM 169 C CA . PHE A 1 57 ? 3.851 -17.686 10.382 1.00 213.73 ? 70 PHE A CA 1 ATOM 170 C C . PHE A 1 57 ? 4.436 -17.643 11.785 1.00 215.27 ? 70 PHE A C 1 ATOM 171 O O . PHE A 1 57 ? 4.402 -18.628 12.519 1.00 216.47 ? 70 PHE A O 1 ATOM 172 C CB . PHE A 1 57 ? 4.828 -18.308 9.410 1.00 215.88 ? 70 PHE A CB 1 ATOM 173 N N . LEU A 1 58 ? 4.976 -16.487 12.149 1.00 153.75 ? 71 LEU A N 1 ATOM 174 C CA . LEU A 1 58 ? 5.451 -16.259 13.506 1.00 161.24 ? 71 LEU A CA 1 ATOM 175 C C . LEU A 1 58 ? 4.274 -16.130 14.482 1.00 175.25 ? 71 LEU A C 1 ATOM 176 O O . LEU A 1 58 ? 4.481 -15.969 15.686 1.00 177.21 ? 71 LEU A O 1 ATOM 177 C CB . LEU A 1 58 ? 6.346 -15.021 13.563 1.00 153.77 ? 71 LEU A CB 1 ATOM 178 N N . TYR A 1 59 ? 3.050 -16.175 13.952 1.00 184.07 ? 72 TYR A N 1 ATOM 179 C CA . TYR A 1 59 ? 1.836 -15.981 14.747 1.00 187.26 ? 72 TYR A CA 1 ATOM 180 C C . TYR A 1 59 ? 2.031 -14.862 15.754 1.00 192.29 ? 72 TYR A C 1 ATOM 181 O O . TYR A 1 59 ? 2.059 -15.091 16.961 1.00 198.58 ? 72 TYR A O 1 ATOM 182 C CB . TYR A 1 59 ? 1.428 -17.267 15.460 1.00 187.63 ? 72 TYR A CB 1 ATOM 183 C CG . TYR A 1 59 ? 0.589 -18.193 14.615 1.00 198.70 ? 72 TYR A CG 1 ATOM 184 C CD1 . TYR A 1 59 ? -0.794 -18.189 14.717 1.00 204.69 ? 72 TYR A CD1 1 ATOM 185 C CD2 . TYR A 1 59 ? 1.176 -19.075 13.711 1.00 201.10 ? 72 TYR A CD2 1 ATOM 186 C CE1 . TYR A 1 59 ? -1.576 -19.042 13.945 1.00 208.61 ? 72 TYR A CE1 1 ATOM 187 C CE2 . TYR A 1 59 ? 0.405 -19.933 12.935 1.00 202.72 ? 72 TYR A CE2 1 ATOM 188 C CZ . TYR A 1 59 ? -0.971 -19.911 13.057 1.00 205.85 ? 72 TYR A CZ 1 ATOM 189 O OH . TYR A 1 59 ? -1.746 -20.758 12.296 1.00 206.61 ? 72 TYR A OH 1 ATOM 190 N N . PRO A 1 60 ? 2.171 -13.637 15.250 1.00 189.89 ? 73 PRO A N 1 ATOM 191 C CA . PRO A 1 60 ? 2.477 -12.442 16.033 1.00 182.96 ? 73 PRO A CA 1 ATOM 192 C C . PRO A 1 60 ? 1.242 -11.904 16.734 1.00 181.46 ? 73 PRO A C 1 ATOM 193 O O . PRO A 1 60 ? 0.125 -12.084 16.235 1.00 184.42 ? 73 PRO A O 1 ATOM 194 C CB . PRO A 1 60 ? 2.908 -11.458 14.958 1.00 186.85 ? 73 PRO A CB 1 ATOM 195 C CG . PRO A 1 60 ? 2.035 -11.813 13.798 1.00 194.12 ? 73 PRO A CG 1 ATOM 196 C CD . PRO A 1 60 ? 1.838 -13.307 13.855 1.00 195.48 ? 73 PRO A CD 1 ATOM 197 N N . HIS A 1 61 ? 1.443 -11.234 17.864 1.00 178.81 ? 74 HIS A N 1 ATOM 198 C CA . HIS A 1 61 ? 0.331 -10.621 18.584 1.00 180.91 ? 74 HIS A CA 1 ATOM 199 C C . HIS A 1 61 ? 0.642 -9.201 19.064 1.00 176.05 ? 74 HIS A C 1 ATOM 200 O O . HIS A 1 61 ? 1.760 -8.706 18.917 1.00 171.05 ? 74 HIS A O 1 ATOM 201 C CB . HIS A 1 61 ? -0.067 -11.491 19.778 1.00 182.32 ? 74 HIS A CB 1 ATOM 202 C CG . HIS A 1 61 ? 1.036 -11.688 20.775 1.00 179.13 ? 74 HIS A CG 1 ATOM 203 N ND1 . HIS A 1 61 ? 1.806 -10.797 21.445 1.00 179.39 ? 74 HIS A ND1 1 ATOM 204 C CD2 . HIS A 1 61 ? 1.461 -12.938 21.179 1.00 168.80 ? 74 HIS A CD2 1 ATOM 205 C CE1 . HIS A 1 61 ? 2.669 -11.518 22.235 1.00 169.26 ? 74 HIS A CE1 1 ATOM 206 N NE2 . HIS A 1 61 ? 2.440 -12.807 22.057 1.00 164.98 ? 74 HIS A NE2 1 ATOM 207 N N . VAL A 1 62 ? -0.357 -8.562 19.661 1.00 177.71 ? 75 VAL A N 1 ATOM 208 C CA . VAL A 1 62 ? -0.198 -7.221 20.209 1.00 178.68 ? 75 VAL A CA 1 ATOM 209 C C . VAL A 1 62 ? -1.026 -7.107 21.494 1.00 177.72 ? 75 VAL A C 1 ATOM 210 O O . VAL A 1 62 ? -2.139 -7.629 21.562 1.00 187.16 ? 75 VAL A O 1 ATOM 211 C CB . VAL A 1 62 ? -0.617 -6.141 19.175 1.00 196.46 ? 75 VAL A CB 1 ATOM 212 C CG1 . VAL A 1 62 ? -2.100 -5.796 19.310 1.00 196.28 ? 75 VAL A CG1 1 ATOM 213 C CG2 . VAL A 1 62 ? 0.238 -4.895 19.323 1.00 195.30 ? 75 VAL A CG2 1 ATOM 214 N N . THR A 1 63 ? -0.485 -6.444 22.514 1.00 163.71 ? 76 THR A N 1 ATOM 215 C CA . THR A 1 63 ? -1.191 -6.297 23.786 1.00 155.37 ? 76 THR A CA 1 ATOM 216 C C . THR A 1 63 ? -1.980 -5.002 23.820 1.00 143.36 ? 76 THR A C 1 ATOM 217 O O . THR A 1 63 ? -1.398 -3.928 23.925 1.00 138.02 ? 76 THR A O 1 ATOM 218 C CB . THR A 1 63 ? -0.200 -6.218 24.946 1.00 163.10 ? 76 THR A CB 1 ATOM 219 O OG1 . THR A 1 63 ? 0.886 -5.376 24.552 1.00 171.18 ? 76 THR A OG1 1 ATOM 220 C CG2 . THR A 1 63 ? 0.343 -7.590 25.302 1.00 164.69 ? 76 THR A CG2 1 ATOM 221 N N . LYS A 1 64 ? -3.303 -5.102 23.781 1.00 146.79 ? 77 LYS A N 1 ATOM 222 C CA . LYS A 1 64 ? -4.154 -3.917 23.704 1.00 149.69 ? 77 LYS A CA 1 ATOM 223 C C . LYS A 1 64 ? -4.596 -3.481 25.089 1.00 154.77 ? 77 LYS A C 1 ATOM 224 O O . LYS A 1 64 ? -5.411 -4.144 25.732 1.00 165.85 ? 77 LYS A O 1 ATOM 225 C CB . LYS A 1 64 ? -5.373 -4.184 22.820 1.00 146.65 ? 77 LYS A CB 1 ATOM 226 N N . LEU A 1 65 ? -4.067 -2.349 25.533 1.00 144.23 ? 78 LEU A N 1 ATOM 227 C CA . LEU A 1 65 ? -4.375 -1.826 26.853 1.00 140.44 ? 78 LEU A CA 1 ATOM 228 C C . LEU A 1 65 ? -5.544 -0.851 26.787 1.00 147.38 ? 78 LEU A C 1 ATOM 229 O O . LEU A 1 65 ? -5.555 0.058 25.975 1.00 150.63 ? 78 LEU A O 1 ATOM 230 C CB . LEU A 1 65 ? -3.132 -1.166 27.456 1.00 132.42 ? 78 LEU A CB 1 ATOM 231 C CG . LEU A 1 65 ? -3.320 -0.036 28.466 1.00 129.59 ? 78 LEU A CG 1 ATOM 232 C CD1 . LEU A 1 65 ? -2.183 -0.012 29.455 1.00 123.59 ? 78 LEU A CD1 1 ATOM 233 C CD2 . LEU A 1 65 ? -3.416 1.286 27.742 1.00 134.60 ? 78 LEU A CD2 1 ATOM 234 N N . ASP A 1 66 ? -6.536 -1.044 27.641 1.00 153.88 ? 79 ASP A N 1 ATOM 235 C CA . ASP A 1 66 ? -7.692 -0.170 27.626 1.00 161.65 ? 79 ASP A CA 1 ATOM 236 C C . ASP A 1 66 ? -8.167 0.180 29.030 1.00 169.43 ? 79 ASP A C 1 ATOM 237 O O . ASP A 1 66 ? -8.244 -0.683 29.903 1.00 175.96 ? 79 ASP A O 1 ATOM 238 C CB . ASP A 1 66 ? -8.820 -0.819 26.830 1.00 168.64 ? 79 ASP A CB 1 ATOM 239 C CG . ASP A 1 66 ? -9.425 0.126 25.820 1.00 178.49 ? 79 ASP A CG 1 ATOM 240 O OD1 . ASP A 1 66 ? -8.758 1.134 25.497 1.00 178.55 ? 79 ASP A OD1 1 ATOM 241 O OD2 . ASP A 1 66 ? -10.554 -0.137 25.347 1.00 183.74 ? 79 ASP A OD2 1 ATOM 242 N N . GLU A 1 67 ? -8.473 1.457 29.243 1.00 167.67 ? 80 GLU A N 1 ATOM 243 C CA . GLU A 1 67 ? -9.060 1.918 30.499 1.00 161.21 ? 80 GLU A CA 1 ATOM 244 C C . GLU A 1 67 ? -10.519 2.247 30.228 1.00 156.17 ? 80 GLU A C 1 ATOM 245 O O . GLU A 1 67 ? -10.809 3.195 29.504 1.00 158.77 ? 80 GLU A O 1 ATOM 246 C CB . GLU A 1 67 ? -8.359 3.187 30.995 1.00 155.60 ? 80 GLU A CB 1 ATOM 247 C CG . GLU A 1 67 ? -6.843 3.170 30.911 1.00 150.52 ? 80 GLU A CG 1 ATOM 248 C CD . GLU A 1 67 ? -6.202 2.591 32.147 1.00 152.79 ? 80 GLU A CD 1 ATOM 249 O OE1 . GLU A 1 67 ? -6.946 2.363 33.122 1.00 157.45 ? 80 GLU A OE1 1 ATOM 250 O OE2 . GLU A 1 67 ? -4.965 2.365 32.147 1.00 150.45 ? 80 GLU A OE2 1 ATOM 251 N N . VAL A 1 68 ? -11.444 1.480 30.793 1.00 150.29 ? 81 VAL A N 1 ATOM 252 C CA . VAL A 1 68 ? -12.864 1.775 30.590 1.00 154.54 ? 81 VAL A CA 1 ATOM 253 C C . VAL A 1 68 ? -13.593 2.139 31.872 1.00 168.16 ? 81 VAL A C 1 ATOM 254 O O . VAL A 1 68 ? -13.433 1.469 32.890 1.00 179.04 ? 81 VAL A O 1 ATOM 255 C CB . VAL A 1 68 ? -13.615 0.603 29.948 1.00 145.46 ? 81 VAL A CB 1 ATOM 256 C CG1 . VAL A 1 68 ? -12.925 -0.711 30.262 1.00 140.72 ? 81 VAL A CG1 1 ATOM 257 C CG2 . VAL A 1 68 ? -15.054 0.600 30.433 1.00 142.65 ? 81 VAL A CG2 1 ATOM 258 N N . ALA A 1 69 ? -14.403 3.191 31.828 1.00 169.67 ? 82 ALA A N 1 ATOM 259 C CA . ALA A 1 69 ? -15.154 3.580 33.013 1.00 172.17 ? 82 ALA A CA 1 ATOM 260 C C . ALA A 1 69 ? -16.623 3.235 32.859 1.00 169.25 ? 82 ALA A C 1 ATOM 261 O O . ALA A 1 69 ? -17.352 3.896 32.125 1.00 171.06 ? 82 ALA A O 1 ATOM 262 C CB . ALA A 1 69 ? -14.976 5.067 33.302 1.00 174.29 ? 82 ALA A CB 1 ATOM 263 N N . ALA A 1 70 ? -17.056 2.212 33.581 1.00 165.71 ? 83 ALA A N 1 ATOM 264 C CA . ALA A 1 70 ? -18.448 1.813 33.534 1.00 173.50 ? 83 ALA A CA 1 ATOM 265 C C . ALA A 1 70 ? -19.217 2.517 34.640 1.00 169.96 ? 83 ALA A C 1 ATOM 266 O O . ALA A 1 70 ? -18.646 3.294 35.411 1.00 162.94 ? 83 ALA A O 1 ATOM 267 C CB . ALA A 1 70 ? -18.578 0.301 33.662 1.00 178.28 ? 83 ALA A CB 1 ATOM 268 N N . THR A 1 71 ? -20.522 2.271 34.676 1.00 170.07 ? 84 THR A N 1 ATOM 269 C CA . THR A 1 71 ? -21.362 2.704 35.780 1.00 171.41 ? 84 THR A CA 1 ATOM 270 C C . THR A 1 71 ? -21.613 1.556 36.763 1.00 169.70 ? 84 THR A C 1 ATOM 271 O O . THR A 1 71 ? -22.256 1.736 37.799 1.00 171.95 ? 84 THR A O 1 ATOM 272 C CB . THR A 1 71 ? -22.692 3.236 35.248 1.00 179.48 ? 84 THR A CB 1 ATOM 273 O OG1 . THR A 1 71 ? -22.436 4.009 34.068 1.00 175.82 ? 84 THR A OG1 1 ATOM 274 C CG2 . THR A 1 71 ? -23.400 4.097 36.302 1.00 185.38 ? 84 THR A CG2 1 ATOM 275 N N . ARG A 1 72 ? -21.106 0.376 36.423 1.00 164.94 ? 85 ARG A N 1 ATOM 276 C CA . ARG A 1 72 ? -21.328 -0.825 37.221 1.00 161.34 ? 85 ARG A CA 1 ATOM 277 C C . ARG A 1 72 ? -20.047 -1.634 37.338 1.00 162.39 ? 85 ARG A C 1 ATOM 278 O O . ARG A 1 72 ? -19.425 -1.990 36.336 1.00 171.03 ? 85 ARG A O 1 ATOM 279 C CB . ARG A 1 72 ? -22.445 -1.685 36.612 1.00 156.78 ? 85 ARG A CB 1 ATOM 280 N N . LEU A 1 73 ? -19.647 -1.916 38.571 1.00 150.61 ? 86 LEU A N 1 ATOM 281 C CA . LEU A 1 73 ? -18.576 -2.864 38.820 1.00 132.98 ? 86 LEU A CA 1 ATOM 282 C C . LEU A 1 73 ? -19.119 -4.052 39.596 1.00 135.87 ? 86 LEU A C 1 ATOM 283 O O . LEU A 1 73 ? -19.906 -3.889 40.530 1.00 140.99 ? 86 LEU A O 1 ATOM 284 C CB . LEU A 1 73 ? -17.453 -2.195 39.588 1.00 124.07 ? 86 LEU A CB 1 ATOM 285 C CG . LEU A 1 73 ? -16.642 -1.358 38.617 1.00 131.04 ? 86 LEU A CG 1 ATOM 286 C CD1 . LEU A 1 73 ? -15.439 -0.696 39.278 1.00 126.82 ? 86 LEU A CD1 1 ATOM 287 C CD2 . LEU A 1 73 ? -16.217 -2.279 37.489 1.00 139.19 ? 86 LEU A CD2 1 ATOM 288 N N . THR A 1 74 ? -18.727 -5.253 39.190 1.00 130.84 ? 87 THR A N 1 ATOM 289 C CA . THR A 1 74 ? -19.100 -6.450 39.928 1.00 131.73 ? 87 THR A CA 1 ATOM 290 C C . THR A 1 74 ? -18.145 -6.611 41.096 1.00 124.65 ? 87 THR A C 1 ATOM 291 O O . THR A 1 74 ? -16.936 -6.724 40.901 1.00 130.56 ? 87 THR A O 1 ATOM 292 C CB . THR A 1 74 ? -19.022 -7.690 39.035 1.00 144.49 ? 87 THR A CB 1 ATOM 293 O OG1 . THR A 1 74 ? -20.008 -7.594 37.995 1.00 156.29 ? 87 THR A OG1 1 ATOM 294 C CG2 . THR A 1 74 ? -19.258 -8.948 39.850 1.00 145.82 ? 87 THR A CG2 1 ATOM 295 N N . PHE A 1 75 ? -18.677 -6.609 42.311 1.00 116.57 ? 88 PHE A N 1 ATOM 296 C CA . PHE A 1 75 ? -17.832 -6.558 43.502 1.00 110.17 ? 88 PHE A CA 1 ATOM 297 C C . PHE A 1 75 ? -17.097 -7.877 43.814 1.00 111.87 ? 88 PHE A C 1 ATOM 298 O O . PHE A 1 75 ? -17.673 -8.969 43.734 1.00 100.17 ? 88 PHE A O 1 ATOM 299 C CB . PHE A 1 75 ? -18.644 -6.091 44.702 1.00 110.86 ? 88 PHE A CB 1 ATOM 300 C CG . PHE A 1 75 ? -17.813 -5.557 45.812 1.00 113.85 ? 88 PHE A CG 1 ATOM 301 C CD1 . PHE A 1 75 ? -17.295 -4.284 45.753 1.00 118.84 ? 88 PHE A CD1 1 ATOM 302 C CD2 . PHE A 1 75 ? -17.540 -6.330 46.916 1.00 114.21 ? 88 PHE A CD2 1 ATOM 303 C CE1 . PHE A 1 75 ? -16.525 -3.790 46.789 1.00 117.81 ? 88 PHE A CE1 1 ATOM 304 C CE2 . PHE A 1 75 ? -16.768 -5.842 47.947 1.00 110.61 ? 88 PHE A CE2 1 ATOM 305 C CZ . PHE A 1 75 ? -16.266 -4.568 47.882 1.00 112.22 ? 88 PHE A CZ 1 ATOM 306 N N . PRO A 1 76 ? -15.804 -7.776 44.177 1.00 114.43 ? 89 PRO A N 1 ATOM 307 C CA . PRO A 1 76 ? -14.983 -8.989 44.285 1.00 107.18 ? 89 PRO A CA 1 ATOM 308 C C . PRO A 1 76 ? -15.427 -9.847 45.448 1.00 112.90 ? 89 PRO A C 1 ATOM 309 O O . PRO A 1 76 ? -16.052 -9.353 46.373 1.00 117.49 ? 89 PRO A O 1 ATOM 310 C CB . PRO A 1 76 ? -13.589 -8.433 44.555 1.00 94.16 ? 89 PRO A CB 1 ATOM 311 C CG . PRO A 1 76 ? -13.859 -7.159 45.281 1.00 95.38 ? 89 PRO A CG 1 ATOM 312 C CD . PRO A 1 76 ? -15.077 -6.577 44.637 1.00 103.05 ? 89 PRO A CD 1 ATOM 313 N N . ALA A 1 77 ? -15.116 -11.131 45.405 1.00 114.32 ? 90 ALA A N 1 ATOM 314 C CA . ALA A 1 77 ? -15.363 -11.946 46.572 1.00 112.03 ? 90 ALA A CA 1 ATOM 315 C C . ALA A 1 77 ? -14.282 -11.571 47.587 1.00 124.00 ? 90 ALA A C 1 ATOM 316 O O . ALA A 1 77 ? -13.147 -11.246 47.214 1.00 121.98 ? 90 ALA A O 1 ATOM 317 C CB . ALA A 1 77 ? -15.336 -13.414 46.224 1.00 96.30 ? 90 ALA A CB 1 ATOM 318 N N . VAL A 1 78 ? -14.648 -11.569 48.864 1.00 128.37 ? 91 VAL A N 1 ATOM 319 C CA . VAL A 1 78 ? -13.722 -11.192 49.921 1.00 116.36 ? 91 VAL A CA 1 ATOM 320 C C . VAL A 1 78 ? -13.667 -12.279 50.980 1.00 123.88 ? 91 VAL A C 1 ATOM 321 O O . VAL A 1 78 ? -14.632 -12.474 51.697 1.00 136.84 ? 91 VAL A O 1 ATOM 322 C CB . VAL A 1 78 ? -14.217 -9.917 50.612 1.00 100.43 ? 91 VAL A CB 1 ATOM 323 C CG1 . VAL A 1 78 ? -13.364 -9.618 51.789 1.00 95.60 ? 91 VAL A CG1 1 ATOM 324 C CG2 . VAL A 1 78 ? -14.240 -8.753 49.632 1.00 97.97 ? 91 VAL A CG2 1 ATOM 325 N N . THR A 1 79 ? -12.542 -12.976 51.095 1.00 121.64 ? 92 THR A N 1 ATOM 326 C CA . THR A 1 79 ? -12.396 -14.026 52.104 1.00 120.31 ? 92 THR A CA 1 ATOM 327 C C . THR A 1 79 ? -11.517 -13.531 53.220 1.00 117.24 ? 92 THR A C 1 ATOM 328 O O . THR A 1 79 ? -10.528 -12.844 52.982 1.00 118.46 ? 92 THR A O 1 ATOM 329 C CB . THR A 1 79 ? -11.726 -15.300 51.555 1.00 118.44 ? 92 THR A CB 1 ATOM 330 O OG1 . THR A 1 79 ? -12.645 -16.033 50.726 1.00 120.71 ? 92 THR A OG1 1 ATOM 331 C CG2 . THR A 1 79 ? -11.262 -16.174 52.711 1.00 107.27 ? 92 THR A CG2 1 ATOM 332 N N . PHE A 1 80 ? -11.885 -13.860 54.446 1.00 116.49 ? 93 PHE A N 1 ATOM 333 C CA . PHE A 1 80 ? -11.080 -13.454 55.583 1.00 116.17 ? 93 PHE A CA 1 ATOM 334 C C . PHE A 1 80 ? -11.020 -14.556 56.629 1.00 117.29 ? 93 PHE A C 1 ATOM 335 O O . PHE A 1 80 ? -12.045 -15.058 57.059 1.00 123.01 ? 93 PHE A O 1 ATOM 336 C CB . PHE A 1 80 ? -11.655 -12.184 56.186 1.00 116.54 ? 93 PHE A CB 1 ATOM 337 C CG . PHE A 1 80 ? -12.753 -12.427 57.166 1.00 126.80 ? 93 PHE A CG 1 ATOM 338 C CD1 . PHE A 1 80 ? -12.461 -12.755 58.487 1.00 126.33 ? 93 PHE A CD1 1 ATOM 339 C CD2 . PHE A 1 80 ? -14.076 -12.314 56.779 1.00 134.34 ? 93 PHE A CD2 1 ATOM 340 C CE1 . PHE A 1 80 ? -13.467 -12.974 59.392 1.00 130.58 ? 93 PHE A CE1 1 ATOM 341 C CE2 . PHE A 1 80 ? -15.088 -12.532 57.683 1.00 140.11 ? 93 PHE A CE2 1 ATOM 342 C CZ . PHE A 1 80 ? -14.786 -12.861 58.991 1.00 137.03 ? 93 PHE A CZ 1 ATOM 343 N N . CYS A 1 81 ? -9.819 -14.937 57.039 1.00 117.10 ? 94 CYS A N 1 ATOM 344 C CA . CYS A 1 81 ? -9.664 -15.947 58.077 1.00 115.58 ? 94 CYS A CA 1 ATOM 345 C C . CYS A 1 81 ? -9.194 -15.286 59.347 1.00 120.83 ? 94 CYS A C 1 ATOM 346 O O . CYS A 1 81 ? -8.503 -14.278 59.304 1.00 124.19 ? 94 CYS A O 1 ATOM 347 C CB . CYS A 1 81 ? -8.638 -16.998 57.674 1.00 101.88 ? 94 CYS A CB 1 ATOM 348 S SG . CYS A 1 81 ? -9.311 -18.367 56.731 1.00 126.61 ? 94 CYS A SG 1 ATOM 349 N N . ASN A 1 82 ? -9.587 -15.837 60.483 1.00 119.73 ? 95 ASN A N 1 ATOM 350 C CA . ASN A 1 82 ? -8.959 -15.444 61.719 1.00 112.72 ? 95 ASN A CA 1 ATOM 351 C C . ASN A 1 82 ? -7.651 -16.209 61.774 1.00 118.17 ? 95 ASN A C 1 ATOM 352 O O . ASN A 1 82 ? -7.536 -17.257 61.124 1.00 122.50 ? 95 ASN A O 1 ATOM 353 C CB . ASN A 1 82 ? -9.853 -15.769 62.909 1.00 107.89 ? 95 ASN A CB 1 ATOM 354 C CG . ASN A 1 82 ? -9.376 -15.103 64.167 1.00 107.73 ? 95 ASN A CG 1 ATOM 355 O OD1 . ASN A 1 82 ? -8.188 -14.803 64.296 1.00 105.32 ? 95 ASN A OD1 1 ATOM 356 N ND2 . ASN A 1 82 ? -10.290 -14.848 65.100 1.00 109.56 ? 95 ASN A ND2 1 ATOM 357 N N . LEU A 1 83 ? -6.666 -15.680 62.505 1.00 113.76 ? 96 LEU A N 1 ATOM 358 C CA . LEU A 1 83 ? -5.344 -16.319 62.616 1.00 108.38 ? 96 LEU A CA 1 ATOM 359 C C . LEU A 1 83 ? -5.274 -17.479 63.630 1.00 112.33 ? 96 LEU A C 1 ATOM 360 O O . LEU A 1 83 ? -4.497 -18.424 63.477 1.00 110.74 ? 96 LEU A O 1 ATOM 361 C CB . LEU A 1 83 ? -4.287 -15.260 62.906 1.00 95.73 ? 96 LEU A CB 1 ATOM 362 C CG . LEU A 1 83 ? -4.254 -14.236 61.780 1.00 93.46 ? 96 LEU A CG 1 ATOM 363 C CD1 . LEU A 1 83 ? -3.041 -13.335 61.845 1.00 97.02 ? 96 LEU A CD1 1 ATOM 364 C CD2 . LEU A 1 83 ? -4.268 -14.969 60.461 1.00 100.20 ? 96 LEU A CD2 1 ATOM 365 N N . ASN A 1 84 ? -6.087 -17.378 64.671 1.00 113.05 ? 97 ASN A N 1 ATOM 366 C CA . ASN A 1 84 ? -6.287 -18.448 65.628 1.00 116.92 ? 97 ASN A CA 1 ATOM 367 C C . ASN A 1 84 ? -7.178 -19.518 65.005 1.00 123.74 ? 97 ASN A C 1 ATOM 368 O O . ASN A 1 84 ? -8.298 -19.233 64.567 1.00 124.17 ? 97 ASN A O 1 ATOM 369 C CB . ASN A 1 84 ? -6.958 -17.856 66.871 1.00 123.30 ? 97 ASN A CB 1 ATOM 370 C CG . ASN A 1 84 ? -6.983 -18.805 68.047 1.00 130.93 ? 97 ASN A CG 1 ATOM 371 O OD1 . ASN A 1 84 ? -5.938 -19.141 68.607 1.00 133.12 ? 97 ASN A OD1 1 ATOM 372 N ND2 . ASN A 1 84 ? -8.186 -19.204 68.464 1.00 133.54 ? 97 ASN A ND2 1 ATOM 373 N N . GLU A 1 85 ? -6.689 -20.753 64.967 1.00 131.16 ? 98 GLU A N 1 ATOM 374 C CA . GLU A 1 85 ? -7.438 -21.834 64.323 1.00 134.64 ? 98 GLU A CA 1 ATOM 375 C C . GLU A 1 85 ? -8.686 -22.299 65.092 1.00 130.44 ? 98 GLU A C 1 ATOM 376 O O . GLU A 1 85 ? -9.689 -22.623 64.462 1.00 128.71 ? 98 GLU A O 1 ATOM 377 C CB . GLU A 1 85 ? -6.537 -23.033 63.997 1.00 139.66 ? 98 GLU A CB 1 ATOM 378 C CG . GLU A 1 85 ? -5.408 -22.744 63.013 1.00 139.22 ? 98 GLU A CG 1 ATOM 379 C CD . GLU A 1 85 ? -4.957 -23.991 62.249 1.00 145.90 ? 98 GLU A CD 1 ATOM 380 O OE1 . GLU A 1 85 ? -5.474 -25.095 62.540 1.00 150.74 ? 98 GLU A OE1 1 ATOM 381 O OE2 . GLU A 1 85 ? -4.094 -23.872 61.350 1.00 144.58 ? 98 GLU A OE2 1 ATOM 382 N N . PHE A 1 86 ? -8.625 -22.341 66.430 1.00 127.15 ? 99 PHE A N 1 ATOM 383 C CA . PHE A 1 86 ? -9.782 -22.738 67.261 1.00 123.35 ? 99 PHE A CA 1 ATOM 384 C C . PHE A 1 86 ? -9.903 -21.982 68.587 1.00 124.45 ? 99 PHE A C 1 ATOM 385 O O . PHE A 1 86 ? -8.909 -21.571 69.165 1.00 127.69 ? 99 PHE A O 1 ATOM 386 C CB . PHE A 1 86 ? -9.728 -24.218 67.612 1.00 126.00 ? 99 PHE A CB 1 ATOM 387 C CG . PHE A 1 86 ? -8.923 -25.053 66.666 1.00 132.28 ? 99 PHE A CG 1 ATOM 388 C CD1 . PHE A 1 86 ? -7.544 -24.940 66.614 1.00 129.49 ? 99 PHE A CD1 1 ATOM 389 C CD2 . PHE A 1 86 ? -9.544 -25.999 65.862 1.00 140.09 ? 99 PHE A CD2 1 ATOM 390 C CE1 . PHE A 1 86 ? -6.801 -25.735 65.748 1.00 132.54 ? 99 PHE A CE1 1 ATOM 391 C CE2 . PHE A 1 86 ? -8.807 -26.796 64.998 1.00 139.20 ? 99 PHE A CE2 1 ATOM 392 C CZ . PHE A 1 86 ? -7.433 -26.664 64.939 1.00 134.96 ? 99 PHE A CZ 1 ATOM 393 N N . ARG A 1 87 ? -11.122 -21.840 69.093 1.00 130.12 ? 100 ARG A N 1 ATOM 394 C CA . ARG A 1 87 ? -11.337 -21.244 70.417 1.00 140.44 ? 100 ARG A CA 1 ATOM 395 C C . ARG A 1 87 ? -11.075 -22.252 71.540 1.00 138.84 ? 100 ARG A C 1 ATOM 396 O O . ARG A 1 87 ? -11.573 -23.380 71.492 1.00 147.18 ? 100 ARG A O 1 ATOM 397 C CB . ARG A 1 87 ? -12.773 -20.713 70.544 1.00 149.35 ? 100 ARG A CB 1 ATOM 398 C CG . ARG A 1 87 ? -13.201 -19.776 69.424 1.00 150.35 ? 100 ARG A CG 1 ATOM 399 C CD . ARG A 1 87 ? -14.716 -19.764 69.224 1.00 153.59 ? 100 ARG A CD 1 ATOM 400 N NE . ARG A 1 87 ? -15.183 -20.858 68.365 1.00 156.32 ? 100 ARG A NE 1 ATOM 401 C CZ . ARG A 1 87 ? -16.456 -21.051 68.029 1.00 158.22 ? 100 ARG A CZ 1 ATOM 402 N NH1 . ARG A 1 87 ? -17.392 -20.223 68.471 1.00 164.62 ? 100 ARG A NH1 1 ATOM 403 N NH2 . ARG A 1 87 ? -16.798 -22.065 67.249 1.00 153.39 ? 100 ARG A NH2 1 ATOM 404 N N . PHE A 1 88 ? -10.313 -21.846 72.553 1.00 129.62 ? 101 PHE A N 1 ATOM 405 C CA . PHE A 1 88 ? -10.089 -22.699 73.727 1.00 140.45 ? 101 PHE A CA 1 ATOM 406 C C . PHE A 1 88 ? -11.389 -22.861 74.525 1.00 141.86 ? 101 PHE A C 1 ATOM 407 O O . PHE A 1 88 ? -11.611 -23.865 75.203 1.00 133.61 ? 101 PHE A O 1 ATOM 408 C CB . PHE A 1 88 ? -8.997 -22.123 74.634 1.00 147.47 ? 101 PHE A CB 1 ATOM 409 C CG . PHE A 1 88 ? -9.529 -21.282 75.749 1.00 158.22 ? 101 PHE A CG 1 ATOM 410 C CD1 . PHE A 1 88 ? -9.278 -21.616 77.061 1.00 159.40 ? 101 PHE A CD1 1 ATOM 411 C CD2 . PHE A 1 88 ? -10.303 -20.152 75.478 1.00 170.48 ? 101 PHE A CD2 1 ATOM 412 C CE1 . PHE A 1 88 ? -9.785 -20.828 78.090 1.00 172.58 ? 101 PHE A CE1 1 ATOM 413 C CE2 . PHE A 1 88 ? -10.819 -19.360 76.498 1.00 174.25 ? 101 PHE A CE2 1 ATOM 414 C CZ . PHE A 1 88 ? -10.560 -19.696 77.805 1.00 176.25 ? 101 PHE A CZ 1 ATOM 415 N N . SER A 1 89 ? -12.240 -21.846 74.433 1.00 149.84 ? 102 SER A N 1 ATOM 416 C CA . SER A 1 89 ? -13.560 -21.863 75.044 1.00 150.75 ? 102 SER A CA 1 ATOM 417 C C . SER A 1 89 ? -14.316 -23.064 74.511 1.00 145.70 ? 102 SER A C 1 ATOM 418 O O . SER A 1 89 ? -15.085 -23.684 75.221 1.00 148.54 ? 102 SER A O 1 ATOM 419 C CB . SER A 1 89 ? -14.314 -20.566 74.700 1.00 155.13 ? 102 SER A CB 1 ATOM 420 O OG . SER A 1 89 ? -13.606 -19.754 73.751 1.00 146.37 ? 102 SER A OG 1 ATOM 421 N N . ARG A 1 90 ? -14.087 -23.370 73.240 1.00 148.06 ? 103 ARG A N 1 ATOM 422 C CA . ARG A 1 90 ? -14.820 -24.412 72.528 1.00 156.19 ? 103 ARG A CA 1 ATOM 423 C C . ARG A 1 90 ? -14.146 -25.783 72.396 1.00 166.97 ? 103 ARG A C 1 ATOM 424 O O . ARG A 1 90 ? -14.675 -26.663 71.719 1.00 178.50 ? 103 ARG A O 1 ATOM 425 C CB . ARG A 1 90 ? -15.324 -23.905 71.170 1.00 152.00 ? 103 ARG A CB 1 ATOM 426 C CG . ARG A 1 90 ? -16.761 -23.364 71.231 1.00 153.70 ? 103 ARG A CG 1 ATOM 427 C CD . ARG A 1 90 ? -16.971 -22.394 72.400 1.00 155.49 ? 103 ARG A CD 1 ATOM 428 N NE . ARG A 1 90 ? -18.380 -22.044 72.582 1.00 168.46 ? 103 ARG A NE 1 ATOM 429 C CZ . ARG A 1 90 ? -18.972 -20.972 72.061 1.00 177.74 ? 103 ARG A CZ 1 ATOM 430 N NH1 . ARG A 1 90 ? -18.278 -20.122 71.315 1.00 178.71 ? 103 ARG A NH1 1 ATOM 431 N NH2 . ARG A 1 90 ? -20.262 -20.746 72.287 1.00 182.45 ? 103 ARG A NH2 1 ATOM 432 N N . VAL A 1 91 ? -12.986 -25.973 73.018 1.00 163.29 ? 104 VAL A N 1 ATOM 433 C CA . VAL A 1 91 ? -12.330 -27.288 72.977 1.00 156.71 ? 104 VAL A CA 1 ATOM 434 C C . VAL A 1 91 ? -12.557 -28.119 74.255 1.00 163.29 ? 104 VAL A C 1 ATOM 435 O O . VAL A 1 91 ? -12.617 -27.581 75.368 1.00 160.66 ? 104 VAL A O 1 ATOM 436 C CB . VAL A 1 91 ? -10.824 -27.171 72.653 1.00 139.79 ? 104 VAL A CB 1 ATOM 437 C CG1 . VAL A 1 91 ? -9.993 -27.683 73.802 1.00 141.84 ? 104 VAL A CG1 1 ATOM 438 C CG2 . VAL A 1 91 ? -10.508 -27.939 71.395 1.00 129.88 ? 104 VAL A CG2 1 ATOM 439 N N . THR A 1 92 ? -12.690 -29.432 74.084 1.00 172.58 ? 105 THR A N 1 ATOM 440 C CA . THR A 1 92 ? -13.047 -30.321 75.195 1.00 183.02 ? 105 THR A CA 1 ATOM 441 C C . THR A 1 92 ? -11.930 -31.303 75.572 1.00 185.50 ? 105 THR A C 1 ATOM 442 O O . THR A 1 92 ? -10.874 -31.334 74.926 1.00 186.14 ? 105 THR A O 1 ATOM 443 C CB . THR A 1 92 ? -14.310 -31.138 74.866 1.00 183.41 ? 105 THR A CB 1 ATOM 444 O OG1 . THR A 1 92 ? -13.934 -32.361 74.218 1.00 184.72 ? 105 THR A OG1 1 ATOM 445 C CG2 . THR A 1 92 ? -15.240 -30.339 73.960 1.00 178.81 ? 105 THR A CG2 1 ATOM 446 N N . LYS A 1 93 ? -12.168 -32.104 76.614 1.00 179.12 ? 106 LYS A N 1 ATOM 447 C CA . LYS A 1 93 ? -11.195 -33.107 77.019 1.00 167.60 ? 106 LYS A CA 1 ATOM 448 C C . LYS A 1 93 ? -10.948 -33.999 75.810 1.00 171.14 ? 106 LYS A C 1 ATOM 449 O O . LYS A 1 93 ? -9.805 -34.302 75.456 1.00 165.76 ? 106 LYS A O 1 ATOM 450 C CB . LYS A 1 93 ? -11.703 -33.922 78.216 1.00 156.46 ? 106 LYS A CB 1 ATOM 451 N N . ASN A 1 94 ? -12.039 -34.377 75.154 1.00 179.25 ? 107 ASN A N 1 ATOM 452 C CA . ASN A 1 94 ? -11.987 -35.268 74.004 1.00 185.19 ? 107 ASN A CA 1 ATOM 453 C C . ASN A 1 94 ? -10.968 -34.849 72.934 1.00 183.89 ? 107 ASN A C 1 ATOM 454 O O . ASN A 1 94 ? -10.013 -35.583 72.666 1.00 176.39 ? 107 ASN A O 1 ATOM 455 C CB . ASN A 1 94 ? -13.386 -35.444 73.413 1.00 187.10 ? 107 ASN A CB 1 ATOM 456 C CG . ASN A 1 94 ? -13.404 -36.403 72.248 1.00 186.17 ? 107 ASN A CG 1 ATOM 457 O OD1 . ASN A 1 94 ? -12.779 -37.555 72.426 1.00 195.71 ? 107 ASN A OD1 1 ATOM 458 N ND2 . ASN A 1 94 ? -13.957 -36.104 71.190 1.00 173.19 ? 107 ASN A ND2 1 ATOM 459 N N . ASP A 1 95 ? -11.178 -33.678 72.326 1.00 189.48 ? 108 ASP A N 1 ATOM 460 C CA . ASP A 1 95 ? -10.276 -33.162 71.289 1.00 190.08 ? 108 ASP A CA 1 ATOM 461 C C . ASP A 1 95 ? -8.835 -32.948 71.777 1.00 187.05 ? 108 ASP A C 1 ATOM 462 O O . ASP A 1 95 ? -7.886 -33.117 71.003 1.00 182.52 ? 108 ASP A O 1 ATOM 463 C CB . ASP A 1 95 ? -10.792 -31.849 70.679 1.00 188.72 ? 108 ASP A CB 1 ATOM 464 C CG . ASP A 1 95 ? -12.249 -31.575 70.993 1.00 193.52 ? 108 ASP A CG 1 ATOM 465 O OD1 . ASP A 1 95 ? -13.073 -31.574 70.053 1.00 195.07 ? 108 ASP A OD1 1 ATOM 466 O OD2 . ASP A 1 95 ? -12.567 -31.327 72.174 1.00 195.60 ? 108 ASP A OD2 1 ATOM 467 N N . LEU A 1 96 ? -8.673 -32.559 73.043 1.00 186.31 ? 109 LEU A N 1 ATOM 468 C CA . LEU A 1 96 ? -7.340 -32.315 73.603 1.00 180.72 ? 109 LEU A CA 1 ATOM 469 C C . LEU A 1 96 ? -6.475 -33.580 73.658 1.00 188.08 ? 109 LEU A C 1 ATOM 470 O O . LEU A 1 96 ? -5.247 -33.490 73.661 1.00 186.40 ? 109 LEU A O 1 ATOM 471 C CB . LEU A 1 96 ? -7.430 -31.649 74.985 1.00 170.89 ? 109 LEU A CB 1 ATOM 472 N N . TYR A 1 97 ? -7.110 -34.750 73.732 1.00 193.96 ? 110 TYR A N 1 ATOM 473 C CA . TYR A 1 97 ? -6.388 -36.016 73.585 1.00 198.31 ? 110 TYR A CA 1 ATOM 474 C C . TYR A 1 97 ? -5.712 -36.129 72.213 1.00 196.58 ? 110 TYR A C 1 ATOM 475 O O . TYR A 1 97 ? -4.485 -36.045 72.103 1.00 193.85 ? 110 TYR A O 1 ATOM 476 C CB . TYR A 1 97 ? -7.326 -37.205 73.802 1.00 203.22 ? 110 TYR A CB 1 ATOM 477 C CG . TYR A 1 97 ? -6.625 -38.526 74.079 1.00 206.69 ? 110 TYR A CG 1 ATOM 478 C CD1 . TYR A 1 97 ? -6.235 -38.867 75.368 1.00 210.62 ? 110 TYR A CD1 1 ATOM 479 C CD2 . TYR A 1 97 ? -6.373 -39.437 73.058 1.00 207.42 ? 110 TYR A CD2 1 ATOM 480 C CE1 . TYR A 1 97 ? -5.608 -40.072 75.635 1.00 216.03 ? 110 TYR A CE1 1 ATOM 481 C CE2 . TYR A 1 97 ? -5.742 -40.645 73.315 1.00 213.50 ? 110 TYR A CE2 1 ATOM 482 C CZ . TYR A 1 97 ? -5.362 -40.959 74.607 1.00 218.09 ? 110 TYR A CZ 1 ATOM 483 O OH . TYR A 1 97 ? -4.733 -42.158 74.881 1.00 222.66 ? 110 TYR A OH 1 ATOM 484 N N . HIS A 1 98 ? -6.524 -36.296 71.170 1.00 195.61 ? 111 HIS A N 1 ATOM 485 C CA . HIS A 1 98 ? -6.010 -36.539 69.827 1.00 194.11 ? 111 HIS A CA 1 ATOM 486 C C . HIS A 1 98 ? -5.224 -35.335 69.338 1.00 196.69 ? 111 HIS A C 1 ATOM 487 O O . HIS A 1 98 ? -4.053 -35.439 68.959 1.00 200.18 ? 111 HIS A O 1 ATOM 488 C CB . HIS A 1 98 ? -7.150 -36.801 68.838 1.00 191.10 ? 111 HIS A CB 1 ATOM 489 C CG . HIS A 1 98 ? -8.396 -37.361 69.462 1.00 191.30 ? 111 HIS A CG 1 ATOM 490 N ND1 . HIS A 1 98 ? -9.227 -36.852 70.404 1.00 190.08 ? 111 HIS A ND1 1 ATOM 491 C CD2 . HIS A 1 98 ? -8.928 -38.578 69.097 1.00 188.09 ? 111 HIS A CD2 1 ATOM 492 C CE1 . HIS A 1 98 ? -10.229 -37.772 70.598 1.00 190.41 ? 111 HIS A CE1 1 ATOM 493 N NE2 . HIS A 1 98 ? -10.029 -38.803 69.798 1.00 188.29 ? 111 HIS A NE2 1 ATOM 494 N N . ALA A 1 99 ? -5.887 -34.186 69.352 1.00 195.07 ? 112 ALA A N 1 ATOM 495 C CA . ALA A 1 99 ? -5.329 -32.966 68.795 1.00 189.40 ? 112 ALA A CA 1 ATOM 496 C C . ALA A 1 99 ? -4.190 -32.411 69.631 1.00 186.30 ? 112 ALA A C 1 ATOM 497 O O . ALA A 1 99 ? -3.246 -31.839 69.098 1.00 188.65 ? 112 ALA A O 1 ATOM 498 C CB . ALA A 1 99 ? -6.421 -31.922 68.654 1.00 187.57 ? 112 ALA A CB 1 ATOM 499 N N . GLY A 1 100 ? -4.265 -32.615 70.939 1.00 184.22 ? 113 GLY A N 1 ATOM 500 C CA . GLY A 1 100 ? -3.425 -31.888 71.871 1.00 182.43 ? 113 GLY A CA 1 ATOM 501 C C . GLY A 1 100 ? -1.957 -31.783 71.510 1.00 182.49 ? 113 GLY A C 1 ATOM 502 O O . GLY A 1 100 ? -1.342 -30.728 71.682 1.00 178.90 ? 113 GLY A O 1 ATOM 503 N N . GLU A 1 101 ? -1.380 -32.872 71.019 1.00 186.22 ? 114 GLU A N 1 ATOM 504 C CA . GLU A 1 101 ? 0.045 -32.873 70.724 1.00 184.95 ? 114 GLU A CA 1 ATOM 505 C C . GLU A 1 101 ? 0.369 -32.144 69.415 1.00 183.72 ? 114 GLU A C 1 ATOM 506 O O . GLU A 1 101 ? 1.518 -31.767 69.176 1.00 184.13 ? 114 GLU A O 1 ATOM 507 C CB . GLU A 1 101 ? 0.590 -34.299 70.697 1.00 188.49 ? 114 GLU A CB 1 ATOM 508 C CG . GLU A 1 101 ? 2.075 -34.376 70.968 1.00 188.53 ? 114 GLU A CG 1 ATOM 509 C CD . GLU A 1 101 ? 2.714 -35.594 70.347 1.00 191.55 ? 114 GLU A CD 1 ATOM 510 O OE1 . GLU A 1 101 ? 2.999 -35.572 69.128 1.00 186.24 ? 114 GLU A OE1 1 ATOM 511 O OE2 . GLU A 1 101 ? 2.934 -36.573 71.084 1.00 201.27 ? 114 GLU A OE2 1 ATOM 512 N N . LEU A 1 102 ? -0.648 -31.946 68.578 1.00 181.60 ? 115 LEU A N 1 ATOM 513 C CA . LEU A 1 102 ? -0.497 -31.249 67.297 1.00 174.13 ? 115 LEU A CA 1 ATOM 514 C C . LEU A 1 102 ? -0.433 -29.725 67.464 1.00 167.32 ? 115 LEU A C 1 ATOM 515 O O . LEU A 1 102 ? 0.184 -29.026 66.653 1.00 161.06 ? 115 LEU A O 1 ATOM 516 C CB . LEU A 1 102 ? -1.644 -31.635 66.358 1.00 173.99 ? 115 LEU A CB 1 ATOM 517 C CG . LEU A 1 102 ? -1.663 -31.068 64.940 1.00 168.44 ? 115 LEU A CG 1 ATOM 518 C CD1 . LEU A 1 102 ? -0.258 -30.995 64.366 1.00 167.77 ? 115 LEU A CD1 1 ATOM 519 C CD2 . LEU A 1 102 ? -2.571 -31.920 64.065 1.00 168.19 ? 115 LEU A CD2 1 ATOM 520 N N . LEU A 1 103 ? -1.066 -29.231 68.529 1.00 166.02 ? 116 LEU A N 1 ATOM 521 C CA . LEU A 1 103 ? -1.099 -27.809 68.871 1.00 159.10 ? 116 LEU A CA 1 ATOM 522 C C . LEU A 1 103 ? 0.046 -27.475 69.821 1.00 159.10 ? 116 LEU A C 1 ATOM 523 O O . LEU A 1 103 ? 0.147 -26.358 70.330 1.00 154.93 ? 116 LEU A O 1 ATOM 524 C CB . LEU A 1 103 ? -2.428 -27.467 69.544 1.00 156.40 ? 116 LEU A CB 1 ATOM 525 C CG . LEU A 1 103 ? -3.715 -27.409 68.715 1.00 148.29 ? 116 LEU A CG 1 ATOM 526 C CD1 . LEU A 1 103 ? -3.666 -28.373 67.537 1.00 147.68 ? 116 LEU A CD1 1 ATOM 527 C CD2 . LEU A 1 103 ? -4.921 -27.702 69.600 1.00 143.59 ? 116 LEU A CD2 1 ATOM 528 N N . ALA A 1 104 ? 0.888 -28.471 70.072 1.00 164.94 ? 117 ALA A N 1 ATOM 529 C CA . ALA A 1 104 ? 2.034 -28.346 70.962 1.00 166.17 ? 117 ALA A CA 1 ATOM 530 C C . ALA A 1 104 ? 1.610 -28.052 72.386 1.00 164.89 ? 117 ALA A C 1 ATOM 531 O O . ALA A 1 104 ? 2.368 -27.455 73.152 1.00 167.89 ? 117 ALA A O 1 ATOM 532 C CB . ALA A 1 104 ? 2.994 -27.273 70.468 1.00 163.63 ? 117 ALA A CB 1 ATOM 533 N N . LEU A 1 105 ? 0.397 -28.452 72.742 1.00 160.07 ? 118 LEU A N 1 ATOM 534 C CA . LEU A 1 105 ? -0.057 -28.269 74.113 1.00 159.57 ? 118 LEU A CA 1 ATOM 535 C C . LEU A 1 105 ? 0.231 -29.526 74.937 1.00 170.08 ? 118 LEU A C 1 ATOM 536 O O . LEU A 1 105 ? -0.120 -29.593 76.115 1.00 169.53 ? 118 LEU A O 1 ATOM 537 C CB . LEU A 1 105 ? -1.551 -27.901 74.149 1.00 149.63 ? 118 LEU A CB 1 ATOM 538 N N . LEU A 1 106 ? 0.889 -30.508 74.310 1.00 175.50 ? 119 LEU A N 1 ATOM 539 C CA . LEU A 1 106 ? 1.093 -31.837 74.906 1.00 175.24 ? 119 LEU A CA 1 ATOM 540 C C . LEU A 1 106 ? 2.420 -32.541 74.559 1.00 170.99 ? 119 LEU A C 1 ATOM 541 O O . LEU A 1 106 ? 3.109 -32.187 73.589 1.00 161.20 ? 119 LEU A O 1 ATOM 542 C CB . LEU A 1 106 ? -0.076 -32.770 74.562 1.00 173.85 ? 119 LEU A CB 1 ATOM 543 C CG . LEU A 1 106 ? -1.413 -32.529 75.263 1.00 166.56 ? 119 LEU A CG 1 ATOM 544 C CD1 . LEU A 1 106 ? -2.407 -33.621 74.881 1.00 170.06 ? 119 LEU A CD1 1 ATOM 545 C CD2 . LEU A 1 106 ? -1.224 -32.468 76.772 1.00 159.80 ? 119 LEU A CD2 1 ATOM 546 N N . ASN A 1 107 ? 2.750 -33.559 75.361 1.00 171.84 ? 120 ASN A N 1 ATOM 547 C CA . ASN A 1 107 ? 4.002 -34.299 75.218 1.00 160.52 ? 120 ASN A CA 1 ATOM 548 C C . ASN A 1 107 ? 3.766 -35.608 74.488 1.00 173.93 ? 120 ASN A C 1 ATOM 549 O O . ASN A 1 107 ? 2.624 -35.989 74.214 1.00 178.49 ? 120 ASN A O 1 ATOM 550 C CB . ASN A 1 107 ? 4.602 -34.584 76.603 1.00 138.27 ? 120 ASN A CB 1 ATOM 551 N N . ASN A 1 108 ? 4.853 -36.313 74.197 1.00 180.21 ? 121 ASN A N 1 ATOM 552 C CA . ASN A 1 108 ? 4.742 -37.685 73.742 1.00 185.44 ? 121 ASN A CA 1 ATOM 553 C C . ASN A 1 108 ? 3.940 -38.403 74.804 1.00 194.83 ? 121 ASN A C 1 ATOM 554 O O . ASN A 1 108 ? 3.184 -39.326 74.517 1.00 202.00 ? 121 ASN A O 1 ATOM 555 C CB . ASN A 1 108 ? 6.124 -38.329 73.618 1.00 188.72 ? 121 ASN A CB 1 ATOM 556 C CG . ASN A 1 108 ? 7.006 -37.638 72.605 1.00 192.08 ? 121 ASN A CG 1 ATOM 557 O OD1 . ASN A 1 108 ? 6.786 -36.476 72.260 1.00 193.13 ? 121 ASN A OD1 1 ATOM 558 N ND2 . ASN A 1 108 ? 8.018 -38.351 72.121 1.00 194.58 ? 121 ASN A ND2 1 ATOM 559 N N . ARG A 1 109 ? 4.103 -37.941 76.041 1.00 200.12 ? 122 ARG A N 1 ATOM 560 C CA . ARG A 1 109 ? 3.469 -38.555 77.206 1.00 206.93 ? 122 ARG A CA 1 ATOM 561 C C . ARG A 1 109 ? 2.081 -37.985 77.546 1.00 202.90 ? 122 ARG A C 1 ATOM 562 O O . ARG A 1 109 ? 1.520 -38.322 78.592 1.00 206.29 ? 122 ARG A O 1 ATOM 563 C CB . ARG A 1 109 ? 4.400 -38.492 78.423 1.00 206.89 ? 122 ARG A CB 1 ATOM 564 N N . TYR A 1 110 ? 1.543 -37.123 76.677 1.00 189.99 ? 123 TYR A N 1 ATOM 565 C CA . TYR A 1 110 ? 0.239 -36.494 76.904 1.00 177.83 ? 123 TYR A CA 1 ATOM 566 C C . TYR A 1 110 ? 0.289 -35.509 78.060 1.00 177.93 ? 123 TYR A C 1 ATOM 567 O O . TYR A 1 110 ? -0.682 -35.359 78.802 1.00 176.22 ? 123 TYR A O 1 ATOM 568 C CB . TYR A 1 110 ? -0.823 -37.555 77.200 1.00 176.29 ? 123 TYR A CB 1 ATOM 569 C CG . TYR A 1 110 ? -1.257 -38.327 75.984 1.00 177.38 ? 123 TYR A CG 1 ATOM 570 C CD1 . TYR A 1 110 ? -2.600 -38.517 75.703 1.00 172.32 ? 123 TYR A CD1 1 ATOM 571 C CD2 . TYR A 1 110 ? -0.322 -38.838 75.092 1.00 182.74 ? 123 TYR A CD2 1 ATOM 572 C CE1 . TYR A 1 110 ? -2.997 -39.205 74.574 1.00 173.40 ? 123 TYR A CE1 1 ATOM 573 C CE2 . TYR A 1 110 ? -0.713 -39.530 73.960 1.00 182.46 ? 123 TYR A CE2 1 ATOM 574 C CZ . TYR A 1 110 ? -2.052 -39.710 73.707 1.00 178.06 ? 123 TYR A CZ 1 ATOM 575 O OH . TYR A 1 110 ? -2.449 -40.391 72.580 1.00 179.46 ? 123 TYR A OH 1 ATOM 576 N N . GLU A 1 111 ? 1.413 -34.812 78.183 1.00 181.76 ? 124 GLU A N 1 ATOM 577 C CA . GLU A 1 111 ? 1.649 -33.911 79.305 1.00 189.94 ? 124 GLU A CA 1 ATOM 578 C C . GLU A 1 111 ? 2.196 -32.572 78.829 1.00 194.03 ? 124 GLU A C 1 ATOM 579 O O . GLU A 1 111 ? 2.569 -32.421 77.670 1.00 194.82 ? 124 GLU A O 1 ATOM 580 C CB . GLU A 1 111 ? 2.594 -34.553 80.321 1.00 193.70 ? 124 GLU A CB 1 ATOM 581 N N . ILE A 1 112 ? 2.243 -31.604 79.738 1.00 195.58 ? 125 ILE A N 1 ATOM 582 C CA . ILE A 1 112 ? 2.654 -30.236 79.416 1.00 188.32 ? 125 ILE A CA 1 ATOM 583 C C . ILE A 1 112 ? 4.158 -29.962 79.597 1.00 191.19 ? 125 ILE A C 1 ATOM 584 O O . ILE A 1 112 ? 4.682 -30.033 80.706 1.00 190.39 ? 125 ILE A O 1 ATOM 585 C CB . ILE A 1 112 ? 1.875 -29.236 80.281 1.00 182.64 ? 125 ILE A CB 1 ATOM 586 C CG1 . ILE A 1 112 ? 0.762 -29.946 81.067 1.00 173.43 ? 125 ILE A CG1 1 ATOM 587 C CG2 . ILE A 1 112 ? 1.338 -28.111 79.419 1.00 183.70 ? 125 ILE A CG2 1 ATOM 588 C CD1 . ILE A 1 112 ? -0.445 -30.329 80.243 1.00 167.55 ? 125 ILE A CD1 1 ATOM 589 N N . PRO A 1 113 ? 4.847 -29.587 78.512 1.00 199.76 ? 126 PRO A N 1 ATOM 590 C CA . PRO A 1 113 ? 6.313 -29.482 78.527 1.00 208.01 ? 126 PRO A CA 1 ATOM 591 C C . PRO A 1 113 ? 6.834 -28.483 79.560 1.00 214.25 ? 126 PRO A C 1 ATOM 592 O O . PRO A 1 113 ? 6.054 -27.701 80.100 1.00 213.85 ? 126 PRO A O 1 ATOM 593 C CB . PRO A 1 113 ? 6.642 -28.993 77.110 1.00 204.62 ? 126 PRO A CB 1 ATOM 594 C CG . PRO A 1 113 ? 5.398 -28.322 76.637 1.00 199.86 ? 126 PRO A CG 1 ATOM 595 C CD . PRO A 1 113 ? 4.271 -29.106 77.244 1.00 200.58 ? 126 PRO A CD 1 ATOM 596 N N . ASP A 1 114 ? 8.129 -28.544 79.865 1.00 222.79 ? 127 ASP A N 1 ATOM 597 C CA . ASP A 1 114 ? 8.771 -27.488 80.649 1.00 226.87 ? 127 ASP A CA 1 ATOM 598 C C . ASP A 1 114 ? 8.734 -26.165 79.872 1.00 220.49 ? 127 ASP A C 1 ATOM 599 O O . ASP A 1 114 ? 8.977 -25.088 80.426 1.00 219.68 ? 127 ASP A O 1 ATOM 600 C CB . ASP A 1 114 ? 10.210 -27.867 81.058 1.00 228.02 ? 127 ASP A CB 1 ATOM 601 C CG . ASP A 1 114 ? 11.142 -28.086 79.863 1.00 223.14 ? 127 ASP A CG 1 ATOM 602 O OD1 . ASP A 1 114 ? 10.728 -28.741 78.882 1.00 224.62 ? 127 ASP A OD1 1 ATOM 603 O OD2 . ASP A 1 114 ? 12.301 -27.613 79.915 1.00 217.16 ? 127 ASP A OD2 1 ATOM 604 N N . THR A 1 115 ? 8.396 -26.265 78.589 1.00 212.05 ? 128 THR A N 1 ATOM 605 C CA . THR A 1 115 ? 8.250 -25.110 77.720 1.00 204.29 ? 128 THR A CA 1 ATOM 606 C C . THR A 1 115 ? 6.850 -24.525 77.844 1.00 204.81 ? 128 THR A C 1 ATOM 607 O O . THR A 1 115 ? 6.494 -23.594 77.114 1.00 203.54 ? 128 THR A O 1 ATOM 608 C CB . THR A 1 115 ? 8.477 -25.480 76.246 1.00 200.63 ? 128 THR A CB 1 ATOM 609 O OG1 . THR A 1 115 ? 7.380 -26.274 75.779 1.00 199.85 ? 128 THR A OG1 1 ATOM 610 C CG2 . THR A 1 115 ? 9.769 -26.259 76.083 1.00 203.07 ? 128 THR A CG2 1 ATOM 611 N N . GLN A 1 116 ? 6.050 -25.078 78.755 1.00 205.53 ? 129 GLN A N 1 ATOM 612 C CA . GLN A 1 116 ? 4.661 -24.652 78.891 1.00 201.80 ? 129 GLN A CA 1 ATOM 613 C C . GLN A 1 116 ? 4.577 -23.293 79.567 1.00 201.05 ? 129 GLN A C 1 ATOM 614 O O . GLN A 1 116 ? 5.008 -23.118 80.710 1.00 200.08 ? 129 GLN A O 1 ATOM 615 C CB . GLN A 1 116 ? 3.843 -25.683 79.666 1.00 199.97 ? 129 GLN A CB 1 ATOM 616 N N . THR A 1 117 ? 4.005 -22.339 78.838 1.00 197.12 ? 130 THR A N 1 ATOM 617 C CA . THR A 1 117 ? 3.857 -20.962 79.294 1.00 183.94 ? 130 THR A CA 1 ATOM 618 C C . THR A 1 117 ? 2.402 -20.523 79.137 1.00 180.24 ? 130 THR A C 1 ATOM 619 O O . THR A 1 117 ? 1.933 -20.331 78.014 1.00 183.99 ? 130 THR A O 1 ATOM 620 C CB . THR A 1 117 ? 4.730 -20.038 78.432 1.00 166.24 ? 130 THR A CB 1 ATOM 621 O OG1 . THR A 1 117 ? 4.652 -20.461 77.064 1.00 145.79 ? 130 THR A OG1 1 ATOM 622 C CG2 . THR A 1 117 ? 6.187 -20.103 78.876 1.00 172.10 ? 130 THR A CG2 1 ATOM 623 N N . ALA A 1 118 ? 1.700 -20.327 80.251 1.00 168.73 ? 131 ALA A N 1 ATOM 624 C CA . ALA A 1 118 ? 0.255 -20.133 80.181 1.00 157.83 ? 131 ALA A CA 1 ATOM 625 C C . ALA A 1 118 ? -0.331 -19.355 81.351 1.00 158.66 ? 131 ALA A C 1 ATOM 626 O O . ALA A 1 118 ? 0.246 -19.305 82.430 1.00 153.39 ? 131 ALA A O 1 ATOM 627 C CB . ALA A 1 118 ? -0.452 -21.471 80.014 1.00 152.94 ? 131 ALA A CB 1 ATOM 628 N N . ASP A 1 119 ? -1.514 -18.794 81.119 1.00 168.55 ? 132 ASP A N 1 ATOM 629 C CA . ASP A 1 119 ? -2.092 -17.741 81.954 1.00 176.58 ? 132 ASP A CA 1 ATOM 630 C C . ASP A 1 119 ? -2.440 -18.166 83.379 1.00 188.55 ? 132 ASP A C 1 ATOM 631 O O . ASP A 1 119 ? -2.540 -19.357 83.692 1.00 188.32 ? 132 ASP A O 1 ATOM 632 C CB . ASP A 1 119 ? -3.315 -17.135 81.268 1.00 176.58 ? 132 ASP A CB 1 ATOM 633 N N . GLU A 1 120 ? -2.611 -17.172 84.245 1.00 196.51 ? 133 GLU A N 1 ATOM 634 C CA . GLU A 1 120 ? -2.920 -17.418 85.644 1.00 200.71 ? 133 GLU A CA 1 ATOM 635 C C . GLU A 1 120 ? -4.068 -18.412 85.758 1.00 198.09 ? 133 GLU A C 1 ATOM 636 O O . GLU A 1 120 ? -3.927 -19.456 86.388 1.00 196.04 ? 133 GLU A O 1 ATOM 637 C CB . GLU A 1 120 ? -3.289 -16.101 86.349 1.00 205.69 ? 133 GLU A CB 1 ATOM 638 C CG . GLU A 1 120 ? -4.695 -15.556 86.027 1.00 208.90 ? 133 GLU A CG 1 ATOM 639 C CD . GLU A 1 120 ? -4.874 -14.098 86.425 1.00 209.72 ? 133 GLU A CD 1 ATOM 640 O OE1 . GLU A 1 120 ? -3.925 -13.310 86.228 1.00 208.00 ? 133 GLU A OE1 1 ATOM 641 O OE2 . GLU A 1 120 ? -5.961 -13.739 86.931 1.00 212.01 ? 133 GLU A OE2 1 ATOM 642 N N . LYS A 1 121 ? -5.189 -18.091 85.116 1.00 195.71 ? 134 LYS A N 1 ATOM 643 C CA . LYS A 1 121 ? -6.429 -18.850 85.272 1.00 191.67 ? 134 LYS A CA 1 ATOM 644 C C . LYS A 1 121 ? -6.465 -20.115 84.430 1.00 185.02 ? 134 LYS A C 1 ATOM 645 O O . LYS A 1 121 ? -7.199 -21.048 84.753 1.00 187.69 ? 134 LYS A O 1 ATOM 646 C CB . LYS A 1 121 ? -7.642 -17.971 84.958 1.00 189.51 ? 134 LYS A CB 1 ATOM 647 N N . GLN A 1 122 ? -5.676 -20.143 83.358 1.00 175.96 ? 135 GLN A N 1 ATOM 648 C CA . GLN A 1 122 ? -5.712 -21.249 82.403 1.00 171.35 ? 135 GLN A CA 1 ATOM 649 C C . GLN A 1 122 ? -5.304 -22.572 83.040 1.00 190.80 ? 135 GLN A C 1 ATOM 650 O O . GLN A 1 122 ? -5.803 -23.628 82.662 1.00 198.30 ? 135 GLN A O 1 ATOM 651 C CB . GLN A 1 122 ? -4.839 -20.954 81.205 1.00 153.70 ? 135 GLN A CB 1 ATOM 652 N N . LEU A 1 123 ? -4.396 -22.515 84.009 1.00 196.09 ? 136 LEU A N 1 ATOM 653 C CA . LEU A 1 123 ? -3.953 -23.724 84.692 1.00 195.48 ? 136 LEU A CA 1 ATOM 654 C C . LEU A 1 123 ? -5.157 -24.524 85.159 1.00 193.59 ? 136 LEU A C 1 ATOM 655 O O . LEU A 1 123 ? -5.496 -25.540 84.560 1.00 193.98 ? 136 LEU A O 1 ATOM 656 C CB . LEU A 1 123 ? -3.081 -23.368 85.875 1.00 199.68 ? 136 LEU A CB 1 ATOM 657 N N . GLU A 1 124 ? -5.834 -24.028 86.191 1.00 196.16 ? 137 GLU A N 1 ATOM 658 C CA . GLU A 1 124 ? -6.945 -24.758 86.806 1.00 205.02 ? 137 GLU A CA 1 ATOM 659 C C . GLU A 1 124 ? -8.020 -25.178 85.800 1.00 205.29 ? 137 GLU A C 1 ATOM 660 O O . GLU A 1 124 ? -8.680 -26.209 85.980 1.00 208.28 ? 137 GLU A O 1 ATOM 661 C CB . GLU A 1 124 ? -7.561 -23.943 87.951 1.00 205.75 ? 137 GLU A CB 1 ATOM 662 N N . ILE A 1 125 ? -8.211 -24.360 84.765 1.00 197.06 ? 138 ILE A N 1 ATOM 663 C CA . ILE A 1 125 ? -9.184 -24.647 83.713 1.00 186.70 ? 138 ILE A CA 1 ATOM 664 C C . ILE A 1 125 ? -8.631 -25.552 82.611 1.00 180.36 ? 138 ILE A C 1 ATOM 665 O O . ILE A 1 125 ? -9.398 -26.200 81.899 1.00 179.84 ? 138 ILE A O 1 ATOM 666 C CB . ILE A 1 125 ? -9.753 -23.348 83.090 1.00 176.87 ? 138 ILE A CB 1 ATOM 667 C CG1 . ILE A 1 125 ? -8.747 -22.748 82.095 1.00 164.06 ? 138 ILE A CG1 1 ATOM 668 C CG2 . ILE A 1 125 ? -10.207 -22.363 84.209 1.00 130.26 ? 138 ILE A CG2 1 ATOM 669 C CD1 . ILE A 1 125 ? -9.149 -21.399 81.501 1.00 155.27 ? 138 ILE A CD1 1 ATOM 670 N N . LEU A 1 126 ? -7.306 -25.598 82.477 1.00 175.65 ? 139 LEU A N 1 ATOM 671 C CA . LEU A 1 126 ? -6.660 -26.444 81.468 1.00 176.89 ? 139 LEU A CA 1 ATOM 672 C C . LEU A 1 126 ? -6.582 -27.893 81.927 1.00 189.06 ? 139 LEU A C 1 ATOM 673 O O . LEU A 1 126 ? -6.805 -28.810 81.142 1.00 195.00 ? 139 LEU A O 1 ATOM 674 C CB . LEU A 1 126 ? -5.253 -25.945 81.134 1.00 173.27 ? 139 LEU A CB 1 ATOM 675 C CG . LEU A 1 126 ? -4.957 -25.263 79.780 1.00 171.94 ? 139 LEU A CG 1 ATOM 676 C CD1 . LEU A 1 126 ? -5.241 -26.176 78.590 1.00 165.54 ? 139 LEU A CD1 1 ATOM 677 C CD2 . LEU A 1 126 ? -5.698 -23.937 79.618 1.00 173.64 ? 139 LEU A CD2 1 ATOM 678 N N . GLN A 1 127 ? -6.273 -28.089 83.206 1.00 191.04 ? 140 GLN A N 1 ATOM 679 C CA . GLN A 1 127 ? -6.065 -29.421 83.774 1.00 188.35 ? 140 GLN A CA 1 ATOM 680 C C . GLN A 1 127 ? -7.342 -30.172 84.136 1.00 194.23 ? 140 GLN A C 1 ATOM 681 O O . GLN A 1 127 ? -7.383 -31.395 84.046 1.00 196.71 ? 140 GLN A O 1 ATOM 682 C CB . GLN A 1 127 ? -5.156 -29.330 84.992 1.00 184.10 ? 140 GLN A CB 1 ATOM 683 C CG . GLN A 1 127 ? -3.823 -28.672 84.699 1.00 175.78 ? 140 GLN A CG 1 ATOM 684 C CD . GLN A 1 127 ? -3.231 -28.031 85.932 1.00 174.94 ? 140 GLN A CD 1 ATOM 685 O OE1 . GLN A 1 127 ? -3.929 -27.824 86.932 1.00 184.48 ? 140 GLN A OE1 1 ATOM 686 N NE2 . GLN A 1 127 ? -1.937 -27.718 85.878 1.00 160.82 ? 140 GLN A NE2 1 ATOM 687 N N . ASP A 1 128 ? -8.369 -29.450 84.574 1.00 198.79 ? 141 ASP A N 1 ATOM 688 C CA . ASP A 1 128 ? -9.670 -30.067 84.807 1.00 206.39 ? 141 ASP A CA 1 ATOM 689 C C . ASP A 1 128 ? -10.097 -30.706 83.492 1.00 204.68 ? 141 ASP A C 1 ATOM 690 O O . ASP A 1 128 ? -10.805 -31.718 83.472 1.00 205.26 ? 141 ASP A O 1 ATOM 691 C CB . ASP A 1 128 ? -10.695 -29.021 85.257 1.00 207.90 ? 141 ASP A CB 1 ATOM 692 C CG . ASP A 1 128 ? -11.986 -29.644 85.769 1.00 213.00 ? 141 ASP A CG 1 ATOM 693 O OD1 . ASP A 1 128 ? -12.202 -30.853 85.540 1.00 215.66 ? 141 ASP A OD1 1 ATOM 694 O OD2 . ASP A 1 128 ? -12.786 -28.917 86.397 1.00 214.55 ? 141 ASP A OD2 1 ATOM 695 N N . LYS A 1 129 ? -9.656 -30.092 82.394 1.00 197.29 ? 142 LYS A N 1 ATOM 696 C CA . LYS A 1 129 ? -9.845 -30.639 81.057 1.00 191.77 ? 142 LYS A CA 1 ATOM 697 C C . LYS A 1 129 ? -8.654 -31.496 80.642 1.00 192.43 ? 142 LYS A C 1 ATOM 698 O O . LYS A 1 129 ? -8.705 -32.188 79.631 1.00 195.65 ? 142 LYS A O 1 ATOM 699 C CB . LYS A 1 129 ? -10.066 -29.512 80.047 1.00 182.64 ? 142 LYS A CB 1 ATOM 700 N N . ALA A 1 130 ? -7.578 -31.439 81.418 1.00 192.38 ? 143 ALA A N 1 ATOM 701 C CA . ALA A 1 130 ? -6.367 -32.199 81.106 1.00 196.09 ? 143 ALA A CA 1 ATOM 702 C C . ALA A 1 130 ? -6.198 -33.513 81.884 1.00 197.72 ? 143 ALA A C 1 ATOM 703 O O . ALA A 1 130 ? -5.197 -34.214 81.709 1.00 192.17 ? 143 ALA A O 1 ATOM 704 C CB . ALA A 1 130 ? -5.128 -31.321 81.260 1.00 197.97 ? 143 ALA A CB 1 ATOM 705 N N . ASN A 1 131 ? -7.167 -33.855 82.729 1.00 202.77 ? 144 ASN A N 1 ATOM 706 C CA . ASN A 1 131 ? -7.013 -35.018 83.593 1.00 205.05 ? 144 ASN A CA 1 ATOM 707 C C . ASN A 1 131 ? -7.260 -36.310 82.829 1.00 200.00 ? 144 ASN A C 1 ATOM 708 O O . ASN A 1 131 ? -8.364 -36.574 82.353 1.00 197.45 ? 144 ASN A O 1 ATOM 709 C CB . ASN A 1 131 ? -7.969 -34.925 84.784 1.00 213.67 ? 144 ASN A CB 1 ATOM 710 C CG . ASN A 1 131 ? -9.428 -34.876 84.361 1.00 219.70 ? 144 ASN A CG 1 ATOM 711 O OD1 . ASN A 1 131 ? -9.741 -34.688 83.183 1.00 217.57 ? 144 ASN A OD1 1 ATOM 712 N ND2 . ASN A 1 131 ? -10.331 -35.021 85.329 1.00 225.16 ? 144 ASN A ND2 1 ATOM 713 N N . PHE A 1 132 ? -6.212 -37.117 82.722 1.00 199.10 ? 145 PHE A N 1 ATOM 714 C CA . PHE A 1 132 ? -6.290 -38.399 82.028 1.00 200.14 ? 145 PHE A CA 1 ATOM 715 C C . PHE A 1 132 ? -6.447 -39.611 82.979 1.00 210.40 ? 145 PHE A C 1 ATOM 716 O O . PHE A 1 132 ? -6.567 -40.761 82.535 1.00 215.65 ? 145 PHE A O 1 ATOM 717 C CB . PHE A 1 132 ? -5.109 -38.548 81.061 1.00 185.77 ? 145 PHE A CB 1 ATOM 718 C CG . PHE A 1 132 ? -5.161 -37.594 79.887 1.00 173.91 ? 145 PHE A CG 1 ATOM 719 C CD1 . PHE A 1 132 ? -6.345 -37.385 79.194 1.00 165.54 ? 145 PHE A CD1 1 ATOM 720 C CD2 . PHE A 1 132 ? -4.028 -36.896 79.481 1.00 164.78 ? 145 PHE A CD2 1 ATOM 721 C CE1 . PHE A 1 132 ? -6.392 -36.508 78.111 1.00 148.67 ? 145 PHE A CE1 1 ATOM 722 C CE2 . PHE A 1 132 ? -4.074 -36.026 78.405 1.00 145.53 ? 145 PHE A CE2 1 ATOM 723 C CZ . PHE A 1 132 ? -5.258 -35.837 77.723 1.00 139.39 ? 145 PHE A CZ 1 ATOM 724 N N . ARG A 1 133 ? -6.450 -39.351 84.284 1.00 205.97 ? 146 ARG A N 1 ATOM 725 C CA . ARG A 1 133 ? -6.807 -40.384 85.239 1.00 209.26 ? 146 ARG A CA 1 ATOM 726 C C . ARG A 1 133 ? -8.234 -40.816 84.893 1.00 221.71 ? 146 ARG A C 1 ATOM 727 O O . ARG A 1 133 ? -9.084 -39.969 84.608 1.00 219.07 ? 146 ARG A O 1 ATOM 728 C CB . ARG A 1 133 ? -6.717 -39.859 86.679 1.00 203.59 ? 146 ARG A CB 1 ATOM 729 C CG . ARG A 1 133 ? -5.362 -39.261 87.079 1.00 193.22 ? 146 ARG A CG 1 ATOM 730 C CD . ARG A 1 133 ? -5.326 -38.891 88.571 1.00 193.88 ? 146 ARG A CD 1 ATOM 731 N NE . ARG A 1 133 ? -4.691 -39.920 89.395 1.00 203.89 ? 146 ARG A NE 1 ATOM 732 C CZ . ARG A 1 133 ? -4.901 -40.096 90.702 1.00 212.55 ? 146 ARG A CZ 1 ATOM 733 N NH1 . ARG A 1 133 ? -5.746 -39.313 91.357 1.00 217.92 ? 146 ARG A NH1 1 ATOM 734 N NH2 . ARG A 1 133 ? -4.268 -41.064 91.361 1.00 211.55 ? 146 ARG A NH2 1 ATOM 735 N N . ASN A 1 134 ? -8.483 -42.127 84.891 1.00 235.68 ? 147 ASN A N 1 ATOM 736 C CA . ASN A 1 134 ? -9.781 -42.690 84.494 1.00 242.25 ? 147 ASN A CA 1 ATOM 737 C C . ASN A 1 134 ? -10.302 -42.074 83.192 1.00 244.56 ? 147 ASN A C 1 ATOM 738 O O . ASN A 1 134 ? -11.447 -41.624 83.118 1.00 244.73 ? 147 ASN A O 1 ATOM 739 C CB . ASN A 1 134 ? -10.809 -42.554 85.616 1.00 241.34 ? 147 ASN A CB 1 ATOM 740 N N . PHE A 1 135 ? -9.453 -42.063 82.168 1.00 245.57 ? 148 PHE A N 1 ATOM 741 C CA . PHE A 1 135 ? -9.794 -41.444 80.891 1.00 245.40 ? 148 PHE A CA 1 ATOM 742 C C . PHE A 1 135 ? -10.538 -42.391 79.955 1.00 253.23 ? 148 PHE A C 1 ATOM 743 O O . PHE A 1 135 ? -10.073 -43.496 79.683 1.00 259.95 ? 148 PHE A O 1 ATOM 744 C CB . PHE A 1 135 ? -8.535 -40.933 80.214 1.00 242.24 ? 148 PHE A CB 1 ATOM 745 N N . LYS A 1 136 ? -11.690 -41.948 79.460 1.00 254.23 ? 149 LYS A N 1 ATOM 746 C CA . LYS A 1 136 ? -12.423 -42.670 78.422 1.00 258.97 ? 149 LYS A CA 1 ATOM 747 C C . LYS A 1 136 ? -12.524 -41.840 77.132 1.00 259.81 ? 149 LYS A C 1 ATOM 748 O O . LYS A 1 136 ? -13.220 -40.821 77.101 1.00 263.41 ? 149 LYS A O 1 ATOM 749 C CB . LYS A 1 136 ? -13.812 -43.053 78.924 1.00 260.56 ? 149 LYS A CB 1 ATOM 750 N N . PRO A 1 137 ? -11.816 -42.266 76.067 1.00 253.33 ? 150 PRO A N 1 ATOM 751 C CA . PRO A 1 137 ? -11.798 -41.569 74.768 1.00 241.57 ? 150 PRO A CA 1 ATOM 752 C C . PRO A 1 137 ? -13.054 -41.782 73.910 1.00 234.32 ? 150 PRO A C 1 ATOM 753 O O . PRO A 1 137 ? -13.784 -42.754 74.100 1.00 241.16 ? 150 PRO A O 1 ATOM 754 C CB . PRO A 1 137 ? -10.576 -42.174 74.057 1.00 241.38 ? 150 PRO A CB 1 ATOM 755 C CG . PRO A 1 137 ? -9.769 -42.821 75.142 1.00 247.08 ? 150 PRO A CG 1 ATOM 756 C CD . PRO A 1 137 ? -10.773 -43.302 76.143 1.00 254.34 ? 150 PRO A CD 1 ATOM 757 N N . LYS A 1 138 ? -13.293 -40.860 72.978 1.00 219.69 ? 151 LYS A N 1 ATOM 758 C CA . LYS A 1 138 ? -14.388 -40.956 72.011 1.00 209.69 ? 151 LYS A CA 1 ATOM 759 C C . LYS A 1 138 ? -13.957 -40.330 70.676 1.00 203.09 ? 151 LYS A C 1 ATOM 760 O O . LYS A 1 138 ? -13.162 -39.388 70.656 1.00 203.18 ? 151 LYS A O 1 ATOM 761 C CB . LYS A 1 138 ? -15.639 -40.279 72.552 1.00 204.83 ? 151 LYS A CB 1 ATOM 762 N N . PRO A 1 139 ? -14.489 -40.836 69.553 1.00 195.40 ? 152 PRO A N 1 ATOM 763 C CA . PRO A 1 139 ? -13.999 -40.454 68.219 1.00 194.76 ? 152 PRO A CA 1 ATOM 764 C C . PRO A 1 139 ? -14.181 -38.973 67.858 1.00 197.33 ? 152 PRO A C 1 ATOM 765 O O . PRO A 1 139 ? -15.100 -38.324 68.352 1.00 199.72 ? 152 PRO A O 1 ATOM 766 C CB . PRO A 1 139 ? -14.845 -41.325 67.284 1.00 190.17 ? 152 PRO A CB 1 ATOM 767 C CG . PRO A 1 139 ? -16.099 -41.545 68.031 1.00 187.78 ? 152 PRO A CG 1 ATOM 768 C CD . PRO A 1 139 ? -15.681 -41.692 69.469 1.00 190.51 ? 152 PRO A CD 1 ATOM 769 N N . PHE A 1 140 ? -13.305 -38.450 67.004 1.00 199.49 ? 153 PHE A N 1 ATOM 770 C CA . PHE A 1 140 ? -13.503 -37.124 66.420 1.00 203.38 ? 153 PHE A CA 1 ATOM 771 C C . PHE A 1 140 ? -12.794 -36.966 65.070 1.00 203.88 ? 153 PHE A C 1 ATOM 772 O O . PHE A 1 140 ? -11.820 -37.667 64.778 1.00 205.36 ? 153 PHE A O 1 ATOM 773 C CB . PHE A 1 140 ? -13.094 -36.013 67.399 1.00 201.69 ? 153 PHE A CB 1 ATOM 774 C CG . PHE A 1 140 ? -11.753 -35.392 67.102 1.00 199.24 ? 153 PHE A CG 1 ATOM 775 C CD1 . PHE A 1 140 ? -11.631 -34.021 66.961 1.00 197.05 ? 153 PHE A CD1 1 ATOM 776 C CD2 . PHE A 1 140 ? -10.614 -36.168 66.996 1.00 199.80 ? 153 PHE A CD2 1 ATOM 777 C CE1 . PHE A 1 140 ? -10.402 -33.441 66.699 1.00 191.88 ? 153 PHE A CE1 1 ATOM 778 C CE2 . PHE A 1 140 ? -9.386 -35.590 66.731 1.00 194.44 ? 153 PHE A CE2 1 ATOM 779 C CZ . PHE A 1 140 ? -9.281 -34.228 66.585 1.00 189.55 ? 153 PHE A CZ 1 ATOM 780 N N . ASN A 1 141 ? -13.297 -36.054 64.245 1.00 201.01 ? 154 ASN A N 1 ATOM 781 C CA . ASN A 1 141 ? -12.675 -35.771 62.956 1.00 199.37 ? 154 ASN A CA 1 ATOM 782 C C . ASN A 1 141 ? -12.406 -34.276 62.785 1.00 188.36 ? 154 ASN A C 1 ATOM 783 O O . ASN A 1 141 ? -13.217 -33.437 63.182 1.00 185.24 ? 154 ASN A O 1 ATOM 784 C CB . ASN A 1 141 ? -13.496 -36.357 61.790 1.00 209.04 ? 154 ASN A CB 1 ATOM 785 C CG . ASN A 1 141 ? -14.451 -35.350 61.157 1.00 214.08 ? 154 ASN A CG 1 ATOM 786 O OD1 . ASN A 1 141 ? -14.982 -34.464 61.827 1.00 217.96 ? 154 ASN A OD1 1 ATOM 787 N ND2 . ASN A 1 141 ? -14.681 -35.496 59.854 1.00 213.33 ? 154 ASN A ND2 1 ATOM 788 N N . MET A 1 142 ? -11.257 -33.950 62.202 1.00 180.89 ? 155 MET A N 1 ATOM 789 C CA . MET A 1 142 ? -10.810 -32.565 62.119 1.00 169.85 ? 155 MET A CA 1 ATOM 790 C C . MET A 1 142 ? -11.733 -31.679 61.284 1.00 173.07 ? 155 MET A C 1 ATOM 791 O O . MET A 1 142 ? -11.686 -30.459 61.412 1.00 173.56 ? 155 MET A O 1 ATOM 792 C CB . MET A 1 142 ? -9.375 -32.490 61.606 1.00 158.87 ? 155 MET A CB 1 ATOM 793 N N . LEU A 1 143 ? -12.569 -32.274 60.434 1.00 173.12 ? 156 LEU A N 1 ATOM 794 C CA . LEU A 1 143 ? -13.531 -31.476 59.676 1.00 170.87 ? 156 LEU A CA 1 ATOM 795 C C . LEU A 1 143 ? -14.547 -30.879 60.638 1.00 167.89 ? 156 LEU A C 1 ATOM 796 O O . LEU A 1 143 ? -14.799 -29.668 60.614 1.00 164.80 ? 156 LEU A O 1 ATOM 797 C CB . LEU A 1 143 ? -14.235 -32.300 58.592 1.00 176.46 ? 156 LEU A CB 1 ATOM 798 C CG . LEU A 1 143 ? -15.059 -31.588 57.498 1.00 174.13 ? 156 LEU A CG 1 ATOM 799 C CD1 . LEU A 1 143 ? -16.428 -31.137 57.989 1.00 178.02 ? 156 LEU A CD1 1 ATOM 800 C CD2 . LEU A 1 143 ? -14.307 -30.422 56.874 1.00 166.16 ? 156 LEU A CD2 1 ATOM 801 N N . GLU A 1 144 ? -15.128 -31.724 61.490 1.00 162.57 ? 157 GLU A N 1 ATOM 802 C CA . GLU A 1 144 ? -16.101 -31.241 62.469 1.00 153.62 ? 157 GLU A CA 1 ATOM 803 C C . GLU A 1 144 ? -15.424 -30.405 63.565 1.00 154.08 ? 157 GLU A C 1 ATOM 804 O O . GLU A 1 144 ? -15.982 -29.403 64.031 1.00 149.32 ? 157 GLU A O 1 ATOM 805 C CB . GLU A 1 144 ? -16.928 -32.388 63.047 1.00 142.26 ? 157 GLU A CB 1 ATOM 806 C CG . GLU A 1 144 ? -17.655 -32.036 64.315 1.00 144.40 ? 157 GLU A CG 1 ATOM 807 C CD . GLU A 1 144 ? -16.723 -32.038 65.498 1.00 160.30 ? 157 GLU A CD 1 ATOM 808 O OE1 . GLU A 1 144 ? -15.881 -32.955 65.562 1.00 164.47 ? 157 GLU A OE1 1 ATOM 809 O OE2 . GLU A 1 144 ? -16.808 -31.120 66.348 1.00 170.51 ? 157 GLU A OE2 1 ATOM 810 N N . PHE A 1 145 ? -14.219 -30.815 63.962 1.00 152.46 ? 158 PHE A N 1 ATOM 811 C CA . PHE A 1 145 ? -13.411 -30.038 64.898 1.00 146.82 ? 158 PHE A CA 1 ATOM 812 C C . PHE A 1 145 ? -13.290 -28.576 64.446 1.00 150.20 ? 158 PHE A C 1 ATOM 813 O O . PHE A 1 145 ? -13.710 -27.661 65.163 1.00 150.84 ? 158 PHE A O 1 ATOM 814 C CB . PHE A 1 145 ? -12.031 -30.671 65.101 1.00 144.75 ? 158 PHE A CB 1 ATOM 815 C CG . PHE A 1 145 ? -11.222 -30.010 66.184 1.00 150.51 ? 158 PHE A CG 1 ATOM 816 C CD1 . PHE A 1 145 ? -11.786 -29.739 67.419 1.00 158.02 ? 158 PHE A CD1 1 ATOM 817 C CD2 . PHE A 1 145 ? -9.900 -29.650 65.970 1.00 144.33 ? 158 PHE A CD2 1 ATOM 818 C CE1 . PHE A 1 145 ? -11.046 -29.118 68.415 1.00 153.56 ? 158 PHE A CE1 1 ATOM 819 C CE2 . PHE A 1 145 ? -9.155 -29.030 66.966 1.00 135.96 ? 158 PHE A CE2 1 ATOM 820 C CZ . PHE A 1 145 ? -9.726 -28.767 68.183 1.00 141.89 ? 158 PHE A CZ 1 ATOM 821 N N . TYR A 1 146 ? -12.700 -28.362 63.268 1.00 150.33 ? 159 TYR A N 1 ATOM 822 C CA . TYR A 1 146 ? -12.640 -27.028 62.669 1.00 145.37 ? 159 TYR A CA 1 ATOM 823 C C . TYR A 1 146 ? -14.016 -26.365 62.693 1.00 140.34 ? 159 TYR A C 1 ATOM 824 O O . TYR A 1 146 ? -14.144 -25.215 63.099 1.00 132.67 ? 159 TYR A O 1 ATOM 825 C CB . TYR A 1 146 ? -12.094 -27.093 61.237 1.00 147.65 ? 159 TYR A CB 1 ATOM 826 C CG . TYR A 1 146 ? -10.580 -27.089 61.156 1.00 147.80 ? 159 TYR A CG 1 ATOM 827 C CD1 . TYR A 1 146 ? -9.818 -26.444 62.116 1.00 142.94 ? 159 TYR A CD1 1 ATOM 828 C CD2 . TYR A 1 146 ? -9.913 -27.726 60.117 1.00 148.91 ? 159 TYR A CD2 1 ATOM 829 C CE1 . TYR A 1 146 ? -8.437 -26.431 62.050 1.00 137.70 ? 159 TYR A CE1 1 ATOM 830 C CE2 . TYR A 1 146 ? -8.523 -27.719 60.043 1.00 143.79 ? 159 TYR A CE2 1 ATOM 831 C CZ . TYR A 1 146 ? -7.793 -27.069 61.018 1.00 139.94 ? 159 TYR A CZ 1 ATOM 832 O OH . TYR A 1 146 ? -6.417 -27.053 60.961 1.00 136.18 ? 159 TYR A OH 1 ATOM 833 N N . ASP A 1 147 ? -15.040 -27.112 62.285 1.00 143.72 ? 160 ASP A N 1 ATOM 834 C CA . ASP A 1 147 ? -16.424 -26.627 62.266 1.00 143.15 ? 160 ASP A CA 1 ATOM 835 C C . ASP A 1 147 ? -16.940 -26.074 63.602 1.00 139.47 ? 160 ASP A C 1 ATOM 836 O O . ASP A 1 147 ? -17.460 -24.959 63.658 1.00 135.16 ? 160 ASP A O 1 ATOM 837 C CB . ASP A 1 147 ? -17.362 -27.734 61.778 1.00 145.31 ? 160 ASP A CB 1 ATOM 838 C CG . ASP A 1 147 ? -18.744 -27.213 61.431 1.00 150.12 ? 160 ASP A CG 1 ATOM 839 O OD1 . ASP A 1 147 ? -18.853 -26.046 60.989 1.00 150.75 ? 160 ASP A OD1 1 ATOM 840 O OD2 . ASP A 1 147 ? -19.725 -27.969 61.595 1.00 153.99 ? 160 ASP A OD2 1 ATOM 841 N N . ARG A 1 148 ? -16.826 -26.867 64.663 1.00 137.60 ? 161 ARG A N 1 ATOM 842 C CA . ARG A 1 148 ? -17.268 -26.431 65.985 1.00 140.20 ? 161 ARG A CA 1 ATOM 843 C C . ARG A 1 148 ? -16.288 -25.496 66.743 1.00 150.46 ? 161 ARG A C 1 ATOM 844 O O . ARG A 1 148 ? -16.692 -24.458 67.275 1.00 150.83 ? 161 ARG A O 1 ATOM 845 C CB . ARG A 1 148 ? -17.649 -27.657 66.847 1.00 147.37 ? 161 ARG A CB 1 ATOM 846 N N . ALA A 1 149 ? -15.013 -25.879 66.788 1.00 143.27 ? 162 ALA A N 1 ATOM 847 C CA . ALA A 1 149 ? -14.003 -25.166 67.566 1.00 137.23 ? 162 ALA A CA 1 ATOM 848 C C . ALA A 1 149 ? -13.467 -23.923 66.830 1.00 135.93 ? 162 ALA A C 1 ATOM 849 O O . ALA A 1 149 ? -12.983 -22.957 67.450 1.00 118.88 ? 162 ALA A O 1 ATOM 850 C CB . ALA A 1 149 ? -12.883 -26.104 67.939 1.00 129.98 ? 162 ALA A CB 1 ATOM 851 N N . GLY A 1 150 ? -13.536 -23.965 65.504 1.00 144.34 ? 163 GLY A N 1 ATOM 852 C CA . GLY A 1 150 ? -13.164 -22.815 64.705 1.00 152.13 ? 163 GLY A CA 1 ATOM 853 C C . GLY A 1 150 ? -13.990 -21.596 65.073 1.00 155.17 ? 163 GLY A C 1 ATOM 854 O O . GLY A 1 150 ? -15.089 -21.739 65.602 1.00 158.37 ? 163 GLY A O 1 ATOM 855 N N . HIS A 1 151 ? -13.462 -20.402 64.797 1.00 148.18 ? 164 HIS A N 1 ATOM 856 C CA . HIS A 1 151 ? -14.120 -19.159 65.193 1.00 141.08 ? 164 HIS A CA 1 ATOM 857 C C . HIS A 1 151 ? -15.449 -18.996 64.469 1.00 147.97 ? 164 HIS A C 1 ATOM 858 O O . HIS A 1 151 ? -15.650 -19.555 63.393 1.00 152.63 ? 164 HIS A O 1 ATOM 859 C CB . HIS A 1 151 ? -13.218 -17.964 64.915 1.00 133.36 ? 164 HIS A CB 1 ATOM 860 C CG . HIS A 1 151 ? -12.123 -17.774 65.922 1.00 130.30 ? 164 HIS A CG 1 ATOM 861 N ND1 . HIS A 1 151 ? -12.287 -17.012 67.061 1.00 127.82 ? 164 HIS A ND1 1 ATOM 862 C CD2 . HIS A 1 151 ? -10.841 -18.215 65.944 1.00 123.68 ? 164 HIS A CD2 1 ATOM 863 C CE1 . HIS A 1 151 ? -11.160 -17.005 67.751 1.00 124.01 ? 164 HIS A CE1 1 ATOM 864 N NE2 . HIS A 1 151 ? -10.268 -17.726 67.094 1.00 125.48 ? 164 HIS A NE2 1 ATOM 865 N N . ASP A 1 152 ? -16.363 -18.240 65.067 1.00 148.79 ? 165 ASP A N 1 ATOM 866 C CA . ASP A 1 152 ? -17.739 -18.198 64.577 1.00 150.32 ? 165 ASP A CA 1 ATOM 867 C C . ASP A 1 152 ? -18.116 -16.799 64.118 1.00 149.31 ? 165 ASP A C 1 ATOM 868 O O . ASP A 1 152 ? -18.102 -15.858 64.910 1.00 152.04 ? 165 ASP A O 1 ATOM 869 C CB . ASP A 1 152 ? -18.703 -18.658 65.673 1.00 154.36 ? 165 ASP A CB 1 ATOM 870 C CG . ASP A 1 152 ? -20.077 -19.005 65.136 1.00 159.20 ? 165 ASP A CG 1 ATOM 871 O OD1 . ASP A 1 152 ? -20.275 -18.886 63.909 1.00 162.90 ? 165 ASP A OD1 1 ATOM 872 O OD2 . ASP A 1 152 ? -20.961 -19.383 65.938 1.00 157.09 ? 165 ASP A OD2 1 ATOM 873 N N . ILE A 1 153 ? -18.471 -16.657 62.846 1.00 145.26 ? 166 ILE A N 1 ATOM 874 C CA . ILE A 1 153 ? -18.742 -15.326 62.305 1.00 137.80 ? 166 ILE A CA 1 ATOM 875 C C . ILE A 1 153 ? -19.961 -14.683 62.942 1.00 132.47 ? 166 ILE A C 1 ATOM 876 O O . ILE A 1 153 ? -20.139 -13.475 62.860 1.00 132.57 ? 166 ILE A O 1 ATOM 877 C CB . ILE A 1 153 ? -18.902 -15.311 60.765 1.00 133.51 ? 166 ILE A CB 1 ATOM 878 C CG1 . ILE A 1 153 ? -18.626 -13.901 60.228 1.00 122.64 ? 166 ILE A CG1 1 ATOM 879 C CG2 . ILE A 1 153 ? -20.283 -15.783 60.356 1.00 101.79 ? 166 ILE A CG2 1 ATOM 880 C CD1 . ILE A 1 153 ? -18.765 -13.785 58.744 1.00 121.04 ? 166 ILE A CD1 1 ATOM 881 N N . ARG A 1 154 ? -20.806 -15.491 63.564 1.00 132.93 ? 167 ARG A N 1 ATOM 882 C CA . ARG A 1 154 ? -21.931 -14.950 64.302 1.00 143.09 ? 167 ARG A CA 1 ATOM 883 C C . ARG A 1 154 ? -21.350 -14.127 65.440 1.00 151.87 ? 167 ARG A C 1 ATOM 884 O O . ARG A 1 154 ? -21.808 -13.013 65.716 1.00 158.08 ? 167 ARG A O 1 ATOM 885 C CB . ARG A 1 154 ? -22.823 -16.074 64.831 1.00 145.78 ? 167 ARG A CB 1 ATOM 886 N N . GLU A 1 155 ? -20.324 -14.678 66.085 1.00 147.58 ? 168 GLU A N 1 ATOM 887 C CA . GLU A 1 155 ? -19.650 -13.978 67.167 1.00 140.21 ? 168 GLU A CA 1 ATOM 888 C C . GLU A 1 155 ? -18.829 -12.827 66.612 1.00 131.20 ? 168 GLU A C 1 ATOM 889 O O . GLU A 1 155 ? -18.987 -11.690 67.040 1.00 134.18 ? 168 GLU A O 1 ATOM 890 C CB . GLU A 1 155 ? -18.723 -14.910 67.960 1.00 140.73 ? 168 GLU A CB 1 ATOM 891 C CG . GLU A 1 155 ? -19.357 -16.145 68.551 1.00 148.83 ? 168 GLU A CG 1 ATOM 892 C CD . GLU A 1 155 ? -18.704 -16.527 69.867 1.00 158.98 ? 168 GLU A CD 1 ATOM 893 O OE1 . GLU A 1 155 ? -18.034 -17.583 69.950 1.00 157.73 ? 168 GLU A OE1 1 ATOM 894 O OE2 . GLU A 1 155 ? -18.861 -15.752 70.830 1.00 169.45 ? 168 GLU A OE2 1 ATOM 895 N N . MET A 1 156 ? -17.959 -13.121 65.649 1.00 120.50 ? 169 MET A N 1 ATOM 896 C CA . MET A 1 156 ? -16.902 -12.181 65.282 1.00 118.34 ? 169 MET A CA 1 ATOM 897 C C . MET A 1 156 ? -17.446 -10.861 64.755 1.00 125.95 ? 169 MET A C 1 ATOM 898 O O . MET A 1 156 ? -16.907 -9.786 65.052 1.00 127.06 ? 169 MET A O 1 ATOM 899 C CB . MET A 1 156 ? -15.922 -12.798 64.271 1.00 111.48 ? 169 MET A CB 1 ATOM 900 C CG . MET A 1 156 ? -14.733 -13.525 64.893 1.00 106.34 ? 169 MET A CG 1 ATOM 901 S SD . MET A 1 156 ? -13.591 -14.293 63.709 1.00 113.43 ? 169 MET A SD 1 ATOM 902 C CE . MET A 1 156 ? -14.648 -15.471 62.886 1.00 112.31 ? 169 MET A CE 1 ATOM 903 N N . LEU A 1 157 ? -18.551 -10.937 64.024 1.00 128.24 ? 170 LEU A N 1 ATOM 904 C CA . LEU A 1 157 ? -18.983 -9.815 63.206 1.00 126.35 ? 170 LEU A CA 1 ATOM 905 C C . LEU A 1 157 ? -19.904 -8.905 64.004 1.00 115.51 ? 170 LEU A C 1 ATOM 906 O O . LEU A 1 157 ? -21.063 -9.233 64.240 1.00 110.28 ? 170 LEU A O 1 ATOM 907 C CB . LEU A 1 157 ? -19.720 -10.365 61.968 1.00 127.76 ? 170 LEU A CB 1 ATOM 908 C CG . LEU A 1 157 ? -20.456 -9.454 60.980 1.00 116.99 ? 170 LEU A CG 1 ATOM 909 C CD1 . LEU A 1 157 ? -19.507 -8.417 60.333 1.00 107.86 ? 170 LEU A CD1 1 ATOM 910 C CD2 . LEU A 1 157 ? -21.156 -10.319 59.936 1.00 106.44 ? 170 LEU A CD2 1 ATOM 911 N N . LEU A 1 158 ? -19.390 -7.741 64.385 1.00 111.28 ? 171 LEU A N 1 ATOM 912 C CA . LEU A 1 158 ? -20.183 -6.795 65.149 1.00 114.70 ? 171 LEU A CA 1 ATOM 913 C C . LEU A 1 158 ? -21.053 -5.964 64.218 1.00 120.23 ? 171 LEU A C 1 ATOM 914 O O . LEU A 1 158 ? -22.155 -5.582 64.585 1.00 134.67 ? 171 LEU A O 1 ATOM 915 C CB . LEU A 1 158 ? -19.316 -5.893 66.043 1.00 111.52 ? 171 LEU A CB 1 ATOM 916 C CG . LEU A 1 158 ? -18.169 -6.516 66.853 1.00 109.12 ? 171 LEU A CG 1 ATOM 917 C CD1 . LEU A 1 158 ? -17.553 -5.478 67.753 1.00 103.80 ? 171 LEU A CD1 1 ATOM 918 C CD2 . LEU A 1 158 ? -18.605 -7.690 67.678 1.00 111.93 ? 171 LEU A CD2 1 ATOM 919 N N . SER A 1 159 ? -20.542 -5.621 63.040 1.00 110.61 ? 172 SER A N 1 ATOM 920 C CA . SER A 1 159 ? -21.400 -4.980 62.051 1.00 110.58 ? 172 SER A CA 1 ATOM 921 C C . SER A 1 159 ? -20.952 -5.142 60.588 1.00 120.34 ? 172 SER A C 1 ATOM 922 O O . SER A 1 159 ? -19.767 -5.174 60.280 1.00 111.65 ? 172 SER A O 1 ATOM 923 C CB . SER A 1 159 ? -21.573 -3.511 62.388 1.00 103.91 ? 172 SER A CB 1 ATOM 924 O OG . SER A 1 159 ? -20.708 -2.740 61.589 1.00 113.16 ? 172 SER A OG 1 ATOM 925 N N . CYS A 1 160 ? -21.913 -5.224 59.678 1.00 136.53 ? 173 CYS A N 1 ATOM 926 C CA . CYS A 1 160 ? -21.579 -5.397 58.274 1.00 141.92 ? 173 CYS A CA 1 ATOM 927 C C . CYS A 1 160 ? -22.484 -4.582 57.373 1.00 148.93 ? 173 CYS A C 1 ATOM 928 O O . CYS A 1 160 ? -23.706 -4.677 57.448 1.00 153.93 ? 173 CYS A O 1 ATOM 929 C CB . CYS A 1 160 ? -21.639 -6.872 57.882 1.00 142.90 ? 173 CYS A CB 1 ATOM 930 S SG . CYS A 1 160 ? -21.066 -7.171 56.209 1.00 153.01 ? 173 CYS A SG 1 ATOM 931 N N . PHE A 1 161 ? -21.864 -3.793 56.504 1.00 144.88 ? 174 PHE A N 1 ATOM 932 C CA . PHE A 1 161 ? -22.596 -2.987 55.540 1.00 140.46 ? 174 PHE A CA 1 ATOM 933 C C . PHE A 1 161 ? -21.969 -3.074 54.164 1.00 139.62 ? 174 PHE A C 1 ATOM 934 O O . PHE A 1 161 ? -20.772 -2.878 54.001 1.00 132.76 ? 174 PHE A O 1 ATOM 935 C CB . PHE A 1 161 ? -22.635 -1.528 55.977 1.00 132.66 ? 174 PHE A CB 1 ATOM 936 C CG . PHE A 1 161 ? -23.700 -1.227 56.976 1.00 144.61 ? 174 PHE A CG 1 ATOM 937 C CD1 . PHE A 1 161 ? -24.903 -0.678 56.575 1.00 157.33 ? 174 PHE A CD1 1 ATOM 938 C CD2 . PHE A 1 161 ? -23.505 -1.487 58.322 1.00 152.09 ? 174 PHE A CD2 1 ATOM 939 C CE1 . PHE A 1 161 ? -25.899 -0.387 57.503 1.00 165.08 ? 174 PHE A CE1 1 ATOM 940 C CE2 . PHE A 1 161 ? -24.494 -1.203 59.260 1.00 158.05 ? 174 PHE A CE2 1 ATOM 941 C CZ . PHE A 1 161 ? -25.692 -0.652 58.848 1.00 164.05 ? 174 PHE A CZ 1 ATOM 942 N N . PHE A 1 162 ? -22.789 -3.374 53.169 1.00 145.18 ? 175 PHE A N 1 ATOM 943 C CA . PHE A 1 162 ? -22.363 -3.220 51.790 1.00 141.03 ? 175 PHE A CA 1 ATOM 944 C C . PHE A 1 162 ? -23.191 -2.107 51.195 1.00 137.71 ? 175 PHE A C 1 ATOM 945 O O . PHE A 1 162 ? -24.408 -2.117 51.302 1.00 142.06 ? 175 PHE A O 1 ATOM 946 C CB . PHE A 1 162 ? -22.556 -4.507 50.982 1.00 139.78 ? 175 PHE A CB 1 ATOM 947 C CG . PHE A 1 162 ? -22.113 -4.390 49.555 1.00 134.09 ? 175 PHE A CG 1 ATOM 948 C CD1 . PHE A 1 162 ? -20.831 -4.755 49.183 1.00 130.74 ? 175 PHE A CD1 1 ATOM 949 C CD2 . PHE A 1 162 ? -22.969 -3.887 48.592 1.00 132.92 ? 175 PHE A CD2 1 ATOM 950 C CE1 . PHE A 1 162 ? -20.415 -4.637 47.872 1.00 128.12 ? 175 PHE A CE1 1 ATOM 951 C CE2 . PHE A 1 162 ? -22.563 -3.764 47.290 1.00 135.06 ? 175 PHE A CE2 1 ATOM 952 C CZ . PHE A 1 162 ? -21.279 -4.138 46.925 1.00 132.86 ? 175 PHE A CZ 1 ATOM 953 N N . ARG A 1 163 ? -22.523 -1.133 50.595 1.00 129.39 ? 176 ARG A N 1 ATOM 954 C CA . ARG A 1 163 ? -23.202 -0.074 49.883 1.00 123.19 ? 176 ARG A CA 1 ATOM 955 C C . ARG A 1 163 ? -24.383 0.463 50.698 1.00 124.75 ? 176 ARG A C 1 ATOM 956 O O . ARG A 1 163 ? -25.447 0.759 50.156 1.00 128.39 ? 176 ARG A O 1 ATOM 957 C CB . ARG A 1 163 ? -23.643 -0.584 48.509 1.00 123.11 ? 176 ARG A CB 1 ATOM 958 C CG . ARG A 1 163 ? -23.824 0.514 47.481 1.00 133.47 ? 176 ARG A CG 1 ATOM 959 C CD . ARG A 1 163 ? -23.431 0.047 46.097 1.00 137.63 ? 176 ARG A CD 1 ATOM 960 N NE . ARG A 1 163 ? -24.137 -1.164 45.681 1.00 142.45 ? 176 ARG A NE 1 ATOM 961 C CZ . ARG A 1 163 ? -25.322 -1.174 45.076 1.00 140.43 ? 176 ARG A CZ 1 ATOM 962 N NH1 . ARG A 1 163 ? -25.960 -0.037 44.834 1.00 145.70 ? 176 ARG A NH1 1 ATOM 963 N NH2 . ARG A 1 163 ? -25.871 -2.324 44.718 1.00 134.20 ? 176 ARG A NH2 1 ATOM 964 N N . GLY A 1 164 ? -24.200 0.569 52.009 1.00 124.96 ? 177 GLY A N 1 ATOM 965 C CA . GLY A 1 164 ? -25.199 1.206 52.857 1.00 133.48 ? 177 GLY A CA 1 ATOM 966 C C . GLY A 1 164 ? -26.413 0.376 53.256 1.00 139.38 ? 177 GLY A C 1 ATOM 967 O O . GLY A 1 164 ? -27.231 0.810 54.067 1.00 133.23 ? 177 GLY A O 1 ATOM 968 N N . GLU A 1 165 ? -26.541 -0.813 52.679 1.00 148.20 ? 178 GLU A N 1 ATOM 969 C CA . GLU A 1 165 ? -27.569 -1.761 53.099 1.00 150.18 ? 178 GLU A CA 1 ATOM 970 C C . GLU A 1 165 ? -26.986 -2.745 54.114 1.00 140.28 ? 178 GLU A C 1 ATOM 971 O O . GLU A 1 165 ? -26.037 -3.476 53.817 1.00 131.58 ? 178 GLU A O 1 ATOM 972 C CB . GLU A 1 165 ? -28.147 -2.501 51.893 1.00 152.72 ? 178 GLU A CB 1 ATOM 973 N N . GLN A 1 166 ? -27.542 -2.750 55.320 1.00 136.34 ? 179 GLN A N 1 ATOM 974 C CA . GLN A 1 166 ? -27.021 -3.620 56.364 1.00 135.32 ? 179 GLN A CA 1 ATOM 975 C C . GLN A 1 166 ? -27.015 -5.067 55.912 1.00 133.81 ? 179 GLN A C 1 ATOM 976 O O . GLN A 1 166 ? -28.049 -5.595 55.538 1.00 147.60 ? 179 GLN A O 1 ATOM 977 C CB . GLN A 1 166 ? -27.869 -3.487 57.629 1.00 141.91 ? 179 GLN A CB 1 ATOM 978 C CG . GLN A 1 166 ? -27.500 -4.446 58.752 1.00 142.99 ? 179 GLN A CG 1 ATOM 979 C CD . GLN A 1 166 ? -27.665 -3.808 60.126 1.00 147.57 ? 179 GLN A CD 1 ATOM 980 O OE1 . GLN A 1 166 ? -28.786 -3.495 60.539 1.00 147.52 ? 179 GLN A OE1 1 ATOM 981 N NE2 . GLN A 1 166 ? -26.544 -3.601 60.836 1.00 145.00 ? 179 GLN A NE2 1 ATOM 982 N N . CYS A 1 167 ? -25.849 -5.702 55.946 1.00 125.08 ? 180 CYS A N 1 ATOM 983 C CA . CYS A 1 167 ? -25.740 -7.137 55.694 1.00 125.78 ? 180 CYS A CA 1 ATOM 984 C C . CYS A 1 167 ? -25.689 -7.896 57.022 1.00 132.93 ? 180 CYS A C 1 ATOM 985 O O . CYS A 1 167 ? -25.939 -7.323 58.077 1.00 140.21 ? 180 CYS A O 1 ATOM 986 C CB . CYS A 1 167 ? -24.521 -7.456 54.832 1.00 119.50 ? 180 CYS A CB 1 ATOM 987 S SG . CYS A 1 167 ? -22.954 -6.877 55.515 1.00 249.35 ? 180 CYS A SG 1 ATOM 988 N N . SER A 1 168 ? -25.398 -9.190 56.969 1.00 134.23 ? 181 SER A N 1 ATOM 989 C CA . SER A 1 168 ? -25.322 -9.996 58.181 1.00 141.84 ? 181 SER A CA 1 ATOM 990 C C . SER A 1 168 ? -24.658 -11.360 57.928 1.00 143.34 ? 181 SER A C 1 ATOM 991 O O . SER A 1 168 ? -24.361 -11.708 56.785 1.00 141.55 ? 181 SER A O 1 ATOM 992 C CB . SER A 1 168 ? -26.729 -10.167 58.758 1.00 153.78 ? 181 SER A CB 1 ATOM 993 O OG . SER A 1 168 ? -27.647 -10.574 57.755 1.00 160.47 ? 181 SER A OG 1 ATOM 994 N N . PRO A 1 169 ? -24.448 -12.152 58.997 1.00 144.61 ? 182 PRO A N 1 ATOM 995 C CA . PRO A 1 169 ? -23.768 -13.439 58.836 1.00 145.74 ? 182 PRO A CA 1 ATOM 996 C C . PRO A 1 169 ? -24.346 -14.317 57.731 1.00 167.04 ? 182 PRO A C 1 ATOM 997 O O . PRO A 1 169 ? -23.639 -15.179 57.211 1.00 179.45 ? 182 PRO A O 1 ATOM 998 C CB . PRO A 1 169 ? -23.964 -14.091 60.206 1.00 130.83 ? 182 PRO A CB 1 ATOM 999 C CG . PRO A 1 169 ? -23.880 -12.947 61.138 1.00 131.42 ? 182 PRO A CG 1 ATOM 1000 C CD . PRO A 1 169 ? -24.581 -11.803 60.425 1.00 141.00 ? 182 PRO A CD 1 ATOM 1001 N N . GLU A 1 170 ? -25.602 -14.105 57.365 1.00 170.72 ? 183 GLU A N 1 ATOM 1002 C CA . GLU A 1 170 ? -26.197 -14.889 56.291 1.00 175.90 ? 183 GLU A CA 1 ATOM 1003 C C . GLU A 1 170 ? -25.393 -14.796 54.984 1.00 169.27 ? 183 GLU A C 1 ATOM 1004 O O . GLU A 1 170 ? -25.423 -15.710 54.164 1.00 170.02 ? 183 GLU A O 1 ATOM 1005 C CB . GLU A 1 170 ? -27.650 -14.455 56.071 1.00 187.89 ? 183 GLU A CB 1 ATOM 1006 C CG . GLU A 1 170 ? -28.112 -13.361 57.038 1.00 194.95 ? 183 GLU A CG 1 ATOM 1007 C CD . GLU A 1 170 ? -29.205 -13.811 58.011 1.00 203.58 ? 183 GLU A CD 1 ATOM 1008 O OE1 . GLU A 1 170 ? -29.053 -13.556 59.231 1.00 202.57 ? 183 GLU A OE1 1 ATOM 1009 O OE2 . GLU A 1 170 ? -30.218 -14.398 57.557 1.00 207.36 ? 183 GLU A OE2 1 ATOM 1010 N N . ASP A 1 171 ? -24.643 -13.710 54.817 1.00 163.29 ? 184 ASP A N 1 ATOM 1011 C CA . ASP A 1 171 ? -24.072 -13.363 53.513 1.00 161.59 ? 184 ASP A CA 1 ATOM 1012 C C . ASP A 1 171 ? -22.641 -13.876 53.249 1.00 158.92 ? 184 ASP A C 1 ATOM 1013 O O . ASP A 1 171 ? -22.072 -13.618 52.182 1.00 153.97 ? 184 ASP A O 1 ATOM 1014 C CB . ASP A 1 171 ? -24.161 -11.843 53.279 1.00 163.13 ? 184 ASP A CB 1 ATOM 1015 C CG . ASP A 1 171 ? -25.585 -11.295 53.459 1.00 167.83 ? 184 ASP A CG 1 ATOM 1016 O OD1 . ASP A 1 171 ? -26.375 -11.302 52.488 1.00 165.46 ? 184 ASP A OD1 1 ATOM 1017 O OD2 . ASP A 1 171 ? -25.913 -10.859 54.581 1.00 171.53 ? 184 ASP A OD2 1 ATOM 1018 N N . PHE A 1 172 ? -22.087 -14.625 54.205 1.00 159.72 ? 185 PHE A N 1 ATOM 1019 C CA . PHE A 1 172 ? -20.731 -15.182 54.102 1.00 147.79 ? 185 PHE A CA 1 ATOM 1020 C C . PHE A 1 172 ? -20.732 -16.695 53.999 1.00 147.71 ? 185 PHE A C 1 ATOM 1021 O O . PHE A 1 172 ? -20.996 -17.363 54.996 1.00 154.21 ? 185 PHE A O 1 ATOM 1022 C CB . PHE A 1 172 ? -19.952 -14.860 55.372 1.00 138.55 ? 185 PHE A CB 1 ATOM 1023 C CG . PHE A 1 172 ? -19.793 -13.403 55.632 1.00 133.72 ? 185 PHE A CG 1 ATOM 1024 C CD1 . PHE A 1 172 ? -18.613 -12.756 55.296 1.00 123.90 ? 185 PHE A CD1 1 ATOM 1025 C CD2 . PHE A 1 172 ? -20.817 -12.678 56.215 1.00 134.06 ? 185 PHE A CD2 1 ATOM 1026 C CE1 . PHE A 1 172 ? -18.457 -11.421 55.534 1.00 121.54 ? 185 PHE A CE1 1 ATOM 1027 C CE2 . PHE A 1 172 ? -20.666 -11.330 56.457 1.00 134.81 ? 185 PHE A CE2 1 ATOM 1028 C CZ . PHE A 1 172 ? -19.483 -10.697 56.118 1.00 127.12 ? 185 PHE A CZ 1 ATOM 1029 N N . LYS A 1 173 ? -20.398 -17.255 52.839 1.00 140.33 ? 186 LYS A N 1 ATOM 1030 C CA . LYS A 1 173 ? -20.298 -18.713 52.769 1.00 137.88 ? 186 LYS A CA 1 ATOM 1031 C C . LYS A 1 173 ? -19.017 -19.151 53.453 1.00 144.18 ? 186 LYS A C 1 ATOM 1032 O O . LYS A 1 173 ? -18.025 -18.426 53.462 1.00 139.29 ? 186 LYS A O 1 ATOM 1033 C CB . LYS A 1 173 ? -20.372 -19.244 51.332 1.00 126.55 ? 186 LYS A CB 1 ATOM 1034 N N . VAL A 1 174 ? -19.052 -20.332 54.054 1.00 156.42 ? 187 VAL A N 1 ATOM 1035 C CA . VAL A 1 174 ? -17.899 -20.844 54.778 1.00 149.54 ? 187 VAL A CA 1 ATOM 1036 C C . VAL A 1 174 ? -16.962 -21.622 53.851 1.00 155.93 ? 187 VAL A C 1 ATOM 1037 O O . VAL A 1 174 ? -17.389 -22.516 53.110 1.00 163.82 ? 187 VAL A O 1 ATOM 1038 C CB . VAL A 1 174 ? -18.336 -21.709 55.978 1.00 131.51 ? 187 VAL A CB 1 ATOM 1039 C CG1 . VAL A 1 174 ? -17.165 -22.524 56.509 1.00 124.18 ? 187 VAL A CG1 1 ATOM 1040 C CG2 . VAL A 1 174 ? -18.931 -20.826 57.056 1.00 119.87 ? 187 VAL A CG2 1 ATOM 1041 N N . VAL A 1 175 ? -15.689 -21.251 53.874 1.00 148.37 ? 188 VAL A N 1 ATOM 1042 C CA . VAL A 1 175 ? -14.680 -21.966 53.115 1.00 147.93 ? 188 VAL A CA 1 ATOM 1043 C C . VAL A 1 175 ? -13.570 -22.390 54.055 1.00 143.97 ? 188 VAL A C 1 ATOM 1044 O O . VAL A 1 175 ? -13.049 -21.587 54.838 1.00 136.96 ? 188 VAL A O 1 ATOM 1045 C CB . VAL A 1 175 ? -14.087 -21.111 51.992 1.00 148.44 ? 188 VAL A CB 1 ATOM 1046 C CG1 . VAL A 1 175 ? -13.765 -19.719 52.513 1.00 148.24 ? 188 VAL A CG1 1 ATOM 1047 C CG2 . VAL A 1 175 ? -12.842 -21.792 51.403 1.00 146.26 ? 188 VAL A CG2 1 ATOM 1048 N N . PHE A 1 176 ? -13.214 -23.663 53.980 1.00 147.29 ? 189 PHE A N 1 ATOM 1049 C CA . PHE A 1 176 ? -12.136 -24.169 54.801 1.00 142.26 ? 189 PHE A CA 1 ATOM 1050 C C . PHE A 1 176 ? -10.812 -23.896 54.130 1.00 133.45 ? 189 PHE A C 1 ATOM 1051 O O . PHE A 1 176 ? -10.641 -24.141 52.943 1.00 129.25 ? 189 PHE A O 1 ATOM 1052 C CB . PHE A 1 176 ? -12.332 -25.654 55.122 1.00 147.26 ? 189 PHE A CB 1 ATOM 1053 C CG . PHE A 1 176 ? -13.392 -25.897 56.155 1.00 148.77 ? 189 PHE A CG 1 ATOM 1054 C CD1 . PHE A 1 176 ? -13.164 -25.576 57.488 1.00 147.58 ? 189 PHE A CD1 1 ATOM 1055 C CD2 . PHE A 1 176 ? -14.623 -26.402 55.795 1.00 149.88 ? 189 PHE A CD2 1 ATOM 1056 C CE1 . PHE A 1 176 ? -14.137 -25.771 58.444 1.00 148.53 ? 189 PHE A CE1 1 ATOM 1057 C CE2 . PHE A 1 176 ? -15.600 -26.601 56.746 1.00 154.97 ? 189 PHE A CE2 1 ATOM 1058 C CZ . PHE A 1 176 ? -15.356 -26.281 58.074 1.00 154.74 ? 189 PHE A CZ 1 ATOM 1059 N N . THR A 1 177 ? -9.895 -23.329 54.898 1.00 136.38 ? 190 THR A N 1 ATOM 1060 C CA . THR A 1 177 ? -8.557 -23.069 54.418 1.00 135.96 ? 190 THR A CA 1 ATOM 1061 C C . THR A 1 177 ? -7.617 -23.650 55.455 1.00 135.05 ? 190 THR A C 1 ATOM 1062 O O . THR A 1 177 ? -8.056 -24.123 56.509 1.00 133.32 ? 190 THR A O 1 ATOM 1063 C CB . THR A 1 177 ? -8.298 -21.544 54.245 1.00 124.84 ? 190 THR A CB 1 ATOM 1064 O OG1 . THR A 1 177 ? -8.148 -20.922 55.527 1.00 125.04 ? 190 THR A OG1 1 ATOM 1065 C CG2 . THR A 1 177 ? -9.459 -20.888 53.546 1.00 122.97 ? 190 THR A CG2 1 ATOM 1066 N N . ARG A 1 178 ? -6.324 -23.577 55.174 1.00 132.53 ? 191 ARG A N 1 ATOM 1067 C CA . ARG A 1 178 ? -5.328 -24.128 56.069 1.00 130.47 ? 191 ARG A CA 1 ATOM 1068 C C . ARG A 1 178 ? -5.326 -23.370 57.397 1.00 136.66 ? 191 ARG A C 1 ATOM 1069 O O . ARG A 1 178 ? -4.691 -23.784 58.364 1.00 144.12 ? 191 ARG A O 1 ATOM 1070 C CB . ARG A 1 178 ? -3.963 -24.104 55.409 1.00 120.52 ? 191 ARG A CB 1 ATOM 1071 N N . TYR A 1 179 ? -6.044 -22.256 57.445 1.00 132.89 ? 192 TYR A N 1 ATOM 1072 C CA . TYR A 1 179 ? -6.167 -21.525 58.694 1.00 132.39 ? 192 TYR A CA 1 ATOM 1073 C C . TYR A 1 179 ? -7.217 -22.139 59.602 1.00 143.61 ? 192 TYR A C 1 ATOM 1074 O O . TYR A 1 179 ? -7.042 -22.164 60.814 1.00 153.59 ? 192 TYR A O 1 ATOM 1075 C CB . TYR A 1 179 ? -6.468 -20.047 58.451 1.00 132.33 ? 192 TYR A CB 1 ATOM 1076 C CG . TYR A 1 179 ? -5.342 -19.330 57.749 1.00 140.73 ? 192 TYR A CG 1 ATOM 1077 C CD1 . TYR A 1 179 ? -4.559 -18.382 58.411 1.00 138.96 ? 192 TYR A CD1 1 ATOM 1078 C CD2 . TYR A 1 179 ? -5.045 -19.615 56.420 1.00 149.31 ? 192 TYR A CD2 1 ATOM 1079 C CE1 . TYR A 1 179 ? -3.516 -17.726 57.758 1.00 140.96 ? 192 TYR A CE1 1 ATOM 1080 C CE2 . TYR A 1 179 ? -4.005 -18.976 55.758 1.00 151.23 ? 192 TYR A CE2 1 ATOM 1081 C CZ . TYR A 1 179 ? -3.243 -18.035 56.427 1.00 151.23 ? 192 TYR A CZ 1 ATOM 1082 O OH . TYR A 1 179 ? -2.216 -17.419 55.749 1.00 153.88 ? 192 TYR A OH 1 ATOM 1083 N N . GLY A 1 180 ? -8.327 -22.596 59.031 1.00 143.60 ? 193 GLY A N 1 ATOM 1084 C CA . GLY A 1 180 ? -9.427 -23.073 59.851 1.00 143.51 ? 193 GLY A CA 1 ATOM 1085 C C . GLY A 1 180 ? -10.755 -22.808 59.178 1.00 141.12 ? 193 GLY A C 1 ATOM 1086 O O . GLY A 1 180 ? -10.849 -22.757 57.954 1.00 137.05 ? 193 GLY A O 1 ATOM 1087 N N . LYS A 1 181 ? -11.792 -22.658 59.996 1.00 140.85 ? 194 LYS A N 1 ATOM 1088 C CA . LYS A 1 181 ? -13.072 -22.144 59.524 1.00 140.15 ? 194 LYS A CA 1 ATOM 1089 C C . LYS A 1 181 ? -12.883 -20.706 59.030 1.00 146.20 ? 194 LYS A C 1 ATOM 1090 O O . LYS A 1 181 ? -12.394 -19.827 59.764 1.00 145.09 ? 194 LYS A O 1 ATOM 1091 C CB . LYS A 1 181 ? -14.106 -22.179 60.652 1.00 137.95 ? 194 LYS A CB 1 ATOM 1092 C CG . LYS A 1 181 ? -15.551 -22.385 60.205 1.00 138.82 ? 194 LYS A CG 1 ATOM 1093 C CD . LYS A 1 181 ? -16.518 -22.284 61.389 1.00 140.17 ? 194 LYS A CD 1 ATOM 1094 C CE . LYS A 1 181 ? -17.940 -22.657 60.981 1.00 145.79 ? 194 LYS A CE 1 ATOM 1095 N NZ . LYS A 1 181 ? -18.880 -22.750 62.138 1.00 148.18 ? 194 LYS A NZ 1 ATOM 1096 N N . CYS A 1 182 ? -13.292 -20.465 57.788 1.00 148.09 ? 195 CYS A N 1 ATOM 1097 C CA . CYS A 1 182 ? -13.089 -19.168 57.154 1.00 140.19 ? 195 CYS A CA 1 ATOM 1098 C C . CYS A 1 182 ? -14.347 -18.731 56.432 1.00 140.73 ? 195 CYS A C 1 ATOM 1099 O O . CYS A 1 182 ? -15.234 -19.538 56.184 1.00 152.70 ? 195 CYS A O 1 ATOM 1100 C CB . CYS A 1 182 ? -11.942 -19.257 56.157 1.00 135.31 ? 195 CYS A CB 1 ATOM 1101 S SG . CYS A 1 182 ? -11.076 -17.715 55.926 1.00 251.48 ? 195 CYS A SG 1 ATOM 1102 N N . TYR A 1 183 ? -14.416 -17.460 56.066 1.00 132.49 ? 196 TYR A N 1 ATOM 1103 C CA . TYR A 1 183 ? -15.658 -16.903 55.535 1.00 131.14 ? 196 TYR A CA 1 ATOM 1104 C C . TYR A 1 183 ? -15.479 -16.032 54.304 1.00 127.23 ? 196 TYR A C 1 ATOM 1105 O O . TYR A 1 183 ? -14.704 -15.081 54.323 1.00 132.93 ? 196 TYR A O 1 ATOM 1106 C CB . TYR A 1 183 ? -16.358 -16.101 56.632 1.00 130.30 ? 196 TYR A CB 1 ATOM 1107 C CG . TYR A 1 183 ? -16.700 -16.944 57.842 1.00 131.37 ? 196 TYR A CG 1 ATOM 1108 C CD1 . TYR A 1 183 ? -17.899 -17.635 57.916 1.00 133.73 ? 196 TYR A CD1 1 ATOM 1109 C CD2 . TYR A 1 183 ? -15.811 -17.072 58.893 1.00 128.50 ? 196 TYR A CD2 1 ATOM 1110 C CE1 . TYR A 1 183 ? -18.206 -18.408 59.010 1.00 135.90 ? 196 TYR A CE1 1 ATOM 1111 C CE2 . TYR A 1 183 ? -16.113 -17.840 59.993 1.00 129.00 ? 196 TYR A CE2 1 ATOM 1112 C CZ . TYR A 1 183 ? -17.313 -18.507 60.049 1.00 134.16 ? 196 TYR A CZ 1 ATOM 1113 O OH . TYR A 1 183 ? -17.624 -19.279 61.147 1.00 139.20 ? 196 TYR A OH 1 ATOM 1114 N N . THR A 1 184 ? -16.219 -16.344 53.245 1.00 125.01 ? 197 THR A N 1 ATOM 1115 C CA . THR A 1 184 ? -16.105 -15.623 51.973 1.00 130.92 ? 197 THR A CA 1 ATOM 1116 C C . THR A 1 184 ? -17.292 -14.717 51.616 1.00 137.83 ? 197 THR A C 1 ATOM 1117 O O . THR A 1 184 ? -18.378 -15.209 51.273 1.00 146.23 ? 197 THR A O 1 ATOM 1118 C CB . THR A 1 184 ? -15.933 -16.622 50.825 1.00 138.02 ? 197 THR A CB 1 ATOM 1119 O OG1 . THR A 1 184 ? -14.754 -17.401 51.052 1.00 140.14 ? 197 THR A OG1 1 ATOM 1120 C CG2 . THR A 1 184 ? -15.820 -15.901 49.506 1.00 139.30 ? 197 THR A CG2 1 ATOM 1121 N N . PHE A 1 185 ? -17.080 -13.400 51.666 1.00 131.35 ? 198 PHE A N 1 ATOM 1122 C CA . PHE A 1 185 ? -18.134 -12.448 51.322 1.00 128.03 ? 198 PHE A CA 1 ATOM 1123 C C . PHE A 1 185 ? -18.238 -12.209 49.829 1.00 139.48 ? 198 PHE A C 1 ATOM 1124 O O . PHE A 1 185 ? -17.231 -12.214 49.117 1.00 138.94 ? 198 PHE A O 1 ATOM 1125 C CB . PHE A 1 185 ? -17.981 -11.110 52.030 1.00 114.17 ? 198 PHE A CB 1 ATOM 1126 C CG . PHE A 1 185 ? -19.070 -10.127 51.679 1.00 124.77 ? 198 PHE A CG 1 ATOM 1127 C CD1 . PHE A 1 185 ? -20.302 -10.169 52.324 1.00 137.09 ? 198 PHE A CD1 1 ATOM 1128 C CD2 . PHE A 1 185 ? -18.876 -9.175 50.694 1.00 119.83 ? 198 PHE A CD2 1 ATOM 1129 C CE1 . PHE A 1 185 ? -21.310 -9.265 51.996 1.00 135.17 ? 198 PHE A CE1 1 ATOM 1130 C CE2 . PHE A 1 185 ? -19.876 -8.276 50.368 1.00 116.93 ? 198 PHE A CE2 1 ATOM 1131 C CZ . PHE A 1 185 ? -21.088 -8.321 51.016 1.00 124.53 ? 198 PHE A CZ 1 ATOM 1132 N N . ASN A 1 186 ? -19.472 -11.976 49.379 1.00 143.76 ? 199 ASN A N 1 ATOM 1133 C CA . ASN A 1 186 ? -19.796 -11.846 47.964 1.00 139.71 ? 199 ASN A CA 1 ATOM 1134 C C . ASN A 1 186 ? -19.403 -13.112 47.216 1.00 146.21 ? 199 ASN A C 1 ATOM 1135 O O . ASN A 1 186 ? -18.715 -13.063 46.198 1.00 144.07 ? 199 ASN A O 1 ATOM 1136 C CB . ASN A 1 186 ? -19.123 -10.625 47.361 1.00 129.98 ? 199 ASN A CB 1 ATOM 1137 C CG . ASN A 1 186 ? -19.832 -10.128 46.139 1.00 129.45 ? 199 ASN A CG 1 ATOM 1138 O OD1 . ASN A 1 186 ? -20.922 -10.580 45.815 1.00 135.20 ? 199 ASN A OD1 1 ATOM 1139 N ND2 . ASN A 1 186 ? -19.223 -9.182 45.454 1.00 125.67 ? 199 ASN A ND2 1 ATOM 1140 N N . ALA A 1 187 ? -19.850 -14.245 47.751 1.00 154.77 ? 200 ALA A N 1 ATOM 1141 C CA . ALA A 1 187 ? -19.521 -15.565 47.225 1.00 161.29 ? 200 ALA A CA 1 ATOM 1142 C C . ALA A 1 187 ? -19.891 -15.794 45.751 1.00 159.25 ? 200 ALA A C 1 ATOM 1143 O O . ALA A 1 187 ? -19.060 -16.262 44.962 1.00 146.66 ? 200 ALA A O 1 ATOM 1144 C CB . ALA A 1 187 ? -20.173 -16.632 48.097 1.00 169.43 ? 200 ALA A CB 1 ATOM 1145 N N . GLY A 1 188 ? -21.137 -15.486 45.392 1.00 166.94 ? 201 GLY A N 1 ATOM 1146 C CA . GLY A 1 188 ? -21.670 -15.837 44.085 1.00 174.04 ? 201 GLY A CA 1 ATOM 1147 C C . GLY A 1 188 ? -21.827 -17.343 43.945 1.00 183.08 ? 201 GLY A C 1 ATOM 1148 O O . GLY A 1 188 ? -21.963 -17.872 42.837 1.00 185.22 ? 201 GLY A O 1 ATOM 1149 N N . GLN A 1 189 ? -21.853 -18.019 45.092 1.00 185.47 ? 202 GLN A N 1 ATOM 1150 C CA . GLN A 1 189 ? -21.779 -19.473 45.187 1.00 183.15 ? 202 GLN A CA 1 ATOM 1151 C C . GLN A 1 189 ? -23.073 -19.925 45.821 1.00 186.12 ? 202 GLN A C 1 ATOM 1152 O O . GLN A 1 189 ? -23.806 -19.106 46.380 1.00 188.06 ? 202 GLN A O 1 ATOM 1153 C CB . GLN A 1 189 ? -20.584 -19.900 46.046 1.00 175.33 ? 202 GLN A CB 1 ATOM 1154 N N . ASP A 1 190 ? -23.361 -21.219 45.719 1.00 187.90 ? 203 ASP A N 1 ATOM 1155 C CA . ASP A 1 190 ? -24.676 -21.730 46.064 1.00 192.28 ? 203 ASP A CA 1 ATOM 1156 C C . ASP A 1 190 ? -25.649 -20.951 45.200 1.00 192.78 ? 203 ASP A C 1 ATOM 1157 O O . ASP A 1 190 ? -26.734 -20.583 45.639 1.00 195.09 ? 203 ASP A O 1 ATOM 1158 C CB . ASP A 1 190 ? -24.997 -21.521 47.549 1.00 193.57 ? 203 ASP A CB 1 ATOM 1159 C CG . ASP A 1 190 ? -24.272 -22.500 48.456 1.00 197.67 ? 203 ASP A CG 1 ATOM 1160 O OD1 . ASP A 1 190 ? -24.194 -23.700 48.105 1.00 201.59 ? 203 ASP A OD1 1 ATOM 1161 O OD2 . ASP A 1 190 ? -23.783 -22.066 49.526 1.00 197.12 ? 203 ASP A OD2 1 ATOM 1162 N N . GLY A 1 191 ? -25.223 -20.664 43.976 1.00 189.09 ? 204 GLY A N 1 ATOM 1163 C CA . GLY A 1 191 ? -26.067 -19.994 43.008 1.00 188.48 ? 204 GLY A CA 1 ATOM 1164 C C . GLY A 1 191 ? -26.728 -18.716 43.491 1.00 185.51 ? 204 GLY A C 1 ATOM 1165 O O . GLY A 1 191 ? -27.832 -18.388 43.049 1.00 190.67 ? 204 GLY A O 1 ATOM 1166 N N . LYS A 1 192 ? -26.072 -18.001 44.403 1.00 177.30 ? 205 LYS A N 1 ATOM 1167 C CA . LYS A 1 192 ? -26.522 -16.667 44.796 1.00 166.89 ? 205 LYS A CA 1 ATOM 1168 C C . LYS A 1 192 ? -25.989 -15.644 43.782 1.00 162.27 ? 205 LYS A C 1 ATOM 1169 O O . LYS A 1 192 ? -25.127 -15.979 42.958 1.00 158.31 ? 205 LYS A O 1 ATOM 1170 C CB . LYS A 1 192 ? -26.064 -16.336 46.226 1.00 154.82 ? 205 LYS A CB 1 ATOM 1171 N N . PRO A 1 193 ? -26.530 -14.410 43.805 1.00 159.42 ? 206 PRO A N 1 ATOM 1172 C CA . PRO A 1 193 ? -26.079 -13.311 42.940 1.00 156.81 ? 206 PRO A CA 1 ATOM 1173 C C . PRO A 1 193 ? -24.773 -12.631 43.380 1.00 156.05 ? 206 PRO A C 1 ATOM 1174 O O . PRO A 1 193 ? -24.400 -12.606 44.560 1.00 154.56 ? 206 PRO A O 1 ATOM 1175 C CB . PRO A 1 193 ? -27.236 -12.313 43.026 1.00 153.82 ? 206 PRO A CB 1 ATOM 1176 C CG . PRO A 1 193 ? -27.764 -12.518 44.374 1.00 155.57 ? 206 PRO A CG 1 ATOM 1177 C CD . PRO A 1 193 ? -27.693 -14.008 44.610 1.00 158.99 ? 206 PRO A CD 1 ATOM 1178 N N . ARG A 1 194 ? -24.083 -12.069 42.397 1.00 156.02 ? 207 ARG A N 1 ATOM 1179 C CA . ARG A 1 194 ? -22.846 -11.347 42.645 1.00 157.26 ? 207 ARG A CA 1 ATOM 1180 C C . ARG A 1 194 ? -23.141 -9.854 42.714 1.00 150.04 ? 207 ARG A C 1 ATOM 1181 O O . ARG A 1 194 ? -23.792 -9.293 41.830 1.00 151.61 ? 207 ARG A O 1 ATOM 1182 C CB . ARG A 1 194 ? -21.808 -11.676 41.565 1.00 161.30 ? 207 ARG A CB 1 ATOM 1183 C CG . ARG A 1 194 ? -21.587 -13.170 41.415 1.00 163.21 ? 207 ARG A CG 1 ATOM 1184 C CD . ARG A 1 194 ? -20.415 -13.501 40.520 1.00 163.86 ? 207 ARG A CD 1 ATOM 1185 N NE . ARG A 1 194 ? -20.229 -14.950 40.447 1.00 175.54 ? 207 ARG A NE 1 ATOM 1186 C CZ . ARG A 1 194 ? -19.247 -15.549 39.777 1.00 175.23 ? 207 ARG A CZ 1 ATOM 1187 N NH1 . ARG A 1 194 ? -18.355 -14.812 39.114 1.00 166.98 ? 207 ARG A NH1 1 ATOM 1188 N NH2 . ARG A 1 194 ? -19.157 -16.882 39.775 1.00 174.48 ? 207 ARG A NH2 1 ATOM 1189 N N . LEU A 1 195 ? -22.684 -9.215 43.781 1.00 139.97 ? 208 LEU A N 1 ATOM 1190 C CA . LEU A 1 195 ? -23.062 -7.831 44.023 1.00 136.25 ? 208 LEU A CA 1 ATOM 1191 C C . LEU A 1 195 ? -22.291 -6.876 43.119 1.00 137.03 ? 208 LEU A C 1 ATOM 1192 O O . LEU A 1 195 ? -21.162 -7.159 42.728 1.00 137.99 ? 208 LEU A O 1 ATOM 1193 C CB . LEU A 1 195 ? -22.829 -7.445 45.481 1.00 124.97 ? 208 LEU A CB 1 ATOM 1194 C CG . LEU A 1 195 ? -23.166 -8.344 46.670 1.00 111.84 ? 208 LEU A CG 1 ATOM 1195 C CD1 . LEU A 1 195 ? -22.892 -7.521 47.902 1.00 104.05 ? 208 LEU A CD1 1 ATOM 1196 C CD2 . LEU A 1 195 ? -24.597 -8.853 46.675 1.00 105.09 ? 208 LEU A CD2 1 ATOM 1197 N N . ILE A 1 196 ? -22.912 -5.742 42.806 1.00 132.39 ? 209 ILE A N 1 ATOM 1198 C CA . ILE A 1 196 ? -22.343 -4.751 41.905 1.00 130.18 ? 209 ILE A CA 1 ATOM 1199 C C . ILE A 1 196 ? -22.272 -3.436 42.646 1.00 130.21 ? 209 ILE A C 1 ATOM 1200 O O . ILE A 1 196 ? -22.977 -3.255 43.627 1.00 141.22 ? 209 ILE A O 1 ATOM 1201 C CB . ILE A 1 196 ? -23.232 -4.545 40.651 1.00 142.18 ? 209 ILE A CB 1 ATOM 1202 C CG1 . ILE A 1 196 ? -24.648 -5.053 40.905 1.00 138.47 ? 209 ILE A CG1 1 ATOM 1203 C CG2 . ILE A 1 196 ? -22.637 -5.246 39.426 1.00 143.72 ? 209 ILE A CG2 1 ATOM 1204 C CD1 . ILE A 1 196 ? -24.771 -6.571 40.852 1.00 139.50 ? 209 ILE A CD1 1 ATOM 1205 N N . THR A 1 197 ? -21.450 -2.510 42.170 1.00 124.36 ? 210 THR A N 1 ATOM 1206 C CA . THR A 1 197 ? -21.315 -1.211 42.820 1.00 130.07 ? 210 THR A CA 1 ATOM 1207 C C . THR A 1 197 ? -21.579 -0.101 41.814 1.00 137.97 ? 210 THR A C 1 ATOM 1208 O O . THR A 1 197 ? -21.097 -0.152 40.688 1.00 144.09 ? 210 THR A O 1 ATOM 1209 C CB . THR A 1 197 ? -19.910 -1.044 43.473 1.00 156.05 ? 210 THR A CB 1 ATOM 1210 O OG1 . THR A 1 197 ? -19.861 0.159 44.250 1.00 155.49 ? 210 THR A OG1 1 ATOM 1211 C CG2 . THR A 1 197 ? -18.814 -1.001 42.418 1.00 150.85 ? 210 THR A CG2 1 ATOM 1212 N N . MET A 1 198 ? -22.363 0.893 42.214 1.00 143.30 ? 211 MET A N 1 ATOM 1213 C CA . MET A 1 198 ? -22.764 1.969 41.304 1.00 151.26 ? 211 MET A CA 1 ATOM 1214 C C . MET A 1 198 ? -21.824 3.177 41.335 1.00 136.00 ? 211 MET A C 1 ATOM 1215 O O . MET A 1 198 ? -21.912 4.083 40.504 1.00 136.75 ? 211 MET A O 1 ATOM 1216 C CB . MET A 1 198 ? -24.187 2.440 41.649 1.00 164.21 ? 211 MET A CB 1 ATOM 1217 C CG . MET A 1 198 ? -25.203 1.325 41.704 1.00 167.17 ? 211 MET A CG 1 ATOM 1218 S SD . MET A 1 198 ? -25.152 0.387 40.179 1.00 195.83 ? 211 MET A SD 1 ATOM 1219 C CE . MET A 1 198 ? -26.366 1.278 39.204 1.00 175.88 ? 211 MET A CE 1 ATOM 1220 N N . LYS A 1 199 ? -20.935 3.196 42.308 1.00 120.97 ? 212 LYS A N 1 ATOM 1221 C CA . LYS A 1 199 ? -20.115 4.372 42.534 1.00 113.84 ? 212 LYS A CA 1 ATOM 1222 C C . LYS A 1 199 ? -18.762 4.048 43.234 1.00 133.49 ? 212 LYS A C 1 ATOM 1223 O O . LYS A 1 199 ? -18.605 3.040 43.931 1.00 131.24 ? 212 LYS A O 1 ATOM 1224 C CB . LYS A 1 199 ? -20.932 5.426 43.308 1.00 100.88 ? 212 LYS A CB 1 ATOM 1225 N N . GLY A 1 200 ? -17.768 4.893 43.025 1.00 121.79 ? 213 GLY A N 1 ATOM 1226 C CA . GLY A 1 200 ? -16.510 4.709 43.713 1.00 116.47 ? 213 GLY A CA 1 ATOM 1227 C C . GLY A 1 200 ? -16.662 5.137 45.151 1.00 121.92 ? 213 GLY A C 1 ATOM 1228 O O . GLY A 1 200 ? -17.760 5.534 45.556 1.00 124.41 ? 213 GLY A O 1 ATOM 1229 N N . GLY A 1 201 ? -15.572 5.059 45.916 1.00 124.13 ? 214 GLY A N 1 ATOM 1230 C CA . GLY A 1 201 ? -15.542 5.557 47.282 1.00 129.52 ? 214 GLY A CA 1 ATOM 1231 C C . GLY A 1 201 ? -16.094 4.619 48.349 1.00 131.01 ? 214 GLY A C 1 ATOM 1232 O O . GLY A 1 201 ? -16.546 3.510 48.058 1.00 139.02 ? 214 GLY A O 1 ATOM 1233 N N . THR A 1 202 ? -16.091 5.096 49.589 1.00 119.51 ? 215 THR A N 1 ATOM 1234 C CA . THR A 1 202 ? -16.345 4.256 50.746 1.00 121.05 ? 215 THR A CA 1 ATOM 1235 C C . THR A 1 202 ? -17.772 3.717 50.863 1.00 123.96 ? 215 THR A C 1 ATOM 1236 O O . THR A 1 202 ? -17.966 2.511 50.949 1.00 130.20 ? 215 THR A O 1 ATOM 1237 C CB . THR A 1 202 ? -15.926 4.982 52.050 1.00 128.69 ? 215 THR A CB 1 ATOM 1238 O OG1 . THR A 1 202 ? -14.634 4.518 52.456 1.00 122.27 ? 215 THR A OG1 1 ATOM 1239 C CG2 . THR A 1 202 ? -16.926 4.720 53.182 1.00 139.33 ? 215 THR A CG2 1 ATOM 1240 N N . GLY A 1 203 ? -18.765 4.601 50.864 1.00 127.81 ? 216 GLY A N 1 ATOM 1241 C CA . GLY A 1 203 ? -20.144 4.208 51.101 1.00 136.44 ? 216 GLY A CA 1 ATOM 1242 C C . GLY A 1 203 ? -20.636 3.123 50.161 1.00 141.31 ? 216 GLY A C 1 ATOM 1243 O O . GLY A 1 203 ? -21.616 2.430 50.425 1.00 142.21 ? 216 GLY A O 1 ATOM 1244 N N . ASN A 1 204 ? -19.969 3.013 49.026 1.00 141.91 ? 217 ASN A N 1 ATOM 1245 C CA . ASN A 1 204 ? -20.333 2.040 48.013 1.00 142.87 ? 217 ASN A CA 1 ATOM 1246 C C . ASN A 1 204 ? -19.532 0.758 48.013 1.00 134.16 ? 217 ASN A C 1 ATOM 1247 O O . ASN A 1 204 ? -19.580 -0.006 47.057 1.00 144.35 ? 217 ASN A O 1 ATOM 1248 C CB . ASN A 1 204 ? -20.398 2.710 46.653 1.00 154.21 ? 217 ASN A CB 1 ATOM 1249 C CG . ASN A 1 204 ? -21.322 3.898 46.672 1.00 163.54 ? 217 ASN A CG 1 ATOM 1250 O OD1 . ASN A 1 204 ? -20.890 5.030 46.911 1.00 165.86 ? 217 ASN A OD1 1 ATOM 1251 N ND2 . ASN A 1 204 ? -22.613 3.645 46.468 1.00 165.27 ? 217 ASN A ND2 1 ATOM 1252 N N . GLY A 1 205 ? -18.718 0.578 49.040 1.00 124.78 ? 218 GLY A N 1 ATOM 1253 C CA . GLY A 1 205 ? -18.029 -0.685 49.238 1.00 124.63 ? 218 GLY A CA 1 ATOM 1254 C C . GLY A 1 205 ? -18.567 -1.471 50.420 1.00 125.22 ? 218 GLY A C 1 ATOM 1255 O O . GLY A 1 205 ? -19.685 -1.243 50.876 1.00 128.02 ? 218 GLY A O 1 ATOM 1256 N N . LEU A 1 206 ? -17.750 -2.391 50.926 1.00 121.76 ? 219 LEU A N 1 ATOM 1257 C CA . LEU A 1 206 ? -18.077 -3.196 52.107 1.00 117.73 ? 219 LEU A CA 1 ATOM 1258 C C . LEU A 1 206 ? -17.339 -2.685 53.336 1.00 110.17 ? 219 LEU A C 1 ATOM 1259 O O . LEU A 1 206 ? -16.172 -2.401 53.263 1.00 112.23 ? 219 LEU A O 1 ATOM 1260 C CB . LEU A 1 206 ? -17.675 -4.645 51.868 1.00 114.52 ? 219 LEU A CB 1 ATOM 1261 C CG . LEU A 1 206 ? -17.624 -5.578 53.076 1.00 111.95 ? 219 LEU A CG 1 ATOM 1262 C CD1 . LEU A 1 206 ? -18.961 -5.603 53.773 1.00 122.53 ? 219 LEU A CD1 1 ATOM 1263 C CD2 . LEU A 1 206 ? -17.244 -6.977 52.643 1.00 107.88 ? 219 LEU A CD2 1 ATOM 1264 N N . GLU A 1 207 ? -18.025 -2.538 54.455 1.00 110.72 ? 220 GLU A N 1 ATOM 1265 C CA . GLU A 1 207 ? -17.379 -2.075 55.672 1.00 117.97 ? 220 GLU A CA 1 ATOM 1266 C C . GLU A 1 207 ? -17.746 -2.998 56.817 1.00 131.74 ? 220 GLU A C 1 ATOM 1267 O O . GLU A 1 207 ? -18.905 -3.021 57.260 1.00 149.69 ? 220 GLU A O 1 ATOM 1268 C CB . GLU A 1 207 ? -17.804 -0.634 55.992 1.00 124.49 ? 220 GLU A CB 1 ATOM 1269 C CG . GLU A 1 207 ? -17.605 -0.180 57.436 1.00 136.44 ? 220 GLU A CG 1 ATOM 1270 C CD . GLU A 1 207 ? -18.197 1.208 57.710 1.00 157.38 ? 220 GLU A CD 1 ATOM 1271 O OE1 . GLU A 1 207 ? -18.653 1.449 58.853 1.00 166.61 ? 220 GLU A OE1 1 ATOM 1272 O OE2 . GLU A 1 207 ? -18.206 2.066 56.793 1.00 162.22 ? 220 GLU A OE2 1 ATOM 1273 N N . ILE A 1 208 ? -16.761 -3.733 57.328 1.00 119.07 ? 221 ILE A N 1 ATOM 1274 C CA . ILE A 1 208 ? -17.029 -4.644 58.437 1.00 115.13 ? 221 ILE A CA 1 ATOM 1275 C C . ILE A 1 208 ? -16.273 -4.292 59.717 1.00 117.82 ? 221 ILE A C 1 ATOM 1276 O O . ILE A 1 208 ? -15.271 -3.599 59.686 1.00 123.68 ? 221 ILE A O 1 ATOM 1277 C CB . ILE A 1 208 ? -16.807 -6.109 58.043 1.00 106.46 ? 221 ILE A CB 1 ATOM 1278 C CG1 . ILE A 1 208 ? -15.336 -6.467 58.006 1.00 99.96 ? 221 ILE A CG1 1 ATOM 1279 C CG2 . ILE A 1 208 ? -17.428 -6.398 56.695 1.00 112.34 ? 221 ILE A CG2 1 ATOM 1280 C CD1 . ILE A 1 208 ? -15.106 -7.836 57.383 1.00 100.66 ? 221 ILE A CD1 1 ATOM 1281 N N . MET A 1 209 ? -16.805 -4.743 60.843 1.00 118.77 ? 222 MET A N 1 ATOM 1282 C CA . MET A 1 209 ? -16.241 -4.467 62.150 1.00 112.39 ? 222 MET A CA 1 ATOM 1283 C C . MET A 1 209 ? -16.203 -5.755 62.953 1.00 119.32 ? 222 MET A C 1 ATOM 1284 O O . MET A 1 209 ? -17.242 -6.325 63.276 1.00 115.62 ? 222 MET A O 1 ATOM 1285 C CB . MET A 1 209 ? -17.080 -3.420 62.872 1.00 104.22 ? 222 MET A CB 1 ATOM 1286 C CG . MET A 1 209 ? -16.621 -3.122 64.293 1.00 103.21 ? 222 MET A CG 1 ATOM 1287 S SD . MET A 1 209 ? -17.677 -1.946 65.165 1.00 156.18 ? 222 MET A SD 1 ATOM 1288 C CE . MET A 1 209 ? -18.039 -0.750 63.869 1.00 141.69 ? 222 MET A CE 1 ATOM 1289 N N . LEU A 1 210 ? -14.996 -6.199 63.287 1.00 124.65 ? 223 LEU A N 1 ATOM 1290 C CA . LEU A 1 210 ? -14.809 -7.488 63.943 1.00 121.00 ? 223 LEU A CA 1 ATOM 1291 C C . LEU A 1 210 ? -14.271 -7.405 65.376 1.00 129.42 ? 223 LEU A C 1 ATOM 1292 O O . LEU A 1 210 ? -13.519 -6.490 65.729 1.00 131.30 ? 223 LEU A O 1 ATOM 1293 C CB . LEU A 1 210 ? -13.860 -8.356 63.110 1.00 99.90 ? 223 LEU A CB 1 ATOM 1294 C CG . LEU A 1 210 ? -14.209 -8.417 61.637 1.00 97.63 ? 223 LEU A CG 1 ATOM 1295 C CD1 . LEU A 1 210 ? -13.368 -9.496 60.936 1.00 99.10 ? 223 LEU A CD1 1 ATOM 1296 C CD2 . LEU A 1 210 ? -15.707 -8.658 61.482 1.00 96.36 ? 223 LEU A CD2 1 ATOM 1297 N N . ASP A 1 211 ? -14.675 -8.373 66.194 1.00 125.85 ? 224 ASP A N 1 ATOM 1298 C CA . ASP A 1 211 ? -13.935 -8.721 67.398 1.00 121.70 ? 224 ASP A CA 1 ATOM 1299 C C . ASP A 1 211 ? -13.140 -9.999 67.080 1.00 118.02 ? 224 ASP A C 1 ATOM 1300 O O . ASP A 1 211 ? -13.729 -11.063 66.879 1.00 113.38 ? 224 ASP A O 1 ATOM 1301 C CB . ASP A 1 211 ? -14.893 -8.948 68.564 1.00 133.14 ? 224 ASP A CB 1 ATOM 1302 C CG . ASP A 1 211 ? -14.270 -9.757 69.683 1.00 141.20 ? 224 ASP A CG 1 ATOM 1303 O OD1 . ASP A 1 211 ? -13.044 -9.665 69.876 1.00 133.71 ? 224 ASP A OD1 1 ATOM 1304 O OD2 . ASP A 1 211 ? -15.014 -10.484 70.376 1.00 151.93 ? 224 ASP A OD2 1 ATOM 1305 N N . ILE A 1 212 ? -11.810 -9.882 67.002 1.00 119.92 ? 225 ILE A N 1 ATOM 1306 C CA . ILE A 1 212 ? -10.921 -10.986 66.598 1.00 116.09 ? 225 ILE A CA 1 ATOM 1307 C C . ILE A 1 212 ? -10.972 -12.096 67.648 1.00 134.01 ? 225 ILE A C 1 ATOM 1308 O O . ILE A 1 212 ? -10.562 -13.234 67.395 1.00 132.68 ? 225 ILE A O 1 ATOM 1309 C CB . ILE A 1 212 ? -9.479 -10.483 66.401 1.00 99.68 ? 225 ILE A CB 1 ATOM 1310 N N . GLN A 1 213 ? -11.504 -11.740 68.822 1.00 144.75 ? 226 GLN A N 1 ATOM 1311 C CA . GLN A 1 213 ? -11.731 -12.659 69.941 1.00 138.40 ? 226 GLN A CA 1 ATOM 1312 C C . GLN A 1 213 ? -10.478 -13.227 70.578 1.00 140.39 ? 226 GLN A C 1 ATOM 1313 O O . GLN A 1 213 ? -10.439 -14.417 70.878 1.00 146.43 ? 226 GLN A O 1 ATOM 1314 C CB . GLN A 1 213 ? -12.568 -13.836 69.476 1.00 127.27 ? 226 GLN A CB 1 ATOM 1315 C CG . GLN A 1 213 ? -14.019 -13.548 69.283 1.00 119.36 ? 226 GLN A CG 1 ATOM 1316 C CD . GLN A 1 213 ? -14.716 -14.746 68.725 1.00 120.22 ? 226 GLN A CD 1 ATOM 1317 O OE1 . GLN A 1 213 ? -14.208 -15.392 67.804 1.00 117.51 ? 226 GLN A OE1 1 ATOM 1318 N NE2 . GLN A 1 213 ? -15.873 -15.083 69.296 1.00 122.71 ? 226 GLN A NE2 1 ATOM 1319 N N . GLN A 1 214 ? -9.470 -12.398 70.820 1.00 137.51 ? 227 GLN A N 1 ATOM 1320 C CA . GLN A 1 214 ? -8.225 -12.928 71.355 1.00 136.91 ? 227 GLN A CA 1 ATOM 1321 C C . GLN A 1 214 ? -8.440 -13.828 72.578 1.00 146.36 ? 227 GLN A C 1 ATOM 1322 O O . GLN A 1 214 ? -7.763 -14.843 72.723 1.00 155.86 ? 227 GLN A O 1 ATOM 1323 C CB . GLN A 1 214 ? -7.219 -11.816 71.656 1.00 127.52 ? 227 GLN A CB 1 ATOM 1324 C CG . GLN A 1 214 ? -6.556 -11.237 70.429 1.00 120.00 ? 227 GLN A CG 1 ATOM 1325 C CD . GLN A 1 214 ? -5.184 -10.681 70.740 1.00 116.95 ? 227 GLN A CD 1 ATOM 1326 O OE1 . GLN A 1 214 ? -4.442 -11.266 71.513 1.00 114.62 ? 227 GLN A OE1 1 ATOM 1327 N NE2 . GLN A 1 214 ? -4.841 -9.545 70.144 1.00 117.65 ? 227 GLN A NE2 1 ATOM 1328 N N . ASP A 1 215 ? -9.397 -13.476 73.434 1.00 140.49 ? 228 ASP A N 1 ATOM 1329 C CA . ASP A 1 215 ? -9.670 -14.257 74.645 1.00 133.41 ? 228 ASP A CA 1 ATOM 1330 C C . ASP A 1 215 ? -9.904 -15.774 74.367 1.00 141.43 ? 228 ASP A C 1 ATOM 1331 O O . ASP A 1 215 ? -9.637 -16.633 75.225 1.00 138.51 ? 228 ASP A O 1 ATOM 1332 C CB . ASP A 1 215 ? -10.845 -13.635 75.429 1.00 121.86 ? 228 ASP A CB 1 ATOM 1333 N N . GLU A 1 216 ? -10.416 -16.089 73.177 1.00 136.84 ? 229 GLU A N 1 ATOM 1334 C CA . GLU A 1 216 ? -10.643 -17.473 72.745 1.00 133.37 ? 229 GLU A CA 1 ATOM 1335 C C . GLU A 1 216 ? -9.465 -18.026 71.934 1.00 122.53 ? 229 GLU A C 1 ATOM 1336 O O . GLU A 1 216 ? -9.542 -19.078 71.295 1.00 120.52 ? 229 GLU A O 1 ATOM 1337 C CB . GLU A 1 216 ? -11.951 -17.605 71.983 1.00 136.96 ? 229 GLU A CB 1 ATOM 1338 N N . TYR A 1 217 ? -8.389 -17.266 71.914 1.00 116.48 ? 230 TYR A N 1 ATOM 1339 C CA . TYR A 1 217 ? -7.169 -17.716 71.282 1.00 127.15 ? 230 TYR A CA 1 ATOM 1340 C C . TYR A 1 217 ? -6.521 -18.839 72.091 1.00 131.54 ? 230 TYR A C 1 ATOM 1341 O O . TYR A 1 217 ? -6.429 -18.748 73.316 1.00 131.77 ? 230 TYR A O 1 ATOM 1342 C CB . TYR A 1 217 ? -6.207 -16.538 71.166 1.00 134.71 ? 230 TYR A CB 1 ATOM 1343 C CG . TYR A 1 217 ? -6.262 -15.834 69.843 1.00 136.40 ? 230 TYR A CG 1 ATOM 1344 C CD1 . TYR A 1 217 ? -7.432 -15.243 69.393 1.00 135.55 ? 230 TYR A CD1 1 ATOM 1345 C CD2 . TYR A 1 217 ? -5.139 -15.762 69.041 1.00 139.82 ? 230 TYR A CD2 1 ATOM 1346 C CE1 . TYR A 1 217 ? -7.476 -14.601 68.174 1.00 132.67 ? 230 TYR A CE1 1 ATOM 1347 C CE2 . TYR A 1 217 ? -5.176 -15.126 67.828 1.00 137.38 ? 230 TYR A CE2 1 ATOM 1348 C CZ . TYR A 1 217 ? -6.339 -14.549 67.402 1.00 130.77 ? 230 TYR A CZ 1 ATOM 1349 O OH . TYR A 1 217 ? -6.339 -13.922 66.190 1.00 126.02 ? 230 TYR A OH 1 ATOM 1350 N N . LEU A 1 218 ? -6.066 -19.886 71.400 1.00 132.97 ? 231 LEU A N 1 ATOM 1351 C CA . LEU A 1 218 ? -5.313 -20.981 72.024 1.00 132.37 ? 231 LEU A CA 1 ATOM 1352 C C . LEU A 1 218 ? -3.945 -20.491 72.461 1.00 134.45 ? 231 LEU A C 1 ATOM 1353 O O . LEU A 1 218 ? -3.390 -19.570 71.852 1.00 134.22 ? 231 LEU A O 1 ATOM 1354 C CB . LEU A 1 218 ? -5.106 -22.147 71.051 1.00 126.88 ? 231 LEU A CB 1 ATOM 1355 C CG . LEU A 1 218 ? -6.249 -23.102 70.697 1.00 128.67 ? 231 LEU A CG 1 ATOM 1356 C CD1 . LEU A 1 218 ? -5.826 -24.041 69.566 1.00 124.72 ? 231 LEU A CD1 1 ATOM 1357 C CD2 . LEU A 1 218 ? -6.699 -23.878 71.929 1.00 131.32 ? 231 LEU A CD2 1 ATOM 1358 N N . PRO A 1 219 ? -3.395 -21.101 73.523 1.00 131.45 ? 232 PRO A N 1 ATOM 1359 C CA . PRO A 1 219 ? -2.027 -20.808 73.966 1.00 129.68 ? 232 PRO A CA 1 ATOM 1360 C C . PRO A 1 219 ? -0.971 -21.410 73.048 1.00 130.61 ? 232 PRO A C 1 ATOM 1361 O O . PRO A 1 219 ? -1.174 -22.483 72.470 1.00 120.66 ? 232 PRO A O 1 ATOM 1362 C CB . PRO A 1 219 ? -1.956 -21.466 75.348 1.00 124.11 ? 232 PRO A CB 1 ATOM 1363 C CG . PRO A 1 219 ? -3.364 -21.540 75.792 1.00 122.29 ? 232 PRO A CG 1 ATOM 1364 C CD . PRO A 1 219 ? -4.152 -21.827 74.552 1.00 125.34 ? 232 PRO A CD 1 ATOM 1365 N N . VAL A 1 220 ? 0.145 -20.699 72.911 1.00 137.58 ? 233 VAL A N 1 ATOM 1366 C CA . VAL A 1 220 ? 1.267 -21.180 72.122 1.00 147.55 ? 233 VAL A CA 1 ATOM 1367 C C . VAL A 1 220 ? 2.376 -21.569 73.086 1.00 152.13 ? 233 VAL A C 1 ATOM 1368 O O . VAL A 1 220 ? 3.011 -20.714 73.701 1.00 157.28 ? 233 VAL A O 1 ATOM 1369 C CB . VAL A 1 220 ? 1.800 -20.085 71.164 1.00 144.93 ? 233 VAL A CB 1 ATOM 1370 C CG1 . VAL A 1 220 ? 2.576 -20.708 70.000 1.00 139.33 ? 233 VAL A CG1 1 ATOM 1371 C CG2 . VAL A 1 220 ? 0.656 -19.223 70.658 1.00 144.91 ? 233 VAL A CG2 1 ATOM 1372 N N . TRP A 1 221 ? 2.584 -22.867 73.240 1.00 149.17 ? 234 TRP A N 1 ATOM 1373 C CA . TRP A 1 221 ? 3.672 -23.365 74.062 1.00 147.23 ? 234 TRP A CA 1 ATOM 1374 C C . TRP A 1 221 ? 4.865 -23.796 73.233 1.00 153.76 ? 234 TRP A C 1 ATOM 1375 O O . TRP A 1 221 ? 5.849 -24.307 73.762 1.00 163.85 ? 234 TRP A O 1 ATOM 1376 C CB . TRP A 1 221 ? 3.172 -24.472 74.966 1.00 143.72 ? 234 TRP A CB 1 ATOM 1377 C CG . TRP A 1 221 ? 2.160 -23.940 75.903 1.00 141.45 ? 234 TRP A CG 1 ATOM 1378 C CD1 . TRP A 1 221 ? 2.021 -22.643 76.285 1.00 137.23 ? 234 TRP A CD1 1 ATOM 1379 C CD2 . TRP A 1 221 ? 1.120 -24.671 76.566 1.00 147.32 ? 234 TRP A CD2 1 ATOM 1380 N NE1 . TRP A 1 221 ? 0.967 -22.517 77.156 1.00 143.92 ? 234 TRP A NE1 1 ATOM 1381 C CE2 . TRP A 1 221 ? 0.398 -23.747 77.349 1.00 147.30 ? 234 TRP A CE2 1 ATOM 1382 C CE3 . TRP A 1 221 ? 0.734 -26.016 76.579 1.00 153.43 ? 234 TRP A CE3 1 ATOM 1383 C CZ2 . TRP A 1 221 ? -0.689 -24.122 78.139 1.00 151.21 ? 234 TRP A CZ2 1 ATOM 1384 C CZ3 . TRP A 1 221 ? -0.345 -26.387 77.357 1.00 160.01 ? 234 TRP A CZ3 1 ATOM 1385 C CH2 . TRP A 1 221 ? -1.044 -25.444 78.130 1.00 159.39 ? 234 TRP A CH2 1 ATOM 1386 N N . GLY A 1 222 ? 4.757 -23.608 71.924 1.00 147.79 ? 235 GLY A N 1 ATOM 1387 C CA . GLY A 1 222 ? 5.806 -24.020 71.017 1.00 145.28 ? 235 GLY A CA 1 ATOM 1388 C C . GLY A 1 222 ? 5.370 -23.899 69.577 1.00 138.11 ? 235 GLY A C 1 ATOM 1389 O O . GLY A 1 222 ? 4.185 -23.750 69.283 1.00 137.63 ? 235 GLY A O 1 ATOM 1390 N N . GLU A 1 223 ? 6.334 -23.981 68.673 1.00 129.57 ? 236 GLU A N 1 ATOM 1391 C CA . GLU A 1 223 ? 6.069 -23.717 67.281 1.00 132.30 ? 236 GLU A CA 1 ATOM 1392 C C . GLU A 1 223 ? 5.571 -24.953 66.553 1.00 138.35 ? 236 GLU A C 1 ATOM 1393 O O . GLU A 1 223 ? 6.148 -26.029 66.667 1.00 136.91 ? 236 GLU A O 1 ATOM 1394 C CB . GLU A 1 223 ? 7.320 -23.141 66.633 1.00 144.47 ? 236 GLU A CB 1 ATOM 1395 C CG . GLU A 1 223 ? 7.771 -21.855 67.311 1.00 159.28 ? 236 GLU A CG 1 ATOM 1396 C CD . GLU A 1 223 ? 9.201 -21.463 66.979 1.00 171.06 ? 236 GLU A CD 1 ATOM 1397 O OE1 . GLU A 1 223 ? 9.569 -21.460 65.779 1.00 176.39 ? 236 GLU A OE1 1 ATOM 1398 O OE2 . GLU A 1 223 ? 9.953 -21.154 67.931 1.00 169.68 ? 236 GLU A OE2 1 ATOM 1399 N N . THR A 1 224 ? 4.456 -24.777 65.846 1.00 149.53 ? 237 THR A N 1 ATOM 1400 C CA . THR A 1 224 ? 3.858 -25.794 64.974 1.00 152.95 ? 237 THR A CA 1 ATOM 1401 C C . THR A 1 224 ? 2.948 -25.128 63.920 1.00 148.72 ? 237 THR A C 1 ATOM 1402 O O . THR A 1 224 ? 2.537 -23.976 64.085 1.00 150.65 ? 237 THR A O 1 ATOM 1403 C CB . THR A 1 224 ? 3.073 -26.864 65.788 1.00 128.70 ? 237 THR A CB 1 ATOM 1404 O OG1 . THR A 1 224 ? 1.707 -26.910 65.360 1.00 138.40 ? 237 THR A OG1 1 ATOM 1405 C CG2 . THR A 1 224 ? 3.104 -26.553 67.264 1.00 120.83 ? 237 THR A CG2 1 ATOM 1406 N N . ASP A 1 225 ? 2.638 -25.842 62.842 1.00 139.34 ? 238 ASP A N 1 ATOM 1407 C CA . ASP A 1 225 ? 1.824 -25.269 61.772 1.00 135.91 ? 238 ASP A CA 1 ATOM 1408 C C . ASP A 1 225 ? 0.445 -24.782 62.221 1.00 137.46 ? 238 ASP A C 1 ATOM 1409 O O . ASP A 1 225 ? -0.141 -23.917 61.581 1.00 143.88 ? 238 ASP A O 1 ATOM 1410 C CB . ASP A 1 225 ? 1.646 -26.257 60.619 1.00 146.41 ? 238 ASP A CB 1 ATOM 1411 C CG . ASP A 1 225 ? 2.948 -26.588 59.922 1.00 158.65 ? 238 ASP A CG 1 ATOM 1412 O OD1 . ASP A 1 225 ? 3.866 -27.098 60.597 1.00 169.74 ? 238 ASP A OD1 1 ATOM 1413 O OD2 . ASP A 1 225 ? 3.047 -26.356 58.697 1.00 156.17 ? 238 ASP A OD2 1 ATOM 1414 N N . GLU A 1 226 ? -0.088 -25.341 63.300 1.00 134.81 ? 239 GLU A N 1 ATOM 1415 C CA . GLU A 1 226 ? -1.423 -24.962 63.752 1.00 131.91 ? 239 GLU A CA 1 ATOM 1416 C C . GLU A 1 226 ? -1.390 -23.908 64.844 1.00 137.25 ? 239 GLU A C 1 ATOM 1417 O O . GLU A 1 226 ? -2.426 -23.546 65.400 1.00 141.65 ? 239 GLU A O 1 ATOM 1418 C CB . GLU A 1 226 ? -2.231 -26.181 64.194 1.00 134.56 ? 239 GLU A CB 1 ATOM 1419 C CG . GLU A 1 226 ? -2.587 -27.110 63.047 1.00 142.71 ? 239 GLU A CG 1 ATOM 1420 C CD . GLU A 1 226 ? -1.401 -27.933 62.557 1.00 149.54 ? 239 GLU A CD 1 ATOM 1421 O OE1 . GLU A 1 226 ? -0.530 -28.266 63.392 1.00 151.30 ? 239 GLU A OE1 1 ATOM 1422 O OE2 . GLU A 1 226 ? -1.344 -28.250 61.342 1.00 148.99 ? 239 GLU A OE2 1 ATOM 1423 N N . THR A 1 227 ? -0.193 -23.423 65.153 1.00 143.39 ? 240 THR A N 1 ATOM 1424 C CA . THR A 1 227 ? -0.025 -22.374 66.160 1.00 151.73 ? 240 THR A CA 1 ATOM 1425 C C . THR A 1 227 ? 0.714 -21.155 65.592 1.00 145.73 ? 240 THR A C 1 ATOM 1426 O O . THR A 1 227 ? 1.576 -21.303 64.716 1.00 148.34 ? 240 THR A O 1 ATOM 1427 C CB . THR A 1 227 ? 0.725 -22.909 67.395 1.00 152.76 ? 240 THR A CB 1 ATOM 1428 O OG1 . THR A 1 227 ? 1.890 -23.626 66.968 1.00 140.68 ? 240 THR A OG1 1 ATOM 1429 C CG2 . THR A 1 227 ? -0.179 -23.840 68.209 1.00 159.17 ? 240 THR A CG2 1 ATOM 1430 N N . SER A 1 228 ? 0.386 -19.962 66.093 1.00 131.68 ? 241 SER A N 1 ATOM 1431 C CA . SER A 1 228 ? 0.900 -18.721 65.500 1.00 127.04 ? 241 SER A CA 1 ATOM 1432 C C . SER A 1 228 ? 1.226 -17.582 66.471 1.00 116.48 ? 241 SER A C 1 ATOM 1433 O O . SER A 1 228 ? 0.556 -17.396 67.493 1.00 104.42 ? 241 SER A O 1 ATOM 1434 C CB . SER A 1 228 ? -0.078 -18.205 64.438 1.00 139.25 ? 241 SER A CB 1 ATOM 1435 O OG . SER A 1 228 ? -0.236 -16.795 64.526 1.00 140.72 ? 241 SER A OG 1 ATOM 1436 N N . PHE A 1 229 ? 2.252 -16.806 66.121 1.00 116.70 ? 242 PHE A N 1 ATOM 1437 C CA . PHE A 1 229 ? 2.669 -15.661 66.941 1.00 119.22 ? 242 PHE A CA 1 ATOM 1438 C C . PHE A 1 229 ? 1.841 -14.381 66.744 1.00 120.45 ? 242 PHE A C 1 ATOM 1439 O O . PHE A 1 229 ? 1.775 -13.544 67.642 1.00 118.36 ? 242 PHE A O 1 ATOM 1440 C CB . PHE A 1 229 ? 4.166 -15.353 66.759 1.00 115.43 ? 242 PHE A CB 1 ATOM 1441 C CG . PHE A 1 229 ? 5.070 -16.506 67.098 1.00 119.27 ? 242 PHE A CG 1 ATOM 1442 C CD1 . PHE A 1 229 ? 4.770 -17.355 68.148 1.00 130.76 ? 242 PHE A CD1 1 ATOM 1443 C CD2 . PHE A 1 229 ? 6.206 -16.754 66.354 1.00 112.45 ? 242 PHE A CD2 1 ATOM 1444 C CE1 . PHE A 1 229 ? 5.595 -18.427 68.450 1.00 132.48 ? 242 PHE A CE1 1 ATOM 1445 C CE2 . PHE A 1 229 ? 7.031 -17.826 66.643 1.00 112.49 ? 242 PHE A CE2 1 ATOM 1446 C CZ . PHE A 1 229 ? 6.728 -18.662 67.687 1.00 124.66 ? 242 PHE A CZ 1 ATOM 1447 N N . GLU A 1 230 ? 1.209 -14.232 65.582 1.00 117.27 ? 243 GLU A N 1 ATOM 1448 C CA . GLU A 1 230 ? 0.489 -13.003 65.248 1.00 109.66 ? 243 GLU A CA 1 ATOM 1449 C C . GLU A 1 230 ? -0.999 -13.055 65.587 1.00 98.21 ? 243 GLU A C 1 ATOM 1450 O O . GLU A 1 230 ? -1.620 -14.112 65.564 1.00 97.73 ? 243 GLU A O 1 ATOM 1451 C CB . GLU A 1 230 ? 0.689 -12.657 63.778 1.00 117.76 ? 243 GLU A CB 1 ATOM 1452 C CG . GLU A 1 230 ? 2.154 -12.532 63.361 1.00 132.64 ? 243 GLU A CG 1 ATOM 1453 C CD . GLU A 1 230 ? 2.767 -13.854 62.903 1.00 149.77 ? 243 GLU A CD 1 ATOM 1454 O OE1 . GLU A 1 230 ? 1.999 -14.786 62.570 1.00 158.76 ? 243 GLU A OE1 1 ATOM 1455 O OE2 . GLU A 1 230 ? 4.017 -13.961 62.873 1.00 152.83 ? 243 GLU A OE2 1 ATOM 1456 N N . ALA A 1 231 ? -1.554 -11.914 65.956 1.00 94.07 ? 244 ALA A N 1 ATOM 1457 C CA . ALA A 1 231 ? -2.986 -11.807 66.217 1.00 100.53 ? 244 ALA A CA 1 ATOM 1458 C C . ALA A 1 231 ? -3.676 -10.883 65.203 1.00 110.48 ? 244 ALA A C 1 ATOM 1459 O O . ALA A 1 231 ? -3.254 -9.754 64.946 1.00 105.90 ? 244 ALA A O 1 ATOM 1460 C CB . ALA A 1 231 ? -3.257 -11.355 67.657 1.00 91.93 ? 244 ALA A CB 1 ATOM 1461 N N . GLY A 1 232 ? -4.750 -11.386 64.621 1.00 120.05 ? 245 GLY A N 1 ATOM 1462 C CA . GLY A 1 232 ? -5.458 -10.649 63.601 1.00 119.89 ? 245 GLY A CA 1 ATOM 1463 C C . GLY A 1 232 ? -6.142 -11.579 62.618 1.00 117.60 ? 245 GLY A C 1 ATOM 1464 O O . GLY A 1 232 ? -6.350 -12.785 62.867 1.00 107.84 ? 245 GLY A O 1 ATOM 1465 N N . ILE A 1 233 ? -6.441 -11.017 61.457 1.00 113.86 ? 246 ILE A N 1 ATOM 1466 C CA . ILE A 1 233 ? -7.113 -11.756 60.414 1.00 114.20 ? 246 ILE A CA 1 ATOM 1467 C C . ILE A 1 233 ? -6.220 -11.750 59.192 1.00 105.90 ? 246 ILE A C 1 ATOM 1468 O O . ILE A 1 233 ? -5.194 -11.085 59.173 1.00 107.86 ? 246 ILE A O 1 ATOM 1469 C CB . ILE A 1 233 ? -8.461 -11.124 60.074 1.00 121.83 ? 246 ILE A CB 1 ATOM 1470 C CG1 . ILE A 1 233 ? -8.278 -9.988 59.063 1.00 127.40 ? 246 ILE A CG1 1 ATOM 1471 C CG2 . ILE A 1 233 ? -9.150 -10.658 61.346 1.00 124.25 ? 246 ILE A CG2 1 ATOM 1472 C CD1 . ILE A 1 233 ? -9.558 -9.220 58.746 1.00 135.08 ? 246 ILE A CD1 1 ATOM 1473 N N . LYS A 1 234 ? -6.550 -12.578 58.217 1.00 102.39 ? 247 LYS A N 1 ATOM 1474 C CA . LYS A 1 234 ? -5.958 -12.446 56.902 1.00 104.89 ? 247 LYS A CA 1 ATOM 1475 C C . LYS A 1 234 ? -7.080 -12.358 55.871 1.00 112.83 ? 247 LYS A C 1 ATOM 1476 O O . LYS A 1 234 ? -8.035 -13.116 55.929 1.00 123.20 ? 247 LYS A O 1 ATOM 1477 C CB . LYS A 1 234 ? -5.004 -13.607 56.593 1.00 104.18 ? 247 LYS A CB 1 ATOM 1478 C CG . LYS A 1 234 ? -3.836 -13.182 55.714 1.00 105.76 ? 247 LYS A CG 1 ATOM 1479 C CD . LYS A 1 234 ? -2.875 -14.328 55.439 1.00 116.66 ? 247 LYS A CD 1 ATOM 1480 C CE . LYS A 1 234 ? -1.463 -13.844 55.089 1.00 117.12 ? 247 LYS A CE 1 ATOM 1481 N NZ . LYS A 1 234 ? -0.414 -14.871 55.402 1.00 115.86 ? 247 LYS A NZ 1 ATOM 1482 N N . VAL A 1 235 ? -6.975 -11.433 54.931 1.00 108.02 ? 248 VAL A N 1 ATOM 1483 C CA . VAL A 1 235 ? -7.995 -11.301 53.907 1.00 100.79 ? 248 VAL A CA 1 ATOM 1484 C C . VAL A 1 235 ? -7.438 -11.689 52.532 1.00 101.28 ? 248 VAL A C 1 ATOM 1485 O O . VAL A 1 235 ? -6.233 -11.605 52.297 1.00 93.68 ? 248 VAL A O 1 ATOM 1486 C CB . VAL A 1 235 ? -8.524 -9.855 53.845 1.00 87.12 ? 248 VAL A CB 1 ATOM 1487 C CG1 . VAL A 1 235 ? -9.734 -9.813 52.969 1.00 85.52 ? 248 VAL A CG1 1 ATOM 1488 C CG2 . VAL A 1 235 ? -8.860 -9.352 55.233 1.00 83.50 ? 248 VAL A CG2 1 ATOM 1489 N N . GLN A 1 236 ? -8.305 -12.150 51.637 1.00 107.14 ? 249 GLN A N 1 ATOM 1490 C CA . GLN A 1 236 ? -7.953 -12.203 50.226 1.00 113.17 ? 249 GLN A CA 1 ATOM 1491 C C . GLN A 1 236 ? -9.102 -11.710 49.372 1.00 128.41 ? 249 GLN A C 1 ATOM 1492 O O . GLN A 1 236 ? -10.243 -12.107 49.578 1.00 144.08 ? 249 GLN A O 1 ATOM 1493 C CB . GLN A 1 236 ? -7.557 -13.605 49.778 1.00 113.26 ? 249 GLN A CB 1 ATOM 1494 C CG . GLN A 1 236 ? -7.119 -13.611 48.321 1.00 119.22 ? 249 GLN A CG 1 ATOM 1495 C CD . GLN A 1 236 ? -6.756 -14.977 47.802 1.00 126.62 ? 249 GLN A CD 1 ATOM 1496 O OE1 . GLN A 1 236 ? -6.801 -15.965 48.535 1.00 135.12 ? 249 GLN A OE1 1 ATOM 1497 N NE2 . GLN A 1 236 ? -6.395 -15.045 46.525 1.00 123.16 ? 249 GLN A NE2 1 ATOM 1498 N N . ILE A 1 237 ? -8.807 -10.845 48.408 1.00 123.25 ? 250 ILE A N 1 ATOM 1499 C CA . ILE A 1 237 ? -9.847 -10.389 47.488 1.00 119.35 ? 250 ILE A CA 1 ATOM 1500 C C . ILE A 1 237 ? -9.760 -11.091 46.132 1.00 114.66 ? 250 ILE A C 1 ATOM 1501 O O . ILE A 1 237 ? -8.845 -10.830 45.379 1.00 121.12 ? 250 ILE A O 1 ATOM 1502 C CB . ILE A 1 237 ? -9.765 -8.873 47.270 1.00 111.23 ? 250 ILE A CB 1 ATOM 1503 C CG1 . ILE A 1 237 ? -9.965 -8.142 48.601 1.00 102.35 ? 250 ILE A CG1 1 ATOM 1504 C CG2 . ILE A 1 237 ? -10.789 -8.440 46.217 1.00 116.24 ? 250 ILE A CG2 1 ATOM 1505 C CD1 . ILE A 1 237 ? -9.785 -6.654 48.531 1.00 93.81 ? 250 ILE A CD1 1 ATOM 1506 N N . HIS A 1 238 ? -10.703 -11.974 45.818 1.00 107.89 ? 251 HIS A N 1 ATOM 1507 C CA . HIS A 1 238 ? -10.647 -12.701 44.545 1.00 119.41 ? 251 HIS A CA 1 ATOM 1508 C C . HIS A 1 238 ? -11.884 -12.555 43.662 1.00 121.77 ? 251 HIS A C 1 ATOM 1509 O O . HIS A 1 238 ? -12.963 -12.179 44.116 1.00 120.64 ? 251 HIS A O 1 ATOM 1510 C CB . HIS A 1 238 ? -10.368 -14.205 44.745 1.00 130.28 ? 251 HIS A CB 1 ATOM 1511 C CG . HIS A 1 238 ? -10.978 -14.787 45.984 1.00 139.31 ? 251 HIS A CG 1 ATOM 1512 N ND1 . HIS A 1 238 ? -12.276 -14.542 46.368 1.00 145.48 ? 251 HIS A ND1 1 ATOM 1513 C CD2 . HIS A 1 238 ? -10.458 -15.609 46.925 1.00 141.36 ? 251 HIS A CD2 1 ATOM 1514 C CE1 . HIS A 1 238 ? -12.529 -15.179 47.499 1.00 143.81 ? 251 HIS A CE1 1 ATOM 1515 N NE2 . HIS A 1 238 ? -11.443 -15.836 47.856 1.00 142.21 ? 251 HIS A NE2 1 ATOM 1516 N N . SER A 1 239 ? -11.722 -12.866 42.385 1.00 119.39 ? 252 SER A N 1 ATOM 1517 C CA . SER A 1 239 ? -12.892 -13.072 41.565 1.00 126.44 ? 252 SER A CA 1 ATOM 1518 C C . SER A 1 239 ? -13.553 -14.233 42.254 1.00 131.38 ? 252 SER A C 1 ATOM 1519 O O . SER A 1 239 ? -12.873 -15.010 42.938 1.00 132.44 ? 252 SER A O 1 ATOM 1520 C CB . SER A 1 239 ? -12.522 -13.463 40.146 1.00 131.87 ? 252 SER A CB 1 ATOM 1521 O OG . SER A 1 239 ? -13.378 -14.484 39.672 1.00 137.63 ? 252 SER A OG 1 ATOM 1522 N N . GLN A 1 240 ? -14.872 -14.327 42.121 1.00 131.46 ? 253 GLN A N 1 ATOM 1523 C CA . GLN A 1 240 ? -15.602 -15.455 42.671 1.00 130.37 ? 253 GLN A CA 1 ATOM 1524 C C . GLN A 1 240 ? -15.150 -16.711 41.959 1.00 141.19 ? 253 GLN A C 1 ATOM 1525 O O . GLN A 1 240 ? -15.061 -17.774 42.571 1.00 147.81 ? 253 GLN A O 1 ATOM 1526 C CB . GLN A 1 240 ? -17.104 -15.268 42.543 1.00 125.25 ? 253 GLN A CB 1 ATOM 1527 C CG . GLN A 1 240 ? -17.679 -14.183 43.449 1.00 121.77 ? 253 GLN A CG 1 ATOM 1528 C CD . GLN A 1 240 ? -17.323 -12.790 42.987 1.00 116.17 ? 253 GLN A CD 1 ATOM 1529 O OE1 . GLN A 1 240 ? -16.582 -12.620 42.022 1.00 115.20 ? 253 GLN A OE1 1 ATOM 1530 N NE2 . GLN A 1 240 ? -17.851 -11.782 43.670 1.00 115.36 ? 253 GLN A NE2 1 ATOM 1531 N N . ASP A 1 241 ? -14.845 -16.572 40.670 1.00 151.35 ? 254 ASP A N 1 ATOM 1532 C CA . ASP A 1 241 ? -14.363 -17.684 39.844 1.00 167.12 ? 254 ASP A CA 1 ATOM 1533 C C . ASP A 1 241 ? -13.078 -18.309 40.412 1.00 171.35 ? 254 ASP A C 1 ATOM 1534 O O . ASP A 1 241 ? -12.701 -19.428 40.055 1.00 181.07 ? 254 ASP A O 1 ATOM 1535 C CB . ASP A 1 241 ? -14.136 -17.221 38.399 1.00 168.45 ? 254 ASP A CB 1 ATOM 1536 C CG . ASP A 1 241 ? -15.423 -16.805 37.703 1.00 175.05 ? 254 ASP A CG 1 ATOM 1537 O OD1 . ASP A 1 241 ? -16.452 -16.620 38.381 1.00 177.54 ? 254 ASP A OD1 1 ATOM 1538 O OD2 . ASP A 1 241 ? -15.400 -16.652 36.464 1.00 178.22 ? 254 ASP A OD2 1 ATOM 1539 N N . GLU A 1 242 ? -12.392 -17.563 41.270 1.00 161.56 ? 255 GLU A N 1 ATOM 1540 C CA . GLU A 1 242 ? -11.118 -17.991 41.832 1.00 156.98 ? 255 GLU A CA 1 ATOM 1541 C C . GLU A 1 242 ? -11.240 -18.263 43.327 1.00 147.95 ? 255 GLU A C 1 ATOM 1542 O O . GLU A 1 242 ? -11.676 -17.382 44.072 1.00 150.75 ? 255 GLU A O 1 ATOM 1543 C CB . GLU A 1 242 ? -10.068 -16.915 41.576 1.00 163.20 ? 255 GLU A CB 1 ATOM 1544 C CG . GLU A 1 242 ? -8.736 -17.166 42.254 1.00 170.11 ? 255 GLU A CG 1 ATOM 1545 C CD . GLU A 1 242 ? -7.714 -16.093 41.929 1.00 170.07 ? 255 GLU A CD 1 ATOM 1546 O OE1 . GLU A 1 242 ? -7.957 -15.307 40.982 1.00 169.00 ? 255 GLU A OE1 1 ATOM 1547 O OE2 . GLU A 1 242 ? -6.673 -16.039 42.624 1.00 167.37 ? 255 GLU A OE2 1 ATOM 1548 N N . PRO A 1 243 ? -10.866 -19.479 43.771 1.00 135.15 ? 256 PRO A N 1 ATOM 1549 C CA . PRO A 1 243 ? -10.864 -19.848 45.191 1.00 127.91 ? 256 PRO A CA 1 ATOM 1550 C C . PRO A 1 243 ? -9.696 -19.191 45.904 1.00 134.77 ? 256 PRO A C 1 ATOM 1551 O O . PRO A 1 243 ? -8.694 -18.886 45.251 1.00 140.76 ? 256 PRO A O 1 ATOM 1552 C CB . PRO A 1 243 ? -10.606 -21.342 45.147 1.00 119.30 ? 256 PRO A CB 1 ATOM 1553 C CG . PRO A 1 243 ? -9.727 -21.496 43.994 1.00 122.98 ? 256 PRO A CG 1 ATOM 1554 C CD . PRO A 1 243 ? -10.284 -20.552 42.953 1.00 131.92 ? 256 PRO A CD 1 ATOM 1555 N N . PRO A 1 244 ? -9.821 -18.954 47.222 1.00 130.05 ? 257 PRO A N 1 ATOM 1556 C CA . PRO A 1 244 ? -8.696 -18.364 47.951 1.00 120.78 ? 257 PRO A CA 1 ATOM 1557 C C . PRO A 1 244 ? -7.575 -19.367 48.201 1.00 125.83 ? 257 PRO A C 1 ATOM 1558 O O . PRO A 1 244 ? -7.863 -20.548 48.485 1.00 129.95 ? 257 PRO A O 1 ATOM 1559 C CB . PRO A 1 244 ? -9.326 -17.943 49.281 1.00 110.78 ? 257 PRO A CB 1 ATOM 1560 C CG . PRO A 1 244 ? -10.502 -18.838 49.461 1.00 111.59 ? 257 PRO A CG 1 ATOM 1561 C CD . PRO A 1 244 ? -11.001 -19.170 48.082 1.00 123.01 ? 257 PRO A CD 1 ATOM 1562 N N . LEU A 1 245 ? -6.327 -18.912 48.066 1.00 120.65 ? 258 LEU A N 1 ATOM 1563 C CA . LEU A 1 245 ? -5.256 -19.508 48.840 1.00 121.89 ? 258 LEU A CA 1 ATOM 1564 C C . LEU A 1 245 ? -4.782 -18.395 49.769 1.00 112.55 ? 258 LEU A C 1 ATOM 1565 O O . LEU A 1 245 ? -3.839 -17.689 49.450 1.00 104.10 ? 258 LEU A O 1 ATOM 1566 C CB . LEU A 1 245 ? -4.106 -19.999 47.902 1.00 82.87 ? 258 LEU A CB 1 ATOM 1567 N N . ILE A 1 246 ? -5.341 -18.349 50.977 1.00 124.58 ? 259 ILE A N 1 ATOM 1568 C CA . ILE A 1 246 ? -5.138 -17.218 51.883 1.00 119.24 ? 259 ILE A CA 1 ATOM 1569 C C . ILE A 1 246 ? -3.800 -17.348 52.608 1.00 119.50 ? 259 ILE A C 1 ATOM 1570 O O . ILE A 1 246 ? -3.178 -16.363 53.014 1.00 109.72 ? 259 ILE A O 1 ATOM 1571 C CB . ILE A 1 246 ? -6.285 -17.092 52.882 1.00 113.00 ? 259 ILE A CB 1 ATOM 1572 C CG1 . ILE A 1 246 ? -7.372 -16.205 52.308 1.00 110.08 ? 259 ILE A CG1 1 ATOM 1573 C CG2 . ILE A 1 246 ? -5.806 -16.446 54.154 1.00 115.47 ? 259 ILE A CG2 1 ATOM 1574 C CD1 . ILE A 1 246 ? -7.639 -14.967 53.136 1.00 105.36 ? 259 ILE A CD1 1 ATOM 1575 N N . ASP A 1 247 ? -3.368 -18.592 52.745 1.00 124.61 ? 260 ASP A N 1 ATOM 1576 C CA . ASP A 1 247 ? -2.030 -18.909 53.164 1.00 129.21 ? 260 ASP A CA 1 ATOM 1577 C C . ASP A 1 247 ? -1.028 -18.089 52.340 1.00 134.72 ? 260 ASP A C 1 ATOM 1578 O O . ASP A 1 247 ? -0.266 -17.307 52.902 1.00 137.97 ? 260 ASP A O 1 ATOM 1579 C CB . ASP A 1 247 ? -1.793 -20.412 52.977 1.00 139.80 ? 260 ASP A CB 1 ATOM 1580 C CG . ASP A 1 247 ? -0.627 -20.924 53.796 1.00 146.38 ? 260 ASP A CG 1 ATOM 1581 O OD1 . ASP A 1 247 ? -0.725 -20.866 55.046 1.00 142.65 ? 260 ASP A OD1 1 ATOM 1582 O OD2 . ASP A 1 247 ? 0.379 -21.383 53.196 1.00 149.83 ? 260 ASP A OD2 1 ATOM 1583 N N . GLN A 1 248 ? -1.014 -18.306 51.021 1.00 132.99 ? 261 GLN A N 1 ATOM 1584 C CA . GLN A 1 248 ? -0.086 -17.655 50.078 1.00 126.73 ? 261 GLN A CA 1 ATOM 1585 C C . GLN A 1 248 ? -0.402 -16.232 49.558 1.00 121.80 ? 261 GLN A C 1 ATOM 1586 O O . GLN A 1 248 ? 0.473 -15.376 49.458 1.00 119.97 ? 261 GLN A O 1 ATOM 1587 C CB . GLN A 1 248 ? 0.071 -18.553 48.860 1.00 130.55 ? 261 GLN A CB 1 ATOM 1588 C CG . GLN A 1 248 ? 0.647 -19.904 49.162 1.00 136.33 ? 261 GLN A CG 1 ATOM 1589 C CD . GLN A 1 248 ? 2.134 -19.847 49.407 1.00 138.06 ? 261 GLN A CD 1 ATOM 1590 O OE1 . GLN A 1 248 ? 2.945 -20.159 48.516 1.00 136.31 ? 261 GLN A OE1 1 ATOM 1591 N NE2 . GLN A 1 248 ? 2.510 -19.451 50.620 1.00 138.24 ? 261 GLN A NE2 1 ATOM 1592 N N . LEU A 1 249 ? -1.635 -16.021 49.129 1.00 115.10 ? 262 LEU A N 1 ATOM 1593 C CA . LEU A 1 249 ? -1.986 -14.800 48.414 1.00 115.72 ? 262 LEU A CA 1 ATOM 1594 C C . LEU A 1 249 ? -2.692 -13.738 49.241 1.00 123.57 ? 262 LEU A C 1 ATOM 1595 O O . LEU A 1 249 ? -3.154 -12.722 48.703 1.00 127.47 ? 262 LEU A O 1 ATOM 1596 C CB . LEU A 1 249 ? -2.792 -15.127 47.156 1.00 115.32 ? 262 LEU A CB 1 ATOM 1597 C CG . LEU A 1 249 ? -2.141 -16.228 46.319 1.00 115.21 ? 262 LEU A CG 1 ATOM 1598 C CD1 . LEU A 1 249 ? -2.701 -16.212 44.927 1.00 111.69 ? 262 LEU A CD1 1 ATOM 1599 C CD2 . LEU A 1 249 ? -0.617 -16.073 46.296 1.00 117.16 ? 262 LEU A CD2 1 ATOM 1600 N N . GLY A 1 250 ? -2.826 -13.985 50.534 1.00 125.85 ? 263 GLY A N 1 ATOM 1601 C CA . GLY A 1 250 ? -3.599 -13.081 51.366 1.00 131.82 ? 263 GLY A CA 1 ATOM 1602 C C . GLY A 1 250 ? -2.816 -11.901 51.908 1.00 128.46 ? 263 GLY A C 1 ATOM 1603 O O . GLY A 1 250 ? -1.575 -11.945 51.919 1.00 138.69 ? 263 GLY A O 1 ATOM 1604 N N . PHE A 1 251 ? -3.537 -10.871 52.375 1.00 105.94 ? 264 PHE A N 1 ATOM 1605 C CA . PHE A 1 251 ? -2.926 -9.687 52.974 1.00 98.07 ? 264 PHE A CA 1 ATOM 1606 C C . PHE A 1 251 ? -3.456 -9.378 54.367 1.00 101.78 ? 264 PHE A C 1 ATOM 1607 O O . PHE A 1 251 ? -4.659 -9.231 54.534 1.00 105.84 ? 264 PHE A O 1 ATOM 1608 C CB . PHE A 1 251 ? -3.150 -8.476 52.071 1.00 94.61 ? 264 PHE A CB 1 ATOM 1609 C CG . PHE A 1 251 ? -4.510 -7.858 52.196 1.00 88.11 ? 264 PHE A CG 1 ATOM 1610 C CD1 . PHE A 1 251 ? -4.746 -6.889 53.138 1.00 89.90 ? 264 PHE A CD1 1 ATOM 1611 C CD2 . PHE A 1 251 ? -5.543 -8.218 51.335 1.00 95.05 ? 264 PHE A CD2 1 ATOM 1612 C CE1 . PHE A 1 251 ? -6.005 -6.315 53.252 1.00 100.71 ? 264 PHE A CE1 1 ATOM 1613 C CE2 . PHE A 1 251 ? -6.798 -7.644 51.435 1.00 96.69 ? 264 PHE A CE2 1 ATOM 1614 C CZ . PHE A 1 251 ? -7.036 -6.697 52.398 1.00 96.09 ? 264 PHE A CZ 1 ATOM 1615 N N . GLY A 1 252 ? -2.562 -9.235 55.351 1.00 103.67 ? 265 GLY A N 1 ATOM 1616 C CA . GLY A 1 252 ? -2.942 -8.965 56.743 1.00 107.51 ? 265 GLY A CA 1 ATOM 1617 C C . GLY A 1 252 ? -3.834 -7.757 57.085 1.00 107.64 ? 265 GLY A C 1 ATOM 1618 O O . GLY A 1 252 ? -3.896 -6.773 56.364 1.00 114.73 ? 265 GLY A O 1 ATOM 1619 N N . VAL A 1 253 ? -4.575 -7.863 58.181 1.00 97.65 ? 266 VAL A N 1 ATOM 1620 C CA . VAL A 1 253 ? -5.296 -6.744 58.784 1.00 91.23 ? 266 VAL A CA 1 ATOM 1621 C C . VAL A 1 253 ? -5.185 -6.869 60.307 1.00 102.52 ? 266 VAL A C 1 ATOM 1622 O O . VAL A 1 253 ? -5.578 -7.895 60.877 1.00 110.84 ? 266 VAL A O 1 ATOM 1623 C CB . VAL A 1 253 ? -6.772 -6.774 58.414 1.00 94.23 ? 266 VAL A CB 1 ATOM 1624 C CG1 . VAL A 1 253 ? -7.569 -5.801 59.292 1.00 90.47 ? 266 VAL A CG1 1 ATOM 1625 C CG2 . VAL A 1 253 ? -6.920 -6.457 56.952 1.00 108.27 ? 266 VAL A CG2 1 ATOM 1626 N N . ALA A 1 254 ? -4.661 -5.839 60.966 1.00 96.57 ? 267 ALA A N 1 ATOM 1627 C CA . ALA A 1 254 ? -4.476 -5.874 62.411 1.00 89.13 ? 267 ALA A CA 1 ATOM 1628 C C . ALA A 1 254 ? -5.649 -5.297 63.186 1.00 95.46 ? 267 ALA A C 1 ATOM 1629 O O . ALA A 1 254 ? -6.433 -4.485 62.664 1.00 103.84 ? 267 ALA A O 1 ATOM 1630 C CB . ALA A 1 254 ? -3.213 -5.162 62.793 1.00 89.38 ? 267 ALA A CB 1 ATOM 1631 N N . PRO A 1 255 ? -5.783 -5.730 64.448 1.00 90.21 ? 268 PRO A N 1 ATOM 1632 C CA . PRO A 1 255 ? -6.838 -5.282 65.364 1.00 87.97 ? 268 PRO A CA 1 ATOM 1633 C C . PRO A 1 255 ? -6.456 -3.935 65.892 1.00 100.59 ? 268 PRO A C 1 ATOM 1634 O O . PRO A 1 255 ? -5.259 -3.668 66.019 1.00 112.48 ? 268 PRO A O 1 ATOM 1635 C CB . PRO A 1 255 ? -6.715 -6.265 66.511 1.00 85.37 ? 268 PRO A CB 1 ATOM 1636 C CG . PRO A 1 255 ? -5.265 -6.526 66.556 1.00 87.31 ? 268 PRO A CG 1 ATOM 1637 C CD . PRO A 1 255 ? -4.805 -6.585 65.134 1.00 85.40 ? 268 PRO A CD 1 ATOM 1638 N N . GLY A 1 256 ? -7.438 -3.110 66.225 1.00 105.20 ? 269 GLY A N 1 ATOM 1639 C CA . GLY A 1 256 ? -7.182 -1.792 66.794 1.00 109.85 ? 269 GLY A CA 1 ATOM 1640 C C . GLY A 1 256 ? -6.825 -0.767 65.740 1.00 106.68 ? 269 GLY A C 1 ATOM 1641 O O . GLY A 1 256 ? -6.113 0.196 66.012 1.00 112.58 ? 269 GLY A O 1 ATOM 1642 N N . PHE A 1 257 ? -7.308 -1.007 64.529 1.00 101.83 ? 270 PHE A N 1 ATOM 1643 C CA . PHE A 1 257 ? -7.113 -0.110 63.407 1.00 95.69 ? 270 PHE A CA 1 ATOM 1644 C C . PHE A 1 257 ? -8.342 -0.119 62.512 1.00 95.53 ? 270 PHE A C 1 ATOM 1645 O O . PHE A 1 257 ? -8.892 -1.179 62.239 1.00 106.16 ? 270 PHE A O 1 ATOM 1646 C CB . PHE A 1 257 ? -5.955 -0.629 62.575 1.00 99.47 ? 270 PHE A CB 1 ATOM 1647 C CG . PHE A 1 257 ? -4.616 -0.293 63.121 1.00 96.67 ? 270 PHE A CG 1 ATOM 1648 C CD1 . PHE A 1 257 ? -4.070 0.961 62.905 1.00 99.76 ? 270 PHE A CD1 1 ATOM 1649 C CD2 . PHE A 1 257 ? -3.896 -1.230 63.826 1.00 96.59 ? 270 PHE A CD2 1 ATOM 1650 C CE1 . PHE A 1 257 ? -2.848 1.278 63.391 1.00 104.95 ? 270 PHE A CE1 1 ATOM 1651 C CE2 . PHE A 1 257 ? -2.667 -0.924 64.314 1.00 107.83 ? 270 PHE A CE2 1 ATOM 1652 C CZ . PHE A 1 257 ? -2.138 0.334 64.095 1.00 113.87 ? 270 PHE A CZ 1 ATOM 1653 N N . GLN A 1 258 ? -8.771 1.032 62.023 1.00 89.09 ? 271 GLN A N 1 ATOM 1654 C CA . GLN A 1 258 ? -9.611 0.991 60.837 1.00 94.91 ? 271 GLN A CA 1 ATOM 1655 C C . GLN A 1 258 ? -8.666 0.897 59.660 1.00 104.21 ? 271 GLN A C 1 ATOM 1656 O O . GLN A 1 258 ? -7.626 1.567 59.628 1.00 106.80 ? 271 GLN A O 1 ATOM 1657 C CB . GLN A 1 258 ? -10.507 2.208 60.688 1.00 88.02 ? 271 GLN A CB 1 ATOM 1658 C CG . GLN A 1 258 ? -11.376 2.138 59.456 1.00 93.98 ? 271 GLN A CG 1 ATOM 1659 C CD . GLN A 1 258 ? -12.469 3.189 59.465 1.00 121.73 ? 271 GLN A CD 1 ATOM 1660 O OE1 . GLN A 1 258 ? -12.390 4.167 60.198 1.00 133.07 ? 271 GLN A OE1 1 ATOM 1661 N NE2 . GLN A 1 258 ? -13.499 2.993 58.645 1.00 130.21 ? 271 GLN A NE2 1 ATOM 1662 N N . THR A 1 259 ? -9.005 0.036 58.712 1.00 102.46 ? 272 THR A N 1 ATOM 1663 C CA . THR A 1 259 ? -8.158 -0.145 57.557 1.00 92.79 ? 272 THR A CA 1 ATOM 1664 C C . THR A 1 259 ? -8.942 -0.002 56.294 1.00 97.02 ? 272 THR A C 1 ATOM 1665 O O . THR A 1 259 ? -9.814 -0.823 56.021 1.00 108.25 ? 272 THR A O 1 ATOM 1666 C CB . THR A 1 259 ? -7.637 -1.543 57.480 1.00 81.29 ? 272 THR A CB 1 ATOM 1667 O OG1 . THR A 1 259 ? -6.835 -1.807 58.632 1.00 75.73 ? 272 THR A OG1 1 ATOM 1668 C CG2 . THR A 1 259 ? -6.843 -1.706 56.211 1.00 79.29 ? 272 THR A CG2 1 ATOM 1669 N N . PHE A 1 260 ? -8.606 1.022 55.520 1.00 88.12 ? 273 PHE A N 1 ATOM 1670 C CA . PHE A 1 260 ? -9.243 1.264 54.256 1.00 84.01 ? 273 PHE A CA 1 ATOM 1671 C C . PHE A 1 260 ? -8.378 0.538 53.282 1.00 92.99 ? 273 PHE A C 1 ATOM 1672 O O . PHE A 1 260 ? -7.160 0.547 53.418 1.00 86.03 ? 273 PHE A O 1 ATOM 1673 C CB . PHE A 1 260 ? -9.274 2.749 53.951 1.00 80.16 ? 273 PHE A CB 1 ATOM 1674 C CG . PHE A 1 260 ? -9.847 3.559 55.051 1.00 73.16 ? 273 PHE A CG 1 ATOM 1675 C CD1 . PHE A 1 260 ? -11.100 4.101 54.942 1.00 80.56 ? 273 PHE A CD1 1 ATOM 1676 C CD2 . PHE A 1 260 ? -9.142 3.748 56.214 1.00 78.83 ? 273 PHE A CD2 1 ATOM 1677 C CE1 . PHE A 1 260 ? -11.627 4.828 55.986 1.00 95.36 ? 273 PHE A CE1 1 ATOM 1678 C CE2 . PHE A 1 260 ? -9.662 4.460 57.263 1.00 89.35 ? 273 PHE A CE2 1 ATOM 1679 C CZ . PHE A 1 260 ? -10.899 5.005 57.150 1.00 96.77 ? 273 PHE A CZ 1 ATOM 1680 N N . VAL A 1 261 ? -9.024 -0.153 52.349 1.00 102.23 ? 274 VAL A N 1 ATOM 1681 C CA . VAL A 1 261 ? -8.347 -0.870 51.275 1.00 96.81 ? 274 VAL A CA 1 ATOM 1682 C C . VAL A 1 261 ? -9.081 -0.468 50.044 1.00 91.02 ? 274 VAL A C 1 ATOM 1683 O O . VAL A 1 261 ? -10.261 -0.750 49.933 1.00 97.12 ? 274 VAL A O 1 ATOM 1684 C CB . VAL A 1 261 ? -8.504 -2.389 51.397 1.00 90.65 ? 274 VAL A CB 1 ATOM 1685 C CG1 . VAL A 1 261 ? -8.378 -3.050 50.021 1.00 88.81 ? 274 VAL A CG1 1 ATOM 1686 C CG2 . VAL A 1 261 ? -7.482 -2.968 52.412 1.00 65.62 ? 274 VAL A CG2 1 ATOM 1687 N N . SER A 1 262 ? -8.395 0.214 49.139 1.00 83.74 ? 275 SER A N 1 ATOM 1688 C CA . SER A 1 262 ? -9.071 0.888 48.054 1.00 89.63 ? 275 SER A CA 1 ATOM 1689 C C . SER A 1 262 ? -8.504 0.311 46.789 1.00 92.78 ? 275 SER A C 1 ATOM 1690 O O . SER A 1 262 ? -7.286 0.300 46.620 1.00 84.93 ? 275 SER A O 1 ATOM 1691 C CB . SER A 1 262 ? -8.822 2.377 48.142 1.00 92.65 ? 275 SER A CB 1 ATOM 1692 O OG . SER A 1 262 ? -9.185 3.004 46.940 1.00 99.41 ? 275 SER A OG 1 ATOM 1693 N N . CYS A 1 263 ? -9.401 -0.168 45.918 1.00 91.45 ? 276 CYS A N 1 ATOM 1694 C CA . CYS A 1 263 ? -9.061 -1.150 44.900 1.00 82.56 ? 276 CYS A CA 1 ATOM 1695 C C . CYS A 1 263 ? -9.180 -0.577 43.535 1.00 89.23 ? 276 CYS A C 1 ATOM 1696 O O . CYS A 1 263 ? -9.915 0.376 43.325 1.00 94.64 ? 276 CYS A O 1 ATOM 1697 C CB . CYS A 1 263 ? -9.974 -2.373 44.993 1.00 81.28 ? 276 CYS A CB 1 ATOM 1698 S SG . CYS A 1 263 ? -9.902 -3.286 46.587 1.00 88.89 ? 276 CYS A SG 1 ATOM 1699 N N . GLN A 1 264 ? -8.418 -1.142 42.608 1.00 100.11 ? 277 GLN A N 1 ATOM 1700 C CA . GLN A 1 264 ? -8.524 -0.771 41.210 1.00 106.40 ? 277 GLN A CA 1 ATOM 1701 C C . GLN A 1 264 ? -8.623 -2.045 40.372 1.00 109.20 ? 277 GLN A C 1 ATOM 1702 O O . GLN A 1 264 ? -7.696 -2.848 40.372 1.00 114.56 ? 277 GLN A O 1 ATOM 1703 C CB . GLN A 1 264 ? -7.325 0.081 40.794 1.00 109.34 ? 277 GLN A CB 1 ATOM 1704 C CG . GLN A 1 264 ? -7.730 1.367 40.132 1.00 131.50 ? 277 GLN A CG 1 ATOM 1705 C CD . GLN A 1 264 ? -8.980 1.190 39.258 1.00 163.74 ? 277 GLN A CD 1 ATOM 1706 O OE1 . GLN A 1 264 ? -8.790 0.650 38.043 1.00 171.88 ? 277 GLN A OE1 1 ATOM 1707 N NE2 . GLN A 1 264 ? -10.099 1.548 39.664 1.00 170.23 ? 277 GLN A NE2 1 ATOM 1708 N N . GLU A 1 265 ? -9.739 -2.261 39.677 1.00 109.88 ? 278 GLU A N 1 ATOM 1709 C CA . GLU A 1 265 ? -9.900 -3.536 38.984 1.00 120.34 ? 278 GLU A CA 1 ATOM 1710 C C . GLU A 1 265 ? -9.102 -3.571 37.700 1.00 128.38 ? 278 GLU A C 1 ATOM 1711 O O . GLU A 1 265 ? -9.329 -2.770 36.794 1.00 130.75 ? 278 GLU A O 1 ATOM 1712 C CB . GLU A 1 265 ? -11.365 -3.847 38.685 1.00 128.34 ? 278 GLU A CB 1 ATOM 1713 C CG . GLU A 1 265 ? -11.565 -5.159 37.925 1.00 137.16 ? 278 GLU A CG 1 ATOM 1714 C CD . GLU A 1 265 ? -13.028 -5.558 37.814 1.00 145.37 ? 278 GLU A CD 1 ATOM 1715 O OE1 . GLU A 1 265 ? -13.510 -6.319 38.680 1.00 151.73 ? 278 GLU A OE1 1 ATOM 1716 O OE2 . GLU A 1 265 ? -13.700 -5.103 36.866 1.00 142.90 ? 278 GLU A OE2 1 ATOM 1717 N N . GLN A 1 266 ? -8.174 -4.520 37.626 1.00 131.36 ? 279 GLN A N 1 ATOM 1718 C CA . GLN A 1 266 ? -7.342 -4.679 36.449 1.00 134.03 ? 279 GLN A CA 1 ATOM 1719 C C . GLN A 1 266 ? -7.586 -6.046 35.870 1.00 125.66 ? 279 GLN A C 1 ATOM 1720 O O . GLN A 1 266 ? -7.260 -7.042 36.491 1.00 125.90 ? 279 GLN A O 1 ATOM 1721 C CB . GLN A 1 266 ? -5.880 -4.538 36.826 1.00 144.68 ? 279 GLN A CB 1 ATOM 1722 C CG . GLN A 1 266 ? -4.912 -4.838 35.700 1.00 162.34 ? 279 GLN A CG 1 ATOM 1723 C CD . GLN A 1 266 ? -3.480 -4.548 36.110 1.00 173.73 ? 279 GLN A CD 1 ATOM 1724 O OE1 . GLN A 1 266 ? -2.614 -5.429 36.067 1.00 175.80 ? 279 GLN A OE1 1 ATOM 1725 N NE2 . GLN A 1 266 ? -3.224 -3.305 36.525 1.00 174.57 ? 279 GLN A NE2 1 ATOM 1726 N N . ARG A 1 267 ? -8.160 -6.086 34.678 1.00 122.80 ? 280 ARG A N 1 ATOM 1727 C CA . ARG A 1 267 ? -8.579 -7.336 34.075 1.00 134.88 ? 280 ARG A CA 1 ATOM 1728 C C . ARG A 1 267 ? -7.798 -7.577 32.787 1.00 141.35 ? 280 ARG A C 1 ATOM 1729 O O . ARG A 1 267 ? -7.894 -6.775 31.853 1.00 145.15 ? 280 ARG A O 1 ATOM 1730 C CB . ARG A 1 267 ? -10.076 -7.251 33.789 1.00 149.01 ? 280 ARG A CB 1 ATOM 1731 C CG . ARG A 1 267 ? -10.694 -8.524 33.255 1.00 164.85 ? 280 ARG A CG 1 ATOM 1732 C CD . ARG A 1 267 ? -12.164 -8.637 33.634 1.00 171.73 ? 280 ARG A CD 1 ATOM 1733 N NE . ARG A 1 267 ? -12.990 -7.534 33.135 1.00 170.79 ? 280 ARG A NE 1 ATOM 1734 C CZ . ARG A 1 267 ? -13.722 -6.740 33.913 1.00 160.77 ? 280 ARG A CZ 1 ATOM 1735 N NH1 . ARG A 1 267 ? -13.724 -6.923 35.230 1.00 159.04 ? 280 ARG A NH1 1 ATOM 1736 N NH2 . ARG A 1 267 ? -14.456 -5.772 33.375 1.00 148.08 ? 280 ARG A NH2 1 ATOM 1737 N N . LEU A 1 268 ? -7.026 -8.670 32.725 1.00 137.81 ? 281 LEU A N 1 ATOM 1738 C CA . LEU A 1 268 ? -6.101 -8.883 31.588 1.00 134.44 ? 281 LEU A CA 1 ATOM 1739 C C . LEU A 1 268 ? -6.103 -10.260 30.933 1.00 131.49 ? 281 LEU A C 1 ATOM 1740 O O . LEU A 1 268 ? -6.272 -11.269 31.601 1.00 126.54 ? 281 LEU A O 1 ATOM 1741 C CB . LEU A 1 268 ? -4.680 -8.521 31.997 1.00 129.22 ? 281 LEU A CB 1 ATOM 1742 C CG . LEU A 1 268 ? -4.336 -8.843 33.445 1.00 118.46 ? 281 LEU A CG 1 ATOM 1743 C CD1 . LEU A 1 268 ? -3.945 -10.291 33.585 1.00 115.73 ? 281 LEU A CD1 1 ATOM 1744 C CD2 . LEU A 1 268 ? -3.219 -7.930 33.880 1.00 118.26 ? 281 LEU A CD2 1 ATOM 1745 N N . ILE A 1 269 ? -5.862 -10.287 29.623 1.00 135.16 ? 282 ILE A N 1 ATOM 1746 C CA . ILE A 1 269 ? -6.202 -11.455 28.793 1.00 139.65 ? 282 ILE A CA 1 ATOM 1747 C C . ILE A 1 269 ? -5.047 -12.047 27.981 1.00 146.47 ? 282 ILE A C 1 ATOM 1748 O O . ILE A 1 269 ? -4.143 -11.330 27.572 1.00 157.22 ? 282 ILE A O 1 ATOM 1749 C CB . ILE A 1 269 ? -7.348 -11.106 27.820 1.00 131.16 ? 282 ILE A CB 1 ATOM 1750 C CG1 . ILE A 1 269 ? -8.552 -10.592 28.603 1.00 139.15 ? 282 ILE A CG1 1 ATOM 1751 C CG2 . ILE A 1 269 ? -7.767 -12.307 27.031 1.00 125.59 ? 282 ILE A CG2 1 ATOM 1752 C CD1 . ILE A 1 269 ? -8.849 -11.408 29.854 1.00 143.62 ? 282 ILE A CD1 1 ATOM 1753 N N . TYR A 1 270 ? -5.101 -13.354 27.735 1.00 139.88 ? 283 TYR A N 1 ATOM 1754 C CA . TYR A 1 270 ? -4.054 -14.054 26.998 1.00 144.00 ? 283 TYR A CA 1 ATOM 1755 C C . TYR A 1 270 ? -4.625 -14.988 25.914 1.00 164.35 ? 283 TYR A C 1 ATOM 1756 O O . TYR A 1 270 ? -5.826 -15.289 25.909 1.00 172.88 ? 283 TYR A O 1 ATOM 1757 C CB . TYR A 1 270 ? -3.205 -14.860 27.973 1.00 138.68 ? 283 TYR A CB 1 ATOM 1758 C CG . TYR A 1 270 ? -2.489 -14.047 29.037 1.00 136.51 ? 283 TYR A CG 1 ATOM 1759 C CD1 . TYR A 1 270 ? -1.879 -12.835 28.741 1.00 137.43 ? 283 TYR A CD1 1 ATOM 1760 C CD2 . TYR A 1 270 ? -2.409 -14.505 30.343 1.00 137.78 ? 283 TYR A CD2 1 ATOM 1761 C CE1 . TYR A 1 270 ? -1.211 -12.105 29.727 1.00 130.87 ? 283 TYR A CE1 1 ATOM 1762 C CE2 . TYR A 1 270 ? -1.744 -13.785 31.329 1.00 133.57 ? 283 TYR A CE2 1 ATOM 1763 C CZ . TYR A 1 270 ? -1.147 -12.592 31.017 1.00 128.40 ? 283 TYR A CZ 1 ATOM 1764 O OH . TYR A 1 270 ? -0.489 -11.889 32.009 1.00 121.66 ? 283 TYR A OH 1 ATOM 1765 N N . LEU A 1 271 ? -3.765 -15.463 25.010 1.00 169.01 ? 284 LEU A N 1 ATOM 1766 C CA . LEU A 1 271 ? -4.208 -16.302 23.885 1.00 168.69 ? 284 LEU A CA 1 ATOM 1767 C C . LEU A 1 271 ? -3.643 -17.714 23.962 1.00 170.69 ? 284 LEU A C 1 ATOM 1768 O O . LEU A 1 271 ? -2.519 -17.921 24.419 1.00 169.20 ? 284 LEU A O 1 ATOM 1769 C CB . LEU A 1 271 ? -3.761 -15.695 22.553 1.00 163.83 ? 284 LEU A CB 1 ATOM 1770 C CG . LEU A 1 271 ? -4.137 -14.250 22.272 1.00 160.19 ? 284 LEU A CG 1 ATOM 1771 C CD1 . LEU A 1 271 ? -3.260 -13.672 21.168 1.00 158.63 ? 284 LEU A CD1 1 ATOM 1772 C CD2 . LEU A 1 271 ? -5.607 -14.182 21.922 1.00 163.70 ? 284 LEU A CD2 1 ATOM 1773 N N . PRO A 1 272 ? -4.421 -18.699 23.504 1.00 175.48 ? 285 PRO A N 1 ATOM 1774 C CA . PRO A 1 272 ? -3.850 -20.041 23.386 1.00 184.59 ? 285 PRO A CA 1 ATOM 1775 C C . PRO A 1 272 ? -2.801 -20.042 22.277 1.00 196.72 ? 285 PRO A C 1 ATOM 1776 O O . PRO A 1 272 ? -2.765 -19.101 21.483 1.00 201.94 ? 285 PRO A O 1 ATOM 1777 C CB . PRO A 1 272 ? -5.057 -20.904 22.997 1.00 187.06 ? 285 PRO A CB 1 ATOM 1778 C CG . PRO A 1 272 ? -6.019 -19.953 22.356 1.00 185.16 ? 285 PRO A CG 1 ATOM 1779 C CD . PRO A 1 272 ? -5.820 -18.635 23.046 1.00 178.61 ? 285 PRO A CD 1 ATOM 1780 N N . PRO A 1 273 ? -1.939 -21.068 22.229 1.00 201.27 ? 286 PRO A N 1 ATOM 1781 C CA . PRO A 1 273 ? -0.984 -21.164 21.121 1.00 202.50 ? 286 PRO A CA 1 ATOM 1782 C C . PRO A 1 273 ? -1.717 -21.363 19.792 1.00 201.78 ? 286 PRO A C 1 ATOM 1783 O O . PRO A 1 273 ? -2.896 -21.720 19.806 1.00 196.32 ? 286 PRO A O 1 ATOM 1784 C CB . PRO A 1 273 ? -0.163 -22.409 21.476 1.00 205.08 ? 286 PRO A CB 1 ATOM 1785 C CG . PRO A 1 273 ? -1.037 -23.193 22.394 1.00 205.62 ? 286 PRO A CG 1 ATOM 1786 C CD . PRO A 1 273 ? -1.772 -22.166 23.194 1.00 202.18 ? 286 PRO A CD 1 ATOM 1787 N N . PRO A 1 274 ? -1.028 -21.149 18.658 1.00 205.83 ? 287 PRO A N 1 ATOM 1788 C CA . PRO A 1 274 ? 0.398 -20.806 18.549 1.00 204.99 ? 287 PRO A CA 1 ATOM 1789 C C . PRO A 1 274 ? 0.727 -19.451 19.139 1.00 201.68 ? 287 PRO A C 1 ATOM 1790 O O . PRO A 1 274 ? 1.824 -19.270 19.670 1.00 200.68 ? 287 PRO A O 1 ATOM 1791 C CB . PRO A 1 274 ? 0.632 -20.761 17.039 1.00 205.39 ? 287 PRO A CB 1 ATOM 1792 C CG . PRO A 1 274 ? -0.442 -21.633 16.472 1.00 210.61 ? 287 PRO A CG 1 ATOM 1793 C CD . PRO A 1 274 ? -1.632 -21.376 17.336 1.00 208.81 ? 287 PRO A CD 1 ATOM 1794 N N . TRP A 1 275 ? -0.212 -18.516 19.041 1.00 198.40 ? 288 TRP A N 1 ATOM 1795 C CA . TRP A 1 275 ? 0.020 -17.160 19.509 1.00 189.21 ? 288 TRP A CA 1 ATOM 1796 C C . TRP A 1 275 ? 0.631 -17.150 20.902 1.00 185.98 ? 288 TRP A C 1 ATOM 1797 O O . TRP A 1 275 ? 1.795 -16.786 21.073 1.00 179.01 ? 288 TRP A O 1 ATOM 1798 C CB . TRP A 1 275 ? -1.287 -16.367 19.522 1.00 184.72 ? 288 TRP A CB 1 ATOM 1799 C CG . TRP A 1 275 ? -1.827 -16.009 18.156 1.00 187.83 ? 288 TRP A CG 1 ATOM 1800 C CD1 . TRP A 1 275 ? -1.278 -15.138 17.256 1.00 190.54 ? 288 TRP A CD1 1 ATOM 1801 C CD2 . TRP A 1 275 ? -3.041 -16.486 17.562 1.00 185.61 ? 288 TRP A CD2 1 ATOM 1802 N NE1 . TRP A 1 275 ? -2.067 -15.055 16.134 1.00 190.70 ? 288 TRP A NE1 1 ATOM 1803 C CE2 . TRP A 1 275 ? -3.155 -15.870 16.298 1.00 192.68 ? 288 TRP A CE2 1 ATOM 1804 C CE3 . TRP A 1 275 ? -4.037 -17.379 17.970 1.00 177.96 ? 288 TRP A CE3 1 ATOM 1805 C CZ2 . TRP A 1 275 ? -4.227 -16.124 15.445 1.00 197.49 ? 288 TRP A CZ2 1 ATOM 1806 C CZ3 . TRP A 1 275 ? -5.098 -17.625 17.128 1.00 176.18 ? 288 TRP A CZ3 1 ATOM 1807 C CH2 . TRP A 1 275 ? -5.186 -17.001 15.879 1.00 188.93 ? 288 TRP A CH2 1 ATOM 1808 N N . GLY A 1 276 ? -0.178 -17.531 21.889 1.00 196.20 ? 289 GLY A N 1 ATOM 1809 C CA . GLY A 1 276 ? 0.205 -17.490 23.295 1.00 199.62 ? 289 GLY A CA 1 ATOM 1810 C C . GLY A 1 276 ? 0.421 -18.807 24.027 1.00 202.62 ? 289 GLY A C 1 ATOM 1811 O O . GLY A 1 276 ? 0.257 -19.891 23.457 1.00 201.56 ? 289 GLY A O 1 ATOM 1812 N N . ASP A 1 277 ? 0.778 -18.699 25.309 1.00 204.77 ? 290 ASP A N 1 ATOM 1813 C CA . ASP A 1 277 ? 1.017 -19.865 26.166 1.00 206.34 ? 290 ASP A CA 1 ATOM 1814 C C . ASP A 1 277 ? -0.167 -20.280 27.057 1.00 195.42 ? 290 ASP A C 1 ATOM 1815 O O . ASP A 1 277 ? -0.133 -21.336 27.689 1.00 190.20 ? 290 ASP A O 1 ATOM 1816 C CB . ASP A 1 277 ? 2.236 -19.602 27.058 1.00 209.42 ? 290 ASP A CB 1 ATOM 1817 C CG . ASP A 1 277 ? 3.436 -19.090 26.281 1.00 217.09 ? 290 ASP A CG 1 ATOM 1818 O OD1 . ASP A 1 277 ? 3.585 -19.447 25.090 1.00 222.38 ? 290 ASP A OD1 1 ATOM 1819 O OD2 . ASP A 1 277 ? 4.231 -18.327 26.870 1.00 216.81 ? 290 ASP A OD2 1 ATOM 1820 N N . CYS A 1 278 ? -1.225 -19.478 27.072 1.00 188.58 ? 291 CYS A N 1 ATOM 1821 C CA . CYS A 1 278 ? -2.304 -19.669 28.034 1.00 178.61 ? 291 CYS A CA 1 ATOM 1822 C C . CYS A 1 278 ? -3.047 -20.970 27.793 1.00 184.98 ? 291 CYS A C 1 ATOM 1823 O O . CYS A 1 278 ? -2.868 -21.604 26.764 1.00 190.53 ? 291 CYS A O 1 ATOM 1824 C CB . CYS A 1 278 ? -3.281 -18.493 28.008 1.00 168.14 ? 291 CYS A CB 1 ATOM 1825 S SG . CYS A 1 278 ? -4.484 -18.597 26.687 1.00 206.60 ? 291 CYS A SG 1 ATOM 1826 N N . LYS A 1 279 ? -3.821 -21.402 28.783 1.00 189.43 ? 292 LYS A N 1 ATOM 1827 C CA . LYS A 1 279 ? -4.793 -22.475 28.590 1.00 200.30 ? 292 LYS A CA 1 ATOM 1828 C C . LYS A 1 279 ? -6.203 -22.011 28.957 1.00 208.29 ? 292 LYS A C 1 ATOM 1829 O O . LYS A 1 279 ? -6.476 -21.682 30.108 1.00 199.50 ? 292 LYS A O 1 ATOM 1830 C CB . LYS A 1 279 ? -4.410 -23.707 29.402 1.00 198.71 ? 292 LYS A CB 1 ATOM 1831 N N . ALA A 1 280 ? -7.109 -22.001 27.985 1.00 226.73 ? 293 ALA A N 1 ATOM 1832 C CA . ALA A 1 280 ? -8.481 -21.647 28.297 1.00 238.51 ? 293 ALA A CA 1 ATOM 1833 C C . ALA A 1 280 ? -9.208 -22.961 28.480 1.00 253.97 ? 293 ALA A C 1 ATOM 1834 O O . ALA A 1 280 ? -9.503 -23.669 27.515 1.00 259.52 ? 293 ALA A O 1 ATOM 1835 C CB . ALA A 1 280 ? -9.099 -20.842 27.166 1.00 238.53 ? 293 ALA A CB 1 ATOM 1836 N N . THR A 1 281 ? -9.499 -23.272 29.739 1.00 260.49 ? 294 THR A N 1 ATOM 1837 C CA . THR A 1 281 ? -10.067 -24.561 30.099 1.00 269.03 ? 294 THR A CA 1 ATOM 1838 C C . THR A 1 281 ? -11.163 -24.428 31.144 1.00 271.33 ? 294 THR A C 1 ATOM 1839 O O . THR A 1 281 ? -10.919 -23.967 32.257 1.00 270.10 ? 294 THR A O 1 ATOM 1840 C CB . THR A 1 281 ? -8.971 -25.499 30.599 1.00 269.45 ? 294 THR A CB 1 ATOM 1841 N N . THR A 1 282 ? -12.373 -24.828 30.776 1.00 275.11 ? 295 THR A N 1 ATOM 1842 C CA . THR A 1 282 ? -13.447 -25.001 31.744 1.00 274.65 ? 295 THR A CA 1 ATOM 1843 C C . THR A 1 282 ? -13.549 -26.478 32.135 1.00 274.07 ? 295 THR A C 1 ATOM 1844 O O . THR A 1 282 ? -14.392 -26.867 32.943 1.00 274.14 ? 295 THR A O 1 ATOM 1845 C CB . THR A 1 282 ? -14.797 -24.476 31.204 1.00 277.24 ? 295 THR A CB 1 ATOM 1846 O OG1 . THR A 1 282 ? -15.031 -25.002 29.892 1.00 283.52 ? 295 THR A OG1 1 ATOM 1847 C CG2 . THR A 1 282 ? -14.785 -22.954 31.133 1.00 271.75 ? 295 THR A CG2 1 ATOM 1848 N N . GLY A 1 283 ? -12.686 -27.300 31.543 1.00 271.27 ? 296 GLY A N 1 ATOM 1849 C CA . GLY A 1 283 ? -12.710 -28.735 31.761 1.00 267.55 ? 296 GLY A CA 1 ATOM 1850 C C . GLY A 1 283 ? -12.483 -29.123 33.209 1.00 263.81 ? 296 GLY A C 1 ATOM 1851 O O . GLY A 1 283 ? -13.065 -30.094 33.698 1.00 266.21 ? 296 GLY A O 1 ATOM 1852 N N . ASP A 1 284 ? -11.635 -28.356 33.894 1.00 254.92 ? 297 ASP A N 1 ATOM 1853 C CA . ASP A 1 284 ? -11.318 -28.605 35.304 1.00 244.00 ? 297 ASP A CA 1 ATOM 1854 C C . ASP A 1 284 ? -11.099 -30.081 35.618 1.00 238.60 ? 297 ASP A C 1 ATOM 1855 O O . ASP A 1 284 ? -11.892 -30.692 36.333 1.00 233.80 ? 297 ASP A O 1 ATOM 1856 C CB . ASP A 1 284 ? -12.403 -28.023 36.206 1.00 241.26 ? 297 ASP A CB 1 ATOM 1857 N N . ASP A 1 289 ? -15.292 -25.592 37.485 1.00 199.20 ? 302 ASP A N 1 ATOM 1858 C CA . ASP A 1 289 ? -15.883 -24.835 36.383 1.00 203.92 ? 302 ASP A CA 1 ATOM 1859 C C . ASP A 1 289 ? -14.811 -24.149 35.532 1.00 205.37 ? 302 ASP A C 1 ATOM 1860 O O . ASP A 1 289 ? -14.355 -24.714 34.537 1.00 210.44 ? 302 ASP A O 1 ATOM 1861 C CB . ASP A 1 289 ? -16.894 -23.817 36.908 1.00 202.31 ? 302 ASP A CB 1 ATOM 1862 N N . THR A 1 290 ? -14.409 -22.940 35.940 1.00 196.46 ? 303 THR A N 1 ATOM 1863 C CA . THR A 1 290 ? -13.404 -22.135 35.227 1.00 184.61 ? 303 THR A CA 1 ATOM 1864 C C . THR A 1 290 ? -11.989 -22.331 35.784 1.00 172.89 ? 303 THR A C 1 ATOM 1865 O O . THR A 1 290 ? -11.802 -22.540 36.986 1.00 168.01 ? 303 THR A O 1 ATOM 1866 C CB . THR A 1 290 ? -13.779 -20.658 35.249 1.00 180.38 ? 303 THR A CB 1 ATOM 1867 N N . TYR A 1 291 ? -10.994 -22.275 34.903 1.00 167.38 ? 304 TYR A N 1 ATOM 1868 C CA . TYR A 1 291 ? -9.623 -22.564 35.302 1.00 163.25 ? 304 TYR A CA 1 ATOM 1869 C C . TYR A 1 291 ? -8.935 -21.404 36.009 1.00 160.97 ? 304 TYR A C 1 ATOM 1870 O O . TYR A 1 291 ? -8.992 -20.255 35.573 1.00 163.25 ? 304 TYR A O 1 ATOM 1871 C CB . TYR A 1 291 ? -8.771 -23.002 34.112 1.00 164.50 ? 304 TYR A CB 1 ATOM 1872 C CG . TYR A 1 291 ? -7.301 -23.099 34.451 1.00 164.44 ? 304 TYR A CG 1 ATOM 1873 C CD1 . TYR A 1 291 ? -6.845 -24.042 35.356 1.00 162.38 ? 304 TYR A CD1 1 ATOM 1874 C CD2 . TYR A 1 291 ? -6.371 -22.240 33.873 1.00 168.71 ? 304 TYR A CD2 1 ATOM 1875 C CE1 . TYR A 1 291 ? -5.505 -24.132 35.679 1.00 166.35 ? 304 TYR A CE1 1 ATOM 1876 C CE2 . TYR A 1 291 ? -5.021 -22.324 34.188 1.00 167.65 ? 304 TYR A CE2 1 ATOM 1877 C CZ . TYR A 1 291 ? -4.595 -23.272 35.094 1.00 167.78 ? 304 TYR A CZ 1 ATOM 1878 O OH . TYR A 1 291 ? -3.256 -23.359 35.417 1.00 166.72 ? 304 TYR A OH 1 ATOM 1879 N N . SER A 1 292 ? -8.262 -21.733 37.098 1.00 152.57 ? 305 SER A N 1 ATOM 1880 C CA . SER A 1 292 ? -7.572 -20.755 37.903 1.00 147.25 ? 305 SER A CA 1 ATOM 1881 C C . SER A 1 292 ? -6.220 -21.306 38.341 1.00 147.12 ? 305 SER A C 1 ATOM 1882 O O . SER A 1 292 ? -6.058 -22.508 38.543 1.00 140.19 ? 305 SER A O 1 ATOM 1883 C CB . SER A 1 292 ? -8.427 -20.413 39.124 1.00 152.48 ? 305 SER A CB 1 ATOM 1884 O OG . SER A 1 292 ? -7.659 -20.383 40.313 1.00 153.38 ? 305 SER A OG 1 ATOM 1885 N N . ILE A 1 293 ? -5.236 -20.430 38.481 1.00 156.37 ? 306 ILE A N 1 ATOM 1886 C CA . ILE A 1 293 ? -3.977 -20.836 39.086 1.00 160.19 ? 306 ILE A CA 1 ATOM 1887 C C . ILE A 1 293 ? -4.216 -21.407 40.490 1.00 157.49 ? 306 ILE A C 1 ATOM 1888 O O . ILE A 1 293 ? -3.890 -22.569 40.744 1.00 155.05 ? 306 ILE A O 1 ATOM 1889 C CB . ILE A 1 293 ? -2.967 -19.678 39.149 1.00 158.02 ? 306 ILE A CB 1 ATOM 1890 C CG1 . ILE A 1 293 ? -2.387 -19.403 37.764 1.00 154.56 ? 306 ILE A CG1 1 ATOM 1891 C CG2 . ILE A 1 293 ? -1.829 -20.031 40.085 1.00 163.63 ? 306 ILE A CG2 1 ATOM 1892 C CD1 . ILE A 1 293 ? -1.343 -20.415 37.326 1.00 156.08 ? 306 ILE A CD1 1 ATOM 1893 N N . THR A 1 294 ? -4.804 -20.609 41.389 1.00 152.71 ? 307 THR A N 1 ATOM 1894 C CA . THR A 1 294 ? -5.114 -21.105 42.731 1.00 145.38 ? 307 THR A CA 1 ATOM 1895 C C . THR A 1 294 ? -5.882 -22.409 42.590 1.00 139.11 ? 307 THR A C 1 ATOM 1896 O O . THR A 1 294 ? -5.675 -23.348 43.355 1.00 139.89 ? 307 THR A O 1 ATOM 1897 C CB . THR A 1 294 ? -5.954 -20.116 43.573 1.00 145.88 ? 307 THR A CB 1 ATOM 1898 O OG1 . THR A 1 294 ? -5.207 -18.918 43.817 1.00 145.69 ? 307 THR A OG1 1 ATOM 1899 C CG2 . THR A 1 294 ? -6.303 -20.743 44.904 1.00 144.60 ? 307 THR A CG2 1 ATOM 1900 N N . ALA A 1 295 ? -6.760 -22.457 41.592 1.00 131.59 ? 308 ALA A N 1 ATOM 1901 C CA . ALA A 1 295 ? -7.531 -23.653 41.279 1.00 131.44 ? 308 ALA A CA 1 ATOM 1902 C C . ALA A 1 295 ? -6.670 -24.882 40.989 1.00 141.81 ? 308 ALA A C 1 ATOM 1903 O O . ALA A 1 295 ? -6.778 -25.893 41.685 1.00 152.71 ? 308 ALA A O 1 ATOM 1904 C CB . ALA A 1 295 ? -8.488 -23.390 40.152 1.00 131.28 ? 308 ALA A CB 1 ATOM 1905 N N . CYS A 1 296 ? -5.845 -24.819 39.948 1.00 138.58 ? 309 CYS A N 1 ATOM 1906 C CA . CYS A 1 296 ? -4.957 -25.943 39.651 1.00 141.85 ? 309 CYS A CA 1 ATOM 1907 C C . CYS A 1 296 ? -3.974 -26.125 40.799 1.00 138.72 ? 309 CYS A C 1 ATOM 1908 O O . CYS A 1 296 ? -3.630 -27.234 41.182 1.00 137.96 ? 309 CYS A O 1 ATOM 1909 C CB . CYS A 1 296 ? -4.191 -25.705 38.358 1.00 140.93 ? 309 CYS A CB 1 ATOM 1910 S SG . CYS A 1 296 ? -2.908 -24.459 38.506 1.00 289.55 ? 309 CYS A SG 1 ATOM 1911 N N . ARG A 1 297 ? -3.535 -25.012 41.359 1.00 138.02 ? 310 ARG A N 1 ATOM 1912 C CA . ARG A 1 297 ? -2.574 -25.050 42.439 1.00 145.30 ? 310 ARG A CA 1 ATOM 1913 C C . ARG A 1 297 ? -3.097 -25.868 43.609 1.00 148.97 ? 310 ARG A C 1 ATOM 1914 O O . ARG A 1 297 ? -2.318 -26.506 44.310 1.00 154.53 ? 310 ARG A O 1 ATOM 1915 C CB . ARG A 1 297 ? -2.213 -23.625 42.882 1.00 149.16 ? 310 ARG A CB 1 ATOM 1916 C CG . ARG A 1 297 ? -1.143 -23.535 43.972 1.00 147.44 ? 310 ARG A CG 1 ATOM 1917 C CD . ARG A 1 297 ? 0.125 -22.848 43.483 1.00 143.07 ? 310 ARG A CD 1 ATOM 1918 N NE . ARG A 1 297 ? 1.087 -22.649 44.566 1.00 143.06 ? 310 ARG A NE 1 ATOM 1919 C CZ . ARG A 1 297 ? 1.305 -21.476 45.152 1.00 136.75 ? 310 ARG A CZ 1 ATOM 1920 N NH1 . ARG A 1 297 ? 2.197 -21.358 46.142 1.00 119.20 ? 310 ARG A NH1 1 ATOM 1921 N NH2 . ARG A 1 297 ? 0.625 -20.416 44.732 1.00 141.84 ? 310 ARG A NH2 1 ATOM 1922 N N . ILE A 1 298 ? -4.408 -25.854 43.830 1.00 150.27 ? 311 ILE A N 1 ATOM 1923 C CA . ILE A 1 298 ? -4.964 -26.550 44.992 1.00 157.21 ? 311 ILE A CA 1 ATOM 1924 C C . ILE A 1 298 ? -5.071 -28.073 44.850 1.00 157.99 ? 311 ILE A C 1 ATOM 1925 O O . ILE A 1 298 ? -4.608 -28.807 45.721 1.00 156.89 ? 311 ILE A O 1 ATOM 1926 C CB . ILE A 1 298 ? -6.326 -25.983 45.433 1.00 159.67 ? 311 ILE A CB 1 ATOM 1927 C CG1 . ILE A 1 298 ? -6.176 -24.543 45.904 1.00 156.48 ? 311 ILE A CG1 1 ATOM 1928 C CG2 . ILE A 1 298 ? -6.891 -26.801 46.575 1.00 160.24 ? 311 ILE A CG2 1 ATOM 1929 C CD1 . ILE A 1 298 ? -7.448 -23.941 46.436 1.00 156.65 ? 311 ILE A CD1 1 ATOM 1930 N N . ASP A 1 299 ? -5.663 -28.557 43.761 1.00 157.63 ? 312 ASP A N 1 ATOM 1931 C CA . ASP A 1 299 ? -5.823 -30.007 43.615 1.00 164.88 ? 312 ASP A CA 1 ATOM 1932 C C . ASP A 1 299 ? -4.466 -30.682 43.456 1.00 160.85 ? 312 ASP A C 1 ATOM 1933 O O . ASP A 1 299 ? -4.338 -31.889 43.643 1.00 159.00 ? 312 ASP A O 1 ATOM 1934 C CB . ASP A 1 299 ? -6.811 -30.387 42.490 1.00 175.12 ? 312 ASP A CB 1 ATOM 1935 C CG . ASP A 1 299 ? -6.232 -30.212 41.090 1.00 180.01 ? 312 ASP A CG 1 ATOM 1936 O OD1 . ASP A 1 299 ? -5.151 -30.773 40.823 1.00 181.23 ? 312 ASP A OD1 1 ATOM 1937 O OD2 . ASP A 1 299 ? -6.871 -29.532 40.249 1.00 180.85 ? 312 ASP A OD2 1 ATOM 1938 N N . CYS A 1 300 ? -3.459 -29.879 43.126 1.00 159.93 ? 313 CYS A N 1 ATOM 1939 C CA . CYS A 1 300 ? -2.082 -30.342 43.028 1.00 162.18 ? 313 CYS A CA 1 ATOM 1940 C C . CYS A 1 300 ? -1.550 -30.657 44.415 1.00 162.12 ? 313 CYS A C 1 ATOM 1941 O O . CYS A 1 300 ? -0.661 -31.478 44.581 1.00 168.70 ? 313 CYS A O 1 ATOM 1942 C CB . CYS A 1 300 ? -1.212 -29.264 42.390 1.00 163.05 ? 313 CYS A CB 1 ATOM 1943 S SG . CYS A 1 300 ? 0.162 -29.872 41.392 1.00 182.68 ? 313 CYS A SG 1 ATOM 1944 N N . GLU A 1 301 ? -2.077 -29.969 45.413 1.00 159.17 ? 314 GLU A N 1 ATOM 1945 C CA . GLU A 1 301 ? -1.780 -30.298 46.794 1.00 158.89 ? 314 GLU A CA 1 ATOM 1946 C C . GLU A 1 301 ? -2.676 -31.455 47.211 1.00 157.52 ? 314 GLU A C 1 ATOM 1947 O O . GLU A 1 301 ? -2.270 -32.313 47.991 1.00 157.39 ? 314 GLU A O 1 ATOM 1948 C CB . GLU A 1 301 ? -2.009 -29.077 47.680 1.00 162.39 ? 314 GLU A CB 1 ATOM 1949 C CG . GLU A 1 301 ? -1.307 -27.828 47.151 1.00 169.24 ? 314 GLU A CG 1 ATOM 1950 C CD . GLU A 1 301 ? -1.798 -26.552 47.797 1.00 168.76 ? 314 GLU A CD 1 ATOM 1951 O OE1 . GLU A 1 301 ? -2.988 -26.508 48.182 1.00 170.83 ? 314 GLU A OE1 1 ATOM 1952 O OE2 . GLU A 1 301 ? -0.990 -25.602 47.920 1.00 164.19 ? 314 GLU A OE2 1 ATOM 1953 N N . THR A 1 302 ? -3.892 -31.476 46.667 1.00 156.24 ? 315 THR A N 1 ATOM 1954 C CA . THR A 1 302 ? -4.854 -32.533 46.962 1.00 155.40 ? 315 THR A CA 1 ATOM 1955 C C . THR A 1 302 ? -4.302 -33.888 46.514 1.00 161.90 ? 315 THR A C 1 ATOM 1956 O O . THR A 1 302 ? -4.072 -34.775 47.346 1.00 162.42 ? 315 THR A O 1 ATOM 1957 C CB . THR A 1 302 ? -6.199 -32.266 46.258 1.00 148.78 ? 315 THR A CB 1 ATOM 1958 O OG1 . THR A 1 302 ? -6.593 -30.914 46.490 1.00 146.15 ? 315 THR A OG1 1 ATOM 1959 C CG2 . THR A 1 302 ? -7.282 -33.179 46.784 1.00 146.08 ? 315 THR A CG2 1 ATOM 1960 N N . ARG A 1 303 ? -4.041 -34.023 45.211 1.00 160.04 ? 316 ARG A N 1 ATOM 1961 C CA . ARG A 1 303 ? -3.461 -35.248 44.653 1.00 155.54 ? 316 ARG A CA 1 ATOM 1962 C C . ARG A 1 303 ? -2.215 -35.685 45.433 1.00 165.47 ? 316 ARG A C 1 ATOM 1963 O O . ARG A 1 303 ? -2.080 -36.840 45.822 1.00 168.70 ? 316 ARG A O 1 ATOM 1964 C CB . ARG A 1 303 ? -3.136 -35.067 43.158 1.00 141.77 ? 316 ARG A CB 1 ATOM 1965 N N . TYR A 1 304 ? -1.316 -34.739 45.667 1.00 171.74 ? 317 TYR A N 1 ATOM 1966 C CA . TYR A 1 304 ? -0.052 -34.998 46.343 1.00 173.86 ? 317 TYR A CA 1 ATOM 1967 C C . TYR A 1 304 ? -0.240 -35.392 47.802 1.00 175.53 ? 317 TYR A C 1 ATOM 1968 O O . TYR A 1 304 ? 0.370 -36.351 48.270 1.00 178.50 ? 317 TYR A O 1 ATOM 1969 C CB . TYR A 1 304 ? 0.831 -33.755 46.257 1.00 167.39 ? 317 TYR A CB 1 ATOM 1970 C CG . TYR A 1 304 ? 2.220 -33.914 46.822 1.00 159.59 ? 317 TYR A CG 1 ATOM 1971 C CD1 . TYR A 1 304 ? 3.279 -34.269 46.011 1.00 158.66 ? 317 TYR A CD1 1 ATOM 1972 C CD2 . TYR A 1 304 ? 2.475 -33.687 48.159 1.00 155.81 ? 317 TYR A CD2 1 ATOM 1973 C CE1 . TYR A 1 304 ? 4.553 -34.401 46.516 1.00 157.84 ? 317 TYR A CE1 1 ATOM 1974 C CE2 . TYR A 1 304 ? 3.751 -33.817 48.675 1.00 157.63 ? 317 TYR A CE2 1 ATOM 1975 C CZ . TYR A 1 304 ? 4.787 -34.175 47.848 1.00 157.87 ? 317 TYR A CZ 1 ATOM 1976 O OH . TYR A 1 304 ? 6.062 -34.306 48.355 1.00 157.27 ? 317 TYR A OH 1 ATOM 1977 N N . LEU A 1 305 ? -1.066 -34.647 48.529 1.00 173.80 ? 318 LEU A N 1 ATOM 1978 C CA . LEU A 1 305 ? -1.305 -34.960 49.935 1.00 172.78 ? 318 LEU A CA 1 ATOM 1979 C C . LEU A 1 305 ? -1.954 -36.339 50.065 1.00 179.61 ? 318 LEU A C 1 ATOM 1980 O O . LEU A 1 305 ? -1.520 -37.173 50.872 1.00 183.76 ? 318 LEU A O 1 ATOM 1981 C CB . LEU A 1 305 ? -2.172 -33.886 50.592 1.00 160.78 ? 318 LEU A CB 1 ATOM 1982 N N . VAL A 1 306 ? -2.992 -36.575 49.266 1.00 173.14 ? 319 VAL A N 1 ATOM 1983 C CA . VAL A 1 306 ? -3.642 -37.881 49.227 1.00 167.76 ? 319 VAL A CA 1 ATOM 1984 C C . VAL A 1 306 ? -2.616 -38.978 49.001 1.00 167.89 ? 319 VAL A C 1 ATOM 1985 O O . VAL A 1 306 ? -2.335 -39.780 49.894 1.00 164.37 ? 319 VAL A O 1 ATOM 1986 C CB . VAL A 1 306 ? -4.733 -37.947 48.137 1.00 165.22 ? 319 VAL A CB 1 ATOM 1987 C CG1 . VAL A 1 306 ? -5.139 -39.384 47.863 1.00 153.78 ? 319 VAL A CG1 1 ATOM 1988 C CG2 . VAL A 1 306 ? -5.942 -37.105 48.566 1.00 170.73 ? 319 VAL A CG2 1 ATOM 1989 N N . GLU A 1 307 ? -2.029 -38.966 47.810 1.00 172.19 ? 320 GLU A N 1 ATOM 1990 C CA . GLU A 1 307 ? -0.986 -39.910 47.427 1.00 175.15 ? 320 GLU A CA 1 ATOM 1991 C C . GLU A 1 307 ? 0.078 -40.136 48.522 1.00 179.00 ? 320 GLU A C 1 ATOM 1992 O O . GLU A 1 307 ? 0.204 -41.239 49.036 1.00 179.90 ? 320 GLU A O 1 ATOM 1993 C CB . GLU A 1 307 ? -0.361 -39.434 46.117 1.00 173.51 ? 320 GLU A CB 1 ATOM 1994 C CG . GLU A 1 307 ? 1.070 -39.835 45.892 1.00 179.59 ? 320 GLU A CG 1 ATOM 1995 C CD . GLU A 1 307 ? 1.644 -39.184 44.652 1.00 187.56 ? 320 GLU A CD 1 ATOM 1996 O OE1 . GLU A 1 307 ? 2.856 -38.869 44.644 1.00 189.66 ? 320 GLU A OE1 1 ATOM 1997 O OE2 . GLU A 1 307 ? 0.874 -38.983 43.685 1.00 191.18 ? 320 GLU A OE2 1 ATOM 1998 N N . ASN A 1 308 ? 0.837 -39.105 48.880 1.00 185.15 ? 321 ASN A N 1 ATOM 1999 C CA . ASN A 1 308 ? 1.930 -39.274 49.837 1.00 189.67 ? 321 ASN A CA 1 ATOM 2000 C C . ASN A 1 308 ? 1.486 -39.566 51.275 1.00 189.37 ? 321 ASN A C 1 ATOM 2001 O O . ASN A 1 308 ? 2.208 -40.221 52.028 1.00 187.58 ? 321 ASN A O 1 ATOM 2002 C CB . ASN A 1 308 ? 2.888 -38.075 49.793 1.00 188.58 ? 321 ASN A CB 1 ATOM 2003 C CG . ASN A 1 308 ? 4.347 -38.498 49.811 1.00 191.08 ? 321 ASN A CG 1 ATOM 2004 O OD1 . ASN A 1 308 ? 4.764 -39.277 50.666 1.00 199.13 ? 321 ASN A OD1 1 ATOM 2005 N ND2 . ASN A 1 308 ? 5.123 -38.012 48.845 1.00 183.47 ? 321 ASN A ND2 1 ATOM 2006 N N . CYS A 1 309 ? 0.322 -39.057 51.668 1.00 191.83 ? 322 CYS A N 1 ATOM 2007 C CA . CYS A 1 309 ? -0.194 -39.317 53.016 1.00 198.32 ? 322 CYS A CA 1 ATOM 2008 C C . CYS A 1 309 ? -1.272 -40.408 53.145 1.00 207.75 ? 322 CYS A C 1 ATOM 2009 O O . CYS A 1 309 ? -1.653 -40.780 54.262 1.00 211.20 ? 322 CYS A O 1 ATOM 2010 C CB . CYS A 1 309 ? -0.691 -38.012 53.649 1.00 191.57 ? 322 CYS A CB 1 ATOM 2011 S SG . CYS A 1 309 ? 0.589 -36.754 53.750 1.00 420.15 ? 322 CYS A SG 1 ATOM 2012 N N . ASN A 1 310 ? -1.734 -40.943 52.018 1.00 187.31 ? 323 ASN A N 1 ATOM 2013 C CA . ASN A 1 310 ? -2.933 -41.789 52.013 1.00 190.21 ? 323 ASN A CA 1 ATOM 2014 C C . ASN A 1 310 ? -4.079 -41.134 52.790 1.00 189.02 ? 323 ASN A C 1 ATOM 2015 O O . ASN A 1 310 ? -4.851 -41.812 53.476 1.00 193.10 ? 323 ASN A O 1 ATOM 2016 C CB . ASN A 1 310 ? -2.644 -43.207 52.531 1.00 192.47 ? 323 ASN A CB 1 ATOM 2017 C CG . ASN A 1 310 ? -1.964 -44.095 51.481 1.00 189.46 ? 323 ASN A CG 1 ATOM 2018 O OD1 . ASN A 1 310 ? -2.283 -44.032 50.287 1.00 186.01 ? 323 ASN A OD1 1 ATOM 2019 N ND2 . ASN A 1 310 ? -1.023 -44.923 51.928 1.00 185.64 ? 323 ASN A ND2 1 ATOM 2020 N N . CYS A 1 311 ? -4.156 -39.807 52.675 1.00 179.30 ? 324 CYS A N 1 ATOM 2021 C CA . CYS A 1 311 ? -5.215 -39.003 53.272 1.00 169.64 ? 324 CYS A CA 1 ATOM 2022 C C . CYS A 1 311 ? -5.347 -37.649 52.581 1.00 162.89 ? 324 CYS A C 1 ATOM 2023 O O . CYS A 1 311 ? -4.393 -37.152 51.992 1.00 154.24 ? 324 CYS A O 1 ATOM 2024 C CB . CYS A 1 311 ? -4.907 -38.765 54.746 1.00 170.56 ? 324 CYS A CB 1 ATOM 2025 S SG . CYS A 1 311 ? -5.647 -37.267 55.421 1.00 194.24 ? 324 CYS A SG 1 ATOM 2026 N N . ARG A 1 312 ? -6.526 -37.040 52.693 1.00 167.68 ? 325 ARG A N 1 ATOM 2027 C CA . ARG A 1 312 ? -6.738 -35.663 52.261 1.00 164.41 ? 325 ARG A CA 1 ATOM 2028 C C . ARG A 1 312 ? -6.943 -34.784 53.489 1.00 168.02 ? 325 ARG A C 1 ATOM 2029 O O . ARG A 1 312 ? -7.499 -35.226 54.494 1.00 170.02 ? 325 ARG A O 1 ATOM 2030 C CB . ARG A 1 312 ? -7.968 -35.558 51.360 1.00 159.86 ? 325 ARG A CB 1 ATOM 2031 C CG . ARG A 1 312 ? -9.233 -35.104 52.090 1.00 154.16 ? 325 ARG A CG 1 ATOM 2032 C CD . ARG A 1 312 ? -10.463 -35.313 51.238 1.00 155.71 ? 325 ARG A CD 1 ATOM 2033 N NE . ARG A 1 312 ? -11.510 -34.351 51.545 1.00 159.26 ? 325 ARG A NE 1 ATOM 2034 C CZ . ARG A 1 312 ? -12.810 -34.594 51.404 1.00 159.91 ? 325 ARG A CZ 1 ATOM 2035 N NH1 . ARG A 1 312 ? -13.217 -35.777 50.969 1.00 160.03 ? 325 ARG A NH1 1 ATOM 2036 N NH2 . ARG A 1 312 ? -13.702 -33.657 51.703 1.00 154.78 ? 325 ARG A NH2 1 ATOM 2037 N N . MET A 1 313 ? -6.494 -33.537 53.393 1.00 166.27 ? 326 MET A N 1 ATOM 2038 C CA . MET A 1 313 ? -6.584 -32.576 54.488 1.00 167.24 ? 326 MET A CA 1 ATOM 2039 C C . MET A 1 313 ? -7.897 -31.792 54.422 1.00 164.49 ? 326 MET A C 1 ATOM 2040 O O . MET A 1 313 ? -8.341 -31.424 53.337 1.00 162.47 ? 326 MET A O 1 ATOM 2041 C CB . MET A 1 313 ? -5.388 -31.631 54.412 1.00 169.01 ? 326 MET A CB 1 ATOM 2042 C CG . MET A 1 313 ? -5.005 -30.979 55.720 1.00 168.49 ? 326 MET A CG 1 ATOM 2043 S SD . MET A 1 313 ? -3.756 -29.709 55.491 1.00 178.81 ? 326 MET A SD 1 ATOM 2044 C CE . MET A 1 313 ? -2.265 -30.667 55.301 1.00 80.28 ? 326 MET A CE 1 ATOM 2045 N N . VAL A 1 314 ? -8.476 -31.485 55.581 1.00 166.11 ? 327 VAL A N 1 ATOM 2046 C CA . VAL A 1 314 ? -9.857 -30.979 55.679 1.00 167.68 ? 327 VAL A CA 1 ATOM 2047 C C . VAL A 1 314 ? -10.279 -29.882 54.698 1.00 158.32 ? 327 VAL A C 1 ATOM 2048 O O . VAL A 1 314 ? -11.428 -29.840 54.274 1.00 163.05 ? 327 VAL A O 1 ATOM 2049 C CB . VAL A 1 314 ? -10.163 -30.434 57.086 1.00 169.32 ? 327 VAL A CB 1 ATOM 2050 C CG1 . VAL A 1 314 ? -10.050 -31.546 58.131 1.00 174.27 ? 327 VAL A CG1 1 ATOM 2051 C CG2 . VAL A 1 314 ? -9.236 -29.263 57.398 1.00 165.85 ? 327 VAL A CG2 1 ATOM 2052 N N . HIS A 1 315 ? -9.386 -28.961 54.381 1.00 143.99 ? 328 HIS A N 1 ATOM 2053 C CA . HIS A 1 315 ? -9.773 -27.867 53.517 1.00 146.65 ? 328 HIS A CA 1 ATOM 2054 C C . HIS A 1 315 ? -9.600 -28.240 52.051 1.00 156.91 ? 328 HIS A C 1 ATOM 2055 O O . HIS A 1 315 ? -9.845 -27.421 51.162 1.00 162.81 ? 328 HIS A O 1 ATOM 2056 C CB . HIS A 1 315 ? -8.970 -26.617 53.855 1.00 148.51 ? 328 HIS A CB 1 ATOM 2057 C CG . HIS A 1 315 ? -7.493 -26.804 53.733 1.00 151.04 ? 328 HIS A CG 1 ATOM 2058 N ND1 . HIS A 1 315 ? -6.863 -26.970 52.517 1.00 152.73 ? 328 HIS A ND1 1 ATOM 2059 C CD2 . HIS A 1 315 ? -6.524 -26.867 54.671 1.00 155.63 ? 328 HIS A CD2 1 ATOM 2060 C CE1 . HIS A 1 315 ? -5.566 -27.122 52.715 1.00 156.92 ? 328 HIS A CE1 1 ATOM 2061 N NE2 . HIS A 1 315 ? -5.334 -27.063 54.014 1.00 158.74 ? 328 HIS A NE2 1 ATOM 2062 N N . MET A 1 316 ? -9.159 -29.470 51.802 1.00 160.56 ? 329 MET A N 1 ATOM 2063 C CA . MET A 1 316 ? -9.036 -29.983 50.437 1.00 168.96 ? 329 MET A CA 1 ATOM 2064 C C . MET A 1 316 ? -10.306 -30.668 49.955 1.00 179.70 ? 329 MET A C 1 ATOM 2065 O O . MET A 1 316 ? -11.024 -31.294 50.735 1.00 185.54 ? 329 MET A O 1 ATOM 2066 C CB . MET A 1 316 ? -7.873 -30.965 50.319 1.00 170.38 ? 329 MET A CB 1 ATOM 2067 C CG . MET A 1 316 ? -6.519 -30.322 50.274 1.00 165.76 ? 329 MET A CG 1 ATOM 2068 S SD . MET A 1 316 ? -5.313 -31.379 51.068 1.00 160.70 ? 329 MET A SD 1 ATOM 2069 C CE . MET A 1 316 ? -3.870 -30.952 50.128 1.00 122.08 ? 329 MET A CE 1 ATOM 2070 N N . PRO A 1 317 ? -10.572 -30.568 48.650 1.00 181.88 ? 330 PRO A N 1 ATOM 2071 C CA . PRO A 1 317 ? -11.757 -31.145 48.014 1.00 190.48 ? 330 PRO A CA 1 ATOM 2072 C C . PRO A 1 317 ? -11.622 -32.655 47.814 1.00 202.11 ? 330 PRO A C 1 ATOM 2073 O O . PRO A 1 317 ? -10.659 -33.244 48.308 1.00 204.72 ? 330 PRO A O 1 ATOM 2074 C CB . PRO A 1 317 ? -11.779 -30.442 46.662 1.00 186.21 ? 330 PRO A CB 1 ATOM 2075 C CG . PRO A 1 317 ? -10.342 -30.212 46.366 1.00 180.98 ? 330 PRO A CG 1 ATOM 2076 C CD . PRO A 1 317 ? -9.707 -29.879 47.678 1.00 177.54 ? 330 PRO A CD 1 ATOM 2077 N N . GLY A 1 318 ? -12.580 -33.260 47.112 1.00 207.82 ? 331 GLY A N 1 ATOM 2078 C CA . GLY A 1 318 ? -12.513 -34.668 46.749 1.00 212.88 ? 331 GLY A CA 1 ATOM 2079 C C . GLY A 1 318 ? -13.361 -35.578 47.622 1.00 216.72 ? 331 GLY A C 1 ATOM 2080 O O . GLY A 1 318 ? -14.014 -35.122 48.560 1.00 219.60 ? 331 GLY A O 1 ATOM 2081 N N . ASP A 1 319 ? -13.363 -36.868 47.295 1.00 216.08 ? 332 ASP A N 1 ATOM 2082 C CA . ASP A 1 319 ? -14.098 -37.874 48.061 1.00 212.92 ? 332 ASP A CA 1 ATOM 2083 C C . ASP A 1 319 ? -13.245 -38.580 49.123 1.00 207.32 ? 332 ASP A C 1 ATOM 2084 O O . ASP A 1 319 ? -13.771 -39.329 49.942 1.00 211.55 ? 332 ASP A O 1 ATOM 2085 C CB . ASP A 1 319 ? -14.722 -38.902 47.113 1.00 217.36 ? 332 ASP A CB 1 ATOM 2086 C CG . ASP A 1 319 ? -14.037 -38.931 45.757 1.00 220.11 ? 332 ASP A CG 1 ATOM 2087 O OD1 . ASP A 1 319 ? -13.098 -39.738 45.577 1.00 220.76 ? 332 ASP A OD1 1 ATOM 2088 O OD2 . ASP A 1 319 ? -14.435 -38.140 44.871 1.00 220.58 ? 332 ASP A OD2 1 ATOM 2089 N N . ALA A 1 320 ? -11.940 -38.317 49.118 1.00 195.96 ? 333 ALA A N 1 ATOM 2090 C CA . ALA A 1 320 ? -10.968 -39.054 49.939 1.00 187.01 ? 333 ALA A CA 1 ATOM 2091 C C . ALA A 1 320 ? -11.107 -38.850 51.464 1.00 185.10 ? 333 ALA A C 1 ATOM 2092 O O . ALA A 1 320 ? -11.884 -38.007 51.920 1.00 185.32 ? 333 ALA A O 1 ATOM 2093 C CB . ALA A 1 320 ? -9.551 -38.752 49.468 1.00 177.98 ? 333 ALA A CB 1 ATOM 2094 N N . PRO A 1 321 ? -10.380 -39.656 52.261 1.00 178.73 ? 334 PRO A N 1 ATOM 2095 C CA . PRO A 1 321 ? -10.520 -39.616 53.722 1.00 176.80 ? 334 PRO A CA 1 ATOM 2096 C C . PRO A 1 321 ? -9.894 -38.376 54.340 1.00 180.48 ? 334 PRO A C 1 ATOM 2097 O O . PRO A 1 321 ? -8.978 -37.787 53.770 1.00 183.80 ? 334 PRO A O 1 ATOM 2098 C CB . PRO A 1 321 ? -9.720 -40.837 54.166 1.00 176.91 ? 334 PRO A CB 1 ATOM 2099 C CG . PRO A 1 321 ? -8.641 -40.935 53.151 1.00 174.76 ? 334 PRO A CG 1 ATOM 2100 C CD . PRO A 1 321 ? -9.272 -40.536 51.847 1.00 173.14 ? 334 PRO A CD 1 ATOM 2101 N N . TYR A 1 322 ? -10.392 -37.980 55.503 1.00 181.46 ? 335 TYR A N 1 ATOM 2102 C CA . TYR A 1 322 ? -9.784 -36.886 56.252 1.00 176.94 ? 335 TYR A CA 1 ATOM 2103 C C . TYR A 1 322 ? -8.581 -37.365 57.039 1.00 178.77 ? 335 TYR A C 1 ATOM 2104 O O . TYR A 1 322 ? -8.492 -38.537 57.396 1.00 192.44 ? 335 TYR A O 1 ATOM 2105 C CB . TYR A 1 322 ? -10.807 -36.228 57.173 1.00 171.17 ? 335 TYR A CB 1 ATOM 2106 C CG . TYR A 1 322 ? -11.761 -35.367 56.402 1.00 168.82 ? 335 TYR A CG 1 ATOM 2107 C CD1 . TYR A 1 322 ? -11.371 -34.797 55.192 1.00 165.40 ? 335 TYR A CD1 1 ATOM 2108 C CD2 . TYR A 1 322 ? -13.051 -35.135 56.858 1.00 170.73 ? 335 TYR A CD2 1 ATOM 2109 C CE1 . TYR A 1 322 ? -12.233 -34.007 54.462 1.00 163.62 ? 335 TYR A CE1 1 ATOM 2110 C CE2 . TYR A 1 322 ? -13.929 -34.346 56.131 1.00 171.09 ? 335 TYR A CE2 1 ATOM 2111 C CZ . TYR A 1 322 ? -13.512 -33.783 54.934 1.00 170.09 ? 335 TYR A CZ 1 ATOM 2112 O OH . TYR A 1 322 ? -14.377 -32.994 54.211 1.00 173.18 ? 335 TYR A OH 1 ATOM 2113 N N . CYS A 1 323 ? -7.647 -36.463 57.305 1.00 162.33 ? 336 CYS A N 1 ATOM 2114 C CA . CYS A 1 323 ? -6.479 -36.844 58.070 1.00 152.23 ? 336 CYS A CA 1 ATOM 2115 C C . CYS A 1 323 ? -6.808 -36.911 59.550 1.00 148.64 ? 336 CYS A C 1 ATOM 2116 O O . CYS A 1 323 ? -7.918 -36.574 59.979 1.00 140.61 ? 336 CYS A O 1 ATOM 2117 C CB . CYS A 1 323 ? -5.333 -35.865 57.833 1.00 144.86 ? 336 CYS A CB 1 ATOM 2118 S SG . CYS A 1 323 ? -4.191 -36.399 56.565 1.00 225.96 ? 336 CYS A SG 1 ATOM 2119 N N . THR A 1 324 ? -5.823 -37.342 60.325 1.00 150.42 ? 337 THR A N 1 ATOM 2120 C CA . THR A 1 324 ? -5.936 -37.332 61.767 1.00 157.66 ? 337 THR A CA 1 ATOM 2121 C C . THR A 1 324 ? -4.759 -36.555 62.325 1.00 150.71 ? 337 THR A C 1 ATOM 2122 O O . THR A 1 324 ? -3.754 -36.364 61.634 1.00 138.47 ? 337 THR A O 1 ATOM 2123 C CB . THR A 1 324 ? -5.930 -38.759 62.370 1.00 170.10 ? 337 THR A CB 1 ATOM 2124 O OG1 . THR A 1 324 ? -5.039 -39.599 61.626 1.00 172.54 ? 337 THR A OG1 1 ATOM 2125 C CG2 . THR A 1 324 ? -7.326 -39.359 62.355 1.00 173.38 ? 337 THR A CG2 1 ATOM 2126 N N . PRO A 1 325 ? -4.884 -36.109 63.584 1.00 147.59 ? 338 PRO A N 1 ATOM 2127 C CA . PRO A 1 325 ? -3.819 -35.454 64.342 1.00 151.95 ? 338 PRO A CA 1 ATOM 2128 C C . PRO A 1 325 ? -2.505 -36.210 64.198 1.00 167.20 ? 338 PRO A C 1 ATOM 2129 O O . PRO A 1 325 ? -1.464 -35.581 63.998 1.00 169.33 ? 338 PRO A O 1 ATOM 2130 C CB . PRO A 1 325 ? -4.310 -35.583 65.778 1.00 143.92 ? 338 PRO A CB 1 ATOM 2131 C CG . PRO A 1 325 ? -5.790 -35.555 65.660 1.00 137.00 ? 338 PRO A CG 1 ATOM 2132 C CD . PRO A 1 325 ? -6.166 -36.084 64.307 1.00 135.57 ? 338 PRO A CD 1 ATOM 2133 N N . GLU A 1 326 ? -2.556 -37.538 64.287 1.00 170.32 ? 339 GLU A N 1 ATOM 2134 C CA . GLU A 1 326 ? -1.364 -38.347 64.082 1.00 167.56 ? 339 GLU A CA 1 ATOM 2135 C C . GLU A 1 326 ? -0.977 -38.264 62.628 1.00 169.80 ? 339 GLU A C 1 ATOM 2136 O O . GLU A 1 326 ? 0.200 -38.162 62.298 1.00 172.37 ? 339 GLU A O 1 ATOM 2137 C CB . GLU A 1 326 ? -1.605 -39.802 64.455 1.00 170.69 ? 339 GLU A CB 1 ATOM 2138 C CG . GLU A 1 326 ? -0.437 -40.710 64.115 1.00 179.51 ? 339 GLU A CG 1 ATOM 2139 C CD . GLU A 1 326 ? -0.376 -41.930 65.018 1.00 199.47 ? 339 GLU A CD 1 ATOM 2140 O OE1 . GLU A 1 326 ? -1.398 -42.236 65.677 1.00 206.13 ? 339 GLU A OE1 1 ATOM 2141 O OE2 . GLU A 1 326 ? 0.693 -42.576 65.081 1.00 205.35 ? 339 GLU A OE2 1 ATOM 2142 N N . GLN A 1 327 ? -1.981 -38.312 61.757 1.00 172.33 ? 340 GLN A N 1 ATOM 2143 C CA . GLN A 1 327 ? -1.741 -38.290 60.319 1.00 171.03 ? 340 GLN A CA 1 ATOM 2144 C C . GLN A 1 327 ? -1.134 -36.961 59.962 1.00 158.92 ? 340 GLN A C 1 ATOM 2145 O O . GLN A 1 327 ? -0.134 -36.897 59.244 1.00 147.22 ? 340 GLN A O 1 ATOM 2146 C CB . GLN A 1 327 ? -3.030 -38.539 59.530 1.00 175.77 ? 340 GLN A CB 1 ATOM 2147 C CG . GLN A 1 327 ? -3.140 -39.969 58.982 1.00 183.70 ? 340 GLN A CG 1 ATOM 2148 C CD . GLN A 1 327 ? -4.512 -40.297 58.419 1.00 183.25 ? 340 GLN A CD 1 ATOM 2149 O OE1 . GLN A 1 327 ? -5.541 -39.892 58.967 1.00 184.54 ? 340 GLN A OE1 1 ATOM 2150 N NE2 . GLN A 1 327 ? -4.533 -41.041 57.319 1.00 179.75 ? 340 GLN A NE2 1 ATOM 2151 N N . TYR A 1 328 ? -1.742 -35.907 60.499 1.00 164.05 ? 341 TYR A N 1 ATOM 2152 C CA . TYR A 1 328 ? -1.284 -34.540 60.284 1.00 164.00 ? 341 TYR A CA 1 ATOM 2153 C C . TYR A 1 328 ? 0.180 -34.408 60.618 1.00 156.15 ? 341 TYR A C 1 ATOM 2154 O O . TYR A 1 328 ? 1.007 -34.224 59.724 1.00 145.92 ? 341 TYR A O 1 ATOM 2155 C CB . TYR A 1 328 ? -2.098 -33.552 61.126 1.00 169.82 ? 341 TYR A CB 1 ATOM 2156 C CG . TYR A 1 328 ? -3.218 -32.906 60.351 1.00 174.54 ? 341 TYR A CG 1 ATOM 2157 C CD1 . TYR A 1 328 ? -4.512 -33.402 60.422 1.00 180.13 ? 341 TYR A CD1 1 ATOM 2158 C CD2 . TYR A 1 328 ? -2.976 -31.814 59.529 1.00 172.44 ? 341 TYR A CD2 1 ATOM 2159 C CE1 . TYR A 1 328 ? -5.538 -32.822 59.705 1.00 180.05 ? 341 TYR A CE1 1 ATOM 2160 C CE2 . TYR A 1 328 ? -3.992 -31.227 58.807 1.00 171.48 ? 341 TYR A CE2 1 ATOM 2161 C CZ . TYR A 1 328 ? -5.273 -31.735 58.898 1.00 177.02 ? 341 TYR A CZ 1 ATOM 2162 O OH . TYR A 1 328 ? -6.295 -31.155 58.183 1.00 177.64 ? 341 TYR A OH 1 ATOM 2163 N N . LYS A 1 329 ? 0.488 -34.533 61.908 1.00 156.06 ? 342 LYS A N 1 ATOM 2164 C CA . LYS A 1 329 ? 1.848 -34.374 62.411 1.00 147.18 ? 342 LYS A CA 1 ATOM 2165 C C . LYS A 1 329 ? 2.846 -35.198 61.595 1.00 153.75 ? 342 LYS A C 1 ATOM 2166 O O . LYS A 1 329 ? 3.844 -34.675 61.099 1.00 154.76 ? 342 LYS A O 1 ATOM 2167 C CB . LYS A 1 329 ? 1.916 -34.754 63.910 1.00 134.44 ? 342 LYS A CB 1 ATOM 2168 N N . GLU A 1 330 ? 2.577 -36.486 61.446 1.00 156.25 ? 343 GLU A N 1 ATOM 2169 C CA . GLU A 1 330 ? 3.578 -37.360 60.874 1.00 157.65 ? 343 GLU A CA 1 ATOM 2170 C C . GLU A 1 330 ? 3.626 -37.392 59.334 1.00 175.16 ? 343 GLU A C 1 ATOM 2171 O O . GLU A 1 330 ? 4.654 -37.760 58.776 1.00 190.99 ? 343 GLU A O 1 ATOM 2172 C CB . GLU A 1 330 ? 3.479 -38.769 61.481 1.00 144.76 ? 343 GLU A CB 1 ATOM 2173 N N . CYS A 1 331 ? 2.548 -37.015 58.641 1.00 172.61 ? 344 CYS A N 1 ATOM 2174 C CA . CYS A 1 331 ? 2.574 -37.003 57.160 1.00 172.79 ? 344 CYS A CA 1 ATOM 2175 C C . CYS A 1 331 ? 2.053 -35.737 56.483 1.00 165.06 ? 344 CYS A C 1 ATOM 2176 O O . CYS A 1 331 ? 2.785 -35.057 55.759 1.00 149.77 ? 344 CYS A O 1 ATOM 2177 C CB . CYS A 1 331 ? 1.857 -38.218 56.544 1.00 179.60 ? 344 CYS A CB 1 ATOM 2178 S SG . CYS A 1 331 ? 1.729 -38.154 54.692 1.00 138.39 ? 344 CYS A SG 1 ATOM 2179 N N . ALA A 1 332 ? 0.764 -35.473 56.687 1.00 173.81 ? 345 ALA A N 1 ATOM 2180 C CA . ALA A 1 332 ? 0.064 -34.367 56.042 1.00 174.64 ? 345 ALA A CA 1 ATOM 2181 C C . ALA A 1 332 ? 0.822 -33.035 56.137 1.00 175.38 ? 345 ALA A C 1 ATOM 2182 O O . ALA A 1 332 ? 1.268 -32.477 55.119 1.00 166.10 ? 345 ALA A O 1 ATOM 2183 C CB . ALA A 1 332 ? -1.342 -34.227 56.637 1.00 171.15 ? 345 ALA A CB 1 ATOM 2184 N N . ASP A 1 333 ? 0.957 -32.534 57.365 1.00 176.69 ? 346 ASP A N 1 ATOM 2185 C CA . ASP A 1 333 ? 1.580 -31.245 57.600 1.00 170.64 ? 346 ASP A CA 1 ATOM 2186 C C . ASP A 1 333 ? 2.933 -31.193 56.907 1.00 168.14 ? 346 ASP A C 1 ATOM 2187 O O . ASP A 1 333 ? 3.097 -30.460 55.938 1.00 163.83 ? 346 ASP A O 1 ATOM 2188 C CB . ASP A 1 333 ? 1.752 -31.011 59.106 1.00 181.12 ? 346 ASP A CB 1 ATOM 2189 C CG . ASP A 1 333 ? 0.745 -30.016 59.676 1.00 189.39 ? 346 ASP A CG 1 ATOM 2190 O OD1 . ASP A 1 333 ? -0.266 -29.706 59.010 1.00 192.07 ? 346 ASP A OD1 1 ATOM 2191 O OD2 . ASP A 1 333 ? 0.965 -29.543 60.810 1.00 190.91 ? 346 ASP A OD2 1 ATOM 2192 N N . PRO A 1 334 ? 3.887 -32.035 57.339 1.00 179.25 ? 347 PRO A N 1 ATOM 2193 C CA . PRO A 1 334 ? 5.232 -31.907 56.769 1.00 180.73 ? 347 PRO A CA 1 ATOM 2194 C C . PRO A 1 334 ? 5.225 -32.059 55.260 1.00 178.63 ? 347 PRO A C 1 ATOM 2195 O O . PRO A 1 334 ? 5.817 -31.238 54.568 1.00 183.02 ? 347 PRO A O 1 ATOM 2196 C CB . PRO A 1 334 ? 6.006 -33.064 57.414 1.00 187.80 ? 347 PRO A CB 1 ATOM 2197 C CG . PRO A 1 334 ? 4.964 -34.029 57.855 1.00 194.69 ? 347 PRO A CG 1 ATOM 2198 C CD . PRO A 1 334 ? 3.796 -33.179 58.262 1.00 192.02 ? 347 PRO A CD 1 ATOM 2199 N N . ALA A 1 335 ? 4.544 -33.078 54.754 1.00 172.54 ? 348 ALA A N 1 ATOM 2200 C CA . ALA A 1 335 ? 4.471 -33.282 53.317 1.00 167.20 ? 348 ALA A CA 1 ATOM 2201 C C . ALA A 1 335 ? 3.974 -32.018 52.602 1.00 154.60 ? 348 ALA A C 1 ATOM 2202 O O . ALA A 1 335 ? 4.522 -31.620 51.562 1.00 146.80 ? 348 ALA A O 1 ATOM 2203 C CB . ALA A 1 335 ? 3.579 -34.469 52.998 1.00 170.63 ? 348 ALA A CB 1 ATOM 2204 N N . LEU A 1 336 ? 2.943 -31.385 53.158 1.00 143.10 ? 349 LEU A N 1 ATOM 2205 C CA . LEU A 1 336 ? 2.386 -30.202 52.518 1.00 140.09 ? 349 LEU A CA 1 ATOM 2206 C C . LEU A 1 336 ? 3.377 -29.034 52.519 1.00 145.80 ? 349 LEU A C 1 ATOM 2207 O O . LEU A 1 336 ? 3.398 -28.217 51.587 1.00 144.15 ? 349 LEU A O 1 ATOM 2208 C CB . LEU A 1 336 ? 1.053 -29.794 53.151 1.00 131.11 ? 349 LEU A CB 1 ATOM 2209 C CG . LEU A 1 336 ? 0.389 -28.563 52.512 1.00 119.40 ? 349 LEU A CG 1 ATOM 2210 C CD1 . LEU A 1 336 ? 0.191 -28.702 50.994 1.00 111.30 ? 349 LEU A CD1 1 ATOM 2211 C CD2 . LEU A 1 336 ? -0.927 -28.244 53.186 1.00 124.21 ? 349 LEU A CD2 1 ATOM 2212 N N . ASP A 1 337 ? 4.207 -28.972 53.557 1.00 148.54 ? 350 ASP A N 1 ATOM 2213 C CA . ASP A 1 337 ? 5.216 -27.924 53.658 1.00 150.25 ? 350 ASP A CA 1 ATOM 2214 C C . ASP A 1 337 ? 6.304 -28.113 52.599 1.00 157.87 ? 350 ASP A C 1 ATOM 2215 O O . ASP A 1 337 ? 6.622 -27.184 51.860 1.00 160.19 ? 350 ASP A O 1 ATOM 2216 C CB . ASP A 1 337 ? 5.810 -27.871 55.067 1.00 152.40 ? 350 ASP A CB 1 ATOM 2217 C CG . ASP A 1 337 ? 4.767 -27.546 56.127 1.00 156.96 ? 350 ASP A CG 1 ATOM 2218 O OD1 . ASP A 1 337 ? 3.649 -27.124 55.754 1.00 156.10 ? 350 ASP A OD1 1 ATOM 2219 O OD2 . ASP A 1 337 ? 5.061 -27.702 57.334 1.00 161.55 ? 350 ASP A OD2 1 ATOM 2220 N N . PHE A 1 338 ? 6.854 -29.322 52.507 1.00 160.87 ? 351 PHE A N 1 ATOM 2221 C CA . PHE A 1 338 ? 7.813 -29.644 51.450 1.00 159.40 ? 351 PHE A CA 1 ATOM 2222 C C . PHE A 1 338 ? 7.254 -29.312 50.057 1.00 157.11 ? 351 PHE A C 1 ATOM 2223 O O . PHE A 1 338 ? 7.977 -28.818 49.185 1.00 155.84 ? 351 PHE A O 1 ATOM 2224 C CB . PHE A 1 338 ? 8.232 -31.121 51.515 1.00 159.84 ? 351 PHE A CB 1 ATOM 2225 C CG . PHE A 1 338 ? 9.230 -31.509 50.459 1.00 157.85 ? 351 PHE A CG 1 ATOM 2226 C CD1 . PHE A 1 338 ? 10.590 -31.374 50.685 1.00 157.81 ? 351 PHE A CD1 1 ATOM 2227 C CD2 . PHE A 1 338 ? 8.805 -31.981 49.233 1.00 158.83 ? 351 PHE A CD2 1 ATOM 2228 C CE1 . PHE A 1 338 ? 11.507 -31.705 49.710 1.00 159.33 ? 351 PHE A CE1 1 ATOM 2229 C CE2 . PHE A 1 338 ? 9.715 -32.315 48.256 1.00 161.77 ? 351 PHE A CE2 1 ATOM 2230 C CZ . PHE A 1 338 ? 11.070 -32.176 48.494 1.00 162.09 ? 351 PHE A CZ 1 ATOM 2231 N N . LEU A 1 339 ? 5.970 -29.594 49.851 1.00 150.77 ? 352 LEU A N 1 ATOM 2232 C CA . LEU A 1 339 ? 5.344 -29.381 48.554 1.00 139.96 ? 352 LEU A CA 1 ATOM 2233 C C . LEU A 1 339 ? 5.497 -27.938 48.094 1.00 135.45 ? 352 LEU A C 1 ATOM 2234 O O . LEU A 1 339 ? 6.108 -27.664 47.063 1.00 126.38 ? 352 LEU A O 1 ATOM 2235 C CB . LEU A 1 339 ? 3.865 -29.762 48.596 1.00 133.40 ? 352 LEU A CB 1 ATOM 2236 C CG . LEU A 1 339 ? 3.303 -30.410 47.323 1.00 128.32 ? 352 LEU A CG 1 ATOM 2237 C CD1 . LEU A 1 339 ? 1.783 -30.211 47.222 1.00 129.45 ? 352 LEU A CD1 1 ATOM 2238 C CD2 . LEU A 1 339 ? 4.023 -29.940 46.056 1.00 114.43 ? 352 LEU A CD2 1 ATOM 2239 N N . VAL A 1 340 ? 4.924 -27.017 48.868 1.00 140.83 ? 353 VAL A N 1 ATOM 2240 C CA . VAL A 1 340 ? 4.788 -25.616 48.449 1.00 137.76 ? 353 VAL A CA 1 ATOM 2241 C C . VAL A 1 340 ? 6.057 -24.783 48.568 1.00 135.81 ? 353 VAL A C 1 ATOM 2242 O O . VAL A 1 340 ? 6.366 -23.987 47.687 1.00 136.07 ? 353 VAL A O 1 ATOM 2243 C CB . VAL A 1 340 ? 3.660 -24.914 49.208 1.00 130.16 ? 353 VAL A CB 1 ATOM 2244 C CG1 . VAL A 1 340 ? 2.434 -24.795 48.318 1.00 133.04 ? 353 VAL A CG1 1 ATOM 2245 C CG2 . VAL A 1 340 ? 3.339 -25.666 50.485 1.00 126.65 ? 353 VAL A CG2 1 ATOM 2246 N N . GLU A 1 341 ? 6.797 -24.980 49.649 1.00 137.31 ? 354 GLU A N 1 ATOM 2247 C CA . GLU A 1 341 ? 8.081 -24.314 49.806 1.00 140.09 ? 354 GLU A CA 1 ATOM 2248 C C . GLU A 1 341 ? 9.219 -24.939 48.973 1.00 142.32 ? 354 GLU A C 1 ATOM 2249 O O . GLU A 1 341 ? 9.797 -24.282 48.110 1.00 141.14 ? 354 GLU A O 1 ATOM 2250 C CB . GLU A 1 341 ? 8.456 -24.202 51.275 1.00 143.53 ? 354 GLU A CB 1 ATOM 2251 N N . LYS A 1 342 ? 9.536 -26.204 49.229 1.00 150.51 ? 355 LYS A N 1 ATOM 2252 C CA . LYS A 1 342 ? 10.688 -26.853 48.593 1.00 158.90 ? 355 LYS A CA 1 ATOM 2253 C C . LYS A 1 342 ? 10.546 -27.296 47.108 1.00 151.93 ? 355 LYS A C 1 ATOM 2254 O O . LYS A 1 342 ? 11.131 -26.666 46.223 1.00 147.19 ? 355 LYS A O 1 ATOM 2255 C CB . LYS A 1 342 ? 11.221 -28.014 49.495 1.00 87.49 ? 355 LYS A CB 1 ATOM 2256 N N . ASP A 1 343 ? 9.742 -28.321 46.821 1.00 160.36 ? 356 ASP A N 1 ATOM 2257 C CA . ASP A 1 343 ? 9.871 -29.019 45.532 1.00 170.90 ? 356 ASP A CA 1 ATOM 2258 C C . ASP A 1 343 ? 9.039 -28.424 44.402 1.00 180.32 ? 356 ASP A C 1 ATOM 2259 O O . ASP A 1 343 ? 7.821 -28.599 44.363 1.00 187.88 ? 356 ASP A O 1 ATOM 2260 C CB . ASP A 1 343 ? 9.508 -30.489 45.695 1.00 171.67 ? 356 ASP A CB 1 ATOM 2261 N N . ASN A 1 344 ? 9.724 -27.789 43.450 1.00 178.70 ? 357 ASN A N 1 ATOM 2262 C CA . ASN A 1 344 ? 9.077 -27.052 42.365 1.00 170.14 ? 357 ASN A CA 1 ATOM 2263 C C . ASN A 1 344 ? 8.973 -27.829 41.044 1.00 170.78 ? 357 ASN A C 1 ATOM 2264 O O . ASN A 1 344 ? 8.447 -27.309 40.064 1.00 167.72 ? 357 ASN A O 1 ATOM 2265 C CB . ASN A 1 344 ? 9.765 -25.688 42.161 1.00 157.68 ? 357 ASN A CB 1 ATOM 2266 N N . GLU A 1 345 ? 9.473 -29.063 41.020 1.00 174.79 ? 358 GLU A N 1 ATOM 2267 C CA . GLU A 1 345 ? 9.416 -29.892 39.808 1.00 178.34 ? 358 GLU A CA 1 ATOM 2268 C C . GLU A 1 345 ? 8.094 -30.643 39.655 1.00 175.48 ? 358 GLU A C 1 ATOM 2269 O O . GLU A 1 345 ? 7.790 -31.161 38.577 1.00 169.60 ? 358 GLU A O 1 ATOM 2270 C CB . GLU A 1 345 ? 10.588 -30.882 39.762 1.00 181.72 ? 358 GLU A CB 1 ATOM 2271 N N . TYR A 1 346 ? 7.313 -30.696 40.731 1.00 175.48 ? 359 TYR A N 1 ATOM 2272 C CA . TYR A 1 346 ? 6.052 -31.434 40.723 1.00 175.21 ? 359 TYR A CA 1 ATOM 2273 C C . TYR A 1 346 ? 4.949 -30.703 39.991 1.00 179.80 ? 359 TYR A C 1 ATOM 2274 O O . TYR A 1 346 ? 4.382 -31.210 39.027 1.00 180.62 ? 359 TYR A O 1 ATOM 2275 C CB . TYR A 1 346 ? 5.564 -31.718 42.136 1.00 168.02 ? 359 TYR A CB 1 ATOM 2276 C CG . TYR A 1 346 ? 4.275 -32.522 42.178 1.00 164.36 ? 359 TYR A CG 1 ATOM 2277 C CD1 . TYR A 1 346 ? 3.095 -32.022 41.641 1.00 157.25 ? 359 TYR A CD1 1 ATOM 2278 C CD2 . TYR A 1 346 ? 4.238 -33.778 42.770 1.00 167.44 ? 359 TYR A CD2 1 ATOM 2279 C CE1 . TYR A 1 346 ? 1.921 -32.751 41.687 1.00 158.21 ? 359 TYR A CE1 1 ATOM 2280 C CE2 . TYR A 1 346 ? 3.067 -34.512 42.825 1.00 165.41 ? 359 TYR A CE2 1 ATOM 2281 C CZ . TYR A 1 346 ? 1.911 -33.995 42.286 1.00 161.08 ? 359 TYR A CZ 1 ATOM 2282 O OH . TYR A 1 346 ? 0.747 -34.731 42.345 1.00 159.61 ? 359 TYR A OH 1 ATOM 2283 N N . CYS A 1 347 ? 4.593 -29.533 40.501 1.00 183.05 ? 360 CYS A N 1 ATOM 2284 C CA . CYS A 1 347 ? 3.460 -28.824 39.948 1.00 184.48 ? 360 CYS A CA 1 ATOM 2285 C C . CYS A 1 347 ? 3.863 -27.794 38.908 1.00 192.32 ? 360 CYS A C 1 ATOM 2286 O O . CYS A 1 347 ? 4.512 -26.791 39.217 1.00 193.78 ? 360 CYS A O 1 ATOM 2287 C CB . CYS A 1 347 ? 2.634 -28.172 41.053 1.00 177.71 ? 360 CYS A CB 1 ATOM 2288 S SG . CYS A 1 347 ? 0.888 -28.103 40.649 1.00 184.07 ? 360 CYS A SG 1 ATOM 2289 N N . VAL A 1 348 ? 3.481 -28.069 37.667 1.00 197.92 ? 361 VAL A N 1 ATOM 2290 C CA . VAL A 1 348 ? 3.486 -27.062 36.624 1.00 202.07 ? 361 VAL A CA 1 ATOM 2291 C C . VAL A 1 348 ? 2.027 -26.685 36.383 1.00 199.36 ? 361 VAL A C 1 ATOM 2292 O O . VAL A 1 348 ? 1.222 -27.513 35.949 1.00 202.93 ? 361 VAL A O 1 ATOM 2293 C CB . VAL A 1 348 ? 4.118 -27.581 35.322 1.00 206.95 ? 361 VAL A CB 1 ATOM 2294 C CG1 . VAL A 1 348 ? 4.484 -26.410 34.417 1.00 205.59 ? 361 VAL A CG1 1 ATOM 2295 C CG2 . VAL A 1 348 ? 5.346 -28.420 35.633 1.00 209.61 ? 361 VAL A CG2 1 ATOM 2296 N N . CYS A 1 349 ? 1.682 -25.445 36.702 1.00 189.68 ? 362 CYS A N 1 ATOM 2297 C CA . CYS A 1 349 ? 0.317 -24.983 36.539 1.00 183.37 ? 362 CYS A CA 1 ATOM 2298 C C . CYS A 1 349 ? 0.260 -23.921 35.456 1.00 183.79 ? 362 CYS A C 1 ATOM 2299 O O . CYS A 1 349 ? 0.714 -22.795 35.651 1.00 187.78 ? 362 CYS A O 1 ATOM 2300 C CB . CYS A 1 349 ? -0.206 -24.443 37.861 1.00 178.83 ? 362 CYS A CB 1 ATOM 2301 S SG . CYS A 1 349 ? -1.238 -25.613 38.758 1.00 149.38 ? 362 CYS A SG 1 ATOM 2302 N N . GLU A 1 350 ? -0.320 -24.285 34.319 1.00 180.61 ? 363 GLU A N 1 ATOM 2303 C CA . GLU A 1 350 ? -0.243 -23.471 33.111 1.00 175.93 ? 363 GLU A CA 1 ATOM 2304 C C . GLU A 1 350 ? -0.901 -22.082 33.238 1.00 171.32 ? 363 GLU A C 1 ATOM 2305 O O . GLU A 1 350 ? -1.802 -21.870 34.054 1.00 164.45 ? 363 GLU A O 1 ATOM 2306 C CB . GLU A 1 350 ? -0.809 -24.248 31.915 1.00 174.32 ? 363 GLU A CB 1 ATOM 2307 N N . MET A 1 351 ? -0.417 -21.142 32.429 1.00 169.79 ? 364 MET A N 1 ATOM 2308 C CA . MET A 1 351 ? -0.878 -19.758 32.439 1.00 163.13 ? 364 MET A CA 1 ATOM 2309 C C . MET A 1 351 ? -2.277 -19.604 31.834 1.00 163.29 ? 364 MET A C 1 ATOM 2310 O O . MET A 1 351 ? -2.473 -19.897 30.666 1.00 171.24 ? 364 MET A O 1 ATOM 2311 C CB . MET A 1 351 ? 0.118 -18.897 31.679 1.00 156.77 ? 364 MET A CB 1 ATOM 2312 N N . PRO A 1 352 ? -3.253 -19.131 32.626 1.00 153.33 ? 365 PRO A N 1 ATOM 2313 C CA . PRO A 1 352 ? -4.640 -18.935 32.171 1.00 155.01 ? 365 PRO A CA 1 ATOM 2314 C C . PRO A 1 352 ? -4.793 -17.777 31.191 1.00 160.98 ? 365 PRO A C 1 ATOM 2315 O O . PRO A 1 352 ? -3.979 -16.861 31.205 1.00 163.39 ? 365 PRO A O 1 ATOM 2316 C CB . PRO A 1 352 ? -5.395 -18.602 33.462 1.00 148.03 ? 365 PRO A CB 1 ATOM 2317 C CG . PRO A 1 352 ? -4.527 -19.098 34.545 1.00 149.20 ? 365 PRO A CG 1 ATOM 2318 C CD . PRO A 1 352 ? -3.122 -18.911 34.069 1.00 146.78 ? 365 PRO A CD 1 ATOM 2319 N N . CYS A 1 353 ? -5.806 -17.843 30.331 1.00 165.44 ? 366 CYS A N 1 ATOM 2320 C CA . CYS A 1 353 ? -6.095 -16.767 29.382 1.00 165.63 ? 366 CYS A CA 1 ATOM 2321 C C . CYS A 1 353 ? -6.881 -15.607 29.996 1.00 155.28 ? 366 CYS A C 1 ATOM 2322 O O . CYS A 1 353 ? -6.506 -14.444 29.855 1.00 148.20 ? 366 CYS A O 1 ATOM 2323 C CB . CYS A 1 353 ? -6.843 -17.328 28.165 1.00 173.08 ? 366 CYS A CB 1 ATOM 2324 S SG . CYS A 1 353 ? -6.265 -18.959 27.630 1.00 213.08 ? 366 CYS A SG 1 ATOM 2325 N N . ASN A 1 354 ? -7.965 -15.935 30.687 1.00 155.64 ? 367 ASN A N 1 ATOM 2326 C CA . ASN A 1 354 ? -8.835 -14.928 31.277 1.00 164.79 ? 367 ASN A CA 1 ATOM 2327 C C . ASN A 1 354 ? -8.449 -14.794 32.743 1.00 161.24 ? 367 ASN A C 1 ATOM 2328 O O . ASN A 1 354 ? -8.557 -15.754 33.504 1.00 168.06 ? 367 ASN A O 1 ATOM 2329 C CB . ASN A 1 354 ? -10.303 -15.363 31.152 1.00 185.30 ? 367 ASN A CB 1 ATOM 2330 C CG . ASN A 1 354 ? -11.151 -14.401 30.313 1.00 200.73 ? 367 ASN A CG 1 ATOM 2331 O OD1 . ASN A 1 354 ? -10.915 -13.198 30.296 1.00 200.20 ? 367 ASN A OD1 1 ATOM 2332 N ND2 . ASN A 1 354 ? -12.165 -14.941 29.634 1.00 217.26 ? 367 ASN A ND2 1 ATOM 2333 N N . VAL A 1 355 ? -7.958 -13.624 33.140 1.00 151.01 ? 368 VAL A N 1 ATOM 2334 C CA . VAL A 1 355 ? -7.538 -13.417 34.532 1.00 138.17 ? 368 VAL A CA 1 ATOM 2335 C C . VAL A 1 355 ? -7.847 -12.041 35.146 1.00 138.81 ? 368 VAL A C 1 ATOM 2336 O O . VAL A 1 355 ? -7.477 -10.997 34.596 1.00 138.86 ? 368 VAL A O 1 ATOM 2337 C CB . VAL A 1 355 ? -6.047 -13.715 34.694 1.00 123.52 ? 368 VAL A CB 1 ATOM 2338 C CG1 . VAL A 1 355 ? -5.509 -13.092 35.979 1.00 119.35 ? 368 VAL A CG1 1 ATOM 2339 C CG2 . VAL A 1 355 ? -5.831 -15.210 34.666 1.00 123.68 ? 368 VAL A CG2 1 ATOM 2340 N N . THR A 1 356 ? -8.508 -12.050 36.299 1.00 135.10 ? 369 THR A N 1 ATOM 2341 C CA . THR A 1 356 ? -8.791 -10.815 37.014 1.00 137.96 ? 369 THR A CA 1 ATOM 2342 C C . THR A 1 356 ? -7.897 -10.673 38.245 1.00 134.59 ? 369 THR A C 1 ATOM 2343 O O . THR A 1 356 ? -7.616 -11.653 38.934 1.00 137.36 ? 369 THR A O 1 ATOM 2344 C CB . THR A 1 356 ? -10.284 -10.693 37.404 1.00 146.88 ? 369 THR A CB 1 ATOM 2345 O OG1 . THR A 1 356 ? -10.939 -9.782 36.510 1.00 153.78 ? 369 THR A OG1 1 ATOM 2346 C CG2 . THR A 1 356 ? -10.439 -10.178 38.829 1.00 145.00 ? 369 THR A CG2 1 ATOM 2347 N N . ARG A 1 357 ? -7.460 -9.440 38.497 1.00 124.47 ? 370 ARG A N 1 ATOM 2348 C CA . ARG A 1 357 ? -6.551 -9.097 39.577 1.00 116.08 ? 370 ARG A CA 1 ATOM 2349 C C . ARG A 1 357 ? -7.082 -7.804 40.149 1.00 119.36 ? 370 ARG A C 1 ATOM 2350 O O . ARG A 1 357 ? -7.496 -6.934 39.384 1.00 122.99 ? 370 ARG A O 1 ATOM 2351 C CB . ARG A 1 357 ? -5.138 -8.874 39.007 1.00 117.38 ? 370 ARG A CB 1 ATOM 2352 C CG . ARG A 1 357 ? -4.263 -7.890 39.804 1.00 130.67 ? 370 ARG A CG 1 ATOM 2353 C CD . ARG A 1 357 ? -2.941 -7.557 39.115 1.00 142.98 ? 370 ARG A CD 1 ATOM 2354 N NE . ARG A 1 357 ? -2.126 -8.757 38.926 1.00 169.02 ? 370 ARG A NE 1 ATOM 2355 C CZ . ARG A 1 357 ? -1.348 -8.992 37.867 1.00 183.24 ? 370 ARG A CZ 1 ATOM 2356 N NH1 . ARG A 1 357 ? -1.271 -8.098 36.883 1.00 187.00 ? 370 ARG A NH1 1 ATOM 2357 N NH2 . ARG A 1 357 ? -0.647 -10.124 37.787 1.00 182.32 ? 370 ARG A NH2 1 ATOM 2358 N N . TYR A 1 358 ? -7.075 -7.655 41.473 1.00 121.76 ? 371 TYR A N 1 ATOM 2359 C CA . TYR A 1 358 ? -7.470 -6.377 42.088 1.00 123.83 ? 371 TYR A CA 1 ATOM 2360 C C . TYR A 1 358 ? -6.307 -5.657 42.773 1.00 118.84 ? 371 TYR A C 1 ATOM 2361 O O . TYR A 1 358 ? -5.760 -6.162 43.754 1.00 128.10 ? 371 TYR A O 1 ATOM 2362 C CB . TYR A 1 358 ? -8.616 -6.587 43.078 1.00 125.08 ? 371 TYR A CB 1 ATOM 2363 C CG . TYR A 1 358 ? -9.867 -7.070 42.416 1.00 127.14 ? 371 TYR A CG 1 ATOM 2364 C CD1 . TYR A 1 358 ? -10.872 -6.184 42.073 1.00 134.57 ? 371 TYR A CD1 1 ATOM 2365 C CD2 . TYR A 1 358 ? -10.032 -8.409 42.102 1.00 127.36 ? 371 TYR A CD2 1 ATOM 2366 C CE1 . TYR A 1 358 ? -12.016 -6.624 41.447 1.00 139.24 ? 371 TYR A CE1 1 ATOM 2367 C CE2 . TYR A 1 358 ? -11.161 -8.856 41.482 1.00 129.66 ? 371 TYR A CE2 1 ATOM 2368 C CZ . TYR A 1 358 ? -12.149 -7.966 41.153 1.00 138.74 ? 371 TYR A CZ 1 ATOM 2369 O OH . TYR A 1 358 ? -13.278 -8.426 40.528 1.00 147.96 ? 371 TYR A OH 1 ATOM 2370 N N . GLY A 1 359 ? -5.931 -4.487 42.264 1.00 100.79 ? 372 GLY A N 1 ATOM 2371 C CA . GLY A 1 359 ? -4.845 -3.732 42.860 1.00 105.41 ? 372 GLY A CA 1 ATOM 2372 C C . GLY A 1 359 ? -5.381 -2.998 44.058 1.00 117.33 ? 372 GLY A C 1 ATOM 2373 O O . GLY A 1 359 ? -6.502 -2.514 43.990 1.00 129.37 ? 372 GLY A O 1 ATOM 2374 N N . LYS A 1 360 ? -4.601 -2.903 45.137 1.00 119.62 ? 373 LYS A N 1 ATOM 2375 C CA . LYS A 1 360 ? -5.118 -2.427 46.437 1.00 116.40 ? 373 LYS A CA 1 ATOM 2376 C C . LYS A 1 360 ? -4.238 -1.379 47.098 1.00 105.59 ? 373 LYS A C 1 ATOM 2377 O O . LYS A 1 360 ? -3.014 -1.416 46.986 1.00 105.58 ? 373 LYS A O 1 ATOM 2378 C CB . LYS A 1 360 ? -5.304 -3.588 47.445 1.00 106.39 ? 373 LYS A CB 1 ATOM 2379 C CG . LYS A 1 360 ? -5.747 -4.903 46.852 1.00 99.36 ? 373 LYS A CG 1 ATOM 2380 C CD . LYS A 1 360 ? -5.117 -6.056 47.597 1.00 109.77 ? 373 LYS A CD 1 ATOM 2381 C CE . LYS A 1 360 ? -4.710 -7.182 46.646 1.00 119.85 ? 373 LYS A CE 1 ATOM 2382 N NZ . LYS A 1 360 ? -5.443 -8.473 46.921 1.00 131.62 ? 373 LYS A NZ 1 ATOM 2383 N N . GLU A 1 361 ? -4.870 -0.467 47.822 1.00 98.93 ? 374 GLU A N 1 ATOM 2384 C CA . GLU A 1 361 ? -4.122 0.506 48.596 1.00 105.55 ? 374 GLU A CA 1 ATOM 2385 C C . GLU A 1 361 ? -4.663 0.534 50.025 1.00 105.04 ? 374 GLU A C 1 ATOM 2386 O O . GLU A 1 361 ? -5.845 0.774 50.215 1.00 110.93 ? 374 GLU A O 1 ATOM 2387 C CB . GLU A 1 361 ? -4.171 1.907 47.918 1.00 59.22 ? 374 GLU A CB 1 ATOM 2388 N N . LEU A 1 362 ? -3.799 0.276 51.014 1.00 96.38 ? 375 LEU A N 1 ATOM 2389 C CA . LEU A 1 362 ? -4.209 0.131 52.413 1.00 88.56 ? 375 LEU A CA 1 ATOM 2390 C C . LEU A 1 362 ? -3.771 1.279 53.289 1.00 94.62 ? 375 LEU A C 1 ATOM 2391 O O . LEU A 1 362 ? -2.796 1.946 52.995 1.00 102.24 ? 375 LEU A O 1 ATOM 2392 C CB . LEU A 1 362 ? -3.667 -1.152 53.027 1.00 77.32 ? 375 LEU A CB 1 ATOM 2393 C CG . LEU A 1 362 ? -4.383 -2.461 52.740 1.00 79.27 ? 375 LEU A CG 1 ATOM 2394 C CD1 . LEU A 1 362 ? -3.773 -3.154 51.524 1.00 89.76 ? 375 LEU A CD1 1 ATOM 2395 C CD2 . LEU A 1 362 ? -4.224 -3.328 53.960 1.00 81.47 ? 375 LEU A CD2 1 ATOM 2396 N N . SER A 1 363 ? -4.532 1.515 54.350 1.00 92.17 ? 376 SER A N 1 ATOM 2397 C CA . SER A 1 363 ? -4.189 2.510 55.346 1.00 92.20 ? 376 SER A CA 1 ATOM 2398 C C . SER A 1 363 ? -4.934 2.186 56.613 1.00 108.14 ? 376 SER A C 1 ATOM 2399 O O . SER A 1 363 ? -5.960 1.509 56.588 1.00 116.01 ? 376 SER A O 1 ATOM 2400 C CB . SER A 1 363 ? -4.597 3.883 54.873 1.00 83.84 ? 376 SER A CB 1 ATOM 2401 O OG . SER A 1 363 ? -5.656 3.758 53.942 1.00 84.70 ? 376 SER A OG 1 ATOM 2402 N N . MET A 1 364 ? -4.425 2.677 57.731 1.00 106.72 ? 377 MET A N 1 ATOM 2403 C CA . MET A 1 364 ? -4.954 2.273 59.021 1.00 95.73 ? 377 MET A CA 1 ATOM 2404 C C . MET A 1 364 ? -5.177 3.567 59.770 1.00 88.04 ? 377 MET A C 1 ATOM 2405 O O . MET A 1 364 ? -4.619 4.579 59.394 1.00 84.40 ? 377 MET A O 1 ATOM 2406 C CB . MET A 1 364 ? -3.962 1.348 59.773 1.00 83.15 ? 377 MET A CB 1 ATOM 2407 C CG . MET A 1 364 ? -3.163 0.332 58.902 1.00 31.32 ? 377 MET A CG 1 ATOM 2408 S SD . MET A 1 364 ? -2.644 -1.175 59.737 1.00 178.36 ? 377 MET A SD 1 ATOM 2409 C CE . MET A 1 364 ? -3.188 -2.440 58.565 1.00 117.60 ? 377 MET A CE 1 ATOM 2410 N N . VAL A 1 365 ? -6.042 3.554 60.775 1.00 96.08 ? 378 VAL A N 1 ATOM 2411 C CA . VAL A 1 365 ? -6.144 4.647 61.746 1.00 101.09 ? 378 VAL A CA 1 ATOM 2412 C C . VAL A 1 365 ? -6.448 3.987 63.071 1.00 104.40 ? 378 VAL A C 1 ATOM 2413 O O . VAL A 1 365 ? -6.946 2.860 63.069 1.00 108.19 ? 378 VAL A O 1 ATOM 2414 C CB . VAL A 1 365 ? -7.241 5.717 61.403 1.00 93.67 ? 378 VAL A CB 1 ATOM 2415 C CG1 . VAL A 1 365 ? -6.782 6.633 60.292 1.00 96.51 ? 378 VAL A CG1 1 ATOM 2416 C CG2 . VAL A 1 365 ? -8.574 5.107 61.061 1.00 87.50 ? 378 VAL A CG2 1 ATOM 2417 N N . LYS A 1 366 ? -6.121 4.635 64.193 1.00 97.95 ? 379 LYS A N 1 ATOM 2418 C CA . LYS A 1 366 ? -6.368 4.000 65.483 1.00 87.78 ? 379 LYS A CA 1 ATOM 2419 C C . LYS A 1 366 ? -7.885 3.881 65.660 1.00 101.14 ? 379 LYS A C 1 ATOM 2420 O O . LYS A 1 366 ? -8.659 4.744 65.208 1.00 101.29 ? 379 LYS A O 1 ATOM 2421 C CB . LYS A 1 366 ? -5.707 4.765 66.655 1.00 64.84 ? 379 LYS A CB 1 ATOM 2422 N N . ILE A 1 367 ? -8.304 2.750 66.218 1.00 105.30 ? 380 ILE A N 1 ATOM 2423 C CA . ILE A 1 367 ? -9.626 2.580 66.778 1.00 101.66 ? 380 ILE A CA 1 ATOM 2424 C C . ILE A 1 367 ? -9.408 1.711 68.002 1.00 102.94 ? 380 ILE A C 1 ATOM 2425 O O . ILE A 1 367 ? -8.690 0.717 67.919 1.00 108.34 ? 380 ILE A O 1 ATOM 2426 C CB . ILE A 1 367 ? -10.522 1.847 65.762 1.00 103.83 ? 380 ILE A CB 1 ATOM 2427 C CG1 . ILE A 1 367 ? -11.943 1.680 66.293 1.00 107.17 ? 380 ILE A CG1 1 ATOM 2428 C CG2 . ILE A 1 367 ? -9.926 0.502 65.409 1.00 104.70 ? 380 ILE A CG2 1 ATOM 2429 C CD1 . ILE A 1 367 ? -12.833 0.853 65.400 1.00 107.13 ? 380 ILE A CD1 1 ATOM 2430 N N . PRO A 1 368 ? -10.053 2.049 69.131 1.00 103.29 ? 381 PRO A N 1 ATOM 2431 C CA . PRO A 1 368 ? -10.923 3.207 69.314 1.00 109.22 ? 381 PRO A CA 1 ATOM 2432 C C . PRO A 1 368 ? -10.142 4.482 69.461 1.00 115.40 ? 381 PRO A C 1 ATOM 2433 O O . PRO A 1 368 ? -9.011 4.443 69.924 1.00 127.62 ? 381 PRO A O 1 ATOM 2434 C CB . PRO A 1 368 ? -11.553 2.932 70.685 1.00 107.24 ? 381 PRO A CB 1 ATOM 2435 C CG . PRO A 1 368 ? -10.457 2.332 71.439 1.00 101.69 ? 381 PRO A CG 1 ATOM 2436 C CD . PRO A 1 368 ? -9.815 1.379 70.421 1.00 106.24 ? 381 PRO A CD 1 ATOM 2437 N N . SER A 1 369 ? -10.755 5.597 69.096 1.00 111.16 ? 382 SER A N 1 ATOM 2438 C CA . SER A 1 369 ? -10.315 6.879 69.592 1.00 115.93 ? 382 SER A CA 1 ATOM 2439 C C . SER A 1 369 ? -10.407 6.789 71.113 1.00 109.75 ? 382 SER A C 1 ATOM 2440 O O . SER A 1 369 ? -11.214 6.036 71.643 1.00 101.85 ? 382 SER A O 1 ATOM 2441 C CB . SER A 1 369 ? -11.234 7.984 69.065 1.00 128.82 ? 382 SER A CB 1 ATOM 2442 O OG . SER A 1 369 ? -12.605 7.689 69.319 1.00 135.15 ? 382 SER A OG 1 ATOM 2443 N N . LYS A 1 370 ? -9.565 7.520 71.825 1.00 114.17 ? 383 LYS A N 1 ATOM 2444 C CA . LYS A 1 370 ? -9.651 7.490 73.272 1.00 123.71 ? 383 LYS A CA 1 ATOM 2445 C C . LYS A 1 370 ? -11.011 8.002 73.744 1.00 125.89 ? 383 LYS A C 1 ATOM 2446 O O . LYS A 1 370 ? -11.397 7.766 74.881 1.00 134.31 ? 383 LYS A O 1 ATOM 2447 C CB . LYS A 1 370 ? -8.511 8.279 73.924 1.00 130.75 ? 383 LYS A CB 1 ATOM 2448 C CG . LYS A 1 370 ? -8.628 8.388 75.443 1.00 138.23 ? 383 LYS A CG 1 ATOM 2449 C CD . LYS A 1 370 ? -7.443 9.082 76.071 1.00 141.66 ? 383 LYS A CD 1 ATOM 2450 C CE . LYS A 1 370 ? -6.189 8.238 75.950 1.00 151.12 ? 383 LYS A CE 1 ATOM 2451 N NZ . LYS A 1 370 ? -5.066 8.861 76.711 1.00 159.88 ? 383 LYS A NZ 1 ATOM 2452 N N . ALA A 1 371 ? -11.730 8.698 72.868 1.00 125.19 ? 384 ALA A N 1 ATOM 2453 C CA . ALA A 1 371 ? -13.062 9.210 73.197 1.00 138.95 ? 384 ALA A CA 1 ATOM 2454 C C . ALA A 1 371 ? -14.171 8.157 73.131 1.00 139.40 ? 384 ALA A C 1 ATOM 2455 O O . ALA A 1 371 ? -15.103 8.172 73.937 1.00 144.18 ? 384 ALA A O 1 ATOM 2456 C CB . ALA A 1 371 ? -13.414 10.381 72.303 1.00 144.76 ? 384 ALA A CB 1 ATOM 2457 N N . SER A 1 372 ? -14.086 7.256 72.162 1.00 132.98 ? 385 SER A N 1 ATOM 2458 C CA . SER A 1 372 ? -15.152 6.283 71.982 1.00 131.66 ? 385 SER A CA 1 ATOM 2459 C C . SER A 1 372 ? -14.865 4.960 72.697 1.00 134.86 ? 385 SER A C 1 ATOM 2460 O O . SER A 1 372 ? -15.681 4.036 72.670 1.00 141.97 ? 385 SER A O 1 ATOM 2461 C CB . SER A 1 372 ? -15.451 6.066 70.494 1.00 125.06 ? 385 SER A CB 1 ATOM 2462 O OG . SER A 1 372 ? -14.472 5.257 69.868 1.00 118.61 ? 385 SER A OG 1 ATOM 2463 N N . ALA A 1 373 ? -13.712 4.889 73.355 1.00 125.52 ? 386 ALA A N 1 ATOM 2464 C CA . ALA A 1 373 ? -13.304 3.681 74.060 1.00 121.16 ? 386 ALA A CA 1 ATOM 2465 C C . ALA A 1 373 ? -14.436 3.175 74.924 1.00 131.84 ? 386 ALA A C 1 ATOM 2466 O O . ALA A 1 373 ? -14.987 2.104 74.671 1.00 136.10 ? 386 ALA A O 1 ATOM 2467 C CB . ALA A 1 373 ? -12.090 3.948 74.916 1.00 116.94 ? 386 ALA A CB 1 ATOM 2468 N N . LYS A 1 374 ? -14.792 3.962 75.937 1.00 136.61 ? 387 LYS A N 1 ATOM 2469 C CA . LYS A 1 374 ? -15.801 3.557 76.919 1.00 131.32 ? 387 LYS A CA 1 ATOM 2470 C C . LYS A 1 374 ? -17.176 3.320 76.294 1.00 127.59 ? 387 LYS A C 1 ATOM 2471 O O . LYS A 1 374 ? -17.961 2.526 76.813 1.00 122.66 ? 387 LYS A O 1 ATOM 2472 C CB . LYS A 1 374 ? -15.884 4.558 78.054 1.00 123.54 ? 387 LYS A CB 1 ATOM 2473 N N . TYR A 1 375 ? -17.460 3.996 75.180 1.00 125.42 ? 388 TYR A N 1 ATOM 2474 C CA . TYR A 1 375 ? -18.702 3.746 74.473 1.00 128.04 ? 388 TYR A CA 1 ATOM 2475 C C . TYR A 1 375 ? -18.760 2.296 74.052 1.00 133.93 ? 388 TYR A C 1 ATOM 2476 O O . TYR A 1 375 ? -19.759 1.619 74.287 1.00 144.60 ? 388 TYR A O 1 ATOM 2477 C CB . TYR A 1 375 ? -18.876 4.628 73.236 1.00 131.17 ? 388 TYR A CB 1 ATOM 2478 C CG . TYR A 1 375 ? -20.082 4.205 72.427 1.00 143.09 ? 388 TYR A CG 1 ATOM 2479 C CD1 . TYR A 1 375 ? -21.367 4.546 72.834 1.00 154.31 ? 388 TYR A CD1 1 ATOM 2480 C CD2 . TYR A 1 375 ? -19.943 3.426 71.288 1.00 142.66 ? 388 TYR A CD2 1 ATOM 2481 C CE1 . TYR A 1 375 ? -22.481 4.139 72.115 1.00 159.97 ? 388 TYR A CE1 1 ATOM 2482 C CE2 . TYR A 1 375 ? -21.050 3.017 70.562 1.00 148.01 ? 388 TYR A CE2 1 ATOM 2483 C CZ . TYR A 1 375 ? -22.317 3.377 70.979 1.00 157.44 ? 388 TYR A CZ 1 ATOM 2484 O OH . TYR A 1 375 ? -23.423 2.975 70.264 1.00 158.55 ? 388 TYR A OH 1 ATOM 2485 N N . LEU A 1 376 ? -17.683 1.824 73.430 1.00 127.00 ? 389 LEU A N 1 ATOM 2486 C CA . LEU A 1 376 ? -17.632 0.464 72.890 1.00 126.11 ? 389 LEU A CA 1 ATOM 2487 C C . LEU A 1 376 ? -17.279 -0.615 73.940 1.00 127.85 ? 389 LEU A C 1 ATOM 2488 O O . LEU A 1 376 ? -17.451 -1.823 73.713 1.00 117.81 ? 389 LEU A O 1 ATOM 2489 C CB . LEU A 1 376 ? -16.674 0.410 71.688 1.00 116.67 ? 389 LEU A CB 1 ATOM 2490 C CG . LEU A 1 376 ? -17.060 1.227 70.448 1.00 106.96 ? 389 LEU A CG 1 ATOM 2491 C CD1 . LEU A 1 376 ? -16.054 2.341 70.215 1.00 101.73 ? 389 LEU A CD1 1 ATOM 2492 C CD2 . LEU A 1 376 ? -17.178 0.341 69.203 1.00 103.15 ? 389 LEU A CD2 1 ATOM 2493 N N . ALA A 1 377 ? -16.769 -0.175 75.082 1.00 132.68 ? 390 ALA A N 1 ATOM 2494 C CA . ALA A 1 377 ? -16.529 -1.085 76.187 1.00 145.03 ? 390 ALA A CA 1 ATOM 2495 C C . ALA A 1 377 ? -17.871 -1.416 76.843 1.00 152.54 ? 390 ALA A C 1 ATOM 2496 O O . ALA A 1 377 ? -18.101 -2.537 77.315 1.00 157.39 ? 390 ALA A O 1 ATOM 2497 C CB . ALA A 1 377 ? -15.580 -0.454 77.176 1.00 152.56 ? 390 ALA A CB 1 ATOM 2498 N N . LYS A 1 378 ? -18.734 -0.406 76.904 1.00 149.24 ? 391 LYS A N 1 ATOM 2499 C CA . LYS A 1 378 ? -20.155 -0.597 77.155 1.00 146.93 ? 391 LYS A CA 1 ATOM 2500 C C . LYS A 1 378 ? -20.802 -1.477 76.076 1.00 134.78 ? 391 LYS A C 1 ATOM 2501 O O . LYS A 1 378 ? -21.172 -2.619 76.323 1.00 135.05 ? 391 LYS A O 1 ATOM 2502 C CB . LYS A 1 378 ? -20.852 0.763 77.201 1.00 153.96 ? 391 LYS A CB 1 ATOM 2503 C CG . LYS A 1 378 ? -22.349 0.723 76.952 1.00 164.12 ? 391 LYS A CG 1 ATOM 2504 C CD . LYS A 1 378 ? -22.828 1.992 76.241 1.00 169.33 ? 391 LYS A CD 1 ATOM 2505 C CE . LYS A 1 378 ? -24.318 1.918 75.921 1.00 174.23 ? 391 LYS A CE 1 ATOM 2506 N NZ . LYS A 1 378 ? -25.168 1.653 77.132 1.00 176.64 ? 391 LYS A NZ 1 ATOM 2507 N N . LYS A 1 379 ? -20.895 -0.942 74.865 1.00 122.38 ? 392 LYS A N 1 ATOM 2508 C CA . LYS A 1 379 ? -21.725 -1.530 73.823 1.00 119.78 ? 392 LYS A CA 1 ATOM 2509 C C . LYS A 1 379 ? -21.490 -2.999 73.522 1.00 122.06 ? 392 LYS A C 1 ATOM 2510 O O . LYS A 1 379 ? -22.433 -3.714 73.202 1.00 125.26 ? 392 LYS A O 1 ATOM 2511 C CB . LYS A 1 379 ? -21.620 -0.734 72.527 1.00 120.30 ? 392 LYS A CB 1 ATOM 2512 C CG . LYS A 1 379 ? -22.286 -1.419 71.342 1.00 117.10 ? 392 LYS A CG 1 ATOM 2513 C CD . LYS A 1 379 ? -22.359 -0.473 70.175 1.00 113.35 ? 392 LYS A CD 1 ATOM 2514 C CE . LYS A 1 379 ? -22.972 -1.122 68.986 1.00 114.48 ? 392 LYS A CE 1 ATOM 2515 N NZ . LYS A 1 379 ? -22.497 -0.373 67.805 1.00 120.30 ? 392 LYS A NZ 1 ATOM 2516 N N . TYR A 1 380 ? -20.241 -3.445 73.536 1.00 126.61 ? 393 TYR A N 1 ATOM 2517 C CA . TYR A 1 380 ? -19.982 -4.884 73.381 1.00 128.91 ? 393 TYR A CA 1 ATOM 2518 C C . TYR A 1 380 ? -19.668 -5.623 74.699 1.00 142.97 ? 393 TYR A C 1 ATOM 2519 O O . TYR A 1 380 ? -19.418 -6.831 74.699 1.00 140.80 ? 393 TYR A O 1 ATOM 2520 C CB . TYR A 1 380 ? -18.961 -5.146 72.272 1.00 110.33 ? 393 TYR A CB 1 ATOM 2521 C CG . TYR A 1 380 ? -19.378 -4.504 70.973 1.00 109.54 ? 393 TYR A CG 1 ATOM 2522 C CD1 . TYR A 1 380 ? -19.157 -3.153 70.743 1.00 113.90 ? 393 TYR A CD1 1 ATOM 2523 C CD2 . TYR A 1 380 ? -20.019 -5.240 69.981 1.00 113.39 ? 393 TYR A CD2 1 ATOM 2524 C CE1 . TYR A 1 380 ? -19.553 -2.552 69.546 1.00 118.26 ? 393 TYR A CE1 1 ATOM 2525 C CE2 . TYR A 1 380 ? -20.423 -4.651 68.783 1.00 110.90 ? 393 TYR A CE2 1 ATOM 2526 C CZ . TYR A 1 380 ? -20.187 -3.311 68.576 1.00 120.12 ? 393 TYR A CZ 1 ATOM 2527 O OH . TYR A 1 380 ? -20.583 -2.722 67.399 1.00 126.34 ? 393 TYR A OH 1 ATOM 2528 N N . ASN A 1 381 ? -19.696 -4.873 75.805 1.00 152.75 ? 394 ASN A N 1 ATOM 2529 C CA . ASN A 1 381 ? -19.507 -5.387 77.169 1.00 167.49 ? 394 ASN A CA 1 ATOM 2530 C C . ASN A 1 381 ? -18.129 -5.949 77.511 1.00 162.73 ? 394 ASN A C 1 ATOM 2531 O O . ASN A 1 381 ? -18.018 -6.883 78.306 1.00 164.00 ? 394 ASN A O 1 ATOM 2532 C CB . ASN A 1 381 ? -20.578 -6.423 77.516 1.00 192.10 ? 394 ASN A CB 1 ATOM 2533 C CG . ASN A 1 381 ? -20.582 -6.788 78.992 1.00 217.65 ? 394 ASN A CG 1 ATOM 2534 O OD1 . ASN A 1 381 ? -20.119 -6.022 79.840 1.00 214.96 ? 394 ASN A OD1 1 ATOM 2535 N ND2 . ASN A 1 381 ? -21.112 -7.964 79.302 1.00 245.10 ? 394 ASN A ND2 1 ATOM 2536 N N . LYS A 1 382 ? -17.080 -5.380 76.928 1.00 156.44 ? 395 LYS A N 1 ATOM 2537 C CA . LYS A 1 382 ? -15.721 -5.790 77.262 1.00 147.06 ? 395 LYS A CA 1 ATOM 2538 C C . LYS A 1 382 ? -15.004 -4.640 77.945 1.00 139.50 ? 395 LYS A C 1 ATOM 2539 O O . LYS A 1 382 ? -15.581 -3.572 78.135 1.00 141.10 ? 395 LYS A O 1 ATOM 2540 C CB . LYS A 1 382 ? -14.974 -6.233 76.015 1.00 140.84 ? 395 LYS A CB 1 ATOM 2541 N N . SER A 1 383 ? -13.758 -4.868 78.338 1.00 136.20 ? 396 SER A N 1 ATOM 2542 C CA . SER A 1 383 ? -12.962 -3.825 78.972 1.00 142.44 ? 396 SER A CA 1 ATOM 2543 C C . SER A 1 383 ? -12.492 -2.837 77.941 1.00 138.55 ? 396 SER A C 1 ATOM 2544 O O . SER A 1 383 ? -12.473 -3.135 76.750 1.00 139.37 ? 396 SER A O 1 ATOM 2545 C CB . SER A 1 383 ? -11.746 -4.426 79.672 1.00 158.13 ? 396 SER A CB 1 ATOM 2546 O OG . SER A 1 383 ? -11.019 -5.275 78.791 1.00 164.15 ? 396 SER A OG 1 ATOM 2547 N N . GLU A 1 384 ? -12.113 -1.651 78.390 1.00 138.71 ? 397 GLU A N 1 ATOM 2548 C CA . GLU A 1 384 ? -11.487 -0.709 77.486 1.00 141.27 ? 397 GLU A CA 1 ATOM 2549 C C . GLU A 1 384 ? -10.266 -1.383 76.885 1.00 141.98 ? 397 GLU A C 1 ATOM 2550 O O . GLU A 1 384 ? -10.165 -1.554 75.669 1.00 135.80 ? 397 GLU A O 1 ATOM 2551 C CB . GLU A 1 384 ? -11.095 0.558 78.207 1.00 146.70 ? 397 GLU A CB 1 ATOM 2552 C CG . GLU A 1 384 ? -12.232 1.512 78.423 1.00 157.51 ? 397 GLU A CG 1 ATOM 2553 C CD . GLU A 1 384 ? -11.774 2.794 79.061 1.00 175.47 ? 397 GLU A CD 1 ATOM 2554 O OE1 . GLU A 1 384 ? -10.546 3.038 79.054 1.00 181.83 ? 397 GLU A OE1 1 ATOM 2555 O OE2 . GLU A 1 384 ? -12.635 3.551 79.572 1.00 181.18 ? 397 GLU A OE2 1 ATOM 2556 N N . GLN A 1 385 ? -9.349 -1.797 77.746 1.00 152.25 ? 398 GLN A N 1 ATOM 2557 C CA . GLN A 1 385 ? -8.106 -2.393 77.275 1.00 163.09 ? 398 GLN A CA 1 ATOM 2558 C C . GLN A 1 385 ? -8.356 -3.501 76.245 1.00 157.88 ? 398 GLN A C 1 ATOM 2559 O O . GLN A 1 385 ? -7.609 -3.641 75.273 1.00 154.79 ? 398 GLN A O 1 ATOM 2560 C CB . GLN A 1 385 ? -7.296 -2.923 78.454 1.00 174.97 ? 398 GLN A CB 1 ATOM 2561 C CG . GLN A 1 385 ? -6.037 -3.664 78.049 1.00 182.88 ? 398 GLN A CG 1 ATOM 2562 C CD . GLN A 1 385 ? -5.410 -4.360 79.225 1.00 196.24 ? 398 GLN A CD 1 ATOM 2563 O OE1 . GLN A 1 385 ? -5.603 -3.946 80.373 1.00 205.17 ? 398 GLN A OE1 1 ATOM 2564 N NE2 . GLN A 1 385 ? -4.670 -5.433 78.958 1.00 195.97 ? 398 GLN A NE2 1 ATOM 2565 N N . TYR A 1 386 ? -9.414 -4.277 76.473 1.00 153.47 ? 399 TYR A N 1 ATOM 2566 C CA . TYR A 1 386 ? -9.841 -5.322 75.546 1.00 149.22 ? 399 TYR A CA 1 ATOM 2567 C C . TYR A 1 386 ? -10.100 -4.780 74.146 1.00 152.05 ? 399 TYR A C 1 ATOM 2568 O O . TYR A 1 386 ? -9.654 -5.351 73.149 1.00 158.18 ? 399 TYR A O 1 ATOM 2569 C CB . TYR A 1 386 ? -11.119 -5.989 76.053 1.00 146.16 ? 399 TYR A CB 1 ATOM 2570 C CG . TYR A 1 386 ? -11.749 -6.957 75.077 1.00 148.35 ? 399 TYR A CG 1 ATOM 2571 C CD1 . TYR A 1 386 ? -12.242 -6.524 73.851 1.00 143.54 ? 399 TYR A CD1 1 ATOM 2572 C CD2 . TYR A 1 386 ? -11.881 -8.300 75.397 1.00 154.32 ? 399 TYR A CD2 1 ATOM 2573 C CE1 . TYR A 1 386 ? -12.823 -7.404 72.970 1.00 141.65 ? 399 TYR A CE1 1 ATOM 2574 C CE2 . TYR A 1 386 ? -12.463 -9.185 74.519 1.00 150.52 ? 399 TYR A CE2 1 ATOM 2575 C CZ . TYR A 1 386 ? -12.931 -8.732 73.310 1.00 143.96 ? 399 TYR A CZ 1 ATOM 2576 O OH . TYR A 1 386 ? -13.508 -9.617 72.435 1.00 143.45 ? 399 TYR A OH 1 ATOM 2577 N N . ILE A 1 387 ? -10.853 -3.691 74.071 1.00 143.94 ? 400 ILE A N 1 ATOM 2578 C CA . ILE A 1 387 ? -11.261 -3.147 72.788 1.00 135.10 ? 400 ILE A CA 1 ATOM 2579 C C . ILE A 1 387 ? -10.068 -2.866 71.886 1.00 135.58 ? 400 ILE A C 1 ATOM 2580 O O . ILE A 1 387 ? -10.088 -3.196 70.702 1.00 136.36 ? 400 ILE A O 1 ATOM 2581 C CB . ILE A 1 387 ? -12.082 -1.883 72.978 1.00 128.07 ? 400 ILE A CB 1 ATOM 2582 C CG1 . ILE A 1 387 ? -13.231 -2.185 73.926 1.00 134.08 ? 400 ILE A CG1 1 ATOM 2583 C CG2 . ILE A 1 387 ? -12.653 -1.408 71.664 1.00 123.76 ? 400 ILE A CG2 1 ATOM 2584 C CD1 . ILE A 1 387 ? -14.149 -3.259 73.413 1.00 137.83 ? 400 ILE A CD1 1 ATOM 2585 N N . GLY A 1 388 ? -9.023 -2.273 72.450 1.00 133.76 ? 401 GLY A N 1 ATOM 2586 C CA . GLY A 1 388 ? -7.840 -1.941 71.678 1.00 132.98 ? 401 GLY A CA 1 ATOM 2587 C C . GLY A 1 388 ? -7.136 -3.161 71.110 1.00 129.74 ? 401 GLY A C 1 ATOM 2588 O O . GLY A 1 388 ? -6.489 -3.088 70.066 1.00 125.52 ? 401 GLY A O 1 ATOM 2589 N N . GLU A 1 389 ? -7.224 -4.283 71.814 1.00 124.36 ? 402 GLU A N 1 ATOM 2590 C CA . GLU A 1 389 ? -6.624 -5.511 71.307 1.00 123.86 ? 402 GLU A CA 1 ATOM 2591 C C . GLU A 1 389 ? -7.487 -6.234 70.278 1.00 115.24 ? 402 GLU A C 1 ATOM 2592 O O . GLU A 1 389 ? -6.980 -6.714 69.271 1.00 114.68 ? 402 GLU A O 1 ATOM 2593 C CB . GLU A 1 389 ? -6.247 -6.471 72.446 1.00 133.11 ? 402 GLU A CB 1 ATOM 2594 C CG . GLU A 1 389 ? -5.129 -6.003 73.347 1.00 136.24 ? 402 GLU A CG 1 ATOM 2595 C CD . GLU A 1 389 ? -5.378 -6.391 74.783 1.00 148.75 ? 402 GLU A CD 1 ATOM 2596 O OE1 . GLU A 1 389 ? -6.181 -7.326 75.013 1.00 149.57 ? 402 GLU A OE1 1 ATOM 2597 O OE2 . GLU A 1 389 ? -4.794 -5.746 75.679 1.00 156.75 ? 402 GLU A OE2 1 ATOM 2598 N N . ASN A 1 390 ? -8.776 -6.369 70.565 1.00 110.76 ? 403 ASN A N 1 ATOM 2599 C CA . ASN A 1 390 ? -9.618 -7.261 69.775 1.00 118.77 ? 403 ASN A CA 1 ATOM 2600 C C . ASN A 1 390 ? -10.476 -6.686 68.640 1.00 120.00 ? 403 ASN A C 1 ATOM 2601 O O . ASN A 1 390 ? -11.011 -7.441 67.827 1.00 119.45 ? 403 ASN A O 1 ATOM 2602 C CB . ASN A 1 390 ? -10.478 -8.105 70.709 1.00 130.22 ? 403 ASN A CB 1 ATOM 2603 C CG . ASN A 1 390 ? -9.661 -8.790 71.769 1.00 137.32 ? 403 ASN A CG 1 ATOM 2604 O OD1 . ASN A 1 390 ? -8.783 -9.596 71.462 1.00 136.65 ? 403 ASN A OD1 1 ATOM 2605 N ND2 . ASN A 1 390 ? -9.935 -8.470 73.028 1.00 140.45 ? 403 ASN A ND2 1 ATOM 2606 N N . ILE A 1 391 ? -10.595 -5.365 68.568 1.00 114.19 ? 404 ILE A N 1 ATOM 2607 C CA . ILE A 1 391 ? -11.534 -4.750 67.633 1.00 113.98 ? 404 ILE A CA 1 ATOM 2608 C C . ILE A 1 391 ? -10.880 -4.145 66.381 1.00 118.69 ? 404 ILE A C 1 ATOM 2609 O O . ILE A 1 391 ? -10.009 -3.295 66.476 1.00 125.18 ? 404 ILE A O 1 ATOM 2610 C CB . ILE A 1 391 ? -12.357 -3.673 68.338 1.00 115.64 ? 404 ILE A CB 1 ATOM 2611 C CG1 . ILE A 1 391 ? -13.371 -4.313 69.296 1.00 117.79 ? 404 ILE A CG1 1 ATOM 2612 C CG2 . ILE A 1 391 ? -13.038 -2.782 67.312 1.00 120.65 ? 404 ILE A CG2 1 ATOM 2613 C CD1 . ILE A 1 391 ? -14.458 -5.077 68.610 1.00 113.75 ? 404 ILE A CD1 1 ATOM 2614 N N . LEU A 1 392 ? -11.297 -4.590 65.202 1.00 114.21 ? 405 LEU A N 1 ATOM 2615 C CA . LEU A 1 392 ? -10.775 -4.024 63.964 1.00 109.03 ? 405 LEU A CA 1 ATOM 2616 C C . LEU A 1 392 ? -11.939 -3.680 63.035 1.00 113.78 ? 405 LEU A C 1 ATOM 2617 O O . LEU A 1 392 ? -13.006 -4.283 63.149 1.00 116.74 ? 405 LEU A O 1 ATOM 2618 C CB . LEU A 1 392 ? -9.815 -4.999 63.288 1.00 99.79 ? 405 LEU A CB 1 ATOM 2619 C CG . LEU A 1 392 ? -10.416 -6.232 62.613 1.00 94.10 ? 405 LEU A CG 1 ATOM 2620 C CD1 . LEU A 1 392 ? -11.095 -5.862 61.311 1.00 93.84 ? 405 LEU A CD1 1 ATOM 2621 C CD2 . LEU A 1 392 ? -9.373 -7.288 62.339 1.00 89.82 ? 405 LEU A CD2 1 ATOM 2622 N N . VAL A 1 393 ? -11.752 -2.695 62.149 1.00 110.38 ? 406 VAL A N 1 ATOM 2623 C CA . VAL A 1 393 ? -12.790 -2.337 61.178 1.00 102.85 ? 406 VAL A CA 1 ATOM 2624 C C . VAL A 1 393 ? -12.306 -2.229 59.736 1.00 98.16 ? 406 VAL A C 1 ATOM 2625 O O . VAL A 1 393 ? -11.626 -1.262 59.373 1.00 105.88 ? 406 VAL A O 1 ATOM 2626 C CB . VAL A 1 393 ? -13.460 -0.988 61.534 1.00 97.97 ? 406 VAL A CB 1 ATOM 2627 C CG1 . VAL A 1 393 ? -14.458 -0.648 60.477 1.00 93.42 ? 406 VAL A CG1 1 ATOM 2628 C CG2 . VAL A 1 393 ? -14.144 -1.079 62.887 1.00 99.12 ? 406 VAL A CG2 1 ATOM 2629 N N . LEU A 1 394 ? -12.729 -3.173 58.901 1.00 95.26 ? 407 LEU A N 1 ATOM 2630 C CA . LEU A 1 394 ? -12.237 -3.277 57.528 1.00 103.11 ? 407 LEU A CA 1 ATOM 2631 C C . LEU A 1 394 ? -13.147 -2.692 56.451 1.00 107.43 ? 407 LEU A C 1 ATOM 2632 O O . LEU A 1 394 ? -14.281 -3.128 56.276 1.00 113.33 ? 407 LEU A O 1 ATOM 2633 C CB . LEU A 1 394 ? -11.943 -4.734 57.205 1.00 104.53 ? 407 LEU A CB 1 ATOM 2634 C CG . LEU A 1 394 ? -11.413 -5.042 55.812 1.00 105.16 ? 407 LEU A CG 1 ATOM 2635 C CD1 . LEU A 1 394 ? -10.488 -3.922 55.318 1.00 96.10 ? 407 LEU A CD1 1 ATOM 2636 C CD2 . LEU A 1 394 ? -10.695 -6.395 55.886 1.00 111.05 ? 407 LEU A CD2 1 ATOM 2637 N N . ASP A 1 395 ? -12.614 -1.716 55.722 1.00 100.98 ? 408 ASP A N 1 ATOM 2638 C CA . ASP A 1 395 ? -13.330 -1.032 54.663 1.00 93.56 ? 408 ASP A CA 1 ATOM 2639 C C . ASP A 1 395 ? -12.729 -1.316 53.292 1.00 104.55 ? 408 ASP A C 1 ATOM 2640 O O . ASP A 1 395 ? -11.713 -0.732 52.948 1.00 113.96 ? 408 ASP A O 1 ATOM 2641 C CB . ASP A 1 395 ? -13.176 0.458 54.903 1.00 95.06 ? 408 ASP A CB 1 ATOM 2642 C CG . ASP A 1 395 ? -14.480 1.146 55.121 1.00 119.81 ? 408 ASP A CG 1 ATOM 2643 O OD1 . ASP A 1 395 ? -14.592 1.876 56.132 1.00 121.80 ? 408 ASP A OD1 1 ATOM 2644 O OD2 . ASP A 1 395 ? -15.389 0.964 54.278 1.00 136.86 ? 408 ASP A OD2 1 ATOM 2645 N N . ILE A 1 396 ? -13.383 -2.146 52.481 1.00 108.78 ? 409 ILE A N 1 ATOM 2646 C CA . ILE A 1 396 ? -12.985 -2.327 51.081 1.00 110.44 ? 409 ILE A CA 1 ATOM 2647 C C . ILE A 1 396 ? -13.886 -1.596 50.068 1.00 118.91 ? 409 ILE A C 1 ATOM 2648 O O . ILE A 1 396 ? -15.114 -1.660 50.144 1.00 124.41 ? 409 ILE A O 1 ATOM 2649 C CB . ILE A 1 396 ? -12.987 -3.785 50.655 1.00 106.11 ? 409 ILE A CB 1 ATOM 2650 C CG1 . ILE A 1 396 ? -12.181 -4.643 51.634 1.00 102.77 ? 409 ILE A CG1 1 ATOM 2651 C CG2 . ILE A 1 396 ? -12.469 -3.872 49.221 1.00 108.14 ? 409 ILE A CG2 1 ATOM 2652 C CD1 . ILE A 1 396 ? -12.121 -6.122 51.240 1.00 95.02 ? 409 ILE A CD1 1 ATOM 2653 N N . PHE A 1 397 ? -13.271 -0.947 49.088 1.00 120.76 ? 410 PHE A N 1 ATOM 2654 C CA . PHE A 1 397 ? -14.023 -0.147 48.138 1.00 120.89 ? 410 PHE A CA 1 ATOM 2655 C C . PHE A 1 397 ? -13.268 0.017 46.820 1.00 114.59 ? 410 PHE A C 1 ATOM 2656 O O . PHE A 1 397 ? -12.128 -0.424 46.689 1.00 108.01 ? 410 PHE A O 1 ATOM 2657 C CB . PHE A 1 397 ? -14.351 1.223 48.762 1.00 121.04 ? 410 PHE A CB 1 ATOM 2658 C CG . PHE A 1 397 ? -13.158 1.941 49.341 1.00 123.04 ? 410 PHE A CG 1 ATOM 2659 C CD1 . PHE A 1 397 ? -12.687 1.637 50.603 1.00 127.55 ? 410 PHE A CD1 1 ATOM 2660 C CD2 . PHE A 1 397 ? -12.520 2.935 48.624 1.00 121.99 ? 410 PHE A CD2 1 ATOM 2661 C CE1 . PHE A 1 397 ? -11.592 2.303 51.129 1.00 126.63 ? 410 PHE A CE1 1 ATOM 2662 C CE2 . PHE A 1 397 ? -11.435 3.610 49.153 1.00 118.86 ? 410 PHE A CE2 1 ATOM 2663 C CZ . PHE A 1 397 ? -10.969 3.295 50.402 1.00 119.02 ? 410 PHE A CZ 1 ATOM 2664 N N . PHE A 1 398 ? -13.914 0.646 45.843 1.00 111.62 ? 411 PHE A N 1 ATOM 2665 C CA . PHE A 1 398 ? -13.227 1.044 44.617 1.00 103.88 ? 411 PHE A CA 1 ATOM 2666 C C . PHE A 1 398 ? -12.969 2.538 44.649 1.00 93.94 ? 411 PHE A C 1 ATOM 2667 O O . PHE A 1 398 ? -13.773 3.299 45.185 1.00 103.38 ? 411 PHE A O 1 ATOM 2668 C CB . PHE A 1 398 ? -14.009 0.645 43.369 1.00 96.93 ? 411 PHE A CB 1 ATOM 2669 C CG . PHE A 1 398 ? -13.828 -0.786 42.991 1.00 102.43 ? 411 PHE A CG 1 ATOM 2670 C CD1 . PHE A 1 398 ? -14.807 -1.716 43.271 1.00 99.72 ? 411 PHE A CD1 1 ATOM 2671 C CD2 . PHE A 1 398 ? -12.658 -1.205 42.365 1.00 118.40 ? 411 PHE A CD2 1 ATOM 2672 C CE1 . PHE A 1 398 ? -14.638 -3.041 42.915 1.00 115.27 ? 411 PHE A CE1 1 ATOM 2673 C CE2 . PHE A 1 398 ? -12.470 -2.531 42.014 1.00 122.08 ? 411 PHE A CE2 1 ATOM 2674 C CZ . PHE A 1 398 ? -13.463 -3.452 42.286 1.00 122.09 ? 411 PHE A CZ 1 ATOM 2675 N N . GLU A 1 399 ? -11.818 2.962 44.151 1.00 167.25 ? 412 GLU A N 1 ATOM 2676 C CA . GLU A 1 399 ? -11.536 4.375 44.195 1.00 158.91 ? 412 GLU A CA 1 ATOM 2677 C C . GLU A 1 399 ? -12.314 5.003 43.060 1.00 167.36 ? 412 GLU A C 1 ATOM 2678 O O . GLU A 1 399 ? -12.888 6.073 43.206 1.00 175.48 ? 412 GLU A O 1 ATOM 2679 C CB . GLU A 1 399 ? -10.038 4.664 44.106 1.00 147.44 ? 412 GLU A CB 1 ATOM 2680 C CG . GLU A 1 399 ? -9.393 4.186 42.840 1.00 147.48 ? 412 GLU A CG 1 ATOM 2681 C CD . GLU A 1 399 ? -8.306 5.128 42.369 1.00 156.16 ? 412 GLU A CD 1 ATOM 2682 O OE1 . GLU A 1 399 ? -7.969 6.047 43.145 1.00 158.33 ? 412 GLU A OE1 1 ATOM 2683 O OE2 . GLU A 1 399 ? -7.799 4.958 41.231 1.00 158.18 ? 412 GLU A OE2 1 ATOM 2684 N N . ALA A 1 400 ? -12.375 4.306 41.936 1.00 169.00 ? 413 ALA A N 1 ATOM 2685 C CA . ALA A 1 400 ? -13.121 4.807 40.792 1.00 169.89 ? 413 ALA A CA 1 ATOM 2686 C C . ALA A 1 400 ? -14.035 3.717 40.279 1.00 173.90 ? 413 ALA A C 1 ATOM 2687 O O . ALA A 1 400 ? -13.932 2.562 40.701 1.00 180.77 ? 413 ALA A O 1 ATOM 2688 C CB . ALA A 1 400 ? -12.174 5.271 39.690 1.00 170.22 ? 413 ALA A CB 1 ATOM 2689 N N . LEU A 1 401 ? -14.960 4.096 39.401 1.00 171.02 ? 414 LEU A N 1 ATOM 2690 C CA . LEU A 1 401 ? -15.747 3.099 38.686 1.00 171.87 ? 414 LEU A CA 1 ATOM 2691 C C . LEU A 1 401 ? -15.006 2.575 37.454 1.00 178.41 ? 414 LEU A C 1 ATOM 2692 O O . LEU A 1 401 ? -15.275 1.473 36.981 1.00 183.22 ? 414 LEU A O 1 ATOM 2693 C CB . LEU A 1 401 ? -17.134 3.631 38.332 1.00 164.11 ? 414 LEU A CB 1 ATOM 2694 C CG . LEU A 1 401 ? -18.161 3.242 39.400 1.00 154.55 ? 414 LEU A CG 1 ATOM 2695 C CD1 . LEU A 1 401 ? -19.466 3.973 39.190 1.00 157.34 ? 414 LEU A CD1 1 ATOM 2696 C CD2 . LEU A 1 401 ? -18.369 1.739 39.390 1.00 140.43 ? 414 LEU A CD2 1 ATOM 2697 N N . ASN A 1 402 ? -14.040 3.344 36.971 1.00 175.60 ? 415 ASN A N 1 ATOM 2698 C CA . ASN A 1 402 ? -13.155 2.861 35.922 1.00 171.88 ? 415 ASN A CA 1 ATOM 2699 C C . ASN A 1 402 ? -12.460 1.560 36.339 1.00 167.65 ? 415 ASN A C 1 ATOM 2700 O O . ASN A 1 402 ? -12.230 1.306 37.520 1.00 170.83 ? 415 ASN A O 1 ATOM 2701 C CB . ASN A 1 402 ? -12.127 3.945 35.567 1.00 178.97 ? 415 ASN A CB 1 ATOM 2702 C CG . ASN A 1 402 ? -10.767 3.374 35.176 1.00 183.21 ? 415 ASN A CG 1 ATOM 2703 O OD1 . ASN A 1 402 ? -10.522 3.052 34.011 1.00 182.39 ? 415 ASN A OD1 1 ATOM 2704 N ND2 . ASN A 1 402 ? -9.871 3.263 36.152 1.00 186.10 ? 415 ASN A ND2 1 ATOM 2705 N N . TYR A 1 403 ? -12.169 0.716 35.362 1.00 163.05 ? 416 TYR A N 1 ATOM 2706 C CA . TYR A 1 403 ? -11.336 -0.453 35.577 1.00 162.72 ? 416 TYR A CA 1 ATOM 2707 C C . TYR A 1 403 ? -10.587 -0.710 34.274 1.00 154.71 ? 416 TYR A C 1 ATOM 2708 O O . TYR A 1 403 ? -11.095 -0.399 33.199 1.00 156.81 ? 416 TYR A O 1 ATOM 2709 C CB . TYR A 1 403 ? -12.208 -1.649 35.888 1.00 168.13 ? 416 TYR A CB 1 ATOM 2710 C CG . TYR A 1 403 ? -12.901 -2.155 34.659 1.00 173.97 ? 416 TYR A CG 1 ATOM 2711 C CD1 . TYR A 1 403 ? -14.170 -1.720 34.331 1.00 177.97 ? 416 TYR A CD1 1 ATOM 2712 C CD2 . TYR A 1 403 ? -12.275 -3.053 33.809 1.00 181.39 ? 416 TYR A CD2 1 ATOM 2713 C CE1 . TYR A 1 403 ? -14.806 -2.176 33.196 1.00 182.35 ? 416 TYR A CE1 1 ATOM 2714 C CE2 . TYR A 1 403 ? -12.895 -3.509 32.671 1.00 185.75 ? 416 TYR A CE2 1 ATOM 2715 C CZ . TYR A 1 403 ? -14.162 -3.070 32.368 1.00 185.92 ? 416 TYR A CZ 1 ATOM 2716 O OH . TYR A 1 403 ? -14.782 -3.528 31.229 1.00 187.78 ? 416 TYR A OH 1 ATOM 2717 N N . GLU A 1 404 ? -9.400 -1.302 34.350 1.00 144.48 ? 417 GLU A N 1 ATOM 2718 C CA . GLU A 1 404 ? -8.537 -1.414 33.165 1.00 130.98 ? 417 GLU A CA 1 ATOM 2719 C C . GLU A 1 404 ? -8.280 -2.840 32.702 1.00 131.44 ? 417 GLU A C 1 ATOM 2720 O O . GLU A 1 404 ? -8.468 -3.806 33.453 1.00 131.24 ? 417 GLU A O 1 ATOM 2721 C CB . GLU A 1 404 ? -7.221 -0.676 33.377 1.00 120.49 ? 417 GLU A CB 1 ATOM 2722 C CG . GLU A 1 404 ? -6.018 -1.311 32.752 1.00 119.40 ? 417 GLU A CG 1 ATOM 2723 C CD . GLU A 1 404 ? -4.742 -0.790 33.386 1.00 139.26 ? 417 GLU A CD 1 ATOM 2724 O OE1 . GLU A 1 404 ? -4.614 -0.927 34.620 1.00 149.29 ? 417 GLU A OE1 1 ATOM 2725 O OE2 . GLU A 1 404 ? -3.883 -0.219 32.674 1.00 143.73 ? 417 GLU A OE2 1 ATOM 2726 N N . THR A 1 405 ? -7.875 -2.956 31.443 1.00 131.67 ? 418 THR A N 1 ATOM 2727 C CA . THR A 1 405 ? -7.731 -4.248 30.791 1.00 134.83 ? 418 THR A CA 1 ATOM 2728 C C . THR A 1 405 ? -6.445 -4.325 29.975 1.00 130.29 ? 418 THR A C 1 ATOM 2729 O O . THR A 1 405 ? -6.032 -3.350 29.370 1.00 139.51 ? 418 THR A O 1 ATOM 2730 C CB . THR A 1 405 ? -8.931 -4.522 29.861 1.00 137.98 ? 418 THR A CB 1 ATOM 2731 O OG1 . THR A 1 405 ? -9.013 -3.495 28.858 1.00 140.17 ? 418 THR A OG1 1 ATOM 2732 C CG2 . THR A 1 405 ? -10.234 -4.559 30.663 1.00 131.68 ? 418 THR A CG2 1 ATOM 2733 N N . ILE A 1 406 ? -5.806 -5.481 29.962 1.00 121.78 ? 419 ILE A N 1 ATOM 2734 C CA . ILE A 1 406 ? -4.654 -5.666 29.101 1.00 129.04 ? 419 ILE A CA 1 ATOM 2735 C C . ILE A 1 406 ? -4.904 -6.926 28.287 1.00 151.02 ? 419 ILE A C 1 ATOM 2736 O O . ILE A 1 406 ? -4.871 -8.040 28.827 1.00 157.43 ? 419 ILE A O 1 ATOM 2737 C CB . ILE A 1 406 ? -3.383 -5.880 29.919 1.00 129.00 ? 419 ILE A CB 1 ATOM 2738 C CG1 . ILE A 1 406 ? -3.356 -4.967 31.153 1.00 125.79 ? 419 ILE A CG1 1 ATOM 2739 C CG2 . ILE A 1 406 ? -2.176 -5.699 29.045 1.00 133.76 ? 419 ILE A CG2 1 ATOM 2740 C CD1 . ILE A 1 406 ? -3.260 -3.508 30.835 1.00 124.56 ? 419 ILE A CD1 1 ATOM 2741 N N . GLU A 1 407 ? -5.124 -6.762 26.984 1.00 154.95 ? 420 GLU A N 1 ATOM 2742 C CA . GLU A 1 407 ? -5.547 -7.879 26.140 1.00 145.56 ? 420 GLU A CA 1 ATOM 2743 C C . GLU A 1 407 ? -4.504 -8.242 25.107 1.00 141.13 ? 420 GLU A C 1 ATOM 2744 O O . GLU A 1 407 ? -3.914 -7.369 24.481 1.00 134.48 ? 420 GLU A O 1 ATOM 2745 C CB . GLU A 1 407 ? -6.863 -7.559 25.435 1.00 144.93 ? 420 GLU A CB 1 ATOM 2746 C CG . GLU A 1 407 ? -7.901 -8.653 25.596 1.00 157.70 ? 420 GLU A CG 1 ATOM 2747 C CD . GLU A 1 407 ? -8.401 -9.205 24.273 1.00 168.75 ? 420 GLU A CD 1 ATOM 2748 O OE1 . GLU A 1 407 ? -8.587 -8.406 23.330 1.00 174.09 ? 420 GLU A OE1 1 ATOM 2749 O OE2 . GLU A 1 407 ? -8.600 -10.439 24.179 1.00 170.79 ? 420 GLU A OE2 1 ATOM 2750 N N . GLN A 1 408 ? -4.259 -9.539 24.944 1.00 147.66 ? 421 GLN A N 1 ATOM 2751 C CA . GLN A 1 408 ? -3.452 -10.007 23.825 1.00 150.40 ? 421 GLN A CA 1 ATOM 2752 C C . GLN A 1 408 ? -4.377 -10.286 22.625 1.00 161.75 ? 421 GLN A C 1 ATOM 2753 O O . GLN A 1 408 ? -5.289 -11.135 22.681 1.00 151.63 ? 421 GLN A O 1 ATOM 2754 C CB . GLN A 1 408 ? -2.635 -11.239 24.206 1.00 141.15 ? 421 GLN A CB 1 ATOM 2755 N N . LYS A 1 409 ? -4.153 -9.524 21.558 1.00 169.99 ? 422 LYS A N 1 ATOM 2756 C CA . LYS A 1 409 ? -4.923 -9.642 20.330 1.00 167.79 ? 422 LYS A CA 1 ATOM 2757 C C . LYS A 1 409 ? -4.010 -10.186 19.227 1.00 177.04 ? 422 LYS A C 1 ATOM 2758 O O . LYS A 1 409 ? -2.792 -9.998 19.279 1.00 178.76 ? 422 LYS A O 1 ATOM 2759 C CB . LYS A 1 409 ? -5.508 -8.288 19.941 1.00 156.84 ? 422 LYS A CB 1 ATOM 2760 N N . LYS A 1 410 ? -4.596 -10.879 18.249 1.00 175.37 ? 423 LYS A N 1 ATOM 2761 C CA . LYS A 1 410 ? -3.836 -11.439 17.129 1.00 164.52 ? 423 LYS A CA 1 ATOM 2762 C C . LYS A 1 410 ? -3.426 -10.331 16.156 1.00 159.71 ? 423 LYS A C 1 ATOM 2763 O O . LYS A 1 410 ? -4.277 -9.599 15.639 1.00 153.29 ? 423 LYS A O 1 ATOM 2764 C CB . LYS A 1 410 ? -4.655 -12.506 16.414 1.00 153.62 ? 423 LYS A CB 1 ATOM 2765 N N . ALA A 1 411 ? -2.123 -10.203 15.909 1.00 160.20 ? 424 ALA A N 1 ATOM 2766 C CA . ALA A 1 411 ? -1.616 -9.100 15.092 1.00 159.35 ? 424 ALA A CA 1 ATOM 2767 C C . ALA A 1 411 ? -1.901 -9.320 13.614 1.00 173.39 ? 424 ALA A C 1 ATOM 2768 O O . ALA A 1 411 ? -2.414 -8.430 12.933 1.00 173.12 ? 424 ALA A O 1 ATOM 2769 C CB . ALA A 1 411 ? -0.132 -8.901 15.318 1.00 150.79 ? 424 ALA A CB 1 ATOM 2770 N N . TYR A 1 412 ? -1.564 -10.515 13.132 1.00 185.43 ? 425 TYR A N 1 ATOM 2771 C CA . TYR A 1 412 ? -1.763 -10.885 11.735 1.00 189.81 ? 425 TYR A CA 1 ATOM 2772 C C . TYR A 1 412 ? -2.673 -12.088 11.654 1.00 197.71 ? 425 TYR A C 1 ATOM 2773 O O . TYR A 1 412 ? -2.355 -13.143 12.197 1.00 204.73 ? 425 TYR A O 1 ATOM 2774 C CB . TYR A 1 412 ? -0.430 -11.239 11.079 1.00 192.16 ? 425 TYR A CB 1 ATOM 2775 C CG . TYR A 1 412 ? -0.268 -10.632 9.712 1.00 192.47 ? 425 TYR A CG 1 ATOM 2776 C CD1 . TYR A 1 412 ? -1.276 -9.849 9.163 1.00 189.75 ? 425 TYR A CD1 1 ATOM 2777 C CD2 . TYR A 1 412 ? 0.886 -10.834 8.968 1.00 193.03 ? 425 TYR A CD2 1 ATOM 2778 C CE1 . TYR A 1 412 ? -1.141 -9.279 7.912 1.00 186.21 ? 425 TYR A CE1 1 ATOM 2779 C CE2 . TYR A 1 412 ? 1.028 -10.270 7.712 1.00 190.42 ? 425 TYR A CE2 1 ATOM 2780 C CZ . TYR A 1 412 ? 0.010 -9.493 7.191 1.00 186.37 ? 425 TYR A CZ 1 ATOM 2781 O OH . TYR A 1 412 ? 0.140 -8.928 5.946 1.00 184.83 ? 425 TYR A OH 1 ATOM 2782 N N . GLU A 1 413 ? -3.792 -11.945 10.958 1.00 200.08 ? 426 GLU A N 1 ATOM 2783 C CA . GLU A 1 413 ? -4.758 -13.030 10.879 1.00 208.10 ? 426 GLU A CA 1 ATOM 2784 C C . GLU A 1 413 ? -4.910 -13.458 9.428 1.00 215.02 ? 426 GLU A C 1 ATOM 2785 O O . GLU A 1 413 ? -4.504 -12.729 8.525 1.00 220.46 ? 426 GLU A O 1 ATOM 2786 C CB . GLU A 1 413 ? -6.102 -12.589 11.452 1.00 206.49 ? 426 GLU A CB 1 ATOM 2787 C CG . GLU A 1 413 ? -6.019 -11.345 12.320 1.00 206.67 ? 426 GLU A CG 1 ATOM 2788 C CD . GLU A 1 413 ? -7.181 -11.236 13.289 1.00 207.38 ? 426 GLU A CD 1 ATOM 2789 O OE1 . GLU A 1 413 ? -7.726 -10.120 13.448 1.00 209.03 ? 426 GLU A OE1 1 ATOM 2790 O OE2 . GLU A 1 413 ? -7.546 -12.266 13.896 1.00 205.05 ? 426 GLU A OE2 1 ATOM 2791 N N . VAL A 1 414 ? -5.463 -14.648 9.203 1.00 213.11 ? 427 VAL A N 1 ATOM 2792 C CA . VAL A 1 414 ? -5.632 -15.158 7.845 1.00 208.52 ? 427 VAL A CA 1 ATOM 2793 C C . VAL A 1 414 ? -6.252 -14.085 6.945 1.00 205.15 ? 427 VAL A C 1 ATOM 2794 O O . VAL A 1 414 ? -5.809 -13.875 5.813 1.00 205.62 ? 427 VAL A O 1 ATOM 2795 C CB . VAL A 1 414 ? -6.473 -16.429 7.845 1.00 203.39 ? 427 VAL A CB 1 ATOM 2796 N N . ALA A 1 415 ? -7.260 -13.391 7.464 1.00 198.24 ? 428 ALA A N 1 ATOM 2797 C CA . ALA A 1 415 ? -7.891 -12.293 6.738 1.00 191.32 ? 428 ALA A CA 1 ATOM 2798 C C . ALA A 1 415 ? -6.892 -11.192 6.371 1.00 194.12 ? 428 ALA A C 1 ATOM 2799 O O . ALA A 1 415 ? -7.019 -10.547 5.332 1.00 193.69 ? 428 ALA A O 1 ATOM 2800 C CB . ALA A 1 415 ? -9.039 -11.715 7.553 1.00 185.43 ? 428 ALA A CB 1 ATOM 2801 N N . GLY A 1 416 ? -5.904 -10.976 7.234 1.00 197.53 ? 429 GLY A N 1 ATOM 2802 C CA . GLY A 1 416 ? -4.948 -9.897 7.058 1.00 196.08 ? 429 GLY A CA 1 ATOM 2803 C C . GLY A 1 416 ? -3.933 -10.204 5.980 1.00 198.38 ? 429 GLY A C 1 ATOM 2804 O O . GLY A 1 416 ? -3.530 -9.316 5.223 1.00 196.11 ? 429 GLY A O 1 ATOM 2805 N N . LEU A 1 417 ? -3.520 -11.470 5.920 1.00 202.76 ? 430 LEU A N 1 ATOM 2806 C CA . LEU A 1 417 ? -2.573 -11.942 4.910 1.00 201.94 ? 430 LEU A CA 1 ATOM 2807 C C . LEU A 1 417 ? -3.231 -11.931 3.537 1.00 204.68 ? 430 LEU A C 1 ATOM 2808 O O . LEU A 1 417 ? -2.617 -11.528 2.548 1.00 208.25 ? 430 LEU A O 1 ATOM 2809 C CB . LEU A 1 417 ? -2.066 -13.340 5.256 1.00 194.48 ? 430 LEU A CB 1 ATOM 2810 N N . LEU A 1 418 ? -4.486 -12.372 3.488 1.00 201.22 ? 431 LEU A N 1 ATOM 2811 C CA . LEU A 1 418 ? -5.284 -12.280 2.274 1.00 197.39 ? 431 LEU A CA 1 ATOM 2812 C C . LEU A 1 418 ? -5.567 -10.809 1.958 1.00 202.53 ? 431 LEU A C 1 ATOM 2813 O O . LEU A 1 418 ? -5.987 -10.467 0.856 1.00 206.85 ? 431 LEU A O 1 ATOM 2814 C CB . LEU A 1 418 ? -6.584 -13.063 2.429 1.00 188.81 ? 431 LEU A CB 1 ATOM 2815 N N . GLY A 1 419 ? -5.328 -9.944 2.939 1.00 200.40 ? 432 GLY A N 1 ATOM 2816 C CA . GLY A 1 419 ? -5.598 -8.526 2.801 1.00 195.70 ? 432 GLY A CA 1 ATOM 2817 C C . GLY A 1 419 ? -4.424 -7.762 2.228 1.00 196.48 ? 432 GLY A C 1 ATOM 2818 O O . GLY A 1 419 ? -4.599 -6.679 1.671 1.00 196.79 ? 432 GLY A O 1 ATOM 2819 N N . ASP A 1 420 ? -3.226 -8.324 2.374 1.00 199.03 ? 433 ASP A N 1 ATOM 2820 C CA . ASP A 1 420 ? -2.005 -7.698 1.866 1.00 202.47 ? 433 ASP A CA 1 ATOM 2821 C C . ASP A 1 420 ? -1.451 -8.459 0.652 1.00 205.13 ? 433 ASP A C 1 ATOM 2822 O O . ASP A 1 420 ? -1.354 -7.927 -0.459 1.00 201.46 ? 433 ASP A O 1 ATOM 2823 C CB . ASP A 1 420 ? -0.959 -7.599 2.972 1.00 201.70 ? 433 ASP A CB 1 ATOM 2824 N N . ILE A 1 421 ? -1.065 -9.706 0.878 1.00 210.83 ? 434 ILE A N 1 ATOM 2825 C CA . ILE A 1 421 ? -0.541 -10.544 -0.193 1.00 215.80 ? 434 ILE A CA 1 ATOM 2826 C C . ILE A 1 421 ? -1.640 -11.084 -1.098 1.00 219.96 ? 434 ILE A C 1 ATOM 2827 O O . ILE A 1 421 ? -1.543 -11.006 -2.321 1.00 224.80 ? 434 ILE A O 1 ATOM 2828 C CB . ILE A 1 421 ? 0.260 -11.699 0.393 1.00 217.20 ? 434 ILE A CB 1 ATOM 2829 N N . GLY A 1 422 ? -2.690 -11.620 -0.487 1.00 220.48 ? 435 GLY A N 1 ATOM 2830 C CA . GLY A 1 422 ? -3.727 -12.325 -1.217 1.00 221.36 ? 435 GLY A CA 1 ATOM 2831 C C . GLY A 1 422 ? -4.300 -11.559 -2.392 1.00 222.24 ? 435 GLY A C 1 ATOM 2832 O O . GLY A 1 422 ? -4.384 -12.095 -3.500 1.00 221.24 ? 435 GLY A O 1 ATOM 2833 N N . GLY A 1 423 ? -4.694 -10.310 -2.153 1.00 224.62 ? 436 GLY A N 1 ATOM 2834 C CA . GLY A 1 423 ? -5.285 -9.479 -3.189 1.00 225.66 ? 436 GLY A CA 1 ATOM 2835 C C . GLY A 1 423 ? -4.358 -9.261 -4.368 1.00 226.49 ? 436 GLY A C 1 ATOM 2836 O O . GLY A 1 423 ? -4.780 -9.317 -5.524 1.00 228.28 ? 436 GLY A O 1 ATOM 2837 N N . GLN A 1 424 ? -3.086 -9.015 -4.072 1.00 224.38 ? 437 GLN A N 1 ATOM 2838 C CA . GLN A 1 424 ? -2.079 -8.834 -5.110 1.00 219.51 ? 437 GLN A CA 1 ATOM 2839 C C . GLN A 1 424 ? -1.569 -10.177 -5.647 1.00 218.30 ? 437 GLN A C 1 ATOM 2840 O O . GLN A 1 424 ? -0.954 -10.233 -6.711 1.00 221.23 ? 437 GLN A O 1 ATOM 2841 C CB . GLN A 1 424 ? -0.924 -7.980 -4.588 1.00 215.77 ? 437 GLN A CB 1 ATOM 2842 N N . MET A 1 425 ? -1.817 -11.251 -4.899 1.00 212.68 ? 438 MET A N 1 ATOM 2843 C CA . MET A 1 425 ? -1.438 -12.594 -5.325 1.00 208.43 ? 438 MET A CA 1 ATOM 2844 C C . MET A 1 425 ? -2.466 -13.131 -6.310 1.00 207.19 ? 438 MET A C 1 ATOM 2845 O O . MET A 1 425 ? -2.138 -13.912 -7.200 1.00 208.93 ? 438 MET A O 1 ATOM 2846 C CB . MET A 1 425 ? -1.301 -13.522 -4.128 1.00 207.52 ? 438 MET A CB 1 ATOM 2847 N N . GLY A 1 426 ? -3.714 -12.712 -6.135 1.00 204.48 ? 439 GLY A N 1 ATOM 2848 C CA . GLY A 1 426 ? -4.755 -13.004 -7.100 1.00 204.88 ? 439 GLY A CA 1 ATOM 2849 C C . GLY A 1 426 ? -4.564 -12.152 -8.342 1.00 208.43 ? 439 GLY A C 1 ATOM 2850 O O . GLY A 1 426 ? -4.856 -12.586 -9.454 1.00 209.56 ? 439 GLY A O 1 ATOM 2851 N N . LEU A 1 427 ? -4.061 -10.934 -8.151 1.00 210.95 ? 440 LEU A N 1 ATOM 2852 C CA . LEU A 1 427 ? -3.795 -10.019 -9.263 1.00 211.05 ? 440 LEU A CA 1 ATOM 2853 C C . LEU A 1 427 ? -2.605 -10.490 -10.092 1.00 216.83 ? 440 LEU A C 1 ATOM 2854 O O . LEU A 1 427 ? -2.611 -10.398 -11.319 1.00 217.64 ? 440 LEU A O 1 ATOM 2855 C CB . LEU A 1 427 ? -3.558 -8.605 -8.753 1.00 206.48 ? 440 LEU A CB 1 ATOM 2856 N N . PHE A 1 428 ? -1.578 -10.986 -9.408 1.00 220.65 ? 441 PHE A N 1 ATOM 2857 C CA . PHE A 1 428 ? -0.400 -11.526 -10.076 1.00 221.95 ? 441 PHE A CA 1 ATOM 2858 C C . PHE A 1 428 ? -0.746 -12.801 -10.845 1.00 228.90 ? 441 PHE A C 1 ATOM 2859 O O . PHE A 1 428 ? -0.280 -13.006 -11.969 1.00 231.74 ? 441 PHE A O 1 ATOM 2860 C CB . PHE A 1 428 ? 0.711 -11.802 -9.058 1.00 218.01 ? 441 PHE A CB 1 ATOM 2861 C CG . PHE A 1 428 ? 1.683 -12.859 -9.497 1.00 219.37 ? 441 PHE A CG 1 ATOM 2862 C CD1 . PHE A 1 428 ? 2.825 -12.524 -10.206 1.00 218.09 ? 441 PHE A CD1 1 ATOM 2863 C CD2 . PHE A 1 428 ? 1.450 -14.194 -9.205 1.00 221.46 ? 441 PHE A CD2 1 ATOM 2864 C CE1 . PHE A 1 428 ? 3.718 -13.501 -10.611 1.00 218.12 ? 441 PHE A CE1 1 ATOM 2865 C CE2 . PHE A 1 428 ? 2.338 -15.177 -9.609 1.00 220.93 ? 441 PHE A CE2 1 ATOM 2866 C CZ . PHE A 1 428 ? 3.474 -14.829 -10.312 1.00 220.01 ? 441 PHE A CZ 1 ATOM 2867 N N . ILE A 1 429 ? -1.564 -13.654 -10.233 1.00 231.26 ? 442 ILE A N 1 ATOM 2868 C CA . ILE A 1 429 ? -2.006 -14.893 -10.867 1.00 232.28 ? 442 ILE A CA 1 ATOM 2869 C C . ILE A 1 429 ? -2.896 -14.600 -12.075 1.00 235.08 ? 442 ILE A C 1 ATOM 2870 O O . ILE A 1 429 ? -3.111 -15.470 -12.923 1.00 233.99 ? 442 ILE A O 1 ATOM 2871 C CB . ILE A 1 429 ? -2.739 -15.774 -9.861 1.00 229.47 ? 442 ILE A CB 1 ATOM 2872 N N . GLY A 1 430 ? -3.417 -13.375 -12.138 1.00 236.77 ? 443 GLY A N 1 ATOM 2873 C CA . GLY A 1 430 ? -4.204 -12.921 -13.275 1.00 236.80 ? 443 GLY A CA 1 ATOM 2874 C C . GLY A 1 430 ? -3.358 -12.568 -14.489 1.00 235.66 ? 443 GLY A C 1 ATOM 2875 O O . GLY A 1 430 ? -3.670 -12.957 -15.617 1.00 236.27 ? 443 GLY A O 1 ATOM 2876 N N . ALA A 1 431 ? -2.283 -11.822 -14.253 1.00 232.76 ? 444 ALA A N 1 ATOM 2877 C CA . ALA A 1 431 ? -1.347 -11.456 -15.311 1.00 229.07 ? 444 ALA A CA 1 ATOM 2878 C C . ALA A 1 431 ? -0.502 -12.660 -15.727 1.00 230.97 ? 444 ALA A C 1 ATOM 2879 O O . ALA A 1 431 ? 0.305 -12.577 -16.655 1.00 228.62 ? 444 ALA A O 1 ATOM 2880 C CB . ALA A 1 431 ? -0.464 -10.296 -14.866 1.00 225.50 ? 444 ALA A CB 1 ATOM 2881 N N . SER A 1 432 ? -0.680 -13.771 -15.018 1.00 235.90 ? 445 SER A N 1 ATOM 2882 C CA . SER A 1 432 ? 0.016 -15.015 -15.336 1.00 242.94 ? 445 SER A CA 1 ATOM 2883 C C . SER A 1 432 ? -0.487 -15.632 -16.644 1.00 250.17 ? 445 SER A C 1 ATOM 2884 O O . SER A 1 432 ? 0.309 -16.063 -17.482 1.00 248.35 ? 445 SER A O 1 ATOM 2885 C CB . SER A 1 432 ? -0.135 -16.022 -14.191 1.00 241.69 ? 445 SER A CB 1 ATOM 2886 O OG . SER A 1 432 ? 0.406 -15.518 -12.981 1.00 239.38 ? 445 SER A OG 1 ATOM 2887 N N . ILE A 1 433 ? -1.808 -15.681 -16.809 1.00 257.70 ? 446 ILE A N 1 ATOM 2888 C CA . ILE A 1 433 ? -2.418 -16.242 -18.016 1.00 262.23 ? 446 ILE A CA 1 ATOM 2889 C C . ILE A 1 433 ? -2.157 -15.370 -19.245 1.00 262.73 ? 446 ILE A C 1 ATOM 2890 O O . ILE A 1 433 ? -1.696 -15.863 -20.278 1.00 264.34 ? 446 ILE A O 1 ATOM 2891 C CB . ILE A 1 433 ? -3.945 -16.434 -17.855 1.00 262.22 ? 446 ILE A CB 1 ATOM 2892 C CG1 . ILE A 1 433 ? -4.254 -17.350 -16.669 1.00 262.26 ? 446 ILE A CG1 1 ATOM 2893 C CG2 . ILE A 1 433 ? -4.552 -16.996 -19.136 1.00 261.98 ? 446 ILE A CG2 1 ATOM 2894 C CD1 . ILE A 1 433 ? -5.736 -17.498 -16.387 1.00 261.94 ? 446 ILE A CD1 1 ATOM 2895 N N . LEU A 1 434 ? -2.449 -14.076 -19.127 1.00 258.28 ? 447 LEU A N 1 ATOM 2896 C CA . LEU A 1 434 ? -2.263 -13.136 -20.233 1.00 251.16 ? 447 LEU A CA 1 ATOM 2897 C C . LEU A 1 434 ? -0.829 -13.185 -20.763 1.00 249.40 ? 447 LEU A C 1 ATOM 2898 O O . LEU A 1 434 ? -0.555 -12.785 -21.897 1.00 249.43 ? 447 LEU A O 1 ATOM 2899 C CB . LEU A 1 434 ? -2.633 -11.721 -19.802 1.00 245.33 ? 447 LEU A CB 1 ATOM 2900 N N . THR A 1 435 ? 0.078 -13.674 -19.922 1.00 246.14 ? 448 THR A N 1 ATOM 2901 C CA . THR A 1 435 ? 1.482 -13.826 -20.279 1.00 241.98 ? 448 THR A CA 1 ATOM 2902 C C . THR A 1 435 ? 1.736 -15.045 -21.160 1.00 237.54 ? 448 THR A C 1 ATOM 2903 O O . THR A 1 435 ? 2.452 -14.950 -22.156 1.00 235.47 ? 448 THR A O 1 ATOM 2904 C CB . THR A 1 435 ? 2.339 -13.898 -19.023 1.00 243.21 ? 448 THR A CB 1 ATOM 2905 N N . VAL A 1 436 ? 1.153 -16.186 -20.793 1.00 237.78 ? 449 VAL A N 1 ATOM 2906 C CA . VAL A 1 436 ? 1.433 -17.439 -21.496 1.00 240.00 ? 449 VAL A CA 1 ATOM 2907 C C . VAL A 1 436 ? 1.132 -17.310 -22.986 1.00 240.74 ? 449 VAL A C 1 ATOM 2908 O O . VAL A 1 436 ? 1.643 -18.076 -23.804 1.00 238.74 ? 449 VAL A O 1 ATOM 2909 C CB . VAL A 1 436 ? 0.638 -18.639 -20.915 1.00 203.82 ? 449 VAL A CB 1 ATOM 2910 C CG1 . VAL A 1 436 ? 0.637 -18.598 -19.390 1.00 202.50 ? 449 VAL A CG1 1 ATOM 2911 C CG2 . VAL A 1 436 ? -0.787 -18.658 -21.461 1.00 204.46 ? 449 VAL A CG2 1 ATOM 2912 N N . LEU A 1 437 ? 0.306 -16.329 -23.331 1.00 243.20 ? 450 LEU A N 1 ATOM 2913 C CA . LEU A 1 437 ? -0.010 -16.052 -24.723 1.00 243.81 ? 450 LEU A CA 1 ATOM 2914 C C . LEU A 1 437 ? 1.224 -15.537 -25.464 1.00 242.13 ? 450 LEU A C 1 ATOM 2915 O O . LEU A 1 437 ? 2.195 -16.273 -25.663 1.00 240.05 ? 450 LEU A O 1 ATOM 2916 C CB . LEU A 1 437 ? -1.161 -15.043 -24.819 1.00 242.59 ? 450 LEU A CB 1 ATOM 2917 C CG . LEU A 1 437 ? -2.596 -15.578 -24.706 1.00 239.87 ? 450 LEU A CG 1 ATOM 2918 C CD1 . LEU A 1 437 ? -2.990 -16.348 -25.961 1.00 238.81 ? 450 LEU A CD1 1 ATOM 2919 C CD2 . LEU A 1 437 ? -2.788 -16.447 -23.466 1.00 238.05 ? 450 LEU A CD2 1 ATOM 2920 N N . ASP B 2 2 ? 19.258 -46.630 63.268 1.00 204.51 ? 2 ASP D N 1 ATOM 2921 C CA . ASP B 2 2 ? 18.189 -46.964 62.329 1.00 207.99 ? 2 ASP D CA 1 ATOM 2922 C C . ASP B 2 2 ? 17.757 -45.728 61.555 1.00 210.51 ? 2 ASP D C 1 ATOM 2923 O O . ASP B 2 2 ? 17.576 -44.662 62.140 1.00 212.45 ? 2 ASP D O 1 ATOM 2924 C CB . ASP B 2 2 ? 16.994 -47.568 63.068 1.00 206.54 ? 2 ASP D CB 1 ATOM 2925 N N . CYS B 2 3 ? 17.566 -45.873 60.246 1.00 209.20 ? 3 CYS D N 1 ATOM 2926 C CA . CYS B 2 3 ? 17.177 -44.738 59.409 1.00 207.58 ? 3 CYS D CA 1 ATOM 2927 C C . CYS B 2 3 ? 15.818 -44.145 59.824 1.00 207.92 ? 3 CYS D C 1 ATOM 2928 O O . CYS B 2 3 ? 14.993 -44.829 60.437 1.00 209.49 ? 3 CYS D O 1 ATOM 2929 C CB . CYS B 2 3 ? 17.174 -45.128 57.923 1.00 204.03 ? 3 CYS D CB 1 ATOM 2930 S SG . CYS B 2 3 ? 15.670 -45.953 57.314 1.00 257.98 ? 3 CYS D SG 1 ATOM 2931 N N . ILE B 2 4 ? 15.613 -42.860 59.521 1.00 200.77 ? 4 ILE D N 1 ATOM 2932 C CA . ILE B 2 4 ? 14.332 -42.184 59.766 1.00 186.74 ? 4 ILE D CA 1 ATOM 2933 C C . ILE B 2 4 ? 13.599 -41.903 58.456 1.00 183.00 ? 4 ILE D C 1 ATOM 2934 O O . ILE B 2 4 ? 14.135 -41.251 57.568 1.00 179.07 ? 4 ILE D O 1 ATOM 2935 C CB . ILE B 2 4 ? 14.538 -40.895 60.548 1.00 177.62 ? 4 ILE D CB 1 ATOM 2936 N N . PRO B 2 5 ? 12.359 -42.397 58.339 1.00 186.83 ? 5 PRO D N 1 ATOM 2937 C CA . PRO B 2 5 ? 11.576 -42.305 57.100 1.00 187.34 ? 5 PRO D CA 1 ATOM 2938 C C . PRO B 2 5 ? 11.190 -40.874 56.746 1.00 179.49 ? 5 PRO D C 1 ATOM 2939 O O . PRO B 2 5 ? 11.259 -39.984 57.584 1.00 173.82 ? 5 PRO D O 1 ATOM 2940 C CB . PRO B 2 5 ? 10.311 -43.108 57.429 1.00 190.65 ? 5 PRO D CB 1 ATOM 2941 C CG . PRO B 2 5 ? 10.172 -42.997 58.906 1.00 190.66 ? 5 PRO D CG 1 ATOM 2942 C CD . PRO B 2 5 ? 11.581 -42.983 59.445 1.00 189.34 ? 5 PRO D CD 1 ATOM 2943 N N . LYS B 2 6 ? 10.781 -40.660 55.503 1.00 182.05 ? 6 LYS D N 1 ATOM 2944 C CA . LYS B 2 6 ? 10.264 -39.361 55.109 1.00 188.38 ? 6 LYS D CA 1 ATOM 2945 C C . LYS B 2 6 ? 9.057 -39.054 55.992 1.00 193.84 ? 6 LYS D C 1 ATOM 2946 O O . LYS B 2 6 ? 8.389 -39.972 56.487 1.00 191.79 ? 6 LYS D O 1 ATOM 2947 C CB . LYS B 2 6 ? 9.882 -39.345 53.616 1.00 183.96 ? 6 LYS D CB 1 ATOM 2948 N N . TRP B 2 7 ? 8.814 -37.763 56.211 1.00 193.47 ? 7 TRP D N 1 ATOM 2949 C CA . TRP B 2 7 ? 7.628 -37.308 56.919 1.00 187.70 ? 7 TRP D CA 1 ATOM 2950 C C . TRP B 2 7 ? 7.764 -37.329 58.448 1.00 190.68 ? 7 TRP D C 1 ATOM 2951 O O . TRP B 2 7 ? 6.934 -36.770 59.163 1.00 191.17 ? 7 TRP D O 1 ATOM 2952 C CB . TRP B 2 7 ? 6.438 -38.152 56.466 1.00 183.67 ? 7 TRP D CB 1 ATOM 2953 C CG . TRP B 2 7 ? 5.920 -37.777 55.121 1.00 184.52 ? 7 TRP D CG 1 ATOM 2954 C CD1 . TRP B 2 7 ? 4.678 -38.040 54.630 1.00 192.82 ? 7 TRP D CD1 1 ATOM 2955 C CD2 . TRP B 2 7 ? 6.610 -37.044 54.097 1.00 182.27 ? 7 TRP D CD2 1 ATOM 2956 N NE1 . TRP B 2 7 ? 4.545 -37.525 53.362 1.00 195.99 ? 7 TRP D NE1 1 ATOM 2957 C CE2 . TRP B 2 7 ? 5.715 -36.907 53.011 1.00 191.54 ? 7 TRP D CE2 1 ATOM 2958 C CE3 . TRP B 2 7 ? 7.887 -36.488 53.991 1.00 174.37 ? 7 TRP D CE3 1 ATOM 2959 C CZ2 . TRP B 2 7 ? 6.064 -36.242 51.834 1.00 187.84 ? 7 TRP D CZ2 1 ATOM 2960 C CZ3 . TRP B 2 7 ? 8.229 -35.828 52.828 1.00 177.50 ? 7 TRP D CZ3 1 ATOM 2961 C CH2 . TRP B 2 7 ? 7.321 -35.710 51.763 1.00 182.79 ? 7 TRP D CH2 1 ATOM 2962 N N . LYS B 2 8 ? 8.819 -37.961 58.946 1.00 192.36 ? 8 LYS D N 1 ATOM 2963 C CA . LYS B 2 8 ? 9.002 -38.116 60.387 1.00 195.06 ? 8 LYS D CA 1 ATOM 2964 C C . LYS B 2 8 ? 9.920 -37.053 60.999 1.00 195.50 ? 8 LYS D C 1 ATOM 2965 O O . LYS B 2 8 ? 10.885 -36.619 60.365 1.00 197.82 ? 8 LYS D O 1 ATOM 2966 C CB . LYS B 2 8 ? 9.511 -39.511 60.702 1.00 197.39 ? 8 LYS D CB 1 ATOM 2967 N N . GLY B 2 9 ? 9.616 -36.633 62.226 1.00 191.19 ? 9 GLY D N 1 ATOM 2968 C CA . GLY B 2 9 ? 10.403 -35.608 62.895 1.00 187.44 ? 9 GLY D CA 1 ATOM 2969 C C . GLY B 2 9 ? 11.845 -36.004 63.176 1.00 183.48 ? 9 GLY D C 1 ATOM 2970 O O . GLY B 2 9 ? 12.118 -36.979 63.878 1.00 180.97 ? 9 GLY D O 1 ATOM 2971 N N . CYS B 2 10 ? 12.769 -35.212 62.642 1.00 181.97 ? 10 CYS D N 1 ATOM 2972 C CA . CYS B 2 10 ? 14.197 -35.514 62.704 1.00 177.46 ? 10 CYS D CA 1 ATOM 2973 C C . CYS B 2 10 ? 14.917 -34.845 63.878 1.00 174.03 ? 10 CYS D C 1 ATOM 2974 O O . CYS B 2 10 ? 16.145 -34.898 63.971 1.00 162.46 ? 10 CYS D O 1 ATOM 2975 C CB . CYS B 2 10 ? 14.880 -35.174 61.373 1.00 174.75 ? 10 CYS D CB 1 ATOM 2976 S SG . CYS B 2 10 ? 14.685 -33.478 60.813 1.00 326.23 ? 10 CYS D SG 1 ATOM 2977 N N . VAL B 2 11 ? 14.145 -34.215 64.762 1.00 178.06 ? 11 VAL D N 1 ATOM 2978 C CA . VAL B 2 11 ? 14.687 -33.408 65.857 1.00 173.24 ? 11 VAL D CA 1 ATOM 2979 C C . VAL B 2 11 ? 15.786 -34.147 66.629 1.00 184.95 ? 11 VAL D C 1 ATOM 2980 O O . VAL B 2 11 ? 15.655 -35.335 66.915 1.00 187.51 ? 11 VAL D O 1 ATOM 2981 C CB . VAL B 2 11 ? 13.560 -33.002 66.799 1.00 152.99 ? 11 VAL D CB 1 ATOM 2982 N N . ASN B 2 12 ? 16.867 -33.441 66.959 1.00 188.71 ? 12 ASN D N 1 ATOM 2983 C CA . ASN B 2 12 ? 18.048 -34.051 67.586 1.00 195.01 ? 12 ASN D CA 1 ATOM 2984 C C . ASN B 2 12 ? 18.734 -35.115 66.712 1.00 192.20 ? 12 ASN D C 1 ATOM 2985 O O . ASN B 2 12 ? 19.083 -36.204 67.186 1.00 184.25 ? 12 ASN D O 1 ATOM 2986 C CB . ASN B 2 12 ? 17.694 -34.633 68.960 1.00 202.34 ? 12 ASN D CB 1 ATOM 2987 C CG . ASN B 2 12 ? 17.877 -33.636 70.085 1.00 206.51 ? 12 ASN D CG 1 ATOM 2988 O OD1 . ASN B 2 12 ? 18.971 -33.107 70.291 1.00 206.91 ? 12 ASN D OD1 1 ATOM 2989 N ND2 . ASN B 2 12 ? 16.803 -33.375 70.823 1.00 208.46 ? 12 ASN D ND2 1 ATOM 2990 N N . ARG B 2 13 ? 18.930 -34.783 65.438 1.00 192.52 ? 13 ARG D N 1 ATOM 2991 C CA . ARG B 2 13 ? 19.556 -35.694 64.486 1.00 186.83 ? 13 ARG D CA 1 ATOM 2992 C C . ARG B 2 13 ? 20.339 -34.939 63.410 1.00 187.10 ? 13 ARG D C 1 ATOM 2993 O O . ARG B 2 13 ? 19.960 -34.930 62.236 1.00 187.75 ? 13 ARG D O 1 ATOM 2994 C CB . ARG B 2 13 ? 18.509 -36.599 63.849 1.00 181.66 ? 13 ARG D CB 1 ATOM 2995 N N . ASP B 2 16 ? 20.441 -38.937 60.259 1.00 196.21 ? 16 ASP D N 1 ATOM 2996 C CA . ASP B 2 16 ? 19.703 -40.142 60.629 1.00 198.06 ? 16 ASP D CA 1 ATOM 2997 C C . ASP B 2 16 ? 18.403 -40.300 59.836 1.00 203.58 ? 16 ASP D C 1 ATOM 2998 O O . ASP B 2 16 ? 17.453 -40.923 60.308 1.00 202.23 ? 16 ASP D O 1 ATOM 2999 C CB . ASP B 2 16 ? 19.431 -40.167 62.137 1.00 194.28 ? 16 ASP D CB 1 ATOM 3000 N N . CYS B 2 17 ? 18.358 -39.711 58.645 1.00 211.29 ? 17 CYS D N 1 ATOM 3001 C CA . CYS B 2 17 ? 17.225 -39.889 57.742 1.00 218.01 ? 17 CYS D CA 1 ATOM 3002 C C . CYS B 2 17 ? 17.364 -41.192 56.967 1.00 220.66 ? 17 CYS D C 1 ATOM 3003 O O . CYS B 2 17 ? 18.475 -41.686 56.776 1.00 220.82 ? 17 CYS D O 1 ATOM 3004 C CB . CYS B 2 17 ? 17.109 -38.716 56.755 1.00 219.70 ? 17 CYS D CB 1 ATOM 3005 S SG . CYS B 2 17 ? 16.881 -37.083 57.486 1.00 309.80 ? 17 CYS D SG 1 ATOM 3006 N N . CYS B 2 18 ? 16.240 -41.738 56.510 1.00 222.86 ? 18 CYS D N 1 ATOM 3007 C CA . CYS B 2 18 ? 16.266 -42.885 55.610 1.00 224.06 ? 18 CYS D CA 1 ATOM 3008 C C . CYS B 2 18 ? 16.866 -42.469 54.270 1.00 226.81 ? 18 CYS D C 1 ATOM 3009 O O . CYS B 2 18 ? 16.901 -41.290 53.936 1.00 227.60 ? 18 CYS D O 1 ATOM 3010 C CB . CYS B 2 18 ? 14.870 -43.489 55.427 1.00 221.16 ? 18 CYS D CB 1 ATOM 3011 S SG . CYS B 2 18 ? 14.298 -44.501 56.826 1.00 449.75 ? 18 CYS D SG 1 ATOM 3012 N N . GLU B 2 19 ? 17.348 -43.448 53.515 1.00 230.45 ? 19 GLU D N 1 ATOM 3013 C CA . GLU B 2 19 ? 18.054 -43.197 52.266 1.00 231.64 ? 19 GLU D CA 1 ATOM 3014 C C . GLU B 2 19 ? 17.253 -42.313 51.317 1.00 224.95 ? 19 GLU D C 1 ATOM 3015 O O . GLU B 2 19 ? 16.090 -42.597 51.026 1.00 224.91 ? 19 GLU D O 1 ATOM 3016 C CB . GLU B 2 19 ? 18.369 -44.532 51.585 1.00 238.75 ? 19 GLU D CB 1 ATOM 3017 C CG . GLU B 2 19 ? 18.814 -44.423 50.137 1.00 243.96 ? 19 GLU D CG 1 ATOM 3018 C CD . GLU B 2 19 ? 18.338 -45.595 49.300 1.00 247.85 ? 19 GLU D CD 1 ATOM 3019 O OE1 . GLU B 2 19 ? 17.187 -46.040 49.508 1.00 251.89 ? 19 GLU D OE1 1 ATOM 3020 O OE2 . GLU B 2 19 ? 19.108 -46.072 48.438 1.00 245.62 ? 19 GLU D OE2 1 ATOM 3021 N N . GLY B 2 20 ? 17.888 -41.246 50.835 1.00 219.55 ? 20 GLY D N 1 ATOM 3022 C CA . GLY B 2 20 ? 17.288 -40.367 49.843 1.00 214.18 ? 20 GLY D CA 1 ATOM 3023 C C . GLY B 2 20 ? 16.761 -39.040 50.366 1.00 206.07 ? 20 GLY D C 1 ATOM 3024 O O . GLY B 2 20 ? 16.319 -38.196 49.589 1.00 207.19 ? 20 GLY D O 1 ATOM 3025 N N . LEU B 2 21 ? 16.813 -38.853 51.680 1.00 197.61 ? 21 LEU D N 1 ATOM 3026 C CA . LEU B 2 21 ? 16.175 -37.713 52.322 1.00 185.21 ? 21 LEU D CA 1 ATOM 3027 C C . LEU B 2 21 ? 17.178 -36.853 53.074 1.00 190.34 ? 21 LEU D C 1 ATOM 3028 O O . LEU B 2 21 ? 18.226 -37.338 53.501 1.00 197.69 ? 21 LEU D O 1 ATOM 3029 C CB . LEU B 2 21 ? 15.127 -38.198 53.321 1.00 171.41 ? 21 LEU D CB 1 ATOM 3030 C CG . LEU B 2 21 ? 14.213 -39.336 52.887 1.00 169.27 ? 21 LEU D CG 1 ATOM 3031 C CD1 . LEU B 2 21 ? 13.568 -39.946 54.120 1.00 171.21 ? 21 LEU D CD1 1 ATOM 3032 C CD2 . LEU B 2 21 ? 13.173 -38.863 51.883 1.00 164.09 ? 21 LEU D CD2 1 ATOM 3033 N N . GLU B 2 22 ? 16.850 -35.576 53.238 1.00 186.87 ? 22 GLU D N 1 ATOM 3034 C CA . GLU B 2 22 ? 17.648 -34.684 54.067 1.00 186.58 ? 22 GLU D CA 1 ATOM 3035 C C . GLU B 2 22 ? 16.751 -34.078 55.148 1.00 186.64 ? 22 GLU D C 1 ATOM 3036 O O . GLU B 2 22 ? 15.580 -33.787 54.891 1.00 186.83 ? 22 GLU D O 1 ATOM 3037 C CB . GLU B 2 22 ? 18.293 -33.597 53.211 1.00 189.03 ? 22 GLU D CB 1 ATOM 3038 C CG . GLU B 2 22 ? 17.309 -32.572 52.689 1.00 199.22 ? 22 GLU D CG 1 ATOM 3039 C CD . GLU B 2 22 ? 17.833 -31.850 51.471 1.00 209.16 ? 22 GLU D CD 1 ATOM 3040 O OE1 . GLU B 2 22 ? 18.669 -32.453 50.756 1.00 213.76 ? 22 GLU D OE1 1 ATOM 3041 O OE2 . GLU B 2 22 ? 17.413 -30.690 51.236 1.00 206.21 ? 22 GLU D OE2 1 ATOM 3042 N N . CYS B 2 23 ? 17.295 -33.907 56.355 1.00 184.75 ? 23 CYS D N 1 ATOM 3043 C CA . CYS B 2 23 ? 16.523 -33.390 57.488 1.00 181.73 ? 23 CYS D CA 1 ATOM 3044 C C . CYS B 2 23 ? 16.507 -31.868 57.517 1.00 175.09 ? 23 CYS D C 1 ATOM 3045 O O . CYS B 2 23 ? 17.542 -31.228 57.721 1.00 176.57 ? 23 CYS D O 1 ATOM 3046 C CB . CYS B 2 23 ? 17.068 -33.936 58.811 1.00 186.27 ? 23 CYS D CB 1 ATOM 3047 S SG . CYS B 2 23 ? 16.609 -32.990 60.308 1.00 156.98 ? 23 CYS D SG 1 ATOM 3048 N N . TRP B 2 24 ? 15.308 -31.310 57.367 1.00 166.76 ? 24 TRP D N 1 ATOM 3049 C CA . TRP B 2 24 ? 15.119 -29.906 57.046 1.00 156.53 ? 24 TRP D CA 1 ATOM 3050 C C . TRP B 2 24 ? 14.246 -29.181 58.037 1.00 149.34 ? 24 TRP D C 1 ATOM 3051 O O . TRP B 2 24 ? 13.147 -29.630 58.339 1.00 143.95 ? 24 TRP D O 1 ATOM 3052 C CB . TRP B 2 24 ? 14.443 -29.810 55.698 1.00 158.08 ? 24 TRP D CB 1 ATOM 3053 C CG . TRP B 2 24 ? 13.722 -28.529 55.490 1.00 157.17 ? 24 TRP D CG 1 ATOM 3054 C CD1 . TRP B 2 24 ? 14.201 -27.279 55.729 1.00 159.68 ? 24 TRP D CD1 1 ATOM 3055 C CD2 . TRP B 2 24 ? 12.402 -28.360 54.952 1.00 157.17 ? 24 TRP D CD2 1 ATOM 3056 N NE1 . TRP B 2 24 ? 13.258 -26.342 55.385 1.00 164.79 ? 24 TRP D NE1 1 ATOM 3057 C CE2 . TRP B 2 24 ? 12.146 -26.983 54.902 1.00 161.09 ? 24 TRP D CE2 1 ATOM 3058 C CE3 . TRP B 2 24 ? 11.411 -29.241 54.511 1.00 153.23 ? 24 TRP D CE3 1 ATOM 3059 C CZ2 . TRP B 2 24 ? 10.940 -26.466 54.430 1.00 154.54 ? 24 TRP D CZ2 1 ATOM 3060 C CZ3 . TRP B 2 24 ? 10.209 -28.716 54.042 1.00 145.39 ? 24 TRP D CZ3 1 ATOM 3061 C CH2 . TRP B 2 24 ? 9.991 -27.353 54.004 1.00 144.08 ? 24 TRP D CH2 1 ATOM 3062 N N . LYS B 2 25 ? 14.726 -28.033 58.503 1.00 153.26 ? 25 LYS D N 1 ATOM 3063 C CA . LYS B 2 25 ? 14.002 -27.230 59.474 1.00 149.84 ? 25 LYS D CA 1 ATOM 3064 C C . LYS B 2 25 ? 12.932 -26.406 58.778 1.00 151.83 ? 25 LYS D C 1 ATOM 3065 O O . LYS B 2 25 ? 13.252 -25.536 57.974 1.00 154.59 ? 25 LYS D O 1 ATOM 3066 C CB . LYS B 2 25 ? 14.982 -26.312 60.202 1.00 144.62 ? 25 LYS D CB 1 ATOM 3067 C CG . LYS B 2 25 ? 14.337 -25.127 60.850 1.00 152.45 ? 25 LYS D CG 1 ATOM 3068 C CD . LYS B 2 25 ? 13.280 -25.530 61.862 1.00 159.80 ? 25 LYS D CD 1 ATOM 3069 C CE . LYS B 2 25 ? 12.612 -24.285 62.437 1.00 169.19 ? 25 LYS D CE 1 ATOM 3070 N NZ . LYS B 2 25 ? 11.450 -24.612 63.308 1.00 175.54 ? 25 LYS D NZ 1 ATOM 3071 N N . ARG B 2 26 ? 11.668 -26.666 59.115 1.00 155.42 ? 26 ARG D N 1 ATOM 3072 C CA . ARG B 2 26 ? 10.536 -25.961 58.506 1.00 164.62 ? 26 ARG D CA 1 ATOM 3073 C C . ARG B 2 26 ? 10.341 -24.586 59.135 1.00 161.07 ? 26 ARG D C 1 ATOM 3074 O O . ARG B 2 26 ? 10.693 -24.369 60.293 1.00 158.03 ? 26 ARG D O 1 ATOM 3075 C CB . ARG B 2 26 ? 9.233 -26.768 58.633 1.00 168.04 ? 26 ARG D CB 1 ATOM 3076 C CG . ARG B 2 26 ? 9.177 -28.078 57.839 1.00 167.02 ? 26 ARG D CG 1 ATOM 3077 C CD . ARG B 2 26 ? 7.882 -28.830 58.114 1.00 162.96 ? 26 ARG D CD 1 ATOM 3078 N NE . ARG B 2 26 ? 7.878 -29.418 59.451 1.00 161.62 ? 26 ARG D NE 1 ATOM 3079 C CZ . ARG B 2 26 ? 6.785 -29.732 60.142 1.00 157.95 ? 26 ARG D CZ 1 ATOM 3080 N NH1 . ARG B 2 26 ? 5.580 -29.511 59.636 1.00 154.01 ? 26 ARG D NH1 1 ATOM 3081 N NH2 . ARG B 2 26 ? 6.901 -30.268 61.350 1.00 154.81 ? 26 ARG D NH2 1 ATOM 3082 N N . ARG B 2 27 ? 9.764 -23.664 58.374 1.00 156.91 ? 27 ARG D N 1 ATOM 3083 C CA . ARG B 2 27 ? 9.551 -22.314 58.866 1.00 161.33 ? 27 ARG D CA 1 ATOM 3084 C C . ARG B 2 27 ? 8.746 -22.273 60.165 1.00 163.30 ? 27 ARG D C 1 ATOM 3085 O O . ARG B 2 27 ? 9.259 -21.838 61.194 1.00 164.89 ? 27 ARG D O 1 ATOM 3086 C CB . ARG B 2 27 ? 8.888 -21.444 57.797 1.00 172.81 ? 27 ARG D CB 1 ATOM 3087 C CG . ARG B 2 27 ? 9.727 -21.211 56.546 1.00 177.14 ? 27 ARG D CG 1 ATOM 3088 C CD . ARG B 2 27 ? 9.122 -20.105 55.690 1.00 175.11 ? 27 ARG D CD 1 ATOM 3089 N NE . ARG B 2 27 ? 9.895 -19.834 54.479 1.00 177.23 ? 27 ARG D NE 1 ATOM 3090 C CZ . ARG B 2 27 ? 9.648 -18.829 53.640 1.00 182.13 ? 27 ARG D CZ 1 ATOM 3091 N NH1 . ARG B 2 27 ? 8.645 -17.984 53.870 1.00 183.99 ? 27 ARG D NH1 1 ATOM 3092 N NH2 . ARG B 2 27 ? 10.408 -18.665 52.566 1.00 182.68 ? 27 ARG D NH2 1 ATOM 3093 N N . ARG B 2 28 ? 7.495 -22.729 60.121 1.00 165.40 ? 28 ARG D N 1 ATOM 3094 C CA . ARG B 2 28 ? 6.587 -22.589 61.263 1.00 165.75 ? 28 ARG D CA 1 ATOM 3095 C C . ARG B 2 28 ? 6.640 -23.739 62.267 1.00 163.10 ? 28 ARG D C 1 ATOM 3096 O O . ARG B 2 28 ? 5.864 -23.762 63.214 1.00 166.31 ? 28 ARG D O 1 ATOM 3097 C CB . ARG B 2 28 ? 5.138 -22.384 60.807 1.00 166.98 ? 28 ARG D CB 1 ATOM 3098 C CG . ARG B 2 28 ? 4.876 -21.081 60.075 1.00 167.80 ? 28 ARG D CG 1 ATOM 3099 C CD . ARG B 2 28 ? 3.483 -20.556 60.358 1.00 173.84 ? 28 ARG D CD 1 ATOM 3100 N NE . ARG B 2 28 ? 3.555 -19.256 61.024 1.00 184.19 ? 28 ARG D NE 1 ATOM 3101 C CZ . ARG B 2 28 ? 2.514 -18.460 61.261 1.00 186.77 ? 28 ARG D CZ 1 ATOM 3102 N NH1 . ARG B 2 28 ? 1.291 -18.821 60.888 1.00 192.31 ? 28 ARG D NH1 1 ATOM 3103 N NH2 . ARG B 2 28 ? 2.699 -17.297 61.873 1.00 179.48 ? 28 ARG D NH2 1 ATOM 3104 N N . SER B 2 29 ? 7.546 -24.691 62.080 1.00 157.63 ? 29 SER D N 1 ATOM 3105 C CA . SER B 2 29 ? 7.559 -25.850 62.962 1.00 151.54 ? 29 SER D CA 1 ATOM 3106 C C . SER B 2 29 ? 8.833 -26.674 62.886 1.00 154.39 ? 29 SER D C 1 ATOM 3107 O O . SER B 2 29 ? 9.723 -26.400 62.090 1.00 153.48 ? 29 SER D O 1 ATOM 3108 C CB . SER B 2 29 ? 6.374 -26.751 62.642 1.00 149.06 ? 29 SER D CB 1 ATOM 3109 O OG . SER B 2 29 ? 6.041 -27.569 63.740 1.00 144.81 ? 29 SER D OG 1 ATOM 3110 N N . PHE B 2 30 ? 8.879 -27.718 63.707 1.00 160.43 ? 30 PHE D N 1 ATOM 3111 C CA . PHE B 2 30 ? 10.064 -28.561 63.890 1.00 162.80 ? 30 PHE D CA 1 ATOM 3112 C C . PHE B 2 30 ? 10.600 -29.196 62.596 1.00 164.49 ? 30 PHE D C 1 ATOM 3113 O O . PHE B 2 30 ? 9.859 -29.447 61.641 1.00 158.56 ? 30 PHE D O 1 ATOM 3114 C CB . PHE B 2 30 ? 9.775 -29.667 64.922 1.00 157.02 ? 30 PHE D CB 1 ATOM 3115 C CG . PHE B 2 30 ? 8.627 -30.570 64.534 1.00 154.90 ? 30 PHE D CG 1 ATOM 3116 C CD1 . PHE B 2 30 ? 8.835 -31.675 63.730 1.00 148.51 ? 30 PHE D CD1 1 ATOM 3117 C CD2 . PHE B 2 30 ? 7.333 -30.295 64.953 1.00 154.97 ? 30 PHE D CD2 1 ATOM 3118 C CE1 . PHE B 2 30 ? 7.777 -32.496 63.359 1.00 143.36 ? 30 PHE D CE1 1 ATOM 3119 C CE2 . PHE B 2 30 ? 6.269 -31.118 64.580 1.00 148.66 ? 30 PHE D CE2 1 ATOM 3120 C CZ . PHE B 2 30 ? 6.497 -32.216 63.778 1.00 141.94 ? 30 PHE D CZ 1 ATOM 3121 N N . GLU B 2 31 ? 11.905 -29.434 62.588 1.00 170.78 ? 31 GLU D N 1 ATOM 3122 C CA . GLU B 2 31 ? 12.604 -30.042 61.465 1.00 178.93 ? 31 GLU D CA 1 ATOM 3123 C C . GLU B 2 31 ? 12.158 -31.480 61.236 1.00 182.88 ? 31 GLU D C 1 ATOM 3124 O O . GLU B 2 31 ? 11.846 -32.194 62.189 1.00 185.70 ? 31 GLU D O 1 ATOM 3125 C CB . GLU B 2 31 ? 14.114 -29.991 61.709 1.00 181.35 ? 31 GLU D CB 1 ATOM 3126 C CG . GLU B 2 31 ? 14.509 -30.227 63.157 1.00 186.23 ? 31 GLU D CG 1 ATOM 3127 C CD . GLU B 2 31 ? 13.927 -29.186 64.096 1.00 195.66 ? 31 GLU D CD 1 ATOM 3128 O OE1 . GLU B 2 31 ? 13.136 -29.564 64.985 1.00 197.61 ? 31 GLU D OE1 1 ATOM 3129 O OE2 . GLU B 2 31 ? 14.245 -27.987 63.936 1.00 199.92 ? 31 GLU D OE2 1 ATOM 3130 N N . VAL B 2 32 ? 12.138 -31.897 59.969 1.00 180.48 ? 32 VAL D N 1 ATOM 3131 C CA . VAL B 2 32 ? 11.697 -33.239 59.587 1.00 174.60 ? 32 VAL D CA 1 ATOM 3132 C C . VAL B 2 32 ? 12.439 -33.740 58.351 1.00 179.75 ? 32 VAL D C 1 ATOM 3133 O O . VAL B 2 32 ? 12.868 -32.932 57.521 1.00 187.56 ? 32 VAL D O 1 ATOM 3134 C CB . VAL B 2 32 ? 10.210 -33.245 59.255 1.00 165.89 ? 32 VAL D CB 1 ATOM 3135 C CG1 . VAL B 2 32 ? 9.409 -32.789 60.449 1.00 165.50 ? 32 VAL D CG1 1 ATOM 3136 C CG2 . VAL B 2 32 ? 9.944 -32.351 58.059 1.00 160.06 ? 32 VAL D CG2 1 ATOM 3137 N N . CYS B 2 33 ? 12.575 -35.064 58.219 1.00 173.64 ? 33 CYS D N 1 ATOM 3138 C CA . CYS B 2 33 ? 13.245 -35.659 57.050 1.00 169.24 ? 33 CYS D CA 1 ATOM 3139 C C . CYS B 2 33 ? 12.367 -35.664 55.795 1.00 167.40 ? 33 CYS D C 1 ATOM 3140 O O . CYS B 2 33 ? 11.195 -36.047 55.840 1.00 165.74 ? 33 CYS D O 1 ATOM 3141 C CB . CYS B 2 33 ? 13.757 -37.074 57.336 1.00 163.92 ? 33 CYS D CB 1 ATOM 3142 S SG . CYS B 2 33 ? 15.116 -37.153 58.527 1.00 185.45 ? 33 CYS D SG 1 ATOM 3143 N N . VAL B 2 34 ? 12.948 -35.226 54.680 1.00 162.88 ? 34 VAL D N 1 ATOM 3144 C CA . VAL B 2 34 ? 12.220 -35.083 53.428 1.00 157.12 ? 34 VAL D CA 1 ATOM 3145 C C . VAL B 2 34 ? 13.198 -35.318 52.276 1.00 159.57 ? 34 VAL D C 1 ATOM 3146 O O . VAL B 2 34 ? 14.396 -35.420 52.513 1.00 140.50 ? 34 VAL D O 1 ATOM 3147 C CB . VAL B 2 34 ? 11.616 -33.665 53.324 1.00 154.10 ? 34 VAL D CB 1 ATOM 3148 C CG1 . VAL B 2 34 ? 10.966 -33.262 54.642 1.00 147.88 ? 34 VAL D CG1 1 ATOM 3149 C CG2 . VAL B 2 34 ? 12.691 -32.648 52.947 1.00 156.56 ? 34 VAL D CG2 1 ATOM 3150 N N . PRO B 2 35 ? 12.694 -35.359 51.025 1.00 161.95 ? 35 PRO D N 1 ATOM 3151 C CA . PRO B 2 35 ? 13.462 -35.678 49.810 1.00 166.95 ? 35 PRO D CA 1 ATOM 3152 C C . PRO B 2 35 ? 14.627 -34.748 49.499 1.00 179.25 ? 35 PRO D C 1 ATOM 3153 O O . PRO B 2 35 ? 14.462 -33.532 49.497 1.00 181.46 ? 35 PRO D O 1 ATOM 3154 C CB . PRO B 2 35 ? 12.418 -35.547 48.702 1.00 161.88 ? 35 PRO D CB 1 ATOM 3155 C CG . PRO B 2 35 ? 11.159 -35.872 49.350 1.00 160.85 ? 35 PRO D CG 1 ATOM 3156 C CD . PRO B 2 35 ? 11.252 -35.293 50.735 1.00 161.76 ? 35 PRO D CD 1 ATOM 3157 N N . LYS B 2 36 ? 15.788 -35.330 49.216 1.00 192.58 ? 36 LYS D N 1 ATOM 3158 C CA . LYS B 2 36 ? 16.960 -34.563 48.832 1.00 207.18 ? 36 LYS D CA 1 ATOM 3159 C C . LYS B 2 36 ? 16.591 -33.656 47.661 1.00 230.46 ? 36 LYS D C 1 ATOM 3160 O O . LYS B 2 36 ? 15.840 -34.053 46.762 1.00 232.69 ? 36 LYS D O 1 ATOM 3161 C CB . LYS B 2 36 ? 18.105 -35.497 48.459 1.00 206.26 ? 36 LYS D CB 1 ATOM 3162 N N . THR B 2 37 ? 17.120 -32.436 47.681 1.00 249.32 ? 37 THR D N 1 ATOM 3163 C CA . THR B 2 37 ? 16.712 -31.401 46.739 1.00 266.50 ? 37 THR D CA 1 ATOM 3164 C C . THR B 2 37 ? 17.906 -30.813 45.993 1.00 291.15 ? 37 THR D C 1 ATOM 3165 O O . THR B 2 37 ? 18.983 -30.655 46.569 1.00 292.59 ? 37 THR D O 1 ATOM 3166 C CB . THR B 2 37 ? 15.990 -30.254 47.478 1.00 256.25 ? 37 THR D CB 1 ATOM 3167 O OG1 . THR B 2 37 ? 15.296 -30.775 48.618 1.00 249.08 ? 37 THR D OG1 1 ATOM 3168 C CG2 . THR B 2 37 ? 15.001 -29.548 46.554 1.00 256.79 ? 37 THR D CG2 1 ATOM 3169 N N . PRO B 2 38 ? 17.720 -30.485 44.702 1.00 158.73 ? 38 PRO D N 1 ATOM 3170 C CA . PRO B 2 38 ? 18.756 -29.773 43.940 1.00 162.03 ? 38 PRO D CA 1 ATOM 3171 C C . PRO B 2 38 ? 19.007 -28.370 44.492 1.00 159.48 ? 38 PRO D C 1 ATOM 3172 O O . PRO B 2 38 ? 18.070 -27.720 44.959 1.00 155.71 ? 38 PRO D O 1 ATOM 3173 C CB . PRO B 2 38 ? 18.160 -29.682 42.531 1.00 165.10 ? 38 PRO D CB 1 ATOM 3174 C CG . PRO B 2 38 ? 16.677 -29.849 42.729 1.00 167.74 ? 38 PRO D CG 1 ATOM 3175 C CD . PRO B 2 38 ? 16.548 -30.810 43.871 1.00 164.76 ? 38 PRO D CD 1 HETATM 3176 C C1 . NAG C 3 . ? -12.719 -14.030 28.652 1.00 192.89 ? 501 NAG A C1 1 HETATM 3177 C C2 . NAG C 3 . ? -13.710 -15.192 28.472 1.00 205.46 ? 501 NAG A C2 1 HETATM 3178 C C3 . NAG C 3 . ? -15.107 -14.772 27.993 1.00 204.43 ? 501 NAG A C3 1 HETATM 3179 C C4 . NAG C 3 . ? -15.577 -13.489 28.660 1.00 201.02 ? 501 NAG A C4 1 HETATM 3180 C C5 . NAG C 3 . ? -14.488 -12.423 28.598 1.00 196.94 ? 501 NAG A C5 1 HETATM 3181 C C6 . NAG C 3 . ? -14.975 -11.153 29.287 1.00 197.36 ? 501 NAG A C6 1 HETATM 3182 C C7 . NAG C 3 . ? -13.423 -17.480 27.636 1.00 208.47 ? 501 NAG A C7 1 HETATM 3183 C C8 . NAG C 3 . ? -13.120 -18.297 26.412 1.00 205.94 ? 501 NAG A C8 1 HETATM 3184 N N2 . NAG C 3 . ? -13.152 -16.175 27.549 1.00 210.51 ? 501 NAG A N2 1 HETATM 3185 O O3 . NAG C 3 . ? -16.054 -15.789 28.262 1.00 202.10 ? 501 NAG A O3 1 HETATM 3186 O O4 . NAG C 3 . ? -16.756 -13.030 28.028 1.00 198.98 ? 501 NAG A O4 1 HETATM 3187 O O5 . NAG C 3 . ? -13.308 -12.878 29.228 1.00 192.39 ? 501 NAG A O5 1 HETATM 3188 O O6 . NAG C 3 . ? -15.701 -11.488 30.453 1.00 195.55 ? 501 NAG A O6 1 HETATM 3189 O O7 . NAG C 3 . ? -13.895 -18.010 28.646 1.00 205.80 ? 501 NAG A O7 1 HETATM 3190 C C1 . NAG D 3 . ? -20.495 -8.494 80.489 1.00 185.79 ? 502 NAG A C1 1 HETATM 3191 C C2 . NAG D 3 . ? -21.304 -9.772 80.298 1.00 190.05 ? 502 NAG A C2 1 HETATM 3192 C C3 . NAG D 3 . ? -20.957 -10.760 81.408 1.00 192.26 ? 502 NAG A C3 1 HETATM 3193 C C4 . NAG D 3 . ? -19.450 -10.994 81.428 1.00 200.06 ? 502 NAG A C4 1 HETATM 3194 C C5 . NAG D 3 . ? -18.621 -9.705 81.305 1.00 203.26 ? 502 NAG A C5 1 HETATM 3195 C C6 . NAG D 3 . ? -17.157 -10.014 80.978 1.00 201.06 ? 502 NAG A C6 1 HETATM 3196 C C7 . NAG D 3 . ? -23.569 -9.666 81.198 1.00 187.55 ? 502 NAG A C7 1 HETATM 3197 C C8 . NAG D 3 . ? -23.831 -8.494 82.100 1.00 185.31 ? 502 NAG A C8 1 HETATM 3198 N N2 . NAG D 3 . ? -22.719 -9.456 80.205 1.00 188.28 ? 502 NAG A N2 1 HETATM 3199 O O3 . NAG D 3 . ? -21.607 -11.994 81.200 1.00 189.21 ? 502 NAG A O3 1 HETATM 3200 O O4 . NAG D 3 . ? -19.130 -11.639 82.640 1.00 204.84 ? 502 NAG A O4 1 HETATM 3201 O O5 . NAG D 3 . ? -19.127 -8.809 80.327 1.00 201.01 ? 502 NAG A O5 1 HETATM 3202 O O6 . NAG D 3 . ? -17.062 -10.634 79.712 1.00 197.26 ? 502 NAG A O6 1 HETATM 3203 O O7 . NAG D 3 . ? -24.122 -10.751 81.374 1.00 189.04 ? 502 NAG A O7 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . SER A 28 ? 2.1847 2.6224 3.3442 0.2643 -0.0020 -0.0196 41 SER A N 2 C CA . SER A 28 ? 2.2115 2.6639 3.3515 0.2508 0.0040 -0.0007 41 SER A CA 3 C C . SER A 28 ? 2.2577 2.7105 3.3729 0.2412 0.0109 0.0065 41 SER A C 4 O O . SER A 28 ? 2.2822 2.7289 3.3759 0.2249 -0.0005 0.0208 41 SER A O 5 C CB . SER A 28 ? 2.2186 2.6580 3.3534 0.2381 -0.0217 0.0104 41 SER A CB 6 N N . LEU A 29 ? 2.2581 2.7179 3.3758 0.2513 0.0299 -0.0036 42 LEU A N 7 C CA . LEU A 29 ? 2.2339 2.6932 3.3297 0.2440 0.0374 0.0009 42 LEU A CA 8 C C . LEU A 29 ? 2.2092 2.6868 3.2842 0.2302 0.0489 0.0186 42 LEU A C 9 O O . LEU A 29 ? 2.1820 2.6483 3.2345 0.2140 0.0356 0.0302 42 LEU A O 10 C CB . LEU A 29 ? 2.1880 2.6564 3.2930 0.2588 0.0596 -0.0132 42 LEU A CB 11 N N . LYS A 30 ? 2.2310 2.7364 3.3135 0.2365 0.0737 0.0201 43 LYS A N 12 C CA . LYS A 30 ? 2.2971 2.8230 3.3635 0.2247 0.0865 0.0356 43 LYS A CA 13 C C . LYS A 30 ? 2.3706 2.8906 3.4297 0.2104 0.0671 0.0492 43 LYS A C 14 O O . LYS A 30 ? 2.3995 2.9254 3.4381 0.1949 0.0678 0.0634 43 LYS A O 15 C CB . LYS A 30 ? 2.2525 2.8082 3.3322 0.2363 0.1150 0.0329 43 LYS A CB 16 N N . ARG A 31 ? 2.3794 2.8880 3.4552 0.2155 0.0503 0.0446 44 ARG A N 17 C CA . ARG A 31 ? 2.3711 2.8717 3.4416 0.2029 0.0297 0.0564 44 ARG A CA 18 C C . ARG A 31 ? 2.3866 2.8615 3.4341 0.1868 0.0062 0.0638 44 ARG A C 19 O O . ARG A 31 ? 2.3785 2.8516 3.4088 0.1705 -0.0036 0.0784 44 ARG A O 20 C CB . ARG A 31 ? 2.3251 2.8176 3.4197 0.2130 0.0166 0.0481 44 ARG A CB 21 N N . VAL A 32 ? 2.3870 2.8419 3.4341 0.1916 -0.0027 0.0533 45 VAL A N 22 C CA . VAL A 32 ? 2.4099 2.8383 3.4349 0.1779 -0.0248 0.0585 45 VAL A CA 23 C C . VAL A 32 ? 2.4460 2.8828 3.4432 0.1642 -0.0121 0.0699 45 VAL A C 24 O O . VAL A 32 ? 2.4563 2.8822 3.4306 0.1463 -0.0260 0.0831 45 VAL A O 25 C CB . VAL A 32 ? 2.3721 2.7780 3.4058 0.1881 -0.0361 0.0427 45 VAL A CB 26 C CG1 . VAL A 32 ? 2.3999 2.7830 3.4073 0.1748 -0.0512 0.0479 45 VAL A CG1 27 C CG2 . VAL A 32 ? 2.3258 2.7152 3.3815 0.1959 -0.0576 0.0336 45 VAL A CG2 28 N N . VAL A 33 ? 2.4621 2.9180 3.4613 0.1725 0.0143 0.0645 46 VAL A N 29 C CA . VAL A 33 ? 2.4862 2.9538 3.4614 0.1609 0.0298 0.0742 46 VAL A CA 30 C C . VAL A 33 ? 2.4826 2.9651 3.4452 0.1457 0.0328 0.0907 46 VAL A C 31 O O . VAL A 33 ? 2.5014 2.9778 3.4378 0.1280 0.0277 0.1025 46 VAL A O 32 C CB . VAL A 33 ? 2.1002 2.5913 3.0840 0.1742 0.0607 0.0656 46 VAL A CB 33 C CG1 . VAL A 33 ? 2.0844 2.5947 3.0471 0.1622 0.0799 0.0768 46 VAL A CG1 34 C CG2 . VAL A 33 ? 2.0788 2.5534 3.0670 0.1846 0.0581 0.0513 46 VAL A CG2 35 N N . TRP A 34 ? 2.4475 2.9488 3.4286 0.1526 0.0409 0.0913 47 TRP A N 36 C CA . TRP A 34 ? 2.4101 2.9275 3.3829 0.1399 0.0445 0.1058 47 TRP A CA 37 C C . TRP A 34 ? 2.3889 2.8835 3.3403 0.1202 0.0180 0.1180 47 TRP A C 38 O O . TRP A 34 ? 2.3729 2.8747 3.3037 0.1034 0.0213 0.1312 47 TRP A O 39 C CB . TRP A 34 ? 2.3748 2.9090 3.3727 0.1512 0.0505 0.1031 47 TRP A CB 40 N N . ALA A 35 ? 2.3909 2.8581 3.3479 0.1222 -0.0083 0.1132 48 ALA A N 41 C CA . ALA A 35 ? 2.4185 2.8592 3.3548 0.1046 -0.0364 0.1234 48 ALA A CA 42 C C . ALA A 35 ? 2.3943 2.8121 3.3065 0.0954 -0.0461 0.1237 48 ALA A C 43 O O . ALA A 35 ? 2.3878 2.7865 3.2754 0.0773 -0.0644 0.1347 48 ALA A O 44 C CB . ALA A 35 ? 2.4178 2.8391 3.3713 0.1104 -0.0617 0.1183 48 ALA A CB 45 N N . LEU A 36 ? 2.3517 2.7701 3.2707 0.1079 -0.0345 0.1116 49 LEU A N 46 C CA . LEU A 36 ? 2.3332 2.7319 3.2306 0.1009 -0.0410 0.1108 49 LEU A CA 47 C C . LEU A 36 ? 2.3779 2.7854 3.2452 0.0822 -0.0299 0.1248 49 LEU A C 48 O O . LEU A 36 ? 2.4370 2.8236 3.2785 0.0641 -0.0483 0.1351 49 LEU A O 49 C CB . LEU A 36 ? 2.2429 2.6458 3.1552 0.1188 -0.0264 0.0950 49 LEU A CB 50 N N . CYS A 37 ? 2.3165 2.7549 3.1872 0.0863 0.0004 0.1249 50 CYS A N 51 C CA . CYS A 37 ? 2.2913 2.7422 3.1362 0.0695 0.0145 0.1369 50 CYS A CA 52 C C . CYS A 37 ? 2.2944 2.7513 3.1283 0.0527 0.0085 0.1519 50 CYS A C 53 O O . CYS A 37 ? 2.3087 2.7652 3.1158 0.0337 0.0103 0.1634 50 CYS A O 54 C CB . CYS A 37 ? 2.2440 2.7272 3.0985 0.0798 0.0484 0.1317 50 CYS A CB 55 N N . PHE A 38 ? 2.2686 2.7309 3.1230 0.0593 0.0018 0.1515 51 PHE A N 56 C CA . PHE A 38 ? 2.2436 2.7104 3.0894 0.0442 -0.0055 0.1652 51 PHE A CA 57 C C . PHE A 38 ? 2.2920 2.7249 3.1130 0.0263 -0.0358 0.1739 51 PHE A C 58 O O . PHE A 38 ? 2.3277 2.7599 3.1252 0.0064 -0.0388 0.1873 51 PHE A O 59 C CB . PHE A 38 ? 2.1798 2.6593 3.0538 0.0564 -0.0061 0.1621 51 PHE A CB 60 N N . MET A 39 ? 2.2944 2.6987 3.1207 0.0335 -0.0583 0.1657 52 MET A N 61 C CA . MET A 39 ? 2.3332 2.7017 3.1366 0.0183 -0.0890 0.1721 52 MET A CA 62 C C . MET A 39 ? 2.3404 2.6943 3.1149 0.0074 -0.0884 0.1743 52 MET A C 63 O O . MET A 39 ? 2.3719 2.6975 3.1202 -0.0091 -0.1106 0.1822 52 MET A O 64 C CB . MET A 39 ? 2.3167 2.6607 3.1389 0.0307 -0.1140 0.1618 52 MET A CB 65 N N . GLY A 40 ? 2.2692 2.6418 3.0484 0.0167 -0.0631 0.1672 53 GLY A N 66 C CA . GLY A 40 ? 2.2093 2.5733 2.9620 0.0066 -0.0578 0.1694 53 GLY A CA 67 C C . GLY A 40 ? 2.1459 2.5236 2.8723 -0.0143 -0.0451 0.1840 53 GLY A C 68 O O . GLY A 40 ? 2.1356 2.4940 2.8304 -0.0325 -0.0547 0.1920 53 GLY A O 69 N N . SER A 41 ? 2.0733 2.4845 2.8132 -0.0118 -0.0234 0.1869 54 SER A N 70 C CA . SER A 41 ? 2.0023 2.4309 2.7219 -0.0307 -0.0096 0.1999 54 SER A CA 71 C C . SER A 41 ? 1.9868 2.3888 2.6767 -0.0542 -0.0344 0.2132 54 SER A C 72 O O . SER A 41 ? 1.9504 2.3424 2.6091 -0.0724 -0.0345 0.2209 54 SER A O 73 C CB . SER A 41 ? 1.9323 2.3963 2.6750 -0.0234 0.0099 0.2008 54 SER A CB 74 N N . LEU A 42 ? 2.0102 2.4008 2.7097 -0.0539 -0.0553 0.2160 55 LEU A N 75 C CA . LEU A 42 ? 2.0242 2.3882 2.6977 -0.0750 -0.0811 0.2283 55 LEU A CA 76 C C . LEU A 42 ? 2.0346 2.3586 2.6839 -0.0828 -0.1053 0.2280 55 LEU A C 77 O O . LEU A 42 ? 2.0220 2.3224 2.6414 -0.1035 -0.1236 0.2390 55 LEU A O 78 C CB . LEU A 42 ? 1.9754 2.3359 2.6680 -0.0703 -0.0983 0.2297 55 LEU A CB 79 N N . ALA A 43 ? 2.0244 2.3401 2.6867 -0.0661 -0.1060 0.2151 56 ALA A N 80 C CA . ALA A 43 ? 2.0327 2.3128 2.6724 -0.0724 -0.1260 0.2137 56 ALA A CA 81 C C . ALA A 43 ? 2.0425 2.3214 2.6462 -0.0924 -0.1151 0.2228 56 ALA A C 82 O O . ALA A 43 ? 2.0127 2.2683 2.5847 -0.1139 -0.1324 0.2343 56 ALA A O 83 C CB . ALA A 43 ? 2.0045 2.2813 2.6666 -0.0501 -0.1238 0.1973 56 ALA A CB 84 N N . LEU A 44 ? 2.0815 2.3860 2.6902 -0.0855 -0.0860 0.2176 57 LEU A N 85 C CA . LEU A 44 ? 2.1323 2.4399 2.7099 -0.1028 -0.0717 0.2247 57 LEU A CA 86 C C . LEU A 44 ? 2.1018 2.4182 2.6580 -0.1256 -0.0681 0.2398 57 LEU A C 87 O O . LEU A 44 ? 2.1361 2.4331 2.6566 -0.1475 -0.0766 0.2495 57 LEU A O 88 C CB . LEU A 44 ? 2.1615 2.5015 2.7536 -0.0897 -0.0380 0.2162 57 LEU A CB 89 C CG . LEU A 44 ? 2.1387 2.4847 2.7619 -0.0629 -0.0313 0.1998 57 LEU A CG 90 C CD1 . LEU A 44 ? 2.0673 2.4478 2.7004 -0.0538 0.0041 0.1941 57 LEU A CD1 91 C CD2 . LEU A 44 ? 2.1381 2.4473 2.7516 -0.0600 -0.0544 0.1935 57 LEU A CD2 92 N N . LEU A 45 ? 2.0343 2.3794 2.6124 -0.1205 -0.0557 0.2414 58 LEU A N 93 C CA . LEU A 45 ? 2.0275 2.3865 2.5901 -0.1403 -0.0488 0.2543 58 LEU A CA 94 C C . LEU A 45 ? 2.1562 2.4797 2.6846 -0.1637 -0.0769 0.2664 58 LEU A C 95 O O . LEU A 45 ? 2.1807 2.4992 2.6765 -0.1856 -0.0728 0.2757 58 LEU A O 96 C CB . LEU A 45 ? 1.9621 2.3477 2.5555 -0.1295 -0.0412 0.2536 58 LEU A CB 97 N N . ALA A 46 ? 2.2530 2.5519 2.7890 -0.1594 -0.1053 0.2660 59 ALA A N 98 C CA . ALA A 46 ? 2.3364 2.5972 2.8411 -0.1796 -0.1356 0.2762 59 ALA A CA 99 C C . ALA A 46 ? 2.3667 2.5954 2.8430 -0.1871 -0.1478 0.2752 59 ALA A C 100 O O . ALA A 46 ? 2.4171 2.6211 2.8564 -0.2101 -0.1616 0.2859 59 ALA A O 101 C CB . ALA A 46 ? 2.3521 2.5945 2.8747 -0.1707 -0.1631 0.2744 59 ALA A CB 102 N N . LEU A 47 ? 2.3451 2.5735 2.8383 -0.1678 -0.1431 0.2623 60 LEU A N 103 C CA . LEU A 47 ? 2.3794 2.5782 2.8482 -0.1729 -0.1542 0.2601 60 LEU A CA 104 C C . LEU A 47 ? 2.4400 2.6434 2.8735 -0.1946 -0.1377 0.2692 60 LEU A C 105 O O . LEU A 47 ? 2.5424 2.7176 2.9392 -0.2172 -0.1548 0.2798 60 LEU A O 106 C CB . LEU A 47 ? 2.2922 2.4975 2.7874 -0.1481 -0.1454 0.2442 60 LEU A CB 107 N N . VAL A 48 ? 2.3366 2.5755 2.7812 -0.1880 -0.1044 0.2649 61 VAL A N 108 C CA . VAL A 48 ? 2.2422 2.4917 2.6577 -0.2074 -0.0845 0.2724 61 VAL A CA 109 C C . VAL A 48 ? 2.1665 2.4137 2.5570 -0.2328 -0.0893 0.2872 61 VAL A C 110 O O . VAL A 48 ? 2.1650 2.3917 2.5167 -0.2559 -0.0957 0.2962 61 VAL A O 111 C CB . VAL A 48 ? 2.1526 2.4462 2.5908 -0.1946 -0.0474 0.2653 61 VAL A CB 112 N N . CYS A 49 ? 2.0891 2.3569 2.5014 -0.2287 -0.0863 0.2895 62 CYS A N 113 C CA . CYS A 49 ? 2.1135 2.3831 2.5057 -0.2515 -0.0887 0.3029 62 CYS A CA 114 C C . CYS A 49 ? 2.2704 2.4944 2.6229 -0.2737 -0.1198 0.3129 62 CYS A C 115 O O . CYS A 49 ? 2.3171 2.5349 2.6350 -0.2986 -0.1165 0.3232 62 CYS A O 116 C CB . CYS A 49 ? 2.0363 2.3254 2.4593 -0.2414 -0.0897 0.3031 62 CYS A CB 117 S SG . CYS A 49 ? 2.8949 3.1887 3.2971 -0.2681 -0.0921 0.3188 62 CYS A SG 118 N N . THR A 50 ? 2.3594 2.5510 2.7166 -0.2649 -0.1499 0.3096 63 THR A N 119 C CA . THR A 50 ? 2.4506 2.5963 2.7711 -0.2845 -0.1820 0.3185 63 THR A CA 120 C C . THR A 50 ? 2.5070 2.6301 2.7940 -0.2957 -0.1829 0.3190 63 THR A C 121 O O . THR A 50 ? 2.5883 2.6812 2.8350 -0.3195 -0.1989 0.3293 63 THR A O 122 C CB . THR A 50 ? 2.4407 2.5573 2.7768 -0.2713 -0.2152 0.3138 63 THR A CB 123 O OG1 . THR A 50 ? 2.4318 2.5505 2.7948 -0.2462 -0.2128 0.2991 63 THR A OG1 124 C CG2 . THR A 50 ? 2.3594 2.4920 2.7211 -0.2655 -0.2189 0.3161 63 THR A CG2 125 N N . ASN A 51 ? 2.4375 2.5745 2.7406 -0.2787 -0.1659 0.3077 64 ASN A N 126 C CA . ASN A 51 ? 2.4441 2.5657 2.7175 -0.2884 -0.1615 0.3076 64 ASN A CA 127 C C . ASN A 51 ? 2.3751 2.5085 2.6158 -0.3144 -0.1422 0.3185 64 ASN A C 128 O O . ASN A 51 ? 2.3670 2.4696 2.5663 -0.3380 -0.1569 0.3279 64 ASN A O 129 C CB . ASN A 51 ? 2.4809 2.6221 2.7811 -0.2646 -0.1422 0.2934 64 ASN A CB 130 C CG . ASN A 51 ? 2.5425 2.6728 2.8755 -0.2393 -0.1601 0.2817 64 ASN A CG 131 O OD1 . ASN A 51 ? 2.5671 2.6658 2.8957 -0.2413 -0.1916 0.2840 64 ASN A OD1 132 N ND2 . ASN A 51 ? 2.5343 2.6907 2.9005 -0.2155 -0.1401 0.2688 64 ASN A ND2 133 N N . ARG A 52 ? 2.2912 2.4692 2.5509 -0.3102 -0.1092 0.3167 65 ARG A N 134 C CA . ARG A 52 ? 2.2165 2.4111 2.4507 -0.3339 -0.0887 0.3260 65 ARG A CA 135 C C . ARG A 52 ? 2.2114 2.3860 2.4179 -0.3587 -0.1074 0.3398 65 ARG A C 136 O O . ARG A 52 ? 2.2675 2.4367 2.4384 -0.3844 -0.1014 0.3490 65 ARG A O 137 C CB . ARG A 52 ? 2.1005 2.3476 2.3659 -0.3228 -0.0529 0.3211 65 ARG A CB 138 N N . ILE A 53 ? 2.1735 2.3373 2.3960 -0.3516 -0.1295 0.3411 66 ILE A N 139 C CA . ILE A 53 ? 2.2375 2.3780 2.4330 -0.3746 -0.1505 0.3541 66 ILE A CA 140 C C . ILE A 53 ? 2.3442 2.4333 2.4976 -0.3913 -0.1796 0.3598 66 ILE A C 141 O O . ILE A 53 ? 2.3393 2.4085 2.4544 -0.4183 -0.1885 0.3717 66 ILE A O 142 C CB . ILE A 53 ? 2.1838 2.3244 2.4073 -0.3625 -0.1682 0.3540 66 ILE A CB 143 C CG1 . ILE A 53 ? 2.1198 2.3096 2.3795 -0.3507 -0.1408 0.3508 66 ILE A CG1 144 C CG2 . ILE A 53 ? 2.1816 2.2906 2.3731 -0.3866 -0.1944 0.3672 66 ILE A CG2 145 C CD1 . ILE A 53 ? 2.0486 2.2431 2.3444 -0.3314 -0.1542 0.3468 66 ILE A CD1 146 N N . GLN A 54 ? 2.4182 2.4857 2.5790 -0.3751 -0.1943 0.3511 67 GLN A N 147 C CA . GLN A 54 ? 2.5059 2.5238 2.6294 -0.3880 -0.2229 0.3550 67 GLN A CA 148 C C . GLN A 54 ? 2.5818 2.5955 2.6673 -0.4082 -0.2074 0.3594 67 GLN A C 149 O O . GLN A 54 ? 2.6372 2.6155 2.6789 -0.4324 -0.2249 0.3692 67 GLN A O 150 C CB . GLN A 54 ? 2.4550 2.4542 2.6002 -0.3637 -0.2408 0.3429 67 GLN A CB 151 N N . TYR A 55 ? 2.5505 2.6002 2.6526 -0.3982 -0.1744 0.3521 68 TYR A N 152 C CA . TYR A 55 ? 2.5249 2.5756 2.5951 -0.4153 -0.1561 0.3549 68 TYR A CA 153 C C . TYR A 55 ? 2.5513 2.6026 2.5862 -0.4468 -0.1494 0.3683 68 TYR A C 154 O O . TYR A 55 ? 2.6613 2.6920 2.6547 -0.4691 -0.1498 0.3745 68 TYR A O 155 C CB . TYR A 55 ? 2.4211 2.5148 2.5203 -0.3974 -0.1206 0.3441 68 TYR A CB 156 N N . TYR A 56 ? 2.4609 2.5354 2.5119 -0.4491 -0.1433 0.3726 69 TYR A N 157 C CA . TYR A 56 ? 2.5087 2.5827 2.5276 -0.4790 -0.1389 0.3851 69 TYR A CA 158 C C . TYR A 56 ? 2.6402 2.6632 2.6205 -0.4995 -0.1755 0.3960 69 TYR A C 159 O O . TYR A 56 ? 2.7101 2.7207 2.6520 -0.5283 -0.1760 0.4070 69 TYR A O 160 C CB . TYR A 56 ? 2.4613 2.5766 2.5107 -0.4745 -0.1210 0.3860 69 TYR A CB 161 C CG . TYR A 56 ? 2.4884 2.6027 2.5077 -0.5047 -0.1191 0.3987 69 TYR A CG 162 C CD1 . TYR A 56 ? 2.5767 2.6902 2.5588 -0.5303 -0.1034 0.4042 69 TYR A CD1 163 C CD2 . TYR A 56 ? 2.0727 2.1865 2.1006 -0.5079 -0.1327 0.4048 69 TYR A CD2 164 C CE1 . TYR A 56 ? 2.6330 2.7453 2.5872 -0.5586 -0.1012 0.4153 69 TYR A CE1 165 C CE2 . TYR A 56 ? 2.4773 2.5901 2.4777 -0.5357 -0.1307 0.4161 69 TYR A CE2 166 C CZ . TYR A 56 ? 2.5542 2.6663 2.5178 -0.5612 -0.1148 0.4212 69 TYR A CZ 167 O OH . TYR A 56 ? 2.5226 2.6335 2.4583 -0.5896 -0.1123 0.4319 69 TYR A OH 168 N N . PHE A 57 ? 2.6657 2.6588 2.6560 -0.4848 -0.2061 0.3927 70 PHE A N 169 C CA . PHE A 57 ? 2.7401 2.6837 2.6968 -0.5018 -0.2431 0.4023 70 PHE A CA 170 C C . PHE A 57 ? 2.7880 2.6914 2.6997 -0.5181 -0.2560 0.4055 70 PHE A C 171 O O . PHE A 57 ? 2.8302 2.6942 2.7003 -0.5416 -0.2794 0.4161 70 PHE A O 172 C CB . PHE A 57 ? 2.7630 2.6907 2.7489 -0.4799 -0.2712 0.3970 70 PHE A CB 173 N N . LEU A 58 ? 2.0477 2.3183 1.4759 0.0283 -0.4632 -0.4368 71 LEU A N 174 C CA . LEU A 58 ? 2.1482 2.3849 1.5932 0.0445 -0.4448 -0.4260 71 LEU A CA 175 C C . LEU A 58 ? 2.3260 2.5464 1.7864 0.0166 -0.4470 -0.4154 71 LEU A C 176 O O . LEU A 58 ? 2.3561 2.5474 1.8298 0.0253 -0.4328 -0.4069 71 LEU A O 177 C CB . LEU A 58 ? 2.0303 2.3038 1.5083 0.0791 -0.4311 -0.4024 71 LEU A CB 178 N N . TYR A 59 ? 2.4309 2.6727 1.8904 -0.0161 -0.4658 -0.4150 72 TYR A N 179 C CA . TYR A 59 ? 2.4670 2.7033 1.9447 -0.0440 -0.4711 -0.4027 72 TYR A CA 180 C C . TYR A 59 ? 2.5144 2.7608 2.0310 -0.0244 -0.4553 -0.3760 72 TYR A C 181 O O . TYR A 59 ? 2.6067 2.8133 2.1253 -0.0250 -0.4429 -0.3764 72 TYR A O 182 C CB . TYR A 59 ? 2.5023 2.6770 1.9497 -0.0705 -0.4703 -0.4258 72 TYR A CB 183 C CG . TYR A 59 ? 2.6554 2.8233 2.0710 -0.1068 -0.4915 -0.4466 72 TYR A CG 184 C CD1 . TYR A 59 ? 2.7254 2.9019 2.1500 -0.1434 -0.5090 -0.4393 72 TYR A CD1 185 C CD2 . TYR A 59 ? 2.7043 2.8560 2.0805 -0.1045 -0.4954 -0.4737 72 TYR A CD2 186 C CE1 . TYR A 59 ? 2.7884 2.9552 2.1828 -0.1779 -0.5311 -0.4582 72 TYR A CE1 187 C CE2 . TYR A 59 ? 2.7394 2.8805 2.0827 -0.1395 -0.5154 -0.4946 72 TYR A CE2 188 C CZ . TYR A 59 ? 2.7738 2.9216 2.1260 -0.1767 -0.5338 -0.4866 72 TYR A CZ 189 O OH . TYR A 59 ? 2.7992 2.9328 2.1183 -0.2118 -0.5566 -0.5068 72 TYR A OH 190 N N . PRO A 60 ? 2.4561 2.7556 2.0032 -0.0070 -0.4551 -0.3534 73 PRO A N 191 C CA . PRO A 60 ? 2.3521 2.6648 1.9347 0.0139 -0.4395 -0.3285 73 PRO A CA 192 C C . PRO A 60 ? 2.3207 2.6428 1.9311 -0.0073 -0.4452 -0.3101 73 PRO A C 193 O O . PRO A 60 ? 2.3505 2.6930 1.9636 -0.0339 -0.4651 -0.3087 73 PRO A O 194 C CB . PRO A 60 ? 2.3767 2.7459 1.9767 0.0332 -0.4405 -0.3144 73 PRO A CB 195 C CG . PRO A 60 ? 2.4613 2.8621 2.0522 0.0104 -0.4636 -0.3207 73 PRO A CG 196 C CD . PRO A 60 ? 2.5081 2.8611 2.0582 -0.0113 -0.4720 -0.3500 73 PRO A CD 197 N N . HIS A 61 ? 2.2843 2.5935 1.9163 0.0051 -0.4291 -0.2957 74 HIS A N 198 C CA . HIS A 61 ? 2.2970 2.6181 1.9588 -0.0112 -0.4331 -0.2767 74 HIS A CA 199 C C . HIS A 61 ? 2.2163 2.5597 1.9130 0.0112 -0.4192 -0.2515 74 HIS A C 200 O O . HIS A 61 ? 2.1522 2.4982 1.8486 0.0381 -0.4053 -0.2493 74 HIS A O 201 C CB . HIS A 61 ? 2.3361 2.6070 1.9843 -0.0294 -0.4285 -0.2890 74 HIS A CB 202 C CG . HIS A 61 ? 2.3143 2.5403 1.9516 -0.0062 -0.4061 -0.2970 74 HIS A CG 203 N ND1 . HIS A 61 ? 2.3457 2.5199 1.9505 -0.0093 -0.4007 -0.3209 74 HIS A ND1 204 C CD2 . HIS A 61 ? 2.1782 2.4023 1.8332 0.0207 -0.3887 -0.2837 74 HIS A CD2 205 C CE1 . HIS A 61 ? 2.2270 2.3717 1.8324 0.0164 -0.3823 -0.3199 74 HIS A CE1 206 N NE2 . HIS A 61 ? 2.1532 2.3273 1.7879 0.0339 -0.3750 -0.2981 74 HIS A NE2 207 N N . VAL A 62 ? 2.2223 2.5807 1.9492 -0.0008 -0.4232 -0.2329 75 VAL A N 208 C CA . VAL A 62 ? 2.2179 2.5936 1.9777 0.0172 -0.4105 -0.2095 75 VAL A CA 209 C C . VAL A 62 ? 2.2039 2.5663 1.9825 0.0068 -0.4086 -0.2044 75 VAL A C 210 O O . VAL A 62 ? 2.3171 2.6912 2.1031 -0.0134 -0.4252 -0.2112 75 VAL A O 211 C CB . VAL A 62 ? 2.4129 2.8479 2.2037 0.0222 -0.4205 -0.1870 75 VAL A CB 212 C CG1 . VAL A 62 ? 2.3895 2.8530 2.2153 0.0030 -0.4371 -0.1691 75 VAL A CG1 213 C CG2 . VAL A 62 ? 2.3889 2.8349 2.1967 0.0488 -0.4025 -0.1710 75 VAL A CG2 214 N N . THR A 63 ? 2.0289 2.3740 1.8174 0.0252 -0.3900 -0.1986 76 THR A N 215 C CA . THR A 63 ? 1.9190 2.2575 1.7269 0.0245 -0.3883 -0.2010 76 THR A CA 216 C C . THR A 63 ? 1.7341 2.1239 1.5892 0.0313 -0.3930 -0.1774 76 THR A C 217 O O . THR A 63 ? 1.6594 2.0567 1.5281 0.0504 -0.3800 -0.1619 76 THR A O 218 C CB . THR A 63 ? 2.0371 2.3287 1.8313 0.0425 -0.3661 -0.2075 76 THR A CB 219 O OG1 . THR A 63 ? 2.1380 2.4338 1.9323 0.0611 -0.3524 -0.1938 76 THR A OG1 220 C CG2 . THR A 63 ? 2.0880 2.3258 1.8436 0.0362 -0.3610 -0.2307 76 THR A CG2 221 N N . LYS A 64 ? 1.7563 2.1818 1.6392 0.0156 -0.4108 -0.1744 77 LYS A N 222 C CA . LYS A 64 ? 1.7567 2.2391 1.6919 0.0228 -0.4160 -0.1492 77 LYS A CA 223 C C . LYS A 64 ? 1.8125 2.2938 1.7744 0.0312 -0.4081 -0.1490 77 LYS A C 224 O O . LYS A 64 ? 1.9507 2.4306 1.9204 0.0162 -0.4167 -0.1616 77 LYS A O 225 C CB . LYS A 64 ? 1.6937 2.2250 1.6535 0.0033 -0.4399 -0.1426 77 LYS A CB 226 N N . LEU A 65 ? 1.6736 2.1560 1.6504 0.0545 -0.3922 -0.1350 78 LEU A N 227 C CA . LEU A 65 ? 1.6183 2.0981 1.6195 0.0667 -0.3834 -0.1353 78 LEU A CA 228 C C . LEU A 65 ? 1.6625 2.2095 1.7276 0.0715 -0.3891 -0.1092 78 LEU A C 229 O O . LEU A 65 ? 1.6847 2.2656 1.7730 0.0806 -0.3879 -0.0846 78 LEU A O 230 C CB . LEU A 65 ? 1.5368 1.9768 1.5176 0.0892 -0.3624 -0.1364 78 LEU A CB 231 C CG . LEU A 65 ? 1.4861 1.9372 1.5006 0.1096 -0.3518 -0.1260 78 LEU A CG 232 C CD1 . LEU A 65 ? 1.4419 1.8331 1.4208 0.1233 -0.3351 -0.1423 78 LEU A CD1 233 C CD2 . LEU A 65 ? 1.5222 2.0186 1.5733 0.1221 -0.3481 -0.0946 78 LEU A CD2 234 N N . ASP A 66 ? 1.7278 2.2944 1.8247 0.0658 -0.3939 -0.1135 79 ASP A N 235 C CA . ASP A 66 ? 1.7806 2.4160 1.9455 0.0716 -0.3956 -0.0862 79 ASP A CA 236 C C . ASP A 66 ? 1.8649 2.5075 2.0653 0.0834 -0.3855 -0.0886 79 ASP A C 237 O O . ASP A 66 ? 1.9639 2.5749 2.1470 0.0726 -0.3893 -0.1152 79 ASP A O 238 C CB . ASP A 66 ? 1.8466 2.5277 2.0333 0.0463 -0.4158 -0.0820 79 ASP A CB 239 C CG . ASP A 66 ? 1.9363 2.6771 2.1685 0.0544 -0.4180 -0.0493 79 ASP A CG 240 O OD1 . ASP A 66 ? 1.9384 2.6741 2.1717 0.0757 -0.4057 -0.0326 79 ASP A OD1 241 O OD2 . ASP A 66 ? 1.9749 2.7655 2.2408 0.0393 -0.4311 -0.0415 79 ASP A OD2 242 N N . GLU A 67 ? 1.8132 2.4932 2.0643 0.1066 -0.3714 -0.0607 80 GLU A N 243 C CA . GLU A 67 ? 1.7097 2.4080 2.0074 0.1215 -0.3584 -0.0577 80 GLU A CA 244 C C . GLU A 67 ? 1.5956 2.3737 1.9644 0.1157 -0.3582 -0.0277 80 GLU A C 245 O O . GLU A 67 ? 1.6063 2.4185 2.0079 0.1274 -0.3509 0.0049 80 GLU A O 246 C CB . GLU A 67 ? 1.6453 2.3171 1.9497 0.1527 -0.3330 -0.0433 80 GLU A CB 247 C CG . GLU A 67 ? 1.6226 2.2337 1.8627 0.1609 -0.3333 -0.0622 80 GLU A CG 248 C CD . GLU A 67 ? 1.6919 2.2250 1.8885 0.1586 -0.3220 -0.0923 80 GLU A CD 249 O OE1 . GLU A 67 ? 1.7514 2.2634 1.9675 0.1485 -0.3041 -0.0927 80 GLU A OE1 250 O OE2 . GLU A 67 ? 1.6951 2.1848 1.8366 0.1648 -0.3273 -0.1124 80 GLU A OE2 251 N N . VAL A 68 ? 1.5158 2.2942 1.9002 0.0918 -0.3564 -0.0342 81 VAL A N 252 C CA . VAL A 68 ? 1.5202 2.3778 1.9739 0.0852 -0.3546 -0.0040 81 VAL A CA 253 C C . VAL A 68 ? 1.6870 2.5237 2.1785 0.0894 -0.3205 0.0089 81 VAL A C 254 O O . VAL A 68 ? 1.8567 2.6273 2.3188 0.0766 -0.3088 -0.0137 81 VAL A O 255 C CB . VAL A 68 ? 1.3906 2.2923 1.8438 0.0491 -0.3845 -0.0159 81 VAL A CB 256 C CG1 . VAL A 68 ? 1.3789 2.2042 1.7636 0.0261 -0.3969 -0.0589 81 VAL A CG1 257 C CG2 . VAL A 68 ? 1.3188 2.2678 1.8334 0.0354 -0.3727 0.0060 81 VAL A CG2 258 N N . ALA A 69 ? 1.6652 2.5597 2.2218 0.1083 -0.3038 0.0459 82 ALA A N 259 C CA . ALA A 69 ? 1.6886 2.5693 2.2838 0.1145 -0.2701 0.0590 82 ALA A CA 260 C C . ALA A 69 ? 1.6069 2.5656 2.2584 0.0953 -0.2756 0.0791 82 ALA A C 261 O O . ALA A 69 ? 1.5837 2.6259 2.2898 0.1065 -0.2796 0.1124 82 ALA A O 262 C CB . ALA A 69 ? 1.7064 2.5824 2.3335 0.1530 -0.2400 0.0847 82 ALA A CB 263 N N . ALA A 70 ? 1.5748 2.5075 2.2140 0.0665 -0.2750 0.0607 83 ALA A N 264 C CA . ALA A 70 ? 1.6323 2.6367 2.3233 0.0443 -0.2795 0.0784 83 ALA A CA 265 C C . ALA A 70 ? 1.5698 2.5777 2.3103 0.0611 -0.2410 0.1010 83 ALA A C 266 O O . ALA A 70 ? 1.5027 2.4543 2.2340 0.0889 -0.2119 0.1003 83 ALA A O 267 C CB . ALA A 70 ? 1.7136 2.6924 2.3678 0.0011 -0.3005 0.0483 83 ALA A CB 268 N N . THR A 71 ? 1.5298 2.6085 2.3236 0.0444 -0.2411 0.1215 84 THR A N 269 C CA . THR A 71 ? 1.5296 2.6148 2.3685 0.0548 -0.2057 0.1400 84 THR A CA 270 C C . THR A 71 ? 1.5309 2.5715 2.3454 0.0212 -0.2018 0.1171 84 THR A C 271 O O . THR A 71 ? 1.5504 2.5891 2.3940 0.0253 -0.1725 0.1277 84 THR A O 272 C CB . THR A 71 ? 1.5671 2.7662 2.4862 0.0607 -0.2052 0.1821 84 THR A CB 273 O OG1 . THR A 71 ? 1.4991 2.7474 2.4338 0.0829 -0.2200 0.2017 84 THR A OG1 274 C CG2 . THR A 71 ? 1.6227 2.8287 2.5923 0.0875 -0.1623 0.2064 84 THR A CG2 275 N N . ARG A 72 ? 1.5003 2.5054 2.2614 -0.0114 -0.2308 0.0863 85 ARG A N 276 C CA . ARG A 72 ? 1.4772 2.4399 2.2132 -0.0467 -0.2313 0.0652 85 ARG A CA 277 C C . ARG A 72 ? 1.5498 2.4157 2.2047 -0.0571 -0.2442 0.0254 85 ARG A C 278 O O . ARG A 72 ? 1.6714 2.5347 2.2923 -0.0640 -0.2738 0.0096 85 ARG A O 279 C CB . ARG A 72 ? 1.3836 2.4222 2.1513 -0.0869 -0.2571 0.0732 85 ARG A CB 280 N N . LEU A 73 ? 1.4366 2.2255 2.0605 -0.0568 -0.2212 0.0099 86 LEU A N 281 C CA . LEU A 73 ? 1.2677 1.9674 1.8177 -0.0706 -0.2322 -0.0258 86 LEU A CA 282 C C . LEU A 73 ? 1.3159 1.9892 1.8572 -0.1070 -0.2310 -0.0358 86 LEU A C 283 O O . LEU A 73 ? 1.3638 2.0522 1.9410 -0.1087 -0.2058 -0.0194 86 LEU A O 284 C CB . LEU A 73 ? 1.1915 1.8181 1.7045 -0.0384 -0.2077 -0.0363 86 LEU A CB 285 C CG . LEU A 73 ? 1.2795 1.9171 1.7823 -0.0111 -0.2188 -0.0349 86 LEU A CG 286 C CD1 . LEU A 73 ? 1.2630 1.8294 1.7260 0.0182 -0.1976 -0.0468 86 LEU A CD1 287 C CD2 . LEU A 73 ? 1.3947 2.0339 1.8600 -0.0326 -0.2581 -0.0549 86 LEU A CD2 288 N N . THR A 74 ? 1.2804 1.9157 1.7751 -0.1363 -0.2580 -0.0619 87 THR A N 289 C CA . THR A 74 ? 1.3098 1.9066 1.7887 -0.1715 -0.2574 -0.0733 87 THR A CA 290 C C . THR A 74 ? 1.2684 1.7708 1.6968 -0.1579 -0.2350 -0.0898 87 THR A C 291 O O . THR A 74 ? 1.3816 1.8246 1.7544 -0.1441 -0.2428 -0.1119 87 THR A O 292 C CB . THR A 74 ? 1.4861 2.0715 1.9322 -0.2079 -0.2943 -0.0964 87 THR A CB 293 O OG1 . THR A 74 ? 1.5877 2.2682 2.0824 -0.2253 -0.3156 -0.0806 87 THR A OG1 294 C CG2 . THR A 74 ? 1.5291 2.0591 1.9522 -0.2431 -0.2922 -0.1094 87 THR A CG2 295 N N . PHE A 75 ? 1.1628 1.6558 1.6106 -0.1611 -0.2068 -0.0783 88 PHE A N 296 C CA . PHE A 75 ? 1.1214 1.5368 1.5277 -0.1441 -0.1814 -0.0895 88 PHE A CA 297 C C . PHE A 75 ? 1.1921 1.5243 1.5341 -0.1660 -0.1934 -0.1162 88 PHE A C 298 O O . PHE A 75 ? 1.0447 1.3744 1.3869 -0.2025 -0.2080 -0.1199 88 PHE A O 299 C CB . PHE A 75 ? 1.1095 1.5459 1.5568 -0.1389 -0.1462 -0.0683 88 PHE A CB 300 C CG . PHE A 75 ? 1.1774 1.5552 1.5933 -0.1115 -0.1163 -0.0754 88 PHE A CG 301 C CD1 . PHE A 75 ? 1.2371 1.6198 1.6583 -0.0739 -0.1014 -0.0717 88 PHE A CD1 302 C CD2 . PHE A 75 ? 1.2138 1.5316 1.5939 -0.1243 -0.1033 -0.0855 88 PHE A CD2 303 C CE1 . PHE A 75 ? 1.2521 1.5814 1.6426 -0.0514 -0.0741 -0.0801 88 PHE A CE1 304 C CE2 . PHE A 75 ? 1.1949 1.4634 1.5445 -0.1003 -0.0764 -0.0924 88 PHE A CE2 305 C CZ . PHE A 75 ? 1.2115 1.4864 1.5660 -0.0648 -0.0621 -0.0908 88 PHE A CZ 306 N N . PRO A 76 ? 1.2662 1.5290 1.5525 -0.1434 -0.1868 -0.1342 89 PRO A N 307 C CA . PRO A 76 ? 1.2215 1.4066 1.4443 -0.1588 -0.2010 -0.1594 89 PRO A CA 308 C C . PRO A 76 ? 1.3071 1.4571 1.5254 -0.1821 -0.1854 -0.1560 89 PRO A C 309 O O . PRO A 76 ? 1.3460 1.5196 1.5983 -0.1778 -0.1582 -0.1375 89 PRO A O 310 C CB . PRO A 76 ? 1.0896 1.2235 1.2645 -0.1242 -0.1913 -0.1726 89 PRO A CB 311 C CG . PRO A 76 ? 1.0826 1.2473 1.2941 -0.0991 -0.1599 -0.1537 89 PRO A CG 312 C CD . PRO A 76 ? 1.1283 1.3789 1.4081 -0.1042 -0.1633 -0.1314 89 PRO A CD 313 N N . ALA A 77 ? 1.3580 1.4514 1.5344 -0.2064 -0.2016 -0.1733 90 ALA A N 314 C CA . ALA A 77 ? 1.3469 1.3976 1.5123 -0.2255 -0.1854 -0.1694 90 ALA A CA 315 C C . ALA A 77 ? 1.5305 1.5265 1.6543 -0.1950 -0.1615 -0.1746 90 ALA A C 316 O O . ALA A 77 ? 1.5279 1.4944 1.6123 -0.1696 -0.1681 -0.1900 90 ALA A O 317 C CB . ALA A 77 ? 1.1747 1.1764 1.3077 -0.2596 -0.2087 -0.1854 90 ALA A CB 318 N N . VAL A 78 ? 1.5849 1.5736 1.7189 -0.1976 -0.1337 -0.1609 91 VAL A N 319 C CA . VAL A 78 ? 1.4598 1.4044 1.5571 -0.1714 -0.1093 -0.1644 91 VAL A CA 320 C C . VAL A 78 ? 1.5829 1.4731 1.6510 -0.1901 -0.0990 -0.1630 91 VAL A C 321 O O . VAL A 78 ? 1.7280 1.6420 1.8294 -0.2088 -0.0835 -0.1454 91 VAL A O 322 C CB . VAL A 78 ? 1.2273 1.2217 1.3668 -0.1510 -0.0788 -0.1472 91 VAL A CB 323 C CG1 . VAL A 78 ? 1.1933 1.1442 1.2948 -0.1298 -0.0532 -0.1517 91 VAL A CG1 324 C CG2 . VAL A 78 ? 1.1691 1.2147 1.3387 -0.1291 -0.0858 -0.1454 91 VAL A CG2 325 N N . THR A 79 ? 1.5982 1.4180 1.6054 -0.1840 -0.1067 -0.1796 92 THR A N 326 C CA . THR A 79 ? 1.6102 1.3744 1.5865 -0.1990 -0.0967 -0.1764 92 THR A CA 327 C C . THR A 79 ? 1.5908 1.3292 1.5344 -0.1714 -0.0712 -0.1759 92 THR A C 328 O O . THR A 79 ? 1.6179 1.3479 1.5350 -0.1425 -0.0721 -0.1881 92 THR A O 329 C CB . THR A 79 ? 1.6257 1.3218 1.5526 -0.2113 -0.1215 -0.1939 92 THR A CB 330 O OG1 . THR A 79 ? 1.6409 1.3514 1.5942 -0.2462 -0.1436 -0.1946 92 THR A OG1 331 C CG2 . THR A 79 ? 1.5186 1.1516 1.4056 -0.2149 -0.1068 -0.1894 92 THR A CG2 332 N N . PHE A 80 ? 1.5836 1.3133 1.5293 -0.1813 -0.0482 -0.1611 93 PHE A N 333 C CA . PHE A 80 ? 1.5978 1.3056 1.5104 -0.1580 -0.0235 -0.1605 93 PHE A CA 334 C C . PHE A 80 ? 1.6365 1.2986 1.5214 -0.1738 -0.0131 -0.1507 93 PHE A C 335 O O . PHE A 80 ? 1.6935 1.3714 1.6091 -0.2001 -0.0057 -0.1340 93 PHE A O 336 C CB . PHE A 80 ? 1.5696 1.3354 1.5228 -0.1444 0.0037 -0.1497 93 PHE A CB 337 C CG . PHE A 80 ? 1.6795 1.4719 1.6665 -0.1644 0.0257 -0.1285 93 PHE A CG 338 C CD1 . PHE A 80 ? 1.6915 1.4579 1.6504 -0.1634 0.0484 -0.1212 93 PHE A CD1 339 C CD2 . PHE A 80 ? 1.7362 1.5847 1.7835 -0.1838 0.0240 -0.1145 93 PHE A CD2 340 C CE1 . PHE A 80 ? 1.7258 1.5201 1.7155 -0.1815 0.0692 -0.1007 93 PHE A CE1 341 C CE2 . PHE A 80 ? 1.7889 1.6664 1.8684 -0.2020 0.0448 -0.0939 93 PHE A CE2 342 C CZ . PHE A 80 ? 1.7688 1.6186 1.8193 -0.2009 0.0677 -0.0871 93 PHE A CZ 343 N N . CYS A 81 ? 1.6713 1.2793 1.4988 -0.1577 -0.0123 -0.1592 94 CYS A N 344 C CA . CYS A 81 ? 1.6763 1.2404 1.4747 -0.1688 -0.0011 -0.1475 94 CYS A CA 345 C C . CYS A 81 ? 1.7453 1.3196 1.5262 -0.1485 0.0283 -0.1411 94 CYS A C 346 O O . CYS A 81 ? 1.7867 1.3763 1.5558 -0.1220 0.0338 -0.1527 94 CYS A O 347 C CB . CYS A 81 ? 1.5447 1.0378 1.2884 -0.1652 -0.0210 -0.1593 94 CYS A CB 348 S SG . CYS A 81 ? 1.8668 1.3239 1.6198 -0.2011 -0.0486 -0.1616 94 CYS A SG 349 N N . ASN A 82 ? 1.7338 1.3017 1.5136 -0.1622 0.0475 -0.1224 95 ASN A N 350 C CA . ASN A 82 ? 1.6548 1.2228 1.4051 -0.1438 0.0730 -0.1178 95 ASN A CA 351 C C . ASN A 82 ? 1.7652 1.2713 1.4533 -0.1308 0.0621 -0.1246 95 ASN A C 352 O O . ASN A 82 ? 1.8399 1.3005 1.5140 -0.1426 0.0406 -0.1266 95 ASN A O 353 C CB . ASN A 82 ? 1.5800 1.1683 1.3512 -0.1627 0.0976 -0.0939 95 ASN A CB 354 C CG . ASN A 82 ? 1.5796 1.1850 1.3286 -0.1438 0.1265 -0.0908 95 ASN A CG 355 O OD1 . ASN A 82 ? 1.5710 1.1553 1.2754 -0.1203 0.1259 -0.1037 95 ASN A OD1 356 N ND2 . ASN A 82 ? 1.5789 1.2259 1.3581 -0.1541 0.1522 -0.0743 95 ASN A ND2 357 N N . LEU A 83 ? 1.7222 1.2271 1.3731 -0.1063 0.0764 -0.1290 96 LEU A N 358 C CA . LEU A 83 ? 1.6910 1.1448 1.2821 -0.0899 0.0677 -0.1338 96 LEU A CA 359 C C . LEU A 83 ? 1.7618 1.1795 1.3267 -0.1003 0.0779 -0.1125 96 LEU A C 360 O O . LEU A 83 ? 1.7727 1.1372 1.2978 -0.0946 0.0653 -0.1118 96 LEU A O 361 C CB . LEU A 83 ? 1.5343 1.0063 1.0968 -0.0609 0.0767 -0.1473 96 LEU A CB 362 C CG . LEU A 83 ? 1.4893 0.9875 1.0743 -0.0503 0.0636 -0.1668 96 LEU A CG 363 C CD1 . LEU A 83 ? 1.5434 1.0486 1.0945 -0.0230 0.0664 -0.1820 96 LEU A CD1 364 C CD2 . LEU A 83 ? 1.5842 1.0518 1.1711 -0.0573 0.0332 -0.1750 96 LEU A CD2 365 N N . ASN A 84 ? 1.7528 1.2016 1.3409 -0.1141 0.1019 -0.0941 97 ASN A N 366 C CA . ASN A 84 ? 1.8149 1.2383 1.3893 -0.1289 0.1131 -0.0694 97 ASN A CA 367 C C . ASN A 84 ? 1.9024 1.2960 1.5032 -0.1592 0.0972 -0.0601 97 ASN A C 368 O O . ASN A 84 ? 1.8796 1.3076 1.5308 -0.1790 0.0953 -0.0596 97 ASN A O 369 C CB . ASN A 84 ? 1.8711 1.3472 1.4664 -0.1343 0.1444 -0.0542 97 ASN A CB 370 C CG . ASN A 84 ? 1.9808 1.4388 1.5553 -0.1447 0.1599 -0.0270 97 ASN A CG 371 O OD1 . ASN A 84 ? 2.0334 1.4656 1.5591 -0.1280 0.1630 -0.0230 97 ASN A OD1 372 N ND2 . ASN A 84 ? 1.9948 1.4718 1.6075 -0.1720 0.1708 -0.0062 97 ASN A ND2 373 N N . GLU A 85 ? 2.0288 1.3587 1.5961 -0.1631 0.0862 -0.0525 98 GLU A N 374 C CA . GLU A 85 ? 2.0790 1.3707 1.6659 -0.1933 0.0696 -0.0468 98 GLU A CA 375 C C . GLU A 85 ? 2.0069 1.3181 1.6311 -0.2265 0.0856 -0.0195 98 GLU A C 376 O O . GLU A 85 ? 1.9704 1.2864 1.6337 -0.2556 0.0743 -0.0186 98 GLU A O 377 C CB . GLU A 85 ? 2.1854 1.3961 1.7248 -0.1868 0.0535 -0.0484 98 GLU A CB 378 C CG . GLU A 85 ? 2.1983 1.3870 1.7045 -0.1579 0.0334 -0.0760 98 GLU A CG 379 C CD . GLU A 85 ? 2.3192 1.4287 1.7957 -0.1607 0.0118 -0.0828 98 GLU A CD 380 O OE1 . GLU A 85 ? 2.3939 1.4603 1.8732 -0.1851 0.0131 -0.0655 98 GLU A OE1 381 O OE2 . GLU A 85 ? 2.3180 1.4074 1.7681 -0.1389 -0.0061 -0.1056 98 GLU A OE2 382 N N . PHE A 86 ? 1.9645 1.2900 1.5765 -0.2231 0.1111 0.0029 99 PHE A N 383 C CA . PHE A 86 ? 1.8965 1.2471 1.5431 -0.2532 0.1289 0.0313 99 PHE A CA 384 C C . PHE A 86 ? 1.8902 1.2991 1.5394 -0.2429 0.1607 0.0457 99 PHE A C 385 O O . PHE A 86 ? 1.9439 1.3543 1.5535 -0.2151 0.1706 0.0413 99 PHE A O 386 C CB . PHE A 86 ? 1.9592 1.2441 1.5843 -0.2716 0.1261 0.0542 99 PHE A CB 387 C CG . PHE A 86 ? 2.0764 1.2831 1.6665 -0.2650 0.1002 0.0390 99 PHE A CG 388 C CD1 . PHE A 86 ? 2.0680 1.2452 1.6068 -0.2289 0.0957 0.0263 99 PHE A CD1 389 C CD2 . PHE A 86 ? 2.1844 1.3465 1.7917 -0.2958 0.0811 0.0381 99 PHE A CD2 390 C CE1 . PHE A 86 ? 2.1416 1.2470 1.6475 -0.2208 0.0731 0.0126 99 PHE A CE1 391 C CE2 . PHE A 86 ? 2.2098 1.2964 1.7827 -0.2892 0.0585 0.0223 99 PHE A CE2 392 C CZ . PHE A 86 ? 2.1825 1.2407 1.7047 -0.2502 0.0550 0.0097 99 PHE A CZ 393 N N . ARG A 87 ? 1.9303 1.3885 1.6253 -0.2664 0.1770 0.0635 100 ARG A N 394 C CA . ARG A 87 ? 2.0419 1.5549 1.7394 -0.2595 0.2091 0.0788 100 ARG A CA 395 C C . ARG A 87 ? 2.0413 1.5260 1.7078 -0.2664 0.2227 0.1092 100 ARG A C 396 O O . ARG A 87 ? 2.1558 1.6045 1.8320 -0.2938 0.2159 0.1299 100 ARG A O 397 C CB . ARG A 87 ? 2.1112 1.6924 1.8710 -0.2804 0.2230 0.0879 100 ARG A CB 398 C CG . ARG A 87 ? 2.1002 1.7141 1.8982 -0.2761 0.2101 0.0635 100 ARG A CG 399 C CD . ARG A 87 ? 2.1030 1.7669 1.9660 -0.3061 0.2135 0.0777 100 ARG A CD 400 N NE . ARG A 87 ? 2.1454 1.7700 2.0241 -0.3381 0.1879 0.0834 100 ARG A NE 401 C CZ . ARG A 87 ? 2.1391 1.8003 2.0723 -0.3697 0.1846 0.0958 100 ARG A CZ 402 N NH1 . ARG A 87 ? 2.1789 1.9182 2.1577 -0.3707 0.2060 0.1052 100 ARG A NH1 403 N NH2 . ARG A 87 ? 2.0882 1.7093 2.0305 -0.4004 0.1605 0.0983 100 ARG A NH2 404 N N . PHE A 88 ? 1.9311 1.4332 1.5607 -0.2429 0.2421 0.1126 101 PHE A N 405 C CA . PHE A 88 ? 2.0826 1.5700 1.6840 -0.2475 0.2580 0.1445 101 PHE A CA 406 C C . PHE A 88 ? 2.0706 1.6055 1.7139 -0.2759 0.2796 0.1727 101 PHE A C 407 O O . PHE A 88 ? 1.9748 1.4898 1.6120 -0.2935 0.2871 0.2048 101 PHE A O 408 C CB . PHE A 88 ? 2.1810 1.6878 1.7343 -0.2164 0.2740 0.1404 101 PHE A CB 409 C CG . PHE A 88 ? 2.2876 1.8693 1.8549 -0.2157 0.3050 0.1473 101 PHE A CG 410 C CD1 . PHE A 88 ? 2.3063 1.9049 1.8453 -0.2135 0.3267 0.1728 101 PHE A CD1 411 C CD2 . PHE A 88 ? 2.4104 2.0472 2.0198 -0.2166 0.3132 0.1285 101 PHE A CD2 412 C CE1 . PHE A 88 ? 2.4456 2.1154 1.9961 -0.2129 0.3562 0.1770 101 PHE A CE1 413 C CE2 . PHE A 88 ? 2.4313 2.1357 2.0536 -0.2145 0.3435 0.1329 101 PHE A CE2 414 C CZ . PHE A 88 ? 2.4611 2.1824 2.0531 -0.2131 0.3651 0.1558 101 PHE A CZ 415 N N . SER A 89 ? 2.1357 1.7351 1.8224 -0.2791 0.2901 0.1614 102 SER A N 416 C CA . SER A 89 ? 2.1134 1.7674 1.8470 -0.3047 0.3100 0.1851 102 SER A CA 417 C C . SER A 89 ? 2.0529 1.6691 1.8140 -0.3414 0.2934 0.2052 102 SER A C 418 O O . SER A 89 ? 2.0769 1.7097 1.8574 -0.3667 0.3072 0.2368 102 SER A O 419 C CB . SER A 89 ? 2.1312 1.8526 1.9103 -0.2990 0.3184 0.1651 102 SER A CB 420 O OG . SER A 89 ? 2.0288 1.7363 1.7964 -0.2743 0.3018 0.1296 102 SER A OG 421 N N . ARG A 90 ? 2.0992 1.6651 1.8612 -0.3451 0.2635 0.1857 103 ARG A N 422 C CA . ARG A 90 ? 2.2054 1.7339 1.9951 -0.3817 0.2442 0.1970 103 ARG A CA 423 C C . ARG A 90 ? 2.3856 1.8226 2.1358 -0.3898 0.2286 0.2083 103 ARG A C 424 O O . ARG A 90 ? 2.5389 1.9354 2.3078 -0.4206 0.2108 0.2132 103 ARG A O 425 C CB . ARG A 90 ? 2.1351 1.6775 1.9627 -0.3887 0.2220 0.1703 103 ARG A CB 426 C CG . ARG A 90 ? 2.1080 1.7309 2.0011 -0.4110 0.2340 0.1805 103 ARG A CG 427 C CD . ARG A 90 ? 2.1038 1.7997 2.0043 -0.3924 0.2683 0.1892 103 ARG A CD 428 N NE . ARG A 90 ? 2.2222 1.9937 2.1848 -0.4143 0.2825 0.2048 103 ARG A NE 429 C CZ . ARG A 90 ? 2.3061 2.1371 2.3101 -0.4055 0.2845 0.1890 103 ARG A CZ 430 N NH1 . ARG A 90 ? 2.3259 2.1482 2.3160 -0.3763 0.2729 0.1569 103 ARG A NH1 431 N NH2 . ARG A 90 ? 2.3234 2.2248 2.3841 -0.4253 0.2986 0.2071 103 ARG A NH2 432 N N . VAL A 91 ? 2.3682 1.7720 2.0641 -0.3626 0.2352 0.2122 104 VAL A N 433 C CA . VAL A 91 ? 2.3267 1.6431 1.9846 -0.3666 0.2235 0.2264 104 VAL A CA 434 C C . VAL A 91 ? 2.4140 1.7266 2.0637 -0.3811 0.2452 0.2699 104 VAL A C 435 O O . VAL A 91 ? 2.3615 1.7340 2.0087 -0.3711 0.2710 0.2852 104 VAL A O 436 C CB . VAL A 91 ? 2.1464 1.4172 1.7479 -0.3270 0.2119 0.2046 104 VAL A CB 437 C CG1 . VAL A 91 ? 2.1941 1.4456 1.7495 -0.3094 0.2284 0.2312 104 VAL A CG1 438 C CG2 . VAL A 91 ? 2.0507 1.2424 1.6416 -0.3327 0.1818 0.1868 104 VAL A CG2 439 N N . THR A 92 ? 2.5569 1.7984 2.2021 -0.4053 0.2349 0.2898 105 THR A N 440 C CA . THR A 92 ? 2.6919 1.9260 2.3359 -0.4250 0.2539 0.3347 105 THR A CA 441 C C . THR A 92 ? 2.7678 1.9236 2.3566 -0.4065 0.2527 0.3526 105 THR A C 442 O O . THR A 92 ? 2.8053 1.9106 2.3567 -0.3784 0.2363 0.3289 105 THR A O 443 C CB . THR A 92 ? 2.6864 1.9051 2.3771 -0.4754 0.2475 0.3526 105 THR A CB 444 O OG1 . THR A 92 ? 2.7447 1.8602 2.4136 -0.4873 0.2272 0.3539 105 THR A OG1 445 C CG2 . THR A 92 ? 2.5934 1.8653 2.3352 -0.4921 0.2363 0.3259 105 THR A CG2 446 N N . LYS A 93 ? 2.6909 1.8392 2.2758 -0.4213 0.2707 0.3962 106 LYS A N 447 C CA . LYS A 93 ? 2.5857 1.6603 2.1220 -0.4047 0.2712 0.4192 106 LYS A CA 448 C C . LYS A 93 ? 2.6672 1.6407 2.1948 -0.4134 0.2437 0.4021 106 LYS A C 449 O O . LYS A 93 ? 2.6339 1.5474 2.1169 -0.3825 0.2327 0.3904 106 LYS A O 450 C CB . LYS A 93 ? 2.4408 1.5205 1.9833 -0.4270 0.2934 0.4720 106 LYS A CB 451 N N . ASN A 94 ? 2.7602 1.7193 2.3310 -0.4558 0.2325 0.3990 107 ASN A N 452 C CA . ASN A 94 ? 2.8684 1.7329 2.4350 -0.4719 0.2069 0.3819 107 ASN A CA 453 C C . ASN A 94 ? 2.8735 1.7051 2.4084 -0.4368 0.1851 0.3371 107 ASN A C 454 O O . ASN A 94 ? 2.8202 1.5695 2.3123 -0.4159 0.1762 0.3350 107 ASN A O 455 C CB . ASN A 94 ? 2.8691 1.7477 2.4920 -0.5238 0.1974 0.3786 107 ASN A CB 456 C CG . ASN A 94 ? 2.8914 1.6725 2.5097 -0.5456 0.1712 0.3600 107 ASN A CG 457 O OD1 . ASN A 94 ? 2.9993 1.7912 2.6456 -0.5651 0.1517 0.3289 107 ASN A OD1 458 N ND2 . ASN A 94 ? 2.7712 1.4565 2.3528 -0.5412 0.1708 0.3783 107 ASN A ND2 459 N N . ASP A 95 ? 2.9153 1.8119 2.4720 -0.4296 0.1774 0.3030 108 ASP A N 460 C CA . ASP A 95 ? 2.9381 1.8150 2.4691 -0.3976 0.1570 0.2606 108 ASP A CA 461 C C . ASP A 95 ? 2.9217 1.7880 2.3974 -0.3477 0.1640 0.2608 108 ASP A C 462 O O . ASP A 95 ? 2.8936 1.7064 2.3350 -0.3222 0.1470 0.2370 108 ASP A O 463 C CB . ASP A 95 ? 2.8819 1.8397 2.4488 -0.3978 0.1509 0.2293 108 ASP A CB 464 C CG . ASP A 95 ? 2.9006 1.9259 2.5263 -0.4370 0.1616 0.2448 108 ASP A CG 465 O OD1 . ASP A 95 ? 2.9064 1.9363 2.5692 -0.4659 0.1446 0.2281 108 ASP A OD1 466 O OD2 . ASP A 95 ? 2.9059 1.9851 2.5409 -0.4380 0.1870 0.2734 108 ASP A OD2 467 N N . LEU A 96 ? 2.8967 1.8184 2.3638 -0.3340 0.1889 0.2869 109 LEU A N 468 C CA . LEU A 96 ? 2.8423 1.7658 2.2583 -0.2889 0.1967 0.2895 109 LEU A CA 469 C C . LEU A 96 ? 2.9813 1.8109 2.3541 -0.2746 0.1921 0.3088 109 LEU A C 470 O O . LEU A 96 ? 2.9802 1.7935 2.3087 -0.2351 0.1894 0.3017 109 LEU A O 471 C CB . LEU A 96 ? 2.6898 1.6969 2.1063 -0.2813 0.2249 0.3136 109 LEU A CB 472 N N . TYR A 97 ? 3.0715 1.8408 2.4574 -0.3063 0.1925 0.3348 110 TYR A N 473 C CA . TYR A 97 ? 3.1732 1.8395 2.5221 -0.2951 0.1862 0.3496 110 TYR A CA 474 C C . TYR A 97 ? 3.1793 1.7827 2.5070 -0.2773 0.1599 0.3081 110 TYR A C 475 O O . TYR A 97 ? 3.1653 1.7503 2.4500 -0.2348 0.1562 0.2987 110 TYR A O 476 C CB . TYR A 97 ? 3.2463 1.8563 2.6187 -0.3384 0.1903 0.3815 110 TYR A CB 477 C CG . TYR A 97 ? 3.3359 1.8472 2.6703 -0.3257 0.1932 0.4108 110 TYR A CG 478 C CD1 . TYR A 97 ? 3.3882 1.9124 2.7019 -0.3104 0.2160 0.4569 110 TYR A CD1 479 C CD2 . TYR A 97 ? 3.3853 1.7911 2.7047 -0.3289 0.1740 0.3931 110 TYR A CD2 480 C CE1 . TYR A 97 ? 3.4976 1.9323 2.7784 -0.2970 0.2198 0.4871 110 TYR A CE1 481 C CE2 . TYR A 97 ? 3.5051 1.8165 2.7903 -0.3153 0.1784 0.4204 110 TYR A CE2 482 C CZ . TYR A 97 ? 3.5645 1.8905 2.8314 -0.2987 0.2015 0.4688 110 TYR A CZ 483 O OH . TYR A 97 ? 3.6643 1.8973 2.8986 -0.2829 0.2069 0.4994 110 TYR A OH 484 N N . HIS A 98 ? 3.1657 1.7424 2.5243 -0.3103 0.1417 0.2833 111 HIS A N 485 C CA . HIS A 98 ? 3.1743 1.6866 2.5144 -0.2992 0.1164 0.2445 111 HIS A CA 486 C C . HIS A 98 ? 3.1934 1.7615 2.5186 -0.2620 0.1080 0.2096 111 HIS A C 487 O O . HIS A 98 ? 3.2641 1.7951 2.5469 -0.2237 0.1000 0.1956 111 HIS A O 488 C CB . HIS A 98 ? 3.1297 1.6211 2.5102 -0.3460 0.0988 0.2236 111 HIS A CB 489 C CG . HIS A 98 ? 3.1176 1.6136 2.5375 -0.3949 0.1104 0.2564 111 HIS A CG 490 N ND1 . HIS A 98 ? 3.1285 1.5386 2.5551 -0.4311 0.1024 0.2642 111 HIS A ND1 491 C CD2 . HIS A 98 ? 3.0377 1.6157 2.4931 -0.4144 0.1295 0.2827 111 HIS A CD2 492 C CE1 . HIS A 98 ? 3.1096 1.5502 2.5751 -0.4720 0.1157 0.2958 111 HIS A CE1 493 N NE2 . HIS A 98 ? 3.0423 1.5860 2.5258 -0.4616 0.1325 0.3078 111 HIS A NE2 494 N N . ALA A 99 ? 3.1305 1.7891 2.4921 -0.2735 0.1107 0.1969 112 ALA A N 495 C CA . ALA A 99 ? 3.0422 1.7562 2.3981 -0.2452 0.1020 0.1623 112 ALA A CA 496 C C . ALA A 99 ? 3.0035 1.7536 2.3213 -0.2021 0.1164 0.1717 112 ALA A C 497 O O . ALA A 99 ? 3.0393 1.7973 2.3313 -0.1692 0.1062 0.1459 112 ALA A O 498 C CB . ALA A 99 ? 2.9735 1.7719 2.3813 -0.2699 0.1036 0.1501 112 ALA A CB 499 N N . GLY A 100 ? 2.9710 1.7440 2.2844 -0.2032 0.1396 0.2096 113 GLY A N 500 C CA . GLY A 100 ? 2.9382 1.7694 2.2240 -0.1701 0.1558 0.2190 113 GLY A CA 501 C C . GLY A 100 ? 2.9627 1.7714 2.1995 -0.1253 0.1461 0.2029 113 GLY A C 502 O O . GLY A 100 ? 2.9011 1.7712 2.1251 -0.1011 0.1494 0.1878 113 GLY A O 503 N N . GLU A 101 ? 3.0485 1.7696 2.2573 -0.1141 0.1347 0.2063 114 GLU A N 504 C CA . GLU A 101 ? 3.0555 1.7551 2.2166 -0.0694 0.1268 0.1952 114 GLU A CA 505 C C . GLU A 101 ? 3.0372 1.7440 2.1994 -0.0578 0.1046 0.1483 114 GLU A C 506 O O . GLU A 101 ? 3.0505 1.7669 2.1788 -0.0211 0.0988 0.1345 114 GLU A O 507 C CB . GLU A 101 ? 3.1432 1.7459 2.2726 -0.0571 0.1248 0.2168 114 GLU A CB 508 C CG . GLU A 101 ? 3.1623 1.7601 2.2408 -0.0080 0.1269 0.2243 114 GLU A CG 509 C CD . GLU A 101 ? 3.2450 1.7399 2.2930 0.0108 0.1166 0.2264 114 GLU A CD 510 O OE1 . GLU A 101 ? 3.1918 1.6513 2.2332 0.0195 0.0965 0.1900 114 GLU A OE1 511 O OE2 . GLU A 101 ? 3.3894 1.8388 2.4193 0.0179 0.1293 0.2649 114 GLU A OE2 512 N N . LEU A 102 ? 2.9972 1.7038 2.1991 -0.0897 0.0924 0.1258 115 LEU A N 513 C CA . LEU A 102 ? 2.8966 1.6145 2.1050 -0.0832 0.0710 0.0830 115 LEU A CA 514 C C . LEU A 102 ? 2.7740 1.5871 1.9964 -0.0735 0.0762 0.0670 115 LEU A C 515 O O . LEU A 102 ? 2.6923 1.5228 1.9045 -0.0529 0.0624 0.0371 115 LEU A O 516 C CB . LEU A 102 ? 2.8928 1.5788 2.1392 -0.1226 0.0559 0.0671 115 LEU A CB 517 C CG . LEU A 102 ? 2.8166 1.5097 2.0737 -0.1220 0.0320 0.0247 115 LEU A CG 518 C CD1 . LEU A 102 ? 2.8312 1.5014 2.0419 -0.0783 0.0208 0.0053 115 LEU A CD1 519 C CD2 . LEU A 102 ? 2.8251 1.4605 2.1048 -0.1587 0.0162 0.0141 115 LEU A CD2 520 N N . LEU A 103 ? 2.7302 1.6028 1.9751 -0.0884 0.0970 0.0875 116 LEU A N 521 C CA . LEU A 103 ? 2.6085 1.5692 1.8675 -0.0814 0.1066 0.0752 116 LEU A CA 522 C C . LEU A 103 ? 2.6124 1.6031 1.8294 -0.0485 0.1205 0.0876 116 LEU A C 523 O O . LEU A 103 ? 2.5350 1.5959 1.7557 -0.0414 0.1321 0.0807 116 LEU A O 524 C CB . LEU A 103 ? 2.5422 1.5526 1.8475 -0.1149 0.1233 0.0901 116 LEU A CB 525 C CG . LEU A 103 ? 2.4214 1.4347 1.7783 -0.1500 0.1125 0.0769 116 LEU A CG 526 C CD1 . LEU A 103 ? 2.4419 1.3763 1.7928 -0.1579 0.0879 0.0633 116 LEU A CD1 527 C CD2 . LEU A 103 ? 2.3420 1.3791 1.7346 -0.1837 0.1311 0.1065 116 LEU A CD2 528 N N . ALA A 104 ? 2.7177 1.6544 1.8950 -0.0292 0.1199 0.1066 117 ALA A N 529 C CA . ALA A 104 ? 2.7394 1.7006 1.8738 0.0026 0.1317 0.1227 117 ALA A CA 530 C C . ALA A 104 ? 2.7015 1.7204 1.8431 -0.0086 0.1575 0.1506 117 ALA A C 531 O O . ALA A 104 ? 2.7312 1.8015 1.8464 0.0120 0.1688 0.1554 117 ALA A O 532 C CB . ALA A 104 ? 2.6998 1.7023 1.8151 0.0303 0.1224 0.0923 117 ALA A CB 533 N N . LEU A 105 ? 2.6302 1.6446 1.8071 -0.0422 0.1670 0.1686 118 LEU A N 534 C CA . LEU A 105 ? 2.6037 1.6720 1.7873 -0.0536 0.1926 0.1974 118 LEU A CA 535 C C . LEU A 105 ? 2.7597 1.7847 1.9180 -0.0498 0.2027 0.2408 118 LEU A C 536 O O . LEU A 105 ? 2.7392 1.8022 1.8998 -0.0594 0.2241 0.2711 118 LEU A O 537 C CB . LEU A 105 ? 2.4487 1.5497 1.6867 -0.0913 0.2002 0.1957 118 LEU A CB 538 N N . LEU A 106 ? 2.8629 1.8090 1.9962 -0.0342 0.1879 0.2438 119 LEU A N 539 C CA . LEU A 106 ? 2.8859 1.7738 1.9987 -0.0312 0.1956 0.2852 119 LEU A CA 540 C C . LEU A 106 ? 2.8671 1.6967 1.9329 0.0074 0.1853 0.2890 119 LEU A C 541 O O . LEU A 106 ? 2.7521 1.5693 1.8036 0.0285 0.1676 0.2559 119 LEU A O 542 C CB . LEU A 106 ? 2.8772 1.7037 2.0247 -0.0691 0.1924 0.2966 119 LEU A CB 543 C CG . LEU A 106 ? 2.7540 1.6294 1.9450 -0.1081 0.2087 0.3134 119 LEU A CG 544 C CD1 . LEU A 106 ? 2.8121 1.6174 2.0319 -0.1446 0.2035 0.3274 119 LEU A CD1 545 C CD2 . LEU A 106 ? 2.6553 1.5859 1.8303 -0.1007 0.2343 0.3516 119 LEU A CD2 546 N N . ASN A 107 ? 2.8970 1.6920 1.9401 0.0169 0.1972 0.3316 120 ASN A N 547 C CA . ASN A 107 ? 2.7858 1.5291 1.7842 0.0563 0.1917 0.3434 120 ASN A CA 548 C C . ASN A 107 ? 2.9924 1.6235 1.9925 0.0491 0.1816 0.3493 120 ASN A C 549 O O . ASN A 107 ? 3.0501 1.6464 2.0853 0.0106 0.1799 0.3484 120 ASN A O 550 C CB . ASN A 107 ? 2.5017 1.2807 1.4714 0.0755 0.2122 0.3896 120 ASN A CB 551 N N . ASN A 108 ? 3.1036 1.6782 2.0652 0.0861 0.1757 0.3560 121 ASN A N 552 C CA . ASN A 108 ? 3.2091 1.6715 2.1652 0.0836 0.1711 0.3693 121 ASN A CA 553 C C . ASN A 108 ? 3.3266 1.7766 2.2995 0.0563 0.1905 0.4166 121 ASN A C 554 O O . ASN A 108 ? 3.4374 1.8093 2.4282 0.0287 0.1889 0.4253 121 ASN A O 555 C CB . ASN A 108 ? 3.2817 1.6983 2.1904 0.1340 0.1689 0.3808 121 ASN A CB 556 C CG . ASN A 108 ? 3.3249 1.7585 2.2146 0.1636 0.1505 0.3371 121 ASN A CG 557 O OD1 . ASN A 108 ? 3.3098 1.8115 2.2166 0.1526 0.1428 0.3037 121 ASN A OD1 558 N ND2 . ASN A 108 ? 3.3890 1.7607 2.2435 0.2025 0.1442 0.3381 121 ASN A ND2 559 N N . ARG A 109 ? 3.3685 1.8998 2.3352 0.0626 0.2089 0.4465 122 ARG A N 560 C CA . ARG A 109 ? 3.4499 1.9845 2.4281 0.0415 0.2298 0.4967 122 ARG A CA 561 C C . ARG A 109 ? 3.3650 1.9542 2.3901 -0.0068 0.2374 0.4935 122 ARG A C 562 O O . ARG A 109 ? 3.3970 2.0076 2.4335 -0.0255 0.2562 0.5345 122 ARG A O 563 C CB . ARG A 109 ? 3.4414 2.0341 2.3852 0.0748 0.2469 0.5358 122 ARG A CB 564 N N . TYR A 110 ? 3.1840 1.7987 2.2360 -0.0252 0.2234 0.4469 123 TYR A N 565 C CA . TYR A 110 ? 2.9957 1.6670 2.0941 -0.0678 0.2299 0.4407 123 TYR A CA 566 C C . TYR A 110 ? 2.9609 1.7425 2.0573 -0.0624 0.2490 0.4529 123 TYR A C 567 O O . TYR A 110 ? 2.9145 1.7410 2.0400 -0.0924 0.2646 0.4723 123 TYR A O 568 C CB . TYR A 110 ? 2.9850 1.6025 2.1109 -0.1067 0.2378 0.4742 123 TYR A CB 569 C CG . TYR A 110 ? 3.0265 1.5463 2.1669 -0.1271 0.2184 0.4530 123 TYR A CG 570 C CD1 . TYR A 110 ? 2.9508 1.4595 2.1369 -0.1763 0.2161 0.4502 123 TYR A CD1 571 C CD2 . TYR A 110 ? 3.1310 1.5733 2.2389 -0.0973 0.2023 0.4338 123 TYR A CD2 572 C CE1 . TYR A 110 ? 2.9894 1.4116 2.1874 -0.1976 0.1974 0.4282 123 TYR A CE1 573 C CE2 . TYR A 110 ? 3.1537 1.5067 2.2722 -0.1166 0.1845 0.4108 123 TYR A CE2 574 C CZ . TYR A 110 ? 3.0864 1.4295 2.2495 -0.1679 0.1817 0.4075 123 TYR A CZ 575 O OH . TYR A 110 ? 3.1298 1.3868 2.3021 -0.1898 0.1634 0.3829 123 TYR A OH 576 N N . GLU A 111 ? 3.0056 1.8325 2.0678 -0.0252 0.2476 0.4395 124 GLU A N 577 C CA . GLU A 111 ? 3.0791 2.0072 2.1305 -0.0165 0.2656 0.4497 124 GLU A CA 578 C C . GLU A 111 ? 3.1135 2.1014 2.1572 0.0007 0.2563 0.4039 124 GLU A C 579 O O . GLU A 111 ? 3.1369 2.0875 2.1780 0.0119 0.2359 0.3692 124 GLU A O 580 C CB . GLU A 111 ? 3.1396 2.0709 2.1493 0.0123 0.2786 0.4942 124 GLU A CB 581 N N . ILE A 112 ? 3.1038 2.1843 2.1432 0.0021 0.2719 0.4040 125 ILE A N 582 C CA . ILE A 112 ? 2.9925 2.1352 2.0276 0.0137 0.2664 0.3617 125 ILE A CA 583 C C . ILE A 112 ? 3.0371 2.2043 2.0228 0.0536 0.2626 0.3588 125 ILE A C 584 O O . ILE A 112 ? 3.0216 2.2332 1.9793 0.0662 0.2778 0.3879 125 ILE A O 585 C CB . ILE A 112 ? 2.8840 2.1146 1.9409 -0.0073 0.2862 0.3583 125 ILE A CB 586 C CG1 . ILE A 112 ? 2.7593 1.9873 1.8428 -0.0374 0.3036 0.3968 125 ILE A CG1 587 C CG2 . ILE A 112 ? 2.8788 2.1332 1.9677 -0.0193 0.2770 0.3111 125 ILE A CG2 588 C CD1 . ILE A 112 ? 2.6854 1.8643 1.8166 -0.0700 0.2948 0.3887 125 ILE A CD1 589 N N . PRO A 113 ? 3.1562 2.3023 2.1316 0.0726 0.2423 0.3234 126 PRO A N 590 C CA . PRO A 113 ? 3.2712 2.4315 2.2006 0.1111 0.2359 0.3221 126 PRO A CA 591 C C . PRO A 113 ? 3.3252 2.5827 2.2327 0.1189 0.2503 0.3220 126 PRO A C 592 O O . PRO A 113 ? 3.2945 2.6070 2.2240 0.0955 0.2639 0.3135 126 PRO A O 593 C CB . PRO A 113 ? 3.2357 2.3690 2.1701 0.1206 0.2126 0.2770 126 PRO A CB 594 C CG . PRO A 113 ? 3.1560 2.2999 2.1377 0.0870 0.2114 0.2498 126 PRO A CG 595 C CD . PRO A 113 ? 3.1640 2.2853 2.1719 0.0581 0.2251 0.2817 126 PRO A CD 596 N N . ASP A 114 ? 3.4405 2.7197 2.3047 0.1512 0.2483 0.3326 127 ASP A N 597 C CA . ASP A 114 ? 3.4694 2.8410 2.3095 0.1589 0.2576 0.3237 127 ASP A CA 598 C C . ASP A 114 ? 3.3740 2.7750 2.2288 0.1524 0.2474 0.2716 127 ASP A C 599 O O . ASP A 114 ? 3.3425 2.8174 2.1871 0.1495 0.2560 0.2549 127 ASP A O 600 C CB . ASP A 114 ? 3.4940 2.8847 2.2851 0.1950 0.2554 0.3467 127 ASP A CB 601 C CG . ASP A 114 ? 3.4531 2.7960 2.2292 0.2235 0.2327 0.3281 127 ASP A CG 602 O OD1 . ASP A 114 ? 3.4923 2.7543 2.2878 0.2213 0.2205 0.3211 127 ASP A OD1 603 O OD2 . ASP A 114 ? 3.3616 2.7613 2.1283 0.2432 0.2231 0.3147 127 ASP A OD2 604 N N . THR A 115 ? 3.2789 2.6202 2.1580 0.1488 0.2296 0.2465 128 THR A N 605 C CA . THR A 115 ? 3.1679 2.5277 2.0664 0.1419 0.2189 0.2000 128 THR A CA 606 C C . THR A 115 ? 3.1535 2.5314 2.0969 0.1078 0.2299 0.1873 128 THR A C 607 O O . THR A 115 ? 3.1254 2.5149 2.0932 0.0988 0.2227 0.1513 128 THR A O 608 C CB . THR A 115 ? 3.1420 2.4336 2.0473 0.1532 0.1944 0.1791 128 THR A CB 609 O OG1 . THR A 115 ? 3.1421 2.3698 2.0813 0.1319 0.1915 0.1860 128 THR A OG1 610 C CG2 . THR A 115 ? 3.1962 2.4597 2.0597 0.1886 0.1846 0.1956 128 THR A CG2 611 N N . GLN A 116 ? 3.1572 2.5390 2.1129 0.0898 0.2476 0.2186 129 GLN A N 612 C CA . GLN A 116 ? 3.0894 2.4880 2.0901 0.0578 0.2590 0.2112 129 GLN A CA 613 C C . GLN A 116 ? 3.0525 2.5333 2.0533 0.0519 0.2748 0.1902 129 GLN A C 614 O O . GLN A 116 ? 3.0320 2.5656 2.0045 0.0572 0.2911 0.2062 129 GLN A O 615 C CB . GLN A 116 ? 3.0682 2.4478 2.0819 0.0397 0.2736 0.2529 129 GLN A CB 616 N N . THR A 117 ? 2.9887 2.4791 2.0219 0.0406 0.2700 0.1542 130 THR A N 617 C CA . THR A 117 ? 2.7976 2.3560 1.8354 0.0350 0.2841 0.1282 130 THR A CA 618 C C . THR A 117 ? 2.7301 2.2974 1.8208 0.0089 0.2937 0.1180 130 THR A C 619 O O . THR A 117 ? 2.7770 2.3136 1.9001 0.0032 0.2788 0.0972 130 THR A O 620 C CB . THR A 117 ? 2.5758 2.1398 1.6009 0.0516 0.2679 0.0907 130 THR A CB 621 O OG1 . THR A 117 ? 2.3308 1.8335 1.3749 0.0549 0.2442 0.0795 130 THR A OG1 622 C CG2 . THR A 117 ? 2.6609 2.2458 1.6322 0.0759 0.2646 0.0975 130 THR A CG2 623 N N . ALA A 118 ? 2.5658 2.1799 1.6652 -0.0060 0.3187 0.1324 131 ALA A N 624 C CA . ALA A 118 ? 2.4079 2.0300 1.5589 -0.0305 0.3292 0.1312 131 ALA A CA 625 C C . ALA A 118 ? 2.3930 2.0855 1.5497 -0.0410 0.3587 0.1310 131 ALA A C 626 O O . ALA A 118 ? 2.3256 2.0574 1.4450 -0.0340 0.3733 0.1430 131 ALA A O 627 C CB . ALA A 118 ? 2.3555 1.9274 1.5283 -0.0461 0.3240 0.1644 131 ALA A CB 628 N N . ASP A 119 ? 2.4968 2.2060 1.7012 -0.0577 0.3674 0.1184 132 ASP A N 629 C CA . ASP A 119 ? 2.5732 2.3480 1.7882 -0.0641 0.3944 0.1053 132 ASP A CA 630 C C . ASP A 119 ? 2.7148 2.5322 1.9171 -0.0736 0.4202 0.1372 132 ASP A C 631 O O . ASP A 119 ? 2.7211 2.5154 1.9188 -0.0805 0.4184 0.1748 132 ASP A O 632 C CB . ASP A 119 ? 2.5522 2.3317 1.8255 -0.0776 0.3966 0.0878 132 ASP A CB 633 N N . GLU A 120 ? 2.7972 2.6767 1.9927 -0.0738 0.4447 0.1215 133 GLU A N 634 C CA . GLU A 120 ? 2.8384 2.7687 2.0190 -0.0818 0.4712 0.1478 133 GLU A CA 635 C C . GLU A 120 ? 2.7963 2.7144 2.0157 -0.1024 0.4764 0.1850 133 GLU A C 636 O O . GLU A 120 ? 2.7784 2.6906 1.9798 -0.1065 0.4791 0.2239 133 GLU A O 637 C CB . GLU A 120 ? 2.8794 2.8743 2.0616 -0.0825 0.4981 0.1192 133 GLU A CB 638 C CG . GLU A 120 ? 2.8957 2.9044 2.1372 -0.0955 0.5106 0.1083 133 GLU A CG 639 C CD . GLU A 120 ? 2.8898 2.9472 2.1315 -0.0899 0.5331 0.0704 133 GLU A CD 640 O OE1 . GLU A 120 ? 2.8791 2.9338 2.0900 -0.0761 0.5268 0.0385 133 GLU A OE1 641 O OE2 . GLU A 120 ? 2.8950 2.9926 2.1678 -0.0993 0.5575 0.0723 133 GLU A OE2 642 N N . LYS A 121 ? 2.7493 2.6638 2.0228 -0.1154 0.4770 0.1742 134 LYS A N 643 C CA . LYS A 121 ? 2.6836 2.5994 1.9997 -0.1386 0.4851 0.2063 134 LYS A CA 644 C C . LYS A 121 ? 2.6187 2.4632 1.9480 -0.1480 0.4596 0.2300 134 LYS A C 645 O O . LYS A 121 ? 2.6479 2.4859 1.9977 -0.1677 0.4649 0.2660 134 LYS A O 646 C CB . LYS A 121 ? 2.6273 2.5757 1.9974 -0.1486 0.4972 0.1863 134 LYS A CB 647 N N . GLN A 122 ? 2.5258 2.3170 1.8428 -0.1346 0.4326 0.2095 135 GLN A N 648 C CA . GLN A 122 ? 2.4874 2.2060 1.8173 -0.1426 0.4071 0.2241 135 GLN A CA 649 C C . GLN A 122 ? 2.7534 2.4419 2.0542 -0.1447 0.4073 0.2670 135 GLN A C 650 O O . GLN A 122 ? 2.8576 2.4978 2.1790 -0.1617 0.3974 0.2911 135 GLN A O 651 C CB . GLN A 122 ? 2.2832 1.9570 1.5996 -0.1244 0.3802 0.1921 135 GLN A CB 652 N N . LEU A 123 ? 2.8269 2.5442 2.0796 -0.1279 0.4188 0.2770 136 LEU A N 653 C CA . LEU A 123 ? 2.8366 2.5310 2.0597 -0.1266 0.4209 0.3207 136 LEU A CA 654 C C . LEU A 123 ? 2.8002 2.4964 2.0589 -0.1552 0.4340 0.3584 136 LEU A C 655 O O . LEU A 123 ? 2.8198 2.4532 2.0973 -0.1687 0.4198 0.3773 136 LEU A O 656 C CB . LEU A 123 ? 2.8876 2.6379 2.0615 -0.1092 0.4377 0.3278 136 LEU A CB 657 N N . GLU A 124 ? 2.8051 2.5739 2.0743 -0.1656 0.4612 0.3672 137 GLU A N 658 C CA . GLU A 124 ? 2.9023 2.6851 2.2025 -0.1927 0.4770 0.4070 137 GLU A CA 659 C C . GLU A 124 ? 2.9014 2.6415 2.2572 -0.2183 0.4634 0.4068 137 GLU A C 660 O O . GLU A 124 ? 2.9403 2.6568 2.3166 -0.2414 0.4655 0.4444 137 GLU A O 661 C CB . GLU A 124 ? 2.8787 2.7538 2.1852 -0.1982 0.5088 0.4078 137 GLU A CB 662 N N . ILE A 125 ? 2.7911 2.5248 2.1713 -0.2153 0.4501 0.3652 138 ILE A N 663 C CA . ILE A 125 ? 2.6542 2.3533 2.0864 -0.2386 0.4349 0.3602 138 ILE A CA 664 C C . ILE A 125 ? 2.6077 2.2149 2.0304 -0.2372 0.4041 0.3584 138 ILE A C 665 O O . ILE A 125 ? 2.6022 2.1699 2.0611 -0.2617 0.3914 0.3659 138 ILE A O 666 C CB . ILE A 125 ? 2.5043 2.2438 1.9720 -0.2368 0.4357 0.3191 138 ILE A CB 667 C CG1 . ILE A 125 ? 2.3612 2.0663 1.8061 -0.2117 0.4133 0.2785 138 ILE A CG1 668 C CG2 . ILE A 125 ? 1.8827 1.7118 1.3547 -0.2335 0.4684 0.3162 138 ILE A CG2 669 C CD1 . ILE A 125 ? 2.2273 1.9701 1.7020 -0.2054 0.4144 0.2383 138 ILE A CD1 670 N N . LEU A 126 ? 2.5751 2.1502 1.9486 -0.2089 0.3926 0.3480 139 LEU A N 671 C CA . LEU A 126 ? 2.6249 2.1129 1.9834 -0.2025 0.3649 0.3449 139 LEU A CA 672 C C . LEU A 126 ? 2.8010 2.2372 2.1451 -0.2122 0.3659 0.3907 139 LEU A C 673 O O . LEU A 126 ? 2.8958 2.2602 2.2531 -0.2262 0.3484 0.3973 139 LEU A O 674 C CB . LEU A 126 ? 2.5983 2.0746 1.9105 -0.1670 0.3526 0.3177 139 LEU A CB 675 C CG . LEU A 126 ? 2.5863 2.0396 1.9071 -0.1560 0.3293 0.2725 139 LEU A CG 676 C CD1 . LEU A 126 ? 2.5250 1.8995 1.8652 -0.1696 0.3044 0.2711 139 LEU A CD1 677 C CD2 . LEU A 126 ? 2.5750 2.0907 1.9318 -0.1622 0.3380 0.2424 139 LEU A CD2 678 N N . GLN A 127 ? 2.8229 2.2961 2.1395 -0.2052 0.3871 0.4225 140 GLN A N 679 C CA . GLN A 127 ? 2.8100 2.2386 2.1077 -0.2095 0.3906 0.4702 140 GLN A CA 680 C C . GLN A 127 ? 2.8716 2.2978 2.2104 -0.2475 0.4018 0.5059 140 GLN A C 681 O O . GLN A 127 ? 2.9260 2.2847 2.2635 -0.2591 0.3955 0.5372 140 GLN A O 682 C CB . GLN A 127 ? 2.7571 2.2309 2.0069 -0.1853 0.4080 0.4919 140 GLN A CB 683 C CG . GLN A 127 ? 2.6648 2.1425 1.8714 -0.1492 0.3969 0.4607 140 GLN A CG 684 C CD . GLN A 127 ? 2.6394 2.1974 1.8100 -0.1321 0.4177 0.4677 140 GLN A CD 685 O OE1 . GLN A 127 ? 2.7355 2.3558 1.9180 -0.1474 0.4414 0.4864 140 GLN A OE1 686 N NE2 . GLN A 127 ? 2.4747 2.0352 1.6006 -0.1011 0.4092 0.4527 140 GLN A NE2 687 N N . ASP A 128 ? 2.8928 2.3927 2.2675 -0.2664 0.4193 0.5026 141 ASP A N 688 C CA . ASP A 128 ? 2.9724 2.4772 2.3924 -0.3049 0.4286 0.5334 141 ASP A CA 689 C C . ASP A 128 ? 2.9673 2.3927 2.4168 -0.3256 0.4026 0.5216 141 ASP A C 690 O O . ASP A 128 ? 2.9796 2.3663 2.4530 -0.3563 0.4014 0.5524 141 ASP A O 691 C CB . ASP A 128 ? 2.9477 2.5464 2.4052 -0.3180 0.4490 0.5223 141 ASP A CB 692 C CG . ASP A 128 ? 2.9904 2.6117 2.4908 -0.3560 0.4638 0.5613 141 ASP A CG 693 O OD1 . ASP A 128 ? 3.0434 2.5988 2.5518 -0.3775 0.4541 0.5912 141 ASP A OD1 694 O OD2 . ASP A 128 ? 2.9737 2.6784 2.4999 -0.3647 0.4858 0.5619 141 ASP A OD2 695 N N . LYS A 129 ? 2.8820 2.2853 2.3287 -0.3096 0.3818 0.4762 142 LYS A N 696 C CA . LYS A 129 ? 2.8315 2.1581 2.2968 -0.3237 0.3544 0.4586 142 LYS A CA 697 C C . LYS A 129 ? 2.8848 2.1227 2.3041 -0.3014 0.3372 0.4611 142 LYS A C 698 O O . LYS A 129 ? 2.9486 2.1101 2.3750 -0.3125 0.3156 0.4517 142 LYS A O 699 C CB . LYS A 129 ? 2.6986 2.0526 2.1884 -0.3189 0.3411 0.4095 142 LYS A CB 700 N N . ALA A 130 ? 2.8959 2.1462 2.2674 -0.2695 0.3470 0.4730 143 ALA A N 701 C CA . ALA A 130 ? 2.9835 2.1579 2.3093 -0.2427 0.3330 0.4776 143 ALA A CA 702 C C . ALA A 130 ? 3.0261 2.1537 2.3327 -0.2469 0.3429 0.5304 143 ALA A C 703 O O . ALA A 130 ? 2.9898 2.0536 2.2583 -0.2226 0.3338 0.5392 143 ALA A O 704 C CB . ALA A 130 ? 3.0094 2.2204 2.2922 -0.2013 0.3327 0.4541 143 ALA A CB 705 N N . ASN A 131 ? 3.0705 2.2298 2.4040 -0.2766 0.3620 0.5668 144 ASN A N 706 C CA . ASN A 131 ? 3.1167 2.2417 2.4324 -0.2799 0.3744 0.6210 144 ASN A CA 707 C C . ASN A 131 ? 3.0861 2.1008 2.4122 -0.3003 0.3586 0.6340 144 ASN A C 708 O O . ASN A 131 ? 3.0450 2.0423 2.4148 -0.3394 0.3534 0.6318 144 ASN A O 709 C CB . ASN A 131 ? 3.1922 2.3934 2.5329 -0.3053 0.4012 0.6570 144 ASN A CB 710 C CG . ASN A 131 ? 3.2448 2.4580 2.6448 -0.3497 0.4001 0.6514 144 ASN A CG 711 O OD1 . ASN A 131 ? 3.2214 2.4007 2.6447 -0.3604 0.3796 0.6150 144 ASN A OD1 712 N ND2 . ASN A 131 ? 3.2873 2.5553 2.7124 -0.3756 0.4225 0.6883 144 ASN A ND2 713 N N . PHE A 132 ? 3.1130 2.0538 2.3982 -0.2735 0.3513 0.6475 145 PHE A N 714 C CA . PHE A 132 ? 3.1639 1.9895 2.4511 -0.2879 0.3376 0.6593 145 PHE A CA 715 C C . PHE A 132 ? 3.3082 2.0961 2.5899 -0.3001 0.3546 0.7220 145 PHE A C 716 O O . PHE A 132 ? 3.4076 2.0951 2.6912 -0.3148 0.3465 0.7376 145 PHE A O 717 C CB . PHE A 132 ? 3.0178 1.7730 2.2675 -0.2512 0.3164 0.6284 145 PHE A CB 718 C CG . PHE A 132 ? 2.8579 1.6287 2.1213 -0.2492 0.2960 0.5684 145 PHE A CG 719 C CD1 . PHE A 132 ? 2.7345 1.5094 2.0459 -0.2894 0.2870 0.5464 145 PHE A CD1 720 C CD2 . PHE A 132 ? 2.7488 1.5342 1.9779 -0.2075 0.2860 0.5360 145 PHE A CD2 721 C CE1 . PHE A 132 ? 2.5107 1.3027 1.8352 -0.2865 0.2685 0.4941 145 PHE A CE1 722 C CE2 . PHE A 132 ? 2.4958 1.2958 1.7380 -0.2058 0.2677 0.4837 145 PHE A CE2 723 C CZ . PHE A 132 ? 2.4012 1.2041 1.6910 -0.2447 0.2591 0.4634 145 PHE A CZ 724 N N . ARG A 133 ? 3.2281 2.0958 2.5022 -0.2944 0.3785 0.7577 146 ARG A N 725 C CA . ARG A 133 ? 3.2752 2.1235 2.5524 -0.3120 0.3966 0.8194 146 ARG A CA 726 C C . ARG A 133 ? 3.4228 2.2477 2.7534 -0.3672 0.3948 0.8251 146 ARG A C 727 O O . ARG A 133 ? 3.3564 2.2435 2.7237 -0.3899 0.3930 0.7959 146 ARG A O 728 C CB . ARG A 133 ? 3.1715 2.1278 2.4362 -0.3008 0.4228 0.8517 146 ARG A CB 729 C CG . ARG A 133 ? 3.0429 2.0421 2.2566 -0.2498 0.4249 0.8427 146 ARG A CG 730 C CD . ARG A 133 ? 3.0213 2.1241 2.2213 -0.2432 0.4518 0.8795 146 ARG A CD 731 N NE . ARG A 133 ? 3.1684 2.2414 2.3371 -0.2260 0.4632 0.9379 146 ARG A NE 732 C CZ . ARG A 133 ? 3.2575 2.3963 2.4221 -0.2314 0.4866 0.9867 146 ARG A CZ 733 N NH1 . ARG A 133 ? 3.2853 2.5217 2.4730 -0.2536 0.5037 0.9848 146 ARG A NH1 734 N NH2 . ARG A 133 ? 3.2566 2.3781 2.4034 -0.2159 0.4815 1.0233 146 ARG A NH2 735 N N . ASN A 134 ? 3.6283 2.3629 2.9637 -0.3884 0.3950 0.8625 147 ASN A N 736 C CA . ASN A 134 ? 3.7069 2.4064 3.0910 -0.4438 0.3911 0.8694 147 ASN A CA 737 C C . ASN A 134 ? 3.7281 2.4229 3.1413 -0.4620 0.3681 0.8097 147 ASN A C 738 O O . ASN A 134 ? 3.6956 2.4478 3.1551 -0.4993 0.3700 0.8016 147 ASN A O 739 C CB . ASN A 134 ? 3.6548 2.4429 3.0721 -0.4758 0.4153 0.9103 147 ASN A CB 740 N N . PHE A 135 ? 3.7717 2.4011 3.1578 -0.4346 0.3467 0.7696 148 PHE A N 741 C CA . PHE A 135 ? 3.7632 2.3897 3.1711 -0.4458 0.3237 0.7118 148 PHE A CA 742 C C . PHE A 135 ? 3.8849 2.4174 3.3191 -0.4893 0.3069 0.7051 148 PHE A C 743 O O . PHE A 135 ? 4.0142 2.4381 3.4247 -0.4859 0.3008 0.7182 148 PHE A O 744 C CB . PHE A 135 ? 3.7432 2.3510 3.1097 -0.3965 0.3085 0.6708 148 PHE A CB 745 N N . LYS A 136 ? 3.8671 2.4424 3.3500 -0.5299 0.2996 0.6841 149 LYS A N 746 C CA . LYS A 136 ? 3.9439 2.4422 3.4534 -0.5735 0.2800 0.6676 149 LYS A CA 747 C C . LYS A 136 ? 3.9444 2.4601 3.4672 -0.5724 0.2557 0.6061 149 LYS A C 748 O O . LYS A 136 ? 3.9459 2.5587 3.5039 -0.5837 0.2573 0.5894 149 LYS A O 749 C CB . LYS A 136 ? 3.9368 2.4666 3.4968 -0.6307 0.2913 0.7025 149 LYS A CB 750 N N . PRO A 137 ? 3.9028 2.3258 3.3969 -0.5567 0.2340 0.5730 150 PRO A N 751 C CA . PRO A 137 ? 3.7489 2.1797 3.2501 -0.5530 0.2093 0.5149 150 PRO A CA 752 C C . PRO A 137 ? 3.6435 2.0667 3.1928 -0.6100 0.1931 0.4971 150 PRO A C 753 O O . PRO A 137 ? 3.7394 2.1152 3.3083 -0.6534 0.1962 0.5251 150 PRO A O 754 C CB . PRO A 137 ? 3.7988 2.1241 3.2486 -0.5172 0.1947 0.4938 150 PRO A CB 755 C CG . PRO A 137 ? 3.8948 2.1859 3.3072 -0.4879 0.2148 0.5396 150 PRO A CG 756 C CD . PRO A 137 ? 3.9677 2.2828 3.4131 -0.5291 0.2344 0.5897 150 PRO A CD 757 N N . LYS A 138 ? 3.4354 1.9082 3.0038 -0.6099 0.1760 0.4518 151 LYS A N 758 C CA . LYS A 138 ? 3.2943 1.7671 2.9060 -0.6597 0.1570 0.4287 151 LYS A CA 759 C C . LYS A 138 ? 3.2154 1.6842 2.8169 -0.6402 0.1313 0.3718 151 LYS A C 760 O O . LYS A 138 ? 3.2087 1.7223 2.7890 -0.5942 0.1323 0.3523 151 LYS A O 761 C CB . LYS A 138 ? 3.1761 1.7617 2.8448 -0.6925 0.1696 0.4467 151 LYS A CB 762 N N . PRO A 139 ? 3.1299 1.5479 2.7466 -0.6768 0.1080 0.3451 152 PRO A N 763 C CA . PRO A 139 ? 3.1340 1.5315 2.7346 -0.6590 0.0822 0.2921 152 PRO A CA 764 C C . PRO A 139 ? 3.1205 1.6309 2.7464 -0.6420 0.0775 0.2651 152 PRO A C 765 O O . PRO A 139 ? 3.1045 1.7086 2.7754 -0.6619 0.0888 0.2811 152 PRO A O 766 C CB . PRO A 139 ? 3.0889 1.4256 2.7111 -0.7146 0.0616 0.2768 152 PRO A CB 767 C CG . PRO A 139 ? 3.0260 1.4109 2.6978 -0.7641 0.0752 0.3150 152 PRO A CG 768 C CD . PRO A 139 ? 3.0641 1.4556 2.7188 -0.7406 0.1045 0.3625 152 PRO A CD 769 N N . PHE A 140 ? 3.1608 1.6613 2.7577 -0.6046 0.0618 0.2254 153 PHE A N 770 C CA . PHE A 140 ? 3.1706 1.7647 2.7922 -0.5924 0.0531 0.1955 153 PHE A CA 771 C C . PHE A 140 ? 3.1987 1.7541 2.7936 -0.5711 0.0268 0.1476 153 PHE A C 772 O O . PHE A 140 ? 3.2635 1.7289 2.8102 -0.5481 0.0201 0.1374 153 PHE A O 773 C CB . PHE A 140 ? 3.1213 1.8016 2.7404 -0.5532 0.0754 0.2097 153 PHE A CB 774 C CG . PHE A 140 ? 3.1074 1.7814 2.6814 -0.4974 0.0707 0.1839 153 PHE A CG 775 C CD1 . PHE A 140 ? 3.0464 1.8077 2.6328 -0.4724 0.0718 0.1643 153 PHE A CD1 776 C CD2 . PHE A 140 ? 3.1629 1.7454 2.6831 -0.4695 0.0663 0.1811 153 PHE A CD2 777 C CE1 . PHE A 140 ? 2.9955 1.7534 2.5415 -0.4238 0.0675 0.1418 153 PHE A CE1 778 C CE2 . PHE A 140 ? 3.1081 1.6913 2.5885 -0.4191 0.0621 0.1590 153 PHE A CE2 779 C CZ . PHE A 140 ? 3.0124 1.6840 2.5058 -0.3977 0.0623 0.1394 153 PHE A CZ 780 N N . ASN A 141 ? 3.1286 1.7537 2.7553 -0.5783 0.0125 0.1195 154 ASN A N 781 C CA . ASN A 141 ? 3.1222 1.7259 2.7271 -0.5579 -0.0121 0.0747 154 ASN A CA 782 C C . ASN A 141 ? 2.9475 1.6460 2.5633 -0.5236 -0.0111 0.0575 154 ASN A C 783 O O . ASN A 141 ? 2.8626 1.6527 2.5229 -0.5349 -0.0005 0.0695 154 ASN A O 784 C CB . ASN A 141 ? 3.2474 1.8208 2.8743 -0.6051 -0.0374 0.0510 154 ASN A CB 785 C CG . ASN A 141 ? 3.2596 1.9352 2.9393 -0.6251 -0.0482 0.0357 154 ASN A CG 786 O OD1 . ASN A 141 ? 3.2659 2.0336 2.9818 -0.6229 -0.0320 0.0549 154 ASN A OD1 787 N ND2 . ASN A 141 ? 3.2539 1.9138 2.9378 -0.6443 -0.0753 0.0011 154 ASN A ND2 788 N N . MET A 142 ? 2.8742 1.5494 2.4493 -0.4810 -0.0213 0.0301 155 MET A N 789 C CA . MET A 142 ? 2.7070 1.4615 2.2849 -0.4441 -0.0186 0.0155 155 MET A CA 790 C C . MET A 142 ? 2.7051 1.5384 2.3325 -0.4642 -0.0319 -0.0038 155 MET A C 791 O O . MET A 142 ? 2.6796 1.5914 2.3234 -0.4418 -0.0245 -0.0078 155 MET A O 792 C CB . MET A 142 ? 2.6010 1.3108 2.1245 -0.3971 -0.0283 -0.0090 155 MET A CB 793 N N . LEU A 143 ? 2.7043 1.5180 2.3555 -0.5064 -0.0511 -0.0154 156 LEU A N 794 C CA . LEU A 143 ? 2.6317 1.5269 2.3337 -0.5279 -0.0634 -0.0292 156 LEU A CA 795 C C . LEU A 143 ? 2.5483 1.5293 2.3013 -0.5446 -0.0412 0.0021 156 LEU A C 796 O O . LEU A 143 ? 2.4707 1.5381 2.2528 -0.5290 -0.0356 -0.0012 156 LEU A O 797 C CB . LEU A 143 ? 2.7099 1.5688 2.4259 -0.5732 -0.0891 -0.0475 156 LEU A CB 798 C CG . LEU A 143 ? 2.6406 1.5749 2.4007 -0.5931 -0.1090 -0.0685 156 LEU A CG 799 C CD1 . LEU A 143 ? 2.6381 1.6625 2.4633 -0.6265 -0.0976 -0.0424 156 LEU A CD1 800 C CD2 . LEU A 143 ? 2.5286 1.5076 2.2772 -0.5480 -0.1159 -0.0929 156 LEU A CD2 801 N N . GLU A 144 ? 2.4856 1.4423 2.2491 -0.5756 -0.0276 0.0331 157 GLU A N 802 C CA . GLU A 144 ? 2.3296 1.3671 2.1400 -0.5920 -0.0048 0.0650 157 GLU A CA 803 C C . GLU A 144 ? 2.3286 1.4041 2.1216 -0.5478 0.0217 0.0793 157 GLU A C 804 O O . GLU A 144 ? 2.2264 1.3912 2.0557 -0.5424 0.0375 0.0891 157 GLU A O 805 C CB . GLU A 144 ? 2.1913 1.1952 2.0189 -0.6397 0.0019 0.0954 157 GLU A CB 806 C CG . GLU A 144 ? 2.1835 1.2576 2.0454 -0.6484 0.0307 0.1334 157 GLU A CG 807 C CD . GLU A 144 ? 2.4063 1.4573 2.2272 -0.6115 0.0547 0.1534 157 GLU A CD 808 O OE1 . GLU A 144 ? 2.5058 1.4639 2.2793 -0.6023 0.0510 0.1541 157 GLU A OE1 809 O OE2 . GLU A 144 ? 2.5062 1.6318 2.3407 -0.5905 0.0774 0.1674 157 GLU A OE2 810 N N . PHE A 145 ? 2.3489 1.3577 2.0860 -0.5160 0.0267 0.0797 158 PHE A N 811 C CA . PHE A 145 ? 2.2751 1.3155 1.9878 -0.4726 0.0486 0.0883 158 PHE A CA 812 C C . PHE A 145 ? 2.2871 1.4040 2.0159 -0.4452 0.0468 0.0646 158 PHE A C 813 O O . PHE A 145 ? 2.2607 1.4545 2.0161 -0.4380 0.0672 0.0768 158 PHE A O 814 C CB . PHE A 145 ? 2.2978 1.2556 1.9464 -0.4401 0.0480 0.0863 158 PHE A CB 815 C CG . PHE A 145 ? 2.3689 1.3589 1.9909 -0.4006 0.0712 0.0993 158 PHE A CG 816 C CD1 . PHE A 145 ? 2.4385 1.4839 2.0817 -0.4085 0.0978 0.1305 158 PHE A CD1 817 C CD2 . PHE A 145 ? 2.3131 1.2820 1.8886 -0.3565 0.0664 0.0801 158 PHE A CD2 818 C CE1 . PHE A 145 ? 2.3801 1.4578 1.9968 -0.3739 0.1189 0.1402 158 PHE A CE1 819 C CE2 . PHE A 145 ? 2.2043 1.2066 1.7548 -0.3229 0.0869 0.0911 158 PHE A CE2 820 C CZ . PHE A 145 ? 2.2551 1.3109 1.8253 -0.3320 0.1128 0.1201 158 PHE A CZ 821 N N . TYR A 146 ? 2.3020 1.3965 2.0134 -0.4292 0.0233 0.0311 159 TYR A N 822 C CA . TYR A 146 ? 2.2105 1.3729 1.9401 -0.4068 0.0185 0.0084 159 TYR A CA 823 C C . TYR A 146 ? 2.0962 1.3451 1.8910 -0.4331 0.0252 0.0184 159 TYR A C 824 O O . TYR A 146 ? 1.9689 1.2883 1.7838 -0.4134 0.0412 0.0202 159 TYR A O 825 C CB . TYR A 146 ? 2.2576 1.3843 1.9683 -0.3981 -0.0114 -0.0266 159 TYR A CB 826 C CG . TYR A 146 ? 2.2961 1.3728 1.9468 -0.3551 -0.0149 -0.0420 159 TYR A CG 827 C CD1 . TYR A 146 ? 2.2349 1.3338 1.8625 -0.3206 0.0062 -0.0324 159 TYR A CD1 828 C CD2 . TYR A 146 ? 2.3434 1.3539 1.9605 -0.3493 -0.0390 -0.0667 159 TYR A CD2 829 C CE1 . TYR A 146 ? 2.1991 1.2591 1.7736 -0.2824 0.0028 -0.0449 159 TYR A CE1 830 C CE2 . TYR A 146 ? 2.3100 1.2799 1.8736 -0.3085 -0.0414 -0.0793 159 TYR A CE2 831 C CZ . TYR A 146 ? 2.2590 1.2557 1.8025 -0.2756 -0.0207 -0.0672 159 TYR A CZ 832 O OH . TYR A 146 ? 2.2398 1.2027 1.7317 -0.2362 -0.0233 -0.0781 159 TYR A OH 833 N N . ASP A 147 ? 2.1301 1.3729 1.9577 -0.4777 0.0137 0.0254 160 ASP A N 834 C CA . ASP A 147 ? 2.0735 1.3995 1.9660 -0.5068 0.0186 0.0378 160 ASP A CA 835 C C . ASP A 147 ? 1.9974 1.3871 1.9149 -0.5029 0.0516 0.0675 160 ASP A C 836 O O . ASP A 147 ? 1.9029 1.3745 1.8580 -0.4924 0.0622 0.0675 160 ASP A O 837 C CB . ASP A 147 ? 2.1015 1.4010 2.0185 -0.5597 0.0021 0.0444 160 ASP A CB 838 C CG . ASP A 147 ? 2.1097 1.4994 2.0946 -0.5897 -0.0001 0.0517 160 ASP A CG 839 O OD1 . ASP A 147 ? 2.0871 1.5450 2.0959 -0.5679 -0.0009 0.0392 160 ASP A OD1 840 O OD2 . ASP A 147 ? 2.1473 1.5409 2.1627 -0.6351 -0.0008 0.0711 160 ASP A OD2 841 N N . ARG A 148 ? 1.9927 1.3454 1.8902 -0.5114 0.0682 0.0935 161 ARG A N 842 C CA . ARG A 148 ? 2.0001 1.4107 1.9160 -0.5079 0.1003 0.1222 161 ARG A CA 843 C C . ARG A 148 ? 2.1351 1.5644 2.0173 -0.4596 0.1205 0.1170 161 ARG A C 844 O O . ARG A 148 ? 2.1057 1.6107 2.0144 -0.4466 0.1409 0.1216 161 ARG A O 845 C CB . ARG A 148 ? 2.1050 1.4768 2.0174 -0.5401 0.1109 0.1559 161 ARG A CB 846 N N . ALA A 149 ? 2.0864 1.4469 1.9102 -0.4339 0.1151 0.1074 162 ALA A N 847 C CA . ALA A 149 ? 2.0188 1.3905 1.8049 -0.3921 0.1331 0.1044 162 ALA A CA 848 C C . ALA A 149 ? 1.9926 1.3959 1.7762 -0.3596 0.1250 0.0719 162 ALA A C 849 O O . ALA A 149 ? 1.7682 1.2095 1.5392 -0.3298 0.1430 0.0676 162 ALA A O 850 C CB . ALA A 149 ? 1.9734 1.2647 1.7005 -0.3783 0.1310 0.1109 162 ALA A CB 851 N N . GLY A 150 ? 2.1011 1.4876 1.8954 -0.3664 0.0977 0.0490 163 GLY A N 852 C CA . GLY A 150 ? 2.1873 1.6070 1.9860 -0.3399 0.0886 0.0209 163 GLY A CA 853 C C . GLY A 150 ? 2.1802 1.6893 2.0263 -0.3360 0.1083 0.0257 163 GLY A C 854 O O . GLY A 150 ? 2.1940 1.7431 2.0802 -0.3616 0.1220 0.0480 163 GLY A O 855 N N . HIS A 151 ? 2.0830 1.6227 1.9246 -0.3039 0.1105 0.0054 164 HIS A N 856 C CA . HIS A 151 ? 1.9534 1.5719 1.8351 -0.2940 0.1321 0.0080 164 HIS A CA 857 C C . HIS A 151 ? 2.0024 1.6718 1.9479 -0.3198 0.1238 0.0128 164 HIS A C 858 O O . HIS A 151 ? 2.0659 1.7129 2.0205 -0.3384 0.0966 0.0045 164 HIS A O 859 C CB . HIS A 151 ? 1.8583 1.4888 1.7200 -0.2558 0.1333 -0.0164 164 HIS A CB 860 C CG . HIS A 151 ? 1.8436 1.4536 1.6536 -0.2299 0.1508 -0.0177 164 HIS A CG 861 N ND1 . HIS A 151 ? 1.7956 1.4506 1.6102 -0.2184 0.1819 -0.0098 164 HIS A ND1 862 C CD2 . HIS A 151 ? 1.7977 1.3512 1.5502 -0.2127 0.1415 -0.0266 164 HIS A CD2 863 C CE1 . HIS A 151 ? 1.7740 1.4022 1.5356 -0.1976 0.1901 -0.0138 164 HIS A CE1 864 N NE2 . HIS A 151 ? 1.8250 1.3932 1.5494 -0.1931 0.1660 -0.0228 164 HIS A NE2 865 N N . ASP A 152 ? 1.9747 1.7149 1.9638 -0.3207 0.1475 0.0262 165 ASP A N 866 C CA . ASP A 152 ? 1.9539 1.7504 2.0071 -0.3480 0.1433 0.0380 165 ASP A CA 867 C C . ASP A 152 ? 1.9060 1.7688 1.9982 -0.3258 0.1496 0.0277 165 ASP A C 868 O O . ASP A 152 ? 1.9270 1.8264 2.0236 -0.3021 0.1772 0.0292 165 ASP A O 869 C CB . ASP A 152 ? 1.9853 1.8145 2.0651 -0.3729 0.1666 0.0691 165 ASP A CB 870 C CG . ASP A 152 ? 2.0110 1.8864 2.1516 -0.4101 0.1570 0.0845 165 ASP A CG 871 O OD1 . ASP A 152 ? 2.0487 1.9311 2.2095 -0.4164 0.1318 0.0703 165 ASP A OD1 872 O OD2 . ASP A 152 ? 1.9638 1.8727 2.1321 -0.4335 0.1746 0.1115 165 ASP A OD2 873 N N . ILE A 153 ? 1.8398 1.7187 1.9606 -0.3335 0.1248 0.0174 166 ILE A N 874 C CA . ILE A 153 ? 1.7141 1.6514 1.8703 -0.3096 0.1289 0.0084 166 ILE A CA 875 C C . ILE A 153 ? 1.6006 1.6182 1.8143 -0.3126 0.1561 0.0296 166 ILE A C 876 O O . ILE A 153 ? 1.5777 1.6421 1.8172 -0.2864 0.1698 0.0250 166 ILE A O 877 C CB . ILE A 153 ? 1.6505 1.5952 1.8271 -0.3174 0.0957 -0.0047 166 ILE A CB 878 C CG1 . ILE A 153 ? 1.4964 1.4766 1.6868 -0.2815 0.0990 -0.0189 166 ILE A CG1 879 C CG2 . ILE A 153 ? 1.2127 1.2080 1.4468 -0.3551 0.0867 0.0138 166 ILE A CG2 880 C CD1 . ILE A 153 ? 1.4644 1.4596 1.6750 -0.2861 0.0681 -0.0299 166 ILE A CD1 881 N N . ARG A 154 ? 1.5943 1.6277 1.8289 -0.3442 0.1644 0.0535 167 ARG A N 882 C CA . ARG A 154 ? 1.6801 1.7906 1.9659 -0.3464 0.1932 0.0755 167 ARG A CA 883 C C . ARG A 154 ? 1.8004 1.9114 2.0587 -0.3119 0.2263 0.0706 167 ARG A C 884 O O . ARG A 154 ? 1.8493 2.0173 2.1398 -0.2896 0.2495 0.0719 167 ARG A O 885 C CB . ARG A 154 ? 1.7038 1.8250 2.0101 -0.3885 0.1958 0.1029 167 ARG A CB 886 N N . GLU A 155 ? 1.7874 1.8344 1.9854 -0.3073 0.2285 0.0646 168 GLU A N 887 C CA . GLU A 155 ? 1.7066 1.7501 1.8707 -0.2772 0.2574 0.0578 168 GLU A CA 888 C C . GLU A 155 ? 1.6007 1.6357 1.7486 -0.2408 0.2544 0.0300 168 GLU A C 889 O O . GLU A 155 ? 1.6202 1.6948 1.7833 -0.2163 0.2793 0.0249 168 GLU A O 890 C CB . GLU A 155 ? 1.7548 1.7347 1.8575 -0.2820 0.2584 0.0604 168 GLU A CB 891 C CG . GLU A 155 ? 1.8566 1.8315 1.9666 -0.3179 0.2608 0.0888 168 GLU A CG 892 C CD . GLU A 155 ? 2.0101 1.9584 2.0719 -0.3116 0.2817 0.0981 168 GLU A CD 893 O OE1 . GLU A 155 ? 2.0292 1.9142 2.0496 -0.3227 0.2681 0.1027 168 GLU A OE1 894 O OE2 . GLU A 155 ? 2.1270 2.1193 2.1919 -0.2944 0.3127 0.1010 168 GLU A OE2 895 N N . MET A 156 ? 1.4929 1.4756 1.6101 -0.2377 0.2244 0.0120 169 MET A N 896 C CA . MET A 156 ? 1.4825 1.4444 1.5695 -0.2039 0.2216 -0.0139 169 MET A CA 897 C C . MET A 156 ? 1.5450 1.5619 1.6788 -0.1840 0.2298 -0.0200 169 MET A C 898 O O . MET A 156 ? 1.5625 1.5828 1.6824 -0.1543 0.2468 -0.0347 169 MET A O 899 C CB . MET A 156 ? 1.4291 1.3293 1.4774 -0.2051 0.1868 -0.0304 169 MET A CB 900 C CG . MET A 156 ? 1.4078 1.2434 1.3892 -0.2007 0.1853 -0.0355 169 MET A CG 901 S SD . MET A 156 ? 1.5368 1.3005 1.4726 -0.1996 0.1461 -0.0545 169 MET A SD 902 C CE . MET A 156 ? 1.5114 1.2721 1.4838 -0.2407 0.1216 -0.0412 169 MET A CE 903 N N . LEU A 157 ? 1.5401 1.6021 1.7304 -0.2012 0.2194 -0.0071 170 LEU A N 904 C CA . LEU A 157 ? 1.4860 1.5945 1.7204 -0.1827 0.2185 -0.0119 170 LEU A CA 905 C C . LEU A 157 ? 1.3128 1.4852 1.5909 -0.1696 0.2547 0.0009 170 LEU A C 906 O O . LEU A 157 ? 1.2149 1.4369 1.5382 -0.1896 0.2628 0.0234 170 LEU A O 907 C CB . LEU A 157 ? 1.4830 1.6142 1.7572 -0.2079 0.1877 -0.0036 170 LEU A CB 908 C CG . LEU A 157 ? 1.3070 1.4994 1.6387 -0.1974 0.1819 -0.0002 170 LEU A CG 909 C CD1 . LEU A 157 ? 1.2046 1.3772 1.5162 -0.1627 0.1763 -0.0222 170 LEU A CD1 910 C CD2 . LEU A 157 ? 1.1572 1.3683 1.5189 -0.2314 0.1500 0.0092 170 LEU A CD2 911 N N . LEU A 158 ? 1.2639 1.4355 1.5289 -0.1360 0.2764 -0.0141 171 LEU A N 912 C CA . LEU A 158 ? 1.2764 1.5029 1.5787 -0.1191 0.3131 -0.0058 171 LEU A CA 913 C C . LEU A 158 ? 1.3064 1.5894 1.6725 -0.1078 0.3106 0.0018 171 LEU A C 914 O O . LEU A 158 ? 1.4520 1.7964 1.8686 -0.1056 0.3331 0.0194 171 LEU A O 915 C CB . LEU A 158 ? 1.2585 1.4594 1.5192 -0.0895 0.3403 -0.0260 171 LEU A CB 916 C CG . LEU A 158 ? 1.2715 1.4137 1.4609 -0.0936 0.3405 -0.0377 171 LEU A CG 917 C CD1 . LEU A 158 ? 1.2168 1.3510 1.3762 -0.0660 0.3709 -0.0564 171 LEU A CD1 918 C CD2 . LEU A 158 ? 1.3081 1.4538 1.4910 -0.1217 0.3453 -0.0172 171 LEU A CD2 919 N N . SER A 159 ? 1.1910 1.4565 1.5550 -0.0978 0.2852 -0.0106 172 SER A N 920 C CA . SER A 159 ? 1.1509 1.4734 1.5771 -0.0904 0.2784 0.0006 172 SER A CA 921 C C . SER A 159 ? 1.2813 1.5869 1.7043 -0.0944 0.2392 -0.0075 172 SER A C 922 O O . SER A 159 ? 1.2072 1.4552 1.5797 -0.0864 0.2239 -0.0283 172 SER A O 923 C CB . SER A 159 ? 1.0496 1.3990 1.4995 -0.0530 0.3110 -0.0031 172 SER A CB 924 O OG . SER A 159 ? 1.1826 1.5016 1.6152 -0.0299 0.2987 -0.0212 172 SER A OG 925 N N . CYS A 160 ? 1.4494 1.8107 1.9274 -0.1067 0.2231 0.0096 173 CYS A N 926 C CA . CYS A 160 ? 1.5206 1.8741 1.9978 -0.1122 0.1858 0.0028 173 CYS A CA 927 C C . CYS A 160 ? 1.5630 1.9892 2.1063 -0.1004 0.1830 0.0187 173 CYS A C 928 O O . CYS A 160 ? 1.5859 2.0784 2.1842 -0.1130 0.1906 0.0421 173 CYS A O 929 C CB . CYS A 160 ? 1.5456 1.8779 2.0061 -0.1531 0.1547 0.0044 173 CYS A CB 930 S SG . CYS A 160 ? 1.6844 1.9980 2.1313 -0.1601 0.1087 -0.0096 173 CYS A SG 931 N N . PHE A 161 ? 1.5169 1.9329 2.0549 -0.0762 0.1717 0.0077 174 PHE A N 932 C CA . PHE A 161 ? 1.4191 1.9013 2.0166 -0.0621 0.1666 0.0236 174 PHE A CA 933 C C . PHE A 161 ? 1.4181 1.8863 2.0006 -0.0637 0.1294 0.0134 174 PHE A C 934 O O . PHE A 161 ? 1.3675 1.7767 1.9000 -0.0497 0.1220 -0.0082 174 PHE A O 935 C CB . PHE A 161 ? 1.3083 1.8049 1.9274 -0.0204 0.2016 0.0256 174 PHE A CB 936 C CG . PHE A 161 ? 1.4293 1.9745 2.0907 -0.0152 0.2374 0.0440 174 PHE A CG 937 C CD1 . PHE A 161 ? 1.5389 2.1664 2.2726 -0.0061 0.2456 0.0704 174 PHE A CD1 938 C CD2 . PHE A 161 ? 1.5455 2.0585 2.1749 -0.0181 0.2635 0.0361 174 PHE A CD2 939 C CE1 . PHE A 161 ? 1.6074 2.2836 2.3813 0.0009 0.2802 0.0880 174 PHE A CE1 940 C CE2 . PHE A 161 ? 1.5921 2.1533 2.2598 -0.0124 0.2979 0.0528 174 PHE A CE2 941 C CZ . PHE A 161 ? 1.6168 2.2592 2.3570 -0.0024 0.3066 0.0785 174 PHE A CZ 942 N N . PHE A 162 ? 1.4542 1.9814 2.0805 -0.0815 0.1057 0.0293 175 PHE A N 943 C CA . PHE A 162 ? 1.4009 1.9332 2.0245 -0.0778 0.0737 0.0234 175 PHE A CA 944 C C . PHE A 162 ? 1.3106 1.9210 2.0008 -0.0541 0.0822 0.0468 175 PHE A C 945 O O . PHE A 162 ? 1.3235 2.0040 2.0702 -0.0631 0.0909 0.0710 175 PHE A O 946 C CB . PHE A 162 ? 1.3865 1.9229 2.0016 -0.1190 0.0352 0.0206 175 PHE A CB 947 C CG . PHE A 162 ? 1.3137 1.8581 1.9230 -0.1161 0.0018 0.0131 175 PHE A CG 948 C CD1 . PHE A 162 ? 1.3162 1.7897 1.8618 -0.1143 -0.0177 -0.0135 175 PHE A CD1 949 C CD2 . PHE A 162 ? 1.2519 1.8788 1.9196 -0.1133 -0.0093 0.0338 175 PHE A CD2 950 C CE1 . PHE A 162 ? 1.2816 1.7655 1.8207 -0.1108 -0.0477 -0.0203 175 PHE A CE1 951 C CE2 . PHE A 162 ? 1.2771 1.9156 1.9388 -0.1103 -0.0395 0.0279 175 PHE A CE2 952 C CZ . PHE A 162 ? 1.2951 1.8614 1.8917 -0.1092 -0.0587 0.0001 175 PHE A CZ 953 N N . ARG A 163 ? 1.2111 1.8100 1.8952 -0.0228 0.0809 0.0410 176 ARG A N 954 C CA . ARG A 163 ? 1.0890 1.7578 1.8339 0.0018 0.0859 0.0642 176 ARG A CA 955 C C . ARG A 163 ? 1.0705 1.7962 1.8734 0.0138 0.1214 0.0886 176 ARG A C 956 O O . ARG A 163 ? 1.0678 1.8763 1.9343 0.0158 0.1197 0.1159 176 ARG A O 957 C CB . ARG A 163 ? 1.0613 1.7854 1.8309 -0.0204 0.0467 0.0747 176 ARG A CB 958 C CG . ARG A 163 ? 1.1608 1.9382 1.9724 0.0086 0.0422 0.0925 176 ARG A CG 959 C CD . ARG A 163 ? 1.2151 2.0032 2.0109 -0.0075 -0.0008 0.0860 176 ARG A CD 960 N NE . ARG A 163 ? 1.2600 2.0864 2.0662 -0.0515 -0.0285 0.0891 176 ARG A NE 961 C CZ . ARG A 163 ? 1.1825 2.1028 2.0503 -0.0637 -0.0384 0.1159 176 ARG A CZ 962 N NH1 . ARG A 163 ? 1.2073 2.1945 2.1340 -0.0323 -0.0216 0.1442 176 ARG A NH1 963 N NH2 . ARG A 163 ? 1.0935 2.0410 1.9643 -0.1076 -0.0648 0.1147 176 ARG A NH2 964 N N . GLY A 164 ? 1.0940 1.7790 1.8749 0.0217 0.1537 0.0792 177 GLY A N 965 C CA . GLY A 164 ? 1.1696 1.9021 2.0001 0.0393 0.1920 0.0990 177 GLY A CA 966 C C . GLY A 164 ? 1.2112 2.0043 2.0803 0.0092 0.1940 0.1195 177 GLY A C 967 O O . GLY A 164 ? 1.1075 1.9400 2.0145 0.0224 0.2274 0.1354 177 GLY A O 968 N N . GLU A 165 ? 1.3233 2.1246 2.1832 -0.0317 0.1589 0.1190 178 GLU A N 969 C CA . GLU A 165 ? 1.3236 2.1712 2.2113 -0.0675 0.1580 0.1355 178 GLU A CA 970 C C . GLU A 165 ? 1.2419 2.0171 2.0709 -0.0916 0.1621 0.1161 178 GLU A C 971 O O . GLU A 165 ? 1.1727 1.8815 1.9452 -0.1088 0.1369 0.0936 178 GLU A O 972 C CB . GLU A 165 ? 1.3285 2.2306 2.2436 -0.1015 0.1181 0.1472 178 GLU A CB 973 N N . GLN A 166 ? 1.1829 1.9723 2.0251 -0.0910 0.1949 0.1259 179 GLN A N 974 C CA . GLN A 166 ? 1.2090 1.9347 1.9978 -0.1112 0.2021 0.1111 179 GLN A CA 975 C C . GLN A 166 ? 1.2026 1.9107 1.9709 -0.1593 0.1663 0.1084 179 GLN A C 976 O O . GLN A 166 ? 1.3410 2.1125 2.1547 -0.1880 0.1538 0.1289 179 GLN A O 977 C CB . GLN A 166 ? 1.2704 2.0341 2.0875 -0.1081 0.2407 0.1281 179 GLN A CB 978 C CG . GLN A 166 ? 1.3177 2.0286 2.0866 -0.1319 0.2493 0.1191 179 GLN A CG 979 C CD . GLN A 166 ? 1.3742 2.0896 2.1433 -0.1073 0.2952 0.1212 179 GLN A CD 980 O OE1 . GLN A 166 ? 1.3311 2.1191 2.1548 -0.1030 0.3188 0.1445 179 GLN A OE1 981 N NE2 . GLN A 166 ? 1.3870 2.0279 2.0945 -0.0908 0.3085 0.0963 179 GLN A NE2 982 N N . CYS A 167 ? 1.1434 1.7655 1.8436 -0.1683 0.1502 0.0829 180 CYS A N 983 C CA . CYS A 167 ? 1.1726 1.7617 1.8447 -0.2127 0.1205 0.0774 180 CYS A CA 984 C C . CYS A 167 ? 1.2854 1.8369 1.9285 -0.2297 0.1403 0.0787 180 CYS A C 985 O O . CYS A 167 ? 1.3687 1.9362 2.0225 -0.2105 0.1759 0.0867 180 CYS A O 986 C CB . CYS A 167 ? 1.1346 1.6548 1.7511 -0.2121 0.0891 0.0506 180 CYS A CB 987 S SG . CYS A 167 ? 2.8319 3.2641 3.3783 -0.1750 0.1065 0.0236 180 CYS A SG 988 N N . SER A 168 ? 1.3298 1.8329 1.9373 -0.2659 0.1178 0.0716 181 SER A N 989 C CA . SER A 168 ? 1.4485 1.9137 2.0272 -0.2839 0.1343 0.0753 181 SER A CA 990 C C . SER A 168 ? 1.5098 1.8998 2.0365 -0.3165 0.1056 0.0616 181 SER A C 991 O O . SER A 168 ? 1.4963 1.8691 2.0127 -0.3276 0.0725 0.0487 181 SER A O 992 C CB . SER A 168 ? 1.5545 2.0964 2.1922 -0.3050 0.1524 0.1057 181 SER A CB 993 O OG . SER A 168 ? 1.6045 2.2034 2.2893 -0.3354 0.1263 0.1190 181 SER A OG 994 N N . PRO A 169 ? 1.5514 1.8976 2.0457 -0.3317 0.1188 0.0651 182 PRO A N 995 C CA . PRO A 169 ? 1.6090 1.8768 2.0518 -0.3589 0.0948 0.0530 182 PRO A CA 996 C C . PRO A 169 ? 1.8681 2.1470 2.3317 -0.3994 0.0597 0.0545 182 PRO A C 997 O O . PRO A 169 ? 2.0626 2.2735 2.4820 -0.4143 0.0342 0.0370 182 PRO A O 998 C CB . PRO A 169 ? 1.4300 1.6808 1.8600 -0.3743 0.1190 0.0691 182 PRO A CB 999 C CG . PRO A 169 ? 1.4263 1.7055 1.8617 -0.3363 0.1555 0.0720 182 PRO A CG 1000 C CD . PRO A 169 ? 1.5029 1.8588 1.9956 -0.3171 0.1579 0.0765 182 PRO A CD 1001 N N . GLU A 170 ? 1.8644 2.2286 2.3934 -0.4167 0.0584 0.0744 183 GLU A N 1002 C CA . GLU A 170 ? 1.9166 2.2993 2.4674 -0.4574 0.0245 0.0751 183 GLU A CA 1003 C C . GLU A 170 ? 1.8532 2.2031 2.3753 -0.4472 -0.0077 0.0481 183 GLU A C 1004 O O . GLU A 170 ? 1.8743 2.2006 2.3851 -0.4806 -0.0387 0.0379 183 GLU A O 1005 C CB . GLU A 170 ? 2.0053 2.4988 2.6349 -0.4711 0.0296 0.1019 183 GLU A CB 1006 C CG . GLU A 170 ? 2.0635 2.6151 2.7285 -0.4375 0.0699 0.1211 183 GLU A CG 1007 C CD . GLU A 170 ? 2.1439 2.7442 2.8472 -0.4649 0.0914 0.1507 183 GLU A CD 1008 O OE1 . GLU A 170 ? 2.1392 2.7280 2.8296 -0.4464 0.1244 0.1574 183 GLU A OE1 1009 O OE2 . GLU A 170 ? 2.1595 2.8133 2.9058 -0.5053 0.0755 0.1673 183 GLU A OE2 1010 N N . ASP A 171 ? 1.7837 2.1290 2.2916 -0.4015 0.0003 0.0357 184 ASP A N 1011 C CA . ASP A 171 ? 1.7682 2.1079 2.2636 -0.3879 -0.0275 0.0158 184 ASP A CA 1012 C C . ASP A 171 ? 1.7920 2.0336 2.2126 -0.3787 -0.0441 -0.0138 184 ASP A C 1013 O O . ASP A 171 ? 1.7372 1.9706 2.1422 -0.3663 -0.0669 -0.0316 184 ASP A O 1014 C CB . ASP A 171 ? 1.7562 2.1557 2.2862 -0.3453 -0.0124 0.0217 184 ASP A CB 1015 C CG . ASP A 171 ? 1.7563 2.2574 2.3629 -0.3503 0.0042 0.0521 184 ASP A CG 1016 O OD1 . ASP A 171 ? 1.6900 2.2563 2.3406 -0.3681 -0.0166 0.0617 184 ASP A OD1 1017 O OD2 . ASP A 171 ? 1.7921 2.3108 2.4146 -0.3359 0.0384 0.0666 184 ASP A OD2 1018 N N . PHE A 172 ? 1.8404 2.0119 2.2163 -0.3849 -0.0329 -0.0173 185 PHE A N 1019 C CA . PHE A 172 ? 1.7442 1.8224 2.0488 -0.3750 -0.0454 -0.0423 185 PHE A CA 1020 C C . PHE A 172 ? 1.7721 1.7913 2.0489 -0.4156 -0.0648 -0.0475 185 PHE A C 1021 O O . PHE A 172 ? 1.8636 1.8600 2.1356 -0.4339 -0.0492 -0.0335 185 PHE A O 1022 C CB . PHE A 172 ? 1.6527 1.6903 1.9212 -0.3464 -0.0153 -0.0418 185 PHE A CB 1023 C CG . PHE A 172 ? 1.5720 1.6510 1.8577 -0.3055 0.0072 -0.0402 185 PHE A CG 1024 C CD1 . PHE A 172 ? 1.4719 1.5171 1.7187 -0.2709 0.0035 -0.0607 185 PHE A CD1 1025 C CD2 . PHE A 172 ? 1.5342 1.6848 1.8745 -0.3015 0.0329 -0.0183 185 PHE A CD2 1026 C CE1 . PHE A 172 ? 1.4262 1.5039 1.6878 -0.2353 0.0245 -0.0599 185 PHE A CE1 1027 C CE2 . PHE A 172 ? 1.5282 1.7106 1.8832 -0.2631 0.0550 -0.0182 185 PHE A CE2 1028 C CZ . PHE A 172 ? 1.4570 1.6008 1.7723 -0.2308 0.0508 -0.0394 185 PHE A CZ 1029 N N . LYS A 173 ? 1.6953 1.6855 1.9510 -0.4291 -0.0976 -0.0680 186 LYS A N 1030 C CA . LYS A 173 ? 1.6981 1.6195 1.9214 -0.4657 -0.1145 -0.0760 186 LYS A CA 1031 C C . LYS A 173 ? 1.8309 1.6599 1.9872 -0.4441 -0.1055 -0.0876 186 LYS A C 1032 O O . LYS A 173 ? 1.7842 1.5974 1.9108 -0.4038 -0.0998 -0.0997 186 LYS A O 1033 C CB . LYS A 173 ? 1.5575 1.4743 1.7767 -0.4891 -0.1518 -0.0964 186 LYS A CB 1034 N N . VAL A 174 ? 2.0130 1.7834 2.1470 -0.4714 -0.1035 -0.0819 187 VAL A N 1035 C CA . VAL A 174 ? 1.9748 1.6597 2.0472 -0.4524 -0.0939 -0.0883 187 VAL A CA 1036 C C . VAL A 174 ? 2.0990 1.7072 2.1186 -0.4519 -0.1215 -0.1168 187 VAL A C 1037 O O . VAL A 174 ? 2.2052 1.7921 2.2271 -0.4873 -0.1445 -0.1256 187 VAL A O 1038 C CB . VAL A 174 ? 1.7555 1.4131 1.8281 -0.4778 -0.0749 -0.0647 187 VAL A CB 1039 C CG1 . VAL A 174 ? 1.7171 1.2776 1.7234 -0.4648 -0.0719 -0.0718 187 VAL A CG1 1040 C CG2 . VAL A 174 ? 1.5728 1.2982 1.6834 -0.4657 -0.0426 -0.0396 187 VAL A CG2 1041 N N . VAL A 175 ? 2.0317 1.6014 2.0041 -0.4115 -0.1192 -0.1320 188 VAL A N 1042 C CA . VAL A 175 ? 2.0692 1.5643 1.9871 -0.4046 -0.1415 -0.1581 188 VAL A CA 1043 C C . VAL A 175 ? 2.0614 1.4845 1.9242 -0.3805 -0.1259 -0.1563 188 VAL A C 1044 O O . VAL A 175 ? 1.9696 1.4101 1.8241 -0.3486 -0.1045 -0.1485 188 VAL A O 1045 C CB . VAL A 175 ? 2.0690 1.5911 1.9800 -0.3765 -0.1587 -0.1805 188 VAL A CB 1046 C CG1 . VAL A 175 ? 2.0452 1.6183 1.9688 -0.3381 -0.1371 -0.1721 188 VAL A CG1 1047 C CG2 . VAL A 175 ? 2.0894 1.5314 1.9363 -0.3606 -0.1764 -0.2066 188 VAL A CG2 1048 N N . PHE A 176 ? 2.1432 1.4850 1.9680 -0.3963 -0.1365 -0.1635 189 PHE A N 1049 C CA . PHE A 176 ? 2.1209 1.3922 1.8920 -0.3731 -0.1236 -0.1604 189 PHE A CA 1050 C C . PHE A 176 ? 2.0353 1.2762 1.7589 -0.3346 -0.1359 -0.1857 189 PHE A C 1051 O O . PHE A 176 ? 1.9909 1.2164 1.7037 -0.3384 -0.1609 -0.2094 189 PHE A O 1052 C CB . PHE A 176 ? 2.2162 1.4108 1.9683 -0.4045 -0.1260 -0.1529 189 PHE A CB 1053 C CG . PHE A 176 ? 2.2140 1.4342 2.0042 -0.4350 -0.1063 -0.1215 189 PHE A CG 1054 C CD1 . PHE A 176 ? 2.1970 1.4284 1.9821 -0.4166 -0.0773 -0.0978 189 PHE A CD1 1055 C CD2 . PHE A 176 ? 2.2077 1.4474 2.0397 -0.4823 -0.1164 -0.1154 189 PHE A CD2 1056 C CE1 . PHE A 176 ? 2.1877 1.4478 2.0078 -0.4434 -0.0582 -0.0683 189 PHE A CE1 1057 C CE2 . PHE A 176 ? 2.2502 1.5191 2.1189 -0.5103 -0.0977 -0.0849 189 PHE A CE2 1058 C CZ . PHE A 176 ? 2.2458 1.5250 2.1085 -0.4899 -0.0681 -0.0611 189 PHE A CZ 1059 N N . THR A 177 ? 2.0819 1.3214 1.7787 -0.2978 -0.1178 -0.1802 190 THR A N 1060 C CA . THR A 177 ? 2.1012 1.3138 1.7510 -0.2597 -0.1265 -0.2006 190 THR A CA 1061 C C . THR A 177 ? 2.1252 1.2789 1.7271 -0.2402 -0.1104 -0.1897 190 THR A C 1062 O O . THR A 177 ? 2.1050 1.2467 1.7140 -0.2557 -0.0924 -0.1663 190 THR A O 1063 C CB . THR A 177 ? 1.9307 1.2146 1.5979 -0.2309 -0.1210 -0.2053 190 THR A CB 1064 O OG1 . THR A 177 ? 1.9247 1.2323 1.5938 -0.2151 -0.0924 -0.1864 190 THR A OG1 1065 C CG2 . THR A 177 ? 1.8640 1.2186 1.5898 -0.2516 -0.1292 -0.2053 190 THR A CG2 1066 N N . ARG A 178 ? 2.1192 1.2425 1.6737 -0.2053 -0.1163 -0.2049 191 ARG A N 1067 C CA . ARG A 178 ? 2.1267 1.1973 1.6333 -0.1832 -0.1029 -0.1947 191 ARG A CA 1068 C C . ARG A 178 ? 2.1872 1.3018 1.7035 -0.1718 -0.0746 -0.1723 191 ARG A C 1069 O O . ARG A 178 ? 2.3030 1.3864 1.7866 -0.1580 -0.0595 -0.1574 191 ARG A O 1070 C CB . ARG A 178 ? 2.0270 1.0675 1.4846 -0.1472 -0.1159 -0.2158 191 ARG A CB 1071 N N . TYR A 179 ? 2.1000 1.2883 1.6609 -0.1770 -0.0669 -0.1697 192 TYR A N 1072 C CA . TYR A 179 ? 2.0754 1.3067 1.6480 -0.1690 -0.0390 -0.1507 192 TYR A CA 1073 C C . TYR A 179 ? 2.2084 1.4403 1.8078 -0.2002 -0.0232 -0.1249 192 TYR A C 1074 O O . TYR A 179 ? 2.3384 1.5722 1.9253 -0.1940 -0.0006 -0.1058 192 TYR A O 1075 C CB . TYR A 179 ? 2.0379 1.3444 1.6458 -0.1585 -0.0338 -0.1580 192 TYR A CB 1076 C CG . TYR A 179 ? 2.1523 1.4626 1.7322 -0.1259 -0.0451 -0.1795 192 TYR A CG 1077 C CD1 . TYR A 179 ? 2.1275 1.4632 1.6893 -0.0980 -0.0286 -0.1797 192 TYR A CD1 1078 C CD2 . TYR A 179 ? 2.2714 1.5605 1.8412 -0.1240 -0.0725 -0.2000 192 TYR A CD2 1079 C CE1 . TYR A 179 ? 2.1594 1.5001 1.6963 -0.0701 -0.0393 -0.1982 192 TYR A CE1 1080 C CE2 . TYR A 179 ? 2.3022 1.5974 1.8465 -0.0944 -0.0829 -0.2182 192 TYR A CE2 1081 C CZ . TYR A 179 ? 2.2988 1.6198 1.8275 -0.0680 -0.0664 -0.2164 192 TYR A CZ 1082 O OH . TYR A 179 ? 2.3380 1.6662 1.8425 -0.0410 -0.0774 -0.2334 192 TYR A OH 1083 N N . GLY A 180 ? 2.1941 1.4304 1.8315 -0.2349 -0.0347 -0.1235 193 GLY A N 1084 C CA . GLY A 180 ? 2.1783 1.4263 1.8481 -0.2671 -0.0196 -0.0977 193 GLY A CA 1085 C C . GLY A 180 ? 2.1113 1.4106 1.8400 -0.2982 -0.0287 -0.0983 193 GLY A C 1086 O O . GLY A 180 ? 2.0562 1.3574 1.7936 -0.3035 -0.0526 -0.1186 193 GLY A O 1087 N N . LYS A 181 ? 2.0792 1.4237 1.8486 -0.3190 -0.0094 -0.0747 194 LYS A N 1088 C CA . LYS A 181 ? 2.0269 1.4399 1.8582 -0.3428 -0.0126 -0.0712 194 LYS A CA 1089 C C . LYS A 181 ? 2.0779 1.5510 1.9261 -0.3137 -0.0122 -0.0861 194 LYS A C 1090 O O . LYS A 181 ? 2.0592 1.5560 1.8974 -0.2848 0.0086 -0.0837 194 LYS A O 1091 C CB . LYS A 181 ? 1.9729 1.4271 1.8413 -0.3645 0.0126 -0.0410 194 LYS A CB 1092 C CG . LYS A 181 ? 1.9491 1.4488 1.8766 -0.4053 0.0048 -0.0307 194 LYS A CG 1093 C CD . LYS A 181 ? 1.9372 1.4868 1.9017 -0.4217 0.0329 0.0004 194 LYS A CD 1094 C CE . LYS A 181 ? 1.9752 1.5674 1.9968 -0.4661 0.0244 0.0135 194 LYS A CE 1095 N NZ . LYS A 181 ? 1.9796 1.6155 2.0351 -0.4856 0.0509 0.0459 194 LYS A NZ 1096 N N . CYS A 182 ? 2.0847 1.5830 1.9591 -0.3228 -0.0349 -0.1009 195 CYS A N 1097 C CA . CYS A 182 ? 1.9621 1.5121 1.8523 -0.2959 -0.0378 -0.1145 195 CYS A CA 1098 C C . CYS A 182 ? 1.9248 1.5445 1.8778 -0.3175 -0.0462 -0.1098 195 CYS A C 1099 O O . CYS A 182 ? 2.0679 1.6888 2.0452 -0.3546 -0.0566 -0.1019 195 CYS A O 1100 C CB . CYS A 182 ? 1.9297 1.4358 1.7757 -0.2750 -0.0613 -0.1411 195 CYS A CB 1101 S SG . CYS A 182 ? 3.3911 2.9348 3.2293 -0.2299 -0.0553 -0.1547 195 CYS A SG 1102 N N . TYR A 183 ? 1.7923 1.4703 1.7716 -0.2946 -0.0422 -0.1142 196 TYR A N 1103 C CA . TYR A 183 ? 1.7277 1.4831 1.7718 -0.3103 -0.0451 -0.1044 196 TYR A CA 1104 C C . TYR A 183 ? 1.6617 1.4529 1.7196 -0.2923 -0.0631 -0.1197 196 TYR A C 1105 O O . TYR A 183 ? 1.7378 1.5330 1.7799 -0.2571 -0.0551 -0.1283 196 TYR A O 1106 C CB . TYR A 183 ? 1.6857 1.4973 1.7677 -0.3030 -0.0117 -0.0826 196 TYR A CB 1107 C CG . TYR A 183 ? 1.7091 1.4978 1.7846 -0.3240 0.0067 -0.0636 196 TYR A CG 1108 C CD1 . TYR A 183 ? 1.7169 1.5317 1.8324 -0.3635 0.0048 -0.0451 196 TYR A CD1 1109 C CD2 . TYR A 183 ? 1.7035 1.4466 1.7322 -0.3056 0.0252 -0.0630 196 TYR A CD2 1110 C CE1 . TYR A 183 ? 1.7529 1.5476 1.8629 -0.3833 0.0217 -0.0257 196 TYR A CE1 1111 C CE2 . TYR A 183 ? 1.7180 1.4428 1.7405 -0.3241 0.0421 -0.0434 196 TYR A CE2 1112 C CZ . TYR A 183 ? 1.7614 1.5110 1.8249 -0.3628 0.0406 -0.0243 196 TYR A CZ 1113 O OH . TYR A 183 ? 1.8327 1.5653 1.8910 -0.3823 0.0578 -0.0025 196 TYR A OH 1114 N N . THR A 184 ? 1.6136 1.4340 1.7021 -0.3178 -0.0872 -0.1219 197 THR A N 1115 C CA . THR A 184 ? 1.6714 1.5291 1.7737 -0.3040 -0.1074 -0.1347 197 THR A CA 1116 C C . THR A 184 ? 1.7039 1.6565 1.8766 -0.3078 -0.1032 -0.1177 197 THR A C 1117 O O . THR A 184 ? 1.7846 1.7751 1.9964 -0.3423 -0.1139 -0.1071 197 THR A O 1118 C CB . THR A 184 ? 1.7807 1.6033 1.8600 -0.3273 -0.1422 -0.1539 197 THR A CB 1119 O OG1 . THR A 184 ? 1.8590 1.5933 1.8722 -0.3180 -0.1464 -0.1705 197 THR A OG1 1120 C CG2 . THR A 184 ? 1.7781 1.6440 1.8708 -0.3137 -0.1635 -0.1661 197 THR A CG2 1121 N N . PHE A 185 ? 1.6035 1.5947 1.7924 -0.2726 -0.0881 -0.1146 198 PHE A N 1122 C CA . PHE A 185 ? 1.5097 1.5898 1.7651 -0.2696 -0.0821 -0.0971 198 PHE A CA 1123 C C . PHE A 185 ? 1.6368 1.7540 1.9088 -0.2710 -0.1119 -0.1051 198 PHE A C 1124 O O . PHE A 185 ? 1.6560 1.7360 1.8869 -0.2562 -0.1298 -0.1257 198 PHE A O 1125 C CB . PHE A 185 ? 1.3203 1.4268 1.5909 -0.2319 -0.0508 -0.0887 198 PHE A CB 1126 C CG . PHE A 185 ? 1.4016 1.5975 1.7417 -0.2255 -0.0428 -0.0690 198 PHE A CG 1127 C CD1 . PHE A 185 ? 1.5233 1.7718 1.9138 -0.2426 -0.0247 -0.0453 198 PHE A CD1 1128 C CD2 . PHE A 185 ? 1.3220 1.5524 1.6786 -0.2019 -0.0530 -0.0721 198 PHE A CD2 1129 C CE1 . PHE A 185 ? 1.4486 1.7826 1.9047 -0.2340 -0.0165 -0.0254 198 PHE A CE1 1130 C CE2 . PHE A 185 ? 1.2360 1.5490 1.6577 -0.1937 -0.0450 -0.0514 198 PHE A CE2 1131 C CZ . PHE A 185 ? 1.2984 1.6632 1.7698 -0.2088 -0.0266 -0.0283 198 PHE A CZ 1132 N N . ASN A 186 ? 1.6441 1.8403 1.9779 -0.2882 -0.1163 -0.0870 199 ASN A N 1133 C CA . ASN A 186 ? 1.5688 1.8139 1.9258 -0.2964 -0.1457 -0.0904 199 ASN A CA 1134 C C . ASN A 186 ? 1.6825 1.8757 1.9970 -0.3261 -0.1783 -0.1131 199 ASN A C 1135 O O . ASN A 186 ? 1.6685 1.8492 1.9564 -0.3163 -0.2013 -0.1317 199 ASN A O 1136 C CB . ASN A 186 ? 1.4398 1.7034 1.7955 -0.2551 -0.1454 -0.0950 199 ASN A CB 1137 C CG . ASN A 186 ? 1.3901 1.7352 1.7934 -0.2584 -0.1651 -0.0852 199 ASN A CG 1138 O OD1 . ASN A 186 ? 1.4317 1.8298 1.8755 -0.2904 -0.1762 -0.0728 199 ASN A OD1 1139 N ND2 . ASN A 186 ? 1.3385 1.6978 1.7384 -0.2261 -0.1695 -0.0892 199 ASN A ND2 1140 N N . ALA A 187 ? 1.8032 1.9658 2.1116 -0.3624 -0.1789 -0.1110 200 ALA A N 1141 C CA . ALA A 187 ? 1.9203 2.0214 2.1864 -0.3935 -0.2057 -0.1327 200 ALA A CA 1142 C C . ALA A 187 ? 1.8768 2.0179 2.1561 -0.4150 -0.2407 -0.1442 200 ALA A C 1143 O O . ALA A 187 ? 1.7491 1.8420 1.9814 -0.4133 -0.2635 -0.1706 200 ALA A O 1144 C CB . ALA A 187 ? 2.0311 2.1049 2.3015 -0.4317 -0.1972 -0.1221 200 ALA A CB 1145 N N . GLY A 188 ? 1.9229 2.1545 2.2657 -0.4354 -0.2448 -0.1242 201 GLY A N 1146 C CA . GLY A 188 ? 1.9920 2.2694 2.3513 -0.4645 -0.2783 -0.1327 201 GLY A CA 1147 C C . GLY A 188 ? 2.1350 2.3557 2.4655 -0.5130 -0.2979 -0.1499 201 GLY A C 1148 O O . GLY A 188 ? 2.1615 2.3918 2.4841 -0.5387 -0.3287 -0.1676 201 GLY A O 1149 N N . GLN A 189 ? 2.1890 2.3528 2.5054 -0.5264 -0.2791 -0.1435 202 GLN A N 1150 C CA . GLN A 189 ? 2.1980 2.2837 2.4772 -0.5662 -0.2918 -0.1597 202 GLN A CA 1151 C C . GLN A 189 ? 2.2058 2.3319 2.5340 -0.6085 -0.2826 -0.1343 202 GLN A C 1152 O O . GLN A 189 ? 2.1878 2.3885 2.5690 -0.5983 -0.2616 -0.1055 202 GLN A O 1153 C CB . GLN A 189 ? 2.1555 2.1342 2.3720 -0.5426 -0.2760 -0.1713 202 GLN A CB 1154 N N . ASP A 190 ? 2.2502 2.3278 2.5613 -0.6560 -0.2981 -0.1449 203 ASP A N 1155 C CA . ASP A 190 ? 2.2735 2.3982 2.6339 -0.7050 -0.2964 -0.1227 203 ASP A CA 1156 C C . ASP A 190 ? 2.2184 2.4656 2.6408 -0.7128 -0.3095 -0.1100 203 ASP A C 1157 O O . ASP A 190 ? 2.2001 2.5294 2.6831 -0.7260 -0.2962 -0.0794 203 ASP A O 1158 C CB . ASP A 190 ? 2.2813 2.4098 2.6637 -0.6962 -0.2601 -0.0919 203 ASP A CB 1159 C CG . ASP A 190 ? 2.3893 2.4041 2.7172 -0.7005 -0.2483 -0.0988 203 ASP A CG 1160 O OD1 . ASP A 190 ? 2.4713 2.4196 2.7685 -0.7379 -0.2676 -0.1164 203 ASP A OD1 1161 O OD2 . ASP A 190 ? 2.3938 2.3862 2.7097 -0.6664 -0.2193 -0.0862 203 ASP A OD2 1162 N N . GLY A 191 ? 2.1718 2.4341 2.5786 -0.7012 -0.3347 -0.1322 204 GLY A N 1163 C CA . GLY A 191 ? 2.1079 2.4850 2.5684 -0.7090 -0.3514 -0.1218 204 GLY A CA 1164 C C . GLY A 191 ? 2.0163 2.4917 2.5407 -0.6792 -0.3265 -0.0854 204 GLY A C 1165 O O . GLY A 191 ? 2.0268 2.6065 2.6114 -0.6989 -0.3341 -0.0651 204 GLY A O 1166 N N . LYS A 192 ? 1.9270 2.3709 2.4388 -0.6322 -0.2962 -0.0771 205 LYS A N 1167 C CA . LYS A 192 ? 1.7495 2.2766 2.3148 -0.5954 -0.2712 -0.0475 205 LYS A CA 1168 C C . LYS A 192 ? 1.6792 2.2425 2.2438 -0.5562 -0.2828 -0.0553 205 LYS A C 1169 O O . LYS A 192 ? 1.6620 2.1754 2.1775 -0.5536 -0.3063 -0.0845 205 LYS A O 1170 C CB . LYS A 192 ? 1.6180 2.0958 2.1686 -0.5641 -0.2333 -0.0370 205 LYS A CB 1171 N N . PRO A 193 ? 1.5950 2.2471 2.2153 -0.5263 -0.2666 -0.0284 206 PRO A N 1172 C CA . PRO A 193 ? 1.5469 2.2381 2.1732 -0.4858 -0.2731 -0.0296 206 PRO A CA 1173 C C . PRO A 193 ? 1.5763 2.1961 2.1567 -0.4349 -0.2545 -0.0423 206 PRO A C 1174 O O . PRO A 193 ? 1.5821 2.1470 2.1435 -0.4199 -0.2267 -0.0405 206 PRO A O 1175 C CB . PRO A 193 ? 1.4439 2.2506 2.1501 -0.4740 -0.2570 0.0082 206 PRO A CB 1176 C CG . PRO A 193 ? 1.4631 2.2602 2.1877 -0.4823 -0.2267 0.0257 206 PRO A CG 1177 C CD . PRO A 193 ? 1.5430 2.2699 2.2281 -0.5311 -0.2414 0.0070 206 PRO A CD 1178 N N . ARG A 194 ? 1.5799 2.2052 2.1428 -0.4095 -0.2707 -0.0547 207 ARG A N 1179 C CA . ARG A 194 ? 1.6281 2.1964 2.1507 -0.3624 -0.2565 -0.0662 207 ARG A CA 1180 C C . ARG A 194 ? 1.4971 2.1342 2.0696 -0.3215 -0.2347 -0.0400 207 ARG A C 1181 O O . ARG A 194 ? 1.4727 2.1961 2.0915 -0.3196 -0.2468 -0.0238 207 ARG A O 1182 C CB . ARG A 194 ? 1.7117 2.2369 2.1799 -0.3588 -0.2863 -0.0965 207 ARG A CB 1183 C CG . ARG A 194 ? 1.7741 2.2319 2.1951 -0.3995 -0.3081 -0.1231 207 ARG A CG 1184 C CD . ARG A 194 ? 1.8214 2.2237 2.1809 -0.3897 -0.3323 -0.1554 207 ARG A CD 1185 N NE . ARG A 194 ? 2.0081 2.3392 2.3224 -0.4274 -0.3502 -0.1811 207 ARG A NE 1186 C CZ . ARG A 194 ? 2.0451 2.3136 2.2993 -0.4256 -0.3708 -0.2129 207 ARG A CZ 1187 N NH1 . ARG A 194 ? 1.9462 2.2195 2.1789 -0.3887 -0.3770 -0.2219 207 ARG A NH1 1188 N NH2 . ARG A 194 ? 2.0710 2.2715 2.2869 -0.4603 -0.3844 -0.2351 207 ARG A NH2 1189 N N . LEU A 195 ? 1.3852 1.9845 1.9486 -0.2891 -0.2017 -0.0354 208 LEU A N 1190 C CA . LEU A 195 ? 1.3021 1.9600 1.9149 -0.2518 -0.1759 -0.0102 208 LEU A CA 1191 C C . LEU A 195 ? 1.3126 1.9781 1.9157 -0.2160 -0.1848 -0.0149 208 LEU A C 1192 O O . LEU A 195 ? 1.3648 1.9677 1.9106 -0.2100 -0.2002 -0.0405 208 LEU A O 1193 C CB . LEU A 195 ? 1.1767 1.7908 1.7808 -0.2302 -0.1368 -0.0060 208 LEU A CB 1194 C CG . LEU A 195 ? 1.0260 1.6038 1.6196 -0.2566 -0.1212 -0.0055 208 LEU A CG 1195 C CD1 . LEU A 195 ? 0.9356 1.4901 1.5276 -0.2227 -0.0812 0.0008 208 LEU A CD1 1196 C CD2 . LEU A 195 ? 0.8975 1.5483 1.5471 -0.2933 -0.1248 0.0170 208 LEU A CD2 1197 N N . ILE A 196 ? 1.2088 1.9522 1.8694 -0.1915 -0.1740 0.0115 209 ILE A N 1198 C CA . ILE A 196 ? 1.1737 1.9368 1.8358 -0.1581 -0.1814 0.0136 209 ILE A CA 1199 C C . ILE A 196 ? 1.1652 1.9302 1.8519 -0.1148 -0.1440 0.0301 209 ILE A C 1200 O O . ILE A 196 ? 1.2893 2.0692 2.0074 -0.1130 -0.1160 0.0453 209 ILE A O 1201 C CB . ILE A 196 ? 1.2740 2.1396 1.9885 -0.1681 -0.2057 0.0341 209 ILE A CB 1202 C CG1 . ILE A 196 ? 1.1865 2.1206 1.9543 -0.2011 -0.2046 0.0548 209 ILE A CG1 1203 C CG2 . ILE A 196 ? 1.3110 2.1653 1.9843 -0.1877 -0.2462 0.0108 209 ILE A CG2 1204 C CD1 . ILE A 196 ? 1.2207 2.1234 1.9564 -0.2525 -0.2290 0.0336 209 ILE A CD1 1205 N N . THR A 197 ? 1.1002 1.8517 1.7734 -0.0804 -0.1429 0.0275 210 THR A N 1206 C CA . THR A 197 ? 1.1672 1.9137 1.8610 -0.0391 -0.1074 0.0408 210 THR A CA 1207 C C . THR A 197 ? 1.2292 2.0442 1.9687 -0.0120 -0.1117 0.0647 210 THR A C 1208 O O . THR A 197 ? 1.3083 2.1346 2.0317 -0.0131 -0.1404 0.0590 210 THR A O 1209 C CB . THR A 197 ? 1.5508 2.1994 2.1790 -0.0203 -0.0946 0.0141 210 THR A CB 1210 O OG1 . THR A 197 ? 1.5402 2.1801 2.1877 0.0151 -0.0575 0.0247 210 THR A OG1 1211 C CG2 . THR A 197 ? 1.5070 2.1309 2.0936 -0.0126 -0.1219 -0.0023 210 THR A CG2 1212 N N . MET A 198 ? 1.2618 2.1241 2.0589 0.0131 -0.0826 0.0926 211 MET A N 1213 C CA . MET A 198 ? 1.3214 2.2553 2.1705 0.0403 -0.0838 0.1213 211 MET A CA 1214 C C . MET A 198 ? 1.1480 2.0374 1.9818 0.0822 -0.0654 0.1195 211 MET A C 1215 O O . MET A 198 ? 1.1313 2.0663 1.9983 0.1067 -0.0682 0.1411 211 MET A O 1216 C CB . MET A 198 ? 1.4326 2.4482 2.3584 0.0478 -0.0614 0.1562 211 MET A CB 1217 C CG . MET A 198 ? 1.4462 2.5120 2.3935 0.0057 -0.0762 0.1614 211 MET A CG 1218 S SD . MET A 198 ? 1.8004 2.9075 2.7328 -0.0310 -0.1301 0.1535 211 MET A SD 1219 C CE . MET A 198 ? 1.4734 2.7153 2.4939 -0.0142 -0.1339 0.2004 211 MET A CE 1220 N N . LYS A 199 ? 1.0035 1.8052 1.7876 0.0895 -0.0461 0.0948 212 LYS A N 1221 C CA . LYS A 199 ? 0.9324 1.6892 1.7039 0.1267 -0.0237 0.0925 212 LYS A CA 1222 C C . LYS A 199 ? 1.2404 1.8963 1.9353 0.1240 -0.0198 0.0565 212 LYS A C 1223 O O . LYS A 199 ? 1.2375 1.8535 1.8955 0.0991 -0.0221 0.0363 212 LYS A O 1224 C CB . LYS A 199 ? 0.7418 1.5231 1.5680 0.1556 0.0177 0.1159 212 LYS A CB 1225 N N . GLY A 200 ? 1.1131 1.7300 1.7842 0.1491 -0.0147 0.0498 213 GLY A N 1226 C CA . GLY A 200 ? 1.0976 1.6271 1.7008 0.1488 -0.0088 0.0188 213 GLY A CA 1227 C C . GLY A 200 ? 1.1786 1.6711 1.7826 0.1599 0.0316 0.0140 213 GLY A C 1228 O O . GLY A 200 ? 1.1781 1.7135 1.8356 0.1679 0.0540 0.0346 213 GLY A O 1229 N N . GLY A 201 ? 1.2515 1.6684 1.7965 0.1608 0.0411 -0.0128 214 GLY A N 1230 C CA . GLY A 201 ? 1.3354 1.7126 1.8732 0.1726 0.0798 -0.0210 214 GLY A CA 1231 C C . GLY A 201 ? 1.3591 1.7293 1.8892 0.1505 0.0907 -0.0276 214 GLY A C 1232 O O . GLY A 201 ? 1.4523 1.8461 1.9836 0.1233 0.0680 -0.0256 214 GLY A O 1233 N N . THR A 202 ? 1.2261 1.5653 1.7495 0.1618 0.1266 -0.0350 215 THR A N 1234 C CA . THR A 202 ? 1.2586 1.5790 1.7619 0.1425 0.1395 -0.0447 215 THR A CA 1235 C C . THR A 202 ? 1.2570 1.6402 1.8127 0.1273 0.1423 -0.0228 215 THR A C 1236 O O . THR A 202 ? 1.3407 1.7250 1.8812 0.0975 0.1247 -0.0261 215 THR A O 1237 C CB . THR A 202 ? 1.3786 1.6523 1.8587 0.1596 0.1783 -0.0595 215 THR A CB 1238 O OG1 . THR A 202 ? 1.3428 1.5512 1.7516 0.1504 0.1700 -0.0865 215 THR A OG1 1239 C CG2 . THR A 202 ? 1.4984 1.7933 2.0021 0.1531 0.2062 -0.0523 215 THR A CG2 1240 N N . GLY A 203 ? 1.2678 1.7030 1.8855 0.1475 0.1646 0.0002 216 GLY A N 1241 C CA . GLY A 203 ? 1.3380 1.8376 2.0086 0.1356 0.1722 0.0226 216 GLY A CA 1242 C C . GLY A 203 ? 1.3800 1.9244 2.0647 0.1042 0.1340 0.0329 216 GLY A C 1243 O O . GLY A 203 ? 1.3674 1.9548 2.0810 0.0825 0.1338 0.0461 216 GLY A O 1244 N N . ASN A 204 ? 1.3965 1.9336 2.0619 0.1014 0.1017 0.0271 217 ASN A N 1245 C CA . ASN A 204 ? 1.3927 1.9692 2.0666 0.0720 0.0633 0.0331 217 ASN A CA 1246 C C . ASN A 204 ? 1.3221 1.8429 1.9325 0.0417 0.0372 0.0074 217 ASN A C 1247 O O . ASN A 204 ? 1.4462 1.9861 2.0523 0.0191 0.0029 0.0061 217 ASN A O 1248 C CB . ASN A 204 ? 1.5097 2.1342 2.2154 0.0874 0.0438 0.0488 217 ASN A CB 1249 C CG . ASN A 204 ? 1.5852 2.2692 2.3592 0.1174 0.0706 0.0784 217 ASN A CG 1250 O OD1 . ASN A 204 ? 1.6230 2.2808 2.3981 0.1507 0.0945 0.0785 217 ASN A OD1 1251 N ND2 . ASN A 204 ? 1.5614 2.3249 2.3932 0.1056 0.0683 0.1039 217 ASN A ND2 1252 N N . GLY A 205 ? 1.2440 1.6943 1.8029 0.0434 0.0534 -0.0137 218 GLY A N 1253 C CA . GLY A 205 ? 1.2799 1.6754 1.7801 0.0161 0.0338 -0.0355 218 GLY A CA 1254 C C . GLY A 205 ? 1.2921 1.6769 1.7888 -0.0050 0.0508 -0.0345 218 GLY A C 1255 O O . GLY A 205 ? 1.2939 1.7292 1.8412 -0.0060 0.0706 -0.0144 218 GLY A O 1256 N N . LEU A 206 ? 1.2896 1.6099 1.7267 -0.0207 0.0437 -0.0548 219 LEU A N 1257 C CA . LEU A 206 ? 1.2495 1.5498 1.6739 -0.0406 0.0596 -0.0546 219 LEU A CA 1258 C C . LEU A 206 ? 1.1822 1.4338 1.5700 -0.0204 0.0908 -0.0669 219 LEU A C 1259 O O . LEU A 206 ? 1.2395 1.4432 1.5816 -0.0054 0.0870 -0.0852 219 LEU A O 1260 C CB . LEU A 206 ? 1.2369 1.4960 1.6184 -0.0725 0.0308 -0.0672 219 LEU A CB 1261 C CG . LEU A 206 ? 1.2284 1.4463 1.5789 -0.0917 0.0441 -0.0706 219 LEU A CG 1262 C CD1 . LEU A 206 ? 1.3270 1.5986 1.7301 -0.1043 0.0657 -0.0477 219 LEU A CD1 1263 C CD2 . LEU A 206 ? 1.2039 1.3797 1.5155 -0.1215 0.0134 -0.0821 219 LEU A CD2 1264 N N . GLU A 207 ? 1.1767 1.4451 1.5851 -0.0202 0.1220 -0.0568 220 GLU A N 1265 C CA . GLU A 207 ? 1.2944 1.5208 1.6672 -0.0032 0.1524 -0.0694 220 GLU A CA 1266 C C . GLU A 207 ? 1.4765 1.6930 1.8360 -0.0254 0.1661 -0.0653 220 GLU A C 1267 O O . GLU A 207 ? 1.6720 1.9379 2.0777 -0.0332 0.1830 -0.0462 220 GLU A O 1268 C CB . GLU A 207 ? 1.3535 1.6114 1.7653 0.0282 0.1851 -0.0623 220 GLU A CB 1269 C CG . GLU A 207 ? 1.5201 1.7536 1.9105 0.0410 0.2235 -0.0710 220 GLU A CG 1270 C CD . GLU A 207 ? 1.7593 2.0262 2.1942 0.0715 0.2570 -0.0633 220 GLU A CD 1271 O OE1 . GLU A 207 ? 1.8710 2.1466 2.3128 0.0768 0.2906 -0.0616 220 GLU A OE1 1272 O OE2 . GLU A 207 ? 1.8055 2.0897 2.2683 0.0910 0.2510 -0.0586 220 GLU A OE2 1273 N N . ILE A 208 ? 1.3570 1.5125 1.6545 -0.0343 0.1602 -0.0815 221 ILE A N 1274 C CA . ILE A 208 ? 1.3169 1.4596 1.5981 -0.0551 0.1730 -0.0760 221 ILE A CA 1275 C C . ILE A 208 ? 1.3781 1.4837 1.6150 -0.0400 0.2015 -0.0887 221 ILE A C 1276 O O . ILE A 208 ? 1.4738 1.5477 1.6776 -0.0185 0.2042 -0.1065 221 ILE A O 1277 C CB . ILE A 208 ? 1.2272 1.3376 1.4803 -0.0862 0.1421 -0.0773 221 ILE A CB 1278 C CG1 . ILE A 208 ? 1.1911 1.2320 1.3749 -0.0796 0.1280 -0.0992 221 ILE A CG1 1279 C CG2 . ILE A 208 ? 1.2775 1.4226 1.5684 -0.1013 0.1118 -0.0696 221 ILE A CG2 1280 C CD1 . ILE A 208 ? 1.2196 1.2267 1.3784 -0.1063 0.0952 -0.1020 221 ILE A CD1 1281 N N . MET A 209 ? 1.3863 1.5013 1.6250 -0.0524 0.2232 -0.0784 222 MET A N 1282 C CA . MET A 209 ? 1.3271 1.4166 1.5267 -0.0411 0.2521 -0.0883 222 MET A CA 1283 C C . MET A 209 ? 1.4325 1.4994 1.6018 -0.0667 0.2509 -0.0807 222 MET A C 1284 O O . MET A 209 ? 1.3631 1.4640 1.5660 -0.0869 0.2571 -0.0606 222 MET A O 1285 C CB . MET A 209 ? 1.1946 1.3307 1.4347 -0.0237 0.2898 -0.0813 222 MET A CB 1286 C CG . MET A 209 ? 1.2010 1.3180 1.4026 -0.0139 0.3222 -0.0920 222 MET A CG 1287 S SD . MET A 209 ? 1.8380 2.0094 2.0866 0.0068 0.3686 -0.0854 222 MET A SD 1288 C CE . MET A 209 ? 1.6279 1.8261 1.9295 0.0311 0.3620 -0.0845 222 MET A CE 1289 N N . LEU A 210 ? 1.5396 1.5505 1.6460 -0.0655 0.2435 -0.0952 223 LEU A N 1290 C CA . LEU A 210 ? 1.5145 1.4956 1.5872 -0.0881 0.2390 -0.0872 223 LEU A CA 1291 C C . LEU A 210 ? 1.6403 1.6061 1.6711 -0.0806 0.2670 -0.0912 223 LEU A C 1292 O O . LEU A 210 ? 1.6763 1.6317 1.6807 -0.0576 0.2812 -0.1089 223 LEU A O 1293 C CB . LEU A 210 ? 1.2788 1.2063 1.3107 -0.0958 0.2037 -0.0971 223 LEU A CB 1294 C CG . LEU A 210 ? 1.2353 1.1749 1.2994 -0.1021 0.1738 -0.0976 223 LEU A CG 1295 C CD1 . LEU A 210 ? 1.2865 1.1710 1.3080 -0.1135 0.1408 -0.1065 223 LEU A CD1 1296 C CD2 . LEU A 210 ? 1.1802 1.1738 1.3071 -0.1235 0.1763 -0.0757 223 LEU A CD2 1297 N N . ASP A 211 ? 1.5969 1.5630 1.6219 -0.1016 0.2747 -0.0740 224 ASP A N 1298 C CA . ASP A 211 ? 1.5707 1.5103 1.5429 -0.0999 0.2906 -0.0757 224 ASP A CA 1299 C C . ASP A 211 ? 1.5572 1.4406 1.4863 -0.1141 0.2624 -0.0740 224 ASP A C 1300 O O . ASP A 211 ? 1.4952 1.3730 1.4397 -0.1394 0.2495 -0.0566 224 ASP A O 1301 C CB . ASP A 211 ? 1.6956 1.6742 1.6891 -0.1124 0.3196 -0.0553 224 ASP A CB 1302 C CG . ASP A 211 ? 1.8241 1.7749 1.7659 -0.1200 0.3285 -0.0486 224 ASP A CG 1303 O OD1 . ASP A 211 ? 1.7598 1.6728 1.6479 -0.1061 0.3244 -0.0646 224 ASP A OD1 1304 O OD2 . ASP A 211 ? 1.9489 1.9189 1.9048 -0.1401 0.3398 -0.0254 224 ASP A OD2 1305 N N . ILE A 212 ? 1.6129 1.4547 1.4890 -0.0977 0.2530 -0.0922 225 ILE A N 1306 C CA . ILE A 212 ? 1.5974 1.3834 1.4300 -0.1047 0.2261 -0.0933 225 ILE A CA 1307 C C . ILE A 212 ? 1.8379 1.6074 1.6466 -0.1215 0.2357 -0.0733 225 ILE A C 1308 O O . ILE A 212 ? 1.8446 1.5691 1.6275 -0.1329 0.2160 -0.0669 225 ILE A O 1309 C CB . ILE A 212 ? 1.4167 1.1716 1.1990 -0.0805 0.2182 -0.1159 225 ILE A CB 1310 N N . GLN A 213 ? 1.9581 1.7649 1.7768 -0.1222 0.2672 -0.0631 226 GLN A N 1311 C CA . GLN A 213 ? 1.8835 1.6880 1.6870 -0.1385 0.2816 -0.0402 226 GLN A CA 1312 C C . GLN A 213 ? 1.9446 1.7069 1.6828 -0.1302 0.2799 -0.0410 226 GLN A C 1313 O O . GLN A 213 ? 2.0363 1.7697 1.7578 -0.1460 0.2737 -0.0216 226 GLN A O 1314 C CB . GLN A 213 ? 1.7368 1.5298 1.5692 -0.1683 0.2649 -0.0190 226 GLN A CB 1315 C CG . GLN A 213 ? 1.5965 1.4438 1.4949 -0.1838 0.2735 -0.0068 226 GLN A CG 1316 C CD . GLN A 213 ? 1.6048 1.4360 1.5271 -0.2161 0.2529 0.0114 226 GLN A CD 1317 O OE1 . GLN A 213 ? 1.5925 1.3752 1.4970 -0.2216 0.2237 0.0032 226 GLN A OE1 1318 N NE2 . GLN A 213 ? 1.6102 1.4812 1.5712 -0.2388 0.2684 0.0359 226 GLN A NE2 1319 N N . GLN A 214 ? 1.9210 1.6809 1.6228 -0.1063 0.2864 -0.0616 227 GLN A N 1320 C CA . GLN A 214 ? 1.9457 1.6704 1.5857 -0.0975 0.2827 -0.0618 227 GLN A CA 1321 C C . GLN A 214 ? 2.0699 1.7978 1.6933 -0.1111 0.2995 -0.0348 227 GLN A C 1322 O O . GLN A 214 ? 2.2159 1.9036 1.8024 -0.1133 0.2880 -0.0228 227 GLN A O 1323 C CB . GLN A 214 ? 1.8352 1.5693 1.4408 -0.0732 0.2924 -0.0862 227 GLN A CB 1324 C CG . GLN A 214 ? 1.7474 1.4615 1.3505 -0.0584 0.2695 -0.1098 227 GLN A CG 1325 C CD . GLN A 214 ? 1.7293 1.4343 1.2799 -0.0385 0.2709 -0.1281 227 GLN A CD 1326 O OE1 . GLN A 214 ? 1.7190 1.4115 1.2247 -0.0366 0.2742 -0.1199 227 GLN A OE1 1327 N NE2 . GLN A 214 ? 1.7334 1.4467 1.2900 -0.0241 0.2683 -0.1517 227 GLN A NE2 1328 N N . ASP A 215 ? 1.9701 1.7461 1.6217 -0.1194 0.3270 -0.0238 228 ASP A N 1329 C CA . ASP A 215 ? 1.8812 1.6682 1.5196 -0.1327 0.3454 0.0036 228 ASP A CA 1330 C C . ASP A 215 ? 1.9960 1.7412 1.6366 -0.1550 0.3268 0.0304 228 ASP A C 1331 O O . ASP A 215 ? 1.9731 1.7052 1.5846 -0.1615 0.3340 0.0531 228 ASP A O 1332 C CB . ASP A 215 ? 1.7007 1.5505 1.3788 -0.1396 0.3767 0.0114 228 ASP A CB 1333 N N . GLU A 216 ? 1.9332 1.6578 1.6084 -0.1672 0.3035 0.0279 229 GLU A N 1334 C CA . GLU A 216 ? 1.9035 1.5818 1.5820 -0.1898 0.2836 0.0478 229 GLU A CA 1335 C C . GLU A 216 ? 1.8021 1.4147 1.4387 -0.1778 0.2553 0.0351 229 GLU A C 1336 O O . GLU A 216 ? 1.7923 1.3570 1.4298 -0.1932 0.2344 0.0435 229 GLU A O 1337 C CB . GLU A 216 ? 1.9225 1.6193 1.6621 -0.2144 0.2751 0.0539 229 GLU A CB 1338 N N . TYR A 217 ? 1.7376 1.3493 1.3387 -0.1503 0.2548 0.0132 230 TYR A N 1339 C CA . TYR A 217 ? 1.9054 1.4627 1.4629 -0.1349 0.2315 0.0019 230 TYR A CA 1340 C C . TYR A 217 ? 1.9880 1.5087 1.5012 -0.1349 0.2345 0.0254 230 TYR A C 1341 O O . TYR A 217 ? 1.9873 1.5363 1.4832 -0.1322 0.2580 0.0400 230 TYR A O 1342 C CB . TYR A 217 ? 2.0038 1.5784 1.5362 -0.1070 0.2330 -0.0255 230 TYR A CB 1343 C CG . TYR A 217 ? 2.0168 1.5916 1.5740 -0.1006 0.2138 -0.0505 230 TYR A CG 1344 C CD1 . TYR A 217 ? 1.9754 1.5862 1.5888 -0.1124 0.2173 -0.0537 230 TYR A CD1 1345 C CD2 . TYR A 217 ? 2.0818 1.6244 1.6065 -0.0818 0.1925 -0.0692 230 TYR A CD2 1346 C CE1 . TYR A 217 ? 1.9301 1.5441 1.5665 -0.1058 0.1996 -0.0741 230 TYR A CE1 1347 C CE2 . TYR A 217 ? 2.0426 1.5879 1.5892 -0.0759 0.1750 -0.0903 230 TYR A CE2 1348 C CZ . TYR A 217 ? 1.9287 1.5093 1.5306 -0.0879 0.1785 -0.0923 230 TYR A CZ 1349 O OH . TYR A 217 ? 1.8600 1.4454 1.4827 -0.0810 0.1607 -0.1110 230 TYR A OH 1350 N N . LEU A 218 ? 2.0331 1.4916 1.5277 -0.1368 0.2113 0.0290 231 LEU A N 1351 C CA . LEU A 218 ? 2.0547 1.4699 1.5047 -0.1318 0.2118 0.0510 231 LEU A CA 1352 C C . LEU A 218 ? 2.0957 1.5182 1.4944 -0.1008 0.2156 0.0409 231 LEU A C 1353 O O . LEU A 218 ? 2.0904 1.5264 1.4831 -0.0834 0.2072 0.0129 231 LEU A O 1354 C CB . LEU A 218 ? 2.0125 1.3542 1.4542 -0.1381 0.1854 0.0525 231 LEU A CB 1355 C CG . LEU A 218 ? 2.0322 1.3456 1.5111 -0.1722 0.1785 0.0686 231 LEU A CG 1356 C CD1 . LEU A 218 ? 2.0124 1.2507 1.4756 -0.1729 0.1502 0.0590 231 LEU A CD1 1357 C CD2 . LEU A 218 ? 2.0657 1.3806 1.5434 -0.1888 0.1993 0.1060 231 LEU A CD2 1358 N N . PRO A 219 ? 2.0720 1.4886 1.4339 -0.0946 0.2284 0.0651 232 PRO A N 1359 C CA . PRO A 219 ? 2.0649 1.4881 1.3744 -0.0663 0.2303 0.0595 232 PRO A CA 1360 C C . PRO A 219 ? 2.1066 1.4719 1.3842 -0.0475 0.2048 0.0511 232 PRO A C 1361 O O . PRO A 219 ? 1.9982 1.3060 1.2805 -0.0563 0.1903 0.0614 232 PRO A O 1362 C CB . PRO A 219 ? 1.9982 1.4328 1.2845 -0.0693 0.2510 0.0942 232 PRO A CB 1363 C CG . PRO A 219 ? 1.9516 1.4117 1.2830 -0.0977 0.2670 0.1101 232 PRO A CG 1364 C CD . PRO A 219 ? 1.9883 1.4132 1.3610 -0.1150 0.2472 0.0997 232 PRO A CD 1365 N N . VAL A 220 ? 2.2003 1.5815 1.4457 -0.0224 0.2000 0.0313 233 VAL A N 1366 C CA . VAL A 220 ? 2.3531 1.6887 1.5644 -0.0004 0.1779 0.0233 233 VAL A CA 1367 C C . VAL A 220 ? 2.4264 1.7670 1.5867 0.0198 0.1867 0.0430 233 VAL A C 1368 O O . VAL A 220 ? 2.4825 1.8727 1.6208 0.0321 0.1973 0.0350 233 VAL A O 1369 C CB . VAL A 220 ? 2.3138 1.6671 1.5259 0.0141 0.1639 -0.0125 233 VAL A CB 1370 C CG1 . VAL A 220 ? 2.2676 1.5665 1.4597 0.0303 0.1373 -0.0226 233 VAL A CG1 1371 C CG2 . VAL A 220 ? 2.2869 1.6680 1.5512 -0.0045 0.1658 -0.0302 233 VAL A CG2 1372 N N . TRP A 221 ? 2.4120 1.7019 1.5540 0.0224 0.1830 0.0697 234 TRP A N 1373 C CA . TRP A 221 ? 2.4031 1.6941 1.4969 0.0444 0.1894 0.0922 234 TRP A CA 1374 C C . TRP A 221 ? 2.5111 1.7600 1.5710 0.0726 0.1685 0.0838 234 TRP A C 1375 O O . TRP A 221 ? 2.6538 1.8986 1.6733 0.0946 0.1709 0.1033 234 TRP A O 1376 C CB . TRP A 221 ? 2.3658 1.6353 1.4595 0.0318 0.2033 0.1325 234 TRP A CB 1377 C CG . TRP A 221 ? 2.3098 1.6337 1.4309 0.0082 0.2261 0.1411 234 TRP A CG 1378 C CD1 . TRP A 221 ? 2.2312 1.6226 1.3605 0.0060 0.2383 0.1204 234 TRP A CD1 1379 C CD2 . TRP A 221 ? 2.3789 1.6949 1.5237 -0.0167 0.2403 0.1720 234 TRP A CD2 1380 N NE1 . TRP A 221 ? 2.2950 1.7227 1.4507 -0.0166 0.2600 0.1358 234 TRP A NE1 1381 C CE2 . TRP A 221 ? 2.3484 1.7338 1.5145 -0.0314 0.2614 0.1685 234 TRP A CE2 1382 C CE3 . TRP A 221 ? 2.4746 1.7307 1.6244 -0.0283 0.2379 0.2025 234 TRP A CE3 1383 C CZ2 . TRP A 221 ? 2.3835 1.7856 1.5762 -0.0565 0.2798 0.1953 234 TRP A CZ2 1384 C CZ3 . TRP A 221 ? 2.5441 1.8146 1.7208 -0.0554 0.2555 0.2298 234 TRP A CZ3 1385 C CH2 . TRP A 221 ? 2.5041 1.8499 1.7022 -0.0689 0.2762 0.2266 234 TRP A CH2 1386 N N . GLY A 222 ? 2.4392 1.6596 1.5164 0.0724 0.1483 0.0559 235 GLY A N 1387 C CA . GLY A 222 ? 2.4308 1.6103 1.4788 0.0986 0.1280 0.0453 235 GLY A CA 1388 C C . GLY A 222 ? 2.3417 1.4891 1.4166 0.0909 0.1069 0.0163 235 GLY A C 1389 O O . GLY A 222 ? 2.3219 1.4684 1.4389 0.0636 0.1072 0.0098 235 GLY A O 1390 N N . GLU A 223 ? 2.2494 1.3738 1.2997 0.1154 0.0886 -0.0001 236 GLU A N 1391 C CA . GLU A 223 ? 2.2836 1.3884 1.3549 0.1112 0.0680 -0.0302 236 GLU A CA 1392 C C . GLU A 223 ? 2.3832 1.4113 1.4622 0.1012 0.0553 -0.0269 236 GLU A C 1393 O O . GLU A 223 ? 2.3924 1.3685 1.4410 0.1168 0.0536 -0.0103 236 GLU A O 1394 C CB . GLU A 223 ? 2.4415 1.5642 1.4836 0.1411 0.0547 -0.0507 236 GLU A CB 1395 C CG . GLU A 223 ? 2.6060 1.8037 1.6421 0.1466 0.0668 -0.0569 236 GLU A CG 1396 C CD . GLU A 223 ? 2.7612 1.9789 1.7595 0.1775 0.0570 -0.0679 236 GLU A CD 1397 O OE1 . GLU A 223 ? 2.8364 2.0331 1.8327 0.1890 0.0372 -0.0879 236 GLU A OE1 1398 O OE2 . GLU A 223 ? 2.7393 1.9977 1.7099 0.1893 0.0691 -0.0561 236 GLU A OE2 1399 N N . THR A 224 ? 2.5125 1.5353 1.6336 0.0739 0.0475 -0.0420 237 THR A N 1400 C CA . THR A 224 ? 2.5743 1.5292 1.7080 0.0582 0.0326 -0.0464 237 THR A CA 1401 C C . THR A 224 ? 2.4998 1.4746 1.6764 0.0362 0.0189 -0.0736 237 THR A C 1402 O O . THR A 224 ? 2.4941 1.5323 1.6976 0.0286 0.0259 -0.0816 237 THR A O 1403 C CB . THR A 224 ? 2.2770 1.1927 1.4203 0.0351 0.0457 -0.0153 237 THR A CB 1404 O OG1 . THR A 224 ? 2.3854 1.2975 1.5757 -0.0022 0.0416 -0.0213 237 THR A OG1 1405 C CG2 . THR A 224 ? 2.1632 1.1263 1.3015 0.0359 0.0707 0.0122 237 THR A CG2 1406 N N . ASP A 225 ? 2.3967 1.3182 1.5792 0.0264 -0.0001 -0.0876 238 ASP A N 1407 C CA . ASP A 225 ? 2.3334 1.2760 1.5547 0.0065 -0.0151 -0.1124 238 ASP A CA 1408 C C . ASP A 225 ? 2.3211 1.3076 1.5942 -0.0277 -0.0034 -0.1034 238 ASP A C 1409 O O . ASP A 225 ? 2.3765 1.4060 1.6841 -0.0384 -0.0103 -0.1205 238 ASP A O 1410 C CB . ASP A 225 ? 2.4900 1.3657 1.7073 -0.0026 -0.0367 -0.1278 238 ASP A CB 1411 C CG . ASP A 225 ? 2.6726 1.5119 1.8433 0.0327 -0.0505 -0.1432 238 ASP A CG 1412 O OD1 . ASP A 225 ? 2.8345 1.6483 1.9664 0.0576 -0.0412 -0.1265 238 ASP A OD1 1413 O OD2 . ASP A 225 ? 2.6407 1.4794 1.8137 0.0360 -0.0705 -0.1708 238 ASP A OD2 1414 N N . GLU A 226 ? 2.2883 1.2658 1.5680 -0.0442 0.0146 -0.0752 239 GLU A N 1415 C CA . GLU A 226 ? 2.2210 1.2407 1.5501 -0.0766 0.0267 -0.0646 239 GLU A CA 1416 C C . GLU A 226 ? 2.2635 1.3525 1.5988 -0.0684 0.0500 -0.0545 239 GLU A C 1417 O O . GLU A 226 ? 2.2931 1.4224 1.6664 -0.0910 0.0645 -0.0433 239 GLU A O 1418 C CB . GLU A 226 ? 2.2664 1.2394 1.6068 -0.1059 0.0321 -0.0403 239 GLU A CB 1419 C CG . GLU A 226 ? 2.3889 1.2991 1.7343 -0.1241 0.0092 -0.0543 239 GLU A CG 1420 C CD . GLU A 226 ? 2.5163 1.3553 1.8103 -0.0969 -0.0035 -0.0629 239 GLU A CD 1421 O OE1 . GLU A 226 ? 2.5567 1.3782 1.8138 -0.0726 0.0091 -0.0442 239 GLU A OE1 1422 O OE2 . GLU A 226 ? 2.5225 1.3256 1.8129 -0.0990 -0.0256 -0.0878 239 GLU A OE2 1423 N N . THR A 227 ? 2.3490 1.4528 1.6462 -0.0364 0.0538 -0.0591 240 THR A N 1424 C CA . THR A 227 ? 2.4334 1.6015 1.7302 -0.0275 0.0751 -0.0540 240 THR A CA 1425 C C . THR A 227 ? 2.3472 1.5538 1.6362 -0.0052 0.0680 -0.0809 240 THR A C 1426 O O . THR A 227 ? 2.3975 1.5774 1.6615 0.0139 0.0492 -0.0965 240 THR A O 1427 C CB . THR A 227 ? 2.4629 1.6224 1.7190 -0.0131 0.0916 -0.0284 240 THR A CB 1428 O OG1 . THR A 227 ? 2.3413 1.4510 1.5530 0.0121 0.0775 -0.0302 240 THR A OG1 1429 C CG2 . THR A 227 ? 2.5455 1.6852 1.8172 -0.0385 0.1053 0.0023 240 THR A CG2 1430 N N . SER A 228 ? 2.1418 1.4099 1.4517 -0.0074 0.0837 -0.0859 241 SER A N 1431 C CA . SER A 228 ? 2.0706 1.3751 1.3814 0.0088 0.0777 -0.1113 241 SER A CA 1432 C C . SER A 228 ? 1.9210 1.2807 1.2241 0.0179 0.0993 -0.1134 241 SER A C 1433 O O . SER A 228 ? 1.7538 1.1417 1.0721 0.0050 0.1216 -0.0998 241 SER A O 1434 C CB . SER A 228 ? 2.2039 1.5230 1.5639 -0.0068 0.0661 -0.1272 241 SER A CB 1435 O OG . SER A 228 ? 2.1969 1.5714 1.5783 -0.0025 0.0769 -0.1400 241 SER A OG 1436 N N . PHE A 229 ? 1.9263 1.3021 1.2058 0.0393 0.0927 -0.1316 242 PHE A N 1437 C CA . PHE A 229 ? 1.9452 1.3705 1.2140 0.0474 0.1113 -0.1382 242 PHE A CA 1438 C C . PHE A 229 ? 1.9324 1.3992 1.2449 0.0380 0.1207 -0.1537 242 PHE A C 1439 O O . PHE A 229 ? 1.8931 1.3981 1.2058 0.0373 0.1424 -0.1559 242 PHE A O 1440 C CB . PHE A 229 ? 1.9114 1.3396 1.1347 0.0725 0.1020 -0.1495 242 PHE A CB 1441 C CG . PHE A 229 ? 1.9863 1.3813 1.1642 0.0863 0.0964 -0.1324 242 PHE A CG 1442 C CD1 . PHE A 229 ? 2.1385 1.5229 1.3070 0.0784 0.1110 -0.1065 242 PHE A CD1 1443 C CD2 . PHE A 229 ? 1.9171 1.2925 1.0631 0.1082 0.0772 -0.1405 242 PHE A CD2 1444 C CE1 . PHE A 229 ? 2.1844 1.5368 1.3126 0.0931 0.1067 -0.0881 242 PHE A CE1 1445 C CE2 . PHE A 229 ? 1.9413 1.2857 1.0470 0.1238 0.0731 -0.1235 242 PHE A CE2 1446 C CZ . PHE A 229 ? 2.1026 1.4342 1.1997 0.1167 0.0878 -0.0969 242 PHE A CZ 1447 N N . GLU A 230 ? 1.8823 1.3421 1.2314 0.0314 0.1050 -0.1641 243 GLU A N 1448 C CA . GLU A 230 ? 1.7590 1.2571 1.1506 0.0265 0.1120 -0.1777 243 GLU A CA 1449 C C . GLU A 230 ? 1.5918 1.1075 1.0321 0.0044 0.1262 -0.1656 243 GLU A C 1450 O O . GLU A 230 ? 1.5900 1.0819 1.0413 -0.0111 0.1211 -0.1500 243 GLU A O 1451 C CB . GLU A 230 ? 1.8594 1.3505 1.2643 0.0339 0.0875 -0.1950 243 GLU A CB 1452 C CG . GLU A 230 ? 2.0668 1.5464 1.4264 0.0563 0.0732 -0.2072 243 GLU A CG 1453 C CD . GLU A 230 ? 2.3104 1.7426 1.6377 0.0626 0.0531 -0.2012 243 GLU A CD 1454 O OE1 . GLU A 230 ? 2.4275 1.8315 1.7730 0.0480 0.0451 -0.1925 243 GLU A OE1 1455 O OE2 . GLU A 230 ? 2.3665 1.7898 1.6505 0.0820 0.0458 -0.2053 243 GLU A OE2 1456 N N . ALA A 231 ? 1.5160 1.0736 0.9846 0.0031 0.1455 -0.1721 244 ALA A N 1457 C CA . ALA A 231 ? 1.5725 1.1554 1.0916 -0.0151 0.1600 -0.1614 244 ALA A CA 1458 C C . ALA A 231 ? 1.6742 1.2816 1.2419 -0.0149 0.1538 -0.1735 244 ALA A C 1459 O O . ALA A 231 ? 1.6102 1.2351 1.1783 -0.0003 0.1569 -0.1902 244 ALA A O 1460 C CB . ALA A 231 ? 1.4542 1.0692 0.9697 -0.0173 0.1926 -0.1545 244 ALA A CB 1461 N N . GLY A 232 ? 1.7808 1.3901 1.3903 -0.0322 0.1446 -0.1636 245 GLY A N 1462 C CA . GLY A 232 ? 1.7543 1.3894 1.4117 -0.0329 0.1364 -0.1711 245 GLY A CA 1463 C C . GLY A 232 ? 1.7215 1.3422 1.4047 -0.0512 0.1124 -0.1639 245 GLY A C 1464 O O . GLY A 232 ? 1.6106 1.2033 1.2836 -0.0678 0.1070 -0.1507 245 GLY A O 1465 N N . ILE A 233 ? 1.6577 1.2962 1.3723 -0.0483 0.0970 -0.1730 246 ILE A N 1466 C CA . ILE A 233 ? 1.6551 1.2875 1.3963 -0.0664 0.0730 -0.1694 246 ILE A CA 1467 C C . ILE A 233 ? 1.5651 1.1752 1.2833 -0.0534 0.0451 -0.1867 246 ILE A C 1468 O O . ILE A 233 ? 1.6013 1.2070 1.2900 -0.0311 0.0462 -0.1992 246 ILE A O 1469 C CB . ILE A 233 ? 1.7123 1.3977 1.5189 -0.0770 0.0792 -0.1614 246 ILE A CB 1470 C CG1 . ILE A 233 ? 1.7676 1.4793 1.5936 -0.0590 0.0700 -0.1746 246 ILE A CG1 1471 C CG2 . ILE A 233 ? 1.7251 1.4432 1.5526 -0.0793 0.1130 -0.1486 246 ILE A CG2 1472 C CD1 . ILE A 233 ? 1.8239 1.5928 1.7158 -0.0642 0.0784 -0.1651 246 ILE A CD1 1473 N N . LYS A 234 ? 1.5231 1.1169 1.2503 -0.0684 0.0201 -0.1877 247 LYS A N 1474 C CA . LYS A 234 ? 1.5608 1.1468 1.2778 -0.0578 -0.0065 -0.2040 247 LYS A CA 1475 C C . LYS A 234 ? 1.6321 1.2531 1.4017 -0.0748 -0.0214 -0.2017 247 LYS A C 1476 O O . LYS A 234 ? 1.7549 1.3771 1.5490 -0.1008 -0.0238 -0.1908 247 LYS A O 1477 C CB . LYS A 234 ? 1.5891 1.1156 1.2536 -0.0556 -0.0259 -0.2121 247 LYS A CB 1478 C CG . LYS A 234 ? 1.6222 1.1405 1.2557 -0.0313 -0.0430 -0.2304 247 LYS A CG 1479 C CD . LYS A 234 ? 1.7970 1.2575 1.3779 -0.0258 -0.0602 -0.2382 247 LYS A CD 1480 C CE . LYS A 234 ? 1.8188 1.2728 1.3583 0.0036 -0.0674 -0.2522 247 LYS A CE 1481 N NZ . LYS A 234 ? 1.8396 1.2398 1.3227 0.0146 -0.0721 -0.2538 247 LYS A NZ 1482 N N . VAL A 235 ? 1.5547 1.2071 1.3426 -0.0613 -0.0314 -0.2105 248 VAL A N 1483 C CA . VAL A 235 ? 1.4332 1.1256 1.2707 -0.0757 -0.0466 -0.2071 248 VAL A CA 1484 C C . VAL A 235 ? 1.4514 1.1277 1.2690 -0.0735 -0.0791 -0.2229 248 VAL A C 1485 O O . VAL A 235 ? 1.3791 1.0275 1.1528 -0.0529 -0.0866 -0.2363 248 VAL A O 1486 C CB . VAL A 235 ? 1.2249 0.9762 1.1090 -0.0623 -0.0313 -0.2008 248 VAL A CB 1487 C CG1 . VAL A 235 ? 1.1701 0.9693 1.1100 -0.0795 -0.0439 -0.1918 248 VAL A CG1 1488 C CG2 . VAL A 235 ? 1.1715 0.9350 1.0663 -0.0586 0.0031 -0.1898 248 VAL A CG2 1489 N N . GLN A 236 ? 1.5088 1.2046 1.3573 -0.0954 -0.0986 -0.2215 249 GLN A N 1490 C CA . GLN A 236 ? 1.5863 1.2864 1.4271 -0.0918 -0.1278 -0.2361 249 GLN A CA 1491 C C . GLN A 236 ? 1.7380 1.5029 1.6382 -0.1048 -0.1373 -0.2278 249 GLN A C 1492 O O . GLN A 236 ? 1.9169 1.7036 1.8540 -0.1308 -0.1345 -0.2153 249 GLN A O 1493 C CB . GLN A 236 ? 1.6199 1.2635 1.4200 -0.1062 -0.1500 -0.2496 249 GLN A CB 1494 C CG . GLN A 236 ? 1.6972 1.3473 1.4852 -0.1000 -0.1792 -0.2670 249 GLN A CG 1495 C CD . GLN A 236 ? 1.8236 1.4165 1.5710 -0.1134 -0.2009 -0.2834 249 GLN A CD 1496 O OE1 . GLN A 236 ? 1.9546 1.4976 1.6819 -0.1274 -0.1944 -0.2808 249 GLN A OE1 1497 N NE2 . GLN A 236 ? 1.7820 1.3809 1.5166 -0.1089 -0.2264 -0.3003 249 GLN A NE2 1498 N N . ILE A 237 ? 1.6579 1.4570 1.5681 -0.0871 -0.1488 -0.2328 250 ILE A N 1499 C CA . ILE A 237 ? 1.5681 1.4329 1.5336 -0.0978 -0.1603 -0.2236 250 ILE A CA 1500 C C . ILE A 237 ? 1.5134 1.3773 1.4659 -0.1108 -0.1949 -0.2382 250 ILE A C 1501 O O . ILE A 237 ? 1.6072 1.4637 1.5312 -0.0918 -0.2090 -0.2514 250 ILE A O 1502 C CB . ILE A 237 ? 1.4395 1.3527 1.4342 -0.0705 -0.1489 -0.2152 250 ILE A CB 1503 C CG1 . ILE A 237 ? 1.3207 1.2372 1.3310 -0.0591 -0.1133 -0.2026 250 ILE A CG1 1504 C CG2 . ILE A 237 ? 1.4606 1.4445 1.5114 -0.0793 -0.1630 -0.2037 250 ILE A CG2 1505 C CD1 . ILE A 237 ? 1.1935 1.1442 1.2268 -0.0312 -0.0984 -0.1963 250 ILE A CD1 1506 N N . HIS A 238 ? 1.4180 1.2908 1.3906 -0.1440 -0.2085 -0.2365 251 HIS A N 1507 C CA . HIS A 238 ? 1.5700 1.4397 1.5272 -0.1594 -0.2415 -0.2535 251 HIS A CA 1508 C C . HIS A 238 ? 1.5571 1.4998 1.5697 -0.1826 -0.2570 -0.2438 251 HIS A C 1509 O O . HIS A 238 ? 1.5093 1.5000 1.5744 -0.1941 -0.2429 -0.2224 251 HIS A O 1510 C CB . HIS A 238 ? 1.7475 1.5430 1.6594 -0.1812 -0.2516 -0.2694 251 HIS A CB 1511 C CG . HIS A 238 ? 1.8670 1.6372 1.7889 -0.2013 -0.2313 -0.2557 251 HIS A CG 1512 N ND1 . HIS A 238 ? 1.9081 1.7315 1.8878 -0.2222 -0.2201 -0.2343 251 HIS A ND1 1513 C CD2 . HIS A 238 ? 1.9297 1.6299 1.8115 -0.2029 -0.2199 -0.2585 251 HIS A CD2 1514 C CE1 . HIS A 238 ? 1.9009 1.6882 1.8751 -0.2367 -0.2025 -0.2250 251 HIS A CE1 1515 N NE2 . HIS A 238 ? 1.9253 1.6373 1.8406 -0.2255 -0.2021 -0.2389 251 HIS A NE2 1516 N N . SER A 239 ? 1.5271 1.4816 1.5274 -0.1893 -0.2864 -0.2594 252 SER A N 1517 C CA . SER A 239 ? 1.5816 1.5969 1.6258 -0.2195 -0.3050 -0.2536 252 SER A CA 1518 C C . SER A 239 ? 1.6567 1.6349 1.7004 -0.2559 -0.3019 -0.2535 252 SER A C 1519 O O . SER A 239 ? 1.7120 1.6113 1.7089 -0.2555 -0.2950 -0.2650 252 SER A O 1520 C CB . SER A 239 ? 1.6566 1.6780 1.6757 -0.2249 -0.3382 -0.2756 252 SER A CB 1521 O OG . SER A 239 ? 1.7243 1.7520 1.7530 -0.2672 -0.3581 -0.2833 252 SER A OG 1522 N N . GLN A 240 ? 1.6203 1.6571 1.7173 -0.2866 -0.3056 -0.2380 253 GLN A N 1523 C CA . GLN A 240 ? 1.6148 1.6229 1.7158 -0.3265 -0.3051 -0.2365 253 GLN A CA 1524 C C . GLN A 240 ? 1.7890 1.7356 1.8399 -0.3488 -0.3318 -0.2663 253 GLN A C 1525 O O . GLN A 240 ? 1.9057 1.7825 1.9280 -0.3687 -0.3283 -0.2736 253 GLN A O 1526 C CB . GLN A 240 ? 1.4987 1.5915 1.6687 -0.3559 -0.3062 -0.2139 253 GLN A CB 1527 C CG . GLN A 240 ? 1.4199 1.5660 1.6408 -0.3366 -0.2751 -0.1832 253 GLN A CG 1528 C CD . GLN A 240 ? 1.3263 1.5224 1.5651 -0.2961 -0.2701 -0.1757 253 GLN A CD 1529 O OE1 . GLN A 240 ? 1.3248 1.5159 1.5363 -0.2812 -0.2896 -0.1922 253 GLN A OE1 1530 N NE2 . GLN A 240 ? 1.2848 1.5287 1.5695 -0.2777 -0.2433 -0.1503 253 GLN A NE2 1531 N N . ASP A 241 ? 1.9133 1.8848 1.9527 -0.3441 -0.3576 -0.2832 254 ASP A N 1532 C CA . ASP A 241 ? 2.1479 2.0646 2.1372 -0.3618 -0.3842 -0.3154 254 ASP A CA 1533 C C . ASP A 241 ? 2.2586 2.0715 2.1803 -0.3408 -0.3757 -0.3335 254 ASP A C 1534 O O . ASP A 241 ? 2.4186 2.1658 2.2955 -0.3566 -0.3911 -0.3586 254 ASP A O 1535 C CB . ASP A 241 ? 2.1479 2.1171 2.1352 -0.3521 -0.4101 -0.3288 254 ASP A CB 1536 C CG . ASP A 241 ? 2.1764 2.2480 2.2267 -0.3776 -0.4232 -0.3128 254 ASP A CG 1537 O OD1 . ASP A 241 ? 2.1777 2.2890 2.2789 -0.3949 -0.4087 -0.2874 254 ASP A OD1 1538 O OD2 . ASP A 241 ? 2.2020 2.3187 2.2509 -0.3794 -0.4481 -0.3246 254 ASP A OD2 1539 N N . GLU A 242 ? 2.1414 1.9415 2.0555 -0.3041 -0.3512 -0.3209 255 GLU A N 1540 C CA . GLU A 242 ? 2.1324 1.8467 1.9853 -0.2792 -0.3419 -0.3342 255 GLU A CA 1541 C C . GLU A 242 ? 2.0313 1.7049 1.8853 -0.2820 -0.3139 -0.3167 255 GLU A C 1542 O O . GLU A 242 ? 2.0388 1.7571 1.9318 -0.2727 -0.2921 -0.2929 255 GLU A O 1543 C CB . GLU A 242 ? 2.2107 1.9431 2.0470 -0.2339 -0.3378 -0.3359 255 GLU A CB 1544 C CG . GLU A 242 ? 2.3424 2.0000 2.1210 -0.2044 -0.3252 -0.3449 255 GLU A CG 1545 C CD . GLU A 242 ? 2.3392 2.0199 2.1027 -0.1633 -0.3230 -0.3467 255 GLU A CD 1546 O OE1 . GLU A 242 ? 2.2947 2.0410 2.0856 -0.1581 -0.3356 -0.3450 255 GLU A OE1 1547 O OE2 . GLU A 242 ? 2.3329 1.9683 2.0581 -0.1369 -0.3087 -0.3484 255 GLU A OE2 1548 N N . PRO A 243 ? 1.9116 1.5006 1.7230 -0.2943 -0.3136 -0.3277 256 PRO A N 1549 C CA . PRO A 243 ? 1.8368 1.3813 1.6419 -0.2960 -0.2878 -0.3110 256 PRO A CA 1550 C C . PRO A 243 ? 1.9409 1.4647 1.7150 -0.2520 -0.2683 -0.3074 256 PRO A C 1551 O O . PRO A 243 ? 2.0308 1.5460 1.7715 -0.2239 -0.2787 -0.3239 256 PRO A O 1552 C CB . PRO A 243 ? 1.7717 1.2282 1.5328 -0.3172 -0.2986 -0.3281 256 PRO A CB 1553 C CG . PRO A 243 ? 1.8392 1.2745 1.5591 -0.3003 -0.3213 -0.3569 256 PRO A CG 1554 C CD . PRO A 243 ? 1.9083 1.4346 1.6694 -0.3022 -0.3367 -0.3575 256 PRO A CD 1555 N N . PRO A 244 ? 1.8789 1.3990 1.6635 -0.2469 -0.2405 -0.2861 257 PRO A N 1556 C CA . PRO A 244 ? 1.7786 1.2793 1.5310 -0.2078 -0.2221 -0.2837 257 PRO A CA 1557 C C . PRO A 244 ? 1.8929 1.3071 1.5808 -0.1958 -0.2244 -0.2968 257 PRO A C 1558 O O . PRO A 244 ? 1.9675 1.3280 1.6421 -0.2203 -0.2264 -0.2967 257 PRO A O 1559 C CB . PRO A 244 ? 1.6333 1.1579 1.4178 -0.2121 -0.1925 -0.2577 257 PRO A CB 1560 C CG . PRO A 244 ? 1.6354 1.1563 1.4483 -0.2543 -0.1949 -0.2477 257 PRO A CG 1561 C CD . PRO A 244 ? 1.7690 1.3090 1.5960 -0.2767 -0.2249 -0.2633 257 PRO A CD 1562 N N . LEU A 245 ? 1.8444 1.2460 1.4939 -0.1592 -0.2242 -0.3071 258 LEU A N 1563 C CA . LEU A 245 ? 1.8998 1.2353 1.4963 -0.1396 -0.2135 -0.3080 258 LEU A CA 1564 C C . LEU A 245 ? 1.7695 1.1374 1.3696 -0.1128 -0.1896 -0.2939 258 LEU A C 1565 O O . LEU A 245 ? 1.6649 1.0460 1.2443 -0.0832 -0.1919 -0.3025 258 LEU A O 1566 C CB . LEU A 245 ? 1.4338 0.7327 0.9822 -0.1180 -0.2315 -0.3307 258 LEU A CB 1567 N N . ILE A 246 ? 1.7357 1.5962 1.4017 0.2990 -0.3179 -0.1330 259 ILE A N 1568 C CA . ILE A 246 ? 1.6265 1.5549 1.3492 0.3237 -0.2990 -0.1222 259 ILE A CA 1569 C C . ILE A 246 ? 1.6220 1.5577 1.3606 0.3604 -0.2689 -0.1513 259 ILE A C 1570 O O . ILE A 246 ? 1.4745 1.4544 1.2399 0.3810 -0.2447 -0.1578 259 ILE A O 1571 C CB . ILE A 246 ? 1.5143 1.4871 1.2921 0.3205 -0.3169 -0.0809 259 ILE A CB 1572 C CG1 . ILE A 246 ? 1.4675 1.4667 1.2483 0.2959 -0.3337 -0.0512 259 ILE A CG1 1573 C CG2 . ILE A 246 ? 1.5072 1.5367 1.3436 0.3533 -0.2941 -0.0781 259 ILE A CG2 1574 C CD1 . ILE A 246 ? 1.3651 1.4338 1.2042 0.3128 -0.3220 -0.0293 259 ILE A CD1 1575 N N . ASP A 247 ? 1.7081 1.5985 1.4280 0.3673 -0.2709 -0.1685 260 ASP A N 1576 C CA . ASP A 247 ? 1.7675 1.6526 1.4894 0.3997 -0.2441 -0.2004 260 ASP A CA 1577 C C . ASP A 247 ? 1.8455 1.7347 1.5386 0.4063 -0.2186 -0.2307 260 ASP A C 1578 O O . ASP A 247 ? 1.8617 1.7963 1.5842 0.4303 -0.1936 -0.2394 260 ASP A O 1579 C CB . ASP A 247 ? 1.9356 1.7537 1.6224 0.3991 -0.2534 -0.2170 260 ASP A CB 1580 C CG . ASP A 247 ? 2.0119 1.8322 1.7176 0.4363 -0.2309 -0.2393 260 ASP A CG 1581 O OD1 . ASP A 247 ? 1.9325 1.7952 1.6922 0.4539 -0.2288 -0.2210 260 ASP A OD1 1582 O OD2 . ASP A 247 ? 2.0814 1.8629 1.7485 0.4479 -0.2152 -0.2745 260 ASP A OD2 1583 N N . GLN A 248 ? 1.8595 1.7005 1.4932 0.3838 -0.2251 -0.2474 261 GLN A N 1584 C CA . GLN A 248 ? 1.7938 1.6306 1.3906 0.3853 -0.2032 -0.2781 261 GLN A CA 1585 C C . GLN A 248 ? 1.7185 1.5929 1.3165 0.3706 -0.2002 -0.2659 261 GLN A C 1586 O O . GLN A 248 ? 1.6863 1.5876 1.2846 0.3845 -0.1749 -0.2842 261 GLN A O 1587 C CB . GLN A 248 ? 1.8884 1.6544 1.4175 0.3659 -0.2113 -0.3025 261 GLN A CB 1588 C CG . GLN A 248 ? 1.9811 1.7011 1.4976 0.3832 -0.2081 -0.3234 261 GLN A CG 1589 C CD . GLN A 248 ? 1.9979 1.7300 1.5179 0.4185 -0.1746 -0.3584 261 GLN A CD 1590 O OE1 . GLN A 248 ? 2.0040 1.6990 1.4761 0.4197 -0.1612 -0.3930 261 GLN A OE1 1591 N NE2 . GLN A 248 ? 1.9632 1.7495 1.5399 0.4471 -0.1602 -0.3498 261 GLN A NE2 1592 N N . LEU A 249 ? 1.6360 1.5081 1.2291 0.3410 -0.2266 -0.2361 262 LEU A N 1593 C CA . LEU A 249 ? 1.6391 1.5347 1.2229 0.3235 -0.2272 -0.2250 262 LEU A CA 1594 C C . LEU A 249 ? 1.6991 1.6559 1.3401 0.3295 -0.2290 -0.1902 262 LEU A C 1595 O O . LEU A 249 ? 1.7433 1.7195 1.3804 0.3148 -0.2327 -0.1750 262 LEU A O 1596 C CB . LEU A 249 ? 1.6654 1.5184 1.1980 0.2847 -0.2533 -0.2175 262 LEU A CB 1597 C CG . LEU A 249 ? 1.7058 1.4934 1.1784 0.2770 -0.2517 -0.2528 262 LEU A CG 1598 C CD1 . LEU A 249 ? 1.6915 1.4444 1.1078 0.2381 -0.2701 -0.2512 262 LEU A CD1 1599 C CD2 . LEU A 249 ? 1.7342 1.5223 1.1951 0.3047 -0.2171 -0.2939 262 LEU A CD2 1600 N N . GLY A 250 ? 1.7008 1.6868 1.3941 0.3502 -0.2273 -0.1764 263 GLY A N 1601 C CA . GLY A 250 ? 1.7394 1.7815 1.4876 0.3551 -0.2303 -0.1423 263 GLY A CA 1602 C C . GLY A 250 ? 1.6720 1.7605 1.4483 0.3790 -0.1998 -0.1512 263 GLY A C 1603 O O . GLY A 250 ? 1.8081 1.8911 1.5703 0.3969 -0.1749 -0.1843 263 GLY A O 1604 N N . PHE A 251 ? 1.3585 1.4924 1.1742 0.3794 -0.2013 -0.1220 264 PHE A N 1605 C CA . PHE A 251 ? 1.2345 1.4130 1.0789 0.4002 -0.1732 -0.1267 264 PHE A CA 1606 C C . PHE A 251 ? 1.2432 1.4716 1.1524 0.4164 -0.1713 -0.1007 264 PHE A C 1607 O O . PHE A 251 ? 1.2814 1.5254 1.2147 0.4050 -0.1921 -0.0670 264 PHE A O 1608 C CB . PHE A 251 ? 1.1961 1.3796 1.0190 0.3856 -0.1712 -0.1202 264 PHE A CB 1609 C CG . PHE A 251 ? 1.0952 1.3045 0.9480 0.3740 -0.1908 -0.0788 264 PHE A CG 1610 C CD1 . PHE A 251 ? 1.0853 1.3430 0.9874 0.3904 -0.1781 -0.0608 264 PHE A CD1 1611 C CD2 . PHE A 251 ? 1.1984 1.3845 1.0285 0.3462 -0.2214 -0.0582 264 PHE A CD2 1612 C CE1 . PHE A 251 ? 1.2042 1.4871 1.1354 0.3820 -0.1953 -0.0226 264 PHE A CE1 1613 C CE2 . PHE A 251 ? 1.2002 1.4142 1.0594 0.3365 -0.2397 -0.0189 264 PHE A CE2 1614 C CZ . PHE A 251 ? 1.1592 1.4218 1.0700 0.3556 -0.2265 -0.0009 264 PHE A CZ 1615 N N . GLY A 252 ? 1.2486 1.5048 1.1857 0.4422 -0.1459 -0.1159 265 GLY A N 1616 C CA . GLY A 252 ? 1.2608 1.5656 1.2585 0.4583 -0.1410 -0.0947 265 GLY A CA 1617 C C . GLY A 252 ? 1.2432 1.5765 1.2700 0.4405 -0.1362 -0.0636 265 GLY A C 1618 O O . GLY A 252 ? 1.3354 1.6765 1.3474 0.4433 -0.1346 -0.0629 265 GLY A O 1619 N N . VAL A 253 ? 1.0993 1.4440 1.1670 0.4209 -0.1342 -0.0377 266 VAL A N 1620 C CA . VAL A 253 ? 1.0007 1.3655 1.1003 0.4020 -0.1222 -0.0128 266 VAL A CA 1621 C C . VAL A 253 ? 1.1305 1.5002 1.2647 0.3860 -0.1033 -0.0069 266 VAL A C 1622 O O . VAL A 253 ? 1.2308 1.5968 1.3839 0.3809 -0.1154 0.0024 266 VAL A O 1623 C CB . VAL A 253 ? 1.0313 1.4021 1.1471 0.3899 -0.1510 0.0201 266 VAL A CB 1624 C CG1 . VAL A 253 ? 0.9645 1.3518 1.1211 0.3705 -0.1379 0.0437 266 VAL A CG1 1625 C CG2 . VAL A 253 ? 1.2235 1.5886 1.3015 0.3993 -0.1715 0.0190 266 VAL A CG2 1626 N N . ALA A 254 ? 1.0513 1.4268 1.1911 0.3768 -0.0766 -0.0116 267 ALA A N 1627 C CA . ALA A 254 ? 0.9479 1.3241 1.1144 0.3602 -0.0614 -0.0074 267 ALA A CA 1628 C C . ALA A 254 ? 1.0128 1.3979 1.2165 0.3432 -0.0638 0.0171 267 ALA A C 1629 O O . ALA A 254 ? 1.1151 1.5072 1.3230 0.3423 -0.0695 0.0299 267 ALA A O 1630 C CB . ALA A 254 ? 0.9584 1.3303 1.1073 0.3558 -0.0362 -0.0257 267 ALA A CB 1631 N N . PRO A 255 ? 0.9376 1.3216 1.1683 0.3299 -0.0604 0.0228 268 PRO A N 1632 C CA . PRO A 255 ? 0.8960 1.2894 1.1570 0.3171 -0.0624 0.0402 268 PRO A CA 1633 C C . PRO A 255 ? 1.0574 1.4602 1.3044 0.3175 -0.0397 0.0345 268 PRO A C 1634 O O . PRO A 255 ? 1.2175 1.6165 1.4396 0.3208 -0.0236 0.0179 268 PRO A O 1635 C CB . PRO A 255 ? 0.8579 1.2553 1.1303 0.3152 -0.0627 0.0402 268 PRO A CB 1636 C CG . PRO A 255 ? 0.8936 1.2832 1.1405 0.3218 -0.0478 0.0197 268 PRO A CG 1637 C CD . PRO A 255 ? 0.8807 1.2568 1.1072 0.3298 -0.0523 0.0097 268 PRO A CD 1638 N N . GLY A 256 ? 1.1072 1.5215 1.3684 0.3138 -0.0398 0.0486 269 GLY A N 1639 C CA . GLY A 256 ? 1.1677 1.5895 1.4166 0.3140 -0.0197 0.0461 269 GLY A CA 1640 C C . GLY A 256 ? 1.1362 1.5502 1.3668 0.3180 -0.0135 0.0406 269 GLY A C 1641 O O . GLY A 256 ? 1.2176 1.6313 1.4285 0.3189 0.0036 0.0323 269 GLY A O 1642 N N . PHE A 257 ? 1.0751 1.4820 1.3118 0.3197 -0.0298 0.0461 270 PHE A N 1643 C CA . PHE A 257 ? 1.0046 1.4052 1.2261 0.3243 -0.0273 0.0434 270 PHE A CA 1644 C C . PHE A 257 ? 0.9961 1.4058 1.2278 0.3295 -0.0487 0.0636 270 PHE A C 1645 O O . PHE A 257 ? 1.1269 1.5388 1.3680 0.3294 -0.0696 0.0726 270 PHE A O 1646 C CB . PHE A 257 ? 1.0654 1.4617 1.2523 0.3366 -0.0248 0.0249 270 PHE A CB 1647 C CG . PHE A 257 ? 1.0392 1.4261 1.2077 0.3313 -0.0041 0.0053 270 PHE A CG 1648 C CD1 . PHE A 257 ? 1.0856 1.4691 1.2357 0.3307 0.0107 -0.0014 270 PHE A CD1 1649 C CD2 . PHE A 257 ? 1.0400 1.4236 1.2064 0.3283 -0.0013 -0.0048 270 PHE A CD2 1650 C CE1 . PHE A 257 ? 1.1599 1.5404 1.2872 0.3279 0.0255 -0.0166 270 PHE A CE1 1651 C CE2 . PHE A 257 ? 1.1907 1.5737 1.3327 0.3276 0.0137 -0.0199 270 PHE A CE2 1652 C CZ . PHE A 257 ? 1.2740 1.6559 1.3968 0.3266 0.0260 -0.0254 270 PHE A CZ 1653 N N . GLN A 258 ? 0.9142 1.3280 1.1428 0.3332 -0.0458 0.0723 271 GLN A N 1654 C CA . GLN A 258 ? 0.9864 1.4071 1.2128 0.3399 -0.0676 0.0898 271 GLN A CA 1655 C C . GLN A 258 ? 1.1179 1.5363 1.3053 0.3554 -0.0673 0.0764 271 GLN A C 1656 O O . GLN A 258 ? 1.1600 1.5742 1.3238 0.3620 -0.0462 0.0581 271 GLN A O 1657 C CB . GLN A 258 ? 0.8936 1.3194 1.1314 0.3391 -0.0671 0.1066 271 GLN A CB 1658 C CG . GLN A 258 ? 0.9685 1.3998 1.2026 0.3426 -0.0926 0.1273 271 GLN A CG 1659 C CD . GLN A 258 ? 1.3123 1.7489 1.5640 0.3399 -0.0949 0.1466 271 GLN A CD 1660 O OE1 . GLN A 258 ? 1.4538 1.8895 1.7129 0.3404 -0.0742 0.1419 271 GLN A OE1 1661 N NE2 . GLN A 258 ? 1.4170 1.8579 1.6725 0.3364 -0.1211 0.1683 271 GLN A NE2 1662 N N . THR A 259 ? 1.0989 1.5182 1.2759 0.3601 -0.0926 0.0838 272 THR A N 1663 C CA . THR A 259 ? 0.9916 1.4071 1.1268 0.3766 -0.0968 0.0678 272 THR A CA 1664 C C . THR A 259 ? 1.0495 1.4667 1.1702 0.3781 -0.1239 0.0880 272 THR A C 1665 O O . THR A 259 ? 1.1894 1.6055 1.3182 0.3675 -0.1517 0.1062 272 THR A O 1666 C CB . THR A 259 ? 0.8529 1.2610 0.9749 0.3815 -0.1077 0.0525 272 THR A CB 1667 O OG1 . THR A 259 ? 0.7803 1.1847 0.9125 0.3777 -0.0847 0.0348 272 THR A OG1 1668 C CG2 . THR A 259 ? 0.8457 1.2468 0.9201 0.4005 -0.1160 0.0325 272 THR A CG2 1669 N N . PHE A 260 ? 0.9449 1.3628 1.0405 0.3886 -0.1171 0.0854 273 PHE A N 1670 C CA . PHE A 260 ? 0.9008 1.3171 0.9741 0.3875 -0.1434 0.1053 273 PHE A CA 1671 C C . PHE A 260 ? 1.0352 1.4404 1.0576 0.3998 -0.1578 0.0830 273 PHE A C 1672 O O . PHE A 260 ? 0.9559 1.3538 0.9589 0.4113 -0.1353 0.0498 273 PHE A O 1673 C CB . PHE A 260 ? 0.8526 1.2723 0.9210 0.3935 -0.1291 0.1135 273 PHE A CB 1674 C CG . PHE A 260 ? 0.7475 1.1734 0.8588 0.3857 -0.1095 0.1247 273 PHE A CG 1675 C CD1 . PHE A 260 ? 0.8321 1.2618 0.9670 0.3754 -0.1222 0.1543 273 PHE A CD1 1676 C CD2 . PHE A 260 ? 0.8152 1.2407 0.9393 0.3865 -0.0804 0.1044 273 PHE A CD2 1677 C CE1 . PHE A 260 ? 1.0067 1.4401 1.1763 0.3704 -0.1056 0.1600 273 PHE A CE1 1678 C CE2 . PHE A 260 ? 0.9373 1.3644 1.0932 0.3773 -0.0658 0.1125 273 PHE A CE2 1679 C CZ . PHE A 260 ? 1.0223 1.4538 1.2007 0.3714 -0.0778 0.1388 273 PHE A CZ 1680 N N . VAL A 261 ? 1.1664 1.5539 1.1640 0.3804 -0.1895 0.0960 274 VAL A N 1681 C CA . VAL A 261 ? 1.1320 1.4756 1.0708 0.3610 -0.1960 0.0692 274 VAL A CA 1682 C C . VAL A 261 ? 1.0737 1.4019 0.9828 0.3378 -0.2179 0.0903 274 VAL A C 1683 O O . VAL A 261 ? 1.1410 1.4813 1.0680 0.3267 -0.2450 0.1229 274 VAL A O 1684 C CB . VAL A 261 ? 1.0598 1.3888 0.9956 0.3521 -0.2153 0.0640 274 VAL A CB 1685 C CG1 . VAL A 261 ? 1.0722 1.3553 0.9468 0.3242 -0.2333 0.0511 274 VAL A CG1 1686 C CG2 . VAL A 261 ? 0.7360 1.0698 0.6873 0.3730 -0.1929 0.0347 274 VAL A CG2 1687 N N . SER A 262 ? 1.0042 1.3087 0.8687 0.3299 -0.2063 0.0730 275 SER A N 1688 C CA . SER A 262 ? 1.0898 1.3854 0.9305 0.3108 -0.2233 0.0962 275 SER A CA 1689 C C . SER A 262 ? 1.1659 1.4183 0.9412 0.2851 -0.2316 0.0718 275 SER A C 1690 O O . SER A 262 ? 1.0836 1.3161 0.8272 0.2885 -0.2092 0.0347 275 SER A O 1691 C CB . SER A 262 ? 1.1221 1.4291 0.9691 0.3243 -0.2010 0.1006 275 SER A CB 1692 O OG . SER A 262 ? 1.2253 1.5151 1.0369 0.3044 -0.2145 0.1153 275 SER A OG 1693 N N . CYS A 263 ? 1.1596 1.3998 0.9153 0.2589 -0.2634 0.0931 276 CYS A N 1694 C CA . CYS A 263 ? 1.0793 1.2787 0.7788 0.2326 -0.2768 0.0715 276 CYS A CA 1695 C C . CYS A 263 ? 1.1868 1.3657 0.8379 0.2071 -0.2875 0.0772 276 CYS A C 1696 O O . CYS A 263 ? 1.2439 1.4420 0.9098 0.2054 -0.2956 0.1091 276 CYS A O 1697 C CB . CYS A 263 ? 1.0601 1.2579 0.7701 0.2183 -0.3066 0.0887 276 CYS A CB 1698 S SG . CYS A 263 ? 1.1315 1.3501 0.8957 0.2444 -0.2988 0.0832 276 CYS A SG 1699 N N . GLN A 264 ? 1.3572 1.4968 0.9496 0.1878 -0.2863 0.0455 277 GLN A N 1700 C CA . GLN A 264 ? 1.4623 1.5789 1.0017 0.1582 -0.2992 0.0488 277 GLN A CA 1701 C C . GLN A 264 ? 1.5248 1.6059 1.0184 0.1286 -0.3205 0.0360 277 GLN A C 1702 O O . GLN A 264 ? 1.6103 1.6646 1.0780 0.1307 -0.3073 -0.0021 277 GLN A O 1703 C CB . GLN A 264 ? 1.5155 1.6186 1.0205 0.1626 -0.2707 0.0188 277 GLN A CB 1704 C CG . GLN A 264 ? 1.7970 1.9074 1.2921 0.1533 -0.2749 0.0439 277 GLN A CG 1705 C CD . GLN A 264 ? 2.2097 2.3187 1.6930 0.1242 -0.3120 0.0807 277 GLN A CD 1706 O OE1 . GLN A 264 ? 2.2879 2.4273 1.8156 0.1305 -0.3281 0.1218 277 GLN A OE1 1707 N NE2 . GLN A 264 ? 2.3231 2.3988 1.7460 0.0916 -0.3253 0.0660 277 GLN A NE2 1708 N N . GLU A 265 ? 1.5370 1.6176 1.0203 0.1011 -0.3530 0.0675 278 GLU A N 1709 C CA . GLU A 265 ? 1.6950 1.7410 1.1363 0.0721 -0.3736 0.0562 278 GLU A CA 1710 C C . GLU A 265 ? 1.8341 1.8400 1.2036 0.0475 -0.3685 0.0254 278 GLU A C 1711 O O . GLU A 265 ? 1.8726 1.8792 1.2162 0.0288 -0.3761 0.0395 278 GLU A O 1712 C CB . GLU A 265 ? 1.7879 1.8483 1.2402 0.0478 -0.4110 0.0997 278 GLU A CB 1713 C CG . GLU A 265 ? 1.9286 1.9503 1.3325 0.0138 -0.4330 0.0884 278 GLU A CG 1714 C CD . GLU A 265 ? 2.0206 2.0616 1.4411 -0.0094 -0.4697 0.1320 278 GLU A CD 1715 O OE1 . GLU A 265 ? 2.0857 2.1380 1.5414 -0.0012 -0.4782 0.1419 278 GLU A OE1 1716 O OE2 . GLU A 265 ? 1.9946 2.0418 1.3932 -0.0363 -0.4903 0.1575 278 GLU A OE2 1717 N N . GLN A 266 ? 1.8942 1.8654 1.2316 0.0478 -0.3556 -0.0164 279 GLN A N 1718 C CA . GLN A 266 ? 1.9641 1.8962 1.2323 0.0255 -0.3486 -0.0503 279 GLN A CA 1719 C C . GLN A 266 ? 1.8844 1.7773 1.1127 -0.0015 -0.3681 -0.0620 279 GLN A C 1720 O O . GLN A 266 ? 1.8898 1.7669 1.1268 0.0119 -0.3622 -0.0818 279 GLN A O 1721 C CB . GLN A 266 ? 2.1034 2.0284 1.3652 0.0515 -0.3116 -0.0942 279 GLN A CB 1722 C CG . GLN A 266 ? 2.3637 2.2491 1.5553 0.0315 -0.3012 -0.1345 279 GLN A CG 1723 C CD . GLN A 266 ? 2.5076 2.3955 1.6977 0.0587 -0.2638 -0.1745 279 GLN A CD 1724 O OE1 . GLN A 266 ? 2.5508 2.4126 1.7163 0.0642 -0.2500 -0.2127 279 GLN A OE1 1725 N NE2 . GLN A 266 ? 2.4988 2.4186 1.7155 0.0763 -0.2468 -0.1654 279 GLN A NE2 1726 N N . ARG A 267 ? 1.8690 1.7450 1.0518 -0.0403 -0.3915 -0.0493 280 ARG A N 1727 C CA . ARG A 267 ? 2.0476 1.8867 1.1905 -0.0714 -0.4139 -0.0547 280 ARG A CA 1728 C C . ARG A 267 ? 2.1696 1.9651 1.2359 -0.0985 -0.4074 -0.0908 280 ARG A C 1729 O O . ARG A 267 ? 2.2262 2.0260 1.2627 -0.1203 -0.4129 -0.0813 280 ARG A O 1730 C CB . ARG A 267 ? 2.2150 2.0756 1.3710 -0.0980 -0.4506 -0.0047 280 ARG A CB 1731 C CG . ARG A 267 ? 2.4391 2.2661 1.5582 -0.1330 -0.4772 -0.0035 280 ARG A CG 1732 C CD . ARG A 267 ? 2.5017 2.3623 1.6611 -0.1441 -0.5092 0.0470 280 ARG A CD 1733 N NE . ARG A 267 ? 2.4729 2.3720 1.6443 -0.1576 -0.5261 0.0886 280 ARG A NE 1734 C CZ . ARG A 267 ? 2.3071 2.2585 1.5429 -0.1360 -0.5309 0.1277 280 ARG A CZ 1735 N NH1 . ARG A 267 ? 2.2590 2.2315 1.5523 -0.1016 -0.5199 0.1299 280 ARG A NH1 1736 N NH2 . ARG A 267 ? 2.1337 2.1163 1.3763 -0.1485 -0.5466 0.1650 280 ARG A NH2 1737 N N . LEU A 268 ? 2.1497 1.9030 1.1834 -0.0972 -0.3956 -0.1319 281 LEU A N 1738 C CA . LEU A 268 ? 2.1442 1.8571 1.1067 -0.1174 -0.3831 -0.1727 281 LEU A CA 1739 C C . LEU A 268 ? 2.1434 1.8017 1.0510 -0.1446 -0.3941 -0.1965 281 LEU A C 1740 O O . LEU A 268 ? 2.0808 1.7223 1.0049 -0.1341 -0.3983 -0.2004 281 LEU A O 1741 C CB . LEU A 268 ? 2.0755 1.7914 1.0428 -0.0834 -0.3445 -0.2121 281 LEU A CB 1742 C CG . LEU A 268 ? 1.9140 1.6469 0.9401 -0.0399 -0.3278 -0.2179 281 LEU A CG 1743 C CD1 . LEU A 268 ? 1.9008 1.5903 0.9061 -0.0366 -0.3249 -0.2487 281 LEU A CD1 1744 C CD2 . LEU A 268 ? 1.8971 1.6552 0.9409 -0.0089 -0.2939 -0.2390 281 LEU A CD2 1745 N N . ILE A 269 ? 2.2221 1.8510 1.0622 -0.1794 -0.3974 -0.2141 282 ILE A N 1746 C CA . ILE A 269 ? 2.3150 1.8937 1.0972 -0.2170 -0.4158 -0.2259 282 ILE A CA 1747 C C . ILE A 269 ? 2.4332 1.9696 1.1624 -0.2227 -0.3905 -0.2784 282 ILE A C 1748 O O . ILE A 269 ? 2.5632 2.1174 1.2930 -0.2123 -0.3634 -0.2984 282 ILE A O 1749 C CB . ILE A 269 ? 2.2134 1.8007 0.9695 -0.2637 -0.4496 -0.1881 282 ILE A CB 1750 C CG1 . ILE A 269 ? 2.2759 1.9132 1.0980 -0.2555 -0.4719 -0.1333 282 ILE A CG1 1751 C CG2 . ILE A 269 ? 2.1692 1.7157 0.8868 -0.2992 -0.4627 -0.1959 282 ILE A CG2 1752 C CD1 . ILE A 269 ? 2.3154 1.9546 1.1870 -0.2291 -0.4737 -0.1273 282 ILE A CD1 1753 N N . TYR A 270 ? 2.3725 1.8650 1.0772 -0.2356 -0.3939 -0.2966 283 TYR A N 1754 C CA . TYR A 270 ? 2.4427 1.9062 1.1225 -0.2347 -0.3645 -0.3422 283 TYR A CA 1755 C C . TYR A 270 ? 2.7263 2.1527 1.3654 -0.2765 -0.3798 -0.3423 283 TYR A C 1756 O O . TYR A 270 ? 2.8392 2.2583 1.4712 -0.3041 -0.4127 -0.3090 283 TYR A O 1757 C CB . TYR A 270 ? 2.3779 1.8189 1.0723 -0.1958 -0.3431 -0.3750 283 TYR A CB 1758 C CG . TYR A 270 ? 2.3252 1.8013 1.0603 -0.1518 -0.3227 -0.3804 283 TYR A CG 1759 C CD1 . TYR A 270 ? 2.3177 1.8365 1.0674 -0.1440 -0.3027 -0.3828 283 TYR A CD1 1760 C CD2 . TYR A 270 ? 2.3364 1.8026 1.0961 -0.1171 -0.3230 -0.3833 283 TYR A CD2 1761 C CE1 . TYR A 270 ? 2.2111 1.7625 0.9988 -0.1046 -0.2822 -0.3879 283 TYR A CE1 1762 C CE2 . TYR A 270 ? 2.2513 1.7599 1.0640 -0.0744 -0.2997 -0.3857 283 TYR A CE2 1763 C CZ . TYR A 270 ? 2.1740 1.7170 0.9877 -0.0696 -0.2819 -0.3907 283 TYR A CZ 1764 O OH . TYR A 270 ? 2.0580 1.6424 0.9223 -0.0291 -0.2585 -0.3934 283 TYR A OH 1765 N N . LEU A 271 ? 2.8000 2.2062 1.4154 -0.2806 -0.3557 -0.3788 284 LEU A N 1766 C CA . LEU A 271 ? 2.8219 2.1920 1.3954 -0.3199 -0.3668 -0.3817 284 LEU A CA 1767 C C . LEU A 271 ? 2.8702 2.1897 1.4257 -0.3101 -0.3523 -0.4185 284 LEU A C 1768 O O . LEU A 271 ? 2.8452 2.1649 1.4186 -0.2734 -0.3229 -0.4522 284 LEU A O 1769 C CB . LEU A 271 ? 2.7611 2.1473 1.3164 -0.3380 -0.3538 -0.3911 284 LEU A CB 1770 C CG . LEU A 271 ? 2.6947 2.1279 1.2639 -0.3476 -0.3630 -0.3593 284 LEU A CG 1771 C CD1 . LEU A 271 ? 2.6741 2.1217 1.2313 -0.3512 -0.3404 -0.3803 284 LEU A CD1 1772 C CD2 . LEU A 271 ? 2.7427 2.1773 1.2998 -0.3879 -0.4005 -0.3139 284 LEU A CD2 1773 N N . PRO A 272 ? 2.9562 2.2336 1.4777 -0.3433 -0.3723 -0.4112 285 PRO A N 1774 C CA . PRO A 272 ? 3.0966 2.3216 1.5954 -0.3369 -0.3569 -0.4477 285 PRO A CA 1775 C C . PRO A 272 ? 3.2548 2.4813 1.7382 -0.3358 -0.3283 -0.4829 285 PRO A C 1776 O O . PRO A 272 ? 3.3104 2.5706 1.7919 -0.3501 -0.3272 -0.4737 285 PRO A O 1777 C CB . PRO A 272 ? 3.1531 2.3381 1.6163 -0.3803 -0.3878 -0.4255 285 PRO A CB 1778 C CG . PRO A 272 ? 3.1173 2.3396 1.5783 -0.4155 -0.4119 -0.3851 285 PRO A CG 1779 C CD . PRO A 272 ? 3.0013 2.2795 1.5056 -0.3879 -0.4084 -0.3694 285 PRO A CD 1780 N N . PRO A 273 ? 3.3270 2.5190 1.8015 -0.3175 -0.3057 -0.5220 286 PRO A N 1781 C CA . PRO A 273 ? 3.3468 2.5408 1.8065 -0.3178 -0.2814 -0.5547 286 PRO A CA 1782 C C . PRO A 273 ? 3.3610 2.5327 1.7732 -0.3679 -0.2986 -0.5428 286 PRO A C 1783 O O . PRO A 273 ? 3.3074 2.4543 1.6976 -0.4005 -0.3271 -0.5144 286 PRO A O 1784 C CB . PRO A 273 ? 3.3923 2.5478 1.8521 -0.2906 -0.2602 -0.5928 286 PRO A CB 1785 C CG . PRO A 273 ? 3.4154 2.5289 1.8684 -0.2950 -0.2815 -0.5754 286 PRO A CG 1786 C CD . PRO A 273 ? 3.3501 2.5016 1.8301 -0.2940 -0.3016 -0.5372 286 PRO A CD 1787 N N . PRO A 274 ? 3.4138 2.5957 1.8110 -0.3746 -0.2821 -0.5633 287 PRO A N 1788 C CA . PRO A 274 ? 3.3841 2.5973 1.8071 -0.3377 -0.2497 -0.5975 287 PRO A CA 1789 C C . PRO A 274 ? 3.3076 2.5809 1.7744 -0.3133 -0.2435 -0.5840 287 PRO A C 1790 O O . PRO A 274 ? 3.2736 2.5750 1.7763 -0.2726 -0.2186 -0.6080 287 PRO A O 1791 C CB . PRO A 274 ? 3.4025 2.6112 1.7901 -0.3654 -0.2452 -0.6086 287 PRO A CB 1792 C CG . PRO A 274 ? 3.5018 2.6590 1.8415 -0.4100 -0.2677 -0.5948 287 PRO A CG 1793 C CD . PRO A 274 ? 3.4748 2.6343 1.8249 -0.4223 -0.2955 -0.5548 287 PRO A CD 1794 N N . TRP A 275 ? 3.2599 2.5540 1.7244 -0.3383 -0.2659 -0.5453 288 TRP A N 1795 C CA . TRP A 275 ? 3.1133 2.4614 1.6145 -0.3192 -0.2613 -0.5299 288 TRP A CA 1796 C C . TRP A 275 ? 3.0516 2.4176 1.5973 -0.2732 -0.2456 -0.5416 288 TRP A C 1797 O O . TRP A 275 ? 2.9427 2.3412 1.5178 -0.2401 -0.2190 -0.5660 288 TRP A O 1798 C CB . TRP A 275 ? 3.0537 2.4149 1.5498 -0.3499 -0.2922 -0.4821 288 TRP A CB 1799 C CG . TRP A 275 ? 3.1050 2.4651 1.5664 -0.3937 -0.3057 -0.4652 288 TRP A CG 1800 C CD1 . TRP A 275 ? 3.1316 2.5186 1.5896 -0.3988 -0.2940 -0.4695 288 TRP A CD1 1801 C CD2 . TRP A 275 ? 3.0976 2.4304 1.5244 -0.4393 -0.3340 -0.4391 288 TRP A CD2 1802 N NE1 . TRP A 275 ? 3.1490 2.5255 1.5714 -0.4447 -0.3126 -0.4484 288 TRP A NE1 1803 C CE2 . TRP A 275 ? 3.1906 2.5360 1.5944 -0.4703 -0.3371 -0.4293 288 TRP A CE2 1804 C CE3 . TRP A 275 ? 3.0161 2.3161 1.4295 -0.4578 -0.3574 -0.4223 288 TRP A CE3 1805 C CZ2 . TRP A 275 ? 3.2687 2.5970 1.6381 -0.5186 -0.3617 -0.4034 288 TRP A CZ2 1806 C CZ3 . TRP A 275 ? 3.0097 2.2942 1.3900 -0.5056 -0.3822 -0.3964 288 TRP A CZ3 1807 C CH2 . TRP A 275 ? 3.1733 2.4728 1.5324 -0.5355 -0.3838 -0.3872 288 TRP A CH2 1808 N N . GLY A 276 ? 3.1854 2.5325 1.7369 -0.2724 -0.2636 -0.5219 289 GLY A N 1809 C CA . GLY A 276 ? 3.2103 2.5719 1.8023 -0.2325 -0.2529 -0.5261 289 GLY A CA 1810 C C . GLY A 276 ? 3.2620 2.5817 1.8550 -0.2137 -0.2467 -0.5467 289 GLY A C 1811 O O . GLY A 276 ? 3.2755 2.5481 1.8346 -0.2318 -0.2509 -0.5598 289 GLY A O 1812 N N . ASP A 277 ? 3.2712 2.6064 1.9026 -0.1775 -0.2364 -0.5482 290 ASP A N 1813 C CA . ASP A 277 ? 3.3016 2.5986 1.9397 -0.1545 -0.2297 -0.5647 290 ASP A CA 1814 C C . ASP A 277 ? 3.1777 2.4399 1.8074 -0.1618 -0.2618 -0.5346 290 ASP A C 1815 O O . ASP A 277 ? 3.1262 2.3468 1.7538 -0.1474 -0.2617 -0.5450 290 ASP A O 1816 C CB . ASP A 277 ? 3.3109 2.6461 1.9999 -0.1085 -0.1963 -0.5856 290 ASP A CB 1817 C CG . ASP A 277 ? 3.3867 2.7687 2.0932 -0.1005 -0.1663 -0.6128 290 ASP A CG 1818 O OD1 . ASP A 277 ? 3.4687 2.8360 2.1447 -0.1205 -0.1659 -0.6286 290 ASP A OD1 1819 O OD2 . ASP A 277 ? 3.3508 2.7851 2.1019 -0.0749 -0.1438 -0.6174 290 ASP A OD2 1820 N N . CYS A 278 ? 3.0865 2.3666 1.7120 -0.1848 -0.2906 -0.4965 291 CYS A N 1821 C CA . CYS A 278 ? 2.9642 2.2284 1.5937 -0.1875 -0.3225 -0.4646 291 CYS A CA 1822 C C . CYS A 278 ? 3.0772 2.2814 1.6697 -0.2153 -0.3439 -0.4620 291 CYS A C 1823 O O . CYS A 278 ? 3.1681 2.3437 1.7274 -0.2376 -0.3367 -0.4807 291 CYS A O 1824 C CB . CYS A 278 ? 2.8152 2.1204 1.4531 -0.2081 -0.3494 -0.4217 291 CYS A CB 1825 S SG . CYS A 278 ? 3.3198 2.6135 1.9166 -0.2693 -0.3803 -0.3940 291 CYS A SG 1826 N N . LYS A 279 ? 3.1376 2.3225 1.7373 -0.2116 -0.3692 -0.4404 292 LYS A N 1827 C CA . LYS A 279 ? 3.3029 2.4383 1.8694 -0.2458 -0.3971 -0.4271 292 LYS A CA 1828 C C . LYS A 279 ? 3.3920 2.5530 1.9691 -0.2719 -0.4387 -0.3766 292 LYS A C 1829 O O . LYS A 279 ? 3.2593 2.4451 1.8757 -0.2474 -0.4500 -0.3566 292 LYS A O 1830 C CB . LYS A 279 ? 3.3011 2.3832 1.8659 -0.2198 -0.3898 -0.4493 292 LYS A CB 1831 N N . ALA A 280 ? 3.6332 2.7964 2.1851 -0.3196 -0.4599 -0.3533 293 ALA A N 1832 C CA . ALA A 280 ? 3.7662 2.9608 2.3353 -0.3451 -0.4988 -0.3026 293 ALA A CA 1833 C C . ALA A 280 ? 3.9865 3.1308 2.5325 -0.3684 -0.5204 -0.2959 293 ALA A C 1834 O O . ALA A 280 ? 4.0822 3.1912 2.5872 -0.4046 -0.5236 -0.3014 293 ALA A O 1835 C CB . ALA A 280 ? 3.7565 2.9888 2.3176 -0.3827 -0.5096 -0.2767 293 ALA A CB 1836 N N . THR A 281 ? 4.0598 3.2028 2.6348 -0.3469 -0.5346 -0.2829 294 THR A N 1837 C CA . THR A 281 ? 4.1900 3.2834 2.7487 -0.3623 -0.5519 -0.2788 294 THR A CA 1838 C C . THR A 281 ? 4.1795 3.3248 2.8051 -0.3583 -0.5761 -0.2282 294 THR A C 1839 O O . THR A 281 ? 4.1257 3.3160 2.8210 -0.3140 -0.5638 -0.2178 294 THR A O 1840 C CB . THR A 281 ? 4.2183 3.2532 2.7665 -0.3254 -0.5244 -0.3237 294 THR A CB 1841 N N . THR A 282 ? 4.2364 3.3770 2.8395 -0.4060 -0.6104 -0.1969 295 THR A N 1842 C CA . THR A 282 ? 4.2004 3.3780 2.8569 -0.4073 -0.6350 -0.1524 295 THR A CA 1843 C C . THR A 282 ? 4.2258 3.3337 2.8538 -0.4155 -0.6418 -0.1659 295 THR A C 1844 O O . THR A 282 ? 4.2093 3.3346 2.8722 -0.4196 -0.6622 -0.1340 295 THR A O 1845 C CB . THR A 282 ? 4.2165 3.4429 2.8743 -0.4536 -0.6703 -0.1037 295 THR A CB 1846 O OG1 . THR A 282 ? 4.3321 3.5160 2.9243 -0.5012 -0.6750 -0.1139 295 THR A OG1 1847 C CG2 . THR A 282 ? 4.1059 3.4095 2.8099 -0.4361 -0.6642 -0.0824 295 THR A CG2 1848 N N . GLY A 283 ? 4.2385 3.2666 2.8018 -0.4178 -0.6240 -0.2140 296 GLY A N 1849 C CA . GLY A 283 ? 4.2317 3.1798 2.7543 -0.4287 -0.6288 -0.2321 296 GLY A CA 1850 C C . GLY A 283 ? 4.1626 3.1158 2.7453 -0.3819 -0.6194 -0.2287 296 GLY A C 1851 O O . GLY A 283 ? 4.2092 3.1233 2.7821 -0.3952 -0.6354 -0.2199 296 GLY A O 1852 N N . ASP A 284 ? 4.0141 3.0151 2.6567 -0.3291 -0.5935 -0.2357 297 ASP A N 1853 C CA . ASP A 284 ? 3.8501 2.8657 2.5552 -0.2818 -0.5824 -0.2320 297 ASP A CA 1854 C C . ASP A 284 ? 3.8215 2.7530 2.4913 -0.2808 -0.5821 -0.2541 297 ASP A C 1855 O O . ASP A 284 ? 3.7554 2.6839 2.4442 -0.2910 -0.6035 -0.2270 297 ASP A O 1856 C CB . ASP A 284 ? 3.7650 2.8595 2.5422 -0.2820 -0.6050 -0.1784 297 ASP A CB 1857 N N . ASP A 289 ? 3.0987 2.4274 2.0427 -0.2983 -0.6603 -0.0393 302 ASP A N 1858 C CA . ASP A 289 ? 3.1573 2.5141 2.0767 -0.3347 -0.6758 -0.0210 302 ASP A CA 1859 C C . ASP A 289 ? 3.1898 2.5342 2.0791 -0.3219 -0.6492 -0.0564 302 ASP A C 1860 O O . ASP A 289 ? 3.2998 2.5796 2.1165 -0.3454 -0.6451 -0.0890 302 ASP A O 1861 C CB . ASP A 289 ? 3.0828 2.5324 2.0717 -0.3322 -0.6925 0.0308 302 ASP A CB 1862 N N . THR A 290 ? 3.0384 2.4438 1.9822 -0.2854 -0.6308 -0.0503 303 THR A N 1863 C CA . THR A 290 ? 2.8957 2.3001 1.8187 -0.2712 -0.6051 -0.0801 303 THR A CA 1864 C C . THR A 290 ? 2.7535 2.1308 1.6848 -0.2234 -0.5683 -0.1241 303 THR A C 1865 O O . THR A 290 ? 2.6695 2.0620 1.6523 -0.1880 -0.5594 -0.1209 303 THR A O 1866 C CB . THR A 290 ? 2.7995 2.2831 1.7709 -0.2624 -0.6065 -0.0480 303 THR A CB 1867 N N . TYR A 291 ? 2.7134 2.0527 1.5935 -0.2231 -0.5473 -0.1648 304 TYR A N 1868 C CA . TYR A 291 ? 2.6709 1.9809 1.5510 -0.1810 -0.5128 -0.2092 304 TYR A CA 1869 C C . TYR A 291 ? 2.6012 1.9729 1.5422 -0.1355 -0.4873 -0.2093 304 TYR A C 1870 O O . TYR A 291 ? 2.6124 2.0278 1.5626 -0.1396 -0.4849 -0.1974 304 TYR A O 1871 C CB . TYR A 291 ? 2.7344 1.9800 1.5358 -0.1968 -0.4981 -0.2554 304 TYR A CB 1872 C CG . TYR A 291 ? 2.7385 1.9658 1.5436 -0.1510 -0.4603 -0.3003 304 TYR A CG 1873 C CD1 . TYR A 291 ? 2.7175 1.9131 1.5390 -0.1206 -0.4498 -0.3163 304 TYR A CD1 1874 C CD2 . TYR A 291 ? 2.7912 2.0353 1.5837 -0.1386 -0.4356 -0.3254 304 TYR A CD2 1875 C CE1 . TYR A 291 ? 2.7700 1.9534 1.5972 -0.0778 -0.4156 -0.3556 304 TYR A CE1 1876 C CE2 . TYR A 291 ? 2.7801 2.0127 1.5770 -0.0971 -0.4009 -0.3657 304 TYR A CE2 1877 C CZ . TYR A 291 ? 2.7853 1.9889 1.6007 -0.0662 -0.3911 -0.3803 304 TYR A CZ 1878 O OH . TYR A 291 ? 2.7721 1.9684 1.5940 -0.0241 -0.3571 -0.4188 304 TYR A OH 1879 N N . SER A 292 ? 2.4814 1.8539 1.4615 -0.0929 -0.4679 -0.2234 305 SER A N 1880 C CA . SER A 292 ? 2.3761 1.8044 1.4145 -0.0488 -0.4426 -0.2249 305 SER A CA 1881 C C . SER A 292 ? 2.3859 1.7829 1.4212 -0.0098 -0.4111 -0.2685 305 SER A C 1882 O O . SER A 292 ? 2.3230 1.6664 1.3371 -0.0076 -0.4128 -0.2849 305 SER A O 1883 C CB . SER A 292 ? 2.3980 1.8845 1.5111 -0.0346 -0.4560 -0.1817 305 SER A CB 1884 O OG . SER A 292 ? 2.3856 1.8929 1.5492 0.0125 -0.4323 -0.1930 305 SER A OG 1885 N N . ILE A 293 ? 2.4853 1.9156 1.5406 0.0210 -0.3823 -0.2871 306 ILE A N 1886 C CA . ILE A 293 ? 2.5349 1.9510 1.6007 0.0628 -0.3520 -0.3230 306 ILE A CA 1887 C C . ILE A 293 ? 2.4780 1.9065 1.5994 0.0894 -0.3560 -0.3057 306 ILE A C 1888 O O . ILE A 293 ? 2.4695 1.8476 1.5741 0.0986 -0.3539 -0.3245 306 ILE A O 1889 C CB . ILE A 293 ? 2.4848 1.9473 1.5718 0.0911 -0.3216 -0.3397 306 ILE A CB 1890 C CG1 . ILE A 293 ? 2.4714 1.9073 1.4937 0.0701 -0.3113 -0.3698 306 ILE A CG1 1891 C CG2 . ILE A 293 ? 2.5454 2.0104 1.6615 0.1378 -0.2932 -0.3663 306 ILE A CG2 1892 C CD1 . ILE A 293 ? 2.5276 1.9023 1.5005 0.0798 -0.2923 -0.4178 306 ILE A CD1 1893 N N . THR A 294 ? 2.3742 1.8677 1.5603 0.1008 -0.3621 -0.2698 307 THR A N 1894 C CA . THR A 294 ? 2.2579 1.7679 1.4979 0.1227 -0.3675 -0.2505 307 THR A CA 1895 C C . THR A 294 ? 2.2078 1.6613 1.4163 0.0954 -0.3942 -0.2423 307 THR A C 1896 O O . THR A 294 ? 2.2224 1.6500 1.4426 0.1131 -0.3928 -0.2485 307 THR A O 1897 C CB . THR A 294 ? 2.2169 1.8016 1.5243 0.1280 -0.3771 -0.2072 307 THR A CB 1898 O OG1 . THR A 294 ? 2.1876 1.8224 1.5255 0.1552 -0.3507 -0.2151 307 THR A OG1 1899 C CG2 . THR A 294 ? 2.1798 1.7772 1.5370 0.1465 -0.3842 -0.1885 307 THR A CG2 1900 N N . ALA A 295 ? 2.1331 1.5671 1.2995 0.0510 -0.4187 -0.2282 308 ALA A N 1901 C CA . ALA A 295 ? 2.1635 1.5407 1.2898 0.0173 -0.4453 -0.2210 308 ALA A CA 1902 C C . ALA A 295 ? 2.3389 1.6357 1.4134 0.0244 -0.4327 -0.2632 308 ALA A C 1903 O O . ALA A 295 ? 2.4854 1.7501 1.5667 0.0324 -0.4391 -0.2618 308 ALA A O 1904 C CB . ALA A 295 ? 2.1761 1.5497 1.2621 -0.0321 -0.4706 -0.2020 308 ALA A CB 1905 N N . CYS A 296 ? 2.3272 1.5899 1.3484 0.0204 -0.4153 -0.3002 309 CYS A N 1906 C CA . CYS A 296 ? 2.4101 1.5970 1.3824 0.0307 -0.4001 -0.3427 309 CYS A CA 1907 C C . CYS A 296 ? 2.3503 1.5507 1.3696 0.0843 -0.3746 -0.3583 309 CYS A C 1908 O O . CYS A 296 ? 2.3620 1.5106 1.3692 0.0987 -0.3712 -0.3745 309 CYS A O 1909 C CB . CYS A 296 ? 2.4283 1.5864 1.3401 0.0196 -0.3830 -0.3801 309 CYS A CB 1910 S SG . CYS A 296 ? 4.2794 3.4972 3.2249 0.0615 -0.3455 -0.4024 309 CYS A SG 1911 N N . ARG A 297 ? 2.3000 1.5710 1.3730 0.1132 -0.3571 -0.3522 310 ARG A N 1912 C CA . ARG A 297 ? 2.3692 1.6626 1.4888 0.1630 -0.3320 -0.3658 310 ARG A CA 1913 C C . ARG A 297 ? 2.4051 1.6926 1.5623 0.1737 -0.3467 -0.3428 310 ARG A C 1914 O O . ARG A 297 ? 2.4765 1.7467 1.6484 0.2080 -0.3308 -0.3607 310 ARG A O 1915 C CB . ARG A 297 ? 2.3731 1.7486 1.5457 0.1856 -0.3144 -0.3564 310 ARG A CB 1916 C CG . ARG A 297 ? 2.3249 1.7316 1.5457 0.2361 -0.2863 -0.3712 310 ARG A CG 1917 C CD . ARG A 297 ? 2.2685 1.6919 1.4757 0.2566 -0.2537 -0.4067 310 ARG A CD 1918 N NE . ARG A 297 ? 2.2381 1.7017 1.4957 0.3026 -0.2280 -0.4165 310 ARG A NE 1919 C CZ . ARG A 297 ? 2.1184 1.6531 1.4245 0.3194 -0.2146 -0.4045 310 ARG A CZ 1920 N NH1 . ARG A 297 ? 1.8698 1.4401 1.2191 0.3595 -0.1914 -0.4142 310 ARG A NH1 1921 N NH2 . ARG A 297 ? 2.1701 1.7394 1.4799 0.2954 -0.2245 -0.3825 310 ARG A NH2 1922 N N . ILE A 298 ? 2.4109 1.7146 1.5842 0.1445 -0.3772 -0.3025 311 ILE A N 1923 C CA . ILE A 298 ? 2.4851 1.7906 1.6977 0.1527 -0.3922 -0.2775 311 ILE A CA 1924 C C . ILE A 298 ? 2.5392 1.7590 1.7047 0.1400 -0.4045 -0.2900 311 ILE A C 1925 O O . ILE A 298 ? 2.5250 1.7260 1.7102 0.1688 -0.3968 -0.2971 311 ILE A O 1926 C CB . ILE A 298 ? 2.4837 1.8450 1.7380 0.1294 -0.4194 -0.2281 311 ILE A CB 1927 C CG1 . ILE A 298 ? 2.3955 1.8421 1.7078 0.1510 -0.4048 -0.2139 311 ILE A CG1 1928 C CG2 . ILE A 298 ? 2.4805 1.8388 1.7689 0.1347 -0.4354 -0.2043 311 ILE A CG2 1929 C CD1 . ILE A 298 ? 2.3622 1.8681 1.7218 0.1346 -0.4281 -0.1661 311 ILE A CD1 1930 N N . ASP A 299 ? 2.5736 1.7399 1.6756 0.0968 -0.4234 -0.2928 312 ASP A N 1931 C CA . ASP A 299 ? 2.7103 1.7906 1.7636 0.0816 -0.4358 -0.3039 312 ASP A CA 1932 C C . ASP A 299 ? 2.6885 1.7118 1.7114 0.1150 -0.4068 -0.3513 312 ASP A C 1933 O O . ASP A 299 ? 2.6969 1.6517 1.6927 0.1183 -0.4100 -0.3634 312 ASP A O 1934 C CB . ASP A 299 ? 2.8761 1.9118 1.8657 0.0241 -0.4634 -0.2953 312 ASP A CB 1935 C CG . ASP A 299 ? 2.9719 1.9710 1.8965 0.0085 -0.4501 -0.3306 312 ASP A CG 1936 O OD1 . ASP A 299 ? 3.0158 1.9625 1.9076 0.0315 -0.4263 -0.3721 312 ASP A OD1 1937 O OD2 . ASP A 299 ? 2.9809 2.0038 1.8866 -0.0272 -0.4638 -0.3164 312 ASP A OD2 1938 N N . CYS A 300 ? 2.6649 1.7185 1.6933 0.1401 -0.3783 -0.3772 313 CYS A N 1939 C CA . CYS A 300 ? 2.7125 1.7283 1.7214 0.1771 -0.3472 -0.4217 313 CYS A CA 1940 C C . CYS A 300 ? 2.6853 1.7221 1.7523 0.2234 -0.3355 -0.4173 313 CYS A C 1941 O O . CYS A 300 ? 2.7890 1.7793 1.8414 0.2526 -0.3182 -0.4460 313 CYS A O 1942 C CB . CYS A 300 ? 2.7107 1.7673 1.7171 0.1900 -0.3210 -0.4456 313 CYS A CB 1943 S SG . CYS A 300 ? 3.0040 1.9927 1.9442 0.2062 -0.2905 -0.5056 313 CYS A SG 1944 N N . GLU A 301 ? 2.6013 1.7111 1.7354 0.2310 -0.3439 -0.3813 314 GLU A N 1945 C CA . GLU A 301 ? 2.5714 1.7037 1.7620 0.2681 -0.3382 -0.3704 314 GLU A CA 1946 C C . GLU A 301 ? 2.5750 1.6559 1.7542 0.2479 -0.3663 -0.3490 314 GLU A C 1947 O O . GLU A 301 ? 2.5788 1.6308 1.7706 0.2741 -0.3619 -0.3538 314 GLU A O 1948 C CB . GLU A 301 ? 2.5582 1.7889 1.8228 0.2819 -0.3354 -0.3410 314 GLU A CB 1949 C CG . GLU A 301 ? 2.6265 1.9074 1.8965 0.2927 -0.3115 -0.3580 314 GLU A CG 1950 C CD . GLU A 301 ? 2.5700 1.9403 1.9018 0.2946 -0.3137 -0.3256 314 GLU A CD 1951 O OE1 . GLU A 301 ? 2.5823 1.9719 1.9365 0.2713 -0.3401 -0.2880 314 GLU A OE1 1952 O OE2 . GLU A 301 ? 2.4870 1.9077 1.8438 0.3192 -0.2886 -0.3382 314 GLU A OE2 1953 N N . THR A 302 ? 2.5711 1.6407 1.7247 0.1999 -0.3955 -0.3249 315 THR A N 1954 C CA . THR A 302 ? 2.5818 1.6036 1.7190 0.1729 -0.4248 -0.3027 315 THR A CA 1955 C C . THR A 302 ? 2.7197 1.6380 1.7938 0.1754 -0.4198 -0.3360 315 THR A C 1956 O O . THR A 302 ? 2.7328 1.6189 1.8194 0.1972 -0.4197 -0.3356 315 THR A O 1957 C CB . THR A 302 ? 2.5037 1.5324 1.6168 0.1177 -0.4557 -0.2742 315 THR A CB 1958 O OG1 . THR A 302 ? 2.4217 1.5435 1.5879 0.1181 -0.4563 -0.2484 315 THR A OG1 1959 C CG2 . THR A 302 ? 2.4796 1.4803 1.5906 0.0904 -0.4871 -0.2436 315 THR A CG2 1960 N N . ARG A 303 ? 2.7358 1.6024 1.7425 0.1549 -0.4140 -0.3657 316 ARG A N 1961 C CA . ARG A 303 ? 2.7347 1.4996 1.6756 0.1573 -0.4059 -0.4019 316 ARG A CA 1962 C C . ARG A 303 ? 2.8552 1.6091 1.8228 0.2149 -0.3781 -0.4260 316 ARG A C 1963 O O . ARG A 303 ? 2.9240 1.6117 1.8741 0.2254 -0.3811 -0.4324 316 ARG A O 1964 C CB . ARG A 303 ? 2.5951 1.3233 1.4681 0.1345 -0.3959 -0.4349 316 ARG A CB 1965 N N . TYR A 304 ? 2.8982 1.7189 1.9083 0.2514 -0.3515 -0.4379 317 TYR A N 1966 C CA . TYR A 304 ? 2.9149 1.7379 1.9530 0.3069 -0.3228 -0.4614 317 TYR A CA 1967 C C . TYR A 304 ? 2.9092 1.7543 2.0057 0.3306 -0.3313 -0.4333 317 TYR A C 1968 O O . TYR A 304 ? 2.9644 1.7610 2.0568 0.3601 -0.3226 -0.4474 317 TYR A O 1969 C CB . TYR A 304 ? 2.7959 1.6963 1.8678 0.3338 -0.2949 -0.4760 317 TYR A CB 1970 C CG . TYR A 304 ? 2.6849 1.5956 1.7831 0.3899 -0.2629 -0.5029 317 TYR A CG 1971 C CD1 . TYR A 304 ? 2.7036 1.5685 1.7561 0.4078 -0.2378 -0.5476 317 TYR A CD1 1972 C CD2 . TYR A 304 ? 2.5938 1.5636 1.7628 0.4244 -0.2574 -0.4833 317 TYR A CD2 1973 C CE1 . TYR A 304 ? 2.6631 1.5703 1.7637 0.4486 -0.2037 -0.5568 317 TYR A CE1 1974 C CE2 . TYR A 304 ? 2.6038 1.5878 1.7977 0.4749 -0.2286 -0.5064 317 TYR A CE2 1975 C CZ . TYR A 304 ? 2.6233 1.5853 1.7897 0.4830 -0.2007 -0.5380 317 TYR A CZ 1976 O OH . TYR A 304 ? 2.5798 1.5959 1.7999 0.5145 -0.1670 -0.5397 317 TYR A OH 1977 N N . LEU A 305 ? 2.8444 1.7635 1.9957 0.3190 -0.3477 -0.3935 318 LEU A N 1978 C CA . LEU A 305 ? 2.8034 1.7498 2.0118 0.3383 -0.3567 -0.3648 318 LEU A CA 1979 C C . LEU A 305 ? 2.9302 1.7924 2.1018 0.3174 -0.3809 -0.3553 318 LEU A C 1980 O O . LEU A 305 ? 2.9880 1.8205 2.1735 0.3461 -0.3770 -0.3571 318 LEU A O 1981 C CB . LEU A 305 ? 2.6001 1.6397 1.8692 0.3248 -0.3705 -0.3242 318 LEU A CB 1982 N N . VAL A 306 ? 2.8770 1.7008 2.0006 0.2666 -0.4061 -0.3445 319 VAL A N 1983 C CA . VAL A 306 ? 2.8531 1.5901 1.9309 0.2399 -0.4297 -0.3376 319 VAL A CA 1984 C C . VAL A 306 ? 2.8994 1.5463 1.9332 0.2685 -0.4109 -0.3763 319 VAL A C 1985 O O . VAL A 306 ? 2.8583 1.4773 1.9096 0.2945 -0.4105 -0.3722 319 VAL A O 1986 C CB . VAL A 306 ? 2.8514 1.5548 1.8713 0.1795 -0.4551 -0.3290 319 VAL A CB 1987 C CG1 . VAL A 306 ? 2.7639 1.3597 1.7194 0.1535 -0.4729 -0.3342 319 VAL A CG1 1988 C CG2 . VAL A 306 ? 2.8778 1.6643 1.9449 0.1504 -0.4797 -0.2827 319 VAL A CG2 1989 N N . GLU A 307 ? 2.9866 1.5912 1.9648 0.2651 -0.3942 -0.4139 320 GLU A N 1990 C CA . GLU A 307 ? 3.0673 1.5878 1.9997 0.2933 -0.3725 -0.4555 320 GLU A CA 1991 C C . GLU A 307 ? 3.0923 1.6324 2.0766 0.3543 -0.3503 -0.4627 320 GLU A C 1992 O O . GLU A 307 ? 3.1283 1.6050 2.1020 0.3690 -0.3544 -0.4633 320 GLU A O 1993 C CB . GLU A 307 ? 3.0656 1.5752 1.9519 0.2888 -0.3515 -0.4936 320 GLU A CB 1994 C CG . GLU A 307 ? 3.1606 1.6330 2.0301 0.3360 -0.3170 -0.5384 320 GLU A CG 1995 C CD . GLU A 307 ? 3.2688 1.7531 2.1045 0.3285 -0.2954 -0.5706 320 GLU A CD 1996 O OE1 . GLU A 307 ? 3.2611 1.8055 2.1398 0.3630 -0.2579 -0.5850 320 GLU A OE1 1997 O OE2 . GLU A 307 ? 3.3392 1.8004 2.1245 0.2801 -0.3125 -0.5700 320 GLU A OE2 1998 N N . ASN A 308 ? 3.1229 1.7498 2.1621 0.3888 -0.3274 -0.4672 321 ASN A N 1999 C CA . ASN A 308 ? 3.1568 1.8068 2.2431 0.4464 -0.3044 -0.4762 321 ASN A CA 2000 C C . ASN A 308 ? 3.1241 1.8031 2.2680 0.4578 -0.3208 -0.4383 321 ASN A C 2001 O O . ASN A 308 ? 3.1008 1.7617 2.2647 0.4981 -0.3096 -0.4440 321 ASN A O 2002 C CB . ASN A 308 ? 3.1012 1.8371 2.2269 0.4773 -0.2747 -0.4925 321 ASN A CB 2003 C CG . ASN A 308 ? 3.1262 1.8678 2.2663 0.5190 -0.2377 -0.5183 321 ASN A CG 2004 O OD1 . ASN A 308 ? 3.2202 1.9554 2.3903 0.5451 -0.2323 -0.5091 321 ASN A OD1 2005 N ND2 . ASN A 308 ? 3.0208 1.7964 2.1537 0.5141 -0.2094 -0.5399 321 ASN A ND2 2006 N N . CYS A 309 ? 3.1295 1.8573 2.3017 0.4234 -0.3466 -0.3992 322 CYS A N 2007 C CA . CYS A 309 ? 3.1840 1.9418 2.4094 0.4292 -0.3638 -0.3617 322 CYS A CA 2008 C C . CYS A 309 ? 3.3389 2.0248 2.5300 0.3924 -0.3967 -0.3392 322 CYS A C 2009 O O . CYS A 309 ? 3.3648 2.0653 2.5944 0.3976 -0.4110 -0.3100 322 CYS A O 2010 C CB . CYS A 309 ? 3.0380 1.9096 2.3312 0.4234 -0.3680 -0.3305 322 CYS A CB 2011 S SG . CYS A 309 ? 5.8879 4.8478 5.2279 0.4684 -0.3298 -0.3526 322 CYS A SG 2012 N N . ASN A 310 ? 3.0900 1.5933 2.4335 0.2226 0.3554 0.0715 323 ASN A N 2013 C CA . ASN A 310 ? 3.1426 1.6073 2.4773 0.2011 0.3723 0.0724 323 ASN A CA 2014 C C . ASN A 310 ? 3.1364 1.6102 2.4353 0.1794 0.3854 0.0773 323 ASN A C 2015 O O . ASN A 310 ? 3.2138 1.6382 2.4849 0.1675 0.3994 0.0921 323 ASN A O 2016 C CB . ASN A 310 ? 3.1922 1.5900 2.5306 0.2103 0.3674 0.0939 323 ASN A CB 2017 C CG . ASN A 310 ? 3.1466 1.5284 2.5235 0.2234 0.3616 0.0819 323 ASN A CG 2018 O OD1 . ASN A 310 ? 3.0883 1.4935 2.4856 0.2144 0.3695 0.0564 323 ASN A OD1 2019 N ND2 . ASN A 310 ? 3.1079 1.4503 2.4951 0.2448 0.3472 0.1007 323 ASN A ND2 2020 N N . CYS A 311 ? 2.9976 1.5266 2.2883 0.1756 0.3856 0.0655 324 CYS A N 2021 C CA . CYS A 311 ? 2.8847 1.4247 2.1361 0.1565 0.4022 0.0656 324 CYS A CA 2022 C C . CYS A 311 ? 2.7705 1.3834 2.0351 0.1493 0.3993 0.0443 324 CYS A C 2023 O O . CYS A 311 ? 2.6434 1.2888 1.9284 0.1644 0.3866 0.0365 324 CYS A O 2024 C CB . CYS A 311 ? 2.9241 1.4313 2.1252 0.1675 0.4032 0.0917 324 CYS A CB 2025 S SG . CYS A 311 ? 3.2280 1.7689 2.3832 0.1545 0.4154 0.0875 324 CYS A SG 2026 N N . ARG A 312 ? 2.8328 1.4625 2.0758 0.1269 0.4158 0.0369 325 ARG A N 2027 C CA . ARG A 312 ? 2.7694 1.4625 2.0151 0.1191 0.4150 0.0222 325 ARG A CA 2028 C C . ARG A 312 ? 2.8335 1.5222 2.0283 0.1188 0.4218 0.0338 325 ARG A C 2029 O O . ARG A 312 ? 2.8897 1.5280 2.0423 0.1135 0.4368 0.0475 325 ARG A O 2030 C CB . ARG A 312 ? 2.7016 1.4158 1.9567 0.0934 0.4327 0.0043 325 ARG A CB 2031 C CG . ARG A 312 ? 2.6387 1.3553 1.8633 0.0719 0.4481 0.0054 325 ARG A CG 2032 C CD . ARG A 312 ? 2.6509 1.3781 1.8874 0.0471 0.4663 -0.0101 325 ARG A CD 2033 N NE . ARG A 312 ? 2.6916 1.4502 1.9093 0.0274 0.4778 -0.0149 325 ARG A NE 2034 C CZ . ARG A 312 ? 2.7024 1.4577 1.9159 0.0039 0.4966 -0.0228 325 ARG A CZ 2035 N NH1 . ARG A 312 ? 2.7114 1.4320 1.9371 -0.0031 0.5059 -0.0266 325 ARG A NH1 2036 N NH2 . ARG A 312 ? 2.6321 1.4186 1.8302 -0.0129 0.5061 -0.0270 325 ARG A NH2 2037 N N . MET A 313 ? 2.7934 1.5333 1.9908 0.1241 0.4111 0.0283 326 MET A N 2038 C CA . MET A 313 ? 2.8229 1.5613 1.9702 0.1261 0.4166 0.0371 326 MET A CA 2039 C C . MET A 313 ? 2.7840 1.5494 1.9166 0.1000 0.4333 0.0263 326 MET A C 2040 O O . MET A 313 ? 2.7279 1.5437 1.9016 0.0854 0.4298 0.0115 326 MET A O 2041 C CB . MET A 313 ? 2.8275 1.6071 1.9870 0.1453 0.3952 0.0373 326 MET A CB 2042 C CG . MET A 313 ? 2.8451 1.6058 1.9509 0.1587 0.3952 0.0515 326 MET A CG 2043 S SD . MET A 313 ? 2.9504 1.7695 2.0742 0.1767 0.3707 0.0482 326 MET A SD 2044 C CE . MET A 313 ? 1.6979 0.4985 0.8537 0.2048 0.3510 0.0565 326 MET A CE 2045 N N . VAL A 314 ? 2.8331 1.5683 1.9099 0.0947 0.4490 0.0340 327 VAL A N 2046 C CA . VAL A 314 ? 2.8555 1.6027 1.9128 0.0685 0.4693 0.0244 327 VAL A CA 2047 C C . VAL A 314 ? 2.7003 1.5210 1.7942 0.0525 0.4635 0.0119 327 VAL A C 2048 O O . VAL A 314 ? 2.7510 1.5883 1.8557 0.0289 0.4767 0.0030 327 VAL A O 2049 C CB . VAL A 314 ? 2.9076 1.6247 1.9009 0.0693 0.4810 0.0312 327 VAL A CB 2050 C CG1 . VAL A 314 ? 3.0042 1.6501 1.9671 0.0777 0.4852 0.0485 327 VAL A CG1 2051 C CG2 . VAL A 314 ? 2.8575 1.6052 1.8389 0.0865 0.4650 0.0346 327 VAL A CG2 2052 N N . HIS A 315 ? 2.4961 1.3622 1.6125 0.0642 0.4417 0.0133 328 HIS A N 2053 C CA . HIS A 315 ? 2.4914 1.4285 1.6522 0.0480 0.4294 0.0066 328 HIS A CA 2054 C C . HIS A 315 ? 2.5973 1.5570 1.8077 0.0456 0.4238 -0.0040 328 HIS A C 2055 O O . HIS A 315 ? 2.6484 1.6508 1.8870 0.0336 0.4194 -0.0084 328 HIS A O 2056 C CB . HIS A 315 ? 2.5045 1.4744 1.6638 0.0590 0.4100 0.0144 328 HIS A CB 2057 C CG . HIS A 315 ? 2.5316 1.5026 1.7048 0.0861 0.3902 0.0159 328 HIS A CG 2058 N ND1 . HIS A 315 ? 2.5318 1.5245 1.7469 0.0917 0.3800 0.0081 328 HIS A ND1 2059 C CD2 . HIS A 315 ? 2.6150 1.5511 1.7470 0.1101 0.3876 0.0261 328 HIS A CD2 2060 C CE1 . HIS A 315 ? 2.5861 1.5728 1.8034 0.1165 0.3647 0.0116 328 HIS A CE1 2061 N NE2 . HIS A 315 ? 2.6330 1.5910 1.8074 0.1279 0.3659 0.0226 328 HIS A NE2 2062 N N . MET A 316 ? 2.6528 1.5771 1.8708 0.0572 0.4252 -0.0065 329 MET A N 2063 C CA . MET A 316 ? 2.7433 1.6771 1.9995 0.0550 0.4249 -0.0175 329 MET A CA 2064 C C . MET A 316 ? 2.8817 1.8029 2.1433 0.0327 0.4451 -0.0261 329 MET A C 2065 O O . MET A 316 ? 2.9761 1.8612 2.2122 0.0253 0.4589 -0.0230 329 MET A O 2066 C CB . MET A 316 ? 2.7680 1.6704 2.0351 0.0786 0.4147 -0.0156 329 MET A CB 2067 C CG . MET A 316 ? 2.6981 1.6243 1.9756 0.1000 0.3937 -0.0123 329 MET A CG 2068 S SD . MET A 316 ? 2.6538 1.5294 1.9227 0.1287 0.3832 -0.0005 329 MET A SD 2069 C CE . MET A 316 ? 2.1408 1.0522 1.4453 0.1481 0.3627 -0.0070 329 MET A CE 2070 N N . PRO A 317 ? 2.8879 1.8386 2.1841 0.0220 0.4462 -0.0374 330 PRO A N 2071 C CA . PRO A 317 ? 2.9947 1.9408 2.3017 0.0005 0.4644 -0.0474 330 PRO A CA 2072 C C . PRO A 317 ? 3.1571 2.0543 2.4680 0.0071 0.4707 -0.0513 330 PRO A C 2073 O O . PRO A 317 ? 3.2035 2.0677 2.5071 0.0280 0.4612 -0.0438 330 PRO A O 2074 C CB . PRO A 317 ? 2.9110 1.9071 2.2569 -0.0080 0.4576 -0.0567 330 PRO A CB 2075 C CG . PRO A 317 ? 2.8365 1.8431 2.1968 0.0151 0.4369 -0.0552 330 PRO A CG 2076 C CD . PRO A 317 ? 2.8086 1.8000 2.1372 0.0305 0.4289 -0.0418 330 PRO A CD 2077 N N . GLY A 318 ? 3.2266 2.1189 2.5509 -0.0107 0.4858 -0.0619 331 GLY A N 2078 C CA . GLY A 318 ? 3.3021 2.1502 2.6361 -0.0069 0.4911 -0.0666 331 GLY A CA 2079 C C . GLY A 318 ? 3.3759 2.1746 2.6840 -0.0167 0.5070 -0.0620 331 GLY A C 2080 O O . GLY A 318 ? 3.4216 2.2204 2.7018 -0.0262 0.5148 -0.0562 331 GLY A O 2081 N N . ASP A 319 ? 3.3785 2.1346 2.6971 -0.0153 0.5115 -0.0649 332 ASP A N 2082 C CA . ASP A 319 ? 3.3629 2.0660 2.6611 -0.0247 0.5247 -0.0590 332 ASP A CA 2083 C C . ASP A 319 ? 3.3155 1.9654 2.5962 -0.0055 0.5144 -0.0399 332 ASP A C 2084 O O . ASP A 319 ? 3.3908 1.9950 2.6520 -0.0127 0.5225 -0.0298 332 ASP A O 2085 C CB . ASP A 319 ? 3.4179 2.1025 2.7384 -0.0374 0.5362 -0.0716 332 ASP A CB 2086 C CG . ASP A 319 ? 3.4323 2.1417 2.7891 -0.0286 0.5269 -0.0839 332 ASP A CG 2087 O OD1 . ASP A 319 ? 3.4471 2.1246 2.8162 -0.0108 0.5164 -0.0808 332 ASP A OD1 2088 O OD2 . ASP A 319 ? 3.4153 2.1763 2.7895 -0.0398 0.5293 -0.0961 332 ASP A OD2 2089 N N . ALA A 320 ? 3.1666 1.8237 2.4554 0.0183 0.4958 -0.0337 333 ALA A N 2090 C CA . ALA A 320 ? 3.0720 1.6809 2.3525 0.0393 0.4832 -0.0151 333 ALA A CA 2091 C C . ALA A 320 ? 3.0679 1.6540 2.3112 0.0400 0.4828 0.0046 333 ALA A C 2092 O O . ALA A 320 ? 3.0703 1.6801 2.2910 0.0259 0.4924 0.0020 333 ALA A O 2093 C CB . ALA A 320 ? 2.9440 1.5729 2.2455 0.0640 0.4637 -0.0157 333 ALA A CB 2094 N N . PRO A 321 ? 3.0082 1.5421 2.2405 0.0559 0.4748 0.0255 334 PRO A N 2095 C CA . PRO A 321 ? 3.0160 1.5064 2.1953 0.0565 0.4846 0.0479 334 PRO A CA 2096 C C . PRO A 321 ? 3.0608 1.5809 2.2156 0.0699 0.4768 0.0526 334 PRO A C 2097 O O . PRO A 321 ? 3.0805 1.6419 2.2611 0.0855 0.4595 0.0452 334 PRO A O 2098 C CB . PRO A 321 ? 3.0366 1.4670 2.2180 0.0732 0.4752 0.0700 334 PRO A CB 2099 C CG . PRO A 321 ? 2.9844 1.4424 2.2131 0.0920 0.4546 0.0593 334 PRO A CG 2100 C CD . PRO A 321 ? 2.9362 1.4457 2.1968 0.0767 0.4590 0.0307 334 PRO A CD 2101 N N . TYR A 322 ? 3.0964 1.5959 2.2022 0.0631 0.4889 0.0646 335 TYR A N 2102 C CA . TYR A 322 ? 3.0427 1.5611 2.1192 0.0770 0.4813 0.0713 335 TYR A CA 2103 C C . TYR A 322 ? 3.0820 1.5632 2.1474 0.1026 0.4653 0.0969 335 TYR A C 2104 O O . TYR A 322 ? 3.2727 1.7020 2.3372 0.1050 0.4651 0.1152 335 TYR A O 2105 C CB . TYR A 322 ? 2.9869 1.5005 2.0161 0.0595 0.4992 0.0718 335 TYR A CB 2106 C CG . TYR A 322 ? 2.9357 1.5020 1.9768 0.0391 0.5108 0.0458 335 TYR A CG 2107 C CD1 . TYR A 322 ? 2.8581 1.4834 1.9430 0.0428 0.4987 0.0293 335 TYR A CD1 2108 C CD2 . TYR A 322 ? 2.9712 1.5316 1.9840 0.0154 0.5318 0.0391 335 TYR A CD2 2109 C CE1 . TYR A 322 ? 2.8124 1.4908 1.9135 0.0235 0.5061 0.0104 335 TYR A CE1 2110 C CE2 . TYR A 322 ? 2.9541 1.5659 1.9808 -0.0031 0.5416 0.0168 335 TYR A CE2 2111 C CZ . TYR A 322 ? 2.9066 1.5780 1.9780 0.0010 0.5281 0.0047 335 TYR A CZ 2112 O OH . TYR A 322 ? 2.9209 1.6477 2.0116 -0.0184 0.5344 -0.0114 335 TYR A OH 2113 N N . CYS A 323 ? 2.8670 1.3758 1.9251 0.1218 0.4509 0.0994 336 CYS A N 2114 C CA . CYS A 323 ? 2.7522 1.2313 1.8005 0.1472 0.4342 0.1242 336 CYS A CA 2115 C C . CYS A 323 ? 2.7377 1.1763 1.7335 0.1446 0.4403 0.1493 336 CYS A C 2116 O O . CYS A 323 ? 2.6467 1.0824 1.6135 0.1232 0.4576 0.1449 336 CYS A O 2117 C CB . CYS A 323 ? 2.6392 1.1644 1.7003 0.1688 0.4155 0.1180 336 CYS A CB 2118 S SG . CYS A 323 ? 3.6378 2.1847 2.7630 0.1862 0.3957 0.1080 336 CYS A SG 2119 N N . THR A 324 ? 2.7728 1.1836 1.7589 0.1660 0.4246 0.1761 337 THR A N 2120 C CA . THR A 324 ? 2.8900 1.2710 1.8292 0.1663 0.4246 0.2039 337 THR A CA 2121 C C . THR A 324 ? 2.7982 1.2019 1.7262 0.1921 0.4045 0.2140 337 THR A C 2122 O O . THR A 324 ? 2.6240 1.0534 1.5837 0.2116 0.3898 0.2048 337 THR A O 2123 C CB . THR A 324 ? 3.0692 1.3901 2.0039 0.1657 0.4234 0.2349 337 THR A CB 2124 O OG1 . THR A 324 ? 3.0898 1.3992 2.0666 0.1830 0.4105 0.2361 337 THR A OG1 2125 C CG2 . THR A 324 ? 3.1225 1.4167 2.0485 0.1354 0.4458 0.2318 337 THR A CG2 2126 N N . PRO A 325 ? 2.7754 1.1725 1.6600 0.1914 0.4029 0.2330 338 PRO A N 2127 C CA . PRO A 325 ? 2.8298 1.2449 1.6987 0.2150 0.3827 0.2478 338 PRO A CA 2128 C C . PRO A 325 ? 3.0183 1.4198 1.9146 0.2416 0.3623 0.2647 338 PRO A C 2129 O O . PRO A 325 ? 3.0300 1.4641 1.9398 0.2632 0.3458 0.2590 338 PRO A O 2130 C CB . PRO A 325 ? 2.7510 1.1418 1.5754 0.2049 0.3848 0.2765 338 PRO A CB 2131 C CG . PRO A 325 ? 2.6697 1.0538 1.4818 0.1734 0.4091 0.2618 338 PRO A CG 2132 C CD . PRO A 325 ? 2.6401 1.0206 1.4902 0.1649 0.4209 0.2377 338 PRO A CD 2133 N N . GLU A 326 ? 3.0703 1.4248 1.9761 0.2397 0.3632 0.2846 339 GLU A N 2134 C CA . GLU A 326 ? 3.0306 1.3691 1.9667 0.2641 0.3444 0.2991 339 GLU A CA 2135 C C . GLU A 326 ? 3.0329 1.4000 2.0186 0.2700 0.3427 0.2680 339 GLU A C 2136 O O . GLU A 326 ? 3.0499 1.4367 2.0627 0.2934 0.3245 0.2665 339 GLU A O 2137 C CB . GLU A 326 ? 3.0900 1.3694 2.0262 0.2587 0.3469 0.3260 339 GLU A CB 2138 C CG . GLU A 326 ? 3.1957 1.4561 2.1688 0.2830 0.3284 0.3377 339 GLU A CG 2139 C CD . GLU A 326 ? 3.4722 1.6755 2.4312 0.2847 0.3234 0.3767 339 GLU A CD 2140 O OE1 . GLU A 326 ? 3.5765 1.7520 2.5035 0.2624 0.3377 0.3909 339 GLU A OE1 2141 O OE2 . GLU A 326 ? 3.5450 1.7321 2.5254 0.3079 0.3047 0.3936 339 GLU A OE2 2142 N N . GLN A 327 ? 3.0585 1.4311 2.0580 0.2475 0.3611 0.2433 340 GLN A N 2143 C CA . GLN A 327 ? 3.0152 1.4187 2.0643 0.2488 0.3597 0.2139 340 GLN A CA 2144 C C . GLN A 327 ? 2.8398 1.3028 1.8957 0.2595 0.3503 0.1950 340 GLN A C 2145 O O . GLN A 327 ? 2.6698 1.1596 1.7643 0.2764 0.3351 0.1855 340 GLN A O 2146 C CB . GLN A 327 ? 3.0722 1.4746 2.1317 0.2205 0.3808 0.1925 340 GLN A CB 2147 C CG . GLN A 327 ? 3.1757 1.5376 2.2665 0.2170 0.3826 0.1963 340 GLN A CG 2148 C CD . GLN A 327 ? 3.1711 1.5260 2.2655 0.1876 0.4041 0.1797 340 GLN A CD 2149 O OE1 . GLN A 327 ? 3.2002 1.5521 2.2592 0.1679 0.4205 0.1800 340 GLN A OE1 2150 N NE2 . GLN A 327 ? 3.1127 1.4662 2.2509 0.1845 0.4034 0.1644 340 GLN A NE2 2151 N N . TYR A 328 ? 2.9105 1.3936 1.9291 0.2490 0.3592 0.1900 341 TYR A N 2152 C CA . TYR A 328 ? 2.8918 1.4297 1.9099 0.2569 0.3515 0.1731 341 TYR A CA 2153 C C . TYR A 328 ? 2.7856 1.3342 1.8130 0.2866 0.3277 0.1865 341 TYR A C 2154 O O . TYR A 328 ? 2.6311 1.2137 1.6996 0.2983 0.3156 0.1721 341 TYR A O 2155 C CB . TYR A 328 ? 2.9791 1.5248 1.9484 0.2441 0.3628 0.1720 341 TYR A CB 2156 C CG . TYR A 328 ? 3.0280 1.6028 2.0011 0.2193 0.3811 0.1436 341 TYR A CG 2157 C CD1 . TYR A 328 ? 3.1123 1.6601 2.0718 0.1942 0.4020 0.1415 341 TYR A CD1 2158 C CD2 . TYR A 328 ? 2.9755 1.6076 1.9687 0.2201 0.3763 0.1203 341 TYR A CD2 2159 C CE1 . TYR A 328 ? 3.0993 1.6770 2.0648 0.1716 0.4180 0.1161 341 TYR A CE1 2160 C CE2 . TYR A 328 ? 2.9508 1.6139 1.9508 0.1966 0.3910 0.0977 341 TYR A CE2 2161 C CZ . TYR A 328 ? 3.0347 1.6706 2.0206 0.1730 0.4120 0.0952 341 TYR A CZ 2162 O OH . TYR A 328 ? 3.0282 1.6984 2.0231 0.1495 0.4259 0.0740 341 TYR A OH 2163 N N . LYS A 329 ? 2.8053 1.3273 1.7970 0.2975 0.3203 0.2148 342 LYS A N 2164 C CA . LYS A 329 ? 2.6880 1.2208 1.6834 0.3257 0.2969 0.2308 342 LYS A CA 2165 C C . LYS A 329 ? 2.7548 1.2855 1.8015 0.3425 0.2835 0.2296 342 LYS A C 2166 O O . LYS A 329 ? 2.7453 1.3150 1.8198 0.3589 0.2687 0.2183 342 LYS A O 2167 C CB . LYS A 329 ? 2.5522 1.0496 1.5064 0.3314 0.2906 0.2671 342 LYS A CB 2168 N N . GLU A 330 ? 2.7969 1.2824 1.8575 0.3376 0.2885 0.2406 343 GLU A N 2169 C CA . GLU A 330 ? 2.8025 1.2788 1.9085 0.3558 0.2740 0.2437 343 GLU A CA 2170 C C . GLU A 330 ? 2.9966 1.5034 2.1554 0.3501 0.2762 0.2113 343 GLU A C 2171 O O . GLU A 330 ? 3.1800 1.6967 2.3802 0.3676 0.2612 0.2078 343 GLU A O 2172 C CB . GLU A 330 ? 2.6627 1.0754 1.7623 0.3575 0.2737 0.2733 343 GLU A CB 2173 N N . CYS A 331 ? 2.9580 1.4825 2.1178 0.3256 0.2937 0.1879 344 CYS A N 2174 C CA . CYS A 331 ? 2.9311 1.4914 2.1429 0.3185 0.2936 0.1579 344 CYS A CA 2175 C C . CYS A 331 ? 2.8125 1.4315 2.0275 0.3025 0.3002 0.1310 344 CYS A C 2176 O O . CYS A 331 ? 2.5911 1.2610 1.8386 0.3097 0.2877 0.1146 344 CYS A O 2177 C CB . CYS A 331 ? 3.0222 1.5462 2.2556 0.3041 0.3045 0.1538 344 CYS A CB 2178 S SG . CYS A 331 ? 2.4627 1.0365 1.7589 0.2918 0.3038 0.1155 344 CYS A SG 2179 N N . ALA A 332 ? 2.9360 1.5477 2.1202 0.2793 0.3195 0.1270 345 ALA A N 2180 C CA . ALA A 332 ? 2.9283 1.5917 2.1154 0.2604 0.3276 0.1031 345 ALA A CA 2181 C C . ALA A 332 ? 2.9218 1.6362 2.1057 0.2719 0.3144 0.0973 345 ALA A C 2182 O O . ALA A 332 ? 2.7725 1.5403 1.9984 0.2712 0.3039 0.0784 345 ALA A O 2183 C CB . ALA A 332 ? 2.9065 1.5473 2.0493 0.2377 0.3499 0.1055 345 ALA A CB 2184 N N . ASP A 333 ? 2.9597 1.6586 2.0950 0.2815 0.3140 0.1139 346 ASP A N 2185 C CA . ASP A 333 ? 2.8721 1.6146 1.9968 0.2917 0.3027 0.1093 346 ASP A CA 2186 C C . ASP A 333 ? 2.8130 1.5899 1.9857 0.3104 0.2813 0.1033 346 ASP A C 2187 O O . ASP A 333 ? 2.7286 1.5600 1.9361 0.3033 0.2752 0.0832 346 ASP A O 2188 C CB . ASP A 333 ? 3.0331 1.7459 2.1029 0.3048 0.3008 0.1318 346 ASP A CB 2189 C CG . ASP A 333 ? 3.1506 1.8708 2.1744 0.2890 0.3149 0.1258 346 ASP A CG 2190 O OD1 . ASP A 333 ? 3.1769 1.9143 2.2064 0.2657 0.3299 0.1079 346 ASP A OD1 2191 O OD2 . ASP A 333 ? 3.1864 1.8971 2.1702 0.2997 0.3100 0.1392 346 ASP A OD2 2192 N N . PRO A 334 ? 2.9614 1.7078 2.1414 0.3326 0.2693 0.1211 347 PRO A N 2193 C CA . PRO A 334 ? 2.9541 1.7348 2.1780 0.3514 0.2490 0.1150 347 PRO A CA 2194 C C . PRO A 334 ? 2.8961 1.7120 2.1789 0.3395 0.2475 0.0904 347 PRO A C 2195 O O . PRO A 334 ? 2.9231 1.7939 2.2371 0.3403 0.2362 0.0745 347 PRO A O 2196 C CB . PRO A 334 ? 3.0592 1.7921 2.2842 0.3731 0.2396 0.1394 347 PRO A CB 2197 C CG . PRO A 334 ? 3.1740 1.8499 2.3735 0.3602 0.2558 0.1529 347 PRO A CG 2198 C CD . PRO A 334 ? 3.1525 1.8350 2.3082 0.3400 0.2724 0.1476 347 PRO A CD 2199 N N . ALA A 335 ? 2.8235 1.6100 2.1222 0.3274 0.2579 0.0872 348 ALA A N 2200 C CA . ALA A 335 ? 2.7335 1.5437 2.0757 0.3181 0.2601 0.0646 348 ALA A CA 2201 C C . ALA A 335 ? 2.5559 1.4204 1.8978 0.3008 0.2653 0.0452 348 ALA A C 2202 O O . ALA A 335 ? 2.4355 1.3360 1.8064 0.3030 0.2599 0.0298 348 ALA A O 2203 C CB . ALA A 335 ? 2.7907 1.5563 2.1361 0.3054 0.2746 0.0644 348 ALA A CB 2204 N N . LEU A 336 ? 2.4187 1.2892 1.7292 0.2833 0.2752 0.0471 349 LEU A N 2205 C CA . LEU A 336 ? 2.3640 1.2839 1.6749 0.2656 0.2796 0.0318 349 LEU A CA 2206 C C . LEU A 336 ? 2.4188 1.3853 1.7356 0.2774 0.2632 0.0291 349 LEU A C 2207 O O . LEU A 336 ? 2.3770 1.3875 1.7127 0.2684 0.2606 0.0158 349 LEU A O 2208 C CB . LEU A 336 ? 2.2632 1.1782 1.5400 0.2445 0.2938 0.0347 349 LEU A CB 2209 C CG . LEU A 336 ? 2.0975 1.0626 1.3766 0.2247 0.2977 0.0221 349 LEU A CG 2210 C CD1 . LEU A 336 ? 1.9754 0.9621 1.2914 0.2133 0.3015 0.0063 349 LEU A CD1 2211 C CD2 . LEU A 336 ? 2.1720 1.1291 1.4185 0.2046 0.3122 0.0255 349 LEU A CD2 2212 N N . ASP A 337 ? 2.4616 1.4182 1.7639 0.2971 0.2511 0.0431 350 ASP A N 2213 C CA . ASP A 337 ? 2.4679 1.4661 1.7748 0.3099 0.2348 0.0413 350 ASP A CA 2214 C C . ASP A 337 ? 2.5440 1.5620 1.8924 0.3222 0.2248 0.0310 350 ASP A C 2215 O O . ASP A 337 ? 2.5525 1.6163 1.9176 0.3178 0.2187 0.0192 350 ASP A O 2216 C CB . ASP A 337 ? 2.5151 1.4895 1.7859 0.3304 0.2273 0.0605 350 ASP A CB 2217 C CG . ASP A 337 ? 2.6047 1.5479 1.8113 0.3227 0.2431 0.0710 350 ASP A CG 2218 O OD1 . ASP A 337 ? 2.5905 1.5477 1.7927 0.2987 0.2555 0.0610 350 ASP A OD1 2219 O OD2 . ASP A 337 ? 2.6896 1.5963 1.8524 0.3402 0.2422 0.0893 350 ASP A OD2 2220 N N . PHE A 338 ? 2.5877 1.5706 1.9542 0.3367 0.2229 0.0361 351 PHE A N 2221 C CA . PHE A 338 ? 2.5506 1.5477 1.9582 0.3478 0.2155 0.0249 351 PHE A CA 2222 C C . PHE A 338 ? 2.5042 1.5311 1.9341 0.3282 0.2234 0.0048 351 PHE A C 2223 O O . PHE A 338 ? 2.4665 1.5304 1.9244 0.3316 0.2152 -0.0073 351 PHE A O 2224 C CB . PHE A 338 ? 2.5672 1.5154 1.9907 0.3630 0.2149 0.0333 351 PHE A CB 2225 C CG . PHE A 338 ? 2.5235 1.4840 1.9899 0.3755 0.2076 0.0210 351 PHE A CG 2226 C CD1 . PHE A 338 ? 2.5131 1.4874 1.9957 0.3986 0.1916 0.0255 351 PHE A CD1 2227 C CD2 . PHE A 338 ? 2.5279 1.4881 2.0190 0.3639 0.2168 0.0043 351 PHE A CD2 2228 C CE1 . PHE A 338 ? 2.5147 1.5015 2.0375 0.4097 0.1856 0.0131 351 PHE A CE1 2229 C CE2 . PHE A 338 ? 2.5480 1.5202 2.0783 0.3752 0.2103 -0.0082 351 PHE A CE2 2230 C CZ . PHE A 338 ? 2.5423 1.5277 2.0888 0.3981 0.1950 -0.0041 351 PHE A CZ 2231 N N . LEU A 339 ? 2.4330 1.4441 1.8515 0.3074 0.2391 0.0019 352 LEU A N 2232 C CA . LEU A 339 ? 2.2806 1.3167 1.7206 0.2882 0.2468 -0.0151 352 LEU A CA 2233 C C . LEU A 339 ? 2.2021 1.2954 1.6488 0.2799 0.2387 -0.0228 352 LEU A C 2234 O O . LEU A 339 ? 2.0666 1.1902 1.5450 0.2816 0.2316 -0.0349 352 LEU A O 2235 C CB . LEU A 339 ? 2.2112 1.2242 1.6331 0.2662 0.2648 -0.0148 352 LEU A CB 2236 C CG . LEU A 339 ? 2.1391 1.1490 1.5873 0.2530 0.2748 -0.0294 352 LEU A CG 2237 C CD1 . LEU A 339 ? 2.1586 1.1694 1.5907 0.2262 0.2911 -0.0316 352 LEU A CD1 2238 C CD2 . LEU A 339 ? 1.9368 0.9889 1.4221 0.2552 0.2653 -0.0448 352 LEU A CD2 2239 N N . VAL A 340 ? 2.2757 1.3822 1.6929 0.2704 0.2395 -0.0152 353 VAL A N 2240 C CA . VAL A 340 ? 2.2180 1.3754 1.6407 0.2578 0.2328 -0.0206 353 VAL A CA 2241 C C . VAL A 340 ? 2.1794 1.3696 1.6112 0.2736 0.2146 -0.0204 353 VAL A C 2242 O O . VAL A 340 ? 2.1608 1.3917 1.6174 0.2679 0.2067 -0.0296 353 VAL A O 2243 C CB . VAL A 340 ? 2.1319 1.2913 1.5224 0.2409 0.2399 -0.0127 353 VAL A CB 2244 C CG1 . VAL A 340 ? 2.1605 1.3311 1.5632 0.2153 0.2517 -0.0206 353 VAL A CG1 2245 C CG2 . VAL A 340 ? 2.1150 1.2274 1.4696 0.2479 0.2482 0.0000 353 VAL A CG2 2246 N N . GLU A 341 ? 2.2107 1.3828 1.6236 0.2935 0.2078 -0.0095 354 GLU A N 2247 C CA . GLU A 341 ? 2.2334 1.4339 1.6553 0.3105 0.1907 -0.0093 354 GLU A CA 2248 C C . GLU A 341 ? 2.2482 1.4517 1.7077 0.3260 0.1841 -0.0178 354 GLU A C 2249 O O . GLU A 341 ? 2.2117 1.4537 1.6974 0.3244 0.1759 -0.0282 354 GLU A O 2250 C CB . GLU A 341 ? 2.2935 1.4779 1.6822 0.3261 0.1846 0.0054 354 GLU A CB 2251 N N . LYS A 342 ? 2.3643 1.5264 1.8279 0.3406 0.1873 -0.0127 355 LYS A N 2252 C CA . LYS A 342 ? 2.4591 1.6202 1.9581 0.3582 0.1801 -0.0190 355 LYS A CA 2253 C C . LYS A 342 ? 2.3563 1.5250 1.8913 0.3488 0.1862 -0.0363 355 LYS A C 2254 O O . LYS A 342 ? 2.2746 1.4824 1.8355 0.3473 0.1793 -0.0484 355 LYS A O 2255 C CB . LYS A 342 ? 1.5723 0.6863 1.0658 0.3803 0.1777 -0.0044 355 LYS A CB 2256 N N . ASP A 343 ? 2.4745 1.6076 2.0107 0.3412 0.1989 -0.0380 356 ASP A N 2257 C CA . ASP A 343 ? 2.5965 1.7284 2.1687 0.3395 0.2026 -0.0537 356 ASP A CA 2258 C C . ASP A 343 ? 2.7015 1.8649 2.2848 0.3155 0.2090 -0.0681 356 ASP A C 2259 O O . ASP A 343 ? 2.8069 1.9565 2.3753 0.2976 0.2212 -0.0675 356 ASP A O 2260 C CB . ASP A 343 ? 2.6246 1.7014 2.1965 0.3446 0.2117 -0.0494 356 ASP A CB 2261 N N . ASN A 344 ? 2.6578 1.8623 2.2697 0.3157 0.2007 -0.0808 357 ASN A N 2262 C CA . ASN A 344 ? 2.5329 1.7735 2.1583 0.2942 0.2032 -0.0931 357 ASN A CA 2263 C C . ASN A 344 ? 2.5320 1.7686 2.1884 0.2902 0.2087 -0.1099 357 ASN A C 2264 O O . ASN A 344 ? 2.4792 1.7445 2.1490 0.2732 0.2105 -0.1204 357 ASN A O 2265 C CB . ASN A 344 ? 2.3551 1.6461 1.9898 0.2935 0.1901 -0.0956 357 ASN A CB 2266 N N . GLU A 345 ? 2.5907 1.7916 2.2591 0.3062 0.2107 -0.1121 358 GLU A N 2267 C CA . GLU A 345 ? 2.6287 1.8219 2.3255 0.3045 0.2155 -0.1288 358 GLU A CA 2268 C C . GLU A 345 ? 2.6073 1.7691 2.2912 0.2888 0.2303 -0.1293 358 GLU A C 2269 O O . GLU A 345 ? 2.5268 1.6872 2.2300 0.2822 0.2354 -0.1437 358 GLU A O 2270 C CB . GLU A 345 ? 2.6715 1.8413 2.3916 0.3293 0.2100 -0.1324 358 GLU A CB 2271 N N . TYR A 346 ? 2.6266 1.7636 2.2772 0.2828 0.2374 -0.1139 359 TYR A N 2272 C CA . TYR A 346 ? 2.6388 1.7432 2.2751 0.2677 0.2527 -0.1129 359 TYR A CA 2273 C C . TYR A 346 ? 2.6869 1.8223 2.3223 0.2420 0.2597 -0.1199 359 TYR A C 2274 O O . TYR A 346 ? 2.6938 1.8254 2.3434 0.2314 0.2675 -0.1318 359 TYR A O 2275 C CB . TYR A 346 ? 2.5719 1.6396 2.1726 0.2690 0.2586 -0.0942 359 TYR A CB 2276 C CG . TYR A 346 ? 2.5423 1.5743 2.1284 0.2531 0.2753 -0.0930 359 TYR A CG 2277 C CD1 . TYR A 346 ? 2.4468 1.4998 2.0282 0.2283 0.2854 -0.0987 359 TYR A CD1 2278 C CD2 . TYR A 346 ? 2.6024 1.5791 2.1805 0.2628 0.2807 -0.0852 359 TYR A CD2 2279 C CE1 . TYR A 346 ? 2.4736 1.4952 2.0423 0.2132 0.3014 -0.0981 359 TYR A CE1 2280 C CE2 . TYR A 346 ? 2.5922 1.5355 2.1570 0.2474 0.2962 -0.0841 359 TYR A CE2 2281 C CZ . TYR A 346 ? 2.5313 1.4980 2.0911 0.2226 0.3071 -0.0912 359 TYR A CZ 2282 O OH . TYR A 346 ? 2.5275 1.4620 2.0750 0.2069 0.3232 -0.0907 359 TYR A OH 2283 N N . CYS A 347 ? 2.7246 1.8883 2.3423 0.2318 0.2571 -0.1114 360 CYS A N 2284 C CA . CYS A 347 ? 2.7343 1.9246 2.3505 0.2072 0.2635 -0.1150 360 CYS A CA 2285 C C . CYS A 347 ? 2.8076 2.0497 2.4500 0.2022 0.2525 -0.1255 360 CYS A C 2286 O O . CYS A 347 ? 2.8163 2.0878 2.4588 0.2075 0.2404 -0.1211 360 CYS A O 2287 C CB . CYS A 347 ? 2.6600 1.8489 2.2431 0.1962 0.2683 -0.1000 360 CYS A CB 2288 S SG . CYS A 347 ? 2.7423 1.9331 2.3184 0.1666 0.2848 -0.1020 360 CYS A SG 2289 N N . VAL A 348 ? 2.8680 2.1198 2.5323 0.1922 0.2567 -0.1394 361 VAL A N 2290 C CA . VAL A 348 ? 2.8974 2.1970 2.5834 0.1817 0.2489 -0.1483 361 VAL A CA 2291 C C . VAL A 348 ? 2.8626 2.1710 2.5411 0.1568 0.2591 -0.1461 361 VAL A C 2292 O O . VAL A 348 ? 2.9148 2.2019 2.5937 0.1473 0.2721 -0.1514 361 VAL A O 2293 C CB . VAL A 348 ? 2.9464 2.2536 2.6632 0.1885 0.2455 -0.1661 361 VAL A CB 2294 C CG1 . VAL A 348 ? 2.9050 2.2633 2.6431 0.1830 0.2335 -0.1737 361 VAL A CG1 2295 C CG2 . VAL A 348 ? 2.9860 2.2686 2.7098 0.2132 0.2405 -0.1686 361 VAL A CG2 2296 N N . CYS A 349 ? 2.7319 2.0708 2.4042 0.1464 0.2534 -0.1382 362 CYS A N 2297 C CA . CYS A 349 ? 2.6499 1.9997 2.3176 0.1232 0.2620 -0.1351 362 CYS A CA 2298 C C . CYS A 349 ? 2.6312 2.0277 2.3243 0.1128 0.2523 -0.1422 362 CYS A C 2299 O O . CYS A 349 ? 2.6703 2.0968 2.3675 0.1147 0.2391 -0.1379 362 CYS A O 2300 C CB . CYS A 349 ? 2.6043 1.9469 2.2434 0.1185 0.2642 -0.1192 362 CYS A CB 2301 S SG . CYS A 349 ? 2.2586 1.5496 1.8675 0.1124 0.2849 -0.1118 362 CYS A SG 2302 N N . GLU A 350 ? 2.5836 1.9852 2.2936 0.1015 0.2590 -0.1530 363 GLU A N 2303 C CA . GLU A 350 ? 2.5021 1.9443 2.2381 0.0943 0.2499 -0.1618 363 GLU A CA 2304 C C . GLU A 350 ? 2.4318 1.9076 2.1700 0.0793 0.2437 -0.1536 363 GLU A C 2305 O O . GLU A 350 ? 2.3532 1.8203 2.0748 0.0686 0.2508 -0.1432 363 GLU A O 2306 C CB . GLU A 350 ? 2.4787 1.9153 2.2293 0.0851 0.2601 -0.1744 363 GLU A CB 2307 N N . MET A 351 ? 2.3928 1.9062 2.1521 0.0793 0.2301 -0.1589 364 MET A N 2308 C CA . MET A 351 ? 2.2949 1.8420 2.0612 0.0675 0.2215 -0.1525 364 MET A CA 2309 C C . MET A 351 ? 2.2914 1.8471 2.0659 0.0453 0.2313 -0.1530 364 MET A C 2310 O O . MET A 351 ? 2.3838 1.9477 2.1749 0.0394 0.2346 -0.1632 364 MET A O 2311 C CB . MET A 351 ? 2.1958 1.7779 1.9830 0.0751 0.2045 -0.1591 364 MET A CB 2312 N N . PRO A 352 ? 2.1693 1.7237 1.9328 0.0329 0.2361 -0.1425 365 PRO A N 2313 C CA . PRO A 352 ? 2.1844 1.7482 1.9570 0.0110 0.2459 -0.1426 365 PRO A CA 2314 C C . PRO A 352 ? 2.2375 1.8427 2.0363 0.0021 0.2349 -0.1458 365 PRO A C 2315 O O . PRO A 352 ? 2.2584 1.8856 2.0640 0.0110 0.2189 -0.1442 365 PRO A O 2316 C CB . PRO A 352 ? 2.1062 1.6588 1.8593 0.0040 0.2508 -0.1299 365 PRO A CB 2317 C CG . PRO A 352 ? 2.1383 1.6638 1.8670 0.0217 0.2494 -0.1242 365 PRO A CG 2318 C CD . PRO A 352 ? 2.0991 1.6387 1.8391 0.0392 0.2345 -0.1303 365 PRO A CD 2319 N N . CYS A 353 ? 2.2856 1.9009 2.0995 -0.0151 0.2438 -0.1508 366 CYS A N 2320 C CA . CYS A 353 ? 2.2669 1.9202 2.1061 -0.0253 0.2350 -0.1534 366 CYS A CA 2321 C C . CYS A 353 ? 2.1285 1.8004 1.9712 -0.0364 0.2305 -0.1438 366 CYS A C 2322 O O . CYS A 353 ? 2.0256 1.7249 1.8804 -0.0341 0.2157 -0.1413 366 CYS A O 2323 C CB . CYS A 353 ? 2.3541 2.0122 2.2099 -0.0389 0.2463 -0.1635 366 CYS A CB 2324 S SG . CYS A 353 ? 2.8735 2.5003 2.7223 -0.0286 0.2569 -0.1754 366 CYS A SG 2325 N N . ASN A 354 ? 2.1417 1.7979 1.9740 -0.0484 0.2437 -0.1390 367 ASN A N 2326 C CA . ASN A 354 ? 2.2510 1.9228 2.0876 -0.0601 0.2413 -0.1313 367 ASN A CA 2327 C C . ASN A 354 ? 2.2206 1.8736 2.0322 -0.0498 0.2378 -0.1211 367 ASN A C 2328 O O . ASN A 354 ? 2.3259 1.9457 2.1139 -0.0471 0.2496 -0.1182 367 ASN A O 2329 C CB . ASN A 354 ? 2.5107 2.1780 2.3519 -0.0805 0.2587 -0.1331 367 ASN A CB 2330 C CG . ASN A 354 ? 2.6839 2.3880 2.5548 -0.0964 0.2551 -0.1362 367 ASN A CG 2331 O OD1 . ASN A 354 ? 2.6643 2.3944 2.5479 -0.0945 0.2404 -0.1328 367 ASN A OD1 2332 N ND2 . ASN A 354 ? 2.8886 2.5951 2.7712 -0.1120 0.2691 -0.1431 367 ASN A ND2 2333 N N . VAL A 355 ? 2.0829 1.7560 1.8988 -0.0433 0.2216 -0.1160 368 VAL A N 2334 C CA . VAL A 355 ? 1.9332 1.5907 1.7261 -0.0329 0.2169 -0.1068 368 VAL A CA 2335 C C . VAL A 355 ? 1.9314 1.6111 1.7316 -0.0366 0.2055 -0.1006 368 VAL A C 2336 O O . VAL A 355 ? 1.9150 1.6256 1.7355 -0.0347 0.1911 -0.1027 368 VAL A O 2337 C CB . VAL A 355 ? 1.7540 1.4031 1.5361 -0.0115 0.2075 -0.1077 368 VAL A CB 2338 C CG1 . VAL A 355 ? 1.7077 1.3536 1.4736 -0.0007 0.1976 -0.0988 368 VAL A CG1 2339 C CG2 . VAL A 355 ? 1.7727 1.3881 1.5384 -0.0059 0.2212 -0.1112 368 VAL A CG2 2340 N N . THR A 356 ? 1.8959 1.5586 1.6788 -0.0416 0.2120 -0.0933 369 THR A N 2341 C CA . THR A 356 ? 1.9245 1.6046 1.7126 -0.0439 0.2017 -0.0881 369 THR A CA 2342 C C . THR A 356 ? 1.8945 1.5601 1.6593 -0.0274 0.1936 -0.0812 369 THR A C 2343 O O . THR A 356 ? 1.9496 1.5823 1.6873 -0.0203 0.2023 -0.0773 369 THR A O 2344 C CB . THR A 356 ? 2.0374 1.7154 1.8281 -0.0631 0.2133 -0.0863 369 THR A CB 2345 O OG1 . THR A 356 ? 2.1024 1.8153 1.9251 -0.0754 0.2083 -0.0911 369 THR A OG1 2346 C CG2 . THR A 356 ? 2.0224 1.6906 1.7963 -0.0604 0.2099 -0.0787 369 THR A CG2 2347 N N . ARG A 357 ? 1.7543 1.4450 1.5301 -0.0215 0.1771 -0.0800 370 ARG A N 2348 C CA . ARG A 357 ? 1.6557 1.3403 1.4146 -0.0059 0.1669 -0.0746 370 ARG A CA 2349 C C . ARG A 357 ? 1.6864 1.3922 1.4566 -0.0112 0.1580 -0.0726 370 ARG A C 2350 O O . ARG A 357 ? 1.7134 1.4491 1.5106 -0.0195 0.1519 -0.0769 370 ARG A O 2351 C CB . ARG A 357 ? 1.6638 1.3648 1.4313 0.0097 0.1532 -0.0787 370 ARG A CB 2352 C CG . ARG A 357 ? 1.8279 1.5432 1.5939 0.0224 0.1372 -0.0757 370 ARG A CG 2353 C CD . ARG A 357 ? 1.9719 1.7087 1.7518 0.0347 0.1241 -0.0813 370 ARG A CD 2354 N NE . ARG A 357 ? 2.3140 2.0286 2.0793 0.0450 0.1300 -0.0829 370 ARG A NE 2355 C CZ . ARG A 357 ? 2.4853 2.2120 2.2650 0.0502 0.1263 -0.0910 370 ARG A CZ 2356 N NH1 . ARG A 357 ? 2.5126 2.2727 2.3197 0.0459 0.1165 -0.0973 370 ARG A NH1 2357 N NH2 . ARG A 357 ? 2.4854 2.1900 2.2519 0.0601 0.1324 -0.0930 370 ARG A NH2 2358 N N . TYR A 358 ? 1.7285 1.4192 1.4785 -0.0062 0.1571 -0.0665 371 TYR A N 2359 C CA . TYR A 358 ? 1.7439 1.4559 1.5052 -0.0091 0.1474 -0.0661 371 TYR A CA 2360 C C . TYR A 358 ? 1.6784 1.4011 1.4357 0.0079 0.1317 -0.0644 371 TYR A C 2361 O O . TYR A 358 ? 1.8129 1.5111 1.5434 0.0186 0.1332 -0.0587 371 TYR A O 2362 C CB . TYR A 358 ? 1.7716 1.4630 1.5180 -0.0201 0.1590 -0.0623 371 TYR A CB 2363 C CG . TYR A 358 ? 1.7955 1.4835 1.5516 -0.0393 0.1737 -0.0652 371 TYR A CG 2364 C CD1 . TYR A 358 ? 1.8722 1.5865 1.6542 -0.0537 0.1724 -0.0693 371 TYR A CD1 2365 C CD2 . TYR A 358 ? 1.8128 1.4728 1.5536 -0.0431 0.1893 -0.0642 371 TYR A CD2 2366 C CE1 . TYR A 358 ? 1.9279 1.6416 1.7208 -0.0719 0.1860 -0.0725 371 TYR A CE1 2367 C CE2 . TYR A 358 ? 1.8388 1.4976 1.5900 -0.0611 0.2032 -0.0677 371 TYR A CE2 2368 C CZ . TYR A 358 ? 1.9359 1.6221 1.7133 -0.0757 0.2015 -0.0718 371 TYR A CZ 2369 O OH . TYR A 358 ? 2.0486 1.7355 1.8377 -0.0941 0.2156 -0.0757 371 TYR A OH 2370 N N . GLY A 359 ? 1.4292 1.1879 1.2123 0.0102 0.1174 -0.0690 372 GLY A N 2371 C CA . GLY A 359 ? 1.4832 1.2557 1.2662 0.0245 0.1030 -0.0685 372 GLY A CA 2372 C C . GLY A 359 ? 1.6352 1.4094 1.4133 0.0229 0.1006 -0.0664 372 GLY A C 2373 O O . GLY A 359 ? 1.7802 1.5642 1.5709 0.0103 0.1038 -0.0686 372 GLY A O 2374 N N . LYS A 360 ? 1.6731 1.4384 1.4337 0.0355 0.0952 -0.0625 373 LYS A N 2375 C CA . LYS A 360 ? 1.6375 1.3977 1.3875 0.0349 0.0951 -0.0606 373 LYS A CA 2376 C C . LYS A 360 ? 1.4915 1.2730 1.2476 0.0460 0.0810 -0.0616 373 LYS A C 2377 O O . LYS A 360 ? 1.4916 1.2753 1.2447 0.0582 0.0734 -0.0594 373 LYS A O 2378 C CB . LYS A 360 ? 1.5377 1.2543 1.2504 0.0379 0.1072 -0.0530 373 LYS A CB 2379 C CG . LYS A 360 ? 1.4624 1.1505 1.1622 0.0310 0.1223 -0.0503 373 LYS A CG 2380 C CD . LYS A 360 ? 1.6197 1.2683 1.2826 0.0431 0.1289 -0.0421 373 LYS A CD 2381 C CE . LYS A 360 ? 1.7542 1.3876 1.4118 0.0450 0.1366 -0.0415 373 LYS A CE 2382 N NZ . LYS A 360 ? 1.9254 1.5185 1.5569 0.0382 0.1555 -0.0368 373 LYS A NZ 2383 N N . GLU A 361 ? 1.3996 1.1958 1.1634 0.0416 0.0781 -0.0649 374 GLU A N 2384 C CA . GLU A 361 ? 1.4761 1.2902 1.2440 0.0508 0.0667 -0.0660 374 GLU A CA 2385 C C . GLU A 361 ? 1.4812 1.2807 1.2292 0.0514 0.0708 -0.0649 374 GLU A C 2386 O O . GLU A 361 ? 1.5525 1.3562 1.3061 0.0399 0.0765 -0.0691 374 GLU A O 2387 C CB . GLU A 361 ? 0.8626 0.7201 0.6675 0.0451 0.0570 -0.0740 374 GLU A CB 2388 N N . LEU A 362 ? 1.3851 1.1677 1.1093 0.0653 0.0676 -0.0593 375 LEU A N 2389 C CA . LEU A 362 ? 1.2999 1.0646 1.0002 0.0673 0.0722 -0.0580 375 LEU A CA 2390 C C . LEU A 362 ? 1.3663 1.1549 1.0741 0.0733 0.0621 -0.0620 375 LEU A C 2391 O O . LEU A 362 ? 1.4515 1.2598 1.1735 0.0812 0.0510 -0.0617 375 LEU A O 2392 C CB . LEU A 362 ? 1.1844 0.9067 0.8466 0.0793 0.0780 -0.0482 375 LEU A CB 2393 C CG . LEU A 362 ? 1.2276 0.9140 0.8702 0.0719 0.0933 -0.0436 375 LEU A CG 2394 C CD1 . LEU A 362 ? 1.3610 1.0419 1.0076 0.0748 0.0939 -0.0402 375 LEU A CD1 2395 C CD2 . LEU A 362 ? 1.2816 0.9293 0.8847 0.0816 0.0998 -0.0363 375 LEU A CD2 2396 N N . SER A 363 ? 1.3389 1.1262 1.0371 0.0686 0.0667 -0.0660 376 SER A N 2397 C CA . SER A 363 ? 1.3316 1.1391 1.0324 0.0736 0.0593 -0.0704 376 SER A CA 2398 C C . SER A 363 ? 1.5470 1.3389 1.2229 0.0707 0.0677 -0.0723 376 SER A C 2399 O O . SER A 363 ? 1.6561 1.4298 1.3220 0.0609 0.0788 -0.0723 376 SER A O 2400 C CB . SER A 363 ? 1.2000 1.0488 0.9369 0.0630 0.0539 -0.0799 376 SER A CB 2401 O OG . SER A 363 ? 1.2032 1.0584 0.9566 0.0499 0.0597 -0.0837 376 SER A OG 2402 N N . MET A 364 ? 1.5302 1.3291 1.1955 0.0788 0.0627 -0.0739 377 MET A N 2403 C CA . MET A 364 ? 1.4060 1.1888 1.0424 0.0779 0.0705 -0.0751 377 MET A CA 2404 C C . MET A 364 ? 1.2920 1.1109 0.9422 0.0728 0.0659 -0.0855 377 MET A C 2405 O O . MET A 364 ? 1.2288 1.0743 0.9038 0.0742 0.0565 -0.0885 377 MET A O 2406 C CB . MET A 364 ? 1.2695 1.0197 0.8703 0.0956 0.0699 -0.0653 377 MET A CB 2407 C CG . MET A 364 ? 0.6252 0.3471 0.2179 0.1068 0.0690 -0.0543 377 MET A CG 2408 S SD . MET A 364 ? 2.5205 2.1916 2.0647 0.1226 0.0758 -0.0430 377 MET A SD 2409 C CE . MET A 364 ? 1.7642 1.4011 1.3031 0.1148 0.0879 -0.0361 377 MET A CE 2410 N N . VAL A 365 ? 1.3987 1.2185 1.0333 0.0655 0.0732 -0.0911 378 VAL A N 2411 C CA . VAL A 365 ? 1.4504 1.3012 1.0894 0.0619 0.0699 -0.1007 378 VAL A CA 2412 C C . VAL A 365 ? 1.5107 1.3441 1.1121 0.0632 0.0775 -0.0999 378 VAL A C 2413 O O . VAL A 365 ? 1.5766 1.3779 1.1561 0.0620 0.0869 -0.0940 378 VAL A O 2414 C CB . VAL A 365 ? 1.3333 1.2213 1.0043 0.0469 0.0705 -0.1131 378 VAL A CB 2415 C CG1 . VAL A 365 ? 1.3502 1.2598 1.0569 0.0448 0.0625 -0.1146 378 VAL A CG1 2416 C CG2 . VAL A 365 ? 1.2593 1.1368 0.9286 0.0387 0.0793 -0.1140 378 VAL A CG2 2417 N N . LYS A 366 ? 1.4264 1.2778 1.0175 0.0649 0.0743 -0.1047 379 LYS A N 2418 C CA . LYS A 366 ? 1.3149 1.1527 0.8677 0.0657 0.0814 -0.1034 379 LYS A CA 2419 C C . LYS A 366 ? 1.4825 1.3262 1.0343 0.0516 0.0918 -0.1101 379 LYS A C 2420 O O . LYS A 366 ? 1.4644 1.3377 1.0463 0.0425 0.0904 -0.1197 379 LYS A O 2421 C CB . LYS A 366 ? 1.0213 0.8801 0.5624 0.0691 0.0755 -0.1074 379 LYS A CB 2422 N N . ILE A 367 ? 1.5573 1.3692 1.0744 0.0513 0.1020 -0.1037 380 ILE A N 2423 C CA . ILE A 367 ? 1.5145 1.3284 1.0197 0.0398 0.1126 -0.1084 380 ILE A CA 2424 C C . ILE A 367 ? 1.5537 1.3453 1.0124 0.0436 0.1193 -0.1015 380 ILE A C 2425 O O . ILE A 367 ? 1.6417 1.3968 1.0781 0.0528 0.1209 -0.0901 380 ILE A O 2426 C CB . ILE A 367 ? 1.5488 1.3345 1.0618 0.0314 0.1215 -0.1049 380 ILE A CB 2427 C CG1 . ILE A 367 ? 1.5955 1.3793 1.0970 0.0182 0.1332 -0.1095 380 ILE A CG1 2428 C CG2 . ILE A 367 ? 1.5838 1.3211 1.0734 0.0381 0.1266 -0.0919 380 ILE A CG2 2429 C CD1 . ILE A 367 ? 1.6047 1.3560 1.1098 0.0066 0.1442 -0.1056 380 ILE A CD1 2430 N N . PRO A 368 ? 1.5562 1.3696 0.9989 0.0372 0.1234 -0.1075 381 PRO A N 2431 C CA . PRO A 368 ? 1.6093 1.4651 1.0756 0.0297 0.1214 -0.1209 381 PRO A CA 2432 C C . PRO A 368 ? 1.6660 1.5632 1.1553 0.0336 0.1087 -0.1295 381 PRO A C 2433 O O . PRO A 368 ? 1.8269 1.7208 1.3014 0.0396 0.1036 -0.1249 381 PRO A O 2434 C CB . PRO A 368 ? 1.5948 1.4548 1.0249 0.0254 0.1301 -0.1213 381 PRO A CB 2435 C CG . PRO A 368 ? 1.5404 1.3862 0.9371 0.0329 0.1284 -0.1117 381 PRO A CG 2436 C CD . PRO A 368 ? 1.6126 1.4141 1.0100 0.0399 0.1286 -0.1006 381 PRO A CD 2437 N N . SER A 369 ? 1.5895 1.5218 1.1124 0.0306 0.1040 -0.1410 382 SER A N 2438 C CA . SER A 369 ? 1.6299 1.6052 1.1696 0.0299 0.0954 -0.1516 382 SER A CA 2439 C C . SER A 369 ? 1.5598 1.5452 1.0649 0.0286 0.0993 -0.1525 382 SER A C 2440 O O . SER A 369 ? 1.4744 1.4456 0.9498 0.0297 0.1087 -0.1492 382 SER A O 2441 C CB . SER A 369 ? 1.7720 1.7712 1.3513 0.0341 0.0883 -0.1573 382 SER A CB 2442 O OG . SER A 369 ? 1.8652 1.8472 1.4225 0.0369 0.0971 -0.1575 382 SER A OG 2443 N N . LYS A 370 ? 1.6106 1.6118 1.1154 0.0222 0.0942 -0.1550 383 LYS A N 2444 C CA . LYS A 370 ? 1.7381 1.7520 1.2105 0.0194 0.0973 -0.1556 383 LYS A CA 2445 C C . LYS A 370 ? 1.7527 1.7950 1.2355 0.0288 0.0971 -0.1620 383 LYS A C 2446 O O . LYS A 370 ? 1.8683 1.9163 1.3187 0.0325 0.1017 -0.1607 383 LYS A O 2447 C CB . LYS A 370 ? 1.8329 1.8416 1.2933 0.0084 0.0931 -0.1561 383 LYS A CB 2448 C CG . LYS A 370 ? 1.9345 1.9561 1.3614 0.0010 0.0961 -0.1573 383 LYS A CG 2449 C CD . LYS A 370 ? 1.9959 1.9921 1.3946 -0.0021 0.0909 -0.1546 383 LYS A CD 2450 C CE . LYS A 370 ? 2.1287 2.1100 1.5030 0.0162 0.0842 -0.1440 383 LYS A CE 2451 N NZ . LYS A 370 ? 2.2493 2.2236 1.6017 0.0232 0.0745 -0.1412 383 LYS A NZ 2452 N N . ALA A 371 ? 1.7336 1.7758 1.2474 0.0433 0.0909 -0.1643 384 ALA A N 2453 C CA . ALA A 371 ? 1.9266 1.9374 1.4155 0.0588 0.0948 -0.1627 384 ALA A CA 2454 C C . ALA A 371 ? 1.9457 1.9384 1.4125 0.0438 0.1120 -0.1633 384 ALA A C 2455 O O . ALA A 371 ? 2.0181 2.0032 1.4567 0.0400 0.1221 -0.1659 384 ALA A O 2456 C CB . ALA A 371 ? 2.0079 1.9824 1.5101 0.0633 0.0906 -0.1610 384 ALA A CB 2457 N N . SER A 372 ? 1.8656 1.8455 1.3414 0.0350 0.1166 -0.1607 385 SER A N 2458 C CA . SER A 372 ? 1.8637 1.8119 1.3267 0.0192 0.1318 -0.1564 385 SER A CA 2459 C C . SER A 372 ? 1.9234 1.8526 1.3481 0.0139 0.1416 -0.1474 385 SER A C 2460 O O . SER A 372 ? 2.0289 1.9282 1.4373 0.0016 0.1550 -0.1426 385 SER A O 2461 C CB . SER A 372 ? 1.7763 1.7046 1.2710 0.0110 0.1323 -0.1543 385 SER A CB 2462 O OG . SER A 372 ? 1.6991 1.6118 1.1959 0.0129 0.1300 -0.1467 385 SER A OG 2463 N N . ALA A 373 ? 1.8054 1.7496 1.2143 0.0214 0.1352 -0.1445 386 ALA A N 2464 C CA . ALA A 373 ? 1.7720 1.6921 1.1396 0.0181 0.1431 -0.1327 386 ALA A CA 2465 C C . ALA A 373 ? 1.9212 1.8314 1.2569 0.0102 0.1572 -0.1304 386 ALA A C 2466 O O . ALA A 373 ? 1.9927 1.8653 1.3131 0.0008 0.1694 -0.1228 386 ALA A O 2467 C CB . ALA A 373 ? 1.7159 1.6596 1.0678 0.0237 0.1346 -0.1313 386 ALA A CB 2468 N N . LYS A 374 ? 1.9743 1.9169 1.2994 0.0140 0.1561 -0.1372 387 LYS A N 2469 C CA . LYS A 374 ? 1.9207 1.8572 1.2118 0.0064 0.1698 -0.1348 387 LYS A CA 2470 C C . LYS A 374 ? 1.8776 1.7892 1.1811 -0.0086 0.1820 -0.1384 387 LYS A C 2471 O O . LYS A 374 ? 1.8303 1.7240 1.1063 -0.0205 0.1966 -0.1336 387 LYS A O 2472 C CB . LYS A 374 ? 1.8147 1.7866 1.0925 0.0161 0.1656 -0.1417 387 LYS A CB 2473 N N . TYR A 375 ? 1.8360 1.7482 1.1812 -0.0101 0.1763 -0.1463 388 TYR A N 2474 C CA . TYR A 375 ? 1.8708 1.7622 1.2321 -0.0278 0.1872 -0.1499 388 TYR A CA 2475 C C . TYR A 375 ? 1.9635 1.8156 1.3095 -0.0375 0.1980 -0.1397 388 TYR A C 2476 O O . TYR A 375 ? 2.1103 1.9437 1.4403 -0.0529 0.2129 -0.1388 388 TYR A O 2477 C CB . TYR A 375 ? 1.8922 1.7905 1.3011 -0.0287 0.1785 -0.1573 388 TYR A CB 2478 C CG . TYR A 375 ? 2.0440 1.9222 1.4705 -0.0494 0.1898 -0.1598 388 TYR A CG 2479 C CD1 . TYR A 375 ? 2.1831 2.0692 1.6109 -0.0646 0.1995 -0.1682 388 TYR A CD1 2480 C CD2 . TYR A 375 ? 2.0427 1.8943 1.4835 -0.0547 0.1915 -0.1542 388 TYR A CD2 2481 C CE1 . TYR A 375 ? 2.2537 2.1253 1.6990 -0.0851 0.2100 -0.1717 388 TYR A CE1 2482 C CE2 . TYR A 375 ? 2.1109 1.9455 1.5672 -0.0742 0.2021 -0.1570 388 TYR A CE2 2483 C CZ . TYR A 375 ? 2.2255 2.0716 1.6849 -0.0897 0.2111 -0.1660 388 TYR A CZ 2484 O OH . TYR A 375 ? 2.2382 2.0710 1.7149 -0.1102 0.2215 -0.1699 388 TYR A OH 2485 N N . LEU A 376 ? 1.8793 1.7167 1.2295 -0.0288 0.1910 -0.1323 389 LEU A N 2486 C CA . LEU A 376 ? 1.8876 1.6800 1.2239 -0.0354 0.2005 -0.1220 389 LEU A CA 2487 C C . LEU A 376 ? 1.9330 1.7056 1.2193 -0.0340 0.2090 -0.1095 389 LEU A C 2488 O O . LEU A 376 ? 1.8262 1.5574 1.0928 -0.0406 0.2201 -0.1005 389 LEU A O 2489 C CB . LEU A 376 ? 1.7635 1.5437 1.1259 -0.0268 0.1901 -0.1189 389 LEU A CB 2490 C CG . LEU A 376 ? 1.6205 1.4128 1.0306 -0.0305 0.1835 -0.1273 389 LEU A CG 2491 C CD1 . LEU A 376 ? 1.5345 1.3610 0.9699 -0.0152 0.1659 -0.1313 389 LEU A CD1 2492 C CD2 . LEU A 376 ? 1.5809 1.3352 1.0030 -0.0378 0.1891 -0.1217 389 LEU A CD2 2493 N N . ALA A 377 ? 1.9913 1.7936 1.2563 -0.0251 0.2036 -0.1083 390 ALA A N 2494 C CA . ALA A 377 ? 2.1681 1.9582 1.3842 -0.0250 0.2114 -0.0951 390 ALA A CA 2495 C C . ALA A 377 ? 2.2716 2.0574 1.4669 -0.0401 0.2279 -0.0960 390 ALA A C 2496 O O . ALA A 377 ? 2.3544 2.1122 1.5135 -0.0470 0.2405 -0.0838 390 ALA A O 2497 C CB . ALA A 377 ? 2.2557 2.0832 1.4575 -0.0125 0.2000 -0.0937 390 ALA A CB 2498 N N . LYS A 378 ? 2.2132 2.0268 1.4306 -0.0451 0.2276 -0.1100 391 LYS A N 2499 C CA . LYS A 378 ? 2.1883 1.9952 1.3993 -0.0627 0.2431 -0.1148 391 LYS A CA 2500 C C . LYS A 378 ? 2.0435 1.8098 1.2679 -0.0775 0.2535 -0.1142 391 LYS A C 2501 O O . LYS A 378 ? 2.0668 1.8023 1.2621 -0.0872 0.2675 -0.1050 391 LYS A O 2502 C CB . LYS A 378 ? 2.2565 2.0976 1.4958 -0.0643 0.2386 -0.1308 391 LYS A CB 2503 C CG . LYS A 378 ? 2.3837 2.2169 1.6352 -0.0854 0.2521 -0.1398 391 LYS A CG 2504 C CD . LYS A 378 ? 2.4269 2.2824 1.7246 -0.0877 0.2438 -0.1548 391 LYS A CD 2505 C CE . LYS A 378 ? 2.4856 2.3356 1.7989 -0.1110 0.2570 -0.1642 391 LYS A CE 2506 N NZ . LYS A 378 ? 2.5253 2.3811 1.8051 -0.1217 0.2716 -0.1651 391 LYS A NZ 2507 N N . LYS A 379 ? 1.8717 1.6384 1.1397 -0.0787 0.2462 -0.1231 392 LYS A N 2508 C CA . LYS A 379 ? 1.8425 1.5792 1.1294 -0.0950 0.2557 -0.1260 392 LYS A CA 2509 C C . LYS A 379 ? 1.8956 1.5841 1.1582 -0.0984 0.2657 -0.1139 392 LYS A C 2510 O O . LYS A 379 ? 1.9453 1.6082 1.2058 -0.1155 0.2798 -0.1153 392 LYS A O 2511 C CB . LYS A 379 ? 1.8291 1.5760 1.1656 -0.0932 0.2441 -0.1341 392 LYS A CB 2512 C CG . LYS A 379 ? 1.7926 1.5081 1.1486 -0.1087 0.2524 -0.1351 392 LYS A CG 2513 C CD . LYS A 379 ? 1.7222 1.4570 1.1274 -0.1091 0.2414 -0.1429 392 LYS A CD 2514 C CE . LYS A 379 ? 1.7390 1.4467 1.1642 -0.1244 0.2490 -0.1434 392 LYS A CE 2515 N NZ . LYS A 379 ? 1.7938 1.5171 1.2600 -0.1180 0.2353 -0.1447 392 LYS A NZ 2516 N N . TYR A 380 ? 1.9630 1.6376 1.2099 -0.0827 0.2586 -0.1026 393 TYR A N 2517 C CA . TYR A 380 ? 2.0181 1.6437 1.2362 -0.0842 0.2688 -0.0897 393 TYR A CA 2518 C C . TYR A 380 ? 2.2159 1.8345 1.3819 -0.0806 0.2759 -0.0754 393 TYR A C 2519 O O . TYR A 380 ? 2.2115 1.7892 1.3492 -0.0807 0.2846 -0.0625 393 TYR A O 2520 C CB . TYR A 380 ? 1.7845 1.3872 1.0205 -0.0722 0.2595 -0.0855 393 TYR A CB 2521 C CG . TYR A 380 ? 1.7556 1.3659 1.0406 -0.0784 0.2542 -0.0967 393 TYR A CG 2522 C CD1 . TYR A 380 ? 1.7851 1.4384 1.1042 -0.0718 0.2395 -0.1058 393 TYR A CD1 2523 C CD2 . TYR A 380 ? 1.8119 1.3877 1.1086 -0.0916 0.2643 -0.0978 393 TYR A CD2 2524 C CE1 . TYR A 380 ? 1.8225 1.4851 1.1857 -0.0781 0.2346 -0.1139 393 TYR A CE1 2525 C CE2 . TYR A 380 ? 1.7620 1.3484 1.1034 -0.0987 0.2595 -0.1063 393 TYR A CE2 2526 C CZ . TYR A 380 ? 1.8533 1.4835 1.2273 -0.0919 0.2445 -0.1135 393 TYR A CZ 2527 O OH . TYR A 380 ? 1.9136 1.5565 1.3304 -0.0990 0.2397 -0.1200 393 TYR A OH 2528 N N . ASN A 381 ? 2.3304 1.9894 1.4841 -0.0773 0.2721 -0.0771 394 ASN A N 2529 C CA . ASN A 381 ? 2.5318 2.1949 1.6371 -0.0755 0.2781 -0.0630 394 ASN A CA 2530 C C . ASN A 381 ? 2.4846 2.1356 1.5627 -0.0596 0.2703 -0.0461 394 ASN A C 2531 O O . ASN A 381 ? 2.5208 2.1542 1.5562 -0.0611 0.2788 -0.0290 394 ASN A O 2532 C CB . ASN A 381 ? 2.8622 2.4969 1.9398 -0.0935 0.2987 -0.0567 394 ASN A CB 2533 C CG . ASN A 381 ? 3.1976 2.8449 2.2272 -0.0941 0.3056 -0.0419 394 ASN A CG 2534 O OD1 . ASN A 381 ? 3.1533 2.8396 2.1746 -0.0844 0.2962 -0.0415 394 ASN A OD1 2535 N ND2 . ASN A 381 ? 3.5669 3.1815 2.5644 -0.1060 0.3223 -0.0291 394 ASN A ND2 2536 N N . LYS A 382 ? 2.3936 2.0544 1.4960 -0.0448 0.2540 -0.0498 395 LYS A N 2537 C CA . LYS A 382 ? 2.2852 1.9380 1.3645 -0.0295 0.2449 -0.0351 395 LYS A CA 2538 C C . LYS A 382 ? 2.1705 1.8741 1.2558 -0.0191 0.2295 -0.0401 395 LYS A C 2539 O O . LYS A 382 ? 2.1708 1.9130 1.2773 -0.0227 0.2268 -0.0547 395 LYS A O 2540 C CB . LYS A 382 ? 2.2118 1.8286 1.3108 -0.0204 0.2395 -0.0339 395 LYS A CB 2541 N N . SER A 383 ? 2.1355 1.8382 1.2011 -0.0065 0.2197 -0.0280 396 SER A N 2542 C CA . SER A 383 ? 2.1974 1.9466 1.2679 0.0021 0.2047 -0.0327 396 SER A CA 2543 C C . SER A 383 ? 2.1268 1.8912 1.2463 0.0091 0.1917 -0.0486 396 SER A C 2544 O O . SER A 383 ? 2.1391 1.8735 1.2828 0.0107 0.1923 -0.0512 396 SER A O 2545 C CB . SER A 383 ? 2.4114 2.1515 1.4453 0.0120 0.1978 -0.0136 396 SER A CB 2546 O OG . SER A 383 ? 2.5027 2.1963 1.5378 0.0214 0.1961 -0.0046 396 SER A OG 2547 N N . GLU A 384 ? 2.1081 1.9201 1.2423 0.0128 0.1801 -0.0589 397 GLU A N 2548 C CA . GLU A 384 ? 2.1205 1.9483 1.2988 0.0195 0.1667 -0.0714 397 GLU A CA 2549 C C . GLU A 384 ? 2.1426 1.9349 1.3170 0.0308 0.1601 -0.0602 397 GLU A C 2550 O O . GLU A 384 ? 2.0636 1.8310 1.2652 0.0344 0.1592 -0.0627 397 GLU A O 2551 C CB . GLU A 384 ? 2.1682 2.0497 1.3560 0.0212 0.1557 -0.0821 397 GLU A CB 2552 C CG . GLU A 384 ? 2.2864 2.2045 1.4936 0.0162 0.1588 -0.0976 397 GLU A CG 2553 C CD . GLU A 384 ? 2.4924 2.4632 1.7113 0.0195 0.1473 -0.1094 397 GLU A CD 2554 O OE1 . GLU A 384 ? 2.5705 2.5461 1.7921 0.0208 0.1366 -0.1079 397 GLU A OE1 2555 O OE2 . GLU A 384 ? 2.5532 2.5547 1.7762 0.0215 0.1495 -0.1198 397 GLU A OE2 2556 N N . GLN A 385 ? 2.2856 2.0747 1.4245 0.0374 0.1556 -0.0468 398 GLN A N 2557 C CA . GLN A 385 ? 2.4356 2.1923 1.5688 0.0520 0.1479 -0.0356 398 GLN A CA 2558 C C . GLN A 385 ? 2.3864 2.0910 1.5214 0.0551 0.1570 -0.0289 398 GLN A C 2559 O O . GLN A 385 ? 2.3480 2.0309 1.5026 0.0668 0.1507 -0.0286 398 GLN A O 2560 C CB . GLN A 385 ? 2.6022 2.3571 1.6889 0.0576 0.1439 -0.0181 398 GLN A CB 2561 C CG . GLN A 385 ? 2.7177 2.4368 1.7940 0.0755 0.1362 -0.0045 398 GLN A CG 2562 C CD . GLN A 385 ? 2.9052 2.6188 1.9321 0.0799 0.1334 0.0163 398 GLN A CD 2563 O OE1 . GLN A 385 ? 3.0144 2.7612 2.0200 0.0706 0.1322 0.0181 398 GLN A OE1 2564 N NE2 . GLN A 385 ? 2.9219 2.5945 1.9297 0.0939 0.1321 0.0332 398 GLN A NE2 2565 N N . TYR A 386 ? 2.3440 2.0288 1.4582 0.0440 0.1723 -0.0238 399 TYR A N 2566 C CA . TYR A 386 ? 2.3065 1.9417 1.4215 0.0427 0.1834 -0.0193 399 TYR A CA 2567 C C . TYR A 386 ? 2.3264 1.9600 1.4908 0.0416 0.1807 -0.0340 399 TYR A C 2568 O O . TYR A 386 ? 2.4122 2.0111 1.5869 0.0496 0.1803 -0.0306 399 TYR A O 2569 C CB . TYR A 386 ? 2.2803 1.9025 1.3706 0.0267 0.2008 -0.0152 399 TYR A CB 2570 C CG . TYR A 386 ? 2.3228 1.8964 1.4176 0.0210 0.2138 -0.0139 399 TYR A CG 2571 C CD1 . TYR A 386 ? 2.2483 1.8193 1.3863 0.0161 0.2138 -0.0285 399 TYR A CD1 2572 C CD2 . TYR A 386 ? 2.4254 1.9569 1.4810 0.0190 0.2263 0.0028 399 TYR A CD2 2573 C CE1 . TYR A 386 ? 2.2376 1.7652 1.3792 0.0093 0.2257 -0.0277 399 TYR A CE1 2574 C CE2 . TYR A 386 ? 2.3909 1.8777 1.4503 0.0127 0.2389 0.0027 399 TYR A CE2 2575 C CZ . TYR A 386 ? 2.2941 1.7791 1.3965 0.0076 0.2386 -0.0132 399 TYR A CZ 2576 O OH . TYR A 386 ? 2.3011 1.7422 1.4070 0.0000 0.2511 -0.0136 399 TYR A OH 2577 N N . ILE A 387 ? 2.2009 1.8729 1.3952 0.0317 0.1789 -0.0494 400 ILE A N 2578 C CA . ILE A 387 ? 2.0727 1.7472 1.3132 0.0279 0.1766 -0.0614 400 ILE A CA 2579 C C . ILE A 387 ? 2.0716 1.7427 1.3372 0.0423 0.1633 -0.0610 400 ILE A C 2580 O O . ILE A 387 ? 2.0826 1.7289 1.3694 0.0433 0.1645 -0.0609 400 ILE A O 2581 C CB . ILE A 387 ? 1.9587 1.6809 1.2263 0.0185 0.1739 -0.0767 400 ILE A CB 2582 C CG1 . ILE A 387 ? 2.0430 1.7681 1.2834 0.0058 0.1874 -0.0764 400 ILE A CG1 2583 C CG2 . ILE A 387 ? 1.8889 1.6122 1.2013 0.0128 0.1727 -0.0865 400 ILE A CG2 2584 C CD1 . ILE A 387 ? 2.1081 1.7894 1.3395 -0.0056 0.2031 -0.0721 400 ILE A CD1 2585 N N . GLY A 388 ? 2.0414 1.7374 1.3036 0.0529 0.1510 -0.0603 401 GLY A N 2586 C CA . GLY A 388 ? 2.0240 1.7191 1.3094 0.0670 0.1381 -0.0600 401 GLY A CA 2587 C C . GLY A 388 ? 2.0051 1.6505 1.2741 0.0800 0.1403 -0.0469 401 GLY A C 2588 O O . GLY A 388 ? 1.9463 1.5823 1.2404 0.0895 0.1334 -0.0470 401 GLY A O 2589 N N . GLU A 389 ? 1.9615 1.5763 1.1873 0.0811 0.1498 -0.0349 402 GLU A N 2590 C CA . GLU A 389 ? 1.9776 1.5429 1.1855 0.0937 0.1534 -0.0226 402 GLU A CA 2591 C C . GLU A 389 ? 1.8769 1.4065 1.0952 0.0848 0.1660 -0.0237 402 GLU A C 2592 O O . GLU A 389 ? 1.8752 1.3769 1.1051 0.0944 0.1647 -0.0206 402 GLU A O 2593 C CB . GLU A 389 ? 2.1186 1.6640 1.2748 0.0998 0.1577 -0.0066 402 GLU A CB 2594 C CG . GLU A 389 ? 2.1543 1.7259 1.2962 0.1118 0.1439 -0.0014 402 GLU A CG 2595 C CD . GLU A 389 ? 2.3255 1.9041 1.4223 0.1051 0.1486 0.0105 402 GLU A CD 2596 O OE1 . GLU A 389 ? 2.3534 1.9051 1.4244 0.0959 0.1629 0.0190 402 GLU A OE1 2597 O OE2 . GLU A 389 ? 2.4188 2.0308 1.5062 0.1077 0.1381 0.0118 402 GLU A OE2 2598 N N . ASN A 390 ? 1.8223 1.3518 1.0342 0.0664 0.1785 -0.0275 403 ASN A N 2599 C CA . ASN A 390 ? 1.9368 1.4264 1.1496 0.0565 0.1927 -0.0267 403 ASN A CA 2600 C C . ASN A 390 ? 1.9342 1.4347 1.1904 0.0430 0.1939 -0.0386 403 ASN A C 2601 O O . ASN A 390 ? 1.9375 1.4037 1.1974 0.0356 0.2043 -0.0373 403 ASN A O 2602 C CB . ASN A 390 ? 2.1014 1.5717 1.2745 0.0448 0.2084 -0.0202 403 ASN A CB 2603 C CG . ASN A 390 ? 2.2105 1.6685 1.3386 0.0568 0.2076 -0.0044 403 ASN A CG 2604 O OD1 . ASN A 390 ? 2.2180 1.6423 1.3318 0.0719 0.2063 0.0059 403 ASN A OD1 2605 N ND2 . ASN A 390 ? 2.2481 1.7351 1.3532 0.0504 0.2080 -0.0013 403 ASN A ND2 2606 N N . ILE A 391 ? 1.8337 1.3823 1.1227 0.0395 0.1835 -0.0496 404 ILE A N 2607 C CA . ILE A 391 ? 1.8126 1.3774 1.1407 0.0251 0.1846 -0.0599 404 ILE A CA 2608 C C . ILE A 391 ? 1.8544 1.4326 1.2226 0.0321 0.1723 -0.0621 404 ILE A C 2609 O O . ILE A 391 ? 1.9218 1.5302 1.3041 0.0429 0.1585 -0.0643 404 ILE A O 2610 C CB . ILE A 391 ? 1.8148 1.4250 1.1539 0.0142 0.1832 -0.0711 404 ILE A CB 2611 C CG1 . ILE A 391 ? 1.8578 1.4542 1.1634 0.0017 0.1985 -0.0698 404 ILE A CG1 2612 C CG2 . ILE A 391 ? 1.8546 1.4898 1.2396 0.0043 0.1793 -0.0815 404 ILE A CG2 2613 C CD1 . ILE A 391 ? 1.8165 1.3801 1.1252 -0.0141 0.2131 -0.0705 404 ILE A CD1 2614 N N . LEU A 392 ? 1.7989 1.3558 1.1847 0.0247 0.1777 -0.0609 405 LEU A N 2615 C CA . LEU A 392 ? 1.7153 1.2888 1.1386 0.0291 0.1669 -0.0619 405 LEU A CA 2616 C C . LEU A 392 ? 1.7609 1.3466 1.2156 0.0105 0.1716 -0.0687 405 LEU A C 2617 O O . LEU A 392 ? 1.8091 1.3740 1.2526 -0.0042 0.1855 -0.0698 405 LEU A O 2618 C CB . LEU A 392 ? 1.6143 1.1504 1.0268 0.0422 0.1669 -0.0505 405 LEU A CB 2619 C CG . LEU A 392 ? 1.5610 1.0518 0.9624 0.0330 0.1819 -0.0447 405 LEU A CG 2620 C CD1 . LEU A 392 ? 1.5398 1.0467 0.9791 0.0185 0.1825 -0.0491 405 LEU A CD1 2621 C CD2 . LEU A 392 ? 1.5275 0.9785 0.9069 0.0496 0.1829 -0.0327 405 LEU A CD2 2622 N N . VAL A 393 ? 1.6933 1.3139 1.1869 0.0107 0.1603 -0.0734 406 VAL A N 2623 C CA . VAL A 393 ? 1.5829 1.2174 1.1077 -0.0058 0.1636 -0.0789 406 VAL A CA 2624 C C . VAL A 393 ? 1.5117 1.1528 1.0650 -0.0036 0.1570 -0.0756 406 VAL A C 2625 O O . VAL A 393 ? 1.5901 1.2650 1.1677 0.0048 0.1430 -0.0785 406 VAL A O 2626 C CB . VAL A 393 ? 1.4978 1.1786 1.0460 -0.0122 0.1574 -0.0906 406 VAL A CB 2627 C CG1 . VAL A 393 ? 1.4255 1.1187 1.0054 -0.0278 0.1602 -0.0949 406 VAL A CG1 2628 C CG2 . VAL A 393 ? 1.5221 1.2004 1.0436 -0.0176 0.1655 -0.0948 406 VAL A CG2 2629 N N . LEU A 394 ? 1.4853 1.0973 1.0370 -0.0128 0.1677 -0.0705 407 LEU A N 2630 C CA . LEU A 394 ? 1.5763 1.1918 1.1496 -0.0109 0.1634 -0.0663 407 LEU A CA 2631 C C . LEU A 394 ? 1.6100 1.2522 1.2196 -0.0267 0.1638 -0.0722 407 LEU A C 2632 O O . LEU A 394 ? 1.6888 1.3185 1.2988 -0.0440 0.1765 -0.0742 407 LEU A O 2633 C CB . LEU A 394 ? 1.6185 1.1867 1.1664 -0.0088 0.1745 -0.0560 407 LEU A CB 2634 C CG . LEU A 394 ? 1.6205 1.1898 1.1854 -0.0067 0.1722 -0.0512 407 LEU A CG 2635 C CD1 . LEU A 394 ? 1.4826 1.0934 1.0752 0.0047 0.1539 -0.0541 407 LEU A CD1 2636 C CD2 . LEU A 394 ? 1.7215 1.2448 1.2531 0.0038 0.1798 -0.0401 407 LEU A CD2 2637 N N . ASP A 395 ? 1.5062 1.1847 1.1457 -0.0208 0.1500 -0.0749 408 ASP A N 2638 C CA . ASP A 395 ? 1.3909 1.0982 1.0658 -0.0330 0.1480 -0.0800 408 ASP A CA 2639 C C . ASP A 395 ? 1.5242 1.2337 1.2144 -0.0305 0.1448 -0.0754 408 ASP A C 2640 O O . ASP A 395 ? 1.6325 1.3626 1.3347 -0.0175 0.1316 -0.0751 408 ASP A O 2641 C CB . ASP A 395 ? 1.3877 1.1384 1.0856 -0.0272 0.1337 -0.0875 408 ASP A CB 2642 C CG . ASP A 395 ? 1.6900 1.4593 1.4028 -0.0418 0.1375 -0.0953 408 ASP A CG 2643 O OD1 . ASP A 395 ? 1.7114 1.4964 1.4202 -0.0378 0.1332 -0.1008 408 ASP A OD1 2644 O OD2 . ASP A 395 ? 1.9004 1.6700 1.6297 -0.0576 0.1450 -0.0961 408 ASP A OD2 2645 N N . ILE A 396 ? 1.5829 1.2751 1.2751 -0.0438 0.1569 -0.0731 409 ILE A N 2646 C CA . ILE A 396 ? 1.5950 1.2958 1.3055 -0.0439 0.1546 -0.0707 409 ILE A CA 2647 C C . ILE A 396 ? 1.6798 1.4123 1.4261 -0.0586 0.1538 -0.0767 409 ILE A C 2648 O O . ILE A 396 ? 1.7478 1.4792 1.4999 -0.0756 0.1640 -0.0805 409 ILE A O 2649 C CB . ILE A 396 ? 1.5592 1.2224 1.2500 -0.0479 0.1686 -0.0642 409 ILE A CB 2650 C CG1 . ILE A 396 ? 1.5420 1.1683 1.1946 -0.0339 0.1715 -0.0569 409 ILE A CG1 2651 C CG2 . ILE A 396 ? 1.5734 1.2513 1.2842 -0.0463 0.1646 -0.0634 409 ILE A CG2 2652 C CD1 . ILE A 396 ? 1.4644 1.0510 1.0948 -0.0362 0.1861 -0.0497 409 ILE A CD1 2653 N N . PHE A 397 ? 1.6860 1.4461 1.4561 -0.0526 0.1423 -0.0775 410 PHE A N 2654 C CA . PHE A 397 ? 1.6658 1.4576 1.4699 -0.0647 0.1401 -0.0825 410 PHE A CA 2655 C C . PHE A 397 ? 1.5740 1.3830 1.3968 -0.0593 0.1321 -0.0813 410 PHE A C 2656 O O . PHE A 397 ? 1.4984 1.2970 1.3086 -0.0456 0.1274 -0.0774 410 PHE A O 2657 C CB . PHE A 397 ? 1.6530 1.4739 1.4722 -0.0636 0.1306 -0.0881 410 PHE A CB 2658 C CG . PHE A 397 ? 1.6761 1.5087 1.4903 -0.0439 0.1156 -0.0878 410 PHE A CG 2659 C CD1 . PHE A 397 ? 1.7483 1.5629 1.5351 -0.0337 0.1156 -0.0866 410 PHE A CD1 2660 C CD2 . PHE A 397 ? 1.6450 1.5076 1.4823 -0.0361 0.1020 -0.0890 410 PHE A CD2 2661 C CE1 . PHE A 397 ? 1.7325 1.5615 1.5174 -0.0167 0.1024 -0.0875 410 PHE A CE1 2662 C CE2 . PHE A 397 ? 1.6023 1.4773 1.4365 -0.0188 0.0888 -0.0897 410 PHE A CE2 2663 C CZ . PHE A 397 ? 1.6175 1.4777 1.4271 -0.0094 0.0890 -0.0895 410 PHE A CZ 2664 N N . PHE A 398 ? 1.5173 1.3533 1.3704 -0.0704 0.1310 -0.0849 411 PHE A N 2665 C CA . PHE A 398 ? 1.4054 1.2627 1.2787 -0.0654 0.1218 -0.0846 411 PHE A CA 2666 C C . PHE A 398 ? 1.2615 1.1521 1.1558 -0.0593 0.1072 -0.0872 411 PHE A C 2667 O O . PHE A 398 ? 1.3730 1.2775 1.2776 -0.0661 0.1071 -0.0906 411 PHE A O 2668 C CB . PHE A 398 ? 1.3086 1.1730 1.2014 -0.0815 0.1309 -0.0864 411 PHE A CB 2669 C CG . PHE A 398 ? 1.3941 1.2292 1.2686 -0.0831 0.1425 -0.0835 411 PHE A CG 2670 C CD1 . PHE A 398 ? 1.3712 1.1835 1.2343 -0.0969 0.1590 -0.0838 411 PHE A CD1 2671 C CD2 . PHE A 398 ? 1.6000 1.4302 1.4685 -0.0707 0.1372 -0.0811 411 PHE A CD2 2672 C CE1 . PHE A 398 ? 1.5830 1.3676 1.4290 -0.0982 0.1706 -0.0810 411 PHE A CE1 2673 C CE2 . PHE A 398 ? 1.6611 1.4645 1.5128 -0.0714 0.1482 -0.0789 411 PHE A CE2 2674 C CZ . PHE A 398 ? 1.6729 1.4530 1.5131 -0.0851 0.1652 -0.0786 411 PHE A CZ 2675 N N . GLU A 399 ? 1.7566 2.4546 2.1435 -0.4256 0.1466 0.3070 412 GLU A N 2676 C CA . GLU A 399 ? 1.6668 2.3595 2.0115 -0.4842 0.2037 0.2718 412 GLU A CA 2677 C C . GLU A 399 ? 1.8299 2.3987 2.1302 -0.4944 0.2355 0.2839 412 GLU A C 2678 O O . GLU A 399 ? 1.9718 2.4739 2.2217 -0.5261 0.2779 0.2891 412 GLU A O 2679 C CB . GLU A 399 ? 1.4800 2.2845 1.8374 -0.5138 0.2224 0.2074 412 GLU A CB 2680 C CG . GLU A 399 ? 1.4723 2.2844 1.8468 -0.4981 0.2150 0.1840 412 GLU A CG 2681 C CD . GLU A 399 ? 1.5733 2.4325 1.9276 -0.5516 0.2642 0.1190 412 GLU A CD 2682 O OE1 . GLU A 399 ? 1.5944 2.4956 1.9260 -0.6001 0.3006 0.0898 412 GLU A OE1 2683 O OE2 . GLU A 399 ? 1.5995 2.4520 1.9585 -0.5478 0.2686 0.0958 412 GLU A OE2 2684 N N . ALA A 400 ? 1.8565 2.3921 2.1726 -0.4633 0.2148 0.2911 413 ALA A N 2685 C CA . ALA A 400 ? 1.9185 2.3427 2.1939 -0.4654 0.2410 0.3037 413 ALA A CA 2686 C C . ALA A 400 ? 1.9780 2.3516 2.2777 -0.4153 0.1961 0.3492 413 ALA A C 2687 O O . ALA A 400 ? 2.0340 2.4550 2.3796 -0.3816 0.1487 0.3651 413 ALA A O 2688 C CB . ALA A 400 ? 1.9256 2.3559 2.1859 -0.4888 0.2738 0.2549 413 ALA A CB 2689 N N . LEU A 401 ? 1.9859 2.2621 2.2500 -0.4100 0.2134 0.3700 414 LEU A N 2690 C CA . LEU A 401 ? 2.0040 2.2368 2.2896 -0.3681 0.1757 0.4039 414 LEU A CA 2691 C C . LEU A 401 ? 2.0768 2.3206 2.3813 -0.3554 0.1672 0.3776 414 LEU A C 2692 O O . LEU A 401 ? 2.1295 2.3663 2.4657 -0.3208 0.1285 0.3961 414 LEU A O 2693 C CB . LEU A 401 ? 1.9514 2.0893 2.1947 -0.3623 0.1924 0.4396 414 LEU A CB 2694 C CG . LEU A 401 ? 1.8287 1.9601 2.0835 -0.3480 0.1662 0.4836 414 LEU A CG 2695 C CD1 . LEU A 401 ? 1.9071 1.9574 2.1136 -0.3453 0.1891 0.5132 414 LEU A CD1 2696 C CD2 . LEU A 401 ? 1.6256 1.7780 1.9321 -0.3116 0.1114 0.5050 414 LEU A CD2 2697 N N . ASN A 402 ? 2.0417 2.3041 2.3261 -0.3856 0.2047 0.3325 415 ASN A N 2698 C CA . ASN A 402 ? 1.9790 2.2669 2.2848 -0.3768 0.1971 0.3019 415 ASN A CA 2699 C C . ASN A 402 ? 1.8767 2.2506 2.2428 -0.3474 0.1471 0.2996 415 ASN A C 2700 O O . ASN A 402 ? 1.8890 2.3259 2.2758 -0.3458 0.1303 0.3039 415 ASN A O 2701 C CB . ASN A 402 ? 2.0730 2.3798 2.3472 -0.4211 0.2490 0.2488 415 ASN A CB 2702 C CG . ASN A 402 ? 2.0843 2.4785 2.3983 -0.4199 0.2350 0.2060 415 ASN A CG 2703 O OD1 . ASN A 402 ? 2.0799 2.4514 2.3985 -0.4064 0.2318 0.1950 415 ASN A OD1 2704 N ND2 . ASN A 402 ? 2.0765 2.5761 2.4183 -0.4329 0.2273 0.1807 415 ASN A ND2 2705 N N . TYR A 403 ? 1.8111 2.1829 2.2012 -0.3205 0.1240 0.2951 416 TYR A N 2706 C CA . TYR A 403 ? 1.7650 2.2147 2.2028 -0.2906 0.0841 0.2867 416 TYR A CA 2707 C C . TYR A 403 ? 1.6596 2.1128 2.1060 -0.2844 0.0867 0.2566 416 TYR A C 2708 O O . TYR A 403 ? 1.7194 2.0964 2.1422 -0.2880 0.1030 0.2605 416 TYR A O 2709 C CB . TYR A 403 ? 1.8370 2.2550 2.2962 -0.2487 0.0397 0.3342 416 TYR A CB 2710 C CG . TYR A 403 ? 1.9381 2.2778 2.3940 -0.2293 0.0296 0.3520 416 TYR A CG 2711 C CD1 . TYR A 403 ? 2.0259 2.2827 2.4536 -0.2352 0.0416 0.3805 416 TYR A CD1 2712 C CD2 . TYR A 403 ? 2.0196 2.3733 2.4992 -0.2042 0.0092 0.3388 416 TYR A CD2 2713 C CE1 . TYR A 403 ? 2.1024 2.2984 2.5276 -0.2179 0.0323 0.3939 416 TYR A CE1 2714 C CE2 . TYR A 403 ? 2.0987 2.3840 2.5750 -0.1890 0.0011 0.3525 416 TYR A CE2 2715 C CZ . TYR A 403 ? 2.1348 2.3444 2.5848 -0.1966 0.0123 0.3792 416 TYR A CZ 2716 O OH . TYR A 403 ? 2.1783 2.3305 2.6258 -0.1816 0.0038 0.3904 416 TYR A OH 2717 N N . GLU A 404 ? 1.4891 2.0322 1.9681 -0.2716 0.0697 0.2275 417 GLU A N 2718 C CA . GLU A 404 ? 1.3108 1.8688 1.7972 -0.2713 0.0770 0.1920 417 GLU A CA 2719 C C . GLU A 404 ? 1.3009 1.8713 1.8218 -0.2217 0.0335 0.2041 417 GLU A C 2720 O O . GLU A 404 ? 1.2850 1.8752 1.8263 -0.1863 -0.0021 0.2323 417 GLU A O 2721 C CB . GLU A 404 ? 1.1454 1.7997 1.6329 -0.3069 0.1061 0.1354 417 GLU A CB 2722 C CG . GLU A 404 ? 1.0966 1.8253 1.6146 -0.2896 0.0922 0.1002 417 GLU A CG 2723 C CD . GLU A 404 ? 1.3020 2.1584 1.8307 -0.3192 0.1107 0.0475 417 GLU A CD 2724 O OE1 . GLU A 404 ? 1.4005 2.3287 1.9431 -0.3134 0.0963 0.0532 417 GLU A OE1 2725 O OE2 . GLU A 404 ? 1.3506 2.2382 1.8724 -0.3502 0.1413 -0.0011 417 GLU A OE2 2726 N N . THR A 405 ? 1.3103 1.8605 1.8321 -0.2191 0.0396 0.1834 418 THR A N 2727 C CA . THR A 405 ? 1.3451 1.8863 1.8917 -0.1746 0.0040 0.1953 418 THR A CA 2728 C C . THR A 405 ? 1.2627 1.8637 1.8240 -0.1747 0.0105 0.1495 418 THR A C 2729 O O . THR A 405 ? 1.3853 1.9866 1.9290 -0.2119 0.0469 0.1143 418 THR A O 2730 C CB . THR A 405 ? 1.4279 1.8556 1.9593 -0.1645 -0.0012 0.2287 418 THR A CB 2731 O OG1 . THR A 405 ? 1.4806 1.8620 1.9834 -0.1960 0.0363 0.2075 418 THR A OG1 2732 C CG2 . THR A 405 ? 1.3695 1.7447 1.8892 -0.1618 -0.0105 0.2741 418 THR A CG2 2733 N N . ILE A 406 ? 1.1296 1.7785 1.7190 -0.1321 -0.0226 0.1497 419 ILE A N 2734 C CA . ILE A 406 ? 1.1991 1.9006 1.8032 -0.1267 -0.0196 0.1095 419 ILE A CA 2735 C C . ILE A 406 ? 1.4931 2.1380 2.1071 -0.0813 -0.0502 0.1342 419 ILE A C 2736 O O . ILE A 406 ? 1.5647 2.2254 2.1914 -0.0365 -0.0828 0.1584 419 ILE A O 2737 C CB . ILE A 406 ? 1.1444 1.9842 1.7728 -0.1141 -0.0290 0.0784 419 ILE A CB 2738 C CG1 . ILE A 406 ? 1.0864 1.9854 1.7078 -0.1484 -0.0103 0.0680 419 ILE A CG1 2739 C CG2 . ILE A 406 ? 1.1794 2.0834 1.8193 -0.1242 -0.0147 0.0272 419 ILE A CG2 2740 C CD1 . ILE A 406 ? 1.0823 1.9712 1.6791 -0.2126 0.0392 0.0322 419 ILE A CD1 2741 N N . GLU A 407 ? 1.5688 2.1459 2.1727 -0.0920 -0.0375 0.1272 420 GLU A N 2742 C CA . GLU A 407 ? 1.4712 1.9799 2.0797 -0.0559 -0.0626 0.1520 420 GLU A CA 2743 C C . GLU A 407 ? 1.4001 1.9403 2.0220 -0.0430 -0.0635 0.1189 420 GLU A C 2744 O O . GLU A 407 ? 1.3101 1.8726 1.9271 -0.0749 -0.0349 0.0804 420 GLU A O 2745 C CB . GLU A 407 ? 1.5078 1.9053 2.0934 -0.0723 -0.0525 0.1779 420 GLU A CB 2746 C CG . GLU A 407 ? 1.6914 2.0227 2.2776 -0.0420 -0.0822 0.2241 420 GLU A CG 2747 C CD . GLU A 407 ? 1.8583 2.1135 2.4401 -0.0319 -0.0881 0.2320 420 GLU A CD 2748 O OE1 . GLU A 407 ? 1.9416 2.1640 2.5090 -0.0561 -0.0646 0.2166 420 GLU A OE1 2749 O OE2 . GLU A 407 ? 1.8916 2.1175 2.4803 0.0005 -0.1142 0.2529 420 GLU A OE2 2750 N N . GLN A 408 ? 1.4788 2.0177 2.1138 0.0041 -0.0939 0.1334 421 GLN A N 2751 C CA . GLN A 408 ? 1.5070 2.0557 2.1520 0.0206 -0.0969 0.1088 421 GLN A CA 2752 C C . GLN A 408 ? 1.6930 2.1277 2.3250 0.0187 -0.0971 0.1283 421 GLN A C 2753 O O . GLN A 408 ? 1.5905 1.9548 2.2159 0.0404 -0.1168 0.1669 421 GLN A O 2754 C CB . GLN A 408 ? 1.3657 1.9719 2.0255 0.0753 -0.1259 0.1122 421 GLN A CB 2755 N N . LYS A 409 ? 1.8049 2.2235 2.4305 -0.0099 -0.0723 0.0995 422 LYS A N 2756 C CA . LYS A 409 ? 1.8131 2.1367 2.4254 -0.0133 -0.0691 0.1112 422 LYS A CA 2757 C C . LYS A 409 ? 1.9222 2.2582 2.5465 0.0044 -0.0734 0.0852 422 LYS A C 2758 O O . LYS A 409 ? 1.9117 2.3308 2.5497 0.0040 -0.0667 0.0491 422 LYS A O 2759 C CB . LYS A 409 ? 1.6968 1.9792 2.2833 -0.0564 -0.0341 0.1027 422 LYS A CB 2760 N N . LYS A 410 ? 1.9284 2.1870 2.5477 0.0194 -0.0846 0.1022 423 LYS A N 2761 C CA . LYS A 410 ? 1.7881 2.0465 2.4163 0.0368 -0.0889 0.0807 423 LYS A CA 2762 C C . LYS A 410 ? 1.7300 1.9892 2.3491 0.0028 -0.0565 0.0436 423 LYS A C 2763 O O . LYS A 410 ? 1.6773 1.8732 2.2739 -0.0216 -0.0375 0.0504 423 LYS A O 2764 C CB . LYS A 410 ? 1.6808 1.8529 2.3033 0.0591 -0.1084 0.1099 423 LYS A CB 2765 N N . ALA A 411 ? 1.7075 2.0389 2.3405 0.0028 -0.0485 0.0040 424 ALA A N 2766 C CA . ALA A 411 ? 1.6991 2.0357 2.3197 -0.0333 -0.0127 -0.0360 424 ALA A CA 2767 C C . ALA A 411 ? 1.9059 2.1657 2.5163 -0.0287 -0.0097 -0.0367 424 ALA A C 2768 O O . ALA A 411 ? 1.9308 2.1332 2.5137 -0.0552 0.0179 -0.0419 424 ALA A O 2769 C CB . ALA A 411 ? 1.5477 1.9942 2.1874 -0.0384 -0.0039 -0.0818 424 ALA A CB 2770 N N . TYR A 412 ? 2.0532 2.3108 2.6816 0.0076 -0.0368 -0.0309 425 TYR A N 2771 C CA . TYR A 412 ? 2.1330 2.3238 2.7550 0.0154 -0.0376 -0.0321 425 TYR A CA 2772 C C . TYR A 412 ? 2.2538 2.3811 2.8771 0.0455 -0.0680 0.0088 425 TYR A C 2773 O O . TYR A 412 ? 2.3304 2.4811 2.9674 0.0784 -0.0931 0.0222 425 TYR A O 2774 C CB . TYR A 412 ? 2.1394 2.3828 2.7790 0.0286 -0.0381 -0.0682 425 TYR A CB 2775 C CG . TYR A 412 ? 2.1619 2.3642 2.7869 0.0079 -0.0129 -0.0946 425 TYR A CG 2776 C CD1 . TYR A 412 ? 2.1637 2.2874 2.7585 -0.0157 0.0080 -0.0838 425 TYR A CD1 2777 C CD2 . TYR A 412 ? 2.1512 2.3937 2.7895 0.0147 -0.0092 -0.1300 425 TYR A CD2 2778 C CE1 . TYR A 412 ? 2.1393 2.2211 2.7146 -0.0307 0.0330 -0.1067 425 TYR A CE1 2779 C CE2 . TYR A 412 ? 2.1376 2.3377 2.7597 -0.0044 0.0155 -0.1541 425 TYR A CE2 2780 C CZ . TYR A 412 ? 2.1248 2.2423 2.7140 -0.0264 0.0370 -0.1418 425 TYR A CZ 2781 O OH . TYR A 412 ? 2.1280 2.1994 2.6953 -0.0412 0.0631 -0.1644 425 TYR A OH 2782 N N . GLU A 413 ? 2.3166 2.3639 2.9215 0.0351 -0.0637 0.0272 426 GLU A N 2783 C CA . GLU A 413 ? 2.4386 2.4261 3.0422 0.0552 -0.0885 0.0627 426 GLU A CA 2784 C C . GLU A 413 ? 2.5461 2.4788 3.1447 0.0608 -0.0894 0.0561 426 GLU A C 2785 O O . GLU A 413 ? 2.6177 2.5494 3.2093 0.0466 -0.0688 0.0292 426 GLU A O 2786 C CB . GLU A 413 ? 2.4354 2.3867 3.0235 0.0384 -0.0859 0.0923 426 GLU A CB 2787 C CG . GLU A 413 ? 2.4267 2.4188 3.0069 0.0134 -0.0642 0.0847 426 GLU A CG 2788 C CD . GLU A 413 ? 2.4453 2.4175 3.0166 0.0069 -0.0703 0.1191 426 GLU A CD 2789 O OE1 . GLU A 413 ? 2.4765 2.4385 3.0272 -0.0170 -0.0477 0.1204 426 GLU A OE1 2790 O OE2 . GLU A 413 ? 2.4156 2.3788 2.9966 0.0263 -0.0954 0.1449 426 GLU A OE2 2791 N N . VAL A 414 ? 2.5375 2.4230 3.1367 0.0804 -0.1111 0.0790 427 VAL A N 2792 C CA . VAL A 414 ? 2.4979 2.3324 3.0926 0.0853 -0.1133 0.0728 427 VAL A CA 2793 C C . VAL A 414 ? 2.4699 2.2772 3.0477 0.0604 -0.0917 0.0632 427 VAL A C 2794 O O . VAL A 414 ? 2.4809 2.2765 3.0552 0.0592 -0.0809 0.0403 427 VAL A O 2795 C CB . VAL A 414 ? 2.4531 2.2319 3.0430 0.0989 -0.1338 0.1010 427 VAL A CB 2796 N N . ALA A 415 ? 2.3904 2.1875 2.9543 0.0435 -0.0841 0.0812 428 ALA A N 2797 C CA . ALA A 415 ? 2.3194 2.0913 2.8586 0.0259 -0.0607 0.0756 428 ALA A CA 2798 C C . ALA A 415 ? 2.3505 2.1458 2.8793 0.0136 -0.0310 0.0420 428 ALA A C 2799 O O . ALA A 415 ? 2.3628 2.1275 2.8690 0.0074 -0.0105 0.0284 428 ALA A O 2800 C CB . ALA A 415 ? 2.2519 2.0175 2.7762 0.0138 -0.0565 0.1013 428 ALA A CB 2801 N N . GLY A 416 ? 2.3706 2.2214 2.9131 0.0094 -0.0269 0.0273 429 GLY A N 2802 C CA . GLY A 416 ? 2.3462 2.2263 2.8777 -0.0097 0.0050 -0.0080 429 GLY A CA 2803 C C . GLY A 416 ? 2.3702 2.2561 2.9111 -0.0024 0.0079 -0.0388 429 GLY A C 2804 O O . GLY A 416 ? 2.3527 2.2263 2.8722 -0.0189 0.0387 -0.0661 429 GLY A O 2805 N N . LEU A 417 ? 2.4117 2.3118 2.9804 0.0233 -0.0220 -0.0341 430 LEU A N 2806 C CA . LEU A 417 ? 2.3958 2.3014 2.9756 0.0353 -0.0237 -0.0602 430 LEU A CA 2807 C C . LEU A 417 ? 2.4603 2.2953 3.0212 0.0352 -0.0178 -0.0582 430 LEU A C 2808 O O . LEU A 417 ? 2.5108 2.3383 3.0635 0.0293 0.0007 -0.0865 430 LEU A O 2809 C CB . LEU A 417 ? 2.2842 2.2144 2.8906 0.0679 -0.0559 -0.0506 430 LEU A CB 2810 N N . LEU A 418 ? 2.4349 2.2225 2.9882 0.0410 -0.0328 -0.0262 431 LEU A N 2811 C CA . LEU A 418 ? 2.4124 2.1422 2.9455 0.0405 -0.0271 -0.0227 431 LEU A CA 2812 C C . LEU A 418 ? 2.4949 2.2081 2.9923 0.0215 0.0087 -0.0334 431 LEU A C 2813 O O . LEU A 418 ? 2.5715 2.2429 3.0450 0.0230 0.0217 -0.0381 431 LEU A O 2814 C CB . LEU A 418 ? 2.3145 2.0115 2.8481 0.0475 -0.0501 0.0111 431 LEU A CB 2815 N N . GLY A 419 ? 2.4603 2.2041 2.9499 0.0051 0.0266 -0.0373 432 GLY A N 2816 C CA . GLY A 419 ? 2.4227 2.1432 2.8698 -0.0132 0.0657 -0.0455 432 GLY A CA 2817 C C . GLY A 419 ? 2.4351 2.1627 2.8674 -0.0285 0.0993 -0.0866 432 GLY A C 2818 O O . GLY A 419 ? 2.4680 2.1543 2.8549 -0.0398 0.1367 -0.0975 432 GLY A O 2819 N N . ASP A 420 ? 2.4385 2.2185 2.9053 -0.0278 0.0881 -0.1099 433 ASP A N 2820 C CA . ASP A 420 ? 2.4782 2.2778 2.9369 -0.0452 0.1186 -0.1537 433 ASP A CA 2821 C C . ASP A 420 ? 2.5106 2.2984 2.9851 -0.0281 0.1062 -0.1693 433 ASP A C 2822 O O . ASP A 420 ? 2.4887 2.2318 2.9342 -0.0334 0.1317 -0.1872 433 ASP A O 2823 C CB . ASP A 420 ? 2.4317 2.3161 2.9158 -0.0602 0.1204 -0.1754 433 ASP A CB 2824 N N . ILE A 421 ? 2.5565 2.3812 3.0727 -0.0059 0.0689 -0.1622 434 ILE A N 2825 C CA . ILE A 421 ? 2.6179 2.4315 3.1499 0.0128 0.0547 -0.1743 434 ILE A CA 2826 C C . ILE A 421 ? 2.6981 2.4409 3.2186 0.0288 0.0398 -0.1485 434 ILE A C 2827 O O . ILE A 421 ? 2.7765 2.4815 3.2832 0.0314 0.0503 -0.1628 434 ILE A O 2828 C CB . ILE A 421 ? 2.6019 2.4757 3.1749 0.0353 0.0231 -0.1743 434 ILE A CB 2829 N N . GLY A 422 ? 2.7078 2.4363 3.2332 0.0379 0.0166 -0.1124 435 GLY A N 2830 C CA . GLY A 422 ? 2.7380 2.4141 3.2584 0.0513 -0.0016 -0.0897 435 GLY A CA 2831 C C . GLY A 422 ? 2.7773 2.4041 3.2627 0.0465 0.0212 -0.0961 435 GLY A C 2832 O O . GLY A 422 ? 2.7748 2.3714 3.2600 0.0575 0.0138 -0.1008 435 GLY A O 2833 N N . GLY A 423 ? 2.8220 2.4388 3.2736 0.0323 0.0506 -0.0960 436 GLY A N 2834 C CA . GLY A 423 ? 2.8664 2.4335 3.2741 0.0335 0.0766 -0.0994 436 GLY A CA 2835 C C . GLY A 423 ? 2.8868 2.4351 3.2838 0.0336 0.0963 -0.1324 436 GLY A C 2836 O O . GLY A 423 ? 2.9290 2.4376 3.3070 0.0459 0.0990 -0.1330 436 GLY A O 2837 N N . GLN A 424 ? 2.8447 2.4267 3.2540 0.0194 0.1103 -0.1615 437 GLN A N 2838 C CA . GLN A 424 ? 2.7888 2.3602 3.1913 0.0163 0.1297 -0.1966 437 GLN A CA 2839 C C . GLN A 424 ? 2.7544 2.3412 3.1988 0.0344 0.0955 -0.2004 437 GLN A C 2840 O O . GLN A 424 ? 2.7987 2.3682 3.2390 0.0375 0.1049 -0.2239 437 GLN A O 2841 C CB . GLN A 424 ? 2.7310 2.3393 3.1278 -0.0103 0.1622 -0.2309 437 GLN A CB 2842 N N . MET A 425 ? 2.6621 2.2766 3.1421 0.0467 0.0584 -0.1772 438 MET A N 2843 C CA . MET A 425 ? 2.5963 2.2150 3.1082 0.0666 0.0277 -0.1761 438 MET A CA 2844 C C . MET A 425 ? 2.6026 2.1664 3.1033 0.0782 0.0148 -0.1588 438 MET A C 2845 O O . MET A 425 ? 2.6270 2.1734 3.1381 0.0903 0.0032 -0.1673 438 MET A O 2846 C CB . MET A 425 ? 2.5602 2.2205 3.1042 0.0773 -0.0015 -0.1578 438 MET A CB 2847 N N . GLY A 426 ? 2.5830 2.1243 3.0619 0.0745 0.0173 -0.1355 439 GLY A N 2848 C CA . GLY A 426 ? 2.6067 2.1075 3.0702 0.0831 0.0100 -0.1234 439 GLY A CA 2849 C C . GLY A 426 ? 2.6737 2.1422 3.1035 0.0844 0.0388 -0.1452 439 GLY A C 2850 O O . GLY A 426 ? 2.6989 2.1401 3.1235 0.0948 0.0324 -0.1483 439 GLY A O 2851 N N . LEU A 427 ? 2.7144 2.1832 3.1175 0.0730 0.0733 -0.1614 440 LEU A N 2852 C CA . LEU A 427 ? 2.7426 2.1720 3.1042 0.0736 0.1082 -0.1836 440 LEU A CA 2853 C C . LEU A 427 ? 2.8093 2.2395 3.1898 0.0746 0.1079 -0.2135 440 LEU A C 2854 O O . LEU A 427 ? 2.8390 2.2318 3.1985 0.0838 0.1184 -0.2252 440 LEU A O 2855 C CB . LEU A 427 ? 2.7007 2.1224 3.0221 0.0571 0.1505 -0.1942 440 LEU A CB 2856 N N . PHE A 428 ? 2.8295 2.3060 3.2482 0.0674 0.0962 -0.2261 441 PHE A N 2857 C CA . PHE A 428 ? 2.8347 2.3229 3.2756 0.0708 0.0929 -0.2538 441 PHE A CA 2858 C C . PHE A 428 ? 2.9229 2.3902 3.3841 0.0912 0.0604 -0.2415 441 PHE A C 2859 O O . PHE A 428 ? 2.9676 2.4119 3.4256 0.0976 0.0649 -0.2602 441 PHE A O 2860 C CB . PHE A 428 ? 2.7505 2.3057 3.2270 0.0638 0.0855 -0.2679 441 PHE A CB 2861 C CG . PHE A 428 ? 2.7488 2.3270 3.2591 0.0789 0.0651 -0.2829 441 PHE A CG 2862 C CD1 . PHE A 428 ? 2.7292 2.3191 3.2382 0.0720 0.0861 -0.3207 441 PHE A CD1 2863 C CD2 . PHE A 428 ? 2.7638 2.3480 3.3027 0.1003 0.0274 -0.2595 441 PHE A CD2 2864 C CE1 . PHE A 428 ? 2.7118 2.3253 3.2506 0.0890 0.0673 -0.3339 441 PHE A CE1 2865 C CE2 . PHE A 428 ? 2.7440 2.3432 3.3071 0.1184 0.0111 -0.2714 441 PHE A CE2 2866 C CZ . PHE A 428 ? 2.7259 2.3428 3.2905 0.1142 0.0297 -0.3081 441 PHE A CZ 2867 N N . ILE A 429 ? 2.9450 2.4176 3.4243 0.0990 0.0301 -0.2113 442 ILE A N 2868 C CA . ILE A 429 ? 2.9612 2.4095 3.4548 0.1132 0.0024 -0.1992 442 ILE A CA 2869 C C . ILE A 429 ? 3.0209 2.4259 3.4852 0.1164 0.0107 -0.1980 442 ILE A C 2870 O O . ILE A 429 ? 3.0125 2.3947 3.4833 0.1249 -0.0049 -0.1978 442 ILE A O 2871 C CB . ILE A 429 ? 2.9159 2.3751 3.4277 0.1158 -0.0253 -0.1688 442 ILE A CB 2872 N N . GLY A 430 ? 3.0580 2.4519 3.4863 0.1113 0.0367 -0.1972 443 GLY A N 2873 C CA . GLY A 430 ? 3.0824 2.4403 3.4748 0.1204 0.0493 -0.1972 443 GLY A CA 2874 C C . GLY A 430 ? 3.0832 2.4126 3.4582 0.1248 0.0711 -0.2265 443 GLY A C 2875 O O . GLY A 430 ? 3.1015 2.4065 3.4690 0.1363 0.0652 -0.2302 443 GLY A O 2876 N N . ALA A 431 ? 3.0470 2.3818 3.4149 0.1137 0.0977 -0.2494 444 ALA A N 2877 C CA . ALA A 431 ? 3.0142 2.3237 3.3659 0.1137 0.1218 -0.2809 444 ALA A CA 2878 C C . ALA A 431 ? 3.0190 2.3432 3.4137 0.1188 0.0963 -0.2937 444 ALA A C 2879 O O . ALA A 431 ? 2.9969 2.3039 3.3858 0.1200 0.1104 -0.3198 444 ALA A O 2880 C CB . ALA A 431 ? 2.9747 2.2892 3.3040 0.0943 0.1614 -0.3050 444 ALA A CB 2881 N N . SER A 432 ? 3.0591 2.4114 3.4927 0.1228 0.0611 -0.2749 445 SER A N 2882 C CA . SER A 432 ? 3.1344 2.4939 3.6025 0.1325 0.0368 -0.2817 445 SER A CA 2883 C C . SER A 432 ? 3.2427 2.5600 3.7027 0.1436 0.0270 -0.2810 445 SER A C 2884 O O . SER A 432 ? 3.2208 2.5262 3.6890 0.1500 0.0269 -0.3007 445 SER A O 2885 C CB . SER A 432 ? 3.0980 2.4871 3.5981 0.1366 0.0065 -0.2589 445 SER A CB 2886 O OG . SER A 432 ? 3.0498 2.4853 3.5601 0.1282 0.0136 -0.2611 445 SER A OG 2887 N N . ILE A 433 ? 3.3489 2.6494 3.7933 0.1454 0.0188 -0.2597 446 ILE A N 2888 C CA . ILE A 433 ? 3.4193 2.6892 3.8550 0.1536 0.0095 -0.2599 446 ILE A CA 2889 C C . ILE A 433 ? 3.4466 2.6872 3.8488 0.1602 0.0369 -0.2816 446 ILE A C 2890 O O . ILE A 433 ? 3.4728 2.6921 3.8787 0.1665 0.0343 -0.2975 446 ILE A O 2891 C CB . ILE A 433 ? 3.4211 2.6945 3.8475 0.1524 -0.0044 -0.2350 446 ILE A CB 2892 C CG1 . ILE A 433 ? 3.4053 2.6991 3.8604 0.1442 -0.0292 -0.2137 446 ILE A CG1 2893 C CG2 . ILE A 433 ? 3.4282 2.6803 3.8457 0.1585 -0.0128 -0.2398 446 ILE A CG2 2894 C CD1 . ILE A 433 ? 3.4003 2.7046 3.8476 0.1383 -0.0408 -0.1916 446 ILE A CD1 2895 N N . LEU A 434 ? 3.4047 2.6391 3.7696 0.1597 0.0652 -0.2817 447 LEU A N 2896 C CA . LEU A 434 ? 3.3417 2.5388 3.6626 0.1683 0.0975 -0.3004 447 LEU A CA 2897 C C . LEU A 434 ? 3.3195 2.5057 3.6510 0.1633 0.1105 -0.3315 447 LEU A C 2898 O O . LEU A 434 ? 3.3413 2.4917 3.6443 0.1710 0.1310 -0.3497 447 LEU A O 2899 C CB . LEU A 434 ? 3.2875 2.4731 3.5610 0.1678 0.1318 -0.2956 447 LEU A CB 2900 N N . THR A 435 ? 3.2533 2.4744 3.6244 0.1522 0.0989 -0.3378 448 THR A N 2901 C CA . THR A 435 ? 3.1930 2.4204 3.5809 0.1478 0.1076 -0.3680 448 THR A CA 2902 C C . THR A 435 ? 3.1325 2.3478 3.5451 0.1603 0.0827 -0.3720 448 THR A C 2903 O O . THR A 435 ? 3.1161 2.3099 3.5207 0.1631 0.0966 -0.3964 448 THR A O 2904 C CB . THR A 435 ? 3.1800 2.4613 3.5996 0.1356 0.1038 -0.3736 448 THR A CB 2905 N N . VAL A 436 ? 3.1237 2.3483 3.5626 0.1663 0.0487 -0.3489 449 VAL A N 2906 C CA . VAL A 436 ? 3.1499 2.3591 3.6099 0.1764 0.0267 -0.3519 449 VAL A CA 2907 C C . VAL A 436 ? 3.1817 2.3504 3.6149 0.1825 0.0359 -0.3626 449 VAL A C 2908 O O . VAL A 436 ? 3.1592 2.3217 3.5900 0.1866 0.0275 -0.3670 449 VAL A O 2909 C CB . VAL A 436 ? 2.6844 1.8960 3.1638 0.1785 -0.0051 -0.3244 449 VAL A CB 2910 C CG1 . VAL A 436 ? 2.6496 1.8996 3.1449 0.1736 -0.0124 -0.3077 449 VAL A CG1 2911 C CG2 . VAL A 436 ? 2.7063 1.8970 3.1653 0.1762 -0.0106 -0.3097 449 VAL A CG2 2912 N N . LEU A 437 ? 3.2303 2.3847 3.6255 0.1827 0.0541 -0.3579 450 LEU A N 2913 C CA . LEU A 437 ? 3.2612 2.3932 3.6092 0.1899 0.0647 -0.3596 450 LEU A CA 2914 C C . LEU A 437 ? 3.2515 2.3800 3.5684 0.1869 0.0868 -0.3783 450 LEU A C 2915 O O . LEU A 437 ? 3.2142 2.3535 3.5530 0.1847 0.0773 -0.3880 450 LEU A O 2916 C CB . LEU A 437 ? 3.2626 2.3798 3.5748 0.1985 0.0813 -0.3511 450 LEU A CB 2917 C CG . LEU A 437 ? 3.2209 2.3461 3.5468 0.2045 0.0583 -0.3324 450 LEU A CG 2918 C CD1 . LEU A 437 ? 3.2124 2.3235 3.5379 0.2127 0.0443 -0.3390 450 LEU A CD1 2919 C CD2 . LEU A 437 ? 3.1738 2.3310 3.5399 0.1905 0.0309 -0.3138 450 LEU A CD2 2920 N N . ASP B 2 ? 2.3756 2.6082 2.7868 0.9957 0.0409 0.3409 2 ASP D N 2921 C CA . ASP B 2 ? 2.4204 2.6531 2.8293 0.9973 0.0452 0.3345 2 ASP D CA 2922 C C . ASP B 2 ? 2.4513 2.6847 2.8623 0.9961 0.0379 0.3315 2 ASP D C 2923 O O . ASP B 2 ? 2.4754 2.7083 2.8883 0.9948 0.0297 0.3303 2 ASP D O 2924 C CB . ASP B 2 ? 2.4036 2.6349 2.8092 0.9990 0.0489 0.3278 2 ASP D CB 2925 N N . CYS B 3 ? 2.4347 2.6691 2.8450 0.9968 0.0409 0.3303 3 CYS D N 2926 C CA . CYS B 3 ? 2.4133 2.6484 2.8254 0.9959 0.0344 0.3277 3 CYS D CA 2927 C C . CYS B 3 ? 2.4181 2.6525 2.8293 0.9963 0.0303 0.3196 3 CYS D C 2928 O O . CYS B 3 ? 2.4391 2.6729 2.8477 0.9977 0.0346 0.3148 3 CYS D O 2929 C CB . CYS B 3 ? 2.3682 2.6047 2.7794 0.9968 0.0392 0.3277 3 CYS D CB 2930 S SG . CYS B 3 ? 3.0528 3.2894 3.4599 0.9993 0.0465 0.3188 3 CYS D SG 2931 N N . ILE B 4 ? 2.3269 2.5613 2.7402 0.9950 0.0219 0.3182 4 ILE D N 2932 C CA . ILE B 4 ? 2.1496 2.3835 2.5622 0.9955 0.0175 0.3105 4 ILE D CA 2933 C C . ILE B 4 ? 2.1021 2.3372 2.5139 0.9963 0.0177 0.3061 4 ILE D C 2934 O O . ILE B 4 ? 2.0516 2.2870 2.4652 0.9953 0.0142 0.3092 4 ILE D O 2935 C CB . ILE B 4 ? 2.0337 2.2663 2.4488 0.9936 0.0073 0.3117 4 ILE D CB 2936 N N . PRO B 5 ? 2.1513 2.3871 2.5603 0.9982 0.0220 0.2987 5 PRO D N 2937 C CA . PRO B 5 ? 2.1577 2.3948 2.5654 0.9993 0.0235 0.2940 5 PRO D CA 2938 C C . PRO B 5 ? 2.0578 2.2948 2.4673 0.9984 0.0143 0.2917 5 PRO D C 2939 O O . PRO B 5 ? 1.9859 2.2215 2.3969 0.9972 0.0070 0.2921 5 PRO D O 2940 C CB . PRO B 5 ? 2.2005 2.4385 2.6050 1.0015 0.0293 0.2865 5 PRO D CB 2941 C CG . PRO B 5 ? 2.2009 2.4377 2.6055 1.0012 0.0266 0.2858 5 PRO D CG 2942 C CD . PRO B 5 ? 2.1839 2.4193 2.5908 0.9994 0.0250 0.2942 5 PRO D CD 2943 N N . LYS B 6 ? 2.0900 2.3281 2.4989 0.9991 0.0147 0.2892 6 LYS D N 2944 C CA . LYS B 6 ? 2.1700 2.4079 2.5798 0.9986 0.0066 0.2862 6 LYS D CA 2945 C C . LYS B 6 ? 2.2396 2.4775 2.6481 0.9995 0.0040 0.2790 6 LYS D C 2946 O O . LYS B 6 ? 2.2140 2.4529 2.6202 1.0011 0.0100 0.2750 6 LYS D O 2947 C CB . LYS B 6 ? 2.1138 2.3532 2.5226 0.9996 0.0087 0.2840 6 LYS D CB 2948 N N . TRP B 7 ? 2.2349 2.4715 2.6445 0.9987 -0.0050 0.2777 7 TRP D N 2949 C CA . TRP B 7 ? 2.1622 2.3991 2.5706 0.9997 -0.0083 0.2707 7 TRP D CA 2950 C C . TRP B 7 ? 2.2002 2.4357 2.6091 0.9991 -0.0101 0.2714 7 TRP D C 2951 O O . TRP B 7 ? 2.2067 2.4421 2.6148 0.9996 -0.0143 0.2665 7 TRP D O 2952 C CB . TRP B 7 ? 2.1112 2.3508 2.5165 1.0021 -0.0012 0.2634 7 TRP D CB 2953 C CG . TRP B 7 ? 2.1218 2.3628 2.5263 1.0030 -0.0017 0.2604 7 TRP D CG 2954 C CD1 . TRP B 7 ? 2.2269 2.4705 2.6289 1.0051 0.0015 0.2529 7 TRP D CD1 2955 C CD2 . TRP B 7 ? 2.0931 2.3332 2.4993 1.0018 -0.0058 0.2648 7 TRP D CD2 2956 N NE1 . TRP B 7 ? 2.2669 2.5112 2.6688 1.0054 -0.0004 0.2523 7 TRP D NE1 2957 C CE2 . TRP B 7 ? 2.2104 2.4525 2.6149 1.0034 -0.0049 0.2595 7 TRP D CE2 2958 C CE3 . TRP B 7 ? 1.9928 2.2307 2.4017 0.9997 -0.0103 0.2725 7 TRP D CE3 2959 C CZ2 . TRP B 7 ? 2.1633 2.4051 2.5687 1.0029 -0.0081 0.2618 7 TRP D CZ2 2960 C CZ3 . TRP B 7 ? 2.0323 2.2700 2.4420 0.9992 -0.0135 0.2748 7 TRP D CZ3 2961 C CH2 . TRP B 7 ? 2.0992 2.3387 2.5071 1.0008 -0.0124 0.2695 7 TRP D CH2 2962 N N . LYS B 8 ? 2.2214 2.4561 2.6314 0.9980 -0.0072 0.2777 8 LYS D N 2963 C CA . LYS B 8 ? 2.2559 2.4894 2.6661 0.9976 -0.0081 0.2787 8 LYS D CA 2964 C C . LYS B 8 ? 2.2613 2.4923 2.6744 0.9953 -0.0168 0.2843 8 LYS D C 2965 O O . LYS B 8 ? 2.2903 2.5206 2.7055 0.9938 -0.0196 0.2901 8 LYS D O 2966 C CB . LYS B 8 ? 2.2855 2.5195 2.6948 0.9981 0.0007 0.2817 8 LYS D CB 2967 N N . GLY B 9 ? 2.2071 2.4370 2.6202 0.9950 -0.0210 0.2825 9 GLY D N 2968 C CA . GLY B 9 ? 2.1595 2.3870 2.5752 0.9929 -0.0294 0.2873 9 GLY D CA 2969 C C . GLY B 9 ? 2.1090 2.3358 2.5267 0.9913 -0.0281 0.2958 9 GLY D C 2970 O O . GLY B 9 ? 2.0773 2.3046 2.4943 0.9917 -0.0226 0.2974 9 GLY D O 2971 N N . CYS B 10 ? 2.0894 2.3151 2.5094 0.9895 -0.0335 0.3014 10 CYS D N 2972 C CA . CYS B 10 ? 2.0316 2.2573 2.4537 0.9880 -0.0325 0.3098 10 CYS D CA 2973 C C . CYS B 10 ? 1.9882 2.2120 2.4123 0.9862 -0.0392 0.3141 10 CYS D C 2974 O O . CYS B 10 ? 1.8410 2.0649 2.2670 0.9847 -0.0398 0.3214 10 CYS D O 2975 C CB . CYS B 10 ? 1.9967 2.2229 2.4201 0.9872 -0.0335 0.3139 10 CYS D CB 2976 S SG . CYS B 10 ? 3.9155 4.1395 4.3401 0.9860 -0.0442 0.3131 10 CYS D SG 2977 N N . VAL B 11 ? 2.0399 2.2622 2.4633 0.9864 -0.0442 0.3097 11 VAL D N 2978 C CA . VAL B 11 ? 1.9791 2.1992 2.4042 0.9847 -0.0516 0.3130 11 VAL D CA 2979 C C . VAL B 11 ? 2.1268 2.3475 2.5530 0.9839 -0.0484 0.3194 11 VAL D C 2980 O O . VAL B 11 ? 2.1592 2.3814 2.5839 0.9852 -0.0405 0.3185 11 VAL D O 2981 C CB . VAL B 11 ? 1.7234 1.9425 2.1470 0.9857 -0.0547 0.3064 11 VAL D CB 2982 N N . ASN B 12 ? 2.1739 2.3935 2.6026 0.9818 -0.0545 0.3258 12 ASN D N 2983 C CA . ASN B 12 ? 2.2531 2.4735 2.6830 0.9809 -0.0520 0.3327 12 ASN D CA 2984 C C . ASN B 12 ? 2.2166 2.4395 2.6465 0.9814 -0.0439 0.3367 12 ASN D C 2985 O O . ASN B 12 ? 2.1157 2.3400 2.5449 0.9821 -0.0373 0.3387 12 ASN D O 2986 C CB . ASN B 12 ? 2.3464 2.5666 2.7751 0.9817 -0.0497 0.3306 12 ASN D CB 2987 C CG . ASN B 12 ? 2.3996 2.6175 2.8295 0.9803 -0.0583 0.3318 12 ASN D CG 2988 O OD1 . ASN B 12 ? 2.4040 2.6214 2.8362 0.9784 -0.0631 0.3384 12 ASN D OD1 2989 N ND2 . ASN B 12 ? 2.4252 2.6419 2.8535 0.9813 -0.0602 0.3256 12 ASN D ND2 2990 N N . ARG B 13 ? 2.2202 2.4437 2.6508 0.9811 -0.0445 0.3379 13 ARG D N 2991 C CA . ARG B 13 ? 2.1474 2.3733 2.5779 0.9816 -0.0372 0.3415 13 ARG D CA 2992 C C . ARG B 13 ? 2.1500 2.3764 2.5825 0.9803 -0.0413 0.3462 13 ARG D C 2993 O O . ARG B 13 ? 2.1583 2.3852 2.5901 0.9810 -0.0394 0.3440 13 ARG D O 2994 C CB . ARG B 13 ? 2.0825 2.3094 2.5102 0.9839 -0.0294 0.3352 13 ARG D CB 2995 N N . ASP B 16 ? 2.2647 2.4985 2.6920 0.9856 -0.0088 0.3466 16 ASP D N 2996 C CA . ASP B 16 ? 2.2890 2.5228 2.7134 0.9876 -0.0006 0.3422 16 ASP D CA 2997 C C . ASP B 16 ? 2.3598 2.5936 2.7818 0.9892 0.0023 0.3345 16 ASP D C 2998 O O . ASP B 16 ? 2.3436 2.5769 2.7632 0.9907 0.0064 0.3289 16 ASP D O 2999 C CB . ASP B 16 ? 2.2418 2.4741 2.6658 0.9875 -0.0026 0.3406 16 ASP D CB 3000 N N . CYS B 17 ? 2.4571 2.6914 2.8797 0.9890 -0.0001 0.3343 17 CYS D N 3001 C CA . CYS B 17 ? 2.5427 2.7774 2.9632 0.9906 0.0030 0.3276 17 CYS D CA 3002 C C . CYS B 17 ? 2.5764 2.8128 2.9949 0.9922 0.0132 0.3284 17 CYS D C 3003 O O . CYS B 17 ? 2.5778 2.8151 2.9971 0.9918 0.0164 0.3350 17 CYS D O 3004 C CB . CYS B 17 ? 2.5637 2.7983 2.9855 0.9898 -0.0036 0.3270 17 CYS D CB 3005 S SG . CYS B 17 ? 3.7050 3.9371 4.1287 0.9880 -0.0159 0.3258 17 CYS D SG 3006 N N . CYS B 18 ? 2.6050 2.8417 3.0208 0.9940 0.0181 0.3217 18 CYS D N 3007 C CA . CYS B 18 ? 2.6205 2.8585 3.0342 0.9956 0.0274 0.3220 18 CYS D CA 3008 C C . CYS B 18 ? 2.6545 2.8938 3.0695 0.9951 0.0262 0.3255 18 CYS D C 3009 O O . CYS B 18 ? 2.6640 2.9030 3.0809 0.9939 0.0185 0.3258 18 CYS D O 3010 C CB . CYS B 18 ? 2.5849 2.8230 2.9953 0.9977 0.0324 0.3137 18 CYS D CB 3011 S SG . CYS B 18 ? 5.4812 5.7182 5.8891 0.9990 0.0377 0.3104 18 CYS D SG 3012 N N . GLU B 19 ? 2.7006 2.9411 3.1145 0.9961 0.0340 0.3285 19 GLU D N 3013 C CA . GLU B 19 ? 2.7147 2.9567 3.1297 0.9957 0.0339 0.3327 19 GLU D CA 3014 C C . GLU B 19 ? 2.6299 2.8721 3.0450 0.9958 0.0294 0.3280 19 GLU D C 3015 O O . GLU B 19 ? 2.6302 2.8724 3.0429 0.9973 0.0322 0.3211 19 GLU D O 3016 C CB . GLU B 19 ? 2.8052 3.0483 3.2181 0.9974 0.0442 0.3347 19 GLU D CB 3017 C CG . GLU B 19 ? 2.8704 3.1152 3.2836 0.9976 0.0455 0.3374 19 GLU D CG 3018 C CD . GLU B 19 ? 2.9206 3.1660 3.3305 0.9998 0.0551 0.3346 19 GLU D CD 3019 O OE1 . GLU B 19 ? 2.9729 3.2174 3.3803 1.0011 0.0582 0.3278 19 GLU D OE1 3020 O OE2 . GLU B 19 ? 2.8919 3.1387 3.3018 1.0003 0.0596 0.3393 19 GLU D OE2 3021 N N . GLY B 20 ? 2.5606 2.8031 2.9781 0.9943 0.0225 0.3319 20 GLY D N 3022 C CA . GLY B 20 ? 2.4926 2.7352 2.9102 0.9943 0.0181 0.3285 20 GLY D CA 3023 C C . GLY B 20 ? 2.3900 2.6308 2.8089 0.9932 0.0082 0.3255 20 GLY D C 3024 O O . GLY B 20 ? 2.4043 2.6449 2.8232 0.9931 0.0036 0.3231 20 GLY D O 3025 N N . LEU B 21 ? 3.1106 2.0470 2.3508 0.8929 -0.3214 -0.0816 21 LEU D N 3026 C CA . LEU B 21 ? 2.9419 1.8998 2.1954 0.8713 -0.3378 -0.0725 21 LEU D CA 3027 C C . LEU B 21 ? 2.9843 1.9865 2.2613 0.8567 -0.3131 -0.0383 21 LEU D C 3028 O O . LEU B 21 ? 3.0586 2.0869 2.3658 0.8576 -0.2877 -0.0199 21 LEU D O 3029 C CB . LEU B 21 ? 2.7444 1.7142 2.0542 0.8529 -0.3641 -0.0822 21 LEU D CB 3030 C CG . LEU B 21 ? 2.7309 1.6651 2.0354 0.8618 -0.3863 -0.1142 21 LEU D CG 3031 C CD1 . LEU B 21 ? 2.7250 1.6820 2.0982 0.8406 -0.4025 -0.1152 21 LEU D CD1 3032 C CD2 . LEU B 21 ? 2.6956 1.5957 1.9432 0.8701 -0.4121 -0.1393 21 LEU D CD2 3033 N N . GLU B 22 ? 2.9422 1.9530 2.2049 0.8432 -0.3203 -0.0297 22 GLU D N 3034 C CA . GLU B 22 ? 2.9163 1.9696 2.2033 0.8237 -0.2997 0.0012 22 GLU D CA 3035 C C . GLU B 22 ? 2.8959 1.9711 2.2245 0.7977 -0.3204 0.0039 22 GLU D C 3036 O O . GLU B 22 ? 2.9118 1.9632 2.2237 0.7984 -0.3484 -0.0157 22 GLU D O 3037 C CB . GLU B 22 ? 2.9723 2.0137 2.1963 0.8310 -0.2825 0.0118 22 GLU D CB 3038 C CG . GLU B 22 ? 3.1263 2.1380 2.3052 0.8309 -0.3052 -0.0001 22 GLU D CG 3039 C CD . GLU B 22 ? 3.2866 2.2705 2.3899 0.8466 -0.2918 0.0024 22 GLU D CD 3040 O OE1 . GLU B 22 ? 3.3556 2.3315 2.4349 0.8639 -0.2723 0.0017 22 GLU D OE1 3041 O OE2 . GLU B 22 ? 3.2657 2.2354 2.3339 0.8419 -0.3003 0.0053 22 GLU D OE2 3042 N N . CYS B 23 ? 2.8379 1.9607 2.2212 0.7747 -0.3065 0.0278 23 CYS D N 3043 C CA . CYS B 23 ? 2.7760 1.9245 2.2044 0.7478 -0.3234 0.0312 23 CYS D CA 3044 C C . CYS B 23 ? 2.7007 1.8515 2.1004 0.7352 -0.3195 0.0428 23 CYS D C 3045 O O . CYS B 23 ? 2.7133 1.8876 2.1078 0.7256 -0.2927 0.0669 23 CYS D O 3046 C CB . CYS B 23 ? 2.7922 1.9918 2.2935 0.7269 -0.3112 0.0510 23 CYS D CB 3047 S SG . CYS B 23 ? 2.3887 1.6332 1.9425 0.6879 -0.3185 0.0656 23 CYS D SG 3048 N N . TRP B 24 ? 2.6081 1.7362 1.9919 0.7343 -0.3465 0.0257 24 TRP D N 3049 C CA . TRP B 24 ? 2.4982 1.6108 1.8385 0.7313 -0.3467 0.0308 24 TRP D CA 3050 C C . TRP B 24 ? 2.3896 1.5198 1.7647 0.7083 -0.3631 0.0309 24 TRP D C 3051 O O . TRP B 24 ? 2.3126 1.4414 1.7154 0.7068 -0.3903 0.0120 24 TRP D O 3052 C CB . TRP B 24 ? 2.5563 1.6179 1.8321 0.7580 -0.3647 0.0088 24 TRP D CB 3053 C CG . TRP B 24 ? 2.5627 1.6046 1.8044 0.7562 -0.3779 0.0070 24 TRP D CG 3054 C CD1 . TRP B 24 ? 2.5987 1.6458 1.8228 0.7431 -0.3610 0.0273 24 TRP D CD1 3055 C CD2 . TRP B 24 ? 2.5806 1.5926 1.7985 0.7691 -0.4103 -0.0162 24 TRP D CD2 3056 N NE1 . TRP B 24 ? 2.6836 1.7029 1.8749 0.7483 -0.3804 0.0186 24 TRP D NE1 3057 C CE2 . TRP B 24 ? 2.6444 1.6442 1.8322 0.7650 -0.4112 -0.0076 24 TRP D CE2 3058 C CE3 . TRP B 24 ? 2.5360 1.5313 1.7548 0.7831 -0.4384 -0.0433 24 TRP D CE3 3059 C CZ2 . TRP B 24 ? 2.5793 1.5526 1.7399 0.7768 -0.4396 -0.0240 24 TRP D CZ2 3060 C CZ3 . TRP B 24 ? 2.4535 1.4258 1.6450 0.7929 -0.4669 -0.0601 24 TRP D CZ3 3061 C CH2 . TRP B 24 ? 2.4493 1.4118 1.6132 0.7909 -0.4674 -0.0499 24 TRP D CH2 3062 N N . LYS B 25 ? 2.4356 1.5812 1.8062 0.6901 -0.3459 0.0513 25 LYS D N 3063 C CA . LYS B 25 ? 2.3764 1.5389 1.7780 0.6669 -0.3570 0.0530 25 LYS D CA 3064 C C . LYS B 25 ? 2.4305 1.5519 1.7863 0.6810 -0.3797 0.0368 25 LYS D C 3065 O O . LYS B 25 ? 2.4952 1.5869 1.7917 0.6917 -0.3698 0.0431 25 LYS D O 3066 C CB . LYS B 25 ? 2.2974 1.4898 1.7076 0.6412 -0.3277 0.0807 25 LYS D CB 3067 C CG . LYS B 25 ? 2.3943 1.5881 1.8099 0.6218 -0.3344 0.0826 25 LYS D CG 3068 C CD . LYS B 25 ? 2.4587 1.6768 1.9362 0.6071 -0.3584 0.0695 25 LYS D CD 3069 C CE . LYS B 25 ? 2.5779 1.7940 2.0565 0.5902 -0.3642 0.0699 25 LYS D CE 3070 N NZ . LYS B 25 ? 2.6332 1.8700 2.1666 0.5785 -0.3901 0.0540 25 LYS D NZ 3071 N N . ARG B 26 ? 2.4665 1.5882 1.8506 0.6803 -0.4098 0.0169 26 ARG D N 3072 C CA . ARG B 26 ? 2.6067 1.6945 1.9536 0.6951 -0.4345 0.0005 26 ARG D CA 3073 C C . ARG B 26 ? 2.5600 1.6522 1.9076 0.6780 -0.4294 0.0122 26 ARG D C 3074 O O . ARG B 26 ? 2.4939 1.6225 1.8881 0.6500 -0.4159 0.0259 26 ARG D O 3075 C CB . ARG B 26 ? 2.6388 1.7294 2.0167 0.7003 -0.4690 -0.0258 26 ARG D CB 3076 C CG . ARG B 26 ? 2.6346 1.7098 2.0016 0.7201 -0.4789 -0.0431 26 ARG D CG 3077 C CD . ARG B 26 ? 2.5691 1.6516 1.9710 0.7193 -0.5121 -0.0683 26 ARG D CD 3078 N NE . ARG B 26 ? 2.5133 1.6387 1.9890 0.6927 -0.5110 -0.0639 26 ARG D NE 3079 C CZ . ARG B 26 ? 2.4455 1.5904 1.9653 0.6807 -0.5360 -0.0795 26 ARG D CZ 3080 N NH1 . ARG B 26 ? 2.4081 1.5359 1.9077 0.6933 -0.5647 -0.1009 26 ARG D NH1 3081 N NH2 . ARG B 26 ? 2.3710 1.5553 1.9558 0.6555 -0.5323 -0.0730 26 ARG D NH2 3082 N N . ARG B 27 ? 2.5375 1.5917 1.8326 0.6947 -0.4402 0.0067 27 ARG D N 3083 C CA . ARG B 27 ? 2.5971 1.6469 1.8858 0.6817 -0.4349 0.0169 27 ARG D CA 3084 C C . ARG B 27 ? 2.5882 1.6732 1.9432 0.6589 -0.4480 0.0106 27 ARG D C 3085 O O . ARG B 27 ? 2.5879 1.7013 1.9758 0.6308 -0.4288 0.0262 27 ARG D O 3086 C CB . ARG B 27 ? 2.7805 1.7816 2.0040 0.7076 -0.4492 0.0098 27 ARG D CB 3087 C CG . ARG B 27 ? 2.8716 1.8359 2.0231 0.7268 -0.4332 0.0191 27 ARG D CG 3088 C CD . ARG B 27 ? 2.8820 1.8001 1.9711 0.7472 -0.4442 0.0176 27 ARG D CD 3089 N NE . ARG B 27 ? 2.9449 1.8271 1.9621 0.7645 -0.4295 0.0268 27 ARG D NE 3090 C CZ . ARG B 27 ? 3.0426 1.8814 1.9962 0.7815 -0.4328 0.0309 27 ARG D CZ 3091 N NH1 . ARG B 27 ? 3.0711 1.8958 2.0240 0.7856 -0.4503 0.0269 27 ARG D NH1 3092 N NH2 . ARG B 27 ? 3.0805 1.8899 1.9705 0.7949 -0.4184 0.0395 27 ARG D NH2 3093 N N . ARG B 28 ? 2.6084 1.6938 1.9824 0.6697 -0.4803 -0.0124 28 ARG D N 3094 C CA . ARG B 28 ? 2.5833 1.6996 2.0148 0.6504 -0.4954 -0.0207 28 ARG D CA 3095 C C . ARG B 28 ? 2.5106 1.6737 2.0129 0.6284 -0.4978 -0.0241 28 ARG D C 3096 O O . ARG B 28 ? 2.5248 1.7167 2.0774 0.6115 -0.5117 -0.0326 28 ARG D O 3097 C CB . ARG B 28 ? 2.6089 1.7073 2.0282 0.6710 -0.5295 -0.0433 28 ARG D CB 3098 C CG . ARG B 28 ? 2.6533 1.7097 2.0126 0.6899 -0.5298 -0.0390 28 ARG D CG 3099 C CD . ARG B 28 ? 2.7236 1.7825 2.0990 0.6958 -0.5567 -0.0547 28 ARG D CD 3100 N NE . ARG B 28 ? 2.8559 1.9105 2.2319 0.6819 -0.5412 -0.0414 28 ARG D NE 3101 C CZ . ARG B 28 ? 2.8887 1.9382 2.2694 0.6882 -0.5571 -0.0499 28 ARG D CZ 3102 N NH1 . ARG B 28 ? 2.9560 2.0083 2.3426 0.7082 -0.5905 -0.0714 28 ARG D NH1 3103 N NH2 . ARG B 28 ? 2.7995 1.8415 2.1786 0.6742 -0.5390 -0.0371 28 ARG D NH2 3104 N N . SER B 29 ? 2.4371 1.6082 1.9438 0.6288 -0.4842 -0.0172 29 SER D N 3105 C CA . SER B 29 ? 2.3251 1.5363 1.8963 0.6108 -0.4880 -0.0202 29 SER D CA 3106 C C . SER B 29 ? 2.3560 1.5782 1.9320 0.6090 -0.4642 -0.0050 29 SER D C 3107 O O . SER B 29 ? 2.3680 1.5676 1.8961 0.6224 -0.4447 0.0067 29 SER D O 3108 C CB . SER B 29 ? 2.2917 1.4970 1.8748 0.6245 -0.5218 -0.0478 29 SER D CB 3109 O OG . SER B 29 ? 2.2017 1.4475 1.8529 0.6016 -0.5304 -0.0526 29 SER D OG 3110 N N . PHE B 30 ? 2.4014 1.6585 2.0357 0.5932 -0.4669 -0.0055 30 PHE D N 3111 C CA . PHE B 30 ? 2.4188 1.6954 2.0715 0.5885 -0.4442 0.0110 30 PHE D CA 3112 C C . PHE B 30 ? 2.4686 1.7093 2.0720 0.6190 -0.4386 0.0067 30 PHE D C 3113 O O . PHE B 30 ? 2.4173 1.6220 1.9851 0.6425 -0.4592 -0.0149 30 PHE D O 3114 C CB . PHE B 30 ? 2.3098 1.6241 2.0323 0.5698 -0.4543 0.0074 30 PHE D CB 3115 C CG . PHE B 30 ? 2.2875 1.5833 2.0146 0.5836 -0.4860 -0.0210 30 PHE D CG 3116 C CD1 . PHE B 30 ? 2.2206 1.4924 1.9298 0.6049 -0.4884 -0.0305 30 PHE D CD1 3117 C CD2 . PHE B 30 ? 2.2793 1.5818 2.0271 0.5749 -0.5128 -0.0391 30 PHE D CD2 3118 C CE1 . PHE B 30 ? 2.1609 1.4147 1.8713 0.6152 -0.5170 -0.0575 30 PHE D CE1 3119 C CE2 . PHE B 30 ? 2.2032 1.4915 1.9538 0.5859 -0.5421 -0.0656 30 PHE D CE2 3120 C CZ . PHE B 30 ? 2.1329 1.3962 1.8639 0.6052 -0.5442 -0.0749 30 PHE D CZ 3121 N N . GLU B 31 ? 2.5444 1.7981 2.1462 0.6176 -0.4098 0.0275 31 GLU D N 3122 C CA . GLU B 31 ? 2.6712 1.8969 2.2305 0.6443 -0.3989 0.0264 31 GLU D CA 3123 C C . GLU B 31 ? 2.7182 1.9342 2.2963 0.6573 -0.4158 0.0072 31 GLU D C 3124 O O . GLU B 31 ? 2.7248 1.9695 2.3613 0.6406 -0.4244 0.0058 31 GLU D O 3125 C CB . GLU B 31 ? 2.6913 1.9435 2.2556 0.6364 -0.3633 0.0547 31 GLU D CB 3126 C CG . GLU B 31 ? 2.7111 2.0193 2.3456 0.6055 -0.3530 0.0730 31 GLU D CG 3127 C CD . GLU B 31 ? 2.8159 2.1449 2.4735 0.5779 -0.3593 0.0765 31 GLU D CD 3128 O OE1 . GLU B 31 ? 2.8161 2.1674 2.5248 0.5615 -0.3776 0.0681 31 GLU D OE1 3129 O OE2 . GLU B 31 ? 2.8838 2.2054 2.5070 0.5723 -0.3458 0.0870 31 GLU D OE2 3130 N N . VAL B 32 ? 2.7187 1.8933 2.2456 0.6860 -0.4199 -0.0075 32 VAL D N 3131 C CA . VAL B 32 ? 2.6477 1.8045 2.1819 0.7000 -0.4353 -0.0286 32 VAL D CA 3132 C C . VAL B 32 ? 2.7413 1.8645 2.2239 0.7279 -0.4207 -0.0319 32 VAL D C 3133 O O . VAL B 32 ? 2.8651 1.9682 2.2930 0.7406 -0.4093 -0.0264 32 VAL D O 3134 C CB . VAL B 32 ? 2.5485 1.6830 2.0715 0.7053 -0.4709 -0.0572 32 VAL D CB 3135 C CG1 . VAL B 32 ? 2.5154 1.6833 2.0896 0.6788 -0.4861 -0.0565 32 VAL D CG1 3136 C CG2 . VAL B 32 ? 2.5108 1.6076 1.9630 0.7261 -0.4764 -0.0653 32 VAL D CG2 3137 N N . CYS B 33 ? 2.6612 1.7766 2.1597 0.7373 -0.4209 -0.0414 33 CYS D N 3138 C CA . CYS B 33 ? 2.6322 1.7145 2.0836 0.7645 -0.4069 -0.0474 33 CYS D CA 3139 C C . CYS B 33 ? 2.6444 1.6794 2.0366 0.7853 -0.4288 -0.0760 33 CYS D C 3140 O O . CYS B 33 ? 2.6236 1.6482 2.0256 0.7825 -0.4577 -0.0987 33 CYS D O 3141 C CB . CYS B 33 ? 2.5511 1.6385 2.0385 0.7687 -0.3967 -0.0469 33 CYS D CB 3142 S SG . CYS B 33 ? 2.7861 1.9285 2.3315 0.7519 -0.3643 -0.0095 33 CYS D SG 3143 N N . VAL B 34 ? 2.6165 1.6255 1.9466 0.8051 -0.4149 -0.0744 34 VAL D N 3144 C CA . VAL B 34 ? 2.5785 1.5450 1.8462 0.8247 -0.4335 -0.0982 34 VAL D CA 3145 C C . VAL B 34 ? 2.6364 1.5767 1.8497 0.8479 -0.4105 -0.0972 34 VAL D C 3146 O O . VAL B 34 ? 2.3848 1.3433 1.6102 0.8477 -0.3809 -0.0764 34 VAL D O 3147 C CB . VAL B 34 ? 2.5499 1.5146 1.7906 0.8200 -0.4464 -0.0946 34 VAL D CB 3148 C CG1 . VAL B 34 ? 2.4397 1.4392 1.7397 0.7944 -0.4598 -0.0883 34 VAL D CG1 3149 C CG2 . VAL B 34 ? 2.5942 1.5584 1.7959 0.8239 -0.4188 -0.0710 34 VAL D CG2 3150 N N . PRO B 35 ? 2.7002 1.6006 1.8527 0.8674 -0.4239 -0.1192 35 PRO D N 3151 C CA . PRO B 35 ? 2.7922 1.6634 1.8879 0.8904 -0.4056 -0.1241 35 PRO D CA 3152 C C . PRO B 35 ? 2.9562 1.8348 2.0195 0.8940 -0.3762 -0.0989 35 PRO D C 3153 O O . PRO B 35 ? 2.9904 1.8718 2.0325 0.8876 -0.3796 -0.0876 35 PRO D O 3154 C CB . PRO B 35 ? 2.7592 1.5933 1.7983 0.9039 -0.4326 -0.1507 35 PRO D CB 3155 C CG . PRO B 35 ? 2.7302 1.5722 1.8091 0.8911 -0.4639 -0.1669 35 PRO D CG 3156 C CD . PRO B 35 ? 2.7079 1.5910 1.8473 0.8679 -0.4602 -0.1441 35 PRO D CD 3157 N N . LYS B 36 ? 3.1261 2.0067 2.1843 0.9047 -0.3472 -0.0908 36 LYS D N 3158 C CA . LYS B 36 ? 3.3195 2.2082 2.3442 0.9087 -0.3175 -0.0685 36 LYS D CA 3159 C C . LYS B 36 ? 3.6510 2.5059 2.5997 0.9200 -0.3270 -0.0766 36 LYS D C 3160 O O . LYS B 36 ? 3.7034 2.5237 2.6142 0.9346 -0.3467 -0.1023 36 LYS D O 3161 C CB . LYS B 36 ? 3.3082 2.1980 2.3309 0.9241 -0.2886 -0.0658 36 LYS D CB 3162 N N . THR B 37 ? 3.8941 2.7590 2.8198 0.9123 -0.3129 -0.0542 37 THR D N 3163 C CA . THR B 37 ? 4.1445 2.9792 3.0022 0.9199 -0.3232 -0.0574 37 THR D CA 3164 C C . THR B 37 ? 4.4757 3.3059 3.2809 0.9268 -0.2928 -0.0406 37 THR D C 3165 O O . THR B 37 ? 4.4752 3.3369 3.3049 0.9162 -0.2647 -0.0177 37 THR D O 3166 C CB . THR B 37 ? 4.0062 2.8505 2.8797 0.9020 -0.3395 -0.0467 37 THR D CB 3167 O OG1 . THR B 37 ? 3.8840 2.7522 2.8277 0.8875 -0.3564 -0.0522 37 THR D OG1 3168 C CG2 . THR B 37 ? 4.0448 2.8523 2.8596 0.9138 -0.3651 -0.0604 37 THR D CG2 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 GLY 1 14 ? ? ? A . n A 1 2 GLN 2 15 ? ? ? A . n A 1 3 PRO 3 16 ? ? ? A . n A 1 4 VAL 4 17 ? ? ? A . n A 1 5 SER 5 18 ? ? ? A . n A 1 6 ILE 6 19 ? ? ? A . n A 1 7 GLN 7 20 ? ? ? A . n A 1 8 ALA 8 21 ? ? ? A . n A 1 9 PHE 9 22 ? ? ? A . n A 1 10 ALA 10 23 ? ? ? A . n A 1 11 SER 11 24 ? ? ? A . n A 1 12 SER 12 25 ? ? ? A . n A 1 13 SER 13 26 ? ? ? A . n A 1 14 THR 14 27 ? ? ? A . n A 1 15 LEU 15 28 ? ? ? A . n A 1 16 HIS 16 29 ? ? ? A . n A 1 17 GLY 17 30 ? ? ? A . n A 1 18 ILE 18 31 ? ? ? A . n A 1 19 SER 19 32 ? ? ? A . n A 1 20 HIS 20 33 ? ? ? A . n A 1 21 ILE 21 34 ? ? ? A . n A 1 22 PHE 22 35 ? ? ? A . n A 1 23 SER 23 36 ? ? ? A . n A 1 24 TYR 24 37 ? ? ? A . n A 1 25 GLU 25 38 ? ? ? A . n A 1 26 ARG 26 39 ? ? ? A . n A 1 27 LEU 27 40 ? ? ? A . n A 1 28 SER 28 41 41 SER ALA A . n A 1 29 LEU 29 42 42 LEU ALA A . n A 1 30 LYS 30 43 43 LYS ALA A . n A 1 31 ARG 31 44 44 ARG ALA A . n A 1 32 VAL 32 45 45 VAL VAL A . n A 1 33 VAL 33 46 46 VAL VAL A . n A 1 34 TRP 34 47 47 TRP ALA A . n A 1 35 ALA 35 48 48 ALA ALA A . n A 1 36 LEU 36 49 49 LEU ALA A . n A 1 37 CYS 37 50 50 CYS ALA A . n A 1 38 PHE 38 51 51 PHE ALA A . n A 1 39 MET 39 52 52 MET ALA A . n A 1 40 GLY 40 53 53 GLY GLY A . n A 1 41 SER 41 54 54 SER ALA A . n A 1 42 LEU 42 55 55 LEU ALA A . n A 1 43 ALA 43 56 56 ALA ALA A . n A 1 44 LEU 44 57 57 LEU LEU A . n A 1 45 LEU 45 58 58 LEU ALA A . n A 1 46 ALA 46 59 59 ALA ALA A . n A 1 47 LEU 47 60 60 LEU ALA A . n A 1 48 VAL 48 61 61 VAL ALA A . n A 1 49 CYS 49 62 62 CYS CYS A . n A 1 50 THR 50 63 63 THR THR A . n A 1 51 ASN 51 64 64 ASN ASN A . n A 1 52 ARG 52 65 65 ARG ALA A . n A 1 53 ILE 53 66 66 ILE ILE A . n A 1 54 GLN 54 67 67 GLN ALA A . n A 1 55 TYR 55 68 68 TYR ALA A . n A 1 56 TYR 56 69 69 TYR TYR A . n A 1 57 PHE 57 70 70 PHE ALA A . n A 1 58 LEU 58 71 71 LEU ALA A . n A 1 59 TYR 59 72 72 TYR TYR A . n A 1 60 PRO 60 73 73 PRO PRO A . n A 1 61 HIS 61 74 74 HIS HIS A . n A 1 62 VAL 62 75 75 VAL VAL A . n A 1 63 THR 63 76 76 THR THR A . n A 1 64 LYS 64 77 77 LYS ALA A . n A 1 65 LEU 65 78 78 LEU LEU A . n A 1 66 ASP 66 79 79 ASP ASP A . n A 1 67 GLU 67 80 80 GLU GLU A . n A 1 68 VAL 68 81 81 VAL VAL A . n A 1 69 ALA 69 82 82 ALA ALA A . n A 1 70 ALA 70 83 83 ALA ALA A . n A 1 71 THR 71 84 84 THR THR A . n A 1 72 ARG 72 85 85 ARG ALA A . n A 1 73 LEU 73 86 86 LEU LEU A . n A 1 74 THR 74 87 87 THR THR A . n A 1 75 PHE 75 88 88 PHE PHE A . n A 1 76 PRO 76 89 89 PRO PRO A . n A 1 77 ALA 77 90 90 ALA ALA A . n A 1 78 VAL 78 91 91 VAL VAL A . n A 1 79 THR 79 92 92 THR THR A . n A 1 80 PHE 80 93 93 PHE PHE A . n A 1 81 CYS 81 94 94 CYS CYS A . n A 1 82 ASN 82 95 95 ASN ASN A . n A 1 83 LEU 83 96 96 LEU LEU A . n A 1 84 ASN 84 97 97 ASN ASN A . n A 1 85 GLU 85 98 98 GLU GLU A . n A 1 86 PHE 86 99 99 PHE PHE A . n A 1 87 ARG 87 100 100 ARG ARG A . n A 1 88 PHE 88 101 101 PHE PHE A . n A 1 89 SER 89 102 102 SER SER A . n A 1 90 ARG 90 103 103 ARG ARG A . n A 1 91 VAL 91 104 104 VAL VAL A . n A 1 92 THR 92 105 105 THR THR A . n A 1 93 LYS 93 106 106 LYS ALA A . n A 1 94 ASN 94 107 107 ASN ASN A . n A 1 95 ASP 95 108 108 ASP ASP A . n A 1 96 LEU 96 109 109 LEU ALA A . n A 1 97 TYR 97 110 110 TYR TYR A . n A 1 98 HIS 98 111 111 HIS HIS A . n A 1 99 ALA 99 112 112 ALA ALA A . n A 1 100 GLY 100 113 113 GLY GLY A . n A 1 101 GLU 101 114 114 GLU GLU A . n A 1 102 LEU 102 115 115 LEU LEU A . n A 1 103 LEU 103 116 116 LEU LEU A . n A 1 104 ALA 104 117 117 ALA ALA A . n A 1 105 LEU 105 118 118 LEU ALA A . n A 1 106 LEU 106 119 119 LEU LEU A . n A 1 107 ASN 107 120 120 ASN ALA A . n A 1 108 ASN 108 121 121 ASN ASN A . n A 1 109 ARG 109 122 122 ARG ALA A . n A 1 110 TYR 110 123 123 TYR TYR A . n A 1 111 GLU 111 124 124 GLU ALA A . n A 1 112 ILE 112 125 125 ILE ILE A . n A 1 113 PRO 113 126 126 PRO PRO A . n A 1 114 ASP 114 127 127 ASP ASP A . n A 1 115 THR 115 128 128 THR THR A . n A 1 116 GLN 116 129 129 GLN ALA A . n A 1 117 THR 117 130 130 THR THR A . n A 1 118 ALA 118 131 131 ALA ALA A . n A 1 119 ASP 119 132 132 ASP ALA A . n A 1 120 GLU 120 133 133 GLU GLU A . n A 1 121 LYS 121 134 134 LYS ALA A . n A 1 122 GLN 122 135 135 GLN ALA A . n A 1 123 LEU 123 136 136 LEU ALA A . n A 1 124 GLU 124 137 137 GLU ALA A . n A 1 125 ILE 125 138 138 ILE ILE A . n A 1 126 LEU 126 139 139 LEU LEU A . n A 1 127 GLN 127 140 140 GLN GLN A . n A 1 128 ASP 128 141 141 ASP ASP A . n A 1 129 LYS 129 142 142 LYS ALA A . n A 1 130 ALA 130 143 143 ALA ALA A . n A 1 131 ASN 131 144 144 ASN ASN A . n A 1 132 PHE 132 145 145 PHE PHE A . n A 1 133 ARG 133 146 146 ARG ARG A . n A 1 134 ASN 134 147 147 ASN ALA A . n A 1 135 PHE 135 148 148 PHE ALA A . n A 1 136 LYS 136 149 149 LYS ALA A . n A 1 137 PRO 137 150 150 PRO PRO A . n A 1 138 LYS 138 151 151 LYS ALA A . n A 1 139 PRO 139 152 152 PRO PRO A . n A 1 140 PHE 140 153 153 PHE PHE A . n A 1 141 ASN 141 154 154 ASN ASN A . n A 1 142 MET 142 155 155 MET ALA A . n A 1 143 LEU 143 156 156 LEU LEU A . n A 1 144 GLU 144 157 157 GLU GLU A . n A 1 145 PHE 145 158 158 PHE PHE A . n A 1 146 TYR 146 159 159 TYR TYR A . n A 1 147 ASP 147 160 160 ASP ASP A . n A 1 148 ARG 148 161 161 ARG ALA A . n A 1 149 ALA 149 162 162 ALA ALA A . n A 1 150 GLY 150 163 163 GLY GLY A . n A 1 151 HIS 151 164 164 HIS HIS A . n A 1 152 ASP 152 165 165 ASP ASP A . n A 1 153 ILE 153 166 166 ILE ILE A . n A 1 154 ARG 154 167 167 ARG ALA A . n A 1 155 GLU 155 168 168 GLU GLU A . n A 1 156 MET 156 169 169 MET MET A . n A 1 157 LEU 157 170 170 LEU LEU A . n A 1 158 LEU 158 171 171 LEU LEU A . n A 1 159 SER 159 172 172 SER SER A . n A 1 160 CYS 160 173 173 CYS CYS A . n A 1 161 PHE 161 174 174 PHE PHE A . n A 1 162 PHE 162 175 175 PHE PHE A . n A 1 163 ARG 163 176 176 ARG ARG A . n A 1 164 GLY 164 177 177 GLY GLY A . n A 1 165 GLU 165 178 178 GLU ALA A . n A 1 166 GLN 166 179 179 GLN GLN A . n A 1 167 CYS 167 180 180 CYS CYS A . n A 1 168 SER 168 181 181 SER SER A . n A 1 169 PRO 169 182 182 PRO PRO A . n A 1 170 GLU 170 183 183 GLU GLU A . n A 1 171 ASP 171 184 184 ASP ASP A . n A 1 172 PHE 172 185 185 PHE PHE A . n A 1 173 LYS 173 186 186 LYS ALA A . n A 1 174 VAL 174 187 187 VAL VAL A . n A 1 175 VAL 175 188 188 VAL VAL A . n A 1 176 PHE 176 189 189 PHE PHE A . n A 1 177 THR 177 190 190 THR THR A . n A 1 178 ARG 178 191 191 ARG ALA A . n A 1 179 TYR 179 192 192 TYR TYR A . n A 1 180 GLY 180 193 193 GLY GLY A . n A 1 181 LYS 181 194 194 LYS LYS A . n A 1 182 CYS 182 195 195 CYS CYS A . n A 1 183 TYR 183 196 196 TYR TYR A . n A 1 184 THR 184 197 197 THR THR A . n A 1 185 PHE 185 198 198 PHE PHE A . n A 1 186 ASN 186 199 199 ASN ASN A . n A 1 187 ALA 187 200 200 ALA ALA A . n A 1 188 GLY 188 201 201 GLY GLY A . n A 1 189 GLN 189 202 202 GLN ALA A . n A 1 190 ASP 190 203 203 ASP ASP A . n A 1 191 GLY 191 204 204 GLY GLY A . n A 1 192 LYS 192 205 205 LYS ALA A . n A 1 193 PRO 193 206 206 PRO PRO A . n A 1 194 ARG 194 207 207 ARG ARG A . n A 1 195 LEU 195 208 208 LEU LEU A . n A 1 196 ILE 196 209 209 ILE ILE A . n A 1 197 THR 197 210 210 THR THR A . n A 1 198 MET 198 211 211 MET MET A . n A 1 199 LYS 199 212 212 LYS ALA A . n A 1 200 GLY 200 213 213 GLY GLY A . n A 1 201 GLY 201 214 214 GLY GLY A . n A 1 202 THR 202 215 215 THR THR A . n A 1 203 GLY 203 216 216 GLY GLY A . n A 1 204 ASN 204 217 217 ASN ASN A . n A 1 205 GLY 205 218 218 GLY GLY A . n A 1 206 LEU 206 219 219 LEU LEU A . n A 1 207 GLU 207 220 220 GLU GLU A . n A 1 208 ILE 208 221 221 ILE ILE A . n A 1 209 MET 209 222 222 MET MET A . n A 1 210 LEU 210 223 223 LEU LEU A . n A 1 211 ASP 211 224 224 ASP ASP A . n A 1 212 ILE 212 225 225 ILE ALA A . n A 1 213 GLN 213 226 226 GLN GLN A . n A 1 214 GLN 214 227 227 GLN GLN A . n A 1 215 ASP 215 228 228 ASP ALA A . n A 1 216 GLU 216 229 229 GLU ALA A . n A 1 217 TYR 217 230 230 TYR TYR A . n A 1 218 LEU 218 231 231 LEU LEU A . n A 1 219 PRO 219 232 232 PRO PRO A . n A 1 220 VAL 220 233 233 VAL VAL A . n A 1 221 TRP 221 234 234 TRP TRP A . n A 1 222 GLY 222 235 235 GLY GLY A . n A 1 223 GLU 223 236 236 GLU GLU A . n A 1 224 THR 224 237 237 THR THR A . n A 1 225 ASP 225 238 238 ASP ASP A . n A 1 226 GLU 226 239 239 GLU GLU A . n A 1 227 THR 227 240 240 THR THR A . n A 1 228 SER 228 241 241 SER SER A . n A 1 229 PHE 229 242 242 PHE PHE A . n A 1 230 GLU 230 243 243 GLU GLU A . n A 1 231 ALA 231 244 244 ALA ALA A . n A 1 232 GLY 232 245 245 GLY GLY A . n A 1 233 ILE 233 246 246 ILE ILE A . n A 1 234 LYS 234 247 247 LYS LYS A . n A 1 235 VAL 235 248 248 VAL VAL A . n A 1 236 GLN 236 249 249 GLN GLN A . n A 1 237 ILE 237 250 250 ILE ILE A . n A 1 238 HIS 238 251 251 HIS HIS A . n A 1 239 SER 239 252 252 SER SER A . n A 1 240 GLN 240 253 253 GLN GLN A . n A 1 241 ASP 241 254 254 ASP ASP A . n A 1 242 GLU 242 255 255 GLU GLU A . n A 1 243 PRO 243 256 256 PRO PRO A . n A 1 244 PRO 244 257 257 PRO PRO A . n A 1 245 LEU 245 258 258 LEU ALA A . n A 1 246 ILE 246 259 259 ILE ILE A . n A 1 247 ASP 247 260 260 ASP ASP A . n A 1 248 GLN 248 261 261 GLN GLN A . n A 1 249 LEU 249 262 262 LEU LEU A . n A 1 250 GLY 250 263 263 GLY GLY A . n A 1 251 PHE 251 264 264 PHE PHE A . n A 1 252 GLY 252 265 265 GLY GLY A . n A 1 253 VAL 253 266 266 VAL VAL A . n A 1 254 ALA 254 267 267 ALA ALA A . n A 1 255 PRO 255 268 268 PRO PRO A . n A 1 256 GLY 256 269 269 GLY GLY A . n A 1 257 PHE 257 270 270 PHE PHE A . n A 1 258 GLN 258 271 271 GLN GLN A . n A 1 259 THR 259 272 272 THR THR A . n A 1 260 PHE 260 273 273 PHE PHE A . n A 1 261 VAL 261 274 274 VAL VAL A . n A 1 262 SER 262 275 275 SER SER A . n A 1 263 CYS 263 276 276 CYS CYS A . n A 1 264 GLN 264 277 277 GLN GLN A . n A 1 265 GLU 265 278 278 GLU GLU A . n A 1 266 GLN 266 279 279 GLN GLN A . n A 1 267 ARG 267 280 280 ARG ARG A . n A 1 268 LEU 268 281 281 LEU LEU A . n A 1 269 ILE 269 282 282 ILE ILE A . n A 1 270 TYR 270 283 283 TYR TYR A . n A 1 271 LEU 271 284 284 LEU LEU A . n A 1 272 PRO 272 285 285 PRO PRO A . n A 1 273 PRO 273 286 286 PRO PRO A . n A 1 274 PRO 274 287 287 PRO PRO A . n A 1 275 TRP 275 288 288 TRP TRP A . n A 1 276 GLY 276 289 289 GLY GLY A . n A 1 277 ASP 277 290 290 ASP ASP A . n A 1 278 CYS 278 291 291 CYS CYS A . n A 1 279 LYS 279 292 292 LYS ALA A . n A 1 280 ALA 280 293 293 ALA ALA A . n A 1 281 THR 281 294 294 THR ALA A . n A 1 282 THR 282 295 295 THR THR A . n A 1 283 GLY 283 296 296 GLY GLY A . n A 1 284 ASP 284 297 297 ASP ALA A . n A 1 285 SER 285 298 ? ? ? A . n A 1 286 GLU 286 299 ? ? ? A . n A 1 287 PHE 287 300 ? ? ? A . n A 1 288 TYR 288 301 ? ? ? A . n A 1 289 ASP 289 302 302 ASP ALA A . n A 1 290 THR 290 303 303 THR ALA A . n A 1 291 TYR 291 304 304 TYR TYR A . n A 1 292 SER 292 305 305 SER SER A . n A 1 293 ILE 293 306 306 ILE ILE A . n A 1 294 THR 294 307 307 THR THR A . n A 1 295 ALA 295 308 308 ALA ALA A . n A 1 296 CYS 296 309 309 CYS CYS A . n A 1 297 ARG 297 310 310 ARG ARG A . n A 1 298 ILE 298 311 311 ILE ILE A . n A 1 299 ASP 299 312 312 ASP ASP A . n A 1 300 CYS 300 313 313 CYS CYS A . n A 1 301 GLU 301 314 314 GLU GLU A . n A 1 302 THR 302 315 315 THR THR A . n A 1 303 ARG 303 316 316 ARG ALA A . n A 1 304 TYR 304 317 317 TYR TYR A . n A 1 305 LEU 305 318 318 LEU ALA A . n A 1 306 VAL 306 319 319 VAL VAL A . n A 1 307 GLU 307 320 320 GLU GLU A . n A 1 308 ASN 308 321 321 ASN ASN A . n A 1 309 CYS 309 322 322 CYS CYS A . n A 1 310 ASN 310 323 323 ASN ASN A . n A 1 311 CYS 311 324 324 CYS CYS A . n A 1 312 ARG 312 325 325 ARG ARG A . n A 1 313 MET 313 326 326 MET MET A . n A 1 314 VAL 314 327 327 VAL VAL A . n A 1 315 HIS 315 328 328 HIS HIS A . n A 1 316 MET 316 329 329 MET MET A . n A 1 317 PRO 317 330 330 PRO PRO A . n A 1 318 GLY 318 331 331 GLY GLY A . n A 1 319 ASP 319 332 332 ASP ASP A . n A 1 320 ALA 320 333 333 ALA ALA A . n A 1 321 PRO 321 334 334 PRO PRO A . n A 1 322 TYR 322 335 335 TYR TYR A . n A 1 323 CYS 323 336 336 CYS CYS A . n A 1 324 THR 324 337 337 THR THR A . n A 1 325 PRO 325 338 338 PRO PRO A . n A 1 326 GLU 326 339 339 GLU GLU A . n A 1 327 GLN 327 340 340 GLN GLN A . n A 1 328 TYR 328 341 341 TYR TYR A . n A 1 329 LYS 329 342 342 LYS ALA A . n A 1 330 GLU 330 343 343 GLU ALA A . n A 1 331 CYS 331 344 344 CYS CYS A . n A 1 332 ALA 332 345 345 ALA ALA A . n A 1 333 ASP 333 346 346 ASP ASP A . n A 1 334 PRO 334 347 347 PRO PRO A . n A 1 335 ALA 335 348 348 ALA ALA A . n A 1 336 LEU 336 349 349 LEU LEU A . n A 1 337 ASP 337 350 350 ASP ASP A . n A 1 338 PHE 338 351 351 PHE PHE A . n A 1 339 LEU 339 352 352 LEU LEU A . n A 1 340 VAL 340 353 353 VAL VAL A . n A 1 341 GLU 341 354 354 GLU ALA A . n A 1 342 LYS 342 355 355 LYS ALA A . n A 1 343 ASP 343 356 356 ASP ALA A . n A 1 344 ASN 344 357 357 ASN ALA A . n A 1 345 GLU 345 358 358 GLU ALA A . n A 1 346 TYR 346 359 359 TYR TYR A . n A 1 347 CYS 347 360 360 CYS CYS A . n A 1 348 VAL 348 361 361 VAL VAL A . n A 1 349 CYS 349 362 362 CYS CYS A . n A 1 350 GLU 350 363 363 GLU ALA A . n A 1 351 MET 351 364 364 MET ALA A . n A 1 352 PRO 352 365 365 PRO PRO A . n A 1 353 CYS 353 366 366 CYS CYS A . n A 1 354 ASN 354 367 367 ASN ASN A . n A 1 355 VAL 355 368 368 VAL VAL A . n A 1 356 THR 356 369 369 THR THR A . n A 1 357 ARG 357 370 370 ARG ARG A . n A 1 358 TYR 358 371 371 TYR TYR A . n A 1 359 GLY 359 372 372 GLY GLY A . n A 1 360 LYS 360 373 373 LYS LYS A . n A 1 361 GLU 361 374 374 GLU ALA A . n A 1 362 LEU 362 375 375 LEU LEU A . n A 1 363 SER 363 376 376 SER SER A . n A 1 364 MET 364 377 377 MET MET A . n A 1 365 VAL 365 378 378 VAL VAL A . n A 1 366 LYS 366 379 379 LYS ALA A . n A 1 367 ILE 367 380 380 ILE ILE A . n A 1 368 PRO 368 381 381 PRO PRO A . n A 1 369 SER 369 382 382 SER SER A . n A 1 370 LYS 370 383 383 LYS LYS A . n A 1 371 ALA 371 384 384 ALA ALA A . n A 1 372 SER 372 385 385 SER SER A . n A 1 373 ALA 373 386 386 ALA ALA A . n A 1 374 LYS 374 387 387 LYS ALA A . n A 1 375 TYR 375 388 388 TYR TYR A . n A 1 376 LEU 376 389 389 LEU LEU A . n A 1 377 ALA 377 390 390 ALA ALA A . n A 1 378 LYS 378 391 391 LYS LYS A . n A 1 379 LYS 379 392 392 LYS LYS A . n A 1 380 TYR 380 393 393 TYR TYR A . n A 1 381 ASN 381 394 394 ASN ASN A . n A 1 382 LYS 382 395 395 LYS ALA A . n A 1 383 SER 383 396 396 SER SER A . n A 1 384 GLU 384 397 397 GLU GLU A . n A 1 385 GLN 385 398 398 GLN GLN A . n A 1 386 TYR 386 399 399 TYR TYR A . n A 1 387 ILE 387 400 400 ILE ILE A . n A 1 388 GLY 388 401 401 GLY GLY A . n A 1 389 GLU 389 402 402 GLU GLU A . n A 1 390 ASN 390 403 403 ASN ASN A . n A 1 391 ILE 391 404 404 ILE ILE A . n A 1 392 LEU 392 405 405 LEU LEU A . n A 1 393 VAL 393 406 406 VAL VAL A . n A 1 394 LEU 394 407 407 LEU LEU A . n A 1 395 ASP 395 408 408 ASP ASP A . n A 1 396 ILE 396 409 409 ILE ILE A . n A 1 397 PHE 397 410 410 PHE PHE A . n A 1 398 PHE 398 411 411 PHE PHE A . n A 1 399 GLU 399 412 412 GLU GLU A . n A 1 400 ALA 400 413 413 ALA ALA A . n A 1 401 LEU 401 414 414 LEU LEU A . n A 1 402 ASN 402 415 415 ASN ASN A . n A 1 403 TYR 403 416 416 TYR TYR A . n A 1 404 GLU 404 417 417 GLU GLU A . n A 1 405 THR 405 418 418 THR THR A . n A 1 406 ILE 406 419 419 ILE ILE A . n A 1 407 GLU 407 420 420 GLU GLU A . n A 1 408 GLN 408 421 421 GLN ALA A . n A 1 409 LYS 409 422 422 LYS ALA A . n A 1 410 LYS 410 423 423 LYS ALA A . n A 1 411 ALA 411 424 424 ALA ALA A . n A 1 412 TYR 412 425 425 TYR TYR A . n A 1 413 GLU 413 426 426 GLU GLU A . n A 1 414 VAL 414 427 427 VAL ALA A . n A 1 415 ALA 415 428 428 ALA ALA A . n A 1 416 GLY 416 429 429 GLY GLY A . n A 1 417 LEU 417 430 430 LEU ALA A . n A 1 418 LEU 418 431 431 LEU ALA A . n A 1 419 GLY 419 432 432 GLY GLY A . n A 1 420 ASP 420 433 433 ASP ALA A . n A 1 421 ILE 421 434 434 ILE ALA A . n A 1 422 GLY 422 435 435 GLY GLY A . n A 1 423 GLY 423 436 436 GLY GLY A . n A 1 424 GLN 424 437 437 GLN ALA A . n A 1 425 MET 425 438 438 MET ALA A . n A 1 426 GLY 426 439 439 GLY GLY A . n A 1 427 LEU 427 440 440 LEU ALA A . n A 1 428 PHE 428 441 441 PHE PHE A . n A 1 429 ILE 429 442 442 ILE ALA A . n A 1 430 GLY 430 443 443 GLY GLY A . n A 1 431 ALA 431 444 444 ALA ALA A . n A 1 432 SER 432 445 445 SER SER A . n A 1 433 ILE 433 446 446 ILE ILE A . n A 1 434 LEU 434 447 447 LEU ALA A . n A 1 435 THR 435 448 448 THR ALA A . n A 1 436 VAL 436 449 449 VAL VAL A . n A 1 437 LEU 437 450 450 LEU LEU A . n A 1 438 GLU 438 451 ? ? ? A . n A 1 439 LEU 439 452 ? ? ? A . n A 1 440 PHE 440 453 ? ? ? A . n A 1 441 ASP 441 454 ? ? ? A . n A 1 442 TYR 442 455 ? ? ? A . n A 1 443 ALA 443 456 ? ? ? A . n A 1 444 TYR 444 457 ? ? ? A . n A 1 445 GLU 445 458 ? ? ? A . n A 1 446 VAL 446 459 ? ? ? A . n A 1 447 ILE 447 460 ? ? ? A . n A 1 448 LYS 448 461 ? ? ? A . n A 1 449 HIS 449 462 ? ? ? A . n A 1 450 ARG 450 463 ? ? ? A . n B 2 1 GLU 1 1 ? ? ? D . n B 2 2 ASP 2 2 2 ASP ALA D . n B 2 3 CYS 3 3 3 CYS CYS D . n B 2 4 ILE 4 4 4 ILE ALA D . n B 2 5 PRO 5 5 5 PRO PRO D . n B 2 6 LYS 6 6 6 LYS ALA D . n B 2 7 TRP 7 7 7 TRP TRP D . n B 2 8 LYS 8 8 8 LYS ALA D . n B 2 9 GLY 9 9 9 GLY GLY D . n B 2 10 CYS 10 10 10 CYS CYS D . n B 2 11 VAL 11 11 11 VAL ALA D . n B 2 12 ASN 12 12 12 ASN ASN D . n B 2 13 ARG 13 13 13 ARG ALA D . n B 2 14 HIS 14 14 ? ? ? D . n B 2 15 GLY 15 15 ? ? ? D . n B 2 16 ASP 16 16 16 ASP ALA D . n B 2 17 CYS 17 17 17 CYS CYS D . n B 2 18 CYS 18 18 18 CYS CYS D . n B 2 19 GLU 19 19 19 GLU GLU D . n B 2 20 GLY 20 20 20 GLY GLY D . n B 2 21 LEU 21 21 21 LEU LEU D . n B 2 22 GLU 22 22 22 GLU GLU D . n B 2 23 CYS 23 23 23 CYS CYS D . n B 2 24 TRP 24 24 24 TRP TRP D . n B 2 25 LYS 25 25 25 LYS LYS D . n B 2 26 ARG 26 26 26 ARG ARG D . n B 2 27 ARG 27 27 27 ARG ARG D . n B 2 28 ARG 28 28 28 ARG ARG D . n B 2 29 SER 29 29 29 SER SER D . n B 2 30 PHE 30 30 30 PHE PHE D . n B 2 31 GLU 31 31 31 GLU GLU D . n B 2 32 VAL 32 32 32 VAL VAL D . n B 2 33 CYS 33 33 33 CYS CYS D . n B 2 34 VAL 34 34 34 VAL VAL D . n B 2 35 PRO 35 35 35 PRO PRO D . n B 2 36 LYS 36 36 36 LYS ALA D . n B 2 37 THR 37 37 37 THR THR D . n B 2 38 PRO 38 38 38 PRO PRO D . n B 2 39 LYS 39 39 ? ? ? D . n B 2 40 THR 40 40 ? ? ? D . n # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 381 A ASN 394 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 354 A ASN 367 ? 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 hexameric _pdbx_struct_assembly.oligomeric_count 6 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2,3 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 16090 ? 1 MORE -65 ? 1 'SSA (A^2)' 58120 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 2_555 -y,x-y,z -0.5000000000 -0.8660254038 0.0000000000 0.0000000000 0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 3 'crystal symmetry operation' 3_555 -x+y,-x,z -0.5000000000 0.8660254038 0.0000000000 0.0000000000 -0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 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 2012-08-01 2 'Structure model' 1 1 2012-10-03 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # 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[2][2] _pdbx_refine_tls.S[3][3] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] 'X-RAY DIFFRACTION' 1 ? refined 9.5005 -8.5040 -6.5774 1.4636 1.7815 2.0759 -0.0938 -0.0865 0.2270 0.1116 0.6058 0.2692 0.2556 0.1720 0.4203 0.6447 -0.1108 -0.2173 -0.3548 -0.2711 -0.1644 0.7419 0.5354 -0.5272 'X-RAY DIFFRACTION' 2 ? refined -10.8724 -18.2346 59.9509 1.3045 0.8183 1.1041 -0.2250 0.0209 -0.1041 3.0143 0.7630 3.0999 0.1358 -0.5839 -0.8270 0.1165 0.2404 0.3929 -0.2533 -0.7458 1.1523 0.1801 1.1753 -0.9244 'X-RAY DIFFRACTION' 3 ? refined -4.9900 -17.6987 41.8631 1.5845 1.2154 0.8557 0.1210 -0.3462 -0.2297 1.2489 0.6366 2.5271 0.9258 -0.1936 -0.4108 -0.3173 1.0086 -0.4343 0.5763 -0.5749 0.2617 -1.3187 1.1481 -0.2602 'X-RAY DIFFRACTION' 4 ? refined -6.8161 -16.3524 56.8035 1.3349 0.1409 0.1616 0.1823 0.4378 -0.1355 1.6045 1.0252 1.2999 0.2023 0.0595 0.3151 -0.1384 -0.1766 0.6265 -0.8677 -1.1925 -0.1687 0.9021 1.3456 0.0540 'X-RAY DIFFRACTION' 5 ? refined -4.8065 -8.8144 8.4897 1.1376 1.0651 1.6600 -0.0348 0.0260 -0.0108 1.0996 0.5858 6.1368 -0.6591 -2.9219 1.4167 0.5834 0.4298 -0.7657 -0.6773 -0.5120 -0.3598 -0.2592 -0.1410 1.1698 'X-RAY DIFFRACTION' 6 ? refined 14.4284 -39.4748 58.8387 1.5440 1.8926 2.0640 1.4412 0.0324 0.4651 0.0784 0.0632 0.3660 0.0122 0.0056 0.0172 -0.1614 -0.1863 -0.0762 0.0207 0.0010 -0.1021 0.0117 -0.0120 0.0170 'X-RAY DIFFRACTION' 7 ? refined 12.1206 -29.8229 57.0752 2.1564 1.2361 1.5069 0.7348 -0.4179 -0.0168 1.4116 0.5270 2.4809 0.7073 -0.5294 -0.0689 0.4478 -0.6851 0.4543 0.4863 -0.4741 0.1153 -1.3671 -0.0889 0.2554 # 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.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.selection_details _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection 'X-RAY DIFFRACTION' 1 1 A 41 A 70 '( CHAIN A AND RESID 41:70 )' ? ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 71 A 258 '( CHAIN A AND RESID 71:258 )' ? ? ? ? ? 'X-RAY DIFFRACTION' 3 3 A 259 A 322 '( CHAIN A AND RESID 259:322 )' ? ? ? ? ? 'X-RAY DIFFRACTION' 4 4 A 323 A 411 '( CHAIN A AND RESID 323:411 )' ? ? ? ? ? 'X-RAY DIFFRACTION' 5 5 A 412 A 450 '( CHAIN A AND RESID 412:450 )' ? ? ? ? ? 'X-RAY DIFFRACTION' 6 6 D 2 D 20 '( CHAIN D AND RESID 2:20 )' ? ? ? ? ? 'X-RAY DIFFRACTION' 7 7 D 21 D 37 '( CHAIN D AND RESID 21:37 )' ? ? ? ? ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal ADSC 'data collection' Quantum ? 1 PHASER phasing . ? 2 PHENIX refinement '(phenix.refine: 1.7_650)' ? 3 HKL-2000 'data reduction' . ? 4 HKL-2000 'data scaling' . ? 5 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 ND2 A ASN 367 ? ? C2 A NAG 501 ? ? 1.95 2 1 ND2 A ASN 394 ? ? C2 A NAG 502 ? ? 2.07 # 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 ALA A 56 ? ? -60.06 -70.28 2 1 LEU A 60 ? ? -56.53 -70.89 3 1 TYR A 110 ? ? -60.84 -70.59 4 1 LEU A 136 ? ? -50.38 -72.59 5 1 TRP A 288 ? ? -47.55 -70.27 6 1 CYS A 344 ? ? -131.73 -63.78 7 1 LYS A 355 ? ? -76.14 -70.09 8 1 ASP A 433 ? ? -108.75 -63.24 9 1 TRP D 7 ? ? 83.84 -11.37 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A SER 41 ? OG ? A SER 28 OG 2 1 Y 1 A LEU 42 ? CG ? A LEU 29 CG 3 1 Y 1 A LEU 42 ? CD1 ? A LEU 29 CD1 4 1 Y 1 A LEU 42 ? CD2 ? A LEU 29 CD2 5 1 Y 1 A LYS 43 ? CG ? A LYS 30 CG 6 1 Y 1 A LYS 43 ? CD ? A LYS 30 CD 7 1 Y 1 A LYS 43 ? CE ? A LYS 30 CE 8 1 Y 1 A LYS 43 ? NZ ? A LYS 30 NZ 9 1 Y 1 A ARG 44 ? CG ? A ARG 31 CG 10 1 Y 1 A ARG 44 ? CD ? A ARG 31 CD 11 1 Y 1 A ARG 44 ? NE ? A ARG 31 NE 12 1 Y 1 A ARG 44 ? CZ ? A ARG 31 CZ 13 1 Y 1 A ARG 44 ? NH1 ? A ARG 31 NH1 14 1 Y 1 A ARG 44 ? NH2 ? A ARG 31 NH2 15 1 Y 1 A TRP 47 ? CG ? A TRP 34 CG 16 1 Y 1 A TRP 47 ? CD1 ? A TRP 34 CD1 17 1 Y 1 A TRP 47 ? CD2 ? A TRP 34 CD2 18 1 Y 1 A TRP 47 ? NE1 ? A TRP 34 NE1 19 1 Y 1 A TRP 47 ? CE2 ? A TRP 34 CE2 20 1 Y 1 A TRP 47 ? CE3 ? A TRP 34 CE3 21 1 Y 1 A TRP 47 ? CZ2 ? A TRP 34 CZ2 22 1 Y 1 A TRP 47 ? CZ3 ? A TRP 34 CZ3 23 1 Y 1 A TRP 47 ? CH2 ? A TRP 34 CH2 24 1 Y 1 A LEU 49 ? CG ? A LEU 36 CG 25 1 Y 1 A LEU 49 ? CD1 ? A LEU 36 CD1 26 1 Y 1 A LEU 49 ? CD2 ? A LEU 36 CD2 27 1 Y 1 A CYS 50 ? SG ? A CYS 37 SG 28 1 Y 1 A PHE 51 ? CG ? A PHE 38 CG 29 1 Y 1 A PHE 51 ? CD1 ? A PHE 38 CD1 30 1 Y 1 A PHE 51 ? CD2 ? A PHE 38 CD2 31 1 Y 1 A PHE 51 ? CE1 ? A PHE 38 CE1 32 1 Y 1 A PHE 51 ? CE2 ? A PHE 38 CE2 33 1 Y 1 A PHE 51 ? CZ ? A PHE 38 CZ 34 1 Y 1 A MET 52 ? CG ? A MET 39 CG 35 1 Y 1 A MET 52 ? SD ? A MET 39 SD 36 1 Y 1 A MET 52 ? CE ? A MET 39 CE 37 1 Y 1 A SER 54 ? OG ? A SER 41 OG 38 1 Y 1 A LEU 55 ? CG ? A LEU 42 CG 39 1 Y 1 A LEU 55 ? CD1 ? A LEU 42 CD1 40 1 Y 1 A LEU 55 ? CD2 ? A LEU 42 CD2 41 1 Y 1 A LEU 58 ? CG ? A LEU 45 CG 42 1 Y 1 A LEU 58 ? CD1 ? A LEU 45 CD1 43 1 Y 1 A LEU 58 ? CD2 ? A LEU 45 CD2 44 1 Y 1 A LEU 60 ? CG ? A LEU 47 CG 45 1 Y 1 A LEU 60 ? CD1 ? A LEU 47 CD1 46 1 Y 1 A LEU 60 ? CD2 ? A LEU 47 CD2 47 1 Y 1 A VAL 61 ? CG1 ? A VAL 48 CG1 48 1 Y 1 A VAL 61 ? CG2 ? A VAL 48 CG2 49 1 Y 1 A ARG 65 ? CG ? A ARG 52 CG 50 1 Y 1 A ARG 65 ? CD ? A ARG 52 CD 51 1 Y 1 A ARG 65 ? NE ? A ARG 52 NE 52 1 Y 1 A ARG 65 ? CZ ? A ARG 52 CZ 53 1 Y 1 A ARG 65 ? NH1 ? A ARG 52 NH1 54 1 Y 1 A ARG 65 ? NH2 ? A ARG 52 NH2 55 1 Y 1 A GLN 67 ? CG ? A GLN 54 CG 56 1 Y 1 A GLN 67 ? CD ? A GLN 54 CD 57 1 Y 1 A GLN 67 ? OE1 ? A GLN 54 OE1 58 1 Y 1 A GLN 67 ? NE2 ? A GLN 54 NE2 59 1 Y 1 A TYR 68 ? CG ? A TYR 55 CG 60 1 Y 1 A TYR 68 ? CD1 ? A TYR 55 CD1 61 1 Y 1 A TYR 68 ? CD2 ? A TYR 55 CD2 62 1 Y 1 A TYR 68 ? CE1 ? A TYR 55 CE1 63 1 Y 1 A TYR 68 ? CE2 ? A TYR 55 CE2 64 1 Y 1 A TYR 68 ? CZ ? A TYR 55 CZ 65 1 Y 1 A TYR 68 ? OH ? A TYR 55 OH 66 1 Y 1 A PHE 70 ? CG ? A PHE 57 CG 67 1 Y 1 A PHE 70 ? CD1 ? A PHE 57 CD1 68 1 Y 1 A PHE 70 ? CD2 ? A PHE 57 CD2 69 1 Y 1 A PHE 70 ? CE1 ? A PHE 57 CE1 70 1 Y 1 A PHE 70 ? CE2 ? A PHE 57 CE2 71 1 Y 1 A PHE 70 ? CZ ? A PHE 57 CZ 72 1 Y 1 A LEU 71 ? CG ? A LEU 58 CG 73 1 Y 1 A LEU 71 ? CD1 ? A LEU 58 CD1 74 1 Y 1 A LEU 71 ? CD2 ? A LEU 58 CD2 75 1 Y 1 A LYS 77 ? CG ? A LYS 64 CG 76 1 Y 1 A LYS 77 ? CD ? A LYS 64 CD 77 1 Y 1 A LYS 77 ? CE ? A LYS 64 CE 78 1 Y 1 A LYS 77 ? NZ ? A LYS 64 NZ 79 1 Y 1 A ARG 85 ? CG ? A ARG 72 CG 80 1 Y 1 A ARG 85 ? CD ? A ARG 72 CD 81 1 Y 1 A ARG 85 ? NE ? A ARG 72 NE 82 1 Y 1 A ARG 85 ? CZ ? A ARG 72 CZ 83 1 Y 1 A ARG 85 ? NH1 ? A ARG 72 NH1 84 1 Y 1 A ARG 85 ? NH2 ? A ARG 72 NH2 85 1 Y 1 A LYS 106 ? CG ? A LYS 93 CG 86 1 Y 1 A LYS 106 ? CD ? A LYS 93 CD 87 1 Y 1 A LYS 106 ? CE ? A LYS 93 CE 88 1 Y 1 A LYS 106 ? NZ ? A LYS 93 NZ 89 1 Y 1 A LEU 109 ? CG ? A LEU 96 CG 90 1 Y 1 A LEU 109 ? CD1 ? A LEU 96 CD1 91 1 Y 1 A LEU 109 ? CD2 ? A LEU 96 CD2 92 1 Y 1 A LEU 118 ? CG ? A LEU 105 CG 93 1 Y 1 A LEU 118 ? CD1 ? A LEU 105 CD1 94 1 Y 1 A LEU 118 ? CD2 ? A LEU 105 CD2 95 1 Y 1 A ASN 120 ? CG ? A ASN 107 CG 96 1 Y 1 A ASN 120 ? OD1 ? A ASN 107 OD1 97 1 Y 1 A ASN 120 ? ND2 ? A ASN 107 ND2 98 1 Y 1 A ARG 122 ? CG ? A ARG 109 CG 99 1 Y 1 A ARG 122 ? CD ? A ARG 109 CD 100 1 Y 1 A ARG 122 ? NE ? A ARG 109 NE 101 1 Y 1 A ARG 122 ? CZ ? A ARG 109 CZ 102 1 Y 1 A ARG 122 ? NH1 ? A ARG 109 NH1 103 1 Y 1 A ARG 122 ? NH2 ? A ARG 109 NH2 104 1 Y 1 A GLU 124 ? CG ? A GLU 111 CG 105 1 Y 1 A GLU 124 ? CD ? A GLU 111 CD 106 1 Y 1 A GLU 124 ? OE1 ? A GLU 111 OE1 107 1 Y 1 A GLU 124 ? OE2 ? A GLU 111 OE2 108 1 Y 1 A GLN 129 ? CG ? A GLN 116 CG 109 1 Y 1 A GLN 129 ? CD ? A GLN 116 CD 110 1 Y 1 A GLN 129 ? OE1 ? A GLN 116 OE1 111 1 Y 1 A GLN 129 ? NE2 ? A GLN 116 NE2 112 1 Y 1 A ASP 132 ? CG ? A ASP 119 CG 113 1 Y 1 A ASP 132 ? OD1 ? A ASP 119 OD1 114 1 Y 1 A ASP 132 ? OD2 ? A ASP 119 OD2 115 1 Y 1 A LYS 134 ? CG ? A LYS 121 CG 116 1 Y 1 A LYS 134 ? CD ? A LYS 121 CD 117 1 Y 1 A LYS 134 ? CE ? A LYS 121 CE 118 1 Y 1 A LYS 134 ? NZ ? A LYS 121 NZ 119 1 Y 1 A GLN 135 ? CG ? A GLN 122 CG 120 1 Y 1 A GLN 135 ? CD ? A GLN 122 CD 121 1 Y 1 A GLN 135 ? OE1 ? A GLN 122 OE1 122 1 Y 1 A GLN 135 ? NE2 ? A GLN 122 NE2 123 1 Y 1 A LEU 136 ? CG ? A LEU 123 CG 124 1 Y 1 A LEU 136 ? CD1 ? A LEU 123 CD1 125 1 Y 1 A LEU 136 ? CD2 ? A LEU 123 CD2 126 1 Y 1 A GLU 137 ? CG ? A GLU 124 CG 127 1 Y 1 A GLU 137 ? CD ? A GLU 124 CD 128 1 Y 1 A GLU 137 ? OE1 ? A GLU 124 OE1 129 1 Y 1 A GLU 137 ? OE2 ? A GLU 124 OE2 130 1 Y 1 A LYS 142 ? CG ? A LYS 129 CG 131 1 Y 1 A LYS 142 ? CD ? A LYS 129 CD 132 1 Y 1 A LYS 142 ? CE ? A LYS 129 CE 133 1 Y 1 A LYS 142 ? NZ ? A LYS 129 NZ 134 1 Y 1 A ASN 147 ? CG ? A ASN 134 CG 135 1 Y 1 A ASN 147 ? OD1 ? A ASN 134 OD1 136 1 Y 1 A ASN 147 ? ND2 ? A ASN 134 ND2 137 1 Y 1 A PHE 148 ? CG ? A PHE 135 CG 138 1 Y 1 A PHE 148 ? CD1 ? A PHE 135 CD1 139 1 Y 1 A PHE 148 ? CD2 ? A PHE 135 CD2 140 1 Y 1 A PHE 148 ? CE1 ? A PHE 135 CE1 141 1 Y 1 A PHE 148 ? CE2 ? A PHE 135 CE2 142 1 Y 1 A PHE 148 ? CZ ? A PHE 135 CZ 143 1 Y 1 A LYS 149 ? CG ? A LYS 136 CG 144 1 Y 1 A LYS 149 ? CD ? A LYS 136 CD 145 1 Y 1 A LYS 149 ? CE ? A LYS 136 CE 146 1 Y 1 A LYS 149 ? NZ ? A LYS 136 NZ 147 1 Y 1 A LYS 151 ? CG ? A LYS 138 CG 148 1 Y 1 A LYS 151 ? CD ? A LYS 138 CD 149 1 Y 1 A LYS 151 ? CE ? A LYS 138 CE 150 1 Y 1 A LYS 151 ? NZ ? A LYS 138 NZ 151 1 Y 1 A MET 155 ? CG ? A MET 142 CG 152 1 Y 1 A MET 155 ? SD ? A MET 142 SD 153 1 Y 1 A MET 155 ? CE ? A MET 142 CE 154 1 Y 1 A ARG 161 ? CG ? A ARG 148 CG 155 1 Y 1 A ARG 161 ? CD ? A ARG 148 CD 156 1 Y 1 A ARG 161 ? NE ? A ARG 148 NE 157 1 Y 1 A ARG 161 ? CZ ? A ARG 148 CZ 158 1 Y 1 A ARG 161 ? NH1 ? A ARG 148 NH1 159 1 Y 1 A ARG 161 ? NH2 ? A ARG 148 NH2 160 1 Y 1 A ARG 167 ? CG ? A ARG 154 CG 161 1 Y 1 A ARG 167 ? CD ? A ARG 154 CD 162 1 Y 1 A ARG 167 ? NE ? A ARG 154 NE 163 1 Y 1 A ARG 167 ? CZ ? A ARG 154 CZ 164 1 Y 1 A ARG 167 ? NH1 ? A ARG 154 NH1 165 1 Y 1 A ARG 167 ? NH2 ? A ARG 154 NH2 166 1 Y 1 A GLU 178 ? CG ? A GLU 165 CG 167 1 Y 1 A GLU 178 ? CD ? A GLU 165 CD 168 1 Y 1 A GLU 178 ? OE1 ? A GLU 165 OE1 169 1 Y 1 A GLU 178 ? OE2 ? A GLU 165 OE2 170 1 Y 1 A LYS 186 ? CG ? A LYS 173 CG 171 1 Y 1 A LYS 186 ? CD ? A LYS 173 CD 172 1 Y 1 A LYS 186 ? CE ? A LYS 173 CE 173 1 Y 1 A LYS 186 ? NZ ? A LYS 173 NZ 174 1 Y 1 A ARG 191 ? CG ? A ARG 178 CG 175 1 Y 1 A ARG 191 ? CD ? A ARG 178 CD 176 1 Y 1 A ARG 191 ? NE ? A ARG 178 NE 177 1 Y 1 A ARG 191 ? CZ ? A ARG 178 CZ 178 1 Y 1 A ARG 191 ? NH1 ? A ARG 178 NH1 179 1 Y 1 A ARG 191 ? NH2 ? A ARG 178 NH2 180 1 Y 1 A GLN 202 ? CG ? A GLN 189 CG 181 1 Y 1 A GLN 202 ? CD ? A GLN 189 CD 182 1 Y 1 A GLN 202 ? OE1 ? A GLN 189 OE1 183 1 Y 1 A GLN 202 ? NE2 ? A GLN 189 NE2 184 1 Y 1 A LYS 205 ? CG ? A LYS 192 CG 185 1 Y 1 A LYS 205 ? CD ? A LYS 192 CD 186 1 Y 1 A LYS 205 ? CE ? A LYS 192 CE 187 1 Y 1 A LYS 205 ? NZ ? A LYS 192 NZ 188 1 Y 1 A LYS 212 ? CG ? A LYS 199 CG 189 1 Y 1 A LYS 212 ? CD ? A LYS 199 CD 190 1 Y 1 A LYS 212 ? CE ? A LYS 199 CE 191 1 Y 1 A LYS 212 ? NZ ? A LYS 199 NZ 192 1 Y 1 A ILE 225 ? CG1 ? A ILE 212 CG1 193 1 Y 1 A ILE 225 ? CG2 ? A ILE 212 CG2 194 1 Y 1 A ILE 225 ? CD1 ? A ILE 212 CD1 195 1 Y 1 A ASP 228 ? CG ? A ASP 215 CG 196 1 Y 1 A ASP 228 ? OD1 ? A ASP 215 OD1 197 1 Y 1 A ASP 228 ? OD2 ? A ASP 215 OD2 198 1 Y 1 A GLU 229 ? CG ? A GLU 216 CG 199 1 Y 1 A GLU 229 ? CD ? A GLU 216 CD 200 1 Y 1 A GLU 229 ? OE1 ? A GLU 216 OE1 201 1 Y 1 A GLU 229 ? OE2 ? A GLU 216 OE2 202 1 Y 1 A LEU 258 ? CG ? A LEU 245 CG 203 1 Y 1 A LEU 258 ? CD1 ? A LEU 245 CD1 204 1 Y 1 A LEU 258 ? CD2 ? A LEU 245 CD2 205 1 Y 1 A LYS 292 ? CG ? A LYS 279 CG 206 1 Y 1 A LYS 292 ? CD ? A LYS 279 CD 207 1 Y 1 A LYS 292 ? CE ? A LYS 279 CE 208 1 Y 1 A LYS 292 ? NZ ? A LYS 279 NZ 209 1 Y 1 A THR 294 ? OG1 ? A THR 281 OG1 210 1 Y 1 A THR 294 ? CG2 ? A THR 281 CG2 211 1 Y 1 A ASP 297 ? CG ? A ASP 284 CG 212 1 Y 1 A ASP 297 ? OD1 ? A ASP 284 OD1 213 1 Y 1 A ASP 297 ? OD2 ? A ASP 284 OD2 214 1 Y 1 A ASP 302 ? CG ? A ASP 289 CG 215 1 Y 1 A ASP 302 ? OD1 ? A ASP 289 OD1 216 1 Y 1 A ASP 302 ? OD2 ? A ASP 289 OD2 217 1 Y 1 A THR 303 ? OG1 ? A THR 290 OG1 218 1 Y 1 A THR 303 ? CG2 ? A THR 290 CG2 219 1 Y 1 A ARG 316 ? CG ? A ARG 303 CG 220 1 Y 1 A ARG 316 ? CD ? A ARG 303 CD 221 1 Y 1 A ARG 316 ? NE ? A ARG 303 NE 222 1 Y 1 A ARG 316 ? CZ ? A ARG 303 CZ 223 1 Y 1 A ARG 316 ? NH1 ? A ARG 303 NH1 224 1 Y 1 A ARG 316 ? NH2 ? A ARG 303 NH2 225 1 Y 1 A LEU 318 ? CG ? A LEU 305 CG 226 1 Y 1 A LEU 318 ? CD1 ? A LEU 305 CD1 227 1 Y 1 A LEU 318 ? CD2 ? A LEU 305 CD2 228 1 Y 1 A LYS 342 ? CG ? A LYS 329 CG 229 1 Y 1 A LYS 342 ? CD ? A LYS 329 CD 230 1 Y 1 A LYS 342 ? CE ? A LYS 329 CE 231 1 Y 1 A LYS 342 ? NZ ? A LYS 329 NZ 232 1 Y 1 A GLU 343 ? CG ? A GLU 330 CG 233 1 Y 1 A GLU 343 ? CD ? A GLU 330 CD 234 1 Y 1 A GLU 343 ? OE1 ? A GLU 330 OE1 235 1 Y 1 A GLU 343 ? OE2 ? A GLU 330 OE2 236 1 Y 1 A GLU 354 ? CG ? A GLU 341 CG 237 1 Y 1 A GLU 354 ? CD ? A GLU 341 CD 238 1 Y 1 A GLU 354 ? OE1 ? A GLU 341 OE1 239 1 Y 1 A GLU 354 ? OE2 ? A GLU 341 OE2 240 1 Y 1 A LYS 355 ? CG ? A LYS 342 CG 241 1 Y 1 A LYS 355 ? CD ? A LYS 342 CD 242 1 Y 1 A LYS 355 ? CE ? A LYS 342 CE 243 1 Y 1 A LYS 355 ? NZ ? A LYS 342 NZ 244 1 Y 1 A ASP 356 ? CG ? A ASP 343 CG 245 1 Y 1 A ASP 356 ? OD1 ? A ASP 343 OD1 246 1 Y 1 A ASP 356 ? OD2 ? A ASP 343 OD2 247 1 Y 1 A ASN 357 ? CG ? A ASN 344 CG 248 1 Y 1 A ASN 357 ? OD1 ? A ASN 344 OD1 249 1 Y 1 A ASN 357 ? ND2 ? A ASN 344 ND2 250 1 Y 1 A GLU 358 ? CG ? A GLU 345 CG 251 1 Y 1 A GLU 358 ? CD ? A GLU 345 CD 252 1 Y 1 A GLU 358 ? OE1 ? A GLU 345 OE1 253 1 Y 1 A GLU 358 ? OE2 ? A GLU 345 OE2 254 1 Y 1 A GLU 363 ? CG ? A GLU 350 CG 255 1 Y 1 A GLU 363 ? CD ? A GLU 350 CD 256 1 Y 1 A GLU 363 ? OE1 ? A GLU 350 OE1 257 1 Y 1 A GLU 363 ? OE2 ? A GLU 350 OE2 258 1 Y 1 A MET 364 ? CG ? A MET 351 CG 259 1 Y 1 A MET 364 ? SD ? A MET 351 SD 260 1 Y 1 A MET 364 ? CE ? A MET 351 CE 261 1 Y 1 A GLU 374 ? CG ? A GLU 361 CG 262 1 Y 1 A GLU 374 ? CD ? A GLU 361 CD 263 1 Y 1 A GLU 374 ? OE1 ? A GLU 361 OE1 264 1 Y 1 A GLU 374 ? OE2 ? A GLU 361 OE2 265 1 Y 1 A LYS 379 ? CG ? A LYS 366 CG 266 1 Y 1 A LYS 379 ? CD ? A LYS 366 CD 267 1 Y 1 A LYS 379 ? CE ? A LYS 366 CE 268 1 Y 1 A LYS 379 ? NZ ? A LYS 366 NZ 269 1 Y 1 A LYS 387 ? CG ? A LYS 374 CG 270 1 Y 1 A LYS 387 ? CD ? A LYS 374 CD 271 1 Y 1 A LYS 387 ? CE ? A LYS 374 CE 272 1 Y 1 A LYS 387 ? NZ ? A LYS 374 NZ 273 1 Y 1 A LYS 395 ? CG ? A LYS 382 CG 274 1 Y 1 A LYS 395 ? CD ? A LYS 382 CD 275 1 Y 1 A LYS 395 ? CE ? A LYS 382 CE 276 1 Y 1 A LYS 395 ? NZ ? A LYS 382 NZ 277 1 Y 1 A GLN 421 ? CG ? A GLN 408 CG 278 1 Y 1 A GLN 421 ? CD ? A GLN 408 CD 279 1 Y 1 A GLN 421 ? OE1 ? A GLN 408 OE1 280 1 Y 1 A GLN 421 ? NE2 ? A GLN 408 NE2 281 1 Y 1 A LYS 422 ? CG ? A LYS 409 CG 282 1 Y 1 A LYS 422 ? CD ? A LYS 409 CD 283 1 Y 1 A LYS 422 ? CE ? A LYS 409 CE 284 1 Y 1 A LYS 422 ? NZ ? A LYS 409 NZ 285 1 Y 1 A LYS 423 ? CG ? A LYS 410 CG 286 1 Y 1 A LYS 423 ? CD ? A LYS 410 CD 287 1 Y 1 A LYS 423 ? CE ? A LYS 410 CE 288 1 Y 1 A LYS 423 ? NZ ? A LYS 410 NZ 289 1 Y 1 A VAL 427 ? CG1 ? A VAL 414 CG1 290 1 Y 1 A VAL 427 ? CG2 ? A VAL 414 CG2 291 1 Y 1 A LEU 430 ? CG ? A LEU 417 CG 292 1 Y 1 A LEU 430 ? CD1 ? A LEU 417 CD1 293 1 Y 1 A LEU 430 ? CD2 ? A LEU 417 CD2 294 1 Y 1 A LEU 431 ? CG ? A LEU 418 CG 295 1 Y 1 A LEU 431 ? CD1 ? A LEU 418 CD1 296 1 Y 1 A LEU 431 ? CD2 ? A LEU 418 CD2 297 1 Y 1 A ASP 433 ? CG ? A ASP 420 CG 298 1 Y 1 A ASP 433 ? OD1 ? A ASP 420 OD1 299 1 Y 1 A ASP 433 ? OD2 ? A ASP 420 OD2 300 1 Y 1 A ILE 434 ? CG1 ? A ILE 421 CG1 301 1 Y 1 A ILE 434 ? CG2 ? A ILE 421 CG2 302 1 Y 1 A ILE 434 ? CD1 ? A ILE 421 CD1 303 1 Y 1 A GLN 437 ? CG ? A GLN 424 CG 304 1 Y 1 A GLN 437 ? CD ? A GLN 424 CD 305 1 Y 1 A GLN 437 ? OE1 ? A GLN 424 OE1 306 1 Y 1 A GLN 437 ? NE2 ? A GLN 424 NE2 307 1 Y 1 A MET 438 ? CG ? A MET 425 CG 308 1 Y 1 A MET 438 ? SD ? A MET 425 SD 309 1 Y 1 A MET 438 ? CE ? A MET 425 CE 310 1 Y 1 A LEU 440 ? CG ? A LEU 427 CG 311 1 Y 1 A LEU 440 ? CD1 ? A LEU 427 CD1 312 1 Y 1 A LEU 440 ? CD2 ? A LEU 427 CD2 313 1 Y 1 A ILE 442 ? CG1 ? A ILE 429 CG1 314 1 Y 1 A ILE 442 ? CG2 ? A ILE 429 CG2 315 1 Y 1 A ILE 442 ? CD1 ? A ILE 429 CD1 316 1 Y 1 A LEU 447 ? CG ? A LEU 434 CG 317 1 Y 1 A LEU 447 ? CD1 ? A LEU 434 CD1 318 1 Y 1 A LEU 447 ? CD2 ? A LEU 434 CD2 319 1 Y 1 A THR 448 ? OG1 ? A THR 435 OG1 320 1 Y 1 A THR 448 ? CG2 ? A THR 435 CG2 321 1 Y 1 D ASP 2 ? CG ? B ASP 2 CG 322 1 Y 1 D ASP 2 ? OD1 ? B ASP 2 OD1 323 1 Y 1 D ASP 2 ? OD2 ? B ASP 2 OD2 324 1 Y 1 D ILE 4 ? CG1 ? B ILE 4 CG1 325 1 Y 1 D ILE 4 ? CG2 ? B ILE 4 CG2 326 1 Y 1 D ILE 4 ? CD1 ? B ILE 4 CD1 327 1 Y 1 D LYS 6 ? CG ? B LYS 6 CG 328 1 Y 1 D LYS 6 ? CD ? B LYS 6 CD 329 1 Y 1 D LYS 6 ? CE ? B LYS 6 CE 330 1 Y 1 D LYS 6 ? NZ ? B LYS 6 NZ 331 1 Y 1 D LYS 8 ? CG ? B LYS 8 CG 332 1 Y 1 D LYS 8 ? CD ? B LYS 8 CD 333 1 Y 1 D LYS 8 ? CE ? B LYS 8 CE 334 1 Y 1 D LYS 8 ? NZ ? B LYS 8 NZ 335 1 Y 1 D VAL 11 ? CG1 ? B VAL 11 CG1 336 1 Y 1 D VAL 11 ? CG2 ? B VAL 11 CG2 337 1 Y 1 D ARG 13 ? CG ? B ARG 13 CG 338 1 Y 1 D ARG 13 ? CD ? B ARG 13 CD 339 1 Y 1 D ARG 13 ? NE ? B ARG 13 NE 340 1 Y 1 D ARG 13 ? CZ ? B ARG 13 CZ 341 1 Y 1 D ARG 13 ? NH1 ? B ARG 13 NH1 342 1 Y 1 D ARG 13 ? NH2 ? B ARG 13 NH2 343 1 Y 1 D ASP 16 ? CG ? B ASP 16 CG 344 1 Y 1 D ASP 16 ? OD1 ? B ASP 16 OD1 345 1 Y 1 D ASP 16 ? OD2 ? B ASP 16 OD2 346 1 Y 1 D LYS 36 ? CG ? B LYS 36 CG 347 1 Y 1 D LYS 36 ? CD ? B LYS 36 CD 348 1 Y 1 D LYS 36 ? CE ? B LYS 36 CE 349 1 Y 1 D LYS 36 ? NZ ? B LYS 36 NZ # 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 GLY 14 ? A GLY 1 2 1 Y 1 A GLN 15 ? A GLN 2 3 1 Y 1 A PRO 16 ? A PRO 3 4 1 Y 1 A VAL 17 ? A VAL 4 5 1 Y 1 A SER 18 ? A SER 5 6 1 Y 1 A ILE 19 ? A ILE 6 7 1 Y 1 A GLN 20 ? A GLN 7 8 1 Y 1 A ALA 21 ? A ALA 8 9 1 Y 1 A PHE 22 ? A PHE 9 10 1 Y 1 A ALA 23 ? A ALA 10 11 1 Y 1 A SER 24 ? A SER 11 12 1 Y 1 A SER 25 ? A SER 12 13 1 Y 1 A SER 26 ? A SER 13 14 1 Y 1 A THR 27 ? A THR 14 15 1 Y 1 A LEU 28 ? A LEU 15 16 1 Y 1 A HIS 29 ? A HIS 16 17 1 Y 1 A GLY 30 ? A GLY 17 18 1 Y 1 A ILE 31 ? A ILE 18 19 1 Y 1 A SER 32 ? A SER 19 20 1 Y 1 A HIS 33 ? A HIS 20 21 1 Y 1 A ILE 34 ? A ILE 21 22 1 Y 1 A PHE 35 ? A PHE 22 23 1 Y 1 A SER 36 ? A SER 23 24 1 Y 1 A TYR 37 ? A TYR 24 25 1 Y 1 A GLU 38 ? A GLU 25 26 1 Y 1 A ARG 39 ? A ARG 26 27 1 Y 1 A LEU 40 ? A LEU 27 28 1 Y 1 A SER 298 ? A SER 285 29 1 Y 1 A GLU 299 ? A GLU 286 30 1 Y 1 A PHE 300 ? A PHE 287 31 1 Y 1 A TYR 301 ? A TYR 288 32 1 Y 1 A GLU 451 ? A GLU 438 33 1 Y 1 A LEU 452 ? A LEU 439 34 1 Y 1 A PHE 453 ? A PHE 440 35 1 Y 1 A ASP 454 ? A ASP 441 36 1 Y 1 A TYR 455 ? A TYR 442 37 1 Y 1 A ALA 456 ? A ALA 443 38 1 Y 1 A TYR 457 ? A TYR 444 39 1 Y 1 A GLU 458 ? A GLU 445 40 1 Y 1 A VAL 459 ? A VAL 446 41 1 Y 1 A ILE 460 ? A ILE 447 42 1 Y 1 A LYS 461 ? A LYS 448 43 1 Y 1 A HIS 462 ? A HIS 449 44 1 Y 1 A ARG 463 ? A ARG 450 45 1 Y 1 D GLU 1 ? B GLU 1 46 1 Y 1 D HIS 14 ? B HIS 14 47 1 Y 1 D GLY 15 ? B GLY 15 48 1 Y 1 D LYS 39 ? B LYS 39 49 1 Y 1 D THR 40 ? B THR 40 # _pdbx_entity_nonpoly.entity_id 3 _pdbx_entity_nonpoly.name N-ACETYL-D-GLUCOSAMINE _pdbx_entity_nonpoly.comp_id NAG # 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 C 3 NAG 1 501 501 NAG NAG A . D 3 NAG 1 502 502 NAG NAG A . #