data_1YSC # _entry.id 1YSC # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.287 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 1YSC WWPDB D_1000177429 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1YSC _pdbx_database_status.recvd_initial_deposition_date 1994-03-08 _pdbx_database_status.deposit_site ? _pdbx_database_status.process_site BNL _pdbx_database_status.SG_entry . _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Endrizzi, J.A.' 1 'Remington, S.J.' 2 # _citation.id primary _citation.title '2.8-A structure of yeast serine carboxypeptidase' _citation.journal_abbrev Biochemistry _citation.journal_volume 33 _citation.page_first 11106 _citation.page_last 11120 _citation.year 1994 _citation.journal_id_ASTM BICHAW _citation.country US _citation.journal_id_ISSN 0006-2960 _citation.journal_id_CSD 0033 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 7727362 _citation.pdbx_database_id_DOI 10.1021/bi00203a007 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Endrizzi, J.A.' 1 primary 'Breddam, K.' 2 primary 'Remington, S.J.' 3 # _cell.entry_id 1YSC _cell.length_a 111.800 _cell.length_b 111.800 _cell.length_c 111.800 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 12 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1YSC _symmetry.space_group_name_H-M 'P 21 3' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 198 # 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 'SERINE CARBOXYPEPTIDASE' 47355.363 1 3.4.16.5 ? ? ? 2 non-polymer man '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' 221.208 3 ? ? ? ? 3 water nat water 18.015 38 ? ? ? ? # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;KIKDPKILGIDPNVTQYTGYLDVEDEDKHFFFWTFESRNDPAKDPVILWLNGGPGCSSLTGLFFELGPSSIGPDLKPIGN PYSWNSNATVIFLDQPVNVGFSYSGSSGVSNTVAAGKDVYNFLELFFDQFPEYVNKGQDFHIAGESYAGHYIPVFASEIL SHKDRNFNLTSVLIGNGLTDPLTQYNYYEPMACGEGGEPSVLPSEECSAMEDSLERCLGLIESCYDSQSVWSCVPATIYC NNAQLAPYQRTGRNVYDIRKDCEGGNLCYPTLQDIDDYLNQDYVKEAVGAEVDHYESCNFDINRNFLFAGDWMKPYHTAV TDLLNQDLPILVYAGDKDFICNWLGNKAWTDVLPWKYDEEFASQKVRNWTASITDEVAGEVKSYKHFTYLRVFNGGHMVP FDVPENALSMVNEWIHGGFSL ; _entity_poly.pdbx_seq_one_letter_code_can ;KIKDPKILGIDPNVTQYTGYLDVEDEDKHFFFWTFESRNDPAKDPVILWLNGGPGCSSLTGLFFELGPSSIGPDLKPIGN PYSWNSNATVIFLDQPVNVGFSYSGSSGVSNTVAAGKDVYNFLELFFDQFPEYVNKGQDFHIAGESYAGHYIPVFASEIL SHKDRNFNLTSVLIGNGLTDPLTQYNYYEPMACGEGGEPSVLPSEECSAMEDSLERCLGLIESCYDSQSVWSCVPATIYC NNAQLAPYQRTGRNVYDIRKDCEGGNLCYPTLQDIDDYLNQDYVKEAVGAEVDHYESCNFDINRNFLFAGDWMKPYHTAV TDLLNQDLPILVYAGDKDFICNWLGNKAWTDVLPWKYDEEFASQKVRNWTASITDEVAGEVKSYKHFTYLRVFNGGHMVP FDVPENALSMVNEWIHGGFSL ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 LYS n 1 2 ILE n 1 3 LYS n 1 4 ASP n 1 5 PRO n 1 6 LYS n 1 7 ILE n 1 8 LEU n 1 9 GLY n 1 10 ILE n 1 11 ASP n 1 12 PRO n 1 13 ASN n 1 14 VAL n 1 15 THR n 1 16 GLN n 1 17 TYR n 1 18 THR n 1 19 GLY n 1 20 TYR n 1 21 LEU n 1 22 ASP n 1 23 VAL n 1 24 GLU n 1 25 ASP n 1 26 GLU n 1 27 ASP n 1 28 LYS n 1 29 HIS n 1 30 PHE n 1 31 PHE n 1 32 PHE n 1 33 TRP n 1 34 THR n 1 35 PHE n 1 36 GLU n 1 37 SER n 1 38 ARG n 1 39 ASN n 1 40 ASP n 1 41 PRO n 1 42 ALA n 1 43 LYS n 1 44 ASP n 1 45 PRO n 1 46 VAL n 1 47 ILE n 1 48 LEU n 1 49 TRP n 1 50 LEU n 1 51 ASN n 1 52 GLY n 1 53 GLY n 1 54 PRO n 1 55 GLY n 1 56 CYS n 1 57 SER n 1 58 SER n 1 59 LEU n 1 60 THR n 1 61 GLY n 1 62 LEU n 1 63 PHE n 1 64 PHE n 1 65 GLU n 1 66 LEU n 1 67 GLY n 1 68 PRO n 1 69 SER n 1 70 SER n 1 71 ILE n 1 72 GLY n 1 73 PRO n 1 74 ASP n 1 75 LEU n 1 76 LYS n 1 77 PRO n 1 78 ILE n 1 79 GLY n 1 80 ASN n 1 81 PRO n 1 82 TYR n 1 83 SER n 1 84 TRP n 1 85 ASN n 1 86 SER n 1 87 ASN n 1 88 ALA n 1 89 THR n 1 90 VAL n 1 91 ILE n 1 92 PHE n 1 93 LEU n 1 94 ASP n 1 95 GLN n 1 96 PRO n 1 97 VAL n 1 98 ASN n 1 99 VAL n 1 100 GLY n 1 101 PHE n 1 102 SER n 1 103 TYR n 1 104 SER n 1 105 GLY n 1 106 SER n 1 107 SER n 1 108 GLY n 1 109 VAL n 1 110 SER n 1 111 ASN n 1 112 THR n 1 113 VAL n 1 114 ALA n 1 115 ALA n 1 116 GLY n 1 117 LYS n 1 118 ASP n 1 119 VAL n 1 120 TYR n 1 121 ASN n 1 122 PHE n 1 123 LEU n 1 124 GLU n 1 125 LEU n 1 126 PHE n 1 127 PHE n 1 128 ASP n 1 129 GLN n 1 130 PHE n 1 131 PRO n 1 132 GLU n 1 133 TYR n 1 134 VAL n 1 135 ASN n 1 136 LYS n 1 137 GLY n 1 138 GLN n 1 139 ASP n 1 140 PHE n 1 141 HIS n 1 142 ILE n 1 143 ALA n 1 144 GLY n 1 145 GLU n 1 146 SER n 1 147 TYR n 1 148 ALA n 1 149 GLY n 1 150 HIS n 1 151 TYR n 1 152 ILE n 1 153 PRO n 1 154 VAL n 1 155 PHE n 1 156 ALA n 1 157 SER n 1 158 GLU n 1 159 ILE n 1 160 LEU n 1 161 SER n 1 162 HIS n 1 163 LYS n 1 164 ASP n 1 165 ARG n 1 166 ASN n 1 167 PHE n 1 168 ASN n 1 169 LEU n 1 170 THR n 1 171 SER n 1 172 VAL n 1 173 LEU n 1 174 ILE n 1 175 GLY n 1 176 ASN n 1 177 GLY n 1 178 LEU n 1 179 THR n 1 180 ASP n 1 181 PRO n 1 182 LEU n 1 183 THR n 1 184 GLN n 1 185 TYR n 1 186 ASN n 1 187 TYR n 1 188 TYR n 1 189 GLU n 1 190 PRO n 1 191 MET n 1 192 ALA n 1 193 CYS n 1 194 GLY n 1 195 GLU n 1 196 GLY n 1 197 GLY n 1 198 GLU n 1 199 PRO n 1 200 SER n 1 201 VAL n 1 202 LEU n 1 203 PRO n 1 204 SER n 1 205 GLU n 1 206 GLU n 1 207 CYS n 1 208 SER n 1 209 ALA n 1 210 MET n 1 211 GLU n 1 212 ASP n 1 213 SER n 1 214 LEU n 1 215 GLU n 1 216 ARG n 1 217 CYS n 1 218 LEU n 1 219 GLY n 1 220 LEU n 1 221 ILE n 1 222 GLU n 1 223 SER n 1 224 CYS n 1 225 TYR n 1 226 ASP n 1 227 SER n 1 228 GLN n 1 229 SER n 1 230 VAL n 1 231 TRP n 1 232 SER n 1 233 CYS n 1 234 VAL n 1 235 PRO n 1 236 ALA n 1 237 THR n 1 238 ILE n 1 239 TYR n 1 240 CYS n 1 241 ASN n 1 242 ASN n 1 243 ALA n 1 244 GLN n 1 245 LEU n 1 246 ALA n 1 247 PRO n 1 248 TYR n 1 249 GLN n 1 250 ARG n 1 251 THR n 1 252 GLY n 1 253 ARG n 1 254 ASN n 1 255 VAL n 1 256 TYR n 1 257 ASP n 1 258 ILE n 1 259 ARG n 1 260 LYS n 1 261 ASP n 1 262 CYS n 1 263 GLU n 1 264 GLY n 1 265 GLY n 1 266 ASN n 1 267 LEU n 1 268 CYS n 1 269 TYR n 1 270 PRO n 1 271 THR n 1 272 LEU n 1 273 GLN n 1 274 ASP n 1 275 ILE n 1 276 ASP n 1 277 ASP n 1 278 TYR n 1 279 LEU n 1 280 ASN n 1 281 GLN n 1 282 ASP n 1 283 TYR n 1 284 VAL n 1 285 LYS n 1 286 GLU n 1 287 ALA n 1 288 VAL n 1 289 GLY n 1 290 ALA n 1 291 GLU n 1 292 VAL n 1 293 ASP n 1 294 HIS n 1 295 TYR n 1 296 GLU n 1 297 SER n 1 298 CYS n 1 299 ASN n 1 300 PHE n 1 301 ASP n 1 302 ILE n 1 303 ASN n 1 304 ARG n 1 305 ASN n 1 306 PHE n 1 307 LEU n 1 308 PHE n 1 309 ALA n 1 310 GLY n 1 311 ASP n 1 312 TRP n 1 313 MET n 1 314 LYS n 1 315 PRO n 1 316 TYR n 1 317 HIS n 1 318 THR n 1 319 ALA n 1 320 VAL n 1 321 THR n 1 322 ASP n 1 323 LEU n 1 324 LEU n 1 325 ASN n 1 326 GLN n 1 327 ASP n 1 328 LEU n 1 329 PRO n 1 330 ILE n 1 331 LEU n 1 332 VAL n 1 333 TYR n 1 334 ALA n 1 335 GLY n 1 336 ASP n 1 337 LYS n 1 338 ASP n 1 339 PHE n 1 340 ILE n 1 341 CYS n 1 342 ASN n 1 343 TRP n 1 344 LEU n 1 345 GLY n 1 346 ASN n 1 347 LYS n 1 348 ALA n 1 349 TRP n 1 350 THR n 1 351 ASP n 1 352 VAL n 1 353 LEU n 1 354 PRO n 1 355 TRP n 1 356 LYS n 1 357 TYR n 1 358 ASP n 1 359 GLU n 1 360 GLU n 1 361 PHE n 1 362 ALA n 1 363 SER n 1 364 GLN n 1 365 LYS n 1 366 VAL n 1 367 ARG n 1 368 ASN n 1 369 TRP n 1 370 THR n 1 371 ALA n 1 372 SER n 1 373 ILE n 1 374 THR n 1 375 ASP n 1 376 GLU n 1 377 VAL n 1 378 ALA n 1 379 GLY n 1 380 GLU n 1 381 VAL n 1 382 LYS n 1 383 SER n 1 384 TYR n 1 385 LYS n 1 386 HIS n 1 387 PHE n 1 388 THR n 1 389 TYR n 1 390 LEU n 1 391 ARG n 1 392 VAL n 1 393 PHE n 1 394 ASN n 1 395 GLY n 1 396 GLY n 1 397 HIS n 1 398 MET n 1 399 VAL n 1 400 PRO n 1 401 PHE n 1 402 ASP n 1 403 VAL n 1 404 PRO n 1 405 GLU n 1 406 ASN n 1 407 ALA n 1 408 LEU n 1 409 SER n 1 410 MET n 1 411 VAL n 1 412 ASN n 1 413 GLU n 1 414 TRP n 1 415 ILE n 1 416 HIS n 1 417 GLY n 1 418 GLY n 1 419 PHE n 1 420 SER n 1 421 LEU 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 ;baker's yeast ; _entity_src_gen.gene_src_genus Saccharomyces _entity_src_gen.pdbx_gene_src_gene ? _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Saccharomyces cerevisiae' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 4932 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name ? _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id ? _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _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 ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code CBPY_YEAST _struct_ref.entity_id 1 _struct_ref.pdbx_db_accession P00729 _struct_ref.pdbx_align_begin 1 _struct_ref.pdbx_seq_one_letter_code ;MKAFTSLLCGLGLSTTLAKAISLQRPLGLDKDVLLQAAEKFGLDLDLDHLLKELDSNVLDAWAQIEHLYPNQVMSLETST KPKFPEAIKTKKDWDFVVKNDAIENYQLRVNKIKDPKILGIDPNVTQYTGYLDVEDEDKHFFFWTFESRNDPAKDPVILW LNGGPGCSSLTGLFFELGPSSIGPDLKPIGNPYSWNSNATVIFLDQPVNVGFSYSGSSGVSNTVAAGKDVYNFLELFFDQ FPEYVNKGQDFHIAGESYAGHYIPVFASEILSHKDRNFNLTSVLIGNGLTDPLTQYNYYEPMACGEGGEPSVLPSEECSA MEDSLERCLGLIESCYDSQSVWSCVPATIYCNNAQLAPYQRTGRNVYDIRKDCEGGNLCYPTLQDIDDYLNQDYVKEAVG AEVDHYESCNFDINRNFLFAGDWMKPYHTAVTDLLNQDLPILVYAGDKDFICNWLGNKAWTDVLPWKYDEEFASQKVRNW TASITDEVAGEVKSYKHFTYLRVFNGGHMVPFDVPENALSMVNEWIHGGFSL ; _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 1YSC _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 421 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P00729 _struct_ref_seq.db_align_beg 112 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 532 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 421 # 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 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NDG D-saccharide . '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' ? '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 1YSC _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number ? # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.46 _exptl_crystal.density_percent_sol 49.96 _exptl_crystal.description ? # _refine.entry_id 1YSC _refine.ls_number_reflns_obs ? _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low ? _refine.ls_d_res_high 2.8 _refine.ls_percent_reflns_obs ? _refine.ls_R_factor_obs 0.162 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work ? _refine.ls_R_factor_R_free ? _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free ? _refine.ls_number_reflns_R_free ? _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details ? _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct ? _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ? _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 ? _refine.overall_SU_B ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_overall_phase_error ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3253 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 42 _refine_hist.number_atoms_solvent 38 _refine_hist.number_atoms_total 3333 _refine_hist.d_res_high 2.8 _refine_hist.d_res_low . # 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 t_bond_d 0.16 ? ? ? 'X-RAY DIFFRACTION' ? t_angle_deg 2.75 ? ? ? 'X-RAY DIFFRACTION' ? t_dihedral_angle_d ? ? ? ? 'X-RAY DIFFRACTION' ? t_incorr_chiral_ct ? ? ? ? 'X-RAY DIFFRACTION' ? t_pseud_angle ? ? ? ? 'X-RAY DIFFRACTION' ? t_trig_c_planes ? ? ? ? 'X-RAY DIFFRACTION' ? t_gen_planes ? ? ? ? 'X-RAY DIFFRACTION' ? t_it ? ? ? ? 'X-RAY DIFFRACTION' ? t_nbd ? ? ? ? 'X-RAY DIFFRACTION' ? # _struct.entry_id 1YSC _struct.title '2.8 ANGSTROMS STRUCTURE OF YEAST SERINE CARBOXYPEPTIDASE' _struct.pdbx_descriptor 'SERINE CARBOXYPEPTIDASE (CPY, CPD-Y, OR PROTEINASE C) (E.C.3.4.16.5)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1YSC _struct_keywords.pdbx_keywords 'HYDROLASE(CARBOXYPEPTIDASE)' _struct_keywords.text 'HYDROLASE(CARBOXYPEPTIDASE)' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 2 ? E N N 3 ? # _struct_biol.id 1 # 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 A LEU A 59 ? LEU A 62 ? LEU A 59 LEU A 62 1 ? 4 HELX_P HELX_P2 B TRP A 84 ? ASN A 87 ? TRP A 84 ASN A 87 5 ? 4 HELX_P HELX_P3 C VAL A 113 ? GLN A 129 ? VAL A 113 GLN A 129 1 ? 17 HELX_P HELX_P4 D PRO A 131 ? TYR A 133 ? PRO A 131 TYR A 133 5 ? 3 HELX_P HELX_P5 E ALA A 148 ? LEU A 160 ? ALA A 148 LEU A 160 1 ? 13 HELX_P HELX_P6 F PRO A 181 ? ALA A 192 ? PRO A 181 ALA A 192 1 ? 12 HELX_P HELX_P7 G SER A 204 ? SER A 227 ? SER A 204 SER A 227 1 ? 24 HELX_P HELX_P8 H VAL A 230 ? THR A 251 ? VAL A 230 THR A 251 1 ? 22 HELX_P HELX_P9 I THR A 271 ? ASN A 280 ? THR A 271 ASN A 280 1 ? 10 HELX_P HELX_P10 J ASP A 282 ? ALA A 287 ? ASP A 282 ALA A 287 1 ? 6 HELX_P HELX_P11 K PHE A 300 ? LEU A 307 ? PHE A 300 LEU A 307 1 ? 8 HELX_P HELX_P12 L ASP A 311 ? MET A 313 ? ASP A 311 MET A 313 5 ? 3 HELX_P HELX_P13 M HIS A 317 ? ASN A 325 ? HIS A 317 ASN A 325 1 ? 9 HELX_P HELX_P14 N TRP A 343 ? THR A 350 ? TRP A 343 THR A 350 1 ? 8 HELX_P HELX_P15 O GLU A 359 ? SER A 363 ? GLU A 359 SER A 363 1 ? 5 HELX_P HELX_P16 P VAL A 399 ? ASP A 402 ? VAL A 399 ASP A 402 1 ? 4 HELX_P HELX_P17 Q PRO A 404 ? ILE A 415 ? PRO A 404 ILE A 415 1 ? 12 # _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 56 SG ? ? ? 1_555 A CYS 298 SG ? ? A CYS 56 A CYS 298 1_555 ? ? ? ? ? ? ? 1.979 ? disulf2 disulf ? ? A CYS 193 SG ? ? ? 1_555 A CYS 207 SG ? ? A CYS 193 A CYS 207 1_555 ? ? ? ? ? ? ? 2.072 ? disulf3 disulf ? ? A CYS 217 SG ? ? ? 1_555 A CYS 240 SG ? ? A CYS 217 A CYS 240 1_555 ? ? ? ? ? ? ? 2.002 ? disulf4 disulf ? ? A CYS 224 SG ? ? ? 1_555 A CYS 233 SG ? ? A CYS 224 A CYS 233 1_555 ? ? ? ? ? ? ? 1.913 ? disulf5 disulf ? ? A CYS 262 SG ? ? ? 1_555 A CYS 268 SG ? ? A CYS 262 A CYS 268 1_555 ? ? ? ? ? ? ? 2.128 ? covale1 covale ? ? A ASN 87 ND2 ? ? ? 1_555 B NDG . C1 ? ? A ASN 87 A NDG 871 1_555 ? ? ? ? ? ? ? 1.363 ? covale2 covale ? ? A ASN 168 ND2 ? ? ? 1_555 C NDG . C1 ? ? A ASN 168 A NDG 1681 1_555 ? ? ? ? ? ? ? 1.357 ? covale3 covale ? ? A ASN 368 ND2 ? ? ? 1_555 D NDG . C1 ? ? A ASN 368 A NDG 3681 1_555 ? ? ? ? ? ? ? 1.335 ? # 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 GLY 53 A . ? GLY 53 A PRO 54 A ? PRO 54 A 1 1.36 2 GLN 95 A . ? GLN 95 A PRO 96 A ? PRO 96 A 1 2.61 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details S1A ? 11 ? S1B ? 11 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense S1A 1 2 ? anti-parallel S1A 2 3 ? parallel S1A 3 4 ? anti-parallel S1A 4 5 ? anti-parallel S1A 5 6 ? anti-parallel S1A 6 7 ? anti-parallel S1A 7 8 ? anti-parallel S1A 8 9 ? anti-parallel S1A 9 10 ? parallel S1A 10 11 ? anti-parallel S1B 1 2 ? anti-parallel S1B 2 3 ? parallel S1B 3 4 ? anti-parallel S1B 4 5 ? anti-parallel S1B 5 6 ? anti-parallel S1B 6 7 ? anti-parallel S1B 7 8 ? anti-parallel S1B 8 9 ? anti-parallel S1B 9 10 ? parallel S1B 10 11 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id S1A 1 LYS A 1 ? LYS A 3 ? LYS A 1 LYS A 3 S1A 2 TYR A 17 ? VAL A 23 ? TYR A 17 VAL A 23 S1A 3 LYS A 28 ? PHE A 35 ? LYS A 28 PHE A 35 S1A 4 THR A 89 ? ILE A 91 ? THR A 89 ILE A 91 S1A 5 VAL A 46 ? LEU A 50 ? VAL A 46 LEU A 50 S1A 6 PHE A 140 ? GLU A 145 ? PHE A 140 GLU A 145 S1A 7 LEU A 169 ? GLY A 175 ? LEU A 169 GLY A 175 S1A 8 ILE A 330 ? GLY A 335 ? ILE A 330 GLY A 335 S1A 9 PHE A 387 ? VAL A 392 ? PHE A 387 VAL A 392 S1A 10 VAL A 377 ? TYR A 384 ? VAL A 377 TYR A 384 S1A 11 ARG A 367 ? THR A 370 ? ARG A 367 THR A 370 S1B 1 LYS A 1 ? LYS A 3 ? LYS A 1 LYS A 3 S1B 2 TYR A 17 ? VAL A 23 ? TYR A 17 VAL A 23 S1B 3 LYS A 28 ? PHE A 35 ? LYS A 28 PHE A 35 S1B 4 TYR A 103 ? SER A 104 ? TYR A 103 SER A 104 S1B 5 VAL A 46 ? LEU A 50 ? VAL A 46 LEU A 50 S1B 6 PHE A 140 ? GLU A 145 ? PHE A 140 GLU A 145 S1B 7 LEU A 169 ? GLY A 175 ? LEU A 169 GLY A 175 S1B 8 ILE A 330 ? GLY A 335 ? ILE A 330 GLY A 335 S1B 9 PHE A 387 ? VAL A 392 ? PHE A 387 VAL A 392 S1B 10 VAL A 377 ? TYR A 384 ? VAL A 377 TYR A 384 S1B 11 ARG A 367 ? THR A 370 ? ARG A 367 THR A 370 # 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 CAT Unknown ? ? ? ? 4 ? CBS Unknown ? ? ? ? 4 ? S1P Unknown ? ? ? ? 7 ? S1S Unknown ? ? ? ? 6 ? AC1 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NDG A 871' AC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NDG A 1681' AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NDG A 3681' # 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 CAT 4 SER A 146 ? SER A 146 . ? 1_555 ? 2 CAT 4 ASP A 338 ? ASP A 338 . ? 1_555 ? 3 CAT 4 HIS A 397 ? HIS A 397 . ? 1_555 ? 4 CAT 4 GLU A 145 ? GLU A 145 . ? 1_555 ? 5 CBS 4 ASN A 51 ? ASN A 51 . ? 1_555 ? 6 CBS 4 GLY A 52 ? GLY A 52 . ? 1_555 ? 7 CBS 4 GLU A 145 ? GLU A 145 . ? 1_555 ? 8 CBS 4 HIS A 397 ? HIS A 397 . ? 1_555 ? 9 S1P 7 THR A 60 ? THR A 60 . ? 1_555 ? 10 S1P 7 PHE A 64 ? PHE A 64 . ? 1_555 ? 11 S1P 7 GLU A 65 ? GLU A 65 . ? 1_555 ? 12 S1P 7 TYR A 256 ? TYR A 256 . ? 1_555 ? 13 S1P 7 TYR A 269 ? TYR A 269 . ? 1_555 ? 14 S1P 7 LEU A 272 ? LEU A 272 . ? 1_555 ? 15 S1P 7 MET A 398 ? MET A 398 . ? 1_555 ? 16 S1S 6 TYR A 147 ? TYR A 147 . ? 1_555 ? 17 S1S 6 LEU A 178 ? LEU A 178 . ? 1_555 ? 18 S1S 6 LEU A 245 ? LEU A 245 . ? 1_555 ? 19 S1S 6 TRP A 312 ? TRP A 312 . ? 1_555 ? 20 S1S 6 ILE A 340 ? ILE A 340 . ? 1_555 ? 21 S1S 6 CYS A 341 ? CYS A 341 . ? 1_555 ? 22 AC1 3 ASN A 39 ? ASN A 39 . ? 1_555 ? 23 AC1 3 ASN A 87 ? ASN A 87 . ? 1_555 ? 24 AC1 3 HIS A 416 ? HIS A 416 . ? 1_555 ? 25 AC2 2 ARG A 165 ? ARG A 165 . ? 1_555 ? 26 AC2 2 ASN A 168 ? ASN A 168 . ? 1_555 ? 27 AC3 2 ASN A 368 ? ASN A 368 . ? 1_555 ? 28 AC3 2 HOH E . ? HOH A 450 . ? 1_555 ? # _database_PDB_matrix.entry_id 1YSC _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 1YSC _atom_sites.fract_transf_matrix[1][1] 0.008945 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.008945 _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] 0.008945 _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_sites_footnote.id _atom_sites_footnote.text 1 'CIS PROLINE - PRO 54' 2 'CIS PROLINE - PRO 96' 3 'RESIDUE NAG 871 HAS STRONGER ELECTRON DENSITY BETWEEN IT AND ASN 39 THAN ASN 87. IT IS EXPECTED TO RESIDE ON THE LATTER RESIDUE.' # 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 . LYS A 1 1 ? 62.669 18.917 21.945 1.00 78.94 ? 1 LYS A N 1 ATOM 2 C CA . LYS A 1 1 ? 63.411 18.380 20.812 1.00 83.83 ? 1 LYS A CA 1 ATOM 3 C C . LYS A 1 1 ? 62.852 17.024 20.428 1.00 75.12 ? 1 LYS A C 1 ATOM 4 O O . LYS A 1 1 ? 62.943 16.058 21.184 1.00 74.25 ? 1 LYS A O 1 ATOM 5 C CB . LYS A 1 1 ? 64.906 18.309 21.090 1.00 88.17 ? 1 LYS A CB 1 ATOM 6 N N . ILE A 1 2 ? 62.279 16.957 19.252 1.00 65.37 ? 2 ILE A N 1 ATOM 7 C CA . ILE A 1 2 ? 61.697 15.705 18.855 1.00 64.98 ? 2 ILE A CA 1 ATOM 8 C C . ILE A 1 2 ? 62.077 15.132 17.504 1.00 59.34 ? 2 ILE A C 1 ATOM 9 O O . ILE A 1 2 ? 62.273 15.870 16.624 1.00 60.27 ? 2 ILE A O 1 ATOM 10 C CB . ILE A 1 2 ? 60.177 15.989 18.790 1.00 68.16 ? 2 ILE A CB 1 ATOM 11 N N . LYS A 1 3 ? 62.199 13.798 17.414 1.00 70.22 ? 3 LYS A N 1 ATOM 12 C CA . LYS A 1 3 ? 62.542 13.119 16.172 1.00 68.72 ? 3 LYS A CA 1 ATOM 13 C C . LYS A 1 3 ? 61.399 12.280 15.723 1.00 96.50 ? 3 LYS A C 1 ATOM 14 O O . LYS A 1 3 ? 60.438 12.111 16.414 1.00 95.36 ? 3 LYS A O 1 ATOM 15 C CB . LYS A 1 3 ? 63.854 12.394 16.153 1.00 62.39 ? 3 LYS A CB 1 ATOM 16 N N . ASP A 1 4 ? 61.502 11.739 14.521 1.00 96.61 ? 4 ASP A N 1 ATOM 17 C CA . ASP A 1 4 ? 60.434 10.885 13.995 1.00 98.35 ? 4 ASP A CA 1 ATOM 18 C C . ASP A 1 4 ? 60.885 9.452 13.959 1.00 100.00 ? 4 ASP A C 1 ATOM 19 O O . ASP A 1 4 ? 62.014 9.131 13.625 1.00 100.00 ? 4 ASP A O 1 ATOM 20 C CB . ASP A 1 4 ? 60.078 11.321 12.564 1.00 100.00 ? 4 ASP A CB 1 ATOM 21 N N . PRO A 1 5 ? 59.973 8.565 14.178 1.00 97.63 ? 5 PRO A N 1 ATOM 22 C CA . PRO A 1 5 ? 60.219 7.138 14.110 1.00 95.72 ? 5 PRO A CA 1 ATOM 23 C C . PRO A 1 5 ? 60.439 6.765 12.655 1.00 100.00 ? 5 PRO A C 1 ATOM 24 O O . PRO A 1 5 ? 60.621 5.582 12.302 1.00 100.00 ? 5 PRO A O 1 ATOM 25 C CB . PRO A 1 5 ? 58.930 6.557 14.634 1.00 99.10 ? 5 PRO A CB 1 ATOM 26 C CG . PRO A 1 5 ? 57.972 7.700 15.033 1.00 100.00 ? 5 PRO A CG 1 ATOM 27 C CD . PRO A 1 5 ? 58.667 9.014 14.712 1.00 95.06 ? 5 PRO A CD 1 ATOM 28 N N . LYS A 1 6 ? 60.389 7.841 11.817 1.00 96.78 ? 6 LYS A N 1 ATOM 29 C CA . LYS A 1 6 ? 60.619 7.785 10.464 1.00 98.86 ? 6 LYS A CA 1 ATOM 30 C C . LYS A 1 6 ? 61.989 7.110 10.291 1.00 100.00 ? 6 LYS A C 1 ATOM 31 O O . LYS A 1 6 ? 62.180 6.476 9.237 1.00 100.00 ? 6 LYS A O 1 ATOM 32 C CB . LYS A 1 6 ? 60.568 9.177 9.883 1.00 98.32 ? 6 LYS A CB 1 ATOM 33 N N . ILE A 1 7 ? 62.924 7.255 11.284 1.00 100.00 ? 7 ILE A N 1 ATOM 34 C CA . ILE A 1 7 ? 64.281 6.706 11.401 1.00 99.69 ? 7 ILE A CA 1 ATOM 35 C C . ILE A 1 7 ? 64.319 5.159 11.789 1.00 100.00 ? 7 ILE A C 1 ATOM 36 O O . ILE A 1 7 ? 65.137 4.476 11.105 1.00 100.00 ? 7 ILE A O 1 ATOM 37 C CB . ILE A 1 7 ? 65.281 7.604 12.202 1.00 99.28 ? 7 ILE A CB 1 ATOM 38 N N . LEU A 1 8 ? 63.505 4.720 12.816 1.00 100.00 ? 8 LEU A N 1 ATOM 39 C CA . LEU A 1 8 ? 63.350 3.279 13.318 1.00 97.92 ? 8 LEU A CA 1 ATOM 40 C C . LEU A 1 8 ? 62.541 2.334 12.345 1.00 82.08 ? 8 LEU A C 1 ATOM 41 O O . LEU A 1 8 ? 61.942 2.804 11.365 1.00 81.91 ? 8 LEU A O 1 ATOM 42 C CB . LEU A 1 8 ? 62.700 3.099 14.720 1.00 98.06 ? 8 LEU A CB 1 ATOM 43 C CG . LEU A 1 8 ? 63.632 3.100 15.961 1.00 99.35 ? 8 LEU A CG 1 ATOM 44 C CD1 . LEU A 1 8 ? 63.031 2.440 17.214 1.00 96.75 ? 8 LEU A CD1 1 ATOM 45 C CD2 . LEU A 1 8 ? 65.002 2.500 15.646 1.00 91.59 ? 8 LEU A CD2 1 ATOM 46 N N . GLY A 1 9 ? 62.475 1.000 12.607 1.00 64.63 ? 9 GLY A N 1 ATOM 47 C CA . GLY A 1 9 ? 61.703 0.161 11.741 1.00 71.64 ? 9 GLY A CA 1 ATOM 48 C C . GLY A 1 9 ? 60.241 0.458 11.866 1.00 84.93 ? 9 GLY A C 1 ATOM 49 O O . GLY A 1 9 ? 59.600 1.072 10.980 1.00 87.92 ? 9 GLY A O 1 ATOM 50 N N . ILE A 1 10 ? 59.732 0.023 12.989 1.00 87.31 ? 10 ILE A N 1 ATOM 51 C CA . ILE A 1 10 ? 58.378 0.109 13.373 1.00 84.97 ? 10 ILE A CA 1 ATOM 52 C C . ILE A 1 10 ? 57.258 0.205 12.289 1.00 100.00 ? 10 ILE A C 1 ATOM 53 O O . ILE A 1 10 ? 57.197 -0.666 11.375 1.00 100.00 ? 10 ILE A O 1 ATOM 54 C CB . ILE A 1 10 ? 58.158 0.755 14.762 1.00 79.23 ? 10 ILE A CB 1 ATOM 55 C CG1 . ILE A 1 10 ? 59.136 0.164 15.763 1.00 71.17 ? 10 ILE A CG1 1 ATOM 56 C CG2 . ILE A 1 10 ? 56.741 0.442 15.247 1.00 81.63 ? 10 ILE A CG2 1 ATOM 57 C CD1 . ILE A 1 10 ? 60.457 0.882 15.906 1.00 12.22 ? 10 ILE A CD1 1 ATOM 58 N N . ASP A 1 11 ? 56.386 1.209 12.412 1.00 100.00 ? 11 ASP A N 1 ATOM 59 C CA . ASP A 1 11 ? 55.270 1.345 11.461 1.00 97.86 ? 11 ASP A CA 1 ATOM 60 C C . ASP A 1 11 ? 55.585 2.295 10.309 1.00 93.59 ? 11 ASP A C 1 ATOM 61 O O . ASP A 1 11 ? 55.701 3.524 10.490 1.00 96.18 ? 11 ASP A O 1 ATOM 62 C CB . ASP A 1 11 ? 53.944 1.817 12.170 1.00 99.10 ? 11 ASP A CB 1 ATOM 63 C CG . ASP A 1 11 ? 52.630 1.582 11.448 1.00 69.50 ? 11 ASP A CG 1 ATOM 64 O OD1 . ASP A 1 11 ? 52.774 0.969 10.313 1.00 97.73 ? 11 ASP A OD1 1 ATOM 65 O OD2 . ASP A 1 11 ? 51.550 2.052 11.816 1.00 62.75 ? 11 ASP A OD2 1 ATOM 66 N N . PRO A 1 12 ? 55.844 1.692 9.115 1.00 73.65 ? 12 PRO A N 1 ATOM 67 C CA . PRO A 1 12 ? 56.141 2.416 7.889 1.00 79.59 ? 12 PRO A CA 1 ATOM 68 C C . PRO A 1 12 ? 55.007 3.369 7.483 1.00 100.00 ? 12 PRO A C 1 ATOM 69 O O . PRO A 1 12 ? 54.664 4.320 8.223 1.00 100.00 ? 12 PRO A O 1 ATOM 70 C CB . PRO A 1 12 ? 56.336 1.386 6.803 1.00 75.57 ? 12 PRO A CB 1 ATOM 71 C CG . PRO A 1 12 ? 55.975 0.031 7.348 1.00 69.06 ? 12 PRO A CG 1 ATOM 72 C CD . PRO A 1 12 ? 55.894 0.207 8.843 1.00 64.45 ? 12 PRO A CD 1 ATOM 73 N N . ASN A 1 13 ? 54.419 3.023 6.292 1.00 100.00 ? 13 ASN A N 1 ATOM 74 C CA . ASN A 1 13 ? 53.270 3.742 5.611 1.00 100.00 ? 13 ASN A CA 1 ATOM 75 C C . ASN A 1 13 ? 52.679 5.016 6.217 1.00 100.00 ? 13 ASN A C 1 ATOM 76 O O . ASN A 1 13 ? 53.013 6.136 5.740 1.00 96.08 ? 13 ASN A O 1 ATOM 77 C CB . ASN A 1 13 ? 52.294 2.875 4.735 1.00 100.00 ? 13 ASN A CB 1 ATOM 78 N N . VAL A 1 14 ? 51.785 4.811 7.217 1.00 100.00 ? 14 VAL A N 1 ATOM 79 C CA . VAL A 1 14 ? 51.006 5.801 7.954 1.00 100.00 ? 14 VAL A CA 1 ATOM 80 C C . VAL A 1 14 ? 51.618 7.190 8.259 1.00 100.00 ? 14 VAL A C 1 ATOM 81 O O . VAL A 1 14 ? 51.109 8.174 7.708 1.00 100.00 ? 14 VAL A O 1 ATOM 82 C CB . VAL A 1 14 ? 50.513 5.157 9.231 1.00 100.00 ? 14 VAL A CB 1 ATOM 83 N N . THR A 1 15 ? 52.687 7.245 9.118 1.00 100.00 ? 15 THR A N 1 ATOM 84 C CA . THR A 1 15 ? 53.420 8.472 9.543 1.00 99.93 ? 15 THR A CA 1 ATOM 85 C C . THR A 1 15 ? 53.480 8.682 11.050 1.00 95.47 ? 15 THR A C 1 ATOM 86 O O . THR A 1 15 ? 52.604 9.306 11.669 1.00 94.40 ? 15 THR A O 1 ATOM 87 C CB . THR A 1 15 ? 53.088 9.782 8.821 1.00 100.00 ? 15 THR A CB 1 ATOM 88 N N . GLN A 1 16 ? 54.534 8.155 11.631 1.00 77.79 ? 16 GLN A N 1 ATOM 89 C CA . GLN A 1 16 ? 54.708 8.278 13.051 1.00 68.68 ? 16 GLN A CA 1 ATOM 90 C C . GLN A 1 16 ? 55.635 9.443 13.406 1.00 70.47 ? 16 GLN A C 1 ATOM 91 O O . GLN A 1 16 ? 56.451 9.895 12.583 1.00 71.63 ? 16 GLN A O 1 ATOM 92 C CB . GLN A 1 16 ? 55.134 6.926 13.631 1.00 67.07 ? 16 GLN A CB 1 ATOM 93 N N . TYR A 1 17 ? 55.492 9.931 14.639 1.00 56.58 ? 17 TYR A N 1 ATOM 94 C CA . TYR A 1 17 ? 56.265 11.020 15.199 1.00 52.44 ? 17 TYR A CA 1 ATOM 95 C C . TYR A 1 17 ? 56.511 10.780 16.710 1.00 64.63 ? 17 TYR A C 1 ATOM 96 O O . TYR A 1 17 ? 55.622 10.361 17.473 1.00 58.45 ? 17 TYR A O 1 ATOM 97 C CB . TYR A 1 17 ? 55.564 12.357 14.932 1.00 50.94 ? 17 TYR A CB 1 ATOM 98 N N . THR A 1 18 ? 57.738 11.016 17.173 1.00 60.33 ? 18 THR A N 1 ATOM 99 C CA . THR A 1 18 ? 58.026 10.797 18.583 1.00 51.65 ? 18 THR A CA 1 ATOM 100 C C . THR A 1 18 ? 58.844 11.907 19.183 1.00 43.74 ? 18 THR A C 1 ATOM 101 O O . THR A 1 18 ? 59.057 12.912 18.521 1.00 35.06 ? 18 THR A O 1 ATOM 102 C CB . THR A 1 18 ? 58.507 9.366 18.924 1.00 35.95 ? 18 THR A CB 1 ATOM 103 O OG1 . THR A 1 18 ? 59.916 9.166 18.827 1.00 41.28 ? 18 THR A OG1 1 ATOM 104 C CG2 . THR A 1 18 ? 57.754 8.369 18.053 1.00 17.10 ? 18 THR A CG2 1 ATOM 105 N N . GLY A 1 19 ? 59.285 11.728 20.427 1.00 52.09 ? 19 GLY A N 1 ATOM 106 C CA . GLY A 1 19 ? 60.073 12.744 21.110 1.00 53.53 ? 19 GLY A CA 1 ATOM 107 C C . GLY A 1 19 ? 59.542 13.187 22.512 1.00 61.50 ? 19 GLY A C 1 ATOM 108 O O . GLY A 1 19 ? 58.940 12.402 23.253 1.00 53.99 ? 19 GLY A O 1 ATOM 109 N N . TYR A 1 20 ? 59.782 14.478 22.860 1.00 62.70 ? 20 TYR A N 1 ATOM 110 C CA . TYR A 1 20 ? 59.447 15.128 24.136 1.00 60.39 ? 20 TYR A CA 1 ATOM 111 C C . TYR A 1 20 ? 58.688 16.450 24.073 1.00 68.65 ? 20 TYR A C 1 ATOM 112 O O . TYR A 1 20 ? 58.862 17.246 23.167 1.00 93.23 ? 20 TYR A O 1 ATOM 113 C CB . TYR A 1 20 ? 60.775 15.451 24.891 1.00 60.42 ? 20 TYR A CB 1 ATOM 114 C CG . TYR A 1 20 ? 61.468 14.189 25.351 1.00 75.96 ? 20 TYR A CG 1 ATOM 115 C CD1 . TYR A 1 20 ? 61.127 13.621 26.580 1.00 79.80 ? 20 TYR A CD1 1 ATOM 116 C CD2 . TYR A 1 20 ? 62.432 13.549 24.568 1.00 81.85 ? 20 TYR A CD2 1 ATOM 117 C CE1 . TYR A 1 20 ? 61.725 12.443 27.028 1.00 79.31 ? 20 TYR A CE1 1 ATOM 118 C CE2 . TYR A 1 20 ? 63.050 12.373 25.001 1.00 82.79 ? 20 TYR A CE2 1 ATOM 119 C CZ . TYR A 1 20 ? 62.691 11.826 26.232 1.00 85.47 ? 20 TYR A CZ 1 ATOM 120 O OH . TYR A 1 20 ? 63.288 10.676 26.648 1.00 100.00 ? 20 TYR A OH 1 ATOM 121 N N . LEU A 1 21 ? 57.865 16.678 25.094 1.00 47.80 ? 21 LEU A N 1 ATOM 122 C CA . LEU A 1 21 ? 57.088 17.891 25.323 1.00 42.80 ? 21 LEU A CA 1 ATOM 123 C C . LEU A 1 21 ? 57.613 18.325 26.688 1.00 58.86 ? 21 LEU A C 1 ATOM 124 O O . LEU A 1 21 ? 57.595 17.565 27.651 1.00 66.13 ? 21 LEU A O 1 ATOM 125 C CB . LEU A 1 21 ? 55.545 17.703 25.393 1.00 41.73 ? 21 LEU A CB 1 ATOM 126 C CG . LEU A 1 21 ? 54.744 18.140 24.161 1.00 40.28 ? 21 LEU A CG 1 ATOM 127 C CD1 . LEU A 1 21 ? 55.257 17.336 22.990 1.00 41.22 ? 21 LEU A CD1 1 ATOM 128 C CD2 . LEU A 1 21 ? 53.247 17.827 24.320 1.00 15.03 ? 21 LEU A CD2 1 ATOM 129 N N . ASP A 1 22 ? 58.134 19.517 26.800 1.00 61.41 ? 22 ASP A N 1 ATOM 130 C CA . ASP A 1 22 ? 58.665 19.925 28.080 1.00 62.48 ? 22 ASP A CA 1 ATOM 131 C C . ASP A 1 22 ? 57.806 20.967 28.861 1.00 70.13 ? 22 ASP A C 1 ATOM 132 O O . ASP A 1 22 ? 56.946 21.686 28.322 1.00 60.84 ? 22 ASP A O 1 ATOM 133 C CB . ASP A 1 22 ? 60.152 20.356 27.903 1.00 61.81 ? 22 ASP A CB 1 ATOM 134 C CG . ASP A 1 22 ? 61.096 19.308 27.340 1.00 66.20 ? 22 ASP A CG 1 ATOM 135 O OD1 . ASP A 1 22 ? 60.520 18.499 26.460 1.00 85.52 ? 22 ASP A OD1 1 ATOM 136 O OD2 . ASP A 1 22 ? 62.299 19.258 27.645 1.00 46.69 ? 22 ASP A OD2 1 ATOM 137 N N . VAL A 1 23 ? 58.068 21.030 30.172 1.00 69.26 ? 23 VAL A N 1 ATOM 138 C CA . VAL A 1 23 ? 57.420 21.939 31.094 1.00 63.67 ? 23 VAL A CA 1 ATOM 139 C C . VAL A 1 23 ? 58.466 22.710 31.904 1.00 87.12 ? 23 VAL A C 1 ATOM 140 O O . VAL A 1 23 ? 59.012 22.268 32.932 1.00 84.33 ? 23 VAL A O 1 ATOM 141 C CB . VAL A 1 23 ? 56.330 21.296 31.948 1.00 55.37 ? 23 VAL A CB 1 ATOM 142 C CG1 . VAL A 1 23 ? 56.961 20.370 32.949 1.00 63.66 ? 23 VAL A CG1 1 ATOM 143 C CG2 . VAL A 1 23 ? 55.557 22.344 32.721 1.00 49.93 ? 23 VAL A CG2 1 ATOM 144 N N . GLU A 1 24 ? 58.733 23.888 31.375 1.00 95.82 ? 24 GLU A N 1 ATOM 145 C CA . GLU A 1 24 ? 59.666 24.857 31.901 1.00 99.31 ? 24 GLU A CA 1 ATOM 146 C C . GLU A 1 24 ? 59.796 24.898 33.430 1.00 98.43 ? 24 GLU A C 1 ATOM 147 O O . GLU A 1 24 ? 60.642 24.229 34.038 1.00 88.61 ? 24 GLU A O 1 ATOM 148 C CB . GLU A 1 24 ? 59.224 26.219 31.376 1.00 100.00 ? 24 GLU A CB 1 ATOM 149 N N . ASP A 1 25 ? 58.932 25.724 34.014 1.00 98.51 ? 25 ASP A N 1 ATOM 150 C CA . ASP A 1 25 ? 58.856 25.971 35.437 1.00 99.78 ? 25 ASP A CA 1 ATOM 151 C C . ASP A 1 25 ? 58.875 24.724 36.294 1.00 98.29 ? 25 ASP A C 1 ATOM 152 O O . ASP A 1 25 ? 59.449 24.740 37.377 1.00 100.00 ? 25 ASP A O 1 ATOM 153 C CB . ASP A 1 25 ? 57.610 26.799 35.808 1.00 100.00 ? 25 ASP A CB 1 ATOM 154 C CG . ASP A 1 25 ? 56.345 25.993 35.623 1.00 100.00 ? 25 ASP A CG 1 ATOM 155 O OD1 . ASP A 1 25 ? 55.902 25.205 36.470 1.00 100.00 ? 25 ASP A OD1 1 ATOM 156 O OD2 . ASP A 1 25 ? 55.806 26.211 34.437 1.00 100.00 ? 25 ASP A OD2 1 ATOM 157 N N . GLU A 1 26 ? 58.233 23.649 35.866 1.00 77.32 ? 26 GLU A N 1 ATOM 158 C CA . GLU A 1 26 ? 58.268 22.509 36.739 1.00 76.86 ? 26 GLU A CA 1 ATOM 159 C C . GLU A 1 26 ? 59.432 21.546 36.449 1.00 79.75 ? 26 GLU A C 1 ATOM 160 O O . GLU A 1 26 ? 59.780 20.679 37.269 1.00 84.38 ? 26 GLU A O 1 ATOM 161 C CB . GLU A 1 26 ? 56.882 21.906 36.996 1.00 76.91 ? 26 GLU A CB 1 ATOM 162 N N . ASP A 1 27 ? 60.069 21.723 35.283 1.00 59.99 ? 27 ASP A N 1 ATOM 163 C CA . ASP A 1 27 ? 61.203 20.877 34.891 1.00 58.62 ? 27 ASP A CA 1 ATOM 164 C C . ASP A 1 27 ? 60.800 19.430 34.667 1.00 55.87 ? 27 ASP A C 1 ATOM 165 O O . ASP A 1 27 ? 61.449 18.481 35.091 1.00 51.60 ? 27 ASP A O 1 ATOM 166 C CB . ASP A 1 27 ? 62.427 20.974 35.841 1.00 57.07 ? 27 ASP A CB 1 ATOM 167 C CG . ASP A 1 27 ? 63.631 20.148 35.437 1.00 54.74 ? 27 ASP A CG 1 ATOM 168 O OD1 . ASP A 1 27 ? 63.549 19.695 34.229 1.00 49.96 ? 27 ASP A OD1 1 ATOM 169 O OD2 . ASP A 1 27 ? 64.474 19.762 36.208 1.00 70.32 ? 27 ASP A OD2 1 ATOM 170 N N . LYS A 1 28 ? 59.709 19.247 33.975 1.00 54.45 ? 28 LYS A N 1 ATOM 171 C CA . LYS A 1 28 ? 59.254 17.900 33.711 1.00 60.31 ? 28 LYS A CA 1 ATOM 172 C C . LYS A 1 28 ? 59.341 17.548 32.200 1.00 65.74 ? 28 LYS A C 1 ATOM 173 O O . LYS A 1 28 ? 58.918 18.308 31.330 1.00 64.82 ? 28 LYS A O 1 ATOM 174 C CB . LYS A 1 28 ? 57.907 17.597 34.404 1.00 61.36 ? 28 LYS A CB 1 ATOM 175 C CG . LYS A 1 28 ? 57.779 18.111 35.863 1.00 45.12 ? 28 LYS A CG 1 ATOM 176 C CD . LYS A 1 28 ? 56.353 18.503 36.326 1.00 56.28 ? 28 LYS A CD 1 ATOM 177 C CE . LYS A 1 28 ? 56.038 18.358 37.827 1.00 39.24 ? 28 LYS A CE 1 ATOM 178 N NZ . LYS A 1 28 ? 55.377 19.564 38.397 1.00 65.79 ? 28 LYS A NZ 1 ATOM 179 N N . HIS A 1 29 ? 59.900 16.377 31.875 1.00 55.06 ? 29 HIS A N 1 ATOM 180 C CA . HIS A 1 29 ? 60.061 15.998 30.494 1.00 48.00 ? 29 HIS A CA 1 ATOM 181 C C . HIS A 1 29 ? 59.236 14.816 30.013 1.00 32.41 ? 29 HIS A C 1 ATOM 182 O O . HIS A 1 29 ? 59.563 13.631 30.115 1.00 38.07 ? 29 HIS A O 1 ATOM 183 C CB . HIS A 1 29 ? 61.567 15.909 30.206 1.00 59.36 ? 29 HIS A CB 1 ATOM 184 C CG . HIS A 1 29 ? 62.339 16.967 30.977 1.00 69.06 ? 29 HIS A CG 1 ATOM 185 N ND1 . HIS A 1 29 ? 62.955 18.055 30.346 1.00 71.00 ? 29 HIS A ND1 1 ATOM 186 C CD2 . HIS A 1 29 ? 62.562 17.091 32.322 1.00 74.26 ? 29 HIS A CD2 1 ATOM 187 C CE1 . HIS A 1 29 ? 63.523 18.788 31.299 1.00 72.48 ? 29 HIS A CE1 1 ATOM 188 N NE2 . HIS A 1 29 ? 63.306 18.233 32.492 1.00 74.34 ? 29 HIS A NE2 1 ATOM 189 N N . PHE A 1 30 ? 58.113 15.156 29.467 1.00 16.54 ? 30 PHE A N 1 ATOM 190 C CA . PHE A 1 30 ? 57.248 14.134 28.962 1.00 22.38 ? 30 PHE A CA 1 ATOM 191 C C . PHE A 1 30 ? 57.778 13.444 27.725 1.00 33.14 ? 30 PHE A C 1 ATOM 192 O O . PHE A 1 30 ? 58.383 14.053 26.888 1.00 51.70 ? 30 PHE A O 1 ATOM 193 C CB . PHE A 1 30 ? 55.854 14.715 28.794 1.00 28.42 ? 30 PHE A CB 1 ATOM 194 C CG . PHE A 1 30 ? 55.464 15.044 30.206 1.00 47.28 ? 30 PHE A CG 1 ATOM 195 C CD1 . PHE A 1 30 ? 54.913 14.096 31.071 1.00 60.16 ? 30 PHE A CD1 1 ATOM 196 C CD2 . PHE A 1 30 ? 55.738 16.305 30.730 1.00 65.50 ? 30 PHE A CD2 1 ATOM 197 C CE1 . PHE A 1 30 ? 54.589 14.408 32.395 1.00 62.34 ? 30 PHE A CE1 1 ATOM 198 C CE2 . PHE A 1 30 ? 55.417 16.635 32.049 1.00 65.79 ? 30 PHE A CE2 1 ATOM 199 C CZ . PHE A 1 30 ? 54.838 15.686 32.893 1.00 56.00 ? 30 PHE A CZ 1 ATOM 200 N N . PHE A 1 31 ? 57.571 12.163 27.600 1.00 18.84 ? 31 PHE A N 1 ATOM 201 C CA . PHE A 1 31 ? 58.034 11.477 26.422 1.00 23.09 ? 31 PHE A CA 1 ATOM 202 C C . PHE A 1 31 ? 56.843 10.789 25.745 1.00 66.31 ? 31 PHE A C 1 ATOM 203 O O . PHE A 1 31 ? 56.042 10.124 26.401 1.00 85.03 ? 31 PHE A O 1 ATOM 204 C CB . PHE A 1 31 ? 59.122 10.463 26.768 1.00 24.67 ? 31 PHE A CB 1 ATOM 205 C CG . PHE A 1 31 ? 59.317 9.509 25.648 1.00 27.96 ? 31 PHE A CG 1 ATOM 206 C CD1 . PHE A 1 31 ? 58.510 8.381 25.488 1.00 41.13 ? 31 PHE A CD1 1 ATOM 207 C CD2 . PHE A 1 31 ? 60.349 9.743 24.745 1.00 43.31 ? 31 PHE A CD2 1 ATOM 208 C CE1 . PHE A 1 31 ? 58.692 7.530 24.403 1.00 60.06 ? 31 PHE A CE1 1 ATOM 209 C CE2 . PHE A 1 31 ? 60.556 8.887 23.668 1.00 51.64 ? 31 PHE A CE2 1 ATOM 210 C CZ . PHE A 1 31 ? 59.719 7.787 23.495 1.00 59.80 ? 31 PHE A CZ 1 ATOM 211 N N . PHE A 1 32 ? 56.736 10.870 24.425 1.00 54.09 ? 32 PHE A N 1 ATOM 212 C CA . PHE A 1 32 ? 55.625 10.231 23.728 1.00 41.44 ? 32 PHE A CA 1 ATOM 213 C C . PHE A 1 32 ? 56.159 9.607 22.460 1.00 40.42 ? 32 PHE A C 1 ATOM 214 O O . PHE A 1 32 ? 57.305 9.835 22.061 1.00 32.52 ? 32 PHE A O 1 ATOM 215 C CB . PHE A 1 32 ? 54.530 11.254 23.379 1.00 49.01 ? 32 PHE A CB 1 ATOM 216 C CG . PHE A 1 32 ? 55.145 12.329 22.502 1.00 64.27 ? 32 PHE A CG 1 ATOM 217 C CD1 . PHE A 1 32 ? 56.113 13.195 23.014 1.00 70.37 ? 32 PHE A CD1 1 ATOM 218 C CD2 . PHE A 1 32 ? 54.809 12.443 21.151 1.00 73.69 ? 32 PHE A CD2 1 ATOM 219 C CE1 . PHE A 1 32 ? 56.724 14.170 22.226 1.00 73.11 ? 32 PHE A CE1 1 ATOM 220 C CE2 . PHE A 1 32 ? 55.402 13.409 20.340 1.00 73.66 ? 32 PHE A CE2 1 ATOM 221 C CZ . PHE A 1 32 ? 56.361 14.267 20.882 1.00 73.86 ? 32 PHE A CZ 1 ATOM 222 N N . TRP A 1 33 ? 55.301 8.818 21.837 1.00 52.21 ? 33 TRP A N 1 ATOM 223 C CA . TRP A 1 33 ? 55.579 8.083 20.609 1.00 53.95 ? 33 TRP A CA 1 ATOM 224 C C . TRP A 1 33 ? 54.257 7.865 19.903 1.00 60.28 ? 33 TRP A C 1 ATOM 225 O O . TRP A 1 33 ? 53.525 6.913 20.187 1.00 42.79 ? 33 TRP A O 1 ATOM 226 C CB . TRP A 1 33 ? 56.159 6.708 20.982 1.00 53.01 ? 33 TRP A CB 1 ATOM 227 C CG . TRP A 1 33 ? 57.073 5.994 20.005 1.00 57.02 ? 33 TRP A CG 1 ATOM 228 C CD1 . TRP A 1 33 ? 58.319 5.527 20.307 1.00 60.41 ? 33 TRP A CD1 1 ATOM 229 C CD2 . TRP A 1 33 ? 56.837 5.574 18.651 1.00 53.44 ? 33 TRP A CD2 1 ATOM 230 N NE1 . TRP A 1 33 ? 58.885 4.865 19.248 1.00 51.07 ? 33 TRP A NE1 1 ATOM 231 C CE2 . TRP A 1 33 ? 58.007 4.891 18.222 1.00 45.32 ? 33 TRP A CE2 1 ATOM 232 C CE3 . TRP A 1 33 ? 55.769 5.729 17.770 1.00 56.38 ? 33 TRP A CE3 1 ATOM 233 C CZ2 . TRP A 1 33 ? 58.124 4.382 16.958 1.00 41.27 ? 33 TRP A CZ2 1 ATOM 234 C CZ3 . TRP A 1 33 ? 55.890 5.195 16.513 1.00 57.70 ? 33 TRP A CZ3 1 ATOM 235 C CH2 . TRP A 1 33 ? 57.078 4.562 16.101 1.00 54.57 ? 33 TRP A CH2 1 ATOM 236 N N . THR A 1 34 ? 53.969 8.767 18.981 1.00 59.60 ? 34 THR A N 1 ATOM 237 C CA . THR A 1 34 ? 52.731 8.711 18.254 1.00 49.08 ? 34 THR A CA 1 ATOM 238 C C . THR A 1 34 ? 52.753 8.021 16.909 1.00 41.12 ? 34 THR A C 1 ATOM 239 O O . THR A 1 34 ? 53.758 7.834 16.241 1.00 36.17 ? 34 THR A O 1 ATOM 240 C CB . THR A 1 34 ? 52.147 10.112 18.089 1.00 54.14 ? 34 THR A CB 1 ATOM 241 O OG1 . THR A 1 34 ? 52.569 10.965 19.145 1.00 49.47 ? 34 THR A OG1 1 ATOM 242 C CG2 . THR A 1 34 ? 50.640 10.008 18.037 1.00 64.20 ? 34 THR A CG2 1 ATOM 243 N N . PHE A 1 35 ? 51.554 7.667 16.534 1.00 45.63 ? 35 PHE A N 1 ATOM 244 C CA . PHE A 1 35 ? 51.249 7.006 15.293 1.00 44.93 ? 35 PHE A CA 1 ATOM 245 C C . PHE A 1 35 ? 49.886 7.518 14.732 1.00 62.64 ? 35 PHE A C 1 ATOM 246 O O . PHE A 1 35 ? 48.907 7.724 15.478 1.00 61.92 ? 35 PHE A O 1 ATOM 247 C CB . PHE A 1 35 ? 51.431 5.472 15.387 1.00 39.27 ? 35 PHE A CB 1 ATOM 248 N N . GLU A 1 36 ? 49.863 7.755 13.401 1.00 51.64 ? 36 GLU A N 1 ATOM 249 C CA . GLU A 1 36 ? 48.712 8.235 12.670 1.00 44.75 ? 36 GLU A CA 1 ATOM 250 C C . GLU A 1 36 ? 47.879 7.061 12.156 1.00 46.78 ? 36 GLU A C 1 ATOM 251 O O . GLU A 1 36 ? 48.420 6.007 11.829 1.00 56.20 ? 36 GLU A O 1 ATOM 252 C CB . GLU A 1 36 ? 49.208 9.123 11.522 1.00 49.02 ? 36 GLU A CB 1 ATOM 253 C CG . GLU A 1 36 ? 49.500 10.597 11.889 1.00 75.61 ? 36 GLU A CG 1 ATOM 254 C CD . GLU A 1 36 ? 49.326 11.527 10.710 1.00 53.81 ? 36 GLU A CD 1 ATOM 255 O OE1 . GLU A 1 36 ? 49.481 10.927 9.570 1.00 35.31 ? 36 GLU A OE1 1 ATOM 256 O OE2 . GLU A 1 36 ? 49.039 12.710 10.807 1.00 61.76 ? 36 GLU A OE2 1 ATOM 257 N N . SER A 1 37 ? 46.578 7.229 12.087 1.00 33.47 ? 37 SER A N 1 ATOM 258 C CA . SER A 1 37 ? 45.753 6.145 11.626 1.00 34.67 ? 37 SER A CA 1 ATOM 259 C C . SER A 1 37 ? 46.157 5.436 10.331 1.00 51.55 ? 37 SER A C 1 ATOM 260 O O . SER A 1 37 ? 46.558 6.053 9.348 1.00 63.59 ? 37 SER A O 1 ATOM 261 C CB . SER A 1 37 ? 44.301 6.502 11.613 1.00 35.90 ? 37 SER A CB 1 ATOM 262 O OG . SER A 1 37 ? 43.628 5.313 11.293 1.00 33.33 ? 37 SER A OG 1 ATOM 263 N N . ARG A 1 38 ? 46.062 4.109 10.371 1.00 58.64 ? 38 ARG A N 1 ATOM 264 C CA . ARG A 1 38 ? 46.380 3.240 9.239 1.00 67.22 ? 38 ARG A CA 1 ATOM 265 C C . ARG A 1 38 ? 45.367 3.473 8.092 1.00 86.04 ? 38 ARG A C 1 ATOM 266 O O . ARG A 1 38 ? 45.516 3.042 6.931 1.00 85.89 ? 38 ARG A O 1 ATOM 267 C CB . ARG A 1 38 ? 46.460 1.750 9.643 1.00 67.06 ? 38 ARG A CB 1 ATOM 268 C CG . ARG A 1 38 ? 47.022 1.450 11.037 1.00 45.91 ? 38 ARG A CG 1 ATOM 269 C CD . ARG A 1 38 ? 48.378 0.776 10.959 1.00 71.40 ? 38 ARG A CD 1 ATOM 270 N NE . ARG A 1 38 ? 48.382 -0.630 11.357 1.00 74.12 ? 38 ARG A NE 1 ATOM 271 C CZ . ARG A 1 38 ? 49.531 -1.296 11.552 1.00 73.63 ? 38 ARG A CZ 1 ATOM 272 N NH1 . ARG A 1 38 ? 50.719 -0.713 11.410 1.00 34.05 ? 38 ARG A NH1 1 ATOM 273 N NH2 . ARG A 1 38 ? 49.522 -2.572 11.915 1.00 33.24 ? 38 ARG A NH2 1 ATOM 274 N N . ASN A 1 39 ? 44.308 4.179 8.465 1.00 85.65 ? 39 ASN A N 1 ATOM 275 C CA . ASN A 1 39 ? 43.238 4.550 7.563 1.00 82.71 ? 39 ASN A CA 1 ATOM 276 C C . ASN A 1 39 ? 43.345 6.056 7.295 1.00 75.51 ? 39 ASN A C 1 ATOM 277 O O . ASN A 1 39 ? 44.267 6.528 6.634 1.00 81.32 ? 39 ASN A O 1 ATOM 278 C CB . ASN A 1 39 ? 41.851 4.153 8.117 1.00 70.24 ? 39 ASN A CB 1 ATOM 279 C CG . ASN A 1 39 ? 40.856 3.949 7.003 1.00 80.90 ? 39 ASN A CG 1 ATOM 280 O OD1 . ASN A 1 39 ? 41.103 3.144 6.095 1.00 100.00 ? 39 ASN A OD1 1 ATOM 281 N ND2 . ASN A 1 39 ? 39.867 4.831 6.942 1.00 88.39 ? 39 ASN A ND2 1 ATOM 282 N N . ASP A 1 40 ? 42.423 6.831 7.828 1.00 59.16 ? 40 ASP A N 1 ATOM 283 C CA . ASP A 1 40 ? 42.489 8.261 7.646 1.00 63.57 ? 40 ASP A CA 1 ATOM 284 C C . ASP A 1 40 ? 42.659 8.965 8.991 1.00 54.92 ? 40 ASP A C 1 ATOM 285 O O . ASP A 1 40 ? 41.793 8.899 9.869 1.00 51.18 ? 40 ASP A O 1 ATOM 286 C CB . ASP A 1 40 ? 41.323 8.818 6.815 1.00 76.49 ? 40 ASP A CB 1 ATOM 287 C CG . ASP A 1 40 ? 41.544 10.259 6.439 1.00 100.00 ? 40 ASP A CG 1 ATOM 288 O OD1 . ASP A 1 40 ? 42.654 10.734 6.178 1.00 95.11 ? 40 ASP A OD1 1 ATOM 289 O OD2 . ASP A 1 40 ? 40.418 10.946 6.470 1.00 100.00 ? 40 ASP A OD2 1 ATOM 290 N N . PRO A 1 41 ? 43.800 9.631 9.174 1.00 49.29 ? 41 PRO A N 1 ATOM 291 C CA . PRO A 1 41 ? 44.047 10.305 10.444 1.00 47.15 ? 41 PRO A CA 1 ATOM 292 C C . PRO A 1 41 ? 43.085 11.464 10.667 1.00 38.02 ? 41 PRO A C 1 ATOM 293 O O . PRO A 1 41 ? 42.671 11.795 11.761 1.00 30.70 ? 41 PRO A O 1 ATOM 294 C CB . PRO A 1 41 ? 45.512 10.764 10.419 1.00 50.62 ? 41 PRO A CB 1 ATOM 295 C CG . PRO A 1 41 ? 46.183 10.080 9.230 1.00 56.84 ? 41 PRO A CG 1 ATOM 296 C CD . PRO A 1 41 ? 45.065 9.466 8.387 1.00 55.30 ? 41 PRO A CD 1 ATOM 297 N N . ALA A 1 42 ? 42.703 12.067 9.573 1.00 31.45 ? 42 ALA A N 1 ATOM 298 C CA . ALA A 1 42 ? 41.788 13.184 9.575 1.00 26.20 ? 42 ALA A CA 1 ATOM 299 C C . ALA A 1 42 ? 40.420 12.842 10.150 1.00 42.12 ? 42 ALA A C 1 ATOM 300 O O . ALA A 1 42 ? 39.779 13.650 10.822 1.00 42.79 ? 42 ALA A O 1 ATOM 301 C CB . ALA A 1 42 ? 41.595 13.644 8.133 1.00 23.69 ? 42 ALA A CB 1 ATOM 302 N N . LYS A 1 43 ? 39.929 11.657 9.838 1.00 47.52 ? 43 LYS A N 1 ATOM 303 C CA . LYS A 1 43 ? 38.631 11.294 10.348 1.00 48.62 ? 43 LYS A CA 1 ATOM 304 C C . LYS A 1 43 ? 38.866 10.628 11.667 1.00 66.71 ? 43 LYS A C 1 ATOM 305 O O . LYS A 1 43 ? 38.479 11.137 12.714 1.00 66.86 ? 43 LYS A O 1 ATOM 306 C CB . LYS A 1 43 ? 37.844 10.413 9.383 1.00 47.14 ? 43 LYS A CB 1 ATOM 307 N N . ASP A 1 44 ? 39.561 9.500 11.573 1.00 70.98 ? 44 ASP A N 1 ATOM 308 C CA . ASP A 1 44 ? 39.931 8.665 12.700 1.00 65.75 ? 44 ASP A CA 1 ATOM 309 C C . ASP A 1 44 ? 40.253 9.402 14.002 1.00 69.27 ? 44 ASP A C 1 ATOM 310 O O . ASP A 1 44 ? 40.989 10.393 14.017 1.00 69.48 ? 44 ASP A O 1 ATOM 311 C CB . ASP A 1 44 ? 40.890 7.547 12.272 1.00 56.55 ? 44 ASP A CB 1 ATOM 312 C CG . ASP A 1 44 ? 40.169 6.788 11.180 1.00 45.59 ? 44 ASP A CG 1 ATOM 313 O OD1 . ASP A 1 44 ? 38.952 6.829 11.059 1.00 40.89 ? 44 ASP A OD1 1 ATOM 314 O OD2 . ASP A 1 44 ? 40.943 6.130 10.346 1.00 31.48 ? 44 ASP A OD2 1 ATOM 315 N N . PRO A 1 45 ? 39.654 8.908 15.103 1.00 58.82 ? 45 PRO A N 1 ATOM 316 C CA . PRO A 1 45 ? 39.846 9.494 16.409 1.00 54.37 ? 45 PRO A CA 1 ATOM 317 C C . PRO A 1 45 ? 41.293 9.558 16.848 1.00 61.20 ? 45 PRO A C 1 ATOM 318 O O . PRO A 1 45 ? 42.243 9.224 16.132 1.00 62.74 ? 45 PRO A O 1 ATOM 319 C CB . PRO A 1 45 ? 39.063 8.641 17.416 1.00 52.62 ? 45 PRO A CB 1 ATOM 320 C CG . PRO A 1 45 ? 38.257 7.637 16.614 1.00 58.50 ? 45 PRO A CG 1 ATOM 321 C CD . PRO A 1 45 ? 38.564 7.885 15.143 1.00 58.86 ? 45 PRO A CD 1 ATOM 322 N N . VAL A 1 46 ? 41.415 10.026 18.079 1.00 53.20 ? 46 VAL A N 1 ATOM 323 C CA . VAL A 1 46 ? 42.681 10.161 18.761 1.00 44.50 ? 46 VAL A CA 1 ATOM 324 C C . VAL A 1 46 ? 42.583 9.380 20.070 1.00 42.30 ? 46 VAL A C 1 ATOM 325 O O . VAL A 1 46 ? 41.494 9.338 20.745 1.00 27.54 ? 46 VAL A O 1 ATOM 326 C CB . VAL A 1 46 ? 43.125 11.606 18.929 1.00 36.22 ? 46 VAL A CB 1 ATOM 327 C CG1 . VAL A 1 46 ? 44.520 11.653 19.545 1.00 33.06 ? 46 VAL A CG1 1 ATOM 328 C CG2 . VAL A 1 46 ? 43.140 12.254 17.563 1.00 30.76 ? 46 VAL A CG2 1 ATOM 329 N N . ILE A 1 47 ? 43.720 8.741 20.395 1.00 47.34 ? 47 ILE A N 1 ATOM 330 C CA . ILE A 1 47 ? 43.784 7.899 21.580 1.00 48.60 ? 47 ILE A CA 1 ATOM 331 C C . ILE A 1 47 ? 44.988 8.032 22.487 1.00 40.88 ? 47 ILE A C 1 ATOM 332 O O . ILE A 1 47 ? 46.125 7.933 22.016 1.00 40.45 ? 47 ILE A O 1 ATOM 333 C CB . ILE A 1 47 ? 43.626 6.420 21.186 1.00 48.24 ? 47 ILE A CB 1 ATOM 334 C CG1 . ILE A 1 47 ? 42.271 6.154 20.507 1.00 43.54 ? 47 ILE A CG1 1 ATOM 335 C CG2 . ILE A 1 47 ? 43.750 5.574 22.429 1.00 41.88 ? 47 ILE A CG2 1 ATOM 336 C CD1 . ILE A 1 47 ? 41.789 4.712 20.614 1.00 17.53 ? 47 ILE A CD1 1 ATOM 337 N N . LEU A 1 48 ? 44.696 8.097 23.801 1.00 40.32 ? 48 LEU A N 1 ATOM 338 C CA . LEU A 1 48 ? 45.714 8.166 24.843 1.00 30.02 ? 48 LEU A CA 1 ATOM 339 C C . LEU A 1 48 ? 45.892 6.802 25.575 1.00 28.70 ? 48 LEU A C 1 ATOM 340 O O . LEU A 1 48 ? 45.066 6.338 26.356 1.00 16.30 ? 48 LEU A O 1 ATOM 341 C CB . LEU A 1 48 ? 45.633 9.345 25.777 1.00 17.95 ? 48 LEU A CB 1 ATOM 342 C CG . LEU A 1 48 ? 47.044 9.431 26.291 1.00 20.05 ? 48 LEU A CG 1 ATOM 343 C CD1 . LEU A 1 48 ? 47.938 8.929 25.177 1.00 12.42 ? 48 LEU A CD1 1 ATOM 344 C CD2 . LEU A 1 48 ? 47.483 10.861 26.595 1.00 36.01 ? 48 LEU A CD2 1 ATOM 345 N N . TRP A 1 49 ? 46.981 6.109 25.300 1.00 27.97 ? 49 TRP A N 1 ATOM 346 C CA . TRP A 1 49 ? 47.104 4.820 25.980 1.00 34.38 ? 49 TRP A CA 1 ATOM 347 C C . TRP A 1 49 ? 47.840 4.958 27.251 1.00 35.00 ? 49 TRP A C 1 ATOM 348 O O . TRP A 1 49 ? 48.854 5.638 27.260 1.00 33.37 ? 49 TRP A O 1 ATOM 349 C CB . TRP A 1 49 ? 47.718 3.692 25.151 1.00 24.91 ? 49 TRP A CB 1 ATOM 350 C CG . TRP A 1 49 ? 47.954 2.463 25.936 1.00 20.39 ? 49 TRP A CG 1 ATOM 351 C CD1 . TRP A 1 49 ? 49.118 2.093 26.485 1.00 26.02 ? 49 TRP A CD1 1 ATOM 352 C CD2 . TRP A 1 49 ? 47.017 1.439 26.267 1.00 22.13 ? 49 TRP A CD2 1 ATOM 353 N NE1 . TRP A 1 49 ? 48.986 0.876 27.126 1.00 24.40 ? 49 TRP A NE1 1 ATOM 354 C CE2 . TRP A 1 49 ? 47.703 0.445 26.990 1.00 20.25 ? 49 TRP A CE2 1 ATOM 355 C CE3 . TRP A 1 49 ? 45.661 1.251 26.027 1.00 26.47 ? 49 TRP A CE3 1 ATOM 356 C CZ2 . TRP A 1 49 ? 47.068 -0.709 27.459 1.00 14.39 ? 49 TRP A CZ2 1 ATOM 357 C CZ3 . TRP A 1 49 ? 45.041 0.094 26.491 1.00 23.73 ? 49 TRP A CZ3 1 ATOM 358 C CH2 . TRP A 1 49 ? 45.733 -0.883 27.203 1.00 16.38 ? 49 TRP A CH2 1 ATOM 359 N N . LEU A 1 50 ? 47.332 4.315 28.295 1.00 27.84 ? 50 LEU A N 1 ATOM 360 C CA . LEU A 1 50 ? 47.994 4.435 29.585 1.00 30.36 ? 50 LEU A CA 1 ATOM 361 C C . LEU A 1 50 ? 48.232 3.113 30.329 1.00 35.30 ? 50 LEU A C 1 ATOM 362 O O . LEU A 1 50 ? 47.262 2.384 30.640 1.00 27.41 ? 50 LEU A O 1 ATOM 363 C CB . LEU A 1 50 ? 47.179 5.397 30.485 1.00 28.48 ? 50 LEU A CB 1 ATOM 364 C CG . LEU A 1 50 ? 47.215 6.902 30.149 1.00 27.60 ? 50 LEU A CG 1 ATOM 365 C CD1 . LEU A 1 50 ? 45.887 7.547 30.557 1.00 16.93 ? 50 LEU A CD1 1 ATOM 366 C CD2 . LEU A 1 50 ? 48.367 7.620 30.873 1.00 25.26 ? 50 LEU A CD2 1 ATOM 367 N N . ASN A 1 51 ? 49.504 2.796 30.632 1.00 35.17 ? 51 ASN A N 1 ATOM 368 C CA . ASN A 1 51 ? 49.815 1.562 31.392 1.00 40.83 ? 51 ASN A CA 1 ATOM 369 C C . ASN A 1 51 ? 49.856 1.857 32.901 1.00 39.65 ? 51 ASN A C 1 ATOM 370 O O . ASN A 1 51 ? 49.696 3.039 33.305 1.00 19.99 ? 51 ASN A O 1 ATOM 371 C CB . ASN A 1 51 ? 50.991 0.713 30.938 1.00 38.20 ? 51 ASN A CB 1 ATOM 372 C CG . ASN A 1 51 ? 50.751 -0.253 29.788 1.00 69.37 ? 51 ASN A CG 1 ATOM 373 O OD1 . ASN A 1 51 ? 51.224 0.001 28.654 1.00 47.77 ? 51 ASN A OD1 1 ATOM 374 N ND2 . ASN A 1 51 ? 50.197 -1.437 30.096 1.00 33.35 ? 51 ASN A ND2 1 ATOM 375 N N . GLY A 1 52 ? 49.907 0.825 33.770 1.00 30.24 ? 52 GLY A N 1 ATOM 376 C CA . GLY A 1 52 ? 49.855 1.195 35.174 1.00 27.55 ? 52 GLY A CA 1 ATOM 377 C C . GLY A 1 52 ? 51.114 1.300 35.968 1.00 20.90 ? 52 GLY A C 1 ATOM 378 O O . GLY A 1 52 ? 52.017 2.168 35.772 1.00 1.61 ? 52 GLY A O 1 ATOM 379 N N . GLY A 1 53 ? 51.171 0.390 36.921 1.00 12.01 ? 53 GLY A N 1 ATOM 380 C CA . GLY A 1 53 ? 52.327 0.302 37.763 1.00 1.40 ? 53 GLY A CA 1 ATOM 381 C C . GLY A 1 53 ? 52.012 0.073 39.200 1.00 10.39 ? 53 GLY A C 1 ATOM 382 O O . GLY A 1 53 ? 51.785 -1.048 39.666 1.00 7.28 ? 53 GLY A O 1 ATOM 383 N N . PRO A 1 54 ? 52.045 1.185 39.896 1.00 2.59 ? 54 PRO A N 1 ATOM 384 C CA . PRO A 1 54 ? 52.333 2.446 39.244 1.00 1.00 ? 54 PRO A CA 1 ATOM 385 C C . PRO A 1 54 ? 53.778 2.631 38.916 1.00 15.99 ? 54 PRO A C 1 ATOM 386 O O . PRO A 1 54 ? 54.663 2.014 39.507 1.00 23.56 ? 54 PRO A O 1 ATOM 387 C CB . PRO A 1 54 ? 51.970 3.512 40.261 1.00 5.29 ? 54 PRO A CB 1 ATOM 388 C CG . PRO A 1 54 ? 51.538 2.797 41.541 1.00 9.21 ? 54 PRO A CG 1 ATOM 389 C CD . PRO A 1 54 ? 51.597 1.311 41.294 1.00 1.00 ? 54 PRO A CD 1 ATOM 390 N N . GLY A 1 55 ? 54.046 3.505 37.984 1.00 24.89 ? 55 GLY A N 1 ATOM 391 C CA . GLY A 1 55 ? 55.444 3.719 37.634 1.00 20.21 ? 55 GLY A CA 1 ATOM 392 C C . GLY A 1 55 ? 55.959 2.769 36.555 1.00 26.96 ? 55 GLY A C 1 ATOM 393 O O . GLY A 1 55 ? 57.107 2.395 36.570 1.00 20.20 ? 55 GLY A O 1 ATOM 394 N N . CYS A 1 56 ? 55.101 2.396 35.603 1.00 47.41 ? 56 CYS A N 1 ATOM 395 C CA . CYS A 1 56 ? 55.483 1.531 34.474 1.00 54.04 ? 56 CYS A CA 1 ATOM 396 C C . CYS A 1 56 ? 55.395 2.263 33.092 1.00 59.56 ? 56 CYS A C 1 ATOM 397 O O . CYS A 1 56 ? 54.461 3.025 32.846 1.00 61.45 ? 56 CYS A O 1 ATOM 398 C CB . CYS A 1 56 ? 54.740 0.177 34.485 1.00 50.14 ? 56 CYS A CB 1 ATOM 399 S SG . CYS A 1 56 ? 55.145 -0.817 35.936 1.00 46.99 ? 56 CYS A SG 1 ATOM 400 N N . SER A 1 57 ? 56.369 2.048 32.182 1.00 51.30 ? 57 SER A N 1 ATOM 401 C CA . SER A 1 57 ? 56.342 2.710 30.873 1.00 52.45 ? 57 SER A CA 1 ATOM 402 C C . SER A 1 57 ? 55.167 2.250 30.000 1.00 46.43 ? 57 SER A C 1 ATOM 403 O O . SER A 1 57 ? 54.686 1.129 30.165 1.00 45.88 ? 57 SER A O 1 ATOM 404 C CB . SER A 1 57 ? 57.695 2.748 30.178 1.00 55.67 ? 57 SER A CB 1 ATOM 405 O OG . SER A 1 57 ? 57.552 2.837 28.775 1.00 28.62 ? 57 SER A OG 1 ATOM 406 N N . SER A 1 58 ? 54.671 3.127 29.102 1.00 33.46 ? 58 SER A N 1 ATOM 407 C CA . SER A 1 58 ? 53.532 2.776 28.253 1.00 33.37 ? 58 SER A CA 1 ATOM 408 C C . SER A 1 58 ? 53.932 2.060 26.972 1.00 33.05 ? 58 SER A C 1 ATOM 409 O O . SER A 1 58 ? 53.084 1.409 26.346 1.00 22.69 ? 58 SER A O 1 ATOM 410 C CB . SER A 1 58 ? 52.522 3.898 28.043 1.00 27.67 ? 58 SER A CB 1 ATOM 411 O OG . SER A 1 58 ? 52.436 4.687 29.224 1.00 34.76 ? 58 SER A OG 1 ATOM 412 N N . LEU A 1 59 ? 55.250 2.190 26.620 1.00 7.38 ? 59 LEU A N 1 ATOM 413 C CA . LEU A 1 59 ? 55.828 1.568 25.439 1.00 8.22 ? 59 LEU A CA 1 ATOM 414 C C . LEU A 1 59 ? 55.467 0.089 25.451 1.00 28.01 ? 59 LEU A C 1 ATOM 415 O O . LEU A 1 59 ? 55.212 -0.558 24.436 1.00 35.00 ? 59 LEU A O 1 ATOM 416 C CB . LEU A 1 59 ? 57.357 1.849 25.324 1.00 6.04 ? 59 LEU A CB 1 ATOM 417 C CG . LEU A 1 59 ? 57.597 3.363 25.427 1.00 15.66 ? 59 LEU A CG 1 ATOM 418 C CD1 . LEU A 1 59 ? 59.081 3.779 25.520 1.00 4.12 ? 59 LEU A CD1 1 ATOM 419 C CD2 . LEU A 1 59 ? 56.849 4.117 24.304 1.00 26.60 ? 59 LEU A CD2 1 ATOM 420 N N . THR A 1 60 ? 55.419 -0.427 26.652 1.00 15.53 ? 60 THR A N 1 ATOM 421 C CA . THR A 1 60 ? 55.074 -1.793 26.882 1.00 23.24 ? 60 THR A CA 1 ATOM 422 C C . THR A 1 60 ? 53.749 -2.166 26.207 1.00 33.83 ? 60 THR A C 1 ATOM 423 O O . THR A 1 60 ? 53.579 -3.243 25.636 1.00 47.06 ? 60 THR A O 1 ATOM 424 C CB . THR A 1 60 ? 55.015 -2.082 28.391 1.00 46.03 ? 60 THR A CB 1 ATOM 425 O OG1 . THR A 1 60 ? 56.112 -1.460 29.049 1.00 45.80 ? 60 THR A OG1 1 ATOM 426 C CG2 . THR A 1 60 ? 55.052 -3.591 28.588 1.00 3.65 ? 60 THR A CG2 1 ATOM 427 N N . GLY A 1 61 ? 52.769 -1.311 26.266 1.00 18.11 ? 61 GLY A N 1 ATOM 428 C CA . GLY A 1 61 ? 51.559 -1.727 25.592 1.00 20.91 ? 61 GLY A CA 1 ATOM 429 C C . GLY A 1 61 ? 51.829 -1.698 24.093 1.00 28.63 ? 61 GLY A C 1 ATOM 430 O O . GLY A 1 61 ? 51.343 -2.536 23.325 1.00 21.23 ? 61 GLY A O 1 ATOM 431 N N . LEU A 1 62 ? 52.639 -0.704 23.705 1.00 23.79 ? 62 LEU A N 1 ATOM 432 C CA . LEU A 1 62 ? 53.020 -0.533 22.330 1.00 24.23 ? 62 LEU A CA 1 ATOM 433 C C . LEU A 1 62 ? 53.591 -1.858 21.811 1.00 39.19 ? 62 LEU A C 1 ATOM 434 O O . LEU A 1 62 ? 52.968 -2.568 21.034 1.00 37.34 ? 62 LEU A O 1 ATOM 435 C CB . LEU A 1 62 ? 54.039 0.627 22.203 1.00 21.24 ? 62 LEU A CB 1 ATOM 436 C CG . LEU A 1 62 ? 54.377 1.160 20.795 1.00 18.64 ? 62 LEU A CG 1 ATOM 437 C CD1 . LEU A 1 62 ? 55.775 1.767 20.763 1.00 8.04 ? 62 LEU A CD1 1 ATOM 438 C CD2 . LEU A 1 62 ? 54.355 0.095 19.729 1.00 27.15 ? 62 LEU A CD2 1 ATOM 439 N N . PHE A 1 63 ? 54.798 -2.192 22.221 1.00 32.31 ? 63 PHE A N 1 ATOM 440 C CA . PHE A 1 63 ? 55.376 -3.413 21.730 1.00 23.68 ? 63 PHE A CA 1 ATOM 441 C C . PHE A 1 63 ? 54.919 -4.641 22.442 1.00 36.26 ? 63 PHE A C 1 ATOM 442 O O . PHE A 1 63 ? 55.682 -5.589 22.515 1.00 53.89 ? 63 PHE A O 1 ATOM 443 C CB . PHE A 1 63 ? 56.878 -3.401 21.948 1.00 14.87 ? 63 PHE A CB 1 ATOM 444 C CG . PHE A 1 63 ? 57.560 -2.203 21.386 1.00 21.98 ? 63 PHE A CG 1 ATOM 445 C CD1 . PHE A 1 63 ? 58.003 -2.180 20.060 1.00 27.42 ? 63 PHE A CD1 1 ATOM 446 C CD2 . PHE A 1 63 ? 57.800 -1.102 22.208 1.00 30.79 ? 63 PHE A CD2 1 ATOM 447 C CE1 . PHE A 1 63 ? 58.674 -1.060 19.564 1.00 30.43 ? 63 PHE A CE1 1 ATOM 448 C CE2 . PHE A 1 63 ? 58.485 0.017 21.732 1.00 30.84 ? 63 PHE A CE2 1 ATOM 449 C CZ . PHE A 1 63 ? 58.915 0.029 20.406 1.00 32.24 ? 63 PHE A CZ 1 ATOM 450 N N . PHE A 1 64 ? 53.736 -4.701 22.996 1.00 14.38 ? 64 PHE A N 1 ATOM 451 C CA . PHE A 1 64 ? 53.517 -5.948 23.656 1.00 11.35 ? 64 PHE A CA 1 ATOM 452 C C . PHE A 1 64 ? 52.107 -6.440 23.691 1.00 30.25 ? 64 PHE A C 1 ATOM 453 O O . PHE A 1 64 ? 51.846 -7.654 23.901 1.00 27.52 ? 64 PHE A O 1 ATOM 454 C CB . PHE A 1 64 ? 54.114 -5.925 25.073 1.00 15.61 ? 64 PHE A CB 1 ATOM 455 C CG . PHE A 1 64 ? 54.007 -7.265 25.727 1.00 20.31 ? 64 PHE A CG 1 ATOM 456 C CD1 . PHE A 1 64 ? 54.917 -8.256 25.368 1.00 33.95 ? 64 PHE A CD1 1 ATOM 457 C CD2 . PHE A 1 64 ? 53.012 -7.565 26.661 1.00 17.48 ? 64 PHE A CD2 1 ATOM 458 C CE1 . PHE A 1 64 ? 54.844 -9.530 25.927 1.00 36.01 ? 64 PHE A CE1 1 ATOM 459 C CE2 . PHE A 1 64 ? 52.919 -8.836 27.227 1.00 12.08 ? 64 PHE A CE2 1 ATOM 460 C CZ . PHE A 1 64 ? 53.848 -9.812 26.861 1.00 22.61 ? 64 PHE A CZ 1 ATOM 461 N N . GLU A 1 65 ? 51.196 -5.512 23.497 1.00 41.43 ? 65 GLU A N 1 ATOM 462 C CA . GLU A 1 65 ? 49.817 -5.916 23.554 1.00 45.64 ? 65 GLU A CA 1 ATOM 463 C C . GLU A 1 65 ? 48.886 -5.390 22.480 1.00 28.47 ? 65 GLU A C 1 ATOM 464 O O . GLU A 1 65 ? 47.970 -6.079 22.069 1.00 20.29 ? 65 GLU A O 1 ATOM 465 C CB . GLU A 1 65 ? 49.290 -5.478 24.929 1.00 47.14 ? 65 GLU A CB 1 ATOM 466 C CG . GLU A 1 65 ? 50.249 -4.485 25.637 1.00 41.64 ? 65 GLU A CG 1 ATOM 467 C CD . GLU A 1 65 ? 49.707 -4.157 27.000 1.00 93.82 ? 65 GLU A CD 1 ATOM 468 O OE1 . GLU A 1 65 ? 48.670 -4.712 27.375 1.00 11.18 ? 65 GLU A OE1 1 ATOM 469 O OE2 . GLU A 1 65 ? 50.367 -3.181 27.669 1.00 14.86 ? 65 GLU A OE2 1 ATOM 470 N N . LEU A 1 66 ? 49.117 -4.174 22.060 1.00 22.46 ? 66 LEU A N 1 ATOM 471 C CA . LEU A 1 66 ? 48.251 -3.536 21.098 1.00 26.51 ? 66 LEU A CA 1 ATOM 472 C C . LEU A 1 66 ? 48.910 -2.504 20.189 1.00 32.52 ? 66 LEU A C 1 ATOM 473 O O . LEU A 1 66 ? 48.214 -1.775 19.473 1.00 14.77 ? 66 LEU A O 1 ATOM 474 C CB . LEU A 1 66 ? 47.135 -2.811 21.873 1.00 22.20 ? 66 LEU A CB 1 ATOM 475 C CG . LEU A 1 66 ? 47.688 -1.855 22.917 1.00 15.76 ? 66 LEU A CG 1 ATOM 476 C CD1 . LEU A 1 66 ? 47.859 -0.470 22.309 1.00 3.01 ? 66 LEU A CD1 1 ATOM 477 C CD2 . LEU A 1 66 ? 46.713 -1.798 24.076 1.00 17.67 ? 66 LEU A CD2 1 ATOM 478 N N . GLY A 1 67 ? 50.231 -2.410 20.198 1.00 38.50 ? 67 GLY A N 1 ATOM 479 C CA . GLY A 1 67 ? 50.865 -1.451 19.310 1.00 37.39 ? 67 GLY A CA 1 ATOM 480 C C . GLY A 1 67 ? 51.016 -2.068 17.901 1.00 42.60 ? 67 GLY A C 1 ATOM 481 O O . GLY A 1 67 ? 50.482 -3.146 17.580 1.00 33.68 ? 67 GLY A O 1 ATOM 482 N N . PRO A 1 68 ? 51.762 -1.379 17.051 1.00 47.00 ? 68 PRO A N 1 ATOM 483 C CA . PRO A 1 68 ? 52.024 -1.849 15.704 1.00 44.64 ? 68 PRO A CA 1 ATOM 484 C C . PRO A 1 68 ? 53.206 -2.849 15.671 1.00 63.93 ? 68 PRO A C 1 ATOM 485 O O . PRO A 1 68 ? 53.190 -3.917 15.045 1.00 59.71 ? 68 PRO A O 1 ATOM 486 C CB . PRO A 1 68 ? 52.348 -0.580 14.907 1.00 40.29 ? 68 PRO A CB 1 ATOM 487 C CG . PRO A 1 68 ? 51.881 0.626 15.717 1.00 49.32 ? 68 PRO A CG 1 ATOM 488 C CD . PRO A 1 68 ? 51.489 0.091 17.084 1.00 51.59 ? 68 PRO A CD 1 ATOM 489 N N . SER A 1 69 ? 54.248 -2.475 16.390 1.00 74.08 ? 69 SER A N 1 ATOM 490 C CA . SER A 1 69 ? 55.447 -3.279 16.493 1.00 76.85 ? 69 SER A CA 1 ATOM 491 C C . SER A 1 69 ? 55.515 -4.256 17.667 1.00 59.52 ? 69 SER A C 1 ATOM 492 O O . SER A 1 69 ? 54.864 -4.157 18.711 1.00 58.71 ? 69 SER A O 1 ATOM 493 C CB . SER A 1 69 ? 56.690 -2.414 16.414 1.00 81.87 ? 69 SER A CB 1 ATOM 494 N N . SER A 1 70 ? 56.347 -5.243 17.461 1.00 50.99 ? 70 SER A N 1 ATOM 495 C CA . SER A 1 70 ? 56.557 -6.285 18.425 1.00 45.50 ? 70 SER A CA 1 ATOM 496 C C . SER A 1 70 ? 58.012 -6.601 18.511 1.00 34.95 ? 70 SER A C 1 ATOM 497 O O . SER A 1 70 ? 58.745 -6.221 17.598 1.00 33.19 ? 70 SER A O 1 ATOM 498 C CB . SER A 1 70 ? 55.746 -7.494 18.057 1.00 33.10 ? 70 SER A CB 1 ATOM 499 O OG . SER A 1 70 ? 54.694 -7.060 17.224 1.00 51.88 ? 70 SER A OG 1 ATOM 500 N N . ILE A 1 71 ? 58.374 -7.262 19.630 1.00 30.62 ? 71 ILE A N 1 ATOM 501 C CA . ILE A 1 71 ? 59.733 -7.705 19.997 1.00 34.19 ? 71 ILE A CA 1 ATOM 502 C C . ILE A 1 71 ? 60.148 -9.188 19.860 1.00 62.41 ? 71 ILE A C 1 ATOM 503 O O . ILE A 1 71 ? 59.682 -10.067 20.604 1.00 58.97 ? 71 ILE A O 1 ATOM 504 C CB . ILE A 1 71 ? 60.732 -6.635 20.448 1.00 25.49 ? 71 ILE A CB 1 ATOM 505 C CG1 . ILE A 1 71 ? 60.552 -5.419 19.558 1.00 10.88 ? 71 ILE A CG1 1 ATOM 506 C CG2 . ILE A 1 71 ? 62.206 -7.057 20.500 1.00 20.13 ? 71 ILE A CG2 1 ATOM 507 C CD1 . ILE A 1 71 ? 61.168 -4.210 20.174 1.00 10.09 ? 71 ILE A CD1 1 ATOM 508 N N . GLY A 1 72 ? 61.018 -9.450 18.873 1.00 67.94 ? 72 GLY A N 1 ATOM 509 C CA . GLY A 1 72 ? 61.532 -10.781 18.616 1.00 70.95 ? 72 GLY A CA 1 ATOM 510 C C . GLY A 1 72 ? 62.947 -10.850 19.196 1.00 68.72 ? 72 GLY A C 1 ATOM 511 O O . GLY A 1 72 ? 63.568 -9.789 19.373 1.00 70.25 ? 72 GLY A O 1 ATOM 512 N N . PRO A 1 73 ? 63.419 -12.080 19.502 1.00 48.27 ? 73 PRO A N 1 ATOM 513 C CA . PRO A 1 73 ? 64.737 -12.339 20.059 1.00 49.94 ? 73 PRO A CA 1 ATOM 514 C C . PRO A 1 73 ? 65.746 -11.509 19.344 1.00 61.34 ? 73 PRO A C 1 ATOM 515 O O . PRO A 1 73 ? 66.697 -10.970 19.921 1.00 64.06 ? 73 PRO A O 1 ATOM 516 C CB . PRO A 1 73 ? 65.058 -13.820 19.779 1.00 52.79 ? 73 PRO A CB 1 ATOM 517 C CG . PRO A 1 73 ? 63.798 -14.453 19.206 1.00 64.73 ? 73 PRO A CG 1 ATOM 518 C CD . PRO A 1 73 ? 62.788 -13.326 18.975 1.00 57.13 ? 73 PRO A CD 1 ATOM 519 N N . ASP A 1 74 ? 65.444 -11.419 18.065 1.00 60.11 ? 74 ASP A N 1 ATOM 520 C CA . ASP A 1 74 ? 66.214 -10.681 17.120 1.00 65.85 ? 74 ASP A CA 1 ATOM 521 C C . ASP A 1 74 ? 66.310 -9.186 17.461 1.00 65.19 ? 74 ASP A C 1 ATOM 522 O O . ASP A 1 74 ? 67.185 -8.469 16.955 1.00 69.97 ? 74 ASP A O 1 ATOM 523 C CB . ASP A 1 74 ? 65.746 -10.979 15.662 1.00 74.91 ? 74 ASP A CB 1 ATOM 524 C CG . ASP A 1 74 ? 64.255 -10.991 15.378 1.00 87.36 ? 74 ASP A CG 1 ATOM 525 O OD1 . ASP A 1 74 ? 63.380 -11.209 16.224 1.00 100.00 ? 74 ASP A OD1 1 ATOM 526 O OD2 . ASP A 1 74 ? 64.018 -10.778 14.089 1.00 57.00 ? 74 ASP A OD2 1 ATOM 527 N N . LEU A 1 75 ? 65.430 -8.699 18.341 1.00 59.95 ? 75 LEU A N 1 ATOM 528 C CA . LEU A 1 75 ? 65.440 -7.277 18.699 1.00 60.99 ? 75 LEU A CA 1 ATOM 529 C C . LEU A 1 75 ? 65.205 -6.523 17.440 1.00 55.31 ? 75 LEU A C 1 ATOM 530 O O . LEU A 1 75 ? 65.806 -5.478 17.205 1.00 47.98 ? 75 LEU A O 1 ATOM 531 C CB . LEU A 1 75 ? 66.705 -6.757 19.399 1.00 61.47 ? 75 LEU A CB 1 ATOM 532 C CG . LEU A 1 75 ? 66.632 -6.981 20.900 1.00 66.32 ? 75 LEU A CG 1 ATOM 533 C CD1 . LEU A 1 75 ? 65.354 -7.749 21.212 1.00 67.42 ? 75 LEU A CD1 1 ATOM 534 C CD2 . LEU A 1 75 ? 67.839 -7.795 21.369 1.00 82.58 ? 75 LEU A CD2 1 ATOM 535 N N . LYS A 1 76 ? 64.336 -7.177 16.658 1.00 53.44 ? 76 LYS A N 1 ATOM 536 C CA . LYS A 1 76 ? 63.872 -6.745 15.366 1.00 54.48 ? 76 LYS A CA 1 ATOM 537 C C . LYS A 1 76 ? 62.359 -6.557 15.399 1.00 47.69 ? 76 LYS A C 1 ATOM 538 O O . LYS A 1 76 ? 61.568 -7.400 15.873 1.00 26.02 ? 76 LYS A O 1 ATOM 539 C CB . LYS A 1 76 ? 64.335 -7.644 14.211 1.00 57.63 ? 76 LYS A CB 1 ATOM 540 C CG . LYS A 1 76 ? 65.849 -7.636 13.984 1.00 86.89 ? 76 LYS A CG 1 ATOM 541 C CD . LYS A 1 76 ? 66.382 -6.427 13.209 1.00 100.00 ? 76 LYS A CD 1 ATOM 542 C CE . LYS A 1 76 ? 67.868 -6.156 13.468 1.00 100.00 ? 76 LYS A CE 1 ATOM 543 N NZ . LYS A 1 76 ? 68.499 -5.263 12.463 1.00 100.00 ? 76 LYS A NZ 1 ATOM 544 N N . PRO A 1 77 ? 61.976 -5.400 14.893 1.00 48.12 ? 77 PRO A N 1 ATOM 545 C CA . PRO A 1 77 ? 60.584 -5.051 14.857 1.00 38.41 ? 77 PRO A CA 1 ATOM 546 C C . PRO A 1 77 ? 59.732 -6.095 14.216 1.00 40.49 ? 77 PRO A C 1 ATOM 547 O O . PRO A 1 77 ? 60.221 -6.964 13.518 1.00 47.71 ? 77 PRO A O 1 ATOM 548 C CB . PRO A 1 77 ? 60.497 -3.712 14.142 1.00 32.86 ? 77 PRO A CB 1 ATOM 549 C CG . PRO A 1 77 ? 61.908 -3.094 14.244 1.00 49.57 ? 77 PRO A CG 1 ATOM 550 C CD . PRO A 1 77 ? 62.845 -4.179 14.760 1.00 46.88 ? 77 PRO A CD 1 ATOM 551 N N . ILE A 1 78 ? 58.454 -5.984 14.492 1.00 40.14 ? 78 ILE A N 1 ATOM 552 C CA . ILE A 1 78 ? 57.432 -6.874 13.962 1.00 44.46 ? 78 ILE A CA 1 ATOM 553 C C . ILE A 1 78 ? 56.085 -6.136 13.731 1.00 71.36 ? 78 ILE A C 1 ATOM 554 O O . ILE A 1 78 ? 55.696 -5.208 14.460 1.00 86.25 ? 78 ILE A O 1 ATOM 555 C CB . ILE A 1 78 ? 57.301 -8.188 14.734 1.00 36.22 ? 78 ILE A CB 1 ATOM 556 C CG1 . ILE A 1 78 ? 58.469 -9.094 14.340 1.00 28.38 ? 78 ILE A CG1 1 ATOM 557 C CG2 . ILE A 1 78 ? 55.947 -8.843 14.412 1.00 26.42 ? 78 ILE A CG2 1 ATOM 558 C CD1 . ILE A 1 78 ? 59.365 -9.549 15.494 1.00 57.02 ? 78 ILE A CD1 1 ATOM 559 N N . GLY A 1 79 ? 55.359 -6.524 12.693 1.00 53.08 ? 79 GLY A N 1 ATOM 560 C CA . GLY A 1 79 ? 54.108 -5.852 12.428 1.00 52.55 ? 79 GLY A CA 1 ATOM 561 C C . GLY A 1 79 ? 52.941 -6.491 13.138 1.00 52.98 ? 79 GLY A C 1 ATOM 562 O O . GLY A 1 79 ? 52.818 -7.716 13.203 1.00 47.75 ? 79 GLY A O 1 ATOM 563 N N . ASN A 1 80 ? 52.067 -5.671 13.690 1.00 50.49 ? 80 ASN A N 1 ATOM 564 C CA . ASN A 1 80 ? 50.964 -6.312 14.343 1.00 55.51 ? 80 ASN A CA 1 ATOM 565 C C . ASN A 1 80 ? 49.822 -6.578 13.381 1.00 61.56 ? 80 ASN A C 1 ATOM 566 O O . ASN A 1 80 ? 49.382 -5.676 12.656 1.00 45.98 ? 80 ASN A O 1 ATOM 567 C CB . ASN A 1 80 ? 50.691 -5.959 15.838 1.00 46.20 ? 80 ASN A CB 1 ATOM 568 C CG . ASN A 1 80 ? 49.387 -6.487 16.445 1.00 72.10 ? 80 ASN A CG 1 ATOM 569 O OD1 . ASN A 1 80 ? 49.061 -7.723 16.511 1.00 18.02 ? 80 ASN A OD1 1 ATOM 570 N ND2 . ASN A 1 80 ? 48.673 -5.513 16.993 1.00 24.92 ? 80 ASN A ND2 1 ATOM 571 N N . PRO A 1 81 ? 49.390 -7.848 13.357 1.00 83.23 ? 81 PRO A N 1 ATOM 572 C CA . PRO A 1 81 ? 48.312 -8.305 12.468 1.00 88.94 ? 81 PRO A CA 1 ATOM 573 C C . PRO A 1 81 ? 46.904 -7.849 12.874 1.00 79.10 ? 81 PRO A C 1 ATOM 574 O O . PRO A 1 81 ? 45.904 -8.165 12.206 1.00 77.10 ? 81 PRO A O 1 ATOM 575 C CB . PRO A 1 81 ? 48.401 -9.850 12.453 1.00 94.93 ? 81 PRO A CB 1 ATOM 576 C CG . PRO A 1 81 ? 49.567 -10.268 13.365 1.00 100.00 ? 81 PRO A CG 1 ATOM 577 C CD . PRO A 1 81 ? 50.176 -8.990 13.940 1.00 90.42 ? 81 PRO A CD 1 ATOM 578 N N . TYR A 1 82 ? 46.850 -7.106 13.985 1.00 57.98 ? 82 TYR A N 1 ATOM 579 C CA . TYR A 1 82 ? 45.624 -6.603 14.545 1.00 45.47 ? 82 TYR A CA 1 ATOM 580 C C . TYR A 1 82 ? 45.867 -5.358 15.372 1.00 43.20 ? 82 TYR A C 1 ATOM 581 O O . TYR A 1 82 ? 45.139 -5.215 16.378 1.00 31.48 ? 82 TYR A O 1 ATOM 582 C CB . TYR A 1 82 ? 44.889 -7.651 15.440 1.00 40.10 ? 82 TYR A CB 1 ATOM 583 C CG . TYR A 1 82 ? 44.553 -8.947 14.734 1.00 46.47 ? 82 TYR A CG 1 ATOM 584 C CD1 . TYR A 1 82 ? 45.455 -10.012 14.731 1.00 60.35 ? 82 TYR A CD1 1 ATOM 585 C CD2 . TYR A 1 82 ? 43.344 -9.126 14.064 1.00 49.06 ? 82 TYR A CD2 1 ATOM 586 C CE1 . TYR A 1 82 ? 45.186 -11.219 14.083 1.00 68.02 ? 82 TYR A CE1 1 ATOM 587 C CE2 . TYR A 1 82 ? 43.054 -10.323 13.404 1.00 59.95 ? 82 TYR A CE2 1 ATOM 588 C CZ . TYR A 1 82 ? 43.975 -11.373 13.417 1.00 84.37 ? 82 TYR A CZ 1 ATOM 589 O OH . TYR A 1 82 ? 43.723 -12.562 12.789 1.00 100.00 ? 82 TYR A OH 1 ATOM 590 N N . SER A 1 83 ? 46.866 -4.490 14.955 1.00 35.74 ? 83 SER A N 1 ATOM 591 C CA . SER A 1 83 ? 47.203 -3.224 15.692 1.00 33.29 ? 83 SER A CA 1 ATOM 592 C C . SER A 1 83 ? 46.027 -2.319 16.077 1.00 53.37 ? 83 SER A C 1 ATOM 593 O O . SER A 1 83 ? 44.918 -2.382 15.550 1.00 59.55 ? 83 SER A O 1 ATOM 594 C CB . SER A 1 83 ? 48.573 -2.526 15.460 1.00 29.03 ? 83 SER A CB 1 ATOM 595 O OG . SER A 1 83 ? 48.576 -1.095 15.656 1.00 25.41 ? 83 SER A OG 1 ATOM 596 N N . TRP A 1 84 ? 46.274 -1.459 17.035 1.00 52.79 ? 84 TRP A N 1 ATOM 597 C CA . TRP A 1 84 ? 45.229 -0.592 17.540 1.00 47.03 ? 84 TRP A CA 1 ATOM 598 C C . TRP A 1 84 ? 44.904 0.623 16.716 1.00 54.66 ? 84 TRP A C 1 ATOM 599 O O . TRP A 1 84 ? 43.752 1.070 16.642 1.00 44.68 ? 84 TRP A O 1 ATOM 600 C CB . TRP A 1 84 ? 45.431 -0.310 19.062 1.00 39.19 ? 84 TRP A CB 1 ATOM 601 C CG . TRP A 1 84 ? 44.555 -1.239 19.868 1.00 31.60 ? 84 TRP A CG 1 ATOM 602 C CD1 . TRP A 1 84 ? 44.105 -2.473 19.473 1.00 32.27 ? 84 TRP A CD1 1 ATOM 603 C CD2 . TRP A 1 84 ? 43.982 -1.007 21.145 1.00 27.69 ? 84 TRP A CD2 1 ATOM 604 N NE1 . TRP A 1 84 ? 43.291 -3.030 20.411 1.00 29.15 ? 84 TRP A NE1 1 ATOM 605 C CE2 . TRP A 1 84 ? 43.181 -2.149 21.461 1.00 32.57 ? 84 TRP A CE2 1 ATOM 606 C CE3 . TRP A 1 84 ? 44.023 0.052 22.032 1.00 22.27 ? 84 TRP A CE3 1 ATOM 607 C CZ2 . TRP A 1 84 ? 42.455 -2.260 22.669 1.00 25.75 ? 84 TRP A CZ2 1 ATOM 608 C CZ3 . TRP A 1 84 ? 43.267 -0.075 23.192 1.00 16.92 ? 84 TRP A CZ3 1 ATOM 609 C CH2 . TRP A 1 84 ? 42.484 -1.199 23.519 1.00 8.83 ? 84 TRP A CH2 1 ATOM 610 N N . ASN A 1 85 ? 45.955 1.140 16.115 1.00 68.33 ? 85 ASN A N 1 ATOM 611 C CA . ASN A 1 85 ? 45.886 2.314 15.287 1.00 64.63 ? 85 ASN A CA 1 ATOM 612 C C . ASN A 1 85 ? 45.468 1.953 13.859 1.00 47.87 ? 85 ASN A C 1 ATOM 613 O O . ASN A 1 85 ? 45.507 2.783 12.967 1.00 41.23 ? 85 ASN A O 1 ATOM 614 C CB . ASN A 1 85 ? 47.237 3.042 15.353 1.00 60.33 ? 85 ASN A CB 1 ATOM 615 C CG . ASN A 1 85 ? 48.240 2.300 14.496 1.00 85.14 ? 85 ASN A CG 1 ATOM 616 O OD1 . ASN A 1 85 ? 48.574 1.116 14.774 1.00 63.13 ? 85 ASN A OD1 1 ATOM 617 N ND2 . ASN A 1 85 ? 48.513 2.902 13.335 1.00 30.20 ? 85 ASN A ND2 1 ATOM 618 N N . SER A 1 86 ? 45.062 0.701 13.669 1.00 43.15 ? 86 SER A N 1 ATOM 619 C CA . SER A 1 86 ? 44.596 0.228 12.382 1.00 52.09 ? 86 SER A CA 1 ATOM 620 C C . SER A 1 86 ? 43.562 1.198 11.790 1.00 73.79 ? 86 SER A C 1 ATOM 621 O O . SER A 1 86 ? 43.509 1.437 10.583 1.00 83.75 ? 86 SER A O 1 ATOM 622 C CB . SER A 1 86 ? 43.958 -1.139 12.543 1.00 51.77 ? 86 SER A CB 1 ATOM 623 N N . ASN A 1 87 ? 42.772 1.793 12.685 1.00 64.50 ? 87 ASN A N 1 ATOM 624 C CA . ASN A 1 87 ? 41.727 2.749 12.342 1.00 50.31 ? 87 ASN A CA 1 ATOM 625 C C . ASN A 1 87 ? 41.681 3.949 13.321 1.00 41.27 ? 87 ASN A C 1 ATOM 626 O O . ASN A 1 87 ? 40.563 4.366 13.688 1.00 23.61 ? 87 ASN A O 1 ATOM 627 C CB . ASN A 1 87 ? 40.356 2.000 12.299 1.00 15.23 ? 87 ASN A CB 1 ATOM 628 C CG . ASN A 1 87 ? 39.637 2.026 10.939 1.00 100.00 ? 87 ASN A CG 1 ATOM 629 O OD1 . ASN A 1 87 ? 39.054 3.057 10.540 1.00 100.00 ? 87 ASN A OD1 1 ATOM 630 N ND2 . ASN A 1 87 ? 39.566 0.861 10.263 1.00 100.00 ? 87 ASN A ND2 1 ATOM 631 N N . ALA A 1 88 ? 42.882 4.496 13.738 1.00 32.97 ? 88 ALA A N 1 ATOM 632 C CA . ALA A 1 88 ? 42.944 5.629 14.669 1.00 30.09 ? 88 ALA A CA 1 ATOM 633 C C . ALA A 1 88 ? 44.352 6.069 15.087 1.00 29.94 ? 88 ALA A C 1 ATOM 634 O O . ALA A 1 88 ? 45.185 5.220 15.410 1.00 24.04 ? 88 ALA A O 1 ATOM 635 C CB . ALA A 1 88 ? 42.178 5.224 15.933 1.00 27.07 ? 88 ALA A CB 1 ATOM 636 N N . THR A 1 89 ? 44.597 7.393 15.129 1.00 27.53 ? 89 THR A N 1 ATOM 637 C CA . THR A 1 89 ? 45.898 7.910 15.570 1.00 38.88 ? 89 THR A CA 1 ATOM 638 C C . THR A 1 89 ? 46.106 7.770 17.106 1.00 53.55 ? 89 THR A C 1 ATOM 639 O O . THR A 1 89 ? 45.424 8.429 17.899 1.00 46.20 ? 89 THR A O 1 ATOM 640 C CB . THR A 1 89 ? 46.238 9.354 15.091 1.00 50.13 ? 89 THR A CB 1 ATOM 641 O OG1 . THR A 1 89 ? 47.522 9.708 15.591 1.00 43.27 ? 89 THR A OG1 1 ATOM 642 C CG2 . THR A 1 89 ? 45.266 10.358 15.668 1.00 17.22 ? 89 THR A CG2 1 ATOM 643 N N . VAL A 1 90 ? 47.072 6.917 17.536 1.00 57.71 ? 90 VAL A N 1 ATOM 644 C CA . VAL A 1 90 ? 47.358 6.682 18.971 1.00 52.47 ? 90 VAL A CA 1 ATOM 645 C C . VAL A 1 90 ? 48.586 7.397 19.569 1.00 56.15 ? 90 VAL A C 1 ATOM 646 O O . VAL A 1 90 ? 49.571 7.584 18.871 1.00 48.17 ? 90 VAL A O 1 ATOM 647 C CB . VAL A 1 90 ? 47.407 5.184 19.292 1.00 45.39 ? 90 VAL A CB 1 ATOM 648 N N . ILE A 1 91 ? 48.490 7.771 20.883 1.00 58.74 ? 91 ILE A N 1 ATOM 649 C CA . ILE A 1 91 ? 49.556 8.439 21.668 1.00 62.77 ? 91 ILE A CA 1 ATOM 650 C C . ILE A 1 91 ? 50.063 7.536 22.794 1.00 64.38 ? 91 ILE A C 1 ATOM 651 O O . ILE A 1 91 ? 49.242 7.056 23.574 1.00 60.14 ? 91 ILE A O 1 ATOM 652 C CB . ILE A 1 91 ? 49.148 9.760 22.305 1.00 68.78 ? 91 ILE A CB 1 ATOM 653 C CG1 . ILE A 1 91 ? 48.325 10.616 21.345 1.00 64.86 ? 91 ILE A CG1 1 ATOM 654 C CG2 . ILE A 1 91 ? 50.426 10.477 22.744 1.00 73.13 ? 91 ILE A CG2 1 ATOM 655 C CD1 . ILE A 1 91 ? 47.460 11.649 22.054 1.00 58.15 ? 91 ILE A CD1 1 ATOM 656 N N . PHE A 1 92 ? 51.399 7.319 22.877 1.00 64.11 ? 92 PHE A N 1 ATOM 657 C CA . PHE A 1 92 ? 52.043 6.445 23.887 1.00 61.44 ? 92 PHE A CA 1 ATOM 658 C C . PHE A 1 92 ? 52.881 7.193 24.921 1.00 46.18 ? 92 PHE A C 1 ATOM 659 O O . PHE A 1 92 ? 54.088 7.102 24.912 1.00 51.06 ? 92 PHE A O 1 ATOM 660 C CB . PHE A 1 92 ? 52.890 5.289 23.258 1.00 62.89 ? 92 PHE A CB 1 ATOM 661 C CG . PHE A 1 92 ? 52.090 4.104 22.694 1.00 65.92 ? 92 PHE A CG 1 ATOM 662 C CD1 . PHE A 1 92 ? 51.654 3.055 23.509 1.00 62.50 ? 92 PHE A CD1 1 ATOM 663 C CD2 . PHE A 1 92 ? 51.780 4.019 21.334 1.00 63.03 ? 92 PHE A CD2 1 ATOM 664 C CE1 . PHE A 1 92 ? 50.925 1.973 23.005 1.00 52.82 ? 92 PHE A CE1 1 ATOM 665 C CE2 . PHE A 1 92 ? 51.063 2.943 20.806 1.00 54.66 ? 92 PHE A CE2 1 ATOM 666 C CZ . PHE A 1 92 ? 50.627 1.918 21.646 1.00 46.33 ? 92 PHE A CZ 1 ATOM 667 N N . LEU A 1 93 ? 52.212 7.910 25.816 1.00 28.28 ? 93 LEU A N 1 ATOM 668 C CA . LEU A 1 93 ? 52.813 8.704 26.871 1.00 14.61 ? 93 LEU A CA 1 ATOM 669 C C . LEU A 1 93 ? 53.454 7.888 28.000 1.00 32.54 ? 93 LEU A C 1 ATOM 670 O O . LEU A 1 93 ? 52.953 6.817 28.374 1.00 29.40 ? 93 LEU A O 1 ATOM 671 C CB . LEU A 1 93 ? 51.822 9.729 27.413 1.00 10.29 ? 93 LEU A CB 1 ATOM 672 C CG . LEU A 1 93 ? 52.420 10.488 28.590 1.00 17.22 ? 93 LEU A CG 1 ATOM 673 C CD1 . LEU A 1 93 ? 53.752 11.078 28.151 1.00 10.35 ? 93 LEU A CD1 1 ATOM 674 C CD2 . LEU A 1 93 ? 51.480 11.588 29.097 1.00 1.00 ? 93 LEU A CD2 1 ATOM 675 N N . ASP A 1 94 ? 54.577 8.436 28.526 1.00 28.57 ? 94 ASP A N 1 ATOM 676 C CA . ASP A 1 94 ? 55.397 7.867 29.584 1.00 24.83 ? 94 ASP A CA 1 ATOM 677 C C . ASP A 1 94 ? 55.338 8.632 30.858 1.00 34.02 ? 94 ASP A C 1 ATOM 678 O O . ASP A 1 94 ? 56.232 9.429 31.253 1.00 39.05 ? 94 ASP A O 1 ATOM 679 C CB . ASP A 1 94 ? 56.874 7.712 29.206 1.00 30.62 ? 94 ASP A CB 1 ATOM 680 C CG . ASP A 1 94 ? 57.247 6.280 29.015 1.00 33.24 ? 94 ASP A CG 1 ATOM 681 O OD1 . ASP A 1 94 ? 56.422 5.373 29.020 1.00 36.89 ? 94 ASP A OD1 1 ATOM 682 O OD2 . ASP A 1 94 ? 58.552 6.106 29.015 1.00 25.79 ? 94 ASP A OD2 1 ATOM 683 N N . GLN A 1 95 ? 54.250 8.319 31.480 1.00 26.22 ? 95 GLN A N 1 ATOM 684 C CA . GLN A 1 95 ? 53.898 8.860 32.748 1.00 28.45 ? 95 GLN A CA 1 ATOM 685 C C . GLN A 1 95 ? 53.826 7.694 33.714 1.00 39.57 ? 95 GLN A C 1 ATOM 686 O O . GLN A 1 95 ? 53.530 6.527 33.337 1.00 49.11 ? 95 GLN A O 1 ATOM 687 C CB . GLN A 1 95 ? 52.572 9.635 32.673 1.00 24.91 ? 95 GLN A CB 1 ATOM 688 C CG . GLN A 1 95 ? 51.796 9.674 34.010 1.00 32.02 ? 95 GLN A CG 1 ATOM 689 C CD . GLN A 1 95 ? 50.509 8.861 34.056 1.00 68.39 ? 95 GLN A CD 1 ATOM 690 O OE1 . GLN A 1 95 ? 49.594 9.229 34.807 1.00 35.43 ? 95 GLN A OE1 1 ATOM 691 N NE2 . GLN A 1 95 ? 50.404 7.780 33.241 1.00 31.93 ? 95 GLN A NE2 1 ATOM 692 N N . PRO A 1 96 ? 54.115 8.017 34.949 1.00 15.06 ? 96 PRO A N 1 ATOM 693 C CA . PRO A 1 96 ? 54.416 9.364 35.367 1.00 17.46 ? 96 PRO A CA 1 ATOM 694 C C . PRO A 1 96 ? 55.825 9.822 35.071 1.00 24.11 ? 96 PRO A C 1 ATOM 695 O O . PRO A 1 96 ? 56.529 9.258 34.230 1.00 28.51 ? 96 PRO A O 1 ATOM 696 C CB . PRO A 1 96 ? 54.024 9.509 36.833 1.00 24.28 ? 96 PRO A CB 1 ATOM 697 C CG . PRO A 1 96 ? 53.459 8.140 37.238 1.00 35.56 ? 96 PRO A CG 1 ATOM 698 C CD . PRO A 1 96 ? 53.490 7.215 36.012 1.00 30.91 ? 96 PRO A CD 1 ATOM 699 N N . VAL A 1 97 ? 56.223 10.907 35.742 1.00 22.88 ? 97 VAL A N 1 ATOM 700 C CA . VAL A 1 97 ? 57.549 11.475 35.537 1.00 15.71 ? 97 VAL A CA 1 ATOM 701 C C . VAL A 1 97 ? 58.618 10.593 36.105 1.00 30.24 ? 97 VAL A C 1 ATOM 702 O O . VAL A 1 97 ? 58.595 10.219 37.269 1.00 41.62 ? 97 VAL A O 1 ATOM 703 C CB . VAL A 1 97 ? 57.709 12.835 36.141 1.00 9.30 ? 97 VAL A CB 1 ATOM 704 C CG1 . VAL A 1 97 ? 59.011 13.411 35.618 1.00 14.32 ? 97 VAL A CG1 1 ATOM 705 C CG2 . VAL A 1 97 ? 56.521 13.664 35.732 1.00 12.75 ? 97 VAL A CG2 1 ATOM 706 N N . ASN A 1 98 ? 59.553 10.286 35.269 1.00 21.44 ? 98 ASN A N 1 ATOM 707 C CA . ASN A 1 98 ? 60.662 9.441 35.605 1.00 14.30 ? 98 ASN A CA 1 ATOM 708 C C . ASN A 1 98 ? 60.394 8.042 35.254 1.00 12.09 ? 98 ASN A C 1 ATOM 709 O O . ASN A 1 98 ? 61.163 7.153 35.596 1.00 29.87 ? 98 ASN A O 1 ATOM 710 C CB . ASN A 1 98 ? 61.313 9.609 36.977 1.00 1.00 ? 98 ASN A CB 1 ATOM 711 C CG . ASN A 1 98 ? 61.875 11.021 37.164 1.00 44.34 ? 98 ASN A CG 1 ATOM 712 O OD1 . ASN A 1 98 ? 63.041 11.300 36.836 1.00 27.53 ? 98 ASN A OD1 1 ATOM 713 N ND2 . ASN A 1 98 ? 61.008 11.945 37.561 1.00 19.08 ? 98 ASN A ND2 1 ATOM 714 N N . VAL A 1 99 ? 59.284 7.877 34.559 1.00 7.70 ? 99 VAL A N 1 ATOM 715 C CA . VAL A 1 99 ? 58.822 6.588 34.035 1.00 12.32 ? 99 VAL A CA 1 ATOM 716 C C . VAL A 1 99 ? 59.298 6.356 32.582 1.00 41.52 ? 99 VAL A C 1 ATOM 717 O O . VAL A 1 99 ? 59.354 7.300 31.748 1.00 41.62 ? 99 VAL A O 1 ATOM 718 C CB . VAL A 1 99 ? 57.312 6.585 34.004 1.00 16.34 ? 99 VAL A CB 1 ATOM 719 C CG1 . VAL A 1 99 ? 56.775 5.385 33.200 1.00 13.51 ? 99 VAL A CG1 1 ATOM 720 C CG2 . VAL A 1 99 ? 56.768 6.665 35.429 1.00 10.54 ? 99 VAL A CG2 1 ATOM 721 N N . GLY A 1 100 ? 59.591 5.068 32.290 1.00 44.79 ? 100 GLY A N 1 ATOM 722 C CA . GLY A 1 100 ? 60.051 4.642 31.008 1.00 28.25 ? 100 GLY A CA 1 ATOM 723 C C . GLY A 1 100 ? 61.162 5.549 30.538 1.00 35.34 ? 100 GLY A C 1 ATOM 724 O O . GLY A 1 100 ? 62.298 5.452 30.991 1.00 44.08 ? 100 GLY A O 1 ATOM 725 N N . PHE A 1 101 ? 60.784 6.492 29.687 1.00 44.73 ? 101 PHE A N 1 ATOM 726 C CA . PHE A 1 101 ? 61.690 7.492 29.123 1.00 45.50 ? 101 PHE A CA 1 ATOM 727 C C . PHE A 1 101 ? 61.504 8.903 29.683 1.00 54.63 ? 101 PHE A C 1 ATOM 728 O O . PHE A 1 101 ? 62.401 9.709 29.529 1.00 65.14 ? 101 PHE A O 1 ATOM 729 C CB . PHE A 1 101 ? 61.651 7.543 27.577 1.00 44.52 ? 101 PHE A CB 1 ATOM 730 C CG . PHE A 1 101 ? 62.414 6.422 26.860 1.00 53.09 ? 101 PHE A CG 1 ATOM 731 C CD1 . PHE A 1 101 ? 63.780 6.196 27.085 1.00 43.04 ? 101 PHE A CD1 1 ATOM 732 C CD2 . PHE A 1 101 ? 61.755 5.602 25.935 1.00 52.82 ? 101 PHE A CD2 1 ATOM 733 C CE1 . PHE A 1 101 ? 64.480 5.191 26.410 1.00 30.18 ? 101 PHE A CE1 1 ATOM 734 C CE2 . PHE A 1 101 ? 62.434 4.586 25.257 1.00 44.58 ? 101 PHE A CE2 1 ATOM 735 C CZ . PHE A 1 101 ? 63.795 4.388 25.497 1.00 25.61 ? 101 PHE A CZ 1 ATOM 736 N N . SER A 1 102 ? 60.367 9.242 30.313 1.00 31.19 ? 102 SER A N 1 ATOM 737 C CA . SER A 1 102 ? 60.266 10.590 30.827 1.00 16.85 ? 102 SER A CA 1 ATOM 738 C C . SER A 1 102 ? 61.289 10.823 31.955 1.00 30.70 ? 102 SER A C 1 ATOM 739 O O . SER A 1 102 ? 61.987 9.912 32.435 1.00 22.41 ? 102 SER A O 1 ATOM 740 C CB . SER A 1 102 ? 58.870 10.901 31.263 1.00 17.81 ? 102 SER A CB 1 ATOM 741 O OG . SER A 1 102 ? 58.065 11.033 30.124 1.00 29.67 ? 102 SER A OG 1 ATOM 742 N N . TYR A 1 103 ? 61.414 12.052 32.405 1.00 36.54 ? 103 TYR A N 1 ATOM 743 C CA . TYR A 1 103 ? 62.359 12.305 33.469 1.00 38.74 ? 103 TYR A CA 1 ATOM 744 C C . TYR A 1 103 ? 62.180 13.694 34.042 1.00 54.69 ? 103 TYR A C 1 ATOM 745 O O . TYR A 1 103 ? 61.299 14.461 33.630 1.00 52.44 ? 103 TYR A O 1 ATOM 746 C CB . TYR A 1 103 ? 63.813 12.080 33.065 1.00 37.35 ? 103 TYR A CB 1 ATOM 747 C CG . TYR A 1 103 ? 64.204 13.158 32.095 1.00 49.65 ? 103 TYR A CG 1 ATOM 748 C CD1 . TYR A 1 103 ? 63.925 12.982 30.741 1.00 50.84 ? 103 TYR A CD1 1 ATOM 749 C CD2 . TYR A 1 103 ? 64.811 14.353 32.501 1.00 50.70 ? 103 TYR A CD2 1 ATOM 750 C CE1 . TYR A 1 103 ? 64.263 13.965 29.811 1.00 48.43 ? 103 TYR A CE1 1 ATOM 751 C CE2 . TYR A 1 103 ? 65.153 15.351 31.585 1.00 45.29 ? 103 TYR A CE2 1 ATOM 752 C CZ . TYR A 1 103 ? 64.867 15.153 30.231 1.00 68.50 ? 103 TYR A CZ 1 ATOM 753 O OH . TYR A 1 103 ? 65.184 16.110 29.290 1.00 91.74 ? 103 TYR A OH 1 ATOM 754 N N . SER A 1 104 ? 63.052 13.983 35.008 1.00 53.03 ? 104 SER A N 1 ATOM 755 C CA . SER A 1 104 ? 63.105 15.235 35.737 1.00 49.65 ? 104 SER A CA 1 ATOM 756 C C . SER A 1 104 ? 64.280 15.256 36.727 1.00 64.73 ? 104 SER A C 1 ATOM 757 O O . SER A 1 104 ? 64.909 14.237 36.998 1.00 67.97 ? 104 SER A O 1 ATOM 758 C CB . SER A 1 104 ? 61.802 15.511 36.456 1.00 42.11 ? 104 SER A CB 1 ATOM 759 O OG . SER A 1 104 ? 61.957 16.687 37.230 1.00 64.77 ? 104 SER A OG 1 ATOM 760 N N . GLY A 1 105 ? 64.594 16.426 37.273 1.00 65.53 ? 105 GLY A N 1 ATOM 761 C CA . GLY A 1 105 ? 65.693 16.535 38.210 1.00 62.94 ? 105 GLY A CA 1 ATOM 762 C C . GLY A 1 105 ? 65.204 16.519 39.645 1.00 88.11 ? 105 GLY A C 1 ATOM 763 O O . GLY A 1 105 ? 65.875 15.955 40.511 1.00 99.17 ? 105 GLY A O 1 ATOM 764 N N . SER A 1 106 ? 64.022 17.131 39.869 1.00 83.03 ? 106 SER A N 1 ATOM 765 C CA . SER A 1 106 ? 63.423 17.236 41.201 1.00 79.13 ? 106 SER A CA 1 ATOM 766 C C . SER A 1 106 ? 61.914 17.394 41.239 1.00 67.16 ? 106 SER A C 1 ATOM 767 O O . SER A 1 106 ? 61.381 18.486 41.110 1.00 55.32 ? 106 SER A O 1 ATOM 768 C CB . SER A 1 106 ? 63.998 18.451 41.899 1.00 95.17 ? 106 SER A CB 1 ATOM 769 O OG . SER A 1 106 ? 63.394 19.635 41.384 1.00 100.00 ? 106 SER A OG 1 ATOM 770 N N . SER A 1 107 ? 61.176 16.345 41.427 1.00 71.49 ? 107 SER A N 1 ATOM 771 C CA . SER A 1 107 ? 59.775 16.630 41.442 1.00 75.40 ? 107 SER A CA 1 ATOM 772 C C . SER A 1 107 ? 59.013 16.134 42.652 1.00 91.31 ? 107 SER A C 1 ATOM 773 O O . SER A 1 107 ? 59.379 16.360 43.811 1.00 91.78 ? 107 SER A O 1 ATOM 774 C CB . SER A 1 107 ? 59.092 16.250 40.149 1.00 80.49 ? 107 SER A CB 1 ATOM 775 O OG . SER A 1 107 ? 57.927 17.060 40.029 1.00 100.00 ? 107 SER A OG 1 ATOM 776 N N . GLY A 1 108 ? 57.921 15.464 42.319 1.00 90.55 ? 108 GLY A N 1 ATOM 777 C CA . GLY A 1 108 ? 57.009 14.882 43.256 1.00 85.12 ? 108 GLY A CA 1 ATOM 778 C C . GLY A 1 108 ? 56.507 13.544 42.723 1.00 67.31 ? 108 GLY A C 1 ATOM 779 O O . GLY A 1 108 ? 57.237 12.548 42.701 1.00 53.77 ? 108 GLY A O 1 ATOM 780 N N . VAL A 1 109 ? 55.242 13.555 42.285 1.00 56.90 ? 109 VAL A N 1 ATOM 781 C CA . VAL A 1 109 ? 54.547 12.391 41.774 1.00 48.28 ? 109 VAL A CA 1 ATOM 782 C C . VAL A 1 109 ? 54.604 11.195 42.708 1.00 42.20 ? 109 VAL A C 1 ATOM 783 O O . VAL A 1 109 ? 55.155 10.141 42.392 1.00 38.51 ? 109 VAL A O 1 ATOM 784 C CB . VAL A 1 109 ? 54.785 12.026 40.318 1.00 47.47 ? 109 VAL A CB 1 ATOM 785 C CG1 . VAL A 1 109 ? 54.368 13.193 39.434 1.00 44.10 ? 109 VAL A CG1 1 ATOM 786 C CG2 . VAL A 1 109 ? 56.232 11.603 40.063 1.00 46.39 ? 109 VAL A CG2 1 ATOM 787 N N . SER A 1 110 ? 54.016 11.384 43.876 1.00 29.06 ? 110 SER A N 1 ATOM 788 C CA . SER A 1 110 ? 53.945 10.347 44.884 1.00 24.99 ? 110 SER A CA 1 ATOM 789 C C . SER A 1 110 ? 52.483 9.976 45.084 1.00 23.10 ? 110 SER A C 1 ATOM 790 O O . SER A 1 110 ? 52.149 9.292 46.039 1.00 21.63 ? 110 SER A O 1 ATOM 791 C CB . SER A 1 110 ? 54.604 10.765 46.198 1.00 15.25 ? 110 SER A CB 1 ATOM 792 O OG . SER A 1 110 ? 54.004 11.965 46.661 1.00 19.87 ? 110 SER A OG 1 ATOM 793 N N . ASN A 1 111 ? 51.637 10.476 44.152 1.00 20.76 ? 111 ASN A N 1 ATOM 794 C CA . ASN A 1 111 ? 50.178 10.303 44.115 1.00 25.22 ? 111 ASN A CA 1 ATOM 795 C C . ASN A 1 111 ? 49.589 10.484 42.749 1.00 33.48 ? 111 ASN A C 1 ATOM 796 O O . ASN A 1 111 ? 50.349 10.843 41.868 1.00 37.28 ? 111 ASN A O 1 ATOM 797 C CB . ASN A 1 111 ? 49.356 11.005 45.201 1.00 21.47 ? 111 ASN A CB 1 ATOM 798 C CG . ASN A 1 111 ? 48.827 12.378 44.862 1.00 34.97 ? 111 ASN A CG 1 ATOM 799 O OD1 . ASN A 1 111 ? 47.769 12.508 44.218 1.00 68.09 ? 111 ASN A OD1 1 ATOM 800 N ND2 . ASN A 1 111 ? 49.412 13.386 45.525 1.00 25.73 ? 111 ASN A ND2 1 ATOM 801 N N . THR A 1 112 ? 48.263 10.199 42.616 1.00 23.68 ? 112 THR A N 1 ATOM 802 C CA . THR A 1 112 ? 47.494 10.225 41.384 1.00 11.92 ? 112 THR A CA 1 ATOM 803 C C . THR A 1 112 ? 46.983 11.563 40.951 1.00 23.86 ? 112 THR A C 1 ATOM 804 O O . THR A 1 112 ? 47.154 11.922 39.792 1.00 32.03 ? 112 THR A O 1 ATOM 805 C CB . THR A 1 112 ? 46.314 9.281 41.423 1.00 1.00 ? 112 THR A CB 1 ATOM 806 O OG1 . THR A 1 112 ? 46.634 8.122 40.707 1.00 37.46 ? 112 THR A OG1 1 ATOM 807 C CG2 . THR A 1 112 ? 45.166 9.998 40.730 1.00 21.25 ? 112 THR A CG2 1 ATOM 808 N N . VAL A 1 113 ? 46.335 12.274 41.872 1.00 17.18 ? 113 VAL A N 1 ATOM 809 C CA . VAL A 1 113 ? 45.782 13.595 41.591 1.00 16.58 ? 113 VAL A CA 1 ATOM 810 C C . VAL A 1 113 ? 46.737 14.517 40.842 1.00 9.12 ? 113 VAL A C 1 ATOM 811 O O . VAL A 1 113 ? 46.369 15.132 39.845 1.00 20.33 ? 113 VAL A O 1 ATOM 812 C CB . VAL A 1 113 ? 45.259 14.324 42.837 1.00 15.82 ? 113 VAL A CB 1 ATOM 813 C CG1 . VAL A 1 113 ? 45.181 15.827 42.516 1.00 8.05 ? 113 VAL A CG1 1 ATOM 814 C CG2 . VAL A 1 113 ? 43.890 13.773 43.276 1.00 14.39 ? 113 VAL A CG2 1 ATOM 815 N N . ALA A 1 114 ? 47.943 14.597 41.363 1.00 6.77 ? 114 ALA A N 1 ATOM 816 C CA . ALA A 1 114 ? 49.012 15.421 40.855 1.00 18.31 ? 114 ALA A CA 1 ATOM 817 C C . ALA A 1 114 ? 49.614 14.855 39.622 1.00 30.84 ? 114 ALA A C 1 ATOM 818 O O . ALA A 1 114 ? 50.466 15.493 39.008 1.00 36.82 ? 114 ALA A O 1 ATOM 819 C CB . ALA A 1 114 ? 50.148 15.481 41.859 1.00 17.76 ? 114 ALA A CB 1 ATOM 820 N N . ALA A 1 115 ? 49.221 13.646 39.289 1.00 16.04 ? 115 ALA A N 1 ATOM 821 C CA . ALA A 1 115 ? 49.838 13.091 38.111 1.00 23.79 ? 115 ALA A CA 1 ATOM 822 C C . ALA A 1 115 ? 49.062 13.566 36.939 1.00 24.15 ? 115 ALA A C 1 ATOM 823 O O . ALA A 1 115 ? 49.658 14.061 35.984 1.00 12.37 ? 115 ALA A O 1 ATOM 824 C CB . ALA A 1 115 ? 50.005 11.564 38.124 1.00 25.29 ? 115 ALA A CB 1 ATOM 825 N N . GLY A 1 116 ? 47.728 13.390 37.064 1.00 33.13 ? 116 GLY A N 1 ATOM 826 C CA . GLY A 1 116 ? 46.794 13.803 36.033 1.00 37.73 ? 116 GLY A CA 1 ATOM 827 C C . GLY A 1 116 ? 47.135 15.243 35.752 1.00 45.71 ? 116 GLY A C 1 ATOM 828 O O . GLY A 1 116 ? 47.241 15.657 34.594 1.00 48.26 ? 116 GLY A O 1 ATOM 829 N N . LYS A 1 117 ? 47.345 15.970 36.879 1.00 34.66 ? 117 LYS A N 1 ATOM 830 C CA . LYS A 1 117 ? 47.702 17.380 36.873 1.00 17.75 ? 117 LYS A CA 1 ATOM 831 C C . LYS A 1 117 ? 48.820 17.577 35.879 1.00 20.24 ? 117 LYS A C 1 ATOM 832 O O . LYS A 1 117 ? 48.854 18.541 35.165 1.00 44.35 ? 117 LYS A O 1 ATOM 833 C CB . LYS A 1 117 ? 47.964 18.014 38.257 1.00 17.27 ? 117 LYS A CB 1 ATOM 834 C CG . LYS A 1 117 ? 46.743 18.764 38.861 1.00 5.61 ? 117 LYS A CG 1 ATOM 835 C CD . LYS A 1 117 ? 46.919 19.342 40.279 1.00 42.31 ? 117 LYS A CD 1 ATOM 836 C CE . LYS A 1 117 ? 45.596 19.508 41.056 1.00 47.61 ? 117 LYS A CE 1 ATOM 837 N NZ . LYS A 1 117 ? 45.253 20.905 41.435 1.00 41.30 ? 117 LYS A NZ 1 ATOM 838 N N . ASP A 1 118 ? 49.736 16.652 35.769 1.00 13.15 ? 118 ASP A N 1 ATOM 839 C CA . ASP A 1 118 ? 50.760 16.877 34.786 1.00 17.59 ? 118 ASP A CA 1 ATOM 840 C C . ASP A 1 118 ? 50.318 16.358 33.450 1.00 24.73 ? 118 ASP A C 1 ATOM 841 O O . ASP A 1 118 ? 50.702 16.839 32.398 1.00 41.83 ? 118 ASP A O 1 ATOM 842 C CB . ASP A 1 118 ? 52.107 16.283 35.141 1.00 20.65 ? 118 ASP A CB 1 ATOM 843 C CG . ASP A 1 118 ? 52.569 16.891 36.400 1.00 38.80 ? 118 ASP A CG 1 ATOM 844 O OD1 . ASP A 1 118 ? 51.965 17.857 36.875 1.00 36.43 ? 118 ASP A OD1 1 ATOM 845 O OD2 . ASP A 1 118 ? 53.616 16.244 36.924 1.00 13.07 ? 118 ASP A OD2 1 ATOM 846 N N . VAL A 1 119 ? 49.521 15.359 33.491 1.00 2.98 ? 119 VAL A N 1 ATOM 847 C CA . VAL A 1 119 ? 49.086 14.843 32.254 1.00 6.14 ? 119 VAL A CA 1 ATOM 848 C C . VAL A 1 119 ? 48.278 15.864 31.480 1.00 33.90 ? 119 VAL A C 1 ATOM 849 O O . VAL A 1 119 ? 48.472 16.044 30.281 1.00 52.11 ? 119 VAL A O 1 ATOM 850 C CB . VAL A 1 119 ? 48.352 13.570 32.479 1.00 3.60 ? 119 VAL A CB 1 ATOM 851 C CG1 . VAL A 1 119 ? 47.447 13.227 31.297 1.00 1.00 ? 119 VAL A CG1 1 ATOM 852 C CG2 . VAL A 1 119 ? 49.426 12.533 32.766 1.00 1.07 ? 119 VAL A CG2 1 ATOM 853 N N . TYR A 1 120 ? 47.416 16.566 32.153 1.00 32.50 ? 120 TYR A N 1 ATOM 854 C CA . TYR A 1 120 ? 46.663 17.547 31.420 1.00 46.33 ? 120 TYR A CA 1 ATOM 855 C C . TYR A 1 120 ? 47.588 18.615 30.883 1.00 59.65 ? 120 TYR A C 1 ATOM 856 O O . TYR A 1 120 ? 47.330 19.168 29.807 1.00 59.20 ? 120 TYR A O 1 ATOM 857 C CB . TYR A 1 120 ? 45.572 18.196 32.255 1.00 49.92 ? 120 TYR A CB 1 ATOM 858 C CG . TYR A 1 120 ? 44.914 19.403 31.630 1.00 49.37 ? 120 TYR A CG 1 ATOM 859 C CD1 . TYR A 1 120 ? 45.491 20.680 31.610 1.00 41.01 ? 120 TYR A CD1 1 ATOM 860 C CD2 . TYR A 1 120 ? 43.631 19.257 31.111 1.00 62.18 ? 120 TYR A CD2 1 ATOM 861 C CE1 . TYR A 1 120 ? 44.817 21.788 31.074 1.00 40.11 ? 120 TYR A CE1 1 ATOM 862 C CE2 . TYR A 1 120 ? 42.946 20.352 30.581 1.00 92.93 ? 120 TYR A CE2 1 ATOM 863 C CZ . TYR A 1 120 ? 43.527 21.620 30.551 1.00 70.21 ? 120 TYR A CZ 1 ATOM 864 O OH . TYR A 1 120 ? 42.776 22.650 29.999 1.00 16.30 ? 120 TYR A OH 1 ATOM 865 N N . ASN A 1 121 ? 48.673 18.880 31.624 1.00 39.37 ? 121 ASN A N 1 ATOM 866 C CA . ASN A 1 121 ? 49.595 19.880 31.143 1.00 34.63 ? 121 ASN A CA 1 ATOM 867 C C . ASN A 1 121 ? 50.330 19.414 29.910 1.00 45.37 ? 121 ASN A C 1 ATOM 868 O O . ASN A 1 121 ? 50.914 20.186 29.154 1.00 50.53 ? 121 ASN A O 1 ATOM 869 C CB . ASN A 1 121 ? 50.482 20.481 32.229 1.00 14.29 ? 121 ASN A CB 1 ATOM 870 C CG . ASN A 1 121 ? 49.586 21.223 33.156 1.00 34.04 ? 121 ASN A CG 1 ATOM 871 O OD1 . ASN A 1 121 ? 48.491 21.650 32.749 1.00 56.14 ? 121 ASN A OD1 1 ATOM 872 N ND2 . ASN A 1 121 ? 49.991 21.288 34.420 1.00 99.15 ? 121 ASN A ND2 1 ATOM 873 N N . PHE A 1 122 ? 50.292 18.126 29.669 1.00 41.39 ? 122 PHE A N 1 ATOM 874 C CA . PHE A 1 122 ? 50.970 17.714 28.482 1.00 40.69 ? 122 PHE A CA 1 ATOM 875 C C . PHE A 1 122 ? 49.988 17.574 27.348 1.00 46.47 ? 122 PHE A C 1 ATOM 876 O O . PHE A 1 122 ? 50.357 17.739 26.195 1.00 59.18 ? 122 PHE A O 1 ATOM 877 C CB . PHE A 1 122 ? 51.902 16.501 28.663 1.00 38.72 ? 122 PHE A CB 1 ATOM 878 C CG . PHE A 1 122 ? 51.980 15.566 27.459 1.00 42.25 ? 122 PHE A CG 1 ATOM 879 C CD1 . PHE A 1 122 ? 50.900 14.776 27.049 1.00 31.52 ? 122 PHE A CD1 1 ATOM 880 C CD2 . PHE A 1 122 ? 53.178 15.432 26.755 1.00 42.17 ? 122 PHE A CD2 1 ATOM 881 C CE1 . PHE A 1 122 ? 50.983 13.906 25.962 1.00 29.11 ? 122 PHE A CE1 1 ATOM 882 C CE2 . PHE A 1 122 ? 53.277 14.572 25.657 1.00 43.35 ? 122 PHE A CE2 1 ATOM 883 C CZ . PHE A 1 122 ? 52.181 13.807 25.258 1.00 33.51 ? 122 PHE A CZ 1 ATOM 884 N N . LEU A 1 123 ? 48.745 17.217 27.662 1.00 36.92 ? 123 LEU A N 1 ATOM 885 C CA . LEU A 1 123 ? 47.759 17.038 26.597 1.00 33.47 ? 123 LEU A CA 1 ATOM 886 C C . LEU A 1 123 ? 47.487 18.334 25.852 1.00 37.12 ? 123 LEU A C 1 ATOM 887 O O . LEU A 1 123 ? 47.248 18.373 24.657 1.00 43.71 ? 123 LEU A O 1 ATOM 888 C CB . LEU A 1 123 ? 46.494 16.279 27.044 1.00 29.60 ? 123 LEU A CB 1 ATOM 889 C CG . LEU A 1 123 ? 46.369 14.842 26.511 1.00 25.43 ? 123 LEU A CG 1 ATOM 890 C CD1 . LEU A 1 123 ? 45.039 14.718 25.801 1.00 36.64 ? 123 LEU A CD1 1 ATOM 891 C CD2 . LEU A 1 123 ? 47.488 14.439 25.542 1.00 4.13 ? 123 LEU A CD2 1 ATOM 892 N N . GLU A 1 124 ? 47.590 19.426 26.567 1.00 38.21 ? 124 GLU A N 1 ATOM 893 C CA . GLU A 1 124 ? 47.418 20.725 25.975 1.00 34.95 ? 124 GLU A CA 1 ATOM 894 C C . GLU A 1 124 ? 48.691 21.192 25.152 1.00 60.73 ? 124 GLU A C 1 ATOM 895 O O . GLU A 1 124 ? 48.590 21.883 24.143 1.00 61.13 ? 124 GLU A O 1 ATOM 896 C CB . GLU A 1 124 ? 46.886 21.658 27.059 1.00 30.27 ? 124 GLU A CB 1 ATOM 897 C CG . GLU A 1 124 ? 47.005 23.151 26.764 1.00 85.18 ? 124 GLU A CG 1 ATOM 898 C CD . GLU A 1 124 ? 47.638 23.865 27.917 1.00 100.00 ? 124 GLU A CD 1 ATOM 899 O OE1 . GLU A 1 124 ? 48.874 23.459 28.084 1.00 100.00 ? 124 GLU A OE1 1 ATOM 900 O OE2 . GLU A 1 124 ? 47.027 24.614 28.681 1.00 100.00 ? 124 GLU A OE2 1 ATOM 901 N N . LEU A 1 125 ? 49.913 20.773 25.540 1.00 60.94 ? 125 LEU A N 1 ATOM 902 C CA . LEU A 1 125 ? 51.138 21.116 24.806 1.00 53.83 ? 125 LEU A CA 1 ATOM 903 C C . LEU A 1 125 ? 51.266 20.272 23.583 1.00 63.03 ? 125 LEU A C 1 ATOM 904 O O . LEU A 1 125 ? 51.917 20.644 22.632 1.00 78.15 ? 125 LEU A O 1 ATOM 905 C CB . LEU A 1 125 ? 52.421 20.735 25.547 1.00 49.69 ? 125 LEU A CB 1 ATOM 906 C CG . LEU A 1 125 ? 52.370 21.189 26.969 1.00 63.63 ? 125 LEU A CG 1 ATOM 907 C CD1 . LEU A 1 125 ? 53.784 21.400 27.492 1.00 70.04 ? 125 LEU A CD1 1 ATOM 908 C CD2 . LEU A 1 125 ? 51.586 22.489 26.984 1.00 51.10 ? 125 LEU A CD2 1 ATOM 909 N N . PHE A 1 126 ? 50.700 19.098 23.629 1.00 50.75 ? 126 PHE A N 1 ATOM 910 C CA . PHE A 1 126 ? 50.814 18.207 22.500 1.00 47.31 ? 126 PHE A CA 1 ATOM 911 C C . PHE A 1 126 ? 49.809 18.573 21.449 1.00 53.57 ? 126 PHE A C 1 ATOM 912 O O . PHE A 1 126 ? 50.102 18.553 20.250 1.00 50.42 ? 126 PHE A O 1 ATOM 913 C CB . PHE A 1 126 ? 50.589 16.749 22.928 1.00 41.00 ? 126 PHE A CB 1 ATOM 914 C CG . PHE A 1 126 ? 49.970 15.871 21.862 1.00 31.63 ? 126 PHE A CG 1 ATOM 915 C CD1 . PHE A 1 126 ? 48.615 15.869 21.515 1.00 36.78 ? 126 PHE A CD1 1 ATOM 916 C CD2 . PHE A 1 126 ? 50.817 14.975 21.218 1.00 28.32 ? 126 PHE A CD2 1 ATOM 917 C CE1 . PHE A 1 126 ? 48.145 15.014 20.517 1.00 48.76 ? 126 PHE A CE1 1 ATOM 918 C CE2 . PHE A 1 126 ? 50.351 14.108 20.234 1.00 33.37 ? 126 PHE A CE2 1 ATOM 919 C CZ . PHE A 1 126 ? 49.003 14.117 19.880 1.00 37.77 ? 126 PHE A CZ 1 ATOM 920 N N . PHE A 1 127 ? 48.594 18.841 21.928 1.00 36.03 ? 127 PHE A N 1 ATOM 921 C CA . PHE A 1 127 ? 47.563 19.168 21.020 1.00 30.01 ? 127 PHE A CA 1 ATOM 922 C C . PHE A 1 127 ? 47.948 20.413 20.318 1.00 50.21 ? 127 PHE A C 1 ATOM 923 O O . PHE A 1 127 ? 47.589 20.664 19.179 1.00 60.00 ? 127 PHE A O 1 ATOM 924 C CB . PHE A 1 127 ? 46.245 19.336 21.719 1.00 33.90 ? 127 PHE A CB 1 ATOM 925 C CG . PHE A 1 127 ? 45.606 17.988 21.719 1.00 45.95 ? 127 PHE A CG 1 ATOM 926 C CD1 . PHE A 1 127 ? 45.874 17.077 20.701 1.00 53.39 ? 127 PHE A CD1 1 ATOM 927 C CD2 . PHE A 1 127 ? 44.767 17.587 22.753 1.00 50.72 ? 127 PHE A CD2 1 ATOM 928 C CE1 . PHE A 1 127 ? 45.277 15.818 20.695 1.00 48.16 ? 127 PHE A CE1 1 ATOM 929 C CE2 . PHE A 1 127 ? 44.175 16.327 22.781 1.00 46.49 ? 127 PHE A CE2 1 ATOM 930 C CZ . PHE A 1 127 ? 44.439 15.441 21.741 1.00 44.33 ? 127 PHE A CZ 1 ATOM 931 N N . ASP A 1 128 ? 48.709 21.201 21.018 1.00 45.99 ? 128 ASP A N 1 ATOM 932 C CA . ASP A 1 128 ? 49.160 22.433 20.444 1.00 42.95 ? 128 ASP A CA 1 ATOM 933 C C . ASP A 1 128 ? 49.990 22.224 19.187 1.00 60.25 ? 128 ASP A C 1 ATOM 934 O O . ASP A 1 128 ? 49.620 22.676 18.091 1.00 70.49 ? 128 ASP A O 1 ATOM 935 C CB . ASP A 1 128 ? 49.975 23.219 21.460 1.00 39.86 ? 128 ASP A CB 1 ATOM 936 C CG . ASP A 1 128 ? 49.285 24.490 21.852 1.00 93.43 ? 128 ASP A CG 1 ATOM 937 O OD1 . ASP A 1 128 ? 48.339 24.511 22.613 1.00 100.00 ? 128 ASP A OD1 1 ATOM 938 O OD2 . ASP A 1 128 ? 49.756 25.553 21.237 1.00 100.00 ? 128 ASP A OD2 1 ATOM 939 N N . GLN A 1 129 ? 51.126 21.539 19.383 1.00 48.20 ? 129 GLN A N 1 ATOM 940 C CA . GLN A 1 129 ? 52.097 21.237 18.343 1.00 44.20 ? 129 GLN A CA 1 ATOM 941 C C . GLN A 1 129 ? 51.597 20.406 17.185 1.00 54.14 ? 129 GLN A C 1 ATOM 942 O O . GLN A 1 129 ? 52.203 20.464 16.108 1.00 64.10 ? 129 GLN A O 1 ATOM 943 C CB . GLN A 1 129 ? 53.479 20.801 18.849 1.00 39.83 ? 129 GLN A CB 1 ATOM 944 C CG . GLN A 1 129 ? 53.732 21.259 20.300 1.00 100.00 ? 129 GLN A CG 1 ATOM 945 C CD . GLN A 1 129 ? 54.205 22.705 20.451 1.00 95.96 ? 129 GLN A CD 1 ATOM 946 O OE1 . GLN A 1 129 ? 55.294 22.975 21.003 1.00 55.31 ? 129 GLN A OE1 1 ATOM 947 N NE2 . GLN A 1 129 ? 53.356 23.648 20.041 1.00 98.16 ? 129 GLN A NE2 1 ATOM 948 N N . PHE A 1 130 ? 50.507 19.658 17.425 1.00 41.28 ? 130 PHE A N 1 ATOM 949 C CA . PHE A 1 130 ? 49.843 18.796 16.431 1.00 43.70 ? 130 PHE A CA 1 ATOM 950 C C . PHE A 1 130 ? 48.330 19.025 16.496 1.00 50.57 ? 130 PHE A C 1 ATOM 951 O O . PHE A 1 130 ? 47.536 18.112 16.822 1.00 49.75 ? 130 PHE A O 1 ATOM 952 C CB . PHE A 1 130 ? 50.131 17.295 16.628 1.00 44.08 ? 130 PHE A CB 1 ATOM 953 C CG . PHE A 1 130 ? 51.593 16.944 16.733 1.00 49.39 ? 130 PHE A CG 1 ATOM 954 C CD1 . PHE A 1 130 ? 52.343 17.338 17.838 1.00 52.02 ? 130 PHE A CD1 1 ATOM 955 C CD2 . PHE A 1 130 ? 52.223 16.213 15.724 1.00 65.30 ? 130 PHE A CD2 1 ATOM 956 C CE1 . PHE A 1 130 ? 53.695 17.013 17.928 1.00 63.32 ? 130 PHE A CE1 1 ATOM 957 C CE2 . PHE A 1 130 ? 53.577 15.884 15.786 1.00 74.32 ? 130 PHE A CE2 1 ATOM 958 C CZ . PHE A 1 130 ? 54.309 16.288 16.903 1.00 73.07 ? 130 PHE A CZ 1 ATOM 959 N N . PRO A 1 131 ? 47.957 20.274 16.203 1.00 33.25 ? 131 PRO A N 1 ATOM 960 C CA . PRO A 1 131 ? 46.592 20.750 16.231 1.00 28.61 ? 131 PRO A CA 1 ATOM 961 C C . PRO A 1 131 ? 45.766 20.065 15.168 1.00 36.39 ? 131 PRO A C 1 ATOM 962 O O . PRO A 1 131 ? 44.537 20.244 15.090 1.00 28.74 ? 131 PRO A O 1 ATOM 963 C CB . PRO A 1 131 ? 46.701 22.236 15.958 1.00 32.13 ? 131 PRO A CB 1 ATOM 964 C CG . PRO A 1 131 ? 48.145 22.490 15.501 1.00 38.76 ? 131 PRO A CG 1 ATOM 965 C CD . PRO A 1 131 ? 48.814 21.145 15.359 1.00 27.06 ? 131 PRO A CD 1 ATOM 966 N N . GLU A 1 132 ? 46.512 19.271 14.387 1.00 22.44 ? 132 GLU A N 1 ATOM 967 C CA . GLU A 1 132 ? 46.050 18.453 13.306 1.00 18.31 ? 132 GLU A CA 1 ATOM 968 C C . GLU A 1 132 ? 45.215 17.278 13.767 1.00 39.64 ? 132 GLU A C 1 ATOM 969 O O . GLU A 1 132 ? 44.957 16.342 13.028 1.00 48.27 ? 132 GLU A O 1 ATOM 970 C CB . GLU A 1 132 ? 47.320 17.973 12.692 1.00 15.50 ? 132 GLU A CB 1 ATOM 971 C CG . GLU A 1 132 ? 48.391 18.911 13.267 1.00 31.42 ? 132 GLU A CG 1 ATOM 972 C CD . GLU A 1 132 ? 49.757 18.345 13.144 1.00 68.54 ? 132 GLU A CD 1 ATOM 973 O OE1 . GLU A 1 132 ? 49.970 17.275 12.587 1.00 100.00 ? 132 GLU A OE1 1 ATOM 974 O OE2 . GLU A 1 132 ? 50.681 19.171 13.588 1.00 60.62 ? 132 GLU A OE2 1 ATOM 975 N N . TYR A 1 133 ? 44.772 17.317 14.989 1.00 46.93 ? 133 TYR A N 1 ATOM 976 C CA . TYR A 1 133 ? 43.983 16.219 15.432 1.00 54.65 ? 133 TYR A CA 1 ATOM 977 C C . TYR A 1 133 ? 42.664 16.663 16.033 1.00 88.35 ? 133 TYR A C 1 ATOM 978 O O . TYR A 1 133 ? 41.835 15.861 16.435 1.00 94.92 ? 133 TYR A O 1 ATOM 979 C CB . TYR A 1 133 ? 44.785 15.324 16.381 1.00 48.82 ? 133 TYR A CB 1 ATOM 980 C CG . TYR A 1 133 ? 46.079 14.849 15.785 1.00 33.78 ? 133 TYR A CG 1 ATOM 981 C CD1 . TYR A 1 133 ? 46.132 14.105 14.600 1.00 29.16 ? 133 TYR A CD1 1 ATOM 982 C CD2 . TYR A 1 133 ? 47.271 15.136 16.443 1.00 31.57 ? 133 TYR A CD2 1 ATOM 983 C CE1 . TYR A 1 133 ? 47.346 13.663 14.064 1.00 21.98 ? 133 TYR A CE1 1 ATOM 984 C CE2 . TYR A 1 133 ? 48.492 14.705 15.917 1.00 35.80 ? 133 TYR A CE2 1 ATOM 985 C CZ . TYR A 1 133 ? 48.540 13.964 14.727 1.00 58.73 ? 133 TYR A CZ 1 ATOM 986 O OH . TYR A 1 133 ? 49.759 13.524 14.197 1.00 35.08 ? 133 TYR A OH 1 ATOM 987 N N . VAL A 1 134 ? 42.461 17.961 16.104 1.00 99.73 ? 134 VAL A N 1 ATOM 988 C CA . VAL A 1 134 ? 41.218 18.450 16.672 1.00 100.00 ? 134 VAL A CA 1 ATOM 989 C C . VAL A 1 134 ? 40.302 19.066 15.621 1.00 100.00 ? 134 VAL A C 1 ATOM 990 O O . VAL A 1 134 ? 39.336 18.391 15.237 1.00 100.00 ? 134 VAL A O 1 ATOM 991 C CB . VAL A 1 134 ? 41.409 19.343 17.911 1.00 100.00 ? 134 VAL A CB 1 ATOM 992 C CG1 . VAL A 1 134 ? 40.063 19.786 18.472 1.00 98.89 ? 134 VAL A CG1 1 ATOM 993 C CG2 . VAL A 1 134 ? 42.222 18.638 19.000 1.00 99.29 ? 134 VAL A CG2 1 ATOM 994 N N . ASN A 1 135 ? 40.649 20.314 15.191 1.00 99.81 ? 135 ASN A N 1 ATOM 995 C CA . ASN A 1 135 ? 39.947 21.140 14.195 1.00 98.06 ? 135 ASN A CA 1 ATOM 996 C C . ASN A 1 135 ? 38.984 20.355 13.330 1.00 92.75 ? 135 ASN A C 1 ATOM 997 O O . ASN A 1 135 ? 37.802 20.713 13.225 1.00 96.35 ? 135 ASN A O 1 ATOM 998 C CB . ASN A 1 135 ? 40.889 21.990 13.314 1.00 89.37 ? 135 ASN A CB 1 ATOM 999 C CG . ASN A 1 135 ? 42.374 21.716 13.521 1.00 100.00 ? 135 ASN A CG 1 ATOM 1000 O OD1 . ASN A 1 135 ? 42.891 20.668 13.113 1.00 100.00 ? 135 ASN A OD1 1 ATOM 1001 N ND2 . ASN A 1 135 ? 43.077 22.698 14.087 1.00 100.00 ? 135 ASN A ND2 1 ATOM 1002 N N . LYS A 1 136 ? 39.537 19.253 12.776 1.00 70.67 ? 136 LYS A N 1 ATOM 1003 C CA . LYS A 1 136 ? 38.831 18.322 11.912 1.00 68.22 ? 136 LYS A CA 1 ATOM 1004 C C . LYS A 1 136 ? 37.647 17.662 12.591 1.00 75.79 ? 136 LYS A C 1 ATOM 1005 O O . LYS A 1 136 ? 36.906 16.925 11.931 1.00 69.12 ? 136 LYS A O 1 ATOM 1006 C CB . LYS A 1 136 ? 39.761 17.254 11.338 1.00 65.20 ? 136 LYS A CB 1 ATOM 1007 C CG . LYS A 1 136 ? 40.820 17.822 10.401 1.00 100.00 ? 136 LYS A CG 1 ATOM 1008 C CD . LYS A 1 136 ? 40.201 18.715 9.315 1.00 100.00 ? 136 LYS A CD 1 ATOM 1009 C CE . LYS A 1 136 ? 41.167 19.225 8.248 1.00 100.00 ? 136 LYS A CE 1 ATOM 1010 N NZ . LYS A 1 136 ? 40.565 20.271 7.380 1.00 100.00 ? 136 LYS A NZ 1 ATOM 1011 N N . GLY A 1 137 ? 37.493 17.937 13.904 1.00 77.42 ? 137 GLY A N 1 ATOM 1012 C CA . GLY A 1 137 ? 36.435 17.361 14.735 1.00 77.06 ? 137 GLY A CA 1 ATOM 1013 C C . GLY A 1 137 ? 36.796 15.901 15.059 1.00 80.47 ? 137 GLY A C 1 ATOM 1014 O O . GLY A 1 137 ? 35.996 14.968 14.911 1.00 81.25 ? 137 GLY A O 1 ATOM 1015 N N . GLN A 1 138 ? 38.044 15.705 15.492 1.00 75.85 ? 138 GLN A N 1 ATOM 1016 C CA . GLN A 1 138 ? 38.536 14.380 15.814 1.00 70.73 ? 138 GLN A CA 1 ATOM 1017 C C . GLN A 1 138 ? 38.389 13.901 17.259 1.00 52.50 ? 138 GLN A C 1 ATOM 1018 O O . GLN A 1 138 ? 39.215 14.207 18.135 1.00 58.05 ? 138 GLN A O 1 ATOM 1019 C CB . GLN A 1 138 ? 39.986 14.104 15.314 1.00 69.73 ? 138 GLN A CB 1 ATOM 1020 C CG . GLN A 1 138 ? 40.166 13.951 13.793 1.00 58.87 ? 138 GLN A CG 1 ATOM 1021 C CD . GLN A 1 138 ? 41.475 14.509 13.251 1.00 100.00 ? 138 GLN A CD 1 ATOM 1022 O OE1 . GLN A 1 138 ? 41.500 15.268 12.262 1.00 100.00 ? 138 GLN A OE1 1 ATOM 1023 N NE2 . GLN A 1 138 ? 42.580 14.079 13.856 1.00 100.00 ? 138 GLN A NE2 1 ATOM 1024 N N . ASP A 1 139 ? 37.342 13.112 17.445 1.00 22.49 ? 139 ASP A N 1 ATOM 1025 C CA . ASP A 1 139 ? 37.012 12.413 18.657 1.00 37.98 ? 139 ASP A CA 1 ATOM 1026 C C . ASP A 1 139 ? 38.301 11.887 19.385 1.00 48.64 ? 139 ASP A C 1 ATOM 1027 O O . ASP A 1 139 ? 39.043 11.012 18.896 1.00 43.55 ? 139 ASP A O 1 ATOM 1028 C CB . ASP A 1 139 ? 36.248 11.126 18.201 1.00 47.92 ? 139 ASP A CB 1 ATOM 1029 C CG . ASP A 1 139 ? 34.735 11.086 18.398 1.00 81.56 ? 139 ASP A CG 1 ATOM 1030 O OD1 . ASP A 1 139 ? 34.153 12.284 18.419 1.00 100.00 ? 139 ASP A OD1 1 ATOM 1031 O OD2 . ASP A 1 139 ? 34.121 10.018 18.499 1.00 51.39 ? 139 ASP A OD2 1 ATOM 1032 N N . PHE A 1 140 ? 38.570 12.422 20.575 1.00 37.32 ? 140 PHE A N 1 ATOM 1033 C CA . PHE A 1 140 ? 39.716 12.005 21.338 1.00 34.88 ? 140 PHE A CA 1 ATOM 1034 C C . PHE A 1 140 ? 39.304 11.237 22.570 1.00 44.09 ? 140 PHE A C 1 ATOM 1035 O O . PHE A 1 140 ? 38.399 11.680 23.281 1.00 43.89 ? 140 PHE A O 1 ATOM 1036 C CB . PHE A 1 140 ? 40.469 13.217 21.842 1.00 32.22 ? 140 PHE A CB 1 ATOM 1037 C CG . PHE A 1 140 ? 41.415 12.811 22.922 1.00 25.80 ? 140 PHE A CG 1 ATOM 1038 C CD1 . PHE A 1 140 ? 42.251 11.718 22.719 1.00 24.04 ? 140 PHE A CD1 1 ATOM 1039 C CD2 . PHE A 1 140 ? 41.494 13.510 24.124 1.00 27.41 ? 140 PHE A CD2 1 ATOM 1040 C CE1 . PHE A 1 140 ? 43.177 11.323 23.681 1.00 28.87 ? 140 PHE A CE1 1 ATOM 1041 C CE2 . PHE A 1 140 ? 42.393 13.121 25.116 1.00 25.32 ? 140 PHE A CE2 1 ATOM 1042 C CZ . PHE A 1 140 ? 43.227 12.021 24.887 1.00 28.33 ? 140 PHE A CZ 1 ATOM 1043 N N . HIS A 1 141 ? 39.968 10.104 22.835 1.00 35.66 ? 141 HIS A N 1 ATOM 1044 C CA . HIS A 1 141 ? 39.615 9.356 24.035 1.00 37.90 ? 141 HIS A CA 1 ATOM 1045 C C . HIS A 1 141 ? 40.824 8.849 24.709 1.00 52.06 ? 141 HIS A C 1 ATOM 1046 O O . HIS A 1 141 ? 41.897 8.884 24.149 1.00 48.04 ? 141 HIS A O 1 ATOM 1047 C CB . HIS A 1 141 ? 38.716 8.129 23.922 1.00 33.30 ? 141 HIS A CB 1 ATOM 1048 C CG . HIS A 1 141 ? 37.905 8.005 22.703 1.00 33.11 ? 141 HIS A CG 1 ATOM 1049 N ND1 . HIS A 1 141 ? 36.838 7.112 22.670 1.00 32.73 ? 141 HIS A ND1 1 ATOM 1050 C CD2 . HIS A 1 141 ? 38.006 8.629 21.510 1.00 24.45 ? 141 HIS A CD2 1 ATOM 1051 C CE1 . HIS A 1 141 ? 36.303 7.231 21.472 1.00 28.03 ? 141 HIS A CE1 1 ATOM 1052 N NE2 . HIS A 1 141 ? 36.976 8.132 20.756 1.00 25.92 ? 141 HIS A NE2 1 ATOM 1053 N N . ILE A 1 142 ? 40.612 8.350 25.921 1.00 60.14 ? 142 ILE A N 1 ATOM 1054 C CA . ILE A 1 142 ? 41.706 7.787 26.689 1.00 54.36 ? 142 ILE A CA 1 ATOM 1055 C C . ILE A 1 142 ? 41.445 6.373 27.175 1.00 35.14 ? 142 ILE A C 1 ATOM 1056 O O . ILE A 1 142 ? 40.335 6.010 27.570 1.00 24.95 ? 142 ILE A O 1 ATOM 1057 C CB . ILE A 1 142 ? 42.246 8.636 27.816 1.00 54.54 ? 142 ILE A CB 1 ATOM 1058 C CG1 . ILE A 1 142 ? 41.948 10.108 27.595 1.00 65.26 ? 142 ILE A CG1 1 ATOM 1059 C CG2 . ILE A 1 142 ? 43.751 8.424 27.905 1.00 48.29 ? 142 ILE A CG2 1 ATOM 1060 C CD1 . ILE A 1 142 ? 41.731 10.864 28.911 1.00 52.42 ? 142 ILE A CD1 1 ATOM 1061 N N . ALA A 1 143 ? 42.509 5.595 27.126 1.00 18.62 ? 143 ALA A N 1 ATOM 1062 C CA . ALA A 1 143 ? 42.451 4.249 27.563 1.00 20.81 ? 143 ALA A CA 1 ATOM 1063 C C . ALA A 1 143 ? 43.701 3.801 28.360 1.00 25.25 ? 143 ALA A C 1 ATOM 1064 O O . ALA A 1 143 ? 44.830 4.342 28.249 1.00 13.72 ? 143 ALA A O 1 ATOM 1065 C CB . ALA A 1 143 ? 41.794 3.292 26.569 1.00 18.99 ? 143 ALA A CB 1 ATOM 1066 N N . GLY A 1 144 ? 43.476 2.807 29.200 1.00 14.90 ? 144 GLY A N 1 ATOM 1067 C CA . GLY A 1 144 ? 44.533 2.298 30.028 1.00 12.62 ? 144 GLY A CA 1 ATOM 1068 C C . GLY A 1 144 ? 44.119 0.978 30.654 1.00 21.44 ? 144 GLY A C 1 ATOM 1069 O O . GLY A 1 144 ? 42.963 0.478 30.490 1.00 11.30 ? 144 GLY A O 1 ATOM 1070 N N . GLU A 1 145 ? 45.085 0.439 31.393 1.00 11.00 ? 145 GLU A N 1 ATOM 1071 C CA . GLU A 1 145 ? 44.901 -0.827 32.038 1.00 13.52 ? 145 GLU A CA 1 ATOM 1072 C C . GLU A 1 145 ? 45.453 -0.902 33.474 1.00 20.83 ? 145 GLU A C 1 ATOM 1073 O O . GLU A 1 145 ? 46.449 -0.247 33.824 1.00 9.00 ? 145 GLU A O 1 ATOM 1074 C CB . GLU A 1 145 ? 45.616 -1.835 31.072 1.00 15.94 ? 145 GLU A CB 1 ATOM 1075 C CG . GLU A 1 145 ? 46.080 -3.221 31.577 1.00 37.16 ? 145 GLU A CG 1 ATOM 1076 C CD . GLU A 1 145 ? 47.418 -3.665 31.005 1.00 52.20 ? 145 GLU A CD 1 ATOM 1077 O OE1 . GLU A 1 145 ? 47.370 -3.860 29.710 1.00 56.31 ? 145 GLU A OE1 1 ATOM 1078 O OE2 . GLU A 1 145 ? 48.428 -3.853 31.683 1.00 71.30 ? 145 GLU A OE2 1 ATOM 1079 N N . SER A 1 146 ? 44.814 -1.743 34.310 1.00 20.55 ? 146 SER A N 1 ATOM 1080 C CA . SER A 1 146 ? 45.255 -1.965 35.692 1.00 16.87 ? 146 SER A CA 1 ATOM 1081 C C . SER A 1 146 ? 45.232 -0.742 36.615 1.00 13.24 ? 146 SER A C 1 ATOM 1082 O O . SER A 1 146 ? 44.186 -0.277 37.028 1.00 22.41 ? 146 SER A O 1 ATOM 1083 C CB . SER A 1 146 ? 46.558 -2.779 35.735 1.00 31.38 ? 146 SER A CB 1 ATOM 1084 O OG . SER A 1 146 ? 47.758 -2.019 35.820 1.00 42.39 ? 146 SER A OG 1 ATOM 1085 N N . TYR A 1 147 ? 46.387 -0.196 36.951 1.00 13.28 ? 147 TYR A N 1 ATOM 1086 C CA . TYR A 1 147 ? 46.453 0.977 37.819 1.00 4.46 ? 147 TYR A CA 1 ATOM 1087 C C . TYR A 1 147 ? 45.896 2.183 37.159 1.00 20.00 ? 147 TYR A C 1 ATOM 1088 O O . TYR A 1 147 ? 45.607 3.144 37.854 1.00 22.18 ? 147 TYR A O 1 ATOM 1089 C CB . TYR A 1 147 ? 47.848 1.356 38.281 1.00 1.00 ? 147 TYR A CB 1 ATOM 1090 C CG . TYR A 1 147 ? 47.780 1.930 39.654 1.00 1.00 ? 147 TYR A CG 1 ATOM 1091 C CD1 . TYR A 1 147 ? 47.573 1.064 40.718 1.00 1.00 ? 147 TYR A CD1 1 ATOM 1092 C CD2 . TYR A 1 147 ? 47.950 3.293 39.901 1.00 2.00 ? 147 TYR A CD2 1 ATOM 1093 C CE1 . TYR A 1 147 ? 47.492 1.560 42.012 1.00 1.00 ? 147 TYR A CE1 1 ATOM 1094 C CE2 . TYR A 1 147 ? 47.871 3.804 41.197 1.00 6.74 ? 147 TYR A CE2 1 ATOM 1095 C CZ . TYR A 1 147 ? 47.636 2.925 42.252 1.00 7.72 ? 147 TYR A CZ 1 ATOM 1096 O OH . TYR A 1 147 ? 47.556 3.393 43.542 1.00 1.00 ? 147 TYR A OH 1 ATOM 1097 N N . ALA A 1 148 ? 45.785 2.136 35.819 1.00 24.75 ? 148 ALA A N 1 ATOM 1098 C CA . ALA A 1 148 ? 45.244 3.264 35.083 1.00 9.83 ? 148 ALA A CA 1 ATOM 1099 C C . ALA A 1 148 ? 43.793 3.340 35.384 1.00 9.59 ? 148 ALA A C 1 ATOM 1100 O O . ALA A 1 148 ? 43.159 4.319 35.039 1.00 16.33 ? 148 ALA A O 1 ATOM 1101 C CB . ALA A 1 148 ? 45.509 3.281 33.609 1.00 1.00 ? 148 ALA A CB 1 ATOM 1102 N N . GLY A 1 149 ? 43.292 2.297 36.075 1.00 7.69 ? 149 GLY A N 1 ATOM 1103 C CA . GLY A 1 149 ? 41.890 2.214 36.509 1.00 6.63 ? 149 GLY A CA 1 ATOM 1104 C C . GLY A 1 149 ? 41.600 3.172 37.707 1.00 15.72 ? 149 GLY A C 1 ATOM 1105 O O . GLY A 1 149 ? 40.419 3.274 38.097 1.00 1.00 ? 149 GLY A O 1 ATOM 1106 N N . HIS A 1 150 ? 42.727 3.817 38.237 1.00 11.29 ? 150 HIS A N 1 ATOM 1107 C CA . HIS A 1 150 ? 42.932 4.822 39.325 1.00 2.82 ? 150 HIS A CA 1 ATOM 1108 C C . HIS A 1 150 ? 43.143 6.184 38.621 1.00 13.96 ? 150 HIS A C 1 ATOM 1109 O O . HIS A 1 150 ? 42.372 7.118 38.758 1.00 27.86 ? 150 HIS A O 1 ATOM 1110 C CB . HIS A 1 150 ? 44.247 4.500 40.138 1.00 8.95 ? 150 HIS A CB 1 ATOM 1111 C CG . HIS A 1 150 ? 44.065 3.754 41.466 1.00 10.96 ? 150 HIS A CG 1 ATOM 1112 N ND1 . HIS A 1 150 ? 43.453 2.505 41.551 1.00 7.78 ? 150 HIS A ND1 1 ATOM 1113 C CD2 . HIS A 1 150 ? 44.403 4.106 42.734 1.00 5.90 ? 150 HIS A CD2 1 ATOM 1114 C CE1 . HIS A 1 150 ? 43.415 2.137 42.811 1.00 1.00 ? 150 HIS A CE1 1 ATOM 1115 N NE2 . HIS A 1 150 ? 43.958 3.080 43.549 1.00 3.46 ? 150 HIS A NE2 1 ATOM 1116 N N . TYR A 1 151 ? 44.198 6.245 37.817 1.00 11.25 ? 151 TYR A N 1 ATOM 1117 C CA . TYR A 1 151 ? 44.649 7.363 36.971 1.00 16.85 ? 151 TYR A CA 1 ATOM 1118 C C . TYR A 1 151 ? 43.567 8.040 36.082 1.00 21.79 ? 151 TYR A C 1 ATOM 1119 O O . TYR A 1 151 ? 43.246 9.233 36.140 1.00 15.28 ? 151 TYR A O 1 ATOM 1120 C CB . TYR A 1 151 ? 45.571 6.697 35.938 1.00 16.36 ? 151 TYR A CB 1 ATOM 1121 C CG . TYR A 1 151 ? 46.980 6.317 36.325 1.00 29.68 ? 151 TYR A CG 1 ATOM 1122 C CD1 . TYR A 1 151 ? 47.595 6.760 37.504 1.00 24.22 ? 151 TYR A CD1 1 ATOM 1123 C CD2 . TYR A 1 151 ? 47.720 5.522 35.445 1.00 31.47 ? 151 TYR A CD2 1 ATOM 1124 C CE1 . TYR A 1 151 ? 48.919 6.421 37.811 1.00 12.27 ? 151 TYR A CE1 1 ATOM 1125 C CE2 . TYR A 1 151 ? 49.041 5.175 35.743 1.00 36.44 ? 151 TYR A CE2 1 ATOM 1126 C CZ . TYR A 1 151 ? 49.650 5.624 36.924 1.00 21.04 ? 151 TYR A CZ 1 ATOM 1127 O OH . TYR A 1 151 ? 50.983 5.285 37.211 1.00 5.96 ? 151 TYR A OH 1 ATOM 1128 N N . ILE A 1 152 ? 43.067 7.209 35.179 1.00 16.96 ? 152 ILE A N 1 ATOM 1129 C CA . ILE A 1 152 ? 42.064 7.511 34.175 1.00 17.99 ? 152 ILE A CA 1 ATOM 1130 C C . ILE A 1 152 ? 40.975 8.440 34.673 1.00 21.67 ? 152 ILE A C 1 ATOM 1131 O O . ILE A 1 152 ? 40.898 9.551 34.138 1.00 24.92 ? 152 ILE A O 1 ATOM 1132 C CB . ILE A 1 152 ? 41.469 6.257 33.475 1.00 23.83 ? 152 ILE A CB 1 ATOM 1133 C CG1 . ILE A 1 152 ? 42.382 5.698 32.355 1.00 27.61 ? 152 ILE A CG1 1 ATOM 1134 C CG2 . ILE A 1 152 ? 40.092 6.550 32.901 1.00 19.35 ? 152 ILE A CG2 1 ATOM 1135 C CD1 . ILE A 1 152 ? 41.801 4.528 31.532 1.00 1.00 ? 152 ILE A CD1 1 ATOM 1136 N N . PRO A 1 153 ? 40.146 7.984 35.652 1.00 1.96 ? 153 PRO A N 1 ATOM 1137 C CA . PRO A 1 153 ? 39.066 8.800 36.172 1.00 1.00 ? 153 PRO A CA 1 ATOM 1138 C C . PRO A 1 153 ? 39.590 10.083 36.728 1.00 23.46 ? 153 PRO A C 1 ATOM 1139 O O . PRO A 1 153 ? 39.096 11.193 36.424 1.00 31.37 ? 153 PRO A O 1 ATOM 1140 C CB . PRO A 1 153 ? 38.269 8.027 37.231 1.00 1.00 ? 153 PRO A CB 1 ATOM 1141 C CG . PRO A 1 153 ? 38.760 6.599 37.080 1.00 11.00 ? 153 PRO A CG 1 ATOM 1142 C CD . PRO A 1 153 ? 40.076 6.632 36.266 1.00 7.92 ? 153 PRO A CD 1 ATOM 1143 N N . VAL A 1 154 ? 40.615 9.941 37.528 1.00 8.95 ? 154 VAL A N 1 ATOM 1144 C CA . VAL A 1 154 ? 41.182 11.105 38.102 1.00 1.00 ? 154 VAL A CA 1 ATOM 1145 C C . VAL A 1 154 ? 41.652 12.093 37.063 1.00 6.98 ? 154 VAL A C 1 ATOM 1146 O O . VAL A 1 154 ? 41.394 13.271 37.242 1.00 11.60 ? 154 VAL A O 1 ATOM 1147 C CB . VAL A 1 154 ? 42.220 10.697 39.056 1.00 1.83 ? 154 VAL A CB 1 ATOM 1148 C CG1 . VAL A 1 154 ? 42.621 11.887 39.873 1.00 1.10 ? 154 VAL A CG1 1 ATOM 1149 C CG2 . VAL A 1 154 ? 41.691 9.555 39.941 1.00 4.65 ? 154 VAL A CG2 1 ATOM 1150 N N . PHE A 1 155 ? 42.285 11.602 35.975 1.00 4.29 ? 155 PHE A N 1 ATOM 1151 C CA . PHE A 1 155 ? 42.779 12.460 34.875 1.00 12.07 ? 155 PHE A CA 1 ATOM 1152 C C . PHE A 1 155 ? 41.630 13.006 34.064 1.00 30.38 ? 155 PHE A C 1 ATOM 1153 O O . PHE A 1 155 ? 41.696 14.121 33.588 1.00 28.40 ? 155 PHE A O 1 ATOM 1154 C CB . PHE A 1 155 ? 43.747 11.811 33.886 1.00 8.00 ? 155 PHE A CB 1 ATOM 1155 C CG . PHE A 1 155 ? 44.880 11.201 34.616 1.00 13.90 ? 155 PHE A CG 1 ATOM 1156 C CD1 . PHE A 1 155 ? 45.040 11.366 35.984 1.00 18.87 ? 155 PHE A CD1 1 ATOM 1157 C CD2 . PHE A 1 155 ? 45.837 10.463 33.940 1.00 27.27 ? 155 PHE A CD2 1 ATOM 1158 C CE1 . PHE A 1 155 ? 46.096 10.784 36.677 1.00 18.24 ? 155 PHE A CE1 1 ATOM 1159 C CE2 . PHE A 1 155 ? 46.910 9.891 34.617 1.00 26.12 ? 155 PHE A CE2 1 ATOM 1160 C CZ . PHE A 1 155 ? 47.044 10.039 35.991 1.00 12.42 ? 155 PHE A CZ 1 ATOM 1161 N N . ALA A 1 156 ? 40.604 12.181 33.931 1.00 11.34 ? 156 ALA A N 1 ATOM 1162 C CA . ALA A 1 156 ? 39.409 12.526 33.258 1.00 8.31 ? 156 ALA A CA 1 ATOM 1163 C C . ALA A 1 156 ? 38.748 13.677 33.972 1.00 20.36 ? 156 ALA A C 1 ATOM 1164 O O . ALA A 1 156 ? 38.156 14.529 33.370 1.00 10.51 ? 156 ALA A O 1 ATOM 1165 C CB . ALA A 1 156 ? 38.464 11.382 33.432 1.00 10.30 ? 156 ALA A CB 1 ATOM 1166 N N . SER A 1 157 ? 38.767 13.728 35.282 1.00 26.52 ? 157 SER A N 1 ATOM 1167 C CA . SER A 1 157 ? 38.127 14.904 35.868 1.00 27.23 ? 157 SER A CA 1 ATOM 1168 C C . SER A 1 157 ? 38.954 16.152 35.497 1.00 38.66 ? 157 SER A C 1 ATOM 1169 O O . SER A 1 157 ? 38.494 17.099 34.865 1.00 24.45 ? 157 SER A O 1 ATOM 1170 C CB . SER A 1 157 ? 38.074 14.834 37.377 1.00 19.96 ? 157 SER A CB 1 ATOM 1171 O OG . SER A 1 157 ? 37.043 13.965 37.766 1.00 41.03 ? 157 SER A OG 1 ATOM 1172 N N . GLU A 1 158 ? 40.204 16.078 35.928 1.00 47.26 ? 158 GLU A N 1 ATOM 1173 C CA . GLU A 1 158 ? 41.237 17.070 35.770 1.00 44.37 ? 158 GLU A CA 1 ATOM 1174 C C . GLU A 1 158 ? 41.119 17.828 34.486 1.00 46.16 ? 158 GLU A C 1 ATOM 1175 O O . GLU A 1 158 ? 41.150 19.071 34.436 1.00 43.57 ? 158 GLU A O 1 ATOM 1176 C CB . GLU A 1 158 ? 42.610 16.392 35.813 1.00 42.06 ? 158 GLU A CB 1 ATOM 1177 C CG . GLU A 1 158 ? 43.750 17.408 35.959 1.00 26.14 ? 158 GLU A CG 1 ATOM 1178 C CD . GLU A 1 158 ? 43.473 18.372 37.067 1.00 20.16 ? 158 GLU A CD 1 ATOM 1179 O OE1 . GLU A 1 158 ? 42.637 18.158 37.930 1.00 100.00 ? 158 GLU A OE1 1 ATOM 1180 O OE2 . GLU A 1 158 ? 44.255 19.430 37.057 1.00 34.89 ? 158 GLU A OE2 1 ATOM 1181 N N . ILE A 1 159 ? 40.928 17.027 33.465 1.00 31.94 ? 159 ILE A N 1 ATOM 1182 C CA . ILE A 1 159 ? 40.812 17.563 32.158 1.00 43.85 ? 159 ILE A CA 1 ATOM 1183 C C . ILE A 1 159 ? 39.511 18.337 32.000 1.00 34.43 ? 159 ILE A C 1 ATOM 1184 O O . ILE A 1 159 ? 39.486 19.541 31.724 1.00 24.26 ? 159 ILE A O 1 ATOM 1185 C CB . ILE A 1 159 ? 41.021 16.406 31.206 1.00 66.23 ? 159 ILE A CB 1 ATOM 1186 C CG1 . ILE A 1 159 ? 40.577 16.722 29.807 1.00 76.91 ? 159 ILE A CG1 1 ATOM 1187 C CG2 . ILE A 1 159 ? 40.160 15.262 31.620 1.00 77.29 ? 159 ILE A CG2 1 ATOM 1188 C CD1 . ILE A 1 159 ? 39.970 15.478 29.165 1.00 71.60 ? 159 ILE A CD1 1 ATOM 1189 N N . LEU A 1 160 ? 38.426 17.648 32.219 1.00 29.49 ? 160 LEU A N 1 ATOM 1190 C CA . LEU A 1 160 ? 37.130 18.261 32.141 1.00 24.24 ? 160 LEU A CA 1 ATOM 1191 C C . LEU A 1 160 ? 37.047 19.460 33.067 1.00 47.12 ? 160 LEU A C 1 ATOM 1192 O O . LEU A 1 160 ? 36.151 20.276 32.978 1.00 61.22 ? 160 LEU A O 1 ATOM 1193 C CB . LEU A 1 160 ? 36.068 17.252 32.619 1.00 21.74 ? 160 LEU A CB 1 ATOM 1194 C CG . LEU A 1 160 ? 35.907 15.993 31.730 1.00 36.48 ? 160 LEU A CG 1 ATOM 1195 C CD1 . LEU A 1 160 ? 34.889 14.995 32.319 1.00 42.20 ? 160 LEU A CD1 1 ATOM 1196 C CD2 . LEU A 1 160 ? 35.488 16.327 30.292 1.00 18.94 ? 160 LEU A CD2 1 ATOM 1197 N N . SER A 1 161 ? 37.978 19.566 33.990 1.00 54.23 ? 161 SER A N 1 ATOM 1198 C CA . SER A 1 161 ? 37.929 20.681 34.913 1.00 51.32 ? 161 SER A CA 1 ATOM 1199 C C . SER A 1 161 ? 38.170 21.992 34.267 1.00 38.29 ? 161 SER A C 1 ATOM 1200 O O . SER A 1 161 ? 37.667 23.003 34.739 1.00 37.30 ? 161 SER A O 1 ATOM 1201 C CB . SER A 1 161 ? 38.787 20.545 36.144 1.00 47.61 ? 161 SER A CB 1 ATOM 1202 O OG . SER A 1 161 ? 37.892 20.461 37.230 1.00 30.76 ? 161 SER A OG 1 ATOM 1203 N N . HIS A 1 162 ? 38.929 21.949 33.207 1.00 25.18 ? 162 HIS A N 1 ATOM 1204 C CA . HIS A 1 162 ? 39.229 23.150 32.499 1.00 33.09 ? 162 HIS A CA 1 ATOM 1205 C C . HIS A 1 162 ? 38.236 23.414 31.402 1.00 64.69 ? 162 HIS A C 1 ATOM 1206 O O . HIS A 1 162 ? 38.065 22.578 30.516 1.00 59.61 ? 162 HIS A O 1 ATOM 1207 C CB . HIS A 1 162 ? 40.601 23.073 31.852 1.00 34.27 ? 162 HIS A CB 1 ATOM 1208 C CG . HIS A 1 162 ? 41.633 23.027 32.879 1.00 42.14 ? 162 HIS A CG 1 ATOM 1209 N ND1 . HIS A 1 162 ? 41.487 22.208 33.970 1.00 52.77 ? 162 HIS A ND1 1 ATOM 1210 C CD2 . HIS A 1 162 ? 42.797 23.696 32.971 1.00 50.73 ? 162 HIS A CD2 1 ATOM 1211 C CE1 . HIS A 1 162 ? 42.573 22.380 34.701 1.00 57.47 ? 162 HIS A CE1 1 ATOM 1212 N NE2 . HIS A 1 162 ? 43.382 23.269 34.125 1.00 55.10 ? 162 HIS A NE2 1 ATOM 1213 N N . LYS A 1 163 ? 37.581 24.591 31.473 1.00 80.03 ? 163 LYS A N 1 ATOM 1214 C CA . LYS A 1 163 ? 36.629 24.992 30.435 1.00 80.17 ? 163 LYS A CA 1 ATOM 1215 C C . LYS A 1 163 ? 37.487 25.721 29.426 1.00 67.24 ? 163 LYS A C 1 ATOM 1216 O O . LYS A 1 163 ? 37.175 25.887 28.237 1.00 63.05 ? 163 LYS A O 1 ATOM 1217 C CB . LYS A 1 163 ? 35.445 25.808 30.922 1.00 76.88 ? 163 LYS A CB 1 ATOM 1218 C CG . LYS A 1 163 ? 34.455 24.952 31.702 1.00 84.94 ? 163 LYS A CG 1 ATOM 1219 C CD . LYS A 1 163 ? 33.193 24.580 30.929 1.00 66.62 ? 163 LYS A CD 1 ATOM 1220 C CE . LYS A 1 163 ? 32.500 23.338 31.484 1.00 79.75 ? 163 LYS A CE 1 ATOM 1221 N NZ . LYS A 1 163 ? 31.316 23.624 32.312 1.00 100.00 ? 163 LYS A NZ 1 ATOM 1222 N N . ASP A 1 164 ? 38.618 26.072 30.028 1.00 54.64 ? 164 ASP A N 1 ATOM 1223 C CA . ASP A 1 164 ? 39.781 26.753 29.503 1.00 63.99 ? 164 ASP A CA 1 ATOM 1224 C C . ASP A 1 164 ? 40.387 25.980 28.302 1.00 69.26 ? 164 ASP A C 1 ATOM 1225 O O . ASP A 1 164 ? 40.959 26.563 27.389 1.00 58.84 ? 164 ASP A O 1 ATOM 1226 C CB . ASP A 1 164 ? 40.780 26.757 30.721 1.00 72.58 ? 164 ASP A CB 1 ATOM 1227 C CG . ASP A 1 164 ? 41.992 27.692 30.738 1.00 100.00 ? 164 ASP A CG 1 ATOM 1228 O OD1 . ASP A 1 164 ? 41.922 28.920 30.810 1.00 100.00 ? 164 ASP A OD1 1 ATOM 1229 O OD2 . ASP A 1 164 ? 43.115 27.042 30.997 1.00 100.00 ? 164 ASP A OD2 1 ATOM 1230 N N . ARG A 1 165 ? 40.242 24.644 28.330 1.00 70.59 ? 165 ARG A N 1 ATOM 1231 C CA . ARG A 1 165 ? 40.747 23.673 27.365 1.00 56.20 ? 165 ARG A CA 1 ATOM 1232 C C . ARG A 1 165 ? 40.917 23.983 25.913 1.00 54.25 ? 165 ARG A C 1 ATOM 1233 O O . ARG A 1 165 ? 40.098 24.637 25.250 1.00 58.71 ? 165 ARG A O 1 ATOM 1234 C CB . ARG A 1 165 ? 40.223 22.256 27.529 1.00 45.52 ? 165 ARG A CB 1 ATOM 1235 C CG . ARG A 1 165 ? 38.709 22.143 27.498 1.00 57.15 ? 165 ARG A CG 1 ATOM 1236 C CD . ARG A 1 165 ? 38.265 20.894 28.281 1.00 61.46 ? 165 ARG A CD 1 ATOM 1237 N NE . ARG A 1 165 ? 36.886 20.871 28.790 1.00 45.02 ? 165 ARG A NE 1 ATOM 1238 C CZ . ARG A 1 165 ? 35.852 20.442 28.050 1.00 100.00 ? 165 ARG A CZ 1 ATOM 1239 N NH1 . ARG A 1 165 ? 36.016 20.027 26.799 1.00 100.00 ? 165 ARG A NH1 1 ATOM 1240 N NH2 . ARG A 1 165 ? 34.623 20.422 28.571 1.00 75.10 ? 165 ARG A NH2 1 ATOM 1241 N N . ASN A 1 166 ? 42.029 23.394 25.462 1.00 53.28 ? 166 ASN A N 1 ATOM 1242 C CA . ASN A 1 166 ? 42.556 23.401 24.096 1.00 57.47 ? 166 ASN A CA 1 ATOM 1243 C C . ASN A 1 166 ? 42.203 22.050 23.366 1.00 62.25 ? 166 ASN A C 1 ATOM 1244 O O . ASN A 1 166 ? 42.776 21.596 22.358 1.00 59.05 ? 166 ASN A O 1 ATOM 1245 C CB . ASN A 1 166 ? 44.078 23.794 24.096 1.00 44.42 ? 166 ASN A CB 1 ATOM 1246 C CG . ASN A 1 166 ? 45.047 22.873 23.337 1.00 82.71 ? 166 ASN A CG 1 ATOM 1247 O OD1 . ASN A 1 166 ? 45.163 21.658 23.605 1.00 85.15 ? 166 ASN A OD1 1 ATOM 1248 N ND2 . ASN A 1 166 ? 45.627 23.392 22.259 1.00 100.00 ? 166 ASN A ND2 1 ATOM 1249 N N . PHE A 1 167 ? 41.194 21.354 23.884 1.00 59.24 ? 167 PHE A N 1 ATOM 1250 C CA . PHE A 1 167 ? 40.788 20.085 23.282 1.00 53.67 ? 167 PHE A CA 1 ATOM 1251 C C . PHE A 1 167 ? 39.514 19.513 23.890 1.00 51.11 ? 167 PHE A C 1 ATOM 1252 O O . PHE A 1 167 ? 38.997 20.047 24.882 1.00 49.55 ? 167 PHE A O 1 ATOM 1253 C CB . PHE A 1 167 ? 41.930 19.046 23.175 1.00 54.46 ? 167 PHE A CB 1 ATOM 1254 C CG . PHE A 1 167 ? 42.660 18.779 24.479 1.00 49.72 ? 167 PHE A CG 1 ATOM 1255 C CD1 . PHE A 1 167 ? 43.689 19.626 24.904 1.00 39.47 ? 167 PHE A CD1 1 ATOM 1256 C CD2 . PHE A 1 167 ? 42.342 17.654 25.244 1.00 40.95 ? 167 PHE A CD2 1 ATOM 1257 C CE1 . PHE A 1 167 ? 44.379 19.402 26.096 1.00 42.53 ? 167 PHE A CE1 1 ATOM 1258 C CE2 . PHE A 1 167 ? 43.029 17.419 26.433 1.00 41.01 ? 167 PHE A CE2 1 ATOM 1259 C CZ . PHE A 1 167 ? 44.043 18.284 26.857 1.00 38.93 ? 167 PHE A CZ 1 ATOM 1260 N N . ASN A 1 168 ? 39.026 18.424 23.266 1.00 59.56 ? 168 ASN A N 1 ATOM 1261 C CA . ASN A 1 168 ? 37.798 17.696 23.657 1.00 62.59 ? 168 ASN A CA 1 ATOM 1262 C C . ASN A 1 168 ? 37.985 16.115 23.897 1.00 62.29 ? 168 ASN A C 1 ATOM 1263 O O . ASN A 1 168 ? 38.581 15.324 23.127 1.00 69.12 ? 168 ASN A O 1 ATOM 1264 C CB . ASN A 1 168 ? 36.623 18.082 22.695 1.00 31.33 ? 168 ASN A CB 1 ATOM 1265 C CG . ASN A 1 168 ? 35.724 19.281 23.060 1.00 78.32 ? 168 ASN A CG 1 ATOM 1266 O OD1 . ASN A 1 168 ? 34.700 19.141 23.766 1.00 44.28 ? 168 ASN A OD1 1 ATOM 1267 N ND2 . ASN A 1 168 ? 35.951 20.413 22.378 1.00 100.00 ? 168 ASN A ND2 1 ATOM 1268 N N . LEU A 1 169 ? 37.466 15.635 25.016 1.00 26.35 ? 169 LEU A N 1 ATOM 1269 C CA . LEU A 1 169 ? 37.560 14.252 25.383 1.00 26.46 ? 169 LEU A CA 1 ATOM 1270 C C . LEU A 1 169 ? 36.225 13.593 25.087 1.00 26.65 ? 169 LEU A C 1 ATOM 1271 O O . LEU A 1 169 ? 35.169 14.054 25.512 1.00 41.81 ? 169 LEU A O 1 ATOM 1272 C CB . LEU A 1 169 ? 37.994 14.158 26.885 1.00 33.56 ? 169 LEU A CB 1 ATOM 1273 C CG . LEU A 1 169 ? 37.845 12.813 27.639 1.00 26.47 ? 169 LEU A CG 1 ATOM 1274 C CD1 . LEU A 1 169 ? 39.126 11.954 27.552 1.00 4.72 ? 169 LEU A CD1 1 ATOM 1275 C CD2 . LEU A 1 169 ? 37.519 13.132 29.106 1.00 1.29 ? 169 LEU A CD2 1 ATOM 1276 N N . THR A 1 170 ? 36.248 12.503 24.360 1.00 16.82 ? 170 THR A N 1 ATOM 1277 C CA . THR A 1 170 ? 34.996 11.854 24.002 1.00 19.67 ? 170 THR A CA 1 ATOM 1278 C C . THR A 1 170 ? 34.520 10.622 24.815 1.00 27.51 ? 170 THR A C 1 ATOM 1279 O O . THR A 1 170 ? 33.292 10.445 25.009 1.00 20.54 ? 170 THR A O 1 ATOM 1280 C CB . THR A 1 170 ? 35.078 11.580 22.516 1.00 34.26 ? 170 THR A CB 1 ATOM 1281 O OG1 . THR A 1 170 ? 35.975 12.531 21.976 1.00 41.14 ? 170 THR A OG1 1 ATOM 1282 C CG2 . THR A 1 170 ? 33.703 11.776 21.941 1.00 34.03 ? 170 THR A CG2 1 ATOM 1283 N N . SER A 1 171 ? 35.475 9.775 25.267 1.00 25.55 ? 171 SER A N 1 ATOM 1284 C CA . SER A 1 171 ? 35.174 8.591 26.073 1.00 25.55 ? 171 SER A CA 1 ATOM 1285 C C . SER A 1 171 ? 36.427 8.061 26.768 1.00 24.55 ? 171 SER A C 1 ATOM 1286 O O . SER A 1 171 ? 37.581 8.565 26.525 1.00 12.71 ? 171 SER A O 1 ATOM 1287 C CB . SER A 1 171 ? 34.458 7.495 25.275 1.00 40.96 ? 171 SER A CB 1 ATOM 1288 O OG . SER A 1 171 ? 35.351 6.634 24.553 1.00 40.91 ? 171 SER A OG 1 ATOM 1289 N N . VAL A 1 172 ? 36.166 7.040 27.622 1.00 17.98 ? 172 VAL A N 1 ATOM 1290 C CA . VAL A 1 172 ? 37.224 6.343 28.381 1.00 24.76 ? 172 VAL A CA 1 ATOM 1291 C C . VAL A 1 172 ? 37.213 4.830 28.354 1.00 12.39 ? 172 VAL A C 1 ATOM 1292 O O . VAL A 1 172 ? 36.232 4.123 28.594 1.00 20.41 ? 172 VAL A O 1 ATOM 1293 C CB . VAL A 1 172 ? 37.364 6.728 29.838 1.00 33.12 ? 172 VAL A CB 1 ATOM 1294 C CG1 . VAL A 1 172 ? 37.993 8.107 29.917 1.00 36.21 ? 172 VAL A CG1 1 ATOM 1295 C CG2 . VAL A 1 172 ? 35.993 6.660 30.515 1.00 29.77 ? 172 VAL A CG2 1 ATOM 1296 N N . LEU A 1 173 ? 38.361 4.302 28.123 1.00 12.63 ? 173 LEU A N 1 ATOM 1297 C CA . LEU A 1 173 ? 38.444 2.877 28.112 1.00 17.13 ? 173 LEU A CA 1 ATOM 1298 C C . LEU A 1 173 ? 39.335 2.399 29.249 1.00 19.07 ? 173 LEU A C 1 ATOM 1299 O O . LEU A 1 173 ? 40.477 2.876 29.429 1.00 14.20 ? 173 LEU A O 1 ATOM 1300 C CB . LEU A 1 173 ? 38.853 2.397 26.726 1.00 21.07 ? 173 LEU A CB 1 ATOM 1301 C CG . LEU A 1 173 ? 37.634 2.455 25.822 1.00 30.24 ? 173 LEU A CG 1 ATOM 1302 C CD1 . LEU A 1 173 ? 37.793 3.659 24.886 1.00 34.43 ? 173 LEU A CD1 1 ATOM 1303 C CD2 . LEU A 1 173 ? 37.482 1.121 25.076 1.00 17.50 ? 173 LEU A CD2 1 ATOM 1304 N N . ILE A 1 174 ? 38.807 1.461 30.049 1.00 12.13 ? 174 ILE A N 1 ATOM 1305 C CA . ILE A 1 174 ? 39.621 0.959 31.166 1.00 19.59 ? 174 ILE A CA 1 ATOM 1306 C C . ILE A 1 174 ? 39.760 -0.564 31.141 1.00 23.62 ? 174 ILE A C 1 ATOM 1307 O O . ILE A 1 174 ? 38.798 -1.279 31.380 1.00 31.13 ? 174 ILE A O 1 ATOM 1308 C CB . ILE A 1 174 ? 39.117 1.460 32.523 1.00 27.02 ? 174 ILE A CB 1 ATOM 1309 C CG1 . ILE A 1 174 ? 39.461 2.925 32.711 1.00 31.88 ? 174 ILE A CG1 1 ATOM 1310 C CG2 . ILE A 1 174 ? 39.764 0.689 33.660 1.00 40.07 ? 174 ILE A CG2 1 ATOM 1311 C CD1 . ILE A 1 174 ? 38.621 3.565 33.806 1.00 1.00 ? 174 ILE A CD1 1 ATOM 1312 N N . GLY A 1 175 ? 40.946 -1.083 30.877 1.00 20.12 ? 175 GLY A N 1 ATOM 1313 C CA . GLY A 1 175 ? 41.069 -2.532 30.862 1.00 16.12 ? 175 GLY A CA 1 ATOM 1314 C C . GLY A 1 175 ? 41.803 -3.147 32.069 1.00 21.39 ? 175 GLY A C 1 ATOM 1315 O O . GLY A 1 175 ? 42.925 -2.749 32.404 1.00 20.99 ? 175 GLY A O 1 ATOM 1316 N N . ASN A 1 176 ? 41.148 -4.132 32.695 1.00 3.02 ? 176 ASN A N 1 ATOM 1317 C CA . ASN A 1 176 ? 41.664 -4.877 33.858 1.00 6.19 ? 176 ASN A CA 1 ATOM 1318 C C . ASN A 1 176 ? 42.377 -3.963 34.842 1.00 29.39 ? 176 ASN A C 1 ATOM 1319 O O . ASN A 1 176 ? 43.550 -4.165 35.182 1.00 19.36 ? 176 ASN A O 1 ATOM 1320 C CB . ASN A 1 176 ? 42.501 -6.117 33.444 1.00 12.87 ? 176 ASN A CB 1 ATOM 1321 C CG . ASN A 1 176 ? 41.730 -7.221 32.685 1.00 1.92 ? 176 ASN A CG 1 ATOM 1322 O OD1 . ASN A 1 176 ? 41.756 -7.299 31.467 1.00 21.89 ? 176 ASN A OD1 1 ATOM 1323 N ND2 . ASN A 1 176 ? 41.089 -8.135 33.384 1.00 1.00 ? 176 ASN A ND2 1 ATOM 1324 N N . GLY A 1 177 ? 41.625 -2.925 35.260 1.00 30.89 ? 177 GLY A N 1 ATOM 1325 C CA . GLY A 1 177 ? 42.121 -1.910 36.165 1.00 19.84 ? 177 GLY A CA 1 ATOM 1326 C C . GLY A 1 177 ? 41.624 -1.980 37.613 1.00 16.53 ? 177 GLY A C 1 ATOM 1327 O O . GLY A 1 177 ? 40.635 -2.625 37.946 1.00 12.02 ? 177 GLY A O 1 ATOM 1328 N N . LEU A 1 178 ? 42.365 -1.298 38.488 1.00 7.77 ? 178 LEU A N 1 ATOM 1329 C CA . LEU A 1 178 ? 42.037 -1.191 39.888 1.00 5.33 ? 178 LEU A CA 1 ATOM 1330 C C . LEU A 1 178 ? 41.240 0.107 39.992 1.00 13.74 ? 178 LEU A C 1 ATOM 1331 O O . LEU A 1 178 ? 41.797 1.176 39.698 1.00 6.82 ? 178 LEU A O 1 ATOM 1332 C CB . LEU A 1 178 ? 43.295 -1.102 40.784 1.00 1.00 ? 178 LEU A CB 1 ATOM 1333 C CG . LEU A 1 178 ? 42.966 -1.591 42.185 1.00 2.09 ? 178 LEU A CG 1 ATOM 1334 C CD1 . LEU A 1 178 ? 42.055 -2.800 42.141 1.00 1.00 ? 178 LEU A CD1 1 ATOM 1335 C CD2 . LEU A 1 178 ? 44.212 -1.981 42.898 1.00 11.50 ? 178 LEU A CD2 1 ATOM 1336 N N . THR A 1 179 ? 39.956 0.040 40.362 1.00 5.20 ? 179 THR A N 1 ATOM 1337 C CA . THR A 1 179 ? 39.171 1.274 40.426 1.00 5.79 ? 179 THR A CA 1 ATOM 1338 C C . THR A 1 179 ? 38.449 1.547 41.742 1.00 5.45 ? 179 THR A C 1 ATOM 1339 O O . THR A 1 179 ? 38.595 2.636 42.295 1.00 1.00 ? 179 THR A O 1 ATOM 1340 C CB . THR A 1 179 ? 38.275 1.493 39.186 1.00 6.69 ? 179 THR A CB 1 ATOM 1341 O OG1 . THR A 1 179 ? 38.986 1.368 37.956 1.00 15.06 ? 179 THR A OG1 1 ATOM 1342 C CG2 . THR A 1 179 ? 37.598 2.842 39.271 1.00 1.00 ? 179 THR A CG2 1 ATOM 1343 N N . ASP A 1 180 ? 37.695 0.546 42.221 1.00 1.00 ? 180 ASP A N 1 ATOM 1344 C CA . ASP A 1 180 ? 36.955 0.624 43.466 1.00 3.34 ? 180 ASP A CA 1 ATOM 1345 C C . ASP A 1 180 ? 37.276 -0.579 44.397 1.00 18.84 ? 180 ASP A C 1 ATOM 1346 O O . ASP A 1 180 ? 36.495 -1.550 44.615 1.00 4.18 ? 180 ASP A O 1 ATOM 1347 C CB . ASP A 1 180 ? 35.514 1.099 43.313 1.00 1.00 ? 180 ASP A CB 1 ATOM 1348 C CG . ASP A 1 180 ? 34.536 0.370 44.175 1.00 6.20 ? 180 ASP A CG 1 ATOM 1349 O OD1 . ASP A 1 180 ? 34.701 0.620 45.428 1.00 13.14 ? 180 ASP A OD1 1 ATOM 1350 O OD2 . ASP A 1 180 ? 33.849 -0.543 43.773 1.00 32.01 ? 180 ASP A OD2 1 ATOM 1351 N N . PRO A 1 181 ? 38.518 -0.469 44.925 1.00 4.75 ? 181 PRO A N 1 ATOM 1352 C CA . PRO A 1 181 ? 39.092 -1.465 45.751 1.00 3.33 ? 181 PRO A CA 1 ATOM 1353 C C . PRO A 1 181 ? 38.164 -2.030 46.784 1.00 18.15 ? 181 PRO A C 1 ATOM 1354 O O . PRO A 1 181 ? 38.116 -3.228 47.071 1.00 13.75 ? 181 PRO A O 1 ATOM 1355 C CB . PRO A 1 181 ? 40.304 -0.806 46.371 1.00 1.00 ? 181 PRO A CB 1 ATOM 1356 C CG . PRO A 1 181 ? 40.503 0.522 45.715 1.00 1.00 ? 181 PRO A CG 1 ATOM 1357 C CD . PRO A 1 181 ? 39.252 0.825 45.003 1.00 1.00 ? 181 PRO A CD 1 ATOM 1358 N N . LEU A 1 182 ? 37.403 -1.128 47.339 1.00 31.13 ? 182 LEU A N 1 ATOM 1359 C CA . LEU A 1 182 ? 36.491 -1.519 48.378 1.00 26.74 ? 182 LEU A CA 1 ATOM 1360 C C . LEU A 1 182 ? 35.545 -2.591 47.946 1.00 20.36 ? 182 LEU A C 1 ATOM 1361 O O . LEU A 1 182 ? 35.200 -3.470 48.689 1.00 20.86 ? 182 LEU A O 1 ATOM 1362 C CB . LEU A 1 182 ? 35.715 -0.359 48.991 1.00 20.99 ? 182 LEU A CB 1 ATOM 1363 C CG . LEU A 1 182 ? 34.717 -0.911 49.997 1.00 14.46 ? 182 LEU A CG 1 ATOM 1364 C CD1 . LEU A 1 182 ? 35.485 -1.669 51.079 1.00 13.88 ? 182 LEU A CD1 1 ATOM 1365 C CD2 . LEU A 1 182 ? 33.952 0.233 50.639 1.00 1.00 ? 182 LEU A CD2 1 ATOM 1366 N N . THR A 1 183 ? 35.138 -2.488 46.721 1.00 12.47 ? 183 THR A N 1 ATOM 1367 C CA . THR A 1 183 ? 34.230 -3.431 46.208 1.00 1.99 ? 183 THR A CA 1 ATOM 1368 C C . THR A 1 183 ? 34.926 -4.606 45.514 1.00 14.32 ? 183 THR A C 1 ATOM 1369 O O . THR A 1 183 ? 34.638 -5.764 45.784 1.00 14.62 ? 183 THR A O 1 ATOM 1370 C CB . THR A 1 183 ? 33.170 -2.683 45.431 1.00 11.93 ? 183 THR A CB 1 ATOM 1371 O OG1 . THR A 1 183 ? 32.124 -2.353 46.333 1.00 41.21 ? 183 THR A OG1 1 ATOM 1372 C CG2 . THR A 1 183 ? 32.669 -3.508 44.251 1.00 33.78 ? 183 THR A CG2 1 ATOM 1373 N N . GLN A 1 184 ? 35.894 -4.325 44.651 1.00 8.59 ? 184 GLN A N 1 ATOM 1374 C CA . GLN A 1 184 ? 36.634 -5.362 43.938 1.00 1.34 ? 184 GLN A CA 1 ATOM 1375 C C . GLN A 1 184 ? 37.377 -6.405 44.816 1.00 13.49 ? 184 GLN A C 1 ATOM 1376 O O . GLN A 1 184 ? 37.582 -7.590 44.455 1.00 16.74 ? 184 GLN A O 1 ATOM 1377 C CB . GLN A 1 184 ? 37.575 -4.629 42.986 1.00 1.12 ? 184 GLN A CB 1 ATOM 1378 C CG . GLN A 1 184 ? 36.901 -3.444 42.238 1.00 8.53 ? 184 GLN A CG 1 ATOM 1379 C CD . GLN A 1 184 ? 37.824 -2.800 41.190 1.00 14.61 ? 184 GLN A CD 1 ATOM 1380 O OE1 . GLN A 1 184 ? 37.986 -1.579 41.198 1.00 15.62 ? 184 GLN A OE1 1 ATOM 1381 N NE2 . GLN A 1 184 ? 38.528 -3.605 40.373 1.00 1.00 ? 184 GLN A NE2 1 ATOM 1382 N N . TYR A 1 185 ? 37.788 -5.944 45.980 1.00 10.32 ? 185 TYR A N 1 ATOM 1383 C CA . TYR A 1 185 ? 38.503 -6.737 46.938 1.00 3.10 ? 185 TYR A CA 1 ATOM 1384 C C . TYR A 1 185 ? 37.830 -8.043 47.390 1.00 13.52 ? 185 TYR A C 1 ATOM 1385 O O . TYR A 1 185 ? 38.478 -9.057 47.706 1.00 15.27 ? 185 TYR A O 1 ATOM 1386 C CB . TYR A 1 185 ? 39.135 -5.852 48.029 1.00 9.84 ? 185 TYR A CB 1 ATOM 1387 C CG . TYR A 1 185 ? 40.598 -5.580 47.667 1.00 11.08 ? 185 TYR A CG 1 ATOM 1388 C CD1 . TYR A 1 185 ? 40.971 -4.574 46.769 1.00 8.84 ? 185 TYR A CD1 1 ATOM 1389 C CD2 . TYR A 1 185 ? 41.621 -6.374 48.197 1.00 13.71 ? 185 TYR A CD2 1 ATOM 1390 C CE1 . TYR A 1 185 ? 42.320 -4.365 46.440 1.00 9.53 ? 185 TYR A CE1 1 ATOM 1391 C CE2 . TYR A 1 185 ? 42.974 -6.191 47.873 1.00 8.47 ? 185 TYR A CE2 1 ATOM 1392 C CZ . TYR A 1 185 ? 43.327 -5.182 46.976 1.00 21.11 ? 185 TYR A CZ 1 ATOM 1393 O OH . TYR A 1 185 ? 44.665 -5.027 46.640 1.00 4.18 ? 185 TYR A OH 1 ATOM 1394 N N . ASN A 1 186 ? 36.525 -8.102 47.428 1.00 2.82 ? 186 ASN A N 1 ATOM 1395 C CA . ASN A 1 186 ? 35.972 -9.400 47.832 1.00 1.00 ? 186 ASN A CA 1 ATOM 1396 C C . ASN A 1 186 ? 36.036 -10.377 46.678 1.00 3.34 ? 186 ASN A C 1 ATOM 1397 O O . ASN A 1 186 ? 35.840 -11.539 46.881 1.00 13.85 ? 186 ASN A O 1 ATOM 1398 C CB . ASN A 1 186 ? 34.512 -9.404 48.312 1.00 1.00 ? 186 ASN A CB 1 ATOM 1399 C CG . ASN A 1 186 ? 33.812 -8.109 48.012 1.00 9.60 ? 186 ASN A CG 1 ATOM 1400 O OD1 . ASN A 1 186 ? 33.487 -7.357 48.934 1.00 41.41 ? 186 ASN A OD1 1 ATOM 1401 N ND2 . ASN A 1 186 ? 33.864 -7.724 46.743 1.00 62.21 ? 186 ASN A ND2 1 ATOM 1402 N N . TYR A 1 187 ? 36.294 -9.908 45.470 1.00 1.22 ? 187 TYR A N 1 ATOM 1403 C CA . TYR A 1 187 ? 36.330 -10.828 44.383 1.00 1.64 ? 187 TYR A CA 1 ATOM 1404 C C . TYR A 1 187 ? 37.593 -11.624 44.288 1.00 17.96 ? 187 TYR A C 1 ATOM 1405 O O . TYR A 1 187 ? 37.843 -12.356 43.349 1.00 21.99 ? 187 TYR A O 1 ATOM 1406 C CB . TYR A 1 187 ? 35.689 -10.309 43.081 1.00 14.23 ? 187 TYR A CB 1 ATOM 1407 C CG . TYR A 1 187 ? 34.278 -9.945 43.463 1.00 20.79 ? 187 TYR A CG 1 ATOM 1408 C CD1 . TYR A 1 187 ? 33.322 -10.942 43.686 1.00 13.39 ? 187 TYR A CD1 1 ATOM 1409 C CD2 . TYR A 1 187 ? 33.898 -8.620 43.681 1.00 24.46 ? 187 TYR A CD2 1 ATOM 1410 C CE1 . TYR A 1 187 ? 32.015 -10.669 44.109 1.00 3.28 ? 187 TYR A CE1 1 ATOM 1411 C CE2 . TYR A 1 187 ? 32.588 -8.321 44.068 1.00 29.35 ? 187 TYR A CE2 1 ATOM 1412 C CZ . TYR A 1 187 ? 31.648 -9.336 44.288 1.00 35.05 ? 187 TYR A CZ 1 ATOM 1413 O OH . TYR A 1 187 ? 30.376 -9.035 44.721 1.00 23.83 ? 187 TYR A OH 1 ATOM 1414 N N . TYR A 1 188 ? 38.401 -11.525 45.317 1.00 18.56 ? 188 TYR A N 1 ATOM 1415 C CA . TYR A 1 188 ? 39.655 -12.287 45.316 1.00 12.54 ? 188 TYR A CA 1 ATOM 1416 C C . TYR A 1 188 ? 39.456 -13.794 45.571 1.00 17.78 ? 188 TYR A C 1 ATOM 1417 O O . TYR A 1 188 ? 39.916 -14.568 44.778 1.00 21.50 ? 188 TYR A O 1 ATOM 1418 C CB . TYR A 1 188 ? 40.761 -11.612 46.161 1.00 4.19 ? 188 TYR A CB 1 ATOM 1419 C CG . TYR A 1 188 ? 41.283 -10.414 45.405 1.00 4.47 ? 188 TYR A CG 1 ATOM 1420 C CD1 . TYR A 1 188 ? 41.777 -10.655 44.124 1.00 8.02 ? 188 TYR A CD1 1 ATOM 1421 C CD2 . TYR A 1 188 ? 41.233 -9.101 45.874 1.00 1.00 ? 188 TYR A CD2 1 ATOM 1422 C CE1 . TYR A 1 188 ? 42.262 -9.635 43.308 1.00 6.37 ? 188 TYR A CE1 1 ATOM 1423 C CE2 . TYR A 1 188 ? 41.694 -8.075 45.047 1.00 11.23 ? 188 TYR A CE2 1 ATOM 1424 C CZ . TYR A 1 188 ? 42.204 -8.329 43.767 1.00 5.36 ? 188 TYR A CZ 1 ATOM 1425 O OH . TYR A 1 188 ? 42.684 -7.329 42.952 1.00 1.02 ? 188 TYR A OH 1 ATOM 1426 N N . GLU A 1 189 ? 38.746 -14.190 46.648 1.00 6.25 ? 189 GLU A N 1 ATOM 1427 C CA . GLU A 1 189 ? 38.473 -15.566 47.021 1.00 8.20 ? 189 GLU A CA 1 ATOM 1428 C C . GLU A 1 189 ? 37.699 -16.306 45.937 1.00 21.81 ? 189 GLU A C 1 ATOM 1429 O O . GLU A 1 189 ? 38.109 -17.353 45.450 1.00 20.87 ? 189 GLU A O 1 ATOM 1430 C CB . GLU A 1 189 ? 37.784 -15.622 48.410 1.00 15.92 ? 189 GLU A CB 1 ATOM 1431 C CG . GLU A 1 189 ? 37.733 -17.007 49.077 1.00 13.20 ? 189 GLU A CG 1 ATOM 1432 C CD . GLU A 1 189 ? 36.591 -17.903 48.603 1.00 86.90 ? 189 GLU A CD 1 ATOM 1433 O OE1 . GLU A 1 189 ? 35.532 -17.434 48.229 1.00 61.43 ? 189 GLU A OE1 1 ATOM 1434 O OE2 . GLU A 1 189 ? 36.812 -19.226 48.712 1.00 43.24 ? 189 GLU A OE2 1 ATOM 1435 N N . PRO A 1 190 ? 36.589 -15.748 45.533 1.00 18.42 ? 190 PRO A N 1 ATOM 1436 C CA . PRO A 1 190 ? 35.769 -16.333 44.499 1.00 17.27 ? 190 PRO A CA 1 ATOM 1437 C C . PRO A 1 190 ? 36.519 -16.674 43.252 1.00 25.05 ? 190 PRO A C 1 ATOM 1438 O O . PRO A 1 190 ? 36.471 -17.792 42.757 1.00 40.76 ? 190 PRO A O 1 ATOM 1439 C CB . PRO A 1 190 ? 34.700 -15.295 44.191 1.00 21.53 ? 190 PRO A CB 1 ATOM 1440 C CG . PRO A 1 190 ? 34.616 -14.435 45.469 1.00 29.47 ? 190 PRO A CG 1 ATOM 1441 C CD . PRO A 1 190 ? 35.879 -14.701 46.290 1.00 15.34 ? 190 PRO A CD 1 ATOM 1442 N N . MET A 1 191 ? 37.215 -15.709 42.725 1.00 13.67 ? 191 MET A N 1 ATOM 1443 C CA . MET A 1 191 ? 37.981 -15.975 41.508 1.00 13.39 ? 191 MET A CA 1 ATOM 1444 C C . MET A 1 191 ? 39.085 -17.015 41.600 1.00 23.68 ? 191 MET A C 1 ATOM 1445 O O . MET A 1 191 ? 39.469 -17.578 40.584 1.00 28.65 ? 191 MET A O 1 ATOM 1446 C CB . MET A 1 191 ? 38.743 -14.709 41.120 1.00 16.68 ? 191 MET A CB 1 ATOM 1447 C CG . MET A 1 191 ? 39.425 -14.793 39.791 1.00 23.07 ? 191 MET A CG 1 ATOM 1448 S SD . MET A 1 191 ? 38.229 -14.811 38.420 1.00 39.00 ? 191 MET A SD 1 ATOM 1449 C CE . MET A 1 191 ? 39.182 -13.881 37.178 1.00 25.40 ? 191 MET A CE 1 ATOM 1450 N N . ALA A 1 192 ? 39.682 -17.219 42.776 1.00 22.73 ? 192 ALA A N 1 ATOM 1451 C CA . ALA A 1 192 ? 40.783 -18.179 42.873 1.00 22.13 ? 192 ALA A CA 1 ATOM 1452 C C . ALA A 1 192 ? 40.328 -19.541 43.375 1.00 25.96 ? 192 ALA A C 1 ATOM 1453 O O . ALA A 1 192 ? 41.001 -20.611 43.179 1.00 15.62 ? 192 ALA A O 1 ATOM 1454 C CB . ALA A 1 192 ? 42.001 -17.611 43.594 1.00 18.95 ? 192 ALA A CB 1 ATOM 1455 N N . CYS A 1 193 ? 39.156 -19.438 44.016 1.00 15.86 ? 193 CYS A N 1 ATOM 1456 C CA . CYS A 1 193 ? 38.438 -20.551 44.608 1.00 20.96 ? 193 CYS A CA 1 ATOM 1457 C C . CYS A 1 193 ? 37.408 -21.238 43.754 1.00 33.77 ? 193 CYS A C 1 ATOM 1458 O O . CYS A 1 193 ? 36.457 -21.860 44.264 1.00 28.00 ? 193 CYS A O 1 ATOM 1459 C CB . CYS A 1 193 ? 38.107 -20.526 46.097 1.00 18.27 ? 193 CYS A CB 1 ATOM 1460 S SG . CYS A 1 193 ? 39.556 -19.927 46.948 1.00 19.35 ? 193 CYS A SG 1 ATOM 1461 N N . GLY A 1 194 ? 37.630 -21.124 42.452 1.00 19.54 ? 194 GLY A N 1 ATOM 1462 C CA . GLY A 1 194 ? 36.805 -21.815 41.513 1.00 22.03 ? 194 GLY A CA 1 ATOM 1463 C C . GLY A 1 194 ? 35.488 -21.288 41.169 1.00 37.04 ? 194 GLY A C 1 ATOM 1464 O O . GLY A 1 194 ? 34.549 -22.080 41.081 1.00 44.99 ? 194 GLY A O 1 ATOM 1465 N N . GLU A 1 195 ? 35.404 -19.996 40.924 1.00 37.01 ? 195 GLU A N 1 ATOM 1466 C CA . GLU A 1 195 ? 34.099 -19.464 40.545 1.00 24.44 ? 195 GLU A CA 1 ATOM 1467 C C . GLU A 1 195 ? 34.109 -18.443 39.444 1.00 14.38 ? 195 GLU A C 1 ATOM 1468 O O . GLU A 1 195 ? 33.260 -17.607 39.580 1.00 6.84 ? 195 GLU A O 1 ATOM 1469 C CB . GLU A 1 195 ? 33.347 -18.754 41.689 1.00 19.07 ? 195 GLU A CB 1 ATOM 1470 C CG . GLU A 1 195 ? 33.606 -19.275 43.115 1.00 43.44 ? 195 GLU A CG 1 ATOM 1471 C CD . GLU A 1 195 ? 32.508 -18.858 44.078 1.00 29.05 ? 195 GLU A CD 1 ATOM 1472 O OE1 . GLU A 1 195 ? 31.351 -18.697 43.741 1.00 97.22 ? 195 GLU A OE1 1 ATOM 1473 O OE2 . GLU A 1 195 ? 32.927 -18.706 45.315 1.00 92.38 ? 195 GLU A OE2 1 ATOM 1474 N N . GLY A 1 196 ? 34.993 -18.455 38.401 1.00 14.43 ? 196 GLY A N 1 ATOM 1475 C CA . GLY A 1 196 ? 34.945 -17.388 37.389 1.00 9.10 ? 196 GLY A CA 1 ATOM 1476 C C . GLY A 1 196 ? 35.471 -17.792 36.030 1.00 35.73 ? 196 GLY A C 1 ATOM 1477 O O . GLY A 1 196 ? 35.998 -16.975 35.243 1.00 36.05 ? 196 GLY A O 1 ATOM 1478 N N . GLY A 1 197 ? 35.313 -19.087 35.754 1.00 42.17 ? 197 GLY A N 1 ATOM 1479 C CA . GLY A 1 197 ? 35.792 -19.661 34.497 1.00 46.43 ? 197 GLY A CA 1 ATOM 1480 C C . GLY A 1 197 ? 36.695 -20.813 34.892 1.00 50.42 ? 197 GLY A C 1 ATOM 1481 O O . GLY A 1 197 ? 36.178 -21.891 35.190 1.00 38.17 ? 197 GLY A O 1 ATOM 1482 N N . GLU A 1 198 ? 38.035 -20.553 34.940 1.00 51.26 ? 198 GLU A N 1 ATOM 1483 C CA . GLU A 1 198 ? 38.977 -21.569 35.364 1.00 42.15 ? 198 GLU A CA 1 ATOM 1484 C C . GLU A 1 198 ? 38.642 -21.985 36.768 1.00 36.96 ? 198 GLU A C 1 ATOM 1485 O O . GLU A 1 198 ? 37.927 -21.320 37.547 1.00 33.19 ? 198 GLU A O 1 ATOM 1486 C CB . GLU A 1 198 ? 40.468 -21.295 35.181 1.00 45.71 ? 198 GLU A CB 1 ATOM 1487 C CG . GLU A 1 198 ? 41.040 -22.126 34.022 1.00 67.02 ? 198 GLU A CG 1 ATOM 1488 C CD . GLU A 1 198 ? 40.504 -21.624 32.700 1.00 100.00 ? 198 GLU A CD 1 ATOM 1489 O OE1 . GLU A 1 198 ? 39.550 -20.853 32.628 1.00 100.00 ? 198 GLU A OE1 1 ATOM 1490 O OE2 . GLU A 1 198 ? 41.202 -22.028 31.653 1.00 100.00 ? 198 GLU A OE2 1 ATOM 1491 N N . PRO A 1 199 ? 39.174 -23.116 37.071 1.00 31.18 ? 199 PRO A N 1 ATOM 1492 C CA . PRO A 1 199 ? 38.903 -23.757 38.320 1.00 25.97 ? 199 PRO A CA 1 ATOM 1493 C C . PRO A 1 199 ? 39.801 -23.477 39.529 1.00 41.45 ? 199 PRO A C 1 ATOM 1494 O O . PRO A 1 199 ? 40.934 -22.985 39.376 1.00 34.56 ? 199 PRO A O 1 ATOM 1495 C CB . PRO A 1 199 ? 38.712 -25.228 37.961 1.00 25.43 ? 199 PRO A CB 1 ATOM 1496 C CG . PRO A 1 199 ? 39.385 -25.418 36.598 1.00 26.88 ? 199 PRO A CG 1 ATOM 1497 C CD . PRO A 1 199 ? 39.624 -24.041 36.003 1.00 30.00 ? 199 PRO A CD 1 ATOM 1498 N N . SER A 1 200 ? 39.225 -23.815 40.734 1.00 37.04 ? 200 SER A N 1 ATOM 1499 C CA . SER A 1 200 ? 39.849 -23.613 42.030 1.00 24.39 ? 200 SER A CA 1 ATOM 1500 C C . SER A 1 200 ? 41.349 -23.781 42.050 1.00 24.68 ? 200 SER A C 1 ATOM 1501 O O . SER A 1 200 ? 41.868 -24.837 41.686 1.00 34.25 ? 200 SER A O 1 ATOM 1502 C CB . SER A 1 200 ? 39.256 -24.431 43.116 1.00 22.13 ? 200 SER A CB 1 ATOM 1503 O OG . SER A 1 200 ? 40.124 -24.206 44.202 1.00 16.93 ? 200 SER A OG 1 ATOM 1504 N N . VAL A 1 201 ? 42.085 -22.767 42.477 1.00 12.73 ? 201 VAL A N 1 ATOM 1505 C CA . VAL A 1 201 ? 43.519 -23.047 42.452 1.00 22.59 ? 201 VAL A CA 1 ATOM 1506 C C . VAL A 1 201 ? 44.098 -23.182 43.819 1.00 29.30 ? 201 VAL A C 1 ATOM 1507 O O . VAL A 1 201 ? 45.285 -23.470 43.971 1.00 28.92 ? 201 VAL A O 1 ATOM 1508 C CB . VAL A 1 201 ? 44.410 -22.088 41.661 1.00 11.58 ? 201 VAL A CB 1 ATOM 1509 C CG1 . VAL A 1 201 ? 43.928 -21.969 40.222 1.00 6.60 ? 201 VAL A CG1 1 ATOM 1510 C CG2 . VAL A 1 201 ? 44.475 -20.742 42.369 1.00 6.63 ? 201 VAL A CG2 1 ATOM 1511 N N . LEU A 1 202 ? 43.250 -22.945 44.777 1.00 13.86 ? 202 LEU A N 1 ATOM 1512 C CA . LEU A 1 202 ? 43.697 -22.963 46.114 1.00 22.34 ? 202 LEU A CA 1 ATOM 1513 C C . LEU A 1 202 ? 42.946 -23.891 47.002 1.00 27.76 ? 202 LEU A C 1 ATOM 1514 O O . LEU A 1 202 ? 41.717 -23.897 46.966 1.00 35.47 ? 202 LEU A O 1 ATOM 1515 C CB . LEU A 1 202 ? 43.533 -21.542 46.648 1.00 24.83 ? 202 LEU A CB 1 ATOM 1516 C CG . LEU A 1 202 ? 44.831 -20.801 46.841 1.00 19.10 ? 202 LEU A CG 1 ATOM 1517 C CD1 . LEU A 1 202 ? 45.242 -20.170 45.543 1.00 28.94 ? 202 LEU A CD1 1 ATOM 1518 C CD2 . LEU A 1 202 ? 44.535 -19.706 47.824 1.00 22.13 ? 202 LEU A CD2 1 ATOM 1519 N N . PRO A 1 203 ? 43.723 -24.637 47.797 1.00 17.70 ? 203 PRO A N 1 ATOM 1520 C CA . PRO A 1 203 ? 43.222 -25.596 48.739 1.00 19.24 ? 203 PRO A CA 1 ATOM 1521 C C . PRO A 1 203 ? 42.166 -24.902 49.527 1.00 38.45 ? 203 PRO A C 1 ATOM 1522 O O . PRO A 1 203 ? 42.357 -23.761 49.908 1.00 55.00 ? 203 PRO A O 1 ATOM 1523 C CB . PRO A 1 203 ? 44.402 -25.987 49.616 1.00 23.09 ? 203 PRO A CB 1 ATOM 1524 C CG . PRO A 1 203 ? 45.642 -25.453 48.927 1.00 23.76 ? 203 PRO A CG 1 ATOM 1525 C CD . PRO A 1 203 ? 45.193 -24.642 47.741 1.00 20.71 ? 203 PRO A CD 1 ATOM 1526 N N . SER A 1 204 ? 41.039 -25.551 49.696 1.00 32.95 ? 204 SER A N 1 ATOM 1527 C CA . SER A 1 204 ? 39.935 -24.936 50.377 1.00 30.52 ? 204 SER A CA 1 ATOM 1528 C C . SER A 1 204 ? 40.296 -24.297 51.689 1.00 29.07 ? 204 SER A C 1 ATOM 1529 O O . SER A 1 204 ? 39.588 -23.419 52.173 1.00 30.16 ? 204 SER A O 1 ATOM 1530 C CB . SER A 1 204 ? 38.735 -25.848 50.436 1.00 28.71 ? 204 SER A CB 1 ATOM 1531 N N . GLU A 1 205 ? 41.415 -24.767 52.224 1.00 39.69 ? 205 GLU A N 1 ATOM 1532 C CA . GLU A 1 205 ? 41.977 -24.311 53.496 1.00 50.26 ? 205 GLU A CA 1 ATOM 1533 C C . GLU A 1 205 ? 42.419 -22.891 53.338 1.00 45.29 ? 205 GLU A C 1 ATOM 1534 O O . GLU A 1 205 ? 42.038 -22.020 54.109 1.00 52.41 ? 205 GLU A O 1 ATOM 1535 C CB . GLU A 1 205 ? 43.188 -25.167 53.848 1.00 59.92 ? 205 GLU A CB 1 ATOM 1536 C CG . GLU A 1 205 ? 43.268 -25.594 55.327 1.00 100.00 ? 205 GLU A CG 1 ATOM 1537 C CD . GLU A 1 205 ? 44.563 -26.339 55.567 1.00 100.00 ? 205 GLU A CD 1 ATOM 1538 O OE1 . GLU A 1 205 ? 45.597 -25.757 54.953 1.00 100.00 ? 205 GLU A OE1 1 ATOM 1539 O OE2 . GLU A 1 205 ? 44.617 -27.423 56.158 1.00 100.00 ? 205 GLU A OE2 1 ATOM 1540 N N . GLU A 1 206 ? 43.241 -22.690 52.310 1.00 25.96 ? 206 GLU A N 1 ATOM 1541 C CA . GLU A 1 206 ? 43.719 -21.392 51.918 1.00 22.92 ? 206 GLU A CA 1 ATOM 1542 C C . GLU A 1 206 ? 42.464 -20.498 51.686 1.00 22.68 ? 206 GLU A C 1 ATOM 1543 O O . GLU A 1 206 ? 42.361 -19.371 52.174 1.00 19.15 ? 206 GLU A O 1 ATOM 1544 C CB . GLU A 1 206 ? 44.510 -21.486 50.594 1.00 23.78 ? 206 GLU A CB 1 ATOM 1545 C CG . GLU A 1 206 ? 45.966 -21.923 50.734 1.00 17.59 ? 206 GLU A CG 1 ATOM 1546 C CD . GLU A 1 206 ? 46.884 -20.905 50.108 1.00 96.67 ? 206 GLU A CD 1 ATOM 1547 O OE1 . GLU A 1 206 ? 46.929 -19.818 50.849 1.00 97.83 ? 206 GLU A OE1 1 ATOM 1548 O OE2 . GLU A 1 206 ? 47.420 -21.016 48.988 1.00 43.25 ? 206 GLU A OE2 1 ATOM 1549 N N . CYS A 1 207 ? 41.474 -20.997 50.931 1.00 16.14 ? 207 CYS A N 1 ATOM 1550 C CA . CYS A 1 207 ? 40.247 -20.228 50.687 1.00 18.90 ? 207 CYS A CA 1 ATOM 1551 C C . CYS A 1 207 ? 39.590 -19.668 51.973 1.00 23.04 ? 207 CYS A C 1 ATOM 1552 O O . CYS A 1 207 ? 39.363 -18.470 52.101 1.00 33.72 ? 207 CYS A O 1 ATOM 1553 C CB . CYS A 1 207 ? 39.275 -20.981 49.789 1.00 13.29 ? 207 CYS A CB 1 ATOM 1554 S SG . CYS A 1 207 ? 40.147 -21.422 48.255 1.00 18.83 ? 207 CYS A SG 1 ATOM 1555 N N . SER A 1 208 ? 39.308 -20.518 52.948 1.00 6.78 ? 208 SER A N 1 ATOM 1556 C CA . SER A 1 208 ? 38.717 -20.097 54.187 1.00 13.58 ? 208 SER A CA 1 ATOM 1557 C C . SER A 1 208 ? 39.615 -19.035 54.829 1.00 24.84 ? 208 SER A C 1 ATOM 1558 O O . SER A 1 208 ? 39.185 -18.166 55.592 1.00 32.56 ? 208 SER A O 1 ATOM 1559 C CB . SER A 1 208 ? 38.455 -21.304 55.139 1.00 20.52 ? 208 SER A CB 1 ATOM 1560 O OG . SER A 1 208 ? 37.310 -21.142 56.017 1.00 23.15 ? 208 SER A OG 1 ATOM 1561 N N . ALA A 1 209 ? 40.895 -19.105 54.531 1.00 16.23 ? 209 ALA A N 1 ATOM 1562 C CA . ALA A 1 209 ? 41.827 -18.148 55.094 1.00 18.10 ? 209 ALA A CA 1 ATOM 1563 C C . ALA A 1 209 ? 41.543 -16.758 54.558 1.00 17.72 ? 209 ALA A C 1 ATOM 1564 O O . ALA A 1 209 ? 41.606 -15.754 55.299 1.00 21.17 ? 209 ALA A O 1 ATOM 1565 C CB . ALA A 1 209 ? 43.249 -18.563 54.741 1.00 23.73 ? 209 ALA A CB 1 ATOM 1566 N N . MET A 1 210 ? 41.242 -16.723 53.254 1.00 1.00 ? 210 MET A N 1 ATOM 1567 C CA . MET A 1 210 ? 40.940 -15.488 52.647 1.00 1.00 ? 210 MET A CA 1 ATOM 1568 C C . MET A 1 210 ? 39.677 -14.941 53.256 1.00 24.05 ? 210 MET A C 1 ATOM 1569 O O . MET A 1 210 ? 39.667 -13.764 53.628 1.00 38.20 ? 210 MET A O 1 ATOM 1570 C CB . MET A 1 210 ? 40.889 -15.574 51.148 1.00 3.27 ? 210 MET A CB 1 ATOM 1571 C CG . MET A 1 210 ? 42.146 -16.203 50.581 1.00 5.84 ? 210 MET A CG 1 ATOM 1572 S SD . MET A 1 210 ? 42.168 -15.866 48.796 1.00 20.06 ? 210 MET A SD 1 ATOM 1573 C CE . MET A 1 210 ? 43.765 -16.559 48.287 1.00 20.20 ? 210 MET A CE 1 ATOM 1574 N N . GLU A 1 211 ? 38.622 -15.803 53.390 1.00 27.63 ? 211 GLU A N 1 ATOM 1575 C CA . GLU A 1 211 ? 37.293 -15.444 54.005 1.00 16.22 ? 211 GLU A CA 1 ATOM 1576 C C . GLU A 1 211 ? 37.408 -14.970 55.460 1.00 7.42 ? 211 GLU A C 1 ATOM 1577 O O . GLU A 1 211 ? 36.602 -14.158 55.907 1.00 13.03 ? 211 GLU A O 1 ATOM 1578 C CB . GLU A 1 211 ? 36.198 -16.523 53.914 1.00 14.05 ? 211 GLU A CB 1 ATOM 1579 C CG . GLU A 1 211 ? 35.292 -16.476 52.666 1.00 57.25 ? 211 GLU A CG 1 ATOM 1580 C CD . GLU A 1 211 ? 34.319 -17.629 52.702 1.00 100.00 ? 211 GLU A CD 1 ATOM 1581 O OE1 . GLU A 1 211 ? 33.676 -17.681 53.855 1.00 64.24 ? 211 GLU A OE1 1 ATOM 1582 O OE2 . GLU A 1 211 ? 34.259 -18.499 51.829 1.00 100.00 ? 211 GLU A OE2 1 ATOM 1583 N N . ASP A 1 212 ? 38.413 -15.421 56.238 1.00 3.67 ? 212 ASP A N 1 ATOM 1584 C CA . ASP A 1 212 ? 38.477 -14.876 57.593 1.00 11.40 ? 212 ASP A CA 1 ATOM 1585 C C . ASP A 1 212 ? 39.090 -13.472 57.511 1.00 28.10 ? 212 ASP A C 1 ATOM 1586 O O . ASP A 1 212 ? 38.517 -12.475 58.014 1.00 23.05 ? 212 ASP A O 1 ATOM 1587 C CB . ASP A 1 212 ? 39.137 -15.810 58.612 1.00 5.54 ? 212 ASP A CB 1 ATOM 1588 C CG . ASP A 1 212 ? 38.393 -17.115 58.706 1.00 59.32 ? 212 ASP A CG 1 ATOM 1589 O OD1 . ASP A 1 212 ? 37.181 -17.221 58.561 1.00 53.88 ? 212 ASP A OD1 1 ATOM 1590 O OD2 . ASP A 1 212 ? 39.191 -18.124 58.949 1.00 96.36 ? 212 ASP A OD2 1 ATOM 1591 N N . SER A 1 213 ? 40.240 -13.457 56.798 1.00 15.37 ? 213 SER A N 1 ATOM 1592 C CA . SER A 1 213 ? 41.076 -12.304 56.521 1.00 10.52 ? 213 SER A CA 1 ATOM 1593 C C . SER A 1 213 ? 40.378 -11.205 55.810 1.00 23.66 ? 213 SER A C 1 ATOM 1594 O O . SER A 1 213 ? 40.990 -10.171 55.558 1.00 26.25 ? 213 SER A O 1 ATOM 1595 C CB . SER A 1 213 ? 42.137 -12.701 55.521 1.00 10.46 ? 213 SER A CB 1 ATOM 1596 N N . LEU A 1 214 ? 39.120 -11.431 55.456 1.00 15.59 ? 214 LEU A N 1 ATOM 1597 C CA . LEU A 1 214 ? 38.411 -10.421 54.714 1.00 14.85 ? 214 LEU A CA 1 ATOM 1598 C C . LEU A 1 214 ? 37.790 -9.203 55.436 1.00 23.53 ? 214 LEU A C 1 ATOM 1599 O O . LEU A 1 214 ? 38.084 -8.042 55.089 1.00 8.94 ? 214 LEU A O 1 ATOM 1600 C CB . LEU A 1 214 ? 37.776 -10.954 53.423 1.00 19.87 ? 214 LEU A CB 1 ATOM 1601 C CG . LEU A 1 214 ? 36.810 -9.970 52.778 1.00 37.51 ? 214 LEU A CG 1 ATOM 1602 C CD1 . LEU A 1 214 ? 37.587 -8.765 52.266 1.00 38.12 ? 214 LEU A CD1 1 ATOM 1603 C CD2 . LEU A 1 214 ? 36.045 -10.660 51.645 1.00 26.56 ? 214 LEU A CD2 1 ATOM 1604 N N . GLU A 1 215 ? 36.949 -9.481 56.445 1.00 39.20 ? 215 GLU A N 1 ATOM 1605 C CA . GLU A 1 215 ? 36.284 -8.465 57.258 1.00 41.88 ? 215 GLU A CA 1 ATOM 1606 C C . GLU A 1 215 ? 37.284 -7.362 57.645 1.00 27.52 ? 215 GLU A C 1 ATOM 1607 O O . GLU A 1 215 ? 37.109 -6.196 57.293 1.00 34.27 ? 215 GLU A O 1 ATOM 1608 C CB . GLU A 1 215 ? 35.606 -9.128 58.489 1.00 46.91 ? 215 GLU A CB 1 ATOM 1609 C CG . GLU A 1 215 ? 34.072 -8.911 58.648 1.00 75.04 ? 215 GLU A CG 1 ATOM 1610 C CD . GLU A 1 215 ? 33.510 -9.309 60.024 1.00 100.00 ? 215 GLU A CD 1 ATOM 1611 O OE1 . GLU A 1 215 ? 33.645 -8.638 61.059 1.00 100.00 ? 215 GLU A OE1 1 ATOM 1612 O OE2 . GLU A 1 215 ? 32.807 -10.434 59.990 1.00 100.00 ? 215 GLU A OE2 1 ATOM 1613 N N . ARG A 1 216 ? 38.336 -7.763 58.317 1.00 10.74 ? 216 ARG A N 1 ATOM 1614 C CA . ARG A 1 216 ? 39.366 -6.850 58.693 1.00 18.47 ? 216 ARG A CA 1 ATOM 1615 C C . ARG A 1 216 ? 39.862 -6.039 57.490 1.00 19.98 ? 216 ARG A C 1 ATOM 1616 O O . ARG A 1 216 ? 39.949 -4.815 57.526 1.00 19.70 ? 216 ARG A O 1 ATOM 1617 C CB . ARG A 1 216 ? 40.556 -7.591 59.331 1.00 23.04 ? 216 ARG A CB 1 ATOM 1618 C CG . ARG A 1 216 ? 41.780 -6.693 59.511 1.00 1.00 ? 216 ARG A CG 1 ATOM 1619 C CD . ARG A 1 216 ? 42.110 -6.389 60.987 1.00 50.79 ? 216 ARG A CD 1 ATOM 1620 N NE . ARG A 1 216 ? 42.161 -4.941 61.304 1.00 100.00 ? 216 ARG A NE 1 ATOM 1621 C CZ . ARG A 1 216 ? 41.441 -4.258 62.233 1.00 100.00 ? 216 ARG A CZ 1 ATOM 1622 N NH1 . ARG A 1 216 ? 40.541 -4.842 63.045 1.00 100.00 ? 216 ARG A NH1 1 ATOM 1623 N NH2 . ARG A 1 216 ? 41.638 -2.935 62.346 1.00 51.28 ? 216 ARG A NH2 1 ATOM 1624 N N . CYS A 1 217 ? 40.158 -6.720 56.400 1.00 14.17 ? 217 CYS A N 1 ATOM 1625 C CA . CYS A 1 217 ? 40.681 -6.019 55.258 1.00 2.75 ? 217 CYS A CA 1 ATOM 1626 C C . CYS A 1 217 ? 39.831 -4.909 54.752 1.00 1.00 ? 217 CYS A C 1 ATOM 1627 O O . CYS A 1 217 ? 40.262 -3.828 54.381 1.00 3.97 ? 217 CYS A O 1 ATOM 1628 C CB . CYS A 1 217 ? 41.064 -6.948 54.142 1.00 1.00 ? 217 CYS A CB 1 ATOM 1629 S SG . CYS A 1 217 ? 41.134 -6.000 52.642 1.00 8.38 ? 217 CYS A SG 1 ATOM 1630 N N . LEU A 1 218 ? 38.588 -5.194 54.778 1.00 3.41 ? 218 LEU A N 1 ATOM 1631 C CA . LEU A 1 218 ? 37.614 -4.282 54.290 1.00 5.66 ? 218 LEU A CA 1 ATOM 1632 C C . LEU A 1 218 ? 37.326 -3.053 55.083 1.00 12.74 ? 218 LEU A C 1 ATOM 1633 O O . LEU A 1 218 ? 37.129 -1.981 54.494 1.00 17.37 ? 218 LEU A O 1 ATOM 1634 C CB . LEU A 1 218 ? 36.398 -5.069 53.920 1.00 12.46 ? 218 LEU A CB 1 ATOM 1635 C CG . LEU A 1 218 ? 36.793 -5.907 52.723 1.00 25.99 ? 218 LEU A CG 1 ATOM 1636 C CD1 . LEU A 1 218 ? 35.571 -6.560 52.061 1.00 11.81 ? 218 LEU A CD1 1 ATOM 1637 C CD2 . LEU A 1 218 ? 37.603 -4.997 51.777 1.00 27.84 ? 218 LEU A CD2 1 ATOM 1638 N N . GLY A 1 219 ? 37.278 -3.208 56.400 1.00 1.38 ? 219 GLY A N 1 ATOM 1639 C CA . GLY A 1 219 ? 37.031 -2.069 57.274 1.00 1.00 ? 219 GLY A CA 1 ATOM 1640 C C . GLY A 1 219 ? 38.163 -1.093 57.100 1.00 14.38 ? 219 GLY A C 1 ATOM 1641 O O . GLY A 1 219 ? 38.030 0.109 57.336 1.00 15.11 ? 219 GLY A O 1 ATOM 1642 N N . LEU A 1 220 ? 39.292 -1.656 56.662 1.00 15.94 ? 220 LEU A N 1 ATOM 1643 C CA . LEU A 1 220 ? 40.465 -0.869 56.411 1.00 15.93 ? 220 LEU A CA 1 ATOM 1644 C C . LEU A 1 220 ? 40.239 -0.080 55.164 1.00 4.23 ? 220 LEU A C 1 ATOM 1645 O O . LEU A 1 220 ? 40.508 1.120 55.190 1.00 17.38 ? 220 LEU A O 1 ATOM 1646 C CB . LEU A 1 220 ? 41.723 -1.720 56.236 1.00 25.14 ? 220 LEU A CB 1 ATOM 1647 C CG . LEU A 1 220 ? 42.207 -2.454 57.503 1.00 15.77 ? 220 LEU A CG 1 ATOM 1648 C CD1 . LEU A 1 220 ? 43.235 -3.449 57.045 1.00 3.38 ? 220 LEU A CD1 1 ATOM 1649 C CD2 . LEU A 1 220 ? 42.873 -1.520 58.520 1.00 1.00 ? 220 LEU A CD2 1 ATOM 1650 N N . ILE A 1 221 ? 39.703 -0.742 54.074 1.00 1.81 ? 221 ILE A N 1 ATOM 1651 C CA . ILE A 1 221 ? 39.418 0.016 52.836 1.00 2.29 ? 221 ILE A CA 1 ATOM 1652 C C . ILE A 1 221 ? 38.484 1.198 53.110 1.00 12.87 ? 221 ILE A C 1 ATOM 1653 O O . ILE A 1 221 ? 38.734 2.326 52.656 1.00 3.93 ? 221 ILE A O 1 ATOM 1654 C CB . ILE A 1 221 ? 39.003 -0.748 51.617 1.00 2.40 ? 221 ILE A CB 1 ATOM 1655 C CG1 . ILE A 1 221 ? 40.187 -1.556 51.115 1.00 5.92 ? 221 ILE A CG1 1 ATOM 1656 C CG2 . ILE A 1 221 ? 38.619 0.280 50.567 1.00 1.00 ? 221 ILE A CG2 1 ATOM 1657 C CD1 . ILE A 1 221 ? 39.814 -3.006 50.890 1.00 4.01 ? 221 ILE A CD1 1 ATOM 1658 N N . GLU A 1 222 ? 37.420 0.928 53.892 1.00 11.26 ? 222 GLU A N 1 ATOM 1659 C CA . GLU A 1 222 ? 36.435 1.936 54.318 1.00 10.12 ? 222 GLU A CA 1 ATOM 1660 C C . GLU A 1 222 ? 37.082 3.164 54.961 1.00 13.90 ? 222 GLU A C 1 ATOM 1661 O O . GLU A 1 222 ? 36.895 4.279 54.495 1.00 15.17 ? 222 GLU A O 1 ATOM 1662 C CB . GLU A 1 222 ? 35.440 1.345 55.321 1.00 7.69 ? 222 GLU A CB 1 ATOM 1663 C CG . GLU A 1 222 ? 34.141 0.834 54.662 1.00 73.93 ? 222 GLU A CG 1 ATOM 1664 C CD . GLU A 1 222 ? 33.384 -0.237 55.425 1.00 100.00 ? 222 GLU A CD 1 ATOM 1665 O OE1 . GLU A 1 222 ? 33.074 0.128 56.661 1.00 100.00 ? 222 GLU A OE1 1 ATOM 1666 O OE2 . GLU A 1 222 ? 32.965 -1.261 54.879 1.00 28.89 ? 222 GLU A OE2 1 ATOM 1667 N N . SER A 1 223 ? 37.822 2.923 56.039 1.00 4.63 ? 223 SER A N 1 ATOM 1668 C CA . SER A 1 223 ? 38.513 3.917 56.783 1.00 1.00 ? 223 SER A CA 1 ATOM 1669 C C . SER A 1 223 ? 39.313 4.716 55.813 1.00 8.21 ? 223 SER A C 1 ATOM 1670 O O . SER A 1 223 ? 39.344 5.964 55.814 1.00 3.74 ? 223 SER A O 1 ATOM 1671 C CB . SER A 1 223 ? 39.483 3.181 57.644 1.00 1.00 ? 223 SER A CB 1 ATOM 1672 O OG . SER A 1 223 ? 39.973 4.039 58.631 1.00 28.94 ? 223 SER A OG 1 ATOM 1673 N N . CYS A 1 224 ? 39.989 4.015 54.929 1.00 1.00 ? 224 CYS A N 1 ATOM 1674 C CA . CYS A 1 224 ? 40.741 4.815 53.963 1.00 12.55 ? 224 CYS A CA 1 ATOM 1675 C C . CYS A 1 224 ? 39.819 5.724 53.100 1.00 14.34 ? 224 CYS A C 1 ATOM 1676 O O . CYS A 1 224 ? 40.038 6.902 52.859 1.00 10.10 ? 224 CYS A O 1 ATOM 1677 C CB . CYS A 1 224 ? 41.630 3.910 53.083 1.00 10.31 ? 224 CYS A CB 1 ATOM 1678 S SG . CYS A 1 224 ? 42.505 4.841 51.817 1.00 9.18 ? 224 CYS A SG 1 ATOM 1679 N N . TYR A 1 225 ? 38.740 5.127 52.693 1.00 6.39 ? 225 TYR A N 1 ATOM 1680 C CA . TYR A 1 225 ? 37.774 5.761 51.900 1.00 6.77 ? 225 TYR A CA 1 ATOM 1681 C C . TYR A 1 225 ? 37.267 6.989 52.505 1.00 10.35 ? 225 TYR A C 1 ATOM 1682 O O . TYR A 1 225 ? 37.249 8.065 51.898 1.00 30.75 ? 225 TYR A O 1 ATOM 1683 C CB . TYR A 1 225 ? 36.588 4.824 51.632 1.00 18.05 ? 225 TYR A CB 1 ATOM 1684 C CG . TYR A 1 225 ? 36.786 4.027 50.350 1.00 24.34 ? 225 TYR A CG 1 ATOM 1685 C CD1 . TYR A 1 225 ? 38.046 3.981 49.747 1.00 35.07 ? 225 TYR A CD1 1 ATOM 1686 C CD2 . TYR A 1 225 ? 35.734 3.336 49.751 1.00 4.88 ? 225 TYR A CD2 1 ATOM 1687 C CE1 . TYR A 1 225 ? 38.282 3.278 48.568 1.00 40.11 ? 225 TYR A CE1 1 ATOM 1688 C CE2 . TYR A 1 225 ? 35.966 2.600 48.591 1.00 10.89 ? 225 TYR A CE2 1 ATOM 1689 C CZ . TYR A 1 225 ? 37.225 2.586 47.989 1.00 36.71 ? 225 TYR A CZ 1 ATOM 1690 O OH . TYR A 1 225 ? 37.444 1.877 46.842 1.00 28.88 ? 225 TYR A OH 1 ATOM 1691 N N . ASP A 1 226 ? 36.819 6.824 53.703 1.00 1.49 ? 226 ASP A N 1 ATOM 1692 C CA . ASP A 1 226 ? 36.267 7.985 54.347 1.00 7.28 ? 226 ASP A CA 1 ATOM 1693 C C . ASP A 1 226 ? 37.251 8.959 54.898 1.00 18.25 ? 226 ASP A C 1 ATOM 1694 O O . ASP A 1 226 ? 36.967 10.147 54.923 1.00 11.38 ? 226 ASP A O 1 ATOM 1695 C CB . ASP A 1 226 ? 34.973 7.789 55.163 1.00 12.45 ? 226 ASP A CB 1 ATOM 1696 C CG . ASP A 1 226 ? 35.001 6.588 56.047 1.00 32.69 ? 226 ASP A CG 1 ATOM 1697 O OD1 . ASP A 1 226 ? 35.915 6.653 57.026 1.00 13.50 ? 226 ASP A OD1 1 ATOM 1698 O OD2 . ASP A 1 226 ? 34.215 5.680 55.871 1.00 29.63 ? 226 ASP A OD2 1 ATOM 1699 N N . SER A 1 227 ? 38.415 8.445 55.328 1.00 25.95 ? 227 SER A N 1 ATOM 1700 C CA . SER A 1 227 ? 39.445 9.301 55.883 1.00 16.33 ? 227 SER A CA 1 ATOM 1701 C C . SER A 1 227 ? 40.415 9.809 54.843 1.00 17.75 ? 227 SER A C 1 ATOM 1702 O O . SER A 1 227 ? 40.635 10.991 54.747 1.00 15.19 ? 227 SER A O 1 ATOM 1703 C CB . SER A 1 227 ? 40.105 8.845 57.203 1.00 11.75 ? 227 SER A CB 1 ATOM 1704 O OG . SER A 1 227 ? 40.971 7.726 57.025 1.00 8.55 ? 227 SER A OG 1 ATOM 1705 N N . GLN A 1 228 ? 41.000 8.928 54.045 1.00 25.07 ? 228 GLN A N 1 ATOM 1706 C CA . GLN A 1 228 ? 41.971 9.359 53.042 1.00 12.03 ? 228 GLN A CA 1 ATOM 1707 C C . GLN A 1 228 ? 43.328 9.711 53.673 1.00 11.98 ? 228 GLN A C 1 ATOM 1708 O O . GLN A 1 228 ? 44.166 10.394 53.122 1.00 26.76 ? 228 GLN A O 1 ATOM 1709 C CB . GLN A 1 228 ? 41.408 10.400 52.050 1.00 2.03 ? 228 GLN A CB 1 ATOM 1710 C CG . GLN A 1 228 ? 40.006 9.950 51.549 1.00 40.08 ? 228 GLN A CG 1 ATOM 1711 C CD . GLN A 1 228 ? 39.417 10.632 50.286 1.00 77.96 ? 228 GLN A CD 1 ATOM 1712 O OE1 . GLN A 1 228 ? 40.093 11.378 49.508 1.00 3.56 ? 228 GLN A OE1 1 ATOM 1713 N NE2 . GLN A 1 228 ? 38.099 10.400 50.102 1.00 57.86 ? 228 GLN A NE2 1 ATOM 1714 N N . SER A 1 229 ? 43.548 9.190 54.852 1.00 14.14 ? 229 SER A N 1 ATOM 1715 C CA . SER A 1 229 ? 44.752 9.388 55.647 1.00 20.50 ? 229 SER A CA 1 ATOM 1716 C C . SER A 1 229 ? 45.850 8.398 55.320 1.00 16.74 ? 229 SER A C 1 ATOM 1717 O O . SER A 1 229 ? 45.614 7.313 54.815 1.00 13.98 ? 229 SER A O 1 ATOM 1718 C CB . SER A 1 229 ? 44.351 9.147 57.106 1.00 24.01 ? 229 SER A CB 1 ATOM 1719 O OG . SER A 1 229 ? 45.150 9.833 58.038 1.00 1.00 ? 229 SER A OG 1 ATOM 1720 N N . VAL A 1 230 ? 47.068 8.763 55.624 1.00 16.05 ? 230 VAL A N 1 ATOM 1721 C CA . VAL A 1 230 ? 48.081 7.799 55.366 1.00 3.33 ? 230 VAL A CA 1 ATOM 1722 C C . VAL A 1 230 ? 47.838 6.730 56.378 1.00 4.96 ? 230 VAL A C 1 ATOM 1723 O O . VAL A 1 230 ? 47.758 5.579 56.020 1.00 14.84 ? 230 VAL A O 1 ATOM 1724 C CB . VAL A 1 230 ? 49.454 8.353 55.594 1.00 3.05 ? 230 VAL A CB 1 ATOM 1725 C CG1 . VAL A 1 230 ? 50.378 7.257 55.190 1.00 7.18 ? 230 VAL A CG1 1 ATOM 1726 C CG2 . VAL A 1 230 ? 49.621 9.470 54.632 1.00 7.06 ? 230 VAL A CG2 1 ATOM 1727 N N . TRP A 1 231 ? 47.648 7.157 57.639 1.00 7.54 ? 231 TRP A N 1 ATOM 1728 C CA . TRP A 1 231 ? 47.410 6.225 58.752 1.00 6.40 ? 231 TRP A CA 1 ATOM 1729 C C . TRP A 1 231 ? 46.520 5.047 58.535 1.00 2.31 ? 231 TRP A C 1 ATOM 1730 O O . TRP A 1 231 ? 46.666 4.114 59.306 1.00 6.75 ? 231 TRP A O 1 ATOM 1731 C CB . TRP A 1 231 ? 47.207 6.843 60.143 1.00 3.54 ? 231 TRP A CB 1 ATOM 1732 C CG . TRP A 1 231 ? 48.123 7.980 60.246 1.00 8.73 ? 231 TRP A CG 1 ATOM 1733 C CD1 . TRP A 1 231 ? 47.772 9.269 60.292 1.00 12.71 ? 231 TRP A CD1 1 ATOM 1734 C CD2 . TRP A 1 231 ? 49.557 7.948 60.194 1.00 8.62 ? 231 TRP A CD2 1 ATOM 1735 N NE1 . TRP A 1 231 ? 48.903 10.062 60.317 1.00 11.65 ? 231 TRP A NE1 1 ATOM 1736 C CE2 . TRP A 1 231 ? 50.010 9.267 60.206 1.00 15.65 ? 231 TRP A CE2 1 ATOM 1737 C CE3 . TRP A 1 231 ? 50.504 6.953 60.086 1.00 8.21 ? 231 TRP A CE3 1 ATOM 1738 C CZ2 . TRP A 1 231 ? 51.378 9.592 60.219 1.00 18.80 ? 231 TRP A CZ2 1 ATOM 1739 C CZ3 . TRP A 1 231 ? 51.849 7.272 60.013 1.00 9.42 ? 231 TRP A CZ3 1 ATOM 1740 C CH2 . TRP A 1 231 ? 52.301 8.587 60.091 1.00 11.59 ? 231 TRP A CH2 1 ATOM 1741 N N . SER A 1 232 ? 45.615 5.083 57.530 1.00 5.06 ? 232 SER A N 1 ATOM 1742 C CA . SER A 1 232 ? 44.694 3.991 57.272 1.00 1.00 ? 232 SER A CA 1 ATOM 1743 C C . SER A 1 232 ? 44.908 3.401 55.918 1.00 10.29 ? 232 SER A C 1 ATOM 1744 O O . SER A 1 232 ? 44.821 2.214 55.689 1.00 7.48 ? 232 SER A O 1 ATOM 1745 C CB . SER A 1 232 ? 43.257 4.489 57.323 1.00 1.00 ? 232 SER A CB 1 ATOM 1746 N N . CYS A 1 233 ? 45.153 4.259 54.988 1.00 6.58 ? 233 CYS A N 1 ATOM 1747 C CA . CYS A 1 233 ? 45.334 3.765 53.678 1.00 3.59 ? 233 CYS A CA 1 ATOM 1748 C C . CYS A 1 233 ? 46.597 2.922 53.554 1.00 10.10 ? 233 CYS A C 1 ATOM 1749 O O . CYS A 1 233 ? 46.734 1.929 52.814 1.00 11.65 ? 233 CYS A O 1 ATOM 1750 C CB . CYS A 1 233 ? 45.335 4.918 52.704 1.00 2.81 ? 233 CYS A CB 1 ATOM 1751 S SG . CYS A 1 233 ? 43.799 5.867 52.782 1.00 11.65 ? 233 CYS A SG 1 ATOM 1752 N N . VAL A 1 234 ? 47.580 3.287 54.282 1.00 1.00 ? 234 VAL A N 1 ATOM 1753 C CA . VAL A 1 234 ? 48.765 2.493 54.125 1.00 5.64 ? 234 VAL A CA 1 ATOM 1754 C C . VAL A 1 234 ? 48.706 1.048 54.619 1.00 16.22 ? 234 VAL A C 1 ATOM 1755 O O . VAL A 1 234 ? 49.102 0.148 53.911 1.00 20.60 ? 234 VAL A O 1 ATOM 1756 C CB . VAL A 1 234 ? 50.016 3.264 54.406 1.00 2.11 ? 234 VAL A CB 1 ATOM 1757 C CG1 . VAL A 1 234 ? 51.157 2.286 54.692 1.00 1.00 ? 234 VAL A CG1 1 ATOM 1758 C CG2 . VAL A 1 234 ? 50.246 4.210 53.224 1.00 1.00 ? 234 VAL A CG2 1 ATOM 1759 N N . PRO A 1 235 ? 48.213 0.816 55.830 1.00 1.00 ? 235 PRO A N 1 ATOM 1760 C CA . PRO A 1 235 ? 48.069 -0.488 56.360 1.00 1.00 ? 235 PRO A CA 1 ATOM 1761 C C . PRO A 1 235 ? 46.964 -1.200 55.610 1.00 7.50 ? 235 PRO A C 1 ATOM 1762 O O . PRO A 1 235 ? 46.916 -2.410 55.536 1.00 17.42 ? 235 PRO A O 1 ATOM 1763 C CB . PRO A 1 235 ? 47.485 -0.261 57.722 1.00 4.28 ? 235 PRO A CB 1 ATOM 1764 C CG . PRO A 1 235 ? 47.571 1.225 58.019 1.00 2.83 ? 235 PRO A CG 1 ATOM 1765 C CD . PRO A 1 235 ? 48.384 1.789 56.909 1.00 1.00 ? 235 PRO A CD 1 ATOM 1766 N N . ALA A 1 236 ? 46.035 -0.464 55.033 1.00 3.47 ? 236 ALA A N 1 ATOM 1767 C CA . ALA A 1 236 ? 44.952 -1.142 54.311 1.00 1.23 ? 236 ALA A CA 1 ATOM 1768 C C . ALA A 1 236 ? 45.464 -1.824 53.107 1.00 1.00 ? 236 ALA A C 1 ATOM 1769 O O . ALA A 1 236 ? 44.898 -2.776 52.649 1.00 5.82 ? 236 ALA A O 1 ATOM 1770 C CB . ALA A 1 236 ? 43.849 -0.197 53.874 1.00 2.37 ? 236 ALA A CB 1 ATOM 1771 N N . THR A 1 237 ? 46.541 -1.283 52.597 1.00 5.89 ? 237 THR A N 1 ATOM 1772 C CA . THR A 1 237 ? 47.158 -1.785 51.419 1.00 1.00 ? 237 THR A CA 1 ATOM 1773 C C . THR A 1 237 ? 47.903 -3.028 51.719 1.00 1.00 ? 237 THR A C 1 ATOM 1774 O O . THR A 1 237 ? 47.630 -4.091 51.174 1.00 5.94 ? 237 THR A O 1 ATOM 1775 C CB . THR A 1 237 ? 48.068 -0.760 50.720 1.00 1.00 ? 237 THR A CB 1 ATOM 1776 O OG1 . THR A 1 237 ? 47.377 0.316 50.108 1.00 1.00 ? 237 THR A OG1 1 ATOM 1777 C CG2 . THR A 1 237 ? 48.819 -1.528 49.689 1.00 1.00 ? 237 THR A CG2 1 ATOM 1778 N N . ILE A 1 238 ? 48.852 -2.886 52.592 1.00 2.20 ? 238 ILE A N 1 ATOM 1779 C CA . ILE A 1 238 ? 49.694 -3.988 53.000 1.00 10.47 ? 238 ILE A CA 1 ATOM 1780 C C . ILE A 1 238 ? 48.984 -5.203 53.531 1.00 16.64 ? 238 ILE A C 1 ATOM 1781 O O . ILE A 1 238 ? 49.354 -6.302 53.184 1.00 16.09 ? 238 ILE A O 1 ATOM 1782 C CB . ILE A 1 238 ? 50.678 -3.588 54.032 1.00 11.66 ? 238 ILE A CB 1 ATOM 1783 C CG1 . ILE A 1 238 ? 51.467 -2.435 53.446 1.00 7.14 ? 238 ILE A CG1 1 ATOM 1784 C CG2 . ILE A 1 238 ? 51.554 -4.820 54.169 1.00 25.81 ? 238 ILE A CG2 1 ATOM 1785 C CD1 . ILE A 1 238 ? 52.235 -1.680 54.502 1.00 10.76 ? 238 ILE A CD1 1 ATOM 1786 N N . TYR A 1 239 ? 48.002 -4.962 54.371 1.00 9.43 ? 239 TYR A N 1 ATOM 1787 C CA . TYR A 1 239 ? 47.175 -5.963 54.985 1.00 1.11 ? 239 TYR A CA 1 ATOM 1788 C C . TYR A 1 239 ? 46.351 -6.711 53.953 1.00 1.00 ? 239 TYR A C 1 ATOM 1789 O O . TYR A 1 239 ? 46.389 -7.911 53.871 1.00 1.00 ? 239 TYR A O 1 ATOM 1790 C CB . TYR A 1 239 ? 46.237 -5.390 56.095 1.00 1.00 ? 239 TYR A CB 1 ATOM 1791 C CG . TYR A 1 239 ? 45.387 -6.493 56.667 1.00 1.00 ? 239 TYR A CG 1 ATOM 1792 C CD1 . TYR A 1 239 ? 44.195 -6.921 56.089 1.00 1.00 ? 239 TYR A CD1 1 ATOM 1793 C CD2 . TYR A 1 239 ? 45.816 -7.181 57.788 1.00 3.85 ? 239 TYR A CD2 1 ATOM 1794 C CE1 . TYR A 1 239 ? 43.450 -7.971 56.613 1.00 1.00 ? 239 TYR A CE1 1 ATOM 1795 C CE2 . TYR A 1 239 ? 45.099 -8.247 58.326 1.00 10.29 ? 239 TYR A CE2 1 ATOM 1796 C CZ . TYR A 1 239 ? 43.906 -8.649 57.737 1.00 20.99 ? 239 TYR A CZ 1 ATOM 1797 O OH . TYR A 1 239 ? 43.202 -9.702 58.266 1.00 9.76 ? 239 TYR A OH 1 ATOM 1798 N N . CYS A 1 240 ? 45.592 -6.003 53.181 1.00 1.00 ? 240 CYS A N 1 ATOM 1799 C CA . CYS A 1 240 ? 44.732 -6.573 52.163 1.00 1.00 ? 240 CYS A CA 1 ATOM 1800 C C . CYS A 1 240 ? 45.504 -7.293 51.081 1.00 1.00 ? 240 CYS A C 1 ATOM 1801 O O . CYS A 1 240 ? 45.155 -8.367 50.670 1.00 1.00 ? 240 CYS A O 1 ATOM 1802 C CB . CYS A 1 240 ? 43.841 -5.464 51.526 1.00 1.00 ? 240 CYS A CB 1 ATOM 1803 S SG . CYS A 1 240 ? 42.723 -4.787 52.751 1.00 6.03 ? 240 CYS A SG 1 ATOM 1804 N N . ASN A 1 241 ? 46.577 -6.683 50.602 1.00 1.00 ? 241 ASN A N 1 ATOM 1805 C CA . ASN A 1 241 ? 47.347 -7.283 49.591 1.00 1.00 ? 241 ASN A CA 1 ATOM 1806 C C . ASN A 1 241 ? 47.982 -8.494 50.106 1.00 11.70 ? 241 ASN A C 1 ATOM 1807 O O . ASN A 1 241 ? 48.483 -9.330 49.362 1.00 27.68 ? 241 ASN A O 1 ATOM 1808 C CB . ASN A 1 241 ? 48.447 -6.352 49.182 1.00 1.00 ? 241 ASN A CB 1 ATOM 1809 C CG . ASN A 1 241 ? 47.877 -5.364 48.251 1.00 1.00 ? 241 ASN A CG 1 ATOM 1810 O OD1 . ASN A 1 241 ? 48.617 -4.675 47.609 1.00 1.00 ? 241 ASN A OD1 1 ATOM 1811 N ND2 . ASN A 1 241 ? 46.604 -5.518 47.960 1.00 1.00 ? 241 ASN A ND2 1 ATOM 1812 N N . ASN A 1 242 ? 47.994 -8.570 51.407 1.00 10.08 ? 242 ASN A N 1 ATOM 1813 C CA . ASN A 1 242 ? 48.614 -9.694 52.039 1.00 1.00 ? 242 ASN A CA 1 ATOM 1814 C C . ASN A 1 242 ? 47.750 -10.885 52.106 1.00 6.66 ? 242 ASN A C 1 ATOM 1815 O O . ASN A 1 242 ? 48.115 -11.923 51.541 1.00 16.57 ? 242 ASN A O 1 ATOM 1816 C CB . ASN A 1 242 ? 49.019 -9.419 53.416 1.00 1.00 ? 242 ASN A CB 1 ATOM 1817 C CG . ASN A 1 242 ? 49.835 -10.594 53.873 1.00 45.37 ? 242 ASN A CG 1 ATOM 1818 O OD1 . ASN A 1 242 ? 49.351 -11.424 54.669 1.00 37.55 ? 242 ASN A OD1 1 ATOM 1819 N ND2 . ASN A 1 242 ? 51.007 -10.754 53.250 1.00 1.00 ? 242 ASN A ND2 1 ATOM 1820 N N . ALA A 1 243 ? 46.641 -10.682 52.838 1.00 1.00 ? 243 ALA A N 1 ATOM 1821 C CA . ALA A 1 243 ? 45.565 -11.608 53.090 1.00 1.00 ? 243 ALA A CA 1 ATOM 1822 C C . ALA A 1 243 ? 44.983 -12.127 51.807 1.00 10.50 ? 243 ALA A C 1 ATOM 1823 O O . ALA A 1 243 ? 44.579 -13.261 51.733 1.00 18.56 ? 243 ALA A O 1 ATOM 1824 C CB . ALA A 1 243 ? 44.466 -10.841 53.759 1.00 1.00 ? 243 ALA A CB 1 ATOM 1825 N N . GLN A 1 244 ? 44.939 -11.305 50.770 1.00 14.31 ? 244 GLN A N 1 ATOM 1826 C CA . GLN A 1 244 ? 44.327 -11.699 49.526 1.00 2.96 ? 244 GLN A CA 1 ATOM 1827 C C . GLN A 1 244 ? 45.141 -11.894 48.293 1.00 12.75 ? 244 GLN A C 1 ATOM 1828 O O . GLN A 1 244 ? 44.688 -12.494 47.320 1.00 15.56 ? 244 GLN A O 1 ATOM 1829 C CB . GLN A 1 244 ? 43.294 -10.649 49.211 1.00 1.00 ? 244 GLN A CB 1 ATOM 1830 C CG . GLN A 1 244 ? 41.938 -11.300 49.096 1.00 45.50 ? 244 GLN A CG 1 ATOM 1831 C CD . GLN A 1 244 ? 41.285 -11.402 50.441 1.00 38.39 ? 244 GLN A CD 1 ATOM 1832 O OE1 . GLN A 1 244 ? 40.236 -12.040 50.563 1.00 18.21 ? 244 GLN A OE1 1 ATOM 1833 N NE2 . GLN A 1 244 ? 41.944 -10.831 51.450 1.00 25.54 ? 244 GLN A NE2 1 ATOM 1834 N N . LEU A 1 245 ? 46.312 -11.376 48.251 1.00 10.65 ? 245 LEU A N 1 ATOM 1835 C CA . LEU A 1 245 ? 46.986 -11.610 46.999 1.00 12.85 ? 245 LEU A CA 1 ATOM 1836 C C . LEU A 1 245 ? 48.060 -12.637 47.095 1.00 13.93 ? 245 LEU A C 1 ATOM 1837 O O . LEU A 1 245 ? 48.422 -13.310 46.157 1.00 9.15 ? 245 LEU A O 1 ATOM 1838 C CB . LEU A 1 245 ? 47.630 -10.335 46.389 1.00 13.24 ? 245 LEU A CB 1 ATOM 1839 C CG . LEU A 1 245 ? 46.742 -9.095 46.298 1.00 18.28 ? 245 LEU A CG 1 ATOM 1840 C CD1 . LEU A 1 245 ? 47.655 -7.876 46.341 1.00 14.24 ? 245 LEU A CD1 1 ATOM 1841 C CD2 . LEU A 1 245 ? 45.992 -9.094 44.977 1.00 1.00 ? 245 LEU A CD2 1 ATOM 1842 N N . ALA A 1 246 ? 48.636 -12.716 48.236 1.00 15.41 ? 246 ALA A N 1 ATOM 1843 C CA . ALA A 1 246 ? 49.733 -13.596 48.401 1.00 1.03 ? 246 ALA A CA 1 ATOM 1844 C C . ALA A 1 246 ? 49.466 -15.085 48.314 1.00 13.03 ? 246 ALA A C 1 ATOM 1845 O O . ALA A 1 246 ? 50.336 -15.819 47.842 1.00 13.08 ? 246 ALA A O 1 ATOM 1846 C CB . ALA A 1 246 ? 50.340 -13.212 49.706 1.00 1.00 ? 246 ALA A CB 1 ATOM 1847 N N . PRO A 1 247 ? 48.309 -15.550 48.800 1.00 16.71 ? 247 PRO A N 1 ATOM 1848 C CA . PRO A 1 247 ? 48.092 -16.973 48.745 1.00 10.58 ? 247 PRO A CA 1 ATOM 1849 C C . PRO A 1 247 ? 48.147 -17.432 47.311 1.00 20.22 ? 247 PRO A C 1 ATOM 1850 O O . PRO A 1 247 ? 48.784 -18.420 46.976 1.00 30.83 ? 247 PRO A O 1 ATOM 1851 C CB . PRO A 1 247 ? 46.748 -17.281 49.408 1.00 8.11 ? 247 PRO A CB 1 ATOM 1852 C CG . PRO A 1 247 ? 46.373 -16.011 50.148 1.00 21.50 ? 247 PRO A CG 1 ATOM 1853 C CD . PRO A 1 247 ? 47.197 -14.882 49.543 1.00 19.89 ? 247 PRO A CD 1 ATOM 1854 N N . TYR A 1 248 ? 47.523 -16.677 46.442 1.00 14.28 ? 248 TYR A N 1 ATOM 1855 C CA . TYR A 1 248 ? 47.570 -17.054 45.053 1.00 13.18 ? 248 TYR A CA 1 ATOM 1856 C C . TYR A 1 248 ? 49.033 -17.061 44.561 1.00 13.98 ? 248 TYR A C 1 ATOM 1857 O O . TYR A 1 248 ? 49.533 -17.991 43.932 1.00 8.93 ? 248 TYR A O 1 ATOM 1858 C CB . TYR A 1 248 ? 46.540 -16.214 44.235 1.00 9.56 ? 248 TYR A CB 1 ATOM 1859 C CG . TYR A 1 248 ? 46.546 -16.432 42.766 1.00 6.47 ? 248 TYR A CG 1 ATOM 1860 C CD1 . TYR A 1 248 ? 47.595 -15.935 41.993 1.00 8.06 ? 248 TYR A CD1 1 ATOM 1861 C CD2 . TYR A 1 248 ? 45.511 -17.128 42.149 1.00 10.31 ? 248 TYR A CD2 1 ATOM 1862 C CE1 . TYR A 1 248 ? 47.650 -16.144 40.615 1.00 9.61 ? 248 TYR A CE1 1 ATOM 1863 C CE2 . TYR A 1 248 ? 45.549 -17.329 40.771 1.00 2.81 ? 248 TYR A CE2 1 ATOM 1864 C CZ . TYR A 1 248 ? 46.612 -16.849 40.013 1.00 1.00 ? 248 TYR A CZ 1 ATOM 1865 O OH . TYR A 1 248 ? 46.630 -17.066 38.678 1.00 17.51 ? 248 TYR A OH 1 ATOM 1866 N N . GLN A 1 249 ? 49.764 -16.013 44.888 1.00 21.15 ? 249 GLN A N 1 ATOM 1867 C CA . GLN A 1 249 ? 51.158 -15.888 44.502 1.00 2.72 ? 249 GLN A CA 1 ATOM 1868 C C . GLN A 1 249 ? 51.997 -17.048 44.931 1.00 4.46 ? 249 GLN A C 1 ATOM 1869 O O . GLN A 1 249 ? 52.888 -17.474 44.189 1.00 17.72 ? 249 GLN A O 1 ATOM 1870 C CB . GLN A 1 249 ? 51.751 -14.577 44.968 1.00 1.00 ? 249 GLN A CB 1 ATOM 1871 C CG . GLN A 1 249 ? 51.319 -13.462 44.005 1.00 23.59 ? 249 GLN A CG 1 ATOM 1872 C CD . GLN A 1 249 ? 51.898 -12.085 44.311 1.00 4.35 ? 249 GLN A CD 1 ATOM 1873 O OE1 . GLN A 1 249 ? 51.737 -11.574 45.404 1.00 1.00 ? 249 GLN A OE1 1 ATOM 1874 N NE2 . GLN A 1 249 ? 52.474 -11.430 43.303 1.00 12.11 ? 249 GLN A NE2 1 ATOM 1875 N N . ARG A 1 250 ? 51.727 -17.550 46.118 1.00 12.59 ? 250 ARG A N 1 ATOM 1876 C CA . ARG A 1 250 ? 52.488 -18.696 46.589 1.00 19.19 ? 250 ARG A CA 1 ATOM 1877 C C . ARG A 1 250 ? 52.445 -19.829 45.574 1.00 32.33 ? 250 ARG A C 1 ATOM 1878 O O . ARG A 1 250 ? 53.502 -20.284 45.128 1.00 54.09 ? 250 ARG A O 1 ATOM 1879 C CB . ARG A 1 250 ? 52.229 -19.170 48.023 1.00 1.80 ? 250 ARG A CB 1 ATOM 1880 C CG . ARG A 1 250 ? 51.361 -18.237 48.866 1.00 7.43 ? 250 ARG A CG 1 ATOM 1881 C CD . ARG A 1 250 ? 51.428 -18.596 50.344 1.00 21.08 ? 250 ARG A CD 1 ATOM 1882 N NE . ARG A 1 250 ? 52.516 -19.517 50.646 1.00 24.39 ? 250 ARG A NE 1 ATOM 1883 C CZ . ARG A 1 250 ? 52.492 -20.254 51.746 1.00 51.27 ? 250 ARG A CZ 1 ATOM 1884 N NH1 . ARG A 1 250 ? 51.469 -20.161 52.582 1.00 18.17 ? 250 ARG A NH1 1 ATOM 1885 N NH2 . ARG A 1 250 ? 53.498 -21.090 52.036 1.00 1.00 ? 250 ARG A NH2 1 ATOM 1886 N N . THR A 1 251 ? 51.226 -20.213 45.166 1.00 16.13 ? 251 THR A N 1 ATOM 1887 C CA . THR A 1 251 ? 50.993 -21.295 44.172 1.00 16.25 ? 251 THR A CA 1 ATOM 1888 C C . THR A 1 251 ? 51.847 -21.145 42.943 1.00 27.58 ? 251 THR A C 1 ATOM 1889 O O . THR A 1 251 ? 52.184 -22.104 42.263 1.00 31.23 ? 251 THR A O 1 ATOM 1890 C CB . THR A 1 251 ? 49.552 -21.443 43.656 1.00 19.23 ? 251 THR A CB 1 ATOM 1891 O OG1 . THR A 1 251 ? 49.456 -20.690 42.437 1.00 14.35 ? 251 THR A OG1 1 ATOM 1892 C CG2 . THR A 1 251 ? 48.433 -21.218 44.728 1.00 1.00 ? 251 THR A CG2 1 ATOM 1893 N N . GLY A 1 252 ? 52.192 -19.920 42.654 1.00 30.15 ? 252 GLY A N 1 ATOM 1894 C CA . GLY A 1 252 ? 53.020 -19.718 41.520 1.00 23.47 ? 252 GLY A CA 1 ATOM 1895 C C . GLY A 1 252 ? 52.269 -19.955 40.262 1.00 21.91 ? 252 GLY A C 1 ATOM 1896 O O . GLY A 1 252 ? 52.697 -20.704 39.430 1.00 29.51 ? 252 GLY A O 1 ATOM 1897 N N . ARG A 1 253 ? 51.150 -19.286 40.132 1.00 21.70 ? 253 ARG A N 1 ATOM 1898 C CA . ARG A 1 253 ? 50.326 -19.347 38.952 1.00 11.13 ? 253 ARG A CA 1 ATOM 1899 C C . ARG A 1 253 ? 50.538 -18.024 38.271 1.00 3.85 ? 253 ARG A C 1 ATOM 1900 O O . ARG A 1 253 ? 50.909 -17.082 38.941 1.00 20.65 ? 253 ARG A O 1 ATOM 1901 C CB . ARG A 1 253 ? 48.920 -19.297 39.488 1.00 4.69 ? 253 ARG A CB 1 ATOM 1902 C CG . ARG A 1 253 ? 47.950 -20.075 38.659 1.00 52.12 ? 253 ARG A CG 1 ATOM 1903 C CD . ARG A 1 253 ? 48.641 -21.012 37.694 1.00 71.79 ? 253 ARG A CD 1 ATOM 1904 N NE . ARG A 1 253 ? 47.638 -21.930 37.235 1.00 42.36 ? 253 ARG A NE 1 ATOM 1905 C CZ . ARG A 1 253 ? 47.239 -22.936 37.971 1.00 67.66 ? 253 ARG A CZ 1 ATOM 1906 N NH1 . ARG A 1 253 ? 47.783 -23.184 39.170 1.00 39.29 ? 253 ARG A NH1 1 ATOM 1907 N NH2 . ARG A 1 253 ? 46.289 -23.713 37.471 1.00 55.56 ? 253 ARG A NH2 1 ATOM 1908 N N . ASN A 1 254 ? 50.305 -17.832 36.993 1.00 20.20 ? 254 ASN A N 1 ATOM 1909 C CA . ASN A 1 254 ? 50.522 -16.423 36.546 1.00 21.86 ? 254 ASN A CA 1 ATOM 1910 C C . ASN A 1 254 ? 49.493 -15.429 37.188 1.00 25.70 ? 254 ASN A C 1 ATOM 1911 O O . ASN A 1 254 ? 48.333 -15.728 37.470 1.00 17.08 ? 254 ASN A O 1 ATOM 1912 C CB . ASN A 1 254 ? 50.646 -16.246 35.038 1.00 14.97 ? 254 ASN A CB 1 ATOM 1913 C CG . ASN A 1 254 ? 50.958 -14.847 34.618 1.00 10.71 ? 254 ASN A CG 1 ATOM 1914 O OD1 . ASN A 1 254 ? 51.717 -14.219 35.458 1.00 37.53 ? 254 ASN A OD1 1 ATOM 1915 N ND2 . ASN A 1 254 ? 50.659 -14.396 33.533 1.00 39.83 ? 254 ASN A ND2 1 ATOM 1916 N N . VAL A 1 255 ? 49.888 -14.221 37.476 1.00 29.12 ? 255 VAL A N 1 ATOM 1917 C CA . VAL A 1 255 ? 48.947 -13.327 38.137 1.00 24.98 ? 255 VAL A CA 1 ATOM 1918 C C . VAL A 1 255 ? 47.941 -12.630 37.251 1.00 23.60 ? 255 VAL A C 1 ATOM 1919 O O . VAL A 1 255 ? 46.818 -12.210 37.706 1.00 4.36 ? 255 VAL A O 1 ATOM 1920 C CB . VAL A 1 255 ? 49.601 -12.529 39.264 1.00 16.07 ? 255 VAL A CB 1 ATOM 1921 C CG1 . VAL A 1 255 ? 49.239 -11.083 39.223 1.00 9.19 ? 255 VAL A CG1 1 ATOM 1922 C CG2 . VAL A 1 255 ? 49.262 -13.161 40.612 1.00 16.19 ? 255 VAL A CG2 1 ATOM 1923 N N . TYR A 1 256 ? 48.370 -12.593 35.975 1.00 21.49 ? 256 TYR A N 1 ATOM 1924 C CA . TYR A 1 256 ? 47.657 -12.010 34.850 1.00 20.57 ? 256 TYR A CA 1 ATOM 1925 C C . TYR A 1 256 ? 46.994 -13.033 34.011 1.00 11.86 ? 256 TYR A C 1 ATOM 1926 O O . TYR A 1 256 ? 46.572 -12.711 32.933 1.00 24.85 ? 256 TYR A O 1 ATOM 1927 C CB . TYR A 1 256 ? 48.675 -11.431 33.870 1.00 25.80 ? 256 TYR A CB 1 ATOM 1928 C CG . TYR A 1 256 ? 49.665 -10.668 34.645 1.00 26.73 ? 256 TYR A CG 1 ATOM 1929 C CD1 . TYR A 1 256 ? 49.211 -9.580 35.378 1.00 26.96 ? 256 TYR A CD1 1 ATOM 1930 C CD2 . TYR A 1 256 ? 50.997 -11.061 34.718 1.00 37.58 ? 256 TYR A CD2 1 ATOM 1931 C CE1 . TYR A 1 256 ? 50.091 -8.840 36.157 1.00 35.69 ? 256 TYR A CE1 1 ATOM 1932 C CE2 . TYR A 1 256 ? 51.883 -10.324 35.501 1.00 51.30 ? 256 TYR A CE2 1 ATOM 1933 C CZ . TYR A 1 256 ? 51.429 -9.215 36.217 1.00 57.26 ? 256 TYR A CZ 1 ATOM 1934 O OH . TYR A 1 256 ? 52.291 -8.469 36.988 1.00 48.66 ? 256 TYR A OH 1 ATOM 1935 N N . ASP A 1 257 ? 46.929 -14.249 34.463 1.00 8.22 ? 257 ASP A N 1 ATOM 1936 C CA . ASP A 1 257 ? 46.344 -15.279 33.641 1.00 5.70 ? 257 ASP A CA 1 ATOM 1937 C C . ASP A 1 257 ? 46.367 -16.567 34.442 1.00 10.01 ? 257 ASP A C 1 ATOM 1938 O O . ASP A 1 257 ? 47.379 -17.288 34.561 1.00 6.58 ? 257 ASP A O 1 ATOM 1939 C CB . ASP A 1 257 ? 47.287 -15.368 32.418 1.00 9.70 ? 257 ASP A CB 1 ATOM 1940 C CG . ASP A 1 257 ? 46.749 -16.172 31.266 1.00 33.24 ? 257 ASP A CG 1 ATOM 1941 O OD1 . ASP A 1 257 ? 45.932 -17.144 31.689 1.00 15.51 ? 257 ASP A OD1 1 ATOM 1942 O OD2 . ASP A 1 257 ? 47.084 -15.954 30.077 1.00 1.61 ? 257 ASP A OD2 1 ATOM 1943 N N . ILE A 1 258 ? 45.243 -16.847 35.044 1.00 7.77 ? 258 ILE A N 1 ATOM 1944 C CA . ILE A 1 258 ? 45.117 -18.026 35.890 1.00 11.53 ? 258 ILE A CA 1 ATOM 1945 C C . ILE A 1 258 ? 45.533 -19.350 35.190 1.00 39.68 ? 258 ILE A C 1 ATOM 1946 O O . ILE A 1 258 ? 46.063 -20.243 35.856 1.00 51.61 ? 258 ILE A O 1 ATOM 1947 C CB . ILE A 1 258 ? 43.749 -18.006 36.604 1.00 11.79 ? 258 ILE A CB 1 ATOM 1948 C CG1 . ILE A 1 258 ? 43.769 -18.433 38.068 1.00 16.48 ? 258 ILE A CG1 1 ATOM 1949 C CG2 . ILE A 1 258 ? 42.676 -18.780 35.843 1.00 8.35 ? 258 ILE A CG2 1 ATOM 1950 C CD1 . ILE A 1 258 ? 42.352 -18.751 38.630 1.00 6.76 ? 258 ILE A CD1 1 ATOM 1951 N N . ARG A 1 259 ? 45.310 -19.459 33.848 1.00 42.27 ? 259 ARG A N 1 ATOM 1952 C CA . ARG A 1 259 ? 45.625 -20.646 32.992 1.00 42.16 ? 259 ARG A CA 1 ATOM 1953 C C . ARG A 1 259 ? 47.120 -20.962 32.845 1.00 39.48 ? 259 ARG A C 1 ATOM 1954 O O . ARG A 1 259 ? 47.568 -22.103 32.843 1.00 35.89 ? 259 ARG A O 1 ATOM 1955 C CB . ARG A 1 259 ? 45.030 -20.510 31.569 1.00 28.81 ? 259 ARG A CB 1 ATOM 1956 C CG . ARG A 1 259 ? 43.544 -20.181 31.514 1.00 4.91 ? 259 ARG A CG 1 ATOM 1957 C CD . ARG A 1 259 ? 43.144 -19.439 30.266 1.00 33.28 ? 259 ARG A CD 1 ATOM 1958 N NE . ARG A 1 259 ? 44.051 -18.362 29.932 1.00 9.06 ? 259 ARG A NE 1 ATOM 1959 C CZ . ARG A 1 259 ? 44.126 -17.847 28.704 1.00 1.00 ? 259 ARG A CZ 1 ATOM 1960 N NH1 . ARG A 1 259 ? 43.379 -18.324 27.716 1.00 18.09 ? 259 ARG A NH1 1 ATOM 1961 N NH2 . ARG A 1 259 ? 44.995 -16.840 28.439 1.00 1.00 ? 259 ARG A NH2 1 ATOM 1962 N N . LYS A 1 260 ? 47.882 -19.911 32.685 1.00 39.52 ? 260 LYS A N 1 ATOM 1963 C CA . LYS A 1 260 ? 49.306 -19.970 32.525 1.00 32.89 ? 260 LYS A CA 1 ATOM 1964 C C . LYS A 1 260 ? 49.957 -20.007 33.896 1.00 52.88 ? 260 LYS A C 1 ATOM 1965 O O . LYS A 1 260 ? 49.480 -19.462 34.912 1.00 48.15 ? 260 LYS A O 1 ATOM 1966 C CB . LYS A 1 260 ? 49.764 -18.683 31.813 1.00 37.92 ? 260 LYS A CB 1 ATOM 1967 C CG . LYS A 1 260 ? 50.199 -18.794 30.340 1.00 58.12 ? 260 LYS A CG 1 ATOM 1968 C CD . LYS A 1 260 ? 49.189 -18.293 29.306 1.00 2.90 ? 260 LYS A CD 1 ATOM 1969 C CE . LYS A 1 260 ? 49.647 -17.055 28.551 1.00 81.90 ? 260 LYS A CE 1 ATOM 1970 N NZ . LYS A 1 260 ? 48.631 -16.554 27.596 1.00 100.00 ? 260 LYS A NZ 1 ATOM 1971 N N . ASP A 1 261 ? 51.077 -20.652 33.945 1.00 61.68 ? 261 ASP A N 1 ATOM 1972 C CA . ASP A 1 261 ? 51.738 -20.654 35.201 1.00 69.27 ? 261 ASP A CA 1 ATOM 1973 C C . ASP A 1 261 ? 53.017 -19.818 35.087 1.00 79.33 ? 261 ASP A C 1 ATOM 1974 O O . ASP A 1 261 ? 53.562 -19.632 34.004 1.00 75.45 ? 261 ASP A O 1 ATOM 1975 C CB . ASP A 1 261 ? 51.944 -22.046 35.787 1.00 72.96 ? 261 ASP A CB 1 ATOM 1976 C CG . ASP A 1 261 ? 52.735 -22.886 34.861 1.00 93.89 ? 261 ASP A CG 1 ATOM 1977 O OD1 . ASP A 1 261 ? 53.042 -22.512 33.741 1.00 95.65 ? 261 ASP A OD1 1 ATOM 1978 O OD2 . ASP A 1 261 ? 53.058 -24.037 35.392 1.00 100.00 ? 261 ASP A OD2 1 ATOM 1979 N N . CYS A 1 262 ? 53.467 -19.289 36.228 1.00 82.14 ? 262 CYS A N 1 ATOM 1980 C CA . CYS A 1 262 ? 54.662 -18.467 36.390 1.00 75.18 ? 262 CYS A CA 1 ATOM 1981 C C . CYS A 1 262 ? 55.067 -18.536 37.878 1.00 99.98 ? 262 CYS A C 1 ATOM 1982 O O . CYS A 1 262 ? 54.256 -18.090 38.711 1.00 98.98 ? 262 CYS A O 1 ATOM 1983 C CB . CYS A 1 262 ? 54.428 -17.002 35.885 1.00 65.66 ? 262 CYS A CB 1 ATOM 1984 S SG . CYS A 1 262 ? 55.371 -15.729 36.789 1.00 63.89 ? 262 CYS A SG 1 ATOM 1985 N N . GLU A 1 263 ? 56.280 -19.110 38.212 1.00 100.00 ? 263 GLU A N 1 ATOM 1986 C CA . GLU A 1 263 ? 56.775 -19.224 39.617 1.00 94.99 ? 263 GLU A CA 1 ATOM 1987 C C . GLU A 1 263 ? 57.375 -17.925 39.990 1.00 100.00 ? 263 GLU A C 1 ATOM 1988 O O . GLU A 1 263 ? 57.809 -17.169 39.104 1.00 100.00 ? 263 GLU A O 1 ATOM 1989 C CB . GLU A 1 263 ? 57.937 -20.179 39.940 1.00 93.00 ? 263 GLU A CB 1 ATOM 1990 C CG . GLU A 1 263 ? 57.559 -21.627 40.191 1.00 97.34 ? 263 GLU A CG 1 ATOM 1991 C CD . GLU A 1 263 ? 57.943 -22.387 38.962 1.00 100.00 ? 263 GLU A CD 1 ATOM 1992 O OE1 . GLU A 1 263 ? 58.481 -21.825 38.006 1.00 100.00 ? 263 GLU A OE1 1 ATOM 1993 O OE2 . GLU A 1 263 ? 57.661 -23.673 39.010 1.00 100.00 ? 263 GLU A OE2 1 ATOM 1994 N N . GLY A 1 264 ? 57.437 -17.717 41.302 1.00 99.07 ? 264 GLY A N 1 ATOM 1995 C CA . GLY A 1 264 ? 57.986 -16.487 41.860 1.00 100.00 ? 264 GLY A CA 1 ATOM 1996 C C . GLY A 1 264 ? 59.464 -16.174 41.556 1.00 100.00 ? 264 GLY A C 1 ATOM 1997 O O . GLY A 1 264 ? 60.347 -17.037 41.745 1.00 100.00 ? 264 GLY A O 1 ATOM 1998 N N . GLY A 1 265 ? 59.703 -14.907 41.122 1.00 100.00 ? 265 GLY A N 1 ATOM 1999 C CA . GLY A 1 265 ? 61.028 -14.361 40.779 1.00 100.00 ? 265 GLY A CA 1 ATOM 2000 C C . GLY A 1 265 ? 61.177 -13.958 39.300 1.00 100.00 ? 265 GLY A C 1 ATOM 2001 O O . GLY A 1 265 ? 61.288 -12.782 38.903 1.00 98.91 ? 265 GLY A O 1 ATOM 2002 N N . ASN A 1 266 ? 61.170 -14.979 38.466 1.00 96.87 ? 266 ASN A N 1 ATOM 2003 C CA . ASN A 1 266 ? 61.305 -14.759 37.064 1.00 87.64 ? 266 ASN A CA 1 ATOM 2004 C C . ASN A 1 266 ? 60.105 -14.086 36.462 1.00 70.20 ? 266 ASN A C 1 ATOM 2005 O O . ASN A 1 266 ? 59.177 -13.632 37.139 1.00 50.73 ? 266 ASN A O 1 ATOM 2006 C CB . ASN A 1 266 ? 61.664 -16.051 36.331 1.00 80.39 ? 266 ASN A CB 1 ATOM 2007 C CG . ASN A 1 266 ? 63.159 -16.287 36.440 1.00 100.00 ? 266 ASN A CG 1 ATOM 2008 O OD1 . ASN A 1 266 ? 63.923 -15.849 35.566 1.00 100.00 ? 266 ASN A OD1 1 ATOM 2009 N ND2 . ASN A 1 266 ? 63.591 -16.856 37.571 1.00 100.00 ? 266 ASN A ND2 1 ATOM 2010 N N . LEU A 1 267 ? 60.167 -14.033 35.154 1.00 73.42 ? 267 LEU A N 1 ATOM 2011 C CA . LEU A 1 267 ? 59.092 -13.436 34.452 1.00 74.15 ? 267 LEU A CA 1 ATOM 2012 C C . LEU A 1 267 ? 58.037 -14.451 34.180 1.00 70.17 ? 267 LEU A C 1 ATOM 2013 O O . LEU A 1 267 ? 58.259 -15.678 34.166 1.00 62.90 ? 267 LEU A O 1 ATOM 2014 C CB . LEU A 1 267 ? 59.471 -12.637 33.195 1.00 76.53 ? 267 LEU A CB 1 ATOM 2015 C CG . LEU A 1 267 ? 59.838 -11.190 33.520 1.00 82.45 ? 267 LEU A CG 1 ATOM 2016 C CD1 . LEU A 1 267 ? 60.349 -10.459 32.280 1.00 80.21 ? 267 LEU A CD1 1 ATOM 2017 C CD2 . LEU A 1 267 ? 58.644 -10.460 34.124 1.00 77.53 ? 267 LEU A CD2 1 ATOM 2018 N N . CYS A 1 268 ? 56.871 -13.869 34.027 1.00 64.79 ? 268 CYS A N 1 ATOM 2019 C CA . CYS A 1 268 ? 55.660 -14.571 33.739 1.00 62.37 ? 268 CYS A CA 1 ATOM 2020 C C . CYS A 1 268 ? 55.485 -14.510 32.247 1.00 64.10 ? 268 CYS A C 1 ATOM 2021 O O . CYS A 1 268 ? 54.850 -15.363 31.618 1.00 61.76 ? 268 CYS A O 1 ATOM 2022 C CB . CYS A 1 268 ? 54.504 -13.855 34.443 1.00 61.11 ? 268 CYS A CB 1 ATOM 2023 S SG . CYS A 1 268 ? 54.799 -13.761 36.217 1.00 63.56 ? 268 CYS A SG 1 ATOM 2024 N N . TYR A 1 269 ? 56.095 -13.435 31.738 1.00 62.40 ? 269 TYR A N 1 ATOM 2025 C CA . TYR A 1 269 ? 56.167 -13.027 30.347 1.00 57.15 ? 269 TYR A CA 1 ATOM 2026 C C . TYR A 1 269 ? 57.594 -12.600 30.124 1.00 55.05 ? 269 TYR A C 1 ATOM 2027 O O . TYR A 1 269 ? 57.973 -11.463 30.388 1.00 42.48 ? 269 TYR A O 1 ATOM 2028 C CB . TYR A 1 269 ? 55.202 -11.858 30.001 1.00 50.43 ? 269 TYR A CB 1 ATOM 2029 C CG . TYR A 1 269 ? 53.737 -12.228 30.132 1.00 32.07 ? 269 TYR A CG 1 ATOM 2030 C CD1 . TYR A 1 269 ? 53.115 -13.035 29.180 1.00 26.48 ? 269 TYR A CD1 1 ATOM 2031 C CD2 . TYR A 1 269 ? 52.995 -11.817 31.238 1.00 26.72 ? 269 TYR A CD2 1 ATOM 2032 C CE1 . TYR A 1 269 ? 51.775 -13.391 29.330 1.00 23.78 ? 269 TYR A CE1 1 ATOM 2033 C CE2 . TYR A 1 269 ? 51.657 -12.169 31.398 1.00 12.88 ? 269 TYR A CE2 1 ATOM 2034 C CZ . TYR A 1 269 ? 51.039 -12.955 30.433 1.00 17.37 ? 269 TYR A CZ 1 ATOM 2035 O OH . TYR A 1 269 ? 49.711 -13.294 30.584 1.00 23.44 ? 269 TYR A OH 1 ATOM 2036 N N . PRO A 1 270 ? 58.389 -13.551 29.670 1.00 55.47 ? 270 PRO A N 1 ATOM 2037 C CA . PRO A 1 270 ? 59.800 -13.315 29.433 1.00 51.57 ? 270 PRO A CA 1 ATOM 2038 C C . PRO A 1 270 ? 60.093 -12.340 28.269 1.00 49.65 ? 270 PRO A C 1 ATOM 2039 O O . PRO A 1 270 ? 60.963 -11.464 28.366 1.00 50.74 ? 270 PRO A O 1 ATOM 2040 C CB . PRO A 1 270 ? 60.394 -14.716 29.195 1.00 54.72 ? 270 PRO A CB 1 ATOM 2041 C CG . PRO A 1 270 ? 59.236 -15.719 29.056 1.00 58.59 ? 270 PRO A CG 1 ATOM 2042 C CD . PRO A 1 270 ? 57.966 -14.962 29.394 1.00 53.83 ? 270 PRO A CD 1 ATOM 2043 N N . THR A 1 271 ? 59.348 -12.524 27.168 1.00 24.65 ? 271 THR A N 1 ATOM 2044 C CA . THR A 1 271 ? 59.451 -11.759 25.970 1.00 10.97 ? 271 THR A CA 1 ATOM 2045 C C . THR A 1 271 ? 59.617 -10.263 26.212 1.00 33.76 ? 271 THR A C 1 ATOM 2046 O O . THR A 1 271 ? 60.134 -9.524 25.372 1.00 28.58 ? 271 THR A O 1 ATOM 2047 C CB . THR A 1 271 ? 58.203 -12.043 25.150 1.00 54.66 ? 271 THR A CB 1 ATOM 2048 O OG1 . THR A 1 271 ? 58.106 -13.440 24.920 1.00 42.83 ? 271 THR A OG1 1 ATOM 2049 C CG2 . THR A 1 271 ? 58.208 -11.204 23.867 1.00 56.45 ? 271 THR A CG2 1 ATOM 2050 N N . LEU A 1 272 ? 59.158 -9.801 27.389 1.00 49.91 ? 272 LEU A N 1 ATOM 2051 C CA . LEU A 1 272 ? 59.258 -8.368 27.771 1.00 44.90 ? 272 LEU A CA 1 ATOM 2052 C C . LEU A 1 272 ? 60.650 -8.066 28.151 1.00 47.50 ? 272 LEU A C 1 ATOM 2053 O O . LEU A 1 272 ? 61.002 -6.930 28.456 1.00 45.14 ? 272 LEU A O 1 ATOM 2054 C CB . LEU A 1 272 ? 58.444 -7.878 28.997 1.00 36.97 ? 272 LEU A CB 1 ATOM 2055 C CG . LEU A 1 272 ? 57.157 -8.618 29.255 1.00 35.19 ? 272 LEU A CG 1 ATOM 2056 C CD1 . LEU A 1 272 ? 56.707 -8.450 30.700 1.00 26.36 ? 272 LEU A CD1 1 ATOM 2057 C CD2 . LEU A 1 272 ? 56.102 -8.143 28.266 1.00 57.78 ? 272 LEU A CD2 1 ATOM 2058 N N . GLN A 1 273 ? 61.415 -9.121 28.189 1.00 55.66 ? 273 GLN A N 1 ATOM 2059 C CA . GLN A 1 273 ? 62.767 -8.934 28.539 1.00 57.81 ? 273 GLN A CA 1 ATOM 2060 C C . GLN A 1 273 ? 63.420 -8.362 27.298 1.00 57.51 ? 273 GLN A C 1 ATOM 2061 O O . GLN A 1 273 ? 64.125 -7.340 27.368 1.00 50.17 ? 273 GLN A O 1 ATOM 2062 C CB . GLN A 1 273 ? 63.393 -10.230 29.059 1.00 60.70 ? 273 GLN A CB 1 ATOM 2063 C CG . GLN A 1 273 ? 64.908 -10.090 29.225 1.00 100.00 ? 273 GLN A CG 1 ATOM 2064 C CD . GLN A 1 273 ? 65.233 -9.060 30.273 1.00 69.07 ? 273 GLN A CD 1 ATOM 2065 O OE1 . GLN A 1 273 ? 65.720 -9.399 31.354 1.00 74.59 ? 273 GLN A OE1 1 ATOM 2066 N NE2 . GLN A 1 273 ? 64.902 -7.809 29.981 1.00 77.13 ? 273 GLN A NE2 1 ATOM 2067 N N . ASP A 1 274 ? 63.113 -9.018 26.156 1.00 47.34 ? 274 ASP A N 1 ATOM 2068 C CA . ASP A 1 274 ? 63.639 -8.594 24.871 1.00 41.25 ? 274 ASP A CA 1 ATOM 2069 C C . ASP A 1 274 ? 63.267 -7.144 24.642 1.00 33.84 ? 274 ASP A C 1 ATOM 2070 O O . ASP A 1 274 ? 64.063 -6.351 24.160 1.00 24.27 ? 274 ASP A O 1 ATOM 2071 C CB . ASP A 1 274 ? 63.175 -9.518 23.761 1.00 37.11 ? 274 ASP A CB 1 ATOM 2072 C CG . ASP A 1 274 ? 62.838 -10.842 24.345 1.00 67.50 ? 274 ASP A CG 1 ATOM 2073 O OD1 . ASP A 1 274 ? 63.654 -11.522 24.948 1.00 82.74 ? 274 ASP A OD1 1 ATOM 2074 O OD2 . ASP A 1 274 ? 61.558 -11.107 24.265 1.00 87.68 ? 274 ASP A OD2 1 ATOM 2075 N N . ILE A 1 275 ? 62.049 -6.804 25.042 1.00 17.69 ? 275 ILE A N 1 ATOM 2076 C CA . ILE A 1 275 ? 61.594 -5.444 24.910 1.00 15.81 ? 275 ILE A CA 1 ATOM 2077 C C . ILE A 1 275 ? 62.543 -4.432 25.597 1.00 28.75 ? 275 ILE A C 1 ATOM 2078 O O . ILE A 1 275 ? 63.010 -3.500 24.977 1.00 37.88 ? 275 ILE A O 1 ATOM 2079 C CB . ILE A 1 275 ? 60.144 -5.221 25.396 1.00 20.68 ? 275 ILE A CB 1 ATOM 2080 C CG1 . ILE A 1 275 ? 59.769 -3.722 25.312 1.00 6.35 ? 275 ILE A CG1 1 ATOM 2081 C CG2 . ILE A 1 275 ? 59.082 -6.184 24.802 1.00 20.65 ? 275 ILE A CG2 1 ATOM 2082 N N . ASP A 1 276 ? 62.821 -4.566 26.891 1.00 37.53 ? 276 ASP A N 1 ATOM 2083 C CA . ASP A 1 276 ? 63.707 -3.601 27.563 1.00 44.71 ? 276 ASP A CA 1 ATOM 2084 C C . ASP A 1 276 ? 65.058 -3.597 26.854 1.00 44.53 ? 276 ASP A C 1 ATOM 2085 O O . ASP A 1 276 ? 65.848 -2.634 26.942 1.00 19.89 ? 276 ASP A O 1 ATOM 2086 C CB . ASP A 1 276 ? 63.855 -3.875 29.098 1.00 52.27 ? 276 ASP A CB 1 ATOM 2087 C CG . ASP A 1 276 ? 63.435 -2.758 30.052 1.00 75.13 ? 276 ASP A CG 1 ATOM 2088 O OD1 . ASP A 1 276 ? 62.479 -1.989 29.586 1.00 68.74 ? 276 ASP A OD1 1 ATOM 2089 O OD2 . ASP A 1 276 ? 63.917 -2.628 31.178 1.00 75.87 ? 276 ASP A OD2 1 ATOM 2090 N N . ASP A 1 277 ? 65.264 -4.726 26.133 1.00 51.31 ? 277 ASP A N 1 ATOM 2091 C CA . ASP A 1 277 ? 66.448 -4.986 25.340 1.00 53.53 ? 277 ASP A CA 1 ATOM 2092 C C . ASP A 1 277 ? 66.437 -4.059 24.084 1.00 43.39 ? 277 ASP A C 1 ATOM 2093 O O . ASP A 1 277 ? 67.242 -3.139 23.931 1.00 34.69 ? 277 ASP A O 1 ATOM 2094 C CB . ASP A 1 277 ? 66.684 -6.521 25.081 1.00 56.85 ? 277 ASP A CB 1 ATOM 2095 C CG . ASP A 1 277 ? 66.837 -7.360 26.348 1.00 61.44 ? 277 ASP A CG 1 ATOM 2096 O OD1 . ASP A 1 277 ? 66.964 -6.830 27.435 1.00 53.68 ? 277 ASP A OD1 1 ATOM 2097 O OD2 . ASP A 1 277 ? 66.855 -8.704 26.166 1.00 40.23 ? 277 ASP A OD2 1 ATOM 2098 N N . TYR A 1 278 ? 65.494 -4.248 23.211 1.00 32.11 ? 278 TYR A N 1 ATOM 2099 C CA . TYR A 1 278 ? 65.374 -3.431 22.025 1.00 42.62 ? 278 TYR A CA 1 ATOM 2100 C C . TYR A 1 278 ? 65.411 -1.871 22.253 1.00 62.50 ? 278 TYR A C 1 ATOM 2101 O O . TYR A 1 278 ? 65.914 -1.129 21.379 1.00 61.76 ? 278 TYR A O 1 ATOM 2102 C CB . TYR A 1 278 ? 64.115 -3.886 21.305 1.00 50.18 ? 278 TYR A CB 1 ATOM 2103 C CG . TYR A 1 278 ? 63.914 -3.218 19.997 1.00 76.14 ? 278 TYR A CG 1 ATOM 2104 C CD1 . TYR A 1 278 ? 63.646 -1.843 19.865 1.00 82.77 ? 278 TYR A CD1 1 ATOM 2105 C CD2 . TYR A 1 278 ? 63.904 -4.008 18.857 1.00 85.48 ? 278 TYR A CD2 1 ATOM 2106 C CE1 . TYR A 1 278 ? 63.492 -1.283 18.617 1.00 86.97 ? 278 TYR A CE1 1 ATOM 2107 C CE2 . TYR A 1 278 ? 63.727 -3.460 17.587 1.00 95.82 ? 278 TYR A CE2 1 ATOM 2108 C CZ . TYR A 1 278 ? 63.448 -2.080 17.469 1.00 100.00 ? 278 TYR A CZ 1 ATOM 2109 O OH . TYR A 1 278 ? 63.362 -1.566 16.210 1.00 100.00 ? 278 TYR A OH 1 ATOM 2110 N N . LEU A 1 279 ? 64.803 -1.411 23.371 1.00 58.59 ? 279 LEU A N 1 ATOM 2111 C CA . LEU A 1 279 ? 64.658 -0.004 23.794 1.00 48.18 ? 279 LEU A CA 1 ATOM 2112 C C . LEU A 1 279 ? 65.990 0.635 24.077 1.00 51.66 ? 279 LEU A C 1 ATOM 2113 O O . LEU A 1 279 ? 66.288 1.702 23.571 1.00 60.80 ? 279 LEU A O 1 ATOM 2114 C CB . LEU A 1 279 ? 63.836 0.140 25.104 1.00 48.32 ? 279 LEU A CB 1 ATOM 2115 C CG . LEU A 1 279 ? 62.362 0.442 24.889 1.00 52.64 ? 279 LEU A CG 1 ATOM 2116 C CD1 . LEU A 1 279 ? 62.111 0.608 23.396 1.00 60.03 ? 279 LEU A CD1 1 ATOM 2117 C CD2 . LEU A 1 279 ? 61.512 -0.712 25.409 1.00 14.56 ? 279 LEU A CD2 1 ATOM 2118 N N . ASN A 1 280 ? 66.777 -0.020 24.918 1.00 49.58 ? 280 ASN A N 1 ATOM 2119 C CA . ASN A 1 280 ? 68.094 0.450 25.310 1.00 56.78 ? 280 ASN A CA 1 ATOM 2120 C C . ASN A 1 280 ? 69.099 0.456 24.173 1.00 78.26 ? 280 ASN A C 1 ATOM 2121 O O . ASN A 1 280 ? 70.063 1.232 24.260 1.00 86.98 ? 280 ASN A O 1 ATOM 2122 C CB . ASN A 1 280 ? 68.728 -0.457 26.385 1.00 78.74 ? 280 ASN A CB 1 ATOM 2123 C CG . ASN A 1 280 ? 68.303 -0.212 27.813 1.00 95.95 ? 280 ASN A CG 1 ATOM 2124 O OD1 . ASN A 1 280 ? 68.731 0.783 28.430 1.00 69.89 ? 280 ASN A OD1 1 ATOM 2125 N ND2 . ASN A 1 280 ? 67.637 -1.232 28.388 1.00 31.40 ? 280 ASN A ND2 1 ATOM 2126 N N . GLN A 1 281 ? 68.900 -0.436 23.153 1.00 62.02 ? 281 GLN A N 1 ATOM 2127 C CA . GLN A 1 281 ? 69.832 -0.540 22.024 1.00 45.97 ? 281 GLN A CA 1 ATOM 2128 C C . GLN A 1 281 ? 70.304 0.820 21.517 1.00 63.24 ? 281 GLN A C 1 ATOM 2129 O O . GLN A 1 281 ? 69.615 1.843 21.701 1.00 61.00 ? 281 GLN A O 1 ATOM 2130 C CB . GLN A 1 281 ? 69.538 -1.623 20.977 1.00 35.65 ? 281 GLN A CB 1 ATOM 2131 N N . ASP A 1 282 ? 71.499 0.830 20.916 1.00 70.81 ? 282 ASP A N 1 ATOM 2132 C CA . ASP A 1 282 ? 72.103 2.061 20.425 1.00 77.66 ? 282 ASP A CA 1 ATOM 2133 C C . ASP A 1 282 ? 71.457 2.769 19.267 1.00 68.92 ? 282 ASP A C 1 ATOM 2134 O O . ASP A 1 282 ? 71.407 4.005 19.262 1.00 57.29 ? 282 ASP A O 1 ATOM 2135 C CB . ASP A 1 282 ? 73.637 2.117 20.428 1.00 88.34 ? 282 ASP A CB 1 ATOM 2136 C CG . ASP A 1 282 ? 74.217 2.233 21.831 1.00 100.00 ? 282 ASP A CG 1 ATOM 2137 O OD1 . ASP A 1 282 ? 74.457 1.261 22.538 1.00 100.00 ? 282 ASP A OD1 1 ATOM 2138 O OD2 . ASP A 1 282 ? 74.372 3.480 22.252 1.00 100.00 ? 282 ASP A OD2 1 ATOM 2139 N N . TYR A 1 283 ? 70.968 1.988 18.306 1.00 62.25 ? 283 TYR A N 1 ATOM 2140 C CA . TYR A 1 283 ? 70.294 2.580 17.183 1.00 61.32 ? 283 TYR A CA 1 ATOM 2141 C C . TYR A 1 283 ? 68.918 3.090 17.633 1.00 65.06 ? 283 TYR A C 1 ATOM 2142 O O . TYR A 1 283 ? 68.598 4.295 17.441 1.00 46.94 ? 283 TYR A O 1 ATOM 2143 C CB . TYR A 1 283 ? 70.201 1.639 15.965 1.00 61.19 ? 283 TYR A CB 1 ATOM 2144 C CG . TYR A 1 283 ? 69.429 0.351 16.181 1.00 60.02 ? 283 TYR A CG 1 ATOM 2145 C CD1 . TYR A 1 283 ? 69.741 -0.497 17.244 1.00 67.29 ? 283 TYR A CD1 1 ATOM 2146 C CD2 . TYR A 1 283 ? 68.412 -0.034 15.302 1.00 54.61 ? 283 TYR A CD2 1 ATOM 2147 C CE1 . TYR A 1 283 ? 69.054 -1.697 17.442 1.00 74.65 ? 283 TYR A CE1 1 ATOM 2148 C CE2 . TYR A 1 283 ? 67.707 -1.226 15.485 1.00 37.12 ? 283 TYR A CE2 1 ATOM 2149 C CZ . TYR A 1 283 ? 68.031 -2.055 16.562 1.00 83.83 ? 283 TYR A CZ 1 ATOM 2150 O OH . TYR A 1 283 ? 67.345 -3.229 16.765 1.00 100.00 ? 283 TYR A OH 1 ATOM 2151 N N . VAL A 1 284 ? 68.137 2.145 18.256 1.00 59.67 ? 284 VAL A N 1 ATOM 2152 C CA . VAL A 1 284 ? 66.782 2.399 18.771 1.00 54.77 ? 284 VAL A CA 1 ATOM 2153 C C . VAL A 1 284 ? 66.712 3.556 19.817 1.00 61.49 ? 284 VAL A C 1 ATOM 2154 O O . VAL A 1 284 ? 65.802 4.393 19.814 1.00 65.53 ? 284 VAL A O 1 ATOM 2155 C CB . VAL A 1 284 ? 65.921 1.136 19.017 1.00 45.21 ? 284 VAL A CB 1 ATOM 2156 N N . LYS A 1 285 ? 67.696 3.653 20.692 1.00 36.33 ? 285 LYS A N 1 ATOM 2157 C CA . LYS A 1 285 ? 67.643 4.741 21.622 1.00 43.26 ? 285 LYS A CA 1 ATOM 2158 C C . LYS A 1 285 ? 67.873 6.111 20.951 1.00 54.49 ? 285 LYS A C 1 ATOM 2159 O O . LYS A 1 285 ? 67.516 7.158 21.515 1.00 43.28 ? 285 LYS A O 1 ATOM 2160 C CB . LYS A 1 285 ? 68.682 4.520 22.695 1.00 51.80 ? 285 LYS A CB 1 ATOM 2161 C CG . LYS A 1 285 ? 68.113 3.870 23.932 1.00 78.89 ? 285 LYS A CG 1 ATOM 2162 C CD . LYS A 1 285 ? 68.702 4.457 25.202 1.00 95.37 ? 285 LYS A CD 1 ATOM 2163 C CE . LYS A 1 285 ? 69.889 3.669 25.729 1.00 78.43 ? 285 LYS A CE 1 ATOM 2164 N NZ . LYS A 1 285 ? 71.053 4.512 26.060 1.00 79.16 ? 285 LYS A NZ 1 ATOM 2165 N N . GLU A 1 286 ? 68.484 6.073 19.739 1.00 63.54 ? 286 GLU A N 1 ATOM 2166 C CA . GLU A 1 286 ? 68.883 7.223 18.896 1.00 62.06 ? 286 GLU A CA 1 ATOM 2167 C C . GLU A 1 286 ? 67.794 8.003 18.230 1.00 60.27 ? 286 GLU A C 1 ATOM 2168 O O . GLU A 1 286 ? 67.697 9.219 18.404 1.00 53.17 ? 286 GLU A O 1 ATOM 2169 C CB . GLU A 1 286 ? 69.816 6.778 17.762 1.00 64.54 ? 286 GLU A CB 1 ATOM 2170 C CG . GLU A 1 286 ? 71.277 6.585 18.204 1.00 100.00 ? 286 GLU A CG 1 ATOM 2171 C CD . GLU A 1 286 ? 71.488 6.896 19.665 1.00 100.00 ? 286 GLU A CD 1 ATOM 2172 O OE1 . GLU A 1 286 ? 71.403 8.198 19.895 1.00 76.94 ? 286 GLU A OE1 1 ATOM 2173 O OE2 . GLU A 1 286 ? 71.674 6.026 20.529 1.00 84.68 ? 286 GLU A OE2 1 ATOM 2174 N N . ALA A 1 287 ? 67.032 7.255 17.428 1.00 70.02 ? 287 ALA A N 1 ATOM 2175 C CA . ALA A 1 287 ? 65.906 7.715 16.613 1.00 68.81 ? 287 ALA A CA 1 ATOM 2176 C C . ALA A 1 287 ? 64.971 8.660 17.341 1.00 88.42 ? 287 ALA A C 1 ATOM 2177 O O . ALA A 1 287 ? 64.796 9.834 16.981 1.00 91.56 ? 287 ALA A O 1 ATOM 2178 C CB . ALA A 1 287 ? 65.131 6.500 16.091 1.00 62.65 ? 287 ALA A CB 1 ATOM 2179 N N . VAL A 1 288 ? 64.421 8.056 18.367 1.00 86.88 ? 288 VAL A N 1 ATOM 2180 C CA . VAL A 1 288 ? 63.495 8.652 19.268 1.00 80.68 ? 288 VAL A CA 1 ATOM 2181 C C . VAL A 1 288 ? 64.078 9.891 19.871 1.00 76.09 ? 288 VAL A C 1 ATOM 2182 O O . VAL A 1 288 ? 63.340 10.830 20.227 1.00 73.37 ? 288 VAL A O 1 ATOM 2183 C CB . VAL A 1 288 ? 63.251 7.673 20.367 1.00 82.40 ? 288 VAL A CB 1 ATOM 2184 C CG1 . VAL A 1 288 ? 62.516 8.391 21.466 1.00 85.05 ? 288 VAL A CG1 1 ATOM 2185 C CG2 . VAL A 1 288 ? 62.457 6.496 19.821 1.00 81.92 ? 288 VAL A CG2 1 ATOM 2186 N N . GLY A 1 289 ? 65.412 9.853 19.966 1.00 67.28 ? 289 GLY A N 1 ATOM 2187 C CA . GLY A 1 289 ? 66.197 10.937 20.522 1.00 69.01 ? 289 GLY A CA 1 ATOM 2188 C C . GLY A 1 289 ? 65.736 11.203 21.936 1.00 66.74 ? 289 GLY A C 1 ATOM 2189 O O . GLY A 1 289 ? 65.248 12.278 22.287 1.00 57.73 ? 289 GLY A O 1 ATOM 2190 N N . ALA A 1 290 ? 65.865 10.177 22.740 1.00 65.52 ? 290 ALA A N 1 ATOM 2191 C CA . ALA A 1 290 ? 65.457 10.303 24.101 1.00 69.29 ? 290 ALA A CA 1 ATOM 2192 C C . ALA A 1 290 ? 66.674 10.723 24.918 1.00 95.21 ? 290 ALA A C 1 ATOM 2193 O O . ALA A 1 290 ? 67.767 10.206 24.687 1.00 96.87 ? 290 ALA A O 1 ATOM 2194 C CB . ALA A 1 290 ? 64.828 9.005 24.552 1.00 69.38 ? 290 ALA A CB 1 ATOM 2195 N N . GLU A 1 291 ? 66.478 11.681 25.846 1.00 94.13 ? 291 GLU A N 1 ATOM 2196 C CA . GLU A 1 291 ? 67.546 12.217 26.688 1.00 85.81 ? 291 GLU A CA 1 ATOM 2197 C C . GLU A 1 291 ? 67.866 11.420 27.948 1.00 64.16 ? 291 GLU A C 1 ATOM 2198 O O . GLU A 1 291 ? 68.534 11.909 28.857 1.00 56.22 ? 291 GLU A O 1 ATOM 2199 C CB . GLU A 1 291 ? 67.322 13.693 26.979 1.00 88.23 ? 291 GLU A CB 1 ATOM 2200 N N . VAL A 1 292 ? 67.405 10.179 27.998 1.00 64.54 ? 292 VAL A N 1 ATOM 2201 C CA . VAL A 1 292 ? 67.636 9.271 29.136 1.00 65.66 ? 292 VAL A CA 1 ATOM 2202 C C . VAL A 1 292 ? 68.871 8.380 28.886 1.00 91.39 ? 292 VAL A C 1 ATOM 2203 O O . VAL A 1 292 ? 69.217 8.145 27.734 1.00 100.00 ? 292 VAL A O 1 ATOM 2204 C CB . VAL A 1 292 ? 66.378 8.437 29.378 1.00 54.93 ? 292 VAL A CB 1 ATOM 2205 C CG1 . VAL A 1 292 ? 66.697 6.960 29.604 1.00 44.13 ? 292 VAL A CG1 1 ATOM 2206 C CG2 . VAL A 1 292 ? 65.579 9.034 30.525 1.00 53.18 ? 292 VAL A CG2 1 ATOM 2207 N N . ASP A 1 293 ? 69.556 7.875 29.933 1.00 85.43 ? 293 ASP A N 1 ATOM 2208 C CA . ASP A 1 293 ? 70.745 7.032 29.710 1.00 84.33 ? 293 ASP A CA 1 ATOM 2209 C C . ASP A 1 293 ? 70.493 5.507 29.695 1.00 99.34 ? 293 ASP A C 1 ATOM 2210 O O . ASP A 1 293 ? 71.140 4.746 28.959 1.00 100.00 ? 293 ASP A O 1 ATOM 2211 C CB . ASP A 1 293 ? 71.902 7.397 30.677 1.00 80.20 ? 293 ASP A CB 1 ATOM 2212 C CG . ASP A 1 293 ? 73.171 7.871 30.009 1.00 67.97 ? 293 ASP A CG 1 ATOM 2213 O OD1 . ASP A 1 293 ? 73.380 7.862 28.791 1.00 65.81 ? 293 ASP A OD1 1 ATOM 2214 O OD2 . ASP A 1 293 ? 74.011 8.353 30.889 1.00 70.05 ? 293 ASP A OD2 1 ATOM 2215 N N . HIS A 1 294 ? 69.546 5.071 30.533 1.00 93.99 ? 294 HIS A N 1 ATOM 2216 C CA . HIS A 1 294 ? 69.172 3.669 30.726 1.00 85.18 ? 294 HIS A CA 1 ATOM 2217 C C . HIS A 1 294 ? 67.644 3.595 30.922 1.00 76.45 ? 294 HIS A C 1 ATOM 2218 O O . HIS A 1 294 ? 67.123 4.258 31.811 1.00 79.21 ? 294 HIS A O 1 ATOM 2219 C CB . HIS A 1 294 ? 69.944 3.171 31.980 1.00 83.48 ? 294 HIS A CB 1 ATOM 2220 C CG . HIS A 1 294 ? 69.792 1.739 32.362 1.00 84.78 ? 294 HIS A CG 1 ATOM 2221 N ND1 . HIS A 1 294 ? 68.536 1.099 32.409 1.00 83.45 ? 294 HIS A ND1 1 ATOM 2222 C CD2 . HIS A 1 294 ? 70.725 0.861 32.740 1.00 84.11 ? 294 HIS A CD2 1 ATOM 2223 C CE1 . HIS A 1 294 ? 68.753 -0.118 32.764 1.00 82.57 ? 294 HIS A CE1 1 ATOM 2224 N NE2 . HIS A 1 294 ? 70.064 -0.314 33.054 1.00 82.68 ? 294 HIS A NE2 1 ATOM 2225 N N . TYR A 1 295 ? 66.937 2.802 30.100 1.00 55.44 ? 295 TYR A N 1 ATOM 2226 C CA . TYR A 1 295 ? 65.502 2.660 30.219 1.00 38.85 ? 295 TYR A CA 1 ATOM 2227 C C . TYR A 1 295 ? 65.019 1.399 30.903 1.00 31.37 ? 295 TYR A C 1 ATOM 2228 O O . TYR A 1 295 ? 65.249 0.267 30.476 1.00 15.10 ? 295 TYR A O 1 ATOM 2229 C CB . TYR A 1 295 ? 64.795 2.805 28.875 1.00 32.83 ? 295 TYR A CB 1 ATOM 2230 C CG . TYR A 1 295 ? 63.368 2.331 28.872 1.00 27.83 ? 295 TYR A CG 1 ATOM 2231 C CD1 . TYR A 1 295 ? 63.037 0.981 28.723 1.00 27.17 ? 295 TYR A CD1 1 ATOM 2232 C CD2 . TYR A 1 295 ? 62.341 3.268 28.944 1.00 30.19 ? 295 TYR A CD2 1 ATOM 2233 C CE1 . TYR A 1 295 ? 61.706 0.552 28.700 1.00 27.31 ? 295 TYR A CE1 1 ATOM 2234 C CE2 . TYR A 1 295 ? 61.007 2.850 28.817 1.00 39.88 ? 295 TYR A CE2 1 ATOM 2235 C CZ . TYR A 1 295 ? 60.687 1.496 28.747 1.00 41.55 ? 295 TYR A CZ 1 ATOM 2236 O OH . TYR A 1 295 ? 59.381 1.044 28.746 1.00 35.23 ? 295 TYR A OH 1 ATOM 2237 N N . GLU A 1 296 ? 64.256 1.636 31.946 1.00 32.12 ? 296 GLU A N 1 ATOM 2238 C CA . GLU A 1 296 ? 63.646 0.590 32.698 1.00 22.06 ? 296 GLU A CA 1 ATOM 2239 C C . GLU A 1 296 ? 62.157 0.585 32.447 1.00 16.97 ? 296 GLU A C 1 ATOM 2240 O O . GLU A 1 296 ? 61.555 1.604 32.032 1.00 21.78 ? 296 GLU A O 1 ATOM 2241 C CB . GLU A 1 296 ? 63.953 0.728 34.181 1.00 26.74 ? 296 GLU A CB 1 ATOM 2242 C CG . GLU A 1 296 ? 65.278 0.020 34.518 1.00 92.37 ? 296 GLU A CG 1 ATOM 2243 C CD . GLU A 1 296 ? 65.458 -0.238 35.981 1.00 97.85 ? 296 GLU A CD 1 ATOM 2244 O OE1 . GLU A 1 296 ? 65.326 0.844 36.712 1.00 50.45 ? 296 GLU A OE1 1 ATOM 2245 O OE2 . GLU A 1 296 ? 65.671 -1.343 36.442 1.00 50.33 ? 296 GLU A OE2 1 ATOM 2246 N N . SER A 1 297 ? 61.560 -0.568 32.662 1.00 1.00 ? 297 SER A N 1 ATOM 2247 C CA . SER A 1 297 ? 60.157 -0.654 32.457 1.00 1.00 ? 297 SER A CA 1 ATOM 2248 C C . SER A 1 297 ? 59.424 0.136 33.502 1.00 16.85 ? 297 SER A C 1 ATOM 2249 O O . SER A 1 297 ? 58.621 1.002 33.179 1.00 19.64 ? 297 SER A O 1 ATOM 2250 C CB . SER A 1 297 ? 59.652 -2.067 32.386 1.00 8.82 ? 297 SER A CB 1 ATOM 2251 O OG . SER A 1 297 ? 60.058 -2.643 31.149 1.00 94.26 ? 297 SER A OG 1 ATOM 2252 N N . CYS A 1 298 ? 59.720 -0.200 34.766 1.00 31.08 ? 298 CYS A N 1 ATOM 2253 C CA . CYS A 1 298 ? 59.131 0.405 35.947 1.00 30.85 ? 298 CYS A CA 1 ATOM 2254 C C . CYS A 1 298 ? 60.195 0.966 36.882 1.00 36.65 ? 298 CYS A C 1 ATOM 2255 O O . CYS A 1 298 ? 61.339 0.529 36.887 1.00 45.95 ? 298 CYS A O 1 ATOM 2256 C CB . CYS A 1 298 ? 58.103 -0.493 36.706 1.00 29.12 ? 298 CYS A CB 1 ATOM 2257 S SG . CYS A 1 298 ? 56.988 -1.478 35.649 1.00 42.50 ? 298 CYS A SG 1 ATOM 2258 N N . ASN A 1 299 ? 59.777 1.957 37.672 1.00 15.74 ? 299 ASN A N 1 ATOM 2259 C CA . ASN A 1 299 ? 60.593 2.636 38.632 1.00 16.24 ? 299 ASN A CA 1 ATOM 2260 C C . ASN A 1 299 ? 60.175 2.375 40.094 1.00 48.64 ? 299 ASN A C 1 ATOM 2261 O O . ASN A 1 299 ? 59.265 3.037 40.597 1.00 50.82 ? 299 ASN A O 1 ATOM 2262 C CB . ASN A 1 299 ? 60.494 4.149 38.351 1.00 19.68 ? 299 ASN A CB 1 ATOM 2263 C CG . ASN A 1 299 ? 61.387 4.909 39.298 1.00 62.37 ? 299 ASN A CG 1 ATOM 2264 O OD1 . ASN A 1 299 ? 62.312 4.314 39.877 1.00 61.48 ? 299 ASN A OD1 1 ATOM 2265 N ND2 . ASN A 1 299 ? 61.123 6.205 39.474 1.00 65.71 ? 299 ASN A ND2 1 ATOM 2266 N N . PHE A 1 300 ? 60.873 1.431 40.758 1.00 53.35 ? 300 PHE A N 1 ATOM 2267 C CA . PHE A 1 300 ? 60.676 1.009 42.165 1.00 43.39 ? 300 PHE A CA 1 ATOM 2268 C C . PHE A 1 300 ? 60.235 2.151 43.061 1.00 24.75 ? 300 PHE A C 1 ATOM 2269 O O . PHE A 1 300 ? 59.275 2.016 43.836 1.00 37.19 ? 300 PHE A O 1 ATOM 2270 C CB . PHE A 1 300 ? 62.010 0.429 42.724 1.00 44.93 ? 300 PHE A CB 1 ATOM 2271 C CG . PHE A 1 300 ? 61.963 -0.328 44.039 1.00 47.24 ? 300 PHE A CG 1 ATOM 2272 C CD1 . PHE A 1 300 ? 61.313 -1.560 44.123 1.00 55.10 ? 300 PHE A CD1 1 ATOM 2273 C CD2 . PHE A 1 300 ? 62.601 0.170 45.178 1.00 52.97 ? 300 PHE A CD2 1 ATOM 2274 C CE1 . PHE A 1 300 ? 61.260 -2.270 45.323 1.00 57.15 ? 300 PHE A CE1 1 ATOM 2275 C CE2 . PHE A 1 300 ? 62.564 -0.522 46.389 1.00 62.44 ? 300 PHE A CE2 1 ATOM 2276 C CZ . PHE A 1 300 ? 61.893 -1.745 46.452 1.00 62.81 ? 300 PHE A CZ 1 ATOM 2277 N N . ASP A 1 301 ? 60.961 3.268 42.933 1.00 18.49 ? 301 ASP A N 1 ATOM 2278 C CA . ASP A 1 301 ? 60.734 4.491 43.714 1.00 25.94 ? 301 ASP A CA 1 ATOM 2279 C C . ASP A 1 301 ? 59.342 4.990 43.598 1.00 18.02 ? 301 ASP A C 1 ATOM 2280 O O . ASP A 1 301 ? 58.687 5.148 44.637 1.00 12.53 ? 301 ASP A O 1 ATOM 2281 C CB . ASP A 1 301 ? 61.727 5.642 43.466 1.00 26.82 ? 301 ASP A CB 1 ATOM 2282 C CG . ASP A 1 301 ? 63.092 5.231 43.848 1.00 69.72 ? 301 ASP A CG 1 ATOM 2283 O OD1 . ASP A 1 301 ? 63.427 5.047 45.007 1.00 86.67 ? 301 ASP A OD1 1 ATOM 2284 O OD2 . ASP A 1 301 ? 63.804 4.896 42.807 1.00 92.72 ? 301 ASP A OD2 1 ATOM 2285 N N . ILE A 1 302 ? 58.946 5.243 42.333 1.00 9.83 ? 302 ILE A N 1 ATOM 2286 C CA . ILE A 1 302 ? 57.606 5.724 42.075 1.00 8.95 ? 302 ILE A CA 1 ATOM 2287 C C . ILE A 1 302 ? 56.618 4.749 42.731 1.00 17.90 ? 302 ILE A C 1 ATOM 2288 O O . ILE A 1 302 ? 55.761 5.187 43.505 1.00 33.22 ? 302 ILE A O 1 ATOM 2289 C CB . ILE A 1 302 ? 57.285 5.994 40.596 1.00 10.50 ? 302 ILE A CB 1 ATOM 2290 C CG1 . ILE A 1 302 ? 55.769 5.893 40.451 1.00 15.52 ? 302 ILE A CG1 1 ATOM 2291 C CG2 . ILE A 1 302 ? 57.748 7.415 40.179 1.00 4.71 ? 302 ILE A CG2 1 ATOM 2292 N N . ASN A 1 303 ? 56.749 3.440 42.424 1.00 1.00 ? 303 ASN A N 1 ATOM 2293 C CA . ASN A 1 303 ? 55.897 2.419 43.006 1.00 9.99 ? 303 ASN A CA 1 ATOM 2294 C C . ASN A 1 303 ? 55.850 2.615 44.525 1.00 18.78 ? 303 ASN A C 1 ATOM 2295 O O . ASN A 1 303 ? 54.745 2.782 45.118 1.00 19.74 ? 303 ASN A O 1 ATOM 2296 C CB . ASN A 1 303 ? 56.239 0.944 42.587 1.00 1.00 ? 303 ASN A CB 1 ATOM 2297 C CG . ASN A 1 303 ? 55.549 -0.146 43.411 1.00 10.58 ? 303 ASN A CG 1 ATOM 2298 O OD1 . ASN A 1 303 ? 56.227 -0.920 44.086 1.00 92.26 ? 303 ASN A OD1 1 ATOM 2299 N ND2 . ASN A 1 303 ? 54.205 -0.229 43.393 1.00 51.65 ? 303 ASN A ND2 1 ATOM 2300 N N . ARG A 1 304 ? 57.053 2.668 45.112 1.00 1.00 ? 304 ARG A N 1 ATOM 2301 C CA . ARG A 1 304 ? 57.127 2.863 46.521 1.00 1.00 ? 304 ARG A CA 1 ATOM 2302 C C . ARG A 1 304 ? 56.364 4.101 47.043 1.00 14.57 ? 304 ARG A C 1 ATOM 2303 O O . ARG A 1 304 ? 55.539 4.050 47.996 1.00 11.08 ? 304 ARG A O 1 ATOM 2304 C CB . ARG A 1 304 ? 58.542 2.805 46.975 1.00 1.00 ? 304 ARG A CB 1 ATOM 2305 C CG . ARG A 1 304 ? 58.937 3.955 47.892 1.00 53.74 ? 304 ARG A CG 1 ATOM 2306 C CD . ARG A 1 304 ? 60.275 3.695 48.609 1.00 96.44 ? 304 ARG A CD 1 ATOM 2307 N NE . ARG A 1 304 ? 61.397 4.473 48.051 1.00 65.12 ? 304 ARG A NE 1 ATOM 2308 C CZ . ARG A 1 304 ? 61.397 5.805 47.941 1.00 100.00 ? 304 ARG A CZ 1 ATOM 2309 N NH1 . ARG A 1 304 ? 60.369 6.574 48.334 1.00 100.00 ? 304 ARG A NH1 1 ATOM 2310 N NH2 . ARG A 1 304 ? 62.469 6.386 47.417 1.00 100.00 ? 304 ARG A NH2 1 ATOM 2311 N N . ASN A 1 305 ? 56.612 5.237 46.440 1.00 1.00 ? 305 ASN A N 1 ATOM 2312 C CA . ASN A 1 305 ? 55.915 6.375 46.923 1.00 1.00 ? 305 ASN A CA 1 ATOM 2313 C C . ASN A 1 305 ? 54.428 6.304 46.797 1.00 12.18 ? 305 ASN A C 1 ATOM 2314 O O . ASN A 1 305 ? 53.725 6.858 47.633 1.00 14.61 ? 305 ASN A O 1 ATOM 2315 C CB . ASN A 1 305 ? 56.374 7.682 46.319 1.00 1.00 ? 305 ASN A CB 1 ATOM 2316 C CG . ASN A 1 305 ? 57.864 7.761 46.261 1.00 52.07 ? 305 ASN A CG 1 ATOM 2317 O OD1 . ASN A 1 305 ? 58.499 7.160 47.138 1.00 9.05 ? 305 ASN A OD1 1 ATOM 2318 N ND2 . ASN A 1 305 ? 58.392 8.493 45.238 1.00 18.10 ? 305 ASN A ND2 1 ATOM 2319 N N . PHE A 1 306 ? 53.942 5.661 45.761 1.00 1.00 ? 306 PHE A N 1 ATOM 2320 C CA . PHE A 1 306 ? 52.525 5.624 45.664 1.00 1.00 ? 306 PHE A CA 1 ATOM 2321 C C . PHE A 1 306 ? 51.985 4.806 46.811 1.00 7.42 ? 306 PHE A C 1 ATOM 2322 O O . PHE A 1 306 ? 51.006 5.132 47.485 1.00 10.23 ? 306 PHE A O 1 ATOM 2323 C CB . PHE A 1 306 ? 52.084 5.072 44.336 1.00 9.73 ? 306 PHE A CB 1 ATOM 2324 C CG . PHE A 1 306 ? 51.808 6.170 43.330 1.00 24.72 ? 306 PHE A CG 1 ATOM 2325 C CD1 . PHE A 1 306 ? 52.840 6.988 42.850 1.00 35.33 ? 306 PHE A CD1 1 ATOM 2326 C CD2 . PHE A 1 306 ? 50.510 6.365 42.844 1.00 33.67 ? 306 PHE A CD2 1 ATOM 2327 C CE1 . PHE A 1 306 ? 52.585 7.984 41.906 1.00 38.17 ? 306 PHE A CE1 1 ATOM 2328 C CE2 . PHE A 1 306 ? 50.234 7.364 41.905 1.00 38.18 ? 306 PHE A CE2 1 ATOM 2329 C CZ . PHE A 1 306 ? 51.278 8.169 41.438 1.00 31.64 ? 306 PHE A CZ 1 ATOM 2330 N N . LEU A 1 307 ? 52.663 3.721 47.040 1.00 14.34 ? 307 LEU A N 1 ATOM 2331 C CA . LEU A 1 307 ? 52.313 2.820 48.108 1.00 15.87 ? 307 LEU A CA 1 ATOM 2332 C C . LEU A 1 307 ? 52.426 3.536 49.443 1.00 7.28 ? 307 LEU A C 1 ATOM 2333 O O . LEU A 1 307 ? 51.549 3.431 50.264 1.00 6.01 ? 307 LEU A O 1 ATOM 2334 C CB . LEU A 1 307 ? 53.257 1.592 48.106 1.00 15.83 ? 307 LEU A CB 1 ATOM 2335 C CG . LEU A 1 307 ? 53.089 0.699 49.331 1.00 11.38 ? 307 LEU A CG 1 ATOM 2336 C CD1 . LEU A 1 307 ? 52.173 -0.413 48.957 1.00 1.00 ? 307 LEU A CD1 1 ATOM 2337 C CD2 . LEU A 1 307 ? 54.415 0.083 49.796 1.00 23.44 ? 307 LEU A CD2 1 ATOM 2338 N N . PHE A 1 308 ? 53.508 4.266 49.647 1.00 1.00 ? 308 PHE A N 1 ATOM 2339 C CA . PHE A 1 308 ? 53.613 4.934 50.890 1.00 1.00 ? 308 PHE A CA 1 ATOM 2340 C C . PHE A 1 308 ? 52.786 6.140 51.038 1.00 13.45 ? 308 PHE A C 1 ATOM 2341 O O . PHE A 1 308 ? 52.866 6.799 52.079 1.00 24.86 ? 308 PHE A O 1 ATOM 2342 C CB . PHE A 1 308 ? 55.027 5.167 51.374 1.00 18.15 ? 308 PHE A CB 1 ATOM 2343 C CG . PHE A 1 308 ? 55.596 3.807 51.663 1.00 39.27 ? 308 PHE A CG 1 ATOM 2344 C CD1 . PHE A 1 308 ? 55.185 3.094 52.791 1.00 43.73 ? 308 PHE A CD1 1 ATOM 2345 C CD2 . PHE A 1 308 ? 56.491 3.214 50.775 1.00 53.00 ? 308 PHE A CD2 1 ATOM 2346 C CE1 . PHE A 1 308 ? 55.668 1.819 53.076 1.00 49.64 ? 308 PHE A CE1 1 ATOM 2347 C CE2 . PHE A 1 308 ? 56.988 1.941 51.043 1.00 61.09 ? 308 PHE A CE2 1 ATOM 2348 C CZ . PHE A 1 308 ? 56.565 1.245 52.178 1.00 54.05 ? 308 PHE A CZ 1 ATOM 2349 N N . ALA A 1 309 ? 51.978 6.442 50.033 1.00 7.68 ? 309 ALA A N 1 ATOM 2350 C CA . ALA A 1 309 ? 51.138 7.618 50.143 1.00 1.00 ? 309 ALA A CA 1 ATOM 2351 C C . ALA A 1 309 ? 49.643 7.320 50.367 1.00 1.33 ? 309 ALA A C 1 ATOM 2352 O O . ALA A 1 309 ? 48.843 8.180 50.690 1.00 1.00 ? 309 ALA A O 1 ATOM 2353 C CB . ALA A 1 309 ? 51.383 8.532 48.979 1.00 2.80 ? 309 ALA A CB 1 ATOM 2354 N N . GLY A 1 310 ? 49.228 6.086 50.229 1.00 2.38 ? 310 GLY A N 1 ATOM 2355 C CA . GLY A 1 310 ? 47.825 5.824 50.467 1.00 1.00 ? 310 GLY A CA 1 ATOM 2356 C C . GLY A 1 310 ? 47.112 5.468 49.192 1.00 11.69 ? 310 GLY A C 1 ATOM 2357 O O . GLY A 1 310 ? 46.067 4.835 49.207 1.00 16.10 ? 310 GLY A O 1 ATOM 2358 N N . ASP A 1 311 ? 47.740 5.886 48.108 1.00 7.19 ? 311 ASP A N 1 ATOM 2359 C CA . ASP A 1 311 ? 47.272 5.749 46.780 1.00 1.00 ? 311 ASP A CA 1 ATOM 2360 C C . ASP A 1 311 ? 46.283 4.684 46.451 1.00 7.12 ? 311 ASP A C 1 ATOM 2361 O O . ASP A 1 311 ? 45.111 4.916 46.364 1.00 11.03 ? 311 ASP A O 1 ATOM 2362 C CB . ASP A 1 311 ? 48.182 6.193 45.659 1.00 1.00 ? 311 ASP A CB 1 ATOM 2363 C CG . ASP A 1 311 ? 47.344 7.027 44.770 1.00 36.91 ? 311 ASP A CG 1 ATOM 2364 O OD1 . ASP A 1 311 ? 47.090 8.189 45.081 1.00 31.34 ? 311 ASP A OD1 1 ATOM 2365 O OD2 . ASP A 1 311 ? 46.638 6.292 43.909 1.00 35.34 ? 311 ASP A OD2 1 ATOM 2366 N N . TRP A 1 312 ? 46.814 3.553 46.270 1.00 13.88 ? 312 TRP A N 1 ATOM 2367 C CA . TRP A 1 312 ? 46.151 2.364 45.965 1.00 12.04 ? 312 TRP A CA 1 ATOM 2368 C C . TRP A 1 312 ? 44.783 2.209 46.586 1.00 3.62 ? 312 TRP A C 1 ATOM 2369 O O . TRP A 1 312 ? 43.931 1.610 45.973 1.00 12.24 ? 312 TRP A O 1 ATOM 2370 C CB . TRP A 1 312 ? 47.051 1.393 46.729 1.00 21.25 ? 312 TRP A CB 1 ATOM 2371 C CG . TRP A 1 312 ? 47.110 0.019 46.192 1.00 24.70 ? 312 TRP A CG 1 ATOM 2372 C CD1 . TRP A 1 312 ? 46.233 -1.010 46.359 1.00 26.23 ? 312 TRP A CD1 1 ATOM 2373 C CD2 . TRP A 1 312 ? 48.172 -0.469 45.414 1.00 24.65 ? 312 TRP A CD2 1 ATOM 2374 N NE1 . TRP A 1 312 ? 46.691 -2.144 45.712 1.00 18.21 ? 312 TRP A NE1 1 ATOM 2375 C CE2 . TRP A 1 312 ? 47.879 -1.831 45.124 1.00 20.68 ? 312 TRP A CE2 1 ATOM 2376 C CE3 . TRP A 1 312 ? 49.344 0.139 44.973 1.00 26.64 ? 312 TRP A CE3 1 ATOM 2377 C CZ2 . TRP A 1 312 ? 48.735 -2.590 44.372 1.00 23.51 ? 312 TRP A CZ2 1 ATOM 2378 C CZ3 . TRP A 1 312 ? 50.197 -0.625 44.225 1.00 36.18 ? 312 TRP A CZ3 1 ATOM 2379 C CH2 . TRP A 1 312 ? 49.882 -1.960 43.914 1.00 38.54 ? 312 TRP A CH2 1 ATOM 2380 N N . MET A 1 313 ? 44.575 2.764 47.805 1.00 1.00 ? 313 MET A N 1 ATOM 2381 C CA . MET A 1 313 ? 43.287 2.587 48.495 1.00 1.00 ? 313 MET A CA 1 ATOM 2382 C C . MET A 1 313 ? 42.280 3.746 48.510 1.00 17.73 ? 313 MET A C 1 ATOM 2383 O O . MET A 1 313 ? 41.263 3.711 49.194 1.00 20.36 ? 313 MET A O 1 ATOM 2384 C CB . MET A 1 313 ? 43.417 1.944 49.881 1.00 2.34 ? 313 MET A CB 1 ATOM 2385 C CG . MET A 1 313 ? 43.846 0.451 49.996 1.00 18.74 ? 313 MET A CG 1 ATOM 2386 S SD . MET A 1 313 ? 43.269 -0.829 48.792 1.00 18.71 ? 313 MET A SD 1 ATOM 2387 C CE . MET A 1 313 ? 43.236 -2.263 49.911 1.00 15.33 ? 313 MET A CE 1 ATOM 2388 N N . LYS A 1 314 ? 42.549 4.775 47.743 1.00 9.77 ? 314 LYS A N 1 ATOM 2389 C CA . LYS A 1 314 ? 41.688 5.931 47.659 1.00 5.39 ? 314 LYS A CA 1 ATOM 2390 C C . LYS A 1 314 ? 40.477 5.675 46.716 1.00 15.02 ? 314 LYS A C 1 ATOM 2391 O O . LYS A 1 314 ? 40.558 4.985 45.711 1.00 15.99 ? 314 LYS A O 1 ATOM 2392 C CB . LYS A 1 314 ? 42.512 7.186 47.394 1.00 6.19 ? 314 LYS A CB 1 ATOM 2393 C CG . LYS A 1 314 ? 43.808 7.314 48.223 1.00 1.00 ? 314 LYS A CG 1 ATOM 2394 C CD . LYS A 1 314 ? 43.713 8.044 49.556 1.00 10.61 ? 314 LYS A CD 1 ATOM 2395 C CE . LYS A 1 314 ? 44.714 9.198 49.726 1.00 31.84 ? 314 LYS A CE 1 ATOM 2396 N NZ . LYS A 1 314 ? 45.827 9.231 48.743 1.00 24.69 ? 314 LYS A NZ 1 ATOM 2397 N N . PRO A 1 315 ? 39.313 6.208 47.072 1.00 23.22 ? 315 PRO A N 1 ATOM 2398 C CA . PRO A 1 315 ? 38.075 5.974 46.364 1.00 22.10 ? 315 PRO A CA 1 ATOM 2399 C C . PRO A 1 315 ? 37.913 6.904 45.187 1.00 35.86 ? 315 PRO A C 1 ATOM 2400 O O . PRO A 1 315 ? 37.147 7.902 45.199 1.00 25.67 ? 315 PRO A O 1 ATOM 2401 C CB . PRO A 1 315 ? 37.054 6.341 47.430 1.00 26.41 ? 315 PRO A CB 1 ATOM 2402 C CG . PRO A 1 315 ? 37.695 7.494 48.224 1.00 26.77 ? 315 PRO A CG 1 ATOM 2403 C CD . PRO A 1 315 ? 39.172 7.457 47.885 1.00 16.46 ? 315 PRO A CD 1 ATOM 2404 N N . TYR A 1 316 ? 38.678 6.556 44.170 1.00 30.72 ? 316 TYR A N 1 ATOM 2405 C CA . TYR A 1 316 ? 38.673 7.297 42.947 1.00 19.16 ? 316 TYR A CA 1 ATOM 2406 C C . TYR A 1 316 ? 37.503 6.787 42.155 1.00 18.00 ? 316 TYR A C 1 ATOM 2407 O O . TYR A 1 316 ? 37.170 7.238 41.078 1.00 5.64 ? 316 TYR A O 1 ATOM 2408 C CB . TYR A 1 316 ? 39.956 6.967 42.243 1.00 14.89 ? 316 TYR A CB 1 ATOM 2409 C CG . TYR A 1 316 ? 41.131 7.645 42.838 1.00 14.80 ? 316 TYR A CG 1 ATOM 2410 C CD1 . TYR A 1 316 ? 41.206 9.035 42.883 1.00 17.99 ? 316 TYR A CD1 1 ATOM 2411 C CD2 . TYR A 1 316 ? 42.180 6.890 43.355 1.00 16.14 ? 316 TYR A CD2 1 ATOM 2412 C CE1 . TYR A 1 316 ? 42.310 9.676 43.444 1.00 15.94 ? 316 TYR A CE1 1 ATOM 2413 C CE2 . TYR A 1 316 ? 43.300 7.517 43.898 1.00 28.69 ? 316 TYR A CE2 1 ATOM 2414 C CZ . TYR A 1 316 ? 43.362 8.909 43.942 1.00 23.34 ? 316 TYR A CZ 1 ATOM 2415 O OH . TYR A 1 316 ? 44.468 9.535 44.462 1.00 17.03 ? 316 TYR A OH 1 ATOM 2416 N N . HIS A 1 317 ? 36.840 5.798 42.701 1.00 23.96 ? 317 HIS A N 1 ATOM 2417 C CA . HIS A 1 317 ? 35.713 5.293 41.964 1.00 22.42 ? 317 HIS A CA 1 ATOM 2418 C C . HIS A 1 317 ? 34.643 6.365 41.898 1.00 21.82 ? 317 HIS A C 1 ATOM 2419 O O . HIS A 1 317 ? 33.772 6.345 41.027 1.00 22.70 ? 317 HIS A O 1 ATOM 2420 C CB . HIS A 1 317 ? 35.203 3.969 42.518 1.00 18.79 ? 317 HIS A CB 1 ATOM 2421 C CG . HIS A 1 317 ? 34.850 4.122 43.945 1.00 22.79 ? 317 HIS A CG 1 ATOM 2422 N ND1 . HIS A 1 317 ? 33.591 3.767 44.408 1.00 20.29 ? 317 HIS A ND1 1 ATOM 2423 C CD2 . HIS A 1 317 ? 35.580 4.590 44.997 1.00 28.55 ? 317 HIS A CD2 1 ATOM 2424 C CE1 . HIS A 1 317 ? 33.570 4.015 45.703 1.00 18.84 ? 317 HIS A CE1 1 ATOM 2425 N NE2 . HIS A 1 317 ? 34.739 4.514 46.091 1.00 25.13 ? 317 HIS A NE2 1 ATOM 2426 N N . THR A 1 318 ? 34.755 7.328 42.821 1.00 8.59 ? 318 THR A N 1 ATOM 2427 C CA . THR A 1 318 ? 33.832 8.457 42.925 1.00 15.72 ? 318 THR A CA 1 ATOM 2428 C C . THR A 1 318 ? 33.758 9.282 41.617 1.00 27.84 ? 318 THR A C 1 ATOM 2429 O O . THR A 1 318 ? 32.693 9.659 41.104 1.00 31.15 ? 318 THR A O 1 ATOM 2430 C CB . THR A 1 318 ? 34.054 9.306 44.241 1.00 27.88 ? 318 THR A CB 1 ATOM 2431 O OG1 . THR A 1 318 ? 35.366 9.876 44.372 1.00 21.38 ? 318 THR A OG1 1 ATOM 2432 C CG2 . THR A 1 318 ? 33.708 8.472 45.481 1.00 1.00 ? 318 THR A CG2 1 ATOM 2433 N N . ALA A 1 319 ? 34.931 9.532 41.071 1.00 13.85 ? 319 ALA A N 1 ATOM 2434 C CA . ALA A 1 319 ? 35.089 10.258 39.848 1.00 18.96 ? 319 ALA A CA 1 ATOM 2435 C C . ALA A 1 319 ? 34.236 9.661 38.749 1.00 28.77 ? 319 ALA A C 1 ATOM 2436 O O . ALA A 1 319 ? 33.694 10.372 37.909 1.00 35.69 ? 319 ALA A O 1 ATOM 2437 C CB . ALA A 1 319 ? 36.572 10.208 39.442 1.00 25.29 ? 319 ALA A CB 1 ATOM 2438 N N . VAL A 1 320 ? 34.133 8.335 38.752 1.00 23.54 ? 320 VAL A N 1 ATOM 2439 C CA . VAL A 1 320 ? 33.359 7.635 37.753 1.00 22.68 ? 320 VAL A CA 1 ATOM 2440 C C . VAL A 1 320 ? 31.917 8.140 37.639 1.00 30.22 ? 320 VAL A C 1 ATOM 2441 O O . VAL A 1 320 ? 31.396 8.375 36.538 1.00 25.40 ? 320 VAL A O 1 ATOM 2442 C CB . VAL A 1 320 ? 33.420 6.149 37.957 1.00 28.25 ? 320 VAL A CB 1 ATOM 2443 C CG1 . VAL A 1 320 ? 32.156 5.550 37.337 1.00 32.21 ? 320 VAL A CG1 1 ATOM 2444 C CG2 . VAL A 1 320 ? 34.679 5.616 37.261 1.00 26.16 ? 320 VAL A CG2 1 ATOM 2445 N N . THR A 1 321 ? 31.292 8.308 38.802 1.00 19.15 ? 321 THR A N 1 ATOM 2446 C CA . THR A 1 321 ? 29.946 8.799 38.902 1.00 20.73 ? 321 THR A CA 1 ATOM 2447 C C . THR A 1 321 ? 29.771 10.205 38.315 1.00 26.38 ? 321 THR A C 1 ATOM 2448 O O . THR A 1 321 ? 28.813 10.448 37.578 1.00 27.81 ? 321 THR A O 1 ATOM 2449 C CB . THR A 1 321 ? 29.517 8.723 40.353 1.00 33.15 ? 321 THR A CB 1 ATOM 2450 O OG1 . THR A 1 321 ? 29.463 7.351 40.703 1.00 16.26 ? 321 THR A OG1 1 ATOM 2451 C CG2 . THR A 1 321 ? 28.182 9.421 40.520 1.00 11.22 ? 321 THR A CG2 1 ATOM 2452 N N . ASP A 1 322 ? 30.704 11.122 38.627 1.00 15.63 ? 322 ASP A N 1 ATOM 2453 C CA . ASP A 1 322 ? 30.667 12.504 38.126 1.00 23.36 ? 322 ASP A CA 1 ATOM 2454 C C . ASP A 1 322 ? 30.688 12.511 36.639 1.00 27.93 ? 322 ASP A C 1 ATOM 2455 O O . ASP A 1 322 ? 29.847 13.114 36.019 1.00 38.56 ? 322 ASP A O 1 ATOM 2456 C CB . ASP A 1 322 ? 31.769 13.480 38.651 1.00 35.46 ? 322 ASP A CB 1 ATOM 2457 C CG . ASP A 1 322 ? 31.817 13.787 40.152 1.00 77.03 ? 322 ASP A CG 1 ATOM 2458 O OD1 . ASP A 1 322 ? 30.866 13.716 40.936 1.00 70.83 ? 322 ASP A OD1 1 ATOM 2459 O OD2 . ASP A 1 322 ? 33.033 14.124 40.532 1.00 77.42 ? 322 ASP A OD2 1 ATOM 2460 N N . LEU A 1 323 ? 31.661 11.815 36.108 1.00 29.00 ? 323 LEU A N 1 ATOM 2461 C CA . LEU A 1 323 ? 31.815 11.676 34.686 1.00 26.66 ? 323 LEU A CA 1 ATOM 2462 C C . LEU A 1 323 ? 30.531 11.126 34.071 1.00 31.40 ? 323 LEU A C 1 ATOM 2463 O O . LEU A 1 323 ? 30.041 11.657 33.063 1.00 20.32 ? 323 LEU A O 1 ATOM 2464 C CB . LEU A 1 323 ? 33.047 10.840 34.350 1.00 17.70 ? 323 LEU A CB 1 ATOM 2465 C CG . LEU A 1 323 ? 34.293 11.485 34.961 1.00 24.57 ? 323 LEU A CG 1 ATOM 2466 C CD1 . LEU A 1 323 ? 35.285 10.425 35.420 1.00 28.22 ? 323 LEU A CD1 1 ATOM 2467 C CD2 . LEU A 1 323 ? 34.955 12.423 33.969 1.00 20.67 ? 323 LEU A CD2 1 ATOM 2468 N N . LEU A 1 324 ? 29.969 10.079 34.695 1.00 29.99 ? 324 LEU A N 1 ATOM 2469 C CA . LEU A 1 324 ? 28.705 9.506 34.191 1.00 35.39 ? 324 LEU A CA 1 ATOM 2470 C C . LEU A 1 324 ? 27.628 10.597 34.319 1.00 42.41 ? 324 LEU A C 1 ATOM 2471 O O . LEU A 1 324 ? 26.745 10.835 33.459 1.00 20.91 ? 324 LEU A O 1 ATOM 2472 C CB . LEU A 1 324 ? 28.263 8.169 34.886 1.00 28.32 ? 324 LEU A CB 1 ATOM 2473 C CG . LEU A 1 324 ? 29.193 6.995 34.547 1.00 36.25 ? 324 LEU A CG 1 ATOM 2474 C CD1 . LEU A 1 324 ? 28.961 5.795 35.461 1.00 29.08 ? 324 LEU A CD1 1 ATOM 2475 C CD2 . LEU A 1 324 ? 29.136 6.583 33.061 1.00 18.92 ? 324 LEU A CD2 1 ATOM 2476 N N . ASN A 1 325 ? 27.740 11.303 35.432 1.00 36.46 ? 325 ASN A N 1 ATOM 2477 C CA . ASN A 1 325 ? 26.807 12.359 35.652 1.00 31.75 ? 325 ASN A CA 1 ATOM 2478 C C . ASN A 1 325 ? 26.944 13.441 34.583 1.00 16.84 ? 325 ASN A C 1 ATOM 2479 O O . ASN A 1 325 ? 25.969 14.016 34.126 1.00 31.29 ? 325 ASN A O 1 ATOM 2480 C CB . ASN A 1 325 ? 26.439 12.688 37.138 1.00 14.99 ? 325 ASN A CB 1 ATOM 2481 C CG . ASN A 1 325 ? 25.656 11.501 37.754 1.00 66.93 ? 325 ASN A CG 1 ATOM 2482 O OD1 . ASN A 1 325 ? 25.148 10.616 37.015 1.00 22.72 ? 325 ASN A OD1 1 ATOM 2483 N ND2 . ASN A 1 325 ? 25.586 11.413 39.101 1.00 20.88 ? 325 ASN A ND2 1 ATOM 2484 N N . GLN A 1 326 ? 28.165 13.664 34.150 1.00 9.87 ? 326 GLN A N 1 ATOM 2485 C CA . GLN A 1 326 ? 28.464 14.616 33.098 1.00 13.71 ? 326 GLN A CA 1 ATOM 2486 C C . GLN A 1 326 ? 28.322 13.939 31.716 1.00 26.72 ? 326 GLN A C 1 ATOM 2487 O O . GLN A 1 326 ? 29.044 14.207 30.747 1.00 32.48 ? 326 GLN A O 1 ATOM 2488 C CB . GLN A 1 326 ? 29.864 15.262 33.226 1.00 11.83 ? 326 GLN A CB 1 ATOM 2489 C CG . GLN A 1 326 ? 30.345 15.468 34.663 1.00 14.79 ? 326 GLN A CG 1 ATOM 2490 C CD . GLN A 1 326 ? 31.201 16.709 34.753 1.00 88.40 ? 326 GLN A CD 1 ATOM 2491 O OE1 . GLN A 1 326 ? 30.987 17.562 35.622 1.00 90.43 ? 326 GLN A OE1 1 ATOM 2492 N NE2 . GLN A 1 326 ? 32.108 16.866 33.785 1.00 37.02 ? 326 GLN A NE2 1 ATOM 2493 N N . ASP A 1 327 ? 27.396 13.014 31.634 1.00 31.99 ? 327 ASP A N 1 ATOM 2494 C CA . ASP A 1 327 ? 27.105 12.279 30.406 1.00 38.17 ? 327 ASP A CA 1 ATOM 2495 C C . ASP A 1 327 ? 28.300 11.758 29.581 1.00 38.92 ? 327 ASP A C 1 ATOM 2496 O O . ASP A 1 327 ? 28.289 11.816 28.341 1.00 26.98 ? 327 ASP A O 1 ATOM 2497 C CB . ASP A 1 327 ? 26.145 13.109 29.523 1.00 43.96 ? 327 ASP A CB 1 ATOM 2498 C CG . ASP A 1 327 ? 24.667 12.950 29.833 1.00 33.77 ? 327 ASP A CG 1 ATOM 2499 O OD1 . ASP A 1 327 ? 24.203 12.850 30.944 1.00 36.17 ? 327 ASP A OD1 1 ATOM 2500 O OD2 . ASP A 1 327 ? 23.921 12.987 28.765 1.00 43.24 ? 327 ASP A OD2 1 ATOM 2501 N N . LEU A 1 328 ? 29.335 11.234 30.256 1.00 49.32 ? 328 LEU A N 1 ATOM 2502 C CA . LEU A 1 328 ? 30.494 10.705 29.540 1.00 41.18 ? 328 LEU A CA 1 ATOM 2503 C C . LEU A 1 328 ? 30.402 9.193 29.382 1.00 41.66 ? 328 LEU A C 1 ATOM 2504 O O . LEU A 1 328 ? 30.260 8.472 30.382 1.00 35.75 ? 328 LEU A O 1 ATOM 2505 C CB . LEU A 1 328 ? 31.871 11.159 30.106 1.00 30.00 ? 328 LEU A CB 1 ATOM 2506 C CG . LEU A 1 328 ? 32.944 11.330 29.019 1.00 20.16 ? 328 LEU A CG 1 ATOM 2507 C CD1 . LEU A 1 328 ? 34.265 11.821 29.618 1.00 6.37 ? 328 LEU A CD1 1 ATOM 2508 C CD2 . LEU A 1 328 ? 33.244 9.970 28.392 1.00 26.78 ? 328 LEU A CD2 1 ATOM 2509 N N . PRO A 1 329 ? 30.472 8.747 28.102 1.00 29.73 ? 329 PRO A N 1 ATOM 2510 C CA . PRO A 1 329 ? 30.432 7.337 27.725 1.00 22.71 ? 329 PRO A CA 1 ATOM 2511 C C . PRO A 1 329 ? 31.679 6.610 28.264 1.00 39.41 ? 329 PRO A C 1 ATOM 2512 O O . PRO A 1 329 ? 32.837 6.956 27.939 1.00 43.91 ? 329 PRO A O 1 ATOM 2513 C CB . PRO A 1 329 ? 30.449 7.297 26.203 1.00 16.11 ? 329 PRO A CB 1 ATOM 2514 C CG . PRO A 1 329 ? 31.033 8.641 25.794 1.00 28.36 ? 329 PRO A CG 1 ATOM 2515 C CD . PRO A 1 329 ? 30.673 9.608 26.910 1.00 28.70 ? 329 PRO A CD 1 ATOM 2516 N N . ILE A 1 330 ? 31.435 5.604 29.106 1.00 32.27 ? 330 ILE A N 1 ATOM 2517 C CA . ILE A 1 330 ? 32.518 4.863 29.702 1.00 30.00 ? 330 ILE A CA 1 ATOM 2518 C C . ILE A 1 330 ? 32.474 3.399 29.417 1.00 17.26 ? 330 ILE A C 1 ATOM 2519 O O . ILE A 1 330 ? 31.406 2.814 29.441 1.00 13.63 ? 330 ILE A O 1 ATOM 2520 C CB . ILE A 1 330 ? 32.459 4.984 31.223 1.00 48.30 ? 330 ILE A CB 1 ATOM 2521 C CG1 . ILE A 1 330 ? 32.335 6.441 31.684 1.00 59.67 ? 330 ILE A CG1 1 ATOM 2522 C CG2 . ILE A 1 330 ? 33.715 4.378 31.841 1.00 57.70 ? 330 ILE A CG2 1 ATOM 2523 C CD1 . ILE A 1 330 ? 33.420 6.878 32.683 1.00 12.04 ? 330 ILE A CD1 1 ATOM 2524 N N . LEU A 1 331 ? 33.668 2.801 29.189 1.00 21.38 ? 331 LEU A N 1 ATOM 2525 C CA . LEU A 1 331 ? 33.821 1.354 28.941 1.00 29.37 ? 331 LEU A CA 1 ATOM 2526 C C . LEU A 1 331 ? 34.888 0.645 29.800 1.00 22.19 ? 331 LEU A C 1 ATOM 2527 O O . LEU A 1 331 ? 36.127 0.844 29.671 1.00 14.47 ? 331 LEU A O 1 ATOM 2528 C CB . LEU A 1 331 ? 33.971 0.991 27.468 1.00 36.30 ? 331 LEU A CB 1 ATOM 2529 C CG . LEU A 1 331 ? 34.383 -0.444 27.230 1.00 38.64 ? 331 LEU A CG 1 ATOM 2530 C CD1 . LEU A 1 331 ? 33.859 -0.796 25.858 1.00 36.16 ? 331 LEU A CD1 1 ATOM 2531 C CD2 . LEU A 1 331 ? 35.925 -0.557 27.254 1.00 43.97 ? 331 LEU A CD2 1 ATOM 2532 N N . VAL A 1 332 ? 34.322 -0.183 30.673 1.00 11.51 ? 332 VAL A N 1 ATOM 2533 C CA . VAL A 1 332 ? 34.980 -1.035 31.636 1.00 12.71 ? 332 VAL A CA 1 ATOM 2534 C C . VAL A 1 332 ? 35.014 -2.423 31.014 1.00 31.86 ? 332 VAL A C 1 ATOM 2535 O O . VAL A 1 332 ? 33.959 -3.060 30.952 1.00 36.03 ? 332 VAL A O 1 ATOM 2536 C CB . VAL A 1 332 ? 34.132 -1.179 32.935 1.00 7.20 ? 332 VAL A CB 1 ATOM 2537 C CG1 . VAL A 1 332 ? 34.823 -2.109 33.882 1.00 3.57 ? 332 VAL A CG1 1 ATOM 2538 C CG2 . VAL A 1 332 ? 33.818 0.113 33.694 1.00 1.00 ? 332 VAL A CG2 1 ATOM 2539 N N . TYR A 1 333 ? 36.195 -2.887 30.562 1.00 24.60 ? 333 TYR A N 1 ATOM 2540 C CA . TYR A 1 333 ? 36.349 -4.208 29.978 1.00 11.20 ? 333 TYR A CA 1 ATOM 2541 C C . TYR A 1 333 ? 37.335 -5.114 30.727 1.00 13.67 ? 333 TYR A C 1 ATOM 2542 O O . TYR A 1 333 ? 38.391 -4.682 31.154 1.00 27.84 ? 333 TYR A O 1 ATOM 2543 C CB . TYR A 1 333 ? 36.748 -4.001 28.590 1.00 12.09 ? 333 TYR A CB 1 ATOM 2544 C CG . TYR A 1 333 ? 38.108 -3.429 28.340 1.00 8.10 ? 333 TYR A CG 1 ATOM 2545 C CD1 . TYR A 1 333 ? 38.379 -2.060 28.276 1.00 8.71 ? 333 TYR A CD1 1 ATOM 2546 C CD2 . TYR A 1 333 ? 39.135 -4.309 28.017 1.00 8.38 ? 333 TYR A CD2 1 ATOM 2547 C CE1 . TYR A 1 333 ? 39.664 -1.603 27.933 1.00 9.57 ? 333 TYR A CE1 1 ATOM 2548 C CE2 . TYR A 1 333 ? 40.418 -3.870 27.671 1.00 5.63 ? 333 TYR A CE2 1 ATOM 2549 C CZ . TYR A 1 333 ? 40.697 -2.504 27.619 1.00 23.15 ? 333 TYR A CZ 1 ATOM 2550 O OH . TYR A 1 333 ? 41.992 -2.105 27.240 1.00 1.00 ? 333 TYR A OH 1 ATOM 2551 N N . ALA A 1 334 ? 37.011 -6.392 30.909 1.00 11.33 ? 334 ALA A N 1 ATOM 2552 C CA . ALA A 1 334 ? 37.890 -7.303 31.669 1.00 4.99 ? 334 ALA A CA 1 ATOM 2553 C C . ALA A 1 334 ? 38.300 -8.650 31.080 1.00 19.27 ? 334 ALA A C 1 ATOM 2554 O O . ALA A 1 334 ? 37.428 -9.473 30.857 1.00 18.72 ? 334 ALA A O 1 ATOM 2555 C CB . ALA A 1 334 ? 37.092 -7.719 32.916 1.00 1.00 ? 334 ALA A CB 1 ATOM 2556 N N . GLY A 1 335 ? 39.609 -8.938 30.914 1.00 25.65 ? 335 GLY A N 1 ATOM 2557 C CA . GLY A 1 335 ? 40.015 -10.284 30.448 1.00 18.54 ? 335 GLY A CA 1 ATOM 2558 C C . GLY A 1 335 ? 39.469 -11.271 31.513 1.00 20.22 ? 335 GLY A C 1 ATOM 2559 O O . GLY A 1 335 ? 39.622 -11.114 32.745 1.00 24.14 ? 335 GLY A O 1 ATOM 2560 N N . ASP A 1 336 ? 38.767 -12.278 31.084 1.00 1.26 ? 336 ASP A N 1 ATOM 2561 C CA . ASP A 1 336 ? 38.195 -13.189 32.082 1.00 5.63 ? 336 ASP A CA 1 ATOM 2562 C C . ASP A 1 336 ? 39.142 -14.210 32.630 1.00 20.78 ? 336 ASP A C 1 ATOM 2563 O O . ASP A 1 336 ? 38.689 -15.125 33.361 1.00 25.17 ? 336 ASP A O 1 ATOM 2564 C CB . ASP A 1 336 ? 36.910 -13.949 31.566 1.00 15.61 ? 336 ASP A CB 1 ATOM 2565 C CG . ASP A 1 336 ? 37.158 -14.950 30.441 1.00 35.56 ? 336 ASP A CG 1 ATOM 2566 O OD1 . ASP A 1 336 ? 37.878 -14.447 29.480 1.00 36.35 ? 336 ASP A OD1 1 ATOM 2567 O OD2 . ASP A 1 336 ? 36.810 -16.124 30.458 1.00 24.41 ? 336 ASP A OD2 1 ATOM 2568 N N . LYS A 1 337 ? 40.431 -14.123 32.249 1.00 35.82 ? 337 LYS A N 1 ATOM 2569 C CA . LYS A 1 337 ? 41.431 -15.110 32.737 1.00 33.54 ? 337 LYS A CA 1 ATOM 2570 C C . LYS A 1 337 ? 42.496 -14.494 33.635 1.00 38.62 ? 337 LYS A C 1 ATOM 2571 O O . LYS A 1 337 ? 43.548 -15.105 33.818 1.00 44.56 ? 337 LYS A O 1 ATOM 2572 C CB . LYS A 1 337 ? 42.161 -15.907 31.638 1.00 14.27 ? 337 LYS A CB 1 ATOM 2573 C CG . LYS A 1 337 ? 41.295 -16.612 30.598 1.00 38.42 ? 337 LYS A CG 1 ATOM 2574 C CD . LYS A 1 337 ? 40.665 -17.933 31.031 1.00 14.95 ? 337 LYS A CD 1 ATOM 2575 C CE . LYS A 1 337 ? 39.174 -18.019 30.707 1.00 26.06 ? 337 LYS A CE 1 ATOM 2576 N NZ . LYS A 1 337 ? 38.390 -18.738 31.737 1.00 87.78 ? 337 LYS A NZ 1 ATOM 2577 N N . ASP A 1 338 ? 42.217 -13.296 34.165 1.00 20.29 ? 338 ASP A N 1 ATOM 2578 C CA . ASP A 1 338 ? 43.112 -12.543 35.011 1.00 9.65 ? 338 ASP A CA 1 ATOM 2579 C C . ASP A 1 338 ? 42.723 -12.578 36.458 1.00 22.12 ? 338 ASP A C 1 ATOM 2580 O O . ASP A 1 338 ? 41.533 -12.446 36.706 1.00 43.12 ? 338 ASP A O 1 ATOM 2581 C CB . ASP A 1 338 ? 43.143 -11.105 34.553 1.00 10.75 ? 338 ASP A CB 1 ATOM 2582 C CG . ASP A 1 338 ? 43.958 -10.259 35.464 1.00 19.99 ? 338 ASP A CG 1 ATOM 2583 O OD1 . ASP A 1 338 ? 45.051 -10.600 35.883 1.00 34.08 ? 338 ASP A OD1 1 ATOM 2584 O OD2 . ASP A 1 338 ? 43.439 -9.070 35.626 1.00 12.58 ? 338 ASP A OD2 1 ATOM 2585 N N . PHE A 1 339 ? 43.719 -12.734 37.395 1.00 10.95 ? 339 PHE A N 1 ATOM 2586 C CA . PHE A 1 339 ? 43.447 -12.782 38.833 1.00 5.11 ? 339 PHE A CA 1 ATOM 2587 C C . PHE A 1 339 ? 43.591 -11.339 39.498 1.00 21.88 ? 339 PHE A C 1 ATOM 2588 O O . PHE A 1 339 ? 42.708 -10.823 40.195 1.00 1.00 ? 339 PHE A O 1 ATOM 2589 C CB . PHE A 1 339 ? 44.214 -13.923 39.499 1.00 1.00 ? 339 PHE A CB 1 ATOM 2590 C CG . PHE A 1 339 ? 44.235 -13.793 40.974 1.00 1.00 ? 339 PHE A CG 1 ATOM 2591 C CD1 . PHE A 1 339 ? 43.144 -14.217 41.726 1.00 13.10 ? 339 PHE A CD1 1 ATOM 2592 C CD2 . PHE A 1 339 ? 45.304 -13.216 41.657 1.00 3.85 ? 339 PHE A CD2 1 ATOM 2593 C CE1 . PHE A 1 339 ? 43.122 -14.068 43.116 1.00 14.78 ? 339 PHE A CE1 1 ATOM 2594 C CE2 . PHE A 1 339 ? 45.300 -13.048 43.045 1.00 5.51 ? 339 PHE A CE2 1 ATOM 2595 C CZ . PHE A 1 339 ? 44.198 -13.478 43.789 1.00 3.60 ? 339 PHE A CZ 1 ATOM 2596 N N . ILE A 1 340 ? 44.697 -10.651 39.222 1.00 9.77 ? 340 ILE A N 1 ATOM 2597 C CA . ILE A 1 340 ? 44.978 -9.338 39.746 1.00 8.91 ? 340 ILE A CA 1 ATOM 2598 C C . ILE A 1 340 ? 43.888 -8.256 39.590 1.00 14.88 ? 340 ILE A C 1 ATOM 2599 O O . ILE A 1 340 ? 43.736 -7.425 40.453 1.00 18.55 ? 340 ILE A O 1 ATOM 2600 C CB . ILE A 1 340 ? 46.351 -8.898 39.264 1.00 28.52 ? 340 ILE A CB 1 ATOM 2601 C CG1 . ILE A 1 340 ? 46.770 -7.489 39.698 1.00 42.79 ? 340 ILE A CG1 1 ATOM 2602 C CG2 . ILE A 1 340 ? 46.408 -9.030 37.760 1.00 50.42 ? 340 ILE A CG2 1 ATOM 2603 C CD1 . ILE A 1 340 ? 48.175 -7.455 40.344 1.00 45.87 ? 340 ILE A CD1 1 ATOM 2604 N N . CYS A 1 341 ? 43.118 -8.224 38.509 1.00 23.21 ? 341 CYS A N 1 ATOM 2605 C CA . CYS A 1 341 ? 42.006 -7.255 38.292 1.00 9.34 ? 341 CYS A CA 1 ATOM 2606 C C . CYS A 1 341 ? 40.839 -7.971 37.581 1.00 15.78 ? 341 CYS A C 1 ATOM 2607 O O . CYS A 1 341 ? 40.458 -7.567 36.490 1.00 19.25 ? 341 CYS A O 1 ATOM 2608 C CB . CYS A 1 341 ? 42.389 -6.002 37.498 1.00 10.57 ? 341 CYS A CB 1 ATOM 2609 S SG . CYS A 1 341 ? 43.606 -4.949 38.338 1.00 13.96 ? 341 CYS A SG 1 ATOM 2610 N N . ASN A 1 342 ? 40.315 -9.059 38.198 1.00 1.36 ? 342 ASN A N 1 ATOM 2611 C CA . ASN A 1 342 ? 39.225 -9.902 37.710 1.00 1.00 ? 342 ASN A CA 1 ATOM 2612 C C . ASN A 1 342 ? 38.079 -9.189 37.069 1.00 22.36 ? 342 ASN A C 1 ATOM 2613 O O . ASN A 1 342 ? 37.788 -8.028 37.313 1.00 21.61 ? 342 ASN A O 1 ATOM 2614 C CB . ASN A 1 342 ? 38.464 -10.583 38.865 1.00 1.22 ? 342 ASN A CB 1 ATOM 2615 C CG . ASN A 1 342 ? 39.294 -11.280 39.887 1.00 18.59 ? 342 ASN A CG 1 ATOM 2616 O OD1 . ASN A 1 342 ? 39.056 -11.142 41.110 1.00 23.56 ? 342 ASN A OD1 1 ATOM 2617 N ND2 . ASN A 1 342 ? 40.179 -12.124 39.378 1.00 10.49 ? 342 ASN A ND2 1 ATOM 2618 N N . TRP A 1 343 ? 37.363 -9.986 36.313 1.00 24.74 ? 343 TRP A N 1 ATOM 2619 C CA . TRP A 1 343 ? 36.186 -9.543 35.668 1.00 21.23 ? 343 TRP A CA 1 ATOM 2620 C C . TRP A 1 343 ? 35.119 -9.738 36.750 1.00 18.10 ? 343 TRP A C 1 ATOM 2621 O O . TRP A 1 343 ? 34.059 -9.104 36.754 1.00 24.82 ? 343 TRP A O 1 ATOM 2622 C CB . TRP A 1 343 ? 35.892 -10.343 34.368 1.00 27.01 ? 343 TRP A CB 1 ATOM 2623 C CG . TRP A 1 343 ? 35.583 -11.733 34.783 1.00 35.02 ? 343 TRP A CG 1 ATOM 2624 C CD1 . TRP A 1 343 ? 36.470 -12.698 35.128 1.00 37.67 ? 343 TRP A CD1 1 ATOM 2625 C CD2 . TRP A 1 343 ? 34.292 -12.280 35.022 1.00 34.63 ? 343 TRP A CD2 1 ATOM 2626 N NE1 . TRP A 1 343 ? 35.797 -13.829 35.545 1.00 29.91 ? 343 TRP A NE1 1 ATOM 2627 C CE2 . TRP A 1 343 ? 34.464 -13.582 35.496 1.00 30.75 ? 343 TRP A CE2 1 ATOM 2628 C CE3 . TRP A 1 343 ? 33.028 -11.785 34.867 1.00 31.26 ? 343 TRP A CE3 1 ATOM 2629 C CZ2 . TRP A 1 343 ? 33.398 -14.385 35.780 1.00 31.00 ? 343 TRP A CZ2 1 ATOM 2630 C CZ3 . TRP A 1 343 ? 31.974 -12.575 35.190 1.00 28.49 ? 343 TRP A CZ3 1 ATOM 2631 C CH2 . TRP A 1 343 ? 32.158 -13.858 35.631 1.00 30.18 ? 343 TRP A CH2 1 ATOM 2632 N N . LEU A 1 344 ? 35.386 -10.619 37.710 1.00 14.88 ? 344 LEU A N 1 ATOM 2633 C CA . LEU A 1 344 ? 34.373 -10.815 38.778 1.00 17.72 ? 344 LEU A CA 1 ATOM 2634 C C . LEU A 1 344 ? 34.193 -9.547 39.500 1.00 8.23 ? 344 LEU A C 1 ATOM 2635 O O . LEU A 1 344 ? 33.114 -9.079 39.623 1.00 4.84 ? 344 LEU A O 1 ATOM 2636 C CB . LEU A 1 344 ? 34.690 -11.810 39.913 1.00 18.64 ? 344 LEU A CB 1 ATOM 2637 C CG . LEU A 1 344 ? 34.566 -13.272 39.498 1.00 21.29 ? 344 LEU A CG 1 ATOM 2638 C CD1 . LEU A 1 344 ? 34.471 -14.195 40.708 1.00 15.61 ? 344 LEU A CD1 1 ATOM 2639 C CD2 . LEU A 1 344 ? 33.352 -13.438 38.616 1.00 8.98 ? 344 LEU A CD2 1 ATOM 2640 N N . GLY A 1 345 ? 35.301 -9.013 39.966 1.00 6.13 ? 345 GLY A N 1 ATOM 2641 C CA . GLY A 1 345 ? 35.278 -7.798 40.696 1.00 1.00 ? 345 GLY A CA 1 ATOM 2642 C C . GLY A 1 345 ? 35.007 -6.603 39.813 1.00 25.00 ? 345 GLY A C 1 ATOM 2643 O O . GLY A 1 345 ? 34.275 -5.720 40.226 1.00 41.82 ? 345 GLY A O 1 ATOM 2644 N N . ASN A 1 346 ? 35.569 -6.503 38.603 1.00 4.82 ? 346 ASN A N 1 ATOM 2645 C CA . ASN A 1 346 ? 35.225 -5.290 37.863 1.00 1.00 ? 346 ASN A CA 1 ATOM 2646 C C . ASN A 1 346 ? 33.762 -5.329 37.480 1.00 14.82 ? 346 ASN A C 1 ATOM 2647 O O . ASN A 1 346 ? 33.095 -4.315 37.235 1.00 13.15 ? 346 ASN A O 1 ATOM 2648 C CB . ASN A 1 346 ? 36.047 -4.989 36.615 1.00 1.00 ? 346 ASN A CB 1 ATOM 2649 C CG . ASN A 1 346 ? 37.479 -4.563 36.808 1.00 16.77 ? 346 ASN A CG 1 ATOM 2650 O OD1 . ASN A 1 346 ? 37.861 -3.486 36.344 1.00 25.26 ? 346 ASN A OD1 1 ATOM 2651 N ND2 . ASN A 1 346 ? 38.320 -5.530 37.150 1.00 4.12 ? 346 ASN A ND2 1 ATOM 2652 N N . LYS A 1 347 ? 33.245 -6.535 37.437 1.00 16.93 ? 347 LYS A N 1 ATOM 2653 C CA . LYS A 1 347 ? 31.852 -6.675 37.103 1.00 19.07 ? 347 LYS A CA 1 ATOM 2654 C C . LYS A 1 347 ? 30.946 -5.911 38.036 1.00 20.19 ? 347 LYS A C 1 ATOM 2655 O O . LYS A 1 347 ? 30.138 -5.069 37.627 1.00 30.88 ? 347 LYS A O 1 ATOM 2656 C CB . LYS A 1 347 ? 31.376 -8.109 37.202 1.00 22.28 ? 347 LYS A CB 1 ATOM 2657 C CG . LYS A 1 347 ? 29.849 -8.170 37.016 1.00 52.71 ? 347 LYS A CG 1 ATOM 2658 C CD . LYS A 1 347 ? 29.305 -9.532 36.551 1.00 21.69 ? 347 LYS A CD 1 ATOM 2659 C CE . LYS A 1 347 ? 28.446 -10.280 37.582 1.00 100.00 ? 347 LYS A CE 1 ATOM 2660 N NZ . LYS A 1 347 ? 29.198 -10.998 38.648 1.00 100.00 ? 347 LYS A NZ 1 ATOM 2661 N N . ALA A 1 348 ? 31.140 -6.286 39.287 1.00 2.93 ? 348 ALA A N 1 ATOM 2662 C CA . ALA A 1 348 ? 30.438 -5.858 40.471 1.00 12.42 ? 348 ALA A CA 1 ATOM 2663 C C . ALA A 1 348 ? 30.580 -4.449 40.866 1.00 19.02 ? 348 ALA A C 1 ATOM 2664 O O . ALA A 1 348 ? 29.602 -3.845 41.306 1.00 38.29 ? 348 ALA A O 1 ATOM 2665 C CB . ALA A 1 348 ? 30.593 -6.806 41.664 1.00 20.44 ? 348 ALA A CB 1 ATOM 2666 N N . TRP A 1 349 ? 31.770 -3.915 40.721 1.00 12.85 ? 349 TRP A N 1 ATOM 2667 C CA . TRP A 1 349 ? 31.934 -2.524 41.084 1.00 3.30 ? 349 TRP A CA 1 ATOM 2668 C C . TRP A 1 349 ? 31.010 -1.690 40.253 1.00 14.19 ? 349 TRP A C 1 ATOM 2669 O O . TRP A 1 349 ? 30.353 -0.820 40.782 1.00 36.35 ? 349 TRP A O 1 ATOM 2670 C CB . TRP A 1 349 ? 33.370 -2.064 41.214 1.00 1.00 ? 349 TRP A CB 1 ATOM 2671 C CG . TRP A 1 349 ? 34.086 -1.613 39.986 1.00 1.00 ? 349 TRP A CG 1 ATOM 2672 C CD1 . TRP A 1 349 ? 35.123 -2.256 39.402 1.00 7.26 ? 349 TRP A CD1 1 ATOM 2673 C CD2 . TRP A 1 349 ? 33.947 -0.379 39.297 1.00 3.81 ? 349 TRP A CD2 1 ATOM 2674 N NE1 . TRP A 1 349 ? 35.629 -1.539 38.360 1.00 9.99 ? 349 TRP A NE1 1 ATOM 2675 C CE2 . TRP A 1 349 ? 34.915 -0.357 38.278 1.00 17.24 ? 349 TRP A CE2 1 ATOM 2676 C CE3 . TRP A 1 349 ? 33.093 0.724 39.427 1.00 12.96 ? 349 TRP A CE3 1 ATOM 2677 C CZ2 . TRP A 1 349 ? 35.021 0.739 37.383 1.00 18.92 ? 349 TRP A CZ2 1 ATOM 2678 C CZ3 . TRP A 1 349 ? 33.217 1.788 38.557 1.00 14.82 ? 349 TRP A CZ3 1 ATOM 2679 C CH2 . TRP A 1 349 ? 34.166 1.791 37.531 1.00 10.14 ? 349 TRP A CH2 1 ATOM 2680 N N . THR A 1 350 ? 30.929 -2.053 38.976 1.00 23.21 ? 350 THR A N 1 ATOM 2681 C CA . THR A 1 350 ? 30.071 -1.470 37.935 1.00 27.69 ? 350 THR A CA 1 ATOM 2682 C C . THR A 1 350 ? 28.599 -1.643 38.350 1.00 12.90 ? 350 THR A C 1 ATOM 2683 O O . THR A 1 350 ? 27.753 -0.759 38.395 1.00 1.02 ? 350 THR A O 1 ATOM 2684 C CB . THR A 1 350 ? 30.335 -2.248 36.600 1.00 31.26 ? 350 THR A CB 1 ATOM 2685 O OG1 . THR A 1 350 ? 31.274 -1.585 35.772 1.00 26.20 ? 350 THR A OG1 1 ATOM 2686 C CG2 . THR A 1 350 ? 29.045 -2.452 35.841 1.00 57.34 ? 350 THR A CG2 1 ATOM 2687 N N . ASP A 1 351 ? 28.292 -2.842 38.670 1.00 11.11 ? 351 ASP A N 1 ATOM 2688 C CA . ASP A 1 351 ? 26.978 -3.181 39.090 1.00 9.26 ? 351 ASP A CA 1 ATOM 2689 C C . ASP A 1 351 ? 26.511 -2.426 40.294 1.00 25.77 ? 351 ASP A C 1 ATOM 2690 O O . ASP A 1 351 ? 25.356 -2.553 40.701 1.00 36.93 ? 351 ASP A O 1 ATOM 2691 C CB . ASP A 1 351 ? 26.927 -4.661 39.392 1.00 8.33 ? 351 ASP A CB 1 ATOM 2692 C CG . ASP A 1 351 ? 26.544 -5.323 38.130 1.00 30.59 ? 351 ASP A CG 1 ATOM 2693 O OD1 . ASP A 1 351 ? 26.461 -4.665 37.074 1.00 17.93 ? 351 ASP A OD1 1 ATOM 2694 O OD2 . ASP A 1 351 ? 26.113 -6.559 38.367 1.00 1.00 ? 351 ASP A OD2 1 ATOM 2695 N N . VAL A 1 352 ? 27.390 -1.637 40.888 1.00 30.39 ? 352 VAL A N 1 ATOM 2696 C CA . VAL A 1 352 ? 26.935 -0.870 42.058 1.00 31.53 ? 352 VAL A CA 1 ATOM 2697 C C . VAL A 1 352 ? 27.274 0.635 42.089 1.00 29.15 ? 352 VAL A C 1 ATOM 2698 O O . VAL A 1 352 ? 26.883 1.370 42.976 1.00 25.90 ? 352 VAL A O 1 ATOM 2699 C CB . VAL A 1 352 ? 27.154 -1.508 43.424 1.00 18.88 ? 352 VAL A CB 1 ATOM 2700 C CG1 . VAL A 1 352 ? 26.660 -2.937 43.502 1.00 1.50 ? 352 VAL A CG1 1 ATOM 2701 C CG2 . VAL A 1 352 ? 28.570 -1.281 43.907 1.00 18.51 ? 352 VAL A CG2 1 ATOM 2702 N N . LEU A 1 353 ? 28.018 1.085 41.121 1.00 15.86 ? 353 LEU A N 1 ATOM 2703 C CA . LEU A 1 353 ? 28.393 2.454 41.057 1.00 3.95 ? 353 LEU A CA 1 ATOM 2704 C C . LEU A 1 353 ? 27.170 3.250 40.927 1.00 16.95 ? 353 LEU A C 1 ATOM 2705 O O . LEU A 1 353 ? 26.229 2.877 40.223 1.00 31.28 ? 353 LEU A O 1 ATOM 2706 C CB . LEU A 1 353 ? 29.160 2.647 39.748 1.00 5.32 ? 353 LEU A CB 1 ATOM 2707 C CG . LEU A 1 353 ? 29.568 4.087 39.555 1.00 8.50 ? 353 LEU A CG 1 ATOM 2708 C CD1 . LEU A 1 353 ? 30.998 4.222 39.976 1.00 6.34 ? 353 LEU A CD1 1 ATOM 2709 C CD2 . LEU A 1 353 ? 29.490 4.414 38.069 1.00 16.61 ? 353 LEU A CD2 1 ATOM 2710 N N . PRO A 1 354 ? 27.168 4.372 41.573 1.00 30.49 ? 354 PRO A N 1 ATOM 2711 C CA . PRO A 1 354 ? 26.011 5.208 41.439 1.00 35.36 ? 354 PRO A CA 1 ATOM 2712 C C . PRO A 1 354 ? 26.179 6.270 40.333 1.00 38.23 ? 354 PRO A C 1 ATOM 2713 O O . PRO A 1 354 ? 27.232 6.838 40.036 1.00 26.00 ? 354 PRO A O 1 ATOM 2714 C CB . PRO A 1 354 ? 25.664 5.763 42.820 1.00 31.80 ? 354 PRO A CB 1 ATOM 2715 C CG . PRO A 1 354 ? 26.472 4.939 43.817 1.00 23.05 ? 354 PRO A CG 1 ATOM 2716 C CD . PRO A 1 354 ? 27.443 4.091 43.001 1.00 24.35 ? 354 PRO A CD 1 ATOM 2717 N N . TRP A 1 355 ? 25.085 6.516 39.698 1.00 40.98 ? 355 TRP A N 1 ATOM 2718 C CA . TRP A 1 355 ? 25.048 7.465 38.650 1.00 37.34 ? 355 TRP A CA 1 ATOM 2719 C C . TRP A 1 355 ? 23.546 7.663 38.307 1.00 31.13 ? 355 TRP A C 1 ATOM 2720 O O . TRP A 1 355 ? 22.680 6.981 38.917 1.00 18.75 ? 355 TRP A O 1 ATOM 2721 C CB . TRP A 1 355 ? 26.011 6.983 37.543 1.00 33.43 ? 355 TRP A CB 1 ATOM 2722 C CG . TRP A 1 355 ? 25.481 5.794 36.841 1.00 33.34 ? 355 TRP A CG 1 ATOM 2723 C CD1 . TRP A 1 355 ? 25.249 4.557 37.345 1.00 37.31 ? 355 TRP A CD1 1 ATOM 2724 C CD2 . TRP A 1 355 ? 25.045 5.783 35.497 1.00 32.63 ? 355 TRP A CD2 1 ATOM 2725 N NE1 . TRP A 1 355 ? 24.693 3.750 36.367 1.00 39.51 ? 355 TRP A NE1 1 ATOM 2726 C CE2 . TRP A 1 355 ? 24.552 4.494 35.223 1.00 42.62 ? 355 TRP A CE2 1 ATOM 2727 C CE3 . TRP A 1 355 ? 25.024 6.758 34.503 1.00 31.36 ? 355 TRP A CE3 1 ATOM 2728 C CZ2 . TRP A 1 355 ? 24.061 4.166 33.959 1.00 43.34 ? 355 TRP A CZ2 1 ATOM 2729 C CZ3 . TRP A 1 355 ? 24.535 6.448 33.258 1.00 30.09 ? 355 TRP A CZ3 1 ATOM 2730 C CH2 . TRP A 1 355 ? 24.060 5.162 32.994 1.00 34.29 ? 355 TRP A CH2 1 ATOM 2731 N N . LYS A 1 356 ? 23.187 8.578 37.391 1.00 13.91 ? 356 LYS A N 1 ATOM 2732 C CA . LYS A 1 356 ? 21.739 8.745 37.149 1.00 18.21 ? 356 LYS A CA 1 ATOM 2733 C C . LYS A 1 356 ? 20.967 7.500 36.714 1.00 20.76 ? 356 LYS A C 1 ATOM 2734 O O . LYS A 1 356 ? 19.891 7.213 37.204 1.00 19.35 ? 356 LYS A O 1 ATOM 2735 C CB . LYS A 1 356 ? 21.392 9.917 36.295 1.00 10.15 ? 356 LYS A CB 1 ATOM 2736 C CG . LYS A 1 356 ? 22.022 9.763 34.942 1.00 25.43 ? 356 LYS A CG 1 ATOM 2737 C CD . LYS A 1 356 ? 23.074 10.816 34.755 1.00 38.79 ? 356 LYS A CD 1 ATOM 2738 C CE . LYS A 1 356 ? 22.518 12.082 34.182 1.00 33.35 ? 356 LYS A CE 1 ATOM 2739 N NZ . LYS A 1 356 ? 23.260 12.399 32.974 1.00 14.79 ? 356 LYS A NZ 1 ATOM 2740 N N . TYR A 1 357 ? 21.518 6.741 35.791 1.00 29.57 ? 357 TYR A N 1 ATOM 2741 C CA . TYR A 1 357 ? 20.871 5.531 35.315 1.00 21.62 ? 357 TYR A CA 1 ATOM 2742 C C . TYR A 1 357 ? 21.126 4.282 36.193 1.00 21.68 ? 357 TYR A C 1 ATOM 2743 O O . TYR A 1 357 ? 20.961 3.105 35.796 1.00 5.68 ? 357 TYR A O 1 ATOM 2744 C CB . TYR A 1 357 ? 21.103 5.390 33.825 1.00 23.84 ? 357 TYR A CB 1 ATOM 2745 C CG . TYR A 1 357 ? 20.724 6.678 33.086 1.00 34.35 ? 357 TYR A CG 1 ATOM 2746 C CD1 . TYR A 1 357 ? 19.480 7.291 33.270 1.00 33.83 ? 357 TYR A CD1 1 ATOM 2747 C CD2 . TYR A 1 357 ? 21.610 7.270 32.185 1.00 32.79 ? 357 TYR A CD2 1 ATOM 2748 C CE1 . TYR A 1 357 ? 19.117 8.461 32.596 1.00 28.52 ? 357 TYR A CE1 1 ATOM 2749 C CE2 . TYR A 1 357 ? 21.273 8.445 31.509 1.00 47.63 ? 357 TYR A CE2 1 ATOM 2750 C CZ . TYR A 1 357 ? 20.026 9.044 31.713 1.00 51.89 ? 357 TYR A CZ 1 ATOM 2751 O OH . TYR A 1 357 ? 19.686 10.204 31.044 1.00 56.85 ? 357 TYR A OH 1 ATOM 2752 N N . ASP A 1 358 ? 21.508 4.614 37.443 1.00 6.63 ? 358 ASP A N 1 ATOM 2753 C CA . ASP A 1 358 ? 21.765 3.725 38.555 1.00 1.71 ? 358 ASP A CA 1 ATOM 2754 C C . ASP A 1 358 ? 20.894 2.452 38.502 1.00 16.96 ? 358 ASP A C 1 ATOM 2755 O O . ASP A 1 358 ? 21.424 1.369 38.384 1.00 28.31 ? 358 ASP A O 1 ATOM 2756 C CB . ASP A 1 358 ? 21.483 4.565 39.838 1.00 5.57 ? 358 ASP A CB 1 ATOM 2757 C CG . ASP A 1 358 ? 21.862 4.044 41.196 1.00 22.04 ? 358 ASP A CG 1 ATOM 2758 O OD1 . ASP A 1 358 ? 22.257 2.795 41.203 1.00 81.47 ? 358 ASP A OD1 1 ATOM 2759 O OD2 . ASP A 1 358 ? 21.833 4.757 42.196 1.00 36.79 ? 358 ASP A OD2 1 ATOM 2760 N N . GLU A 1 359 ? 19.557 2.584 38.579 1.00 20.64 ? 359 GLU A N 1 ATOM 2761 C CA . GLU A 1 359 ? 18.642 1.439 38.571 1.00 28.36 ? 359 GLU A CA 1 ATOM 2762 C C . GLU A 1 359 ? 18.437 0.796 37.202 1.00 31.39 ? 359 GLU A C 1 ATOM 2763 O O . GLU A 1 359 ? 18.167 -0.396 37.014 1.00 32.14 ? 359 GLU A O 1 ATOM 2764 C CB . GLU A 1 359 ? 17.292 1.739 39.265 1.00 33.34 ? 359 GLU A CB 1 ATOM 2765 N N . GLU A 1 360 ? 18.555 1.584 36.207 1.00 26.06 ? 360 GLU A N 1 ATOM 2766 C CA . GLU A 1 360 ? 18.354 0.981 34.946 1.00 20.97 ? 360 GLU A CA 1 ATOM 2767 C C . GLU A 1 360 ? 19.541 0.078 34.635 1.00 32.76 ? 360 GLU A C 1 ATOM 2768 O O . GLU A 1 360 ? 19.333 -1.057 34.234 1.00 27.69 ? 360 GLU A O 1 ATOM 2769 C CB . GLU A 1 360 ? 17.887 2.012 33.912 1.00 21.14 ? 360 GLU A CB 1 ATOM 2770 C CG . GLU A 1 360 ? 16.571 2.736 34.340 1.00 39.88 ? 360 GLU A CG 1 ATOM 2771 C CD . GLU A 1 360 ? 16.619 3.502 35.654 1.00 69.59 ? 360 GLU A CD 1 ATOM 2772 O OE1 . GLU A 1 360 ? 17.162 4.705 35.581 1.00 56.77 ? 360 GLU A OE1 1 ATOM 2773 O OE2 . GLU A 1 360 ? 16.248 3.008 36.702 1.00 87.22 ? 360 GLU A OE2 1 ATOM 2774 N N . PHE A 1 361 ? 20.773 0.570 34.887 1.00 33.24 ? 361 PHE A N 1 ATOM 2775 C CA . PHE A 1 361 ? 21.957 -0.258 34.645 1.00 30.89 ? 361 PHE A CA 1 ATOM 2776 C C . PHE A 1 361 ? 21.831 -1.595 35.363 1.00 36.65 ? 361 PHE A C 1 ATOM 2777 O O . PHE A 1 361 ? 22.054 -2.646 34.801 1.00 46.28 ? 361 PHE A O 1 ATOM 2778 C CB . PHE A 1 361 ? 23.333 0.406 34.971 1.00 29.19 ? 361 PHE A CB 1 ATOM 2779 C CG . PHE A 1 361 ? 24.551 -0.446 34.538 1.00 36.31 ? 361 PHE A CG 1 ATOM 2780 C CD1 . PHE A 1 361 ? 25.025 -1.527 35.295 1.00 41.24 ? 361 PHE A CD1 1 ATOM 2781 C CD2 . PHE A 1 361 ? 25.242 -0.158 33.360 1.00 31.90 ? 361 PHE A CD2 1 ATOM 2782 C CE1 . PHE A 1 361 ? 26.118 -2.296 34.892 1.00 29.57 ? 361 PHE A CE1 1 ATOM 2783 C CE2 . PHE A 1 361 ? 26.339 -0.902 32.925 1.00 22.11 ? 361 PHE A CE2 1 ATOM 2784 C CZ . PHE A 1 361 ? 26.762 -1.981 33.696 1.00 29.09 ? 361 PHE A CZ 1 ATOM 2785 N N . ALA A 1 362 ? 21.434 -1.573 36.604 1.00 35.16 ? 362 ALA A N 1 ATOM 2786 C CA . ALA A 1 362 ? 21.322 -2.811 37.342 1.00 51.36 ? 362 ALA A CA 1 ATOM 2787 C C . ALA A 1 362 ? 20.198 -3.716 36.875 1.00 75.83 ? 362 ALA A C 1 ATOM 2788 O O . ALA A 1 362 ? 20.189 -4.906 37.212 1.00 88.22 ? 362 ALA A O 1 ATOM 2789 C CB . ALA A 1 362 ? 21.221 -2.579 38.835 1.00 57.67 ? 362 ALA A CB 1 ATOM 2790 N N . SER A 1 363 ? 19.262 -3.141 36.108 1.00 76.76 ? 363 SER A N 1 ATOM 2791 C CA . SER A 1 363 ? 18.121 -3.881 35.557 1.00 78.93 ? 363 SER A CA 1 ATOM 2792 C C . SER A 1 363 ? 18.501 -4.657 34.282 1.00 78.43 ? 363 SER A C 1 ATOM 2793 O O . SER A 1 363 ? 18.300 -5.886 34.208 1.00 74.48 ? 363 SER A O 1 ATOM 2794 C CB . SER A 1 363 ? 16.900 -2.980 35.305 1.00 85.69 ? 363 SER A CB 1 ATOM 2795 O OG . SER A 1 363 ? 15.862 -3.661 34.605 1.00 94.19 ? 363 SER A OG 1 ATOM 2796 N N . GLN A 1 364 ? 19.045 -3.885 33.297 1.00 63.16 ? 364 GLN A N 1 ATOM 2797 C CA . GLN A 1 364 ? 19.485 -4.355 31.987 1.00 47.63 ? 364 GLN A CA 1 ATOM 2798 C C . GLN A 1 364 ? 20.209 -5.704 32.059 1.00 74.38 ? 364 GLN A C 1 ATOM 2799 O O . GLN A 1 364 ? 21.124 -5.888 32.857 1.00 86.60 ? 364 GLN A O 1 ATOM 2800 C CB . GLN A 1 364 ? 20.211 -3.281 31.187 1.00 39.70 ? 364 GLN A CB 1 ATOM 2801 N N . LYS A 1 365 ? 19.775 -6.657 31.225 1.00 73.59 ? 365 LYS A N 1 ATOM 2802 C CA . LYS A 1 365 ? 20.350 -7.990 31.204 1.00 71.95 ? 365 LYS A CA 1 ATOM 2803 C C . LYS A 1 365 ? 21.618 -8.166 30.382 1.00 45.98 ? 365 LYS A C 1 ATOM 2804 O O . LYS A 1 365 ? 21.876 -7.497 29.366 1.00 30.08 ? 365 LYS A O 1 ATOM 2805 C CB . LYS A 1 365 ? 19.318 -9.082 30.915 1.00 75.31 ? 365 LYS A CB 1 ATOM 2806 N N . VAL A 1 366 ? 22.386 -9.127 30.891 1.00 30.20 ? 366 VAL A N 1 ATOM 2807 C CA . VAL A 1 366 ? 23.637 -9.543 30.334 1.00 27.00 ? 366 VAL A CA 1 ATOM 2808 C C . VAL A 1 366 ? 23.438 -10.181 28.941 1.00 39.33 ? 366 VAL A C 1 ATOM 2809 O O . VAL A 1 366 ? 22.577 -11.035 28.726 1.00 25.08 ? 366 VAL A O 1 ATOM 2810 C CB . VAL A 1 366 ? 24.319 -10.517 31.314 1.00 14.95 ? 366 VAL A CB 1 ATOM 2811 C CG1 . VAL A 1 366 ? 25.478 -11.233 30.657 1.00 15.64 ? 366 VAL A CG1 1 ATOM 2812 C CG2 . VAL A 1 366 ? 24.858 -9.760 32.520 1.00 16.71 ? 366 VAL A CG2 1 ATOM 2813 N N . ARG A 1 367 ? 24.222 -9.787 27.955 1.00 34.54 ? 367 ARG A N 1 ATOM 2814 C CA . ARG A 1 367 ? 24.023 -10.450 26.710 1.00 28.23 ? 367 ARG A CA 1 ATOM 2815 C C . ARG A 1 367 ? 25.326 -10.931 26.152 1.00 36.20 ? 367 ARG A C 1 ATOM 2816 O O . ARG A 1 367 ? 26.373 -10.407 26.543 1.00 49.33 ? 367 ARG A O 1 ATOM 2817 C CB . ARG A 1 367 ? 23.007 -9.863 25.730 1.00 45.88 ? 367 ARG A CB 1 ATOM 2818 C CG . ARG A 1 367 ? 23.129 -8.404 25.288 1.00 45.26 ? 367 ARG A CG 1 ATOM 2819 C CD . ARG A 1 367 ? 22.050 -8.105 24.224 1.00 62.38 ? 367 ARG A CD 1 ATOM 2820 N NE . ARG A 1 367 ? 22.353 -8.644 22.867 1.00 100.00 ? 367 ARG A NE 1 ATOM 2821 C CZ . ARG A 1 367 ? 21.506 -8.837 21.811 1.00 97.59 ? 367 ARG A CZ 1 ATOM 2822 N NH1 . ARG A 1 367 ? 20.184 -8.550 21.836 1.00 15.51 ? 367 ARG A NH1 1 ATOM 2823 N NH2 . ARG A 1 367 ? 22.031 -9.342 20.667 1.00 30.37 ? 367 ARG A NH2 1 ATOM 2824 N N . ASN A 1 368 ? 25.274 -11.959 25.302 1.00 31.57 ? 368 ASN A N 1 ATOM 2825 C CA . ASN A 1 368 ? 26.490 -12.466 24.677 1.00 34.68 ? 368 ASN A CA 1 ATOM 2826 C C . ASN A 1 368 ? 26.780 -11.564 23.481 1.00 37.02 ? 368 ASN A C 1 ATOM 2827 O O . ASN A 1 368 ? 25.901 -11.271 22.658 1.00 40.18 ? 368 ASN A O 1 ATOM 2828 C CB . ASN A 1 368 ? 26.581 -13.970 24.317 1.00 37.24 ? 368 ASN A CB 1 ATOM 2829 C CG . ASN A 1 368 ? 25.354 -14.797 24.608 1.00 25.47 ? 368 ASN A CG 1 ATOM 2830 O OD1 . ASN A 1 368 ? 24.255 -14.293 24.891 1.00 74.07 ? 368 ASN A OD1 1 ATOM 2831 N ND2 . ASN A 1 368 ? 25.541 -16.088 24.525 1.00 41.27 ? 368 ASN A ND2 1 ATOM 2832 N N . TRP A 1 369 ? 28.022 -11.106 23.429 1.00 24.12 ? 369 TRP A N 1 ATOM 2833 C CA . TRP A 1 369 ? 28.520 -10.189 22.423 1.00 26.68 ? 369 TRP A CA 1 ATOM 2834 C C . TRP A 1 369 ? 29.347 -10.896 21.358 1.00 38.05 ? 369 TRP A C 1 ATOM 2835 O O . TRP A 1 369 ? 30.133 -11.756 21.715 1.00 30.56 ? 369 TRP A O 1 ATOM 2836 C CB . TRP A 1 369 ? 29.311 -9.059 23.149 1.00 22.14 ? 369 TRP A CB 1 ATOM 2837 C CG . TRP A 1 369 ? 30.272 -8.250 22.331 1.00 18.97 ? 369 TRP A CG 1 ATOM 2838 C CD1 . TRP A 1 369 ? 29.946 -7.157 21.642 1.00 27.06 ? 369 TRP A CD1 1 ATOM 2839 C CD2 . TRP A 1 369 ? 31.694 -8.390 22.158 1.00 17.46 ? 369 TRP A CD2 1 ATOM 2840 N NE1 . TRP A 1 369 ? 31.037 -6.594 21.041 1.00 28.70 ? 369 TRP A NE1 1 ATOM 2841 C CE2 . TRP A 1 369 ? 32.125 -7.324 21.314 1.00 19.35 ? 369 TRP A CE2 1 ATOM 2842 C CE3 . TRP A 1 369 ? 32.649 -9.295 22.631 1.00 17.36 ? 369 TRP A CE3 1 ATOM 2843 C CZ2 . TRP A 1 369 ? 33.437 -7.134 20.914 1.00 5.73 ? 369 TRP A CZ2 1 ATOM 2844 C CZ3 . TRP A 1 369 ? 33.961 -9.107 22.246 1.00 13.80 ? 369 TRP A CZ3 1 ATOM 2845 C CH2 . TRP A 1 369 ? 34.337 -8.043 21.399 1.00 13.32 ? 369 TRP A CH2 1 ATOM 2846 N N . THR A 1 370 ? 29.136 -10.508 20.071 1.00 40.63 ? 370 THR A N 1 ATOM 2847 C CA . THR A 1 370 ? 29.806 -11.065 18.897 1.00 35.40 ? 370 THR A CA 1 ATOM 2848 C C . THR A 1 370 ? 30.930 -10.193 18.366 1.00 32.82 ? 370 THR A C 1 ATOM 2849 O O . THR A 1 370 ? 30.717 -9.063 17.947 1.00 36.80 ? 370 THR A O 1 ATOM 2850 C CB . THR A 1 370 ? 28.796 -11.388 17.769 1.00 74.57 ? 370 THR A CB 1 ATOM 2851 O OG1 . THR A 1 370 ? 28.339 -12.739 17.812 1.00 71.44 ? 370 THR A OG1 1 ATOM 2852 C CG2 . THR A 1 370 ? 29.414 -11.051 16.410 1.00 83.32 ? 370 THR A CG2 1 ATOM 2853 N N . ALA A 1 371 ? 32.138 -10.737 18.379 1.00 33.13 ? 371 ALA A N 1 ATOM 2854 C CA . ALA A 1 371 ? 33.302 -10.025 17.892 1.00 37.76 ? 371 ALA A CA 1 ATOM 2855 C C . ALA A 1 371 ? 33.074 -9.477 16.486 1.00 41.53 ? 371 ALA A C 1 ATOM 2856 O O . ALA A 1 371 ? 32.683 -10.201 15.572 1.00 36.39 ? 371 ALA A O 1 ATOM 2857 C CB . ALA A 1 371 ? 34.529 -10.927 17.940 1.00 39.95 ? 371 ALA A CB 1 ATOM 2858 N N . SER A 1 372 ? 33.320 -8.181 16.350 1.00 41.72 ? 372 SER A N 1 ATOM 2859 C CA . SER A 1 372 ? 33.169 -7.481 15.098 1.00 47.10 ? 372 SER A CA 1 ATOM 2860 C C . SER A 1 372 ? 33.763 -8.219 13.957 1.00 33.71 ? 372 SER A C 1 ATOM 2861 O O . SER A 1 372 ? 33.102 -8.487 13.010 1.00 32.24 ? 372 SER A O 1 ATOM 2862 C CB . SER A 1 372 ? 33.802 -6.097 15.131 1.00 51.21 ? 372 SER A CB 1 ATOM 2863 N N . ILE A 1 373 ? 35.018 -8.538 14.090 1.00 42.41 ? 373 ILE A N 1 ATOM 2864 C CA . ILE A 1 373 ? 35.800 -9.249 13.082 1.00 54.55 ? 373 ILE A CA 1 ATOM 2865 C C . ILE A 1 373 ? 35.523 -10.758 12.859 1.00 69.60 ? 373 ILE A C 1 ATOM 2866 O O . ILE A 1 373 ? 34.860 -11.183 11.910 1.00 78.20 ? 373 ILE A O 1 ATOM 2867 C CB . ILE A 1 373 ? 37.272 -9.043 13.392 1.00 56.46 ? 373 ILE A CB 1 ATOM 2868 C CG1 . ILE A 1 373 ? 37.667 -7.593 13.120 1.00 52.80 ? 373 ILE A CG1 1 ATOM 2869 C CG2 . ILE A 1 373 ? 38.098 -10.016 12.568 1.00 56.96 ? 373 ILE A CG2 1 ATOM 2870 C CD1 . ILE A 1 373 ? 38.656 -7.054 14.144 1.00 34.45 ? 373 ILE A CD1 1 ATOM 2871 N N . THR A 1 374 ? 36.086 -11.564 13.748 1.00 56.31 ? 374 THR A N 1 ATOM 2872 C CA . THR A 1 374 ? 35.993 -13.009 13.760 1.00 55.31 ? 374 THR A CA 1 ATOM 2873 C C . THR A 1 374 ? 34.600 -13.649 13.872 1.00 55.22 ? 374 THR A C 1 ATOM 2874 O O . THR A 1 374 ? 34.504 -14.876 13.858 1.00 57.20 ? 374 THR A O 1 ATOM 2875 C CB . THR A 1 374 ? 36.930 -13.592 14.848 1.00 61.08 ? 374 THR A CB 1 ATOM 2876 O OG1 . THR A 1 374 ? 36.237 -13.985 16.040 1.00 45.34 ? 374 THR A OG1 1 ATOM 2877 C CG2 . THR A 1 374 ? 37.999 -12.556 15.178 1.00 26.53 ? 374 THR A CG2 1 ATOM 2878 N N . ASP A 1 375 ? 33.515 -12.896 14.004 1.00 36.21 ? 375 ASP A N 1 ATOM 2879 C CA . ASP A 1 375 ? 32.207 -13.559 14.099 1.00 39.12 ? 375 ASP A CA 1 ATOM 2880 C C . ASP A 1 375 ? 32.049 -14.657 15.192 1.00 42.47 ? 375 ASP A C 1 ATOM 2881 O O . ASP A 1 375 ? 31.490 -15.742 14.992 1.00 35.11 ? 375 ASP A O 1 ATOM 2882 C CB . ASP A 1 375 ? 31.658 -13.982 12.696 1.00 46.65 ? 375 ASP A CB 1 ATOM 2883 C CG . ASP A 1 375 ? 30.151 -14.118 12.543 1.00 89.89 ? 375 ASP A CG 1 ATOM 2884 O OD1 . ASP A 1 375 ? 29.415 -13.186 12.237 1.00 100.00 ? 375 ASP A OD1 1 ATOM 2885 O OD2 . ASP A 1 375 ? 29.763 -15.379 12.517 1.00 100.00 ? 375 ASP A OD2 1 ATOM 2886 N N . GLU A 1 376 ? 32.510 -14.393 16.406 1.00 39.53 ? 376 GLU A N 1 ATOM 2887 C CA . GLU A 1 376 ? 32.326 -15.387 17.436 1.00 35.61 ? 376 GLU A CA 1 ATOM 2888 C C . GLU A 1 376 ? 32.052 -14.664 18.705 1.00 22.71 ? 376 GLU A C 1 ATOM 2889 O O . GLU A 1 376 ? 32.666 -13.590 18.854 1.00 19.42 ? 376 GLU A O 1 ATOM 2890 C CB . GLU A 1 376 ? 33.581 -16.260 17.674 1.00 47.38 ? 376 GLU A CB 1 ATOM 2891 C CG . GLU A 1 376 ? 33.592 -17.597 16.872 1.00 100.00 ? 376 GLU A CG 1 ATOM 2892 C CD . GLU A 1 376 ? 33.356 -18.868 17.665 1.00 100.00 ? 376 GLU A CD 1 ATOM 2893 O OE1 . GLU A 1 376 ? 32.068 -19.151 17.798 1.00 100.00 ? 376 GLU A OE1 1 ATOM 2894 O OE2 . GLU A 1 376 ? 34.272 -19.635 17.982 1.00 100.00 ? 376 GLU A OE2 1 ATOM 2895 N N . VAL A 1 377 ? 31.154 -15.248 19.582 1.00 17.54 ? 377 VAL A N 1 ATOM 2896 C CA . VAL A 1 377 ? 30.855 -14.659 20.878 1.00 16.31 ? 377 VAL A CA 1 ATOM 2897 C C . VAL A 1 377 ? 32.207 -14.466 21.491 1.00 29.63 ? 377 VAL A C 1 ATOM 2898 O O . VAL A 1 377 ? 33.047 -15.361 21.436 1.00 49.37 ? 377 VAL A O 1 ATOM 2899 C CB . VAL A 1 377 ? 29.896 -15.409 21.802 1.00 31.56 ? 377 VAL A CB 1 ATOM 2900 C CG1 . VAL A 1 377 ? 28.859 -16.177 20.998 1.00 38.22 ? 377 VAL A CG1 1 ATOM 2901 C CG2 . VAL A 1 377 ? 30.612 -16.298 22.842 1.00 28.03 ? 377 VAL A CG2 1 ATOM 2902 N N . ALA A 1 378 ? 32.451 -13.282 22.001 1.00 32.53 ? 378 ALA A N 1 ATOM 2903 C CA . ALA A 1 378 ? 33.740 -13.001 22.556 1.00 33.52 ? 378 ALA A CA 1 ATOM 2904 C C . ALA A 1 378 ? 33.695 -12.524 23.982 1.00 30.81 ? 378 ALA A C 1 ATOM 2905 O O . ALA A 1 378 ? 34.764 -12.373 24.592 1.00 31.85 ? 378 ALA A O 1 ATOM 2906 C CB . ALA A 1 378 ? 34.479 -12.022 21.648 1.00 31.13 ? 378 ALA A CB 1 ATOM 2907 N N . GLY A 1 379 ? 32.485 -12.277 24.488 1.00 19.59 ? 379 GLY A N 1 ATOM 2908 C CA . GLY A 1 379 ? 32.412 -11.801 25.832 1.00 27.67 ? 379 GLY A CA 1 ATOM 2909 C C . GLY A 1 379 ? 31.022 -11.591 26.311 1.00 22.78 ? 379 GLY A C 1 ATOM 2910 O O . GLY A 1 379 ? 30.114 -12.157 25.727 1.00 18.34 ? 379 GLY A O 1 ATOM 2911 N N . GLU A 1 380 ? 30.866 -10.803 27.383 1.00 6.98 ? 380 GLU A N 1 ATOM 2912 C CA . GLU A 1 380 ? 29.542 -10.601 27.855 1.00 13.26 ? 380 GLU A CA 1 ATOM 2913 C C . GLU A 1 380 ? 29.185 -9.189 28.175 1.00 33.58 ? 380 GLU A C 1 ATOM 2914 O O . GLU A 1 380 ? 29.785 -8.590 29.068 1.00 27.61 ? 380 GLU A O 1 ATOM 2915 C CB . GLU A 1 380 ? 29.177 -11.463 29.023 1.00 12.66 ? 380 GLU A CB 1 ATOM 2916 C CG . GLU A 1 380 ? 29.369 -12.922 28.700 1.00 19.00 ? 380 GLU A CG 1 ATOM 2917 C CD . GLU A 1 380 ? 28.828 -13.776 29.795 1.00 53.63 ? 380 GLU A CD 1 ATOM 2918 O OE1 . GLU A 1 380 ? 28.822 -13.172 30.978 1.00 29.89 ? 380 GLU A OE1 1 ATOM 2919 O OE2 . GLU A 1 380 ? 28.461 -14.911 29.591 1.00 13.19 ? 380 GLU A OE2 1 ATOM 2920 N N . VAL A 1 381 ? 28.162 -8.686 27.462 1.00 26.11 ? 381 VAL A N 1 ATOM 2921 C CA . VAL A 1 381 ? 27.721 -7.338 27.729 1.00 17.27 ? 381 VAL A CA 1 ATOM 2922 C C . VAL A 1 381 ? 26.624 -7.177 28.770 1.00 36.72 ? 381 VAL A C 1 ATOM 2923 O O . VAL A 1 381 ? 25.826 -8.076 29.105 1.00 23.52 ? 381 VAL A O 1 ATOM 2924 C CB . VAL A 1 381 ? 27.404 -6.393 26.582 1.00 7.57 ? 381 VAL A CB 1 ATOM 2925 C CG1 . VAL A 1 381 ? 28.490 -5.349 26.250 1.00 6.00 ? 381 VAL A CG1 1 ATOM 2926 C CG2 . VAL A 1 381 ? 26.701 -7.046 25.410 1.00 9.04 ? 381 VAL A CG2 1 ATOM 2927 N N . LYS A 1 382 ? 26.697 -5.915 29.220 1.00 35.60 ? 382 LYS A N 1 ATOM 2928 C CA . LYS A 1 382 ? 25.909 -5.151 30.147 1.00 21.26 ? 382 LYS A CA 1 ATOM 2929 C C . LYS A 1 382 ? 26.109 -3.740 29.658 1.00 20.47 ? 382 LYS A C 1 ATOM 2930 O O . LYS A 1 382 ? 27.208 -3.205 29.785 1.00 32.59 ? 382 LYS A O 1 ATOM 2931 C CB . LYS A 1 382 ? 26.272 -5.289 31.602 1.00 15.65 ? 382 LYS A CB 1 ATOM 2932 C CG . LYS A 1 382 ? 25.096 -5.788 32.419 1.00 7.19 ? 382 LYS A CG 1 ATOM 2933 C CD . LYS A 1 382 ? 24.579 -4.788 33.459 1.00 9.72 ? 382 LYS A CD 1 ATOM 2934 C CE . LYS A 1 382 ? 24.018 -5.497 34.718 1.00 2.83 ? 382 LYS A CE 1 ATOM 2935 N NZ . LYS A 1 382 ? 24.116 -4.713 35.982 1.00 16.59 ? 382 LYS A NZ 1 ATOM 2936 N N . SER A 1 383 ? 25.073 -3.207 29.005 1.00 16.51 ? 383 SER A N 1 ATOM 2937 C CA . SER A 1 383 ? 25.086 -1.861 28.467 1.00 23.37 ? 383 SER A CA 1 ATOM 2938 C C . SER A 1 383 ? 23.878 -1.061 28.920 1.00 39.89 ? 383 SER A C 1 ATOM 2939 O O . SER A 1 383 ? 22.829 -1.618 29.203 1.00 41.07 ? 383 SER A O 1 ATOM 2940 C CB . SER A 1 383 ? 25.388 -1.686 27.003 1.00 21.83 ? 383 SER A CB 1 ATOM 2941 O OG . SER A 1 383 ? 25.941 -0.382 26.858 1.00 18.76 ? 383 SER A OG 1 ATOM 2942 N N . TYR A 1 384 ? 24.068 0.241 29.042 1.00 39.16 ? 384 TYR A N 1 ATOM 2943 C CA . TYR A 1 384 ? 23.081 1.225 29.452 1.00 44.36 ? 384 TYR A CA 1 ATOM 2944 C C . TYR A 1 384 ? 23.681 2.555 29.147 1.00 42.90 ? 384 TYR A C 1 ATOM 2945 O O . TYR A 1 384 ? 24.666 2.965 29.753 1.00 48.58 ? 384 TYR A O 1 ATOM 2946 C CB . TYR A 1 384 ? 22.312 1.118 30.835 1.00 56.98 ? 384 TYR A CB 1 ATOM 2947 C CG . TYR A 1 384 ? 21.040 1.996 30.864 1.00 77.57 ? 384 TYR A CG 1 ATOM 2948 C CD1 . TYR A 1 384 ? 21.128 3.355 31.172 1.00 85.75 ? 384 TYR A CD1 1 ATOM 2949 C CD2 . TYR A 1 384 ? 19.770 1.507 30.533 1.00 81.21 ? 384 TYR A CD2 1 ATOM 2950 C CE1 . TYR A 1 384 ? 20.017 4.201 31.178 1.00 87.34 ? 384 TYR A CE1 1 ATOM 2951 C CE2 . TYR A 1 384 ? 18.644 2.336 30.520 1.00 84.76 ? 384 TYR A CE2 1 ATOM 2952 C CZ . TYR A 1 384 ? 18.765 3.686 30.845 1.00 96.73 ? 384 TYR A CZ 1 ATOM 2953 O OH . TYR A 1 384 ? 17.675 4.512 30.850 1.00 100.00 ? 384 TYR A OH 1 ATOM 2954 N N . LYS A 1 385 ? 23.079 3.176 28.159 1.00 33.56 ? 385 LYS A N 1 ATOM 2955 C CA . LYS A 1 385 ? 23.507 4.447 27.674 1.00 31.82 ? 385 LYS A CA 1 ATOM 2956 C C . LYS A 1 385 ? 25.005 4.475 27.437 1.00 38.26 ? 385 LYS A C 1 ATOM 2957 O O . LYS A 1 385 ? 25.558 3.537 26.846 1.00 53.22 ? 385 LYS A O 1 ATOM 2958 C CB . LYS A 1 385 ? 22.841 5.650 28.323 1.00 29.74 ? 385 LYS A CB 1 ATOM 2959 C CG . LYS A 1 385 ? 21.428 5.342 28.800 1.00 20.10 ? 385 LYS A CG 1 ATOM 2960 C CD . LYS A 1 385 ? 20.322 5.943 27.935 1.00 30.37 ? 385 LYS A CD 1 ATOM 2961 C CE . LYS A 1 385 ? 18.931 5.831 28.574 1.00 76.01 ? 385 LYS A CE 1 ATOM 2962 N NZ . LYS A 1 385 ? 17.965 6.859 28.131 1.00 100.00 ? 385 LYS A NZ 1 ATOM 2963 N N . HIS A 1 386 ? 25.647 5.512 27.915 1.00 26.29 ? 386 HIS A N 1 ATOM 2964 C CA . HIS A 1 386 ? 27.071 5.708 27.747 1.00 31.46 ? 386 HIS A CA 1 ATOM 2965 C C . HIS A 1 386 ? 27.923 4.910 28.726 1.00 28.90 ? 386 HIS A C 1 ATOM 2966 O O . HIS A 1 386 ? 29.132 5.146 28.818 1.00 14.85 ? 386 HIS A O 1 ATOM 2967 C CB . HIS A 1 386 ? 27.401 7.213 27.836 1.00 36.94 ? 386 HIS A CB 1 ATOM 2968 C CG . HIS A 1 386 ? 26.628 7.807 28.964 1.00 49.75 ? 386 HIS A CG 1 ATOM 2969 N ND1 . HIS A 1 386 ? 27.088 7.739 30.270 1.00 60.43 ? 386 HIS A ND1 1 ATOM 2970 C CD2 . HIS A 1 386 ? 25.420 8.424 28.987 1.00 62.44 ? 386 HIS A CD2 1 ATOM 2971 C CE1 . HIS A 1 386 ? 26.189 8.328 31.051 1.00 61.34 ? 386 HIS A CE1 1 ATOM 2972 N NE2 . HIS A 1 386 ? 25.174 8.746 30.309 1.00 63.94 ? 386 HIS A NE2 1 ATOM 2973 N N . PHE A 1 387 ? 27.294 3.968 29.459 1.00 15.65 ? 387 PHE A N 1 ATOM 2974 C CA . PHE A 1 387 ? 28.017 3.137 30.424 1.00 9.72 ? 387 PHE A CA 1 ATOM 2975 C C . PHE A 1 387 ? 27.873 1.647 30.149 1.00 22.65 ? 387 PHE A C 1 ATOM 2976 O O . PHE A 1 387 ? 26.801 1.073 30.339 1.00 20.89 ? 387 PHE A O 1 ATOM 2977 C CB . PHE A 1 387 ? 27.606 3.417 31.859 1.00 20.26 ? 387 PHE A CB 1 ATOM 2978 C CG . PHE A 1 387 ? 28.497 2.786 32.922 1.00 26.87 ? 387 PHE A CG 1 ATOM 2979 C CD1 . PHE A 1 387 ? 29.885 2.978 32.903 1.00 28.54 ? 387 PHE A CD1 1 ATOM 2980 C CD2 . PHE A 1 387 ? 27.938 2.037 33.961 1.00 23.17 ? 387 PHE A CD2 1 ATOM 2981 C CE1 . PHE A 1 387 ? 30.721 2.422 33.873 1.00 5.56 ? 387 PHE A CE1 1 ATOM 2982 C CE2 . PHE A 1 387 ? 28.746 1.485 34.955 1.00 20.57 ? 387 PHE A CE2 1 ATOM 2983 C CZ . PHE A 1 387 ? 30.130 1.679 34.896 1.00 16.65 ? 387 PHE A CZ 1 ATOM 2984 N N . THR A 1 388 ? 28.988 1.037 29.733 1.00 23.12 ? 388 THR A N 1 ATOM 2985 C CA . THR A 1 388 ? 29.007 -0.351 29.409 1.00 24.21 ? 388 THR A CA 1 ATOM 2986 C C . THR A 1 388 ? 30.062 -1.202 30.051 1.00 25.82 ? 388 THR A C 1 ATOM 2987 O O . THR A 1 388 ? 31.239 -0.899 29.982 1.00 32.68 ? 388 THR A O 1 ATOM 2988 C CB . THR A 1 388 ? 29.183 -0.485 27.896 1.00 46.12 ? 388 THR A CB 1 ATOM 2989 O OG1 . THR A 1 388 ? 28.155 0.272 27.230 1.00 21.35 ? 388 THR A OG1 1 ATOM 2990 C CG2 . THR A 1 388 ? 29.247 -1.993 27.560 1.00 11.64 ? 388 THR A CG2 1 ATOM 2991 N N . TYR A 1 389 ? 29.615 -2.310 30.621 1.00 24.69 ? 389 TYR A N 1 ATOM 2992 C CA . TYR A 1 389 ? 30.496 -3.274 31.245 1.00 18.16 ? 389 TYR A CA 1 ATOM 2993 C C . TYR A 1 389 ? 30.587 -4.567 30.403 1.00 27.22 ? 389 TYR A C 1 ATOM 2994 O O . TYR A 1 389 ? 29.626 -5.348 30.335 1.00 22.05 ? 389 TYR A O 1 ATOM 2995 C CB . TYR A 1 389 ? 30.120 -3.662 32.698 1.00 5.86 ? 389 TYR A CB 1 ATOM 2996 C CG . TYR A 1 389 ? 31.013 -4.841 33.085 1.00 30.19 ? 389 TYR A CG 1 ATOM 2997 C CD1 . TYR A 1 389 ? 32.382 -4.663 33.348 1.00 35.61 ? 389 TYR A CD1 1 ATOM 2998 C CD2 . TYR A 1 389 ? 30.518 -6.150 33.125 1.00 29.44 ? 389 TYR A CD2 1 ATOM 2999 C CE1 . TYR A 1 389 ? 33.233 -5.722 33.682 1.00 15.86 ? 389 TYR A CE1 1 ATOM 3000 C CE2 . TYR A 1 389 ? 31.350 -7.222 33.457 1.00 25.22 ? 389 TYR A CE2 1 ATOM 3001 C CZ . TYR A 1 389 ? 32.706 -7.018 33.746 1.00 41.32 ? 389 TYR A CZ 1 ATOM 3002 O OH . TYR A 1 389 ? 33.520 -8.111 34.090 1.00 19.79 ? 389 TYR A OH 1 ATOM 3003 N N . LEU A 1 390 ? 31.746 -4.820 29.778 1.00 16.61 ? 390 LEU A N 1 ATOM 3004 C CA . LEU A 1 390 ? 31.980 -6.031 28.951 1.00 18.33 ? 390 LEU A CA 1 ATOM 3005 C C . LEU A 1 390 ? 32.959 -7.084 29.562 1.00 22.38 ? 390 LEU A C 1 ATOM 3006 O O . LEU A 1 390 ? 34.042 -6.768 30.036 1.00 39.46 ? 390 LEU A O 1 ATOM 3007 C CB . LEU A 1 390 ? 32.566 -5.580 27.595 1.00 14.94 ? 390 LEU A CB 1 ATOM 3008 C CG . LEU A 1 390 ? 32.834 -6.695 26.623 1.00 1.00 ? 390 LEU A CG 1 ATOM 3009 C CD1 . LEU A 1 390 ? 31.519 -7.361 26.239 1.00 1.00 ? 390 LEU A CD1 1 ATOM 3010 C CD2 . LEU A 1 390 ? 33.521 -6.053 25.435 1.00 1.00 ? 390 LEU A CD2 1 ATOM 3011 N N . ARG A 1 391 ? 32.616 -8.359 29.534 1.00 17.88 ? 391 ARG A N 1 ATOM 3012 C CA . ARG A 1 391 ? 33.518 -9.394 30.048 1.00 16.96 ? 391 ARG A CA 1 ATOM 3013 C C . ARG A 1 391 ? 34.261 -10.053 28.867 1.00 19.88 ? 391 ARG A C 1 ATOM 3014 O O . ARG A 1 391 ? 33.667 -10.784 28.118 1.00 19.92 ? 391 ARG A O 1 ATOM 3015 C CB . ARG A 1 391 ? 32.768 -10.497 30.798 1.00 10.18 ? 391 ARG A CB 1 ATOM 3016 C CG . ARG A 1 391 ? 33.498 -11.849 30.702 1.00 23.89 ? 391 ARG A CG 1 ATOM 3017 C CD . ARG A 1 391 ? 32.819 -12.981 31.464 1.00 25.29 ? 391 ARG A CD 1 ATOM 3018 N NE . ARG A 1 391 ? 33.461 -14.281 31.301 1.00 22.96 ? 391 ARG A NE 1 ATOM 3019 C CZ . ARG A 1 391 ? 32.966 -15.416 31.821 1.00 51.87 ? 391 ARG A CZ 1 ATOM 3020 N NH1 . ARG A 1 391 ? 31.837 -15.484 32.529 1.00 32.54 ? 391 ARG A NH1 1 ATOM 3021 N NH2 . ARG A 1 391 ? 33.621 -16.538 31.625 1.00 9.23 ? 391 ARG A NH2 1 ATOM 3022 N N . VAL A 1 392 ? 35.552 -9.805 28.670 1.00 23.78 ? 392 VAL A N 1 ATOM 3023 C CA . VAL A 1 392 ? 36.284 -10.409 27.554 1.00 17.78 ? 392 VAL A CA 1 ATOM 3024 C C . VAL A 1 392 ? 36.654 -11.871 27.786 1.00 20.04 ? 392 VAL A C 1 ATOM 3025 O O . VAL A 1 392 ? 37.502 -12.162 28.627 1.00 22.49 ? 392 VAL A O 1 ATOM 3026 C CB . VAL A 1 392 ? 37.422 -9.534 27.069 1.00 14.57 ? 392 VAL A CB 1 ATOM 3027 C CG1 . VAL A 1 392 ? 38.163 -10.234 25.953 1.00 22.71 ? 392 VAL A CG1 1 ATOM 3028 C CG2 . VAL A 1 392 ? 36.775 -8.326 26.441 1.00 11.26 ? 392 VAL A CG2 1 ATOM 3029 N N . PHE A 1 393 ? 35.963 -12.757 27.047 1.00 20.52 ? 393 PHE A N 1 ATOM 3030 C CA . PHE A 1 393 ? 36.092 -14.221 27.075 1.00 13.04 ? 393 PHE A CA 1 ATOM 3031 C C . PHE A 1 393 ? 37.467 -14.539 26.616 1.00 16.40 ? 393 PHE A C 1 ATOM 3032 O O . PHE A 1 393 ? 37.904 -14.022 25.575 1.00 23.97 ? 393 PHE A O 1 ATOM 3033 C CB . PHE A 1 393 ? 35.125 -14.854 26.055 1.00 19.95 ? 393 PHE A CB 1 ATOM 3034 C CG . PHE A 1 393 ? 33.718 -15.190 26.510 1.00 24.85 ? 393 PHE A CG 1 ATOM 3035 C CD1 . PHE A 1 393 ? 33.324 -15.043 27.839 1.00 44.18 ? 393 PHE A CD1 1 ATOM 3036 C CD2 . PHE A 1 393 ? 32.780 -15.695 25.611 1.00 29.00 ? 393 PHE A CD2 1 ATOM 3037 C CE1 . PHE A 1 393 ? 32.035 -15.382 28.261 1.00 43.96 ? 393 PHE A CE1 1 ATOM 3038 C CE2 . PHE A 1 393 ? 31.488 -16.043 26.011 1.00 32.61 ? 393 PHE A CE2 1 ATOM 3039 C CZ . PHE A 1 393 ? 31.113 -15.885 27.345 1.00 29.44 ? 393 PHE A CZ 1 ATOM 3040 N N . ASN A 1 394 ? 38.122 -15.365 27.413 1.00 18.90 ? 394 ASN A N 1 ATOM 3041 C CA . ASN A 1 394 ? 39.492 -15.796 27.194 1.00 19.91 ? 394 ASN A CA 1 ATOM 3042 C C . ASN A 1 394 ? 40.393 -14.600 27.005 1.00 29.72 ? 394 ASN A C 1 ATOM 3043 O O . ASN A 1 394 ? 40.803 -14.316 25.860 1.00 31.44 ? 394 ASN A O 1 ATOM 3044 C CB . ASN A 1 394 ? 39.676 -16.881 26.093 1.00 13.59 ? 394 ASN A CB 1 ATOM 3045 C CG . ASN A 1 394 ? 38.738 -18.066 26.254 1.00 52.75 ? 394 ASN A CG 1 ATOM 3046 O OD1 . ASN A 1 394 ? 38.763 -18.795 27.270 1.00 74.72 ? 394 ASN A OD1 1 ATOM 3047 N ND2 . ASN A 1 394 ? 37.931 -18.277 25.217 1.00 41.92 ? 394 ASN A ND2 1 ATOM 3048 N N . GLY A 1 395 ? 40.651 -13.937 28.163 1.00 35.63 ? 395 GLY A N 1 ATOM 3049 C CA . GLY A 1 395 ? 41.482 -12.739 28.327 1.00 33.60 ? 395 GLY A CA 1 ATOM 3050 C C . GLY A 1 395 ? 42.256 -12.706 29.646 1.00 25.70 ? 395 GLY A C 1 ATOM 3051 O O . GLY A 1 395 ? 41.826 -13.136 30.733 1.00 14.76 ? 395 GLY A O 1 ATOM 3052 N N . GLY A 1 396 ? 43.452 -12.199 29.548 1.00 19.37 ? 396 GLY A N 1 ATOM 3053 C CA . GLY A 1 396 ? 44.219 -12.124 30.748 1.00 25.65 ? 396 GLY A CA 1 ATOM 3054 C C . GLY A 1 396 ? 44.333 -10.660 31.121 1.00 36.76 ? 396 GLY A C 1 ATOM 3055 O O . GLY A 1 396 ? 43.629 -9.827 30.591 1.00 46.41 ? 396 GLY A O 1 ATOM 3056 N N . HIS A 1 397 ? 45.233 -10.345 32.009 1.00 33.16 ? 397 HIS A N 1 ATOM 3057 C CA . HIS A 1 397 ? 45.435 -8.980 32.444 1.00 36.05 ? 397 HIS A CA 1 ATOM 3058 C C . HIS A 1 397 ? 45.667 -7.986 31.337 1.00 36.13 ? 397 HIS A C 1 ATOM 3059 O O . HIS A 1 397 ? 45.463 -6.804 31.520 1.00 41.73 ? 397 HIS A O 1 ATOM 3060 C CB . HIS A 1 397 ? 46.600 -8.881 33.423 1.00 31.22 ? 397 HIS A CB 1 ATOM 3061 C CG . HIS A 1 397 ? 46.655 -7.575 34.109 1.00 16.75 ? 397 HIS A CG 1 ATOM 3062 N ND1 . HIS A 1 397 ? 45.703 -7.238 35.056 1.00 7.96 ? 397 HIS A ND1 1 ATOM 3063 C CD2 . HIS A 1 397 ? 47.567 -6.589 33.985 1.00 7.26 ? 397 HIS A CD2 1 ATOM 3064 C CE1 . HIS A 1 397 ? 46.036 -6.045 35.489 1.00 8.03 ? 397 HIS A CE1 1 ATOM 3065 N NE2 . HIS A 1 397 ? 47.159 -5.634 34.864 1.00 9.90 ? 397 HIS A NE2 1 ATOM 3066 N N . MET A 1 398 ? 46.118 -8.466 30.212 1.00 23.72 ? 398 MET A N 1 ATOM 3067 C CA . MET A 1 398 ? 46.370 -7.617 29.071 1.00 19.22 ? 398 MET A CA 1 ATOM 3068 C C . MET A 1 398 ? 45.698 -8.297 27.930 1.00 21.06 ? 398 MET A C 1 ATOM 3069 O O . MET A 1 398 ? 46.230 -9.108 27.211 1.00 32.43 ? 398 MET A O 1 ATOM 3070 C CB . MET A 1 398 ? 47.858 -7.499 28.856 1.00 24.03 ? 398 MET A CB 1 ATOM 3071 C CG . MET A 1 398 ? 48.571 -7.998 30.075 1.00 33.00 ? 398 MET A CG 1 ATOM 3072 S SD . MET A 1 398 ? 50.319 -7.667 29.905 1.00 48.07 ? 398 MET A SD 1 ATOM 3073 C CE . MET A 1 398 ? 50.695 -7.553 31.674 1.00 50.68 ? 398 MET A CE 1 ATOM 3074 N N . VAL A 1 399 ? 44.476 -7.965 27.836 1.00 16.65 ? 399 VAL A N 1 ATOM 3075 C CA . VAL A 1 399 ? 43.585 -8.496 26.879 1.00 12.66 ? 399 VAL A CA 1 ATOM 3076 C C . VAL A 1 399 ? 44.059 -8.429 25.454 1.00 25.96 ? 399 VAL A C 1 ATOM 3077 O O . VAL A 1 399 ? 43.827 -9.392 24.729 1.00 23.76 ? 399 VAL A O 1 ATOM 3078 C CB . VAL A 1 399 ? 42.263 -7.772 27.075 1.00 6.69 ? 399 VAL A CB 1 ATOM 3079 C CG1 . VAL A 1 399 ? 41.436 -7.779 25.806 1.00 1.20 ? 399 VAL A CG1 1 ATOM 3080 C CG2 . VAL A 1 399 ? 41.493 -8.450 28.215 1.00 7.18 ? 399 VAL A CG2 1 ATOM 3081 N N . PRO A 1 400 ? 44.699 -7.293 25.050 1.00 19.66 ? 400 PRO A N 1 ATOM 3082 C CA . PRO A 1 400 ? 45.159 -7.117 23.671 1.00 8.70 ? 400 PRO A CA 1 ATOM 3083 C C . PRO A 1 400 ? 46.252 -8.066 23.289 1.00 19.47 ? 400 PRO A C 1 ATOM 3084 O O . PRO A 1 400 ? 46.401 -8.487 22.150 1.00 16.26 ? 400 PRO A O 1 ATOM 3085 C CB . PRO A 1 400 ? 45.608 -5.707 23.508 1.00 1.35 ? 400 PRO A CB 1 ATOM 3086 C CG . PRO A 1 400 ? 45.266 -5.021 24.794 1.00 10.73 ? 400 PRO A CG 1 ATOM 3087 C CD . PRO A 1 400 ? 45.118 -6.127 25.840 1.00 10.47 ? 400 PRO A CD 1 ATOM 3088 N N . PHE A 1 401 ? 46.998 -8.432 24.284 1.00 28.52 ? 401 PHE A N 1 ATOM 3089 C CA . PHE A 1 401 ? 48.062 -9.363 24.073 1.00 25.33 ? 401 PHE A CA 1 ATOM 3090 C C . PHE A 1 401 ? 47.490 -10.727 23.796 1.00 6.56 ? 401 PHE A C 1 ATOM 3091 O O . PHE A 1 401 ? 47.772 -11.373 22.813 1.00 34.37 ? 401 PHE A O 1 ATOM 3092 C CB . PHE A 1 401 ? 48.945 -9.391 25.291 1.00 28.82 ? 401 PHE A CB 1 ATOM 3093 C CG . PHE A 1 401 ? 49.730 -10.648 25.375 1.00 40.36 ? 401 PHE A CG 1 ATOM 3094 C CD1 . PHE A 1 401 ? 50.984 -10.737 24.774 1.00 47.25 ? 401 PHE A CD1 1 ATOM 3095 C CD2 . PHE A 1 401 ? 49.244 -11.736 26.103 1.00 50.11 ? 401 PHE A CD2 1 ATOM 3096 C CE1 . PHE A 1 401 ? 51.728 -11.911 24.884 1.00 40.56 ? 401 PHE A CE1 1 ATOM 3097 C CE2 . PHE A 1 401 ? 49.976 -12.915 26.229 1.00 43.14 ? 401 PHE A CE2 1 ATOM 3098 C CZ . PHE A 1 401 ? 51.220 -12.986 25.610 1.00 31.13 ? 401 PHE A CZ 1 ATOM 3099 N N . ASP A 1 402 ? 46.657 -11.146 24.648 1.00 12.97 ? 402 ASP A N 1 ATOM 3100 C CA . ASP A 1 402 ? 46.015 -12.429 24.487 1.00 24.42 ? 402 ASP A CA 1 ATOM 3101 C C . ASP A 1 402 ? 45.164 -12.525 23.178 1.00 52.94 ? 402 ASP A C 1 ATOM 3102 O O . ASP A 1 402 ? 45.525 -13.260 22.269 1.00 72.14 ? 402 ASP A O 1 ATOM 3103 C CB . ASP A 1 402 ? 45.249 -12.911 25.782 1.00 24.94 ? 402 ASP A CB 1 ATOM 3104 C CG . ASP A 1 402 ? 45.971 -12.671 27.121 1.00 56.91 ? 402 ASP A CG 1 ATOM 3105 O OD1 . ASP A 1 402 ? 47.109 -13.327 27.262 1.00 53.86 ? 402 ASP A OD1 1 ATOM 3106 O OD2 . ASP A 1 402 ? 45.504 -11.960 28.008 1.00 58.44 ? 402 ASP A OD2 1 ATOM 3107 N N . VAL A 1 403 ? 44.050 -11.762 23.084 1.00 34.70 ? 403 VAL A N 1 ATOM 3108 C CA . VAL A 1 403 ? 43.141 -11.807 21.936 1.00 16.94 ? 403 VAL A CA 1 ATOM 3109 C C . VAL A 1 403 ? 43.069 -10.538 21.076 1.00 26.09 ? 403 VAL A C 1 ATOM 3110 O O . VAL A 1 403 ? 42.133 -9.738 21.105 1.00 24.91 ? 403 VAL A O 1 ATOM 3111 C CB . VAL A 1 403 ? 41.776 -12.176 22.475 1.00 18.94 ? 403 VAL A CB 1 ATOM 3112 C CG1 . VAL A 1 403 ? 41.799 -13.545 23.165 1.00 27.12 ? 403 VAL A CG1 1 ATOM 3113 C CG2 . VAL A 1 403 ? 41.466 -11.164 23.539 1.00 14.38 ? 403 VAL A CG2 1 ATOM 3114 N N . PRO A 1 404 ? 44.069 -10.363 20.250 1.00 30.12 ? 404 PRO A N 1 ATOM 3115 C CA . PRO A 1 404 ? 44.110 -9.212 19.405 1.00 24.20 ? 404 PRO A CA 1 ATOM 3116 C C . PRO A 1 404 ? 42.902 -9.023 18.520 1.00 17.26 ? 404 PRO A C 1 ATOM 3117 O O . PRO A 1 404 ? 42.432 -7.911 18.346 1.00 19.45 ? 404 PRO A O 1 ATOM 3118 C CB . PRO A 1 404 ? 45.395 -9.368 18.584 1.00 26.97 ? 404 PRO A CB 1 ATOM 3119 C CG . PRO A 1 404 ? 46.302 -10.344 19.314 1.00 21.80 ? 404 PRO A CG 1 ATOM 3120 C CD . PRO A 1 404 ? 45.429 -10.966 20.398 1.00 30.17 ? 404 PRO A CD 1 ATOM 3121 N N . GLU A 1 405 ? 42.441 -10.097 17.925 1.00 17.53 ? 405 GLU A N 1 ATOM 3122 C CA . GLU A 1 405 ? 41.297 -9.997 17.049 1.00 19.76 ? 405 GLU A CA 1 ATOM 3123 C C . GLU A 1 405 ? 40.176 -9.359 17.809 1.00 26.67 ? 405 GLU A C 1 ATOM 3124 O O . GLU A 1 405 ? 39.791 -8.242 17.489 1.00 31.55 ? 405 GLU A O 1 ATOM 3125 C CB . GLU A 1 405 ? 40.913 -11.374 16.481 1.00 20.49 ? 405 GLU A CB 1 ATOM 3126 C CG . GLU A 1 405 ? 41.752 -12.512 17.125 1.00 60.86 ? 405 GLU A CG 1 ATOM 3127 C CD . GLU A 1 405 ? 42.861 -13.070 16.255 1.00 100.00 ? 405 GLU A CD 1 ATOM 3128 O OE1 . GLU A 1 405 ? 42.732 -13.295 15.062 1.00 84.86 ? 405 GLU A OE1 1 ATOM 3129 O OE2 . GLU A 1 405 ? 43.974 -13.329 16.920 1.00 100.00 ? 405 GLU A OE2 1 ATOM 3130 N N . ASN A 1 406 ? 39.772 -10.019 18.888 1.00 22.72 ? 406 ASN A N 1 ATOM 3131 C CA . ASN A 1 406 ? 38.725 -9.500 19.718 1.00 15.33 ? 406 ASN A CA 1 ATOM 3132 C C . ASN A 1 406 ? 38.917 -8.082 20.277 1.00 30.71 ? 406 ASN A C 1 ATOM 3133 O O . ASN A 1 406 ? 37.999 -7.275 20.208 1.00 14.17 ? 406 ASN A O 1 ATOM 3134 C CB . ASN A 1 406 ? 38.019 -10.553 20.560 1.00 32.59 ? 406 ASN A CB 1 ATOM 3135 C CG . ASN A 1 406 ? 37.731 -11.796 19.726 1.00 30.56 ? 406 ASN A CG 1 ATOM 3136 O OD1 . ASN A 1 406 ? 38.459 -12.050 18.796 1.00 52.45 ? 406 ASN A OD1 1 ATOM 3137 N ND2 . ASN A 1 406 ? 36.718 -12.599 20.073 1.00 82.94 ? 406 ASN A ND2 1 ATOM 3138 N N . ALA A 1 407 ? 40.118 -7.755 20.790 1.00 40.48 ? 407 ALA A N 1 ATOM 3139 C CA . ALA A 1 407 ? 40.388 -6.419 21.323 1.00 35.03 ? 407 ALA A CA 1 ATOM 3140 C C . ALA A 1 407 ? 40.020 -5.337 20.317 1.00 57.38 ? 407 ALA A C 1 ATOM 3141 O O . ALA A 1 407 ? 39.241 -4.404 20.584 1.00 65.30 ? 407 ALA A O 1 ATOM 3142 C CB . ALA A 1 407 ? 41.850 -6.264 21.678 1.00 31.12 ? 407 ALA A CB 1 ATOM 3143 N N . LEU A 1 408 ? 40.598 -5.455 19.134 1.00 50.03 ? 408 LEU A N 1 ATOM 3144 C CA . LEU A 1 408 ? 40.301 -4.469 18.124 1.00 40.33 ? 408 LEU A CA 1 ATOM 3145 C C . LEU A 1 408 ? 38.827 -4.466 17.822 1.00 16.77 ? 408 LEU A C 1 ATOM 3146 O O . LEU A 1 408 ? 38.231 -3.414 17.679 1.00 2.72 ? 408 LEU A O 1 ATOM 3147 C CB . LEU A 1 408 ? 41.136 -4.619 16.862 1.00 35.26 ? 408 LEU A CB 1 ATOM 3148 C CG . LEU A 1 408 ? 40.962 -3.389 16.007 1.00 39.23 ? 408 LEU A CG 1 ATOM 3149 C CD1 . LEU A 1 408 ? 40.645 -2.223 16.922 1.00 44.11 ? 408 LEU A CD1 1 ATOM 3150 C CD2 . LEU A 1 408 ? 42.240 -3.086 15.259 1.00 38.04 ? 408 LEU A CD2 1 ATOM 3151 N N . SER A 1 409 ? 38.283 -5.678 17.772 1.00 4.24 ? 409 SER A N 1 ATOM 3152 C CA . SER A 1 409 ? 36.883 -5.897 17.529 1.00 13.93 ? 409 SER A CA 1 ATOM 3153 C C . SER A 1 409 ? 36.085 -4.995 18.480 1.00 24.83 ? 409 SER A C 1 ATOM 3154 O O . SER A 1 409 ? 35.260 -4.156 18.057 1.00 17.94 ? 409 SER A O 1 ATOM 3155 C CB . SER A 1 409 ? 36.542 -7.376 17.767 1.00 21.48 ? 409 SER A CB 1 ATOM 3156 O OG . SER A 1 409 ? 36.396 -8.076 16.536 1.00 13.03 ? 409 SER A OG 1 ATOM 3157 N N . MET A 1 410 ? 36.397 -5.185 19.775 1.00 17.20 ? 410 MET A N 1 ATOM 3158 C CA . MET A 1 410 ? 35.834 -4.445 20.875 1.00 12.19 ? 410 MET A CA 1 ATOM 3159 C C . MET A 1 410 ? 36.282 -3.020 20.765 1.00 17.42 ? 410 MET A C 1 ATOM 3160 O O . MET A 1 410 ? 35.505 -2.124 21.085 1.00 19.54 ? 410 MET A O 1 ATOM 3161 C CB . MET A 1 410 ? 36.308 -4.990 22.224 1.00 17.82 ? 410 MET A CB 1 ATOM 3162 C CG . MET A 1 410 ? 35.994 -4.129 23.458 1.00 25.14 ? 410 MET A CG 1 ATOM 3163 S SD . MET A 1 410 ? 37.351 -4.176 24.683 1.00 26.79 ? 410 MET A SD 1 ATOM 3164 C CE . MET A 1 410 ? 38.593 -3.376 23.629 1.00 4.99 ? 410 MET A CE 1 ATOM 3165 N N . VAL A 1 411 ? 37.509 -2.825 20.294 1.00 7.88 ? 411 VAL A N 1 ATOM 3166 C CA . VAL A 1 411 ? 37.992 -1.476 20.157 1.00 8.01 ? 411 VAL A CA 1 ATOM 3167 C C . VAL A 1 411 ? 37.249 -0.587 19.185 1.00 35.93 ? 411 VAL A C 1 ATOM 3168 O O . VAL A 1 411 ? 36.469 0.253 19.618 1.00 32.49 ? 411 VAL A O 1 ATOM 3169 C CB . VAL A 1 411 ? 39.502 -1.291 20.143 1.00 8.00 ? 411 VAL A CB 1 ATOM 3170 C CG1 . VAL A 1 411 ? 39.843 0.075 19.542 1.00 1.00 ? 411 VAL A CG1 1 ATOM 3171 C CG2 . VAL A 1 411 ? 39.879 -1.217 21.609 1.00 14.79 ? 411 VAL A CG2 1 ATOM 3172 N N . ASN A 1 412 ? 37.495 -0.766 17.870 1.00 44.74 ? 412 ASN A N 1 ATOM 3173 C CA . ASN A 1 412 ? 36.867 0.047 16.824 1.00 35.74 ? 412 ASN A CA 1 ATOM 3174 C C . ASN A 1 412 ? 35.395 0.183 17.012 1.00 22.93 ? 412 ASN A C 1 ATOM 3175 O O . ASN A 1 412 ? 34.866 1.279 16.958 1.00 26.46 ? 412 ASN A O 1 ATOM 3176 C CB . ASN A 1 412 ? 37.254 -0.313 15.377 1.00 29.38 ? 412 ASN A CB 1 ATOM 3177 C CG . ASN A 1 412 ? 38.715 -0.013 15.090 1.00 34.52 ? 412 ASN A CG 1 ATOM 3178 O OD1 . ASN A 1 412 ? 39.147 0.028 13.929 1.00 28.93 ? 412 ASN A OD1 1 ATOM 3179 N ND2 . ASN A 1 412 ? 39.455 0.315 16.145 1.00 21.36 ? 412 ASN A ND2 1 ATOM 3180 N N . GLU A 1 413 ? 34.749 -0.933 17.233 1.00 18.14 ? 413 GLU A N 1 ATOM 3181 C CA . GLU A 1 413 ? 33.328 -0.912 17.460 1.00 30.80 ? 413 GLU A CA 1 ATOM 3182 C C . GLU A 1 413 ? 32.966 0.113 18.575 1.00 44.54 ? 413 GLU A C 1 ATOM 3183 O O . GLU A 1 413 ? 32.043 0.908 18.430 1.00 43.87 ? 413 GLU A O 1 ATOM 3184 C CB . GLU A 1 413 ? 32.795 -2.342 17.675 1.00 34.62 ? 413 GLU A CB 1 ATOM 3185 C CG . GLU A 1 413 ? 31.630 -2.412 18.688 1.00 39.68 ? 413 GLU A CG 1 ATOM 3186 C CD . GLU A 1 413 ? 30.912 -3.730 18.652 1.00 100.00 ? 413 GLU A CD 1 ATOM 3187 O OE1 . GLU A 1 413 ? 31.711 -4.731 18.332 1.00 100.00 ? 413 GLU A OE1 1 ATOM 3188 O OE2 . GLU A 1 413 ? 29.713 -3.844 18.882 1.00 40.44 ? 413 GLU A OE2 1 ATOM 3189 N N . TRP A 1 414 ? 33.738 0.179 19.671 1.00 36.75 ? 414 TRP A N 1 ATOM 3190 C CA . TRP A 1 414 ? 33.431 1.198 20.660 1.00 26.60 ? 414 TRP A CA 1 ATOM 3191 C C . TRP A 1 414 ? 33.910 2.523 20.084 1.00 28.56 ? 414 TRP A C 1 ATOM 3192 O O . TRP A 1 414 ? 33.185 3.503 20.140 1.00 35.79 ? 414 TRP A O 1 ATOM 3193 C CB . TRP A 1 414 ? 34.062 1.015 22.076 1.00 21.65 ? 414 TRP A CB 1 ATOM 3194 C CG . TRP A 1 414 ? 34.004 2.241 22.996 1.00 17.76 ? 414 TRP A CG 1 ATOM 3195 C CD1 . TRP A 1 414 ? 34.849 3.383 23.024 1.00 20.68 ? 414 TRP A CD1 1 ATOM 3196 C CD2 . TRP A 1 414 ? 33.047 2.425 24.066 1.00 8.77 ? 414 TRP A CD2 1 ATOM 3197 N NE1 . TRP A 1 414 ? 34.422 4.270 24.028 1.00 11.12 ? 414 TRP A NE1 1 ATOM 3198 C CE2 . TRP A 1 414 ? 33.329 3.684 24.678 1.00 7.01 ? 414 TRP A CE2 1 ATOM 3199 C CE3 . TRP A 1 414 ? 31.967 1.636 24.544 1.00 5.70 ? 414 TRP A CE3 1 ATOM 3200 C CZ2 . TRP A 1 414 ? 32.514 4.121 25.737 1.00 17.58 ? 414 TRP A CZ2 1 ATOM 3201 C CZ3 . TRP A 1 414 ? 31.159 2.056 25.584 1.00 7.39 ? 414 TRP A CZ3 1 ATOM 3202 C CH2 . TRP A 1 414 ? 31.440 3.297 26.178 1.00 17.73 ? 414 TRP A CH2 1 ATOM 3203 N N . ILE A 1 415 ? 35.130 2.581 19.530 1.00 16.00 ? 415 ILE A N 1 ATOM 3204 C CA . ILE A 1 415 ? 35.619 3.854 18.997 1.00 19.00 ? 415 ILE A CA 1 ATOM 3205 C C . ILE A 1 415 ? 34.702 4.432 17.953 1.00 48.86 ? 415 ILE A C 1 ATOM 3206 O O . ILE A 1 415 ? 34.471 5.651 17.909 1.00 55.54 ? 415 ILE A O 1 ATOM 3207 C CB . ILE A 1 415 ? 36.949 3.714 18.296 1.00 39.17 ? 415 ILE A CB 1 ATOM 3208 C CG1 . ILE A 1 415 ? 37.685 5.045 18.253 1.00 38.04 ? 415 ILE A CG1 1 ATOM 3209 C CG2 . ILE A 1 415 ? 37.803 2.599 18.899 1.00 46.34 ? 415 ILE A CG2 1 ATOM 3210 N N . HIS A 1 416 ? 34.214 3.541 17.073 1.00 54.43 ? 416 HIS A N 1 ATOM 3211 C CA . HIS A 1 416 ? 33.337 3.928 15.960 1.00 46.07 ? 416 HIS A CA 1 ATOM 3212 C C . HIS A 1 416 ? 31.835 3.727 16.233 1.00 61.66 ? 416 HIS A C 1 ATOM 3213 O O . HIS A 1 416 ? 31.110 4.699 16.403 1.00 57.72 ? 416 HIS A O 1 ATOM 3214 C CB . HIS A 1 416 ? 33.823 3.400 14.560 1.00 31.68 ? 416 HIS A CB 1 ATOM 3215 C CG . HIS A 1 416 ? 35.250 3.787 14.181 1.00 32.19 ? 416 HIS A CG 1 ATOM 3216 N ND1 . HIS A 1 416 ? 35.547 4.953 13.470 1.00 34.86 ? 416 HIS A ND1 1 ATOM 3217 C CD2 . HIS A 1 416 ? 36.458 3.158 14.420 1.00 35.28 ? 416 HIS A CD2 1 ATOM 3218 C CE1 . HIS A 1 416 ? 36.889 5.016 13.300 1.00 32.50 ? 416 HIS A CE1 1 ATOM 3219 N NE2 . HIS A 1 416 ? 37.463 3.951 13.851 1.00 33.96 ? 416 HIS A NE2 1 ATOM 3220 N N . GLY A 1 417 ? 31.420 2.457 16.297 1.00 63.82 ? 417 GLY A N 1 ATOM 3221 C CA . GLY A 1 417 ? 30.059 1.944 16.531 1.00 65.73 ? 417 GLY A CA 1 ATOM 3222 C C . GLY A 1 417 ? 29.073 2.692 17.432 1.00 62.36 ? 417 GLY A C 1 ATOM 3223 O O . GLY A 1 417 ? 27.993 2.205 17.802 1.00 47.77 ? 417 GLY A O 1 ATOM 3224 N N . GLY A 1 418 ? 29.399 3.887 17.799 1.00 74.78 ? 418 GLY A N 1 ATOM 3225 C CA . GLY A 1 418 ? 28.437 4.595 18.608 1.00 81.11 ? 418 GLY A CA 1 ATOM 3226 C C . GLY A 1 418 ? 28.356 4.210 20.070 1.00 86.28 ? 418 GLY A C 1 ATOM 3227 O O . GLY A 1 418 ? 27.285 3.879 20.546 1.00 95.77 ? 418 GLY A O 1 ATOM 3228 N N . PHE A 1 419 ? 29.511 4.372 20.734 1.00 65.35 ? 419 PHE A N 1 ATOM 3229 C CA . PHE A 1 419 ? 29.755 4.147 22.148 1.00 53.81 ? 419 PHE A CA 1 ATOM 3230 C C . PHE A 1 419 ? 28.874 3.136 22.831 1.00 64.23 ? 419 PHE A C 1 ATOM 3231 O O . PHE A 1 419 ? 28.405 3.339 23.969 1.00 63.34 ? 419 PHE A O 1 ATOM 3232 C CB . PHE A 1 419 ? 29.778 5.486 22.900 1.00 52.24 ? 419 PHE A CB 1 ATOM 3233 C CG . PHE A 1 419 ? 30.651 6.445 22.131 1.00 48.78 ? 419 PHE A CG 1 ATOM 3234 C CD1 . PHE A 1 419 ? 32.038 6.364 22.232 1.00 35.50 ? 419 PHE A CD1 1 ATOM 3235 C CD2 . PHE A 1 419 ? 30.112 7.410 21.277 1.00 46.36 ? 419 PHE A CD2 1 ATOM 3236 C CE1 . PHE A 1 419 ? 32.850 7.238 21.506 1.00 38.01 ? 419 PHE A CE1 1 ATOM 3237 C CE2 . PHE A 1 419 ? 30.911 8.298 20.550 1.00 32.40 ? 419 PHE A CE2 1 ATOM 3238 C CZ . PHE A 1 419 ? 32.293 8.208 20.671 1.00 27.54 ? 419 PHE A CZ 1 ATOM 3239 N N . SER A 1 420 ? 28.679 2.034 22.114 1.00 60.71 ? 420 SER A N 1 ATOM 3240 C CA . SER A 1 420 ? 27.880 0.911 22.582 1.00 51.75 ? 420 SER A CA 1 ATOM 3241 C C . SER A 1 420 ? 28.352 -0.417 21.989 1.00 54.38 ? 420 SER A C 1 ATOM 3242 O O . SER A 1 420 ? 28.896 -0.514 20.882 1.00 43.41 ? 420 SER A O 1 ATOM 3243 C CB . SER A 1 420 ? 26.361 1.101 22.422 1.00 51.63 ? 420 SER A CB 1 ATOM 3244 O OG . SER A 1 420 ? 25.873 0.513 21.192 1.00 81.92 ? 420 SER A OG 1 ATOM 3245 N N . LEU A 1 421 ? 28.122 -1.436 22.794 1.00 60.97 ? 421 LEU A N 1 ATOM 3246 C CA . LEU A 1 421 ? 28.397 -2.808 22.484 1.00 49.92 ? 421 LEU A CA 1 ATOM 3247 C C . LEU A 1 421 ? 27.098 -3.542 22.778 1.00 100.00 ? 421 LEU A C 1 ATOM 3248 O O . LEU A 1 421 ? 26.685 -4.285 21.857 1.00 100.00 ? 421 LEU A O 1 ATOM 3249 C CB . LEU A 1 421 ? 29.558 -3.435 23.276 1.00 49.73 ? 421 LEU A CB 1 ATOM 3250 C CG . LEU A 1 421 ? 30.842 -2.623 23.265 1.00 57.45 ? 421 LEU A CG 1 ATOM 3251 C CD1 . LEU A 1 421 ? 31.885 -3.374 24.083 1.00 59.11 ? 421 LEU A CD1 1 ATOM 3252 C CD2 . LEU A 1 421 ? 31.348 -2.378 21.846 1.00 71.60 ? 421 LEU A CD2 1 ATOM 3253 O OXT . LEU A 1 421 ? 26.444 -3.192 23.827 1.00 48.76 ? 421 LEU A OXT 1 HETATM 3254 C C1 . NDG B 2 . ? 39.295 1.306 9.004 1.00 2.81 ? 871 NDG A C1 1 HETATM 3255 C C2 . NDG B 2 . ? 37.761 1.267 8.696 1.00 100.00 ? 871 NDG A C2 1 HETATM 3256 C C3 . NDG B 2 . ? 37.309 0.136 7.740 1.00 100.00 ? 871 NDG A C3 1 HETATM 3257 C C4 . NDG B 2 . ? 38.283 0.062 6.569 1.00 100.00 ? 871 NDG A C4 1 HETATM 3258 C C5 . NDG B 2 . ? 39.720 -0.214 7.014 1.00 100.00 ? 871 NDG A C5 1 HETATM 3259 C C6 . NDG B 2 . ? 40.712 -0.103 5.842 1.00 100.00 ? 871 NDG A C6 1 HETATM 3260 C C7 . NDG B 2 . ? 35.916 0.755 10.364 1.00 2.35 ? 871 NDG A C7 1 HETATM 3261 C C8 . NDG B 2 . ? 35.636 0.841 11.847 1.00 95.20 ? 871 NDG A C8 1 HETATM 3262 O O . NDG B 2 . ? 40.193 0.681 8.053 1.00 100.00 ? 871 NDG A O 1 HETATM 3263 O O3 . NDG B 2 . ? 35.985 0.404 7.231 1.00 100.00 ? 871 NDG A O3 1 HETATM 3264 O O4 . NDG B 2 . ? 37.900 -0.985 5.661 1.00 33.63 ? 871 NDG A O4 1 HETATM 3265 O O6 . NDG B 2 . ? 41.369 0.544 4.733 1.00 46.51 ? 871 NDG A O6 1 HETATM 3266 O O7 . NDG B 2 . ? 35.209 -0.028 9.718 1.00 100.00 ? 871 NDG A O7 1 HETATM 3267 N N2 . NDG B 2 . ? 36.850 1.596 9.835 1.00 30.82 ? 871 NDG A N2 1 HETATM 3268 C C1 . NDG C 2 . ? 36.259 21.734 22.346 1.00 100.00 ? 1681 NDG A C1 1 HETATM 3269 C C2 . NDG C 2 . ? 34.973 22.579 22.588 1.00 100.00 ? 1681 NDG A C2 1 HETATM 3270 C C3 . NDG C 2 . ? 35.009 23.860 21.693 1.00 100.00 ? 1681 NDG A C3 1 HETATM 3271 C C4 . NDG C 2 . ? 36.453 24.396 21.568 1.00 100.00 ? 1681 NDG A C4 1 HETATM 3272 C C5 . NDG C 2 . ? 37.449 23.355 21.028 1.00 29.30 ? 1681 NDG A C5 1 HETATM 3273 C C6 . NDG C 2 . ? 38.772 23.419 21.809 1.00 100.00 ? 1681 NDG A C6 1 HETATM 3274 C C7 . NDG C 2 . ? 32.554 21.785 23.100 1.00 100.00 ? 1681 NDG A C7 1 HETATM 3275 C C8 . NDG C 2 . ? 31.512 22.818 22.665 1.00 18.27 ? 1681 NDG A C8 1 HETATM 3276 O O . NDG C 2 . ? 36.900 22.032 21.084 1.00 69.01 ? 1681 NDG A O 1 HETATM 3277 O O3 . NDG C 2 . ? 34.141 24.877 22.243 1.00 100.00 ? 1681 NDG A O3 1 HETATM 3278 O O4 . NDG C 2 . ? 36.542 25.567 20.729 1.00 69.10 ? 1681 NDG A O4 1 HETATM 3279 O O6 . NDG C 2 . ? 39.337 24.479 22.607 1.00 100.00 ? 1681 NDG A O6 1 HETATM 3280 O O7 . NDG C 2 . ? 32.113 20.898 23.864 1.00 98.49 ? 1681 NDG A O7 1 HETATM 3281 N N2 . NDG C 2 . ? 33.749 21.730 22.413 1.00 100.00 ? 1681 NDG A N2 1 HETATM 3282 C C1 . NDG D 2 . ? 24.720 -16.975 25.093 1.00 100.00 ? 3681 NDG A C1 1 HETATM 3283 C C2 . NDG D 2 . ? 25.275 -18.361 24.731 1.00 17.90 ? 3681 NDG A C2 1 HETATM 3284 C C3 . NDG D 2 . ? 24.167 -19.437 24.737 1.00 100.00 ? 3681 NDG A C3 1 HETATM 3285 C C4 . NDG D 2 . ? 22.873 -19.002 25.446 1.00 31.24 ? 3681 NDG A C4 1 HETATM 3286 C C5 . NDG D 2 . ? 22.424 -17.549 25.158 1.00 99.90 ? 3681 NDG A C5 1 HETATM 3287 C C6 . NDG D 2 . ? 22.055 -16.742 26.392 1.00 42.83 ? 3681 NDG A C6 1 HETATM 3288 C C7 . NDG D 2 . ? 26.749 -19.204 22.987 1.00 23.68 ? 3681 NDG A C7 1 HETATM 3289 C C8 . NDG D 2 . ? 27.648 -19.754 24.058 1.00 100.00 ? 3681 NDG A C8 1 HETATM 3290 O O . NDG D 2 . ? 23.440 -16.795 24.507 1.00 100.00 ? 3681 NDG A O 1 HETATM 3291 O O3 . NDG D 2 . ? 24.695 -20.624 25.355 1.00 58.59 ? 3681 NDG A O3 1 HETATM 3292 O O4 . NDG D 2 . ? 21.814 -19.860 24.995 1.00 81.25 ? 3681 NDG A O4 1 HETATM 3293 O O6 . NDG D 2 . ? 20.732 -16.673 26.927 1.00 88.95 ? 3681 NDG A O6 1 HETATM 3294 O O7 . NDG D 2 . ? 26.753 -19.594 21.808 1.00 85.06 ? 3681 NDG A O7 1 HETATM 3295 N N2 . NDG D 2 . ? 25.917 -18.270 23.425 1.00 100.00 ? 3681 NDG A N2 1 HETATM 3296 O O . HOH E 3 . ? 24.971 -16.913 21.022 1.00 36.64 ? 450 HOH A O 1 HETATM 3297 O O . HOH E 3 . ? 40.390 -11.937 61.123 1.00 41.60 ? 451 HOH A O 1 HETATM 3298 O O . HOH E 3 . ? 39.627 -10.252 58.828 1.00 33.17 ? 452 HOH A O 1 HETATM 3299 O O . HOH E 3 . ? 35.701 0.431 59.122 1.00 39.32 ? 453 HOH A O 1 HETATM 3300 O O . HOH E 3 . ? 25.152 0.380 38.202 1.00 38.06 ? 454 HOH A O 1 HETATM 3301 O O . HOH E 3 . ? 47.312 10.249 51.670 1.00 50.60 ? 455 HOH A O 1 HETATM 3302 O O . HOH E 3 . ? 38.800 -20.106 40.693 1.00 37.45 ? 456 HOH A O 1 HETATM 3303 O O . HOH E 3 . ? 38.337 -12.153 48.066 1.00 5.47 ? 457 HOH A O 1 HETATM 3304 O O . HOH E 3 . ? 43.401 -5.617 30.847 1.00 1.19 ? 458 HOH A O 1 HETATM 3305 O O . HOH E 3 . ? 41.587 0.970 15.684 1.00 20.94 ? 459 HOH A O 1 HETATM 3306 O O . HOH E 3 . ? 24.598 -5.446 23.846 1.00 43.96 ? 460 HOH A O 1 HETATM 3307 O O . HOH E 3 . ? 43.355 11.079 13.818 1.00 23.29 ? 461 HOH A O 1 HETATM 3308 O O . HOH E 3 . ? 44.359 -5.662 19.562 1.00 34.48 ? 462 HOH A O 1 HETATM 3309 O O . HOH E 3 . ? 59.804 3.277 33.998 1.00 45.51 ? 463 HOH A O 1 HETATM 3310 O O . HOH E 3 . ? 40.934 3.951 43.645 1.00 10.00 ? 464 HOH A O 1 HETATM 3311 O O . HOH E 3 . ? 48.617 2.862 49.146 1.00 19.31 ? 465 HOH A O 1 HETATM 3312 O O . HOH E 3 . ? 28.440 -14.729 15.608 1.00 52.79 ? 466 HOH A O 1 HETATM 3313 O O . HOH E 3 . ? 38.606 -2.507 34.105 1.00 50.23 ? 467 HOH A O 1 HETATM 3314 O O . HOH E 3 . ? 39.295 -25.152 46.252 1.00 31.09 ? 468 HOH A O 1 HETATM 3315 O O . HOH E 3 . ? 27.823 -7.498 32.782 1.00 25.61 ? 469 HOH A O 1 HETATM 3316 O O . HOH E 3 . ? 47.146 11.893 55.142 1.00 33.04 ? 470 HOH A O 1 HETATM 3317 O O . HOH E 3 . ? 38.366 -7.276 40.082 1.00 19.69 ? 471 HOH A O 1 HETATM 3318 O O . HOH E 3 . ? 54.903 -1.594 31.704 1.00 33.31 ? 472 HOH A O 1 HETATM 3319 O O . HOH E 3 . ? 58.541 20.463 22.476 1.00 43.74 ? 473 HOH A O 1 HETATM 3320 O O . HOH E 3 . ? 26.832 -15.796 27.673 1.00 62.91 ? 474 HOH A O 1 HETATM 3321 O O . HOH E 3 . ? 21.449 -18.302 21.685 1.00 28.78 ? 475 HOH A O 1 HETATM 3322 O O . HOH E 3 . ? 51.904 12.107 35.609 1.00 47.63 ? 476 HOH A O 1 HETATM 3323 O O . HOH E 3 . ? 27.757 -4.739 34.900 1.00 8.00 ? 477 HOH A O 1 HETATM 3324 O O . HOH E 3 . ? 22.906 -5.672 28.081 1.00 23.50 ? 478 HOH A O 1 HETATM 3325 O O . HOH E 3 . ? 52.667 20.272 13.881 1.00 13.75 ? 479 HOH A O 1 HETATM 3326 O O . HOH E 3 . ? 35.523 -18.162 57.288 1.00 31.61 ? 480 HOH A O 1 HETATM 3327 O O . HOH E 3 . ? 51.762 -6.305 42.367 1.00 53.49 ? 481 HOH A O 1 HETATM 3328 O O . HOH E 3 . ? 55.915 -11.038 34.382 1.00 33.41 ? 482 HOH A O 1 HETATM 3329 O O . HOH E 3 . ? 52.813 -16.327 41.473 1.00 40.00 ? 483 HOH A O 1 HETATM 3330 O O . HOH E 3 . ? 56.581 -14.399 26.788 1.00 42.79 ? 484 HOH A O 1 HETATM 3331 O O . HOH E 3 . ? 37.608 -4.541 59.522 1.00 38.28 ? 485 HOH A O 1 HETATM 3332 O O . HOH E 3 . ? 47.265 -10.451 30.351 1.00 54.79 ? 486 HOH A O 1 HETATM 3333 O O . HOH E 3 . ? 43.819 -3.873 28.325 1.00 35.51 ? 487 HOH A O 1 # _database_PDB_caveat.id 1 _database_PDB_caveat.text 'Chirality error in several residues' # 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 LYS 1 1 1 LYS LYS A . n A 1 2 ILE 2 2 2 ILE ILE A . n A 1 3 LYS 3 3 3 LYS LYS A . n A 1 4 ASP 4 4 4 ASP ASP A . n A 1 5 PRO 5 5 5 PRO PRO A . n A 1 6 LYS 6 6 6 LYS LYS A . n A 1 7 ILE 7 7 7 ILE ILE A . n A 1 8 LEU 8 8 8 LEU LEU A . n A 1 9 GLY 9 9 9 GLY GLY A . n A 1 10 ILE 10 10 10 ILE ILE A . n A 1 11 ASP 11 11 11 ASP ASP A . n A 1 12 PRO 12 12 12 PRO PRO A . n A 1 13 ASN 13 13 13 ASN ASN A . n A 1 14 VAL 14 14 14 VAL VAL A . n A 1 15 THR 15 15 15 THR THR A . n A 1 16 GLN 16 16 16 GLN GLN A . n A 1 17 TYR 17 17 17 TYR TYR A . n A 1 18 THR 18 18 18 THR THR A . n A 1 19 GLY 19 19 19 GLY GLY A . n A 1 20 TYR 20 20 20 TYR TYR A . n A 1 21 LEU 21 21 21 LEU LEU A . n A 1 22 ASP 22 22 22 ASP ASP A . n A 1 23 VAL 23 23 23 VAL VAL A . n A 1 24 GLU 24 24 24 GLU GLU A . n A 1 25 ASP 25 25 25 ASP ASP A . n A 1 26 GLU 26 26 26 GLU GLU A . n A 1 27 ASP 27 27 27 ASP ASP A . n A 1 28 LYS 28 28 28 LYS LYS A . n A 1 29 HIS 29 29 29 HIS HIS A . n A 1 30 PHE 30 30 30 PHE PHE A . n A 1 31 PHE 31 31 31 PHE PHE A . n A 1 32 PHE 32 32 32 PHE PHE A . n A 1 33 TRP 33 33 33 TRP TRP A . n A 1 34 THR 34 34 34 THR THR A . n A 1 35 PHE 35 35 35 PHE PHE A . n A 1 36 GLU 36 36 36 GLU GLU A . n A 1 37 SER 37 37 37 SER SER A . n A 1 38 ARG 38 38 38 ARG ARG A . n A 1 39 ASN 39 39 39 ASN ASN A . n A 1 40 ASP 40 40 40 ASP ASP A . n A 1 41 PRO 41 41 41 PRO PRO A . n A 1 42 ALA 42 42 42 ALA ALA A . n A 1 43 LYS 43 43 43 LYS LYS A . n A 1 44 ASP 44 44 44 ASP ASP A . n A 1 45 PRO 45 45 45 PRO PRO A . n A 1 46 VAL 46 46 46 VAL VAL A . n A 1 47 ILE 47 47 47 ILE ILE A . n A 1 48 LEU 48 48 48 LEU LEU A . n A 1 49 TRP 49 49 49 TRP TRP A . n A 1 50 LEU 50 50 50 LEU LEU A . n A 1 51 ASN 51 51 51 ASN ASN A . n A 1 52 GLY 52 52 52 GLY GLY A . n A 1 53 GLY 53 53 53 GLY GLY A . n A 1 54 PRO 54 54 54 PRO PRO A . n A 1 55 GLY 55 55 55 GLY GLY A . n A 1 56 CYS 56 56 56 CYS CYS A . n A 1 57 SER 57 57 57 SER SER A . n A 1 58 SER 58 58 58 SER SER A . n A 1 59 LEU 59 59 59 LEU LEU A . n A 1 60 THR 60 60 60 THR THR A . n A 1 61 GLY 61 61 61 GLY GLY A . n A 1 62 LEU 62 62 62 LEU LEU A . n A 1 63 PHE 63 63 63 PHE PHE A . n A 1 64 PHE 64 64 64 PHE PHE A . n A 1 65 GLU 65 65 65 GLU GLU A . n A 1 66 LEU 66 66 66 LEU LEU A . n A 1 67 GLY 67 67 67 GLY GLY A . n A 1 68 PRO 68 68 68 PRO PRO A . n A 1 69 SER 69 69 69 SER SER A . n A 1 70 SER 70 70 70 SER SER A . n A 1 71 ILE 71 71 71 ILE ILE A . n A 1 72 GLY 72 72 72 GLY GLY A . n A 1 73 PRO 73 73 73 PRO PRO A . n A 1 74 ASP 74 74 74 ASP ASP A . n A 1 75 LEU 75 75 75 LEU LEU A . n A 1 76 LYS 76 76 76 LYS LYS A . n A 1 77 PRO 77 77 77 PRO PRO A . n A 1 78 ILE 78 78 78 ILE ILE A . n A 1 79 GLY 79 79 79 GLY GLY A . n A 1 80 ASN 80 80 80 ASN ASN A . n A 1 81 PRO 81 81 81 PRO PRO A . n A 1 82 TYR 82 82 82 TYR TYR A . n A 1 83 SER 83 83 83 SER SER A . n A 1 84 TRP 84 84 84 TRP TRP A . n A 1 85 ASN 85 85 85 ASN ASN A . n A 1 86 SER 86 86 86 SER SER A . n A 1 87 ASN 87 87 87 ASN ASN A . n A 1 88 ALA 88 88 88 ALA ALA A . n A 1 89 THR 89 89 89 THR THR A . n A 1 90 VAL 90 90 90 VAL VAL A . n A 1 91 ILE 91 91 91 ILE ILE A . n A 1 92 PHE 92 92 92 PHE PHE A . n A 1 93 LEU 93 93 93 LEU LEU A . n A 1 94 ASP 94 94 94 ASP ASP A . n A 1 95 GLN 95 95 95 GLN GLN A . n A 1 96 PRO 96 96 96 PRO PRO A . n A 1 97 VAL 97 97 97 VAL VAL A . n A 1 98 ASN 98 98 98 ASN ASN A . n A 1 99 VAL 99 99 99 VAL VAL A . n A 1 100 GLY 100 100 100 GLY GLY A . n A 1 101 PHE 101 101 101 PHE PHE A . n A 1 102 SER 102 102 102 SER SER A . n A 1 103 TYR 103 103 103 TYR TYR A . n A 1 104 SER 104 104 104 SER SER A . n A 1 105 GLY 105 105 105 GLY GLY A . n A 1 106 SER 106 106 106 SER SER A . n A 1 107 SER 107 107 107 SER SER A . n A 1 108 GLY 108 108 108 GLY GLY A . n A 1 109 VAL 109 109 109 VAL VAL A . n A 1 110 SER 110 110 110 SER SER A . n A 1 111 ASN 111 111 111 ASN ASN A . n A 1 112 THR 112 112 112 THR THR A . n A 1 113 VAL 113 113 113 VAL VAL A . n A 1 114 ALA 114 114 114 ALA ALA A . n A 1 115 ALA 115 115 115 ALA ALA A . n A 1 116 GLY 116 116 116 GLY GLY A . n A 1 117 LYS 117 117 117 LYS LYS A . n A 1 118 ASP 118 118 118 ASP ASP A . n A 1 119 VAL 119 119 119 VAL VAL A . n A 1 120 TYR 120 120 120 TYR TYR A . n A 1 121 ASN 121 121 121 ASN ASN A . n A 1 122 PHE 122 122 122 PHE PHE A . n A 1 123 LEU 123 123 123 LEU LEU A . n A 1 124 GLU 124 124 124 GLU GLU A . n A 1 125 LEU 125 125 125 LEU LEU A . n A 1 126 PHE 126 126 126 PHE PHE A . n A 1 127 PHE 127 127 127 PHE PHE A . n A 1 128 ASP 128 128 128 ASP ASP A . n A 1 129 GLN 129 129 129 GLN GLN A . n A 1 130 PHE 130 130 130 PHE PHE A . n A 1 131 PRO 131 131 131 PRO PRO A . n A 1 132 GLU 132 132 132 GLU GLU A . n A 1 133 TYR 133 133 133 TYR TYR A . n A 1 134 VAL 134 134 134 VAL VAL A . n A 1 135 ASN 135 135 135 ASN ASN A . n A 1 136 LYS 136 136 136 LYS LYS A . n A 1 137 GLY 137 137 137 GLY GLY A . n A 1 138 GLN 138 138 138 GLN GLN A . n A 1 139 ASP 139 139 139 ASP ASP A . n A 1 140 PHE 140 140 140 PHE PHE A . n A 1 141 HIS 141 141 141 HIS HIS A . n A 1 142 ILE 142 142 142 ILE ILE A . n A 1 143 ALA 143 143 143 ALA ALA A . n A 1 144 GLY 144 144 144 GLY GLY A . n A 1 145 GLU 145 145 145 GLU GLU A . n A 1 146 SER 146 146 146 SER SER A . n A 1 147 TYR 147 147 147 TYR TYR A . n A 1 148 ALA 148 148 148 ALA ALA A . n A 1 149 GLY 149 149 149 GLY GLY A . n A 1 150 HIS 150 150 150 HIS HIS A . n A 1 151 TYR 151 151 151 TYR TYR A . n A 1 152 ILE 152 152 152 ILE ILE A . n A 1 153 PRO 153 153 153 PRO PRO A . n A 1 154 VAL 154 154 154 VAL VAL A . n A 1 155 PHE 155 155 155 PHE PHE A . n A 1 156 ALA 156 156 156 ALA ALA A . n A 1 157 SER 157 157 157 SER SER A . n A 1 158 GLU 158 158 158 GLU GLU A . n A 1 159 ILE 159 159 159 ILE ILE A . n A 1 160 LEU 160 160 160 LEU LEU A . n A 1 161 SER 161 161 161 SER SER A . n A 1 162 HIS 162 162 162 HIS HIS A . n A 1 163 LYS 163 163 163 LYS LYS A . n A 1 164 ASP 164 164 164 ASP ASP A . n A 1 165 ARG 165 165 165 ARG ARG A . n A 1 166 ASN 166 166 166 ASN ASN A . n A 1 167 PHE 167 167 167 PHE PHE A . n A 1 168 ASN 168 168 168 ASN ASN A . n A 1 169 LEU 169 169 169 LEU LEU A . n A 1 170 THR 170 170 170 THR THR A . n A 1 171 SER 171 171 171 SER SER A . n A 1 172 VAL 172 172 172 VAL VAL A . n A 1 173 LEU 173 173 173 LEU LEU A . n A 1 174 ILE 174 174 174 ILE ILE A . n A 1 175 GLY 175 175 175 GLY GLY A . n A 1 176 ASN 176 176 176 ASN ASN A . n A 1 177 GLY 177 177 177 GLY GLY A . n A 1 178 LEU 178 178 178 LEU LEU A . n A 1 179 THR 179 179 179 THR THR A . n A 1 180 ASP 180 180 180 ASP ASP A . n A 1 181 PRO 181 181 181 PRO PRO A . n A 1 182 LEU 182 182 182 LEU LEU A . n A 1 183 THR 183 183 183 THR THR A . n A 1 184 GLN 184 184 184 GLN GLN A . n A 1 185 TYR 185 185 185 TYR TYR A . n A 1 186 ASN 186 186 186 ASN ASN A . n A 1 187 TYR 187 187 187 TYR TYR A . n A 1 188 TYR 188 188 188 TYR TYR A . n A 1 189 GLU 189 189 189 GLU GLU A . n A 1 190 PRO 190 190 190 PRO PRO A . n A 1 191 MET 191 191 191 MET MET A . n A 1 192 ALA 192 192 192 ALA ALA A . n A 1 193 CYS 193 193 193 CYS CYS A . n A 1 194 GLY 194 194 194 GLY GLY A . n A 1 195 GLU 195 195 195 GLU GLU A . n A 1 196 GLY 196 196 196 GLY GLY A . n A 1 197 GLY 197 197 197 GLY GLY A . n A 1 198 GLU 198 198 198 GLU GLU A . n A 1 199 PRO 199 199 199 PRO PRO A . n A 1 200 SER 200 200 200 SER SER A . n A 1 201 VAL 201 201 201 VAL VAL A . n A 1 202 LEU 202 202 202 LEU LEU A . n A 1 203 PRO 203 203 203 PRO PRO A . n A 1 204 SER 204 204 204 SER SER A . n A 1 205 GLU 205 205 205 GLU GLU A . n A 1 206 GLU 206 206 206 GLU GLU A . n A 1 207 CYS 207 207 207 CYS CYS A . n A 1 208 SER 208 208 208 SER SER A . n A 1 209 ALA 209 209 209 ALA ALA A . n A 1 210 MET 210 210 210 MET MET A . n A 1 211 GLU 211 211 211 GLU GLU A . n A 1 212 ASP 212 212 212 ASP ASP A . n A 1 213 SER 213 213 213 SER SER A . n A 1 214 LEU 214 214 214 LEU LEU A . n A 1 215 GLU 215 215 215 GLU GLU A . n A 1 216 ARG 216 216 216 ARG ARG A . n A 1 217 CYS 217 217 217 CYS CYS A . n A 1 218 LEU 218 218 218 LEU LEU A . n A 1 219 GLY 219 219 219 GLY GLY A . n A 1 220 LEU 220 220 220 LEU LEU A . n A 1 221 ILE 221 221 221 ILE ILE A . n A 1 222 GLU 222 222 222 GLU GLU A . n A 1 223 SER 223 223 223 SER SER A . n A 1 224 CYS 224 224 224 CYS CYS A . n A 1 225 TYR 225 225 225 TYR TYR A . n A 1 226 ASP 226 226 226 ASP ASP A . n A 1 227 SER 227 227 227 SER SER A . n A 1 228 GLN 228 228 228 GLN GLN A . n A 1 229 SER 229 229 229 SER SER A . n A 1 230 VAL 230 230 230 VAL VAL A . n A 1 231 TRP 231 231 231 TRP TRP A . n A 1 232 SER 232 232 232 SER SER A . n A 1 233 CYS 233 233 233 CYS CYS A . n A 1 234 VAL 234 234 234 VAL VAL A . n A 1 235 PRO 235 235 235 PRO PRO A . n A 1 236 ALA 236 236 236 ALA ALA A . n A 1 237 THR 237 237 237 THR THR A . n A 1 238 ILE 238 238 238 ILE ILE A . n A 1 239 TYR 239 239 239 TYR TYR A . n A 1 240 CYS 240 240 240 CYS CYS A . n A 1 241 ASN 241 241 241 ASN ASN A . n A 1 242 ASN 242 242 242 ASN ASN A . n A 1 243 ALA 243 243 243 ALA ALA A . n A 1 244 GLN 244 244 244 GLN GLN A . n A 1 245 LEU 245 245 245 LEU LEU A . n A 1 246 ALA 246 246 246 ALA ALA A . n A 1 247 PRO 247 247 247 PRO PRO A . n A 1 248 TYR 248 248 248 TYR TYR A . n A 1 249 GLN 249 249 249 GLN GLN A . n A 1 250 ARG 250 250 250 ARG ARG A . n A 1 251 THR 251 251 251 THR THR A . n A 1 252 GLY 252 252 252 GLY GLY A . n A 1 253 ARG 253 253 253 ARG ARG A . n A 1 254 ASN 254 254 254 ASN ASN A . n A 1 255 VAL 255 255 255 VAL VAL A . n A 1 256 TYR 256 256 256 TYR TYR A . n A 1 257 ASP 257 257 257 ASP ASP A . n A 1 258 ILE 258 258 258 ILE ILE A . n A 1 259 ARG 259 259 259 ARG ARG A . n A 1 260 LYS 260 260 260 LYS LYS A . n A 1 261 ASP 261 261 261 ASP ASP A . n A 1 262 CYS 262 262 262 CYS CYS A . n A 1 263 GLU 263 263 263 GLU GLU A . n A 1 264 GLY 264 264 264 GLY GLY A . n A 1 265 GLY 265 265 265 GLY GLY A . n A 1 266 ASN 266 266 266 ASN ASN A . n A 1 267 LEU 267 267 267 LEU LEU A . n A 1 268 CYS 268 268 268 CYS CYS A . n A 1 269 TYR 269 269 269 TYR TYR A . n A 1 270 PRO 270 270 270 PRO PRO A . n A 1 271 THR 271 271 271 THR THR A . n A 1 272 LEU 272 272 272 LEU LEU A . n A 1 273 GLN 273 273 273 GLN GLN A . n A 1 274 ASP 274 274 274 ASP ASP A . n A 1 275 ILE 275 275 275 ILE ILE A . n A 1 276 ASP 276 276 276 ASP ASP A . n A 1 277 ASP 277 277 277 ASP ASP A . n A 1 278 TYR 278 278 278 TYR TYR A . n A 1 279 LEU 279 279 279 LEU LEU A . n A 1 280 ASN 280 280 280 ASN ASN A . n A 1 281 GLN 281 281 281 GLN GLN A . n A 1 282 ASP 282 282 282 ASP ASP A . n A 1 283 TYR 283 283 283 TYR TYR A . n A 1 284 VAL 284 284 284 VAL VAL A . n A 1 285 LYS 285 285 285 LYS LYS A . n A 1 286 GLU 286 286 286 GLU GLU A . n A 1 287 ALA 287 287 287 ALA ALA A . n A 1 288 VAL 288 288 288 VAL VAL A . n A 1 289 GLY 289 289 289 GLY GLY A . n A 1 290 ALA 290 290 290 ALA ALA A . n A 1 291 GLU 291 291 291 GLU GLU A . n A 1 292 VAL 292 292 292 VAL VAL A . n A 1 293 ASP 293 293 293 ASP ASP A . n A 1 294 HIS 294 294 294 HIS HIS A . n A 1 295 TYR 295 295 295 TYR TYR A . n A 1 296 GLU 296 296 296 GLU GLU A . n A 1 297 SER 297 297 297 SER SER A . n A 1 298 CYS 298 298 298 CYS CYS A . n A 1 299 ASN 299 299 299 ASN ASN A . n A 1 300 PHE 300 300 300 PHE PHE A . n A 1 301 ASP 301 301 301 ASP ASP A . n A 1 302 ILE 302 302 302 ILE ILE A . n A 1 303 ASN 303 303 303 ASN ASN A . n A 1 304 ARG 304 304 304 ARG ARG A . n A 1 305 ASN 305 305 305 ASN ASN A . n A 1 306 PHE 306 306 306 PHE PHE A . n A 1 307 LEU 307 307 307 LEU LEU A . n A 1 308 PHE 308 308 308 PHE PHE A . n A 1 309 ALA 309 309 309 ALA ALA A . n A 1 310 GLY 310 310 310 GLY GLY A . n A 1 311 ASP 311 311 311 ASP ASP A . n A 1 312 TRP 312 312 312 TRP TRP A . n A 1 313 MET 313 313 313 MET MET A . n A 1 314 LYS 314 314 314 LYS LYS A . n A 1 315 PRO 315 315 315 PRO PRO A . n A 1 316 TYR 316 316 316 TYR TYR A . n A 1 317 HIS 317 317 317 HIS HIS A . n A 1 318 THR 318 318 318 THR THR A . n A 1 319 ALA 319 319 319 ALA ALA A . n A 1 320 VAL 320 320 320 VAL VAL A . n A 1 321 THR 321 321 321 THR THR A . n A 1 322 ASP 322 322 322 ASP ASP A . n A 1 323 LEU 323 323 323 LEU LEU A . n A 1 324 LEU 324 324 324 LEU LEU A . n A 1 325 ASN 325 325 325 ASN ASN A . n A 1 326 GLN 326 326 326 GLN GLN A . n A 1 327 ASP 327 327 327 ASP ASP A . n A 1 328 LEU 328 328 328 LEU LEU A . n A 1 329 PRO 329 329 329 PRO PRO A . n A 1 330 ILE 330 330 330 ILE ILE A . n A 1 331 LEU 331 331 331 LEU LEU A . n A 1 332 VAL 332 332 332 VAL VAL A . n A 1 333 TYR 333 333 333 TYR TYR A . n A 1 334 ALA 334 334 334 ALA ALA A . n A 1 335 GLY 335 335 335 GLY GLY A . n A 1 336 ASP 336 336 336 ASP ASP A . n A 1 337 LYS 337 337 337 LYS LYS A . n A 1 338 ASP 338 338 338 ASP ASP A . n A 1 339 PHE 339 339 339 PHE PHE A . n A 1 340 ILE 340 340 340 ILE ILE A . n A 1 341 CYS 341 341 341 CYS CYS A . n A 1 342 ASN 342 342 342 ASN ASN A . n A 1 343 TRP 343 343 343 TRP TRP A . n A 1 344 LEU 344 344 344 LEU LEU A . n A 1 345 GLY 345 345 345 GLY GLY A . n A 1 346 ASN 346 346 346 ASN ASN A . n A 1 347 LYS 347 347 347 LYS LYS A . n A 1 348 ALA 348 348 348 ALA ALA A . n A 1 349 TRP 349 349 349 TRP TRP A . n A 1 350 THR 350 350 350 THR THR A . n A 1 351 ASP 351 351 351 ASP ASP A . n A 1 352 VAL 352 352 352 VAL VAL A . n A 1 353 LEU 353 353 353 LEU LEU A . n A 1 354 PRO 354 354 354 PRO PRO A . n A 1 355 TRP 355 355 355 TRP TRP A . n A 1 356 LYS 356 356 356 LYS LYS A . n A 1 357 TYR 357 357 357 TYR TYR A . n A 1 358 ASP 358 358 358 ASP ASP A . n A 1 359 GLU 359 359 359 GLU GLU A . n A 1 360 GLU 360 360 360 GLU GLU A . n A 1 361 PHE 361 361 361 PHE PHE A . n A 1 362 ALA 362 362 362 ALA ALA A . n A 1 363 SER 363 363 363 SER SER A . n A 1 364 GLN 364 364 364 GLN GLN A . n A 1 365 LYS 365 365 365 LYS LYS A . n A 1 366 VAL 366 366 366 VAL VAL A . n A 1 367 ARG 367 367 367 ARG ARG A . n A 1 368 ASN 368 368 368 ASN ASN A . n A 1 369 TRP 369 369 369 TRP TRP A . n A 1 370 THR 370 370 370 THR THR A . n A 1 371 ALA 371 371 371 ALA ALA A . n A 1 372 SER 372 372 372 SER SER A . n A 1 373 ILE 373 373 373 ILE ILE A . n A 1 374 THR 374 374 374 THR THR A . n A 1 375 ASP 375 375 375 ASP ASP A . n A 1 376 GLU 376 376 376 GLU GLU A . n A 1 377 VAL 377 377 377 VAL VAL A . n A 1 378 ALA 378 378 378 ALA ALA A . n A 1 379 GLY 379 379 379 GLY GLY A . n A 1 380 GLU 380 380 380 GLU GLU A . n A 1 381 VAL 381 381 381 VAL VAL A . n A 1 382 LYS 382 382 382 LYS LYS A . n A 1 383 SER 383 383 383 SER SER A . n A 1 384 TYR 384 384 384 TYR TYR A . n A 1 385 LYS 385 385 385 LYS LYS A . n A 1 386 HIS 386 386 386 HIS HIS A . n A 1 387 PHE 387 387 387 PHE PHE A . n A 1 388 THR 388 388 388 THR THR A . n A 1 389 TYR 389 389 389 TYR TYR A . n A 1 390 LEU 390 390 390 LEU LEU A . n A 1 391 ARG 391 391 391 ARG ARG A . n A 1 392 VAL 392 392 392 VAL VAL A . n A 1 393 PHE 393 393 393 PHE PHE A . n A 1 394 ASN 394 394 394 ASN ASN A . n A 1 395 GLY 395 395 395 GLY GLY A . n A 1 396 GLY 396 396 396 GLY GLY A . n A 1 397 HIS 397 397 397 HIS HIS A . n A 1 398 MET 398 398 398 MET MET A . n A 1 399 VAL 399 399 399 VAL VAL A . n A 1 400 PRO 400 400 400 PRO PRO A . n A 1 401 PHE 401 401 401 PHE PHE A . n A 1 402 ASP 402 402 402 ASP ASP A . n A 1 403 VAL 403 403 403 VAL VAL A . n A 1 404 PRO 404 404 404 PRO PRO A . n A 1 405 GLU 405 405 405 GLU GLU A . n A 1 406 ASN 406 406 406 ASN ASN A . n A 1 407 ALA 407 407 407 ALA ALA A . n A 1 408 LEU 408 408 408 LEU LEU A . n A 1 409 SER 409 409 409 SER SER A . n A 1 410 MET 410 410 410 MET MET A . n A 1 411 VAL 411 411 411 VAL VAL A . n A 1 412 ASN 412 412 412 ASN ASN A . n A 1 413 GLU 413 413 413 GLU GLU A . n A 1 414 TRP 414 414 414 TRP TRP A . n A 1 415 ILE 415 415 415 ILE ILE A . n A 1 416 HIS 416 416 416 HIS HIS A . n A 1 417 GLY 417 417 417 GLY GLY A . n A 1 418 GLY 418 418 418 GLY GLY A . n A 1 419 PHE 419 419 419 PHE PHE A . n A 1 420 SER 420 420 420 SER SER A . n A 1 421 LEU 421 421 421 LEU LEU A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NDG 1 871 871 NDG NAG A . C 2 NDG 1 1681 1681 NDG NAG A . D 2 NDG 1 3681 3681 NDG NAG A . E 3 HOH 1 450 450 HOH HOH A . E 3 HOH 2 451 451 HOH HOH A . E 3 HOH 3 452 452 HOH HOH A . E 3 HOH 4 453 453 HOH HOH A . E 3 HOH 5 454 454 HOH HOH A . E 3 HOH 6 455 455 HOH HOH A . E 3 HOH 7 456 456 HOH HOH A . E 3 HOH 8 457 457 HOH HOH A . E 3 HOH 9 458 458 HOH HOH A . E 3 HOH 10 459 459 HOH HOH A . E 3 HOH 11 460 460 HOH HOH A . E 3 HOH 12 461 461 HOH HOH A . E 3 HOH 13 462 462 HOH HOH A . E 3 HOH 14 463 463 HOH HOH A . E 3 HOH 15 464 464 HOH HOH A . E 3 HOH 16 465 465 HOH HOH A . E 3 HOH 17 466 466 HOH HOH A . E 3 HOH 18 467 467 HOH HOH A . E 3 HOH 19 468 468 HOH HOH A . E 3 HOH 20 469 469 HOH HOH A . E 3 HOH 21 470 470 HOH HOH A . E 3 HOH 22 471 471 HOH HOH A . E 3 HOH 23 472 472 HOH HOH A . E 3 HOH 24 473 473 HOH HOH A . E 3 HOH 25 474 474 HOH HOH A . E 3 HOH 26 475 475 HOH HOH A . E 3 HOH 27 476 476 HOH HOH A . E 3 HOH 28 477 477 HOH HOH A . E 3 HOH 29 478 478 HOH HOH A . E 3 HOH 30 479 479 HOH HOH A . E 3 HOH 31 480 480 HOH HOH A . E 3 HOH 32 481 481 HOH HOH A . E 3 HOH 33 482 482 HOH HOH A . E 3 HOH 34 483 483 HOH HOH A . E 3 HOH 35 484 484 HOH HOH A . E 3 HOH 36 485 485 HOH HOH A . E 3 HOH 37 486 486 HOH HOH A . E 3 HOH 38 487 487 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 87 A ASN 87 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 168 A ASN 168 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 368 A ASN 368 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 1994-06-22 2 'Structure model' 1 1 2008-03-03 3 'Structure model' 1 2 2011-07-13 4 'Structure model' 1 3 2017-11-29 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Version format compliance' 3 4 'Structure model' 'Derived calculations' 4 4 'Structure model' Other # loop_ _pdbx_audit_revision_category.ordinal _pdbx_audit_revision_category.revision_ordinal _pdbx_audit_revision_category.data_content_type _pdbx_audit_revision_category.category 1 4 'Structure model' pdbx_database_status 2 4 'Structure model' struct_conf 3 4 'Structure model' struct_conf_type # _pdbx_audit_revision_item.ordinal 1 _pdbx_audit_revision_item.revision_ordinal 4 _pdbx_audit_revision_item.data_content_type 'Structure model' _pdbx_audit_revision_item.item '_pdbx_database_status.process_site' # _software.name TNT _software.classification refinement _software.version . _software.citation_id ? _software.pdbx_ordinal 1 # _pdbx_database_remark.id 700 _pdbx_database_remark.text ;SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. STRANDS 1, 2, 3, 5, 6, 7, 8, 9, 10 AND 11 OF S1A AND S1B ARE IDENTICAL. ; # _pdbx_validate_close_contact.id 1 _pdbx_validate_close_contact.PDB_model_num 1 _pdbx_validate_close_contact.auth_atom_id_1 CG _pdbx_validate_close_contact.auth_asym_id_1 A _pdbx_validate_close_contact.auth_comp_id_1 ASN _pdbx_validate_close_contact.auth_seq_id_1 87 _pdbx_validate_close_contact.PDB_ins_code_1 ? _pdbx_validate_close_contact.label_alt_id_1 ? _pdbx_validate_close_contact.auth_atom_id_2 C1 _pdbx_validate_close_contact.auth_asym_id_2 A _pdbx_validate_close_contact.auth_comp_id_2 NDG _pdbx_validate_close_contact.auth_seq_id_2 871 _pdbx_validate_close_contact.PDB_ins_code_2 ? _pdbx_validate_close_contact.label_alt_id_2 ? _pdbx_validate_close_contact.dist 2.09 # loop_ _pdbx_validate_rmsd_bond.id _pdbx_validate_rmsd_bond.PDB_model_num _pdbx_validate_rmsd_bond.auth_atom_id_1 _pdbx_validate_rmsd_bond.auth_asym_id_1 _pdbx_validate_rmsd_bond.auth_comp_id_1 _pdbx_validate_rmsd_bond.auth_seq_id_1 _pdbx_validate_rmsd_bond.PDB_ins_code_1 _pdbx_validate_rmsd_bond.label_alt_id_1 _pdbx_validate_rmsd_bond.auth_atom_id_2 _pdbx_validate_rmsd_bond.auth_asym_id_2 _pdbx_validate_rmsd_bond.auth_comp_id_2 _pdbx_validate_rmsd_bond.auth_seq_id_2 _pdbx_validate_rmsd_bond.PDB_ins_code_2 _pdbx_validate_rmsd_bond.label_alt_id_2 _pdbx_validate_rmsd_bond.bond_value _pdbx_validate_rmsd_bond.bond_target_value _pdbx_validate_rmsd_bond.bond_deviation _pdbx_validate_rmsd_bond.bond_standard_deviation _pdbx_validate_rmsd_bond.linker_flag 1 1 CD A GLU 65 ? ? OE2 A GLU 65 ? ? 1.355 1.252 0.103 0.011 N 2 1 CD A GLU 189 ? ? OE2 A GLU 189 ? ? 1.346 1.252 0.094 0.011 N 3 1 CD A GLU 198 ? ? OE2 A GLU 198 ? ? 1.322 1.252 0.070 0.011 N 4 1 CD A GLU 205 ? ? OE1 A GLU 205 ? ? 1.336 1.252 0.084 0.011 N 5 1 CD A GLU 211 ? ? OE1 A GLU 211 ? ? 1.321 1.252 0.069 0.011 N 6 1 CD A GLU 215 ? ? OE2 A GLU 215 ? ? 1.327 1.252 0.075 0.011 N 7 1 CD A GLU 222 ? ? OE1 A GLU 222 ? ? 1.326 1.252 0.074 0.011 N 8 1 CD A GLU 286 ? ? OE1 A GLU 286 ? ? 1.325 1.252 0.073 0.011 N 9 1 CD A GLU 360 ? ? OE1 A GLU 360 ? ? 1.322 1.252 0.070 0.011 N 10 1 CD A GLU 376 ? ? OE1 A GLU 376 ? ? 1.325 1.252 0.073 0.011 N 11 1 CD A GLU 380 ? ? OE1 A GLU 380 ? ? 1.328 1.252 0.076 0.011 N 12 1 CD A GLU 405 ? ? OE2 A GLU 405 ? ? 1.322 1.252 0.070 0.011 N 13 1 CD A GLU 413 ? ? OE1 A GLU 413 ? ? 1.320 1.252 0.068 0.011 N # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 CB A ASP 11 ? ? CG A ASP 11 ? ? OD2 A ASP 11 ? ? 123.84 118.30 5.54 0.90 N 2 1 CB A ASP 25 ? ? CG A ASP 25 ? ? OD1 A ASP 25 ? ? 123.70 118.30 5.40 0.90 N 3 1 CB A ASP 25 ? ? CG A ASP 25 ? ? OD2 A ASP 25 ? ? 111.31 118.30 -6.99 0.90 N 4 1 CB A ASP 27 ? ? CG A ASP 27 ? ? OD2 A ASP 27 ? ? 124.03 118.30 5.73 0.90 N 5 1 CB A ASP 40 ? ? CG A ASP 40 ? ? OD2 A ASP 40 ? ? 111.54 118.30 -6.76 0.90 N 6 1 C A GLY 67 ? ? N A PRO 68 ? ? CD A PRO 68 ? ? 113.23 128.40 -15.17 2.10 Y 7 1 CB A ASP 74 ? ? CG A ASP 74 ? ? OD1 A ASP 74 ? ? 124.65 118.30 6.35 0.90 N 8 1 CB A ASP 74 ? ? CG A ASP 74 ? ? OD2 A ASP 74 ? ? 110.84 118.30 -7.46 0.90 N 9 1 N A SER 83 ? ? CA A SER 83 ? ? CB A SER 83 ? ? 120.16 110.50 9.66 1.50 N 10 1 CB A ASP 94 ? ? CG A ASP 94 ? ? OD2 A ASP 94 ? ? 112.00 118.30 -6.30 0.90 N 11 1 CB A ASP 118 ? ? CG A ASP 118 ? ? OD2 A ASP 118 ? ? 112.38 118.30 -5.92 0.90 N 12 1 CB A ALA 143 ? ? CA A ALA 143 ? ? C A ALA 143 ? ? 120.04 110.10 9.94 1.50 N 13 1 N A PRO 153 ? ? CA A PRO 153 ? ? CB A PRO 153 ? ? 110.54 103.30 7.24 1.20 N 14 1 CB A ASP 164 ? ? CG A ASP 164 ? ? OD1 A ASP 164 ? ? 124.36 118.30 6.06 0.90 N 15 1 CB A ASP 164 ? ? CG A ASP 164 ? ? OD2 A ASP 164 ? ? 111.97 118.30 -6.33 0.90 N 16 1 CB A ASP 180 ? ? CG A ASP 180 ? ? OD1 A ASP 180 ? ? 112.50 118.30 -5.80 0.90 N 17 1 CB A TYR 188 ? ? CG A TYR 188 ? ? CD1 A TYR 188 ? ? 116.46 121.00 -4.54 0.60 N 18 1 CB A ASP 212 ? ? CG A ASP 212 ? ? OD1 A ASP 212 ? ? 123.82 118.30 5.52 0.90 N 19 1 CB A ASP 212 ? ? CG A ASP 212 ? ? OD2 A ASP 212 ? ? 112.24 118.30 -6.06 0.90 N 20 1 NE A ARG 253 ? ? CZ A ARG 253 ? ? NH2 A ARG 253 ? ? 117.20 120.30 -3.10 0.50 N 21 1 CB A ASP 257 ? ? CG A ASP 257 ? ? OD1 A ASP 257 ? ? 111.37 118.30 -6.93 0.90 N 22 1 CB A ASP 261 ? ? CG A ASP 261 ? ? OD2 A ASP 261 ? ? 112.18 118.30 -6.12 0.90 N 23 1 CB A ASP 274 ? ? CG A ASP 274 ? ? OD2 A ASP 274 ? ? 112.21 118.30 -6.09 0.90 N 24 1 CB A ASP 293 ? ? CG A ASP 293 ? ? OD1 A ASP 293 ? ? 125.15 118.30 6.85 0.90 N 25 1 CB A ASP 293 ? ? CG A ASP 293 ? ? OD2 A ASP 293 ? ? 110.95 118.30 -7.35 0.90 N 26 1 CB A ASP 301 ? ? CG A ASP 301 ? ? OD2 A ASP 301 ? ? 111.69 118.30 -6.61 0.90 N 27 1 CB A ASP 311 ? ? CG A ASP 311 ? ? OD2 A ASP 311 ? ? 112.15 118.30 -6.15 0.90 N 28 1 N A TRP 312 ? ? CA A TRP 312 ? ? CB A TRP 312 ? ? 98.76 110.60 -11.84 1.80 N 29 1 CB A ASP 322 ? ? CG A ASP 322 ? ? OD1 A ASP 322 ? ? 125.89 118.30 7.59 0.90 N 30 1 CB A ASP 322 ? ? CG A ASP 322 ? ? OD2 A ASP 322 ? ? 111.25 118.30 -7.05 0.90 N 31 1 CB A ASN 325 ? ? CA A ASN 325 ? ? C A ASN 325 ? ? 122.45 110.40 12.05 2.00 N 32 1 CB A ASP 327 ? ? CG A ASP 327 ? ? OD1 A ASP 327 ? ? 124.77 118.30 6.47 0.90 N 33 1 CB A ASP 327 ? ? CG A ASP 327 ? ? OD2 A ASP 327 ? ? 112.76 118.30 -5.54 0.90 N 34 1 CB A ASP 336 ? ? CG A ASP 336 ? ? OD1 A ASP 336 ? ? 112.37 118.30 -5.93 0.90 N 35 1 CB A ASP 336 ? ? CG A ASP 336 ? ? OD2 A ASP 336 ? ? 124.92 118.30 6.62 0.90 N 36 1 CB A ASP 338 ? ? CG A ASP 338 ? ? OD2 A ASP 338 ? ? 112.08 118.30 -6.22 0.90 N 37 1 CB A ASP 351 ? ? CG A ASP 351 ? ? OD2 A ASP 351 ? ? 110.40 118.30 -7.90 0.90 N 38 1 C A LEU 353 ? ? N A PRO 354 ? ? CD A PRO 354 ? ? 108.44 128.40 -19.96 2.10 Y 39 1 NE A ARG 367 ? ? CZ A ARG 367 ? ? NH1 A ARG 367 ? ? 124.13 120.30 3.83 0.50 N 40 1 CB A ASP 375 ? ? CG A ASP 375 ? ? OD2 A ASP 375 ? ? 112.26 118.30 -6.04 0.90 N 41 1 N A TYR 384 ? ? CA A TYR 384 ? ? CB A TYR 384 ? ? 121.99 110.60 11.39 1.80 N 42 1 NE A ARG 391 ? ? CZ A ARG 391 ? ? NH1 A ARG 391 ? ? 124.08 120.30 3.78 0.50 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ILE A 10 ? ? 25.10 -127.64 2 1 PRO A 12 ? ? -58.99 -115.76 3 1 ASN A 13 ? ? 2.36 -81.32 4 1 THR A 15 ? ? 123.99 91.29 5 1 GLU A 24 ? ? -33.00 -88.84 6 1 ASN A 39 ? ? -108.18 -108.94 7 1 ASP A 44 ? ? -34.91 132.19 8 1 PRO A 45 ? ? -57.19 -176.20 9 1 LEU A 62 ? ? -52.91 -74.15 10 1 PHE A 64 ? ? -149.07 -20.30 11 1 GLU A 65 ? ? -135.58 -35.33 12 1 LEU A 66 ? ? -150.73 9.99 13 1 TYR A 82 ? ? -154.86 34.31 14 1 SER A 83 ? ? -48.21 160.45 15 1 ALA A 88 ? ? 176.96 137.19 16 1 PHE A 92 ? ? -111.19 71.38 17 1 ASP A 94 ? ? -111.52 79.50 18 1 PRO A 96 ? ? -79.68 -163.47 19 1 ASN A 98 ? ? 93.64 8.13 20 1 SER A 107 ? ? -126.77 -130.36 21 1 GLU A 132 ? ? -69.43 15.07 22 1 VAL A 134 ? ? -109.46 -76.23 23 1 ASN A 135 ? ? -17.26 -50.67 24 1 ASP A 139 ? ? -37.12 114.75 25 1 SER A 146 ? ? 62.09 -107.04 26 1 HIS A 150 ? ? -102.41 -61.18 27 1 ARG A 165 ? ? -30.86 142.03 28 1 THR A 179 ? ? -126.75 -51.00 29 1 SER A 200 ? ? -34.34 122.87 30 1 SER A 213 ? ? -58.27 -3.44 31 1 ASP A 257 ? ? -178.23 97.68 32 1 ASN A 266 ? ? -69.13 -172.30 33 1 GLN A 281 ? ? -41.92 153.62 34 1 ASP A 311 ? ? -23.03 -81.89 35 1 TRP A 312 ? ? -33.94 -32.72 36 1 GLN A 326 ? ? -86.33 33.14 37 1 CYS A 341 ? ? -142.37 57.68 38 1 ASN A 342 ? ? -40.71 160.56 39 1 ASP A 351 ? ? -58.47 -5.71 40 1 ILE A 373 ? ? -72.49 -79.91 41 1 THR A 374 ? ? -59.68 -2.45 42 1 TYR A 384 ? ? -167.87 110.68 43 1 LYS A 385 ? ? 48.02 -132.76 44 1 ASN A 394 ? ? 52.74 74.50 45 1 VAL A 403 ? ? -113.67 77.64 46 1 VAL A 411 ? ? -63.10 -77.24 47 1 HIS A 416 ? ? -97.64 -69.94 48 1 PHE A 419 ? ? 27.11 43.04 # loop_ _pdbx_validate_chiral.id _pdbx_validate_chiral.PDB_model_num _pdbx_validate_chiral.auth_atom_id _pdbx_validate_chiral.label_alt_id _pdbx_validate_chiral.auth_asym_id _pdbx_validate_chiral.auth_comp_id _pdbx_validate_chiral.auth_seq_id _pdbx_validate_chiral.PDB_ins_code _pdbx_validate_chiral.details _pdbx_validate_chiral.omega 1 1 CA ? A ILE 71 ? PLANAR . 2 1 CB ? A ILE 275 ? 'WRONG HAND' . 3 1 CB ? A ILE 302 ? 'WRONG HAND' . 4 1 CB ? A ILE 415 ? 'WRONG HAND' . # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A LYS 1 ? CG ? A LYS 1 CG 2 1 Y 1 A LYS 1 ? CD ? A LYS 1 CD 3 1 Y 1 A LYS 1 ? CE ? A LYS 1 CE 4 1 Y 1 A LYS 1 ? NZ ? A LYS 1 NZ 5 1 Y 1 A ILE 2 ? CG1 ? A ILE 2 CG1 6 1 Y 1 A ILE 2 ? CG2 ? A ILE 2 CG2 7 1 Y 1 A ILE 2 ? CD1 ? A ILE 2 CD1 8 1 Y 1 A LYS 3 ? CG ? A LYS 3 CG 9 1 Y 1 A LYS 3 ? CD ? A LYS 3 CD 10 1 Y 1 A LYS 3 ? CE ? A LYS 3 CE 11 1 Y 1 A LYS 3 ? NZ ? A LYS 3 NZ 12 1 Y 1 A ASP 4 ? CG ? A ASP 4 CG 13 1 Y 1 A ASP 4 ? OD1 ? A ASP 4 OD1 14 1 Y 1 A ASP 4 ? OD2 ? A ASP 4 OD2 15 1 Y 1 A LYS 6 ? CG ? A LYS 6 CG 16 1 Y 1 A LYS 6 ? CD ? A LYS 6 CD 17 1 Y 1 A LYS 6 ? CE ? A LYS 6 CE 18 1 Y 1 A LYS 6 ? NZ ? A LYS 6 NZ 19 1 Y 1 A ILE 7 ? CG1 ? A ILE 7 CG1 20 1 Y 1 A ILE 7 ? CG2 ? A ILE 7 CG2 21 1 Y 1 A ILE 7 ? CD1 ? A ILE 7 CD1 22 1 Y 1 A ASN 13 ? CG ? A ASN 13 CG 23 1 Y 1 A ASN 13 ? OD1 ? A ASN 13 OD1 24 1 Y 1 A ASN 13 ? ND2 ? A ASN 13 ND2 25 1 Y 1 A VAL 14 ? CG1 ? A VAL 14 CG1 26 1 Y 1 A VAL 14 ? CG2 ? A VAL 14 CG2 27 1 Y 1 A THR 15 ? OG1 ? A THR 15 OG1 28 1 Y 1 A THR 15 ? CG2 ? A THR 15 CG2 29 1 Y 1 A GLN 16 ? CG ? A GLN 16 CG 30 1 Y 1 A GLN 16 ? CD ? A GLN 16 CD 31 1 Y 1 A GLN 16 ? OE1 ? A GLN 16 OE1 32 1 Y 1 A GLN 16 ? NE2 ? A GLN 16 NE2 33 1 Y 1 A TYR 17 ? CG ? A TYR 17 CG 34 1 Y 1 A TYR 17 ? CD1 ? A TYR 17 CD1 35 1 Y 1 A TYR 17 ? CD2 ? A TYR 17 CD2 36 1 Y 1 A TYR 17 ? CE1 ? A TYR 17 CE1 37 1 Y 1 A TYR 17 ? CE2 ? A TYR 17 CE2 38 1 Y 1 A TYR 17 ? CZ ? A TYR 17 CZ 39 1 Y 1 A TYR 17 ? OH ? A TYR 17 OH 40 1 Y 1 A GLU 24 ? CG ? A GLU 24 CG 41 1 Y 1 A GLU 24 ? CD ? A GLU 24 CD 42 1 Y 1 A GLU 24 ? OE1 ? A GLU 24 OE1 43 1 Y 1 A GLU 24 ? OE2 ? A GLU 24 OE2 44 1 Y 1 A GLU 26 ? CG ? A GLU 26 CG 45 1 Y 1 A GLU 26 ? CD ? A GLU 26 CD 46 1 Y 1 A GLU 26 ? OE1 ? A GLU 26 OE1 47 1 Y 1 A GLU 26 ? OE2 ? A GLU 26 OE2 48 1 Y 1 A PHE 35 ? CG ? A PHE 35 CG 49 1 Y 1 A PHE 35 ? CD1 ? A PHE 35 CD1 50 1 Y 1 A PHE 35 ? CD2 ? A PHE 35 CD2 51 1 Y 1 A PHE 35 ? CE1 ? A PHE 35 CE1 52 1 Y 1 A PHE 35 ? CE2 ? A PHE 35 CE2 53 1 Y 1 A PHE 35 ? CZ ? A PHE 35 CZ 54 1 Y 1 A LYS 43 ? CG ? A LYS 43 CG 55 1 Y 1 A LYS 43 ? CD ? A LYS 43 CD 56 1 Y 1 A LYS 43 ? CE ? A LYS 43 CE 57 1 Y 1 A LYS 43 ? NZ ? A LYS 43 NZ 58 1 Y 1 A SER 69 ? OG ? A SER 69 OG 59 1 Y 1 A SER 86 ? OG ? A SER 86 OG 60 1 Y 1 A VAL 90 ? CG1 ? A VAL 90 CG1 61 1 Y 1 A VAL 90 ? CG2 ? A VAL 90 CG2 62 1 Y 1 A SER 204 ? OG ? A SER 204 OG 63 1 Y 1 A SER 213 ? OG ? A SER 213 OG 64 1 Y 1 A SER 232 ? OG ? A SER 232 OG 65 1 Y 1 A ILE 275 ? CD1 ? A ILE 275 CD1 66 1 Y 1 A GLN 281 ? CG ? A GLN 281 CG 67 1 Y 1 A GLN 281 ? CD ? A GLN 281 CD 68 1 Y 1 A GLN 281 ? OE1 ? A GLN 281 OE1 69 1 Y 1 A GLN 281 ? NE2 ? A GLN 281 NE2 70 1 Y 1 A VAL 284 ? CG1 ? A VAL 284 CG1 71 1 Y 1 A VAL 284 ? CG2 ? A VAL 284 CG2 72 1 Y 1 A GLU 291 ? CG ? A GLU 291 CG 73 1 Y 1 A GLU 291 ? CD ? A GLU 291 CD 74 1 Y 1 A GLU 291 ? OE1 ? A GLU 291 OE1 75 1 Y 1 A GLU 291 ? OE2 ? A GLU 291 OE2 76 1 Y 1 A ILE 302 ? CD1 ? A ILE 302 CD1 77 1 Y 1 A GLU 359 ? CG ? A GLU 359 CG 78 1 Y 1 A GLU 359 ? CD ? A GLU 359 CD 79 1 Y 1 A GLU 359 ? OE1 ? A GLU 359 OE1 80 1 Y 1 A GLU 359 ? OE2 ? A GLU 359 OE2 81 1 Y 1 A GLN 364 ? CG ? A GLN 364 CG 82 1 Y 1 A GLN 364 ? CD ? A GLN 364 CD 83 1 Y 1 A GLN 364 ? OE1 ? A GLN 364 OE1 84 1 Y 1 A GLN 364 ? NE2 ? A GLN 364 NE2 85 1 Y 1 A LYS 365 ? CG ? A LYS 365 CG 86 1 Y 1 A LYS 365 ? CD ? A LYS 365 CD 87 1 Y 1 A LYS 365 ? CE ? A LYS 365 CE 88 1 Y 1 A LYS 365 ? NZ ? A LYS 365 NZ 89 1 Y 1 A SER 372 ? OG ? A SER 372 OG 90 1 Y 1 A ILE 415 ? CD1 ? A ILE 415 CD1 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' NDG 3 water HOH #