data_4CQU # _entry.id 4CQU # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4CQU PDBE EBI-59788 WWPDB D_1290059788 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 4CQP unspecified 'CRYSTAL STRUCTURE OF H5 (VN1194) SER227ASN/GLN196ARG MUTANT HAEMAGGLUTININ' PDB 4CQQ unspecified ;H5 (VN1194) SER227ASN/GLN196ARG MUTANT HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'SLN ; PDB 4CQR unspecified ;H5 (VN1194) SER227ASN/GLN196ARG MUTANT HAEMAGGLUTININ IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6'SLN ; PDB 4CQS unspecified ;H5 (VN1194) ASN186LYS MUTANT HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'SLN ; PDB 4CQT unspecified ;H5 (VN1194) ASN186LYS MUTANT HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'SLN ; PDB 4CQV unspecified 'CRYSTAL STRUCTURE OF H5 (TYTY) DEL133/ILE155THR MUTANT HAEMAGGLUTININ' PDB 4CQW unspecified ;H5 (TYTY) DEL133/ILE155THR MUTANT HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'SLN ; PDB 4CQX unspecified ;H5 (TYTY) DEL133/ILE155THR MUTANT HAEMAGGLUTININ IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6'SLN ; PDB 4CQY unspecified 'H5 (TYTY) DEL133/ILE155THR MUTANT HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE LSTA' PDB 4CQZ unspecified 'CRYSTAL STRUCTURE OF H5 (VN1194) GLN196ARG MUTANT HAEMAGGLUTININ' PDB 4CR0 unspecified 'CRYSTAL STRUCTURE OF H5 (VN1194) ASN186LYS/GLY143ARG MUTANT HAEMAGGLUTININ' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4CQU _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2014-02-21 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Xiong, X.' 1 'Xiao, H.' 2 'Martin, S.R.' 3 'Coombs, P.J.' 4 'Liu, J.' 5 'Collins, P.J.' 6 'Vachieri, S.G.' 7 'Walker, P.A.' 8 'Lin, Y.P.' 9 'McCauley, J.W.' 10 'Gamblin, S.J.' 11 'Skehel, J.J.' 12 # _citation.id primary _citation.title 'Enhanced Human Receptor Binding by H5 Haemagglutinins.' _citation.journal_abbrev Virology _citation.journal_volume 456 _citation.page_first 179 _citation.page_last ? _citation.year 2014 _citation.journal_id_ASTM VIRLAX _citation.country US _citation.journal_id_ISSN 0042-6822 _citation.journal_id_CSD 0922 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 24889237 _citation.pdbx_database_id_DOI 10.1016/J.VIROL.2014.03.008 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Xiong, X.' 1 primary 'Xiao, H.' 2 primary 'Martin, S.R.' 3 primary 'Coombs, P.J.' 4 primary 'Liu, J.' 5 primary 'Collins, P.J.' 6 primary 'Vachieri, S.G.' 7 primary 'Walker, P.A.' 8 primary 'Lin, Y.P.' 9 primary 'Mccauley, J.W.' 10 primary 'Gamblin, S.J.' 11 primary 'Skehel, J.J.' 12 # _cell.entry_id 4CQU _cell.length_a 101.464 _cell.length_b 101.464 _cell.length_c 452.187 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 18 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4CQU _symmetry.space_group_name_H-M 'H 3 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 155 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer nat 'HAEMAGGLUTININ HA1' 36965.844 1 ? YES 'HA1 OF TRYPSIN RELEASED ECTODOMAIN, RESIDUES 17-342' ? 2 polymer nat 'HAEMAGGLUTININ HA2' 19097.990 1 ? ? 'HA2 OF TRYPSIN RELEASED ECTODOMAIN, RESIDUES 347-512' ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 8 ? ? ? ? 4 non-polymer man ALPHA-D-MANNOSE 180.156 2 ? ? ? ? 5 non-polymer man BETA-D-MANNOSE 180.156 2 ? ? ? ? 6 non-polymer man 'O-SIALIC ACID' 309.270 1 ? ? ? ? 7 non-polymer man BETA-D-GALACTOSE 180.156 1 ? ? ? ? 8 non-polymer syn '3[N-MORPHOLINO]PROPANE SULFONIC ACID' 209.263 1 ? ? ? ? 9 water nat water 18.015 102 ? ? ? ? # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 'polypeptide(L)' no no ;DQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYIV EKANPVNDLCYPGDFNDYEELKHLLSRINHFEKIQIIPKSSWSSHEASLGVSSACPYQGKSSFFRNVVWLIKKNSTYPTI KRSYNNTNQEDLLVLWGIHHPKDAAEQTKLYQNPTTYISVGTSTLNQRLVPRIATRSKVNGQSGRMEFFWTILKPNDAIN FESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGLRNS PQRETR ; ;DQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYIV EKANPVNDLCYPGDFNDYEELKHLLSRINHFEKIQIIPKSSWSSHEASLGVSSACPYQGKSSFFRNVVWLIKKNSTYPTI KRSYNNTNQEDLLVLWGIHHPKDAAEQTKLYQNPTTYISVGTSTLNQRLVPRIATRSKVNGQSGRMEFFWTILKPNDAIN FESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGLRNS PQRETR ; A ? 2 'polypeptide(L)' no no ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP QYSEEA ; ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP QYSEEA ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ASP n 1 2 GLN n 1 3 ILE n 1 4 CYS n 1 5 ILE n 1 6 GLY n 1 7 TYR n 1 8 HIS n 1 9 ALA n 1 10 ASN n 1 11 ASN n 1 12 SER n 1 13 THR n 1 14 GLU n 1 15 GLN n 1 16 VAL n 1 17 ASP n 1 18 THR n 1 19 ILE n 1 20 MET n 1 21 GLU n 1 22 LYS n 1 23 ASN n 1 24 VAL n 1 25 THR n 1 26 VAL n 1 27 THR n 1 28 HIS n 1 29 ALA n 1 30 GLN n 1 31 ASP n 1 32 ILE n 1 33 LEU n 1 34 GLU n 1 35 LYS n 1 36 THR n 1 37 HIS n 1 38 ASN n 1 39 GLY n 1 40 LYS n 1 41 LEU n 1 42 CYS n 1 43 ASP n 1 44 LEU n 1 45 ASP n 1 46 GLY n 1 47 VAL n 1 48 LYS n 1 49 PRO n 1 50 LEU n 1 51 ILE n 1 52 LEU n 1 53 ARG n 1 54 ASP n 1 55 CYS n 1 56 SER n 1 57 VAL n 1 58 ALA n 1 59 GLY n 1 60 TRP n 1 61 LEU n 1 62 LEU n 1 63 GLY n 1 64 ASN n 1 65 PRO n 1 66 MET n 1 67 CYS n 1 68 ASP n 1 69 GLU n 1 70 PHE n 1 71 ILE n 1 72 ASN n 1 73 VAL n 1 74 PRO n 1 75 GLU n 1 76 TRP n 1 77 SER n 1 78 TYR n 1 79 ILE n 1 80 VAL n 1 81 GLU n 1 82 LYS n 1 83 ALA n 1 84 ASN n 1 85 PRO n 1 86 VAL n 1 87 ASN n 1 88 ASP n 1 89 LEU n 1 90 CYS n 1 91 TYR n 1 92 PRO n 1 93 GLY n 1 94 ASP n 1 95 PHE n 1 96 ASN n 1 97 ASP n 1 98 TYR n 1 99 GLU n 1 100 GLU n 1 101 LEU n 1 102 LYS n 1 103 HIS n 1 104 LEU n 1 105 LEU n 1 106 SER n 1 107 ARG n 1 108 ILE n 1 109 ASN n 1 110 HIS n 1 111 PHE n 1 112 GLU n 1 113 LYS n 1 114 ILE n 1 115 GLN n 1 116 ILE n 1 117 ILE n 1 118 PRO n 1 119 LYS n 1 120 SER n 1 121 SER n 1 122 TRP n 1 123 SER n 1 124 SER n 1 125 HIS n 1 126 GLU n 1 127 ALA n 1 128 SER n 1 129 LEU n 1 130 GLY n 1 131 VAL n 1 132 SER n 1 133 SER n 1 134 ALA n 1 135 CYS n 1 136 PRO n 1 137 TYR n 1 138 GLN n 1 139 GLY n 1 140 LYS n 1 141 SER n 1 142 SER n 1 143 PHE n 1 144 PHE n 1 145 ARG n 1 146 ASN n 1 147 VAL n 1 148 VAL n 1 149 TRP n 1 150 LEU n 1 151 ILE n 1 152 LYS n 1 153 LYS n 1 154 ASN n 1 155 SER n 1 156 THR n 1 157 TYR n 1 158 PRO n 1 159 THR n 1 160 ILE n 1 161 LYS n 1 162 ARG n 1 163 SER n 1 164 TYR n 1 165 ASN n 1 166 ASN n 1 167 THR n 1 168 ASN n 1 169 GLN n 1 170 GLU n 1 171 ASP n 1 172 LEU n 1 173 LEU n 1 174 VAL n 1 175 LEU n 1 176 TRP n 1 177 GLY n 1 178 ILE n 1 179 HIS n 1 180 HIS n 1 181 PRO n 1 182 LYS n 1 183 ASP n 1 184 ALA n 1 185 ALA n 1 186 GLU n 1 187 GLN n 1 188 THR n 1 189 LYS n 1 190 LEU n 1 191 TYR n 1 192 GLN n 1 193 ASN n 1 194 PRO n 1 195 THR n 1 196 THR n 1 197 TYR n 1 198 ILE n 1 199 SER n 1 200 VAL n 1 201 GLY n 1 202 THR n 1 203 SER n 1 204 THR n 1 205 LEU n 1 206 ASN n 1 207 GLN n 1 208 ARG n 1 209 LEU n 1 210 VAL n 1 211 PRO n 1 212 ARG n 1 213 ILE n 1 214 ALA n 1 215 THR n 1 216 ARG n 1 217 SER n 1 218 LYS n 1 219 VAL n 1 220 ASN n 1 221 GLY n 1 222 GLN n 1 223 SER n 1 224 GLY n 1 225 ARG n 1 226 MET n 1 227 GLU n 1 228 PHE n 1 229 PHE n 1 230 TRP n 1 231 THR n 1 232 ILE n 1 233 LEU n 1 234 LYS n 1 235 PRO n 1 236 ASN n 1 237 ASP n 1 238 ALA n 1 239 ILE n 1 240 ASN n 1 241 PHE n 1 242 GLU n 1 243 SER n 1 244 ASN n 1 245 GLY n 1 246 ASN n 1 247 PHE n 1 248 ILE n 1 249 ALA n 1 250 PRO n 1 251 GLU n 1 252 TYR n 1 253 ALA n 1 254 TYR n 1 255 LYS n 1 256 ILE n 1 257 VAL n 1 258 LYS n 1 259 LYS n 1 260 GLY n 1 261 ASP n 1 262 SER n 1 263 THR n 1 264 ILE n 1 265 MET n 1 266 LYS n 1 267 SER n 1 268 GLU n 1 269 LEU n 1 270 GLU n 1 271 TYR n 1 272 GLY n 1 273 ASN n 1 274 CYS n 1 275 ASN n 1 276 THR n 1 277 LYS n 1 278 CYS n 1 279 GLN n 1 280 THR n 1 281 PRO n 1 282 MET n 1 283 GLY n 1 284 ALA n 1 285 ILE n 1 286 ASN n 1 287 SER n 1 288 SER n 1 289 MET n 1 290 PRO n 1 291 PHE n 1 292 HIS n 1 293 ASN n 1 294 ILE n 1 295 HIS n 1 296 PRO n 1 297 LEU n 1 298 THR n 1 299 ILE n 1 300 GLY n 1 301 GLU n 1 302 CYS n 1 303 PRO n 1 304 LYS n 1 305 TYR n 1 306 VAL n 1 307 LYS n 1 308 SER n 1 309 ASN n 1 310 ARG n 1 311 LEU n 1 312 VAL n 1 313 LEU n 1 314 ALA n 1 315 THR n 1 316 GLY n 1 317 LEU n 1 318 ARG n 1 319 ASN n 1 320 SER n 1 321 PRO n 1 322 GLN n 1 323 ARG n 1 324 GLU n 1 325 THR n 1 326 ARG n 2 1 GLY n 2 2 LEU n 2 3 PHE n 2 4 GLY n 2 5 ALA n 2 6 ILE n 2 7 ALA n 2 8 GLY n 2 9 PHE n 2 10 ILE n 2 11 GLU n 2 12 GLY n 2 13 GLY n 2 14 TRP n 2 15 GLN n 2 16 GLY n 2 17 MET n 2 18 VAL n 2 19 ASP n 2 20 GLY n 2 21 TRP n 2 22 TYR n 2 23 GLY n 2 24 TYR n 2 25 HIS n 2 26 HIS n 2 27 SER n 2 28 ASN n 2 29 GLU n 2 30 GLN n 2 31 GLY n 2 32 SER n 2 33 GLY n 2 34 TYR n 2 35 ALA n 2 36 ALA n 2 37 ASP n 2 38 LYS n 2 39 GLU n 2 40 SER n 2 41 THR n 2 42 GLN n 2 43 LYS n 2 44 ALA n 2 45 ILE n 2 46 ASP n 2 47 GLY n 2 48 VAL n 2 49 THR n 2 50 ASN n 2 51 LYS n 2 52 VAL n 2 53 ASN n 2 54 SER n 2 55 ILE n 2 56 ILE n 2 57 ASP n 2 58 LYS n 2 59 MET n 2 60 ASN n 2 61 THR n 2 62 GLN n 2 63 PHE n 2 64 GLU n 2 65 ALA n 2 66 VAL n 2 67 GLY n 2 68 ARG n 2 69 GLU n 2 70 PHE n 2 71 ASN n 2 72 ASN n 2 73 LEU n 2 74 GLU n 2 75 ARG n 2 76 ARG n 2 77 ILE n 2 78 GLU n 2 79 ASN n 2 80 LEU n 2 81 ASN n 2 82 LYS n 2 83 LYS n 2 84 MET n 2 85 GLU n 2 86 ASP n 2 87 GLY n 2 88 PHE n 2 89 LEU n 2 90 ASP n 2 91 VAL n 2 92 TRP n 2 93 THR n 2 94 TYR n 2 95 ASN n 2 96 ALA n 2 97 GLU n 2 98 LEU n 2 99 LEU n 2 100 VAL n 2 101 LEU n 2 102 MET n 2 103 GLU n 2 104 ASN n 2 105 GLU n 2 106 ARG n 2 107 THR n 2 108 LEU n 2 109 ASP n 2 110 PHE n 2 111 HIS n 2 112 ASP n 2 113 SER n 2 114 ASN n 2 115 VAL n 2 116 LYS n 2 117 ASN n 2 118 LEU n 2 119 TYR n 2 120 ASP n 2 121 LYS n 2 122 VAL n 2 123 ARG n 2 124 LEU n 2 125 GLN n 2 126 LEU n 2 127 ARG n 2 128 ASP n 2 129 ASN n 2 130 ALA n 2 131 LYS n 2 132 GLU n 2 133 LEU n 2 134 GLY n 2 135 ASN n 2 136 GLY n 2 137 CYS n 2 138 PHE n 2 139 GLU n 2 140 PHE n 2 141 TYR n 2 142 HIS n 2 143 LYS n 2 144 CYS n 2 145 ASP n 2 146 ASN n 2 147 GLU n 2 148 CYS n 2 149 MET n 2 150 GLU n 2 151 SER n 2 152 VAL n 2 153 ARG n 2 154 ASN n 2 155 GLY n 2 156 THR n 2 157 TYR n 2 158 ASP n 2 159 TYR n 2 160 PRO n 2 161 GLN n 2 162 TYR n 2 163 SER n 2 164 GLU n 2 165 GLU n 2 166 ALA n # loop_ _entity_src_nat.entity_id _entity_src_nat.pdbx_src_id _entity_src_nat.pdbx_alt_source_flag _entity_src_nat.pdbx_beg_seq_num _entity_src_nat.pdbx_end_seq_num _entity_src_nat.common_name _entity_src_nat.pdbx_organism_scientific _entity_src_nat.pdbx_ncbi_taxonomy_id _entity_src_nat.genus _entity_src_nat.species _entity_src_nat.strain _entity_src_nat.tissue _entity_src_nat.tissue_fraction _entity_src_nat.pdbx_secretion _entity_src_nat.pdbx_fragment _entity_src_nat.pdbx_variant _entity_src_nat.pdbx_cell_line _entity_src_nat.pdbx_atcc _entity_src_nat.pdbx_cellular_location _entity_src_nat.pdbx_organ _entity_src_nat.pdbx_organelle _entity_src_nat.pdbx_cell _entity_src_nat.pdbx_plasmid_name _entity_src_nat.pdbx_plasmid_details _entity_src_nat.details 1 1 sample ? ? ? 'INFLUENZA A VIRUS (A/VIETNAM/1194/2004(H5N1))' 644788 ? ? ? ? ? ? ? 'ASN186LYS MUTANT' ? ? ? ? ? ? ? ? ? 2 1 sample ? ? ? 'INFLUENZA A VIRUS (A/VIETNAM/1194/2004(H5N1))' 644788 ? ? ? ? ? ? ? 'ASN186LYS MUTANT' ? ? ? ? ? ? ? ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_accession _struct_ref.pdbx_db_isoform 1 UNP Q6DQ34_9INFA 1 ? ? Q6DQ34 ? 2 UNP Q6DQ34_9INFA 2 ? ? Q6DQ34 ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 4CQU A 1 ? 326 ? Q6DQ34 17 ? 342 ? 1 326 2 2 4CQU B 1 ? 166 ? Q6DQ34 347 ? 512 ? 1 166 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 4CQU LYS A 182 ? UNP Q6DQ34 ASN 198 'engineered mutation' 182 1 1 4CQU THR A 325 ? UNP Q6DQ34 ARG 341 conflict 325 2 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GAL D-saccharide . BETA-D-GALACTOSE ? 'C6 H12 O6' 180.156 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 MPO non-polymer . '3[N-MORPHOLINO]PROPANE SULFONIC ACID' ? 'C7 H15 N O4 S' 209.263 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 SIA non-polymer . 'O-SIALIC ACID' ? 'C11 H19 N O9' 309.270 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 4CQU _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.74 _exptl_crystal.density_percent_sol 67 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '0.1 M HEPES/MOPS PH 7.0, 0.05 M MGCL2, 28-30% PEG 550 MME, SEEDED WITH CRUSHED WILD-TYPE VN1194 HA CRYSTALS.' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC CCD' _diffrn_detector.pdbx_collection_date ? _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.92 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'DIAMOND BEAMLINE I04-1' _diffrn_source.pdbx_synchrotron_site Diamond _diffrn_source.pdbx_synchrotron_beamline I04-1 _diffrn_source.pdbx_wavelength 0.92 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4CQU _reflns.observed_criterion_sigma_I 2.8 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 35.70 _reflns.d_resolution_high 2.48 _reflns.number_obs 32430 _reflns.number_all ? _reflns.percent_possible_obs 100.0 _reflns.pdbx_Rmerge_I_obs 0.07 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 2.80 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 9.4 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.48 _reflns_shell.d_res_low 2.61 _reflns_shell.percent_possible_all 100.0 _reflns_shell.Rmerge_I_obs 0.68 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.80 _reflns_shell.pdbx_redundancy 9.3 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4CQU _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 30783 _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 150.73 _refine.ls_d_res_high 2.48 _refine.ls_percent_reflns_obs 99.89 _refine.ls_R_factor_obs 0.20602 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.20416 _refine.ls_R_factor_R_free 0.24127 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 1645 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.955 _refine.correlation_coeff_Fo_to_Fc_free 0.938 _refine.B_iso_mean 85.126 _refine.aniso_B[1][1] 2.66 _refine.aniso_B[2][2] 2.66 _refine.aniso_B[3][3] -8.63 _refine.aniso_B[1][2] 1.33 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. WITH TLS ADDED' _refine.pdbx_starting_model 'PDB ENTRY 4BGW' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.280 _refine.pdbx_overall_ESU_R_Free 0.224 _refine.overall_SU_ML 0.186 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 16.986 _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 3860 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 201 _refine_hist.number_atoms_solvent 102 _refine_hist.number_atoms_total 4163 _refine_hist.d_res_high 2.48 _refine_hist.d_res_low 150.73 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.005 0.019 ? 4173 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 3811 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.030 1.995 ? 5675 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.669 3.003 ? 8756 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.525 5.000 ? 483 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 36.135 25.150 ? 200 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 14.583 15.000 ? 681 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 16.811 15.000 ? 17 'X-RAY DIFFRACTION' ? r_chiral_restr 0.055 0.200 ? 638 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.003 0.020 ? 4620 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 944 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 1.428 4.661 ? 1932 'X-RAY DIFFRACTION' ? r_mcbond_other 1.426 4.661 ? 1931 'X-RAY DIFFRACTION' ? r_mcangle_it 2.363 6.990 ? 2412 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 2.526 5.615 ? 2240 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 2.480 _refine_ls_shell.d_res_low 2.544 _refine_ls_shell.number_reflns_R_work 2252 _refine_ls_shell.R_factor_R_work 0.324 _refine_ls_shell.percent_reflns_obs 99.92 _refine_ls_shell.R_factor_R_free 0.386 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 105 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 4CQU _struct.title ;H5 (VN1194) Asn186Lys Mutant Haemagglutinin in Complex with Human Receptor Analogue 6'SLN ; _struct.pdbx_descriptor 'HAEMAGGLUTININ HA1, HAEMAGGLUTININ HA2' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4CQU _struct_keywords.pdbx_keywords 'VIRAL PROTEIN' _struct_keywords.text ;VIRAL PROTEIN, SIALIC ACID, GLYCOPROTEIN, VIRUS RECEPTOR, AVIAN FLU, SIALYLLACTOSAMINE, 3SLN, 3'SLN, 6SLN, 6'SLN, LSTA ; # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 3 ? F N N 3 ? G N N 3 ? H N N 4 ? I N N 5 ? J N N 4 ? K N N 3 ? L N N 6 ? M N N 7 ? N N N 3 ? O N N 3 ? P N N 5 ? Q N N 8 ? R N N 9 ? S N N 9 ? # _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 1 SER A 56 ? GLY A 63 ? SER A 56 GLY A 63 1 ? 8 HELX_P HELX_P2 2 ASN A 64 ? ILE A 71 ? ASN A 64 ILE A 71 5 ? 8 HELX_P HELX_P3 3 ASP A 97 ? SER A 106 ? ASP A 97 SER A 106 1 ? 10 HELX_P HELX_P4 4 ASP A 183 ? GLN A 192 ? ASP A 183 GLN A 192 1 ? 10 HELX_P HELX_P5 5 ASP B 37 ? MET B 59 ? ASP B 37 MET B 59 1 ? 23 HELX_P HELX_P6 6 GLU B 74 ? ARG B 127 ? GLU B 74 ARG B 127 1 ? 54 HELX_P HELX_P7 7 ASP B 145 ? GLY B 155 ? ASP B 145 GLY B 155 1 ? 11 # _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 4 SG ? ? ? 1_555 B CYS 137 SG ? ? A CYS 4 B CYS 137 1_555 ? ? ? ? ? ? ? 2.094 ? disulf2 disulf ? ? A CYS 42 SG ? ? ? 1_555 A CYS 274 SG ? ? A CYS 42 A CYS 274 1_555 ? ? ? ? ? ? ? 2.034 ? disulf3 disulf ? ? A CYS 55 SG ? ? ? 1_555 A CYS 67 SG ? ? A CYS 55 A CYS 67 1_555 ? ? ? ? ? ? ? 2.044 ? disulf4 disulf ? ? A CYS 90 SG ? ? ? 1_555 A CYS 135 SG ? ? A CYS 90 A CYS 135 1_555 ? ? ? ? ? ? ? 2.061 ? disulf5 disulf ? ? A CYS 278 SG ? ? ? 1_555 A CYS 302 SG ? ? A CYS 278 A CYS 302 1_555 ? ? ? ? ? ? ? 2.053 ? disulf6 disulf ? ? B CYS 144 SG ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.049 ? covale1 covale ? ? A ASN 11 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 11 A NAG 1011 1_555 ? ? ? ? ? ? ? 1.454 ? covale2 covale ? ? A ASN 23 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 23 A NAG 1023 1_555 ? ? ? ? ? ? ? 1.439 ? covale3 covale ? ? A ASN 165 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 165 A NAG 1165 1_555 ? ? ? ? ? ? ? 1.446 ? covale4 covale ? ? A ASN 286 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 286 A NAG 1286 1_555 ? ? ? ? ? ? ? 1.455 ? covale5 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 1023 A NAG 1024 1_555 ? ? ? ? ? ? ? 1.442 ? covale6 covale ? ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 1165 A NAG 1166 1_555 ? ? ? ? ? ? ? 1.440 ? covale7 covale ? ? G NAG . O4 ? ? ? 1_555 H MAN . C1 ? ? A NAG 1166 A MAN 1167 1_555 ? ? ? ? ? ? ? 1.457 ? covale8 covale ? ? H MAN . O3 ? ? ? 1_555 I BMA . C1 ? ? A MAN 1167 A BMA 1168 1_555 ? ? ? ? ? ? ? 1.442 ? covale9 covale ? ? H MAN . O6 ? ? ? 1_555 J MAN . C1 ? ? A MAN 1167 A MAN 1169 1_555 ? ? ? ? ? ? ? 1.455 ? covale10 covale ? ? L SIA . C2 ? ? ? 1_555 M GAL . O6 ? ? A SIA 1322 A GAL 1323 1_555 ? ? ? ? ? ? ? 1.429 ? covale11 covale ? ? B ASN 154 ND2 ? ? ? 1_555 N NAG . C1 ? ? B ASN 154 B NAG 1154 1_555 ? ? ? ? ? ? ? 1.441 ? covale12 covale ? ? N NAG . O4 ? ? ? 1_555 O NAG . C1 ? ? B NAG 1154 B NAG 1155 1_555 ? ? ? ? ? ? ? 1.446 ? covale13 covale ? ? O NAG . O4 ? ? ? 1_555 P BMA . C1 ? ? B NAG 1155 B BMA 1156 1_555 ? ? ? ? ? ? ? 1.447 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details BA ? 5 ? AA ? 2 ? AB ? 2 ? AC ? 3 ? AD ? 2 ? AE ? 3 ? AF ? 5 ? AG ? 5 ? AH ? 2 ? AI ? 4 ? AJ ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense BA 1 2 ? anti-parallel BA 2 3 ? anti-parallel BA 3 4 ? anti-parallel BA 4 5 ? anti-parallel AA 1 2 ? anti-parallel AB 1 2 ? anti-parallel AC 1 2 ? parallel AC 2 3 ? parallel AD 1 2 ? parallel AE 1 2 ? parallel AE 2 3 ? parallel AF 1 2 ? parallel AF 2 3 ? anti-parallel AF 3 4 ? anti-parallel AF 4 5 ? anti-parallel AG 1 2 ? parallel AG 2 3 ? anti-parallel AG 3 4 ? anti-parallel AG 4 5 ? anti-parallel AH 1 2 ? anti-parallel AI 1 2 ? anti-parallel AI 2 3 ? anti-parallel AI 3 4 ? anti-parallel AJ 1 2 ? anti-parallel AJ 2 3 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id BA 1 GLY B 31 ? ALA B 36 ? GLY B 31 ALA B 36 BA 2 TYR B 22 ? ASN B 28 ? TYR B 22 ASN B 28 BA 3 GLN A 2 ? TYR A 7 ? GLN A 2 TYR A 7 BA 4 CYS B 137 ? PHE B 140 ? CYS B 137 PHE B 140 BA 5 ALA B 130 ? GLU B 132 ? ALA B 130 GLU B 132 AA 1 GLN A 15 ? VAL A 16 ? GLN A 15 VAL A 16 AA 2 VAL A 24 ? THR A 25 ? VAL A 24 THR A 25 AB 1 ALA A 29 ? ASP A 31 ? ALA A 29 ASP A 31 AB 2 VAL A 312 ? ALA A 314 ? VAL A 312 ALA A 314 AC 1 LEU A 33 ? GLU A 34 ? LEU A 33 GLU A 34 AC 2 PHE A 291 ? HIS A 292 ? PHE A 291 HIS A 292 AC 3 LYS A 304 ? TYR A 305 ? LYS A 304 TYR A 305 AD 1 LEU A 41 ? LEU A 44 ? LEU A 41 LEU A 44 AD 2 TYR A 271 ? THR A 276 ? TYR A 271 THR A 276 AE 1 LEU A 50 ? ILE A 51 ? LEU A 50 ILE A 51 AE 2 ILE A 79 ? GLU A 81 ? ILE A 79 GLU A 81 AE 3 ILE A 264 ? LYS A 266 ? ILE A 264 LYS A 266 AF 1 GLY A 93 ? PHE A 95 ? GLY A 93 PHE A 95 AF 2 ARG A 225 ? LEU A 233 ? ARG A 225 LEU A 233 AF 3 LEU A 172 ? HIS A 180 ? LEU A 172 HIS A 180 AF 4 PHE A 247 ? PRO A 250 ? PHE A 247 PRO A 250 AF 5 VAL A 147 ? TRP A 149 ? VAL A 147 TRP A 149 AG 1 GLY A 93 ? PHE A 95 ? GLY A 93 PHE A 95 AG 2 ARG A 225 ? LEU A 233 ? ARG A 225 LEU A 233 AG 3 LEU A 172 ? HIS A 180 ? LEU A 172 HIS A 180 AG 4 TYR A 252 ? LYS A 259 ? TYR A 252 LYS A 259 AG 5 ILE A 108 ? GLN A 115 ? ILE A 108 GLN A 115 AH 1 SER A 132 ? TYR A 137 ? SER A 132 TYR A 137 AH 2 LYS A 140 ? SER A 142 ? LYS A 140 SER A 142 AI 1 ILE A 160 ? ASN A 165 ? ILE A 160 ASN A 165 AI 2 ALA A 238 ? SER A 243 ? ALA A 238 SER A 243 AI 3 ILE A 198 ? GLY A 201 ? ILE A 198 GLY A 201 AI 4 ASN A 206 ? LEU A 209 ? ASN A 206 LEU A 209 AJ 1 GLY A 283 ? ALA A 284 ? GLY A 283 ALA A 284 AJ 2 CYS A 278 ? THR A 280 ? CYS A 278 THR A 280 AJ 3 ILE A 299 ? GLY A 300 ? ILE A 299 GLY A 300 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id BA 1 2 N ALA B 35 ? N ALA B 35 O TYR B 24 ? O TYR B 24 BA 2 3 N SER B 27 ? N SER B 27 O GLN A 2 ? O GLN A 2 BA 3 4 N ILE A 3 ? N ILE A 3 O PHE B 138 ? O PHE B 138 BA 4 5 N GLU B 139 ? N GLU B 139 O LYS B 131 ? O LYS B 131 AA 1 2 N VAL A 16 ? N VAL A 16 O VAL A 24 ? O VAL A 24 AB 1 2 N GLN A 30 ? N GLN A 30 O LEU A 313 ? O LEU A 313 AC 1 2 N GLU A 34 ? N GLU A 34 O PHE A 291 ? O PHE A 291 AC 2 3 N HIS A 292 ? N HIS A 292 O LYS A 304 ? O LYS A 304 AD 1 2 O LEU A 41 ? O LEU A 41 N GLY A 272 ? N GLY A 272 AE 1 2 O LEU A 50 ? O LEU A 50 N VAL A 80 ? N VAL A 80 AE 2 3 N GLU A 81 ? N GLU A 81 O MET A 265 ? O MET A 265 AF 1 2 N ASP A 94 ? N ASP A 94 O MET A 226 ? O MET A 226 AF 2 3 N LEU A 233 ? N LEU A 233 O LEU A 172 ? O LEU A 172 AF 3 4 N GLY A 177 ? N GLY A 177 O ILE A 248 ? O ILE A 248 AF 4 5 N ALA A 249 ? N ALA A 249 O VAL A 148 ? O VAL A 148 AG 1 2 N ASP A 94 ? N ASP A 94 O MET A 226 ? O MET A 226 AG 2 3 N LEU A 233 ? N LEU A 233 O LEU A 172 ? O LEU A 172 AG 3 4 N LEU A 173 ? N LEU A 173 O TYR A 254 ? O TYR A 254 AG 4 5 O LYS A 258 ? O LYS A 258 N ASN A 109 ? N ASN A 109 AH 1 2 N TYR A 137 ? N TYR A 137 O LYS A 140 ? O LYS A 140 AI 1 2 N TYR A 164 ? N TYR A 164 O ILE A 239 ? O ILE A 239 AI 2 3 N GLU A 242 ? N GLU A 242 O SER A 199 ? O SER A 199 AI 3 4 N VAL A 200 ? N VAL A 200 O GLN A 207 ? O GLN A 207 AJ 1 2 N GLY A 283 ? N GLY A 283 O THR A 280 ? O THR A 280 AJ 2 3 N GLN A 279 ? N GLN A 279 O ILE A 299 ? O ILE A 299 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE MPO B 1163' AC2 Software ? ? ? ? 1 'Binding site for Mono-Saccharide NAG A1011 bound to ASN A 11' AC3 Software ? ? ? ? 1 'Binding site for Poly-Saccharide residues NAG A1023 through NAG A1024 bound to ASN A 23' AC4 Software ? ? ? ? 4 'Binding site for Poly-Saccharide residues NAG A1165 through MAN A1169 bound to ASN A 165' AC5 Software ? ? ? ? 1 'Binding site for Mono-Saccharide NAG A1286 bound to ASN A 286' AC6 Software ? ? ? ? 3 'Binding site for Poly-Saccharide residues NAG B1154 through BMA B1156 bound to ASN B 154' AC7 Software ? ? ? ? 11 'Binding site for Poly-Saccharide residues SIA A1322 through GAL A1323' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 4 TRP B 14 ? TRP B 14 . ? 1_555 ? 2 AC1 4 HIS B 25 ? HIS B 25 . ? 1_555 ? 3 AC1 4 TYR B 34 ? TYR B 34 . ? 1_555 ? 4 AC1 4 ASN B 135 ? ASN B 135 . ? 1_555 ? 5 AC2 1 ASN A 11 ? ASN A 11 . ? 1_555 ? 6 AC3 1 ASN A 23 ? ASN A 23 . ? 1_555 ? 7 AC4 4 ARG A 107 ? ARG A 107 . ? 6_555 ? 8 AC4 4 ASN A 165 ? ASN A 165 . ? 1_555 ? 9 AC4 4 ASN A 236 ? ASN A 236 . ? 1_555 ? 10 AC4 4 HIS A 295 ? HIS A 295 . ? 4_545 ? 11 AC5 1 ASN A 286 ? ASN A 286 . ? 1_555 ? 12 AC6 3 GLU B 147 ? GLU B 147 . ? 1_555 ? 13 AC6 3 GLU B 150 ? GLU B 150 . ? 1_555 ? 14 AC6 3 ASN B 154 ? ASN B 154 . ? 1_555 ? 15 AC7 11 TYR A 91 ? TYR A 91 . ? 1_555 ? 16 AC7 11 LEU A 129 ? LEU A 129 . ? 1_555 ? 17 AC7 11 VAL A 131 ? VAL A 131 . ? 1_555 ? 18 AC7 11 SER A 132 ? SER A 132 . ? 1_555 ? 19 AC7 11 SER A 133 ? SER A 133 . ? 1_555 ? 20 AC7 11 HIS A 179 ? HIS A 179 . ? 1_555 ? 21 AC7 11 GLU A 186 ? GLU A 186 . ? 1_555 ? 22 AC7 11 LEU A 190 ? LEU A 190 . ? 1_555 ? 23 AC7 11 GLY A 221 ? GLY A 221 . ? 1_555 ? 24 AC7 11 GLN A 222 ? GLN A 222 . ? 1_555 ? 25 AC7 11 HOH R . ? HOH A 2038 . ? 1_555 ? # _database_PDB_matrix.entry_id 4CQU _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 4CQU _atom_sites.fract_transf_matrix[1][1] 0.009856 _atom_sites.fract_transf_matrix[1][2] 0.005690 _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] 0.011380 _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] 0.002211 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ASP A 1 1 ? 37.116 -15.517 -83.666 1.00 71.18 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? 36.272 -16.092 -82.580 1.00 70.54 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? 37.137 -16.804 -81.557 1.00 68.73 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? 38.029 -17.565 -81.928 1.00 66.29 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? 35.266 -17.095 -83.144 1.00 70.50 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? 34.297 -16.471 -84.109 1.00 72.54 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? 34.433 -15.267 -84.415 1.00 72.58 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? 33.394 -17.198 -84.564 1.00 75.64 ? 1 ASP A OD2 1 ATOM 9 N N . GLN A 1 2 ? 36.866 -16.565 -80.275 1.00 68.62 ? 2 GLN A N 1 ATOM 10 C CA . GLN A 1 2 ? 37.600 -17.243 -79.219 1.00 66.70 ? 2 GLN A CA 1 ATOM 11 C C . GLN A 1 2 ? 36.791 -17.530 -77.974 1.00 64.85 ? 2 GLN A C 1 ATOM 12 O O . GLN A 1 2 ? 35.761 -16.892 -77.702 1.00 64.88 ? 2 GLN A O 1 ATOM 13 C CB . GLN A 1 2 ? 38.860 -16.461 -78.835 1.00 68.22 ? 2 GLN A CB 1 ATOM 14 C CG . GLN A 1 2 ? 38.643 -15.052 -78.333 1.00 71.21 ? 2 GLN A CG 1 ATOM 15 C CD . GLN A 1 2 ? 39.956 -14.299 -78.185 1.00 73.61 ? 2 GLN A CD 1 ATOM 16 O OE1 . GLN A 1 2 ? 40.286 -13.815 -77.106 1.00 74.14 ? 2 GLN A OE1 1 ATOM 17 N NE2 . GLN A 1 2 ? 40.713 -14.202 -79.277 1.00 75.56 ? 2 GLN A NE2 1 ATOM 18 N N . ILE A 1 3 ? 37.288 -18.513 -77.229 1.00 60.44 ? 3 ILE A N 1 ATOM 19 C CA . ILE A 1 3 ? 36.768 -18.846 -75.922 1.00 60.04 ? 3 ILE A CA 1 ATOM 20 C C . ILE A 1 3 ? 37.929 -18.844 -74.941 1.00 58.40 ? 3 ILE A C 1 ATOM 21 O O . ILE A 1 3 ? 39.024 -19.320 -75.256 1.00 56.58 ? 3 ILE A O 1 ATOM 22 C CB . ILE A 1 3 ? 36.023 -20.197 -75.920 1.00 61.68 ? 3 ILE A CB 1 ATOM 23 C CG1 . ILE A 1 3 ? 35.311 -20.406 -74.585 1.00 62.84 ? 3 ILE A CG1 1 ATOM 24 C CG2 . ILE A 1 3 ? 36.962 -21.367 -76.195 1.00 59.92 ? 3 ILE A CG2 1 ATOM 25 C CD1 . ILE A 1 3 ? 34.230 -21.458 -74.652 1.00 65.14 ? 3 ILE A CD1 1 ATOM 26 N N . CYS A 1 4 ? 37.681 -18.290 -73.760 1.00 58.18 ? 4 CYS A N 1 ATOM 27 C CA . CYS A 1 4 ? 38.715 -18.067 -72.767 1.00 56.16 ? 4 CYS A CA 1 ATOM 28 C C . CYS A 1 4 ? 38.306 -18.726 -71.470 1.00 55.28 ? 4 CYS A C 1 ATOM 29 O O . CYS A 1 4 ? 37.120 -18.831 -71.164 1.00 56.48 ? 4 CYS A O 1 ATOM 30 C CB . CYS A 1 4 ? 38.908 -16.565 -72.523 1.00 58.34 ? 4 CYS A CB 1 ATOM 31 S SG . CYS A 1 4 ? 39.361 -15.610 -73.993 1.00 62.84 ? 4 CYS A SG 1 ATOM 32 N N . ILE A 1 5 ? 39.294 -19.159 -70.699 1.00 52.26 ? 5 ILE A N 1 ATOM 33 C CA . ILE A 1 5 ? 39.046 -19.670 -69.367 1.00 51.02 ? 5 ILE A CA 1 ATOM 34 C C . ILE A 1 5 ? 39.519 -18.632 -68.369 1.00 50.19 ? 5 ILE A C 1 ATOM 35 O O . ILE A 1 5 ? 40.575 -18.048 -68.549 1.00 49.16 ? 5 ILE A O 1 ATOM 36 C CB . ILE A 1 5 ? 39.777 -20.996 -69.154 1.00 49.71 ? 5 ILE A CB 1 ATOM 37 C CG1 . ILE A 1 5 ? 39.312 -22.009 -70.200 1.00 51.50 ? 5 ILE A CG1 1 ATOM 38 C CG2 . ILE A 1 5 ? 39.542 -21.529 -67.754 1.00 49.40 ? 5 ILE A CG2 1 ATOM 39 C CD1 . ILE A 1 5 ? 37.899 -22.495 -69.993 1.00 53.72 ? 5 ILE A CD1 1 ATOM 40 N N . GLY A 1 6 ? 38.720 -18.387 -67.334 1.00 50.98 ? 6 GLY A N 1 ATOM 41 C CA . GLY A 1 6 ? 39.070 -17.396 -66.323 1.00 51.80 ? 6 GLY A CA 1 ATOM 42 C C . GLY A 1 6 ? 38.420 -17.636 -64.980 1.00 51.39 ? 6 GLY A C 1 ATOM 43 O O . GLY A 1 6 ? 37.764 -18.649 -64.767 1.00 54.04 ? 6 GLY A O 1 ATOM 44 N N . TYR A 1 7 ? 38.596 -16.683 -64.079 1.00 50.78 ? 7 TYR A N 1 ATOM 45 C CA . TYR A 1 7 ? 38.133 -16.828 -62.721 1.00 51.41 ? 7 TYR A CA 1 ATOM 46 C C . TYR A 1 7 ? 37.590 -15.512 -62.185 1.00 53.38 ? 7 TYR A C 1 ATOM 47 O O . TYR A 1 7 ? 37.803 -14.452 -62.764 1.00 53.49 ? 7 TYR A O 1 ATOM 48 C CB . TYR A 1 7 ? 39.270 -17.344 -61.833 1.00 51.53 ? 7 TYR A CB 1 ATOM 49 C CG . TYR A 1 7 ? 40.547 -16.529 -61.912 1.00 51.52 ? 7 TYR A CG 1 ATOM 50 C CD1 . TYR A 1 7 ? 41.480 -16.753 -62.913 1.00 50.66 ? 7 TYR A CD1 1 ATOM 51 C CD2 . TYR A 1 7 ? 40.818 -15.538 -60.976 1.00 54.26 ? 7 TYR A CD2 1 ATOM 52 C CE1 . TYR A 1 7 ? 42.637 -15.994 -62.992 1.00 52.81 ? 7 TYR A CE1 1 ATOM 53 C CE2 . TYR A 1 7 ? 41.981 -14.784 -61.040 1.00 53.72 ? 7 TYR A CE2 1 ATOM 54 C CZ . TYR A 1 7 ? 42.882 -15.014 -62.045 1.00 53.13 ? 7 TYR A CZ 1 ATOM 55 O OH . TYR A 1 7 ? 44.024 -14.256 -62.110 1.00 54.67 ? 7 TYR A OH 1 ATOM 56 N N . HIS A 1 8 ? 36.892 -15.617 -61.063 1.00 54.17 ? 8 HIS A N 1 ATOM 57 C CA . HIS A 1 8 ? 36.136 -14.528 -60.459 1.00 57.29 ? 8 HIS A CA 1 ATOM 58 C C . HIS A 1 8 ? 37.035 -13.467 -59.827 1.00 59.06 ? 8 HIS A C 1 ATOM 59 O O . HIS A 1 8 ? 38.063 -13.775 -59.222 1.00 58.20 ? 8 HIS A O 1 ATOM 60 C CB . HIS A 1 8 ? 35.225 -15.137 -59.385 1.00 57.94 ? 8 HIS A CB 1 ATOM 61 C CG . HIS A 1 8 ? 34.345 -14.159 -58.673 1.00 59.92 ? 8 HIS A CG 1 ATOM 62 N ND1 . HIS A 1 8 ? 33.306 -13.498 -59.293 1.00 62.34 ? 8 HIS A ND1 1 ATOM 63 C CD2 . HIS A 1 8 ? 34.304 -13.786 -57.370 1.00 59.39 ? 8 HIS A CD2 1 ATOM 64 C CE1 . HIS A 1 8 ? 32.686 -12.734 -58.411 1.00 62.92 ? 8 HIS A CE1 1 ATOM 65 N NE2 . HIS A 1 8 ? 33.271 -12.892 -57.236 1.00 60.76 ? 8 HIS A NE2 1 ATOM 66 N N . ALA A 1 9 ? 36.635 -12.211 -59.978 1.00 61.82 ? 9 ALA A N 1 ATOM 67 C CA . ALA A 1 9 ? 37.214 -11.110 -59.216 1.00 61.36 ? 9 ALA A CA 1 ATOM 68 C C . ALA A 1 9 ? 36.067 -10.253 -58.701 1.00 63.82 ? 9 ALA A C 1 ATOM 69 O O . ALA A 1 9 ? 34.955 -10.330 -59.214 1.00 65.75 ? 9 ALA A O 1 ATOM 70 C CB . ALA A 1 9 ? 38.154 -10.295 -60.080 1.00 60.01 ? 9 ALA A CB 1 ATOM 71 N N . ASN A 1 10 ? 36.329 -9.462 -57.671 1.00 63.94 ? 10 ASN A N 1 ATOM 72 C CA . ASN A 1 10 ? 35.321 -8.573 -57.127 1.00 66.52 ? 10 ASN A CA 1 ATOM 73 C C . ASN A 1 10 ? 35.979 -7.395 -56.402 1.00 69.44 ? 10 ASN A C 1 ATOM 74 O O . ASN A 1 10 ? 37.185 -7.211 -56.509 1.00 67.29 ? 10 ASN A O 1 ATOM 75 C CB . ASN A 1 10 ? 34.370 -9.356 -56.218 1.00 65.42 ? 10 ASN A CB 1 ATOM 76 C CG . ASN A 1 10 ? 35.037 -9.840 -54.953 1.00 63.39 ? 10 ASN A CG 1 ATOM 77 O OD1 . ASN A 1 10 ? 36.175 -9.487 -54.666 1.00 62.56 ? 10 ASN A OD1 1 ATOM 78 N ND2 . ASN A 1 10 ? 34.330 -10.655 -54.188 1.00 62.95 ? 10 ASN A ND2 1 ATOM 79 N N . ASN A 1 11 ? 35.194 -6.602 -55.679 1.00 76.67 ? 11 ASN A N 1 ATOM 80 C CA . ASN A 1 11 ? 35.709 -5.393 -55.028 1.00 82.75 ? 11 ASN A CA 1 ATOM 81 C C . ASN A 1 11 ? 36.237 -5.630 -53.603 1.00 78.14 ? 11 ASN A C 1 ATOM 82 O O . ASN A 1 11 ? 36.476 -4.676 -52.862 1.00 80.31 ? 11 ASN A O 1 ATOM 83 C CB . ASN A 1 11 ? 34.647 -4.266 -55.054 1.00 91.80 ? 11 ASN A CB 1 ATOM 84 C CG . ASN A 1 11 ? 33.368 -4.619 -54.292 1.00 103.04 ? 11 ASN A CG 1 ATOM 85 O OD1 . ASN A 1 11 ? 33.354 -5.526 -53.456 1.00 101.42 ? 11 ASN A OD1 1 ATOM 86 N ND2 . ASN A 1 11 ? 32.279 -3.887 -54.584 1.00 119.71 ? 11 ASN A ND2 1 ATOM 87 N N . SER A 1 12 ? 36.432 -6.895 -53.232 1.00 72.73 ? 12 SER A N 1 ATOM 88 C CA . SER A 1 12 ? 36.845 -7.259 -51.873 1.00 69.02 ? 12 SER A CA 1 ATOM 89 C C . SER A 1 12 ? 38.253 -6.768 -51.533 1.00 67.99 ? 12 SER A C 1 ATOM 90 O O . SER A 1 12 ? 39.157 -6.813 -52.378 1.00 64.54 ? 12 SER A O 1 ATOM 91 C CB . SER A 1 12 ? 36.779 -8.780 -51.678 1.00 66.27 ? 12 SER A CB 1 ATOM 92 O OG . SER A 1 12 ? 37.247 -9.169 -50.396 1.00 63.27 ? 12 SER A OG 1 ATOM 93 N N . THR A 1 13 ? 38.406 -6.293 -50.293 1.00 67.71 ? 13 THR A N 1 ATOM 94 C CA . THR A 1 13 ? 39.693 -5.892 -49.725 1.00 67.42 ? 13 THR A CA 1 ATOM 95 C C . THR A 1 13 ? 40.087 -6.769 -48.535 1.00 66.42 ? 13 THR A C 1 ATOM 96 O O . THR A 1 13 ? 41.098 -6.502 -47.884 1.00 64.15 ? 13 THR A O 1 ATOM 97 C CB . THR A 1 13 ? 39.650 -4.438 -49.223 1.00 71.13 ? 13 THR A CB 1 ATOM 98 O OG1 . THR A 1 13 ? 38.690 -4.329 -48.160 1.00 72.56 ? 13 THR A OG1 1 ATOM 99 C CG2 . THR A 1 13 ? 39.283 -3.478 -50.354 1.00 72.76 ? 13 THR A CG2 1 ATOM 100 N N . GLU A 1 14 ? 39.286 -7.795 -48.239 1.00 66.39 ? 14 GLU A N 1 ATOM 101 C CA . GLU A 1 14 ? 39.631 -8.774 -47.208 1.00 67.33 ? 14 GLU A CA 1 ATOM 102 C C . GLU A 1 14 ? 40.997 -9.401 -47.512 1.00 62.99 ? 14 GLU A C 1 ATOM 103 O O . GLU A 1 14 ? 41.301 -9.705 -48.664 1.00 60.96 ? 14 GLU A O 1 ATOM 104 C CB . GLU A 1 14 ? 38.572 -9.877 -47.131 1.00 72.24 ? 14 GLU A CB 1 ATOM 105 C CG . GLU A 1 14 ? 37.194 -9.427 -46.663 1.00 78.22 ? 14 GLU A CG 1 ATOM 106 C CD . GLU A 1 14 ? 37.183 -8.949 -45.220 1.00 84.84 ? 14 GLU A CD 1 ATOM 107 O OE1 . GLU A 1 14 ? 37.826 -9.608 -44.370 1.00 87.61 ? 14 GLU A OE1 1 ATOM 108 O OE2 . GLU A 1 14 ? 36.538 -7.907 -44.936 1.00 91.86 ? 14 GLU A OE2 1 ATOM 109 N N . GLN A 1 15 ? 41.814 -9.573 -46.478 1.00 60.92 ? 15 GLN A N 1 ATOM 110 C CA . GLN A 1 15 ? 43.164 -10.114 -46.627 1.00 59.42 ? 15 GLN A CA 1 ATOM 111 C C . GLN A 1 15 ? 43.364 -11.312 -45.713 1.00 56.60 ? 15 GLN A C 1 ATOM 112 O O . GLN A 1 15 ? 42.788 -11.375 -44.638 1.00 56.21 ? 15 GLN A O 1 ATOM 113 C CB . GLN A 1 15 ? 44.210 -9.066 -46.263 1.00 62.07 ? 15 GLN A CB 1 ATOM 114 C CG . GLN A 1 15 ? 44.113 -7.754 -47.016 1.00 65.97 ? 15 GLN A CG 1 ATOM 115 C CD . GLN A 1 15 ? 45.254 -6.811 -46.681 1.00 68.93 ? 15 GLN A CD 1 ATOM 116 O OE1 . GLN A 1 15 ? 45.757 -6.097 -47.546 1.00 71.59 ? 15 GLN A OE1 1 ATOM 117 N NE2 . GLN A 1 15 ? 45.672 -6.807 -45.418 1.00 70.73 ? 15 GLN A NE2 1 ATOM 118 N N . VAL A 1 16 ? 44.198 -12.252 -46.140 1.00 54.99 ? 16 VAL A N 1 ATOM 119 C CA . VAL A 1 16 ? 44.555 -13.405 -45.320 1.00 52.75 ? 16 VAL A CA 1 ATOM 120 C C . VAL A 1 16 ? 46.055 -13.567 -45.352 1.00 52.30 ? 16 VAL A C 1 ATOM 121 O O . VAL A 1 16 ? 46.697 -13.092 -46.286 1.00 51.08 ? 16 VAL A O 1 ATOM 122 C CB . VAL A 1 16 ? 43.909 -14.706 -45.838 1.00 51.51 ? 16 VAL A CB 1 ATOM 123 C CG1 . VAL A 1 16 ? 42.405 -14.549 -45.911 1.00 52.82 ? 16 VAL A CG1 1 ATOM 124 C CG2 . VAL A 1 16 ? 44.471 -15.101 -47.199 1.00 51.22 ? 16 VAL A CG2 1 ATOM 125 N N . ASP A 1 17 ? 46.600 -14.252 -44.345 1.00 52.20 ? 17 ASP A N 1 ATOM 126 C CA . ASP A 1 17 ? 48.022 -14.590 -44.312 1.00 51.59 ? 17 ASP A CA 1 ATOM 127 C C . ASP A 1 17 ? 48.266 -16.045 -44.705 1.00 49.91 ? 17 ASP A C 1 ATOM 128 O O . ASP A 1 17 ? 47.423 -16.914 -44.466 1.00 46.75 ? 17 ASP A O 1 ATOM 129 C CB . ASP A 1 17 ? 48.588 -14.361 -42.913 1.00 53.56 ? 17 ASP A CB 1 ATOM 130 C CG . ASP A 1 17 ? 48.668 -12.880 -42.536 1.00 57.08 ? 17 ASP A CG 1 ATOM 131 O OD1 . ASP A 1 17 ? 48.838 -12.025 -43.437 1.00 56.62 ? 17 ASP A OD1 1 ATOM 132 O OD2 . ASP A 1 17 ? 48.587 -12.581 -41.318 1.00 59.11 ? 17 ASP A OD2 1 ATOM 133 N N . THR A 1 18 ? 49.433 -16.288 -45.304 1.00 50.61 ? 18 THR A N 1 ATOM 134 C CA . THR A 1 18 ? 49.948 -17.636 -45.576 1.00 49.67 ? 18 THR A CA 1 ATOM 135 C C . THR A 1 18 ? 51.378 -17.725 -45.052 1.00 50.76 ? 18 THR A C 1 ATOM 136 O O . THR A 1 18 ? 51.933 -16.732 -44.603 1.00 54.48 ? 18 THR A O 1 ATOM 137 C CB . THR A 1 18 ? 49.961 -17.946 -47.093 1.00 49.46 ? 18 THR A CB 1 ATOM 138 O OG1 . THR A 1 18 ? 50.888 -17.083 -47.763 1.00 51.87 ? 18 THR A OG1 1 ATOM 139 C CG2 . THR A 1 18 ? 48.596 -17.747 -47.699 1.00 49.02 ? 18 THR A CG2 1 ATOM 140 N N . ILE A 1 19 ? 51.982 -18.907 -45.125 1.00 54.21 ? 19 ILE A N 1 ATOM 141 C CA . ILE A 1 19 ? 53.370 -19.103 -44.678 1.00 54.81 ? 19 ILE A CA 1 ATOM 142 C C . ILE A 1 19 ? 54.339 -18.227 -45.482 1.00 56.73 ? 19 ILE A C 1 ATOM 143 O O . ILE A 1 19 ? 55.254 -17.610 -44.921 1.00 58.38 ? 19 ILE A O 1 ATOM 144 C CB . ILE A 1 19 ? 53.799 -20.585 -44.846 1.00 59.88 ? 19 ILE A CB 1 ATOM 145 C CG1 . ILE A 1 19 ? 52.976 -21.523 -43.950 1.00 61.87 ? 19 ILE A CG1 1 ATOM 146 C CG2 . ILE A 1 19 ? 55.279 -20.773 -44.555 1.00 61.47 ? 19 ILE A CG2 1 ATOM 147 C CD1 . ILE A 1 19 ? 53.225 -21.371 -42.462 1.00 61.30 ? 19 ILE A CD1 1 ATOM 148 N N . MET A 1 20 ? 54.134 -18.183 -46.797 1.00 56.81 ? 20 MET A N 1 ATOM 149 C CA . MET A 1 20 ? 55.054 -17.509 -47.716 1.00 58.10 ? 20 MET A CA 1 ATOM 150 C C . MET A 1 20 ? 54.704 -16.059 -48.027 1.00 58.74 ? 20 MET A C 1 ATOM 151 O O . MET A 1 20 ? 55.517 -15.346 -48.620 1.00 59.28 ? 20 MET A O 1 ATOM 152 C CB . MET A 1 20 ? 55.101 -18.256 -49.044 1.00 58.90 ? 20 MET A CB 1 ATOM 153 C CG . MET A 1 20 ? 55.918 -19.528 -49.024 1.00 60.63 ? 20 MET A CG 1 ATOM 154 S SD . MET A 1 20 ? 56.087 -20.183 -50.688 1.00 65.00 ? 20 MET A SD 1 ATOM 155 C CE . MET A 1 20 ? 57.730 -20.852 -50.589 1.00 68.47 ? 20 MET A CE 1 ATOM 156 N N . GLU A 1 21 ? 53.499 -15.626 -47.672 1.00 57.23 ? 21 GLU A N 1 ATOM 157 C CA . GLU A 1 21 ? 53.041 -14.298 -48.060 1.00 57.82 ? 21 GLU A CA 1 ATOM 158 C C . GLU A 1 21 ? 51.993 -13.790 -47.088 1.00 57.15 ? 21 GLU A C 1 ATOM 159 O O . GLU A 1 21 ? 51.093 -14.524 -46.684 1.00 55.82 ? 21 GLU A O 1 ATOM 160 C CB . GLU A 1 21 ? 52.475 -14.316 -49.485 1.00 58.46 ? 21 GLU A CB 1 ATOM 161 C CG . GLU A 1 21 ? 52.429 -12.941 -50.144 1.00 63.51 ? 21 GLU A CG 1 ATOM 162 C CD . GLU A 1 21 ? 51.913 -12.963 -51.585 1.00 66.88 ? 21 GLU A CD 1 ATOM 163 O OE1 . GLU A 1 21 ? 51.844 -14.061 -52.195 1.00 64.94 ? 21 GLU A OE1 1 ATOM 164 O OE2 . GLU A 1 21 ? 51.581 -11.869 -52.109 1.00 65.09 ? 21 GLU A OE2 1 ATOM 165 N N . LYS A 1 22 ? 52.110 -12.523 -46.723 1.00 59.34 ? 22 LYS A N 1 ATOM 166 C CA . LYS A 1 22 ? 51.192 -11.918 -45.779 1.00 61.91 ? 22 LYS A CA 1 ATOM 167 C C . LYS A 1 22 ? 50.331 -10.918 -46.521 1.00 59.42 ? 22 LYS A C 1 ATOM 168 O O . LYS A 1 22 ? 50.741 -10.391 -47.556 1.00 59.26 ? 22 LYS A O 1 ATOM 169 C CB . LYS A 1 22 ? 51.981 -11.285 -44.631 1.00 67.86 ? 22 LYS A CB 1 ATOM 170 C CG . LYS A 1 22 ? 52.746 -12.334 -43.827 1.00 72.77 ? 22 LYS A CG 1 ATOM 171 C CD . LYS A 1 22 ? 53.656 -11.739 -42.765 1.00 81.03 ? 22 LYS A CD 1 ATOM 172 C CE . LYS A 1 22 ? 52.914 -11.461 -41.464 1.00 85.68 ? 22 LYS A CE 1 ATOM 173 N NZ . LYS A 1 22 ? 53.842 -11.128 -40.345 1.00 86.78 ? 22 LYS A NZ 1 ATOM 174 N N . ASN A 1 23 ? 49.118 -10.700 -46.029 1.00 57.93 ? 23 ASN A N 1 ATOM 175 C CA . ASN A 1 23 ? 48.234 -9.682 -46.594 1.00 60.82 ? 23 ASN A CA 1 ATOM 176 C C . ASN A 1 23 ? 47.892 -9.915 -48.061 1.00 58.94 ? 23 ASN A C 1 ATOM 177 O O . ASN A 1 23 ? 48.007 -9.015 -48.886 1.00 59.50 ? 23 ASN A O 1 ATOM 178 C CB . ASN A 1 23 ? 48.851 -8.282 -46.407 1.00 65.11 ? 23 ASN A CB 1 ATOM 179 C CG . ASN A 1 23 ? 49.008 -7.910 -44.950 1.00 70.33 ? 23 ASN A CG 1 ATOM 180 O OD1 . ASN A 1 23 ? 48.529 -8.622 -44.058 1.00 69.24 ? 23 ASN A OD1 1 ATOM 181 N ND2 . ASN A 1 23 ? 49.676 -6.790 -44.693 1.00 80.96 ? 23 ASN A ND2 1 ATOM 182 N N . VAL A 1 24 ? 47.470 -11.136 -48.373 1.00 58.52 ? 24 VAL A N 1 ATOM 183 C CA . VAL A 1 24 ? 46.990 -11.485 -49.707 1.00 56.16 ? 24 VAL A CA 1 ATOM 184 C C . VAL A 1 24 ? 45.515 -11.111 -49.793 1.00 55.46 ? 24 VAL A C 1 ATOM 185 O O . VAL A 1 24 ? 44.717 -11.555 -48.975 1.00 54.17 ? 24 VAL A O 1 ATOM 186 C CB . VAL A 1 24 ? 47.149 -12.994 -49.964 1.00 55.67 ? 24 VAL A CB 1 ATOM 187 C CG1 . VAL A 1 24 ? 46.675 -13.356 -51.364 1.00 57.11 ? 24 VAL A CG1 1 ATOM 188 C CG2 . VAL A 1 24 ? 48.600 -13.416 -49.762 1.00 54.72 ? 24 VAL A CG2 1 ATOM 189 N N . THR A 1 25 ? 45.151 -10.273 -50.759 1.00 55.34 ? 25 THR A N 1 ATOM 190 C CA . THR A 1 25 ? 43.755 -9.882 -50.925 1.00 55.08 ? 25 THR A CA 1 ATOM 191 C C . THR A 1 25 ? 43.000 -11.015 -51.593 1.00 54.58 ? 25 THR A C 1 ATOM 192 O O . THR A 1 25 ? 43.427 -11.517 -52.638 1.00 55.48 ? 25 THR A O 1 ATOM 193 C CB . THR A 1 25 ? 43.606 -8.626 -51.790 1.00 57.31 ? 25 THR A CB 1 ATOM 194 O OG1 . THR A 1 25 ? 44.468 -7.604 -51.290 1.00 60.06 ? 25 THR A OG1 1 ATOM 195 C CG2 . THR A 1 25 ? 42.173 -8.113 -51.760 1.00 60.05 ? 25 THR A CG2 1 ATOM 196 N N . VAL A 1 26 ? 41.884 -11.415 -50.993 1.00 53.38 ? 26 VAL A N 1 ATOM 197 C CA . VAL A 1 26 ? 41.069 -12.498 -51.532 1.00 52.10 ? 26 VAL A CA 1 ATOM 198 C C . VAL A 1 26 ? 39.642 -12.046 -51.781 1.00 54.74 ? 26 VAL A C 1 ATOM 199 O O . VAL A 1 26 ? 39.189 -11.065 -51.202 1.00 57.37 ? 26 VAL A O 1 ATOM 200 C CB . VAL A 1 26 ? 41.060 -13.728 -50.610 1.00 49.96 ? 26 VAL A CB 1 ATOM 201 C CG1 . VAL A 1 26 ? 42.435 -14.366 -50.584 1.00 47.78 ? 26 VAL A CG1 1 ATOM 202 C CG2 . VAL A 1 26 ? 40.601 -13.365 -49.203 1.00 51.12 ? 26 VAL A CG2 1 ATOM 203 N N . THR A 1 27 ? 38.945 -12.778 -52.649 1.00 55.83 ? 27 THR A N 1 ATOM 204 C CA . THR A 1 27 ? 37.578 -12.446 -53.042 1.00 56.29 ? 27 THR A CA 1 ATOM 205 C C . THR A 1 27 ? 36.596 -12.697 -51.907 1.00 57.73 ? 27 THR A C 1 ATOM 206 O O . THR A 1 27 ? 35.622 -11.962 -51.757 1.00 61.20 ? 27 THR A O 1 ATOM 207 C CB . THR A 1 27 ? 37.128 -13.252 -54.280 1.00 56.10 ? 27 THR A CB 1 ATOM 208 O OG1 . THR A 1 27 ? 37.142 -14.660 -53.996 1.00 53.30 ? 27 THR A OG1 1 ATOM 209 C CG2 . THR A 1 27 ? 38.031 -12.961 -55.460 1.00 55.29 ? 27 THR A CG2 1 ATOM 210 N N . HIS A 1 28 ? 36.858 -13.738 -51.119 1.00 56.99 ? 28 HIS A N 1 ATOM 211 C CA . HIS A 1 28 ? 36.029 -14.104 -49.971 1.00 57.51 ? 28 HIS A CA 1 ATOM 212 C C . HIS A 1 28 ? 36.871 -14.675 -48.841 1.00 57.64 ? 28 HIS A C 1 ATOM 213 O O . HIS A 1 28 ? 37.860 -15.378 -49.080 1.00 56.14 ? 28 HIS A O 1 ATOM 214 C CB . HIS A 1 28 ? 34.995 -15.145 -50.378 1.00 58.41 ? 28 HIS A CB 1 ATOM 215 C CG . HIS A 1 28 ? 34.176 -14.742 -51.560 1.00 61.28 ? 28 HIS A CG 1 ATOM 216 N ND1 . HIS A 1 28 ? 34.609 -14.919 -52.856 1.00 59.96 ? 28 HIS A ND1 1 ATOM 217 C CD2 . HIS A 1 28 ? 32.963 -14.145 -51.643 1.00 62.51 ? 28 HIS A CD2 1 ATOM 218 C CE1 . HIS A 1 28 ? 33.692 -14.459 -53.688 1.00 61.64 ? 28 HIS A CE1 1 ATOM 219 N NE2 . HIS A 1 28 ? 32.685 -13.984 -52.977 1.00 62.72 ? 28 HIS A NE2 1 ATOM 220 N N . ALA A 1 29 ? 36.447 -14.387 -47.613 1.00 59.19 ? 29 ALA A N 1 ATOM 221 C CA . ALA A 1 29 ? 37.134 -14.834 -46.405 1.00 58.77 ? 29 ALA A CA 1 ATOM 222 C C . ALA A 1 29 ? 36.126 -15.071 -45.290 1.00 59.70 ? 29 ALA A C 1 ATOM 223 O O . ALA A 1 29 ? 34.981 -14.628 -45.368 1.00 63.47 ? 29 ALA A O 1 ATOM 224 C CB . ALA A 1 29 ? 38.152 -13.799 -45.967 1.00 59.57 ? 29 ALA A CB 1 ATOM 225 N N . GLN A 1 30 ? 36.557 -15.782 -44.260 1.00 58.37 ? 30 GLN A N 1 ATOM 226 C CA . GLN A 1 30 ? 35.718 -16.056 -43.100 1.00 60.57 ? 30 GLN A CA 1 ATOM 227 C C . GLN A 1 30 ? 36.528 -15.854 -41.812 1.00 58.38 ? 30 GLN A C 1 ATOM 228 O O . GLN A 1 30 ? 37.485 -16.588 -41.536 1.00 52.62 ? 30 GLN A O 1 ATOM 229 C CB . GLN A 1 30 ? 35.140 -17.476 -43.172 1.00 61.83 ? 30 GLN A CB 1 ATOM 230 C CG . GLN A 1 30 ? 34.291 -17.857 -41.960 1.00 64.45 ? 30 GLN A CG 1 ATOM 231 C CD . GLN A 1 30 ? 33.464 -19.116 -42.163 1.00 65.52 ? 30 GLN A CD 1 ATOM 232 O OE1 . GLN A 1 30 ? 33.180 -19.524 -43.289 1.00 69.75 ? 30 GLN A OE1 1 ATOM 233 N NE2 . GLN A 1 30 ? 33.064 -19.732 -41.065 1.00 66.85 ? 30 GLN A NE2 1 ATOM 234 N N . ASP A 1 31 ? 36.149 -14.829 -41.058 1.00 59.97 ? 31 ASP A N 1 ATOM 235 C CA . ASP A 1 31 ? 36.714 -14.550 -39.744 1.00 61.40 ? 31 ASP A CA 1 ATOM 236 C C . ASP A 1 31 ? 36.182 -15.601 -38.768 1.00 60.80 ? 31 ASP A C 1 ATOM 237 O O . ASP A 1 31 ? 34.979 -15.867 -38.743 1.00 62.55 ? 31 ASP A O 1 ATOM 238 C CB . ASP A 1 31 ? 36.288 -13.150 -39.299 1.00 62.95 ? 31 ASP A CB 1 ATOM 239 C CG . ASP A 1 31 ? 36.985 -12.688 -38.041 1.00 66.14 ? 31 ASP A CG 1 ATOM 240 O OD1 . ASP A 1 31 ? 37.718 -13.484 -37.409 1.00 63.28 ? 31 ASP A OD1 1 ATOM 241 O OD2 . ASP A 1 31 ? 36.799 -11.502 -37.685 1.00 71.96 ? 31 ASP A OD2 1 ATOM 242 N N . ILE A 1 32 ? 37.068 -16.193 -37.972 1.00 57.72 ? 32 ILE A N 1 ATOM 243 C CA . ILE A 1 32 ? 36.664 -17.235 -37.021 1.00 58.49 ? 32 ILE A CA 1 ATOM 244 C C . ILE A 1 32 ? 36.990 -16.913 -35.550 1.00 58.82 ? 32 ILE A C 1 ATOM 245 O O . ILE A 1 32 ? 36.847 -17.779 -34.684 1.00 58.19 ? 32 ILE A O 1 ATOM 246 C CB . ILE A 1 32 ? 37.285 -18.598 -37.404 1.00 57.34 ? 32 ILE A CB 1 ATOM 247 C CG1 . ILE A 1 32 ? 38.813 -18.523 -37.430 1.00 54.68 ? 32 ILE A CG1 1 ATOM 248 C CG2 . ILE A 1 32 ? 36.773 -19.039 -38.766 1.00 58.42 ? 32 ILE A CG2 1 ATOM 249 C CD1 . ILE A 1 32 ? 39.474 -19.878 -37.487 1.00 53.91 ? 32 ILE A CD1 1 ATOM 250 N N . LEU A 1 33 ? 37.407 -15.674 -35.281 1.00 58.82 ? 33 LEU A N 1 ATOM 251 C CA . LEU A 1 33 ? 37.793 -15.227 -33.941 1.00 60.17 ? 33 LEU A CA 1 ATOM 252 C C . LEU A 1 33 ? 36.872 -14.119 -33.434 1.00 63.21 ? 33 LEU A C 1 ATOM 253 O O . LEU A 1 33 ? 36.786 -13.047 -34.043 1.00 63.66 ? 33 LEU A O 1 ATOM 254 C CB . LEU A 1 33 ? 39.232 -14.700 -33.963 1.00 59.65 ? 33 LEU A CB 1 ATOM 255 C CG . LEU A 1 33 ? 39.811 -14.162 -32.647 1.00 59.72 ? 33 LEU A CG 1 ATOM 256 C CD1 . LEU A 1 33 ? 39.950 -15.289 -31.637 1.00 58.78 ? 33 LEU A CD1 1 ATOM 257 C CD2 . LEU A 1 33 ? 41.159 -13.485 -32.867 1.00 59.72 ? 33 LEU A CD2 1 ATOM 258 N N . GLU A 1 34 ? 36.198 -14.374 -32.313 1.00 65.59 ? 34 GLU A N 1 ATOM 259 C CA . GLU A 1 34 ? 35.373 -13.357 -31.668 1.00 68.25 ? 34 GLU A CA 1 ATOM 260 C C . GLU A 1 34 ? 36.246 -12.403 -30.864 1.00 67.66 ? 34 GLU A C 1 ATOM 261 O O . GLU A 1 34 ? 36.990 -12.826 -29.980 1.00 67.29 ? 34 GLU A O 1 ATOM 262 C CB . GLU A 1 34 ? 34.330 -13.994 -30.751 1.00 69.97 ? 34 GLU A CB 1 ATOM 263 C CG . GLU A 1 34 ? 33.416 -12.984 -30.084 1.00 71.79 ? 34 GLU A CG 1 ATOM 264 C CD . GLU A 1 34 ? 32.802 -12.020 -31.078 1.00 74.93 ? 34 GLU A CD 1 ATOM 265 O OE1 . GLU A 1 34 ? 32.058 -12.474 -31.968 1.00 77.70 ? 34 GLU A OE1 1 ATOM 266 O OE2 . GLU A 1 34 ? 33.077 -10.809 -30.983 1.00 79.31 ? 34 GLU A OE2 1 ATOM 267 N N . LYS A 1 35 ? 36.139 -11.114 -31.174 1.00 68.69 ? 35 LYS A N 1 ATOM 268 C CA . LYS A 1 35 ? 36.981 -10.089 -30.561 1.00 68.94 ? 35 LYS A CA 1 ATOM 269 C C . LYS A 1 35 ? 36.221 -9.171 -29.596 1.00 68.67 ? 35 LYS A C 1 ATOM 270 O O . LYS A 1 35 ? 36.845 -8.445 -28.820 1.00 67.41 ? 35 LYS A O 1 ATOM 271 C CB . LYS A 1 35 ? 37.660 -9.252 -31.653 1.00 70.01 ? 35 LYS A CB 1 ATOM 272 C CG . LYS A 1 35 ? 38.908 -9.883 -32.244 1.00 69.44 ? 35 LYS A CG 1 ATOM 273 C CD . LYS A 1 35 ? 39.399 -9.121 -33.471 1.00 71.52 ? 35 LYS A CD 1 ATOM 274 C CE . LYS A 1 35 ? 39.109 -9.854 -34.776 1.00 73.32 ? 35 LYS A CE 1 ATOM 275 N NZ . LYS A 1 35 ? 37.681 -10.244 -34.980 1.00 73.98 ? 35 LYS A NZ 1 ATOM 276 N N . THR A 1 36 ? 34.891 -9.214 -29.627 1.00 68.74 ? 36 THR A N 1 ATOM 277 C CA . THR A 1 36 ? 34.082 -8.291 -28.839 1.00 74.07 ? 36 THR A CA 1 ATOM 278 C C . THR A 1 36 ? 33.348 -8.971 -27.691 1.00 76.58 ? 36 THR A C 1 ATOM 279 O O . THR A 1 36 ? 33.070 -10.170 -27.740 1.00 75.14 ? 36 THR A O 1 ATOM 280 C CB . THR A 1 36 ? 33.034 -7.578 -29.709 1.00 75.87 ? 36 THR A CB 1 ATOM 281 O OG1 . THR A 1 36 ? 32.021 -8.510 -30.099 1.00 77.31 ? 36 THR A OG1 1 ATOM 282 C CG2 . THR A 1 36 ? 33.683 -6.976 -30.947 1.00 75.79 ? 36 THR A CG2 1 ATOM 283 N N . HIS A 1 37 ? 33.047 -8.171 -26.665 1.00 77.58 ? 37 HIS A N 1 ATOM 284 C CA . HIS A 1 37 ? 32.233 -8.578 -25.521 1.00 78.36 ? 37 HIS A CA 1 ATOM 285 C C . HIS A 1 37 ? 31.372 -7.376 -25.095 1.00 81.07 ? 37 HIS A C 1 ATOM 286 O O . HIS A 1 37 ? 31.590 -6.263 -25.570 1.00 81.29 ? 37 HIS A O 1 ATOM 287 C CB . HIS A 1 37 ? 33.124 -9.058 -24.369 1.00 76.51 ? 37 HIS A CB 1 ATOM 288 C CG . HIS A 1 37 ? 34.060 -8.013 -23.842 1.00 78.14 ? 37 HIS A CG 1 ATOM 289 N ND1 . HIS A 1 37 ? 33.792 -7.282 -22.705 1.00 80.17 ? 37 HIS A ND1 1 ATOM 290 C CD2 . HIS A 1 37 ? 35.264 -7.583 -24.288 1.00 77.86 ? 37 HIS A CD2 1 ATOM 291 C CE1 . HIS A 1 37 ? 34.787 -6.446 -22.472 1.00 79.91 ? 37 HIS A CE1 1 ATOM 292 N NE2 . HIS A 1 37 ? 35.695 -6.609 -23.418 1.00 78.89 ? 37 HIS A NE2 1 ATOM 293 N N . ASN A 1 38 ? 30.396 -7.591 -24.218 1.00 81.53 ? 38 ASN A N 1 ATOM 294 C CA . ASN A 1 38 ? 29.481 -6.503 -23.831 1.00 83.79 ? 38 ASN A CA 1 ATOM 295 C C . ASN A 1 38 ? 29.917 -5.732 -22.570 1.00 84.73 ? 38 ASN A C 1 ATOM 296 O O . ASN A 1 38 ? 29.341 -4.698 -22.238 1.00 88.54 ? 38 ASN A O 1 ATOM 297 C CB . ASN A 1 38 ? 28.035 -7.016 -23.706 1.00 83.08 ? 38 ASN A CB 1 ATOM 298 C CG . ASN A 1 38 ? 27.791 -7.817 -22.441 1.00 82.07 ? 38 ASN A CG 1 ATOM 299 O OD1 . ASN A 1 38 ? 28.714 -8.106 -21.677 1.00 80.12 ? 38 ASN A OD1 1 ATOM 300 N ND2 . ASN A 1 38 ? 26.535 -8.182 -22.214 1.00 82.58 ? 38 ASN A ND2 1 ATOM 301 N N . GLY A 1 39 ? 30.914 -6.254 -21.864 1.00 84.37 ? 39 GLY A N 1 ATOM 302 C CA . GLY A 1 39 ? 31.562 -5.529 -20.764 1.00 84.62 ? 39 GLY A CA 1 ATOM 303 C C . GLY A 1 39 ? 30.802 -5.586 -19.452 1.00 86.59 ? 39 GLY A C 1 ATOM 304 O O . GLY A 1 39 ? 31.004 -4.741 -18.573 1.00 85.21 ? 39 GLY A O 1 ATOM 305 N N . LYS A 1 40 ? 29.939 -6.594 -19.322 1.00 87.73 ? 40 LYS A N 1 ATOM 306 C CA . LYS A 1 40 ? 29.002 -6.697 -18.209 1.00 86.84 ? 40 LYS A CA 1 ATOM 307 C C . LYS A 1 40 ? 28.980 -8.090 -17.599 1.00 85.49 ? 40 LYS A C 1 ATOM 308 O O . LYS A 1 40 ? 29.300 -9.075 -18.257 1.00 85.37 ? 40 LYS A O 1 ATOM 309 C CB . LYS A 1 40 ? 27.601 -6.353 -18.696 1.00 88.92 ? 40 LYS A CB 1 ATOM 310 C CG . LYS A 1 40 ? 27.430 -4.894 -19.071 1.00 91.98 ? 40 LYS A CG 1 ATOM 311 C CD . LYS A 1 40 ? 26.102 -4.639 -19.761 1.00 93.69 ? 40 LYS A CD 1 ATOM 312 C CE . LYS A 1 40 ? 26.009 -3.192 -20.210 1.00 96.62 ? 40 LYS A CE 1 ATOM 313 N NZ . LYS A 1 40 ? 24.841 -2.960 -21.100 1.00 100.75 ? 40 LYS A NZ 1 ATOM 314 N N . LEU A 1 41 ? 28.596 -8.159 -16.331 1.00 87.78 ? 41 LEU A N 1 ATOM 315 C CA . LEU A 1 41 ? 28.311 -9.430 -15.679 1.00 87.52 ? 41 LEU A CA 1 ATOM 316 C C . LEU A 1 41 ? 26.818 -9.712 -15.853 1.00 86.24 ? 41 LEU A C 1 ATOM 317 O O . LEU A 1 41 ? 25.986 -8.844 -15.584 1.00 85.53 ? 41 LEU A O 1 ATOM 318 C CB . LEU A 1 41 ? 28.707 -9.369 -14.203 1.00 88.85 ? 41 LEU A CB 1 ATOM 319 C CG . LEU A 1 41 ? 30.163 -8.941 -13.970 1.00 89.38 ? 41 LEU A CG 1 ATOM 320 C CD1 . LEU A 1 41 ? 30.465 -8.851 -12.484 1.00 89.81 ? 41 LEU A CD1 1 ATOM 321 C CD2 . LEU A 1 41 ? 31.138 -9.890 -14.661 1.00 88.03 ? 41 LEU A CD2 1 ATOM 322 N N . CYS A 1 42 ? 26.489 -10.913 -16.319 1.00 84.53 ? 42 CYS A N 1 ATOM 323 C CA . CYS A 1 42 ? 25.126 -11.225 -16.745 1.00 88.31 ? 42 CYS A CA 1 ATOM 324 C C . CYS A 1 42 ? 24.615 -12.519 -16.157 1.00 85.27 ? 42 CYS A C 1 ATOM 325 O O . CYS A 1 42 ? 25.390 -13.354 -15.688 1.00 81.91 ? 42 CYS A O 1 ATOM 326 C CB . CYS A 1 42 ? 25.058 -11.348 -18.273 1.00 91.36 ? 42 CYS A CB 1 ATOM 327 S SG . CYS A 1 42 ? 25.711 -9.931 -19.179 1.00 94.18 ? 42 CYS A SG 1 ATOM 328 N N . ASP A 1 43 ? 23.296 -12.682 -16.209 1.00 86.26 ? 43 ASP A N 1 ATOM 329 C CA . ASP A 1 43 ? 22.670 -13.961 -15.911 1.00 86.32 ? 43 ASP A CA 1 ATOM 330 C C . ASP A 1 43 ? 23.215 -14.979 -16.905 1.00 84.50 ? 43 ASP A C 1 ATOM 331 O O . ASP A 1 43 ? 23.374 -14.676 -18.089 1.00 82.57 ? 43 ASP A O 1 ATOM 332 C CB . ASP A 1 43 ? 21.139 -13.897 -16.055 1.00 89.41 ? 43 ASP A CB 1 ATOM 333 C CG . ASP A 1 43 ? 20.482 -12.875 -15.126 1.00 90.81 ? 43 ASP A CG 1 ATOM 334 O OD1 . ASP A 1 43 ? 21.028 -12.567 -14.049 1.00 89.92 ? 43 ASP A OD1 1 ATOM 335 O OD2 . ASP A 1 43 ? 19.393 -12.379 -15.483 1.00 93.38 ? 43 ASP A OD2 1 ATOM 336 N N . LEU A 1 44 ? 23.518 -16.173 -16.415 1.00 85.89 ? 44 LEU A N 1 ATOM 337 C CA . LEU A 1 44 ? 23.920 -17.281 -17.264 1.00 87.73 ? 44 LEU A CA 1 ATOM 338 C C . LEU A 1 44 ? 22.695 -18.163 -17.485 1.00 93.66 ? 44 LEU A C 1 ATOM 339 O O . LEU A 1 44 ? 22.176 -18.749 -16.536 1.00 95.16 ? 44 LEU A O 1 ATOM 340 C CB . LEU A 1 44 ? 25.042 -18.070 -16.589 1.00 86.51 ? 44 LEU A CB 1 ATOM 341 C CG . LEU A 1 44 ? 25.670 -19.240 -17.355 1.00 87.18 ? 44 LEU A CG 1 ATOM 342 C CD1 . LEU A 1 44 ? 26.263 -18.791 -18.685 1.00 86.66 ? 44 LEU A CD1 1 ATOM 343 C CD2 . LEU A 1 44 ? 26.734 -19.919 -16.505 1.00 85.19 ? 44 LEU A CD2 1 ATOM 344 N N . ASP A 1 45 ? 22.216 -18.234 -18.727 1.00 98.60 ? 45 ASP A N 1 ATOM 345 C CA . ASP A 1 45 ? 20.996 -18.987 -19.049 1.00 102.35 ? 45 ASP A CA 1 ATOM 346 C C . ASP A 1 45 ? 19.832 -18.609 -18.132 1.00 102.03 ? 45 ASP A C 1 ATOM 347 O O . ASP A 1 45 ? 19.095 -19.474 -17.661 1.00 101.54 ? 45 ASP A O 1 ATOM 348 C CB . ASP A 1 45 ? 21.264 -20.498 -18.979 1.00 105.66 ? 45 ASP A CB 1 ATOM 349 C CG . ASP A 1 45 ? 21.243 -21.154 -20.336 1.00 111.35 ? 45 ASP A CG 1 ATOM 350 O OD1 . ASP A 1 45 ? 22.155 -20.880 -21.155 1.00 110.66 ? 45 ASP A OD1 1 ATOM 351 O OD2 . ASP A 1 45 ? 20.307 -21.949 -20.578 1.00 118.55 ? 45 ASP A OD2 1 ATOM 352 N N . GLY A 1 46 ? 19.689 -17.313 -17.865 1.00 101.51 ? 46 GLY A N 1 ATOM 353 C CA . GLY A 1 46 ? 18.621 -16.805 -17.001 1.00 101.82 ? 46 GLY A CA 1 ATOM 354 C C . GLY A 1 46 ? 18.920 -16.847 -15.511 1.00 100.06 ? 46 GLY A C 1 ATOM 355 O O . GLY A 1 46 ? 18.320 -16.093 -14.748 1.00 101.61 ? 46 GLY A O 1 ATOM 356 N N . VAL A 1 47 ? 19.848 -17.713 -15.098 1.00 96.17 ? 47 VAL A N 1 ATOM 357 C CA . VAL A 1 47 ? 20.178 -17.912 -13.682 1.00 93.19 ? 47 VAL A CA 1 ATOM 358 C C . VAL A 1 47 ? 21.242 -16.916 -13.212 1.00 91.46 ? 47 VAL A C 1 ATOM 359 O O . VAL A 1 47 ? 22.417 -17.037 -13.553 1.00 89.25 ? 47 VAL A O 1 ATOM 360 C CB . VAL A 1 47 ? 20.682 -19.346 -13.429 1.00 91.01 ? 47 VAL A CB 1 ATOM 361 C CG1 . VAL A 1 47 ? 21.028 -19.542 -11.958 1.00 92.48 ? 47 VAL A CG1 1 ATOM 362 C CG2 . VAL A 1 47 ? 19.642 -20.362 -13.880 1.00 91.78 ? 47 VAL A CG2 1 ATOM 363 N N . LYS A 1 48 ? 20.814 -15.948 -12.411 1.00 93.57 ? 48 LYS A N 1 ATOM 364 C CA . LYS A 1 48 ? 21.671 -14.864 -11.917 1.00 93.99 ? 48 LYS A CA 1 ATOM 365 C C . LYS A 1 48 ? 22.873 -15.371 -11.104 1.00 90.56 ? 48 LYS A C 1 ATOM 366 O O . LYS A 1 48 ? 22.749 -16.352 -10.369 1.00 91.27 ? 48 LYS A O 1 ATOM 367 C CB . LYS A 1 48 ? 20.815 -13.929 -11.049 1.00 98.27 ? 48 LYS A CB 1 ATOM 368 C CG . LYS A 1 48 ? 21.480 -12.653 -10.554 1.00 100.71 ? 48 LYS A CG 1 ATOM 369 C CD . LYS A 1 48 ? 20.776 -12.129 -9.309 1.00 105.26 ? 48 LYS A CD 1 ATOM 370 C CE . LYS A 1 48 ? 21.449 -10.884 -8.756 1.00 106.94 ? 48 LYS A CE 1 ATOM 371 N NZ . LYS A 1 48 ? 21.223 -9.699 -9.628 1.00 109.98 ? 48 LYS A NZ 1 ATOM 372 N N . PRO A 1 49 ? 24.040 -14.703 -11.236 1.00 86.78 ? 49 PRO A N 1 ATOM 373 C CA . PRO A 1 49 ? 25.173 -15.046 -10.368 1.00 83.95 ? 49 PRO A CA 1 ATOM 374 C C . PRO A 1 49 ? 25.030 -14.478 -8.962 1.00 83.10 ? 49 PRO A C 1 ATOM 375 O O . PRO A 1 49 ? 24.224 -13.575 -8.736 1.00 84.14 ? 49 PRO A O 1 ATOM 376 C CB . PRO A 1 49 ? 26.364 -14.375 -11.060 1.00 79.83 ? 49 PRO A CB 1 ATOM 377 C CG . PRO A 1 49 ? 25.769 -13.193 -11.738 1.00 82.41 ? 49 PRO A CG 1 ATOM 378 C CD . PRO A 1 49 ? 24.403 -13.646 -12.203 1.00 85.29 ? 49 PRO A CD 1 ATOM 379 N N . LEU A 1 50 ? 25.823 -15.011 -8.038 1.00 80.10 ? 50 LEU A N 1 ATOM 380 C CA . LEU A 1 50 ? 25.969 -14.438 -6.711 1.00 79.78 ? 50 LEU A CA 1 ATOM 381 C C . LEU A 1 50 ? 27.075 -13.402 -6.775 1.00 79.76 ? 50 LEU A C 1 ATOM 382 O O . LEU A 1 50 ? 28.244 -13.755 -6.930 1.00 79.90 ? 50 LEU A O 1 ATOM 383 C CB . LEU A 1 50 ? 26.326 -15.526 -5.697 1.00 78.81 ? 50 LEU A CB 1 ATOM 384 C CG . LEU A 1 50 ? 26.671 -15.081 -4.273 1.00 79.77 ? 50 LEU A CG 1 ATOM 385 C CD1 . LEU A 1 50 ? 25.531 -14.299 -3.644 1.00 81.61 ? 50 LEU A CD1 1 ATOM 386 C CD2 . LEU A 1 50 ? 27.025 -16.285 -3.413 1.00 80.62 ? 50 LEU A CD2 1 ATOM 387 N N . ILE A 1 51 ? 26.713 -12.128 -6.678 1.00 82.14 ? 51 ILE A N 1 ATOM 388 C CA . ILE A 1 51 ? 27.701 -11.050 -6.718 1.00 82.82 ? 51 ILE A CA 1 ATOM 389 C C . ILE A 1 51 ? 27.953 -10.544 -5.301 1.00 83.97 ? 51 ILE A C 1 ATOM 390 O O . ILE A 1 51 ? 27.143 -9.803 -4.735 1.00 85.58 ? 51 ILE A O 1 ATOM 391 C CB . ILE A 1 51 ? 27.259 -9.906 -7.652 1.00 84.69 ? 51 ILE A CB 1 ATOM 392 C CG1 . ILE A 1 51 ? 26.900 -10.490 -9.024 1.00 85.46 ? 51 ILE A CG1 1 ATOM 393 C CG2 . ILE A 1 51 ? 28.358 -8.851 -7.769 1.00 84.31 ? 51 ILE A CG2 1 ATOM 394 C CD1 . ILE A 1 51 ? 26.836 -9.485 -10.154 1.00 87.42 ? 51 ILE A CD1 1 ATOM 395 N N . LEU A 1 52 ? 29.093 -10.945 -4.744 1.00 82.14 ? 52 LEU A N 1 ATOM 396 C CA . LEU A 1 52 ? 29.411 -10.678 -3.343 1.00 82.82 ? 52 LEU A CA 1 ATOM 397 C C . LEU A 1 52 ? 29.713 -9.210 -3.059 1.00 85.17 ? 52 LEU A C 1 ATOM 398 O O . LEU A 1 52 ? 29.751 -8.800 -1.897 1.00 86.37 ? 52 LEU A O 1 ATOM 399 C CB . LEU A 1 52 ? 30.583 -11.550 -2.889 1.00 80.39 ? 52 LEU A CB 1 ATOM 400 C CG . LEU A 1 52 ? 30.327 -13.061 -2.946 1.00 80.63 ? 52 LEU A CG 1 ATOM 401 C CD1 . LEU A 1 52 ? 31.588 -13.843 -2.601 1.00 79.09 ? 52 LEU A CD1 1 ATOM 402 C CD2 . LEU A 1 52 ? 29.175 -13.459 -2.028 1.00 82.94 ? 52 LEU A CD2 1 ATOM 403 N N . ARG A 1 53 ? 29.931 -8.428 -4.111 1.00 86.90 ? 53 ARG A N 1 ATOM 404 C CA . ARG A 1 53 ? 30.183 -7.003 -3.978 1.00 91.81 ? 53 ARG A CA 1 ATOM 405 C C . ARG A 1 53 ? 31.431 -6.763 -3.101 1.00 92.41 ? 53 ARG A C 1 ATOM 406 O O . ARG A 1 53 ? 32.514 -7.260 -3.434 1.00 95.23 ? 53 ARG A O 1 ATOM 407 C CB . ARG A 1 53 ? 28.927 -6.305 -3.453 1.00 97.67 ? 53 ARG A CB 1 ATOM 408 C CG . ARG A 1 53 ? 28.839 -4.837 -3.829 1.00 103.59 ? 53 ARG A CG 1 ATOM 409 C CD . ARG A 1 53 ? 27.782 -4.107 -3.016 1.00 110.13 ? 53 ARG A CD 1 ATOM 410 N NE . ARG A 1 53 ? 26.796 -3.451 -3.874 1.00 115.08 ? 53 ARG A NE 1 ATOM 411 C CZ . ARG A 1 53 ? 25.733 -4.051 -4.411 1.00 117.09 ? 53 ARG A CZ 1 ATOM 412 N NH1 . ARG A 1 53 ? 25.489 -5.343 -4.200 1.00 116.70 ? 53 ARG A NH1 1 ATOM 413 N NH2 . ARG A 1 53 ? 24.903 -3.352 -5.175 1.00 119.82 ? 53 ARG A NH2 1 ATOM 414 N N . ASP A 1 54 ? 31.292 -6.036 -1.992 1.00 92.97 ? 54 ASP A N 1 ATOM 415 C CA . ASP A 1 54 ? 32.417 -5.771 -1.087 1.00 92.88 ? 54 ASP A CA 1 ATOM 416 C C . ASP A 1 54 ? 32.695 -6.901 -0.087 1.00 90.98 ? 54 ASP A C 1 ATOM 417 O O . ASP A 1 54 ? 33.636 -6.800 0.698 1.00 93.00 ? 54 ASP A O 1 ATOM 418 C CB . ASP A 1 54 ? 32.182 -4.462 -0.316 1.00 95.36 ? 54 ASP A CB 1 ATOM 419 C CG . ASP A 1 54 ? 32.163 -3.238 -1.223 1.00 97.42 ? 54 ASP A CG 1 ATOM 420 O OD1 . ASP A 1 54 ? 32.959 -3.195 -2.193 1.00 94.94 ? 54 ASP A OD1 1 ATOM 421 O OD2 . ASP A 1 54 ? 31.357 -2.316 -0.956 1.00 98.00 ? 54 ASP A OD2 1 ATOM 422 N N . CYS A 1 55 ? 31.892 -7.964 -0.104 1.00 89.07 ? 55 CYS A N 1 ATOM 423 C CA . CYS A 1 55 ? 32.105 -9.095 0.805 1.00 88.15 ? 55 CYS A CA 1 ATOM 424 C C . CYS A 1 55 ? 32.965 -10.185 0.155 1.00 82.83 ? 55 CYS A C 1 ATOM 425 O O . CYS A 1 55 ? 32.980 -10.332 -1.061 1.00 82.62 ? 55 CYS A O 1 ATOM 426 C CB . CYS A 1 55 ? 30.765 -9.675 1.292 1.00 88.49 ? 55 CYS A CB 1 ATOM 427 S SG . CYS A 1 55 ? 29.796 -8.527 2.310 1.00 96.32 ? 55 CYS A SG 1 ATOM 428 N N . SER A 1 56 ? 33.694 -10.925 0.987 1.00 80.63 ? 56 SER A N 1 ATOM 429 C CA . SER A 1 56 ? 34.449 -12.093 0.557 1.00 78.85 ? 56 SER A CA 1 ATOM 430 C C . SER A 1 56 ? 33.633 -13.353 0.823 1.00 79.05 ? 56 SER A C 1 ATOM 431 O O . SER A 1 56 ? 32.559 -13.295 1.415 1.00 79.12 ? 56 SER A O 1 ATOM 432 C CB . SER A 1 56 ? 35.761 -12.185 1.332 1.00 78.45 ? 56 SER A CB 1 ATOM 433 O OG . SER A 1 56 ? 35.523 -12.630 2.659 1.00 78.56 ? 56 SER A OG 1 ATOM 434 N N . VAL A 1 57 ? 34.158 -14.498 0.402 1.00 78.83 ? 57 VAL A N 1 ATOM 435 C CA . VAL A 1 57 ? 33.490 -15.777 0.652 1.00 79.31 ? 57 VAL A CA 1 ATOM 436 C C . VAL A 1 57 ? 33.440 -16.054 2.163 1.00 79.31 ? 57 VAL A C 1 ATOM 437 O O . VAL A 1 57 ? 32.469 -16.620 2.663 1.00 80.91 ? 57 VAL A O 1 ATOM 438 C CB . VAL A 1 57 ? 34.181 -16.934 -0.111 1.00 77.53 ? 57 VAL A CB 1 ATOM 439 C CG1 . VAL A 1 57 ? 33.600 -18.281 0.284 1.00 78.07 ? 57 VAL A CG1 1 ATOM 440 C CG2 . VAL A 1 57 ? 34.047 -16.730 -1.615 1.00 77.65 ? 57 VAL A CG2 1 ATOM 441 N N . ALA A 1 58 ? 34.482 -15.636 2.880 1.00 77.29 ? 58 ALA A N 1 ATOM 442 C CA . ALA A 1 58 ? 34.542 -15.783 4.333 1.00 77.57 ? 58 ALA A CA 1 ATOM 443 C C . ALA A 1 58 ? 33.524 -14.879 5.040 1.00 79.28 ? 58 ALA A C 1 ATOM 444 O O . ALA A 1 58 ? 32.726 -15.351 5.857 1.00 78.96 ? 58 ALA A O 1 ATOM 445 C CB . ALA A 1 58 ? 35.943 -15.483 4.829 1.00 75.82 ? 58 ALA A CB 1 ATOM 446 N N . GLY A 1 59 ? 33.557 -13.586 4.721 1.00 79.22 ? 59 GLY A N 1 ATOM 447 C CA . GLY A 1 59 ? 32.587 -12.632 5.251 1.00 79.70 ? 59 GLY A CA 1 ATOM 448 C C . GLY A 1 59 ? 31.166 -13.116 5.018 1.00 81.81 ? 59 GLY A C 1 ATOM 449 O O . GLY A 1 59 ? 30.326 -13.060 5.917 1.00 85.73 ? 59 GLY A O 1 ATOM 450 N N . TRP A 1 60 ? 30.903 -13.607 3.811 1.00 79.57 ? 60 TRP A N 1 ATOM 451 C CA . TRP A 1 60 ? 29.602 -14.167 3.474 1.00 78.82 ? 60 TRP A CA 1 ATOM 452 C C . TRP A 1 60 ? 29.259 -15.356 4.367 1.00 80.20 ? 60 TRP A C 1 ATOM 453 O O . TRP A 1 60 ? 28.257 -15.329 5.082 1.00 83.91 ? 60 TRP A O 1 ATOM 454 C CB . TRP A 1 60 ? 29.568 -14.579 1.998 1.00 77.87 ? 60 TRP A CB 1 ATOM 455 C CG . TRP A 1 60 ? 28.434 -15.485 1.631 1.00 78.28 ? 60 TRP A CG 1 ATOM 456 C CD1 . TRP A 1 60 ? 27.155 -15.432 2.101 1.00 80.46 ? 60 TRP A CD1 1 ATOM 457 C CD2 . TRP A 1 60 ? 28.474 -16.569 0.697 1.00 76.54 ? 60 TRP A CD2 1 ATOM 458 N NE1 . TRP A 1 60 ? 26.400 -16.423 1.527 1.00 81.17 ? 60 TRP A NE1 1 ATOM 459 C CE2 . TRP A 1 60 ? 27.185 -17.135 0.661 1.00 78.80 ? 60 TRP A CE2 1 ATOM 460 C CE3 . TRP A 1 60 ? 29.474 -17.118 -0.109 1.00 74.56 ? 60 TRP A CE3 1 ATOM 461 C CZ2 . TRP A 1 60 ? 26.868 -18.224 -0.151 1.00 79.17 ? 60 TRP A CZ2 1 ATOM 462 C CZ3 . TRP A 1 60 ? 29.161 -18.203 -0.913 1.00 74.47 ? 60 TRP A CZ3 1 ATOM 463 C CH2 . TRP A 1 60 ? 27.867 -18.742 -0.931 1.00 76.30 ? 60 TRP A CH2 1 ATOM 464 N N . LEU A 1 61 ? 30.094 -16.389 4.331 1.00 78.99 ? 61 LEU A N 1 ATOM 465 C CA . LEU A 1 61 ? 29.761 -17.665 4.973 1.00 79.39 ? 61 LEU A CA 1 ATOM 466 C C . LEU A 1 61 ? 29.730 -17.593 6.501 1.00 79.78 ? 61 LEU A C 1 ATOM 467 O O . LEU A 1 61 ? 28.815 -18.126 7.133 1.00 79.98 ? 61 LEU A O 1 ATOM 468 C CB . LEU A 1 61 ? 30.721 -18.766 4.517 1.00 77.64 ? 61 LEU A CB 1 ATOM 469 C CG . LEU A 1 61 ? 30.559 -19.232 3.067 1.00 77.29 ? 61 LEU A CG 1 ATOM 470 C CD1 . LEU A 1 61 ? 31.653 -20.228 2.716 1.00 77.38 ? 61 LEU A CD1 1 ATOM 471 C CD2 . LEU A 1 61 ? 29.193 -19.851 2.823 1.00 78.82 ? 61 LEU A CD2 1 ATOM 472 N N . LEU A 1 62 ? 30.725 -16.936 7.087 1.00 79.73 ? 62 LEU A N 1 ATOM 473 C CA . LEU A 1 62 ? 30.751 -16.713 8.538 1.00 81.11 ? 62 LEU A CA 1 ATOM 474 C C . LEU A 1 62 ? 29.636 -15.780 9.017 1.00 82.84 ? 62 LEU A C 1 ATOM 475 O O . LEU A 1 62 ? 29.239 -15.844 10.179 1.00 85.02 ? 62 LEU A O 1 ATOM 476 C CB . LEU A 1 62 ? 32.106 -16.161 8.976 1.00 79.56 ? 62 LEU A CB 1 ATOM 477 C CG . LEU A 1 62 ? 33.236 -17.184 8.931 1.00 78.27 ? 62 LEU A CG 1 ATOM 478 C CD1 . LEU A 1 62 ? 34.581 -16.489 9.042 1.00 78.00 ? 62 LEU A CD1 1 ATOM 479 C CD2 . LEU A 1 62 ? 33.070 -18.220 10.034 1.00 79.58 ? 62 LEU A CD2 1 ATOM 480 N N . GLY A 1 63 ? 29.139 -14.923 8.125 1.00 82.95 ? 63 GLY A N 1 ATOM 481 C CA . GLY A 1 63 ? 28.059 -13.993 8.453 1.00 84.67 ? 63 GLY A CA 1 ATOM 482 C C . GLY A 1 63 ? 28.553 -12.677 9.030 1.00 85.39 ? 63 GLY A C 1 ATOM 483 O O . GLY A 1 63 ? 28.057 -12.226 10.060 1.00 85.77 ? 63 GLY A O 1 ATOM 484 N N . ASN A 1 64 ? 29.540 -12.070 8.369 1.00 84.70 ? 64 ASN A N 1 ATOM 485 C CA . ASN A 1 64 ? 30.007 -10.729 8.712 1.00 85.21 ? 64 ASN A CA 1 ATOM 486 C C . ASN A 1 64 ? 28.808 -9.785 8.723 1.00 88.52 ? 64 ASN A C 1 ATOM 487 O O . ASN A 1 64 ? 28.056 -9.754 7.750 1.00 88.97 ? 64 ASN A O 1 ATOM 488 C CB . ASN A 1 64 ? 31.050 -10.265 7.684 1.00 83.45 ? 64 ASN A CB 1 ATOM 489 C CG . ASN A 1 64 ? 31.640 -8.893 7.998 1.00 82.98 ? 64 ASN A CG 1 ATOM 490 O OD1 . ASN A 1 64 ? 30.929 -7.954 8.349 1.00 83.45 ? 64 ASN A OD1 1 ATOM 491 N ND2 . ASN A 1 64 ? 32.951 -8.769 7.839 1.00 82.01 ? 64 ASN A ND2 1 ATOM 492 N N . PRO A 1 65 ? 28.612 -9.027 9.824 1.00 92.39 ? 65 PRO A N 1 ATOM 493 C CA . PRO A 1 65 ? 27.451 -8.123 9.957 1.00 96.72 ? 65 PRO A CA 1 ATOM 494 C C . PRO A 1 65 ? 27.226 -7.179 8.768 1.00 98.53 ? 65 PRO A C 1 ATOM 495 O O . PRO A 1 65 ? 26.082 -6.848 8.458 1.00 101.82 ? 65 PRO A O 1 ATOM 496 C CB . PRO A 1 65 ? 27.775 -7.313 11.216 1.00 97.09 ? 65 PRO A CB 1 ATOM 497 C CG . PRO A 1 65 ? 28.676 -8.185 12.016 1.00 95.12 ? 65 PRO A CG 1 ATOM 498 C CD . PRO A 1 65 ? 29.449 -9.029 11.041 1.00 92.70 ? 65 PRO A CD 1 ATOM 499 N N . MET A 1 66 ? 28.309 -6.759 8.118 1.00 98.23 ? 66 MET A N 1 ATOM 500 C CA . MET A 1 66 ? 28.235 -5.924 6.914 1.00 100.38 ? 66 MET A CA 1 ATOM 501 C C . MET A 1 66 ? 27.780 -6.694 5.660 1.00 98.49 ? 66 MET A C 1 ATOM 502 O O . MET A 1 66 ? 27.624 -6.095 4.596 1.00 97.87 ? 66 MET A O 1 ATOM 503 C CB . MET A 1 66 ? 29.606 -5.293 6.633 1.00 101.10 ? 66 MET A CB 1 ATOM 504 C CG . MET A 1 66 ? 30.106 -4.335 7.706 1.00 103.07 ? 66 MET A CG 1 ATOM 505 S SD . MET A 1 66 ? 29.404 -2.679 7.552 1.00 108.03 ? 66 MET A SD 1 ATOM 506 C CE . MET A 1 66 ? 30.414 -1.778 8.725 1.00 109.38 ? 66 MET A CE 1 ATOM 507 N N . CYS A 1 67 ? 27.576 -8.007 5.782 1.00 97.41 ? 67 CYS A N 1 ATOM 508 C CA . CYS A 1 67 ? 27.232 -8.868 4.643 1.00 96.18 ? 67 CYS A CA 1 ATOM 509 C C . CYS A 1 67 ? 25.842 -9.491 4.791 1.00 97.75 ? 67 CYS A C 1 ATOM 510 O O . CYS A 1 67 ? 25.609 -10.632 4.374 1.00 96.20 ? 67 CYS A O 1 ATOM 511 C CB . CYS A 1 67 ? 28.292 -9.957 4.493 1.00 92.64 ? 67 CYS A CB 1 ATOM 512 S SG . CYS A 1 67 ? 29.936 -9.269 4.209 1.00 92.07 ? 67 CYS A SG 1 ATOM 513 N N . ASP A 1 68 ? 24.923 -8.724 5.373 1.00 98.60 ? 68 ASP A N 1 ATOM 514 C CA . ASP A 1 68 ? 23.549 -9.173 5.576 1.00 99.79 ? 68 ASP A CA 1 ATOM 515 C C . ASP A 1 68 ? 22.787 -9.320 4.261 1.00 100.94 ? 68 ASP A C 1 ATOM 516 O O . ASP A 1 68 ? 21.833 -10.092 4.188 1.00 102.83 ? 68 ASP A O 1 ATOM 517 C CB . ASP A 1 68 ? 22.802 -8.215 6.512 1.00 101.53 ? 68 ASP A CB 1 ATOM 518 C CG . ASP A 1 68 ? 23.276 -8.314 7.951 1.00 100.90 ? 68 ASP A CG 1 ATOM 519 O OD1 . ASP A 1 68 ? 24.124 -9.178 8.249 1.00 100.83 ? 68 ASP A OD1 1 ATOM 520 O OD2 . ASP A 1 68 ? 22.804 -7.529 8.798 1.00 102.28 ? 68 ASP A OD2 1 ATOM 521 N N . GLU A 1 69 ? 23.205 -8.590 3.226 1.00 99.78 ? 69 GLU A N 1 ATOM 522 C CA . GLU A 1 69 ? 22.632 -8.749 1.887 1.00 99.85 ? 69 GLU A CA 1 ATOM 523 C C . GLU A 1 69 ? 22.596 -10.223 1.488 1.00 97.63 ? 69 GLU A C 1 ATOM 524 O O . GLU A 1 69 ? 21.674 -10.666 0.800 1.00 99.68 ? 69 GLU A O 1 ATOM 525 C CB . GLU A 1 69 ? 23.434 -7.954 0.848 1.00 99.74 ? 69 GLU A CB 1 ATOM 526 C CG . GLU A 1 69 ? 22.801 -7.907 -0.543 1.00 101.24 ? 69 GLU A CG 1 ATOM 527 C CD . GLU A 1 69 ? 23.690 -7.250 -1.593 1.00 101.13 ? 69 GLU A CD 1 ATOM 528 O OE1 . GLU A 1 69 ? 24.774 -6.734 -1.239 1.00 100.72 ? 69 GLU A OE1 1 ATOM 529 O OE2 . GLU A 1 69 ? 23.301 -7.250 -2.782 1.00 101.76 ? 69 GLU A OE2 1 ATOM 530 N N . PHE A 1 70 ? 23.594 -10.975 1.947 1.00 94.19 ? 70 PHE A N 1 ATOM 531 C CA . PHE A 1 70 ? 23.745 -12.384 1.606 1.00 92.21 ? 70 PHE A CA 1 ATOM 532 C C . PHE A 1 70 ? 23.376 -13.311 2.769 1.00 93.87 ? 70 PHE A C 1 ATOM 533 O O . PHE A 1 70 ? 23.947 -14.393 2.917 1.00 92.08 ? 70 PHE A O 1 ATOM 534 C CB . PHE A 1 70 ? 25.185 -12.629 1.145 1.00 88.90 ? 70 PHE A CB 1 ATOM 535 C CG . PHE A 1 70 ? 25.712 -11.550 0.234 1.00 87.15 ? 70 PHE A CG 1 ATOM 536 C CD1 . PHE A 1 70 ? 25.244 -11.437 -1.071 1.00 86.33 ? 70 PHE A CD1 1 ATOM 537 C CD2 . PHE A 1 70 ? 26.641 -10.626 0.691 1.00 86.07 ? 70 PHE A CD2 1 ATOM 538 C CE1 . PHE A 1 70 ? 25.712 -10.440 -1.908 1.00 85.62 ? 70 PHE A CE1 1 ATOM 539 C CE2 . PHE A 1 70 ? 27.113 -9.627 -0.143 1.00 86.08 ? 70 PHE A CE2 1 ATOM 540 C CZ . PHE A 1 70 ? 26.649 -9.534 -1.445 1.00 85.43 ? 70 PHE A CZ 1 ATOM 541 N N . ILE A 1 71 ? 22.409 -12.884 3.579 1.00 97.92 ? 71 ILE A N 1 ATOM 542 C CA . ILE A 1 71 ? 21.918 -13.682 4.707 1.00 101.15 ? 71 ILE A CA 1 ATOM 543 C C . ILE A 1 71 ? 21.283 -14.998 4.230 1.00 102.15 ? 71 ILE A C 1 ATOM 544 O O . ILE A 1 71 ? 21.491 -16.036 4.847 1.00 101.11 ? 71 ILE A O 1 ATOM 545 C CB . ILE A 1 71 ? 20.927 -12.868 5.595 1.00 105.28 ? 71 ILE A CB 1 ATOM 546 C CG1 . ILE A 1 71 ? 20.696 -13.548 6.954 1.00 106.23 ? 71 ILE A CG1 1 ATOM 547 C CG2 . ILE A 1 71 ? 19.600 -12.611 4.884 1.00 107.26 ? 71 ILE A CG2 1 ATOM 548 C CD1 . ILE A 1 71 ? 21.726 -13.185 8.007 1.00 104.53 ? 71 ILE A CD1 1 ATOM 549 N N . ASN A 1 72 ? 20.525 -14.951 3.132 1.00 104.50 ? 72 ASN A N 1 ATOM 550 C CA . ASN A 1 72 ? 19.930 -16.155 2.528 1.00 105.86 ? 72 ASN A CA 1 ATOM 551 C C . ASN A 1 72 ? 19.831 -16.021 1.009 1.00 103.55 ? 72 ASN A C 1 ATOM 552 O O . ASN A 1 72 ? 18.791 -15.648 0.464 1.00 107.42 ? 72 ASN A O 1 ATOM 553 C CB . ASN A 1 72 ? 18.550 -16.451 3.134 1.00 109.74 ? 72 ASN A CB 1 ATOM 554 C CG . ASN A 1 72 ? 18.637 -17.199 4.454 1.00 112.30 ? 72 ASN A CG 1 ATOM 555 O OD1 . ASN A 1 72 ? 19.414 -18.147 4.595 1.00 112.46 ? 72 ASN A OD1 1 ATOM 556 N ND2 . ASN A 1 72 ? 17.837 -16.780 5.428 1.00 115.29 ? 72 ASN A ND2 1 ATOM 557 N N . VAL A 1 73 ? 20.929 -16.332 0.333 1.00 99.40 ? 73 VAL A N 1 ATOM 558 C CA . VAL A 1 73 ? 21.019 -16.148 -1.115 1.00 96.87 ? 73 VAL A CA 1 ATOM 559 C C . VAL A 1 73 ? 20.393 -17.312 -1.878 1.00 95.71 ? 73 VAL A C 1 ATOM 560 O O . VAL A 1 73 ? 20.564 -18.469 -1.497 1.00 96.13 ? 73 VAL A O 1 ATOM 561 C CB . VAL A 1 73 ? 22.480 -15.981 -1.584 1.00 93.68 ? 73 VAL A CB 1 ATOM 562 C CG1 . VAL A 1 73 ? 23.134 -14.810 -0.866 1.00 92.73 ? 73 VAL A CG1 1 ATOM 563 C CG2 . VAL A 1 73 ? 23.283 -17.265 -1.381 1.00 92.76 ? 73 VAL A CG2 1 ATOM 564 N N . PRO A 1 74 ? 19.684 -17.010 -2.976 1.00 95.04 ? 74 PRO A N 1 ATOM 565 C CA . PRO A 1 74 ? 19.113 -18.073 -3.790 1.00 96.16 ? 74 PRO A CA 1 ATOM 566 C C . PRO A 1 74 ? 20.174 -18.768 -4.644 1.00 92.48 ? 74 PRO A C 1 ATOM 567 O O . PRO A 1 74 ? 21.346 -18.386 -4.617 1.00 88.68 ? 74 PRO A O 1 ATOM 568 C CB . PRO A 1 74 ? 18.116 -17.324 -4.679 1.00 98.16 ? 74 PRO A CB 1 ATOM 569 C CG . PRO A 1 74 ? 18.737 -15.983 -4.863 1.00 97.57 ? 74 PRO A CG 1 ATOM 570 C CD . PRO A 1 74 ? 19.470 -15.682 -3.580 1.00 96.20 ? 74 PRO A CD 1 ATOM 571 N N . GLU A 1 75 ? 19.743 -19.783 -5.387 1.00 92.81 ? 75 GLU A N 1 ATOM 572 C CA . GLU A 1 75 ? 20.595 -20.515 -6.313 1.00 92.07 ? 75 GLU A CA 1 ATOM 573 C C . GLU A 1 75 ? 21.359 -19.557 -7.234 1.00 90.17 ? 75 GLU A C 1 ATOM 574 O O . GLU A 1 75 ? 20.809 -18.561 -7.702 1.00 89.29 ? 75 GLU A O 1 ATOM 575 C CB . GLU A 1 75 ? 19.735 -21.471 -7.143 1.00 95.61 ? 75 GLU A CB 1 ATOM 576 C CG . GLU A 1 75 ? 20.500 -22.383 -8.094 1.00 95.78 ? 75 GLU A CG 1 ATOM 577 C CD . GLU A 1 75 ? 19.576 -23.230 -8.954 1.00 99.21 ? 75 GLU A CD 1 ATOM 578 O OE1 . GLU A 1 75 ? 18.512 -23.657 -8.455 1.00 104.57 ? 75 GLU A OE1 1 ATOM 579 O OE2 . GLU A 1 75 ? 19.910 -23.465 -10.136 1.00 98.87 ? 75 GLU A OE2 1 ATOM 580 N N . TRP A 1 76 ? 22.632 -19.853 -7.476 1.00 88.10 ? 76 TRP A N 1 ATOM 581 C CA . TRP A 1 76 ? 23.442 -19.041 -8.382 1.00 87.92 ? 76 TRP A CA 1 ATOM 582 C C . TRP A 1 76 ? 24.011 -19.886 -9.519 1.00 87.18 ? 76 TRP A C 1 ATOM 583 O O . TRP A 1 76 ? 24.078 -21.114 -9.430 1.00 90.83 ? 76 TRP A O 1 ATOM 584 C CB . TRP A 1 76 ? 24.566 -18.330 -7.624 1.00 85.40 ? 76 TRP A CB 1 ATOM 585 C CG . TRP A 1 76 ? 25.535 -19.263 -6.976 1.00 84.87 ? 76 TRP A CG 1 ATOM 586 C CD1 . TRP A 1 76 ? 26.634 -19.831 -7.549 1.00 84.07 ? 76 TRP A CD1 1 ATOM 587 C CD2 . TRP A 1 76 ? 25.493 -19.738 -5.627 1.00 85.70 ? 76 TRP A CD2 1 ATOM 588 N NE1 . TRP A 1 76 ? 27.281 -20.634 -6.639 1.00 84.14 ? 76 TRP A NE1 1 ATOM 589 C CE2 . TRP A 1 76 ? 26.600 -20.594 -5.452 1.00 84.26 ? 76 TRP A CE2 1 ATOM 590 C CE3 . TRP A 1 76 ? 24.624 -19.527 -4.550 1.00 87.85 ? 76 TRP A CE3 1 ATOM 591 C CZ2 . TRP A 1 76 ? 26.861 -21.238 -4.244 1.00 85.66 ? 76 TRP A CZ2 1 ATOM 592 C CZ3 . TRP A 1 76 ? 24.884 -20.167 -3.348 1.00 87.23 ? 76 TRP A CZ3 1 ATOM 593 C CH2 . TRP A 1 76 ? 25.991 -21.013 -3.205 1.00 87.00 ? 76 TRP A CH2 1 ATOM 594 N N . SER A 1 77 ? 24.407 -19.209 -10.590 1.00 86.17 ? 77 SER A N 1 ATOM 595 C CA . SER A 1 77 ? 25.051 -19.845 -11.735 1.00 84.18 ? 77 SER A CA 1 ATOM 596 C C . SER A 1 77 ? 26.562 -19.839 -11.541 1.00 81.89 ? 77 SER A C 1 ATOM 597 O O . SER A 1 77 ? 27.232 -20.850 -11.739 1.00 81.70 ? 77 SER A O 1 ATOM 598 C CB . SER A 1 77 ? 24.696 -19.082 -13.005 1.00 83.80 ? 77 SER A CB 1 ATOM 599 O OG . SER A 1 77 ? 24.831 -17.685 -12.797 1.00 83.78 ? 77 SER A OG 1 ATOM 600 N N . TYR A 1 78 ? 27.090 -18.679 -11.166 1.00 79.76 ? 78 TYR A N 1 ATOM 601 C CA . TYR A 1 78 ? 28.499 -18.539 -10.815 1.00 76.29 ? 78 TYR A CA 1 ATOM 602 C C . TYR A 1 78 ? 28.622 -17.484 -9.727 1.00 75.58 ? 78 TYR A C 1 ATOM 603 O O . TYR A 1 78 ? 27.643 -16.816 -9.401 1.00 77.95 ? 78 TYR A O 1 ATOM 604 C CB . TYR A 1 78 ? 29.340 -18.168 -12.047 1.00 74.31 ? 78 TYR A CB 1 ATOM 605 C CG . TYR A 1 78 ? 28.938 -16.880 -12.747 1.00 73.70 ? 78 TYR A CG 1 ATOM 606 C CD1 . TYR A 1 78 ? 27.858 -16.842 -13.627 1.00 74.60 ? 78 TYR A CD1 1 ATOM 607 C CD2 . TYR A 1 78 ? 29.650 -15.705 -12.540 1.00 73.23 ? 78 TYR A CD2 1 ATOM 608 C CE1 . TYR A 1 78 ? 27.494 -15.666 -14.268 1.00 74.82 ? 78 TYR A CE1 1 ATOM 609 C CE2 . TYR A 1 78 ? 29.293 -14.527 -13.175 1.00 73.13 ? 78 TYR A CE2 1 ATOM 610 C CZ . TYR A 1 78 ? 28.218 -14.509 -14.038 1.00 73.64 ? 78 TYR A CZ 1 ATOM 611 O OH . TYR A 1 78 ? 27.877 -13.326 -14.659 1.00 73.49 ? 78 TYR A OH 1 ATOM 612 N N . ILE A 1 79 ? 29.817 -17.343 -9.165 1.00 73.27 ? 79 ILE A N 1 ATOM 613 C CA . ILE A 1 79 ? 30.044 -16.412 -8.063 1.00 75.02 ? 79 ILE A CA 1 ATOM 614 C C . ILE A 1 79 ? 31.050 -15.357 -8.491 1.00 75.53 ? 79 ILE A C 1 ATOM 615 O O . ILE A 1 79 ? 32.021 -15.668 -9.180 1.00 75.30 ? 79 ILE A O 1 ATOM 616 C CB . ILE A 1 79 ? 30.560 -17.154 -6.812 1.00 75.17 ? 79 ILE A CB 1 ATOM 617 C CG1 . ILE A 1 79 ? 29.469 -18.077 -6.263 1.00 77.30 ? 79 ILE A CG1 1 ATOM 618 C CG2 . ILE A 1 79 ? 31.002 -16.173 -5.732 1.00 76.01 ? 79 ILE A CG2 1 ATOM 619 C CD1 . ILE A 1 79 ? 29.962 -19.044 -5.208 1.00 78.32 ? 79 ILE A CD1 1 ATOM 620 N N . VAL A 1 80 ? 30.823 -14.112 -8.077 1.00 77.13 ? 80 VAL A N 1 ATOM 621 C CA . VAL A 1 80 ? 31.742 -13.024 -8.403 1.00 78.03 ? 80 VAL A CA 1 ATOM 622 C C . VAL A 1 80 ? 32.263 -12.358 -7.135 1.00 79.15 ? 80 VAL A C 1 ATOM 623 O O . VAL A 1 80 ? 31.482 -11.918 -6.292 1.00 81.39 ? 80 VAL A O 1 ATOM 624 C CB . VAL A 1 80 ? 31.081 -11.964 -9.305 1.00 78.93 ? 80 VAL A CB 1 ATOM 625 C CG1 . VAL A 1 80 ? 32.078 -10.860 -9.652 1.00 78.24 ? 80 VAL A CG1 1 ATOM 626 C CG2 . VAL A 1 80 ? 30.529 -12.621 -10.563 1.00 78.58 ? 80 VAL A CG2 1 ATOM 627 N N . GLU A 1 81 ? 33.588 -12.275 -7.033 1.00 77.10 ? 81 GLU A N 1 ATOM 628 C CA . GLU A 1 81 ? 34.264 -11.744 -5.865 1.00 77.99 ? 81 GLU A CA 1 ATOM 629 C C . GLU A 1 81 ? 35.347 -10.783 -6.316 1.00 77.81 ? 81 GLU A C 1 ATOM 630 O O . GLU A 1 81 ? 36.085 -11.075 -7.246 1.00 76.43 ? 81 GLU A O 1 ATOM 631 C CB . GLU A 1 81 ? 34.903 -12.888 -5.076 1.00 80.05 ? 81 GLU A CB 1 ATOM 632 C CG . GLU A 1 81 ? 35.536 -12.470 -3.756 1.00 83.15 ? 81 GLU A CG 1 ATOM 633 C CD . GLU A 1 81 ? 36.309 -13.593 -3.083 1.00 84.53 ? 81 GLU A CD 1 ATOM 634 O OE1 . GLU A 1 81 ? 37.143 -14.237 -3.757 1.00 81.50 ? 81 GLU A OE1 1 ATOM 635 O OE2 . GLU A 1 81 ? 36.081 -13.827 -1.873 1.00 88.07 ? 81 GLU A OE2 1 ATOM 636 N N . LYS A 1 82 ? 35.455 -9.643 -5.648 1.00 81.35 ? 82 LYS A N 1 ATOM 637 C CA . LYS A 1 82 ? 36.527 -8.695 -5.945 1.00 82.16 ? 82 LYS A CA 1 ATOM 638 C C . LYS A 1 82 ? 37.908 -9.257 -5.586 1.00 80.16 ? 82 LYS A C 1 ATOM 639 O O . LYS A 1 82 ? 38.029 -10.286 -4.914 1.00 77.26 ? 82 LYS A O 1 ATOM 640 C CB . LYS A 1 82 ? 36.281 -7.364 -5.223 1.00 84.54 ? 82 LYS A CB 1 ATOM 641 C CG . LYS A 1 82 ? 35.092 -6.589 -5.769 1.00 85.60 ? 82 LYS A CG 1 ATOM 642 C CD . LYS A 1 82 ? 34.976 -5.216 -5.126 1.00 87.88 ? 82 LYS A CD 1 ATOM 643 C CE . LYS A 1 82 ? 34.076 -4.287 -5.926 1.00 90.62 ? 82 LYS A CE 1 ATOM 644 N NZ . LYS A 1 82 ? 32.727 -4.866 -6.174 1.00 92.27 ? 82 LYS A NZ 1 ATOM 645 N N . ALA A 1 83 ? 38.945 -8.578 -6.064 1.00 82.75 ? 83 ALA A N 1 ATOM 646 C CA . ALA A 1 83 ? 40.328 -8.958 -5.780 1.00 82.48 ? 83 ALA A CA 1 ATOM 647 C C . ALA A 1 83 ? 40.673 -8.718 -4.304 1.00 85.50 ? 83 ALA A C 1 ATOM 648 O O . ALA A 1 83 ? 41.308 -9.559 -3.664 1.00 86.56 ? 83 ALA A O 1 ATOM 649 C CB . ALA A 1 83 ? 41.279 -8.189 -6.686 1.00 80.66 ? 83 ALA A CB 1 ATOM 650 N N . ASN A 1 84 ? 40.241 -7.578 -3.769 1.00 87.14 ? 84 ASN A N 1 ATOM 651 C CA . ASN A 1 84 ? 40.470 -7.247 -2.365 1.00 90.64 ? 84 ASN A CA 1 ATOM 652 C C . ASN A 1 84 ? 39.189 -6.767 -1.688 1.00 89.82 ? 84 ASN A C 1 ATOM 653 O O . ASN A 1 84 ? 39.055 -5.581 -1.388 1.00 88.77 ? 84 ASN A O 1 ATOM 654 C CB . ASN A 1 84 ? 41.560 -6.174 -2.247 1.00 95.85 ? 84 ASN A CB 1 ATOM 655 C CG . ASN A 1 84 ? 42.871 -6.603 -2.885 1.00 98.96 ? 84 ASN A CG 1 ATOM 656 O OD1 . ASN A 1 84 ? 43.582 -7.457 -2.352 1.00 101.07 ? 84 ASN A OD1 1 ATOM 657 N ND2 . ASN A 1 84 ? 43.196 -6.013 -4.033 1.00 100.47 ? 84 ASN A ND2 1 ATOM 658 N N . PRO A 1 85 ? 38.240 -7.690 -1.437 1.00 89.88 ? 85 PRO A N 1 ATOM 659 C CA . PRO A 1 85 ? 36.996 -7.274 -0.787 1.00 91.56 ? 85 PRO A CA 1 ATOM 660 C C . PRO A 1 85 ? 37.292 -6.715 0.595 1.00 92.47 ? 85 PRO A C 1 ATOM 661 O O . PRO A 1 85 ? 38.085 -7.308 1.327 1.00 92.49 ? 85 PRO A O 1 ATOM 662 C CB . PRO A 1 85 ? 36.181 -8.575 -0.690 1.00 90.48 ? 85 PRO A CB 1 ATOM 663 C CG . PRO A 1 85 ? 36.850 -9.546 -1.603 1.00 87.21 ? 85 PRO A CG 1 ATOM 664 C CD . PRO A 1 85 ? 38.292 -9.150 -1.627 1.00 87.29 ? 85 PRO A CD 1 ATOM 665 N N . VAL A 1 86 ? 36.680 -5.584 0.939 1.00 94.11 ? 86 VAL A N 1 ATOM 666 C CA . VAL A 1 86 ? 36.978 -4.917 2.214 1.00 95.20 ? 86 VAL A CA 1 ATOM 667 C C . VAL A 1 86 ? 36.319 -5.613 3.409 1.00 94.15 ? 86 VAL A C 1 ATOM 668 O O . VAL A 1 86 ? 36.891 -5.638 4.500 1.00 95.36 ? 86 VAL A O 1 ATOM 669 C CB . VAL A 1 86 ? 36.595 -3.415 2.203 1.00 98.08 ? 86 VAL A CB 1 ATOM 670 C CG1 . VAL A 1 86 ? 37.235 -2.712 1.012 1.00 98.12 ? 86 VAL A CG1 1 ATOM 671 C CG2 . VAL A 1 86 ? 35.081 -3.221 2.206 1.00 99.60 ? 86 VAL A CG2 1 ATOM 672 N N . ASN A 1 87 ? 35.128 -6.173 3.198 1.00 91.09 ? 87 ASN A N 1 ATOM 673 C CA . ASN A 1 87 ? 34.402 -6.874 4.253 1.00 90.63 ? 87 ASN A CA 1 ATOM 674 C C . ASN A 1 87 ? 34.739 -8.357 4.255 1.00 88.82 ? 87 ASN A C 1 ATOM 675 O O . ASN A 1 87 ? 33.980 -9.189 3.753 1.00 88.53 ? 87 ASN A O 1 ATOM 676 C CB . ASN A 1 87 ? 32.894 -6.674 4.101 1.00 92.51 ? 87 ASN A CB 1 ATOM 677 C CG . ASN A 1 87 ? 32.462 -5.249 4.384 1.00 95.30 ? 87 ASN A CG 1 ATOM 678 O OD1 . ASN A 1 87 ? 32.939 -4.612 5.328 1.00 96.17 ? 87 ASN A OD1 1 ATOM 679 N ND2 . ASN A 1 87 ? 31.543 -4.743 3.574 1.00 97.31 ? 87 ASN A ND2 1 ATOM 680 N N . ASP A 1 88 ? 35.896 -8.670 4.825 1.00 87.44 ? 88 ASP A N 1 ATOM 681 C CA . ASP A 1 88 ? 36.370 -10.038 4.953 1.00 84.85 ? 88 ASP A CA 1 ATOM 682 C C . ASP A 1 88 ? 36.149 -10.451 6.418 1.00 85.46 ? 88 ASP A C 1 ATOM 683 O O . ASP A 1 88 ? 35.014 -10.410 6.900 1.00 86.18 ? 88 ASP A O 1 ATOM 684 C CB . ASP A 1 88 ? 37.841 -10.112 4.502 1.00 82.90 ? 88 ASP A CB 1 ATOM 685 C CG . ASP A 1 88 ? 38.331 -11.539 4.273 1.00 81.93 ? 88 ASP A CG 1 ATOM 686 O OD1 . ASP A 1 88 ? 37.509 -12.471 4.197 1.00 79.93 ? 88 ASP A OD1 1 ATOM 687 O OD2 . ASP A 1 88 ? 39.560 -11.727 4.162 1.00 86.09 ? 88 ASP A OD2 1 ATOM 688 N N . LEU A 1 89 ? 37.211 -10.829 7.124 1.00 84.40 ? 89 LEU A N 1 ATOM 689 C CA . LEU A 1 89 ? 37.127 -11.146 8.543 1.00 84.56 ? 89 LEU A CA 1 ATOM 690 C C . LEU A 1 89 ? 37.189 -9.839 9.331 1.00 84.79 ? 89 LEU A C 1 ATOM 691 O O . LEU A 1 89 ? 38.261 -9.240 9.460 1.00 82.67 ? 89 LEU A O 1 ATOM 692 C CB . LEU A 1 89 ? 38.280 -12.073 8.952 1.00 83.80 ? 89 LEU A CB 1 ATOM 693 C CG . LEU A 1 89 ? 38.416 -13.380 8.155 1.00 82.24 ? 89 LEU A CG 1 ATOM 694 C CD1 . LEU A 1 89 ? 39.679 -14.124 8.567 1.00 81.00 ? 89 LEU A CD1 1 ATOM 695 C CD2 . LEU A 1 89 ? 37.186 -14.264 8.314 1.00 80.64 ? 89 LEU A CD2 1 ATOM 696 N N . CYS A 1 90 ? 36.039 -9.404 9.847 1.00 86.15 ? 90 CYS A N 1 ATOM 697 C CA . CYS A 1 90 ? 35.946 -8.136 10.569 1.00 87.28 ? 90 CYS A CA 1 ATOM 698 C C . CYS A 1 90 ? 36.827 -8.164 11.817 1.00 86.43 ? 90 CYS A C 1 ATOM 699 O O . CYS A 1 90 ? 37.626 -7.256 12.032 1.00 88.08 ? 90 CYS A O 1 ATOM 700 C CB . CYS A 1 90 ? 34.489 -7.794 10.910 1.00 91.14 ? 90 CYS A CB 1 ATOM 701 S SG . CYS A 1 90 ? 33.526 -9.076 11.759 1.00 94.28 ? 90 CYS A SG 1 ATOM 702 N N . TYR A 1 91 ? 36.688 -9.216 12.618 1.00 85.42 ? 91 TYR A N 1 ATOM 703 C CA . TYR A 1 91 ? 37.638 -9.517 13.688 1.00 85.72 ? 91 TYR A CA 1 ATOM 704 C C . TYR A 1 91 ? 38.810 -10.259 13.050 1.00 83.93 ? 91 TYR A C 1 ATOM 705 O O . TYR A 1 91 ? 38.606 -11.300 12.423 1.00 83.66 ? 91 TYR A O 1 ATOM 706 C CB . TYR A 1 91 ? 36.978 -10.392 14.762 1.00 87.94 ? 91 TYR A CB 1 ATOM 707 C CG . TYR A 1 91 ? 37.676 -10.377 16.112 1.00 90.64 ? 91 TYR A CG 1 ATOM 708 C CD1 . TYR A 1 91 ? 38.888 -11.037 16.302 1.00 90.34 ? 91 TYR A CD1 1 ATOM 709 C CD2 . TYR A 1 91 ? 37.118 -9.707 17.203 1.00 91.59 ? 91 TYR A CD2 1 ATOM 710 C CE1 . TYR A 1 91 ? 39.523 -11.029 17.532 1.00 90.72 ? 91 TYR A CE1 1 ATOM 711 C CE2 . TYR A 1 91 ? 37.747 -9.696 18.438 1.00 91.62 ? 91 TYR A CE2 1 ATOM 712 C CZ . TYR A 1 91 ? 38.950 -10.357 18.596 1.00 91.41 ? 91 TYR A CZ 1 ATOM 713 O OH . TYR A 1 91 ? 39.582 -10.351 19.817 1.00 91.72 ? 91 TYR A OH 1 ATOM 714 N N . PRO A 1 92 ? 40.043 -9.744 13.209 1.00 83.80 ? 92 PRO A N 1 ATOM 715 C CA . PRO A 1 92 ? 41.174 -10.339 12.496 1.00 81.68 ? 92 PRO A CA 1 ATOM 716 C C . PRO A 1 92 ? 41.452 -11.792 12.886 1.00 82.26 ? 92 PRO A C 1 ATOM 717 O O . PRO A 1 92 ? 41.136 -12.214 14.001 1.00 83.24 ? 92 PRO A O 1 ATOM 718 C CB . PRO A 1 92 ? 42.350 -9.451 12.908 1.00 82.79 ? 92 PRO A CB 1 ATOM 719 C CG . PRO A 1 92 ? 41.976 -8.961 14.264 1.00 85.17 ? 92 PRO A CG 1 ATOM 720 C CD . PRO A 1 92 ? 40.491 -8.733 14.186 1.00 85.94 ? 92 PRO A CD 1 ATOM 721 N N . GLY A 1 93 ? 42.042 -12.543 11.962 1.00 83.92 ? 93 GLY A N 1 ATOM 722 C CA . GLY A 1 93 ? 42.395 -13.936 12.209 1.00 84.62 ? 93 GLY A CA 1 ATOM 723 C C . GLY A 1 93 ? 42.756 -14.706 10.949 1.00 85.37 ? 93 GLY A C 1 ATOM 724 O O . GLY A 1 93 ? 43.336 -14.152 10.010 1.00 82.08 ? 93 GLY A O 1 ATOM 725 N N . ASP A 1 94 ? 42.425 -15.996 10.948 1.00 86.50 ? 94 ASP A N 1 ATOM 726 C CA . ASP A 1 94 ? 42.643 -16.868 9.799 1.00 86.89 ? 94 ASP A CA 1 ATOM 727 C C . ASP A 1 94 ? 41.400 -17.697 9.535 1.00 84.20 ? 94 ASP A C 1 ATOM 728 O O . ASP A 1 94 ? 40.561 -17.888 10.424 1.00 82.71 ? 94 ASP A O 1 ATOM 729 C CB . ASP A 1 94 ? 43.822 -17.808 10.049 1.00 89.65 ? 94 ASP A CB 1 ATOM 730 C CG . ASP A 1 94 ? 45.155 -17.097 9.998 1.00 94.21 ? 94 ASP A CG 1 ATOM 731 O OD1 . ASP A 1 94 ? 45.540 -16.633 8.903 1.00 98.32 ? 94 ASP A OD1 1 ATOM 732 O OD2 . ASP A 1 94 ? 45.826 -17.012 11.048 1.00 98.10 ? 94 ASP A OD2 1 ATOM 733 N N . PHE A 1 95 ? 41.291 -18.175 8.299 1.00 80.11 ? 95 PHE A N 1 ATOM 734 C CA . PHE A 1 95 ? 40.279 -19.143 7.921 1.00 77.52 ? 95 PHE A CA 1 ATOM 735 C C . PHE A 1 95 ? 41.036 -20.377 7.466 1.00 76.04 ? 95 PHE A C 1 ATOM 736 O O . PHE A 1 95 ? 41.732 -20.348 6.456 1.00 77.40 ? 95 PHE A O 1 ATOM 737 C CB . PHE A 1 95 ? 39.406 -18.585 6.802 1.00 76.40 ? 95 PHE A CB 1 ATOM 738 C CG . PHE A 1 95 ? 38.094 -19.295 6.638 1.00 76.83 ? 95 PHE A CG 1 ATOM 739 C CD1 . PHE A 1 95 ? 38.045 -20.605 6.188 1.00 77.98 ? 95 PHE A CD1 1 ATOM 740 C CD2 . PHE A 1 95 ? 36.906 -18.647 6.917 1.00 77.52 ? 95 PHE A CD2 1 ATOM 741 C CE1 . PHE A 1 95 ? 36.834 -21.254 6.022 1.00 78.52 ? 95 PHE A CE1 1 ATOM 742 C CE2 . PHE A 1 95 ? 35.692 -19.289 6.754 1.00 78.96 ? 95 PHE A CE2 1 ATOM 743 C CZ . PHE A 1 95 ? 35.655 -20.597 6.311 1.00 79.06 ? 95 PHE A CZ 1 ATOM 744 N N . ASN A 1 96 ? 40.921 -21.452 8.232 1.00 76.42 ? 96 ASN A N 1 ATOM 745 C CA . ASN A 1 96 ? 41.668 -22.670 7.962 1.00 76.03 ? 96 ASN A CA 1 ATOM 746 C C . ASN A 1 96 ? 41.171 -23.396 6.704 1.00 74.21 ? 96 ASN A C 1 ATOM 747 O O . ASN A 1 96 ? 39.960 -23.548 6.499 1.00 71.32 ? 96 ASN A O 1 ATOM 748 C CB . ASN A 1 96 ? 41.589 -23.597 9.178 1.00 79.41 ? 96 ASN A CB 1 ATOM 749 C CG . ASN A 1 96 ? 42.655 -24.669 9.159 1.00 81.98 ? 96 ASN A CG 1 ATOM 750 O OD1 . ASN A 1 96 ? 43.851 -24.374 9.253 1.00 82.43 ? 96 ASN A OD1 1 ATOM 751 N ND2 . ASN A 1 96 ? 42.230 -25.924 9.038 1.00 83.28 ? 96 ASN A ND2 1 ATOM 752 N N . ASP A 1 97 ? 42.119 -23.846 5.878 1.00 74.24 ? 97 ASP A N 1 ATOM 753 C CA . ASP A 1 97 ? 41.837 -24.505 4.591 1.00 73.50 ? 97 ASP A CA 1 ATOM 754 C C . ASP A 1 97 ? 40.836 -23.706 3.748 1.00 71.02 ? 97 ASP A C 1 ATOM 755 O O . ASP A 1 97 ? 39.893 -24.266 3.168 1.00 68.97 ? 97 ASP A O 1 ATOM 756 C CB . ASP A 1 97 ? 41.336 -25.943 4.813 1.00 77.38 ? 97 ASP A CB 1 ATOM 757 C CG . ASP A 1 97 ? 42.430 -26.886 5.292 1.00 79.46 ? 97 ASP A CG 1 ATOM 758 O OD1 . ASP A 1 97 ? 43.589 -26.731 4.862 1.00 79.61 ? 97 ASP A OD1 1 ATOM 759 O OD2 . ASP A 1 97 ? 42.124 -27.798 6.090 1.00 84.76 ? 97 ASP A OD2 1 ATOM 760 N N . TYR A 1 98 ? 41.049 -22.394 3.694 1.00 69.03 ? 98 TYR A N 1 ATOM 761 C CA . TYR A 1 98 ? 40.132 -21.481 3.013 1.00 68.77 ? 98 TYR A CA 1 ATOM 762 C C . TYR A 1 98 ? 40.045 -21.802 1.522 1.00 68.80 ? 98 TYR A C 1 ATOM 763 O O . TYR A 1 98 ? 38.953 -21.865 0.955 1.00 67.97 ? 98 TYR A O 1 ATOM 764 C CB . TYR A 1 98 ? 40.598 -20.038 3.222 1.00 67.94 ? 98 TYR A CB 1 ATOM 765 C CG . TYR A 1 98 ? 39.650 -18.956 2.737 1.00 68.66 ? 98 TYR A CG 1 ATOM 766 C CD1 . TYR A 1 98 ? 38.287 -19.023 2.999 1.00 70.12 ? 98 TYR A CD1 1 ATOM 767 C CD2 . TYR A 1 98 ? 40.132 -17.838 2.045 1.00 67.92 ? 98 TYR A CD2 1 ATOM 768 C CE1 . TYR A 1 98 ? 37.426 -18.027 2.567 1.00 71.13 ? 98 TYR A CE1 1 ATOM 769 C CE2 . TYR A 1 98 ? 39.281 -16.836 1.613 1.00 67.72 ? 98 TYR A CE2 1 ATOM 770 C CZ . TYR A 1 98 ? 37.928 -16.935 1.877 1.00 71.17 ? 98 TYR A CZ 1 ATOM 771 O OH . TYR A 1 98 ? 37.060 -15.948 1.464 1.00 73.57 ? 98 TYR A OH 1 ATOM 772 N N . GLU A 1 99 ? 41.202 -22.041 0.907 1.00 68.20 ? 99 GLU A N 1 ATOM 773 C CA . GLU A 1 99 ? 41.272 -22.287 -0.531 1.00 68.65 ? 99 GLU A CA 1 ATOM 774 C C . GLU A 1 99 ? 40.610 -23.608 -0.913 1.00 68.57 ? 99 GLU A C 1 ATOM 775 O O . GLU A 1 99 ? 39.918 -23.687 -1.928 1.00 66.95 ? 99 GLU A O 1 ATOM 776 C CB . GLU A 1 99 ? 42.723 -22.259 -1.021 1.00 69.48 ? 99 GLU A CB 1 ATOM 777 C CG . GLU A 1 99 ? 43.368 -20.871 -1.008 1.00 70.91 ? 99 GLU A CG 1 ATOM 778 C CD . GLU A 1 99 ? 43.726 -20.371 0.387 1.00 74.02 ? 99 GLU A CD 1 ATOM 779 O OE1 . GLU A 1 99 ? 44.031 -21.203 1.273 1.00 75.23 ? 99 GLU A OE1 1 ATOM 780 O OE2 . GLU A 1 99 ? 43.701 -19.140 0.599 1.00 75.79 ? 99 GLU A OE2 1 ATOM 781 N N . GLU A 1 100 ? 40.810 -24.638 -0.095 1.00 69.17 ? 100 GLU A N 1 ATOM 782 C CA . GLU A 1 100 ? 40.169 -25.931 -0.332 1.00 69.71 ? 100 GLU A CA 1 ATOM 783 C C . GLU A 1 100 ? 38.648 -25.829 -0.230 1.00 70.78 ? 100 GLU A C 1 ATOM 784 O O . GLU A 1 100 ? 37.930 -26.596 -0.876 1.00 73.78 ? 100 GLU A O 1 ATOM 785 C CB . GLU A 1 100 ? 40.700 -26.999 0.635 1.00 70.16 ? 100 GLU A CB 1 ATOM 786 C CG . GLU A 1 100 ? 42.032 -27.609 0.212 1.00 69.86 ? 100 GLU A CG 1 ATOM 787 C CD . GLU A 1 100 ? 41.907 -28.560 -0.968 1.00 70.60 ? 100 GLU A CD 1 ATOM 788 O OE1 . GLU A 1 100 ? 41.005 -29.431 -0.951 1.00 72.34 ? 100 GLU A OE1 1 ATOM 789 O OE2 . GLU A 1 100 ? 42.712 -28.444 -1.917 1.00 67.41 ? 100 GLU A OE2 1 ATOM 790 N N . LEU A 1 101 ? 38.158 -24.885 0.570 1.00 70.26 ? 101 LEU A N 1 ATOM 791 C CA . LEU A 1 101 ? 36.717 -24.672 0.693 1.00 70.74 ? 101 LEU A CA 1 ATOM 792 C C . LEU A 1 101 ? 36.194 -23.920 -0.520 1.00 69.48 ? 101 LEU A C 1 ATOM 793 O O . LEU A 1 101 ? 35.162 -24.290 -1.089 1.00 65.57 ? 101 LEU A O 1 ATOM 794 C CB . LEU A 1 101 ? 36.376 -23.909 1.977 1.00 71.44 ? 101 LEU A CB 1 ATOM 795 C CG . LEU A 1 101 ? 34.901 -23.577 2.207 1.00 72.10 ? 101 LEU A CG 1 ATOM 796 C CD1 . LEU A 1 101 ? 34.019 -24.819 2.171 1.00 72.82 ? 101 LEU A CD1 1 ATOM 797 C CD2 . LEU A 1 101 ? 34.763 -22.855 3.535 1.00 75.22 ? 101 LEU A CD2 1 ATOM 798 N N . LYS A 1 102 ? 36.904 -22.863 -0.913 1.00 69.53 ? 102 LYS A N 1 ATOM 799 C CA . LYS A 1 102 ? 36.541 -22.120 -2.119 1.00 70.43 ? 102 LYS A CA 1 ATOM 800 C C . LYS A 1 102 ? 36.491 -23.045 -3.331 1.00 69.66 ? 102 LYS A C 1 ATOM 801 O O . LYS A 1 102 ? 35.620 -22.903 -4.188 1.00 70.74 ? 102 LYS A O 1 ATOM 802 C CB . LYS A 1 102 ? 37.500 -20.963 -2.372 1.00 71.84 ? 102 LYS A CB 1 ATOM 803 C CG . LYS A 1 102 ? 37.366 -19.838 -1.360 1.00 76.00 ? 102 LYS A CG 1 ATOM 804 C CD . LYS A 1 102 ? 38.498 -18.818 -1.471 1.00 77.62 ? 102 LYS A CD 1 ATOM 805 C CE . LYS A 1 102 ? 38.133 -17.655 -2.384 1.00 79.39 ? 102 LYS A CE 1 ATOM 806 N NZ . LYS A 1 102 ? 39.157 -16.573 -2.352 1.00 79.45 ? 102 LYS A NZ 1 ATOM 807 N N . HIS A 1 103 ? 37.410 -24.005 -3.391 1.00 69.55 ? 103 HIS A N 1 ATOM 808 C CA . HIS A 1 103 ? 37.394 -24.992 -4.464 1.00 69.44 ? 103 HIS A CA 1 ATOM 809 C C . HIS A 1 103 ? 36.138 -25.859 -4.389 1.00 71.13 ? 103 HIS A C 1 ATOM 810 O O . HIS A 1 103 ? 35.552 -26.206 -5.410 1.00 69.81 ? 103 HIS A O 1 ATOM 811 C CB . HIS A 1 103 ? 38.633 -25.886 -4.413 1.00 69.42 ? 103 HIS A CB 1 ATOM 812 C CG . HIS A 1 103 ? 38.631 -26.960 -5.457 1.00 70.13 ? 103 HIS A CG 1 ATOM 813 N ND1 . HIS A 1 103 ? 39.174 -26.781 -6.712 1.00 69.00 ? 103 HIS A ND1 1 ATOM 814 C CD2 . HIS A 1 103 ? 38.121 -28.214 -5.443 1.00 70.33 ? 103 HIS A CD2 1 ATOM 815 C CE1 . HIS A 1 103 ? 39.009 -27.881 -7.422 1.00 67.78 ? 103 HIS A CE1 1 ATOM 816 N NE2 . HIS A 1 103 ? 38.372 -28.765 -6.676 1.00 69.87 ? 103 HIS A NE2 1 ATOM 817 N N . LEU A 1 104 ? 35.748 -26.213 -3.171 1.00 73.39 ? 104 LEU A N 1 ATOM 818 C CA . LEU A 1 104 ? 34.550 -27.015 -2.936 1.00 77.39 ? 104 LEU A CA 1 ATOM 819 C C . LEU A 1 104 ? 33.298 -26.304 -3.467 1.00 78.92 ? 104 LEU A C 1 ATOM 820 O O . LEU A 1 104 ? 32.379 -26.946 -3.973 1.00 79.63 ? 104 LEU A O 1 ATOM 821 C CB . LEU A 1 104 ? 34.405 -27.293 -1.433 1.00 79.35 ? 104 LEU A CB 1 ATOM 822 C CG . LEU A 1 104 ? 33.841 -28.643 -1.004 1.00 81.47 ? 104 LEU A CG 1 ATOM 823 C CD1 . LEU A 1 104 ? 34.773 -29.778 -1.397 1.00 82.16 ? 104 LEU A CD1 1 ATOM 824 C CD2 . LEU A 1 104 ? 33.619 -28.635 0.499 1.00 82.79 ? 104 LEU A CD2 1 ATOM 825 N N . LEU A 1 105 ? 33.289 -24.977 -3.348 1.00 80.92 ? 105 LEU A N 1 ATOM 826 C CA . LEU A 1 105 ? 32.181 -24.122 -3.800 1.00 80.73 ? 105 LEU A CA 1 ATOM 827 C C . LEU A 1 105 ? 31.970 -24.103 -5.296 1.00 80.46 ? 105 LEU A C 1 ATOM 828 O O . LEU A 1 105 ? 30.872 -23.807 -5.766 1.00 86.01 ? 105 LEU A O 1 ATOM 829 C CB . LEU A 1 105 ? 32.429 -22.672 -3.392 1.00 80.14 ? 105 LEU A CB 1 ATOM 830 C CG . LEU A 1 105 ? 31.878 -22.204 -2.066 1.00 80.46 ? 105 LEU A CG 1 ATOM 831 C CD1 . LEU A 1 105 ? 32.264 -20.746 -1.892 1.00 81.16 ? 105 LEU A CD1 1 ATOM 832 C CD2 . LEU A 1 105 ? 30.370 -22.391 -2.024 1.00 83.41 ? 105 LEU A CD2 1 ATOM 833 N N . SER A 1 106 ? 33.030 -24.368 -6.046 1.00 86.73 ? 106 SER A N 1 ATOM 834 C CA A SER A 1 106 ? 32.954 -24.369 -7.505 0.50 87.45 ? 106 SER A CA 1 ATOM 835 C CA B SER A 1 106 ? 32.950 -24.363 -7.498 0.50 87.18 ? 106 SER A CA 1 ATOM 836 C C . SER A 1 106 ? 32.126 -25.549 -8.002 1.00 88.99 ? 106 SER A C 1 ATOM 837 O O . SER A 1 106 ? 31.766 -25.607 -9.177 1.00 91.54 ? 106 SER A O 1 ATOM 838 C CB A SER A 1 106 ? 34.356 -24.391 -8.134 0.50 87.02 ? 106 SER A CB 1 ATOM 839 C CB B SER A 1 106 ? 34.360 -24.371 -8.088 0.50 86.47 ? 106 SER A CB 1 ATOM 840 O OG A SER A 1 106 ? 34.972 -25.665 -8.025 0.50 86.16 ? 106 SER A OG 1 ATOM 841 O OG B SER A 1 106 ? 35.158 -23.382 -7.451 0.50 83.34 ? 106 SER A OG 1 ATOM 842 N N . ARG A 1 107 ? 31.833 -26.490 -7.103 1.00 91.27 ? 107 ARG A N 1 ATOM 843 C CA . ARG A 1 107 ? 30.949 -27.622 -7.394 1.00 95.82 ? 107 ARG A CA 1 ATOM 844 C C . ARG A 1 107 ? 29.589 -27.455 -6.688 1.00 93.39 ? 107 ARG A C 1 ATOM 845 O O . ARG A 1 107 ? 28.857 -28.430 -6.509 1.00 93.86 ? 107 ARG A O 1 ATOM 846 C CB . ARG A 1 107 ? 31.611 -28.950 -6.978 1.00 99.83 ? 107 ARG A CB 1 ATOM 847 C CG . ARG A 1 107 ? 32.603 -29.525 -7.985 1.00 105.29 ? 107 ARG A CG 1 ATOM 848 C CD . ARG A 1 107 ? 33.996 -28.914 -7.861 1.00 109.03 ? 107 ARG A CD 1 ATOM 849 N NE . ARG A 1 107 ? 34.884 -29.326 -8.961 1.00 114.70 ? 107 ARG A NE 1 ATOM 850 C CZ . ARG A 1 107 ? 35.814 -30.287 -8.906 1.00 117.44 ? 107 ARG A CZ 1 ATOM 851 N NH1 . ARG A 1 107 ? 36.040 -30.989 -7.792 1.00 118.38 ? 107 ARG A NH1 1 ATOM 852 N NH2 . ARG A 1 107 ? 36.539 -30.553 -9.988 1.00 119.10 ? 107 ARG A NH2 1 ATOM 853 N N . ILE A 1 108 ? 29.255 -26.221 -6.297 1.00 90.44 ? 108 ILE A N 1 ATOM 854 C CA . ILE A 1 108 ? 28.015 -25.932 -5.561 1.00 89.55 ? 108 ILE A CA 1 ATOM 855 C C . ILE A 1 108 ? 27.264 -24.733 -6.153 1.00 88.34 ? 108 ILE A C 1 ATOM 856 O O . ILE A 1 108 ? 27.854 -23.677 -6.386 1.00 87.54 ? 108 ILE A O 1 ATOM 857 C CB . ILE A 1 108 ? 28.296 -25.643 -4.065 1.00 88.22 ? 108 ILE A CB 1 ATOM 858 C CG1 . ILE A 1 108 ? 28.935 -26.859 -3.387 1.00 88.41 ? 108 ILE A CG1 1 ATOM 859 C CG2 . ILE A 1 108 ? 27.011 -25.262 -3.338 1.00 87.92 ? 108 ILE A CG2 1 ATOM 860 C CD1 . ILE A 1 108 ? 29.366 -26.611 -1.954 1.00 87.51 ? 108 ILE A CD1 1 ATOM 861 N N . ASN A 1 109 ? 25.960 -24.901 -6.367 1.00 88.40 ? 109 ASN A N 1 ATOM 862 C CA . ASN A 1 109 ? 25.100 -23.831 -6.878 1.00 90.07 ? 109 ASN A CA 1 ATOM 863 C C . ASN A 1 109 ? 24.125 -23.256 -5.849 1.00 90.72 ? 109 ASN A C 1 ATOM 864 O O . ASN A 1 109 ? 23.595 -22.162 -6.058 1.00 89.74 ? 109 ASN A O 1 ATOM 865 C CB . ASN A 1 109 ? 24.295 -24.332 -8.077 1.00 93.00 ? 109 ASN A CB 1 ATOM 866 C CG . ASN A 1 109 ? 25.161 -24.608 -9.285 1.00 94.02 ? 109 ASN A CG 1 ATOM 867 O OD1 . ASN A 1 109 ? 25.857 -23.721 -9.779 1.00 92.84 ? 109 ASN A OD1 1 ATOM 868 N ND2 . ASN A 1 109 ? 25.118 -25.842 -9.774 1.00 97.10 ? 109 ASN A ND2 1 ATOM 869 N N . HIS A 1 110 ? 23.867 -23.981 -4.759 1.00 90.92 ? 110 HIS A N 1 ATOM 870 C CA . HIS A 1 110 ? 22.873 -23.533 -3.782 1.00 91.70 ? 110 HIS A CA 1 ATOM 871 C C . HIS A 1 110 ? 23.101 -24.060 -2.362 1.00 91.03 ? 110 HIS A C 1 ATOM 872 O O . HIS A 1 110 ? 23.317 -25.257 -2.147 1.00 90.49 ? 110 HIS A O 1 ATOM 873 C CB . HIS A 1 110 ? 21.466 -23.906 -4.263 1.00 94.77 ? 110 HIS A CB 1 ATOM 874 C CG . HIS A 1 110 ? 20.366 -23.220 -3.512 1.00 96.42 ? 110 HIS A CG 1 ATOM 875 N ND1 . HIS A 1 110 ? 19.121 -23.785 -3.338 1.00 98.20 ? 110 HIS A ND1 1 ATOM 876 C CD2 . HIS A 1 110 ? 20.327 -22.021 -2.883 1.00 95.85 ? 110 HIS A CD2 1 ATOM 877 C CE1 . HIS A 1 110 ? 18.360 -22.960 -2.642 1.00 98.85 ? 110 HIS A CE1 1 ATOM 878 N NE2 . HIS A 1 110 ? 19.068 -21.883 -2.352 1.00 96.67 ? 110 HIS A NE2 1 ATOM 879 N N . PHE A 1 111 ? 23.047 -23.137 -1.404 1.00 90.56 ? 111 PHE A N 1 ATOM 880 C CA . PHE A 1 111 ? 23.111 -23.455 0.014 1.00 91.31 ? 111 PHE A CA 1 ATOM 881 C C . PHE A 1 111 ? 21.758 -23.175 0.650 1.00 93.39 ? 111 PHE A C 1 ATOM 882 O O . PHE A 1 111 ? 21.058 -22.253 0.238 1.00 93.81 ? 111 PHE A O 1 ATOM 883 C CB . PHE A 1 111 ? 24.146 -22.578 0.730 1.00 88.89 ? 111 PHE A CB 1 ATOM 884 C CG . PHE A 1 111 ? 25.571 -23.062 0.623 1.00 87.34 ? 111 PHE A CG 1 ATOM 885 C CD1 . PHE A 1 111 ? 25.908 -24.392 0.848 1.00 87.45 ? 111 PHE A CD1 1 ATOM 886 C CD2 . PHE A 1 111 ? 26.592 -22.158 0.362 1.00 84.74 ? 111 PHE A CD2 1 ATOM 887 C CE1 . PHE A 1 111 ? 27.227 -24.809 0.777 1.00 85.32 ? 111 PHE A CE1 1 ATOM 888 C CE2 . PHE A 1 111 ? 27.908 -22.573 0.293 1.00 82.51 ? 111 PHE A CE2 1 ATOM 889 C CZ . PHE A 1 111 ? 28.227 -23.900 0.502 1.00 82.73 ? 111 PHE A CZ 1 ATOM 890 N N . GLU A 1 112 ? 21.410 -23.960 1.665 1.00 95.64 ? 112 GLU A N 1 ATOM 891 C CA . GLU A 1 112 ? 20.231 -23.704 2.494 1.00 99.02 ? 112 GLU A CA 1 ATOM 892 C C . GLU A 1 112 ? 20.671 -23.584 3.946 1.00 96.83 ? 112 GLU A C 1 ATOM 893 O O . GLU A 1 112 ? 21.066 -24.577 4.557 1.00 94.99 ? 112 GLU A O 1 ATOM 894 C CB . GLU A 1 112 ? 19.217 -24.840 2.352 1.00 102.33 ? 112 GLU A CB 1 ATOM 895 C CG . GLU A 1 112 ? 18.266 -24.693 1.173 1.00 106.10 ? 112 GLU A CG 1 ATOM 896 C CD . GLU A 1 112 ? 17.051 -23.833 1.474 1.00 108.71 ? 112 GLU A CD 1 ATOM 897 O OE1 . GLU A 1 112 ? 16.711 -23.655 2.666 1.00 108.76 ? 112 GLU A OE1 1 ATOM 898 O OE2 . GLU A 1 112 ? 16.425 -23.348 0.502 1.00 111.16 ? 112 GLU A OE2 1 ATOM 899 N N . LYS A 1 113 ? 20.611 -22.374 4.494 1.00 95.81 ? 113 LYS A N 1 ATOM 900 C CA . LYS A 1 113 ? 21.039 -22.144 5.873 1.00 97.18 ? 113 LYS A CA 1 ATOM 901 C C . LYS A 1 113 ? 20.020 -22.689 6.864 1.00 99.07 ? 113 LYS A C 1 ATOM 902 O O . LYS A 1 113 ? 18.825 -22.423 6.734 1.00 101.48 ? 113 LYS A O 1 ATOM 903 C CB . LYS A 1 113 ? 21.256 -20.656 6.129 1.00 97.43 ? 113 LYS A CB 1 ATOM 904 C CG . LYS A 1 113 ? 21.779 -20.350 7.522 1.00 98.90 ? 113 LYS A CG 1 ATOM 905 C CD . LYS A 1 113 ? 22.793 -19.216 7.513 1.00 99.47 ? 113 LYS A CD 1 ATOM 906 C CE . LYS A 1 113 ? 22.163 -17.883 7.154 1.00 100.59 ? 113 LYS A CE 1 ATOM 907 N NZ . LYS A 1 113 ? 23.182 -16.940 6.618 1.00 99.08 ? 113 LYS A NZ 1 ATOM 908 N N . ILE A 1 114 ? 20.491 -23.460 7.842 1.00 98.61 ? 114 ILE A N 1 ATOM 909 C CA . ILE A 1 114 ? 19.628 -23.931 8.926 1.00 101.93 ? 114 ILE A CA 1 ATOM 910 C C . ILE A 1 114 ? 20.311 -23.831 10.287 1.00 101.86 ? 114 ILE A C 1 ATOM 911 O O . ILE A 1 114 ? 21.541 -23.847 10.386 1.00 102.75 ? 114 ILE A O 1 ATOM 912 C CB . ILE A 1 114 ? 19.152 -25.382 8.708 1.00 103.54 ? 114 ILE A CB 1 ATOM 913 C CG1 . ILE A 1 114 ? 20.343 -26.336 8.575 1.00 103.55 ? 114 ILE A CG1 1 ATOM 914 C CG2 . ILE A 1 114 ? 18.255 -25.471 7.480 1.00 103.88 ? 114 ILE A CG2 1 ATOM 915 C CD1 . ILE A 1 114 ? 19.978 -27.774 8.868 1.00 106.03 ? 114 ILE A CD1 1 ATOM 916 N N . GLN A 1 115 ? 19.492 -23.739 11.329 1.00 102.68 ? 115 GLN A N 1 ATOM 917 C CA . GLN A 1 115 ? 19.969 -23.627 12.700 1.00 101.67 ? 115 GLN A CA 1 ATOM 918 C C . GLN A 1 115 ? 20.199 -25.019 13.285 1.00 100.82 ? 115 GLN A C 1 ATOM 919 O O . GLN A 1 115 ? 19.283 -25.842 13.302 1.00 100.97 ? 115 GLN A O 1 ATOM 920 C CB . GLN A 1 115 ? 18.942 -22.872 13.544 1.00 103.30 ? 115 GLN A CB 1 ATOM 921 C CG . GLN A 1 115 ? 19.470 -22.396 14.887 1.00 104.15 ? 115 GLN A CG 1 ATOM 922 C CD . GLN A 1 115 ? 18.381 -21.826 15.773 1.00 106.29 ? 115 GLN A CD 1 ATOM 923 O OE1 . GLN A 1 115 ? 18.461 -20.680 16.212 1.00 106.94 ? 115 GLN A OE1 1 ATOM 924 N NE2 . GLN A 1 115 ? 17.356 -22.624 16.040 1.00 107.57 ? 115 GLN A NE2 1 ATOM 925 N N . ILE A 1 116 ? 21.414 -25.273 13.766 1.00 98.62 ? 116 ILE A N 1 ATOM 926 C CA . ILE A 1 116 ? 21.752 -26.571 14.367 1.00 99.61 ? 116 ILE A CA 1 ATOM 927 C C . ILE A 1 116 ? 21.935 -26.497 15.887 1.00 101.59 ? 116 ILE A C 1 ATOM 928 O O . ILE A 1 116 ? 21.612 -27.454 16.592 1.00 104.49 ? 116 ILE A O 1 ATOM 929 C CB . ILE A 1 116 ? 22.994 -27.224 13.709 1.00 97.19 ? 116 ILE A CB 1 ATOM 930 C CG1 . ILE A 1 116 ? 24.183 -26.261 13.676 1.00 94.70 ? 116 ILE A CG1 1 ATOM 931 C CG2 . ILE A 1 116 ? 22.656 -27.690 12.299 1.00 96.31 ? 116 ILE A CG2 1 ATOM 932 C CD1 . ILE A 1 116 ? 25.488 -26.925 13.301 1.00 93.19 ? 116 ILE A CD1 1 ATOM 933 N N . ILE A 1 117 ? 22.449 -25.372 16.388 1.00 101.78 ? 117 ILE A N 1 ATOM 934 C CA . ILE A 1 117 ? 22.545 -25.132 17.834 1.00 103.20 ? 117 ILE A CA 1 ATOM 935 C C . ILE A 1 117 ? 21.988 -23.744 18.171 1.00 103.87 ? 117 ILE A C 1 ATOM 936 O O . ILE A 1 117 ? 22.676 -22.739 17.974 1.00 102.01 ? 117 ILE A O 1 ATOM 937 C CB . ILE A 1 117 ? 23.996 -25.255 18.349 1.00 102.19 ? 117 ILE A CB 1 ATOM 938 C CG1 . ILE A 1 117 ? 24.646 -26.534 17.808 1.00 100.33 ? 117 ILE A CG1 1 ATOM 939 C CG2 . ILE A 1 117 ? 24.017 -25.243 19.875 1.00 104.73 ? 117 ILE A CG2 1 ATOM 940 C CD1 . ILE A 1 117 ? 25.997 -26.851 18.413 1.00 99.78 ? 117 ILE A CD1 1 ATOM 941 N N . PRO A 1 118 ? 20.741 -23.685 18.686 1.00 106.98 ? 118 PRO A N 1 ATOM 942 C CA . PRO A 1 118 ? 20.099 -22.404 18.994 1.00 108.52 ? 118 PRO A CA 1 ATOM 943 C C . PRO A 1 118 ? 20.898 -21.536 19.962 1.00 109.48 ? 118 PRO A C 1 ATOM 944 O O . PRO A 1 118 ? 21.592 -22.052 20.839 1.00 108.87 ? 118 PRO A O 1 ATOM 945 C CB . PRO A 1 118 ? 18.768 -22.814 19.638 1.00 111.85 ? 118 PRO A CB 1 ATOM 946 C CG . PRO A 1 118 ? 18.506 -24.194 19.155 1.00 111.28 ? 118 PRO A CG 1 ATOM 947 C CD . PRO A 1 118 ? 19.855 -24.826 18.987 1.00 109.49 ? 118 PRO A CD 1 ATOM 948 N N . LYS A 1 119 ? 20.783 -20.225 19.793 1.00 111.08 ? 119 LYS A N 1 ATOM 949 C CA . LYS A 1 119 ? 21.476 -19.265 20.642 1.00 112.98 ? 119 LYS A CA 1 ATOM 950 C C . LYS A 1 119 ? 20.914 -19.284 22.063 1.00 116.22 ? 119 LYS A C 1 ATOM 951 O O . LYS A 1 119 ? 21.653 -19.123 23.036 1.00 117.74 ? 119 LYS A O 1 ATOM 952 C CB . LYS A 1 119 ? 21.346 -17.866 20.043 1.00 113.92 ? 119 LYS A CB 1 ATOM 953 C CG . LYS A 1 119 ? 22.316 -16.846 20.603 1.00 114.73 ? 119 LYS A CG 1 ATOM 954 C CD . LYS A 1 119 ? 22.277 -15.579 19.769 1.00 115.48 ? 119 LYS A CD 1 ATOM 955 C CE . LYS A 1 119 ? 23.321 -14.576 20.220 1.00 116.61 ? 119 LYS A CE 1 ATOM 956 N NZ . LYS A 1 119 ? 23.480 -13.484 19.220 1.00 116.87 ? 119 LYS A NZ 1 ATOM 957 N N . SER A 1 120 ? 19.603 -19.493 22.170 1.00 118.13 ? 120 SER A N 1 ATOM 958 C CA . SER A 1 120 ? 18.912 -19.540 23.459 1.00 119.08 ? 120 SER A CA 1 ATOM 959 C C . SER A 1 120 ? 19.292 -20.753 24.311 1.00 119.18 ? 120 SER A C 1 ATOM 960 O O . SER A 1 120 ? 19.196 -20.703 25.532 1.00 122.65 ? 120 SER A O 1 ATOM 961 C CB . SER A 1 120 ? 17.398 -19.549 23.236 1.00 120.36 ? 120 SER A CB 1 ATOM 962 O OG . SER A 1 120 ? 17.002 -20.691 22.494 1.00 119.38 ? 120 SER A OG 1 ATOM 963 N N . SER A 1 121 ? 19.729 -21.836 23.671 1.00 117.37 ? 121 SER A N 1 ATOM 964 C CA . SER A 1 121 ? 19.965 -23.102 24.373 1.00 117.52 ? 121 SER A CA 1 ATOM 965 C C . SER A 1 121 ? 21.250 -23.151 25.221 1.00 116.57 ? 121 SER A C 1 ATOM 966 O O . SER A 1 121 ? 21.540 -24.179 25.833 1.00 115.67 ? 121 SER A O 1 ATOM 967 C CB . SER A 1 121 ? 19.964 -24.257 23.367 1.00 115.28 ? 121 SER A CB 1 ATOM 968 O OG . SER A 1 121 ? 20.971 -24.075 22.390 1.00 112.04 ? 121 SER A OG 1 ATOM 969 N N . TRP A 1 122 ? 22.014 -22.060 25.257 1.00 115.41 ? 122 TRP A N 1 ATOM 970 C CA . TRP A 1 122 ? 23.228 -21.993 26.075 1.00 115.04 ? 122 TRP A CA 1 ATOM 971 C C . TRP A 1 122 ? 22.905 -21.485 27.478 1.00 118.61 ? 122 TRP A C 1 ATOM 972 O O . TRP A 1 122 ? 23.208 -20.342 27.822 1.00 120.21 ? 122 TRP A O 1 ATOM 973 C CB . TRP A 1 122 ? 24.268 -21.091 25.412 1.00 112.21 ? 122 TRP A CB 1 ATOM 974 C CG . TRP A 1 122 ? 24.784 -21.636 24.121 1.00 109.83 ? 122 TRP A CG 1 ATOM 975 C CD1 . TRP A 1 122 ? 24.547 -21.146 22.868 1.00 107.48 ? 122 TRP A CD1 1 ATOM 976 C CD2 . TRP A 1 122 ? 25.629 -22.779 23.952 1.00 108.36 ? 122 TRP A CD2 1 ATOM 977 N NE1 . TRP A 1 122 ? 25.195 -21.912 21.931 1.00 105.47 ? 122 TRP A NE1 1 ATOM 978 C CE2 . TRP A 1 122 ? 25.866 -22.921 22.567 1.00 105.42 ? 122 TRP A CE2 1 ATOM 979 C CE3 . TRP A 1 122 ? 26.209 -23.697 24.836 1.00 108.43 ? 122 TRP A CE3 1 ATOM 980 C CZ2 . TRP A 1 122 ? 26.660 -23.944 22.045 1.00 103.94 ? 122 TRP A CZ2 1 ATOM 981 C CZ3 . TRP A 1 122 ? 26.997 -24.714 24.318 1.00 106.99 ? 122 TRP A CZ3 1 ATOM 982 C CH2 . TRP A 1 122 ? 27.216 -24.828 22.933 1.00 105.41 ? 122 TRP A CH2 1 ATOM 983 N N . SER A 1 123 ? 22.304 -22.353 28.287 1.00 120.87 ? 123 SER A N 1 ATOM 984 C CA . SER A 1 123 ? 21.760 -21.964 29.592 1.00 124.51 ? 123 SER A CA 1 ATOM 985 C C . SER A 1 123 ? 22.801 -21.824 30.713 1.00 125.76 ? 123 SER A C 1 ATOM 986 O O . SER A 1 123 ? 22.491 -21.277 31.770 1.00 128.87 ? 123 SER A O 1 ATOM 987 C CB . SER A 1 123 ? 20.672 -22.957 30.022 1.00 126.73 ? 123 SER A CB 1 ATOM 988 O OG . SER A 1 123 ? 21.145 -24.291 29.975 1.00 125.02 ? 123 SER A OG 1 ATOM 989 N N . SER A 1 124 ? 24.018 -22.318 30.489 1.00 123.99 ? 124 SER A N 1 ATOM 990 C CA . SER A 1 124 ? 25.097 -22.246 31.486 1.00 123.90 ? 124 SER A CA 1 ATOM 991 C C . SER A 1 124 ? 26.204 -21.252 31.107 1.00 121.86 ? 124 SER A C 1 ATOM 992 O O . SER A 1 124 ? 27.164 -21.076 31.857 1.00 121.64 ? 124 SER A O 1 ATOM 993 C CB . SER A 1 124 ? 25.718 -23.631 31.676 1.00 123.45 ? 124 SER A CB 1 ATOM 994 O OG . SER A 1 124 ? 24.717 -24.626 31.789 1.00 124.43 ? 124 SER A OG 1 ATOM 995 N N . HIS A 1 125 ? 26.074 -20.620 29.942 1.00 120.16 ? 125 HIS A N 1 ATOM 996 C CA . HIS A 1 125 ? 27.084 -19.695 29.434 1.00 117.99 ? 125 HIS A CA 1 ATOM 997 C C . HIS A 1 125 ? 26.420 -18.440 28.878 1.00 119.02 ? 125 HIS A C 1 ATOM 998 O O . HIS A 1 125 ? 25.250 -18.463 28.488 1.00 118.67 ? 125 HIS A O 1 ATOM 999 C CB . HIS A 1 125 ? 27.910 -20.360 28.326 1.00 113.58 ? 125 HIS A CB 1 ATOM 1000 C CG . HIS A 1 125 ? 28.621 -21.607 28.754 1.00 112.39 ? 125 HIS A CG 1 ATOM 1001 N ND1 . HIS A 1 125 ? 28.042 -22.857 28.682 1.00 112.39 ? 125 HIS A ND1 1 ATOM 1002 C CD2 . HIS A 1 125 ? 29.870 -21.799 29.241 1.00 111.87 ? 125 HIS A CD2 1 ATOM 1003 C CE1 . HIS A 1 125 ? 28.900 -23.762 29.116 1.00 112.58 ? 125 HIS A CE1 1 ATOM 1004 N NE2 . HIS A 1 125 ? 30.018 -23.147 29.459 1.00 112.37 ? 125 HIS A NE2 1 ATOM 1005 N N . GLU A 1 126 ? 27.180 -17.349 28.829 1.00 119.77 ? 126 GLU A N 1 ATOM 1006 C CA . GLU A 1 126 ? 26.680 -16.081 28.307 1.00 120.03 ? 126 GLU A CA 1 ATOM 1007 C C . GLU A 1 126 ? 26.899 -15.992 26.795 1.00 116.66 ? 126 GLU A C 1 ATOM 1008 O O . GLU A 1 126 ? 28.030 -15.853 26.317 1.00 116.31 ? 126 GLU A O 1 ATOM 1009 C CB . GLU A 1 126 ? 27.357 -14.914 29.023 1.00 122.68 ? 126 GLU A CB 1 ATOM 1010 C CG . GLU A 1 126 ? 26.805 -13.543 28.662 1.00 124.64 ? 126 GLU A CG 1 ATOM 1011 C CD . GLU A 1 126 ? 25.315 -13.414 28.931 1.00 127.68 ? 126 GLU A CD 1 ATOM 1012 O OE1 . GLU A 1 126 ? 24.899 -13.551 30.105 1.00 126.48 ? 126 GLU A OE1 1 ATOM 1013 O OE2 . GLU A 1 126 ? 24.563 -13.174 27.958 1.00 128.76 ? 126 GLU A OE2 1 ATOM 1014 N N . ALA A 1 127 ? 25.802 -16.057 26.048 1.00 115.36 ? 127 ALA A N 1 ATOM 1015 C CA . ALA A 1 127 ? 25.855 -16.163 24.592 1.00 111.27 ? 127 ALA A CA 1 ATOM 1016 C C . ALA A 1 127 ? 25.537 -14.855 23.864 1.00 110.78 ? 127 ALA A C 1 ATOM 1017 O O . ALA A 1 127 ? 25.680 -14.781 22.640 1.00 108.40 ? 127 ALA A O 1 ATOM 1018 C CB . ALA A 1 127 ? 24.903 -17.256 24.131 1.00 110.41 ? 127 ALA A CB 1 ATOM 1019 N N . SER A 1 128 ? 25.117 -13.831 24.606 1.00 112.73 ? 128 SER A N 1 ATOM 1020 C CA . SER A 1 128 ? 24.657 -12.575 24.006 1.00 112.52 ? 128 SER A CA 1 ATOM 1021 C C . SER A 1 128 ? 25.604 -11.401 24.242 1.00 111.11 ? 128 SER A C 1 ATOM 1022 O O . SER A 1 128 ? 25.260 -10.260 23.938 1.00 110.47 ? 128 SER A O 1 ATOM 1023 C CB . SER A 1 128 ? 23.259 -12.239 24.525 1.00 116.76 ? 128 SER A CB 1 ATOM 1024 O OG . SER A 1 128 ? 22.297 -13.069 23.901 1.00 118.35 ? 128 SER A OG 1 ATOM 1025 N N . LEU A 1 129 ? 26.793 -11.684 24.768 1.00 109.96 ? 129 LEU A N 1 ATOM 1026 C CA . LEU A 1 129 ? 27.806 -10.656 24.984 1.00 110.22 ? 129 LEU A CA 1 ATOM 1027 C C . LEU A 1 129 ? 29.057 -10.927 24.155 1.00 107.16 ? 129 LEU A C 1 ATOM 1028 O O . LEU A 1 129 ? 30.116 -10.367 24.426 1.00 107.06 ? 129 LEU A O 1 ATOM 1029 C CB . LEU A 1 129 ? 28.164 -10.573 26.470 1.00 113.56 ? 129 LEU A CB 1 ATOM 1030 C CG . LEU A 1 129 ? 27.018 -10.248 27.437 1.00 117.07 ? 129 LEU A CG 1 ATOM 1031 C CD1 . LEU A 1 129 ? 27.552 -10.083 28.852 1.00 119.23 ? 129 LEU A CD1 1 ATOM 1032 C CD2 . LEU A 1 129 ? 26.259 -8.999 27.008 1.00 118.41 ? 129 LEU A CD2 1 ATOM 1033 N N . GLY A 1 130 ? 28.921 -11.767 23.130 1.00 104.95 ? 130 GLY A N 1 ATOM 1034 C CA . GLY A 1 130 ? 30.036 -12.127 22.261 1.00 101.56 ? 130 GLY A CA 1 ATOM 1035 C C . GLY A 1 130 ? 30.209 -11.201 21.068 1.00 99.72 ? 130 GLY A C 1 ATOM 1036 O O . GLY A 1 130 ? 30.085 -11.635 19.914 1.00 96.89 ? 130 GLY A O 1 ATOM 1037 N N . VAL A 1 131 ? 30.534 -9.938 21.354 1.00 99.77 ? 131 VAL A N 1 ATOM 1038 C CA . VAL A 1 131 ? 30.613 -8.876 20.341 1.00 97.78 ? 131 VAL A CA 1 ATOM 1039 C C . VAL A 1 131 ? 31.947 -8.117 20.375 1.00 97.27 ? 131 VAL A C 1 ATOM 1040 O O . VAL A 1 131 ? 32.760 -8.311 21.278 1.00 99.00 ? 131 VAL A O 1 ATOM 1041 C CB . VAL A 1 131 ? 29.453 -7.869 20.506 1.00 99.37 ? 131 VAL A CB 1 ATOM 1042 C CG1 . VAL A 1 131 ? 28.123 -8.548 20.220 1.00 98.82 ? 131 VAL A CG1 1 ATOM 1043 C CG2 . VAL A 1 131 ? 29.452 -7.249 21.901 1.00 101.98 ? 131 VAL A CG2 1 ATOM 1044 N N . SER A 1 132 ? 32.161 -7.256 19.380 1.00 95.90 ? 132 SER A N 1 ATOM 1045 C CA . SER A 1 132 ? 33.386 -6.457 19.283 1.00 94.45 ? 132 SER A CA 1 ATOM 1046 C C . SER A 1 132 ? 33.201 -5.205 18.432 1.00 94.84 ? 132 SER A C 1 ATOM 1047 O O . SER A 1 132 ? 32.383 -5.181 17.505 1.00 93.76 ? 132 SER A O 1 ATOM 1048 C CB . SER A 1 132 ? 34.526 -7.289 18.688 1.00 90.83 ? 132 SER A CB 1 ATOM 1049 O OG . SER A 1 132 ? 35.658 -6.479 18.409 1.00 88.93 ? 132 SER A OG 1 ATOM 1050 N N . SER A 1 133 ? 33.988 -4.176 18.750 1.00 95.77 ? 133 SER A N 1 ATOM 1051 C CA . SER A 1 133 ? 34.037 -2.947 17.960 1.00 95.85 ? 133 SER A CA 1 ATOM 1052 C C . SER A 1 133 ? 34.630 -3.184 16.562 1.00 93.37 ? 133 SER A C 1 ATOM 1053 O O . SER A 1 133 ? 34.411 -2.387 15.653 1.00 92.13 ? 133 SER A O 1 ATOM 1054 C CB . SER A 1 133 ? 34.847 -1.880 18.697 1.00 97.75 ? 133 SER A CB 1 ATOM 1055 O OG . SER A 1 133 ? 36.135 -2.367 19.034 1.00 97.15 ? 133 SER A OG 1 ATOM 1056 N N . ALA A 1 134 ? 35.376 -4.277 16.400 1.00 92.94 ? 134 ALA A N 1 ATOM 1057 C CA . ALA A 1 134 ? 35.908 -4.681 15.092 1.00 91.83 ? 134 ALA A CA 1 ATOM 1058 C C . ALA A 1 134 ? 34.822 -5.116 14.097 1.00 91.29 ? 134 ALA A C 1 ATOM 1059 O O . ALA A 1 134 ? 35.027 -5.037 12.883 1.00 88.00 ? 134 ALA A O 1 ATOM 1060 C CB . ALA A 1 134 ? 36.927 -5.798 15.266 1.00 90.82 ? 134 ALA A CB 1 ATOM 1061 N N . CYS A 1 135 ? 33.678 -5.571 14.612 1.00 93.95 ? 135 CYS A N 1 ATOM 1062 C CA . CYS A 1 135 ? 32.545 -5.988 13.780 1.00 93.72 ? 135 CYS A CA 1 ATOM 1063 C C . CYS A 1 135 ? 31.303 -5.139 14.071 1.00 93.32 ? 135 CYS A C 1 ATOM 1064 O O . CYS A 1 135 ? 30.364 -5.611 14.717 1.00 91.51 ? 135 CYS A O 1 ATOM 1065 C CB . CYS A 1 135 ? 32.235 -7.464 14.031 1.00 95.58 ? 135 CYS A CB 1 ATOM 1066 S SG . CYS A 1 135 ? 33.638 -8.563 13.752 1.00 97.57 ? 135 CYS A SG 1 ATOM 1067 N N . PRO A 1 136 ? 31.294 -3.880 13.589 1.00 92.46 ? 136 PRO A N 1 ATOM 1068 C CA . PRO A 1 136 ? 30.199 -2.960 13.886 1.00 94.26 ? 136 PRO A CA 1 ATOM 1069 C C . PRO A 1 136 ? 28.968 -3.168 13.004 1.00 93.98 ? 136 PRO A C 1 ATOM 1070 O O . PRO A 1 136 ? 29.098 -3.549 11.842 1.00 91.24 ? 136 PRO A O 1 ATOM 1071 C CB . PRO A 1 136 ? 30.818 -1.592 13.601 1.00 95.12 ? 136 PRO A CB 1 ATOM 1072 C CG . PRO A 1 136 ? 31.787 -1.861 12.502 1.00 92.28 ? 136 PRO A CG 1 ATOM 1073 C CD . PRO A 1 136 ? 32.337 -3.234 12.767 1.00 90.40 ? 136 PRO A CD 1 ATOM 1074 N N . TYR A 1 137 ? 27.789 -2.908 13.565 1.00 97.46 ? 137 TYR A N 1 ATOM 1075 C CA . TYR A 1 137 ? 26.528 -2.959 12.824 1.00 98.14 ? 137 TYR A CA 1 ATOM 1076 C C . TYR A 1 137 ? 25.603 -1.849 13.302 1.00 100.25 ? 137 TYR A C 1 ATOM 1077 O O . TYR A 1 137 ? 25.124 -1.885 14.435 1.00 102.69 ? 137 TYR A O 1 ATOM 1078 C CB . TYR A 1 137 ? 25.847 -4.314 13.016 1.00 98.48 ? 137 TYR A CB 1 ATOM 1079 C CG . TYR A 1 137 ? 24.502 -4.427 12.327 1.00 99.51 ? 137 TYR A CG 1 ATOM 1080 C CD1 . TYR A 1 137 ? 24.416 -4.517 10.936 1.00 98.77 ? 137 TYR A CD1 1 ATOM 1081 C CD2 . TYR A 1 137 ? 23.319 -4.450 13.063 1.00 100.80 ? 137 TYR A CD2 1 ATOM 1082 C CE1 . TYR A 1 137 ? 23.189 -4.625 10.301 1.00 99.37 ? 137 TYR A CE1 1 ATOM 1083 C CE2 . TYR A 1 137 ? 22.089 -4.557 12.436 1.00 102.04 ? 137 TYR A CE2 1 ATOM 1084 C CZ . TYR A 1 137 ? 22.030 -4.646 11.057 1.00 101.28 ? 137 TYR A CZ 1 ATOM 1085 O OH . TYR A 1 137 ? 20.812 -4.753 10.430 1.00 102.38 ? 137 TYR A OH 1 ATOM 1086 N N . GLN A 1 138 ? 25.357 -0.872 12.432 1.00 100.30 ? 138 GLN A N 1 ATOM 1087 C CA . GLN A 1 138 ? 24.558 0.302 12.773 1.00 103.66 ? 138 GLN A CA 1 ATOM 1088 C C . GLN A 1 138 ? 25.113 1.010 14.014 1.00 105.57 ? 138 GLN A C 1 ATOM 1089 O O . GLN A 1 138 ? 24.371 1.347 14.939 1.00 107.82 ? 138 GLN A O 1 ATOM 1090 C CB . GLN A 1 138 ? 23.088 -0.081 12.980 1.00 106.08 ? 138 GLN A CB 1 ATOM 1091 C CG . GLN A 1 138 ? 22.480 -0.851 11.817 1.00 105.42 ? 138 GLN A CG 1 ATOM 1092 C CD . GLN A 1 138 ? 20.996 -1.123 11.995 1.00 107.65 ? 138 GLN A CD 1 ATOM 1093 O OE1 . GLN A 1 138 ? 20.393 -0.732 12.992 1.00 109.78 ? 138 GLN A OE1 1 ATOM 1094 N NE2 . GLN A 1 138 ? 20.402 -1.801 11.023 1.00 107.89 ? 138 GLN A NE2 1 ATOM 1095 N N . GLY A 1 139 ? 26.430 1.211 14.029 1.00 104.37 ? 139 GLY A N 1 ATOM 1096 C CA . GLY A 1 139 ? 27.098 1.980 15.081 1.00 105.44 ? 139 GLY A CA 1 ATOM 1097 C C . GLY A 1 139 ? 27.401 1.239 16.372 1.00 104.63 ? 139 GLY A C 1 ATOM 1098 O O . GLY A 1 139 ? 28.045 1.795 17.263 1.00 104.76 ? 139 GLY A O 1 ATOM 1099 N N . LYS A 1 140 ? 26.955 -0.013 16.469 1.00 102.96 ? 140 LYS A N 1 ATOM 1100 C CA . LYS A 1 140 ? 27.075 -0.798 17.696 1.00 103.94 ? 140 LYS A CA 1 ATOM 1101 C C . LYS A 1 140 ? 27.953 -2.015 17.454 1.00 100.38 ? 140 LYS A C 1 ATOM 1102 O O . LYS A 1 140 ? 28.079 -2.473 16.322 1.00 97.68 ? 140 LYS A O 1 ATOM 1103 C CB . LYS A 1 140 ? 25.693 -1.262 18.165 1.00 106.12 ? 140 LYS A CB 1 ATOM 1104 C CG . LYS A 1 140 ? 24.689 -0.138 18.380 1.00 110.12 ? 140 LYS A CG 1 ATOM 1105 C CD . LYS A 1 140 ? 23.260 -0.603 18.126 1.00 111.67 ? 140 LYS A CD 1 ATOM 1106 C CE . LYS A 1 140 ? 22.288 0.567 18.050 1.00 114.66 ? 140 LYS A CE 1 ATOM 1107 N NZ . LYS A 1 140 ? 22.106 1.241 19.366 1.00 117.94 ? 140 LYS A NZ 1 ATOM 1108 N N . SER A 1 141 ? 28.540 -2.540 18.526 1.00 101.23 ? 141 SER A N 1 ATOM 1109 C CA . SER A 1 141 ? 29.403 -3.721 18.447 1.00 98.93 ? 141 SER A CA 1 ATOM 1110 C C . SER A 1 141 ? 28.594 -4.999 18.193 1.00 97.68 ? 141 SER A C 1 ATOM 1111 O O . SER A 1 141 ? 27.633 -5.292 18.907 1.00 99.36 ? 141 SER A O 1 ATOM 1112 C CB . SER A 1 141 ? 30.221 -3.864 19.733 1.00 100.30 ? 141 SER A CB 1 ATOM 1113 O OG . SER A 1 141 ? 31.132 -2.785 19.875 1.00 101.99 ? 141 SER A OG 1 ATOM 1114 N N . SER A 1 142 ? 28.995 -5.754 17.173 1.00 95.13 ? 142 SER A N 1 ATOM 1115 C CA . SER A 1 142 ? 28.289 -6.967 16.758 1.00 94.22 ? 142 SER A CA 1 ATOM 1116 C C . SER A 1 142 ? 29.310 -8.087 16.524 1.00 91.64 ? 142 SER A C 1 ATOM 1117 O O . SER A 1 142 ? 30.424 -8.018 17.045 1.00 90.63 ? 142 SER A O 1 ATOM 1118 C CB . SER A 1 142 ? 27.466 -6.674 15.496 1.00 94.44 ? 142 SER A CB 1 ATOM 1119 O OG . SER A 1 142 ? 26.680 -7.786 15.111 1.00 94.80 ? 142 SER A OG 1 ATOM 1120 N N . PHE A 1 143 ? 28.935 -9.117 15.762 1.00 90.02 ? 143 PHE A N 1 ATOM 1121 C CA . PHE A 1 143 ? 29.830 -10.248 15.490 1.00 88.05 ? 143 PHE A CA 1 ATOM 1122 C C . PHE A 1 143 ? 29.304 -11.116 14.355 1.00 87.89 ? 143 PHE A C 1 ATOM 1123 O O . PHE A 1 143 ? 28.139 -11.011 13.974 1.00 89.32 ? 143 PHE A O 1 ATOM 1124 C CB . PHE A 1 143 ? 29.999 -11.111 16.746 1.00 88.67 ? 143 PHE A CB 1 ATOM 1125 C CG . PHE A 1 143 ? 31.216 -12.005 16.724 1.00 86.54 ? 143 PHE A CG 1 ATOM 1126 C CD1 . PHE A 1 143 ? 32.496 -11.461 16.699 1.00 84.76 ? 143 PHE A CD1 1 ATOM 1127 C CD2 . PHE A 1 143 ? 31.083 -13.390 16.754 1.00 85.14 ? 143 PHE A CD2 1 ATOM 1128 C CE1 . PHE A 1 143 ? 33.616 -12.278 16.695 1.00 83.60 ? 143 PHE A CE1 1 ATOM 1129 C CE2 . PHE A 1 143 ? 32.202 -14.211 16.750 1.00 83.77 ? 143 PHE A CE2 1 ATOM 1130 C CZ . PHE A 1 143 ? 33.469 -13.656 16.719 1.00 82.60 ? 143 PHE A CZ 1 ATOM 1131 N N . PHE A 1 144 ? 30.178 -11.967 13.818 1.00 86.85 ? 144 PHE A N 1 ATOM 1132 C CA . PHE A 1 144 ? 29.796 -12.963 12.820 1.00 85.88 ? 144 PHE A CA 1 ATOM 1133 C C . PHE A 1 144 ? 28.476 -13.624 13.226 1.00 86.88 ? 144 PHE A C 1 ATOM 1134 O O . PHE A 1 144 ? 28.401 -14.289 14.252 1.00 90.68 ? 144 PHE A O 1 ATOM 1135 C CB . PHE A 1 144 ? 30.881 -14.039 12.682 1.00 85.09 ? 144 PHE A CB 1 ATOM 1136 C CG . PHE A 1 144 ? 32.212 -13.521 12.190 1.00 84.56 ? 144 PHE A CG 1 ATOM 1137 C CD1 . PHE A 1 144 ? 32.359 -13.057 10.892 1.00 83.51 ? 144 PHE A CD1 1 ATOM 1138 C CD2 . PHE A 1 144 ? 33.325 -13.512 13.028 1.00 85.71 ? 144 PHE A CD2 1 ATOM 1139 C CE1 . PHE A 1 144 ? 33.584 -12.590 10.438 1.00 83.03 ? 144 PHE A CE1 1 ATOM 1140 C CE2 . PHE A 1 144 ? 34.553 -13.048 12.579 1.00 85.00 ? 144 PHE A CE2 1 ATOM 1141 C CZ . PHE A 1 144 ? 34.683 -12.588 11.280 1.00 83.37 ? 144 PHE A CZ 1 ATOM 1142 N N . ARG A 1 145 ? 27.444 -13.441 12.412 1.00 86.32 ? 145 ARG A N 1 ATOM 1143 C CA . ARG A 1 145 ? 26.088 -13.848 12.772 1.00 86.72 ? 145 ARG A CA 1 ATOM 1144 C C . ARG A 1 145 ? 25.840 -15.355 12.857 1.00 88.19 ? 145 ARG A C 1 ATOM 1145 O O . ARG A 1 145 ? 24.862 -15.779 13.465 1.00 93.40 ? 145 ARG A O 1 ATOM 1146 C CB . ARG A 1 145 ? 25.091 -13.260 11.776 1.00 85.09 ? 145 ARG A CB 1 ATOM 1147 C CG . ARG A 1 145 ? 25.104 -11.746 11.692 1.00 85.05 ? 145 ARG A CG 1 ATOM 1148 C CD . ARG A 1 145 ? 23.780 -11.267 11.139 1.00 86.84 ? 145 ARG A CD 1 ATOM 1149 N NE . ARG A 1 145 ? 23.729 -9.825 10.929 1.00 88.68 ? 145 ARG A NE 1 ATOM 1150 C CZ . ARG A 1 145 ? 23.553 -8.922 11.892 1.00 91.40 ? 145 ARG A CZ 1 ATOM 1151 N NH1 . ARG A 1 145 ? 23.452 -9.283 13.171 1.00 92.57 ? 145 ARG A NH1 1 ATOM 1152 N NH2 . ARG A 1 145 ? 23.500 -7.637 11.571 1.00 93.22 ? 145 ARG A NH2 1 ATOM 1153 N N . ASN A 1 146 ? 26.698 -16.160 12.242 1.00 89.12 ? 146 ASN A N 1 ATOM 1154 C CA . ASN A 1 146 ? 26.449 -17.602 12.138 1.00 89.39 ? 146 ASN A CA 1 ATOM 1155 C C . ASN A 1 146 ? 27.139 -18.415 13.224 1.00 89.62 ? 146 ASN A C 1 ATOM 1156 O O . ASN A 1 146 ? 26.885 -19.617 13.362 1.00 89.71 ? 146 ASN A O 1 ATOM 1157 C CB . ASN A 1 146 ? 26.855 -18.110 10.751 1.00 87.61 ? 146 ASN A CB 1 ATOM 1158 C CG . ASN A 1 146 ? 26.029 -17.486 9.645 1.00 88.58 ? 146 ASN A CG 1 ATOM 1159 O OD1 . ASN A 1 146 ? 24.840 -17.220 9.821 1.00 93.07 ? 146 ASN A OD1 1 ATOM 1160 N ND2 . ASN A 1 146 ? 26.652 -17.252 8.498 1.00 88.53 ? 146 ASN A ND2 1 ATOM 1161 N N . VAL A 1 147 ? 27.998 -17.759 13.996 1.00 89.45 ? 147 VAL A N 1 ATOM 1162 C CA . VAL A 1 147 ? 28.685 -18.411 15.103 1.00 89.91 ? 147 VAL A CA 1 ATOM 1163 C C . VAL A 1 147 ? 28.507 -17.602 16.380 1.00 90.61 ? 147 VAL A C 1 ATOM 1164 O O . VAL A 1 147 ? 28.289 -16.394 16.336 1.00 91.42 ? 147 VAL A O 1 ATOM 1165 C CB . VAL A 1 147 ? 30.177 -18.640 14.788 1.00 89.95 ? 147 VAL A CB 1 ATOM 1166 C CG1 . VAL A 1 147 ? 30.324 -19.631 13.642 1.00 88.60 ? 147 VAL A CG1 1 ATOM 1167 C CG2 . VAL A 1 147 ? 30.883 -17.334 14.445 1.00 89.91 ? 147 VAL A CG2 1 ATOM 1168 N N . VAL A 1 148 ? 28.593 -18.285 17.515 1.00 91.90 ? 148 VAL A N 1 ATOM 1169 C CA . VAL A 1 148 ? 28.273 -17.695 18.810 1.00 93.02 ? 148 VAL A CA 1 ATOM 1170 C C . VAL A 1 148 ? 29.528 -17.636 19.668 1.00 93.14 ? 148 VAL A C 1 ATOM 1171 O O . VAL A 1 148 ? 30.088 -18.673 20.022 1.00 94.64 ? 148 VAL A O 1 ATOM 1172 C CB . VAL A 1 148 ? 27.197 -18.529 19.536 1.00 95.09 ? 148 VAL A CB 1 ATOM 1173 C CG1 . VAL A 1 148 ? 26.771 -17.852 20.832 1.00 98.89 ? 148 VAL A CG1 1 ATOM 1174 C CG2 . VAL A 1 148 ? 25.994 -18.754 18.628 1.00 95.24 ? 148 VAL A CG2 1 ATOM 1175 N N . TRP A 1 149 ? 29.972 -16.425 19.991 1.00 93.39 ? 149 TRP A N 1 ATOM 1176 C CA . TRP A 1 149 ? 31.134 -16.233 20.857 1.00 94.63 ? 149 TRP A CA 1 ATOM 1177 C C . TRP A 1 149 ? 30.699 -16.371 22.321 1.00 98.05 ? 149 TRP A C 1 ATOM 1178 O O . TRP A 1 149 ? 30.173 -15.428 22.911 1.00 100.41 ? 149 TRP A O 1 ATOM 1179 C CB . TRP A 1 149 ? 31.759 -14.860 20.596 1.00 94.04 ? 149 TRP A CB 1 ATOM 1180 C CG . TRP A 1 149 ? 33.042 -14.582 21.331 1.00 94.29 ? 149 TRP A CG 1 ATOM 1181 C CD1 . TRP A 1 149 ? 33.654 -15.369 22.269 1.00 94.95 ? 149 TRP A CD1 1 ATOM 1182 C CD2 . TRP A 1 149 ? 33.859 -13.414 21.198 1.00 94.18 ? 149 TRP A CD2 1 ATOM 1183 N NE1 . TRP A 1 149 ? 34.808 -14.769 22.710 1.00 95.61 ? 149 TRP A NE1 1 ATOM 1184 C CE2 . TRP A 1 149 ? 34.956 -13.567 22.071 1.00 94.63 ? 149 TRP A CE2 1 ATOM 1185 C CE3 . TRP A 1 149 ? 33.774 -12.256 20.419 1.00 94.46 ? 149 TRP A CE3 1 ATOM 1186 C CZ2 . TRP A 1 149 ? 35.960 -12.605 22.188 1.00 94.76 ? 149 TRP A CZ2 1 ATOM 1187 C CZ3 . TRP A 1 149 ? 34.775 -11.297 20.537 1.00 95.22 ? 149 TRP A CZ3 1 ATOM 1188 C CH2 . TRP A 1 149 ? 35.852 -11.480 21.415 1.00 95.00 ? 149 TRP A CH2 1 ATOM 1189 N N . LEU A 1 150 ? 30.924 -17.550 22.899 1.00 99.36 ? 150 LEU A N 1 ATOM 1190 C CA . LEU A 1 150 ? 30.480 -17.846 24.261 1.00 102.21 ? 150 LEU A CA 1 ATOM 1191 C C . LEU A 1 150 ? 31.504 -17.380 25.284 1.00 103.16 ? 150 LEU A C 1 ATOM 1192 O O . LEU A 1 150 ? 32.707 -17.560 25.079 1.00 101.20 ? 150 LEU A O 1 ATOM 1193 C CB . LEU A 1 150 ? 30.247 -19.350 24.436 1.00 103.40 ? 150 LEU A CB 1 ATOM 1194 C CG . LEU A 1 150 ? 29.175 -19.995 23.551 1.00 103.41 ? 150 LEU A CG 1 ATOM 1195 C CD1 . LEU A 1 150 ? 29.242 -21.512 23.651 1.00 104.08 ? 150 LEU A CD1 1 ATOM 1196 C CD2 . LEU A 1 150 ? 27.785 -19.500 23.918 1.00 105.08 ? 150 LEU A CD2 1 ATOM 1197 N N . ILE A 1 151 ? 31.016 -16.785 26.377 1.00 105.32 ? 151 ILE A N 1 ATOM 1198 C CA . ILE A 1 151 ? 31.855 -16.390 27.519 1.00 106.70 ? 151 ILE A CA 1 ATOM 1199 C C . ILE A 1 151 ? 31.256 -16.865 28.850 1.00 108.67 ? 151 ILE A C 1 ATOM 1200 O O . ILE A 1 151 ? 30.121 -17.340 28.903 1.00 108.43 ? 151 ILE A O 1 ATOM 1201 C CB . ILE A 1 151 ? 32.080 -14.859 27.570 1.00 107.85 ? 151 ILE A CB 1 ATOM 1202 C CG1 . ILE A 1 151 ? 30.782 -14.121 27.915 1.00 110.84 ? 151 ILE A CG1 1 ATOM 1203 C CG2 . ILE A 1 151 ? 32.641 -14.356 26.247 1.00 104.86 ? 151 ILE A CG2 1 ATOM 1204 C CD1 . ILE A 1 151 ? 30.955 -12.629 28.114 1.00 112.21 ? 151 ILE A CD1 1 ATOM 1205 N N . LYS A 1 152 ? 32.032 -16.720 29.920 1.00 111.08 ? 152 LYS A N 1 ATOM 1206 C CA . LYS A 1 152 ? 31.629 -17.155 31.265 1.00 114.92 ? 152 LYS A CA 1 ATOM 1207 C C . LYS A 1 152 ? 30.338 -16.502 31.776 1.00 118.89 ? 152 LYS A C 1 ATOM 1208 O O . LYS A 1 152 ? 30.040 -15.353 31.443 1.00 119.01 ? 152 LYS A O 1 ATOM 1209 C CB . LYS A 1 152 ? 32.754 -16.859 32.262 1.00 116.11 ? 152 LYS A CB 1 ATOM 1210 C CG . LYS A 1 152 ? 32.989 -15.375 32.518 1.00 117.01 ? 152 LYS A CG 1 ATOM 1211 C CD . LYS A 1 152 ? 34.158 -15.165 33.457 1.00 118.54 ? 152 LYS A CD 1 ATOM 1212 C CE . LYS A 1 152 ? 34.195 -13.757 34.022 1.00 120.59 ? 152 LYS A CE 1 ATOM 1213 N NZ . LYS A 1 152 ? 35.405 -13.558 34.865 1.00 122.41 ? 152 LYS A NZ 1 ATOM 1214 N N . LYS A 1 153 ? 29.594 -17.236 32.603 1.00 122.61 ? 153 LYS A N 1 ATOM 1215 C CA . LYS A 1 153 ? 28.378 -16.716 33.233 1.00 126.42 ? 153 LYS A CA 1 ATOM 1216 C C . LYS A 1 153 ? 28.490 -16.783 34.755 1.00 129.63 ? 153 LYS A C 1 ATOM 1217 O O . LYS A 1 153 ? 28.711 -17.856 35.320 1.00 128.94 ? 153 LYS A O 1 ATOM 1218 C CB . LYS A 1 153 ? 27.147 -17.492 32.757 1.00 126.93 ? 153 LYS A CB 1 ATOM 1219 C CG . LYS A 1 153 ? 25.840 -16.742 32.973 1.00 129.74 ? 153 LYS A CG 1 ATOM 1220 C CD . LYS A 1 153 ? 24.701 -17.327 32.151 1.00 129.61 ? 153 LYS A CD 1 ATOM 1221 C CE . LYS A 1 153 ? 24.049 -18.510 32.845 1.00 130.94 ? 153 LYS A CE 1 ATOM 1222 N NZ . LYS A 1 153 ? 23.052 -18.077 33.858 1.00 134.68 ? 153 LYS A NZ 1 ATOM 1223 N N . ASN A 1 154 ? 28.334 -15.627 35.401 1.00 133.09 ? 154 ASN A N 1 ATOM 1224 C CA . ASN A 1 154 ? 28.492 -15.482 36.856 1.00 137.96 ? 154 ASN A CA 1 ATOM 1225 C C . ASN A 1 154 ? 29.843 -16.020 37.349 1.00 137.48 ? 154 ASN A C 1 ATOM 1226 O O . ASN A 1 154 ? 29.920 -16.683 38.387 1.00 139.57 ? 154 ASN A O 1 ATOM 1227 C CB . ASN A 1 154 ? 27.322 -16.147 37.605 1.00 141.04 ? 154 ASN A CB 1 ATOM 1228 C CG . ASN A 1 154 ? 27.212 -15.694 39.056 1.00 147.16 ? 154 ASN A CG 1 ATOM 1229 O OD1 . ASN A 1 154 ? 27.830 -14.709 39.465 1.00 149.22 ? 154 ASN A OD1 1 ATOM 1230 N ND2 . ASN A 1 154 ? 26.418 -16.416 39.843 1.00 150.78 ? 154 ASN A ND2 1 ATOM 1231 N N . SER A 1 155 ? 30.899 -15.717 36.592 1.00 134.42 ? 155 SER A N 1 ATOM 1232 C CA . SER A 1 155 ? 32.258 -16.177 36.891 1.00 133.80 ? 155 SER A CA 1 ATOM 1233 C C . SER A 1 155 ? 32.363 -17.705 36.882 1.00 132.12 ? 155 SER A C 1 ATOM 1234 O O . SER A 1 155 ? 32.815 -18.308 37.853 1.00 136.53 ? 155 SER A O 1 ATOM 1235 C CB . SER A 1 155 ? 32.746 -15.615 38.239 1.00 137.68 ? 155 SER A CB 1 ATOM 1236 O OG . SER A 1 155 ? 32.576 -14.210 38.306 1.00 138.89 ? 155 SER A OG 1 ATOM 1237 N N . THR A 1 156 ? 31.926 -18.331 35.794 1.00 128.18 ? 156 THR A N 1 ATOM 1238 C CA . THR A 1 156 ? 32.075 -19.780 35.624 1.00 126.29 ? 156 THR A CA 1 ATOM 1239 C C . THR A 1 156 ? 31.932 -20.158 34.156 1.00 122.74 ? 156 THR A C 1 ATOM 1240 O O . THR A 1 156 ? 30.969 -19.758 33.504 1.00 124.73 ? 156 THR A O 1 ATOM 1241 C CB . THR A 1 156 ? 31.019 -20.577 36.423 1.00 127.56 ? 156 THR A CB 1 ATOM 1242 O OG1 . THR A 1 156 ? 30.909 -20.054 37.751 1.00 131.67 ? 156 THR A OG1 1 ATOM 1243 C CG2 . THR A 1 156 ? 31.397 -22.051 36.507 1.00 126.57 ? 156 THR A CG2 1 ATOM 1244 N N . TYR A 1 157 ? 32.896 -20.917 33.640 1.00 120.06 ? 157 TYR A N 1 ATOM 1245 C CA . TYR A 1 157 ? 32.787 -21.516 32.311 1.00 115.33 ? 157 TYR A CA 1 ATOM 1246 C C . TYR A 1 157 ? 32.871 -23.032 32.481 1.00 115.01 ? 157 TYR A C 1 ATOM 1247 O O . TYR A 1 157 ? 33.966 -23.601 32.483 1.00 112.80 ? 157 TYR A O 1 ATOM 1248 C CB . TYR A 1 157 ? 33.890 -21.003 31.379 1.00 112.46 ? 157 TYR A CB 1 ATOM 1249 C CG . TYR A 1 157 ? 33.594 -21.184 29.892 1.00 109.30 ? 157 TYR A CG 1 ATOM 1250 C CD1 . TYR A 1 157 ? 33.519 -22.453 29.319 1.00 107.71 ? 157 TYR A CD1 1 ATOM 1251 C CD2 . TYR A 1 157 ? 33.391 -20.083 29.063 1.00 107.47 ? 157 TYR A CD2 1 ATOM 1252 C CE1 . TYR A 1 157 ? 33.257 -22.618 27.966 1.00 106.11 ? 157 TYR A CE1 1 ATOM 1253 C CE2 . TYR A 1 157 ? 33.127 -20.238 27.713 1.00 105.09 ? 157 TYR A CE2 1 ATOM 1254 C CZ . TYR A 1 157 ? 33.059 -21.509 27.166 1.00 104.38 ? 157 TYR A CZ 1 ATOM 1255 O OH . TYR A 1 157 ? 32.799 -21.667 25.821 1.00 100.19 ? 157 TYR A OH 1 ATOM 1256 N N . PRO A 1 158 ? 31.712 -23.690 32.657 1.00 116.47 ? 158 PRO A N 1 ATOM 1257 C CA . PRO A 1 158 ? 31.727 -25.143 32.784 1.00 116.73 ? 158 PRO A CA 1 ATOM 1258 C C . PRO A 1 158 ? 31.977 -25.812 31.438 1.00 112.96 ? 158 PRO A C 1 ATOM 1259 O O . PRO A 1 158 ? 31.744 -25.204 30.391 1.00 110.62 ? 158 PRO A O 1 ATOM 1260 C CB . PRO A 1 158 ? 30.324 -25.467 33.312 1.00 118.83 ? 158 PRO A CB 1 ATOM 1261 C CG . PRO A 1 158 ? 29.469 -24.353 32.823 1.00 118.43 ? 158 PRO A CG 1 ATOM 1262 C CD . PRO A 1 158 ? 30.350 -23.136 32.784 1.00 118.00 ? 158 PRO A CD 1 ATOM 1263 N N . THR A 1 159 ? 32.456 -27.051 31.476 1.00 113.00 ? 159 THR A N 1 ATOM 1264 C CA . THR A 1 159 ? 32.784 -27.787 30.262 1.00 110.02 ? 159 THR A CA 1 ATOM 1265 C C . THR A 1 159 ? 31.546 -27.943 29.383 1.00 110.16 ? 159 THR A C 1 ATOM 1266 O O . THR A 1 159 ? 30.498 -28.390 29.852 1.00 111.79 ? 159 THR A O 1 ATOM 1267 C CB . THR A 1 159 ? 33.352 -29.186 30.583 1.00 110.25 ? 159 THR A CB 1 ATOM 1268 O OG1 . THR A 1 159 ? 34.424 -29.070 31.526 1.00 110.59 ? 159 THR A OG1 1 ATOM 1269 C CG2 . THR A 1 159 ? 33.868 -29.870 29.322 1.00 107.74 ? 159 THR A CG2 1 ATOM 1270 N N . ILE A 1 160 ? 31.677 -27.553 28.116 1.00 108.75 ? 160 ILE A N 1 ATOM 1271 C CA . ILE A 1 160 ? 30.614 -27.711 27.123 1.00 108.37 ? 160 ILE A CA 1 ATOM 1272 C C . ILE A 1 160 ? 30.729 -29.089 26.481 1.00 109.22 ? 160 ILE A C 1 ATOM 1273 O O . ILE A 1 160 ? 31.827 -29.535 26.164 1.00 108.34 ? 160 ILE A O 1 ATOM 1274 C CB . ILE A 1 160 ? 30.702 -26.620 26.030 1.00 105.62 ? 160 ILE A CB 1 ATOM 1275 C CG1 . ILE A 1 160 ? 30.381 -25.251 26.635 1.00 107.04 ? 160 ILE A CG1 1 ATOM 1276 C CG2 . ILE A 1 160 ? 29.754 -26.924 24.873 1.00 104.31 ? 160 ILE A CG2 1 ATOM 1277 C CD1 . ILE A 1 160 ? 30.793 -24.074 25.780 1.00 105.03 ? 160 ILE A CD1 1 ATOM 1278 N N . LYS A 1 161 ? 29.595 -29.763 26.308 1.00 111.88 ? 161 LYS A N 1 ATOM 1279 C CA . LYS A 1 161 ? 29.542 -31.044 25.602 1.00 112.52 ? 161 LYS A CA 1 ATOM 1280 C C . LYS A 1 161 ? 28.288 -31.084 24.740 1.00 112.96 ? 161 LYS A C 1 ATOM 1281 O O . LYS A 1 161 ? 27.208 -31.433 25.219 1.00 115.12 ? 161 LYS A O 1 ATOM 1282 C CB . LYS A 1 161 ? 29.540 -32.217 26.586 1.00 116.51 ? 161 LYS A CB 1 ATOM 1283 C CG . LYS A 1 161 ? 30.877 -32.480 27.262 1.00 118.55 ? 161 LYS A CG 1 ATOM 1284 C CD . LYS A 1 161 ? 30.757 -33.544 28.345 1.00 122.25 ? 161 LYS A CD 1 ATOM 1285 C CE . LYS A 1 161 ? 32.081 -33.772 29.060 1.00 123.80 ? 161 LYS A CE 1 ATOM 1286 N NZ . LYS A 1 161 ? 31.913 -34.511 30.344 1.00 127.82 ? 161 LYS A NZ 1 ATOM 1287 N N . ARG A 1 162 ? 28.434 -30.715 23.471 1.00 111.30 ? 162 ARG A N 1 ATOM 1288 C CA . ARG A 1 162 ? 27.301 -30.646 22.561 1.00 111.73 ? 162 ARG A CA 1 ATOM 1289 C C . ARG A 1 162 ? 27.487 -31.557 21.362 1.00 110.65 ? 162 ARG A C 1 ATOM 1290 O O . ARG A 1 162 ? 28.594 -31.700 20.840 1.00 110.04 ? 162 ARG A O 1 ATOM 1291 C CB . ARG A 1 162 ? 27.094 -29.212 22.080 1.00 111.29 ? 162 ARG A CB 1 ATOM 1292 C CG . ARG A 1 162 ? 26.265 -28.352 23.015 1.00 114.69 ? 162 ARG A CG 1 ATOM 1293 C CD . ARG A 1 162 ? 24.841 -28.877 23.173 1.00 117.57 ? 162 ARG A CD 1 ATOM 1294 N NE . ARG A 1 162 ? 23.845 -27.831 22.949 1.00 118.06 ? 162 ARG A NE 1 ATOM 1295 C CZ . ARG A 1 162 ? 23.659 -26.771 23.734 1.00 119.09 ? 162 ARG A CZ 1 ATOM 1296 N NH1 . ARG A 1 162 ? 24.401 -26.583 24.822 1.00 120.40 ? 162 ARG A NH1 1 ATOM 1297 N NH2 . ARG A 1 162 ? 22.724 -25.882 23.424 1.00 119.89 ? 162 ARG A NH2 1 ATOM 1298 N N . SER A 1 163 ? 26.382 -32.153 20.925 1.00 109.42 ? 163 SER A N 1 ATOM 1299 C CA . SER A 1 163 ? 26.382 -33.052 19.788 1.00 106.65 ? 163 SER A CA 1 ATOM 1300 C C . SER A 1 163 ? 25.246 -32.698 18.835 1.00 105.82 ? 163 SER A C 1 ATOM 1301 O O . SER A 1 163 ? 24.125 -32.456 19.268 1.00 107.30 ? 163 SER A O 1 ATOM 1302 C CB . SER A 1 163 ? 26.227 -34.492 20.270 1.00 108.04 ? 163 SER A CB 1 ATOM 1303 O OG . SER A 1 163 ? 26.215 -35.393 19.179 1.00 109.75 ? 163 SER A OG 1 ATOM 1304 N N . TYR A 1 164 ? 25.544 -32.645 17.539 1.00 104.15 ? 164 TYR A N 1 ATOM 1305 C CA . TYR A 1 164 ? 24.504 -32.509 16.527 1.00 103.55 ? 164 TYR A CA 1 ATOM 1306 C C . TYR A 1 164 ? 24.578 -33.666 15.534 1.00 104.25 ? 164 TYR A C 1 ATOM 1307 O O . TYR A 1 164 ? 25.655 -34.022 15.059 1.00 102.18 ? 164 TYR A O 1 ATOM 1308 C CB . TYR A 1 164 ? 24.602 -31.177 15.790 1.00 100.51 ? 164 TYR A CB 1 ATOM 1309 C CG . TYR A 1 164 ? 23.675 -31.124 14.602 1.00 100.73 ? 164 TYR A CG 1 ATOM 1310 C CD1 . TYR A 1 164 ? 22.311 -30.915 14.768 1.00 103.19 ? 164 TYR A CD1 1 ATOM 1311 C CD2 . TYR A 1 164 ? 24.155 -31.327 13.314 1.00 100.07 ? 164 TYR A CD2 1 ATOM 1312 C CE1 . TYR A 1 164 ? 21.453 -30.885 13.680 1.00 103.69 ? 164 TYR A CE1 1 ATOM 1313 C CE2 . TYR A 1 164 ? 23.308 -31.299 12.220 1.00 100.38 ? 164 TYR A CE2 1 ATOM 1314 C CZ . TYR A 1 164 ? 21.961 -31.078 12.406 1.00 102.55 ? 164 TYR A CZ 1 ATOM 1315 O OH . TYR A 1 164 ? 21.129 -31.052 11.312 1.00 103.34 ? 164 TYR A OH 1 ATOM 1316 N N . ASN A 1 165 ? 23.414 -34.229 15.225 1.00 107.49 ? 165 ASN A N 1 ATOM 1317 C CA . ASN A 1 165 ? 23.286 -35.372 14.334 1.00 110.27 ? 165 ASN A CA 1 ATOM 1318 C C . ASN A 1 165 ? 22.673 -34.903 13.024 1.00 108.54 ? 165 ASN A C 1 ATOM 1319 O O . ASN A 1 165 ? 21.577 -34.344 13.022 1.00 109.76 ? 165 ASN A O 1 ATOM 1320 C CB . ASN A 1 165 ? 22.401 -36.419 15.012 1.00 116.58 ? 165 ASN A CB 1 ATOM 1321 C CG . ASN A 1 165 ? 22.113 -37.633 14.140 1.00 121.80 ? 165 ASN A CG 1 ATOM 1322 O OD1 . ASN A 1 165 ? 21.798 -37.518 12.957 1.00 118.14 ? 165 ASN A OD1 1 ATOM 1323 N ND2 . ASN A 1 165 ? 22.203 -38.818 14.748 1.00 131.33 ? 165 ASN A ND2 1 ATOM 1324 N N . ASN A 1 166 ? 23.383 -35.121 11.917 1.00 105.55 ? 166 ASN A N 1 ATOM 1325 C CA . ASN A 1 166 ? 22.885 -34.727 10.600 1.00 103.59 ? 166 ASN A CA 1 ATOM 1326 C C . ASN A 1 166 ? 21.765 -35.654 10.135 1.00 105.62 ? 166 ASN A C 1 ATOM 1327 O O . ASN A 1 166 ? 22.018 -36.705 9.536 1.00 105.18 ? 166 ASN A O 1 ATOM 1328 C CB . ASN A 1 166 ? 24.016 -34.701 9.565 1.00 100.07 ? 166 ASN A CB 1 ATOM 1329 C CG . ASN A 1 166 ? 23.590 -34.068 8.251 1.00 99.29 ? 166 ASN A CG 1 ATOM 1330 O OD1 . ASN A 1 166 ? 22.530 -33.442 8.163 1.00 99.08 ? 166 ASN A OD1 1 ATOM 1331 N ND2 . ASN A 1 166 ? 24.418 -34.227 7.218 1.00 97.50 ? 166 ASN A ND2 1 ATOM 1332 N N . THR A 1 167 ? 20.529 -35.249 10.425 1.00 106.66 ? 167 THR A N 1 ATOM 1333 C CA . THR A 1 167 ? 19.338 -35.997 10.021 1.00 110.27 ? 167 THR A CA 1 ATOM 1334 C C . THR A 1 167 ? 18.821 -35.564 8.643 1.00 111.56 ? 167 THR A C 1 ATOM 1335 O O . THR A 1 167 ? 17.858 -36.137 8.128 1.00 114.70 ? 167 THR A O 1 ATOM 1336 C CB . THR A 1 167 ? 18.207 -35.843 11.058 1.00 112.20 ? 167 THR A CB 1 ATOM 1337 O OG1 . THR A 1 167 ? 17.860 -34.459 11.197 1.00 111.51 ? 167 THR A OG1 1 ATOM 1338 C CG2 . THR A 1 167 ? 18.645 -36.393 12.407 1.00 111.71 ? 167 THR A CG2 1 ATOM 1339 N N . ASN A 1 168 ? 19.464 -34.560 8.049 1.00 109.28 ? 168 ASN A N 1 ATOM 1340 C CA . ASN A 1 168 ? 19.114 -34.106 6.709 1.00 107.02 ? 168 ASN A CA 1 ATOM 1341 C C . ASN A 1 168 ? 19.634 -35.075 5.670 1.00 106.48 ? 168 ASN A C 1 ATOM 1342 O O . ASN A 1 168 ? 20.542 -35.856 5.945 1.00 107.37 ? 168 ASN A O 1 ATOM 1343 C CB . ASN A 1 168 ? 19.714 -32.732 6.434 1.00 105.11 ? 168 ASN A CB 1 ATOM 1344 C CG . ASN A 1 168 ? 19.296 -31.701 7.456 1.00 105.30 ? 168 ASN A CG 1 ATOM 1345 O OD1 . ASN A 1 168 ? 18.204 -31.138 7.368 1.00 107.67 ? 168 ASN A OD1 1 ATOM 1346 N ND2 . ASN A 1 168 ? 20.166 -31.440 8.430 1.00 102.82 ? 168 ASN A ND2 1 ATOM 1347 N N . GLN A 1 169 ? 19.063 -35.011 4.471 1.00 106.65 ? 169 GLN A N 1 ATOM 1348 C CA . GLN A 1 169 ? 19.532 -35.823 3.348 1.00 107.05 ? 169 GLN A CA 1 ATOM 1349 C C . GLN A 1 169 ? 20.812 -35.262 2.749 1.00 102.92 ? 169 GLN A C 1 ATOM 1350 O O . GLN A 1 169 ? 21.604 -35.998 2.166 1.00 101.95 ? 169 GLN A O 1 ATOM 1351 C CB . GLN A 1 169 ? 18.459 -35.896 2.258 1.00 110.43 ? 169 GLN A CB 1 ATOM 1352 C CG . GLN A 1 169 ? 17.151 -36.486 2.738 1.00 114.18 ? 169 GLN A CG 1 ATOM 1353 C CD . GLN A 1 169 ? 17.379 -37.745 3.546 1.00 117.40 ? 169 GLN A CD 1 ATOM 1354 O OE1 . GLN A 1 169 ? 17.946 -38.714 3.041 1.00 119.01 ? 169 GLN A OE1 1 ATOM 1355 N NE2 . GLN A 1 169 ? 16.966 -37.733 4.814 1.00 119.08 ? 169 GLN A NE2 1 ATOM 1356 N N . GLU A 1 170 ? 21.008 -33.959 2.914 1.00 99.79 ? 170 GLU A N 1 ATOM 1357 C CA . GLU A 1 170 ? 22.088 -33.236 2.268 1.00 95.60 ? 170 GLU A CA 1 ATOM 1358 C C . GLU A 1 170 ? 23.338 -33.215 3.140 1.00 94.18 ? 170 GLU A C 1 ATOM 1359 O O . GLU A 1 170 ? 23.245 -33.242 4.367 1.00 94.82 ? 170 GLU A O 1 ATOM 1360 C CB . GLU A 1 170 ? 21.637 -31.805 1.979 1.00 93.90 ? 170 GLU A CB 1 ATOM 1361 C CG . GLU A 1 170 ? 20.403 -31.711 1.083 1.00 95.82 ? 170 GLU A CG 1 ATOM 1362 C CD . GLU A 1 170 ? 19.076 -31.823 1.826 1.00 97.02 ? 170 GLU A CD 1 ATOM 1363 O OE1 . GLU A 1 170 ? 19.055 -32.271 2.992 1.00 97.02 ? 170 GLU A OE1 1 ATOM 1364 O OE2 . GLU A 1 170 ? 18.037 -31.464 1.236 1.00 92.13 ? 170 GLU A OE2 1 ATOM 1365 N N . ASP A 1 171 ? 24.503 -33.184 2.495 1.00 93.81 ? 171 ASP A N 1 ATOM 1366 C CA . ASP A 1 171 ? 25.766 -32.903 3.172 1.00 91.91 ? 171 ASP A CA 1 ATOM 1367 C C . ASP A 1 171 ? 25.635 -31.538 3.825 1.00 90.60 ? 171 ASP A C 1 ATOM 1368 O O . ASP A 1 171 ? 24.982 -30.649 3.275 1.00 89.31 ? 171 ASP A O 1 ATOM 1369 C CB . ASP A 1 171 ? 26.941 -32.850 2.178 1.00 93.21 ? 171 ASP A CB 1 ATOM 1370 C CG . ASP A 1 171 ? 27.350 -34.220 1.643 1.00 96.26 ? 171 ASP A CG 1 ATOM 1371 O OD1 . ASP A 1 171 ? 26.933 -35.257 2.199 1.00 101.03 ? 171 ASP A OD1 1 ATOM 1372 O OD2 . ASP A 1 171 ? 28.115 -34.254 0.654 1.00 97.25 ? 171 ASP A OD2 1 ATOM 1373 N N . LEU A 1 172 ? 26.265 -31.369 4.984 1.00 90.71 ? 172 LEU A N 1 ATOM 1374 C CA . LEU A 1 172 ? 26.160 -30.127 5.739 1.00 91.94 ? 172 LEU A CA 1 ATOM 1375 C C . LEU A 1 172 ? 27.532 -29.492 5.960 1.00 89.94 ? 172 LEU A C 1 ATOM 1376 O O . LEU A 1 172 ? 28.451 -30.144 6.452 1.00 89.49 ? 172 LEU A O 1 ATOM 1377 C CB . LEU A 1 172 ? 25.493 -30.401 7.086 1.00 94.70 ? 172 LEU A CB 1 ATOM 1378 C CG . LEU A 1 172 ? 24.968 -29.168 7.830 1.00 97.71 ? 172 LEU A CG 1 ATOM 1379 C CD1 . LEU A 1 172 ? 23.651 -28.692 7.232 1.00 99.63 ? 172 LEU A CD1 1 ATOM 1380 C CD2 . LEU A 1 172 ? 24.797 -29.453 9.318 1.00 99.38 ? 172 LEU A CD2 1 ATOM 1381 N N . LEU A 1 173 ? 27.661 -28.219 5.594 1.00 88.19 ? 173 LEU A N 1 ATOM 1382 C CA . LEU A 1 173 ? 28.861 -27.451 5.893 1.00 87.32 ? 173 LEU A CA 1 ATOM 1383 C C . LEU A 1 173 ? 28.741 -26.850 7.283 1.00 88.25 ? 173 LEU A C 1 ATOM 1384 O O . LEU A 1 173 ? 27.885 -26.000 7.517 1.00 90.19 ? 173 LEU A O 1 ATOM 1385 C CB . LEU A 1 173 ? 29.059 -26.327 4.877 1.00 87.40 ? 173 LEU A CB 1 ATOM 1386 C CG . LEU A 1 173 ? 30.207 -25.346 5.164 1.00 86.68 ? 173 LEU A CG 1 ATOM 1387 C CD1 . LEU A 1 173 ? 31.534 -26.069 5.339 1.00 85.89 ? 173 LEU A CD1 1 ATOM 1388 C CD2 . LEU A 1 173 ? 30.315 -24.317 4.050 1.00 86.26 ? 173 LEU A CD2 1 ATOM 1389 N N . VAL A 1 174 ? 29.610 -27.282 8.194 1.00 87.39 ? 174 VAL A N 1 ATOM 1390 C CA . VAL A 1 174 ? 29.622 -26.786 9.569 1.00 86.13 ? 174 VAL A CA 1 ATOM 1391 C C . VAL A 1 174 ? 30.845 -25.897 9.790 1.00 83.70 ? 174 VAL A C 1 ATOM 1392 O O . VAL A 1 174 ? 31.961 -26.277 9.434 1.00 83.67 ? 174 VAL A O 1 ATOM 1393 C CB . VAL A 1 174 ? 29.664 -27.951 10.577 1.00 87.12 ? 174 VAL A CB 1 ATOM 1394 C CG1 . VAL A 1 174 ? 29.650 -27.427 12.005 1.00 89.01 ? 174 VAL A CG1 1 ATOM 1395 C CG2 . VAL A 1 174 ? 28.499 -28.901 10.341 1.00 88.56 ? 174 VAL A CG2 1 ATOM 1396 N N . LEU A 1 175 ? 30.626 -24.724 10.381 1.00 82.62 ? 175 LEU A N 1 ATOM 1397 C CA . LEU A 1 175 ? 31.695 -23.778 10.698 1.00 81.79 ? 175 LEU A CA 1 ATOM 1398 C C . LEU A 1 175 ? 31.779 -23.544 12.197 1.00 83.10 ? 175 LEU A C 1 ATOM 1399 O O . LEU A 1 175 ? 30.754 -23.424 12.865 1.00 85.54 ? 175 LEU A O 1 ATOM 1400 C CB . LEU A 1 175 ? 31.425 -22.437 10.024 1.00 81.66 ? 175 LEU A CB 1 ATOM 1401 C CG . LEU A 1 175 ? 31.409 -22.415 8.495 1.00 81.82 ? 175 LEU A CG 1 ATOM 1402 C CD1 . LEU A 1 175 ? 30.657 -21.192 7.993 1.00 83.18 ? 175 LEU A CD1 1 ATOM 1403 C CD2 . LEU A 1 175 ? 32.823 -22.436 7.940 1.00 79.71 ? 175 LEU A CD2 1 ATOM 1404 N N . TRP A 1 176 ? 32.999 -23.471 12.720 1.00 82.74 ? 176 TRP A N 1 ATOM 1405 C CA . TRP A 1 176 ? 33.224 -23.087 14.113 1.00 83.53 ? 176 TRP A CA 1 ATOM 1406 C C . TRP A 1 176 ? 34.549 -22.333 14.241 1.00 82.79 ? 176 TRP A C 1 ATOM 1407 O O . TRP A 1 176 ? 35.216 -22.083 13.237 1.00 80.70 ? 176 TRP A O 1 ATOM 1408 C CB . TRP A 1 176 ? 33.180 -24.319 15.027 1.00 85.46 ? 176 TRP A CB 1 ATOM 1409 C CG . TRP A 1 176 ? 34.300 -25.293 14.819 1.00 85.72 ? 176 TRP A CG 1 ATOM 1410 C CD1 . TRP A 1 176 ? 35.455 -25.382 15.543 1.00 86.16 ? 176 TRP A CD1 1 ATOM 1411 C CD2 . TRP A 1 176 ? 34.367 -26.323 13.828 1.00 84.10 ? 176 TRP A CD2 1 ATOM 1412 N NE1 . TRP A 1 176 ? 36.240 -26.401 15.060 1.00 84.97 ? 176 TRP A NE1 1 ATOM 1413 C CE2 . TRP A 1 176 ? 35.595 -26.997 14.009 1.00 84.01 ? 176 TRP A CE2 1 ATOM 1414 C CE3 . TRP A 1 176 ? 33.507 -26.747 12.807 1.00 83.23 ? 176 TRP A CE3 1 ATOM 1415 C CZ2 . TRP A 1 176 ? 35.985 -28.067 13.206 1.00 83.67 ? 176 TRP A CZ2 1 ATOM 1416 C CZ3 . TRP A 1 176 ? 33.893 -27.809 12.013 1.00 83.07 ? 176 TRP A CZ3 1 ATOM 1417 C CH2 . TRP A 1 176 ? 35.124 -28.457 12.214 1.00 83.46 ? 176 TRP A CH2 1 ATOM 1418 N N . GLY A 1 177 ? 34.927 -21.958 15.463 1.00 84.64 ? 177 GLY A N 1 ATOM 1419 C CA . GLY A 1 177 ? 36.154 -21.184 15.669 1.00 84.25 ? 177 GLY A CA 1 ATOM 1420 C C . GLY A 1 177 ? 36.758 -21.229 17.062 1.00 85.09 ? 177 GLY A C 1 ATOM 1421 O O . GLY A 1 177 ? 36.176 -21.779 17.996 1.00 86.31 ? 177 GLY A O 1 ATOM 1422 N N . ILE A 1 178 ? 37.938 -20.631 17.181 1.00 84.94 ? 178 ILE A N 1 ATOM 1423 C CA . ILE A 1 178 ? 38.678 -20.559 18.435 1.00 86.55 ? 178 ILE A CA 1 ATOM 1424 C C . ILE A 1 178 ? 39.167 -19.118 18.601 1.00 87.40 ? 178 ILE A C 1 ATOM 1425 O O . ILE A 1 178 ? 39.640 -18.512 17.643 1.00 85.40 ? 178 ILE A O 1 ATOM 1426 C CB . ILE A 1 178 ? 39.864 -21.568 18.461 1.00 87.48 ? 178 ILE A CB 1 ATOM 1427 C CG1 . ILE A 1 178 ? 40.703 -21.446 19.745 1.00 90.99 ? 178 ILE A CG1 1 ATOM 1428 C CG2 . ILE A 1 178 ? 40.783 -21.392 17.264 1.00 86.05 ? 178 ILE A CG2 1 ATOM 1429 C CD1 . ILE A 1 178 ? 40.589 -22.617 20.697 1.00 93.13 ? 178 ILE A CD1 1 ATOM 1430 N N . HIS A 1 179 ? 39.034 -18.571 19.809 1.00 89.10 ? 179 HIS A N 1 ATOM 1431 C CA . HIS A 1 179 ? 39.535 -17.231 20.108 1.00 89.97 ? 179 HIS A CA 1 ATOM 1432 C C . HIS A 1 179 ? 40.919 -17.293 20.752 1.00 91.02 ? 179 HIS A C 1 ATOM 1433 O O . HIS A 1 179 ? 41.116 -17.979 21.758 1.00 93.62 ? 179 HIS A O 1 ATOM 1434 C CB . HIS A 1 179 ? 38.569 -16.475 21.026 1.00 91.08 ? 179 HIS A CB 1 ATOM 1435 C CG . HIS A 1 179 ? 39.080 -15.138 21.468 1.00 91.33 ? 179 HIS A CG 1 ATOM 1436 N ND1 . HIS A 1 179 ? 39.092 -14.744 22.789 1.00 94.13 ? 179 HIS A ND1 1 ATOM 1437 C CD2 . HIS A 1 179 ? 39.613 -14.111 20.765 1.00 90.56 ? 179 HIS A CD2 1 ATOM 1438 C CE1 . HIS A 1 179 ? 39.598 -13.527 22.880 1.00 94.81 ? 179 HIS A CE1 1 ATOM 1439 N NE2 . HIS A 1 179 ? 39.922 -13.120 21.665 1.00 93.57 ? 179 HIS A NE2 1 ATOM 1440 N N . HIS A 1 180 ? 41.865 -16.567 20.161 1.00 89.80 ? 180 HIS A N 1 ATOM 1441 C CA . HIS A 1 180 ? 43.213 -16.443 20.689 1.00 91.06 ? 180 HIS A CA 1 ATOM 1442 C C . HIS A 1 180 ? 43.316 -15.101 21.404 1.00 94.06 ? 180 HIS A C 1 ATOM 1443 O O . HIS A 1 180 ? 43.308 -14.057 20.758 1.00 93.81 ? 180 HIS A O 1 ATOM 1444 C CB . HIS A 1 180 ? 44.234 -16.505 19.557 1.00 90.25 ? 180 HIS A CB 1 ATOM 1445 C CG . HIS A 1 180 ? 44.222 -17.797 18.803 1.00 89.38 ? 180 HIS A CG 1 ATOM 1446 N ND1 . HIS A 1 180 ? 44.279 -19.020 19.432 1.00 91.11 ? 180 HIS A ND1 1 ATOM 1447 C CD2 . HIS A 1 180 ? 44.167 -18.059 17.476 1.00 87.49 ? 180 HIS A CD2 1 ATOM 1448 C CE1 . HIS A 1 180 ? 44.253 -19.982 18.526 1.00 88.77 ? 180 HIS A CE1 1 ATOM 1449 N NE2 . HIS A 1 180 ? 44.185 -19.425 17.332 1.00 87.01 ? 180 HIS A NE2 1 ATOM 1450 N N . PRO A 1 181 ? 43.402 -15.117 22.741 1.00 96.50 ? 181 PRO A N 1 ATOM 1451 C CA . PRO A 1 181 ? 43.403 -13.863 23.487 1.00 99.19 ? 181 PRO A CA 1 ATOM 1452 C C . PRO A 1 181 ? 44.760 -13.155 23.529 1.00 99.85 ? 181 PRO A C 1 ATOM 1453 O O . PRO A 1 181 ? 45.794 -13.751 23.218 1.00 97.19 ? 181 PRO A O 1 ATOM 1454 C CB . PRO A 1 181 ? 42.987 -14.302 24.891 1.00 102.73 ? 181 PRO A CB 1 ATOM 1455 C CG . PRO A 1 181 ? 43.497 -15.696 25.008 1.00 102.23 ? 181 PRO A CG 1 ATOM 1456 C CD . PRO A 1 181 ? 43.441 -16.292 23.630 1.00 98.48 ? 181 PRO A CD 1 ATOM 1457 N N . LYS A 1 182 ? 44.726 -11.887 23.929 1.00 101.99 ? 182 LYS A N 1 ATOM 1458 C CA . LYS A 1 182 ? 45.910 -11.032 24.012 1.00 104.31 ? 182 LYS A CA 1 ATOM 1459 C C . LYS A 1 182 ? 46.902 -11.518 25.075 1.00 105.65 ? 182 LYS A C 1 ATOM 1460 O O . LYS A 1 182 ? 48.078 -11.732 24.774 1.00 105.59 ? 182 LYS A O 1 ATOM 1461 C CB . LYS A 1 182 ? 45.471 -9.592 24.310 1.00 107.48 ? 182 LYS A CB 1 ATOM 1462 C CG . LYS A 1 182 ? 46.593 -8.584 24.514 1.00 111.83 ? 182 LYS A CG 1 ATOM 1463 C CD . LYS A 1 182 ? 46.074 -7.332 25.211 1.00 115.99 ? 182 LYS A CD 1 ATOM 1464 C CE . LYS A 1 182 ? 47.204 -6.418 25.663 1.00 119.69 ? 182 LYS A CE 1 ATOM 1465 N NZ . LYS A 1 182 ? 47.896 -5.774 24.512 1.00 119.61 ? 182 LYS A NZ 1 ATOM 1466 N N . ASP A 1 183 ? 46.422 -11.685 26.310 1.00 106.88 ? 183 ASP A N 1 ATOM 1467 C CA . ASP A 1 183 ? 47.274 -12.090 27.441 1.00 108.80 ? 183 ASP A CA 1 ATOM 1468 C C . ASP A 1 183 ? 46.530 -12.940 28.481 1.00 108.08 ? 183 ASP A C 1 ATOM 1469 O O . ASP A 1 183 ? 45.315 -13.117 28.396 1.00 106.03 ? 183 ASP A O 1 ATOM 1470 C CB . ASP A 1 183 ? 47.910 -10.853 28.108 1.00 111.43 ? 183 ASP A CB 1 ATOM 1471 C CG . ASP A 1 183 ? 46.882 -9.806 28.538 1.00 112.63 ? 183 ASP A CG 1 ATOM 1472 O OD1 . ASP A 1 183 ? 45.805 -10.175 29.056 1.00 112.64 ? 183 ASP A OD1 1 ATOM 1473 O OD2 . ASP A 1 183 ? 47.167 -8.599 28.373 1.00 113.06 ? 183 ASP A OD2 1 ATOM 1474 N N . ALA A 1 184 ? 47.273 -13.454 29.460 1.00 109.65 ? 184 ALA A N 1 ATOM 1475 C CA . ALA A 1 184 ? 46.717 -14.316 30.518 1.00 111.04 ? 184 ALA A CA 1 ATOM 1476 C C . ALA A 1 184 ? 45.531 -13.694 31.265 1.00 112.16 ? 184 ALA A C 1 ATOM 1477 O O . ALA A 1 184 ? 44.608 -14.406 31.670 1.00 111.25 ? 184 ALA A O 1 ATOM 1478 C CB . ALA A 1 184 ? 47.808 -14.705 31.510 1.00 112.37 ? 184 ALA A CB 1 ATOM 1479 N N . ALA A 1 185 ? 45.568 -12.376 31.449 1.00 113.65 ? 185 ALA A N 1 ATOM 1480 C CA . ALA A 1 185 ? 44.503 -11.657 32.150 1.00 115.36 ? 185 ALA A CA 1 ATOM 1481 C C . ALA A 1 185 ? 43.194 -11.721 31.372 1.00 113.00 ? 185 ALA A C 1 ATOM 1482 O O . ALA A 1 185 ? 42.141 -12.012 31.934 1.00 113.46 ? 185 ALA A O 1 ATOM 1483 C CB . ALA A 1 185 ? 44.906 -10.210 32.387 1.00 117.29 ? 185 ALA A CB 1 ATOM 1484 N N . GLU A 1 186 ? 43.268 -11.455 30.074 1.00 111.40 ? 186 GLU A N 1 ATOM 1485 C CA . GLU A 1 186 ? 42.093 -11.524 29.202 1.00 110.12 ? 186 GLU A CA 1 ATOM 1486 C C . GLU A 1 186 ? 41.473 -12.929 29.143 1.00 108.28 ? 186 GLU A C 1 ATOM 1487 O O . GLU A 1 186 ? 40.253 -13.067 29.057 1.00 106.14 ? 186 GLU A O 1 ATOM 1488 C CB . GLU A 1 186 ? 42.461 -11.056 27.797 1.00 108.05 ? 186 GLU A CB 1 ATOM 1489 C CG . GLU A 1 186 ? 41.291 -10.970 26.834 1.00 107.05 ? 186 GLU A CG 1 ATOM 1490 C CD . GLU A 1 186 ? 41.667 -10.256 25.554 1.00 105.54 ? 186 GLU A CD 1 ATOM 1491 O OE1 . GLU A 1 186 ? 41.816 -9.017 25.593 1.00 106.65 ? 186 GLU A OE1 1 ATOM 1492 O OE2 . GLU A 1 186 ? 41.837 -10.936 24.519 1.00 105.21 ? 186 GLU A OE2 1 ATOM 1493 N N . GLN A 1 187 ? 42.314 -13.961 29.189 1.00 108.52 ? 187 GLN A N 1 ATOM 1494 C CA . GLN A 1 187 ? 41.846 -15.352 29.182 1.00 107.78 ? 187 GLN A CA 1 ATOM 1495 C C . GLN A 1 187 ? 40.916 -15.627 30.365 1.00 110.92 ? 187 GLN A C 1 ATOM 1496 O O . GLN A 1 187 ? 39.792 -16.106 30.185 1.00 110.83 ? 187 GLN A O 1 ATOM 1497 C CB . GLN A 1 187 ? 43.041 -16.319 29.209 1.00 106.83 ? 187 GLN A CB 1 ATOM 1498 C CG . GLN A 1 187 ? 42.684 -17.792 29.378 1.00 105.87 ? 187 GLN A CG 1 ATOM 1499 C CD . GLN A 1 187 ? 41.794 -18.323 28.266 1.00 102.22 ? 187 GLN A CD 1 ATOM 1500 O OE1 . GLN A 1 187 ? 42.002 -18.022 27.093 1.00 99.23 ? 187 GLN A OE1 1 ATOM 1501 N NE2 . GLN A 1 187 ? 40.804 -19.129 28.633 1.00 101.92 ? 187 GLN A NE2 1 ATOM 1502 N N . THR A 1 188 ? 41.389 -15.317 31.570 1.00 114.12 ? 188 THR A N 1 ATOM 1503 C CA . THR A 1 188 ? 40.595 -15.514 32.782 1.00 116.35 ? 188 THR A CA 1 ATOM 1504 C C . THR A 1 188 ? 39.428 -14.521 32.842 1.00 116.59 ? 188 THR A C 1 ATOM 1505 O O . THR A 1 188 ? 38.362 -14.841 33.367 1.00 118.20 ? 188 THR A O 1 ATOM 1506 C CB . THR A 1 188 ? 41.457 -15.405 34.061 1.00 119.71 ? 188 THR A CB 1 ATOM 1507 O OG1 . THR A 1 188 ? 41.988 -14.081 34.186 1.00 121.07 ? 188 THR A OG1 1 ATOM 1508 C CG2 . THR A 1 188 ? 42.608 -16.410 34.027 1.00 119.47 ? 188 THR A CG2 1 ATOM 1509 N N . LYS A 1 189 ? 39.628 -13.329 32.288 1.00 115.19 ? 189 LYS A N 1 ATOM 1510 C CA . LYS A 1 189 ? 38.576 -12.317 32.232 1.00 116.19 ? 189 LYS A CA 1 ATOM 1511 C C . LYS A 1 189 ? 37.363 -12.799 31.422 1.00 114.72 ? 189 LYS A C 1 ATOM 1512 O O . LYS A 1 189 ? 36.224 -12.580 31.830 1.00 115.31 ? 189 LYS A O 1 ATOM 1513 C CB . LYS A 1 189 ? 39.133 -11.019 31.640 1.00 116.46 ? 189 LYS A CB 1 ATOM 1514 C CG . LYS A 1 189 ? 38.183 -9.832 31.679 1.00 119.29 ? 189 LYS A CG 1 ATOM 1515 C CD . LYS A 1 189 ? 38.697 -8.706 30.794 1.00 119.64 ? 189 LYS A CD 1 ATOM 1516 C CE . LYS A 1 189 ? 37.664 -7.606 30.611 1.00 121.12 ? 189 LYS A CE 1 ATOM 1517 N NZ . LYS A 1 189 ? 37.970 -6.779 29.411 1.00 119.29 ? 189 LYS A NZ 1 ATOM 1518 N N . LEU A 1 190 ? 37.611 -13.457 30.289 1.00 111.42 ? 190 LEU A N 1 ATOM 1519 C CA . LEU A 1 190 ? 36.533 -13.944 29.415 1.00 110.28 ? 190 LEU A CA 1 ATOM 1520 C C . LEU A 1 190 ? 36.054 -15.356 29.759 1.00 110.28 ? 190 LEU A C 1 ATOM 1521 O O . LEU A 1 190 ? 34.855 -15.638 29.691 1.00 109.84 ? 190 LEU A O 1 ATOM 1522 C CB . LEU A 1 190 ? 36.970 -13.920 27.941 1.00 106.84 ? 190 LEU A CB 1 ATOM 1523 C CG . LEU A 1 190 ? 37.448 -12.594 27.336 1.00 106.93 ? 190 LEU A CG 1 ATOM 1524 C CD1 . LEU A 1 190 ? 37.388 -12.655 25.819 1.00 103.59 ? 190 LEU A CD1 1 ATOM 1525 C CD2 . LEU A 1 190 ? 36.647 -11.406 27.847 1.00 109.56 ? 190 LEU A CD2 1 ATOM 1526 N N . TYR A 1 191 ? 36.986 -16.241 30.110 1.00 110.54 ? 191 TYR A N 1 ATOM 1527 C CA . TYR A 1 191 ? 36.682 -17.670 30.247 1.00 110.39 ? 191 TYR A CA 1 ATOM 1528 C C . TYR A 1 191 ? 37.049 -18.306 31.599 1.00 113.91 ? 191 TYR A C 1 ATOM 1529 O O . TYR A 1 191 ? 36.791 -19.495 31.800 1.00 114.64 ? 191 TYR A O 1 ATOM 1530 C CB . TYR A 1 191 ? 37.384 -18.443 29.125 1.00 107.80 ? 191 TYR A CB 1 ATOM 1531 C CG . TYR A 1 191 ? 37.279 -17.786 27.759 1.00 104.74 ? 191 TYR A CG 1 ATOM 1532 C CD1 . TYR A 1 191 ? 36.077 -17.785 27.055 1.00 103.35 ? 191 TYR A CD1 1 ATOM 1533 C CD2 . TYR A 1 191 ? 38.381 -17.163 27.175 1.00 103.08 ? 191 TYR A CD2 1 ATOM 1534 C CE1 . TYR A 1 191 ? 35.977 -17.184 25.806 1.00 100.56 ? 191 TYR A CE1 1 ATOM 1535 C CE2 . TYR A 1 191 ? 38.287 -16.558 25.931 1.00 100.22 ? 191 TYR A CE2 1 ATOM 1536 C CZ . TYR A 1 191 ? 37.083 -16.573 25.252 1.00 98.54 ? 191 TYR A CZ 1 ATOM 1537 O OH . TYR A 1 191 ? 36.978 -15.976 24.020 1.00 94.88 ? 191 TYR A OH 1 ATOM 1538 N N . GLN A 1 192 ? 37.641 -17.532 32.511 1.00 115.99 ? 192 GLN A N 1 ATOM 1539 C CA . GLN A 1 192 ? 38.091 -18.025 33.830 1.00 119.51 ? 192 GLN A CA 1 ATOM 1540 C C . GLN A 1 192 ? 39.270 -18.994 33.768 1.00 118.59 ? 192 GLN A C 1 ATOM 1541 O O . GLN A 1 192 ? 40.353 -18.706 34.288 1.00 118.45 ? 192 GLN A O 1 ATOM 1542 C CB . GLN A 1 192 ? 36.944 -18.688 34.608 1.00 122.26 ? 192 GLN A CB 1 ATOM 1543 C CG . GLN A 1 192 ? 35.861 -17.728 35.056 1.00 124.09 ? 192 GLN A CG 1 ATOM 1544 C CD . GLN A 1 192 ? 36.048 -17.265 36.481 1.00 125.83 ? 192 GLN A CD 1 ATOM 1545 O OE1 . GLN A 1 192 ? 35.370 -17.740 37.379 1.00 129.00 ? 192 GLN A OE1 1 ATOM 1546 N NE2 . GLN A 1 192 ? 36.981 -16.351 36.698 1.00 126.58 ? 192 GLN A NE2 1 ATOM 1547 N N . ASN A 1 193 ? 39.039 -20.147 33.147 1.00 117.12 ? 193 ASN A N 1 ATOM 1548 C CA . ASN A 1 193 ? 40.012 -21.231 33.112 1.00 117.34 ? 193 ASN A CA 1 ATOM 1549 C C . ASN A 1 193 ? 41.263 -20.803 32.350 1.00 115.53 ? 193 ASN A C 1 ATOM 1550 O O . ASN A 1 193 ? 41.160 -20.317 31.227 1.00 112.64 ? 193 ASN A O 1 ATOM 1551 C CB . ASN A 1 193 ? 39.393 -22.471 32.460 1.00 116.78 ? 193 ASN A CB 1 ATOM 1552 C CG . ASN A 1 193 ? 38.026 -22.816 33.034 1.00 119.60 ? 193 ASN A CG 1 ATOM 1553 O OD1 . ASN A 1 193 ? 37.533 -22.145 33.944 1.00 124.23 ? 193 ASN A OD1 1 ATOM 1554 N ND2 . ASN A 1 193 ? 37.407 -23.862 32.502 1.00 118.50 ? 193 ASN A ND2 1 ATOM 1555 N N . PRO A 1 194 ? 42.448 -20.963 32.964 1.00 117.20 ? 194 PRO A N 1 ATOM 1556 C CA . PRO A 1 194 ? 43.677 -20.513 32.310 1.00 115.63 ? 194 PRO A CA 1 ATOM 1557 C C . PRO A 1 194 ? 44.120 -21.425 31.164 1.00 112.35 ? 194 PRO A C 1 ATOM 1558 O O . PRO A 1 194 ? 44.693 -20.941 30.190 1.00 109.17 ? 194 PRO A O 1 ATOM 1559 C CB . PRO A 1 194 ? 44.701 -20.531 33.448 1.00 118.89 ? 194 PRO A CB 1 ATOM 1560 C CG . PRO A 1 194 ? 44.217 -21.596 34.367 1.00 120.68 ? 194 PRO A CG 1 ATOM 1561 C CD . PRO A 1 194 ? 42.716 -21.579 34.278 1.00 120.29 ? 194 PRO A CD 1 ATOM 1562 N N . THR A 1 195 ? 43.859 -22.726 31.290 1.00 112.05 ? 195 THR A N 1 ATOM 1563 C CA . THR A 1 195 ? 44.227 -23.705 30.267 1.00 109.57 ? 195 THR A CA 1 ATOM 1564 C C . THR A 1 195 ? 42.968 -24.340 29.681 1.00 106.99 ? 195 THR A C 1 ATOM 1565 O O . THR A 1 195 ? 42.268 -25.092 30.359 1.00 107.45 ? 195 THR A O 1 ATOM 1566 C CB . THR A 1 195 ? 45.132 -24.809 30.854 1.00 111.17 ? 195 THR A CB 1 ATOM 1567 O OG1 . THR A 1 195 ? 46.242 -24.209 31.528 1.00 112.86 ? 195 THR A OG1 1 ATOM 1568 C CG2 . THR A 1 195 ? 45.653 -25.733 29.759 1.00 109.44 ? 195 THR A CG2 1 ATOM 1569 N N . THR A 1 196 ? 42.687 -24.037 28.418 1.00 104.34 ? 196 THR A N 1 ATOM 1570 C CA . THR A 1 196 ? 41.457 -24.490 27.774 1.00 102.70 ? 196 THR A CA 1 ATOM 1571 C C . THR A 1 196 ? 41.743 -25.222 26.465 1.00 100.36 ? 196 THR A C 1 ATOM 1572 O O . THR A 1 196 ? 42.898 -25.385 26.065 1.00 97.45 ? 196 THR A O 1 ATOM 1573 C CB . THR A 1 196 ? 40.514 -23.304 27.502 1.00 101.92 ? 196 THR A CB 1 ATOM 1574 O OG1 . THR A 1 196 ? 41.145 -22.394 26.597 1.00 100.17 ? 196 THR A OG1 1 ATOM 1575 C CG2 . THR A 1 196 ? 40.182 -22.577 28.796 1.00 104.69 ? 196 THR A CG2 1 ATOM 1576 N N . TYR A 1 197 ? 40.676 -25.672 25.812 1.00 99.95 ? 197 TYR A N 1 ATOM 1577 C CA . TYR A 1 197 ? 40.782 -26.428 24.578 1.00 97.96 ? 197 TYR A CA 1 ATOM 1578 C C . TYR A 1 197 ? 39.429 -26.524 23.894 1.00 98.74 ? 197 TYR A C 1 ATOM 1579 O O . TYR A 1 197 ? 38.401 -26.196 24.485 1.00 99.62 ? 197 TYR A O 1 ATOM 1580 C CB . TYR A 1 197 ? 41.278 -27.844 24.872 1.00 98.67 ? 197 TYR A CB 1 ATOM 1581 C CG . TYR A 1 197 ? 40.322 -28.652 25.725 1.00 99.84 ? 197 TYR A CG 1 ATOM 1582 C CD1 . TYR A 1 197 ? 40.263 -28.470 27.109 1.00 102.38 ? 197 TYR A CD1 1 ATOM 1583 C CD2 . TYR A 1 197 ? 39.469 -29.591 25.150 1.00 98.39 ? 197 TYR A CD2 1 ATOM 1584 C CE1 . TYR A 1 197 ? 39.387 -29.204 27.893 1.00 103.36 ? 197 TYR A CE1 1 ATOM 1585 C CE2 . TYR A 1 197 ? 38.591 -30.331 25.925 1.00 100.09 ? 197 TYR A CE2 1 ATOM 1586 C CZ . TYR A 1 197 ? 38.553 -30.135 27.298 1.00 102.85 ? 197 TYR A CZ 1 ATOM 1587 O OH . TYR A 1 197 ? 37.678 -30.868 28.071 1.00 103.14 ? 197 TYR A OH 1 ATOM 1588 N N . ILE A 1 198 ? 39.444 -26.970 22.643 1.00 97.98 ? 198 ILE A N 1 ATOM 1589 C CA . ILE A 1 198 ? 38.228 -27.347 21.935 1.00 99.22 ? 198 ILE A CA 1 ATOM 1590 C C . ILE A 1 198 ? 38.501 -28.658 21.212 1.00 98.77 ? 198 ILE A C 1 ATOM 1591 O O . ILE A 1 198 ? 39.402 -28.728 20.374 1.00 98.42 ? 198 ILE A O 1 ATOM 1592 C CB . ILE A 1 198 ? 37.804 -26.298 20.888 1.00 99.72 ? 198 ILE A CB 1 ATOM 1593 C CG1 . ILE A 1 198 ? 37.660 -24.913 21.521 1.00 100.63 ? 198 ILE A CG1 1 ATOM 1594 C CG2 . ILE A 1 198 ? 36.489 -26.707 20.230 1.00 99.80 ? 198 ILE A CG2 1 ATOM 1595 C CD1 . ILE A 1 198 ? 37.584 -23.803 20.497 1.00 99.95 ? 198 ILE A CD1 1 ATOM 1596 N N . SER A 1 199 ? 37.734 -29.693 21.537 1.00 98.31 ? 199 SER A N 1 ATOM 1597 C CA . SER A 1 199 ? 37.871 -30.976 20.865 1.00 97.86 ? 199 SER A CA 1 ATOM 1598 C C . SER A 1 199 ? 36.669 -31.204 19.958 1.00 95.91 ? 199 SER A C 1 ATOM 1599 O O . SER A 1 199 ? 35.526 -31.079 20.390 1.00 95.65 ? 199 SER A O 1 ATOM 1600 C CB . SER A 1 199 ? 38.014 -32.110 21.882 1.00 100.42 ? 199 SER A CB 1 ATOM 1601 O OG . SER A 1 199 ? 36.784 -32.393 22.516 1.00 102.53 ? 199 SER A OG 1 ATOM 1602 N N . VAL A 1 200 ? 36.937 -31.530 18.698 1.00 94.80 ? 200 VAL A N 1 ATOM 1603 C CA . VAL A 1 200 ? 35.882 -31.735 17.712 1.00 94.51 ? 200 VAL A CA 1 ATOM 1604 C C . VAL A 1 200 ? 36.048 -33.105 17.072 1.00 94.46 ? 200 VAL A C 1 ATOM 1605 O O . VAL A 1 200 ? 37.143 -33.473 16.642 1.00 93.79 ? 200 VAL A O 1 ATOM 1606 C CB . VAL A 1 200 ? 35.906 -30.653 16.613 1.00 92.47 ? 200 VAL A CB 1 ATOM 1607 C CG1 . VAL A 1 200 ? 34.582 -30.630 15.863 1.00 92.12 ? 200 VAL A CG1 1 ATOM 1608 C CG2 . VAL A 1 200 ? 36.196 -29.284 17.214 1.00 92.83 ? 200 VAL A CG2 1 ATOM 1609 N N . GLY A 1 201 ? 34.955 -33.857 17.015 1.00 96.21 ? 201 GLY A N 1 ATOM 1610 C CA . GLY A 1 201 ? 34.973 -35.193 16.442 1.00 97.37 ? 201 GLY A CA 1 ATOM 1611 C C . GLY A 1 201 ? 33.792 -35.435 15.529 1.00 97.17 ? 201 GLY A C 1 ATOM 1612 O O . GLY A 1 201 ? 32.717 -34.879 15.735 1.00 96.67 ? 201 GLY A O 1 ATOM 1613 N N . THR A 1 202 ? 34.019 -36.247 14.500 1.00 98.18 ? 202 THR A N 1 ATOM 1614 C CA . THR A 1 202 ? 32.957 -36.776 13.648 1.00 99.64 ? 202 THR A CA 1 ATOM 1615 C C . THR A 1 202 ? 33.319 -38.221 13.336 1.00 103.53 ? 202 THR A C 1 ATOM 1616 O O . THR A 1 202 ? 34.161 -38.814 14.015 1.00 104.76 ? 202 THR A O 1 ATOM 1617 C CB . THR A 1 202 ? 32.816 -35.994 12.320 1.00 97.50 ? 202 THR A CB 1 ATOM 1618 O OG1 . THR A 1 202 ? 33.948 -36.254 11.477 1.00 94.35 ? 202 THR A OG1 1 ATOM 1619 C CG2 . THR A 1 202 ? 32.690 -34.506 12.571 1.00 96.34 ? 202 THR A CG2 1 ATOM 1620 N N . SER A 1 203 ? 32.685 -38.785 12.312 1.00 106.32 ? 203 SER A N 1 ATOM 1621 C CA . SER A 1 203 ? 33.046 -40.106 11.814 1.00 108.94 ? 203 SER A CA 1 ATOM 1622 C C . SER A 1 203 ? 34.531 -40.170 11.471 1.00 108.05 ? 203 SER A C 1 ATOM 1623 O O . SER A 1 203 ? 35.217 -41.115 11.853 1.00 110.68 ? 203 SER A O 1 ATOM 1624 C CB . SER A 1 203 ? 32.216 -40.446 10.576 1.00 110.45 ? 203 SER A CB 1 ATOM 1625 O OG . SER A 1 203 ? 32.726 -41.589 9.918 1.00 115.23 ? 203 SER A OG 1 ATOM 1626 N N . THR A 1 204 ? 35.015 -39.159 10.752 1.00 105.10 ? 204 THR A N 1 ATOM 1627 C CA . THR A 1 204 ? 36.411 -39.100 10.326 1.00 103.39 ? 204 THR A CA 1 ATOM 1628 C C . THR A 1 204 ? 37.239 -38.136 11.171 1.00 103.72 ? 204 THR A C 1 ATOM 1629 O O . THR A 1 204 ? 38.385 -38.434 11.508 1.00 107.44 ? 204 THR A O 1 ATOM 1630 C CB . THR A 1 204 ? 36.525 -38.659 8.855 1.00 100.09 ? 204 THR A CB 1 ATOM 1631 O OG1 . THR A 1 204 ? 35.924 -37.369 8.691 1.00 96.12 ? 204 THR A OG1 1 ATOM 1632 C CG2 . THR A 1 204 ? 35.836 -39.660 7.941 1.00 100.78 ? 204 THR A CG2 1 ATOM 1633 N N . LEU A 1 205 ? 36.659 -36.987 11.512 1.00 101.18 ? 205 LEU A N 1 ATOM 1634 C CA . LEU A 1 205 ? 37.411 -35.911 12.154 1.00 98.86 ? 205 LEU A CA 1 ATOM 1635 C C . LEU A 1 205 ? 37.831 -36.243 13.595 1.00 98.82 ? 205 LEU A C 1 ATOM 1636 O O . LEU A 1 205 ? 37.067 -36.841 14.362 1.00 97.94 ? 205 LEU A O 1 ATOM 1637 C CB . LEU A 1 205 ? 36.604 -34.607 12.127 1.00 98.82 ? 205 LEU A CB 1 ATOM 1638 C CG . LEU A 1 205 ? 37.393 -33.323 12.413 1.00 99.52 ? 205 LEU A CG 1 ATOM 1639 C CD1 . LEU A 1 205 ? 38.451 -33.081 11.341 1.00 98.25 ? 205 LEU A CD1 1 ATOM 1640 C CD2 . LEU A 1 205 ? 36.461 -32.126 12.519 1.00 98.36 ? 205 LEU A CD2 1 ATOM 1641 N N . ASN A 1 206 ? 39.057 -35.846 13.939 1.00 95.79 ? 206 ASN A N 1 ATOM 1642 C CA . ASN A 1 206 ? 39.612 -36.044 15.275 1.00 95.03 ? 206 ASN A CA 1 ATOM 1643 C C . ASN A 1 206 ? 40.479 -34.844 15.671 1.00 92.74 ? 206 ASN A C 1 ATOM 1644 O O . ASN A 1 206 ? 41.703 -34.910 15.630 1.00 91.80 ? 206 ASN A O 1 ATOM 1645 C CB . ASN A 1 206 ? 40.425 -37.342 15.319 1.00 96.10 ? 206 ASN A CB 1 ATOM 1646 C CG . ASN A 1 206 ? 40.970 -37.651 16.704 1.00 97.69 ? 206 ASN A CG 1 ATOM 1647 O OD1 . ASN A 1 206 ? 40.344 -37.345 17.719 1.00 97.33 ? 206 ASN A OD1 1 ATOM 1648 N ND2 . ASN A 1 206 ? 42.148 -38.263 16.748 1.00 99.29 ? 206 ASN A ND2 1 ATOM 1649 N N . GLN A 1 207 ? 39.828 -33.756 16.069 1.00 91.01 ? 207 GLN A N 1 ATOM 1650 C CA . GLN A 1 207 ? 40.509 -32.485 16.297 1.00 90.40 ? 207 GLN A CA 1 ATOM 1651 C C . GLN A 1 207 ? 40.577 -32.116 17.779 1.00 92.01 ? 207 GLN A C 1 ATOM 1652 O O . GLN A 1 207 ? 39.687 -32.455 18.554 1.00 92.97 ? 207 GLN A O 1 ATOM 1653 C CB . GLN A 1 207 ? 39.781 -31.391 15.517 1.00 88.57 ? 207 GLN A CB 1 ATOM 1654 C CG . GLN A 1 207 ? 40.331 -29.986 15.691 1.00 88.02 ? 207 GLN A CG 1 ATOM 1655 C CD . GLN A 1 207 ? 39.549 -28.977 14.881 1.00 88.44 ? 207 GLN A CD 1 ATOM 1656 O OE1 . GLN A 1 207 ? 38.803 -28.166 15.431 1.00 90.31 ? 207 GLN A OE1 1 ATOM 1657 N NE2 . GLN A 1 207 ? 39.694 -29.036 13.561 1.00 88.43 ? 207 GLN A NE2 1 ATOM 1658 N N . ARG A 1 208 ? 41.650 -31.426 18.159 1.00 93.08 ? 208 ARG A N 1 ATOM 1659 C CA . ARG A 1 208 ? 41.758 -30.804 19.475 1.00 96.37 ? 208 ARG A CA 1 ATOM 1660 C C . ARG A 1 208 ? 42.565 -29.511 19.365 1.00 97.11 ? 208 ARG A C 1 ATOM 1661 O O . ARG A 1 208 ? 43.777 -29.542 19.140 1.00 97.78 ? 208 ARG A O 1 ATOM 1662 C CB . ARG A 1 208 ? 42.408 -31.747 20.489 1.00 99.42 ? 208 ARG A CB 1 ATOM 1663 C CG . ARG A 1 208 ? 42.235 -31.294 21.934 1.00 102.25 ? 208 ARG A CG 1 ATOM 1664 C CD . ARG A 1 208 ? 43.206 -31.993 22.876 1.00 105.10 ? 208 ARG A CD 1 ATOM 1665 N NE . ARG A 1 208 ? 42.896 -31.736 24.283 1.00 107.02 ? 208 ARG A NE 1 ATOM 1666 C CZ . ARG A 1 208 ? 41.915 -32.327 24.968 1.00 109.61 ? 208 ARG A CZ 1 ATOM 1667 N NH1 . ARG A 1 208 ? 41.117 -33.220 24.388 1.00 109.51 ? 208 ARG A NH1 1 ATOM 1668 N NH2 . ARG A 1 208 ? 41.723 -32.020 26.249 1.00 112.69 ? 208 ARG A NH2 1 ATOM 1669 N N . LEU A 1 209 ? 41.885 -28.380 19.523 1.00 97.29 ? 209 LEU A N 1 ATOM 1670 C CA . LEU A 1 209 ? 42.515 -27.071 19.401 1.00 97.22 ? 209 LEU A CA 1 ATOM 1671 C C . LEU A 1 209 ? 42.856 -26.527 20.782 1.00 99.30 ? 209 LEU A C 1 ATOM 1672 O O . LEU A 1 209 ? 42.125 -26.763 21.741 1.00 100.29 ? 209 LEU A O 1 ATOM 1673 C CB . LEU A 1 209 ? 41.574 -26.098 18.688 1.00 96.71 ? 209 LEU A CB 1 ATOM 1674 C CG . LEU A 1 209 ? 40.996 -26.548 17.340 1.00 96.17 ? 209 LEU A CG 1 ATOM 1675 C CD1 . LEU A 1 209 ? 39.901 -25.593 16.887 1.00 95.33 ? 209 LEU A CD1 1 ATOM 1676 C CD2 . LEU A 1 209 ? 42.087 -26.666 16.285 1.00 95.14 ? 209 LEU A CD2 1 ATOM 1677 N N . VAL A 1 210 ? 43.970 -25.807 20.877 1.00 99.78 ? 210 VAL A N 1 ATOM 1678 C CA . VAL A 1 210 ? 44.324 -25.081 22.096 1.00 103.06 ? 210 VAL A CA 1 ATOM 1679 C C . VAL A 1 210 ? 44.608 -23.617 21.745 1.00 102.60 ? 210 VAL A C 1 ATOM 1680 O O . VAL A 1 210 ? 45.259 -23.341 20.733 1.00 101.10 ? 210 VAL A O 1 ATOM 1681 C CB . VAL A 1 210 ? 45.528 -25.712 22.841 1.00 105.33 ? 210 VAL A CB 1 ATOM 1682 C CG1 . VAL A 1 210 ? 45.151 -27.080 23.387 1.00 106.08 ? 210 VAL A CG1 1 ATOM 1683 C CG2 . VAL A 1 210 ? 46.760 -25.816 21.950 1.00 105.36 ? 210 VAL A CG2 1 ATOM 1684 N N . PRO A 1 211 ? 44.100 -22.670 22.561 1.00 104.41 ? 211 PRO A N 1 ATOM 1685 C CA . PRO A 1 211 ? 44.364 -21.261 22.264 1.00 104.44 ? 211 PRO A CA 1 ATOM 1686 C C . PRO A 1 211 ? 45.828 -20.893 22.470 1.00 105.35 ? 211 PRO A C 1 ATOM 1687 O O . PRO A 1 211 ? 46.405 -21.202 23.511 1.00 106.23 ? 211 PRO A O 1 ATOM 1688 C CB . PRO A 1 211 ? 43.479 -20.499 23.262 1.00 105.53 ? 211 PRO A CB 1 ATOM 1689 C CG . PRO A 1 211 ? 42.520 -21.497 23.797 1.00 105.67 ? 211 PRO A CG 1 ATOM 1690 C CD . PRO A 1 211 ? 43.194 -22.828 23.711 1.00 105.45 ? 211 PRO A CD 1 ATOM 1691 N N . ARG A 1 212 ? 46.416 -20.262 21.462 1.00 105.79 ? 212 ARG A N 1 ATOM 1692 C CA . ARG A 1 212 ? 47.787 -19.788 21.525 1.00 108.36 ? 212 ARG A CA 1 ATOM 1693 C C . ARG A 1 212 ? 47.803 -18.306 21.885 1.00 109.27 ? 212 ARG A C 1 ATOM 1694 O O . ARG A 1 212 ? 47.102 -17.500 21.270 1.00 105.20 ? 212 ARG A O 1 ATOM 1695 C CB . ARG A 1 212 ? 48.486 -20.054 20.186 1.00 108.29 ? 212 ARG A CB 1 ATOM 1696 C CG . ARG A 1 212 ? 48.936 -21.504 20.035 1.00 108.97 ? 212 ARG A CG 1 ATOM 1697 C CD . ARG A 1 212 ? 48.454 -22.156 18.751 1.00 107.63 ? 212 ARG A CD 1 ATOM 1698 N NE . ARG A 1 212 ? 49.010 -21.528 17.550 1.00 106.42 ? 212 ARG A NE 1 ATOM 1699 C CZ . ARG A 1 212 ? 48.300 -21.058 16.523 1.00 105.62 ? 212 ARG A CZ 1 ATOM 1700 N NH1 . ARG A 1 212 ? 46.970 -21.128 16.497 1.00 103.74 ? 212 ARG A NH1 1 ATOM 1701 N NH2 . ARG A 1 212 ? 48.933 -20.520 15.490 1.00 106.74 ? 212 ARG A NH2 1 ATOM 1702 N N . ILE A 1 213 ? 48.596 -17.966 22.900 1.00 114.45 ? 213 ILE A N 1 ATOM 1703 C CA . ILE A 1 213 ? 48.705 -16.595 23.398 1.00 117.21 ? 213 ILE A CA 1 ATOM 1704 C C . ILE A 1 213 ? 50.017 -15.967 22.932 1.00 119.30 ? 213 ILE A C 1 ATOM 1705 O O . ILE A 1 213 ? 51.066 -16.617 22.933 1.00 120.86 ? 213 ILE A O 1 ATOM 1706 C CB . ILE A 1 213 ? 48.616 -16.552 24.941 1.00 118.15 ? 213 ILE A CB 1 ATOM 1707 C CG1 . ILE A 1 213 ? 47.205 -16.947 25.390 1.00 117.20 ? 213 ILE A CG1 1 ATOM 1708 C CG2 . ILE A 1 213 ? 48.968 -15.164 25.471 1.00 119.87 ? 213 ILE A CG2 1 ATOM 1709 C CD1 . ILE A 1 213 ? 47.094 -17.303 26.857 1.00 119.45 ? 213 ILE A CD1 1 ATOM 1710 N N . ALA A 1 214 ? 49.939 -14.701 22.528 1.00 119.41 ? 214 ALA A N 1 ATOM 1711 C CA . ALA A 1 214 ? 51.110 -13.934 22.121 1.00 120.03 ? 214 ALA A CA 1 ATOM 1712 C C . ALA A 1 214 ? 50.758 -12.458 22.000 1.00 120.70 ? 214 ALA A C 1 ATOM 1713 O O . ALA A 1 214 ? 49.592 -12.098 21.815 1.00 119.60 ? 214 ALA A O 1 ATOM 1714 C CB . ALA A 1 214 ? 51.655 -14.448 20.795 1.00 118.08 ? 214 ALA A CB 1 ATOM 1715 N N . THR A 1 215 ? 51.774 -11.610 22.117 1.00 122.49 ? 215 THR A N 1 ATOM 1716 C CA . THR A 1 215 ? 51.622 -10.188 21.843 1.00 121.54 ? 215 THR A CA 1 ATOM 1717 C C . THR A 1 215 ? 51.532 -10.011 20.334 1.00 116.58 ? 215 THR A C 1 ATOM 1718 O O . THR A 1 215 ? 52.407 -10.467 19.594 1.00 116.51 ? 215 THR A O 1 ATOM 1719 C CB . THR A 1 215 ? 52.808 -9.374 22.392 1.00 124.67 ? 215 THR A CB 1 ATOM 1720 O OG1 . THR A 1 215 ? 52.934 -9.608 23.798 1.00 127.50 ? 215 THR A OG1 1 ATOM 1721 C CG2 . THR A 1 215 ? 52.608 -7.879 22.145 1.00 125.87 ? 215 THR A CG2 1 ATOM 1722 N N . ARG A 1 216 ? 50.467 -9.360 19.881 1.00 112.18 ? 216 ARG A N 1 ATOM 1723 C CA . ARG A 1 216 ? 50.214 -9.209 18.458 1.00 108.00 ? 216 ARG A CA 1 ATOM 1724 C C . ARG A 1 216 ? 49.873 -7.770 18.109 1.00 106.39 ? 216 ARG A C 1 ATOM 1725 O O . ARG A 1 216 ? 49.322 -7.037 18.928 1.00 105.93 ? 216 ARG A O 1 ATOM 1726 C CB . ARG A 1 216 ? 49.075 -10.137 18.037 1.00 105.51 ? 216 ARG A CB 1 ATOM 1727 C CG . ARG A 1 216 ? 49.419 -11.614 18.145 1.00 105.31 ? 216 ARG A CG 1 ATOM 1728 C CD . ARG A 1 216 ? 48.271 -12.493 17.669 1.00 103.28 ? 216 ARG A CD 1 ATOM 1729 N NE . ARG A 1 216 ? 47.260 -12.697 18.708 1.00 103.97 ? 216 ARG A NE 1 ATOM 1730 C CZ . ARG A 1 216 ? 47.278 -13.671 19.620 1.00 103.10 ? 216 ARG A CZ 1 ATOM 1731 N NH1 . ARG A 1 216 ? 48.262 -14.562 19.655 1.00 103.26 ? 216 ARG A NH1 1 ATOM 1732 N NH2 . ARG A 1 216 ? 46.297 -13.754 20.513 1.00 103.48 ? 216 ARG A NH2 1 ATOM 1733 N N . SER A 1 217 ? 50.205 -7.376 16.883 1.00 104.84 ? 217 SER A N 1 ATOM 1734 C CA . SER A 1 217 ? 49.865 -6.054 16.371 1.00 104.64 ? 217 SER A CA 1 ATOM 1735 C C . SER A 1 217 ? 48.349 -5.903 16.270 1.00 103.37 ? 217 SER A C 1 ATOM 1736 O O . SER A 1 217 ? 47.624 -6.892 16.160 1.00 100.16 ? 217 SER A O 1 ATOM 1737 C CB . SER A 1 217 ? 50.506 -5.835 15.000 1.00 103.93 ? 217 SER A CB 1 ATOM 1738 O OG . SER A 1 217 ? 51.897 -6.101 15.045 1.00 105.80 ? 217 SER A OG 1 ATOM 1739 N N . LYS A 1 218 ? 47.875 -4.662 16.312 1.00 104.88 ? 218 LYS A N 1 ATOM 1740 C CA . LYS A 1 218 ? 46.439 -4.387 16.315 1.00 103.94 ? 218 LYS A CA 1 ATOM 1741 C C . LYS A 1 218 ? 45.874 -4.239 14.906 1.00 102.00 ? 218 LYS A C 1 ATOM 1742 O O . LYS A 1 218 ? 46.103 -3.233 14.234 1.00 103.43 ? 218 LYS A O 1 ATOM 1743 C CB . LYS A 1 218 ? 46.125 -3.134 17.137 1.00 105.69 ? 218 LYS A CB 1 ATOM 1744 C CG . LYS A 1 218 ? 46.242 -3.343 18.635 1.00 107.07 ? 218 LYS A CG 1 ATOM 1745 C CD . LYS A 1 218 ? 45.683 -2.159 19.406 1.00 109.37 ? 218 LYS A CD 1 ATOM 1746 C CE . LYS A 1 218 ? 45.876 -2.334 20.903 1.00 111.31 ? 218 LYS A CE 1 ATOM 1747 N NZ . LYS A 1 218 ? 45.127 -1.306 21.674 1.00 114.05 ? 218 LYS A NZ 1 ATOM 1748 N N . VAL A 1 219 ? 45.132 -5.251 14.472 1.00 98.70 ? 219 VAL A N 1 ATOM 1749 C CA . VAL A 1 219 ? 44.384 -5.191 13.230 1.00 96.88 ? 219 VAL A CA 1 ATOM 1750 C C . VAL A 1 219 ? 42.932 -4.910 13.597 1.00 97.26 ? 219 VAL A C 1 ATOM 1751 O O . VAL A 1 219 ? 42.367 -5.589 14.450 1.00 98.07 ? 219 VAL A O 1 ATOM 1752 C CB . VAL A 1 219 ? 44.492 -6.518 12.464 1.00 95.71 ? 219 VAL A CB 1 ATOM 1753 C CG1 . VAL A 1 219 ? 43.769 -6.424 11.127 1.00 93.94 ? 219 VAL A CG1 1 ATOM 1754 C CG2 . VAL A 1 219 ? 45.956 -6.896 12.272 1.00 96.04 ? 219 VAL A CG2 1 ATOM 1755 N N . ASN A 1 220 ? 42.337 -3.901 12.967 1.00 98.07 ? 220 ASN A N 1 ATOM 1756 C CA . ASN A 1 220 ? 41.012 -3.405 13.359 1.00 99.84 ? 220 ASN A CA 1 ATOM 1757 C C . ASN A 1 220 ? 40.911 -3.126 14.865 1.00 98.81 ? 220 ASN A C 1 ATOM 1758 O O . ASN A 1 220 ? 39.855 -3.311 15.474 1.00 98.99 ? 220 ASN A O 1 ATOM 1759 C CB . ASN A 1 220 ? 39.909 -4.379 12.918 1.00 102.66 ? 220 ASN A CB 1 ATOM 1760 C CG . ASN A 1 220 ? 39.489 -4.177 11.474 1.00 104.31 ? 220 ASN A CG 1 ATOM 1761 O OD1 . ASN A 1 220 ? 38.300 -4.049 11.179 1.00 107.96 ? 220 ASN A OD1 1 ATOM 1762 N ND2 . ASN A 1 220 ? 40.461 -4.147 10.566 1.00 104.86 ? 220 ASN A ND2 1 ATOM 1763 N N . GLY A 1 221 ? 42.014 -2.673 15.454 1.00 97.00 ? 221 GLY A N 1 ATOM 1764 C CA . GLY A 1 221 ? 42.066 -2.395 16.881 1.00 97.57 ? 221 GLY A CA 1 ATOM 1765 C C . GLY A 1 221 ? 41.967 -3.611 17.789 1.00 95.43 ? 221 GLY A C 1 ATOM 1766 O O . GLY A 1 221 ? 41.548 -3.486 18.933 1.00 96.69 ? 221 GLY A O 1 ATOM 1767 N N . GLN A 1 222 ? 42.359 -4.784 17.295 1.00 92.69 ? 222 GLN A N 1 ATOM 1768 C CA . GLN A 1 222 ? 42.331 -6.004 18.105 1.00 92.52 ? 222 GLN A CA 1 ATOM 1769 C C . GLN A 1 222 ? 43.697 -6.683 18.140 1.00 91.82 ? 222 GLN A C 1 ATOM 1770 O O . GLN A 1 222 ? 44.337 -6.850 17.099 1.00 90.32 ? 222 GLN A O 1 ATOM 1771 C CB . GLN A 1 222 ? 41.292 -6.996 17.566 1.00 90.20 ? 222 GLN A CB 1 ATOM 1772 C CG . GLN A 1 222 ? 39.896 -6.422 17.355 1.00 90.80 ? 222 GLN A CG 1 ATOM 1773 C CD . GLN A 1 222 ? 39.313 -5.744 18.588 1.00 92.83 ? 222 GLN A CD 1 ATOM 1774 O OE1 . GLN A 1 222 ? 39.580 -6.140 19.727 1.00 92.67 ? 222 GLN A OE1 1 ATOM 1775 N NE2 . GLN A 1 222 ? 38.502 -4.716 18.360 1.00 93.68 ? 222 GLN A NE2 1 ATOM 1776 N N . SER A 1 223 ? 44.130 -7.065 19.344 1.00 92.65 ? 223 SER A N 1 ATOM 1777 C CA . SER A 1 223 ? 45.342 -7.866 19.542 1.00 93.35 ? 223 SER A CA 1 ATOM 1778 C C . SER A 1 223 ? 45.010 -9.351 19.638 1.00 92.57 ? 223 SER A C 1 ATOM 1779 O O . SER A 1 223 ? 45.893 -10.199 19.516 1.00 92.14 ? 223 SER A O 1 ATOM 1780 C CB . SER A 1 223 ? 46.072 -7.436 20.815 1.00 96.21 ? 223 SER A CB 1 ATOM 1781 O OG . SER A 1 223 ? 46.403 -6.060 20.770 1.00 98.74 ? 223 SER A OG 1 ATOM 1782 N N . GLY A 1 224 ? 43.739 -9.660 19.888 1.00 92.99 ? 224 GLY A N 1 ATOM 1783 C CA . GLY A 1 224 ? 43.259 -11.035 19.863 1.00 91.39 ? 224 GLY A CA 1 ATOM 1784 C C . GLY A 1 224 ? 43.027 -11.484 18.435 1.00 88.72 ? 224 GLY A C 1 ATOM 1785 O O . GLY A 1 224 ? 42.950 -10.653 17.531 1.00 86.96 ? 224 GLY A O 1 ATOM 1786 N N . ARG A 1 225 ? 42.916 -12.798 18.239 1.00 88.72 ? 225 ARG A N 1 ATOM 1787 C CA . ARG A 1 225 ? 42.693 -13.389 16.913 1.00 88.23 ? 225 ARG A CA 1 ATOM 1788 C C . ARG A 1 225 ? 41.604 -14.461 16.946 1.00 88.04 ? 225 ARG A C 1 ATOM 1789 O O . ARG A 1 225 ? 41.378 -15.094 17.973 1.00 89.69 ? 225 ARG A O 1 ATOM 1790 C CB . ARG A 1 225 ? 43.988 -14.013 16.374 1.00 87.02 ? 225 ARG A CB 1 ATOM 1791 C CG . ARG A 1 225 ? 45.126 -13.034 16.132 1.00 87.10 ? 225 ARG A CG 1 ATOM 1792 C CD . ARG A 1 225 ? 44.885 -12.176 14.902 1.00 85.80 ? 225 ARG A CD 1 ATOM 1793 N NE . ARG A 1 225 ? 46.051 -11.345 14.593 1.00 86.88 ? 225 ARG A NE 1 ATOM 1794 C CZ . ARG A 1 225 ? 46.256 -10.103 15.035 1.00 88.08 ? 225 ARG A CZ 1 ATOM 1795 N NH1 . ARG A 1 225 ? 45.375 -9.492 15.828 1.00 89.00 ? 225 ARG A NH1 1 ATOM 1796 N NH2 . ARG A 1 225 ? 47.363 -9.462 14.678 1.00 88.15 ? 225 ARG A NH2 1 ATOM 1797 N N . MET A 1 226 ? 40.937 -14.650 15.812 1.00 86.97 ? 226 MET A N 1 ATOM 1798 C CA . MET A 1 226 ? 39.968 -15.724 15.643 1.00 87.81 ? 226 MET A CA 1 ATOM 1799 C C . MET A 1 226 ? 40.441 -16.634 14.515 1.00 87.65 ? 226 MET A C 1 ATOM 1800 O O . MET A 1 226 ? 40.637 -16.176 13.392 1.00 87.99 ? 226 MET A O 1 ATOM 1801 C CB . MET A 1 226 ? 38.597 -15.156 15.282 1.00 89.13 ? 226 MET A CB 1 ATOM 1802 C CG . MET A 1 226 ? 37.940 -14.331 16.374 1.00 92.67 ? 226 MET A CG 1 ATOM 1803 S SD . MET A 1 226 ? 37.162 -15.333 17.654 1.00 95.78 ? 226 MET A SD 1 ATOM 1804 C CE . MET A 1 226 ? 36.456 -14.036 18.667 1.00 99.65 ? 226 MET A CE 1 ATOM 1805 N N . GLU A 1 227 ? 40.628 -17.916 14.818 1.00 87.14 ? 227 GLU A N 1 ATOM 1806 C CA . GLU A 1 227 ? 40.980 -18.918 13.815 1.00 85.00 ? 227 GLU A CA 1 ATOM 1807 C C . GLU A 1 227 ? 39.743 -19.766 13.539 1.00 84.25 ? 227 GLU A C 1 ATOM 1808 O O . GLU A 1 227 ? 39.170 -20.343 14.463 1.00 84.53 ? 227 GLU A O 1 ATOM 1809 C CB . GLU A 1 227 ? 42.131 -19.785 14.324 1.00 86.06 ? 227 GLU A CB 1 ATOM 1810 C CG . GLU A 1 227 ? 42.780 -20.659 13.263 1.00 87.33 ? 227 GLU A CG 1 ATOM 1811 C CD . GLU A 1 227 ? 44.135 -21.200 13.691 1.00 88.84 ? 227 GLU A CD 1 ATOM 1812 O OE1 . GLU A 1 227 ? 44.475 -21.109 14.890 1.00 88.83 ? 227 GLU A OE1 1 ATOM 1813 O OE2 . GLU A 1 227 ? 44.869 -21.713 12.821 1.00 90.46 ? 227 GLU A OE2 1 ATOM 1814 N N . PHE A 1 228 ? 39.318 -19.825 12.279 1.00 81.54 ? 228 PHE A N 1 ATOM 1815 C CA . PHE A 1 228 ? 38.070 -20.501 11.933 1.00 80.31 ? 228 PHE A CA 1 ATOM 1816 C C . PHE A 1 228 ? 38.322 -21.804 11.190 1.00 78.36 ? 228 PHE A C 1 ATOM 1817 O O . PHE A 1 228 ? 39.235 -21.894 10.370 1.00 77.14 ? 228 PHE A O 1 ATOM 1818 C CB . PHE A 1 228 ? 37.175 -19.578 11.109 1.00 80.90 ? 228 PHE A CB 1 ATOM 1819 C CG . PHE A 1 228 ? 36.603 -18.435 11.900 1.00 82.72 ? 228 PHE A CG 1 ATOM 1820 C CD1 . PHE A 1 228 ? 35.485 -18.620 12.704 1.00 83.38 ? 228 PHE A CD1 1 ATOM 1821 C CD2 . PHE A 1 228 ? 37.190 -17.177 11.856 1.00 83.64 ? 228 PHE A CD2 1 ATOM 1822 C CE1 . PHE A 1 228 ? 34.961 -17.570 13.441 1.00 84.48 ? 228 PHE A CE1 1 ATOM 1823 C CE2 . PHE A 1 228 ? 36.668 -16.123 12.590 1.00 84.71 ? 228 PHE A CE2 1 ATOM 1824 C CZ . PHE A 1 228 ? 35.554 -16.320 13.386 1.00 84.51 ? 228 PHE A CZ 1 ATOM 1825 N N . PHE A 1 229 ? 37.496 -22.805 11.493 1.00 76.59 ? 229 PHE A N 1 ATOM 1826 C CA . PHE A 1 229 ? 37.622 -24.139 10.920 1.00 75.97 ? 229 PHE A CA 1 ATOM 1827 C C . PHE A 1 229 ? 36.290 -24.604 10.361 1.00 77.41 ? 229 PHE A C 1 ATOM 1828 O O . PHE A 1 229 ? 35.234 -24.050 10.687 1.00 77.98 ? 229 PHE A O 1 ATOM 1829 C CB . PHE A 1 229 ? 38.085 -25.136 11.979 1.00 76.97 ? 229 PHE A CB 1 ATOM 1830 C CG . PHE A 1 229 ? 39.445 -24.838 12.536 1.00 77.79 ? 229 PHE A CG 1 ATOM 1831 C CD1 . PHE A 1 229 ? 39.601 -23.919 13.565 1.00 78.15 ? 229 PHE A CD1 1 ATOM 1832 C CD2 . PHE A 1 229 ? 40.571 -25.479 12.035 1.00 77.86 ? 229 PHE A CD2 1 ATOM 1833 C CE1 . PHE A 1 229 ? 40.853 -23.641 14.084 1.00 78.52 ? 229 PHE A CE1 1 ATOM 1834 C CE2 . PHE A 1 229 ? 41.826 -25.203 12.549 1.00 79.06 ? 229 PHE A CE2 1 ATOM 1835 C CZ . PHE A 1 229 ? 41.968 -24.282 13.576 1.00 78.96 ? 229 PHE A CZ 1 ATOM 1836 N N . TRP A 1 230 ? 36.344 -25.634 9.522 1.00 77.59 ? 230 TRP A N 1 ATOM 1837 C CA . TRP A 1 230 ? 35.142 -26.167 8.908 1.00 76.94 ? 230 TRP A CA 1 ATOM 1838 C C . TRP A 1 230 ? 35.245 -27.656 8.661 1.00 77.18 ? 230 TRP A C 1 ATOM 1839 O O . TRP A 1 230 ? 36.331 -28.227 8.697 1.00 76.91 ? 230 TRP A O 1 ATOM 1840 C CB . TRP A 1 230 ? 34.873 -25.451 7.587 1.00 76.20 ? 230 TRP A CB 1 ATOM 1841 C CG . TRP A 1 230 ? 35.983 -25.568 6.585 1.00 75.31 ? 230 TRP A CG 1 ATOM 1842 C CD1 . TRP A 1 230 ? 37.084 -24.769 6.485 1.00 74.98 ? 230 TRP A CD1 1 ATOM 1843 C CD2 . TRP A 1 230 ? 36.090 -26.533 5.535 1.00 75.03 ? 230 TRP A CD2 1 ATOM 1844 N NE1 . TRP A 1 230 ? 37.873 -25.178 5.441 1.00 74.01 ? 230 TRP A NE1 1 ATOM 1845 C CE2 . TRP A 1 230 ? 37.285 -26.259 4.840 1.00 74.98 ? 230 TRP A CE2 1 ATOM 1846 C CE3 . TRP A 1 230 ? 35.291 -27.601 5.112 1.00 75.46 ? 230 TRP A CE3 1 ATOM 1847 C CZ2 . TRP A 1 230 ? 37.701 -27.016 3.743 1.00 76.41 ? 230 TRP A CZ2 1 ATOM 1848 C CZ3 . TRP A 1 230 ? 35.706 -28.354 4.024 1.00 76.67 ? 230 TRP A CZ3 1 ATOM 1849 C CH2 . TRP A 1 230 ? 36.900 -28.060 3.353 1.00 76.08 ? 230 TRP A CH2 1 ATOM 1850 N N . THR A 1 231 ? 34.095 -28.276 8.418 1.00 77.62 ? 231 THR A N 1 ATOM 1851 C CA . THR A 1 231 ? 34.045 -29.641 7.917 1.00 78.17 ? 231 THR A CA 1 ATOM 1852 C C . THR A 1 231 ? 32.722 -29.905 7.195 1.00 79.64 ? 231 THR A C 1 ATOM 1853 O O . THR A 1 231 ? 31.763 -29.144 7.339 1.00 79.70 ? 231 THR A O 1 ATOM 1854 C CB . THR A 1 231 ? 34.248 -30.661 9.054 1.00 79.29 ? 231 THR A CB 1 ATOM 1855 O OG1 . THR A 1 231 ? 34.599 -31.933 8.496 1.00 80.05 ? 231 THR A OG1 1 ATOM 1856 C CG2 . THR A 1 231 ? 32.988 -30.799 9.919 1.00 79.29 ? 231 THR A CG2 1 ATOM 1857 N N . ILE A 1 232 ? 32.690 -30.973 6.405 1.00 81.96 ? 232 ILE A N 1 ATOM 1858 C CA . ILE A 1 232 ? 31.466 -31.428 5.751 1.00 83.74 ? 232 ILE A CA 1 ATOM 1859 C C . ILE A 1 232 ? 30.968 -32.617 6.546 1.00 86.26 ? 232 ILE A C 1 ATOM 1860 O O . ILE A 1 232 ? 31.613 -33.661 6.584 1.00 88.93 ? 232 ILE A O 1 ATOM 1861 C CB . ILE A 1 232 ? 31.694 -31.808 4.261 1.00 83.57 ? 232 ILE A CB 1 ATOM 1862 C CG1 . ILE A 1 232 ? 31.382 -30.619 3.349 1.00 82.57 ? 232 ILE A CG1 1 ATOM 1863 C CG2 . ILE A 1 232 ? 30.798 -32.965 3.823 1.00 84.64 ? 232 ILE A CG2 1 ATOM 1864 C CD1 . ILE A 1 232 ? 32.110 -29.352 3.717 1.00 82.20 ? 232 ILE A CD1 1 ATOM 1865 N N . LEU A 1 233 ? 29.828 -32.440 7.198 1.00 89.22 ? 233 LEU A N 1 ATOM 1866 C CA . LEU A 1 233 ? 29.220 -33.495 7.987 1.00 91.16 ? 233 LEU A CA 1 ATOM 1867 C C . LEU A 1 233 ? 28.276 -34.274 7.084 1.00 92.95 ? 233 LEU A C 1 ATOM 1868 O O . LEU A 1 233 ? 27.285 -33.729 6.597 1.00 93.11 ? 233 LEU A O 1 ATOM 1869 C CB . LEU A 1 233 ? 28.459 -32.885 9.164 1.00 92.50 ? 233 LEU A CB 1 ATOM 1870 C CG . LEU A 1 233 ? 27.918 -33.832 10.238 1.00 94.59 ? 233 LEU A CG 1 ATOM 1871 C CD1 . LEU A 1 233 ? 29.051 -34.551 10.958 1.00 94.62 ? 233 LEU A CD1 1 ATOM 1872 C CD2 . LEU A 1 233 ? 27.059 -33.052 11.224 1.00 95.20 ? 233 LEU A CD2 1 ATOM 1873 N N . LYS A 1 234 ? 28.589 -35.543 6.853 1.00 95.13 ? 234 LYS A N 1 ATOM 1874 C CA . LYS A 1 234 ? 27.786 -36.371 5.959 1.00 99.72 ? 234 LYS A CA 1 ATOM 1875 C C . LYS A 1 234 ? 26.483 -36.799 6.635 1.00 101.99 ? 234 LYS A C 1 ATOM 1876 O O . LYS A 1 234 ? 26.379 -36.742 7.861 1.00 103.62 ? 234 LYS A O 1 ATOM 1877 C CB . LYS A 1 234 ? 28.605 -37.570 5.478 1.00 104.10 ? 234 LYS A CB 1 ATOM 1878 C CG . LYS A 1 234 ? 29.519 -37.204 4.315 1.00 106.11 ? 234 LYS A CG 1 ATOM 1879 C CD . LYS A 1 234 ? 30.370 -38.368 3.840 1.00 110.88 ? 234 LYS A CD 1 ATOM 1880 C CE . LYS A 1 234 ? 31.497 -38.675 4.813 1.00 113.07 ? 234 LYS A CE 1 ATOM 1881 N NZ . LYS A 1 234 ? 32.517 -39.559 4.183 1.00 116.05 ? 234 LYS A NZ 1 ATOM 1882 N N . PRO A 1 235 ? 25.473 -37.208 5.838 1.00 103.27 ? 235 PRO A N 1 ATOM 1883 C CA . PRO A 1 235 ? 24.185 -37.573 6.436 1.00 103.00 ? 235 PRO A CA 1 ATOM 1884 C C . PRO A 1 235 ? 24.310 -38.752 7.395 1.00 104.29 ? 235 PRO A C 1 ATOM 1885 O O . PRO A 1 235 ? 25.167 -39.614 7.198 1.00 103.63 ? 235 PRO A O 1 ATOM 1886 C CB . PRO A 1 235 ? 23.324 -37.944 5.223 1.00 104.33 ? 235 PRO A CB 1 ATOM 1887 C CG . PRO A 1 235 ? 24.298 -38.299 4.154 1.00 103.83 ? 235 PRO A CG 1 ATOM 1888 C CD . PRO A 1 235 ? 25.461 -37.386 4.373 1.00 101.88 ? 235 PRO A CD 1 ATOM 1889 N N . ASN A 1 236 ? 23.472 -38.767 8.432 1.00 105.58 ? 236 ASN A N 1 ATOM 1890 C CA . ASN A 1 236 ? 23.516 -39.788 9.484 1.00 107.03 ? 236 ASN A CA 1 ATOM 1891 C C . ASN A 1 236 ? 24.787 -39.786 10.335 1.00 106.73 ? 236 ASN A C 1 ATOM 1892 O O . ASN A 1 236 ? 24.982 -40.687 11.151 1.00 108.61 ? 236 ASN A O 1 ATOM 1893 C CB . ASN A 1 236 ? 23.285 -41.195 8.905 1.00 109.52 ? 236 ASN A CB 1 ATOM 1894 C CG . ASN A 1 236 ? 21.850 -41.650 9.036 1.00 113.73 ? 236 ASN A CG 1 ATOM 1895 O OD1 . ASN A 1 236 ? 21.211 -41.454 10.072 1.00 115.08 ? 236 ASN A OD1 1 ATOM 1896 N ND2 . ASN A 1 236 ? 21.336 -42.278 7.986 1.00 116.08 ? 236 ASN A ND2 1 ATOM 1897 N N . ASP A 1 237 ? 25.641 -38.781 10.161 1.00 104.10 ? 237 ASP A N 1 ATOM 1898 C CA . ASP A 1 237 ? 26.831 -38.648 10.990 1.00 103.18 ? 237 ASP A CA 1 ATOM 1899 C C . ASP A 1 237 ? 26.608 -37.543 12.013 1.00 101.27 ? 237 ASP A C 1 ATOM 1900 O O . ASP A 1 237 ? 25.810 -36.629 11.793 1.00 100.00 ? 237 ASP A O 1 ATOM 1901 C CB . ASP A 1 237 ? 28.063 -38.343 10.138 1.00 101.86 ? 237 ASP A CB 1 ATOM 1902 C CG . ASP A 1 237 ? 29.363 -38.491 10.913 1.00 101.98 ? 237 ASP A CG 1 ATOM 1903 O OD1 . ASP A 1 237 ? 29.388 -39.234 11.920 1.00 103.21 ? 237 ASP A OD1 1 ATOM 1904 O OD2 . ASP A 1 237 ? 30.366 -37.862 10.514 1.00 101.71 ? 237 ASP A OD2 1 ATOM 1905 N N . ALA A 1 238 ? 27.314 -37.642 13.133 1.00 101.15 ? 238 ALA A N 1 ATOM 1906 C CA . ALA A 1 238 ? 27.173 -36.690 14.225 1.00 100.77 ? 238 ALA A CA 1 ATOM 1907 C C . ALA A 1 238 ? 28.484 -35.958 14.462 1.00 98.29 ? 238 ALA A C 1 ATOM 1908 O O . ALA A 1 238 ? 29.554 -36.561 14.376 1.00 99.41 ? 238 ALA A O 1 ATOM 1909 C CB . ALA A 1 238 ? 26.740 -37.415 15.487 1.00 101.63 ? 238 ALA A CB 1 ATOM 1910 N N . ILE A 1 239 ? 28.394 -34.660 14.747 1.00 96.35 ? 239 ILE A N 1 ATOM 1911 C CA . ILE A 1 239 ? 29.558 -33.875 15.169 1.00 94.80 ? 239 ILE A CA 1 ATOM 1912 C C . ILE A 1 239 ? 29.513 -33.626 16.685 1.00 96.82 ? 239 ILE A C 1 ATOM 1913 O O . ILE A 1 239 ? 28.460 -33.304 17.241 1.00 96.10 ? 239 ILE A O 1 ATOM 1914 C CB . ILE A 1 239 ? 29.684 -32.545 14.389 1.00 92.30 ? 239 ILE A CB 1 ATOM 1915 C CG1 . ILE A 1 239 ? 31.048 -31.901 14.660 1.00 92.23 ? 239 ILE A CG1 1 ATOM 1916 C CG2 . ILE A 1 239 ? 28.562 -31.574 14.740 1.00 92.11 ? 239 ILE A CG2 1 ATOM 1917 C CD1 . ILE A 1 239 ? 31.423 -30.817 13.672 1.00 90.27 ? 239 ILE A CD1 1 ATOM 1918 N N . ASN A 1 240 ? 30.662 -33.783 17.340 1.00 97.39 ? 240 ASN A N 1 ATOM 1919 C CA . ASN A 1 240 ? 30.758 -33.701 18.795 1.00 99.02 ? 240 ASN A CA 1 ATOM 1920 C C . ASN A 1 240 ? 31.747 -32.636 19.237 1.00 97.79 ? 240 ASN A C 1 ATOM 1921 O O . ASN A 1 240 ? 32.906 -32.654 18.827 1.00 96.94 ? 240 ASN A O 1 ATOM 1922 C CB . ASN A 1 240 ? 31.192 -35.048 19.358 1.00 101.34 ? 240 ASN A CB 1 ATOM 1923 C CG . ASN A 1 240 ? 30.138 -36.118 19.170 1.00 104.54 ? 240 ASN A CG 1 ATOM 1924 O OD1 . ASN A 1 240 ? 29.019 -35.989 19.666 1.00 104.36 ? 240 ASN A OD1 1 ATOM 1925 N ND2 . ASN A 1 240 ? 30.488 -37.183 18.451 1.00 106.81 ? 240 ASN A ND2 1 ATOM 1926 N N . PHE A 1 241 ? 31.285 -31.717 20.080 1.00 97.33 ? 241 PHE A N 1 ATOM 1927 C CA . PHE A 1 241 ? 32.130 -30.659 20.614 1.00 96.66 ? 241 PHE A CA 1 ATOM 1928 C C . PHE A 1 241 ? 32.358 -30.857 22.109 1.00 98.14 ? 241 PHE A C 1 ATOM 1929 O O . PHE A 1 241 ? 31.483 -31.352 22.817 1.00 99.70 ? 241 PHE A O 1 ATOM 1930 C CB . PHE A 1 241 ? 31.489 -29.296 20.367 1.00 95.90 ? 241 PHE A CB 1 ATOM 1931 C CG . PHE A 1 241 ? 31.386 -28.932 18.914 1.00 95.04 ? 241 PHE A CG 1 ATOM 1932 C CD1 . PHE A 1 241 ? 32.445 -28.314 18.262 1.00 93.57 ? 241 PHE A CD1 1 ATOM 1933 C CD2 . PHE A 1 241 ? 30.232 -29.207 18.197 1.00 95.14 ? 241 PHE A CD2 1 ATOM 1934 C CE1 . PHE A 1 241 ? 32.354 -27.974 16.924 1.00 92.94 ? 241 PHE A CE1 1 ATOM 1935 C CE2 . PHE A 1 241 ? 30.134 -28.869 16.859 1.00 93.53 ? 241 PHE A CE2 1 ATOM 1936 C CZ . PHE A 1 241 ? 31.197 -28.252 16.220 1.00 92.76 ? 241 PHE A CZ 1 ATOM 1937 N N . GLU A 1 242 ? 33.549 -30.487 22.569 1.00 98.19 ? 242 GLU A N 1 ATOM 1938 C CA . GLU A 1 242 ? 33.849 -30.383 23.997 1.00 101.06 ? 242 GLU A CA 1 ATOM 1939 C C . GLU A 1 242 ? 34.850 -29.242 24.193 1.00 100.18 ? 242 GLU A C 1 ATOM 1940 O O . GLU A 1 242 ? 35.812 -29.135 23.425 1.00 98.69 ? 242 GLU A O 1 ATOM 1941 C CB . GLU A 1 242 ? 34.403 -31.703 24.555 1.00 102.97 ? 242 GLU A CB 1 ATOM 1942 C CG . GLU A 1 242 ? 34.505 -31.738 26.078 1.00 106.63 ? 242 GLU A CG 1 ATOM 1943 C CD . GLU A 1 242 ? 35.176 -32.994 26.615 1.00 108.12 ? 242 GLU A CD 1 ATOM 1944 O OE1 . GLU A 1 242 ? 34.624 -34.101 26.430 1.00 108.79 ? 242 GLU A OE1 1 ATOM 1945 O OE2 . GLU A 1 242 ? 36.249 -32.872 27.246 1.00 108.10 ? 242 GLU A OE2 1 ATOM 1946 N N . SER A 1 243 ? 34.627 -28.389 25.198 1.00 101.66 ? 243 SER A N 1 ATOM 1947 C CA . SER A 1 243 ? 35.505 -27.228 25.416 1.00 101.19 ? 243 SER A CA 1 ATOM 1948 C C . SER A 1 243 ? 35.467 -26.606 26.818 1.00 104.39 ? 243 SER A C 1 ATOM 1949 O O . SER A 1 243 ? 34.430 -26.594 27.476 1.00 105.84 ? 243 SER A O 1 ATOM 1950 C CB . SER A 1 243 ? 35.187 -26.139 24.391 1.00 98.19 ? 243 SER A CB 1 ATOM 1951 O OG . SER A 1 243 ? 36.003 -24.999 24.596 1.00 96.97 ? 243 SER A OG 1 ATOM 1952 N N . ASN A 1 244 ? 36.619 -26.070 27.230 1.00 106.95 ? 244 ASN A N 1 ATOM 1953 C CA . ASN A 1 244 ? 36.789 -25.319 28.486 1.00 109.65 ? 244 ASN A CA 1 ATOM 1954 C C . ASN A 1 244 ? 36.617 -23.811 28.336 1.00 107.94 ? 244 ASN A C 1 ATOM 1955 O O . ASN A 1 244 ? 36.485 -23.096 29.331 1.00 108.02 ? 244 ASN A O 1 ATOM 1956 C CB . ASN A 1 244 ? 38.197 -25.546 29.039 1.00 112.58 ? 244 ASN A CB 1 ATOM 1957 C CG . ASN A 1 244 ? 38.271 -26.700 30.005 1.00 116.60 ? 244 ASN A CG 1 ATOM 1958 O OD1 . ASN A 1 244 ? 37.276 -27.375 30.271 1.00 119.58 ? 244 ASN A OD1 1 ATOM 1959 N ND2 . ASN A 1 244 ? 39.462 -26.932 30.548 1.00 118.42 ? 244 ASN A ND2 1 ATOM 1960 N N . GLY A 1 245 ? 36.659 -23.335 27.096 1.00 104.47 ? 245 GLY A N 1 ATOM 1961 C CA . GLY A 1 245 ? 36.625 -21.911 26.802 1.00 103.78 ? 245 GLY A CA 1 ATOM 1962 C C . GLY A 1 245 ? 37.219 -21.622 25.437 1.00 101.74 ? 245 GLY A C 1 ATOM 1963 O O . GLY A 1 245 ? 37.769 -22.516 24.784 1.00 100.36 ? 245 GLY A O 1 ATOM 1964 N N . ASN A 1 246 ? 37.104 -20.364 25.016 1.00 101.08 ? 246 ASN A N 1 ATOM 1965 C CA . ASN A 1 246 ? 37.616 -19.889 23.723 1.00 98.58 ? 246 ASN A CA 1 ATOM 1966 C C . ASN A 1 246 ? 36.860 -20.466 22.521 1.00 95.72 ? 246 ASN A C 1 ATOM 1967 O O . ASN A 1 246 ? 37.293 -20.318 21.386 1.00 94.68 ? 246 ASN A O 1 ATOM 1968 C CB . ASN A 1 246 ? 39.128 -20.148 23.594 1.00 98.53 ? 246 ASN A CB 1 ATOM 1969 C CG . ASN A 1 246 ? 39.936 -19.482 24.700 1.00 100.61 ? 246 ASN A CG 1 ATOM 1970 O OD1 . ASN A 1 246 ? 40.323 -18.320 24.585 1.00 102.43 ? 246 ASN A OD1 1 ATOM 1971 N ND2 . ASN A 1 246 ? 40.213 -20.223 25.764 1.00 100.81 ? 246 ASN A ND2 1 ATOM 1972 N N . PHE A 1 247 ? 35.708 -21.081 22.778 1.00 96.50 ? 247 PHE A N 1 ATOM 1973 C CA . PHE A 1 247 ? 34.930 -21.756 21.746 1.00 93.22 ? 247 PHE A CA 1 ATOM 1974 C C . PHE A 1 247 ? 34.015 -20.767 21.042 1.00 91.87 ? 247 PHE A C 1 ATOM 1975 O O . PHE A 1 247 ? 33.291 -20.009 21.682 1.00 94.36 ? 247 PHE A O 1 ATOM 1976 C CB . PHE A 1 247 ? 34.115 -22.890 22.385 1.00 95.16 ? 247 PHE A CB 1 ATOM 1977 C CG . PHE A 1 247 ? 33.321 -23.725 21.408 1.00 94.19 ? 247 PHE A CG 1 ATOM 1978 C CD1 . PHE A 1 247 ? 33.870 -24.156 20.210 1.00 91.81 ? 247 PHE A CD1 1 ATOM 1979 C CD2 . PHE A 1 247 ? 32.029 -24.126 21.723 1.00 95.87 ? 247 PHE A CD2 1 ATOM 1980 C CE1 . PHE A 1 247 ? 33.138 -24.937 19.334 1.00 91.90 ? 247 PHE A CE1 1 ATOM 1981 C CE2 . PHE A 1 247 ? 31.293 -24.911 20.853 1.00 94.43 ? 247 PHE A CE2 1 ATOM 1982 C CZ . PHE A 1 247 ? 31.847 -25.317 19.657 1.00 93.59 ? 247 PHE A CZ 1 ATOM 1983 N N . ILE A 1 248 ? 34.078 -20.764 19.717 1.00 90.10 ? 248 ILE A N 1 ATOM 1984 C CA . ILE A 1 248 ? 33.169 -19.982 18.901 1.00 88.77 ? 248 ILE A CA 1 ATOM 1985 C C . ILE A 1 248 ? 32.222 -21.005 18.294 1.00 88.74 ? 248 ILE A C 1 ATOM 1986 O O . ILE A 1 248 ? 32.548 -21.668 17.308 1.00 87.21 ? 248 ILE A O 1 ATOM 1987 C CB . ILE A 1 248 ? 33.922 -19.188 17.817 1.00 87.00 ? 248 ILE A CB 1 ATOM 1988 C CG1 . ILE A 1 248 ? 35.162 -18.503 18.403 1.00 87.28 ? 248 ILE A CG1 1 ATOM 1989 C CG2 . ILE A 1 248 ? 33.007 -18.153 17.185 1.00 86.94 ? 248 ILE A CG2 1 ATOM 1990 C CD1 . ILE A 1 248 ? 34.868 -17.531 19.526 1.00 89.62 ? 248 ILE A CD1 1 ATOM 1991 N N . ALA A 1 249 ? 31.063 -21.162 18.919 1.00 90.64 ? 249 ALA A N 1 ATOM 1992 C CA . ALA A 1 249 ? 30.170 -22.271 18.598 1.00 92.21 ? 249 ALA A CA 1 ATOM 1993 C C . ALA A 1 249 ? 29.337 -21.993 17.352 1.00 91.88 ? 249 ALA A C 1 ATOM 1994 O O . ALA A 1 249 ? 28.982 -20.849 17.087 1.00 92.05 ? 249 ALA A O 1 ATOM 1995 C CB . ALA A 1 249 ? 29.258 -22.564 19.778 1.00 94.64 ? 249 ALA A CB 1 ATOM 1996 N N . PRO A 1 250 ? 29.028 -23.041 16.573 1.00 92.71 ? 250 PRO A N 1 ATOM 1997 C CA . PRO A 1 250 ? 28.111 -22.838 15.455 1.00 93.21 ? 250 PRO A CA 1 ATOM 1998 C C . PRO A 1 250 ? 26.695 -22.526 15.930 1.00 95.64 ? 250 PRO A C 1 ATOM 1999 O O . PRO A 1 250 ? 26.255 -23.075 16.938 1.00 98.21 ? 250 PRO A O 1 ATOM 2000 C CB . PRO A 1 250 ? 28.132 -24.183 14.717 1.00 92.12 ? 250 PRO A CB 1 ATOM 2001 C CG . PRO A 1 250 ? 28.731 -25.165 15.659 1.00 92.19 ? 250 PRO A CG 1 ATOM 2002 C CD . PRO A 1 250 ? 29.619 -24.391 16.577 1.00 92.66 ? 250 PRO A CD 1 ATOM 2003 N N . GLU A 1 251 ? 26.006 -21.632 15.225 1.00 96.03 ? 251 GLU A N 1 ATOM 2004 C CA . GLU A 1 251 ? 24.562 -21.488 15.377 1.00 98.69 ? 251 GLU A CA 1 ATOM 2005 C C . GLU A 1 251 ? 23.871 -21.971 14.106 1.00 98.55 ? 251 GLU A C 1 ATOM 2006 O O . GLU A 1 251 ? 23.007 -22.850 14.161 1.00 98.36 ? 251 GLU A O 1 ATOM 2007 C CB . GLU A 1 251 ? 24.165 -20.042 15.671 1.00 101.07 ? 251 GLU A CB 1 ATOM 2008 C CG . GLU A 1 251 ? 22.803 -19.933 16.348 1.00 104.23 ? 251 GLU A CG 1 ATOM 2009 C CD . GLU A 1 251 ? 22.212 -18.539 16.296 1.00 106.11 ? 251 GLU A CD 1 ATOM 2010 O OE1 . GLU A 1 251 ? 22.934 -17.585 15.930 1.00 107.47 ? 251 GLU A OE1 1 ATOM 2011 O OE2 . GLU A 1 251 ? 21.016 -18.401 16.623 1.00 108.20 ? 251 GLU A OE2 1 ATOM 2012 N N . TYR A 1 252 ? 24.267 -21.391 12.971 1.00 96.71 ? 252 TYR A N 1 ATOM 2013 C CA . TYR A 1 252 ? 23.736 -21.762 11.661 1.00 96.14 ? 252 TYR A CA 1 ATOM 2014 C C . TYR A 1 252 ? 24.782 -22.494 10.823 1.00 94.78 ? 252 TYR A C 1 ATOM 2015 O O . TYR A 1 252 ? 25.963 -22.134 10.820 1.00 91.36 ? 252 TYR A O 1 ATOM 2016 C CB . TYR A 1 252 ? 23.279 -20.518 10.895 1.00 96.78 ? 252 TYR A CB 1 ATOM 2017 C CG . TYR A 1 252 ? 22.167 -19.739 11.560 1.00 100.48 ? 252 TYR A CG 1 ATOM 2018 C CD1 . TYR A 1 252 ? 20.831 -20.062 11.332 1.00 102.60 ? 252 TYR A CD1 1 ATOM 2019 C CD2 . TYR A 1 252 ? 22.447 -18.673 12.411 1.00 100.58 ? 252 TYR A CD2 1 ATOM 2020 C CE1 . TYR A 1 252 ? 19.809 -19.349 11.936 1.00 104.24 ? 252 TYR A CE1 1 ATOM 2021 C CE2 . TYR A 1 252 ? 21.432 -17.953 13.017 1.00 102.48 ? 252 TYR A CE2 1 ATOM 2022 C CZ . TYR A 1 252 ? 20.113 -18.295 12.777 1.00 104.83 ? 252 TYR A CZ 1 ATOM 2023 O OH . TYR A 1 252 ? 19.098 -17.585 13.381 1.00 107.32 ? 252 TYR A OH 1 ATOM 2024 N N . ALA A 1 253 ? 24.331 -23.521 10.107 1.00 94.71 ? 253 ALA A N 1 ATOM 2025 C CA . ALA A 1 253 ? 25.157 -24.226 9.133 1.00 91.56 ? 253 ALA A CA 1 ATOM 2026 C C . ALA A 1 253 ? 24.398 -24.306 7.808 1.00 91.57 ? 253 ALA A C 1 ATOM 2027 O O . ALA A 1 253 ? 23.181 -24.119 7.775 1.00 93.68 ? 253 ALA A O 1 ATOM 2028 C CB . ALA A 1 253 ? 25.501 -25.615 9.647 1.00 91.82 ? 253 ALA A CB 1 ATOM 2029 N N . TYR A 1 254 ? 25.121 -24.584 6.725 1.00 90.52 ? 254 TYR A N 1 ATOM 2030 C CA . TYR A 1 254 ? 24.555 -24.572 5.375 1.00 89.78 ? 254 TYR A CA 1 ATOM 2031 C C . TYR A 1 254 ? 24.350 -25.981 4.818 1.00 89.16 ? 254 TYR A C 1 ATOM 2032 O O . TYR A 1 254 ? 25.290 -26.769 4.755 1.00 86.64 ? 254 TYR A O 1 ATOM 2033 C CB . TYR A 1 254 ? 25.486 -23.818 4.427 1.00 88.57 ? 254 TYR A CB 1 ATOM 2034 C CG . TYR A 1 254 ? 25.682 -22.348 4.735 1.00 88.02 ? 254 TYR A CG 1 ATOM 2035 C CD1 . TYR A 1 254 ? 24.818 -21.384 4.216 1.00 89.12 ? 254 TYR A CD1 1 ATOM 2036 C CD2 . TYR A 1 254 ? 26.750 -21.918 5.514 1.00 87.49 ? 254 TYR A CD2 1 ATOM 2037 C CE1 . TYR A 1 254 ? 25.002 -20.037 4.479 1.00 89.19 ? 254 TYR A CE1 1 ATOM 2038 C CE2 . TYR A 1 254 ? 26.944 -20.572 5.783 1.00 88.01 ? 254 TYR A CE2 1 ATOM 2039 C CZ . TYR A 1 254 ? 26.067 -19.634 5.262 1.00 89.07 ? 254 TYR A CZ 1 ATOM 2040 O OH . TYR A 1 254 ? 26.254 -18.296 5.526 1.00 90.45 ? 254 TYR A OH 1 ATOM 2041 N N . LYS A 1 255 ? 23.124 -26.291 4.407 1.00 90.85 ? 255 LYS A N 1 ATOM 2042 C CA . LYS A 1 255 ? 22.855 -27.530 3.676 1.00 92.72 ? 255 LYS A CA 1 ATOM 2043 C C . LYS A 1 255 ? 23.310 -27.363 2.236 1.00 91.25 ? 255 LYS A C 1 ATOM 2044 O O . LYS A 1 255 ? 23.141 -26.295 1.650 1.00 89.99 ? 255 LYS A O 1 ATOM 2045 C CB . LYS A 1 255 ? 21.364 -27.872 3.677 1.00 95.94 ? 255 LYS A CB 1 ATOM 2046 C CG . LYS A 1 255 ? 20.765 -28.185 5.037 1.00 97.78 ? 255 LYS A CG 1 ATOM 2047 C CD . LYS A 1 255 ? 19.384 -28.823 4.916 1.00 100.96 ? 255 LYS A CD 1 ATOM 2048 C CE . LYS A 1 255 ? 18.357 -27.879 4.305 1.00 102.53 ? 255 LYS A CE 1 ATOM 2049 N NZ . LYS A 1 255 ? 17.008 -28.501 4.211 1.00 105.75 ? 255 LYS A NZ 1 ATOM 2050 N N . ILE A 1 256 ? 23.879 -28.424 1.675 1.00 91.74 ? 256 ILE A N 1 ATOM 2051 C CA . ILE A 1 256 ? 24.277 -28.450 0.273 1.00 92.10 ? 256 ILE A CA 1 ATOM 2052 C C . ILE A 1 256 ? 23.190 -29.157 -0.532 1.00 93.04 ? 256 ILE A C 1 ATOM 2053 O O . ILE A 1 256 ? 23.180 -30.387 -0.640 1.00 92.53 ? 256 ILE A O 1 ATOM 2054 C CB . ILE A 1 256 ? 25.619 -29.182 0.092 1.00 92.60 ? 256 ILE A CB 1 ATOM 2055 C CG1 . ILE A 1 256 ? 26.709 -28.487 0.915 1.00 92.63 ? 256 ILE A CG1 1 ATOM 2056 C CG2 . ILE A 1 256 ? 26.004 -29.224 -1.383 1.00 92.82 ? 256 ILE A CG2 1 ATOM 2057 C CD1 . ILE A 1 256 ? 28.002 -29.267 1.025 1.00 92.61 ? 256 ILE A CD1 1 ATOM 2058 N N . VAL A 1 257 ? 22.276 -28.373 -1.096 1.00 94.19 ? 257 VAL A N 1 ATOM 2059 C CA . VAL A 1 257 ? 21.104 -28.935 -1.783 1.00 98.38 ? 257 VAL A CA 1 ATOM 2060 C C . VAL A 1 257 ? 21.353 -29.210 -3.268 1.00 99.30 ? 257 VAL A C 1 ATOM 2061 O O . VAL A 1 257 ? 20.887 -30.225 -3.803 1.00 99.30 ? 257 VAL A O 1 ATOM 2062 C CB . VAL A 1 257 ? 19.836 -28.058 -1.610 1.00 100.42 ? 257 VAL A CB 1 ATOM 2063 C CG1 . VAL A 1 257 ? 19.365 -28.092 -0.164 1.00 100.85 ? 257 VAL A CG1 1 ATOM 2064 C CG2 . VAL A 1 257 ? 20.064 -26.619 -2.061 1.00 99.88 ? 257 VAL A CG2 1 ATOM 2065 N N . LYS A 1 258 ? 22.089 -28.315 -3.923 1.00 98.78 ? 258 LYS A N 1 ATOM 2066 C CA . LYS A 1 258 ? 22.351 -28.437 -5.351 1.00 100.49 ? 258 LYS A CA 1 ATOM 2067 C C . LYS A 1 258 ? 23.852 -28.438 -5.632 1.00 98.15 ? 258 LYS A C 1 ATOM 2068 O O . LYS A 1 258 ? 24.546 -27.469 -5.324 1.00 94.15 ? 258 LYS A O 1 ATOM 2069 C CB . LYS A 1 258 ? 21.669 -27.296 -6.109 1.00 102.53 ? 258 LYS A CB 1 ATOM 2070 C CG . LYS A 1 258 ? 21.233 -27.667 -7.517 1.00 106.57 ? 258 LYS A CG 1 ATOM 2071 C CD . LYS A 1 258 ? 20.997 -26.432 -8.376 1.00 108.63 ? 258 LYS A CD 1 ATOM 2072 C CE . LYS A 1 258 ? 20.012 -26.706 -9.503 1.00 111.71 ? 258 LYS A CE 1 ATOM 2073 N NZ . LYS A 1 258 ? 20.406 -27.877 -10.330 1.00 113.72 ? 258 LYS A NZ 1 ATOM 2074 N N . LYS A 1 259 ? 24.341 -29.539 -6.202 1.00 100.04 ? 259 LYS A N 1 ATOM 2075 C CA . LYS A 1 259 ? 25.725 -29.644 -6.665 1.00 100.33 ? 259 LYS A CA 1 ATOM 2076 C C . LYS A 1 259 ? 25.754 -29.610 -8.185 1.00 100.64 ? 259 LYS A C 1 ATOM 2077 O O . LYS A 1 259 ? 24.994 -30.320 -8.840 1.00 103.95 ? 259 LYS A O 1 ATOM 2078 C CB . LYS A 1 259 ? 26.368 -30.943 -6.170 1.00 102.51 ? 259 LYS A CB 1 ATOM 2079 C CG . LYS A 1 259 ? 26.692 -30.945 -4.684 1.00 104.09 ? 259 LYS A CG 1 ATOM 2080 C CD . LYS A 1 259 ? 27.270 -32.276 -4.222 1.00 105.08 ? 259 LYS A CD 1 ATOM 2081 C CE . LYS A 1 259 ? 27.196 -32.406 -2.707 1.00 105.55 ? 259 LYS A CE 1 ATOM 2082 N NZ . LYS A 1 259 ? 27.591 -33.755 -2.217 1.00 106.25 ? 259 LYS A NZ 1 ATOM 2083 N N . GLY A 1 260 ? 26.633 -28.788 -8.749 1.00 99.59 ? 260 GLY A N 1 ATOM 2084 C CA . GLY A 1 260 ? 26.750 -28.686 -10.200 1.00 99.78 ? 260 GLY A CA 1 ATOM 2085 C C . GLY A 1 260 ? 27.894 -27.801 -10.642 1.00 97.83 ? 260 GLY A C 1 ATOM 2086 O O . GLY A 1 260 ? 28.806 -27.518 -9.868 1.00 97.58 ? 260 GLY A O 1 ATOM 2087 N N . ASP A 1 261 ? 27.835 -27.362 -11.895 1.00 98.96 ? 261 ASP A N 1 ATOM 2088 C CA . ASP A 1 261 ? 28.906 -26.568 -12.489 1.00 98.20 ? 261 ASP A CA 1 ATOM 2089 C C . ASP A 1 261 ? 28.821 -25.128 -12.023 1.00 94.12 ? 261 ASP A C 1 ATOM 2090 O O . ASP A 1 261 ? 27.774 -24.493 -12.128 1.00 94.62 ? 261 ASP A O 1 ATOM 2091 C CB . ASP A 1 261 ? 28.842 -26.619 -14.022 1.00 101.76 ? 261 ASP A CB 1 ATOM 2092 C CG . ASP A 1 261 ? 29.391 -27.918 -14.591 1.00 105.89 ? 261 ASP A CG 1 ATOM 2093 O OD1 . ASP A 1 261 ? 30.123 -28.629 -13.867 1.00 106.74 ? 261 ASP A OD1 1 ATOM 2094 O OD2 . ASP A 1 261 ? 29.098 -28.222 -15.771 1.00 109.96 ? 261 ASP A OD2 1 ATOM 2095 N N . SER A 1 262 ? 29.934 -24.622 -11.511 1.00 89.90 ? 262 SER A N 1 ATOM 2096 C CA . SER A 1 262 ? 30.006 -23.255 -11.020 1.00 89.81 ? 262 SER A CA 1 ATOM 2097 C C . SER A 1 262 ? 31.466 -22.815 -11.032 1.00 88.42 ? 262 SER A C 1 ATOM 2098 O O . SER A 1 262 ? 32.350 -23.582 -11.429 1.00 91.58 ? 262 SER A O 1 ATOM 2099 C CB . SER A 1 262 ? 29.413 -23.165 -9.604 1.00 89.82 ? 262 SER A CB 1 ATOM 2100 O OG . SER A 1 262 ? 29.312 -21.823 -9.151 1.00 89.55 ? 262 SER A OG 1 ATOM 2101 N N . THR A 1 263 ? 31.714 -21.575 -10.621 1.00 85.42 ? 263 THR A N 1 ATOM 2102 C CA . THR A 1 263 ? 33.067 -21.049 -10.539 1.00 80.65 ? 263 THR A CA 1 ATOM 2103 C C . THR A 1 263 ? 33.061 -19.755 -9.754 1.00 77.13 ? 263 THR A C 1 ATOM 2104 O O . THR A 1 263 ? 32.048 -19.058 -9.708 1.00 76.63 ? 263 THR A O 1 ATOM 2105 C CB . THR A 1 263 ? 33.678 -20.796 -11.941 1.00 79.11 ? 263 THR A CB 1 ATOM 2106 O OG1 . THR A 1 263 ? 35.060 -20.452 -11.811 1.00 77.27 ? 263 THR A OG1 1 ATOM 2107 C CG2 . THR A 1 263 ? 32.960 -19.671 -12.671 1.00 78.42 ? 263 THR A CG2 1 ATOM 2108 N N . ILE A 1 264 ? 34.193 -19.449 -9.130 1.00 75.78 ? 264 ILE A N 1 ATOM 2109 C CA . ILE A 1 264 ? 34.392 -18.164 -8.472 1.00 73.95 ? 264 ILE A CA 1 ATOM 2110 C C . ILE A 1 264 ? 35.218 -17.297 -9.408 1.00 73.02 ? 264 ILE A C 1 ATOM 2111 O O . ILE A 1 264 ? 36.357 -17.619 -9.737 1.00 74.30 ? 264 ILE A O 1 ATOM 2112 C CB . ILE A 1 264 ? 35.089 -18.312 -7.110 1.00 73.41 ? 264 ILE A CB 1 ATOM 2113 C CG1 . ILE A 1 264 ? 34.343 -19.343 -6.255 1.00 75.59 ? 264 ILE A CG1 1 ATOM 2114 C CG2 . ILE A 1 264 ? 35.139 -16.970 -6.392 1.00 72.17 ? 264 ILE A CG2 1 ATOM 2115 C CD1 . ILE A 1 264 ? 34.963 -19.594 -4.901 1.00 76.65 ? 264 ILE A CD1 1 ATOM 2116 N N . MET A 1 265 ? 34.622 -16.193 -9.831 1.00 73.01 ? 265 MET A N 1 ATOM 2117 C CA . MET A 1 265 ? 35.176 -15.338 -10.863 1.00 72.44 ? 265 MET A CA 1 ATOM 2118 C C . MET A 1 265 ? 35.680 -14.058 -10.209 1.00 73.11 ? 265 MET A C 1 ATOM 2119 O O . MET A 1 265 ? 34.951 -13.419 -9.462 1.00 76.05 ? 265 MET A O 1 ATOM 2120 C CB . MET A 1 265 ? 34.059 -15.032 -11.851 1.00 72.63 ? 265 MET A CB 1 ATOM 2121 C CG . MET A 1 265 ? 34.473 -14.437 -13.169 1.00 72.07 ? 265 MET A CG 1 ATOM 2122 S SD . MET A 1 265 ? 33.026 -14.336 -14.236 1.00 73.96 ? 265 MET A SD 1 ATOM 2123 C CE . MET A 1 265 ? 32.949 -16.014 -14.856 1.00 73.97 ? 265 MET A CE 1 ATOM 2124 N N . LYS A 1 266 ? 36.930 -13.698 -10.467 1.00 74.68 ? 266 LYS A N 1 ATOM 2125 C CA . LYS A 1 266 ? 37.515 -12.504 -9.869 1.00 76.95 ? 266 LYS A CA 1 ATOM 2126 C C . LYS A 1 266 ? 37.274 -11.324 -10.800 1.00 77.08 ? 266 LYS A C 1 ATOM 2127 O O . LYS A 1 266 ? 37.700 -11.345 -11.957 1.00 77.44 ? 266 LYS A O 1 ATOM 2128 C CB . LYS A 1 266 ? 39.017 -12.686 -9.612 1.00 80.38 ? 266 LYS A CB 1 ATOM 2129 C CG . LYS A 1 266 ? 39.417 -14.025 -8.994 1.00 83.94 ? 266 LYS A CG 1 ATOM 2130 C CD . LYS A 1 266 ? 38.705 -14.337 -7.681 1.00 87.58 ? 266 LYS A CD 1 ATOM 2131 C CE . LYS A 1 266 ? 39.131 -13.410 -6.556 1.00 90.77 ? 266 LYS A CE 1 ATOM 2132 N NZ . LYS A 1 266 ? 40.597 -13.487 -6.298 1.00 94.83 ? 266 LYS A NZ 1 ATOM 2133 N N . SER A 1 267 ? 36.585 -10.303 -10.294 1.00 78.64 ? 267 SER A N 1 ATOM 2134 C CA . SER A 1 267 ? 36.188 -9.152 -11.106 1.00 79.22 ? 267 SER A CA 1 ATOM 2135 C C . SER A 1 267 ? 35.735 -7.980 -10.241 1.00 81.72 ? 267 SER A C 1 ATOM 2136 O O . SER A 1 267 ? 35.151 -8.168 -9.173 1.00 84.77 ? 267 SER A O 1 ATOM 2137 C CB . SER A 1 267 ? 35.055 -9.548 -12.057 1.00 79.07 ? 267 SER A CB 1 ATOM 2138 O OG . SER A 1 267 ? 34.603 -8.433 -12.807 1.00 80.76 ? 267 SER A OG 1 ATOM 2139 N N . GLU A 1 268 ? 36.002 -6.770 -10.720 1.00 83.08 ? 268 GLU A N 1 ATOM 2140 C CA . GLU A 1 268 ? 35.592 -5.552 -10.033 1.00 83.81 ? 268 GLU A CA 1 ATOM 2141 C C . GLU A 1 268 ? 34.261 -5.026 -10.569 1.00 84.98 ? 268 GLU A C 1 ATOM 2142 O O . GLU A 1 268 ? 33.716 -4.058 -10.037 1.00 89.97 ? 268 GLU A O 1 ATOM 2143 C CB . GLU A 1 268 ? 36.670 -4.474 -10.184 1.00 85.07 ? 268 GLU A CB 1 ATOM 2144 C CG . GLU A 1 268 ? 38.081 -4.932 -9.837 1.00 84.40 ? 268 GLU A CG 1 ATOM 2145 C CD . GLU A 1 268 ? 38.200 -5.509 -8.431 1.00 85.83 ? 268 GLU A CD 1 ATOM 2146 O OE1 . GLU A 1 268 ? 37.733 -4.858 -7.461 1.00 81.21 ? 268 GLU A OE1 1 ATOM 2147 O OE2 . GLU A 1 268 ? 38.773 -6.619 -8.303 1.00 85.19 ? 268 GLU A OE2 1 ATOM 2148 N N . LEU A 1 269 ? 33.738 -5.666 -11.611 1.00 84.48 ? 269 LEU A N 1 ATOM 2149 C CA . LEU A 1 269 ? 32.489 -5.238 -12.241 1.00 86.51 ? 269 LEU A CA 1 ATOM 2150 C C . LEU A 1 269 ? 31.287 -5.603 -11.389 1.00 88.08 ? 269 LEU A C 1 ATOM 2151 O O . LEU A 1 269 ? 31.358 -6.507 -10.561 1.00 85.82 ? 269 LEU A O 1 ATOM 2152 C CB . LEU A 1 269 ? 32.335 -5.881 -13.623 1.00 85.85 ? 269 LEU A CB 1 ATOM 2153 C CG . LEU A 1 269 ? 33.400 -5.511 -14.658 1.00 84.89 ? 269 LEU A CG 1 ATOM 2154 C CD1 . LEU A 1 269 ? 33.368 -6.472 -15.834 1.00 84.11 ? 269 LEU A CD1 1 ATOM 2155 C CD2 . LEU A 1 269 ? 33.210 -4.078 -15.130 1.00 87.85 ? 269 LEU A CD2 1 ATOM 2156 N N . GLU A 1 270 ? 30.189 -4.883 -11.612 1.00 93.94 ? 270 GLU A N 1 ATOM 2157 C CA . GLU A 1 270 ? 28.922 -5.124 -10.926 1.00 97.28 ? 270 GLU A CA 1 ATOM 2158 C C . GLU A 1 270 ? 27.927 -5.762 -11.903 1.00 94.31 ? 270 GLU A C 1 ATOM 2159 O O . GLU A 1 270 ? 28.264 -6.018 -13.061 1.00 94.38 ? 270 GLU A O 1 ATOM 2160 C CB . GLU A 1 270 ? 28.362 -3.808 -10.366 1.00 104.49 ? 270 GLU A CB 1 ATOM 2161 C CG . GLU A 1 270 ? 29.326 -3.008 -9.490 1.00 109.15 ? 270 GLU A CG 1 ATOM 2162 C CD . GLU A 1 270 ? 29.442 -3.536 -8.061 1.00 112.41 ? 270 GLU A CD 1 ATOM 2163 O OE1 . GLU A 1 270 ? 29.708 -4.748 -7.878 1.00 112.16 ? 270 GLU A OE1 1 ATOM 2164 O OE2 . GLU A 1 270 ? 29.271 -2.733 -7.113 1.00 114.39 ? 270 GLU A OE2 1 ATOM 2165 N N . TYR A 1 271 ? 26.708 -6.016 -11.429 1.00 92.73 ? 271 TYR A N 1 ATOM 2166 C CA . TYR A 1 271 ? 25.667 -6.673 -12.227 1.00 91.72 ? 271 TYR A CA 1 ATOM 2167 C C . TYR A 1 271 ? 25.210 -5.808 -13.402 1.00 93.45 ? 271 TYR A C 1 ATOM 2168 O O . TYR A 1 271 ? 24.972 -4.611 -13.246 1.00 93.31 ? 271 TYR A O 1 ATOM 2169 C CB . TYR A 1 271 ? 24.469 -6.999 -11.335 1.00 93.40 ? 271 TYR A CB 1 ATOM 2170 C CG . TYR A 1 271 ? 23.376 -7.806 -12.001 1.00 93.72 ? 271 TYR A CG 1 ATOM 2171 C CD1 . TYR A 1 271 ? 23.650 -9.033 -12.596 1.00 90.59 ? 271 TYR A CD1 1 ATOM 2172 C CD2 . TYR A 1 271 ? 22.058 -7.353 -12.009 1.00 95.81 ? 271 TYR A CD2 1 ATOM 2173 C CE1 . TYR A 1 271 ? 22.648 -9.777 -13.195 1.00 92.07 ? 271 TYR A CE1 1 ATOM 2174 C CE2 . TYR A 1 271 ? 21.050 -8.092 -12.600 1.00 96.85 ? 271 TYR A CE2 1 ATOM 2175 C CZ . TYR A 1 271 ? 21.349 -9.302 -13.192 1.00 95.17 ? 271 TYR A CZ 1 ATOM 2176 O OH . TYR A 1 271 ? 20.348 -10.034 -13.778 1.00 95.95 ? 271 TYR A OH 1 ATOM 2177 N N . GLY A 1 272 ? 25.076 -6.427 -14.573 1.00 94.38 ? 272 GLY A N 1 ATOM 2178 C CA . GLY A 1 272 ? 24.750 -5.703 -15.800 1.00 97.13 ? 272 GLY A CA 1 ATOM 2179 C C . GLY A 1 272 ? 23.274 -5.602 -16.153 1.00 102.03 ? 272 GLY A C 1 ATOM 2180 O O . GLY A 1 272 ? 22.924 -4.896 -17.103 1.00 102.20 ? 272 GLY A O 1 ATOM 2181 N N . ASN A 1 273 ? 22.411 -6.286 -15.393 1.00 105.04 ? 273 ASN A N 1 ATOM 2182 C CA . ASN A 1 273 ? 20.979 -6.415 -15.724 1.00 110.48 ? 273 ASN A CA 1 ATOM 2183 C C . ASN A 1 273 ? 20.848 -6.993 -17.127 1.00 108.15 ? 273 ASN A C 1 ATOM 2184 O O . ASN A 1 273 ? 20.432 -6.314 -18.065 1.00 108.92 ? 273 ASN A O 1 ATOM 2185 C CB . ASN A 1 273 ? 20.243 -5.073 -15.601 1.00 115.24 ? 273 ASN A CB 1 ATOM 2186 C CG . ASN A 1 273 ? 20.223 -4.545 -14.176 1.00 118.59 ? 273 ASN A CG 1 ATOM 2187 O OD1 . ASN A 1 273 ? 20.967 -3.626 -13.833 1.00 119.66 ? 273 ASN A OD1 1 ATOM 2188 N ND2 . ASN A 1 273 ? 19.370 -5.126 -13.337 1.00 120.59 ? 273 ASN A ND2 1 ATOM 2189 N N . CYS A 1 274 ? 21.197 -8.267 -17.247 1.00 105.17 ? 274 CYS A N 1 ATOM 2190 C CA . CYS A 1 274 ? 21.696 -8.798 -18.507 1.00 103.75 ? 274 CYS A CA 1 ATOM 2191 C C . CYS A 1 274 ? 21.576 -10.323 -18.580 1.00 97.35 ? 274 CYS A C 1 ATOM 2192 O O . CYS A 1 274 ? 21.532 -10.985 -17.548 1.00 97.08 ? 274 CYS A O 1 ATOM 2193 C CB . CYS A 1 274 ? 23.164 -8.375 -18.601 1.00 104.14 ? 274 CYS A CB 1 ATOM 2194 S SG . CYS A 1 274 ? 24.069 -9.047 -19.991 1.00 110.87 ? 274 CYS A SG 1 ATOM 2195 N N . ASN A 1 275 ? 21.534 -10.877 -19.791 1.00 93.73 ? 275 ASN A N 1 ATOM 2196 C CA . ASN A 1 275 ? 21.523 -12.342 -19.975 1.00 93.29 ? 275 ASN A CA 1 ATOM 2197 C C . ASN A 1 275 ? 22.459 -12.815 -21.100 1.00 91.41 ? 275 ASN A C 1 ATOM 2198 O O . ASN A 1 275 ? 22.585 -12.154 -22.131 1.00 93.63 ? 275 ASN A O 1 ATOM 2199 C CB . ASN A 1 275 ? 20.095 -12.837 -20.238 1.00 95.83 ? 275 ASN A CB 1 ATOM 2200 C CG . ASN A 1 275 ? 19.979 -14.354 -20.205 1.00 94.34 ? 275 ASN A CG 1 ATOM 2201 O OD1 . ASN A 1 275 ? 20.527 -15.016 -19.331 1.00 92.63 ? 275 ASN A OD1 1 ATOM 2202 N ND2 . ASN A 1 275 ? 19.253 -14.907 -21.158 1.00 97.02 ? 275 ASN A ND2 1 ATOM 2203 N N . THR A 1 276 ? 23.106 -13.964 -20.896 1.00 89.33 ? 276 THR A N 1 ATOM 2204 C CA . THR A 1 276 ? 24.095 -14.493 -21.844 1.00 84.53 ? 276 THR A CA 1 ATOM 2205 C C . THR A 1 276 ? 24.223 -16.004 -21.696 1.00 84.38 ? 276 THR A C 1 ATOM 2206 O O . THR A 1 276 ? 23.771 -16.568 -20.705 1.00 86.87 ? 276 THR A O 1 ATOM 2207 C CB . THR A 1 276 ? 25.483 -13.851 -21.609 1.00 81.83 ? 276 THR A CB 1 ATOM 2208 O OG1 . THR A 1 276 ? 26.363 -14.158 -22.696 1.00 81.25 ? 276 THR A OG1 1 ATOM 2209 C CG2 . THR A 1 276 ? 26.119 -14.343 -20.295 1.00 81.09 ? 276 THR A CG2 1 ATOM 2210 N N . LYS A 1 277 ? 24.847 -16.648 -22.677 1.00 84.60 ? 277 LYS A N 1 ATOM 2211 C CA . LYS A 1 277 ? 25.157 -18.082 -22.608 1.00 87.02 ? 277 LYS A CA 1 ATOM 2212 C C . LYS A 1 277 ? 26.635 -18.344 -22.314 1.00 82.67 ? 277 LYS A C 1 ATOM 2213 O O . LYS A 1 277 ? 27.040 -19.490 -22.135 1.00 82.20 ? 277 LYS A O 1 ATOM 2214 C CB . LYS A 1 277 ? 24.771 -18.785 -23.918 1.00 91.48 ? 277 LYS A CB 1 ATOM 2215 C CG . LYS A 1 277 ? 23.282 -19.075 -24.070 1.00 98.66 ? 277 LYS A CG 1 ATOM 2216 C CD . LYS A 1 277 ? 23.029 -20.078 -25.192 1.00 102.42 ? 277 LYS A CD 1 ATOM 2217 C CE . LYS A 1 277 ? 21.551 -20.408 -25.349 1.00 108.67 ? 277 LYS A CE 1 ATOM 2218 N NZ . LYS A 1 277 ? 20.971 -21.030 -24.123 1.00 112.46 ? 277 LYS A NZ 1 ATOM 2219 N N . CYS A 1 278 ? 27.439 -17.286 -22.276 1.00 79.69 ? 278 CYS A N 1 ATOM 2220 C CA . CYS A 1 278 ? 28.874 -17.424 -22.065 1.00 77.66 ? 278 CYS A CA 1 ATOM 2221 C C . CYS A 1 278 ? 29.410 -16.179 -21.373 1.00 73.56 ? 278 CYS A C 1 ATOM 2222 O O . CYS A 1 278 ? 29.267 -15.071 -21.889 1.00 73.09 ? 278 CYS A O 1 ATOM 2223 C CB . CYS A 1 278 ? 29.582 -17.641 -23.407 1.00 78.04 ? 278 CYS A CB 1 ATOM 2224 S SG . CYS A 1 278 ? 31.392 -17.631 -23.325 1.00 78.05 ? 278 CYS A SG 1 ATOM 2225 N N . GLN A 1 279 ? 30.021 -16.364 -20.206 1.00 71.28 ? 279 GLN A N 1 ATOM 2226 C CA . GLN A 1 279 ? 30.466 -15.237 -19.387 1.00 69.75 ? 279 GLN A CA 1 ATOM 2227 C C . GLN A 1 279 ? 31.961 -15.275 -19.120 1.00 67.41 ? 279 GLN A C 1 ATOM 2228 O O . GLN A 1 279 ? 32.521 -16.337 -18.865 1.00 66.99 ? 279 GLN A O 1 ATOM 2229 C CB . GLN A 1 279 ? 29.730 -15.231 -18.049 1.00 70.33 ? 279 GLN A CB 1 ATOM 2230 C CG . GLN A 1 279 ? 29.982 -13.984 -17.216 1.00 70.07 ? 279 GLN A CG 1 ATOM 2231 C CD . GLN A 1 279 ? 29.249 -12.769 -17.747 1.00 71.33 ? 279 GLN A CD 1 ATOM 2232 O OE1 . GLN A 1 279 ? 28.024 -12.779 -17.862 1.00 74.70 ? 279 GLN A OE1 1 ATOM 2233 N NE2 . GLN A 1 279 ? 29.989 -11.712 -18.065 1.00 69.92 ? 279 GLN A NE2 1 ATOM 2234 N N . THR A 1 280 ? 32.585 -14.101 -19.162 1.00 66.75 ? 280 THR A N 1 ATOM 2235 C CA . THR A 1 280 ? 33.971 -13.922 -18.736 1.00 66.07 ? 280 THR A CA 1 ATOM 2236 C C . THR A 1 280 ? 34.042 -12.837 -17.658 1.00 67.67 ? 280 THR A C 1 ATOM 2237 O O . THR A 1 280 ? 33.102 -12.045 -17.514 1.00 67.97 ? 280 THR A O 1 ATOM 2238 C CB . THR A 1 280 ? 34.877 -13.495 -19.909 1.00 64.70 ? 280 THR A CB 1 ATOM 2239 O OG1 . THR A 1 280 ? 34.873 -12.066 -20.044 1.00 63.01 ? 280 THR A OG1 1 ATOM 2240 C CG2 . THR A 1 280 ? 34.423 -14.138 -21.209 1.00 65.34 ? 280 THR A CG2 1 ATOM 2241 N N . PRO A 1 281 ? 35.162 -12.781 -16.912 1.00 68.82 ? 281 PRO A N 1 ATOM 2242 C CA . PRO A 1 281 ? 35.371 -11.735 -15.900 1.00 69.88 ? 281 PRO A CA 1 ATOM 2243 C C . PRO A 1 281 ? 35.409 -10.306 -16.451 1.00 71.73 ? 281 PRO A C 1 ATOM 2244 O O . PRO A 1 281 ? 35.289 -9.354 -15.676 1.00 72.46 ? 281 PRO A O 1 ATOM 2245 C CB . PRO A 1 281 ? 36.733 -12.084 -15.294 1.00 70.24 ? 281 PRO A CB 1 ATOM 2246 C CG . PRO A 1 281 ? 36.982 -13.506 -15.634 1.00 69.68 ? 281 PRO A CG 1 ATOM 2247 C CD . PRO A 1 281 ? 36.221 -13.806 -16.884 1.00 68.52 ? 281 PRO A CD 1 ATOM 2248 N N . MET A 1 282 ? 35.597 -10.165 -17.763 1.00 74.46 ? 282 MET A N 1 ATOM 2249 C CA . MET A 1 282 ? 35.600 -8.858 -18.430 1.00 76.85 ? 282 MET A CA 1 ATOM 2250 C C . MET A 1 282 ? 34.261 -8.506 -19.071 1.00 75.56 ? 282 MET A C 1 ATOM 2251 O O . MET A 1 282 ? 34.028 -7.347 -19.410 1.00 77.39 ? 282 MET A O 1 ATOM 2252 C CB . MET A 1 282 ? 36.674 -8.828 -19.511 1.00 80.75 ? 282 MET A CB 1 ATOM 2253 C CG . MET A 1 282 ? 38.079 -8.639 -18.973 1.00 86.01 ? 282 MET A CG 1 ATOM 2254 S SD . MET A 1 282 ? 39.311 -8.841 -20.273 1.00 96.22 ? 282 MET A SD 1 ATOM 2255 C CE . MET A 1 282 ? 38.634 -7.825 -21.590 1.00 93.78 ? 282 MET A CE 1 ATOM 2256 N N . GLY A 1 283 ? 33.395 -9.501 -19.248 1.00 72.43 ? 283 GLY A N 1 ATOM 2257 C CA . GLY A 1 283 ? 32.112 -9.301 -19.915 1.00 72.44 ? 283 GLY A CA 1 ATOM 2258 C C . GLY A 1 283 ? 31.647 -10.569 -20.600 1.00 71.65 ? 283 GLY A C 1 ATOM 2259 O O . GLY A 1 283 ? 32.400 -11.538 -20.692 1.00 70.01 ? 283 GLY A O 1 ATOM 2260 N N . ALA A 1 284 ? 30.413 -10.556 -21.095 1.00 72.16 ? 284 ALA A N 1 ATOM 2261 C CA . ALA A 1 284 ? 29.795 -11.746 -21.684 1.00 72.83 ? 284 ALA A CA 1 ATOM 2262 C C . ALA A 1 284 ? 29.993 -11.819 -23.204 1.00 74.63 ? 284 ALA A C 1 ATOM 2263 O O . ALA A 1 284 ? 30.371 -10.829 -23.842 1.00 74.38 ? 284 ALA A O 1 ATOM 2264 C CB . ALA A 1 284 ? 28.316 -11.777 -21.344 1.00 74.77 ? 284 ALA A CB 1 ATOM 2265 N N . ILE A 1 285 ? 29.709 -12.994 -23.772 1.00 75.85 ? 285 ILE A N 1 ATOM 2266 C CA . ILE A 1 285 ? 29.945 -13.274 -25.194 1.00 77.88 ? 285 ILE A CA 1 ATOM 2267 C C . ILE A 1 285 ? 28.696 -13.833 -25.871 1.00 82.40 ? 285 ILE A C 1 ATOM 2268 O O . ILE A 1 285 ? 28.087 -14.790 -25.390 1.00 86.11 ? 285 ILE A O 1 ATOM 2269 C CB . ILE A 1 285 ? 31.118 -14.272 -25.383 1.00 75.65 ? 285 ILE A CB 1 ATOM 2270 C CG1 . ILE A 1 285 ? 32.456 -13.566 -25.149 1.00 73.24 ? 285 ILE A CG1 1 ATOM 2271 C CG2 . ILE A 1 285 ? 31.114 -14.884 -26.777 1.00 75.08 ? 285 ILE A CG2 1 ATOM 2272 C CD1 . ILE A 1 285 ? 33.620 -14.509 -24.934 1.00 71.71 ? 285 ILE A CD1 1 ATOM 2273 N N . ASN A 1 286 ? 28.332 -13.223 -26.995 1.00 86.55 ? 286 ASN A N 1 ATOM 2274 C CA . ASN A 1 286 ? 27.244 -13.693 -27.844 1.00 92.24 ? 286 ASN A CA 1 ATOM 2275 C C . ASN A 1 286 ? 27.781 -13.832 -29.261 1.00 87.38 ? 286 ASN A C 1 ATOM 2276 O O . ASN A 1 286 ? 27.817 -12.872 -30.026 1.00 84.76 ? 286 ASN A O 1 ATOM 2277 C CB . ASN A 1 286 ? 26.082 -12.704 -27.794 1.00 101.16 ? 286 ASN A CB 1 ATOM 2278 C CG . ASN A 1 286 ? 24.940 -13.088 -28.713 1.00 114.54 ? 286 ASN A CG 1 ATOM 2279 O OD1 . ASN A 1 286 ? 24.629 -14.270 -28.885 1.00 113.77 ? 286 ASN A OD1 1 ATOM 2280 N ND2 . ASN A 1 286 ? 24.299 -12.071 -29.309 1.00 132.54 ? 286 ASN A ND2 1 ATOM 2281 N N . SER A 1 287 ? 28.219 -15.035 -29.598 1.00 84.48 ? 287 SER A N 1 ATOM 2282 C CA . SER A 1 287 ? 28.939 -15.254 -30.839 1.00 82.44 ? 287 SER A CA 1 ATOM 2283 C C . SER A 1 287 ? 28.771 -16.685 -31.327 1.00 81.66 ? 287 SER A C 1 ATOM 2284 O O . SER A 1 287 ? 28.602 -17.602 -30.531 1.00 82.15 ? 287 SER A O 1 ATOM 2285 C CB . SER A 1 287 ? 30.424 -14.947 -30.619 1.00 79.94 ? 287 SER A CB 1 ATOM 2286 O OG . SER A 1 287 ? 31.140 -14.915 -31.839 1.00 77.03 ? 287 SER A OG 1 ATOM 2287 N N . SER A 1 288 ? 28.812 -16.863 -32.642 1.00 82.44 ? 288 SER A N 1 ATOM 2288 C CA . SER A 1 288 ? 28.803 -18.193 -33.244 1.00 83.62 ? 288 SER A CA 1 ATOM 2289 C C . SER A 1 288 ? 30.207 -18.598 -33.720 1.00 78.73 ? 288 SER A C 1 ATOM 2290 O O . SER A 1 288 ? 30.378 -19.651 -34.326 1.00 77.76 ? 288 SER A O 1 ATOM 2291 C CB . SER A 1 288 ? 27.801 -18.233 -34.399 1.00 88.37 ? 288 SER A CB 1 ATOM 2292 O OG . SER A 1 288 ? 27.990 -17.134 -35.276 1.00 90.58 ? 288 SER A OG 1 ATOM 2293 N N . MET A 1 289 ? 31.206 -17.771 -33.420 1.00 75.60 ? 289 MET A N 1 ATOM 2294 C CA . MET A 1 289 ? 32.589 -18.042 -33.811 1.00 74.75 ? 289 MET A CA 1 ATOM 2295 C C . MET A 1 289 ? 33.151 -19.211 -33.011 1.00 73.48 ? 289 MET A C 1 ATOM 2296 O O . MET A 1 289 ? 32.807 -19.379 -31.847 1.00 75.47 ? 289 MET A O 1 ATOM 2297 C CB . MET A 1 289 ? 33.481 -16.831 -33.538 1.00 76.18 ? 289 MET A CB 1 ATOM 2298 C CG . MET A 1 289 ? 33.068 -15.543 -34.221 1.00 78.19 ? 289 MET A CG 1 ATOM 2299 S SD . MET A 1 289 ? 33.421 -15.560 -35.976 1.00 79.54 ? 289 MET A SD 1 ATOM 2300 C CE . MET A 1 289 ? 33.589 -13.794 -36.232 1.00 77.62 ? 289 MET A CE 1 ATOM 2301 N N . PRO A 1 290 ? 34.030 -20.017 -33.625 1.00 72.11 ? 290 PRO A N 1 ATOM 2302 C CA . PRO A 1 290 ? 34.654 -21.113 -32.884 1.00 71.33 ? 290 PRO A CA 1 ATOM 2303 C C . PRO A 1 290 ? 35.742 -20.675 -31.899 1.00 69.92 ? 290 PRO A C 1 ATOM 2304 O O . PRO A 1 290 ? 36.089 -21.450 -31.010 1.00 73.00 ? 290 PRO A O 1 ATOM 2305 C CB . PRO A 1 290 ? 35.259 -21.978 -33.994 1.00 70.56 ? 290 PRO A CB 1 ATOM 2306 C CG . PRO A 1 290 ? 35.537 -21.017 -35.092 1.00 70.26 ? 290 PRO A CG 1 ATOM 2307 C CD . PRO A 1 290 ? 34.394 -20.049 -35.054 1.00 70.38 ? 290 PRO A CD 1 ATOM 2308 N N . PHE A 1 291 ? 36.273 -19.461 -32.055 1.00 66.57 ? 291 PHE A N 1 ATOM 2309 C CA . PHE A 1 291 ? 37.333 -18.953 -31.180 1.00 65.28 ? 291 PHE A CA 1 ATOM 2310 C C . PHE A 1 291 ? 36.997 -17.585 -30.629 1.00 62.81 ? 291 PHE A C 1 ATOM 2311 O O . PHE A 1 291 ? 36.208 -16.857 -31.216 1.00 62.48 ? 291 PHE A O 1 ATOM 2312 C CB . PHE A 1 291 ? 38.641 -18.779 -31.946 1.00 66.61 ? 291 PHE A CB 1 ATOM 2313 C CG . PHE A 1 291 ? 39.287 -20.053 -32.372 1.00 68.18 ? 291 PHE A CG 1 ATOM 2314 C CD1 . PHE A 1 291 ? 39.969 -20.836 -31.455 1.00 71.24 ? 291 PHE A CD1 1 ATOM 2315 C CD2 . PHE A 1 291 ? 39.254 -20.451 -33.701 1.00 70.31 ? 291 PHE A CD2 1 ATOM 2316 C CE1 . PHE A 1 291 ? 40.591 -22.007 -31.850 1.00 72.95 ? 291 PHE A CE1 1 ATOM 2317 C CE2 . PHE A 1 291 ? 39.872 -21.621 -34.105 1.00 71.96 ? 291 PHE A CE2 1 ATOM 2318 C CZ . PHE A 1 291 ? 40.539 -22.400 -33.177 1.00 73.27 ? 291 PHE A CZ 1 ATOM 2319 N N . HIS A 1 292 ? 37.640 -17.230 -29.517 1.00 61.47 ? 292 HIS A N 1 ATOM 2320 C CA . HIS A 1 292 ? 37.622 -15.855 -29.009 1.00 59.89 ? 292 HIS A CA 1 ATOM 2321 C C . HIS A 1 292 ? 38.943 -15.535 -28.320 1.00 58.79 ? 292 HIS A C 1 ATOM 2322 O O . HIS A 1 292 ? 39.739 -16.442 -28.048 1.00 57.47 ? 292 HIS A O 1 ATOM 2323 C CB . HIS A 1 292 ? 36.454 -15.642 -28.043 1.00 61.90 ? 292 HIS A CB 1 ATOM 2324 C CG . HIS A 1 292 ? 36.622 -16.330 -26.724 1.00 61.84 ? 292 HIS A CG 1 ATOM 2325 N ND1 . HIS A 1 292 ? 37.175 -15.711 -25.625 1.00 61.34 ? 292 HIS A ND1 1 ATOM 2326 C CD2 . HIS A 1 292 ? 36.312 -17.585 -26.328 1.00 62.86 ? 292 HIS A CD2 1 ATOM 2327 C CE1 . HIS A 1 292 ? 37.199 -16.555 -24.610 1.00 62.24 ? 292 HIS A CE1 1 ATOM 2328 N NE2 . HIS A 1 292 ? 36.683 -17.701 -25.011 1.00 63.68 ? 292 HIS A NE2 1 ATOM 2329 N N . ASN A 1 293 ? 39.172 -14.250 -28.048 1.00 57.41 ? 293 ASN A N 1 ATOM 2330 C CA . ASN A 1 293 ? 40.394 -13.794 -27.369 1.00 57.76 ? 293 ASN A CA 1 ATOM 2331 C C . ASN A 1 293 ? 40.128 -12.815 -26.210 1.00 59.80 ? 293 ASN A C 1 ATOM 2332 O O . ASN A 1 293 ? 40.979 -11.997 -25.863 1.00 60.80 ? 293 ASN A O 1 ATOM 2333 C CB . ASN A 1 293 ? 41.342 -13.161 -28.390 1.00 57.73 ? 293 ASN A CB 1 ATOM 2334 C CG . ASN A 1 293 ? 40.847 -11.821 -28.910 1.00 57.75 ? 293 ASN A CG 1 ATOM 2335 O OD1 . ASN A 1 293 ? 39.730 -11.400 -28.629 1.00 58.09 ? 293 ASN A OD1 1 ATOM 2336 N ND2 . ASN A 1 293 ? 41.688 -11.140 -29.663 1.00 58.83 ? 293 ASN A ND2 1 ATOM 2337 N N . ILE A 1 294 ? 38.945 -12.911 -25.615 1.00 61.23 ? 294 ILE A N 1 ATOM 2338 C CA . ILE A 1 294 ? 38.537 -12.026 -24.526 1.00 63.70 ? 294 ILE A CA 1 ATOM 2339 C C . ILE A 1 294 ? 39.268 -12.325 -23.214 1.00 64.04 ? 294 ILE A C 1 ATOM 2340 O O . ILE A 1 294 ? 39.921 -11.445 -22.659 1.00 65.09 ? 294 ILE A O 1 ATOM 2341 C CB . ILE A 1 294 ? 37.013 -12.113 -24.268 1.00 64.98 ? 294 ILE A CB 1 ATOM 2342 C CG1 . ILE A 1 294 ? 36.210 -11.883 -25.564 1.00 64.93 ? 294 ILE A CG1 1 ATOM 2343 C CG2 . ILE A 1 294 ? 36.600 -11.118 -23.197 1.00 66.52 ? 294 ILE A CG2 1 ATOM 2344 C CD1 . ILE A 1 294 ? 36.636 -10.667 -26.361 1.00 65.81 ? 294 ILE A CD1 1 ATOM 2345 N N . HIS A 1 295 ? 39.145 -13.560 -22.726 1.00 63.50 ? 295 HIS A N 1 ATOM 2346 C CA . HIS A 1 295 ? 39.693 -13.961 -21.428 1.00 64.00 ? 295 HIS A CA 1 ATOM 2347 C C . HIS A 1 295 ? 39.660 -15.504 -21.309 1.00 64.01 ? 295 HIS A C 1 ATOM 2348 O O . HIS A 1 295 ? 38.696 -16.126 -21.752 1.00 61.56 ? 295 HIS A O 1 ATOM 2349 C CB . HIS A 1 295 ? 38.843 -13.328 -20.326 1.00 66.37 ? 295 HIS A CB 1 ATOM 2350 C CG . HIS A 1 295 ? 39.501 -13.287 -18.985 1.00 68.74 ? 295 HIS A CG 1 ATOM 2351 N ND1 . HIS A 1 295 ? 39.711 -14.416 -18.228 1.00 69.73 ? 295 HIS A ND1 1 ATOM 2352 C CD2 . HIS A 1 295 ? 39.963 -12.251 -18.247 1.00 71.01 ? 295 HIS A CD2 1 ATOM 2353 C CE1 . HIS A 1 295 ? 40.297 -14.085 -17.092 1.00 70.77 ? 295 HIS A CE1 1 ATOM 2354 N NE2 . HIS A 1 295 ? 40.459 -12.775 -17.077 1.00 71.42 ? 295 HIS A NE2 1 ATOM 2355 N N . PRO A 1 296 ? 40.700 -16.126 -20.709 1.00 64.71 ? 296 PRO A N 1 ATOM 2356 C CA . PRO A 1 296 ? 40.730 -17.600 -20.638 1.00 65.40 ? 296 PRO A CA 1 ATOM 2357 C C . PRO A 1 296 ? 39.711 -18.245 -19.687 1.00 67.20 ? 296 PRO A C 1 ATOM 2358 O O . PRO A 1 296 ? 39.224 -19.339 -19.966 1.00 67.79 ? 296 PRO A O 1 ATOM 2359 C CB . PRO A 1 296 ? 42.161 -17.909 -20.175 1.00 66.61 ? 296 PRO A CB 1 ATOM 2360 C CG . PRO A 1 296 ? 42.642 -16.663 -19.522 1.00 67.15 ? 296 PRO A CG 1 ATOM 2361 C CD . PRO A 1 296 ? 41.959 -15.528 -20.229 1.00 65.89 ? 296 PRO A CD 1 ATOM 2362 N N . LEU A 1 297 ? 39.409 -17.594 -18.570 1.00 68.53 ? 297 LEU A N 1 ATOM 2363 C CA . LEU A 1 297 ? 38.449 -18.128 -17.594 1.00 71.77 ? 297 LEU A CA 1 ATOM 2364 C C . LEU A 1 297 ? 36.998 -17.809 -17.970 1.00 70.74 ? 297 LEU A C 1 ATOM 2365 O O . LEU A 1 297 ? 36.517 -16.707 -17.734 1.00 73.40 ? 297 LEU A O 1 ATOM 2366 C CB . LEU A 1 297 ? 38.766 -17.593 -16.188 1.00 72.98 ? 297 LEU A CB 1 ATOM 2367 C CG . LEU A 1 297 ? 40.216 -17.763 -15.723 1.00 75.57 ? 297 LEU A CG 1 ATOM 2368 C CD1 . LEU A 1 297 ? 40.428 -17.102 -14.365 1.00 76.88 ? 297 LEU A CD1 1 ATOM 2369 C CD2 . LEU A 1 297 ? 40.607 -19.234 -15.677 1.00 77.78 ? 297 LEU A CD2 1 ATOM 2370 N N . THR A 1 298 ? 36.300 -18.773 -18.555 1.00 70.42 ? 298 THR A N 1 ATOM 2371 C CA . THR A 1 298 ? 34.907 -18.572 -18.946 1.00 68.74 ? 298 THR A CA 1 ATOM 2372 C C . THR A 1 298 ? 34.015 -19.644 -18.342 1.00 69.89 ? 298 THR A C 1 ATOM 2373 O O . THR A 1 298 ? 34.497 -20.637 -17.803 1.00 68.87 ? 298 THR A O 1 ATOM 2374 C CB . THR A 1 298 ? 34.731 -18.585 -20.479 1.00 68.75 ? 298 THR A CB 1 ATOM 2375 O OG1 . THR A 1 298 ? 34.782 -19.930 -20.972 1.00 70.02 ? 298 THR A OG1 1 ATOM 2376 C CG2 . THR A 1 298 ? 35.813 -17.767 -21.152 1.00 68.89 ? 298 THR A CG2 1 ATOM 2377 N N . ILE A 1 299 ? 32.709 -19.428 -18.435 1.00 71.39 ? 299 ILE A N 1 ATOM 2378 C CA . ILE A 1 299 ? 31.732 -20.405 -17.976 1.00 74.58 ? 299 ILE A CA 1 ATOM 2379 C C . ILE A 1 299 ? 30.549 -20.373 -18.930 1.00 76.46 ? 299 ILE A C 1 ATOM 2380 O O . ILE A 1 299 ? 30.158 -19.298 -19.392 1.00 75.35 ? 299 ILE A O 1 ATOM 2381 C CB . ILE A 1 299 ? 31.293 -20.132 -16.516 1.00 76.86 ? 299 ILE A CB 1 ATOM 2382 C CG1 . ILE A 1 299 ? 30.285 -21.182 -16.044 1.00 79.40 ? 299 ILE A CG1 1 ATOM 2383 C CG2 . ILE A 1 299 ? 30.713 -18.730 -16.356 1.00 76.71 ? 299 ILE A CG2 1 ATOM 2384 C CD1 . ILE A 1 299 ? 30.105 -21.207 -14.542 1.00 80.76 ? 299 ILE A CD1 1 ATOM 2385 N N . GLY A 1 300 ? 30.005 -21.552 -19.235 1.00 79.59 ? 300 GLY A N 1 ATOM 2386 C CA . GLY A 1 300 ? 28.896 -21.685 -20.177 1.00 83.89 ? 300 GLY A CA 1 ATOM 2387 C C . GLY A 1 300 ? 29.310 -22.324 -21.492 1.00 86.95 ? 300 GLY A C 1 ATOM 2388 O O . GLY A 1 300 ? 30.358 -22.965 -21.580 1.00 86.78 ? 300 GLY A O 1 ATOM 2389 N N . GLU A 1 301 ? 28.478 -22.148 -22.518 1.00 91.58 ? 301 GLU A N 1 ATOM 2390 C CA . GLU A 1 301 ? 28.753 -22.700 -23.843 1.00 94.74 ? 301 GLU A CA 1 ATOM 2391 C C . GLU A 1 301 ? 29.561 -21.670 -24.615 1.00 89.33 ? 301 GLU A C 1 ATOM 2392 O O . GLU A 1 301 ? 28.997 -20.754 -25.217 1.00 89.56 ? 301 GLU A O 1 ATOM 2393 C CB . GLU A 1 301 ? 27.449 -23.044 -24.580 1.00 102.30 ? 301 GLU A CB 1 ATOM 2394 C CG . GLU A 1 301 ? 27.494 -24.375 -25.318 1.00 109.46 ? 301 GLU A CG 1 ATOM 2395 C CD . GLU A 1 301 ? 27.486 -25.568 -24.369 1.00 117.12 ? 301 GLU A CD 1 ATOM 2396 O OE1 . GLU A 1 301 ? 26.529 -25.701 -23.569 1.00 119.91 ? 301 GLU A OE1 1 ATOM 2397 O OE2 . GLU A 1 301 ? 28.446 -26.369 -24.411 1.00 122.17 ? 301 GLU A OE2 1 ATOM 2398 N N . CYS A 1 302 ? 30.884 -21.818 -24.586 1.00 84.80 ? 302 CYS A N 1 ATOM 2399 C CA . CYS A 1 302 ? 31.784 -20.784 -25.091 1.00 80.17 ? 302 CYS A CA 1 ATOM 2400 C C . CYS A 1 302 ? 32.634 -21.217 -26.288 1.00 76.73 ? 302 CYS A C 1 ATOM 2401 O O . CYS A 1 302 ? 32.869 -22.408 -26.506 1.00 74.20 ? 302 CYS A O 1 ATOM 2402 C CB . CYS A 1 302 ? 32.717 -20.324 -23.971 1.00 79.93 ? 302 CYS A CB 1 ATOM 2403 S SG . CYS A 1 302 ? 31.887 -19.486 -22.599 1.00 83.72 ? 302 CYS A SG 1 ATOM 2404 N N . PRO A 1 303 ? 33.113 -20.235 -27.066 1.00 73.73 ? 303 PRO A N 1 ATOM 2405 C CA . PRO A 1 303 ? 34.166 -20.542 -28.023 1.00 72.53 ? 303 PRO A CA 1 ATOM 2406 C C . PRO A 1 303 ? 35.476 -20.856 -27.299 1.00 71.72 ? 303 PRO A C 1 ATOM 2407 O O . PRO A 1 303 ? 35.592 -20.613 -26.095 1.00 71.50 ? 303 PRO A O 1 ATOM 2408 C CB . PRO A 1 303 ? 34.288 -19.257 -28.858 1.00 71.16 ? 303 PRO A CB 1 ATOM 2409 C CG . PRO A 1 303 ? 33.119 -18.404 -28.497 1.00 71.30 ? 303 PRO A CG 1 ATOM 2410 C CD . PRO A 1 303 ? 32.695 -18.825 -27.128 1.00 72.57 ? 303 PRO A CD 1 ATOM 2411 N N . LYS A 1 304 ? 36.452 -21.387 -28.027 1.00 71.37 ? 304 LYS A N 1 ATOM 2412 C CA . LYS A 1 304 ? 37.737 -21.740 -27.433 1.00 72.21 ? 304 LYS A CA 1 ATOM 2413 C C . LYS A 1 304 ? 38.621 -20.507 -27.391 1.00 68.22 ? 304 LYS A C 1 ATOM 2414 O O . LYS A 1 304 ? 38.684 -19.742 -28.351 1.00 68.35 ? 304 LYS A O 1 ATOM 2415 C CB . LYS A 1 304 ? 38.424 -22.858 -28.218 1.00 76.15 ? 304 LYS A CB 1 ATOM 2416 C CG . LYS A 1 304 ? 37.542 -24.075 -28.481 1.00 82.62 ? 304 LYS A CG 1 ATOM 2417 C CD . LYS A 1 304 ? 37.181 -24.835 -27.206 1.00 88.23 ? 304 LYS A CD 1 ATOM 2418 C CE . LYS A 1 304 ? 35.724 -25.281 -27.209 1.00 91.80 ? 304 LYS A CE 1 ATOM 2419 N NZ . LYS A 1 304 ? 35.388 -26.045 -25.975 1.00 96.35 ? 304 LYS A NZ 1 ATOM 2420 N N . TYR A 1 305 ? 39.296 -20.312 -26.269 1.00 65.84 ? 305 TYR A N 1 ATOM 2421 C CA . TYR A 1 305 ? 40.114 -19.136 -26.086 1.00 64.53 ? 305 TYR A CA 1 ATOM 2422 C C . TYR A 1 305 ? 41.470 -19.321 -26.748 1.00 64.18 ? 305 TYR A C 1 ATOM 2423 O O . TYR A 1 305 ? 42.103 -20.363 -26.587 1.00 66.06 ? 305 TYR A O 1 ATOM 2424 C CB . TYR A 1 305 ? 40.300 -18.833 -24.596 1.00 64.89 ? 305 TYR A CB 1 ATOM 2425 C CG . TYR A 1 305 ? 41.230 -17.673 -24.353 1.00 63.88 ? 305 TYR A CG 1 ATOM 2426 C CD1 . TYR A 1 305 ? 40.789 -16.362 -24.493 1.00 62.40 ? 305 TYR A CD1 1 ATOM 2427 C CD2 . TYR A 1 305 ? 42.556 -17.885 -24.019 1.00 65.13 ? 305 TYR A CD2 1 ATOM 2428 C CE1 . TYR A 1 305 ? 41.643 -15.298 -24.288 1.00 63.05 ? 305 TYR A CE1 1 ATOM 2429 C CE2 . TYR A 1 305 ? 43.419 -16.823 -23.806 1.00 66.37 ? 305 TYR A CE2 1 ATOM 2430 C CZ . TYR A 1 305 ? 42.958 -15.533 -23.944 1.00 64.67 ? 305 TYR A CZ 1 ATOM 2431 O OH . TYR A 1 305 ? 43.816 -14.478 -23.740 1.00 65.99 ? 305 TYR A OH 1 ATOM 2432 N N . VAL A 1 306 ? 41.911 -18.301 -27.484 1.00 63.11 ? 306 VAL A N 1 ATOM 2433 C CA . VAL A 1 306 ? 43.282 -18.236 -28.006 1.00 62.48 ? 306 VAL A CA 1 ATOM 2434 C C . VAL A 1 306 ? 43.860 -16.842 -27.774 1.00 62.42 ? 306 VAL A C 1 ATOM 2435 O O . VAL A 1 306 ? 43.120 -15.882 -27.633 1.00 62.26 ? 306 VAL A O 1 ATOM 2436 C CB . VAL A 1 306 ? 43.356 -18.570 -29.515 1.00 61.34 ? 306 VAL A CB 1 ATOM 2437 C CG1 . VAL A 1 306 ? 42.922 -20.000 -29.771 1.00 62.35 ? 306 VAL A CG1 1 ATOM 2438 C CG2 . VAL A 1 306 ? 42.505 -17.616 -30.341 1.00 60.10 ? 306 VAL A CG2 1 ATOM 2439 N N . LYS A 1 307 ? 45.182 -16.740 -27.762 1.00 65.30 ? 307 LYS A N 1 ATOM 2440 C CA . LYS A 1 307 ? 45.871 -15.456 -27.615 1.00 69.86 ? 307 LYS A CA 1 ATOM 2441 C C . LYS A 1 307 ? 46.019 -14.639 -28.919 1.00 70.09 ? 307 LYS A C 1 ATOM 2442 O O . LYS A 1 307 ? 46.687 -13.612 -28.918 1.00 77.32 ? 307 LYS A O 1 ATOM 2443 C CB . LYS A 1 307 ? 47.270 -15.676 -27.014 1.00 72.62 ? 307 LYS A CB 1 ATOM 2444 C CG . LYS A 1 307 ? 47.318 -15.719 -25.500 1.00 74.32 ? 307 LYS A CG 1 ATOM 2445 C CD . LYS A 1 307 ? 48.670 -16.244 -25.051 1.00 79.62 ? 307 LYS A CD 1 ATOM 2446 C CE . LYS A 1 307 ? 48.886 -16.091 -23.557 1.00 83.76 ? 307 LYS A CE 1 ATOM 2447 N NZ . LYS A 1 307 ? 50.210 -16.648 -23.148 1.00 89.24 ? 307 LYS A NZ 1 ATOM 2448 N N . SER A 1 308 ? 45.416 -15.072 -30.020 1.00 67.90 ? 308 SER A N 1 ATOM 2449 C CA . SER A 1 308 ? 45.567 -14.361 -31.296 1.00 66.11 ? 308 SER A CA 1 ATOM 2450 C C . SER A 1 308 ? 44.878 -13.003 -31.289 1.00 65.95 ? 308 SER A C 1 ATOM 2451 O O . SER A 1 308 ? 43.873 -12.810 -30.608 1.00 66.20 ? 308 SER A O 1 ATOM 2452 C CB . SER A 1 308 ? 44.981 -15.179 -32.457 1.00 63.04 ? 308 SER A CB 1 ATOM 2453 O OG . SER A 1 308 ? 45.323 -16.543 -32.360 1.00 62.43 ? 308 SER A OG 1 ATOM 2454 N N . ASN A 1 309 ? 45.419 -12.079 -32.076 1.00 68.51 ? 309 ASN A N 1 ATOM 2455 C CA . ASN A 1 309 ? 44.718 -10.846 -32.431 1.00 71.54 ? 309 ASN A CA 1 ATOM 2456 C C . ASN A 1 309 ? 43.827 -11.021 -33.667 1.00 69.12 ? 309 ASN A C 1 ATOM 2457 O O . ASN A 1 309 ? 42.895 -10.245 -33.873 1.00 69.58 ? 309 ASN A O 1 ATOM 2458 C CB . ASN A 1 309 ? 45.724 -9.722 -32.693 1.00 76.93 ? 309 ASN A CB 1 ATOM 2459 C CG . ASN A 1 309 ? 46.424 -9.256 -31.426 1.00 82.53 ? 309 ASN A CG 1 ATOM 2460 O OD1 . ASN A 1 309 ? 45.787 -9.028 -30.389 1.00 85.42 ? 309 ASN A OD1 1 ATOM 2461 N ND2 . ASN A 1 309 ? 47.742 -9.095 -31.506 1.00 86.43 ? 309 ASN A ND2 1 ATOM 2462 N N . ARG A 1 310 ? 44.110 -12.045 -34.474 1.00 66.86 ? 310 ARG A N 1 ATOM 2463 C CA . ARG A 1 310 ? 43.484 -12.194 -35.784 1.00 65.89 ? 310 ARG A CA 1 ATOM 2464 C C . ARG A 1 310 ? 43.516 -13.653 -36.293 1.00 62.07 ? 310 ARG A C 1 ATOM 2465 O O . ARG A 1 310 ? 44.582 -14.265 -36.374 1.00 61.64 ? 310 ARG A O 1 ATOM 2466 C CB . ARG A 1 310 ? 44.215 -11.278 -36.766 1.00 69.99 ? 310 ARG A CB 1 ATOM 2467 C CG . ARG A 1 310 ? 43.518 -11.061 -38.096 1.00 74.04 ? 310 ARG A CG 1 ATOM 2468 C CD . ARG A 1 310 ? 44.349 -10.181 -39.018 1.00 77.20 ? 310 ARG A CD 1 ATOM 2469 N NE . ARG A 1 310 ? 44.036 -10.436 -40.425 1.00 82.16 ? 310 ARG A NE 1 ATOM 2470 C CZ . ARG A 1 310 ? 42.954 -9.988 -41.062 1.00 84.27 ? 310 ARG A CZ 1 ATOM 2471 N NH1 . ARG A 1 310 ? 42.046 -9.245 -40.436 1.00 85.96 ? 310 ARG A NH1 1 ATOM 2472 N NH2 . ARG A 1 310 ? 42.777 -10.285 -42.343 1.00 85.79 ? 310 ARG A NH2 1 ATOM 2473 N N . LEU A 1 311 ? 42.348 -14.205 -36.620 1.00 58.15 ? 311 LEU A N 1 ATOM 2474 C CA . LEU A 1 311 ? 42.264 -15.508 -37.302 1.00 58.41 ? 311 LEU A CA 1 ATOM 2475 C C . LEU A 1 311 ? 41.233 -15.444 -38.427 1.00 56.03 ? 311 LEU A C 1 ATOM 2476 O O . LEU A 1 311 ? 40.030 -15.449 -38.173 1.00 55.97 ? 311 LEU A O 1 ATOM 2477 C CB . LEU A 1 311 ? 41.907 -16.652 -36.339 1.00 58.05 ? 311 LEU A CB 1 ATOM 2478 C CG . LEU A 1 311 ? 42.897 -17.040 -35.233 1.00 59.93 ? 311 LEU A CG 1 ATOM 2479 C CD1 . LEU A 1 311 ? 42.278 -18.113 -34.356 1.00 60.85 ? 311 LEU A CD1 1 ATOM 2480 C CD2 . LEU A 1 311 ? 44.231 -17.538 -35.767 1.00 60.86 ? 311 LEU A CD2 1 ATOM 2481 N N . VAL A 1 312 ? 41.721 -15.392 -39.666 1.00 54.33 ? 312 VAL A N 1 ATOM 2482 C CA . VAL A 1 312 ? 40.870 -15.265 -40.846 1.00 53.25 ? 312 VAL A CA 1 ATOM 2483 C C . VAL A 1 312 ? 41.250 -16.294 -41.907 1.00 52.63 ? 312 VAL A C 1 ATOM 2484 O O . VAL A 1 312 ? 42.376 -16.283 -42.401 1.00 50.62 ? 312 VAL A O 1 ATOM 2485 C CB . VAL A 1 312 ? 41.010 -13.865 -41.460 1.00 53.43 ? 312 VAL A CB 1 ATOM 2486 C CG1 . VAL A 1 312 ? 40.158 -13.744 -42.718 1.00 53.70 ? 312 VAL A CG1 1 ATOM 2487 C CG2 . VAL A 1 312 ? 40.653 -12.803 -40.424 1.00 53.48 ? 312 VAL A CG2 1 ATOM 2488 N N . LEU A 1 313 ? 40.299 -17.170 -42.240 1.00 52.38 ? 313 LEU A N 1 ATOM 2489 C CA . LEU A 1 313 ? 40.476 -18.215 -43.258 1.00 52.11 ? 313 LEU A CA 1 ATOM 2490 C C . LEU A 1 313 ? 40.061 -17.738 -44.636 1.00 52.51 ? 313 LEU A C 1 ATOM 2491 O O . LEU A 1 313 ? 39.014 -17.110 -44.789 1.00 54.60 ? 313 LEU A O 1 ATOM 2492 C CB . LEU A 1 313 ? 39.610 -19.434 -42.950 1.00 52.07 ? 313 LEU A CB 1 ATOM 2493 C CG . LEU A 1 313 ? 40.054 -20.344 -41.820 1.00 54.10 ? 313 LEU A CG 1 ATOM 2494 C CD1 . LEU A 1 313 ? 38.905 -21.252 -41.414 1.00 55.34 ? 313 LEU A CD1 1 ATOM 2495 C CD2 . LEU A 1 313 ? 41.273 -21.159 -42.239 1.00 55.30 ? 313 LEU A CD2 1 ATOM 2496 N N . ALA A 1 314 ? 40.864 -18.077 -45.641 1.00 51.69 ? 314 ALA A N 1 ATOM 2497 C CA . ALA A 1 314 ? 40.485 -17.864 -47.030 1.00 51.63 ? 314 ALA A CA 1 ATOM 2498 C C . ALA A 1 314 ? 39.423 -18.877 -47.414 1.00 52.00 ? 314 ALA A C 1 ATOM 2499 O O . ALA A 1 314 ? 39.511 -20.057 -47.051 1.00 52.39 ? 314 ALA A O 1 ATOM 2500 C CB . ALA A 1 314 ? 41.693 -18.003 -47.946 1.00 51.98 ? 314 ALA A CB 1 ATOM 2501 N N . THR A 1 315 ? 38.407 -18.402 -48.124 1.00 52.70 ? 315 THR A N 1 ATOM 2502 C CA . THR A 1 315 ? 37.430 -19.273 -48.778 1.00 53.53 ? 315 THR A CA 1 ATOM 2503 C C . THR A 1 315 ? 37.514 -19.076 -50.285 1.00 52.16 ? 315 THR A C 1 ATOM 2504 O O . THR A 1 315 ? 37.593 -20.036 -51.041 1.00 52.43 ? 315 THR A O 1 ATOM 2505 C CB . THR A 1 315 ? 36.004 -18.965 -48.307 1.00 55.04 ? 315 THR A CB 1 ATOM 2506 O OG1 . THR A 1 315 ? 35.822 -17.546 -48.266 1.00 56.22 ? 315 THR A OG1 1 ATOM 2507 C CG2 . THR A 1 315 ? 35.764 -19.545 -46.919 1.00 55.70 ? 315 THR A CG2 1 ATOM 2508 N N . GLY A 1 316 ? 37.518 -17.823 -50.719 1.00 51.24 ? 316 GLY A N 1 ATOM 2509 C CA . GLY A 1 316 ? 37.660 -17.514 -52.127 1.00 51.13 ? 316 GLY A CA 1 ATOM 2510 C C . GLY A 1 316 ? 39.100 -17.563 -52.584 1.00 51.32 ? 316 GLY A C 1 ATOM 2511 O O . GLY A 1 316 ? 39.957 -18.190 -51.947 1.00 49.49 ? 316 GLY A O 1 ATOM 2512 N N . LEU A 1 317 ? 39.374 -16.866 -53.678 1.00 51.35 ? 317 LEU A N 1 ATOM 2513 C CA . LEU A 1 317 ? 40.671 -16.949 -54.314 1.00 53.03 ? 317 LEU A CA 1 ATOM 2514 C C . LEU A 1 317 ? 41.328 -15.568 -54.384 1.00 52.69 ? 317 LEU A C 1 ATOM 2515 O O . LEU A 1 317 ? 40.718 -14.565 -54.025 1.00 51.66 ? 317 LEU A O 1 ATOM 2516 C CB . LEU A 1 317 ? 40.540 -17.617 -55.694 1.00 55.38 ? 317 LEU A CB 1 ATOM 2517 C CG . LEU A 1 317 ? 39.385 -17.154 -56.588 1.00 57.16 ? 317 LEU A CG 1 ATOM 2518 C CD1 . LEU A 1 317 ? 39.676 -15.757 -57.096 1.00 59.01 ? 317 LEU A CD1 1 ATOM 2519 C CD2 . LEU A 1 317 ? 39.165 -18.097 -57.756 1.00 57.74 ? 317 LEU A CD2 1 ATOM 2520 N N . ARG A 1 318 ? 42.583 -15.549 -54.818 1.00 52.22 ? 318 ARG A N 1 ATOM 2521 C CA . ARG A 1 318 ? 43.387 -14.338 -54.886 1.00 54.62 ? 318 ARG A CA 1 ATOM 2522 C C . ARG A 1 318 ? 42.724 -13.298 -55.767 1.00 56.03 ? 318 ARG A C 1 ATOM 2523 O O . ARG A 1 318 ? 42.504 -13.532 -56.951 1.00 56.55 ? 318 ARG A O 1 ATOM 2524 C CB . ARG A 1 318 ? 44.775 -14.684 -55.430 1.00 57.10 ? 318 ARG A CB 1 ATOM 2525 C CG . ARG A 1 318 ? 45.761 -13.533 -55.456 1.00 61.74 ? 318 ARG A CG 1 ATOM 2526 C CD . ARG A 1 318 ? 47.084 -13.973 -56.050 1.00 65.11 ? 318 ARG A CD 1 ATOM 2527 N NE . ARG A 1 318 ? 47.861 -14.767 -55.099 1.00 67.59 ? 318 ARG A NE 1 ATOM 2528 C CZ . ARG A 1 318 ? 48.737 -14.267 -54.229 1.00 70.59 ? 318 ARG A CZ 1 ATOM 2529 N NH1 . ARG A 1 318 ? 48.971 -12.954 -54.164 1.00 71.66 ? 318 ARG A NH1 1 ATOM 2530 N NH2 . ARG A 1 318 ? 49.386 -15.090 -53.410 1.00 72.12 ? 318 ARG A NH2 1 ATOM 2531 N N . ASN A 1 319 ? 42.412 -12.146 -55.185 1.00 59.93 ? 319 ASN A N 1 ATOM 2532 C CA . ASN A 1 319 ? 41.671 -11.101 -55.886 1.00 62.27 ? 319 ASN A CA 1 ATOM 2533 C C . ASN A 1 319 ? 42.600 -10.198 -56.685 1.00 69.12 ? 319 ASN A C 1 ATOM 2534 O O . ASN A 1 319 ? 43.700 -9.880 -56.249 1.00 72.78 ? 319 ASN A O 1 ATOM 2535 C CB . ASN A 1 319 ? 40.847 -10.275 -54.903 1.00 60.76 ? 319 ASN A CB 1 ATOM 2536 C CG . ASN A 1 319 ? 39.732 -9.498 -55.578 1.00 61.00 ? 319 ASN A CG 1 ATOM 2537 O OD1 . ASN A 1 319 ? 39.449 -9.685 -56.756 1.00 59.26 ? 319 ASN A OD1 1 ATOM 2538 N ND2 . ASN A 1 319 ? 39.089 -8.619 -54.822 1.00 61.76 ? 319 ASN A ND2 1 ATOM 2539 N N . SER A 1 320 ? 42.139 -9.792 -57.861 1.00 77.97 ? 320 SER A N 1 ATOM 2540 C CA . SER A 1 320 ? 42.964 -9.065 -58.819 1.00 85.02 ? 320 SER A CA 1 ATOM 2541 C C . SER A 1 320 ? 42.859 -7.551 -58.616 1.00 92.18 ? 320 SER A C 1 ATOM 2542 O O . SER A 1 320 ? 41.776 -7.045 -58.300 1.00 89.80 ? 320 SER A O 1 ATOM 2543 C CB . SER A 1 320 ? 42.525 -9.415 -60.243 1.00 84.11 ? 320 SER A CB 1 ATOM 2544 O OG . SER A 1 320 ? 42.303 -10.806 -60.354 1.00 83.47 ? 320 SER A OG 1 ATOM 2545 N N . PRO A 1 321 ? 43.985 -6.827 -58.784 1.00 100.41 ? 321 PRO A N 1 ATOM 2546 C CA . PRO A 1 321 ? 43.920 -5.365 -58.870 1.00 107.37 ? 321 PRO A CA 1 ATOM 2547 C C . PRO A 1 321 ? 43.352 -4.901 -60.211 1.00 109.13 ? 321 PRO A C 1 ATOM 2548 O O . PRO A 1 321 ? 42.440 -4.075 -60.239 1.00 112.50 ? 321 PRO A O 1 ATOM 2549 C CB . PRO A 1 321 ? 45.388 -4.928 -58.725 1.00 109.51 ? 321 PRO A CB 1 ATOM 2550 C CG . PRO A 1 321 ? 46.097 -6.098 -58.127 1.00 106.33 ? 321 PRO A CG 1 ATOM 2551 C CD . PRO A 1 321 ? 45.373 -7.304 -58.643 1.00 102.37 ? 321 PRO A CD 1 ATOM 2552 N N . GLY B 2 1 ? 51.081 -18.731 -58.112 1.00 53.96 ? 1 GLY B N 1 ATOM 2553 C CA . GLY B 2 1 ? 50.625 -19.979 -57.447 1.00 50.95 ? 1 GLY B CA 1 ATOM 2554 C C . GLY B 2 1 ? 51.292 -21.228 -57.991 1.00 50.27 ? 1 GLY B C 1 ATOM 2555 O O . GLY B 2 1 ? 51.862 -21.232 -59.084 1.00 51.11 ? 1 GLY B O 1 ATOM 2556 N N . LEU B 2 2 ? 51.201 -22.305 -57.224 1.00 48.34 ? 2 LEU B N 1 ATOM 2557 C CA . LEU B 2 2 ? 51.863 -23.539 -57.590 1.00 48.55 ? 2 LEU B CA 1 ATOM 2558 C C . LEU B 2 2 ? 51.454 -24.051 -58.970 1.00 48.19 ? 2 LEU B C 1 ATOM 2559 O O . LEU B 2 2 ? 52.263 -24.673 -59.648 1.00 49.48 ? 2 LEU B O 1 ATOM 2560 C CB . LEU B 2 2 ? 51.576 -24.621 -56.557 1.00 47.27 ? 2 LEU B CB 1 ATOM 2561 C CG . LEU B 2 2 ? 52.286 -24.477 -55.226 1.00 46.97 ? 2 LEU B CG 1 ATOM 2562 C CD1 . LEU B 2 2 ? 51.855 -25.610 -54.311 1.00 45.60 ? 2 LEU B CD1 1 ATOM 2563 C CD2 . LEU B 2 2 ? 53.798 -24.441 -55.404 1.00 48.80 ? 2 LEU B CD2 1 ATOM 2564 N N . PHE B 2 3 ? 50.220 -23.780 -59.385 1.00 45.62 ? 3 PHE B N 1 ATOM 2565 C CA . PHE B 2 3 ? 49.690 -24.378 -60.612 1.00 46.48 ? 3 PHE B CA 1 ATOM 2566 C C . PHE B 2 3 ? 49.777 -23.493 -61.850 1.00 48.24 ? 3 PHE B C 1 ATOM 2567 O O . PHE B 2 3 ? 49.486 -23.946 -62.961 1.00 48.46 ? 3 PHE B O 1 ATOM 2568 C CB . PHE B 2 3 ? 48.276 -24.927 -60.350 1.00 44.54 ? 3 PHE B CB 1 ATOM 2569 C CG . PHE B 2 3 ? 48.295 -26.065 -59.378 1.00 43.82 ? 3 PHE B CG 1 ATOM 2570 C CD1 . PHE B 2 3 ? 48.550 -27.350 -59.814 1.00 43.77 ? 3 PHE B CD1 1 ATOM 2571 C CD2 . PHE B 2 3 ? 48.188 -25.831 -58.011 1.00 43.70 ? 3 PHE B CD2 1 ATOM 2572 C CE1 . PHE B 2 3 ? 48.643 -28.395 -58.910 1.00 44.79 ? 3 PHE B CE1 1 ATOM 2573 C CE2 . PHE B 2 3 ? 48.293 -26.874 -57.099 1.00 43.24 ? 3 PHE B CE2 1 ATOM 2574 C CZ . PHE B 2 3 ? 48.517 -28.154 -57.547 1.00 43.59 ? 3 PHE B CZ 1 ATOM 2575 N N . GLY B 2 4 ? 50.209 -22.246 -61.654 1.00 49.85 ? 4 GLY B N 1 ATOM 2576 C CA . GLY B 2 4 ? 50.552 -21.353 -62.752 1.00 50.79 ? 4 GLY B CA 1 ATOM 2577 C C . GLY B 2 4 ? 49.409 -20.640 -63.451 1.00 50.59 ? 4 GLY B C 1 ATOM 2578 O O . GLY B 2 4 ? 49.656 -19.824 -64.331 1.00 55.10 ? 4 GLY B O 1 ATOM 2579 N N . ALA B 2 5 ? 48.162 -20.923 -63.094 1.00 48.53 ? 5 ALA B N 1 ATOM 2580 C CA . ALA B 2 5 ? 47.036 -20.303 -63.794 1.00 47.44 ? 5 ALA B CA 1 ATOM 2581 C C . ALA B 2 5 ? 46.688 -18.931 -63.218 1.00 47.91 ? 5 ALA B C 1 ATOM 2582 O O . ALA B 2 5 ? 46.868 -17.912 -63.885 1.00 48.24 ? 5 ALA B O 1 ATOM 2583 C CB . ALA B 2 5 ? 45.821 -21.220 -63.774 1.00 46.37 ? 5 ALA B CB 1 ATOM 2584 N N . ILE B 2 6 ? 46.204 -18.913 -61.975 1.00 47.57 ? 6 ILE B N 1 ATOM 2585 C CA . ILE B 2 6 ? 45.740 -17.679 -61.339 1.00 48.34 ? 6 ILE B CA 1 ATOM 2586 C C . ILE B 2 6 ? 46.906 -16.711 -61.160 1.00 50.30 ? 6 ILE B C 1 ATOM 2587 O O . ILE B 2 6 ? 47.932 -17.065 -60.586 1.00 49.42 ? 6 ILE B O 1 ATOM 2588 C CB . ILE B 2 6 ? 45.076 -17.964 -59.980 1.00 47.83 ? 6 ILE B CB 1 ATOM 2589 C CG1 . ILE B 2 6 ? 43.752 -18.690 -60.205 1.00 47.28 ? 6 ILE B CG1 1 ATOM 2590 C CG2 . ILE B 2 6 ? 44.845 -16.673 -59.203 1.00 48.81 ? 6 ILE B CG2 1 ATOM 2591 C CD1 . ILE B 2 6 ? 43.039 -19.097 -58.936 1.00 47.04 ? 6 ILE B CD1 1 ATOM 2592 N N . ALA B 2 7 ? 46.741 -15.496 -61.673 1.00 52.47 ? 7 ALA B N 1 ATOM 2593 C CA . ALA B 2 7 ? 47.815 -14.511 -61.699 1.00 55.86 ? 7 ALA B CA 1 ATOM 2594 C C . ALA B 2 7 ? 49.104 -15.129 -62.238 1.00 57.76 ? 7 ALA B C 1 ATOM 2595 O O . ALA B 2 7 ? 50.189 -14.866 -61.729 1.00 59.75 ? 7 ALA B O 1 ATOM 2596 C CB . ALA B 2 7 ? 48.032 -13.929 -60.306 1.00 56.45 ? 7 ALA B CB 1 ATOM 2597 N N . GLY B 2 8 ? 48.963 -15.974 -63.254 1.00 58.47 ? 8 GLY B N 1 ATOM 2598 C CA . GLY B 2 8 ? 50.097 -16.571 -63.960 1.00 58.93 ? 8 GLY B CA 1 ATOM 2599 C C . GLY B 2 8 ? 49.870 -16.360 -65.449 1.00 60.15 ? 8 GLY B C 1 ATOM 2600 O O . GLY B 2 8 ? 49.963 -15.235 -65.925 1.00 61.72 ? 8 GLY B O 1 ATOM 2601 N N . PHE B 2 9 ? 49.543 -17.422 -66.185 1.00 57.97 ? 9 PHE B N 1 ATOM 2602 C CA . PHE B 2 9 ? 49.277 -17.270 -67.609 1.00 58.63 ? 9 PHE B CA 1 ATOM 2603 C C . PHE B 2 9 ? 47.895 -16.642 -67.839 1.00 58.41 ? 9 PHE B C 1 ATOM 2604 O O . PHE B 2 9 ? 47.636 -16.082 -68.903 1.00 60.06 ? 9 PHE B O 1 ATOM 2605 C CB . PHE B 2 9 ? 49.507 -18.574 -68.395 1.00 58.58 ? 9 PHE B CB 1 ATOM 2606 C CG . PHE B 2 9 ? 48.496 -19.655 -68.138 1.00 56.78 ? 9 PHE B CG 1 ATOM 2607 C CD1 . PHE B 2 9 ? 47.286 -19.670 -68.816 1.00 57.26 ? 9 PHE B CD1 1 ATOM 2608 C CD2 . PHE B 2 9 ? 48.773 -20.681 -67.259 1.00 55.21 ? 9 PHE B CD2 1 ATOM 2609 C CE1 . PHE B 2 9 ? 46.351 -20.670 -68.590 1.00 55.84 ? 9 PHE B CE1 1 ATOM 2610 C CE2 . PHE B 2 9 ? 47.852 -21.688 -67.035 1.00 54.68 ? 9 PHE B CE2 1 ATOM 2611 C CZ . PHE B 2 9 ? 46.638 -21.682 -67.696 1.00 54.52 ? 9 PHE B CZ 1 ATOM 2612 N N . ILE B 2 10 ? 47.021 -16.719 -66.836 1.00 57.19 ? 10 ILE B N 1 ATOM 2613 C CA . ILE B 2 10 ? 45.804 -15.913 -66.815 1.00 57.78 ? 10 ILE B CA 1 ATOM 2614 C C . ILE B 2 10 ? 46.092 -14.732 -65.899 1.00 60.86 ? 10 ILE B C 1 ATOM 2615 O O . ILE B 2 10 ? 46.129 -14.875 -64.680 1.00 61.96 ? 10 ILE B O 1 ATOM 2616 C CB . ILE B 2 10 ? 44.587 -16.709 -66.327 1.00 55.76 ? 10 ILE B CB 1 ATOM 2617 C CG1 . ILE B 2 10 ? 44.459 -18.005 -67.119 1.00 55.50 ? 10 ILE B CG1 1 ATOM 2618 C CG2 . ILE B 2 10 ? 43.316 -15.890 -66.490 1.00 56.06 ? 10 ILE B CG2 1 ATOM 2619 C CD1 . ILE B 2 10 ? 43.366 -18.917 -66.615 1.00 54.77 ? 10 ILE B CD1 1 ATOM 2620 N N . GLU B 2 11 ? 46.324 -13.571 -66.503 1.00 65.40 ? 11 GLU B N 1 ATOM 2621 C CA . GLU B 2 11 ? 46.862 -12.411 -65.791 1.00 69.03 ? 11 GLU B CA 1 ATOM 2622 C C . GLU B 2 11 ? 46.008 -11.936 -64.623 1.00 66.92 ? 11 GLU B C 1 ATOM 2623 O O . GLU B 2 11 ? 46.540 -11.550 -63.576 1.00 67.69 ? 11 GLU B O 1 ATOM 2624 C CB . GLU B 2 11 ? 47.070 -11.240 -66.752 1.00 75.77 ? 11 GLU B CB 1 ATOM 2625 C CG . GLU B 2 11 ? 48.513 -11.015 -67.174 1.00 81.61 ? 11 GLU B CG 1 ATOM 2626 C CD . GLU B 2 11 ? 48.781 -9.555 -67.506 1.00 89.43 ? 11 GLU B CD 1 ATOM 2627 O OE1 . GLU B 2 11 ? 47.896 -8.906 -68.121 1.00 91.22 ? 11 GLU B OE1 1 ATOM 2628 O OE2 . GLU B 2 11 ? 49.871 -9.054 -67.140 1.00 95.09 ? 11 GLU B OE2 1 ATOM 2629 N N . GLY B 2 12 ? 44.693 -11.944 -64.808 1.00 64.21 ? 12 GLY B N 1 ATOM 2630 C CA . GLY B 2 12 ? 43.778 -11.463 -63.778 1.00 63.46 ? 12 GLY B CA 1 ATOM 2631 C C . GLY B 2 12 ? 42.391 -12.052 -63.868 1.00 61.18 ? 12 GLY B C 1 ATOM 2632 O O . GLY B 2 12 ? 42.025 -12.669 -64.868 1.00 61.43 ? 12 GLY B O 1 ATOM 2633 N N . GLY B 2 13 ? 41.622 -11.860 -62.805 1.00 60.21 ? 13 GLY B N 1 ATOM 2634 C CA . GLY B 2 13 ? 40.250 -12.332 -62.743 1.00 59.57 ? 13 GLY B CA 1 ATOM 2635 C C . GLY B 2 13 ? 39.278 -11.429 -63.489 1.00 60.89 ? 13 GLY B C 1 ATOM 2636 O O . GLY B 2 13 ? 39.681 -10.442 -64.107 1.00 62.56 ? 13 GLY B O 1 ATOM 2637 N N . TRP B 2 14 ? 37.997 -11.787 -63.418 1.00 59.68 ? 14 TRP B N 1 ATOM 2638 C CA . TRP B 2 14 ? 36.932 -11.119 -64.144 1.00 60.57 ? 14 TRP B CA 1 ATOM 2639 C C . TRP B 2 14 ? 35.868 -10.579 -63.194 1.00 64.15 ? 14 TRP B C 1 ATOM 2640 O O . TRP B 2 14 ? 35.146 -11.341 -62.557 1.00 62.98 ? 14 TRP B O 1 ATOM 2641 C CB . TRP B 2 14 ? 36.260 -12.099 -65.112 1.00 58.28 ? 14 TRP B CB 1 ATOM 2642 C CG . TRP B 2 14 ? 37.106 -12.536 -66.269 1.00 55.87 ? 14 TRP B CG 1 ATOM 2643 C CD1 . TRP B 2 14 ? 38.099 -11.828 -66.873 1.00 56.05 ? 14 TRP B CD1 1 ATOM 2644 C CD2 . TRP B 2 14 ? 36.994 -13.769 -66.998 1.00 53.53 ? 14 TRP B CD2 1 ATOM 2645 N NE1 . TRP B 2 14 ? 38.622 -12.546 -67.922 1.00 54.30 ? 14 TRP B NE1 1 ATOM 2646 C CE2 . TRP B 2 14 ? 37.960 -13.737 -68.023 1.00 52.97 ? 14 TRP B CE2 1 ATOM 2647 C CE3 . TRP B 2 14 ? 36.166 -14.890 -66.888 1.00 52.41 ? 14 TRP B CE3 1 ATOM 2648 C CZ2 . TRP B 2 14 ? 38.134 -14.789 -68.922 1.00 52.50 ? 14 TRP B CZ2 1 ATOM 2649 C CZ3 . TRP B 2 14 ? 36.332 -15.932 -67.786 1.00 51.47 ? 14 TRP B CZ3 1 ATOM 2650 C CH2 . TRP B 2 14 ? 37.312 -15.877 -68.789 1.00 51.58 ? 14 TRP B CH2 1 ATOM 2651 N N . GLN B 2 15 ? 35.765 -9.256 -63.118 1.00 69.85 ? 15 GLN B N 1 ATOM 2652 C CA . GLN B 2 15 ? 34.655 -8.599 -62.426 1.00 74.00 ? 15 GLN B CA 1 ATOM 2653 C C . GLN B 2 15 ? 33.318 -9.021 -63.034 1.00 73.69 ? 15 GLN B C 1 ATOM 2654 O O . GLN B 2 15 ? 32.318 -9.117 -62.331 1.00 75.25 ? 15 GLN B O 1 ATOM 2655 C CB . GLN B 2 15 ? 34.789 -7.073 -62.515 1.00 78.40 ? 15 GLN B CB 1 ATOM 2656 C CG . GLN B 2 15 ? 35.993 -6.484 -61.787 1.00 80.75 ? 15 GLN B CG 1 ATOM 2657 C CD . GLN B 2 15 ? 35.784 -6.337 -60.288 1.00 83.01 ? 15 GLN B CD 1 ATOM 2658 O OE1 . GLN B 2 15 ? 36.645 -6.711 -59.497 1.00 83.65 ? 15 GLN B OE1 1 ATOM 2659 N NE2 . GLN B 2 15 ? 34.641 -5.784 -59.893 1.00 86.77 ? 15 GLN B NE2 1 ATOM 2660 N N . GLY B 2 16 ? 33.313 -9.268 -64.342 1.00 73.61 ? 16 GLY B N 1 ATOM 2661 C CA . GLY B 2 16 ? 32.090 -9.583 -65.082 1.00 74.55 ? 16 GLY B CA 1 ATOM 2662 C C . GLY B 2 16 ? 31.503 -10.980 -64.913 1.00 73.67 ? 16 GLY B C 1 ATOM 2663 O O . GLY B 2 16 ? 30.369 -11.217 -65.336 1.00 76.05 ? 16 GLY B O 1 ATOM 2664 N N . MET B 2 17 ? 32.257 -11.910 -64.326 1.00 70.26 ? 17 MET B N 1 ATOM 2665 C CA . MET B 2 17 ? 31.727 -13.245 -64.029 1.00 69.84 ? 17 MET B CA 1 ATOM 2666 C C . MET B 2 17 ? 31.273 -13.324 -62.574 1.00 70.24 ? 17 MET B C 1 ATOM 2667 O O . MET B 2 17 ? 32.074 -13.525 -61.658 1.00 68.27 ? 17 MET B O 1 ATOM 2668 C CB . MET B 2 17 ? 32.757 -14.333 -64.311 1.00 69.53 ? 17 MET B CB 1 ATOM 2669 C CG . MET B 2 17 ? 32.201 -15.731 -64.103 1.00 69.84 ? 17 MET B CG 1 ATOM 2670 S SD . MET B 2 17 ? 33.281 -16.974 -64.802 1.00 68.43 ? 17 MET B SD 1 ATOM 2671 C CE . MET B 2 17 ? 34.707 -16.733 -63.748 1.00 69.36 ? 17 MET B CE 1 ATOM 2672 N N . VAL B 2 18 ? 29.967 -13.196 -62.390 1.00 72.83 ? 18 VAL B N 1 ATOM 2673 C CA . VAL B 2 18 ? 29.355 -12.971 -61.085 1.00 75.11 ? 18 VAL B CA 1 ATOM 2674 C C . VAL B 2 18 ? 28.795 -14.257 -60.473 1.00 74.49 ? 18 VAL B C 1 ATOM 2675 O O . VAL B 2 18 ? 28.647 -14.355 -59.261 1.00 73.89 ? 18 VAL B O 1 ATOM 2676 C CB . VAL B 2 18 ? 28.231 -11.918 -61.242 1.00 79.75 ? 18 VAL B CB 1 ATOM 2677 C CG1 . VAL B 2 18 ? 27.213 -11.984 -60.117 1.00 83.41 ? 18 VAL B CG1 1 ATOM 2678 C CG2 . VAL B 2 18 ? 28.834 -10.523 -61.347 1.00 81.06 ? 18 VAL B CG2 1 ATOM 2679 N N . ASP B 2 19 ? 28.501 -15.245 -61.312 1.00 75.11 ? 19 ASP B N 1 ATOM 2680 C CA . ASP B 2 19 ? 27.689 -16.399 -60.907 1.00 76.10 ? 19 ASP B CA 1 ATOM 2681 C C . ASP B 2 19 ? 28.503 -17.671 -60.632 1.00 71.69 ? 19 ASP B C 1 ATOM 2682 O O . ASP B 2 19 ? 27.943 -18.754 -60.504 1.00 74.27 ? 19 ASP B O 1 ATOM 2683 C CB . ASP B 2 19 ? 26.595 -16.665 -61.965 1.00 78.76 ? 19 ASP B CB 1 ATOM 2684 C CG . ASP B 2 19 ? 27.143 -16.741 -63.393 1.00 80.01 ? 19 ASP B CG 1 ATOM 2685 O OD1 . ASP B 2 19 ? 28.378 -16.604 -63.598 1.00 76.62 ? 19 ASP B OD1 1 ATOM 2686 O OD2 . ASP B 2 19 ? 26.324 -16.935 -64.321 1.00 83.73 ? 19 ASP B OD2 1 ATOM 2687 N N . GLY B 2 20 ? 29.819 -17.549 -60.531 1.00 66.59 ? 20 GLY B N 1 ATOM 2688 C CA . GLY B 2 20 ? 30.648 -18.703 -60.224 1.00 63.93 ? 20 GLY B CA 1 ATOM 2689 C C . GLY B 2 20 ? 32.087 -18.314 -59.984 1.00 61.91 ? 20 GLY B C 1 ATOM 2690 O O . GLY B 2 20 ? 32.470 -17.166 -60.203 1.00 63.50 ? 20 GLY B O 1 ATOM 2691 N N . TRP B 2 21 ? 32.892 -19.274 -59.542 1.00 59.73 ? 21 TRP B N 1 ATOM 2692 C CA . TRP B 2 21 ? 34.290 -19.000 -59.225 1.00 57.51 ? 21 TRP B CA 1 ATOM 2693 C C . TRP B 2 21 ? 35.180 -19.128 -60.449 1.00 54.16 ? 21 TRP B C 1 ATOM 2694 O O . TRP B 2 21 ? 36.157 -18.390 -60.586 1.00 51.60 ? 21 TRP B O 1 ATOM 2695 C CB . TRP B 2 21 ? 34.792 -19.918 -58.105 1.00 58.67 ? 21 TRP B CB 1 ATOM 2696 C CG . TRP B 2 21 ? 34.723 -19.313 -56.717 1.00 61.68 ? 21 TRP B CG 1 ATOM 2697 C CD1 . TRP B 2 21 ? 34.822 -17.989 -56.377 1.00 63.45 ? 21 TRP B CD1 1 ATOM 2698 C CD2 . TRP B 2 21 ? 34.584 -20.025 -55.493 1.00 64.07 ? 21 TRP B CD2 1 ATOM 2699 N NE1 . TRP B 2 21 ? 34.736 -17.837 -55.017 1.00 64.62 ? 21 TRP B NE1 1 ATOM 2700 C CE2 . TRP B 2 21 ? 34.589 -19.074 -54.450 1.00 65.34 ? 21 TRP B CE2 1 ATOM 2701 C CE3 . TRP B 2 21 ? 34.469 -21.379 -55.173 1.00 67.44 ? 21 TRP B CE3 1 ATOM 2702 C CZ2 . TRP B 2 21 ? 34.470 -19.434 -53.112 1.00 68.56 ? 21 TRP B CZ2 1 ATOM 2703 C CZ3 . TRP B 2 21 ? 34.357 -21.742 -53.835 1.00 69.91 ? 21 TRP B CZ3 1 ATOM 2704 C CH2 . TRP B 2 21 ? 34.356 -20.771 -52.821 1.00 69.99 ? 21 TRP B CH2 1 ATOM 2705 N N . TYR B 2 22 ? 34.841 -20.077 -61.320 1.00 52.35 ? 22 TYR B N 1 ATOM 2706 C CA . TYR B 2 22 ? 35.567 -20.299 -62.561 1.00 50.78 ? 22 TYR B CA 1 ATOM 2707 C C . TYR B 2 22 ? 34.591 -20.432 -63.713 1.00 51.13 ? 22 TYR B C 1 ATOM 2708 O O . TYR B 2 22 ? 33.442 -20.843 -63.521 1.00 52.19 ? 22 TYR B O 1 ATOM 2709 C CB . TYR B 2 22 ? 36.391 -21.586 -62.483 1.00 49.46 ? 22 TYR B CB 1 ATOM 2710 C CG . TYR B 2 22 ? 36.827 -21.980 -61.092 1.00 48.46 ? 22 TYR B CG 1 ATOM 2711 C CD1 . TYR B 2 22 ? 37.783 -21.243 -60.409 1.00 47.76 ? 22 TYR B CD1 1 ATOM 2712 C CD2 . TYR B 2 22 ? 36.302 -23.111 -60.471 1.00 48.85 ? 22 TYR B CD2 1 ATOM 2713 C CE1 . TYR B 2 22 ? 38.193 -21.608 -59.138 1.00 47.49 ? 22 TYR B CE1 1 ATOM 2714 C CE2 . TYR B 2 22 ? 36.710 -23.488 -59.201 1.00 48.20 ? 22 TYR B CE2 1 ATOM 2715 C CZ . TYR B 2 22 ? 37.653 -22.735 -58.540 1.00 47.91 ? 22 TYR B CZ 1 ATOM 2716 O OH . TYR B 2 22 ? 38.069 -23.098 -57.279 1.00 47.48 ? 22 TYR B OH 1 ATOM 2717 N N . GLY B 2 23 ? 35.050 -20.119 -64.920 1.00 50.21 ? 23 GLY B N 1 ATOM 2718 C CA . GLY B 2 23 ? 34.177 -20.235 -66.077 1.00 51.61 ? 23 GLY B CA 1 ATOM 2719 C C . GLY B 2 23 ? 34.789 -19.759 -67.366 1.00 52.18 ? 23 GLY B C 1 ATOM 2720 O O . GLY B 2 23 ? 36.018 -19.681 -67.493 1.00 51.50 ? 23 GLY B O 1 ATOM 2721 N N . TYR B 2 24 ? 33.912 -19.427 -68.312 1.00 54.53 ? 24 TYR B N 1 ATOM 2722 C CA . TYR B 2 24 ? 34.282 -19.177 -69.704 1.00 55.05 ? 24 TYR B CA 1 ATOM 2723 C C . TYR B 2 24 ? 33.872 -17.794 -70.148 1.00 55.00 ? 24 TYR B C 1 ATOM 2724 O O . TYR B 2 24 ? 32.862 -17.274 -69.696 1.00 56.08 ? 24 TYR B O 1 ATOM 2725 C CB . TYR B 2 24 ? 33.574 -20.168 -70.627 1.00 57.11 ? 24 TYR B CB 1 ATOM 2726 C CG . TYR B 2 24 ? 33.660 -21.602 -70.181 1.00 58.59 ? 24 TYR B CG 1 ATOM 2727 C CD1 . TYR B 2 24 ? 32.714 -22.135 -69.322 1.00 59.40 ? 24 TYR B CD1 1 ATOM 2728 C CD2 . TYR B 2 24 ? 34.691 -22.429 -70.624 1.00 60.16 ? 24 TYR B CD2 1 ATOM 2729 C CE1 . TYR B 2 24 ? 32.781 -23.449 -68.910 1.00 61.11 ? 24 TYR B CE1 1 ATOM 2730 C CE2 . TYR B 2 24 ? 34.770 -23.750 -70.215 1.00 60.92 ? 24 TYR B CE2 1 ATOM 2731 C CZ . TYR B 2 24 ? 33.812 -24.251 -69.355 1.00 62.07 ? 24 TYR B CZ 1 ATOM 2732 O OH . TYR B 2 24 ? 33.875 -25.556 -68.934 1.00 65.14 ? 24 TYR B OH 1 ATOM 2733 N N . HIS B 2 25 ? 34.654 -17.212 -71.050 1.00 55.29 ? 25 HIS B N 1 ATOM 2734 C CA . HIS B 2 25 ? 34.246 -16.006 -71.757 1.00 57.67 ? 25 HIS B CA 1 ATOM 2735 C C . HIS B 2 25 ? 34.351 -16.274 -73.239 1.00 58.37 ? 25 HIS B C 1 ATOM 2736 O O . HIS B 2 25 ? 35.401 -16.679 -73.713 1.00 58.19 ? 25 HIS B O 1 ATOM 2737 C CB . HIS B 2 25 ? 35.125 -14.812 -71.412 1.00 57.65 ? 25 HIS B CB 1 ATOM 2738 C CG . HIS B 2 25 ? 34.672 -13.541 -72.056 1.00 59.98 ? 25 HIS B CG 1 ATOM 2739 N ND1 . HIS B 2 25 ? 35.274 -13.018 -73.180 1.00 60.70 ? 25 HIS B ND1 1 ATOM 2740 C CD2 . HIS B 2 25 ? 33.654 -12.701 -71.749 1.00 61.77 ? 25 HIS B CD2 1 ATOM 2741 C CE1 . HIS B 2 25 ? 34.661 -11.900 -73.524 1.00 62.28 ? 25 HIS B CE1 1 ATOM 2742 N NE2 . HIS B 2 25 ? 33.672 -11.688 -72.674 1.00 63.19 ? 25 HIS B NE2 1 ATOM 2743 N N . HIS B 2 26 ? 33.264 -16.043 -73.967 1.00 60.63 ? 26 HIS B N 1 ATOM 2744 C CA . HIS B 2 26 ? 33.231 -16.324 -75.402 1.00 61.45 ? 26 HIS B CA 1 ATOM 2745 C C . HIS B 2 26 ? 33.099 -15.025 -76.185 1.00 63.03 ? 26 HIS B C 1 ATOM 2746 O O . HIS B 2 26 ? 32.600 -14.032 -75.673 1.00 63.15 ? 26 HIS B O 1 ATOM 2747 C CB . HIS B 2 26 ? 32.084 -17.281 -75.733 1.00 61.51 ? 26 HIS B CB 1 ATOM 2748 C CG . HIS B 2 26 ? 30.749 -16.620 -75.801 1.00 63.90 ? 26 HIS B CG 1 ATOM 2749 N ND1 . HIS B 2 26 ? 29.971 -16.400 -74.687 1.00 65.80 ? 26 HIS B ND1 1 ATOM 2750 C CD2 . HIS B 2 26 ? 30.053 -16.125 -76.850 1.00 65.52 ? 26 HIS B CD2 1 ATOM 2751 C CE1 . HIS B 2 26 ? 28.852 -15.796 -75.044 1.00 67.25 ? 26 HIS B CE1 1 ATOM 2752 N NE2 . HIS B 2 26 ? 28.875 -15.625 -76.353 1.00 68.31 ? 26 HIS B NE2 1 ATOM 2753 N N . SER B 2 27 ? 33.548 -15.048 -77.432 1.00 64.67 ? 27 SER B N 1 ATOM 2754 C CA . SER B 2 27 ? 33.548 -13.858 -78.274 1.00 66.74 ? 27 SER B CA 1 ATOM 2755 C C . SER B 2 27 ? 33.474 -14.236 -79.762 1.00 66.94 ? 27 SER B C 1 ATOM 2756 O O . SER B 2 27 ? 34.408 -14.816 -80.306 1.00 65.58 ? 27 SER B O 1 ATOM 2757 C CB . SER B 2 27 ? 34.809 -13.049 -77.984 1.00 66.90 ? 27 SER B CB 1 ATOM 2758 O OG . SER B 2 27 ? 34.852 -11.887 -78.772 1.00 70.96 ? 27 SER B OG 1 ATOM 2759 N N . ASN B 2 28 ? 32.355 -13.906 -80.403 1.00 68.93 ? 28 ASN B N 1 ATOM 2760 C CA . ASN B 2 28 ? 32.125 -14.225 -81.817 1.00 69.17 ? 28 ASN B CA 1 ATOM 2761 C C . ASN B 2 28 ? 31.283 -13.124 -82.483 1.00 73.13 ? 28 ASN B C 1 ATOM 2762 O O . ASN B 2 28 ? 31.127 -12.044 -81.913 1.00 73.98 ? 28 ASN B O 1 ATOM 2763 C CB . ASN B 2 28 ? 31.470 -15.612 -81.934 1.00 67.32 ? 28 ASN B CB 1 ATOM 2764 C CG . ASN B 2 28 ? 30.127 -15.692 -81.230 1.00 66.68 ? 28 ASN B CG 1 ATOM 2765 O OD1 . ASN B 2 28 ? 29.458 -14.678 -81.030 1.00 68.99 ? 28 ASN B OD1 1 ATOM 2766 N ND2 . ASN B 2 28 ? 29.723 -16.902 -80.854 1.00 64.61 ? 28 ASN B ND2 1 ATOM 2767 N N . GLU B 2 29 ? 30.749 -13.385 -83.677 1.00 76.62 ? 29 GLU B N 1 ATOM 2768 C CA . GLU B 2 29 ? 29.983 -12.371 -84.408 1.00 81.39 ? 29 GLU B CA 1 ATOM 2769 C C . GLU B 2 29 ? 28.627 -12.057 -83.780 1.00 83.47 ? 29 GLU B C 1 ATOM 2770 O O . GLU B 2 29 ? 28.099 -10.964 -83.965 1.00 84.90 ? 29 GLU B O 1 ATOM 2771 C CB . GLU B 2 29 ? 29.769 -12.797 -85.859 1.00 84.97 ? 29 GLU B CB 1 ATOM 2772 C CG . GLU B 2 29 ? 31.059 -12.904 -86.659 1.00 86.43 ? 29 GLU B CG 1 ATOM 2773 C CD . GLU B 2 29 ? 30.826 -13.078 -88.155 1.00 89.41 ? 29 GLU B CD 1 ATOM 2774 O OE1 . GLU B 2 29 ? 29.871 -12.491 -88.722 1.00 91.96 ? 29 GLU B OE1 1 ATOM 2775 O OE2 . GLU B 2 29 ? 31.623 -13.804 -88.770 1.00 90.35 ? 29 GLU B OE2 1 ATOM 2776 N N . GLN B 2 30 ? 28.063 -13.019 -83.056 1.00 84.36 ? 30 GLN B N 1 ATOM 2777 C CA . GLN B 2 30 ? 26.771 -12.832 -82.387 1.00 86.18 ? 30 GLN B CA 1 ATOM 2778 C C . GLN B 2 30 ? 26.894 -12.001 -81.112 1.00 83.21 ? 30 GLN B C 1 ATOM 2779 O O . GLN B 2 30 ? 25.908 -11.448 -80.632 1.00 83.54 ? 30 GLN B O 1 ATOM 2780 C CB . GLN B 2 30 ? 26.146 -14.187 -82.050 1.00 88.74 ? 30 GLN B CB 1 ATOM 2781 C CG . GLN B 2 30 ? 25.640 -14.957 -83.262 1.00 92.50 ? 30 GLN B CG 1 ATOM 2782 C CD . GLN B 2 30 ? 25.922 -16.447 -83.152 1.00 94.62 ? 30 GLN B CD 1 ATOM 2783 O OE1 . GLN B 2 30 ? 27.072 -16.885 -83.271 1.00 95.65 ? 30 GLN B OE1 1 ATOM 2784 N NE2 . GLN B 2 30 ? 24.875 -17.234 -82.928 1.00 96.92 ? 30 GLN B NE2 1 ATOM 2785 N N . GLY B 2 31 ? 28.101 -11.923 -80.561 1.00 79.57 ? 31 GLY B N 1 ATOM 2786 C CA . GLY B 2 31 ? 28.337 -11.178 -79.324 1.00 78.24 ? 31 GLY B CA 1 ATOM 2787 C C . GLY B 2 31 ? 29.324 -11.865 -78.406 1.00 73.87 ? 31 GLY B C 1 ATOM 2788 O O . GLY B 2 31 ? 30.106 -12.712 -78.836 1.00 71.83 ? 31 GLY B O 1 ATOM 2789 N N . SER B 2 32 ? 29.283 -11.501 -77.131 1.00 72.41 ? 32 SER B N 1 ATOM 2790 C CA . SER B 2 32 ? 30.239 -12.024 -76.167 1.00 68.58 ? 32 SER B CA 1 ATOM 2791 C C . SER B 2 32 ? 29.660 -12.063 -74.775 1.00 68.28 ? 32 SER B C 1 ATOM 2792 O O . SER B 2 32 ? 28.661 -11.407 -74.494 1.00 70.38 ? 32 SER B O 1 ATOM 2793 C CB . SER B 2 32 ? 31.491 -11.154 -76.161 1.00 68.16 ? 32 SER B CB 1 ATOM 2794 O OG . SER B 2 32 ? 31.185 -9.834 -75.767 1.00 69.50 ? 32 SER B OG 1 ATOM 2795 N N . GLY B 2 33 ? 30.296 -12.830 -73.897 1.00 66.45 ? 33 GLY B N 1 ATOM 2796 C CA . GLY B 2 33 ? 29.847 -12.897 -72.516 1.00 67.01 ? 33 GLY B CA 1 ATOM 2797 C C . GLY B 2 33 ? 30.492 -13.953 -71.651 1.00 63.93 ? 33 GLY B C 1 ATOM 2798 O O . GLY B 2 33 ? 31.316 -14.731 -72.111 1.00 63.20 ? 33 GLY B O 1 ATOM 2799 N N . TYR B 2 34 ? 30.088 -13.962 -70.385 1.00 64.42 ? 34 TYR B N 1 ATOM 2800 C CA . TYR B 2 34 ? 30.649 -14.839 -69.372 1.00 62.79 ? 34 TYR B CA 1 ATOM 2801 C C . TYR B 2 34 ? 29.680 -15.960 -69.046 1.00 62.79 ? 34 TYR B C 1 ATOM 2802 O O . TYR B 2 34 ? 28.480 -15.762 -69.037 1.00 64.30 ? 34 TYR B O 1 ATOM 2803 C CB . TYR B 2 34 ? 30.936 -14.049 -68.095 1.00 63.11 ? 34 TYR B CB 1 ATOM 2804 C CG . TYR B 2 34 ? 31.896 -12.891 -68.271 1.00 63.95 ? 34 TYR B CG 1 ATOM 2805 C CD1 . TYR B 2 34 ? 33.271 -13.076 -68.187 1.00 62.18 ? 34 TYR B CD1 1 ATOM 2806 C CD2 . TYR B 2 34 ? 31.424 -11.603 -68.511 1.00 67.73 ? 34 TYR B CD2 1 ATOM 2807 C CE1 . TYR B 2 34 ? 34.147 -12.011 -68.343 1.00 63.55 ? 34 TYR B CE1 1 ATOM 2808 C CE2 . TYR B 2 34 ? 32.292 -10.534 -68.669 1.00 68.15 ? 34 TYR B CE2 1 ATOM 2809 C CZ . TYR B 2 34 ? 33.647 -10.744 -68.583 1.00 67.26 ? 34 TYR B CZ 1 ATOM 2810 O OH . TYR B 2 34 ? 34.499 -9.680 -68.733 1.00 70.18 ? 34 TYR B OH 1 ATOM 2811 N N . ALA B 2 35 ? 30.214 -17.139 -68.764 1.00 62.19 ? 35 ALA B N 1 ATOM 2812 C CA . ALA B 2 35 ? 29.405 -18.249 -68.275 1.00 63.32 ? 35 ALA B CA 1 ATOM 2813 C C . ALA B 2 35 ? 30.208 -19.071 -67.259 1.00 62.28 ? 35 ALA B C 1 ATOM 2814 O O . ALA B 2 35 ? 31.299 -19.557 -67.558 1.00 61.63 ? 35 ALA B O 1 ATOM 2815 C CB . ALA B 2 35 ? 28.957 -19.120 -69.428 1.00 63.52 ? 35 ALA B CB 1 ATOM 2816 N N . ALA B 2 36 ? 29.653 -19.217 -66.064 1.00 62.82 ? 36 ALA B N 1 ATOM 2817 C CA . ALA B 2 36 ? 30.278 -19.982 -65.002 1.00 63.10 ? 36 ALA B CA 1 ATOM 2818 C C . ALA B 2 36 ? 30.217 -21.483 -65.286 1.00 64.51 ? 36 ALA B C 1 ATOM 2819 O O . ALA B 2 36 ? 29.205 -21.986 -65.763 1.00 67.46 ? 36 ALA B O 1 ATOM 2820 C CB . ALA B 2 36 ? 29.595 -19.676 -63.680 1.00 64.48 ? 36 ALA B CB 1 ATOM 2821 N N . ASP B 2 37 ? 31.310 -22.187 -64.997 1.00 64.11 ? 37 ASP B N 1 ATOM 2822 C CA . ASP B 2 37 ? 31.330 -23.644 -65.026 1.00 65.16 ? 37 ASP B CA 1 ATOM 2823 C C . ASP B 2 37 ? 30.765 -24.152 -63.693 1.00 68.47 ? 37 ASP B C 1 ATOM 2824 O O . ASP B 2 37 ? 31.380 -23.979 -62.636 1.00 65.29 ? 37 ASP B O 1 ATOM 2825 C CB . ASP B 2 37 ? 32.758 -24.145 -65.231 1.00 64.62 ? 37 ASP B CB 1 ATOM 2826 C CG . ASP B 2 37 ? 32.829 -25.642 -65.449 1.00 65.68 ? 37 ASP B CG 1 ATOM 2827 O OD1 . ASP B 2 37 ? 32.585 -26.088 -66.591 1.00 67.61 ? 37 ASP B OD1 1 ATOM 2828 O OD2 . ASP B 2 37 ? 33.139 -26.369 -64.482 1.00 65.44 ? 37 ASP B OD2 1 ATOM 2829 N N . LYS B 2 38 ? 29.587 -24.769 -63.756 1.00 74.77 ? 38 LYS B N 1 ATOM 2830 C CA . LYS B 2 38 ? 28.835 -25.197 -62.571 1.00 78.60 ? 38 LYS B CA 1 ATOM 2831 C C . LYS B 2 38 ? 29.569 -26.278 -61.787 1.00 75.68 ? 38 LYS B C 1 ATOM 2832 O O . LYS B 2 38 ? 29.725 -26.180 -60.571 1.00 74.01 ? 38 LYS B O 1 ATOM 2833 C CB . LYS B 2 38 ? 27.470 -25.738 -63.007 1.00 85.95 ? 38 LYS B CB 1 ATOM 2834 C CG . LYS B 2 38 ? 26.501 -26.067 -61.874 1.00 92.68 ? 38 LYS B CG 1 ATOM 2835 C CD . LYS B 2 38 ? 25.773 -27.397 -62.092 1.00 98.30 ? 38 LYS B CD 1 ATOM 2836 C CE . LYS B 2 38 ? 24.927 -27.439 -63.366 1.00 101.72 ? 38 LYS B CE 1 ATOM 2837 N NZ . LYS B 2 38 ? 23.664 -26.653 -63.270 1.00 105.64 ? 38 LYS B NZ 1 ATOM 2838 N N . GLU B 2 39 ? 30.010 -27.305 -62.500 1.00 75.71 ? 39 GLU B N 1 ATOM 2839 C CA . GLU B 2 39 ? 30.617 -28.479 -61.890 1.00 76.64 ? 39 GLU B CA 1 ATOM 2840 C C . GLU B 2 39 ? 31.862 -28.143 -61.081 1.00 71.65 ? 39 GLU B C 1 ATOM 2841 O O . GLU B 2 39 ? 31.939 -28.493 -59.907 1.00 72.99 ? 39 GLU B O 1 ATOM 2842 C CB . GLU B 2 39 ? 30.964 -29.518 -62.965 1.00 80.94 ? 39 GLU B CB 1 ATOM 2843 C CG . GLU B 2 39 ? 31.768 -30.704 -62.450 1.00 85.11 ? 39 GLU B CG 1 ATOM 2844 C CD . GLU B 2 39 ? 31.917 -31.803 -63.483 1.00 89.97 ? 39 GLU B CD 1 ATOM 2845 O OE1 . GLU B 2 39 ? 30.883 -32.370 -63.899 1.00 95.49 ? 39 GLU B OE1 1 ATOM 2846 O OE2 . GLU B 2 39 ? 33.067 -32.094 -63.881 1.00 89.51 ? 39 GLU B OE2 1 ATOM 2847 N N . SER B 2 40 ? 32.837 -27.488 -61.709 1.00 65.86 ? 40 SER B N 1 ATOM 2848 C CA . SER B 2 40 ? 34.082 -27.161 -61.024 1.00 62.27 ? 40 SER B CA 1 ATOM 2849 C C . SER B 2 40 ? 33.863 -26.152 -59.893 1.00 60.65 ? 40 SER B C 1 ATOM 2850 O O . SER B 2 40 ? 34.538 -26.227 -58.859 1.00 58.55 ? 40 SER B O 1 ATOM 2851 C CB . SER B 2 40 ? 35.148 -26.655 -62.001 1.00 60.08 ? 40 SER B CB 1 ATOM 2852 O OG . SER B 2 40 ? 34.740 -25.467 -62.647 1.00 62.02 ? 40 SER B OG 1 ATOM 2853 N N . THR B 2 41 ? 32.922 -25.226 -60.080 1.00 59.42 ? 41 THR B N 1 ATOM 2854 C CA . THR B 2 41 ? 32.576 -24.269 -59.031 1.00 58.58 ? 41 THR B CA 1 ATOM 2855 C C . THR B 2 41 ? 32.001 -24.965 -57.796 1.00 59.27 ? 41 THR B C 1 ATOM 2856 O O . THR B 2 41 ? 32.407 -24.676 -56.675 1.00 57.07 ? 41 THR B O 1 ATOM 2857 C CB . THR B 2 41 ? 31.582 -23.197 -59.532 1.00 59.92 ? 41 THR B CB 1 ATOM 2858 O OG1 . THR B 2 41 ? 32.211 -22.390 -60.534 1.00 58.40 ? 41 THR B OG1 1 ATOM 2859 C CG2 . THR B 2 41 ? 31.123 -22.288 -58.392 1.00 60.38 ? 41 THR B CG2 1 ATOM 2860 N N . GLN B 2 42 ? 31.064 -25.883 -58.001 1.00 63.04 ? 42 GLN B N 1 ATOM 2861 C CA . GLN B 2 42 ? 30.407 -26.572 -56.880 1.00 66.30 ? 42 GLN B CA 1 ATOM 2862 C C . GLN B 2 42 ? 31.369 -27.508 -56.167 1.00 65.46 ? 42 GLN B C 1 ATOM 2863 O O . GLN B 2 42 ? 31.292 -27.678 -54.953 1.00 66.15 ? 42 GLN B O 1 ATOM 2864 C CB . GLN B 2 42 ? 29.186 -27.361 -57.358 1.00 70.14 ? 42 GLN B CB 1 ATOM 2865 C CG . GLN B 2 42 ? 28.367 -27.986 -56.233 1.00 73.63 ? 42 GLN B CG 1 ATOM 2866 C CD . GLN B 2 42 ? 27.776 -26.955 -55.285 1.00 75.80 ? 42 GLN B CD 1 ATOM 2867 O OE1 . GLN B 2 42 ? 27.997 -27.005 -54.073 1.00 75.73 ? 42 GLN B OE1 1 ATOM 2868 N NE2 . GLN B 2 42 ? 27.015 -26.011 -55.835 1.00 77.94 ? 42 GLN B NE2 1 ATOM 2869 N N . LYS B 2 43 ? 32.253 -28.129 -56.938 1.00 65.41 ? 43 LYS B N 1 ATOM 2870 C CA . LYS B 2 43 ? 33.371 -28.894 -56.392 1.00 66.69 ? 43 LYS B CA 1 ATOM 2871 C C . LYS B 2 43 ? 34.171 -28.027 -55.411 1.00 62.87 ? 43 LYS B C 1 ATOM 2872 O O . LYS B 2 43 ? 34.464 -28.445 -54.288 1.00 64.52 ? 43 LYS B O 1 ATOM 2873 C CB . LYS B 2 43 ? 34.281 -29.364 -57.537 1.00 70.72 ? 43 LYS B CB 1 ATOM 2874 C CG . LYS B 2 43 ? 34.564 -30.859 -57.586 1.00 77.57 ? 43 LYS B CG 1 ATOM 2875 C CD . LYS B 2 43 ? 34.268 -31.443 -58.969 1.00 84.02 ? 43 LYS B CD 1 ATOM 2876 C CE . LYS B 2 43 ? 35.167 -32.629 -59.310 1.00 88.16 ? 43 LYS B CE 1 ATOM 2877 N NZ . LYS B 2 43 ? 35.177 -33.679 -58.251 1.00 90.79 ? 43 LYS B NZ 1 ATOM 2878 N N . ALA B 2 44 ? 34.508 -26.811 -55.832 1.00 57.73 ? 44 ALA B N 1 ATOM 2879 C CA . ALA B 2 44 ? 35.291 -25.913 -54.997 1.00 55.69 ? 44 ALA B CA 1 ATOM 2880 C C . ALA B 2 44 ? 34.545 -25.508 -53.733 1.00 56.58 ? 44 ALA B C 1 ATOM 2881 O O . ALA B 2 44 ? 35.132 -25.438 -52.660 1.00 55.58 ? 44 ALA B O 1 ATOM 2882 C CB . ALA B 2 44 ? 35.697 -24.678 -55.780 1.00 54.94 ? 44 ALA B CB 1 ATOM 2883 N N . ILE B 2 45 ? 33.252 -25.233 -53.856 1.00 58.34 ? 45 ILE B N 1 ATOM 2884 C CA . ILE B 2 45 ? 32.457 -24.856 -52.693 1.00 60.50 ? 45 ILE B CA 1 ATOM 2885 C C . ILE B 2 45 ? 32.382 -25.992 -51.671 1.00 61.28 ? 45 ILE B C 1 ATOM 2886 O O . ILE B 2 45 ? 32.473 -25.746 -50.471 1.00 62.89 ? 45 ILE B O 1 ATOM 2887 C CB . ILE B 2 45 ? 31.041 -24.391 -53.101 1.00 63.70 ? 45 ILE B CB 1 ATOM 2888 C CG1 . ILE B 2 45 ? 31.125 -23.018 -53.778 1.00 62.97 ? 45 ILE B CG1 1 ATOM 2889 C CG2 . ILE B 2 45 ? 30.112 -24.326 -51.891 1.00 65.34 ? 45 ILE B CG2 1 ATOM 2890 C CD1 . ILE B 2 45 ? 29.873 -22.647 -54.544 1.00 66.36 ? 45 ILE B CD1 1 ATOM 2891 N N . ASP B 2 46 ? 32.226 -27.225 -52.143 1.00 61.49 ? 46 ASP B N 1 ATOM 2892 C CA . ASP B 2 46 ? 32.180 -28.382 -51.247 1.00 63.85 ? 46 ASP B CA 1 ATOM 2893 C C . ASP B 2 46 ? 33.503 -28.602 -50.505 1.00 61.30 ? 46 ASP B C 1 ATOM 2894 O O . ASP B 2 46 ? 33.506 -28.896 -49.313 1.00 63.76 ? 46 ASP B O 1 ATOM 2895 C CB . ASP B 2 46 ? 31.796 -29.653 -52.014 1.00 66.19 ? 46 ASP B CB 1 ATOM 2896 C CG . ASP B 2 46 ? 30.386 -29.587 -52.599 1.00 70.45 ? 46 ASP B CG 1 ATOM 2897 O OD1 . ASP B 2 46 ? 29.650 -28.623 -52.285 1.00 72.10 ? 46 ASP B OD1 1 ATOM 2898 O OD2 . ASP B 2 46 ? 30.015 -30.498 -53.379 1.00 73.02 ? 46 ASP B OD2 1 ATOM 2899 N N . GLY B 2 47 ? 34.620 -28.447 -51.200 1.00 58.07 ? 47 GLY B N 1 ATOM 2900 C CA . GLY B 2 47 ? 35.928 -28.682 -50.593 1.00 56.46 ? 47 GLY B CA 1 ATOM 2901 C C . GLY B 2 47 ? 36.260 -27.670 -49.518 1.00 56.25 ? 47 GLY B C 1 ATOM 2902 O O . GLY B 2 47 ? 36.673 -28.029 -48.411 1.00 56.17 ? 47 GLY B O 1 ATOM 2903 N N . VAL B 2 48 ? 36.060 -26.398 -49.845 1.00 56.19 ? 48 VAL B N 1 ATOM 2904 C CA . VAL B 2 48 ? 36.350 -25.308 -48.924 1.00 55.02 ? 48 VAL B CA 1 ATOM 2905 C C . VAL B 2 48 ? 35.416 -25.360 -47.716 1.00 56.35 ? 48 VAL B C 1 ATOM 2906 O O . VAL B 2 48 ? 35.851 -25.155 -46.589 1.00 56.86 ? 48 VAL B O 1 ATOM 2907 C CB . VAL B 2 48 ? 36.252 -23.950 -49.640 1.00 55.65 ? 48 VAL B CB 1 ATOM 2908 C CG1 . VAL B 2 48 ? 36.389 -22.801 -48.657 1.00 56.29 ? 48 VAL B CG1 1 ATOM 2909 C CG2 . VAL B 2 48 ? 37.336 -23.854 -50.708 1.00 55.10 ? 48 VAL B CG2 1 ATOM 2910 N N . THR B 2 49 ? 34.144 -25.667 -47.942 1.00 57.58 ? 49 THR B N 1 ATOM 2911 C CA . THR B 2 49 ? 33.189 -25.792 -46.841 1.00 60.06 ? 49 THR B CA 1 ATOM 2912 C C . THR B 2 49 ? 33.565 -26.933 -45.895 1.00 62.06 ? 49 THR B C 1 ATOM 2913 O O . THR B 2 49 ? 33.589 -26.766 -44.670 1.00 62.70 ? 49 THR B O 1 ATOM 2914 C CB . THR B 2 49 ? 31.767 -26.033 -47.369 1.00 61.83 ? 49 THR B CB 1 ATOM 2915 O OG1 . THR B 2 49 ? 31.405 -24.970 -48.259 1.00 59.84 ? 49 THR B OG1 1 ATOM 2916 C CG2 . THR B 2 49 ? 30.774 -26.114 -46.228 1.00 64.07 ? 49 THR B CG2 1 ATOM 2917 N N . ASN B 2 50 ? 33.867 -28.095 -46.464 1.00 63.25 ? 50 ASN B N 1 ATOM 2918 C CA . ASN B 2 50 ? 34.310 -29.228 -45.654 1.00 64.98 ? 50 ASN B CA 1 ATOM 2919 C C . ASN B 2 50 ? 35.560 -28.885 -44.850 1.00 62.98 ? 50 ASN B C 1 ATOM 2920 O O . ASN B 2 50 ? 35.690 -29.289 -43.700 1.00 63.28 ? 50 ASN B O 1 ATOM 2921 C CB . ASN B 2 50 ? 34.557 -30.463 -46.528 1.00 65.99 ? 50 ASN B CB 1 ATOM 2922 C CG . ASN B 2 50 ? 33.270 -31.038 -47.115 1.00 70.07 ? 50 ASN B CG 1 ATOM 2923 O OD1 . ASN B 2 50 ? 32.167 -30.654 -46.733 1.00 72.07 ? 50 ASN B OD1 1 ATOM 2924 N ND2 . ASN B 2 50 ? 33.412 -31.958 -48.060 1.00 71.65 ? 50 ASN B ND2 1 ATOM 2925 N N . LYS B 2 51 ? 36.467 -28.123 -45.459 1.00 61.53 ? 51 LYS B N 1 ATOM 2926 C CA . LYS B 2 51 ? 37.707 -27.706 -44.803 1.00 59.70 ? 51 LYS B CA 1 ATOM 2927 C C . LYS B 2 51 ? 37.425 -26.834 -43.579 1.00 60.45 ? 51 LYS B C 1 ATOM 2928 O O . LYS B 2 51 ? 37.952 -27.082 -42.498 1.00 61.10 ? 51 LYS B O 1 ATOM 2929 C CB . LYS B 2 51 ? 38.604 -26.953 -45.792 1.00 57.98 ? 51 LYS B CB 1 ATOM 2930 C CG . LYS B 2 51 ? 39.816 -26.289 -45.161 1.00 57.74 ? 51 LYS B CG 1 ATOM 2931 C CD . LYS B 2 51 ? 40.615 -25.500 -46.182 1.00 57.23 ? 51 LYS B CD 1 ATOM 2932 C CE . LYS B 2 51 ? 41.344 -26.414 -47.149 1.00 56.53 ? 51 LYS B CE 1 ATOM 2933 N NZ . LYS B 2 51 ? 42.542 -25.728 -47.693 1.00 56.76 ? 51 LYS B NZ 1 ATOM 2934 N N . VAL B 2 52 ? 36.593 -25.817 -43.749 1.00 60.17 ? 52 VAL B N 1 ATOM 2935 C CA . VAL B 2 52 ? 36.271 -24.930 -42.643 1.00 61.26 ? 52 VAL B CA 1 ATOM 2936 C C . VAL B 2 52 ? 35.699 -25.752 -41.480 1.00 63.19 ? 52 VAL B C 1 ATOM 2937 O O . VAL B 2 52 ? 36.172 -25.648 -40.341 1.00 63.37 ? 52 VAL B O 1 ATOM 2938 C CB . VAL B 2 52 ? 35.287 -23.813 -43.071 1.00 62.59 ? 52 VAL B CB 1 ATOM 2939 C CG1 . VAL B 2 52 ? 34.907 -22.943 -41.876 1.00 64.86 ? 52 VAL B CG1 1 ATOM 2940 C CG2 . VAL B 2 52 ? 35.897 -22.952 -44.167 1.00 60.53 ? 52 VAL B CG2 1 ATOM 2941 N N . ASN B 2 53 ? 34.708 -26.590 -41.772 1.00 64.68 ? 53 ASN B N 1 ATOM 2942 C CA . ASN B 2 53 ? 34.087 -27.425 -40.737 1.00 67.91 ? 53 ASN B CA 1 ATOM 2943 C C . ASN B 2 53 ? 35.080 -28.402 -40.116 1.00 67.13 ? 53 ASN B C 1 ATOM 2944 O O . ASN B 2 53 ? 35.029 -28.660 -38.916 1.00 68.14 ? 53 ASN B O 1 ATOM 2945 C CB . ASN B 2 53 ? 32.881 -28.191 -41.290 1.00 70.64 ? 53 ASN B CB 1 ATOM 2946 C CG . ASN B 2 53 ? 31.801 -27.274 -41.829 1.00 72.62 ? 53 ASN B CG 1 ATOM 2947 O OD1 . ASN B 2 53 ? 31.631 -26.152 -41.359 1.00 74.25 ? 53 ASN B OD1 1 ATOM 2948 N ND2 . ASN B 2 53 ? 31.070 -27.748 -42.828 1.00 74.48 ? 53 ASN B ND2 1 ATOM 2949 N N . SER B 2 54 ? 35.987 -28.937 -40.928 1.00 66.62 ? 54 SER B N 1 ATOM 2950 C CA . SER B 2 54 ? 37.050 -29.799 -40.410 1.00 67.63 ? 54 SER B CA 1 ATOM 2951 C C . SER B 2 54 ? 37.931 -29.023 -39.435 1.00 68.51 ? 54 SER B C 1 ATOM 2952 O O . SER B 2 54 ? 38.252 -29.526 -38.358 1.00 68.80 ? 54 SER B O 1 ATOM 2953 C CB . SER B 2 54 ? 37.906 -30.395 -41.539 1.00 65.50 ? 54 SER B CB 1 ATOM 2954 O OG . SER B 2 54 ? 37.268 -31.503 -42.140 1.00 65.85 ? 54 SER B OG 1 ATOM 2955 N N . ILE B 2 55 ? 38.308 -27.802 -39.814 1.00 69.05 ? 55 ILE B N 1 ATOM 2956 C CA . ILE B 2 55 ? 39.118 -26.941 -38.951 1.00 71.19 ? 55 ILE B CA 1 ATOM 2957 C C . ILE B 2 55 ? 38.386 -26.622 -37.652 1.00 75.18 ? 55 ILE B C 1 ATOM 2958 O O . ILE B 2 55 ? 38.915 -26.860 -36.567 1.00 76.29 ? 55 ILE B O 1 ATOM 2959 C CB . ILE B 2 55 ? 39.524 -25.630 -39.663 1.00 71.30 ? 55 ILE B CB 1 ATOM 2960 C CG1 . ILE B 2 55 ? 40.593 -25.928 -40.714 1.00 69.91 ? 55 ILE B CG1 1 ATOM 2961 C CG2 . ILE B 2 55 ? 40.051 -24.602 -38.666 1.00 72.97 ? 55 ILE B CG2 1 ATOM 2962 C CD1 . ILE B 2 55 ? 40.927 -24.762 -41.614 1.00 70.28 ? 55 ILE B CD1 1 ATOM 2963 N N . ILE B 2 56 ? 37.174 -26.084 -37.764 1.00 78.24 ? 56 ILE B N 1 ATOM 2964 C CA . ILE B 2 56 ? 36.379 -25.754 -36.585 1.00 80.75 ? 56 ILE B CA 1 ATOM 2965 C C . ILE B 2 56 ? 36.281 -26.966 -35.658 1.00 85.35 ? 56 ILE B C 1 ATOM 2966 O O . ILE B 2 56 ? 36.529 -26.858 -34.458 1.00 87.26 ? 56 ILE B O 1 ATOM 2967 C CB . ILE B 2 56 ? 34.954 -25.315 -36.968 1.00 82.36 ? 56 ILE B CB 1 ATOM 2968 C CG1 . ILE B 2 56 ? 34.985 -23.978 -37.716 1.00 81.06 ? 56 ILE B CG1 1 ATOM 2969 C CG2 . ILE B 2 56 ? 34.068 -25.218 -35.726 1.00 85.20 ? 56 ILE B CG2 1 ATOM 2970 C CD1 . ILE B 2 56 ? 33.705 -23.665 -38.461 1.00 82.39 ? 56 ILE B CD1 1 ATOM 2971 N N . ASP B 2 57 ? 35.929 -28.117 -36.229 1.00 88.76 ? 57 ASP B N 1 ATOM 2972 C CA . ASP B 2 57 ? 35.656 -29.324 -35.445 1.00 93.04 ? 57 ASP B CA 1 ATOM 2973 C C . ASP B 2 57 ? 36.886 -29.877 -34.721 1.00 90.60 ? 57 ASP B C 1 ATOM 2974 O O . ASP B 2 57 ? 36.784 -30.333 -33.590 1.00 90.50 ? 57 ASP B O 1 ATOM 2975 C CB . ASP B 2 57 ? 35.054 -30.417 -36.335 1.00 95.81 ? 57 ASP B CB 1 ATOM 2976 C CG . ASP B 2 57 ? 34.694 -31.664 -35.554 1.00 101.30 ? 57 ASP B CG 1 ATOM 2977 O OD1 . ASP B 2 57 ? 33.828 -31.573 -34.656 1.00 107.68 ? 57 ASP B OD1 1 ATOM 2978 O OD2 . ASP B 2 57 ? 35.285 -32.730 -35.825 1.00 102.59 ? 57 ASP B OD2 1 ATOM 2979 N N . LYS B 2 58 ? 38.041 -29.847 -35.378 1.00 89.17 ? 58 LYS B N 1 ATOM 2980 C CA . LYS B 2 58 ? 39.278 -30.347 -34.773 1.00 88.58 ? 58 LYS B CA 1 ATOM 2981 C C . LYS B 2 58 ? 39.711 -29.540 -33.552 1.00 92.00 ? 58 LYS B C 1 ATOM 2982 O O . LYS B 2 58 ? 40.331 -30.080 -32.638 1.00 91.35 ? 58 LYS B O 1 ATOM 2983 C CB . LYS B 2 58 ? 40.410 -30.411 -35.812 1.00 85.79 ? 58 LYS B CB 1 ATOM 2984 C CG . LYS B 2 58 ? 40.853 -31.818 -36.205 1.00 85.94 ? 58 LYS B CG 1 ATOM 2985 C CD . LYS B 2 58 ? 39.769 -32.871 -36.017 1.00 89.25 ? 58 LYS B CD 1 ATOM 2986 C CE . LYS B 2 58 ? 40.133 -34.176 -36.693 1.00 90.08 ? 58 LYS B CE 1 ATOM 2987 N NZ . LYS B 2 58 ? 39.370 -35.324 -36.126 1.00 93.48 ? 58 LYS B NZ 1 ATOM 2988 N N . MET B 2 59 ? 39.361 -28.257 -33.528 1.00 96.61 ? 59 MET B N 1 ATOM 2989 C CA . MET B 2 59 ? 39.678 -27.387 -32.398 1.00 100.14 ? 59 MET B CA 1 ATOM 2990 C C . MET B 2 59 ? 38.586 -27.435 -31.316 1.00 106.57 ? 59 MET B C 1 ATOM 2991 O O . MET B 2 59 ? 38.651 -26.693 -30.338 1.00 108.75 ? 59 MET B O 1 ATOM 2992 C CB . MET B 2 59 ? 39.870 -25.951 -32.889 1.00 99.09 ? 59 MET B CB 1 ATOM 2993 C CG . MET B 2 59 ? 40.859 -25.797 -34.042 1.00 96.58 ? 59 MET B CG 1 ATOM 2994 S SD . MET B 2 59 ? 42.603 -26.034 -33.634 1.00 97.28 ? 59 MET B SD 1 ATOM 2995 C CE . MET B 2 59 ? 42.805 -25.113 -32.110 1.00 99.74 ? 59 MET B CE 1 ATOM 2996 N N . ASN B 2 60 ? 37.594 -28.310 -31.495 1.00 111.44 ? 60 ASN B N 1 ATOM 2997 C CA . ASN B 2 60 ? 36.477 -28.467 -30.555 1.00 116.53 ? 60 ASN B CA 1 ATOM 2998 C C . ASN B 2 60 ? 36.931 -28.861 -29.148 1.00 117.57 ? 60 ASN B C 1 ATOM 2999 O O . ASN B 2 60 ? 36.635 -28.164 -28.176 1.00 117.66 ? 60 ASN B O 1 ATOM 3000 C CB . ASN B 2 60 ? 35.494 -29.516 -31.093 1.00 118.82 ? 60 ASN B CB 1 ATOM 3001 C CG . ASN B 2 60 ? 34.341 -29.785 -30.149 1.00 123.64 ? 60 ASN B CG 1 ATOM 3002 O OD1 . ASN B 2 60 ? 34.183 -30.900 -29.651 1.00 124.84 ? 60 ASN B OD1 1 ATOM 3003 N ND2 . ASN B 2 60 ? 33.529 -28.765 -29.898 1.00 126.22 ? 60 ASN B ND2 1 ATOM 3004 N N . THR B 2 61 ? 37.631 -29.987 -29.044 1.00 120.87 ? 61 THR B N 1 ATOM 3005 C CA . THR B 2 61 ? 38.208 -30.404 -27.774 1.00 118.93 ? 61 THR B CA 1 ATOM 3006 C C . THR B 2 61 ? 39.527 -29.669 -27.623 1.00 114.69 ? 61 THR B C 1 ATOM 3007 O O . THR B 2 61 ? 40.428 -29.815 -28.448 1.00 116.36 ? 61 THR B O 1 ATOM 3008 C CB . THR B 2 61 ? 38.444 -31.923 -27.693 1.00 123.37 ? 61 THR B CB 1 ATOM 3009 O OG1 . THR B 2 61 ? 37.282 -32.621 -28.155 1.00 128.40 ? 61 THR B OG1 1 ATOM 3010 C CG2 . THR B 2 61 ? 38.741 -32.336 -26.254 1.00 122.43 ? 61 THR B CG2 1 ATOM 3011 N N . GLN B 2 62 ? 39.618 -28.869 -26.570 1.00 111.64 ? 62 GLN B N 1 ATOM 3012 C CA . GLN B 2 62 ? 40.771 -28.012 -26.338 1.00 108.75 ? 62 GLN B CA 1 ATOM 3013 C C . GLN B 2 62 ? 40.752 -27.537 -24.881 1.00 104.84 ? 62 GLN B C 1 ATOM 3014 O O . GLN B 2 62 ? 39.694 -27.510 -24.238 1.00 109.13 ? 62 GLN B O 1 ATOM 3015 C CB . GLN B 2 62 ? 40.749 -26.837 -27.329 1.00 108.54 ? 62 GLN B CB 1 ATOM 3016 C CG . GLN B 2 62 ? 41.548 -25.606 -26.918 1.00 106.16 ? 62 GLN B CG 1 ATOM 3017 C CD . GLN B 2 62 ? 41.568 -24.530 -27.986 1.00 108.33 ? 62 GLN B CD 1 ATOM 3018 O OE1 . GLN B 2 62 ? 41.295 -24.792 -29.158 1.00 112.03 ? 62 GLN B OE1 1 ATOM 3019 N NE2 . GLN B 2 62 ? 41.893 -23.306 -27.584 1.00 108.30 ? 62 GLN B NE2 1 ATOM 3020 N N . PHE B 2 63 ? 41.926 -27.172 -24.375 1.00 98.29 ? 63 PHE B N 1 ATOM 3021 C CA . PHE B 2 63 ? 42.114 -26.841 -22.963 1.00 94.01 ? 63 PHE B CA 1 ATOM 3022 C C . PHE B 2 63 ? 41.208 -25.715 -22.456 1.00 95.98 ? 63 PHE B C 1 ATOM 3023 O O . PHE B 2 63 ? 41.112 -24.652 -23.069 1.00 98.62 ? 63 PHE B O 1 ATOM 3024 C CB . PHE B 2 63 ? 43.573 -26.470 -22.706 1.00 87.61 ? 63 PHE B CB 1 ATOM 3025 C CG . PHE B 2 63 ? 43.924 -26.383 -21.253 1.00 83.51 ? 63 PHE B CG 1 ATOM 3026 C CD1 . PHE B 2 63 ? 44.160 -27.535 -20.518 1.00 80.30 ? 63 PHE B CD1 1 ATOM 3027 C CD2 . PHE B 2 63 ? 44.016 -25.149 -20.617 1.00 82.66 ? 63 PHE B CD2 1 ATOM 3028 C CE1 . PHE B 2 63 ? 44.483 -27.458 -19.176 1.00 79.42 ? 63 PHE B CE1 1 ATOM 3029 C CE2 . PHE B 2 63 ? 44.338 -25.066 -19.271 1.00 78.37 ? 63 PHE B CE2 1 ATOM 3030 C CZ . PHE B 2 63 ? 44.574 -26.223 -18.552 1.00 77.94 ? 63 PHE B CZ 1 ATOM 3031 N N . GLU B 2 64 ? 40.546 -25.972 -21.331 1.00 96.35 ? 64 GLU B N 1 ATOM 3032 C CA . GLU B 2 64 ? 39.748 -24.972 -20.641 1.00 98.08 ? 64 GLU B CA 1 ATOM 3033 C C . GLU B 2 64 ? 40.356 -24.715 -19.269 1.00 94.56 ? 64 GLU B C 1 ATOM 3034 O O . GLU B 2 64 ? 40.525 -25.639 -18.470 1.00 94.66 ? 64 GLU B O 1 ATOM 3035 C CB . GLU B 2 64 ? 38.310 -25.456 -20.484 1.00 102.23 ? 64 GLU B CB 1 ATOM 3036 C CG . GLU B 2 64 ? 37.584 -25.684 -21.800 1.00 105.87 ? 64 GLU B CG 1 ATOM 3037 C CD . GLU B 2 64 ? 36.223 -26.322 -21.603 1.00 111.24 ? 64 GLU B CD 1 ATOM 3038 O OE1 . GLU B 2 64 ? 35.682 -26.234 -20.479 1.00 111.57 ? 64 GLU B OE1 1 ATOM 3039 O OE2 . GLU B 2 64 ? 35.699 -26.914 -22.572 1.00 114.20 ? 64 GLU B OE2 1 ATOM 3040 N N . ALA B 2 65 ? 40.686 -23.458 -18.999 1.00 93.48 ? 65 ALA B N 1 ATOM 3041 C CA . ALA B 2 65 ? 41.269 -23.079 -17.718 1.00 92.21 ? 65 ALA B CA 1 ATOM 3042 C C . ALA B 2 65 ? 40.196 -22.999 -16.626 1.00 93.96 ? 65 ALA B C 1 ATOM 3043 O O . ALA B 2 65 ? 39.055 -22.616 -16.894 1.00 91.16 ? 65 ALA B O 1 ATOM 3044 C CB . ALA B 2 65 ? 42.003 -21.750 -17.847 1.00 91.49 ? 65 ALA B CB 1 ATOM 3045 N N . VAL B 2 66 ? 40.575 -23.375 -15.405 1.00 94.29 ? 66 VAL B N 1 ATOM 3046 C CA . VAL B 2 66 ? 39.694 -23.296 -14.238 1.00 97.34 ? 66 VAL B CA 1 ATOM 3047 C C . VAL B 2 66 ? 40.368 -22.447 -13.167 1.00 95.02 ? 66 VAL B C 1 ATOM 3048 O O . VAL B 2 66 ? 41.595 -22.412 -13.087 1.00 93.41 ? 66 VAL B O 1 ATOM 3049 C CB . VAL B 2 66 ? 39.391 -24.696 -13.661 1.00 100.32 ? 66 VAL B CB 1 ATOM 3050 C CG1 . VAL B 2 66 ? 38.394 -24.608 -12.507 1.00 104.79 ? 66 VAL B CG1 1 ATOM 3051 C CG2 . VAL B 2 66 ? 38.868 -25.617 -14.757 1.00 103.59 ? 66 VAL B CG2 1 ATOM 3052 N N . GLY B 2 67 ? 39.564 -21.771 -12.349 1.00 96.30 ? 67 GLY B N 1 ATOM 3053 C CA . GLY B 2 67 ? 40.079 -20.960 -11.248 1.00 93.59 ? 67 GLY B CA 1 ATOM 3054 C C . GLY B 2 67 ? 40.543 -21.806 -10.072 1.00 90.81 ? 67 GLY B C 1 ATOM 3055 O O . GLY B 2 67 ? 39.794 -22.646 -9.569 1.00 92.03 ? 67 GLY B O 1 ATOM 3056 N N . ARG B 2 68 ? 41.789 -21.596 -9.650 1.00 84.48 ? 68 ARG B N 1 ATOM 3057 C CA . ARG B 2 68 ? 42.325 -22.212 -8.434 1.00 80.81 ? 68 ARG B CA 1 ATOM 3058 C C . ARG B 2 68 ? 43.092 -21.161 -7.657 1.00 78.80 ? 68 ARG B C 1 ATOM 3059 O O . ARG B 2 68 ? 43.866 -20.400 -8.236 1.00 80.87 ? 68 ARG B O 1 ATOM 3060 C CB . ARG B 2 68 ? 43.273 -23.357 -8.767 1.00 78.13 ? 68 ARG B CB 1 ATOM 3061 C CG . ARG B 2 68 ? 42.634 -24.510 -9.510 1.00 77.58 ? 68 ARG B CG 1 ATOM 3062 C CD . ARG B 2 68 ? 43.651 -25.592 -9.832 1.00 74.63 ? 68 ARG B CD 1 ATOM 3063 N NE . ARG B 2 68 ? 43.173 -26.416 -10.932 1.00 76.23 ? 68 ARG B NE 1 ATOM 3064 C CZ . ARG B 2 68 ? 43.277 -26.100 -12.222 1.00 77.58 ? 68 ARG B CZ 1 ATOM 3065 N NH1 . ARG B 2 68 ? 43.886 -24.986 -12.622 1.00 74.20 ? 68 ARG B NH1 1 ATOM 3066 N NH2 . ARG B 2 68 ? 42.769 -26.918 -13.135 1.00 84.47 ? 68 ARG B NH2 1 ATOM 3067 N N . GLU B 2 69 ? 42.893 -21.127 -6.345 1.00 78.76 ? 69 GLU B N 1 ATOM 3068 C CA . GLU B 2 69 ? 43.551 -20.141 -5.502 1.00 75.18 ? 69 GLU B CA 1 ATOM 3069 C C . GLU B 2 69 ? 44.480 -20.814 -4.520 1.00 70.99 ? 69 GLU B C 1 ATOM 3070 O O . GLU B 2 69 ? 44.275 -21.971 -4.154 1.00 67.92 ? 69 GLU B O 1 ATOM 3071 C CB . GLU B 2 69 ? 42.519 -19.300 -4.771 1.00 82.00 ? 69 GLU B CB 1 ATOM 3072 C CG . GLU B 2 69 ? 41.651 -18.507 -5.730 1.00 86.06 ? 69 GLU B CG 1 ATOM 3073 C CD . GLU B 2 69 ? 40.700 -17.577 -5.023 1.00 93.92 ? 69 GLU B CD 1 ATOM 3074 O OE1 . GLU B 2 69 ? 41.128 -16.902 -4.063 1.00 98.67 ? 69 GLU B OE1 1 ATOM 3075 O OE2 . GLU B 2 69 ? 39.524 -17.518 -5.434 1.00 100.97 ? 69 GLU B OE2 1 ATOM 3076 N N . PHE B 2 70 ? 45.506 -20.073 -4.108 1.00 69.19 ? 70 PHE B N 1 ATOM 3077 C CA . PHE B 2 70 ? 46.565 -20.592 -3.255 1.00 67.98 ? 70 PHE B CA 1 ATOM 3078 C C . PHE B 2 70 ? 46.994 -19.543 -2.237 1.00 68.89 ? 70 PHE B C 1 ATOM 3079 O O . PHE B 2 70 ? 47.015 -18.354 -2.539 1.00 69.65 ? 70 PHE B O 1 ATOM 3080 C CB . PHE B 2 70 ? 47.766 -20.982 -4.112 1.00 64.61 ? 70 PHE B CB 1 ATOM 3081 C CG . PHE B 2 70 ? 47.432 -21.929 -5.231 1.00 62.15 ? 70 PHE B CG 1 ATOM 3082 C CD1 . PHE B 2 70 ? 47.454 -23.301 -5.025 1.00 61.74 ? 70 PHE B CD1 1 ATOM 3083 C CD2 . PHE B 2 70 ? 47.096 -21.446 -6.492 1.00 59.99 ? 70 PHE B CD2 1 ATOM 3084 C CE1 . PHE B 2 70 ? 47.150 -24.177 -6.057 1.00 60.80 ? 70 PHE B CE1 1 ATOM 3085 C CE2 . PHE B 2 70 ? 46.786 -22.315 -7.525 1.00 59.59 ? 70 PHE B CE2 1 ATOM 3086 C CZ . PHE B 2 70 ? 46.816 -23.683 -7.309 1.00 59.18 ? 70 PHE B CZ 1 ATOM 3087 N N . ASN B 2 71 ? 47.347 -19.982 -1.032 1.00 70.33 ? 71 ASN B N 1 ATOM 3088 C CA . ASN B 2 71 ? 47.731 -19.042 0.029 1.00 72.10 ? 71 ASN B CA 1 ATOM 3089 C C . ASN B 2 71 ? 49.160 -18.546 -0.164 1.00 69.33 ? 71 ASN B C 1 ATOM 3090 O O . ASN B 2 71 ? 49.812 -18.895 -1.148 1.00 65.12 ? 71 ASN B O 1 ATOM 3091 C CB . ASN B 2 71 ? 47.496 -19.638 1.435 1.00 74.71 ? 71 ASN B CB 1 ATOM 3092 C CG . ASN B 2 71 ? 48.503 -20.712 1.819 1.00 72.96 ? 71 ASN B CG 1 ATOM 3093 O OD1 . ASN B 2 71 ? 49.707 -20.565 1.623 1.00 71.08 ? 71 ASN B OD1 1 ATOM 3094 N ND2 . ASN B 2 71 ? 48.008 -21.794 2.404 1.00 76.54 ? 71 ASN B ND2 1 ATOM 3095 N N . ASN B 2 72 ? 49.637 -17.735 0.775 1.00 73.70 ? 72 ASN B N 1 ATOM 3096 C CA . ASN B 2 72 ? 50.946 -17.089 0.659 1.00 75.45 ? 72 ASN B CA 1 ATOM 3097 C C . ASN B 2 72 ? 52.147 -18.046 0.752 1.00 72.89 ? 72 ASN B C 1 ATOM 3098 O O . ASN B 2 72 ? 53.228 -17.727 0.252 1.00 71.17 ? 72 ASN B O 1 ATOM 3099 C CB . ASN B 2 72 ? 51.076 -15.985 1.713 1.00 81.37 ? 72 ASN B CB 1 ATOM 3100 C CG . ASN B 2 72 ? 52.297 -15.115 1.501 1.00 83.93 ? 72 ASN B CG 1 ATOM 3101 O OD1 . ASN B 2 72 ? 52.636 -14.771 0.370 1.00 85.90 ? 72 ASN B OD1 1 ATOM 3102 N ND2 . ASN B 2 72 ? 52.966 -14.758 2.588 1.00 88.36 ? 72 ASN B ND2 1 ATOM 3103 N N . LEU B 2 73 ? 51.961 -19.198 1.401 1.00 71.63 ? 73 LEU B N 1 ATOM 3104 C CA . LEU B 2 73 ? 52.994 -20.239 1.463 1.00 70.80 ? 73 LEU B CA 1 ATOM 3105 C C . LEU B 2 73 ? 52.688 -21.434 0.536 1.00 68.34 ? 73 LEU B C 1 ATOM 3106 O O . LEU B 2 73 ? 53.060 -22.574 0.829 1.00 65.73 ? 73 LEU B O 1 ATOM 3107 C CB . LEU B 2 73 ? 53.178 -20.713 2.909 1.00 74.58 ? 73 LEU B CB 1 ATOM 3108 C CG . LEU B 2 73 ? 53.799 -19.703 3.881 1.00 78.61 ? 73 LEU B CG 1 ATOM 3109 C CD1 . LEU B 2 73 ? 53.721 -20.226 5.306 1.00 81.49 ? 73 LEU B CD1 1 ATOM 3110 C CD2 . LEU B 2 73 ? 55.243 -19.382 3.511 1.00 78.00 ? 73 LEU B CD2 1 ATOM 3111 N N . GLU B 2 74 ? 52.017 -21.163 -0.584 1.00 65.81 ? 74 GLU B N 1 ATOM 3112 C CA . GLU B 2 74 ? 51.808 -22.161 -1.635 1.00 63.09 ? 74 GLU B CA 1 ATOM 3113 C C . GLU B 2 74 ? 52.207 -21.556 -2.975 1.00 60.25 ? 74 GLU B C 1 ATOM 3114 O O . GLU B 2 74 ? 51.527 -21.754 -3.979 1.00 56.25 ? 74 GLU B O 1 ATOM 3115 C CB . GLU B 2 74 ? 50.347 -22.611 -1.668 1.00 64.07 ? 74 GLU B CB 1 ATOM 3116 C CG . GLU B 2 74 ? 49.902 -23.400 -0.447 1.00 66.05 ? 74 GLU B CG 1 ATOM 3117 C CD . GLU B 2 74 ? 48.418 -23.720 -0.470 1.00 69.29 ? 74 GLU B CD 1 ATOM 3118 O OE1 . GLU B 2 74 ? 47.633 -22.905 -0.994 1.00 70.88 ? 74 GLU B OE1 1 ATOM 3119 O OE2 . GLU B 2 74 ? 48.026 -24.787 0.040 1.00 72.18 ? 74 GLU B OE2 1 ATOM 3120 N N . ARG B 2 75 ? 53.308 -20.804 -2.976 1.00 61.52 ? 75 ARG B N 1 ATOM 3121 C CA . ARG B 2 75 ? 53.760 -20.104 -4.171 1.00 61.49 ? 75 ARG B CA 1 ATOM 3122 C C . ARG B 2 75 ? 54.259 -21.063 -5.240 1.00 59.94 ? 75 ARG B C 1 ATOM 3123 O O . ARG B 2 75 ? 54.072 -20.819 -6.425 1.00 59.46 ? 75 ARG B O 1 ATOM 3124 C CB . ARG B 2 75 ? 54.860 -19.087 -3.833 1.00 66.74 ? 75 ARG B CB 1 ATOM 3125 C CG . ARG B 2 75 ? 54.415 -17.905 -2.975 1.00 71.88 ? 75 ARG B CG 1 ATOM 3126 C CD . ARG B 2 75 ? 53.238 -17.166 -3.599 1.00 77.83 ? 75 ARG B CD 1 ATOM 3127 N NE . ARG B 2 75 ? 52.806 -16.005 -2.823 1.00 87.68 ? 75 ARG B NE 1 ATOM 3128 C CZ . ARG B 2 75 ? 51.757 -15.240 -3.133 1.00 92.27 ? 75 ARG B CZ 1 ATOM 3129 N NH1 . ARG B 2 75 ? 51.021 -15.507 -4.211 1.00 90.98 ? 75 ARG B NH1 1 ATOM 3130 N NH2 . ARG B 2 75 ? 51.439 -14.202 -2.362 1.00 96.04 ? 75 ARG B NH2 1 ATOM 3131 N N . ARG B 2 76 ? 54.892 -22.155 -4.830 1.00 60.79 ? 76 ARG B N 1 ATOM 3132 C CA . ARG B 2 76 ? 55.446 -23.094 -5.798 1.00 58.65 ? 76 ARG B CA 1 ATOM 3133 C C . ARG B 2 76 ? 54.354 -23.712 -6.659 1.00 57.89 ? 76 ARG B C 1 ATOM 3134 O O . ARG B 2 76 ? 54.443 -23.661 -7.885 1.00 58.36 ? 76 ARG B O 1 ATOM 3135 C CB . ARG B 2 76 ? 56.258 -24.175 -5.101 1.00 59.07 ? 76 ARG B CB 1 ATOM 3136 C CG . ARG B 2 76 ? 57.552 -23.667 -4.497 1.00 59.78 ? 76 ARG B CG 1 ATOM 3137 C CD . ARG B 2 76 ? 58.174 -24.738 -3.626 1.00 62.28 ? 76 ARG B CD 1 ATOM 3138 N NE . ARG B 2 76 ? 57.268 -25.093 -2.538 1.00 61.08 ? 76 ARG B NE 1 ATOM 3139 C CZ . ARG B 2 76 ? 57.253 -26.256 -1.902 1.00 62.57 ? 76 ARG B CZ 1 ATOM 3140 N NH1 . ARG B 2 76 ? 58.104 -27.223 -2.225 1.00 66.39 ? 76 ARG B NH1 1 ATOM 3141 N NH2 . ARG B 2 76 ? 56.364 -26.459 -0.939 1.00 62.81 ? 76 ARG B NH2 1 ATOM 3142 N N . ILE B 2 77 ? 53.323 -24.277 -6.028 1.00 59.09 ? 77 ILE B N 1 ATOM 3143 C CA . ILE B 2 77 ? 52.209 -24.873 -6.781 1.00 60.68 ? 77 ILE B CA 1 ATOM 3144 C C . ILE B 2 77 ? 51.340 -23.831 -7.500 1.00 60.84 ? 77 ILE B C 1 ATOM 3145 O O . ILE B 2 77 ? 50.758 -24.122 -8.544 1.00 60.31 ? 77 ILE B O 1 ATOM 3146 C CB . ILE B 2 77 ? 51.318 -25.802 -5.929 1.00 61.82 ? 77 ILE B CB 1 ATOM 3147 C CG1 . ILE B 2 77 ? 50.636 -25.046 -4.795 1.00 65.75 ? 77 ILE B CG1 1 ATOM 3148 C CG2 . ILE B 2 77 ? 52.130 -26.970 -5.384 1.00 64.79 ? 77 ILE B CG2 1 ATOM 3149 C CD1 . ILE B 2 77 ? 49.716 -25.922 -3.962 1.00 70.45 ? 77 ILE B CD1 1 ATOM 3150 N N . GLU B 2 78 ? 51.244 -22.627 -6.952 1.00 60.32 ? 78 GLU B N 1 ATOM 3151 C CA . GLU B 2 78 ? 50.561 -21.554 -7.658 1.00 60.74 ? 78 GLU B CA 1 ATOM 3152 C C . GLU B 2 78 ? 51.285 -21.278 -8.980 1.00 57.63 ? 78 GLU B C 1 ATOM 3153 O O . GLU B 2 78 ? 50.653 -21.103 -10.017 1.00 53.31 ? 78 GLU B O 1 ATOM 3154 C CB . GLU B 2 78 ? 50.510 -20.285 -6.811 1.00 66.36 ? 78 GLU B CB 1 ATOM 3155 C CG . GLU B 2 78 ? 49.918 -19.075 -7.528 1.00 72.53 ? 78 GLU B CG 1 ATOM 3156 C CD . GLU B 2 78 ? 49.916 -17.827 -6.668 1.00 82.75 ? 78 GLU B CD 1 ATOM 3157 O OE1 . GLU B 2 78 ? 50.929 -17.556 -5.984 1.00 91.88 ? 78 GLU B OE1 1 ATOM 3158 O OE2 . GLU B 2 78 ? 48.899 -17.107 -6.672 1.00 92.40 ? 78 GLU B OE2 1 ATOM 3159 N N . ASN B 2 79 ? 52.611 -21.243 -8.928 1.00 56.41 ? 79 ASN B N 1 ATOM 3160 C CA . ASN B 2 79 ? 53.417 -21.003 -10.112 1.00 59.97 ? 79 ASN B CA 1 ATOM 3161 C C . ASN B 2 79 ? 53.276 -22.155 -11.090 1.00 59.91 ? 79 ASN B C 1 ATOM 3162 O O . ASN B 2 79 ? 53.219 -21.948 -12.296 1.00 58.43 ? 79 ASN B O 1 ATOM 3163 C CB . ASN B 2 79 ? 54.883 -20.845 -9.729 1.00 64.12 ? 79 ASN B CB 1 ATOM 3164 C CG . ASN B 2 79 ? 55.742 -20.395 -10.890 1.00 66.77 ? 79 ASN B CG 1 ATOM 3165 O OD1 . ASN B 2 79 ? 55.416 -19.432 -11.573 1.00 72.62 ? 79 ASN B OD1 1 ATOM 3166 N ND2 . ASN B 2 79 ? 56.859 -21.071 -11.098 1.00 69.68 ? 79 ASN B ND2 1 ATOM 3167 N N . LEU B 2 80 ? 53.213 -23.367 -10.549 1.00 60.01 ? 80 LEU B N 1 ATOM 3168 C CA . LEU B 2 80 ? 53.040 -24.563 -11.352 1.00 60.18 ? 80 LEU B CA 1 ATOM 3169 C C . LEU B 2 80 ? 51.729 -24.447 -12.101 1.00 57.26 ? 80 LEU B C 1 ATOM 3170 O O . LEU B 2 80 ? 51.677 -24.642 -13.309 1.00 56.11 ? 80 LEU B O 1 ATOM 3171 C CB . LEU B 2 80 ? 53.039 -25.799 -10.452 1.00 63.16 ? 80 LEU B CB 1 ATOM 3172 C CG . LEU B 2 80 ? 53.313 -27.158 -11.088 1.00 66.33 ? 80 LEU B CG 1 ATOM 3173 C CD1 . LEU B 2 80 ? 53.520 -28.200 -9.997 1.00 68.42 ? 80 LEU B CD1 1 ATOM 3174 C CD2 . LEU B 2 80 ? 52.183 -27.568 -12.011 1.00 69.58 ? 80 LEU B CD2 1 ATOM 3175 N N . ASN B 2 81 ? 50.675 -24.105 -11.369 1.00 57.42 ? 81 ASN B N 1 ATOM 3176 C CA . ASN B 2 81 ? 49.343 -23.931 -11.944 1.00 56.92 ? 81 ASN B CA 1 ATOM 3177 C C . ASN B 2 81 ? 49.332 -22.919 -13.078 1.00 59.03 ? 81 ASN B C 1 ATOM 3178 O O . ASN B 2 81 ? 48.722 -23.154 -14.116 1.00 58.07 ? 81 ASN B O 1 ATOM 3179 C CB . ASN B 2 81 ? 48.366 -23.471 -10.872 1.00 57.30 ? 81 ASN B CB 1 ATOM 3180 C CG . ASN B 2 81 ? 46.937 -23.437 -11.368 1.00 59.07 ? 81 ASN B CG 1 ATOM 3181 O OD1 . ASN B 2 81 ? 46.369 -24.472 -11.719 1.00 63.74 ? 81 ASN B OD1 1 ATOM 3182 N ND2 . ASN B 2 81 ? 46.343 -22.251 -11.389 1.00 57.09 ? 81 ASN B ND2 1 ATOM 3183 N N . LYS B 2 82 ? 50.015 -21.796 -12.868 1.00 60.84 ? 82 LYS B N 1 ATOM 3184 C CA . LYS B 2 82 ? 50.037 -20.722 -13.837 1.00 63.79 ? 82 LYS B CA 1 ATOM 3185 C C . LYS B 2 82 ? 50.798 -21.147 -15.083 1.00 64.00 ? 82 LYS B C 1 ATOM 3186 O O . LYS B 2 82 ? 50.346 -20.903 -16.196 1.00 61.06 ? 82 LYS B O 1 ATOM 3187 C CB . LYS B 2 82 ? 50.677 -19.473 -13.237 1.00 69.96 ? 82 LYS B CB 1 ATOM 3188 C CG . LYS B 2 82 ? 50.521 -18.228 -14.104 1.00 78.85 ? 82 LYS B CG 1 ATOM 3189 C CD . LYS B 2 82 ? 51.495 -17.137 -13.685 1.00 89.22 ? 82 LYS B CD 1 ATOM 3190 C CE . LYS B 2 82 ? 51.446 -15.944 -14.630 1.00 99.22 ? 82 LYS B CE 1 ATOM 3191 N NZ . LYS B 2 82 ? 52.336 -14.845 -14.158 1.00 106.18 ? 82 LYS B NZ 1 ATOM 3192 N N . LYS B 2 83 ? 51.959 -21.767 -14.882 1.00 65.85 ? 83 LYS B N 1 ATOM 3193 C CA . LYS B 2 83 ? 52.791 -22.257 -15.985 1.00 68.16 ? 83 LYS B CA 1 ATOM 3194 C C . LYS B 2 83 ? 52.077 -23.338 -16.791 1.00 65.33 ? 83 LYS B C 1 ATOM 3195 O O . LYS B 2 83 ? 52.205 -23.404 -18.009 1.00 64.89 ? 83 LYS B O 1 ATOM 3196 C CB . LYS B 2 83 ? 54.135 -22.781 -15.461 1.00 72.94 ? 83 LYS B CB 1 ATOM 3197 C CG . LYS B 2 83 ? 55.358 -22.040 -15.978 1.00 83.74 ? 83 LYS B CG 1 ATOM 3198 C CD . LYS B 2 83 ? 55.276 -20.524 -15.827 1.00 89.61 ? 83 LYS B CD 1 ATOM 3199 C CE . LYS B 2 83 ? 56.527 -19.861 -16.393 1.00 98.83 ? 83 LYS B CE 1 ATOM 3200 N NZ . LYS B 2 83 ? 56.222 -18.642 -17.195 1.00 101.99 ? 83 LYS B NZ 1 ATOM 3201 N N . MET B 2 84 ? 51.313 -24.169 -16.094 1.00 63.77 ? 84 MET B N 1 ATOM 3202 C CA . MET B 2 84 ? 50.491 -25.189 -16.724 1.00 60.89 ? 84 MET B CA 1 ATOM 3203 C C . MET B 2 84 ? 49.426 -24.556 -17.618 1.00 57.63 ? 84 MET B C 1 ATOM 3204 O O . MET B 2 84 ? 49.303 -24.926 -18.786 1.00 60.75 ? 84 MET B O 1 ATOM 3205 C CB . MET B 2 84 ? 49.839 -26.050 -15.645 1.00 62.11 ? 84 MET B CB 1 ATOM 3206 C CG . MET B 2 84 ? 49.439 -27.452 -16.072 1.00 64.84 ? 84 MET B CG 1 ATOM 3207 S SD . MET B 2 84 ? 47.671 -27.644 -16.289 1.00 69.46 ? 84 MET B SD 1 ATOM 3208 C CE . MET B 2 84 ? 47.016 -27.131 -14.702 1.00 67.40 ? 84 MET B CE 1 ATOM 3209 N N . GLU B 2 85 ? 48.685 -23.586 -17.092 1.00 78.95 ? 85 GLU B N 1 ATOM 3210 C CA . GLU B 2 85 ? 47.576 -22.995 -17.845 1.00 77.07 ? 85 GLU B CA 1 ATOM 3211 C C . GLU B 2 85 ? 48.058 -22.185 -19.048 1.00 73.02 ? 85 GLU B C 1 ATOM 3212 O O . GLU B 2 85 ? 47.533 -22.330 -20.151 1.00 69.83 ? 85 GLU B O 1 ATOM 3213 C CB . GLU B 2 85 ? 46.677 -22.165 -16.932 1.00 80.87 ? 85 GLU B CB 1 ATOM 3214 C CG . GLU B 2 85 ? 46.105 -22.987 -15.782 1.00 86.21 ? 85 GLU B CG 1 ATOM 3215 C CD . GLU B 2 85 ? 44.618 -22.800 -15.575 1.00 91.52 ? 85 GLU B CD 1 ATOM 3216 O OE1 . GLU B 2 85 ? 44.209 -21.692 -15.165 1.00 96.38 ? 85 GLU B OE1 1 ATOM 3217 O OE2 . GLU B 2 85 ? 43.863 -23.773 -15.802 1.00 94.60 ? 85 GLU B OE2 1 ATOM 3218 N N . ASP B 2 86 ? 49.075 -21.358 -18.834 1.00 72.07 ? 86 ASP B N 1 ATOM 3219 C CA . ASP B 2 86 ? 49.725 -20.619 -19.917 1.00 70.83 ? 86 ASP B CA 1 ATOM 3220 C C . ASP B 2 86 ? 50.357 -21.519 -20.972 1.00 67.39 ? 86 ASP B C 1 ATOM 3221 O O . ASP B 2 86 ? 50.315 -21.209 -22.161 1.00 65.81 ? 86 ASP B O 1 ATOM 3222 C CB . ASP B 2 86 ? 50.809 -19.694 -19.355 1.00 73.84 ? 86 ASP B CB 1 ATOM 3223 C CG . ASP B 2 86 ? 50.265 -18.357 -18.939 1.00 77.43 ? 86 ASP B CG 1 ATOM 3224 O OD1 . ASP B 2 86 ? 49.514 -17.756 -19.742 1.00 81.17 ? 86 ASP B OD1 1 ATOM 3225 O OD2 . ASP B 2 86 ? 50.588 -17.903 -17.823 1.00 80.07 ? 86 ASP B OD2 1 ATOM 3226 N N . GLY B 2 87 ? 50.966 -22.612 -20.529 1.00 65.40 ? 87 GLY B N 1 ATOM 3227 C CA . GLY B 2 87 ? 51.591 -23.562 -21.432 1.00 63.79 ? 87 GLY B CA 1 ATOM 3228 C C . GLY B 2 87 ? 50.621 -24.092 -22.472 1.00 61.95 ? 87 GLY B C 1 ATOM 3229 O O . GLY B 2 87 ? 50.934 -24.116 -23.670 1.00 59.92 ? 87 GLY B O 1 ATOM 3230 N N . PHE B 2 88 ? 49.441 -24.505 -22.016 1.00 60.59 ? 88 PHE B N 1 ATOM 3231 C CA . PHE B 2 88 ? 48.418 -25.031 -22.912 1.00 60.10 ? 88 PHE B CA 1 ATOM 3232 C C . PHE B 2 88 ? 47.834 -23.947 -23.833 1.00 60.39 ? 88 PHE B C 1 ATOM 3233 O O . PHE B 2 88 ? 47.574 -24.210 -25.007 1.00 59.76 ? 88 PHE B O 1 ATOM 3234 C CB . PHE B 2 88 ? 47.312 -25.735 -22.115 1.00 61.20 ? 88 PHE B CB 1 ATOM 3235 C CG . PHE B 2 88 ? 47.711 -27.091 -21.586 1.00 61.94 ? 88 PHE B CG 1 ATOM 3236 C CD1 . PHE B 2 88 ? 48.039 -28.119 -22.457 1.00 61.42 ? 88 PHE B CD1 1 ATOM 3237 C CD2 . PHE B 2 88 ? 47.759 -27.342 -20.222 1.00 64.12 ? 88 PHE B CD2 1 ATOM 3238 C CE1 . PHE B 2 88 ? 48.401 -29.367 -21.990 1.00 62.59 ? 88 PHE B CE1 1 ATOM 3239 C CE2 . PHE B 2 88 ? 48.114 -28.594 -19.744 1.00 65.55 ? 88 PHE B CE2 1 ATOM 3240 C CZ . PHE B 2 88 ? 48.440 -29.606 -20.632 1.00 65.59 ? 88 PHE B CZ 1 ATOM 3241 N N . LEU B 2 89 ? 47.645 -22.734 -23.321 1.00 61.84 ? 89 LEU B N 1 ATOM 3242 C CA . LEU B 2 89 ? 47.172 -21.634 -24.161 1.00 62.92 ? 89 LEU B CA 1 ATOM 3243 C C . LEU B 2 89 ? 48.138 -21.342 -25.310 1.00 60.50 ? 89 LEU B C 1 ATOM 3244 O O . LEU B 2 89 ? 47.718 -21.143 -26.440 1.00 58.40 ? 89 LEU B O 1 ATOM 3245 C CB . LEU B 2 89 ? 46.975 -20.356 -23.351 1.00 66.08 ? 89 LEU B CB 1 ATOM 3246 C CG . LEU B 2 89 ? 45.907 -20.367 -22.255 1.00 71.15 ? 89 LEU B CG 1 ATOM 3247 C CD1 . LEU B 2 89 ? 45.894 -18.989 -21.600 1.00 74.02 ? 89 LEU B CD1 1 ATOM 3248 C CD2 . LEU B 2 89 ? 44.515 -20.762 -22.761 1.00 71.80 ? 89 LEU B CD2 1 ATOM 3249 N N . ASP B 2 90 ? 49.429 -21.309 -25.008 1.00 60.46 ? 90 ASP B N 1 ATOM 3250 C CA . ASP B 2 90 ? 50.439 -21.059 -26.025 1.00 59.67 ? 90 ASP B CA 1 ATOM 3251 C C . ASP B 2 90 ? 50.428 -22.158 -27.093 1.00 57.46 ? 90 ASP B C 1 ATOM 3252 O O . ASP B 2 90 ? 50.510 -21.872 -28.285 1.00 55.81 ? 90 ASP B O 1 ATOM 3253 C CB . ASP B 2 90 ? 51.824 -20.937 -25.388 1.00 61.23 ? 90 ASP B CB 1 ATOM 3254 C CG . ASP B 2 90 ? 51.966 -19.691 -24.536 1.00 65.82 ? 90 ASP B CG 1 ATOM 3255 O OD1 . ASP B 2 90 ? 51.156 -18.753 -24.702 1.00 67.21 ? 90 ASP B OD1 1 ATOM 3256 O OD2 . ASP B 2 90 ? 52.892 -19.641 -23.694 1.00 71.30 ? 90 ASP B OD2 1 ATOM 3257 N N . VAL B 2 91 ? 50.313 -23.406 -26.651 1.00 57.20 ? 91 VAL B N 1 ATOM 3258 C CA . VAL B 2 91 ? 50.220 -24.553 -27.548 1.00 56.28 ? 91 VAL B CA 1 ATOM 3259 C C . VAL B 2 91 ? 49.001 -24.481 -28.472 1.00 55.77 ? 91 VAL B C 1 ATOM 3260 O O . VAL B 2 91 ? 49.118 -24.730 -29.676 1.00 56.58 ? 91 VAL B O 1 ATOM 3261 C CB . VAL B 2 91 ? 50.175 -25.880 -26.758 1.00 56.42 ? 91 VAL B CB 1 ATOM 3262 C CG1 . VAL B 2 91 ? 49.752 -27.042 -27.658 1.00 55.74 ? 91 VAL B CG1 1 ATOM 3263 C CG2 . VAL B 2 91 ? 51.533 -26.157 -26.124 1.00 56.96 ? 91 VAL B CG2 1 ATOM 3264 N N . TRP B 2 92 ? 47.838 -24.159 -27.917 1.00 55.47 ? 92 TRP B N 1 ATOM 3265 C CA . TRP B 2 92 ? 46.623 -24.094 -28.726 1.00 54.74 ? 92 TRP B CA 1 ATOM 3266 C C . TRP B 2 92 ? 46.565 -22.837 -29.590 1.00 54.22 ? 92 TRP B C 1 ATOM 3267 O O . TRP B 2 92 ? 45.945 -22.843 -30.642 1.00 54.82 ? 92 TRP B O 1 ATOM 3268 C CB . TRP B 2 92 ? 45.379 -24.210 -27.852 1.00 54.91 ? 92 TRP B CB 1 ATOM 3269 C CG . TRP B 2 92 ? 45.159 -25.604 -27.379 1.00 56.84 ? 92 TRP B CG 1 ATOM 3270 C CD1 . TRP B 2 92 ? 45.283 -26.066 -26.102 1.00 58.58 ? 92 TRP B CD1 1 ATOM 3271 C CD2 . TRP B 2 92 ? 44.789 -26.735 -28.178 1.00 56.36 ? 92 TRP B CD2 1 ATOM 3272 N NE1 . TRP B 2 92 ? 45.002 -27.407 -26.053 1.00 59.52 ? 92 TRP B NE1 1 ATOM 3273 C CE2 . TRP B 2 92 ? 44.698 -27.843 -27.315 1.00 58.00 ? 92 TRP B CE2 1 ATOM 3274 C CE3 . TRP B 2 92 ? 44.516 -26.915 -29.537 1.00 55.71 ? 92 TRP B CE3 1 ATOM 3275 C CZ2 . TRP B 2 92 ? 44.343 -29.114 -27.763 1.00 59.45 ? 92 TRP B CZ2 1 ATOM 3276 C CZ3 . TRP B 2 92 ? 44.163 -28.176 -29.982 1.00 56.25 ? 92 TRP B CZ3 1 ATOM 3277 C CH2 . TRP B 2 92 ? 44.080 -29.260 -29.097 1.00 58.62 ? 92 TRP B CH2 1 ATOM 3278 N N . THR B 2 93 ? 47.209 -21.765 -29.146 1.00 54.54 ? 93 THR B N 1 ATOM 3279 C CA . THR B 2 93 ? 47.305 -20.559 -29.943 1.00 54.36 ? 93 THR B CA 1 ATOM 3280 C C . THR B 2 93 ? 48.182 -20.833 -31.159 1.00 54.35 ? 93 THR B C 1 ATOM 3281 O O . THR B 2 93 ? 47.850 -20.416 -32.273 1.00 54.00 ? 93 THR B O 1 ATOM 3282 C CB . THR B 2 93 ? 47.873 -19.391 -29.123 1.00 55.89 ? 93 THR B CB 1 ATOM 3283 O OG1 . THR B 2 93 ? 46.940 -19.055 -28.093 1.00 57.73 ? 93 THR B OG1 1 ATOM 3284 C CG2 . THR B 2 93 ? 48.098 -18.170 -29.991 1.00 56.83 ? 93 THR B CG2 1 ATOM 3285 N N . TYR B 2 94 ? 49.288 -21.543 -30.934 1.00 54.86 ? 94 TYR B N 1 ATOM 3286 C CA . TYR B 2 94 ? 50.203 -21.939 -32.000 1.00 54.37 ? 94 TYR B CA 1 ATOM 3287 C C . TYR B 2 94 ? 49.465 -22.822 -32.989 1.00 53.70 ? 94 TYR B C 1 ATOM 3288 O O . TYR B 2 94 ? 49.469 -22.542 -34.180 1.00 52.41 ? 94 TYR B O 1 ATOM 3289 C CB . TYR B 2 94 ? 51.441 -22.647 -31.429 1.00 55.99 ? 94 TYR B CB 1 ATOM 3290 C CG . TYR B 2 94 ? 52.306 -23.370 -32.446 1.00 56.58 ? 94 TYR B CG 1 ATOM 3291 C CD1 . TYR B 2 94 ? 52.042 -24.695 -32.794 1.00 56.21 ? 94 TYR B CD1 1 ATOM 3292 C CD2 . TYR B 2 94 ? 53.398 -22.744 -33.043 1.00 57.74 ? 94 TYR B CD2 1 ATOM 3293 C CE1 . TYR B 2 94 ? 52.822 -25.365 -33.717 1.00 56.78 ? 94 TYR B CE1 1 ATOM 3294 C CE2 . TYR B 2 94 ? 54.187 -23.410 -33.973 1.00 58.06 ? 94 TYR B CE2 1 ATOM 3295 C CZ . TYR B 2 94 ? 53.889 -24.724 -34.305 1.00 57.92 ? 94 TYR B CZ 1 ATOM 3296 O OH . TYR B 2 94 ? 54.651 -25.412 -35.217 1.00 59.32 ? 94 TYR B OH 1 ATOM 3297 N N . ASN B 2 95 ? 48.802 -23.862 -32.492 1.00 55.26 ? 95 ASN B N 1 ATOM 3298 C CA . ASN B 2 95 ? 48.060 -24.781 -33.359 1.00 54.82 ? 95 ASN B CA 1 ATOM 3299 C C . ASN B 2 95 ? 47.075 -24.054 -34.265 1.00 55.28 ? 95 ASN B C 1 ATOM 3300 O O . ASN B 2 95 ? 47.029 -24.307 -35.471 1.00 55.62 ? 95 ASN B O 1 ATOM 3301 C CB . ASN B 2 95 ? 47.301 -25.828 -32.544 1.00 55.58 ? 95 ASN B CB 1 ATOM 3302 C CG . ASN B 2 95 ? 48.217 -26.856 -31.906 1.00 58.53 ? 95 ASN B CG 1 ATOM 3303 O OD1 . ASN B 2 95 ? 49.399 -26.923 -32.215 1.00 60.27 ? 95 ASN B OD1 1 ATOM 3304 N ND2 . ASN B 2 95 ? 47.667 -27.663 -31.006 1.00 60.66 ? 95 ASN B ND2 1 ATOM 3305 N N . ALA B 2 96 ? 46.286 -23.159 -33.680 1.00 54.59 ? 96 ALA B N 1 ATOM 3306 C CA . ALA B 2 96 ? 45.269 -22.430 -34.434 1.00 54.14 ? 96 ALA B CA 1 ATOM 3307 C C . ALA B 2 96 ? 45.897 -21.515 -35.492 1.00 52.90 ? 96 ALA B C 1 ATOM 3308 O O . ALA B 2 96 ? 45.468 -21.506 -36.632 1.00 51.83 ? 96 ALA B O 1 ATOM 3309 C CB . ALA B 2 96 ? 44.388 -21.623 -33.493 1.00 54.99 ? 96 ALA B CB 1 ATOM 3310 N N . GLU B 2 97 ? 46.916 -20.751 -35.118 1.00 53.39 ? 97 GLU B N 1 ATOM 3311 C CA . GLU B 2 97 ? 47.527 -19.824 -36.067 1.00 54.61 ? 97 GLU B CA 1 ATOM 3312 C C . GLU B 2 97 ? 48.241 -20.543 -37.205 1.00 53.61 ? 97 GLU B C 1 ATOM 3313 O O . GLU B 2 97 ? 48.163 -20.113 -38.354 1.00 52.73 ? 97 GLU B O 1 ATOM 3314 C CB . GLU B 2 97 ? 48.457 -18.850 -35.350 1.00 56.47 ? 97 GLU B CB 1 ATOM 3315 C CG . GLU B 2 97 ? 47.671 -17.803 -34.573 1.00 59.69 ? 97 GLU B CG 1 ATOM 3316 C CD . GLU B 2 97 ? 48.521 -16.909 -33.707 1.00 63.50 ? 97 GLU B CD 1 ATOM 3317 O OE1 . GLU B 2 97 ? 49.765 -17.011 -33.757 1.00 66.33 ? 97 GLU B OE1 1 ATOM 3318 O OE2 . GLU B 2 97 ? 47.934 -16.095 -32.967 1.00 67.81 ? 97 GLU B OE2 1 ATOM 3319 N N . LEU B 2 98 ? 48.908 -21.650 -36.887 1.00 53.54 ? 98 LEU B N 1 ATOM 3320 C CA . LEU B 2 98 ? 49.658 -22.393 -37.880 1.00 52.15 ? 98 LEU B CA 1 ATOM 3321 C C . LEU B 2 98 ? 48.712 -23.087 -38.831 1.00 50.83 ? 98 LEU B C 1 ATOM 3322 O O . LEU B 2 98 ? 48.975 -23.154 -40.024 1.00 50.97 ? 98 LEU B O 1 ATOM 3323 C CB . LEU B 2 98 ? 50.575 -23.423 -37.228 1.00 53.40 ? 98 LEU B CB 1 ATOM 3324 C CG . LEU B 2 98 ? 51.442 -24.222 -38.209 1.00 53.67 ? 98 LEU B CG 1 ATOM 3325 C CD1 . LEU B 2 98 ? 52.561 -23.340 -38.740 1.00 54.60 ? 98 LEU B CD1 1 ATOM 3326 C CD2 . LEU B 2 98 ? 51.997 -25.485 -37.559 1.00 55.09 ? 98 LEU B CD2 1 ATOM 3327 N N . LEU B 2 99 ? 47.611 -23.604 -38.310 1.00 50.91 ? 99 LEU B N 1 ATOM 3328 C CA . LEU B 2 99 ? 46.650 -24.301 -39.150 1.00 51.79 ? 99 LEU B CA 1 ATOM 3329 C C . LEU B 2 99 ? 46.026 -23.329 -40.145 1.00 50.97 ? 99 LEU B C 1 ATOM 3330 O O . LEU B 2 99 ? 45.856 -23.652 -41.322 1.00 50.98 ? 99 LEU B O 1 ATOM 3331 C CB . LEU B 2 99 ? 45.566 -24.964 -38.300 1.00 54.70 ? 99 LEU B CB 1 ATOM 3332 C CG . LEU B 2 99 ? 44.542 -25.823 -39.052 1.00 58.29 ? 99 LEU B CG 1 ATOM 3333 C CD1 . LEU B 2 99 ? 45.207 -27.012 -39.722 1.00 59.61 ? 99 LEU B CD1 1 ATOM 3334 C CD2 . LEU B 2 99 ? 43.440 -26.297 -38.112 1.00 61.43 ? 99 LEU B CD2 1 ATOM 3335 N N . VAL B 2 100 ? 45.691 -22.131 -39.676 1.00 50.27 ? 100 VAL B N 1 ATOM 3336 C CA . VAL B 2 100 ? 45.123 -21.120 -40.558 1.00 49.32 ? 100 VAL B CA 1 ATOM 3337 C C . VAL B 2 100 ? 46.100 -20.726 -41.668 1.00 47.53 ? 100 VAL B C 1 ATOM 3338 O O . VAL B 2 100 ? 45.702 -20.647 -42.831 1.00 44.22 ? 100 VAL B O 1 ATOM 3339 C CB . VAL B 2 100 ? 44.630 -19.896 -39.770 1.00 50.64 ? 100 VAL B CB 1 ATOM 3340 C CG1 . VAL B 2 100 ? 44.383 -18.708 -40.695 1.00 51.53 ? 100 VAL B CG1 1 ATOM 3341 C CG2 . VAL B 2 100 ? 43.351 -20.269 -39.030 1.00 51.76 ? 100 VAL B CG2 1 ATOM 3342 N N . LEU B 2 101 ? 47.366 -20.498 -41.314 1.00 47.39 ? 101 LEU B N 1 ATOM 3343 C CA . LEU B 2 101 ? 48.383 -20.163 -42.311 1.00 47.85 ? 101 LEU B CA 1 ATOM 3344 C C . LEU B 2 101 ? 48.557 -21.287 -43.339 1.00 48.26 ? 101 LEU B C 1 ATOM 3345 O O . LEU B 2 101 ? 48.522 -21.047 -44.546 1.00 48.92 ? 101 LEU B O 1 ATOM 3346 C CB . LEU B 2 101 ? 49.730 -19.878 -41.648 1.00 48.68 ? 101 LEU B CB 1 ATOM 3347 C CG . LEU B 2 101 ? 49.885 -18.599 -40.826 1.00 50.49 ? 101 LEU B CG 1 ATOM 3348 C CD1 . LEU B 2 101 ? 51.311 -18.513 -40.305 1.00 51.73 ? 101 LEU B CD1 1 ATOM 3349 C CD2 . LEU B 2 101 ? 49.536 -17.349 -41.617 1.00 51.56 ? 101 LEU B CD2 1 ATOM 3350 N N . MET B 2 102 ? 48.752 -22.506 -42.854 1.00 48.67 ? 102 MET B N 1 ATOM 3351 C CA . MET B 2 102 ? 48.978 -23.645 -43.725 1.00 50.12 ? 102 MET B CA 1 ATOM 3352 C C . MET B 2 102 ? 47.796 -23.908 -44.645 1.00 50.23 ? 102 MET B C 1 ATOM 3353 O O . MET B 2 102 ? 47.985 -24.166 -45.835 1.00 52.48 ? 102 MET B O 1 ATOM 3354 C CB . MET B 2 102 ? 49.265 -24.905 -42.911 1.00 53.11 ? 102 MET B CB 1 ATOM 3355 C CG . MET B 2 102 ? 50.599 -24.900 -42.195 1.00 57.06 ? 102 MET B CG 1 ATOM 3356 S SD . MET B 2 102 ? 50.881 -26.471 -41.343 1.00 62.92 ? 102 MET B SD 1 ATOM 3357 C CE . MET B 2 102 ? 51.932 -27.262 -42.564 1.00 67.63 ? 102 MET B CE 1 ATOM 3358 N N . GLU B 2 103 ? 46.580 -23.851 -44.111 1.00 49.25 ? 103 GLU B N 1 ATOM 3359 C CA . GLU B 2 103 ? 45.408 -24.181 -44.917 1.00 49.65 ? 103 GLU B CA 1 ATOM 3360 C C . GLU B 2 103 ? 44.983 -23.043 -45.847 1.00 48.80 ? 103 GLU B C 1 ATOM 3361 O O . GLU B 2 103 ? 44.413 -23.294 -46.904 1.00 48.25 ? 103 GLU B O 1 ATOM 3362 C CB . GLU B 2 103 ? 44.253 -24.642 -44.031 1.00 51.43 ? 103 GLU B CB 1 ATOM 3363 C CG . GLU B 2 103 ? 44.507 -26.002 -43.387 1.00 53.60 ? 103 GLU B CG 1 ATOM 3364 C CD . GLU B 2 103 ? 44.552 -27.148 -44.393 1.00 55.48 ? 103 GLU B CD 1 ATOM 3365 O OE1 . GLU B 2 103 ? 43.892 -27.061 -45.451 1.00 54.00 ? 103 GLU B OE1 1 ATOM 3366 O OE2 . GLU B 2 103 ? 45.249 -28.150 -44.122 1.00 59.59 ? 103 GLU B OE2 1 ATOM 3367 N N . ASN B 2 104 ? 45.254 -21.799 -45.461 1.00 49.18 ? 104 ASN B N 1 ATOM 3368 C CA . ASN B 2 104 ? 45.081 -20.672 -46.373 1.00 47.91 ? 104 ASN B CA 1 ATOM 3369 C C . ASN B 2 104 ? 45.966 -20.843 -47.613 1.00 47.90 ? 104 ASN B C 1 ATOM 3370 O O . ASN B 2 104 ? 45.517 -20.642 -48.729 1.00 44.49 ? 104 ASN B O 1 ATOM 3371 C CB . ASN B 2 104 ? 45.411 -19.344 -45.683 1.00 48.24 ? 104 ASN B CB 1 ATOM 3372 C CG . ASN B 2 104 ? 44.305 -18.866 -44.757 1.00 49.18 ? 104 ASN B CG 1 ATOM 3373 O OD1 . ASN B 2 104 ? 43.208 -19.420 -44.740 1.00 48.99 ? 104 ASN B OD1 1 ATOM 3374 N ND2 . ASN B 2 104 ? 44.594 -17.826 -43.978 1.00 50.10 ? 104 ASN B ND2 1 ATOM 3375 N N . GLU B 2 105 ? 47.226 -21.219 -47.421 1.00 49.48 ? 105 GLU B N 1 ATOM 3376 C CA . GLU B 2 105 ? 48.084 -21.482 -48.561 1.00 51.28 ? 105 GLU B CA 1 ATOM 3377 C C . GLU B 2 105 ? 47.472 -22.565 -49.449 1.00 49.28 ? 105 GLU B C 1 ATOM 3378 O O . GLU B 2 105 ? 47.436 -22.430 -50.669 1.00 46.57 ? 105 GLU B O 1 ATOM 3379 C CB . GLU B 2 105 ? 49.465 -21.918 -48.111 1.00 56.38 ? 105 GLU B CB 1 ATOM 3380 C CG . GLU B 2 105 ? 50.530 -21.695 -49.161 1.00 64.01 ? 105 GLU B CG 1 ATOM 3381 C CD . GLU B 2 105 ? 51.881 -21.486 -48.529 1.00 74.49 ? 105 GLU B CD 1 ATOM 3382 O OE1 . GLU B 2 105 ? 52.367 -22.442 -47.873 1.00 83.95 ? 105 GLU B OE1 1 ATOM 3383 O OE2 . GLU B 2 105 ? 52.438 -20.367 -48.666 1.00 76.32 ? 105 GLU B OE2 1 ATOM 3384 N N . ARG B 2 106 ? 46.969 -23.627 -48.835 1.00 48.46 ? 106 ARG B N 1 ATOM 3385 C CA . ARG B 2 106 ? 46.411 -24.723 -49.617 1.00 52.59 ? 106 ARG B CA 1 ATOM 3386 C C . ARG B 2 106 ? 45.095 -24.357 -50.299 1.00 50.09 ? 106 ARG B C 1 ATOM 3387 O O . ARG B 2 106 ? 44.793 -24.874 -51.373 1.00 49.60 ? 106 ARG B O 1 ATOM 3388 C CB . ARG B 2 106 ? 46.278 -25.991 -48.769 1.00 56.23 ? 106 ARG B CB 1 ATOM 3389 C CG . ARG B 2 106 ? 47.631 -26.481 -48.244 1.00 60.34 ? 106 ARG B CG 1 ATOM 3390 C CD . ARG B 2 106 ? 47.647 -27.981 -48.014 1.00 67.53 ? 106 ARG B CD 1 ATOM 3391 N NE . ARG B 2 106 ? 47.920 -28.726 -49.256 1.00 73.08 ? 106 ARG B NE 1 ATOM 3392 C CZ . ARG B 2 106 ? 47.365 -29.892 -49.588 1.00 77.70 ? 106 ARG B CZ 1 ATOM 3393 N NH1 . ARG B 2 106 ? 46.471 -30.481 -48.798 1.00 81.06 ? 106 ARG B NH1 1 ATOM 3394 N NH2 . ARG B 2 106 ? 47.695 -30.478 -50.734 1.00 83.88 ? 106 ARG B NH2 1 ATOM 3395 N N . THR B 2 107 ? 44.330 -23.447 -49.699 1.00 48.62 ? 107 THR B N 1 ATOM 3396 C CA . THR B 2 107 ? 43.077 -23.008 -50.296 1.00 45.80 ? 107 THR B CA 1 ATOM 3397 C C . THR B 2 107 ? 43.352 -22.193 -51.569 1.00 44.78 ? 107 THR B C 1 ATOM 3398 O O . THR B 2 107 ? 42.713 -22.410 -52.596 1.00 42.06 ? 107 THR B O 1 ATOM 3399 C CB . THR B 2 107 ? 42.212 -22.227 -49.293 1.00 46.49 ? 107 THR B CB 1 ATOM 3400 O OG1 . THR B 2 107 ? 41.736 -23.125 -48.277 1.00 46.48 ? 107 THR B OG1 1 ATOM 3401 C CG2 . THR B 2 107 ? 41.005 -21.576 -49.996 1.00 47.15 ? 107 THR B CG2 1 ATOM 3402 N N . LEU B 2 108 ? 44.321 -21.287 -51.514 1.00 42.99 ? 108 LEU B N 1 ATOM 3403 C CA . LEU B 2 108 ? 44.659 -20.501 -52.689 1.00 43.73 ? 108 LEU B CA 1 ATOM 3404 C C . LEU B 2 108 ? 45.190 -21.381 -53.828 1.00 44.11 ? 108 LEU B C 1 ATOM 3405 O O . LEU B 2 108 ? 44.764 -21.237 -54.975 1.00 43.19 ? 108 LEU B O 1 ATOM 3406 C CB . LEU B 2 108 ? 45.662 -19.412 -52.336 1.00 44.66 ? 108 LEU B CB 1 ATOM 3407 C CG . LEU B 2 108 ? 45.193 -18.421 -51.258 1.00 47.21 ? 108 LEU B CG 1 ATOM 3408 C CD1 . LEU B 2 108 ? 46.236 -17.332 -51.083 1.00 48.87 ? 108 LEU B CD1 1 ATOM 3409 C CD2 . LEU B 2 108 ? 43.831 -17.807 -51.560 1.00 47.84 ? 108 LEU B CD2 1 ATOM 3410 N N . ASP B 2 109 ? 46.112 -22.288 -53.505 1.00 44.64 ? 109 ASP B N 1 ATOM 3411 C CA . ASP B 2 109 ? 46.617 -23.264 -54.471 1.00 44.85 ? 109 ASP B CA 1 ATOM 3412 C C . ASP B 2 109 ? 45.503 -24.160 -55.067 1.00 44.91 ? 109 ASP B C 1 ATOM 3413 O O . ASP B 2 109 ? 45.558 -24.521 -56.238 1.00 47.92 ? 109 ASP B O 1 ATOM 3414 C CB . ASP B 2 109 ? 47.675 -24.154 -53.819 1.00 47.10 ? 109 ASP B CB 1 ATOM 3415 C CG . ASP B 2 109 ? 48.978 -23.400 -53.459 1.00 49.94 ? 109 ASP B CG 1 ATOM 3416 O OD1 . ASP B 2 109 ? 49.368 -22.451 -54.170 1.00 49.64 ? 109 ASP B OD1 1 ATOM 3417 O OD2 . ASP B 2 109 ? 49.637 -23.811 -52.466 1.00 53.75 ? 109 ASP B OD2 1 ATOM 3418 N N . PHE B 2 110 ? 44.510 -24.525 -54.256 1.00 43.08 ? 110 PHE B N 1 ATOM 3419 C CA . PHE B 2 110 ? 43.396 -25.384 -54.683 1.00 42.09 ? 110 PHE B CA 1 ATOM 3420 C C . PHE B 2 110 ? 42.598 -24.724 -55.802 1.00 42.15 ? 110 PHE B C 1 ATOM 3421 O O . PHE B 2 110 ? 42.312 -25.344 -56.823 1.00 42.69 ? 110 PHE B O 1 ATOM 3422 C CB . PHE B 2 110 ? 42.514 -25.678 -53.465 1.00 42.76 ? 110 PHE B CB 1 ATOM 3423 C CG . PHE B 2 110 ? 41.248 -26.431 -53.766 1.00 43.96 ? 110 PHE B CG 1 ATOM 3424 C CD1 . PHE B 2 110 ? 41.281 -27.677 -54.369 1.00 45.23 ? 110 PHE B CD1 1 ATOM 3425 C CD2 . PHE B 2 110 ? 40.020 -25.913 -53.390 1.00 44.17 ? 110 PHE B CD2 1 ATOM 3426 C CE1 . PHE B 2 110 ? 40.111 -28.372 -54.624 1.00 47.45 ? 110 PHE B CE1 1 ATOM 3427 C CE2 . PHE B 2 110 ? 38.842 -26.607 -53.646 1.00 46.71 ? 110 PHE B CE2 1 ATOM 3428 C CZ . PHE B 2 110 ? 38.887 -27.838 -54.265 1.00 48.00 ? 110 PHE B CZ 1 ATOM 3429 N N . HIS B 2 111 ? 42.264 -23.452 -55.606 1.00 41.93 ? 111 HIS B N 1 ATOM 3430 C CA . HIS B 2 111 ? 41.616 -22.644 -56.630 1.00 42.53 ? 111 HIS B CA 1 ATOM 3431 C C . HIS B 2 111 ? 42.450 -22.553 -57.918 1.00 42.58 ? 111 HIS B C 1 ATOM 3432 O O . HIS B 2 111 ? 41.917 -22.672 -59.028 1.00 43.30 ? 111 HIS B O 1 ATOM 3433 C CB . HIS B 2 111 ? 41.360 -21.229 -56.103 1.00 42.96 ? 111 HIS B CB 1 ATOM 3434 C CG . HIS B 2 111 ? 40.260 -21.142 -55.092 1.00 43.36 ? 111 HIS B CG 1 ATOM 3435 N ND1 . HIS B 2 111 ? 38.951 -21.451 -55.391 1.00 44.89 ? 111 HIS B ND1 1 ATOM 3436 C CD2 . HIS B 2 111 ? 40.270 -20.746 -53.797 1.00 43.17 ? 111 HIS B CD2 1 ATOM 3437 C CE1 . HIS B 2 111 ? 38.203 -21.265 -54.318 1.00 46.51 ? 111 HIS B CE1 1 ATOM 3438 N NE2 . HIS B 2 111 ? 38.979 -20.834 -53.338 1.00 45.37 ? 111 HIS B NE2 1 ATOM 3439 N N . ASP B 2 112 ? 43.750 -22.326 -57.757 1.00 41.12 ? 112 ASP B N 1 ATOM 3440 C CA . ASP B 2 112 ? 44.678 -22.259 -58.874 1.00 41.03 ? 112 ASP B CA 1 ATOM 3441 C C . ASP B 2 112 ? 44.610 -23.581 -59.658 1.00 42.39 ? 112 ASP B C 1 ATOM 3442 O O . ASP B 2 112 ? 44.488 -23.594 -60.882 1.00 43.74 ? 112 ASP B O 1 ATOM 3443 C CB . ASP B 2 112 ? 46.089 -22.010 -58.327 1.00 41.56 ? 112 ASP B CB 1 ATOM 3444 C CG . ASP B 2 112 ? 47.079 -21.596 -59.396 1.00 44.04 ? 112 ASP B CG 1 ATOM 3445 O OD1 . ASP B 2 112 ? 46.665 -21.259 -60.534 1.00 44.93 ? 112 ASP B OD1 1 ATOM 3446 O OD2 . ASP B 2 112 ? 48.294 -21.607 -59.089 1.00 45.89 ? 112 ASP B OD2 1 ATOM 3447 N N . SER B 2 113 ? 44.655 -24.693 -58.933 1.00 42.11 ? 113 SER B N 1 ATOM 3448 C CA . SER B 2 113 ? 44.525 -26.017 -59.522 1.00 42.57 ? 113 SER B CA 1 ATOM 3449 C C . SER B 2 113 ? 43.218 -26.215 -60.290 1.00 43.29 ? 113 SER B C 1 ATOM 3450 O O . SER B 2 113 ? 43.209 -26.784 -61.392 1.00 43.90 ? 113 SER B O 1 ATOM 3451 C CB . SER B 2 113 ? 44.604 -27.070 -58.422 1.00 42.83 ? 113 SER B CB 1 ATOM 3452 O OG . SER B 2 113 ? 44.320 -28.349 -58.933 1.00 44.91 ? 113 SER B OG 1 ATOM 3453 N N . ASN B 2 114 ? 42.109 -25.785 -59.702 1.00 42.12 ? 114 ASN B N 1 ATOM 3454 C CA . ASN B 2 114 ? 40.820 -25.953 -60.367 1.00 42.96 ? 114 ASN B CA 1 ATOM 3455 C C . ASN B 2 114 ? 40.771 -25.193 -61.690 1.00 42.62 ? 114 ASN B C 1 ATOM 3456 O O . ASN B 2 114 ? 40.184 -25.677 -62.651 1.00 43.01 ? 114 ASN B O 1 ATOM 3457 C CB . ASN B 2 114 ? 39.674 -25.523 -59.461 1.00 43.09 ? 114 ASN B CB 1 ATOM 3458 C CG . ASN B 2 114 ? 39.526 -26.416 -58.256 1.00 44.12 ? 114 ASN B CG 1 ATOM 3459 O OD1 . ASN B 2 114 ? 39.764 -27.623 -58.327 1.00 45.32 ? 114 ASN B OD1 1 ATOM 3460 N ND2 . ASN B 2 114 ? 39.130 -25.832 -57.138 1.00 44.45 ? 114 ASN B ND2 1 ATOM 3461 N N . VAL B 2 115 ? 41.419 -24.026 -61.745 1.00 42.16 ? 115 VAL B N 1 ATOM 3462 C CA . VAL B 2 115 ? 41.446 -23.220 -62.969 1.00 42.89 ? 115 VAL B CA 1 ATOM 3463 C C . VAL B 2 115 ? 42.317 -23.892 -64.022 1.00 43.68 ? 115 VAL B C 1 ATOM 3464 O O . VAL B 2 115 ? 41.933 -23.985 -65.183 1.00 44.38 ? 115 VAL B O 1 ATOM 3465 C CB . VAL B 2 115 ? 41.977 -21.792 -62.712 1.00 43.38 ? 115 VAL B CB 1 ATOM 3466 C CG1 . VAL B 2 115 ? 42.172 -21.047 -64.025 1.00 44.82 ? 115 VAL B CG1 1 ATOM 3467 C CG2 . VAL B 2 115 ? 41.025 -21.012 -61.821 1.00 44.13 ? 115 VAL B CG2 1 ATOM 3468 N N . LYS B 2 116 ? 43.495 -24.348 -63.604 1.00 44.42 ? 116 LYS B N 1 ATOM 3469 C CA . LYS B 2 116 ? 44.415 -25.042 -64.488 1.00 45.76 ? 116 LYS B CA 1 ATOM 3470 C C . LYS B 2 116 ? 43.760 -26.271 -65.108 1.00 46.49 ? 116 LYS B C 1 ATOM 3471 O O . LYS B 2 116 ? 43.881 -26.504 -66.306 1.00 45.89 ? 116 LYS B O 1 ATOM 3472 C CB . LYS B 2 116 ? 45.675 -25.424 -63.708 1.00 48.14 ? 116 LYS B CB 1 ATOM 3473 C CG . LYS B 2 116 ? 46.731 -26.214 -64.462 1.00 50.67 ? 116 LYS B CG 1 ATOM 3474 C CD . LYS B 2 116 ? 47.155 -25.505 -65.732 1.00 54.23 ? 116 LYS B CD 1 ATOM 3475 C CE . LYS B 2 116 ? 48.467 -26.066 -66.267 1.00 58.90 ? 116 LYS B CE 1 ATOM 3476 N NZ . LYS B 2 116 ? 49.628 -25.475 -65.548 1.00 60.90 ? 116 LYS B NZ 1 ATOM 3477 N N . ASN B 2 117 ? 43.042 -27.041 -64.298 1.00 47.58 ? 117 ASN B N 1 ATOM 3478 C CA . ASN B 2 117 ? 42.391 -28.256 -64.793 1.00 50.86 ? 117 ASN B CA 1 ATOM 3479 C C . ASN B 2 117 ? 41.243 -27.954 -65.750 1.00 52.04 ? 117 ASN B C 1 ATOM 3480 O O . ASN B 2 117 ? 41.018 -28.691 -66.712 1.00 53.77 ? 117 ASN B O 1 ATOM 3481 C CB . ASN B 2 117 ? 41.905 -29.128 -63.631 1.00 51.87 ? 117 ASN B CB 1 ATOM 3482 C CG . ASN B 2 117 ? 43.050 -29.691 -62.808 1.00 53.53 ? 117 ASN B CG 1 ATOM 3483 O OD1 . ASN B 2 117 ? 44.173 -29.832 -63.290 1.00 54.73 ? 117 ASN B OD1 1 ATOM 3484 N ND2 . ASN B 2 117 ? 42.772 -30.008 -61.558 1.00 55.08 ? 117 ASN B ND2 1 ATOM 3485 N N . LEU B 2 118 ? 40.519 -26.873 -65.494 1.00 51.32 ? 118 LEU B N 1 ATOM 3486 C CA . LEU B 2 118 ? 39.445 -26.470 -66.388 1.00 52.54 ? 118 LEU B CA 1 ATOM 3487 C C . LEU B 2 118 ? 40.036 -26.025 -67.715 1.00 52.61 ? 118 LEU B C 1 ATOM 3488 O O . LEU B 2 118 ? 39.524 -26.361 -68.783 1.00 55.95 ? 118 LEU B O 1 ATOM 3489 C CB . LEU B 2 118 ? 38.633 -25.349 -65.760 1.00 53.36 ? 118 LEU B CB 1 ATOM 3490 C CG . LEU B 2 118 ? 37.415 -24.856 -66.518 1.00 54.45 ? 118 LEU B CG 1 ATOM 3491 C CD1 . LEU B 2 118 ? 36.431 -25.989 -66.747 1.00 58.43 ? 118 LEU B CD1 1 ATOM 3492 C CD2 . LEU B 2 118 ? 36.778 -23.736 -65.721 1.00 54.58 ? 118 LEU B CD2 1 ATOM 3493 N N . TYR B 2 119 ? 41.139 -25.293 -67.651 1.00 50.64 ? 119 TYR B N 1 ATOM 3494 C CA . TYR B 2 119 ? 41.834 -24.884 -68.861 1.00 50.13 ? 119 TYR B CA 1 ATOM 3495 C C . TYR B 2 119 ? 42.322 -26.099 -69.656 1.00 52.39 ? 119 TYR B C 1 ATOM 3496 O O . TYR B 2 119 ? 42.142 -26.161 -70.871 1.00 53.76 ? 119 TYR B O 1 ATOM 3497 C CB . TYR B 2 119 ? 42.996 -23.953 -68.517 1.00 48.53 ? 119 TYR B CB 1 ATOM 3498 C CG . TYR B 2 119 ? 43.826 -23.541 -69.705 1.00 49.90 ? 119 TYR B CG 1 ATOM 3499 C CD1 . TYR B 2 119 ? 43.412 -22.504 -70.546 1.00 50.11 ? 119 TYR B CD1 1 ATOM 3500 C CD2 . TYR B 2 119 ? 45.031 -24.176 -69.989 1.00 50.71 ? 119 TYR B CD2 1 ATOM 3501 C CE1 . TYR B 2 119 ? 44.172 -22.120 -71.639 1.00 50.88 ? 119 TYR B CE1 1 ATOM 3502 C CE2 . TYR B 2 119 ? 45.798 -23.794 -71.076 1.00 52.16 ? 119 TYR B CE2 1 ATOM 3503 C CZ . TYR B 2 119 ? 45.360 -22.772 -71.897 1.00 53.26 ? 119 TYR B CZ 1 ATOM 3504 O OH . TYR B 2 119 ? 46.117 -22.396 -72.974 1.00 55.81 ? 119 TYR B OH 1 ATOM 3505 N N . ASP B 2 120 ? 42.933 -27.067 -68.984 1.00 53.59 ? 120 ASP B N 1 ATOM 3506 C CA . ASP B 2 120 ? 43.418 -28.256 -69.685 1.00 57.26 ? 120 ASP B CA 1 ATOM 3507 C C . ASP B 2 120 ? 42.261 -29.055 -70.302 1.00 57.81 ? 120 ASP B C 1 ATOM 3508 O O . ASP B 2 120 ? 42.350 -29.497 -71.440 1.00 58.88 ? 120 ASP B O 1 ATOM 3509 C CB . ASP B 2 120 ? 44.288 -29.131 -68.765 1.00 59.42 ? 120 ASP B CB 1 ATOM 3510 C CG . ASP B 2 120 ? 45.637 -28.487 -68.445 1.00 60.51 ? 120 ASP B CG 1 ATOM 3511 O OD1 . ASP B 2 120 ? 46.174 -27.758 -69.311 1.00 62.56 ? 120 ASP B OD1 1 ATOM 3512 O OD2 . ASP B 2 120 ? 46.170 -28.706 -67.330 1.00 60.84 ? 120 ASP B OD2 1 ATOM 3513 N N . LYS B 2 121 ? 41.175 -29.211 -69.557 1.00 59.10 ? 121 LYS B N 1 ATOM 3514 C CA . LYS B 2 121 ? 39.956 -29.872 -70.054 1.00 64.14 ? 121 LYS B CA 1 ATOM 3515 C C . LYS B 2 121 ? 39.515 -29.341 -71.420 1.00 63.64 ? 121 LYS B C 1 ATOM 3516 O O . LYS B 2 121 ? 39.180 -30.106 -72.312 1.00 67.04 ? 121 LYS B O 1 ATOM 3517 C CB . LYS B 2 121 ? 38.828 -29.654 -69.043 1.00 66.68 ? 121 LYS B CB 1 ATOM 3518 C CG . LYS B 2 121 ? 37.533 -30.408 -69.289 1.00 71.50 ? 121 LYS B CG 1 ATOM 3519 C CD . LYS B 2 121 ? 36.521 -30.024 -68.210 1.00 74.13 ? 121 LYS B CD 1 ATOM 3520 C CE . LYS B 2 121 ? 35.377 -31.019 -68.087 1.00 80.50 ? 121 LYS B CE 1 ATOM 3521 N NZ . LYS B 2 121 ? 34.409 -30.902 -69.214 1.00 85.99 ? 121 LYS B NZ 1 ATOM 3522 N N . VAL B 2 122 ? 39.520 -28.022 -71.567 1.00 60.40 ? 122 VAL B N 1 ATOM 3523 C CA . VAL B 2 122 ? 39.147 -27.374 -72.810 1.00 59.32 ? 122 VAL B CA 1 ATOM 3524 C C . VAL B 2 122 ? 40.227 -27.554 -73.875 1.00 61.52 ? 122 VAL B C 1 ATOM 3525 O O . VAL B 2 122 ? 39.919 -27.844 -75.037 1.00 62.26 ? 122 VAL B O 1 ATOM 3526 C CB . VAL B 2 122 ? 38.853 -25.882 -72.571 1.00 57.03 ? 122 VAL B CB 1 ATOM 3527 C CG1 . VAL B 2 122 ? 38.753 -25.107 -73.882 1.00 57.02 ? 122 VAL B CG1 1 ATOM 3528 C CG2 . VAL B 2 122 ? 37.574 -25.745 -71.755 1.00 56.99 ? 122 VAL B CG2 1 ATOM 3529 N N . ARG B 2 123 ? 41.484 -27.382 -73.488 1.00 60.58 ? 123 ARG B N 1 ATOM 3530 C CA . ARG B 2 123 ? 42.595 -27.597 -74.410 1.00 63.35 ? 123 ARG B CA 1 ATOM 3531 C C . ARG B 2 123 ? 42.530 -29.003 -75.025 1.00 67.09 ? 123 ARG B C 1 ATOM 3532 O O . ARG B 2 123 ? 42.656 -29.165 -76.244 1.00 68.36 ? 123 ARG B O 1 ATOM 3533 C CB . ARG B 2 123 ? 43.919 -27.405 -73.678 1.00 64.82 ? 123 ARG B CB 1 ATOM 3534 C CG . ARG B 2 123 ? 45.139 -27.435 -74.576 1.00 67.96 ? 123 ARG B CG 1 ATOM 3535 C CD . ARG B 2 123 ? 46.410 -27.222 -73.773 1.00 69.96 ? 123 ARG B CD 1 ATOM 3536 N NE . ARG B 2 123 ? 46.530 -28.132 -72.629 1.00 70.94 ? 123 ARG B NE 1 ATOM 3537 C CZ . ARG B 2 123 ? 46.900 -29.412 -72.704 1.00 73.84 ? 123 ARG B CZ 1 ATOM 3538 N NH1 . ARG B 2 123 ? 47.182 -29.982 -73.876 1.00 76.41 ? 123 ARG B NH1 1 ATOM 3539 N NH2 . ARG B 2 123 ? 46.983 -30.133 -71.593 1.00 73.81 ? 123 ARG B NH2 1 ATOM 3540 N N . LEU B 2 124 ? 42.307 -30.005 -74.175 1.00 68.47 ? 124 LEU B N 1 ATOM 3541 C CA . LEU B 2 124 ? 42.226 -31.407 -74.603 1.00 72.73 ? 124 LEU B CA 1 ATOM 3542 C C . LEU B 2 124 ? 41.040 -31.725 -75.538 1.00 75.15 ? 124 LEU B C 1 ATOM 3543 O O . LEU B 2 124 ? 41.068 -32.732 -76.246 1.00 78.55 ? 124 LEU B O 1 ATOM 3544 C CB . LEU B 2 124 ? 42.184 -32.329 -73.379 1.00 74.10 ? 124 LEU B CB 1 ATOM 3545 C CG . LEU B 2 124 ? 43.457 -32.330 -72.515 1.00 75.40 ? 124 LEU B CG 1 ATOM 3546 C CD1 . LEU B 2 124 ? 43.215 -32.908 -71.114 1.00 75.85 ? 124 LEU B CD1 1 ATOM 3547 C CD2 . LEU B 2 124 ? 44.584 -33.071 -73.222 1.00 78.70 ? 124 LEU B CD2 1 ATOM 3548 N N . GLN B 2 125 ? 40.001 -30.890 -75.533 1.00 73.76 ? 125 GLN B N 1 ATOM 3549 C CA . GLN B 2 125 ? 38.887 -31.048 -76.475 1.00 75.35 ? 125 GLN B CA 1 ATOM 3550 C C . GLN B 2 125 ? 39.223 -30.422 -77.814 1.00 74.45 ? 125 GLN B C 1 ATOM 3551 O O . GLN B 2 125 ? 39.083 -31.055 -78.857 1.00 79.49 ? 125 GLN B O 1 ATOM 3552 C CB . GLN B 2 125 ? 37.618 -30.392 -75.950 1.00 75.07 ? 125 GLN B CB 1 ATOM 3553 C CG . GLN B 2 125 ? 37.006 -31.066 -74.741 1.00 77.46 ? 125 GLN B CG 1 ATOM 3554 C CD . GLN B 2 125 ? 35.698 -30.415 -74.350 1.00 78.40 ? 125 GLN B CD 1 ATOM 3555 O OE1 . GLN B 2 125 ? 34.681 -30.621 -75.004 1.00 82.50 ? 125 GLN B OE1 1 ATOM 3556 N NE2 . GLN B 2 125 ? 35.719 -29.613 -73.292 1.00 76.92 ? 125 GLN B NE2 1 ATOM 3557 N N . LEU B 2 126 ? 39.666 -29.174 -77.773 1.00 71.84 ? 126 LEU B N 1 ATOM 3558 C CA . LEU B 2 126 ? 39.932 -28.411 -78.982 1.00 73.46 ? 126 LEU B CA 1 ATOM 3559 C C . LEU B 2 126 ? 41.108 -28.961 -79.772 1.00 77.82 ? 126 LEU B C 1 ATOM 3560 O O . LEU B 2 126 ? 41.059 -29.002 -80.994 1.00 81.88 ? 126 LEU B O 1 ATOM 3561 C CB . LEU B 2 126 ? 40.157 -26.931 -78.651 1.00 69.58 ? 126 LEU B CB 1 ATOM 3562 C CG . LEU B 2 126 ? 38.980 -26.243 -77.951 1.00 66.85 ? 126 LEU B CG 1 ATOM 3563 C CD1 . LEU B 2 126 ? 39.219 -24.748 -77.829 1.00 64.60 ? 126 LEU B CD1 1 ATOM 3564 C CD2 . LEU B 2 126 ? 37.680 -26.522 -78.685 1.00 69.25 ? 126 LEU B CD2 1 ATOM 3565 N N . ARG B 2 127 ? 42.156 -29.386 -79.078 1.00 84.15 ? 127 ARG B N 1 ATOM 3566 C CA . ARG B 2 127 ? 43.337 -29.962 -79.730 1.00 89.33 ? 127 ARG B CA 1 ATOM 3567 C C . ARG B 2 127 ? 43.896 -28.996 -80.797 1.00 89.17 ? 127 ARG B C 1 ATOM 3568 O O . ARG B 2 127 ? 44.298 -27.884 -80.454 1.00 88.22 ? 127 ARG B O 1 ATOM 3569 C CB . ARG B 2 127 ? 43.016 -31.366 -80.283 1.00 94.69 ? 127 ARG B CB 1 ATOM 3570 C CG . ARG B 2 127 ? 42.786 -32.410 -79.191 1.00 96.57 ? 127 ARG B CG 1 ATOM 3571 C CD . ARG B 2 127 ? 41.796 -33.494 -79.596 1.00 99.59 ? 127 ARG B CD 1 ATOM 3572 N NE . ARG B 2 127 ? 42.259 -34.296 -80.724 1.00 105.03 ? 127 ARG B NE 1 ATOM 3573 C CZ . ARG B 2 127 ? 41.582 -35.316 -81.256 1.00 110.84 ? 127 ARG B CZ 1 ATOM 3574 N NH1 . ARG B 2 127 ? 40.399 -35.670 -80.764 1.00 112.73 ? 127 ARG B NH1 1 ATOM 3575 N NH2 . ARG B 2 127 ? 42.092 -35.990 -82.283 1.00 113.55 ? 127 ARG B NH2 1 ATOM 3576 N N . ASP B 2 128 ? 43.901 -29.386 -82.071 1.00 90.30 ? 128 ASP B N 1 ATOM 3577 C CA . ASP B 2 128 ? 44.491 -28.538 -83.114 1.00 90.86 ? 128 ASP B CA 1 ATOM 3578 C C . ASP B 2 128 ? 43.455 -27.784 -83.969 1.00 87.80 ? 128 ASP B C 1 ATOM 3579 O O . ASP B 2 128 ? 43.796 -27.240 -85.013 1.00 90.08 ? 128 ASP B O 1 ATOM 3580 C CB . ASP B 2 128 ? 45.451 -29.354 -83.996 1.00 96.37 ? 128 ASP B CB 1 ATOM 3581 C CG . ASP B 2 128 ? 44.784 -30.549 -84.655 1.00 100.90 ? 128 ASP B CG 1 ATOM 3582 O OD1 . ASP B 2 128 ? 43.546 -30.693 -84.562 1.00 99.96 ? 128 ASP B OD1 1 ATOM 3583 O OD2 . ASP B 2 128 ? 45.512 -31.355 -85.268 1.00 109.76 ? 128 ASP B OD2 1 ATOM 3584 N N . ASN B 2 129 ? 42.201 -27.747 -83.520 1.00 84.76 ? 129 ASN B N 1 ATOM 3585 C CA . ASN B 2 129 ? 41.168 -26.927 -84.162 1.00 82.41 ? 129 ASN B CA 1 ATOM 3586 C C . ASN B 2 129 ? 41.143 -25.469 -83.670 1.00 79.46 ? 129 ASN B C 1 ATOM 3587 O O . ASN B 2 129 ? 40.251 -24.707 -84.056 1.00 79.61 ? 129 ASN B O 1 ATOM 3588 C CB . ASN B 2 129 ? 39.781 -27.555 -83.961 1.00 84.29 ? 129 ASN B CB 1 ATOM 3589 C CG . ASN B 2 129 ? 39.603 -28.857 -84.726 1.00 89.58 ? 129 ASN B CG 1 ATOM 3590 O OD1 . ASN B 2 129 ? 40.561 -29.420 -85.259 1.00 96.29 ? 129 ASN B OD1 1 ATOM 3591 N ND2 . ASN B 2 129 ? 38.370 -29.346 -84.776 1.00 89.08 ? 129 ASN B ND2 1 ATOM 3592 N N . ALA B 2 130 ? 42.112 -25.077 -82.836 1.00 76.60 ? 130 ALA B N 1 ATOM 3593 C CA . ALA B 2 130 ? 42.196 -23.702 -82.324 1.00 74.03 ? 130 ALA B CA 1 ATOM 3594 C C . ALA B 2 130 ? 43.630 -23.329 -81.964 1.00 73.70 ? 130 ALA B C 1 ATOM 3595 O O . ALA B 2 130 ? 44.427 -24.201 -81.663 1.00 75.03 ? 130 ALA B O 1 ATOM 3596 C CB . ALA B 2 130 ? 41.302 -23.546 -81.104 1.00 72.08 ? 130 ALA B CB 1 ATOM 3597 N N . LYS B 2 131 ? 43.947 -22.034 -81.991 1.00 74.16 ? 131 LYS B N 1 ATOM 3598 C CA . LYS B 2 131 ? 45.266 -21.546 -81.579 1.00 75.97 ? 131 LYS B CA 1 ATOM 3599 C C . LYS B 2 131 ? 45.296 -21.255 -80.083 1.00 72.68 ? 131 LYS B C 1 ATOM 3600 O O . LYS B 2 131 ? 44.504 -20.464 -79.580 1.00 71.02 ? 131 LYS B O 1 ATOM 3601 C CB . LYS B 2 131 ? 45.648 -20.277 -82.341 1.00 81.45 ? 131 LYS B CB 1 ATOM 3602 C CG . LYS B 2 131 ? 45.803 -20.495 -83.837 1.00 89.96 ? 131 LYS B CG 1 ATOM 3603 C CD . LYS B 2 131 ? 46.624 -19.400 -84.519 1.00 98.71 ? 131 LYS B CD 1 ATOM 3604 C CE . LYS B 2 131 ? 47.448 -19.943 -85.693 1.00 104.50 ? 131 LYS B CE 1 ATOM 3605 N NZ . LYS B 2 131 ? 48.734 -19.214 -85.904 1.00 107.38 ? 131 LYS B NZ 1 ATOM 3606 N N . GLU B 2 132 ? 46.218 -21.892 -79.373 1.00 70.65 ? 132 GLU B N 1 ATOM 3607 C CA . GLU B 2 132 ? 46.419 -21.611 -77.963 1.00 66.94 ? 132 GLU B CA 1 ATOM 3608 C C . GLU B 2 132 ? 47.204 -20.303 -77.840 1.00 67.66 ? 132 GLU B C 1 ATOM 3609 O O . GLU B 2 132 ? 48.394 -20.267 -78.126 1.00 70.32 ? 132 GLU B O 1 ATOM 3610 C CB . GLU B 2 132 ? 47.162 -22.768 -77.314 1.00 66.62 ? 132 GLU B CB 1 ATOM 3611 C CG . GLU B 2 132 ? 47.172 -22.716 -75.806 1.00 65.28 ? 132 GLU B CG 1 ATOM 3612 C CD . GLU B 2 132 ? 47.835 -23.919 -75.165 1.00 67.12 ? 132 GLU B CD 1 ATOM 3613 O OE1 . GLU B 2 132 ? 48.458 -24.746 -75.879 1.00 69.76 ? 132 GLU B OE1 1 ATOM 3614 O OE2 . GLU B 2 132 ? 47.729 -24.028 -73.924 1.00 66.41 ? 132 GLU B OE2 1 ATOM 3615 N N . LEU B 2 133 ? 46.532 -19.229 -77.427 1.00 65.99 ? 133 LEU B N 1 ATOM 3616 C CA . LEU B 2 133 ? 47.124 -17.885 -77.467 1.00 66.54 ? 133 LEU B CA 1 ATOM 3617 C C . LEU B 2 133 ? 48.161 -17.607 -76.385 1.00 68.39 ? 133 LEU B C 1 ATOM 3618 O O . LEU B 2 133 ? 49.004 -16.730 -76.560 1.00 71.33 ? 133 LEU B O 1 ATOM 3619 C CB . LEU B 2 133 ? 46.030 -16.819 -77.390 1.00 66.34 ? 133 LEU B CB 1 ATOM 3620 C CG . LEU B 2 133 ? 45.093 -16.706 -78.600 1.00 66.22 ? 133 LEU B CG 1 ATOM 3621 C CD1 . LEU B 2 133 ? 44.120 -15.565 -78.383 1.00 66.53 ? 133 LEU B CD1 1 ATOM 3622 C CD2 . LEU B 2 133 ? 45.872 -16.492 -79.891 1.00 68.36 ? 133 LEU B CD2 1 ATOM 3623 N N . GLY B 2 134 ? 48.082 -18.328 -75.267 1.00 66.60 ? 134 GLY B N 1 ATOM 3624 C CA . GLY B 2 134 ? 49.056 -18.197 -74.179 1.00 67.20 ? 134 GLY B CA 1 ATOM 3625 C C . GLY B 2 134 ? 48.578 -17.386 -72.986 1.00 66.01 ? 134 GLY B C 1 ATOM 3626 O O . GLY B 2 134 ? 49.353 -17.121 -72.070 1.00 65.96 ? 134 GLY B O 1 ATOM 3627 N N . ASN B 2 135 ? 47.300 -17.008 -72.981 1.00 64.12 ? 135 ASN B N 1 ATOM 3628 C CA . ASN B 2 135 ? 46.760 -16.110 -71.952 1.00 63.45 ? 135 ASN B CA 1 ATOM 3629 C C . ASN B 2 135 ? 45.440 -16.607 -71.340 1.00 60.04 ? 135 ASN B C 1 ATOM 3630 O O . ASN B 2 135 ? 44.716 -15.842 -70.699 1.00 59.36 ? 135 ASN B O 1 ATOM 3631 C CB . ASN B 2 135 ? 46.552 -14.724 -72.559 1.00 65.29 ? 135 ASN B CB 1 ATOM 3632 C CG . ASN B 2 135 ? 45.549 -14.738 -73.694 1.00 65.88 ? 135 ASN B CG 1 ATOM 3633 O OD1 . ASN B 2 135 ? 45.122 -15.798 -74.145 1.00 64.48 ? 135 ASN B OD1 1 ATOM 3634 N ND2 . ASN B 2 135 ? 45.179 -13.566 -74.169 1.00 68.90 ? 135 ASN B ND2 1 ATOM 3635 N N . GLY B 2 136 ? 45.135 -17.885 -71.538 1.00 57.15 ? 136 GLY B N 1 ATOM 3636 C CA . GLY B 2 136 ? 43.853 -18.441 -71.135 1.00 54.97 ? 136 GLY B CA 1 ATOM 3637 C C . GLY B 2 136 ? 42.869 -18.606 -72.280 1.00 54.05 ? 136 GLY B C 1 ATOM 3638 O O . GLY B 2 136 ? 41.832 -19.240 -72.104 1.00 52.77 ? 136 GLY B O 1 ATOM 3639 N N . CYS B 2 137 ? 43.199 -18.062 -73.452 1.00 56.07 ? 137 CYS B N 1 ATOM 3640 C CA . CYS B 2 137 ? 42.266 -18.011 -74.576 1.00 58.05 ? 137 CYS B CA 1 ATOM 3641 C C . CYS B 2 137 ? 42.660 -18.916 -75.742 1.00 58.82 ? 137 CYS B C 1 ATOM 3642 O O . CYS B 2 137 ? 43.836 -19.201 -75.970 1.00 59.14 ? 137 CYS B O 1 ATOM 3643 C CB . CYS B 2 137 ? 42.107 -16.576 -75.084 1.00 59.80 ? 137 CYS B CB 1 ATOM 3644 S SG . CYS B 2 137 ? 41.442 -15.411 -73.874 1.00 62.18 ? 137 CYS B SG 1 ATOM 3645 N N . PHE B 2 138 ? 41.637 -19.335 -76.482 1.00 59.33 ? 138 PHE B N 1 ATOM 3646 C CA . PHE B 2 138 ? 41.783 -20.188 -77.643 1.00 60.24 ? 138 PHE B CA 1 ATOM 3647 C C . PHE B 2 138 ? 41.094 -19.520 -78.815 1.00 62.66 ? 138 PHE B C 1 ATOM 3648 O O . PHE B 2 138 ? 39.907 -19.254 -78.754 1.00 63.46 ? 138 PHE B O 1 ATOM 3649 C CB . PHE B 2 138 ? 41.139 -21.551 -77.392 1.00 58.70 ? 138 PHE B CB 1 ATOM 3650 C CG . PHE B 2 138 ? 41.832 -22.359 -76.332 1.00 58.53 ? 138 PHE B CG 1 ATOM 3651 C CD1 . PHE B 2 138 ? 42.955 -23.120 -76.641 1.00 58.06 ? 138 PHE B CD1 1 ATOM 3652 C CD2 . PHE B 2 138 ? 41.367 -22.353 -75.017 1.00 57.81 ? 138 PHE B CD2 1 ATOM 3653 C CE1 . PHE B 2 138 ? 43.590 -23.867 -75.667 1.00 57.47 ? 138 PHE B CE1 1 ATOM 3654 C CE2 . PHE B 2 138 ? 42.006 -23.098 -74.038 1.00 57.02 ? 138 PHE B CE2 1 ATOM 3655 C CZ . PHE B 2 138 ? 43.122 -23.850 -74.364 1.00 57.15 ? 138 PHE B CZ 1 ATOM 3656 N N . GLU B 2 139 ? 41.839 -19.270 -79.885 1.00 65.65 ? 139 GLU B N 1 ATOM 3657 C CA . GLU B 2 139 ? 41.291 -18.671 -81.084 1.00 68.80 ? 139 GLU B CA 1 ATOM 3658 C C . GLU B 2 139 ? 40.959 -19.766 -82.098 1.00 68.86 ? 139 GLU B C 1 ATOM 3659 O O . GLU B 2 139 ? 41.836 -20.516 -82.530 1.00 70.63 ? 139 GLU B O 1 ATOM 3660 C CB . GLU B 2 139 ? 42.301 -17.689 -81.658 1.00 74.03 ? 139 GLU B CB 1 ATOM 3661 C CG . GLU B 2 139 ? 41.776 -16.818 -82.779 1.00 79.06 ? 139 GLU B CG 1 ATOM 3662 C CD . GLU B 2 139 ? 42.846 -15.881 -83.292 1.00 86.26 ? 139 GLU B CD 1 ATOM 3663 O OE1 . GLU B 2 139 ? 43.847 -16.375 -83.861 1.00 91.99 ? 139 GLU B OE1 1 ATOM 3664 O OE2 . GLU B 2 139 ? 42.704 -14.655 -83.100 1.00 92.41 ? 139 GLU B OE2 1 ATOM 3665 N N . PHE B 2 140 ? 39.687 -19.854 -82.470 1.00 68.84 ? 140 PHE B N 1 ATOM 3666 C CA . PHE B 2 140 ? 39.207 -20.900 -83.377 1.00 70.05 ? 140 PHE B CA 1 ATOM 3667 C C . PHE B 2 140 ? 39.642 -20.676 -84.828 1.00 72.74 ? 140 PHE B C 1 ATOM 3668 O O . PHE B 2 140 ? 39.765 -19.536 -85.274 1.00 72.66 ? 140 PHE B O 1 ATOM 3669 C CB . PHE B 2 140 ? 37.679 -20.982 -83.313 1.00 68.17 ? 140 PHE B CB 1 ATOM 3670 C CG . PHE B 2 140 ? 37.163 -21.522 -82.021 1.00 65.82 ? 140 PHE B CG 1 ATOM 3671 C CD1 . PHE B 2 140 ? 36.918 -20.680 -80.952 1.00 65.45 ? 140 PHE B CD1 1 ATOM 3672 C CD2 . PHE B 2 140 ? 36.932 -22.879 -81.869 1.00 66.63 ? 140 PHE B CD2 1 ATOM 3673 C CE1 . PHE B 2 140 ? 36.439 -21.176 -79.754 1.00 64.38 ? 140 PHE B CE1 1 ATOM 3674 C CE2 . PHE B 2 140 ? 36.457 -23.388 -80.674 1.00 66.11 ? 140 PHE B CE2 1 ATOM 3675 C CZ . PHE B 2 140 ? 36.212 -22.534 -79.614 1.00 65.76 ? 140 PHE B CZ 1 ATOM 3676 N N . TYR B 2 141 ? 39.873 -21.769 -85.557 1.00 76.39 ? 141 TYR B N 1 ATOM 3677 C CA . TYR B 2 141 ? 40.131 -21.690 -87.009 1.00 80.39 ? 141 TYR B CA 1 ATOM 3678 C C . TYR B 2 141 ? 38.828 -21.567 -87.791 1.00 79.46 ? 141 TYR B C 1 ATOM 3679 O O . TYR B 2 141 ? 38.767 -20.872 -88.802 1.00 85.32 ? 141 TYR B O 1 ATOM 3680 C CB . TYR B 2 141 ? 40.909 -22.908 -87.504 1.00 81.30 ? 141 TYR B CB 1 ATOM 3681 C CG . TYR B 2 141 ? 42.288 -22.992 -86.920 1.00 83.34 ? 141 TYR B CG 1 ATOM 3682 C CD1 . TYR B 2 141 ? 43.196 -21.943 -87.072 1.00 84.79 ? 141 TYR B CD1 1 ATOM 3683 C CD2 . TYR B 2 141 ? 42.688 -24.107 -86.195 1.00 84.70 ? 141 TYR B CD2 1 ATOM 3684 C CE1 . TYR B 2 141 ? 44.462 -22.012 -86.523 1.00 86.36 ? 141 TYR B CE1 1 ATOM 3685 C CE2 . TYR B 2 141 ? 43.953 -24.184 -85.645 1.00 85.17 ? 141 TYR B CE2 1 ATOM 3686 C CZ . TYR B 2 141 ? 44.834 -23.138 -85.812 1.00 87.01 ? 141 TYR B CZ 1 ATOM 3687 O OH . TYR B 2 141 ? 46.090 -23.240 -85.262 1.00 90.58 ? 141 TYR B OH 1 ATOM 3688 N N . HIS B 2 142 ? 37.796 -22.248 -87.310 1.00 106.49 ? 142 HIS B N 1 ATOM 3689 C CA . HIS B 2 142 ? 36.462 -22.161 -87.888 1.00 107.30 ? 142 HIS B CA 1 ATOM 3690 C C . HIS B 2 142 ? 35.641 -21.121 -87.136 1.00 101.98 ? 142 HIS B C 1 ATOM 3691 O O . HIS B 2 142 ? 36.027 -20.681 -86.052 1.00 96.72 ? 142 HIS B O 1 ATOM 3692 C CB . HIS B 2 142 ? 35.769 -23.527 -87.820 1.00 109.43 ? 142 HIS B CB 1 ATOM 3693 C CG . HIS B 2 142 ? 35.717 -24.114 -86.442 1.00 104.96 ? 142 HIS B CG 1 ATOM 3694 N ND1 . HIS B 2 142 ? 34.624 -23.976 -85.614 1.00 103.23 ? 142 HIS B ND1 1 ATOM 3695 C CD2 . HIS B 2 142 ? 36.628 -24.835 -85.746 1.00 102.74 ? 142 HIS B CD2 1 ATOM 3696 C CE1 . HIS B 2 142 ? 34.862 -24.591 -84.469 1.00 99.76 ? 142 HIS B CE1 1 ATOM 3697 N NE2 . HIS B 2 142 ? 36.072 -25.119 -84.523 1.00 99.44 ? 142 HIS B NE2 1 ATOM 3698 N N . LYS B 2 143 ? 34.517 -20.716 -87.718 1.00 104.06 ? 143 LYS B N 1 ATOM 3699 C CA . LYS B 2 143 ? 33.545 -19.912 -86.984 1.00 100.83 ? 143 LYS B CA 1 ATOM 3700 C C . LYS B 2 143 ? 32.944 -20.773 -85.891 1.00 96.38 ? 143 LYS B C 1 ATOM 3701 O O . LYS B 2 143 ? 32.653 -21.949 -86.115 1.00 98.71 ? 143 LYS B O 1 ATOM 3702 C CB . LYS B 2 143 ? 32.426 -19.405 -87.884 1.00 106.62 ? 143 LYS B CB 1 ATOM 3703 C CG . LYS B 2 143 ? 32.737 -18.099 -88.582 1.00 109.97 ? 143 LYS B CG 1 ATOM 3704 C CD . LYS B 2 143 ? 31.472 -17.499 -89.172 1.00 115.30 ? 143 LYS B CD 1 ATOM 3705 C CE . LYS B 2 143 ? 31.793 -16.366 -90.130 1.00 119.85 ? 143 LYS B CE 1 ATOM 3706 N NZ . LYS B 2 143 ? 32.284 -16.836 -91.452 1.00 126.19 ? 143 LYS B NZ 1 ATOM 3707 N N . CYS B 2 144 ? 32.770 -20.186 -84.712 1.00 89.38 ? 144 CYS B N 1 ATOM 3708 C CA . CYS B 2 144 ? 32.190 -20.893 -83.588 1.00 85.95 ? 144 CYS B CA 1 ATOM 3709 C C . CYS B 2 144 ? 31.026 -20.066 -83.053 1.00 84.96 ? 144 CYS B C 1 ATOM 3710 O O . CYS B 2 144 ? 31.221 -19.131 -82.277 1.00 82.00 ? 144 CYS B O 1 ATOM 3711 C CB . CYS B 2 144 ? 33.258 -21.135 -82.514 1.00 81.11 ? 144 CYS B CB 1 ATOM 3712 S SG . CYS B 2 144 ? 32.848 -22.379 -81.264 1.00 80.14 ? 144 CYS B SG 1 ATOM 3713 N N . ASP B 2 145 ? 29.817 -20.402 -83.497 1.00 88.38 ? 145 ASP B N 1 ATOM 3714 C CA . ASP B 2 145 ? 28.603 -19.711 -83.048 1.00 88.72 ? 145 ASP B CA 1 ATOM 3715 C C . ASP B 2 145 ? 28.238 -20.150 -81.623 1.00 85.19 ? 145 ASP B C 1 ATOM 3716 O O . ASP B 2 145 ? 28.958 -20.939 -81.015 1.00 82.89 ? 145 ASP B O 1 ATOM 3717 C CB . ASP B 2 145 ? 27.440 -19.921 -84.043 1.00 94.89 ? 145 ASP B CB 1 ATOM 3718 C CG . ASP B 2 145 ? 27.072 -21.389 -84.242 1.00 98.36 ? 145 ASP B CG 1 ATOM 3719 O OD1 . ASP B 2 145 ? 27.343 -22.220 -83.356 1.00 96.24 ? 145 ASP B OD1 1 ATOM 3720 O OD2 . ASP B 2 145 ? 26.491 -21.713 -85.296 1.00 104.98 ? 145 ASP B OD2 1 ATOM 3721 N N . ASN B 2 146 ? 27.131 -19.641 -81.090 1.00 85.69 ? 146 ASN B N 1 ATOM 3722 C CA . ASN B 2 146 ? 26.787 -19.888 -79.686 1.00 83.35 ? 146 ASN B CA 1 ATOM 3723 C C . ASN B 2 146 ? 26.572 -21.361 -79.340 1.00 85.97 ? 146 ASN B C 1 ATOM 3724 O O . ASN B 2 146 ? 26.922 -21.793 -78.241 1.00 83.77 ? 146 ASN B O 1 ATOM 3725 C CB . ASN B 2 146 ? 25.568 -19.063 -79.272 1.00 84.21 ? 146 ASN B CB 1 ATOM 3726 C CG . ASN B 2 146 ? 25.838 -17.565 -79.280 1.00 81.40 ? 146 ASN B CG 1 ATOM 3727 O OD1 . ASN B 2 146 ? 26.984 -17.106 -79.331 1.00 77.01 ? 146 ASN B OD1 1 ATOM 3728 N ND2 . ASN B 2 146 ? 24.771 -16.793 -79.218 1.00 83.89 ? 146 ASN B ND2 1 ATOM 3729 N N . GLU B 2 147 ? 26.019 -22.135 -80.270 1.00 92.33 ? 147 GLU B N 1 ATOM 3730 C CA . GLU B 2 147 ? 25.878 -23.585 -80.061 1.00 96.18 ? 147 GLU B CA 1 ATOM 3731 C C . GLU B 2 147 ? 27.245 -24.267 -80.084 1.00 92.28 ? 147 GLU B C 1 ATOM 3732 O O . GLU B 2 147 ? 27.496 -25.203 -79.326 1.00 92.65 ? 147 GLU B O 1 ATOM 3733 C CB . GLU B 2 147 ? 24.978 -24.231 -81.117 1.00 104.09 ? 147 GLU B CB 1 ATOM 3734 C CG . GLU B 2 147 ? 23.579 -23.643 -81.211 1.00 109.95 ? 147 GLU B CG 1 ATOM 3735 C CD . GLU B 2 147 ? 23.465 -22.597 -82.305 1.00 112.08 ? 147 GLU B CD 1 ATOM 3736 O OE1 . GLU B 2 147 ? 24.101 -21.526 -82.172 1.00 107.66 ? 147 GLU B OE1 1 ATOM 3737 O OE2 . GLU B 2 147 ? 22.748 -22.852 -83.298 1.00 118.34 ? 147 GLU B OE2 1 ATOM 3738 N N . CYS B 2 148 ? 28.118 -23.799 -80.971 1.00 89.95 ? 148 CYS B N 1 ATOM 3739 C CA . CYS B 2 148 ? 29.499 -24.261 -81.016 1.00 87.10 ? 148 CYS B CA 1 ATOM 3740 C C . CYS B 2 148 ? 30.179 -23.976 -79.664 1.00 80.56 ? 148 CYS B C 1 ATOM 3741 O O . CYS B 2 148 ? 30.749 -24.878 -79.047 1.00 78.89 ? 148 CYS B O 1 ATOM 3742 C CB . CYS B 2 148 ? 30.229 -23.588 -82.185 1.00 87.95 ? 148 CYS B CB 1 ATOM 3743 S SG . CYS B 2 148 ? 31.998 -23.918 -82.316 1.00 87.69 ? 148 CYS B SG 1 ATOM 3744 N N . MET B 2 149 ? 30.071 -22.736 -79.189 1.00 76.43 ? 149 MET B N 1 ATOM 3745 C CA . MET B 2 149 ? 30.603 -22.364 -77.875 1.00 72.02 ? 149 MET B CA 1 ATOM 3746 C C . MET B 2 149 ? 30.045 -23.240 -76.758 1.00 73.46 ? 149 MET B C 1 ATOM 3747 O O . MET B 2 149 ? 30.793 -23.714 -75.905 1.00 70.88 ? 149 MET B O 1 ATOM 3748 C CB . MET B 2 149 ? 30.302 -20.896 -77.558 1.00 69.82 ? 149 MET B CB 1 ATOM 3749 C CG . MET B 2 149 ? 31.019 -19.887 -78.442 1.00 68.62 ? 149 MET B CG 1 ATOM 3750 S SD . MET B 2 149 ? 32.812 -20.074 -78.443 1.00 66.11 ? 149 MET B SD 1 ATOM 3751 C CE . MET B 2 149 ? 33.304 -18.732 -79.524 1.00 66.38 ? 149 MET B CE 1 ATOM 3752 N N . GLU B 2 150 ? 28.734 -23.453 -76.764 1.00 78.72 ? 150 GLU B N 1 ATOM 3753 C CA . GLU B 2 150 ? 28.085 -24.257 -75.729 1.00 81.98 ? 150 GLU B CA 1 ATOM 3754 C C . GLU B 2 150 ? 28.650 -25.673 -75.674 1.00 83.40 ? 150 GLU B C 1 ATOM 3755 O O . GLU B 2 150 ? 28.837 -26.217 -74.585 1.00 82.98 ? 150 GLU B O 1 ATOM 3756 C CB . GLU B 2 150 ? 26.565 -24.283 -75.942 1.00 88.33 ? 150 GLU B CB 1 ATOM 3757 C CG . GLU B 2 150 ? 25.759 -25.073 -74.908 1.00 92.97 ? 150 GLU B CG 1 ATOM 3758 C CD . GLU B 2 150 ? 25.889 -24.553 -73.480 1.00 91.58 ? 150 GLU B CD 1 ATOM 3759 O OE1 . GLU B 2 150 ? 26.471 -23.468 -73.258 1.00 88.72 ? 150 GLU B OE1 1 ATOM 3760 O OE2 . GLU B 2 150 ? 25.398 -25.240 -72.561 1.00 95.13 ? 150 GLU B OE2 1 ATOM 3761 N N . SER B 2 151 ? 28.943 -26.254 -76.838 1.00 85.19 ? 151 SER B N 1 ATOM 3762 C CA . SER B 2 151 ? 29.498 -27.610 -76.902 1.00 88.22 ? 151 SER B CA 1 ATOM 3763 C C . SER B 2 151 ? 30.889 -27.697 -76.271 1.00 85.30 ? 151 SER B C 1 ATOM 3764 O O . SER B 2 151 ? 31.294 -28.758 -75.790 1.00 87.35 ? 151 SER B O 1 ATOM 3765 C CB . SER B 2 151 ? 29.563 -28.112 -78.347 1.00 91.50 ? 151 SER B CB 1 ATOM 3766 O OG . SER B 2 151 ? 30.641 -27.520 -79.049 1.00 88.26 ? 151 SER B OG 1 ATOM 3767 N N . VAL B 2 152 ? 31.624 -26.587 -76.288 1.00 82.05 ? 152 VAL B N 1 ATOM 3768 C CA . VAL B 2 152 ? 32.918 -26.521 -75.615 1.00 79.05 ? 152 VAL B CA 1 ATOM 3769 C C . VAL B 2 152 ? 32.693 -26.564 -74.107 1.00 79.48 ? 152 VAL B C 1 ATOM 3770 O O . VAL B 2 152 ? 33.328 -27.345 -73.406 1.00 79.27 ? 152 VAL B O 1 ATOM 3771 C CB . VAL B 2 152 ? 33.707 -25.254 -75.993 1.00 75.30 ? 152 VAL B CB 1 ATOM 3772 C CG1 . VAL B 2 152 ? 35.052 -25.230 -75.278 1.00 73.01 ? 152 VAL B CG1 1 ATOM 3773 C CG2 . VAL B 2 152 ? 33.900 -25.187 -77.501 1.00 76.81 ? 152 VAL B CG2 1 ATOM 3774 N N . ARG B 2 153 ? 31.768 -25.741 -73.621 1.00 80.82 ? 153 ARG B N 1 ATOM 3775 C CA . ARG B 2 153 ? 31.418 -25.740 -72.202 1.00 83.07 ? 153 ARG B CA 1 ATOM 3776 C C . ARG B 2 153 ? 30.787 -27.061 -71.775 1.00 90.10 ? 153 ARG B C 1 ATOM 3777 O O . ARG B 2 153 ? 30.930 -27.460 -70.622 1.00 90.62 ? 153 ARG B O 1 ATOM 3778 C CB . ARG B 2 153 ? 30.454 -24.604 -71.877 1.00 82.74 ? 153 ARG B CB 1 ATOM 3779 C CG . ARG B 2 153 ? 30.948 -23.227 -72.265 1.00 78.64 ? 153 ARG B CG 1 ATOM 3780 C CD . ARG B 2 153 ? 29.995 -22.159 -71.762 1.00 80.01 ? 153 ARG B CD 1 ATOM 3781 N NE . ARG B 2 153 ? 30.011 -20.991 -72.639 1.00 78.84 ? 153 ARG B NE 1 ATOM 3782 C CZ . ARG B 2 153 ? 29.098 -20.706 -73.565 1.00 80.13 ? 153 ARG B CZ 1 ATOM 3783 N NH1 . ARG B 2 153 ? 28.037 -21.485 -73.754 1.00 83.74 ? 153 ARG B NH1 1 ATOM 3784 N NH2 . ARG B 2 153 ? 29.246 -19.614 -74.307 1.00 79.73 ? 153 ARG B NH2 1 ATOM 3785 N N . ASN B 2 154 ? 30.076 -27.711 -72.703 1.00 97.81 ? 154 ASN B N 1 ATOM 3786 C CA . ASN B 2 154 ? 29.466 -29.035 -72.482 1.00 106.28 ? 154 ASN B CA 1 ATOM 3787 C C . ASN B 2 154 ? 30.457 -30.124 -72.112 1.00 105.28 ? 154 ASN B C 1 ATOM 3788 O O . ASN B 2 154 ? 30.210 -30.916 -71.205 1.00 109.42 ? 154 ASN B O 1 ATOM 3789 C CB . ASN B 2 154 ? 28.775 -29.533 -73.758 1.00 114.85 ? 154 ASN B CB 1 ATOM 3790 C CG . ASN B 2 154 ? 27.371 -29.013 -73.922 1.00 125.23 ? 154 ASN B CG 1 ATOM 3791 O OD1 . ASN B 2 154 ? 26.961 -28.062 -73.261 1.00 125.32 ? 154 ASN B OD1 1 ATOM 3792 N ND2 . ASN B 2 154 ? 26.621 -29.646 -74.822 1.00 140.93 ? 154 ASN B ND2 1 ATOM 3793 N N . GLY B 2 155 ? 31.567 -30.166 -72.843 1.00 100.27 ? 155 GLY B N 1 ATOM 3794 C CA . GLY B 2 155 ? 32.412 -31.354 -72.920 1.00 99.40 ? 155 GLY B CA 1 ATOM 3795 C C . GLY B 2 155 ? 32.142 -32.116 -74.211 1.00 100.64 ? 155 GLY B C 1 ATOM 3796 O O . GLY B 2 155 ? 32.750 -33.157 -74.461 1.00 102.23 ? 155 GLY B O 1 ATOM 3797 N N . THR B 2 156 ? 31.260 -31.565 -75.043 1.00 99.64 ? 156 THR B N 1 ATOM 3798 C CA . THR B 2 156 ? 30.698 -32.254 -76.203 1.00 103.68 ? 156 THR B CA 1 ATOM 3799 C C . THR B 2 156 ? 31.248 -31.713 -77.522 1.00 101.49 ? 156 THR B C 1 ATOM 3800 O O . THR B 2 156 ? 30.749 -32.054 -78.587 1.00 105.17 ? 156 THR B O 1 ATOM 3801 C CB . THR B 2 156 ? 29.161 -32.093 -76.199 1.00 107.56 ? 156 THR B CB 1 ATOM 3802 O OG1 . THR B 2 156 ? 28.636 -32.596 -74.965 1.00 109.74 ? 156 THR B OG1 1 ATOM 3803 C CG2 . THR B 2 156 ? 28.500 -32.842 -77.346 1.00 114.67 ? 156 THR B CG2 1 ATOM 3804 N N . TYR B 2 157 ? 32.280 -30.877 -77.460 1.00 97.26 ? 157 TYR B N 1 ATOM 3805 C CA . TYR B 2 157 ? 32.821 -30.261 -78.672 1.00 96.71 ? 157 TYR B CA 1 ATOM 3806 C C . TYR B 2 157 ? 33.204 -31.325 -79.689 1.00 102.68 ? 157 TYR B C 1 ATOM 3807 O O . TYR B 2 157 ? 34.170 -32.064 -79.493 1.00 102.72 ? 157 TYR B O 1 ATOM 3808 C CB . TYR B 2 157 ? 34.037 -29.389 -78.361 1.00 90.47 ? 157 TYR B CB 1 ATOM 3809 C CG . TYR B 2 157 ? 34.693 -28.821 -79.603 1.00 89.37 ? 157 TYR B CG 1 ATOM 3810 C CD1 . TYR B 2 157 ? 34.103 -27.775 -80.311 1.00 88.98 ? 157 TYR B CD1 1 ATOM 3811 C CD2 . TYR B 2 157 ? 35.894 -29.336 -80.077 1.00 89.12 ? 157 TYR B CD2 1 ATOM 3812 C CE1 . TYR B 2 157 ? 34.696 -27.254 -81.450 1.00 88.74 ? 157 TYR B CE1 1 ATOM 3813 C CE2 . TYR B 2 157 ? 36.495 -28.820 -81.215 1.00 89.41 ? 157 TYR B CE2 1 ATOM 3814 C CZ . TYR B 2 157 ? 35.894 -27.781 -81.897 1.00 88.78 ? 157 TYR B CZ 1 ATOM 3815 O OH . TYR B 2 157 ? 36.495 -27.269 -83.022 1.00 88.71 ? 157 TYR B OH 1 ATOM 3816 N N . ASP B 2 158 ? 32.440 -31.390 -80.775 1.00 109.63 ? 158 ASP B N 1 ATOM 3817 C CA . ASP B 2 158 ? 32.617 -32.427 -81.783 1.00 117.60 ? 158 ASP B CA 1 ATOM 3818 C C . ASP B 2 158 ? 33.810 -32.094 -82.682 1.00 118.39 ? 158 ASP B C 1 ATOM 3819 O O . ASP B 2 158 ? 33.691 -31.350 -83.660 1.00 118.94 ? 158 ASP B O 1 ATOM 3820 C CB . ASP B 2 158 ? 31.332 -32.603 -82.601 1.00 123.61 ? 158 ASP B CB 1 ATOM 3821 C CG . ASP B 2 158 ? 31.275 -33.931 -83.319 1.00 130.47 ? 158 ASP B CG 1 ATOM 3822 O OD1 . ASP B 2 158 ? 32.081 -34.828 -82.995 1.00 130.92 ? 158 ASP B OD1 1 ATOM 3823 O OD2 . ASP B 2 158 ? 30.417 -34.081 -84.209 1.00 137.26 ? 158 ASP B OD2 1 ATOM 3824 N N . TYR B 2 159 ? 34.962 -32.655 -82.324 1.00 119.56 ? 159 TYR B N 1 ATOM 3825 C CA . TYR B 2 159 ? 36.231 -32.342 -82.978 1.00 119.74 ? 159 TYR B CA 1 ATOM 3826 C C . TYR B 2 159 ? 36.266 -32.749 -84.462 1.00 127.55 ? 159 TYR B C 1 ATOM 3827 O O . TYR B 2 159 ? 36.666 -31.942 -85.305 1.00 128.96 ? 159 TYR B O 1 ATOM 3828 C CB . TYR B 2 159 ? 37.396 -32.961 -82.186 1.00 117.90 ? 159 TYR B CB 1 ATOM 3829 C CG . TYR B 2 159 ? 38.717 -32.990 -82.915 1.00 119.03 ? 159 TYR B CG 1 ATOM 3830 C CD1 . TYR B 2 159 ? 39.059 -34.065 -83.738 1.00 124.55 ? 159 TYR B CD1 1 ATOM 3831 C CD2 . TYR B 2 159 ? 39.633 -31.952 -82.774 1.00 115.01 ? 159 TYR B CD2 1 ATOM 3832 C CE1 . TYR B 2 159 ? 40.270 -34.097 -84.407 1.00 125.94 ? 159 TYR B CE1 1 ATOM 3833 C CE2 . TYR B 2 159 ? 40.847 -31.976 -83.436 1.00 116.85 ? 159 TYR B CE2 1 ATOM 3834 C CZ . TYR B 2 159 ? 41.160 -33.049 -84.252 1.00 122.49 ? 159 TYR B CZ 1 ATOM 3835 O OH . TYR B 2 159 ? 42.364 -33.080 -84.914 1.00 125.03 ? 159 TYR B OH 1 ATOM 3836 N N . PRO B 2 160 ? 35.849 -33.993 -84.790 1.00 134.63 ? 160 PRO B N 1 ATOM 3837 C CA . PRO B 2 160 ? 35.800 -34.393 -86.211 1.00 141.96 ? 160 PRO B CA 1 ATOM 3838 C C . PRO B 2 160 ? 34.897 -33.521 -87.098 1.00 143.60 ? 160 PRO B C 1 ATOM 3839 O O . PRO B 2 160 ? 35.134 -33.428 -88.304 1.00 148.17 ? 160 PRO B O 1 ATOM 3840 C CB . PRO B 2 160 ? 35.267 -35.832 -86.156 1.00 147.59 ? 160 PRO B CB 1 ATOM 3841 C CG . PRO B 2 160 ? 35.638 -36.323 -84.801 1.00 144.22 ? 160 PRO B CG 1 ATOM 3842 C CD . PRO B 2 160 ? 35.540 -35.126 -83.896 1.00 136.32 ? 160 PRO B CD 1 ATOM 3843 N N . GLN B 2 161 ? 33.878 -32.897 -86.508 1.00 141.28 ? 161 GLN B N 1 ATOM 3844 C CA . GLN B 2 161 ? 32.983 -31.997 -87.244 1.00 143.19 ? 161 GLN B CA 1 ATOM 3845 C C . GLN B 2 161 ? 33.731 -30.788 -87.814 1.00 138.32 ? 161 GLN B C 1 ATOM 3846 O O . GLN B 2 161 ? 33.341 -30.245 -88.849 1.00 142.07 ? 161 GLN B O 1 ATOM 3847 C CB . GLN B 2 161 ? 31.838 -31.522 -86.341 1.00 141.91 ? 161 GLN B CB 1 ATOM 3848 C CG . GLN B 2 161 ? 30.666 -30.894 -87.084 1.00 146.43 ? 161 GLN B CG 1 ATOM 3849 C CD . GLN B 2 161 ? 29.580 -30.399 -86.146 1.00 145.10 ? 161 GLN B CD 1 ATOM 3850 O OE1 . GLN B 2 161 ? 29.421 -30.907 -85.036 1.00 143.34 ? 161 GLN B OE1 1 ATOM 3851 N NE2 . GLN B 2 161 ? 28.825 -29.400 -86.590 1.00 146.62 ? 161 GLN B NE2 1 ATOM 3852 N N . TYR B 2 162 ? 34.796 -30.372 -87.132 1.00 129.83 ? 162 TYR B N 1 ATOM 3853 C CA . TYR B 2 162 ? 35.650 -29.291 -87.607 1.00 125.69 ? 162 TYR B CA 1 ATOM 3854 C C . TYR B 2 162 ? 37.079 -29.804 -87.761 1.00 123.65 ? 162 TYR B C 1 ATOM 3855 O O . TYR B 2 162 ? 37.784 -29.452 -88.705 1.00 123.61 ? 162 TYR B O 1 ATOM 3856 C CB . TYR B 2 162 ? 35.610 -28.117 -86.627 1.00 119.40 ? 162 TYR B CB 1 ATOM 3857 C CG . TYR B 2 162 ? 34.228 -27.780 -86.096 1.00 118.93 ? 162 TYR B CG 1 ATOM 3858 C CD1 . TYR B 2 162 ? 33.357 -26.970 -86.822 1.00 121.77 ? 162 TYR B CD1 1 ATOM 3859 C CD2 . TYR B 2 162 ? 33.798 -28.264 -84.862 1.00 116.22 ? 162 TYR B CD2 1 ATOM 3860 C CE1 . TYR B 2 162 ? 32.095 -26.655 -86.336 1.00 121.64 ? 162 TYR B CE1 1 ATOM 3861 C CE2 . TYR B 2 162 ? 32.539 -27.955 -84.368 1.00 116.15 ? 162 TYR B CE2 1 ATOM 3862 C CZ . TYR B 2 162 ? 31.692 -27.150 -85.107 1.00 119.10 ? 162 TYR B CZ 1 ATOM 3863 O OH . TYR B 2 162 ? 30.442 -26.840 -84.619 1.00 119.79 ? 162 TYR B OH 1 HETATM 3864 C C1 . NAG C 3 . ? 30.967 -4.062 -53.982 1.00 107.68 ? 1011 NAG A C1 1 HETATM 3865 C C2 . NAG C 3 . ? 30.217 -2.840 -53.443 1.00 119.24 ? 1011 NAG A C2 1 HETATM 3866 C C3 . NAG C 3 . ? 28.883 -3.235 -52.807 1.00 123.48 ? 1011 NAG A C3 1 HETATM 3867 C C4 . NAG C 3 . ? 28.063 -4.123 -53.740 1.00 126.29 ? 1011 NAG A C4 1 HETATM 3868 C C5 . NAG C 3 . ? 28.925 -5.256 -54.296 1.00 122.55 ? 1011 NAG A C5 1 HETATM 3869 C C6 . NAG C 3 . ? 28.165 -6.081 -55.334 1.00 121.44 ? 1011 NAG A C6 1 HETATM 3870 C C7 . NAG C 3 . ? 31.833 -1.105 -52.843 1.00 122.27 ? 1011 NAG A C7 1 HETATM 3871 C C8 . NAG C 3 . ? 32.624 -0.440 -51.752 1.00 120.17 ? 1011 NAG A C8 1 HETATM 3872 N N2 . NAG C 3 . ? 31.035 -2.113 -52.484 1.00 120.93 ? 1011 NAG A N2 1 HETATM 3873 O O3 . NAG C 3 . ? 28.134 -2.083 -52.493 1.00 124.98 ? 1011 NAG A O3 1 HETATM 3874 O O4 . NAG C 3 . ? 26.945 -4.641 -53.047 1.00 128.29 ? 1011 NAG A O4 1 HETATM 3875 O O5 . NAG C 3 . ? 30.099 -4.723 -54.889 1.00 116.40 ? 1011 NAG A O5 1 HETATM 3876 O O6 . NAG C 3 . ? 28.121 -7.431 -54.929 1.00 122.40 ? 1011 NAG A O6 1 HETATM 3877 O O7 . NAG C 3 . ? 31.944 -0.709 -54.003 1.00 124.01 ? 1011 NAG A O7 1 HETATM 3878 C C1 . NAG D 3 . ? 49.846 -6.344 -43.335 1.00 81.00 ? 1023 NAG A C1 1 HETATM 3879 C C2 . NAG D 3 . ? 51.149 -5.707 -42.855 1.00 92.20 ? 1023 NAG A C2 1 HETATM 3880 C C3 . NAG D 3 . ? 51.018 -5.200 -41.418 1.00 97.55 ? 1023 NAG A C3 1 HETATM 3881 C C4 . NAG D 3 . ? 49.741 -4.386 -41.246 1.00 100.49 ? 1023 NAG A C4 1 HETATM 3882 C C5 . NAG D 3 . ? 48.564 -5.254 -41.670 1.00 95.47 ? 1023 NAG A C5 1 HETATM 3883 C C6 . NAG D 3 . ? 47.207 -4.600 -41.415 1.00 93.56 ? 1023 NAG A C6 1 HETATM 3884 C C7 . NAG D 3 . ? 53.095 -6.758 -43.937 1.00 93.87 ? 1023 NAG A C7 1 HETATM 3885 C C8 . NAG D 3 . ? 54.175 -7.801 -43.860 1.00 91.92 ? 1023 NAG A C8 1 HETATM 3886 N N2 . NAG D 3 . ? 52.240 -6.672 -42.912 1.00 94.55 ? 1023 NAG A N2 1 HETATM 3887 O O3 . NAG D 3 . ? 52.150 -4.432 -41.086 1.00 99.32 ? 1023 NAG A O3 1 HETATM 3888 O O4 . NAG D 3 . ? 49.582 -3.970 -39.903 1.00 116.16 ? 1023 NAG A O4 1 HETATM 3889 O O5 . NAG D 3 . ? 48.733 -5.520 -43.044 1.00 84.71 ? 1023 NAG A O5 1 HETATM 3890 O O6 . NAG D 3 . ? 47.127 -3.384 -42.118 1.00 96.16 ? 1023 NAG A O6 1 HETATM 3891 O O7 . NAG D 3 . ? 53.035 -6.034 -44.928 1.00 97.49 ? 1023 NAG A O7 1 HETATM 3892 C C1 . NAG E 3 . ? 49.886 -2.568 -39.759 1.00 129.86 ? 1024 NAG A C1 1 HETATM 3893 C C2 . NAG E 3 . ? 49.333 -2.047 -38.434 1.00 133.20 ? 1024 NAG A C2 1 HETATM 3894 C C3 . NAG E 3 . ? 49.750 -0.599 -38.181 1.00 136.81 ? 1024 NAG A C3 1 HETATM 3895 C C4 . NAG E 3 . ? 51.212 -0.318 -38.532 1.00 138.69 ? 1024 NAG A C4 1 HETATM 3896 C C5 . NAG E 3 . ? 51.637 -0.985 -39.841 1.00 137.28 ? 1024 NAG A C5 1 HETATM 3897 C C6 . NAG E 3 . ? 53.145 -0.886 -40.058 1.00 135.69 ? 1024 NAG A C6 1 HETATM 3898 C C7 . NAG E 3 . ? 47.206 -3.118 -37.820 1.00 128.56 ? 1024 NAG A C7 1 HETATM 3899 C C8 . NAG E 3 . ? 45.706 -3.060 -37.896 1.00 124.27 ? 1024 NAG A C8 1 HETATM 3900 N N2 . NAG E 3 . ? 47.878 -2.131 -38.419 1.00 132.41 ? 1024 NAG A N2 1 HETATM 3901 O O3 . NAG E 3 . ? 49.521 -0.292 -36.823 1.00 136.04 ? 1024 NAG A O3 1 HETATM 3902 O O4 . NAG E 3 . ? 51.385 1.078 -38.644 1.00 141.07 ? 1024 NAG A O4 1 HETATM 3903 O O5 . NAG E 3 . ? 51.277 -2.349 -39.818 1.00 133.80 ? 1024 NAG A O5 1 HETATM 3904 O O6 . NAG E 3 . ? 53.803 -1.930 -39.374 1.00 133.80 ? 1024 NAG A O6 1 HETATM 3905 O O7 . NAG E 3 . ? 47.755 -4.050 -37.228 1.00 123.80 ? 1024 NAG A O7 1 HETATM 3906 C C1 . NAG F 3 . ? 21.916 -40.065 14.074 1.00 93.43 ? 1165 NAG A C1 1 HETATM 3907 C C2 . NAG F 3 . ? 22.688 -41.359 14.308 1.00 99.77 ? 1165 NAG A C2 1 HETATM 3908 C C3 . NAG F 3 . ? 22.162 -42.458 13.393 1.00 104.33 ? 1165 NAG A C3 1 HETATM 3909 C C4 . NAG F 3 . ? 20.663 -42.624 13.599 1.00 108.76 ? 1165 NAG A C4 1 HETATM 3910 C C5 . NAG F 3 . ? 19.941 -41.291 13.420 1.00 107.28 ? 1165 NAG A C5 1 HETATM 3911 C C6 . NAG F 3 . ? 18.446 -41.428 13.739 1.00 110.25 ? 1165 NAG A C6 1 HETATM 3912 C C7 . NAG F 3 . ? 25.047 -41.395 15.019 1.00 109.34 ? 1165 NAG A C7 1 HETATM 3913 C C8 . NAG F 3 . ? 26.479 -41.149 14.631 1.00 108.83 ? 1165 NAG A C8 1 HETATM 3914 N N2 . NAG F 3 . ? 24.111 -41.161 14.088 1.00 106.08 ? 1165 NAG A N2 1 HETATM 3915 O O3 . NAG F 3 . ? 22.822 -43.684 13.636 1.00 102.77 ? 1165 NAG A O3 1 HETATM 3916 O O4 . NAG F 3 . ? 20.195 -43.563 12.655 1.00 119.05 ? 1165 NAG A O4 1 HETATM 3917 O O5 . NAG F 3 . ? 20.531 -40.313 14.254 1.00 99.11 ? 1165 NAG A O5 1 HETATM 3918 O O6 . NAG F 3 . ? 17.922 -40.323 14.448 1.00 108.45 ? 1165 NAG A O6 1 HETATM 3919 O O7 . NAG F 3 . ? 24.799 -41.793 16.157 1.00 107.33 ? 1165 NAG A O7 1 HETATM 3920 C C1 . NAG G 3 . ? 19.529 -44.687 13.260 1.00 130.76 ? 1166 NAG A C1 1 HETATM 3921 C C2 . NAG G 3 . ? 19.190 -45.679 12.158 1.00 135.90 ? 1166 NAG A C2 1 HETATM 3922 C C3 . NAG G 3 . ? 18.474 -46.914 12.699 1.00 143.95 ? 1166 NAG A C3 1 HETATM 3923 C C4 . NAG G 3 . ? 18.995 -47.430 14.050 1.00 148.13 ? 1166 NAG A C4 1 HETATM 3924 C C5 . NAG G 3 . ? 19.551 -46.318 14.954 1.00 139.95 ? 1166 NAG A C5 1 HETATM 3925 C C6 . NAG G 3 . ? 20.440 -46.889 16.056 1.00 137.45 ? 1166 NAG A C6 1 HETATM 3926 C C7 . NAG G 3 . ? 18.883 -44.440 10.062 1.00 136.54 ? 1166 NAG A C7 1 HETATM 3927 C C8 . NAG G 3 . ? 17.904 -43.841 9.097 1.00 136.35 ? 1166 NAG A C8 1 HETATM 3928 N N2 . NAG G 3 . ? 18.369 -45.048 11.133 1.00 137.66 ? 1166 NAG A N2 1 HETATM 3929 O O3 . NAG G 3 . ? 18.592 -47.925 11.720 1.00 146.43 ? 1166 NAG A O3 1 HETATM 3930 O O4 . NAG G 3 . ? 17.972 -48.110 14.777 1.00 161.14 ? 1166 NAG A O4 1 HETATM 3931 O O5 . NAG G 3 . ? 20.302 -45.367 14.224 1.00 132.73 ? 1166 NAG A O5 1 HETATM 3932 O O6 . NAG G 3 . ? 20.665 -45.897 17.031 1.00 131.63 ? 1166 NAG A O6 1 HETATM 3933 O O7 . NAG G 3 . ? 20.090 -44.350 9.842 1.00 134.80 ? 1166 NAG A O7 1 HETATM 3934 C C1 . MAN H 4 . ? 17.445 -49.354 14.231 1.00 172.38 ? 1167 MAN A C1 1 HETATM 3935 C C2 . MAN H 4 . ? 18.548 -50.396 14.029 1.00 174.34 ? 1167 MAN A C2 1 HETATM 3936 C C3 . MAN H 4 . ? 17.973 -51.756 13.629 1.00 176.80 ? 1167 MAN A C3 1 HETATM 3937 C C4 . MAN H 4 . ? 16.635 -51.618 12.913 1.00 180.35 ? 1167 MAN A C4 1 HETATM 3938 C C5 . MAN H 4 . ? 16.572 -50.301 12.146 1.00 180.52 ? 1167 MAN A C5 1 HETATM 3939 C C6 . MAN H 4 . ? 15.279 -50.201 11.342 1.00 179.31 ? 1167 MAN A C6 1 HETATM 3940 O O2 . MAN H 4 . ? 19.317 -50.516 15.233 1.00 175.20 ? 1167 MAN A O2 1 HETATM 3941 O O3 . MAN H 4 . ? 17.783 -52.596 14.781 1.00 173.89 ? 1167 MAN A O3 1 HETATM 3942 O O4 . MAN H 4 . ? 16.461 -52.724 12.018 1.00 181.82 ? 1167 MAN A O4 1 HETATM 3943 O O5 . MAN H 4 . ? 16.663 -49.178 13.036 1.00 178.25 ? 1167 MAN A O5 1 HETATM 3944 O O6 . MAN H 4 . ? 15.291 -51.149 10.257 1.00 177.09 ? 1167 MAN A O6 1 HETATM 3945 C C1 . BMA I 5 . ? 18.429 -53.873 14.602 1.00 167.58 ? 1168 BMA A C1 1 HETATM 3946 C C2 . BMA I 5 . ? 19.819 -53.813 15.225 1.00 164.63 ? 1168 BMA A C2 1 HETATM 3947 C C3 . BMA I 5 . ? 20.548 -55.132 14.989 1.00 160.37 ? 1168 BMA A C3 1 HETATM 3948 C C4 . BMA I 5 . ? 19.675 -56.312 15.409 1.00 158.08 ? 1168 BMA A C4 1 HETATM 3949 C C5 . BMA I 5 . ? 18.259 -56.201 14.841 1.00 156.08 ? 1168 BMA A C5 1 HETATM 3950 C C6 . BMA I 5 . ? 17.360 -57.311 15.374 1.00 151.62 ? 1168 BMA A C6 1 HETATM 3951 O O2 . BMA I 5 . ? 19.707 -53.563 16.609 1.00 164.63 ? 1168 BMA A O2 1 HETATM 3952 O O3 . BMA I 5 . ? 21.763 -55.153 15.706 1.00 157.77 ? 1168 BMA A O3 1 HETATM 3953 O O4 . BMA I 5 . ? 20.274 -57.510 14.964 1.00 154.65 ? 1168 BMA A O4 1 HETATM 3954 O O5 . BMA I 5 . ? 17.706 -54.942 15.177 1.00 162.52 ? 1168 BMA A O5 1 HETATM 3955 O O6 . BMA I 5 . ? 16.022 -57.063 15.008 1.00 144.32 ? 1168 BMA A O6 1 HETATM 3956 C C1 . MAN J 4 . ? 15.218 -50.637 8.897 1.00 174.45 ? 1169 MAN A C1 1 HETATM 3957 C C2 . MAN J 4 . ? 16.420 -49.752 8.548 1.00 172.83 ? 1169 MAN A C2 1 HETATM 3958 C C3 . MAN J 4 . ? 16.209 -48.250 8.775 1.00 174.46 ? 1169 MAN A C3 1 HETATM 3959 C C4 . MAN J 4 . ? 14.796 -47.768 8.454 1.00 176.57 ? 1169 MAN A C4 1 HETATM 3960 C C5 . MAN J 4 . ? 13.691 -48.724 8.903 1.00 174.41 ? 1169 MAN A C5 1 HETATM 3961 C C6 . MAN J 4 . ? 12.365 -48.346 8.254 1.00 169.61 ? 1169 MAN A C6 1 HETATM 3962 O O2 . MAN J 4 . ? 16.776 -49.984 7.200 1.00 165.05 ? 1169 MAN A O2 1 HETATM 3963 O O3 . MAN J 4 . ? 17.118 -47.520 7.979 1.00 170.78 ? 1169 MAN A O3 1 HETATM 3964 O O4 . MAN J 4 . ? 14.600 -46.530 9.103 1.00 177.91 ? 1169 MAN A O4 1 HETATM 3965 O O5 . MAN J 4 . ? 13.967 -50.062 8.541 1.00 174.52 ? 1169 MAN A O5 1 HETATM 3966 O O6 . MAN J 4 . ? 11.826 -47.223 8.915 1.00 164.88 ? 1169 MAN A O6 1 HETATM 3967 C C1 . NAG K 3 . ? 23.181 -12.205 -30.231 1.00 122.68 ? 1286 NAG A C1 1 HETATM 3968 C C2 . NAG K 3 . ? 21.729 -11.949 -29.795 1.00 132.81 ? 1286 NAG A C2 1 HETATM 3969 C C3 . NAG K 3 . ? 20.725 -12.028 -30.947 1.00 136.44 ? 1286 NAG A C3 1 HETATM 3970 C C4 . NAG K 3 . ? 21.231 -11.259 -32.167 1.00 140.53 ? 1286 NAG A C4 1 HETATM 3971 C C5 . NAG K 3 . ? 22.628 -11.760 -32.530 1.00 137.89 ? 1286 NAG A C5 1 HETATM 3972 C C6 . NAG K 3 . ? 23.207 -11.075 -33.767 1.00 135.44 ? 1286 NAG A C6 1 HETATM 3973 C C7 . NAG K 3 . ? 21.328 -12.486 -27.423 1.00 128.55 ? 1286 NAG A C7 1 HETATM 3974 C C8 . NAG K 3 . ? 20.907 -13.518 -26.415 1.00 123.32 ? 1286 NAG A C8 1 HETATM 3975 N N2 . NAG K 3 . ? 21.340 -12.851 -28.712 1.00 131.01 ? 1286 NAG A N2 1 HETATM 3976 O O3 . NAG K 3 . ? 19.492 -11.492 -30.520 1.00 134.97 ? 1286 NAG A O3 1 HETATM 3977 O O4 . NAG K 3 . ? 20.332 -11.412 -33.248 1.00 145.31 ? 1286 NAG A O4 1 HETATM 3978 O O5 . NAG K 3 . ? 23.488 -11.513 -31.435 1.00 131.77 ? 1286 NAG A O5 1 HETATM 3979 O O6 . NAG K 3 . ? 24.097 -11.953 -34.420 1.00 134.86 ? 1286 NAG A O6 1 HETATM 3980 O O7 . NAG K 3 . ? 21.643 -11.363 -27.028 1.00 129.26 ? 1286 NAG A O7 1 HETATM 3981 C C1 . SIA L 6 . ? 36.163 -5.092 21.734 1.00 101.17 ? 1322 SIA A C1 1 HETATM 3982 C C2 . SIA L 6 . ? 36.407 -5.233 23.227 1.00 98.10 ? 1322 SIA A C2 1 HETATM 3983 C C3 . SIA L 6 . ? 35.084 -5.100 23.980 1.00 94.26 ? 1322 SIA A C3 1 HETATM 3984 C C4 . SIA L 6 . ? 34.230 -6.346 23.841 1.00 92.86 ? 1322 SIA A C4 1 HETATM 3985 C C5 . SIA L 6 . ? 35.032 -7.554 24.295 1.00 92.67 ? 1322 SIA A C5 1 HETATM 3986 C C6 . SIA L 6 . ? 36.295 -7.665 23.439 1.00 91.01 ? 1322 SIA A C6 1 HETATM 3987 C C7 . SIA L 6 . ? 37.216 -8.836 23.795 1.00 89.13 ? 1322 SIA A C7 1 HETATM 3988 C C8 . SIA L 6 . ? 38.572 -8.759 23.083 1.00 87.10 ? 1322 SIA A C8 1 HETATM 3989 C C9 . SIA L 6 . ? 39.239 -10.133 23.029 1.00 85.55 ? 1322 SIA A C9 1 HETATM 3990 C C10 . SIA L 6 . ? 34.207 -9.825 24.714 1.00 97.61 ? 1322 SIA A C10 1 HETATM 3991 C C11 . SIA L 6 . ? 33.226 -10.882 24.296 1.00 96.93 ? 1322 SIA A C11 1 HETATM 3992 N N5 . SIA L 6 . ? 34.156 -8.689 24.023 1.00 96.16 ? 1322 SIA A N5 1 HETATM 3993 O O1A . SIA L 6 . ? 35.417 -4.170 21.322 1.00 97.73 ? 1322 SIA A O1A 1 HETATM 3994 O O1B . SIA L 6 . ? 36.722 -5.898 20.955 1.00 103.68 ? 1322 SIA A O1B 1 HETATM 3995 O O4 . SIA L 6 . ? 33.038 -6.207 24.619 1.00 90.55 ? 1322 SIA A O4 1 HETATM 3996 O O6 . SIA L 6 . ? 37.059 -6.466 23.557 1.00 90.29 ? 1322 SIA A O6 1 HETATM 3997 O O7 . SIA L 6 . ? 37.432 -8.872 25.207 1.00 90.21 ? 1322 SIA A O7 1 HETATM 3998 O O8 . SIA L 6 . ? 38.427 -8.270 21.740 1.00 87.70 ? 1322 SIA A O8 1 HETATM 3999 O O9 . SIA L 6 . ? 40.599 -10.009 22.589 1.00 82.76 ? 1322 SIA A O9 1 HETATM 4000 O O10 . SIA L 6 . ? 35.005 -10.005 25.619 1.00 98.71 ? 1322 SIA A O10 1 HETATM 4001 C C1 . GAL M 7 . ? 38.265 -0.429 22.738 1.00 133.22 ? 1323 GAL A C1 1 HETATM 4002 C C2 . GAL M 7 . ? 39.468 -0.066 21.862 1.00 131.55 ? 1323 GAL A C2 1 HETATM 4003 C C3 . GAL M 7 . ? 39.948 -1.218 20.968 1.00 126.85 ? 1323 GAL A C3 1 HETATM 4004 C C4 . GAL M 7 . ? 39.943 -2.570 21.684 1.00 124.24 ? 1323 GAL A C4 1 HETATM 4005 C C5 . GAL M 7 . ? 38.625 -2.755 22.421 1.00 122.16 ? 1323 GAL A C5 1 HETATM 4006 C C6 . GAL M 7 . ? 38.560 -4.092 23.144 1.00 114.31 ? 1323 GAL A C6 1 HETATM 4007 O O1 . GAL M 7 . ? 38.085 0.567 23.746 1.00 133.40 ? 1323 GAL A O1 1 HETATM 4008 O O2 . GAL M 7 . ? 39.101 1.043 21.032 1.00 130.56 ? 1323 GAL A O2 1 HETATM 4009 O O3 . GAL M 7 . ? 41.269 -0.940 20.488 1.00 120.33 ? 1323 GAL A O3 1 HETATM 4010 O O4 . GAL M 7 . ? 41.036 -2.670 22.606 1.00 123.07 ? 1323 GAL A O4 1 HETATM 4011 O O5 . GAL M 7 . ? 38.460 -1.698 23.367 1.00 131.18 ? 1323 GAL A O5 1 HETATM 4012 O O6 . GAL M 7 . ? 37.249 -4.182 23.705 1.00 108.05 ? 1323 GAL A O6 1 HETATM 4013 C C1 . NAG N 3 . ? 25.252 -29.317 -75.128 1.00 94.97 ? 1154 NAG B C1 1 HETATM 4014 C C2 . NAG N 3 . ? 24.262 -30.490 -75.254 1.00 105.62 ? 1154 NAG B C2 1 HETATM 4015 C C3 . NAG N 3 . ? 23.873 -30.865 -76.685 1.00 111.20 ? 1154 NAG B C3 1 HETATM 4016 C C4 . NAG N 3 . ? 23.732 -29.620 -77.547 1.00 117.18 ? 1154 NAG B C4 1 HETATM 4017 C C5 . NAG N 3 . ? 25.047 -28.849 -77.479 1.00 110.92 ? 1154 NAG B C5 1 HETATM 4018 C C6 . NAG N 3 . ? 25.105 -27.675 -78.456 1.00 109.17 ? 1154 NAG B C6 1 HETATM 4019 C C7 . NAG N 3 . ? 24.855 -31.736 -73.236 1.00 108.24 ? 1154 NAG B C7 1 HETATM 4020 C C8 . NAG N 3 . ? 25.408 -33.002 -72.644 1.00 107.85 ? 1154 NAG B C8 1 HETATM 4021 N N2 . NAG N 3 . ? 24.778 -31.666 -74.568 1.00 105.11 ? 1154 NAG B N2 1 HETATM 4022 O O3 . NAG N 3 . ? 22.653 -31.572 -76.668 1.00 110.19 ? 1154 NAG B O3 1 HETATM 4023 O O4 . NAG N 3 . ? 23.349 -29.971 -78.871 1.00 127.97 ? 1154 NAG B O4 1 HETATM 4024 O O5 . NAG N 3 . ? 25.169 -28.352 -76.164 1.00 103.23 ? 1154 NAG B O5 1 HETATM 4025 O O6 . NAG N 3 . ? 24.174 -26.686 -78.073 1.00 106.37 ? 1154 NAG B O6 1 HETATM 4026 O O7 . NAG N 3 . ? 24.501 -30.821 -72.490 1.00 108.15 ? 1154 NAG B O7 1 HETATM 4027 C C1 . NAG O 3 . ? 22.102 -29.335 -79.233 1.00 134.41 ? 1155 NAG B C1 1 HETATM 4028 C C2 . NAG O 3 . ? 21.765 -29.654 -80.692 1.00 135.85 ? 1155 NAG B C2 1 HETATM 4029 C C3 . NAG O 3 . ? 20.327 -29.265 -81.067 1.00 144.01 ? 1155 NAG B C3 1 HETATM 4030 C C4 . NAG O 3 . ? 19.302 -29.581 -79.974 1.00 147.55 ? 1155 NAG B C4 1 HETATM 4031 C C5 . NAG O 3 . ? 19.831 -29.059 -78.639 1.00 142.57 ? 1155 NAG B C5 1 HETATM 4032 C C6 . NAG O 3 . ? 18.867 -29.274 -77.474 1.00 138.89 ? 1155 NAG B C6 1 HETATM 4033 C C7 . NAG O 3 . ? 23.878 -29.473 -81.954 1.00 125.54 ? 1155 NAG B C7 1 HETATM 4034 C C8 . NAG O 3 . ? 24.711 -28.637 -82.883 1.00 122.68 ? 1155 NAG B C8 1 HETATM 4035 N N2 . NAG O 3 . ? 22.695 -28.972 -81.587 1.00 131.35 ? 1155 NAG B N2 1 HETATM 4036 O O3 . NAG O 3 . ? 19.969 -29.901 -82.276 1.00 146.47 ? 1155 NAG B O3 1 HETATM 4037 O O4 . NAG O 3 . ? 18.056 -28.969 -80.276 1.00 157.03 ? 1155 NAG B O4 1 HETATM 4038 O O5 . NAG O 3 . ? 21.046 -29.730 -78.376 1.00 139.44 ? 1155 NAG B O5 1 HETATM 4039 O O6 . NAG O 3 . ? 18.654 -30.652 -77.271 1.00 135.46 ? 1155 NAG B O6 1 HETATM 4040 O O7 . NAG O 3 . ? 24.306 -30.561 -81.574 1.00 124.39 ? 1155 NAG B O7 1 HETATM 4041 C C1 . BMA P 5 . ? 17.089 -29.880 -80.849 1.00 163.65 ? 1156 BMA B C1 1 HETATM 4042 C C2 . BMA P 5 . ? 15.690 -29.289 -80.692 1.00 164.68 ? 1156 BMA B C2 1 HETATM 4043 C C3 . BMA P 5 . ? 14.641 -30.246 -81.257 1.00 165.31 ? 1156 BMA B C3 1 HETATM 4044 C C4 . BMA P 5 . ? 14.993 -30.664 -82.685 1.00 163.79 ? 1156 BMA B C4 1 HETATM 4045 C C5 . BMA P 5 . ? 16.443 -31.140 -82.784 1.00 161.37 ? 1156 BMA B C5 1 HETATM 4046 C C6 . BMA P 5 . ? 16.846 -31.432 -84.228 1.00 157.02 ? 1156 BMA B C6 1 HETATM 4047 O O2 . BMA P 5 . ? 15.615 -28.026 -81.368 1.00 161.23 ? 1156 BMA B O2 1 HETATM 4048 O O3 . BMA P 5 . ? 13.347 -29.631 -81.237 1.00 166.61 ? 1156 BMA B O3 1 HETATM 4049 O O4 . BMA P 5 . ? 14.112 -31.716 -83.096 1.00 160.66 ? 1156 BMA B O4 1 HETATM 4050 O O5 . BMA P 5 . ? 17.327 -30.157 -82.234 1.00 164.76 ? 1156 BMA B O5 1 HETATM 4051 O O6 . BMA P 5 . ? 16.879 -30.222 -84.994 1.00 154.34 ? 1156 BMA B O6 1 HETATM 4052 S S1 . MPO Q 8 . ? 38.358 -11.349 -71.377 1.00 121.07 ? 1163 MPO B S1 1 HETATM 4053 O O1 . MPO Q 8 . ? 38.061 -10.790 -72.664 1.00 128.44 ? 1163 MPO B O1 1 HETATM 4054 O O2 . MPO Q 8 . ? 37.931 -12.718 -71.339 1.00 121.28 ? 1163 MPO B O2 1 HETATM 4055 O O4 . MPO Q 8 . ? 43.648 -8.615 -72.471 1.00 123.34 ? 1163 MPO B O4 1 HETATM 4056 N N1 . MPO Q 8 . ? 42.758 -10.932 -71.912 1.00 114.16 ? 1163 MPO B N1 1 HETATM 4057 C C1 . MPO Q 8 . ? 39.997 -11.251 -71.112 1.00 114.22 ? 1163 MPO B C1 1 HETATM 4058 O O3 . MPO Q 8 . ? 37.545 -10.485 -70.248 1.00 120.38 ? 1163 MPO B O3 1 HETATM 4059 C C2 . MPO Q 8 . ? 40.742 -12.333 -71.886 1.00 104.57 ? 1163 MPO B C2 1 HETATM 4060 C C3 . MPO Q 8 . ? 42.235 -12.275 -71.595 1.00 108.34 ? 1163 MPO B C3 1 HETATM 4061 C C4 . MPO Q 8 . ? 43.924 -11.008 -72.808 1.00 114.34 ? 1163 MPO B C4 1 HETATM 4062 C C5 . MPO Q 8 . ? 44.500 -9.615 -73.045 1.00 117.05 ? 1163 MPO B C5 1 HETATM 4063 C C6 . MPO Q 8 . ? 43.474 -8.754 -71.054 1.00 122.97 ? 1163 MPO B C6 1 HETATM 4064 C C7 . MPO Q 8 . ? 43.138 -10.200 -70.691 1.00 119.90 ? 1163 MPO B C7 1 HETATM 4065 O O . HOH R 9 . ? 38.893 -14.007 -82.302 1.00 77.07 ? 2001 HOH A O 1 HETATM 4066 O O . HOH R 9 . ? 36.194 -14.211 -75.408 1.00 62.65 ? 2002 HOH A O 1 HETATM 4067 O O . HOH R 9 . ? 42.974 -13.032 -76.382 1.00 68.96 ? 2003 HOH A O 1 HETATM 4068 O O . HOH R 9 . ? 41.538 -15.793 -70.069 1.00 57.00 ? 2004 HOH A O 1 HETATM 4069 O O . HOH R 9 . ? 40.081 -14.481 -65.528 1.00 52.84 ? 2005 HOH A O 1 HETATM 4070 O O . HOH R 9 . ? 40.498 -12.638 -58.797 1.00 54.54 ? 2006 HOH A O 1 HETATM 4071 O O . HOH R 9 . ? 31.507 -11.429 -54.731 1.00 70.97 ? 2007 HOH A O 1 HETATM 4072 O O . HOH R 9 . ? 32.749 -2.255 -57.585 1.00 77.60 ? 2008 HOH A O 1 HETATM 4073 O O . HOH R 9 . ? 34.317 -10.458 -49.744 1.00 72.59 ? 2009 HOH A O 1 HETATM 4074 O O . HOH R 9 . ? 36.289 -6.184 -48.729 1.00 71.56 ? 2010 HOH A O 1 HETATM 4075 O O . HOH R 9 . ? 42.960 -5.596 -49.471 1.00 74.91 ? 2011 HOH A O 1 HETATM 4076 O O . HOH R 9 . ? 40.819 -7.663 -44.208 1.00 75.90 ? 2012 HOH A O 1 HETATM 4077 O O . HOH R 9 . ? 45.849 -7.752 -42.579 1.00 78.23 ? 2013 HOH A O 1 HETATM 4078 O O . HOH R 9 . ? 46.260 -10.523 -43.763 1.00 64.25 ? 2014 HOH A O 1 HETATM 4079 O O . HOH R 9 . ? 44.916 -15.018 -42.224 1.00 47.11 ? 2015 HOH A O 1 HETATM 4080 O O . HOH R 9 . ? 49.736 -9.854 -41.231 1.00 64.79 ? 2016 HOH A O 1 HETATM 4081 O O . HOH R 9 . ? 46.596 -12.797 -39.411 1.00 69.22 ? 2017 HOH A O 1 HETATM 4082 O O . HOH R 9 . ? 51.554 -18.254 -50.337 1.00 67.41 ? 2018 HOH A O 1 HETATM 4083 O O . HOH R 9 . ? 56.243 -14.122 -50.988 1.00 62.43 ? 2019 HOH A O 1 HETATM 4084 O O . HOH R 9 . ? 52.608 -16.584 -52.051 1.00 66.11 ? 2020 HOH A O 1 HETATM 4085 O O . HOH R 9 . ? 54.340 -11.087 -47.511 1.00 77.12 ? 2021 HOH A O 1 HETATM 4086 O O . HOH R 9 . ? 31.811 -17.773 -50.516 1.00 76.11 ? 2022 HOH A O 1 HETATM 4087 O O . HOH R 9 . ? 34.356 -12.061 -47.453 1.00 62.37 ? 2023 HOH A O 1 HETATM 4088 O O . HOH R 9 . ? 32.437 -13.908 -47.783 1.00 70.66 ? 2024 HOH A O 1 HETATM 4089 O O . HOH R 9 . ? 40.256 -12.434 -36.800 1.00 57.52 ? 2025 HOH A O 1 HETATM 4090 O O . HOH R 9 . ? 34.784 -10.081 -33.522 1.00 78.07 ? 2026 HOH A O 1 HETATM 4091 O O . HOH R 9 . ? 47.798 -29.077 -1.261 1.00 63.07 ? 2027 HOH A O 1 HETATM 4092 O O . HOH R 9 . ? 30.665 -11.409 -28.022 1.00 65.97 ? 2028 HOH A O 1 HETATM 4093 O O . HOH R 9 . ? 22.715 -21.131 -16.254 1.00 76.80 ? 2029 HOH A O 1 HETATM 4094 O O . HOH R 9 . ? 25.588 -13.608 5.696 1.00 75.17 ? 2030 HOH A O 1 HETATM 4095 O O . HOH R 9 . ? 33.681 -6.144 7.718 1.00 75.93 ? 2031 HOH A O 1 HETATM 4096 O O . HOH R 9 . ? 25.262 -6.892 3.200 1.00 74.36 ? 2032 HOH A O 1 HETATM 4097 O O . HOH R 9 . ? 21.018 -5.652 7.698 1.00 72.61 ? 2033 HOH A O 1 HETATM 4098 O O . HOH R 9 . ? 17.961 -18.598 8.735 1.00 76.40 ? 2034 HOH A O 1 HETATM 4099 O O . HOH R 9 . ? 18.696 -16.312 9.440 1.00 76.00 ? 2035 HOH A O 1 HETATM 4100 O O . HOH R 9 . ? 38.132 -14.630 -0.377 1.00 62.76 ? 2036 HOH A O 1 HETATM 4101 O O . HOH R 9 . ? 32.470 -7.228 -7.950 1.00 85.53 ? 2037 HOH A O 1 HETATM 4102 O O . HOH R 9 . ? 41.156 -7.976 21.041 1.00 74.00 ? 2038 HOH A O 1 HETATM 4103 O O . HOH R 9 . ? 43.250 -24.809 1.648 1.00 64.21 ? 2039 HOH A O 1 HETATM 4104 O O . HOH R 9 . ? 45.284 -29.176 -2.828 1.00 55.71 ? 2040 HOH A O 1 HETATM 4105 O O . HOH R 9 . ? 28.222 0.493 11.691 1.00 70.06 ? 2041 HOH A O 1 HETATM 4106 O O . HOH R 9 . ? 39.598 -13.554 -13.259 1.00 74.15 ? 2042 HOH A O 1 HETATM 4107 O O . HOH R 9 . ? 27.776 -10.529 -25.197 1.00 79.19 ? 2043 HOH A O 1 HETATM 4108 O O . HOH R 9 . ? 36.690 -19.883 -23.252 1.00 78.48 ? 2044 HOH A O 1 HETATM 4109 O O . HOH R 9 . ? 40.502 -8.758 -24.378 1.00 76.55 ? 2045 HOH A O 1 HETATM 4110 O O . HOH R 9 . ? 41.917 -8.603 -30.975 1.00 73.84 ? 2046 HOH A O 1 HETATM 4111 O O . HOH R 9 . ? 47.903 -12.626 -33.568 1.00 76.73 ? 2047 HOH A O 1 HETATM 4112 O O . HOH R 9 . ? 45.222 -15.393 -39.526 1.00 55.00 ? 2048 HOH A O 1 HETATM 4113 O O . HOH R 9 . ? 40.154 -9.787 -37.969 1.00 69.69 ? 2049 HOH A O 1 HETATM 4114 O O . HOH R 9 . ? 41.601 -21.691 -45.985 1.00 52.59 ? 2050 HOH A O 1 HETATM 4115 O O . HOH R 9 . ? 32.456 -20.165 -49.736 1.00 74.51 ? 2051 HOH A O 1 HETATM 4116 O O . HOH R 9 . ? 44.103 -18.260 -55.576 1.00 45.95 ? 2052 HOH A O 1 HETATM 4117 O O . HOH R 9 . ? 46.846 -18.149 -56.004 1.00 55.06 ? 2053 HOH A O 1 HETATM 4118 O O . HOH R 9 . ? 48.347 -17.024 -57.716 1.00 62.13 ? 2054 HOH A O 1 HETATM 4119 O O . HOH S 9 . ? 49.407 -19.467 -60.347 1.00 47.02 ? 2001 HOH B O 1 HETATM 4120 O O . HOH S 9 . ? 50.915 -15.317 -57.159 1.00 76.18 ? 2002 HOH B O 1 HETATM 4121 O O . HOH S 9 . ? 52.823 -25.902 -61.996 1.00 56.72 ? 2003 HOH B O 1 HETATM 4122 O O . HOH S 9 . ? 50.716 -12.923 -64.849 1.00 67.60 ? 2004 HOH B O 1 HETATM 4123 O O . HOH S 9 . ? 45.591 -13.278 -69.509 1.00 70.16 ? 2005 HOH B O 1 HETATM 4124 O O . HOH S 9 . ? 43.499 -12.219 -67.991 1.00 66.45 ? 2006 HOH B O 1 HETATM 4125 O O . HOH S 9 . ? 49.474 -11.485 -63.305 1.00 66.91 ? 2007 HOH B O 1 HETATM 4126 O O . HOH S 9 . ? 41.856 -8.986 -65.584 1.00 75.46 ? 2008 HOH B O 1 HETATM 4127 O O . HOH S 9 . ? 41.300 -13.704 -68.381 1.00 60.23 ? 2009 HOH B O 1 HETATM 4128 O O . HOH S 9 . ? 35.275 -8.870 -66.256 1.00 63.43 ? 2010 HOH B O 1 HETATM 4129 O O . HOH S 9 . ? 28.251 -13.118 -64.983 1.00 71.03 ? 2011 HOH B O 1 HETATM 4130 O O . HOH S 9 . ? 30.968 -17.591 -56.040 1.00 64.89 ? 2012 HOH B O 1 HETATM 4131 O O . HOH S 9 . ? 25.671 -14.582 -74.601 0.50 43.34 ? 2013 HOH B O 1 HETATM 4132 O O . HOH S 9 . ? 31.417 -9.706 -79.387 1.00 77.92 ? 2014 HOH B O 1 HETATM 4133 O O . HOH S 9 . ? 38.200 -31.715 -56.271 1.00 74.26 ? 2015 HOH B O 1 HETATM 4134 O O . HOH S 9 . ? 28.407 -25.709 -66.049 1.00 73.35 ? 2016 HOH B O 1 HETATM 4135 O O . HOH S 9 . ? 32.627 -21.400 -47.479 1.00 75.44 ? 2017 HOH B O 1 HETATM 4136 O O . HOH S 9 . ? 42.918 -27.372 -49.997 1.00 55.53 ? 2018 HOH B O 1 HETATM 4137 O O . HOH S 9 . ? 37.273 -34.180 -42.485 1.00 61.74 ? 2019 HOH B O 1 HETATM 4138 O O . HOH S 9 . ? 41.133 -33.144 -31.765 1.00 72.57 ? 2020 HOH B O 1 HETATM 4139 O O . HOH S 9 . ? 43.790 -21.297 -12.377 1.00 81.71 ? 2021 HOH B O 1 HETATM 4140 O O . HOH S 9 . ? 46.273 -18.105 -5.864 1.00 78.38 ? 2022 HOH B O 1 HETATM 4141 O O . HOH S 9 . ? 47.850 -15.769 2.148 1.00 78.07 ? 2023 HOH B O 1 HETATM 4142 O O . HOH S 9 . ? 56.097 -14.655 2.496 1.00 78.82 ? 2024 HOH B O 1 HETATM 4143 O O . HOH S 9 . ? 53.994 -24.966 0.229 1.00 63.97 ? 2025 HOH B O 1 HETATM 4144 O O . HOH S 9 . ? 53.820 -18.024 -7.099 1.00 69.25 ? 2026 HOH B O 1 HETATM 4145 O O . HOH S 9 . ? 47.787 -20.012 -10.425 1.00 63.12 ? 2027 HOH B O 1 HETATM 4146 O O . HOH S 9 . ? 52.514 -19.952 -29.048 1.00 70.04 ? 2028 HOH B O 1 HETATM 4147 O O . HOH S 9 . ? 47.670 -26.934 -35.966 1.00 50.72 ? 2029 HOH B O 1 HETATM 4148 O O . HOH S 9 . ? 47.209 -17.401 -38.669 1.00 55.57 ? 2030 HOH B O 1 HETATM 4149 O O . HOH S 9 . ? 45.768 -30.130 -45.643 1.00 72.29 ? 2031 HOH B O 1 HETATM 4150 O O . HOH S 9 . ? 46.080 -27.230 -52.255 1.00 50.67 ? 2032 HOH B O 1 HETATM 4151 O O . HOH S 9 . ? 44.752 -29.330 -51.231 1.00 50.27 ? 2033 HOH B O 1 HETATM 4152 O O . HOH S 9 . ? 49.789 -31.899 -52.534 1.00 48.79 ? 2034 HOH B O 1 HETATM 4153 O O . HOH S 9 . ? 51.872 -22.450 -52.494 1.00 44.92 ? 2035 HOH B O 1 HETATM 4154 O O . HOH S 9 . ? 42.056 -29.133 -57.789 1.00 53.62 ? 2036 HOH B O 1 HETATM 4155 O O . HOH S 9 . ? 38.518 -27.622 -62.406 1.00 53.14 ? 2037 HOH B O 1 HETATM 4156 O O . HOH S 9 . ? 37.659 -29.448 -57.472 1.00 66.49 ? 2038 HOH B O 1 HETATM 4157 O O . HOH S 9 . ? 41.928 -31.276 -66.967 1.00 65.10 ? 2039 HOH B O 1 HETATM 4158 O O . HOH S 9 . ? 45.203 -30.613 -65.593 1.00 58.59 ? 2040 HOH B O 1 HETATM 4159 O O . HOH S 9 . ? 37.906 -29.030 -64.645 1.00 68.22 ? 2041 HOH B O 1 HETATM 4160 O O . HOH S 9 . ? 45.820 -19.744 -73.804 1.00 56.35 ? 2042 HOH B O 1 HETATM 4161 O O . HOH S 9 . ? 38.541 -32.629 -72.080 1.00 67.40 ? 2043 HOH B O 1 HETATM 4162 O O . HOH S 9 . ? 48.916 -25.469 -71.955 1.00 66.54 ? 2044 HOH B O 1 HETATM 4163 O O . HOH S 9 . ? 46.988 -25.577 -80.751 1.00 72.38 ? 2045 HOH B O 1 HETATM 4164 O O . HOH S 9 . ? 48.417 -23.313 -81.243 1.00 70.89 ? 2046 HOH B O 1 HETATM 4165 O O . HOH S 9 . ? 49.577 -27.600 -75.505 1.00 68.89 ? 2047 HOH B O 1 HETATM 4166 O O . HOH S 9 . ? 50.105 -14.139 -73.032 1.00 74.34 ? 2048 HOH B O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . ASP A 1 ? 0.9516 0.9851 0.7678 0.2668 -0.1322 0.0068 1 ASP A N 2 C CA . ASP A 1 ? 0.9128 1.0036 0.7638 0.2648 -0.1336 -0.0027 1 ASP A CA 3 C C . ASP A 1 ? 0.8862 0.9607 0.7647 0.2325 -0.1245 -0.0045 1 ASP A C 4 O O . ASP A 1 ? 0.8566 0.9159 0.7462 0.2047 -0.1186 -0.0040 1 ASP A O 5 C CB . ASP A 1 ? 0.8772 1.0469 0.7545 0.2583 -0.1389 -0.0132 1 ASP A CB 6 C CG . ASP A 1 ? 0.9007 1.1009 0.7545 0.2919 -0.1490 -0.0129 1 ASP A CG 7 O OD1 . ASP A 1 ? 0.9305 1.0834 0.7437 0.3218 -0.1516 -0.0036 1 ASP A OD1 8 O OD2 . ASP A 1 ? 0.9098 1.1811 0.7832 0.2879 -0.1539 -0.0222 1 ASP A OD2 9 N N . GLN A 2 ? 0.8798 0.9591 0.7682 0.2382 -0.1233 -0.0065 2 GLN A N 10 C CA . GLN A 2 ? 0.8507 0.9190 0.7647 0.2103 -0.1152 -0.0085 2 GLN A CA 11 C C . GLN A 2 ? 0.8050 0.9155 0.7435 0.2120 -0.1159 -0.0159 2 GLN A C 12 O O . GLN A 2 ? 0.7985 0.9370 0.7296 0.2397 -0.1221 -0.0182 2 GLN A O 13 C CB . GLN A 2 ? 0.9012 0.8976 0.7934 0.2063 -0.1088 0.0006 2 GLN A CB 14 C CG . GLN A 2 ? 0.9623 0.9224 0.8211 0.2349 -0.1109 0.0059 2 GLN A CG 15 C CD . GLN A 2 ? 1.0262 0.9130 0.8574 0.2250 -0.1037 0.0143 2 GLN A CD 16 O OE1 . GLN A 2 ? 1.0433 0.9038 0.8699 0.2241 -0.0998 0.0155 2 GLN A OE1 17 N NE2 . GLN A 2 ? 1.0678 0.9237 0.8796 0.2158 -0.1016 0.0195 2 GLN A NE2 18 N N . ILE A 3 ? 0.7388 0.8531 0.7045 0.1831 -0.1091 -0.0195 3 ILE A N 19 C CA . ILE A 3 ? 0.7165 0.8601 0.7045 0.1788 -0.1076 -0.0256 3 ILE A CA 20 C C . ILE A 3 ? 0.7103 0.8068 0.7020 0.1635 -0.0996 -0.0211 3 ILE A C 21 O O . ILE A 3 ? 0.6972 0.7629 0.6898 0.1436 -0.0940 -0.0176 3 ILE A O 22 C CB . ILE A 3 ? 0.7079 0.9115 0.7240 0.1570 -0.1071 -0.0365 3 ILE A CB 23 C CG1 . ILE A 3 ? 0.7047 0.9431 0.7399 0.1553 -0.1062 -0.0432 3 ILE A CG1 24 C CG2 . ILE A 3 ? 0.6892 0.8721 0.7153 0.1244 -0.0997 -0.0368 3 ILE A CG2 25 C CD1 . ILE A 3 ? 0.7043 1.0112 0.7594 0.1390 -0.1073 -0.0551 3 ILE A CD1 26 N N . CYS A 4 ? 0.7079 0.8019 0.7009 0.1742 -0.0993 -0.0214 4 CYS A N 27 C CA . CYS A 4 ? 0.6968 0.7474 0.6896 0.1638 -0.0926 -0.0170 4 CYS A CA 28 C C . CYS A 4 ? 0.6665 0.7478 0.6859 0.1533 -0.0900 -0.0234 4 CYS A C 29 O O . CYS A 4 ? 0.6624 0.7916 0.6920 0.1630 -0.0942 -0.0301 4 CYS A O 30 C CB . CYS A 4 ? 0.7503 0.7558 0.7106 0.1875 -0.0939 -0.0103 4 CYS A CB 31 S SG . CYS A 4 ? 0.8365 0.7957 0.7553 0.2013 -0.0964 -0.0019 4 CYS A SG 32 N N . ILE A 5 ? 0.6334 0.6895 0.6626 0.1338 -0.0830 -0.0215 5 ILE A N 33 C CA . ILE A 5 ? 0.6045 0.6797 0.6541 0.1246 -0.0798 -0.0261 5 ILE A CA 34 C C . ILE A 5 ? 0.6094 0.6501 0.6476 0.1350 -0.0781 -0.0216 5 ILE A C 35 O O . ILE A 5 ? 0.6170 0.6124 0.6383 0.1331 -0.0753 -0.0151 5 ILE A O 36 C CB . ILE A 5 ? 0.5834 0.6559 0.6497 0.0965 -0.0730 -0.0276 5 ILE A CB 37 C CG1 . ILE A 5 ? 0.5949 0.6952 0.6666 0.0849 -0.0740 -0.0325 5 ILE A CG1 38 C CG2 . ILE A 5 ? 0.5687 0.6564 0.6521 0.0870 -0.0693 -0.0318 5 ILE A CG2 39 C CD1 . ILE A 5 ? 0.6005 0.7560 0.6845 0.0835 -0.0770 -0.0419 5 ILE A CD1 40 N N . GLY A 6 ? 0.6093 0.6729 0.6550 0.1449 -0.0795 -0.0258 6 GLY A N 41 C CA . GLY A 6 ? 0.6346 0.6660 0.6677 0.1552 -0.0777 -0.0226 6 GLY A CA 42 C C . GLY A 6 ? 0.6134 0.6745 0.6647 0.1551 -0.0768 -0.0283 6 GLY A C 43 O O . GLY A 6 ? 0.6245 0.7301 0.6986 0.1434 -0.0765 -0.0348 6 GLY A O 44 N N . TYR A 7 ? 0.6190 0.6534 0.6571 0.1668 -0.0757 -0.0261 7 TYR A N 45 C CA . TYR A 7 ? 0.6145 0.6709 0.6680 0.1661 -0.0740 -0.0308 7 TYR A CA 46 C C . TYR A 7 ? 0.6514 0.6944 0.6824 0.1946 -0.0769 -0.0307 7 TYR A C 47 O O . TYR A 7 ? 0.6769 0.6800 0.6756 0.2123 -0.0788 -0.0258 7 TYR A O 48 C CB . TYR A 7 ? 0.6200 0.6529 0.6849 0.1422 -0.0670 -0.0285 7 TYR A CB 49 C CG . TYR A 7 ? 0.6462 0.6226 0.6886 0.1394 -0.0638 -0.0213 7 TYR A CG 50 C CD1 . TYR A 7 ? 0.6448 0.5993 0.6808 0.1275 -0.0621 -0.0168 7 TYR A CD1 51 C CD2 . TYR A 7 ? 0.6963 0.6429 0.7225 0.1468 -0.0619 -0.0199 7 TYR A CD2 52 C CE1 . TYR A 7 ? 0.6947 0.6027 0.7090 0.1220 -0.0587 -0.0113 7 TYR A CE1 53 C CE2 . TYR A 7 ? 0.7140 0.6105 0.7167 0.1400 -0.0582 -0.0145 7 TYR A CE2 54 C CZ . TYR A 7 ? 0.7140 0.5934 0.7113 0.1268 -0.0565 -0.0103 7 TYR A CZ 55 O OH . TYR A 7 ? 0.7566 0.5911 0.7295 0.1172 -0.0523 -0.0059 7 TYR A OH 56 N N . HIS A 8 ? 0.6463 0.7202 0.6917 0.1986 -0.0766 -0.0363 8 HIS A N 57 C CA . HIS A 8 ? 0.6919 0.7656 0.7191 0.2282 -0.0795 -0.0383 8 HIS A CA 58 C C . HIS A 8 ? 0.7456 0.7537 0.7445 0.2322 -0.0756 -0.0327 8 HIS A C 59 O O . HIS A 8 ? 0.7402 0.7238 0.7473 0.2082 -0.0699 -0.0303 8 HIS A O 60 C CB . HIS A 8 ? 0.6720 0.8025 0.7270 0.2250 -0.0791 -0.0467 8 HIS A CB 61 C CG . HIS A 8 ? 0.6981 0.8396 0.7388 0.2561 -0.0819 -0.0502 8 HIS A CG 62 N ND1 . HIS A 8 ? 0.7258 0.8929 0.7500 0.2899 -0.0885 -0.0529 8 HIS A ND1 63 C CD2 . HIS A 8 ? 0.6937 0.8284 0.7343 0.2597 -0.0789 -0.0523 8 HIS A CD2 64 C CE1 . HIS A 8 ? 0.7349 0.9081 0.7477 0.3148 -0.0894 -0.0562 8 HIS A CE1 65 N NE2 . HIS A 8 ? 0.7109 0.8640 0.7337 0.2960 -0.0835 -0.0560 8 HIS A NE2 66 N N . ALA A 9 ? 0.8024 0.7818 0.7647 0.2631 -0.0785 -0.0311 9 ALA A N 67 C CA . ALA A 9 ? 0.8275 0.7467 0.7571 0.2697 -0.0745 -0.0279 9 ALA A CA 68 C C . ALA A 9 ? 0.8617 0.7916 0.7717 0.3068 -0.0782 -0.0320 9 ALA A C 69 O O . ALA A 9 ? 0.8690 0.8458 0.7834 0.3304 -0.0844 -0.0358 9 ALA A O 70 C CB . ALA A 9 ? 0.8471 0.6971 0.7359 0.2683 -0.0725 -0.0202 9 ALA A CB 71 N N . ASN A 10 ? 0.8835 0.7740 0.7718 0.3121 -0.0743 -0.0319 10 ASN A N 72 C CA . ASN A 10 ? 0.9234 0.8165 0.7874 0.3497 -0.0770 -0.0357 10 ASN A CA 73 C C . ASN A 10 ? 1.0018 0.8164 0.8202 0.3542 -0.0714 -0.0327 10 ASN A C 74 O O . ASN A 10 ? 0.9977 0.7581 0.8010 0.3285 -0.0660 -0.0275 10 ASN A O 75 C CB . ASN A 10 ? 0.8689 0.8405 0.7763 0.3501 -0.0786 -0.0444 10 ASN A CB 76 C CG . ASN A 10 ? 0.8361 0.8049 0.7677 0.3200 -0.0723 -0.0458 10 ASN A CG 77 O OD1 . ASN A 10 ? 0.8505 0.7610 0.7654 0.3019 -0.0670 -0.0410 10 ASN A OD1 78 N ND2 . ASN A 10 ? 0.7961 0.8300 0.7658 0.3136 -0.0727 -0.0528 10 ASN A ND2 79 N N . ASN A 11 ? 1.1027 0.9127 0.8975 0.3860 -0.0723 -0.0365 11 ASN A N 80 C CA . ASN A 11 ? 1.2240 0.9534 0.9666 0.3934 -0.0667 -0.0343 11 ASN A CA 81 C C . ASN A 11 ? 1.1584 0.8885 0.9223 0.3676 -0.0608 -0.0376 11 ASN A C 82 O O . ASN A 11 ? 1.2177 0.8918 0.9419 0.3749 -0.0563 -0.0379 11 ASN A O 83 C CB . ASN A 11 ? 1.3615 1.0713 1.0551 0.4460 -0.0702 -0.0360 11 ASN A CB 84 C CG . ASN A 11 ? 1.4665 1.2565 1.1922 0.4703 -0.0746 -0.0447 11 ASN A CG 85 O OD1 . ASN A 11 ? 1.4108 1.2552 1.1875 0.4454 -0.0732 -0.0496 11 ASN A OD1 86 N ND2 . ASN A 11 ? 1.6857 1.4838 1.3789 0.5203 -0.0798 -0.0469 11 ASN A ND2 87 N N . SER A 12 ? 1.0505 0.8402 0.8729 0.3375 -0.0605 -0.0401 12 SER A N 88 C CA . SER A 12 ? 0.9919 0.7920 0.8387 0.3146 -0.0557 -0.0433 12 SER A CA 89 C C . SER A 12 ? 1.0098 0.7418 0.8316 0.2871 -0.0485 -0.0391 12 SER A C 90 O O . SER A 12 ? 0.9792 0.6813 0.7916 0.2680 -0.0469 -0.0338 12 SER A O 91 C CB . SER A 12 ? 0.9122 0.7848 0.8209 0.2886 -0.0566 -0.0460 12 SER A CB 92 O OG . SER A 12 ? 0.8648 0.7446 0.7947 0.2664 -0.0518 -0.0483 12 SER A OG 93 N N . THR A 13 ? 1.0167 0.7285 0.8273 0.2849 -0.0442 -0.0423 13 THR A N 94 C CA . THR A 13 ? 1.0369 0.6963 0.8285 0.2555 -0.0371 -0.0403 13 THR A CA 95 C C . THR A 13 ? 0.9953 0.6964 0.8319 0.2294 -0.0344 -0.0435 13 THR A C 96 O O . THR A 13 ? 0.9807 0.6503 0.8066 0.2054 -0.0288 -0.0432 13 THR A O 97 C CB . THR A 13 ? 1.1289 0.7161 0.8578 0.2733 -0.0330 -0.0416 13 THR A CB 98 O OG1 . THR A 13 ? 1.1349 0.7503 0.8718 0.2961 -0.0342 -0.0477 13 THR A OG1 99 C CG2 . THR A 13 ? 1.1856 0.7198 0.8592 0.3020 -0.0348 -0.0379 13 THR A CG2 100 N N . GLU A 14 ? 0.9558 0.7273 0.8395 0.2336 -0.0382 -0.0469 14 GLU A N 101 C CA . GLU A 14 ? 0.9402 0.7518 0.8661 0.2090 -0.0358 -0.0490 14 GLU A CA 102 C C . GLU A 14 ? 0.8834 0.6865 0.8236 0.1748 -0.0328 -0.0443 14 GLU A C 103 O O . GLU A 14 ? 0.8577 0.6588 0.7996 0.1697 -0.0345 -0.0403 14 GLU A O 104 C CB . GLU A 14 ? 0.9634 0.8485 0.9329 0.2151 -0.0399 -0.0529 14 GLU A CB 105 C CG . GLU A 14 ? 1.0320 0.9440 0.9959 0.2470 -0.0427 -0.0591 14 GLU A CG 106 C CD . GLU A 14 ? 1.1220 1.0232 1.0782 0.2486 -0.0388 -0.0631 14 GLU A CD 107 O OE1 . GLU A 14 ? 1.1453 1.0577 1.1256 0.2220 -0.0352 -0.0631 14 GLU A OE1 108 O OE2 . GLU A 14 ? 1.2289 1.1090 1.1524 0.2780 -0.0393 -0.0663 14 GLU A OE2 109 N N . GLN A 15 ? 0.8551 0.6552 0.8042 0.1530 -0.0283 -0.0450 15 GLN A N 110 C CA . GLN A 15 ? 0.8333 0.6301 0.7943 0.1228 -0.0252 -0.0413 15 GLN A CA 111 C C . GLN A 15 ? 0.7684 0.6116 0.7708 0.1074 -0.0242 -0.0425 15 GLN A C 112 O O . GLN A 15 ? 0.7542 0.6155 0.7661 0.1133 -0.0238 -0.0464 15 GLN A O 113 C CB . GLN A 15 ? 0.8969 0.6407 0.8208 0.1082 -0.0198 -0.0411 15 GLN A CB 114 C CG . GLN A 15 ? 0.9841 0.6672 0.8551 0.1210 -0.0190 -0.0400 15 GLN A CG 115 C CD . GLN A 15 ? 1.0525 0.6824 0.8843 0.0988 -0.0123 -0.0404 15 GLN A CD 116 O OE1 . GLN A 15 ? 1.1143 0.6976 0.9082 0.0927 -0.0100 -0.0379 15 GLN A OE1 117 N NE2 . GLN A 15 ? 1.0703 0.7077 0.9093 0.0847 -0.0088 -0.0441 15 GLN A NE2 118 N N . VAL A 16 ? 0.7353 0.5954 0.7589 0.0887 -0.0235 -0.0390 16 VAL A N 119 C CA . VAL A 16 ? 0.6843 0.5800 0.7399 0.0745 -0.0220 -0.0390 16 VAL A CA 120 C C . VAL A 16 ? 0.6819 0.5688 0.7365 0.0530 -0.0187 -0.0359 16 VAL A C 121 O O . VAL A 16 ? 0.6803 0.5433 0.7172 0.0474 -0.0182 -0.0335 16 VAL A O 122 C CB . VAL A 16 ? 0.6461 0.5805 0.7305 0.0765 -0.0245 -0.0383 16 VAL A CB 123 C CG1 . VAL A 16 ? 0.6560 0.6088 0.7423 0.0965 -0.0279 -0.0424 16 VAL A CG1 124 C CG2 . VAL A 16 ? 0.6441 0.5732 0.7288 0.0706 -0.0256 -0.0341 16 VAL A CG2 125 N N . ASP A 17 ? 0.6672 0.5761 0.7399 0.0416 -0.0164 -0.0362 17 ASP A N 126 C CA . ASP A 17 ? 0.6568 0.5704 0.7328 0.0234 -0.0137 -0.0337 17 ASP A CA 127 C C . ASP A 17 ? 0.6174 0.5605 0.7185 0.0211 -0.0144 -0.0303 17 ASP A C 128 O O . ASP A 17 ? 0.5653 0.5276 0.6831 0.0282 -0.0156 -0.0306 17 ASP A O 129 C CB . ASP A 17 ? 0.6803 0.5989 0.7556 0.0139 -0.0108 -0.0362 17 ASP A CB 130 C CG . ASP A 17 ? 0.7477 0.6300 0.7910 0.0110 -0.0086 -0.0399 17 ASP A CG 131 O OD1 . ASP A 17 ? 0.7616 0.6111 0.7788 0.0096 -0.0081 -0.0394 17 ASP A OD1 132 O OD2 . ASP A 17 ? 0.7737 0.6574 0.8148 0.0094 -0.0069 -0.0432 17 ASP A OD2 133 N N . THR A 18 ? 0.6257 0.5712 0.7260 0.0105 -0.0131 -0.0275 18 THR A N 134 C CA . THR A 18 ? 0.5997 0.5694 0.7180 0.0087 -0.0128 -0.0243 18 THR A CA 135 C C . THR A 18 ? 0.6088 0.5929 0.7272 -0.0028 -0.0100 -0.0237 18 THR A C 136 O O . THR A 18 ? 0.6630 0.6389 0.7681 -0.0126 -0.0083 -0.0262 18 THR A O 137 C CB . THR A 18 ? 0.5992 0.5637 0.7163 0.0108 -0.0143 -0.0216 18 THR A CB 138 O OG1 . THR A 18 ? 0.6400 0.5902 0.7407 0.0013 -0.0131 -0.0212 18 THR A OG1 139 C CG2 . THR A 18 ? 0.5974 0.5523 0.7128 0.0222 -0.0175 -0.0228 18 THR A CG2 140 N N . ILE A 19 ? 0.6412 0.6469 0.7717 -0.0014 -0.0093 -0.0208 19 ILE A N 141 C CA . ILE A 19 ? 0.6408 0.6694 0.7724 -0.0086 -0.0072 -0.0204 19 ILE A CA 142 C C . ILE A 19 ? 0.6700 0.6963 0.7891 -0.0215 -0.0060 -0.0216 19 ILE A C 143 O O . ILE A 19 ? 0.6892 0.7276 0.8015 -0.0342 -0.0038 -0.0243 19 ILE A O 144 C CB . ILE A 19 ? 0.6952 0.7430 0.8368 0.0006 -0.0067 -0.0165 19 ILE A CB 145 C CG1 . ILE A 19 ? 0.7184 0.7658 0.8666 0.0098 -0.0065 -0.0154 19 ILE A CG1 146 C CG2 . ILE A 19 ? 0.7054 0.7830 0.8472 -0.0029 -0.0050 -0.0163 19 ILE A CG2 147 C CD1 . ILE A 19 ? 0.7065 0.7667 0.8561 0.0082 -0.0055 -0.0168 19 ILE A CD1 148 N N . MET A 20 ? 0.6774 0.6893 0.7919 -0.0200 -0.0070 -0.0199 20 MET A N 149 C CA . MET A 20 ? 0.6987 0.7085 0.8002 -0.0329 -0.0053 -0.0205 20 MET A CA 150 C C . MET A 20 ? 0.7272 0.7003 0.8043 -0.0423 -0.0046 -0.0229 20 MET A C 151 O O . MET A 20 ? 0.7418 0.7086 0.8019 -0.0577 -0.0020 -0.0242 20 MET A O 152 C CB . MET A 20 ? 0.7065 0.7186 0.8129 -0.0263 -0.0064 -0.0172 20 MET A CB 153 C CG . MET A 20 ? 0.7128 0.7580 0.8328 -0.0196 -0.0056 -0.0151 20 MET A CG 154 S SD . MET A 20 ? 0.7687 0.8121 0.8887 -0.0143 -0.0060 -0.0122 20 MET A SD 155 C CE . MET A 20 ? 0.7964 0.8842 0.9211 -0.0144 -0.0033 -0.0123 20 MET A CE 156 N N . GLU A 21 ? 0.7183 0.6661 0.7903 -0.0328 -0.0065 -0.0237 21 GLU A N 157 C CA . GLU A 21 ? 0.7492 0.6553 0.7924 -0.0356 -0.0060 -0.0253 21 GLU A CA 158 C C . GLU A 21 ? 0.7481 0.6371 0.7860 -0.0254 -0.0070 -0.0277 21 GLU A C 159 O O . GLU A 21 ? 0.7197 0.6236 0.7775 -0.0110 -0.0098 -0.0272 21 GLU A O 160 C CB . GLU A 21 ? 0.7653 0.6534 0.8026 -0.0264 -0.0085 -0.0223 21 GLU A CB 161 C CG . GLU A 21 ? 0.8571 0.6994 0.8567 -0.0321 -0.0069 -0.0229 21 GLU A CG 162 C CD . GLU A 21 ? 0.9075 0.7336 0.9000 -0.0220 -0.0097 -0.0196 21 GLU A CD 163 O OE1 . GLU A 21 ? 0.8657 0.7190 0.8829 -0.0158 -0.0121 -0.0172 21 GLU A OE1 164 O OE2 . GLU A 21 ? 0.9105 0.6935 0.8690 -0.0200 -0.0091 -0.0195 21 GLU A OE2 165 N N . LYS A 22 ? 0.7968 0.6531 0.8046 -0.0340 -0.0043 -0.0309 22 LYS A N 166 C CA . LYS A 22 ? 0.8391 0.6763 0.8369 -0.0237 -0.0046 -0.0339 22 LYS A CA 167 C C . LYS A 22 ? 0.8335 0.6245 0.7998 -0.0110 -0.0056 -0.0337 22 LYS A C 168 O O . LYS A 22 ? 0.8480 0.6127 0.7909 -0.0179 -0.0043 -0.0321 22 LYS A O 169 C CB . LYS A 22 ? 0.9199 0.7541 0.9042 -0.0417 -0.0002 -0.0382 22 LYS A CB 170 C CG . LYS A 22 ? 0.9548 0.8393 0.9707 -0.0491 -0.0001 -0.0381 22 LYS A CG 171 C CD . LYS A 22 ? 1.0619 0.9513 1.0655 -0.0691 0.0041 -0.0428 22 LYS A CD 172 C CE . LYS A 22 ? 1.1235 1.0058 1.1262 -0.0612 0.0041 -0.0459 22 LYS A CE 173 N NZ . LYS A 22 ? 1.1343 1.0317 1.1312 -0.0807 0.0076 -0.0505 22 LYS A NZ 174 N N . ASN A 23 ? 0.8176 0.6008 0.7827 0.0093 -0.0081 -0.0354 23 ASN A N 175 C CA . ASN A 23 ? 0.8801 0.6198 0.8112 0.0269 -0.0092 -0.0356 23 ASN A CA 176 C C . ASN A 23 ? 0.8573 0.5940 0.7880 0.0371 -0.0127 -0.0316 23 ASN A C 177 O O . ASN A 23 ? 0.8914 0.5845 0.7850 0.0379 -0.0114 -0.0302 23 ASN A O 178 C CB . ASN A 23 ? 0.9696 0.6535 0.8506 0.0137 -0.0036 -0.0380 23 ASN A CB 179 C CG . ASN A 23 ? 1.0381 0.7200 0.9140 0.0061 -0.0004 -0.0429 23 ASN A CG 180 O OD1 . ASN A 23 ? 1.0008 0.7207 0.9093 0.0144 -0.0026 -0.0442 23 ASN A OD1 181 N ND2 . ASN A 23 ? 1.2027 0.8385 1.0349 -0.0113 0.0055 -0.0459 23 ASN A ND2 182 N N . VAL A 24 ? 0.8246 0.6053 0.7937 0.0440 -0.0166 -0.0299 24 VAL A N 183 C CA . VAL A 24 ? 0.7921 0.5769 0.7649 0.0549 -0.0204 -0.0268 24 VAL A CA 184 C C . VAL A 24 ? 0.7866 0.5685 0.7519 0.0827 -0.0246 -0.0286 24 VAL A C 185 O O . VAL A 24 ? 0.7534 0.5651 0.7398 0.0921 -0.0263 -0.0317 24 VAL A O 186 C CB . VAL A 24 ? 0.7566 0.5883 0.7702 0.0490 -0.0221 -0.0251 24 VAL A CB 187 C CG1 . VAL A 24 ? 0.7727 0.6085 0.7888 0.0582 -0.0257 -0.0225 24 VAL A CG1 188 C CG2 . VAL A 24 ? 0.7385 0.5802 0.7603 0.0262 -0.0181 -0.0237 24 VAL A CG2 189 N N . THR A 25 ? 0.8074 0.5547 0.7405 0.0964 -0.0262 -0.0270 25 THR A N 190 C CA . THR A 25 ? 0.8069 0.5556 0.7302 0.1269 -0.0308 -0.0288 25 THR A CA 191 C C . THR A 25 ? 0.7716 0.5716 0.7308 0.1344 -0.0358 -0.0288 25 THR A C 192 O O . THR A 25 ? 0.7791 0.5836 0.7454 0.1255 -0.0367 -0.0254 25 THR A O 193 C CB . THR A 25 ? 0.8710 0.5633 0.7430 0.1424 -0.0310 -0.0266 25 THR A CB 194 O OG1 . THR A 25 ? 0.9373 0.5749 0.7699 0.1286 -0.0248 -0.0267 25 THR A OG1 195 C CG2 . THR A 25 ? 0.9096 0.6045 0.7674 0.1787 -0.0355 -0.0292 25 THR A CG2 196 N N . VAL A 26 ? 0.7365 0.5755 0.7164 0.1489 -0.0387 -0.0331 26 VAL A N 197 C CA . VAL A 26 ? 0.6925 0.5829 0.7040 0.1529 -0.0427 -0.0346 26 VAL A CA 198 C C . VAL A 26 ? 0.7224 0.6320 0.7256 0.1831 -0.0478 -0.0384 26 VAL A C 199 O O . VAL A 26 ? 0.7701 0.6604 0.7493 0.2025 -0.0478 -0.0406 26 VAL A O 200 C CB . VAL A 26 ? 0.6386 0.5717 0.6880 0.1362 -0.0408 -0.0372 26 VAL A CB 201 C CG1 . VAL A 26 ? 0.6111 0.5339 0.6705 0.1104 -0.0368 -0.0331 26 VAL A CG1 202 C CG2 . VAL A 26 ? 0.6507 0.5907 0.7009 0.1427 -0.0392 -0.0416 26 VAL A CG2 203 N N . THR A 27 ? 0.7168 0.6661 0.7384 0.1874 -0.0519 -0.0395 27 THR A N 204 C CA . THR A 27 ? 0.7144 0.6938 0.7306 0.2163 -0.0574 -0.0437 27 THR A CA 205 C C . THR A 27 ? 0.7107 0.7365 0.7461 0.2238 -0.0576 -0.0509 27 THR A C 206 O O . THR A 27 ? 0.7555 0.7936 0.7761 0.2529 -0.0608 -0.0549 27 THR A O 207 C CB . THR A 27 ? 0.6943 0.7103 0.7269 0.2145 -0.0615 -0.0440 27 THR A CB 208 O OG1 . THR A 27 ? 0.6326 0.6904 0.7023 0.1888 -0.0594 -0.0467 27 THR A OG1 209 C CG2 . THR A 27 ? 0.7056 0.6775 0.7177 0.2092 -0.0615 -0.0371 27 THR A CG2 210 N N . HIS A 28 ? 0.6826 0.7339 0.7487 0.1985 -0.0539 -0.0527 28 HIS A N 211 C CA . HIS A 28 ? 0.6681 0.7634 0.7537 0.1994 -0.0529 -0.0595 28 HIS A CA 212 C C . HIS A 28 ? 0.6685 0.7530 0.7685 0.1740 -0.0472 -0.0582 28 HIS A C 213 O O . HIS A 28 ? 0.6519 0.7207 0.7604 0.1512 -0.0445 -0.0536 28 HIS A O 214 C CB . HIS A 28 ? 0.6489 0.8096 0.7609 0.1945 -0.0553 -0.0652 28 HIS A CB 215 C CG . HIS A 28 ? 0.6818 0.8630 0.7834 0.2178 -0.0614 -0.0669 28 HIS A CG 216 N ND1 . HIS A 28 ? 0.6726 0.8371 0.7684 0.2135 -0.0635 -0.0622 28 HIS A ND1 217 C CD2 . HIS A 28 ? 0.6875 0.9059 0.7818 0.2478 -0.0661 -0.0727 28 HIS A CD2 218 C CE1 . HIS A 28 ? 0.6889 0.8786 0.7744 0.2390 -0.0694 -0.0648 28 HIS A CE1 219 N NE2 . HIS A 28 ? 0.6917 0.9156 0.7759 0.2612 -0.0712 -0.0713 28 HIS A NE2 220 N N . ALA A 29 ? 0.6837 0.7796 0.7855 0.1799 -0.0454 -0.0625 29 ALA A N 221 C CA . ALA A 29 ? 0.6771 0.7656 0.7903 0.1594 -0.0402 -0.0618 29 ALA A CA 222 C C . ALA A 29 ? 0.6694 0.8015 0.7972 0.1633 -0.0392 -0.0690 29 ALA A C 223 O O . ALA A 29 ? 0.7078 0.8710 0.8326 0.1854 -0.0424 -0.0747 29 ALA A O 224 C CB . ALA A 29 ? 0.7145 0.7467 0.8024 0.1607 -0.0379 -0.0579 29 ALA A CB 225 N N . GLN A 30 ? 0.6463 0.7829 0.7888 0.1427 -0.0347 -0.0688 30 GLN A N 226 C CA . GLN A 30 ? 0.6570 0.8320 0.8124 0.1423 -0.0326 -0.0753 30 GLN A CA 227 C C . GLN A 30 ? 0.6396 0.7872 0.7915 0.1331 -0.0283 -0.0734 30 GLN A C 228 O O . GLN A 30 ? 0.5693 0.7017 0.7284 0.1117 -0.0251 -0.0688 30 GLN A O 229 C CB . GLN A 30 ? 0.6499 0.8708 0.8286 0.1219 -0.0308 -0.0785 30 GLN A CB 230 C CG . GLN A 30 ? 0.6653 0.9272 0.8563 0.1167 -0.0276 -0.0855 30 GLN A CG 231 C CD . GLN A 30 ? 0.6572 0.9678 0.8646 0.0971 -0.0256 -0.0906 30 GLN A CD 232 O OE1 . GLN A 30 ? 0.7051 1.0303 0.9149 0.0939 -0.0279 -0.0912 30 GLN A OE1 233 N NE2 . GLN A 30 ? 0.6630 0.9980 0.8790 0.0822 -0.0208 -0.0948 30 GLN A NE2 234 N N . ASP A 31 ? 0.6664 0.8076 0.8046 0.1514 -0.0285 -0.0771 31 ASP A N 235 C CA . ASP A 31 ? 0.6923 0.8141 0.8264 0.1446 -0.0246 -0.0770 31 ASP A CA 236 C C . ASP A 31 ? 0.6624 0.8277 0.8201 0.1297 -0.0214 -0.0809 31 ASP A C 237 O O . ASP A 31 ? 0.6654 0.8775 0.8338 0.1366 -0.0223 -0.0873 31 ASP A O 238 C CB . ASP A 31 ? 0.7269 0.8295 0.8356 0.1707 -0.0254 -0.0809 31 ASP A CB 239 C CG . ASP A 31 ? 0.7800 0.8542 0.8787 0.1634 -0.0213 -0.0809 31 ASP A CG 240 O OD1 . ASP A 31 ? 0.7377 0.8147 0.8522 0.1396 -0.0182 -0.0782 31 ASP A OD1 241 O OD2 . ASP A 31 ? 0.8719 0.9188 0.9436 0.1828 -0.0211 -0.0837 31 ASP A OD2 242 N N . ILE A 32 ? 0.6259 0.7774 0.7898 0.1092 -0.0175 -0.0772 32 ILE A N 243 C CA . ILE A 32 ? 0.6190 0.8032 0.7999 0.0933 -0.0136 -0.0798 32 ILE A CA 244 C C . ILE A 32 ? 0.6273 0.8025 0.8049 0.0908 -0.0103 -0.0809 32 ILE A C 245 O O . ILE A 32 ? 0.6095 0.8039 0.7976 0.0760 -0.0065 -0.0818 32 ILE A O 246 C CB . ILE A 32 ? 0.6023 0.7836 0.7927 0.0701 -0.0113 -0.0745 32 ILE A CB 247 C CG1 . ILE A 32 ? 0.5854 0.7244 0.7679 0.0630 -0.0107 -0.0668 32 ILE A CG1 248 C CG2 . ILE A 32 ? 0.6093 0.8063 0.8039 0.0703 -0.0140 -0.0750 32 ILE A CG2 249 C CD1 . ILE A 32 ? 0.5750 0.7100 0.7632 0.0440 -0.0076 -0.0617 32 ILE A CD1 250 N N . LEU A 33 ? 0.6438 0.7875 0.8034 0.1043 -0.0112 -0.0810 33 LEU A N 251 C CA . LEU A 33 ? 0.6674 0.7984 0.8204 0.1021 -0.0082 -0.0823 33 LEU A CA 252 C C . LEU A 33 ? 0.7085 0.8449 0.8484 0.1253 -0.0088 -0.0896 33 LEU A C 253 O O . LEU A 33 ? 0.7301 0.8404 0.8483 0.1445 -0.0113 -0.0904 33 LEU A O 254 C CB . LEU A 33 ? 0.6814 0.7661 0.8191 0.0944 -0.0077 -0.0769 33 LEU A CB 255 C CG . LEU A 33 ? 0.6910 0.7593 0.8190 0.0896 -0.0046 -0.0784 33 LEU A CG 256 C CD1 . LEU A 33 ? 0.6643 0.7581 0.8109 0.0734 -0.0016 -0.0772 33 LEU A CD1 257 C CD2 . LEU A 33 ? 0.7112 0.7374 0.8205 0.0813 -0.0042 -0.0746 33 LEU A CD2 258 N N . GLU A 34 ? 0.7250 0.8926 0.8745 0.1243 -0.0062 -0.0948 34 GLU A N 259 C CA . GLU A 34 ? 0.7608 0.9351 0.8971 0.1471 -0.0061 -0.1021 34 GLU A CA 260 C C . GLU A 34 ? 0.7768 0.9039 0.8902 0.1479 -0.0039 -0.1013 34 GLU A C 261 O O . GLU A 34 ? 0.7720 0.8931 0.8916 0.1286 -0.0009 -0.0990 34 GLU A O 262 C CB . GLU A 34 ? 0.7582 0.9871 0.9131 0.1441 -0.0035 -0.1086 34 GLU A CB 263 C CG . GLU A 34 ? 0.7810 1.0235 0.9232 0.1702 -0.0034 -0.1170 34 GLU A CG 264 C CD . GLU A 34 ? 0.8287 1.0658 0.9526 0.2018 -0.0078 -0.1197 34 GLU A CD 265 O OE1 . GLU A 34 ? 0.8464 1.1225 0.9832 0.2068 -0.0107 -0.1214 34 GLU A OE1 266 O OE2 . GLU A 34 ? 0.9096 1.1010 1.0029 0.2214 -0.0081 -0.1201 34 GLU A OE2 267 N N . LYS A 35 ? 0.8115 0.9038 0.8948 0.1704 -0.0052 -0.1036 35 LYS A N 268 C CA . LYS A 35 ? 0.8423 0.8815 0.8958 0.1695 -0.0026 -0.1035 35 LYS A CA 269 C C . LYS A 35 ? 0.8463 0.8828 0.8800 0.1912 -0.0006 -0.1114 35 LYS A C 270 O O . LYS A 35 ? 0.8510 0.8488 0.8615 0.1868 0.0027 -0.1127 35 LYS A O 271 C CB . LYS A 35 ? 0.8840 0.8688 0.9074 0.1743 -0.0040 -0.0996 35 LYS A CB 272 C CG . LYS A 35 ? 0.8776 0.8492 0.9118 0.1474 -0.0041 -0.0920 35 LYS A CG 273 C CD . LYS A 35 ? 0.9290 0.8538 0.9346 0.1526 -0.0056 -0.0886 35 LYS A CD 274 C CE . LYS A 35 ? 0.9376 0.8858 0.9623 0.1549 -0.0097 -0.0845 35 LYS A CE 275 N NZ . LYS A 35 ? 0.9241 0.9206 0.9662 0.1752 -0.0127 -0.0886 35 LYS A NZ 276 N N . THR A 36 ? 0.8298 0.9100 0.8719 0.2140 -0.0023 -0.1172 36 THR A N 277 C CA . THR A 36 ? 0.9045 0.9846 0.9252 0.2406 -0.0007 -0.1252 36 THR A CA 278 C C . THR A 36 ? 0.9076 1.0464 0.9558 0.2353 0.0016 -0.1309 36 THR A C 279 O O . THR A 36 ? 0.8610 1.0500 0.9440 0.2174 0.0013 -0.1299 36 THR A O 280 C CB . THR A 36 ? 0.9316 1.0181 0.9331 0.2788 -0.0044 -0.1290 36 THR A CB 281 O OG1 . THR A 36 ? 0.9132 1.0742 0.9498 0.2815 -0.0072 -0.1318 36 THR A OG1 282 C CG2 . THR A 36 ? 0.9592 0.9883 0.9321 0.2840 -0.0067 -0.1229 36 THR A CG2 283 N N . HIS A 37 ? 0.9306 1.0584 0.9586 0.2503 0.0045 -0.1372 37 HIS A N 284 C CA . HIS A 37 ? 0.9162 1.0976 0.9636 0.2507 0.0072 -0.1441 37 HIS A CA 285 C C . HIS A 37 ? 0.9630 1.1380 0.9794 0.2891 0.0080 -0.1527 37 HIS A C 286 O O . HIS A 37 ? 0.9982 1.1160 0.9744 0.3110 0.0072 -0.1523 37 HIS A O 287 C CB . HIS A 37 ? 0.8930 1.0635 0.9504 0.2197 0.0113 -0.1415 37 HIS A CB 288 C CG . HIS A 37 ? 0.9477 1.0515 0.9698 0.2192 0.0138 -0.1410 37 HIS A CG 289 N ND1 . HIS A 37 ? 0.9832 1.0770 0.9858 0.2306 0.0174 -0.1478 37 HIS A ND1 290 C CD2 . HIS A 37 ? 0.9706 1.0158 0.9719 0.2062 0.0138 -0.1352 37 HIS A CD2 291 C CE1 . HIS A 37 ? 1.0123 1.0417 0.9820 0.2237 0.0196 -0.1465 37 HIS A CE1 292 N NE2 . HIS A 37 ? 1.0094 1.0101 0.9780 0.2080 0.0176 -0.1390 37 HIS A NE2 293 N N . ASN A 38 ? 0.9451 1.1763 0.9763 0.2978 0.0099 -0.1607 38 ASN A N 294 C CA . ASN A 38 ? 0.9828 1.2159 0.9851 0.3385 0.0105 -0.1697 38 ASN A CA 295 C C . ASN A 38 ? 1.0187 1.2072 0.9935 0.3393 0.0156 -0.1730 38 ASN A C 296 O O . ASN A 38 ? 1.0837 1.2557 1.0248 0.3740 0.0168 -0.1799 38 ASN A O 297 C CB . ASN A 38 ? 0.9337 1.2596 0.9635 0.3540 0.0096 -0.1784 38 ASN A CB 298 C CG . ASN A 38 ? 0.8946 1.2702 0.9533 0.3297 0.0142 -0.1825 38 ASN A CG 299 O OD1 . ASN A 38 ? 0.8796 1.2232 0.9413 0.3009 0.0175 -0.1780 38 ASN A OD1 300 N ND2 . ASN A 38 ? 0.8671 1.3244 0.9462 0.3410 0.0145 -0.1914 38 ASN A ND2 301 N N . GLY A 39 ? 1.0157 1.1864 1.0034 0.3025 0.0185 -0.1684 39 GLY A N 302 C CA . GLY A 39 ? 1.0447 1.1658 1.0046 0.2973 0.0231 -0.1705 39 GLY A CA 303 C C . GLY A 39 ? 1.0524 1.2167 1.0211 0.3039 0.0267 -0.1790 39 GLY A C 304 O O . GLY A 39 ? 1.0579 1.1838 0.9959 0.3117 0.0305 -0.1835 39 GLY A O 305 N N . LYS A 40 ? 1.0269 1.2707 1.0356 0.2986 0.0261 -0.1816 40 LYS A N 306 C CA . LYS A 40 ? 0.9941 1.2921 1.0133 0.3072 0.0296 -0.1907 40 LYS A CA 307 C C . LYS A 40 ? 0.9446 1.2979 1.0059 0.2709 0.0317 -0.1888 40 LYS A C 308 O O . LYS A 40 ? 0.9303 1.2974 1.0161 0.2468 0.0298 -0.1819 40 LYS A O 309 C CB . LYS A 40 ? 1.0035 1.3540 1.0211 0.3463 0.0274 -0.1992 40 LYS A CB 310 C CG . LYS A 40 ? 1.0770 1.3732 1.0447 0.3901 0.0262 -0.2027 40 LYS A CG 311 C CD . LYS A 40 ? 1.0801 1.4324 1.0472 0.4313 0.0228 -0.2097 40 LYS A CD 312 C CE . LYS A 40 ? 1.1582 1.4450 1.0680 0.4774 0.0217 -0.2118 40 LYS A CE 313 N NZ . LYS A 40 ? 1.1944 1.5321 1.1016 0.5198 0.0170 -0.2169 40 LYS A NZ 314 N N . LEU A 41 ? 0.9628 1.3440 1.0286 0.2678 0.0362 -0.1950 41 LEU A N 315 C CA . LEU A 41 ? 0.9287 1.3677 1.0290 0.2377 0.0393 -0.1950 41 LEU A CA 316 C C . LEU A 41 ? 0.8790 1.4008 0.9969 0.2536 0.0395 -0.2044 41 LEU A C 317 O O . LEU A 41 ? 0.8685 1.4101 0.9712 0.2878 0.0400 -0.2140 41 LEU A O 318 C CB . LEU A 41 ? 0.9516 1.3781 1.0462 0.2241 0.0442 -0.1966 41 LEU A CB 319 C CG . LEU A 41 ? 0.9907 1.3407 1.0648 0.2103 0.0440 -0.1892 41 LEU A CG 320 C CD1 . LEU A 41 ? 1.0001 1.3441 1.0681 0.1986 0.0487 -0.1920 41 LEU A CD1 321 C CD2 . LEU A 41 ? 0.9734 1.3068 1.0644 0.1805 0.0415 -0.1777 41 LEU A CD2 322 N N . CYS A 42 ? 0.8315 1.4016 0.9788 0.2291 0.0395 -0.2023 42 CYS A N 323 C CA . CYS A 42 ? 0.8463 1.4986 1.0107 0.2405 0.0392 -0.2114 42 CYS A CA 324 C C . CYS A 42 ? 0.7783 1.4924 0.9692 0.2048 0.0445 -0.2139 42 CYS A C 325 O O . CYS A 42 ? 0.7427 1.4300 0.9394 0.1700 0.0476 -0.2062 42 CYS A O 326 C CB . CYS A 42 ? 0.8828 1.5366 1.0517 0.2476 0.0336 -0.2077 42 CYS A CB 327 S SG . CYS A 42 ? 0.9572 1.5310 1.0904 0.2854 0.0276 -0.2031 42 CYS A SG 328 N N . ASP A 43 ? 0.7585 1.5563 0.9627 0.2140 0.0459 -0.2251 43 ASP A N 329 C CA . ASP A 43 ? 0.7301 1.5926 0.9570 0.1772 0.0513 -0.2288 43 ASP A CA 330 C C . ASP A 43 ? 0.7109 1.5524 0.9473 0.1467 0.0498 -0.2193 43 ASP A C 331 O O . ASP A 43 ? 0.6928 1.5173 0.9271 0.1624 0.0439 -0.2160 43 ASP A O 332 C CB . ASP A 43 ? 0.7315 1.6948 0.9709 0.1933 0.0522 -0.2435 43 ASP A CB 333 C CG . ASP A 43 ? 0.7432 1.7351 0.9720 0.2287 0.0537 -0.2542 43 ASP A CG 334 O OD1 . ASP A 43 ? 0.7497 1.6998 0.9668 0.2264 0.0569 -0.2520 43 ASP A OD1 335 O OD2 . ASP A 43 ? 0.7523 1.8120 0.9837 0.2603 0.0516 -0.2654 43 ASP A OD2 336 N N . LEU A 44 ? 0.7273 1.5657 0.9703 0.1043 0.0555 -0.2147 44 LEU A N 337 C CA . LEU A 44 ? 0.7540 1.5765 1.0027 0.0731 0.0556 -0.2069 44 LEU A CA 338 C C . LEU A 44 ? 0.7970 1.7025 1.0593 0.0506 0.0603 -0.2167 44 LEU A C 339 O O . LEU A 44 ? 0.8030 1.7457 1.0671 0.0271 0.0677 -0.2223 44 LEU A O 340 C CB . LEU A 44 ? 0.7616 1.5234 1.0021 0.0421 0.0595 -0.1955 44 LEU A CB 341 C CG . LEU A 44 ? 0.7812 1.5105 1.0208 0.0115 0.0602 -0.1856 44 LEU A CG 342 C CD1 . LEU A 44 ? 0.7867 1.4797 1.0262 0.0299 0.0524 -0.1794 44 LEU A CD1 343 C CD2 . LEU A 44 ? 0.7787 1.4517 1.0062 -0.0121 0.0642 -0.1752 44 LEU A CD2 344 N N . ASP A 45 ? 0.8464 1.7831 1.1167 0.0568 0.0562 -0.2196 45 ASP A N 345 C CA . ASP A 45 ? 0.8608 1.8845 1.1437 0.0358 0.0602 -0.2307 45 ASP A CA 346 C C . ASP A 45 ? 0.8271 1.9327 1.1168 0.0461 0.0642 -0.2453 45 ASP A C 347 O O . ASP A 45 ? 0.8001 1.9629 1.0949 0.0122 0.0720 -0.2531 45 ASP A O 348 C CB . ASP A 45 ? 0.9097 1.9168 1.1882 -0.0176 0.0677 -0.2256 45 ASP A CB 349 C CG . ASP A 45 ? 0.9803 1.9890 1.2615 -0.0329 0.0655 -0.2234 45 ASP A CG 350 O OD1 . ASP A 45 ? 0.9934 1.9404 1.2708 -0.0183 0.0590 -0.2129 45 ASP A OD1 351 O OD2 . ASP A 45 ? 1.0484 2.1215 1.3342 -0.0615 0.0707 -0.2326 45 ASP A OD2 352 N N . GLY A 46 ? 0.8209 1.9289 1.1071 0.0925 0.0595 -0.2492 46 GLY A N 353 C CA . GLY A 46 ? 0.7980 1.9818 1.0887 0.1105 0.0626 -0.2633 46 GLY A CA 354 C C . GLY A 46 ? 0.7855 1.9472 1.0691 0.0977 0.0691 -0.2626 46 GLY A C 355 O O . GLY A 46 ? 0.7927 1.9929 1.0750 0.1240 0.0702 -0.2720 46 GLY A O 356 N N . VAL A 47 ? 0.7591 1.8587 1.0363 0.0597 0.0733 -0.2514 47 VAL A N 357 C CA . VAL A 47 ? 0.7313 1.8087 1.0006 0.0427 0.0798 -0.2497 47 VAL A CA 358 C C . VAL A 47 ? 0.7406 1.7383 0.9960 0.0710 0.0754 -0.2414 47 VAL A C 359 O O . VAL A 47 ? 0.7411 1.6615 0.9884 0.0647 0.0723 -0.2285 47 VAL A O 360 C CB . VAL A 47 ? 0.7160 1.7622 0.9797 -0.0099 0.0867 -0.2413 47 VAL A CB 361 C CG1 . VAL A 47 ? 0.7460 1.7686 0.9992 -0.0255 0.0932 -0.2390 47 VAL A CG1 362 C CG2 . VAL A 47 ? 0.6987 1.8182 0.9703 -0.0436 0.0925 -0.2502 47 VAL A CG2 363 N N . LYS A 48 ? 0.7616 1.7808 1.0126 0.1008 0.0758 -0.2497 48 LYS A N 364 C CA . LYS A 48 ? 0.7959 1.7456 1.0296 0.1292 0.0724 -0.2448 48 LYS A CA 365 C C . LYS A 48 ? 0.7786 1.6588 1.0034 0.1003 0.0753 -0.2331 48 LYS A C 366 O O . LYS A 48 ? 0.7800 1.6791 1.0088 0.0657 0.0821 -0.2328 48 LYS A O 367 C CB . LYS A 48 ? 0.8365 1.8322 1.0652 0.1610 0.0744 -0.2577 48 LYS A CB 368 C CG . LYS A 48 ? 0.8970 1.8271 1.1024 0.1948 0.0716 -0.2558 48 LYS A CG 369 C CD . LYS A 48 ? 0.9430 1.9136 1.1429 0.2105 0.0766 -0.2673 48 LYS A CD 370 C CE . LYS A 48 ? 0.9971 1.8973 1.1689 0.2409 0.0748 -0.2660 48 LYS A CE 371 N NZ . LYS A 48 ? 1.0479 1.9301 1.2006 0.2894 0.0689 -0.2694 48 LYS A NZ 372 N N . PRO A 49 ? 0.7621 1.5626 0.9724 0.1143 0.0705 -0.2239 49 PRO A N 373 C CA . PRO A 49 ? 0.7488 1.4911 0.9500 0.0920 0.0728 -0.2143 49 PRO A CA 374 C C . PRO A 49 ? 0.7393 1.4869 0.9313 0.1002 0.0769 -0.2205 49 PRO A C 375 O O . PRO A 49 ? 0.7424 1.5236 0.9307 0.1303 0.0769 -0.2314 49 PRO A O 376 C CB . PRO A 49 ? 0.7259 1.3927 0.9146 0.1064 0.0662 -0.2049 49 PRO A CB 377 C CG . PRO A 49 ? 0.7574 1.4346 0.9391 0.1468 0.0618 -0.2125 49 PRO A CG 378 C CD . PRO A 49 ? 0.7603 1.5208 0.9596 0.1487 0.0631 -0.2218 49 PRO A CD 379 N N . LEU A 50 ? 0.7143 1.4285 0.9007 0.0753 0.0803 -0.2134 50 LEU A N 380 C CA . LEU A 50 ? 0.7172 1.4217 0.8922 0.0816 0.0834 -0.2172 50 LEU A CA 381 C C . LEU A 50 ? 0.7466 1.3801 0.9036 0.1005 0.0784 -0.2122 50 LEU A C 382 O O . LEU A 50 ? 0.7668 1.3493 0.9198 0.0842 0.0761 -0.2011 50 LEU A O 383 C CB . LEU A 50 ? 0.7059 1.4076 0.8809 0.0456 0.0893 -0.2115 50 LEU A CB 384 C CG . LEU A 50 ? 0.7276 1.4132 0.8902 0.0469 0.0924 -0.2134 50 LEU A CG 385 C CD1 . LEU A 50 ? 0.7335 1.4713 0.8960 0.0694 0.0957 -0.2280 50 LEU A CD1 386 C CD2 . LEU A 50 ? 0.7405 1.4219 0.9009 0.0111 0.0980 -0.2063 50 LEU A CD2 387 N N . ILE A 51 ? 0.7827 1.4125 0.9258 0.1348 0.0770 -0.2208 51 ILE A N 388 C CA . ILE A 51 ? 0.8229 1.3819 0.9421 0.1511 0.0734 -0.2178 51 ILE A CA 389 C C . ILE A 51 ? 0.8477 1.3914 0.9513 0.1512 0.0775 -0.2219 51 ILE A C 390 O O . ILE A 51 ? 0.8636 1.4309 0.9572 0.1749 0.0801 -0.2330 51 ILE A O 391 C CB . ILE A 51 ? 0.8554 1.4030 0.9593 0.1898 0.0694 -0.2235 51 ILE A CB 392 C CG1 . ILE A 51 ? 0.8509 1.4236 0.9727 0.1887 0.0655 -0.2200 51 ILE A CG1 393 C CG2 . ILE A 51 ? 0.8880 1.3539 0.9614 0.2005 0.0668 -0.2197 51 ILE A CG2 394 C CD1 . ILE A 51 ? 0.8913 1.4349 0.9954 0.2223 0.0603 -0.2212 51 ILE A CD1 395 N N . LEU A 52 ? 0.8384 1.3436 0.9389 0.1259 0.0777 -0.2133 52 LEU A N 396 C CA . LEU A 52 ? 0.8546 1.3492 0.9430 0.1196 0.0816 -0.2161 52 LEU A CA 397 C C . LEU A 52 ? 0.9100 1.3584 0.9677 0.1443 0.0811 -0.2225 52 LEU A C 398 O O . LEU A 52 ? 0.9309 1.3751 0.9755 0.1448 0.0848 -0.2279 52 LEU A O 399 C CB . LEU A 52 ? 0.8309 1.3001 0.9233 0.0873 0.0815 -0.2047 52 LEU A CB 400 C CG . LEU A 52 ? 0.8150 1.3201 0.9285 0.0609 0.0837 -0.1981 52 LEU A CG 401 C CD1 . LEU A 52 ? 0.8073 1.2790 0.9187 0.0357 0.0827 -0.1859 52 LEU A CD1 402 C CD2 . LEU A 52 ? 0.8227 1.3852 0.9433 0.0561 0.0903 -0.2063 52 LEU A CD2 403 N N . ARG A 53 ? 0.9495 1.3601 0.9922 0.1636 0.0770 -0.2221 53 ARG A N 404 C CA . ARG A 53 ? 1.0418 1.3993 1.0473 0.1873 0.0773 -0.2283 53 ARG A CA 405 C C . ARG A 53 ? 1.0711 1.3807 1.0595 0.1655 0.0786 -0.2251 53 ARG A C 406 O O . ARG A 53 ? 1.1121 1.3983 1.1078 0.1414 0.0756 -0.2153 53 ARG A O 407 C CB . ARG A 53 ? 1.1093 1.4989 1.1028 0.2195 0.0810 -0.2415 53 ARG A CB 408 C CG . ARG A 53 ? 1.2162 1.5524 1.1672 0.2553 0.0806 -0.2482 53 ARG A CG 409 C CD . ARG A 53 ? 1.2970 1.6577 1.2299 0.2869 0.0852 -0.2615 53 ARG A CD 410 N NE . ARG A 53 ? 1.3601 1.7334 1.2792 0.3296 0.0835 -0.2680 53 ARG A NE 411 C CZ . ARG A 53 ? 1.3505 1.7989 1.2993 0.3410 0.0819 -0.2705 53 ARG A CZ 412 N NH1 . ARG A 53 ? 1.3092 1.8233 1.3015 0.3102 0.0825 -0.2672 53 ARG A NH1 413 N NH2 . ARG A 53 ? 1.3877 1.8453 1.3196 0.3833 0.0799 -0.2766 53 ARG A NH2 414 N N . ASP A 54 ? 1.0891 1.3881 1.0552 0.1738 0.0829 -0.2336 54 ASP A N 415 C CA . ASP A 54 ? 1.1069 1.3663 1.0558 0.1526 0.0843 -0.2322 54 ASP A CA 416 C C . ASP A 54 ? 1.0614 1.3592 1.0361 0.1238 0.0859 -0.2271 54 ASP A C 417 O O . ASP A 54 ? 1.0988 1.3725 1.0624 0.1054 0.0866 -0.2254 54 ASP A O 418 C CB . ASP A 54 ? 1.1632 1.3886 1.0717 0.1732 0.0888 -0.2440 54 ASP A CB 419 C CG . ASP A 54 ? 1.2215 1.3887 1.0912 0.1998 0.0880 -0.2481 54 ASP A CG 420 O OD1 . ASP A 54 ? 1.2039 1.3342 1.0692 0.1898 0.0843 -0.2409 54 ASP A OD1 421 O OD2 . ASP A 54 ? 1.2420 1.3987 1.0828 0.2314 0.0914 -0.2586 54 ASP A OD2 422 N N . CYS A 55 ? 1.0077 1.3636 1.0131 0.1190 0.0867 -0.2250 55 CYS A N 423 C CA . CYS A 55 ? 0.9793 1.3664 1.0036 0.0920 0.0888 -0.2195 55 CYS A CA 424 C C . CYS A 55 ? 0.9080 1.2891 0.9501 0.0683 0.0849 -0.2059 55 CYS A C 425 O O . CYS A 55 ? 0.9049 1.2793 0.9550 0.0726 0.0812 -0.2016 55 CYS A O 426 C CB . CYS A 55 ? 0.9565 1.4077 0.9981 0.0955 0.0935 -0.2254 55 CYS A CB 427 S SG . CYS A 55 ? 1.0575 1.5238 1.0785 0.1229 0.0989 -0.2416 55 CYS A SG 428 N N . SER A 56 ? 0.8785 1.2608 0.9242 0.0452 0.0857 -0.1992 56 SER A N 429 C CA . SER A 56 ? 0.8521 1.2323 0.9115 0.0247 0.0829 -0.1863 56 SER A CA 430 C C . SER A 56 ? 0.8348 1.2581 0.9106 0.0125 0.0868 -0.1834 56 SER A C 431 O O . SER A 56 ? 0.8232 1.2817 0.9014 0.0174 0.0917 -0.1917 56 SER A O 432 C CB . SER A 56 ? 0.8583 1.2148 0.9074 0.0088 0.0815 -0.1805 56 SER A CB 433 O OG . SER A 56 ? 0.8526 1.2321 0.9002 -0.0007 0.0859 -0.1818 56 SER A OG 434 N N . VAL A 57 ? 0.8306 1.2499 0.9145 -0.0043 0.0853 -0.1719 57 VAL A N 435 C CA . VAL A 57 ? 0.8239 1.2740 0.9157 -0.0204 0.0900 -0.1683 57 VAL A CA 436 C C . VAL A 57 ? 0.8228 1.2854 0.9052 -0.0313 0.0951 -0.1695 57 VAL A C 437 O O . VAL A 57 ? 0.8308 1.3276 0.9158 -0.0400 0.1011 -0.1731 57 VAL A O 438 C CB . VAL A 57 ? 0.8065 1.2383 0.9010 -0.0347 0.0877 -0.1551 57 VAL A CB 439 C CG1 . VAL A 57 ? 0.8072 1.2591 0.8999 -0.0547 0.0938 -0.1509 57 VAL A CG1 440 C CG2 . VAL A 57 ? 0.8065 1.2321 0.9116 -0.0251 0.0835 -0.1548 57 VAL A CG2 441 N N . ALA A 58 ? 0.8097 1.2468 0.8803 -0.0319 0.0928 -0.1671 58 ALA A N 442 C CA . ALA A 58 ? 0.8136 1.2601 0.8737 -0.0405 0.0968 -0.1684 58 ALA A CA 443 C C . ALA A 58 ? 0.8273 1.2993 0.8858 -0.0289 0.1012 -0.1825 58 ALA A C 444 O O . ALA A 58 ? 0.8129 1.3161 0.8713 -0.0369 0.1073 -0.1859 58 ALA A O 445 C CB . ALA A 58 ? 0.8051 1.2221 0.8535 -0.0433 0.0926 -0.1633 58 ALA A CB 446 N N . GLY A 59 ? 0.8333 1.2898 0.8869 -0.0099 0.0986 -0.1908 59 GLY A N 447 C CA . GLY A 59 ? 0.8347 1.3107 0.8827 0.0070 0.1025 -0.2047 59 GLY A CA 448 C C . GLY A 59 ? 0.8399 1.3660 0.9025 0.0100 0.1070 -0.2101 59 GLY A C 449 O O . GLY A 59 ? 0.8783 1.4392 0.9398 0.0112 0.1127 -0.2183 59 GLY A O 450 N N . TRP A 60 ? 0.8047 1.3378 0.8807 0.0097 0.1047 -0.2059 60 TRP A N 451 C CA . TRP A 60 ? 0.7731 1.3582 0.8635 0.0083 0.1088 -0.2110 60 TRP A CA 452 C C . TRP A 60 ? 0.7807 1.3943 0.8723 -0.0185 0.1155 -0.2078 60 TRP A C 453 O O . TRP A 60 ? 0.8123 1.4704 0.9054 -0.0188 0.1215 -0.2173 60 TRP A O 454 C CB . TRP A 60 ? 0.7579 1.3400 0.8606 0.0086 0.1048 -0.2056 60 TRP A CB 455 C CG . TRP A 60 ? 0.7412 1.3753 0.8578 -0.0034 0.1093 -0.2083 60 TRP A CG 456 C CD1 . TRP A 60 ? 0.7472 1.4402 0.8696 -0.0004 0.1151 -0.2200 60 TRP A CD1 457 C CD2 . TRP A 60 ? 0.7165 1.3504 0.8412 -0.0216 0.1087 -0.2000 60 TRP A CD2 458 N NE1 . TRP A 60 ? 0.7395 1.4714 0.8732 -0.0185 0.1184 -0.2198 60 TRP A NE1 459 C CE2 . TRP A 60 ? 0.7222 1.4156 0.8562 -0.0320 0.1147 -0.2076 60 TRP A CE2 460 C CE3 . TRP A 60 ? 0.7063 1.2968 0.8297 -0.0306 0.1041 -0.1875 60 TRP A CE3 461 C CZ2 . TRP A 60 ? 0.7206 1.4271 0.8603 -0.0531 0.1166 -0.2032 60 TRP A CZ2 462 C CZ3 . TRP A 60 ? 0.6997 1.3011 0.8289 -0.0485 0.1057 -0.1827 60 TRP A CZ3 463 C CH2 . TRP A 60 ? 0.7019 1.3588 0.8381 -0.0606 0.1120 -0.1906 60 TRP A CH2 464 N N . LEU A 61 ? 0.7758 1.3621 0.8633 -0.0403 0.1147 -0.1947 61 LEU A N 465 C CA . LEU A 61 ? 0.7767 1.3808 0.8591 -0.0673 0.1215 -0.1901 61 LEU A CA 466 C C . LEU A 61 ? 0.7826 1.3956 0.8528 -0.0737 0.1264 -0.1932 61 LEU A C 467 O O . LEU A 61 ? 0.7732 1.4240 0.8416 -0.0880 0.1341 -0.1980 61 LEU A O 468 C CB . LEU A 61 ? 0.7702 1.3348 0.8448 -0.0843 0.1193 -0.1746 61 LEU A CB 469 C CG . LEU A 61 ? 0.7633 1.3252 0.8480 -0.0862 0.1168 -0.1709 61 LEU A CG 470 C CD1 . LEU A 61 ? 0.7836 1.3003 0.8563 -0.0988 0.1144 -0.1556 61 LEU A CD1 471 C CD2 . LEU A 61 ? 0.7646 1.3746 0.8555 -0.1003 0.1238 -0.1779 61 LEU A CD2 472 N N . LEU A 62 ? 0.7962 1.3763 0.8570 -0.0649 0.1224 -0.1910 62 LEU A N 473 C CA . LEU A 62 ? 0.8152 1.4025 0.8640 -0.0684 0.1264 -0.1949 62 LEU A CA 474 C C . LEU A 62 ? 0.8224 1.4499 0.8754 -0.0530 0.1306 -0.2109 62 LEU A C 475 O O . LEU A 62 ? 0.8450 1.4944 0.8907 -0.0598 0.1363 -0.2157 62 LEU A O 476 C CB . LEU A 62 ? 0.8133 1.3588 0.8507 -0.0630 0.1207 -0.1899 62 LEU A CB 477 C CG . LEU A 62 ? 0.8102 1.3245 0.8390 -0.0780 0.1178 -0.1743 62 LEU A CG 478 C CD1 . LEU A 62 ? 0.8202 1.3012 0.8422 -0.0703 0.1109 -0.1712 62 LEU A CD1 479 C CD2 . LEU A 62 ? 0.8286 1.3523 0.8430 -0.0972 0.1241 -0.1691 62 LEU A CD2 480 N N . GLY A 63 ? 0.8175 1.4543 0.8801 -0.0305 0.1277 -0.2190 63 GLY A N 481 C CA . GLY A 63 ? 0.8260 1.5010 0.8902 -0.0095 0.1312 -0.2346 63 GLY A CA 482 C C . GLY A 63 ? 0.8507 1.4950 0.8989 0.0113 0.1290 -0.2411 63 GLY A C 483 O O . GLY A 63 ? 0.8511 1.5165 0.8913 0.0174 0.1338 -0.2505 63 GLY A O 484 N N . ASN A 64 ? 0.8613 1.4545 0.9022 0.0204 0.1223 -0.2365 64 ASN A N 485 C CA . ASN A 64 ? 0.8869 1.4434 0.9072 0.0393 0.1206 -0.2436 64 ASN A CA 486 C C . ASN A 64 ? 0.9217 1.5052 0.9367 0.0688 0.1240 -0.2586 64 ASN A C 487 O O . ASN A 64 ? 0.9160 1.5224 0.9420 0.0837 0.1229 -0.2615 64 ASN A O 488 C CB . ASN A 64 ? 0.8844 1.3879 0.8983 0.0436 0.1136 -0.2373 64 ASN A CB 489 C CG . ASN A 64 ? 0.9034 1.3603 0.8893 0.0577 0.1125 -0.2444 64 ASN A CG 490 O OD1 . ASN A 64 ? 0.9134 1.3731 0.8840 0.0797 0.1159 -0.2566 64 ASN A OD1 491 N ND2 . ASN A 64 ? 0.9087 1.3221 0.8852 0.0448 0.1082 -0.2373 64 ASN A ND2 492 N N . PRO A 65 ? 0.9767 1.5599 0.9738 0.0788 0.1281 -0.2685 65 PRO A N 493 C CA . PRO A 65 ? 1.0253 1.6360 1.0136 0.1105 0.1319 -0.2835 65 PRO A CA 494 C C . PRO A 65 ? 1.0601 1.6459 1.0376 0.1425 0.1280 -0.2879 65 PRO A C 495 O O . PRO A 65 ? 1.0874 1.7137 1.0678 0.1688 0.1300 -0.2975 65 PRO A O 496 C CB . PRO A 65 ? 1.0472 1.6328 1.0091 0.1147 0.1353 -0.2909 65 PRO A CB 497 C CG . PRO A 65 ? 1.0227 1.6011 0.9901 0.0799 0.1353 -0.2807 65 PRO A CG 498 C CD . PRO A 65 ? 0.9927 1.5534 0.9760 0.0613 0.1295 -0.2663 65 PRO A CD 499 N N . MET A 66 ? 1.0822 1.6044 1.0459 0.1403 0.1227 -0.2811 66 MET A N 500 C CA . MET A 66 ? 1.1250 1.6142 1.0749 0.1672 0.1189 -0.2832 66 MET A CA 501 C C . MET A 66 ? 1.0803 1.6031 1.0587 0.1669 0.1153 -0.2771 66 MET A C 502 O O . MET A 66 ? 1.0824 1.5844 1.0517 0.1900 0.1119 -0.2784 66 MET A O 503 C CB . MET A 66 ? 1.1685 1.5796 1.0934 0.1588 0.1152 -0.2777 66 MET A CB 504 C CG . MET A 66 ? 1.2195 1.5879 1.1089 0.1601 0.1187 -0.2851 66 MET A CG 505 S SD . MET A 66 ? 1.3113 1.6394 1.1537 0.2058 0.1220 -0.3001 66 MET A SD 506 C CE . MET A 66 ? 1.3638 1.6285 1.1635 0.1920 0.1257 -0.3055 66 MET A CE 507 N N . CYS A 67 ? 1.0407 1.6111 1.0495 0.1403 0.1163 -0.2706 67 CYS A N 508 C CA . CYS A 67 ? 1.0067 1.6066 1.0411 0.1333 0.1135 -0.2643 67 CYS A CA 509 C C . CYS A 67 ? 0.9925 1.6739 1.0477 0.1342 0.1183 -0.2717 67 CYS A C 510 O O . CYS A 67 ? 0.9542 1.6692 1.0317 0.1112 0.1187 -0.2657 67 CYS A O 511 C CB . CYS A 67 ? 0.9652 1.5430 1.0119 0.0981 0.1108 -0.2494 67 CYS A CB 512 S SG . CYS A 67 ? 0.9929 1.4872 1.0180 0.0949 0.1051 -0.2416 67 CYS A SG 513 N N . ASP A 68 ? 0.9961 1.7092 1.0413 0.1605 0.1222 -0.2853 68 ASP A N 514 C CA . ASP A 68 ? 0.9765 1.7754 1.0398 0.1637 0.1273 -0.2948 68 ASP A CA 515 C C . ASP A 68 ? 0.9726 1.8109 1.0520 0.1783 0.1242 -0.2968 68 ASP A C 516 O O . ASP A 68 ? 0.9648 1.8769 1.0656 0.1666 0.1277 -0.3012 68 ASP A O 517 C CB . ASP A 68 ? 0.9962 1.8191 1.0425 0.1930 0.1320 -0.3096 68 ASP A CB 518 C CG . ASP A 68 ? 0.9967 1.8041 1.0329 0.1732 0.1368 -0.3093 68 ASP A CG 519 O OD1 . ASP A 68 ? 1.0014 1.7853 1.0445 0.1373 0.1364 -0.2977 68 ASP A OD1 520 O OD2 . ASP A 68 ? 1.0161 1.8346 1.0355 0.1950 0.1409 -0.3208 68 ASP A OD2 521 N N . GLU A 69 ? 0.9779 1.7682 1.0452 0.2018 0.1179 -0.2940 69 GLU A N 522 C CA . GLU A 69 ? 0.9639 1.7843 1.0455 0.2147 0.1139 -0.2941 69 GLU A CA 523 C C . GLU A 69 ? 0.9143 1.7702 1.0250 0.1743 0.1146 -0.2860 69 GLU A C 524 O O . GLU A 69 ? 0.9134 1.8318 1.0424 0.1757 0.1148 -0.2905 69 GLU A O 525 C CB . GLU A 69 ? 0.9938 1.7398 1.0563 0.2346 0.1069 -0.2880 69 GLU A CB 526 C CG . GLU A 69 ? 1.0003 1.7741 1.0724 0.2557 0.1024 -0.2892 69 GLU A CG 527 C CD . GLU A 69 ? 1.0313 1.7271 1.0840 0.2693 0.0959 -0.2814 69 GLU A CD 528 O OE1 . GLU A 69 ? 1.0588 1.6798 1.0884 0.2636 0.0952 -0.2763 69 GLU A OE1 529 O OE2 . GLU A 69 ? 1.0317 1.7432 1.0913 0.2844 0.0916 -0.2808 69 GLU A OE2 530 N N . PHE A 70 ? 0.8838 1.6997 0.9955 0.1388 0.1153 -0.2745 70 PHE A N 531 C CA . PHE A 70 ? 0.8475 1.6783 0.9777 0.1001 0.1164 -0.2651 70 PHE A CA 532 C C . PHE A 70 ? 0.8539 1.7239 0.9890 0.0687 0.1244 -0.2664 70 PHE A C 533 O O . PHE A 70 ? 0.8370 1.6877 0.9739 0.0342 0.1261 -0.2557 70 PHE A O 534 C CB . PHE A 70 ? 0.8331 1.5875 0.9572 0.0854 0.1110 -0.2500 70 PHE A CB 535 C CG . PHE A 70 ? 0.8317 1.5360 0.9437 0.1147 0.1041 -0.2489 70 PHE A CG 536 C CD1 . PHE A 70 ? 0.8133 1.5330 0.9338 0.1307 0.1000 -0.2501 70 PHE A CD1 537 C CD2 . PHE A 70 ? 0.8462 1.4887 0.9355 0.1254 0.1021 -0.2476 70 PHE A CD2 538 C CE1 . PHE A 70 ? 0.8261 1.4961 0.9312 0.1574 0.0942 -0.2489 70 PHE A CE1 539 C CE2 . PHE A 70 ? 0.8687 1.4609 0.9412 0.1493 0.0968 -0.2470 70 PHE A CE2 540 C CZ . PHE A 70 ? 0.8540 1.4582 0.9337 0.1659 0.0929 -0.2473 70 PHE A CZ 541 N N . ILE A 71 ? 0.8874 1.8113 1.0217 0.0820 0.1297 -0.2797 71 ILE A N 542 C CA . ILE A 71 ? 0.9128 1.8805 1.0500 0.0533 0.1382 -0.2828 71 ILE A CA 543 C C . ILE A 71 ? 0.9038 1.9211 1.0564 0.0191 0.1426 -0.2813 71 ILE A C 544 O O . ILE A 71 ? 0.8936 1.9060 1.0419 -0.0179 0.1482 -0.2750 71 ILE A O 545 C CB . ILE A 71 ? 0.9480 1.9705 1.0817 0.0781 0.1430 -0.2990 71 ILE A CB 546 C CG1 . ILE A 71 ? 0.9516 2.0018 1.0827 0.0483 0.1518 -0.3009 71 ILE A CG1 547 C CG2 . ILE A 71 ? 0.9416 2.0443 1.0894 0.1007 0.1436 -0.3122 71 ILE A CG2 548 C CD1 . ILE A 71 ? 0.9575 1.9444 1.0696 0.0463 0.1515 -0.2950 71 ILE A CD1 549 N N . ASN A 72 ? 0.9140 1.9759 1.0806 0.0311 0.1403 -0.2871 72 ASN A N 550 C CA . ASN A 72 ? 0.9120 2.0192 1.0910 -0.0026 0.1443 -0.2866 72 ASN A CA 551 C C . ASN A 72 ? 0.8782 1.9880 1.0683 0.0126 0.1374 -0.2854 72 ASN A C 552 O O . ASN A 72 ? 0.9003 2.0786 1.1025 0.0325 0.1369 -0.2973 72 ASN A O 553 C CB . ASN A 72 ? 0.9261 2.1304 1.1132 -0.0140 0.1533 -0.3016 72 ASN A CB 554 C CG . ASN A 72 ? 0.9631 2.1654 1.1385 -0.0496 0.1623 -0.2995 72 ASN A CG 555 O OD1 . ASN A 72 ? 0.9867 2.1356 1.1506 -0.0830 0.1641 -0.2863 72 ASN A OD1 556 N ND2 . ASN A 72 ? 0.9816 2.2416 1.1575 -0.0409 0.1680 -0.3124 72 ASN A ND2 557 N N . VAL A 73 ? 0.8512 1.8886 1.0368 0.0040 0.1320 -0.2710 73 VAL A N 558 C CA . VAL A 73 ? 0.8198 1.8471 1.0136 0.0193 0.1248 -0.2682 73 VAL A CA 559 C C . VAL A 73 ? 0.7865 1.8586 0.9916 -0.0127 0.1282 -0.2686 73 VAL A C 560 O O . VAL A 73 ? 0.7972 1.8597 0.9958 -0.0537 0.1345 -0.2626 73 VAL A O 561 C CB . VAL A 73 ? 0.8140 1.7473 0.9980 0.0230 0.1176 -0.2531 73 VAL A CB 562 C CG1 . VAL A 73 ? 0.8223 1.7093 0.9918 0.0507 0.1147 -0.2534 73 VAL A CG1 563 C CG2 . VAL A 73 ? 0.8183 1.7103 0.9959 -0.0184 0.1207 -0.2397 73 VAL A CG2 564 N N . PRO A 74 ? 0.7585 1.8760 0.9767 0.0061 0.1243 -0.2757 74 PRO A N 565 C CA . PRO A 74 ? 0.7555 1.9150 0.9832 -0.0250 0.1273 -0.2768 74 PRO A CA 566 C C . PRO A 74 ? 0.7356 1.8208 0.9575 -0.0440 0.1235 -0.2611 74 PRO A C 567 O O . PRO A 74 ? 0.7166 1.7237 0.9293 -0.0315 0.1181 -0.2498 74 PRO A O 568 C CB . PRO A 74 ? 0.7525 1.9818 0.9953 0.0094 0.1227 -0.2893 74 PRO A CB 569 C CG . PRO A 74 ? 0.7652 1.9413 1.0007 0.0580 0.1141 -0.2864 74 PRO A CG 570 C CD . PRO A 74 ? 0.7704 1.8939 0.9910 0.0570 0.1167 -0.2818 74 PRO A CD 571 N N . GLU A 75 ? 0.7292 1.8419 0.9551 -0.0747 0.1267 -0.2614 75 GLU A N 572 C CA . GLU A 75 ? 0.7426 1.7936 0.9623 -0.0925 0.1237 -0.2481 75 GLU A CA 573 C C . GLU A 75 ? 0.7328 1.7357 0.9574 -0.0539 0.1125 -0.2417 75 GLU A C 574 O O . GLU A 75 ? 0.7061 1.7455 0.9412 -0.0180 0.1073 -0.2503 75 GLU A O 575 C CB . GLU A 75 ? 0.7679 1.8724 0.9926 -0.1232 0.1282 -0.2538 75 GLU A CB 576 C CG . GLU A 75 ? 0.7935 1.8376 1.0083 -0.1461 0.1267 -0.2412 75 GLU A CG 577 C CD . GLU A 75 ? 0.8170 1.9173 1.0352 -0.1757 0.1313 -0.2488 75 GLU A CD 578 O OE1 . GLU A 75 ? 0.8612 2.0328 1.0794 -0.2008 0.1399 -0.2609 75 GLU A OE1 579 O OE2 . GLU A 75 ? 0.8205 1.8956 1.0405 -0.1755 0.1264 -0.2433 75 GLU A OE2 580 N N . TRP A 76 ? 0.7376 1.6582 0.9516 -0.0605 0.1091 -0.2268 76 TRP A N 581 C CA . TRP A 76 ? 0.7512 1.6223 0.9671 -0.0300 0.0993 -0.2202 76 TRP A CA 582 C C . TRP A 76 ? 0.7543 1.5892 0.9689 -0.0485 0.0970 -0.2100 76 TRP A C 583 O O . TRP A 76 ? 0.8062 1.6326 1.0122 -0.0849 0.1030 -0.2052 76 TRP A O 584 C CB . TRP A 76 ? 0.7447 1.5510 0.9490 -0.0140 0.0962 -0.2128 76 TRP A CB 585 C CG . TRP A 76 ? 0.7598 1.5143 0.9506 -0.0435 0.0997 -0.2008 76 TRP A CG 586 C CD1 . TRP A 76 ? 0.7719 1.4668 0.9555 -0.0543 0.0966 -0.1876 76 TRP A CD1 587 C CD2 . TRP A 76 ? 0.7724 1.5310 0.9529 -0.0634 0.1069 -0.2010 76 TRP A CD2 588 N NE1 . TRP A 76 ? 0.7891 1.4508 0.9573 -0.0775 0.1012 -0.1793 76 TRP A NE1 589 C CE2 . TRP A 76 ? 0.7792 1.4774 0.9448 -0.0841 0.1076 -0.1871 76 TRP A CE2 590 C CE3 . TRP A 76 ? 0.7826 1.5913 0.9639 -0.0646 0.1129 -0.2117 76 TRP A CE3 591 C CZ2 . TRP A 76 ? 0.8072 1.4907 0.9568 -0.1052 0.1139 -0.1831 76 TRP A CZ2 592 C CZ3 . TRP A 76 ? 0.7844 1.5787 0.9514 -0.0882 0.1195 -0.2079 76 TRP A CZ3 593 C CH2 . TRP A 76 ? 0.8080 1.5390 0.9586 -0.1079 0.1198 -0.1934 76 TRP A CH2 594 N N . SER A 77 ? 0.7478 1.5587 0.9675 -0.0227 0.0887 -0.2070 77 SER A N 595 C CA . SER A 77 ? 0.7359 1.5080 0.9545 -0.0347 0.0854 -0.1971 77 SER A CA 596 C C . SER A 77 ? 0.7383 1.4287 0.9446 -0.0345 0.0823 -0.1832 77 SER A C 597 O O . SER A 77 ? 0.7512 1.4043 0.9487 -0.0586 0.0841 -0.1733 77 SER A O 598 C CB . SER A 77 ? 0.7214 1.5120 0.9507 -0.0061 0.0781 -0.2012 77 SER A CB 599 O OG . SER A 77 ? 0.7259 1.5044 0.9529 0.0328 0.0730 -0.2045 77 SER A OG 600 N N . TYR A 78 ? 0.7212 1.3849 0.9245 -0.0068 0.0778 -0.1831 78 TYR A N 601 C CA . TYR A 78 ? 0.7035 1.2997 0.8954 -0.0066 0.0751 -0.1720 78 TYR A CA 602 C C . TYR A 78 ? 0.6987 1.2889 0.8839 0.0121 0.0751 -0.1769 78 TYR A C 603 O O . TYR A 78 ? 0.7131 1.3466 0.9020 0.0289 0.0765 -0.1882 78 TYR A O 604 C CB . TYR A 78 ? 0.6928 1.2460 0.8847 0.0066 0.0677 -0.1648 78 TYR A CB 605 C CG . TYR A 78 ? 0.6814 1.2431 0.8758 0.0401 0.0623 -0.1717 78 TYR A CG 606 C CD1 . TYR A 78 ? 0.6733 1.2830 0.8783 0.0497 0.0611 -0.1791 78 TYR A CD1 607 C CD2 . TYR A 78 ? 0.6935 1.2134 0.8757 0.0620 0.0585 -0.1709 78 TYR A CD2 608 C CE1 . TYR A 78 ? 0.6754 1.2896 0.8779 0.0841 0.0561 -0.1848 78 TYR A CE1 609 C CE2 . TYR A 78 ? 0.6947 1.2128 0.8711 0.0936 0.0543 -0.1768 78 TYR A CE2 610 C CZ . TYR A 78 ? 0.6825 1.2468 0.8687 0.1066 0.0529 -0.1832 78 TYR A CZ 611 O OH . TYR A 78 ? 0.6859 1.2448 0.8616 0.1417 0.0486 -0.1884 78 TYR A OH 612 N N . ILE A 79 ? 0.6902 1.2293 0.8644 0.0094 0.0737 -0.1689 79 ILE A N 613 C CA . ILE A 79 ? 0.7191 1.2474 0.8838 0.0226 0.0742 -0.1731 79 ILE A CA 614 C C . ILE A 79 ? 0.7461 1.2230 0.9007 0.0412 0.0681 -0.1699 79 ILE A C 615 O O . ILE A 79 ? 0.7556 1.1963 0.9092 0.0338 0.0645 -0.1604 79 ILE A O 616 C CB . ILE A 79 ? 0.7272 1.2448 0.8843 -0.0001 0.0789 -0.1679 79 ILE A CB 617 C CG1 . ILE A 79 ? 0.7360 1.3035 0.8975 -0.0196 0.0864 -0.1728 79 ILE A CG1 618 C CG2 . ILE A 79 ? 0.7475 1.2471 0.8934 0.0122 0.0788 -0.1714 79 ILE A CG2 619 C CD1 . ILE A 79 ? 0.7582 1.3097 0.9078 -0.0448 0.0915 -0.1657 79 ILE A CD1 620 N N . VAL A 80 ? 0.7714 1.2439 0.9154 0.0645 0.0676 -0.1781 80 VAL A N 621 C CA . VAL A 80 ? 0.8061 1.2252 0.9334 0.0795 0.0632 -0.1764 80 VAL A CA 622 C C . VAL A 80 ? 0.8334 1.2300 0.9440 0.0800 0.0654 -0.1793 80 VAL A C 623 O O . VAL A 80 ? 0.8551 1.2763 0.9611 0.0907 0.0691 -0.1884 80 VAL A O 624 C CB . VAL A 80 ? 0.8203 1.2389 0.9399 0.1104 0.0602 -0.1834 80 VAL A CB 625 C CG1 . VAL A 80 ? 0.8409 1.1958 0.9363 0.1218 0.0569 -0.1814 80 VAL A CG1 626 C CG2 . VAL A 80 ? 0.8009 1.2470 0.9376 0.1098 0.0578 -0.1812 80 VAL A CG2 627 N N . GLU A 81 ? 0.8252 1.1777 0.9263 0.0683 0.0632 -0.1720 81 GLU A N 628 C CA . GLU A 81 ? 0.8493 1.1797 0.9344 0.0637 0.0650 -0.1739 81 GLU A CA 629 C C . GLU A 81 ? 0.8715 1.1487 0.9364 0.0672 0.0616 -0.1724 81 GLU A C 630 O O . GLU A 81 ? 0.8589 1.1173 0.9280 0.0599 0.0579 -0.1648 81 GLU A O 631 C CB . GLU A 81 ? 0.8694 1.2089 0.9631 0.0383 0.0665 -0.1658 81 GLU A CB 632 C CG . GLU A 81 ? 0.9178 1.2441 0.9972 0.0319 0.0685 -0.1679 81 GLU A CG 633 C CD . GLU A 81 ? 0.9321 1.2632 1.0166 0.0099 0.0690 -0.1585 81 GLU A CD 634 O OE1 . GLU A 81 ? 0.8967 1.2140 0.9861 0.0008 0.0656 -0.1488 81 GLU A OE1 635 O OE2 . GLU A 81 ? 0.9721 1.3204 1.0536 0.0034 0.0729 -0.1608 81 GLU A OE2 636 N N . LYS A 82 ? 0.9328 1.1849 0.9732 0.0769 0.0635 -0.1802 82 LYS A N 637 C CA . LYS A 82 ? 0.9694 1.1678 0.9844 0.0748 0.0617 -0.1800 82 LYS A CA 638 C C . LYS A 82 ? 0.9455 1.1354 0.9649 0.0482 0.0601 -0.1719 82 LYS A C 639 O O . LYS A 82 ? 0.8928 1.1128 0.9300 0.0344 0.0608 -0.1669 82 LYS A O 640 C CB . LYS A 82 ? 1.0202 1.1901 1.0019 0.0896 0.0653 -0.1910 82 LYS A CB 641 C CG . LYS A 82 ? 1.0388 1.2064 1.0072 0.1219 0.0662 -0.1989 82 LYS A CG 642 C CD . LYS A 82 ? 1.0953 1.2217 1.0220 0.1382 0.0701 -0.2094 82 LYS A CD 643 C CE . LYS A 82 ? 1.1446 1.2511 1.0473 0.1738 0.0702 -0.2158 82 LYS A CE 644 N NZ . LYS A 82 ? 1.1353 1.3046 1.0658 0.1937 0.0695 -0.2181 82 LYS A NZ 645 N N . ALA A 83 ? 0.9980 1.1472 0.9987 0.0415 0.0582 -0.1709 83 ALA A N 646 C CA . ALA A 83 ? 0.9956 1.1404 0.9979 0.0180 0.0564 -0.1647 83 ALA A CA 647 C C . ALA A 83 ? 1.0361 1.1856 1.0270 0.0077 0.0594 -0.1695 83 ALA A C 648 O O . ALA A 83 ? 1.0372 1.2104 1.0412 -0.0072 0.0585 -0.1637 83 ALA A O 649 C CB . ALA A 83 ? 0.9928 1.0965 0.9755 0.0119 0.0544 -0.1643 83 ALA A CB 650 N N . ASN A 84 ? 1.0737 1.1993 1.0378 0.0174 0.0631 -0.1801 84 ASN A N 651 C CA . ASN A 84 ? 1.1218 1.2498 1.0723 0.0088 0.0665 -0.1860 84 ASN A CA 652 C C . ASN A 84 ? 1.1122 1.2465 1.0538 0.0289 0.0709 -0.1953 84 ASN A C 653 O O . ASN A 84 ? 1.1220 1.2204 1.0302 0.0375 0.0743 -0.2050 84 ASN A O 654 C CB . ASN A 84 ? 1.2135 1.2983 1.1301 -0.0056 0.0675 -0.1912 84 ASN A CB 655 C CG . ASN A 84 ? 1.2497 1.3357 1.1748 -0.0261 0.0633 -0.1832 84 ASN A CG 656 O OD1 . ASN A 84 ? 1.2594 1.3781 1.2027 -0.0407 0.0611 -0.1772 84 ASN A OD1 657 N ND2 . ASN A 84 ? 1.2855 1.3364 1.1957 -0.0258 0.0623 -0.1832 84 ASN A ND2 658 N N . PRO A 85 ? 1.0889 1.2686 1.0575 0.0359 0.0715 -0.1930 85 PRO A N 659 C CA . PRO A 85 ? 1.1071 1.3021 1.0694 0.0552 0.0759 -0.2025 85 PRO A CA 660 C C . PRO A 85 ? 1.1286 1.3145 1.0703 0.0482 0.0798 -0.2096 85 PRO A C 661 O O . PRO A 85 ? 1.1218 1.3208 1.0716 0.0270 0.0791 -0.2048 85 PRO A O 662 C CB . PRO A 85 ? 1.0636 1.3142 1.0601 0.0535 0.0762 -0.1976 85 PRO A CB 663 C CG . PRO A 85 ? 1.0144 1.2683 1.0309 0.0395 0.0717 -0.1856 85 PRO A CG 664 C CD . PRO A 85 ? 1.0323 1.2503 1.0339 0.0247 0.0692 -0.1823 85 PRO A CD 665 N N . VAL A 86 ? 1.1667 1.3293 1.0796 0.0672 0.0837 -0.2210 86 VAL A N 666 C CA . VAL A 86 ? 1.1944 1.3410 1.0818 0.0607 0.0879 -0.2290 86 VAL A CA 667 C C . VAL A 86 ? 1.1579 1.3549 1.0646 0.0590 0.0908 -0.2306 86 VAL A C 668 O O . VAL A 86 ? 1.1748 1.3736 1.0747 0.0427 0.0925 -0.2318 86 VAL A O 669 C CB . VAL A 86 ? 1.2633 1.3583 1.1050 0.0824 0.0919 -0.2411 86 VAL A CB 670 C CG1 . VAL A 86 ? 1.2906 1.3302 1.1076 0.0825 0.0899 -0.2394 86 VAL A CG1 671 C CG2 . VAL A 86 ? 1.2739 1.3934 1.1172 0.1158 0.0946 -0.2482 86 VAL A CG2 672 N N . ASN A 87 ? 1.0975 1.3367 1.0266 0.0744 0.0917 -0.2308 87 ASN A N 673 C CA . ASN A 87 ? 1.0692 1.3587 1.0156 0.0712 0.0953 -0.2326 87 ASN A CA 674 C C . ASN A 87 ? 1.0244 1.3480 1.0021 0.0483 0.0931 -0.2204 87 ASN A C 675 O O . ASN A 87 ? 1.0012 1.3604 1.0020 0.0503 0.0931 -0.2169 87 ASN A O 676 C CB . ASN A 87 ? 1.0804 1.4031 1.0315 0.0982 0.0984 -0.2411 87 ASN A CB 677 C CG . ASN A 87 ? 1.1385 1.4294 1.0532 0.1249 0.1018 -0.2541 87 ASN A CG 678 O OD1 . ASN A 87 ? 1.1671 1.4303 1.0567 0.1196 0.1047 -0.2594 87 ASN A OD1 679 N ND2 . ASN A 87 ? 1.1648 1.4589 1.0737 0.1549 0.1017 -0.2595 87 ASN A ND2 680 N N . ASP A 88 ? 1.0120 1.3234 0.9867 0.0267 0.0915 -0.2143 88 ASP A N 681 C CA . ASP A 88 ? 0.9642 1.2995 0.9601 0.0069 0.0896 -0.2022 88 ASP A CA 682 C C . ASP A 88 ? 0.9636 1.3253 0.9583 -0.0023 0.0939 -0.2040 88 ASP A C 683 O O . ASP A 88 ? 0.9628 1.3517 0.9599 0.0068 0.0987 -0.2113 88 ASP A O 684 C CB . ASP A 88 ? 0.9501 1.2575 0.9422 -0.0072 0.0843 -0.1940 88 ASP A CB 685 C CG . ASP A 88 ? 0.9252 1.2510 0.9366 -0.0211 0.0815 -0.1804 88 ASP A CG 686 O OD1 . ASP A 88 ? 0.8862 1.2384 0.9124 -0.0211 0.0837 -0.1767 88 ASP A OD1 687 O OD2 . ASP A 88 ? 0.9830 1.2963 0.9916 -0.0322 0.0775 -0.1737 88 ASP A OD2 688 N N . LEU A 89 ? 0.9534 1.3102 0.9433 -0.0193 0.0922 -0.1980 89 LEU A N 689 C CA . LEU A 89 ? 0.9502 1.3276 0.9352 -0.0281 0.0960 -0.1994 89 LEU A CA 690 C C . LEU A 89 ? 0.9668 1.3263 0.9284 -0.0224 0.0984 -0.2120 89 LEU A C 691 O O . LEU A 89 ? 0.9540 1.2872 0.9000 -0.0303 0.0958 -0.2130 89 LEU A O 692 C CB . LEU A 89 ? 0.9393 1.3188 0.9257 -0.0456 0.0927 -0.1876 89 LEU A CB 693 C CG . LEU A 89 ? 0.9120 1.2987 0.9141 -0.0510 0.0902 -0.1742 89 LEU A CG 694 C CD1 . LEU A 89 ? 0.8985 1.2832 0.8958 -0.0627 0.0864 -0.1633 89 LEU A CD1 695 C CD2 . LEU A 89 ? 0.8795 1.2934 0.8911 -0.0520 0.0956 -0.1731 89 LEU A CD2 696 N N . CYS A 90 ? 0.9803 1.3553 0.9377 -0.0092 0.1039 -0.2223 90 CYS A N 697 C CA . CYS A 90 ? 1.0102 1.3647 0.9412 -0.0003 0.1072 -0.2353 90 CYS A CA 698 C C . CYS A 90 ? 1.0039 1.3572 0.9228 -0.0183 0.1076 -0.2349 90 CYS A C 699 O O . CYS A 90 ? 1.0436 1.3641 0.9391 -0.0232 0.1068 -0.2403 90 CYS A O 700 C CB . CYS A 90 ? 1.0511 1.4305 0.9814 0.0198 0.1131 -0.2460 90 CYS A CB 701 S SG . CYS A 90 ? 1.0625 1.5038 1.0158 0.0110 0.1179 -0.2431 90 CYS A SG 702 N N . TYR A 91 ? 0.9752 1.3632 0.9072 -0.0294 0.1091 -0.2287 91 TYR A N 703 C CA . TYR A 91 ? 0.9804 1.3722 0.9043 -0.0470 0.1080 -0.2249 91 TYR A CA 704 C C . TYR A 91 ? 0.9566 1.3426 0.8898 -0.0592 0.1014 -0.2116 91 TYR A C 705 O O . TYR A 91 ? 0.9429 1.3418 0.8940 -0.0597 0.1000 -0.2014 91 TYR A O 706 C CB . TYR A 91 ? 0.9941 1.4226 0.9246 -0.0523 0.1126 -0.2227 91 TYR A CB 707 C CG . TYR A 91 ? 1.0316 1.4647 0.9474 -0.0650 0.1132 -0.2233 91 TYR A CG 708 C CD1 . TYR A 91 ? 1.0279 1.4611 0.9434 -0.0789 0.1080 -0.2124 91 TYR A CD1 709 C CD2 . TYR A 91 ? 1.0463 1.4863 0.9476 -0.0614 0.1187 -0.2351 91 TYR A CD2 710 C CE1 . TYR A 91 ? 1.0345 1.4763 0.9362 -0.0893 0.1081 -0.2131 91 TYR A CE1 711 C CE2 . TYR A 91 ? 1.0494 1.4949 0.9370 -0.0735 0.1191 -0.2359 91 TYR A CE2 712 C CZ . TYR A 91 ? 1.0459 1.4933 0.9341 -0.0877 0.1137 -0.2248 91 TYR A CZ 713 O OH . TYR A 91 ? 1.0512 1.5082 0.9254 -0.0986 0.1136 -0.2256 91 TYR A OH 714 N N . PRO A 92 ? 0.9654 1.3338 0.8849 -0.0695 0.0977 -0.2123 92 PRO A N 715 C CA . PRO A 92 ? 0.9364 1.3026 0.8644 -0.0783 0.0912 -0.2010 92 PRO A CA 716 C C . PRO A 92 ? 0.9309 1.3240 0.8707 -0.0841 0.0894 -0.1873 92 PRO A C 717 O O . PRO A 92 ? 0.9386 1.3502 0.8740 -0.0872 0.0926 -0.1870 92 PRO A O 718 C CB . PRO A 92 ? 0.9618 1.3141 0.8696 -0.0909 0.0890 -0.2072 92 PRO A CB 719 C CG . PRO A 92 ? 0.9953 1.3538 0.8871 -0.0930 0.0939 -0.2167 92 PRO A CG 720 C CD . PRO A 92 ? 1.0048 1.3609 0.8997 -0.0761 0.0996 -0.2231 92 PRO A CD 721 N N . GLY A 93 ? 0.9486 1.3404 0.8996 -0.0847 0.0846 -0.1761 93 GLY A N 722 C CA . GLY A 93 ? 0.9504 1.3587 0.9059 -0.0876 0.0828 -0.1622 93 GLY A CA 723 C C . GLY A 93 ? 0.9585 1.3593 0.9258 -0.0841 0.0787 -0.1512 93 GLY A C 724 O O . GLY A 93 ? 0.9198 1.3077 0.8910 -0.0833 0.0747 -0.1527 93 GLY A O 725 N N . ASP A 94 ? 0.9704 1.3764 0.9397 -0.0830 0.0802 -0.1402 94 ASP A N 726 C CA . ASP A 94 ? 0.9761 1.3723 0.9532 -0.0794 0.0774 -0.1294 94 ASP A CA 727 C C . ASP A 94 ? 0.9410 1.3361 0.9221 -0.0797 0.0832 -0.1263 94 ASP A C 728 O O . ASP A 94 ? 0.9205 1.3265 0.8957 -0.0840 0.0891 -0.1295 94 ASP A O 729 C CB . ASP A 94 ? 1.0132 1.4132 0.9799 -0.0786 0.0730 -0.1168 94 ASP A CB 730 C CG . ASP A 94 ? 1.0685 1.4766 1.0345 -0.0795 0.0665 -0.1193 94 ASP A CG 731 O OD1 . ASP A 94 ? 1.1201 1.5197 1.0958 -0.0784 0.0630 -0.1209 94 ASP A OD1 732 O OD2 . ASP A 94 ? 1.1160 1.5408 1.0706 -0.0825 0.0650 -0.1199 94 ASP A OD2 733 N N . PHE A 95 ? 0.8900 1.2736 0.8802 -0.0767 0.0817 -0.1207 95 PHE A N 734 C CA . PHE A 95 ? 0.8575 1.2394 0.8486 -0.0804 0.0869 -0.1164 95 PHE A CA 735 C C . PHE A 95 ? 0.8479 1.2128 0.8285 -0.0800 0.0845 -0.1017 95 PHE A C 736 O O . PHE A 95 ? 0.8662 1.2207 0.8539 -0.0740 0.0792 -0.0976 95 PHE A O 737 C CB . PHE A 95 ? 0.8369 1.2201 0.8460 -0.0763 0.0875 -0.1239 95 PHE A CB 738 C CG . PHE A 95 ? 0.8379 1.2321 0.8494 -0.0830 0.0943 -0.1247 95 PHE A CG 739 C CD1 . PHE A 95 ? 0.8593 1.2413 0.8624 -0.0907 0.0964 -0.1140 95 PHE A CD1 740 C CD2 . PHE A 95 ? 0.8362 1.2536 0.8557 -0.0818 0.0990 -0.1369 95 PHE A CD2 741 C CE1 . PHE A 95 ? 0.8624 1.2558 0.8651 -0.1013 0.1034 -0.1159 95 PHE A CE1 742 C CE2 . PHE A 95 ? 0.8473 1.2833 0.8697 -0.0901 0.1055 -0.1390 95 PHE A CE2 743 C CZ . PHE A 95 ? 0.8552 1.2795 0.8691 -0.1020 0.1079 -0.1287 95 PHE A CZ 744 N N . ASN A 96 ? 0.8613 1.2211 0.8212 -0.0854 0.0888 -0.0936 96 ASN A N 745 C CA . ASN A 96 ? 0.8701 1.2079 0.8109 -0.0820 0.0872 -0.0791 96 ASN A CA 746 C C . ASN A 96 ? 0.8525 1.1716 0.7954 -0.0845 0.0892 -0.0745 96 ASN A C 747 O O . ASN A 96 ? 0.8131 1.1363 0.7603 -0.0951 0.0955 -0.0795 96 ASN A O 748 C CB . ASN A 96 ? 0.9251 1.2559 0.8361 -0.0869 0.0924 -0.0720 96 ASN A CB 749 C CG . ASN A 96 ? 0.9743 1.2818 0.8588 -0.0769 0.0894 -0.0570 96 ASN A CG 750 O OD1 . ASN A 96 ? 0.9764 1.2931 0.8623 -0.0646 0.0820 -0.0543 96 ASN A OD1 751 N ND2 . ASN A 96 ? 1.0099 1.2873 0.8671 -0.0819 0.0955 -0.0477 96 ASN A ND2 752 N N . ASP A 97 ? 0.8598 1.1619 0.7991 -0.0750 0.0840 -0.0654 97 ASP A N 753 C CA . ASP A 97 ? 0.8567 1.1387 0.7972 -0.0760 0.0849 -0.0607 97 ASP A CA 754 C C . ASP A 97 ? 0.8111 1.1078 0.7795 -0.0814 0.0859 -0.0719 97 ASP A C 755 O O . ASP A 97 ? 0.7875 1.0783 0.7549 -0.0908 0.0911 -0.0723 97 ASP A O 756 C CB . ASP A 97 ? 0.9261 1.1801 0.8338 -0.0850 0.0926 -0.0514 97 ASP A CB 757 C CG . ASP A 97 ? 0.9719 1.2011 0.8460 -0.0735 0.0908 -0.0378 97 ASP A CG 758 O OD1 . ASP A 97 ? 0.9718 1.2023 0.8507 -0.0575 0.0831 -0.0333 97 ASP A OD1 759 O OD2 . ASP A 97 ? 1.0572 1.2657 0.8976 -0.0800 0.0975 -0.0316 97 ASP A OD2 760 N N . TYR A 98 ? 0.7726 1.0877 0.7625 -0.0754 0.0812 -0.0813 98 TYR A N 761 C CA . TYR A 98 ? 0.7573 1.0858 0.7698 -0.0757 0.0818 -0.0926 98 TYR A CA 762 C C . TYR A 98 ? 0.7587 1.0747 0.7807 -0.0736 0.0798 -0.0893 98 TYR A C 763 O O . TYR A 98 ? 0.7426 1.0667 0.7734 -0.0784 0.0835 -0.0942 98 TYR A O 764 C CB . TYR A 98 ? 0.7396 1.0782 0.7637 -0.0684 0.0772 -0.1019 98 TYR A CB 765 C CG . TYR A 98 ? 0.7400 1.0889 0.7801 -0.0644 0.0782 -0.1143 98 TYR A CG 766 C CD1 . TYR A 98 ? 0.7511 1.1183 0.7948 -0.0680 0.0844 -0.1211 98 TYR A CD1 767 C CD2 . TYR A 98 ? 0.7305 1.0712 0.7789 -0.0562 0.0732 -0.1197 98 TYR A CD2 768 C CE1 . TYR A 98 ? 0.7555 1.1353 0.8117 -0.0597 0.0850 -0.1326 98 TYR A CE1 769 C CE2 . TYR A 98 ? 0.7238 1.0686 0.7806 -0.0488 0.0742 -0.1305 98 TYR A CE2 770 C CZ . TYR A 98 ? 0.7591 1.1247 0.8202 -0.0485 0.0798 -0.1368 98 TYR A CZ 771 O OH . TYR A 98 ? 0.7849 1.1580 0.8524 -0.0367 0.0805 -0.1478 98 TYR A OH 772 N N . GLU A 99 ? 0.7573 1.0573 0.7768 -0.0664 0.0741 -0.0812 99 GLU A N 773 C CA . GLU A 99 ? 0.7643 1.0515 0.7925 -0.0633 0.0716 -0.0779 99 GLU A CA 774 C C . GLU A 99 ? 0.7730 1.0450 0.7873 -0.0720 0.0772 -0.0713 99 GLU A C 775 O O . GLU A 99 ? 0.7491 1.0210 0.7737 -0.0753 0.0783 -0.0738 99 GLU A O 776 C CB . GLU A 99 ? 0.7785 1.0559 0.8056 -0.0536 0.0645 -0.0710 99 GLU A CB 777 C CG . GLU A 99 ? 0.7881 1.0777 0.8286 -0.0493 0.0593 -0.0789 99 GLU A CG 778 C CD . GLU A 99 ? 0.8253 1.1292 0.8581 -0.0512 0.0595 -0.0828 99 GLU A CD 779 O OE1 . GLU A 99 ? 0.8460 1.1505 0.8621 -0.0515 0.0610 -0.0758 99 GLU A OE1 780 O OE2 . GLU A 99 ? 0.8427 1.1543 0.8828 -0.0521 0.0584 -0.0929 99 GLU A OE2 781 N N . GLU A 100 ? 0.7944 1.0518 0.7819 -0.0764 0.0812 -0.0630 100 GLU A N 782 C CA . GLU A 100 ? 0.8161 1.0514 0.7812 -0.0882 0.0882 -0.0570 100 GLU A CA 783 C C . GLU A 100 ? 0.8200 1.0764 0.7930 -0.1047 0.0953 -0.0669 100 GLU A C 784 O O . GLU A 100 ? 0.8640 1.1109 0.8286 -0.1173 0.1005 -0.0660 100 GLU A O 785 C CB . GLU A 100 ? 0.8428 1.0525 0.7703 -0.0885 0.0916 -0.0462 100 GLU A CB 786 C CG . GLU A 100 ? 0.8534 1.0367 0.7640 -0.0721 0.0864 -0.0341 100 GLU A CG 787 C CD . GLU A 100 ? 0.8783 1.0295 0.7748 -0.0744 0.0887 -0.0278 100 GLU A CD 788 O OE1 . GLU A 100 ? 0.9151 1.0452 0.7884 -0.0911 0.0974 -0.0266 100 GLU A OE1 789 O OE2 . GLU A 100 ? 0.8360 0.9828 0.7425 -0.0612 0.0824 -0.0244 100 GLU A OE2 790 N N . LEU A 101 ? 0.7982 1.0852 0.7861 -0.1048 0.0959 -0.0769 101 LEU A N 791 C CA . LEU A 101 ? 0.7911 1.1077 0.7890 -0.1172 0.1022 -0.0878 101 LEU A CA 792 C C . LEU A 101 ? 0.7596 1.0949 0.7853 -0.1107 0.0987 -0.0958 101 LEU A C 793 O O . LEU A 101 ? 0.7038 1.0540 0.7333 -0.1219 0.1032 -0.1003 101 LEU A O 794 C CB . LEU A 101 ? 0.7898 1.1328 0.7918 -0.1165 0.1041 -0.0961 101 LEU A CB 795 C CG . LEU A 101 ? 0.7813 1.1635 0.7948 -0.1260 0.1104 -0.1087 101 LEU A CG 796 C CD1 . LEU A 101 ? 0.7967 1.1785 0.7915 -0.1496 0.1197 -0.1067 101 LEU A CD1 797 C CD2 . LEU A 101 ? 0.8138 1.2165 0.8276 -0.1228 0.1119 -0.1156 101 LEU A CD2 798 N N . LYS A 102 ? 0.7548 1.0896 0.7974 -0.0935 0.0909 -0.0980 102 LYS A N 799 C CA . LYS A 102 ? 0.7555 1.1006 0.8200 -0.0845 0.0869 -0.1043 102 LYS A CA 800 C C . LYS A 102 ? 0.7518 1.0812 0.8138 -0.0907 0.0872 -0.0978 102 LYS A C 801 O O . LYS A 102 ? 0.7551 1.1023 0.8304 -0.0920 0.0879 -0.1038 102 LYS A O 802 C CB . LYS A 102 ? 0.7731 1.1088 0.8476 -0.0680 0.0792 -0.1057 102 LYS A CB 803 C CG . LYS A 102 ? 0.8200 1.1708 0.8968 -0.0616 0.0794 -0.1151 102 LYS A CG 804 C CD . LYS A 102 ? 0.8456 1.1800 0.9235 -0.0510 0.0729 -0.1156 102 LYS A CD 805 C CE . LYS A 102 ? 0.8646 1.1984 0.9534 -0.0387 0.0700 -0.1241 102 LYS A CE 806 N NZ . LYS A 102 ? 0.8735 1.1884 0.9569 -0.0327 0.0654 -0.1264 102 LYS A NZ 807 N N . HIS A 103 ? 0.7676 1.0645 0.8105 -0.0935 0.0867 -0.0858 103 HIS A N 808 C CA . HIS A 103 ? 0.7761 1.0519 0.8104 -0.1001 0.0879 -0.0792 103 HIS A CA 809 C C . HIS A 103 ? 0.7983 1.0836 0.8207 -0.1215 0.0970 -0.0823 103 HIS A C 810 O O . HIS A 103 ? 0.7791 1.0676 0.8058 -0.1291 0.0985 -0.0842 103 HIS A O 811 C CB . HIS A 103 ? 0.7968 1.0339 0.8069 -0.0958 0.0862 -0.0656 103 HIS A CB 812 C CG . HIS A 103 ? 0.8201 1.0293 0.8152 -0.1019 0.0884 -0.0587 103 HIS A CG 813 N ND1 . HIS A 103 ? 0.8045 1.0049 0.8122 -0.0918 0.0825 -0.0563 103 HIS A ND1 814 C CD2 . HIS A 103 ? 0.8403 1.0261 0.8058 -0.1188 0.0964 -0.0542 103 HIS A CD2 815 C CE1 . HIS A 103 ? 0.8046 0.9783 0.7925 -0.1006 0.0865 -0.0506 103 HIS A CE1 816 N NE2 . HIS A 103 ? 0.8439 1.0064 0.8045 -0.1177 0.0951 -0.0494 103 HIS A NE2 817 N N . LEU A 104 ? 0.8307 1.1214 0.8364 -0.1330 0.1034 -0.0832 104 LEU A N 818 C CA . LEU A 104 ? 0.8823 1.1850 0.8733 -0.1577 0.1134 -0.0873 104 LEU A CA 819 C C . LEU A 104 ? 0.8751 1.2288 0.8947 -0.1607 0.1142 -0.1013 104 LEU A C 820 O O . LEU A 104 ? 0.8814 1.2484 0.8959 -0.1800 0.1202 -0.1051 104 LEU A O 821 C CB . LEU A 104 ? 0.9138 1.2173 0.8840 -0.1674 0.1195 -0.0868 104 LEU A CB 822 C CG . LEU A 104 ? 0.9605 1.2429 0.8921 -0.1949 0.1307 -0.0829 104 LEU A CG 823 C CD1 . LEU A 104 ? 1.0017 1.2227 0.8974 -0.1945 0.1312 -0.0683 104 LEU A CD1 824 C CD2 . LEU A 104 ? 0.9787 1.2709 0.8960 -0.2021 0.1360 -0.0845 104 LEU A CD2 825 N N . LEU A 105 ? 0.8822 1.2636 0.9288 -0.1410 0.1082 -0.1091 105 LEU A N 826 C CA . LEU A 105 ? 0.8548 1.2853 0.9273 -0.1353 0.1077 -0.1225 105 LEU A CA 827 C C . LEU A 105 ? 0.8457 1.2796 0.9319 -0.1313 0.1040 -0.1235 105 LEU A C 828 O O . LEU A 105 ? 0.8965 1.3736 0.9979 -0.1324 0.1055 -0.1338 105 LEU A O 829 C CB . LEU A 105 ? 0.8370 1.2808 0.9270 -0.1109 0.1017 -0.1289 105 LEU A CB 830 C CG . LEU A 105 ? 0.8321 1.3043 0.9210 -0.1113 0.1061 -0.1369 105 LEU A CG 831 C CD1 . LEU A 105 ? 0.8365 1.3096 0.9376 -0.0859 0.0997 -0.1426 105 LEU A CD1 832 C CD2 . LEU A 105 ? 0.8496 1.3744 0.9451 -0.1235 0.1130 -0.1482 105 LEU A CD2 833 N N . SER A 106 ? 0.9318 1.5361 0.8273 -0.0725 0.1469 -0.1264 106 SER A N 834 C CA A SER A 106 ? 0.9401 1.5574 0.8252 -0.0750 0.1472 -0.1274 106 SER A CA 835 C CA B SER A 106 ? 0.9366 1.5541 0.8219 -0.0750 0.1472 -0.1274 106 SER A CA 836 C C . SER A 106 ? 0.9698 1.5832 0.8284 -0.0955 0.1503 -0.1408 106 SER A C 837 O O . SER A 106 ? 1.0019 1.6290 0.8472 -0.1019 0.1484 -0.1439 106 SER A O 838 C CB A SER A 106 ? 0.9426 1.5392 0.8245 -0.0625 0.1541 -0.1212 106 SER A CB 839 C CB B SER A 106 ? 0.9355 1.5321 0.8181 -0.0622 0.1539 -0.1210 106 SER A CB 840 O OG A SER A 106 ? 0.9506 1.5106 0.8124 -0.0666 0.1647 -0.1285 106 SER A OG 841 O OG B SER A 106 ? 0.8871 1.4839 0.7955 -0.0462 0.1498 -0.1084 106 SER A OG 842 N N . ARG A 107 ? 1.0084 1.6016 0.8578 -0.1068 0.1543 -0.1482 107 ARG A N 843 C CA . ARG A 107 ? 1.0755 1.6634 0.9018 -0.1292 0.1560 -0.1607 107 ARG A CA 844 C C . ARG A 107 ? 1.0299 1.6485 0.8698 -0.1419 0.1500 -0.1621 107 ARG A C 845 O O . ARG A 107 ? 1.0428 1.6550 0.8687 -0.1621 0.1516 -0.1706 107 ARG A O 846 C CB . ARG A 107 ? 1.1500 1.6890 0.9540 -0.1346 0.1661 -0.1675 107 ARG A CB 847 C CG . ARG A 107 ? 1.2364 1.7456 1.0186 -0.1289 0.1745 -0.1715 107 ARG A CG 848 C CD . ARG A 107 ? 1.2817 1.7807 1.0802 -0.1049 0.1789 -0.1599 107 ARG A CD 849 N NE . ARG A 107 ? 1.3662 1.8451 1.1469 -0.0977 0.1888 -0.1627 107 ARG A NE 850 C CZ . ARG A 107 ? 1.4189 1.8569 1.1863 -0.0922 0.2007 -0.1660 107 ARG A CZ 851 N NH1 . ARG A 107 ? 1.4396 1.8495 1.2089 -0.0935 0.2028 -0.1659 107 ARG A NH1 852 N NH2 . ARG A 107 ? 1.4498 1.8743 1.2013 -0.0843 0.2113 -0.1689 107 ARG A NH2 853 N N . ILE A 108 ? 0.9724 1.6237 0.8401 -0.1300 0.1438 -0.1535 108 ILE A N 854 C CA . ILE A 108 ? 0.9448 1.6281 0.8297 -0.1376 0.1405 -0.1536 108 ILE A CA 855 C C . ILE A 108 ? 0.9054 1.6366 0.8144 -0.1304 0.1310 -0.1472 108 ILE A C 856 O O . ILE A 108 ? 0.8891 1.6254 0.8115 -0.1115 0.1273 -0.1388 108 ILE A O 857 C CB . ILE A 108 ? 0.9288 1.5991 0.8241 -0.1280 0.1448 -0.1499 108 ILE A CB 858 C CG1 . ILE A 108 ? 0.9539 1.5786 0.8266 -0.1359 0.1530 -0.1542 108 ILE A CG1 859 C CG2 . ILE A 108 ? 0.9071 1.6130 0.8206 -0.1334 0.1442 -0.1500 108 ILE A CG2 860 C CD1 . ILE A 108 ? 0.9468 1.5542 0.8242 -0.1266 0.1558 -0.1496 108 ILE A CD1 861 N N . ASN A 109 ? 0.8920 1.6582 0.8084 -0.1457 0.1264 -0.1502 109 ASN A N 862 C CA . ASN A 109 ? 0.8882 1.7035 0.8307 -0.1394 0.1166 -0.1431 109 ASN A CA 863 C C . ASN A 109 ? 0.8760 1.7233 0.8477 -0.1355 0.1180 -0.1403 109 ASN A C 864 O O . ASN A 109 ? 0.8428 1.7262 0.8409 -0.1229 0.1114 -0.1328 109 ASN A O 865 C CB . ASN A 109 ? 0.9204 1.7597 0.8535 -0.1588 0.1079 -0.1467 109 ASN A CB 866 C CG . ASN A 109 ? 0.9509 1.7660 0.8556 -0.1588 0.1060 -0.1486 109 ASN A CG 867 O OD1 . ASN A 109 ? 0.9342 1.7495 0.8439 -0.1407 0.1036 -0.1402 109 ASN A OD1 868 N ND2 . ASN A 109 ? 1.0075 1.8004 0.8814 -0.1795 0.1078 -0.1596 109 ASN A ND2 869 N N . HIS A 110 ? 0.8845 1.7189 0.8511 -0.1457 0.1272 -0.1457 110 HIS A N 870 C CA . HIS A 110 ? 0.8754 1.7417 0.8670 -0.1433 0.1314 -0.1437 110 HIS A CA 871 C C . HIS A 110 ? 0.8803 1.7179 0.8607 -0.1458 0.1438 -0.1474 110 HIS A C 872 O O . HIS A 110 ? 0.8910 1.6994 0.8477 -0.1633 0.1488 -0.1528 110 HIS A O 873 C CB . HIS A 110 ? 0.8936 1.8067 0.9004 -0.1629 0.1269 -0.1444 110 HIS A CB 874 C CG . HIS A 110 ? 0.8883 1.8461 0.9291 -0.1563 0.1309 -0.1401 110 HIS A CG 875 N ND1 . HIS A 110 ? 0.8934 1.8883 0.9493 -0.1762 0.1330 -0.1407 110 HIS A ND1 876 C CD2 . HIS A 110 ? 0.8694 1.8400 0.9324 -0.1317 0.1341 -0.1352 110 HIS A CD2 877 C CE1 . HIS A 110 ? 0.8789 1.9105 0.9666 -0.1626 0.1388 -0.1360 110 HIS A CE1 878 N NE2 . HIS A 110 ? 0.8556 1.8710 0.9464 -0.1352 0.1397 -0.1334 110 HIS A NE2 879 N N . PHE A 111 ? 0.8670 1.7112 0.8627 -0.1279 0.1482 -0.1443 111 PHE A N 880 C CA . PHE A 111 ? 0.8870 1.7102 0.8722 -0.1289 0.1596 -0.1469 111 PHE A CA 881 C C . PHE A 111 ? 0.8910 1.7582 0.8992 -0.1314 0.1671 -0.1465 111 PHE A C 882 O O . PHE A 111 ? 0.8730 1.7815 0.9100 -0.1204 0.1631 -0.1428 111 PHE A O 883 C CB . PHE A 111 ? 0.8680 1.6609 0.8486 -0.1059 0.1596 -0.1447 111 PHE A CB 884 C CG . PHE A 111 ? 0.8728 1.6163 0.8293 -0.1047 0.1566 -0.1443 111 PHE A CG 885 C CD1 . PHE A 111 ? 0.8928 1.6054 0.8246 -0.1219 0.1614 -0.1477 111 PHE A CD1 886 C CD2 . PHE A 111 ? 0.8438 1.5715 0.8045 -0.0856 0.1494 -0.1396 111 PHE A CD2 887 C CE1 . PHE A 111 ? 0.8863 1.5554 0.8001 -0.1180 0.1594 -0.1463 111 PHE A CE1 888 C CE2 . PHE A 111 ? 0.8347 1.5216 0.7785 -0.0834 0.1473 -0.1378 111 PHE A CE2 889 C CZ . PHE A 111 ? 0.8546 1.5130 0.7757 -0.0987 0.1526 -0.1411 111 PHE A CZ 890 N N . GLU A 112 ? 0.9265 1.7849 0.9226 -0.1450 0.1787 -0.1492 112 GLU A N 891 C CA . GLU A 112 ? 0.9499 1.8466 0.9657 -0.1457 0.1900 -0.1484 112 GLU A CA 892 C C . GLU A 112 ? 0.9392 1.8044 0.9353 -0.1367 0.2016 -0.1502 112 GLU A C 893 O O . GLU A 112 ? 0.9366 1.7675 0.9051 -0.1512 0.2069 -0.1514 112 GLU A O 894 C CB . GLU A 112 ? 0.9821 1.9039 1.0020 -0.1751 0.1942 -0.1486 112 GLU A CB 895 C CG . GLU A 112 ? 1.0025 1.9764 1.0525 -0.1833 0.1843 -0.1458 112 GLU A CG 896 C CD . GLU A 112 ? 1.0022 2.0359 1.0926 -0.1730 0.1903 -0.1411 112 GLU A CD 897 O OE1 . GLU A 112 ? 1.0004 2.0385 1.0935 -0.1668 0.2060 -0.1414 112 GLU A OE1 898 O OE2 . GLU A 112 ? 1.0090 2.0860 1.1284 -0.1708 0.1794 -0.1368 112 GLU A OE2 899 N N . LYS A 113 ? 0.9193 1.7935 0.9273 -0.1129 0.2049 -0.1503 113 LYS A N 900 C CA . LYS A 113 ? 0.9547 1.7975 0.9400 -0.1032 0.2146 -0.1530 113 LYS A CA 901 C C . LYS A 113 ? 0.9726 1.8359 0.9559 -0.1160 0.2324 -0.1537 113 LYS A C 902 O O . LYS A 113 ? 0.9759 1.8906 0.9895 -0.1165 0.2398 -0.1524 113 LYS A O 903 C CB . LYS A 113 ? 0.9543 1.7972 0.9503 -0.0743 0.2125 -0.1544 113 LYS A CB 904 C CG . LYS A 113 ? 0.9949 1.8005 0.9625 -0.0643 0.2201 -0.1586 113 LYS A CG 905 C CD . LYS A 113 ? 1.0137 1.7889 0.9769 -0.0418 0.2084 -0.1595 113 LYS A CD 906 C CE . LYS A 113 ? 1.0067 1.8138 1.0014 -0.0200 0.2080 -0.1602 113 LYS A CE 907 N NZ . LYS A 113 ? 0.9951 1.7769 0.9926 -0.0037 0.1919 -0.1579 113 LYS A NZ 908 N N . ILE A 114 ? 0.9909 1.8158 0.9401 -0.1264 0.2393 -0.1544 114 ILE A N 909 C CA . ILE A 114 ? 1.0306 1.8699 0.9725 -0.1376 0.2579 -0.1540 114 ILE A CA 910 C C . ILE A 114 ? 1.0571 1.8522 0.9609 -0.1299 0.2648 -0.1560 114 ILE A C 911 O O . ILE A 114 ? 1.0926 1.8398 0.9717 -0.1245 0.2533 -0.1562 114 ILE A O 912 C CB . ILE A 114 ? 1.0504 1.8953 0.9882 -0.1695 0.2612 -0.1501 114 ILE A CB 913 C CG1 . ILE A 114 ? 1.0808 1.8683 0.9854 -0.1808 0.2511 -0.1493 114 ILE A CG1 914 C CG2 . ILE A 114 ? 1.0255 1.9207 1.0009 -0.1798 0.2552 -0.1484 114 ILE A CG2 915 C CD1 . ILE A 114 ? 1.1210 1.8982 1.0095 -0.2107 0.2582 -0.1457 114 ILE A CD1 916 N N . GLN A 115 ? 1.0630 1.8761 0.9622 -0.1301 0.2836 -0.1568 115 GLN A N 917 C CA . GLN A 115 ? 1.0763 1.8513 0.9356 -0.1239 0.2918 -0.1590 115 GLN A CA 918 C C . GLN A 115 ? 1.0860 1.8315 0.9131 -0.1494 0.2959 -0.1530 115 GLN A C 919 O O . GLN A 115 ? 1.0754 1.8488 0.9121 -0.1702 0.3076 -0.1486 115 GLN A O 920 C CB . GLN A 115 ? 1.0833 1.8916 0.9501 -0.1112 0.3127 -0.1631 115 GLN A CB 921 C CG . GLN A 115 ? 1.1219 1.8898 0.9457 -0.0984 0.3195 -0.1683 115 GLN A CG 922 C CD . GLN A 115 ? 1.1374 1.9373 0.9639 -0.0879 0.3446 -0.1729 115 GLN A CD 923 O OE1 . GLN A 115 ? 1.1503 1.9422 0.9706 -0.0634 0.3479 -0.1815 115 GLN A OE1 924 N NE2 . GLN A 115 ? 1.1385 1.9743 0.9745 -0.1065 0.3631 -0.1671 115 GLN A NE2 925 N N . ILE A 116 ? 1.0889 1.7787 0.8797 -0.1481 0.2857 -0.1518 116 ILE A N 926 C CA . ILE A 116 ? 1.1239 1.7791 0.8817 -0.1701 0.2878 -0.1447 116 ILE A CA 927 C C . ILE A 116 ? 1.1725 1.7995 0.8880 -0.1673 0.2977 -0.1438 116 ILE A C 928 O O . ILE A 116 ? 1.2196 1.8379 0.9126 -0.1866 0.3087 -0.1371 116 ILE A O 929 C CB . ILE A 116 ? 1.1106 1.7230 0.8591 -0.1747 0.2683 -0.1410 116 ILE A CB 930 C CG1 . ILE A 116 ? 1.0908 1.6743 0.8331 -0.1514 0.2524 -0.1442 116 ILE A CG1 931 C CG2 . ILE A 116 ? 1.0806 1.7178 0.8610 -0.1856 0.2623 -0.1412 116 ILE A CG2 932 C CD1 . ILE A 116 ? 1.0907 1.6298 0.8205 -0.1546 0.2360 -0.1388 116 ILE A CD1 933 N N . ILE A 117 ? 1.1846 1.7956 0.8871 -0.1445 0.2934 -0.1503 117 ILE A N 934 C CA . ILE A 117 ? 1.2253 1.8112 0.8846 -0.1400 0.3029 -0.1518 117 ILE A CA 935 C C . ILE A 117 ? 1.2235 1.8325 0.8906 -0.1165 0.3132 -0.1629 117 ILE A C 936 O O . ILE A 117 ? 1.2050 1.7968 0.8740 -0.0968 0.2993 -0.1694 117 ILE A O 937 C CB . ILE A 117 ? 1.2452 1.7711 0.8666 -0.1372 0.2838 -0.1484 117 ILE A CB 938 C CG1 . ILE A 117 ? 1.2294 1.7319 0.8507 -0.1555 0.2719 -0.1378 117 ILE A CG1 939 C CG2 . ILE A 117 ? 1.3032 1.8023 0.8737 -0.1383 0.2934 -0.1481 117 ILE A CG2 940 C CD1 . ILE A 117 ? 1.2529 1.6996 0.8387 -0.1549 0.2548 -0.1312 117 ILE A CD1 941 N N . PRO A 118 ? 1.2484 1.8957 0.9209 -0.1184 0.3382 -0.1648 118 PRO A N 942 C CA . PRO A 118 ? 1.2564 1.9280 0.9390 -0.0945 0.3513 -0.1758 118 PRO A CA 943 C C . PRO A 118 ? 1.2994 1.9233 0.9373 -0.0768 0.3460 -0.1847 118 PRO A C 944 O O . PRO A 118 ? 1.3220 1.9022 0.9122 -0.0864 0.3414 -0.1812 118 PRO A O 945 C CB . PRO A 118 ? 1.2840 1.9966 0.9692 -0.1045 0.3814 -0.1733 118 PRO A CB 946 C CG . PRO A 118 ? 1.2677 1.9942 0.9662 -0.1340 0.3806 -0.1609 118 PRO A CG 947 C CD . PRO A 118 ? 1.2726 1.9433 0.9442 -0.1432 0.3563 -0.1561 118 PRO A CD 948 N N . LYS A 119 ? 1.3119 1.9435 0.9651 -0.0515 0.3455 -0.1956 119 LYS A N 949 C CA . LYS A 119 ? 1.3645 1.9509 0.9773 -0.0339 0.3395 -0.2062 119 LYS A CA 950 C C . LYS A 119 ? 1.4236 2.0019 0.9901 -0.0338 0.3639 -0.2117 119 LYS A C 951 O O . LYS A 119 ? 1.4774 2.0061 0.9902 -0.0326 0.3573 -0.2159 119 LYS A O 952 C CB . LYS A 119 ? 1.3617 1.9605 1.0060 -0.0072 0.3350 -0.2165 119 LYS A CB 953 C CG . LYS A 119 ? 1.4016 1.9469 1.0106 0.0091 0.3198 -0.2267 119 LYS A CG 954 C CD . LYS A 119 ? 1.3946 1.9511 1.0419 0.0326 0.3115 -0.2335 119 LYS A CD 955 C CE . LYS A 119 ? 1.4383 1.9389 1.0536 0.0460 0.2928 -0.2427 119 LYS A CE 956 N NZ . LYS A 119 ? 1.4256 1.9331 1.0816 0.0646 0.2795 -0.2452 119 LYS A NZ 957 N N . SER A 120 ? 1.4240 2.0526 1.0116 -0.0358 0.3919 -0.2109 120 SER A N 958 C CA . SER A 120 ? 1.4487 2.0787 0.9970 -0.0357 0.4203 -0.2152 120 SER A CA 959 C C . SER A 120 ? 1.4765 2.0763 0.9755 -0.0615 0.4214 -0.2044 120 SER A C 960 O O . SER A 120 ? 1.5453 2.1229 0.9919 -0.0609 0.4366 -0.2085 120 SER A O 961 C CB . SER A 120 ? 1.4269 2.1262 1.0199 -0.0331 0.4502 -0.2138 120 SER A CB 962 O OG . SER A 120 ? 1.3906 2.1257 1.0197 -0.0581 0.4488 -0.1989 120 SER A OG 963 N N . SER A 121 ? 1.4497 2.0466 0.9632 -0.0837 0.4053 -0.1906 121 SER A N 964 C CA . SER A 121 ? 1.4726 2.0456 0.9469 -0.1095 0.4074 -0.1776 121 SER A CA 965 C C . SER A 121 ? 1.5035 2.0088 0.9167 -0.1108 0.3876 -0.1770 121 SER A C 966 O O . SER A 121 ? 1.5121 1.9927 0.8901 -0.1310 0.3867 -0.1649 121 SER A O 967 C CB . SER A 121 ? 1.4262 2.0165 0.9375 -0.1322 0.3974 -0.1638 121 SER A CB 968 O OG . SER A 121 ? 1.3851 1.9548 0.9171 -0.1264 0.3681 -0.1643 121 SER A OG 969 N N . TRP A 122 ? 1.5027 1.9781 0.9042 -0.0902 0.3706 -0.1887 122 TRP A N 970 C CA . TRP A 122 ? 1.5374 1.9510 0.8828 -0.0910 0.3496 -0.1884 122 TRP A CA 971 C C . TRP A 122 ? 1.6094 2.0028 0.8945 -0.0840 0.3676 -0.1983 122 TRP A C 972 O O . TRP A 122 ? 1.6442 2.0145 0.9089 -0.0647 0.3621 -0.2134 122 TRP A O 973 C CB . TRP A 122 ? 1.5036 1.8936 0.8663 -0.0752 0.3204 -0.1951 122 TRP A CB 974 C CG . TRP A 122 ? 1.4534 1.8546 0.8651 -0.0825 0.3013 -0.1848 122 TRP A CG 975 C CD1 . TRP A 122 ? 1.3933 1.8281 0.8622 -0.0722 0.2976 -0.1881 122 TRP A CD1 976 C CD2 . TRP A 122 ? 1.4448 1.8221 0.8505 -0.1009 0.2839 -0.1693 122 TRP A CD2 977 N NE1 . TRP A 122 ? 1.3596 1.7923 0.8556 -0.0835 0.2799 -0.1768 122 TRP A NE1 978 C CE2 . TRP A 122 ? 1.3828 1.7804 0.8423 -0.1004 0.2718 -0.1655 122 TRP A CE2 979 C CE3 . TRP A 122 ? 1.4734 1.8133 0.8329 -0.1170 0.2775 -0.1577 122 TRP A CE3 980 C CZ2 . TRP A 122 ? 1.3668 1.7474 0.8350 -0.1142 0.2554 -0.1522 122 TRP A CZ2 981 C CZ3 . TRP A 122 ? 1.4567 1.7804 0.8281 -0.1304 0.2600 -0.1432 122 TRP A CZ3 982 C CH2 . TRP A 122 ? 1.4121 1.7557 0.8374 -0.1284 0.2500 -0.1413 122 TRP A CH2 983 N N . SER A 123 ? 1.6462 2.0459 0.9004 -0.1006 0.3890 -0.1897 123 SER A N 984 C CA . SER A 123 ? 1.7143 2.1041 0.9123 -0.0950 0.4136 -0.1985 123 SER A CA 985 C C . SER A 123 ? 1.7772 2.1017 0.8994 -0.0968 0.3955 -0.2003 123 SER A C 986 O O . SER A 123 ? 1.8395 2.1477 0.9090 -0.0885 0.4123 -0.2117 123 SER A O 987 C CB . SER A 123 ? 1.7317 2.1567 0.9266 -0.1136 0.4454 -0.1867 123 SER A CB 988 O OG . SER A 123 ? 1.7178 2.1269 0.9053 -0.1400 0.4324 -0.1665 123 SER A OG 989 N N . SER A 124 ? 1.7688 2.0569 0.8852 -0.1073 0.3619 -0.1891 124 SER A N 990 C CA . SER A 124 ? 1.8102 2.0378 0.8595 -0.1109 0.3394 -0.1879 124 SER A CA 991 C C . SER A 124 ? 1.7925 1.9886 0.8489 -0.0960 0.3063 -0.1977 124 SER A C 992 O O . SER A 124 ? 1.8229 1.9699 0.8287 -0.0985 0.2834 -0.1974 124 SER A O 993 C CB . SER A 124 ? 1.8168 2.0237 0.8501 -0.1352 0.3247 -0.1644 124 SER A CB 994 O OG . SER A 124 ? 1.8165 2.0554 0.8558 -0.1515 0.3528 -0.1529 124 SER A OG 995 N N . HIS A 125 ? 1.7404 1.9653 0.8597 -0.0820 0.3029 -0.2051 125 HIS A N 996 C CA . HIS A 125 ? 1.7159 1.9160 0.8510 -0.0690 0.2726 -0.2123 125 HIS A CA 997 C C . HIS A 125 ? 1.7092 1.9343 0.8787 -0.0456 0.2851 -0.2310 125 HIS A C 998 O O . HIS A 125 ? 1.6778 1.9502 0.8809 -0.0403 0.3132 -0.2341 125 HIS A O 999 C CB . HIS A 125 ? 1.6414 1.8474 0.8267 -0.0778 0.2478 -0.1963 125 HIS A CB 1000 C CG . HIS A 125 ? 1.6434 1.8244 0.8026 -0.0986 0.2338 -0.1767 125 HIS A CG 1001 N ND1 . HIS A 125 ? 1.6337 1.8361 0.8007 -0.1154 0.2503 -0.1627 125 HIS A ND1 1002 C CD2 . HIS A 125 ? 1.6621 1.7984 0.7899 -0.1051 0.2040 -0.1676 125 HIS A CD2 1003 C CE1 . HIS A 125 ? 1.6561 1.8254 0.7959 -0.1302 0.2319 -0.1461 125 HIS A CE1 1004 N NE2 . HIS A 125 ? 1.6740 1.8047 0.7909 -0.1239 0.2035 -0.1482 125 HIS A NE2 1005 N N . GLU A 126 ? 1.7313 1.9247 0.8947 -0.0321 0.2631 -0.2422 126 GLU A N 1006 C CA . GLU A 126 ? 1.7193 1.9280 0.9134 -0.0086 0.2712 -0.2593 126 GLU A CA 1007 C C . GLU A 126 ? 1.6413 1.8807 0.9105 -0.0045 0.2576 -0.2519 126 GLU A C 1008 O O . GLU A 126 ? 1.6401 1.8567 0.9225 -0.0072 0.2270 -0.2457 126 GLU A O 1009 C CB . GLU A 126 ? 1.7863 1.9415 0.9336 0.0029 0.2544 -0.2756 126 GLU A CB 1010 C CG . GLU A 126 ? 1.8013 1.9636 0.9708 0.0286 0.2646 -0.2948 126 GLU A CG 1011 C CD . GLU A 126 ? 1.8262 2.0265 0.9985 0.0413 0.3066 -0.3050 126 GLU A CD 1012 O OE1 . GLU A 126 ? 1.8362 2.0203 0.9490 0.0394 0.3262 -0.3125 126 GLU A OE1 1013 O OE2 . GLU A 126 ? 1.8032 2.0513 1.0379 0.0531 0.3198 -0.3046 126 GLU A OE2 1014 N N . ALA A 127 ? 1.5906 1.8836 0.9089 0.0018 0.2808 -0.2521 127 ALA A N 1015 C CA . ALA A 127 ? 1.5044 1.8322 0.8913 0.0028 0.2711 -0.2433 127 ALA A CA 1016 C C . ALA A 127 ? 1.4804 1.8230 0.9059 0.0265 0.2714 -0.2550 127 ALA A C 1017 O O . ALA A 127 ? 1.4242 1.7911 0.9033 0.0288 0.2604 -0.2482 127 ALA A O 1018 C CB . ALA A 127 ? 1.4660 1.8445 0.8847 -0.0102 0.2921 -0.2325 127 ALA A CB 1019 N N . SER A 128 ? 1.5202 1.8462 0.9170 0.0444 0.2839 -0.2723 128 SER A N 1020 C CA . SER A 128 ? 1.5011 1.8409 0.9332 0.0691 0.2882 -0.2838 128 SER A CA 1021 C C . SER A 128 ? 1.5095 1.7946 0.9175 0.0809 0.2645 -0.2950 128 SER A C 1022 O O . SER A 128 ? 1.4950 1.7804 0.9219 0.1026 0.2681 -0.3063 128 SER A O 1023 C CB . SER A 128 ? 1.5460 1.9157 0.9748 0.0843 0.3250 -0.2956 128 SER A CB 1024 O OG . SER A 128 ? 1.5300 1.9620 1.0047 0.0766 0.3439 -0.2841 128 SER A OG 1025 N N . LEU A 129 ? 1.5237 1.7623 0.8919 0.0662 0.2394 -0.2908 129 LEU A N 1026 C CA . LEU A 129 ? 1.5520 1.7377 0.8981 0.0726 0.2126 -0.2992 129 LEU A CA 1027 C C . LEU A 129 ? 1.5059 1.6835 0.8823 0.0602 0.1791 -0.2829 129 LEU A C 1028 O O . LEU A 129 ? 1.5266 1.6595 0.8819 0.0579 0.1522 -0.2847 129 LEU A O 1029 C CB . LEU A 129 ? 1.6384 1.7715 0.9051 0.0671 0.2102 -0.3102 129 LEU A CB 1030 C CG . LEU A 129 ? 1.6963 1.8298 0.9222 0.0802 0.2446 -0.3282 129 LEU A CG 1031 C CD1 . LEU A 129 ? 1.7716 1.8453 0.9134 0.0737 0.2368 -0.3395 129 LEU A CD1 1032 C CD2 . LEU A 129 ? 1.7000 1.8443 0.9549 0.1079 0.2594 -0.3440 129 LEU A CD2 1033 N N . GLY A 130 ? 1.4465 1.6681 0.8731 0.0522 0.1812 -0.2671 130 GLY A N 1034 C CA . GLY A 130 ? 1.3935 1.6132 0.8521 0.0416 0.1540 -0.2509 130 GLY A CA 1035 C C . GLY A 130 ? 1.3485 1.5812 0.8593 0.0548 0.1433 -0.2498 130 GLY A C 1036 O O . GLY A 130 ? 1.2835 1.5545 0.8435 0.0526 0.1442 -0.2382 130 GLY A O 1037 N N . VAL A 131 ? 1.3655 1.5631 0.8621 0.0674 0.1320 -0.2615 131 VAL A N 1038 C CA . VAL A 131 ? 1.3233 1.5277 0.8643 0.0820 0.1232 -0.2617 131 VAL A CA 1039 C C . VAL A 131 ? 1.3346 1.4931 0.8682 0.0789 0.0908 -0.2596 131 VAL A C 1040 O O . VAL A 131 ? 1.3837 1.5033 0.8747 0.0668 0.0748 -0.2603 131 VAL A O 1041 C CB . VAL A 131 ? 1.3410 1.5521 0.8825 0.1051 0.1451 -0.2788 131 VAL A CB 1042 C CG1 . VAL A 131 ? 1.3075 1.5749 0.8725 0.1086 0.1756 -0.2774 131 VAL A CG1 1043 C CG2 . VAL A 131 ? 1.4122 1.5728 0.8899 0.1106 0.1479 -0.2980 131 VAL A CG2 1044 N N . SER A 132 ? 1.3012 1.4654 0.8771 0.0888 0.0804 -0.2558 132 SER A N 1045 C CA . SER A 132 ? 1.2957 1.4205 0.8726 0.0854 0.0500 -0.2521 132 SER A CA 1046 C C . SER A 132 ? 1.2881 1.4139 0.9014 0.1023 0.0466 -0.2540 132 SER A C 1047 O O . SER A 132 ? 1.2467 1.4149 0.9009 0.1133 0.0623 -0.2502 132 SER A O 1048 C CB . SER A 132 ? 1.2381 1.3732 0.8398 0.0676 0.0300 -0.2309 132 SER A CB 1049 O OG . SER A 132 ? 1.2193 1.3259 0.8339 0.0647 0.0020 -0.2245 132 SER A OG 1050 N N . SER A 133 ? 1.3211 1.3988 0.9191 0.1030 0.0244 -0.2590 133 SER A N 1051 C CA . SER A 133 ? 1.3136 1.3834 0.9447 0.1162 0.0160 -0.2582 133 SER A CA 1052 C C . SER A 133 ? 1.2514 1.3557 0.9405 0.1100 0.0046 -0.2351 133 SER A C 1053 O O . SER A 133 ? 1.2201 1.3349 0.9457 0.1219 0.0040 -0.2306 133 SER A O 1054 C CB . SER A 133 ? 1.3704 1.3759 0.9678 0.1141 -0.0077 -0.2682 133 SER A CB 1055 O OG . SER A 133 ? 1.3736 1.3596 0.9581 0.0919 -0.0337 -0.2573 133 SER A OG 1056 N N . ALA A 134 ? 1.2384 1.3588 0.9342 0.0920 -0.0037 -0.2204 134 ALA A N 1057 C CA . ALA A 134 ? 1.1955 1.3514 0.9425 0.0861 -0.0103 -0.1991 134 ALA A CA 1058 C C . ALA A 134 ? 1.1591 1.3690 0.9404 0.0955 0.0128 -0.1953 134 ALA A C 1059 O O . ALA A 134 ? 1.0946 1.3309 0.9183 0.0965 0.0092 -0.1810 134 ALA A O 1060 C CB . ALA A 134 ? 1.1836 1.3412 0.9261 0.0666 -0.0225 -0.1860 134 ALA A CB 1061 N N . CYS A 135 ? 1.1935 1.4203 0.9559 0.1014 0.0361 -0.2075 135 CYS A N 1062 C CA . CYS A 135 ? 1.1628 1.4421 0.9562 0.1091 0.0577 -0.2048 135 CYS A CA 1063 C C . CYS A 135 ? 1.1575 1.4406 0.9476 0.1299 0.0756 -0.2200 135 CYS A C 1064 O O . CYS A 135 ? 1.1360 1.4339 0.9072 0.1328 0.0967 -0.2304 135 CYS A O 1065 C CB . CYS A 135 ? 1.1815 1.4866 0.9633 0.0956 0.0713 -0.2025 135 CYS A CB 1066 S SG . CYS A 135 ? 1.2073 1.5072 0.9925 0.0738 0.0532 -0.1852 135 CYS A SG 1067 N N . PRO A 136 ? 1.1442 1.4144 0.9543 0.1449 0.0679 -0.2205 136 PRO A N 1068 C CA . PRO A 136 ? 1.1683 1.4365 0.9766 0.1677 0.0837 -0.2349 136 PRO A CA 1069 C C . PRO A 136 ? 1.1313 1.4590 0.9805 0.1791 0.1031 -0.2297 136 PRO A C 1070 O O . PRO A 136 ? 1.0727 1.4353 0.9589 0.1729 0.0975 -0.2134 136 PRO A O 1071 C CB . PRO A 136 ? 1.1894 1.4181 1.0065 0.1771 0.0642 -0.2340 136 PRO A CB 1072 C CG . PRO A 136 ? 1.1376 1.3806 0.9880 0.1632 0.0453 -0.2125 136 PRO A CG 1073 C CD . PRO A 136 ? 1.1147 1.3697 0.9504 0.1417 0.0442 -0.2067 136 PRO A CD 1074 N N . TYR A 137 ? 1.1741 1.5131 1.0158 0.1957 0.1255 -0.2435 137 TYR A N 1075 C CA . TYR A 137 ? 1.1500 1.5461 1.0328 0.2089 0.1436 -0.2391 137 TYR A CA 1076 C C . TYR A 137 ? 1.1803 1.5664 1.0622 0.2368 0.1586 -0.2536 137 TYR A C 1077 O O . TYR A 137 ? 1.2277 1.5991 1.0749 0.2427 0.1760 -0.2702 137 TYR A O 1078 C CB . TYR A 137 ? 1.1401 1.5807 1.0208 0.1957 0.1622 -0.2380 137 TYR A CB 1079 C CG . TYR A 137 ? 1.1181 1.6211 1.0416 0.2069 0.1802 -0.2334 137 TYR A CG 1080 C CD1 . TYR A 137 ? 1.0807 1.6226 1.0496 0.2047 0.1708 -0.2167 137 TYR A CD1 1081 C CD2 . TYR A 137 ? 1.1290 1.6536 1.0473 0.2191 0.2064 -0.2450 137 TYR A CD2 1082 C CE1 . TYR A 137 ? 1.0555 1.6560 1.0640 0.2134 0.1845 -0.2114 137 TYR A CE1 1083 C CE2 . TYR A 137 ? 1.1097 1.6955 1.0717 0.2286 0.2217 -0.2391 137 TYR A CE2 1084 C CZ . TYR A 137 ? 1.0725 1.6960 1.0796 0.2252 0.2093 -0.2222 137 TYR A CZ 1085 O OH . TYR A 137 ? 1.0512 1.7368 1.1021 0.2332 0.2218 -0.2154 137 TYR A OH 1086 N N . GLN A 138 ? 1.1660 1.5593 1.0854 0.2544 0.1525 -0.2467 138 GLN A N 1087 C CA . GLN A 138 ? 1.2120 1.5912 1.1352 0.2839 0.1647 -0.2590 138 GLN A CA 1088 C C . GLN A 138 ? 1.2783 1.5852 1.1476 0.2888 0.1615 -0.2791 138 GLN A C 1089 O O . GLN A 138 ? 1.3188 1.6134 1.1644 0.3058 0.1823 -0.2974 138 GLN A O 1090 C CB . GLN A 138 ? 1.2188 1.6521 1.1595 0.2972 0.1947 -0.2641 138 GLN A CB 1091 C CG . GLN A 138 ? 1.1697 1.6752 1.1604 0.2896 0.1970 -0.2453 138 GLN A CG 1092 C CD . GLN A 138 ? 1.1712 1.7331 1.1857 0.3032 0.2252 -0.2487 138 GLN A CD 1093 O OE1 . GLN A 138 ? 1.2094 1.7580 1.2037 0.3202 0.2458 -0.2653 138 GLN A OE1 1094 N NE2 . GLN A 138 ? 1.1388 1.7645 1.1960 0.2951 0.2263 -0.2330 138 GLN A NE2 1095 N N . GLY A 139 ? 1.2854 1.5453 1.1350 0.2731 0.1352 -0.2755 139 GLY A N 1096 C CA . GLY A 139 ? 1.3400 1.5266 1.1397 0.2749 0.1255 -0.2929 139 GLY A CA 1097 C C . GLY A 139 ? 1.3573 1.5191 1.0992 0.2596 0.1306 -0.3068 139 GLY A C 1098 O O . GLY A 139 ? 1.3950 1.4947 1.0906 0.2573 0.1194 -0.3208 139 GLY A O 1099 N N . LYS A 140 ? 1.3202 1.5286 1.0632 0.2478 0.1462 -0.3023 140 LYS A N 1100 C CA . LYS A 140 ? 1.3565 1.5475 1.0454 0.2342 0.1546 -0.3138 140 LYS A CA 1101 C C . LYS A 140 ? 1.3066 1.5120 0.9955 0.2051 0.1395 -0.2978 140 LYS A C 1102 O O . LYS A 140 ? 1.2439 1.4894 0.9781 0.1977 0.1328 -0.2795 140 LYS A O 1103 C CB . LYS A 140 ? 1.3711 1.6032 1.0580 0.2461 0.1899 -0.3228 140 LYS A CB 1104 C CG . LYS A 140 ? 1.4215 1.6480 1.1144 0.2783 0.2097 -0.3379 140 LYS A CG 1105 C CD . LYS A 140 ? 1.4061 1.7018 1.1351 0.2908 0.2409 -0.3351 140 LYS A CD 1106 C CE . LYS A 140 ? 1.4355 1.7340 1.1870 0.3257 0.2582 -0.3451 140 LYS A CE 1107 N NZ . LYS A 140 ? 1.5139 1.7587 1.2085 0.3418 0.2738 -0.3710 140 LYS A NZ 1108 N N . SER A 141 ? 1.3460 1.5178 0.9824 0.1894 0.1346 -0.3049 141 SER A N 1109 C CA . SER A 141 ? 1.3155 1.4958 0.9477 0.1630 0.1207 -0.2903 141 SER A CA 1110 C C . SER A 141 ? 1.2745 1.5128 0.9242 0.1555 0.1423 -0.2823 141 SER A C 1111 O O . SER A 141 ? 1.2981 1.5501 0.9269 0.1612 0.1675 -0.2929 141 SER A O 1112 C CB . SER A 141 ? 1.3719 1.4980 0.9411 0.1494 0.1081 -0.2996 141 SER A CB 1113 O OG . SER A 141 ? 1.4156 1.4882 0.9715 0.1508 0.0828 -0.3043 141 SER A OG 1114 N N . SER A 142 ? 1.2188 1.4898 0.9060 0.1421 0.1327 -0.2636 142 SER A N 1115 C CA . SER A 142 ? 1.1824 1.5070 0.8905 0.1329 0.1498 -0.2548 142 SER A CA 1116 C C . SER A 142 ? 1.1510 1.4738 0.8570 0.1092 0.1338 -0.2402 142 SER A C 1117 O O . SER A 142 ? 1.1616 1.4418 0.8402 0.1000 0.1139 -0.2393 142 SER A O 1118 C CB . SER A 142 ? 1.1495 1.5242 0.9145 0.1453 0.1578 -0.2474 142 SER A CB 1119 O OG . SER A 142 ? 1.1303 1.5569 0.9150 0.1360 0.1742 -0.2404 142 SER A OG 1120 N N . PHE A 143 ? 1.1059 1.4737 0.8405 0.0993 0.1421 -0.2288 143 PHE A N 1121 C CA . PHE A 143 ? 1.0814 1.4483 0.8157 0.0787 0.1298 -0.2153 143 PHE A CA 1122 C C . PHE A 143 ? 1.0496 1.4669 0.8229 0.0719 0.1386 -0.2045 143 PHE A C 1123 O O . PHE A 143 ? 1.0474 1.5034 0.8431 0.0801 0.1557 -0.2075 143 PHE A O 1124 C CB . PHE A 143 ? 1.1133 1.4570 0.7988 0.0652 0.1344 -0.2190 143 PHE A CB 1125 C CG . PHE A 143 ? 1.0951 1.4203 0.7728 0.0472 0.1159 -0.2060 143 PHE A CG 1126 C CD1 . PHE A 143 ? 1.0845 1.3753 0.7606 0.0460 0.0901 -0.2010 143 PHE A CD1 1127 C CD2 . PHE A 143 ? 1.0734 1.4151 0.7464 0.0316 0.1243 -0.1982 143 PHE A CD2 1128 C CE1 . PHE A 143 ? 1.0755 1.3524 0.7484 0.0312 0.0738 -0.1880 143 PHE A CE1 1129 C CE2 . PHE A 143 ? 1.0641 1.3874 0.7312 0.0174 0.1081 -0.1859 143 PHE A CE2 1130 C CZ . PHE A 143 ? 1.0590 1.3518 0.7274 0.0181 0.0832 -0.1806 143 PHE A CZ 1131 N N . PHE A 144 ? 1.0341 1.4503 0.8156 0.0571 0.1263 -0.1918 144 PHE A N 1132 C CA . PHE A 144 ? 0.9991 1.4553 0.8086 0.0473 0.1336 -0.1826 144 PHE A CA 1133 C C . PHE A 144 ? 1.0036 1.4905 0.8068 0.0432 0.1573 -0.1886 144 PHE A C 1134 O O . PHE A 144 ? 1.0682 1.5400 0.8371 0.0338 0.1651 -0.1920 144 PHE A O 1135 C CB . PHE A 144 ? 0.9968 1.4370 0.7990 0.0305 0.1220 -0.1717 144 PHE A CB 1136 C CG . PHE A 144 ? 0.9937 1.4109 0.8084 0.0327 0.0998 -0.1629 144 PHE A CG 1137 C CD1 . PHE A 144 ? 0.9608 1.3988 0.8134 0.0388 0.0941 -0.1556 144 PHE A CD1 1138 C CD2 . PHE A 144 ? 1.0304 1.4066 0.8195 0.0277 0.0842 -0.1607 144 PHE A CD2 1139 C CE1 . PHE A 144 ? 0.9565 1.3759 0.8224 0.0399 0.0753 -0.1461 144 PHE A CE1 1140 C CE2 . PHE A 144 ? 1.0219 1.3809 0.8269 0.0285 0.0638 -0.1511 144 PHE A CE2 1141 C CZ . PHE A 144 ? 0.9808 1.3618 0.8249 0.0346 0.0603 -0.1436 144 PHE A CZ 1142 N N . ARG A 145 ? 0.9704 1.5016 0.8077 0.0496 0.1681 -0.1884 145 ARG A N 1143 C CA . ARG A 145 ? 0.9631 1.5296 0.8021 0.0482 0.1911 -0.1937 145 ARG A CA 1144 C C . ARG A 145 ? 0.9801 1.5605 0.8100 0.0258 0.1999 -0.1885 145 ARG A C 1145 O O . ARG A 145 ? 1.0420 1.6430 0.8639 0.0213 0.2190 -0.1925 145 ARG A O 1146 C CB . ARG A 145 ? 0.9119 1.5258 0.7955 0.0603 0.1971 -0.1924 145 ARG A CB 1147 C CG . ARG A 145 ? 0.9108 1.5141 0.8065 0.0842 0.1915 -0.1973 145 ARG A CG 1148 C CD . ARG A 145 ? 0.9039 1.5578 0.8378 0.0976 0.2046 -0.1977 145 ARG A CD 1149 N NE . ARG A 145 ? 0.9247 1.5699 0.8748 0.1219 0.1992 -0.2008 145 ARG A NE 1150 C CZ . ARG A 145 ? 0.9746 1.5934 0.9049 0.1393 0.2068 -0.2132 145 ARG A CZ 1151 N NH1 . ARG A 145 ? 1.0096 1.6077 0.8999 0.1352 0.2201 -0.2237 145 ARG A NH1 1152 N NH2 . ARG A 145 ? 0.9946 1.6046 0.9428 0.1612 0.2009 -0.2149 145 ARG A NH2 1153 N N . ASN A 146 ? 0.9949 1.5643 0.8268 0.0121 0.1871 -0.1793 146 ASN A N 1154 C CA . ASN A 146 ? 0.9961 1.5775 0.8230 -0.0091 0.1944 -0.1740 146 ASN A CA 1155 C C . ASN A 146 ? 1.0262 1.5677 0.8114 -0.0214 0.1931 -0.1725 146 ASN A C 1156 O O . ASN A 146 ? 1.0293 1.5748 0.8045 -0.0390 0.2008 -0.1684 146 ASN A O 1157 C CB . ASN A 146 ? 0.9603 1.5548 0.8138 -0.0166 0.1839 -0.1656 146 ASN A CB 1158 C CG . ASN A 146 ? 0.9447 1.5834 0.8376 -0.0079 0.1855 -0.1653 146 ASN A CG 1159 O OD1 . ASN A 146 ? 0.9860 1.6586 0.8918 -0.0038 0.1992 -0.1696 146 ASN A OD1 1160 N ND2 . ASN A 146 ? 0.9369 1.5771 0.8498 -0.0049 0.1719 -0.1592 146 ASN A ND2 1161 N N . VAL A 147 ? 1.0455 1.5475 0.8057 -0.0129 0.1822 -0.1752 147 VAL A N 1162 C CA . VAL A 147 ? 1.0785 1.5411 0.7966 -0.0232 0.1783 -0.1729 147 VAL A CA 1163 C C . VAL A 147 ? 1.1063 1.5468 0.7896 -0.0136 0.1831 -0.1832 147 VAL A C 1164 O O . VAL A 147 ? 1.1128 1.5557 0.8050 0.0034 0.1825 -0.1915 147 VAL A O 1165 C CB . VAL A 147 ? 1.0898 1.5203 0.8076 -0.0264 0.1558 -0.1635 147 VAL A CB 1166 C CG1 . VAL A 147 ? 1.0581 1.5061 0.8020 -0.0369 0.1549 -0.1546 147 VAL A CG1 1167 C CG2 . VAL A 147 ? 1.0885 1.5068 0.8210 -0.0106 0.1395 -0.1653 147 VAL A CG2 1168 N N . VAL A 148 ? 1.1444 1.5614 0.7859 -0.0246 0.1879 -0.1825 148 VAL A N 1169 C CA . VAL A 148 ? 1.1791 1.5760 0.7794 -0.0179 0.1966 -0.1930 148 VAL A CA 1170 C C . VAL A 148 ? 1.2115 1.5560 0.7716 -0.0214 0.1758 -0.1906 148 VAL A C 1171 O O . VAL A 148 ? 1.2430 1.5695 0.7835 -0.0365 0.1695 -0.1803 148 VAL A O 1172 C CB . VAL A 148 ? 1.2061 1.6214 0.7856 -0.0290 0.2218 -0.1937 148 VAL A CB 1173 C CG1 . VAL A 148 ? 1.2746 1.6722 0.8105 -0.0201 0.2346 -0.2060 148 VAL A CG1 1174 C CG2 . VAL A 148 ? 1.1746 1.6456 0.7985 -0.0296 0.2398 -0.1932 148 VAL A CG2 1175 N N . TRP A 149 ? 1.2268 1.5461 0.7753 -0.0077 0.1641 -0.1995 149 TRP A N 1176 C CA . TRP A 149 ? 1.2721 1.5418 0.7815 -0.0113 0.1422 -0.1982 149 TRP A CA 1177 C C . TRP A 149 ? 1.3428 1.5900 0.7926 -0.0153 0.1545 -0.2061 149 TRP A C 1178 O O . TRP A 149 ? 1.3831 1.6214 0.8105 -0.0029 0.1641 -0.2214 149 TRP A O 1179 C CB . TRP A 149 ? 1.2675 1.5176 0.7879 0.0029 0.1238 -0.2048 149 TRP A CB 1180 C CG . TRP A 149 ? 1.2976 1.4992 0.7856 -0.0022 0.0967 -0.2022 149 TRP A CG 1181 C CD1 . TRP A 149 ? 1.3288 1.5025 0.7762 -0.0163 0.0870 -0.1950 149 TRP A CD1 1182 C CD2 . TRP A 149 ? 1.3028 1.4786 0.7971 0.0059 0.0742 -0.2057 149 TRP A CD2 1183 N NE1 . TRP A 149 ? 1.3562 1.4908 0.7858 -0.0176 0.0589 -0.1937 149 TRP A NE1 1184 C CE2 . TRP A 149 ? 1.3343 1.4690 0.7922 -0.0049 0.0507 -0.2005 149 TRP A CE2 1185 C CE3 . TRP A 149 ? 1.2928 1.4758 0.8205 0.0204 0.0707 -0.2115 149 TRP A CE3 1186 C CZ2 . TRP A 149 ? 1.3477 1.4497 0.8029 -0.0030 0.0236 -0.2015 149 TRP A CZ2 1187 C CZ3 . TRP A 149 ? 1.3154 1.4633 0.8392 0.0226 0.0449 -0.2124 149 TRP A CZ3 1188 C CH2 . TRP A 149 ? 1.3375 1.4460 0.8259 0.0102 0.0215 -0.2077 149 TRP A CH2 1189 N N . LEU A 150 ? 1.3720 1.6085 0.7947 -0.0321 0.1547 -0.1955 150 LEU A N 1190 C CA . LEU A 150 ? 1.4339 1.6515 0.7980 -0.0385 0.1681 -0.2002 150 LEU A CA 1191 C C . LEU A 150 ? 1.4804 1.6454 0.7940 -0.0398 0.1448 -0.2025 150 LEU A C 1192 O O . LEU A 150 ? 1.4601 1.6040 0.7812 -0.0457 0.1171 -0.1912 150 LEU A O 1193 C CB . LEU A 150 ? 1.4484 1.6762 0.8044 -0.0573 0.1782 -0.1858 150 LEU A CB 1194 C CG . LEU A 150 ? 1.4172 1.6952 0.8165 -0.0611 0.2012 -0.1827 150 LEU A CG 1195 C CD1 . LEU A 150 ? 1.4286 1.7058 0.8203 -0.0818 0.2039 -0.1666 150 LEU A CD1 1196 C CD2 . LEU A 150 ? 1.4305 1.7375 0.8246 -0.0527 0.2314 -0.1958 150 LEU A CD2 1197 N N . ILE A 151 ? 1.5316 1.6764 0.7939 -0.0344 0.1563 -0.2171 151 ILE A N 1198 C CA . ILE A 151 ? 1.5866 1.6786 0.7888 -0.0380 0.1357 -0.2210 151 ILE A CA 1199 C C . ILE A 151 ? 1.6387 1.7157 0.7744 -0.0459 0.1546 -0.2247 151 ILE A C 1200 O O . ILE A 151 ? 1.6243 1.7331 0.7626 -0.0464 0.1859 -0.2260 151 ILE A O 1201 C CB . ILE A 151 ? 1.6111 1.6791 0.8074 -0.0218 0.1249 -0.2391 151 ILE A CB 1202 C CG1 . ILE A 151 ? 1.6502 1.7304 0.8310 -0.0057 0.1569 -0.2596 151 ILE A CG1 1203 C CG2 . ILE A 151 ? 1.5463 1.6301 0.8080 -0.0145 0.1076 -0.2340 151 ILE A CG2 1204 C CD1 . ILE A 151 ? 1.6832 1.7314 0.8489 0.0108 0.1479 -0.2791 151 ILE A CD1 1205 N N . LYS A 152 ? 1.7053 1.7342 0.7811 -0.0528 0.1346 -0.2255 152 LYS A N 1206 C CA . LYS A 152 ? 1.7852 1.7927 0.7885 -0.0617 0.1486 -0.2276 152 LYS A CA 1207 C C . LYS A 152 ? 1.8409 1.8591 0.8174 -0.0482 0.1846 -0.2486 152 LYS A C 1208 O O . LYS A 152 ? 1.8362 1.8563 0.8293 -0.0299 0.1895 -0.2665 152 LYS A O 1209 C CB . LYS A 152 ? 1.8392 1.7902 0.7824 -0.0695 0.1163 -0.2274 152 LYS A CB 1210 C CG . LYS A 152 ? 1.8684 1.7874 0.7899 -0.0558 0.1048 -0.2496 152 LYS A CG 1211 C CD . LYS A 152 ? 1.9252 1.7894 0.7894 -0.0670 0.0688 -0.2474 152 LYS A CD 1212 C CE . LYS A 152 ? 1.9788 1.8028 0.8001 -0.0560 0.0625 -0.2729 152 LYS A CE 1213 N NZ . LYS A 152 ? 2.0369 1.8082 0.8059 -0.0696 0.0226 -0.2697 152 LYS A NZ 1214 N N . LYS A 153 ? 1.8997 1.9240 0.8347 -0.0569 0.2101 -0.2457 153 LYS A N 1215 C CA . LYS A 153 ? 1.9549 1.9896 0.8588 -0.0448 0.2472 -0.2641 153 LYS A CA 1216 C C . LYS A 153 ? 2.0416 2.0317 0.8520 -0.0528 0.2496 -0.2690 153 LYS A C 1217 O O . LYS A 153 ? 2.0462 2.0279 0.8249 -0.0721 0.2467 -0.2515 153 LYS A O 1218 C CB . LYS A 153 ? 1.9279 2.0215 0.8734 -0.0471 0.2829 -0.2564 153 LYS A CB 1219 C CG . LYS A 153 ? 1.9552 2.0750 0.8992 -0.0281 0.3216 -0.2757 153 LYS A CG 1220 C CD . LYS A 153 ? 1.9099 2.0966 0.9181 -0.0285 0.3505 -0.2675 153 LYS A CD 1221 C CE . LYS A 153 ? 1.9306 2.1342 0.9105 -0.0474 0.3751 -0.2540 153 LYS A CE 1222 N NZ . LYS A 153 ? 1.9918 2.1999 0.9256 -0.0373 0.4120 -0.2684 153 LYS A NZ 1223 N N . ASN A 154 ? 2.1107 2.0702 0.8760 -0.0377 0.2550 -0.2930 154 ASN A N 1224 C CA . ASN A 154 ? 2.2210 2.1311 0.8896 -0.0433 0.2553 -0.3020 154 ASN A CA 1225 C C . ASN A 154 ? 2.2423 2.1086 0.8726 -0.0641 0.2131 -0.2856 154 ASN A C 1226 O O . ASN A 154 ? 2.2982 2.1421 0.8626 -0.0790 0.2145 -0.2773 154 ASN A O 1227 C CB . ASN A 154 ? 2.2641 2.1977 0.8970 -0.0472 0.2985 -0.3005 154 ASN A CB 1228 C CG . ASN A 154 ? 2.3911 2.2773 0.9231 -0.0459 0.3086 -0.3171 154 ASN A CG 1229 O OD1 . ASN A 154 ? 2.4474 2.2845 0.9378 -0.0384 0.2876 -0.3350 154 ASN A OD1 1230 N ND2 . ASN A 154 ? 2.4464 2.3461 0.9365 -0.0542 0.3412 -0.3111 154 ASN A ND2 1231 N N . SER A 155 ? 2.1926 2.0488 0.8661 -0.0647 0.1757 -0.2799 155 SER A N 1232 C CA . SER A 155 ? 2.2031 2.0244 0.8562 -0.0826 0.1326 -0.2623 155 SER A CA 1233 C C . SER A 155 ? 2.1719 2.0129 0.8351 -0.1012 0.1331 -0.2337 155 SER A C 1234 O O . SER A 155 ? 2.2581 2.0685 0.8610 -0.1168 0.1201 -0.2220 155 SER A O 1235 C CB . SER A 155 ? 2.3043 2.0648 0.8623 -0.0877 0.1157 -0.2748 155 SER A CB 1236 O OG . SER A 155 ? 2.3324 2.0696 0.8753 -0.0704 0.1178 -0.3032 155 SER A OG 1237 N N . THR A 156 ? 2.0810 1.9710 0.8182 -0.0999 0.1478 -0.2223 156 THR A N 1238 C CA . THR A 156 ? 2.0457 1.9523 0.8007 -0.1170 0.1464 -0.1954 156 THR A CA 1239 C C . THR A 156 ? 1.9550 1.9076 0.8011 -0.1130 0.1506 -0.1868 156 THR A C 1240 O O . THR A 156 ? 1.9546 1.9446 0.8400 -0.1008 0.1774 -0.1990 156 THR A O 1241 C CB . THR A 156 ? 2.0724 1.9905 0.7837 -0.1262 0.1820 -0.1910 156 THR A CB 1242 O OG1 . THR A 156 ? 2.1665 2.0461 0.7903 -0.1263 0.1865 -0.2042 156 THR A OG1 1243 C CG2 . THR A 156 ? 2.0597 1.9776 0.7719 -0.1466 0.1732 -0.1619 156 THR A CG2 1244 N N . TYR A 157 ? 1.9111 1.8608 0.7899 -0.1227 0.1240 -0.1658 157 TYR A N 1245 C CA . TYR A 157 ? 1.8118 1.8015 0.7685 -0.1221 0.1287 -0.1553 157 TYR A CA 1246 C C . TYR A 157 ? 1.8094 1.7995 0.7608 -0.1401 0.1304 -0.1313 157 TYR A C 1247 O O . TYR A 157 ? 1.7878 1.7560 0.7421 -0.1478 0.1016 -0.1136 157 TYR A O 1248 C CB . TYR A 157 ? 1.7595 1.7459 0.7673 -0.1147 0.0972 -0.1529 157 TYR A CB 1249 C CG . TYR A 157 ? 1.6785 1.7086 0.7659 -0.1082 0.1067 -0.1506 157 TYR A CG 1250 C CD1 . TYR A 157 ? 1.6413 1.6912 0.7601 -0.1187 0.1130 -0.1331 157 TYR A CD1 1251 C CD2 . TYR A 157 ? 1.6354 1.6843 0.7636 -0.0921 0.1089 -0.1660 157 TYR A CD2 1252 C CE1 . TYR A 157 ? 1.5864 1.6734 0.7721 -0.1137 0.1208 -0.1321 157 TYR A CE1 1253 C CE2 . TYR A 157 ? 1.5696 1.6575 0.7659 -0.0869 0.1165 -0.1633 157 TYR A CE2 1254 C CZ . TYR A 157 ? 1.5451 1.6522 0.7688 -0.0980 0.1223 -0.1470 157 TYR A CZ 1255 O OH . TYR A 157 ? 1.4589 1.6026 0.7454 -0.0937 0.1291 -0.1454 157 TYR A OH 1256 N N . PRO A 158 ? 1.8223 1.8369 0.7661 -0.1469 0.1641 -0.1298 158 PRO A N 1257 C CA . PRO A 158 ? 1.8273 1.8407 0.7673 -0.1650 0.1668 -0.1068 158 PRO A CA 1258 C C . PRO A 158 ? 1.7471 1.7850 0.7601 -0.1661 0.1611 -0.0960 158 PRO A C 1259 O O . PRO A 158 ? 1.6897 1.7571 0.7563 -0.1539 0.1653 -0.1077 158 PRO A O 1260 C CB . PRO A 158 ? 1.8548 1.8911 0.7692 -0.1714 0.2067 -0.1108 158 PRO A CB 1261 C CG . PRO A 158 ? 1.8292 1.8987 0.7720 -0.1539 0.2276 -0.1343 158 PRO A CG 1262 C CD . PRO A 158 ? 1.8336 1.8776 0.7723 -0.1387 0.2010 -0.1480 158 PRO A CD 1263 N N . THR A 159 ? 1.7526 1.7759 0.7649 -0.1801 0.1513 -0.0739 159 THR A N 1264 C CA . THR A 159 ? 1.6888 1.7280 0.7633 -0.1815 0.1452 -0.0634 159 THR A CA 1265 C C . THR A 159 ? 1.6610 1.7463 0.7782 -0.1822 0.1758 -0.0721 159 THR A C 1266 O O . THR A 159 ? 1.6841 1.7832 0.7801 -0.1927 0.2023 -0.0715 159 THR A O 1267 C CB . THR A 159 ? 1.7057 1.7180 0.7654 -0.1969 0.1341 -0.0382 159 THR A CB 1268 O OG1 . THR A 159 ? 1.7383 1.7096 0.7541 -0.1976 0.1056 -0.0282 159 THR A OG1 1269 C CG2 . THR A 159 ? 1.6501 1.6719 0.7717 -0.1955 0.1251 -0.0290 159 THR A CG2 1270 N N . ILE A 160 ? 1.6150 1.7250 0.7921 -0.1714 0.1713 -0.0794 160 ILE A N 1271 C CA . ILE A 160 ? 1.5797 1.7344 0.8033 -0.1723 0.1951 -0.0863 160 ILE A CA 1272 C C . ILE A 160 ? 1.5825 1.7365 0.8310 -0.1865 0.1947 -0.0704 160 ILE A C 1273 O O . ILE A 160 ? 1.5757 1.7053 0.8355 -0.1857 0.1721 -0.0592 160 ILE A O 1274 C CB . ILE A 160 ? 1.5198 1.6999 0.7933 -0.1541 0.1895 -0.1011 160 ILE A CB 1275 C CG1 . ILE A 160 ? 1.5452 1.7267 0.7952 -0.1398 0.1943 -0.1189 160 ILE A CG1 1276 C CG2 . ILE A 160 ? 1.4711 1.6961 0.7959 -0.1565 0.2085 -0.1050 160 ILE A CG2 1277 C CD1 . ILE A 160 ? 1.5035 1.6950 0.7921 -0.1215 0.1811 -0.1308 160 ILE A CD1 1278 N N . LYS A 161 ? 1.6045 1.7848 0.8617 -0.1996 0.2198 -0.0692 161 LYS A N 1279 C CA . LYS A 161 ? 1.6041 1.7846 0.8866 -0.2143 0.2218 -0.0569 161 LYS A CA 1280 C C . LYS A 161 ? 1.5802 1.8093 0.9025 -0.2194 0.2449 -0.0661 161 LYS A C 1281 O O . LYS A 161 ? 1.6058 1.8539 0.9145 -0.2326 0.2681 -0.0648 161 LYS A O 1282 C CB . LYS A 161 ? 1.6799 1.8292 0.9180 -0.2335 0.2253 -0.0386 161 LYS A CB 1283 C CG . LYS A 161 ? 1.7327 1.8328 0.9388 -0.2310 0.1985 -0.0245 161 LYS A CG 1284 C CD . LYS A 161 ? 1.8060 1.8761 0.9627 -0.2497 0.2034 -0.0057 161 LYS A CD 1285 C CE . LYS A 161 ? 1.8522 1.8749 0.9767 -0.2467 0.1746 0.0099 161 LYS A CE 1286 N NZ . LYS A 161 ? 1.9326 1.9264 0.9974 -0.2629 0.1790 0.0269 161 LYS A NZ 1287 N N . ARG A 162 ? 1.5355 1.7861 0.9072 -0.2095 0.2382 -0.0743 162 ARG A N 1288 C CA . ARG A 162 ? 1.5114 1.8100 0.9237 -0.2131 0.2560 -0.0832 162 ARG A CA 1289 C C . ARG A 162 ? 1.4858 1.7852 0.9332 -0.2222 0.2500 -0.0784 162 ARG A C 1290 O O . ARG A 162 ? 1.4832 1.7570 0.9407 -0.2147 0.2304 -0.0748 162 ARG A O 1291 C CB . ARG A 162 ? 1.4867 1.8162 0.9255 -0.1919 0.2560 -0.0996 162 ARG A CB 1292 C CG . ARG A 162 ? 1.5315 1.8790 0.9471 -0.1851 0.2740 -0.1088 162 ARG A CG 1293 C CD . ARG A 162 ? 1.5534 1.9388 0.9748 -0.2006 0.3023 -0.1074 162 ARG A CD 1294 N NE . ARG A 162 ? 1.5353 1.9678 0.9826 -0.1871 0.3190 -0.1212 162 ARG A NE 1295 C CZ . ARG A 162 ? 1.5559 1.9888 0.9801 -0.1707 0.3271 -0.1317 162 ARG A CZ 1296 N NH1 . ARG A 162 ? 1.6050 1.9936 0.9762 -0.1672 0.3189 -0.1308 162 ARG A NH1 1297 N NH2 . ARG A 162 ? 1.5414 2.0185 0.9952 -0.1573 0.3429 -0.1434 162 ARG A NH2 1298 N N . SER A 163 ? 1.4538 1.7837 0.9200 -0.2385 0.2674 -0.0787 163 SER A N 1299 C CA . SER A 163 ? 1.4086 1.7395 0.9041 -0.2500 0.2638 -0.0763 163 SER A CA 1300 C C . SER A 163 ? 1.3661 1.7516 0.9029 -0.2529 0.2759 -0.0869 163 SER A C 1301 O O . SER A 163 ? 1.3726 1.7935 0.9108 -0.2591 0.2946 -0.0892 163 SER A O 1302 C CB . SER A 163 ? 1.4437 1.7463 0.9148 -0.2745 0.2696 -0.0619 163 SER A CB 1303 O OG . SER A 163 ? 1.4586 1.7570 0.9544 -0.2864 0.2662 -0.0610 163 SER A OG 1304 N N . TYR A 164 ? 1.3309 1.7248 0.9016 -0.2476 0.2654 -0.0926 164 TYR A N 1305 C CA . TYR A 164 ? 1.2941 1.7369 0.9033 -0.2538 0.2737 -0.1004 164 TYR A CA 1306 C C . TYR A 164 ? 1.3034 1.7330 0.9246 -0.2713 0.2685 -0.0979 164 TYR A C 1307 O O . TYR A 164 ? 1.2905 1.6835 0.9082 -0.2653 0.2542 -0.0962 164 TYR A O 1308 C CB . TYR A 164 ? 1.2357 1.7082 0.8750 -0.2305 0.2669 -0.1117 164 TYR A CB 1309 C CG . TYR A 164 ? 1.2095 1.7288 0.8890 -0.2370 0.2709 -0.1178 164 TYR A CG 1310 C CD1 . TYR A 164 ? 1.2185 1.7871 0.9151 -0.2451 0.2878 -0.1197 164 TYR A CD1 1311 C CD2 . TYR A 164 ? 1.1957 1.7107 0.8956 -0.2358 0.2579 -0.1209 164 TYR A CD2 1312 C CE1 . TYR A 164 ? 1.1970 1.8107 0.9319 -0.2522 0.2890 -0.1239 164 TYR A CE1 1313 C CE2 . TYR A 164 ? 1.1748 1.7314 0.9077 -0.2432 0.2595 -0.1261 164 TYR A CE2 1314 C CZ . TYR A 164 ? 1.1798 1.7860 0.9308 -0.2519 0.2738 -0.1272 164 TYR A CZ 1315 O OH . TYR A 164 ? 1.1638 1.8133 0.9492 -0.2600 0.2728 -0.1310 164 TYR A OH 1316 N N . ASN A 165 ? 1.3292 1.7896 0.9653 -0.2929 0.2805 -0.0979 165 ASN A N 1317 C CA . ASN A 165 ? 1.3658 1.8140 1.0099 -0.3138 0.2770 -0.0968 165 ASN A CA 1318 C C . ASN A 165 ? 1.3156 1.8092 0.9991 -0.3127 0.2741 -0.1073 165 ASN A C 1319 O O . ASN A 165 ? 1.3060 1.8522 1.0122 -0.3153 0.2842 -0.1102 165 ASN A O 1320 C CB . ASN A 165 ? 1.4509 1.8982 1.0805 -0.3431 0.2912 -0.0873 165 ASN A CB 1321 C CG . ASN A 165 ? 1.5191 1.9533 1.1557 -0.3686 0.2882 -0.0869 165 ASN A CG 1322 O OD1 . ASN A 165 ? 1.4553 1.9141 1.1194 -0.3709 0.2826 -0.0961 165 ASN A OD1 1323 N ND2 . ASN A 165 ? 1.6627 2.0556 1.2716 -0.3889 0.2917 -0.0758 165 ASN A ND2 1324 N N . ASN A 166 ? 1.2817 1.7557 0.9729 -0.3080 0.2608 -0.1124 166 ASN A N 1325 C CA . ASN A 166 ? 1.2331 1.7459 0.9569 -0.3077 0.2559 -0.1218 166 ASN A CA 1326 C C . ASN A 166 ? 1.2489 1.7818 0.9825 -0.3388 0.2613 -0.1218 166 ASN A C 1327 O O . ASN A 166 ? 1.2579 1.7578 0.9807 -0.3548 0.2559 -0.1229 166 ASN A O 1328 C CB . ASN A 166 ? 1.1979 1.6818 0.9226 -0.2936 0.2414 -0.1270 166 ASN A CB 1329 C CG . ASN A 166 ? 1.1642 1.6891 0.9193 -0.2890 0.2354 -0.1359 166 ASN A CG 1330 O OD1 . ASN A 166 ? 1.1360 1.7135 0.9151 -0.2913 0.2403 -0.1378 166 ASN A OD1 1331 N ND2 . ASN A 166 ? 1.1494 1.6513 0.9037 -0.2819 0.2251 -0.1407 166 ASN A ND2 1332 N N . THR A 167 ? 1.2368 1.8240 0.9917 -0.3469 0.2722 -0.1207 167 THR A N 1333 C CA . THR A 167 ? 1.2670 1.8844 1.0381 -0.3776 0.2770 -0.1195 167 THR A CA 1334 C C . THR A 167 ? 1.2580 1.9180 1.0626 -0.3780 0.2671 -0.1280 167 THR A C 1335 O O . THR A 167 ? 1.2833 1.9708 1.1042 -0.4040 0.2670 -0.1278 167 THR A O 1336 C CB . THR A 167 ? 1.2744 1.9338 1.0550 -0.3879 0.2953 -0.1118 167 THR A CB 1337 O OG1 . THR A 167 ? 1.2414 1.9489 1.0465 -0.3630 0.3001 -0.1153 167 THR A OG1 1338 C CG2 . THR A 167 ? 1.2954 1.9113 1.0379 -0.3917 0.3051 -0.1021 167 THR A CG2 1339 N N . ASN A 168 ? 1.2242 1.8893 1.0385 -0.3505 0.2577 -0.1343 168 ASN A N 1340 C CA . ASN A 168 ? 1.1748 1.8754 1.0163 -0.3486 0.2465 -0.1412 168 ASN A CA 1341 C C . ASN A 168 ? 1.1866 1.8478 1.0112 -0.3630 0.2350 -0.1470 168 ASN A C 1342 O O . ASN A 168 ? 1.2277 1.8302 1.0215 -0.3647 0.2346 -0.1463 168 ASN A O 1343 C CB . ASN A 168 ? 1.1421 1.8552 0.9963 -0.3146 0.2405 -0.1447 168 ASN A CB 1344 C CG . ASN A 168 ? 1.1298 1.8745 0.9967 -0.2970 0.2519 -0.1412 168 ASN A CG 1345 O OD1 . ASN A 168 ? 1.1302 1.9320 1.0287 -0.2975 0.2572 -0.1403 168 ASN A OD1 1346 N ND2 . ASN A 168 ? 1.1191 1.8264 0.9612 -0.2807 0.2555 -0.1393 168 ASN A ND2 1347 N N . GLN A 169 ? 1.1719 1.8648 1.0157 -0.3724 0.2254 -0.1526 169 GLN A N 1348 C CA . GLN A 169 ? 1.1951 1.8519 1.0204 -0.3844 0.2143 -0.1606 169 GLN A CA 1349 C C . GLN A 169 ? 1.1560 1.7838 0.9706 -0.3561 0.2069 -0.1655 169 GLN A C 1350 O O . GLN A 169 ? 1.1680 1.7476 0.9579 -0.3589 0.2024 -0.1711 169 GLN A O 1351 C CB . GLN A 169 ? 1.2154 1.9180 1.0625 -0.4050 0.2049 -0.1648 169 GLN A CB 1352 C CG . GLN A 169 ? 1.2463 1.9828 1.1091 -0.4360 0.2111 -0.1589 169 GLN A CG 1353 C CD . GLN A 169 ? 1.3148 1.9982 1.1475 -0.4565 0.2195 -0.1556 169 GLN A CD 1354 O OE1 . GLN A 169 ? 1.3631 1.9922 1.1665 -0.4687 0.2136 -0.1619 169 GLN A OE1 1355 N NE2 . GLN A 169 ? 1.3303 2.0262 1.1679 -0.4593 0.2340 -0.1455 169 GLN A NE2 1356 N N . GLU A 170 ? 1.1004 1.7571 0.9342 -0.3288 0.2066 -0.1631 170 GLU A N 1357 C CA . GLU A 170 ? 1.0533 1.6945 0.8847 -0.3025 0.1990 -0.1661 170 GLU A CA 1358 C C . GLU A 170 ? 1.0579 1.6511 0.8694 -0.2839 0.2029 -0.1622 170 GLU A C 1359 O O . GLU A 170 ? 1.0698 1.6570 0.8760 -0.2837 0.2111 -0.1563 170 GLU A O 1360 C CB . GLU A 170 ? 1.0026 1.6987 0.8664 -0.2835 0.1952 -0.1644 170 GLU A CB 1361 C CG . GLU A 170 ? 1.0010 1.7507 0.8891 -0.2995 0.1890 -0.1662 170 GLU A CG 1362 C CD . GLU A 170 ? 0.9945 1.7879 0.9040 -0.3162 0.1975 -0.1613 170 GLU A CD 1363 O OE1 . GLU A 170 ? 1.0043 1.7797 0.9023 -0.3219 0.2094 -0.1575 170 GLU A OE1 1364 O OE2 . GLU A 170 ? 0.9046 1.7525 0.8432 -0.3237 0.1923 -0.1601 170 GLU A OE2 1365 N N . ASP A 171 ? 1.0680 1.6281 0.8684 -0.2690 0.1969 -0.1649 171 ASP A N 1366 C CA . ASP A 171 ? 1.0595 1.5834 0.8494 -0.2473 0.1974 -0.1599 171 ASP A CA 1367 C C . ASP A 171 ? 1.0255 1.5821 0.8348 -0.2276 0.1975 -0.1555 171 ASP A C 1368 O O . ASP A 171 ? 0.9863 1.5879 0.8192 -0.2221 0.1944 -0.1574 171 ASP A O 1369 C CB . ASP A 171 ? 1.0865 1.5842 0.8711 -0.2322 0.1911 -0.1627 171 ASP A CB 1370 C CG . ASP A 171 ? 1.1485 1.6006 0.9085 -0.2462 0.1928 -0.1678 171 ASP A CG 1371 O OD1 . ASP A 171 ? 1.2213 1.6517 0.9655 -0.2664 0.1977 -0.1674 171 ASP A OD1 1372 O OD2 . ASP A 171 ? 1.1679 1.6038 0.9232 -0.2365 0.1899 -0.1719 171 ASP A OD2 1373 N N . LEU A 172 ? 1.0387 1.5709 0.8369 -0.2168 0.2001 -0.1498 172 LEU A N 1374 C CA . LEU A 172 ? 1.0426 1.5979 0.8529 -0.1991 0.2008 -0.1471 172 LEU A CA 1375 C C . LEU A 172 ? 1.0283 1.5547 0.8342 -0.1761 0.1930 -0.1434 172 LEU A C 1376 O O . LEU A 172 ? 1.0434 1.5270 0.8298 -0.1758 0.1916 -0.1390 172 LEU A O 1377 C CB . LEU A 172 ? 1.0810 1.6379 0.8793 -0.2092 0.2113 -0.1437 172 LEU A CB 1378 C CG . LEU A 172 ? 1.1042 1.6935 0.9150 -0.1946 0.2159 -0.1437 172 LEU A CG 1379 C CD1 . LEU A 172 ? 1.0992 1.7463 0.9400 -0.1991 0.2200 -0.1473 172 LEU A CD1 1380 C CD2 . LEU A 172 ? 1.1383 1.7118 0.9257 -0.1999 0.2260 -0.1395 172 LEU A CD2 1381 N N . LEU A 173 ? 0.9915 1.5418 0.8174 -0.1574 0.1873 -0.1441 173 LEU A N 1382 C CA . LEU A 173 ? 0.9879 1.5163 0.8135 -0.1367 0.1792 -0.1399 173 LEU A CA 1383 C C . LEU A 173 ? 1.0040 1.5289 0.8201 -0.1300 0.1816 -0.1382 173 LEU A C 1384 O O . LEU A 173 ? 1.0139 1.5711 0.8420 -0.1247 0.1857 -0.1416 173 LEU A O 1385 C CB . LEU A 173 ? 0.9727 1.5254 0.8227 -0.1208 0.1716 -0.1406 173 LEU A CB 1386 C CG . LEU A 173 ? 0.9678 1.5032 0.8223 -0.1002 0.1623 -0.1355 173 LEU A CG 1387 C CD1 . LEU A 173 ? 0.9768 1.4693 0.8174 -0.0990 0.1580 -0.1297 173 LEU A CD1 1388 C CD2 . LEU A 173 ? 0.9462 1.5063 0.8250 -0.0873 0.1556 -0.1349 173 LEU A CD2 1389 N N . VAL A 174 ? 1.0138 1.4990 0.8076 -0.1292 0.1789 -0.1329 174 VAL A N 1390 C CA . VAL A 174 ? 1.0069 1.4816 0.7838 -0.1238 0.1799 -0.1314 174 VAL A CA 1391 C C . VAL A 174 ? 0.9827 1.4366 0.7611 -0.1053 0.1662 -0.1277 174 VAL A C 1392 O O . VAL A 174 ? 0.9903 1.4190 0.7697 -0.1020 0.1575 -0.1217 174 VAL A O 1393 C CB . VAL A 174 ? 1.0399 1.4839 0.7864 -0.1390 0.1853 -0.1264 174 VAL A CB 1394 C CG1 . VAL A 174 ? 1.0751 1.5081 0.7988 -0.1341 0.1866 -0.1251 174 VAL A CG1 1395 C CG2 . VAL A 174 ? 1.0522 1.5145 0.7982 -0.1603 0.1981 -0.1288 174 VAL A CG2 1396 N N . LEU A 175 ? 0.9653 1.4294 0.7444 -0.0934 0.1647 -0.1312 175 LEU A N 1397 C CA . LEU A 175 ? 0.9614 1.4054 0.7407 -0.0778 0.1506 -0.1283 175 LEU A CA 1398 C C . LEU A 175 ? 0.9961 1.4170 0.7443 -0.0771 0.1496 -0.1287 175 LEU A C 1399 O O . LEU A 175 ? 1.0268 1.4614 0.7621 -0.0806 0.1620 -0.1348 175 LEU A O 1400 C CB . LEU A 175 ? 0.9421 1.4133 0.7475 -0.0630 0.1473 -0.1329 175 LEU A CB 1401 C CG . LEU A 175 ? 0.9263 1.4213 0.7613 -0.0613 0.1459 -0.1318 175 LEU A CG 1402 C CD1 . LEU A 175 ? 0.9246 1.4533 0.7825 -0.0497 0.1468 -0.1366 175 LEU A CD1 1403 C CD2 . LEU A 175 ? 0.9042 1.3770 0.7475 -0.0552 0.1333 -0.1236 175 LEU A CD2 1404 N N . TRP A 176 ? 1.0069 1.3939 0.7430 -0.0726 0.1350 -0.1218 176 TRP A N 1405 C CA . TRP A 176 ? 1.0360 1.3979 0.7398 -0.0709 0.1299 -0.1223 176 TRP A CA 1406 C C . TRP A 176 ? 1.0332 1.3715 0.7410 -0.0603 0.1087 -0.1169 176 TRP A C 1407 O O . TRP A 176 ? 0.9944 1.3395 0.7325 -0.0537 0.1005 -0.1125 176 TRP A O 1408 C CB . TRP A 176 ? 1.0791 1.4181 0.7500 -0.0858 0.1351 -0.1164 176 TRP A CB 1409 C CG . TRP A 176 ? 1.0907 1.4032 0.7631 -0.0902 0.1242 -0.1039 176 TRP A CG 1410 C CD1 . TRP A 176 ? 1.1126 1.3917 0.7694 -0.0880 0.1076 -0.0941 176 TRP A CD1 1411 C CD2 . TRP A 176 ? 1.0627 1.3794 0.7531 -0.0968 0.1293 -0.0998 176 TRP A CD2 1412 N NE1 . TRP A 176 ? 1.0988 1.3630 0.7665 -0.0912 0.1030 -0.0833 176 TRP A NE1 1413 C CE2 . TRP A 176 ? 1.0738 1.3582 0.7601 -0.0963 0.1169 -0.0876 176 TRP A CE2 1414 C CE3 . TRP A 176 ? 1.0367 1.3802 0.7454 -0.1033 0.1426 -0.1056 176 TRP A CE3 1415 C CZ2 . TRP A 176 ? 1.0679 1.3441 0.7670 -0.1002 0.1195 -0.0820 176 TRP A CZ2 1416 C CZ3 . TRP A 176 ? 1.0351 1.3686 0.7528 -0.1092 0.1437 -0.1009 176 TRP A CZ3 1417 C CH2 . TRP A 176 ? 1.0532 1.3521 0.7657 -0.1068 0.1333 -0.0897 176 TRP A CH2 1418 N N . GLY A 177 ? 1.0759 1.3872 0.7528 -0.0594 0.0997 -0.1169 177 GLY A N 1419 C CA . GLY A 177 ? 1.0774 1.3663 0.7576 -0.0515 0.0775 -0.1118 177 GLY A CA 1420 C C . GLY A 177 ? 1.1133 1.3660 0.7536 -0.0559 0.0643 -0.1080 177 GLY A C 1421 O O . GLY A 177 ? 1.1442 1.3869 0.7484 -0.0643 0.0738 -0.1102 177 GLY A O 1422 N N . ILE A 178 ? 1.1154 1.3494 0.7626 -0.0511 0.0417 -0.1014 178 ILE A N 1423 C CA . ILE A 178 ? 1.1593 1.3583 0.7710 -0.0555 0.0235 -0.0965 178 ILE A CA 1424 C C . ILE A 178 ? 1.1727 1.3611 0.7870 -0.0475 0.0062 -0.1022 178 ILE A C 1425 O O . ILE A 178 ? 1.1295 1.3315 0.7837 -0.0402 -0.0008 -0.0994 178 ILE A O 1426 C CB . ILE A 178 ? 1.1735 1.3568 0.7934 -0.0610 0.0086 -0.0776 178 ILE A CB 1427 C CG1 . ILE A 178 ? 1.2413 1.3898 0.8263 -0.0661 -0.0144 -0.0704 178 ILE A CG1 1428 C CG2 . ILE A 178 ? 1.1334 1.3314 0.8046 -0.0537 -0.0005 -0.0683 178 ILE A CG2 1429 C CD1 . ILE A 178 ? 1.2880 1.4163 0.8343 -0.0770 -0.0117 -0.0625 178 ILE A CD1 1430 N N . HIS A 179 ? 1.2177 1.3802 0.7876 -0.0493 -0.0002 -0.1104 179 HIS A N 1431 C CA . HIS A 179 ? 1.2365 1.3804 0.8016 -0.0437 -0.0188 -0.1167 179 HIS A CA 1432 C C . HIS A 179 ? 1.2629 1.3775 0.8179 -0.0510 -0.0493 -0.1033 179 HIS A C 1433 O O . HIS A 179 ? 1.3159 1.4089 0.8324 -0.0601 -0.0554 -0.0980 179 HIS A O 1434 C CB . HIS A 179 ? 1.2701 1.4000 0.7904 -0.0403 -0.0081 -0.1361 179 HIS A CB 1435 C CG . HIS A 179 ? 1.2871 1.3893 0.7938 -0.0358 -0.0281 -0.1443 179 HIS A CG 1436 N ND1 . HIS A 179 ? 1.3539 1.4193 0.8034 -0.0397 -0.0364 -0.1539 179 HIS A ND1 1437 C CD2 . HIS A 179 ? 1.2656 1.3687 0.8065 -0.0289 -0.0420 -0.1442 179 HIS A CD2 1438 C CE1 . HIS A 179 ? 1.3700 1.4134 0.8187 -0.0356 -0.0552 -0.1606 179 HIS A CE1 1439 N NE2 . HIS A 179 ? 1.3280 1.3940 0.8332 -0.0292 -0.0589 -0.1542 179 HIS A NE2 1440 N N . HIS A 180 ? 1.2352 1.3507 0.8261 -0.0474 -0.0688 -0.0965 180 HIS A N 1441 C CA . HIS A 180 ? 1.2594 1.3517 0.8490 -0.0543 -0.1002 -0.0830 180 HIS A CA 1442 C C . HIS A 180 ? 1.3164 1.3800 0.8776 -0.0545 -0.1170 -0.0957 180 HIS A C 1443 O O . HIS A 180 ? 1.3025 1.3722 0.8898 -0.0475 -0.1190 -0.1017 180 HIS A O 1444 C CB . HIS A 180 ? 1.2216 1.3352 0.8724 -0.0513 -0.1106 -0.0659 180 HIS A CB 1445 C CG . HIS A 180 ? 1.1936 1.3310 0.8715 -0.0501 -0.0947 -0.0545 180 HIS A CG 1446 N ND1 . HIS A 180 ? 1.2268 1.3538 0.8813 -0.0568 -0.0928 -0.0463 180 HIS A ND1 1447 C CD2 . HIS A 180 ? 1.1442 1.3121 0.8678 -0.0433 -0.0803 -0.0503 180 HIS A CD2 1448 C CE1 . HIS A 180 ? 1.1799 1.3280 0.8651 -0.0538 -0.0776 -0.0384 180 HIS A CE1 1449 N NE2 . HIS A 180 ? 1.1356 1.3089 0.8616 -0.0458 -0.0697 -0.0413 180 HIS A NE2 1450 N N . PRO A 181 ? 1.3773 1.4070 0.8822 -0.0628 -0.1292 -0.1000 181 PRO A N 1451 C CA . PRO A 181 ? 1.4343 1.4312 0.9033 -0.0633 -0.1435 -0.1154 181 PRO A CA 1452 C C . PRO A 181 ? 1.4421 1.4217 0.9299 -0.0701 -0.1801 -0.1046 181 PRO A C 1453 O O . PRO A 181 ? 1.3929 1.3844 0.9155 -0.0756 -0.1966 -0.0831 181 PRO A O 1454 C CB . PRO A 181 ? 1.5126 1.4804 0.9105 -0.0709 -0.1415 -0.1229 181 PRO A CB 1455 C CG . PRO A 181 ? 1.5013 1.4779 0.9051 -0.0792 -0.1455 -0.1019 181 PRO A CG 1456 C CD . PRO A 181 ? 1.4187 1.4364 0.8865 -0.0721 -0.1293 -0.0915 181 PRO A CD 1457 N N . LYS A 182 ? 1.4865 1.4377 0.9512 -0.0696 -0.1919 -0.1199 182 LYS A N 1458 C CA . LYS A 182 ? 1.5176 1.4488 0.9968 -0.0778 -0.2273 -0.1125 182 LYS A CA 1459 C C . LYS A 182 ? 1.5529 1.4597 1.0016 -0.0937 -0.2584 -0.0995 182 LYS A C 1460 O O . LYS A 182 ? 1.5347 1.4526 1.0245 -0.1009 -0.2825 -0.0777 182 LYS A O 1461 C CB . LYS A 182 ? 1.5779 1.4770 1.0289 -0.0736 -0.2303 -0.1353 182 LYS A CB 1462 C CG . LYS A 182 ? 1.6403 1.5109 1.0978 -0.0844 -0.2680 -0.1310 182 LYS A CG 1463 C CD . LYS A 182 ? 1.7256 1.5501 1.1314 -0.0823 -0.2712 -0.1574 182 LYS A CD 1464 C CE . LYS A 182 ? 1.7871 1.5745 1.1859 -0.0975 -0.3126 -0.1543 182 LYS A CE 1465 N NZ . LYS A 182 ? 1.7558 1.5633 1.2256 -0.0974 -0.3242 -0.1401 182 LYS A NZ 1466 N N . ASP A 183 ? 1.6029 1.4780 0.9802 -0.0988 -0.2575 -0.1120 183 ASP A N 1467 C CA . ASP A 183 ? 1.6495 1.4972 0.9873 -0.1146 -0.2883 -0.1010 183 ASP A CA 1468 C C . ASP A 183 ? 1.6677 1.5001 0.9388 -0.1173 -0.2729 -0.1073 183 ASP A C 1469 O O . ASP A 183 ? 1.6446 1.4862 0.8978 -0.1074 -0.2379 -0.1224 183 ASP A O 1470 C CB . ASP A 183 ? 1.7065 1.5123 1.0150 -0.1249 -0.3222 -0.1102 183 ASP A CB 1471 C CG . ASP A 183 ? 1.7498 1.5233 1.0062 -0.1176 -0.3063 -0.1420 183 ASP A CG 1472 O OD1 . ASP A 183 ? 1.7678 1.5357 0.9765 -0.1112 -0.2783 -0.1569 183 ASP A OD1 1473 O OD2 . ASP A 183 ? 1.7598 1.5124 1.0234 -0.1184 -0.3219 -0.1517 183 ASP A OD2 1474 N N . ALA A 184 ? 1.7065 1.5172 0.9424 -0.1312 -0.2998 -0.0943 184 ALA A N 1475 C CA . ALA A 184 ? 1.7517 1.5456 0.9216 -0.1363 -0.2892 -0.0959 184 ALA A CA 1476 C C . ALA A 184 ? 1.7986 1.5646 0.8981 -0.1322 -0.2667 -0.1257 184 ALA A C 1477 O O . ALA A 184 ? 1.7979 1.5675 0.8617 -0.1298 -0.2388 -0.1305 184 ALA A O 1478 C CB . ALA A 184 ? 1.7871 1.5562 0.9262 -0.1530 -0.3285 -0.0778 184 ALA A CB 1479 N N . ALA A 185 ? 1.8334 1.5712 0.9138 -0.1313 -0.2784 -0.1450 185 ALA A N 1480 C CA . ALA A 185 ? 1.8870 1.5949 0.9014 -0.1251 -0.2574 -0.1750 185 ALA A CA 1481 C C . ALA A 185 ? 1.8370 1.5784 0.8779 -0.1069 -0.2115 -0.1875 185 ALA A C 1482 O O . ALA A 185 ? 1.8594 1.5978 0.8539 -0.1021 -0.1822 -0.2005 185 ALA A O 1483 C CB . ALA A 185 ? 1.9308 1.5993 0.9264 -0.1273 -0.2813 -0.1924 185 ALA A CB 1484 N N . GLU A 186 ? 1.7805 1.5556 0.8966 -0.0973 -0.2058 -0.1822 186 GLU A N 1485 C CA . GLU A 186 ? 1.7409 1.5527 0.8906 -0.0808 -0.1659 -0.1911 186 GLU A CA 1486 C C . GLU A 186 ? 1.7060 1.5494 0.8586 -0.0816 -0.1398 -0.1799 186 GLU A C 1487 O O . GLU A 186 ? 1.6759 1.5368 0.8200 -0.0720 -0.1048 -0.1923 186 GLU A O 1488 C CB . GLU A 186 ? 1.6780 1.5197 0.9076 -0.0730 -0.1696 -0.1833 186 GLU A CB 1489 C CG . GLU A 186 ? 1.6410 1.5196 0.9069 -0.0562 -0.1328 -0.1926 186 GLU A CG 1490 C CD . GLU A 186 ? 1.5924 1.4916 0.9262 -0.0486 -0.1395 -0.1873 186 GLU A CD 1491 O OE1 . GLU A 186 ? 1.6169 1.4900 0.9454 -0.0447 -0.1516 -0.1996 186 GLU A OE1 1492 O OE2 . GLU A 186 ? 1.5561 1.4951 0.9463 -0.0471 -0.1329 -0.1707 186 GLU A OE2 1493 N N . GLN A 187 ? 1.7023 1.5526 0.8684 -0.0930 -0.1571 -0.1560 187 GLN A N 1494 C CA . GLN A 187 ? 1.6849 1.5586 0.8515 -0.0959 -0.1361 -0.1434 187 GLN A CA 1495 C C . GLN A 187 ? 1.7566 1.6101 0.8477 -0.0992 -0.1165 -0.1559 187 GLN A C 1496 O O . GLN A 187 ? 1.7476 1.6248 0.8386 -0.0937 -0.0817 -0.1617 187 GLN A O 1497 C CB . GLN A 187 ? 1.6659 1.5406 0.8525 -0.1072 -0.1629 -0.1155 187 GLN A CB 1498 C CG . GLN A 187 ? 1.6521 1.5401 0.8304 -0.1122 -0.1460 -0.1011 187 GLN A CG 1499 C CD . GLN A 187 ? 1.5764 1.5057 0.8019 -0.1030 -0.1117 -0.1025 187 GLN A CD 1500 O OE1 . GLN A 187 ? 1.5096 1.4647 0.7962 -0.0948 -0.1106 -0.1008 187 GLN A OE1 1501 N NE2 . GLN A 187 ? 1.5801 1.5157 0.7765 -0.1057 -0.0844 -0.1049 187 GLN A NE2 1502 N N . THR A 188 ? 1.8330 1.6434 0.8597 -0.1090 -0.1390 -0.1595 188 THR A N 1503 C CA . THR A 188 ? 1.8957 1.6824 0.8428 -0.1129 -0.1218 -0.1713 188 THR A CA 1504 C C . THR A 188 ? 1.9068 1.6910 0.8322 -0.0986 -0.0921 -0.2007 188 THR A C 1505 O O . THR A 188 ? 1.9387 1.7271 0.8252 -0.0959 -0.0604 -0.2102 188 THR A O 1506 C CB . THR A 188 ? 1.9769 1.7155 0.8559 -0.1279 -0.1562 -0.1676 188 THR A CB 1507 O OG1 . THR A 188 ? 2.0076 1.7160 0.8763 -0.1266 -0.1807 -0.1827 188 THR A OG1 1508 C CG2 . THR A 188 ? 1.9641 1.7074 0.8678 -0.1405 -0.1860 -0.1364 188 THR A CG2 1509 N N . LYS A 189 ? 1.8817 1.6601 0.8350 -0.0890 -0.1014 -0.2138 189 LYS A N 1510 C CA . LYS A 189 ? 1.8991 1.6750 0.8404 -0.0725 -0.0746 -0.2408 189 LYS A CA 1511 C C . LYS A 189 ? 1.8492 1.6761 0.8337 -0.0602 -0.0333 -0.2418 189 LYS A C 1512 O O . LYS A 189 ? 1.8660 1.6959 0.8195 -0.0507 -0.0015 -0.2592 189 LYS A O 1513 C CB . LYS A 189 ? 1.8968 1.6580 0.8702 -0.0653 -0.0956 -0.2501 189 LYS A CB 1514 C CG . LYS A 189 ? 1.9426 1.6909 0.8989 -0.0473 -0.0731 -0.2787 189 LYS A CG 1515 C CD . LYS A 189 ? 1.9321 1.6755 0.9381 -0.0399 -0.0915 -0.2823 189 LYS A CD 1516 C CE . LYS A 189 ? 1.9536 1.6916 0.9569 -0.0186 -0.0656 -0.3078 189 LYS A CE 1517 N NZ . LYS A 189 ? 1.9034 1.6544 0.9746 -0.0096 -0.0758 -0.3049 189 LYS A NZ 1518 N N . LEU A 190 ? 1.7704 1.6375 0.8254 -0.0609 -0.0340 -0.2232 190 LEU A N 1519 C CA . LEU A 190 ? 1.7245 1.6411 0.8247 -0.0517 0.0009 -0.2226 190 LEU A CA 1520 C C . LEU A 190 ? 1.7236 1.6585 0.8082 -0.0623 0.0195 -0.2096 190 LEU A C 1521 O O . LEU A 190 ? 1.7085 1.6708 0.7941 -0.0569 0.0537 -0.2165 190 LEU A O 1522 C CB . LEU A 190 ? 1.6425 1.5925 0.8245 -0.0469 -0.0074 -0.2107 190 LEU A CB 1523 C CG . LEU A 190 ? 1.6371 1.5767 0.8492 -0.0369 -0.0248 -0.2190 190 LEU A CG 1524 C CD1 . LEU A 190 ? 1.5542 1.5376 0.8442 -0.0293 -0.0185 -0.2097 190 LEU A CD1 1525 C CD2 . LEU A 190 ? 1.6895 1.6075 0.8658 -0.0234 -0.0106 -0.2452 190 LEU A CD2 1526 N N . TYR A 191 ? 1.7354 1.6559 0.8087 -0.0774 -0.0033 -0.1897 191 TYR A N 1527 C CA . TYR A 191 ? 1.7291 1.6665 0.7985 -0.0883 0.0108 -0.1731 191 TYR A CA 1528 C C . TYR A 191 ? 1.8091 1.7108 0.8080 -0.1031 -0.0007 -0.1643 191 TYR A C 1529 O O . TYR A 191 ? 1.8180 1.7291 0.8087 -0.1130 0.0107 -0.1496 191 TYR A O 1530 C CB . TYR A 191 ? 1.6657 1.6281 0.8020 -0.0913 -0.0012 -0.1523 191 TYR A CB 1531 C CG . TYR A 191 ? 1.5939 1.5874 0.7982 -0.0782 0.0031 -0.1579 191 TYR A CG 1532 C CD1 . TYR A 191 ? 1.5543 1.5853 0.7872 -0.0696 0.0351 -0.1673 191 TYR A CD1 1533 C CD2 . TYR A 191 ? 1.5632 1.5500 0.8035 -0.0752 -0.0255 -0.1526 191 TYR A CD2 1534 C CE1 . TYR A 191 ? 1.4898 1.5488 0.7822 -0.0579 0.0378 -0.1711 191 TYR A CE1 1535 C CE2 . TYR A 191 ? 1.4980 1.5123 0.7975 -0.0638 -0.0212 -0.1563 191 TYR A CE2 1536 C CZ . TYR A 191 ? 1.4570 1.5064 0.7807 -0.0550 0.0100 -0.1657 191 TYR A CZ 1537 O OH . TYR A 191 ? 1.3829 1.4594 0.7627 -0.0440 0.0132 -0.1682 191 TYR A OH 1538 N N . GLN A 192 ? 1.8669 1.7263 0.8139 -0.1057 -0.0240 -0.1726 192 GLN A N 1539 C CA . GLN A 192 ? 1.9482 1.7698 0.8230 -0.1205 -0.0401 -0.1641 192 GLN A CA 1540 C C . GLN A 192 ? 1.9316 1.7486 0.8258 -0.1330 -0.0709 -0.1352 192 GLN A C 1541 O O . GLN A 192 ? 1.9471 1.7333 0.8200 -0.1404 -0.1075 -0.1284 192 GLN A O 1542 C CB . GLN A 192 ? 1.9989 1.8242 0.8223 -0.1245 -0.0054 -0.1674 192 GLN A CB 1543 C CG . GLN A 192 ? 2.0365 1.8571 0.8212 -0.1128 0.0232 -0.1957 192 GLN A CG 1544 C CD . GLN A 192 ? 2.1061 1.8765 0.7984 -0.1190 0.0126 -0.2066 192 GLN A CD 1545 O OE1 . GLN A 192 ? 2.1680 1.9312 0.8022 -0.1246 0.0345 -0.2078 192 GLN A OE1 1546 N NE2 . GLN A 192 ? 2.1327 1.8673 0.8093 -0.1191 -0.0217 -0.2141 192 GLN A NE2 1547 N N . ASN A 193 ? 1.8896 1.7365 0.8238 -0.1354 -0.0560 -0.1184 193 ASN A N 1548 C CA . ASN A 193 ? 1.8880 1.7310 0.8395 -0.1455 -0.0791 -0.0903 193 ASN A CA 1549 C C . ASN A 193 ? 1.8450 1.6912 0.8533 -0.1416 -0.1120 -0.0813 193 ASN A C 1550 O O . ASN A 193 ? 1.7797 1.6531 0.8471 -0.1307 -0.1042 -0.0885 193 ASN A O 1551 C CB . ASN A 193 ? 1.8588 1.7326 0.8456 -0.1471 -0.0526 -0.0779 193 ASN A CB 1552 C CG . ASN A 193 ? 1.9072 1.7870 0.8501 -0.1506 -0.0157 -0.0874 193 ASN A CG 1553 O OD1 . ASN A 193 ? 1.9917 1.8528 0.8757 -0.1504 -0.0078 -0.1035 193 ASN A OD1 1554 N ND2 . ASN A 193 ? 1.8753 1.7809 0.8464 -0.1542 0.0077 -0.0777 193 ASN A ND2 1555 N N . PRO A 194 ? 1.8807 1.7008 0.8718 -0.1508 -0.1492 -0.0645 194 PRO A N 1556 C CA . PRO A 194 ? 1.8410 1.6659 0.8867 -0.1481 -0.1813 -0.0547 194 PRO A CA 1557 C C . PRO A 194 ? 1.7635 1.6207 0.8845 -0.1433 -0.1784 -0.0346 194 PRO A C 1558 O O . PRO A 194 ? 1.6965 1.5730 0.8783 -0.1357 -0.1877 -0.0331 194 PRO A O 1559 C CB . PRO A 194 ? 1.9100 1.6985 0.9089 -0.1610 -0.2207 -0.0413 194 PRO A CB 1560 C CG . PRO A 194 ? 1.9563 1.7302 0.8986 -0.1701 -0.2090 -0.0316 194 PRO A CG 1561 C CD . PRO A 194 ? 1.9539 1.7408 0.8759 -0.1646 -0.1640 -0.0521 194 PRO A CD 1562 N N . THR A 195 ? 1.7604 1.6214 0.8754 -0.1478 -0.1652 -0.0194 195 THR A N 1563 C CA . THR A 195 ? 1.6995 1.5854 0.8784 -0.1431 -0.1603 -0.0014 195 THR A CA 1564 C C . THR A 195 ? 1.6560 1.5645 0.8446 -0.1404 -0.1196 -0.0099 195 THR A C 1565 O O . THR A 195 ? 1.6798 1.5780 0.8247 -0.1486 -0.1035 -0.0074 195 THR A O 1566 C CB . THR A 195 ? 1.7289 1.5967 0.8985 -0.1509 -0.1831 0.0271 195 THR A CB 1567 O OG1 . THR A 195 ? 1.7620 1.6091 0.9170 -0.1557 -0.2228 0.0354 195 THR A OG1 1568 C CG2 . THR A 195 ? 1.6764 1.5667 0.9152 -0.1436 -0.1798 0.0449 195 THR A CG2 1569 N N . THR A 196 ? 1.5929 1.5329 0.8387 -0.1300 -0.1040 -0.0189 196 THR A N 1570 C CA . THR A 196 ? 1.5594 1.5244 0.8182 -0.1279 -0.0673 -0.0288 196 THR A CA 1571 C C . THR A 196 ? 1.4999 1.4895 0.8237 -0.1223 -0.0607 -0.0185 196 THR A C 1572 O O . THR A 196 ? 1.4516 1.4398 0.8113 -0.1185 -0.0824 -0.0034 196 THR A O 1573 C CB . THR A 196 ? 1.5445 1.5258 0.8021 -0.1203 -0.0490 -0.0546 196 THR A CB 1574 O OG1 . THR A 196 ? 1.5014 1.4961 0.8085 -0.1100 -0.0626 -0.0585 196 THR A OG1 1575 C CG2 . THR A 196 ? 1.6114 1.5654 0.8008 -0.1244 -0.0524 -0.0673 196 THR A CG2 1576 N N . TYR A 197 ? 1.4824 1.4948 0.8202 -0.1221 -0.0303 -0.0267 197 TYR A N 1577 C CA . TYR A 197 ? 1.4327 1.4657 0.8238 -0.1182 -0.0206 -0.0198 197 TYR A CA 1578 C C . TYR A 197 ? 1.4295 1.4907 0.8315 -0.1186 0.0116 -0.0349 197 TYR A C 1579 O O . TYR A 197 ? 1.4509 1.5155 0.8186 -0.1227 0.0280 -0.0474 197 TYR A O 1580 C CB . TYR A 197 ? 1.4505 1.4635 0.8349 -0.1254 -0.0258 0.0016 197 TYR A CB 1581 C CG . TYR A 197 ? 1.4862 1.4861 0.8212 -0.1387 -0.0080 0.0028 197 TYR A CG 1582 C CD1 . TYR A 197 ? 1.5468 1.5215 0.8216 -0.1467 -0.0166 0.0049 197 TYR A CD1 1583 C CD2 . TYR A 197 ? 1.4599 1.4721 0.8066 -0.1445 0.0173 0.0020 197 TYR A CD2 1584 C CE1 . TYR A 197 ? 1.5781 1.5420 0.8069 -0.1595 0.0012 0.0074 197 TYR A CE1 1585 C CE2 . TYR A 197 ? 1.4992 1.5008 0.8029 -0.1583 0.0340 0.0047 197 TYR A CE2 1586 C CZ . TYR A 197 ? 1.5614 1.5397 0.8066 -0.1655 0.0268 0.0080 197 TYR A CZ 1587 O OH . TYR A 197 ? 1.5827 1.5516 0.7845 -0.1798 0.0449 0.0121 197 TYR A OH 1588 N N . ILE A 198 ? 1.3968 1.4789 0.8470 -0.1143 0.0206 -0.0333 198 ILE A N 1589 C CA . ILE A 198 ? 1.3997 1.5077 0.8625 -0.1178 0.0487 -0.0436 198 ILE A CA 1590 C C . ILE A 198 ? 1.3870 1.4919 0.8739 -0.1217 0.0533 -0.0315 198 ILE A C 1591 O O . ILE A 198 ? 1.3690 1.4763 0.8941 -0.1130 0.0428 -0.0250 198 ILE A O 1592 C CB . ILE A 198 ? 1.3826 1.5239 0.8825 -0.1070 0.0564 -0.0592 198 ILE A CB 1593 C CG1 . ILE A 198 ? 1.4012 1.5412 0.8811 -0.1005 0.0501 -0.0717 198 ILE A CG1 1594 C CG2 . ILE A 198 ? 1.3702 1.5403 0.8814 -0.1122 0.0837 -0.0688 198 ILE A CG2 1595 C CD1 . ILE A 198 ? 1.3706 1.5366 0.8906 -0.0879 0.0505 -0.0828 198 ILE A CD1 1596 N N . SER A 199 ? 1.3909 1.4893 0.8551 -0.1348 0.0695 -0.0283 199 SER A N 1597 C CA . SER A 199 ? 1.3815 1.4724 0.8643 -0.1397 0.0757 -0.0188 199 SER A CA 1598 C C . SER A 199 ? 1.3412 1.4611 0.8417 -0.1458 0.1000 -0.0317 199 SER A C 1599 O O . SER A 199 ? 1.3402 1.4742 0.8198 -0.1550 0.1163 -0.0400 199 SER A O 1600 C CB . SER A 199 ? 1.4382 1.4943 0.8832 -0.1518 0.0729 -0.0023 199 SER A CB 1601 O OG . SER A 199 ? 1.4750 1.5351 0.8857 -0.1665 0.0924 -0.0072 199 SER A OG 1602 N N . VAL A 200 ? 1.3110 1.4408 0.8502 -0.1407 0.1023 -0.0331 200 VAL A N 1603 C CA . VAL A 200 ? 1.2918 1.4494 0.8500 -0.1469 0.1218 -0.0451 200 VAL A CA 1604 C C . VAL A 200 ? 1.2944 1.4335 0.8613 -0.1543 0.1270 -0.0383 200 VAL A C 1605 O O . VAL A 200 ? 1.2863 1.4069 0.8703 -0.1448 0.1162 -0.0298 200 VAL A O 1606 C CB . VAL A 200 ? 1.2425 1.4330 0.8381 -0.1335 0.1208 -0.0571 200 VAL A CB 1607 C CG1 . VAL A 200 ? 1.2225 1.4472 0.8305 -0.1412 0.1400 -0.0702 200 VAL A CG1 1608 C CG2 . VAL A 200 ? 1.2468 1.4436 0.8369 -0.1224 0.1092 -0.0610 200 VAL A CG2 1609 N N . GLY A 201 ? 1.3185 1.4626 0.8743 -0.1713 0.1441 -0.0420 201 GLY A N 1610 C CA . GLY A 201 ? 1.3393 1.4617 0.8985 -0.1810 0.1501 -0.0373 201 GLY A CA 1611 C C . GLY A 201 ? 1.3233 1.4729 0.8958 -0.1936 0.1668 -0.0503 201 GLY A C 1612 O O . GLY A 201 ? 1.3072 1.4890 0.8768 -0.2008 0.1770 -0.0586 201 GLY A O 1613 N N . THR A 202 ? 1.3352 1.4721 0.9230 -0.1955 0.1692 -0.0520 202 THR A N 1614 C CA . THR A 202 ? 1.3458 1.4990 0.9409 -0.2118 0.1828 -0.0624 202 THR A CA 1615 C C . THR A 202 ? 1.4126 1.5221 0.9989 -0.2207 0.1844 -0.0566 202 THR A C 1616 O O . THR A 202 ? 1.4464 1.5164 1.0177 -0.2165 0.1772 -0.0428 202 THR A O 1617 C CB . THR A 202 ? 1.2961 1.4853 0.9231 -0.2022 0.1835 -0.0764 202 THR A CB 1618 O OG1 . THR A 202 ? 1.2584 1.4264 0.9002 -0.1879 0.1765 -0.0751 202 THR A OG1 1619 C CG2 . THR A 202 ? 1.2654 1.4911 0.9038 -0.1888 0.1795 -0.0810 202 THR A CG2 1620 N N . SER A 203 ? 1.4433 1.5583 1.0381 -0.2330 0.1930 -0.0668 203 SER A N 1621 C CA . SER A 203 ? 1.4937 1.5645 1.0810 -0.2398 0.1950 -0.0648 203 SER A CA 1622 C C . SER A 203 ? 1.4882 1.5309 1.0865 -0.2158 0.1857 -0.0592 203 SER A C 1623 O O . SER A 203 ? 1.5409 1.5378 1.1268 -0.2141 0.1829 -0.0479 203 SER A O 1624 C CB . SER A 203 ? 1.5047 1.5905 1.1014 -0.2538 0.2032 -0.0801 203 SER A CB 1625 O OG . SER A 203 ? 1.5826 1.6230 1.1727 -0.2558 0.2045 -0.0814 203 SER A OG 1626 N N . THR A 204 ? 1.4329 1.5041 1.0562 -0.1971 0.1812 -0.0660 204 THR A N 1627 C CA . THR A 204 ? 1.4116 1.4650 1.0517 -0.1737 0.1737 -0.0606 204 THR A CA 1628 C C . THR A 204 ? 1.4098 1.4733 1.0578 -0.1568 0.1604 -0.0493 204 THR A C 1629 O O . THR A 204 ? 1.4645 1.5010 1.1167 -0.1432 0.1516 -0.0363 204 THR A O 1630 C CB . THR A 204 ? 1.3545 1.4308 1.0178 -0.1641 0.1777 -0.0743 204 THR A CB 1631 O OG1 . THR A 204 ? 1.2831 1.4091 0.9598 -0.1628 0.1762 -0.0818 204 THR A OG1 1632 C CG2 . THR A 204 ? 1.3719 1.4328 1.0245 -0.1805 0.1888 -0.0863 204 THR A CG2 1633 N N . LEU A 205 ? 1.3641 1.4657 1.0148 -0.1578 0.1583 -0.0542 205 LEU A N 1634 C CA . LEU A 205 ? 1.3281 1.4412 0.9870 -0.1421 0.1447 -0.0469 205 LEU A CA 1635 C C . LEU A 205 ? 1.3455 1.4296 0.9796 -0.1445 0.1351 -0.0311 205 LEU A C 1636 O O . LEU A 205 ? 1.3480 1.4196 0.9538 -0.1615 0.1412 -0.0285 205 LEU A O 1637 C CB . LEU A 205 ? 1.3106 1.4679 0.9762 -0.1424 0.1461 -0.0578 205 LEU A CB 1638 C CG . LEU A 205 ? 1.3099 1.4816 0.9899 -0.1250 0.1321 -0.0543 205 LEU A CG 1639 C CD1 . LEU A 205 ? 1.2820 1.4570 0.9941 -0.1081 0.1269 -0.0528 205 LEU A CD1 1640 C CD2 . LEU A 205 ? 1.2822 1.4914 0.9636 -0.1262 0.1351 -0.0654 205 LEU A CD2 1641 N N . ASN A 206 ? 1.3066 1.3812 0.9516 -0.1281 0.1195 -0.0196 206 ASN A N 1642 C CA . ASN A 206 ? 1.3131 1.3617 0.9358 -0.1284 0.1061 -0.0033 206 ASN A CA 1643 C C . ASN A 206 ? 1.2752 1.3378 0.9109 -0.1139 0.0880 0.0017 206 ASN A C 1644 O O . ASN A 206 ? 1.2609 1.3114 0.9158 -0.1003 0.0746 0.0142 206 ASN A O 1645 C CB . ASN A 206 ? 1.3408 1.3477 0.9628 -0.1253 0.1032 0.0115 206 ASN A CB 1646 C CG . ASN A 206 ? 1.3788 1.3572 0.9759 -0.1268 0.0882 0.0308 206 ASN A CG 1647 O OD1 . ASN A 206 ? 1.3839 1.3645 0.9495 -0.1386 0.0866 0.0316 206 ASN A OD1 1648 N ND2 . ASN A 206 ? 1.4033 1.3552 1.0141 -0.1142 0.0772 0.0470 206 ASN A ND2 1649 N N . GLN A 207 ? 1.2483 1.3359 0.8739 -0.1171 0.0876 -0.0079 207 GLN A N 1650 C CA . GLN A 207 ? 1.2314 1.3337 0.8697 -0.1049 0.0713 -0.0070 207 GLN A CA 1651 C C . GLN A 207 ? 1.2687 1.3561 0.8713 -0.1099 0.0581 -0.0001 207 GLN A C 1652 O O . GLN A 207 ? 1.2952 1.3751 0.8620 -0.1233 0.0671 -0.0022 207 GLN A O 1653 C CB . GLN A 207 ? 1.1897 1.3300 0.8453 -0.1020 0.0800 -0.0245 207 GLN A CB 1654 C CG . GLN A 207 ? 1.1738 1.3288 0.8418 -0.0909 0.0647 -0.0258 207 GLN A CG 1655 C CD . GLN A 207 ? 1.1617 1.3518 0.8468 -0.0876 0.0743 -0.0418 207 GLN A CD 1656 O OE1 . GLN A 207 ? 1.1872 1.3888 0.8554 -0.0902 0.0765 -0.0511 207 GLN A OE1 1657 N NE2 . GLN A 207 ? 1.1452 1.3520 0.8628 -0.0814 0.0809 -0.0451 207 GLN A NE2 1658 N N . ARG A 208 ? 1.2804 1.3638 0.8922 -0.0998 0.0367 0.0086 208 ARG A N 1659 C CA . ARG A 208 ? 1.3375 1.4091 0.9149 -0.1036 0.0214 0.0121 208 ARG A CA 1660 C C . ARG A 208 ? 1.3352 1.4199 0.9348 -0.0924 0.0027 0.0109 208 ARG A C 1661 O O . ARG A 208 ? 1.3356 1.4159 0.9637 -0.0835 -0.0141 0.0244 208 ARG A O 1662 C CB . ARG A 208 ? 1.3964 1.4327 0.9483 -0.1085 0.0079 0.0320 208 ARG A CB 1663 C CG . ARG A 208 ? 1.4539 1.4747 0.9565 -0.1169 -0.0037 0.0340 208 ARG A CG 1664 C CD . ARG A 208 ? 1.5071 1.4951 0.9912 -0.1186 -0.0253 0.0570 208 ARG A CD 1665 N NE . ARG A 208 ? 1.5565 1.5262 0.9837 -0.1294 -0.0335 0.0588 208 ARG A NE 1666 C CZ . ARG A 208 ? 1.6081 1.5656 0.9911 -0.1431 -0.0175 0.0575 208 ARG A CZ 1667 N NH1 . ARG A 208 ? 1.6030 1.5646 0.9934 -0.1492 0.0064 0.0545 208 ARG A NH1 1668 N NH2 . ARG A 208 ? 1.6706 1.6113 0.9999 -0.1517 -0.0254 0.0592 208 ARG A NH2 1669 N N . LEU A 209 ? 1.3359 1.4366 0.9241 -0.0930 0.0060 -0.0046 209 LEU A N 1670 C CA . LEU A 209 ? 1.3252 1.4363 0.9323 -0.0840 -0.0107 -0.0077 209 LEU A CA 1671 C C . LEU A 209 ? 1.3725 1.4606 0.9399 -0.0887 -0.0310 -0.0044 209 LEU A C 1672 O O . LEU A 209 ? 1.4055 1.4792 0.9260 -0.0981 -0.0243 -0.0084 209 LEU A O 1673 C CB . LEU A 209 ? 1.3052 1.4450 0.9244 -0.0803 0.0045 -0.0272 209 LEU A CB 1674 C CG . LEU A 209 ? 1.2795 1.4442 0.9302 -0.0779 0.0256 -0.0335 209 LEU A CG 1675 C CD1 . LEU A 209 ? 1.2584 1.4505 0.9131 -0.0758 0.0395 -0.0516 209 LEU A CD1 1676 C CD2 . LEU A 209 ? 1.2487 1.4208 0.9454 -0.0678 0.0182 -0.0236 209 LEU A CD2 1677 N N . VAL A 210 ? 1.3738 1.4583 0.9591 -0.0831 -0.0559 0.0034 210 VAL A N 1678 C CA . VAL A 210 ? 1.4348 1.4978 0.9830 -0.0880 -0.0783 0.0040 210 VAL A CA 1679 C C . VAL A 210 ? 1.4183 1.4929 0.9870 -0.0817 -0.0896 -0.0058 210 VAL A C 1680 O O . VAL A 210 ? 1.3760 1.4696 0.9956 -0.0736 -0.0937 -0.0006 210 VAL A O 1681 C CB . VAL A 210 ? 1.4732 1.5130 1.0159 -0.0912 -0.1048 0.0271 210 VAL A CB 1682 C CG1 . VAL A 210 ? 1.4988 1.5204 1.0111 -0.0987 -0.0946 0.0366 210 VAL A CG1 1683 C CG2 . VAL A 210 ? 1.4486 1.5026 1.0520 -0.0815 -0.1179 0.0427 210 VAL A CG2 1684 N N . PRO A 211 ? 1.4591 1.5210 0.9872 -0.0852 -0.0932 -0.0203 211 PRO A N 1685 C CA . PRO A 211 ? 1.4518 1.5193 0.9971 -0.0796 -0.1048 -0.0298 211 PRO A CA 1686 C C . PRO A 211 ? 1.4603 1.5171 1.0255 -0.0810 -0.1389 -0.0138 211 PRO A C 1687 O O . PRO A 211 ? 1.4899 1.5221 1.0242 -0.0890 -0.1597 -0.0033 211 PRO A O 1688 C CB . PRO A 211 ? 1.4907 1.5395 0.9793 -0.0832 -0.1002 -0.0489 211 PRO A CB 1689 C CG . PRO A 211 ? 1.5063 1.5515 0.9572 -0.0893 -0.0781 -0.0513 211 PRO A CG 1690 C CD . PRO A 211 ? 1.4997 1.5420 0.9650 -0.0935 -0.0837 -0.0297 211 PRO A CD 1691 N N . ARG A 212 ? 1.4415 1.5187 1.0594 -0.0738 -0.1446 -0.0105 212 ARG A N 1692 C CA . ARG A 212 ? 1.4659 1.5394 1.1118 -0.0754 -0.1760 0.0050 212 ARG A CA 1693 C C . ARG A 212 ? 1.4870 1.5468 1.1178 -0.0781 -0.1918 -0.0081 212 ARG A C 1694 O O . ARG A 212 ? 1.4290 1.4996 1.0684 -0.0718 -0.1767 -0.0239 212 ARG A O 1695 C CB . ARG A 212 ? 1.4318 1.5364 1.1463 -0.0665 -0.1715 0.0187 212 ARG A CB 1696 C CG . ARG A 212 ? 1.4336 1.5425 1.1643 -0.0644 -0.1666 0.0365 212 ARG A CG 1697 C CD . ARG A 212 ? 1.3974 1.5314 1.1608 -0.0552 -0.1368 0.0337 212 ARG A CD 1698 N NE . ARG A 212 ? 1.3546 1.5157 1.1733 -0.0468 -0.1360 0.0375 212 ARG A NE 1699 C CZ . ARG A 212 ? 1.3322 1.5139 1.1670 -0.0411 -0.1155 0.0244 212 ARG A CZ 1700 N NH1 . ARG A 212 ? 1.3185 1.5002 1.1229 -0.0423 -0.0939 0.0061 212 ARG A NH1 1701 N NH2 . ARG A 212 ? 1.3225 1.5271 1.2060 -0.0344 -0.1168 0.0312 212 ARG A NH2 1702 N N . ILE A 213 ? 1.5693 1.6034 1.1758 -0.0876 -0.2231 -0.0012 213 ILE A N 1703 C CA . ILE A 213 ? 1.6188 1.6313 1.2034 -0.0925 -0.2423 -0.0136 213 ILE A CA 1704 C C . ILE A 213 ? 1.6246 1.6467 1.2615 -0.0951 -0.2705 0.0025 213 ILE A C 1705 O O . ILE A 213 ? 1.6313 1.6627 1.2982 -0.0981 -0.2881 0.0256 213 ILE A O 1706 C CB . ILE A 213 ? 1.6683 1.6408 1.1802 -0.1040 -0.2593 -0.0198 213 ILE A CB 1707 C CG1 . ILE A 213 ? 1.6764 1.6408 1.1358 -0.1013 -0.2283 -0.0382 213 ILE A CG1 1708 C CG2 . ILE A 213 ? 1.7062 1.6515 1.1967 -0.1107 -0.2850 -0.0307 213 ILE A CG2 1709 C CD1 . ILE A 213 ? 1.7406 1.6701 1.1277 -0.1122 -0.2391 -0.0397 213 ILE A CD1 1710 N N . ALA A 214 ? 1.6224 1.6427 1.2718 -0.0936 -0.2742 -0.0089 214 ALA A N 1711 C CA . ALA A 214 ? 1.6122 1.6396 1.3088 -0.0982 -0.3010 0.0051 214 ALA A CA 1712 C C . ALA A 214 ? 1.6290 1.6401 1.3170 -0.0985 -0.3047 -0.0130 214 ALA A C 1713 O O . ALA A 214 ? 1.6240 1.6312 1.2890 -0.0899 -0.2797 -0.0341 214 ALA A O 1714 C CB . ALA A 214 ? 1.5489 1.6189 1.3185 -0.0894 -0.2894 0.0237 214 ALA A CB 1715 N N . THR A 215 ? 1.6482 1.6495 1.3562 -0.1085 -0.3366 -0.0039 215 THR A N 1716 C CA . THR A 215 ? 1.6403 1.6265 1.3512 -0.1092 -0.3425 -0.0172 215 THR A CA 1717 C C . THR A 215 ? 1.5434 1.5684 1.3178 -0.0975 -0.3213 -0.0105 215 THR A C 1718 O O . THR A 215 ? 1.5125 1.5702 1.3443 -0.0972 -0.3249 0.0125 215 THR A O 1719 C CB . THR A 215 ? 1.6855 1.6496 1.4019 -0.1263 -0.3853 -0.0072 215 THR A CB 1720 O OG1 . THR A 215 ? 1.7539 1.6823 1.4084 -0.1382 -0.4069 -0.0121 215 THR A OG1 1721 C CG2 . THR A 215 ? 1.7084 1.6502 1.4238 -0.1277 -0.3915 -0.0220 215 THR A CG2 1722 N N . ARG A 216 ? 1.4923 1.5141 1.2557 -0.0872 -0.2985 -0.0301 216 ARG A N 1723 C CA . ARG A 216 ? 1.4102 1.4676 1.2258 -0.0755 -0.2765 -0.0253 216 ARG A CA 1724 C C . ARG A 216 ? 1.3942 1.4356 1.2125 -0.0729 -0.2786 -0.0375 216 ARG A C 1725 O O . ARG A 216 ? 1.4175 1.4206 1.1868 -0.0742 -0.2839 -0.0578 216 ARG A O 1726 C CB . ARG A 216 ? 1.3746 1.4540 1.1805 -0.0627 -0.2401 -0.0344 216 ARG A CB 1727 C CG . ARG A 216 ? 1.3641 1.4614 1.1759 -0.0639 -0.2349 -0.0202 216 ARG A CG 1728 C CD . ARG A 216 ? 1.3344 1.4520 1.1378 -0.0533 -0.1997 -0.0295 216 ARG A CD 1729 N NE . ARG A 216 ? 1.3719 1.4653 1.1133 -0.0542 -0.1901 -0.0484 216 ARG A NE 1730 C CZ . ARG A 216 ? 1.3766 1.4574 1.0832 -0.0603 -0.1923 -0.0457 216 ARG A CZ 1731 N NH1 . ARG A 216 ? 1.3690 1.4576 1.0970 -0.0651 -0.2050 -0.0248 216 ARG A NH1 1732 N NH2 . ARG A 216 ? 1.4071 1.4674 1.0571 -0.0609 -0.1810 -0.0633 216 ARG A NH2 1733 N N . SER A 217 ? 1.3465 1.4159 1.2209 -0.0686 -0.2737 -0.0248 217 SER A N 1734 C CA . SER A 217 ? 1.3449 1.4025 1.2285 -0.0646 -0.2735 -0.0332 217 SER A CA 1735 C C . SER A 217 ? 1.3405 1.3944 1.1928 -0.0493 -0.2444 -0.0566 217 SER A C 1736 O O . SER A 217 ? 1.2962 1.3712 1.1383 -0.0415 -0.2203 -0.0610 217 SER A O 1737 C CB . SER A 217 ? 1.3014 1.3954 1.2523 -0.0628 -0.2707 -0.0118 217 SER A CB 1738 O OG . SER A 217 ? 1.3094 1.4148 1.2957 -0.0755 -0.2941 0.0119 217 SER A OG 1739 N N . LYS A 218 ? 1.3733 1.4000 1.2117 -0.0453 -0.2471 -0.0708 218 LYS A N 1740 C CA . LYS A 218 ? 1.3729 1.3941 1.1823 -0.0297 -0.2214 -0.0932 218 LYS A CA 1741 C C . LYS A 218 ? 1.3212 1.3800 1.1743 -0.0163 -0.1990 -0.0874 218 LYS A C 1742 O O . LYS A 218 ? 1.3312 1.3863 1.2125 -0.0146 -0.2063 -0.0817 218 LYS A O 1743 C CB . LYS A 218 ? 1.4262 1.3954 1.1943 -0.0294 -0.2337 -0.1135 218 LYS A CB 1744 C CG . LYS A 218 ? 1.4773 1.4068 1.1842 -0.0391 -0.2479 -0.1268 218 LYS A CG 1745 C CD . LYS A 218 ? 1.5398 1.4170 1.1986 -0.0348 -0.2525 -0.1517 218 LYS A CD 1746 C CE . LYS A 218 ? 1.6004 1.4353 1.1935 -0.0461 -0.2684 -0.1648 218 LYS A CE 1747 N NZ . LYS A 218 ? 1.6703 1.4543 1.2087 -0.0383 -0.2654 -0.1932 218 LYS A NZ 1748 N N . VAL A 219 ? 1.2666 1.3602 1.1233 -0.0080 -0.1727 -0.0885 219 VAL A N 1749 C CA . VAL A 219 ? 1.2213 1.3499 1.1096 0.0049 -0.1501 -0.0863 219 VAL A CA 1750 C C . VAL A 219 ? 1.2399 1.3607 1.0947 0.0183 -0.1300 -0.1092 219 VAL A C 1751 O O . VAL A 219 ? 1.2647 1.3797 1.0818 0.0181 -0.1200 -0.1216 219 VAL A O 1752 C CB . VAL A 219 ? 1.1834 1.3554 1.0976 0.0045 -0.1345 -0.0730 219 VAL A CB 1753 C CG1 . VAL A 219 ? 1.1389 1.3466 1.0840 0.0160 -0.1137 -0.0701 219 VAL A CG1 1754 C CG2 . VAL A 219 ? 1.1750 1.3540 1.1200 -0.0073 -0.1530 -0.0508 219 VAL A CG2 1755 N N . ASN A 220 ? 1.2451 1.3664 1.1149 0.0300 -0.1239 -0.1137 220 ASN A N 1756 C CA . ASN A 220 ? 1.2804 1.3911 1.1222 0.0448 -0.1070 -0.1351 220 ASN A CA 1757 C C . ASN A 220 ? 1.3017 1.3653 1.0875 0.0420 -0.1147 -0.1545 220 ASN A C 1758 O O . ASN A 220 ? 1.3155 1.3769 1.0686 0.0511 -0.0958 -0.1721 220 ASN A O 1759 C CB . ASN A 220 ? 1.3002 1.4540 1.1463 0.0530 -0.0783 -0.1385 220 ASN A CB 1760 C CG . ASN A 220 ? 1.2934 1.4857 1.1842 0.0624 -0.0671 -0.1280 220 ASN A CG 1761 O OD1 . ASN A 220 ? 1.3326 1.5442 1.2251 0.0756 -0.0481 -0.1369 220 ASN A OD1 1762 N ND2 . ASN A 220 ? 1.2838 1.4891 1.2113 0.0555 -0.0786 -0.1081 220 ASN A ND2 1763 N N . GLY A 221 ? 1.2946 1.3216 1.0692 0.0288 -0.1426 -0.1507 221 GLY A N 1764 C CA . GLY A 221 ? 1.3371 1.3155 1.0546 0.0235 -0.1540 -0.1682 221 GLY A CA 1765 C C . GLY A 221 ? 1.3211 1.3033 1.0016 0.0161 -0.1476 -0.1721 221 GLY A C 1766 O O . GLY A 221 ? 1.3661 1.3153 0.9923 0.0166 -0.1459 -0.1906 221 GLY A O 1767 N N . GLN A 222 ? 1.2648 1.2849 0.9722 0.0092 -0.1437 -0.1546 222 GLN A N 1768 C CA . GLN A 222 ? 1.2722 1.2955 0.9475 0.0014 -0.1388 -0.1550 222 GLN A CA 1769 C C . GLN A 222 ? 1.2561 1.2831 0.9496 -0.0147 -0.1620 -0.1338 222 GLN A C 1770 O O . GLN A 222 ? 1.2102 1.2659 0.9556 -0.0161 -0.1657 -0.1151 222 GLN A O 1771 C CB . GLN A 222 ? 1.2249 1.2911 0.9110 0.0098 -0.1071 -0.1558 222 GLN A CB 1772 C CG . GLN A 222 ? 1.2315 1.3063 0.9120 0.0269 -0.0822 -0.1732 222 GLN A CG 1773 C CD . GLN A 222 ? 1.2897 1.3233 0.9141 0.0319 -0.0799 -0.1960 222 GLN A CD 1774 O OE1 . GLN A 222 ? 1.3122 1.3188 0.8901 0.0222 -0.0875 -0.2014 222 GLN A OE1 1775 N NE2 . GLN A 222 ? 1.3015 1.3293 0.9287 0.0480 -0.0688 -0.2095 222 GLN A NE2 1776 N N . SER A 223 ? 1.2906 1.2890 0.9406 -0.0261 -0.1772 -0.1362 223 SER A N 1777 C CA . SER A 223 ? 1.2935 1.2966 0.9567 -0.0404 -0.1984 -0.1156 223 SER A CA 1778 C C . SER A 223 ? 1.2779 1.3055 0.9340 -0.0406 -0.1804 -0.1098 223 SER A C 1779 O O . SER A 223 ? 1.2603 1.3018 0.9388 -0.0482 -0.1910 -0.0905 223 SER A O 1780 C CB . SER A 223 ? 1.3598 1.3166 0.9792 -0.0542 -0.2295 -0.1194 223 SER A CB 1781 O OG . SER A 223 ? 1.3999 1.3287 1.0231 -0.0559 -0.2480 -0.1254 223 SER A OG 1782 N N . GLY A 224 ? 1.2920 1.3238 0.9174 -0.0324 -0.1532 -0.1261 224 GLY A N 1783 C CA . GLY A 224 ? 1.2651 1.3213 0.8861 -0.0327 -0.1327 -0.1214 224 GLY A CA 1784 C C . GLY A 224 ? 1.1983 1.2989 0.8739 -0.0252 -0.1143 -0.1119 224 GLY A C 1785 O O . GLY A 224 ? 1.1605 1.2737 0.8700 -0.0175 -0.1125 -0.1124 224 GLY A O 1786 N N . ARG A 225 ? 1.1892 1.3109 0.8707 -0.0279 -0.1013 -0.1031 225 ARG A N 1787 C CA . ARG A 225 ? 1.1547 1.3159 0.8817 -0.0223 -0.0834 -0.0949 225 ARG A CA 1788 C C . ARG A 225 ? 1.1525 1.3304 0.8621 -0.0220 -0.0567 -0.1013 225 ARG A C 1789 O O . ARG A 225 ? 1.1927 1.3534 0.8616 -0.0286 -0.0549 -0.1044 225 ARG A O 1790 C CB . ARG A 225 ? 1.1232 1.2949 0.8883 -0.0271 -0.0975 -0.0728 225 ARG A CB 1791 C CG . ARG A 225 ? 1.1170 1.2812 0.9113 -0.0288 -0.1227 -0.0624 225 ARG A CG 1792 C CD . ARG A 225 ? 1.0804 1.2664 0.9133 -0.0199 -0.1145 -0.0632 225 ARG A CD 1793 N NE . ARG A 225 ? 1.0845 1.2661 0.9503 -0.0233 -0.1378 -0.0498 225 ARG A NE 1794 C CZ . ARG A 225 ? 1.1117 1.2672 0.9677 -0.0258 -0.1560 -0.0556 225 ARG A CZ 1795 N NH1 . ARG A 225 ? 1.1470 1.2760 0.9587 -0.0232 -0.1530 -0.0761 225 ARG A NH1 1796 N NH2 . ARG A 225 ? 1.1012 1.2562 0.9921 -0.0310 -0.1771 -0.0405 225 ARG A NH2 1797 N N . MET A 226 ? 1.1177 1.3288 0.8578 -0.0154 -0.0370 -0.1024 226 MET A N 1798 C CA . MET A 226 ? 1.1244 1.3555 0.8566 -0.0172 -0.0131 -0.1061 226 MET A CA 1799 C C . MET A 226 ? 1.1020 1.3563 0.8719 -0.0184 -0.0085 -0.0924 226 MET A C 1800 O O . MET A 226 ? 1.0873 1.3616 0.8944 -0.0122 -0.0081 -0.0883 226 MET A O 1801 C CB . MET A 226 ? 1.1339 1.3857 0.8668 -0.0087 0.0073 -0.1213 226 MET A CB 1802 C CG . MET A 226 ? 1.1989 1.4294 0.8927 -0.0049 0.0092 -0.1374 226 MET A CG 1803 S SD . MET A 226 ? 1.2593 1.4792 0.9006 -0.0138 0.0246 -0.1444 226 MET A SD 1804 C CE . MET A 226 ? 1.3290 1.5259 0.9314 -0.0045 0.0280 -0.1648 226 MET A CE 1805 N N . GLU A 227 ? 1.1012 1.3506 0.8593 -0.0262 -0.0048 -0.0853 227 GLU A N 1806 C CA . GLU A 227 ? 1.0584 1.3253 0.8460 -0.0269 0.0027 -0.0746 227 GLU A CA 1807 C C . GLU A 227 ? 1.0469 1.3306 0.8238 -0.0307 0.0268 -0.0831 227 GLU A C 1808 O O . GLU A 227 ? 1.0660 1.3376 0.8083 -0.0379 0.0335 -0.0876 227 GLU A O 1809 C CB . GLU A 227 ? 1.0795 1.3262 0.8644 -0.0322 -0.0113 -0.0592 227 GLU A CB 1810 C CG . GLU A 227 ? 1.0792 1.3398 0.8990 -0.0298 -0.0063 -0.0469 227 GLU A CG 1811 C CD . GLU A 227 ? 1.1013 1.3446 0.9298 -0.0310 -0.0241 -0.0292 227 GLU A CD 1812 O OE1 . GLU A 227 ? 1.1179 1.3373 0.9197 -0.0363 -0.0403 -0.0260 227 GLU A OE1 1813 O OE2 . GLU A 227 ? 1.1068 1.3610 0.9691 -0.0262 -0.0218 -0.0180 227 GLU A OE2 1814 N N . PHE A 228 ? 0.9937 1.3056 0.7989 -0.0269 0.0393 -0.0849 228 PHE A N 1815 C CA . PHE A 228 ? 0.9739 1.3053 0.7722 -0.0318 0.0604 -0.0936 228 PHE A CA 1816 C C . PHE A 228 ? 0.9443 1.2793 0.7535 -0.0374 0.0682 -0.0867 228 PHE A C 1817 O O . PHE A 228 ? 0.9195 1.2567 0.7546 -0.0326 0.0626 -0.0777 228 PHE A O 1818 C CB . PHE A 228 ? 0.9650 1.3263 0.7824 -0.0245 0.0688 -0.1028 228 PHE A CB 1819 C CG . PHE A 228 ? 0.9947 1.3518 0.7966 -0.0186 0.0669 -0.1129 228 PHE A CG 1820 C CD1 . PHE A 228 ? 1.0112 1.3710 0.7859 -0.0224 0.0805 -0.1233 228 PHE A CD1 1821 C CD2 . PHE A 228 ? 1.0051 1.3539 0.8189 -0.0092 0.0523 -0.1120 228 PHE A CD2 1822 C CE1 . PHE A 228 ? 1.0323 1.3865 0.7909 -0.0149 0.0810 -0.1338 228 PHE A CE1 1823 C CE2 . PHE A 228 ? 1.0274 1.3671 0.8242 -0.0028 0.0510 -0.1228 228 PHE A CE2 1824 C CZ . PHE A 228 ? 1.0335 1.3756 0.8020 -0.0047 0.0661 -0.1344 228 PHE A CZ 1825 N N . PHE A 229 ? 0.9291 1.2636 0.7175 -0.0476 0.0819 -0.0910 229 PHE A N 1826 C CA . PHE A 229 ? 0.9212 1.2522 0.7129 -0.0546 0.0902 -0.0863 229 PHE A CA 1827 C C . PHE A 229 ? 0.9324 1.2868 0.7222 -0.0630 0.1082 -0.0963 229 PHE A C 1828 O O . PHE A 229 ? 0.9361 1.3083 0.7185 -0.0644 0.1152 -0.1053 229 PHE A O 1829 C CB . PHE A 229 ? 0.9535 1.2523 0.7188 -0.0623 0.0861 -0.0783 229 PHE A CB 1830 C CG . PHE A 229 ? 0.9703 1.2467 0.7388 -0.0557 0.0663 -0.0663 229 PHE A CG 1831 C CD1 . PHE A 229 ? 0.9841 1.2497 0.7355 -0.0538 0.0534 -0.0673 229 PHE A CD1 1832 C CD2 . PHE A 229 ? 0.9679 1.2340 0.7566 -0.0515 0.0604 -0.0539 229 PHE A CD2 1833 C CE1 . PHE A 229 ? 0.9942 1.2402 0.7490 -0.0500 0.0325 -0.0556 229 PHE A CE1 1834 C CE2 . PHE A 229 ? 0.9858 1.2358 0.7824 -0.0459 0.0410 -0.0410 229 PHE A CE2 1835 C CZ . PHE A 229 ? 0.9933 1.2337 0.7732 -0.0463 0.0258 -0.0415 229 PHE A CZ 1836 N N . TRP A 230 ? 0.9324 1.2866 0.7292 -0.0686 0.1156 -0.0946 230 TRP A N 1837 C CA . TRP A 230 ? 0.9173 1.2929 0.7132 -0.0791 0.1303 -0.1033 230 TRP A CA 1838 C C . TRP A 230 ? 0.9305 1.2862 0.7159 -0.0906 0.1373 -0.1008 230 TRP A C 1839 O O . TRP A 230 ? 0.9361 1.2647 0.7213 -0.0866 0.1316 -0.0921 230 TRP A O 1840 C CB . TRP A 230 ? 0.8883 1.2955 0.7113 -0.0723 0.1318 -0.1079 230 TRP A CB 1841 C CG . TRP A 230 ? 0.8732 1.2737 0.7146 -0.0641 0.1269 -0.1015 230 TRP A CG 1842 C CD1 . TRP A 230 ? 0.8649 1.2607 0.7233 -0.0508 0.1155 -0.0936 230 TRP A CD1 1843 C CD2 . TRP A 230 ? 0.8696 1.2675 0.7138 -0.0690 0.1345 -0.1026 230 TRP A CD2 1844 N NE1 . TRP A 230 ? 0.8484 1.2419 0.7220 -0.0463 0.1170 -0.0887 230 TRP A NE1 1845 C CE2 . TRP A 230 ? 0.8643 1.2573 0.7274 -0.0565 0.1290 -0.0950 230 TRP A CE2 1846 C CE3 . TRP A 230 ? 0.8792 1.2773 0.7107 -0.0834 0.1455 -0.1096 230 TRP A CE3 1847 C CZ2 . TRP A 230 ? 0.8826 1.2705 0.7502 -0.0561 0.1361 -0.0951 230 TRP A CZ2 1848 C CZ3 . TRP A 230 ? 0.8964 1.2861 0.7306 -0.0841 0.1505 -0.1105 230 TRP A CZ3 1849 C CH2 . TRP A 230 ? 0.8852 1.2694 0.7361 -0.0697 0.1467 -0.1038 230 TRP A CH2 1850 N N . THR A 231 ? 0.9341 1.3032 0.7118 -0.1048 0.1494 -0.1081 231 THR A N 1851 C CA . THR A 231 ? 0.9497 1.3015 0.7191 -0.1170 0.1566 -0.1084 231 THR A CA 1852 C C . THR A 231 ? 0.9577 1.3382 0.7300 -0.1311 0.1670 -0.1184 231 THR A C 1853 O O . THR A 231 ? 0.9451 1.3586 0.7243 -0.1323 0.1699 -0.1234 231 THR A O 1854 C CB . THR A 231 ? 0.9848 1.3006 0.7275 -0.1266 0.1575 -0.1012 231 THR A CB 1855 O OG1 . THR A 231 ? 1.0050 1.2941 0.7424 -0.1334 0.1617 -0.0996 231 THR A OG1 1856 C CG2 . THR A 231 ? 0.9869 1.3146 0.7112 -0.1419 0.1665 -0.1048 231 THR A CG2 1857 N N . ILE A 232 ? 0.9929 1.3604 0.7608 -0.1414 0.1721 -0.1212 232 ILE A N 1858 C CA . ILE A 232 ? 1.0082 1.3979 0.7757 -0.1590 0.1800 -0.1300 232 ILE A CA 1859 C C . ILE A 232 ? 1.0556 1.4219 0.8000 -0.1787 0.1869 -0.1282 232 ILE A C 1860 O O . ILE A 232 ? 1.1077 1.4337 0.8374 -0.1826 0.1875 -0.1247 232 ILE A O 1861 C CB . ILE A 232 ? 1.0041 1.3932 0.7779 -0.1595 0.1804 -0.1360 232 ILE A CB 1862 C CG1 . ILE A 232 ? 0.9698 1.4010 0.7664 -0.1497 0.1765 -0.1398 232 ILE A CG1 1863 C CG2 . ILE A 232 ? 1.0239 1.4081 0.7839 -0.1832 0.1873 -0.1432 232 ILE A CG2 1864 C CD1 . ILE A 232 ? 0.9572 1.3966 0.7694 -0.1284 0.1690 -0.1334 232 ILE A CD1 1865 N N . LEU A 233 ? 1.0854 1.4770 0.8276 -0.1905 0.1927 -0.1296 233 LEU A N 1866 C CA . LEU A 233 ? 1.1226 1.4973 0.8439 -0.2114 0.2005 -0.1266 233 LEU A CA 1867 C C . LEU A 233 ? 1.1400 1.5276 0.8642 -0.2329 0.2057 -0.1339 233 LEU A C 1868 O O . LEU A 233 ? 1.1209 1.5536 0.8632 -0.2380 0.2077 -0.1397 233 LEU A O 1869 C CB . LEU A 233 ? 1.1330 1.5311 0.8506 -0.2131 0.2062 -0.1240 233 LEU A CB 1870 C CG . LEU A 233 ? 1.1734 1.5540 0.8666 -0.2330 0.2151 -0.1177 233 LEU A CG 1871 C CD1 . LEU A 233 ? 1.2002 1.5264 0.8684 -0.2298 0.2098 -0.1077 233 LEU A CD1 1872 C CD2 . LEU A 233 ? 1.1707 1.5835 0.8631 -0.2324 0.2234 -0.1173 233 LEU A CD2 1873 N N . LYS A 234 ? 1.1869 1.5340 0.8937 -0.2455 0.2071 -0.1335 234 LYS A N 1874 C CA . LYS A 234 ? 1.2441 1.5953 0.9494 -0.2679 0.2101 -0.1414 234 LYS A CA 1875 C C . LYS A 234 ? 1.2673 1.6384 0.9693 -0.2932 0.2179 -0.1393 234 LYS A C 1876 O O . LYS A 234 ? 1.2921 1.6598 0.9851 -0.2939 0.2228 -0.1307 234 LYS A O 1877 C CB . LYS A 234 ? 1.3246 1.6203 1.0105 -0.2715 0.2094 -0.1428 234 LYS A CB 1878 C CG . LYS A 234 ? 1.3489 1.6394 1.0432 -0.2521 0.2045 -0.1489 234 LYS A CG 1879 C CD . LYS A 234 ? 1.4343 1.6690 1.1097 -0.2522 0.2062 -0.1511 234 LYS A CD 1880 C CE . LYS A 234 ? 1.4783 1.6722 1.1456 -0.2376 0.2054 -0.1387 234 LYS A CE 1881 N NZ . LYS A 234 ? 1.5358 1.6810 1.1927 -0.2290 0.2073 -0.1406 234 LYS A NZ 1882 N N . PRO A 235 ? 1.2734 1.6675 0.9828 -0.3148 0.2190 -0.1465 235 PRO A N 1883 C CA . PRO A 235 ? 1.2604 1.6805 0.9726 -0.3401 0.2268 -0.1431 235 PRO A CA 1884 C C . PRO A 235 ? 1.3013 1.6749 0.9864 -0.3568 0.2329 -0.1345 235 PRO A C 1885 O O . PRO A 235 ? 1.3180 1.6370 0.9826 -0.3565 0.2298 -0.1344 235 PRO A O 1886 C CB . PRO A 235 ? 1.2657 1.7093 0.9889 -0.3609 0.2229 -0.1524 235 PRO A CB 1887 C CG . PRO A 235 ? 1.2766 1.6815 0.9870 -0.3520 0.2154 -0.1606 235 PRO A CG 1888 C CD . PRO A 235 ? 1.2533 1.6502 0.9673 -0.3186 0.2129 -0.1574 235 PRO A CD 1889 N N . ASN A 236 ? 1.3105 1.7054 0.9955 -0.3698 0.2423 -0.1265 236 ASN A N 1890 C CA . ASN A 236 ? 1.3513 1.7058 1.0096 -0.3860 0.2490 -0.1155 236 ASN A CA 1891 C C . ASN A 236 ? 1.3708 1.6783 1.0062 -0.3654 0.2463 -0.1070 236 ASN A C 1892 O O . ASN A 236 ? 1.4164 1.6834 1.0269 -0.3769 0.2497 -0.0965 236 ASN A O 1893 C CB . ASN A 236 ? 1.3994 1.7175 1.0444 -0.4140 0.2477 -0.1176 236 ASN A CB 1894 C CG . ASN A 236 ? 1.4381 1.7901 1.0929 -0.4471 0.2552 -0.1152 236 ASN A CG 1895 O OD1 . ASN A 236 ? 1.4462 1.8235 1.1030 -0.4540 0.2658 -0.1054 236 ASN A OD1 1896 N ND2 . ASN A 236 ? 1.4661 1.8185 1.1262 -0.4688 0.2500 -0.1239 236 ASN A ND2 1897 N N . ASP A 237 ? 1.3326 1.6459 0.9768 -0.3361 0.2392 -0.1101 237 ASP A N 1898 C CA . ASP A 237 ? 1.3394 1.6152 0.9660 -0.3165 0.2343 -0.1013 237 ASP A CA 1899 C C . ASP A 237 ? 1.3046 1.6112 0.9321 -0.3043 0.2377 -0.0975 237 ASP A C 1900 O O . ASP A 237 ? 1.2644 1.6220 0.9132 -0.3013 0.2419 -0.1042 237 ASP A O 1901 C CB . ASP A 237 ? 1.3263 1.5827 0.9613 -0.2929 0.2234 -0.1060 237 ASP A CB 1902 C CG . ASP A 237 ? 1.3482 1.5600 0.9666 -0.2763 0.2166 -0.0949 237 ASP A CG 1903 O OD1 . ASP A 237 ? 1.3820 1.5631 0.9764 -0.2869 0.2193 -0.0836 237 ASP A OD1 1904 O OD2 . ASP A 237 ? 1.3419 1.5505 0.9721 -0.2531 0.2081 -0.0961 237 ASP A OD2 1905 N N . ALA A 238 ? 1.3221 1.5959 0.9252 -0.2971 0.2356 -0.0866 238 ALA A N 1906 C CA . ALA A 238 ? 1.3136 1.6069 0.9084 -0.2867 0.2388 -0.0834 238 ALA A CA 1907 C C . ALA A 238 ? 1.2903 1.5628 0.8814 -0.2603 0.2250 -0.0813 238 ALA A C 1908 O O . ALA A 238 ? 1.3215 1.5516 0.9042 -0.2548 0.2152 -0.0747 238 ALA A O 1909 C CB . ALA A 238 ? 1.3409 1.6160 0.9045 -0.3047 0.2483 -0.0713 238 ALA A CB 1910 N N . ILE A 239 ? 1.2532 1.5556 0.8523 -0.2442 0.2241 -0.0865 239 ILE A N 1911 C CA . ILE A 239 ? 1.2416 1.5255 0.8348 -0.2219 0.2103 -0.0837 239 ILE A CA 1912 C C . ILE A 239 ? 1.2825 1.5545 0.8418 -0.2224 0.2126 -0.0768 239 ILE A C 1913 O O . ILE A 239 ? 1.2666 1.5661 0.8187 -0.2296 0.2266 -0.0803 239 ILE A O 1914 C CB . ILE A 239 ? 1.1890 1.5060 0.8121 -0.2022 0.2046 -0.0944 239 ILE A CB 1915 C CG1 . ILE A 239 ? 1.1971 1.4898 0.8175 -0.1819 0.1878 -0.0900 239 ILE A CG1 1916 C CG2 . ILE A 239 ? 1.1702 1.5305 0.7990 -0.2006 0.2157 -0.1023 239 ILE A CG2 1917 C CD1 . ILE A 239 ? 1.1539 1.4698 0.8060 -0.1639 0.1800 -0.0977 239 ILE A CD1 1918 N N . ASN A 240 ? 1.3099 1.5419 0.8486 -0.2145 0.1990 -0.0667 240 ASN A N 1919 C CA . ASN A 240 ? 1.3501 1.5626 0.8497 -0.2165 0.1983 -0.0584 240 ASN A CA 1920 C C . ASN A 240 ? 1.3397 1.5422 0.8337 -0.1964 0.1814 -0.0588 240 ASN A C 1921 O O . ASN A 240 ? 1.3311 1.5137 0.8385 -0.1852 0.1647 -0.0538 240 ASN A O 1922 C CB . ASN A 240 ? 1.4031 1.5712 0.8763 -0.2300 0.1954 -0.0422 240 ASN A CB 1923 C CG . ASN A 240 ? 1.4426 1.6157 0.9136 -0.2538 0.2124 -0.0404 240 ASN A CG 1924 O OD1 . ASN A 240 ? 1.4351 1.6341 0.8961 -0.2659 0.2286 -0.0430 240 ASN A OD1 1925 N ND2 . ASN A 240 ? 1.4763 1.6244 0.9574 -0.2609 0.2092 -0.0359 240 ASN A ND2 1926 N N . PHE A 241 ? 1.3359 1.5520 0.8102 -0.1922 0.1862 -0.0647 241 PHE A N 1927 C CA . PHE A 241 ? 1.3350 1.5391 0.7985 -0.1756 0.1699 -0.0664 241 PHE A CA 1928 C C . PHE A 241 ? 1.3815 1.5541 0.7933 -0.1816 0.1660 -0.0570 241 PHE A C 1929 O O . PHE A 241 ? 1.4099 1.5844 0.7939 -0.1957 0.1827 -0.0545 241 PHE A O 1930 C CB . PHE A 241 ? 1.3082 1.5483 0.7874 -0.1633 0.1767 -0.0828 241 PHE A CB 1931 C CG . PHE A 241 ? 1.2710 1.5410 0.7990 -0.1553 0.1768 -0.0908 241 PHE A CG 1932 C CD1 . PHE A 241 ? 1.2466 1.5104 0.7983 -0.1402 0.1586 -0.0910 241 PHE A CD1 1933 C CD2 . PHE A 241 ? 1.2531 1.5586 0.8033 -0.1639 0.1944 -0.0971 241 PHE A CD2 1934 C CE1 . PHE A 241 ? 1.2158 1.5066 0.8090 -0.1332 0.1592 -0.0973 241 PHE A CE1 1935 C CE2 . PHE A 241 ? 1.2099 1.5424 0.8013 -0.1573 0.1931 -0.1039 241 PHE A CE2 1936 C CZ . PHE A 241 ? 1.1964 1.5206 0.8076 -0.1416 0.1760 -0.1040 241 PHE A CZ 1937 N N . GLU A 242 ? 1.3957 1.5401 0.7950 -0.1718 0.1433 -0.0506 242 GLU A N 1938 C CA . GLU A 242 ? 1.4590 1.5744 0.8066 -0.1750 0.1353 -0.0437 242 GLU A CA 1939 C C . GLU A 242 ? 1.4513 1.5560 0.7989 -0.1594 0.1120 -0.0474 242 GLU A C 1940 O O . GLU A 242 ? 1.4216 1.5238 0.8043 -0.1501 0.0951 -0.0434 242 GLU A O 1941 C CB . GLU A 242 ? 1.5034 1.5819 0.8270 -0.1872 0.1275 -0.0230 242 GLU A CB 1942 C CG . GLU A 242 ? 1.5794 1.6294 0.8429 -0.1943 0.1222 -0.0144 242 GLU A CG 1943 C CD . GLU A 242 ? 1.6184 1.6298 0.8600 -0.2045 0.1106 0.0087 242 GLU A CD 1944 O OE1 . GLU A 242 ? 1.6273 1.6358 0.8703 -0.2180 0.1254 0.0165 242 GLU A OE1 1945 O OE2 . GLU A 242 ? 1.6339 1.6170 0.8565 -0.1995 0.0859 0.0198 242 GLU A OE2 1946 N N . SER A 243 ? 1.4854 1.5834 0.7937 -0.1571 0.1116 -0.0553 243 SER A N 1947 C CA . SER A 243 ? 1.4844 1.5704 0.7901 -0.1442 0.0889 -0.0606 243 SER A CA 1948 C C . SER A 243 ? 1.5530 1.6150 0.7984 -0.1457 0.0839 -0.0652 243 SER A C 1949 O O . SER A 243 ? 1.5807 1.6488 0.7918 -0.1513 0.1059 -0.0727 243 SER A O 1950 C CB . SER A 243 ? 1.4212 1.5394 0.7700 -0.1303 0.0942 -0.0772 243 SER A CB 1951 O OG . SER A 243 ? 1.4112 1.5158 0.7575 -0.1194 0.0725 -0.0823 243 SER A OG 1952 N N . ASN A 244 ? 1.5980 1.6338 0.8319 -0.1409 0.0548 -0.0607 244 ASN A N 1953 C CA . ASN A 244 ? 1.6605 1.6688 0.8367 -0.1415 0.0437 -0.0667 244 ASN A CA 1954 C C . ASN A 244 ? 1.6347 1.6507 0.8158 -0.1283 0.0427 -0.0881 244 ASN A C 1955 O O . ASN A 244 ? 1.6598 1.6545 0.7900 -0.1279 0.0401 -0.0986 244 ASN A O 1956 C CB . ASN A 244 ? 1.7142 1.6883 0.8753 -0.1451 0.0083 -0.0492 244 ASN A CB 1957 C CG . ASN A 244 ? 1.7887 1.7374 0.9043 -0.1593 0.0065 -0.0309 244 ASN A CG 1958 O OD1 . ASN A 244 ? 1.8312 1.7867 0.9256 -0.1679 0.0325 -0.0308 244 ASN A OD1 1959 N ND2 . ASN A 244 ? 1.8261 1.7461 0.9274 -0.1625 -0.0253 -0.0138 244 ASN A ND2 1960 N N . GLY A 245 ? 1.5620 1.6050 0.8022 -0.1176 0.0438 -0.0941 245 GLY A N 1961 C CA . GLY A 245 ? 1.5472 1.5959 0.8002 -0.1044 0.0398 -0.1116 245 GLY A CA 1962 C C . GLY A 245 ? 1.4921 1.5619 0.8118 -0.0955 0.0294 -0.1083 245 GLY A C 1963 O O . GLY A 245 ? 1.4612 1.5381 0.8138 -0.0991 0.0237 -0.0928 245 GLY A O 1964 N N . ASN A 246 ? 1.4750 1.5529 0.8126 -0.0835 0.0279 -0.1229 246 ASN A N 1965 C CA . ASN A 246 ? 1.4163 1.5146 0.8146 -0.0744 0.0189 -0.1209 246 ASN A CA 1966 C C . ASN A 246 ? 1.3517 1.4899 0.7951 -0.0721 0.0417 -0.1203 246 ASN A C 1967 O O . ASN A 246 ? 1.3164 1.4724 0.8084 -0.0663 0.0360 -0.1159 246 ASN A O 1968 C CB . ASN A 246 ? 1.4151 1.4965 0.8319 -0.0779 -0.0118 -0.1028 246 ASN A CB 1969 C CG . ASN A 246 ? 1.4676 1.5112 0.8439 -0.0814 -0.0388 -0.1030 246 ASN A CG 1970 O OD1 . ASN A 246 ? 1.4904 1.5263 0.8752 -0.0752 -0.0532 -0.1108 246 ASN A OD1 1971 N ND2 . ASN A 246 ? 1.4934 1.5118 0.8250 -0.0923 -0.0472 -0.0935 246 ASN A ND2 1972 N N . PHE A 247 ? 1.3627 1.5154 0.7885 -0.0775 0.0674 -0.1249 247 PHE A N 1973 C CA . PHE A 247 ? 1.2967 1.4855 0.7596 -0.0791 0.0879 -0.1238 247 PHE A CA 1974 C C . PHE A 247 ? 1.2599 1.4807 0.7501 -0.0669 0.1026 -0.1390 247 PHE A C 1975 O O . PHE A 247 ? 1.2996 1.5203 0.7654 -0.0610 0.1135 -0.1523 247 PHE A O 1976 C CB . PHE A 247 ? 1.3310 1.5210 0.7638 -0.0928 0.1074 -0.1200 247 PHE A CB 1977 C CG . PHE A 247 ? 1.2962 1.5197 0.7630 -0.0986 0.1267 -0.1180 247 PHE A CG 1978 C CD1 . PHE A 247 ? 1.2481 1.4819 0.7582 -0.0976 0.1193 -0.1106 247 PHE A CD1 1979 C CD2 . PHE A 247 ? 1.3151 1.5591 0.7684 -0.1063 0.1524 -0.1230 247 PHE A CD2 1980 C CE1 . PHE A 247 ? 1.2317 1.4924 0.7677 -0.1046 0.1356 -0.1100 247 PHE A CE1 1981 C CE2 . PHE A 247 ? 1.2768 1.5507 0.7603 -0.1143 0.1679 -0.1209 247 PHE A CE2 1982 C CZ . PHE A 247 ? 1.2508 1.5313 0.7738 -0.1138 0.1587 -0.1150 247 PHE A CZ 1983 N N . ILE A 248 ? 1.2121 1.4591 0.7521 -0.0623 0.1027 -0.1364 248 ILE A N 1984 C CA . ILE A 248 ? 1.1734 1.4551 0.7443 -0.0517 0.1163 -0.1476 248 ILE A CA 1985 C C . ILE A 248 ? 1.1564 1.4704 0.7448 -0.0610 0.1367 -0.1452 248 ILE A C 1986 O O . ILE A 248 ? 1.1237 1.4485 0.7416 -0.0654 0.1336 -0.1371 248 ILE A O 1987 C CB . ILE A 248 ? 1.1352 1.4231 0.7475 -0.0409 0.1003 -0.1454 248 ILE A CB 1988 C CG1 . ILE A 248 ? 1.1560 1.4071 0.7531 -0.0376 0.0749 -0.1423 248 ILE A CG1 1989 C CG2 . ILE A 248 ? 1.1163 1.4337 0.7535 -0.0278 0.1116 -0.1570 248 ILE A CG2 1990 C CD1 . ILE A 248 ? 1.2063 1.4349 0.7639 -0.0320 0.0741 -0.1555 248 ILE A CD1 1991 N N . ALA A 249 ? 1.1825 1.5106 0.7507 -0.0650 0.1579 -0.1521 249 ALA A N 1992 C CA . ALA A 249 ? 1.1907 1.5448 0.7681 -0.0785 0.1764 -0.1483 249 ALA A CA 1993 C C . ALA A 249 ? 1.1559 1.5554 0.7797 -0.0736 0.1864 -0.1531 249 ALA A C 1994 O O . ALA A 249 ? 1.1469 1.5632 0.7874 -0.0585 0.1879 -0.1621 249 ALA A O 1995 C CB . ALA A 249 ? 1.2341 1.5884 0.7733 -0.0861 0.1958 -0.1518 249 ALA A CB 1996 N N . PRO A 250 ? 1.1537 1.5714 0.7975 -0.0867 0.1922 -0.1469 250 PRO A N 1997 C CA . PRO A 250 ? 1.1316 1.5946 0.8155 -0.0846 0.2016 -0.1512 250 PRO A CA 1998 C C . PRO A 250 ? 1.1510 1.6480 0.8349 -0.0840 0.2234 -0.1587 250 PRO A C 1999 O O . PRO A 250 ? 1.1958 1.6860 0.8498 -0.0942 0.2362 -0.1576 250 PRO A O 2000 C CB . PRO A 250 ? 1.1130 1.5794 0.8077 -0.1023 0.2025 -0.1433 250 PRO A CB 2001 C CG . PRO A 250 ? 1.1393 1.5664 0.7971 -0.1146 0.2000 -0.1352 250 PRO A CG 2002 C CD . PRO A 250 ? 1.1647 1.5591 0.7969 -0.1026 0.1873 -0.1356 250 PRO A CD 2003 N N . GLU A 251 ? 1.1324 1.6662 0.8500 -0.0713 0.2279 -0.1651 251 GLU A N 2004 C CA . GLU A 251 ? 1.1471 1.7246 0.8782 -0.0715 0.2495 -0.1700 251 GLU A CA 2005 C C . GLU A 251 ? 1.1171 1.7375 0.8897 -0.0808 0.2516 -0.1663 251 GLU A C 2006 O O . GLU A 251 ? 1.1054 1.7500 0.8818 -0.0981 0.2652 -0.1632 251 GLU A O 2007 C CB . GLU A 251 ? 1.1714 1.7597 0.9090 -0.0480 0.2545 -0.1801 251 GLU A CB 2008 C CG . GLU A 251 ? 1.2001 1.8228 0.9375 -0.0466 0.2804 -0.1852 251 GLU A CG 2009 C CD . GLU A 251 ? 1.2099 1.8541 0.9677 -0.0215 0.2872 -0.1949 251 GLU A CD 2010 O OE1 . GLU A 251 ? 1.2322 1.8557 0.9956 -0.0053 0.2709 -0.1984 251 GLU A OE1 2011 O OE2 . GLU A 251 ? 1.2198 1.9018 0.9894 -0.0178 0.3094 -0.1982 251 GLU A OE2 2012 N N . TYR A 252 ? 1.0813 1.7100 0.8830 -0.0705 0.2375 -0.1663 252 TYR A N 2013 C CA . TYR A 252 ? 1.0497 1.7157 0.8875 -0.0785 0.2357 -0.1631 252 TYR A CA 2014 C C . TYR A 252 ? 1.0418 1.6818 0.8776 -0.0878 0.2201 -0.1574 252 TYR A C 2015 O O . TYR A 252 ? 1.0134 1.6189 0.8391 -0.0782 0.2063 -0.1559 252 TYR A O 2016 C CB . TYR A 252 ? 1.0347 1.7344 0.9082 -0.0590 0.2328 -0.1663 252 TYR A CB 2017 C CG . TYR A 252 ? 1.0681 1.7986 0.9511 -0.0466 0.2496 -0.1721 252 TYR A CG 2018 C CD1 . TYR A 252 ? 1.0687 1.8513 0.9782 -0.0548 0.2640 -0.1707 252 TYR A CD1 2019 C CD2 . TYR A 252 ? 1.0827 1.7902 0.9488 -0.0264 0.2512 -0.1790 252 TYR A CD2 2020 C CE1 . TYR A 252 ? 1.0750 1.8888 0.9967 -0.0414 0.2815 -0.1753 252 TYR A CE1 2021 C CE2 . TYR A 252 ? 1.0956 1.8292 0.9691 -0.0127 0.2688 -0.1855 252 TYR A CE2 2022 C CZ . TYR A 252 ? 1.0973 1.8856 1.0002 -0.0193 0.2848 -0.1832 252 TYR A CZ 2023 O OH . TYR A 252 ? 1.1156 1.9328 1.0293 -0.0038 0.3043 -0.1889 252 TYR A OH 2024 N N . ALA A 253 ? 1.0317 1.6889 0.8778 -0.1066 0.2226 -0.1544 253 ALA A N 2025 C CA . ALA A 253 ? 0.9981 1.6357 0.8451 -0.1145 0.2104 -0.1507 253 ALA A CA 2026 C C . ALA A 253 ? 0.9743 1.6531 0.8520 -0.1209 0.2091 -0.1514 253 ALA A C 2027 O O . ALA A 253 ? 0.9802 1.7020 0.8773 -0.1245 0.2181 -0.1530 253 ALA A O 2028 C CB . ALA A 253 ? 1.0219 1.6263 0.8406 -0.1341 0.2135 -0.1468 253 ALA A CB 2029 N N . TYR A 254 ? 0.9636 1.6301 0.8456 -0.1221 0.1978 -0.1498 254 TYR A N 2030 C CA . TYR A 254 ? 0.9345 1.6356 0.8410 -0.1270 0.1934 -0.1505 254 TYR A CA 2031 C C . TYR A 254 ? 0.9323 1.6268 0.8287 -0.1518 0.1946 -0.1511 254 TYR A C 2032 O O . TYR A 254 ? 0.9211 1.5744 0.7964 -0.1570 0.1915 -0.1503 254 TYR A O 2033 C CB . TYR A 254 ? 0.9187 1.6115 0.8350 -0.1106 0.1804 -0.1486 254 TYR A CB 2034 C CG . TYR A 254 ? 0.9052 1.6043 0.8347 -0.0868 0.1765 -0.1477 254 TYR A CG 2035 C CD1 . TYR A 254 ? 0.8955 1.6371 0.8535 -0.0766 0.1756 -0.1477 254 TYR A CD1 2036 C CD2 . TYR A 254 ? 0.9164 1.5775 0.8302 -0.0746 0.1722 -0.1464 254 TYR A CD2 2037 C CE1 . TYR A 254 ? 0.8923 1.6349 0.8615 -0.0543 0.1720 -0.1472 254 TYR A CE1 2038 C CE2 . TYR A 254 ? 0.9193 1.5816 0.8431 -0.0543 0.1675 -0.1465 254 TYR A CE2 2039 C CZ . TYR A 254 ? 0.9106 1.6119 0.8616 -0.0438 0.1680 -0.1472 254 TYR A CZ 2040 O OH . TYR A 254 ? 0.9261 1.6242 0.8862 -0.0232 0.1634 -0.1476 254 TYR A OH 2041 N N . LYS A 255 ? 0.9348 1.6697 0.8475 -0.1670 0.1987 -0.1524 255 LYS A N 2042 C CA . LYS A 255 ? 0.9624 1.6932 0.8672 -0.1918 0.1972 -0.1542 255 LYS A CA 2043 C C . LYS A 255 ? 0.9415 1.6735 0.8521 -0.1877 0.1850 -0.1559 255 LYS A C 2044 O O . LYS A 255 ? 0.9082 1.6702 0.8409 -0.1725 0.1788 -0.1545 255 LYS A O 2045 C CB . LYS A 255 ? 0.9817 1.7590 0.9047 -0.2113 0.2035 -0.1542 255 LYS A CB 2046 C CG . LYS A 255 ? 1.0058 1.7865 0.9228 -0.2195 0.2184 -0.1517 255 LYS A CG 2047 C CD . LYS A 255 ? 1.0261 1.8492 0.9607 -0.2449 0.2244 -0.1503 255 LYS A CD 2048 C CE . LYS A 255 ? 1.0108 1.8983 0.9865 -0.2372 0.2218 -0.1491 255 LYS A CE 2049 N NZ . LYS A 255 ? 1.0292 1.9624 1.0264 -0.2630 0.2267 -0.1462 255 LYS A NZ 2050 N N . ILE A 256 ? 0.9664 1.6641 0.8553 -0.2009 0.1824 -0.1588 256 ILE A N 2051 C CA . ILE A 256 ? 0.9719 1.6677 0.8597 -0.2001 0.1731 -0.1616 256 ILE A CA 2052 C C . ILE A 256 ? 0.9740 1.6962 0.8647 -0.2253 0.1702 -0.1659 256 ILE A C 2053 O O . ILE A 256 ? 0.9840 1.6787 0.8531 -0.2462 0.1723 -0.1705 256 ILE A O 2054 C CB . ILE A 256 ? 1.0058 1.6457 0.8668 -0.1974 0.1730 -0.1632 256 ILE A CB 2055 C CG1 . ILE A 256 ? 1.0143 1.6304 0.8749 -0.1743 0.1735 -0.1574 256 ILE A CG1 2056 C CG2 . ILE A 256 ? 1.0105 1.6488 0.8673 -0.1964 0.1660 -0.1668 256 ILE A CG2 2057 C CD1 . ILE A 256 ? 1.0391 1.6021 0.8776 -0.1713 0.1747 -0.1565 256 ILE A CD1 2058 N N . VAL A 257 ? 0.9621 1.7367 0.8800 -0.2234 0.1644 -0.1640 257 VAL A N 2059 C CA . VAL A 257 ? 1.0010 1.8098 0.9272 -0.2484 0.1595 -0.1665 257 VAL A CA 2060 C C . VAL A 257 ? 1.0191 1.8218 0.9318 -0.2554 0.1479 -0.1714 257 VAL A C 2061 O O . VAL A 257 ? 1.0258 1.8232 0.9241 -0.2814 0.1443 -0.1773 257 VAL A O 2062 C CB . VAL A 257 ? 0.9920 1.8661 0.9575 -0.2454 0.1587 -0.1607 257 VAL A CB 2063 C CG1 . VAL A 257 ? 0.9924 1.8734 0.9660 -0.2459 0.1730 -0.1577 257 VAL A CG1 2064 C CG2 . VAL A 257 ? 0.9699 1.8680 0.9569 -0.2173 0.1519 -0.1558 257 VAL A CG2 2065 N N . LYS A 258 ? 1.0122 1.8137 0.9274 -0.2332 0.1421 -0.1689 258 LYS A N 2066 C CA . LYS A 258 ? 1.0398 1.8378 0.9404 -0.2372 0.1321 -0.1726 258 LYS A CA 2067 C C . LYS A 258 ? 1.0340 1.7837 0.9115 -0.2202 0.1355 -0.1740 258 LYS A C 2068 O O . LYS A 258 ? 0.9797 1.7280 0.8696 -0.1959 0.1368 -0.1672 258 LYS A O 2069 C CB . LYS A 258 ? 1.0382 1.8905 0.9668 -0.2280 0.1207 -0.1657 258 LYS A CB 2070 C CG . LYS A 258 ? 1.0888 1.9556 1.0049 -0.2453 0.1079 -0.1695 258 LYS A CG 2071 C CD . LYS A 258 ? 1.0939 2.0021 1.0313 -0.2296 0.0960 -0.1605 258 LYS A CD 2072 C CE . LYS A 258 ? 1.1214 2.0651 1.0581 -0.2512 0.0806 -0.1614 258 LYS A CE 2073 N NZ . LYS A 258 ? 1.1750 2.0789 1.0670 -0.2721 0.0785 -0.1736 258 LYS A NZ 2074 N N . LYS A 259 ? 1.0822 1.7919 0.9269 -0.2334 0.1373 -0.1827 259 LYS A N 2075 C CA . LYS A 259 ? 1.1071 1.7744 0.9306 -0.2184 0.1415 -0.1843 259 LYS A CA 2076 C C . LYS A 259 ? 1.1141 1.7881 0.9216 -0.2221 0.1342 -0.1885 259 LYS A C 2077 O O . LYS A 259 ? 1.1594 1.8389 0.9512 -0.2452 0.1285 -0.1965 259 LYS A O 2078 C CB . LYS A 259 ? 1.1625 1.7739 0.9585 -0.2272 0.1513 -0.1912 259 LYS A CB 2079 C CG . LYS A 259 ? 1.1847 1.7801 0.9903 -0.2193 0.1588 -0.1853 259 LYS A CG 2080 C CD . LYS A 259 ? 1.2246 1.7647 1.0032 -0.2287 0.1672 -0.1904 259 LYS A CD 2081 C CE . LYS A 259 ? 1.2313 1.7625 1.0168 -0.2288 0.1726 -0.1842 259 LYS A CE 2082 N NZ . LYS A 259 ? 1.2660 1.7450 1.0260 -0.2407 0.1795 -0.1874 259 LYS A NZ 2083 N N . GLY A 260 ? 1.1004 1.7734 0.9103 -0.2004 0.1339 -0.1826 260 GLY A N 2084 C CA . GLY A 260 ? 1.1071 1.7856 0.8986 -0.2020 0.1282 -0.1852 260 GLY A CA 2085 C C . GLY A 260 ? 1.0829 1.7557 0.8785 -0.1766 0.1312 -0.1765 260 GLY A C 2086 O O . GLY A 260 ? 1.0823 1.7356 0.8895 -0.1594 0.1387 -0.1707 260 GLY A O 2087 N N . ASP A 261 ? 1.0945 1.7851 0.8803 -0.1756 0.1245 -0.1746 261 ASP A N 2088 C CA . ASP A 261 ? 1.0861 1.7723 0.8729 -0.1541 0.1280 -0.1654 261 ASP A CA 2089 C C . ASP A 261 ? 1.0101 1.7301 0.8361 -0.1361 0.1212 -0.1499 261 ASP A C 2090 O O . ASP A 261 ? 0.9965 1.7574 0.8412 -0.1399 0.1096 -0.1451 261 ASP A O 2091 C CB . ASP A 261 ? 1.1388 1.8312 0.8965 -0.1605 0.1236 -0.1682 261 ASP A CB 2092 C CG . ASP A 261 ? 1.2211 1.8676 0.9347 -0.1706 0.1346 -0.1836 261 ASP A CG 2093 O OD1 . ASP A 261 ? 1.2461 1.8539 0.9558 -0.1662 0.1472 -0.1886 261 ASP A OD1 2094 O OD2 . ASP A 261 ? 1.2829 1.9306 0.9645 -0.1824 0.1303 -0.1905 261 ASP A OD2 2095 N N . SER A 262 ? 0.9582 1.6601 0.7973 -0.1164 0.1283 -0.1420 262 SER A N 2096 C CA . SER A 262 ? 0.9379 1.6630 0.8115 -0.0987 0.1223 -0.1281 262 SER A CA 2097 C C . SER A 262 ? 0.9266 1.6282 0.8045 -0.0802 0.1294 -0.1192 262 SER A C 2098 O O . SER A 262 ? 0.9838 1.6556 0.8402 -0.0803 0.1397 -0.1236 262 SER A O 2099 C CB . SER A 262 ? 0.9289 1.6598 0.8240 -0.0994 0.1215 -0.1296 262 SER A CB 2100 O OG . SER A 262 ? 0.9079 1.6609 0.8339 -0.0830 0.1151 -0.1183 262 SER A OG 2101 N N . THR A 263 ? 1.1762 1.1782 0.8909 -0.1239 0.0823 -0.1348 263 THR A N 2102 C CA . THR A 263 ? 1.1061 1.1067 0.8517 -0.0727 0.0721 -0.1300 263 THR A CA 2103 C C . THR A 263 ? 1.0081 1.0922 0.8301 -0.0593 0.0676 -0.1429 263 THR A C 2104 O O . THR A 263 ? 0.9656 1.1136 0.8323 -0.0783 0.0694 -0.1548 263 THR A O 2105 C CB . THR A 263 ? 1.0785 1.0735 0.8537 -0.0496 0.0654 -0.1254 263 THR A CB 2106 O OG1 . THR A 263 ? 1.0497 1.0448 0.8415 -0.0056 0.0573 -0.1224 263 THR A OG1 2107 C CG2 . THR A 263 ? 1.0184 1.0889 0.8726 -0.0565 0.0629 -0.1365 263 THR A CG2 2108 N N . ILE A 264 ? 0.9875 1.0731 0.8188 -0.0254 0.0621 -0.1418 264 ILE A N 2109 C CA . ILE A 264 ? 0.9182 1.0742 0.8174 -0.0120 0.0586 -0.1549 264 ILE A CA 2110 C C . ILE A 264 ? 0.8834 1.0590 0.8321 0.0122 0.0526 -0.1576 264 ILE A C 2111 O O . ILE A 264 ? 0.9129 1.0650 0.8452 0.0360 0.0485 -0.1513 264 ILE A O 2112 C CB . ILE A 264 ? 0.9183 1.0750 0.7960 0.0033 0.0580 -0.1556 264 ILE A CB 2113 C CG1 . ILE A 264 ? 0.9815 1.0989 0.7916 -0.0223 0.0654 -0.1502 264 ILE A CG1 2114 C CG2 . ILE A 264 ? 0.8568 1.0849 0.8006 0.0089 0.0564 -0.1715 264 ILE A CG2 2115 C CD1 . ILE A 264 ? 1.0076 1.1187 0.7859 -0.0054 0.0652 -0.1492 264 ILE A CD1 2116 N N . MET A 265 ? 0.8506 1.0696 0.8538 0.0072 0.0528 -0.1678 265 MET A N 2117 C CA . MET A 265 ? 0.8285 1.0549 0.8691 0.0226 0.0498 -0.1703 265 MET A CA 2118 C C . MET A 265 ? 0.8118 1.0750 0.8909 0.0326 0.0505 -0.1841 265 MET A C 2119 O O . MET A 265 ? 0.8333 1.1265 0.9298 0.0265 0.0533 -0.1942 265 MET A O 2120 C CB . MET A 265 ? 0.8215 1.0584 0.8799 0.0121 0.0510 -0.1716 265 MET A CB 2121 C CG . MET A 265 ? 0.8103 1.0372 0.8909 0.0254 0.0487 -0.1699 265 MET A CG 2122 S SD . MET A 265 ? 0.8247 1.0703 0.9152 0.0160 0.0496 -0.1707 265 MET A SD 2123 C CE . MET A 265 ? 0.8559 1.0578 0.8966 -0.0044 0.0500 -0.1566 265 MET A CE 2124 N N . LYS A 266 ? 0.8289 1.0920 0.9165 0.0459 0.0489 -0.1864 266 LYS A N 2125 C CA . LYS A 266 ? 0.8385 1.1320 0.9531 0.0474 0.0520 -0.2018 266 LYS A CA 2126 C C . LYS A 266 ? 0.8358 1.1199 0.9729 0.0457 0.0558 -0.2083 266 LYS A C 2127 O O . LYS A 266 ? 0.8473 1.1111 0.9838 0.0488 0.0548 -0.2028 266 LYS A O 2128 C CB . LYS A 266 ? 0.8783 1.1897 0.9861 0.0573 0.0501 -0.2050 266 LYS A CB 2129 C CG . LYS A 266 ? 0.9381 1.2440 1.0071 0.0716 0.0452 -0.1947 266 LYS A CG 2130 C CD . LYS A 266 ? 0.9872 1.2983 1.0420 0.0656 0.0467 -0.1952 266 LYS A CD 2131 C CE . LYS A 266 ? 1.0027 1.3634 1.0826 0.0631 0.0495 -0.2122 266 LYS A CE 2132 N NZ . LYS A 266 ? 1.0437 1.4408 1.1184 0.0796 0.0468 -0.2185 266 LYS A NZ 2133 N N . SER A 267 ? 0.8481 1.1417 0.9980 0.0435 0.0605 -0.2197 267 SER A N 2134 C CA . SER A 267 ? 0.8612 1.1320 1.0166 0.0487 0.0650 -0.2254 267 SER A CA 2135 C C . SER A 267 ? 0.8910 1.1665 1.0476 0.0512 0.0714 -0.2409 267 SER A C 2136 O O . SER A 267 ? 0.9180 1.2238 1.0791 0.0505 0.0704 -0.2450 267 SER A O 2137 C CB . SER A 267 ? 0.8617 1.1261 1.0165 0.0563 0.0614 -0.2155 267 SER A CB 2138 O OG . SER A 267 ? 0.8914 1.1331 1.0440 0.0698 0.0652 -0.2205 267 SER A OG 2139 N N . GLU A 268 ? 0.9245 1.1629 1.0693 0.0537 0.0789 -0.2496 268 GLU A N 2140 C CA . GLU A 268 ? 0.9436 1.1664 1.0745 0.0596 0.0867 -0.2647 268 GLU A CA 2141 C C . GLU A 268 ? 0.9676 1.1745 1.0869 0.0876 0.0861 -0.2637 268 GLU A C 2142 O O . GLU A 268 ? 1.0419 1.2341 1.1426 0.1027 0.0915 -0.2755 268 GLU A O 2143 C CB . GLU A 268 ? 0.9827 1.1605 1.0892 0.0433 0.0985 -0.2770 268 GLU A CB 2144 C CG . GLU A 268 ? 0.9597 1.1698 1.0775 0.0170 0.0992 -0.2811 268 GLU A CG 2145 C CD . GLU A 268 ? 0.9524 1.2200 1.0887 0.0126 0.0950 -0.2856 268 GLU A CD 2146 O OE1 . GLU A 268 ? 0.8953 1.1644 1.0261 0.0133 0.0997 -0.2972 268 GLU A OE1 2147 O OE2 . GLU A 268 ? 0.9263 1.2339 1.0769 0.0115 0.0872 -0.2774 268 GLU A OE2 2148 N N . LEU A 269 ? 0.9565 1.1701 1.0833 0.0973 0.0796 -0.2509 269 LEU A N 2149 C CA . LEU A 269 ? 0.9854 1.1997 1.1018 0.1277 0.0778 -0.2507 269 LEU A CA 2150 C C . LEU A 269 ? 0.9777 1.2596 1.1092 0.1364 0.0730 -0.2559 269 LEU A C 2151 O O . LEU A 269 ? 0.9292 1.2520 1.0796 0.1141 0.0699 -0.2542 269 LEU A O 2152 C CB . LEU A 269 ? 0.9761 1.1880 1.0979 0.1309 0.0724 -0.2369 269 LEU A CB 2153 C CG . LEU A 269 ? 0.9901 1.1396 1.0956 0.1244 0.0770 -0.2316 269 LEU A CG 2154 C CD1 . LEU A 269 ? 0.9726 1.1320 1.0911 0.1212 0.0701 -0.2170 269 LEU A CD1 2155 C CD2 . LEU A 269 ? 1.0634 1.1481 1.1265 0.1490 0.0856 -0.2386 269 LEU A CD2 2156 N N . GLU A 270 ? 1.0529 1.3464 1.1699 0.1709 0.0730 -0.2628 270 GLU A N 2157 C CA . GLU A 270 ? 1.0645 1.4373 1.1944 0.1825 0.0686 -0.2710 270 GLU A CA 2158 C C . GLU A 270 ? 1.0053 1.4328 1.1451 0.1914 0.0621 -0.2660 270 GLU A C 2159 O O . GLU A 270 ? 1.0174 1.4141 1.1546 0.1897 0.0607 -0.2550 270 GLU A O 2160 C CB . GLU A 270 ? 1.1690 1.5302 1.2709 0.2211 0.0731 -0.2864 270 GLU A CB 2161 C CG . GLU A 270 ? 1.2555 1.5537 1.3378 0.2108 0.0820 -0.2942 270 GLU A CG 2162 C CD . GLU A 270 ? 1.2710 1.6201 1.3799 0.1837 0.0811 -0.3001 270 GLU A CD 2163 O OE1 . GLU A 270 ? 1.2450 1.6329 1.3837 0.1514 0.0763 -0.2909 270 GLU A OE1 2164 O OE2 . GLU A 270 ? 1.3032 1.6468 1.3962 0.1964 0.0859 -0.3139 270 GLU A OE2 2165 N N . TYR A 271 ? 0.9524 1.4679 1.1030 0.1984 0.0588 -0.2758 271 TYR A N 2166 C CA . TYR A 271 ? 0.9114 1.5015 1.0719 0.1994 0.0537 -0.2757 271 TYR A CA 2167 C C . TYR A 271 ? 0.9439 1.5225 1.0841 0.2495 0.0518 -0.2770 271 TYR A C 2168 O O . TYR A 271 ? 0.9594 1.5137 1.0723 0.2964 0.0538 -0.2858 271 TYR A O 2169 C CB . TYR A 271 ? 0.8922 1.5913 1.0653 0.1935 0.0522 -0.2908 271 TYR A CB 2170 C CG . TYR A 271 ? 0.8610 1.6559 1.0438 0.1802 0.0490 -0.2951 271 TYR A CG 2171 C CD1 . TYR A 271 ? 0.8235 1.6084 1.0100 0.1335 0.0496 -0.2831 271 TYR A CD1 2172 C CD2 . TYR A 271 ? 0.8519 1.7528 1.0355 0.2140 0.0460 -0.3132 271 TYR A CD2 2173 C CE1 . TYR A 271 ? 0.8120 1.6843 1.0018 0.1134 0.0488 -0.2896 271 TYR A CE1 2174 C CE2 . TYR A 271 ? 0.8274 1.8325 1.0200 0.1963 0.0441 -0.3209 271 TYR A CE2 2175 C CZ . TYR A 271 ? 0.8109 1.7991 1.0061 0.1420 0.0463 -0.3093 271 TYR A CZ 2176 O OH . TYR A 271 ? 0.7854 1.8762 0.9840 0.1170 0.0464 -0.3192 271 TYR A OH 2177 N N . GLY A 272 ? 0.9496 1.5406 1.0958 0.2414 0.0486 -0.2682 272 GLY A N 2178 C CA . GLY A 272 ? 0.9974 1.5713 1.1218 0.2881 0.0466 -0.2668 272 GLY A CA 2179 C C . GLY A 272 ? 1.0217 1.7086 1.1464 0.3238 0.0412 -0.2805 272 GLY A C 2180 O O . GLY A 272 ? 1.0355 1.7124 1.1352 0.3740 0.0390 -0.2806 272 GLY A O 2181 N N . ASN A 273 ? 1.0149 1.8127 1.1633 0.2990 0.0396 -0.2930 273 ASN A N 2182 C CA . ASN A 273 ? 1.0355 1.9719 1.1905 0.3202 0.0348 -0.3096 273 ASN A CA 2183 C C . ASN A 273 ? 0.9990 1.9522 1.1580 0.3112 0.0321 -0.3020 273 ASN A C 2184 O O . ASN A 273 ? 1.0107 1.9761 1.1516 0.3660 0.0282 -0.3040 273 ASN A O 2185 C CB . ASN A 273 ? 1.0957 2.0609 1.2220 0.4011 0.0320 -0.3240 273 ASN A CB 2186 C CG . ASN A 273 ? 1.1404 2.1036 1.2620 0.4094 0.0348 -0.3346 273 ASN A CG 2187 O OD1 . ASN A 273 ? 1.2012 2.0521 1.2934 0.4349 0.0388 -0.3295 273 ASN A OD1 2188 N ND2 . ASN A 273 ? 1.1155 2.2037 1.2626 0.3835 0.0338 -0.3506 273 ASN A ND2 2189 N N . CYS A 274 ? 0.9567 1.9065 1.1330 0.2433 0.0347 -0.2935 274 CYS A N 2190 C CA . CYS A 274 ? 0.9554 1.8565 1.1303 0.2271 0.0340 -0.2787 274 CYS A CA 2191 C C . CYS A 274 ? 0.8595 1.7959 1.0436 0.1535 0.0375 -0.2770 274 CYS A C 2192 O O . CYS A 274 ? 0.8503 1.8027 1.0357 0.1090 0.0421 -0.2810 274 CYS A O 2193 C CB . CYS A 274 ? 1.0133 1.7665 1.1771 0.2322 0.0361 -0.2596 274 CYS A CB 2194 S SG . CYS A 274 ? 1.1247 1.8011 1.2869 0.2088 0.0358 -0.2395 274 CYS A SG 2195 N N . ASN A 275 ? 0.8132 1.7526 0.9954 0.1402 0.0366 -0.2710 275 ASN A N 2196 C CA . ASN A 275 ? 0.8076 1.7537 0.9834 0.0687 0.0420 -0.2680 275 ASN A CA 2197 C C . ASN A 275 ? 0.8187 1.6689 0.9857 0.0583 0.0415 -0.2484 275 ASN A C 2198 O O . ASN A 275 ? 0.8509 1.6850 1.0217 0.1010 0.0365 -0.2432 275 ASN A O 2199 C CB . ASN A 275 ? 0.7895 1.8843 0.9675 0.0447 0.0438 -0.2899 275 ASN A CB 2200 C CG . ASN A 275 ? 0.7775 1.8737 0.9335 -0.0395 0.0532 -0.2907 275 ASN A CG 2201 O OD1 . ASN A 275 ? 0.7851 1.8123 0.9221 -0.0810 0.0593 -0.2831 275 ASN A OD1 2202 N ND2 . ASN A 275 ? 0.7881 1.9594 0.9387 -0.0647 0.0553 -0.3005 275 ASN A ND2 2203 N N . THR A 276 ? 0.8205 1.6045 0.9692 0.0042 0.0469 -0.2377 276 THR A N 2204 C CA . THR A 276 ? 0.7957 1.4843 0.9319 -0.0051 0.0465 -0.2191 276 THR A CA 2205 C C . THR A 276 ? 0.8173 1.4709 0.9179 -0.0701 0.0542 -0.2149 276 THR A C 2206 O O . THR A 276 ? 0.8460 1.5259 0.9286 -0.1082 0.0607 -0.2234 276 THR A O 2207 C CB . THR A 276 ? 0.7953 1.3774 0.9363 0.0255 0.0435 -0.2034 276 THR A CB 2208 O OG1 . THR A 276 ? 0.8146 1.3241 0.9483 0.0268 0.0418 -0.1881 276 THR A OG1 2209 C CG2 . THR A 276 ? 0.8061 1.3412 0.9340 -0.0008 0.0474 -0.1996 276 THR A CG2 2210 N N . LYS A 277 ? 0.8483 1.4349 0.9311 -0.0817 0.0545 -0.2018 277 LYS A N 2211 C CA . LYS A 277 ? 0.9178 1.4387 0.9500 -0.1359 0.0625 -0.1948 277 LYS A CA 2212 C C . LYS A 277 ? 0.9090 1.3095 0.9227 -0.1230 0.0608 -0.1754 277 LYS A C 2213 O O . LYS A 277 ? 0.9445 1.2729 0.9057 -0.1561 0.0669 -0.1676 277 LYS A O 2214 C CB . LYS A 277 ? 0.9772 1.5080 0.9908 -0.1613 0.0652 -0.1957 277 LYS A CB 2215 C CG . LYS A 277 ? 1.0290 1.6808 1.0390 -0.2000 0.0714 -0.2182 277 LYS A CG 2216 C CD . LYS A 277 ? 1.0920 1.7330 1.0663 -0.2427 0.0778 -0.2192 277 LYS A CD 2217 C CE . LYS A 277 ? 1.1287 1.9037 1.0967 -0.2898 0.0857 -0.2453 277 LYS A CE 2218 N NZ . LYS A 277 ? 1.1815 1.9794 1.1122 -0.3472 0.0977 -0.2585 277 LYS A NZ 2219 N N . CYS A 278 ? 0.8664 1.2454 0.9158 -0.0746 0.0532 -0.1689 278 CYS A N 2220 C CA . CYS A 278 ? 0.8750 1.1628 0.9129 -0.0595 0.0510 -0.1540 278 CYS A CA 2221 C C . CYS A 278 ? 0.8097 1.1025 0.8829 -0.0225 0.0468 -0.1559 278 CYS A C 2222 O O . CYS A 278 ? 0.7849 1.1035 0.8888 0.0089 0.0433 -0.1595 278 CYS A O 2223 C CB . CYS A 278 ? 0.8972 1.1368 0.9311 -0.0476 0.0476 -0.1425 278 CYS A CB 2224 S SG . CYS A 278 ? 0.9281 1.0821 0.9555 -0.0213 0.0435 -0.1279 278 CYS A SG 2225 N N . GLN A 279 ? 0.7947 1.0577 0.8558 -0.0265 0.0483 -0.1540 279 GLN A N 2226 C CA . GLN A 279 ? 0.7631 1.0346 0.8524 0.0001 0.0464 -0.1589 279 GLN A CA 2227 C C . GLN A 279 ? 0.7552 0.9679 0.8380 0.0121 0.0447 -0.1501 279 GLN A C 2228 O O . GLN A 279 ? 0.7750 0.9469 0.8233 -0.0005 0.0454 -0.1421 279 GLN A O 2229 C CB . GLN A 279 ? 0.7564 1.0715 0.8443 -0.0142 0.0497 -0.1695 279 GLN A CB 2230 C CG . GLN A 279 ? 0.7389 1.0692 0.8543 0.0127 0.0486 -0.1773 279 GLN A CG 2231 C CD . GLN A 279 ? 0.7327 1.1050 0.8725 0.0423 0.0469 -0.1866 279 GLN A CD 2232 O OE1 . GLN A 279 ? 0.7519 1.1907 0.8958 0.0398 0.0471 -0.1960 279 GLN A OE1 2233 N NE2 . GLN A 279 ? 0.7244 1.0589 0.8733 0.0710 0.0462 -0.1853 279 GLN A NE2 2234 N N . THR A 280 ? 0.7393 0.9488 0.8480 0.0368 0.0433 -0.1533 280 THR A N 2235 C CA . THR A 280 ? 0.7414 0.9196 0.8492 0.0453 0.0428 -0.1510 280 THR A CA 2236 C C . THR A 280 ? 0.7492 0.9475 0.8744 0.0533 0.0455 -0.1627 280 THR A C 2237 O O . THR A 280 ? 0.7397 0.9654 0.8773 0.0608 0.0472 -0.1711 280 THR A O 2238 C CB . THR A 280 ? 0.7309 0.8814 0.8458 0.0583 0.0414 -0.1463 280 THR A CB 2239 O OG1 . THR A 280 ? 0.7029 0.8557 0.8353 0.0718 0.0446 -0.1545 280 THR A OG1 2240 C CG2 . THR A 280 ? 0.7454 0.8854 0.8517 0.0550 0.0392 -0.1377 280 THR A CG2 2241 N N . PRO A 281 ? 0.7677 0.9562 0.8908 0.0542 0.0461 -0.1645 281 PRO A N 2242 C CA . PRO A 281 ? 0.7717 0.9756 0.9077 0.0578 0.0499 -0.1771 281 PRO A CA 2243 C C . PRO A 281 ? 0.7974 0.9861 0.9420 0.0686 0.0545 -0.1849 281 PRO A C 2244 O O . PRO A 281 ? 0.8047 0.9975 0.9511 0.0718 0.0593 -0.1964 281 PRO A O 2245 C CB . PRO A 281 ? 0.7792 0.9814 0.9084 0.0559 0.0492 -0.1775 281 PRO A CB 2246 C CG . PRO A 281 ? 0.7858 0.9714 0.8903 0.0558 0.0444 -0.1643 281 PRO A CG 2247 C CD . PRO A 281 ? 0.7778 0.9458 0.8797 0.0534 0.0431 -0.1562 281 PRO A CD 2248 N N . MET A 282 ? 0.8414 1.0047 0.9832 0.0740 0.0541 -0.1787 282 MET A N 2249 C CA . MET A 282 ? 0.8846 1.0163 1.0192 0.0850 0.0599 -0.1841 282 MET A CA 2250 C C . MET A 282 ? 0.8680 1.0038 0.9991 0.1056 0.0585 -0.1828 282 MET A C 2251 O O . MET A 282 ? 0.9076 1.0119 1.0209 0.1235 0.0638 -0.1880 282 MET A O 2252 C CB . MET A 282 ? 0.9459 1.0476 1.0745 0.0791 0.0613 -0.1790 282 MET A CB 2253 C CG . MET A 282 ? 1.0121 1.1169 1.1392 0.0620 0.0656 -0.1871 282 MET A CG 2254 S SD . MET A 282 ? 1.1474 1.2386 1.2700 0.0535 0.0660 -0.1822 282 MET A SD 2255 C CE . MET A 282 ? 1.1416 1.1764 1.2451 0.0634 0.0716 -0.1787 282 MET A CE 2256 N N . GLY A 283 ? 0.8128 0.9861 0.9531 0.1033 0.0524 -0.1769 283 GLY A N 2257 C CA . GLY A 283 ? 0.8044 1.0041 0.9441 0.1219 0.0503 -0.1778 283 GLY A CA 2258 C C . GLY A 283 ? 0.7836 1.0107 0.9280 0.1067 0.0453 -0.1694 283 GLY A C 2259 O O . GLY A 283 ? 0.7707 0.9778 0.9115 0.0865 0.0439 -0.1609 283 GLY A O 2260 N N . ALA A 284 ? 0.7739 1.0474 0.9204 0.1177 0.0432 -0.1731 284 ALA A N 2261 C CA . ALA A 284 ? 0.7710 1.0791 0.9170 0.0958 0.0406 -0.1691 284 ALA A CA 2262 C C . ALA A 284 ? 0.8025 1.0875 0.9456 0.1044 0.0384 -0.1603 284 ALA A C 2263 O O . ALA A 284 ? 0.8117 1.0622 0.9522 0.1317 0.0389 -0.1583 284 ALA A O 2264 C CB . ALA A 284 ? 0.7658 1.1585 0.9168 0.0962 0.0403 -0.1818 284 ALA A CB 2265 N N . ILE A 285 ? 0.8154 1.1144 0.9520 0.0786 0.0373 -0.1556 285 ILE A N 2266 C CA . ILE A 285 ? 0.8497 1.1269 0.9826 0.0813 0.0351 -0.1468 285 ILE A CA 2267 C C . ILE A 285 ? 0.8855 1.2284 1.0169 0.0694 0.0345 -0.1526 285 ILE A C 2268 O O . ILE A 285 ? 0.9251 1.3018 1.0449 0.0342 0.0374 -0.1580 285 ILE A O 2269 C CB . ILE A 285 ? 0.8469 1.0627 0.9646 0.0601 0.0351 -0.1347 285 ILE A CB 2270 C CG1 . ILE A 285 ? 0.8315 0.9972 0.9541 0.0760 0.0353 -0.1307 285 ILE A CG1 2271 C CG2 . ILE A 285 ? 0.8464 1.0503 0.9559 0.0546 0.0333 -0.1272 285 ILE A CG2 2272 C CD1 . ILE A 285 ? 0.8313 0.9555 0.9377 0.0624 0.0346 -0.1227 285 ILE A CD1 2273 N N . ASN A 286 ? 0.9300 1.2907 1.0679 0.0970 0.0317 -0.1525 286 ASN A N 2274 C CA . ASN A 286 ? 0.9786 1.4095 1.1164 0.0888 0.0306 -0.1590 286 ASN A CA 2275 C C . ASN A 286 ? 0.9320 1.3218 1.0662 0.0959 0.0283 -0.1475 286 ASN A C 2276 O O . ASN A 286 ? 0.9007 1.2819 1.0381 0.1353 0.0257 -0.1449 286 ASN A O 2277 C CB . ASN A 286 ? 1.0605 1.5751 1.2081 0.1268 0.0282 -0.1730 286 ASN A CB 2278 C CG . ASN A 286 ? 1.1982 1.8060 1.3480 0.1232 0.0266 -0.1827 286 ASN A CG 2279 O OD1 . ASN A 286 ? 1.1813 1.8172 1.3244 0.0738 0.0299 -0.1860 286 ASN A OD1 2280 N ND2 . ASN A 286 ? 1.4097 2.0645 1.5616 0.1766 0.0222 -0.1886 286 ASN A ND2 2281 N N . SER A 287 ? 0.9113 1.2674 1.0310 0.0588 0.0300 -0.1405 287 SER A N 2282 C CA . SER A 287 ? 0.9035 1.2102 1.0184 0.0636 0.0280 -0.1287 287 SER A CA 2283 C C . SER A 287 ? 0.9033 1.2051 0.9943 0.0211 0.0308 -0.1273 287 SER A C 2284 O O . SER A 287 ? 0.9197 1.2150 0.9868 -0.0152 0.0357 -0.1308 287 SER A O 2285 C CB . SER A 287 ? 0.9001 1.1234 1.0138 0.0751 0.0275 -0.1172 287 SER A CB 2286 O OG . SER A 287 ? 0.8771 1.0604 0.9892 0.0855 0.0254 -0.1072 287 SER A OG 2287 N N . SER A 288 ? 0.9149 1.2127 1.0047 0.0251 0.0288 -0.1226 288 SER A N 2288 C CA . SER A 288 ? 0.9477 1.2228 1.0067 -0.0138 0.0323 -0.1204 288 SER A CA 2289 C C . SER A 288 ? 0.9220 1.1038 0.9656 -0.0068 0.0305 -0.1047 288 SER A C 2290 O O . SER A 288 ? 0.9325 1.0780 0.9439 -0.0306 0.0330 -0.1009 288 SER A O 2291 C CB . SER A 288 ? 0.9817 1.3284 1.0474 -0.0179 0.0318 -0.1285 288 SER A CB 2292 O OG . SER A 288 ? 0.9979 1.3533 1.0906 0.0298 0.0254 -0.1231 288 SER A OG 2293 N N . MET A 289 ? 0.8881 1.0341 0.9500 0.0244 0.0269 -0.0975 289 MET A N 2294 C CA . MET A 289 ? 0.9039 0.9810 0.9553 0.0340 0.0248 -0.0858 289 MET A CA 2295 C C . MET A 289 ? 0.9186 0.9440 0.9294 0.0141 0.0275 -0.0825 289 MET A C 2296 O O . MET A 289 ? 0.9448 0.9775 0.9453 0.0010 0.0306 -0.0877 289 MET A O 2297 C CB . MET A 289 ? 0.9183 0.9814 0.9948 0.0639 0.0226 -0.0833 289 MET A CB 2298 C CG . MET A 289 ? 0.9275 1.0164 1.0271 0.0899 0.0216 -0.0851 289 MET A CG 2299 S SD . MET A 289 ? 0.9507 1.0218 1.0495 0.0999 0.0191 -0.0765 289 MET A SD 2300 C CE . MET A 289 ? 0.9273 0.9867 1.0354 0.1346 0.0208 -0.0765 289 MET A CE 2301 N N . PRO A 290 ? 0.9293 0.8995 0.9111 0.0157 0.0263 -0.0739 290 PRO A N 2302 C CA . PRO A 290 ? 0.9569 0.8665 0.8867 0.0082 0.0286 -0.0698 290 PRO A CA 2303 C C . PRO A 290 ? 0.9392 0.8384 0.8789 0.0330 0.0255 -0.0680 290 PRO A C 2304 O O . PRO A 290 ? 1.0058 0.8655 0.9023 0.0310 0.0275 -0.0662 290 PRO A O 2305 C CB . PRO A 290 ? 0.9759 0.8346 0.8706 0.0121 0.0275 -0.0620 290 PRO A CB 2306 C CG . PRO A 290 ? 0.9435 0.8374 0.8886 0.0323 0.0222 -0.0603 290 PRO A CG 2307 C CD . PRO A 290 ? 0.9093 0.8687 0.8960 0.0259 0.0232 -0.0681 290 PRO A CD 2308 N N . PHE A 291 ? 0.8699 0.8013 0.8581 0.0544 0.0219 -0.0695 291 PHE A N 2309 C CA . PHE A 291 ? 0.8490 0.7826 0.8487 0.0723 0.0202 -0.0712 291 PHE A CA 2310 C C . PHE A 291 ? 0.7903 0.7642 0.8320 0.0749 0.0219 -0.0789 291 PHE A C 2311 O O . PHE A 291 ? 0.7712 0.7679 0.8350 0.0746 0.0228 -0.0810 291 PHE A O 2312 C CB . PHE A 291 ? 0.8661 0.7928 0.8721 0.0924 0.0166 -0.0680 291 PHE A CB 2313 C CG . PHE A 291 ? 0.9152 0.8004 0.8749 0.1019 0.0139 -0.0612 291 PHE A CG 2314 C CD1 . PHE A 291 ? 0.9758 0.8362 0.8949 0.1158 0.0128 -0.0603 291 PHE A CD1 2315 C CD2 . PHE A 291 ? 0.9508 0.8188 0.9018 0.1020 0.0125 -0.0559 291 PHE A CD2 2316 C CE1 . PHE A 291 ? 1.0319 0.8446 0.8952 0.1334 0.0104 -0.0539 291 PHE A CE1 2317 C CE2 . PHE A 291 ? 1.0038 0.8263 0.9042 0.1148 0.0104 -0.0501 291 PHE A CE2 2318 C CZ . PHE A 291 ? 1.0464 0.8379 0.8995 0.1325 0.0095 -0.0491 291 PHE A CZ 2319 N N . HIS A 292 ? 0.7695 0.7501 0.8160 0.0809 0.0225 -0.0835 292 HIS A N 2320 C CA . HIS A 292 ? 0.7304 0.7367 0.8084 0.0847 0.0253 -0.0916 292 HIS A CA 2321 C C . HIS A 292 ? 0.7137 0.7254 0.7945 0.0914 0.0257 -0.0965 292 HIS A C 2322 O O . HIS A 292 ? 0.7067 0.7112 0.7657 0.0983 0.0225 -0.0939 292 HIS A O 2323 C CB . HIS A 292 ? 0.7468 0.7752 0.8299 0.0762 0.0276 -0.0975 292 HIS A CB 2324 C CG . HIS A 292 ? 0.7532 0.7787 0.8176 0.0693 0.0280 -0.0991 292 HIS A CG 2325 N ND1 . HIS A 292 ? 0.7388 0.7776 0.8143 0.0741 0.0294 -0.1061 292 HIS A ND1 2326 C CD2 . HIS A 292 ? 0.7853 0.7902 0.8129 0.0570 0.0283 -0.0950 292 HIS A CD2 2327 C CE1 . HIS A 292 ? 0.7608 0.7926 0.8116 0.0691 0.0293 -0.1053 292 HIS A CE1 2328 N NE2 . HIS A 292 ? 0.7989 0.8043 0.8162 0.0586 0.0291 -0.0982 292 HIS A NE2 2329 N N . ASN A 293 ? 0.6857 0.7096 0.7862 0.0904 0.0303 -0.1049 293 ASN A N 2330 C CA . ASN A 293 ? 0.6831 0.7243 0.7872 0.0889 0.0327 -0.1139 293 ASN A CA 2331 C C . ASN A 293 ? 0.7022 0.7542 0.8156 0.0820 0.0384 -0.1246 293 ASN A C 2332 O O . ASN A 293 ? 0.7101 0.7732 0.8266 0.0736 0.0440 -0.1352 293 ASN A O 2333 C CB . ASN A 293 ? 0.6819 0.7221 0.7896 0.0855 0.0359 -0.1165 293 ASN A CB 2334 C CG . ASN A 293 ? 0.6897 0.7047 0.7997 0.0788 0.0436 -0.1195 293 ASN A CG 2335 O OD1 . ASN A 293 ? 0.6979 0.7006 0.8086 0.0839 0.0449 -0.1189 293 ASN A OD1 2336 N ND2 . ASN A 293 ? 0.7082 0.7145 0.8124 0.0689 0.0494 -0.1236 293 ASN A ND2 2337 N N . ILE A 294 ? 0.7197 0.7720 0.8345 0.0828 0.0378 -0.1236 294 ILE A N 2338 C CA . ILE A 294 ? 0.7456 0.8075 0.8671 0.0799 0.0427 -0.1336 294 ILE A CA 2339 C C . ILE A 294 ? 0.7425 0.8276 0.8630 0.0754 0.0425 -0.1402 294 ILE A C 2340 O O . ILE A 294 ? 0.7514 0.8457 0.8759 0.0683 0.0482 -0.1516 294 ILE A O 2341 C CB . ILE A 294 ? 0.7581 0.8288 0.8820 0.0838 0.0414 -0.1322 294 ILE A CB 2342 C CG1 . ILE A 294 ? 0.7605 0.8221 0.8844 0.0930 0.0405 -0.1268 294 ILE A CG1 2343 C CG2 . ILE A 294 ? 0.7730 0.8533 0.9014 0.0858 0.0462 -0.1433 294 ILE A CG2 2344 C CD1 . ILE A 294 ? 0.7839 0.8143 0.9021 0.1014 0.0458 -0.1288 294 ILE A CD1 2345 N N . HIS A 295 ? 0.7381 0.8285 0.8461 0.0785 0.0371 -0.1338 295 HIS A N 2346 C CA . HIS A 295 ? 0.7406 0.8507 0.8403 0.0802 0.0361 -0.1385 295 HIS A CA 2347 C C . HIS A 295 ? 0.7587 0.8495 0.8240 0.0881 0.0308 -0.1273 295 HIS A C 2348 O O . HIS A 295 ? 0.7407 0.8068 0.7915 0.0812 0.0303 -0.1193 295 HIS A O 2349 C CB . HIS A 295 ? 0.7628 0.8858 0.8732 0.0728 0.0399 -0.1462 295 HIS A CB 2350 C CG . HIS A 295 ? 0.7846 0.9336 0.8937 0.0728 0.0408 -0.1548 295 HIS A CG 2351 N ND1 . HIS A 295 ? 0.8047 0.9554 0.8895 0.0801 0.0366 -0.1496 295 HIS A ND1 2352 C CD2 . HIS A 295 ? 0.8013 0.9725 0.9241 0.0661 0.0461 -0.1687 295 HIS A CD2 2353 C CE1 . HIS A 295 ? 0.8060 0.9877 0.8953 0.0811 0.0381 -0.1597 295 HIS A CE1 2354 N NE2 . HIS A 295 ? 0.8004 0.9981 0.9150 0.0701 0.0440 -0.1722 295 HIS A NE2 2355 N N . PRO A 296 ? 0.7716 0.8717 0.8155 0.1029 0.0277 -0.1279 296 PRO A N 2356 C CA . PRO A 296 ? 0.8105 0.8718 0.8025 0.1163 0.0239 -0.1164 296 PRO A CA 2357 C C . PRO A 296 ? 0.8526 0.8865 0.8143 0.1043 0.0266 -0.1123 296 PRO A C 2358 O O . PRO A 296 ? 0.8932 0.8757 0.8067 0.1001 0.0273 -0.1023 296 PRO A O 2359 C CB . PRO A 296 ? 0.8226 0.9109 0.7975 0.1440 0.0197 -0.1205 296 PRO A CB 2360 C CG . PRO A 296 ? 0.7946 0.9434 0.8135 0.1346 0.0228 -0.1363 296 PRO A CG 2361 C CD . PRO A 296 ? 0.7663 0.9125 0.8245 0.1100 0.0281 -0.1400 296 PRO A CD 2362 N N . LEU A 297 ? 0.8517 0.9169 0.8351 0.0956 0.0292 -0.1211 297 LEU A N 2363 C CA . LEU A 297 ? 0.9074 0.9555 0.8639 0.0806 0.0326 -0.1192 297 LEU A CA 2364 C C . LEU A 297 ? 0.8857 0.9404 0.8617 0.0536 0.0366 -0.1209 297 LEU A C 2365 O O . LEU A 297 ? 0.8913 0.9867 0.9110 0.0482 0.0382 -0.1306 297 LEU A O 2366 C CB . LEU A 297 ? 0.9055 0.9911 0.8765 0.0848 0.0334 -0.1288 297 LEU A CB 2367 C CG . LEU A 297 ? 0.9365 1.0406 0.8944 0.1132 0.0292 -0.1314 297 LEU A CG 2368 C CD1 . LEU A 297 ? 0.9308 1.0810 0.9093 0.1123 0.0307 -0.1433 297 LEU A CD1 2369 C CD2 . LEU A 297 ? 1.0073 1.0567 0.8915 0.1358 0.0264 -0.1186 297 LEU A CD2 2370 N N . THR A 298 ? 0.9071 0.9237 0.8450 0.0379 0.0388 -0.1131 298 THR A N 2371 C CA . THR A 298 ? 0.8728 0.9125 0.8265 0.0115 0.0426 -0.1173 298 THR A CA 2372 C C . THR A 298 ? 0.9139 0.9282 0.8133 -0.0195 0.0493 -0.1159 298 THR A C 2373 O O . THR A 298 ? 0.9404 0.8975 0.7789 -0.0184 0.0514 -0.1085 298 THR A O 2374 C CB . THR A 298 ? 0.8720 0.9049 0.8354 0.0109 0.0410 -0.1132 298 THR A CB 2375 O OG1 . THR A 298 ? 0.9284 0.9013 0.8309 -0.0001 0.0432 -0.1036 298 THR A OG1 2376 C CG2 . THR A 298 ? 0.8598 0.8996 0.8582 0.0379 0.0360 -0.1126 298 THR A CG2 2377 N N . ILE A 299 ? 0.9129 0.9711 0.8285 -0.0466 0.0534 -0.1243 299 ILE A N 2378 C CA . ILE A 299 ? 0.9754 1.0201 0.8381 -0.0879 0.0623 -0.1265 299 ILE A CA 2379 C C . ILE A 299 ? 0.9788 1.0704 0.8559 -0.1147 0.0654 -0.1342 299 ILE A C 2380 O O . ILE A 299 ? 0.9219 1.0811 0.8601 -0.0977 0.0605 -0.1418 299 ILE A O 2381 C CB . ILE A 299 ? 0.9912 1.0707 0.8584 -0.0984 0.0655 -0.1350 299 ILE A CB 2382 C CG1 . ILE A 299 ? 1.0498 1.1134 0.8536 -0.1491 0.0769 -0.1385 299 ILE A CG1 2383 C CG2 . ILE A 299 ? 0.9343 1.1041 0.8764 -0.0851 0.0616 -0.1483 299 ILE A CG2 2384 C CD1 . ILE A 299 ? 1.0692 1.1420 0.8572 -0.1595 0.0810 -0.1431 299 ILE A CD1 2385 N N . GLY A 300 ? 1.0530 1.1053 0.8660 -0.1554 0.0742 -0.1329 300 GLY A N 2386 C CA . GLY A 300 ? 1.0889 1.1912 0.9074 -0.1873 0.0784 -0.1422 300 GLY A CA 2387 C C . GLY A 300 ? 1.1564 1.2011 0.9462 -0.1874 0.0782 -0.1328 300 GLY A C 2388 O O . GLY A 300 ? 1.2002 1.1525 0.9445 -0.1707 0.0772 -0.1190 300 GLY A O 2389 N N . GLU A 301 ? 1.1868 1.2916 1.0012 -0.2028 0.0787 -0.1412 301 GLU A N 2390 C CA . GLU A 301 ? 1.2491 1.3098 1.0409 -0.2053 0.0786 -0.1341 301 GLU A CA 2391 C C . GLU A 301 ? 1.1537 1.2296 1.0108 -0.1503 0.0658 -0.1268 301 GLU A C 2392 O O . GLU A 301 ? 1.1116 1.2661 1.0251 -0.1359 0.0611 -0.1343 301 GLU A O 2393 C CB . GLU A 301 ? 1.3261 1.4515 1.1095 -0.2524 0.0862 -0.1486 301 GLU A CB 2394 C CG . GLU A 301 ? 1.4724 1.5129 1.1738 -0.2923 0.0962 -0.1443 301 GLU A CG 2395 C CD . GLU A 301 ? 1.6342 1.5809 1.2351 -0.3366 0.1104 -0.1425 301 GLU A CD 2396 O OE1 . GLU A 301 ? 1.6584 1.6545 1.2433 -0.3818 0.1201 -0.1567 301 GLU A OE1 2397 O OE2 . GLU A 301 ? 1.7627 1.5846 1.2947 -0.3238 0.1122 -0.1271 301 GLU A OE2 2398 N N . CYS A 302 ? 1.1258 1.1275 0.9688 -0.1188 0.0610 -0.1131 302 CYS A N 2399 C CA . CYS A 302 ? 1.0436 1.0589 0.9437 -0.0721 0.0509 -0.1080 302 CYS A CA 2400 C C . CYS A 302 ? 1.0230 0.9855 0.9068 -0.0565 0.0474 -0.0972 302 CYS A C 2401 O O . CYS A 302 ? 1.0361 0.9288 0.8545 -0.0710 0.0517 -0.0907 302 CYS A O 2402 C CB . CYS A 302 ? 1.0412 1.0431 0.9528 -0.0455 0.0474 -0.1055 302 CYS A CB 2403 S SG . CYS A 302 ? 1.0550 1.1256 1.0003 -0.0527 0.0494 -0.1185 302 CYS A SG 2404 N N . PRO A 303 ? 0.9584 0.9481 0.8948 -0.0262 0.0404 -0.0956 303 PRO A N 2405 C CA . PRO A 303 ? 0.9623 0.9062 0.8874 -0.0062 0.0362 -0.0858 303 PRO A CA 2406 C C . PRO A 303 ? 0.9749 0.8747 0.8756 0.0171 0.0336 -0.0798 303 PRO A C 2407 O O . PRO A 303 ? 0.9675 0.8780 0.8712 0.0200 0.0343 -0.0834 303 PRO A O 2408 C CB . PRO A 303 ? 0.9101 0.8984 0.8953 0.0163 0.0313 -0.0875 303 PRO A CB 2409 C CG . PRO A 303 ? 0.8796 0.9315 0.8979 0.0104 0.0329 -0.0978 303 PRO A CG 2410 C CD . PRO A 303 ? 0.9010 0.9575 0.8987 -0.0088 0.0372 -0.1031 303 PRO A CD 2411 N N . LYS A 304 ? 0.9924 0.8505 0.8688 0.0361 0.0302 -0.0720 304 LYS A N 2412 C CA . LYS A 304 ? 1.0218 0.8509 0.8710 0.0655 0.0267 -0.0680 304 LYS A CA 2413 C C . LYS A 304 ? 0.9326 0.8167 0.8427 0.0877 0.0217 -0.0732 304 LYS A C 2414 O O . LYS A 304 ? 0.9118 0.8224 0.8627 0.0893 0.0201 -0.0745 304 LYS A O 2415 C CB . LYS A 304 ? 1.1125 0.8784 0.9023 0.0816 0.0252 -0.0592 304 LYS A CB 2416 C CG . LYS A 304 ? 1.2415 0.9386 0.9590 0.0521 0.0329 -0.0551 304 LYS A CG 2417 C CD . LYS A 304 ? 1.3511 0.9987 1.0027 0.0377 0.0400 -0.0546 304 LYS A CD 2418 C CE . LYS A 304 ? 1.4097 1.0451 1.0333 -0.0170 0.0508 -0.0594 304 LYS A CE 2419 N NZ . LYS A 304 ? 1.5104 1.0901 1.0605 -0.0365 0.0597 -0.0591 304 LYS A NZ 2420 N N . TYR A 305 ? 0.8975 0.7965 0.8077 0.1020 0.0205 -0.0771 305 TYR A N 2421 C CA . TYR A 305 ? 0.8465 0.7987 0.8069 0.1137 0.0185 -0.0854 305 TYR A CA 2422 C C . TYR A 305 ? 0.8415 0.8015 0.7956 0.1388 0.0137 -0.0848 305 TYR A C 2423 O O . TYR A 305 ? 0.8909 0.8237 0.7955 0.1619 0.0104 -0.0801 305 TYR A O 2424 C CB . TYR A 305 ? 0.8417 0.8177 0.8059 0.1159 0.0197 -0.0925 305 TYR A CB 2425 C CG . TYR A 305 ? 0.7972 0.8265 0.8036 0.1220 0.0196 -0.1037 305 TYR A CG 2426 C CD1 . TYR A 305 ? 0.7564 0.8086 0.8058 0.1056 0.0240 -0.1111 305 TYR A CD1 2427 C CD2 . TYR A 305 ? 0.8077 0.8640 0.8029 0.1441 0.0162 -0.1083 305 TYR A CD2 2428 C CE1 . TYR A 305 ? 0.7442 0.8323 0.8189 0.1032 0.0271 -0.1227 305 TYR A CE1 2429 C CE2 . TYR A 305 ? 0.7930 0.9056 0.8230 0.1404 0.0183 -0.1219 305 TYR A CE2 2430 C CZ . TYR A 305 ? 0.7560 0.8780 0.8231 0.1159 0.0247 -0.1291 305 TYR A CZ 2431 O OH . TYR A 305 ? 0.7511 0.9165 0.8398 0.1046 0.0298 -0.1440 305 TYR A OH 2432 N N . VAL A 306 ? 0.8017 0.7974 0.7988 0.1355 0.0141 -0.0903 306 VAL A N 2433 C CA . VAL A 306 ? 0.7825 0.8087 0.7825 0.1536 0.0109 -0.0946 306 VAL A CA 2434 C C . VAL A 306 ? 0.7501 0.8293 0.7925 0.1397 0.0155 -0.1084 306 VAL A C 2435 O O . VAL A 306 ? 0.7414 0.8162 0.8081 0.1194 0.0211 -0.1114 306 VAL A O 2436 C CB . VAL A 306 ? 0.7768 0.7823 0.7716 0.1571 0.0087 -0.0874 306 VAL A CB 2437 C CG1 . VAL A 306 ? 0.8277 0.7731 0.7681 0.1683 0.0059 -0.0756 306 VAL A CG1 2438 C CG2 . VAL A 306 ? 0.7508 0.7521 0.7807 0.1337 0.0131 -0.0865 306 VAL A CG2 2439 N N . LYS A 307 ? 0.7693 0.8984 0.8134 0.1507 0.0141 -0.1180 307 LYS A N 2440 C CA . LYS A 307 ? 0.8003 0.9800 0.8742 0.1289 0.0211 -0.1341 307 LYS A CA 2441 C C . LYS A 307 ? 0.7999 0.9740 0.8893 0.1090 0.0266 -0.1356 307 LYS A C 2442 O O . LYS A 307 ? 0.8766 1.0834 0.9777 0.0855 0.0348 -0.1498 307 LYS A O 2443 C CB . LYS A 307 ? 0.8122 1.0669 0.8801 0.1443 0.0185 -0.1481 307 LYS A CB 2444 C CG . LYS A 307 ? 0.8267 1.1068 0.8905 0.1502 0.0182 -0.1551 307 LYS A CG 2445 C CD . LYS A 307 ? 0.8726 1.2313 0.9215 0.1789 0.0127 -0.1669 307 LYS A CD 2446 C CE . LYS A 307 ? 0.9111 1.3117 0.9599 0.1821 0.0135 -0.1776 307 LYS A CE 2447 N NZ . LYS A 307 ? 0.9570 1.4460 0.9878 0.2177 0.0069 -0.1901 307 LYS A NZ 2448 N N . SER A 308 ? 0.7885 0.9192 0.8723 0.1149 0.0235 -0.1221 308 SER A N 2449 C CA . SER A 308 ? 0.7656 0.8875 0.8587 0.0994 0.0283 -0.1221 308 SER A CA 2450 C C . SER A 308 ? 0.7710 0.8618 0.8730 0.0748 0.0385 -0.1254 308 SER A C 2451 O O . SER A 308 ? 0.7817 0.8477 0.8858 0.0757 0.0392 -0.1224 308 SER A O 2452 C CB . SER A 308 ? 0.7429 0.8257 0.8265 0.1131 0.0223 -0.1067 308 SER A CB 2453 O OG . SER A 308 ? 0.7426 0.8273 0.8022 0.1398 0.0136 -0.1012 308 SER A OG 2454 N N . ASN A 309 ? 0.8049 0.8936 0.9046 0.0545 0.0469 -0.1318 309 ASN A N 2455 C CA . ASN A 309 ? 0.8646 0.8994 0.9544 0.0387 0.0571 -0.1312 309 ASN A CA 2456 C C . ASN A 309 ? 0.8493 0.8411 0.9359 0.0527 0.0535 -0.1157 309 ASN A C 2457 O O . ASN A 309 ? 0.8741 0.8201 0.9496 0.0552 0.0582 -0.1118 309 ASN A O 2458 C CB . ASN A 309 ? 0.9373 0.9757 1.0101 0.0049 0.0711 -0.1461 309 ASN A CB 2459 C CG . ASN A 309 ? 0.9952 1.0734 1.0671 -0.0164 0.0781 -0.1647 309 ASN A CG 2460 O OD1 . ASN A 309 ? 1.0362 1.0998 1.1096 -0.0119 0.0786 -0.1660 309 ASN A OD1 2461 N ND2 . ASN A 309 ? 1.0262 1.1627 1.0952 -0.0413 0.0839 -0.1810 309 ASN A ND2 2462 N N . ARG A 310 ? 0.8132 0.8216 0.9055 0.0654 0.0449 -0.1079 310 ARG A N 2463 C CA . ARG A 310 ? 0.8125 0.7895 0.9016 0.0743 0.0423 -0.0956 310 ARG A CA 2464 C C . ARG A 310 ? 0.7583 0.7495 0.8504 0.0922 0.0311 -0.0865 310 ARG A C 2465 O O . ARG A 310 ? 0.7428 0.7666 0.8327 0.0967 0.0275 -0.0904 310 ARG A O 2466 C CB . ARG A 310 ? 0.8734 0.8370 0.9491 0.0560 0.0516 -0.0998 310 ARG A CB 2467 C CG . ARG A 310 ? 0.9415 0.8640 1.0079 0.0645 0.0517 -0.0879 310 ARG A CG 2468 C CD . ARG A 310 ? 0.9949 0.8988 1.0395 0.0427 0.0624 -0.0924 310 ARG A CD 2469 N NE . ARG A 310 ? 1.0651 0.9501 1.1065 0.0542 0.0587 -0.0806 310 ARG A NE 2470 C CZ . ARG A 310 ? 1.1121 0.9506 1.1392 0.0702 0.0595 -0.0704 310 ARG A CZ 2471 N NH1 . ARG A 310 ? 1.1497 0.9543 1.1619 0.0803 0.0636 -0.0706 310 ARG A NH1 2472 N NH2 . ARG A 310 ? 1.1343 0.9652 1.1602 0.0797 0.0558 -0.0609 310 ARG A NH2 2473 N N . LEU A 311 ? 0.7166 0.6849 0.8079 0.1026 0.0262 -0.0761 311 LEU A N 2474 C CA . LEU A 311 ? 0.7243 0.6885 0.8064 0.1139 0.0184 -0.0675 311 LEU A CA 2475 C C . LEU A 311 ? 0.7005 0.6442 0.7840 0.1148 0.0179 -0.0590 311 LEU A C 2476 O O . LEU A 311 ? 0.7006 0.6403 0.7859 0.1144 0.0177 -0.0571 311 LEU A O 2477 C CB . LEU A 311 ? 0.7265 0.6864 0.7930 0.1206 0.0137 -0.0657 311 LEU A CB 2478 C CG . LEU A 311 ? 0.7467 0.7274 0.8030 0.1292 0.0119 -0.0724 311 LEU A CG 2479 C CD1 . LEU A 311 ? 0.7754 0.7322 0.8043 0.1345 0.0091 -0.0682 311 LEU A CD1 2480 C CD2 . LEU A 311 ? 0.7549 0.7576 0.7999 0.1445 0.0081 -0.0747 311 LEU A CD2 2481 N N . VAL A 312 ? 0.6806 0.6206 0.7631 0.1163 0.0175 -0.0555 312 VAL A N 2482 C CA . VAL A 312 ? 0.6714 0.5973 0.7545 0.1194 0.0170 -0.0480 312 VAL A CA 2483 C C . VAL A 312 ? 0.6671 0.5910 0.7416 0.1239 0.0117 -0.0423 312 VAL A C 2484 O O . VAL A 312 ? 0.6394 0.5714 0.7124 0.1252 0.0116 -0.0439 312 VAL A O 2485 C CB . VAL A 312 ? 0.6791 0.5896 0.7613 0.1170 0.0244 -0.0487 312 VAL A CB 2486 C CG1 . VAL A 312 ? 0.6875 0.5864 0.7664 0.1268 0.0230 -0.0406 312 VAL A CG1 2487 C CG2 . VAL A 312 ? 0.6843 0.5842 0.7637 0.1147 0.0310 -0.0550 312 VAL A CG2 2488 N N . LEU A 313 ? 0.6693 0.5858 0.7351 0.1241 0.0081 -0.0375 313 LEU A N 2489 C CA . LEU A 313 ? 0.6751 0.5801 0.7247 0.1268 0.0040 -0.0324 313 LEU A CA 2490 C C . LEU A 313 ? 0.6756 0.5841 0.7354 0.1278 0.0044 -0.0277 313 LEU A C 2491 O O . LEU A 313 ? 0.6956 0.6140 0.7651 0.1275 0.0062 -0.0273 313 LEU A O 2492 C CB . LEU A 313 ? 0.6890 0.5771 0.7125 0.1181 0.0027 -0.0314 313 LEU A CB 2493 C CG . LEU A 313 ? 0.7326 0.5979 0.7251 0.1203 0.0020 -0.0333 313 LEU A CG 2494 C CD1 . LEU A 313 ? 0.7658 0.6093 0.7275 0.1008 0.0048 -0.0339 313 LEU A CD1 2495 C CD2 . LEU A 313 ? 0.7640 0.6090 0.7282 0.1390 -0.0019 -0.0312 313 LEU A CD2 2496 N N . ALA A 314 ? 0.6686 0.5725 0.7227 0.1327 0.0022 -0.0247 314 ALA A N 2497 C CA . ALA A 314 ? 0.6662 0.5709 0.7247 0.1342 0.0018 -0.0194 314 ALA A CA 2498 C C . ALA A 314 ? 0.6759 0.5785 0.7213 0.1277 -0.0007 -0.0178 314 ALA A C 2499 O O . ALA A 314 ? 0.6961 0.5792 0.7155 0.1225 -0.0022 -0.0189 314 ALA A O 2500 C CB . ALA A 314 ? 0.6716 0.5766 0.7269 0.1394 0.0004 -0.0180 314 ALA A CB 2501 N N . THR A 315 ? 0.6750 0.5962 0.7310 0.1279 0.0000 -0.0163 315 THR A N 2502 C CA . THR A 315 ? 0.6853 0.6185 0.7300 0.1168 -0.0012 -0.0171 315 THR A CA 2503 C C . THR A 315 ? 0.6641 0.6038 0.7139 0.1249 -0.0029 -0.0121 315 THR A C 2504 O O . THR A 315 ? 0.6763 0.6062 0.7097 0.1171 -0.0045 -0.0113 315 THR A O 2505 C CB . THR A 315 ? 0.6885 0.6612 0.7415 0.1108 0.0005 -0.0231 315 THR A CB 2506 O OG1 . THR A 315 ? 0.6922 0.6799 0.7642 0.1323 0.0014 -0.0217 315 THR A OG1 2507 C CG2 . THR A 315 ? 0.7034 0.6694 0.7435 0.0943 0.0027 -0.0291 315 THR A CG2 2508 N N . GLY A 316 ? 0.6447 0.5928 0.7096 0.1411 -0.0017 -0.0085 316 GLY A N 2509 C CA . GLY A 316 ? 0.6426 0.5918 0.7082 0.1507 -0.0026 -0.0027 316 GLY A CA 2510 C C . GLY A 316 ? 0.6549 0.5781 0.7170 0.1505 -0.0025 0.0008 316 GLY A C 2511 O O . GLY A 316 ? 0.6375 0.5489 0.6939 0.1448 -0.0035 -0.0021 316 GLY A O 2512 N N . LEU A 317 ? 0.6571 0.5754 0.7187 0.1589 -0.0010 0.0063 317 LEU A N 2513 C CA . LEU A 317 ? 0.6833 0.5903 0.7415 0.1557 -0.0006 0.0080 317 LEU A CA 2514 C C . LEU A 317 ? 0.6877 0.5752 0.7392 0.1549 0.0072 0.0093 317 LEU A C 2515 O O . LEU A 317 ? 0.6829 0.5537 0.7260 0.1615 0.0120 0.0106 317 LEU A O 2516 C CB . LEU A 317 ? 0.7112 0.6264 0.7666 0.1582 -0.0045 0.0120 317 LEU A CB 2517 C CG . LEU A 317 ? 0.7292 0.6576 0.7850 0.1683 -0.0046 0.0165 317 LEU A CG 2518 C CD1 . LEU A 317 ? 0.7633 0.6697 0.8090 0.1790 0.0012 0.0225 317 LEU A CD1 2519 C CD2 . LEU A 317 ? 0.7323 0.6756 0.7859 0.1658 -0.0090 0.0177 317 LEU A CD2 2520 N N . ARG A 318 ? 0.6823 0.5710 0.7307 0.1457 0.0092 0.0075 318 ARG A N 2521 C CA . ARG A 318 ? 0.7242 0.5936 0.7574 0.1329 0.0193 0.0057 318 ARG A CA 2522 C C . ARG A 318 ? 0.7624 0.5944 0.7720 0.1410 0.0253 0.0143 318 ARG A C 2523 O O . ARG A 318 ? 0.7686 0.6038 0.7763 0.1493 0.0224 0.0208 318 ARG A O 2524 C CB . ARG A 318 ? 0.7464 0.6421 0.7811 0.1201 0.0197 0.0003 318 ARG A CB 2525 C CG . ARG A 318 ? 0.8150 0.7011 0.8299 0.0947 0.0324 -0.0059 318 ARG A CG 2526 C CD . ARG A 318 ? 0.8404 0.7735 0.8602 0.0825 0.0319 -0.0138 318 ARG A CD 2527 N NE . ARG A 318 ? 0.8486 0.8342 0.8852 0.0860 0.0260 -0.0254 318 ARG A NE 2528 C CZ . ARG A 318 ? 0.8776 0.8927 0.9118 0.0656 0.0330 -0.0390 318 ARG A CZ 2529 N NH1 . ARG A 318 ? 0.9076 0.8963 0.9187 0.0331 0.0480 -0.0434 318 ARG A NH1 2530 N NH2 . ARG A 318 ? 0.8749 0.9432 0.9222 0.0780 0.0257 -0.0489 318 ARG A NH2 2531 N N . ASN A 319 ? 0.8333 0.6256 0.8183 0.1415 0.0341 0.0143 319 ASN A N 2532 C CA . ASN A 319 ? 0.8915 0.6355 0.8390 0.1596 0.0402 0.0230 319 ASN A CA 2533 C C . ASN A 319 ? 1.0078 0.7046 0.9138 0.1401 0.0529 0.0248 319 ASN A C 2534 O O . ASN A 319 ? 1.0590 0.7503 0.9559 0.1078 0.0617 0.0160 319 ASN A O 2535 C CB . ASN A 319 ? 0.8898 0.6023 0.8166 0.1755 0.0445 0.0221 319 ASN A CB 2536 C CG . ASN A 319 ? 0.9166 0.5950 0.8061 0.2124 0.0459 0.0312 319 ASN A CG 2537 O OD1 . ASN A 319 ? 0.8929 0.5798 0.7788 0.2266 0.0422 0.0384 319 ASN A OD1 2538 N ND2 . ASN A 319 ? 0.9490 0.5905 0.8071 0.2323 0.0510 0.0303 319 ASN A ND2 2539 N N . SER A 320 ? 1.1394 0.8063 1.0169 0.1580 0.0545 0.0350 320 SER A N 2540 C CA . SER A 320 ? 1.2589 0.8792 1.0921 0.1380 0.0666 0.0379 320 SER A CA 2541 C C . SER A 320 ? 1.4086 0.9301 1.1639 0.1369 0.0839 0.0405 320 SER A C 2542 O O . SER A 320 ? 1.3984 0.8850 1.1285 0.1737 0.0830 0.0461 320 SER A O 2543 C CB . SER A 320 ? 1.2432 0.8748 1.0776 0.1596 0.0600 0.0483 320 SER A CB 2544 O OG . SER A 320 ? 1.1888 0.8984 1.0843 0.1667 0.0444 0.0462 320 SER A OG 2545 N N . PRO A 321 ? 1.5429 1.0188 1.2532 0.0941 0.1006 0.0350 321 PRO A N 2546 C CA . PRO A 321 ? 1.7028 1.0605 1.3162 0.0892 0.1205 0.0389 321 PRO A CA 2547 C C . PRO A 321 ? 1.7631 1.0609 1.3223 0.1203 0.1230 0.0545 321 PRO A C 2548 O O . PRO A 321 ? 1.8532 1.0723 1.3490 0.1607 0.1276 0.0637 321 PRO A O 2549 C CB . PRO A 321 ? 1.7437 1.0881 1.3292 0.0222 0.1382 0.0250 321 PRO A CB 2550 C CG . PRO A 321 ? 1.6336 1.0983 1.3081 0.0028 0.1255 0.0119 321 PRO A CG 2551 C CD . PRO A 321 ? 1.5382 1.0721 1.2793 0.0459 0.1033 0.0214 321 PRO A CD 2552 N N . GLY B 1 ? 0.5632 0.6253 0.8617 -0.0580 -0.1098 0.1203 1 GLY B N 2553 C CA . GLY B 1 ? 0.5287 0.5816 0.8256 -0.0332 -0.0961 0.0964 1 GLY B CA 2554 C C . GLY B 1 ? 0.4954 0.6069 0.8078 -0.0138 -0.0829 0.0971 1 GLY B C 2555 O O . GLY B 1 ? 0.4830 0.6492 0.8098 -0.0115 -0.0795 0.1122 1 GLY B O 2556 N N . LEU B 2 ? 0.4789 0.5755 0.7824 0.0031 -0.0757 0.0806 2 LEU B N 2557 C CA . LEU B 2 ? 0.4677 0.6048 0.7721 0.0272 -0.0660 0.0790 2 LEU B CA 2558 C C . LEU B 2 ? 0.4559 0.6145 0.7605 0.0459 -0.0553 0.0745 2 LEU B C 2559 O O . LEU B 2 ? 0.4551 0.6637 0.7613 0.0657 -0.0506 0.0818 2 LEU B O 2560 C CB . LEU B 2 ? 0.4722 0.5683 0.7553 0.0423 -0.0610 0.0596 2 LEU B CB 2561 C CG . LEU B 2 ? 0.4725 0.5601 0.7520 0.0341 -0.0702 0.0639 2 LEU B CG 2562 C CD1 . LEU B 2 ? 0.4795 0.5206 0.7326 0.0507 -0.0633 0.0446 2 LEU B CD1 2563 C CD2 . LEU B 2 ? 0.4670 0.6253 0.7621 0.0358 -0.0763 0.0848 2 LEU B CD2 2564 N N . PHE B 3 ? 0.4358 0.5608 0.7365 0.0425 -0.0522 0.0627 3 PHE B N 2565 C CA . PHE B 3 ? 0.4442 0.5812 0.7405 0.0605 -0.0436 0.0542 3 PHE B CA 2566 C C . PHE B 3 ? 0.4490 0.6238 0.7601 0.0557 -0.0446 0.0701 3 PHE B C 2567 O O . PHE B 3 ? 0.4474 0.6394 0.7544 0.0729 -0.0383 0.0651 3 PHE B O 2568 C CB . PHE B 3 ? 0.4418 0.5277 0.7229 0.0619 -0.0390 0.0304 3 PHE B CB 2569 C CG . PHE B 3 ? 0.4508 0.5032 0.7109 0.0690 -0.0365 0.0172 3 PHE B CG 2570 C CD1 . PHE B 3 ? 0.4595 0.5076 0.6962 0.0908 -0.0330 0.0084 3 PHE B CD1 2571 C CD2 . PHE B 3 ? 0.4605 0.4822 0.7178 0.0566 -0.0394 0.0151 3 PHE B CD2 2572 C CE1 . PHE B 3 ? 0.4948 0.5031 0.7037 0.0978 -0.0325 -0.0020 3 PHE B CE1 2573 C CE2 . PHE B 3 ? 0.4725 0.4629 0.7074 0.0634 -0.0372 0.0054 3 PHE B CE2 2574 C CZ . PHE B 3 ? 0.4883 0.4698 0.6983 0.0829 -0.0339 -0.0026 3 PHE B CZ 2575 N N . GLY B 4 ? 0.4627 0.6457 0.7858 0.0318 -0.0541 0.0898 4 GLY B N 2576 C CA . GLY B 4 ? 0.4583 0.6792 0.7924 0.0225 -0.0568 0.1115 4 GLY B CA 2577 C C . GLY B 4 ? 0.4678 0.6593 0.7951 0.0206 -0.0573 0.1058 4 GLY B C 2578 O O . GLY B 4 ? 0.5159 0.7303 0.8472 0.0116 -0.0605 0.1249 4 GLY B O 2579 N N . ALA B 5 ? 0.4605 0.6066 0.7768 0.0289 -0.0542 0.0815 5 ALA B N 2580 C CA . ALA B 5 ? 0.4548 0.5831 0.7646 0.0325 -0.0544 0.0751 5 ALA B CA 2581 C C . ALA B 5 ? 0.4802 0.5638 0.7763 0.0165 -0.0670 0.0817 5 ALA B C 2582 O O . ALA B 5 ? 0.4869 0.5694 0.7765 0.0075 -0.0745 0.0991 5 ALA B O 2583 C CB . ALA B 5 ? 0.4481 0.5610 0.7527 0.0480 -0.0463 0.0482 5 ALA B CB 2584 N N . ILE B 6 ? 0.4932 0.5355 0.7789 0.0146 -0.0703 0.0685 6 ILE B N 2585 C CA . ILE B 6 ? 0.5286 0.5180 0.7900 0.0080 -0.0835 0.0700 6 ILE B CA 2586 C C . ILE B 6 ? 0.5609 0.5365 0.8136 -0.0181 -0.1001 0.0952 6 ILE B C 2587 O O . ILE B 6 ? 0.5401 0.5332 0.8044 -0.0321 -0.1028 0.1041 6 ILE B O 2588 C CB . ILE B 6 ? 0.5372 0.4926 0.7877 0.0147 -0.0826 0.0512 6 ILE B CB 2589 C CG1 . ILE B 6 ? 0.5233 0.4937 0.7793 0.0339 -0.0690 0.0301 6 ILE B CG1 2590 C CG2 . ILE B 6 ? 0.5810 0.4763 0.7975 0.0115 -0.0993 0.0539 6 ILE B CG2 2591 C CD1 . ILE B 6 ? 0.5294 0.4805 0.7775 0.0396 -0.0649 0.0142 6 ILE B CD1 2592 N N . ALA B 7 ? 0.6066 0.5509 0.8361 -0.0255 -0.1126 0.1077 7 ALA B N 2593 C CA . ALA B 7 ? 0.6588 0.5880 0.8756 -0.0578 -0.1311 0.1359 7 ALA B CA 2594 C C . ALA B 7 ? 0.6450 0.6519 0.8977 -0.0736 -0.1244 0.1566 7 ALA B C 2595 O O . ALA B 7 ? 0.6654 0.6827 0.9221 -0.1017 -0.1364 0.1755 7 ALA B O 2596 C CB . ALA B 7 ? 0.6965 0.5631 0.8854 -0.0725 -0.1498 0.1342 7 ALA B CB 2597 N N . GLY B 8 ? 0.6269 0.6914 0.9033 -0.0531 -0.1061 0.1524 8 GLY B N 2598 C CA . GLY B 8 ? 0.5962 0.7418 0.9012 -0.0570 -0.0977 0.1714 8 GLY B CA 2599 C C . GLY B 8 ? 0.6007 0.7774 0.9072 -0.0474 -0.0905 0.1815 8 GLY B C 2600 O O . GLY B 8 ? 0.6324 0.7899 0.9227 -0.0676 -0.1017 0.2023 8 GLY B O 2601 N N . PHE B 9 ? 0.5555 0.7721 0.8749 -0.0166 -0.0735 0.1665 9 PHE B N 2602 C CA . PHE B 9 ? 0.5547 0.8001 0.8729 -0.0035 -0.0668 0.1736 9 PHE B CA 2603 C C . PHE B 9 ? 0.5788 0.7660 0.8747 0.0060 -0.0705 0.1575 9 PHE B C 2604 O O . PHE B 9 ? 0.6006 0.7942 0.8871 0.0104 -0.0704 0.1676 9 PHE B O 2605 C CB . PHE B 9 ? 0.5292 0.8353 0.8612 0.0275 -0.0507 0.1647 9 PHE B CB 2606 C CG . PHE B 9 ? 0.5179 0.7955 0.8441 0.0530 -0.0437 0.1290 9 PHE B CG 2607 C CD1 . PHE B 9 ? 0.5342 0.7911 0.8504 0.0683 -0.0413 0.1113 9 PHE B CD1 2608 C CD2 . PHE B 9 ? 0.4982 0.7725 0.8269 0.0600 -0.0406 0.1150 9 PHE B CD2 2609 C CE1 . PHE B 9 ? 0.5249 0.7606 0.8361 0.0843 -0.0369 0.0815 9 PHE B CE1 2610 C CE2 . PHE B 9 ? 0.5048 0.7490 0.8237 0.0771 -0.0359 0.0854 9 PHE B CE2 2611 C CZ . PHE B 9 ? 0.5112 0.7378 0.8226 0.0864 -0.0346 0.0693 9 PHE B CZ 2612 N N . ILE B 10 ? 0.5839 0.7194 0.8698 0.0111 -0.0736 0.1338 10 ILE B N 2613 C CA . ILE B 10 ? 0.6176 0.6997 0.8782 0.0200 -0.0801 0.1219 10 ILE B CA 2614 C C . ILE B 10 ? 0.6860 0.7068 0.9195 -0.0029 -0.0986 0.1346 10 ILE B C 2615 O O . ILE B 10 ? 0.7103 0.7031 0.9408 -0.0085 -0.1031 0.1250 10 ILE B O 2616 C CB . ILE B 10 ? 0.5941 0.6668 0.8579 0.0421 -0.0719 0.0896 10 ILE B CB 2617 C CG1 . ILE B 10 ? 0.5670 0.6902 0.8513 0.0584 -0.0579 0.0773 10 ILE B CG1 2618 C CG2 . ILE B 10 ? 0.6176 0.6555 0.8571 0.0581 -0.0770 0.0790 10 ILE B CG2 2619 C CD1 . ILE B 10 ? 0.5586 0.6759 0.8465 0.0704 -0.0517 0.0490 10 ILE B CD1 2620 N N . GLU B 11 ? 0.7604 0.7555 0.9689 -0.0170 -0.1110 0.1570 11 GLU B N 2621 C CA . GLU B 11 ? 0.8386 0.7705 1.0138 -0.0468 -0.1335 0.1754 11 GLU B CA 2622 C C . GLU B 11 ? 0.8499 0.7035 0.9892 -0.0343 -0.1450 0.1543 11 GLU B C 2623 O O . GLU B 11 ? 0.8792 0.6907 1.0018 -0.0553 -0.1603 0.1593 11 GLU B O 2624 C CB . GLU B 11 ? 0.9433 0.8486 1.0869 -0.0628 -0.1461 0.2024 11 GLU B CB 2625 C CG . GLU B 11 ? 0.9972 0.9473 1.1565 -0.1042 -0.1514 0.2403 11 GLU B CG 2626 C CD . GLU B 11 ? 1.1350 1.0188 1.2443 -0.1360 -0.1751 0.2697 11 GLU B CD 2627 O OE1 . GLU B 11 ? 1.1872 1.0203 1.2583 -0.1155 -0.1788 0.2648 11 GLU B OE1 2628 O OE2 . GLU B 11 ? 1.2093 1.0896 1.3140 -0.1824 -0.1917 0.2983 11 GLU B OE2 2629 N N . GLY B 12 ? 0.8251 0.6637 0.9509 0.0013 -0.1385 0.1314 12 GLY B N 2630 C CA . GLY B 12 ? 0.8495 0.6240 0.9378 0.0218 -0.1476 0.1117 12 GLY B CA 2631 C C . GLY B 12 ? 0.8072 0.6110 0.9062 0.0609 -0.1319 0.0839 12 GLY B C 2632 O O . GLY B 12 ? 0.7819 0.6428 0.9093 0.0721 -0.1174 0.0795 12 GLY B O 2633 N N . GLY B 13 ? 0.8150 0.5831 0.8898 0.0811 -0.1357 0.0660 13 GLY B N 2634 C CA . GLY B 13 ? 0.7924 0.5953 0.8757 0.1160 -0.1222 0.0420 13 GLY B CA 2635 C C . GLY B 13 ? 0.8280 0.6117 0.8740 0.1483 -0.1282 0.0387 13 GLY B C 2636 O O . GLY B 13 ? 0.8777 0.6122 0.8872 0.1432 -0.1429 0.0554 13 GLY B O 2637 N N . TRP B 14 ? 0.7959 0.6217 0.8498 0.1807 -0.1172 0.0184 14 TRP B N 2638 C CA . TRP B 14 ? 0.8158 0.6445 0.8412 0.2180 -0.1199 0.0121 14 TRP B CA 2639 C C . TRP B 14 ? 0.8810 0.6899 0.8664 0.2588 -0.1243 -0.0038 14 TRP B C 2640 O O . TRP B 14 ? 0.8373 0.7041 0.8514 0.2686 -0.1107 -0.0186 14 TRP B O 2641 C CB . TRP B 14 ? 0.7398 0.6597 0.8148 0.2229 -0.1024 0.0026 14 TRP B CB 2642 C CG . TRP B 14 ? 0.6920 0.6349 0.7959 0.1970 -0.0982 0.0162 14 TRP B CG 2643 C CD1 . TRP B 14 ? 0.7158 0.6151 0.7987 0.1802 -0.1086 0.0383 14 TRP B CD1 2644 C CD2 . TRP B 14 ? 0.6214 0.6376 0.7749 0.1872 -0.0835 0.0093 14 TRP B CD2 2645 N NE1 . TRP B 14 ? 0.6646 0.6144 0.7841 0.1644 -0.0988 0.0459 14 TRP B NE1 2646 C CE2 . TRP B 14 ? 0.6124 0.6282 0.7719 0.1707 -0.0845 0.0269 14 TRP B CE2 2647 C CE3 . TRP B 14 ? 0.5744 0.6540 0.7630 0.1896 -0.0714 -0.0090 14 TRP B CE3 2648 C CZ2 . TRP B 14 ? 0.5757 0.6480 0.7710 0.1631 -0.0737 0.0242 14 TRP B CZ2 2649 C CZ3 . TRP B 14 ? 0.5360 0.6624 0.7574 0.1766 -0.0634 -0.0116 14 TRP B CZ3 2650 C CH2 . TRP B 14 ? 0.5389 0.6594 0.7615 0.1670 -0.0646 0.0036 14 TRP B CH2 2651 N N . GLN B 15 ? 1.0048 0.7307 0.9187 0.2839 -0.1442 0.0005 15 GLN B N 2652 C CA . GLN B 15 ? 1.0808 0.7875 0.9435 0.3367 -0.1499 -0.0150 15 GLN B CA 2653 C C . GLN B 15 ? 1.0353 0.8390 0.9257 0.3720 -0.1340 -0.0291 15 GLN B C 2654 O O . GLN B 15 ? 1.0425 0.8886 0.9281 0.4071 -0.1273 -0.0437 15 GLN B O 2655 C CB . GLN B 15 ? 1.2069 0.7961 0.9761 0.3609 -0.1772 -0.0072 15 GLN B CB 2656 C CG . GLN B 15 ? 1.2858 0.7690 1.0134 0.3270 -0.1990 0.0065 15 GLN B CG 2657 C CD . GLN B 15 ? 1.3385 0.7836 1.0320 0.3474 -0.2058 -0.0069 15 GLN B CD 2658 O OE1 . GLN B 15 ? 1.3457 0.7746 1.0581 0.3107 -0.2080 -0.0022 15 GLN B OE1 2659 N NE2 . GLN B 15 ? 1.4076 0.8416 1.0478 0.4096 -0.2091 -0.0233 15 GLN B NE2 2660 N N . GLY B 16 ? 1.0113 0.8552 0.9302 0.3622 -0.1286 -0.0236 16 GLY B N 2661 C CA . GLY B 16 ? 0.9857 0.9194 0.9275 0.3930 -0.1175 -0.0355 16 GLY B CA 2662 C C . GLY B 16 ? 0.9126 0.9587 0.9278 0.3762 -0.0970 -0.0470 16 GLY B C 2663 O O . GLY B 16 ? 0.9101 1.0373 0.9423 0.4012 -0.0898 -0.0574 16 GLY B O 2664 N N . MET B 17 ? 0.8544 0.9055 0.9099 0.3329 -0.0890 -0.0443 17 MET B N 2665 C CA . MET B 17 ? 0.7995 0.9404 0.9137 0.3131 -0.0723 -0.0539 17 MET B CA 2666 C C . MET B 17 ? 0.8041 0.9541 0.9104 0.3247 -0.0678 -0.0608 17 MET B C 2667 O O . MET B 17 ? 0.7951 0.8994 0.8994 0.3029 -0.0684 -0.0569 17 MET B O 2668 C CB . MET B 17 ? 0.7805 0.9230 0.9383 0.2633 -0.0660 -0.0477 17 MET B CB 2669 C CG . MET B 17 ? 0.7421 0.9620 0.9493 0.2405 -0.0524 -0.0571 17 MET B CG 2670 S SD . MET B 17 ? 0.7128 0.9307 0.9566 0.1952 -0.0482 -0.0525 17 MET B SD 2671 C CE . MET B 17 ? 0.7562 0.8953 0.9838 0.1776 -0.0520 -0.0411 17 MET B CE 2672 N N . VAL B 18 ? 0.8152 1.0337 0.9183 0.3605 -0.0627 -0.0703 18 VAL B N 2673 C CA . VAL B 18 ? 0.8465 1.0789 0.9284 0.3881 -0.0593 -0.0760 18 VAL B CA 2674 C C . VAL B 18 ? 0.7893 1.1150 0.9261 0.3604 -0.0419 -0.0791 18 VAL B C 2675 O O . VAL B 18 ? 0.7832 1.1127 0.9117 0.3664 -0.0365 -0.0802 18 VAL B O 2676 C CB . VAL B 18 ? 0.9128 1.1689 0.9484 0.4536 -0.0650 -0.0828 18 VAL B CB 2677 C CG1 . VAL B 18 ? 0.9377 1.2631 0.9685 0.4864 -0.0554 -0.0896 18 VAL B CG1 2678 C CG2 . VAL B 18 ? 0.9965 1.1291 0.9544 0.4844 -0.0858 -0.0792 18 VAL B CG2 2679 N N . ASP B 19 ? 0.7569 1.1520 0.9448 0.3283 -0.0346 -0.0798 19 ASP B N 2680 C CA . ASP B 19 ? 0.7215 1.2147 0.9554 0.3026 -0.0211 -0.0817 19 ASP B CA 2681 C C . ASP B 19 ? 0.6621 1.1330 0.9287 0.2444 -0.0157 -0.0779 19 ASP B C 2682 O O . ASP B 19 ? 0.6606 1.1986 0.9625 0.2124 -0.0077 -0.0779 19 ASP B O 2683 C CB . ASP B 19 ? 0.7126 1.3053 0.9746 0.3069 -0.0199 -0.0858 19 ASP B CB 2684 C CG . ASP B 19 ? 0.7366 1.2976 1.0059 0.2923 -0.0282 -0.0863 19 ASP B CG 2685 O OD1 . ASP B 19 ? 0.7288 1.1982 0.9840 0.2779 -0.0336 -0.0817 19 ASP B OD1 2686 O OD2 . ASP B 19 ? 0.7526 1.3871 1.0415 0.2958 -0.0296 -0.0905 19 ASP B OD2 2687 N N . GLY B 20 ? 0.6339 1.0110 0.8854 0.2304 -0.0215 -0.0737 20 GLY B N 2688 C CA . GLY B 20 ? 0.6010 0.9528 0.8754 0.1840 -0.0172 -0.0706 20 GLY B CA 2689 C C . GLY B 20 ? 0.6140 0.8711 0.8670 0.1785 -0.0244 -0.0646 20 GLY B C 2690 O O . GLY B 20 ? 0.6614 0.8686 0.8827 0.2034 -0.0345 -0.0615 20 GLY B O 2691 N N . TRP B 21 ? 0.5901 0.8222 0.8572 0.1447 -0.0208 -0.0619 21 TRP B N 2692 C CA . TRP B 21 ? 0.5925 0.7485 0.8439 0.1368 -0.0275 -0.0549 21 TRP B CA 2693 C C . TRP B 21 ? 0.5535 0.6906 0.8137 0.1238 -0.0327 -0.0496 21 TRP B C 2694 O O . TRP B 21 ? 0.5434 0.6304 0.7867 0.1263 -0.0415 -0.0405 21 TRP B O 2695 C CB . TRP B 21 ? 0.6109 0.7501 0.8683 0.1131 -0.0214 -0.0540 21 TRP B CB 2696 C CG . TRP B 21 ? 0.6661 0.7794 0.8980 0.1303 -0.0221 -0.0539 21 TRP B CG 2697 C CD1 . TRP B 21 ? 0.7148 0.7856 0.9103 0.1599 -0.0327 -0.0528 21 TRP B CD1 2698 C CD2 . TRP B 21 ? 0.6935 0.8137 0.9271 0.1193 -0.0134 -0.0547 21 TRP B CD2 2699 N NE1 . TRP B 21 ? 0.7428 0.7953 0.9171 0.1708 -0.0315 -0.0546 21 TRP B NE1 2700 C CE2 . TRP B 21 ? 0.7320 0.8187 0.9318 0.1464 -0.0184 -0.0551 21 TRP B CE2 2701 C CE3 . TRP B 21 ? 0.7214 0.8656 0.9755 0.0892 -0.0034 -0.0546 21 TRP B CE3 2702 C CZ2 . TRP B 21 ? 0.7761 0.8618 0.9669 0.1462 -0.0117 -0.0554 21 TRP B CZ2 2703 C CZ3 . TRP B 21 ? 0.7569 0.8976 1.0017 0.0858 0.0035 -0.0533 21 TRP B CZ3 2704 C CH2 . TRP B 21 ? 0.7758 0.8918 0.9916 0.1151 0.0003 -0.0537 21 TRP B CH2 2705 N N . TYR B 22 ? 0.5089 0.6873 0.7930 0.1089 -0.0283 -0.0542 22 TYR B N 2706 C CA . TYR B 22 ? 0.4895 0.6597 0.7802 0.1018 -0.0319 -0.0504 22 TYR B CA 2707 C C . TYR B 22 ? 0.4732 0.6947 0.7749 0.1089 -0.0322 -0.0574 22 TYR B C 2708 O O . TYR B 22 ? 0.4664 0.7374 0.7794 0.1063 -0.0285 -0.0656 22 TYR B O 2709 C CB . TYR B 22 ? 0.4744 0.6301 0.7747 0.0763 -0.0289 -0.0505 22 TYR B CB 2710 C CG . TYR B 22 ? 0.4729 0.6002 0.7680 0.0647 -0.0255 -0.0491 22 TYR B CG 2711 C CD1 . TYR B 22 ? 0.4825 0.5676 0.7645 0.0694 -0.0299 -0.0401 22 TYR B CD1 2712 C CD2 . TYR B 22 ? 0.4718 0.6121 0.7721 0.0462 -0.0195 -0.0558 22 TYR B CD2 2713 C CE1 . TYR B 22 ? 0.4896 0.5493 0.7654 0.0606 -0.0277 -0.0395 22 TYR B CE1 2714 C CE2 . TYR B 22 ? 0.4755 0.5879 0.7679 0.0370 -0.0161 -0.0538 22 TYR B CE2 2715 C CZ . TYR B 22 ? 0.4885 0.5622 0.7695 0.0464 -0.0198 -0.0465 22 TYR B CZ 2716 O OH . TYR B 22 ? 0.4952 0.5418 0.7669 0.0392 -0.0173 -0.0452 22 TYR B OH 2717 N N . GLY B 23 ? 0.4644 0.6799 0.7634 0.1161 -0.0368 -0.0531 23 GLY B N 2718 C CA . GLY B 23 ? 0.4638 0.7261 0.7709 0.1245 -0.0386 -0.0602 23 GLY B CA 2719 C C . GLY B 23 ? 0.4776 0.7281 0.7768 0.1360 -0.0432 -0.0530 23 GLY B C 2720 O O . GLY B 23 ? 0.4830 0.6973 0.7765 0.1298 -0.0439 -0.0416 23 GLY B O 2721 N N . TYR B 24 ? 0.4949 0.7831 0.7939 0.1533 -0.0463 -0.0583 24 TYR B N 2722 C CA . TYR B 24 ? 0.5034 0.7923 0.7960 0.1642 -0.0500 -0.0534 24 TYR B CA 2723 C C . TYR B 24 ? 0.5117 0.7958 0.7823 0.1942 -0.0549 -0.0474 24 TYR B C 2724 O O . TYR B 24 ? 0.5208 0.8252 0.7848 0.2124 -0.0561 -0.0540 24 TYR B O 2725 C CB . TYR B 24 ? 0.5093 0.8451 0.8156 0.1584 -0.0519 -0.0669 24 TYR B CB 2726 C CG . TYR B 24 ? 0.5242 0.8600 0.8419 0.1289 -0.0506 -0.0758 24 TYR B CG 2727 C CD1 . TYR B 24 ? 0.5209 0.8852 0.8509 0.1121 -0.0494 -0.0846 24 TYR B CD1 2728 C CD2 . TYR B 24 ? 0.5561 0.8627 0.8672 0.1194 -0.0512 -0.0743 24 TYR B CD2 2729 C CE1 . TYR B 24 ? 0.5450 0.8991 0.8779 0.0817 -0.0502 -0.0910 24 TYR B CE1 2730 C CE2 . TYR B 24 ? 0.5707 0.8636 0.8804 0.0956 -0.0525 -0.0831 24 TYR B CE2 2731 C CZ . TYR B 24 ? 0.5759 0.8874 0.8951 0.0745 -0.0527 -0.0911 24 TYR B CZ 2732 O OH . TYR B 24 ? 0.6253 0.9137 0.9361 0.0474 -0.0558 -0.0980 24 TYR B OH 2733 N N . HIS B 25 ? 0.5289 0.7875 0.7844 0.2013 -0.0580 -0.0339 25 HIS B N 2734 C CA . HIS B 25 ? 0.5710 0.8212 0.7991 0.2299 -0.0643 -0.0278 25 HIS B CA 2735 C C . HIS B 25 ? 0.5700 0.8464 0.8013 0.2359 -0.0646 -0.0263 25 HIS B C 2736 O O . HIS B 25 ? 0.5693 0.8358 0.8059 0.2217 -0.0618 -0.0159 25 HIS B O 2737 C CB . HIS B 25 ? 0.6046 0.7861 0.7996 0.2311 -0.0705 -0.0080 25 HIS B CB 2738 C CG . HIS B 25 ? 0.6557 0.8128 0.8104 0.2613 -0.0793 -0.0014 25 HIS B CG 2739 N ND1 . HIS B 25 ? 0.6767 0.8159 0.8136 0.2630 -0.0828 0.0156 25 HIS B ND1 2740 C CD2 . HIS B 25 ? 0.6917 0.8397 0.8156 0.2944 -0.0857 -0.0092 25 HIS B CD2 2741 C CE1 . HIS B 25 ? 0.7204 0.8314 0.8146 0.2935 -0.0918 0.0182 25 HIS B CE1 2742 N NE2 . HIS B 25 ? 0.7338 0.8491 0.8180 0.3156 -0.0941 0.0023 25 HIS B NE2 2743 N N . HIS B 26 ? 0.5875 0.9022 0.8139 0.2601 -0.0680 -0.0364 26 HIS B N 2744 C CA . HIS B 26 ? 0.5883 0.9312 0.8154 0.2691 -0.0695 -0.0374 26 HIS B CA 2745 C C . HIS B 26 ? 0.6269 0.9493 0.8187 0.2992 -0.0750 -0.0256 26 HIS B C 2746 O O . HIS B 26 ? 0.6449 0.9436 0.8110 0.3194 -0.0797 -0.0239 26 HIS B O 2747 C CB . HIS B 26 ? 0.5596 0.9678 0.8095 0.2685 -0.0715 -0.0595 26 HIS B CB 2748 C CG . HIS B 26 ? 0.5787 1.0276 0.8216 0.2968 -0.0762 -0.0686 26 HIS B CG 2749 N ND1 . HIS B 26 ? 0.5948 1.0628 0.8427 0.3013 -0.0751 -0.0749 26 HIS B ND1 2750 C CD2 . HIS B 26 ? 0.5935 1.0732 0.8227 0.3263 -0.0820 -0.0720 26 HIS B CD2 2751 C CE1 . HIS B 26 ? 0.6014 1.1146 0.8393 0.3343 -0.0797 -0.0817 26 HIS B CE1 2752 N NE2 . HIS B 26 ? 0.6164 1.1361 0.8431 0.3493 -0.0845 -0.0805 26 HIS B NE2 2753 N N . SER B 27 ? 0.6481 0.9763 0.8328 0.3049 -0.0750 -0.0173 27 SER B N 2754 C CA . SER B 27 ? 0.6954 0.9983 0.8422 0.3306 -0.0802 -0.0025 27 SER B CA 2755 C C . SER B 27 ? 0.6849 1.0261 0.8324 0.3439 -0.0799 -0.0043 27 SER B C 2756 O O . SER B 27 ? 0.6631 1.0087 0.8200 0.3298 -0.0747 0.0047 27 SER B O 2757 C CB . SER B 27 ? 0.7271 0.9644 0.8505 0.3141 -0.0807 0.0254 27 SER B CB 2758 O OG . SER B 27 ? 0.8046 1.0071 0.8845 0.3337 -0.0872 0.0428 27 SER B OG 2759 N N . ASN B 28 ? 0.7039 1.0760 0.8390 0.3746 -0.0858 -0.0161 28 ASN B N 2760 C CA . ASN B 28 ? 0.6953 1.1053 0.8274 0.3915 -0.0877 -0.0206 28 ASN B CA 2761 C C . ASN B 28 ? 0.7576 1.1677 0.8533 0.4320 -0.0952 -0.0192 28 ASN B C 2762 O O . ASN B 28 ? 0.7936 1.1592 0.8581 0.4465 -0.0988 -0.0103 28 ASN B O 2763 C CB . ASN B 28 ? 0.6400 1.1104 0.8073 0.3798 -0.0897 -0.0466 28 ASN B CB 2764 C CG . ASN B 28 ? 0.6122 1.1261 0.7954 0.3848 -0.0949 -0.0662 28 ASN B CG 2765 O OD1 . ASN B 28 ? 0.6484 1.1618 0.8112 0.4128 -0.0980 -0.0645 28 ASN B OD1 2766 N ND2 . ASN B 28 ? 0.5624 1.1148 0.7776 0.3586 -0.0965 -0.0838 28 ASN B ND2 2767 N N . GLU B 29 ? 0.7879 1.2422 0.8811 0.4528 -0.0990 -0.0284 29 GLU B N 2768 C CA . GLU B 29 ? 0.8605 1.3165 0.9156 0.4953 -0.1064 -0.0269 29 GLU B CA 2769 C C . GLU B 29 ? 0.8746 1.3670 0.9301 0.5201 -0.1130 -0.0454 29 GLU B C 2770 O O . GLU B 29 ? 0.9134 1.3861 0.9263 0.5592 -0.1191 -0.0410 29 GLU B O 2771 C CB . GLU B 29 ? 0.8922 1.3912 0.9452 0.5120 -0.1094 -0.0331 29 GLU B CB 2772 C CG . GLU B 29 ? 0.9240 1.3938 0.9660 0.5003 -0.1022 -0.0114 29 GLU B CG 2773 C CD . GLU B 29 ? 0.9555 1.4596 0.9821 0.5266 -0.1058 -0.0149 29 GLU B CD 2774 O OE1 . GLU B 29 ? 0.9891 1.5121 0.9929 0.5618 -0.1140 -0.0222 29 GLU B OE1 2775 O OE2 . GLU B 29 ? 0.9620 1.4749 0.9961 0.5156 -0.1006 -0.0104 29 GLU B OE2 2776 N N . GLN B 30 ? 0.8528 1.4000 0.9524 0.4990 -0.1122 -0.0647 30 GLN B N 2777 C CA . GLN B 30 ? 0.8552 1.4567 0.9625 0.5196 -0.1167 -0.0806 30 GLN B CA 2778 C C . GLN B 30 ? 0.8424 1.3914 0.9277 0.5271 -0.1141 -0.0722 30 GLN B C 2779 O O . GLN B 30 ? 0.8412 1.4202 0.9127 0.5606 -0.1179 -0.0804 30 GLN B O 2780 C CB . GLN B 30 ? 0.8432 1.5239 1.0045 0.4871 -0.1174 -0.1005 30 GLN B CB 2781 C CG . GLN B 30 ? 0.8654 1.6076 1.0415 0.4859 -0.1260 -0.1143 30 GLN B CG 2782 C CD . GLN B 30 ? 0.8748 1.6330 1.0873 0.4365 -0.1271 -0.1249 30 GLN B CD 2783 O OE1 . GLN B 30 ? 0.9079 1.6096 1.1168 0.4155 -0.1218 -0.1167 30 GLN B OE1 2784 N NE2 . GLN B 30 ? 0.8678 1.7033 1.1115 0.4179 -0.1352 -0.1419 30 GLN B NE2 2785 N N . GLY B 31 ? 0.8230 1.2973 0.9029 0.4982 -0.1086 -0.0563 31 GLY B N 2786 C CA . GLY B 31 ? 0.8346 1.2484 0.8898 0.5008 -0.1085 -0.0485 31 GLY B CA 2787 C C . GLY B 31 ? 0.7789 1.1636 0.8641 0.4532 -0.1010 -0.0429 31 GLY B C 2788 O O . GLY B 31 ? 0.7419 1.1322 0.8549 0.4211 -0.0957 -0.0392 31 GLY B O 2789 N N . SER B 32 ? 0.7740 1.1278 0.8494 0.4530 -0.1009 -0.0429 32 SER B N 2790 C CA . SER B 32 ? 0.7295 1.0492 0.8270 0.4115 -0.0950 -0.0367 32 SER B CA 2791 C C . SER B 32 ? 0.7198 1.0510 0.8236 0.4149 -0.0933 -0.0472 32 SER B C 2792 O O . SER B 32 ? 0.7487 1.0979 0.8276 0.4545 -0.0977 -0.0552 32 SER B O 2793 C CB . SER B 32 ? 0.7687 0.9935 0.8275 0.4005 -0.0992 -0.0122 32 SER B CB 2794 O OG . SER B 32 ? 0.8269 0.9882 0.8257 0.4329 -0.1101 -0.0066 32 SER B OG 2795 N N . GLY B 33 ? 0.6893 1.0120 0.8234 0.3768 -0.0867 -0.0467 33 GLY B N 2796 C CA . GLY B 33 ? 0.6921 1.0229 0.8311 0.3778 -0.0840 -0.0546 33 GLY B CA 2797 C C . GLY B 33 ? 0.6404 0.9714 0.8171 0.3338 -0.0759 -0.0553 33 GLY B C 2798 O O . GLY B 33 ? 0.6251 0.9512 0.8249 0.3027 -0.0725 -0.0509 33 GLY B O 2799 N N . TYR B 34 ? 0.6444 0.9814 0.8220 0.3364 -0.0731 -0.0610 34 TYR B N 2800 C CA . TYR B 34 ? 0.6172 0.9463 0.8220 0.2995 -0.0661 -0.0612 34 TYR B CA 2801 C C . TYR B 34 ? 0.5751 0.9901 0.8208 0.2844 -0.0587 -0.0746 34 TYR B C 2802 O O . TYR B 34 ? 0.5718 1.0518 0.8195 0.3088 -0.0587 -0.0827 34 TYR B O 2803 C CB . TYR B 34 ? 0.6523 0.9213 0.8243 0.3109 -0.0690 -0.0564 34 TYR B CB 2804 C CG . TYR B 34 ? 0.7104 0.8846 0.8347 0.3187 -0.0803 -0.0411 34 TYR B CG 2805 C CD1 . TYR B 34 ? 0.7035 0.8259 0.8333 0.2831 -0.0814 -0.0273 34 TYR B CD1 2806 C CD2 . TYR B 34 ? 0.7891 0.9257 0.8586 0.3611 -0.0915 -0.0392 34 TYR B CD2 2807 C CE1 . TYR B 34 ? 0.7623 0.8034 0.8491 0.2824 -0.0937 -0.0099 34 TYR B CE1 2808 C CE2 . TYR B 34 ? 0.8435 0.8838 0.8620 0.3622 -0.1050 -0.0231 34 TYR B CE2 2809 C CZ . TYR B 34 ? 0.8434 0.8391 0.8731 0.3192 -0.1062 -0.0075 34 TYR B CZ 2810 O OH . TYR B 34 ? 0.9271 0.8326 0.9067 0.3130 -0.1214 0.0115 34 TYR B OH 2811 N N . ALA B 35 ? 0.5574 0.9730 0.8326 0.2434 -0.0535 -0.0755 35 ALA B N 2812 C CA . ALA B 35 ? 0.5388 1.0206 0.8465 0.2193 -0.0483 -0.0849 35 ALA B CA 2813 C C . ALA B 35 ? 0.5355 0.9782 0.8528 0.1846 -0.0428 -0.0818 35 ALA B C 2814 O O . ALA B 35 ? 0.5431 0.9380 0.8606 0.1647 -0.0435 -0.0776 35 ALA B O 2815 C CB . ALA B 35 ? 0.5175 1.0493 0.8467 0.2026 -0.0524 -0.0927 35 ALA B CB 2816 N N . ALA B 36 ? 0.5320 0.9999 0.8551 0.1810 -0.0369 -0.0833 36 ALA B N 2817 C CA . ALA B 36 ? 0.5444 0.9793 0.8737 0.1510 -0.0314 -0.0806 36 ALA B CA 2818 C C . ALA B 36 ? 0.5482 1.0031 0.8999 0.1088 -0.0313 -0.0852 36 ALA B C 2819 O O . ALA B 36 ? 0.5580 1.0787 0.9264 0.0977 -0.0337 -0.0911 36 ALA B O 2820 C CB . ALA B 36 ? 0.5541 1.0162 0.8797 0.1628 -0.0249 -0.0802 36 ALA B CB 2821 N N . ASP B 37 ? 0.5644 0.9599 0.9115 0.0858 -0.0306 -0.0824 37 ASP B N 2822 C CA . ASP B 37 ? 0.5762 0.9695 0.9302 0.0476 -0.0323 -0.0868 37 ASP B CA 2823 C C . ASP B 37 ? 0.6090 1.0231 0.9696 0.0263 -0.0256 -0.0848 37 ASP B C 2824 O O . ASP B 37 ? 0.5848 0.9596 0.9364 0.0290 -0.0197 -0.0795 37 ASP B O 2825 C CB . ASP B 37 ? 0.5980 0.9198 0.9374 0.0405 -0.0342 -0.0843 37 ASP B CB 2826 C CG . ASP B 37 ? 0.6198 0.9237 0.9519 0.0085 -0.0395 -0.0907 37 ASP B CG 2827 O OD1 . ASP B 37 ? 0.6418 0.9567 0.9704 0.0050 -0.0482 -0.0978 37 ASP B OD1 2828 O OD2 . ASP B 37 ? 0.6301 0.9023 0.9540 -0.0116 -0.0367 -0.0890 37 ASP B OD2 2829 N N . LYS B 38 ? 0.6617 1.1416 1.0376 0.0036 -0.0271 -0.0877 38 LYS B N 2830 C CA . LYS B 38 ? 0.6934 1.2147 1.0785 -0.0181 -0.0198 -0.0826 38 LYS B CA 2831 C C . LYS B 38 ? 0.6827 1.1396 1.0532 -0.0515 -0.0186 -0.0794 38 LYS B C 2832 O O . LYS B 38 ? 0.6669 1.1122 1.0330 -0.0505 -0.0096 -0.0732 38 LYS B O 2833 C CB . LYS B 38 ? 0.7494 1.3612 1.1552 -0.0440 -0.0246 -0.0838 38 LYS B CB 2834 C CG . LYS B 38 ? 0.8064 1.4884 1.2268 -0.0664 -0.0161 -0.0747 38 LYS B CG 2835 C CD . LYS B 38 ? 0.8630 1.5804 1.2917 -0.1264 -0.0253 -0.0720 38 LYS B CD 2836 C CE . LYS B 38 ? 0.8788 1.6629 1.3234 -0.1333 -0.0381 -0.0784 38 LYS B CE 2837 N NZ . LYS B 38 ? 0.8758 1.7886 1.3496 -0.1113 -0.0319 -0.0738 38 LYS B NZ 2838 N N . GLU B 39 ? 0.7024 1.1145 1.0597 -0.0774 -0.0288 -0.0845 39 GLU B N 2839 C CA . GLU B 39 ? 0.7438 1.0902 1.0780 -0.1087 -0.0308 -0.0828 39 GLU B CA 2840 C C . GLU B 39 ? 0.7068 0.9885 1.0270 -0.0872 -0.0233 -0.0789 39 GLU B C 2841 O O . GLU B 39 ? 0.7319 0.9968 1.0447 -0.1006 -0.0168 -0.0730 39 GLU B O 2842 C CB . GLU B 39 ? 0.8223 1.1203 1.1327 -0.1279 -0.0461 -0.0913 39 GLU B CB 2843 C CG . GLU B 39 ? 0.9164 1.1281 1.1893 -0.1499 -0.0506 -0.0913 39 GLU B CG 2844 C CD . GLU B 39 ? 1.0064 1.1674 1.2446 -0.1678 -0.0689 -0.1012 39 GLU B CD 2845 O OE1 . GLU B 39 ? 1.0665 1.2578 1.3040 -0.2029 -0.0806 -0.1036 39 GLU B OE1 2846 O OE2 . GLU B 39 ? 1.0330 1.1262 1.2419 -0.1459 -0.0727 -0.1063 39 GLU B OE2 2847 N N . SER B 40 ? 0.6458 0.8947 0.9619 -0.0564 -0.0248 -0.0809 40 SER B N 2848 C CA . SER B 40 ? 0.6225 0.8165 0.9270 -0.0395 -0.0203 -0.0760 40 SER B CA 2849 C C . SER B 40 ? 0.5930 0.8056 0.9059 -0.0230 -0.0115 -0.0698 40 SER B C 2850 O O . SER B 40 ? 0.5830 0.7569 0.8846 -0.0230 -0.0076 -0.0655 40 SER B O 2851 C CB . SER B 40 ? 0.6051 0.7725 0.9053 -0.0148 -0.0246 -0.0758 40 SER B CB 2852 O OG . SER B 40 ? 0.6120 0.8175 0.9268 0.0081 -0.0248 -0.0747 40 SER B OG 2853 N N . THR B 41 ? 0.5536 0.8230 0.8810 -0.0056 -0.0096 -0.0702 41 THR B N 2854 C CA . THR B 41 ? 0.5378 0.8241 0.8637 0.0163 -0.0029 -0.0663 41 THR B CA 2855 C C . THR B 41 ? 0.5395 0.8466 0.8659 -0.0049 0.0054 -0.0625 41 THR B C 2856 O O . THR B 41 ? 0.5252 0.8042 0.8390 0.0048 0.0101 -0.0587 41 THR B O 2857 C CB . THR B 41 ? 0.5324 0.8781 0.8660 0.0457 -0.0034 -0.0684 41 THR B CB 2858 O OG1 . THR B 41 ? 0.5257 0.8413 0.8521 0.0677 -0.0110 -0.0692 41 THR B OG1 2859 C CG2 . THR B 41 ? 0.5365 0.8987 0.8589 0.0739 0.0024 -0.0658 41 THR B CG2 2860 N N . GLN B 42 ? 0.5670 0.9229 0.9055 -0.0361 0.0060 -0.0623 42 GLN B N 2861 C CA . GLN B 42 ? 0.5980 0.9837 0.9373 -0.0621 0.0141 -0.0550 42 GLN B CA 2862 C C . GLN B 42 ? 0.6210 0.9284 0.9378 -0.0845 0.0141 -0.0522 42 GLN B C 2863 O O . GLN B 42 ? 0.6330 0.9387 0.9418 -0.0899 0.0224 -0.0453 42 GLN B O 2864 C CB . GLN B 42 ? 0.6167 1.0749 0.9734 -0.0989 0.0116 -0.0527 42 GLN B CB 2865 C CG . GLN B 42 ? 0.6434 1.1503 1.0038 -0.1294 0.0207 -0.0406 42 GLN B CG 2866 C CD . GLN B 42 ? 0.6465 1.2182 1.0152 -0.0925 0.0341 -0.0351 42 GLN B CD 2867 O OE1 . GLN B 42 ? 0.6561 1.2098 1.0116 -0.0898 0.0433 -0.0284 42 GLN B OE1 2868 N NE2 . GLN B 42 ? 0.6436 1.2890 1.0287 -0.0597 0.0345 -0.0386 42 GLN B NE2 2869 N N . LYS B 43 ? 0.6456 0.8910 0.9488 -0.0939 0.0047 -0.0576 43 LYS B N 2870 C CA . LYS B 43 ? 0.6977 0.8625 0.9737 -0.1027 0.0031 -0.0566 43 LYS B CA 2871 C C . LYS B 43 ? 0.6595 0.7981 0.9311 -0.0730 0.0092 -0.0535 43 LYS B C 2872 O O . LYS B 43 ? 0.6955 0.8048 0.9513 -0.0805 0.0140 -0.0488 43 LYS B O 2873 C CB . LYS B 43 ? 0.7707 0.8839 1.0323 -0.0998 -0.0079 -0.0639 43 LYS B CB 2874 C CG . LYS B 43 ? 0.8889 0.9425 1.1160 -0.1292 -0.0160 -0.0660 43 LYS B CG 2875 C CD . LYS B 43 ? 0.9743 1.0253 1.1929 -0.1414 -0.0290 -0.0743 43 LYS B CD 2876 C CE . LYS B 43 ? 1.0713 1.0359 1.2422 -0.1457 -0.0404 -0.0801 43 LYS B CE 2877 N NZ . LYS B 43 ? 1.1345 1.0454 1.2698 -0.1735 -0.0415 -0.0752 43 LYS B NZ 2878 N N . ALA B 44 ? 0.5888 0.7343 0.8702 -0.0407 0.0073 -0.0556 44 ALA B N 2879 C CA . ALA B 44 ? 0.5766 0.6905 0.8489 -0.0156 0.0082 -0.0527 44 ALA B CA 2880 C C . ALA B 44 ? 0.5798 0.7215 0.8484 -0.0074 0.0167 -0.0493 44 ALA B C 2881 O O . ALA B 44 ? 0.5846 0.6899 0.8371 -0.0015 0.0184 -0.0465 44 ALA B O 2882 C CB . ALA B 44 ? 0.5664 0.6777 0.8434 0.0116 0.0014 -0.0537 44 ALA B CB 2883 N N . ILE B 45 ? 0.5742 0.7859 0.8565 -0.0041 0.0219 -0.0492 45 ILE B N 2884 C CA . ILE B 45 ? 0.5897 0.8417 0.8672 0.0090 0.0314 -0.0449 45 ILE B CA 2885 C C . ILE B 45 ? 0.6042 0.8500 0.8743 -0.0219 0.0395 -0.0376 45 ILE B C 2886 O O . ILE B 45 ? 0.6330 0.8688 0.8875 -0.0083 0.0455 -0.0340 45 ILE B O 2887 C CB . ILE B 45 ? 0.5933 0.9384 0.8885 0.0212 0.0359 -0.0449 45 ILE B CB 2888 C CG1 . ILE B 45 ? 0.5883 0.9274 0.8768 0.0638 0.0281 -0.0515 45 ILE B CG1 2889 C CG2 . ILE B 45 ? 0.5951 1.0003 0.8871 0.0296 0.0484 -0.0378 45 ILE B CG2 2890 C CD1 . ILE B 45 ? 0.5965 1.0227 0.9023 0.0772 0.0295 -0.0533 45 ILE B CD1 2891 N N . ASP B 46 ? 0.6056 0.8503 0.8805 -0.0627 0.0380 -0.0354 46 ASP B N 2892 C CA . ASP B 46 ? 0.6469 0.8727 0.9065 -0.0966 0.0433 -0.0269 46 ASP B CA 2893 C C . ASP B 46 ? 0.6527 0.7914 0.8851 -0.0883 0.0412 -0.0279 46 ASP B C 2894 O O . ASP B 46 ? 0.6928 0.8207 0.9092 -0.0925 0.0487 -0.0209 46 ASP B O 2895 C CB . ASP B 46 ? 0.6774 0.9015 0.9362 -0.1435 0.0368 -0.0251 46 ASP B CB 2896 C CG . ASP B 46 ? 0.6894 1.0112 0.9761 -0.1604 0.0382 -0.0215 46 ASP B CG 2897 O OD1 . ASP B 46 ? 0.6787 1.0762 0.9844 -0.1330 0.0470 -0.0191 46 ASP B OD1 2898 O OD2 . ASP B 46 ? 0.7219 1.0445 1.0078 -0.1993 0.0289 -0.0213 46 ASP B OD2 2899 N N . GLY B 47 ? 0.6315 0.7156 0.8591 -0.0753 0.0313 -0.0354 47 GLY B N 2900 C CA . GLY B 47 ? 0.6429 0.6551 0.8472 -0.0669 0.0279 -0.0358 47 GLY B CA 2901 C C . GLY B 47 ? 0.6441 0.6504 0.8427 -0.0378 0.0306 -0.0346 47 GLY B C 2902 O O . GLY B 47 ? 0.6607 0.6346 0.8387 -0.0386 0.0338 -0.0310 47 GLY B O 2903 N N . VAL B 48 ? 0.6307 0.6629 0.8413 -0.0112 0.0276 -0.0380 48 VAL B N 2904 C CA . VAL B 48 ? 0.6260 0.6423 0.8221 0.0188 0.0255 -0.0386 48 VAL B CA 2905 C C . VAL B 48 ? 0.6349 0.6856 0.8206 0.0239 0.0374 -0.0342 48 VAL B C 2906 O O . VAL B 48 ? 0.6593 0.6784 0.8227 0.0372 0.0375 -0.0332 48 VAL B O 2907 C CB . VAL B 48 ? 0.6291 0.6555 0.8300 0.0457 0.0169 -0.0429 48 VAL B CB 2908 C CG1 . VAL B 48 ? 0.6545 0.6559 0.8285 0.0775 0.0114 -0.0444 48 VAL B CG1 2909 C CG2 . VAL B 48 ? 0.6309 0.6230 0.8397 0.0403 0.0057 -0.0437 48 VAL B CG2 2910 N N . THR B 49 ? 0.6217 0.7426 0.8234 0.0125 0.0472 -0.0305 49 THR B N 2911 C CA . THR B 49 ? 0.6385 0.8100 0.8336 0.0152 0.0607 -0.0227 49 THR B CA 2912 C C . THR B 49 ? 0.6812 0.8176 0.8594 -0.0122 0.0667 -0.0147 49 THR B C 2913 O O . THR B 49 ? 0.6983 0.8283 0.8557 0.0033 0.0729 -0.0109 49 THR B O 2914 C CB . THR B 49 ? 0.6203 0.8879 0.8411 0.0004 0.0695 -0.0171 49 THR B CB 2915 O OG1 . THR B 49 ? 0.5808 0.8798 0.8132 0.0303 0.0636 -0.0250 49 THR B OG1 2916 C CG2 . THR B 49 ? 0.6275 0.9633 0.8434 0.0047 0.0849 -0.0059 49 THR B CG2 2917 N N . ASN B 50 ? 0.7050 0.8127 0.8854 -0.0503 0.0637 -0.0125 50 ASN B N 2918 C CA . ASN B 50 ? 0.7518 0.8105 0.9067 -0.0752 0.0667 -0.0053 50 ASN B CA 2919 C C . ASN B 50 ? 0.7572 0.7475 0.8882 -0.0488 0.0614 -0.0101 50 ASN B C 2920 O O . ASN B 50 ? 0.7758 0.7453 0.8832 -0.0503 0.0675 -0.0037 50 ASN B O 2921 C CB . ASN B 50 ? 0.7794 0.7996 0.9284 -0.1132 0.0593 -0.0052 50 ASN B CB 2922 C CG . ASN B 50 ? 0.8046 0.8877 0.9701 -0.1509 0.0625 0.0023 50 ASN B CG 2923 O OD1 . ASN B 50 ? 0.7965 0.9619 0.9798 -0.1518 0.0731 0.0105 50 ASN B OD1 2924 N ND2 . ASN B 50 ? 0.8395 0.8866 0.9964 -0.1809 0.0519 -0.0004 50 ASN B ND2 2925 N N . LYS B 51 ? 0.7471 0.7066 0.8841 -0.0264 0.0494 -0.0199 51 LYS B N 2926 C CA . LYS B 51 ? 0.7493 0.6516 0.8674 -0.0047 0.0409 -0.0237 51 LYS B CA 2927 C C . LYS B 51 ? 0.7613 0.6725 0.8631 0.0229 0.0442 -0.0232 51 LYS B C 2928 O O . LYS B 51 ? 0.7895 0.6653 0.8668 0.0284 0.0447 -0.0211 51 LYS B O 2929 C CB . LYS B 51 ? 0.7297 0.6125 0.8609 0.0084 0.0268 -0.0306 51 LYS B CB 2930 C CG . LYS B 51 ? 0.7471 0.5841 0.8628 0.0280 0.0150 -0.0327 51 LYS B CG 2931 C CD . LYS B 51 ? 0.7385 0.5671 0.8690 0.0345 0.0011 -0.0352 51 LYS B CD 2932 C CE . LYS B 51 ? 0.7290 0.5490 0.8699 0.0192 -0.0009 -0.0342 51 LYS B CE 2933 N NZ . LYS B 51 ? 0.7334 0.5412 0.8822 0.0266 -0.0148 -0.0324 51 LYS B NZ 2934 N N . VAL B 52 ? 0.7398 0.6963 0.8500 0.0443 0.0456 -0.0258 52 VAL B N 2935 C CA . VAL B 52 ? 0.7599 0.7217 0.8459 0.0782 0.0469 -0.0271 52 VAL B CA 2936 C C . VAL B 52 ? 0.7813 0.7664 0.8532 0.0690 0.0631 -0.0172 52 VAL B C 2937 O O . VAL B 52 ? 0.8052 0.7544 0.8481 0.0849 0.0619 -0.0172 52 VAL B O 2938 C CB . VAL B 52 ? 0.7585 0.7709 0.8489 0.1074 0.0470 -0.0313 52 VAL B CB 2939 C CG1 . VAL B 52 ? 0.7987 0.8128 0.8531 0.1494 0.0478 -0.0336 52 VAL B CG1 2940 C CG2 . VAL B 52 ? 0.7410 0.7209 0.8381 0.1158 0.0299 -0.0392 52 VAL B CG2 2941 N N . ASN B 53 ? 0.7742 0.8186 0.8650 0.0402 0.0770 -0.0074 53 ASN B N 2942 C CA . ASN B 53 ? 0.8095 0.8831 0.8876 0.0236 0.0930 0.0066 53 ASN B CA 2943 C C . ASN B 53 ? 0.8330 0.8313 0.8863 0.0043 0.0905 0.0098 53 ASN B C 2944 O O . ASN B 53 ? 0.8563 0.8486 0.8841 0.0098 0.0989 0.0174 53 ASN B O 2945 C CB . ASN B 53 ? 0.8098 0.9607 0.9135 -0.0142 0.1047 0.0190 53 ASN B CB 2946 C CG . ASN B 53 ? 0.7971 1.0371 0.9249 0.0084 0.1087 0.0172 53 ASN B CG 2947 O OD1 . ASN B 53 ? 0.8167 1.0730 0.9315 0.0564 0.1086 0.0109 53 ASN B OD1 2948 N ND2 . ASN B 53 ? 0.7927 1.0868 0.9505 -0.0240 0.1101 0.0218 53 ASN B ND2 2949 N N . SER B 54 ? 0.8438 0.7865 0.9009 -0.0140 0.0791 0.0042 54 SER B N 2950 C CA . SER B 54 ? 0.8910 0.7591 0.9196 -0.0233 0.0744 0.0053 54 SER B CA 2951 C C . SER B 54 ? 0.9219 0.7518 0.9294 0.0129 0.0672 -0.0013 54 SER B C 2952 O O . SER B 54 ? 0.9460 0.7444 0.9238 0.0147 0.0710 0.0038 54 SER B O 2953 C CB . SER B 54 ? 0.8777 0.6998 0.9114 -0.0388 0.0623 -0.0010 54 SER B CB 2954 O OG . SER B 54 ? 0.8803 0.7084 0.9133 -0.0775 0.0662 0.0061 54 SER B OG 2955 N N . ILE B 55 ? 0.9252 0.7544 0.9439 0.0397 0.0552 -0.0120 55 ILE B N 2956 C CA . ILE B 55 ? 0.9732 0.7631 0.9687 0.0707 0.0435 -0.0187 55 ILE B CA 2957 C C . ILE B 55 ? 1.0255 0.8360 0.9949 0.0929 0.0536 -0.0151 55 ILE B C 2958 O O . ILE B 55 ? 1.0615 0.8358 1.0016 0.1020 0.0526 -0.0139 55 ILE B O 2959 C CB . ILE B 55 ? 0.9736 0.7555 0.9801 0.0898 0.0263 -0.0286 55 ILE B CB 2960 C CG1 . ILE B 55 ? 0.9580 0.7140 0.9841 0.0722 0.0147 -0.0305 55 ILE B CG1 2961 C CG2 . ILE B 55 ? 1.0183 0.7617 0.9924 0.1206 0.0122 -0.0349 55 ILE B CG2 2962 C CD1 . ILE B 55 ? 0.9586 0.7128 0.9988 0.0815 -0.0007 -0.0358 55 ILE B CD1 2963 N N . ILE B 56 ? 1.0406 0.9135 1.0188 0.1051 0.0635 -0.0132 56 ILE B N 2964 C CA . ILE B 56 ? 1.0697 0.9763 1.0221 0.1322 0.0750 -0.0087 56 ILE B CA 2965 C C . ILE B 56 ? 1.1330 1.0396 1.0703 0.1101 0.0902 0.0053 56 ILE B C 2966 O O . ILE B 56 ? 1.1765 1.0594 1.0796 0.1320 0.0913 0.0060 56 ILE B O 2967 C CB . ILE B 56 ? 1.0547 1.0505 1.0243 0.1434 0.0878 -0.0045 56 ILE B CB 2968 C CG1 . ILE B 56 ? 1.0405 1.0282 1.0111 0.1752 0.0719 -0.0186 56 ILE B CG1 2969 C CG2 . ILE B 56 ? 1.0818 1.1294 1.0259 0.1694 0.1042 0.0043 56 ILE B CG2 2970 C CD1 . ILE B 56 ? 1.0202 1.0955 1.0150 0.1820 0.0822 -0.0157 56 ILE B CD1 2971 N N . ASP B 57 ? 1.1628 1.0895 1.1202 0.0660 0.1000 0.0166 57 ASP B N 2972 C CA . ASP B 57 ? 1.2232 1.1501 1.1619 0.0379 0.1145 0.0334 57 ASP B CA 2973 C C . ASP B 57 ? 1.2325 1.0727 1.1370 0.0399 0.1062 0.0309 57 ASP B C 2974 O O . ASP B 57 ? 1.2440 1.0765 1.1179 0.0418 0.1160 0.0412 57 ASP B O 2975 C CB . ASP B 57 ? 1.2427 1.1949 1.2027 -0.0143 0.1209 0.0452 57 ASP B CB 2976 C CG . ASP B 57 ? 1.3227 1.2695 1.2567 -0.0497 0.1338 0.0655 57 ASP B CG 2977 O OD1 . ASP B 57 ? 1.3854 1.3939 1.3121 -0.0446 0.1501 0.0798 57 ASP B OD1 2978 O OD2 . ASP B 57 ? 1.3677 1.2468 1.2835 -0.0805 0.1271 0.0680 57 ASP B OD2 2979 N N . LYS B 58 ? 1.2325 1.0139 1.1417 0.0407 0.0887 0.0186 58 LYS B N 2980 C CA . LYS B 58 ? 1.2599 0.9674 1.1386 0.0465 0.0792 0.0156 58 LYS B CA 2981 C C . LYS B 58 ? 1.3184 1.0075 1.1699 0.0849 0.0737 0.0097 58 LYS B C 2982 O O . LYS B 58 ? 1.3356 0.9812 1.1542 0.0902 0.0728 0.0125 58 LYS B O 2983 C CB . LYS B 58 ? 1.2331 0.8998 1.1266 0.0425 0.0618 0.0049 58 LYS B CB 2984 C CG . LYS B 58 ? 1.2554 0.8775 1.1326 0.0160 0.0618 0.0101 58 LYS B CG 2985 C CD . LYS B 58 ? 1.2983 0.9325 1.1604 -0.0184 0.0777 0.0259 58 LYS B CD 2986 C CE . LYS B 58 ? 1.3344 0.9136 1.1748 -0.0458 0.0726 0.0286 58 LYS B CE 2987 N NZ . LYS B 58 ? 1.3950 0.9570 1.1997 -0.0804 0.0837 0.0465 58 LYS B NZ 2988 N N . MET B 59 ? 1.3648 1.0824 1.2237 0.1134 0.0686 0.0012 59 MET B N 2989 C CA . MET B 59 ? 1.4283 1.1231 1.2536 0.1523 0.0599 -0.0061 59 MET B CA 2990 C C . MET B 59 ? 1.5029 1.2421 1.3041 0.1687 0.0797 0.0043 59 MET B C 2991 O O . MET B 59 ? 1.5463 1.2720 1.3135 0.2063 0.0743 -0.0018 59 MET B O 2992 C CB . MET B 59 ? 1.4150 1.1036 1.2465 0.1774 0.0408 -0.0207 59 MET B CB 2993 C CG . MET B 59 ? 1.3835 1.0432 1.2427 0.1596 0.0226 -0.0276 59 MET B CG 2994 S SD . MET B 59 ? 1.4195 1.0129 1.2636 0.1574 0.0014 -0.0323 59 MET B SD 2995 C CE . MET B 59 ? 1.4796 1.0373 1.2728 0.1955 -0.0119 -0.0400 59 MET B CE 2996 N N . ASN B 60 ? 1.5415 1.3350 1.3576 0.1395 0.1015 0.0210 60 ASN B N 2997 C CA . ASN B 60 ? 1.5911 1.4460 1.3903 0.1482 0.1234 0.0364 60 ASN B CA 2998 C C . ASN B 60 ? 1.6331 1.4477 1.3861 0.1630 0.1268 0.0417 60 ASN B C 2999 O O . ASN B 60 ? 1.6386 1.4696 1.3622 0.2042 0.1297 0.0395 60 ASN B O 3000 C CB . ASN B 60 ? 1.5914 1.5064 1.4167 0.0994 0.1426 0.0568 60 ASN B CB 3001 C CG . ASN B 60 ? 1.6314 1.6233 1.4432 0.1001 0.1667 0.0781 60 ASN B CG 3002 O OD1 . ASN B 60 ? 1.6535 1.6403 1.4494 0.0655 0.1788 0.0976 60 ASN B OD1 3003 N ND2 . ASN B 60 ? 1.6394 1.7032 1.4533 0.1409 0.1733 0.0756 60 ASN B ND2 3004 N N . THR B 61 ? 1.3115 1.9153 1.3659 -0.1398 -0.2210 -0.3332 61 THR B N 3005 C CA . THR B 61 ? 1.3154 1.8285 1.3751 -0.1429 -0.1990 -0.3270 61 THR B CA 3006 C C . THR B 61 ? 1.2777 1.7609 1.3192 -0.0956 -0.1775 -0.3069 61 THR B C 3007 O O . THR B 61 ? 1.3152 1.7922 1.3137 -0.0748 -0.1781 -0.3254 61 THR B O 3008 C CB . THR B 61 ? 1.4191 1.8295 1.4390 -0.1749 -0.2113 -0.3667 61 THR B CB 3009 O OG1 . THR B 61 ? 1.4723 1.9125 1.4939 -0.2293 -0.2393 -0.3885 61 THR B OG1 3010 C CG2 . THR B 61 ? 1.4339 1.7561 1.4618 -0.1889 -0.1964 -0.3495 61 THR B CG2 3011 N N . GLN B 62 ? 1.2304 1.7080 1.3036 -0.0816 -0.1593 -0.2716 62 GLN B N 3012 C CA . GLN B 62 ? 1.2058 1.6616 1.2645 -0.0469 -0.1425 -0.2457 62 GLN B CA 3013 C C . GLN B 62 ? 1.1562 1.5802 1.2471 -0.0424 -0.1246 -0.2195 62 GLN B C 3014 O O . GLN B 62 ? 1.1878 1.6417 1.3170 -0.0580 -0.1251 -0.2164 62 GLN B O 3015 C CB . GLN B 62 ? 1.1867 1.7059 1.2316 -0.0283 -0.1562 -0.2212 62 GLN B CB 3016 C CG . GLN B 62 ? 1.1664 1.6653 1.2018 -0.0065 -0.1479 -0.1794 62 GLN B CG 3017 C CD . GLN B 62 ? 1.1908 1.7312 1.1940 0.0005 -0.1708 -0.1489 62 GLN B CD 3018 O OE1 . GLN B 62 ? 1.2279 1.8213 1.2073 -0.0085 -0.1869 -0.1615 62 GLN B OE1 3019 N NE2 . GLN B 62 ? 1.2046 1.7121 1.1982 0.0129 -0.1773 -0.1069 62 GLN B NE2 3020 N N . PHE B 63 ? 1.0937 1.4728 1.1681 -0.0230 -0.1086 -0.2035 63 PHE B N 3021 C CA . PHE B 63 ? 1.0463 1.3857 1.1399 -0.0196 -0.0916 -0.1837 63 PHE B CA 3022 C C . PHE B 63 ? 1.0473 1.4257 1.1736 -0.0076 -0.0946 -0.1634 63 PHE B C 3023 O O . PHE B 63 ? 1.0749 1.4776 1.1946 0.0143 -0.1102 -0.1465 63 PHE B O 3024 C CB . PHE B 63 ? 0.9860 1.2885 1.0542 -0.0010 -0.0794 -0.1689 63 PHE B CB 3025 C CG . PHE B 63 ? 0.9467 1.2005 1.0257 -0.0006 -0.0636 -0.1546 63 PHE B CG 3026 C CD1 . PHE B 63 ? 0.9252 1.1257 1.0001 -0.0129 -0.0577 -0.1685 63 PHE B CD1 3027 C CD2 . PHE B 63 ? 0.9351 1.1857 1.0197 0.0115 -0.0603 -0.1275 63 PHE B CD2 3028 C CE1 . PHE B 63 ? 0.9262 1.0867 1.0047 -0.0155 -0.0452 -0.1521 63 PHE B CE1 3029 C CE2 . PHE B 63 ? 0.8923 1.1036 0.9817 0.0109 -0.0463 -0.1181 63 PHE B CE2 3030 C CZ . PHE B 63 ? 0.9000 1.0740 0.9875 -0.0039 -0.0370 -0.1287 63 PHE B CZ 3031 N N . GLU B 64 ? 1.0401 1.4243 1.1963 -0.0209 -0.0830 -0.1665 64 GLU B N 3032 C CA . GLU B 64 ? 1.0360 1.4658 1.2248 0.0010 -0.0825 -0.1586 64 GLU B CA 3033 C C . GLU B 64 ? 1.0097 1.3901 1.1931 0.0061 -0.0620 -0.1477 64 GLU B C 3034 O O . GLU B 64 ? 1.0204 1.3754 1.2007 -0.0250 -0.0459 -0.1504 64 GLU B O 3035 C CB . GLU B 64 ? 1.0428 1.5658 1.2756 -0.0219 -0.0840 -0.1767 64 GLU B CB 3036 C CG . GLU B 64 ? 1.0654 1.6504 1.3067 -0.0293 -0.1081 -0.1893 64 GLU B CG 3037 C CD . GLU B 64 ? 1.0838 1.7731 1.3695 -0.0671 -0.1095 -0.2069 64 GLU B CD 3038 O OE1 . GLU B 64 ? 1.0598 1.8020 1.3773 -0.0745 -0.0919 -0.2079 64 GLU B OE1 3039 O OE2 . GLU B 64 ? 1.1079 1.8369 1.3944 -0.0940 -0.1282 -0.2205 64 GLU B OE2 3040 N N . ALA B 65 ? 1.0070 1.3638 1.1812 0.0426 -0.0680 -0.1340 65 ALA B N 3041 C CA . ALA B 65 ? 1.0096 1.3204 1.1735 0.0490 -0.0524 -0.1265 65 ALA B CA 3042 C C . ALA B 65 ? 0.9986 1.3744 1.1971 0.0540 -0.0394 -0.1439 65 ALA B C 3043 O O . ALA B 65 ? 0.9247 1.3820 1.1571 0.0758 -0.0500 -0.1602 65 ALA B O 3044 C CB . ALA B 65 ? 1.0310 1.2822 1.1629 0.0789 -0.0701 -0.1074 65 ALA B CB 3045 N N . VAL B 66 ? 1.0131 1.3668 1.2025 0.0344 -0.0172 -0.1411 66 VAL B N 3046 C CA . VAL B 66 ? 1.0186 1.4475 1.2322 0.0334 0.0004 -0.1570 66 VAL B CA 3047 C C . VAL B 66 ? 1.0154 1.3923 1.2025 0.0594 0.0065 -0.1556 66 VAL B C 3048 O O . VAL B 66 ? 1.0379 1.3222 1.1889 0.0528 0.0042 -0.1358 66 VAL B O 3049 C CB . VAL B 66 ? 1.0458 1.5042 1.2618 -0.0317 0.0197 -0.1517 66 VAL B CB 3050 C CG1 . VAL B 66 ? 1.0567 1.6276 1.2971 -0.0431 0.0408 -0.1661 66 VAL B CG1 3051 C CG2 . VAL B 66 ? 1.0746 1.5573 1.3042 -0.0656 0.0072 -0.1540 66 VAL B CG2 3052 N N . GLY B 67 ? 1.0022 1.4497 1.2073 0.0902 0.0130 -0.1811 67 GLY B N 3053 C CA . GLY B 67 ? 0.9925 1.3955 1.1679 0.1161 0.0170 -0.1890 67 GLY B CA 3054 C C . GLY B 67 ? 0.9651 1.3658 1.1193 0.0661 0.0452 -0.1757 67 GLY B C 3055 O O . GLY B 67 ? 0.9439 1.4361 1.1166 0.0265 0.0667 -0.1783 67 GLY B O 3056 N N . ARG B 68 ? 0.9330 1.2320 1.0448 0.0618 0.0415 -0.1573 68 ARG B N 3057 C CA . ARG B 68 ? 0.9003 1.1868 0.9834 0.0241 0.0610 -0.1436 68 ARG B CA 3058 C C . ARG B 68 ? 0.9074 1.1333 0.9533 0.0524 0.0536 -0.1511 68 ARG B C 3059 O O . ARG B 68 ? 0.9669 1.1107 0.9953 0.0736 0.0300 -0.1437 68 ARG B O 3060 C CB . ARG B 68 ? 0.8951 1.1122 0.9612 -0.0179 0.0581 -0.1090 68 ARG B CB 3061 C CG . ARG B 68 ? 0.8707 1.1179 0.9590 -0.0523 0.0585 -0.1028 68 ARG B CG 3062 C CD . ARG B 68 ? 0.8710 1.0305 0.9342 -0.0773 0.0475 -0.0784 68 ARG B CD 3063 N NE . ARG B 68 ? 0.8844 1.0480 0.9639 -0.0942 0.0372 -0.0820 68 ARG B NE 3064 C CZ . ARG B 68 ? 0.8969 1.0583 0.9924 -0.0675 0.0246 -0.0924 68 ARG B CZ 3065 N NH1 . ARG B 68 ? 0.8591 1.0070 0.9533 -0.0281 0.0184 -0.0934 68 ARG B NH1 3066 N NH2 . ARG B 68 ? 0.9783 1.1477 1.0834 -0.0871 0.0146 -0.0997 68 ARG B NH2 3067 N N . GLU B 69 ? 0.8987 1.1673 0.9263 0.0450 0.0718 -0.1642 69 GLU B N 3068 C CA . GLU B 69 ? 0.8857 1.0991 0.8717 0.0696 0.0630 -0.1781 69 GLU B CA 3069 C C . GLU B 69 ? 0.8552 1.0387 0.8035 0.0247 0.0736 -0.1502 69 GLU B C 3070 O O . GLU B 69 ? 0.8019 1.0270 0.7518 -0.0205 0.0911 -0.1284 69 GLU B O 3071 C CB . GLU B 69 ? 0.9441 1.2380 0.9334 0.1157 0.0701 -0.2302 69 GLU B CB 3072 C CG . GLU B 69 ? 0.9777 1.2909 1.0013 0.1753 0.0490 -0.2605 69 GLU B CG 3073 C CD . GLU B 69 ? 1.0511 1.4404 1.0771 0.2408 0.0486 -0.3226 69 GLU B CD 3074 O OE1 . GLU B 69 ? 1.1417 1.4863 1.1210 0.2606 0.0436 -0.3467 69 GLU B OE1 3075 O OE2 . GLU B 69 ? 1.0871 1.5877 1.1618 0.2764 0.0509 -0.3519 69 GLU B OE2 3076 N N . PHE B 70 ? 0.8716 0.9765 0.7810 0.0342 0.0569 -0.1485 70 PHE B N 3077 C CA . PHE B 70 ? 0.8797 0.9508 0.7526 -0.0020 0.0587 -0.1205 70 PHE B CA 3078 C C . PHE B 70 ? 0.9168 0.9579 0.7430 0.0133 0.0493 -0.1442 70 PHE B C 3079 O O . PHE B 70 ? 0.9474 0.9370 0.7621 0.0486 0.0272 -0.1699 70 PHE B O 3080 C CB . PHE B 70 ? 0.8577 0.8615 0.7355 -0.0163 0.0406 -0.0846 70 PHE B CB 3081 C CG . PHE B 70 ? 0.8087 0.8274 0.7251 -0.0240 0.0438 -0.0698 70 PHE B CG 3082 C CD1 . PHE B 70 ? 0.8012 0.8272 0.7173 -0.0557 0.0512 -0.0467 70 PHE B CD1 3083 C CD2 . PHE B 70 ? 0.7736 0.7879 0.7177 -0.0008 0.0334 -0.0790 70 PHE B CD2 3084 C CE1 . PHE B 70 ? 0.7808 0.8056 0.7239 -0.0626 0.0485 -0.0392 70 PHE B CE1 3085 C CE2 . PHE B 70 ? 0.7530 0.7837 0.7274 -0.0086 0.0350 -0.0702 70 PHE B CE2 3086 C CZ . PHE B 70 ? 0.7467 0.7809 0.7208 -0.0388 0.0426 -0.0535 70 PHE B CZ 3087 N N . ASN B 71 ? 0.9398 1.0018 0.7306 -0.0155 0.0605 -0.1345 71 ASN B N 3088 C CA . ASN B 71 ? 0.9869 1.0265 0.7262 -0.0044 0.0515 -0.1617 71 ASN B CA 3089 C C . ASN B 71 ? 0.9918 0.9359 0.7065 -0.0159 0.0202 -0.1403 71 ASN B C 3090 O O . ASN B 71 ? 0.9401 0.8522 0.6819 -0.0275 0.0089 -0.1074 71 ASN B O 3091 C CB . ASN B 71 ? 1.0071 1.1210 0.7106 -0.0341 0.0752 -0.1609 71 ASN B CB 3092 C CG . ASN B 71 ? 1.0002 1.0881 0.6837 -0.0828 0.0700 -0.1052 71 ASN B CG 3093 O OD1 . ASN B 71 ? 1.0025 1.0214 0.6770 -0.0871 0.0455 -0.0840 71 ASN B OD1 3094 N ND2 . ASN B 71 ? 1.0292 1.1772 0.7020 -0.1212 0.0894 -0.0805 71 ASN B ND2 3095 N N . ASN B 72 ? 1.0756 0.9868 0.7378 -0.0154 0.0059 -0.1616 72 ASN B N 3096 C CA . ASN B 72 ? 1.1344 0.9641 0.7684 -0.0346 -0.0279 -0.1451 72 ASN B CA 3097 C C . ASN B 72 ? 1.0937 0.9403 0.7354 -0.0752 -0.0300 -0.0941 72 ASN B C 3098 O O . ASN B 72 ? 1.0834 0.8950 0.7258 -0.0939 -0.0542 -0.0722 72 ASN B O 3099 C CB . ASN B 72 ? 1.2457 1.0320 0.8140 -0.0262 -0.0467 -0.1870 72 ASN B CB 3100 C CG . ASN B 72 ? 1.3208 1.0136 0.8546 -0.0537 -0.0887 -0.1735 72 ASN B CG 3101 O OD1 . ASN B 72 ? 1.3558 0.9991 0.9088 -0.0612 -0.1088 -0.1520 72 ASN B OD1 3102 N ND2 . ASN B 72 ? 1.4009 1.0772 0.8794 -0.0765 -0.1035 -0.1838 72 ASN B ND2 3103 N N . LEU B 73 ? 1.0581 0.9616 0.7018 -0.0893 -0.0088 -0.0749 73 LEU B N 3104 C CA . LEU B 73 ? 1.0421 0.9548 0.6933 -0.1132 -0.0171 -0.0289 73 LEU B CA 3105 C C . LEU B 73 ? 0.9907 0.9164 0.6894 -0.1082 -0.0068 -0.0038 73 LEU B C 3106 O O . LEU B 73 ? 0.9573 0.8878 0.6523 -0.1201 -0.0109 0.0277 73 LEU B O 3107 C CB . LEU B 73 ? 1.0974 1.0371 0.6991 -0.1358 -0.0149 -0.0180 73 LEU B CB 3108 C CG . LEU B 73 ? 1.1712 1.0968 0.7189 -0.1463 -0.0323 -0.0388 73 LEU B CG 3109 C CD1 . LEU B 73 ? 1.2120 1.1784 0.7059 -0.1687 -0.0253 -0.0302 73 LEU B CD1 3110 C CD2 . LEU B 73 ? 1.1690 1.0702 0.7244 -0.1600 -0.0644 -0.0178 73 LEU B CD2 3111 N N . GLU B 74 ? 0.9476 0.8688 0.6842 -0.0890 0.0006 -0.0188 74 GLU B N 3112 C CA . GLU B 74 ? 0.8971 0.8235 0.6763 -0.0837 0.0052 -0.0017 74 GLU B CA 3113 C C . GLU B 74 ? 0.8556 0.7673 0.6661 -0.0685 -0.0062 -0.0054 74 GLU B C 3114 O O . GLU B 74 ? 0.7922 0.7104 0.6345 -0.0561 0.0010 -0.0116 74 GLU B O 3115 C CB . GLU B 74 ? 0.8946 0.8532 0.6866 -0.0851 0.0285 -0.0142 74 GLU B CB 3116 C CG . GLU B 74 ? 0.9218 0.9087 0.6789 -0.1157 0.0408 -0.0005 74 GLU B CG 3117 C CD . GLU B 74 ? 0.9379 0.9856 0.7093 -0.1280 0.0655 -0.0139 74 GLU B CD 3118 O OE1 . GLU B 74 ? 0.9368 1.0191 0.7371 -0.1004 0.0755 -0.0492 74 GLU B OE1 3119 O OE2 . GLU B 74 ? 0.9759 1.0395 0.7271 -0.1681 0.0713 0.0127 74 GLU B OE2 3120 N N . ARG B 75 ? 0.8808 0.7794 0.6774 -0.0771 -0.0258 0.0009 75 ARG B N 3121 C CA . ARG B 75 ? 0.8773 0.7684 0.6905 -0.0779 -0.0393 0.0043 75 ARG B CA 3122 C C . ARG B 75 ? 0.8309 0.7623 0.6843 -0.0701 -0.0373 0.0204 75 ARG B C 3123 O O . ARG B 75 ? 0.8159 0.7541 0.6892 -0.0653 -0.0379 0.0191 75 ARG B O 3124 C CB . ARG B 75 ? 0.9598 0.8350 0.7411 -0.1054 -0.0637 0.0119 75 ARG B CB 3125 C CG . ARG B 75 ? 1.0622 0.8753 0.7935 -0.1091 -0.0753 -0.0131 75 ARG B CG 3126 C CD . ARG B 75 ? 1.1538 0.9191 0.8841 -0.0824 -0.0769 -0.0378 75 ARG B CD 3127 N NE . ARG B 75 ? 1.3186 1.0154 0.9973 -0.0711 -0.0948 -0.0721 75 ARG B NE 3128 C CZ . ARG B 75 ? 1.3958 1.0446 1.0653 -0.0338 -0.1042 -0.1036 75 ARG B CZ 3129 N NH1 . ARG B 75 ? 1.3592 1.0278 1.0699 -0.0112 -0.0960 -0.0998 75 ARG B NH1 3130 N NH2 . ARG B 75 ? 1.4838 1.0646 1.1007 -0.0137 -0.1257 -0.1432 75 ARG B NH2 3131 N N . ARG B 76 ? 0.8312 0.7869 0.6914 -0.0644 -0.0388 0.0331 76 ARG B N 3132 C CA . ARG B 76 ? 0.7807 0.7731 0.6747 -0.0443 -0.0421 0.0379 76 ARG B CA 3133 C C . ARG B 76 ? 0.7704 0.7448 0.6843 -0.0291 -0.0295 0.0257 76 ARG B C 3134 O O . ARG B 76 ? 0.7593 0.7617 0.6964 -0.0200 -0.0289 0.0194 76 ARG B O 3135 C CB . ARG B 76 ? 0.7837 0.7864 0.6742 -0.0289 -0.0554 0.0495 76 ARG B CB 3136 C CG . ARG B 76 ? 0.7795 0.8299 0.6620 -0.0408 -0.0720 0.0612 76 ARG B CG 3137 C CD . ARG B 76 ? 0.8149 0.8644 0.6872 -0.0195 -0.0906 0.0737 76 ARG B CD 3138 N NE . ARG B 76 ? 0.8366 0.8159 0.6681 -0.0337 -0.0861 0.0825 76 ARG B NE 3139 C CZ . ARG B 76 ? 0.8770 0.8145 0.6859 -0.0210 -0.1020 0.0989 76 ARG B CZ 3140 N NH1 . ARG B 76 ? 0.9181 0.8620 0.7425 0.0201 -0.1285 0.1026 76 ARG B NH1 3141 N NH2 . ARG B 76 ? 0.9103 0.8000 0.6762 -0.0491 -0.0945 0.1111 76 ARG B NH2 3142 N N . ILE B 77 ? 0.8015 0.7401 0.7034 -0.0331 -0.0200 0.0233 77 ILE B N 3143 C CA . ILE B 77 ? 0.8191 0.7477 0.7389 -0.0288 -0.0103 0.0124 77 ILE B CA 3144 C C . ILE B 77 ? 0.8111 0.7550 0.7456 -0.0282 -0.0006 -0.0033 77 ILE B C 3145 O O . ILE B 77 ? 0.7936 0.7475 0.7504 -0.0206 0.0019 -0.0126 77 ILE B O 3146 C CB . ILE B 77 ? 0.8495 0.7495 0.7496 -0.0478 -0.0049 0.0194 77 ILE B CB 3147 C CG1 . ILE B 77 ? 0.9008 0.8183 0.7790 -0.0675 0.0104 0.0163 77 ILE B CG1 3148 C CG2 . ILE B 77 ? 0.9086 0.7675 0.7856 -0.0444 -0.0260 0.0393 77 ILE B CG2 3149 C CD1 . ILE B 77 ? 0.9681 0.8850 0.8235 -0.0995 0.0192 0.0275 77 ILE B CD1 3150 N N . GLU B 78 ? 0.8121 0.7504 0.7293 -0.0328 -0.0007 -0.0083 78 GLU B N 3151 C CA . GLU B 78 ? 0.8168 0.7510 0.7401 -0.0227 -0.0037 -0.0222 78 GLU B CA 3152 C C . GLU B 78 ? 0.7711 0.7139 0.7047 -0.0236 -0.0166 -0.0108 78 GLU B C 3153 O O . GLU B 78 ? 0.7090 0.6591 0.6573 -0.0145 -0.0186 -0.0162 78 GLU B O 3154 C CB . GLU B 78 ? 0.9095 0.8121 0.7999 -0.0217 -0.0123 -0.0333 78 GLU B CB 3155 C CG . GLU B 78 ? 1.0002 0.8706 0.8849 -0.0038 -0.0290 -0.0467 78 GLU B CG 3156 C CD . GLU B 78 ? 1.1630 0.9771 1.0040 0.0038 -0.0470 -0.0646 78 GLU B CD 3157 O OE1 . GLU B 78 ? 1.2974 1.0867 1.1071 -0.0206 -0.0568 -0.0539 78 GLU B OE1 3158 O OE2 . GLU B 78 ? 1.2931 1.0883 1.1294 0.0380 -0.0550 -0.0935 78 GLU B OE2 3159 N N . ASN B 79 ? 0.7536 0.7110 0.6785 -0.0372 -0.0257 0.0056 79 ASN B N 3160 C CA . ASN B 79 ? 0.7835 0.7794 0.7157 -0.0465 -0.0349 0.0179 79 ASN B CA 3161 C C . ASN B 79 ? 0.7589 0.7961 0.7213 -0.0261 -0.0254 0.0080 79 ASN B C 3162 O O . ASN B 79 ? 0.7282 0.7949 0.6968 -0.0276 -0.0279 0.0086 79 ASN B O 3163 C CB . ASN B 79 ? 0.8260 0.8609 0.7492 -0.0671 -0.0443 0.0342 79 ASN B CB 3164 C CG . ASN B 79 ? 0.8373 0.9368 0.7628 -0.0901 -0.0527 0.0499 79 ASN B CG 3165 O OD1 . ASN B 79 ? 0.9276 0.9996 0.8318 -0.1123 -0.0642 0.0614 79 ASN B OD1 3166 N ND2 . ASN B 79 ? 0.8362 1.0275 0.7839 -0.0850 -0.0500 0.0509 79 ASN B ND2 3167 N N . LEU B 80 ? 0.7593 0.7891 0.7315 -0.0092 -0.0192 -0.0008 80 LEU B N 3168 C CA . LEU B 80 ? 0.7513 0.7934 0.7417 0.0127 -0.0178 -0.0162 80 LEU B CA 3169 C C . LEU B 80 ? 0.7155 0.7456 0.7145 0.0101 -0.0119 -0.0270 80 LEU B C 3170 O O . LEU B 80 ? 0.6871 0.7484 0.6963 0.0184 -0.0135 -0.0373 80 LEU B O 3171 C CB . LEU B 80 ? 0.8062 0.8045 0.7890 0.0238 -0.0225 -0.0180 80 LEU B CB 3172 C CG . LEU B 80 ? 0.8481 0.8359 0.8364 0.0540 -0.0347 -0.0360 80 LEU B CG 3173 C CD1 . LEU B 80 ? 0.9044 0.8257 0.8697 0.0612 -0.0513 -0.0271 80 LEU B CD1 3174 C CD2 . LEU B 80 ? 0.8932 0.8626 0.8880 0.0499 -0.0312 -0.0531 80 LEU B CD2 3175 N N . ASN B 81 ? 0.7291 0.7287 0.7239 0.0002 -0.0055 -0.0273 81 ASN B N 3176 C CA . ASN B 81 ? 0.7157 0.7224 0.7248 0.0008 -0.0016 -0.0394 81 ASN B CA 3177 C C . ASN B 81 ? 0.7359 0.7613 0.7455 0.0057 -0.0115 -0.0366 81 ASN B C 3178 O O . ASN B 81 ? 0.7119 0.7596 0.7347 0.0108 -0.0141 -0.0456 81 ASN B O 3179 C CB . ASN B 81 ? 0.7236 0.7239 0.7297 -0.0043 0.0071 -0.0443 81 ASN B CB 3180 C CG . ASN B 81 ? 0.7269 0.7608 0.7567 0.0000 0.0110 -0.0607 81 ASN B CG 3181 O OD1 . ASN B 81 ? 0.7763 0.8254 0.8201 -0.0130 0.0146 -0.0662 81 ASN B OD1 3182 N ND2 . ASN B 81 ? 0.6981 0.7411 0.7299 0.0194 0.0052 -0.0703 81 ASN B ND2 3183 N N . LYS B 82 ? 0.7713 0.7813 0.7592 -0.0017 -0.0217 -0.0211 82 LYS B N 3184 C CA . LYS B 82 ? 0.8151 0.8215 0.7872 -0.0073 -0.0395 -0.0084 82 LYS B CA 3185 C C . LYS B 82 ? 0.7979 0.8613 0.7726 -0.0168 -0.0399 -0.0008 82 LYS B C 3186 O O . LYS B 82 ? 0.7559 0.8364 0.7276 -0.0170 -0.0486 0.0018 82 LYS B O 3187 C CB . LYS B 82 ? 0.9213 0.8798 0.8569 -0.0247 -0.0573 0.0095 82 LYS B CB 3188 C CG . LYS B 82 ? 1.0581 0.9768 0.9610 -0.0353 -0.0872 0.0284 82 LYS B CG 3189 C CD . LYS B 82 ? 1.2228 1.0891 1.0782 -0.0710 -0.1113 0.0532 82 LYS B CD 3190 C CE . LYS B 82 ? 1.3845 1.1930 1.1923 -0.0938 -0.1501 0.0822 82 LYS B CE 3191 N NZ . LYS B 82 ? 1.5159 1.2521 1.2664 -0.1396 -0.1812 0.1083 82 LYS B NZ 3192 N N . LYS B 83 ? 0.8067 0.9096 0.7857 -0.0210 -0.0320 0.0003 83 LYS B N 3193 C CA . LYS B 83 ? 0.8073 0.9911 0.7915 -0.0213 -0.0292 -0.0028 83 LYS B CA 3194 C C . LYS B 83 ? 0.7606 0.9590 0.7626 0.0042 -0.0231 -0.0318 83 LYS B C 3195 O O . LYS B 83 ? 0.7372 0.9935 0.7349 0.0033 -0.0244 -0.0373 83 LYS B O 3196 C CB . LYS B 83 ? 0.8478 1.0832 0.8403 -0.0163 -0.0244 -0.0050 83 LYS B CB 3197 C CG . LYS B 83 ? 0.9594 1.2829 0.9393 -0.0491 -0.0290 0.0172 83 LYS B CG 3198 C CD . LYS B 83 ? 1.0630 1.3360 1.0058 -0.0983 -0.0464 0.0543 83 LYS B CD 3199 C CE . LYS B 83 ? 1.1539 1.5233 1.0779 -0.1487 -0.0535 0.0831 83 LYS B CE 3200 N NZ . LYS B 83 ? 1.2220 1.5547 1.0986 -0.1984 -0.0757 0.1197 83 LYS B NZ 3201 N N . MET B 84 ? 0.7537 0.9001 0.7691 0.0196 -0.0187 -0.0489 84 MET B N 3202 C CA . MET B 84 ? 0.7160 0.8560 0.7417 0.0326 -0.0188 -0.0750 84 MET B CA 3203 C C . MET B 84 ? 0.6697 0.8232 0.6967 0.0236 -0.0240 -0.0729 84 MET B C 3204 O O . MET B 84 ? 0.6971 0.8890 0.7222 0.0282 -0.0279 -0.0880 84 MET B O 3205 C CB . MET B 84 ? 0.7508 0.8278 0.7813 0.0317 -0.0170 -0.0819 84 MET B CB 3206 C CG . MET B 84 ? 0.7954 0.8439 0.8243 0.0394 -0.0252 -0.1083 84 MET B CG 3207 S SD . MET B 84 ? 0.8531 0.8925 0.8937 0.0124 -0.0257 -0.1150 84 MET B SD 3208 C CE . MET B 84 ? 0.8304 0.8542 0.8764 -0.0104 -0.0131 -0.0924 84 MET B CE 3209 N N . GLU B 85 ? 1.0093 1.1446 0.8458 0.0860 -0.0433 -0.0363 85 GLU B N 3210 C CA . GLU B 85 ? 0.9786 1.1227 0.8272 0.0884 -0.0391 -0.0479 85 GLU B CA 3211 C C . GLU B 85 ? 0.9315 1.0446 0.7982 0.0847 -0.0524 -0.0553 85 GLU B C 3212 O O . GLU B 85 ? 0.8845 0.9972 0.7714 0.0783 -0.0451 -0.0530 85 GLU B O 3213 C CB . GLU B 85 ? 1.0254 1.1966 0.8507 0.1115 -0.0410 -0.0662 85 GLU B CB 3214 C CG . GLU B 85 ? 1.0836 1.2999 0.8922 0.1105 -0.0261 -0.0564 85 GLU B CG 3215 C CD . GLU B 85 ? 1.1304 1.4130 0.9339 0.1228 -0.0137 -0.0638 85 GLU B CD 3216 O OE1 . GLU B 85 ? 1.1942 1.4897 0.9781 0.1581 -0.0230 -0.0863 85 GLU B OE1 3217 O OE2 . GLU B 85 ? 1.1533 1.4767 0.9645 0.0973 0.0037 -0.0466 85 GLU B OE2 3218 N N . ASP B 86 ? 0.9313 1.0200 0.7870 0.0834 -0.0727 -0.0622 86 ASP B N 3219 C CA . ASP B 86 ? 0.9219 0.9819 0.7875 0.0692 -0.0879 -0.0645 86 ASP B CA 3220 C C . ASP B 86 ? 0.8624 0.9359 0.7621 0.0551 -0.0795 -0.0459 86 ASP B C 3221 O O . ASP B 86 ? 0.8410 0.9020 0.7575 0.0464 -0.0816 -0.0459 86 ASP B O 3222 C CB . ASP B 86 ? 0.9760 1.0148 0.8146 0.0572 -0.1133 -0.0706 86 ASP B CB 3223 C CG . ASP B 86 ? 1.0553 1.0428 0.8440 0.0691 -0.1318 -0.0935 86 ASP B CG 3224 O OD1 . ASP B 86 ? 1.1162 1.0720 0.8959 0.0789 -0.1339 -0.1036 86 ASP B OD1 3225 O OD2 . ASP B 86 ? 1.1059 1.0795 0.8568 0.0727 -0.1457 -0.1022 86 ASP B OD2 3226 N N . GLY B 87 ? 0.8296 0.9241 0.7312 0.0578 -0.0715 -0.0308 87 GLY B N 3227 C CA . GLY B 87 ? 0.8011 0.9031 0.7196 0.0569 -0.0647 -0.0145 87 GLY B CA 3228 C C . GLY B 87 ? 0.7799 0.8639 0.7099 0.0542 -0.0502 -0.0117 87 GLY B C 3229 O O . GLY B 87 ? 0.7488 0.8300 0.6980 0.0497 -0.0512 -0.0077 87 GLY B O 3230 N N . PHE B 88 ? 0.7684 0.8485 0.6854 0.0538 -0.0374 -0.0132 88 PHE B N 3231 C CA . PHE B 88 ? 0.7625 0.8351 0.6861 0.0436 -0.0246 -0.0096 88 PHE B CA 3232 C C . PHE B 88 ? 0.7559 0.8347 0.7041 0.0426 -0.0289 -0.0238 88 PHE B C 3233 O O . PHE B 88 ? 0.7455 0.8161 0.7092 0.0349 -0.0242 -0.0201 88 PHE B O 3234 C CB . PHE B 88 ? 0.7801 0.8654 0.6799 0.0342 -0.0112 -0.0045 88 PHE B CB 3235 C CG . PHE B 88 ? 0.8131 0.8667 0.6736 0.0291 -0.0063 0.0142 88 PHE B CG 3236 C CD1 . PHE B 88 ? 0.8291 0.8349 0.6697 0.0246 -0.0045 0.0275 88 PHE B CD1 3237 C CD2 . PHE B 88 ? 0.8473 0.9091 0.6798 0.0326 -0.0052 0.0180 88 PHE B CD2 3238 C CE1 . PHE B 88 ? 0.8798 0.8346 0.6638 0.0263 -0.0035 0.0439 88 PHE B CE1 3239 C CE2 . PHE B 88 ? 0.8963 0.9149 0.6795 0.0301 -0.0027 0.0360 88 PHE B CE2 3240 C CZ . PHE B 88 ? 0.9264 0.8853 0.6804 0.0283 -0.0028 0.0488 88 PHE B CZ 3241 N N . LEU B 89 ? 0.7745 0.8582 0.7168 0.0534 -0.0397 -0.0403 89 LEU B N 3242 C CA . LEU B 89 ? 0.7903 0.8620 0.7385 0.0593 -0.0479 -0.0545 89 LEU B CA 3243 C C . LEU B 89 ? 0.7623 0.8091 0.7272 0.0459 -0.0583 -0.0490 89 LEU B C 3244 O O . LEU B 89 ? 0.7333 0.7730 0.7126 0.0435 -0.0565 -0.0507 89 LEU B O 3245 C CB . LEU B 89 ? 0.8464 0.9023 0.7619 0.0787 -0.0635 -0.0740 89 LEU B CB 3246 C CG . LEU B 89 ? 0.9050 0.9982 0.8003 0.1014 -0.0548 -0.0835 89 LEU B CG 3247 C CD1 . LEU B 89 ? 0.9692 1.0256 0.8177 0.1283 -0.0757 -0.1055 89 LEU B CD1 3248 C CD2 . LEU B 89 ? 0.8905 1.0364 0.8011 0.1074 -0.0373 -0.0836 89 LEU B CD2 3249 N N . ASP B 90 ? 0.7633 0.8083 0.7258 0.0365 -0.0692 -0.0418 90 ASP B N 3250 C CA . ASP B 90 ? 0.7483 0.7926 0.7265 0.0204 -0.0790 -0.0337 90 ASP B CA 3251 C C . ASP B 90 ? 0.7076 0.7649 0.7109 0.0222 -0.0639 -0.0208 90 ASP B C 3252 O O . ASP B 90 ? 0.6827 0.7358 0.7020 0.0144 -0.0662 -0.0191 90 ASP B O 3253 C CB . ASP B 90 ? 0.7626 0.8300 0.7338 0.0092 -0.0926 -0.0261 90 ASP B CB 3254 C CG . ASP B 90 ? 0.8419 0.8813 0.7778 -0.0015 -0.1138 -0.0390 90 ASP B CG 3255 O OD1 . ASP B 90 ? 0.8839 0.8746 0.7951 0.0022 -0.1218 -0.0541 90 ASP B OD1 3256 O OD2 . ASP B 90 ? 0.9076 0.9697 0.8320 -0.0109 -0.1242 -0.0348 90 ASP B OD2 3257 N N . VAL B 91 ? 0.7045 0.7676 0.7010 0.0325 -0.0502 -0.0118 91 VAL B N 3258 C CA . VAL B 91 ? 0.6955 0.7486 0.6942 0.0365 -0.0385 -0.0008 91 VAL B CA 3259 C C . VAL B 91 ? 0.6898 0.7295 0.6997 0.0276 -0.0304 -0.0063 91 VAL B C 3260 O O . VAL B 91 ? 0.6984 0.7309 0.7204 0.0260 -0.0285 -0.0020 91 VAL B O 3261 C CB . VAL B 91 ? 0.7145 0.7501 0.6793 0.0460 -0.0292 0.0095 91 VAL B CB 3262 C CG1 . VAL B 91 ? 0.7250 0.7225 0.6702 0.0451 -0.0198 0.0186 91 VAL B CG1 3263 C CG2 . VAL B 91 ? 0.7193 0.7736 0.6714 0.0640 -0.0369 0.0173 91 VAL B CG2 3264 N N . TRP B 92 ? 0.6853 0.7319 0.6904 0.0247 -0.0255 -0.0157 92 TRP B N 3265 C CA . TRP B 92 ? 0.6700 0.7242 0.6858 0.0181 -0.0178 -0.0208 92 TRP B CA 3266 C C . TRP B 92 ? 0.6586 0.7097 0.6917 0.0240 -0.0280 -0.0325 92 TRP B C 3267 O O . TRP B 92 ? 0.6610 0.7148 0.7073 0.0207 -0.0237 -0.0338 92 TRP B O 3268 C CB . TRP B 92 ? 0.6655 0.7522 0.6688 0.0158 -0.0087 -0.0253 92 TRP B CB 3269 C CG . TRP B 92 ? 0.7006 0.7805 0.6784 -0.0031 0.0020 -0.0097 92 TRP B CG 3270 C CD1 . TRP B 92 ? 0.7309 0.8125 0.6824 -0.0045 0.0043 -0.0038 92 TRP B CD1 3271 C CD2 . TRP B 92 ? 0.7078 0.7633 0.6702 -0.0263 0.0092 0.0029 92 TRP B CD2 3272 N NE1 . TRP B 92 ? 0.7636 0.8181 0.6796 -0.0288 0.0118 0.0129 92 TRP B NE1 3273 C CE2 . TRP B 92 ? 0.7509 0.7840 0.6690 -0.0436 0.0139 0.0169 92 TRP B CE2 3274 C CE3 . TRP B 92 ? 0.6999 0.7430 0.6738 -0.0356 0.0103 0.0038 92 TRP B CE3 3275 C CZ2 . TRP B 92 ? 0.7995 0.7855 0.6740 -0.0730 0.0172 0.0320 92 TRP B CZ2 3276 C CZ3 . TRP B 92 ? 0.7316 0.7365 0.6692 -0.0626 0.0148 0.0173 92 TRP B CZ3 3277 C CH2 . TRP B 92 ? 0.7912 0.7616 0.6746 -0.0825 0.0170 0.0314 92 TRP B CH2 3278 N N . THR B 93 ? 0.6701 0.7080 0.6941 0.0299 -0.0435 -0.0403 93 THR B N 3279 C CA . THR B 93 ? 0.6771 0.6898 0.6987 0.0302 -0.0578 -0.0488 93 THR B CA 3280 C C . THR B 93 ? 0.6702 0.6812 0.7138 0.0148 -0.0593 -0.0361 93 THR B C 3281 O O . THR B 93 ? 0.6668 0.6664 0.7186 0.0130 -0.0612 -0.0384 93 THR B O 3282 C CB . THR B 93 ? 0.7180 0.6997 0.7061 0.0309 -0.0786 -0.0580 93 THR B CB 3283 O OG1 . THR B 93 ? 0.7493 0.7328 0.7113 0.0547 -0.0776 -0.0728 93 THR B OG1 3284 C CG2 . THR B 93 ? 0.7525 0.6867 0.7200 0.0227 -0.0978 -0.0634 93 THR B CG2 3285 N N . TYR B 94 ? 0.6685 0.6975 0.7186 0.0089 -0.0584 -0.0229 94 TYR B N 3286 C CA . TYR B 94 ? 0.6506 0.6965 0.7188 0.0028 -0.0585 -0.0101 94 TYR B CA 3287 C C . TYR B 94 ? 0.6410 0.6795 0.7199 0.0095 -0.0439 -0.0076 94 TYR B C 3288 O O . TYR B 94 ? 0.6203 0.6578 0.7134 0.0047 -0.0454 -0.0064 94 TYR B O 3289 C CB . TYR B 94 ? 0.6609 0.7402 0.7261 0.0085 -0.0594 0.0021 94 TYR B CB 3290 C CG . TYR B 94 ? 0.6544 0.7643 0.7313 0.0178 -0.0560 0.0152 94 TYR B CG 3291 C CD1 . TYR B 94 ? 0.6602 0.7511 0.7243 0.0400 -0.0430 0.0199 94 TYR B CD1 3292 C CD2 . TYR B 94 ? 0.6485 0.8059 0.7394 0.0038 -0.0675 0.0234 94 TYR B CD2 3293 C CE1 . TYR B 94 ? 0.6606 0.7734 0.7234 0.0593 -0.0413 0.0294 94 TYR B CE1 3294 C CE2 . TYR B 94 ? 0.6346 0.8365 0.7349 0.0197 -0.0636 0.0350 94 TYR B CE2 3295 C CZ . TYR B 94 ? 0.6465 0.8230 0.7314 0.0532 -0.0503 0.0364 94 TYR B CZ 3296 O OH . TYR B 94 ? 0.6530 0.8659 0.7351 0.0797 -0.0477 0.0454 94 TYR B OH 3297 N N . ASN B 95 ? 0.6682 0.6977 0.7338 0.0156 -0.0315 -0.0062 95 ASN B N 3298 C CA . ASN B 95 ? 0.6689 0.6824 0.7314 0.0131 -0.0204 -0.0028 95 ASN B CA 3299 C C . ASN B 95 ? 0.6667 0.6855 0.7483 0.0063 -0.0198 -0.0121 95 ASN B C 3300 O O . ASN B 95 ? 0.6701 0.6823 0.7609 0.0042 -0.0177 -0.0092 95 ASN B O 3301 C CB . ASN B 95 ? 0.6936 0.6916 0.7265 0.0067 -0.0107 0.0008 95 ASN B CB 3302 C CG . ASN B 95 ? 0.7506 0.7240 0.7493 0.0187 -0.0111 0.0121 95 ASN B CG 3303 O OD1 . ASN B 95 ? 0.7703 0.7493 0.7704 0.0372 -0.0169 0.0172 95 ASN B OD1 3304 N ND2 . ASN B 95 ? 0.7969 0.7483 0.7595 0.0094 -0.0056 0.0171 95 ASN B ND2 3305 N N . ALA B 96 ? 0.6536 0.6849 0.7355 0.0087 -0.0225 -0.0241 96 ALA B N 3306 C CA . ALA B 96 ? 0.6416 0.6824 0.7329 0.0127 -0.0229 -0.0346 96 ALA B CA 3307 C C . ALA B 96 ? 0.6303 0.6497 0.7301 0.0137 -0.0348 -0.0356 96 ALA B C 3308 O O . ALA B 96 ? 0.6124 0.6329 0.7242 0.0128 -0.0322 -0.0359 96 ALA B O 3309 C CB . ALA B 96 ? 0.6508 0.7106 0.7279 0.0285 -0.0254 -0.0488 96 ALA B CB 3310 N N . GLU B 97 ? 0.6459 0.6474 0.7354 0.0103 -0.0490 -0.0344 97 GLU B N 3311 C CA . GLU B 97 ? 0.6690 0.6492 0.7567 0.0005 -0.0628 -0.0321 97 GLU B CA 3312 C C . GLU B 97 ? 0.6411 0.6420 0.7537 -0.0088 -0.0568 -0.0181 97 GLU B C 3313 O O . GLU B 97 ? 0.6306 0.6236 0.7493 -0.0134 -0.0603 -0.0168 97 GLU B O 3314 C CB . GLU B 97 ? 0.7093 0.6664 0.7698 -0.0130 -0.0824 -0.0318 97 GLU B CB 3315 C CG . GLU B 97 ? 0.7789 0.6919 0.7972 0.0029 -0.0943 -0.0495 97 GLU B CG 3316 C CD . GLU B 97 ? 0.8534 0.7289 0.8304 -0.0135 -0.1161 -0.0506 97 GLU B CD 3317 O OE1 . GLU B 97 ? 0.8792 0.7755 0.8655 -0.0439 -0.1228 -0.0358 97 GLU B OE1 3318 O OE2 . GLU B 97 ? 0.9391 0.7682 0.8691 0.0054 -0.1278 -0.0666 97 GLU B OE2 3319 N N . LEU B 98 ? 0.6300 0.6547 0.7497 -0.0058 -0.0485 -0.0081 98 LEU B N 3320 C CA . LEU B 98 ? 0.6013 0.6470 0.7334 -0.0028 -0.0440 0.0037 98 LEU B CA 3321 C C . LEU B 98 ? 0.5885 0.6181 0.7246 0.0035 -0.0328 0.0009 98 LEU B C 3322 O O . LEU B 98 ? 0.5845 0.6211 0.7308 0.0044 -0.0324 0.0056 98 LEU B O 3323 C CB . LEU B 98 ? 0.6133 0.6801 0.7356 0.0113 -0.0401 0.0130 98 LEU B CB 3324 C CG . LEU B 98 ? 0.6076 0.7006 0.7310 0.0284 -0.0369 0.0239 98 LEU B CG 3325 C CD1 . LEU B 98 ? 0.5939 0.7446 0.7361 0.0146 -0.0478 0.0331 98 LEU B CD1 3326 C CD2 . LEU B 98 ? 0.6362 0.7270 0.7300 0.0571 -0.0321 0.0295 98 LEU B CD2 3327 N N . LEU B 99 ? 0.5980 0.6124 0.7240 0.0040 -0.0243 -0.0057 99 LEU B N 3328 C CA . LEU B 99 ? 0.6133 0.6170 0.7373 0.0004 -0.0155 -0.0073 99 LEU B CA 3329 C C . LEU B 99 ? 0.5938 0.6059 0.7371 -0.0015 -0.0190 -0.0146 99 LEU B C 3330 O O . LEU B 99 ? 0.5928 0.6018 0.7422 -0.0027 -0.0161 -0.0126 99 LEU B O 3331 C CB . LEU B 99 ? 0.6569 0.6585 0.7629 -0.0097 -0.0075 -0.0101 99 LEU B CB 3332 C CG . LEU B 99 ? 0.7089 0.7029 0.8031 -0.0263 -0.0003 -0.0091 99 LEU B CG 3333 C CD1 . LEU B 99 ? 0.7521 0.6976 0.8152 -0.0239 -0.0003 0.0004 99 LEU B CD1 3334 C CD2 . LEU B 99 ? 0.7485 0.7607 0.8247 -0.0470 0.0061 -0.0093 99 LEU B CD2 3335 N N . VAL B 100 ? 0.5837 0.5987 0.7274 0.0022 -0.0268 -0.0238 100 VAL B N 3336 C CA . VAL B 100 ? 0.5724 0.5822 0.7194 0.0077 -0.0332 -0.0314 100 VAL B CA 3337 C C . VAL B 100 ? 0.5512 0.5492 0.7053 0.0001 -0.0409 -0.0223 100 VAL B C 3338 O O . VAL B 100 ? 0.5064 0.5047 0.6690 0.0015 -0.0395 -0.0227 100 VAL B O 3339 C CB . VAL B 100 ? 0.6013 0.5973 0.7255 0.0222 -0.0440 -0.0444 100 VAL B CB 3340 C CG1 . VAL B 100 ? 0.6280 0.5935 0.7362 0.0320 -0.0568 -0.0504 100 VAL B CG1 3341 C CG2 . VAL B 100 ? 0.6033 0.6374 0.7258 0.0344 -0.0337 -0.0539 100 VAL B CG2 3342 N N . LEU B 101 ? 0.5506 0.5491 0.7010 -0.0101 -0.0491 -0.0129 101 LEU B N 3343 C CA . LEU B 101 ? 0.5506 0.5599 0.7077 -0.0233 -0.0562 -0.0007 101 LEU B CA 3344 C C . LEU B 101 ? 0.5414 0.5756 0.7166 -0.0142 -0.0440 0.0063 101 LEU B C 3345 O O . LEU B 101 ? 0.5463 0.5832 0.7292 -0.0167 -0.0449 0.0093 101 LEU B O 3346 C CB . LEU B 101 ? 0.5557 0.5872 0.7068 -0.0399 -0.0663 0.0103 101 LEU B CB 3347 C CG . LEU B 101 ? 0.6012 0.5967 0.7205 -0.0585 -0.0852 0.0065 101 LEU B CG 3348 C CD1 . LEU B 101 ? 0.6036 0.6409 0.7211 -0.0826 -0.0945 0.0207 101 LEU B CD1 3349 C CD2 . LEU B 101 ? 0.6416 0.5851 0.7322 -0.0715 -0.1006 0.0040 101 LEU B CD2 3350 N N . MET B 102 ? 0.5449 0.5876 0.7169 -0.0016 -0.0343 0.0086 102 MET B N 3351 C CA . MET B 102 ? 0.5630 0.6097 0.7315 0.0133 -0.0262 0.0137 102 MET B CA 3352 C C . MET B 102 ? 0.5721 0.5949 0.7413 0.0115 -0.0204 0.0062 102 MET B C 3353 O O . MET B 102 ? 0.5983 0.6256 0.7701 0.0178 -0.0191 0.0096 102 MET B O 3354 C CB . MET B 102 ? 0.6145 0.6472 0.7564 0.0299 -0.0205 0.0160 102 MET B CB 3355 C CG . MET B 102 ? 0.6524 0.7237 0.7918 0.0408 -0.0254 0.0249 102 MET B CG 3356 S SD . MET B 102 ? 0.7536 0.7916 0.8454 0.0709 -0.0203 0.0272 102 MET B SD 3357 C CE . MET B 102 ? 0.8118 0.8738 0.8839 0.1107 -0.0203 0.0349 102 MET B CE 3358 N N . GLU B 103 ? 0.5657 0.5739 0.7318 0.0033 -0.0172 -0.0035 103 GLU B N 3359 C CA . GLU B 103 ? 0.5727 0.5750 0.7387 -0.0025 -0.0121 -0.0096 103 GLU B CA 3360 C C . GLU B 103 ? 0.5514 0.5663 0.7365 -0.0013 -0.0171 -0.0145 103 GLU B C 3361 O O . GLU B 103 ? 0.5424 0.5595 0.7312 -0.0025 -0.0143 -0.0164 103 GLU B O 3362 C CB . GLU B 103 ? 0.5985 0.6032 0.7523 -0.0148 -0.0065 -0.0155 103 GLU B CB 3363 C CG . GLU B 103 ? 0.6488 0.6209 0.7669 -0.0214 -0.0026 -0.0087 103 GLU B CG 3364 C CD . GLU B 103 ? 0.6971 0.6278 0.7832 -0.0240 -0.0019 -0.0045 103 GLU B CD 3365 O OE1 . GLU B 103 ? 0.6725 0.6114 0.7677 -0.0323 -0.0015 -0.0082 103 GLU B OE1 3366 O OE2 . GLU B 103 ? 0.7789 0.6630 0.8223 -0.0140 -0.0034 0.0019 103 GLU B OE2 3367 N N . ASN B 104 ? 0.5559 0.5696 0.7433 0.0007 -0.0267 -0.0163 104 ASN B N 3368 C CA . ASN B 104 ? 0.5424 0.5474 0.7304 0.0030 -0.0356 -0.0184 104 ASN B CA 3369 C C . ASN B 104 ? 0.5368 0.5489 0.7344 -0.0025 -0.0362 -0.0066 104 ASN B C 3370 O O . ASN B 104 ? 0.4923 0.5039 0.6943 0.0004 -0.0362 -0.0079 104 ASN B O 3371 C CB . ASN B 104 ? 0.5633 0.5403 0.7292 0.0018 -0.0507 -0.0205 104 ASN B CB 3372 C CG . ASN B 104 ? 0.5837 0.5533 0.7318 0.0200 -0.0526 -0.0360 104 ASN B CG 3373 O OD1 . ASN B 104 ? 0.5669 0.5689 0.7255 0.0304 -0.0419 -0.0439 104 ASN B OD1 3374 N ND2 . ASN B 104 ? 0.6194 0.5502 0.7342 0.0229 -0.0675 -0.0400 104 ASN B ND2 3375 N N . GLU B 105 ? 0.5503 0.5794 0.7502 -0.0071 -0.0366 0.0052 105 GLU B N 3376 C CA . GLU B 105 ? 0.5616 0.6172 0.7696 -0.0063 -0.0358 0.0167 105 GLU B CA 3377 C C . GLU B 105 ? 0.5384 0.5878 0.7463 0.0084 -0.0255 0.0119 105 GLU B C 3378 O O . GLU B 105 ? 0.4996 0.5566 0.7133 0.0101 -0.0257 0.0144 105 GLU B O 3379 C CB . GLU B 105 ? 0.6129 0.7084 0.8210 -0.0038 -0.0361 0.0288 105 GLU B CB 3380 C CG . GLU B 105 ? 0.6893 0.8370 0.9058 -0.0079 -0.0393 0.0437 105 GLU B CG 3381 C CD . GLU B 105 ? 0.8017 1.0092 1.0195 -0.0183 -0.0455 0.0576 105 GLU B CD 3382 O OE1 . GLU B 105 ? 0.9158 1.1455 1.1283 0.0066 -0.0396 0.0576 105 GLU B OE1 3383 O OE2 . GLU B 105 ? 0.8178 1.0472 1.0347 -0.0534 -0.0580 0.0692 105 GLU B OE2 3384 N N . ARG B 106 ? 0.5395 0.5688 0.7331 0.0147 -0.0185 0.0058 106 ARG B N 3385 C CA . ARG B 106 ? 0.6048 0.6121 0.7812 0.0207 -0.0127 0.0021 106 ARG B CA 3386 C C . ARG B 106 ? 0.5700 0.5766 0.7567 0.0093 -0.0119 -0.0068 106 ARG B C 3387 O O . ARG B 106 ? 0.5692 0.5676 0.7480 0.0110 -0.0103 -0.0081 106 ARG B O 3388 C CB . ARG B 106 ? 0.6752 0.6459 0.8154 0.0227 -0.0091 0.0007 106 ARG B CB 3389 C CG . ARG B 106 ? 0.7322 0.7060 0.8543 0.0459 -0.0104 0.0090 106 ARG B CG 3390 C CD . ARG B 106 ? 0.8638 0.7766 0.9256 0.0603 -0.0098 0.0085 106 ARG B CD 3391 N NE . ARG B 106 ? 0.9538 0.8405 0.9825 0.0833 -0.0114 0.0083 106 ARG B NE 3392 C CZ . ARG B 106 ? 1.0596 0.8677 1.0251 0.0826 -0.0143 0.0041 106 ARG B CZ 3393 N NH1 . ARG B 106 ? 1.1319 0.8858 1.0620 0.0523 -0.0155 0.0022 106 ARG B NH1 3394 N NH2 . ARG B 106 ? 1.1586 0.9399 1.0884 0.1092 -0.0176 0.0025 106 ARG B NH2 3395 N N . THR B 107 ? 0.5430 0.5617 0.7425 0.0025 -0.0142 -0.0134 107 THR B N 3396 C CA . THR B 107 ? 0.4994 0.5338 0.7069 0.0006 -0.0142 -0.0224 107 THR B CA 3397 C C . THR B 107 ? 0.4828 0.5185 0.7000 0.0086 -0.0197 -0.0195 107 THR B C 3398 O O . THR B 107 ? 0.4446 0.4890 0.6645 0.0091 -0.0178 -0.0229 107 THR B O 3399 C CB . THR B 107 ? 0.5015 0.5544 0.7105 0.0044 -0.0162 -0.0316 107 THR B CB 3400 O OG1 . THR B 107 ? 0.5009 0.5644 0.7008 -0.0088 -0.0095 -0.0331 107 THR B OG1 3401 C CG2 . THR B 107 ? 0.4983 0.5806 0.7124 0.0152 -0.0181 -0.0413 107 THR B CG2 3402 N N . LEU B 108 ? 0.4630 0.4901 0.6805 0.0097 -0.0275 -0.0118 108 LEU B N 3403 C CA . LEU B 108 ? 0.4728 0.4975 0.6912 0.0098 -0.0342 -0.0054 108 LEU B CA 3404 C C . LEU B 108 ? 0.4695 0.5112 0.6951 0.0123 -0.0279 0.0017 108 LEU B C 3405 O O . LEU B 108 ? 0.4560 0.5007 0.6842 0.0160 -0.0282 0.0004 108 LEU B O 3406 C CB . LEU B 108 ? 0.4935 0.5038 0.6995 -0.0027 -0.0464 0.0051 108 LEU B CB 3407 C CG . LEU B 108 ? 0.5458 0.5202 0.7276 -0.0007 -0.0569 -0.0034 108 LEU B CG 3408 C CD1 . LEU B 108 ? 0.5859 0.5307 0.7402 -0.0235 -0.0735 0.0091 108 LEU B CD1 3409 C CD2 . LEU B 108 ? 0.5649 0.5215 0.7314 0.0215 -0.0604 -0.0177 108 LEU B CD2 3410 N N . ASP B 109 ? 0.4740 0.5258 0.6964 0.0161 -0.0232 0.0081 109 ASP B N 3411 C CA . ASP B 109 ? 0.4758 0.5375 0.6907 0.0304 -0.0183 0.0121 109 ASP B CA 3412 C C . ASP B 109 ? 0.4906 0.5247 0.6910 0.0328 -0.0140 0.0008 109 ASP B C 3413 O O . ASP B 109 ? 0.5307 0.5659 0.7241 0.0421 -0.0133 0.0012 109 ASP B O 3414 C CB . ASP B 109 ? 0.5067 0.5768 0.7060 0.0458 -0.0156 0.0178 109 ASP B CB 3415 C CG . ASP B 109 ? 0.5208 0.6423 0.7342 0.0407 -0.0204 0.0323 109 ASP B CG 3416 O OD1 . ASP B 109 ? 0.5022 0.6547 0.7292 0.0261 -0.0256 0.0421 109 ASP B OD1 3417 O OD2 . ASP B 109 ? 0.5680 0.7009 0.7735 0.0486 -0.0199 0.0352 109 ASP B OD2 3418 N N . PHE B 110 ? 0.4765 0.4914 0.6688 0.0205 -0.0122 -0.0083 110 PHE B N 3419 C CA . PHE B 110 ? 0.4767 0.4729 0.6495 0.0088 -0.0104 -0.0168 110 PHE B CA 3420 C C . PHE B 110 ? 0.4628 0.4844 0.6545 0.0069 -0.0120 -0.0213 110 PHE B C 3421 O O . PHE B 110 ? 0.4783 0.4891 0.6547 0.0056 -0.0123 -0.0238 110 PHE B O 3422 C CB . PHE B 110 ? 0.4885 0.4829 0.6534 -0.0117 -0.0086 -0.0219 110 PHE B CB 3423 C CG . PHE B 110 ? 0.5108 0.5040 0.6553 -0.0381 -0.0084 -0.0280 110 PHE B CG 3424 C CD1 . PHE B 110 ? 0.5608 0.5007 0.6569 -0.0484 -0.0115 -0.0274 110 PHE B CD1 3425 C CD2 . PHE B 110 ? 0.4888 0.5361 0.6535 -0.0533 -0.0070 -0.0340 110 PHE B CD2 3426 C CE1 . PHE B 110 ? 0.5991 0.5360 0.6677 -0.0851 -0.0144 -0.0310 110 PHE B CE1 3427 C CE2 . PHE B 110 ? 0.5199 0.5881 0.6668 -0.0860 -0.0076 -0.0371 110 PHE B CE2 3428 C CZ . PHE B 110 ? 0.5715 0.5820 0.6701 -0.1081 -0.0119 -0.0347 110 PHE B CZ 3429 N N . HIS B 111 ? 0.4431 0.4908 0.6592 0.0103 -0.0148 -0.0229 111 HIS B N 3430 C CA . HIS B 111 ? 0.4404 0.5077 0.6679 0.0172 -0.0182 -0.0264 111 HIS B CA 3431 C C . HIS B 111 ? 0.4427 0.5042 0.6707 0.0256 -0.0198 -0.0179 111 HIS B C 3432 O O . HIS B 111 ? 0.4490 0.5194 0.6768 0.0281 -0.0200 -0.0213 111 HIS B O 3433 C CB . HIS B 111 ? 0.4428 0.5145 0.6749 0.0284 -0.0249 -0.0287 111 HIS B CB 3434 C CG . HIS B 111 ? 0.4396 0.5370 0.6709 0.0305 -0.0236 -0.0397 111 HIS B CG 3435 N ND1 . HIS B 111 ? 0.4419 0.5866 0.6772 0.0289 -0.0207 -0.0489 111 HIS B ND1 3436 C CD2 . HIS B 111 ? 0.4401 0.5342 0.6661 0.0345 -0.0252 -0.0425 111 HIS B CD2 3437 C CE1 . HIS B 111 ? 0.4511 0.6306 0.6854 0.0331 -0.0195 -0.0561 111 HIS B CE1 3438 N NE2 . HIS B 111 ? 0.4508 0.5947 0.6783 0.0388 -0.0221 -0.0532 111 HIS B NE2 3439 N N . ASP B 112 ? 0.4252 0.4832 0.6540 0.0287 -0.0211 -0.0062 112 ASP B N 3440 C CA . ASP B 112 ? 0.4191 0.4914 0.6485 0.0356 -0.0217 0.0047 112 ASP B CA 3441 C C . ASP B 112 ? 0.4445 0.5091 0.6568 0.0472 -0.0166 -0.0002 112 ASP B C 3442 O O . ASP B 112 ? 0.4594 0.5322 0.6703 0.0539 -0.0170 0.0000 112 ASP B O 3443 C CB . ASP B 112 ? 0.4186 0.5103 0.6501 0.0332 -0.0233 0.0190 112 ASP B CB 3444 C CG . ASP B 112 ? 0.4361 0.5661 0.6711 0.0331 -0.0255 0.0344 112 ASP B CG 3445 O OD1 . ASP B 112 ? 0.4471 0.5773 0.6826 0.0342 -0.0269 0.0347 112 ASP B OD1 3446 O OD2 . ASP B 112 ? 0.4456 0.6158 0.6823 0.0312 -0.0258 0.0476 112 ASP B OD2 3447 N N . SER B 113 ? 0.4576 0.4955 0.6467 0.0495 -0.0139 -0.0049 113 SER B N 3448 C CA . SER B 113 ? 0.4892 0.4903 0.6379 0.0590 -0.0136 -0.0111 113 SER B CA 3449 C C . SER B 113 ? 0.5040 0.4945 0.6464 0.0419 -0.0157 -0.0212 113 SER B C 3450 O O . SER B 113 ? 0.5256 0.4992 0.6433 0.0513 -0.0178 -0.0241 113 SER B O 3451 C CB . SER B 113 ? 0.5211 0.4752 0.6312 0.0575 -0.0138 -0.0142 113 SER B CB 3452 O OG . SER B 113 ? 0.5881 0.4801 0.6382 0.0608 -0.0180 -0.0211 113 SER B OG 3453 N N . ASN B 114 ? 0.4775 0.4845 0.6382 0.0188 -0.0157 -0.0268 114 ASN B N 3454 C CA . ASN B 114 ? 0.4849 0.5051 0.6422 0.0004 -0.0180 -0.0354 114 ASN B CA 3455 C C . ASN B 114 ? 0.4641 0.5128 0.6423 0.0155 -0.0193 -0.0347 114 ASN B C 3456 O O . ASN B 114 ? 0.4749 0.5216 0.6375 0.0088 -0.0220 -0.0402 114 ASN B O 3457 C CB . ASN B 114 ? 0.4669 0.5273 0.6432 -0.0196 -0.0171 -0.0407 114 ASN B CB 3458 C CG . ASN B 114 ? 0.4974 0.5323 0.6468 -0.0433 -0.0162 -0.0406 114 ASN B CG 3459 O OD1 . ASN B 114 ? 0.5487 0.5245 0.6489 -0.0561 -0.0194 -0.0398 114 ASN B OD1 3460 N ND2 . ASN B 114 ? 0.4822 0.5531 0.6535 -0.0471 -0.0135 -0.0415 114 ASN B ND2 3461 N N . VAL B 115 ? 0.4427 0.5113 0.6480 0.0320 -0.0192 -0.0267 115 VAL B N 3462 C CA . VAL B 115 ? 0.4415 0.5293 0.6587 0.0441 -0.0218 -0.0231 115 VAL B CA 3463 C C . VAL B 115 ? 0.4601 0.5387 0.6610 0.0567 -0.0205 -0.0179 115 VAL B C 3464 O O . VAL B 115 ? 0.4683 0.5538 0.6642 0.0613 -0.0220 -0.0210 115 VAL B O 3465 C CB . VAL B 115 ? 0.4410 0.5347 0.6726 0.0500 -0.0259 -0.0130 115 VAL B CB 3466 C CG1 . VAL B 115 ? 0.4565 0.5584 0.6880 0.0581 -0.0300 -0.0054 115 VAL B CG1 3467 C CG2 . VAL B 115 ? 0.4481 0.5450 0.6835 0.0502 -0.0297 -0.0210 115 VAL B CG2 3468 N N . LYS B 116 ? 0.4759 0.5460 0.6659 0.0671 -0.0179 -0.0104 116 LYS B N 3469 C CA . LYS B 116 ? 0.5001 0.5713 0.6673 0.0907 -0.0166 -0.0063 116 LYS B CA 3470 C C . LYS B 116 ? 0.5393 0.5642 0.6628 0.0941 -0.0195 -0.0197 116 LYS B C 3471 O O . LYS B 116 ? 0.5358 0.5637 0.6442 0.1099 -0.0208 -0.0210 116 LYS B O 3472 C CB . LYS B 116 ? 0.5312 0.6099 0.6881 0.1074 -0.0141 0.0018 116 LYS B CB 3473 C CG . LYS B 116 ? 0.5693 0.6614 0.6944 0.1454 -0.0128 0.0052 116 LYS B CG 3474 C CD . LYS B 116 ? 0.5879 0.7388 0.7338 0.1520 -0.0115 0.0157 116 LYS B CD 3475 C CE . LYS B 116 ? 0.6383 0.8383 0.7612 0.1942 -0.0088 0.0233 116 LYS B CE 3476 N NZ . LYS B 116 ? 0.6300 0.9049 0.7791 0.1907 -0.0063 0.0410 116 LYS B NZ 3477 N N . ASN B 117 ? 0.5771 0.5566 0.6739 0.0746 -0.0220 -0.0290 117 ASN B N 3478 C CA . ASN B 117 ? 0.6585 0.5776 0.6965 0.0650 -0.0290 -0.0402 117 ASN B CA 3479 C C . ASN B 117 ? 0.6603 0.6044 0.7125 0.0442 -0.0321 -0.0467 117 ASN B C 3480 O O . ASN B 117 ? 0.7086 0.6172 0.7171 0.0454 -0.0386 -0.0535 117 ASN B O 3481 C CB . ASN B 117 ? 0.7034 0.5665 0.7008 0.0376 -0.0330 -0.0447 117 ASN B CB 3482 C CG . ASN B 117 ? 0.7492 0.5717 0.7130 0.0654 -0.0324 -0.0402 117 ASN B CG 3483 O OD1 . ASN B 117 ? 0.7684 0.5936 0.7176 0.1091 -0.0313 -0.0367 117 ASN B OD1 3484 N ND2 . ASN B 117 ? 0.7823 0.5777 0.7328 0.0427 -0.0330 -0.0398 117 ASN B ND2 3485 N N . LEU B 118 ? 0.6135 0.6170 0.7194 0.0294 -0.0290 -0.0453 118 LEU B N 3486 C CA . LEU B 118 ? 0.6106 0.6532 0.7324 0.0180 -0.0319 -0.0510 118 LEU B CA 3487 C C . LEU B 118 ? 0.6045 0.6601 0.7342 0.0461 -0.0314 -0.0466 118 LEU B C 3488 O O . LEU B 118 ? 0.6527 0.7079 0.7652 0.0435 -0.0358 -0.0529 118 LEU B O 3489 C CB . LEU B 118 ? 0.5860 0.6883 0.7530 0.0113 -0.0298 -0.0512 118 LEU B CB 3490 C CG . LEU B 118 ? 0.5758 0.7344 0.7587 0.0068 -0.0331 -0.0578 118 LEU B CG 3491 C CD1 . LEU B 118 ? 0.6358 0.7972 0.7870 -0.0310 -0.0387 -0.0664 118 LEU B CD1 3492 C CD2 . LEU B 118 ? 0.5496 0.7602 0.7640 0.0162 -0.0320 -0.0589 118 LEU B CD2 3493 N N . TYR B 119 ? 0.5672 0.6377 0.7190 0.0687 -0.0269 -0.0346 119 TYR B N 3494 C CA . TYR B 119 ? 0.5522 0.6437 0.7086 0.0911 -0.0260 -0.0266 119 TYR B CA 3495 C C . TYR B 119 ? 0.6077 0.6662 0.7165 0.1103 -0.0277 -0.0319 119 TYR B C 3496 O O . TYR B 119 ? 0.6259 0.6921 0.7246 0.1200 -0.0299 -0.0345 119 TYR B O 3497 C CB . TYR B 119 ? 0.5143 0.6343 0.6952 0.1000 -0.0225 -0.0094 119 TYR B CB 3498 C CG . TYR B 119 ? 0.5194 0.6742 0.7024 0.1161 -0.0214 0.0032 119 TYR B CG 3499 C CD1 . TYR B 119 ? 0.5110 0.6846 0.7082 0.1109 -0.0247 0.0092 119 TYR B CD1 3500 C CD2 . TYR B 119 ? 0.5290 0.7032 0.6946 0.1398 -0.0176 0.0100 119 TYR B CD2 3501 C CE1 . TYR B 119 ? 0.5097 0.7181 0.7056 0.1202 -0.0239 0.0233 119 TYR B CE1 3502 C CE2 . TYR B 119 ? 0.5294 0.7545 0.6979 0.1532 -0.0158 0.0234 119 TYR B CE2 3503 C CZ . TYR B 119 ? 0.5327 0.7735 0.7176 0.1390 -0.0188 0.0308 119 TYR B CZ 3504 O OH . TYR B 119 ? 0.5476 0.8409 0.7321 0.1469 -0.0172 0.0464 119 TYR B OH 3505 N N . ASP B 120 ? 0.6501 0.6654 0.7207 0.1208 -0.0281 -0.0343 120 ASP B N 3506 C CA . ASP B 120 ? 0.7348 0.7009 0.7398 0.1499 -0.0328 -0.0416 120 ASP B CA 3507 C C . ASP B 120 ? 0.7765 0.6858 0.7343 0.1271 -0.0431 -0.0568 120 ASP B C 3508 O O . ASP B 120 ? 0.8087 0.6992 0.7294 0.1470 -0.0479 -0.0625 120 ASP B O 3509 C CB . ASP B 120 ? 0.7930 0.7128 0.7518 0.1732 -0.0336 -0.0419 120 ASP B CB 3510 C CG . ASP B 120 ? 0.7701 0.7627 0.7662 0.2020 -0.0249 -0.0261 120 ASP B CG 3511 O OD1 . ASP B 120 ? 0.7614 0.8252 0.7903 0.2151 -0.0203 -0.0156 120 ASP B OD1 3512 O OD2 . ASP B 120 ? 0.7792 0.7632 0.7693 0.2077 -0.0234 -0.0229 120 ASP B OD2 3513 N N . LYS B 121 ? 0.7988 0.6897 0.7570 0.0826 -0.0470 -0.0623 121 LYS B N 3514 C CA . LYS B 121 ? 0.8873 0.7444 0.8053 0.0451 -0.0581 -0.0739 121 LYS B CA 3515 C C . LYS B 121 ? 0.8565 0.7625 0.7989 0.0507 -0.0587 -0.0762 121 LYS B C 3516 O O . LYS B 121 ? 0.9332 0.7943 0.8199 0.0453 -0.0691 -0.0856 121 LYS B O 3517 C CB . LYS B 121 ? 0.9001 0.7879 0.8455 -0.0051 -0.0582 -0.0743 121 LYS B CB 3518 C CG . LYS B 121 ? 0.9819 0.8513 0.8834 -0.0589 -0.0707 -0.0830 121 LYS B CG 3519 C CD . LYS B 121 ? 0.9799 0.9154 0.9212 -0.1018 -0.0676 -0.0804 121 LYS B CD 3520 C CE . LYS B 121 ? 1.0872 1.0016 0.9698 -0.1698 -0.0814 -0.0847 121 LYS B CE 3521 N NZ . LYS B 121 ? 1.1351 1.1077 1.0242 -0.1913 -0.0881 -0.0905 121 LYS B NZ 3522 N N . VAL B 122 ? 0.7634 0.7516 0.7799 0.0614 -0.0496 -0.0675 122 VAL B N 3523 C CA . VAL B 122 ? 0.7258 0.7616 0.7664 0.0705 -0.0499 -0.0675 122 VAL B CA 3524 C C . VAL B 122 ? 0.7651 0.7892 0.7833 0.1112 -0.0484 -0.0638 122 VAL B C 3525 O O . VAL B 122 ? 0.7843 0.8034 0.7780 0.1169 -0.0539 -0.0704 122 VAL B O 3526 C CB . VAL B 122 ? 0.6507 0.7578 0.7583 0.0729 -0.0437 -0.0586 122 VAL B CB 3527 C CG1 . VAL B 122 ? 0.6319 0.7778 0.7568 0.0914 -0.0441 -0.0548 122 VAL B CG1 3528 C CG2 . VAL B 122 ? 0.6347 0.7721 0.7587 0.0412 -0.0462 -0.0655 122 VAL B CG2 3529 N N . ARG B 123 ? 0.7484 0.7791 0.7741 0.1395 -0.0413 -0.0529 123 ARG B N 3530 C CA . ARG B 123 ? 0.7875 0.8287 0.7909 0.1821 -0.0389 -0.0479 123 ARG B CA 3531 C C . ARG B 123 ? 0.8894 0.8523 0.8073 0.2000 -0.0493 -0.0643 123 ARG B C 3532 O O . ARG B 123 ? 0.9113 0.8801 0.8061 0.2236 -0.0519 -0.0678 123 ARG B O 3533 C CB . ARG B 123 ? 0.7922 0.8620 0.8087 0.2057 -0.0311 -0.0344 123 ARG B CB 3534 C CG . ARG B 123 ? 0.8194 0.9388 0.8241 0.2504 -0.0266 -0.0250 123 ARG B CG 3535 C CD . ARG B 123 ? 0.8223 0.9925 0.8434 0.2680 -0.0195 -0.0101 123 ARG B CD 3536 N NE . ARG B 123 ? 0.8685 0.9759 0.8512 0.2764 -0.0226 -0.0196 123 ARG B NE 3537 C CZ . ARG B 123 ? 0.9522 0.9975 0.8561 0.3193 -0.0287 -0.0326 123 ARG B CZ 3538 N NH1 . ARG B 123 ? 1.0036 1.0421 0.8574 0.3617 -0.0324 -0.0397 123 ARG B NH1 3539 N NH2 . ARG B 123 ? 0.9863 0.9669 0.8513 0.3231 -0.0327 -0.0389 123 ARG B NH2 3540 N N . LEU B 124 ? 0.9532 0.8335 0.8150 0.1872 -0.0572 -0.0743 124 LEU B N 3541 C CA . LEU B 124 ? 1.0790 0.8509 0.8334 0.1998 -0.0724 -0.0903 124 LEU B CA 3542 C C . LEU B 124 ? 1.1297 0.8720 0.8537 0.1648 -0.0847 -0.1024 124 LEU B C 3543 O O . LEU B 124 ? 1.2331 0.8883 0.8633 0.1806 -0.0989 -0.1153 124 LEU B O 3544 C CB . LEU B 124 ? 1.1483 0.8264 0.8406 0.1840 -0.0805 -0.0954 124 LEU B CB 3545 C CG . LEU B 124 ? 1.1596 0.8497 0.8555 0.2287 -0.0721 -0.0867 124 LEU B CG 3546 C CD1 . LEU B 124 ? 1.2009 0.8192 0.8619 0.2002 -0.0773 -0.0880 124 LEU B CD1 3547 C CD2 . LEU B 124 ? 1.2385 0.8943 0.8576 0.3035 -0.0764 -0.0921 124 LEU B CD2 3548 N N . GLN B 125 ? 1.0654 0.8778 0.8595 0.1203 -0.0810 -0.0990 125 GLN B N 3549 C CA . GLN B 125 ? 1.0904 0.9047 0.8679 0.0884 -0.0916 -0.1086 125 GLN B CA 3550 C C . GLN B 125 ? 1.0503 0.9219 0.8566 0.1258 -0.0863 -0.1059 125 GLN B C 3551 O O . GLN B 125 ? 1.1479 0.9772 0.8951 0.1347 -0.0971 -0.1166 125 GLN B O 3552 C CB . GLN B 125 ? 1.0426 0.9282 0.8813 0.0350 -0.0899 -0.1064 125 GLN B CB 3553 C CG . GLN B 125 ? 1.0978 0.9407 0.9046 -0.0160 -0.0970 -0.1089 125 GLN B CG 3554 C CD . GLN B 125 ? 1.0576 0.9972 0.9240 -0.0625 -0.0953 -0.1072 125 GLN B CD 3555 O OE1 . GLN B 125 ? 1.1046 1.0732 0.9570 -0.0977 -0.1053 -0.1137 125 GLN B OE1 3556 N NE2 . GLN B 125 ? 0.9986 0.9955 0.9285 -0.0594 -0.0835 -0.0989 125 GLN B NE2 3557 N N . LEU B 126 ? 0.9599 0.9207 0.8490 0.1445 -0.0714 -0.0908 126 LEU B N 3558 C CA . LEU B 126 ? 0.9495 0.9718 0.8700 0.1717 -0.0661 -0.0839 126 LEU B CA 3559 C C . LEU B 126 ? 1.0271 1.0296 0.9001 0.2237 -0.0653 -0.0839 126 LEU B C 3560 O O . LEU B 126 ? 1.0804 1.0949 0.9358 0.2417 -0.0684 -0.0875 126 LEU B O 3561 C CB . LEU B 126 ? 0.8462 0.9491 0.8483 0.1724 -0.0540 -0.0654 126 LEU B CB 3562 C CG . LEU B 126 ? 0.7876 0.9200 0.8325 0.1362 -0.0552 -0.0666 126 LEU B CG 3563 C CD1 . LEU B 126 ? 0.7223 0.9093 0.8228 0.1451 -0.0480 -0.0498 126 LEU B CD1 3564 C CD2 . LEU B 126 ? 0.8191 0.9623 0.8498 0.1139 -0.0650 -0.0800 126 LEU B CD2 3565 N N . ARG B 127 ? 1.1223 1.1024 0.9724 0.2522 -0.0614 -0.0802 127 ARG B N 3566 C CA . ARG B 127 ? 1.2066 1.1822 1.0051 0.3131 -0.0606 -0.0808 127 ARG B CA 3567 C C . ARG B 127 ? 1.1530 1.2332 1.0020 0.3353 -0.0500 -0.0649 127 ARG B C 3568 O O . ARG B 127 ? 1.0907 1.2507 1.0105 0.3221 -0.0389 -0.0445 127 ARG B O 3569 C CB . ARG B 127 ? 1.3507 1.2107 1.0365 0.3296 -0.0785 -0.1038 127 ARG B CB 3570 C CG . ARG B 127 ? 1.4374 1.1812 1.0505 0.3128 -0.0907 -0.1154 127 ARG B CG 3571 C CD . ARG B 127 ? 1.5504 1.1705 1.0631 0.2820 -0.1134 -0.1357 127 ARG B CD 3572 N NE . ARG B 127 ? 1.6733 1.2291 1.0884 0.3366 -0.1253 -0.1495 127 ARG B NE 3573 C CZ . ARG B 127 ? 1.8258 1.2565 1.1290 0.3183 -0.1490 -0.1683 127 ARG B CZ 3574 N NH1 . ARG B 127 ? 1.8785 1.2470 1.1575 0.2385 -0.1629 -0.1732 127 ARG B NH1 3575 N NH2 . ARG B 127 ? 1.9119 1.2820 1.1205 0.3781 -0.1601 -0.1818 127 ARG B NH2 3576 N N . ASP B 128 ? 1.1832 1.2580 0.9898 0.3642 -0.0551 -0.0731 128 ASP B N 3577 C CA . ASP B 128 ? 1.1433 1.3193 0.9898 0.3854 -0.0453 -0.0563 128 ASP B CA 3578 C C . ASP B 128 ? 1.0852 1.2832 0.9677 0.3524 -0.0476 -0.0551 128 ASP B C 3579 O O . ASP B 128 ? 1.0875 1.3499 0.9852 0.3693 -0.0427 -0.0439 128 ASP B O 3580 C CB . ASP B 128 ? 1.2333 1.4166 1.0118 0.4537 -0.0464 -0.0626 128 ASP B CB 3581 C CG . ASP B 128 ? 1.3602 1.4305 1.0429 0.4703 -0.0639 -0.0906 128 ASP B CG 3582 O OD1 . ASP B 128 ? 1.3726 1.3761 1.0494 0.4202 -0.0747 -0.1026 128 ASP B OD1 3583 O OD2 . ASP B 128 ? 1.5044 1.5553 1.1108 0.5343 -0.0684 -0.1005 128 ASP B OD2 3584 N N . ASN B 129 ? 1.0576 1.2112 0.9517 0.3071 -0.0551 -0.0655 129 ASN B N 3585 C CA . ASN B 129 ? 1.0037 1.1912 0.9362 0.2795 -0.0573 -0.0637 129 ASN B CA 3586 C C . ASN B 129 ? 0.9223 1.1698 0.9271 0.2587 -0.0489 -0.0426 129 ASN B C 3587 O O . ASN B 129 ? 0.9080 1.1781 0.9388 0.2422 -0.0519 -0.0411 129 ASN B O 3588 C CB . ASN B 129 ? 1.0542 1.1871 0.9614 0.2418 -0.0707 -0.0843 129 ASN B CB 3589 C CG . ASN B 129 ? 1.1746 1.2342 0.9950 0.2527 -0.0848 -0.1050 129 ASN B CG 3590 O OD1 . ASN B 129 ? 1.2837 1.3203 1.0548 0.2989 -0.0845 -0.1072 129 ASN B OD1 3591 N ND2 . ASN B 129 ? 1.1888 1.2132 0.9825 0.2101 -0.0987 -0.1201 129 ASN B ND2 3592 N N . ALA B 130 ? 0.8713 1.1400 0.8990 0.2617 -0.0404 -0.0266 130 ALA B N 3593 C CA . ALA B 130 ? 0.8101 1.1152 0.8876 0.2397 -0.0360 -0.0060 130 ALA B CA 3594 C C . ALA B 130 ? 0.7871 1.1367 0.8764 0.2469 -0.0276 0.0164 130 ALA B C 3595 O O . ALA B 130 ? 0.8107 1.1619 0.8783 0.2698 -0.0240 0.0125 130 ALA B O 3596 C CB . ALA B 130 ? 0.7902 1.0619 0.8866 0.2115 -0.0395 -0.0148 130 ALA B CB 3597 N N . LYS B 131 ? 0.7729 1.1570 0.8880 0.2265 -0.0263 0.0402 131 LYS B N 3598 C CA . LYS B 131 ? 0.7746 1.2110 0.9008 0.2177 -0.0206 0.0653 131 LYS B CA 3599 C C . LYS B 131 ? 0.7369 1.1439 0.8805 0.1936 -0.0216 0.0668 131 LYS B C 3600 O O . LYS B 131 ? 0.7270 1.0912 0.8800 0.1708 -0.0279 0.0659 131 LYS B O 3601 C CB . LYS B 131 ? 0.8295 1.3062 0.9590 0.1956 -0.0224 0.0938 131 LYS B CB 3602 C CG . LYS B 131 ? 0.9277 1.4492 1.0412 0.2189 -0.0201 0.0969 131 LYS B CG 3603 C CD . LYS B 131 ? 1.0191 1.6022 1.1294 0.1931 -0.0200 0.1322 131 LYS B CD 3604 C CE . LYS B 131 ? 1.0660 1.7398 1.1646 0.2232 -0.0120 0.1399 131 LYS B CE 3605 N NZ . LYS B 131 ? 1.0686 1.8426 1.1688 0.1938 -0.0083 0.1779 131 LYS B NZ 3606 N N . GLU B 132 ? 0.7032 1.1352 0.8461 0.2045 -0.0160 0.0683 132 GLU B N 3607 C CA . GLU B 132 ? 0.6568 1.0708 0.8158 0.1820 -0.0165 0.0721 132 GLU B CA 3608 C C . GLU B 132 ? 0.6478 1.1044 0.8183 0.1452 -0.0187 0.1033 132 GLU B C 3609 O O . GLU B 132 ? 0.6541 1.1929 0.8249 0.1448 -0.0140 0.1234 132 GLU B O 3610 C CB . GLU B 132 ? 0.6525 1.0796 0.7991 0.2105 -0.0109 0.0635 132 GLU B CB 3611 C CG . GLU B 132 ? 0.6415 1.0376 0.8014 0.1917 -0.0117 0.0615 132 GLU B CG 3612 C CD . GLU B 132 ? 0.6719 1.0688 0.8095 0.2253 -0.0078 0.0515 132 GLU B CD 3613 O OE1 . GLU B 132 ? 0.7053 1.1334 0.8120 0.2690 -0.0049 0.0479 132 GLU B OE1 3614 O OE2 . GLU B 132 ? 0.6723 1.0346 0.8163 0.2125 -0.0086 0.0469 132 GLU B OE2 3615 N N . LEU B 133 ? 0.6450 1.0462 0.8160 0.1143 -0.0277 0.1076 133 LEU B N 3616 C CA . LEU B 133 ? 0.6532 1.0633 0.8118 0.0725 -0.0357 0.1376 133 LEU B CA 3617 C C . LEU B 133 ? 0.6651 1.1047 0.8289 0.0422 -0.0365 0.1546 133 LEU B C 3618 O O . LEU B 133 ? 0.6957 1.1706 0.8441 0.0013 -0.0425 0.1844 133 LEU B O 3619 C CB . LEU B 133 ? 0.6877 1.0087 0.8242 0.0592 -0.0489 0.1344 133 LEU B CB 3620 C CG . LEU B 133 ? 0.6964 0.9987 0.8208 0.0809 -0.0517 0.1258 133 LEU B CG 3621 C CD1 . LEU B 133 ? 0.7392 0.9570 0.8316 0.0759 -0.0665 0.1239 133 LEU B CD1 3622 C CD2 . LEU B 133 ? 0.7080 1.0691 0.8202 0.0731 -0.0497 0.1489 133 LEU B CD2 3623 N N . GLY B 134 ? 0.6419 1.0663 0.8223 0.0567 -0.0320 0.1373 134 GLY B N 3624 C CA . GLY B 134 ? 0.6357 1.0942 0.8232 0.0331 -0.0322 0.1507 134 GLY B CA 3625 C C . GLY B 134 ? 0.6508 1.0282 0.8291 0.0038 -0.0430 0.1485 134 GLY B C 3626 O O . GLY B 134 ? 0.6430 1.0409 0.8222 -0.0229 -0.0459 0.1609 134 GLY B O 3627 N N . ASN B 135 ? 0.6593 0.9514 0.8257 0.0128 -0.0496 0.1318 135 ASN B N 3628 C CA . ASN B 135 ? 0.6850 0.8956 0.8301 -0.0056 -0.0621 0.1287 135 ASN B CA 3629 C C . ASN B 135 ? 0.6532 0.8171 0.8109 0.0267 -0.0593 0.0979 135 ASN B C 3630 O O . ASN B 135 ? 0.6737 0.7728 0.8089 0.0261 -0.0698 0.0910 135 ASN B O 3631 C CB . ASN B 135 ? 0.7452 0.8955 0.8398 -0.0297 -0.0790 0.1454 135 ASN B CB 3632 C CG . ASN B 135 ? 0.7607 0.8934 0.8492 0.0014 -0.0787 0.1339 135 ASN B CG 3633 O OD1 . ASN B 135 ? 0.7172 0.8923 0.8404 0.0336 -0.0659 0.1161 135 ASN B OD1 3634 N ND2 . ASN B 135 ? 0.8397 0.9033 0.8748 -0.0084 -0.0949 0.1444 135 ASN B ND2 3635 N N . GLY B 136 ? 0.5964 0.7936 0.7813 0.0542 -0.0469 0.0802 136 GLY B N 3636 C CA . GLY B 136 ? 0.5752 0.7442 0.7691 0.0746 -0.0449 0.0543 136 GLY B CA 3637 C C . GLY B 136 ? 0.5637 0.7353 0.7546 0.0935 -0.0453 0.0430 136 GLY B C 3638 O O . GLY B 136 ? 0.5459 0.7147 0.7445 0.1048 -0.0433 0.0228 136 GLY B O 3639 N N . CYS B 137 ? 0.5897 0.7732 0.7674 0.0926 -0.0485 0.0573 137 CYS B N 3640 C CA . CYS B 137 ? 0.6168 0.8014 0.7876 0.1106 -0.0509 0.0485 137 CYS B CA 3641 C C . CYS B 137 ? 0.6105 0.8379 0.7865 0.1222 -0.0433 0.0483 137 CYS B C 3642 O O . CYS B 137 ? 0.6023 0.8651 0.7797 0.1187 -0.0378 0.0624 137 CYS B O 3643 C CB . CYS B 137 ? 0.6622 0.8104 0.7994 0.1066 -0.0637 0.0631 137 CYS B CB 3644 S SG . CYS B 137 ? 0.7270 0.8031 0.8326 0.1084 -0.0778 0.0588 137 CYS B SG 3645 N N . PHE B 138 ? 0.6166 0.8464 0.7914 0.1383 -0.0441 0.0318 138 PHE B N 3646 C CA . PHE B 138 ? 0.6210 0.8777 0.7903 0.1528 -0.0399 0.0272 138 PHE B CA 3647 C C . PHE B 138 ? 0.6531 0.9152 0.8125 0.1618 -0.0459 0.0288 138 PHE B C 3648 O O . PHE B 138 ? 0.6664 0.9188 0.8260 0.1670 -0.0517 0.0158 138 PHE B O 3649 C CB . PHE B 138 ? 0.6066 0.8515 0.7721 0.1578 -0.0380 0.0033 138 PHE B CB 3650 C CG . PHE B 138 ? 0.6104 0.8401 0.7735 0.1547 -0.0331 0.0009 138 PHE B CG 3651 C CD1 . PHE B 138 ? 0.6062 0.8480 0.7518 0.1732 -0.0281 0.0054 138 PHE B CD1 3652 C CD2 . PHE B 138 ? 0.6050 0.8127 0.7787 0.1389 -0.0339 -0.0059 138 PHE B CD2 3653 C CE1 . PHE B 138 ? 0.6075 0.8332 0.7428 0.1781 -0.0249 0.0027 138 PHE B CE1 3654 C CE2 . PHE B 138 ? 0.6030 0.7931 0.7703 0.1373 -0.0300 -0.0074 138 PHE B CE2 3655 C CZ . PHE B 138 ? 0.6096 0.8057 0.7562 0.1579 -0.0260 -0.0031 138 PHE B CZ 3656 N N . GLU B 139 ? 0.6859 0.9733 0.8351 0.1657 -0.0444 0.0451 139 GLU B N 3657 C CA . GLU B 139 ? 0.7292 1.0206 0.8641 0.1754 -0.0501 0.0486 139 GLU B CA 3658 C C . GLU B 139 ? 0.7226 1.0392 0.8547 0.1945 -0.0468 0.0323 139 GLU B C 3659 O O . GLU B 139 ? 0.7385 1.0803 0.8646 0.2041 -0.0402 0.0350 139 GLU B O 3660 C CB . GLU B 139 ? 0.7976 1.0998 0.9152 0.1612 -0.0521 0.0791 139 GLU B CB 3661 C CG . GLU B 139 ? 0.8742 1.1638 0.9658 0.1681 -0.0606 0.0874 139 GLU B CG 3662 C CD . GLU B 139 ? 0.9721 1.2683 1.0371 0.1422 -0.0640 0.1216 139 GLU B CD 3663 O OE1 . GLU B 139 ? 1.0198 1.3814 1.0940 0.1379 -0.0548 0.1341 139 GLU B OE1 3664 O OE2 . GLU B 139 ? 1.0830 1.3186 1.1097 0.1255 -0.0773 0.1367 139 GLU B OE2 3665 N N . PHE B 140 ? 0.7243 1.0368 0.8545 0.2024 -0.0527 0.0148 140 PHE B N 3666 C CA . PHE B 140 ? 0.7387 1.0651 0.8577 0.2132 -0.0533 -0.0029 140 PHE B CA 3667 C C . PHE B 140 ? 0.7694 1.1211 0.8735 0.2294 -0.0528 0.0081 140 PHE B C 3668 O O . PHE B 140 ? 0.7674 1.1250 0.8686 0.2300 -0.0554 0.0266 140 PHE B O 3669 C CB . PHE B 140 ? 0.7112 1.0447 0.8341 0.2094 -0.0611 -0.0226 140 PHE B CB 3670 C CG . PHE B 140 ? 0.6818 1.0041 0.8151 0.1904 -0.0613 -0.0359 140 PHE B CG 3671 C CD1 . PHE B 140 ? 0.6726 0.9916 0.8224 0.1874 -0.0618 -0.0312 140 PHE B CD1 3672 C CD2 . PHE B 140 ? 0.7030 1.0098 0.8188 0.1745 -0.0628 -0.0527 140 PHE B CD2 3673 C CE1 . PHE B 140 ? 0.6562 0.9738 0.8161 0.1697 -0.0613 -0.0425 140 PHE B CE1 3674 C CE2 . PHE B 140 ? 0.6989 0.9945 0.8184 0.1504 -0.0637 -0.0623 140 PHE B CE2 3675 C CZ . PHE B 140 ? 0.6806 0.9901 0.8278 0.1484 -0.0616 -0.0569 140 PHE B CZ 3676 N N . TYR B 141 ? 0.8198 1.1782 0.9044 0.2431 -0.0511 -0.0032 141 TYR B N 3677 C CA . TYR B 141 ? 0.8663 1.2540 0.9340 0.2624 -0.0510 0.0031 141 TYR B CA 3678 C C . TYR B 141 ? 0.8552 1.2466 0.9175 0.2646 -0.0600 -0.0107 141 TYR B C 3679 O O . TYR B 141 ? 0.9235 1.3377 0.9806 0.2756 -0.0618 0.0004 141 TYR B O 3680 C CB . TYR B 141 ? 0.8873 1.2774 0.9244 0.2857 -0.0473 -0.0056 141 TYR B CB 3681 C CG . TYR B 141 ? 0.9046 1.3167 0.9450 0.2936 -0.0380 0.0100 141 TYR B CG 3682 C CD1 . TYR B 141 ? 0.8990 1.3645 0.9580 0.2855 -0.0319 0.0404 141 TYR B CD1 3683 C CD2 . TYR B 141 ? 0.9398 1.3205 0.9579 0.3062 -0.0370 -0.0042 141 TYR B CD2 3684 C CE1 . TYR B 141 ? 0.9035 1.4102 0.9677 0.2881 -0.0239 0.0562 141 TYR B CE1 3685 C CE2 . TYR B 141 ? 0.9334 1.3482 0.9545 0.3191 -0.0286 0.0098 141 TYR B CE2 3686 C CZ . TYR B 141 ? 0.9232 1.4108 0.9719 0.3091 -0.0215 0.0400 141 TYR B CZ 3687 O OH . TYR B 141 ? 0.9493 1.4901 1.0022 0.3184 -0.0138 0.0547 141 TYR B OH 3688 N N . HIS B 142 ? 1.3544 1.6751 1.0165 0.4377 -0.0677 -0.2053 142 HIS B N 3689 C CA . HIS B 142 ? 1.3658 1.7225 0.9886 0.4556 -0.1134 -0.2336 142 HIS B CA 3690 C C . HIS B 142 ? 1.2730 1.6526 0.9490 0.4279 -0.1122 -0.1992 142 HIS B C 3691 O O . HIS B 142 ? 1.1918 1.5492 0.9340 0.3871 -0.0851 -0.1659 142 HIS B O 3692 C CB . HIS B 142 ? 1.3891 1.7378 1.0307 0.4297 -0.1746 -0.3061 142 HIS B CB 3693 C CG . HIS B 142 ? 1.3101 1.6271 1.0508 0.3594 -0.1813 -0.3122 142 HIS B CG 3694 N ND1 . HIS B 142 ? 1.2587 1.5943 1.0693 0.3142 -0.2043 -0.3144 142 HIS B ND1 3695 C CD2 . HIS B 142 ? 1.2868 1.5539 1.0628 0.3326 -0.1652 -0.3130 142 HIS B CD2 3696 C CE1 . HIS B 142 ? 1.2074 1.5003 1.0828 0.2632 -0.1989 -0.3144 142 HIS B CE1 3697 N NE2 . HIS B 142 ? 1.2247 1.4748 1.0789 0.2740 -0.1787 -0.3140 142 HIS B NE2 3698 N N . LYS B 143 ? 1.2955 1.7192 0.9392 0.4551 -0.1438 -0.2092 143 LYS B N 3699 C CA . LYS B 143 ? 1.2265 1.6766 0.9281 0.4301 -0.1505 -0.1875 143 LYS B CA 3700 C C . LYS B 143 ? 1.1406 1.5862 0.9350 0.3645 -0.1813 -0.2228 143 LYS B C 3701 O O . LYS B 143 ? 1.1667 1.6131 0.9707 0.3510 -0.2222 -0.2779 143 LYS B O 3702 C CB . LYS B 143 ? 1.2967 1.8040 0.9505 0.4789 -0.1847 -0.1955 143 LYS B CB 3703 C CG . LYS B 143 ? 1.3644 1.8718 0.9422 0.5387 -0.1419 -0.1357 143 LYS B CG 3704 C CD . LYS B 143 ? 1.4226 1.9879 0.9703 0.5826 -0.1796 -0.1381 143 LYS B CD 3705 C CE . LYS B 143 ? 1.5177 2.0747 0.9614 0.6575 -0.1398 -0.0810 143 LYS B CE 3706 N NZ . LYS B 143 ? 1.6398 2.1932 0.9617 0.7212 -0.1445 -0.0978 143 LYS B NZ 3707 N N . CYS B 144 ? 1.0345 1.4686 0.8930 0.3258 -0.1587 -0.1905 144 CYS B N 3708 C CA . CYS B 144 ? 0.9668 1.3921 0.9067 0.2676 -0.1754 -0.2121 144 CYS B CA 3709 C C . CYS B 144 ? 0.9254 1.3915 0.9111 0.2600 -0.1761 -0.1935 144 CYS B C 3710 O O . CYS B 144 ? 0.8919 1.3357 0.8879 0.2532 -0.1405 -0.1513 144 CYS B O 3711 C CB . CYS B 144 ? 0.9192 1.2795 0.8832 0.2315 -0.1437 -0.1923 144 CYS B CB 3712 S SG . CYS B 144 ? 0.8940 1.2201 0.9307 0.1685 -0.1594 -0.2193 144 CYS B SG 3713 N N . ASP B 145 ? 0.9380 1.4657 0.9542 0.2639 -0.2190 -0.2283 145 ASP B N 3714 C CA . ASP B 145 ? 0.9054 1.4865 0.9790 0.2606 -0.2219 -0.2147 145 ASP B CA 3715 C C . ASP B 145 ? 0.8396 1.3992 0.9981 0.2006 -0.2041 -0.2118 145 ASP B C 3716 O O . ASP B 145 ? 0.8288 1.3281 0.9924 0.1653 -0.1921 -0.2176 145 ASP B O 3717 C CB . ASP B 145 ? 0.9495 1.6164 1.0396 0.2880 -0.2786 -0.2549 145 ASP B CB 3718 C CG . ASP B 145 ? 0.9718 1.6511 1.1142 0.2520 -0.3266 -0.3191 145 ASP B CG 3719 O OD1 . ASP B 145 ? 0.9444 1.5751 1.1375 0.1974 -0.3112 -0.3265 145 ASP B OD1 3720 O OD2 . ASP B 145 ? 1.0413 1.7754 1.1721 0.2804 -0.3824 -0.3638 145 ASP B OD2 3721 N N . ASN B 146 ? 0.8092 1.4167 1.0299 0.1945 -0.1992 -0.2000 146 ASN B N 3722 C CA . ASN B 146 ? 0.7659 1.3488 1.0523 0.1470 -0.1691 -0.1867 146 ASN B CA 3723 C C . ASN B 146 ? 0.7816 1.3523 1.1325 0.0951 -0.1851 -0.2223 146 ASN B C 3724 O O . ASN B 146 ? 0.7707 1.2795 1.1329 0.0595 -0.1541 -0.2070 146 ASN B O 3725 C CB . ASN B 146 ? 0.7368 1.3822 1.0806 0.1579 -0.1567 -0.1678 146 ASN B CB 3726 C CG . ASN B 146 ? 0.7276 1.3571 1.0083 0.2036 -0.1285 -0.1250 146 ASN B CG 3727 O OD1 . ASN B 146 ? 0.7191 1.2821 0.9249 0.2162 -0.1094 -0.1038 146 ASN B OD1 3728 N ND2 . ASN B 146 ? 0.7254 1.4161 1.0458 0.2284 -0.1245 -0.1119 146 ASN B ND2 3729 N N . GLU B 147 ? 0.8325 1.4546 1.2209 0.0929 -0.2347 -0.2704 147 GLU B N 3730 C CA . GLU B 147 ? 0.8684 1.4665 1.3195 0.0424 -0.2524 -0.3087 147 GLU B CA 3731 C C . GLU B 147 ? 0.8749 1.3796 1.2516 0.0383 -0.2459 -0.3139 147 GLU B C 3732 O O . GLU B 147 ? 0.8904 1.3339 1.2960 -0.0030 -0.2310 -0.3163 147 GLU B O 3733 C CB . GLU B 147 ? 0.9236 1.5964 1.4350 0.0415 -0.3162 -0.3684 147 GLU B CB 3734 C CG . GLU B 147 ? 0.9305 1.7134 1.5335 0.0486 -0.3331 -0.3701 147 GLU B CG 3735 C CD . GLU B 147 ? 0.9610 1.8044 1.4931 0.1185 -0.3633 -0.3689 147 GLU B CD 3736 O OE1 . GLU B 147 ? 0.9450 1.7559 1.3897 0.1562 -0.3249 -0.3204 147 GLU B OE1 3737 O OE2 . GLU B 147 ? 1.0048 1.9240 1.5675 0.1368 -0.4268 -0.4169 147 GLU B OE2 3738 N N . CYS B 148 ? 0.8800 1.3749 1.1627 0.0851 -0.2539 -0.3127 148 CYS B N 3739 C CA . CYS B 148 ? 0.8923 1.3097 1.1073 0.0904 -0.2411 -0.3109 148 CYS B CA 3740 C C . CYS B 148 ? 0.8319 1.1857 1.0435 0.0683 -0.1931 -0.2645 148 CYS B C 3741 O O . CYS B 148 ? 0.8305 1.1197 1.0473 0.0412 -0.1850 -0.2685 148 CYS B O 3742 C CB . CYS B 148 ? 0.9297 1.3602 1.0520 0.1493 -0.2456 -0.3066 148 CYS B CB 3743 S SG . CYS B 148 ? 0.9762 1.3302 1.0256 0.1655 -0.2198 -0.2958 148 CYS B SG 3744 N N . MET B 149 ? 0.7782 1.1469 0.9787 0.0825 -0.1648 -0.2231 149 MET B N 3745 C CA . MET B 149 ? 0.7447 1.0552 0.9366 0.0655 -0.1267 -0.1851 149 MET B CA 3746 C C . MET B 149 ? 0.7552 1.0356 1.0004 0.0210 -0.1155 -0.1864 149 MET B C 3747 O O . MET B 149 ? 0.7530 0.9628 0.9772 0.0051 -0.0998 -0.1739 149 MET B O 3748 C CB . MET B 149 ? 0.7140 1.0460 0.8928 0.0874 -0.1025 -0.1489 149 MET B CB 3749 C CG . MET B 149 ? 0.7151 1.0549 0.8374 0.1300 -0.0987 -0.1324 149 MET B CG 3750 S SD . MET B 149 ? 0.7203 0.9942 0.7972 0.1326 -0.0869 -0.1234 149 MET B SD 3751 C CE . MET B 149 ? 0.7318 1.0280 0.7625 0.1814 -0.0702 -0.0952 149 MET B CE 3752 N N . GLU B 150 ? 0.7794 1.1149 1.0966 0.0032 -0.1220 -0.1991 150 GLU B N 3753 C CA . GLU B 150 ? 0.8080 1.1195 1.1872 -0.0400 -0.1010 -0.1938 150 GLU B CA 3754 C C . GLU B 150 ? 0.8473 1.0920 1.2296 -0.0678 -0.1121 -0.2158 150 GLU B C 3755 O O . GLU B 150 ? 0.8648 1.0424 1.2456 -0.0911 -0.0829 -0.1937 150 GLU B O 3756 C CB . GLU B 150 ? 0.8256 1.2247 1.3058 -0.0555 -0.1087 -0.2079 150 GLU B CB 3757 C CG . GLU B 150 ? 0.8614 1.2461 1.4251 -0.1022 -0.0765 -0.1967 150 GLU B CG 3758 C CD . GLU B 150 ? 0.8751 1.2065 1.3982 -0.1001 -0.0189 -0.1456 150 GLU B CD 3759 O OE1 . GLU B 150 ? 0.8714 1.1854 1.3143 -0.0649 -0.0082 -0.1230 150 GLU B OE1 3760 O OE2 . GLU B 150 ? 0.9144 1.2163 1.4839 -0.1328 0.0173 -0.1281 150 GLU B OE2 3761 N N . SER B 151 ? 0.8684 1.1242 1.2442 -0.0591 -0.1530 -0.2583 151 SER B N 3762 C CA . SER B 151 ? 0.9299 1.1165 1.3055 -0.0797 -0.1661 -0.2846 151 SER B CA 3763 C C . SER B 151 ? 0.9460 1.0488 1.2461 -0.0659 -0.1452 -0.2578 151 SER B C 3764 O O . SER B 151 ? 0.9965 1.0251 1.2975 -0.0850 -0.1402 -0.2606 151 SER B O 3765 C CB . SER B 151 ? 0.9649 1.1788 1.3328 -0.0628 -0.2159 -0.3406 151 SER B CB 3766 O OG . SER B 151 ? 0.9545 1.1663 1.2327 -0.0148 -0.2202 -0.3366 151 SER B OG 3767 N N . VAL B 152 ? 0.9207 1.0351 1.1617 -0.0320 -0.1348 -0.2322 152 VAL B N 3768 C CA . VAL B 152 ? 0.9227 0.9722 1.1085 -0.0195 -0.1192 -0.2068 152 VAL B CA 3769 C C . VAL B 152 ? 0.9444 0.9438 1.1315 -0.0410 -0.0893 -0.1723 152 VAL B C 3770 O O . VAL B 152 ? 0.9731 0.9000 1.1386 -0.0475 -0.0837 -0.1636 152 VAL B O 3771 C CB . VAL B 152 ? 0.8808 0.9584 1.0218 0.0162 -0.1145 -0.1885 152 VAL B CB 3772 C CG1 . VAL B 152 ? 0.8831 0.9028 0.9880 0.0251 -0.1054 -0.1678 152 VAL B CG1 3773 C CG2 . VAL B 152 ? 0.8897 1.0138 1.0151 0.0451 -0.1356 -0.2157 152 VAL B CG2 3774 N N . ARG B 153 ? 0.9427 0.9789 1.1490 -0.0463 -0.0690 -0.1520 153 ARG B N 3775 C CA . ARG B 153 ? 0.9894 0.9799 1.1869 -0.0605 -0.0346 -0.1187 153 ARG B CA 3776 C C . ARG B 153 ? 1.0753 1.0280 1.3203 -0.0960 -0.0213 -0.1210 153 ARG B C 3777 O O . ARG B 153 ? 1.1155 0.9981 1.3297 -0.1024 0.0065 -0.0919 153 ARG B O 3778 C CB . ARG B 153 ? 0.9626 1.0057 1.1755 -0.0542 -0.0117 -0.0998 153 ARG B CB 3779 C CG . ARG B 153 ? 0.9147 0.9865 1.0867 -0.0209 -0.0195 -0.0939 153 ARG B CG 3780 C CD . ARG B 153 ? 0.9179 1.0238 1.0982 -0.0111 0.0075 -0.0732 153 ARG B CD 3781 N NE . ARG B 153 ? 0.8878 1.0458 1.0618 0.0174 -0.0044 -0.0757 153 ARG B NE 3782 C CZ . ARG B 153 ? 0.8616 1.0996 1.0835 0.0264 -0.0152 -0.0874 153 ARG B CZ 3783 N NH1 . ARG B 153 ? 0.8663 1.1528 1.1626 0.0040 -0.0197 -0.1034 153 ARG B NH1 3784 N NH2 . ARG B 153 ? 0.8537 1.1231 1.0525 0.0591 -0.0224 -0.0823 153 ARG B NH2 3785 N N . ASN B 154 ? 1.1338 1.1302 1.4525 -0.1175 -0.0416 -0.1556 154 ASN B N 3786 C CA . ASN B 154 ? 1.2313 1.1909 1.6160 -0.1582 -0.0330 -0.1650 154 ASN B CA 3787 C C . ASN B 154 ? 1.2685 1.1236 1.6080 -0.1597 -0.0337 -0.1624 154 ASN B C 3788 O O . ASN B 154 ? 1.3396 1.1265 1.6914 -0.1827 -0.0019 -0.1375 154 ASN B O 3789 C CB . ASN B 154 ? 1.2920 1.3140 1.7578 -0.1765 -0.0730 -0.2178 154 ASN B CB 3790 C CG . ASN B 154 ? 1.3602 1.4799 1.9180 -0.1928 -0.0688 -0.2215 154 ASN B CG 3791 O OD1 . ASN B 154 ? 1.3527 1.5046 1.9041 -0.1813 -0.0360 -0.1854 154 ASN B OD1 3792 N ND2 . ASN B 154 ? 1.5129 1.6818 2.1600 -0.2174 -0.1055 -0.2692 154 ASN B ND2 3793 N N . GLY B 155 ? 1.2261 1.0691 1.5147 -0.1315 -0.0667 -0.1856 155 GLY B N 3794 C CA . GLY B 155 ? 1.2503 1.0102 1.5164 -0.1300 -0.0790 -0.1998 155 GLY B CA 3795 C C . GLY B 155 ? 1.2438 1.0232 1.5569 -0.1408 -0.1157 -0.2573 155 GLY B C 3796 O O . GLY B 155 ? 1.2912 1.0020 1.5911 -0.1382 -0.1291 -0.2789 155 GLY B O 3797 N N . THR B 156 ? 1.1846 1.0559 1.5453 -0.1468 -0.1353 -0.2842 156 THR B N 3798 C CA . THR B 156 ? 1.2090 1.1077 1.6229 -0.1609 -0.1763 -0.3445 156 THR B CA 3799 C C . THR B 156 ? 1.1823 1.1344 1.5397 -0.1152 -0.2135 -0.3792 156 THR B C 3800 O O . THR B 156 ? 1.2082 1.1966 1.5911 -0.1152 -0.2542 -0.4326 156 THR B O 3801 C CB . THR B 156 ? 1.1979 1.1709 1.7179 -0.1994 -0.1770 -0.3529 156 THR B CB 3802 O OG1 . THR B 156 ? 1.2243 1.1471 1.7981 -0.2404 -0.1309 -0.3141 156 THR B OG1 3803 C CG2 . THR B 156 ? 1.2553 1.2591 1.8424 -0.2181 -0.2293 -0.4226 156 THR B CG2 3804 N N . TYR B 157 ? 1.1530 1.1084 1.4339 -0.0748 -0.1995 -0.3495 157 TYR B N 3805 C CA . TYR B 157 ? 1.1479 1.1535 1.3732 -0.0284 -0.2213 -0.3703 157 TYR B CA 3806 C C . TYR B 157 ? 1.2422 1.2136 1.4457 -0.0137 -0.2541 -0.4262 157 TYR B C 3807 O O . TYR B 157 ? 1.2771 1.1754 1.4504 -0.0038 -0.2465 -0.4271 157 TYR B O 3808 C CB . TYR B 157 ? 1.0919 1.0906 1.2549 0.0059 -0.1953 -0.3282 157 TYR B CB 3809 C CG . TYR B 157 ? 1.0819 1.1237 1.1899 0.0546 -0.2054 -0.3417 157 TYR B CG 3810 C CD1 . TYR B 157 ? 1.0549 1.1733 1.1527 0.0747 -0.2112 -0.3390 157 TYR B CD1 3811 C CD2 . TYR B 157 ? 1.1058 1.1105 1.1699 0.0854 -0.2046 -0.3536 157 TYR B CD2 3812 C CE1 . TYR B 157 ? 1.0612 1.2118 1.0988 0.1238 -0.2127 -0.3440 157 TYR B CE1 3813 C CE2 . TYR B 157 ? 1.1141 1.1576 1.1256 0.1333 -0.2033 -0.3602 157 TYR B CE2 3814 C CZ . TYR B 157 ? 1.0885 1.2017 1.0829 0.1521 -0.2059 -0.3536 157 TYR B CZ 3815 O OH . TYR B 157 ? 1.0979 1.2421 1.0306 0.2040 -0.1972 -0.3530 157 TYR B OH 3816 N N . ASP B 158 ? 1.3085 1.3327 1.5241 -0.0075 -0.2934 -0.4751 158 ASP B N 3817 C CA . ASP B 158 ? 1.4288 1.4184 1.6209 0.0067 -0.3319 -0.5397 158 ASP B CA 3818 C C . ASP B 158 ? 1.4728 1.4634 1.5621 0.0716 -0.3276 -0.5428 158 ASP B C 3819 O O . ASP B 158 ? 1.4744 1.5301 1.5146 0.1119 -0.3418 -0.5530 158 ASP B O 3820 C CB . ASP B 158 ? 1.4686 1.5176 1.7104 -0.0081 -0.3838 -0.5967 158 ASP B CB 3821 C CG . ASP B 158 ? 1.5738 1.5649 1.8186 -0.0141 -0.4283 -0.6716 158 ASP B CG 3822 O OD1 . ASP B 158 ? 1.6180 1.5133 1.8430 -0.0167 -0.4126 -0.6742 158 ASP B OD1 3823 O OD2 . ASP B 158 ? 1.6362 1.6758 1.9033 -0.0137 -0.4828 -0.7307 158 ASP B OD2 3824 N N . TYR B 159 ? 1.5216 1.4402 1.5809 0.0843 -0.3045 -0.5299 159 TYR B N 3825 C CA . TYR B 159 ? 1.5497 1.4704 1.5297 0.1435 -0.2863 -0.5211 159 TYR B CA 3826 C C . TYR B 159 ? 1.6687 1.5967 1.5807 0.1901 -0.3179 -0.5824 159 TYR B C 3827 O O . TYR B 159 ? 1.6915 1.6709 1.5375 0.2409 -0.3064 -0.5719 159 TYR B O 3828 C CB . TYR B 159 ? 1.5511 1.3973 1.5313 0.1460 -0.2591 -0.4967 159 TYR B CB 3829 C CG . TYR B 159 ? 1.5878 1.4296 1.5054 0.2059 -0.2419 -0.4989 159 TYR B CG 3830 C CD1 . TYR B 159 ? 1.6888 1.4793 1.5645 0.2367 -0.2594 -0.5535 159 TYR B CD1 3831 C CD2 . TYR B 159 ? 1.5252 1.4125 1.4321 0.2320 -0.2057 -0.4473 159 TYR B CD2 3832 C CE1 . TYR B 159 ? 1.7248 1.5153 1.5451 0.2968 -0.2360 -0.5532 159 TYR B CE1 3833 C CE2 . TYR B 159 ? 1.5604 1.4523 1.4270 0.2856 -0.1825 -0.4451 159 TYR B CE2 3834 C CZ . TYR B 159 ? 1.6621 1.5083 1.4834 0.3203 -0.1950 -0.4964 159 TYR B CZ 3835 O OH . TYR B 159 ? 1.7044 1.5590 1.4870 0.3787 -0.1648 -0.4923 159 TYR B OH 3836 N N . PRO B 160 ? 1.7739 1.6446 1.6968 0.1754 -0.3563 -0.6466 160 PRO B N 3837 C CA . PRO B 160 ? 1.8915 1.7642 1.7382 0.2232 -0.3944 -0.7147 160 PRO B CA 3838 C C . PRO B 160 ? 1.8912 1.8557 1.7091 0.2440 -0.4264 -0.7315 160 PRO B C 3839 O O . PRO B 160 ? 1.9763 1.9573 1.6963 0.3057 -0.4429 -0.7655 160 PRO B O 3840 C CB . PRO B 160 ? 1.9749 1.7659 1.8670 0.1850 -0.4360 -0.7811 160 PRO B CB 3841 C CG . PRO B 160 ? 1.9328 1.6554 1.8916 0.1406 -0.4002 -0.7364 160 PRO B CG 3842 C CD . PRO B 160 ? 1.7986 1.5870 1.7938 0.1206 -0.3629 -0.6593 160 PRO B CD 3843 N N . GLN B 161 ? 1.8165 1.8387 1.7129 0.1992 -0.4336 -0.7067 161 GLN B N 3844 C CA . GLN B 161 ? 1.8157 1.9307 1.6941 0.2211 -0.4639 -0.7153 161 GLN B CA 3845 C C . GLN B 161 ? 1.7716 1.9310 1.5531 0.2866 -0.4251 -0.6656 161 GLN B C 3846 O O . GLN B 161 ? 1.8240 2.0374 1.5366 0.3352 -0.4507 -0.6831 161 GLN B O 3847 C CB . GLN B 161 ? 1.7438 1.9118 1.7364 0.1620 -0.4668 -0.6880 161 GLN B CB 3848 C CG . GLN B 161 ? 1.7663 2.0295 1.7679 0.1774 -0.5149 -0.7138 161 GLN B CG 3849 C CD . GLN B 161 ? 1.6901 2.0106 1.8125 0.1234 -0.5087 -0.6819 161 GLN B CD 3850 O OE1 . GLN B 161 ? 1.6510 1.9317 1.8634 0.0633 -0.4844 -0.6639 161 GLN B OE1 3851 N NE2 . GLN B 161 ? 1.6794 2.0921 1.7993 0.1501 -0.5274 -0.6721 161 GLN B NE2 3852 N N . TYR B 162 ? 1.6727 1.8081 1.4523 0.2883 -0.3644 -0.6031 162 TYR B N 3853 C CA . TYR B 162 ? 1.6341 1.8015 1.3402 0.3434 -0.3184 -0.5519 162 TYR B CA 3854 C C . TYR B 162 ? 1.6408 1.7547 1.3027 0.3757 -0.2811 -0.5461 162 TYR B C 3855 O O . TYR B 162 ? 1.6645 1.7920 1.2402 0.4387 -0.2557 -0.5376 162 TYR B O 3856 C CB . TYR B 162 ? 1.5241 1.7252 1.2872 0.3148 -0.2794 -0.4795 162 TYR B CB 3857 C CG . TYR B 162 ? 1.4799 1.7239 1.3151 0.2713 -0.3079 -0.4808 162 TYR B CG 3858 C CD1 . TYR B 162 ? 1.5015 1.8150 1.3100 0.3000 -0.3307 -0.4831 162 TYR B CD1 3859 C CD2 . TYR B 162 ? 1.4236 1.6397 1.3527 0.2066 -0.3083 -0.4761 162 TYR B CD2 3860 C CE1 . TYR B 162 ? 1.4579 1.8200 1.3438 0.2641 -0.3547 -0.4836 162 TYR B CE1 3861 C CE2 . TYR B 162 ? 1.3833 1.6441 1.3857 0.1694 -0.3255 -0.4738 162 TYR B CE2 3862 C CZ . TYR B 162 ? 1.4002 1.7380 1.3872 0.1975 -0.3493 -0.4789 162 TYR B CZ 3863 O OH . TYR B 162 ? 1.3631 1.7544 1.4340 0.1642 -0.3648 -0.4763 162 TYR B OH # _database_PDB_caveat.id 1 _database_PDB_caveat.text 'NAG B1154 HAS WRONG CHIRALITY AT ATOM C1' # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ASP 1 1 1 ASP ASP A . n A 1 2 GLN 2 2 2 GLN GLN A . n A 1 3 ILE 3 3 3 ILE ILE A . n A 1 4 CYS 4 4 4 CYS CYS A . n A 1 5 ILE 5 5 5 ILE ILE A . n A 1 6 GLY 6 6 6 GLY GLY A . n A 1 7 TYR 7 7 7 TYR TYR A . n A 1 8 HIS 8 8 8 HIS HIS A . n A 1 9 ALA 9 9 9 ALA ALA A . n A 1 10 ASN 10 10 10 ASN ASN A . n A 1 11 ASN 11 11 11 ASN ASN A . n A 1 12 SER 12 12 12 SER SER A . n A 1 13 THR 13 13 13 THR THR A . n A 1 14 GLU 14 14 14 GLU GLU A . n A 1 15 GLN 15 15 15 GLN GLN A . n A 1 16 VAL 16 16 16 VAL VAL A . n A 1 17 ASP 17 17 17 ASP ASP A . n A 1 18 THR 18 18 18 THR THR A . n A 1 19 ILE 19 19 19 ILE ILE A . n A 1 20 MET 20 20 20 MET MET A . n A 1 21 GLU 21 21 21 GLU GLU A . n A 1 22 LYS 22 22 22 LYS LYS A . n A 1 23 ASN 23 23 23 ASN ASN A . n A 1 24 VAL 24 24 24 VAL VAL A . n A 1 25 THR 25 25 25 THR THR A . n A 1 26 VAL 26 26 26 VAL VAL A . n A 1 27 THR 27 27 27 THR THR A . n A 1 28 HIS 28 28 28 HIS HIS A . n A 1 29 ALA 29 29 29 ALA ALA A . n A 1 30 GLN 30 30 30 GLN GLN A . n A 1 31 ASP 31 31 31 ASP ASP A . n A 1 32 ILE 32 32 32 ILE ILE A . n A 1 33 LEU 33 33 33 LEU LEU A . n A 1 34 GLU 34 34 34 GLU GLU A . n A 1 35 LYS 35 35 35 LYS LYS A . n A 1 36 THR 36 36 36 THR THR A . n A 1 37 HIS 37 37 37 HIS HIS A . n A 1 38 ASN 38 38 38 ASN ASN A . n A 1 39 GLY 39 39 39 GLY GLY A . n A 1 40 LYS 40 40 40 LYS LYS A . n A 1 41 LEU 41 41 41 LEU LEU A . n A 1 42 CYS 42 42 42 CYS CYS A . n A 1 43 ASP 43 43 43 ASP ASP A . n A 1 44 LEU 44 44 44 LEU LEU A . n A 1 45 ASP 45 45 45 ASP ASP A . n A 1 46 GLY 46 46 46 GLY GLY A . n A 1 47 VAL 47 47 47 VAL VAL A . n A 1 48 LYS 48 48 48 LYS LYS A . n A 1 49 PRO 49 49 49 PRO PRO A . n A 1 50 LEU 50 50 50 LEU LEU A . n A 1 51 ILE 51 51 51 ILE ILE A . n A 1 52 LEU 52 52 52 LEU LEU A . n A 1 53 ARG 53 53 53 ARG ARG A . n A 1 54 ASP 54 54 54 ASP ASP A . n A 1 55 CYS 55 55 55 CYS CYS A . n A 1 56 SER 56 56 56 SER SER A . n A 1 57 VAL 57 57 57 VAL VAL A . n A 1 58 ALA 58 58 58 ALA ALA A . n A 1 59 GLY 59 59 59 GLY GLY A . n A 1 60 TRP 60 60 60 TRP TRP A . n A 1 61 LEU 61 61 61 LEU LEU A . n A 1 62 LEU 62 62 62 LEU LEU A . n A 1 63 GLY 63 63 63 GLY GLY A . n A 1 64 ASN 64 64 64 ASN ASN A . n A 1 65 PRO 65 65 65 PRO PRO A . n A 1 66 MET 66 66 66 MET MET A . n A 1 67 CYS 67 67 67 CYS CYS A . n A 1 68 ASP 68 68 68 ASP ASP A . n A 1 69 GLU 69 69 69 GLU GLU A . n A 1 70 PHE 70 70 70 PHE PHE A . n A 1 71 ILE 71 71 71 ILE ILE A . n A 1 72 ASN 72 72 72 ASN ASN A . n A 1 73 VAL 73 73 73 VAL VAL A . n A 1 74 PRO 74 74 74 PRO PRO A . n A 1 75 GLU 75 75 75 GLU GLU A . n A 1 76 TRP 76 76 76 TRP TRP A . n A 1 77 SER 77 77 77 SER SER A . n A 1 78 TYR 78 78 78 TYR TYR A . n A 1 79 ILE 79 79 79 ILE ILE A . n A 1 80 VAL 80 80 80 VAL VAL A . n A 1 81 GLU 81 81 81 GLU GLU A . n A 1 82 LYS 82 82 82 LYS LYS A . n A 1 83 ALA 83 83 83 ALA ALA A . n A 1 84 ASN 84 84 84 ASN ASN A . n A 1 85 PRO 85 85 85 PRO PRO A . n A 1 86 VAL 86 86 86 VAL VAL A . n A 1 87 ASN 87 87 87 ASN ASN A . n A 1 88 ASP 88 88 88 ASP ASP A . n A 1 89 LEU 89 89 89 LEU LEU A . n A 1 90 CYS 90 90 90 CYS CYS A . n A 1 91 TYR 91 91 91 TYR TYR A . n A 1 92 PRO 92 92 92 PRO PRO A . n A 1 93 GLY 93 93 93 GLY GLY A . n A 1 94 ASP 94 94 94 ASP ASP A . n A 1 95 PHE 95 95 95 PHE PHE A . n A 1 96 ASN 96 96 96 ASN ASN A . n A 1 97 ASP 97 97 97 ASP ASP A . n A 1 98 TYR 98 98 98 TYR TYR A . n A 1 99 GLU 99 99 99 GLU GLU A . n A 1 100 GLU 100 100 100 GLU GLU A . n A 1 101 LEU 101 101 101 LEU LEU A . n A 1 102 LYS 102 102 102 LYS LYS A . n A 1 103 HIS 103 103 103 HIS HIS A . n A 1 104 LEU 104 104 104 LEU LEU A . n A 1 105 LEU 105 105 105 LEU LEU A . n A 1 106 SER 106 106 106 SER SER A . n A 1 107 ARG 107 107 107 ARG ARG A . n A 1 108 ILE 108 108 108 ILE ILE A . n A 1 109 ASN 109 109 109 ASN ASN A . n A 1 110 HIS 110 110 110 HIS HIS A . n A 1 111 PHE 111 111 111 PHE PHE A . n A 1 112 GLU 112 112 112 GLU GLU A . n A 1 113 LYS 113 113 113 LYS LYS A . n A 1 114 ILE 114 114 114 ILE ILE A . n A 1 115 GLN 115 115 115 GLN GLN A . n A 1 116 ILE 116 116 116 ILE ILE A . n A 1 117 ILE 117 117 117 ILE ILE A . n A 1 118 PRO 118 118 118 PRO PRO A . n A 1 119 LYS 119 119 119 LYS LYS A . n A 1 120 SER 120 120 120 SER SER A . n A 1 121 SER 121 121 121 SER SER A . n A 1 122 TRP 122 122 122 TRP TRP A . n A 1 123 SER 123 123 123 SER SER A . n A 1 124 SER 124 124 124 SER SER A . n A 1 125 HIS 125 125 125 HIS HIS A . n A 1 126 GLU 126 126 126 GLU GLU A . n A 1 127 ALA 127 127 127 ALA ALA A . n A 1 128 SER 128 128 128 SER SER A . n A 1 129 LEU 129 129 129 LEU LEU A . n A 1 130 GLY 130 130 130 GLY GLY A . n A 1 131 VAL 131 131 131 VAL VAL A . n A 1 132 SER 132 132 132 SER SER A . n A 1 133 SER 133 133 133 SER SER A . n A 1 134 ALA 134 134 134 ALA ALA A . n A 1 135 CYS 135 135 135 CYS CYS A . n A 1 136 PRO 136 136 136 PRO PRO A . n A 1 137 TYR 137 137 137 TYR TYR A . n A 1 138 GLN 138 138 138 GLN GLN A . n A 1 139 GLY 139 139 139 GLY GLY A . n A 1 140 LYS 140 140 140 LYS LYS A . n A 1 141 SER 141 141 141 SER SER A . n A 1 142 SER 142 142 142 SER SER A . n A 1 143 PHE 143 143 143 PHE PHE A . n A 1 144 PHE 144 144 144 PHE PHE A . n A 1 145 ARG 145 145 145 ARG ARG A . n A 1 146 ASN 146 146 146 ASN ASN A . n A 1 147 VAL 147 147 147 VAL VAL A . n A 1 148 VAL 148 148 148 VAL VAL A . n A 1 149 TRP 149 149 149 TRP TRP A . n A 1 150 LEU 150 150 150 LEU LEU A . n A 1 151 ILE 151 151 151 ILE ILE A . n A 1 152 LYS 152 152 152 LYS LYS A . n A 1 153 LYS 153 153 153 LYS LYS A . n A 1 154 ASN 154 154 154 ASN ASN A . n A 1 155 SER 155 155 155 SER SER A . n A 1 156 THR 156 156 156 THR THR A . n A 1 157 TYR 157 157 157 TYR TYR A . n A 1 158 PRO 158 158 158 PRO PRO A . n A 1 159 THR 159 159 159 THR THR A . n A 1 160 ILE 160 160 160 ILE ILE A . n A 1 161 LYS 161 161 161 LYS LYS A . n A 1 162 ARG 162 162 162 ARG ARG A . n A 1 163 SER 163 163 163 SER SER A . n A 1 164 TYR 164 164 164 TYR TYR A . n A 1 165 ASN 165 165 165 ASN ASN A . n A 1 166 ASN 166 166 166 ASN ASN A . n A 1 167 THR 167 167 167 THR THR A . n A 1 168 ASN 168 168 168 ASN ASN A . n A 1 169 GLN 169 169 169 GLN GLN A . n A 1 170 GLU 170 170 170 GLU GLU A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 LEU 172 172 172 LEU LEU A . n A 1 173 LEU 173 173 173 LEU LEU A . n A 1 174 VAL 174 174 174 VAL VAL A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 TRP 176 176 176 TRP TRP A . n A 1 177 GLY 177 177 177 GLY GLY A . n A 1 178 ILE 178 178 178 ILE ILE A . n A 1 179 HIS 179 179 179 HIS HIS A . n A 1 180 HIS 180 180 180 HIS HIS A . n A 1 181 PRO 181 181 181 PRO PRO A . n A 1 182 LYS 182 182 182 LYS LYS A . n A 1 183 ASP 183 183 183 ASP ASP A . n A 1 184 ALA 184 184 184 ALA ALA A . n A 1 185 ALA 185 185 185 ALA ALA A . n A 1 186 GLU 186 186 186 GLU GLU A . n A 1 187 GLN 187 187 187 GLN GLN A . n A 1 188 THR 188 188 188 THR THR A . n A 1 189 LYS 189 189 189 LYS LYS A . n A 1 190 LEU 190 190 190 LEU LEU A . n A 1 191 TYR 191 191 191 TYR TYR A . n A 1 192 GLN 192 192 192 GLN GLN A . n A 1 193 ASN 193 193 193 ASN ASN A . n A 1 194 PRO 194 194 194 PRO PRO A . n A 1 195 THR 195 195 195 THR THR A . n A 1 196 THR 196 196 196 THR THR A . n A 1 197 TYR 197 197 197 TYR TYR A . n A 1 198 ILE 198 198 198 ILE ILE A . n A 1 199 SER 199 199 199 SER SER A . n A 1 200 VAL 200 200 200 VAL VAL A . n A 1 201 GLY 201 201 201 GLY GLY A . n A 1 202 THR 202 202 202 THR THR A . n A 1 203 SER 203 203 203 SER SER A . n A 1 204 THR 204 204 204 THR THR A . n A 1 205 LEU 205 205 205 LEU LEU A . n A 1 206 ASN 206 206 206 ASN ASN A . n A 1 207 GLN 207 207 207 GLN GLN A . n A 1 208 ARG 208 208 208 ARG ARG A . n A 1 209 LEU 209 209 209 LEU LEU A . n A 1 210 VAL 210 210 210 VAL VAL A . n A 1 211 PRO 211 211 211 PRO PRO A . n A 1 212 ARG 212 212 212 ARG ARG A . n A 1 213 ILE 213 213 213 ILE ILE A . n A 1 214 ALA 214 214 214 ALA ALA A . n A 1 215 THR 215 215 215 THR THR A . n A 1 216 ARG 216 216 216 ARG ARG A . n A 1 217 SER 217 217 217 SER SER A . n A 1 218 LYS 218 218 218 LYS LYS A . n A 1 219 VAL 219 219 219 VAL VAL A . n A 1 220 ASN 220 220 220 ASN ASN A . n A 1 221 GLY 221 221 221 GLY GLY A . n A 1 222 GLN 222 222 222 GLN GLN A . n A 1 223 SER 223 223 223 SER SER A . n A 1 224 GLY 224 224 224 GLY GLY A . n A 1 225 ARG 225 225 225 ARG ARG A . n A 1 226 MET 226 226 226 MET MET A . n A 1 227 GLU 227 227 227 GLU GLU A . n A 1 228 PHE 228 228 228 PHE PHE A . n A 1 229 PHE 229 229 229 PHE PHE A . n A 1 230 TRP 230 230 230 TRP TRP A . n A 1 231 THR 231 231 231 THR THR A . n A 1 232 ILE 232 232 232 ILE ILE A . n A 1 233 LEU 233 233 233 LEU LEU A . n A 1 234 LYS 234 234 234 LYS LYS A . n A 1 235 PRO 235 235 235 PRO PRO A . n A 1 236 ASN 236 236 236 ASN ASN A . n A 1 237 ASP 237 237 237 ASP ASP A . n A 1 238 ALA 238 238 238 ALA ALA A . n A 1 239 ILE 239 239 239 ILE ILE A . n A 1 240 ASN 240 240 240 ASN ASN A . n A 1 241 PHE 241 241 241 PHE PHE A . n A 1 242 GLU 242 242 242 GLU GLU A . n A 1 243 SER 243 243 243 SER SER A . n A 1 244 ASN 244 244 244 ASN ASN A . n A 1 245 GLY 245 245 245 GLY GLY A . n A 1 246 ASN 246 246 246 ASN ASN A . n A 1 247 PHE 247 247 247 PHE PHE A . n A 1 248 ILE 248 248 248 ILE ILE A . n A 1 249 ALA 249 249 249 ALA ALA A . n A 1 250 PRO 250 250 250 PRO PRO A . n A 1 251 GLU 251 251 251 GLU GLU A . n A 1 252 TYR 252 252 252 TYR TYR A . n A 1 253 ALA 253 253 253 ALA ALA A . n A 1 254 TYR 254 254 254 TYR TYR A . n A 1 255 LYS 255 255 255 LYS LYS A . n A 1 256 ILE 256 256 256 ILE ILE A . n A 1 257 VAL 257 257 257 VAL VAL A . n A 1 258 LYS 258 258 258 LYS LYS A . n A 1 259 LYS 259 259 259 LYS LYS A . n A 1 260 GLY 260 260 260 GLY GLY A . n A 1 261 ASP 261 261 261 ASP ASP A . n A 1 262 SER 262 262 262 SER SER A . n A 1 263 THR 263 263 263 THR THR A . n A 1 264 ILE 264 264 264 ILE ILE A . n A 1 265 MET 265 265 265 MET MET A . n A 1 266 LYS 266 266 266 LYS LYS A . n A 1 267 SER 267 267 267 SER SER A . n A 1 268 GLU 268 268 268 GLU GLU A . n A 1 269 LEU 269 269 269 LEU LEU A . n A 1 270 GLU 270 270 270 GLU GLU A . n A 1 271 TYR 271 271 271 TYR TYR A . n A 1 272 GLY 272 272 272 GLY GLY A . n A 1 273 ASN 273 273 273 ASN ASN A . n A 1 274 CYS 274 274 274 CYS CYS A . n A 1 275 ASN 275 275 275 ASN ASN A . n A 1 276 THR 276 276 276 THR THR A . n A 1 277 LYS 277 277 277 LYS LYS A . n A 1 278 CYS 278 278 278 CYS CYS A . n A 1 279 GLN 279 279 279 GLN GLN A . n A 1 280 THR 280 280 280 THR THR A . n A 1 281 PRO 281 281 281 PRO PRO A . n A 1 282 MET 282 282 282 MET MET A . n A 1 283 GLY 283 283 283 GLY GLY A . n A 1 284 ALA 284 284 284 ALA ALA A . n A 1 285 ILE 285 285 285 ILE ILE A . n A 1 286 ASN 286 286 286 ASN ASN A . n A 1 287 SER 287 287 287 SER SER A . n A 1 288 SER 288 288 288 SER SER A . n A 1 289 MET 289 289 289 MET MET A . n A 1 290 PRO 290 290 290 PRO PRO A . n A 1 291 PHE 291 291 291 PHE PHE A . n A 1 292 HIS 292 292 292 HIS HIS A . n A 1 293 ASN 293 293 293 ASN ASN A . n A 1 294 ILE 294 294 294 ILE ILE A . n A 1 295 HIS 295 295 295 HIS HIS A . n A 1 296 PRO 296 296 296 PRO PRO A . n A 1 297 LEU 297 297 297 LEU LEU A . n A 1 298 THR 298 298 298 THR THR A . n A 1 299 ILE 299 299 299 ILE ILE A . n A 1 300 GLY 300 300 300 GLY GLY A . n A 1 301 GLU 301 301 301 GLU GLU A . n A 1 302 CYS 302 302 302 CYS CYS A . n A 1 303 PRO 303 303 303 PRO PRO A . n A 1 304 LYS 304 304 304 LYS LYS A . n A 1 305 TYR 305 305 305 TYR TYR A . n A 1 306 VAL 306 306 306 VAL VAL A . n A 1 307 LYS 307 307 307 LYS LYS A . n A 1 308 SER 308 308 308 SER SER A . n A 1 309 ASN 309 309 309 ASN ASN A . n A 1 310 ARG 310 310 310 ARG ARG A . n A 1 311 LEU 311 311 311 LEU LEU A . n A 1 312 VAL 312 312 312 VAL VAL A . n A 1 313 LEU 313 313 313 LEU LEU A . n A 1 314 ALA 314 314 314 ALA ALA A . n A 1 315 THR 315 315 315 THR THR A . n A 1 316 GLY 316 316 316 GLY GLY A . n A 1 317 LEU 317 317 317 LEU LEU A . n A 1 318 ARG 318 318 318 ARG ARG A . n A 1 319 ASN 319 319 319 ASN ASN A . n A 1 320 SER 320 320 320 SER SER A . n A 1 321 PRO 321 321 321 PRO PRO A . n A 1 322 GLN 322 322 ? ? ? A . n A 1 323 ARG 323 323 ? ? ? A . n A 1 324 GLU 324 324 ? ? ? A . n A 1 325 THR 325 325 ? ? ? A . n A 1 326 ARG 326 326 ? ? ? A . n B 2 1 GLY 1 1 1 GLY GLY B . n B 2 2 LEU 2 2 2 LEU LEU B . n B 2 3 PHE 3 3 3 PHE PHE B . n B 2 4 GLY 4 4 4 GLY GLY B . n B 2 5 ALA 5 5 5 ALA ALA B . n B 2 6 ILE 6 6 6 ILE ILE B . n B 2 7 ALA 7 7 7 ALA ALA B . n B 2 8 GLY 8 8 8 GLY GLY B . n B 2 9 PHE 9 9 9 PHE PHE B . n B 2 10 ILE 10 10 10 ILE ILE B . n B 2 11 GLU 11 11 11 GLU GLU B . n B 2 12 GLY 12 12 12 GLY GLY B . n B 2 13 GLY 13 13 13 GLY GLY B . n B 2 14 TRP 14 14 14 TRP TRP B . n B 2 15 GLN 15 15 15 GLN GLN B . n B 2 16 GLY 16 16 16 GLY GLY B . n B 2 17 MET 17 17 17 MET MET B . n B 2 18 VAL 18 18 18 VAL VAL B . n B 2 19 ASP 19 19 19 ASP ASP B . n B 2 20 GLY 20 20 20 GLY GLY B . n B 2 21 TRP 21 21 21 TRP TRP B . n B 2 22 TYR 22 22 22 TYR TYR B . n B 2 23 GLY 23 23 23 GLY GLY B . n B 2 24 TYR 24 24 24 TYR TYR B . n B 2 25 HIS 25 25 25 HIS HIS B . n B 2 26 HIS 26 26 26 HIS HIS B . n B 2 27 SER 27 27 27 SER SER B . n B 2 28 ASN 28 28 28 ASN ASN B . n B 2 29 GLU 29 29 29 GLU GLU B . n B 2 30 GLN 30 30 30 GLN GLN B . n B 2 31 GLY 31 31 31 GLY GLY B . n B 2 32 SER 32 32 32 SER SER B . n B 2 33 GLY 33 33 33 GLY GLY B . n B 2 34 TYR 34 34 34 TYR TYR B . n B 2 35 ALA 35 35 35 ALA ALA B . n B 2 36 ALA 36 36 36 ALA ALA B . n B 2 37 ASP 37 37 37 ASP ASP B . n B 2 38 LYS 38 38 38 LYS LYS B . n B 2 39 GLU 39 39 39 GLU GLU B . n B 2 40 SER 40 40 40 SER SER B . n B 2 41 THR 41 41 41 THR THR B . n B 2 42 GLN 42 42 42 GLN GLN B . n B 2 43 LYS 43 43 43 LYS LYS B . n B 2 44 ALA 44 44 44 ALA ALA B . n B 2 45 ILE 45 45 45 ILE ILE B . n B 2 46 ASP 46 46 46 ASP ASP B . n B 2 47 GLY 47 47 47 GLY GLY B . n B 2 48 VAL 48 48 48 VAL VAL B . n B 2 49 THR 49 49 49 THR THR B . n B 2 50 ASN 50 50 50 ASN ASN B . n B 2 51 LYS 51 51 51 LYS LYS B . n B 2 52 VAL 52 52 52 VAL VAL B . n B 2 53 ASN 53 53 53 ASN ASN B . n B 2 54 SER 54 54 54 SER SER B . n B 2 55 ILE 55 55 55 ILE ILE B . n B 2 56 ILE 56 56 56 ILE ILE B . n B 2 57 ASP 57 57 57 ASP ASP B . n B 2 58 LYS 58 58 58 LYS LYS B . n B 2 59 MET 59 59 59 MET MET B . n B 2 60 ASN 60 60 60 ASN ASN B . n B 2 61 THR 61 61 61 THR THR B . n B 2 62 GLN 62 62 62 GLN GLN B . n B 2 63 PHE 63 63 63 PHE PHE B . n B 2 64 GLU 64 64 64 GLU GLU B . n B 2 65 ALA 65 65 65 ALA ALA B . n B 2 66 VAL 66 66 66 VAL VAL B . n B 2 67 GLY 67 67 67 GLY GLY B . n B 2 68 ARG 68 68 68 ARG ARG B . n B 2 69 GLU 69 69 69 GLU GLU B . n B 2 70 PHE 70 70 70 PHE PHE B . n B 2 71 ASN 71 71 71 ASN ASN B . n B 2 72 ASN 72 72 72 ASN ASN B . n B 2 73 LEU 73 73 73 LEU LEU B . n B 2 74 GLU 74 74 74 GLU GLU B . n B 2 75 ARG 75 75 75 ARG ARG B . n B 2 76 ARG 76 76 76 ARG ARG B . n B 2 77 ILE 77 77 77 ILE ILE B . n B 2 78 GLU 78 78 78 GLU GLU B . n B 2 79 ASN 79 79 79 ASN ASN B . n B 2 80 LEU 80 80 80 LEU LEU B . n B 2 81 ASN 81 81 81 ASN ASN B . n B 2 82 LYS 82 82 82 LYS LYS B . n B 2 83 LYS 83 83 83 LYS LYS B . n B 2 84 MET 84 84 84 MET MET B . n B 2 85 GLU 85 85 85 GLU GLU B . n B 2 86 ASP 86 86 86 ASP ASP B . n B 2 87 GLY 87 87 87 GLY GLY B . n B 2 88 PHE 88 88 88 PHE PHE B . n B 2 89 LEU 89 89 89 LEU LEU B . n B 2 90 ASP 90 90 90 ASP ASP B . n B 2 91 VAL 91 91 91 VAL VAL B . n B 2 92 TRP 92 92 92 TRP TRP B . n B 2 93 THR 93 93 93 THR THR B . n B 2 94 TYR 94 94 94 TYR TYR B . n B 2 95 ASN 95 95 95 ASN ASN B . n B 2 96 ALA 96 96 96 ALA ALA B . n B 2 97 GLU 97 97 97 GLU GLU B . n B 2 98 LEU 98 98 98 LEU LEU B . n B 2 99 LEU 99 99 99 LEU LEU B . n B 2 100 VAL 100 100 100 VAL VAL B . n B 2 101 LEU 101 101 101 LEU LEU B . n B 2 102 MET 102 102 102 MET MET B . n B 2 103 GLU 103 103 103 GLU GLU B . n B 2 104 ASN 104 104 104 ASN ASN B . n B 2 105 GLU 105 105 105 GLU GLU B . n B 2 106 ARG 106 106 106 ARG ARG B . n B 2 107 THR 107 107 107 THR THR B . n B 2 108 LEU 108 108 108 LEU LEU B . n B 2 109 ASP 109 109 109 ASP ASP B . n B 2 110 PHE 110 110 110 PHE PHE B . n B 2 111 HIS 111 111 111 HIS HIS B . n B 2 112 ASP 112 112 112 ASP ASP B . n B 2 113 SER 113 113 113 SER SER B . n B 2 114 ASN 114 114 114 ASN ASN B . n B 2 115 VAL 115 115 115 VAL VAL B . n B 2 116 LYS 116 116 116 LYS LYS B . n B 2 117 ASN 117 117 117 ASN ASN B . n B 2 118 LEU 118 118 118 LEU LEU B . n B 2 119 TYR 119 119 119 TYR TYR B . n B 2 120 ASP 120 120 120 ASP ASP B . n B 2 121 LYS 121 121 121 LYS LYS B . n B 2 122 VAL 122 122 122 VAL VAL B . n B 2 123 ARG 123 123 123 ARG ARG B . n B 2 124 LEU 124 124 124 LEU LEU B . n B 2 125 GLN 125 125 125 GLN GLN B . n B 2 126 LEU 126 126 126 LEU LEU B . n B 2 127 ARG 127 127 127 ARG ARG B . n B 2 128 ASP 128 128 128 ASP ASP B . n B 2 129 ASN 129 129 129 ASN ASN B . n B 2 130 ALA 130 130 130 ALA ALA B . n B 2 131 LYS 131 131 131 LYS LYS B . n B 2 132 GLU 132 132 132 GLU GLU B . n B 2 133 LEU 133 133 133 LEU LEU B . n B 2 134 GLY 134 134 134 GLY GLY B . n B 2 135 ASN 135 135 135 ASN ASN B . n B 2 136 GLY 136 136 136 GLY GLY B . n B 2 137 CYS 137 137 137 CYS CYS B . n B 2 138 PHE 138 138 138 PHE PHE B . n B 2 139 GLU 139 139 139 GLU GLU B . n B 2 140 PHE 140 140 140 PHE PHE B . n B 2 141 TYR 141 141 141 TYR TYR B . n B 2 142 HIS 142 142 142 HIS HIS B . n B 2 143 LYS 143 143 143 LYS LYS B . n B 2 144 CYS 144 144 144 CYS CYS B . n B 2 145 ASP 145 145 145 ASP ASP B . n B 2 146 ASN 146 146 146 ASN ASN B . n B 2 147 GLU 147 147 147 GLU GLU B . n B 2 148 CYS 148 148 148 CYS CYS B . n B 2 149 MET 149 149 149 MET MET B . n B 2 150 GLU 150 150 150 GLU GLU B . n B 2 151 SER 151 151 151 SER SER B . n B 2 152 VAL 152 152 152 VAL VAL B . n B 2 153 ARG 153 153 153 ARG ARG B . n B 2 154 ASN 154 154 154 ASN ASN B . n B 2 155 GLY 155 155 155 GLY GLY B . n B 2 156 THR 156 156 156 THR THR B . n B 2 157 TYR 157 157 157 TYR TYR B . n B 2 158 ASP 158 158 158 ASP ASP B . n B 2 159 TYR 159 159 159 TYR TYR B . n B 2 160 PRO 160 160 160 PRO PRO B . n B 2 161 GLN 161 161 161 GLN GLN B . n B 2 162 TYR 162 162 162 TYR TYR B . n B 2 163 SER 163 163 ? ? ? B . n B 2 164 GLU 164 164 ? ? ? B . n B 2 165 GLU 165 165 ? ? ? B . n B 2 166 ALA 166 166 ? ? ? B . 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 C 3 NAG 1 1011 1011 NAG NAG A . D 3 NAG 1 1023 1023 NAG NAG A . E 3 NAG 2 1024 1024 NAG NAG A . F 3 NAG 1 1165 1165 NAG NAG A . G 3 NAG 2 1166 1166 NAG NAG A . H 4 MAN 3 1167 1167 MAN MAN A . I 5 BMA 4 1168 1168 BMA BMA A . J 4 MAN 5 1169 1169 MAN MAN A . K 3 NAG 1 1286 1286 NAG NAG A . L 6 SIA 1 1322 1322 SIA SIA A . M 7 GAL 2 1323 1323 GAL GAL A . N 3 NAG 1 1154 1154 NAG NAG B . O 3 NAG 2 1155 1155 NAG NAG B . P 5 BMA 3 1156 1156 BMA BMA B . Q 8 MPO 1 1163 1163 MPO MPO B . R 9 HOH 1 2001 2001 HOH HOH A . R 9 HOH 2 2002 2002 HOH HOH A . R 9 HOH 3 2003 2003 HOH HOH A . R 9 HOH 4 2004 2004 HOH HOH A . R 9 HOH 5 2005 2005 HOH HOH A . R 9 HOH 6 2006 2006 HOH HOH A . R 9 HOH 7 2007 2007 HOH HOH A . R 9 HOH 8 2008 2008 HOH HOH A . R 9 HOH 9 2009 2009 HOH HOH A . R 9 HOH 10 2010 2010 HOH HOH A . R 9 HOH 11 2011 2011 HOH HOH A . R 9 HOH 12 2012 2012 HOH HOH A . R 9 HOH 13 2013 2013 HOH HOH A . R 9 HOH 14 2014 2014 HOH HOH A . R 9 HOH 15 2015 2015 HOH HOH A . R 9 HOH 16 2016 2016 HOH HOH A . R 9 HOH 17 2017 2017 HOH HOH A . R 9 HOH 18 2018 2018 HOH HOH A . R 9 HOH 19 2019 2019 HOH HOH A . R 9 HOH 20 2020 2020 HOH HOH A . R 9 HOH 21 2021 2021 HOH HOH A . R 9 HOH 22 2022 2022 HOH HOH A . R 9 HOH 23 2023 2023 HOH HOH A . R 9 HOH 24 2024 2024 HOH HOH A . R 9 HOH 25 2025 2025 HOH HOH A . R 9 HOH 26 2026 2026 HOH HOH A . R 9 HOH 27 2027 2027 HOH HOH A . R 9 HOH 28 2028 2028 HOH HOH A . R 9 HOH 29 2029 2029 HOH HOH A . R 9 HOH 30 2030 2030 HOH HOH A . R 9 HOH 31 2031 2031 HOH HOH A . R 9 HOH 32 2032 2032 HOH HOH A . R 9 HOH 33 2033 2033 HOH HOH A . R 9 HOH 34 2034 2034 HOH HOH A . R 9 HOH 35 2035 2035 HOH HOH A . R 9 HOH 36 2036 2036 HOH HOH A . R 9 HOH 37 2037 2037 HOH HOH A . R 9 HOH 38 2038 2038 HOH HOH A . R 9 HOH 39 2039 2039 HOH HOH A . R 9 HOH 40 2040 2040 HOH HOH A . R 9 HOH 41 2041 2041 HOH HOH A . R 9 HOH 42 2042 2042 HOH HOH A . R 9 HOH 43 2043 2043 HOH HOH A . R 9 HOH 44 2044 2044 HOH HOH A . R 9 HOH 45 2045 2045 HOH HOH A . R 9 HOH 46 2046 2046 HOH HOH A . R 9 HOH 47 2047 2047 HOH HOH A . R 9 HOH 48 2048 2048 HOH HOH A . R 9 HOH 49 2049 2049 HOH HOH A . R 9 HOH 50 2050 2050 HOH HOH A . R 9 HOH 51 2051 2051 HOH HOH A . R 9 HOH 52 2052 2052 HOH HOH A . R 9 HOH 53 2053 2053 HOH HOH A . R 9 HOH 54 2054 2054 HOH HOH A . S 9 HOH 1 2001 2001 HOH HOH B . S 9 HOH 2 2002 2002 HOH HOH B . S 9 HOH 3 2003 2003 HOH HOH B . S 9 HOH 4 2004 2004 HOH HOH B . S 9 HOH 5 2005 2005 HOH HOH B . S 9 HOH 6 2006 2006 HOH HOH B . S 9 HOH 7 2007 2007 HOH HOH B . S 9 HOH 8 2008 2008 HOH HOH B . S 9 HOH 9 2009 2009 HOH HOH B . S 9 HOH 10 2010 2010 HOH HOH B . S 9 HOH 11 2011 2011 HOH HOH B . S 9 HOH 12 2012 2012 HOH HOH B . S 9 HOH 13 2013 2013 HOH HOH B . S 9 HOH 14 2014 2014 HOH HOH B . S 9 HOH 15 2015 2015 HOH HOH B . S 9 HOH 16 2016 2016 HOH HOH B . S 9 HOH 17 2017 2017 HOH HOH B . S 9 HOH 18 2018 2018 HOH HOH B . S 9 HOH 19 2019 2019 HOH HOH B . S 9 HOH 20 2020 2020 HOH HOH B . S 9 HOH 21 2021 2021 HOH HOH B . S 9 HOH 22 2022 2022 HOH HOH B . S 9 HOH 23 2023 2023 HOH HOH B . S 9 HOH 24 2024 2024 HOH HOH B . S 9 HOH 25 2025 2025 HOH HOH B . S 9 HOH 26 2026 2026 HOH HOH B . S 9 HOH 27 2027 2027 HOH HOH B . S 9 HOH 28 2028 2028 HOH HOH B . S 9 HOH 29 2029 2029 HOH HOH B . S 9 HOH 30 2030 2030 HOH HOH B . S 9 HOH 31 2031 2031 HOH HOH B . S 9 HOH 32 2032 2032 HOH HOH B . S 9 HOH 33 2033 2033 HOH HOH B . S 9 HOH 34 2034 2034 HOH HOH B . S 9 HOH 35 2035 2035 HOH HOH B . S 9 HOH 36 2036 2036 HOH HOH B . S 9 HOH 37 2037 2037 HOH HOH B . S 9 HOH 38 2038 2038 HOH HOH B . S 9 HOH 39 2039 2039 HOH HOH B . S 9 HOH 40 2040 2040 HOH HOH B . S 9 HOH 41 2041 2041 HOH HOH B . S 9 HOH 42 2042 2042 HOH HOH B . S 9 HOH 43 2043 2043 HOH HOH B . S 9 HOH 44 2044 2044 HOH HOH B . S 9 HOH 45 2045 2045 HOH HOH B . S 9 HOH 46 2046 2046 HOH HOH B . S 9 HOH 47 2047 2047 HOH HOH B . S 9 HOH 48 2048 2048 HOH HOH B . # 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 11 A ASN 11 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 23 A ASN 23 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 165 A ASN 165 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 286 A ASN 286 ? ASN 'GLYCOSYLATION SITE' 5 B ASN 154 B ASN 154 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details hexameric _pdbx_struct_assembly.oligomeric_count 6 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2,3 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 37600 ? 1 MORE -31.9 ? 1 'SSA (A^2)' 64560 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 2_545 -y,x-y-1,z -0.5000000000 -0.8660254038 0.0000000000 50.7320000000 0.8660254038 -0.5000000000 0.0000000000 -87.8704015696 0.0000000000 0.0000000000 1.0000000000 0.0000000000 3 'crystal symmetry operation' 3_655 -x+y+1,-x,z -0.5000000000 0.8660254038 0.0000000000 101.4640000000 -0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2014-05-28 2 'Structure model' 1 1 2014-06-11 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 34.4139 -14.0423 -18.7729 0.1030 0.3897 0.2550 0.0894 0.0302 -0.1332 0.5091 0.3701 4.6895 0.0238 -0.4965 0.5301 0.0633 -0.2039 0.1201 0.0465 -0.1948 0.1608 -0.5051 -0.9128 0.1315 'X-RAY DIFFRACTION' 2 ? refined 32.2904 -21.5243 16.5748 0.5023 0.8468 0.1443 -0.0623 0.1369 -0.1388 1.9272 2.5838 2.3602 0.2750 0.1352 -0.8371 -0.0282 -0.3572 0.0737 0.8924 -0.1657 0.0210 0.0755 -0.6249 0.1939 'X-RAY DIFFRACTION' 3 ? refined 35.6299 -14.7231 -26.9588 0.2032 0.2620 0.3032 0.0760 0.0309 -0.1074 0.9528 0.3141 10.1527 -0.1795 -1.1504 1.7389 0.1028 -0.2562 0.2414 0.0257 -0.1072 0.0650 0.2109 -0.5231 0.0044 'X-RAY DIFFRACTION' 4 ? refined 36.2477 -21.0340 -58.7921 0.1405 0.2482 0.4145 0.0796 -0.0228 -0.0490 1.6712 1.5517 8.0571 -1.3044 1.7842 -1.0768 -0.0949 0.1453 0.0007 0.2210 -0.1022 0.1184 -0.3553 -1.0107 0.1971 'X-RAY DIFFRACTION' 5 ? refined 48.2407 -22.7370 -10.3347 0.0816 0.0761 0.0786 -0.0013 0.0072 -0.0458 8.5513 3.6717 15.2761 1.5702 5.6208 1.2384 -0.0126 -0.1023 -0.0131 0.3281 -0.3363 0.3570 -0.2061 -0.5064 0.3489 'X-RAY DIFFRACTION' 6 ? refined 44.6221 -23.9640 -56.8070 0.0764 0.1154 0.2823 0.0330 -0.0147 -0.0043 1.6975 0.7441 13.3725 -0.5423 2.2886 -0.6837 0.0468 0.1601 0.0527 0.0101 -0.2588 0.0183 0.4959 0.2272 0.2120 'X-RAY DIFFRACTION' 7 ? refined 31.6443 -26.0846 -80.8223 0.5362 0.8078 0.6908 0.0750 -0.2321 -0.3338 7.1268 9.8625 6.4223 -4.4301 -0.8195 0.0706 0.8217 1.6606 -1.4072 -0.8718 -0.7622 1.2882 0.8736 -1.0979 -0.0595 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 A 1 ? ? A 105 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 106 ? ? A 262 ? ? ? ? 'X-RAY DIFFRACTION' 3 3 A 263 ? ? A 321 ? ? ? ? 'X-RAY DIFFRACTION' 4 4 B 1 ? ? B 60 ? ? ? ? 'X-RAY DIFFRACTION' 5 5 B 61 ? ? B 84 ? ? ? ? 'X-RAY DIFFRACTION' 6 6 B 85 ? ? B 141 ? ? ? ? 'X-RAY DIFFRACTION' 7 7 B 142 ? ? B 163 ? ? ? ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.8.0046 ? 1 xia2 'data reduction' . ? 2 SCALA 'data scaling' . ? 3 PHASER phasing . ? 4 # _pdbx_entry_details.entry_id 4CQU _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details 'MULTIBASIC SITE REMOVED' # 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 ARG A 53 ? ? 58.99 -121.30 2 1 ASP A 88 ? ? -103.65 -121.27 3 1 CYS A 135 ? ? -119.31 74.51 4 1 SER A 142 ? ? -134.29 -159.66 5 1 GLN A 192 ? ? 68.45 -64.09 6 1 ASN A 273 ? ? 55.55 70.31 7 1 ARG B 127 ? ? 54.35 -117.08 # _pdbx_validate_chiral.id 1 _pdbx_validate_chiral.PDB_model_num 1 _pdbx_validate_chiral.auth_atom_id C1 _pdbx_validate_chiral.label_alt_id ? _pdbx_validate_chiral.auth_asym_id B _pdbx_validate_chiral.auth_comp_id NAG _pdbx_validate_chiral.auth_seq_id 1154 _pdbx_validate_chiral.PDB_ins_code ? _pdbx_validate_chiral.details 'WRONG HAND' _pdbx_validate_chiral.omega . # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A GLN 322 ? A GLN 322 2 1 Y 1 A ARG 323 ? A ARG 323 3 1 Y 1 A GLU 324 ? A GLU 324 4 1 Y 1 A THR 325 ? A THR 325 5 1 Y 1 A ARG 326 ? A ARG 326 6 1 Y 1 B SER 163 ? B SER 163 7 1 Y 1 B GLU 164 ? B GLU 164 8 1 Y 1 B GLU 165 ? B GLU 165 9 1 Y 1 B ALA 166 ? B ALA 166 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 N-ACETYL-D-GLUCOSAMINE NAG 4 ALPHA-D-MANNOSE MAN 5 BETA-D-MANNOSE BMA 6 'O-SIALIC ACID' SIA 7 BETA-D-GALACTOSE GAL 8 '3[N-MORPHOLINO]PROPANE SULFONIC ACID' MPO 9 water HOH #